data_3K4P
# 
_entry.id   3K4P 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3K4P         
RCSB  RCSB055542   
WWPDB D_1000055542 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1ihp 'Aspergillus niger phytase'                                                          unspecified 
PDB 2gfi 'Debaryomyces castellii CBS 2923 phytase'                                            unspecified 
PDB 1dkl 'Escherichia coli phytase'                                                           unspecified 
PDB 1dkq 'Escherichia coli phytase H17A mutant in complex with myo-inositol hexakisphosphate' unspecified 
PDB 1qfx 'Aspergillus niger pH 2.5 acid phosphatase'                                          unspecified 
PDB 3k4q 'Aspergillus niger Phytase in complex with myo-inositol hexakis sulfate'             unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3K4P 
_pdbx_database_status.recvd_initial_deposition_date   2009-10-06 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
_audit_author.name           'Oakley, A.J.' 
_audit_author.pdbx_ordinal   1 
# 
_citation.id                        primary 
_citation.title                     'The structure of Aspergillus niger phytase PhyA in complex with a phytate mimetic' 
_citation.journal_abbrev            Biochem.Biophys.Res.Commun. 
_citation.journal_volume            397 
_citation.page_first                745 
_citation.page_last                 749 
_citation.year                      2010 
_citation.journal_id_ASTM           BBRCA9 
_citation.country                   US 
_citation.journal_id_ISSN           0006-291X 
_citation.journal_id_CSD            0146 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20541524 
_citation.pdbx_database_id_DOI      10.1016/j.bbrc.2010.06.024 
# 
_citation_author.citation_id   primary 
_citation_author.name          'Oakley, A.J.' 
_citation_author.ordinal       1 
# 
_cell.entry_id           3K4P 
_cell.length_a           71.066 
_cell.length_b           87.457 
_cell.length_c           82.185 
_cell.angle_alpha        90.00 
_cell.angle_beta         110.98 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3K4P 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
# 
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 '3-phytase A'          48888.996 2   3.1.3.8 ? ? ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   6   ?       ? ? ? 
3 water       nat water                  18.015    316 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'3 phytase A, Myo-inositol-hexaphosphate 3-phosphohydrolase A, Myo-inositol hexakisphosphate phosphohydrolase A' 
# 
_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       
;ASRNQSSCDTVDQGYQCFSETSHLWGQYAPFFSLANESVISPEVPAGCRVTFAQVLSRHGARYPTDSKGKKYSALIEEIQ
QNATTFDGKYAFLKTYNYSLGADDLTPFGEQELVNSGIKFYQRYESLTRNIVPFIRSSGSSRVIASGKKFIEGFQSTKLK
DPRAQPGQSSPKIDVVISEASSSNNTLDPGTCTVFEDSELADTVEANFTATFVPSIRQRLENDLSGVTLTDTEVTYLMDM
CSFDTISTSTVDTKLSPFCDLFTHDEWINYDYLQSLKKYYGHGAGNPLGPTQGVGYANELIARLTHSPVHDDTSSNHTLD
SSPATFPLNSTLYADFSHDNGIISILFALGLYNGTKPLSTTTVENITQTDGFSSAWTVPFASRLYVEMMQCQAEQEPLVR
VLVNDRVVPLHGCPVDALGRCTRDSFVRGLSFARSGGDWAECFA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ASRNQSSCDTVDQGYQCFSETSHLWGQYAPFFSLANESVISPEVPAGCRVTFAQVLSRHGARYPTDSKGKKYSALIEEIQ
QNATTFDGKYAFLKTYNYSLGADDLTPFGEQELVNSGIKFYQRYESLTRNIVPFIRSSGSSRVIASGKKFIEGFQSTKLK
DPRAQPGQSSPKIDVVISEASSSNNTLDPGTCTVFEDSELADTVEANFTATFVPSIRQRLENDLSGVTLTDTEVTYLMDM
CSFDTISTSTVDTKLSPFCDLFTHDEWINYDYLQSLKKYYGHGAGNPLGPTQGVGYANELIARLTHSPVHDDTSSNHTLD
SSPATFPLNSTLYADFSHDNGIISILFALGLYNGTKPLSTTTVENITQTDGFSSAWTVPFASRLYVEMMQCQAEQEPLVR
VLVNDRVVPLHGCPVDALGRCTRDSFVRGLSFARSGGDWAECFA
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   SER n 
1 3   ARG n 
1 4   ASN n 
1 5   GLN n 
1 6   SER n 
1 7   SER n 
1 8   CYS n 
1 9   ASP n 
1 10  THR n 
1 11  VAL n 
1 12  ASP n 
1 13  GLN n 
1 14  GLY n 
1 15  TYR n 
1 16  GLN n 
1 17  CYS n 
1 18  PHE n 
1 19  SER n 
1 20  GLU n 
1 21  THR n 
1 22  SER n 
1 23  HIS n 
1 24  LEU n 
1 25  TRP n 
1 26  GLY n 
1 27  GLN n 
1 28  TYR n 
1 29  ALA n 
1 30  PRO n 
1 31  PHE n 
1 32  PHE n 
1 33  SER n 
1 34  LEU n 
1 35  ALA n 
1 36  ASN n 
1 37  GLU n 
1 38  SER n 
1 39  VAL n 
1 40  ILE n 
1 41  SER n 
1 42  PRO n 
1 43  GLU n 
1 44  VAL n 
1 45  PRO n 
1 46  ALA n 
1 47  GLY n 
1 48  CYS n 
1 49  ARG n 
1 50  VAL n 
1 51  THR n 
1 52  PHE n 
1 53  ALA n 
1 54  GLN n 
1 55  VAL n 
1 56  LEU n 
1 57  SER n 
1 58  ARG n 
1 59  HIS n 
1 60  GLY n 
1 61  ALA n 
1 62  ARG n 
1 63  TYR n 
1 64  PRO n 
1 65  THR n 
1 66  ASP n 
1 67  SER n 
1 68  LYS n 
1 69  GLY n 
1 70  LYS n 
1 71  LYS n 
1 72  TYR n 
1 73  SER n 
1 74  ALA n 
1 75  LEU n 
1 76  ILE n 
1 77  GLU n 
1 78  GLU n 
1 79  ILE n 
1 80  GLN n 
1 81  GLN n 
1 82  ASN n 
1 83  ALA n 
1 84  THR n 
1 85  THR n 
1 86  PHE n 
1 87  ASP n 
1 88  GLY n 
1 89  LYS n 
1 90  TYR n 
1 91  ALA n 
1 92  PHE n 
1 93  LEU n 
1 94  LYS n 
1 95  THR n 
1 96  TYR n 
1 97  ASN n 
1 98  TYR n 
1 99  SER n 
1 100 LEU n 
1 101 GLY n 
1 102 ALA n 
1 103 ASP n 
1 104 ASP n 
1 105 LEU n 
1 106 THR n 
1 107 PRO n 
1 108 PHE n 
1 109 GLY n 
1 110 GLU n 
1 111 GLN n 
1 112 GLU n 
1 113 LEU n 
1 114 VAL n 
1 115 ASN n 
1 116 SER n 
1 117 GLY n 
1 118 ILE n 
1 119 LYS n 
1 120 PHE n 
1 121 TYR n 
1 122 GLN n 
1 123 ARG n 
1 124 TYR n 
1 125 GLU n 
1 126 SER n 
1 127 LEU n 
1 128 THR n 
1 129 ARG n 
1 130 ASN n 
1 131 ILE n 
1 132 VAL n 
1 133 PRO n 
1 134 PHE n 
1 135 ILE n 
1 136 ARG n 
1 137 SER n 
1 138 SER n 
1 139 GLY n 
1 140 SER n 
1 141 SER n 
1 142 ARG n 
1 143 VAL n 
1 144 ILE n 
1 145 ALA n 
1 146 SER n 
1 147 GLY n 
1 148 LYS n 
1 149 LYS n 
1 150 PHE n 
1 151 ILE n 
1 152 GLU n 
1 153 GLY n 
1 154 PHE n 
1 155 GLN n 
1 156 SER n 
1 157 THR n 
1 158 LYS n 
1 159 LEU n 
1 160 LYS n 
1 161 ASP n 
1 162 PRO n 
1 163 ARG n 
1 164 ALA n 
1 165 GLN n 
1 166 PRO n 
1 167 GLY n 
1 168 GLN n 
1 169 SER n 
1 170 SER n 
1 171 PRO n 
1 172 LYS n 
1 173 ILE n 
1 174 ASP n 
1 175 VAL n 
1 176 VAL n 
1 177 ILE n 
1 178 SER n 
1 179 GLU n 
1 180 ALA n 
1 181 SER n 
1 182 SER n 
1 183 SER n 
1 184 ASN n 
1 185 ASN n 
1 186 THR n 
1 187 LEU n 
1 188 ASP n 
1 189 PRO n 
1 190 GLY n 
1 191 THR n 
1 192 CYS n 
1 193 THR n 
1 194 VAL n 
1 195 PHE n 
1 196 GLU n 
1 197 ASP n 
1 198 SER n 
1 199 GLU n 
1 200 LEU n 
1 201 ALA n 
1 202 ASP n 
1 203 THR n 
1 204 VAL n 
1 205 GLU n 
1 206 ALA n 
1 207 ASN n 
1 208 PHE n 
1 209 THR n 
1 210 ALA n 
1 211 THR n 
1 212 PHE n 
1 213 VAL n 
1 214 PRO n 
1 215 SER n 
1 216 ILE n 
1 217 ARG n 
1 218 GLN n 
1 219 ARG n 
1 220 LEU n 
1 221 GLU n 
1 222 ASN n 
1 223 ASP n 
1 224 LEU n 
1 225 SER n 
1 226 GLY n 
1 227 VAL n 
1 228 THR n 
1 229 LEU n 
1 230 THR n 
1 231 ASP n 
1 232 THR n 
1 233 GLU n 
1 234 VAL n 
1 235 THR n 
1 236 TYR n 
1 237 LEU n 
1 238 MET n 
1 239 ASP n 
1 240 MET n 
1 241 CYS n 
1 242 SER n 
1 243 PHE n 
1 244 ASP n 
1 245 THR n 
1 246 ILE n 
1 247 SER n 
1 248 THR n 
1 249 SER n 
1 250 THR n 
1 251 VAL n 
1 252 ASP n 
1 253 THR n 
1 254 LYS n 
1 255 LEU n 
1 256 SER n 
1 257 PRO n 
1 258 PHE n 
1 259 CYS n 
1 260 ASP n 
1 261 LEU n 
1 262 PHE n 
1 263 THR n 
1 264 HIS n 
1 265 ASP n 
1 266 GLU n 
1 267 TRP n 
1 268 ILE n 
1 269 ASN n 
1 270 TYR n 
1 271 ASP n 
1 272 TYR n 
1 273 LEU n 
1 274 GLN n 
1 275 SER n 
1 276 LEU n 
1 277 LYS n 
1 278 LYS n 
1 279 TYR n 
1 280 TYR n 
1 281 GLY n 
1 282 HIS n 
1 283 GLY n 
1 284 ALA n 
1 285 GLY n 
1 286 ASN n 
1 287 PRO n 
1 288 LEU n 
1 289 GLY n 
1 290 PRO n 
1 291 THR n 
1 292 GLN n 
1 293 GLY n 
1 294 VAL n 
1 295 GLY n 
1 296 TYR n 
1 297 ALA n 
1 298 ASN n 
1 299 GLU n 
1 300 LEU n 
1 301 ILE n 
1 302 ALA n 
1 303 ARG n 
1 304 LEU n 
1 305 THR n 
1 306 HIS n 
1 307 SER n 
1 308 PRO n 
1 309 VAL n 
1 310 HIS n 
1 311 ASP n 
1 312 ASP n 
1 313 THR n 
1 314 SER n 
1 315 SER n 
1 316 ASN n 
1 317 HIS n 
1 318 THR n 
1 319 LEU n 
1 320 ASP n 
1 321 SER n 
1 322 SER n 
1 323 PRO n 
1 324 ALA n 
1 325 THR n 
1 326 PHE n 
1 327 PRO n 
1 328 LEU n 
1 329 ASN n 
1 330 SER n 
1 331 THR n 
1 332 LEU n 
1 333 TYR n 
1 334 ALA n 
1 335 ASP n 
1 336 PHE n 
1 337 SER n 
1 338 HIS n 
1 339 ASP n 
1 340 ASN n 
1 341 GLY n 
1 342 ILE n 
1 343 ILE n 
1 344 SER n 
1 345 ILE n 
1 346 LEU n 
1 347 PHE n 
1 348 ALA n 
1 349 LEU n 
1 350 GLY n 
1 351 LEU n 
1 352 TYR n 
1 353 ASN n 
1 354 GLY n 
1 355 THR n 
1 356 LYS n 
1 357 PRO n 
1 358 LEU n 
1 359 SER n 
1 360 THR n 
1 361 THR n 
1 362 THR n 
1 363 VAL n 
1 364 GLU n 
1 365 ASN n 
1 366 ILE n 
1 367 THR n 
1 368 GLN n 
1 369 THR n 
1 370 ASP n 
1 371 GLY n 
1 372 PHE n 
1 373 SER n 
1 374 SER n 
1 375 ALA n 
1 376 TRP n 
1 377 THR n 
1 378 VAL n 
1 379 PRO n 
1 380 PHE n 
1 381 ALA n 
1 382 SER n 
1 383 ARG n 
1 384 LEU n 
1 385 TYR n 
1 386 VAL n 
1 387 GLU n 
1 388 MET n 
1 389 MET n 
1 390 GLN n 
1 391 CYS n 
1 392 GLN n 
1 393 ALA n 
1 394 GLU n 
1 395 GLN n 
1 396 GLU n 
1 397 PRO n 
1 398 LEU n 
1 399 VAL n 
1 400 ARG n 
1 401 VAL n 
1 402 LEU n 
1 403 VAL n 
1 404 ASN n 
1 405 ASP n 
1 406 ARG n 
1 407 VAL n 
1 408 VAL n 
1 409 PRO n 
1 410 LEU n 
1 411 HIS n 
1 412 GLY n 
1 413 CYS n 
1 414 PRO n 
1 415 VAL n 
1 416 ASP n 
1 417 ALA n 
1 418 LEU n 
1 419 GLY n 
1 420 ARG n 
1 421 CYS n 
1 422 THR n 
1 423 ARG n 
1 424 ASP n 
1 425 SER n 
1 426 PHE n 
1 427 VAL n 
1 428 ARG n 
1 429 GLY n 
1 430 LEU n 
1 431 SER n 
1 432 PHE n 
1 433 ALA n 
1 434 ARG n 
1 435 SER n 
1 436 GLY n 
1 437 GLY n 
1 438 ASP n 
1 439 TRP n 
1 440 ALA n 
1 441 GLU n 
1 442 CYS n 
1 443 PHE n 
1 444 ALA 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 phyA 
_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      'Aspergillus niger' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5061 
_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      'Aspergillus niger' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     5061 
_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                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PHYA_ASPNG 
_struct_ref.pdbx_db_accession          P34752 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ASRNQSSCDTVDQGYQCFSETSHLWGQYAPFFSLANESVISPEVPAGCRVTFAQVLSRHGARYPTDSKGKKYSALIEEIQ
QNATTFDGKYAFLKTYNYSLGADDLTPFGEQELVNSGIKFYQRYESLTRNIVPFIRSSGSSRVIASGKKFIEGFQSTKLK
DPRAQPGQSSPKIDVVISEASSSNNTLDPGTCTVFEDSELADTVEANFTATFVPSIRQRLENDLSGVTLTDTEVTYLMDM
CSFDTISTSTVDTKLSPFCDLFTHDEWINYDYLQSLKKYYGHGAGNPLGPTQGVGYANELIARLTHSPVHDDTSSNHTLD
SSPATFPLNSTLYADFSHDNGIISILFALGLYNGTKPLSTTTVENITQTDGFSSAWTVPFASRLYVEMMQCQAEQEPLVR
VLVNDRVVPLHGCPVDALGRCTRDSFVRGLSFARSGGDWAECFA
;
_struct_ref.pdbx_align_begin           24 
_struct_ref.pdbx_db_isoform            ? 
# 
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 3K4P A 1 ? 444 ? P34752 24 ? 467 ? 1 444 
2 1 3K4P B 1 ? 444 ? P34752 24 ? 467 ? 1 444 
# 
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  
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 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
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 
# 
_exptl.entry_id          3K4P 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.44 
_exptl_crystal.density_percent_sol   49.57 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7 
_exptl_crystal_grow.pdbx_details    
'25% (w/v) PEG 3350, 0.4M ammonium nitrate, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315r' 
_diffrn_detector.pdbx_collection_date   2009-08-28 
_diffrn_detector.details                'BEAMLINE OPTICS' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'BEAMLINE OPTICS' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.953715 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.953715 
# 
_reflns.entry_id                     3K4P 
_reflns.observed_criterion_sigma_I   -3 
_reflns.observed_criterion_sigma_F   -3 
_reflns.d_resolution_low             76.74 
_reflns.d_resolution_high            2.4 
_reflns.number_obs                   35613 
_reflns.number_all                   35613 
_reflns.percent_possible_obs         96.6 
_reflns.pdbx_Rmerge_I_obs            0.138 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        6.6 
_reflns.B_iso_Wilson_estimate        35.4 
_reflns.pdbx_redundancy              3.5 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.4 
_reflns_shell.d_res_low              2.53 
_reflns_shell.percent_possible_all   99.8 
_reflns_shell.Rmerge_I_obs           0.542 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.4 
_reflns_shell.pdbx_redundancy        3.5 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      5338 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3K4P 
_refine.ls_number_reflns_obs                     33827 
_refine.ls_number_reflns_all                     33827 
_refine.pdbx_ls_sigma_I                          -1 
_refine.pdbx_ls_sigma_F                          -1 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             66.36 
_refine.ls_d_res_high                            2.40 
_refine.ls_percent_reflns_obs                    96.55 
_refine.ls_R_factor_obs                          0.21825 
_refine.ls_R_factor_all                          0.21825 
_refine.ls_R_factor_R_work                       0.21528 
_refine.ls_R_factor_R_free                       0.27548 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  1770 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.correlation_coeff_Fo_to_Fc               0.919 
_refine.correlation_coeff_Fo_to_Fc_free          0.873 
_refine.B_iso_mean                               26.967 
_refine.aniso_B[1][1]                            -0.30 
_refine.aniso_B[2][2]                            0.08 
_refine.aniso_B[3][3]                            -1.95 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -3.04 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      'PDB ENTRY 1IHP' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.635 
_refine.pdbx_overall_ESU_R_Free                  0.314 
_refine.overall_SU_ML                            0.229 
_refine.overall_SU_B                             9.744 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_max                                57.71 
_refine.B_iso_min                                2.05 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6777 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         84 
_refine_hist.number_atoms_solvent             316 
_refine_hist.number_atoms_total               7177 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        66.36 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.016  0.022  ? 7060 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.680  1.962  ? 9629 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.722  5.000  ? 880  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       38.047 24.224 ? 322  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       16.495 15.000 ? 1078 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       18.610 15.000 ? 37   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.111  0.200  ? 1085 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.021  ? 5455 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.727  1.500  ? 4373 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.330  2.000  ? 7086 'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.023  3.000  ? 2687 'X-RAY DIFFRACTION' ? 
r_scangle_it                 3.247  4.500  ? 2540 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
1 A 3363 0.04 0.05 'tight positional' 1 1 'X-RAY DIFFRACTION' ? ? ? 
1 A 3363 0.12 0.50 'tight thermal'    1 2 'X-RAY DIFFRACTION' ? ? ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.400 
_refine_ls_shell.d_res_low                        2.462 
_refine_ls_shell.number_reflns_R_work             2559 
_refine_ls_shell.R_factor_R_work                  0.249 
_refine_ls_shell.percent_reflns_obs               99.70 
_refine_ls_shell.R_factor_R_free                  0.353 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             124 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                2559 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1 A 1 
2 B 1 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.selection_details 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
1 1 1 1 A 7 A 444 ? . . . . . . . . 
1 2 1 1 B 7 B 444 ? . . . . . . . . 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                  3K4P 
_struct.title                     'Aspergillus niger Phytase' 
_struct.pdbx_descriptor           '3-phytase A (E.C.3.1.3.8)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            N 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3K4P 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Phytase, PhyA, 3-Phosphotase, myo-inositol hexakis phosphate phosphohydrolase, 37288-11-2, Disulfide bond, Glycoprotein, Hydrolase, Secreted
;
# 
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 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 3 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  1  PHE A 18  ? HIS A 23  ? PHE A 18  HIS A 23  1 ? 6  
HELX_P HELX_P2  2  LEU A 24  ? ALA A 29  ? LEU A 24  ALA A 29  5 ? 6  
HELX_P HELX_P3  3  LEU A 34  ? SER A 38  ? LEU A 34  SER A 38  5 ? 5  
HELX_P HELX_P4  4  THR A 65  ? ALA A 83  ? THR A 65  ALA A 83  1 ? 19 
HELX_P HELX_P5  5  ASP A 87  ? LYS A 94  ? ASP A 87  LYS A 94  5 ? 8  
HELX_P HELX_P6  6  THR A 106 ? TYR A 124 ? THR A 106 TYR A 124 1 ? 19 
HELX_P HELX_P7  7  TYR A 124 ? ARG A 129 ? TYR A 124 ARG A 129 1 ? 6  
HELX_P HELX_P8  8  SER A 140 ? LYS A 160 ? SER A 140 LYS A 160 1 ? 21 
HELX_P HELX_P9  9  CYS A 192 ? SER A 198 ? CYS A 192 SER A 198 1 ? 7  
HELX_P HELX_P10 10 GLU A 199 ? ALA A 210 ? GLU A 199 ALA A 210 1 ? 12 
HELX_P HELX_P11 11 VAL A 213 ? LEU A 224 ? VAL A 213 LEU A 224 1 ? 12 
HELX_P HELX_P12 12 THR A 230 ? SER A 247 ? THR A 230 SER A 247 1 ? 18 
HELX_P HELX_P13 13 THR A 248 ? THR A 253 ? THR A 248 THR A 253 5 ? 6  
HELX_P HELX_P14 14 SER A 256 ? PHE A 262 ? SER A 256 PHE A 262 5 ? 7  
HELX_P HELX_P15 15 THR A 263 ? HIS A 282 ? THR A 263 HIS A 282 1 ? 20 
HELX_P HELX_P16 16 GLY A 289 ? GLN A 292 ? GLY A 289 GLN A 292 5 ? 4  
HELX_P HELX_P17 17 GLY A 293 ? HIS A 306 ? GLY A 293 HIS A 306 1 ? 14 
HELX_P HELX_P18 18 ASN A 316 ? SER A 321 ? ASN A 316 SER A 321 1 ? 6  
HELX_P HELX_P19 19 HIS A 338 ? LEU A 349 ? HIS A 338 LEU A 349 1 ? 12 
HELX_P HELX_P20 20 SER A 373 ? VAL A 378 ? SER A 373 VAL A 378 1 ? 6  
HELX_P HELX_P21 21 ARG A 423 ? LEU A 430 ? ARG A 423 LEU A 430 1 ? 8  
HELX_P HELX_P22 22 LEU A 430 ? SER A 435 ? LEU A 430 SER A 435 1 ? 6  
HELX_P HELX_P23 23 ASP A 438 ? PHE A 443 ? ASP A 438 PHE A 443 5 ? 6  
HELX_P HELX_P24 24 PHE B 18  ? HIS B 23  ? PHE B 18  HIS B 23  1 ? 6  
HELX_P HELX_P25 25 LEU B 24  ? ALA B 29  ? LEU B 24  ALA B 29  5 ? 6  
HELX_P HELX_P26 26 LEU B 34  ? SER B 38  ? LEU B 34  SER B 38  5 ? 5  
HELX_P HELX_P27 27 THR B 65  ? ALA B 83  ? THR B 65  ALA B 83  1 ? 19 
HELX_P HELX_P28 28 ASP B 87  ? LYS B 94  ? ASP B 87  LYS B 94  5 ? 8  
HELX_P HELX_P29 29 THR B 106 ? TYR B 124 ? THR B 106 TYR B 124 1 ? 19 
HELX_P HELX_P30 30 TYR B 124 ? ARG B 129 ? TYR B 124 ARG B 129 1 ? 6  
HELX_P HELX_P31 31 SER B 140 ? LYS B 160 ? SER B 140 LYS B 160 1 ? 21 
HELX_P HELX_P32 32 CYS B 192 ? SER B 198 ? CYS B 192 SER B 198 1 ? 7  
HELX_P HELX_P33 33 GLU B 199 ? ALA B 210 ? GLU B 199 ALA B 210 1 ? 12 
HELX_P HELX_P34 34 VAL B 213 ? LEU B 224 ? VAL B 213 LEU B 224 1 ? 12 
HELX_P HELX_P35 35 THR B 230 ? SER B 247 ? THR B 230 SER B 247 1 ? 18 
HELX_P HELX_P36 36 THR B 248 ? THR B 253 ? THR B 248 THR B 253 5 ? 6  
HELX_P HELX_P37 37 SER B 256 ? PHE B 262 ? SER B 256 PHE B 262 5 ? 7  
HELX_P HELX_P38 38 THR B 263 ? HIS B 282 ? THR B 263 HIS B 282 1 ? 20 
HELX_P HELX_P39 39 LEU B 288 ? GLY B 293 ? LEU B 288 GLY B 293 1 ? 6  
HELX_P HELX_P40 40 GLY B 293 ? HIS B 306 ? GLY B 293 HIS B 306 1 ? 14 
HELX_P HELX_P41 41 ASN B 316 ? SER B 321 ? ASN B 316 SER B 321 1 ? 6  
HELX_P HELX_P42 42 HIS B 338 ? LEU B 349 ? HIS B 338 LEU B 349 1 ? 12 
HELX_P HELX_P43 43 SER B 373 ? VAL B 378 ? SER B 373 VAL B 378 1 ? 6  
HELX_P HELX_P44 44 ARG B 423 ? LEU B 430 ? ARG B 423 LEU B 430 1 ? 8  
HELX_P HELX_P45 45 LEU B 430 ? SER B 435 ? LEU B 430 SER B 435 1 ? 6  
HELX_P HELX_P46 46 ASP B 438 ? PHE B 443 ? ASP B 438 PHE B 443 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 8   SG  ? ? ? 1_555 A CYS 17  SG ? ? A CYS 8   A CYS 17   1_555 ? ? ? ? ? ? ? 2.017 ? 
disulf2  disulf ? ? A CYS 48  SG  ? ? ? 1_555 A CYS 391 SG ? ? A CYS 48  A CYS 391  1_555 ? ? ? ? ? ? ? 2.010 ? 
disulf3  disulf ? ? A CYS 192 SG  ? ? ? 1_555 A CYS 442 SG ? ? A CYS 192 A CYS 442  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf4  disulf ? ? A CYS 241 SG  ? ? ? 1_555 A CYS 259 SG ? ? A CYS 241 A CYS 259  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf5  disulf ? ? A CYS 413 SG  ? ? ? 1_555 A CYS 421 SG ? ? A CYS 413 A CYS 421  1_555 ? ? ? ? ? ? ? 2.053 ? 
disulf6  disulf ? ? B CYS 8   SG  ? ? ? 1_555 B CYS 17  SG ? ? B CYS 8   B CYS 17   1_555 ? ? ? ? ? ? ? 2.066 ? 
disulf7  disulf ? ? B CYS 48  SG  ? ? ? 1_555 B CYS 391 SG ? ? B CYS 48  B CYS 391  1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf8  disulf ? ? B CYS 192 SG  ? ? ? 1_555 B CYS 442 SG ? ? B CYS 192 B CYS 442  1_555 ? ? ? ? ? ? ? 2.007 ? 
disulf9  disulf ? ? B CYS 241 SG  ? ? ? 1_555 B CYS 259 SG ? ? B CYS 241 B CYS 259  1_555 ? ? ? ? ? ? ? 2.051 ? 
disulf10 disulf ? ? B CYS 413 SG  ? ? ? 1_555 B CYS 421 SG ? ? B CYS 413 B CYS 421  1_555 ? ? ? ? ? ? ? 2.040 ? 
covale1  covale ? ? A ASN 82  ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 82  A NAG 1001 1_555 ? ? ? ? ? ? ? 1.452 ? 
covale2  covale ? ? A ASN 316 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 316 A NAG 1002 1_555 ? ? ? ? ? ? ? 1.433 ? 
covale3  covale ? ? A ASN 353 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 353 A NAG 1003 1_555 ? ? ? ? ? ? ? 1.399 ? 
covale4  covale ? ? B ASN 82  ND2 ? ? ? 1_555 F NAG .   C1 ? ? B ASN 82  B NAG 1001 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale5  covale ? ? B ASN 316 ND2 ? ? ? 1_555 G NAG .   C1 ? ? B ASN 316 B NAG 1002 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale6  covale ? ? B ASN 353 ND2 ? ? ? 1_555 H NAG .   C1 ? ? B ASN 353 B NAG 1003 1_555 ? ? ? ? ? ? ? 1.417 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2 ? 
B ? 7 ? 
C ? 7 ? 
D ? 2 ? 
E ? 7 ? 
F ? 7 ? 
# 
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 
A 1 2 ? anti-parallel 
B 1 2 ? parallel      
B 2 3 ? parallel      
B 3 4 ? parallel      
B 4 5 ? anti-parallel 
B 5 6 ? anti-parallel 
B 6 7 ? anti-parallel 
C 1 2 ? parallel      
C 2 3 ? parallel      
C 3 4 ? parallel      
C 4 5 ? anti-parallel 
C 5 6 ? anti-parallel 
C 6 7 ? anti-parallel 
D 1 2 ? anti-parallel 
E 1 2 ? parallel      
E 2 3 ? parallel      
E 3 4 ? parallel      
E 4 5 ? anti-parallel 
E 5 6 ? anti-parallel 
E 6 7 ? anti-parallel 
F 1 2 ? parallel      
F 2 3 ? parallel      
F 3 4 ? parallel      
F 4 5 ? anti-parallel 
F 5 6 ? anti-parallel 
F 6 7 ? 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 
A 1 ASP A 9   ? THR A 10  ? ASP A 9   THR A 10  
A 2 GLY A 14  ? TYR A 15  ? GLY A 14  TYR A 15  
B 1 VAL A 175 ? ILE A 177 ? VAL A 175 ILE A 177 
B 2 PHE A 134 ? SER A 138 ? PHE A 134 SER A 138 
B 3 LEU A 332 ? SER A 337 ? LEU A 332 SER A 337 
B 4 ARG A 49  ? ARG A 58  ? ARG A 49  ARG A 58  
B 5 ARG A 383 ? GLN A 390 ? ARG A 383 GLN A 390 
B 6 LEU A 398 ? VAL A 403 ? LEU A 398 VAL A 403 
B 7 ARG A 406 ? VAL A 407 ? ARG A 406 VAL A 407 
C 1 VAL A 175 ? ILE A 177 ? VAL A 175 ILE A 177 
C 2 PHE A 134 ? SER A 138 ? PHE A 134 SER A 138 
C 3 LEU A 332 ? SER A 337 ? LEU A 332 SER A 337 
C 4 ARG A 49  ? ARG A 58  ? ARG A 49  ARG A 58  
C 5 ARG A 383 ? GLN A 390 ? ARG A 383 GLN A 390 
C 6 LEU A 398 ? VAL A 403 ? LEU A 398 VAL A 403 
C 7 CYS A 421 ? THR A 422 ? CYS A 421 THR A 422 
D 1 ASP B 9   ? THR B 10  ? ASP B 9   THR B 10  
D 2 GLY B 14  ? TYR B 15  ? GLY B 14  TYR B 15  
E 1 VAL B 175 ? ILE B 177 ? VAL B 175 ILE B 177 
E 2 PHE B 134 ? SER B 138 ? PHE B 134 SER B 138 
E 3 LEU B 332 ? SER B 337 ? LEU B 332 SER B 337 
E 4 ARG B 49  ? ARG B 58  ? ARG B 49  ARG B 58  
E 5 ARG B 383 ? GLN B 390 ? ARG B 383 GLN B 390 
E 6 LEU B 398 ? VAL B 403 ? LEU B 398 VAL B 403 
E 7 ARG B 406 ? VAL B 407 ? ARG B 406 VAL B 407 
F 1 VAL B 175 ? ILE B 177 ? VAL B 175 ILE B 177 
F 2 PHE B 134 ? SER B 138 ? PHE B 134 SER B 138 
F 3 LEU B 332 ? SER B 337 ? LEU B 332 SER B 337 
F 4 ARG B 49  ? ARG B 58  ? ARG B 49  ARG B 58  
F 5 ARG B 383 ? GLN B 390 ? ARG B 383 GLN B 390 
F 6 LEU B 398 ? VAL B 403 ? LEU B 398 VAL B 403 
F 7 CYS B 421 ? THR B 422 ? CYS B 421 THR B 422 
# 
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 
A 1 2 N THR A 10  ? N THR A 10  O GLY A 14  ? O GLY A 14  
B 1 2 O ILE A 177 ? O ILE A 177 N SER A 137 ? N SER A 137 
B 2 3 N ARG A 136 ? N ARG A 136 O ALA A 334 ? O ALA A 334 
B 3 4 O ASP A 335 ? O ASP A 335 N SER A 57  ? N SER A 57  
B 4 5 N ARG A 49  ? N ARG A 49  O GLN A 390 ? O GLN A 390 
B 5 6 N GLU A 387 ? N GLU A 387 O ARG A 400 ? O ARG A 400 
B 6 7 N VAL A 403 ? N VAL A 403 O ARG A 406 ? O ARG A 406 
C 1 2 O ILE A 177 ? O ILE A 177 N SER A 137 ? N SER A 137 
C 2 3 N ARG A 136 ? N ARG A 136 O ALA A 334 ? O ALA A 334 
C 3 4 O ASP A 335 ? O ASP A 335 N SER A 57  ? N SER A 57  
C 4 5 N ARG A 49  ? N ARG A 49  O GLN A 390 ? O GLN A 390 
C 5 6 N GLU A 387 ? N GLU A 387 O ARG A 400 ? O ARG A 400 
C 6 7 N VAL A 399 ? N VAL A 399 O CYS A 421 ? O CYS A 421 
D 1 2 N THR B 10  ? N THR B 10  O GLY B 14  ? O GLY B 14  
E 1 2 O ILE B 177 ? O ILE B 177 N SER B 137 ? N SER B 137 
E 2 3 N ARG B 136 ? N ARG B 136 O ALA B 334 ? O ALA B 334 
E 3 4 O ASP B 335 ? O ASP B 335 N SER B 57  ? N SER B 57  
E 4 5 N ARG B 49  ? N ARG B 49  O GLN B 390 ? O GLN B 390 
E 5 6 N GLU B 387 ? N GLU B 387 O ARG B 400 ? O ARG B 400 
E 6 7 N VAL B 403 ? N VAL B 403 O ARG B 406 ? O ARG B 406 
F 1 2 O ILE B 177 ? O ILE B 177 N SER B 137 ? N SER B 137 
F 2 3 N ARG B 136 ? N ARG B 136 O ALA B 334 ? O ALA B 334 
F 3 4 O ASP B 335 ? O ASP B 335 N SER B 57  ? N SER B 57  
F 4 5 N ARG B 49  ? N ARG B 49  O GLN B 390 ? O GLN B 390 
F 5 6 N GLU B 387 ? N GLU B 387 O ARG B 400 ? O ARG B 400 
F 6 7 N VAL B 399 ? N VAL B 399 O CYS B 421 ? O CYS B 421 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG A 1001' 
AC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG A 1002' 
AC3 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG A 1003' 
AC4 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG B 1001' 
AC5 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG B 1002' 
AC6 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE NAG B 1003' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 5  GLU A 78  ? GLU A 78  . ? 1_555 ? 
2  AC1 5  ASN A 82  ? ASN A 82  . ? 1_555 ? 
3  AC1 5  VAL A 227 ? VAL A 227 . ? 1_555 ? 
4  AC1 5  THR A 228 ? THR A 228 . ? 1_555 ? 
5  AC1 5  HOH I .   ? HOH A 471 . ? 1_555 ? 
6  AC2 5  SER A 182 ? SER A 182 . ? 1_555 ? 
7  AC2 5  SER A 183 ? SER A 183 . ? 1_555 ? 
8  AC2 5  ASN A 184 ? ASN A 184 . ? 1_555 ? 
9  AC2 5  ASN A 316 ? ASN A 316 . ? 1_555 ? 
10 AC2 5  HOH I .   ? HOH A 466 . ? 1_555 ? 
11 AC3 10 ASN A 353 ? ASN A 353 . ? 1_555 ? 
12 AC3 10 GLY A 412 ? GLY A 412 . ? 1_555 ? 
13 AC3 10 GLY A 429 ? GLY A 429 . ? 1_555 ? 
14 AC3 10 PHE A 432 ? PHE A 432 . ? 1_555 ? 
15 AC3 10 HOH I .   ? HOH A 593 . ? 1_555 ? 
16 AC3 10 HOH I .   ? HOH A 598 . ? 1_555 ? 
17 AC3 10 ASN B 130 ? ASN B 130 . ? 1_556 ? 
18 AC3 10 ARG B 163 ? ARG B 163 . ? 1_556 ? 
19 AC3 10 ALA B 164 ? ALA B 164 . ? 1_556 ? 
20 AC3 10 GLN B 165 ? GLN B 165 . ? 1_556 ? 
21 AC4 5  GLU B 78  ? GLU B 78  . ? 1_555 ? 
22 AC4 5  ASN B 82  ? ASN B 82  . ? 1_555 ? 
23 AC4 5  VAL B 227 ? VAL B 227 . ? 1_555 ? 
24 AC4 5  THR B 228 ? THR B 228 . ? 1_555 ? 
25 AC4 5  HOH J .   ? HOH B 484 . ? 1_555 ? 
26 AC5 4  SER B 183 ? SER B 183 . ? 1_555 ? 
27 AC5 4  ASN B 184 ? ASN B 184 . ? 1_555 ? 
28 AC5 4  ASN B 316 ? ASN B 316 . ? 1_555 ? 
29 AC5 4  HOH J .   ? HOH B 471 . ? 1_555 ? 
30 AC6 11 ASN A 130 ? ASN A 130 . ? 1_655 ? 
31 AC6 11 ARG A 163 ? ARG A 163 . ? 1_655 ? 
32 AC6 11 ALA A 164 ? ALA A 164 . ? 1_655 ? 
33 AC6 11 GLN A 165 ? GLN A 165 . ? 1_655 ? 
34 AC6 11 ASN B 353 ? ASN B 353 . ? 1_555 ? 
35 AC6 11 HIS B 411 ? HIS B 411 . ? 1_555 ? 
36 AC6 11 GLY B 412 ? GLY B 412 . ? 1_555 ? 
37 AC6 11 GLY B 429 ? GLY B 429 . ? 1_555 ? 
38 AC6 11 PHE B 432 ? PHE B 432 . ? 1_555 ? 
39 AC6 11 HOH J .   ? HOH B 451 . ? 1_555 ? 
40 AC6 11 HOH J .   ? HOH B 549 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3K4P 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3K4P 
_atom_sites.fract_transf_matrix[1][1]   0.014071 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005396 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011434 
_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]   0.013032 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
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   . SER A 1 7   ? 2.533   0.280   9.265   1.00 43.08 ? 7    SER A N   1 
ATOM   2    C CA  . SER A 1 7   ? 2.501   -1.178  8.864   1.00 43.27 ? 7    SER A CA  1 
ATOM   3    C C   . SER A 1 7   ? 2.993   -2.154  9.957   1.00 42.87 ? 7    SER A C   1 
ATOM   4    O O   . SER A 1 7   ? 2.853   -3.371  9.806   1.00 43.30 ? 7    SER A O   1 
ATOM   5    C CB  . SER A 1 7   ? 3.259   -1.410  7.557   1.00 43.80 ? 7    SER A CB  1 
ATOM   6    O OG  . SER A 1 7   ? 2.730   -0.600  6.504   1.00 45.66 ? 7    SER A OG  1 
ATOM   7    N N   . CYS A 1 8   ? 3.595   -1.616  11.025  1.00 41.72 ? 8    CYS A N   1 
ATOM   8    C CA  . CYS A 1 8   ? 3.784   -2.334  12.306  1.00 40.51 ? 8    CYS A CA  1 
ATOM   9    C C   . CYS A 1 8   ? 2.697   -1.810  13.257  1.00 39.30 ? 8    CYS A C   1 
ATOM   10   O O   . CYS A 1 8   ? 2.558   -2.271  14.386  1.00 39.20 ? 8    CYS A O   1 
ATOM   11   C CB  . CYS A 1 8   ? 5.208   -2.139  12.903  1.00 39.99 ? 8    CYS A CB  1 
ATOM   12   S SG  . CYS A 1 8   ? 5.916   -0.402  12.896  1.00 40.75 ? 8    CYS A SG  1 
ATOM   13   N N   . ASP A 1 9   ? 1.947   -0.830  12.772  1.00 37.46 ? 9    ASP A N   1 
ATOM   14   C CA  . ASP A 1 9   ? 0.786   -0.308  13.447  1.00 36.75 ? 9    ASP A CA  1 
ATOM   15   C C   . ASP A 1 9   ? -0.466  -0.597  12.591  1.00 36.23 ? 9    ASP A C   1 
ATOM   16   O O   . ASP A 1 9   ? -0.729  0.121   11.612  1.00 36.98 ? 9    ASP A O   1 
ATOM   17   C CB  . ASP A 1 9   ? 0.955   1.201   13.623  1.00 36.78 ? 9    ASP A CB  1 
ATOM   18   C CG  . ASP A 1 9   ? -0.105  1.824   14.525  1.00 36.67 ? 9    ASP A CG  1 
ATOM   19   O OD1 . ASP A 1 9   ? -0.697  1.113   15.376  1.00 37.88 ? 9    ASP A OD1 1 
ATOM   20   O OD2 . ASP A 1 9   ? -0.315  3.044   14.404  1.00 37.08 ? 9    ASP A OD2 1 
ATOM   21   N N   . THR A 1 10  ? -1.224  -1.625  12.958  1.00 34.11 ? 10   THR A N   1 
ATOM   22   C CA  . THR A 1 10  ? -2.386  -2.037  12.194  1.00 33.14 ? 10   THR A CA  1 
ATOM   23   C C   . THR A 1 10  ? -3.684  -1.905  12.993  1.00 32.78 ? 10   THR A C   1 
ATOM   24   O O   . THR A 1 10  ? -3.677  -1.714  14.214  1.00 32.18 ? 10   THR A O   1 
ATOM   25   C CB  . THR A 1 10  ? -2.275  -3.504  11.790  1.00 32.96 ? 10   THR A CB  1 
ATOM   26   O OG1 . THR A 1 10  ? -2.052  -4.292  12.959  1.00 32.96 ? 10   THR A OG1 1 
ATOM   27   C CG2 . THR A 1 10  ? -1.132  -3.731  10.813  1.00 32.50 ? 10   THR A CG2 1 
ATOM   28   N N   . VAL A 1 11  ? -4.808  -2.058  12.312  1.00 32.29 ? 11   VAL A N   1 
ATOM   29   C CA  . VAL A 1 11  ? -6.090  -2.053  13.017  1.00 32.20 ? 11   VAL A CA  1 
ATOM   30   C C   . VAL A 1 11  ? -6.190  -3.278  13.897  1.00 31.90 ? 11   VAL A C   1 
ATOM   31   O O   . VAL A 1 11  ? -6.651  -3.194  15.033  1.00 31.45 ? 11   VAL A O   1 
ATOM   32   C CB  . VAL A 1 11  ? -7.290  -1.984  12.053  1.00 32.30 ? 11   VAL A CB  1 
ATOM   33   C CG1 . VAL A 1 11  ? -8.619  -2.318  12.774  1.00 31.49 ? 11   VAL A CG1 1 
ATOM   34   C CG2 . VAL A 1 11  ? -7.338  -0.596  11.374  1.00 32.42 ? 11   VAL A CG2 1 
ATOM   35   N N   . ASP A 1 12  ? -5.728  -4.414  13.388  1.00 32.10 ? 12   ASP A N   1 
ATOM   36   C CA  . ASP A 1 12  ? -5.986  -5.655  14.091  1.00 32.13 ? 12   ASP A CA  1 
ATOM   37   C C   . ASP A 1 12  ? -5.048  -5.929  15.256  1.00 31.26 ? 12   ASP A C   1 
ATOM   38   O O   . ASP A 1 12  ? -5.483  -6.420  16.310  1.00 30.76 ? 12   ASP A O   1 
ATOM   39   C CB  . ASP A 1 12  ? -5.965  -6.830  13.132  1.00 32.94 ? 12   ASP A CB  1 
ATOM   40   C CG  . ASP A 1 12  ? -7.203  -7.699  13.278  1.00 36.48 ? 12   ASP A CG  1 
ATOM   41   O OD1 . ASP A 1 12  ? -7.210  -8.615  14.180  1.00 32.56 ? 12   ASP A OD1 1 
ATOM   42   O OD2 . ASP A 1 12  ? -8.157  -7.427  12.468  1.00 39.91 ? 12   ASP A OD2 1 
ATOM   43   N N   . GLN A 1 13  ? -3.774  -5.610  15.066  1.00 30.09 ? 13   GLN A N   1 
ATOM   44   C CA  . GLN A 1 13  ? -2.752  -6.017  16.018  1.00 29.65 ? 13   GLN A CA  1 
ATOM   45   C C   . GLN A 1 13  ? -2.279  -4.876  16.905  1.00 28.96 ? 13   GLN A C   1 
ATOM   46   O O   . GLN A 1 13  ? -1.582  -5.124  17.892  1.00 28.89 ? 13   GLN A O   1 
ATOM   47   C CB  . GLN A 1 13  ? -1.588  -6.711  15.306  1.00 29.69 ? 13   GLN A CB  1 
ATOM   48   C CG  . GLN A 1 13  ? -1.905  -8.156  14.907  1.00 31.85 ? 13   GLN A CG  1 
ATOM   49   C CD  . GLN A 1 13  ? -2.043  -9.089  16.114  1.00 35.89 ? 13   GLN A CD  1 
ATOM   50   O OE1 . GLN A 1 13  ? -1.044  -9.403  16.772  1.00 38.04 ? 13   GLN A OE1 1 
ATOM   51   N NE2 . GLN A 1 13  ? -3.283  -9.551  16.401  1.00 35.51 ? 13   GLN A NE2 1 
ATOM   52   N N   . GLY A 1 14  ? -2.678  -3.644  16.567  1.00 28.39 ? 14   GLY A N   1 
ATOM   53   C CA  . GLY A 1 14  ? -2.474  -2.473  17.427  1.00 28.07 ? 14   GLY A CA  1 
ATOM   54   C C   . GLY A 1 14  ? -1.100  -1.918  17.119  1.00 28.50 ? 14   GLY A C   1 
ATOM   55   O O   . GLY A 1 14  ? -0.670  -1.985  15.971  1.00 28.72 ? 14   GLY A O   1 
ATOM   56   N N   . TYR A 1 15  ? -0.397  -1.402  18.128  1.00 27.88 ? 15   TYR A N   1 
ATOM   57   C CA  . TYR A 1 15  ? 0.885   -0.767  17.888  1.00 28.65 ? 15   TYR A CA  1 
ATOM   58   C C   . TYR A 1 15  ? 2.081   -1.676  18.159  1.00 29.15 ? 15   TYR A C   1 
ATOM   59   O O   . TYR A 1 15  ? 2.551   -1.756  19.299  1.00 29.51 ? 15   TYR A O   1 
ATOM   60   C CB  . TYR A 1 15  ? 0.972   0.474   18.720  1.00 27.83 ? 15   TYR A CB  1 
ATOM   61   C CG  . TYR A 1 15  ? 2.215   1.300   18.501  1.00 29.19 ? 15   TYR A CG  1 
ATOM   62   C CD1 . TYR A 1 15  ? 2.251   2.320   17.527  1.00 29.20 ? 15   TYR A CD1 1 
ATOM   63   C CD2 . TYR A 1 15  ? 3.353   1.099   19.287  1.00 27.91 ? 15   TYR A CD2 1 
ATOM   64   C CE1 . TYR A 1 15  ? 3.391   3.114   17.361  1.00 28.20 ? 15   TYR A CE1 1 
ATOM   65   C CE2 . TYR A 1 15  ? 4.478   1.871   19.117  1.00 27.69 ? 15   TYR A CE2 1 
ATOM   66   C CZ  . TYR A 1 15  ? 4.500   2.875   18.167  1.00 28.10 ? 15   TYR A CZ  1 
ATOM   67   O OH  . TYR A 1 15  ? 5.653   3.609   18.052  1.00 27.00 ? 15   TYR A OH  1 
ATOM   68   N N   . GLN A 1 16  ? 2.569   -2.350  17.114  1.00 29.85 ? 16   GLN A N   1 
ATOM   69   C CA  . GLN A 1 16  ? 3.675   -3.337  17.243  1.00 30.82 ? 16   GLN A CA  1 
ATOM   70   C C   . GLN A 1 16  ? 5.050   -2.795  16.805  1.00 31.94 ? 16   GLN A C   1 
ATOM   71   O O   . GLN A 1 16  ? 6.020   -3.535  16.722  1.00 33.32 ? 16   GLN A O   1 
ATOM   72   C CB  . GLN A 1 16  ? 3.358   -4.667  16.512  1.00 29.89 ? 16   GLN A CB  1 
ATOM   73   C CG  . GLN A 1 16  ? 2.033   -5.287  16.856  1.00 29.29 ? 16   GLN A CG  1 
ATOM   74   C CD  . GLN A 1 16  ? 1.990   -5.989  18.225  1.00 31.44 ? 16   GLN A CD  1 
ATOM   75   O OE1 . GLN A 1 16  ? 3.021   -6.242  18.851  1.00 28.59 ? 16   GLN A OE1 1 
ATOM   76   N NE2 . GLN A 1 16  ? 0.777   -6.330  18.679  1.00 30.34 ? 16   GLN A NE2 1 
ATOM   77   N N   . CYS A 1 17  ? 5.137   -1.505  16.518  1.00 33.08 ? 17   CYS A N   1 
ATOM   78   C CA  . CYS A 1 17  ? 6.416   -0.870  16.272  1.00 33.66 ? 17   CYS A CA  1 
ATOM   79   C C   . CYS A 1 17  ? 7.197   -0.784  17.591  1.00 33.82 ? 17   CYS A C   1 
ATOM   80   O O   . CYS A 1 17  ? 6.603   -0.512  18.657  1.00 34.12 ? 17   CYS A O   1 
ATOM   81   C CB  . CYS A 1 17  ? 6.180   0.533   15.722  1.00 34.08 ? 17   CYS A CB  1 
ATOM   82   S SG  . CYS A 1 17  ? 4.975   0.623   14.356  1.00 36.46 ? 17   CYS A SG  1 
ATOM   83   N N   . PHE A 1 18  ? 8.515   -1.031  17.519  1.00 33.00 ? 18   PHE A N   1 
ATOM   84   C CA  . PHE A 1 18  ? 9.445   -0.796  18.634  1.00 32.30 ? 18   PHE A CA  1 
ATOM   85   C C   . PHE A 1 18  ? 9.037   -1.500  19.935  1.00 32.08 ? 18   PHE A C   1 
ATOM   86   O O   . PHE A 1 18  ? 9.234   -0.964  21.045  1.00 32.24 ? 18   PHE A O   1 
ATOM   87   C CB  . PHE A 1 18  ? 9.576   0.701   18.906  1.00 31.84 ? 18   PHE A CB  1 
ATOM   88   C CG  . PHE A 1 18  ? 9.788   1.511   17.681  1.00 32.06 ? 18   PHE A CG  1 
ATOM   89   C CD1 . PHE A 1 18  ? 10.884  1.255   16.844  1.00 31.69 ? 18   PHE A CD1 1 
ATOM   90   C CD2 . PHE A 1 18  ? 8.890   2.530   17.336  1.00 30.81 ? 18   PHE A CD2 1 
ATOM   91   C CE1 . PHE A 1 18  ? 11.074  2.018   15.674  1.00 30.73 ? 18   PHE A CE1 1 
ATOM   92   C CE2 . PHE A 1 18  ? 9.086   3.294   16.187  1.00 29.68 ? 18   PHE A CE2 1 
ATOM   93   C CZ  . PHE A 1 18  ? 10.179  3.048   15.366  1.00 29.13 ? 18   PHE A CZ  1 
ATOM   94   N N   . SER A 1 19  ? 8.493   -2.700  19.781  1.00 31.82 ? 19   SER A N   1 
ATOM   95   C CA  . SER A 1 19  ? 7.733   -3.371  20.832  1.00 31.74 ? 19   SER A CA  1 
ATOM   96   C C   . SER A 1 19  ? 8.545   -3.627  22.105  1.00 30.65 ? 19   SER A C   1 
ATOM   97   O O   . SER A 1 19  ? 7.972   -3.692  23.189  1.00 30.43 ? 19   SER A O   1 
ATOM   98   C CB  . SER A 1 19  ? 7.167   -4.683  20.294  1.00 31.94 ? 19   SER A CB  1 
ATOM   99   O OG  . SER A 1 19  ? 8.241   -5.587  20.057  1.00 34.15 ? 19   SER A OG  1 
ATOM   100  N N   . GLU A 1 20  ? 9.867   -3.745  21.960  1.00 29.68 ? 20   GLU A N   1 
ATOM   101  C CA  . GLU A 1 20  ? 10.773  -4.057  23.082  1.00 29.24 ? 20   GLU A CA  1 
ATOM   102  C C   . GLU A 1 20  ? 10.909  -2.888  24.052  1.00 27.69 ? 20   GLU A C   1 
ATOM   103  O O   . GLU A 1 20  ? 11.310  -3.081  25.179  1.00 27.48 ? 20   GLU A O   1 
ATOM   104  C CB  . GLU A 1 20  ? 12.165  -4.578  22.601  1.00 29.98 ? 20   GLU A CB  1 
ATOM   105  C CG  . GLU A 1 20  ? 13.098  -3.530  21.933  1.00 32.52 ? 20   GLU A CG  1 
ATOM   106  C CD  . GLU A 1 20  ? 12.545  -2.951  20.590  1.00 39.20 ? 20   GLU A CD  1 
ATOM   107  O OE1 . GLU A 1 20  ? 11.941  -3.725  19.787  1.00 37.48 ? 20   GLU A OE1 1 
ATOM   108  O OE2 . GLU A 1 20  ? 12.714  -1.712  20.344  1.00 41.81 ? 20   GLU A OE2 1 
ATOM   109  N N   . THR A 1 21  ? 10.554  -1.692  23.590  1.00 26.30 ? 21   THR A N   1 
ATOM   110  C CA  . THR A 1 21  ? 10.461  -0.491  24.393  1.00 25.19 ? 21   THR A CA  1 
ATOM   111  C C   . THR A 1 21  ? 8.988   -0.049  24.594  1.00 25.59 ? 21   THR A C   1 
ATOM   112  O O   . THR A 1 21  ? 8.529   0.122   25.732  1.00 24.89 ? 21   THR A O   1 
ATOM   113  C CB  . THR A 1 21  ? 11.236  0.620   23.704  1.00 24.43 ? 21   THR A CB  1 
ATOM   114  O OG1 . THR A 1 21  ? 12.605  0.258   23.700  1.00 26.35 ? 21   THR A OG1 1 
ATOM   115  C CG2 . THR A 1 21  ? 11.087  1.938   24.420  1.00 23.20 ? 21   THR A CG2 1 
ATOM   116  N N   . SER A 1 22  ? 8.259   0.128   23.488  1.00 25.47 ? 22   SER A N   1 
ATOM   117  C CA  . SER A 1 22  ? 6.918   0.753   23.515  1.00 26.07 ? 22   SER A CA  1 
ATOM   118  C C   . SER A 1 22  ? 5.883   -0.006  24.351  1.00 26.58 ? 22   SER A C   1 
ATOM   119  O O   . SER A 1 22  ? 4.906   0.592   24.818  1.00 27.77 ? 22   SER A O   1 
ATOM   120  C CB  . SER A 1 22  ? 6.385   0.947   22.093  1.00 25.72 ? 22   SER A CB  1 
ATOM   121  O OG  . SER A 1 22  ? 6.293   -0.297  21.398  1.00 25.48 ? 22   SER A OG  1 
ATOM   122  N N   . HIS A 1 23  ? 6.089   -1.312  24.521  1.00 25.91 ? 23   HIS A N   1 
ATOM   123  C CA  . HIS A 1 23  ? 5.190   -2.181  25.281  1.00 25.31 ? 23   HIS A CA  1 
ATOM   124  C C   . HIS A 1 23  ? 5.419   -2.105  26.804  1.00 24.98 ? 23   HIS A C   1 
ATOM   125  O O   . HIS A 1 23  ? 4.589   -2.585  27.592  1.00 24.33 ? 23   HIS A O   1 
ATOM   126  C CB  . HIS A 1 23  ? 5.293   -3.626  24.765  1.00 24.86 ? 23   HIS A CB  1 
ATOM   127  C CG  . HIS A 1 23  ? 4.673   -3.829  23.412  1.00 28.03 ? 23   HIS A CG  1 
ATOM   128  N ND1 . HIS A 1 23  ? 4.414   -5.083  22.883  1.00 31.83 ? 23   HIS A ND1 1 
ATOM   129  C CD2 . HIS A 1 23  ? 4.236   -2.936  22.486  1.00 28.22 ? 23   HIS A CD2 1 
ATOM   130  C CE1 . HIS A 1 23  ? 3.842   -4.948  21.693  1.00 29.78 ? 23   HIS A CE1 1 
ATOM   131  N NE2 . HIS A 1 23  ? 3.718   -3.657  21.433  1.00 27.38 ? 23   HIS A NE2 1 
ATOM   132  N N   . LEU A 1 24  ? 6.521   -1.477  27.216  1.00 24.65 ? 24   LEU A N   1 
ATOM   133  C CA  . LEU A 1 24  ? 6.846   -1.386  28.642  1.00 24.47 ? 24   LEU A CA  1 
ATOM   134  C C   . LEU A 1 24  ? 6.599   0.016   29.181  1.00 23.52 ? 24   LEU A C   1 
ATOM   135  O O   . LEU A 1 24  ? 7.241   0.415   30.158  1.00 23.19 ? 24   LEU A O   1 
ATOM   136  C CB  . LEU A 1 24  ? 8.289   -1.873  28.944  1.00 24.61 ? 24   LEU A CB  1 
ATOM   137  C CG  . LEU A 1 24  ? 8.637   -3.313  28.513  1.00 25.25 ? 24   LEU A CG  1 
ATOM   138  C CD1 . LEU A 1 24  ? 10.141  -3.526  28.380  1.00 26.55 ? 24   LEU A CD1 1 
ATOM   139  C CD2 . LEU A 1 24  ? 8.042   -4.377  29.400  1.00 23.75 ? 24   LEU A CD2 1 
ATOM   140  N N   . TRP A 1 25  ? 5.668   0.757   28.557  1.00 22.02 ? 25   TRP A N   1 
ATOM   141  C CA  . TRP A 1 25  ? 5.307   2.087   29.076  1.00 21.18 ? 25   TRP A CA  1 
ATOM   142  C C   . TRP A 1 25  ? 4.052   2.005   29.974  1.00 19.75 ? 25   TRP A C   1 
ATOM   143  O O   . TRP A 1 25  ? 3.422   3.005   30.306  1.00 18.53 ? 25   TRP A O   1 
ATOM   144  C CB  . TRP A 1 25  ? 5.110   3.089   27.941  1.00 21.16 ? 25   TRP A CB  1 
ATOM   145  C CG  . TRP A 1 25  ? 6.343   3.311   27.079  1.00 23.47 ? 25   TRP A CG  1 
ATOM   146  C CD1 . TRP A 1 25  ? 7.639   3.227   27.471  1.00 23.59 ? 25   TRP A CD1 1 
ATOM   147  C CD2 . TRP A 1 25  ? 6.371   3.691   25.693  1.00 24.41 ? 25   TRP A CD2 1 
ATOM   148  N NE1 . TRP A 1 25  ? 8.478   3.516   26.427  1.00 23.33 ? 25   TRP A NE1 1 
ATOM   149  C CE2 . TRP A 1 25  ? 7.728   3.813   25.323  1.00 25.05 ? 25   TRP A CE2 1 
ATOM   150  C CE3 . TRP A 1 25  ? 5.382   3.941   24.732  1.00 23.72 ? 25   TRP A CE3 1 
ATOM   151  C CZ2 . TRP A 1 25  ? 8.130   4.158   24.011  1.00 25.03 ? 25   TRP A CZ2 1 
ATOM   152  C CZ3 . TRP A 1 25  ? 5.781   4.297   23.429  1.00 25.10 ? 25   TRP A CZ3 1 
ATOM   153  C CH2 . TRP A 1 25  ? 7.141   4.410   23.090  1.00 24.59 ? 25   TRP A CH2 1 
ATOM   154  N N   . GLY A 1 26  ? 3.688   0.803   30.361  1.00 19.06 ? 26   GLY A N   1 
ATOM   155  C CA  . GLY A 1 26  ? 2.445   0.626   31.162  1.00 19.71 ? 26   GLY A CA  1 
ATOM   156  C C   . GLY A 1 26  ? 1.209   1.243   30.535  1.00 19.20 ? 26   GLY A C   1 
ATOM   157  O O   . GLY A 1 26  ? 0.875   0.933   29.395  1.00 19.90 ? 26   GLY A O   1 
ATOM   158  N N   . GLN A 1 27  ? 0.556   2.131   31.279  1.00 18.65 ? 27   GLN A N   1 
ATOM   159  C CA  . GLN A 1 27  ? -0.676  2.743   30.865  1.00 18.17 ? 27   GLN A CA  1 
ATOM   160  C C   . GLN A 1 27  ? -0.380  3.901   29.949  1.00 18.65 ? 27   GLN A C   1 
ATOM   161  O O   . GLN A 1 27  ? -1.317  4.591   29.457  1.00 18.72 ? 27   GLN A O   1 
ATOM   162  C CB  . GLN A 1 27  ? -1.534  3.201   32.065  1.00 18.27 ? 27   GLN A CB  1 
ATOM   163  C CG  . GLN A 1 27  ? -1.032  4.460   32.859  1.00 18.32 ? 27   GLN A CG  1 
ATOM   164  C CD  . GLN A 1 27  ? 0.225   4.200   33.678  1.00 21.50 ? 27   GLN A CD  1 
ATOM   165  O OE1 . GLN A 1 27  ? 0.361   3.146   34.317  1.00 22.63 ? 27   GLN A OE1 1 
ATOM   166  N NE2 . GLN A 1 27  ? 1.159   5.173   33.670  1.00 21.36 ? 27   GLN A NE2 1 
ATOM   167  N N   . TYR A 1 28  ? 0.911   4.116   29.713  1.00 18.53 ? 28   TYR A N   1 
ATOM   168  C CA  . TYR A 1 28  ? 1.344   5.038   28.648  1.00 19.48 ? 28   TYR A CA  1 
ATOM   169  C C   . TYR A 1 28  ? 1.666   4.305   27.353  1.00 19.48 ? 28   TYR A C   1 
ATOM   170  O O   . TYR A 1 28  ? 2.110   4.920   26.412  1.00 19.68 ? 28   TYR A O   1 
ATOM   171  C CB  . TYR A 1 28  ? 2.540   5.912   29.086  1.00 20.00 ? 28   TYR A CB  1 
ATOM   172  C CG  . TYR A 1 28  ? 2.252   6.844   30.256  1.00 20.73 ? 28   TYR A CG  1 
ATOM   173  C CD1 . TYR A 1 28  ? 0.970   7.434   30.429  1.00 23.40 ? 28   TYR A CD1 1 
ATOM   174  C CD2 . TYR A 1 28  ? 3.228   7.133   31.191  1.00 21.22 ? 28   TYR A CD2 1 
ATOM   175  C CE1 . TYR A 1 28  ? 0.689   8.272   31.513  1.00 21.62 ? 28   TYR A CE1 1 
ATOM   176  C CE2 . TYR A 1 28  ? 2.958   7.995   32.291  1.00 22.57 ? 28   TYR A CE2 1 
ATOM   177  C CZ  . TYR A 1 28  ? 1.693   8.542   32.440  1.00 23.05 ? 28   TYR A CZ  1 
ATOM   178  O OH  . TYR A 1 28  ? 1.442   9.380   33.497  1.00 23.23 ? 28   TYR A OH  1 
ATOM   179  N N   . ALA A 1 29  ? 1.459   2.988   27.311  1.00 19.63 ? 29   ALA A N   1 
ATOM   180  C CA  . ALA A 1 29  ? 1.733   2.224   26.095  1.00 19.61 ? 29   ALA A CA  1 
ATOM   181  C C   . ALA A 1 29  ? 0.541   2.287   25.188  1.00 20.10 ? 29   ALA A C   1 
ATOM   182  O O   . ALA A 1 29  ? -0.610  2.181   25.642  1.00 21.20 ? 29   ALA A O   1 
ATOM   183  C CB  . ALA A 1 29  ? 2.063   0.791   26.393  1.00 19.26 ? 29   ALA A CB  1 
ATOM   184  N N   . PRO A 1 30  ? 0.793   2.472   23.894  1.00 20.23 ? 30   PRO A N   1 
ATOM   185  C CA  . PRO A 1 30  ? -0.326  2.444   22.937  1.00 19.15 ? 30   PRO A CA  1 
ATOM   186  C C   . PRO A 1 30  ? -0.909  1.064   22.909  1.00 18.39 ? 30   PRO A C   1 
ATOM   187  O O   . PRO A 1 30  ? -0.157  0.087   23.090  1.00 18.54 ? 30   PRO A O   1 
ATOM   188  C CB  . PRO A 1 30  ? 0.337   2.728   21.600  1.00 19.86 ? 30   PRO A CB  1 
ATOM   189  C CG  . PRO A 1 30  ? 1.839   2.617   21.817  1.00 20.07 ? 30   PRO A CG  1 
ATOM   190  C CD  . PRO A 1 30  ? 2.127   2.371   23.256  1.00 20.40 ? 30   PRO A CD  1 
ATOM   191  N N   . PHE A 1 31  ? -2.232  0.945   22.748  1.00 17.93 ? 31   PHE A N   1 
ATOM   192  C CA  . PHE A 1 31  ? -2.821  -0.403  22.565  1.00 17.04 ? 31   PHE A CA  1 
ATOM   193  C C   . PHE A 1 31  ? -1.965  -1.345  21.682  1.00 16.84 ? 31   PHE A C   1 
ATOM   194  O O   . PHE A 1 31  ? -1.569  -0.977  20.592  1.00 16.12 ? 31   PHE A O   1 
ATOM   195  C CB  . PHE A 1 31  ? -4.191  -0.333  21.922  1.00 16.84 ? 31   PHE A CB  1 
ATOM   196  C CG  . PHE A 1 31  ? -4.728  -1.688  21.574  1.00 16.74 ? 31   PHE A CG  1 
ATOM   197  C CD1 . PHE A 1 31  ? -5.084  -2.573  22.581  1.00 15.81 ? 31   PHE A CD1 1 
ATOM   198  C CD2 . PHE A 1 31  ? -4.850  -2.098  20.250  1.00 17.10 ? 31   PHE A CD2 1 
ATOM   199  C CE1 . PHE A 1 31  ? -5.568  -3.861  22.264  1.00 17.09 ? 31   PHE A CE1 1 
ATOM   200  C CE2 . PHE A 1 31  ? -5.339  -3.383  19.919  1.00 14.91 ? 31   PHE A CE2 1 
ATOM   201  C CZ  . PHE A 1 31  ? -5.682  -4.258  20.918  1.00 15.51 ? 31   PHE A CZ  1 
ATOM   202  N N   . PHE A 1 32  ? -1.729  -2.569  22.151  1.00 17.50 ? 32   PHE A N   1 
ATOM   203  C CA  . PHE A 1 32  ? -1.135  -3.623  21.329  1.00 18.11 ? 32   PHE A CA  1 
ATOM   204  C C   . PHE A 1 32  ? -1.841  -4.898  21.648  1.00 18.44 ? 32   PHE A C   1 
ATOM   205  O O   . PHE A 1 32  ? -1.923  -5.257  22.802  1.00 18.59 ? 32   PHE A O   1 
ATOM   206  C CB  . PHE A 1 32  ? 0.401   -3.750  21.519  1.00 18.18 ? 32   PHE A CB  1 
ATOM   207  C CG  . PHE A 1 32  ? 0.827   -4.017  22.953  1.00 19.06 ? 32   PHE A CG  1 
ATOM   208  C CD1 . PHE A 1 32  ? 0.969   -2.959  23.860  1.00 19.30 ? 32   PHE A CD1 1 
ATOM   209  C CD2 . PHE A 1 32  ? 1.084   -5.328  23.380  1.00 20.98 ? 32   PHE A CD2 1 
ATOM   210  C CE1 . PHE A 1 32  ? 1.315   -3.199  25.180  1.00 21.75 ? 32   PHE A CE1 1 
ATOM   211  C CE2 . PHE A 1 32  ? 1.440   -5.597  24.700  1.00 22.86 ? 32   PHE A CE2 1 
ATOM   212  C CZ  . PHE A 1 32  ? 1.551   -4.537  25.607  1.00 23.30 ? 32   PHE A CZ  1 
ATOM   213  N N   . SER A 1 33  ? -2.367  -5.575  20.614  1.00 19.04 ? 33   SER A N   1 
ATOM   214  C CA  . SER A 1 33  ? -3.130  -6.803  20.788  1.00 18.86 ? 33   SER A CA  1 
ATOM   215  C C   . SER A 1 33  ? -2.351  -7.978  21.370  1.00 19.83 ? 33   SER A C   1 
ATOM   216  O O   . SER A 1 33  ? -1.278  -8.296  20.931  1.00 19.92 ? 33   SER A O   1 
ATOM   217  C CB  . SER A 1 33  ? -3.751  -7.267  19.470  1.00 18.80 ? 33   SER A CB  1 
ATOM   218  O OG  . SER A 1 33  ? -4.353  -8.567  19.632  1.00 16.15 ? 33   SER A OG  1 
ATOM   219  N N   . LEU A 1 34  ? -2.954  -8.657  22.333  1.00 20.65 ? 34   LEU A N   1 
ATOM   220  C CA  . LEU A 1 34  ? -2.304  -9.766  22.967  1.00 21.09 ? 34   LEU A CA  1 
ATOM   221  C C   . LEU A 1 34  ? -2.775  -11.092 22.400  1.00 22.50 ? 34   LEU A C   1 
ATOM   222  O O   . LEU A 1 34  ? -2.643  -12.125 23.049  1.00 21.86 ? 34   LEU A O   1 
ATOM   223  C CB  . LEU A 1 34  ? -2.582  -9.695  24.473  1.00 20.67 ? 34   LEU A CB  1 
ATOM   224  C CG  . LEU A 1 34  ? -1.948  -8.480  25.169  1.00 18.97 ? 34   LEU A CG  1 
ATOM   225  C CD1 . LEU A 1 34  ? -2.402  -8.379  26.587  1.00 18.64 ? 34   LEU A CD1 1 
ATOM   226  C CD2 . LEU A 1 34  ? -0.445  -8.612  25.084  1.00 19.65 ? 34   LEU A CD2 1 
ATOM   227  N N   . ALA A 1 35  ? -3.342  -11.066 21.195  1.00 24.33 ? 35   ALA A N   1 
ATOM   228  C CA  . ALA A 1 35  ? -4.001  -12.267 20.654  1.00 26.29 ? 35   ALA A CA  1 
ATOM   229  C C   . ALA A 1 35  ? -3.017  -13.429 20.531  1.00 27.94 ? 35   ALA A C   1 
ATOM   230  O O   . ALA A 1 35  ? -3.374  -14.553 20.857  1.00 28.73 ? 35   ALA A O   1 
ATOM   231  C CB  . ALA A 1 35  ? -4.714  -11.980 19.288  1.00 25.53 ? 35   ALA A CB  1 
ATOM   232  N N   . ASN A 1 36  ? -1.794  -13.140 20.070  1.00 30.21 ? 36   ASN A N   1 
ATOM   233  C CA  . ASN A 1 36  ? -0.683  -14.096 19.963  1.00 32.78 ? 36   ASN A CA  1 
ATOM   234  C C   . ASN A 1 36  ? -0.188  -14.637 21.287  1.00 33.61 ? 36   ASN A C   1 
ATOM   235  O O   . ASN A 1 36  ? 0.508   -15.662 21.345  1.00 33.80 ? 36   ASN A O   1 
ATOM   236  C CB  . ASN A 1 36  ? 0.502   -13.393 19.350  1.00 33.51 ? 36   ASN A CB  1 
ATOM   237  C CG  . ASN A 1 36  ? 0.346   -13.205 17.878  1.00 37.95 ? 36   ASN A CG  1 
ATOM   238  O OD1 . ASN A 1 36  ? -0.650  -13.650 17.270  1.00 41.57 ? 36   ASN A OD1 1 
ATOM   239  N ND2 . ASN A 1 36  ? 1.332   -12.539 17.268  1.00 41.85 ? 36   ASN A ND2 1 
ATOM   240  N N   . GLU A 1 37  ? -0.520  -13.911 22.351  1.00 34.39 ? 37   GLU A N   1 
ATOM   241  C CA  . GLU A 1 37  ? -0.160  -14.293 23.701  1.00 35.10 ? 37   GLU A CA  1 
ATOM   242  C C   . GLU A 1 37  ? -1.251  -15.104 24.400  1.00 35.12 ? 37   GLU A C   1 
ATOM   243  O O   . GLU A 1 37  ? -1.049  -15.596 25.517  1.00 34.95 ? 37   GLU A O   1 
ATOM   244  C CB  . GLU A 1 37  ? 0.162   -13.037 24.493  1.00 35.55 ? 37   GLU A CB  1 
ATOM   245  C CG  . GLU A 1 37  ? 1.380   -12.268 23.967  1.00 38.43 ? 37   GLU A CG  1 
ATOM   246  C CD  . GLU A 1 37  ? 2.689   -12.981 24.253  1.00 41.93 ? 37   GLU A CD  1 
ATOM   247  O OE1 . GLU A 1 37  ? 2.677   -14.053 24.913  1.00 43.28 ? 37   GLU A OE1 1 
ATOM   248  O OE2 . GLU A 1 37  ? 3.739   -12.470 23.813  1.00 45.15 ? 37   GLU A OE2 1 
ATOM   249  N N   . SER A 1 38  ? -2.396  -15.251 23.733  1.00 35.02 ? 38   SER A N   1 
ATOM   250  C CA  . SER A 1 38  ? -3.527  -15.971 24.298  1.00 35.43 ? 38   SER A CA  1 
ATOM   251  C C   . SER A 1 38  ? -3.283  -17.471 24.166  1.00 36.26 ? 38   SER A C   1 
ATOM   252  O O   . SER A 1 38  ? -3.125  -18.000 23.036  1.00 37.24 ? 38   SER A O   1 
ATOM   253  C CB  . SER A 1 38  ? -4.820  -15.583 23.575  1.00 35.41 ? 38   SER A CB  1 
ATOM   254  O OG  . SER A 1 38  ? -5.969  -15.931 24.332  1.00 34.37 ? 38   SER A OG  1 
ATOM   255  N N   . VAL A 1 39  ? -3.246  -18.175 25.293  1.00 35.93 ? 39   VAL A N   1 
ATOM   256  C CA  . VAL A 1 39  ? -3.098  -19.613 25.218  1.00 35.55 ? 39   VAL A CA  1 
ATOM   257  C C   . VAL A 1 39  ? -4.416  -20.235 24.774  1.00 35.38 ? 39   VAL A C   1 
ATOM   258  O O   . VAL A 1 39  ? -4.426  -21.254 24.076  1.00 35.82 ? 39   VAL A O   1 
ATOM   259  C CB  . VAL A 1 39  ? -2.578  -20.197 26.538  1.00 35.89 ? 39   VAL A CB  1 
ATOM   260  C CG1 . VAL A 1 39  ? -2.523  -21.731 26.499  1.00 34.80 ? 39   VAL A CG1 1 
ATOM   261  C CG2 . VAL A 1 39  ? -1.187  -19.592 26.842  1.00 36.85 ? 39   VAL A CG2 1 
ATOM   262  N N   . ILE A 1 40  ? -5.537  -19.638 25.163  1.00 34.81 ? 40   ILE A N   1 
ATOM   263  C CA  . ILE A 1 40  ? -6.826  -20.123 24.660  1.00 34.37 ? 40   ILE A CA  1 
ATOM   264  C C   . ILE A 1 40  ? -7.151  -19.336 23.399  1.00 34.88 ? 40   ILE A C   1 
ATOM   265  O O   . ILE A 1 40  ? -6.856  -18.125 23.311  1.00 34.57 ? 40   ILE A O   1 
ATOM   266  C CB  . ILE A 1 40  ? -7.942  -20.004 25.724  1.00 34.15 ? 40   ILE A CB  1 
ATOM   267  C CG1 . ILE A 1 40  ? -7.624  -20.900 26.935  1.00 33.48 ? 40   ILE A CG1 1 
ATOM   268  C CG2 . ILE A 1 40  ? -9.306  -20.319 25.136  1.00 32.47 ? 40   ILE A CG2 1 
ATOM   269  C CD1 . ILE A 1 40  ? -8.201  -20.383 28.281  1.00 31.03 ? 40   ILE A CD1 1 
ATOM   270  N N   . SER A 1 41  ? -7.719  -20.016 22.411  1.00 35.56 ? 41   SER A N   1 
ATOM   271  C CA  . SER A 1 41  ? -8.005  -19.360 21.138  1.00 36.89 ? 41   SER A CA  1 
ATOM   272  C C   . SER A 1 41  ? -9.149  -18.363 21.311  1.00 37.26 ? 41   SER A C   1 
ATOM   273  O O   . SER A 1 41  ? -10.190 -18.695 21.900  1.00 37.58 ? 41   SER A O   1 
ATOM   274  C CB  . SER A 1 41  ? -8.303  -20.369 20.016  1.00 37.02 ? 41   SER A CB  1 
ATOM   275  O OG  . SER A 1 41  ? -8.394  -19.705 18.759  1.00 38.23 ? 41   SER A OG  1 
ATOM   276  N N   . PRO A 1 42  ? -8.939  -17.126 20.835  1.00 38.11 ? 42   PRO A N   1 
ATOM   277  C CA  . PRO A 1 42  ? -10.006 -16.118 20.846  1.00 38.82 ? 42   PRO A CA  1 
ATOM   278  C C   . PRO A 1 42  ? -11.184 -16.451 19.903  1.00 39.35 ? 42   PRO A C   1 
ATOM   279  O O   . PRO A 1 42  ? -12.314 -16.009 20.153  1.00 39.57 ? 42   PRO A O   1 
ATOM   280  C CB  . PRO A 1 42  ? -9.281  -14.822 20.436  1.00 38.74 ? 42   PRO A CB  1 
ATOM   281  C CG  . PRO A 1 42  ? -8.072  -15.299 19.645  1.00 38.24 ? 42   PRO A CG  1 
ATOM   282  C CD  . PRO A 1 42  ? -7.664  -16.591 20.301  1.00 37.96 ? 42   PRO A CD  1 
ATOM   283  N N   . GLU A 1 43  ? -10.934 -17.223 18.847  1.00 39.98 ? 43   GLU A N   1 
ATOM   284  C CA  . GLU A 1 43  ? -12.019 -17.669 17.956  1.00 41.13 ? 43   GLU A CA  1 
ATOM   285  C C   . GLU A 1 43  ? -13.223 -18.295 18.679  1.00 41.38 ? 43   GLU A C   1 
ATOM   286  O O   . GLU A 1 43  ? -13.092 -18.961 19.732  1.00 41.41 ? 43   GLU A O   1 
ATOM   287  C CB  . GLU A 1 43  ? -11.514 -18.630 16.883  1.00 40.97 ? 43   GLU A CB  1 
ATOM   288  C CG  . GLU A 1 43  ? -10.986 -17.932 15.648  1.00 43.74 ? 43   GLU A CG  1 
ATOM   289  C CD  . GLU A 1 43  ? -9.484  -17.710 15.715  1.00 48.57 ? 43   GLU A CD  1 
ATOM   290  O OE1 . GLU A 1 43  ? -8.722  -18.550 15.169  1.00 51.31 ? 43   GLU A OE1 1 
ATOM   291  O OE2 . GLU A 1 43  ? -9.048  -16.712 16.331  1.00 49.11 ? 43   GLU A OE2 1 
ATOM   292  N N   . VAL A 1 44  ? -14.385 -18.065 18.087  1.00 41.17 ? 44   VAL A N   1 
ATOM   293  C CA  . VAL A 1 44  ? -15.639 -18.663 18.516  1.00 41.71 ? 44   VAL A CA  1 
ATOM   294  C C   . VAL A 1 44  ? -15.597 -20.159 18.198  1.00 41.58 ? 44   VAL A C   1 
ATOM   295  O O   . VAL A 1 44  ? -15.332 -20.542 17.049  1.00 41.78 ? 44   VAL A O   1 
ATOM   296  C CB  . VAL A 1 44  ? -16.817 -18.029 17.732  1.00 42.09 ? 44   VAL A CB  1 
ATOM   297  C CG1 . VAL A 1 44  ? -18.177 -18.444 18.311  1.00 42.76 ? 44   VAL A CG1 1 
ATOM   298  C CG2 . VAL A 1 44  ? -16.671 -16.509 17.689  1.00 42.52 ? 44   VAL A CG2 1 
ATOM   299  N N   . PRO A 1 45  ? -15.856 -21.017 19.205  1.00 41.21 ? 45   PRO A N   1 
ATOM   300  C CA  . PRO A 1 45  ? -15.768 -22.437 18.889  1.00 40.73 ? 45   PRO A CA  1 
ATOM   301  C C   . PRO A 1 45  ? -16.877 -22.864 17.941  1.00 40.48 ? 45   PRO A C   1 
ATOM   302  O O   . PRO A 1 45  ? -17.925 -22.197 17.839  1.00 39.86 ? 45   PRO A O   1 
ATOM   303  C CB  . PRO A 1 45  ? -15.933 -23.120 20.262  1.00 40.75 ? 45   PRO A CB  1 
ATOM   304  C CG  . PRO A 1 45  ? -15.511 -22.109 21.236  1.00 40.45 ? 45   PRO A CG  1 
ATOM   305  C CD  . PRO A 1 45  ? -15.952 -20.790 20.660  1.00 41.07 ? 45   PRO A CD  1 
ATOM   306  N N   . ALA A 1 46  ? -16.635 -23.978 17.257  1.00 39.80 ? 46   ALA A N   1 
ATOM   307  C CA  . ALA A 1 46  ? -17.640 -24.564 16.396  1.00 39.16 ? 46   ALA A CA  1 
ATOM   308  C C   . ALA A 1 46  ? -18.815 -25.014 17.249  1.00 38.04 ? 46   ALA A C   1 
ATOM   309  O O   . ALA A 1 46  ? -18.635 -25.430 18.391  1.00 38.54 ? 46   ALA A O   1 
ATOM   310  C CB  . ALA A 1 46  ? -17.050 -25.744 15.623  1.00 39.72 ? 46   ALA A CB  1 
ATOM   311  N N   . GLY A 1 47  ? -20.009 -24.924 16.683  1.00 36.97 ? 47   GLY A N   1 
ATOM   312  C CA  . GLY A 1 47  ? -21.240 -25.281 17.376  1.00 35.79 ? 47   GLY A CA  1 
ATOM   313  C C   . GLY A 1 47  ? -21.758 -24.111 18.190  1.00 34.96 ? 47   GLY A C   1 
ATOM   314  O O   . GLY A 1 47  ? -22.898 -24.150 18.654  1.00 35.20 ? 47   GLY A O   1 
ATOM   315  N N   . CYS A 1 48  ? -20.922 -23.071 18.323  1.00 33.50 ? 48   CYS A N   1 
ATOM   316  C CA  . CYS A 1 48  ? -21.185 -21.930 19.195  1.00 32.65 ? 48   CYS A CA  1 
ATOM   317  C C   . CYS A 1 48  ? -21.546 -20.629 18.456  1.00 31.56 ? 48   CYS A C   1 
ATOM   318  O O   . CYS A 1 48  ? -20.967 -20.293 17.395  1.00 31.29 ? 48   CYS A O   1 
ATOM   319  C CB  . CYS A 1 48  ? -19.966 -21.671 20.103  1.00 33.31 ? 48   CYS A CB  1 
ATOM   320  S SG  . CYS A 1 48  ? -19.640 -22.985 21.370  1.00 32.83 ? 48   CYS A SG  1 
ATOM   321  N N   . ARG A 1 49  ? -22.463 -19.878 19.055  1.00 29.25 ? 49   ARG A N   1 
ATOM   322  C CA  A ARG A 1 49  ? -22.950 -18.616 18.510  0.50 28.12 ? 49   ARG A CA  1 
ATOM   323  C CA  B ARG A 1 49  ? -22.774 -18.562 18.520  0.50 27.59 ? 49   ARG A CA  1 
ATOM   324  C C   . ARG A 1 49  ? -22.946 -17.486 19.574  1.00 26.81 ? 49   ARG A C   1 
ATOM   325  O O   . ARG A 1 49  ? -23.610 -17.645 20.603  1.00 26.31 ? 49   ARG A O   1 
ATOM   326  C CB  A ARG A 1 49  ? -24.369 -18.890 17.963  0.50 28.10 ? 49   ARG A CB  1 
ATOM   327  C CB  B ARG A 1 49  ? -23.943 -18.581 17.519  0.50 27.50 ? 49   ARG A CB  1 
ATOM   328  C CG  A ARG A 1 49  ? -25.128 -17.722 17.377  0.50 29.15 ? 49   ARG A CG  1 
ATOM   329  C CG  B ARG A 1 49  ? -23.622 -17.744 16.274  0.50 25.48 ? 49   ARG A CG  1 
ATOM   330  C CD  A ARG A 1 49  ? -26.581 -18.121 17.067  0.50 29.85 ? 49   ARG A CD  1 
ATOM   331  C CD  B ARG A 1 49  ? -24.789 -17.620 15.323  0.50 23.01 ? 49   ARG A CD  1 
ATOM   332  N NE  A ARG A 1 49  ? -27.230 -18.842 18.162  0.50 28.64 ? 49   ARG A NE  1 
ATOM   333  N NE  B ARG A 1 49  ? -24.320 -17.653 13.948  0.50 20.04 ? 49   ARG A NE  1 
ATOM   334  C CZ  A ARG A 1 49  ? -28.376 -18.478 18.727  0.50 29.41 ? 49   ARG A CZ  1 
ATOM   335  C CZ  B ARG A 1 49  ? -24.178 -18.779 13.261  0.50 18.27 ? 49   ARG A CZ  1 
ATOM   336  N NH1 A ARG A 1 49  ? -29.020 -17.390 18.319  0.50 30.18 ? 49   ARG A NH1 1 
ATOM   337  N NH1 B ARG A 1 49  ? -24.474 -19.950 13.833  0.50 18.60 ? 49   ARG A NH1 1 
ATOM   338  N NH2 A ARG A 1 49  ? -28.887 -19.207 19.705  0.50 29.43 ? 49   ARG A NH2 1 
ATOM   339  N NH2 B ARG A 1 49  ? -23.735 -18.740 12.020  0.50 14.68 ? 49   ARG A NH2 1 
ATOM   340  N N   . VAL A 1 50  ? -22.258 -16.370 19.315  1.00 25.75 ? 50   VAL A N   1 
ATOM   341  C CA  . VAL A 1 50  ? -22.259 -15.208 20.211  1.00 23.69 ? 50   VAL A CA  1 
ATOM   342  C C   . VAL A 1 50  ? -23.634 -14.495 20.187  1.00 23.50 ? 50   VAL A C   1 
ATOM   343  O O   . VAL A 1 50  ? -24.142 -14.117 19.125  1.00 23.05 ? 50   VAL A O   1 
ATOM   344  C CB  . VAL A 1 50  ? -21.172 -14.187 19.823  1.00 24.53 ? 50   VAL A CB  1 
ATOM   345  C CG1 . VAL A 1 50  ? -21.021 -13.105 20.894  1.00 23.44 ? 50   VAL A CG1 1 
ATOM   346  C CG2 . VAL A 1 50  ? -19.807 -14.851 19.531  1.00 23.96 ? 50   VAL A CG2 1 
ATOM   347  N N   . THR A 1 51  ? -24.235 -14.309 21.355  1.00 22.65 ? 51   THR A N   1 
ATOM   348  C CA  . THR A 1 51  ? -25.580 -13.729 21.451  1.00 22.38 ? 51   THR A CA  1 
ATOM   349  C C   . THR A 1 51  ? -25.642 -12.424 22.278  1.00 21.66 ? 51   THR A C   1 
ATOM   350  O O   . THR A 1 51  ? -26.739 -11.930 22.579  1.00 21.74 ? 51   THR A O   1 
ATOM   351  C CB  . THR A 1 51  ? -26.555 -14.752 22.060  1.00 23.06 ? 51   THR A CB  1 
ATOM   352  O OG1 . THR A 1 51  ? -26.149 -15.081 23.405  1.00 23.60 ? 51   THR A OG1 1 
ATOM   353  C CG2 . THR A 1 51  ? -26.572 -16.031 21.233  1.00 23.57 ? 51   THR A CG2 1 
ATOM   354  N N   . PHE A 1 52  ? -24.459 -11.902 22.652  1.00 20.72 ? 52   PHE A N   1 
ATOM   355  C CA  . PHE A 1 52  ? -24.264 -10.717 23.576  1.00 19.46 ? 52   PHE A CA  1 
ATOM   356  C C   . PHE A 1 52  ? -22.825 -10.269 23.389  1.00 18.53 ? 52   PHE A C   1 
ATOM   357  O O   . PHE A 1 52  ? -21.917 -11.103 23.366  1.00 18.42 ? 52   PHE A O   1 
ATOM   358  C CB  . PHE A 1 52  ? -24.479 -11.121 25.055  1.00 19.16 ? 52   PHE A CB  1 
ATOM   359  C CG  . PHE A 1 52  ? -24.308 -9.991  26.070  1.00 18.66 ? 52   PHE A CG  1 
ATOM   360  C CD1 . PHE A 1 52  ? -23.055 -9.676  26.583  1.00 15.38 ? 52   PHE A CD1 1 
ATOM   361  C CD2 . PHE A 1 52  ? -25.434 -9.277  26.562  1.00 18.69 ? 52   PHE A CD2 1 
ATOM   362  C CE1 . PHE A 1 52  ? -22.899 -8.650  27.490  1.00 15.15 ? 52   PHE A CE1 1 
ATOM   363  C CE2 . PHE A 1 52  ? -25.283 -8.243  27.506  1.00 15.89 ? 52   PHE A CE2 1 
ATOM   364  C CZ  . PHE A 1 52  ? -24.015 -7.928  27.945  1.00 16.58 ? 52   PHE A CZ  1 
ATOM   365  N N   . ALA A 1 53  ? -22.620 -8.972  23.211  1.00 17.51 ? 53   ALA A N   1 
ATOM   366  C CA  . ALA A 1 53  ? -21.281 -8.400  23.300  1.00 17.00 ? 53   ALA A CA  1 
ATOM   367  C C   . ALA A 1 53  ? -21.298 -7.007  23.919  1.00 15.61 ? 53   ALA A C   1 
ATOM   368  O O   . ALA A 1 53  ? -21.968 -6.116  23.442  1.00 14.96 ? 53   ALA A O   1 
ATOM   369  C CB  . ALA A 1 53  ? -20.529 -8.421  21.907  1.00 16.62 ? 53   ALA A CB  1 
ATOM   370  N N   . GLN A 1 54  ? -20.582 -6.870  25.033  1.00 15.48 ? 54   GLN A N   1 
ATOM   371  C CA  . GLN A 1 54  ? -20.312 -5.594  25.712  1.00 14.40 ? 54   GLN A CA  1 
ATOM   372  C C   . GLN A 1 54  ? -18.834 -5.317  25.563  1.00 13.99 ? 54   GLN A C   1 
ATOM   373  O O   . GLN A 1 54  ? -18.017 -6.215  25.764  1.00 14.00 ? 54   GLN A O   1 
ATOM   374  C CB  . GLN A 1 54  ? -20.665 -5.646  27.204  1.00 14.12 ? 54   GLN A CB  1 
ATOM   375  C CG  . GLN A 1 54  ? -20.361 -4.318  27.991  1.00 15.95 ? 54   GLN A CG  1 
ATOM   376  C CD  . GLN A 1 54  ? -21.256 -4.129  29.224  1.00 19.20 ? 54   GLN A CD  1 
ATOM   377  O OE1 . GLN A 1 54  ? -22.489 -3.988  29.112  1.00 20.64 ? 54   GLN A OE1 1 
ATOM   378  N NE2 . GLN A 1 54  ? -20.635 -4.102  30.412  1.00 17.07 ? 54   GLN A NE2 1 
ATOM   379  N N   . VAL A 1 55  ? -18.495 -4.089  25.187  1.00 13.92 ? 55   VAL A N   1 
ATOM   380  C CA  . VAL A 1 55  ? -17.100 -3.658  25.170  1.00 14.60 ? 55   VAL A CA  1 
ATOM   381  C C   . VAL A 1 55  ? -16.917 -2.506  26.162  1.00 14.72 ? 55   VAL A C   1 
ATOM   382  O O   . VAL A 1 55  ? -17.705 -1.569  26.159  1.00 15.25 ? 55   VAL A O   1 
ATOM   383  C CB  . VAL A 1 55  ? -16.635 -3.220  23.789  1.00 14.41 ? 55   VAL A CB  1 
ATOM   384  C CG1 . VAL A 1 55  ? -17.636 -2.203  23.184  1.00 13.64 ? 55   VAL A CG1 1 
ATOM   385  C CG2 . VAL A 1 55  ? -15.211 -2.631  23.869  1.00 13.83 ? 55   VAL A CG2 1 
ATOM   386  N N   . LEU A 1 56  ? -15.930 -2.623  27.040  1.00 14.37 ? 56   LEU A N   1 
ATOM   387  C CA  . LEU A 1 56  ? -15.499 -1.500  27.873  1.00 14.44 ? 56   LEU A CA  1 
ATOM   388  C C   . LEU A 1 56  ? -14.152 -0.971  27.363  1.00 15.35 ? 56   LEU A C   1 
ATOM   389  O O   . LEU A 1 56  ? -13.178 -1.739  27.190  1.00 15.86 ? 56   LEU A O   1 
ATOM   390  C CB  . LEU A 1 56  ? -15.446 -1.909  29.355  1.00 14.71 ? 56   LEU A CB  1 
ATOM   391  C CG  . LEU A 1 56  ? -14.970 -0.842  30.383  1.00 13.45 ? 56   LEU A CG  1 
ATOM   392  C CD1 . LEU A 1 56  ? -15.865 0.397   30.466  1.00 6.90  ? 56   LEU A CD1 1 
ATOM   393  C CD2 . LEU A 1 56  ? -14.879 -1.492  31.709  1.00 11.04 ? 56   LEU A CD2 1 
ATOM   394  N N   . SER A 1 57  ? -14.088 0.327   27.063  1.00 16.20 ? 57   SER A N   1 
ATOM   395  C CA  . SER A 1 57  ? -12.909 0.846   26.386  1.00 15.97 ? 57   SER A CA  1 
ATOM   396  C C   . SER A 1 57  ? -12.347 2.057   27.075  1.00 17.13 ? 57   SER A C   1 
ATOM   397  O O   . SER A 1 57  ? -13.096 2.881   27.629  1.00 18.60 ? 57   SER A O   1 
ATOM   398  C CB  . SER A 1 57  ? -13.225 1.168   24.911  1.00 16.73 ? 57   SER A CB  1 
ATOM   399  O OG  . SER A 1 57  ? -12.087 1.690   24.220  1.00 14.89 ? 57   SER A OG  1 
ATOM   400  N N   . ARG A 1 58  ? -11.015 2.186   27.049  1.00 17.69 ? 58   ARG A N   1 
ATOM   401  C CA  . ARG A 1 58  ? -10.371 3.352   27.612  1.00 16.94 ? 58   ARG A CA  1 
ATOM   402  C C   . ARG A 1 58  ? -10.341 4.381   26.516  1.00 17.17 ? 58   ARG A C   1 
ATOM   403  O O   . ARG A 1 58  ? -10.514 4.025   25.366  1.00 16.91 ? 58   ARG A O   1 
ATOM   404  C CB  . ARG A 1 58  ? -8.950  3.019   28.043  1.00 17.40 ? 58   ARG A CB  1 
ATOM   405  C CG  . ARG A 1 58  ? -8.273  4.171   28.807  1.00 15.21 ? 58   ARG A CG  1 
ATOM   406  C CD  . ARG A 1 58  ? -6.931  3.785   29.304  1.00 13.63 ? 58   ARG A CD  1 
ATOM   407  N NE  . ARG A 1 58  ? -6.200  4.974   29.740  1.00 15.86 ? 58   ARG A NE  1 
ATOM   408  C CZ  . ARG A 1 58  ? -4.873  5.062   29.857  1.00 11.70 ? 58   ARG A CZ  1 
ATOM   409  N NH1 . ARG A 1 58  ? -4.096  4.022   29.579  1.00 10.04 ? 58   ARG A NH1 1 
ATOM   410  N NH2 . ARG A 1 58  ? -4.341  6.218   30.218  1.00 8.81  ? 58   ARG A NH2 1 
ATOM   411  N N   . HIS A 1 59  ? -10.119 5.650   26.852  1.00 17.18 ? 59   HIS A N   1 
ATOM   412  C CA  . HIS A 1 59  ? -9.829  6.635   25.820  1.00 16.98 ? 59   HIS A CA  1 
ATOM   413  C C   . HIS A 1 59  ? -8.519  6.319   25.137  1.00 16.98 ? 59   HIS A C   1 
ATOM   414  O O   . HIS A 1 59  ? -7.789  5.416   25.537  1.00 16.29 ? 59   HIS A O   1 
ATOM   415  C CB  . HIS A 1 59  ? -9.798  8.066   26.346  1.00 16.90 ? 59   HIS A CB  1 
ATOM   416  C CG  . HIS A 1 59  ? -8.810  8.267   27.440  1.00 16.58 ? 59   HIS A CG  1 
ATOM   417  N ND1 . HIS A 1 59  ? -7.455  8.415   27.205  1.00 15.61 ? 59   HIS A ND1 1 
ATOM   418  C CD2 . HIS A 1 59  ? -8.980  8.351   28.781  1.00 11.99 ? 59   HIS A CD2 1 
ATOM   419  C CE1 . HIS A 1 59  ? -6.833  8.568   28.361  1.00 14.02 ? 59   HIS A CE1 1 
ATOM   420  N NE2 . HIS A 1 59  ? -7.735  8.536   29.329  1.00 13.63 ? 59   HIS A NE2 1 
ATOM   421  N N   . GLY A 1 60  ? -8.257  7.055   24.062  1.00 17.37 ? 60   GLY A N   1 
ATOM   422  C CA  . GLY A 1 60  ? -7.055  6.841   23.275  1.00 18.04 ? 60   GLY A CA  1 
ATOM   423  C C   . GLY A 1 60  ? -5.900  7.599   23.875  1.00 18.38 ? 60   GLY A C   1 
ATOM   424  O O   . GLY A 1 60  ? -6.066  8.303   24.857  1.00 18.50 ? 60   GLY A O   1 
ATOM   425  N N   . ALA A 1 61  ? -4.737  7.436   23.259  1.00 19.18 ? 61   ALA A N   1 
ATOM   426  C CA  . ALA A 1 61  ? -3.547  8.186   23.561  1.00 20.29 ? 61   ALA A CA  1 
ATOM   427  C C   . ALA A 1 61  ? -3.796  9.689   23.664  1.00 22.12 ? 61   ALA A C   1 
ATOM   428  O O   . ALA A 1 61  ? -4.488  10.286  22.833  1.00 22.99 ? 61   ALA A O   1 
ATOM   429  C CB  . ALA A 1 61  ? -2.502  7.881   22.513  1.00 19.89 ? 61   ALA A CB  1 
ATOM   430  N N   . ARG A 1 62  ? -3.254  10.302  24.706  1.00 23.61 ? 62   ARG A N   1 
ATOM   431  C CA  . ARG A 1 62  ? -3.497  11.719  24.963  1.00 25.09 ? 62   ARG A CA  1 
ATOM   432  C C   . ARG A 1 62  ? -2.194  12.500  25.153  1.00 25.02 ? 62   ARG A C   1 
ATOM   433  O O   . ARG A 1 62  ? -1.174  11.948  25.514  1.00 26.03 ? 62   ARG A O   1 
ATOM   434  C CB  . ARG A 1 62  ? -4.405  11.902  26.198  1.00 25.07 ? 62   ARG A CB  1 
ATOM   435  C CG  . ARG A 1 62  ? -3.788  11.333  27.510  1.00 25.97 ? 62   ARG A CG  1 
ATOM   436  C CD  . ARG A 1 62  ? -4.449  11.888  28.750  1.00 26.92 ? 62   ARG A CD  1 
ATOM   437  N NE  . ARG A 1 62  ? -3.906  11.384  30.027  1.00 28.76 ? 62   ARG A NE  1 
ATOM   438  C CZ  . ARG A 1 62  ? -2.693  11.656  30.531  1.00 30.35 ? 62   ARG A CZ  1 
ATOM   439  N NH1 . ARG A 1 62  ? -1.795  12.371  29.859  1.00 31.54 ? 62   ARG A NH1 1 
ATOM   440  N NH2 . ARG A 1 62  ? -2.352  11.186  31.724  1.00 30.17 ? 62   ARG A NH2 1 
ATOM   441  N N   . TYR A 1 63  ? -2.247  13.790  24.906  1.00 25.37 ? 63   TYR A N   1 
ATOM   442  C CA  . TYR A 1 63  ? -1.238  14.697  25.424  1.00 26.65 ? 63   TYR A CA  1 
ATOM   443  C C   . TYR A 1 63  ? -1.126  14.636  26.957  1.00 27.82 ? 63   TYR A C   1 
ATOM   444  O O   . TYR A 1 63  ? -2.100  14.244  27.641  1.00 27.64 ? 63   TYR A O   1 
ATOM   445  C CB  . TYR A 1 63  ? -1.585  16.111  25.018  1.00 26.34 ? 63   TYR A CB  1 
ATOM   446  C CG  . TYR A 1 63  ? -1.480  16.326  23.534  1.00 25.65 ? 63   TYR A CG  1 
ATOM   447  C CD1 . TYR A 1 63  ? -0.276  16.050  22.854  1.00 23.10 ? 63   TYR A CD1 1 
ATOM   448  C CD2 . TYR A 1 63  ? -2.577  16.789  22.800  1.00 24.95 ? 63   TYR A CD2 1 
ATOM   449  C CE1 . TYR A 1 63  ? -0.167  16.247  21.470  1.00 23.95 ? 63   TYR A CE1 1 
ATOM   450  C CE2 . TYR A 1 63  ? -2.484  16.979  21.402  1.00 26.17 ? 63   TYR A CE2 1 
ATOM   451  C CZ  . TYR A 1 63  ? -1.276  16.720  20.761  1.00 27.21 ? 63   TYR A CZ  1 
ATOM   452  O OH  . TYR A 1 63  ? -1.183  16.911  19.401  1.00 32.13 ? 63   TYR A OH  1 
ATOM   453  N N   . PRO A 1 64  ? 0.058   15.009  27.501  1.00 28.49 ? 64   PRO A N   1 
ATOM   454  C CA  . PRO A 1 64  ? 0.240   15.068  28.957  1.00 29.49 ? 64   PRO A CA  1 
ATOM   455  C C   . PRO A 1 64  ? -0.755  16.031  29.625  1.00 30.33 ? 64   PRO A C   1 
ATOM   456  O O   . PRO A 1 64  ? -1.202  16.992  29.008  1.00 30.18 ? 64   PRO A O   1 
ATOM   457  C CB  . PRO A 1 64  ? 1.679   15.577  29.113  1.00 29.42 ? 64   PRO A CB  1 
ATOM   458  C CG  . PRO A 1 64  ? 2.366   15.275  27.803  1.00 28.76 ? 64   PRO A CG  1 
ATOM   459  C CD  . PRO A 1 64  ? 1.283   15.397  26.770  1.00 28.52 ? 64   PRO A CD  1 
ATOM   460  N N   . THR A 1 65  ? -1.118  15.794  30.872  1.00 31.99 ? 65   THR A N   1 
ATOM   461  C CA  . THR A 1 65  ? -2.029  16.745  31.492  1.00 34.35 ? 65   THR A CA  1 
ATOM   462  C C   . THR A 1 65  ? -1.314  18.098  31.648  1.00 35.96 ? 65   THR A C   1 
ATOM   463  O O   . THR A 1 65  ? -0.070  18.169  31.550  1.00 36.58 ? 65   THR A O   1 
ATOM   464  C CB  . THR A 1 65  ? -2.556  16.303  32.850  1.00 34.32 ? 65   THR A CB  1 
ATOM   465  O OG1 . THR A 1 65  ? -1.627  16.703  33.856  1.00 36.56 ? 65   THR A OG1 1 
ATOM   466  C CG2 . THR A 1 65  ? -2.810  14.786  32.923  1.00 34.52 ? 65   THR A CG2 1 
ATOM   467  N N   . ASP A 1 66  ? -2.084  19.168  31.876  1.00 37.34 ? 66   ASP A N   1 
ATOM   468  C CA  . ASP A 1 66  ? -1.496  20.504  31.980  1.00 38.90 ? 66   ASP A CA  1 
ATOM   469  C C   . ASP A 1 66  ? -0.413  20.569  33.073  1.00 39.16 ? 66   ASP A C   1 
ATOM   470  O O   . ASP A 1 66  ? 0.721   20.981  32.830  1.00 39.34 ? 66   ASP A O   1 
ATOM   471  C CB  . ASP A 1 66  ? -2.575  21.545  32.218  1.00 39.38 ? 66   ASP A CB  1 
ATOM   472  C CG  . ASP A 1 66  ? -2.094  22.962  31.928  1.00 41.10 ? 66   ASP A CG  1 
ATOM   473  O OD1 . ASP A 1 66  ? -1.639  23.218  30.778  1.00 44.05 ? 66   ASP A OD1 1 
ATOM   474  O OD2 . ASP A 1 66  ? -2.184  23.807  32.858  1.00 41.04 ? 66   ASP A OD2 1 
ATOM   475  N N   . SER A 1 67  ? -0.777  20.111  34.260  1.00 40.09 ? 67   SER A N   1 
ATOM   476  C CA  . SER A 1 67  ? 0.156   19.866  35.348  1.00 40.77 ? 67   SER A CA  1 
ATOM   477  C C   . SER A 1 67  ? 1.501   19.304  34.868  1.00 41.21 ? 67   SER A C   1 
ATOM   478  O O   . SER A 1 67  ? 2.521   19.998  34.878  1.00 41.10 ? 67   SER A O   1 
ATOM   479  C CB  . SER A 1 67  ? -0.480  18.865  36.296  1.00 41.08 ? 67   SER A CB  1 
ATOM   480  O OG  . SER A 1 67  ? -0.243  19.242  37.632  1.00 42.40 ? 67   SER A OG  1 
ATOM   481  N N   . LYS A 1 68  ? 1.476   18.049  34.425  1.00 41.36 ? 68   LYS A N   1 
ATOM   482  C CA  . LYS A 1 68  ? 2.688   17.301  34.081  1.00 41.17 ? 68   LYS A CA  1 
ATOM   483  C C   . LYS A 1 68  ? 3.515   17.940  32.990  1.00 41.21 ? 68   LYS A C   1 
ATOM   484  O O   . LYS A 1 68  ? 4.747   17.921  33.051  1.00 40.84 ? 68   LYS A O   1 
ATOM   485  C CB  . LYS A 1 68  ? 2.346   15.866  33.689  1.00 41.22 ? 68   LYS A CB  1 
ATOM   486  C CG  . LYS A 1 68  ? 1.668   15.060  34.792  1.00 40.61 ? 68   LYS A CG  1 
ATOM   487  C CD  . LYS A 1 68  ? 2.689   14.462  35.703  1.00 41.42 ? 68   LYS A CD  1 
ATOM   488  C CE  . LYS A 1 68  ? 2.183   13.201  36.347  1.00 41.27 ? 68   LYS A CE  1 
ATOM   489  N NZ  . LYS A 1 68  ? 3.397   12.366  36.485  1.00 44.00 ? 68   LYS A NZ  1 
ATOM   490  N N   . GLY A 1 69  ? 2.839   18.510  31.997  1.00 41.68 ? 69   GLY A N   1 
ATOM   491  C CA  . GLY A 1 69  ? 3.524   19.146  30.874  1.00 41.72 ? 69   GLY A CA  1 
ATOM   492  C C   . GLY A 1 69  ? 4.298   20.386  31.296  1.00 42.10 ? 69   GLY A C   1 
ATOM   493  O O   . GLY A 1 69  ? 5.388   20.651  30.772  1.00 41.34 ? 69   GLY A O   1 
ATOM   494  N N   . LYS A 1 70  ? 3.710   21.158  32.222  1.00 42.73 ? 70   LYS A N   1 
ATOM   495  C CA  . LYS A 1 70  ? 4.391   22.302  32.833  1.00 43.25 ? 70   LYS A CA  1 
ATOM   496  C C   . LYS A 1 70  ? 5.732   21.754  33.285  1.00 43.17 ? 70   LYS A C   1 
ATOM   497  O O   . LYS A 1 70  ? 6.788   22.148  32.783  1.00 43.48 ? 70   LYS A O   1 
ATOM   498  C CB  . LYS A 1 70  ? 3.651   22.808  34.079  1.00 43.61 ? 70   LYS A CB  1 
ATOM   499  C CG  . LYS A 1 70  ? 2.193   23.254  33.891  1.00 44.69 ? 70   LYS A CG  1 
ATOM   500  C CD  . LYS A 1 70  ? 2.079   24.747  33.684  1.00 45.63 ? 70   LYS A CD  1 
ATOM   501  C CE  . LYS A 1 70  ? 0.676   25.158  33.313  1.00 44.15 ? 70   LYS A CE  1 
ATOM   502  N NZ  . LYS A 1 70  ? 0.709   26.501  32.662  1.00 45.40 ? 70   LYS A NZ  1 
ATOM   503  N N   . LYS A 1 71  ? 5.669   20.797  34.205  1.00 42.42 ? 71   LYS A N   1 
ATOM   504  C CA  . LYS A 1 71  ? 6.859   20.200  34.786  1.00 41.58 ? 71   LYS A CA  1 
ATOM   505  C C   . LYS A 1 71  ? 7.840   19.678  33.742  1.00 41.04 ? 71   LYS A C   1 
ATOM   506  O O   . LYS A 1 71  ? 9.008   20.049  33.782  1.00 41.48 ? 71   LYS A O   1 
ATOM   507  C CB  . LYS A 1 71  ? 6.461   19.158  35.825  1.00 41.28 ? 71   LYS A CB  1 
ATOM   508  C CG  . LYS A 1 71  ? 5.611   19.791  36.912  1.00 40.91 ? 71   LYS A CG  1 
ATOM   509  C CD  . LYS A 1 71  ? 4.955   18.810  37.860  1.00 41.54 ? 71   LYS A CD  1 
ATOM   510  C CE  . LYS A 1 71  ? 3.871   19.550  38.675  1.00 42.86 ? 71   LYS A CE  1 
ATOM   511  N NZ  . LYS A 1 71  ? 3.330   18.727  39.796  1.00 43.45 ? 71   LYS A NZ  1 
ATOM   512  N N   . TYR A 1 72  ? 7.364   18.888  32.780  1.00 40.38 ? 72   TYR A N   1 
ATOM   513  C CA  . TYR A 1 72  ? 8.240   18.358  31.731  1.00 39.48 ? 72   TYR A CA  1 
ATOM   514  C C   . TYR A 1 72  ? 8.969   19.501  31.049  1.00 39.06 ? 72   TYR A C   1 
ATOM   515  O O   . TYR A 1 72  ? 10.196  19.489  30.933  1.00 38.08 ? 72   TYR A O   1 
ATOM   516  C CB  . TYR A 1 72  ? 7.475   17.545  30.653  1.00 39.54 ? 72   TYR A CB  1 
ATOM   517  C CG  . TYR A 1 72  ? 6.747   16.285  31.094  1.00 37.97 ? 72   TYR A CG  1 
ATOM   518  C CD1 . TYR A 1 72  ? 7.187   15.534  32.154  1.00 37.67 ? 72   TYR A CD1 1 
ATOM   519  C CD2 . TYR A 1 72  ? 5.636   15.827  30.401  1.00 37.29 ? 72   TYR A CD2 1 
ATOM   520  C CE1 . TYR A 1 72  ? 6.515   14.369  32.543  1.00 36.82 ? 72   TYR A CE1 1 
ATOM   521  C CE2 . TYR A 1 72  ? 4.967   14.687  30.784  1.00 35.24 ? 72   TYR A CE2 1 
ATOM   522  C CZ  . TYR A 1 72  ? 5.421   13.953  31.856  1.00 34.84 ? 72   TYR A CZ  1 
ATOM   523  O OH  . TYR A 1 72  ? 4.793   12.797  32.253  1.00 32.61 ? 72   TYR A OH  1 
ATOM   524  N N   . SER A 1 73  ? 8.186   20.480  30.599  1.00 39.24 ? 73   SER A N   1 
ATOM   525  C CA  . SER A 1 73  ? 8.705   21.667  29.937  1.00 39.45 ? 73   SER A CA  1 
ATOM   526  C C   . SER A 1 73  ? 9.718   22.404  30.840  1.00 39.14 ? 73   SER A C   1 
ATOM   527  O O   . SER A 1 73  ? 10.843  22.717  30.413  1.00 38.55 ? 73   SER A O   1 
ATOM   528  C CB  . SER A 1 73  ? 7.550   22.577  29.527  1.00 39.77 ? 73   SER A CB  1 
ATOM   529  O OG  . SER A 1 73  ? 8.006   23.767  28.867  1.00 42.02 ? 73   SER A OG  1 
ATOM   530  N N   . ALA A 1 74  ? 9.326   22.645  32.087  1.00 38.84 ? 74   ALA A N   1 
ATOM   531  C CA  . ALA A 1 74  ? 10.226  23.231  33.086  1.00 39.25 ? 74   ALA A CA  1 
ATOM   532  C C   . ALA A 1 74  ? 11.509  22.431  33.251  1.00 39.28 ? 74   ALA A C   1 
ATOM   533  O O   . ALA A 1 74  ? 12.597  23.002  33.244  1.00 39.88 ? 74   ALA A O   1 
ATOM   534  C CB  . ALA A 1 74  ? 9.527   23.390  34.438  1.00 38.81 ? 74   ALA A CB  1 
ATOM   535  N N   . LEU A 1 75  ? 11.382  21.115  33.400  1.00 39.06 ? 75   LEU A N   1 
ATOM   536  C CA  . LEU A 1 75  ? 12.541  20.270  33.609  1.00 39.09 ? 75   LEU A CA  1 
ATOM   537  C C   . LEU A 1 75  ? 13.524  20.397  32.449  1.00 39.58 ? 75   LEU A C   1 
ATOM   538  O O   . LEU A 1 75  ? 14.729  20.553  32.665  1.00 39.49 ? 75   LEU A O   1 
ATOM   539  C CB  . LEU A 1 75  ? 12.132  18.805  33.858  1.00 38.54 ? 75   LEU A CB  1 
ATOM   540  C CG  . LEU A 1 75  ? 13.229  17.725  33.925  1.00 38.60 ? 75   LEU A CG  1 
ATOM   541  C CD1 . LEU A 1 75  ? 14.290  18.074  34.965  1.00 37.92 ? 75   LEU A CD1 1 
ATOM   542  C CD2 . LEU A 1 75  ? 12.695  16.339  34.215  1.00 37.87 ? 75   LEU A CD2 1 
ATOM   543  N N   . ILE A 1 76  ? 13.018  20.337  31.221  1.00 40.41 ? 76   ILE A N   1 
ATOM   544  C CA  . ILE A 1 76  ? 13.903  20.381  30.044  1.00 41.16 ? 76   ILE A CA  1 
ATOM   545  C C   . ILE A 1 76  ? 14.577  21.750  29.851  1.00 41.50 ? 76   ILE A C   1 
ATOM   546  O O   . ILE A 1 76  ? 15.667  21.820  29.294  1.00 41.37 ? 76   ILE A O   1 
ATOM   547  C CB  . ILE A 1 76  ? 13.212  19.891  28.750  1.00 40.75 ? 76   ILE A CB  1 
ATOM   548  C CG1 . ILE A 1 76  ? 12.637  18.490  28.954  1.00 41.17 ? 76   ILE A CG1 1 
ATOM   549  C CG2 . ILE A 1 76  ? 14.207  19.826  27.612  1.00 41.00 ? 76   ILE A CG2 1 
ATOM   550  C CD1 . ILE A 1 76  ? 11.281  18.266  28.246  1.00 42.21 ? 76   ILE A CD1 1 
ATOM   551  N N   . GLU A 1 77  ? 13.946  22.823  30.324  1.00 41.97 ? 77   GLU A N   1 
ATOM   552  C CA  . GLU A 1 77  ? 14.595  24.132  30.298  1.00 43.43 ? 77   GLU A CA  1 
ATOM   553  C C   . GLU A 1 77  ? 15.810  24.114  31.243  1.00 43.78 ? 77   GLU A C   1 
ATOM   554  O O   . GLU A 1 77  ? 16.936  24.446  30.835  1.00 43.74 ? 77   GLU A O   1 
ATOM   555  C CB  . GLU A 1 77  ? 13.620  25.257  30.666  1.00 43.79 ? 77   GLU A CB  1 
ATOM   556  C CG  . GLU A 1 77  ? 12.463  25.421  29.659  1.00 46.44 ? 77   GLU A CG  1 
ATOM   557  C CD  . GLU A 1 77  ? 12.037  26.879  29.459  1.00 51.19 ? 77   GLU A CD  1 
ATOM   558  O OE1 . GLU A 1 77  ? 11.729  27.571  30.467  1.00 52.01 ? 77   GLU A OE1 1 
ATOM   559  O OE2 . GLU A 1 77  ? 12.023  27.339  28.283  1.00 52.31 ? 77   GLU A OE2 1 
ATOM   560  N N   . GLU A 1 78  ? 15.571  23.681  32.486  1.00 43.91 ? 78   GLU A N   1 
ATOM   561  C CA  . GLU A 1 78  ? 16.613  23.529  33.505  1.00 44.14 ? 78   GLU A CA  1 
ATOM   562  C C   . GLU A 1 78  ? 17.751  22.632  33.078  1.00 43.74 ? 78   GLU A C   1 
ATOM   563  O O   . GLU A 1 78  ? 18.911  22.911  33.379  1.00 43.43 ? 78   GLU A O   1 
ATOM   564  C CB  . GLU A 1 78  ? 16.021  23.003  34.809  1.00 44.36 ? 78   GLU A CB  1 
ATOM   565  C CG  . GLU A 1 78  ? 15.280  24.055  35.594  1.00 46.64 ? 78   GLU A CG  1 
ATOM   566  C CD  . GLU A 1 78  ? 14.756  23.567  36.939  1.00 50.58 ? 78   GLU A CD  1 
ATOM   567  O OE1 . GLU A 1 78  ? 13.707  24.112  37.350  1.00 53.98 ? 78   GLU A OE1 1 
ATOM   568  O OE2 . GLU A 1 78  ? 15.363  22.675  37.592  1.00 50.81 ? 78   GLU A OE2 1 
ATOM   569  N N   . ILE A 1 79  ? 17.421  21.556  32.378  1.00 43.50 ? 79   ILE A N   1 
ATOM   570  C CA  . ILE A 1 79  ? 18.452  20.710  31.811  1.00 43.78 ? 79   ILE A CA  1 
ATOM   571  C C   . ILE A 1 79  ? 19.288  21.499  30.780  1.00 44.28 ? 79   ILE A C   1 
ATOM   572  O O   . ILE A 1 79  ? 20.504  21.377  30.747  1.00 43.76 ? 79   ILE A O   1 
ATOM   573  C CB  . ILE A 1 79  ? 17.861  19.398  31.254  1.00 43.52 ? 79   ILE A CB  1 
ATOM   574  C CG1 . ILE A 1 79  ? 17.377  18.546  32.415  1.00 42.27 ? 79   ILE A CG1 1 
ATOM   575  C CG2 . ILE A 1 79  ? 18.891  18.625  30.444  1.00 42.79 ? 79   ILE A CG2 1 
ATOM   576  C CD1 . ILE A 1 79  ? 16.457  17.464  32.003  1.00 41.00 ? 79   ILE A CD1 1 
ATOM   577  N N   . GLN A 1 80  ? 18.626  22.332  29.981  1.00 45.31 ? 80   GLN A N   1 
ATOM   578  C CA  . GLN A 1 80  ? 19.308  23.139  28.958  1.00 46.49 ? 80   GLN A CA  1 
ATOM   579  C C   . GLN A 1 80  ? 20.078  24.341  29.523  1.00 46.64 ? 80   GLN A C   1 
ATOM   580  O O   . GLN A 1 80  ? 21.083  24.751  28.956  1.00 46.11 ? 80   GLN A O   1 
ATOM   581  C CB  . GLN A 1 80  ? 18.315  23.583  27.881  1.00 46.56 ? 80   GLN A CB  1 
ATOM   582  C CG  . GLN A 1 80  ? 17.880  22.426  26.993  1.00 47.76 ? 80   GLN A CG  1 
ATOM   583  C CD  . GLN A 1 80  ? 16.699  22.744  26.076  1.00 49.01 ? 80   GLN A CD  1 
ATOM   584  O OE1 . GLN A 1 80  ? 15.983  23.746  26.246  1.00 48.21 ? 80   GLN A OE1 1 
ATOM   585  N NE2 . GLN A 1 80  ? 16.492  21.872  25.091  1.00 48.73 ? 80   GLN A NE2 1 
ATOM   586  N N   . GLN A 1 81  ? 19.602  24.894  30.637  1.00 47.34 ? 81   GLN A N   1 
ATOM   587  C CA  . GLN A 1 81  ? 20.295  25.998  31.290  1.00 48.09 ? 81   GLN A CA  1 
ATOM   588  C C   . GLN A 1 81  ? 21.579  25.579  31.995  1.00 47.95 ? 81   GLN A C   1 
ATOM   589  O O   . GLN A 1 81  ? 22.531  26.355  32.033  1.00 48.21 ? 81   GLN A O   1 
ATOM   590  C CB  . GLN A 1 81  ? 19.387  26.689  32.290  1.00 48.33 ? 81   GLN A CB  1 
ATOM   591  C CG  . GLN A 1 81  ? 18.567  27.812  31.710  1.00 50.95 ? 81   GLN A CG  1 
ATOM   592  C CD  . GLN A 1 81  ? 17.441  28.203  32.640  1.00 55.24 ? 81   GLN A CD  1 
ATOM   593  O OE1 . GLN A 1 81  ? 17.578  28.136  33.866  1.00 56.03 ? 81   GLN A OE1 1 
ATOM   594  N NE2 . GLN A 1 81  ? 16.306  28.610  32.066  1.00 57.09 ? 81   GLN A NE2 1 
ATOM   595  N N   . ASN A 1 82  ? 21.611  24.363  32.539  1.00 47.68 ? 82   ASN A N   1 
ATOM   596  C CA  . ASN A 1 82  ? 22.674  23.964  33.463  1.00 47.37 ? 82   ASN A CA  1 
ATOM   597  C C   . ASN A 1 82  ? 23.795  23.107  32.848  1.00 48.04 ? 82   ASN A C   1 
ATOM   598  O O   . ASN A 1 82  ? 24.961  23.270  33.205  1.00 48.30 ? 82   ASN A O   1 
ATOM   599  C CB  . ASN A 1 82  ? 22.107  23.240  34.704  1.00 47.05 ? 82   ASN A CB  1 
ATOM   600  C CG  . ASN A 1 82  ? 21.164  24.105  35.576  1.00 44.77 ? 82   ASN A CG  1 
ATOM   601  O OD1 . ASN A 1 82  ? 20.853  25.260  35.276  1.00 42.67 ? 82   ASN A OD1 1 
ATOM   602  N ND2 . ASN A 1 82  ? 20.712  23.494  36.683  1.00 43.65 ? 82   ASN A ND2 1 
ATOM   603  N N   . ALA A 1 83  ? 23.459  22.198  31.938  1.00 48.53 ? 83   ALA A N   1 
ATOM   604  C CA  . ALA A 1 83  ? 24.444  21.210  31.462  1.00 49.30 ? 83   ALA A CA  1 
ATOM   605  C C   . ALA A 1 83  ? 25.482  21.756  30.470  1.00 50.05 ? 83   ALA A C   1 
ATOM   606  O O   . ALA A 1 83  ? 25.200  22.668  29.695  1.00 49.78 ? 83   ALA A O   1 
ATOM   607  C CB  . ALA A 1 83  ? 23.746  19.992  30.876  1.00 48.91 ? 83   ALA A CB  1 
ATOM   608  N N   . THR A 1 84  ? 26.675  21.165  30.484  1.00 51.28 ? 84   THR A N   1 
ATOM   609  C CA  . THR A 1 84  ? 27.796  21.662  29.671  1.00 52.63 ? 84   THR A CA  1 
ATOM   610  C C   . THR A 1 84  ? 28.183  20.698  28.550  1.00 53.28 ? 84   THR A C   1 
ATOM   611  O O   . THR A 1 84  ? 28.896  21.075  27.622  1.00 53.77 ? 84   THR A O   1 
ATOM   612  C CB  . THR A 1 84  ? 29.049  21.973  30.532  1.00 52.73 ? 84   THR A CB  1 
ATOM   613  O OG1 . THR A 1 84  ? 29.561  20.747  31.088  1.00 52.72 ? 84   THR A OG1 1 
ATOM   614  C CG2 . THR A 1 84  ? 28.717  22.999  31.669  1.00 52.42 ? 84   THR A CG2 1 
ATOM   615  N N   . THR A 1 85  ? 27.738  19.449  28.648  1.00 53.98 ? 85   THR A N   1 
ATOM   616  C CA  . THR A 1 85  ? 27.933  18.486  27.555  1.00 54.66 ? 85   THR A CA  1 
ATOM   617  C C   . THR A 1 85  ? 26.656  17.724  27.159  1.00 54.43 ? 85   THR A C   1 
ATOM   618  O O   . THR A 1 85  ? 26.250  16.759  27.832  1.00 54.58 ? 85   THR A O   1 
ATOM   619  C CB  . THR A 1 85  ? 29.112  17.472  27.810  1.00 54.88 ? 85   THR A CB  1 
ATOM   620  O OG1 . THR A 1 85  ? 28.976  16.857  29.102  1.00 55.48 ? 85   THR A OG1 1 
ATOM   621  C CG2 . THR A 1 85  ? 30.484  18.161  27.686  1.00 55.44 ? 85   THR A CG2 1 
ATOM   622  N N   . PHE A 1 86  ? 26.036  18.154  26.065  1.00 53.83 ? 86   PHE A N   1 
ATOM   623  C CA  . PHE A 1 86  ? 25.020  17.338  25.421  1.00 53.60 ? 86   PHE A CA  1 
ATOM   624  C C   . PHE A 1 86  ? 25.661  16.653  24.234  1.00 53.18 ? 86   PHE A C   1 
ATOM   625  O O   . PHE A 1 86  ? 25.628  17.185  23.124  1.00 53.18 ? 86   PHE A O   1 
ATOM   626  C CB  . PHE A 1 86  ? 23.845  18.178  24.906  1.00 53.75 ? 86   PHE A CB  1 
ATOM   627  C CG  . PHE A 1 86  ? 23.322  19.189  25.886  1.00 53.60 ? 86   PHE A CG  1 
ATOM   628  C CD1 . PHE A 1 86  ? 22.271  18.868  26.737  1.00 52.81 ? 86   PHE A CD1 1 
ATOM   629  C CD2 . PHE A 1 86  ? 23.854  20.478  25.925  1.00 54.28 ? 86   PHE A CD2 1 
ATOM   630  C CE1 . PHE A 1 86  ? 21.769  19.805  27.627  1.00 53.32 ? 86   PHE A CE1 1 
ATOM   631  C CE2 . PHE A 1 86  ? 23.358  21.430  26.811  1.00 54.72 ? 86   PHE A CE2 1 
ATOM   632  C CZ  . PHE A 1 86  ? 22.302  21.094  27.664  1.00 54.24 ? 86   PHE A CZ  1 
ATOM   633  N N   . ASP A 1 87  ? 26.276  15.499  24.454  1.00 52.81 ? 87   ASP A N   1 
ATOM   634  C CA  . ASP A 1 87  ? 26.785  14.739  23.315  1.00 52.94 ? 87   ASP A CA  1 
ATOM   635  C C   . ASP A 1 87  ? 26.524  13.239  23.430  1.00 52.53 ? 87   ASP A C   1 
ATOM   636  O O   . ASP A 1 87  ? 25.938  12.781  24.420  1.00 52.87 ? 87   ASP A O   1 
ATOM   637  C CB  . ASP A 1 87  ? 28.246  15.098  22.976  1.00 53.42 ? 87   ASP A CB  1 
ATOM   638  C CG  . ASP A 1 87  ? 29.218  14.809  24.118  1.00 54.60 ? 87   ASP A CG  1 
ATOM   639  O OD1 . ASP A 1 87  ? 29.246  13.650  24.599  1.00 54.80 ? 87   ASP A OD1 1 
ATOM   640  O OD2 . ASP A 1 87  ? 29.969  15.740  24.514  1.00 55.84 ? 87   ASP A OD2 1 
ATOM   641  N N   . GLY A 1 88  ? 26.940  12.480  22.414  1.00 51.98 ? 88   GLY A N   1 
ATOM   642  C CA  . GLY A 1 88  ? 26.465  11.100  22.228  1.00 50.83 ? 88   GLY A CA  1 
ATOM   643  C C   . GLY A 1 88  ? 24.942  11.132  22.117  1.00 50.12 ? 88   GLY A C   1 
ATOM   644  O O   . GLY A 1 88  ? 24.372  12.026  21.462  1.00 49.74 ? 88   GLY A O   1 
ATOM   645  N N   . LYS A 1 89  ? 24.282  10.194  22.802  1.00 49.32 ? 89   LYS A N   1 
ATOM   646  C CA  . LYS A 1 89  ? 22.818  10.102  22.807  1.00 47.96 ? 89   LYS A CA  1 
ATOM   647  C C   . LYS A 1 89  ? 22.125  11.292  23.459  1.00 47.09 ? 89   LYS A C   1 
ATOM   648  O O   . LYS A 1 89  ? 20.908  11.389  23.436  1.00 47.05 ? 89   LYS A O   1 
ATOM   649  C CB  . LYS A 1 89  ? 22.364  8.786   23.451  1.00 48.48 ? 89   LYS A CB  1 
ATOM   650  C CG  . LYS A 1 89  ? 22.959  8.452   24.843  1.00 48.99 ? 89   LYS A CG  1 
ATOM   651  C CD  . LYS A 1 89  ? 22.927  6.926   25.058  1.00 51.14 ? 89   LYS A CD  1 
ATOM   652  C CE  . LYS A 1 89  ? 23.250  6.512   26.508  1.00 53.02 ? 89   LYS A CE  1 
ATOM   653  N NZ  . LYS A 1 89  ? 23.031  5.044   26.742  1.00 51.29 ? 89   LYS A NZ  1 
ATOM   654  N N   . TYR A 1 90  ? 22.901  12.211  24.019  1.00 46.03 ? 90   TYR A N   1 
ATOM   655  C CA  . TYR A 1 90  ? 22.334  13.367  24.703  1.00 45.04 ? 90   TYR A CA  1 
ATOM   656  C C   . TYR A 1 90  ? 22.166  14.585  23.817  1.00 44.81 ? 90   TYR A C   1 
ATOM   657  O O   . TYR A 1 90  ? 21.451  15.515  24.186  1.00 44.84 ? 90   TYR A O   1 
ATOM   658  C CB  . TYR A 1 90  ? 23.159  13.737  25.957  1.00 44.66 ? 90   TYR A CB  1 
ATOM   659  C CG  . TYR A 1 90  ? 23.111  12.683  27.023  1.00 42.75 ? 90   TYR A CG  1 
ATOM   660  C CD1 . TYR A 1 90  ? 22.067  12.644  27.936  1.00 41.83 ? 90   TYR A CD1 1 
ATOM   661  C CD2 . TYR A 1 90  ? 24.094  11.704  27.101  1.00 41.64 ? 90   TYR A CD2 1 
ATOM   662  C CE1 . TYR A 1 90  ? 22.010  11.657  28.930  1.00 41.19 ? 90   TYR A CE1 1 
ATOM   663  C CE2 . TYR A 1 90  ? 24.055  10.717  28.081  1.00 41.01 ? 90   TYR A CE2 1 
ATOM   664  C CZ  . TYR A 1 90  ? 23.005  10.695  28.998  1.00 41.00 ? 90   TYR A CZ  1 
ATOM   665  O OH  . TYR A 1 90  ? 22.956  9.715   29.972  1.00 39.02 ? 90   TYR A OH  1 
ATOM   666  N N   . ALA A 1 91  ? 22.809  14.579  22.656  1.00 44.80 ? 91   ALA A N   1 
ATOM   667  C CA  . ALA A 1 91  ? 22.891  15.780  21.812  1.00 45.06 ? 91   ALA A CA  1 
ATOM   668  C C   . ALA A 1 91  ? 21.549  16.490  21.603  1.00 45.06 ? 91   ALA A C   1 
ATOM   669  O O   . ALA A 1 91  ? 21.439  17.724  21.737  1.00 44.68 ? 91   ALA A O   1 
ATOM   670  C CB  . ALA A 1 91  ? 23.563  15.452  20.479  1.00 45.15 ? 91   ALA A CB  1 
ATOM   671  N N   . PHE A 1 92  ? 20.527  15.686  21.317  1.00 45.46 ? 92   PHE A N   1 
ATOM   672  C CA  . PHE A 1 92  ? 19.171  16.174  20.995  1.00 45.36 ? 92   PHE A CA  1 
ATOM   673  C C   . PHE A 1 92  ? 18.562  17.098  22.039  1.00 45.68 ? 92   PHE A C   1 
ATOM   674  O O   . PHE A 1 92  ? 17.729  17.966  21.720  1.00 45.37 ? 92   PHE A O   1 
ATOM   675  C CB  . PHE A 1 92  ? 18.228  14.985  20.747  1.00 45.59 ? 92   PHE A CB  1 
ATOM   676  C CG  . PHE A 1 92  ? 17.759  14.289  21.998  1.00 43.87 ? 92   PHE A CG  1 
ATOM   677  C CD1 . PHE A 1 92  ? 18.444  13.188  22.493  1.00 42.95 ? 92   PHE A CD1 1 
ATOM   678  C CD2 . PHE A 1 92  ? 16.602  14.711  22.650  1.00 43.58 ? 92   PHE A CD2 1 
ATOM   679  C CE1 . PHE A 1 92  ? 17.994  12.524  23.642  1.00 42.61 ? 92   PHE A CE1 1 
ATOM   680  C CE2 . PHE A 1 92  ? 16.151  14.067  23.800  1.00 43.07 ? 92   PHE A CE2 1 
ATOM   681  C CZ  . PHE A 1 92  ? 16.854  12.961  24.295  1.00 42.77 ? 92   PHE A CZ  1 
ATOM   682  N N   . LEU A 1 93  ? 18.969  16.897  23.291  1.00 46.01 ? 93   LEU A N   1 
ATOM   683  C CA  . LEU A 1 93  ? 18.433  17.681  24.389  1.00 46.52 ? 93   LEU A CA  1 
ATOM   684  C C   . LEU A 1 93  ? 18.850  19.128  24.331  1.00 47.18 ? 93   LEU A C   1 
ATOM   685  O O   . LEU A 1 93  ? 18.159  19.974  24.898  1.00 46.69 ? 93   LEU A O   1 
ATOM   686  C CB  . LEU A 1 93  ? 18.850  17.095  25.724  1.00 46.27 ? 93   LEU A CB  1 
ATOM   687  C CG  . LEU A 1 93  ? 17.928  16.042  26.305  1.00 45.74 ? 93   LEU A CG  1 
ATOM   688  C CD1 . LEU A 1 93  ? 18.653  15.421  27.479  1.00 45.39 ? 93   LEU A CD1 1 
ATOM   689  C CD2 . LEU A 1 93  ? 16.628  16.689  26.726  1.00 42.53 ? 93   LEU A CD2 1 
ATOM   690  N N   . LYS A 1 94  ? 19.977  19.410  23.662  1.00 48.34 ? 94   LYS A N   1 
ATOM   691  C CA  . LYS A 1 94  ? 20.481  20.781  23.594  1.00 49.62 ? 94   LYS A CA  1 
ATOM   692  C C   . LYS A 1 94  ? 19.390  21.711  23.061  1.00 50.06 ? 94   LYS A C   1 
ATOM   693  O O   . LYS A 1 94  ? 19.062  22.734  23.694  1.00 50.22 ? 94   LYS A O   1 
ATOM   694  C CB  . LYS A 1 94  ? 21.782  20.902  22.779  1.00 49.86 ? 94   LYS A CB  1 
ATOM   695  C CG  . LYS A 1 94  ? 22.337  22.341  22.795  1.00 51.46 ? 94   LYS A CG  1 
ATOM   696  C CD  . LYS A 1 94  ? 23.854  22.449  22.515  1.00 54.55 ? 94   LYS A CD  1 
ATOM   697  C CE  . LYS A 1 94  ? 24.265  23.940  22.381  1.00 55.51 ? 94   LYS A CE  1 
ATOM   698  N NZ  . LYS A 1 94  ? 25.670  24.235  22.819  1.00 56.86 ? 94   LYS A NZ  1 
ATOM   699  N N   . THR A 1 95  ? 18.803  21.311  21.931  1.00 50.37 ? 95   THR A N   1 
ATOM   700  C CA  . THR A 1 95  ? 17.861  22.148  21.178  1.00 50.69 ? 95   THR A CA  1 
ATOM   701  C C   . THR A 1 95  ? 16.399  21.765  21.369  1.00 50.43 ? 95   THR A C   1 
ATOM   702  O O   . THR A 1 95  ? 15.499  22.549  21.012  1.00 50.89 ? 95   THR A O   1 
ATOM   703  C CB  . THR A 1 95  ? 18.148  22.113  19.643  1.00 51.25 ? 95   THR A CB  1 
ATOM   704  O OG1 . THR A 1 95  ? 18.428  20.759  19.218  1.00 51.42 ? 95   THR A OG1 1 
ATOM   705  C CG2 . THR A 1 95  ? 19.308  23.055  19.279  1.00 50.78 ? 95   THR A CG2 1 
ATOM   706  N N   . TYR A 1 96  ? 16.155  20.572  21.914  1.00 49.54 ? 96   TYR A N   1 
ATOM   707  C CA  . TYR A 1 96  ? 14.783  20.087  22.053  1.00 48.42 ? 96   TYR A CA  1 
ATOM   708  C C   . TYR A 1 96  ? 13.802  21.185  22.481  1.00 48.28 ? 96   TYR A C   1 
ATOM   709  O O   . TYR A 1 96  ? 14.029  21.890  23.466  1.00 47.88 ? 96   TYR A O   1 
ATOM   710  C CB  . TYR A 1 96  ? 14.679  18.882  22.987  1.00 48.07 ? 96   TYR A CB  1 
ATOM   711  C CG  . TYR A 1 96  ? 13.288  18.301  22.980  1.00 45.91 ? 96   TYR A CG  1 
ATOM   712  C CD1 . TYR A 1 96  ? 12.942  17.320  22.072  1.00 44.41 ? 96   TYR A CD1 1 
ATOM   713  C CD2 . TYR A 1 96  ? 12.304  18.769  23.853  1.00 44.45 ? 96   TYR A CD2 1 
ATOM   714  C CE1 . TYR A 1 96  ? 11.668  16.796  22.050  1.00 43.19 ? 96   TYR A CE1 1 
ATOM   715  C CE2 . TYR A 1 96  ? 11.033  18.256  23.834  1.00 42.91 ? 96   TYR A CE2 1 
ATOM   716  C CZ  . TYR A 1 96  ? 10.721  17.272  22.932  1.00 42.95 ? 96   TYR A CZ  1 
ATOM   717  O OH  . TYR A 1 96  ? 9.453   16.740  22.908  1.00 43.93 ? 96   TYR A OH  1 
ATOM   718  N N   . ASN A 1 97  ? 12.719  21.302  21.708  1.00 48.26 ? 97   ASN A N   1 
ATOM   719  C CA  . ASN A 1 97  ? 11.785  22.431  21.772  1.00 48.08 ? 97   ASN A CA  1 
ATOM   720  C C   . ASN A 1 97  ? 10.373  21.938  22.046  1.00 47.29 ? 97   ASN A C   1 
ATOM   721  O O   . ASN A 1 97  ? 9.600   21.666  21.124  1.00 47.68 ? 97   ASN A O   1 
ATOM   722  C CB  . ASN A 1 97  ? 11.833  23.242  20.457  1.00 48.63 ? 97   ASN A CB  1 
ATOM   723  C CG  . ASN A 1 97  ? 11.032  24.544  20.521  1.00 49.29 ? 97   ASN A CG  1 
ATOM   724  O OD1 . ASN A 1 97  ? 10.526  24.949  21.574  1.00 49.69 ? 97   ASN A OD1 1 
ATOM   725  N ND2 . ASN A 1 97  ? 10.918  25.204  19.381  1.00 50.96 ? 97   ASN A ND2 1 
ATOM   726  N N   . TYR A 1 98  ? 10.055  21.832  23.329  1.00 46.20 ? 98   TYR A N   1 
ATOM   727  C CA  . TYR A 1 98  ? 8.816   21.222  23.797  1.00 45.04 ? 98   TYR A CA  1 
ATOM   728  C C   . TYR A 1 98  ? 7.593   21.945  23.224  1.00 44.69 ? 98   TYR A C   1 
ATOM   729  O O   . TYR A 1 98  ? 7.370   23.137  23.493  1.00 44.60 ? 98   TYR A O   1 
ATOM   730  C CB  . TYR A 1 98  ? 8.790   21.190  25.325  1.00 44.04 ? 98   TYR A CB  1 
ATOM   731  C CG  . TYR A 1 98  ? 7.641   20.432  25.936  1.00 42.89 ? 98   TYR A CG  1 
ATOM   732  C CD1 . TYR A 1 98  ? 6.401   21.058  26.162  1.00 43.30 ? 98   TYR A CD1 1 
ATOM   733  C CD2 . TYR A 1 98  ? 7.789   19.110  26.344  1.00 40.30 ? 98   TYR A CD2 1 
ATOM   734  C CE1 . TYR A 1 98  ? 5.341   20.378  26.756  1.00 40.88 ? 98   TYR A CE1 1 
ATOM   735  C CE2 . TYR A 1 98  ? 6.736   18.426  26.947  1.00 38.31 ? 98   TYR A CE2 1 
ATOM   736  C CZ  . TYR A 1 98  ? 5.514   19.059  27.139  1.00 39.08 ? 98   TYR A CZ  1 
ATOM   737  O OH  . TYR A 1 98  ? 4.457   18.395  27.722  1.00 38.22 ? 98   TYR A OH  1 
ATOM   738  N N   . SER A 1 99  ? 6.821   21.206  22.425  1.00 44.02 ? 99   SER A N   1 
ATOM   739  C CA  . SER A 1 99  ? 5.638   21.742  21.752  1.00 43.41 ? 99   SER A CA  1 
ATOM   740  C C   . SER A 1 99  ? 4.340   20.964  21.981  1.00 43.23 ? 99   SER A C   1 
ATOM   741  O O   . SER A 1 99  ? 3.263   21.484  21.651  1.00 43.70 ? 99   SER A O   1 
ATOM   742  C CB  . SER A 1 99  ? 5.889   21.912  20.260  1.00 43.12 ? 99   SER A CB  1 
ATOM   743  O OG  . SER A 1 99  ? 6.960   21.098  19.827  1.00 43.33 ? 99   SER A OG  1 
ATOM   744  N N   . LEU A 1 100 ? 4.435   19.752  22.553  1.00 41.81 ? 100  LEU A N   1 
ATOM   745  C CA  . LEU A 1 100 ? 3.262   18.912  22.887  1.00 40.39 ? 100  LEU A CA  1 
ATOM   746  C C   . LEU A 1 100 ? 1.994   19.647  23.380  1.00 39.78 ? 100  LEU A C   1 
ATOM   747  O O   . LEU A 1 100 ? 2.076   20.655  24.090  1.00 39.66 ? 100  LEU A O   1 
ATOM   748  C CB  . LEU A 1 100 ? 3.631   17.885  23.947  1.00 40.04 ? 100  LEU A CB  1 
ATOM   749  C CG  . LEU A 1 100 ? 4.860   17.008  23.769  1.00 39.80 ? 100  LEU A CG  1 
ATOM   750  C CD1 . LEU A 1 100 ? 4.901   15.948  24.874  1.00 38.17 ? 100  LEU A CD1 1 
ATOM   751  C CD2 . LEU A 1 100 ? 4.867   16.381  22.385  1.00 40.89 ? 100  LEU A CD2 1 
ATOM   752  N N   . GLY A 1 101 ? 0.827   19.103  23.025  1.00 38.46 ? 101  GLY A N   1 
ATOM   753  C CA  . GLY A 1 101 ? -0.443  19.635  23.456  1.00 37.35 ? 101  GLY A CA  1 
ATOM   754  C C   . GLY A 1 101 ? -0.732  19.237  24.883  1.00 36.79 ? 101  GLY A C   1 
ATOM   755  O O   . GLY A 1 101 ? 0.149   18.734  25.576  1.00 36.47 ? 101  GLY A O   1 
ATOM   756  N N   . ALA A 1 102 ? -1.977  19.424  25.317  1.00 36.09 ? 102  ALA A N   1 
ATOM   757  C CA  . ALA A 1 102 ? -2.333  19.208  26.714  1.00 36.12 ? 102  ALA A CA  1 
ATOM   758  C C   . ALA A 1 102 ? -3.756  18.716  26.953  1.00 36.12 ? 102  ALA A C   1 
ATOM   759  O O   . ALA A 1 102 ? -4.741  19.356  26.550  1.00 36.50 ? 102  ALA A O   1 
ATOM   760  C CB  . ALA A 1 102 ? -2.096  20.490  27.526  1.00 36.45 ? 102  ALA A CB  1 
ATOM   761  N N   . ASP A 1 103 ? -3.842  17.603  27.675  1.00 35.86 ? 103  ASP A N   1 
ATOM   762  C CA  . ASP A 1 103 ? -5.105  16.923  28.029  1.00 35.77 ? 103  ASP A CA  1 
ATOM   763  C C   . ASP A 1 103 ? -5.797  16.215  26.853  1.00 35.19 ? 103  ASP A C   1 
ATOM   764  O O   . ASP A 1 103 ? -6.389  15.146  27.036  1.00 35.65 ? 103  ASP A O   1 
ATOM   765  C CB  . ASP A 1 103 ? -6.093  17.880  28.718  1.00 36.31 ? 103  ASP A CB  1 
ATOM   766  C CG  . ASP A 1 103 ? -5.519  18.508  29.963  1.00 38.11 ? 103  ASP A CG  1 
ATOM   767  O OD1 . ASP A 1 103 ? -5.462  17.801  30.999  1.00 38.18 ? 103  ASP A OD1 1 
ATOM   768  O OD2 . ASP A 1 103 ? -5.127  19.699  29.892  1.00 38.07 ? 103  ASP A OD2 1 
ATOM   769  N N   . ASP A 1 104 ? -5.703  16.805  25.660  1.00 34.39 ? 104  ASP A N   1 
ATOM   770  C CA  . ASP A 1 104 ? -6.529  16.430  24.526  1.00 33.50 ? 104  ASP A CA  1 
ATOM   771  C C   . ASP A 1 104 ? -6.070  15.073  24.003  1.00 32.11 ? 104  ASP A C   1 
ATOM   772  O O   . ASP A 1 104 ? -4.988  14.620  24.327  1.00 31.94 ? 104  ASP A O   1 
ATOM   773  C CB  . ASP A 1 104 ? -6.510  17.532  23.432  1.00 34.31 ? 104  ASP A CB  1 
ATOM   774  C CG  . ASP A 1 104 ? -7.182  18.883  23.889  1.00 36.14 ? 104  ASP A CG  1 
ATOM   775  O OD1 . ASP A 1 104 ? -7.839  18.935  24.958  1.00 38.34 ? 104  ASP A OD1 1 
ATOM   776  O OD2 . ASP A 1 104 ? -7.057  19.903  23.162  1.00 36.35 ? 104  ASP A OD2 1 
ATOM   777  N N   . LEU A 1 105 ? -6.940  14.390  23.273  1.00 30.33 ? 105  LEU A N   1 
ATOM   778  C CA  . LEU A 1 105 ? -6.574  13.215  22.502  1.00 29.17 ? 105  LEU A CA  1 
ATOM   779  C C   . LEU A 1 105 ? -5.549  13.654  21.422  1.00 28.61 ? 105  LEU A C   1 
ATOM   780  O O   . LEU A 1 105 ? -5.603  14.792  20.943  1.00 29.51 ? 105  LEU A O   1 
ATOM   781  C CB  . LEU A 1 105 ? -7.865  12.723  21.836  1.00 29.06 ? 105  LEU A CB  1 
ATOM   782  C CG  . LEU A 1 105 ? -8.505  11.357  21.953  1.00 27.77 ? 105  LEU A CG  1 
ATOM   783  C CD1 . LEU A 1 105 ? -8.414  10.897  23.356  1.00 28.12 ? 105  LEU A CD1 1 
ATOM   784  C CD2 . LEU A 1 105 ? -9.966  11.424  21.501  1.00 26.86 ? 105  LEU A CD2 1 
ATOM   785  N N   . THR A 1 106 ? -4.616  12.794  21.040  1.00 27.55 ? 106  THR A N   1 
ATOM   786  C CA  . THR A 1 106 ? -3.705  13.112  19.917  1.00 27.03 ? 106  THR A CA  1 
ATOM   787  C C   . THR A 1 106 ? -4.208  12.523  18.574  1.00 27.37 ? 106  THR A C   1 
ATOM   788  O O   . THR A 1 106 ? -5.071  11.640  18.575  1.00 27.28 ? 106  THR A O   1 
ATOM   789  C CB  . THR A 1 106 ? -2.356  12.535  20.156  1.00 26.68 ? 106  THR A CB  1 
ATOM   790  O OG1 . THR A 1 106 ? -2.457  11.097  20.103  1.00 27.29 ? 106  THR A OG1 1 
ATOM   791  C CG2 . THR A 1 106 ? -1.809  13.009  21.510  1.00 25.47 ? 106  THR A CG2 1 
ATOM   792  N N   . PRO A 1 107 ? -3.684  13.006  17.421  1.00 27.61 ? 107  PRO A N   1 
ATOM   793  C CA  . PRO A 1 107 ? -4.210  12.404  16.186  1.00 27.13 ? 107  PRO A CA  1 
ATOM   794  C C   . PRO A 1 107 ? -4.154  10.899  16.280  1.00 26.47 ? 107  PRO A C   1 
ATOM   795  O O   . PRO A 1 107 ? -5.168  10.237  16.020  1.00 26.78 ? 107  PRO A O   1 
ATOM   796  C CB  . PRO A 1 107 ? -3.248  12.920  15.104  1.00 27.72 ? 107  PRO A CB  1 
ATOM   797  C CG  . PRO A 1 107 ? -2.861  14.306  15.609  1.00 28.29 ? 107  PRO A CG  1 
ATOM   798  C CD  . PRO A 1 107 ? -3.021  14.299  17.140  1.00 27.66 ? 107  PRO A CD  1 
ATOM   799  N N   . PHE A 1 108 ? -2.985  10.383  16.656  1.00 24.70 ? 108  PHE A N   1 
ATOM   800  C CA  . PHE A 1 108 ? -2.791  8.954   16.902  1.00 23.50 ? 108  PHE A CA  1 
ATOM   801  C C   . PHE A 1 108 ? -3.842  8.349   17.861  1.00 22.44 ? 108  PHE A C   1 
ATOM   802  O O   . PHE A 1 108 ? -4.472  7.351   17.552  1.00 21.78 ? 108  PHE A O   1 
ATOM   803  C CB  . PHE A 1 108 ? -1.377  8.713   17.450  1.00 23.19 ? 108  PHE A CB  1 
ATOM   804  C CG  . PHE A 1 108 ? -1.087  7.290   17.740  1.00 22.84 ? 108  PHE A CG  1 
ATOM   805  C CD1 . PHE A 1 108 ? -0.792  6.408   16.722  1.00 21.63 ? 108  PHE A CD1 1 
ATOM   806  C CD2 . PHE A 1 108 ? -1.120  6.819   19.044  1.00 24.24 ? 108  PHE A CD2 1 
ATOM   807  C CE1 . PHE A 1 108 ? -0.538  5.081   16.990  1.00 22.75 ? 108  PHE A CE1 1 
ATOM   808  C CE2 . PHE A 1 108 ? -0.878  5.483   19.325  1.00 25.42 ? 108  PHE A CE2 1 
ATOM   809  C CZ  . PHE A 1 108 ? -0.589  4.615   18.292  1.00 24.95 ? 108  PHE A CZ  1 
ATOM   810  N N   . GLY A 1 109 ? -4.005  8.946   19.037  1.00 22.10 ? 109  GLY A N   1 
ATOM   811  C CA  . GLY A 1 109 ? -5.050  8.517   19.960  1.00 21.77 ? 109  GLY A CA  1 
ATOM   812  C C   . GLY A 1 109 ? -6.431  8.446   19.332  1.00 20.74 ? 109  GLY A C   1 
ATOM   813  O O   . GLY A 1 109 ? -7.215  7.604   19.659  1.00 22.22 ? 109  GLY A O   1 
ATOM   814  N N   . GLU A 1 110 ? -6.718  9.354   18.430  1.00 20.55 ? 110  GLU A N   1 
ATOM   815  C CA  . GLU A 1 110 ? -7.991  9.433   17.730  1.00 19.90 ? 110  GLU A CA  1 
ATOM   816  C C   . GLU A 1 110 ? -8.133  8.216   16.837  1.00 18.77 ? 110  GLU A C   1 
ATOM   817  O O   . GLU A 1 110 ? -9.134  7.494   16.932  1.00 17.82 ? 110  GLU A O   1 
ATOM   818  C CB  . GLU A 1 110 ? -8.045  10.743  16.929  1.00 19.55 ? 110  GLU A CB  1 
ATOM   819  C CG  . GLU A 1 110 ? -8.240  11.972  17.826  1.00 22.93 ? 110  GLU A CG  1 
ATOM   820  C CD  . GLU A 1 110 ? -8.323  13.283  17.055  1.00 24.49 ? 110  GLU A CD  1 
ATOM   821  O OE1 . GLU A 1 110 ? -8.399  13.245  15.827  1.00 26.57 ? 110  GLU A OE1 1 
ATOM   822  O OE2 . GLU A 1 110 ? -8.285  14.364  17.661  1.00 27.55 ? 110  GLU A OE2 1 
ATOM   823  N N   . GLN A 1 111 ? -7.107  7.972   16.014  1.00 17.96 ? 111  GLN A N   1 
ATOM   824  C CA  . GLN A 1 111 ? -7.093  6.855   15.101  1.00 18.54 ? 111  GLN A CA  1 
ATOM   825  C C   . GLN A 1 111 ? -7.211  5.501   15.812  1.00 19.11 ? 111  GLN A C   1 
ATOM   826  O O   . GLN A 1 111 ? -7.839  4.590   15.283  1.00 19.13 ? 111  GLN A O   1 
ATOM   827  C CB  . GLN A 1 111 ? -5.844  6.871   14.213  1.00 19.05 ? 111  GLN A CB  1 
ATOM   828  C CG  . GLN A 1 111 ? -5.859  5.731   13.153  1.00 19.14 ? 111  GLN A CG  1 
ATOM   829  C CD  . GLN A 1 111 ? -6.965  5.981   12.129  1.00 21.03 ? 111  GLN A CD  1 
ATOM   830  O OE1 . GLN A 1 111 ? -7.077  7.093   11.654  1.00 22.02 ? 111  GLN A OE1 1 
ATOM   831  N NE2 . GLN A 1 111 ? -7.800  4.971   11.825  1.00 18.79 ? 111  GLN A NE2 1 
ATOM   832  N N   . GLU A 1 112 ? -6.593  5.377   16.989  1.00 19.38 ? 112  GLU A N   1 
ATOM   833  C CA  . GLU A 1 112 ? -6.738  4.180   17.835  1.00 20.84 ? 112  GLU A CA  1 
ATOM   834  C C   . GLU A 1 112 ? -8.208  3.836   18.090  1.00 20.81 ? 112  GLU A C   1 
ATOM   835  O O   . GLU A 1 112 ? -8.583  2.658   18.094  1.00 20.61 ? 112  GLU A O   1 
ATOM   836  C CB  . GLU A 1 112 ? -6.043  4.337   19.212  1.00 20.51 ? 112  GLU A CB  1 
ATOM   837  C CG  . GLU A 1 112 ? -4.561  3.893   19.274  1.00 22.27 ? 112  GLU A CG  1 
ATOM   838  C CD  . GLU A 1 112 ? -3.923  4.120   20.656  1.00 23.93 ? 112  GLU A CD  1 
ATOM   839  O OE1 . GLU A 1 112 ? -4.288  5.093   21.327  1.00 25.78 ? 112  GLU A OE1 1 
ATOM   840  O OE2 . GLU A 1 112 ? -3.074  3.321   21.092  1.00 22.87 ? 112  GLU A OE2 1 
ATOM   841  N N   . LEU A 1 113 ? -9.033  4.846   18.338  1.00 20.72 ? 113  LEU A N   1 
ATOM   842  C CA  . LEU A 1 113 ? -10.398 4.510   18.738  1.00 21.10 ? 113  LEU A CA  1 
ATOM   843  C C   . LEU A 1 113 ? -11.242 4.250   17.495  1.00 21.12 ? 113  LEU A C   1 
ATOM   844  O O   . LEU A 1 113 ? -12.240 3.535   17.584  1.00 21.16 ? 113  LEU A O   1 
ATOM   845  C CB  . LEU A 1 113 ? -11.007 5.585   19.645  1.00 20.78 ? 113  LEU A CB  1 
ATOM   846  C CG  . LEU A 1 113 ? -10.781 5.467   21.159  1.00 21.67 ? 113  LEU A CG  1 
ATOM   847  C CD1 . LEU A 1 113 ? -11.896 4.673   21.870  1.00 21.85 ? 113  LEU A CD1 1 
ATOM   848  C CD2 . LEU A 1 113 ? -9.412  4.931   21.502  1.00 20.34 ? 113  LEU A CD2 1 
ATOM   849  N N   . VAL A 1 114 ? -10.804 4.811   16.354  1.00 20.67 ? 114  VAL A N   1 
ATOM   850  C CA  . VAL A 1 114 ? -11.422 4.571   15.050  1.00 19.39 ? 114  VAL A CA  1 
ATOM   851  C C   . VAL A 1 114 ? -11.180 3.100   14.779  1.00 19.59 ? 114  VAL A C   1 
ATOM   852  O O   . VAL A 1 114 ? -12.140 2.340   14.535  1.00 19.21 ? 114  VAL A O   1 
ATOM   853  C CB  . VAL A 1 114 ? -10.802 5.453   13.925  1.00 19.73 ? 114  VAL A CB  1 
ATOM   854  C CG1 . VAL A 1 114 ? -11.170 4.940   12.485  1.00 18.47 ? 114  VAL A CG1 1 
ATOM   855  C CG2 . VAL A 1 114 ? -11.211 6.880   14.108  1.00 18.00 ? 114  VAL A CG2 1 
ATOM   856  N N   . ASN A 1 115 ? -9.909  2.706   14.896  1.00 18.40 ? 115  ASN A N   1 
ATOM   857  C CA  . ASN A 1 115 ? -9.486  1.317   14.718  1.00 18.08 ? 115  ASN A CA  1 
ATOM   858  C C   . ASN A 1 115 ? -10.175 0.288   15.653  1.00 17.18 ? 115  ASN A C   1 
ATOM   859  O O   . ASN A 1 115 ? -10.520 -0.809  15.236  1.00 17.40 ? 115  ASN A O   1 
ATOM   860  C CB  . ASN A 1 115 ? -7.968  1.222   14.837  1.00 17.35 ? 115  ASN A CB  1 
ATOM   861  C CG  . ASN A 1 115 ? -7.265  1.884   13.689  1.00 19.09 ? 115  ASN A CG  1 
ATOM   862  O OD1 . ASN A 1 115 ? -7.918  2.452   12.791  1.00 18.73 ? 115  ASN A OD1 1 
ATOM   863  N ND2 . ASN A 1 115 ? -5.912  1.803   13.677  1.00 15.18 ? 115  ASN A ND2 1 
ATOM   864  N N   . SER A 1 116 ? -10.333 0.647   16.918  1.00 16.88 ? 116  SER A N   1 
ATOM   865  C CA  . SER A 1 116 ? -11.100 -0.145  17.872  1.00 16.54 ? 116  SER A CA  1 
ATOM   866  C C   . SER A 1 116 ? -12.571 -0.319  17.404  1.00 15.98 ? 116  SER A C   1 
ATOM   867  O O   . SER A 1 116 ? -13.147 -1.383  17.581  1.00 15.37 ? 116  SER A O   1 
ATOM   868  C CB  . SER A 1 116 ? -11.042 0.522   19.255  1.00 16.48 ? 116  SER A CB  1 
ATOM   869  O OG  . SER A 1 116 ? -11.804 -0.189  20.253  1.00 17.27 ? 116  SER A OG  1 
ATOM   870  N N   . GLY A 1 117 ? -13.140 0.732   16.798  1.00 16.08 ? 117  GLY A N   1 
ATOM   871  C CA  . GLY A 1 117 ? -14.494 0.710   16.236  1.00 15.25 ? 117  GLY A CA  1 
ATOM   872  C C   . GLY A 1 117 ? -14.605 -0.211  15.024  1.00 15.02 ? 117  GLY A C   1 
ATOM   873  O O   . GLY A 1 117 ? -15.529 -1.007  14.921  1.00 14.31 ? 117  GLY A O   1 
ATOM   874  N N   . ILE A 1 118 ? -13.647 -0.116  14.109  1.00 14.57 ? 118  ILE A N   1 
ATOM   875  C CA  . ILE A 1 118 ? -13.644 -1.037  12.993  1.00 14.49 ? 118  ILE A CA  1 
ATOM   876  C C   . ILE A 1 118 ? -13.562 -2.470  13.563  1.00 15.14 ? 118  ILE A C   1 
ATOM   877  O O   . ILE A 1 118 ? -14.396 -3.356  13.263  1.00 13.88 ? 118  ILE A O   1 
ATOM   878  C CB  . ILE A 1 118 ? -12.475 -0.749  12.048  1.00 13.84 ? 118  ILE A CB  1 
ATOM   879  C CG1 . ILE A 1 118 ? -12.630 0.646   11.501  1.00 13.09 ? 118  ILE A CG1 1 
ATOM   880  C CG2 . ILE A 1 118 ? -12.470 -1.787  10.889  1.00 13.87 ? 118  ILE A CG2 1 
ATOM   881  C CD1 . ILE A 1 118 ? -11.472 1.163   10.770  1.00 9.34  ? 118  ILE A CD1 1 
ATOM   882  N N   . LYS A 1 119 ? -12.572 -2.674  14.437  1.00 15.23 ? 119  LYS A N   1 
ATOM   883  C CA  . LYS A 1 119 ? -12.323 -4.025  14.976  1.00 15.47 ? 119  LYS A CA  1 
ATOM   884  C C   . LYS A 1 119 ? -13.567 -4.601  15.632  1.00 15.38 ? 119  LYS A C   1 
ATOM   885  O O   . LYS A 1 119 ? -13.910 -5.755  15.371  1.00 15.37 ? 119  LYS A O   1 
ATOM   886  C CB  . LYS A 1 119 ? -11.059 -4.063  15.878  1.00 14.96 ? 119  LYS A CB  1 
ATOM   887  C CG  . LYS A 1 119 ? -10.707 -5.453  16.356  1.00 15.80 ? 119  LYS A CG  1 
ATOM   888  C CD  . LYS A 1 119 ? -9.243  -5.679  16.523  1.00 16.95 ? 119  LYS A CD  1 
ATOM   889  C CE  . LYS A 1 119 ? -9.051  -7.078  17.000  1.00 16.94 ? 119  LYS A CE  1 
ATOM   890  N NZ  . LYS A 1 119 ? -7.728  -7.216  17.651  1.00 16.31 ? 119  LYS A NZ  1 
ATOM   891  N N   . PHE A 1 120 ? -14.256 -3.784  16.439  1.00 15.54 ? 120  PHE A N   1 
ATOM   892  C CA  . PHE A 1 120 ? -15.482 -4.269  17.143  1.00 16.41 ? 120  PHE A CA  1 
ATOM   893  C C   . PHE A 1 120 ? -16.603 -4.601  16.137  1.00 16.65 ? 120  PHE A C   1 
ATOM   894  O O   . PHE A 1 120 ? -17.335 -5.587  16.299  1.00 15.28 ? 120  PHE A O   1 
ATOM   895  C CB  . PHE A 1 120 ? -15.995 -3.251  18.196  1.00 14.91 ? 120  PHE A CB  1 
ATOM   896  C CG  . PHE A 1 120 ? -17.139 -3.756  19.035  1.00 14.57 ? 120  PHE A CG  1 
ATOM   897  C CD1 . PHE A 1 120 ? -16.930 -4.687  20.061  1.00 16.08 ? 120  PHE A CD1 1 
ATOM   898  C CD2 . PHE A 1 120 ? -18.403 -3.271  18.864  1.00 14.77 ? 120  PHE A CD2 1 
ATOM   899  C CE1 . PHE A 1 120 ? -17.998 -5.150  20.890  1.00 13.86 ? 120  PHE A CE1 1 
ATOM   900  C CE2 . PHE A 1 120 ? -19.479 -3.715  19.674  1.00 16.34 ? 120  PHE A CE2 1 
ATOM   901  C CZ  . PHE A 1 120 ? -19.253 -4.662  20.687  1.00 16.16 ? 120  PHE A CZ  1 
ATOM   902  N N   . TYR A 1 121 ? -16.723 -3.749  15.107  1.00 17.11 ? 121  TYR A N   1 
ATOM   903  C CA  . TYR A 1 121 ? -17.746 -3.961  14.113  1.00 17.96 ? 121  TYR A CA  1 
ATOM   904  C C   . TYR A 1 121 ? -17.623 -5.356  13.535  1.00 18.59 ? 121  TYR A C   1 
ATOM   905  O O   . TYR A 1 121 ? -18.597 -6.082  13.509  1.00 19.19 ? 121  TYR A O   1 
ATOM   906  C CB  . TYR A 1 121 ? -17.745 -2.929  12.967  1.00 17.77 ? 121  TYR A CB  1 
ATOM   907  C CG  . TYR A 1 121 ? -18.899 -3.238  12.019  1.00 18.15 ? 121  TYR A CG  1 
ATOM   908  C CD1 . TYR A 1 121 ? -18.712 -3.980  10.844  1.00 16.60 ? 121  TYR A CD1 1 
ATOM   909  C CD2 . TYR A 1 121 ? -20.204 -2.841  12.351  1.00 16.84 ? 121  TYR A CD2 1 
ATOM   910  C CE1 . TYR A 1 121 ? -19.795 -4.270  9.988   1.00 13.64 ? 121  TYR A CE1 1 
ATOM   911  C CE2 . TYR A 1 121 ? -21.264 -3.158  11.547  1.00 15.82 ? 121  TYR A CE2 1 
ATOM   912  C CZ  . TYR A 1 121 ? -21.065 -3.873  10.387  1.00 14.18 ? 121  TYR A CZ  1 
ATOM   913  O OH  . TYR A 1 121 ? -22.151 -4.120  9.643   1.00 15.03 ? 121  TYR A OH  1 
ATOM   914  N N   . GLN A 1 122 ? -16.405 -5.701  13.124  1.00 18.32 ? 122  GLN A N   1 
ATOM   915  C CA  . GLN A 1 122 ? -16.090 -6.903  12.408  1.00 19.69 ? 122  GLN A CA  1 
ATOM   916  C C   . GLN A 1 122 ? -16.148 -8.191  13.219  1.00 20.29 ? 122  GLN A C   1 
ATOM   917  O O   . GLN A 1 122 ? -16.653 -9.193  12.721  1.00 19.89 ? 122  GLN A O   1 
ATOM   918  C CB  . GLN A 1 122 ? -14.695 -6.761  11.780  1.00 20.23 ? 122  GLN A CB  1 
ATOM   919  C CG  . GLN A 1 122 ? -14.561 -5.450  11.055  1.00 23.67 ? 122  GLN A CG  1 
ATOM   920  C CD  . GLN A 1 122 ? -13.552 -5.494  9.954   1.00 30.02 ? 122  GLN A CD  1 
ATOM   921  O OE1 . GLN A 1 122 ? -12.329 -5.592  10.209  1.00 32.08 ? 122  GLN A OE1 1 
ATOM   922  N NE2 . GLN A 1 122 ? -14.045 -5.399  8.697   1.00 30.65 ? 122  GLN A NE2 1 
ATOM   923  N N   . ARG A 1 123 ? -15.581 -8.169  14.437  1.00 19.98 ? 123  ARG A N   1 
ATOM   924  C CA  . ARG A 1 123 ? -15.544 -9.337  15.284  1.00 19.77 ? 123  ARG A CA  1 
ATOM   925  C C   . ARG A 1 123 ? -16.967 -9.812  15.529  1.00 19.94 ? 123  ARG A C   1 
ATOM   926  O O   . ARG A 1 123 ? -17.240 -11.020 15.618  1.00 20.27 ? 123  ARG A O   1 
ATOM   927  C CB  . ARG A 1 123 ? -14.865 -9.000  16.617  1.00 19.75 ? 123  ARG A CB  1 
ATOM   928  C CG  . ARG A 1 123 ? -14.663 -10.208 17.496  1.00 19.56 ? 123  ARG A CG  1 
ATOM   929  C CD  . ARG A 1 123 ? -13.851 -9.903  18.740  1.00 22.29 ? 123  ARG A CD  1 
ATOM   930  N NE  . ARG A 1 123 ? -13.982 -10.989 19.680  1.00 21.93 ? 123  ARG A NE  1 
ATOM   931  C CZ  . ARG A 1 123 ? -13.218 -12.083 19.717  1.00 22.91 ? 123  ARG A CZ  1 
ATOM   932  N NH1 . ARG A 1 123 ? -12.181 -12.252 18.903  1.00 20.63 ? 123  ARG A NH1 1 
ATOM   933  N NH2 . ARG A 1 123 ? -13.505 -13.019 20.608  1.00 24.88 ? 123  ARG A NH2 1 
ATOM   934  N N   . TYR A 1 124 ? -17.886 -8.873  15.637  1.00 19.74 ? 124  TYR A N   1 
ATOM   935  C CA  . TYR A 1 124 ? -19.249 -9.252  15.964  1.00 20.30 ? 124  TYR A CA  1 
ATOM   936  C C   . TYR A 1 124 ? -20.228 -8.880  14.844  1.00 20.64 ? 124  TYR A C   1 
ATOM   937  O O   . TYR A 1 124 ? -21.452 -8.659  15.086  1.00 19.31 ? 124  TYR A O   1 
ATOM   938  C CB  . TYR A 1 124 ? -19.658 -8.653  17.315  1.00 20.24 ? 124  TYR A CB  1 
ATOM   939  C CG  . TYR A 1 124 ? -18.706 -9.058  18.413  1.00 19.90 ? 124  TYR A CG  1 
ATOM   940  C CD1 . TYR A 1 124 ? -18.776 -10.322 18.989  1.00 19.20 ? 124  TYR A CD1 1 
ATOM   941  C CD2 . TYR A 1 124 ? -17.719 -8.169  18.864  1.00 19.52 ? 124  TYR A CD2 1 
ATOM   942  C CE1 . TYR A 1 124 ? -17.866 -10.706 19.996  1.00 19.09 ? 124  TYR A CE1 1 
ATOM   943  C CE2 . TYR A 1 124 ? -16.852 -8.517  19.873  1.00 19.62 ? 124  TYR A CE2 1 
ATOM   944  C CZ  . TYR A 1 124 ? -16.918 -9.780  20.428  1.00 19.59 ? 124  TYR A CZ  1 
ATOM   945  O OH  . TYR A 1 124 ? -16.028 -10.102 21.406  1.00 18.16 ? 124  TYR A OH  1 
ATOM   946  N N   . GLU A 1 125 ? -19.658 -8.857  13.629  1.00 20.44 ? 125  GLU A N   1 
ATOM   947  C CA  . GLU A 1 125 ? -20.376 -8.564  12.369  1.00 21.14 ? 125  GLU A CA  1 
ATOM   948  C C   . GLU A 1 125 ? -21.786 -9.168  12.291  1.00 21.23 ? 125  GLU A C   1 
ATOM   949  O O   . GLU A 1 125 ? -22.758 -8.492  11.885  1.00 21.67 ? 125  GLU A O   1 
ATOM   950  C CB  . GLU A 1 125 ? -19.533 -9.015  11.162  1.00 21.21 ? 125  GLU A CB  1 
ATOM   951  C CG  . GLU A 1 125 ? -19.958 -8.404  9.849   1.00 21.14 ? 125  GLU A CG  1 
ATOM   952  C CD  . GLU A 1 125 ? -21.108 -9.148  9.241   1.00 19.84 ? 125  GLU A CD  1 
ATOM   953  O OE1 . GLU A 1 125 ? -21.131 -10.386 9.330   1.00 17.82 ? 125  GLU A OE1 1 
ATOM   954  O OE2 . GLU A 1 125 ? -21.998 -8.491  8.690   1.00 20.73 ? 125  GLU A OE2 1 
ATOM   955  N N   . SER A 1 126 ? -21.923 -10.418 12.701  1.00 20.15 ? 126  SER A N   1 
ATOM   956  C CA  . SER A 1 126 ? -23.184 -11.051 12.455  1.00 20.64 ? 126  SER A CA  1 
ATOM   957  C C   . SER A 1 126 ? -24.245 -10.494 13.418  1.00 19.54 ? 126  SER A C   1 
ATOM   958  O O   . SER A 1 126 ? -25.432 -10.837 13.289  1.00 18.98 ? 126  SER A O   1 
ATOM   959  C CB  . SER A 1 126 ? -23.092 -12.595 12.403  1.00 20.71 ? 126  SER A CB  1 
ATOM   960  O OG  . SER A 1 126 ? -23.303 -13.120 13.688  1.00 23.80 ? 126  SER A OG  1 
ATOM   961  N N   . LEU A 1 127 ? -23.823 -9.573  14.306  1.00 18.51 ? 127  LEU A N   1 
ATOM   962  C CA  . LEU A 1 127 ? -24.756 -8.814  15.177  1.00 17.05 ? 127  LEU A CA  1 
ATOM   963  C C   . LEU A 1 127 ? -24.732 -7.313  14.967  1.00 18.14 ? 127  LEU A C   1 
ATOM   964  O O   . LEU A 1 127 ? -25.767 -6.639  15.127  1.00 18.66 ? 127  LEU A O   1 
ATOM   965  C CB  . LEU A 1 127 ? -24.490 -9.095  16.642  1.00 17.00 ? 127  LEU A CB  1 
ATOM   966  C CG  . LEU A 1 127 ? -24.477 -10.533 17.148  1.00 13.44 ? 127  LEU A CG  1 
ATOM   967  C CD1 . LEU A 1 127 ? -23.925 -10.528 18.535  1.00 9.21  ? 127  LEU A CD1 1 
ATOM   968  C CD2 . LEU A 1 127 ? -25.851 -11.039 17.163  1.00 14.15 ? 127  LEU A CD2 1 
ATOM   969  N N   . THR A 1 128 ? -23.564 -6.789  14.585  1.00 18.48 ? 128  THR A N   1 
ATOM   970  C CA  . THR A 1 128 ? -23.350 -5.380  14.400  1.00 18.29 ? 128  THR A CA  1 
ATOM   971  C C   . THR A 1 128 ? -23.996 -4.919  13.063  1.00 19.76 ? 128  THR A C   1 
ATOM   972  O O   . THR A 1 128 ? -24.174 -3.731  12.785  1.00 19.57 ? 128  THR A O   1 
ATOM   973  C CB  . THR A 1 128 ? -21.812 -5.002  14.532  1.00 18.32 ? 128  THR A CB  1 
ATOM   974  O OG1 . THR A 1 128 ? -21.017 -5.678  13.556  1.00 17.83 ? 128  THR A OG1 1 
ATOM   975  C CG2 . THR A 1 128 ? -21.273 -5.370  15.874  1.00 17.88 ? 128  THR A CG2 1 
ATOM   976  N N   . ARG A 1 129 ? -24.367 -5.883  12.242  1.00 21.22 ? 129  ARG A N   1 
ATOM   977  C CA  . ARG A 1 129 ? -24.978 -5.572  10.986  1.00 21.85 ? 129  ARG A CA  1 
ATOM   978  C C   . ARG A 1 129 ? -26.383 -5.058  11.136  1.00 22.38 ? 129  ARG A C   1 
ATOM   979  O O   . ARG A 1 129 ? -26.825 -4.315  10.270  1.00 22.37 ? 129  ARG A O   1 
ATOM   980  C CB  . ARG A 1 129 ? -24.936 -6.760  10.061  1.00 22.28 ? 129  ARG A CB  1 
ATOM   981  C CG  . ARG A 1 129 ? -25.907 -7.888  10.356  1.00 23.02 ? 129  ARG A CG  1 
ATOM   982  C CD  . ARG A 1 129 ? -25.142 -9.120  9.972   1.00 24.80 ? 129  ARG A CD  1 
ATOM   983  N NE  . ARG A 1 129 ? -25.949 -10.123 9.334   1.00 25.76 ? 129  ARG A NE  1 
ATOM   984  C CZ  . ARG A 1 129 ? -25.460 -11.204 8.733   1.00 26.00 ? 129  ARG A CZ  1 
ATOM   985  N NH1 . ARG A 1 129 ? -24.150 -11.436 8.679   1.00 24.98 ? 129  ARG A NH1 1 
ATOM   986  N NH2 . ARG A 1 129 ? -26.309 -12.051 8.172   1.00 26.31 ? 129  ARG A NH2 1 
ATOM   987  N N   . ASN A 1 130 ? -27.072 -5.380  12.228  1.00 22.63 ? 130  ASN A N   1 
ATOM   988  C CA  . ASN A 1 130 ? -28.472 -4.915  12.328  1.00 23.41 ? 130  ASN A CA  1 
ATOM   989  C C   . ASN A 1 130 ? -28.956 -4.572  13.727  1.00 23.36 ? 130  ASN A C   1 
ATOM   990  O O   . ASN A 1 130 ? -30.154 -4.444  13.972  1.00 24.45 ? 130  ASN A O   1 
ATOM   991  C CB  . ASN A 1 130 ? -29.411 -5.938  11.711  1.00 23.88 ? 130  ASN A CB  1 
ATOM   992  C CG  . ASN A 1 130 ? -29.438 -7.236  12.488  1.00 25.58 ? 130  ASN A CG  1 
ATOM   993  O OD1 . ASN A 1 130 ? -28.616 -7.441  13.388  1.00 27.22 ? 130  ASN A OD1 1 
ATOM   994  N ND2 . ASN A 1 130 ? -30.357 -8.134  12.131  1.00 24.37 ? 130  ASN A ND2 1 
ATOM   995  N N   . ILE A 1 131 ? -28.015 -4.446  14.650  1.00 23.15 ? 131  ILE A N   1 
ATOM   996  C CA  . ILE A 1 131 ? -28.311 -4.017  16.002  1.00 22.23 ? 131  ILE A CA  1 
ATOM   997  C C   . ILE A 1 131 ? -27.454 -2.809  16.332  1.00 22.12 ? 131  ILE A C   1 
ATOM   998  O O   . ILE A 1 131 ? -26.227 -2.813  16.167  1.00 22.01 ? 131  ILE A O   1 
ATOM   999  C CB  . ILE A 1 131 ? -28.123 -5.147  17.050  1.00 22.43 ? 131  ILE A CB  1 
ATOM   1000 C CG1 . ILE A 1 131 ? -29.306 -6.135  16.950  1.00 22.19 ? 131  ILE A CG1 1 
ATOM   1001 C CG2 . ILE A 1 131 ? -28.151 -4.578  18.458  1.00 21.38 ? 131  ILE A CG2 1 
ATOM   1002 C CD1 . ILE A 1 131 ? -28.917 -7.563  17.053  1.00 20.95 ? 131  ILE A CD1 1 
ATOM   1003 N N   . VAL A 1 132 ? -28.134 -1.775  16.803  1.00 21.59 ? 132  VAL A N   1 
ATOM   1004 C CA  . VAL A 1 132 ? -27.507 -0.568  17.237  1.00 20.99 ? 132  VAL A CA  1 
ATOM   1005 C C   . VAL A 1 132 ? -27.171 -0.760  18.710  1.00 20.61 ? 132  VAL A C   1 
ATOM   1006 O O   . VAL A 1 132 ? -28.084 -0.956  19.543  1.00 20.12 ? 132  VAL A O   1 
ATOM   1007 C CB  . VAL A 1 132 ? -28.461 0.608   16.998  1.00 21.03 ? 132  VAL A CB  1 
ATOM   1008 C CG1 . VAL A 1 132 ? -27.847 1.920   17.445  1.00 21.16 ? 132  VAL A CG1 1 
ATOM   1009 C CG2 . VAL A 1 132 ? -28.776 0.672   15.486  1.00 21.52 ? 132  VAL A CG2 1 
ATOM   1010 N N   . PRO A 1 133 ? -25.857 -0.713  19.040  1.00 19.56 ? 133  PRO A N   1 
ATOM   1011 C CA  . PRO A 1 133 ? -25.381 -0.884  20.418  1.00 19.29 ? 133  PRO A CA  1 
ATOM   1012 C C   . PRO A 1 133 ? -25.806 0.257   21.339  1.00 19.25 ? 133  PRO A C   1 
ATOM   1013 O O   . PRO A 1 133 ? -25.915 1.427   20.900  1.00 18.70 ? 133  PRO A O   1 
ATOM   1014 C CB  . PRO A 1 133 ? -23.852 -0.908  20.274  1.00 18.94 ? 133  PRO A CB  1 
ATOM   1015 C CG  . PRO A 1 133 ? -23.586 -0.989  18.801  1.00 19.50 ? 133  PRO A CG  1 
ATOM   1016 C CD  . PRO A 1 133 ? -24.758 -0.347  18.146  1.00 19.63 ? 133  PRO A CD  1 
ATOM   1017 N N   . PHE A 1 134 ? -26.088 -0.082  22.595  1.00 18.03 ? 134  PHE A N   1 
ATOM   1018 C CA  . PHE A 1 134 ? -26.370 0.967   23.553  1.00 17.52 ? 134  PHE A CA  1 
ATOM   1019 C C   . PHE A 1 134 ? -25.067 1.478   24.166  1.00 16.53 ? 134  PHE A C   1 
ATOM   1020 O O   . PHE A 1 134 ? -24.239 0.705   24.721  1.00 15.16 ? 134  PHE A O   1 
ATOM   1021 C CB  . PHE A 1 134 ? -27.382 0.553   24.636  1.00 17.32 ? 134  PHE A CB  1 
ATOM   1022 C CG  . PHE A 1 134 ? -27.784 1.692   25.534  1.00 18.10 ? 134  PHE A CG  1 
ATOM   1023 C CD1 . PHE A 1 134 ? -28.756 2.600   25.139  1.00 17.55 ? 134  PHE A CD1 1 
ATOM   1024 C CD2 . PHE A 1 134 ? -27.180 1.855   26.778  1.00 18.80 ? 134  PHE A CD2 1 
ATOM   1025 C CE1 . PHE A 1 134 ? -29.135 3.655   25.989  1.00 19.22 ? 134  PHE A CE1 1 
ATOM   1026 C CE2 . PHE A 1 134 ? -27.536 2.912   27.631  1.00 19.30 ? 134  PHE A CE2 1 
ATOM   1027 C CZ  . PHE A 1 134 ? -28.514 3.813   27.237  1.00 19.31 ? 134  PHE A CZ  1 
ATOM   1028 N N   . ILE A 1 135 ? -24.898 2.793   24.091  1.00 16.12 ? 135  ILE A N   1 
ATOM   1029 C CA  . ILE A 1 135 ? -23.556 3.374   24.332  1.00 16.96 ? 135  ILE A CA  1 
ATOM   1030 C C   . ILE A 1 135 ? -23.456 4.419   25.453  1.00 17.39 ? 135  ILE A C   1 
ATOM   1031 O O   . ILE A 1 135 ? -24.141 5.478   25.416  1.00 17.01 ? 135  ILE A O   1 
ATOM   1032 C CB  . ILE A 1 135 ? -22.948 3.948   23.046  1.00 16.95 ? 135  ILE A CB  1 
ATOM   1033 C CG1 . ILE A 1 135 ? -22.807 2.845   21.996  1.00 16.43 ? 135  ILE A CG1 1 
ATOM   1034 C CG2 . ILE A 1 135 ? -21.586 4.642   23.357  1.00 16.08 ? 135  ILE A CG2 1 
ATOM   1035 C CD1 . ILE A 1 135 ? -22.016 3.290   20.723  1.00 18.70 ? 135  ILE A CD1 1 
ATOM   1036 N N   . ARG A 1 136 ? -22.577 4.135   26.422  1.00 17.55 ? 136  ARG A N   1 
ATOM   1037 C CA  . ARG A 1 136 ? -22.356 5.060   27.530  1.00 17.50 ? 136  ARG A CA  1 
ATOM   1038 C C   . ARG A 1 136 ? -20.927 5.609   27.614  1.00 17.56 ? 136  ARG A C   1 
ATOM   1039 O O   . ARG A 1 136 ? -19.988 4.987   27.130  1.00 17.34 ? 136  ARG A O   1 
ATOM   1040 C CB  . ARG A 1 136 ? -22.777 4.419   28.826  1.00 17.67 ? 136  ARG A CB  1 
ATOM   1041 C CG  . ARG A 1 136 ? -24.259 4.184   28.957  1.00 16.38 ? 136  ARG A CG  1 
ATOM   1042 C CD  . ARG A 1 136 ? -24.552 3.650   30.346  1.00 16.82 ? 136  ARG A CD  1 
ATOM   1043 N NE  . ARG A 1 136 ? -23.648 2.533   30.646  1.00 16.85 ? 136  ARG A NE  1 
ATOM   1044 C CZ  . ARG A 1 136 ? -23.510 1.963   31.840  1.00 15.97 ? 136  ARG A CZ  1 
ATOM   1045 N NH1 . ARG A 1 136 ? -24.248 2.359   32.848  1.00 15.05 ? 136  ARG A NH1 1 
ATOM   1046 N NH2 . ARG A 1 136 ? -22.639 0.984   32.010  1.00 17.29 ? 136  ARG A NH2 1 
ATOM   1047 N N   . SER A 1 137 ? -20.768 6.789   28.212  1.00 18.40 ? 137  SER A N   1 
ATOM   1048 C CA  . SER A 1 137 ? -19.443 7.396   28.330  1.00 19.71 ? 137  SER A CA  1 
ATOM   1049 C C   . SER A 1 137 ? -19.308 8.196   29.596  1.00 20.11 ? 137  SER A C   1 
ATOM   1050 O O   . SER A 1 137 ? -20.146 9.032   29.899  1.00 21.70 ? 137  SER A O   1 
ATOM   1051 C CB  . SER A 1 137 ? -19.132 8.299   27.125  1.00 20.49 ? 137  SER A CB  1 
ATOM   1052 O OG  . SER A 1 137 ? -17.796 8.824   27.120  1.00 20.45 ? 137  SER A OG  1 
ATOM   1053 N N   . SER A 1 138 ? -18.231 7.974   30.334  1.00 20.82 ? 138  SER A N   1 
ATOM   1054 C CA  . SER A 1 138 ? -17.912 8.872   31.445  1.00 21.17 ? 138  SER A CA  1 
ATOM   1055 C C   . SER A 1 138 ? -17.820 10.299  30.873  1.00 21.34 ? 138  SER A C   1 
ATOM   1056 O O   . SER A 1 138 ? -17.593 10.462  29.690  1.00 20.70 ? 138  SER A O   1 
ATOM   1057 C CB  . SER A 1 138 ? -16.590 8.458   32.103  1.00 20.36 ? 138  SER A CB  1 
ATOM   1058 O OG  . SER A 1 138 ? -16.399 9.154   33.326  1.00 20.54 ? 138  SER A OG  1 
ATOM   1059 N N   . GLY A 1 139 ? -17.988 11.326  31.697  1.00 22.36 ? 139  GLY A N   1 
ATOM   1060 C CA  . GLY A 1 139 ? -17.937 12.685  31.165  1.00 23.77 ? 139  GLY A CA  1 
ATOM   1061 C C   . GLY A 1 139 ? -16.592 13.383  31.245  1.00 25.06 ? 139  GLY A C   1 
ATOM   1062 O O   . GLY A 1 139 ? -16.316 14.088  32.223  1.00 27.31 ? 139  GLY A O   1 
ATOM   1063 N N   . SER A 1 140 ? -15.753 13.225  30.235  1.00 24.41 ? 140  SER A N   1 
ATOM   1064 C CA  . SER A 1 140 ? -14.458 13.907  30.187  1.00 23.74 ? 140  SER A CA  1 
ATOM   1065 C C   . SER A 1 140 ? -14.140 14.104  28.702  1.00 23.44 ? 140  SER A C   1 
ATOM   1066 O O   . SER A 1 140 ? -14.284 13.169  27.923  1.00 23.25 ? 140  SER A O   1 
ATOM   1067 C CB  . SER A 1 140 ? -13.391 13.048  30.867  1.00 23.85 ? 140  SER A CB  1 
ATOM   1068 O OG  . SER A 1 140 ? -12.055 13.396  30.461  1.00 24.27 ? 140  SER A OG  1 
ATOM   1069 N N   . SER A 1 141 ? -13.723 15.295  28.295  1.00 22.45 ? 141  SER A N   1 
ATOM   1070 C CA  . SER A 1 141 ? -13.585 15.545  26.873  1.00 22.74 ? 141  SER A CA  1 
ATOM   1071 C C   . SER A 1 141 ? -12.919 14.378  26.158  1.00 21.93 ? 141  SER A C   1 
ATOM   1072 O O   . SER A 1 141 ? -13.413 13.950  25.116  1.00 22.49 ? 141  SER A O   1 
ATOM   1073 C CB  . SER A 1 141 ? -12.778 16.798  26.577  1.00 22.43 ? 141  SER A CB  1 
ATOM   1074 O OG  . SER A 1 141 ? -13.134 17.800  27.471  1.00 27.72 ? 141  SER A OG  1 
ATOM   1075 N N   . ARG A 1 142 ? -11.789 13.887  26.674  1.00 21.06 ? 142  ARG A N   1 
ATOM   1076 C CA  . ARG A 1 142 ? -11.058 12.806  25.979  1.00 20.35 ? 142  ARG A CA  1 
ATOM   1077 C C   . ARG A 1 142 ? -11.835 11.462  25.879  1.00 19.88 ? 142  ARG A C   1 
ATOM   1078 O O   . ARG A 1 142 ? -11.675 10.671  24.911  1.00 19.35 ? 142  ARG A O   1 
ATOM   1079 C CB  . ARG A 1 142 ? -9.681  12.617  26.574  1.00 21.02 ? 142  ARG A CB  1 
ATOM   1080 C CG  . ARG A 1 142 ? -9.610  12.188  28.085  1.00 23.16 ? 142  ARG A CG  1 
ATOM   1081 C CD  . ARG A 1 142 ? -8.142  12.127  28.535  1.00 28.92 ? 142  ARG A CD  1 
ATOM   1082 N NE  . ARG A 1 142 ? -7.979  11.796  29.953  1.00 34.90 ? 142  ARG A NE  1 
ATOM   1083 C CZ  . ARG A 1 142 ? -7.981  12.690  30.943  1.00 38.45 ? 142  ARG A CZ  1 
ATOM   1084 N NH1 . ARG A 1 142 ? -8.146  13.988  30.693  1.00 38.03 ? 142  ARG A NH1 1 
ATOM   1085 N NH2 . ARG A 1 142 ? -7.826  12.277  32.194  1.00 39.75 ? 142  ARG A NH2 1 
ATOM   1086 N N   . VAL A 1 143 ? -12.705 11.216  26.850  1.00 18.97 ? 143  VAL A N   1 
ATOM   1087 C CA  . VAL A 1 143 ? -13.439 9.952   26.878  1.00 19.59 ? 143  VAL A CA  1 
ATOM   1088 C C   . VAL A 1 143 ? -14.595 9.996   25.840  1.00 18.68 ? 143  VAL A C   1 
ATOM   1089 O O   . VAL A 1 143 ? -14.668 9.141   24.959  1.00 17.72 ? 143  VAL A O   1 
ATOM   1090 C CB  . VAL A 1 143 ? -13.862 9.541   28.322  1.00 19.50 ? 143  VAL A CB  1 
ATOM   1091 C CG1 . VAL A 1 143 ? -14.600 8.207   28.329  1.00 18.80 ? 143  VAL A CG1 1 
ATOM   1092 C CG2 . VAL A 1 143 ? -12.650 9.420   29.151  1.00 19.65 ? 143  VAL A CG2 1 
ATOM   1093 N N   . ILE A 1 144 ? -15.405 11.049  25.946  1.00 19.20 ? 144  ILE A N   1 
ATOM   1094 C CA  . ILE A 1 144 ? -16.458 11.463  25.000  1.00 19.21 ? 144  ILE A CA  1 
ATOM   1095 C C   . ILE A 1 144 ? -15.993 11.504  23.545  1.00 18.86 ? 144  ILE A C   1 
ATOM   1096 O O   . ILE A 1 144 ? -16.603 10.890  22.647  1.00 19.56 ? 144  ILE A O   1 
ATOM   1097 C CB  . ILE A 1 144 ? -16.974 12.851  25.367  1.00 19.49 ? 144  ILE A CB  1 
ATOM   1098 C CG1 . ILE A 1 144 ? -17.792 12.807  26.653  1.00 21.56 ? 144  ILE A CG1 1 
ATOM   1099 C CG2 . ILE A 1 144 ? -17.871 13.384  24.304  1.00 20.80 ? 144  ILE A CG2 1 
ATOM   1100 C CD1 . ILE A 1 144 ? -18.138 14.229  27.223  1.00 24.52 ? 144  ILE A CD1 1 
ATOM   1101 N N   . ALA A 1 145 ? -14.907 12.211  23.312  1.00 17.81 ? 145  ALA A N   1 
ATOM   1102 C CA  . ALA A 1 145 ? -14.320 12.232  21.984  1.00 17.06 ? 145  ALA A CA  1 
ATOM   1103 C C   . ALA A 1 145 ? -13.932 10.851  21.495  1.00 16.19 ? 145  ALA A C   1 
ATOM   1104 O O   . ALA A 1 145 ? -14.146 10.512  20.310  1.00 16.66 ? 145  ALA A O   1 
ATOM   1105 C CB  . ALA A 1 145 ? -13.129 13.183  21.933  1.00 16.57 ? 145  ALA A CB  1 
ATOM   1106 N N   . SER A 1 146 ? -13.343 10.057  22.387  1.00 16.12 ? 146  SER A N   1 
ATOM   1107 C CA  . SER A 1 146 ? -12.884 8.677   22.039  1.00 15.36 ? 146  SER A CA  1 
ATOM   1108 C C   . SER A 1 146 ? -14.062 7.759   21.728  1.00 14.98 ? 146  SER A C   1 
ATOM   1109 O O   . SER A 1 146 ? -14.028 7.029   20.754  1.00 14.98 ? 146  SER A O   1 
ATOM   1110 C CB  . SER A 1 146 ? -12.110 8.070   23.184  1.00 15.70 ? 146  SER A CB  1 
ATOM   1111 O OG  . SER A 1 146 ? -10.802 8.556   23.259  1.00 16.57 ? 146  SER A OG  1 
ATOM   1112 N N   . GLY A 1 147 ? -15.104 7.828   22.556  1.00 14.14 ? 147  GLY A N   1 
ATOM   1113 C CA  . GLY A 1 147 ? -16.353 7.194   22.262  1.00 14.82 ? 147  GLY A CA  1 
ATOM   1114 C C   . GLY A 1 147 ? -16.777 7.491   20.829  1.00 16.28 ? 147  GLY A C   1 
ATOM   1115 O O   . GLY A 1 147 ? -17.064 6.545   20.032  1.00 16.65 ? 147  GLY A O   1 
ATOM   1116 N N   . LYS A 1 148 ? -16.780 8.778   20.477  1.00 16.24 ? 148  LYS A N   1 
ATOM   1117 C CA  . LYS A 1 148 ? -17.201 9.210   19.154  1.00 16.66 ? 148  LYS A CA  1 
ATOM   1118 C C   . LYS A 1 148 ? -16.255 8.798   18.020  1.00 17.18 ? 148  LYS A C   1 
ATOM   1119 O O   . LYS A 1 148 ? -16.696 8.560   16.905  1.00 18.49 ? 148  LYS A O   1 
ATOM   1120 C CB  . LYS A 1 148 ? -17.433 10.723  19.164  1.00 17.52 ? 148  LYS A CB  1 
ATOM   1121 C CG  . LYS A 1 148 ? -18.718 11.148  19.915  1.00 17.43 ? 148  LYS A CG  1 
ATOM   1122 C CD  . LYS A 1 148 ? -18.816 12.655  20.013  1.00 19.66 ? 148  LYS A CD  1 
ATOM   1123 C CE  . LYS A 1 148 ? -19.921 13.067  20.975  1.00 21.88 ? 148  LYS A CE  1 
ATOM   1124 N NZ  . LYS A 1 148 ? -19.559 14.333  21.757  1.00 20.63 ? 148  LYS A NZ  1 
ATOM   1125 N N   . LYS A 1 149 ? -14.957 8.684   18.271  1.00 17.55 ? 149  LYS A N   1 
ATOM   1126 C CA  . LYS A 1 149 ? -14.084 8.156   17.230  1.00 17.86 ? 149  LYS A CA  1 
ATOM   1127 C C   . LYS A 1 149 ? -14.291 6.652   17.016  1.00 19.04 ? 149  LYS A C   1 
ATOM   1128 O O   . LYS A 1 149 ? -14.060 6.109   15.912  1.00 20.54 ? 149  LYS A O   1 
ATOM   1129 C CB  . LYS A 1 149 ? -12.631 8.428   17.562  1.00 18.12 ? 149  LYS A CB  1 
ATOM   1130 C CG  . LYS A 1 149 ? -12.206 9.833   17.343  1.00 17.55 ? 149  LYS A CG  1 
ATOM   1131 C CD  . LYS A 1 149 ? -11.794 10.073  15.895  1.00 18.69 ? 149  LYS A CD  1 
ATOM   1132 C CE  . LYS A 1 149 ? -11.865 11.568  15.550  1.00 20.01 ? 149  LYS A CE  1 
ATOM   1133 N NZ  . LYS A 1 149 ? -11.707 11.859  14.122  1.00 19.67 ? 149  LYS A NZ  1 
ATOM   1134 N N   . PHE A 1 150 ? -14.705 5.963   18.070  1.00 18.72 ? 150  PHE A N   1 
ATOM   1135 C CA  . PHE A 1 150 ? -15.029 4.567   17.959  1.00 18.60 ? 150  PHE A CA  1 
ATOM   1136 C C   . PHE A 1 150 ? -16.318 4.437   17.136  1.00 18.68 ? 150  PHE A C   1 
ATOM   1137 O O   . PHE A 1 150 ? -16.374 3.628   16.224  1.00 18.63 ? 150  PHE A O   1 
ATOM   1138 C CB  . PHE A 1 150 ? -15.117 3.954   19.371  1.00 18.98 ? 150  PHE A CB  1 
ATOM   1139 C CG  . PHE A 1 150 ? -15.686 2.530   19.439  1.00 18.22 ? 150  PHE A CG  1 
ATOM   1140 C CD1 . PHE A 1 150 ? -17.022 2.263   19.146  1.00 18.77 ? 150  PHE A CD1 1 
ATOM   1141 C CD2 . PHE A 1 150 ? -14.889 1.469   19.879  1.00 18.73 ? 150  PHE A CD2 1 
ATOM   1142 C CE1 . PHE A 1 150 ? -17.513 0.950   19.264  1.00 18.75 ? 150  PHE A CE1 1 
ATOM   1143 C CE2 . PHE A 1 150 ? -15.380 0.179   20.002  1.00 16.64 ? 150  PHE A CE2 1 
ATOM   1144 C CZ  . PHE A 1 150 ? -16.684 -0.082  19.698  1.00 16.59 ? 150  PHE A CZ  1 
ATOM   1145 N N   . ILE A 1 151 ? -17.331 5.252   17.434  1.00 18.92 ? 151  ILE A N   1 
ATOM   1146 C CA  . ILE A 1 151 ? -18.620 5.188   16.712  1.00 19.62 ? 151  ILE A CA  1 
ATOM   1147 C C   . ILE A 1 151 ? -18.413 5.533   15.270  1.00 20.52 ? 151  ILE A C   1 
ATOM   1148 O O   . ILE A 1 151 ? -19.050 4.963   14.399  1.00 21.34 ? 151  ILE A O   1 
ATOM   1149 C CB  . ILE A 1 151 ? -19.660 6.174   17.257  1.00 19.56 ? 151  ILE A CB  1 
ATOM   1150 C CG1 . ILE A 1 151 ? -20.243 5.639   18.561  1.00 15.81 ? 151  ILE A CG1 1 
ATOM   1151 C CG2 . ILE A 1 151 ? -20.755 6.497   16.160  1.00 17.91 ? 151  ILE A CG2 1 
ATOM   1152 C CD1 . ILE A 1 151 ? -20.933 6.726   19.391  1.00 15.21 ? 151  ILE A CD1 1 
ATOM   1153 N N   . GLU A 1 152 ? -17.502 6.469   15.033  1.00 21.85 ? 152  GLU A N   1 
ATOM   1154 C CA  . GLU A 1 152 ? -17.053 6.840   13.675  1.00 22.03 ? 152  GLU A CA  1 
ATOM   1155 C C   . GLU A 1 152 ? -16.536 5.677   12.834  1.00 21.93 ? 152  GLU A C   1 
ATOM   1156 O O   . GLU A 1 152 ? -16.979 5.481   11.718  1.00 21.86 ? 152  GLU A O   1 
ATOM   1157 C CB  . GLU A 1 152 ? -15.966 7.889   13.784  1.00 22.25 ? 152  GLU A CB  1 
ATOM   1158 C CG  . GLU A 1 152 ? -15.879 8.796   12.576  1.00 23.45 ? 152  GLU A CG  1 
ATOM   1159 C CD  . GLU A 1 152 ? -14.745 9.827   12.647  1.00 23.90 ? 152  GLU A CD  1 
ATOM   1160 O OE1 . GLU A 1 152 ? -14.528 10.469  13.710  1.00 23.79 ? 152  GLU A OE1 1 
ATOM   1161 O OE2 . GLU A 1 152 ? -14.080 10.015  11.600  1.00 25.80 ? 152  GLU A OE2 1 
ATOM   1162 N N   . GLY A 1 153 ? -15.577 4.920   13.354  1.00 22.01 ? 153  GLY A N   1 
ATOM   1163 C CA  . GLY A 1 153 ? -15.057 3.767   12.638  1.00 21.60 ? 153  GLY A CA  1 
ATOM   1164 C C   . GLY A 1 153 ? -16.072 2.623   12.512  1.00 22.08 ? 153  GLY A C   1 
ATOM   1165 O O   . GLY A 1 153 ? -16.186 2.005   11.450  1.00 22.68 ? 153  GLY A O   1 
ATOM   1166 N N   . PHE A 1 154 ? -16.810 2.332   13.577  1.00 21.78 ? 154  PHE A N   1 
ATOM   1167 C CA  . PHE A 1 154 ? -17.931 1.361   13.525  1.00 21.97 ? 154  PHE A CA  1 
ATOM   1168 C C   . PHE A 1 154 ? -18.887 1.717   12.384  1.00 22.79 ? 154  PHE A C   1 
ATOM   1169 O O   . PHE A 1 154 ? -19.267 0.849   11.597  1.00 22.42 ? 154  PHE A O   1 
ATOM   1170 C CB  . PHE A 1 154 ? -18.665 1.377   14.866  1.00 21.29 ? 154  PHE A CB  1 
ATOM   1171 C CG  . PHE A 1 154 ? -19.810 0.383   15.015  1.00 19.59 ? 154  PHE A CG  1 
ATOM   1172 C CD1 . PHE A 1 154 ? -21.088 0.664   14.519  1.00 16.29 ? 154  PHE A CD1 1 
ATOM   1173 C CD2 . PHE A 1 154 ? -19.649 -0.764  15.783  1.00 17.97 ? 154  PHE A CD2 1 
ATOM   1174 C CE1 . PHE A 1 154 ? -22.146 -0.232  14.708  1.00 13.08 ? 154  PHE A CE1 1 
ATOM   1175 C CE2 . PHE A 1 154 ? -20.723 -1.655  15.998  1.00 14.85 ? 154  PHE A CE2 1 
ATOM   1176 C CZ  . PHE A 1 154 ? -21.954 -1.385  15.465  1.00 14.47 ? 154  PHE A CZ  1 
ATOM   1177 N N   . GLN A 1 155 ? -19.254 2.997   12.282  1.00 23.56 ? 155  GLN A N   1 
ATOM   1178 C CA  . GLN A 1 155 ? -20.209 3.443   11.270  1.00 24.88 ? 155  GLN A CA  1 
ATOM   1179 C C   . GLN A 1 155 ? -19.638 3.362   9.840   1.00 24.10 ? 155  GLN A C   1 
ATOM   1180 O O   . GLN A 1 155 ? -20.369 3.042   8.899   1.00 24.09 ? 155  GLN A O   1 
ATOM   1181 C CB  . GLN A 1 155 ? -20.778 4.836   11.627  1.00 25.80 ? 155  GLN A CB  1 
ATOM   1182 C CG  . GLN A 1 155 ? -21.970 5.330   10.737  1.00 32.99 ? 155  GLN A CG  1 
ATOM   1183 C CD  . GLN A 1 155 ? -23.195 4.346   10.690  1.00 39.30 ? 155  GLN A CD  1 
ATOM   1184 O OE1 . GLN A 1 155 ? -23.874 4.163   11.703  1.00 44.06 ? 155  GLN A OE1 1 
ATOM   1185 N NE2 . GLN A 1 155 ? -23.465 3.731   9.504   1.00 36.05 ? 155  GLN A NE2 1 
ATOM   1186 N N   . SER A 1 156 ? -18.335 3.614   9.689   1.00 23.07 ? 156  SER A N   1 
ATOM   1187 C CA  . SER A 1 156 ? -17.653 3.456   8.387   1.00 22.82 ? 156  SER A CA  1 
ATOM   1188 C C   . SER A 1 156 ? -17.580 2.032   7.882   1.00 21.72 ? 156  SER A C   1 
ATOM   1189 O O   . SER A 1 156 ? -17.553 1.780   6.680   1.00 22.39 ? 156  SER A O   1 
ATOM   1190 C CB  . SER A 1 156 ? -16.222 4.018   8.426   1.00 22.57 ? 156  SER A CB  1 
ATOM   1191 O OG  . SER A 1 156 ? -16.311 5.425   8.370   1.00 24.81 ? 156  SER A OG  1 
ATOM   1192 N N   . THR A 1 157 ? -17.470 1.108   8.804   1.00 20.52 ? 157  THR A N   1 
ATOM   1193 C CA  . THR A 1 157 ? -17.383 -0.286  8.452   1.00 20.24 ? 157  THR A CA  1 
ATOM   1194 C C   . THR A 1 157 ? -18.775 -0.808  8.116   1.00 20.22 ? 157  THR A C   1 
ATOM   1195 O O   . THR A 1 157 ? -18.918 -1.547  7.162   1.00 20.67 ? 157  THR A O   1 
ATOM   1196 C CB  . THR A 1 157 ? -16.790 -1.069  9.605   1.00 19.75 ? 157  THR A CB  1 
ATOM   1197 O OG1 . THR A 1 157 ? -15.679 -0.335  10.096  1.00 19.37 ? 157  THR A OG1 1 
ATOM   1198 C CG2 . THR A 1 157 ? -16.350 -2.439  9.163   1.00 18.00 ? 157  THR A CG2 1 
ATOM   1199 N N   . LYS A 1 158 ? -19.785 -0.372  8.875   1.00 20.45 ? 158  LYS A N   1 
ATOM   1200 C CA  . LYS A 1 158 ? -21.183 -0.749  8.651   1.00 20.77 ? 158  LYS A CA  1 
ATOM   1201 C C   . LYS A 1 158 ? -21.663 -0.366  7.237   1.00 22.88 ? 158  LYS A C   1 
ATOM   1202 O O   . LYS A 1 158 ? -22.333 -1.165  6.555   1.00 24.11 ? 158  LYS A O   1 
ATOM   1203 C CB  . LYS A 1 158 ? -22.111 -0.204  9.761   1.00 19.33 ? 158  LYS A CB  1 
ATOM   1204 C CG  . LYS A 1 158 ? -23.503 -0.772  9.720   1.00 17.10 ? 158  LYS A CG  1 
ATOM   1205 C CD  . LYS A 1 158 ? -24.395 -0.251  10.766  1.00 12.66 ? 158  LYS A CD  1 
ATOM   1206 C CE  . LYS A 1 158 ? -25.671 -1.108  10.879  1.00 12.71 ? 158  LYS A CE  1 
ATOM   1207 N NZ  . LYS A 1 158 ? -26.808 -0.339  11.577  1.00 14.36 ? 158  LYS A NZ  1 
ATOM   1208 N N   . LEU A 1 159 ? -21.298 0.826   6.777   1.00 24.22 ? 159  LEU A N   1 
ATOM   1209 C CA  . LEU A 1 159 ? -21.628 1.239   5.431   1.00 25.50 ? 159  LEU A CA  1 
ATOM   1210 C C   . LEU A 1 159 ? -20.919 0.422   4.352   1.00 26.15 ? 159  LEU A C   1 
ATOM   1211 O O   . LEU A 1 159 ? -21.399 0.348   3.216   1.00 26.63 ? 159  LEU A O   1 
ATOM   1212 C CB  . LEU A 1 159 ? -21.296 2.714   5.216   1.00 26.40 ? 159  LEU A CB  1 
ATOM   1213 C CG  . LEU A 1 159 ? -22.201 3.850   5.719   1.00 28.53 ? 159  LEU A CG  1 
ATOM   1214 C CD1 . LEU A 1 159 ? -21.469 5.196   5.488   1.00 29.92 ? 159  LEU A CD1 1 
ATOM   1215 C CD2 . LEU A 1 159 ? -23.623 3.839   5.120   1.00 26.89 ? 159  LEU A CD2 1 
ATOM   1216 N N   . LYS A 1 160 ? -19.776 -0.175  4.650   1.00 26.08 ? 160  LYS A N   1 
ATOM   1217 C CA  . LYS A 1 160 ? -19.128 -0.940  3.592   1.00 27.00 ? 160  LYS A CA  1 
ATOM   1218 C C   . LYS A 1 160 ? -19.518 -2.409  3.620   1.00 26.94 ? 160  LYS A C   1 
ATOM   1219 O O   . LYS A 1 160 ? -18.958 -3.240  2.903   1.00 26.20 ? 160  LYS A O   1 
ATOM   1220 C CB  . LYS A 1 160 ? -17.613 -0.757  3.611   1.00 27.57 ? 160  LYS A CB  1 
ATOM   1221 C CG  . LYS A 1 160 ? -17.202 0.642   3.138   1.00 30.86 ? 160  LYS A CG  1 
ATOM   1222 C CD  . LYS A 1 160 ? -15.709 0.730   2.691   1.00 37.44 ? 160  LYS A CD  1 
ATOM   1223 C CE  . LYS A 1 160 ? -14.753 0.990   3.911   1.00 39.62 ? 160  LYS A CE  1 
ATOM   1224 N NZ  . LYS A 1 160 ? -14.430 -0.265  4.679   1.00 38.49 ? 160  LYS A NZ  1 
ATOM   1225 N N   . ASP A 1 161 ? -20.501 -2.730  4.451   1.00 26.76 ? 161  ASP A N   1 
ATOM   1226 C CA  . ASP A 1 161 ? -20.774 -4.110  4.714   1.00 26.47 ? 161  ASP A CA  1 
ATOM   1227 C C   . ASP A 1 161 ? -22.068 -4.547  3.992   1.00 27.13 ? 161  ASP A C   1 
ATOM   1228 O O   . ASP A 1 161 ? -23.194 -4.116  4.358   1.00 26.89 ? 161  ASP A O   1 
ATOM   1229 C CB  . ASP A 1 161 ? -20.799 -4.347  6.223   1.00 26.05 ? 161  ASP A CB  1 
ATOM   1230 C CG  . ASP A 1 161 ? -21.300 -5.731  6.584   1.00 24.44 ? 161  ASP A CG  1 
ATOM   1231 O OD1 . ASP A 1 161 ? -21.328 -6.615  5.690   1.00 26.66 ? 161  ASP A OD1 1 
ATOM   1232 O OD2 . ASP A 1 161 ? -21.693 -5.938  7.743   1.00 19.61 ? 161  ASP A OD2 1 
ATOM   1233 N N   . PRO A 1 162 ? -21.910 -5.421  2.977   1.00 27.06 ? 162  PRO A N   1 
ATOM   1234 C CA  . PRO A 1 162 ? -23.022 -5.810  2.136   1.00 26.93 ? 162  PRO A CA  1 
ATOM   1235 C C   . PRO A 1 162 ? -24.164 -6.461  2.951   1.00 27.46 ? 162  PRO A C   1 
ATOM   1236 O O   . PRO A 1 162 ? -25.318 -6.419  2.538   1.00 25.64 ? 162  PRO A O   1 
ATOM   1237 C CB  . PRO A 1 162 ? -22.377 -6.809  1.156   1.00 27.42 ? 162  PRO A CB  1 
ATOM   1238 C CG  . PRO A 1 162 ? -21.190 -7.362  1.870   1.00 26.38 ? 162  PRO A CG  1 
ATOM   1239 C CD  . PRO A 1 162 ? -20.682 -6.183  2.646   1.00 27.45 ? 162  PRO A CD  1 
ATOM   1240 N N   . ARG A 1 163 ? -23.845 -7.023  4.120   1.00 28.71 ? 163  ARG A N   1 
ATOM   1241 C CA  . ARG A 1 163 ? -24.884 -7.693  4.926   1.00 29.37 ? 163  ARG A CA  1 
ATOM   1242 C C   . ARG A 1 163 ? -25.603 -6.798  5.929   1.00 28.88 ? 163  ARG A C   1 
ATOM   1243 O O   . ARG A 1 163 ? -26.496 -7.253  6.634   1.00 28.55 ? 163  ARG A O   1 
ATOM   1244 C CB  . ARG A 1 163 ? -24.366 -8.977  5.567   1.00 29.84 ? 163  ARG A CB  1 
ATOM   1245 C CG  . ARG A 1 163 ? -23.709 -9.876  4.550   1.00 32.23 ? 163  ARG A CG  1 
ATOM   1246 C CD  . ARG A 1 163 ? -22.796 -10.892 5.172   1.00 36.04 ? 163  ARG A CD  1 
ATOM   1247 N NE  . ARG A 1 163 ? -21.539 -10.937 4.429   1.00 41.20 ? 163  ARG A NE  1 
ATOM   1248 C CZ  . ARG A 1 163 ? -21.357 -11.504 3.239   1.00 41.33 ? 163  ARG A CZ  1 
ATOM   1249 N NH1 . ARG A 1 163 ? -22.350 -12.106 2.619   1.00 42.23 ? 163  ARG A NH1 1 
ATOM   1250 N NH2 . ARG A 1 163 ? -20.163 -11.457 2.673   1.00 41.46 ? 163  ARG A NH2 1 
ATOM   1251 N N   . ALA A 1 164 ? -25.266 -5.515  5.944   1.00 28.73 ? 164  ALA A N   1 
ATOM   1252 C CA  . ALA A 1 164 ? -25.906 -4.582  6.880   1.00 29.39 ? 164  ALA A CA  1 
ATOM   1253 C C   . ALA A 1 164 ? -27.380 -4.292  6.567   1.00 29.85 ? 164  ALA A C   1 
ATOM   1254 O O   . ALA A 1 164 ? -27.749 -4.238  5.399   1.00 30.91 ? 164  ALA A O   1 
ATOM   1255 C CB  . ALA A 1 164 ? -25.129 -3.278  6.940   1.00 28.92 ? 164  ALA A CB  1 
ATOM   1256 N N   . GLN A 1 165 ? -28.206 -4.089  7.603   1.00 29.80 ? 165  GLN A N   1 
ATOM   1257 C CA  . GLN A 1 165 ? -29.521 -3.477  7.451   1.00 30.38 ? 165  GLN A CA  1 
ATOM   1258 C C   . GLN A 1 165 ? -29.330 -1.959  7.518   1.00 31.72 ? 165  GLN A C   1 
ATOM   1259 O O   . GLN A 1 165 ? -29.139 -1.404  8.601   1.00 32.00 ? 165  GLN A O   1 
ATOM   1260 C CB  . GLN A 1 165 ? -30.520 -3.976  8.519   1.00 30.08 ? 165  GLN A CB  1 
ATOM   1261 C CG  . GLN A 1 165 ? -31.884 -3.282  8.453   1.00 28.57 ? 165  GLN A CG  1 
ATOM   1262 C CD  . GLN A 1 165 ? -32.924 -3.888  9.372   1.00 29.74 ? 165  GLN A CD  1 
ATOM   1263 O OE1 . GLN A 1 165 ? -32.818 -5.036  9.825   1.00 31.74 ? 165  GLN A OE1 1 
ATOM   1264 N NE2 . GLN A 1 165 ? -33.958 -3.121  9.643   1.00 28.99 ? 165  GLN A NE2 1 
ATOM   1265 N N   . PRO A 1 166 ? -29.373 -1.275  6.351   1.00 32.88 ? 166  PRO A N   1 
ATOM   1266 C CA  . PRO A 1 166 ? -29.055 0.149   6.264   1.00 33.00 ? 166  PRO A CA  1 
ATOM   1267 C C   . PRO A 1 166 ? -30.252 1.011   6.652   1.00 33.32 ? 166  PRO A C   1 
ATOM   1268 O O   . PRO A 1 166 ? -31.368 0.488   6.816   1.00 32.84 ? 166  PRO A O   1 
ATOM   1269 C CB  . PRO A 1 166 ? -28.725 0.326   4.793   1.00 33.40 ? 166  PRO A CB  1 
ATOM   1270 C CG  . PRO A 1 166 ? -29.661 -0.632  4.114   1.00 33.48 ? 166  PRO A CG  1 
ATOM   1271 C CD  . PRO A 1 166 ? -29.800 -1.809  5.044   1.00 33.15 ? 166  PRO A CD  1 
ATOM   1272 N N   . GLY A 1 167 ? -30.006 2.308   6.842   1.00 33.45 ? 167  GLY A N   1 
ATOM   1273 C CA  . GLY A 1 167 ? -31.043 3.212   7.305   1.00 33.85 ? 167  GLY A CA  1 
ATOM   1274 C C   . GLY A 1 167 ? -31.624 2.972   8.693   1.00 34.02 ? 167  GLY A C   1 
ATOM   1275 O O   . GLY A 1 167 ? -32.795 3.321   8.949   1.00 34.46 ? 167  GLY A O   1 
ATOM   1276 N N   . GLN A 1 168 ? -30.820 2.381   9.587   1.00 33.34 ? 168  GLN A N   1 
ATOM   1277 C CA  . GLN A 1 168 ? -31.157 2.291   11.005  1.00 32.19 ? 168  GLN A CA  1 
ATOM   1278 C C   . GLN A 1 168 ? -30.655 3.583   11.652  1.00 31.33 ? 168  GLN A C   1 
ATOM   1279 O O   . GLN A 1 168 ? -29.865 4.314   11.034  1.00 31.70 ? 168  GLN A O   1 
ATOM   1280 C CB  . GLN A 1 168 ? -30.490 1.085   11.624  1.00 32.28 ? 168  GLN A CB  1 
ATOM   1281 C CG  . GLN A 1 168 ? -31.177 -0.220  11.282  1.00 33.09 ? 168  GLN A CG  1 
ATOM   1282 C CD  . GLN A 1 168 ? -30.509 -1.382  11.941  1.00 33.53 ? 168  GLN A CD  1 
ATOM   1283 O OE1 . GLN A 1 168 ? -29.295 -1.566  11.829  1.00 31.47 ? 168  GLN A OE1 1 
ATOM   1284 N NE2 . GLN A 1 168 ? -31.296 -2.194  12.630  1.00 33.49 ? 168  GLN A NE2 1 
ATOM   1285 N N   . SER A 1 169 ? -31.092 3.908   12.865  1.00 29.96 ? 169  SER A N   1 
ATOM   1286 C CA  . SER A 1 169 ? -30.521 5.113   13.479  1.00 29.08 ? 169  SER A CA  1 
ATOM   1287 C C   . SER A 1 169 ? -28.999 4.933   13.699  1.00 28.34 ? 169  SER A C   1 
ATOM   1288 O O   . SER A 1 169 ? -28.477 3.824   13.843  1.00 28.12 ? 169  SER A O   1 
ATOM   1289 C CB  . SER A 1 169 ? -31.241 5.539   14.743  1.00 27.98 ? 169  SER A CB  1 
ATOM   1290 O OG  . SER A 1 169 ? -31.356 4.445   15.580  1.00 28.83 ? 169  SER A OG  1 
ATOM   1291 N N   . SER A 1 170 ? -28.290 6.039   13.625  1.00 28.05 ? 170  SER A N   1 
ATOM   1292 C CA  . SER A 1 170 ? -26.922 6.111   14.104  1.00 28.35 ? 170  SER A CA  1 
ATOM   1293 C C   . SER A 1 170 ? -26.729 5.452   15.474  1.00 26.31 ? 170  SER A C   1 
ATOM   1294 O O   . SER A 1 170 ? -27.589 5.535   16.351  1.00 25.28 ? 170  SER A O   1 
ATOM   1295 C CB  . SER A 1 170 ? -26.502 7.588   14.235  1.00 28.98 ? 170  SER A CB  1 
ATOM   1296 O OG  . SER A 1 170 ? -25.762 7.987   13.097  1.00 33.87 ? 170  SER A OG  1 
ATOM   1297 N N   . PRO A 1 171 ? -25.584 4.806   15.657  1.00 25.61 ? 171  PRO A N   1 
ATOM   1298 C CA  . PRO A 1 171 ? -25.114 4.646   17.031  1.00 25.34 ? 171  PRO A CA  1 
ATOM   1299 C C   . PRO A 1 171 ? -24.628 6.021   17.540  1.00 25.20 ? 171  PRO A C   1 
ATOM   1300 O O   . PRO A 1 171 ? -24.093 6.811   16.767  1.00 25.44 ? 171  PRO A O   1 
ATOM   1301 C CB  . PRO A 1 171 ? -23.966 3.661   16.887  1.00 25.30 ? 171  PRO A CB  1 
ATOM   1302 C CG  . PRO A 1 171 ? -23.510 3.810   15.493  1.00 25.25 ? 171  PRO A CG  1 
ATOM   1303 C CD  . PRO A 1 171 ? -24.651 4.259   14.662  1.00 24.96 ? 171  PRO A CD  1 
ATOM   1304 N N   . LYS A 1 172 ? -24.838 6.325   18.816  1.00 25.58 ? 172  LYS A N   1 
ATOM   1305 C CA  . LYS A 1 172 ? -24.449 7.631   19.373  1.00 24.84 ? 172  LYS A CA  1 
ATOM   1306 C C   . LYS A 1 172 ? -24.082 7.413   20.830  1.00 24.90 ? 172  LYS A C   1 
ATOM   1307 O O   . LYS A 1 172 ? -24.249 6.300   21.343  1.00 25.46 ? 172  LYS A O   1 
ATOM   1308 C CB  . LYS A 1 172 ? -25.629 8.579   19.285  1.00 24.87 ? 172  LYS A CB  1 
ATOM   1309 C CG  . LYS A 1 172 ? -26.846 8.044   20.027  1.00 25.99 ? 172  LYS A CG  1 
ATOM   1310 C CD  . LYS A 1 172 ? -28.062 8.914   19.918  1.00 24.31 ? 172  LYS A CD  1 
ATOM   1311 C CE  . LYS A 1 172 ? -29.275 8.046   20.088  1.00 25.47 ? 172  LYS A CE  1 
ATOM   1312 N NZ  . LYS A 1 172 ? -30.365 8.956   20.333  1.00 29.63 ? 172  LYS A NZ  1 
ATOM   1313 N N   . ILE A 1 173 ? -23.586 8.457   21.507  1.00 24.15 ? 173  ILE A N   1 
ATOM   1314 C CA  . ILE A 1 173 ? -23.430 8.376   22.950  1.00 22.82 ? 173  ILE A CA  1 
ATOM   1315 C C   . ILE A 1 173 ? -24.752 8.621   23.718  1.00 23.81 ? 173  ILE A C   1 
ATOM   1316 O O   . ILE A 1 173 ? -25.186 9.749   23.939  1.00 24.31 ? 173  ILE A O   1 
ATOM   1317 C CB  . ILE A 1 173 ? -22.318 9.262   23.475  1.00 21.98 ? 173  ILE A CB  1 
ATOM   1318 C CG1 . ILE A 1 173 ? -21.023 8.923   22.776  1.00 18.97 ? 173  ILE A CG1 1 
ATOM   1319 C CG2 . ILE A 1 173 ? -22.120 8.977   24.948  1.00 21.28 ? 173  ILE A CG2 1 
ATOM   1320 C CD1 . ILE A 1 173 ? -19.936 9.895   23.087  1.00 18.94 ? 173  ILE A CD1 1 
ATOM   1321 N N   . ASP A 1 174 ? -25.367 7.538   24.137  1.00 24.11 ? 174  ASP A N   1 
ATOM   1322 C CA  . ASP A 1 174 ? -26.708 7.593   24.669  1.00 25.13 ? 174  ASP A CA  1 
ATOM   1323 C C   . ASP A 1 174 ? -26.792 8.261   26.016  1.00 25.63 ? 174  ASP A C   1 
ATOM   1324 O O   . ASP A 1 174 ? -27.850 8.754   26.415  1.00 26.48 ? 174  ASP A O   1 
ATOM   1325 C CB  . ASP A 1 174 ? -27.254 6.169   24.786  1.00 25.08 ? 174  ASP A CB  1 
ATOM   1326 C CG  . ASP A 1 174 ? -27.446 5.516   23.428  1.00 25.98 ? 174  ASP A CG  1 
ATOM   1327 O OD1 . ASP A 1 174 ? -28.486 5.780   22.804  1.00 29.06 ? 174  ASP A OD1 1 
ATOM   1328 O OD2 . ASP A 1 174 ? -26.562 4.774   22.972  1.00 23.88 ? 174  ASP A OD2 1 
ATOM   1329 N N   . VAL A 1 175 ? -25.685 8.250   26.740  1.00 25.74 ? 175  VAL A N   1 
ATOM   1330 C CA  . VAL A 1 175 ? -25.695 8.696   28.114  1.00 24.87 ? 175  VAL A CA  1 
ATOM   1331 C C   . VAL A 1 175 ? -24.282 9.118   28.348  1.00 25.06 ? 175  VAL A C   1 
ATOM   1332 O O   . VAL A 1 175 ? -23.358 8.308   28.204  1.00 24.94 ? 175  VAL A O   1 
ATOM   1333 C CB  . VAL A 1 175 ? -26.098 7.562   29.109  1.00 24.60 ? 175  VAL A CB  1 
ATOM   1334 C CG1 . VAL A 1 175 ? -25.851 7.977   30.534  1.00 23.06 ? 175  VAL A CG1 1 
ATOM   1335 C CG2 . VAL A 1 175 ? -27.558 7.154   28.943  1.00 24.69 ? 175  VAL A CG2 1 
ATOM   1336 N N   . VAL A 1 176 ? -24.108 10.403  28.643  1.00 25.71 ? 176  VAL A N   1 
ATOM   1337 C CA  . VAL A 1 176 ? -22.841 10.913  29.196  1.00 25.72 ? 176  VAL A CA  1 
ATOM   1338 C C   . VAL A 1 176 ? -23.005 10.876  30.707  1.00 25.94 ? 176  VAL A C   1 
ATOM   1339 O O   . VAL A 1 176 ? -23.919 11.537  31.243  1.00 26.44 ? 176  VAL A O   1 
ATOM   1340 C CB  . VAL A 1 176 ? -22.572 12.340  28.770  1.00 25.83 ? 176  VAL A CB  1 
ATOM   1341 C CG1 . VAL A 1 176 ? -21.259 12.844  29.389  1.00 27.27 ? 176  VAL A CG1 1 
ATOM   1342 C CG2 . VAL A 1 176 ? -22.501 12.423  27.262  1.00 25.24 ? 176  VAL A CG2 1 
ATOM   1343 N N   . ILE A 1 177 ? -22.173 10.075  31.387  1.00 24.85 ? 177  ILE A N   1 
ATOM   1344 C CA  . ILE A 1 177 ? -22.223 10.006  32.855  1.00 23.76 ? 177  ILE A CA  1 
ATOM   1345 C C   . ILE A 1 177 ? -21.265 11.029  33.464  1.00 23.50 ? 177  ILE A C   1 
ATOM   1346 O O   . ILE A 1 177 ? -20.079 11.006  33.181  1.00 23.51 ? 177  ILE A O   1 
ATOM   1347 C CB  . ILE A 1 177 ? -21.821 8.616   33.430  1.00 23.30 ? 177  ILE A CB  1 
ATOM   1348 C CG1 . ILE A 1 177 ? -22.603 7.495   32.773  1.00 21.48 ? 177  ILE A CG1 1 
ATOM   1349 C CG2 . ILE A 1 177 ? -22.036 8.599   34.928  1.00 21.46 ? 177  ILE A CG2 1 
ATOM   1350 C CD1 . ILE A 1 177 ? -22.383 6.135   33.431  1.00 21.49 ? 177  ILE A CD1 1 
ATOM   1351 N N   . SER A 1 178 ? -21.791 11.868  34.338  1.00 23.38 ? 178  SER A N   1 
ATOM   1352 C CA  . SER A 1 178 ? -21.035 12.908  34.991  1.00 23.97 ? 178  SER A CA  1 
ATOM   1353 C C   . SER A 1 178 ? -19.883 12.448  35.909  1.00 24.40 ? 178  SER A C   1 
ATOM   1354 O O   . SER A 1 178 ? -20.027 11.470  36.667  1.00 23.66 ? 178  SER A O   1 
ATOM   1355 C CB  . SER A 1 178 ? -21.981 13.804  35.804  1.00 23.47 ? 178  SER A CB  1 
ATOM   1356 O OG  . SER A 1 178 ? -21.209 14.842  36.382  1.00 24.68 ? 178  SER A OG  1 
ATOM   1357 N N   . GLU A 1 179 ? -18.779 13.205  35.857  1.00 24.30 ? 179  GLU A N   1 
ATOM   1358 C CA  . GLU A 1 179 ? -17.658 13.062  36.786  1.00 24.98 ? 179  GLU A CA  1 
ATOM   1359 C C   . GLU A 1 179 ? -17.670 14.031  37.982  1.00 25.36 ? 179  GLU A C   1 
ATOM   1360 O O   . GLU A 1 179 ? -16.727 14.025  38.776  1.00 24.70 ? 179  GLU A O   1 
ATOM   1361 C CB  . GLU A 1 179 ? -16.317 13.199  36.036  1.00 25.45 ? 179  GLU A CB  1 
ATOM   1362 C CG  . GLU A 1 179 ? -16.197 12.204  34.889  1.00 27.38 ? 179  GLU A CG  1 
ATOM   1363 C CD  . GLU A 1 179 ? -14.805 12.067  34.266  1.00 30.02 ? 179  GLU A CD  1 
ATOM   1364 O OE1 . GLU A 1 179 ? -13.917 12.927  34.489  1.00 30.24 ? 179  GLU A OE1 1 
ATOM   1365 O OE2 . GLU A 1 179 ? -14.615 11.073  33.526  1.00 32.49 ? 179  GLU A OE2 1 
ATOM   1366 N N   . ALA A 1 180 ? -18.711 14.872  38.127  1.00 26.21 ? 180  ALA A N   1 
ATOM   1367 C CA  . ALA A 1 180 ? -18.767 15.790  39.287  1.00 26.51 ? 180  ALA A CA  1 
ATOM   1368 C C   . ALA A 1 180 ? -18.652 14.954  40.542  1.00 27.54 ? 180  ALA A C   1 
ATOM   1369 O O   . ALA A 1 180 ? -19.077 13.775  40.596  1.00 27.31 ? 180  ALA A O   1 
ATOM   1370 C CB  . ALA A 1 180 ? -20.015 16.631  39.327  1.00 25.99 ? 180  ALA A CB  1 
ATOM   1371 N N   . SER A 1 181 ? -18.051 15.579  41.547  1.00 28.26 ? 181  SER A N   1 
ATOM   1372 C CA  . SER A 1 181 ? -17.660 14.899  42.767  1.00 28.42 ? 181  SER A CA  1 
ATOM   1373 C C   . SER A 1 181 ? -18.851 14.247  43.441  1.00 27.74 ? 181  SER A C   1 
ATOM   1374 O O   . SER A 1 181 ? -18.655 13.336  44.230  1.00 28.66 ? 181  SER A O   1 
ATOM   1375 C CB  . SER A 1 181 ? -16.934 15.868  43.724  1.00 28.66 ? 181  SER A CB  1 
ATOM   1376 O OG  . SER A 1 181 ? -17.542 17.166  43.667  1.00 29.43 ? 181  SER A OG  1 
ATOM   1377 N N   . SER A 1 182 ? -20.069 14.699  43.135  1.00 27.19 ? 182  SER A N   1 
ATOM   1378 C CA  . SER A 1 182 ? -21.270 14.102  43.735  1.00 26.78 ? 182  SER A CA  1 
ATOM   1379 C C   . SER A 1 182 ? -22.066 13.143  42.811  1.00 26.07 ? 182  SER A C   1 
ATOM   1380 O O   . SER A 1 182 ? -23.176 12.674  43.187  1.00 26.14 ? 182  SER A O   1 
ATOM   1381 C CB  . SER A 1 182 ? -22.205 15.187  44.194  1.00 27.25 ? 182  SER A CB  1 
ATOM   1382 O OG  . SER A 1 182 ? -22.847 15.748  43.069  1.00 28.79 ? 182  SER A OG  1 
ATOM   1383 N N   . SER A 1 183 ? -21.527 12.874  41.618  1.00 24.25 ? 183  SER A N   1 
ATOM   1384 C CA  . SER A 1 183 ? -22.182 11.984  40.667  1.00 23.17 ? 183  SER A CA  1 
ATOM   1385 C C   . SER A 1 183 ? -21.881 10.507  40.947  1.00 22.29 ? 183  SER A C   1 
ATOM   1386 O O   . SER A 1 183 ? -20.715 10.085  40.990  1.00 22.77 ? 183  SER A O   1 
ATOM   1387 C CB  . SER A 1 183 ? -21.737 12.333  39.243  1.00 24.06 ? 183  SER A CB  1 
ATOM   1388 O OG  . SER A 1 183 ? -22.300 11.465  38.262  1.00 22.28 ? 183  SER A OG  1 
ATOM   1389 N N   . ASN A 1 184 ? -22.927 9.717   41.144  1.00 20.44 ? 184  ASN A N   1 
ATOM   1390 C CA  . ASN A 1 184 ? -22.766 8.272   41.146  1.00 18.98 ? 184  ASN A CA  1 
ATOM   1391 C C   . ASN A 1 184 ? -22.369 7.860   39.741  1.00 17.78 ? 184  ASN A C   1 
ATOM   1392 O O   . ASN A 1 184 ? -23.187 7.862   38.871  1.00 18.14 ? 184  ASN A O   1 
ATOM   1393 C CB  . ASN A 1 184 ? -24.058 7.565   41.646  1.00 19.12 ? 184  ASN A CB  1 
ATOM   1394 C CG  . ASN A 1 184 ? -24.377 7.890   43.115  1.00 19.34 ? 184  ASN A CG  1 
ATOM   1395 O OD1 . ASN A 1 184 ? -23.555 8.486   43.810  1.00 21.99 ? 184  ASN A OD1 1 
ATOM   1396 N ND2 . ASN A 1 184 ? -25.561 7.484   43.597  1.00 19.96 ? 184  ASN A ND2 1 
ATOM   1397 N N   . ASN A 1 185 ? -21.103 7.530   39.531  1.00 17.33 ? 185  ASN A N   1 
ATOM   1398 C CA  . ASN A 1 185 ? -20.542 7.218   38.214  1.00 16.83 ? 185  ASN A CA  1 
ATOM   1399 C C   . ASN A 1 185 ? -19.877 5.818   38.173  1.00 17.00 ? 185  ASN A C   1 
ATOM   1400 O O   . ASN A 1 185 ? -18.773 5.664   38.714  1.00 16.61 ? 185  ASN A O   1 
ATOM   1401 C CB  . ASN A 1 185 ? -19.480 8.260   37.864  1.00 15.94 ? 185  ASN A CB  1 
ATOM   1402 C CG  . ASN A 1 185 ? -18.778 7.986   36.507  1.00 17.36 ? 185  ASN A CG  1 
ATOM   1403 O OD1 . ASN A 1 185 ? -18.211 8.893   35.899  1.00 18.24 ? 185  ASN A OD1 1 
ATOM   1404 N ND2 . ASN A 1 185 ? -18.856 6.763   36.022  1.00 19.00 ? 185  ASN A ND2 1 
ATOM   1405 N N   . THR A 1 186 ? -20.490 4.821   37.515  1.00 16.69 ? 186  THR A N   1 
ATOM   1406 C CA  . THR A 1 186 ? -20.011 3.438   37.675  1.00 17.38 ? 186  THR A CA  1 
ATOM   1407 C C   . THR A 1 186 ? -18.779 3.135   36.843  1.00 18.15 ? 186  THR A C   1 
ATOM   1408 O O   . THR A 1 186 ? -18.133 2.099   37.035  1.00 18.27 ? 186  THR A O   1 
ATOM   1409 C CB  . THR A 1 186 ? -21.042 2.354   37.318  1.00 17.04 ? 186  THR A CB  1 
ATOM   1410 O OG1 . THR A 1 186 ? -21.410 2.468   35.924  1.00 19.10 ? 186  THR A OG1 1 
ATOM   1411 C CG2 . THR A 1 186 ? -22.266 2.436   38.189  1.00 15.84 ? 186  THR A CG2 1 
ATOM   1412 N N   . LEU A 1 187 ? -18.497 4.019   35.900  1.00 19.14 ? 187  LEU A N   1 
ATOM   1413 C CA  . LEU A 1 187 ? -17.394 3.895   34.957  1.00 20.40 ? 187  LEU A CA  1 
ATOM   1414 C C   . LEU A 1 187 ? -16.094 4.271   35.636  1.00 20.86 ? 187  LEU A C   1 
ATOM   1415 O O   . LEU A 1 187 ? -15.007 3.816   35.208  1.00 20.76 ? 187  LEU A O   1 
ATOM   1416 C CB  . LEU A 1 187 ? -17.617 4.799   33.708  1.00 19.95 ? 187  LEU A CB  1 
ATOM   1417 C CG  . LEU A 1 187 ? -18.882 4.504   32.861  1.00 21.15 ? 187  LEU A CG  1 
ATOM   1418 C CD1 . LEU A 1 187 ? -19.039 5.372   31.591  1.00 18.17 ? 187  LEU A CD1 1 
ATOM   1419 C CD2 . LEU A 1 187 ? -18.977 3.041   32.474  1.00 18.32 ? 187  LEU A CD2 1 
ATOM   1420 N N   . ASP A 1 188 ? -16.193 5.117   36.671  1.00 21.10 ? 188  ASP A N   1 
ATOM   1421 C CA  . ASP A 1 188 ? -14.986 5.596   37.404  1.00 22.43 ? 188  ASP A CA  1 
ATOM   1422 C C   . ASP A 1 188 ? -15.439 6.391   38.636  1.00 21.54 ? 188  ASP A C   1 
ATOM   1423 O O   . ASP A 1 188 ? -15.442 7.634   38.620  1.00 21.14 ? 188  ASP A O   1 
ATOM   1424 C CB  . ASP A 1 188 ? -14.053 6.390   36.477  1.00 22.91 ? 188  ASP A CB  1 
ATOM   1425 C CG  . ASP A 1 188 ? -12.771 6.883   37.175  1.00 27.62 ? 188  ASP A CG  1 
ATOM   1426 O OD1 . ASP A 1 188 ? -11.691 6.247   37.055  1.00 30.03 ? 188  ASP A OD1 1 
ATOM   1427 O OD2 . ASP A 1 188 ? -12.828 7.958   37.807  1.00 35.74 ? 188  ASP A OD2 1 
ATOM   1428 N N   . PRO A 1 189 ? -15.878 5.660   39.685  1.00 20.85 ? 189  PRO A N   1 
ATOM   1429 C CA  . PRO A 1 189 ? -16.619 6.261   40.787  1.00 20.73 ? 189  PRO A CA  1 
ATOM   1430 C C   . PRO A 1 189 ? -15.792 7.272   41.549  1.00 21.11 ? 189  PRO A C   1 
ATOM   1431 O O   . PRO A 1 189 ? -14.563 7.119   41.679  1.00 19.73 ? 189  PRO A O   1 
ATOM   1432 C CB  . PRO A 1 189 ? -16.960 5.064   41.678  1.00 20.16 ? 189  PRO A CB  1 
ATOM   1433 C CG  . PRO A 1 189 ? -16.822 3.894   40.822  1.00 19.44 ? 189  PRO A CG  1 
ATOM   1434 C CD  . PRO A 1 189 ? -15.752 4.198   39.865  1.00 20.04 ? 189  PRO A CD  1 
ATOM   1435 N N   . GLY A 1 190 ? -16.466 8.303   42.042  1.00 21.59 ? 190  GLY A N   1 
ATOM   1436 C CA  . GLY A 1 190 ? -15.748 9.381   42.700  1.00 23.38 ? 190  GLY A CA  1 
ATOM   1437 C C   . GLY A 1 190 ? -16.271 9.695   44.081  1.00 24.21 ? 190  GLY A C   1 
ATOM   1438 O O   . GLY A 1 190 ? -15.920 10.733  44.656  1.00 24.54 ? 190  GLY A O   1 
ATOM   1439 N N   . THR A 1 191 ? -17.109 8.810   44.611  1.00 24.70 ? 191  THR A N   1 
ATOM   1440 C CA  . THR A 1 191 ? -17.855 9.142   45.823  1.00 25.88 ? 191  THR A CA  1 
ATOM   1441 C C   . THR A 1 191 ? -17.389 8.420   47.068  1.00 25.98 ? 191  THR A C   1 
ATOM   1442 O O   . THR A 1 191 ? -17.869 8.714   48.129  1.00 26.73 ? 191  THR A O   1 
ATOM   1443 C CB  . THR A 1 191 ? -19.393 8.936   45.658  1.00 25.82 ? 191  THR A CB  1 
ATOM   1444 O OG1 . THR A 1 191 ? -19.662 7.798   44.817  1.00 26.09 ? 191  THR A OG1 1 
ATOM   1445 C CG2 . THR A 1 191 ? -20.004 10.139  45.044  1.00 26.09 ? 191  THR A CG2 1 
ATOM   1446 N N   . CYS A 1 192 ? -16.480 7.470   46.934  1.00 26.46 ? 192  CYS A N   1 
ATOM   1447 C CA  . CYS A 1 192 ? -16.016 6.680   48.068  1.00 27.52 ? 192  CYS A CA  1 
ATOM   1448 C C   . CYS A 1 192 ? -14.938 7.452   48.825  1.00 27.98 ? 192  CYS A C   1 
ATOM   1449 O O   . CYS A 1 192 ? -13.739 7.280   48.589  1.00 27.65 ? 192  CYS A O   1 
ATOM   1450 C CB  . CYS A 1 192 ? -15.466 5.352   47.566  1.00 27.68 ? 192  CYS A CB  1 
ATOM   1451 S SG  . CYS A 1 192 ? -15.011 4.142   48.806  1.00 30.02 ? 192  CYS A SG  1 
ATOM   1452 N N   . THR A 1 193 ? -15.383 8.312   49.732  1.00 28.58 ? 193  THR A N   1 
ATOM   1453 C CA  . THR A 1 193 ? -14.513 9.264   50.465  1.00 29.33 ? 193  THR A CA  1 
ATOM   1454 C C   . THR A 1 193 ? -13.186 8.670   51.001  1.00 28.35 ? 193  THR A C   1 
ATOM   1455 O O   . THR A 1 193 ? -12.119 9.221   50.783  1.00 28.28 ? 193  THR A O   1 
ATOM   1456 C CB  . THR A 1 193 ? -15.301 9.872   51.662  1.00 29.94 ? 193  THR A CB  1 
ATOM   1457 O OG1 . THR A 1 193 ? -16.684 10.034  51.301  1.00 30.73 ? 193  THR A OG1 1 
ATOM   1458 C CG2 . THR A 1 193 ? -14.700 11.205  52.096  1.00 31.92 ? 193  THR A CG2 1 
ATOM   1459 N N   . VAL A 1 194 ? -13.265 7.538   51.699  1.00 28.21 ? 194  VAL A N   1 
ATOM   1460 C CA  . VAL A 1 194 ? -12.081 6.923   52.292  1.00 27.34 ? 194  VAL A CA  1 
ATOM   1461 C C   . VAL A 1 194 ? -11.089 6.511   51.181  1.00 28.06 ? 194  VAL A C   1 
ATOM   1462 O O   . VAL A 1 194 ? -9.866  6.736   51.329  1.00 28.10 ? 194  VAL A O   1 
ATOM   1463 C CB  . VAL A 1 194 ? -12.429 5.783   53.288  1.00 27.08 ? 194  VAL A CB  1 
ATOM   1464 C CG1 . VAL A 1 194 ? -11.160 5.096   53.808  1.00 26.72 ? 194  VAL A CG1 1 
ATOM   1465 C CG2 . VAL A 1 194 ? -13.275 6.334   54.472  1.00 26.24 ? 194  VAL A CG2 1 
ATOM   1466 N N   . PHE A 1 195 ? -11.615 5.964   50.065  1.00 27.38 ? 195  PHE A N   1 
ATOM   1467 C CA  . PHE A 1 195 ? -10.777 5.580   48.918  1.00 26.63 ? 195  PHE A CA  1 
ATOM   1468 C C   . PHE A 1 195 ? -10.162 6.804   48.232  1.00 27.97 ? 195  PHE A C   1 
ATOM   1469 O O   . PHE A 1 195 ? -8.985  6.812   47.849  1.00 27.69 ? 195  PHE A O   1 
ATOM   1470 C CB  . PHE A 1 195 ? -11.544 4.712   47.897  1.00 25.85 ? 195  PHE A CB  1 
ATOM   1471 C CG  . PHE A 1 195 ? -10.791 4.487   46.615  1.00 20.94 ? 195  PHE A CG  1 
ATOM   1472 C CD1 . PHE A 1 195 ? -9.771  3.526   46.545  1.00 19.76 ? 195  PHE A CD1 1 
ATOM   1473 C CD2 . PHE A 1 195 ? -11.029 5.285   45.505  1.00 16.69 ? 195  PHE A CD2 1 
ATOM   1474 C CE1 . PHE A 1 195 ? -9.020  3.327   45.343  1.00 13.89 ? 195  PHE A CE1 1 
ATOM   1475 C CE2 . PHE A 1 195 ? -10.292 5.097   44.331  1.00 12.91 ? 195  PHE A CE2 1 
ATOM   1476 C CZ  . PHE A 1 195 ? -9.286  4.109   44.262  1.00 10.03 ? 195  PHE A CZ  1 
ATOM   1477 N N   . GLU A 1 196 ? -10.954 7.847   48.083  1.00 29.29 ? 196  GLU A N   1 
ATOM   1478 C CA  . GLU A 1 196 ? -10.435 9.053   47.450  1.00 31.26 ? 196  GLU A CA  1 
ATOM   1479 C C   . GLU A 1 196 ? -9.202  9.605   48.214  1.00 32.28 ? 196  GLU A C   1 
ATOM   1480 O O   . GLU A 1 196 ? -8.306  10.213  47.600  1.00 32.37 ? 196  GLU A O   1 
ATOM   1481 C CB  . GLU A 1 196 ? -11.567 10.115  47.285  1.00 31.45 ? 196  GLU A CB  1 
ATOM   1482 C CG  . GLU A 1 196 ? -12.591 9.815   46.129  1.00 30.85 ? 196  GLU A CG  1 
ATOM   1483 C CD  . GLU A 1 196 ? -11.910 9.441   44.796  1.00 32.20 ? 196  GLU A CD  1 
ATOM   1484 O OE1 . GLU A 1 196 ? -10.900 10.102  44.460  1.00 31.72 ? 196  GLU A OE1 1 
ATOM   1485 O OE2 . GLU A 1 196 ? -12.376 8.489   44.095  1.00 30.73 ? 196  GLU A OE2 1 
ATOM   1486 N N   . ASP A 1 197 ? -9.168  9.363   49.534  1.00 32.25 ? 197  ASP A N   1 
ATOM   1487 C CA  . ASP A 1 197 ? -8.132  9.891   50.421  1.00 32.75 ? 197  ASP A CA  1 
ATOM   1488 C C   . ASP A 1 197 ? -6.875  8.977   50.495  1.00 33.34 ? 197  ASP A C   1 
ATOM   1489 O O   . ASP A 1 197 ? -5.776  9.455   50.820  1.00 33.84 ? 197  ASP A O   1 
ATOM   1490 C CB  . ASP A 1 197 ? -8.715  10.100  51.837  1.00 33.19 ? 197  ASP A CB  1 
ATOM   1491 C CG  . ASP A 1 197 ? -9.554  11.410  51.997  1.00 32.11 ? 197  ASP A CG  1 
ATOM   1492 O OD1 . ASP A 1 197 ? -9.738  12.207  51.072  1.00 32.30 ? 197  ASP A OD1 1 
ATOM   1493 O OD2 . ASP A 1 197 ? -10.047 11.639  53.103  1.00 31.74 ? 197  ASP A OD2 1 
ATOM   1494 N N   . SER A 1 198 ? -7.039  7.683   50.192  1.00 32.96 ? 198  SER A N   1 
ATOM   1495 C CA  . SER A 1 198 ? -5.948  6.694   50.265  1.00 32.91 ? 198  SER A CA  1 
ATOM   1496 C C   . SER A 1 198 ? -4.610  7.199   49.709  1.00 33.49 ? 198  SER A C   1 
ATOM   1497 O O   . SER A 1 198 ? -4.579  7.900   48.697  1.00 33.60 ? 198  SER A O   1 
ATOM   1498 C CB  . SER A 1 198 ? -6.330  5.382   49.555  1.00 32.60 ? 198  SER A CB  1 
ATOM   1499 O OG  . SER A 1 198 ? -5.231  4.482   49.480  1.00 30.14 ? 198  SER A OG  1 
ATOM   1500 N N   . GLU A 1 199 ? -3.513  6.802   50.355  1.00 33.74 ? 199  GLU A N   1 
ATOM   1501 C CA  . GLU A 1 199 ? -2.171  7.206   49.934  1.00 34.28 ? 199  GLU A CA  1 
ATOM   1502 C C   . GLU A 1 199 ? -1.237  5.999   49.794  1.00 33.03 ? 199  GLU A C   1 
ATOM   1503 O O   . GLU A 1 199 ? -0.036  6.173   49.660  1.00 33.81 ? 199  GLU A O   1 
ATOM   1504 C CB  . GLU A 1 199 ? -1.593  8.273   50.900  1.00 35.32 ? 199  GLU A CB  1 
ATOM   1505 C CG  . GLU A 1 199 ? -2.504  9.537   51.076  1.00 39.32 ? 199  GLU A CG  1 
ATOM   1506 C CD  . GLU A 1 199 ? -1.979  10.581  52.107  1.00 46.44 ? 199  GLU A CD  1 
ATOM   1507 O OE1 . GLU A 1 199 ? -1.769  10.215  53.302  1.00 47.45 ? 199  GLU A OE1 1 
ATOM   1508 O OE2 . GLU A 1 199 ? -1.807  11.778  51.720  1.00 47.10 ? 199  GLU A OE2 1 
ATOM   1509 N N   . LEU A 1 200 ? -1.800  4.786   49.805  1.00 32.22 ? 200  LEU A N   1 
ATOM   1510 C CA  . LEU A 1 200 ? -1.047  3.518   49.676  1.00 30.69 ? 200  LEU A CA  1 
ATOM   1511 C C   . LEU A 1 200 ? -0.202  3.450   48.383  1.00 30.72 ? 200  LEU A C   1 
ATOM   1512 O O   . LEU A 1 200 ? 0.988   3.110   48.428  1.00 30.60 ? 200  LEU A O   1 
ATOM   1513 C CB  . LEU A 1 200 ? -1.986  2.317   49.811  1.00 30.17 ? 200  LEU A CB  1 
ATOM   1514 C CG  . LEU A 1 200 ? -1.504  0.861   49.679  1.00 30.60 ? 200  LEU A CG  1 
ATOM   1515 C CD1 . LEU A 1 200 ? -0.309  0.473   50.615  1.00 28.57 ? 200  LEU A CD1 1 
ATOM   1516 C CD2 . LEU A 1 200 ? -2.674  -0.042  49.948  1.00 27.75 ? 200  LEU A CD2 1 
ATOM   1517 N N   . ALA A 1 201 ? -0.801  3.827   47.255  1.00 29.98 ? 201  ALA A N   1 
ATOM   1518 C CA  . ALA A 1 201 ? -0.097  3.880   45.964  1.00 30.01 ? 201  ALA A CA  1 
ATOM   1519 C C   . ALA A 1 201 ? 1.195   4.706   45.979  1.00 29.91 ? 201  ALA A C   1 
ATOM   1520 O O   . ALA A 1 201 ? 2.246   4.206   45.574  1.00 28.97 ? 201  ALA A O   1 
ATOM   1521 C CB  . ALA A 1 201 ? -1.052  4.345   44.818  1.00 29.63 ? 201  ALA A CB  1 
ATOM   1522 N N   . ASP A 1 202 ? 1.096   5.962   46.436  1.00 30.62 ? 202  ASP A N   1 
ATOM   1523 C CA  . ASP A 1 202 ? 2.252   6.831   46.679  1.00 31.28 ? 202  ASP A CA  1 
ATOM   1524 C C   . ASP A 1 202 ? 3.341   6.136   47.486  1.00 31.37 ? 202  ASP A C   1 
ATOM   1525 O O   . ASP A 1 202 ? 4.531   6.156   47.123  1.00 31.07 ? 202  ASP A O   1 
ATOM   1526 C CB  . ASP A 1 202 ? 1.835   8.083   47.426  1.00 31.77 ? 202  ASP A CB  1 
ATOM   1527 C CG  . ASP A 1 202 ? 1.092   9.072   46.549  1.00 34.54 ? 202  ASP A CG  1 
ATOM   1528 O OD1 . ASP A 1 202 ? 1.269   9.027   45.315  1.00 37.49 ? 202  ASP A OD1 1 
ATOM   1529 O OD2 . ASP A 1 202 ? 0.331   9.910   47.098  1.00 38.54 ? 202  ASP A OD2 1 
ATOM   1530 N N   . THR A 1 203 ? 2.949   5.507   48.584  1.00 31.58 ? 203  THR A N   1 
ATOM   1531 C CA  . THR A 1 203 ? 3.961   4.873   49.406  1.00 31.43 ? 203  THR A CA  1 
ATOM   1532 C C   . THR A 1 203 ? 4.720   3.863   48.566  1.00 31.52 ? 203  THR A C   1 
ATOM   1533 O O   . THR A 1 203 ? 5.952   3.980   48.430  1.00 31.99 ? 203  THR A O   1 
ATOM   1534 C CB  . THR A 1 203 ? 3.370   4.342   50.685  1.00 31.06 ? 203  THR A CB  1 
ATOM   1535 O OG1 . THR A 1 203 ? 2.811   5.469   51.372  1.00 31.35 ? 203  THR A OG1 1 
ATOM   1536 C CG2 . THR A 1 203 ? 4.458   3.756   51.577  1.00 32.03 ? 203  THR A CG2 1 
ATOM   1537 N N   . VAL A 1 204 ? 3.993   2.940   47.928  1.00 31.25 ? 204  VAL A N   1 
ATOM   1538 C CA  . VAL A 1 204 ? 4.619   1.937   47.061  1.00 30.89 ? 204  VAL A CA  1 
ATOM   1539 C C   . VAL A 1 204 ? 5.460   2.548   45.917  1.00 30.10 ? 204  VAL A C   1 
ATOM   1540 O O   . VAL A 1 204 ? 6.510   2.038   45.568  1.00 29.58 ? 204  VAL A O   1 
ATOM   1541 C CB  . VAL A 1 204 ? 3.587   0.994   46.452  1.00 31.22 ? 204  VAL A CB  1 
ATOM   1542 C CG1 . VAL A 1 204 ? 4.310   -0.121  45.702  1.00 31.22 ? 204  VAL A CG1 1 
ATOM   1543 C CG2 . VAL A 1 204 ? 2.659   0.447   47.527  1.00 30.57 ? 204  VAL A CG2 1 
ATOM   1544 N N   . GLU A 1 205 ? 4.975   3.641   45.346  1.00 29.84 ? 205  GLU A N   1 
ATOM   1545 C CA  . GLU A 1 205 ? 5.652   4.287   44.245  1.00 29.16 ? 205  GLU A CA  1 
ATOM   1546 C C   . GLU A 1 205 ? 7.014   4.769   44.719  1.00 29.34 ? 205  GLU A C   1 
ATOM   1547 O O   . GLU A 1 205 ? 8.023   4.480   44.076  1.00 29.32 ? 205  GLU A O   1 
ATOM   1548 C CB  . GLU A 1 205 ? 4.844   5.458   43.679  1.00 28.86 ? 205  GLU A CB  1 
ATOM   1549 C CG  . GLU A 1 205 ? 5.575   6.189   42.497  1.00 29.13 ? 205  GLU A CG  1 
ATOM   1550 C CD  . GLU A 1 205 ? 4.769   7.307   41.802  1.00 29.15 ? 205  GLU A CD  1 
ATOM   1551 O OE1 . GLU A 1 205 ? 3.627   7.636   42.217  1.00 30.55 ? 205  GLU A OE1 1 
ATOM   1552 O OE2 . GLU A 1 205 ? 5.286   7.848   40.810  1.00 30.78 ? 205  GLU A OE2 1 
ATOM   1553 N N   . ALA A 1 206 ? 7.041   5.499   45.837  1.00 29.25 ? 206  ALA A N   1 
ATOM   1554 C CA  . ALA A 1 206 ? 8.289   5.990   46.434  1.00 28.92 ? 206  ALA A CA  1 
ATOM   1555 C C   . ALA A 1 206 ? 9.189   4.837   46.843  1.00 28.82 ? 206  ALA A C   1 
ATOM   1556 O O   . ALA A 1 206 ? 10.363  4.794   46.455  1.00 28.47 ? 206  ALA A O   1 
ATOM   1557 C CB  . ALA A 1 206 ? 8.014   6.905   47.631  1.00 28.50 ? 206  ALA A CB  1 
ATOM   1558 N N   . ASN A 1 207 ? 8.646   3.880   47.594  1.00 29.01 ? 207  ASN A N   1 
ATOM   1559 C CA  . ASN A 1 207 ? 9.473   2.746   47.993  1.00 29.73 ? 207  ASN A CA  1 
ATOM   1560 C C   . ASN A 1 207 ? 10.127  2.014   46.811  1.00 29.54 ? 207  ASN A C   1 
ATOM   1561 O O   . ASN A 1 207 ? 11.339  1.777   46.833  1.00 29.70 ? 207  ASN A O   1 
ATOM   1562 C CB  . ASN A 1 207 ? 8.742   1.800   48.949  1.00 30.33 ? 207  ASN A CB  1 
ATOM   1563 C CG  . ASN A 1 207 ? 8.520   2.410   50.367  1.00 33.05 ? 207  ASN A CG  1 
ATOM   1564 O OD1 . ASN A 1 207 ? 8.598   3.636   50.579  1.00 34.41 ? 207  ASN A OD1 1 
ATOM   1565 N ND2 . ASN A 1 207 ? 8.223   1.540   51.332  1.00 33.19 ? 207  ASN A ND2 1 
ATOM   1566 N N   . PHE A 1 208 ? 9.358   1.706   45.760  1.00 29.69 ? 208  PHE A N   1 
ATOM   1567 C CA  . PHE A 1 208 ? 9.919   0.931   44.636  1.00 29.17 ? 208  PHE A CA  1 
ATOM   1568 C C   . PHE A 1 208 ? 10.788  1.757   43.735  1.00 29.46 ? 208  PHE A C   1 
ATOM   1569 O O   . PHE A 1 208 ? 11.694  1.204   43.135  1.00 29.19 ? 208  PHE A O   1 
ATOM   1570 C CB  . PHE A 1 208 ? 8.862   0.175   43.810  1.00 29.06 ? 208  PHE A CB  1 
ATOM   1571 C CG  . PHE A 1 208 ? 9.445   -0.620  42.625  1.00 28.42 ? 208  PHE A CG  1 
ATOM   1572 C CD1 . PHE A 1 208 ? 10.051  -1.880  42.821  1.00 29.39 ? 208  PHE A CD1 1 
ATOM   1573 C CD2 . PHE A 1 208 ? 9.364   -0.126  41.320  1.00 27.28 ? 208  PHE A CD2 1 
ATOM   1574 C CE1 . PHE A 1 208 ? 10.592  -2.613  41.737  1.00 27.65 ? 208  PHE A CE1 1 
ATOM   1575 C CE2 . PHE A 1 208 ? 9.892   -0.845  40.229  1.00 25.92 ? 208  PHE A CE2 1 
ATOM   1576 C CZ  . PHE A 1 208 ? 10.501  -2.089  40.438  1.00 27.46 ? 208  PHE A CZ  1 
ATOM   1577 N N   . THR A 1 209 ? 10.543  3.064   43.648  1.00 29.76 ? 209  THR A N   1 
ATOM   1578 C CA  . THR A 1 209 ? 11.430  3.905   42.851  1.00 31.64 ? 209  THR A CA  1 
ATOM   1579 C C   . THR A 1 209 ? 12.815  4.093   43.486  1.00 32.27 ? 209  THR A C   1 
ATOM   1580 O O   . THR A 1 209 ? 13.788  4.443   42.793  1.00 33.07 ? 209  THR A O   1 
ATOM   1581 C CB  . THR A 1 209 ? 10.879  5.302   42.579  1.00 31.25 ? 209  THR A CB  1 
ATOM   1582 O OG1 . THR A 1 209 ? 10.557  5.910   43.816  1.00 35.07 ? 209  THR A OG1 1 
ATOM   1583 C CG2 . THR A 1 209 ? 9.647   5.279   41.718  1.00 31.68 ? 209  THR A CG2 1 
ATOM   1584 N N   . ALA A 1 210 ? 12.900  3.892   44.800  1.00 33.05 ? 210  ALA A N   1 
ATOM   1585 C CA  . ALA A 1 210 ? 14.161  4.032   45.534  1.00 33.05 ? 210  ALA A CA  1 
ATOM   1586 C C   . ALA A 1 210 ? 15.072  2.833   45.269  1.00 33.66 ? 210  ALA A C   1 
ATOM   1587 O O   . ALA A 1 210 ? 16.277  2.885   45.515  1.00 33.40 ? 210  ALA A O   1 
ATOM   1588 C CB  . ALA A 1 210 ? 13.907  4.205   47.022  1.00 32.83 ? 210  ALA A CB  1 
ATOM   1589 N N   . THR A 1 211 ? 14.500  1.763   44.725  1.00 33.94 ? 211  THR A N   1 
ATOM   1590 C CA  . THR A 1 211 ? 15.294  0.590   44.417  1.00 34.36 ? 211  THR A CA  1 
ATOM   1591 C C   . THR A 1 211 ? 15.963  0.606   43.032  1.00 34.29 ? 211  THR A C   1 
ATOM   1592 O O   . THR A 1 211 ? 16.805  -0.256  42.746  1.00 34.46 ? 211  THR A O   1 
ATOM   1593 C CB  . THR A 1 211 ? 14.463  -0.663  44.495  1.00 34.35 ? 211  THR A CB  1 
ATOM   1594 O OG1 . THR A 1 211 ? 13.577  -0.675  43.390  1.00 35.70 ? 211  THR A OG1 1 
ATOM   1595 C CG2 . THR A 1 211 ? 13.653  -0.730  45.811  1.00 35.92 ? 211  THR A CG2 1 
ATOM   1596 N N   . PHE A 1 212 ? 15.592  1.544   42.162  1.00 33.68 ? 212  PHE A N   1 
ATOM   1597 C CA  . PHE A 1 212 ? 16.085  1.474   40.771  1.00 33.31 ? 212  PHE A CA  1 
ATOM   1598 C C   . PHE A 1 212 ? 16.354  2.786   40.056  1.00 31.98 ? 212  PHE A C   1 
ATOM   1599 O O   . PHE A 1 212 ? 17.201  2.834   39.173  1.00 31.63 ? 212  PHE A O   1 
ATOM   1600 C CB  . PHE A 1 212 ? 15.204  0.562   39.892  1.00 33.60 ? 212  PHE A CB  1 
ATOM   1601 C CG  . PHE A 1 212 ? 14.050  1.274   39.227  1.00 34.33 ? 212  PHE A CG  1 
ATOM   1602 C CD1 . PHE A 1 212 ? 12.821  1.376   39.869  1.00 32.26 ? 212  PHE A CD1 1 
ATOM   1603 C CD2 . PHE A 1 212 ? 14.186  1.812   37.934  1.00 34.72 ? 212  PHE A CD2 1 
ATOM   1604 C CE1 . PHE A 1 212 ? 11.746  2.043   39.252  1.00 32.94 ? 212  PHE A CE1 1 
ATOM   1605 C CE2 . PHE A 1 212 ? 13.115  2.474   37.309  1.00 34.51 ? 212  PHE A CE2 1 
ATOM   1606 C CZ  . PHE A 1 212 ? 11.892  2.589   37.974  1.00 33.84 ? 212  PHE A CZ  1 
ATOM   1607 N N   . VAL A 1 213 ? 15.625  3.827   40.418  1.00 31.23 ? 213  VAL A N   1 
ATOM   1608 C CA  . VAL A 1 213 ? 15.871  5.161   39.852  1.00 31.05 ? 213  VAL A CA  1 
ATOM   1609 C C   . VAL A 1 213 ? 17.238  5.830   40.235  1.00 30.93 ? 213  VAL A C   1 
ATOM   1610 O O   . VAL A 1 213 ? 17.844  6.466   39.369  1.00 30.79 ? 213  VAL A O   1 
ATOM   1611 C CB  . VAL A 1 213 ? 14.638  6.107   40.041  1.00 31.19 ? 213  VAL A CB  1 
ATOM   1612 C CG1 . VAL A 1 213 ? 14.874  7.495   39.478  1.00 30.94 ? 213  VAL A CG1 1 
ATOM   1613 C CG2 . VAL A 1 213 ? 13.413  5.505   39.392  1.00 31.15 ? 213  VAL A CG2 1 
ATOM   1614 N N   . PRO A 1 214 ? 17.738  5.676   41.499  1.00 30.79 ? 214  PRO A N   1 
ATOM   1615 C CA  . PRO A 1 214 ? 19.041  6.295   41.867  1.00 30.22 ? 214  PRO A CA  1 
ATOM   1616 C C   . PRO A 1 214 ? 20.245  5.995   40.951  1.00 29.73 ? 214  PRO A C   1 
ATOM   1617 O O   . PRO A 1 214 ? 21.008  6.892   40.666  1.00 29.34 ? 214  PRO A O   1 
ATOM   1618 C CB  . PRO A 1 214 ? 19.304  5.756   43.275  1.00 29.72 ? 214  PRO A CB  1 
ATOM   1619 C CG  . PRO A 1 214 ? 17.959  5.595   43.845  1.00 31.03 ? 214  PRO A CG  1 
ATOM   1620 C CD  . PRO A 1 214 ? 17.095  5.074   42.689  1.00 30.98 ? 214  PRO A CD  1 
ATOM   1621 N N   . SER A 1 215 ? 20.417  4.756   40.510  1.00 29.68 ? 215  SER A N   1 
ATOM   1622 C CA  . SER A 1 215 ? 21.474  4.395   39.563  1.00 30.36 ? 215  SER A CA  1 
ATOM   1623 C C   . SER A 1 215 ? 21.367  5.147   38.215  1.00 30.42 ? 215  SER A C   1 
ATOM   1624 O O   . SER A 1 215 ? 22.366  5.306   37.514  1.00 30.19 ? 215  SER A O   1 
ATOM   1625 C CB  . SER A 1 215 ? 21.396  2.902   39.210  1.00 30.30 ? 215  SER A CB  1 
ATOM   1626 O OG  . SER A 1 215 ? 21.064  2.098   40.310  1.00 32.73 ? 215  SER A OG  1 
ATOM   1627 N N   . ILE A 1 216 ? 20.146  5.535   37.841  1.00 30.22 ? 216  ILE A N   1 
ATOM   1628 C CA  . ILE A 1 216 ? 19.861  6.149   36.561  1.00 30.18 ? 216  ILE A CA  1 
ATOM   1629 C C   . ILE A 1 216 ? 20.148  7.621   36.742  1.00 30.39 ? 216  ILE A C   1 
ATOM   1630 O O   . ILE A 1 216 ? 20.863  8.217   35.923  1.00 30.98 ? 216  ILE A O   1 
ATOM   1631 C CB  . ILE A 1 216 ? 18.388  5.946   36.132  1.00 30.25 ? 216  ILE A CB  1 
ATOM   1632 C CG1 . ILE A 1 216 ? 18.046  4.465   36.009  1.00 30.62 ? 216  ILE A CG1 1 
ATOM   1633 C CG2 . ILE A 1 216 ? 18.112  6.613   34.831  1.00 29.52 ? 216  ILE A CG2 1 
ATOM   1634 C CD1 . ILE A 1 216 ? 16.496  4.207   36.039  1.00 31.80 ? 216  ILE A CD1 1 
ATOM   1635 N N   . ARG A 1 217 ? 19.608  8.201   37.820  1.00 29.86 ? 217  ARG A N   1 
ATOM   1636 C CA  . ARG A 1 217 ? 19.954  9.566   38.250  1.00 29.92 ? 217  ARG A CA  1 
ATOM   1637 C C   . ARG A 1 217 ? 21.476  9.820   38.248  1.00 29.75 ? 217  ARG A C   1 
ATOM   1638 O O   . ARG A 1 217 ? 21.943  10.823  37.689  1.00 29.03 ? 217  ARG A O   1 
ATOM   1639 C CB  . ARG A 1 217 ? 19.375  9.873   39.638  1.00 29.63 ? 217  ARG A CB  1 
ATOM   1640 C CG  . ARG A 1 217 ? 19.572  11.333  40.042  1.00 31.84 ? 217  ARG A CG  1 
ATOM   1641 C CD  . ARG A 1 217 ? 19.551  11.619  41.576  1.00 32.51 ? 217  ARG A CD  1 
ATOM   1642 N NE  . ARG A 1 217 ? 20.109  10.557  42.433  1.00 34.38 ? 217  ARG A NE  1 
ATOM   1643 C CZ  . ARG A 1 217 ? 21.402  10.392  42.739  1.00 30.66 ? 217  ARG A CZ  1 
ATOM   1644 N NH1 . ARG A 1 217 ? 22.334  11.192  42.234  1.00 26.68 ? 217  ARG A NH1 1 
ATOM   1645 N NH2 . ARG A 1 217 ? 21.760  9.376   43.521  1.00 27.87 ? 217  ARG A NH2 1 
ATOM   1646 N N   . GLN A 1 218 ? 22.230  8.913   38.870  1.00 29.80 ? 218  GLN A N   1 
ATOM   1647 C CA  . GLN A 1 218 ? 23.675  9.058   38.977  1.00 31.09 ? 218  GLN A CA  1 
ATOM   1648 C C   . GLN A 1 218 ? 24.233  9.181   37.566  1.00 30.94 ? 218  GLN A C   1 
ATOM   1649 O O   . GLN A 1 218 ? 24.846  10.207  37.220  1.00 30.17 ? 218  GLN A O   1 
ATOM   1650 C CB  . GLN A 1 218 ? 24.273  7.860   39.686  1.00 31.09 ? 218  GLN A CB  1 
ATOM   1651 C CG  . GLN A 1 218 ? 25.601  8.120   40.362  1.00 33.68 ? 218  GLN A CG  1 
ATOM   1652 C CD  . GLN A 1 218 ? 25.818  7.142   41.514  1.00 36.29 ? 218  GLN A CD  1 
ATOM   1653 O OE1 . GLN A 1 218 ? 25.710  5.921   41.342  1.00 36.13 ? 218  GLN A OE1 1 
ATOM   1654 N NE2 . GLN A 1 218 ? 26.072  7.677   42.699  1.00 36.04 ? 218  GLN A NE2 1 
ATOM   1655 N N   . ARG A 1 219 ? 23.934  8.161   36.754  1.00 31.13 ? 219  ARG A N   1 
ATOM   1656 C CA  . ARG A 1 219 ? 24.378  8.099   35.369  1.00 31.67 ? 219  ARG A CA  1 
ATOM   1657 C C   . ARG A 1 219 ? 24.014  9.338   34.602  1.00 31.99 ? 219  ARG A C   1 
ATOM   1658 O O   . ARG A 1 219 ? 24.867  9.908   33.952  1.00 32.97 ? 219  ARG A O   1 
ATOM   1659 C CB  . ARG A 1 219 ? 23.884  6.849   34.634  1.00 31.02 ? 219  ARG A CB  1 
ATOM   1660 C CG  . ARG A 1 219 ? 24.604  6.660   33.288  1.00 31.03 ? 219  ARG A CG  1 
ATOM   1661 C CD  . ARG A 1 219 ? 24.122  5.443   32.478  1.00 32.09 ? 219  ARG A CD  1 
ATOM   1662 N NE  . ARG A 1 219 ? 22.716  5.569   32.082  1.00 31.67 ? 219  ARG A NE  1 
ATOM   1663 C CZ  . ARG A 1 219 ? 21.724  4.812   32.558  1.00 32.15 ? 219  ARG A CZ  1 
ATOM   1664 N NH1 . ARG A 1 219 ? 21.963  3.837   33.456  1.00 31.49 ? 219  ARG A NH1 1 
ATOM   1665 N NH2 . ARG A 1 219 ? 20.488  5.023   32.122  1.00 32.14 ? 219  ARG A NH2 1 
ATOM   1666 N N   . LEU A 1 220 ? 22.769  9.775   34.694  1.00 32.50 ? 220  LEU A N   1 
ATOM   1667 C CA  . LEU A 1 220 ? 22.365  10.975  33.978  1.00 33.37 ? 220  LEU A CA  1 
ATOM   1668 C C   . LEU A 1 220 ? 23.079  12.258  34.430  1.00 34.01 ? 220  LEU A C   1 
ATOM   1669 O O   . LEU A 1 220 ? 23.315  13.146  33.615  1.00 34.14 ? 220  LEU A O   1 
ATOM   1670 C CB  . LEU A 1 220 ? 20.856  11.174  34.063  1.00 33.45 ? 220  LEU A CB  1 
ATOM   1671 C CG  . LEU A 1 220 ? 19.890  10.185  33.409  1.00 34.18 ? 220  LEU A CG  1 
ATOM   1672 C CD1 . LEU A 1 220 ? 18.425  10.617  33.698  1.00 31.95 ? 220  LEU A CD1 1 
ATOM   1673 C CD2 . LEU A 1 220 ? 20.195  10.064  31.898  1.00 32.72 ? 220  LEU A CD2 1 
ATOM   1674 N N   . GLU A 1 221 ? 23.370  12.384  35.730  1.00 35.20 ? 221  GLU A N   1 
ATOM   1675 C CA  . GLU A 1 221 ? 24.089  13.567  36.247  1.00 36.00 ? 221  GLU A CA  1 
ATOM   1676 C C   . GLU A 1 221 ? 25.542  13.473  35.822  1.00 36.30 ? 221  GLU A C   1 
ATOM   1677 O O   . GLU A 1 221 ? 26.186  14.480  35.573  1.00 36.15 ? 221  GLU A O   1 
ATOM   1678 C CB  . GLU A 1 221 ? 23.994  13.689  37.778  1.00 35.73 ? 221  GLU A CB  1 
ATOM   1679 C CG  . GLU A 1 221 ? 22.678  14.234  38.291  1.00 36.40 ? 221  GLU A CG  1 
ATOM   1680 C CD  . GLU A 1 221 ? 22.528  14.092  39.798  1.00 36.82 ? 221  GLU A CD  1 
ATOM   1681 O OE1 . GLU A 1 221 ? 23.090  13.142  40.384  1.00 38.89 ? 221  GLU A OE1 1 
ATOM   1682 O OE2 . GLU A 1 221 ? 21.840  14.937  40.404  1.00 37.15 ? 221  GLU A OE2 1 
ATOM   1683 N N   . ASN A 1 222 ? 26.027  12.242  35.724  1.00 37.09 ? 222  ASN A N   1 
ATOM   1684 C CA  . ASN A 1 222 ? 27.379  11.979  35.290  1.00 38.34 ? 222  ASN A CA  1 
ATOM   1685 C C   . ASN A 1 222 ? 27.585  12.423  33.856  1.00 38.29 ? 222  ASN A C   1 
ATOM   1686 O O   . ASN A 1 222 ? 28.598  13.055  33.541  1.00 38.33 ? 222  ASN A O   1 
ATOM   1687 C CB  . ASN A 1 222 ? 27.654  10.487  35.371  1.00 38.90 ? 222  ASN A CB  1 
ATOM   1688 C CG  . ASN A 1 222 ? 28.837  10.158  36.263  1.00 42.84 ? 222  ASN A CG  1 
ATOM   1689 O OD1 . ASN A 1 222 ? 29.934  9.841   35.774  1.00 46.68 ? 222  ASN A OD1 1 
ATOM   1690 N ND2 . ASN A 1 222 ? 28.620  10.215  37.581  1.00 43.88 ? 222  ASN A ND2 1 
ATOM   1691 N N   . ASP A 1 223 ? 26.623  12.085  32.997  1.00 37.92 ? 223  ASP A N   1 
ATOM   1692 C CA  . ASP A 1 223 ? 26.738  12.335  31.567  1.00 38.12 ? 223  ASP A CA  1 
ATOM   1693 C C   . ASP A 1 223 ? 26.391  13.782  31.219  1.00 37.95 ? 223  ASP A C   1 
ATOM   1694 O O   . ASP A 1 223 ? 26.874  14.317  30.223  1.00 38.25 ? 223  ASP A O   1 
ATOM   1695 C CB  . ASP A 1 223 ? 25.819  11.408  30.769  1.00 38.17 ? 223  ASP A CB  1 
ATOM   1696 C CG  . ASP A 1 223 ? 26.201  9.929   30.864  1.00 39.60 ? 223  ASP A CG  1 
ATOM   1697 O OD1 . ASP A 1 223 ? 27.413  9.610   30.895  1.00 40.95 ? 223  ASP A OD1 1 
ATOM   1698 O OD2 . ASP A 1 223 ? 25.262  9.073   30.867  1.00 39.88 ? 223  ASP A OD2 1 
ATOM   1699 N N   . LEU A 1 224 ? 25.526  14.403  32.015  1.00 37.62 ? 224  LEU A N   1 
ATOM   1700 C CA  . LEU A 1 224 ? 25.135  15.789  31.792  1.00 37.26 ? 224  LEU A CA  1 
ATOM   1701 C C   . LEU A 1 224 ? 25.691  16.684  32.899  1.00 37.46 ? 224  LEU A C   1 
ATOM   1702 O O   . LEU A 1 224 ? 24.972  17.057  33.834  1.00 37.56 ? 224  LEU A O   1 
ATOM   1703 C CB  . LEU A 1 224 ? 23.618  15.897  31.713  1.00 37.38 ? 224  LEU A CB  1 
ATOM   1704 C CG  . LEU A 1 224 ? 22.904  15.337  30.467  1.00 37.34 ? 224  LEU A CG  1 
ATOM   1705 C CD1 . LEU A 1 224 ? 21.545  14.683  30.849  1.00 36.41 ? 224  LEU A CD1 1 
ATOM   1706 C CD2 . LEU A 1 224 ? 22.715  16.410  29.393  1.00 35.17 ? 224  LEU A CD2 1 
ATOM   1707 N N   . SER A 1 225 ? 26.982  17.019  32.780  1.00 37.41 ? 225  SER A N   1 
ATOM   1708 C CA  . SER A 1 225 ? 27.729  17.816  33.775  1.00 37.31 ? 225  SER A CA  1 
ATOM   1709 C C   . SER A 1 225 ? 27.138  19.174  34.079  1.00 36.71 ? 225  SER A C   1 
ATOM   1710 O O   . SER A 1 225 ? 27.039  20.002  33.201  1.00 37.35 ? 225  SER A O   1 
ATOM   1711 C CB  . SER A 1 225 ? 29.174  18.021  33.298  1.00 37.67 ? 225  SER A CB  1 
ATOM   1712 O OG  . SER A 1 225 ? 29.945  16.848  33.522  1.00 39.78 ? 225  SER A OG  1 
ATOM   1713 N N   . GLY A 1 226 ? 26.781  19.420  35.330  1.00 36.40 ? 226  GLY A N   1 
ATOM   1714 C CA  . GLY A 1 226 ? 26.159  20.693  35.712  1.00 36.34 ? 226  GLY A CA  1 
ATOM   1715 C C   . GLY A 1 226 ? 24.690  20.560  36.119  1.00 35.78 ? 226  GLY A C   1 
ATOM   1716 O O   . GLY A 1 226 ? 24.092  21.484  36.690  1.00 36.25 ? 226  GLY A O   1 
ATOM   1717 N N   . VAL A 1 227 ? 24.128  19.386  35.866  1.00 34.85 ? 227  VAL A N   1 
ATOM   1718 C CA  . VAL A 1 227 ? 22.709  19.113  36.095  1.00 33.59 ? 227  VAL A CA  1 
ATOM   1719 C C   . VAL A 1 227 ? 22.542  18.360  37.397  1.00 33.07 ? 227  VAL A C   1 
ATOM   1720 O O   . VAL A 1 227 ? 23.324  17.461  37.707  1.00 32.28 ? 227  VAL A O   1 
ATOM   1721 C CB  . VAL A 1 227 ? 22.180  18.240  34.936  1.00 33.52 ? 227  VAL A CB  1 
ATOM   1722 C CG1 . VAL A 1 227 ? 21.041  17.322  35.381  1.00 34.08 ? 227  VAL A CG1 1 
ATOM   1723 C CG2 . VAL A 1 227 ? 21.787  19.108  33.744  1.00 33.07 ? 227  VAL A CG2 1 
ATOM   1724 N N   . THR A 1 228 ? 21.516  18.698  38.164  1.00 32.69 ? 228  THR A N   1 
ATOM   1725 C CA  . THR A 1 228 ? 21.254  17.920  39.364  1.00 32.62 ? 228  THR A CA  1 
ATOM   1726 C C   . THR A 1 228 ? 19.783  17.518  39.341  1.00 32.15 ? 228  THR A C   1 
ATOM   1727 O O   . THR A 1 228 ? 18.923  18.343  39.071  1.00 32.58 ? 228  THR A O   1 
ATOM   1728 C CB  . THR A 1 228 ? 21.749  18.650  40.698  1.00 32.96 ? 228  THR A CB  1 
ATOM   1729 O OG1 . THR A 1 228 ? 20.668  19.286  41.385  1.00 33.21 ? 228  THR A OG1 1 
ATOM   1730 C CG2 . THR A 1 228 ? 22.825  19.719  40.417  1.00 33.60 ? 228  THR A CG2 1 
ATOM   1731 N N   . LEU A 1 229 ? 19.496  16.244  39.577  1.00 31.92 ? 229  LEU A N   1 
ATOM   1732 C CA  . LEU A 1 229 ? 18.162  15.656  39.313  1.00 31.55 ? 229  LEU A CA  1 
ATOM   1733 C C   . LEU A 1 229 ? 17.558  14.956  40.526  1.00 32.05 ? 229  LEU A C   1 
ATOM   1734 O O   . LEU A 1 229 ? 18.282  14.287  41.275  1.00 32.25 ? 229  LEU A O   1 
ATOM   1735 C CB  . LEU A 1 229 ? 18.260  14.637  38.178  1.00 31.03 ? 229  LEU A CB  1 
ATOM   1736 C CG  . LEU A 1 229 ? 18.450  15.125  36.726  1.00 31.24 ? 229  LEU A CG  1 
ATOM   1737 C CD1 . LEU A 1 229 ? 18.856  13.966  35.791  1.00 29.57 ? 229  LEU A CD1 1 
ATOM   1738 C CD2 . LEU A 1 229 ? 17.226  15.931  36.167  1.00 28.03 ? 229  LEU A CD2 1 
ATOM   1739 N N   . THR A 1 230 ? 16.249  15.119  40.735  1.00 31.65 ? 230  THR A N   1 
ATOM   1740 C CA  . THR A 1 230 ? 15.538  14.287  41.710  1.00 31.73 ? 230  THR A CA  1 
ATOM   1741 C C   . THR A 1 230 ? 15.029  13.030  41.023  1.00 32.12 ? 230  THR A C   1 
ATOM   1742 O O   . THR A 1 230 ? 14.757  13.035  39.821  1.00 32.68 ? 230  THR A O   1 
ATOM   1743 C CB  . THR A 1 230 ? 14.297  14.967  42.343  1.00 31.42 ? 230  THR A CB  1 
ATOM   1744 O OG1 . THR A 1 230 ? 13.281  15.124  41.350  1.00 30.44 ? 230  THR A OG1 1 
ATOM   1745 C CG2 . THR A 1 230 ? 14.644  16.315  42.971  1.00 30.79 ? 230  THR A CG2 1 
ATOM   1746 N N   . ASP A 1 231 ? 14.861  11.968  41.794  1.00 32.22 ? 231  ASP A N   1 
ATOM   1747 C CA  . ASP A 1 231 ? 14.289  10.743  41.270  1.00 32.75 ? 231  ASP A CA  1 
ATOM   1748 C C   . ASP A 1 231 ? 13.010  10.995  40.432  1.00 32.48 ? 231  ASP A C   1 
ATOM   1749 O O   . ASP A 1 231 ? 12.794  10.369  39.366  1.00 33.09 ? 231  ASP A O   1 
ATOM   1750 C CB  . ASP A 1 231 ? 14.022  9.793   42.428  1.00 33.04 ? 231  ASP A CB  1 
ATOM   1751 C CG  . ASP A 1 231 ? 15.315  9.336   43.110  1.00 34.65 ? 231  ASP A CG  1 
ATOM   1752 O OD1 . ASP A 1 231 ? 16.389  9.443   42.471  1.00 36.83 ? 231  ASP A OD1 1 
ATOM   1753 O OD2 . ASP A 1 231 ? 15.264  8.847   44.274  1.00 35.91 ? 231  ASP A OD2 1 
ATOM   1754 N N   . THR A 1 232 ? 12.200  11.945  40.886  1.00 30.94 ? 232  THR A N   1 
ATOM   1755 C CA  . THR A 1 232 ? 10.909  12.187  40.260  1.00 29.98 ? 232  THR A CA  1 
ATOM   1756 C C   . THR A 1 232 ? 11.190  12.707  38.882  1.00 29.25 ? 232  THR A C   1 
ATOM   1757 O O   . THR A 1 232 ? 10.585  12.258  37.904  1.00 30.21 ? 232  THR A O   1 
ATOM   1758 C CB  . THR A 1 232 ? 9.993   13.115  41.120  1.00 29.74 ? 232  THR A CB  1 
ATOM   1759 O OG1 . THR A 1 232 ? 9.663   12.442  42.348  1.00 29.82 ? 232  THR A OG1 1 
ATOM   1760 C CG2 . THR A 1 232 ? 8.702   13.402  40.412  1.00 30.34 ? 232  THR A CG2 1 
ATOM   1761 N N   . GLU A 1 233 ? 12.182  13.585  38.789  1.00 27.84 ? 233  GLU A N   1 
ATOM   1762 C CA  . GLU A 1 233 ? 12.546  14.150  37.514  1.00 26.55 ? 233  GLU A CA  1 
ATOM   1763 C C   . GLU A 1 233 ? 13.018  13.074  36.566  1.00 25.64 ? 233  GLU A C   1 
ATOM   1764 O O   . GLU A 1 233 ? 12.734  13.112  35.396  1.00 25.75 ? 233  GLU A O   1 
ATOM   1765 C CB  . GLU A 1 233 ? 13.531  15.295  37.701  1.00 26.50 ? 233  GLU A CB  1 
ATOM   1766 C CG  . GLU A 1 233 ? 12.780  16.533  38.262  1.00 27.88 ? 233  GLU A CG  1 
ATOM   1767 C CD  . GLU A 1 233 ? 13.661  17.606  38.876  1.00 29.00 ? 233  GLU A CD  1 
ATOM   1768 O OE1 . GLU A 1 233 ? 14.878  17.315  39.104  1.00 32.16 ? 233  GLU A OE1 1 
ATOM   1769 O OE2 . GLU A 1 233 ? 13.130  18.738  39.110  1.00 27.38 ? 233  GLU A OE2 1 
ATOM   1770 N N   . VAL A 1 234 ? 13.687  12.067  37.081  1.00 25.19 ? 234  VAL A N   1 
ATOM   1771 C CA  . VAL A 1 234 ? 14.136  11.013  36.216  1.00 24.83 ? 234  VAL A CA  1 
ATOM   1772 C C   . VAL A 1 234 ? 12.926  10.285  35.632  1.00 25.34 ? 234  VAL A C   1 
ATOM   1773 O O   . VAL A 1 234 ? 12.921  9.985   34.453  1.00 24.69 ? 234  VAL A O   1 
ATOM   1774 C CB  . VAL A 1 234 ? 15.032  10.017  36.931  1.00 25.13 ? 234  VAL A CB  1 
ATOM   1775 C CG1 . VAL A 1 234 ? 15.315  8.844   36.009  1.00 24.79 ? 234  VAL A CG1 1 
ATOM   1776 C CG2 . VAL A 1 234 ? 16.344  10.686  37.426  1.00 22.95 ? 234  VAL A CG2 1 
ATOM   1777 N N   . THR A 1 235 ? 11.891  10.019  36.436  1.00 24.99 ? 235  THR A N   1 
ATOM   1778 C CA  . THR A 1 235 ? 10.727  9.380   35.850  1.00 24.72 ? 235  THR A CA  1 
ATOM   1779 C C   . THR A 1 235 ? 10.070  10.276  34.784  1.00 24.67 ? 235  THR A C   1 
ATOM   1780 O O   . THR A 1 235 ? 9.508   9.753   33.813  1.00 24.58 ? 235  THR A O   1 
ATOM   1781 C CB  . THR A 1 235 ? 9.686   8.863   36.885  1.00 24.83 ? 235  THR A CB  1 
ATOM   1782 O OG1 . THR A 1 235 ? 8.922   9.959   37.420  1.00 24.73 ? 235  THR A OG1 1 
ATOM   1783 C CG2 . THR A 1 235 ? 10.386  8.074   38.012  1.00 25.22 ? 235  THR A CG2 1 
ATOM   1784 N N   . TYR A 1 236 ? 10.164  11.602  34.934  1.00 24.34 ? 236  TYR A N   1 
ATOM   1785 C CA  . TYR A 1 236 ? 9.671   12.510  33.895  1.00 24.51 ? 236  TYR A CA  1 
ATOM   1786 C C   . TYR A 1 236 ? 10.380  12.302  32.548  1.00 24.55 ? 236  TYR A C   1 
ATOM   1787 O O   . TYR A 1 236 ? 9.721   12.155  31.541  1.00 25.08 ? 236  TYR A O   1 
ATOM   1788 C CB  . TYR A 1 236 ? 9.721   13.978  34.315  1.00 24.68 ? 236  TYR A CB  1 
ATOM   1789 C CG  . TYR A 1 236 ? 8.864   14.350  35.523  1.00 27.81 ? 236  TYR A CG  1 
ATOM   1790 C CD1 . TYR A 1 236 ? 7.853   13.499  36.006  1.00 27.89 ? 236  TYR A CD1 1 
ATOM   1791 C CD2 . TYR A 1 236 ? 9.057   15.580  36.173  1.00 29.40 ? 236  TYR A CD2 1 
ATOM   1792 C CE1 . TYR A 1 236 ? 7.086   13.858  37.121  1.00 30.83 ? 236  TYR A CE1 1 
ATOM   1793 C CE2 . TYR A 1 236 ? 8.290   15.959  37.272  1.00 30.41 ? 236  TYR A CE2 1 
ATOM   1794 C CZ  . TYR A 1 236 ? 7.309   15.096  37.750  1.00 32.59 ? 236  TYR A CZ  1 
ATOM   1795 O OH  . TYR A 1 236 ? 6.537   15.492  38.840  1.00 34.81 ? 236  TYR A OH  1 
ATOM   1796 N N   . LEU A 1 237 ? 11.707  12.269  32.511  1.00 24.28 ? 237  LEU A N   1 
ATOM   1797 C CA  . LEU A 1 237 ? 12.413  11.910  31.264  1.00 24.19 ? 237  LEU A CA  1 
ATOM   1798 C C   . LEU A 1 237 ? 12.050  10.526  30.707  1.00 25.05 ? 237  LEU A C   1 
ATOM   1799 O O   . LEU A 1 237 ? 12.112  10.272  29.484  1.00 25.53 ? 237  LEU A O   1 
ATOM   1800 C CB  . LEU A 1 237 ? 13.918  12.002  31.458  1.00 23.61 ? 237  LEU A CB  1 
ATOM   1801 C CG  . LEU A 1 237 ? 14.448  13.396  31.813  1.00 23.55 ? 237  LEU A CG  1 
ATOM   1802 C CD1 . LEU A 1 237 ? 15.893  13.274  32.189  1.00 23.09 ? 237  LEU A CD1 1 
ATOM   1803 C CD2 . LEU A 1 237 ? 14.246  14.475  30.702  1.00 17.74 ? 237  LEU A CD2 1 
ATOM   1804 N N   . MET A 1 238 ? 11.684  9.611   31.589  1.00 25.17 ? 238  MET A N   1 
ATOM   1805 C CA  . MET A 1 238 ? 11.187  8.324   31.127  1.00 25.57 ? 238  MET A CA  1 
ATOM   1806 C C   . MET A 1 238 ? 9.761   8.494   30.549  1.00 26.21 ? 238  MET A C   1 
ATOM   1807 O O   . MET A 1 238 ? 9.462   7.964   29.464  1.00 26.42 ? 238  MET A O   1 
ATOM   1808 C CB  . MET A 1 238 ? 11.262  7.285   32.248  1.00 25.36 ? 238  MET A CB  1 
ATOM   1809 C CG  . MET A 1 238 ? 12.689  6.979   32.678  1.00 25.11 ? 238  MET A CG  1 
ATOM   1810 S SD  . MET A 1 238 ? 12.884  5.572   33.776  1.00 26.17 ? 238  MET A SD  1 
ATOM   1811 C CE  . MET A 1 238 ? 12.909  4.194   32.677  1.00 22.11 ? 238  MET A CE  1 
ATOM   1812 N N   . ASP A 1 239 ? 8.904   9.241   31.260  1.00 25.96 ? 239  ASP A N   1 
ATOM   1813 C CA  . ASP A 1 239 ? 7.554   9.564   30.781  1.00 26.03 ? 239  ASP A CA  1 
ATOM   1814 C C   . ASP A 1 239 ? 7.631   10.156  29.357  1.00 26.57 ? 239  ASP A C   1 
ATOM   1815 O O   . ASP A 1 239 ? 6.865   9.764   28.486  1.00 26.44 ? 239  ASP A O   1 
ATOM   1816 C CB  . ASP A 1 239 ? 6.844   10.558  31.726  1.00 25.41 ? 239  ASP A CB  1 
ATOM   1817 C CG  . ASP A 1 239 ? 6.267   9.904   33.020  1.00 24.45 ? 239  ASP A CG  1 
ATOM   1818 O OD1 . ASP A 1 239 ? 6.317   8.677   33.252  1.00 22.43 ? 239  ASP A OD1 1 
ATOM   1819 O OD2 . ASP A 1 239 ? 5.738   10.660  33.840  1.00 25.35 ? 239  ASP A OD2 1 
ATOM   1820 N N   . MET A 1 240 ? 8.591   11.054  29.114  1.00 27.26 ? 240  MET A N   1 
ATOM   1821 C CA  . MET A 1 240 ? 8.771   11.692  27.798  1.00 27.55 ? 240  MET A CA  1 
ATOM   1822 C C   . MET A 1 240 ? 9.053   10.753  26.627  1.00 28.03 ? 240  MET A C   1 
ATOM   1823 O O   . MET A 1 240 ? 8.761   11.090  25.484  1.00 28.80 ? 240  MET A O   1 
ATOM   1824 C CB  . MET A 1 240 ? 9.850   12.759  27.850  1.00 27.56 ? 240  MET A CB  1 
ATOM   1825 C CG  . MET A 1 240 ? 9.385   14.026  28.524  1.00 28.33 ? 240  MET A CG  1 
ATOM   1826 S SD  . MET A 1 240 ? 7.941   14.788  27.701  1.00 32.78 ? 240  MET A SD  1 
ATOM   1827 C CE  . MET A 1 240 ? 8.729   15.264  26.150  1.00 28.62 ? 240  MET A CE  1 
ATOM   1828 N N   . CYS A 1 241 ? 9.611   9.581   26.886  1.00 28.11 ? 241  CYS A N   1 
ATOM   1829 C CA  . CYS A 1 241 ? 9.828   8.625   25.813  1.00 28.60 ? 241  CYS A CA  1 
ATOM   1830 C C   . CYS A 1 241 ? 8.498   8.097   25.207  1.00 28.59 ? 241  CYS A C   1 
ATOM   1831 O O   . CYS A 1 241 ? 8.395   7.850   24.015  1.00 29.27 ? 241  CYS A O   1 
ATOM   1832 C CB  . CYS A 1 241 ? 10.720  7.516   26.307  1.00 28.50 ? 241  CYS A CB  1 
ATOM   1833 S SG  . CYS A 1 241 ? 10.570  6.004   25.374  1.00 32.08 ? 241  CYS A SG  1 
ATOM   1834 N N   . SER A 1 242 ? 7.463   7.963   26.023  1.00 28.12 ? 242  SER A N   1 
ATOM   1835 C CA  . SER A 1 242 ? 6.173   7.610   25.498  1.00 26.94 ? 242  SER A CA  1 
ATOM   1836 C C   . SER A 1 242 ? 5.613   8.802   24.703  1.00 27.16 ? 242  SER A C   1 
ATOM   1837 O O   . SER A 1 242 ? 5.351   8.687   23.497  1.00 26.56 ? 242  SER A O   1 
ATOM   1838 C CB  . SER A 1 242 ? 5.237   7.226   26.632  1.00 26.77 ? 242  SER A CB  1 
ATOM   1839 O OG  . SER A 1 242 ? 4.045   6.692   26.120  1.00 25.12 ? 242  SER A OG  1 
ATOM   1840 N N   . PHE A 1 243 ? 5.483   9.947   25.375  1.00 26.78 ? 243  PHE A N   1 
ATOM   1841 C CA  . PHE A 1 243 ? 4.847   11.127  24.809  1.00 27.13 ? 243  PHE A CA  1 
ATOM   1842 C C   . PHE A 1 243 ? 5.526   11.711  23.580  1.00 27.71 ? 243  PHE A C   1 
ATOM   1843 O O   . PHE A 1 243 ? 4.858   12.123  22.645  1.00 28.05 ? 243  PHE A O   1 
ATOM   1844 C CB  . PHE A 1 243 ? 4.729   12.183  25.882  1.00 27.15 ? 243  PHE A CB  1 
ATOM   1845 C CG  . PHE A 1 243 ? 3.700   11.856  26.913  1.00 27.33 ? 243  PHE A CG  1 
ATOM   1846 C CD1 . PHE A 1 243 ? 2.344   11.873  26.587  1.00 26.74 ? 243  PHE A CD1 1 
ATOM   1847 C CD2 . PHE A 1 243 ? 4.082   11.514  28.208  1.00 26.47 ? 243  PHE A CD2 1 
ATOM   1848 C CE1 . PHE A 1 243 ? 1.384   11.560  27.531  1.00 27.87 ? 243  PHE A CE1 1 
ATOM   1849 C CE2 . PHE A 1 243 ? 3.118   11.196  29.175  1.00 27.71 ? 243  PHE A CE2 1 
ATOM   1850 C CZ  . PHE A 1 243 ? 1.768   11.209  28.834  1.00 27.37 ? 243  PHE A CZ  1 
ATOM   1851 N N   . ASP A 1 244 ? 6.848   11.749  23.573  1.00 28.37 ? 244  ASP A N   1 
ATOM   1852 C CA  . ASP A 1 244 ? 7.571   12.264  22.414  1.00 29.00 ? 244  ASP A CA  1 
ATOM   1853 C C   . ASP A 1 244 ? 7.497   11.285  21.244  1.00 29.87 ? 244  ASP A C   1 
ATOM   1854 O O   . ASP A 1 244 ? 7.663   11.664  20.096  1.00 30.59 ? 244  ASP A O   1 
ATOM   1855 C CB  . ASP A 1 244 ? 9.017   12.609  22.773  1.00 28.53 ? 244  ASP A CB  1 
ATOM   1856 C CG  . ASP A 1 244 ? 9.731   13.385  21.679  1.00 28.20 ? 244  ASP A CG  1 
ATOM   1857 O OD1 . ASP A 1 244 ? 9.427   14.570  21.470  1.00 27.67 ? 244  ASP A OD1 1 
ATOM   1858 O OD2 . ASP A 1 244 ? 10.612  12.813  21.025  1.00 28.85 ? 244  ASP A OD2 1 
ATOM   1859 N N   . THR A 1 245 ? 7.242   10.019  21.514  1.00 31.38 ? 245  THR A N   1 
ATOM   1860 C CA  . THR A 1 245 ? 7.056   9.077   20.418  1.00 32.79 ? 245  THR A CA  1 
ATOM   1861 C C   . THR A 1 245 ? 5.671   9.243   19.750  1.00 33.80 ? 245  THR A C   1 
ATOM   1862 O O   . THR A 1 245 ? 5.548   9.638   18.581  1.00 33.96 ? 245  THR A O   1 
ATOM   1863 C CB  . THR A 1 245 ? 7.309   7.642   20.899  1.00 32.41 ? 245  THR A CB  1 
ATOM   1864 O OG1 . THR A 1 245 ? 8.651   7.565   21.376  1.00 34.08 ? 245  THR A OG1 1 
ATOM   1865 C CG2 . THR A 1 245 ? 7.146   6.618   19.758  1.00 32.19 ? 245  THR A CG2 1 
ATOM   1866 N N   . ILE A 1 246 ? 4.641   8.995   20.537  1.00 35.09 ? 246  ILE A N   1 
ATOM   1867 C CA  . ILE A 1 246 ? 3.316   8.776   20.020  1.00 36.24 ? 246  ILE A CA  1 
ATOM   1868 C C   . ILE A 1 246 ? 2.460   10.036  19.925  1.00 37.62 ? 246  ILE A C   1 
ATOM   1869 O O   . ILE A 1 246 ? 1.245   9.954   19.704  1.00 38.26 ? 246  ILE A O   1 
ATOM   1870 C CB  . ILE A 1 246 ? 2.616   7.626   20.808  1.00 36.13 ? 246  ILE A CB  1 
ATOM   1871 C CG1 . ILE A 1 246 ? 2.189   8.058   22.220  1.00 34.52 ? 246  ILE A CG1 1 
ATOM   1872 C CG2 . ILE A 1 246 ? 3.501   6.373   20.853  1.00 33.67 ? 246  ILE A CG2 1 
ATOM   1873 C CD1 . ILE A 1 246 ? 1.512   6.920   22.985  1.00 32.30 ? 246  ILE A CD1 1 
ATOM   1874 N N   . SER A 1 247 ? 3.107   11.189  20.067  1.00 39.27 ? 247  SER A N   1 
ATOM   1875 C CA  . SER A 1 247 ? 2.450   12.496  19.926  1.00 41.17 ? 247  SER A CA  1 
ATOM   1876 C C   . SER A 1 247 ? 2.695   13.140  18.577  1.00 41.98 ? 247  SER A C   1 
ATOM   1877 O O   . SER A 1 247 ? 2.013   14.072  18.216  1.00 42.77 ? 247  SER A O   1 
ATOM   1878 C CB  . SER A 1 247 ? 2.921   13.482  20.995  1.00 41.05 ? 247  SER A CB  1 
ATOM   1879 O OG  . SER A 1 247 ? 2.434   13.124  22.280  1.00 42.26 ? 247  SER A OG  1 
ATOM   1880 N N   . THR A 1 248 ? 3.673   12.666  17.830  1.00 43.51 ? 248  THR A N   1 
ATOM   1881 C CA  . THR A 1 248 ? 3.981   13.307  16.553  1.00 44.96 ? 248  THR A CA  1 
ATOM   1882 C C   . THR A 1 248 ? 3.670   12.483  15.315  1.00 44.98 ? 248  THR A C   1 
ATOM   1883 O O   . THR A 1 248 ? 3.159   11.355  15.390  1.00 44.73 ? 248  THR A O   1 
ATOM   1884 C CB  . THR A 1 248 ? 5.473   13.766  16.457  1.00 45.74 ? 248  THR A CB  1 
ATOM   1885 O OG1 . THR A 1 248 ? 5.876   13.830  15.070  1.00 46.94 ? 248  THR A OG1 1 
ATOM   1886 C CG2 . THR A 1 248 ? 6.400   12.801  17.221  1.00 45.95 ? 248  THR A CG2 1 
ATOM   1887 N N   . SER A 1 249 ? 3.998   13.104  14.178  1.00 45.32 ? 249  SER A N   1 
ATOM   1888 C CA  . SER A 1 249 ? 4.087   12.476  12.857  1.00 45.21 ? 249  SER A CA  1 
ATOM   1889 C C   . SER A 1 249 ? 4.761   11.116  12.923  1.00 44.48 ? 249  SER A C   1 
ATOM   1890 O O   . SER A 1 249 ? 4.268   10.130  12.348  1.00 44.68 ? 249  SER A O   1 
ATOM   1891 C CB  . SER A 1 249 ? 4.908   13.391  11.924  1.00 45.93 ? 249  SER A CB  1 
ATOM   1892 O OG  . SER A 1 249 ? 5.166   12.774  10.653  1.00 47.17 ? 249  SER A OG  1 
ATOM   1893 N N   . THR A 1 250 ? 5.874   11.066  13.648  1.00 43.45 ? 250  THR A N   1 
ATOM   1894 C CA  . THR A 1 250 ? 6.787   9.939   13.553  1.00 42.65 ? 250  THR A CA  1 
ATOM   1895 C C   . THR A 1 250 ? 6.357   8.709   14.326  1.00 41.94 ? 250  THR A C   1 
ATOM   1896 O O   . THR A 1 250 ? 7.133   7.744   14.451  1.00 41.32 ? 250  THR A O   1 
ATOM   1897 C CB  . THR A 1 250 ? 8.255   10.338  13.883  1.00 43.06 ? 250  THR A CB  1 
ATOM   1898 O OG1 . THR A 1 250 ? 8.289   11.436  14.815  1.00 42.59 ? 250  THR A OG1 1 
ATOM   1899 C CG2 . THR A 1 250 ? 8.934   10.763  12.608  1.00 43.95 ? 250  THR A CG2 1 
ATOM   1900 N N   . VAL A 1 251 ? 5.114   8.726   14.802  1.00 41.30 ? 251  VAL A N   1 
ATOM   1901 C CA  . VAL A 1 251 ? 4.619   7.652   15.635  1.00 41.45 ? 251  VAL A CA  1 
ATOM   1902 C C   . VAL A 1 251 ? 5.019   6.282   15.118  1.00 41.57 ? 251  VAL A C   1 
ATOM   1903 O O   . VAL A 1 251 ? 5.462   5.437   15.904  1.00 40.90 ? 251  VAL A O   1 
ATOM   1904 C CB  . VAL A 1 251 ? 3.108   7.790   15.934  1.00 41.61 ? 251  VAL A CB  1 
ATOM   1905 C CG1 . VAL A 1 251 ? 2.264   7.787   14.705  1.00 41.82 ? 251  VAL A CG1 1 
ATOM   1906 C CG2 . VAL A 1 251 ? 2.665   6.783   16.952  1.00 41.82 ? 251  VAL A CG2 1 
ATOM   1907 N N   . ASP A 1 252 ? 4.936   6.096   13.796  1.00 42.17 ? 252  ASP A N   1 
ATOM   1908 C CA  . ASP A 1 252 ? 5.210   4.794   13.153  1.00 42.47 ? 252  ASP A CA  1 
ATOM   1909 C C   . ASP A 1 252 ? 6.675   4.621   12.689  1.00 42.00 ? 252  ASP A C   1 
ATOM   1910 O O   . ASP A 1 252 ? 7.141   3.511   12.491  1.00 41.79 ? 252  ASP A O   1 
ATOM   1911 C CB  . ASP A 1 252 ? 4.213   4.543   12.007  1.00 42.38 ? 252  ASP A CB  1 
ATOM   1912 C CG  . ASP A 1 252 ? 2.837   4.080   12.506  1.00 44.79 ? 252  ASP A CG  1 
ATOM   1913 O OD1 . ASP A 1 252 ? 2.564   2.877   12.418  1.00 47.19 ? 252  ASP A OD1 1 
ATOM   1914 O OD2 . ASP A 1 252 ? 2.021   4.889   12.992  1.00 46.77 ? 252  ASP A OD2 1 
ATOM   1915 N N   . THR A 1 253 ? 7.403   5.720   12.542  1.00 42.49 ? 253  THR A N   1 
ATOM   1916 C CA  . THR A 1 253 ? 8.720   5.674   11.878  1.00 43.06 ? 253  THR A CA  1 
ATOM   1917 C C   . THR A 1 253 ? 9.928   5.741   12.821  1.00 43.28 ? 253  THR A C   1 
ATOM   1918 O O   . THR A 1 253 ? 10.912  5.032   12.598  1.00 43.55 ? 253  THR A O   1 
ATOM   1919 C CB  . THR A 1 253 ? 8.861   6.745   10.759  1.00 43.12 ? 253  THR A CB  1 
ATOM   1920 O OG1 . THR A 1 253 ? 8.229   7.957   11.170  1.00 43.68 ? 253  THR A OG1 1 
ATOM   1921 C CG2 . THR A 1 253 ? 8.210   6.286   9.465   1.00 43.53 ? 253  THR A CG2 1 
ATOM   1922 N N   . LYS A 1 254 ? 9.859   6.589   13.857  1.00 43.22 ? 254  LYS A N   1 
ATOM   1923 C CA  . LYS A 1 254 ? 10.968  6.745   14.827  1.00 43.22 ? 254  LYS A CA  1 
ATOM   1924 C C   . LYS A 1 254 ? 10.522  6.602   16.275  1.00 42.47 ? 254  LYS A C   1 
ATOM   1925 O O   . LYS A 1 254 ? 9.518   7.201   16.693  1.00 42.31 ? 254  LYS A O   1 
ATOM   1926 C CB  . LYS A 1 254 ? 11.684  8.109   14.696  1.00 43.27 ? 254  LYS A CB  1 
ATOM   1927 C CG  . LYS A 1 254 ? 12.409  8.382   13.361  1.00 46.87 ? 254  LYS A CG  1 
ATOM   1928 C CD  . LYS A 1 254 ? 12.915  9.862   13.239  1.00 49.87 ? 254  LYS A CD  1 
ATOM   1929 C CE  . LYS A 1 254 ? 12.573  10.493  11.858  1.00 50.10 ? 254  LYS A CE  1 
ATOM   1930 N NZ  . LYS A 1 254 ? 12.806  9.531   10.742  1.00 51.49 ? 254  LYS A NZ  1 
ATOM   1931 N N   . LEU A 1 255 ? 11.292  5.827   17.036  1.00 41.80 ? 255  LEU A N   1 
ATOM   1932 C CA  . LEU A 1 255 ? 11.179  5.822   18.498  1.00 41.28 ? 255  LEU A CA  1 
ATOM   1933 C C   . LEU A 1 255 ? 11.791  7.126   19.057  1.00 40.78 ? 255  LEU A C   1 
ATOM   1934 O O   . LEU A 1 255 ? 12.832  7.590   18.555  1.00 41.10 ? 255  LEU A O   1 
ATOM   1935 C CB  . LEU A 1 255 ? 11.864  4.574   19.075  1.00 41.30 ? 255  LEU A CB  1 
ATOM   1936 C CG  . LEU A 1 255 ? 11.691  4.193   20.552  1.00 40.44 ? 255  LEU A CG  1 
ATOM   1937 C CD1 . LEU A 1 255 ? 10.230  4.099   20.934  1.00 39.19 ? 255  LEU A CD1 1 
ATOM   1938 C CD2 . LEU A 1 255 ? 12.386  2.877   20.824  1.00 38.48 ? 255  LEU A CD2 1 
ATOM   1939 N N   . SER A 1 256 ? 11.154  7.738   20.055  1.00 39.55 ? 256  SER A N   1 
ATOM   1940 C CA  . SER A 1 256 ? 11.682  9.006   20.601  1.00 39.01 ? 256  SER A CA  1 
ATOM   1941 C C   . SER A 1 256 ? 13.163  8.936   21.012  1.00 38.39 ? 256  SER A C   1 
ATOM   1942 O O   . SER A 1 256 ? 13.634  7.892   21.470  1.00 38.23 ? 256  SER A O   1 
ATOM   1943 C CB  . SER A 1 256 ? 10.862  9.481   21.791  1.00 38.94 ? 256  SER A CB  1 
ATOM   1944 O OG  . SER A 1 256 ? 11.393  10.680  22.301  1.00 38.13 ? 256  SER A OG  1 
ATOM   1945 N N   . PRO A 1 257 ? 13.904  10.042  20.849  1.00 38.00 ? 257  PRO A N   1 
ATOM   1946 C CA  . PRO A 1 257 ? 15.315  10.041  21.291  1.00 37.44 ? 257  PRO A CA  1 
ATOM   1947 C C   . PRO A 1 257 ? 15.467  9.800   22.823  1.00 36.76 ? 257  PRO A C   1 
ATOM   1948 O O   . PRO A 1 257 ? 16.472  9.197   23.265  1.00 36.24 ? 257  PRO A O   1 
ATOM   1949 C CB  . PRO A 1 257 ? 15.821  11.444  20.912  1.00 37.66 ? 257  PRO A CB  1 
ATOM   1950 C CG  . PRO A 1 257 ? 14.800  12.027  19.961  1.00 38.18 ? 257  PRO A CG  1 
ATOM   1951 C CD  . PRO A 1 257 ? 13.489  11.335  20.264  1.00 38.22 ? 257  PRO A CD  1 
ATOM   1952 N N   . PHE A 1 258 ? 14.458  10.256  23.583  1.00 35.12 ? 258  PHE A N   1 
ATOM   1953 C CA  . PHE A 1 258 ? 14.340  10.055  25.023  1.00 33.85 ? 258  PHE A CA  1 
ATOM   1954 C C   . PHE A 1 258 ? 14.471  8.602   25.450  1.00 32.94 ? 258  PHE A C   1 
ATOM   1955 O O   . PHE A 1 258 ? 15.011  8.303   26.507  1.00 32.42 ? 258  PHE A O   1 
ATOM   1956 C CB  . PHE A 1 258 ? 12.995  10.599  25.524  1.00 33.61 ? 258  PHE A CB  1 
ATOM   1957 C CG  . PHE A 1 258 ? 12.966  12.092  25.705  1.00 33.75 ? 258  PHE A CG  1 
ATOM   1958 C CD1 . PHE A 1 258 ? 13.746  12.710  26.678  1.00 34.09 ? 258  PHE A CD1 1 
ATOM   1959 C CD2 . PHE A 1 258 ? 12.140  12.887  24.918  1.00 34.52 ? 258  PHE A CD2 1 
ATOM   1960 C CE1 . PHE A 1 258 ? 13.703  14.105  26.860  1.00 33.28 ? 258  PHE A CE1 1 
ATOM   1961 C CE2 . PHE A 1 258 ? 12.097  14.289  25.077  1.00 34.09 ? 258  PHE A CE2 1 
ATOM   1962 C CZ  . PHE A 1 258 ? 12.877  14.897  26.048  1.00 33.90 ? 258  PHE A CZ  1 
ATOM   1963 N N   . CYS A 1 259 ? 13.962  7.703   24.624  1.00 32.13 ? 259  CYS A N   1 
ATOM   1964 C CA  . CYS A 1 259 ? 13.942  6.284   24.945  1.00 31.85 ? 259  CYS A CA  1 
ATOM   1965 C C   . CYS A 1 259 ? 15.335  5.675   25.045  1.00 32.22 ? 259  CYS A C   1 
ATOM   1966 O O   . CYS A 1 259 ? 15.540  4.735   25.836  1.00 32.26 ? 259  CYS A O   1 
ATOM   1967 C CB  . CYS A 1 259 ? 13.113  5.518   23.923  1.00 31.40 ? 259  CYS A CB  1 
ATOM   1968 S SG  . CYS A 1 259 ? 11.551  6.280   23.615  1.00 30.66 ? 259  CYS A SG  1 
ATOM   1969 N N   . ASP A 1 260 ? 16.278  6.216   24.269  1.00 31.92 ? 260  ASP A N   1 
ATOM   1970 C CA  . ASP A 1 260 ? 17.621  5.647   24.197  1.00 32.75 ? 260  ASP A CA  1 
ATOM   1971 C C   . ASP A 1 260 ? 18.486  6.008   25.429  1.00 31.86 ? 260  ASP A C   1 
ATOM   1972 O O   . ASP A 1 260 ? 19.507  5.375   25.681  1.00 31.43 ? 260  ASP A O   1 
ATOM   1973 C CB  . ASP A 1 260 ? 18.312  5.998   22.868  1.00 33.25 ? 260  ASP A CB  1 
ATOM   1974 C CG  . ASP A 1 260 ? 19.546  5.098   22.567  1.00 37.74 ? 260  ASP A CG  1 
ATOM   1975 O OD1 . ASP A 1 260 ? 19.650  3.927   23.078  1.00 40.38 ? 260  ASP A OD1 1 
ATOM   1976 O OD2 . ASP A 1 260 ? 20.430  5.583   21.808  1.00 40.18 ? 260  ASP A OD2 1 
ATOM   1977 N N   . LEU A 1 261 ? 18.027  6.986   26.219  1.00 31.00 ? 261  LEU A N   1 
ATOM   1978 C CA  . LEU A 1 261 ? 18.711  7.383   27.468  1.00 29.47 ? 261  LEU A CA  1 
ATOM   1979 C C   . LEU A 1 261 ? 18.526  6.365   28.590  1.00 28.76 ? 261  LEU A C   1 
ATOM   1980 O O   . LEU A 1 261 ? 19.152  6.464   29.635  1.00 29.13 ? 261  LEU A O   1 
ATOM   1981 C CB  . LEU A 1 261 ? 18.231  8.758   27.939  1.00 28.65 ? 261  LEU A CB  1 
ATOM   1982 C CG  . LEU A 1 261 ? 18.214  9.872   26.901  1.00 27.84 ? 261  LEU A CG  1 
ATOM   1983 C CD1 . LEU A 1 261 ? 17.537  11.054  27.534  1.00 25.77 ? 261  LEU A CD1 1 
ATOM   1984 C CD2 . LEU A 1 261 ? 19.637  10.240  26.379  1.00 25.91 ? 261  LEU A CD2 1 
ATOM   1985 N N   . PHE A 1 262 ? 17.679  5.381   28.368  1.00 28.06 ? 262  PHE A N   1 
ATOM   1986 C CA  . PHE A 1 262 ? 17.464  4.343   29.370  1.00 27.57 ? 262  PHE A CA  1 
ATOM   1987 C C   . PHE A 1 262 ? 17.654  2.975   28.736  1.00 27.85 ? 262  PHE A C   1 
ATOM   1988 O O   . PHE A 1 262 ? 17.493  2.823   27.528  1.00 28.47 ? 262  PHE A O   1 
ATOM   1989 C CB  . PHE A 1 262 ? 16.064  4.520   29.952  1.00 26.55 ? 262  PHE A CB  1 
ATOM   1990 C CG  . PHE A 1 262 ? 15.789  5.929   30.384  1.00 25.13 ? 262  PHE A CG  1 
ATOM   1991 C CD1 . PHE A 1 262 ? 16.285  6.411   31.596  1.00 25.23 ? 262  PHE A CD1 1 
ATOM   1992 C CD2 . PHE A 1 262 ? 15.056  6.776   29.595  1.00 21.04 ? 262  PHE A CD2 1 
ATOM   1993 C CE1 . PHE A 1 262 ? 16.040  7.740   32.015  1.00 23.54 ? 262  PHE A CE1 1 
ATOM   1994 C CE2 . PHE A 1 262 ? 14.799  8.087   30.011  1.00 24.49 ? 262  PHE A CE2 1 
ATOM   1995 C CZ  . PHE A 1 262 ? 15.306  8.574   31.225  1.00 23.48 ? 262  PHE A CZ  1 
ATOM   1996 N N   . THR A 1 263 ? 18.034  1.986   29.532  1.00 28.36 ? 263  THR A N   1 
ATOM   1997 C CA  . THR A 1 263 ? 18.294  0.649   29.015  1.00 28.06 ? 263  THR A CA  1 
ATOM   1998 C C   . THR A 1 263 ? 17.023  -0.200  29.074  1.00 29.32 ? 263  THR A C   1 
ATOM   1999 O O   . THR A 1 263 ? 16.045  0.150   29.797  1.00 28.22 ? 263  THR A O   1 
ATOM   2000 C CB  . THR A 1 263 ? 19.330  -0.061  29.848  1.00 28.12 ? 263  THR A CB  1 
ATOM   2001 O OG1 . THR A 1 263 ? 18.785  -0.352  31.142  1.00 25.74 ? 263  THR A OG1 1 
ATOM   2002 C CG2 . THR A 1 263 ? 20.590  0.793   29.982  1.00 28.88 ? 263  THR A CG2 1 
ATOM   2003 N N   . HIS A 1 264 ? 17.055  -1.324  28.341  1.00 29.89 ? 264  HIS A N   1 
ATOM   2004 C CA  . HIS A 1 264 ? 15.938  -2.257  28.323  1.00 31.20 ? 264  HIS A CA  1 
ATOM   2005 C C   . HIS A 1 264 ? 15.520  -2.582  29.749  1.00 31.58 ? 264  HIS A C   1 
ATOM   2006 O O   . HIS A 1 264 ? 14.351  -2.393  30.104  1.00 32.29 ? 264  HIS A O   1 
ATOM   2007 C CB  . HIS A 1 264 ? 16.277  -3.531  27.535  1.00 31.57 ? 264  HIS A CB  1 
ATOM   2008 C CG  . HIS A 1 264 ? 15.142  -4.518  27.435  1.00 33.23 ? 264  HIS A CG  1 
ATOM   2009 N ND1 . HIS A 1 264 ? 13.962  -4.245  26.771  1.00 34.14 ? 264  HIS A ND1 1 
ATOM   2010 C CD2 . HIS A 1 264 ? 15.024  -5.791  27.893  1.00 33.93 ? 264  HIS A CD2 1 
ATOM   2011 C CE1 . HIS A 1 264 ? 13.160  -5.294  26.850  1.00 32.98 ? 264  HIS A CE1 1 
ATOM   2012 N NE2 . HIS A 1 264 ? 13.782  -6.247  27.518  1.00 33.11 ? 264  HIS A NE2 1 
ATOM   2013 N N   . ASP A 1 265 ? 16.486  -3.011  30.565  1.00 31.45 ? 265  ASP A N   1 
ATOM   2014 C CA  . ASP A 1 265 ? 16.231  -3.460  31.932  1.00 31.59 ? 265  ASP A CA  1 
ATOM   2015 C C   . ASP A 1 265 ? 15.617  -2.335  32.770  1.00 30.45 ? 265  ASP A C   1 
ATOM   2016 O O   . ASP A 1 265 ? 14.694  -2.555  33.580  1.00 29.76 ? 265  ASP A O   1 
ATOM   2017 C CB  . ASP A 1 265 ? 17.518  -4.042  32.562  1.00 32.54 ? 265  ASP A CB  1 
ATOM   2018 C CG  . ASP A 1 265 ? 17.441  -4.110  34.077  1.00 36.20 ? 265  ASP A CG  1 
ATOM   2019 O OD1 . ASP A 1 265 ? 18.015  -3.206  34.763  1.00 39.32 ? 265  ASP A OD1 1 
ATOM   2020 O OD2 . ASP A 1 265 ? 16.779  -5.054  34.575  1.00 39.40 ? 265  ASP A OD2 1 
ATOM   2021 N N   . GLU A 1 266 ? 16.121  -1.129  32.540  1.00 29.27 ? 266  GLU A N   1 
ATOM   2022 C CA  . GLU A 1 266 ? 15.521  0.075   33.082  1.00 28.08 ? 266  GLU A CA  1 
ATOM   2023 C C   . GLU A 1 266 ? 14.095  0.288   32.609  1.00 27.47 ? 266  GLU A C   1 
ATOM   2024 O O   . GLU A 1 266 ? 13.262  0.682   33.426  1.00 27.88 ? 266  GLU A O   1 
ATOM   2025 C CB  . GLU A 1 266 ? 16.372  1.282   32.788  1.00 28.15 ? 266  GLU A CB  1 
ATOM   2026 C CG  . GLU A 1 266 ? 17.500  1.415   33.787  1.00 29.43 ? 266  GLU A CG  1 
ATOM   2027 C CD  . GLU A 1 266 ? 18.656  2.260   33.272  1.00 31.69 ? 266  GLU A CD  1 
ATOM   2028 O OE1 . GLU A 1 266 ? 18.435  3.222   32.482  1.00 29.68 ? 266  GLU A OE1 1 
ATOM   2029 O OE2 . GLU A 1 266 ? 19.800  1.956   33.679  1.00 34.27 ? 266  GLU A OE2 1 
ATOM   2030 N N   . TRP A 1 267 ? 13.797  -0.011  31.336  1.00 25.83 ? 267  TRP A N   1 
ATOM   2031 C CA  . TRP A 1 267 ? 12.406  -0.058  30.882  1.00 24.44 ? 267  TRP A CA  1 
ATOM   2032 C C   . TRP A 1 267 ? 11.567  -1.114  31.632  1.00 24.80 ? 267  TRP A C   1 
ATOM   2033 O O   . TRP A 1 267 ? 10.423  -0.850  32.016  1.00 24.44 ? 267  TRP A O   1 
ATOM   2034 C CB  . TRP A 1 267 ? 12.287  -0.174  29.357  1.00 23.58 ? 267  TRP A CB  1 
ATOM   2035 C CG  . TRP A 1 267 ? 12.639  1.135   28.720  1.00 21.29 ? 267  TRP A CG  1 
ATOM   2036 C CD1 . TRP A 1 267 ? 13.709  1.406   27.875  1.00 18.84 ? 267  TRP A CD1 1 
ATOM   2037 C CD2 . TRP A 1 267 ? 11.977  2.379   28.928  1.00 17.47 ? 267  TRP A CD2 1 
ATOM   2038 N NE1 . TRP A 1 267 ? 13.715  2.738   27.537  1.00 17.22 ? 267  TRP A NE1 1 
ATOM   2039 C CE2 . TRP A 1 267 ? 12.672  3.360   28.173  1.00 18.04 ? 267  TRP A CE2 1 
ATOM   2040 C CE3 . TRP A 1 267 ? 10.851  2.768   29.672  1.00 18.95 ? 267  TRP A CE3 1 
ATOM   2041 C CZ2 . TRP A 1 267 ? 12.280  4.695   28.152  1.00 17.47 ? 267  TRP A CZ2 1 
ATOM   2042 C CZ3 . TRP A 1 267 ? 10.471  4.103   29.652  1.00 18.33 ? 267  TRP A CZ3 1 
ATOM   2043 C CH2 . TRP A 1 267 ? 11.187  5.048   28.906  1.00 18.37 ? 267  TRP A CH2 1 
ATOM   2044 N N   . ILE A 1 268 ? 12.155  -2.277  31.893  1.00 24.54 ? 268  ILE A N   1 
ATOM   2045 C CA  . ILE A 1 268 ? 11.459  -3.324  32.631  1.00 25.02 ? 268  ILE A CA  1 
ATOM   2046 C C   . ILE A 1 268 ? 10.954  -2.876  34.002  1.00 25.17 ? 268  ILE A C   1 
ATOM   2047 O O   . ILE A 1 268 ? 9.797   -3.174  34.384  1.00 25.23 ? 268  ILE A O   1 
ATOM   2048 C CB  . ILE A 1 268 ? 12.303  -4.590  32.760  1.00 25.18 ? 268  ILE A CB  1 
ATOM   2049 C CG1 . ILE A 1 268 ? 12.265  -5.363  31.450  1.00 25.53 ? 268  ILE A CG1 1 
ATOM   2050 C CG2 . ILE A 1 268 ? 11.762  -5.487  33.861  1.00 25.44 ? 268  ILE A CG2 1 
ATOM   2051 C CD1 . ILE A 1 268 ? 13.128  -6.606  31.454  1.00 27.59 ? 268  ILE A CD1 1 
ATOM   2052 N N   . ASN A 1 269 ? 11.809  -2.157  34.722  1.00 23.91 ? 269  ASN A N   1 
ATOM   2053 C CA  . ASN A 1 269 ? 11.430  -1.608  35.992  1.00 23.09 ? 269  ASN A CA  1 
ATOM   2054 C C   . ASN A 1 269 ? 10.344  -0.569  35.806  1.00 22.88 ? 269  ASN A C   1 
ATOM   2055 O O   . ASN A 1 269 ? 9.332   -0.587  36.521  1.00 23.83 ? 269  ASN A O   1 
ATOM   2056 C CB  . ASN A 1 269 ? 12.640  -1.011  36.716  1.00 23.09 ? 269  ASN A CB  1 
ATOM   2057 C CG  . ASN A 1 269 ? 13.611  -2.068  37.211  1.00 25.03 ? 269  ASN A CG  1 
ATOM   2058 O OD1 . ASN A 1 269 ? 13.283  -2.918  38.039  1.00 27.69 ? 269  ASN A OD1 1 
ATOM   2059 N ND2 . ASN A 1 269 ? 14.818  -2.010  36.710  1.00 26.89 ? 269  ASN A ND2 1 
ATOM   2060 N N   . TYR A 1 270 ? 10.541  0.344   34.854  1.00 22.43 ? 270  TYR A N   1 
ATOM   2061 C CA  . TYR A 1 270 ? 9.529   1.359   34.564  1.00 21.32 ? 270  TYR A CA  1 
ATOM   2062 C C   . TYR A 1 270 ? 8.138   0.728   34.407  1.00 20.88 ? 270  TYR A C   1 
ATOM   2063 O O   . TYR A 1 270 ? 7.178   1.114   35.115  1.00 19.42 ? 270  TYR A O   1 
ATOM   2064 C CB  . TYR A 1 270 ? 9.892   2.131   33.318  1.00 21.36 ? 270  TYR A CB  1 
ATOM   2065 C CG  . TYR A 1 270 ? 8.969   3.303   33.029  1.00 22.44 ? 270  TYR A CG  1 
ATOM   2066 C CD1 . TYR A 1 270 ? 9.119   4.528   33.683  1.00 21.02 ? 270  TYR A CD1 1 
ATOM   2067 C CD2 . TYR A 1 270 ? 7.944   3.179   32.098  1.00 22.26 ? 270  TYR A CD2 1 
ATOM   2068 C CE1 . TYR A 1 270 ? 8.252   5.598   33.413  1.00 20.47 ? 270  TYR A CE1 1 
ATOM   2069 C CE2 . TYR A 1 270 ? 7.075   4.220   31.839  1.00 22.11 ? 270  TYR A CE2 1 
ATOM   2070 C CZ  . TYR A 1 270 ? 7.236   5.432   32.478  1.00 23.30 ? 270  TYR A CZ  1 
ATOM   2071 O OH  . TYR A 1 270 ? 6.359   6.469   32.149  1.00 21.84 ? 270  TYR A OH  1 
ATOM   2072 N N   . ASP A 1 271 ? 8.046   -0.279  33.528  1.00 20.20 ? 271  ASP A N   1 
ATOM   2073 C CA  . ASP A 1 271 ? 6.779   -0.975  33.316  1.00 19.88 ? 271  ASP A CA  1 
ATOM   2074 C C   . ASP A 1 271 ? 6.203   -1.491  34.617  1.00 19.94 ? 271  ASP A C   1 
ATOM   2075 O O   . ASP A 1 271 ? 5.028   -1.240  34.941  1.00 20.72 ? 271  ASP A O   1 
ATOM   2076 C CB  . ASP A 1 271 ? 6.942   -2.102  32.306  1.00 20.46 ? 271  ASP A CB  1 
ATOM   2077 C CG  . ASP A 1 271 ? 5.634   -2.781  31.977  1.00 20.12 ? 271  ASP A CG  1 
ATOM   2078 O OD1 . ASP A 1 271 ? 4.790   -2.158  31.292  1.00 15.30 ? 271  ASP A OD1 1 
ATOM   2079 O OD2 . ASP A 1 271 ? 5.488   -3.952  32.398  1.00 20.16 ? 271  ASP A OD2 1 
ATOM   2080 N N   . TYR A 1 272 ? 7.055   -2.147  35.402  1.00 19.28 ? 272  TYR A N   1 
ATOM   2081 C CA  . TYR A 1 272 ? 6.621   -2.777  36.619  1.00 18.51 ? 272  TYR A CA  1 
ATOM   2082 C C   . TYR A 1 272 ? 6.165   -1.762  37.631  1.00 18.33 ? 272  TYR A C   1 
ATOM   2083 O O   . TYR A 1 272 ? 5.161   -1.990  38.334  1.00 17.85 ? 272  TYR A O   1 
ATOM   2084 C CB  . TYR A 1 272 ? 7.737   -3.647  37.206  1.00 19.15 ? 272  TYR A CB  1 
ATOM   2085 C CG  . TYR A 1 272 ? 7.244   -4.487  38.360  1.00 19.62 ? 272  TYR A CG  1 
ATOM   2086 C CD1 . TYR A 1 272 ? 6.378   -5.579  38.146  1.00 20.49 ? 272  TYR A CD1 1 
ATOM   2087 C CD2 . TYR A 1 272 ? 7.609   -4.183  39.655  1.00 19.20 ? 272  TYR A CD2 1 
ATOM   2088 C CE1 . TYR A 1 272 ? 5.899   -6.334  39.221  1.00 21.99 ? 272  TYR A CE1 1 
ATOM   2089 C CE2 . TYR A 1 272 ? 7.155   -4.947  40.724  1.00 21.11 ? 272  TYR A CE2 1 
ATOM   2090 C CZ  . TYR A 1 272 ? 6.305   -6.008  40.509  1.00 21.34 ? 272  TYR A CZ  1 
ATOM   2091 O OH  . TYR A 1 272 ? 5.845   -6.726  41.598  1.00 23.35 ? 272  TYR A OH  1 
ATOM   2092 N N   . LEU A 1 273 ? 6.901   -0.649  37.711  1.00 18.01 ? 273  LEU A N   1 
ATOM   2093 C CA  . LEU A 1 273 ? 6.452   0.482   38.525  1.00 18.23 ? 273  LEU A CA  1 
ATOM   2094 C C   . LEU A 1 273 ? 5.006   0.837   38.194  1.00 18.23 ? 273  LEU A C   1 
ATOM   2095 O O   . LEU A 1 273 ? 4.211   1.070   39.105  1.00 19.33 ? 273  LEU A O   1 
ATOM   2096 C CB  . LEU A 1 273 ? 7.292   1.732   38.311  1.00 17.43 ? 273  LEU A CB  1 
ATOM   2097 C CG  . LEU A 1 273 ? 6.633   2.983   38.951  1.00 19.20 ? 273  LEU A CG  1 
ATOM   2098 C CD1 . LEU A 1 273 ? 6.875   3.098   40.481  1.00 20.40 ? 273  LEU A CD1 1 
ATOM   2099 C CD2 . LEU A 1 273 ? 7.113   4.234   38.314  1.00 22.29 ? 273  LEU A CD2 1 
ATOM   2100 N N   . GLN A 1 274 ? 4.686   0.923   36.894  1.00 18.39 ? 274  GLN A N   1 
ATOM   2101 C CA  . GLN A 1 274 ? 3.352   1.344   36.439  1.00 17.51 ? 274  GLN A CA  1 
ATOM   2102 C C   . GLN A 1 274 ? 2.328   0.269   36.855  1.00 17.09 ? 274  GLN A C   1 
ATOM   2103 O O   . GLN A 1 274 ? 1.254   0.596   37.345  1.00 18.08 ? 274  GLN A O   1 
ATOM   2104 C CB  . GLN A 1 274 ? 3.295   1.560   34.917  1.00 17.83 ? 274  GLN A CB  1 
ATOM   2105 C CG  . GLN A 1 274 ? 4.223   2.573   34.255  1.00 16.39 ? 274  GLN A CG  1 
ATOM   2106 C CD  . GLN A 1 274 ? 4.415   3.882   35.016  1.00 22.83 ? 274  GLN A CD  1 
ATOM   2107 O OE1 . GLN A 1 274 ? 3.468   4.488   35.554  1.00 24.24 ? 274  GLN A OE1 1 
ATOM   2108 N NE2 . GLN A 1 274 ? 5.674   4.352   35.034  1.00 24.23 ? 274  GLN A NE2 1 
ATOM   2109 N N   . SER A 1 275 ? 2.669   -1.003  36.710  1.00 15.71 ? 275  SER A N   1 
ATOM   2110 C CA  . SER A 1 275 ? 1.799   -2.043  37.221  1.00 15.64 ? 275  SER A CA  1 
ATOM   2111 C C   . SER A 1 275 ? 1.525   -1.843  38.709  1.00 15.94 ? 275  SER A C   1 
ATOM   2112 O O   . SER A 1 275 ? 0.402   -2.061  39.140  1.00 14.66 ? 275  SER A O   1 
ATOM   2113 C CB  . SER A 1 275 ? 2.381   -3.435  36.974  1.00 15.33 ? 275  SER A CB  1 
ATOM   2114 O OG  . SER A 1 275 ? 2.515   -3.683  35.609  1.00 15.39 ? 275  SER A OG  1 
ATOM   2115 N N   . LEU A 1 276 ? 2.551   -1.437  39.482  1.00 16.62 ? 276  LEU A N   1 
ATOM   2116 C CA  . LEU A 1 276 ? 2.375   -1.176  40.951  1.00 17.26 ? 276  LEU A CA  1 
ATOM   2117 C C   . LEU A 1 276 ? 1.445   -0.010  41.313  1.00 17.14 ? 276  LEU A C   1 
ATOM   2118 O O   . LEU A 1 276 ? 0.571   -0.158  42.210  1.00 17.05 ? 276  LEU A O   1 
ATOM   2119 C CB  . LEU A 1 276 ? 3.712   -0.926  41.654  1.00 17.47 ? 276  LEU A CB  1 
ATOM   2120 C CG  . LEU A 1 276 ? 4.610   -2.131  41.936  1.00 18.61 ? 276  LEU A CG  1 
ATOM   2121 C CD1 . LEU A 1 276 ? 5.982   -1.618  42.332  1.00 15.04 ? 276  LEU A CD1 1 
ATOM   2122 C CD2 . LEU A 1 276 ? 3.997   -2.983  43.047  1.00 20.17 ? 276  LEU A CD2 1 
ATOM   2123 N N   . LYS A 1 277 ? 1.661   1.134   40.657  1.00 15.94 ? 277  LYS A N   1 
ATOM   2124 C CA  . LYS A 1 277 ? 0.753   2.270   40.787  1.00 16.69 ? 277  LYS A CA  1 
ATOM   2125 C C   . LYS A 1 277 ? -0.718  1.804   40.585  1.00 16.90 ? 277  LYS A C   1 
ATOM   2126 O O   . LYS A 1 277 ? -1.585  2.094   41.422  1.00 16.38 ? 277  LYS A O   1 
ATOM   2127 C CB  . LYS A 1 277 ? 1.069   3.394   39.787  1.00 17.03 ? 277  LYS A CB  1 
ATOM   2128 C CG  . LYS A 1 277 ? 2.469   4.094   39.802  1.00 18.12 ? 277  LYS A CG  1 
ATOM   2129 C CD  . LYS A 1 277 ? 2.212   5.590   39.287  1.00 20.81 ? 277  LYS A CD  1 
ATOM   2130 C CE  . LYS A 1 277 ? 3.417   6.238   38.564  1.00 26.37 ? 277  LYS A CE  1 
ATOM   2131 N NZ  . LYS A 1 277 ? 3.187   7.150   37.333  1.00 25.03 ? 277  LYS A NZ  1 
ATOM   2132 N N   . LYS A 1 278 ? -0.980  1.058   39.493  1.00 16.88 ? 278  LYS A N   1 
ATOM   2133 C CA  . LYS A 1 278 ? -2.327  0.554   39.199  1.00 16.56 ? 278  LYS A CA  1 
ATOM   2134 C C   . LYS A 1 278 ? -2.786  -0.509  40.191  1.00 17.25 ? 278  LYS A C   1 
ATOM   2135 O O   . LYS A 1 278 ? -3.885  -0.377  40.760  1.00 17.28 ? 278  LYS A O   1 
ATOM   2136 C CB  . LYS A 1 278 ? -2.490  0.103   37.729  1.00 16.36 ? 278  LYS A CB  1 
ATOM   2137 C CG  . LYS A 1 278 ? -2.238  1.243   36.681  1.00 16.87 ? 278  LYS A CG  1 
ATOM   2138 C CD  . LYS A 1 278 ? -2.820  2.614   37.108  1.00 15.08 ? 278  LYS A CD  1 
ATOM   2139 C CE  . LYS A 1 278 ? -2.846  3.620   35.954  1.00 15.42 ? 278  LYS A CE  1 
ATOM   2140 N NZ  . LYS A 1 278 ? -3.604  4.885   36.325  1.00 13.25 ? 278  LYS A NZ  1 
ATOM   2141 N N   . TYR A 1 279 ? -1.952  -1.522  40.459  1.00 17.22 ? 279  TYR A N   1 
ATOM   2142 C CA  . TYR A 1 279 ? -2.346  -2.559  41.421  1.00 17.93 ? 279  TYR A CA  1 
ATOM   2143 C C   . TYR A 1 279 ? -2.700  -2.078  42.823  1.00 18.42 ? 279  TYR A C   1 
ATOM   2144 O O   . TYR A 1 279 ? -3.715  -2.554  43.413  1.00 18.69 ? 279  TYR A O   1 
ATOM   2145 C CB  . TYR A 1 279 ? -1.283  -3.642  41.525  1.00 18.28 ? 279  TYR A CB  1 
ATOM   2146 C CG  . TYR A 1 279 ? -1.708  -4.845  42.326  1.00 19.52 ? 279  TYR A CG  1 
ATOM   2147 C CD1 . TYR A 1 279 ? -2.518  -5.841  41.767  1.00 21.63 ? 279  TYR A CD1 1 
ATOM   2148 C CD2 . TYR A 1 279 ? -1.296  -5.002  43.642  1.00 20.63 ? 279  TYR A CD2 1 
ATOM   2149 C CE1 . TYR A 1 279 ? -2.908  -6.966  42.517  1.00 21.88 ? 279  TYR A CE1 1 
ATOM   2150 C CE2 . TYR A 1 279 ? -1.678  -6.118  44.392  1.00 21.24 ? 279  TYR A CE2 1 
ATOM   2151 C CZ  . TYR A 1 279 ? -2.474  -7.099  43.838  1.00 22.32 ? 279  TYR A CZ  1 
ATOM   2152 O OH  . TYR A 1 279 ? -2.834  -8.193  44.617  1.00 22.33 ? 279  TYR A OH  1 
ATOM   2153 N N   . TYR A 1 280 ? -1.858  -1.189  43.377  1.00 18.33 ? 280  TYR A N   1 
ATOM   2154 C CA  . TYR A 1 280 ? -2.064  -0.689  44.743  1.00 17.94 ? 280  TYR A CA  1 
ATOM   2155 C C   . TYR A 1 280 ? -2.958  0.556   44.761  1.00 18.48 ? 280  TYR A C   1 
ATOM   2156 O O   . TYR A 1 280 ? -3.482  0.910   45.804  1.00 18.53 ? 280  TYR A O   1 
ATOM   2157 C CB  . TYR A 1 280 ? -0.729  -0.514  45.526  1.00 17.63 ? 280  TYR A CB  1 
ATOM   2158 C CG  . TYR A 1 280 ? -0.106  -1.854  45.881  1.00 15.06 ? 280  TYR A CG  1 
ATOM   2159 C CD1 . TYR A 1 280 ? -0.665  -2.674  46.878  1.00 14.07 ? 280  TYR A CD1 1 
ATOM   2160 C CD2 . TYR A 1 280 ? 1.026   -2.341  45.178  1.00 14.06 ? 280  TYR A CD2 1 
ATOM   2161 C CE1 . TYR A 1 280 ? -0.109  -3.984  47.170  1.00 13.75 ? 280  TYR A CE1 1 
ATOM   2162 C CE2 . TYR A 1 280 ? 1.585   -3.624  45.443  1.00 10.21 ? 280  TYR A CE2 1 
ATOM   2163 C CZ  . TYR A 1 280 ? 1.027   -4.444  46.447  1.00 13.91 ? 280  TYR A CZ  1 
ATOM   2164 O OH  . TYR A 1 280 ? 1.581   -5.728  46.672  1.00 11.18 ? 280  TYR A OH  1 
ATOM   2165 N N   . GLY A 1 281 ? -3.146  1.206   43.608  1.00 18.37 ? 281  GLY A N   1 
ATOM   2166 C CA  . GLY A 1 281 ? -4.016  2.384   43.514  1.00 17.45 ? 281  GLY A CA  1 
ATOM   2167 C C   . GLY A 1 281 ? -5.489  2.007   43.402  1.00 18.02 ? 281  GLY A C   1 
ATOM   2168 O O   . GLY A 1 281 ? -6.332  2.599   44.072  1.00 17.14 ? 281  GLY A O   1 
ATOM   2169 N N   . HIS A 1 282 ? -5.788  0.998   42.568  1.00 18.39 ? 282  HIS A N   1 
ATOM   2170 C CA  . HIS A 1 282 ? -7.152  0.723   42.143  1.00 18.85 ? 282  HIS A CA  1 
ATOM   2171 C C   . HIS A 1 282 ? -7.531  -0.767  42.084  1.00 18.87 ? 282  HIS A C   1 
ATOM   2172 O O   . HIS A 1 282 ? -8.722  -1.140  42.209  1.00 18.66 ? 282  HIS A O   1 
ATOM   2173 C CB  . HIS A 1 282 ? -7.420  1.440   40.820  1.00 18.71 ? 282  HIS A CB  1 
ATOM   2174 C CG  . HIS A 1 282 ? -7.308  2.919   40.931  1.00 20.27 ? 282  HIS A CG  1 
ATOM   2175 N ND1 . HIS A 1 282 ? -8.389  3.727   41.243  1.00 21.47 ? 282  HIS A ND1 1 
ATOM   2176 C CD2 . HIS A 1 282 ? -6.236  3.736   40.827  1.00 21.56 ? 282  HIS A CD2 1 
ATOM   2177 C CE1 . HIS A 1 282 ? -7.982  4.981   41.313  1.00 22.75 ? 282  HIS A CE1 1 
ATOM   2178 N NE2 . HIS A 1 282 ? -6.681  5.013   41.070  1.00 25.14 ? 282  HIS A NE2 1 
ATOM   2179 N N   . GLY A 1 283 ? -6.529  -1.606  41.931  1.00 17.81 ? 283  GLY A N   1 
ATOM   2180 C CA  . GLY A 1 283 ? -6.753  -3.038  41.947  1.00 17.43 ? 283  GLY A CA  1 
ATOM   2181 C C   . GLY A 1 283 ? -6.760  -3.643  43.339  1.00 17.49 ? 283  GLY A C   1 
ATOM   2182 O O   . GLY A 1 283 ? -7.051  -2.952  44.322  1.00 17.43 ? 283  GLY A O   1 
ATOM   2183 N N   . ALA A 1 284 ? -6.464  -4.950  43.395  1.00 17.40 ? 284  ALA A N   1 
ATOM   2184 C CA  . ALA A 1 284 ? -6.578  -5.785  44.592  1.00 17.48 ? 284  ALA A CA  1 
ATOM   2185 C C   . ALA A 1 284 ? -5.671  -5.387  45.720  1.00 17.62 ? 284  ALA A C   1 
ATOM   2186 O O   . ALA A 1 284 ? -5.999  -5.617  46.893  1.00 17.68 ? 284  ALA A O   1 
ATOM   2187 C CB  . ALA A 1 284 ? -6.347  -7.259  44.260  1.00 17.46 ? 284  ALA A CB  1 
ATOM   2188 N N   . GLY A 1 285 ? -4.505  -4.857  45.391  1.00 17.29 ? 285  GLY A N   1 
ATOM   2189 C CA  . GLY A 1 285 ? -3.618  -4.424  46.433  1.00 17.55 ? 285  GLY A CA  1 
ATOM   2190 C C   . GLY A 1 285 ? -4.121  -3.277  47.294  1.00 17.48 ? 285  GLY A C   1 
ATOM   2191 O O   . GLY A 1 285 ? -3.506  -2.974  48.315  1.00 17.74 ? 285  GLY A O   1 
ATOM   2192 N N   . ASN A 1 286 ? -5.204  -2.617  46.873  1.00 16.96 ? 286  ASN A N   1 
ATOM   2193 C CA  . ASN A 1 286 ? -5.788  -1.537  47.644  1.00 16.63 ? 286  ASN A CA  1 
ATOM   2194 C C   . ASN A 1 286 ? -7.117  -1.990  48.268  1.00 17.29 ? 286  ASN A C   1 
ATOM   2195 O O   . ASN A 1 286 ? -7.988  -2.457  47.580  1.00 16.54 ? 286  ASN A O   1 
ATOM   2196 C CB  . ASN A 1 286 ? -6.028  -0.362  46.745  1.00 15.65 ? 286  ASN A CB  1 
ATOM   2197 C CG  . ASN A 1 286 ? -6.502  0.802   47.488  1.00 17.60 ? 286  ASN A CG  1 
ATOM   2198 O OD1 . ASN A 1 286 ? -7.637  0.832   48.012  1.00 22.76 ? 286  ASN A OD1 1 
ATOM   2199 N ND2 . ASN A 1 286 ? -5.650  1.794   47.582  1.00 13.75 ? 286  ASN A ND2 1 
ATOM   2200 N N   . PRO A 1 287 ? -7.281  -1.821  49.579  1.00 18.20 ? 287  PRO A N   1 
ATOM   2201 C CA  . PRO A 1 287 ? -8.426  -2.471  50.233  1.00 18.47 ? 287  PRO A CA  1 
ATOM   2202 C C   . PRO A 1 287 ? -9.778  -2.088  49.661  1.00 18.25 ? 287  PRO A C   1 
ATOM   2203 O O   . PRO A 1 287 ? -10.700 -2.862  49.763  1.00 19.03 ? 287  PRO A O   1 
ATOM   2204 C CB  . PRO A 1 287 ? -8.352  -1.991  51.685  1.00 18.06 ? 287  PRO A CB  1 
ATOM   2205 C CG  . PRO A 1 287 ? -7.409  -0.830  51.688  1.00 19.27 ? 287  PRO A CG  1 
ATOM   2206 C CD  . PRO A 1 287 ? -6.557  -0.874  50.455  1.00 18.28 ? 287  PRO A CD  1 
ATOM   2207 N N   . LEU A 1 288 ? -9.875  -0.906  49.070  1.00 18.13 ? 288  LEU A N   1 
ATOM   2208 C CA  . LEU A 1 288 ? -11.123 -0.367  48.551  1.00 16.98 ? 288  LEU A CA  1 
ATOM   2209 C C   . LEU A 1 288 ? -11.136 -0.284  47.027  1.00 16.68 ? 288  LEU A C   1 
ATOM   2210 O O   . LEU A 1 288 ? -12.096 0.200   46.432  1.00 17.67 ? 288  LEU A O   1 
ATOM   2211 C CB  . LEU A 1 288 ? -11.314 1.028   49.141  1.00 17.47 ? 288  LEU A CB  1 
ATOM   2212 C CG  . LEU A 1 288 ? -12.026 1.037   50.506  1.00 19.58 ? 288  LEU A CG  1 
ATOM   2213 C CD1 . LEU A 1 288 ? -12.069 2.425   51.141  1.00 19.35 ? 288  LEU A CD1 1 
ATOM   2214 C CD2 . LEU A 1 288 ? -13.459 0.473   50.352  1.00 21.53 ? 288  LEU A CD2 1 
ATOM   2215 N N   . GLY A 1 289 ? -10.057 -0.742  46.393  1.00 15.57 ? 289  GLY A N   1 
ATOM   2216 C CA  . GLY A 1 289 ? -9.908  -0.676  44.961  1.00 14.10 ? 289  GLY A CA  1 
ATOM   2217 C C   . GLY A 1 289 ? -10.943 -1.462  44.168  1.00 13.15 ? 289  GLY A C   1 
ATOM   2218 O O   . GLY A 1 289 ? -11.652 -0.865  43.376  1.00 12.20 ? 289  GLY A O   1 
ATOM   2219 N N   . PRO A 1 290 ? -11.012 -2.810  44.355  1.00 12.57 ? 290  PRO A N   1 
ATOM   2220 C CA  . PRO A 1 290 ? -12.033 -3.611  43.640  1.00 12.20 ? 290  PRO A CA  1 
ATOM   2221 C C   . PRO A 1 290 ? -13.466 -3.127  44.035  1.00 13.51 ? 290  PRO A C   1 
ATOM   2222 O O   . PRO A 1 290 ? -14.463 -3.386  43.313  1.00 11.96 ? 290  PRO A O   1 
ATOM   2223 C CB  . PRO A 1 290 ? -11.810 -5.054  44.158  1.00 11.54 ? 290  PRO A CB  1 
ATOM   2224 C CG  . PRO A 1 290 ? -10.445 -5.079  44.847  1.00 12.34 ? 290  PRO A CG  1 
ATOM   2225 C CD  . PRO A 1 290 ? -10.218 -3.617  45.307  1.00 12.45 ? 290  PRO A CD  1 
ATOM   2226 N N   . THR A 1 291 ? -13.568 -2.419  45.164  1.00 13.45 ? 291  THR A N   1 
ATOM   2227 C CA  . THR A 1 291 ? -14.870 -1.963  45.581  1.00 14.66 ? 291  THR A CA  1 
ATOM   2228 C C   . THR A 1 291 ? -15.265 -0.803  44.666  1.00 15.50 ? 291  THR A C   1 
ATOM   2229 O O   . THR A 1 291 ? -16.450 -0.484  44.499  1.00 16.41 ? 291  THR A O   1 
ATOM   2230 C CB  . THR A 1 291 ? -14.881 -1.545  47.056  1.00 14.65 ? 291  THR A CB  1 
ATOM   2231 O OG1 . THR A 1 291 ? -15.245 -2.684  47.871  1.00 14.26 ? 291  THR A OG1 1 
ATOM   2232 C CG2 . THR A 1 291 ? -15.822 -0.372  47.261  1.00 11.40 ? 291  THR A CG2 1 
ATOM   2233 N N   . GLN A 1 292 ? -14.274 -0.171  44.060  1.00 15.24 ? 292  GLN A N   1 
ATOM   2234 C CA  . GLN A 1 292 ? -14.591 0.861   43.059  1.00 15.63 ? 292  GLN A CA  1 
ATOM   2235 C C   . GLN A 1 292 ? -15.283 0.232   41.824  1.00 15.25 ? 292  GLN A C   1 
ATOM   2236 O O   . GLN A 1 292 ? -16.004 0.903   41.132  1.00 14.06 ? 292  GLN A O   1 
ATOM   2237 C CB  . GLN A 1 292 ? -13.340 1.688   42.690  1.00 15.65 ? 292  GLN A CB  1 
ATOM   2238 C CG  . GLN A 1 292 ? -12.709 2.409   43.908  1.00 14.68 ? 292  GLN A CG  1 
ATOM   2239 C CD  . GLN A 1 292 ? -13.778 3.128   44.753  1.00 14.11 ? 292  GLN A CD  1 
ATOM   2240 O OE1 . GLN A 1 292 ? -14.338 4.154   44.334  1.00 15.53 ? 292  GLN A OE1 1 
ATOM   2241 N NE2 . GLN A 1 292 ? -14.038 2.607   45.949  1.00 9.47  ? 292  GLN A NE2 1 
ATOM   2242 N N   . GLY A 1 293 ? -15.110 -1.079  41.608  1.00 15.75 ? 293  GLY A N   1 
ATOM   2243 C CA  . GLY A 1 293 ? -15.698 -1.749  40.443  1.00 15.44 ? 293  GLY A CA  1 
ATOM   2244 C C   . GLY A 1 293 ? -17.069 -2.397  40.649  1.00 15.60 ? 293  GLY A C   1 
ATOM   2245 O O   . GLY A 1 293 ? -17.625 -3.009  39.733  1.00 15.31 ? 293  GLY A O   1 
ATOM   2246 N N   . VAL A 1 294 ? -17.621 -2.339  41.851  1.00 16.05 ? 294  VAL A N   1 
ATOM   2247 C CA  . VAL A 1 294 ? -18.781 -3.184  42.059  1.00 16.14 ? 294  VAL A CA  1 
ATOM   2248 C C   . VAL A 1 294 ? -20.046 -2.676  41.385  1.00 14.78 ? 294  VAL A C   1 
ATOM   2249 O O   . VAL A 1 294 ? -20.830 -3.472  40.960  1.00 14.83 ? 294  VAL A O   1 
ATOM   2250 C CB  . VAL A 1 294 ? -18.953 -3.755  43.530  1.00 16.84 ? 294  VAL A CB  1 
ATOM   2251 C CG1 . VAL A 1 294 ? -17.661 -3.617  44.293  1.00 17.48 ? 294  VAL A CG1 1 
ATOM   2252 C CG2 . VAL A 1 294 ? -20.176 -3.154  44.249  1.00 15.49 ? 294  VAL A CG2 1 
ATOM   2253 N N   . GLY A 1 295 ? -20.158 -1.363  41.203  1.00 15.12 ? 295  GLY A N   1 
ATOM   2254 C CA  . GLY A 1 295 ? -21.268 -0.733  40.500  1.00 13.99 ? 295  GLY A CA  1 
ATOM   2255 C C   . GLY A 1 295 ? -21.392 -1.235  39.071  1.00 14.08 ? 295  GLY A C   1 
ATOM   2256 O O   . GLY A 1 295 ? -22.499 -1.618  38.638  1.00 14.82 ? 295  GLY A O   1 
ATOM   2257 N N   . TYR A 1 296 ? -20.272 -1.250  38.344  1.00 12.37 ? 296  TYR A N   1 
ATOM   2258 C CA  . TYR A 1 296 ? -20.245 -1.679  36.998  1.00 11.93 ? 296  TYR A CA  1 
ATOM   2259 C C   . TYR A 1 296 ? -20.474 -3.165  36.889  1.00 12.55 ? 296  TYR A C   1 
ATOM   2260 O O   . TYR A 1 296 ? -21.118 -3.612  35.958  1.00 13.87 ? 296  TYR A O   1 
ATOM   2261 C CB  . TYR A 1 296 ? -18.882 -1.331  36.350  1.00 13.13 ? 296  TYR A CB  1 
ATOM   2262 C CG  . TYR A 1 296 ? -18.904 -1.436  34.835  1.00 12.56 ? 296  TYR A CG  1 
ATOM   2263 C CD1 . TYR A 1 296 ? -19.411 -0.402  34.042  1.00 14.28 ? 296  TYR A CD1 1 
ATOM   2264 C CD2 . TYR A 1 296 ? -18.479 -2.602  34.200  1.00 16.09 ? 296  TYR A CD2 1 
ATOM   2265 C CE1 . TYR A 1 296 ? -19.422 -0.519  32.639  1.00 17.27 ? 296  TYR A CE1 1 
ATOM   2266 C CE2 . TYR A 1 296 ? -18.471 -2.726  32.814  1.00 16.80 ? 296  TYR A CE2 1 
ATOM   2267 C CZ  . TYR A 1 296 ? -18.933 -1.688  32.033  1.00 19.09 ? 296  TYR A CZ  1 
ATOM   2268 O OH  . TYR A 1 296 ? -18.957 -1.853  30.649  1.00 20.41 ? 296  TYR A OH  1 
ATOM   2269 N N   . ALA A 1 297 ? -19.899 -3.937  37.799  1.00 12.44 ? 297  ALA A N   1 
ATOM   2270 C CA  . ALA A 1 297 ? -20.096 -5.361  37.861  1.00 13.10 ? 297  ALA A CA  1 
ATOM   2271 C C   . ALA A 1 297 ? -21.574 -5.653  38.049  1.00 14.00 ? 297  ALA A C   1 
ATOM   2272 O O   . ALA A 1 297 ? -22.046 -6.611  37.501  1.00 14.71 ? 297  ALA A O   1 
ATOM   2273 C CB  . ALA A 1 297 ? -19.280 -5.990  39.012  1.00 11.77 ? 297  ALA A CB  1 
ATOM   2274 N N   . ASN A 1 298 ? -22.309 -4.848  38.817  1.00 14.90 ? 298  ASN A N   1 
ATOM   2275 C CA  . ASN A 1 298 ? -23.740 -5.158  39.018  1.00 16.10 ? 298  ASN A CA  1 
ATOM   2276 C C   . ASN A 1 298 ? -24.544 -4.768  37.789  1.00 17.05 ? 298  ASN A C   1 
ATOM   2277 O O   . ASN A 1 298 ? -25.540 -5.439  37.475  1.00 17.98 ? 298  ASN A O   1 
ATOM   2278 C CB  . ASN A 1 298 ? -24.332 -4.512  40.285  1.00 15.88 ? 298  ASN A CB  1 
ATOM   2279 C CG  . ASN A 1 298 ? -23.822 -5.154  41.565  1.00 17.39 ? 298  ASN A CG  1 
ATOM   2280 O OD1 . ASN A 1 298 ? -23.880 -6.411  41.759  1.00 15.09 ? 298  ASN A OD1 1 
ATOM   2281 N ND2 . ASN A 1 298 ? -23.308 -4.302  42.461  1.00 15.39 ? 298  ASN A ND2 1 
ATOM   2282 N N   . GLU A 1 299 ? -24.118 -3.706  37.088  1.00 16.31 ? 299  GLU A N   1 
ATOM   2283 C CA  . GLU A 1 299 ? -24.731 -3.369  35.784  1.00 16.05 ? 299  GLU A CA  1 
ATOM   2284 C C   . GLU A 1 299 ? -24.479 -4.462  34.740  1.00 16.46 ? 299  GLU A C   1 
ATOM   2285 O O   . GLU A 1 299 ? -25.389 -4.904  34.059  1.00 15.89 ? 299  GLU A O   1 
ATOM   2286 C CB  . GLU A 1 299 ? -24.226 -2.031  35.285  1.00 15.50 ? 299  GLU A CB  1 
ATOM   2287 C CG  . GLU A 1 299 ? -24.715 -0.914  36.153  1.00 14.57 ? 299  GLU A CG  1 
ATOM   2288 C CD  . GLU A 1 299 ? -24.261 0.426   35.671  1.00 16.65 ? 299  GLU A CD  1 
ATOM   2289 O OE1 . GLU A 1 299 ? -23.128 0.504   35.168  1.00 16.56 ? 299  GLU A OE1 1 
ATOM   2290 O OE2 . GLU A 1 299 ? -25.055 1.385   35.750  1.00 18.19 ? 299  GLU A OE2 1 
ATOM   2291 N N   . LEU A 1 300 ? -23.247 -4.943  34.634  1.00 17.12 ? 300  LEU A N   1 
ATOM   2292 C CA  . LEU A 1 300 ? -23.044 -6.099  33.754  1.00 17.45 ? 300  LEU A CA  1 
ATOM   2293 C C   . LEU A 1 300 ? -23.979 -7.284  34.136  1.00 17.41 ? 300  LEU A C   1 
ATOM   2294 O O   . LEU A 1 300 ? -24.580 -7.903  33.256  1.00 19.01 ? 300  LEU A O   1 
ATOM   2295 C CB  . LEU A 1 300 ? -21.589 -6.531  33.728  1.00 17.04 ? 300  LEU A CB  1 
ATOM   2296 C CG  . LEU A 1 300 ? -21.376 -7.827  32.935  1.00 16.76 ? 300  LEU A CG  1 
ATOM   2297 C CD1 . LEU A 1 300 ? -21.442 -7.534  31.456  1.00 15.65 ? 300  LEU A CD1 1 
ATOM   2298 C CD2 . LEU A 1 300 ? -19.972 -8.457  33.275  1.00 14.75 ? 300  LEU A CD2 1 
ATOM   2299 N N   . ILE A 1 301 ? -24.125 -7.577  35.420  1.00 16.88 ? 301  ILE A N   1 
ATOM   2300 C CA  . ILE A 1 301 ? -24.988 -8.677  35.852  1.00 17.23 ? 301  ILE A CA  1 
ATOM   2301 C C   . ILE A 1 301 ? -26.436 -8.465  35.361  1.00 17.26 ? 301  ILE A C   1 
ATOM   2302 O O   . ILE A 1 301 ? -27.023 -9.353  34.758  1.00 18.13 ? 301  ILE A O   1 
ATOM   2303 C CB  . ILE A 1 301 ? -24.889 -8.905  37.384  1.00 17.20 ? 301  ILE A CB  1 
ATOM   2304 C CG1 . ILE A 1 301 ? -23.667 -9.706  37.744  1.00 15.94 ? 301  ILE A CG1 1 
ATOM   2305 C CG2 . ILE A 1 301 ? -26.155 -9.581  37.985  1.00 16.73 ? 301  ILE A CG2 1 
ATOM   2306 C CD1 . ILE A 1 301 ? -23.342 -9.531  39.214  1.00 18.99 ? 301  ILE A CD1 1 
ATOM   2307 N N   . ALA A 1 302 ? -26.980 -7.276  35.586  1.00 17.48 ? 302  ALA A N   1 
ATOM   2308 C CA  . ALA A 1 302 ? -28.265 -6.855  35.007  1.00 17.69 ? 302  ALA A CA  1 
ATOM   2309 C C   . ALA A 1 302 ? -28.406 -7.188  33.526  1.00 18.13 ? 302  ALA A C   1 
ATOM   2310 O O   . ALA A 1 302 ? -29.378 -7.806  33.072  1.00 17.59 ? 302  ALA A O   1 
ATOM   2311 C CB  . ALA A 1 302 ? -28.436 -5.354  35.200  1.00 17.39 ? 302  ALA A CB  1 
ATOM   2312 N N   . ARG A 1 303 ? -27.394 -6.774  32.781  1.00 19.15 ? 303  ARG A N   1 
ATOM   2313 C CA  . ARG A 1 303 ? -27.347 -7.003  31.352  1.00 18.84 ? 303  ARG A CA  1 
ATOM   2314 C C   . ARG A 1 303 ? -27.269 -8.483  30.999  1.00 19.56 ? 303  ARG A C   1 
ATOM   2315 O O   . ARG A 1 303 ? -27.945 -8.927  30.093  1.00 20.46 ? 303  ARG A O   1 
ATOM   2316 C CB  . ARG A 1 303 ? -26.207 -6.216  30.730  1.00 18.25 ? 303  ARG A CB  1 
ATOM   2317 C CG  . ARG A 1 303 ? -26.464 -4.744  30.784  1.00 15.33 ? 303  ARG A CG  1 
ATOM   2318 C CD  . ARG A 1 303 ? -25.299 -3.935  30.247  1.00 13.01 ? 303  ARG A CD  1 
ATOM   2319 N NE  . ARG A 1 303 ? -25.678 -2.527  30.087  1.00 11.71 ? 303  ARG A NE  1 
ATOM   2320 C CZ  . ARG A 1 303 ? -24.828 -1.521  29.842  1.00 14.52 ? 303  ARG A CZ  1 
ATOM   2321 N NH1 . ARG A 1 303 ? -23.513 -1.759  29.706  1.00 15.22 ? 303  ARG A NH1 1 
ATOM   2322 N NH2 . ARG A 1 303 ? -25.293 -0.279  29.666  1.00 8.64  ? 303  ARG A NH2 1 
ATOM   2323 N N   . LEU A 1 304 ? -26.468 -9.257  31.718  1.00 20.46 ? 304  LEU A N   1 
ATOM   2324 C CA  . LEU A 1 304 ? -26.307 -10.642 31.362  1.00 19.81 ? 304  LEU A CA  1 
ATOM   2325 C C   . LEU A 1 304 ? -27.555 -11.393 31.706  1.00 20.66 ? 304  LEU A C   1 
ATOM   2326 O O   . LEU A 1 304 ? -27.848 -12.383 31.031  1.00 20.88 ? 304  LEU A O   1 
ATOM   2327 C CB  . LEU A 1 304 ? -25.147 -11.268 32.092  1.00 19.45 ? 304  LEU A CB  1 
ATOM   2328 C CG  . LEU A 1 304 ? -23.684 -10.954 31.781  1.00 19.95 ? 304  LEU A CG  1 
ATOM   2329 C CD1 . LEU A 1 304 ? -22.838 -11.811 32.701  1.00 16.23 ? 304  LEU A CD1 1 
ATOM   2330 C CD2 . LEU A 1 304 ? -23.277 -11.140 30.297  1.00 20.12 ? 304  LEU A CD2 1 
ATOM   2331 N N   . THR A 1 305 ? -28.265 -10.939 32.756  1.00 20.96 ? 305  THR A N   1 
ATOM   2332 C CA  . THR A 1 305 ? -29.516 -11.584 33.226  1.00 21.69 ? 305  THR A CA  1 
ATOM   2333 C C   . THR A 1 305 ? -30.817 -10.885 32.823  1.00 22.46 ? 305  THR A C   1 
ATOM   2334 O O   . THR A 1 305 ? -31.886 -11.347 33.216  1.00 22.47 ? 305  THR A O   1 
ATOM   2335 C CB  . THR A 1 305 ? -29.563 -11.712 34.760  1.00 21.43 ? 305  THR A CB  1 
ATOM   2336 O OG1 . THR A 1 305 ? -29.253 -10.447 35.339  1.00 22.14 ? 305  THR A OG1 1 
ATOM   2337 C CG2 . THR A 1 305 ? -28.582 -12.766 35.288  1.00 21.50 ? 305  THR A CG2 1 
ATOM   2338 N N   . HIS A 1 306 ? -30.729 -9.768  32.073  1.00 23.47 ? 306  HIS A N   1 
ATOM   2339 C CA  . HIS A 1 306 ? -31.900 -9.043  31.544  1.00 23.30 ? 306  HIS A CA  1 
ATOM   2340 C C   . HIS A 1 306 ? -32.886 -8.805  32.663  1.00 24.46 ? 306  HIS A C   1 
ATOM   2341 O O   . HIS A 1 306 ? -34.120 -9.013  32.492  1.00 23.87 ? 306  HIS A O   1 
ATOM   2342 C CB  . HIS A 1 306 ? -32.586 -9.821  30.417  1.00 23.32 ? 306  HIS A CB  1 
ATOM   2343 C CG  . HIS A 1 306 ? -31.632 -10.518 29.494  1.00 24.91 ? 306  HIS A CG  1 
ATOM   2344 N ND1 . HIS A 1 306 ? -30.928 -9.859  28.504  1.00 25.72 ? 306  HIS A ND1 1 
ATOM   2345 C CD2 . HIS A 1 306 ? -31.255 -11.822 29.422  1.00 25.48 ? 306  HIS A CD2 1 
ATOM   2346 C CE1 . HIS A 1 306 ? -30.151 -10.725 27.871  1.00 26.38 ? 306  HIS A CE1 1 
ATOM   2347 N NE2 . HIS A 1 306 ? -30.339 -11.925 28.403  1.00 25.32 ? 306  HIS A NE2 1 
ATOM   2348 N N   . SER A 1 307 ? -32.325 -8.402  33.819  1.00 24.87 ? 307  SER A N   1 
ATOM   2349 C CA  . SER A 1 307 ? -33.052 -8.134  35.071  1.00 24.75 ? 307  SER A CA  1 
ATOM   2350 C C   . SER A 1 307 ? -32.618 -6.770  35.579  1.00 24.81 ? 307  SER A C   1 
ATOM   2351 O O   . SER A 1 307 ? -31.549 -6.300  35.193  1.00 24.37 ? 307  SER A O   1 
ATOM   2352 C CB  . SER A 1 307 ? -32.661 -9.156  36.155  1.00 24.93 ? 307  SER A CB  1 
ATOM   2353 O OG  . SER A 1 307 ? -32.945 -10.473 35.739  1.00 25.39 ? 307  SER A OG  1 
ATOM   2354 N N   . PRO A 1 308 ? -33.417 -6.146  36.473  1.00 25.16 ? 308  PRO A N   1 
ATOM   2355 C CA  . PRO A 1 308 ? -33.044 -4.876  37.127  1.00 25.86 ? 308  PRO A CA  1 
ATOM   2356 C C   . PRO A 1 308 ? -31.658 -4.879  37.854  1.00 26.75 ? 308  PRO A C   1 
ATOM   2357 O O   . PRO A 1 308 ? -31.212 -5.929  38.354  1.00 26.80 ? 308  PRO A O   1 
ATOM   2358 C CB  . PRO A 1 308 ? -34.162 -4.677  38.158  1.00 26.00 ? 308  PRO A CB  1 
ATOM   2359 C CG  . PRO A 1 308 ? -35.344 -5.444  37.609  1.00 26.07 ? 308  PRO A CG  1 
ATOM   2360 C CD  . PRO A 1 308 ? -34.792 -6.576  36.822  1.00 25.26 ? 308  PRO A CD  1 
ATOM   2361 N N   . VAL A 1 309 ? -31.018 -3.706  37.932  1.00 27.02 ? 309  VAL A N   1 
ATOM   2362 C CA  . VAL A 1 309 ? -29.727 -3.558  38.565  1.00 27.31 ? 309  VAL A CA  1 
ATOM   2363 C C   . VAL A 1 309 ? -29.969 -3.693  40.038  1.00 28.47 ? 309  VAL A C   1 
ATOM   2364 O O   . VAL A 1 309 ? -30.912 -3.084  40.555  1.00 28.99 ? 309  VAL A O   1 
ATOM   2365 C CB  . VAL A 1 309 ? -29.105 -2.173  38.295  1.00 27.39 ? 309  VAL A CB  1 
ATOM   2366 C CG1 . VAL A 1 309 ? -27.688 -2.125  38.804  1.00 25.45 ? 309  VAL A CG1 1 
ATOM   2367 C CG2 . VAL A 1 309 ? -29.129 -1.858  36.813  1.00 26.31 ? 309  VAL A CG2 1 
ATOM   2368 N N   . HIS A 1 310 ? -29.153 -4.521  40.702  1.00 29.05 ? 310  HIS A N   1 
ATOM   2369 C CA  . HIS A 1 310 ? -29.117 -4.578  42.166  1.00 29.78 ? 310  HIS A CA  1 
ATOM   2370 C C   . HIS A 1 310 ? -27.770 -4.054  42.648  1.00 29.13 ? 310  HIS A C   1 
ATOM   2371 O O   . HIS A 1 310 ? -26.729 -4.723  42.550  1.00 29.43 ? 310  HIS A O   1 
ATOM   2372 C CB  . HIS A 1 310 ? -29.475 -5.972  42.692  1.00 30.11 ? 310  HIS A CB  1 
ATOM   2373 C CG  . HIS A 1 310 ? -30.801 -6.452  42.179  1.00 35.19 ? 310  HIS A CG  1 
ATOM   2374 N ND1 . HIS A 1 310 ? -30.930 -7.551  41.349  1.00 38.25 ? 310  HIS A ND1 1 
ATOM   2375 C CD2 . HIS A 1 310 ? -32.048 -5.926  42.306  1.00 37.58 ? 310  HIS A CD2 1 
ATOM   2376 C CE1 . HIS A 1 310 ? -32.203 -7.700  41.012  1.00 39.32 ? 310  HIS A CE1 1 
ATOM   2377 N NE2 . HIS A 1 310 ? -32.902 -6.726  41.577  1.00 39.68 ? 310  HIS A NE2 1 
ATOM   2378 N N   . ASP A 1 311 ? -27.807 -2.811  43.111  1.00 28.32 ? 311  ASP A N   1 
ATOM   2379 C CA  . ASP A 1 311 ? -26.613 -2.090  43.462  1.00 28.03 ? 311  ASP A CA  1 
ATOM   2380 C C   . ASP A 1 311 ? -26.912 -0.865  44.285  1.00 27.90 ? 311  ASP A C   1 
ATOM   2381 O O   . ASP A 1 311 ? -27.771 -0.053  43.958  1.00 28.49 ? 311  ASP A O   1 
ATOM   2382 C CB  . ASP A 1 311 ? -25.857 -1.659  42.208  1.00 27.77 ? 311  ASP A CB  1 
ATOM   2383 C CG  . ASP A 1 311 ? -24.616 -0.865  42.529  1.00 27.50 ? 311  ASP A CG  1 
ATOM   2384 O OD1 . ASP A 1 311 ? -23.557 -1.478  42.813  1.00 28.34 ? 311  ASP A OD1 1 
ATOM   2385 O OD2 . ASP A 1 311 ? -24.708 0.376   42.494  1.00 27.10 ? 311  ASP A OD2 1 
ATOM   2386 N N   . ASP A 1 312 ? -26.126 -0.695  45.321  1.00 28.02 ? 312  ASP A N   1 
ATOM   2387 C CA  . ASP A 1 312 ? -26.336 0.383   46.231  1.00 28.32 ? 312  ASP A CA  1 
ATOM   2388 C C   . ASP A 1 312 ? -24.998 1.113   46.487  1.00 26.80 ? 312  ASP A C   1 
ATOM   2389 O O   . ASP A 1 312 ? -24.880 1.931   47.398  1.00 26.75 ? 312  ASP A O   1 
ATOM   2390 C CB  . ASP A 1 312 ? -26.999 -0.228  47.460  1.00 29.50 ? 312  ASP A CB  1 
ATOM   2391 C CG  . ASP A 1 312 ? -27.478 0.776   48.415  1.00 34.35 ? 312  ASP A CG  1 
ATOM   2392 O OD1 . ASP A 1 312 ? -28.092 1.782   47.966  1.00 39.38 ? 312  ASP A OD1 1 
ATOM   2393 O OD2 . ASP A 1 312 ? -27.248 0.541   49.636  1.00 40.37 ? 312  ASP A OD2 1 
ATOM   2394 N N   . THR A 1 313 ? -24.026 0.861   45.608  1.00 25.04 ? 313  THR A N   1 
ATOM   2395 C CA  . THR A 1 313 ? -22.722 1.510   45.658  1.00 23.12 ? 313  THR A CA  1 
ATOM   2396 C C   . THR A 1 313 ? -22.576 2.762   44.741  1.00 24.02 ? 313  THR A C   1 
ATOM   2397 O O   . THR A 1 313 ? -22.906 3.900   45.131  1.00 23.75 ? 313  THR A O   1 
ATOM   2398 C CB  . THR A 1 313 ? -21.577 0.464   45.409  1.00 22.94 ? 313  THR A CB  1 
ATOM   2399 O OG1 . THR A 1 313 ? -21.348 0.246   43.999  1.00 17.20 ? 313  THR A OG1 1 
ATOM   2400 C CG2 . THR A 1 313 ? -21.900 -0.853  46.124  1.00 21.24 ? 313  THR A CG2 1 
ATOM   2401 N N   . SER A 1 314 ? -22.100 2.545   43.513  1.00 24.17 ? 314  SER A N   1 
ATOM   2402 C CA  . SER A 1 314 ? -21.710 3.627   42.616  1.00 23.70 ? 314  SER A CA  1 
ATOM   2403 C C   . SER A 1 314 ? -22.703 3.911   41.491  1.00 24.13 ? 314  SER A C   1 
ATOM   2404 O O   . SER A 1 314 ? -22.517 4.875   40.750  1.00 24.08 ? 314  SER A O   1 
ATOM   2405 C CB  . SER A 1 314 ? -20.337 3.343   42.008  1.00 23.36 ? 314  SER A CB  1 
ATOM   2406 O OG  . SER A 1 314 ? -20.440 2.304   41.048  1.00 22.91 ? 314  SER A OG  1 
ATOM   2407 N N   . SER A 1 315 ? -23.729 3.072   41.330  1.00 24.51 ? 315  SER A N   1 
ATOM   2408 C CA  . SER A 1 315 ? -24.724 3.286   40.259  1.00 25.34 ? 315  SER A CA  1 
ATOM   2409 C C   . SER A 1 315 ? -25.688 4.434   40.537  1.00 25.84 ? 315  SER A C   1 
ATOM   2410 O O   . SER A 1 315 ? -26.068 4.659   41.667  1.00 26.84 ? 315  SER A O   1 
ATOM   2411 C CB  . SER A 1 315 ? -25.504 2.004   39.955  1.00 24.58 ? 315  SER A CB  1 
ATOM   2412 O OG  . SER A 1 315 ? -26.300 1.606   41.052  1.00 27.03 ? 315  SER A OG  1 
ATOM   2413 N N   . ASN A 1 316 ? -26.053 5.166   39.506  1.00 26.46 ? 316  ASN A N   1 
ATOM   2414 C CA  . ASN A 1 316 ? -27.119 6.137   39.594  1.00 27.53 ? 316  ASN A CA  1 
ATOM   2415 C C   . ASN A 1 316 ? -28.469 5.443   39.332  1.00 27.71 ? 316  ASN A C   1 
ATOM   2416 O O   . ASN A 1 316 ? -28.653 4.818   38.280  1.00 28.54 ? 316  ASN A O   1 
ATOM   2417 C CB  . ASN A 1 316 ? -26.854 7.243   38.577  1.00 27.39 ? 316  ASN A CB  1 
ATOM   2418 C CG  . ASN A 1 316 ? -27.919 8.329   38.577  1.00 29.54 ? 316  ASN A CG  1 
ATOM   2419 O OD1 . ASN A 1 316 ? -29.127 8.073   38.811  1.00 29.58 ? 316  ASN A OD1 1 
ATOM   2420 N ND2 . ASN A 1 316 ? -27.473 9.562   38.309  1.00 30.32 ? 316  ASN A ND2 1 
ATOM   2421 N N   . HIS A 1 317 ? -29.410 5.582   40.267  1.00 27.94 ? 317  HIS A N   1 
ATOM   2422 C CA  . HIS A 1 317 ? -30.703 4.869   40.240  1.00 27.72 ? 317  HIS A CA  1 
ATOM   2423 C C   . HIS A 1 317 ? -31.720 5.448   39.267  1.00 27.27 ? 317  HIS A C   1 
ATOM   2424 O O   . HIS A 1 317 ? -32.534 4.728   38.684  1.00 26.97 ? 317  HIS A O   1 
ATOM   2425 C CB  . HIS A 1 317 ? -31.301 4.809   41.645  1.00 28.27 ? 317  HIS A CB  1 
ATOM   2426 C CG  . HIS A 1 317 ? -30.596 3.846   42.548  1.00 30.17 ? 317  HIS A CG  1 
ATOM   2427 N ND1 . HIS A 1 317 ? -31.021 2.548   42.729  1.00 34.21 ? 317  HIS A ND1 1 
ATOM   2428 C CD2 . HIS A 1 317 ? -29.463 3.971   43.277  1.00 33.07 ? 317  HIS A CD2 1 
ATOM   2429 C CE1 . HIS A 1 317 ? -30.198 1.921   43.556  1.00 33.99 ? 317  HIS A CE1 1 
ATOM   2430 N NE2 . HIS A 1 317 ? -29.236 2.759   43.890  1.00 34.10 ? 317  HIS A NE2 1 
ATOM   2431 N N   . THR A 1 318 ? -31.689 6.757   39.117  1.00 26.52 ? 318  THR A N   1 
ATOM   2432 C CA  . THR A 1 318 ? -32.466 7.410   38.091  1.00 25.89 ? 318  THR A CA  1 
ATOM   2433 C C   . THR A 1 318 ? -32.038 6.872   36.715  1.00 25.77 ? 318  THR A C   1 
ATOM   2434 O O   . THR A 1 318 ? -32.884 6.461   35.898  1.00 25.74 ? 318  THR A O   1 
ATOM   2435 C CB  . THR A 1 318 ? -32.205 8.922   38.112  1.00 26.09 ? 318  THR A CB  1 
ATOM   2436 O OG1 . THR A 1 318 ? -32.437 9.440   39.421  1.00 24.83 ? 318  THR A OG1 1 
ATOM   2437 C CG2 . THR A 1 318 ? -33.071 9.643   37.074  1.00 25.38 ? 318  THR A CG2 1 
ATOM   2438 N N   . LEU A 1 319 ? -30.726 6.891   36.463  1.00 25.15 ? 319  LEU A N   1 
ATOM   2439 C CA  . LEU A 1 319 ? -30.173 6.399   35.209  1.00 24.14 ? 319  LEU A CA  1 
ATOM   2440 C C   . LEU A 1 319 ? -30.458 4.903   34.996  1.00 24.42 ? 319  LEU A C   1 
ATOM   2441 O O   . LEU A 1 319 ? -30.863 4.490   33.886  1.00 24.79 ? 319  LEU A O   1 
ATOM   2442 C CB  . LEU A 1 319 ? -28.692 6.665   35.176  1.00 23.91 ? 319  LEU A CB  1 
ATOM   2443 C CG  . LEU A 1 319 ? -28.048 7.643   34.200  1.00 23.66 ? 319  LEU A CG  1 
ATOM   2444 C CD1 . LEU A 1 319 ? -28.932 8.782   33.799  1.00 24.46 ? 319  LEU A CD1 1 
ATOM   2445 C CD2 . LEU A 1 319 ? -26.714 8.144   34.773  1.00 21.53 ? 319  LEU A CD2 1 
ATOM   2446 N N   . ASP A 1 320 ? -30.298 4.095   36.046  1.00 23.39 ? 320  ASP A N   1 
ATOM   2447 C CA  . ASP A 1 320 ? -30.472 2.657   35.892  1.00 23.03 ? 320  ASP A CA  1 
ATOM   2448 C C   . ASP A 1 320 ? -31.867 2.082   35.931  1.00 23.47 ? 320  ASP A C   1 
ATOM   2449 O O   . ASP A 1 320 ? -32.069 1.025   35.374  1.00 23.66 ? 320  ASP A O   1 
ATOM   2450 C CB  . ASP A 1 320 ? -29.564 1.857   36.841  1.00 22.61 ? 320  ASP A CB  1 
ATOM   2451 C CG  . ASP A 1 320 ? -28.134 1.839   36.380  1.00 20.35 ? 320  ASP A CG  1 
ATOM   2452 O OD1 . ASP A 1 320 ? -27.749 2.688   35.534  1.00 22.55 ? 320  ASP A OD1 1 
ATOM   2453 O OD2 . ASP A 1 320 ? -27.372 0.997   36.861  1.00 16.17 ? 320  ASP A OD2 1 
ATOM   2454 N N   . SER A 1 321 ? -32.833 2.726   36.567  1.00 24.09 ? 321  SER A N   1 
ATOM   2455 C CA  . SER A 1 321 ? -34.144 2.063   36.721  1.00 25.39 ? 321  SER A CA  1 
ATOM   2456 C C   . SER A 1 321 ? -35.094 2.371   35.565  1.00 25.67 ? 321  SER A C   1 
ATOM   2457 O O   . SER A 1 321 ? -36.285 2.122   35.640  1.00 24.78 ? 321  SER A O   1 
ATOM   2458 C CB  . SER A 1 321 ? -34.789 2.378   38.090  1.00 25.50 ? 321  SER A CB  1 
ATOM   2459 O OG  . SER A 1 321 ? -35.245 3.719   38.128  1.00 27.09 ? 321  SER A OG  1 
ATOM   2460 N N   . SER A 1 322 ? -34.516 2.880   34.475  1.00 26.88 ? 322  SER A N   1 
ATOM   2461 C CA  . SER A 1 322 ? -35.270 3.380   33.320  1.00 27.08 ? 322  SER A CA  1 
ATOM   2462 C C   . SER A 1 322 ? -34.757 2.775   32.016  1.00 26.85 ? 322  SER A C   1 
ATOM   2463 O O   . SER A 1 322 ? -33.577 2.968   31.688  1.00 27.53 ? 322  SER A O   1 
ATOM   2464 C CB  . SER A 1 322 ? -35.168 4.912   33.293  1.00 27.02 ? 322  SER A CB  1 
ATOM   2465 O OG  . SER A 1 322 ? -35.146 5.409   31.957  1.00 29.76 ? 322  SER A OG  1 
ATOM   2466 N N   . PRO A 1 323 ? -35.633 2.077   31.242  1.00 26.63 ? 323  PRO A N   1 
ATOM   2467 C CA  . PRO A 1 323 ? -35.151 1.393   30.029  1.00 25.83 ? 323  PRO A CA  1 
ATOM   2468 C C   . PRO A 1 323 ? -34.455 2.339   29.061  1.00 25.78 ? 323  PRO A C   1 
ATOM   2469 O O   . PRO A 1 323 ? -33.469 1.931   28.447  1.00 27.10 ? 323  PRO A O   1 
ATOM   2470 C CB  . PRO A 1 323 ? -36.415 0.807   29.391  1.00 26.13 ? 323  PRO A CB  1 
ATOM   2471 C CG  . PRO A 1 323 ? -37.508 0.934   30.417  1.00 27.34 ? 323  PRO A CG  1 
ATOM   2472 C CD  . PRO A 1 323 ? -37.110 2.118   31.296  1.00 26.95 ? 323  PRO A CD  1 
ATOM   2473 N N   . ALA A 1 324 ? -34.911 3.592   28.954  1.00 24.89 ? 324  ALA A N   1 
ATOM   2474 C CA  . ALA A 1 324 ? -34.277 4.607   28.081  1.00 24.03 ? 324  ALA A CA  1 
ATOM   2475 C C   . ALA A 1 324 ? -32.753 4.812   28.315  1.00 23.97 ? 324  ALA A C   1 
ATOM   2476 O O   . ALA A 1 324 ? -31.958 4.951   27.375  1.00 24.04 ? 324  ALA A O   1 
ATOM   2477 C CB  . ALA A 1 324 ? -34.999 5.954   28.225  1.00 23.37 ? 324  ALA A CB  1 
ATOM   2478 N N   . THR A 1 325 ? -32.369 4.861   29.590  1.00 23.43 ? 325  THR A N   1 
ATOM   2479 C CA  . THR A 1 325 ? -31.015 5.168   29.992  1.00 22.25 ? 325  THR A CA  1 
ATOM   2480 C C   . THR A 1 325 ? -30.266 3.930   30.499  1.00 22.43 ? 325  THR A C   1 
ATOM   2481 O O   . THR A 1 325 ? -29.056 3.985   30.675  1.00 22.88 ? 325  THR A O   1 
ATOM   2482 C CB  . THR A 1 325 ? -31.025 6.286   31.014  1.00 22.10 ? 325  THR A CB  1 
ATOM   2483 O OG1 . THR A 1 325 ? -32.147 6.105   31.891  1.00 21.34 ? 325  THR A OG1 1 
ATOM   2484 C CG2 . THR A 1 325 ? -31.219 7.601   30.292  1.00 22.23 ? 325  THR A CG2 1 
ATOM   2485 N N   . PHE A 1 326 ? -30.978 2.821   30.732  1.00 21.26 ? 326  PHE A N   1 
ATOM   2486 C CA  . PHE A 1 326 ? -30.307 1.555   30.971  1.00 20.64 ? 326  PHE A CA  1 
ATOM   2487 C C   . PHE A 1 326 ? -31.118 0.364   30.404  1.00 20.61 ? 326  PHE A C   1 
ATOM   2488 O O   . PHE A 1 326 ? -31.753 -0.362  31.195  1.00 21.62 ? 326  PHE A O   1 
ATOM   2489 C CB  . PHE A 1 326 ? -30.033 1.366   32.482  1.00 19.90 ? 326  PHE A CB  1 
ATOM   2490 C CG  . PHE A 1 326 ? -29.101 0.226   32.785  1.00 20.26 ? 326  PHE A CG  1 
ATOM   2491 C CD1 . PHE A 1 326 ? -27.708 0.383   32.652  1.00 19.65 ? 326  PHE A CD1 1 
ATOM   2492 C CD2 . PHE A 1 326 ? -29.604 -1.033  33.140  1.00 19.56 ? 326  PHE A CD2 1 
ATOM   2493 C CE1 . PHE A 1 326 ? -26.841 -0.705  32.913  1.00 18.38 ? 326  PHE A CE1 1 
ATOM   2494 C CE2 . PHE A 1 326 ? -28.748 -2.119  33.390  1.00 19.54 ? 326  PHE A CE2 1 
ATOM   2495 C CZ  . PHE A 1 326 ? -27.365 -1.945  33.272  1.00 19.67 ? 326  PHE A CZ  1 
ATOM   2496 N N   . PRO A 1 327 ? -31.105 0.145   29.063  1.00 19.76 ? 327  PRO A N   1 
ATOM   2497 C CA  . PRO A 1 327 ? -31.956 -0.918  28.526  1.00 19.91 ? 327  PRO A CA  1 
ATOM   2498 C C   . PRO A 1 327 ? -31.350 -2.305  28.766  1.00 19.59 ? 327  PRO A C   1 
ATOM   2499 O O   . PRO A 1 327 ? -30.147 -2.472  28.638  1.00 19.29 ? 327  PRO A O   1 
ATOM   2500 C CB  . PRO A 1 327 ? -32.031 -0.576  27.006  1.00 19.76 ? 327  PRO A CB  1 
ATOM   2501 C CG  . PRO A 1 327 ? -30.754 0.115   26.746  1.00 19.37 ? 327  PRO A CG  1 
ATOM   2502 C CD  . PRO A 1 327 ? -30.361 0.836   27.987  1.00 19.44 ? 327  PRO A CD  1 
ATOM   2503 N N   . LEU A 1 328 ? -32.188 -3.292  29.071  1.00 19.87 ? 328  LEU A N   1 
ATOM   2504 C CA  . LEU A 1 328 ? -31.698 -4.644  29.493  1.00 20.75 ? 328  LEU A CA  1 
ATOM   2505 C C   . LEU A 1 328 ? -31.596 -5.703  28.391  1.00 20.95 ? 328  LEU A C   1 
ATOM   2506 O O   . LEU A 1 328 ? -31.127 -6.831  28.637  1.00 21.12 ? 328  LEU A O   1 
ATOM   2507 C CB  . LEU A 1 328 ? -32.601 -5.212  30.611  1.00 19.93 ? 328  LEU A CB  1 
ATOM   2508 C CG  . LEU A 1 328 ? -32.796 -4.291  31.827  1.00 22.41 ? 328  LEU A CG  1 
ATOM   2509 C CD1 . LEU A 1 328 ? -33.909 -4.773  32.769  1.00 20.26 ? 328  LEU A CD1 1 
ATOM   2510 C CD2 . LEU A 1 328 ? -31.463 -4.184  32.562  1.00 21.30 ? 328  LEU A CD2 1 
ATOM   2511 N N   . ASN A 1 329 ? -32.100 -5.389  27.206  1.00 21.78 ? 329  ASN A N   1 
ATOM   2512 C CA  . ASN A 1 329 ? -32.197 -6.408  26.160  1.00 23.22 ? 329  ASN A CA  1 
ATOM   2513 C C   . ASN A 1 329 ? -31.622 -5.882  24.887  1.00 22.45 ? 329  ASN A C   1 
ATOM   2514 O O   . ASN A 1 329 ? -32.082 -6.265  23.809  1.00 22.98 ? 329  ASN A O   1 
ATOM   2515 C CB  . ASN A 1 329 ? -33.654 -6.802  25.862  1.00 23.98 ? 329  ASN A CB  1 
ATOM   2516 C CG  . ASN A 1 329 ? -34.340 -7.481  27.025  1.00 28.19 ? 329  ASN A CG  1 
ATOM   2517 O OD1 . ASN A 1 329 ? -33.930 -8.558  27.463  1.00 33.59 ? 329  ASN A OD1 1 
ATOM   2518 N ND2 . ASN A 1 329 ? -35.414 -6.873  27.514  1.00 30.88 ? 329  ASN A ND2 1 
ATOM   2519 N N   . SER A 1 330 ? -30.660 -4.975  24.982  1.00 21.77 ? 330  SER A N   1 
ATOM   2520 C CA  . SER A 1 330 ? -29.944 -4.614  23.793  1.00 21.60 ? 330  SER A CA  1 
ATOM   2521 C C   . SER A 1 330 ? -29.092 -5.858  23.697  1.00 22.00 ? 330  SER A C   1 
ATOM   2522 O O   . SER A 1 330 ? -29.207 -6.811  24.545  1.00 23.34 ? 330  SER A O   1 
ATOM   2523 C CB  . SER A 1 330 ? -29.108 -3.380  24.009  1.00 21.47 ? 330  SER A CB  1 
ATOM   2524 O OG  . SER A 1 330 ? -29.904 -2.400  24.611  1.00 20.71 ? 330  SER A OG  1 
ATOM   2525 N N   . THR A 1 331 ? -28.275 -5.921  22.685  1.00 20.45 ? 331  THR A N   1 
ATOM   2526 C CA  . THR A 1 331 ? -27.492 -7.137  22.539  1.00 19.80 ? 331  THR A CA  1 
ATOM   2527 C C   . THR A 1 331 ? -26.020 -6.755  22.546  1.00 19.07 ? 331  THR A C   1 
ATOM   2528 O O   . THR A 1 331 ? -25.150 -7.578  22.874  1.00 19.11 ? 331  THR A O   1 
ATOM   2529 C CB  . THR A 1 331 ? -27.896 -7.831  21.216  1.00 20.04 ? 331  THR A CB  1 
ATOM   2530 O OG1 . THR A 1 331 ? -29.075 -8.586  21.464  1.00 19.19 ? 331  THR A OG1 1 
ATOM   2531 C CG2 . THR A 1 331 ? -26.780 -8.711  20.614  1.00 18.96 ? 331  THR A CG2 1 
ATOM   2532 N N   . LEU A 1 332 ? -25.782 -5.489  22.203  1.00 16.98 ? 332  LEU A N   1 
ATOM   2533 C CA  . LEU A 1 332 ? -24.460 -4.922  22.144  1.00 16.68 ? 332  LEU A CA  1 
ATOM   2534 C C   . LEU A 1 332 ? -24.441 -3.649  22.965  1.00 15.70 ? 332  LEU A C   1 
ATOM   2535 O O   . LEU A 1 332 ? -25.429 -2.922  23.012  1.00 16.66 ? 332  LEU A O   1 
ATOM   2536 C CB  . LEU A 1 332 ? -24.074 -4.592  20.699  1.00 16.43 ? 332  LEU A CB  1 
ATOM   2537 C CG  . LEU A 1 332 ? -24.213 -5.702  19.664  1.00 14.55 ? 332  LEU A CG  1 
ATOM   2538 C CD1 . LEU A 1 332 ? -24.375 -5.065  18.334  1.00 14.09 ? 332  LEU A CD1 1 
ATOM   2539 C CD2 . LEU A 1 332 ? -22.957 -6.560  19.681  1.00 13.64 ? 332  LEU A CD2 1 
ATOM   2540 N N   . TYR A 1 333 ? -23.303 -3.376  23.569  1.00 14.54 ? 333  TYR A N   1 
ATOM   2541 C CA  . TYR A 1 333 ? -23.150 -2.330  24.568  1.00 13.33 ? 333  TYR A CA  1 
ATOM   2542 C C   . TYR A 1 333 ? -21.690 -1.902  24.462  1.00 14.28 ? 333  TYR A C   1 
ATOM   2543 O O   . TYR A 1 333 ? -20.767 -2.725  24.237  1.00 13.19 ? 333  TYR A O   1 
ATOM   2544 C CB  . TYR A 1 333 ? -23.413 -2.858  25.975  1.00 12.88 ? 333  TYR A CB  1 
ATOM   2545 C CG  . TYR A 1 333 ? -24.870 -3.203  26.337  1.00 12.30 ? 333  TYR A CG  1 
ATOM   2546 C CD1 . TYR A 1 333 ? -25.735 -2.245  26.837  1.00 11.03 ? 333  TYR A CD1 1 
ATOM   2547 C CD2 . TYR A 1 333 ? -25.344 -4.515  26.207  1.00 10.72 ? 333  TYR A CD2 1 
ATOM   2548 C CE1 . TYR A 1 333 ? -27.088 -2.604  27.204  1.00 11.18 ? 333  TYR A CE1 1 
ATOM   2549 C CE2 . TYR A 1 333 ? -26.607 -4.873  26.551  1.00 10.40 ? 333  TYR A CE2 1 
ATOM   2550 C CZ  . TYR A 1 333 ? -27.504 -3.919  27.043  1.00 12.97 ? 333  TYR A CZ  1 
ATOM   2551 O OH  . TYR A 1 333 ? -28.811 -4.304  27.366  1.00 12.31 ? 333  TYR A OH  1 
ATOM   2552 N N   . ALA A 1 334 ? -21.487 -0.605  24.588  1.00 14.18 ? 334  ALA A N   1 
ATOM   2553 C CA  . ALA A 1 334 ? -20.181 -0.049  24.519  1.00 14.36 ? 334  ALA A CA  1 
ATOM   2554 C C   . ALA A 1 334 ? -20.079 1.037   25.611  1.00 15.53 ? 334  ALA A C   1 
ATOM   2555 O O   . ALA A 1 334 ? -20.977 1.941   25.736  1.00 15.24 ? 334  ALA A O   1 
ATOM   2556 C CB  . ALA A 1 334 ? -19.942 0.503   23.138  1.00 13.85 ? 334  ALA A CB  1 
ATOM   2557 N N   . ASP A 1 335 ? -19.034 0.896   26.454  1.00 15.97 ? 335  ASP A N   1 
ATOM   2558 C CA  . ASP A 1 335 ? -18.750 1.859   27.530  1.00 15.72 ? 335  ASP A CA  1 
ATOM   2559 C C   . ASP A 1 335 ? -17.316 2.409   27.375  1.00 16.07 ? 335  ASP A C   1 
ATOM   2560 O O   . ASP A 1 335 ? -16.388 1.720   26.904  1.00 16.95 ? 335  ASP A O   1 
ATOM   2561 C CB  . ASP A 1 335 ? -18.963 1.259   28.914  1.00 15.62 ? 335  ASP A CB  1 
ATOM   2562 C CG  . ASP A 1 335 ? -20.417 0.912   29.226  1.00 17.31 ? 335  ASP A CG  1 
ATOM   2563 O OD1 . ASP A 1 335 ? -21.314 1.822   29.191  1.00 15.87 ? 335  ASP A OD1 1 
ATOM   2564 O OD2 . ASP A 1 335 ? -20.643 -0.289  29.592  1.00 17.11 ? 335  ASP A OD2 1 
ATOM   2565 N N   . PHE A 1 336 ? -17.135 3.660   27.769  1.00 16.13 ? 336  PHE A N   1 
ATOM   2566 C CA  . PHE A 1 336 ? -15.875 4.372   27.583  1.00 16.09 ? 336  PHE A CA  1 
ATOM   2567 C C   . PHE A 1 336 ? -15.515 5.072   28.870  1.00 16.62 ? 336  PHE A C   1 
ATOM   2568 O O   . PHE A 1 336 ? -16.355 5.805   29.448  1.00 17.75 ? 336  PHE A O   1 
ATOM   2569 C CB  . PHE A 1 336 ? -16.006 5.393   26.423  1.00 16.54 ? 336  PHE A CB  1 
ATOM   2570 C CG  . PHE A 1 336 ? -16.174 4.744   25.091  1.00 14.66 ? 336  PHE A CG  1 
ATOM   2571 C CD1 . PHE A 1 336 ? -17.424 4.348   24.664  1.00 11.96 ? 336  PHE A CD1 1 
ATOM   2572 C CD2 . PHE A 1 336 ? -15.064 4.464   24.303  1.00 14.49 ? 336  PHE A CD2 1 
ATOM   2573 C CE1 . PHE A 1 336 ? -17.578 3.711   23.453  1.00 13.09 ? 336  PHE A CE1 1 
ATOM   2574 C CE2 . PHE A 1 336 ? -15.190 3.805   23.099  1.00 12.54 ? 336  PHE A CE2 1 
ATOM   2575 C CZ  . PHE A 1 336 ? -16.461 3.417   22.683  1.00 15.47 ? 336  PHE A CZ  1 
ATOM   2576 N N   . SER A 1 337 ? -14.278 4.876   29.323  1.00 16.25 ? 337  SER A N   1 
ATOM   2577 C CA  . SER A 1 337 ? -13.896 5.315   30.665  1.00 15.82 ? 337  SER A CA  1 
ATOM   2578 C C   . SER A 1 337 ? -12.379 5.563   30.778  1.00 16.12 ? 337  SER A C   1 
ATOM   2579 O O   . SER A 1 337 ? -11.699 5.666   29.739  1.00 17.64 ? 337  SER A O   1 
ATOM   2580 C CB  . SER A 1 337 ? -14.364 4.302   31.695  1.00 15.24 ? 337  SER A CB  1 
ATOM   2581 O OG  . SER A 1 337 ? -14.489 4.886   32.971  1.00 17.26 ? 337  SER A OG  1 
ATOM   2582 N N   . HIS A 1 338 ? -11.863 5.697   32.016  1.00 15.70 ? 338  HIS A N   1 
ATOM   2583 C CA  . HIS A 1 338 ? -10.417 5.836   32.252  1.00 14.48 ? 338  HIS A CA  1 
ATOM   2584 C C   . HIS A 1 338 ? -9.818  4.534   32.711  1.00 14.68 ? 338  HIS A C   1 
ATOM   2585 O O   . HIS A 1 338 ? -10.531 3.638   33.190  1.00 14.76 ? 338  HIS A O   1 
ATOM   2586 C CB  . HIS A 1 338 ? -10.111 6.879   33.323  1.00 14.38 ? 338  HIS A CB  1 
ATOM   2587 C CG  . HIS A 1 338 ? -10.786 8.195   33.112  1.00 12.84 ? 338  HIS A CG  1 
ATOM   2588 N ND1 . HIS A 1 338 ? -10.147 9.267   32.533  1.00 10.91 ? 338  HIS A ND1 1 
ATOM   2589 C CD2 . HIS A 1 338 ? -12.041 8.617   33.418  1.00 14.17 ? 338  HIS A CD2 1 
ATOM   2590 C CE1 . HIS A 1 338 ? -10.983 10.290  32.470  1.00 14.57 ? 338  HIS A CE1 1 
ATOM   2591 N NE2 . HIS A 1 338 ? -12.137 9.923   33.005  1.00 16.11 ? 338  HIS A NE2 1 
ATOM   2592 N N   . ASP A 1 339 ? -8.500  4.479   32.616  1.00 15.08 ? 339  ASP A N   1 
ATOM   2593 C CA  . ASP A 1 339 ? -7.675  3.405   33.139  1.00 15.98 ? 339  ASP A CA  1 
ATOM   2594 C C   . ASP A 1 339 ? -8.011  3.025   34.592  1.00 16.01 ? 339  ASP A C   1 
ATOM   2595 O O   . ASP A 1 339 ? -8.173  1.849   34.899  1.00 16.87 ? 339  ASP A O   1 
ATOM   2596 C CB  . ASP A 1 339 ? -6.154  3.736   32.955  1.00 15.18 ? 339  ASP A CB  1 
ATOM   2597 C CG  . ASP A 1 339 ? -5.686  4.946   33.770  1.00 16.05 ? 339  ASP A CG  1 
ATOM   2598 O OD1 . ASP A 1 339 ? -6.461  5.494   34.585  1.00 15.14 ? 339  ASP A OD1 1 
ATOM   2599 O OD2 . ASP A 1 339 ? -4.518  5.367   33.611  1.00 17.05 ? 339  ASP A OD2 1 
ATOM   2600 N N   . ASN A 1 340 ? -8.144  4.017   35.465  1.00 15.95 ? 340  ASN A N   1 
ATOM   2601 C CA  . ASN A 1 340 ? -8.281  3.735   36.880  1.00 16.80 ? 340  ASN A CA  1 
ATOM   2602 C C   . ASN A 1 340 ? -9.556  2.995   37.169  1.00 17.14 ? 340  ASN A C   1 
ATOM   2603 O O   . ASN A 1 340 ? -9.525  2.004   37.905  1.00 17.25 ? 340  ASN A O   1 
ATOM   2604 C CB  . ASN A 1 340 ? -8.176  4.999   37.745  1.00 16.30 ? 340  ASN A CB  1 
ATOM   2605 C CG  . ASN A 1 340 ? -6.759  5.576   37.775  1.00 17.47 ? 340  ASN A CG  1 
ATOM   2606 O OD1 . ASN A 1 340 ? -5.742  4.868   37.495  1.00 14.91 ? 340  ASN A OD1 1 
ATOM   2607 N ND2 . ASN A 1 340 ? -6.678  6.874   38.073  1.00 15.09 ? 340  ASN A ND2 1 
ATOM   2608 N N   . GLY A 1 341 ? -10.676 3.457   36.612  1.00 16.13 ? 341  GLY A N   1 
ATOM   2609 C CA  . GLY A 1 341 ? -11.916 2.767   36.854  1.00 16.30 ? 341  GLY A CA  1 
ATOM   2610 C C   . GLY A 1 341 ? -11.928 1.386   36.193  1.00 16.76 ? 341  GLY A C   1 
ATOM   2611 O O   . GLY A 1 341 ? -12.716 0.510   36.573  1.00 16.61 ? 341  GLY A O   1 
ATOM   2612 N N   . ILE A 1 342 ? -11.088 1.196   35.171  1.00 16.71 ? 342  ILE A N   1 
ATOM   2613 C CA  . ILE A 1 342 ? -11.154 -0.028  34.382  1.00 16.45 ? 342  ILE A CA  1 
ATOM   2614 C C   . ILE A 1 342 ? -10.411 -1.084  35.185  1.00 17.28 ? 342  ILE A C   1 
ATOM   2615 O O   . ILE A 1 342 ? -10.782 -2.249  35.180  1.00 18.07 ? 342  ILE A O   1 
ATOM   2616 C CB  . ILE A 1 342 ? -10.526 0.154   32.945  1.00 16.72 ? 342  ILE A CB  1 
ATOM   2617 C CG1 . ILE A 1 342 ? -11.479 0.901   32.031  1.00 15.60 ? 342  ILE A CG1 1 
ATOM   2618 C CG2 . ILE A 1 342 ? -10.308 -1.156  32.289  1.00 14.46 ? 342  ILE A CG2 1 
ATOM   2619 C CD1 . ILE A 1 342 ? -10.823 1.436   30.788  1.00 17.19 ? 342  ILE A CD1 1 
ATOM   2620 N N   . ILE A 1 343 ? -9.334  -0.670  35.866  1.00 17.56 ? 343  ILE A N   1 
ATOM   2621 C CA  . ILE A 1 343 ? -8.595  -1.551  36.750  1.00 15.98 ? 343  ILE A CA  1 
ATOM   2622 C C   . ILE A 1 343 ? -9.595  -2.038  37.794  1.00 15.03 ? 343  ILE A C   1 
ATOM   2623 O O   . ILE A 1 343 ? -9.836  -3.224  37.923  1.00 15.42 ? 343  ILE A O   1 
ATOM   2624 C CB  . ILE A 1 343 ? -7.360  -0.844  37.400  1.00 16.03 ? 343  ILE A CB  1 
ATOM   2625 C CG1 . ILE A 1 343 ? -6.300  -0.428  36.354  1.00 14.18 ? 343  ILE A CG1 1 
ATOM   2626 C CG2 . ILE A 1 343 ? -6.753  -1.736  38.460  1.00 15.99 ? 343  ILE A CG2 1 
ATOM   2627 C CD1 . ILE A 1 343 ? -5.411  -1.537  35.840  1.00 7.42  ? 343  ILE A CD1 1 
ATOM   2628 N N   . SER A 1 344 ? -10.217 -1.130  38.519  1.00 14.81 ? 344  SER A N   1 
ATOM   2629 C CA  . SER A 1 344 ? -11.174 -1.541  39.572  1.00 14.81 ? 344  SER A CA  1 
ATOM   2630 C C   . SER A 1 344 ? -12.227 -2.508  39.054  1.00 15.17 ? 344  SER A C   1 
ATOM   2631 O O   . SER A 1 344 ? -12.584 -3.493  39.722  1.00 15.80 ? 344  SER A O   1 
ATOM   2632 C CB  . SER A 1 344 ? -11.844 -0.356  40.241  1.00 14.04 ? 344  SER A CB  1 
ATOM   2633 O OG  . SER A 1 344 ? -10.886 0.518   40.772  1.00 15.41 ? 344  SER A OG  1 
ATOM   2634 N N   . ILE A 1 345 ? -12.692 -2.258  37.842  1.00 14.89 ? 345  ILE A N   1 
ATOM   2635 C CA  . ILE A 1 345 ? -13.702 -3.121  37.248  1.00 15.26 ? 345  ILE A CA  1 
ATOM   2636 C C   . ILE A 1 345 ? -13.219 -4.562  36.932  1.00 14.63 ? 345  ILE A C   1 
ATOM   2637 O O   . ILE A 1 345 ? -13.926 -5.524  37.204  1.00 13.11 ? 345  ILE A O   1 
ATOM   2638 C CB  . ILE A 1 345 ? -14.342 -2.442  36.005  1.00 15.11 ? 345  ILE A CB  1 
ATOM   2639 C CG1 . ILE A 1 345 ? -15.117 -1.199  36.423  1.00 14.16 ? 345  ILE A CG1 1 
ATOM   2640 C CG2 . ILE A 1 345 ? -15.243 -3.426  35.279  1.00 13.80 ? 345  ILE A CG2 1 
ATOM   2641 C CD1 . ILE A 1 345 ? -15.568 -0.345  35.235  1.00 14.92 ? 345  ILE A CD1 1 
ATOM   2642 N N   . LEU A 1 346 ? -12.033 -4.668  36.314  1.00 14.92 ? 346  LEU A N   1 
ATOM   2643 C CA  . LEU A 1 346 ? -11.410 -5.927  35.994  1.00 15.08 ? 346  LEU A CA  1 
ATOM   2644 C C   . LEU A 1 346 ? -11.288 -6.824  37.273  1.00 16.29 ? 346  LEU A C   1 
ATOM   2645 O O   . LEU A 1 346 ? -11.638 -8.034  37.241  1.00 16.23 ? 346  LEU A O   1 
ATOM   2646 C CB  . LEU A 1 346 ? -10.030 -5.685  35.367  1.00 15.43 ? 346  LEU A CB  1 
ATOM   2647 C CG  . LEU A 1 346 ? -9.913  -5.017  33.994  1.00 16.23 ? 346  LEU A CG  1 
ATOM   2648 C CD1 . LEU A 1 346 ? -8.464  -4.969  33.441  1.00 17.22 ? 346  LEU A CD1 1 
ATOM   2649 C CD2 . LEU A 1 346 ? -10.870 -5.644  32.976  1.00 15.93 ? 346  LEU A CD2 1 
ATOM   2650 N N   . PHE A 1 347 ? -10.801 -6.221  38.372  1.00 15.68 ? 347  PHE A N   1 
ATOM   2651 C CA  . PHE A 1 347 ? -10.632 -6.909  39.644  1.00 16.05 ? 347  PHE A CA  1 
ATOM   2652 C C   . PHE A 1 347 ? -11.945 -7.279  40.322  1.00 16.31 ? 347  PHE A C   1 
ATOM   2653 O O   . PHE A 1 347 ? -12.074 -8.410  40.789  1.00 16.97 ? 347  PHE A O   1 
ATOM   2654 C CB  . PHE A 1 347 ? -9.694  -6.160  40.595  1.00 15.24 ? 347  PHE A CB  1 
ATOM   2655 C CG  . PHE A 1 347 ? -8.206  -6.357  40.266  1.00 14.53 ? 347  PHE A CG  1 
ATOM   2656 C CD1 . PHE A 1 347 ? -7.491  -7.451  40.778  1.00 11.81 ? 347  PHE A CD1 1 
ATOM   2657 C CD2 . PHE A 1 347 ? -7.516  -5.436  39.470  1.00 10.27 ? 347  PHE A CD2 1 
ATOM   2658 C CE1 . PHE A 1 347 ? -6.101  -7.608  40.484  1.00 12.20 ? 347  PHE A CE1 1 
ATOM   2659 C CE2 . PHE A 1 347 ? -6.103  -5.594  39.171  1.00 10.95 ? 347  PHE A CE2 1 
ATOM   2660 C CZ  . PHE A 1 347 ? -5.413  -6.659  39.671  1.00 10.09 ? 347  PHE A CZ  1 
ATOM   2661 N N   . ALA A 1 348 ? -12.926 -6.375  40.323  1.00 16.24 ? 348  ALA A N   1 
ATOM   2662 C CA  . ALA A 1 348 ? -14.261 -6.695  40.860  1.00 16.20 ? 348  ALA A CA  1 
ATOM   2663 C C   . ALA A 1 348 ? -14.938 -7.815  40.080  1.00 16.62 ? 348  ALA A C   1 
ATOM   2664 O O   . ALA A 1 348 ? -15.847 -8.477  40.588  1.00 15.75 ? 348  ALA A O   1 
ATOM   2665 C CB  . ALA A 1 348 ? -15.141 -5.495  40.879  1.00 16.25 ? 348  ALA A CB  1 
ATOM   2666 N N   . LEU A 1 349 ? -14.469 -8.048  38.846  1.00 16.50 ? 349  LEU A N   1 
ATOM   2667 C CA  . LEU A 1 349 ? -15.067 -9.105  38.021  1.00 16.37 ? 349  LEU A CA  1 
ATOM   2668 C C   . LEU A 1 349 ? -14.390 -10.444 38.277  1.00 16.73 ? 349  LEU A C   1 
ATOM   2669 O O   . LEU A 1 349 ? -14.758 -11.450 37.688  1.00 17.55 ? 349  LEU A O   1 
ATOM   2670 C CB  . LEU A 1 349 ? -15.053 -8.737  36.524  1.00 15.50 ? 349  LEU A CB  1 
ATOM   2671 C CG  . LEU A 1 349 ? -16.057 -7.634  36.160  1.00 16.53 ? 349  LEU A CG  1 
ATOM   2672 C CD1 . LEU A 1 349 ? -15.873 -7.117  34.754  1.00 14.37 ? 349  LEU A CD1 1 
ATOM   2673 C CD2 . LEU A 1 349 ? -17.453 -8.144  36.387  1.00 16.21 ? 349  LEU A CD2 1 
ATOM   2674 N N   . GLY A 1 350 ? -13.389 -10.449 39.147  1.00 17.09 ? 350  GLY A N   1 
ATOM   2675 C CA  . GLY A 1 350 ? -12.640 -11.660 39.451  1.00 17.21 ? 350  GLY A CA  1 
ATOM   2676 C C   . GLY A 1 350 ? -11.516 -11.965 38.481  1.00 18.19 ? 350  GLY A C   1 
ATOM   2677 O O   . GLY A 1 350 ? -10.781 -12.922 38.698  1.00 18.72 ? 350  GLY A O   1 
ATOM   2678 N N   . LEU A 1 351 ? -11.346 -11.162 37.429  1.00 18.45 ? 351  LEU A N   1 
ATOM   2679 C CA  . LEU A 1 351 ? -10.468 -11.573 36.309  1.00 19.25 ? 351  LEU A CA  1 
ATOM   2680 C C   . LEU A 1 351 ? -9.022  -11.782 36.694  1.00 19.31 ? 351  LEU A C   1 
ATOM   2681 O O   . LEU A 1 351 ? -8.238  -12.372 35.913  1.00 20.67 ? 351  LEU A O   1 
ATOM   2682 C CB  . LEU A 1 351 ? -10.542 -10.608 35.109  1.00 19.09 ? 351  LEU A CB  1 
ATOM   2683 C CG  . LEU A 1 351 ? -11.977 -10.232 34.712  1.00 21.30 ? 351  LEU A CG  1 
ATOM   2684 C CD1 . LEU A 1 351 ? -11.972 -9.226  33.559  1.00 20.31 ? 351  LEU A CD1 1 
ATOM   2685 C CD2 . LEU A 1 351 ? -12.809 -11.492 34.370  1.00 20.94 ? 351  LEU A CD2 1 
ATOM   2686 N N   . TYR A 1 352 ? -8.648  -11.288 37.869  1.00 19.19 ? 352  TYR A N   1 
ATOM   2687 C CA  . TYR A 1 352 ? -7.241  -11.414 38.287  1.00 19.18 ? 352  TYR A CA  1 
ATOM   2688 C C   . TYR A 1 352 ? -7.074  -12.115 39.631  1.00 19.63 ? 352  TYR A C   1 
ATOM   2689 O O   . TYR A 1 352 ? -6.146  -11.848 40.391  1.00 19.34 ? 352  TYR A O   1 
ATOM   2690 C CB  . TYR A 1 352 ? -6.451  -10.094 38.124  1.00 17.88 ? 352  TYR A CB  1 
ATOM   2691 C CG  . TYR A 1 352 ? -6.312  -9.765  36.667  1.00 17.05 ? 352  TYR A CG  1 
ATOM   2692 C CD1 . TYR A 1 352 ? -5.341  -10.392 35.865  1.00 15.12 ? 352  TYR A CD1 1 
ATOM   2693 C CD2 . TYR A 1 352 ? -7.190  -8.861  36.055  1.00 13.23 ? 352  TYR A CD2 1 
ATOM   2694 C CE1 . TYR A 1 352 ? -5.242  -10.102 34.481  1.00 13.07 ? 352  TYR A CE1 1 
ATOM   2695 C CE2 . TYR A 1 352 ? -7.085  -8.566  34.688  1.00 13.87 ? 352  TYR A CE2 1 
ATOM   2696 C CZ  . TYR A 1 352 ? -6.132  -9.200  33.905  1.00 14.73 ? 352  TYR A CZ  1 
ATOM   2697 O OH  . TYR A 1 352 ? -6.082  -8.868  32.551  1.00 16.41 ? 352  TYR A OH  1 
ATOM   2698 N N   . ASN A 1 353 ? -7.969  -13.064 39.865  1.00 20.22 ? 353  ASN A N   1 
ATOM   2699 C CA  . ASN A 1 353 ? -8.008  -13.778 41.114  1.00 21.44 ? 353  ASN A CA  1 
ATOM   2700 C C   . ASN A 1 353 ? -7.097  -15.003 41.175  1.00 22.28 ? 353  ASN A C   1 
ATOM   2701 O O   . ASN A 1 353 ? -7.245  -15.844 42.060  1.00 22.72 ? 353  ASN A O   1 
ATOM   2702 C CB  . ASN A 1 353 ? -9.447  -14.142 41.426  1.00 21.48 ? 353  ASN A CB  1 
ATOM   2703 C CG  . ASN A 1 353 ? -10.096 -13.161 42.297  1.00 21.15 ? 353  ASN A CG  1 
ATOM   2704 O OD1 . ASN A 1 353 ? -9.696  -11.996 42.376  1.00 20.33 ? 353  ASN A OD1 1 
ATOM   2705 N ND2 . ASN A 1 353 ? -11.118 -13.616 42.970  1.00 21.07 ? 353  ASN A ND2 1 
ATOM   2706 N N   . GLY A 1 354 ? -6.156  -15.102 40.245  1.00 23.16 ? 354  GLY A N   1 
ATOM   2707 C CA  . GLY A 1 354 ? -5.108  -16.104 40.340  1.00 24.25 ? 354  GLY A CA  1 
ATOM   2708 C C   . GLY A 1 354 ? -3.778  -15.389 40.436  1.00 25.48 ? 354  GLY A C   1 
ATOM   2709 O O   . GLY A 1 354 ? -2.728  -16.034 40.436  1.00 26.11 ? 354  GLY A O   1 
ATOM   2710 N N   . THR A 1 355 ? -3.835  -14.049 40.504  1.00 25.78 ? 355  THR A N   1 
ATOM   2711 C CA  . THR A 1 355 ? -2.668  -13.154 40.595  1.00 25.68 ? 355  THR A CA  1 
ATOM   2712 C C   . THR A 1 355 ? -2.297  -12.881 42.083  1.00 26.77 ? 355  THR A C   1 
ATOM   2713 O O   . THR A 1 355 ? -3.160  -12.497 42.902  1.00 26.45 ? 355  THR A O   1 
ATOM   2714 C CB  . THR A 1 355 ? -2.947  -11.789 39.864  1.00 25.72 ? 355  THR A CB  1 
ATOM   2715 O OG1 . THR A 1 355 ? -3.068  -11.971 38.440  1.00 23.77 ? 355  THR A OG1 1 
ATOM   2716 C CG2 . THR A 1 355 ? -1.855  -10.726 40.181  1.00 24.18 ? 355  THR A CG2 1 
ATOM   2717 N N   . LYS A 1 356 ? -1.020  -13.076 42.425  1.00 26.92 ? 356  LYS A N   1 
ATOM   2718 C CA  . LYS A 1 356 ? -0.534  -12.850 43.799  1.00 27.35 ? 356  LYS A CA  1 
ATOM   2719 C C   . LYS A 1 356 ? -0.070  -11.407 43.965  1.00 26.76 ? 356  LYS A C   1 
ATOM   2720 O O   . LYS A 1 356 ? 0.624   -10.892 43.097  1.00 28.40 ? 356  LYS A O   1 
ATOM   2721 C CB  . LYS A 1 356 ? 0.586   -13.839 44.145  1.00 27.29 ? 356  LYS A CB  1 
ATOM   2722 C CG  . LYS A 1 356 ? 0.083   -14.993 44.970  1.00 30.77 ? 356  LYS A CG  1 
ATOM   2723 C CD  . LYS A 1 356 ? 0.523   -16.381 44.464  1.00 36.04 ? 356  LYS A CD  1 
ATOM   2724 C CE  . LYS A 1 356 ? -0.369  -17.434 45.160  1.00 42.19 ? 356  LYS A CE  1 
ATOM   2725 N NZ  . LYS A 1 356 ? -0.003  -18.900 44.981  1.00 44.97 ? 356  LYS A NZ  1 
ATOM   2726 N N   . PRO A 1 357 ? -0.419  -10.761 45.081  1.00 26.13 ? 357  PRO A N   1 
ATOM   2727 C CA  . PRO A 1 357 ? -0.091  -9.353  45.294  1.00 26.14 ? 357  PRO A CA  1 
ATOM   2728 C C   . PRO A 1 357 ? 1.323   -9.073  44.816  1.00 25.96 ? 357  PRO A C   1 
ATOM   2729 O O   . PRO A 1 357 ? 2.237   -9.853  45.111  1.00 26.46 ? 357  PRO A O   1 
ATOM   2730 C CB  . PRO A 1 357 ? -0.180  -9.195  46.821  1.00 26.39 ? 357  PRO A CB  1 
ATOM   2731 C CG  . PRO A 1 357 ? -1.118  -10.245 47.251  1.00 26.78 ? 357  PRO A CG  1 
ATOM   2732 C CD  . PRO A 1 357 ? -0.974  -11.398 46.285  1.00 26.18 ? 357  PRO A CD  1 
ATOM   2733 N N   . LEU A 1 358 ? 1.515   -8.010  44.058  1.00 25.34 ? 358  LEU A N   1 
ATOM   2734 C CA  . LEU A 1 358 ? 2.805   -7.818  43.462  1.00 25.74 ? 358  LEU A CA  1 
ATOM   2735 C C   . LEU A 1 358 ? 3.796   -7.376  44.528  1.00 27.38 ? 358  LEU A C   1 
ATOM   2736 O O   . LEU A 1 358 ? 3.451   -6.549  45.406  1.00 27.31 ? 358  LEU A O   1 
ATOM   2737 C CB  . LEU A 1 358 ? 2.762   -6.786  42.334  1.00 24.54 ? 358  LEU A CB  1 
ATOM   2738 C CG  . LEU A 1 358 ? 1.633   -6.789  41.306  1.00 24.85 ? 358  LEU A CG  1 
ATOM   2739 C CD1 . LEU A 1 358 ? 2.009   -5.833  40.195  1.00 22.11 ? 358  LEU A CD1 1 
ATOM   2740 C CD2 . LEU A 1 358 ? 1.258   -8.168  40.743  1.00 20.57 ? 358  LEU A CD2 1 
ATOM   2741 N N   . SER A 1 359 ? 5.016   -7.927  44.427  1.00 28.62 ? 359  SER A N   1 
ATOM   2742 C CA  . SER A 1 359 ? 6.158   -7.568  45.266  1.00 29.52 ? 359  SER A CA  1 
ATOM   2743 C C   . SER A 1 359 ? 6.394   -6.072  45.167  1.00 29.92 ? 359  SER A C   1 
ATOM   2744 O O   . SER A 1 359 ? 6.416   -5.516  44.071  1.00 30.37 ? 359  SER A O   1 
ATOM   2745 C CB  . SER A 1 359 ? 7.432   -8.342  44.823  1.00 29.93 ? 359  SER A CB  1 
ATOM   2746 O OG  . SER A 1 359 ? 8.640   -7.699  45.250  1.00 29.76 ? 359  SER A OG  1 
ATOM   2747 N N   . THR A 1 360 ? 6.560   -5.427  46.312  1.00 30.48 ? 360  THR A N   1 
ATOM   2748 C CA  . THR A 1 360 ? 6.901   -3.999  46.350  1.00 31.48 ? 360  THR A CA  1 
ATOM   2749 C C   . THR A 1 360 ? 8.406   -3.703  46.084  1.00 31.90 ? 360  THR A C   1 
ATOM   2750 O O   . THR A 1 360 ? 8.789   -2.548  45.934  1.00 31.43 ? 360  THR A O   1 
ATOM   2751 C CB  . THR A 1 360 ? 6.419   -3.354  47.688  1.00 31.47 ? 360  THR A CB  1 
ATOM   2752 O OG1 . THR A 1 360 ? 7.029   -4.035  48.779  1.00 30.18 ? 360  THR A OG1 1 
ATOM   2753 C CG2 . THR A 1 360 ? 4.891   -3.501  47.848  1.00 31.17 ? 360  THR A CG2 1 
ATOM   2754 N N   . THR A 1 361 ? 9.230   -4.745  45.969  1.00 33.32 ? 361  THR A N   1 
ATOM   2755 C CA  . THR A 1 361 ? 10.702  -4.602  46.017  1.00 34.58 ? 361  THR A CA  1 
ATOM   2756 C C   . THR A 1 361 ? 11.436  -5.154  44.788  1.00 35.27 ? 361  THR A C   1 
ATOM   2757 O O   . THR A 1 361 ? 12.498  -4.657  44.410  1.00 35.04 ? 361  THR A O   1 
ATOM   2758 C CB  . THR A 1 361 ? 11.283  -5.370  47.232  1.00 34.80 ? 361  THR A CB  1 
ATOM   2759 O OG1 . THR A 1 361 ? 11.145  -6.776  46.992  1.00 34.31 ? 361  THR A OG1 1 
ATOM   2760 C CG2 . THR A 1 361 ? 10.557  -4.995  48.548  1.00 34.52 ? 361  THR A CG2 1 
ATOM   2761 N N   . THR A 1 362 ? 10.881  -6.217  44.194  1.00 36.74 ? 362  THR A N   1 
ATOM   2762 C CA  . THR A 1 362 ? 11.429  -6.833  42.961  1.00 37.11 ? 362  THR A CA  1 
ATOM   2763 C C   . THR A 1 362 ? 10.425  -6.852  41.790  1.00 36.70 ? 362  THR A C   1 
ATOM   2764 O O   . THR A 1 362 ? 9.223   -7.000  42.006  1.00 36.79 ? 362  THR A O   1 
ATOM   2765 C CB  . THR A 1 362 ? 11.832  -8.312  43.208  1.00 37.92 ? 362  THR A CB  1 
ATOM   2766 O OG1 . THR A 1 362 ? 11.624  -8.662  44.593  1.00 39.39 ? 362  THR A OG1 1 
ATOM   2767 C CG2 . THR A 1 362 ? 13.295  -8.551  42.768  1.00 38.34 ? 362  THR A CG2 1 
ATOM   2768 N N   . VAL A 1 363 ? 10.938  -6.697  40.565  1.00 36.25 ? 363  VAL A N   1 
ATOM   2769 C CA  . VAL A 1 363 ? 10.219  -6.972  39.317  1.00 35.93 ? 363  VAL A CA  1 
ATOM   2770 C C   . VAL A 1 363 ? 9.591   -8.390  39.264  1.00 35.59 ? 363  VAL A C   1 
ATOM   2771 O O   . VAL A 1 363 ? 10.258  -9.390  39.591  1.00 34.96 ? 363  VAL A O   1 
ATOM   2772 C CB  . VAL A 1 363 ? 11.188  -6.883  38.116  1.00 36.11 ? 363  VAL A CB  1 
ATOM   2773 C CG1 . VAL A 1 363 ? 10.433  -7.076  36.805  1.00 37.08 ? 363  VAL A CG1 1 
ATOM   2774 C CG2 . VAL A 1 363 ? 11.929  -5.565  38.109  1.00 36.24 ? 363  VAL A CG2 1 
ATOM   2775 N N   . GLU A 1 364 ? 8.321   -8.461  38.846  1.00 34.62 ? 364  GLU A N   1 
ATOM   2776 C CA  . GLU A 1 364 ? 7.654   -9.745  38.550  1.00 34.15 ? 364  GLU A CA  1 
ATOM   2777 C C   . GLU A 1 364 ? 7.201   -9.783  37.092  1.00 33.71 ? 364  GLU A C   1 
ATOM   2778 O O   . GLU A 1 364 ? 6.408   -8.923  36.657  1.00 34.18 ? 364  GLU A O   1 
ATOM   2779 C CB  . GLU A 1 364 ? 6.463   -10.014 39.497  1.00 33.49 ? 364  GLU A CB  1 
ATOM   2780 C CG  . GLU A 1 364 ? 6.892   -10.073 40.954  1.00 34.16 ? 364  GLU A CG  1 
ATOM   2781 C CD  . GLU A 1 364 ? 5.802   -10.482 41.955  1.00 35.50 ? 364  GLU A CD  1 
ATOM   2782 O OE1 . GLU A 1 364 ? 6.153   -11.218 42.902  1.00 38.95 ? 364  GLU A OE1 1 
ATOM   2783 O OE2 . GLU A 1 364 ? 4.624   -10.077 41.854  1.00 33.68 ? 364  GLU A OE2 1 
ATOM   2784 N N   . ASN A 1 365 ? 7.702   -10.769 36.340  1.00 32.65 ? 365  ASN A N   1 
ATOM   2785 C CA  . ASN A 1 365 ? 7.329   -10.931 34.929  1.00 31.75 ? 365  ASN A CA  1 
ATOM   2786 C C   . ASN A 1 365 ? 5.848   -11.282 34.737  1.00 31.59 ? 365  ASN A C   1 
ATOM   2787 O O   . ASN A 1 365 ? 5.103   -11.489 35.713  1.00 30.97 ? 365  ASN A O   1 
ATOM   2788 C CB  . ASN A 1 365 ? 8.266   -11.907 34.192  1.00 31.39 ? 365  ASN A CB  1 
ATOM   2789 C CG  . ASN A 1 365 ? 8.181   -13.335 34.714  1.00 32.21 ? 365  ASN A CG  1 
ATOM   2790 O OD1 . ASN A 1 365 ? 7.084   -13.916 34.808  1.00 33.46 ? 365  ASN A OD1 1 
ATOM   2791 N ND2 . ASN A 1 365 ? 9.344   -13.935 35.020  1.00 31.84 ? 365  ASN A ND2 1 
ATOM   2792 N N   . ILE A 1 366 ? 5.418   -11.355 33.479  1.00 31.38 ? 366  ILE A N   1 
ATOM   2793 C CA  . ILE A 1 366 ? 3.993   -11.531 33.210  1.00 30.80 ? 366  ILE A CA  1 
ATOM   2794 C C   . ILE A 1 366 ? 3.455   -12.921 33.595  1.00 30.86 ? 366  ILE A C   1 
ATOM   2795 O O   . ILE A 1 366 ? 2.236   -13.105 33.701  1.00 30.44 ? 366  ILE A O   1 
ATOM   2796 C CB  . ILE A 1 366 ? 3.618   -11.145 31.754  1.00 30.88 ? 366  ILE A CB  1 
ATOM   2797 C CG1 . ILE A 1 366 ? 2.096   -10.969 31.624  1.00 30.12 ? 366  ILE A CG1 1 
ATOM   2798 C CG2 . ILE A 1 366 ? 4.142   -12.182 30.775  1.00 28.23 ? 366  ILE A CG2 1 
ATOM   2799 C CD1 . ILE A 1 366 ? 1.509   -9.761  32.316  1.00 28.20 ? 366  ILE A CD1 1 
ATOM   2800 N N   . THR A 1 367 ? 4.364   -13.876 33.823  1.00 30.82 ? 367  THR A N   1 
ATOM   2801 C CA  . THR A 1 367 ? 3.993   -15.198 34.361  1.00 30.94 ? 367  THR A CA  1 
ATOM   2802 C C   . THR A 1 367 ? 3.750   -15.119 35.856  1.00 30.71 ? 367  THR A C   1 
ATOM   2803 O O   . THR A 1 367 ? 2.708   -15.529 36.353  1.00 30.55 ? 367  THR A O   1 
ATOM   2804 C CB  . THR A 1 367 ? 5.090   -16.221 34.096  1.00 31.08 ? 367  THR A CB  1 
ATOM   2805 O OG1 . THR A 1 367 ? 5.466   -16.129 32.718  1.00 31.35 ? 367  THR A OG1 1 
ATOM   2806 C CG2 . THR A 1 367 ? 4.612   -17.652 34.434  1.00 32.03 ? 367  THR A CG2 1 
ATOM   2807 N N   . GLN A 1 368 ? 4.720   -14.553 36.572  1.00 30.73 ? 368  GLN A N   1 
ATOM   2808 C CA  . GLN A 1 368 ? 4.618   -14.434 38.028  1.00 29.78 ? 368  GLN A CA  1 
ATOM   2809 C C   . GLN A 1 368 ? 3.326   -13.710 38.381  1.00 29.04 ? 368  GLN A C   1 
ATOM   2810 O O   . GLN A 1 368 ? 2.655   -14.100 39.343  1.00 28.81 ? 368  GLN A O   1 
ATOM   2811 C CB  . GLN A 1 368 ? 5.854   -13.753 38.624  1.00 29.81 ? 368  GLN A CB  1 
ATOM   2812 C CG  . GLN A 1 368 ? 7.167   -14.341 38.103  1.00 31.28 ? 368  GLN A CG  1 
ATOM   2813 C CD  . GLN A 1 368 ? 8.409   -13.610 38.619  1.00 32.34 ? 368  GLN A CD  1 
ATOM   2814 O OE1 . GLN A 1 368 ? 9.104   -12.921 37.872  1.00 30.82 ? 368  GLN A OE1 1 
ATOM   2815 N NE2 . GLN A 1 368 ? 8.699   -13.781 39.898  1.00 33.87 ? 368  GLN A NE2 1 
ATOM   2816 N N   . THR A 1 369 ? 2.933   -12.714 37.575  1.00 27.72 ? 369  THR A N   1 
ATOM   2817 C CA  . THR A 1 369 ? 1.698   -11.959 37.868  1.00 26.72 ? 369  THR A CA  1 
ATOM   2818 C C   . THR A 1 369 ? 0.395   -12.580 37.268  1.00 26.30 ? 369  THR A C   1 
ATOM   2819 O O   . THR A 1 369 ? -0.713  -12.005 37.384  1.00 25.52 ? 369  THR A O   1 
ATOM   2820 C CB  . THR A 1 369 ? 1.827   -10.446 37.529  1.00 26.30 ? 369  THR A CB  1 
ATOM   2821 O OG1 . THR A 1 369 ? 1.985   -10.283 36.115  1.00 27.35 ? 369  THR A OG1 1 
ATOM   2822 C CG2 . THR A 1 369 ? 2.996   -9.841  38.216  1.00 24.34 ? 369  THR A CG2 1 
ATOM   2823 N N   . ASP A 1 370 ? 0.545   -13.760 36.637  1.00 26.55 ? 370  ASP A N   1 
ATOM   2824 C CA  . ASP A 1 370 ? -0.561  -14.515 36.005  1.00 24.88 ? 370  ASP A CA  1 
ATOM   2825 C C   . ASP A 1 370 ? -1.342  -13.596 35.031  1.00 24.37 ? 370  ASP A C   1 
ATOM   2826 O O   . ASP A 1 370 ? -2.591  -13.527 35.037  1.00 23.90 ? 370  ASP A O   1 
ATOM   2827 C CB  . ASP A 1 370 ? -1.482  -15.124 37.064  1.00 25.06 ? 370  ASP A CB  1 
ATOM   2828 C CG  . ASP A 1 370 ? -2.438  -16.152 36.494  1.00 27.72 ? 370  ASP A CG  1 
ATOM   2829 O OD1 . ASP A 1 370 ? -1.976  -16.953 35.656  1.00 30.29 ? 370  ASP A OD1 1 
ATOM   2830 O OD2 . ASP A 1 370 ? -3.643  -16.187 36.895  1.00 29.03 ? 370  ASP A OD2 1 
ATOM   2831 N N   . GLY A 1 371 ? -0.601  -12.866 34.211  1.00 22.53 ? 371  GLY A N   1 
ATOM   2832 C CA  . GLY A 1 371 ? -1.238  -12.039 33.198  1.00 21.94 ? 371  GLY A CA  1 
ATOM   2833 C C   . GLY A 1 371 ? -1.637  -10.626 33.584  1.00 20.84 ? 371  GLY A C   1 
ATOM   2834 O O   . GLY A 1 371 ? -2.285  -9.954  32.831  1.00 20.92 ? 371  GLY A O   1 
ATOM   2835 N N   . PHE A 1 372 ? -1.224  -10.145 34.741  1.00 20.28 ? 372  PHE A N   1 
ATOM   2836 C CA  . PHE A 1 372 ? -1.539  -8.765  35.077  1.00 19.01 ? 372  PHE A CA  1 
ATOM   2837 C C   . PHE A 1 372 ? -0.396  -7.805  34.875  1.00 18.77 ? 372  PHE A C   1 
ATOM   2838 O O   . PHE A 1 372 ? 0.720   -8.040  35.348  1.00 18.80 ? 372  PHE A O   1 
ATOM   2839 C CB  . PHE A 1 372 ? -2.028  -8.581  36.513  1.00 19.22 ? 372  PHE A CB  1 
ATOM   2840 C CG  . PHE A 1 372 ? -2.255  -7.166  36.827  1.00 18.01 ? 372  PHE A CG  1 
ATOM   2841 C CD1 . PHE A 1 372 ? -3.433  -6.552  36.431  1.00 18.27 ? 372  PHE A CD1 1 
ATOM   2842 C CD2 . PHE A 1 372 ? -1.244  -6.405  37.393  1.00 18.26 ? 372  PHE A CD2 1 
ATOM   2843 C CE1 . PHE A 1 372 ? -3.616  -5.209  36.640  1.00 18.37 ? 372  PHE A CE1 1 
ATOM   2844 C CE2 . PHE A 1 372 ? -1.410  -5.075  37.607  1.00 17.24 ? 372  PHE A CE2 1 
ATOM   2845 C CZ  . PHE A 1 372 ? -2.592  -4.459  37.229  1.00 18.11 ? 372  PHE A CZ  1 
ATOM   2846 N N   . SER A 1 373 ? -0.676  -6.722  34.163  1.00 18.10 ? 373  SER A N   1 
ATOM   2847 C CA  . SER A 1 373 ? 0.213   -5.583  34.118  1.00 17.88 ? 373  SER A CA  1 
ATOM   2848 C C   . SER A 1 373 ? -0.587  -4.418  33.589  1.00 17.34 ? 373  SER A C   1 
ATOM   2849 O O   . SER A 1 373 ? -1.603  -4.621  32.921  1.00 17.62 ? 373  SER A O   1 
ATOM   2850 C CB  . SER A 1 373 ? 1.430   -5.843  33.225  1.00 18.28 ? 373  SER A CB  1 
ATOM   2851 O OG  . SER A 1 373 ? 1.120   -5.678  31.856  1.00 17.89 ? 373  SER A OG  1 
ATOM   2852 N N   . SER A 1 374 ? -0.144  -3.201  33.879  1.00 16.07 ? 374  SER A N   1 
ATOM   2853 C CA  . SER A 1 374 ? -0.815  -2.048  33.327  1.00 16.57 ? 374  SER A CA  1 
ATOM   2854 C C   . SER A 1 374 ? -0.965  -2.168  31.842  1.00 16.19 ? 374  SER A C   1 
ATOM   2855 O O   . SER A 1 374 ? -2.050  -1.947  31.307  1.00 16.80 ? 374  SER A O   1 
ATOM   2856 C CB  . SER A 1 374 ? -0.028  -0.800  33.593  1.00 15.84 ? 374  SER A CB  1 
ATOM   2857 O OG  . SER A 1 374 ? -0.334  -0.332  34.875  1.00 21.54 ? 374  SER A OG  1 
ATOM   2858 N N   . ALA A 1 375 ? 0.155   -2.474  31.194  1.00 15.45 ? 375  ALA A N   1 
ATOM   2859 C CA  . ALA A 1 375 ? 0.267   -2.459  29.758  1.00 15.78 ? 375  ALA A CA  1 
ATOM   2860 C C   . ALA A 1 375 ? -0.575  -3.568  29.107  1.00 15.32 ? 375  ALA A C   1 
ATOM   2861 O O   . ALA A 1 375 ? -1.064  -3.376  27.987  1.00 15.79 ? 375  ALA A O   1 
ATOM   2862 C CB  . ALA A 1 375 ? 1.787   -2.575  29.322  1.00 15.91 ? 375  ALA A CB  1 
ATOM   2863 N N   . TRP A 1 376 ? -0.733  -4.695  29.803  1.00 13.61 ? 376  TRP A N   1 
ATOM   2864 C CA  . TRP A 1 376 ? -1.593  -5.779  29.345  1.00 14.55 ? 376  TRP A CA  1 
ATOM   2865 C C   . TRP A 1 376 ? -3.074  -5.542  29.691  1.00 14.90 ? 376  TRP A C   1 
ATOM   2866 O O   . TRP A 1 376 ? -3.931  -6.299  29.254  1.00 15.72 ? 376  TRP A O   1 
ATOM   2867 C CB  . TRP A 1 376 ? -1.115  -7.140  29.924  1.00 12.60 ? 376  TRP A CB  1 
ATOM   2868 C CG  . TRP A 1 376 ? 0.073   -7.692  29.188  1.00 14.54 ? 376  TRP A CG  1 
ATOM   2869 C CD1 . TRP A 1 376 ? 1.142   -6.983  28.655  1.00 15.45 ? 376  TRP A CD1 1 
ATOM   2870 C CD2 . TRP A 1 376 ? 0.314   -9.065  28.870  1.00 14.46 ? 376  TRP A CD2 1 
ATOM   2871 N NE1 . TRP A 1 376 ? 2.005   -7.838  28.029  1.00 16.07 ? 376  TRP A NE1 1 
ATOM   2872 C CE2 . TRP A 1 376 ? 1.524   -9.121  28.151  1.00 14.24 ? 376  TRP A CE2 1 
ATOM   2873 C CE3 . TRP A 1 376 ? -0.396  -10.261 29.120  1.00 14.38 ? 376  TRP A CE3 1 
ATOM   2874 C CZ2 . TRP A 1 376 ? 2.049   -10.324 27.666  1.00 14.91 ? 376  TRP A CZ2 1 
ATOM   2875 C CZ3 . TRP A 1 376 ? 0.130   -11.454 28.669  1.00 16.06 ? 376  TRP A CZ3 1 
ATOM   2876 C CH2 . TRP A 1 376 ? 1.348   -11.481 27.944  1.00 17.44 ? 376  TRP A CH2 1 
ATOM   2877 N N   . THR A 1 377 ? -3.394  -4.518  30.466  1.00 14.88 ? 377  THR A N   1 
ATOM   2878 C CA  . THR A 1 377 ? -4.800  -4.352  30.851  1.00 15.85 ? 377  THR A CA  1 
ATOM   2879 C C   . THR A 1 377 ? -5.365  -2.994  30.442  1.00 15.89 ? 377  THR A C   1 
ATOM   2880 O O   . THR A 1 377 ? -6.354  -2.922  29.706  1.00 16.86 ? 377  THR A O   1 
ATOM   2881 C CB  . THR A 1 377 ? -5.052  -4.639  32.360  1.00 15.91 ? 377  THR A CB  1 
ATOM   2882 O OG1 . THR A 1 377 ? -4.300  -3.708  33.133  1.00 17.51 ? 377  THR A OG1 1 
ATOM   2883 C CG2 . THR A 1 377 ? -4.557  -6.028  32.751  1.00 15.63 ? 377  THR A CG2 1 
ATOM   2884 N N   . VAL A 1 378 ? -4.737  -1.914  30.896  1.00 16.20 ? 378  VAL A N   1 
ATOM   2885 C CA  . VAL A 1 378 ? -5.194  -0.580  30.565  1.00 14.99 ? 378  VAL A CA  1 
ATOM   2886 C C   . VAL A 1 378 ? -4.223  0.274   29.781  1.00 15.60 ? 378  VAL A C   1 
ATOM   2887 O O   . VAL A 1 378 ? -3.914  1.392   30.199  1.00 15.10 ? 378  VAL A O   1 
ATOM   2888 C CB  . VAL A 1 378 ? -5.543  0.142   31.822  1.00 15.99 ? 378  VAL A CB  1 
ATOM   2889 C CG1 . VAL A 1 378 ? -6.626  -0.588  32.481  1.00 13.25 ? 378  VAL A CG1 1 
ATOM   2890 C CG2 . VAL A 1 378 ? -4.253  0.263   32.802  1.00 16.09 ? 378  VAL A CG2 1 
ATOM   2891 N N   . PRO A 1 379 ? -3.782  -0.203  28.605  1.00 16.10 ? 379  PRO A N   1 
ATOM   2892 C CA  . PRO A 1 379 ? -2.959  0.680   27.785  1.00 16.78 ? 379  PRO A CA  1 
ATOM   2893 C C   . PRO A 1 379 ? -3.805  1.786   27.217  1.00 17.73 ? 379  PRO A C   1 
ATOM   2894 O O   . PRO A 1 379 ? -5.020  1.810   27.473  1.00 18.81 ? 379  PRO A O   1 
ATOM   2895 C CB  . PRO A 1 379 ? -2.489  -0.231  26.648  1.00 17.47 ? 379  PRO A CB  1 
ATOM   2896 C CG  . PRO A 1 379 ? -3.501  -1.379  26.640  1.00 16.97 ? 379  PRO A CG  1 
ATOM   2897 C CD  . PRO A 1 379 ? -3.853  -1.570  28.061  1.00 15.74 ? 379  PRO A CD  1 
ATOM   2898 N N   . PHE A 1 380 ? -3.203  2.700   26.465  1.00 17.66 ? 380  PHE A N   1 
ATOM   2899 C CA  . PHE A 1 380 ? -4.026  3.646   25.718  1.00 18.95 ? 380  PHE A CA  1 
ATOM   2900 C C   . PHE A 1 380 ? -4.975  2.833   24.802  1.00 19.33 ? 380  PHE A C   1 
ATOM   2901 O O   . PHE A 1 380 ? -4.530  1.833   24.155  1.00 18.94 ? 380  PHE A O   1 
ATOM   2902 C CB  . PHE A 1 380 ? -3.173  4.582   24.848  1.00 18.53 ? 380  PHE A CB  1 
ATOM   2903 C CG  . PHE A 1 380 ? -2.525  5.691   25.604  1.00 19.33 ? 380  PHE A CG  1 
ATOM   2904 C CD1 . PHE A 1 380 ? -3.251  6.461   26.480  1.00 19.05 ? 380  PHE A CD1 1 
ATOM   2905 C CD2 . PHE A 1 380 ? -1.173  5.989   25.402  1.00 20.81 ? 380  PHE A CD2 1 
ATOM   2906 C CE1 . PHE A 1 380 ? -2.656  7.497   27.158  1.00 20.11 ? 380  PHE A CE1 1 
ATOM   2907 C CE2 . PHE A 1 380 ? -0.574  7.035   26.065  1.00 22.57 ? 380  PHE A CE2 1 
ATOM   2908 C CZ  . PHE A 1 380 ? -1.321  7.796   26.950  1.00 20.44 ? 380  PHE A CZ  1 
ATOM   2909 N N   . ALA A 1 381 ? -6.259  3.246   24.765  1.00 18.99 ? 381  ALA A N   1 
ATOM   2910 C CA  . ALA A 1 381 ? -7.259  2.618   23.900  1.00 18.30 ? 381  ALA A CA  1 
ATOM   2911 C C   . ALA A 1 381 ? -7.543  1.122   24.233  1.00 17.97 ? 381  ALA A C   1 
ATOM   2912 O O   . ALA A 1 381 ? -8.035  0.378   23.410  1.00 18.41 ? 381  ALA A O   1 
ATOM   2913 C CB  . ALA A 1 381 ? -6.802  2.767   22.455  1.00 17.32 ? 381  ALA A CB  1 
ATOM   2914 N N   . SER A 1 382 ? -7.227  0.686   25.439  1.00 17.50 ? 382  SER A N   1 
ATOM   2915 C CA  . SER A 1 382 ? -7.525  -0.664  25.879  1.00 17.05 ? 382  SER A CA  1 
ATOM   2916 C C   . SER A 1 382 ? -8.978  -1.019  25.643  1.00 17.14 ? 382  SER A C   1 
ATOM   2917 O O   . SER A 1 382 ? -9.880  -0.142  25.628  1.00 16.86 ? 382  SER A O   1 
ATOM   2918 C CB  . SER A 1 382 ? -7.283  -0.789  27.374  1.00 16.81 ? 382  SER A CB  1 
ATOM   2919 O OG  . SER A 1 382 ? -8.351  -0.181  28.085  1.00 18.87 ? 382  SER A OG  1 
ATOM   2920 N N   . ARG A 1 383 ? -9.229  -2.320  25.551  1.00 17.05 ? 383  ARG A N   1 
ATOM   2921 C CA  . ARG A 1 383 ? -10.622 -2.805  25.466  1.00 17.53 ? 383  ARG A CA  1 
ATOM   2922 C C   . ARG A 1 383 ? -10.863 -4.123  26.235  1.00 17.78 ? 383  ARG A C   1 
ATOM   2923 O O   . ARG A 1 383 ? -9.987  -5.035  26.274  1.00 17.31 ? 383  ARG A O   1 
ATOM   2924 C CB  . ARG A 1 383 ? -11.120 -2.882  23.989  1.00 17.20 ? 383  ARG A CB  1 
ATOM   2925 C CG  . ARG A 1 383 ? -10.441 -3.946  23.088  1.00 16.77 ? 383  ARG A CG  1 
ATOM   2926 C CD  . ARG A 1 383 ? -8.945  -3.744  22.800  1.00 17.24 ? 383  ARG A CD  1 
ATOM   2927 N NE  . ARG A 1 383 ? -8.590  -2.411  22.302  1.00 17.61 ? 383  ARG A NE  1 
ATOM   2928 C CZ  . ARG A 1 383 ? -8.388  -2.106  21.025  1.00 15.99 ? 383  ARG A CZ  1 
ATOM   2929 N NH1 . ARG A 1 383 ? -8.561  -3.034  20.093  1.00 16.57 ? 383  ARG A NH1 1 
ATOM   2930 N NH2 . ARG A 1 383 ? -8.040  -0.877  20.681  1.00 12.75 ? 383  ARG A NH2 1 
ATOM   2931 N N   . LEU A 1 384 ? -12.029 -4.179  26.875  1.00 16.56 ? 384  LEU A N   1 
ATOM   2932 C CA  . LEU A 1 384 ? -12.508 -5.398  27.447  1.00 17.36 ? 384  LEU A CA  1 
ATOM   2933 C C   . LEU A 1 384 ? -13.698 -5.828  26.636  1.00 17.48 ? 384  LEU A C   1 
ATOM   2934 O O   . LEU A 1 384 ? -14.604 -4.991  26.422  1.00 18.22 ? 384  LEU A O   1 
ATOM   2935 C CB  . LEU A 1 384 ? -13.009 -5.107  28.878  1.00 18.66 ? 384  LEU A CB  1 
ATOM   2936 C CG  . LEU A 1 384 ? -13.932 -6.086  29.654  1.00 18.13 ? 384  LEU A CG  1 
ATOM   2937 C CD1 . LEU A 1 384 ? -13.088 -7.271  30.282  1.00 19.97 ? 384  LEU A CD1 1 
ATOM   2938 C CD2 . LEU A 1 384 ? -14.713 -5.369  30.720  1.00 12.16 ? 384  LEU A CD2 1 
ATOM   2939 N N   . TYR A 1 385 ? -13.764 -7.104  26.229  1.00 16.77 ? 385  TYR A N   1 
ATOM   2940 C CA  . TYR A 1 385 ? -15.005 -7.647  25.629  1.00 15.95 ? 385  TYR A CA  1 
ATOM   2941 C C   . TYR A 1 385 ? -15.640 -8.717  26.528  1.00 16.57 ? 385  TYR A C   1 
ATOM   2942 O O   . TYR A 1 385 ? -15.012 -9.752  26.851  1.00 16.59 ? 385  TYR A O   1 
ATOM   2943 C CB  . TYR A 1 385 ? -14.791 -8.311  24.264  1.00 16.18 ? 385  TYR A CB  1 
ATOM   2944 C CG  . TYR A 1 385 ? -14.094 -7.531  23.157  1.00 15.85 ? 385  TYR A CG  1 
ATOM   2945 C CD1 . TYR A 1 385 ? -14.362 -6.158  22.928  1.00 14.99 ? 385  TYR A CD1 1 
ATOM   2946 C CD2 . TYR A 1 385 ? -13.216 -8.175  22.301  1.00 15.85 ? 385  TYR A CD2 1 
ATOM   2947 C CE1 . TYR A 1 385 ? -13.728 -5.458  21.909  1.00 14.70 ? 385  TYR A CE1 1 
ATOM   2948 C CE2 . TYR A 1 385 ? -12.575 -7.484  21.252  1.00 17.78 ? 385  TYR A CE2 1 
ATOM   2949 C CZ  . TYR A 1 385 ? -12.846 -6.138  21.063  1.00 16.80 ? 385  TYR A CZ  1 
ATOM   2950 O OH  . TYR A 1 385 ? -12.218 -5.488  20.054  1.00 16.02 ? 385  TYR A OH  1 
ATOM   2951 N N   . VAL A 1 386 ? -16.882 -8.491  26.934  1.00 16.07 ? 386  VAL A N   1 
ATOM   2952 C CA  . VAL A 1 386 ? -17.596 -9.551  27.555  1.00 16.38 ? 386  VAL A CA  1 
ATOM   2953 C C   . VAL A 1 386 ? -18.493 -10.209 26.471  1.00 18.26 ? 386  VAL A C   1 
ATOM   2954 O O   . VAL A 1 386 ? -19.239 -9.499  25.736  1.00 18.49 ? 386  VAL A O   1 
ATOM   2955 C CB  . VAL A 1 386 ? -18.417 -9.023  28.724  1.00 16.81 ? 386  VAL A CB  1 
ATOM   2956 C CG1 . VAL A 1 386 ? -19.259 -10.157 29.363  1.00 14.95 ? 386  VAL A CG1 1 
ATOM   2957 C CG2 . VAL A 1 386 ? -17.502 -8.335  29.774  1.00 14.28 ? 386  VAL A CG2 1 
ATOM   2958 N N   . GLU A 1 387 ? -18.391 -11.534 26.308  1.00 18.44 ? 387  GLU A N   1 
ATOM   2959 C CA  . GLU A 1 387 ? -19.365 -12.229 25.434  1.00 19.97 ? 387  GLU A CA  1 
ATOM   2960 C C   . GLU A 1 387 ? -20.205 -13.238 26.162  1.00 20.21 ? 387  GLU A C   1 
ATOM   2961 O O   . GLU A 1 387 ? -19.864 -13.758 27.227  1.00 20.67 ? 387  GLU A O   1 
ATOM   2962 C CB  . GLU A 1 387 ? -18.756 -12.834 24.149  1.00 18.70 ? 387  GLU A CB  1 
ATOM   2963 C CG  . GLU A 1 387 ? -17.316 -12.750 24.154  1.00 21.56 ? 387  GLU A CG  1 
ATOM   2964 C CD  . GLU A 1 387 ? -16.651 -13.398 22.993  1.00 21.11 ? 387  GLU A CD  1 
ATOM   2965 O OE1 . GLU A 1 387 ? -16.361 -12.661 22.006  1.00 18.47 ? 387  GLU A OE1 1 
ATOM   2966 O OE2 . GLU A 1 387 ? -16.329 -14.615 23.144  1.00 20.06 ? 387  GLU A OE2 1 
ATOM   2967 N N   . MET A 1 388 ? -21.340 -13.474 25.564  1.00 21.28 ? 388  MET A N   1 
ATOM   2968 C CA  . MET A 1 388 ? -22.191 -14.541 25.958  1.00 22.43 ? 388  MET A CA  1 
ATOM   2969 C C   . MET A 1 388 ? -22.449 -15.291 24.655  1.00 22.64 ? 388  MET A C   1 
ATOM   2970 O O   . MET A 1 388 ? -22.700 -14.671 23.643  1.00 22.77 ? 388  MET A O   1 
ATOM   2971 C CB  . MET A 1 388 ? -23.429 -13.906 26.562  1.00 22.20 ? 388  MET A CB  1 
ATOM   2972 C CG  . MET A 1 388 ? -24.330 -14.809 27.329  1.00 24.44 ? 388  MET A CG  1 
ATOM   2973 S SD  . MET A 1 388 ? -25.077 -13.924 28.702  1.00 23.79 ? 388  MET A SD  1 
ATOM   2974 C CE  . MET A 1 388 ? -26.167 -12.812 27.848  1.00 24.91 ? 388  MET A CE  1 
ATOM   2975 N N   . MET A 1 389 ? -22.331 -16.612 24.658  1.00 24.03 ? 389  MET A N   1 
ATOM   2976 C CA  . MET A 1 389 ? -22.543 -17.414 23.449  1.00 25.37 ? 389  MET A CA  1 
ATOM   2977 C C   . MET A 1 389 ? -23.412 -18.575 23.757  1.00 27.35 ? 389  MET A C   1 
ATOM   2978 O O   . MET A 1 389 ? -23.463 -19.044 24.894  1.00 27.45 ? 389  MET A O   1 
ATOM   2979 C CB  . MET A 1 389 ? -21.220 -17.964 22.867  1.00 24.91 ? 389  MET A CB  1 
ATOM   2980 C CG  . MET A 1 389 ? -20.425 -18.882 23.774  1.00 22.51 ? 389  MET A CG  1 
ATOM   2981 S SD  . MET A 1 389 ? -18.803 -19.451 23.097  1.00 24.37 ? 389  MET A SD  1 
ATOM   2982 C CE  . MET A 1 389 ? -18.000 -17.891 22.691  1.00 24.02 ? 389  MET A CE  1 
ATOM   2983 N N   . GLN A 1 390 ? -24.075 -19.064 22.726  1.00 29.38 ? 390  GLN A N   1 
ATOM   2984 C CA  . GLN A 1 390 ? -24.905 -20.237 22.861  1.00 31.80 ? 390  GLN A CA  1 
ATOM   2985 C C   . GLN A 1 390 ? -24.283 -21.332 22.054  1.00 32.71 ? 390  GLN A C   1 
ATOM   2986 O O   . GLN A 1 390 ? -23.921 -21.130 20.913  1.00 32.97 ? 390  GLN A O   1 
ATOM   2987 C CB  . GLN A 1 390 ? -26.317 -19.985 22.381  1.00 31.73 ? 390  GLN A CB  1 
ATOM   2988 C CG  . GLN A 1 390 ? -27.271 -20.777 23.177  1.00 34.28 ? 390  GLN A CG  1 
ATOM   2989 C CD  . GLN A 1 390 ? -27.673 -20.053 24.415  1.00 37.92 ? 390  GLN A CD  1 
ATOM   2990 O OE1 . GLN A 1 390 ? -28.474 -20.558 25.178  1.00 42.02 ? 390  GLN A OE1 1 
ATOM   2991 N NE2 . GLN A 1 390 ? -27.157 -18.835 24.607  1.00 38.81 ? 390  GLN A NE2 1 
ATOM   2992 N N   . CYS A 1 391 ? -24.123 -22.486 22.667  1.00 34.88 ? 391  CYS A N   1 
ATOM   2993 C CA  . CYS A 1 391 ? -23.339 -23.531 22.042  1.00 37.70 ? 391  CYS A CA  1 
ATOM   2994 C C   . CYS A 1 391 ? -24.148 -24.773 21.803  1.00 39.89 ? 391  CYS A C   1 
ATOM   2995 O O   . CYS A 1 391 ? -25.212 -24.959 22.401  1.00 40.46 ? 391  CYS A O   1 
ATOM   2996 C CB  . CYS A 1 391 ? -22.100 -23.851 22.860  1.00 37.29 ? 391  CYS A CB  1 
ATOM   2997 S SG  . CYS A 1 391 ? -20.923 -22.502 22.840  1.00 35.76 ? 391  CYS A SG  1 
ATOM   2998 N N   . GLN A 1 392 ? -23.621 -25.611 20.911  1.00 42.95 ? 392  GLN A N   1 
ATOM   2999 C CA  . GLN A 1 392 ? -24.288 -26.829 20.451  1.00 45.33 ? 392  GLN A CA  1 
ATOM   3000 C C   . GLN A 1 392 ? -24.570 -27.768 21.599  1.00 45.99 ? 392  GLN A C   1 
ATOM   3001 O O   . GLN A 1 392 ? -25.719 -28.155 21.807  1.00 47.25 ? 392  GLN A O   1 
ATOM   3002 C CB  . GLN A 1 392 ? -23.460 -27.535 19.368  1.00 45.64 ? 392  GLN A CB  1 
ATOM   3003 N N   . ALA A 1 393 ? -23.543 -28.099 22.370  1.00 46.41 ? 393  ALA A N   1 
ATOM   3004 C CA  . ALA A 1 393 ? -23.686 -29.180 23.341  1.00 46.84 ? 393  ALA A CA  1 
ATOM   3005 C C   . ALA A 1 393 ? -24.492 -28.890 24.641  1.00 46.61 ? 393  ALA A C   1 
ATOM   3006 O O   . ALA A 1 393 ? -24.733 -29.815 25.431  1.00 46.29 ? 393  ALA A O   1 
ATOM   3007 C CB  . ALA A 1 393 ? -22.289 -29.787 23.653  1.00 47.31 ? 393  ALA A CB  1 
ATOM   3008 N N   . GLU A 1 394 ? -24.914 -27.628 24.841  1.00 46.30 ? 394  GLU A N   1 
ATOM   3009 C CA  . GLU A 1 394 ? -25.355 -27.123 26.171  1.00 45.31 ? 394  GLU A CA  1 
ATOM   3010 C C   . GLU A 1 394 ? -26.566 -26.164 26.143  1.00 44.46 ? 394  GLU A C   1 
ATOM   3011 O O   . GLU A 1 394 ? -26.632 -25.272 25.302  1.00 44.53 ? 394  GLU A O   1 
ATOM   3012 C CB  . GLU A 1 394 ? -24.155 -26.471 26.886  1.00 45.48 ? 394  GLU A CB  1 
ATOM   3013 C CG  . GLU A 1 394 ? -24.471 -25.491 28.035  1.00 46.72 ? 394  GLU A CG  1 
ATOM   3014 C CD  . GLU A 1 394 ? -24.658 -26.143 29.415  1.00 49.34 ? 394  GLU A CD  1 
ATOM   3015 O OE1 . GLU A 1 394 ? -23.725 -26.829 29.903  1.00 49.10 ? 394  GLU A OE1 1 
ATOM   3016 O OE2 . GLU A 1 394 ? -25.737 -25.929 30.028  1.00 49.61 ? 394  GLU A OE2 1 
ATOM   3017 N N   . GLN A 1 395 ? -27.501 -26.329 27.082  1.00 43.11 ? 395  GLN A N   1 
ATOM   3018 C CA  . GLN A 1 395 ? -28.726 -25.492 27.137  1.00 41.63 ? 395  GLN A CA  1 
ATOM   3019 C C   . GLN A 1 395 ? -28.495 -24.024 27.546  1.00 40.12 ? 395  GLN A C   1 
ATOM   3020 O O   . GLN A 1 395 ? -29.169 -23.124 27.048  1.00 39.73 ? 395  GLN A O   1 
ATOM   3021 C CB  . GLN A 1 395 ? -29.775 -26.124 28.068  1.00 42.03 ? 395  GLN A CB  1 
ATOM   3022 N N   . GLU A 1 396 ? -27.525 -23.800 28.434  1.00 37.62 ? 396  GLU A N   1 
ATOM   3023 C CA  . GLU A 1 396 ? -27.265 -22.490 29.053  1.00 35.17 ? 396  GLU A CA  1 
ATOM   3024 C C   . GLU A 1 396 ? -26.278 -21.592 28.293  1.00 32.65 ? 396  GLU A C   1 
ATOM   3025 O O   . GLU A 1 396 ? -25.356 -22.097 27.631  1.00 32.83 ? 396  GLU A O   1 
ATOM   3026 C CB  . GLU A 1 396 ? -26.676 -22.718 30.442  1.00 35.47 ? 396  GLU A CB  1 
ATOM   3027 C CG  . GLU A 1 396 ? -27.691 -22.816 31.573  1.00 38.32 ? 396  GLU A CG  1 
ATOM   3028 C CD  . GLU A 1 396 ? -27.036 -22.703 32.953  1.00 41.98 ? 396  GLU A CD  1 
ATOM   3029 O OE1 . GLU A 1 396 ? -26.686 -21.543 33.351  1.00 43.68 ? 396  GLU A OE1 1 
ATOM   3030 O OE2 . GLU A 1 396 ? -26.888 -23.770 33.613  1.00 39.38 ? 396  GLU A OE2 1 
ATOM   3031 N N   . PRO A 1 397 ? -26.419 -20.257 28.441  1.00 29.53 ? 397  PRO A N   1 
ATOM   3032 C CA  . PRO A 1 397 ? -25.422 -19.375 27.823  1.00 27.22 ? 397  PRO A CA  1 
ATOM   3033 C C   . PRO A 1 397 ? -24.066 -19.453 28.540  1.00 24.97 ? 397  PRO A C   1 
ATOM   3034 O O   . PRO A 1 397 ? -24.024 -19.553 29.739  1.00 24.13 ? 397  PRO A O   1 
ATOM   3035 C CB  . PRO A 1 397 ? -26.045 -17.974 27.957  1.00 26.88 ? 397  PRO A CB  1 
ATOM   3036 C CG  . PRO A 1 397 ? -27.316 -18.144 28.796  1.00 27.46 ? 397  PRO A CG  1 
ATOM   3037 C CD  . PRO A 1 397 ? -27.320 -19.525 29.354  1.00 29.27 ? 397  PRO A CD  1 
ATOM   3038 N N   . LEU A 1 398 ? -22.985 -19.423 27.792  1.00 22.90 ? 398  LEU A N   1 
ATOM   3039 C CA  . LEU A 1 398 ? -21.655 -19.510 28.328  1.00 21.98 ? 398  LEU A CA  1 
ATOM   3040 C C   . LEU A 1 398 ? -20.989 -18.108 28.249  1.00 22.12 ? 398  LEU A C   1 
ATOM   3041 O O   . LEU A 1 398 ? -21.013 -17.476 27.165  1.00 22.85 ? 398  LEU A O   1 
ATOM   3042 C CB  . LEU A 1 398 ? -20.850 -20.513 27.482  1.00 22.14 ? 398  LEU A CB  1 
ATOM   3043 C CG  . LEU A 1 398 ? -21.179 -22.022 27.467  1.00 20.47 ? 398  LEU A CG  1 
ATOM   3044 C CD1 . LEU A 1 398 ? -19.964 -22.755 27.016  1.00 19.36 ? 398  LEU A CD1 1 
ATOM   3045 C CD2 . LEU A 1 398 ? -21.564 -22.542 28.847  1.00 19.44 ? 398  LEU A CD2 1 
ATOM   3046 N N   . VAL A 1 399 ? -20.418 -17.604 29.358  1.00 19.86 ? 399  VAL A N   1 
ATOM   3047 C CA  . VAL A 1 399 ? -19.832 -16.279 29.359  1.00 17.85 ? 399  VAL A CA  1 
ATOM   3048 C C   . VAL A 1 399 ? -18.358 -16.393 29.021  1.00 18.45 ? 399  VAL A C   1 
ATOM   3049 O O   . VAL A 1 399 ? -17.674 -17.269 29.535  1.00 17.81 ? 399  VAL A O   1 
ATOM   3050 C CB  . VAL A 1 399 ? -19.938 -15.659 30.727  1.00 17.76 ? 399  VAL A CB  1 
ATOM   3051 C CG1 . VAL A 1 399 ? -19.113 -14.393 30.791  1.00 17.95 ? 399  VAL A CG1 1 
ATOM   3052 C CG2 . VAL A 1 399 ? -21.373 -15.367 31.090  1.00 16.08 ? 399  VAL A CG2 1 
ATOM   3053 N N   . ARG A 1 400 ? -17.843 -15.514 28.162  1.00 18.49 ? 400  ARG A N   1 
ATOM   3054 C CA  . ARG A 1 400 ? -16.395 -15.449 27.957  1.00 18.36 ? 400  ARG A CA  1 
ATOM   3055 C C   . ARG A 1 400 ? -15.922 -14.005 27.979  1.00 18.81 ? 400  ARG A C   1 
ATOM   3056 O O   . ARG A 1 400 ? -16.687 -13.105 27.596  1.00 19.63 ? 400  ARG A O   1 
ATOM   3057 C CB  . ARG A 1 400 ? -16.003 -16.136 26.672  1.00 18.58 ? 400  ARG A CB  1 
ATOM   3058 C CG  . ARG A 1 400 ? -14.561 -15.960 26.296  1.00 20.26 ? 400  ARG A CG  1 
ATOM   3059 C CD  . ARG A 1 400 ? -14.173 -16.822 25.084  1.00 20.06 ? 400  ARG A CD  1 
ATOM   3060 N NE  . ARG A 1 400 ? -14.564 -16.188 23.830  1.00 23.42 ? 400  ARG A NE  1 
ATOM   3061 C CZ  . ARG A 1 400 ? -14.140 -16.562 22.627  1.00 23.20 ? 400  ARG A CZ  1 
ATOM   3062 N NH1 . ARG A 1 400 ? -13.296 -17.571 22.517  1.00 23.52 ? 400  ARG A NH1 1 
ATOM   3063 N NH2 . ARG A 1 400 ? -14.551 -15.901 21.535  1.00 21.73 ? 400  ARG A NH2 1 
ATOM   3064 N N   . VAL A 1 401 ? -14.677 -13.787 28.422  1.00 18.42 ? 401  VAL A N   1 
ATOM   3065 C CA  . VAL A 1 401 ? -14.093 -12.454 28.605  1.00 17.44 ? 401  VAL A CA  1 
ATOM   3066 C C   . VAL A 1 401 ? -12.751 -12.339 27.892  1.00 17.45 ? 401  VAL A C   1 
ATOM   3067 O O   . VAL A 1 401 ? -11.896 -13.215 28.077  1.00 16.69 ? 401  VAL A O   1 
ATOM   3068 C CB  . VAL A 1 401 ? -13.892 -12.160 30.084  1.00 16.68 ? 401  VAL A CB  1 
ATOM   3069 C CG1 . VAL A 1 401 ? -12.803 -11.148 30.275  1.00 17.89 ? 401  VAL A CG1 1 
ATOM   3070 C CG2 . VAL A 1 401 ? -15.171 -11.614 30.697  1.00 16.94 ? 401  VAL A CG2 1 
ATOM   3071 N N   . LEU A 1 402 ? -12.561 -11.300 27.065  1.00 16.86 ? 402  LEU A N   1 
ATOM   3072 C CA  . LEU A 1 402 ? -11.208 -11.046 26.521  1.00 17.84 ? 402  LEU A CA  1 
ATOM   3073 C C   . LEU A 1 402 ? -10.661 -9.689  26.971  1.00 18.66 ? 402  LEU A C   1 
ATOM   3074 O O   . LEU A 1 402 ? -11.398 -8.700  27.063  1.00 20.16 ? 402  LEU A O   1 
ATOM   3075 C CB  . LEU A 1 402 ? -11.134 -11.186 24.994  1.00 17.70 ? 402  LEU A CB  1 
ATOM   3076 C CG  . LEU A 1 402 ? -11.683 -12.499 24.392  1.00 17.01 ? 402  LEU A CG  1 
ATOM   3077 C CD1 . LEU A 1 402 ? -13.207 -12.469 24.363  1.00 11.18 ? 402  LEU A CD1 1 
ATOM   3078 C CD2 . LEU A 1 402 ? -11.137 -12.704 22.993  1.00 13.70 ? 402  LEU A CD2 1 
ATOM   3079 N N   . VAL A 1 403 ? -9.368  -9.638  27.262  1.00 19.09 ? 403  VAL A N   1 
ATOM   3080 C CA  . VAL A 1 403 ? -8.730  -8.404  27.734  1.00 19.02 ? 403  VAL A CA  1 
ATOM   3081 C C   . VAL A 1 403 ? -7.590  -8.075  26.785  1.00 18.67 ? 403  VAL A C   1 
ATOM   3082 O O   . VAL A 1 403 ? -6.578  -8.748  26.763  1.00 18.55 ? 403  VAL A O   1 
ATOM   3083 C CB  . VAL A 1 403 ? -8.278  -8.561  29.221  1.00 19.02 ? 403  VAL A CB  1 
ATOM   3084 C CG1 . VAL A 1 403 ? -7.448  -7.378  29.675  1.00 18.82 ? 403  VAL A CG1 1 
ATOM   3085 C CG2 . VAL A 1 403 ? -9.536  -8.751  30.104  1.00 18.95 ? 403  VAL A CG2 1 
ATOM   3086 N N   . ASN A 1 404 ? -7.807  -7.055  25.963  1.00 19.52 ? 404  ASN A N   1 
ATOM   3087 C CA  . ASN A 1 404 ? -6.957  -6.730  24.800  1.00 19.43 ? 404  ASN A CA  1 
ATOM   3088 C C   . ASN A 1 404 ? -6.613  -7.891  23.895  1.00 20.51 ? 404  ASN A C   1 
ATOM   3089 O O   . ASN A 1 404 ? -5.467  -8.034  23.477  1.00 20.90 ? 404  ASN A O   1 
ATOM   3090 C CB  . ASN A 1 404 ? -5.708  -5.988  25.229  1.00 19.82 ? 404  ASN A CB  1 
ATOM   3091 C CG  . ASN A 1 404 ? -6.040  -4.694  25.947  1.00 19.64 ? 404  ASN A CG  1 
ATOM   3092 O OD1 . ASN A 1 404 ? -6.552  -3.739  25.343  1.00 16.22 ? 404  ASN A OD1 1 
ATOM   3093 N ND2 . ASN A 1 404 ? -5.812  -4.676  27.266  1.00 21.43 ? 404  ASN A ND2 1 
ATOM   3094 N N   . ASP A 1 405 ? -7.629  -8.708  23.588  1.00 21.16 ? 405  ASP A N   1 
ATOM   3095 C CA  . ASP A 1 405 ? -7.570  -9.793  22.581  1.00 21.72 ? 405  ASP A CA  1 
ATOM   3096 C C   . ASP A 1 405 ? -7.019  -11.117 23.147  1.00 22.49 ? 405  ASP A C   1 
ATOM   3097 O O   . ASP A 1 405 ? -6.790  -12.069 22.401  1.00 23.01 ? 405  ASP A O   1 
ATOM   3098 C CB  . ASP A 1 405 ? -6.837  -9.386  21.292  1.00 20.23 ? 405  ASP A CB  1 
ATOM   3099 C CG  . ASP A 1 405 ? -7.397  -8.129  20.672  1.00 21.99 ? 405  ASP A CG  1 
ATOM   3100 O OD1 . ASP A 1 405 ? -8.558  -7.777  20.995  1.00 23.41 ? 405  ASP A OD1 1 
ATOM   3101 O OD2 . ASP A 1 405 ? -6.696  -7.482  19.836  1.00 17.82 ? 405  ASP A OD2 1 
ATOM   3102 N N   . ARG A 1 406 ? -6.798  -11.135 24.467  1.00 23.34 ? 406  ARG A N   1 
ATOM   3103 C CA  . ARG A 1 406 ? -6.401  -12.315 25.251  1.00 22.75 ? 406  ARG A CA  1 
ATOM   3104 C C   . ARG A 1 406 ? -7.601  -12.875 26.004  1.00 22.51 ? 406  ARG A C   1 
ATOM   3105 O O   . ARG A 1 406 ? -8.291  -12.158 26.748  1.00 22.05 ? 406  ARG A O   1 
ATOM   3106 C CB  . ARG A 1 406 ? -5.345  -11.913 26.261  1.00 23.16 ? 406  ARG A CB  1 
ATOM   3107 C CG  . ARG A 1 406 ? -4.827  -13.062 27.110  1.00 25.34 ? 406  ARG A CG  1 
ATOM   3108 C CD  . ARG A 1 406 ? -3.839  -12.597 28.181  1.00 28.05 ? 406  ARG A CD  1 
ATOM   3109 N NE  . ARG A 1 406 ? -3.481  -13.700 29.085  1.00 31.79 ? 406  ARG A NE  1 
ATOM   3110 C CZ  . ARG A 1 406 ? -3.916  -13.837 30.345  1.00 34.16 ? 406  ARG A CZ  1 
ATOM   3111 N NH1 . ARG A 1 406 ? -4.721  -12.932 30.891  1.00 32.67 ? 406  ARG A NH1 1 
ATOM   3112 N NH2 . ARG A 1 406 ? -3.533  -14.887 31.080  1.00 36.76 ? 406  ARG A NH2 1 
ATOM   3113 N N   . VAL A 1 407 ? -7.881  -14.164 25.797  1.00 22.24 ? 407  VAL A N   1 
ATOM   3114 C CA  . VAL A 1 407 ? -8.921  -14.814 26.584  1.00 20.44 ? 407  VAL A CA  1 
ATOM   3115 C C   . VAL A 1 407 ? -8.393  -14.926 28.012  1.00 21.15 ? 407  VAL A C   1 
ATOM   3116 O O   . VAL A 1 407 ? -7.241  -15.320 28.230  1.00 21.25 ? 407  VAL A O   1 
ATOM   3117 C CB  . VAL A 1 407 ? -9.282  -16.207 26.046  1.00 20.56 ? 407  VAL A CB  1 
ATOM   3118 C CG1 . VAL A 1 407 ? -10.427 -16.807 26.851  1.00 18.00 ? 407  VAL A CG1 1 
ATOM   3119 C CG2 . VAL A 1 407 ? -9.670  -16.144 24.543  1.00 17.00 ? 407  VAL A CG2 1 
ATOM   3120 N N   . VAL A 1 408 ? -9.217  -14.545 28.974  1.00 20.48 ? 408  VAL A N   1 
ATOM   3121 C CA  . VAL A 1 408 ? -8.819  -14.532 30.351  1.00 20.32 ? 408  VAL A CA  1 
ATOM   3122 C C   . VAL A 1 408 ? -9.814  -15.429 31.020  1.00 20.63 ? 408  VAL A C   1 
ATOM   3123 O O   . VAL A 1 408 ? -11.004 -15.125 30.976  1.00 20.78 ? 408  VAL A O   1 
ATOM   3124 C CB  . VAL A 1 408 ? -8.797  -13.084 31.009  1.00 20.36 ? 408  VAL A CB  1 
ATOM   3125 C CG1 . VAL A 1 408 ? -8.471  -13.184 32.503  1.00 20.11 ? 408  VAL A CG1 1 
ATOM   3126 C CG2 . VAL A 1 408 ? -7.792  -12.194 30.332  1.00 18.58 ? 408  VAL A CG2 1 
ATOM   3127 N N   . PRO A 1 409 ? -9.336  -16.559 31.597  1.00 20.42 ? 409  PRO A N   1 
ATOM   3128 C CA  . PRO A 1 409 ? -10.210 -17.553 32.167  1.00 20.48 ? 409  PRO A CA  1 
ATOM   3129 C C   . PRO A 1 409 ? -10.927 -17.003 33.377  1.00 21.13 ? 409  PRO A C   1 
ATOM   3130 O O   . PRO A 1 409 ? -10.279 -16.536 34.319  1.00 22.37 ? 409  PRO A O   1 
ATOM   3131 C CB  . PRO A 1 409 ? -9.250  -18.674 32.622  1.00 20.40 ? 409  PRO A CB  1 
ATOM   3132 C CG  . PRO A 1 409 ? -8.001  -18.475 31.842  1.00 21.63 ? 409  PRO A CG  1 
ATOM   3133 C CD  . PRO A 1 409 ? -7.923  -16.984 31.601  1.00 20.43 ? 409  PRO A CD  1 
ATOM   3134 N N   . LEU A 1 410 ? -12.252 -17.106 33.388  1.00 20.95 ? 410  LEU A N   1 
ATOM   3135 C CA  . LEU A 1 410 ? -13.058 -16.683 34.545  1.00 21.02 ? 410  LEU A CA  1 
ATOM   3136 C C   . LEU A 1 410 ? -12.657 -17.352 35.885  1.00 21.24 ? 410  LEU A C   1 
ATOM   3137 O O   . LEU A 1 410 ? -12.119 -18.474 35.907  1.00 20.36 ? 410  LEU A O   1 
ATOM   3138 C CB  . LEU A 1 410 ? -14.533 -16.949 34.255  1.00 21.01 ? 410  LEU A CB  1 
ATOM   3139 C CG  . LEU A 1 410 ? -15.059 -16.366 32.932  1.00 20.68 ? 410  LEU A CG  1 
ATOM   3140 C CD1 . LEU A 1 410 ? -16.564 -16.398 32.945  1.00 19.65 ? 410  LEU A CD1 1 
ATOM   3141 C CD2 . LEU A 1 410 ? -14.523 -14.961 32.662  1.00 16.80 ? 410  LEU A CD2 1 
ATOM   3142 N N   . HIS A 1 411 ? -12.900 -16.640 36.986  1.00 20.74 ? 411  HIS A N   1 
ATOM   3143 C CA  . HIS A 1 411 ? -12.627 -17.171 38.317  1.00 20.66 ? 411  HIS A CA  1 
ATOM   3144 C C   . HIS A 1 411 ? -13.940 -17.118 39.049  1.00 20.48 ? 411  HIS A C   1 
ATOM   3145 O O   . HIS A 1 411 ? -14.858 -16.348 38.659  1.00 19.54 ? 411  HIS A O   1 
ATOM   3146 C CB  . HIS A 1 411 ? -11.555 -16.354 39.065  1.00 20.73 ? 411  HIS A CB  1 
ATOM   3147 C CG  . HIS A 1 411 ? -10.138 -16.651 38.634  1.00 21.14 ? 411  HIS A CG  1 
ATOM   3148 N ND1 . HIS A 1 411 ? -9.488  -15.933 37.652  1.00 22.78 ? 411  HIS A ND1 1 
ATOM   3149 C CD2 . HIS A 1 411 ? -9.249  -17.573 39.064  1.00 21.36 ? 411  HIS A CD2 1 
ATOM   3150 C CE1 . HIS A 1 411 ? -8.267  -16.411 37.478  1.00 23.66 ? 411  HIS A CE1 1 
ATOM   3151 N NE2 . HIS A 1 411 ? -8.097  -17.405 38.325  1.00 24.33 ? 411  HIS A NE2 1 
ATOM   3152 N N   . GLY A 1 412 ? -14.042 -17.959 40.080  1.00 19.89 ? 412  GLY A N   1 
ATOM   3153 C CA  . GLY A 1 412 ? -15.199 -17.963 40.976  1.00 19.05 ? 412  GLY A CA  1 
ATOM   3154 C C   . GLY A 1 412 ? -16.324 -18.841 40.475  1.00 19.37 ? 412  GLY A C   1 
ATOM   3155 O O   . GLY A 1 412 ? -17.428 -18.869 41.051  1.00 17.59 ? 412  GLY A O   1 
ATOM   3156 N N   . CYS A 1 413 ? -16.027 -19.573 39.396  1.00 20.45 ? 413  CYS A N   1 
ATOM   3157 C CA  . CYS A 1 413 ? -16.988 -20.500 38.767  1.00 21.43 ? 413  CYS A CA  1 
ATOM   3158 C C   . CYS A 1 413 ? -16.276 -21.636 38.023  1.00 21.62 ? 413  CYS A C   1 
ATOM   3159 O O   . CYS A 1 413 ? -15.063 -21.537 37.729  1.00 22.31 ? 413  CYS A O   1 
ATOM   3160 C CB  . CYS A 1 413 ? -17.928 -19.733 37.839  1.00 21.41 ? 413  CYS A CB  1 
ATOM   3161 S SG  . CYS A 1 413 ? -17.115 -18.796 36.543  1.00 22.31 ? 413  CYS A SG  1 
ATOM   3162 N N   . PRO A 1 414 ? -17.004 -22.730 37.726  1.00 22.11 ? 414  PRO A N   1 
ATOM   3163 C CA  . PRO A 1 414 ? -16.286 -23.860 37.089  1.00 22.13 ? 414  PRO A CA  1 
ATOM   3164 C C   . PRO A 1 414 ? -15.841 -23.556 35.650  1.00 22.37 ? 414  PRO A C   1 
ATOM   3165 O O   . PRO A 1 414 ? -16.538 -23.916 34.709  1.00 23.57 ? 414  PRO A O   1 
ATOM   3166 C CB  . PRO A 1 414 ? -17.309 -25.002 37.109  1.00 20.78 ? 414  PRO A CB  1 
ATOM   3167 C CG  . PRO A 1 414 ? -18.410 -24.556 38.121  1.00 21.89 ? 414  PRO A CG  1 
ATOM   3168 C CD  . PRO A 1 414 ? -18.410 -23.057 38.062  1.00 21.61 ? 414  PRO A CD  1 
ATOM   3169 N N   . VAL A 1 415 ? -14.687 -22.933 35.464  1.00 22.92 ? 415  VAL A N   1 
ATOM   3170 C CA  . VAL A 1 415 ? -14.205 -22.708 34.090  1.00 24.05 ? 415  VAL A CA  1 
ATOM   3171 C C   . VAL A 1 415 ? -14.015 -23.977 33.347  1.00 24.47 ? 415  VAL A C   1 
ATOM   3172 O O   . VAL A 1 415 ? -13.620 -24.971 33.940  1.00 25.81 ? 415  VAL A O   1 
ATOM   3173 C CB  . VAL A 1 415 ? -12.856 -21.949 33.942  1.00 24.49 ? 415  VAL A CB  1 
ATOM   3174 C CG1 . VAL A 1 415 ? -13.114 -20.529 33.514  1.00 23.68 ? 415  VAL A CG1 1 
ATOM   3175 C CG2 . VAL A 1 415 ? -11.907 -22.071 35.168  1.00 23.88 ? 415  VAL A CG2 1 
ATOM   3176 N N   . ASP A 1 416 ? -14.317 -23.944 32.058  1.00 24.85 ? 416  ASP A N   1 
ATOM   3177 C CA  . ASP A 1 416 ? -13.954 -25.021 31.133  1.00 25.33 ? 416  ASP A CA  1 
ATOM   3178 C C   . ASP A 1 416 ? -12.593 -24.696 30.497  1.00 25.50 ? 416  ASP A C   1 
ATOM   3179 O O   . ASP A 1 416 ? -11.987 -23.699 30.868  1.00 26.21 ? 416  ASP A O   1 
ATOM   3180 C CB  . ASP A 1 416 ? -15.089 -25.271 30.125  1.00 25.22 ? 416  ASP A CB  1 
ATOM   3181 C CG  . ASP A 1 416 ? -15.336 -24.093 29.166  1.00 26.69 ? 416  ASP A CG  1 
ATOM   3182 O OD1 . ASP A 1 416 ? -14.364 -23.433 28.749  1.00 25.96 ? 416  ASP A OD1 1 
ATOM   3183 O OD2 . ASP A 1 416 ? -16.523 -23.862 28.818  1.00 26.82 ? 416  ASP A OD2 1 
ATOM   3184 N N   . ALA A 1 417 ? -12.083 -25.523 29.593  1.00 26.29 ? 417  ALA A N   1 
ATOM   3185 C CA  . ALA A 1 417 ? -10.717 -25.304 29.041  1.00 27.21 ? 417  ALA A CA  1 
ATOM   3186 C C   . ALA A 1 417 ? -10.660 -24.166 28.028  1.00 27.64 ? 417  ALA A C   1 
ATOM   3187 O O   . ALA A 1 417 ? -9.556  -23.780 27.554  1.00 28.06 ? 417  ALA A O   1 
ATOM   3188 C CB  . ALA A 1 417 ? -10.168 -26.589 28.384  1.00 27.59 ? 417  ALA A CB  1 
ATOM   3189 N N   . LEU A 1 418 ? -11.847 -23.653 27.672  1.00 27.00 ? 418  LEU A N   1 
ATOM   3190 C CA  . LEU A 1 418 ? -11.950 -22.565 26.710  1.00 26.19 ? 418  LEU A CA  1 
ATOM   3191 C C   . LEU A 1 418 ? -12.099 -21.222 27.430  1.00 25.61 ? 418  LEU A C   1 
ATOM   3192 O O   . LEU A 1 418 ? -12.281 -20.165 26.784  1.00 25.29 ? 418  LEU A O   1 
ATOM   3193 C CB  . LEU A 1 418 ? -13.058 -22.842 25.691  1.00 25.96 ? 418  LEU A CB  1 
ATOM   3194 C CG  . LEU A 1 418 ? -12.826 -24.109 24.840  1.00 26.60 ? 418  LEU A CG  1 
ATOM   3195 C CD1 . LEU A 1 418 ? -14.024 -24.422 23.989  1.00 24.80 ? 418  LEU A CD1 1 
ATOM   3196 C CD2 . LEU A 1 418 ? -11.544 -24.042 23.973  1.00 25.44 ? 418  LEU A CD2 1 
ATOM   3197 N N   . GLY A 1 419 ? -11.966 -21.271 28.760  1.00 24.03 ? 419  GLY A N   1 
ATOM   3198 C CA  . GLY A 1 419 ? -12.012 -20.075 29.592  1.00 23.35 ? 419  GLY A CA  1 
ATOM   3199 C C   . GLY A 1 419 ? -13.391 -19.620 30.044  1.00 22.99 ? 419  GLY A C   1 
ATOM   3200 O O   . GLY A 1 419 ? -13.501 -18.570 30.665  1.00 22.25 ? 419  GLY A O   1 
ATOM   3201 N N   . ARG A 1 420 ? -14.429 -20.407 29.758  1.00 22.47 ? 420  ARG A N   1 
ATOM   3202 C CA  . ARG A 1 420 ? -15.815 -19.947 29.903  1.00 23.31 ? 420  ARG A CA  1 
ATOM   3203 C C   . ARG A 1 420 ? -16.520 -20.494 31.124  1.00 23.26 ? 420  ARG A C   1 
ATOM   3204 O O   . ARG A 1 420 ? -16.248 -21.593 31.589  1.00 24.96 ? 420  ARG A O   1 
ATOM   3205 C CB  . ARG A 1 420 ? -16.674 -20.340 28.675  1.00 23.28 ? 420  ARG A CB  1 
ATOM   3206 C CG  . ARG A 1 420 ? -16.050 -20.100 27.288  1.00 23.74 ? 420  ARG A CG  1 
ATOM   3207 C CD  . ARG A 1 420 ? -16.882 -20.788 26.150  1.00 24.71 ? 420  ARG A CD  1 
ATOM   3208 N NE  . ARG A 1 420 ? -16.918 -22.258 26.254  1.00 24.38 ? 420  ARG A NE  1 
ATOM   3209 C CZ  . ARG A 1 420 ? -17.160 -23.094 25.235  1.00 25.51 ? 420  ARG A CZ  1 
ATOM   3210 N NH1 . ARG A 1 420 ? -17.395 -22.616 24.004  1.00 25.64 ? 420  ARG A NH1 1 
ATOM   3211 N NH2 . ARG A 1 420 ? -17.172 -24.411 25.443  1.00 20.13 ? 420  ARG A NH2 1 
ATOM   3212 N N   . CYS A 1 421 ? -17.475 -19.763 31.633  1.00 23.37 ? 421  CYS A N   1 
ATOM   3213 C CA  . CYS A 1 421 ? -18.380 -20.371 32.617  1.00 24.00 ? 421  CYS A CA  1 
ATOM   3214 C C   . CYS A 1 421 ? -19.776 -20.245 32.126  1.00 23.33 ? 421  CYS A C   1 
ATOM   3215 O O   . CYS A 1 421 ? -20.078 -19.338 31.351  1.00 23.97 ? 421  CYS A O   1 
ATOM   3216 C CB  . CYS A 1 421 ? -18.312 -19.657 33.953  1.00 23.76 ? 421  CYS A CB  1 
ATOM   3217 S SG  . CYS A 1 421 ? -16.905 -20.101 34.972  1.00 27.56 ? 421  CYS A SG  1 
ATOM   3218 N N   . THR A 1 422 ? -20.662 -21.099 32.614  1.00 23.27 ? 422  THR A N   1 
ATOM   3219 C CA  . THR A 1 422 ? -22.076 -20.876 32.359  1.00 22.85 ? 422  THR A CA  1 
ATOM   3220 C C   . THR A 1 422 ? -22.472 -19.560 33.009  1.00 23.37 ? 422  THR A C   1 
ATOM   3221 O O   . THR A 1 422 ? -21.952 -19.212 34.060  1.00 24.29 ? 422  THR A O   1 
ATOM   3222 C CB  . THR A 1 422 ? -22.952 -21.983 32.917  1.00 22.77 ? 422  THR A CB  1 
ATOM   3223 O OG1 . THR A 1 422 ? -23.026 -21.849 34.327  1.00 22.22 ? 422  THR A OG1 1 
ATOM   3224 C CG2 . THR A 1 422 ? -22.442 -23.399 32.521  1.00 21.22 ? 422  THR A CG2 1 
ATOM   3225 N N   . ARG A 1 423 ? -23.408 -18.843 32.402  1.00 23.81 ? 423  ARG A N   1 
ATOM   3226 C CA  . ARG A 1 423 ? -23.843 -17.545 32.905  1.00 24.13 ? 423  ARG A CA  1 
ATOM   3227 C C   . ARG A 1 423 ? -24.305 -17.591 34.333  1.00 24.38 ? 423  ARG A C   1 
ATOM   3228 O O   . ARG A 1 423 ? -23.928 -16.710 35.117  1.00 24.30 ? 423  ARG A O   1 
ATOM   3229 C CB  . ARG A 1 423 ? -24.920 -16.933 32.013  1.00 23.76 ? 423  ARG A CB  1 
ATOM   3230 C CG  . ARG A 1 423 ? -25.334 -15.520 32.350  1.00 25.23 ? 423  ARG A CG  1 
ATOM   3231 C CD  . ARG A 1 423 ? -26.661 -15.468 33.138  1.00 27.92 ? 423  ARG A CD  1 
ATOM   3232 N NE  . ARG A 1 423 ? -27.686 -16.399 32.667  1.00 27.57 ? 423  ARG A NE  1 
ATOM   3233 C CZ  . ARG A 1 423 ? -28.600 -16.131 31.722  1.00 30.15 ? 423  ARG A CZ  1 
ATOM   3234 N NH1 . ARG A 1 423 ? -28.627 -14.947 31.084  1.00 29.88 ? 423  ARG A NH1 1 
ATOM   3235 N NH2 . ARG A 1 423 ? -29.497 -17.068 31.394  1.00 26.94 ? 423  ARG A NH2 1 
ATOM   3236 N N   . ASP A 1 424 ? -25.102 -18.602 34.684  1.00 25.17 ? 424  ASP A N   1 
ATOM   3237 C CA  . ASP A 1 424 ? -25.703 -18.658 36.048  1.00 25.80 ? 424  ASP A CA  1 
ATOM   3238 C C   . ASP A 1 424 ? -24.633 -18.785 37.116  1.00 25.23 ? 424  ASP A C   1 
ATOM   3239 O O   . ASP A 1 424 ? -24.738 -18.163 38.189  1.00 25.08 ? 424  ASP A O   1 
ATOM   3240 C CB  . ASP A 1 424 ? -26.732 -19.797 36.205  1.00 26.61 ? 424  ASP A CB  1 
ATOM   3241 C CG  . ASP A 1 424 ? -28.128 -19.417 35.706  1.00 30.30 ? 424  ASP A CG  1 
ATOM   3242 O OD1 . ASP A 1 424 ? -28.422 -18.205 35.460  1.00 35.03 ? 424  ASP A OD1 1 
ATOM   3243 O OD2 . ASP A 1 424 ? -28.958 -20.341 35.547  1.00 34.71 ? 424  ASP A OD2 1 
ATOM   3244 N N   . SER A 1 425 ? -23.592 -19.557 36.796  1.00 24.12 ? 425  SER A N   1 
ATOM   3245 C CA  . SER A 1 425 ? -22.518 -19.816 37.737  1.00 23.72 ? 425  SER A CA  1 
ATOM   3246 C C   . SER A 1 425 ? -21.513 -18.640 37.765  1.00 23.27 ? 425  SER A C   1 
ATOM   3247 O O   . SER A 1 425 ? -20.950 -18.303 38.807  1.00 23.82 ? 425  SER A O   1 
ATOM   3248 C CB  . SER A 1 425 ? -21.835 -21.147 37.423  1.00 22.85 ? 425  SER A CB  1 
ATOM   3249 O OG  . SER A 1 425 ? -20.949 -20.973 36.337  1.00 24.17 ? 425  SER A OG  1 
ATOM   3250 N N   . PHE A 1 426 ? -21.287 -18.007 36.628  1.00 22.73 ? 426  PHE A N   1 
ATOM   3251 C CA  . PHE A 1 426 ? -20.545 -16.748 36.617  1.00 21.85 ? 426  PHE A CA  1 
ATOM   3252 C C   . PHE A 1 426 ? -21.184 -15.691 37.524  1.00 22.04 ? 426  PHE A C   1 
ATOM   3253 O O   . PHE A 1 426 ? -20.482 -15.029 38.311  1.00 21.79 ? 426  PHE A O   1 
ATOM   3254 C CB  . PHE A 1 426 ? -20.404 -16.207 35.203  1.00 20.72 ? 426  PHE A CB  1 
ATOM   3255 C CG  . PHE A 1 426 ? -19.586 -14.984 35.126  1.00 19.79 ? 426  PHE A CG  1 
ATOM   3256 C CD1 . PHE A 1 426 ? -18.234 -15.018 35.474  1.00 21.07 ? 426  PHE A CD1 1 
ATOM   3257 C CD2 . PHE A 1 426 ? -20.163 -13.775 34.741  1.00 19.65 ? 426  PHE A CD2 1 
ATOM   3258 C CE1 . PHE A 1 426 ? -17.453 -13.875 35.415  1.00 22.47 ? 426  PHE A CE1 1 
ATOM   3259 C CE2 . PHE A 1 426 ? -19.380 -12.595 34.681  1.00 20.22 ? 426  PHE A CE2 1 
ATOM   3260 C CZ  . PHE A 1 426 ? -18.043 -12.639 35.002  1.00 21.10 ? 426  PHE A CZ  1 
ATOM   3261 N N   . VAL A 1 427 ? -22.500 -15.526 37.413  1.00 22.15 ? 427  VAL A N   1 
ATOM   3262 C CA  . VAL A 1 427 ? -23.186 -14.491 38.201  1.00 22.51 ? 427  VAL A CA  1 
ATOM   3263 C C   . VAL A 1 427 ? -23.062 -14.827 39.677  1.00 22.84 ? 427  VAL A C   1 
ATOM   3264 O O   . VAL A 1 427 ? -22.601 -14.015 40.501  1.00 23.66 ? 427  VAL A O   1 
ATOM   3265 C CB  . VAL A 1 427 ? -24.644 -14.294 37.740  1.00 22.44 ? 427  VAL A CB  1 
ATOM   3266 C CG1 . VAL A 1 427 ? -25.481 -13.566 38.797  1.00 22.20 ? 427  VAL A CG1 1 
ATOM   3267 C CG2 . VAL A 1 427 ? -24.666 -13.523 36.411  1.00 21.49 ? 427  VAL A CG2 1 
ATOM   3268 N N   . ARG A 1 428 ? -23.408 -16.059 40.002  1.00 23.81 ? 428  ARG A N   1 
ATOM   3269 C CA  . ARG A 1 428 ? -23.245 -16.590 41.352  1.00 24.27 ? 428  ARG A CA  1 
ATOM   3270 C C   . ARG A 1 428 ? -21.838 -16.358 41.919  1.00 23.70 ? 428  ARG A C   1 
ATOM   3271 O O   . ARG A 1 428 ? -21.720 -16.091 43.103  1.00 23.71 ? 428  ARG A O   1 
ATOM   3272 C CB  . ARG A 1 428 ? -23.620 -18.066 41.370  1.00 24.71 ? 428  ARG A CB  1 
ATOM   3273 C CG  . ARG A 1 428 ? -23.394 -18.820 42.685  1.00 29.78 ? 428  ARG A CG  1 
ATOM   3274 C CD  . ARG A 1 428 ? -22.839 -20.210 42.375  1.00 37.01 ? 428  ARG A CD  1 
ATOM   3275 N NE  . ARG A 1 428 ? -23.237 -21.194 43.379  1.00 44.77 ? 428  ARG A NE  1 
ATOM   3276 C CZ  . ARG A 1 428 ? -23.697 -22.419 43.093  1.00 48.47 ? 428  ARG A CZ  1 
ATOM   3277 N NH1 . ARG A 1 428 ? -23.837 -22.804 41.818  1.00 48.87 ? 428  ARG A NH1 1 
ATOM   3278 N NH2 . ARG A 1 428 ? -24.049 -23.250 44.084  1.00 48.37 ? 428  ARG A NH2 1 
ATOM   3279 N N   . GLY A 1 429 ? -20.784 -16.442 41.086  1.00 23.28 ? 429  GLY A N   1 
ATOM   3280 C CA  . GLY A 1 429 ? -19.405 -16.215 41.561  1.00 21.90 ? 429  GLY A CA  1 
ATOM   3281 C C   . GLY A 1 429 ? -19.117 -14.753 41.960  1.00 21.68 ? 429  GLY A C   1 
ATOM   3282 O O   . GLY A 1 429 ? -18.153 -14.446 42.710  1.00 22.51 ? 429  GLY A O   1 
ATOM   3283 N N   . LEU A 1 430 ? -19.952 -13.838 41.488  1.00 19.71 ? 430  LEU A N   1 
ATOM   3284 C CA  . LEU A 1 430 ? -19.712 -12.414 41.730  1.00 18.19 ? 430  LEU A CA  1 
ATOM   3285 C C   . LEU A 1 430 ? -20.468 -11.913 42.948  1.00 18.03 ? 430  LEU A C   1 
ATOM   3286 O O   . LEU A 1 430 ? -21.039 -10.783 42.949  1.00 17.74 ? 430  LEU A O   1 
ATOM   3287 C CB  . LEU A 1 430 ? -20.043 -11.585 40.479  1.00 17.54 ? 430  LEU A CB  1 
ATOM   3288 C CG  . LEU A 1 430 ? -19.364 -11.858 39.121  1.00 14.85 ? 430  LEU A CG  1 
ATOM   3289 C CD1 . LEU A 1 430 ? -20.047 -10.973 38.088  1.00 14.70 ? 430  LEU A CD1 1 
ATOM   3290 C CD2 . LEU A 1 430 ? -17.829 -11.620 39.127  1.00 9.64  ? 430  LEU A CD2 1 
ATOM   3291 N N   . SER A 1 431 ? -20.470 -12.771 43.979  1.00 18.01 ? 431  SER A N   1 
ATOM   3292 C CA  . SER A 1 431 ? -21.051 -12.473 45.291  1.00 18.36 ? 431  SER A CA  1 
ATOM   3293 C C   . SER A 1 431 ? -20.402 -11.266 45.932  1.00 18.53 ? 431  SER A C   1 
ATOM   3294 O O   . SER A 1 431 ? -21.076 -10.515 46.640  1.00 18.57 ? 431  SER A O   1 
ATOM   3295 C CB  . SER A 1 431 ? -20.884 -13.667 46.229  1.00 18.74 ? 431  SER A CB  1 
ATOM   3296 O OG  . SER A 1 431 ? -19.634 -14.273 46.007  1.00 17.82 ? 431  SER A OG  1 
ATOM   3297 N N   . PHE A 1 432 ? -19.100 -11.066 45.682  1.00 18.78 ? 432  PHE A N   1 
ATOM   3298 C CA  . PHE A 1 432 ? -18.441 -9.871  46.184  1.00 19.05 ? 432  PHE A CA  1 
ATOM   3299 C C   . PHE A 1 432 ? -19.224 -8.659  45.683  1.00 19.80 ? 432  PHE A C   1 
ATOM   3300 O O   . PHE A 1 432 ? -19.795 -7.935  46.485  1.00 20.15 ? 432  PHE A O   1 
ATOM   3301 C CB  . PHE A 1 432 ? -16.964 -9.831  45.802  1.00 19.62 ? 432  PHE A CB  1 
ATOM   3302 C CG  . PHE A 1 432 ? -16.255 -8.520  46.178  1.00 20.18 ? 432  PHE A CG  1 
ATOM   3303 C CD1 . PHE A 1 432 ? -15.831 -8.282  47.490  1.00 18.92 ? 432  PHE A CD1 1 
ATOM   3304 C CD2 . PHE A 1 432 ? -16.019 -7.550  45.215  1.00 19.69 ? 432  PHE A CD2 1 
ATOM   3305 C CE1 . PHE A 1 432 ? -15.218 -7.124  47.822  1.00 18.45 ? 432  PHE A CE1 1 
ATOM   3306 C CE2 . PHE A 1 432 ? -15.386 -6.371  45.542  1.00 20.79 ? 432  PHE A CE2 1 
ATOM   3307 C CZ  . PHE A 1 432 ? -15.013 -6.133  46.856  1.00 20.03 ? 432  PHE A CZ  1 
ATOM   3308 N N   . ALA A 1 433 ? -19.334 -8.473  44.365  1.00 19.64 ? 433  ALA A N   1 
ATOM   3309 C CA  . ALA A 1 433 ? -20.084 -7.310  43.842  1.00 19.02 ? 433  ALA A CA  1 
ATOM   3310 C C   . ALA A 1 433 ? -21.573 -7.352  44.230  1.00 19.45 ? 433  ALA A C   1 
ATOM   3311 O O   . ALA A 1 433 ? -22.224 -6.309  44.484  1.00 17.51 ? 433  ALA A O   1 
ATOM   3312 C CB  . ALA A 1 433 ? -19.898 -7.191  42.338  1.00 17.86 ? 433  ALA A CB  1 
ATOM   3313 N N   . ARG A 1 434 ? -22.101 -8.572  44.309  1.00 20.81 ? 434  ARG A N   1 
ATOM   3314 C CA  . ARG A 1 434 ? -23.554 -8.726  44.510  1.00 22.39 ? 434  ARG A CA  1 
ATOM   3315 C C   . ARG A 1 434 ? -23.950 -8.279  45.904  1.00 22.57 ? 434  ARG A C   1 
ATOM   3316 O O   . ARG A 1 434 ? -25.090 -7.821  46.112  1.00 22.87 ? 434  ARG A O   1 
ATOM   3317 C CB  . ARG A 1 434 ? -24.081 -10.156 44.215  1.00 21.82 ? 434  ARG A CB  1 
ATOM   3318 C CG  . ARG A 1 434 ? -24.533 -10.394 42.777  1.00 24.26 ? 434  ARG A CG  1 
ATOM   3319 C CD  . ARG A 1 434 ? -25.230 -11.815 42.478  1.00 25.48 ? 434  ARG A CD  1 
ATOM   3320 N NE  . ARG A 1 434 ? -24.486 -12.989 42.972  1.00 29.00 ? 434  ARG A NE  1 
ATOM   3321 C CZ  . ARG A 1 434 ? -24.748 -13.594 44.133  1.00 28.11 ? 434  ARG A CZ  1 
ATOM   3322 N NH1 . ARG A 1 434 ? -25.733 -13.134 44.898  1.00 28.46 ? 434  ARG A NH1 1 
ATOM   3323 N NH2 . ARG A 1 434 ? -24.034 -14.643 44.539  1.00 25.96 ? 434  ARG A NH2 1 
ATOM   3324 N N   . SER A 1 435 ? -23.013 -8.402  46.848  1.00 22.96 ? 435  SER A N   1 
ATOM   3325 C CA  . SER A 1 435 ? -23.255 -8.025  48.254  1.00 23.08 ? 435  SER A CA  1 
ATOM   3326 C C   . SER A 1 435 ? -22.970 -6.543  48.493  1.00 23.01 ? 435  SER A C   1 
ATOM   3327 O O   . SER A 1 435 ? -23.282 -5.997  49.548  1.00 23.60 ? 435  SER A O   1 
ATOM   3328 C CB  . SER A 1 435 ? -22.494 -8.946  49.237  1.00 23.13 ? 435  SER A CB  1 
ATOM   3329 O OG  . SER A 1 435 ? -21.103 -9.121  48.889  1.00 23.96 ? 435  SER A OG  1 
ATOM   3330 N N   . GLY A 1 436 ? -22.440 -5.874  47.484  1.00 22.66 ? 436  GLY A N   1 
ATOM   3331 C CA  . GLY A 1 436 ? -22.037 -4.476  47.636  1.00 22.73 ? 436  GLY A CA  1 
ATOM   3332 C C   . GLY A 1 436 ? -20.540 -4.284  47.922  1.00 22.28 ? 436  GLY A C   1 
ATOM   3333 O O   . GLY A 1 436 ? -20.102 -3.178  48.233  1.00 21.70 ? 436  GLY A O   1 
ATOM   3334 N N   . GLY A 1 437 ? -19.758 -5.359  47.821  1.00 22.06 ? 437  GLY A N   1 
ATOM   3335 C CA  . GLY A 1 437 ? -18.328 -5.342  48.169  1.00 22.89 ? 437  GLY A CA  1 
ATOM   3336 C C   . GLY A 1 437 ? -18.069 -4.686  49.524  1.00 23.10 ? 437  GLY A C   1 
ATOM   3337 O O   . GLY A 1 437 ? -18.793 -4.951  50.484  1.00 24.41 ? 437  GLY A O   1 
ATOM   3338 N N   . ASP A 1 438 ? -17.070 -3.806  49.605  1.00 22.57 ? 438  ASP A N   1 
ATOM   3339 C CA  . ASP A 1 438 ? -16.792 -3.082  50.845  1.00 22.74 ? 438  ASP A CA  1 
ATOM   3340 C C   . ASP A 1 438 ? -17.253 -1.647  50.764  1.00 23.34 ? 438  ASP A C   1 
ATOM   3341 O O   . ASP A 1 438 ? -16.652 -0.763  51.380  1.00 23.76 ? 438  ASP A O   1 
ATOM   3342 C CB  . ASP A 1 438 ? -15.311 -3.153  51.229  1.00 21.39 ? 438  ASP A CB  1 
ATOM   3343 C CG  . ASP A 1 438 ? -14.811 -4.571  51.272  1.00 21.72 ? 438  ASP A CG  1 
ATOM   3344 O OD1 . ASP A 1 438 ? -15.491 -5.427  51.869  1.00 23.18 ? 438  ASP A OD1 1 
ATOM   3345 O OD2 . ASP A 1 438 ? -13.749 -4.860  50.698  1.00 21.47 ? 438  ASP A OD2 1 
ATOM   3346 N N   . TRP A 1 439 ? -18.331 -1.400  50.031  1.00 23.67 ? 439  TRP A N   1 
ATOM   3347 C CA  . TRP A 1 439 ? -18.743 -0.032  49.824  1.00 23.69 ? 439  TRP A CA  1 
ATOM   3348 C C   . TRP A 1 439 ? -19.076 0.638   51.177  1.00 25.03 ? 439  TRP A C   1 
ATOM   3349 O O   . TRP A 1 439 ? -18.850 1.856   51.345  1.00 24.39 ? 439  TRP A O   1 
ATOM   3350 C CB  . TRP A 1 439 ? -19.893 0.053   48.817  1.00 22.22 ? 439  TRP A CB  1 
ATOM   3351 C CG  . TRP A 1 439 ? -20.200 1.445   48.421  1.00 20.60 ? 439  TRP A CG  1 
ATOM   3352 C CD1 . TRP A 1 439 ? -21.147 2.277   48.979  1.00 18.39 ? 439  TRP A CD1 1 
ATOM   3353 C CD2 . TRP A 1 439 ? -19.523 2.221   47.417  1.00 19.27 ? 439  TRP A CD2 1 
ATOM   3354 N NE1 . TRP A 1 439 ? -21.109 3.505   48.366  1.00 19.70 ? 439  TRP A NE1 1 
ATOM   3355 C CE2 . TRP A 1 439 ? -20.120 3.500   47.408  1.00 18.40 ? 439  TRP A CE2 1 
ATOM   3356 C CE3 . TRP A 1 439 ? -18.484 1.950   46.505  1.00 18.44 ? 439  TRP A CE3 1 
ATOM   3357 C CZ2 . TRP A 1 439 ? -19.725 4.490   46.529  1.00 18.47 ? 439  TRP A CZ2 1 
ATOM   3358 C CZ3 . TRP A 1 439 ? -18.091 2.951   45.611  1.00 17.95 ? 439  TRP A CZ3 1 
ATOM   3359 C CH2 . TRP A 1 439 ? -18.711 4.204   45.632  1.00 18.57 ? 439  TRP A CH2 1 
ATOM   3360 N N   . ALA A 1 440 ? -19.587 -0.151  52.142  1.00 26.75 ? 440  ALA A N   1 
ATOM   3361 C CA  . ALA A 1 440 ? -19.927 0.391   53.489  1.00 28.46 ? 440  ALA A CA  1 
ATOM   3362 C C   . ALA A 1 440 ? -18.725 1.044   54.207  1.00 29.57 ? 440  ALA A C   1 
ATOM   3363 O O   . ALA A 1 440 ? -18.890 1.893   55.071  1.00 29.87 ? 440  ALA A O   1 
ATOM   3364 C CB  . ALA A 1 440 ? -20.574 -0.693  54.381  1.00 27.94 ? 440  ALA A CB  1 
ATOM   3365 N N   . GLU A 1 441 ? -17.517 0.643   53.818  1.00 31.28 ? 441  GLU A N   1 
ATOM   3366 C CA  . GLU A 1 441 ? -16.299 1.144   54.415  1.00 32.90 ? 441  GLU A CA  1 
ATOM   3367 C C   . GLU A 1 441 ? -15.848 2.465   53.823  1.00 33.20 ? 441  GLU A C   1 
ATOM   3368 O O   . GLU A 1 441 ? -14.807 2.987   54.203  1.00 33.42 ? 441  GLU A O   1 
ATOM   3369 C CB  . GLU A 1 441 ? -15.211 0.084   54.307  1.00 33.64 ? 441  GLU A CB  1 
ATOM   3370 C CG  . GLU A 1 441 ? -15.619 -1.204  55.036  1.00 37.35 ? 441  GLU A CG  1 
ATOM   3371 C CD  . GLU A 1 441 ? -14.482 -2.214  55.195  1.00 42.48 ? 441  GLU A CD  1 
ATOM   3372 O OE1 . GLU A 1 441 ? -13.305 -1.837  54.990  1.00 43.93 ? 441  GLU A OE1 1 
ATOM   3373 O OE2 . GLU A 1 441 ? -14.781 -3.387  55.551  1.00 43.73 ? 441  GLU A OE2 1 
ATOM   3374 N N   . CYS A 1 442 ? -16.642 3.021   52.910  1.00 33.78 ? 442  CYS A N   1 
ATOM   3375 C CA  . CYS A 1 442 ? -16.284 4.262   52.227  1.00 33.87 ? 442  CYS A CA  1 
ATOM   3376 C C   . CYS A 1 442 ? -16.433 5.437   53.174  1.00 35.68 ? 442  CYS A C   1 
ATOM   3377 O O   . CYS A 1 442 ? -15.924 6.531   52.913  1.00 35.40 ? 442  CYS A O   1 
ATOM   3378 C CB  . CYS A 1 442 ? -17.143 4.475   50.974  1.00 33.25 ? 442  CYS A CB  1 
ATOM   3379 S SG  . CYS A 1 442 ? -16.781 3.410   49.506  1.00 30.08 ? 442  CYS A SG  1 
ATOM   3380 N N   . PHE A 1 443 ? -17.117 5.198   54.292  1.00 38.00 ? 443  PHE A N   1 
ATOM   3381 C CA  . PHE A 1 443 ? -17.596 6.283   55.161  1.00 40.40 ? 443  PHE A CA  1 
ATOM   3382 C C   . PHE A 1 443 ? -17.131 6.217   56.626  1.00 41.97 ? 443  PHE A C   1 
ATOM   3383 O O   . PHE A 1 443 ? -16.777 7.237   57.201  1.00 42.48 ? 443  PHE A O   1 
ATOM   3384 C CB  . PHE A 1 443 ? -19.117 6.403   55.011  1.00 40.42 ? 443  PHE A CB  1 
ATOM   3385 C CG  . PHE A 1 443 ? -19.546 6.498   53.583  1.00 40.02 ? 443  PHE A CG  1 
ATOM   3386 C CD1 . PHE A 1 443 ? -19.313 7.666   52.862  1.00 39.53 ? 443  PHE A CD1 1 
ATOM   3387 C CD2 . PHE A 1 443 ? -20.093 5.394   52.928  1.00 40.73 ? 443  PHE A CD2 1 
ATOM   3388 C CE1 . PHE A 1 443 ? -19.655 7.765   51.532  1.00 39.10 ? 443  PHE A CE1 1 
ATOM   3389 C CE2 . PHE A 1 443 ? -20.463 5.485   51.578  1.00 41.45 ? 443  PHE A CE2 1 
ATOM   3390 C CZ  . PHE A 1 443 ? -20.239 6.684   50.884  1.00 41.17 ? 443  PHE A CZ  1 
ATOM   3391 N N   . ALA A 1 444 ? -17.118 5.025   57.215  1.00 44.15 ? 444  ALA A N   1 
ATOM   3392 C CA  . ALA A 1 444 ? -16.440 4.800   58.508  1.00 46.25 ? 444  ALA A CA  1 
ATOM   3393 C C   . ALA A 1 444 ? -14.928 4.440   58.353  1.00 47.24 ? 444  ALA A C   1 
ATOM   3394 O O   . ALA A 1 444 ? -14.038 5.322   58.420  1.00 47.76 ? 444  ALA A O   1 
ATOM   3395 C CB  . ALA A 1 444 ? -17.196 3.709   59.349  1.00 46.78 ? 444  ALA A CB  1 
ATOM   3396 O OXT . ALA A 1 444 ? -14.553 3.260   58.166  1.00 47.38 ? 444  ALA A OXT 1 
ATOM   3397 N N   . SER B 1 7   ? 1.683   -19.579 -1.389  1.00 43.03 ? 7    SER B N   1 
ATOM   3398 C CA  . SER B 1 7   ? 1.339   -18.124 -1.606  1.00 43.23 ? 7    SER B CA  1 
ATOM   3399 C C   . SER B 1 7   ? 1.953   -17.140 -0.577  1.00 42.92 ? 7    SER B C   1 
ATOM   3400 O O   . SER B 1 7   ? 1.771   -15.910 -0.716  1.00 43.13 ? 7    SER B O   1 
ATOM   3401 C CB  . SER B 1 7   ? -0.179  -17.919 -1.666  1.00 43.93 ? 7    SER B CB  1 
ATOM   3402 O OG  . SER B 1 7   ? -0.797  -18.706 -2.698  1.00 45.77 ? 7    SER B OG  1 
ATOM   3403 N N   . CYS B 1 8   ? 2.616   -17.690 0.462   1.00 41.76 ? 8    CYS B N   1 
ATOM   3404 C CA  . CYS B 1 8   ? 3.620   -16.976 1.313   1.00 40.63 ? 8    CYS B CA  1 
ATOM   3405 C C   . CYS B 1 8   ? 5.023   -17.519 0.922   1.00 39.46 ? 8    CYS B C   1 
ATOM   3406 O O   . CYS B 1 8   ? 6.067   -17.084 1.409   1.00 39.31 ? 8    CYS B O   1 
ATOM   3407 C CB  . CYS B 1 8   ? 3.341   -17.145 2.828   1.00 40.10 ? 8    CYS B CB  1 
ATOM   3408 S SG  . CYS B 1 8   ? 2.958   -18.885 3.382   1.00 41.29 ? 8    CYS B SG  1 
ATOM   3409 N N   . ASP B 1 9   ? 5.005   -18.467 0.002   1.00 37.78 ? 9    ASP B N   1 
ATOM   3410 C CA  . ASP B 1 9   ? 6.189   -19.010 -0.596  1.00 36.83 ? 9    ASP B CA  1 
ATOM   3411 C C   . ASP B 1 9   ? 6.176   -18.758 -2.109  1.00 36.29 ? 9    ASP B C   1 
ATOM   3412 O O   . ASP B 1 9   ? 5.562   -19.530 -2.875  1.00 36.93 ? 9    ASP B O   1 
ATOM   3413 C CB  . ASP B 1 9   ? 6.241   -20.514 -0.342  1.00 36.58 ? 9    ASP B CB  1 
ATOM   3414 C CG  . ASP B 1 9   ? 7.576   -21.127 -0.725  1.00 36.49 ? 9    ASP B CG  1 
ATOM   3415 O OD1 . ASP B 1 9   ? 8.600   -20.417 -0.778  1.00 37.34 ? 9    ASP B OD1 1 
ATOM   3416 O OD2 . ASP B 1 9   ? 7.608   -22.335 -0.962  1.00 37.14 ? 9    ASP B OD2 1 
ATOM   3417 N N   . THR B 1 10  ? 6.877   -17.706 -2.533  1.00 34.41 ? 10   THR B N   1 
ATOM   3418 C CA  . THR B 1 10  ? 6.887   -17.262 -3.924  1.00 33.12 ? 10   THR B CA  1 
ATOM   3419 C C   . THR B 1 10  ? 8.277   -17.345 -4.555  1.00 32.76 ? 10   THR B C   1 
ATOM   3420 O O   . THR B 1 10  ? 9.306   -17.515 -3.866  1.00 32.09 ? 10   THR B O   1 
ATOM   3421 C CB  . THR B 1 10  ? 6.419   -15.807 -4.037  1.00 32.99 ? 10   THR B CB  1 
ATOM   3422 O OG1 . THR B 1 10  ? 7.235   -14.967 -3.205  1.00 33.40 ? 10   THR B OG1 1 
ATOM   3423 C CG2 . THR B 1 10  ? 4.947   -15.662 -3.601  1.00 32.63 ? 10   THR B CG2 1 
ATOM   3424 N N   . VAL B 1 11  ? 8.306   -17.213 -5.872  1.00 32.06 ? 11   VAL B N   1 
ATOM   3425 C CA  . VAL B 1 11  ? 9.571   -17.225 -6.599  1.00 32.23 ? 11   VAL B CA  1 
ATOM   3426 C C   . VAL B 1 11  ? 10.378  -15.998 -6.217  1.00 31.78 ? 11   VAL B C   1 
ATOM   3427 O O   . VAL B 1 11  ? 11.600  -16.042 -6.103  1.00 31.09 ? 11   VAL B O   1 
ATOM   3428 C CB  . VAL B 1 11  ? 9.356   -17.266 -8.151  1.00 32.36 ? 11   VAL B CB  1 
ATOM   3429 C CG1 . VAL B 1 11  ? 10.640  -16.928 -8.896  1.00 31.69 ? 11   VAL B CG1 1 
ATOM   3430 C CG2 . VAL B 1 11  ? 8.810   -18.634 -8.588  1.00 32.36 ? 11   VAL B CG2 1 
ATOM   3431 N N   . ASP B 1 12  ? 9.679   -14.895 -5.998  1.00 32.12 ? 12   ASP B N   1 
ATOM   3432 C CA  . ASP B 1 12  ? 10.393  -13.654 -5.854  1.00 32.23 ? 12   ASP B CA  1 
ATOM   3433 C C   . ASP B 1 12  ? 10.836  -13.370 -4.423  1.00 31.37 ? 12   ASP B C   1 
ATOM   3434 O O   . ASP B 1 12  ? 11.956  -12.902 -4.202  1.00 30.70 ? 12   ASP B O   1 
ATOM   3435 C CB  . ASP B 1 12  ? 9.591   -12.499 -6.428  1.00 33.11 ? 12   ASP B CB  1 
ATOM   3436 C CG  . ASP B 1 12  ? 10.431  -11.651 -7.361  1.00 36.40 ? 12   ASP B CG  1 
ATOM   3437 O OD1 . ASP B 1 12  ? 11.192  -10.755 -6.858  1.00 33.03 ? 12   ASP B OD1 1 
ATOM   3438 O OD2 . ASP B 1 12  ? 10.323  -11.924 -8.595  1.00 39.81 ? 12   ASP B OD2 1 
ATOM   3439 N N   . GLN B 1 13  ? 9.962   -13.649 -3.462  1.00 30.12 ? 13   GLN B N   1 
ATOM   3440 C CA  . GLN B 1 13  ? 10.255  -13.282 -2.098  1.00 29.49 ? 13   GLN B CA  1 
ATOM   3441 C C   . GLN B 1 13  ? 10.749  -14.455 -1.274  1.00 28.99 ? 13   GLN B C   1 
ATOM   3442 O O   . GLN B 1 13  ? 11.240  -14.251 -0.177  1.00 28.71 ? 13   GLN B O   1 
ATOM   3443 C CB  . GLN B 1 13  ? 9.070   -12.568 -1.450  1.00 29.72 ? 13   GLN B CB  1 
ATOM   3444 C CG  . GLN B 1 13  ? 8.888   -11.127 -1.923  1.00 31.48 ? 13   GLN B CG  1 
ATOM   3445 C CD  . GLN B 1 13  ? 9.986   -10.182 -1.425  1.00 35.53 ? 13   GLN B CD  1 
ATOM   3446 O OE1 . GLN B 1 13  ? 10.054  -9.849  -0.229  1.00 37.79 ? 13   GLN B OE1 1 
ATOM   3447 N NE2 . GLN B 1 13  ? 10.833  -9.723  -2.345  1.00 35.45 ? 13   GLN B NE2 1 
ATOM   3448 N N   . GLY B 1 14  ? 10.662  -15.674 -1.827  1.00 28.41 ? 14   GLY B N   1 
ATOM   3449 C CA  . GLY B 1 14  ? 11.161  -16.873 -1.167  1.00 27.85 ? 14   GLY B CA  1 
ATOM   3450 C C   . GLY B 1 14  ? 10.195  -17.358 -0.091  1.00 28.26 ? 14   GLY B C   1 
ATOM   3451 O O   . GLY B 1 14  ? 8.986   -17.241 -0.240  1.00 28.12 ? 14   GLY B O   1 
ATOM   3452 N N   . TYR B 1 15  ? 10.723  -17.887 1.012   1.00 27.85 ? 15   TYR B N   1 
ATOM   3453 C CA  . TYR B 1 15  ? 9.869   -18.539 1.973   1.00 28.58 ? 15   TYR B CA  1 
ATOM   3454 C C   . TYR B 1 15  ? 9.479   -17.601 3.100   1.00 29.13 ? 15   TYR B C   1 
ATOM   3455 O O   . TYR B 1 15  ? 10.251  -17.386 4.035   1.00 29.48 ? 15   TYR B O   1 
ATOM   3456 C CB  . TYR B 1 15  ? 10.534  -19.795 2.482   1.00 27.95 ? 15   TYR B CB  1 
ATOM   3457 C CG  . TYR B 1 15  ? 9.676   -20.633 3.390   1.00 29.03 ? 15   TYR B CG  1 
ATOM   3458 C CD1 . TYR B 1 15  ? 8.919   -21.673 2.888   1.00 29.16 ? 15   TYR B CD1 1 
ATOM   3459 C CD2 . TYR B 1 15  ? 9.637   -20.393 4.759   1.00 28.02 ? 15   TYR B CD2 1 
ATOM   3460 C CE1 . TYR B 1 15  ? 8.144   -22.455 3.723   1.00 28.73 ? 15   TYR B CE1 1 
ATOM   3461 C CE2 . TYR B 1 15  ? 8.888   -21.158 5.591   1.00 27.52 ? 15   TYR B CE2 1 
ATOM   3462 C CZ  . TYR B 1 15  ? 8.143   -22.188 5.082   1.00 28.31 ? 15   TYR B CZ  1 
ATOM   3463 O OH  . TYR B 1 15  ? 7.371   -22.949 5.925   1.00 27.32 ? 15   TYR B OH  1 
ATOM   3464 N N   . GLN B 1 16  ? 8.286   -17.017 2.992   1.00 30.02 ? 16   GLN B N   1 
ATOM   3465 C CA  . GLN B 1 16  ? 7.828   -15.990 3.964   1.00 30.98 ? 16   GLN B CA  1 
ATOM   3466 C C   . GLN B 1 16  ? 6.694   -16.519 4.839   1.00 32.02 ? 16   GLN B C   1 
ATOM   3467 O O   . GLN B 1 16  ? 6.052   -15.757 5.558   1.00 33.38 ? 16   GLN B O   1 
ATOM   3468 C CB  . GLN B 1 16  ? 7.399   -14.669 3.279   1.00 30.08 ? 16   GLN B CB  1 
ATOM   3469 C CG  . GLN B 1 16  ? 8.412   -14.040 2.347   1.00 29.41 ? 16   GLN B CG  1 
ATOM   3470 C CD  . GLN B 1 16  ? 9.533   -13.304 3.074   1.00 31.64 ? 16   GLN B CD  1 
ATOM   3471 O OE1 . GLN B 1 16  ? 9.400   -12.971 4.265   1.00 28.49 ? 16   GLN B OE1 1 
ATOM   3472 N NE2 . GLN B 1 16  ? 10.652  -13.017 2.346   1.00 30.01 ? 16   GLN B NE2 1 
ATOM   3473 N N   . CYS B 1 17  ? 6.419   -17.815 4.753   1.00 33.11 ? 17   CYS B N   1 
ATOM   3474 C CA  . CYS B 1 17  ? 5.506   -18.463 5.682   1.00 33.86 ? 17   CYS B CA  1 
ATOM   3475 C C   . CYS B 1 17  ? 6.176   -18.546 7.058   1.00 33.91 ? 17   CYS B C   1 
ATOM   3476 O O   . CYS B 1 17  ? 7.386   -18.842 7.132   1.00 34.55 ? 17   CYS B O   1 
ATOM   3477 C CB  . CYS B 1 17  ? 5.193   -19.862 5.181   1.00 33.99 ? 17   CYS B CB  1 
ATOM   3478 S SG  . CYS B 1 17  ? 4.758   -19.898 3.435   1.00 38.07 ? 17   CYS B SG  1 
ATOM   3479 N N   . PHE B 1 18  ? 5.416   -18.264 8.124   1.00 32.89 ? 18   PHE B N   1 
ATOM   3480 C CA  . PHE B 1 18  ? 5.841   -18.520 9.507   1.00 32.32 ? 18   PHE B CA  1 
ATOM   3481 C C   . PHE B 1 18  ? 7.133   -17.815 9.896   1.00 32.09 ? 18   PHE B C   1 
ATOM   3482 O O   . PHE B 1 18  ? 7.941   -18.336 10.679  1.00 32.48 ? 18   PHE B O   1 
ATOM   3483 C CB  . PHE B 1 18  ? 6.008   -20.022 9.711   1.00 31.98 ? 18   PHE B CB  1 
ATOM   3484 C CG  . PHE B 1 18  ? 4.858   -20.810 9.228   1.00 32.03 ? 18   PHE B CG  1 
ATOM   3485 C CD1 . PHE B 1 18  ? 3.571   -20.580 9.742   1.00 31.47 ? 18   PHE B CD1 1 
ATOM   3486 C CD2 . PHE B 1 18  ? 5.040   -21.793 8.265   1.00 30.73 ? 18   PHE B CD2 1 
ATOM   3487 C CE1 . PHE B 1 18  ? 2.493   -21.325 9.287   1.00 30.69 ? 18   PHE B CE1 1 
ATOM   3488 C CE2 . PHE B 1 18  ? 3.979   -22.549 7.811   1.00 29.54 ? 18   PHE B CE2 1 
ATOM   3489 C CZ  . PHE B 1 18  ? 2.689   -22.316 8.321   1.00 29.44 ? 18   PHE B CZ  1 
ATOM   3490 N N   . SER B 1 19  ? 7.294   -16.612 9.369   1.00 31.95 ? 19   SER B N   1 
ATOM   3491 C CA  . SER B 1 19  ? 8.574   -15.941 9.286   1.00 31.62 ? 19   SER B CA  1 
ATOM   3492 C C   . SER B 1 19  ? 9.195   -15.660 10.663  1.00 30.80 ? 19   SER B C   1 
ATOM   3493 O O   . SER B 1 19  ? 10.426  -15.581 10.787  1.00 30.49 ? 19   SER B O   1 
ATOM   3494 C CB  . SER B 1 19  ? 8.386   -14.644 8.509   1.00 32.07 ? 19   SER B CB  1 
ATOM   3495 O OG  . SER B 1 19  ? 7.626   -13.748 9.315   1.00 34.05 ? 19   SER B OG  1 
ATOM   3496 N N   . GLU B 1 20  ? 8.350   -15.516 11.688  1.00 29.74 ? 20   GLU B N   1 
ATOM   3497 C CA  . GLU B 1 20  ? 8.832   -15.244 13.060  1.00 29.38 ? 20   GLU B CA  1 
ATOM   3498 C C   . GLU B 1 20  ? 9.618   -16.435 13.680  1.00 27.73 ? 20   GLU B C   1 
ATOM   3499 O O   . GLU B 1 20  ? 10.393  -16.259 14.602  1.00 27.26 ? 20   GLU B O   1 
ATOM   3500 C CB  . GLU B 1 20  ? 7.697   -14.714 13.990  1.00 29.73 ? 20   GLU B CB  1 
ATOM   3501 C CG  . GLU B 1 20  ? 6.635   -15.741 14.397  1.00 32.64 ? 20   GLU B CG  1 
ATOM   3502 C CD  . GLU B 1 20  ? 5.775   -16.292 13.205  1.00 39.32 ? 20   GLU B CD  1 
ATOM   3503 O OE1 . GLU B 1 20  ? 5.352   -15.497 12.300  1.00 37.02 ? 20   GLU B OE1 1 
ATOM   3504 O OE2 . GLU B 1 20  ? 5.511   -17.545 13.201  1.00 42.18 ? 20   GLU B OE2 1 
ATOM   3505 N N   . THR B 1 21  ? 9.402   -17.628 13.139  1.00 26.19 ? 21   THR B N   1 
ATOM   3506 C CA  . THR B 1 21  ? 10.136  -18.829 13.505  1.00 25.40 ? 21   THR B CA  1 
ATOM   3507 C C   . THR B 1 21  ? 11.092  -19.260 12.371  1.00 25.78 ? 21   THR B C   1 
ATOM   3508 O O   . THR B 1 21  ? 12.302  -19.463 12.595  1.00 25.17 ? 21   THR B O   1 
ATOM   3509 C CB  . THR B 1 21  ? 9.123   -19.945 13.782  1.00 24.67 ? 21   THR B CB  1 
ATOM   3510 O OG1 . THR B 1 21  ? 8.409   -19.566 14.948  1.00 27.40 ? 21   THR B OG1 1 
ATOM   3511 C CG2 . THR B 1 21  ? 9.756   -21.263 14.032  1.00 22.98 ? 21   THR B CG2 1 
ATOM   3512 N N   . SER B 1 22  ? 10.547  -19.369 11.154  1.00 25.42 ? 22   SER B N   1 
ATOM   3513 C CA  . SER B 1 22  ? 11.262  -20.025 10.053  1.00 26.25 ? 22   SER B CA  1 
ATOM   3514 C C   . SER B 1 22  ? 12.523  -19.260 9.641   1.00 26.75 ? 22   SER B C   1 
ATOM   3515 O O   . SER B 1 22  ? 13.434  -19.837 9.017   1.00 27.75 ? 22   SER B O   1 
ATOM   3516 C CB  . SER B 1 22  ? 10.355  -20.216 8.847   1.00 25.97 ? 22   SER B CB  1 
ATOM   3517 O OG  . SER B 1 22  ? 10.077  -18.951 8.248   1.00 25.79 ? 22   SER B OG  1 
ATOM   3518 N N   . HIS B 1 23  ? 12.578  -17.976 9.996   1.00 26.10 ? 23   HIS B N   1 
ATOM   3519 C CA  . HIS B 1 23  ? 13.703  -17.105 9.616   1.00 25.57 ? 23   HIS B CA  1 
ATOM   3520 C C   . HIS B 1 23  ? 14.876  -17.167 10.616  1.00 24.96 ? 23   HIS B C   1 
ATOM   3521 O O   . HIS B 1 23  ? 15.963  -16.649 10.339  1.00 24.64 ? 23   HIS B O   1 
ATOM   3522 C CB  . HIS B 1 23  ? 13.209  -15.669 9.404   1.00 24.76 ? 23   HIS B CB  1 
ATOM   3523 C CG  . HIS B 1 23  ? 12.401  -15.484 8.146   1.00 27.98 ? 23   HIS B CG  1 
ATOM   3524 N ND1 . HIS B 1 23  ? 12.127  -14.240 7.603   1.00 31.81 ? 23   HIS B ND1 1 
ATOM   3525 C CD2 . HIS B 1 23  ? 11.824  -16.386 7.312   1.00 28.25 ? 23   HIS B CD2 1 
ATOM   3526 C CE1 . HIS B 1 23  ? 11.428  -14.388 6.488   1.00 29.91 ? 23   HIS B CE1 1 
ATOM   3527 N NE2 . HIS B 1 23  ? 11.235  -15.680 6.286   1.00 27.60 ? 23   HIS B NE2 1 
ATOM   3528 N N   . LEU B 1 24  ? 14.658  -17.821 11.756  1.00 24.62 ? 24   LEU B N   1 
ATOM   3529 C CA  . LEU B 1 24  ? 15.699  -17.938 12.798  1.00 24.24 ? 24   LEU B CA  1 
ATOM   3530 C C   . LEU B 1 24  ? 16.287  -19.349 12.880  1.00 23.41 ? 24   LEU B C   1 
ATOM   3531 O O   . LEU B 1 24  ? 16.814  -19.735 13.923  1.00 22.97 ? 24   LEU B O   1 
ATOM   3532 C CB  . LEU B 1 24  ? 15.198  -17.484 14.172  1.00 24.12 ? 24   LEU B CB  1 
ATOM   3533 C CG  . LEU B 1 24  ? 14.653  -16.045 14.181  1.00 25.56 ? 24   LEU B CG  1 
ATOM   3534 C CD1 . LEU B 1 24  ? 13.666  -15.793 15.345  1.00 26.30 ? 24   LEU B CD1 1 
ATOM   3535 C CD2 . LEU B 1 24  ? 15.777  -14.993 14.142  1.00 23.70 ? 24   LEU B CD2 1 
ATOM   3536 N N   . TRP B 1 25  ? 16.208  -20.104 11.779  1.00 21.73 ? 25   TRP B N   1 
ATOM   3537 C CA  . TRP B 1 25  ? 16.836  -21.408 11.737  1.00 21.03 ? 25   TRP B CA  1 
ATOM   3538 C C   . TRP B 1 25  ? 18.317  -21.330 11.252  1.00 19.59 ? 25   TRP B C   1 
ATOM   3539 O O   . TRP B 1 25  ? 18.922  -22.326 10.933  1.00 18.57 ? 25   TRP B O   1 
ATOM   3540 C CB  . TRP B 1 25  ? 16.000  -22.383 10.901  1.00 21.04 ? 25   TRP B CB  1 
ATOM   3541 C CG  . TRP B 1 25  ? 14.620  -22.633 11.467  1.00 23.45 ? 25   TRP B CG  1 
ATOM   3542 C CD1 . TRP B 1 25  ? 14.249  -22.551 12.767  1.00 23.57 ? 25   TRP B CD1 1 
ATOM   3543 C CD2 . TRP B 1 25  ? 13.429  -23.020 10.739  1.00 24.64 ? 25   TRP B CD2 1 
ATOM   3544 N NE1 . TRP B 1 25  ? 12.911  -22.858 12.910  1.00 23.80 ? 25   TRP B NE1 1 
ATOM   3545 C CE2 . TRP B 1 25  ? 12.384  -23.146 11.683  1.00 24.98 ? 25   TRP B CE2 1 
ATOM   3546 C CE3 . TRP B 1 25  ? 13.152  -23.275 9.390   1.00 23.80 ? 25   TRP B CE3 1 
ATOM   3547 C CZ2 . TRP B 1 25  ? 11.074  -23.515 11.322  1.00 25.16 ? 25   TRP B CZ2 1 
ATOM   3548 C CZ3 . TRP B 1 25  ? 11.855  -23.645 9.025   1.00 25.06 ? 25   TRP B CZ3 1 
ATOM   3549 C CH2 . TRP B 1 25  ? 10.827  -23.763 9.998   1.00 24.79 ? 25   TRP B CH2 1 
ATOM   3550 N N   . GLY B 1 26  ? 18.895  -20.146 11.221  1.00 18.93 ? 26   GLY B N   1 
ATOM   3551 C CA  . GLY B 1 26  ? 20.220  -19.980 10.587  1.00 19.36 ? 26   GLY B CA  1 
ATOM   3552 C C   . GLY B 1 26  ? 20.344  -20.577 9.204   1.00 18.90 ? 26   GLY B C   1 
ATOM   3553 O O   . GLY B 1 26  ? 19.624  -20.183 8.292   1.00 19.78 ? 26   GLY B O   1 
ATOM   3554 N N   . GLN B 1 27  ? 21.269  -21.514 9.052   1.00 18.40 ? 27   GLN B N   1 
ATOM   3555 C CA  . GLN B 1 27  ? 21.610  -22.059 7.771   1.00 17.84 ? 27   GLN B CA  1 
ATOM   3556 C C   . GLN B 1 27  ? 20.691  -23.217 7.452   1.00 18.37 ? 27   GLN B C   1 
ATOM   3557 O O   . GLN B 1 27  ? 20.816  -23.874 6.372   1.00 18.38 ? 27   GLN B O   1 
ATOM   3558 C CB  . GLN B 1 27  ? 23.064  -22.510 7.717   1.00 18.01 ? 27   GLN B CB  1 
ATOM   3559 C CG  . GLN B 1 27  ? 23.425  -23.803 8.505   1.00 18.17 ? 27   GLN B CG  1 
ATOM   3560 C CD  . GLN B 1 27  ? 23.533  -23.545 10.006  1.00 21.56 ? 27   GLN B CD  1 
ATOM   3561 O OE1 . GLN B 1 27  ? 24.034  -22.475 10.450  1.00 22.57 ? 27   GLN B OE1 1 
ATOM   3562 N NE2 . GLN B 1 27  ? 23.025  -24.498 10.807  1.00 20.79 ? 27   GLN B NE2 1 
ATOM   3563 N N   . TYR B 1 28  ? 19.811  -23.491 8.405   1.00 17.98 ? 28   TYR B N   1 
ATOM   3564 C CA  . TYR B 1 28  ? 18.682  -24.379 8.180   1.00 19.31 ? 28   TYR B CA  1 
ATOM   3565 C C   . TYR B 1 28  ? 17.439  -23.625 7.721   1.00 19.43 ? 28   TYR B C   1 
ATOM   3566 O O   . TYR B 1 28  ? 16.416  -24.250 7.482   1.00 19.77 ? 28   TYR B O   1 
ATOM   3567 C CB  . TYR B 1 28  ? 18.369  -25.269 9.408   1.00 19.89 ? 28   TYR B CB  1 
ATOM   3568 C CG  . TYR B 1 28  ? 19.515  -26.210 9.807   1.00 20.77 ? 28   TYR B CG  1 
ATOM   3569 C CD1 . TYR B 1 28  ? 20.328  -26.818 8.844   1.00 23.31 ? 28   TYR B CD1 1 
ATOM   3570 C CD2 . TYR B 1 28  ? 19.799  -26.464 11.131  1.00 21.28 ? 28   TYR B CD2 1 
ATOM   3571 C CE1 . TYR B 1 28  ? 21.383  -27.646 9.191   1.00 21.75 ? 28   TYR B CE1 1 
ATOM   3572 C CE2 . TYR B 1 28  ? 20.859  -27.295 11.498  1.00 22.33 ? 28   TYR B CE2 1 
ATOM   3573 C CZ  . TYR B 1 28  ? 21.647  -27.877 10.534  1.00 22.94 ? 28   TYR B CZ  1 
ATOM   3574 O OH  . TYR B 1 28  ? 22.658  -28.724 10.906  1.00 22.28 ? 28   TYR B OH  1 
ATOM   3575 N N   . ALA B 1 29  ? 17.528  -22.299 7.573   1.00 19.49 ? 29   ALA B N   1 
ATOM   3576 C CA  . ALA B 1 29  ? 16.373  -21.522 7.111   1.00 19.70 ? 29   ALA B CA  1 
ATOM   3577 C C   . ALA B 1 29  ? 16.206  -21.624 5.607   1.00 20.15 ? 29   ALA B C   1 
ATOM   3578 O O   . ALA B 1 29  ? 17.190  -21.599 4.835   1.00 20.29 ? 29   ALA B O   1 
ATOM   3579 C CB  . ALA B 1 29  ? 16.472  -20.068 7.523   1.00 19.14 ? 29   ALA B CB  1 
ATOM   3580 N N   . PRO B 1 30  ? 14.947  -21.722 5.164   1.00 20.31 ? 30   PRO B N   1 
ATOM   3581 C CA  . PRO B 1 30  ? 14.736  -21.736 3.690   1.00 19.10 ? 30   PRO B CA  1 
ATOM   3582 C C   . PRO B 1 30  ? 15.065  -20.356 3.143   1.00 18.28 ? 30   PRO B C   1 
ATOM   3583 O O   . PRO B 1 30  ? 14.798  -19.374 3.829   1.00 18.19 ? 30   PRO B O   1 
ATOM   3584 C CB  . PRO B 1 30  ? 13.252  -22.016 3.538   1.00 19.63 ? 30   PRO B CB  1 
ATOM   3585 C CG  . PRO B 1 30  ? 12.617  -21.940 4.954   1.00 19.64 ? 30   PRO B CG  1 
ATOM   3586 C CD  . PRO B 1 30  ? 13.696  -21.649 5.956   1.00 20.43 ? 30   PRO B CD  1 
ATOM   3587 N N   . PHE B 1 31  ? 15.669  -20.256 1.961   1.00 17.21 ? 31   PHE B N   1 
ATOM   3588 C CA  . PHE B 1 31  ? 15.822  -18.935 1.353   1.00 17.04 ? 31   PHE B CA  1 
ATOM   3589 C C   . PHE B 1 31  ? 14.633  -17.988 1.605   1.00 16.93 ? 31   PHE B C   1 
ATOM   3590 O O   . PHE B 1 31  ? 13.495  -18.364 1.353   1.00 16.59 ? 31   PHE B O   1 
ATOM   3591 C CB  . PHE B 1 31  ? 15.967  -18.995 -0.159  1.00 16.79 ? 31   PHE B CB  1 
ATOM   3592 C CG  . PHE B 1 31  ? 15.949  -17.619 -0.781  1.00 17.15 ? 31   PHE B CG  1 
ATOM   3593 C CD1 . PHE B 1 31  ? 17.007  -16.736 -0.558  1.00 15.56 ? 31   PHE B CD1 1 
ATOM   3594 C CD2 . PHE B 1 31  ? 14.848  -17.171 -1.530  1.00 17.73 ? 31   PHE B CD2 1 
ATOM   3595 C CE1 . PHE B 1 31  ? 17.004  -15.464 -1.104  1.00 17.22 ? 31   PHE B CE1 1 
ATOM   3596 C CE2 . PHE B 1 31  ? 14.839  -15.877 -2.078  1.00 15.58 ? 31   PHE B CE2 1 
ATOM   3597 C CZ  . PHE B 1 31  ? 15.927  -15.024 -1.857  1.00 15.88 ? 31   PHE B CZ  1 
ATOM   3598 N N   . PHE B 1 32  ? 14.897  -16.765 2.055   1.00 17.18 ? 32   PHE B N   1 
ATOM   3599 C CA  . PHE B 1 32  ? 13.858  -15.726 2.131   1.00 18.16 ? 32   PHE B CA  1 
ATOM   3600 C C   . PHE B 1 32  ? 14.537  -14.429 1.727   1.00 18.51 ? 32   PHE B C   1 
ATOM   3601 O O   . PHE B 1 32  ? 15.558  -14.098 2.288   1.00 19.40 ? 32   PHE B O   1 
ATOM   3602 C CB  . PHE B 1 32  ? 13.202  -15.630 3.530   1.00 17.82 ? 32   PHE B CB  1 
ATOM   3603 C CG  . PHE B 1 32  ? 14.181  -15.335 4.658   1.00 19.03 ? 32   PHE B CG  1 
ATOM   3604 C CD1 . PHE B 1 32  ? 14.853  -16.380 5.304   1.00 19.28 ? 32   PHE B CD1 1 
ATOM   3605 C CD2 . PHE B 1 32  ? 14.428  -14.020 5.057   1.00 20.93 ? 32   PHE B CD2 1 
ATOM   3606 C CE1 . PHE B 1 32  ? 15.765  -16.132 6.317   1.00 21.43 ? 32   PHE B CE1 1 
ATOM   3607 C CE2 . PHE B 1 32  ? 15.330  -13.740 6.085   1.00 23.38 ? 32   PHE B CE2 1 
ATOM   3608 C CZ  . PHE B 1 32  ? 16.013  -14.808 6.713   1.00 23.35 ? 32   PHE B CZ  1 
ATOM   3609 N N   . SER B 1 33  ? 13.986  -13.738 0.728   1.00 19.21 ? 33   SER B N   1 
ATOM   3610 C CA  . SER B 1 33  ? 14.494  -12.477 0.183   1.00 18.92 ? 33   SER B CA  1 
ATOM   3611 C C   . SER B 1 33  ? 14.558  -11.334 1.145   1.00 19.54 ? 33   SER B C   1 
ATOM   3612 O O   . SER B 1 33  ? 13.597  -11.012 1.819   1.00 19.87 ? 33   SER B O   1 
ATOM   3613 C CB  . SER B 1 33  ? 13.631  -12.000 -0.990  1.00 18.82 ? 33   SER B CB  1 
ATOM   3614 O OG  . SER B 1 33  ? 14.059  -10.691 -1.360  1.00 16.73 ? 33   SER B OG  1 
ATOM   3615 N N   . LEU B 1 34  ? 15.697  -10.671 1.146   1.00 20.61 ? 34   LEU B N   1 
ATOM   3616 C CA  . LEU B 1 34  ? 15.891  -9.545  2.027   1.00 21.18 ? 34   LEU B CA  1 
ATOM   3617 C C   . LEU B 1 34  ? 15.663  -8.220  1.315   1.00 22.56 ? 34   LEU B C   1 
ATOM   3618 O O   . LEU B 1 34  ? 16.122  -7.172  1.796   1.00 21.97 ? 34   LEU B O   1 
ATOM   3619 C CB  . LEU B 1 34  ? 17.293  -9.603  2.611   1.00 20.40 ? 34   LEU B CB  1 
ATOM   3620 C CG  . LEU B 1 34  ? 17.503  -10.802 3.524   1.00 19.16 ? 34   LEU B CG  1 
ATOM   3621 C CD1 . LEU B 1 34  ? 18.985  -10.964 3.863   1.00 18.53 ? 34   LEU B CD1 1 
ATOM   3622 C CD2 . LEU B 1 34  ? 16.624  -10.620 4.757   1.00 19.70 ? 34   LEU B CD2 1 
ATOM   3623 N N   . ALA B 1 35  ? 14.966  -8.263  0.172   1.00 24.13 ? 35   ALA B N   1 
ATOM   3624 C CA  . ALA B 1 35  ? 14.856  -7.089  -0.679  1.00 26.09 ? 35   ALA B CA  1 
ATOM   3625 C C   . ALA B 1 35  ? 14.209  -5.911  0.071   1.00 28.01 ? 35   ALA B C   1 
ATOM   3626 O O   . ALA B 1 35  ? 14.702  -4.780  -0.024  1.00 28.44 ? 35   ALA B O   1 
ATOM   3627 C CB  . ALA B 1 35  ? 14.108  -7.412  -1.982  1.00 25.44 ? 35   ALA B CB  1 
ATOM   3628 N N   . ASN B 1 36  ? 13.139  -6.203  0.823   1.00 30.02 ? 36   ASN B N   1 
ATOM   3629 C CA  A ASN B 1 36  ? 12.429  -5.187  1.593   0.50 31.53 ? 36   ASN B CA  1 
ATOM   3630 C CA  B ASN B 1 36  ? 12.406  -5.209  1.620   0.50 31.79 ? 36   ASN B CA  1 
ATOM   3631 C C   . ASN B 1 36  ? 13.199  -4.705  2.848   1.00 33.02 ? 36   ASN B C   1 
ATOM   3632 O O   . ASN B 1 36  ? 12.812  -3.699  3.504   1.00 33.36 ? 36   ASN B O   1 
ATOM   3633 C CB  A ASN B 1 36  ? 11.005  -5.673  1.886   0.50 31.24 ? 36   ASN B CB  1 
ATOM   3634 C CB  B ASN B 1 36  ? 11.000  -5.733  1.996   0.50 31.64 ? 36   ASN B CB  1 
ATOM   3635 C CG  A ASN B 1 36  ? 10.180  -5.803  0.617   0.50 30.97 ? 36   ASN B CG  1 
ATOM   3636 C CG  B ASN B 1 36  ? 10.987  -6.553  3.284   0.50 32.64 ? 36   ASN B CG  1 
ATOM   3637 O OD1 A ASN B 1 36  ? 9.890   -4.812  -0.040  0.50 30.78 ? 36   ASN B OD1 1 
ATOM   3638 O OD1 B ASN B 1 36  ? 10.753  -7.767  3.261   0.50 32.31 ? 36   ASN B OD1 1 
ATOM   3639 N ND2 A ASN B 1 36  ? 9.834   -7.031  0.246   0.50 31.93 ? 36   ASN B ND2 1 
ATOM   3640 N ND2 B ASN B 1 36  ? 11.212  -5.884  4.419   0.50 33.49 ? 36   ASN B ND2 1 
ATOM   3641 N N   . GLU B 1 37  ? 14.314  -5.391  3.143   1.00 33.87 ? 37   GLU B N   1 
ATOM   3642 C CA  . GLU B 1 37  ? 15.232  -5.008  4.197   1.00 35.01 ? 37   GLU B CA  1 
ATOM   3643 C C   . GLU B 1 37  ? 16.419  -4.206  3.676   1.00 35.19 ? 37   GLU B C   1 
ATOM   3644 O O   . GLU B 1 37  ? 17.237  -3.713  4.472   1.00 35.09 ? 37   GLU B O   1 
ATOM   3645 C CB  . GLU B 1 37  ? 15.728  -6.257  4.929   1.00 35.48 ? 37   GLU B CB  1 
ATOM   3646 C CG  . GLU B 1 37  ? 14.631  -7.006  5.671   1.00 38.40 ? 37   GLU B CG  1 
ATOM   3647 C CD  . GLU B 1 37  ? 14.180  -6.267  6.924   1.00 42.15 ? 37   GLU B CD  1 
ATOM   3648 O OE1 . GLU B 1 37  ? 14.748  -5.184  7.234   1.00 43.06 ? 37   GLU B OE1 1 
ATOM   3649 O OE2 . GLU B 1 37  ? 13.255  -6.776  7.596   1.00 45.02 ? 37   GLU B OE2 1 
ATOM   3650 N N   . SER B 1 38  ? 16.516  -4.075  2.349   1.00 35.26 ? 38   SER B N   1 
ATOM   3651 C CA  . SER B 1 38  ? 17.613  -3.337  1.719   1.00 35.38 ? 38   SER B CA  1 
ATOM   3652 C C   . SER B 1 38  ? 17.368  -1.833  1.877   1.00 36.16 ? 38   SER B C   1 
ATOM   3653 O O   . SER B 1 38  ? 16.329  -1.309  1.444   1.00 37.05 ? 38   SER B O   1 
ATOM   3654 C CB  . SER B 1 38  ? 17.729  -3.727  0.234   1.00 35.51 ? 38   SER B CB  1 
ATOM   3655 O OG  . SER B 1 38  ? 19.005  -3.412  -0.335  1.00 34.00 ? 38   SER B OG  1 
ATOM   3656 N N   . VAL B 1 39  ? 18.306  -1.129  2.508   1.00 36.26 ? 39   VAL B N   1 
ATOM   3657 C CA  . VAL B 1 39  ? 18.191  0.328   2.616   1.00 35.70 ? 39   VAL B CA  1 
ATOM   3658 C C   . VAL B 1 39  ? 18.581  0.965   1.293   1.00 35.28 ? 39   VAL B C   1 
ATOM   3659 O O   . VAL B 1 39  ? 18.112  2.050   0.936   1.00 35.98 ? 39   VAL B O   1 
ATOM   3660 C CB  . VAL B 1 39  ? 19.012  0.885   3.800   1.00 35.87 ? 39   VAL B CB  1 
ATOM   3661 C CG1 . VAL B 1 39  ? 18.990  2.412   3.841   1.00 35.01 ? 39   VAL B CG1 1 
ATOM   3662 C CG2 . VAL B 1 39  ? 18.461  0.309   5.112   1.00 37.01 ? 39   VAL B CG2 1 
ATOM   3663 N N   . ILE B 1 40  ? 19.431  0.295   0.547   1.00 34.69 ? 40   ILE B N   1 
ATOM   3664 C CA  . ILE B 1 40  ? 19.719  0.761   -0.806  1.00 34.55 ? 40   ILE B CA  1 
ATOM   3665 C C   . ILE B 1 40  ? 18.814  -0.004  -1.783  1.00 34.82 ? 40   ILE B C   1 
ATOM   3666 O O   . ILE B 1 40  ? 18.568  -1.197  -1.622  1.00 34.21 ? 40   ILE B O   1 
ATOM   3667 C CB  . ILE B 1 40  ? 21.233  0.654   -1.121  1.00 34.31 ? 40   ILE B CB  1 
ATOM   3668 C CG1 . ILE B 1 40  ? 22.024  1.547   -0.135  1.00 33.53 ? 40   ILE B CG1 1 
ATOM   3669 C CG2 . ILE B 1 40  ? 21.545  1.000   -2.608  1.00 32.85 ? 40   ILE B CG2 1 
ATOM   3670 C CD1 . ILE B 1 40  ? 23.494  1.188   0.005   1.00 31.27 ? 40   ILE B CD1 1 
ATOM   3671 N N   . SER B 1 41  ? 18.268  0.701   -2.758  1.00 35.81 ? 41   SER B N   1 
ATOM   3672 C CA  . SER B 1 41  ? 17.376  0.056   -3.706  1.00 36.94 ? 41   SER B CA  1 
ATOM   3673 C C   . SER B 1 41  ? 18.164  -0.914  -4.588  1.00 37.22 ? 41   SER B C   1 
ATOM   3674 O O   . SER B 1 41  ? 19.222  -0.557  -5.115  1.00 37.49 ? 41   SER B O   1 
ATOM   3675 C CB  . SER B 1 41  ? 16.632  1.081   -4.545  1.00 36.92 ? 41   SER B CB  1 
ATOM   3676 O OG  . SER B 1 41  ? 15.646  0.435   -5.325  1.00 38.38 ? 41   SER B OG  1 
ATOM   3677 N N   . PRO B 1 42  ? 17.664  -2.152  -4.717  1.00 38.09 ? 42   PRO B N   1 
ATOM   3678 C CA  . PRO B 1 42  ? 18.277  -3.151  -5.616  1.00 38.84 ? 42   PRO B CA  1 
ATOM   3679 C C   . PRO B 1 42  ? 18.112  -2.812  -7.098  1.00 39.35 ? 42   PRO B C   1 
ATOM   3680 O O   . PRO B 1 42  ? 18.886  -3.290  -7.918  1.00 39.59 ? 42   PRO B O   1 
ATOM   3681 C CB  . PRO B 1 42  ? 17.536  -4.448  -5.269  1.00 38.77 ? 42   PRO B CB  1 
ATOM   3682 C CG  . PRO B 1 42  ? 16.224  -3.979  -4.654  1.00 38.26 ? 42   PRO B CG  1 
ATOM   3683 C CD  . PRO B 1 42  ? 16.559  -2.724  -3.924  1.00 37.84 ? 42   PRO B CD  1 
ATOM   3684 N N   . GLU B 1 43  ? 17.111  -2.011  -7.444  1.00 39.89 ? 43   GLU B N   1 
ATOM   3685 C CA  . GLU B 1 43  ? 16.951  -1.582  -8.827  1.00 41.12 ? 43   GLU B CA  1 
ATOM   3686 C C   . GLU B 1 43  ? 18.222  -0.972  -9.425  1.00 41.41 ? 43   GLU B C   1 
ATOM   3687 O O   . GLU B 1 43  ? 19.049  -0.337  -8.726  1.00 41.38 ? 43   GLU B O   1 
ATOM   3688 C CB  . GLU B 1 43  ? 15.772  -0.618  -9.009  1.00 41.09 ? 43   GLU B CB  1 
ATOM   3689 C CG  . GLU B 1 43  ? 14.440  -1.317  -9.257  1.00 43.75 ? 43   GLU B CG  1 
ATOM   3690 C CD  . GLU B 1 43  ? 13.670  -1.553  -7.976  1.00 48.50 ? 43   GLU B CD  1 
ATOM   3691 O OE1 . GLU B 1 43  ? 12.777  -0.720  -7.664  1.00 51.41 ? 43   GLU B OE1 1 
ATOM   3692 O OE2 . GLU B 1 43  ? 13.961  -2.548  -7.271  1.00 48.91 ? 43   GLU B OE2 1 
ATOM   3693 N N   . VAL B 1 44  ? 18.365  -1.206  -10.722 1.00 41.20 ? 44   VAL B N   1 
ATOM   3694 C CA  . VAL B 1 44  ? 19.393  -0.607  -11.535 1.00 41.58 ? 44   VAL B CA  1 
ATOM   3695 C C   . VAL B 1 44  ? 19.079  0.889   -11.669 1.00 41.63 ? 44   VAL B C   1 
ATOM   3696 O O   . VAL B 1 44  ? 17.977  1.272   -12.088 1.00 41.72 ? 44   VAL B O   1 
ATOM   3697 C CB  . VAL B 1 44  ? 19.348  -1.240  -12.938 1.00 42.05 ? 44   VAL B CB  1 
ATOM   3698 C CG1 . VAL B 1 44  ? 20.582  -0.858  -13.749 1.00 42.67 ? 44   VAL B CG1 1 
ATOM   3699 C CG2 . VAL B 1 44  ? 19.159  -2.783  -12.844 1.00 42.39 ? 44   VAL B CG2 1 
ATOM   3700 N N   . PRO B 1 45  ? 20.034  1.756   -11.303 1.00 41.26 ? 45   PRO B N   1 
ATOM   3701 C CA  . PRO B 1 45  ? 19.744  3.172   -11.454 1.00 40.69 ? 45   PRO B CA  1 
ATOM   3702 C C   . PRO B 1 45  ? 19.561  3.598   -12.920 1.00 40.40 ? 45   PRO B C   1 
ATOM   3703 O O   . PRO B 1 45  ? 20.009  2.898   -13.853 1.00 39.54 ? 45   PRO B O   1 
ATOM   3704 C CB  . PRO B 1 45  ? 20.982  3.847   -10.841 1.00 40.81 ? 45   PRO B CB  1 
ATOM   3705 C CG  . PRO B 1 45  ? 21.521  2.849   -9.901  1.00 40.44 ? 45   PRO B CG  1 
ATOM   3706 C CD  . PRO B 1 45  ? 21.282  1.528   -10.555 1.00 41.10 ? 45   PRO B CD  1 
ATOM   3707 N N   . ALA B 1 46  ? 18.896  4.742   -13.102 1.00 39.67 ? 46   ALA B N   1 
ATOM   3708 C CA  . ALA B 1 46  ? 18.703  5.313   -14.425 1.00 39.12 ? 46   ALA B CA  1 
ATOM   3709 C C   . ALA B 1 46  ? 20.046  5.762   -14.952 1.00 38.13 ? 46   ALA B C   1 
ATOM   3710 O O   . ALA B 1 46  ? 20.912  6.169   -14.189 1.00 38.70 ? 46   ALA B O   1 
ATOM   3711 C CB  . ALA B 1 46  ? 17.744  6.479   -14.378 1.00 39.59 ? 46   ALA B CB  1 
ATOM   3712 N N   . GLY B 1 47  ? 20.222  5.665   -16.257 1.00 37.07 ? 47   GLY B N   1 
ATOM   3713 C CA  . GLY B 1 47  ? 21.477  6.016   -16.891 1.00 35.75 ? 47   GLY B CA  1 
ATOM   3714 C C   . GLY B 1 47  ? 22.418  4.842   -16.881 1.00 35.02 ? 47   GLY B C   1 
ATOM   3715 O O   . GLY B 1 47  ? 23.420  4.852   -17.605 1.00 35.43 ? 47   GLY B O   1 
ATOM   3716 N N   . CYS B 1 48  ? 22.070  3.816   -16.089 1.00 33.73 ? 48   CYS B N   1 
ATOM   3717 C CA  . CYS B 1 48  ? 22.943  2.665   -15.816 1.00 32.79 ? 48   CYS B CA  1 
ATOM   3718 C C   . CYS B 1 48  ? 22.518  1.360   -16.508 1.00 32.06 ? 48   CYS B C   1 
ATOM   3719 O O   . CYS B 1 48  ? 21.310  1.012   -16.588 1.00 31.31 ? 48   CYS B O   1 
ATOM   3720 C CB  . CYS B 1 48  ? 23.008  2.401   -14.296 1.00 33.42 ? 48   CYS B CB  1 
ATOM   3721 S SG  . CYS B 1 48  ? 23.883  3.650   -13.292 1.00 33.03 ? 48   CYS B SG  1 
ATOM   3722 N N   . ARG B 1 49  ? 23.519  0.599   -16.936 1.00 30.01 ? 49   ARG B N   1 
ATOM   3723 C CA  . ARG B 1 49  ? 23.245  -0.656  -17.597 1.00 29.07 ? 49   ARG B CA  1 
ATOM   3724 C C   . ARG B 1 49  ? 24.174  -1.781  -17.090 1.00 27.03 ? 49   ARG B C   1 
ATOM   3725 O O   . ARG B 1 49  ? 25.394  -1.638  -17.060 1.00 26.21 ? 49   ARG B O   1 
ATOM   3726 C CB  . ARG B 1 49  ? 23.382  -0.405  -19.106 1.00 30.00 ? 49   ARG B CB  1 
ATOM   3727 C CG  . ARG B 1 49  ? 22.866  -1.488  -20.064 1.00 33.68 ? 49   ARG B CG  1 
ATOM   3728 C CD  . ARG B 1 49  ? 23.483  -1.256  -21.467 1.00 40.26 ? 49   ARG B CD  1 
ATOM   3729 N NE  . ARG B 1 49  ? 24.694  -0.390  -21.439 1.00 45.46 ? 49   ARG B NE  1 
ATOM   3730 C CZ  . ARG B 1 49  ? 25.909  -0.712  -21.902 1.00 46.70 ? 49   ARG B CZ  1 
ATOM   3731 N NH1 . ARG B 1 49  ? 26.158  -1.900  -22.460 1.00 47.16 ? 49   ARG B NH1 1 
ATOM   3732 N NH2 . ARG B 1 49  ? 26.892  0.178   -21.814 1.00 49.25 ? 49   ARG B NH2 1 
ATOM   3733 N N   . VAL B 1 50  ? 23.577  -2.900  -16.688 1.00 25.87 ? 50   VAL B N   1 
ATOM   3734 C CA  . VAL B 1 50  ? 24.314  -4.077  -16.222 1.00 23.90 ? 50   VAL B CA  1 
ATOM   3735 C C   . VAL B 1 50  ? 25.055  -4.776  -17.397 1.00 23.59 ? 50   VAL B C   1 
ATOM   3736 O O   . VAL B 1 50  ? 24.444  -5.131  -18.420 1.00 23.03 ? 50   VAL B O   1 
ATOM   3737 C CB  . VAL B 1 50  ? 23.354  -5.088  -15.504 1.00 24.68 ? 50   VAL B CB  1 
ATOM   3738 C CG1 . VAL B 1 50  ? 24.142  -6.246  -14.829 1.00 23.96 ? 50   VAL B CG1 1 
ATOM   3739 C CG2 . VAL B 1 50  ? 22.473  -4.409  -14.477 1.00 23.51 ? 50   VAL B CG2 1 
ATOM   3740 N N   . THR B 1 51  ? 26.367  -4.964  -17.252 1.00 22.52 ? 51   THR B N   1 
ATOM   3741 C CA  . THR B 1 51  ? 27.191  -5.573  -18.299 1.00 22.38 ? 51   THR B CA  1 
ATOM   3742 C C   . THR B 1 51  ? 27.924  -6.856  -17.877 1.00 21.71 ? 51   THR B C   1 
ATOM   3743 O O   . THR B 1 51  ? 28.736  -7.381  -18.636 1.00 22.42 ? 51   THR B O   1 
ATOM   3744 C CB  . THR B 1 51  ? 28.228  -4.574  -18.836 1.00 22.88 ? 51   THR B CB  1 
ATOM   3745 O OG1 . THR B 1 51  ? 29.198  -4.305  -17.824 1.00 23.63 ? 51   THR B OG1 1 
ATOM   3746 C CG2 . THR B 1 51  ? 27.561  -3.260  -19.246 1.00 23.49 ? 51   THR B CG2 1 
ATOM   3747 N N   . PHE B 1 52  ? 27.659  -7.333  -16.658 1.00 20.93 ? 52   PHE B N   1 
ATOM   3748 C CA  . PHE B 1 52  ? 28.284  -8.541  -16.054 1.00 19.57 ? 52   PHE B CA  1 
ATOM   3749 C C   . PHE B 1 52  ? 27.353  -8.986  -14.942 1.00 18.64 ? 52   PHE B C   1 
ATOM   3750 O O   . PHE B 1 52  ? 26.837  -8.156  -14.208 1.00 18.33 ? 52   PHE B O   1 
ATOM   3751 C CB  . PHE B 1 52  ? 29.648  -8.180  -15.461 1.00 19.48 ? 52   PHE B CB  1 
ATOM   3752 C CG  . PHE B 1 52  ? 30.400  -9.331  -14.767 1.00 18.27 ? 52   PHE B CG  1 
ATOM   3753 C CD1 . PHE B 1 52  ? 30.194  -9.600  -13.422 1.00 15.18 ? 52   PHE B CD1 1 
ATOM   3754 C CD2 . PHE B 1 52  ? 31.397  -10.063 -15.456 1.00 18.29 ? 52   PHE B CD2 1 
ATOM   3755 C CE1 . PHE B 1 52  ? 30.905  -10.631 -12.769 1.00 15.72 ? 52   PHE B CE1 1 
ATOM   3756 C CE2 . PHE B 1 52  ? 32.128  -11.118 -14.818 1.00 15.94 ? 52   PHE B CE2 1 
ATOM   3757 C CZ  . PHE B 1 52  ? 31.883  -11.408 -13.491 1.00 16.51 ? 52   PHE B CZ  1 
ATOM   3758 N N   . ALA B 1 53  ? 27.135  -10.286 -14.840 1.00 17.57 ? 53   ALA B N   1 
ATOM   3759 C CA  . ALA B 1 53  ? 26.457  -10.848 -13.683 1.00 17.27 ? 53   ALA B CA  1 
ATOM   3760 C C   . ALA B 1 53  ? 26.967  -12.256 -13.370 1.00 15.98 ? 53   ALA B C   1 
ATOM   3761 O O   . ALA B 1 53  ? 26.934  -13.140 -14.209 1.00 15.57 ? 53   ALA B O   1 
ATOM   3762 C CB  . ALA B 1 53  ? 24.872  -10.787 -13.844 1.00 16.86 ? 53   ALA B CB  1 
ATOM   3763 N N   . GLN B 1 54  ? 27.518  -12.414 -12.170 1.00 15.79 ? 54   GLN B N   1 
ATOM   3764 C CA  . GLN B 1 54  ? 27.923  -13.717 -11.593 1.00 14.69 ? 54   GLN B CA  1 
ATOM   3765 C C   . GLN B 1 54  ? 26.991  -13.986 -10.425 1.00 14.13 ? 54   GLN B C   1 
ATOM   3766 O O   . GLN B 1 54  ? 26.757  -13.116 -9.594  1.00 14.14 ? 54   GLN B O   1 
ATOM   3767 C CB  . GLN B 1 54  ? 29.369  -13.685 -11.081 1.00 14.28 ? 54   GLN B CB  1 
ATOM   3768 C CG  . GLN B 1 54  ? 29.905  -14.946 -10.366 1.00 15.74 ? 54   GLN B CG  1 
ATOM   3769 C CD  . GLN B 1 54  ? 31.476  -15.056 -10.461 1.00 19.35 ? 54   GLN B CD  1 
ATOM   3770 O OE1 . GLN B 1 54  ? 32.058  -15.131 -11.568 1.00 20.82 ? 54   GLN B OE1 1 
ATOM   3771 N NE2 . GLN B 1 54  ? 32.152  -15.064 -9.304  1.00 16.86 ? 54   GLN B NE2 1 
ATOM   3772 N N   . VAL B 1 55  ? 26.464  -15.195 -10.358 1.00 13.99 ? 55   VAL B N   1 
ATOM   3773 C CA  . VAL B 1 55  ? 25.733  -15.625 -9.170  1.00 14.52 ? 55   VAL B CA  1 
ATOM   3774 C C   . VAL B 1 55  ? 26.466  -16.782 -8.491  1.00 14.62 ? 55   VAL B C   1 
ATOM   3775 O O   . VAL B 1 55  ? 26.857  -17.725 -9.155  1.00 15.15 ? 55   VAL B O   1 
ATOM   3776 C CB  . VAL B 1 55  ? 24.316  -16.057 -9.493  1.00 14.09 ? 55   VAL B CB  1 
ATOM   3777 C CG1 . VAL B 1 55  ? 24.287  -17.053 -10.709 1.00 13.39 ? 55   VAL B CG1 1 
ATOM   3778 C CG2 . VAL B 1 55  ? 23.677  -16.660 -8.266  1.00 13.76 ? 55   VAL B CG2 1 
ATOM   3779 N N   . LEU B 1 56  ? 26.676  -16.689 -7.184  1.00 14.71 ? 56   LEU B N   1 
ATOM   3780 C CA  . LEU B 1 56  ? 27.187  -17.820 -6.398  1.00 14.60 ? 56   LEU B CA  1 
ATOM   3781 C C   . LEU B 1 56  ? 26.054  -18.345 -5.525  1.00 15.27 ? 56   LEU B C   1 
ATOM   3782 O O   . LEU B 1 56  ? 25.444  -17.584 -4.741  1.00 15.86 ? 56   LEU B O   1 
ATOM   3783 C CB  . LEU B 1 56  ? 28.420  -17.422 -5.591  1.00 14.44 ? 56   LEU B CB  1 
ATOM   3784 C CG  . LEU B 1 56  ? 28.928  -18.478 -4.570  1.00 13.78 ? 56   LEU B CG  1 
ATOM   3785 C CD1 . LEU B 1 56  ? 29.662  -19.652 -5.224  1.00 6.73  ? 56   LEU B CD1 1 
ATOM   3786 C CD2 . LEU B 1 56  ? 29.815  -17.763 -3.618  1.00 10.84 ? 56   LEU B CD2 1 
ATOM   3787 N N   . SER B 1 57  ? 25.698  -19.622 -5.702  1.00 16.04 ? 57   SER B N   1 
ATOM   3788 C CA  . SER B 1 57  ? 24.484  -20.124 -5.068  1.00 15.83 ? 57   SER B CA  1 
ATOM   3789 C C   . SER B 1 57  ? 24.787  -21.283 -4.163  1.00 16.89 ? 57   SER B C   1 
ATOM   3790 O O   . SER B 1 57  ? 25.657  -22.107 -4.475  1.00 18.31 ? 57   SER B O   1 
ATOM   3791 C CB  . SER B 1 57  ? 23.447  -20.505 -6.149  1.00 16.80 ? 57   SER B CB  1 
ATOM   3792 O OG  . SER B 1 57  ? 22.212  -20.978 -5.618  1.00 13.60 ? 57   SER B OG  1 
ATOM   3793 N N   . ARG B 1 58  ? 24.091  -21.362 -3.022  1.00 17.53 ? 58   ARG B N   1 
ATOM   3794 C CA  . ARG B 1 58  ? 24.151  -22.577 -2.179  1.00 17.09 ? 58   ARG B CA  1 
ATOM   3795 C C   . ARG B 1 58  ? 23.264  -23.634 -2.812  1.00 17.36 ? 58   ARG B C   1 
ATOM   3796 O O   . ARG B 1 58  ? 22.453  -23.281 -3.669  1.00 16.86 ? 58   ARG B O   1 
ATOM   3797 C CB  . ARG B 1 58  ? 23.648  -22.279 -0.760  1.00 17.61 ? 58   ARG B CB  1 
ATOM   3798 C CG  . ARG B 1 58  ? 23.890  -23.426 0.229   1.00 15.23 ? 58   ARG B CG  1 
ATOM   3799 C CD  . ARG B 1 58  ? 23.746  -23.000 1.650   1.00 13.18 ? 58   ARG B CD  1 
ATOM   3800 N NE  . ARG B 1 58  ? 23.713  -24.209 2.440   1.00 15.54 ? 58   ARG B NE  1 
ATOM   3801 C CZ  . ARG B 1 58  ? 22.993  -24.387 3.538   1.00 11.62 ? 58   ARG B CZ  1 
ATOM   3802 N NH1 . ARG B 1 58  ? 22.250  -23.409 4.029   1.00 10.21 ? 58   ARG B NH1 1 
ATOM   3803 N NH2 . ARG B 1 58  ? 23.019  -25.573 4.127   1.00 9.24  ? 58   ARG B NH2 1 
ATOM   3804 N N   . HIS B 1 59  ? 23.418  -24.917 -2.432  1.00 17.20 ? 59   HIS B N   1 
ATOM   3805 C CA  . HIS B 1 59  ? 22.379  -25.912 -2.749  1.00 17.00 ? 59   HIS B CA  1 
ATOM   3806 C C   . HIS B 1 59  ? 21.089  -25.664 -1.990  1.00 16.94 ? 59   HIS B C   1 
ATOM   3807 O O   . HIS B 1 59  ? 21.026  -24.824 -1.095  1.00 16.43 ? 59   HIS B O   1 
ATOM   3808 C CB  . HIS B 1 59  ? 22.814  -27.328 -2.442  1.00 17.41 ? 59   HIS B CB  1 
ATOM   3809 C CG  . HIS B 1 59  ? 23.150  -27.543 -1.011  1.00 16.41 ? 59   HIS B CG  1 
ATOM   3810 N ND1 . HIS B 1 59  ? 22.186  -27.688 -0.030  1.00 15.36 ? 59   HIS B ND1 1 
ATOM   3811 C CD2 . HIS B 1 59  ? 24.350  -27.650 -0.398  1.00 11.79 ? 59   HIS B CD2 1 
ATOM   3812 C CE1 . HIS B 1 59  ? 22.786  -27.859 1.135   1.00 13.65 ? 59   HIS B CE1 1 
ATOM   3813 N NE2 . HIS B 1 59  ? 24.096  -27.856 0.934   1.00 13.79 ? 59   HIS B NE2 1 
ATOM   3814 N N   . GLY B 1 60  ? 20.055  -26.406 -2.361  1.00 17.35 ? 60   GLY B N   1 
ATOM   3815 C CA  . GLY B 1 60  ? 18.727  -26.180 -1.814  1.00 17.62 ? 60   GLY B CA  1 
ATOM   3816 C C   . GLY B 1 60  ? 18.590  -26.950 -0.529  1.00 18.56 ? 60   GLY B C   1 
ATOM   3817 O O   . GLY B 1 60  ? 19.526  -27.651 -0.127  1.00 18.51 ? 60   GLY B O   1 
ATOM   3818 N N   . ALA B 1 61  ? 17.440  -26.772 0.119   1.00 19.08 ? 61   ALA B N   1 
ATOM   3819 C CA  . ALA B 1 61  ? 17.052  -27.508 1.283   1.00 20.34 ? 61   ALA B CA  1 
ATOM   3820 C C   . ALA B 1 61  ? 17.278  -29.021 1.124   1.00 22.05 ? 61   ALA B C   1 
ATOM   3821 O O   . ALA B 1 61  ? 16.973  -29.609 0.090   1.00 22.79 ? 61   ALA B O   1 
ATOM   3822 C CB  . ALA B 1 61  ? 15.584  -27.194 1.605   1.00 19.82 ? 61   ALA B CB  1 
ATOM   3823 N N   . ARG B 1 62  ? 17.845  -29.648 2.149   1.00 23.70 ? 62   ARG B N   1 
ATOM   3824 C CA  . ARG B 1 62  ? 18.212  -31.054 2.089   1.00 24.86 ? 62   ARG B CA  1 
ATOM   3825 C C   . ARG B 1 62  ? 17.683  -31.791 3.307   1.00 25.32 ? 62   ARG B C   1 
ATOM   3826 O O   . ARG B 1 62  ? 17.397  -31.208 4.373   1.00 26.57 ? 62   ARG B O   1 
ATOM   3827 C CB  . ARG B 1 62  ? 19.728  -31.227 2.021   1.00 24.98 ? 62   ARG B CB  1 
ATOM   3828 C CG  . ARG B 1 62  ? 20.471  -30.702 3.279   1.00 26.16 ? 62   ARG B CG  1 
ATOM   3829 C CD  . ARG B 1 62  ? 21.891  -31.276 3.398   1.00 26.85 ? 62   ARG B CD  1 
ATOM   3830 N NE  . ARG B 1 62  ? 22.706  -30.770 4.533   1.00 28.97 ? 62   ARG B NE  1 
ATOM   3831 C CZ  . ARG B 1 62  ? 22.486  -30.994 5.845   1.00 30.44 ? 62   ARG B CZ  1 
ATOM   3832 N NH1 . ARG B 1 62  ? 21.401  -31.654 6.276   1.00 31.88 ? 62   ARG B NH1 1 
ATOM   3833 N NH2 . ARG B 1 62  ? 23.324  -30.503 6.760   1.00 29.71 ? 62   ARG B NH2 1 
ATOM   3834 N N   . TYR B 1 63  ? 17.565  -33.089 3.151   1.00 25.64 ? 63   TYR B N   1 
ATOM   3835 C CA  . TYR B 1 63  ? 17.367  -33.976 4.270   1.00 26.49 ? 63   TYR B CA  1 
ATOM   3836 C C   . TYR B 1 63  ? 18.570  -33.911 5.215   1.00 27.54 ? 63   TYR B C   1 
ATOM   3837 O O   . TYR B 1 63  ? 19.662  -33.470 4.824   1.00 27.20 ? 63   TYR B O   1 
ATOM   3838 C CB  . TYR B 1 63  ? 17.199  -35.374 3.734   1.00 26.30 ? 63   TYR B CB  1 
ATOM   3839 C CG  . TYR B 1 63  ? 15.891  -35.597 3.003   1.00 25.49 ? 63   TYR B CG  1 
ATOM   3840 C CD1 . TYR B 1 63  ? 14.668  -35.299 3.626   1.00 23.02 ? 63   TYR B CD1 1 
ATOM   3841 C CD2 . TYR B 1 63  ? 15.872  -36.104 1.689   1.00 25.08 ? 63   TYR B CD2 1 
ATOM   3842 C CE1 . TYR B 1 63  ? 13.462  -35.505 2.989   1.00 23.86 ? 63   TYR B CE1 1 
ATOM   3843 C CE2 . TYR B 1 63  ? 14.636  -36.331 1.021   1.00 26.42 ? 63   TYR B CE2 1 
ATOM   3844 C CZ  . TYR B 1 63  ? 13.445  -36.021 1.701   1.00 27.07 ? 63   TYR B CZ  1 
ATOM   3845 O OH  . TYR B 1 63  ? 12.234  -36.217 1.103   1.00 31.70 ? 63   TYR B OH  1 
ATOM   3846 N N   . PRO B 1 64  ? 18.373  -34.319 6.477   1.00 28.46 ? 64   PRO B N   1 
ATOM   3847 C CA  . PRO B 1 64  ? 19.499  -34.342 7.420   1.00 29.38 ? 64   PRO B CA  1 
ATOM   3848 C C   . PRO B 1 64  ? 20.570  -35.327 6.953   1.00 30.33 ? 64   PRO B C   1 
ATOM   3849 O O   . PRO B 1 64  ? 20.232  -36.306 6.301   1.00 30.27 ? 64   PRO B O   1 
ATOM   3850 C CB  . PRO B 1 64  ? 18.847  -34.835 8.712   1.00 29.32 ? 64   PRO B CB  1 
ATOM   3851 C CG  . PRO B 1 64  ? 17.351  -34.613 8.534   1.00 28.61 ? 64   PRO B CG  1 
ATOM   3852 C CD  . PRO B 1 64  ? 17.118  -34.803 7.083   1.00 28.43 ? 64   PRO B CD  1 
ATOM   3853 N N   . THR B 1 65  ? 21.837  -35.096 7.258   1.00 31.70 ? 65   THR B N   1 
ATOM   3854 C CA  . THR B 1 65  ? 22.839  -36.052 6.816   1.00 34.25 ? 65   THR B CA  1 
ATOM   3855 C C   . THR B 1 65  ? 22.594  -37.378 7.516   1.00 35.78 ? 65   THR B C   1 
ATOM   3856 O O   . THR B 1 65  ? 21.848  -37.427 8.497   1.00 36.61 ? 65   THR B O   1 
ATOM   3857 C CB  . THR B 1 65  ? 24.278  -35.617 7.094   1.00 34.20 ? 65   THR B CB  1 
ATOM   3858 O OG1 . THR B 1 65  ? 24.634  -36.055 8.403   1.00 36.72 ? 65   THR B OG1 1 
ATOM   3859 C CG2 . THR B 1 65  ? 24.462  -34.097 6.978   1.00 34.45 ? 65   THR B CG2 1 
ATOM   3860 N N   . ASP B 1 66  ? 23.201  -38.457 7.016   1.00 37.30 ? 66   ASP B N   1 
ATOM   3861 C CA  . ASP B 1 66  ? 22.961  -39.794 7.568   1.00 38.82 ? 66   ASP B CA  1 
ATOM   3862 C C   . ASP B 1 66  ? 23.293  -39.890 9.073   1.00 39.17 ? 66   ASP B C   1 
ATOM   3863 O O   . ASP B 1 66  ? 22.476  -40.334 9.872   1.00 39.03 ? 66   ASP B O   1 
ATOM   3864 C CB  . ASP B 1 66  ? 23.746  -40.832 6.788   1.00 39.38 ? 66   ASP B CB  1 
ATOM   3865 C CG  . ASP B 1 66  ? 23.313  -42.237 7.110   1.00 41.05 ? 66   ASP B CG  1 
ATOM   3866 O OD1 . ASP B 1 66  ? 22.111  -42.538 6.890   1.00 44.48 ? 66   ASP B OD1 1 
ATOM   3867 O OD2 . ASP B 1 66  ? 24.163  -43.030 7.585   1.00 40.86 ? 66   ASP B OD2 1 
ATOM   3868 N N   . SER B 1 67  ? 24.500  -39.456 9.427   1.00 39.96 ? 67   SER B N   1 
ATOM   3869 C CA  . SER B 1 67  ? 24.915  -39.197 10.806  1.00 40.77 ? 67   SER B CA  1 
ATOM   3870 C C   . SER B 1 67  ? 23.773  -38.641 11.677  1.00 41.16 ? 67   SER B C   1 
ATOM   3871 O O   . SER B 1 67  ? 23.248  -39.341 12.540  1.00 41.03 ? 67   SER B O   1 
ATOM   3872 C CB  . SER B 1 67  ? 26.065  -38.191 10.765  1.00 41.04 ? 67   SER B CB  1 
ATOM   3873 O OG  . SER B 1 67  ? 27.005  -38.438 11.777  1.00 42.46 ? 67   SER B OG  1 
ATOM   3874 N N   . LYS B 1 68  ? 23.375  -37.391 11.394  1.00 41.50 ? 68   LYS B N   1 
ATOM   3875 C CA  . LYS B 1 68  ? 22.452  -36.602 12.221  1.00 41.18 ? 68   LYS B CA  1 
ATOM   3876 C C   . LYS B 1 68  ? 21.076  -37.216 12.328  1.00 41.23 ? 68   LYS B C   1 
ATOM   3877 O O   . LYS B 1 68  ? 20.451  -37.177 13.400  1.00 40.61 ? 68   LYS B O   1 
ATOM   3878 C CB  . LYS B 1 68  ? 22.322  -35.165 11.693  1.00 41.10 ? 68   LYS B CB  1 
ATOM   3879 C CG  . LYS B 1 68  ? 23.606  -34.329 11.729  1.00 40.65 ? 68   LYS B CG  1 
ATOM   3880 C CD  . LYS B 1 68  ? 23.819  -33.743 13.105  1.00 41.56 ? 68   LYS B CD  1 
ATOM   3881 C CE  . LYS B 1 68  ? 24.671  -32.484 13.088  1.00 41.26 ? 68   LYS B CE  1 
ATOM   3882 N NZ  . LYS B 1 68  ? 24.145  -31.620 14.191  1.00 43.76 ? 68   LYS B NZ  1 
ATOM   3883 N N   . GLY B 1 69  ? 20.607  -37.771 11.214  1.00 41.49 ? 69   GLY B N   1 
ATOM   3884 C CA  . GLY B 1 69  ? 19.305  -38.435 11.162  1.00 41.55 ? 69   GLY B CA  1 
ATOM   3885 C C   . GLY B 1 69  ? 19.243  -39.663 12.055  1.00 42.05 ? 69   GLY B C   1 
ATOM   3886 O O   . GLY B 1 69  ? 18.232  -39.882 12.711  1.00 41.55 ? 69   GLY B O   1 
ATOM   3887 N N   . LYS B 1 70  ? 20.317  -40.471 12.058  1.00 42.72 ? 70   LYS B N   1 
ATOM   3888 C CA  . LYS B 1 70  ? 20.483  -41.607 12.992  1.00 43.34 ? 70   LYS B CA  1 
ATOM   3889 C C   . LYS B 1 70  ? 20.126  -41.081 14.388  1.00 43.17 ? 70   LYS B C   1 
ATOM   3890 O O   . LYS B 1 70  ? 19.147  -41.514 15.018  1.00 43.25 ? 70   LYS B O   1 
ATOM   3891 C CB  . LYS B 1 70  ? 21.945  -42.112 13.047  1.00 43.72 ? 70   LYS B CB  1 
ATOM   3892 C CG  . LYS B 1 70  ? 22.596  -42.573 11.745  1.00 44.64 ? 70   LYS B CG  1 
ATOM   3893 C CD  . LYS B 1 70  ? 22.355  -44.051 11.496  1.00 45.66 ? 70   LYS B CD  1 
ATOM   3894 C CE  . LYS B 1 70  ? 22.815  -44.457 10.120  1.00 44.23 ? 70   LYS B CE  1 
ATOM   3895 N NZ  . LYS B 1 70  ? 22.320  -45.815 9.821   1.00 45.73 ? 70   LYS B NZ  1 
ATOM   3896 N N   . LYS B 1 71  ? 20.927  -40.120 14.835  1.00 42.38 ? 71   LYS B N   1 
ATOM   3897 C CA  . LYS B 1 71  ? 20.765  -39.505 16.147  1.00 41.70 ? 71   LYS B CA  1 
ATOM   3898 C C   . LYS B 1 71  ? 19.338  -38.981 16.400  1.00 41.03 ? 71   LYS B C   1 
ATOM   3899 O O   . LYS B 1 71  ? 18.732  -39.354 17.391  1.00 41.56 ? 71   LYS B O   1 
ATOM   3900 C CB  . LYS B 1 71  ? 21.881  -38.468 16.392  1.00 41.19 ? 71   LYS B CB  1 
ATOM   3901 C CG  . LYS B 1 71  ? 23.266  -39.128 16.345  1.00 40.83 ? 71   LYS B CG  1 
ATOM   3902 C CD  . LYS B 1 71  ? 24.420  -38.167 16.188  1.00 41.45 ? 71   LYS B CD  1 
ATOM   3903 C CE  . LYS B 1 71  ? 25.683  -38.929 15.785  1.00 42.59 ? 71   LYS B CE  1 
ATOM   3904 N NZ  . LYS B 1 71  ? 26.925  -38.103 15.866  1.00 43.43 ? 71   LYS B NZ  1 
ATOM   3905 N N   . TYR B 1 72  ? 18.791  -38.179 15.490  1.00 40.35 ? 72   TYR B N   1 
ATOM   3906 C CA  . TYR B 1 72  ? 17.435  -37.645 15.648  1.00 39.46 ? 72   TYR B CA  1 
ATOM   3907 C C   . TYR B 1 72  ? 16.442  -38.776 15.881  1.00 39.12 ? 72   TYR B C   1 
ATOM   3908 O O   . TYR B 1 72  ? 15.644  -38.735 16.811  1.00 38.13 ? 72   TYR B O   1 
ATOM   3909 C CB  . TYR B 1 72  ? 16.948  -36.840 14.416  1.00 39.49 ? 72   TYR B CB  1 
ATOM   3910 C CG  . TYR B 1 72  ? 17.706  -35.582 14.033  1.00 38.00 ? 72   TYR B CG  1 
ATOM   3911 C CD1 . TYR B 1 72  ? 18.355  -34.820 14.977  1.00 37.43 ? 72   TYR B CD1 1 
ATOM   3912 C CD2 . TYR B 1 72  ? 17.729  -35.135 12.711  1.00 37.35 ? 72   TYR B CD2 1 
ATOM   3913 C CE1 . TYR B 1 72  ? 19.040  -33.671 14.621  1.00 36.54 ? 72   TYR B CE1 1 
ATOM   3914 C CE2 . TYR B 1 72  ? 18.411  -33.977 12.355  1.00 35.11 ? 72   TYR B CE2 1 
ATOM   3915 C CZ  . TYR B 1 72  ? 19.055  -33.253 13.321  1.00 34.75 ? 72   TYR B CZ  1 
ATOM   3916 O OH  . TYR B 1 72  ? 19.747  -32.108 13.010  1.00 33.13 ? 72   TYR B OH  1 
ATOM   3917 N N   . SER B 1 73  ? 16.502  -39.762 14.988  1.00 39.37 ? 73   SER B N   1 
ATOM   3918 C CA  . SER B 1 73  ? 15.687  -40.972 15.025  1.00 39.55 ? 73   SER B CA  1 
ATOM   3919 C C   . SER B 1 73  ? 15.887  -41.713 16.371  1.00 39.22 ? 73   SER B C   1 
ATOM   3920 O O   . SER B 1 73  ? 14.907  -41.999 17.075  1.00 38.43 ? 73   SER B O   1 
ATOM   3921 C CB  . SER B 1 73  ? 16.031  -41.842 13.799  1.00 39.58 ? 73   SER B CB  1 
ATOM   3922 O OG  . SER B 1 73  ? 15.419  -43.118 13.833  1.00 41.78 ? 73   SER B OG  1 
ATOM   3923 N N   . ALA B 1 74  ? 17.153  -41.958 16.731  1.00 38.95 ? 74   ALA B N   1 
ATOM   3924 C CA  . ALA B 1 74  ? 17.524  -42.536 18.034  1.00 39.29 ? 74   ALA B CA  1 
ATOM   3925 C C   . ALA B 1 74  ? 16.966  -41.746 19.193  1.00 39.27 ? 74   ALA B C   1 
ATOM   3926 O O   . ALA B 1 74  ? 16.391  -42.322 20.110  1.00 39.78 ? 74   ALA B O   1 
ATOM   3927 C CB  . ALA B 1 74  ? 19.051  -42.654 18.193  1.00 38.95 ? 74   ALA B CB  1 
ATOM   3928 N N   . LEU B 1 75  ? 17.154  -40.433 19.165  1.00 39.13 ? 75   LEU B N   1 
ATOM   3929 C CA  . LEU B 1 75  ? 16.684  -39.596 20.257  1.00 39.21 ? 75   LEU B CA  1 
ATOM   3930 C C   . LEU B 1 75  ? 15.181  -39.769 20.432  1.00 39.68 ? 75   LEU B C   1 
ATOM   3931 O O   . LEU B 1 75  ? 14.698  -40.003 21.548  1.00 39.61 ? 75   LEU B O   1 
ATOM   3932 C CB  . LEU B 1 75  ? 17.063  -38.118 20.046  1.00 38.84 ? 75   LEU B CB  1 
ATOM   3933 C CG  . LEU B 1 75  ? 16.600  -37.042 21.049  1.00 38.51 ? 75   LEU B CG  1 
ATOM   3934 C CD1 . LEU B 1 75  ? 16.925  -37.424 22.487  1.00 37.69 ? 75   LEU B CD1 1 
ATOM   3935 C CD2 . LEU B 1 75  ? 17.182  -35.680 20.748  1.00 37.59 ? 75   LEU B CD2 1 
ATOM   3936 N N   . ILE B 1 76  ? 14.437  -39.674 19.339  1.00 40.35 ? 76   ILE B N   1 
ATOM   3937 C CA  . ILE B 1 76  ? 12.981  -39.678 19.460  1.00 41.09 ? 76   ILE B CA  1 
ATOM   3938 C C   . ILE B 1 76  ? 12.476  -41.031 19.941  1.00 41.62 ? 76   ILE B C   1 
ATOM   3939 O O   . ILE B 1 76  ? 11.451  -41.083 20.614  1.00 41.81 ? 76   ILE B O   1 
ATOM   3940 C CB  . ILE B 1 76  ? 12.254  -39.204 18.179  1.00 40.78 ? 76   ILE B CB  1 
ATOM   3941 C CG1 . ILE B 1 76  ? 12.778  -37.841 17.767  1.00 41.14 ? 76   ILE B CG1 1 
ATOM   3942 C CG2 . ILE B 1 76  ? 10.768  -39.058 18.433  1.00 40.95 ? 76   ILE B CG2 1 
ATOM   3943 C CD1 . ILE B 1 76  ? 12.824  -37.633 16.267  1.00 42.54 ? 76   ILE B CD1 1 
ATOM   3944 N N   . GLU B 1 77  ? 13.196  -42.110 19.635  1.00 42.14 ? 77   GLU B N   1 
ATOM   3945 C CA  . GLU B 1 77  ? 12.837  -43.416 20.183  1.00 43.58 ? 77   GLU B CA  1 
ATOM   3946 C C   . GLU B 1 77  ? 12.988  -43.420 21.719  1.00 43.67 ? 77   GLU B C   1 
ATOM   3947 O O   . GLU B 1 77  ? 12.084  -43.831 22.447  1.00 43.70 ? 77   GLU B O   1 
ATOM   3948 C CB  . GLU B 1 77  ? 13.671  -44.544 19.554  1.00 44.03 ? 77   GLU B CB  1 
ATOM   3949 C CG  . GLU B 1 77  ? 13.453  -44.729 18.061  1.00 46.32 ? 77   GLU B CG  1 
ATOM   3950 C CD  . GLU B 1 77  ? 13.500  -46.183 17.667  1.00 51.32 ? 77   GLU B CD  1 
ATOM   3951 O OE1 . GLU B 1 77  ? 14.516  -46.846 18.006  1.00 52.08 ? 77   GLU B OE1 1 
ATOM   3952 O OE2 . GLU B 1 77  ? 12.511  -46.676 17.049  1.00 52.36 ? 77   GLU B OE2 1 
ATOM   3953 N N   . GLU B 1 78  ? 14.139  -42.952 22.195  1.00 44.01 ? 78   GLU B N   1 
ATOM   3954 C CA  . GLU B 1 78  ? 14.421  -42.858 23.627  1.00 44.13 ? 78   GLU B CA  1 
ATOM   3955 C C   . GLU B 1 78  ? 13.414  -41.974 24.336  1.00 43.84 ? 78   GLU B C   1 
ATOM   3956 O O   . GLU B 1 78  ? 12.987  -42.275 25.449  1.00 43.35 ? 78   GLU B O   1 
ATOM   3957 C CB  . GLU B 1 78  ? 15.829  -42.334 23.864  1.00 44.26 ? 78   GLU B CB  1 
ATOM   3958 C CG  . GLU B 1 78  ? 16.894  -43.381 23.650  1.00 46.62 ? 78   GLU B CG  1 
ATOM   3959 C CD  . GLU B 1 78  ? 18.304  -42.893 23.970  1.00 50.70 ? 78   GLU B CD  1 
ATOM   3960 O OE1 . GLU B 1 78  ? 19.233  -43.478 23.374  1.00 54.09 ? 78   GLU B OE1 1 
ATOM   3961 O OE2 . GLU B 1 78  ? 18.507  -41.956 24.799  1.00 50.87 ? 78   GLU B OE2 1 
ATOM   3962 N N   . ILE B 1 79  ? 13.032  -40.881 23.682  1.00 43.60 ? 79   ILE B N   1 
ATOM   3963 C CA  . ILE B 1 79  ? 11.989  -40.038 24.218  1.00 43.69 ? 79   ILE B CA  1 
ATOM   3964 C C   . ILE B 1 79  ? 10.680  -40.829 24.399  1.00 44.26 ? 79   ILE B C   1 
ATOM   3965 O O   . ILE B 1 79  ? 10.024  -40.710 25.421  1.00 43.76 ? 79   ILE B O   1 
ATOM   3966 C CB  . ILE B 1 79  ? 11.837  -38.724 23.408  1.00 43.50 ? 79   ILE B CB  1 
ATOM   3967 C CG1 . ILE B 1 79  ? 13.045  -37.829 23.702  1.00 42.26 ? 79   ILE B CG1 1 
ATOM   3968 C CG2 . ILE B 1 79  ? 10.554  -37.991 23.776  1.00 42.79 ? 79   ILE B CG2 1 
ATOM   3969 C CD1 . ILE B 1 79  ? 13.310  -36.764 22.698  1.00 40.88 ? 79   ILE B CD1 1 
ATOM   3970 N N   . GLN B 1 80  ? 10.356  -41.678 23.432  1.00 45.31 ? 80   GLN B N   1 
ATOM   3971 C CA  . GLN B 1 80  ? 9.120   -42.465 23.447  1.00 46.38 ? 80   GLN B CA  1 
ATOM   3972 C C   . GLN B 1 80  ? 9.180   -43.681 24.384  1.00 46.51 ? 80   GLN B C   1 
ATOM   3973 O O   . GLN B 1 80  ? 8.165   -44.104 24.929  1.00 45.74 ? 80   GLN B O   1 
ATOM   3974 C CB  . GLN B 1 80  ? 8.757   -42.896 22.019  1.00 46.63 ? 80   GLN B CB  1 
ATOM   3975 C CG  . GLN B 1 80  ? 8.312   -41.734 21.123  1.00 47.88 ? 80   GLN B CG  1 
ATOM   3976 C CD  . GLN B 1 80  ? 8.155   -42.098 19.644  1.00 49.03 ? 80   GLN B CD  1 
ATOM   3977 O OE1 . GLN B 1 80  ? 8.689   -43.111 19.160  1.00 48.21 ? 80   GLN B OE1 1 
ATOM   3978 N NE2 . GLN B 1 80  ? 7.411   -41.263 18.923  1.00 48.58 ? 80   GLN B NE2 1 
ATOM   3979 N N   . GLN B 1 81  ? 10.371  -44.240 24.566  1.00 47.27 ? 81   GLN B N   1 
ATOM   3980 C CA  . GLN B 1 81  ? 10.538  -45.340 25.514  1.00 48.13 ? 81   GLN B CA  1 
ATOM   3981 C C   . GLN B 1 81  ? 10.420  -44.892 26.979  1.00 47.96 ? 81   GLN B C   1 
ATOM   3982 O O   . GLN B 1 81  ? 9.848   -45.614 27.786  1.00 48.13 ? 81   GLN B O   1 
ATOM   3983 C CB  . GLN B 1 81  ? 11.864  -46.054 25.298  1.00 48.44 ? 81   GLN B CB  1 
ATOM   3984 C CG  . GLN B 1 81  ? 11.811  -47.146 24.273  1.00 50.99 ? 81   GLN B CG  1 
ATOM   3985 C CD  . GLN B 1 81  ? 13.211  -47.559 23.825  1.00 55.54 ? 81   GLN B CD  1 
ATOM   3986 O OE1 . GLN B 1 81  ? 14.175  -47.561 24.625  1.00 56.22 ? 81   GLN B OE1 1 
ATOM   3987 N NE2 . GLN B 1 81  ? 13.337  -47.911 22.536  1.00 56.99 ? 81   GLN B NE2 1 
ATOM   3988 N N   . ASN B 1 82  ? 10.920  -43.695 27.303  1.00 47.63 ? 82   ASN B N   1 
ATOM   3989 C CA  . ASN B 1 82  ? 11.102  -43.276 28.694  1.00 47.34 ? 82   ASN B CA  1 
ATOM   3990 C C   . ASN B 1 82  ? 9.981   -42.430 29.309  1.00 48.10 ? 82   ASN B C   1 
ATOM   3991 O O   . ASN B 1 82  ? 9.648   -42.599 30.488  1.00 48.31 ? 82   ASN B O   1 
ATOM   3992 C CB  . ASN B 1 82  ? 12.464  -42.579 28.905  1.00 47.01 ? 82   ASN B CB  1 
ATOM   3993 C CG  . ASN B 1 82  ? 13.670  -43.448 28.509  1.00 44.96 ? 82   ASN B CG  1 
ATOM   3994 O OD1 . ASN B 1 82  ? 13.536  -44.599 28.070  1.00 42.87 ? 82   ASN B OD1 1 
ATOM   3995 N ND2 . ASN B 1 82  ? 14.858  -42.874 28.660  1.00 43.98 ? 82   ASN B ND2 1 
ATOM   3996 N N   . ALA B 1 83  ? 9.401   -41.519 28.534  1.00 48.71 ? 83   ALA B N   1 
ATOM   3997 C CA  . ALA B 1 83  ? 8.462   -40.531 29.101  1.00 49.32 ? 83   ALA B CA  1 
ATOM   3998 C C   . ALA B 1 83  ? 7.093   -41.119 29.482  1.00 50.18 ? 83   ALA B C   1 
ATOM   3999 O O   . ALA B 1 83  ? 6.664   -42.137 28.932  1.00 50.00 ? 83   ALA B O   1 
ATOM   4000 C CB  . ALA B 1 83  ? 8.302   -39.329 28.166  1.00 48.82 ? 83   ALA B CB  1 
ATOM   4001 N N   . THR B 1 84  ? 6.416   -40.474 30.429  1.00 51.30 ? 84   THR B N   1 
ATOM   4002 C CA  . THR B 1 84  ? 5.131   -40.984 30.922  1.00 52.74 ? 84   THR B CA  1 
ATOM   4003 C C   . THR B 1 84  ? 3.959   -40.052 30.593  1.00 53.34 ? 84   THR B C   1 
ATOM   4004 O O   . THR B 1 84  ? 2.798   -40.478 30.584  1.00 53.71 ? 84   THR B O   1 
ATOM   4005 C CB  . THR B 1 84  ? 5.175   -41.251 32.441  1.00 52.82 ? 84   THR B CB  1 
ATOM   4006 O OG1 . THR B 1 84  ? 5.474   -40.019 33.120  1.00 52.75 ? 84   THR B OG1 1 
ATOM   4007 C CG2 . THR B 1 84  ? 6.246   -42.332 32.777  1.00 52.54 ? 84   THR B CG2 1 
ATOM   4008 N N   . THR B 1 85  ? 4.265   -38.782 30.340  1.00 53.98 ? 85   THR B N   1 
ATOM   4009 C CA  . THR B 1 85  ? 3.249   -37.830 29.866  1.00 54.68 ? 85   THR B CA  1 
ATOM   4010 C C   . THR B 1 85  ? 3.628   -37.053 28.594  1.00 54.42 ? 85   THR B C   1 
ATOM   4011 O O   . THR B 1 85  ? 4.405   -36.081 28.635  1.00 54.57 ? 85   THR B O   1 
ATOM   4012 C CB  . THR B 1 85  ? 2.786   -36.816 30.966  1.00 54.87 ? 85   THR B CB  1 
ATOM   4013 O OG1 . THR B 1 85  ? 3.922   -36.213 31.601  1.00 55.84 ? 85   THR B OG1 1 
ATOM   4014 C CG2 . THR B 1 85  ? 1.945   -37.502 31.993  1.00 55.38 ? 85   THR B CG2 1 
ATOM   4015 N N   . PHE B 1 86  ? 3.062   -37.484 27.471  1.00 53.91 ? 86   PHE B N   1 
ATOM   4016 C CA  . PHE B 1 86  ? 3.090   -36.677 26.271  1.00 53.54 ? 86   PHE B CA  1 
ATOM   4017 C C   . PHE B 1 86  ? 1.750   -36.007 26.186  1.00 53.22 ? 86   PHE B C   1 
ATOM   4018 O O   . PHE B 1 86  ? 0.843   -36.531 25.529  1.00 53.14 ? 86   PHE B O   1 
ATOM   4019 C CB  . PHE B 1 86  ? 3.262   -37.524 25.016  1.00 53.60 ? 86   PHE B CB  1 
ATOM   4020 C CG  . PHE B 1 86  ? 4.363   -38.516 25.088  1.00 53.32 ? 86   PHE B CG  1 
ATOM   4021 C CD1 . PHE B 1 86  ? 5.638   -38.183 24.670  1.00 52.80 ? 86   PHE B CD1 1 
ATOM   4022 C CD2 . PHE B 1 86  ? 4.115   -39.805 25.536  1.00 54.36 ? 86   PHE B CD2 1 
ATOM   4023 C CE1 . PHE B 1 86  ? 6.660   -39.118 24.712  1.00 53.40 ? 86   PHE B CE1 1 
ATOM   4024 C CE2 . PHE B 1 86  ? 5.129   -40.752 25.586  1.00 54.78 ? 86   PHE B CE2 1 
ATOM   4025 C CZ  . PHE B 1 86  ? 6.408   -40.406 25.165  1.00 54.23 ? 86   PHE B CZ  1 
ATOM   4026 N N   . ASP B 1 87  ? 1.600   -34.871 26.861  1.00 52.81 ? 87   ASP B N   1 
ATOM   4027 C CA  . ASP B 1 87  ? 0.399   -34.069 26.646  1.00 52.98 ? 87   ASP B CA  1 
ATOM   4028 C C   . ASP B 1 87  ? 0.634   -32.550 26.447  1.00 52.61 ? 87   ASP B C   1 
ATOM   4029 O O   . ASP B 1 87  ? 1.784   -32.083 26.429  1.00 52.77 ? 87   ASP B O   1 
ATOM   4030 C CB  . ASP B 1 87  ? -0.705  -34.409 27.665  1.00 53.54 ? 87   ASP B CB  1 
ATOM   4031 C CG  . ASP B 1 87  ? -0.317  -34.096 29.103  1.00 54.57 ? 87   ASP B CG  1 
ATOM   4032 O OD1 . ASP B 1 87  ? 0.055   -32.934 29.383  1.00 54.77 ? 87   ASP B OD1 1 
ATOM   4033 O OD2 . ASP B 1 87  ? -0.429  -35.015 29.960  1.00 56.09 ? 87   ASP B OD2 1 
ATOM   4034 N N   . GLY B 1 88  ? -0.458  -31.800 26.270  1.00 51.97 ? 88   GLY B N   1 
ATOM   4035 C CA  . GLY B 1 88  ? -0.409  -30.438 25.718  1.00 50.93 ? 88   GLY B CA  1 
ATOM   4036 C C   . GLY B 1 88  ? 0.329   -30.446 24.383  1.00 50.05 ? 88   GLY B C   1 
ATOM   4037 O O   . GLY B 1 88  ? 0.103   -31.311 23.533  1.00 49.74 ? 88   GLY B O   1 
ATOM   4038 N N   . LYS B 1 89  ? 1.247   -29.498 24.222  1.00 49.34 ? 89   LYS B N   1 
ATOM   4039 C CA  . LYS B 1 89  ? 2.087   -29.410 23.015  1.00 48.21 ? 89   LYS B CA  1 
ATOM   4040 C C   . LYS B 1 89  ? 3.026   -30.607 22.808  1.00 47.17 ? 89   LYS B C   1 
ATOM   4041 O O   . LYS B 1 89  ? 3.671   -30.702 21.776  1.00 47.04 ? 89   LYS B O   1 
ATOM   4042 C CB  . LYS B 1 89  ? 2.859   -28.081 22.979  1.00 48.40 ? 89   LYS B CB  1 
ATOM   4043 C CG  . LYS B 1 89  ? 3.664   -27.754 24.238  1.00 48.98 ? 89   LYS B CG  1 
ATOM   4044 C CD  . LYS B 1 89  ? 3.830   -26.252 24.367  1.00 51.07 ? 89   LYS B CD  1 
ATOM   4045 C CE  . LYS B 1 89  ? 4.855   -25.873 25.438  1.00 52.85 ? 89   LYS B CE  1 
ATOM   4046 N NZ  . LYS B 1 89  ? 5.143   -24.398 25.438  1.00 51.49 ? 89   LYS B NZ  1 
ATOM   4047 N N   . TYR B 1 90  ? 3.064   -31.531 23.763  1.00 45.99 ? 90   TYR B N   1 
ATOM   4048 C CA  . TYR B 1 90  ? 3.932   -32.704 23.641  1.00 45.13 ? 90   TYR B CA  1 
ATOM   4049 C C   . TYR B 1 90  ? 3.254   -33.925 23.022  1.00 44.99 ? 90   TYR B C   1 
ATOM   4050 O O   . TYR B 1 90  ? 3.941   -34.859 22.619  1.00 44.97 ? 90   TYR B O   1 
ATOM   4051 C CB  . TYR B 1 90  ? 4.556   -33.091 24.999  1.00 44.62 ? 90   TYR B CB  1 
ATOM   4052 C CG  . TYR B 1 90  ? 5.465   -32.040 25.548  1.00 42.76 ? 90   TYR B CG  1 
ATOM   4053 C CD1 . TYR B 1 90  ? 6.807   -32.014 25.198  1.00 41.67 ? 90   TYR B CD1 1 
ATOM   4054 C CD2 . TYR B 1 90  ? 4.982   -31.048 26.406  1.00 41.59 ? 90   TYR B CD2 1 
ATOM   4055 C CE1 . TYR B 1 90  ? 7.659   -31.020 25.686  1.00 41.05 ? 90   TYR B CE1 1 
ATOM   4056 C CE2 . TYR B 1 90  ? 5.829   -30.056 26.916  1.00 40.99 ? 90   TYR B CE2 1 
ATOM   4057 C CZ  . TYR B 1 90  ? 7.166   -30.050 26.537  1.00 40.85 ? 90   TYR B CZ  1 
ATOM   4058 O OH  . TYR B 1 90  ? 8.012   -29.086 27.008  1.00 39.02 ? 90   TYR B OH  1 
ATOM   4059 N N   . ALA B 1 91  ? 1.924   -33.921 22.938  1.00 44.99 ? 91   ALA B N   1 
ATOM   4060 C CA  . ALA B 1 91  ? 1.176   -35.125 22.546  1.00 45.13 ? 91   ALA B CA  1 
ATOM   4061 C C   . ALA B 1 91  ? 1.748   -35.829 21.310  1.00 45.14 ? 91   ALA B C   1 
ATOM   4062 O O   . ALA B 1 91  ? 1.898   -37.068 21.294  1.00 44.78 ? 91   ALA B O   1 
ATOM   4063 C CB  . ALA B 1 91  ? -0.291  -34.808 22.363  1.00 45.17 ? 91   ALA B CB  1 
ATOM   4064 N N   . PHE B 1 92  ? 2.124   -35.018 20.315  1.00 45.38 ? 92   PHE B N   1 
ATOM   4065 C CA  . PHE B 1 92  ? 2.541   -35.495 18.986  1.00 45.29 ? 92   PHE B CA  1 
ATOM   4066 C C   . PHE B 1 92  ? 3.732   -36.432 19.042  1.00 45.58 ? 92   PHE B C   1 
ATOM   4067 O O   . PHE B 1 92  ? 3.894   -37.314 18.191  1.00 45.45 ? 92   PHE B O   1 
ATOM   4068 C CB  . PHE B 1 92  ? 2.831   -34.306 18.051  1.00 45.55 ? 92   PHE B CB  1 
ATOM   4069 C CG  . PHE B 1 92  ? 4.136   -33.604 18.330  1.00 44.05 ? 92   PHE B CG  1 
ATOM   4070 C CD1 . PHE B 1 92  ? 4.187   -32.524 19.203  1.00 42.93 ? 92   PHE B CD1 1 
ATOM   4071 C CD2 . PHE B 1 92  ? 5.314   -34.024 17.708  1.00 43.54 ? 92   PHE B CD2 1 
ATOM   4072 C CE1 . PHE B 1 92  ? 5.398   -31.867 19.463  1.00 42.70 ? 92   PHE B CE1 1 
ATOM   4073 C CE2 . PHE B 1 92  ? 6.537   -33.385 17.968  1.00 43.06 ? 92   PHE B CE2 1 
ATOM   4074 C CZ  . PHE B 1 92  ? 6.579   -32.308 18.849  1.00 42.78 ? 92   PHE B CZ  1 
ATOM   4075 N N   . LEU B 1 93  ? 4.560   -36.240 20.057  1.00 45.82 ? 93   LEU B N   1 
ATOM   4076 C CA  . LEU B 1 93  ? 5.750   -37.042 20.214  1.00 46.51 ? 93   LEU B CA  1 
ATOM   4077 C C   . LEU B 1 93  ? 5.459   -38.486 20.548  1.00 47.19 ? 93   LEU B C   1 
ATOM   4078 O O   . LEU B 1 93  ? 6.295   -39.357 20.306  1.00 46.84 ? 93   LEU B O   1 
ATOM   4079 C CB  . LEU B 1 93  ? 6.658   -36.455 21.281  1.00 46.36 ? 93   LEU B CB  1 
ATOM   4080 C CG  . LEU B 1 93  ? 7.612   -35.380 20.784  1.00 45.74 ? 93   LEU B CG  1 
ATOM   4081 C CD1 . LEU B 1 93  ? 8.174   -34.639 21.989  1.00 45.75 ? 93   LEU B CD1 1 
ATOM   4082 C CD2 . LEU B 1 93  ? 8.694   -36.023 19.962  1.00 42.53 ? 93   LEU B CD2 1 
ATOM   4083 N N   . LYS B 1 94  ? 4.280   -38.754 21.103  1.00 48.43 ? 94   LYS B N   1 
ATOM   4084 C CA  . LYS B 1 94  ? 3.965   -40.131 21.492  1.00 49.74 ? 94   LYS B CA  1 
ATOM   4085 C C   . LYS B 1 94  ? 4.099   -41.073 20.299  1.00 50.13 ? 94   LYS B C   1 
ATOM   4086 O O   . LYS B 1 94  ? 4.801   -42.112 20.380  1.00 50.15 ? 94   LYS B O   1 
ATOM   4087 C CB  . LYS B 1 94  ? 2.574   -40.260 22.139  1.00 49.99 ? 94   LYS B CB  1 
ATOM   4088 C CG  . LYS B 1 94  ? 2.255   -41.709 22.533  1.00 51.29 ? 94   LYS B CG  1 
ATOM   4089 C CD  . LYS B 1 94  ? 1.244   -41.832 23.667  1.00 54.40 ? 94   LYS B CD  1 
ATOM   4090 C CE  . LYS B 1 94  ? 0.973   -43.313 23.967  1.00 55.34 ? 94   LYS B CE  1 
ATOM   4091 N NZ  . LYS B 1 94  ? 0.514   -43.575 25.366  1.00 56.90 ? 94   LYS B NZ  1 
ATOM   4092 N N   . THR B 1 95  ? 3.447   -40.670 19.201  1.00 50.31 ? 95   THR B N   1 
ATOM   4093 C CA  . THR B 1 95  ? 3.354   -41.464 17.977  1.00 50.58 ? 95   THR B CA  1 
ATOM   4094 C C   . THR B 1 95  ? 4.335   -41.094 16.868  1.00 50.22 ? 95   THR B C   1 
ATOM   4095 O O   . THR B 1 95  ? 4.540   -41.892 15.942  1.00 50.83 ? 95   THR B O   1 
ATOM   4096 C CB  . THR B 1 95  ? 1.930   -41.396 17.375  1.00 51.11 ? 95   THR B CB  1 
ATOM   4097 O OG1 . THR B 1 95  ? 1.457   -40.033 17.385  1.00 51.17 ? 95   THR B OG1 1 
ATOM   4098 C CG2 . THR B 1 95  ? 0.981   -42.305 18.155  1.00 50.70 ? 95   THR B CG2 1 
ATOM   4099 N N   . TYR B 1 96  ? 4.934   -39.907 16.953  1.00 49.39 ? 96   TYR B N   1 
ATOM   4100 C CA  . TYR B 1 96  ? 5.772   -39.408 15.877  1.00 48.32 ? 96   TYR B CA  1 
ATOM   4101 C C   . TYR B 1 96  ? 6.624   -40.521 15.273  1.00 48.22 ? 96   TYR B C   1 
ATOM   4102 O O   . TYR B 1 96  ? 7.302   -41.266 15.994  1.00 47.95 ? 96   TYR B O   1 
ATOM   4103 C CB  . TYR B 1 96  ? 6.631   -38.204 16.309  1.00 48.07 ? 96   TYR B CB  1 
ATOM   4104 C CG  . TYR B 1 96  ? 7.384   -37.596 15.132  1.00 45.87 ? 96   TYR B CG  1 
ATOM   4105 C CD1 . TYR B 1 96  ? 6.834   -36.561 14.393  1.00 44.23 ? 96   TYR B CD1 1 
ATOM   4106 C CD2 . TYR B 1 96  ? 8.629   -38.099 14.737  1.00 44.51 ? 96   TYR B CD2 1 
ATOM   4107 C CE1 . TYR B 1 96  ? 7.505   -36.032 13.308  1.00 43.17 ? 96   TYR B CE1 1 
ATOM   4108 C CE2 . TYR B 1 96  ? 9.304   -37.571 13.648  1.00 43.29 ? 96   TYR B CE2 1 
ATOM   4109 C CZ  . TYR B 1 96  ? 8.731   -36.540 12.949  1.00 42.75 ? 96   TYR B CZ  1 
ATOM   4110 O OH  . TYR B 1 96  ? 9.385   -36.020 11.881  1.00 43.97 ? 96   TYR B OH  1 
ATOM   4111 N N   . ASN B 1 97  ? 6.573   -40.616 13.941  1.00 48.26 ? 97   ASN B N   1 
ATOM   4112 C CA  . ASN B 1 97  ? 7.160   -41.735 13.188  1.00 48.14 ? 97   ASN B CA  1 
ATOM   4113 C C   . ASN B 1 97  ? 8.181   -41.247 12.170  1.00 47.33 ? 97   ASN B C   1 
ATOM   4114 O O   . ASN B 1 97  ? 7.844   -40.979 11.014  1.00 47.85 ? 97   ASN B O   1 
ATOM   4115 C CB  . ASN B 1 97  ? 6.039   -42.546 12.503  1.00 48.56 ? 97   ASN B CB  1 
ATOM   4116 C CG  . ASN B 1 97  ? 6.531   -43.853 11.895  1.00 49.34 ? 97   ASN B CG  1 
ATOM   4117 O OD1 . ASN B 1 97  ? 7.704   -44.234 12.041  1.00 49.68 ? 97   ASN B OD1 1 
ATOM   4118 N ND2 . ASN B 1 97  ? 5.621   -44.556 11.204  1.00 50.79 ? 97   ASN B ND2 1 
ATOM   4119 N N   . TYR B 1 98  ? 9.430   -41.152 12.609  1.00 46.22 ? 98   TYR B N   1 
ATOM   4120 C CA  . TYR B 1 98  ? 10.511  -40.562 11.815  1.00 45.00 ? 98   TYR B CA  1 
ATOM   4121 C C   . TYR B 1 98  ? 10.694  -41.279 10.475  1.00 44.64 ? 98   TYR B C   1 
ATOM   4122 O O   . TYR B 1 98  ? 11.072  -42.458 10.439  1.00 44.33 ? 98   TYR B O   1 
ATOM   4123 C CB  . TYR B 1 98  ? 11.810  -40.536 12.631  1.00 44.21 ? 98   TYR B CB  1 
ATOM   4124 C CG  . TYR B 1 98  ? 12.954  -39.761 12.016  1.00 42.93 ? 98   TYR B CG  1 
ATOM   4125 C CD1 . TYR B 1 98  ? 13.847  -40.384 11.133  1.00 43.25 ? 98   TYR B CD1 1 
ATOM   4126 C CD2 . TYR B 1 98  ? 13.180  -38.420 12.344  1.00 40.11 ? 98   TYR B CD2 1 
ATOM   4127 C CE1 . TYR B 1 98  ? 14.917  -39.682 10.568  1.00 40.97 ? 98   TYR B CE1 1 
ATOM   4128 C CE2 . TYR B 1 98  ? 14.250  -37.719 11.794  1.00 38.28 ? 98   TYR B CE2 1 
ATOM   4129 C CZ  . TYR B 1 98  ? 15.108  -38.350 10.906  1.00 39.01 ? 98   TYR B CZ  1 
ATOM   4130 O OH  . TYR B 1 98  ? 16.163  -37.662 10.350  1.00 38.73 ? 98   TYR B OH  1 
ATOM   4131 N N   . SER B 1 99  ? 10.411  -40.549 9.387   1.00 44.07 ? 99   SER B N   1 
ATOM   4132 C CA  . SER B 1 99  ? 10.512  -41.088 8.022   1.00 43.48 ? 99   SER B CA  1 
ATOM   4133 C C   . SER B 1 99  ? 11.377  -40.294 7.042   1.00 43.26 ? 99   SER B C   1 
ATOM   4134 O O   . SER B 1 99  ? 11.595  -40.767 5.918   1.00 43.75 ? 99   SER B O   1 
ATOM   4135 C CB  . SER B 1 99  ? 9.136   -41.350 7.409   1.00 43.03 ? 99   SER B CB  1 
ATOM   4136 O OG  . SER B 1 99  ? 8.144   -40.570 8.020   1.00 43.32 ? 99   SER B OG  1 
ATOM   4137 N N   . LEU B 1 100 ? 11.863  -39.116 7.468   1.00 41.89 ? 100  LEU B N   1 
ATOM   4138 C CA  . LEU B 1 100 ? 12.767  -38.252 6.673   1.00 40.49 ? 100  LEU B CA  1 
ATOM   4139 C C   . LEU B 1 100 ? 13.841  -38.993 5.873   1.00 39.79 ? 100  LEU B C   1 
ATOM   4140 O O   . LEU B 1 100 ? 14.357  -40.043 6.322   1.00 40.00 ? 100  LEU B O   1 
ATOM   4141 C CB  . LEU B 1 100 ? 13.467  -37.220 7.570   1.00 40.27 ? 100  LEU B CB  1 
ATOM   4142 C CG  . LEU B 1 100 ? 12.637  -36.336 8.496   1.00 39.66 ? 100  LEU B CG  1 
ATOM   4143 C CD1 . LEU B 1 100 ? 13.523  -35.264 9.099   1.00 38.00 ? 100  LEU B CD1 1 
ATOM   4144 C CD2 . LEU B 1 100 ? 11.458  -35.736 7.759   1.00 41.02 ? 100  LEU B CD2 1 
ATOM   4145 N N   . GLY B 1 101 ? 14.178  -38.437 4.703   1.00 38.43 ? 101  GLY B N   1 
ATOM   4146 C CA  . GLY B 1 101 ? 15.219  -38.990 3.825   1.00 37.47 ? 101  GLY B CA  1 
ATOM   4147 C C   . GLY B 1 101 ? 16.574  -38.603 4.349   1.00 36.73 ? 101  GLY B C   1 
ATOM   4148 O O   . GLY B 1 101 ? 16.662  -38.157 5.487   1.00 36.50 ? 101  GLY B O   1 
ATOM   4149 N N   . ALA B 1 102 ? 17.618  -38.727 3.522   1.00 36.10 ? 102  ALA B N   1 
ATOM   4150 C CA  . ALA B 1 102 ? 18.982  -38.512 3.998   1.00 36.11 ? 102  ALA B CA  1 
ATOM   4151 C C   . ALA B 1 102 ? 19.970  -37.986 2.968   1.00 36.18 ? 102  ALA B C   1 
ATOM   4152 O O   . ALA B 1 102 ? 20.204  -38.610 1.932   1.00 36.82 ? 102  ALA B O   1 
ATOM   4153 C CB  . ALA B 1 102 ? 19.526  -39.798 4.615   1.00 36.50 ? 102  ALA B CB  1 
ATOM   4154 N N   . ASP B 1 103 ? 20.595  -36.862 3.294   1.00 35.93 ? 103  ASP B N   1 
ATOM   4155 C CA  . ASP B 1 103 ? 21.592  -36.208 2.436   1.00 35.76 ? 103  ASP B CA  1 
ATOM   4156 C C   . ASP B 1 103 ? 20.997  -35.510 1.221   1.00 35.11 ? 103  ASP B C   1 
ATOM   4157 O O   . ASP B 1 103 ? 21.476  -34.452 0.811   1.00 35.55 ? 103  ASP B O   1 
ATOM   4158 C CB  . ASP B 1 103 ? 22.682  -37.193 1.992   1.00 36.21 ? 103  ASP B CB  1 
ATOM   4159 C CG  . ASP B 1 103 ? 23.418  -37.821 3.176   1.00 38.19 ? 103  ASP B CG  1 
ATOM   4160 O OD1 . ASP B 1 103 ? 24.236  -37.101 3.819   1.00 37.72 ? 103  ASP B OD1 1 
ATOM   4161 O OD2 . ASP B 1 103 ? 23.164  -39.033 3.447   1.00 38.16 ? 103  ASP B OD2 1 
ATOM   4162 N N   . ASP B 1 104 ? 19.953  -36.109 0.655   1.00 34.30 ? 104  ASP B N   1 
ATOM   4163 C CA  . ASP B 1 104 ? 19.459  -35.729 -0.655  1.00 33.51 ? 104  ASP B CA  1 
ATOM   4164 C C   . ASP B 1 104 ? 18.761  -34.374 -0.545  1.00 32.07 ? 104  ASP B C   1 
ATOM   4165 O O   . ASP B 1 104 ? 18.433  -33.939 0.548   1.00 31.66 ? 104  ASP B O   1 
ATOM   4166 C CB  . ASP B 1 104 ? 18.533  -36.822 -1.241  1.00 34.25 ? 104  ASP B CB  1 
ATOM   4167 C CG  . ASP B 1 104 ? 19.276  -38.172 -1.569  1.00 36.24 ? 104  ASP B CG  1 
ATOM   4168 O OD1 . ASP B 1 104 ? 20.537  -38.227 -1.552  1.00 38.53 ? 104  ASP B OD1 1 
ATOM   4169 O OD2 . ASP B 1 104 ? 18.586  -39.186 -1.862  1.00 36.01 ? 104  ASP B OD2 1 
ATOM   4170 N N   . LEU B 1 105 ? 18.638  -33.676 -1.668  1.00 30.28 ? 105  LEU B N   1 
ATOM   4171 C CA  . LEU B 1 105 ? 17.767  -32.519 -1.784  1.00 29.12 ? 105  LEU B CA  1 
ATOM   4172 C C   . LEU B 1 105 ? 16.305  -32.947 -1.504  1.00 28.56 ? 105  LEU B C   1 
ATOM   4173 O O   . LEU B 1 105 ? 15.920  -34.067 -1.808  1.00 29.71 ? 105  LEU B O   1 
ATOM   4174 C CB  . LEU B 1 105 ? 17.886  -32.011 -3.217  1.00 28.83 ? 105  LEU B CB  1 
ATOM   4175 C CG  . LEU B 1 105 ? 18.481  -30.703 -3.707  1.00 28.22 ? 105  LEU B CG  1 
ATOM   4176 C CD1 . LEU B 1 105 ? 19.608  -30.222 -2.843  1.00 28.19 ? 105  LEU B CD1 1 
ATOM   4177 C CD2 . LEU B 1 105 ? 18.895  -30.782 -5.193  1.00 26.67 ? 105  LEU B CD2 1 
ATOM   4178 N N   . THR B 1 106 ? 15.482  -32.092 -0.930  1.00 27.46 ? 106  THR B N   1 
ATOM   4179 C CA  . THR B 1 106 ? 14.050  -32.407 -0.806  1.00 26.94 ? 106  THR B CA  1 
ATOM   4180 C C   . THR B 1 106 ? 13.221  -31.839 -1.985  1.00 27.16 ? 106  THR B C   1 
ATOM   4181 O O   . THR B 1 106 ? 13.672  -30.922 -2.663  1.00 27.61 ? 106  THR B O   1 
ATOM   4182 C CB  . THR B 1 106 ? 13.501  -31.801 0.450   1.00 26.68 ? 106  THR B CB  1 
ATOM   4183 O OG1 . THR B 1 106 ? 13.648  -30.378 0.363   1.00 27.03 ? 106  THR B OG1 1 
ATOM   4184 C CG2 . THR B 1 106 ? 14.227  -32.336 1.665   1.00 25.56 ? 106  THR B CG2 1 
ATOM   4185 N N   . PRO B 1 107 ? 12.018  -32.374 -2.262  1.00 27.33 ? 107  PRO B N   1 
ATOM   4186 C CA  . PRO B 1 107 ? 11.252  -31.710 -3.323  1.00 26.90 ? 107  PRO B CA  1 
ATOM   4187 C C   . PRO B 1 107 ? 11.256  -30.187 -3.179  1.00 26.37 ? 107  PRO B C   1 
ATOM   4188 O O   . PRO B 1 107 ? 11.495  -29.472 -4.151  1.00 26.85 ? 107  PRO B O   1 
ATOM   4189 C CB  . PRO B 1 107 ? 9.836   -32.272 -3.133  1.00 27.71 ? 107  PRO B CB  1 
ATOM   4190 C CG  . PRO B 1 107 ? 10.057  -33.666 -2.505  1.00 27.99 ? 107  PRO B CG  1 
ATOM   4191 C CD  . PRO B 1 107 ? 11.520  -33.743 -2.039  1.00 27.64 ? 107  PRO B CD  1 
ATOM   4192 N N   . PHE B 1 108 ? 11.025  -29.694 -1.972  1.00 24.91 ? 108  PHE B N   1 
ATOM   4193 C CA  . PHE B 1 108 ? 11.063  -28.255 -1.704  1.00 23.71 ? 108  PHE B CA  1 
ATOM   4194 C C   . PHE B 1 108 ? 12.448  -27.616 -2.046  1.00 22.50 ? 108  PHE B C   1 
ATOM   4195 O O   . PHE B 1 108 ? 12.551  -26.575 -2.685  1.00 21.52 ? 108  PHE B O   1 
ATOM   4196 C CB  . PHE B 1 108 ? 10.652  -28.001 -0.235  1.00 23.46 ? 108  PHE B CB  1 
ATOM   4197 C CG  . PHE B 1 108 ? 10.791  -26.561 0.206   1.00 23.51 ? 108  PHE B CG  1 
ATOM   4198 C CD1 . PHE B 1 108 ? 9.779   -25.649 -0.051  1.00 21.79 ? 108  PHE B CD1 1 
ATOM   4199 C CD2 . PHE B 1 108 ? 11.929  -26.128 0.866   1.00 24.10 ? 108  PHE B CD2 1 
ATOM   4200 C CE1 . PHE B 1 108 ? 9.886   -24.364 0.319   1.00 22.29 ? 108  PHE B CE1 1 
ATOM   4201 C CE2 . PHE B 1 108 ? 12.049  -24.807 1.254   1.00 25.79 ? 108  PHE B CE2 1 
ATOM   4202 C CZ  . PHE B 1 108 ? 11.018  -23.919 0.970   1.00 25.11 ? 108  PHE B CZ  1 
ATOM   4203 N N   . GLY B 1 109 ? 13.512  -28.251 -1.606  1.00 22.17 ? 109  GLY B N   1 
ATOM   4204 C CA  . GLY B 1 109 ? 14.842  -27.771 -1.932  1.00 21.74 ? 109  GLY B CA  1 
ATOM   4205 C C   . GLY B 1 109 ? 15.057  -27.719 -3.430  1.00 20.96 ? 109  GLY B C   1 
ATOM   4206 O O   . GLY B 1 109 ? 15.717  -26.826 -3.946  1.00 21.58 ? 109  GLY B O   1 
ATOM   4207 N N   . GLU B 1 110 ? 14.506  -28.699 -4.123  1.00 20.69 ? 110  GLU B N   1 
ATOM   4208 C CA  . GLU B 1 110 ? 14.552  -28.743 -5.580  1.00 19.90 ? 110  GLU B CA  1 
ATOM   4209 C C   . GLU B 1 110 ? 13.882  -27.521 -6.203  1.00 18.81 ? 110  GLU B C   1 
ATOM   4210 O O   . GLU B 1 110 ? 14.485  -26.821 -7.044  1.00 18.19 ? 110  GLU B O   1 
ATOM   4211 C CB  . GLU B 1 110 ? 13.910  -30.048 -6.076  1.00 19.84 ? 110  GLU B CB  1 
ATOM   4212 C CG  . GLU B 1 110 ? 14.718  -31.290 -5.706  1.00 23.07 ? 110  GLU B CG  1 
ATOM   4213 C CD  . GLU B 1 110 ? 14.144  -32.604 -6.266  1.00 24.59 ? 110  GLU B CD  1 
ATOM   4214 O OE1 . GLU B 1 110 ? 13.234  -32.579 -7.111  1.00 26.32 ? 110  GLU B OE1 1 
ATOM   4215 O OE2 . GLU B 1 110 ? 14.628  -33.680 -5.862  1.00 27.82 ? 110  GLU B OE2 1 
ATOM   4216 N N   . GLN B 1 111 ? 12.641  -27.270 -5.778  1.00 18.26 ? 111  GLN B N   1 
ATOM   4217 C CA  . GLN B 1 111 ? 11.866  -26.145 -6.255  1.00 18.78 ? 111  GLN B CA  1 
ATOM   4218 C C   . GLN B 1 111 ? 12.535  -24.778 -5.964  1.00 19.26 ? 111  GLN B C   1 
ATOM   4219 O O   . GLN B 1 111 ? 12.399  -23.825 -6.742  1.00 19.11 ? 111  GLN B O   1 
ATOM   4220 C CB  . GLN B 1 111 ? 10.437  -26.166 -5.693  1.00 18.90 ? 111  GLN B CB  1 
ATOM   4221 C CG  . GLN B 1 111 ? 9.560   -25.007 -6.283  1.00 18.71 ? 111  GLN B CG  1 
ATOM   4222 C CD  . GLN B 1 111 ? 9.358   -25.217 -7.780  1.00 20.72 ? 111  GLN B CD  1 
ATOM   4223 O OE1 . GLN B 1 111 ? 8.961   -26.304 -8.205  1.00 21.91 ? 111  GLN B OE1 1 
ATOM   4224 N NE2 . GLN B 1 111 ? 9.664   -24.204 -8.582  1.00 18.83 ? 111  GLN B NE2 1 
ATOM   4225 N N   . GLU B 1 112 ? 13.214  -24.688 -4.832  1.00 19.59 ? 112  GLU B N   1 
ATOM   4226 C CA  . GLU B 1 112 ? 13.966  -23.483 -4.472  1.00 20.78 ? 112  GLU B CA  1 
ATOM   4227 C C   . GLU B 1 112 ? 14.963  -23.148 -5.553  1.00 20.77 ? 112  GLU B C   1 
ATOM   4228 O O   . GLU B 1 112 ? 15.110  -21.996 -5.927  1.00 21.07 ? 112  GLU B O   1 
ATOM   4229 C CB  . GLU B 1 112 ? 14.728  -23.677 -3.136  1.00 20.56 ? 112  GLU B CB  1 
ATOM   4230 C CG  . GLU B 1 112 ? 13.994  -23.201 -1.886  1.00 22.22 ? 112  GLU B CG  1 
ATOM   4231 C CD  . GLU B 1 112 ? 14.834  -23.405 -0.590  1.00 24.69 ? 112  GLU B CD  1 
ATOM   4232 O OE1 . GLU B 1 112 ? 15.678  -24.348 -0.590  1.00 26.09 ? 112  GLU B OE1 1 
ATOM   4233 O OE2 . GLU B 1 112 ? 14.633  -22.652 0.417   1.00 22.74 ? 112  GLU B OE2 1 
ATOM   4234 N N   . LEU B 1 113 ? 15.666  -24.143 -6.072  1.00 20.83 ? 113  LEU B N   1 
ATOM   4235 C CA  . LEU B 1 113 ? 16.715  -23.793 -7.030  1.00 21.05 ? 113  LEU B CA  1 
ATOM   4236 C C   . LEU B 1 113 ? 16.114  -23.559 -8.423  1.00 21.45 ? 113  LEU B C   1 
ATOM   4237 O O   . LEU B 1 113 ? 16.754  -22.916 -9.273  1.00 21.83 ? 113  LEU B O   1 
ATOM   4238 C CB  . LEU B 1 113 ? 17.828  -24.841 -7.045  1.00 20.66 ? 113  LEU B CB  1 
ATOM   4239 C CG  . LEU B 1 113 ? 18.976  -24.722 -6.005  1.00 21.59 ? 113  LEU B CG  1 
ATOM   4240 C CD1 . LEU B 1 113 ? 20.225  -23.887 -6.495  1.00 21.46 ? 113  LEU B CD1 1 
ATOM   4241 C CD2 . LEU B 1 113 ? 18.492  -24.229 -4.680  1.00 20.08 ? 113  LEU B CD2 1 
ATOM   4242 N N   . VAL B 1 114 ? 14.890  -24.075 -8.638  1.00 21.07 ? 114  VAL B N   1 
ATOM   4243 C CA  . VAL B 1 114 ? 14.164  -23.875 -9.886  1.00 19.68 ? 114  VAL B CA  1 
ATOM   4244 C C   . VAL B 1 114 ? 13.807  -22.415 -9.819  1.00 19.92 ? 114  VAL B C   1 
ATOM   4245 O O   . VAL B 1 114 ? 14.089  -21.655 -10.760 1.00 19.66 ? 114  VAL B O   1 
ATOM   4246 C CB  . VAL B 1 114 ? 12.873  -24.729 -9.985  1.00 19.72 ? 114  VAL B CB  1 
ATOM   4247 C CG1 . VAL B 1 114 ? 11.910  -24.159 -11.059 1.00 18.35 ? 114  VAL B CG1 1 
ATOM   4248 C CG2 . VAL B 1 114 ? 13.207  -26.169 -10.292 1.00 17.87 ? 114  VAL B CG2 1 
ATOM   4249 N N   . ASN B 1 115 ? 13.228  -22.014 -8.682  1.00 18.76 ? 115  ASN B N   1 
ATOM   4250 C CA  . ASN B 1 115 ? 12.829  -20.633 -8.510  1.00 18.10 ? 115  ASN B CA  1 
ATOM   4251 C C   . ASN B 1 115 ? 14.020  -19.626 -8.617  1.00 17.62 ? 115  ASN B C   1 
ATOM   4252 O O   . ASN B 1 115 ? 13.880  -18.547 -9.196  1.00 18.04 ? 115  ASN B O   1 
ATOM   4253 C CB  . ASN B 1 115 ? 12.071  -20.457 -7.195  1.00 17.75 ? 115  ASN B CB  1 
ATOM   4254 C CG  . ASN B 1 115 ? 10.727  -21.183 -7.177  1.00 19.13 ? 115  ASN B CG  1 
ATOM   4255 O OD1 . ASN B 1 115 ? 10.272  -21.772 -8.175  1.00 18.55 ? 115  ASN B OD1 1 
ATOM   4256 N ND2 . ASN B 1 115 ? 10.083  -21.139 -6.034  1.00 14.89 ? 115  ASN B ND2 1 
ATOM   4257 N N   . SER B 1 116 ? 15.164  -19.960 -8.023  1.00 17.25 ? 116  SER B N   1 
ATOM   4258 C CA  . SER B 1 116 ? 16.376  -19.151 -8.141  1.00 16.63 ? 116  SER B CA  1 
ATOM   4259 C C   . SER B 1 116 ? 16.753  -18.986 -9.633  1.00 16.69 ? 116  SER B C   1 
ATOM   4260 O O   . SER B 1 116 ? 17.182  -17.911 -10.027 1.00 16.41 ? 116  SER B O   1 
ATOM   4261 C CB  . SER B 1 116 ? 17.500  -19.809 -7.347  1.00 16.51 ? 116  SER B CB  1 
ATOM   4262 O OG  . SER B 1 116 ? 18.788  -19.210 -7.513  1.00 16.44 ? 116  SER B OG  1 
ATOM   4263 N N   . GLY B 1 117 ? 16.578  -20.054 -10.444 1.00 16.70 ? 117  GLY B N   1 
ATOM   4264 C CA  . GLY B 1 117 ? 16.843  -20.037 -11.891 1.00 15.13 ? 117  GLY B CA  1 
ATOM   4265 C C   . GLY B 1 117 ? 15.941  -19.063 -12.642 1.00 14.90 ? 117  GLY B C   1 
ATOM   4266 O O   . GLY B 1 117 ? 16.393  -18.247 -13.450 1.00 14.34 ? 117  GLY B O   1 
ATOM   4267 N N   . ILE B 1 118 ? 14.657  -19.130 -12.345 1.00 14.39 ? 118  ILE B N   1 
ATOM   4268 C CA  . ILE B 1 118 ? 13.714  -18.222 -12.911 1.00 14.33 ? 118  ILE B CA  1 
ATOM   4269 C C   . ILE B 1 118 ? 14.125  -16.790 -12.551 1.00 14.80 ? 118  ILE B C   1 
ATOM   4270 O O   . ILE B 1 118 ? 14.261  -15.915 -13.419 1.00 14.04 ? 118  ILE B O   1 
ATOM   4271 C CB  . ILE B 1 118 ? 12.268  -18.558 -12.420 1.00 13.95 ? 118  ILE B CB  1 
ATOM   4272 C CG1 . ILE B 1 118 ? 11.926  -20.002 -12.804 1.00 12.99 ? 118  ILE B CG1 1 
ATOM   4273 C CG2 . ILE B 1 118 ? 11.245  -17.510 -13.013 1.00 13.67 ? 118  ILE B CG2 1 
ATOM   4274 C CD1 . ILE B 1 118 ? 10.556  -20.531 -12.256 1.00 9.54  ? 118  ILE B CD1 1 
ATOM   4275 N N   . LYS B 1 119 ? 14.348  -16.569 -11.261 1.00 14.90 ? 119  LYS B N   1 
ATOM   4276 C CA  . LYS B 1 119 ? 14.624  -15.234 -10.771 1.00 15.17 ? 119  LYS B CA  1 
ATOM   4277 C C   . LYS B 1 119 ? 15.891  -14.720 -11.427 1.00 15.28 ? 119  LYS B C   1 
ATOM   4278 O O   . LYS B 1 119 ? 15.940  -13.567 -11.886 1.00 14.96 ? 119  LYS B O   1 
ATOM   4279 C CB  . LYS B 1 119 ? 14.660  -15.193 -9.235  1.00 14.83 ? 119  LYS B CB  1 
ATOM   4280 C CG  . LYS B 1 119 ? 14.811  -13.792 -8.664  1.00 16.03 ? 119  LYS B CG  1 
ATOM   4281 C CD  . LYS B 1 119 ? 14.191  -13.616 -7.265  1.00 17.16 ? 119  LYS B CD  1 
ATOM   4282 C CE  . LYS B 1 119 ? 14.323  -12.159 -6.873  1.00 17.13 ? 119  LYS B CE  1 
ATOM   4283 N NZ  . LYS B 1 119 ? 14.431  -11.979 -5.423  1.00 15.66 ? 119  LYS B NZ  1 
ATOM   4284 N N   . PHE B 1 120 ? 16.912  -15.565 -11.523 1.00 15.33 ? 120  PHE B N   1 
ATOM   4285 C CA  . PHE B 1 120 ? 18.163  -15.062 -12.145 1.00 16.36 ? 120  PHE B CA  1 
ATOM   4286 C C   . PHE B 1 120 ? 17.910  -14.685 -13.599 1.00 16.57 ? 120  PHE B C   1 
ATOM   4287 O O   . PHE B 1 120 ? 18.389  -13.651 -14.041 1.00 15.27 ? 120  PHE B O   1 
ATOM   4288 C CB  . PHE B 1 120 ? 19.311  -16.058 -12.035 1.00 15.13 ? 120  PHE B CB  1 
ATOM   4289 C CG  . PHE B 1 120 ? 20.635  -15.538 -12.545 1.00 15.05 ? 120  PHE B CG  1 
ATOM   4290 C CD1 . PHE B 1 120 ? 21.381  -14.639 -11.798 1.00 15.49 ? 120  PHE B CD1 1 
ATOM   4291 C CD2 . PHE B 1 120 ? 21.172  -16.016 -13.727 1.00 14.81 ? 120  PHE B CD2 1 
ATOM   4292 C CE1 . PHE B 1 120 ? 22.623  -14.197 -12.237 1.00 13.81 ? 120  PHE B CE1 1 
ATOM   4293 C CE2 . PHE B 1 120 ? 22.405  -15.584 -14.174 1.00 16.54 ? 120  PHE B CE2 1 
ATOM   4294 C CZ  . PHE B 1 120 ? 23.127  -14.646 -13.427 1.00 16.09 ? 120  PHE B CZ  1 
ATOM   4295 N N   . TYR B 1 121 ? 17.094  -15.508 -14.290 1.00 17.32 ? 121  TYR B N   1 
ATOM   4296 C CA  . TYR B 1 121 ? 16.831  -15.311 -15.720 1.00 18.03 ? 121  TYR B CA  1 
ATOM   4297 C C   . TYR B 1 121 ? 16.272  -13.913 -15.935 1.00 18.61 ? 121  TYR B C   1 
ATOM   4298 O O   . TYR B 1 121 ? 16.756  -13.169 -16.790 1.00 19.27 ? 121  TYR B O   1 
ATOM   4299 C CB  . TYR B 1 121 ? 15.869  -16.349 -16.348 1.00 17.88 ? 121  TYR B CB  1 
ATOM   4300 C CG  . TYR B 1 121 ? 15.676  -16.038 -17.829 1.00 18.08 ? 121  TYR B CG  1 
ATOM   4301 C CD1 . TYR B 1 121 ? 14.618  -15.237 -18.296 1.00 17.13 ? 121  TYR B CD1 1 
ATOM   4302 C CD2 . TYR B 1 121 ? 16.629  -16.445 -18.747 1.00 16.93 ? 121  TYR B CD2 1 
ATOM   4303 C CE1 . TYR B 1 121 ? 14.501  -14.925 -19.669 1.00 13.78 ? 121  TYR B CE1 1 
ATOM   4304 C CE2 . TYR B 1 121 ? 16.521  -16.119 -20.055 1.00 16.19 ? 121  TYR B CE2 1 
ATOM   4305 C CZ  . TYR B 1 121 ? 15.486  -15.368 -20.506 1.00 13.83 ? 121  TYR B CZ  1 
ATOM   4306 O OH  . TYR B 1 121 ? 15.505  -15.113 -21.820 1.00 15.68 ? 121  TYR B OH  1 
ATOM   4307 N N   . GLN B 1 122 ? 15.277  -13.586 -15.125 1.00 18.31 ? 122  GLN B N   1 
ATOM   4308 C CA  . GLN B 1 122 ? 14.488  -12.390 -15.254 1.00 19.64 ? 122  GLN B CA  1 
ATOM   4309 C C   . GLN B 1 122 ? 15.238  -11.093 -14.902 1.00 20.44 ? 122  GLN B C   1 
ATOM   4310 O O   . GLN B 1 122 ? 15.111  -10.095 -15.611 1.00 20.48 ? 122  GLN B O   1 
ATOM   4311 C CB  . GLN B 1 122 ? 13.216  -12.549 -14.399 1.00 20.17 ? 122  GLN B CB  1 
ATOM   4312 C CG  . GLN B 1 122 ? 12.532  -13.860 -14.708 1.00 23.48 ? 122  GLN B CG  1 
ATOM   4313 C CD  . GLN B 1 122 ? 11.026  -13.841 -14.478 1.00 29.91 ? 122  GLN B CD  1 
ATOM   4314 O OE1 . GLN B 1 122 ? 10.554  -13.665 -13.343 1.00 32.03 ? 122  GLN B OE1 1 
ATOM   4315 N NE2 . GLN B 1 122 ? 10.255  -14.067 -15.560 1.00 30.81 ? 122  GLN B NE2 1 
ATOM   4316 N N   . ARG B 1 123 ? 15.967  -11.101 -13.777 1.00 20.11 ? 123  ARG B N   1 
ATOM   4317 C CA  . ARG B 1 123 ? 16.616  -9.944  -13.260 1.00 19.86 ? 123  ARG B CA  1 
ATOM   4318 C C   . ARG B 1 123 ? 17.633  -9.476  -14.293 1.00 20.24 ? 123  ARG B C   1 
ATOM   4319 O O   . ARG B 1 123 ? 17.919  -8.274  -14.433 1.00 20.56 ? 123  ARG B O   1 
ATOM   4320 C CB  . ARG B 1 123 ? 17.325  -10.316 -11.952 1.00 19.85 ? 123  ARG B CB  1 
ATOM   4321 C CG  . ARG B 1 123 ? 18.027  -9.141  -11.332 1.00 20.31 ? 123  ARG B CG  1 
ATOM   4322 C CD  . ARG B 1 123 ? 18.575  -9.410  -9.899  1.00 22.72 ? 123  ARG B CD  1 
ATOM   4323 N NE  . ARG B 1 123 ? 19.462  -8.303  -9.551  1.00 22.07 ? 123  ARG B NE  1 
ATOM   4324 C CZ  . ARG B 1 123 ? 19.075  -7.175  -8.952  1.00 23.06 ? 123  ARG B CZ  1 
ATOM   4325 N NH1 . ARG B 1 123 ? 17.814  -7.010  -8.571  1.00 20.73 ? 123  ARG B NH1 1 
ATOM   4326 N NH2 . ARG B 1 123 ? 19.964  -6.210  -8.725  1.00 24.42 ? 123  ARG B NH2 1 
ATOM   4327 N N   . TYR B 1 124 ? 18.198  -10.420 -15.012 1.00 19.86 ? 124  TYR B N   1 
ATOM   4328 C CA  . TYR B 1 124 ? 19.217  -10.051 -15.987 1.00 20.19 ? 124  TYR B CA  1 
ATOM   4329 C C   . TYR B 1 124 ? 18.784  -10.411 -17.417 1.00 20.46 ? 124  TYR B C   1 
ATOM   4330 O O   . TYR B 1 124 ? 19.611  -10.559 -18.321 1.00 19.07 ? 124  TYR B O   1 
ATOM   4331 C CB  . TYR B 1 124 ? 20.544  -10.663 -15.597 1.00 20.03 ? 124  TYR B CB  1 
ATOM   4332 C CG  . TYR B 1 124 ? 20.960  -10.242 -14.208 1.00 19.84 ? 124  TYR B CG  1 
ATOM   4333 C CD1 . TYR B 1 124 ? 21.410  -8.944  -13.949 1.00 19.01 ? 124  TYR B CD1 1 
ATOM   4334 C CD2 . TYR B 1 124 ? 20.892  -11.145 -13.152 1.00 19.64 ? 124  TYR B CD2 1 
ATOM   4335 C CE1 . TYR B 1 124 ? 21.771  -8.542  -12.650 1.00 18.76 ? 124  TYR B CE1 1 
ATOM   4336 C CE2 . TYR B 1 124 ? 21.255  -10.787 -11.889 1.00 19.76 ? 124  TYR B CE2 1 
ATOM   4337 C CZ  . TYR B 1 124 ? 21.684  -9.481  -11.622 1.00 19.64 ? 124  TYR B CZ  1 
ATOM   4338 O OH  . TYR B 1 124 ? 22.041  -9.166  -10.322 1.00 18.02 ? 124  TYR B OH  1 
ATOM   4339 N N   . GLU B 1 125 ? 17.457  -10.490 -17.583 1.00 20.32 ? 125  GLU B N   1 
ATOM   4340 C CA  . GLU B 1 125 ? 16.808  -10.751 -18.875 1.00 21.26 ? 125  GLU B CA  1 
ATOM   4341 C C   . GLU B 1 125 ? 17.471  -10.123 -20.116 1.00 21.22 ? 125  GLU B C   1 
ATOM   4342 O O   . GLU B 1 125 ? 17.614  -10.770 -21.175 1.00 21.03 ? 125  GLU B O   1 
ATOM   4343 C CB  . GLU B 1 125 ? 15.353  -10.306 -18.816 1.00 21.11 ? 125  GLU B CB  1 
ATOM   4344 C CG  . GLU B 1 125 ? 14.527  -10.901 -19.903 1.00 21.30 ? 125  GLU B CG  1 
ATOM   4345 C CD  . GLU B 1 125 ? 14.592  -10.130 -21.186 1.00 20.04 ? 125  GLU B CD  1 
ATOM   4346 O OE1 . GLU B 1 125 ? 14.681  -8.885  -21.155 1.00 17.94 ? 125  GLU B OE1 1 
ATOM   4347 O OE2 . GLU B 1 125 ? 14.584  -10.803 -22.234 1.00 20.97 ? 125  GLU B OE2 1 
ATOM   4348 N N   . SER B 1 126 ? 17.846  -8.855  -20.003 1.00 20.35 ? 126  SER B N   1 
ATOM   4349 C CA  . SER B 1 126 ? 18.354  -8.212  -21.179 1.00 20.80 ? 126  SER B CA  1 
ATOM   4350 C C   . SER B 1 126 ? 19.750  -8.761  -21.518 1.00 19.39 ? 126  SER B C   1 
ATOM   4351 O O   . SER B 1 126 ? 20.277  -8.447  -22.574 1.00 19.67 ? 126  SER B O   1 
ATOM   4352 C CB  . SER B 1 126 ? 18.251  -6.675  -21.112 1.00 20.85 ? 126  SER B CB  1 
ATOM   4353 O OG  . SER B 1 126 ? 19.401  -6.184  -20.509 1.00 23.85 ? 126  SER B OG  1 
ATOM   4354 N N   . LEU B 1 127 ? 20.279  -9.657  -20.681 1.00 18.45 ? 127  LEU B N   1 
ATOM   4355 C CA  . LEU B 1 127 ? 21.509  -10.409 -21.003 1.00 17.05 ? 127  LEU B CA  1 
ATOM   4356 C C   . LEU B 1 127 ? 21.335  -11.908 -21.136 1.00 17.97 ? 127  LEU B C   1 
ATOM   4357 O O   . LEU B 1 127 ? 22.101  -12.558 -21.889 1.00 18.01 ? 127  LEU B O   1 
ATOM   4358 C CB  . LEU B 1 127 ? 22.571  -10.175 -19.959 1.00 16.75 ? 127  LEU B CB  1 
ATOM   4359 C CG  . LEU B 1 127 ? 22.988  -8.742  -19.726 1.00 13.48 ? 127  LEU B CG  1 
ATOM   4360 C CD1 . LEU B 1 127 ? 23.795  -8.630  -18.439 1.00 8.77  ? 127  LEU B CD1 1 
ATOM   4361 C CD2 . LEU B 1 127 ? 23.752  -8.342  -20.915 1.00 14.02 ? 127  LEU B CD2 1 
ATOM   4362 N N   . THR B 1 128 ? 20.354  -12.452 -20.394 1.00 18.20 ? 128  THR B N   1 
ATOM   4363 C CA  . THR B 1 128 ? 20.122  -13.875 -20.277 1.00 18.11 ? 128  THR B CA  1 
ATOM   4364 C C   . THR B 1 128 ? 19.354  -14.357 -21.533 1.00 19.43 ? 128  THR B C   1 
ATOM   4365 O O   . THR B 1 128 ? 19.117  -15.541 -21.740 1.00 19.52 ? 128  THR B O   1 
ATOM   4366 C CB  . THR B 1 128 ? 19.381  -14.253 -18.914 1.00 18.43 ? 128  THR B CB  1 
ATOM   4367 O OG1 . THR B 1 128 ? 18.122  -13.567 -18.795 1.00 18.26 ? 128  THR B OG1 1 
ATOM   4368 C CG2 . THR B 1 128 ? 20.188  -13.893 -17.686 1.00 17.86 ? 128  THR B CG2 1 
ATOM   4369 N N   . ARG B 1 129 ? 18.966  -13.422 -22.380 1.00 20.82 ? 129  ARG B N   1 
ATOM   4370 C CA  . ARG B 1 129 ? 18.182  -13.757 -23.535 1.00 21.83 ? 129  ARG B CA  1 
ATOM   4371 C C   . ARG B 1 129 ? 19.025  -14.308 -24.643 1.00 22.34 ? 129  ARG B C   1 
ATOM   4372 O O   . ARG B 1 129 ? 18.510  -15.057 -25.466 1.00 22.00 ? 129  ARG B O   1 
ATOM   4373 C CB  . ARG B 1 129 ? 17.386  -12.569 -24.033 1.00 22.46 ? 129  ARG B CB  1 
ATOM   4374 C CG  . ARG B 1 129 ? 18.159  -11.397 -24.660 1.00 23.00 ? 129  ARG B CG  1 
ATOM   4375 C CD  . ARG B 1 129 ? 17.312  -10.208 -24.247 1.00 24.72 ? 129  ARG B CD  1 
ATOM   4376 N NE  . ARG B 1 129 ? 17.227  -9.160  -25.229 1.00 25.43 ? 129  ARG B NE  1 
ATOM   4377 C CZ  . ARG B 1 129 ? 16.436  -8.088  -25.129 1.00 25.68 ? 129  ARG B CZ  1 
ATOM   4378 N NH1 . ARG B 1 129 ? 15.627  -7.872  -24.086 1.00 25.18 ? 129  ARG B NH1 1 
ATOM   4379 N NH2 . ARG B 1 129 ? 16.451  -7.216  -26.108 1.00 26.43 ? 129  ARG B NH2 1 
ATOM   4380 N N   . ASN B 1 130 ? 20.313  -13.977 -24.650 1.00 22.61 ? 130  ASN B N   1 
ATOM   4381 C CA  . ASN B 1 130 ? 21.175  -14.387 -25.763 1.00 23.27 ? 130  ASN B CA  1 
ATOM   4382 C C   . ASN B 1 130 ? 22.613  -14.673 -25.363 1.00 23.26 ? 130  ASN B C   1 
ATOM   4383 O O   . ASN B 1 130 ? 23.515  -14.774 -26.207 1.00 24.25 ? 130  ASN B O   1 
ATOM   4384 C CB  . ASN B 1 130 ? 21.160  -13.319 -26.856 1.00 23.80 ? 130  ASN B CB  1 
ATOM   4385 C CG  . ASN B 1 130 ? 21.808  -11.990 -26.416 1.00 25.34 ? 130  ASN B CG  1 
ATOM   4386 O OD1 . ASN B 1 130 ? 22.186  -11.795 -25.256 1.00 26.90 ? 130  ASN B OD1 1 
ATOM   4387 N ND2 . ASN B 1 130 ? 21.901  -11.065 -27.344 1.00 24.79 ? 130  ASN B ND2 1 
ATOM   4388 N N   . ILE B 1 131 ? 22.841  -14.784 -24.068 1.00 23.21 ? 131  ILE B N   1 
ATOM   4389 C CA  . ILE B 1 131 ? 24.148  -15.202 -23.579 1.00 22.29 ? 131  ILE B CA  1 
ATOM   4390 C C   . ILE B 1 131 ? 24.002  -16.405 -22.690 1.00 22.14 ? 131  ILE B C   1 
ATOM   4391 O O   . ILE B 1 131 ? 23.255  -16.366 -21.708 1.00 22.22 ? 131  ILE B O   1 
ATOM   4392 C CB  . ILE B 1 131 ? 24.862  -14.089 -22.823 1.00 21.97 ? 131  ILE B CB  1 
ATOM   4393 C CG1 . ILE B 1 131 ? 25.336  -13.030 -23.833 1.00 22.02 ? 131  ILE B CG1 1 
ATOM   4394 C CG2 . ILE B 1 131 ? 26.072  -14.683 -22.100 1.00 21.56 ? 131  ILE B CG2 1 
ATOM   4395 C CD1 . ILE B 1 131 ? 25.318  -11.653 -23.341 1.00 21.08 ? 131  ILE B CD1 1 
ATOM   4396 N N   . VAL B 1 132 ? 24.727  -17.460 -23.045 1.00 21.82 ? 132  VAL B N   1 
ATOM   4397 C CA  . VAL B 1 132 ? 24.775  -18.685 -22.256 1.00 21.16 ? 132  VAL B CA  1 
ATOM   4398 C C   . VAL B 1 132 ? 25.817  -18.530 -21.135 1.00 20.64 ? 132  VAL B C   1 
ATOM   4399 O O   . VAL B 1 132 ? 27.024  -18.381 -21.411 1.00 20.50 ? 132  VAL B O   1 
ATOM   4400 C CB  . VAL B 1 132 ? 25.041  -19.899 -23.182 1.00 21.13 ? 132  VAL B CB  1 
ATOM   4401 C CG1 . VAL B 1 132 ? 25.116  -21.195 -22.415 1.00 20.89 ? 132  VAL B CG1 1 
ATOM   4402 C CG2 . VAL B 1 132 ? 23.891  -19.994 -24.192 1.00 21.48 ? 132  VAL B CG2 1 
ATOM   4403 N N   . PRO B 1 133 ? 25.344  -18.527 -19.869 1.00 19.70 ? 133  PRO B N   1 
ATOM   4404 C CA  . PRO B 1 133 ? 26.238  -18.386 -18.720 1.00 19.41 ? 133  PRO B CA  1 
ATOM   4405 C C   . PRO B 1 133 ? 27.267  -19.521 -18.609 1.00 19.39 ? 133  PRO B C   1 
ATOM   4406 O O   . PRO B 1 133 ? 26.948  -20.678 -18.933 1.00 19.31 ? 133  PRO B O   1 
ATOM   4407 C CB  . PRO B 1 133 ? 25.278  -18.405 -17.520 1.00 18.89 ? 133  PRO B CB  1 
ATOM   4408 C CG  . PRO B 1 133 ? 23.918  -18.088 -18.086 1.00 19.34 ? 133  PRO B CG  1 
ATOM   4409 C CD  . PRO B 1 133 ? 23.940  -18.711 -19.441 1.00 19.87 ? 133  PRO B CD  1 
ATOM   4410 N N   . PHE B 1 134 ? 28.490  -19.200 -18.175 1.00 17.96 ? 134  PHE B N   1 
ATOM   4411 C CA  . PHE B 1 134 ? 29.456  -20.253 -17.886 1.00 17.49 ? 134  PHE B CA  1 
ATOM   4412 C C   . PHE B 1 134 ? 29.272  -20.730 -16.451 1.00 16.42 ? 134  PHE B C   1 
ATOM   4413 O O   . PHE B 1 134 ? 29.203  -19.917 -15.519 1.00 15.31 ? 134  PHE B O   1 
ATOM   4414 C CB  . PHE B 1 134 ? 30.904  -19.830 -18.158 1.00 17.23 ? 134  PHE B CB  1 
ATOM   4415 C CG  . PHE B 1 134 ? 31.880  -20.953 -17.990 1.00 18.48 ? 134  PHE B CG  1 
ATOM   4416 C CD1 . PHE B 1 134 ? 32.068  -21.888 -19.010 1.00 17.78 ? 134  PHE B CD1 1 
ATOM   4417 C CD2 . PHE B 1 134 ? 32.605  -21.099 -16.799 1.00 18.94 ? 134  PHE B CD2 1 
ATOM   4418 C CE1 . PHE B 1 134 ? 33.008  -22.949 -18.863 1.00 19.15 ? 134  PHE B CE1 1 
ATOM   4419 C CE2 . PHE B 1 134 ? 33.509  -22.144 -16.627 1.00 18.99 ? 134  PHE B CE2 1 
ATOM   4420 C CZ  . PHE B 1 134 ? 33.714  -23.075 -17.669 1.00 19.76 ? 134  PHE B CZ  1 
ATOM   4421 N N   . ILE B 1 135 ? 29.159  -22.042 -16.285 1.00 16.13 ? 135  ILE B N   1 
ATOM   4422 C CA  . ILE B 1 135 ? 28.572  -22.584 -15.038 1.00 16.99 ? 135  ILE B CA  1 
ATOM   4423 C C   . ILE B 1 135 ? 29.448  -23.640 -14.351 1.00 17.42 ? 135  ILE B C   1 
ATOM   4424 O O   . ILE B 1 135 ? 29.795  -24.654 -14.955 1.00 17.16 ? 135  ILE B O   1 
ATOM   4425 C CB  . ILE B 1 135 ? 27.163  -23.168 -15.283 1.00 16.97 ? 135  ILE B CB  1 
ATOM   4426 C CG1 . ILE B 1 135 ? 26.195  -22.071 -15.696 1.00 16.49 ? 135  ILE B CG1 1 
ATOM   4427 C CG2 . ILE B 1 135 ? 26.652  -23.974 -14.066 1.00 15.92 ? 135  ILE B CG2 1 
ATOM   4428 C CD1 . ILE B 1 135 ? 24.710  -22.535 -15.723 1.00 18.17 ? 135  ILE B CD1 1 
ATOM   4429 N N   . ARG B 1 136 ? 29.788  -23.395 -13.085 1.00 17.66 ? 136  ARG B N   1 
ATOM   4430 C CA  . ARG B 1 136 ? 30.590  -24.348 -12.325 1.00 17.49 ? 136  ARG B CA  1 
ATOM   4431 C C   . ARG B 1 136 ? 29.892  -24.876 -11.089 1.00 17.54 ? 136  ARG B C   1 
ATOM   4432 O O   . ARG B 1 136 ? 28.976  -24.245 -10.590 1.00 17.01 ? 136  ARG B O   1 
ATOM   4433 C CB  . ARG B 1 136 ? 31.917  -23.755 -11.954 1.00 17.64 ? 136  ARG B CB  1 
ATOM   4434 C CG  . ARG B 1 136 ? 32.773  -23.454 -13.090 1.00 16.51 ? 136  ARG B CG  1 
ATOM   4435 C CD  . ARG B 1 136 ? 34.049  -22.933 -12.530 1.00 17.69 ? 136  ARG B CD  1 
ATOM   4436 N NE  . ARG B 1 136 ? 33.800  -21.859 -11.536 1.00 16.36 ? 136  ARG B NE  1 
ATOM   4437 C CZ  . ARG B 1 136 ? 34.778  -21.249 -10.848 1.00 16.50 ? 136  ARG B CZ  1 
ATOM   4438 N NH1 . ARG B 1 136 ? 36.067  -21.581 -11.040 1.00 14.52 ? 136  ARG B NH1 1 
ATOM   4439 N NH2 . ARG B 1 136 ? 34.467  -20.277 -9.990  1.00 17.40 ? 136  ARG B NH2 1 
ATOM   4440 N N   . SER B 1 137 ? 30.307  -26.058 -10.620 1.00 18.23 ? 137  SER B N   1 
ATOM   4441 C CA  . SER B 1 137 ? 29.678  -26.646 -9.444  1.00 19.90 ? 137  SER B CA  1 
ATOM   4442 C C   . SER B 1 137 ? 30.655  -27.453 -8.657  1.00 20.22 ? 137  SER B C   1 
ATOM   4443 O O   . SER B 1 137 ? 31.375  -28.249 -9.222  1.00 21.94 ? 137  SER B O   1 
ATOM   4444 C CB  . SER B 1 137 ? 28.482  -27.538 -9.840  1.00 20.58 ? 137  SER B CB  1 
ATOM   4445 O OG  . SER B 1 137 ? 27.890  -28.217 -8.727  1.00 20.88 ? 137  SER B OG  1 
ATOM   4446 N N   . SER B 1 138 ? 30.673  -27.280 -7.341  1.00 20.85 ? 138  SER B N   1 
ATOM   4447 C CA  . SER B 1 138 ? 31.484  -28.169 -6.497  1.00 21.06 ? 138  SER B CA  1 
ATOM   4448 C C   . SER B 1 138 ? 30.933  -29.584 -6.697  1.00 21.51 ? 138  SER B C   1 
ATOM   4449 O O   . SER B 1 138 ? 29.776  -29.739 -7.109  1.00 21.00 ? 138  SER B O   1 
ATOM   4450 C CB  . SER B 1 138 ? 31.405  -27.740 -5.029  1.00 20.40 ? 138  SER B CB  1 
ATOM   4451 O OG  . SER B 1 138 ? 32.335  -28.451 -4.219  1.00 20.39 ? 138  SER B OG  1 
ATOM   4452 N N   . GLY B 1 139 ? 31.727  -30.603 -6.384  1.00 22.42 ? 139  GLY B N   1 
ATOM   4453 C CA  . GLY B 1 139 ? 31.302  -31.976 -6.631  1.00 23.71 ? 139  GLY B CA  1 
ATOM   4454 C C   . GLY B 1 139 ? 30.644  -32.679 -5.461  1.00 25.18 ? 139  GLY B C   1 
ATOM   4455 O O   . GLY B 1 139 ? 31.337  -33.363 -4.701  1.00 27.37 ? 139  GLY B O   1 
ATOM   4456 N N   . SER B 1 140 ? 29.323  -32.542 -5.312  1.00 24.52 ? 140  SER B N   1 
ATOM   4457 C CA  . SER B 1 140 ? 28.566  -33.196 -4.253  1.00 23.57 ? 140  SER B CA  1 
ATOM   4458 C C   . SER B 1 140 ? 27.178  -33.387 -4.814  1.00 23.39 ? 140  SER B C   1 
ATOM   4459 O O   . SER B 1 140 ? 26.620  -32.445 -5.370  1.00 23.47 ? 140  SER B O   1 
ATOM   4460 C CB  . SER B 1 140 ? 28.494  -32.283 -3.032  1.00 23.61 ? 140  SER B CB  1 
ATOM   4461 O OG  . SER B 1 140 ? 27.461  -32.696 -2.131  1.00 24.04 ? 140  SER B OG  1 
ATOM   4462 N N   . SER B 1 141 ? 26.595  -34.569 -4.680  1.00 22.53 ? 141  SER B N   1 
ATOM   4463 C CA  . SER B 1 141 ? 25.308  -34.810 -5.340  1.00 22.90 ? 141  SER B CA  1 
ATOM   4464 C C   . SER B 1 141 ? 24.333  -33.652 -5.141  1.00 21.79 ? 141  SER B C   1 
ATOM   4465 O O   . SER B 1 141 ? 23.689  -33.251 -6.095  1.00 22.16 ? 141  SER B O   1 
ATOM   4466 C CB  . SER B 1 141 ? 24.623  -36.075 -4.856  1.00 22.45 ? 141  SER B CB  1 
ATOM   4467 O OG  . SER B 1 141 ? 25.577  -37.050 -4.647  1.00 27.96 ? 141  SER B OG  1 
ATOM   4468 N N   . ARG B 1 142 ? 24.206  -33.140 -3.917  1.00 20.79 ? 142  ARG B N   1 
ATOM   4469 C CA  . ARG B 1 142 ? 23.194  -32.131 -3.664  1.00 20.41 ? 142  ARG B CA  1 
ATOM   4470 C C   . ARG B 1 142 ? 23.485  -30.813 -4.374  1.00 19.67 ? 142  ARG B C   1 
ATOM   4471 O O   . ARG B 1 142 ? 22.565  -30.082 -4.735  1.00 19.66 ? 142  ARG B O   1 
ATOM   4472 C CB  . ARG B 1 142 ? 22.908  -31.948 -2.181  1.00 20.77 ? 142  ARG B CB  1 
ATOM   4473 C CG  . ARG B 1 142 ? 24.101  -31.492 -1.306  1.00 22.94 ? 142  ARG B CG  1 
ATOM   4474 C CD  . ARG B 1 142 ? 23.690  -31.457 0.165   1.00 28.65 ? 142  ARG B CD  1 
ATOM   4475 N NE  . ARG B 1 142 ? 24.784  -31.111 1.082   1.00 34.97 ? 142  ARG B NE  1 
ATOM   4476 C CZ  . ARG B 1 142 ? 25.677  -31.988 1.560   1.00 38.54 ? 142  ARG B CZ  1 
ATOM   4477 N NH1 . ARG B 1 142 ? 25.620  -33.286 1.216   1.00 38.23 ? 142  ARG B NH1 1 
ATOM   4478 N NH2 . ARG B 1 142 ? 26.632  -31.568 2.388   1.00 39.80 ? 142  ARG B NH2 1 
ATOM   4479 N N   . VAL B 1 143 ? 24.758  -30.542 -4.616  1.00 19.36 ? 143  VAL B N   1 
ATOM   4480 C CA  . VAL B 1 143 ? 25.176  -29.268 -5.196  1.00 19.56 ? 143  VAL B CA  1 
ATOM   4481 C C   . VAL B 1 143 ? 24.937  -29.287 -6.711  1.00 18.97 ? 143  VAL B C   1 
ATOM   4482 O O   . VAL B 1 143 ? 24.249  -28.413 -7.241  1.00 18.21 ? 143  VAL B O   1 
ATOM   4483 C CB  . VAL B 1 143 ? 26.627  -28.854 -4.780  1.00 19.52 ? 143  VAL B CB  1 
ATOM   4484 C CG1 . VAL B 1 143 ? 27.015  -27.491 -5.408  1.00 18.68 ? 143  VAL B CG1 1 
ATOM   4485 C CG2 . VAL B 1 143 ? 26.727  -28.773 -3.282  1.00 19.38 ? 143  VAL B CG2 1 
ATOM   4486 N N   . ILE B 1 144 ? 25.492  -30.322 -7.355  1.00 19.74 ? 144  ILE B N   1 
ATOM   4487 C CA  . ILE B 1 144 ? 25.265  -30.735 -8.764  1.00 19.29 ? 144  ILE B CA  1 
ATOM   4488 C C   . ILE B 1 144 ? 23.791  -30.769 -9.129  1.00 18.73 ? 144  ILE B C   1 
ATOM   4489 O O   . ILE B 1 144 ? 23.350  -30.134 -10.101 1.00 20.01 ? 144  ILE B O   1 
ATOM   4490 C CB  . ILE B 1 144 ? 25.851  -32.138 -8.987  1.00 19.56 ? 144  ILE B CB  1 
ATOM   4491 C CG1 . ILE B 1 144 ? 27.371  -32.115 -8.980  1.00 21.58 ? 144  ILE B CG1 1 
ATOM   4492 C CG2 . ILE B 1 144 ? 25.459  -32.683 -10.309 1.00 21.05 ? 144  ILE B CG2 1 
ATOM   4493 C CD1 . ILE B 1 144 ? 27.988  -33.563 -8.962  1.00 24.48 ? 144  ILE B CD1 1 
ATOM   4494 N N   . ALA B 1 145 ? 23.003  -31.488 -8.355  1.00 17.74 ? 145  ALA B N   1 
ATOM   4495 C CA  . ALA B 1 145 ? 21.558  -31.524 -8.610  1.00 17.00 ? 145  ALA B CA  1 
ATOM   4496 C C   . ALA B 1 145 ? 20.937  -30.146 -8.528  1.00 16.30 ? 145  ALA B C   1 
ATOM   4497 O O   . ALA B 1 145 ? 20.038  -29.817 -9.312  1.00 17.05 ? 145  ALA B O   1 
ATOM   4498 C CB  . ALA B 1 145 ? 20.848  -32.468 -7.635  1.00 16.72 ? 145  ALA B CB  1 
ATOM   4499 N N   . SER B 1 146 ? 21.416  -29.334 -7.594  1.00 15.83 ? 146  SER B N   1 
ATOM   4500 C CA  . SER B 1 146 ? 20.850  -27.999 -7.370  1.00 15.17 ? 146  SER B CA  1 
ATOM   4501 C C   . SER B 1 146 ? 21.233  -27.098 -8.523  1.00 15.10 ? 146  SER B C   1 
ATOM   4502 O O   . SER B 1 146 ? 20.406  -26.347 -8.989  1.00 15.38 ? 146  SER B O   1 
ATOM   4503 C CB  . SER B 1 146 ? 21.364  -27.399 -6.071  1.00 15.57 ? 146  SER B CB  1 
ATOM   4504 O OG  . SER B 1 146 ? 20.738  -27.921 -4.917  1.00 16.50 ? 146  SER B OG  1 
ATOM   4505 N N   . GLY B 1 147 ? 22.490  -27.158 -8.962  1.00 13.99 ? 147  GLY B N   1 
ATOM   4506 C CA  . GLY B 1 147 ? 22.882  -26.464 -10.161 1.00 15.40 ? 147  GLY B CA  1 
ATOM   4507 C C   . GLY B 1 147 ? 21.908  -26.776 -11.308 1.00 16.25 ? 147  GLY B C   1 
ATOM   4508 O O   . GLY B 1 147 ? 21.376  -25.857 -11.971 1.00 16.00 ? 147  GLY B O   1 
ATOM   4509 N N   . LYS B 1 148 ? 21.644  -28.064 -11.515 1.00 16.87 ? 148  LYS B N   1 
ATOM   4510 C CA  . LYS B 1 148 ? 20.776  -28.498 -12.620 1.00 16.93 ? 148  LYS B CA  1 
ATOM   4511 C C   . LYS B 1 148 ? 19.315  -28.111 -12.449 1.00 17.43 ? 148  LYS B C   1 
ATOM   4512 O O   . LYS B 1 148 ? 18.625  -27.894 -13.457 1.00 18.62 ? 148  LYS B O   1 
ATOM   4513 C CB  . LYS B 1 148 ? 20.907  -29.995 -12.842 1.00 17.58 ? 148  LYS B CB  1 
ATOM   4514 C CG  . LYS B 1 148 ? 22.264  -30.423 -13.422 1.00 17.64 ? 148  LYS B CG  1 
ATOM   4515 C CD  . LYS B 1 148 ? 22.324  -31.955 -13.536 1.00 19.87 ? 148  LYS B CD  1 
ATOM   4516 C CE  . LYS B 1 148 ? 23.732  -32.419 -13.912 1.00 22.04 ? 148  LYS B CE  1 
ATOM   4517 N NZ  . LYS B 1 148 ? 24.095  -33.666 -13.136 1.00 20.71 ? 148  LYS B NZ  1 
ATOM   4518 N N   . LYS B 1 149 ? 18.833  -27.966 -11.213 1.00 17.55 ? 149  LYS B N   1 
ATOM   4519 C CA  . LYS B 1 149 ? 17.499  -27.438 -10.998 1.00 17.62 ? 149  LYS B CA  1 
ATOM   4520 C C   . LYS B 1 149 ? 17.406  -25.930 -11.277 1.00 19.19 ? 149  LYS B C   1 
ATOM   4521 O O   . LYS B 1 149 ? 16.318  -25.391 -11.619 1.00 21.02 ? 149  LYS B O   1 
ATOM   4522 C CB  . LYS B 1 149 ? 17.046  -27.702 -9.572  1.00 18.21 ? 149  LYS B CB  1 
ATOM   4523 C CG  . LYS B 1 149 ? 16.610  -29.128 -9.308  1.00 17.74 ? 149  LYS B CG  1 
ATOM   4524 C CD  . LYS B 1 149 ? 15.169  -29.347 -9.752  1.00 19.36 ? 149  LYS B CD  1 
ATOM   4525 C CE  . LYS B 1 149 ? 14.876  -30.870 -10.003 1.00 20.15 ? 149  LYS B CE  1 
ATOM   4526 N NZ  . LYS B 1 149 ? 13.531  -31.089 -10.616 1.00 19.96 ? 149  LYS B NZ  1 
ATOM   4527 N N   . PHE B 1 150 ? 18.508  -25.225 -11.065 1.00 18.65 ? 150  PHE B N   1 
ATOM   4528 C CA  . PHE B 1 150 ? 18.582  -23.837 -11.374 1.00 18.68 ? 150  PHE B CA  1 
ATOM   4529 C C   . PHE B 1 150 ? 18.633  -23.718 -12.912 1.00 18.92 ? 150  PHE B C   1 
ATOM   4530 O O   . PHE B 1 150 ? 17.883  -22.951 -13.485 1.00 18.98 ? 150  PHE B O   1 
ATOM   4531 C CB  . PHE B 1 150 ? 19.821  -23.239 -10.685 1.00 19.16 ? 150  PHE B CB  1 
ATOM   4532 C CG  . PHE B 1 150 ? 20.176  -21.811 -11.107 1.00 18.33 ? 150  PHE B CG  1 
ATOM   4533 C CD1 . PHE B 1 150 ? 20.637  -21.528 -12.392 1.00 18.95 ? 150  PHE B CD1 1 
ATOM   4534 C CD2 . PHE B 1 150 ? 20.129  -20.766 -10.178 1.00 18.69 ? 150  PHE B CD2 1 
ATOM   4535 C CE1 . PHE B 1 150 ? 20.996  -20.203 -12.740 1.00 18.58 ? 150  PHE B CE1 1 
ATOM   4536 C CE2 . PHE B 1 150 ? 20.471  -19.467 -10.506 1.00 16.28 ? 150  PHE B CE2 1 
ATOM   4537 C CZ  . PHE B 1 150 ? 20.914  -19.188 -11.777 1.00 16.85 ? 150  PHE B CZ  1 
ATOM   4538 N N   . ILE B 1 151 ? 19.490  -24.485 -13.578 1.00 18.85 ? 151  ILE B N   1 
ATOM   4539 C CA  . ILE B 1 151 ? 19.516  -24.469 -15.058 1.00 19.73 ? 151  ILE B CA  1 
ATOM   4540 C C   . ILE B 1 151 ? 18.167  -24.790 -15.675 1.00 20.57 ? 151  ILE B C   1 
ATOM   4541 O O   . ILE B 1 151 ? 17.790  -24.231 -16.682 1.00 21.44 ? 151  ILE B O   1 
ATOM   4542 C CB  . ILE B 1 151 ? 20.547  -25.455 -15.631 1.00 19.29 ? 151  ILE B CB  1 
ATOM   4543 C CG1 . ILE B 1 151 ? 21.958  -24.931 -15.349 1.00 15.14 ? 151  ILE B CG1 1 
ATOM   4544 C CG2 . ILE B 1 151 ? 20.234  -25.759 -17.110 1.00 17.60 ? 151  ILE B CG2 1 
ATOM   4545 C CD1 . ILE B 1 151 ? 23.031  -25.980 -15.596 1.00 15.31 ? 151  ILE B CD1 1 
ATOM   4546 N N   . GLU B 1 152 ? 17.460  -25.712 -15.046 1.00 21.78 ? 152  GLU B N   1 
ATOM   4547 C CA  . GLU B 1 152 ? 16.106  -26.104 -15.428 1.00 21.96 ? 152  GLU B CA  1 
ATOM   4548 C C   . GLU B 1 152 ? 15.132  -24.946 -15.462 1.00 21.48 ? 152  GLU B C   1 
ATOM   4549 O O   . GLU B 1 152 ? 14.457  -24.759 -16.439 1.00 21.23 ? 152  GLU B O   1 
ATOM   4550 C CB  . GLU B 1 152 ? 15.602  -27.169 -14.446 1.00 22.36 ? 152  GLU B CB  1 
ATOM   4551 C CG  . GLU B 1 152 ? 14.543  -28.142 -15.012 1.00 23.46 ? 152  GLU B CG  1 
ATOM   4552 C CD  . GLU B 1 152 ? 14.043  -29.163 -13.993 1.00 23.35 ? 152  GLU B CD  1 
ATOM   4553 O OE1 . GLU B 1 152 ? 14.857  -29.770 -13.263 1.00 23.00 ? 152  GLU B OE1 1 
ATOM   4554 O OE2 . GLU B 1 152 ? 12.813  -29.371 -13.945 1.00 25.50 ? 152  GLU B OE2 1 
ATOM   4555 N N   . GLY B 1 153 ? 15.057  -24.188 -14.380 1.00 21.92 ? 153  GLY B N   1 
ATOM   4556 C CA  . GLY B 1 153 ? 14.143  -23.048 -14.272 1.00 21.57 ? 153  GLY B CA  1 
ATOM   4557 C C   . GLY B 1 153 ? 14.547  -21.878 -15.152 1.00 21.88 ? 153  GLY B C   1 
ATOM   4558 O O   . GLY B 1 153 ? 13.687  -21.243 -15.778 1.00 22.15 ? 153  GLY B O   1 
ATOM   4559 N N   . PHE B 1 154 ? 15.857  -21.609 -15.223 1.00 21.88 ? 154  PHE B N   1 
ATOM   4560 C CA  . PHE B 1 154 ? 16.431  -20.665 -16.196 1.00 21.97 ? 154  PHE B CA  1 
ATOM   4561 C C   . PHE B 1 154 ? 15.954  -20.989 -17.618 1.00 22.53 ? 154  PHE B C   1 
ATOM   4562 O O   . PHE B 1 154 ? 15.462  -20.113 -18.346 1.00 22.54 ? 154  PHE B O   1 
ATOM   4563 C CB  . PHE B 1 154 ? 17.961  -20.743 -16.124 1.00 21.41 ? 154  PHE B CB  1 
ATOM   4564 C CG  . PHE B 1 154 ? 18.708  -19.747 -16.996 1.00 19.71 ? 154  PHE B CG  1 
ATOM   4565 C CD1 . PHE B 1 154 ? 18.927  -20.002 -18.357 1.00 16.29 ? 154  PHE B CD1 1 
ATOM   4566 C CD2 . PHE B 1 154 ? 19.280  -18.587 -16.430 1.00 18.13 ? 154  PHE B CD2 1 
ATOM   4567 C CE1 . PHE B 1 154 ? 19.662  -19.101 -19.138 1.00 13.17 ? 154  PHE B CE1 1 
ATOM   4568 C CE2 . PHE B 1 154 ? 20.040  -17.694 -17.220 1.00 14.80 ? 154  PHE B CE2 1 
ATOM   4569 C CZ  . PHE B 1 154 ? 20.208  -17.949 -18.564 1.00 14.42 ? 154  PHE B CZ  1 
ATOM   4570 N N   . GLN B 1 155 ? 16.095  -22.243 -18.005 1.00 23.12 ? 155  GLN B N   1 
ATOM   4571 C CA  . GLN B 1 155 ? 15.795  -22.648 -19.370 1.00 24.81 ? 155  GLN B CA  1 
ATOM   4572 C C   . GLN B 1 155 ? 14.293  -22.561 -19.659 1.00 23.93 ? 155  GLN B C   1 
ATOM   4573 O O   . GLN B 1 155 ? 13.905  -22.163 -20.761 1.00 24.51 ? 155  GLN B O   1 
ATOM   4574 C CB  . GLN B 1 155 ? 16.411  -24.029 -19.655 1.00 25.78 ? 155  GLN B CB  1 
ATOM   4575 C CG  . GLN B 1 155 ? 16.304  -24.559 -21.112 1.00 32.92 ? 155  GLN B CG  1 
ATOM   4576 C CD  . GLN B 1 155 ? 16.917  -23.619 -22.178 1.00 39.21 ? 155  GLN B CD  1 
ATOM   4577 O OE1 . GLN B 1 155 ? 18.142  -23.412 -22.193 1.00 44.02 ? 155  GLN B OE1 1 
ATOM   4578 N NE2 . GLN B 1 155 ? 16.063  -23.051 -23.069 1.00 35.84 ? 155  GLN B NE2 1 
ATOM   4579 N N   . SER B 1 156 ? 13.453  -22.874 -18.669 1.00 23.06 ? 156  SER B N   1 
ATOM   4580 C CA  . SER B 1 156 ? 11.981  -22.777 -18.806 1.00 22.63 ? 156  SER B CA  1 
ATOM   4581 C C   . SER B 1 156 ? 11.495  -21.368 -19.024 1.00 21.83 ? 156  SER B C   1 
ATOM   4582 O O   . SER B 1 156 ? 10.472  -21.162 -19.674 1.00 22.38 ? 156  SER B O   1 
ATOM   4583 C CB  . SER B 1 156 ? 11.254  -23.306 -17.568 1.00 22.46 ? 156  SER B CB  1 
ATOM   4584 O OG  . SER B 1 156 ? 11.337  -24.709 -17.525 1.00 24.60 ? 156  SER B OG  1 
ATOM   4585 N N   . THR B 1 157 ? 12.186  -20.416 -18.414 1.00 20.74 ? 157  THR B N   1 
ATOM   4586 C CA  . THR B 1 157 ? 11.855  -19.010 -18.524 1.00 20.10 ? 157  THR B CA  1 
ATOM   4587 C C   . THR B 1 157 ? 12.381  -18.489 -19.858 1.00 20.15 ? 157  THR B C   1 
ATOM   4588 O O   . THR B 1 157 ? 11.690  -17.765 -20.536 1.00 20.84 ? 157  THR B O   1 
ATOM   4589 C CB  . THR B 1 157 ? 12.481  -18.245 -17.369 1.00 19.69 ? 157  THR B CB  1 
ATOM   4590 O OG1 . THR B 1 157 ? 12.221  -18.963 -16.166 1.00 19.77 ? 157  THR B OG1 1 
ATOM   4591 C CG2 . THR B 1 157 ? 11.934  -16.866 -17.258 1.00 17.76 ? 157  THR B CG2 1 
ATOM   4592 N N   . LYS B 1 158 ? 13.584  -18.894 -20.252 1.00 20.54 ? 158  LYS B N   1 
ATOM   4593 C CA  . LYS B 1 158 ? 14.149  -18.523 -21.564 1.00 20.95 ? 158  LYS B CA  1 
ATOM   4594 C C   . LYS B 1 158 ? 13.235  -18.901 -22.741 1.00 22.88 ? 158  LYS B C   1 
ATOM   4595 O O   . LYS B 1 158 ? 13.047  -18.106 -23.655 1.00 24.27 ? 158  LYS B O   1 
ATOM   4596 C CB  . LYS B 1 158 ? 15.579  -19.098 -21.763 1.00 19.75 ? 158  LYS B CB  1 
ATOM   4597 C CG  . LYS B 1 158 ? 16.332  -18.429 -22.928 1.00 17.12 ? 158  LYS B CG  1 
ATOM   4598 C CD  . LYS B 1 158 ? 17.678  -19.003 -23.198 1.00 12.66 ? 158  LYS B CD  1 
ATOM   4599 C CE  . LYS B 1 158 ? 18.503  -18.108 -24.168 1.00 11.96 ? 158  LYS B CE  1 
ATOM   4600 N NZ  . LYS B 1 158 ? 19.712  -18.893 -24.631 1.00 15.07 ? 158  LYS B NZ  1 
ATOM   4601 N N   . LEU B 1 159 ? 12.672  -20.108 -22.728 1.00 24.53 ? 159  LEU B N   1 
ATOM   4602 C CA  . LEU B 1 159 ? 11.705  -20.505 -23.738 1.00 25.53 ? 159  LEU B CA  1 
ATOM   4603 C C   . LEU B 1 159 ? 10.422  -19.675 -23.726 1.00 26.04 ? 159  LEU B C   1 
ATOM   4604 O O   . LEU B 1 159 ? 9.781   -19.527 -24.764 1.00 26.59 ? 159  LEU B O   1 
ATOM   4605 C CB  . LEU B 1 159 ? 11.317  -21.982 -23.589 1.00 26.39 ? 159  LEU B CB  1 
ATOM   4606 C CG  . LEU B 1 159 ? 12.218  -23.123 -24.095 1.00 28.66 ? 159  LEU B CG  1 
ATOM   4607 C CD1 . LEU B 1 159 ? 11.629  -24.502 -23.681 1.00 30.09 ? 159  LEU B CD1 1 
ATOM   4608 C CD2 . LEU B 1 159 ? 12.508  -23.070 -25.612 1.00 27.46 ? 159  LEU B CD2 1 
ATOM   4609 N N   . LYS B 1 160 ? 9.982   -19.177 -22.586 1.00 26.18 ? 160  LYS B N   1 
ATOM   4610 C CA  . LYS B 1 160 ? 8.740   -18.380 -22.652 1.00 27.15 ? 160  LYS B CA  1 
ATOM   4611 C C   . LYS B 1 160 ? 8.989   -16.911 -22.956 1.00 27.08 ? 160  LYS B C   1 
ATOM   4612 O O   . LYS B 1 160 ? 8.070   -16.081 -22.899 1.00 26.39 ? 160  LYS B O   1 
ATOM   4613 C CB  . LYS B 1 160 ? 7.873   -18.547 -21.410 1.00 27.69 ? 160  LYS B CB  1 
ATOM   4614 C CG  . LYS B 1 160 ? 7.227   -19.934 -21.335 1.00 30.52 ? 160  LYS B CG  1 
ATOM   4615 C CD  . LYS B 1 160 ? 6.110   -20.046 -20.267 1.00 37.26 ? 160  LYS B CD  1 
ATOM   4616 C CE  . LYS B 1 160 ? 6.662   -20.294 -18.835 1.00 39.39 ? 160  LYS B CE  1 
ATOM   4617 N NZ  . LYS B 1 160 ? 7.128   -19.035 -18.162 1.00 38.44 ? 160  LYS B NZ  1 
ATOM   4618 N N   . ASP B 1 161 ? 10.236  -16.592 -23.309 1.00 26.68 ? 161  ASP B N   1 
ATOM   4619 C CA  . ASP B 1 161 ? 10.616  -15.212 -23.416 1.00 26.55 ? 161  ASP B CA  1 
ATOM   4620 C C   . ASP B 1 161 ? 10.653  -14.779 -24.883 1.00 26.99 ? 161  ASP B C   1 
ATOM   4621 O O   . ASP B 1 161 ? 11.494  -15.238 -25.639 1.00 27.07 ? 161  ASP B O   1 
ATOM   4622 C CB  . ASP B 1 161 ? 11.948  -14.996 -22.709 1.00 26.20 ? 161  ASP B CB  1 
ATOM   4623 C CG  . ASP B 1 161 ? 12.490  -13.586 -22.884 1.00 24.35 ? 161  ASP B CG  1 
ATOM   4624 O OD1 . ASP B 1 161 ? 11.718  -12.689 -23.267 1.00 26.00 ? 161  ASP B OD1 1 
ATOM   4625 O OD2 . ASP B 1 161 ? 13.703  -13.383 -22.639 1.00 19.97 ? 161  ASP B OD2 1 
ATOM   4626 N N   . PRO B 1 162 ? 9.749   -13.870 -25.276 1.00 27.05 ? 162  PRO B N   1 
ATOM   4627 C CA  . PRO B 1 162 ? 9.656   -13.456 -26.670 1.00 26.93 ? 162  PRO B CA  1 
ATOM   4628 C C   . PRO B 1 162 ? 10.951  -12.798 -27.212 1.00 27.61 ? 162  PRO B C   1 
ATOM   4629 O O   . PRO B 1 162 ? 11.237  -12.881 -28.406 1.00 25.70 ? 162  PRO B O   1 
ATOM   4630 C CB  . PRO B 1 162 ? 8.487   -12.460 -26.659 1.00 27.51 ? 162  PRO B CB  1 
ATOM   4631 C CG  . PRO B 1 162 ? 8.404   -11.939 -25.241 1.00 26.49 ? 162  PRO B CG  1 
ATOM   4632 C CD  . PRO B 1 162 ? 8.885   -13.066 -24.377 1.00 27.28 ? 162  PRO B CD  1 
ATOM   4633 N N   . ARG B 1 163 ? 11.744  -12.172 -26.338 1.00 28.79 ? 163  ARG B N   1 
ATOM   4634 C CA  . ARG B 1 163 ? 12.975  -11.518 -26.791 1.00 29.23 ? 163  ARG B CA  1 
ATOM   4635 C C   . ARG B 1 163 ? 14.208  -12.412 -26.830 1.00 28.86 ? 163  ARG B C   1 
ATOM   4636 O O   . ARG B 1 163 ? 15.282  -11.926 -27.157 1.00 28.53 ? 163  ARG B O   1 
ATOM   4637 C CB  . ARG B 1 163 ? 13.243  -10.256 -25.992 1.00 29.82 ? 163  ARG B CB  1 
ATOM   4638 C CG  . ARG B 1 163 ? 12.053  -9.362  -25.966 1.00 32.35 ? 163  ARG B CG  1 
ATOM   4639 C CD  . ARG B 1 163 ? 12.091  -8.360  -24.857 1.00 35.77 ? 163  ARG B CD  1 
ATOM   4640 N NE  . ARG B 1 163 ? 10.788  -8.321  -24.201 1.00 41.07 ? 163  ARG B NE  1 
ATOM   4641 C CZ  . ARG B 1 163 ? 9.698   -7.745  -24.696 1.00 41.37 ? 163  ARG B CZ  1 
ATOM   4642 N NH1 . ARG B 1 163 ? 9.739   -7.159  -25.873 1.00 42.28 ? 163  ARG B NH1 1 
ATOM   4643 N NH2 . ARG B 1 163 ? 8.559   -7.776  -24.018 1.00 41.52 ? 163  ARG B NH2 1 
ATOM   4644 N N   . ALA B 1 164 ? 14.045  -13.706 -26.555 1.00 28.56 ? 164  ALA B N   1 
ATOM   4645 C CA  . ALA B 1 164 ? 15.164  -14.652 -26.532 1.00 29.39 ? 164  ALA B CA  1 
ATOM   4646 C C   . ALA B 1 164 ? 15.709  -14.965 -27.921 1.00 30.09 ? 164  ALA B C   1 
ATOM   4647 O O   . ALA B 1 164 ? 14.914  -15.049 -28.859 1.00 31.38 ? 164  ALA B O   1 
ATOM   4648 C CB  . ALA B 1 164 ? 14.738  -15.946 -25.847 1.00 28.81 ? 164  ALA B CB  1 
ATOM   4649 N N   . GLN B 1 165 ? 17.035  -15.154 -28.053 1.00 29.93 ? 165  GLN B N   1 
ATOM   4650 C CA  . GLN B 1 165 ? 17.626  -15.777 -29.234 1.00 30.24 ? 165  GLN B CA  1 
ATOM   4651 C C   . GLN B 1 165 ? 17.591  -17.313 -29.044 1.00 31.79 ? 165  GLN B C   1 
ATOM   4652 O O   . GLN B 1 165 ? 18.406  -17.872 -28.290 1.00 31.97 ? 165  GLN B O   1 
ATOM   4653 C CB  . GLN B 1 165 ? 19.053  -15.260 -29.504 1.00 29.88 ? 165  GLN B CB  1 
ATOM   4654 C CG  . GLN B 1 165 ? 19.757  -15.945 -30.677 1.00 28.64 ? 165  GLN B CG  1 
ATOM   4655 C CD  . GLN B 1 165 ? 21.120  -15.317 -31.044 1.00 30.05 ? 165  GLN B CD  1 
ATOM   4656 O OE1 . GLN B 1 165 ? 21.420  -14.160 -30.712 1.00 31.57 ? 165  GLN B OE1 1 
ATOM   4657 N NE2 . GLN B 1 165 ? 21.938  -16.079 -31.760 1.00 29.00 ? 165  GLN B NE2 1 
ATOM   4658 N N   . PRO B 1 166 ? 16.638  -18.010 -29.714 1.00 32.83 ? 166  PRO B N   1 
ATOM   4659 C CA  . PRO B 1 166 ? 16.386  -19.440 -29.500 1.00 33.03 ? 166  PRO B CA  1 
ATOM   4660 C C   . PRO B 1 166 ? 17.356  -20.310 -30.284 1.00 33.30 ? 166  PRO B C   1 
ATOM   4661 O O   . PRO B 1 166 ? 18.058  -19.789 -31.147 1.00 33.05 ? 166  PRO B O   1 
ATOM   4662 C CB  . PRO B 1 166 ? 14.966  -19.622 -30.020 1.00 33.43 ? 166  PRO B CB  1 
ATOM   4663 C CG  . PRO B 1 166 ? 14.867  -18.645 -31.160 1.00 33.55 ? 166  PRO B CG  1 
ATOM   4664 C CD  . PRO B 1 166 ? 15.780  -17.468 -30.785 1.00 33.41 ? 166  PRO B CD  1 
ATOM   4665 N N   . GLY B 1 167 ? 17.425  -21.604 -29.946 1.00 33.53 ? 167  GLY B N   1 
ATOM   4666 C CA  . GLY B 1 167 ? 18.380  -22.522 -30.574 1.00 33.91 ? 167  GLY B CA  1 
ATOM   4667 C C   . GLY B 1 167 ? 19.872  -22.225 -30.350 1.00 34.13 ? 167  GLY B C   1 
ATOM   4668 O O   . GLY B 1 167 ? 20.728  -22.508 -31.226 1.00 34.39 ? 167  GLY B O   1 
ATOM   4669 N N   . GLN B 1 168 ? 20.188  -21.641 -29.185 1.00 33.48 ? 168  GLN B N   1 
ATOM   4670 C CA  . GLN B 1 168 ? 21.572  -21.561 -28.697 1.00 32.19 ? 168  GLN B CA  1 
ATOM   4671 C C   . GLN B 1 168 ? 21.802  -22.836 -27.921 1.00 31.25 ? 168  GLN B C   1 
ATOM   4672 O O   . GLN B 1 168 ? 20.835  -23.558 -27.597 1.00 31.40 ? 168  GLN B O   1 
ATOM   4673 C CB  . GLN B 1 168 ? 21.783  -20.357 -27.798 1.00 32.28 ? 168  GLN B CB  1 
ATOM   4674 C CG  . GLN B 1 168 ? 21.763  -19.019 -28.532 1.00 33.12 ? 168  GLN B CG  1 
ATOM   4675 C CD  . GLN B 1 168 ? 21.988  -17.855 -27.595 1.00 33.52 ? 168  GLN B CD  1 
ATOM   4676 O OE1 . GLN B 1 168 ? 21.270  -17.688 -26.606 1.00 31.38 ? 168  GLN B OE1 1 
ATOM   4677 N NE2 . GLN B 1 168 ? 22.978  -17.037 -27.900 1.00 33.04 ? 168  GLN B NE2 1 
ATOM   4678 N N   . SER B 1 169 ? 23.059  -23.157 -27.625 1.00 30.07 ? 169  SER B N   1 
ATOM   4679 C CA  . SER B 1 169 ? 23.280  -24.366 -26.812 1.00 28.94 ? 169  SER B CA  1 
ATOM   4680 C C   . SER B 1 169 ? 22.621  -24.203 -25.451 1.00 28.04 ? 169  SER B C   1 
ATOM   4681 O O   . SER B 1 169 ? 22.444  -23.094 -24.946 1.00 27.60 ? 169  SER B O   1 
ATOM   4682 C CB  . SER B 1 169 ? 24.754  -24.756 -26.713 1.00 28.15 ? 169  SER B CB  1 
ATOM   4683 O OG  . SER B 1 169 ? 25.503  -23.650 -26.345 1.00 28.56 ? 169  SER B OG  1 
ATOM   4684 N N   . SER B 1 170 ? 22.170  -25.318 -24.911 1.00 27.98 ? 170  SER B N   1 
ATOM   4685 C CA  . SER B 1 170 ? 21.822  -25.396 -23.490 1.00 28.26 ? 170  SER B CA  1 
ATOM   4686 C C   . SER B 1 170 ? 22.860  -24.738 -22.556 1.00 26.24 ? 170  SER B C   1 
ATOM   4687 O O   . SER B 1 170 ? 24.086  -24.814 -22.777 1.00 24.83 ? 170  SER B O   1 
ATOM   4688 C CB  . SER B 1 170 ? 21.659  -26.874 -23.079 1.00 28.94 ? 170  SER B CB  1 
ATOM   4689 O OG  . SER B 1 170 ? 20.308  -27.288 -23.232 1.00 33.66 ? 170  SER B OG  1 
ATOM   4690 N N   . PRO B 1 171 ? 22.372  -24.093 -21.499 1.00 25.46 ? 171  PRO B N   1 
ATOM   4691 C CA  . PRO B 1 171 ? 23.299  -23.945 -20.383 1.00 25.19 ? 171  PRO B CA  1 
ATOM   4692 C C   . PRO B 1 171 ? 23.483  -25.327 -19.715 1.00 25.11 ? 171  PRO B C   1 
ATOM   4693 O O   . PRO B 1 171 ? 22.540  -26.139 -19.677 1.00 25.29 ? 171  PRO B O   1 
ATOM   4694 C CB  . PRO B 1 171 ? 22.580  -22.964 -19.474 1.00 25.44 ? 171  PRO B CB  1 
ATOM   4695 C CG  . PRO B 1 171 ? 21.137  -23.069 -19.835 1.00 25.02 ? 171  PRO B CG  1 
ATOM   4696 C CD  . PRO B 1 171 ? 21.040  -23.540 -21.228 1.00 24.87 ? 171  PRO B CD  1 
ATOM   4697 N N   . LYS B 1 172 ? 24.683  -25.628 -19.225 1.00 25.13 ? 172  LYS B N   1 
ATOM   4698 C CA  . LYS B 1 172 ? 24.928  -26.909 -18.552 1.00 24.66 ? 172  LYS B CA  1 
ATOM   4699 C C   . LYS B 1 172 ? 25.932  -26.675 -17.443 1.00 24.72 ? 172  LYS B C   1 
ATOM   4700 O O   . LYS B 1 172 ? 26.422  -25.545 -17.307 1.00 25.35 ? 172  LYS B O   1 
ATOM   4701 C CB  . LYS B 1 172 ? 25.502  -27.888 -19.544 1.00 24.67 ? 172  LYS B CB  1 
ATOM   4702 C CG  . LYS B 1 172 ? 26.759  -27.319 -20.186 1.00 26.12 ? 172  LYS B CG  1 
ATOM   4703 C CD  . LYS B 1 172 ? 27.404  -28.222 -21.167 1.00 24.62 ? 172  LYS B CD  1 
ATOM   4704 C CE  . LYS B 1 172 ? 28.122  -27.380 -22.163 1.00 25.57 ? 172  LYS B CE  1 
ATOM   4705 N NZ  . LYS B 1 172 ? 29.011  -28.303 -22.859 1.00 29.73 ? 172  LYS B NZ  1 
ATOM   4706 N N   . ILE B 1 173 ? 26.257  -27.720 -16.661 1.00 23.84 ? 173  ILE B N   1 
ATOM   4707 C CA  . ILE B 1 173 ? 27.352  -27.612 -15.715 1.00 22.53 ? 173  ILE B CA  1 
ATOM   4708 C C   . ILE B 1 173 ? 28.687  -27.854 -16.405 1.00 23.35 ? 173  ILE B C   1 
ATOM   4709 O O   . ILE B 1 173 ? 29.069  -28.981 -16.680 1.00 24.08 ? 173  ILE B O   1 
ATOM   4710 C CB  . ILE B 1 173 ? 27.188  -28.525 -14.508 1.00 22.03 ? 173  ILE B CB  1 
ATOM   4711 C CG1 . ILE B 1 173 ? 25.903  -28.181 -13.793 1.00 18.68 ? 173  ILE B CG1 1 
ATOM   4712 C CG2 . ILE B 1 173 ? 28.366  -28.333 -13.557 1.00 21.03 ? 173  ILE B CG2 1 
ATOM   4713 C CD1 . ILE B 1 173 ? 25.623  -29.117 -12.683 1.00 19.05 ? 173  ILE B CD1 1 
ATOM   4714 N N   . ASP B 1 174 ? 29.392  -26.780 -16.692 1.00 23.75 ? 174  ASP B N   1 
ATOM   4715 C CA  . ASP B 1 174 ? 30.544  -26.872 -17.554 1.00 24.98 ? 174  ASP B CA  1 
ATOM   4716 C C   . ASP B 1 174 ? 31.703  -27.553 -16.901 1.00 25.62 ? 174  ASP B C   1 
ATOM   4717 O O   . ASP B 1 174 ? 32.575  -28.081 -17.576 1.00 26.88 ? 174  ASP B O   1 
ATOM   4718 C CB  . ASP B 1 174 ? 30.981  -25.488 -18.000 1.00 25.02 ? 174  ASP B CB  1 
ATOM   4719 C CG  . ASP B 1 174 ? 29.930  -24.789 -18.847 1.00 26.05 ? 174  ASP B CG  1 
ATOM   4720 O OD1 . ASP B 1 174 ? 29.896  -25.053 -20.057 1.00 28.60 ? 174  ASP B OD1 1 
ATOM   4721 O OD2 . ASP B 1 174 ? 29.167  -23.970 -18.311 1.00 24.39 ? 174  ASP B OD2 1 
ATOM   4722 N N   . VAL B 1 175 ? 31.747  -27.507 -15.579 1.00 25.93 ? 175  VAL B N   1 
ATOM   4723 C CA  . VAL B 1 175 ? 32.901  -27.981 -14.856 1.00 25.01 ? 175  VAL B CA  1 
ATOM   4724 C C   . VAL B 1 175 ? 32.339  -28.414 -13.520 1.00 25.38 ? 175  VAL B C   1 
ATOM   4725 O O   . VAL B 1 175 ? 31.759  -27.591 -12.792 1.00 25.37 ? 175  VAL B O   1 
ATOM   4726 C CB  . VAL B 1 175 ? 33.939  -26.857 -14.635 1.00 24.65 ? 175  VAL B CB  1 
ATOM   4727 C CG1 . VAL B 1 175 ? 34.982  -27.277 -13.602 1.00 23.44 ? 175  VAL B CG1 1 
ATOM   4728 C CG2 . VAL B 1 175 ? 34.610  -26.464 -15.915 1.00 24.50 ? 175  VAL B CG2 1 
ATOM   4729 N N   . VAL B 1 176 ? 32.477  -29.709 -13.220 1.00 25.83 ? 176  VAL B N   1 
ATOM   4730 C CA  . VAL B 1 176 ? 32.304  -30.204 -11.855 1.00 25.77 ? 176  VAL B CA  1 
ATOM   4731 C C   . VAL B 1 176 ? 33.685  -30.176 -11.206 1.00 25.97 ? 176  VAL B C   1 
ATOM   4732 O O   . VAL B 1 176 ? 34.621  -30.851 -11.703 1.00 26.08 ? 176  VAL B O   1 
ATOM   4733 C CB  . VAL B 1 176 ? 31.765  -31.642 -11.828 1.00 26.09 ? 176  VAL B CB  1 
ATOM   4734 C CG1 . VAL B 1 176 ? 31.589  -32.109 -10.380 1.00 27.14 ? 176  VAL B CG1 1 
ATOM   4735 C CG2 . VAL B 1 176 ? 30.454  -31.743 -12.568 1.00 25.11 ? 176  VAL B CG2 1 
ATOM   4736 N N   . ILE B 1 177 ? 33.819  -29.378 -10.135 1.00 24.93 ? 177  ILE B N   1 
ATOM   4737 C CA  . ILE B 1 177 ? 35.056  -29.320 -9.363  1.00 23.59 ? 177  ILE B CA  1 
ATOM   4738 C C   . ILE B 1 177 ? 35.044  -30.340 -8.209  1.00 23.63 ? 177  ILE B C   1 
ATOM   4739 O O   . ILE B 1 177 ? 34.137  -30.357 -7.365  1.00 23.39 ? 177  ILE B O   1 
ATOM   4740 C CB  . ILE B 1 177 ? 35.322  -27.944 -8.718  1.00 23.39 ? 177  ILE B CB  1 
ATOM   4741 C CG1 . ILE B 1 177 ? 35.250  -26.807 -9.720  1.00 21.51 ? 177  ILE B CG1 1 
ATOM   4742 C CG2 . ILE B 1 177 ? 36.663  -27.963 -8.032  1.00 21.83 ? 177  ILE B CG2 1 
ATOM   4743 C CD1 . ILE B 1 177 ? 35.615  -25.473 -9.110  1.00 20.94 ? 177  ILE B CD1 1 
ATOM   4744 N N   . SER B 1 178 ? 36.105  -31.130 -8.144  1.00 23.46 ? 178  SER B N   1 
ATOM   4745 C CA  . SER B 1 178 ? 36.230  -32.174 -7.143  1.00 23.96 ? 178  SER B CA  1 
ATOM   4746 C C   . SER B 1 178 ? 36.357  -31.720 -5.673  1.00 24.18 ? 178  SER B C   1 
ATOM   4747 O O   . SER B 1 178 ? 37.020  -30.739 -5.353  1.00 23.61 ? 178  SER B O   1 
ATOM   4748 C CB  . SER B 1 178 ? 37.399  -33.101 -7.513  1.00 23.41 ? 178  SER B CB  1 
ATOM   4749 O OG  . SER B 1 178 ? 37.504  -34.140 -6.559  1.00 24.63 ? 178  SER B OG  1 
ATOM   4750 N N   . GLU B 1 179 ? 35.722  -32.485 -4.798  1.00 24.62 ? 179  GLU B N   1 
ATOM   4751 C CA  . GLU B 1 179 ? 35.831  -32.338 -3.360  1.00 25.18 ? 179  GLU B CA  1 
ATOM   4752 C C   . GLU B 1 179 ? 36.857  -33.293 -2.701  1.00 25.38 ? 179  GLU B C   1 
ATOM   4753 O O   . GLU B 1 179 ? 37.047  -33.238 -1.483  1.00 24.25 ? 179  GLU B O   1 
ATOM   4754 C CB  . GLU B 1 179 ? 34.454  -32.542 -2.733  1.00 25.21 ? 179  GLU B CB  1 
ATOM   4755 C CG  . GLU B 1 179 ? 33.464  -31.511 -3.231  1.00 27.33 ? 179  GLU B CG  1 
ATOM   4756 C CD  . GLU B 1 179 ? 32.228  -31.335 -2.352  1.00 29.81 ? 179  GLU B CD  1 
ATOM   4757 O OE1 . GLU B 1 179 ? 31.880  -32.209 -1.527  1.00 29.94 ? 179  GLU B OE1 1 
ATOM   4758 O OE2 . GLU B 1 179 ? 31.593  -30.277 -2.512  1.00 33.17 ? 179  GLU B OE2 1 
ATOM   4759 N N   . ALA B 1 180 ? 37.510  -34.163 -3.489  1.00 26.12 ? 180  ALA B N   1 
ATOM   4760 C CA  . ALA B 1 180 ? 38.524  -35.086 -2.905  1.00 26.77 ? 180  ALA B CA  1 
ATOM   4761 C C   . ALA B 1 180 ? 39.520  -34.250 -2.146  1.00 27.47 ? 180  ALA B C   1 
ATOM   4762 O O   . ALA B 1 180 ? 39.811  -33.107 -2.529  1.00 27.82 ? 180  ALA B O   1 
ATOM   4763 C CB  . ALA B 1 180 ? 39.244  -35.918 -3.950  1.00 26.14 ? 180  ALA B CB  1 
ATOM   4764 N N   . SER B 1 181 ? 40.036  -34.829 -1.072  1.00 28.04 ? 181  SER B N   1 
ATOM   4765 C CA  . SER B 1 181 ? 40.874  -34.124 -0.104  1.00 28.29 ? 181  SER B CA  1 
ATOM   4766 C C   . SER B 1 181 ? 42.093  -33.492 -0.755  1.00 27.72 ? 181  SER B C   1 
ATOM   4767 O O   . SER B 1 181 ? 42.653  -32.566 -0.195  1.00 28.44 ? 181  SER B O   1 
ATOM   4768 C CB  . SER B 1 181 ? 41.271  -35.066 1.052   1.00 28.66 ? 181  SER B CB  1 
ATOM   4769 O OG  . SER B 1 181 ? 41.584  -36.382 0.547   1.00 29.40 ? 181  SER B OG  1 
ATOM   4770 N N   . SER B 1 182 ? 42.489  -33.960 -1.940  1.00 27.01 ? 182  SER B N   1 
ATOM   4771 C CA  . SER B 1 182 ? 43.639  -33.366 -2.613  1.00 26.68 ? 182  SER B CA  1 
ATOM   4772 C C   . SER B 1 182 ? 43.270  -32.394 -3.723  1.00 25.86 ? 182  SER B C   1 
ATOM   4773 O O   . SER B 1 182 ? 44.169  -31.906 -4.434  1.00 25.90 ? 182  SER B O   1 
ATOM   4774 C CB  . SER B 1 182 ? 44.529  -34.440 -3.214  1.00 27.21 ? 182  SER B CB  1 
ATOM   4775 O OG  . SER B 1 182 ? 43.941  -34.965 -4.401  1.00 28.72 ? 182  SER B OG  1 
ATOM   4776 N N   . SER B 1 183 ? 41.968  -32.150 -3.898  1.00 24.06 ? 183  SER B N   1 
ATOM   4777 C CA  . SER B 1 183 ? 41.484  -31.274 -4.956  1.00 23.27 ? 183  SER B CA  1 
ATOM   4778 C C   . SER B 1 183 ? 41.555  -29.772 -4.594  1.00 22.47 ? 183  SER B C   1 
ATOM   4779 O O   . SER B 1 183 ? 40.934  -29.336 -3.604  1.00 23.01 ? 183  SER B O   1 
ATOM   4780 C CB  . SER B 1 183 ? 40.044  -31.647 -5.317  1.00 23.85 ? 183  SER B CB  1 
ATOM   4781 O OG  . SER B 1 183 ? 39.547  -30.833 -6.369  1.00 22.15 ? 183  SER B OG  1 
ATOM   4782 N N   . ASN B 1 184 ? 42.302  -28.992 -5.384  1.00 20.61 ? 184  ASN B N   1 
ATOM   4783 C CA  . ASN B 1 184 ? 42.266  -27.529 -5.244  1.00 19.26 ? 184  ASN B CA  1 
ATOM   4784 C C   . ASN B 1 184 ? 40.864  -27.082 -5.659  1.00 18.15 ? 184  ASN B C   1 
ATOM   4785 O O   . ASN B 1 184 ? 40.571  -26.997 -6.827  1.00 18.24 ? 184  ASN B O   1 
ATOM   4786 C CB  . ASN B 1 184 ? 43.397  -26.846 -6.048  1.00 18.94 ? 184  ASN B CB  1 
ATOM   4787 C CG  . ASN B 1 184 ? 44.777  -27.203 -5.521  1.00 19.60 ? 184  ASN B CG  1 
ATOM   4788 O OD1 . ASN B 1 184 ? 44.869  -27.827 -4.469  1.00 22.47 ? 184  ASN B OD1 1 
ATOM   4789 N ND2 . ASN B 1 184 ? 45.864  -26.813 -6.230  1.00 19.77 ? 184  ASN B ND2 1 
ATOM   4790 N N   . ASN B 1 185 ? 39.969  -26.867 -4.695  1.00 17.86 ? 185  ASN B N   1 
ATOM   4791 C CA  . ASN B 1 185 ? 38.572  -26.497 -4.989  1.00 16.76 ? 185  ASN B CA  1 
ATOM   4792 C C   . ASN B 1 185 ? 38.268  -25.073 -4.481  1.00 17.14 ? 185  ASN B C   1 
ATOM   4793 O O   . ASN B 1 185 ? 38.229  -24.873 -3.259  1.00 17.36 ? 185  ASN B O   1 
ATOM   4794 C CB  . ASN B 1 185 ? 37.675  -27.520 -4.324  1.00 16.00 ? 185  ASN B CB  1 
ATOM   4795 C CG  . ASN B 1 185 ? 36.192  -27.209 -4.463  1.00 17.26 ? 185  ASN B CG  1 
ATOM   4796 O OD1 . ASN B 1 185 ? 35.350  -28.088 -4.275  1.00 18.01 ? 185  ASN B OD1 1 
ATOM   4797 N ND2 . ASN B 1 185 ? 35.856  -25.975 -4.810  1.00 19.46 ? 185  ASN B ND2 1 
ATOM   4798 N N   . THR B 1 186 ? 38.015  -24.085 -5.353  1.00 16.60 ? 186  THR B N   1 
ATOM   4799 C CA  . THR B 1 186 ? 37.843  -22.708 -4.834  1.00 17.34 ? 186  THR B CA  1 
ATOM   4800 C C   . THR B 1 186 ? 36.449  -22.443 -4.268  1.00 18.19 ? 186  THR B C   1 
ATOM   4801 O O   . THR B 1 186 ? 36.204  -21.430 -3.588  1.00 17.89 ? 186  THR B O   1 
ATOM   4802 C CB  . THR B 1 186 ? 38.148  -21.598 -5.860  1.00 16.85 ? 186  THR B CB  1 
ATOM   4803 O OG1 . THR B 1 186 ? 37.284  -21.741 -6.977  1.00 19.07 ? 186  THR B OG1 1 
ATOM   4804 C CG2 . THR B 1 186 ? 39.550  -21.658 -6.358  1.00 15.76 ? 186  THR B CG2 1 
ATOM   4805 N N   . LEU B 1 187 ? 35.535  -23.354 -4.551  1.00 19.23 ? 187  LEU B N   1 
ATOM   4806 C CA  . LEU B 1 187 ? 34.142  -23.191 -4.123  1.00 20.47 ? 187  LEU B CA  1 
ATOM   4807 C C   . LEU B 1 187 ? 33.981  -23.550 -2.662  1.00 20.55 ? 187  LEU B C   1 
ATOM   4808 O O   . LEU B 1 187 ? 33.071  -23.053 -2.020  1.00 20.72 ? 187  LEU B O   1 
ATOM   4809 C CB  . LEU B 1 187 ? 33.188  -24.023 -5.001  1.00 20.26 ? 187  LEU B CB  1 
ATOM   4810 C CG  . LEU B 1 187 ? 33.203  -23.768 -6.522  1.00 21.06 ? 187  LEU B CG  1 
ATOM   4811 C CD1 . LEU B 1 187 ? 32.222  -24.690 -7.238  1.00 18.10 ? 187  LEU B CD1 1 
ATOM   4812 C CD2 . LEU B 1 187 ? 32.906  -22.320 -6.862  1.00 18.43 ? 187  LEU B CD2 1 
ATOM   4813 N N   . ASP B 1 188 ? 34.877  -24.406 -2.150  1.00 21.17 ? 188  ASP B N   1 
ATOM   4814 C CA  . ASP B 1 188 ? 34.851  -24.864 -0.743  1.00 22.11 ? 188  ASP B CA  1 
ATOM   4815 C C   . ASP B 1 188 ? 36.158  -25.633 -0.476  1.00 21.50 ? 188  ASP B C   1 
ATOM   4816 O O   . ASP B 1 188 ? 36.166  -26.874 -0.508  1.00 21.21 ? 188  ASP B O   1 
ATOM   4817 C CB  . ASP B 1 188 ? 33.630  -25.738 -0.501  1.00 22.95 ? 188  ASP B CB  1 
ATOM   4818 C CG  . ASP B 1 188 ? 33.514  -26.224 0.937   1.00 27.47 ? 188  ASP B CG  1 
ATOM   4819 O OD1 . ASP B 1 188 ? 32.881  -25.553 1.787   1.00 30.14 ? 188  ASP B OD1 1 
ATOM   4820 O OD2 . ASP B 1 188 ? 34.019  -27.333 1.202   1.00 35.59 ? 188  ASP B OD2 1 
ATOM   4821 N N   . PRO B 1 189 ? 37.278  -24.892 -0.269  1.00 20.82 ? 189  PRO B N   1 
ATOM   4822 C CA  . PRO B 1 189 ? 38.604  -25.499 -0.274  1.00 20.72 ? 189  PRO B CA  1 
ATOM   4823 C C   . PRO B 1 189 ? 38.793  -26.529 0.821   1.00 20.98 ? 189  PRO B C   1 
ATOM   4824 O O   . PRO B 1 189 ? 38.180  -26.439 1.872   1.00 19.50 ? 189  PRO B O   1 
ATOM   4825 C CB  . PRO B 1 189 ? 39.537  -24.317 -0.068  1.00 20.28 ? 189  PRO B CB  1 
ATOM   4826 C CG  . PRO B 1 189 ? 38.738  -23.162 -0.371  1.00 19.81 ? 189  PRO B CG  1 
ATOM   4827 C CD  . PRO B 1 189 ? 37.358  -23.437 -0.058  1.00 19.66 ? 189  PRO B CD  1 
ATOM   4828 N N   . GLY B 1 190 ? 39.621  -27.525 0.546   1.00 21.61 ? 190  GLY B N   1 
ATOM   4829 C CA  . GLY B 1 190 ? 39.775  -28.613 1.494   1.00 23.31 ? 190  GLY B CA  1 
ATOM   4830 C C   . GLY B 1 190 ? 41.217  -28.934 1.773   1.00 24.05 ? 190  GLY B C   1 
ATOM   4831 O O   . GLY B 1 190 ? 41.507  -29.952 2.399   1.00 24.82 ? 190  GLY B O   1 
ATOM   4832 N N   . THR B 1 191 ? 42.121  -28.082 1.303   1.00 24.47 ? 191  THR B N   1 
ATOM   4833 C CA  . THR B 1 191 ? 43.539  -28.403 1.370   1.00 25.68 ? 191  THR B CA  1 
ATOM   4834 C C   . THR B 1 191 ? 44.318  -27.688 2.454   1.00 25.86 ? 191  THR B C   1 
ATOM   4835 O O   . THR B 1 191 ? 45.447  -28.034 2.694   1.00 26.58 ? 191  THR B O   1 
ATOM   4836 C CB  . THR B 1 191 ? 44.275  -28.162 0.023   1.00 25.67 ? 191  THR B CB  1 
ATOM   4837 O OG1 . THR B 1 191 ? 43.718  -27.009 -0.652  1.00 25.97 ? 191  THR B OG1 1 
ATOM   4838 C CG2 . THR B 1 191 ? 44.183  -29.392 -0.846  1.00 26.02 ? 191  THR B CG2 1 
ATOM   4839 N N   . CYS B 1 192 ? 43.736  -26.688 3.087   1.00 26.39 ? 192  CYS B N   1 
ATOM   4840 C CA  . CYS B 1 192 ? 44.436  -25.936 4.128   1.00 27.56 ? 192  CYS B CA  1 
ATOM   4841 C C   . CYS B 1 192 ? 44.472  -26.755 5.434   1.00 28.02 ? 192  CYS B C   1 
ATOM   4842 O O   . CYS B 1 192 ? 43.572  -26.677 6.268   1.00 27.82 ? 192  CYS B O   1 
ATOM   4843 C CB  . CYS B 1 192 ? 43.738  -24.587 4.314   1.00 27.85 ? 192  CYS B CB  1 
ATOM   4844 S SG  . CYS B 1 192 ? 44.493  -23.361 5.367   1.00 30.42 ? 192  CYS B SG  1 
ATOM   4845 N N   . THR B 1 193 ? 45.517  -27.561 5.588   1.00 28.64 ? 193  THR B N   1 
ATOM   4846 C CA  . THR B 1 193 ? 45.632  -28.505 6.714   1.00 29.44 ? 193  THR B CA  1 
ATOM   4847 C C   . THR B 1 193 ? 45.392  -27.924 8.120   1.00 28.35 ? 193  THR B C   1 
ATOM   4848 O O   . THR B 1 193 ? 44.696  -28.531 8.931   1.00 28.36 ? 193  THR B O   1 
ATOM   4849 C CB  . THR B 1 193 ? 47.014  -29.131 6.712   1.00 29.95 ? 193  THR B CB  1 
ATOM   4850 O OG1 . THR B 1 193 ? 47.383  -29.412 5.365   1.00 31.26 ? 193  THR B OG1 1 
ATOM   4851 C CG2 . THR B 1 193 ? 47.030  -30.415 7.530   1.00 32.13 ? 193  THR B CG2 1 
ATOM   4852 N N   . VAL B 1 194 ? 45.979  -26.763 8.404   1.00 27.94 ? 194  VAL B N   1 
ATOM   4853 C CA  . VAL B 1 194 ? 45.839  -26.171 9.728   1.00 27.21 ? 194  VAL B CA  1 
ATOM   4854 C C   . VAL B 1 194 ? 44.370  -25.803 9.975   1.00 28.06 ? 194  VAL B C   1 
ATOM   4855 O O   . VAL B 1 194 ? 43.843  -26.110 11.068  1.00 28.31 ? 194  VAL B O   1 
ATOM   4856 C CB  . VAL B 1 194 ? 46.859  -25.042 9.990   1.00 27.24 ? 194  VAL B CB  1 
ATOM   4857 C CG1 . VAL B 1 194 ? 46.572  -24.323 11.321  1.00 26.81 ? 194  VAL B CG1 1 
ATOM   4858 C CG2 . VAL B 1 194 ? 48.262  -25.622 10.025  1.00 26.07 ? 194  VAL B CG2 1 
ATOM   4859 N N   . PHE B 1 195 ? 43.704  -25.233 8.949   1.00 27.20 ? 195  PHE B N   1 
ATOM   4860 C CA  . PHE B 1 195 ? 42.300  -24.860 9.030   1.00 26.56 ? 195  PHE B CA  1 
ATOM   4861 C C   . PHE B 1 195 ? 41.376  -26.088 9.174   1.00 27.92 ? 195  PHE B C   1 
ATOM   4862 O O   . PHE B 1 195 ? 40.392  -26.086 9.946   1.00 27.14 ? 195  PHE B O   1 
ATOM   4863 C CB  . PHE B 1 195 ? 41.870  -23.973 7.841   1.00 25.80 ? 195  PHE B CB  1 
ATOM   4864 C CG  . PHE B 1 195 ? 40.393  -23.772 7.768   1.00 21.00 ? 195  PHE B CG  1 
ATOM   4865 C CD1 . PHE B 1 195 ? 39.768  -22.846 8.608   1.00 19.66 ? 195  PHE B CD1 1 
ATOM   4866 C CD2 . PHE B 1 195 ? 39.598  -24.576 6.939   1.00 16.82 ? 195  PHE B CD2 1 
ATOM   4867 C CE1 . PHE B 1 195 ? 38.373  -22.674 8.599   1.00 13.51 ? 195  PHE B CE1 1 
ATOM   4868 C CE2 . PHE B 1 195 ? 38.205  -24.421 6.928   1.00 12.78 ? 195  PHE B CE2 1 
ATOM   4869 C CZ  . PHE B 1 195 ? 37.608  -23.461 7.766   1.00 10.51 ? 195  PHE B CZ  1 
ATOM   4870 N N   . GLU B 1 196 ? 41.680  -27.138 8.424   1.00 29.29 ? 196  GLU B N   1 
ATOM   4871 C CA  . GLU B 1 196 ? 40.862  -28.348 8.517   1.00 31.03 ? 196  GLU B CA  1 
ATOM   4872 C C   . GLU B 1 196 ? 40.853  -28.920 9.951   1.00 32.10 ? 196  GLU B C   1 
ATOM   4873 O O   . GLU B 1 196 ? 39.893  -29.577 10.340  1.00 32.49 ? 196  GLU B O   1 
ATOM   4874 C CB  . GLU B 1 196 ? 41.302  -29.397 7.483   1.00 31.18 ? 196  GLU B CB  1 
ATOM   4875 C CG  . GLU B 1 196 ? 40.866  -29.083 6.005   1.00 30.80 ? 196  GLU B CG  1 
ATOM   4876 C CD  . GLU B 1 196 ? 39.367  -28.703 5.864   1.00 32.45 ? 196  GLU B CD  1 
ATOM   4877 O OE1 . GLU B 1 196 ? 38.488  -29.359 6.511   1.00 31.79 ? 196  GLU B OE1 1 
ATOM   4878 O OE2 . GLU B 1 196 ? 39.060  -27.744 5.100   1.00 30.78 ? 196  GLU B OE2 1 
ATOM   4879 N N   . ASP B 1 197 ? 41.920  -28.650 10.720  1.00 32.25 ? 197  ASP B N   1 
ATOM   4880 C CA  . ASP B 1 197 ? 42.086  -29.169 12.085  1.00 32.79 ? 197  ASP B CA  1 
ATOM   4881 C C   . ASP B 1 197 ? 41.500  -28.247 13.193  1.00 33.30 ? 197  ASP B C   1 
ATOM   4882 O O   . ASP B 1 197 ? 41.261  -28.710 14.316  1.00 33.92 ? 197  ASP B O   1 
ATOM   4883 C CB  . ASP B 1 197 ? 43.585  -29.405 12.385  1.00 33.20 ? 197  ASP B CB  1 
ATOM   4884 C CG  . ASP B 1 197 ? 44.146  -30.711 11.776  1.00 32.12 ? 197  ASP B CG  1 
ATOM   4885 O OD1 . ASP B 1 197 ? 43.431  -31.496 11.153  1.00 32.35 ? 197  ASP B OD1 1 
ATOM   4886 O OD2 . ASP B 1 197 ? 45.343  -30.959 11.927  1.00 31.90 ? 197  ASP B OD2 1 
ATOM   4887 N N   . SER B 1 198 ? 41.279  -26.965 12.880  1.00 32.96 ? 198  SER B N   1 
ATOM   4888 C CA  . SER B 1 198 ? 40.762  -25.965 13.836  1.00 32.94 ? 198  SER B CA  1 
ATOM   4889 C C   . SER B 1 198 ? 39.570  -26.457 14.670  1.00 33.48 ? 198  SER B C   1 
ATOM   4890 O O   . SER B 1 198 ? 38.701  -27.150 14.156  1.00 33.44 ? 198  SER B O   1 
ATOM   4891 C CB  . SER B 1 198 ? 40.372  -24.658 13.105  1.00 32.82 ? 198  SER B CB  1 
ATOM   4892 O OG  . SER B 1 198 ? 39.796  -23.695 13.986  1.00 30.63 ? 198  SER B OG  1 
ATOM   4893 N N   . GLU B 1 199 ? 39.533  -26.071 15.945  1.00 33.68 ? 199  GLU B N   1 
ATOM   4894 C CA  . GLU B 1 199 ? 38.444  -26.475 16.831  1.00 34.31 ? 199  GLU B CA  1 
ATOM   4895 C C   . GLU B 1 199 ? 37.870  -25.248 17.540  1.00 33.12 ? 199  GLU B C   1 
ATOM   4896 O O   . GLU B 1 199 ? 37.131  -25.376 18.513  1.00 34.04 ? 199  GLU B O   1 
ATOM   4897 C CB  . GLU B 1 199 ? 38.900  -27.580 17.835  1.00 35.25 ? 199  GLU B CB  1 
ATOM   4898 C CG  . GLU B 1 199 ? 39.519  -28.840 17.169  1.00 39.35 ? 199  GLU B CG  1 
ATOM   4899 C CD  . GLU B 1 199 ? 40.153  -29.876 18.155  1.00 46.38 ? 199  GLU B CD  1 
ATOM   4900 O OE1 . GLU B 1 199 ? 41.095  -29.521 18.925  1.00 47.33 ? 199  GLU B OE1 1 
ATOM   4901 O OE2 . GLU B 1 199 ? 39.723  -31.065 18.126  1.00 47.01 ? 199  GLU B OE2 1 
ATOM   4902 N N   . LEU B 1 200 ? 38.198  -24.056 17.044  1.00 32.12 ? 200  LEU B N   1 
ATOM   4903 C CA  . LEU B 1 200 ? 37.650  -22.804 17.588  1.00 30.72 ? 200  LEU B CA  1 
ATOM   4904 C C   . LEU B 1 200 ? 36.092  -22.754 17.598  1.00 30.66 ? 200  LEU B C   1 
ATOM   4905 O O   . LEU B 1 200 ? 35.486  -22.387 18.613  1.00 30.83 ? 200  LEU B O   1 
ATOM   4906 C CB  . LEU B 1 200 ? 38.283  -21.592 16.871  1.00 30.29 ? 200  LEU B CB  1 
ATOM   4907 C CG  . LEU B 1 200 ? 37.882  -20.127 17.210  1.00 30.65 ? 200  LEU B CG  1 
ATOM   4908 C CD1 . LEU B 1 200 ? 37.952  -19.807 18.682  1.00 28.67 ? 200  LEU B CD1 1 
ATOM   4909 C CD2 . LEU B 1 200 ? 38.740  -19.138 16.460  1.00 27.55 ? 200  LEU B CD2 1 
ATOM   4910 N N   . ALA B 1 201 ? 35.460  -23.132 16.486  1.00 29.81 ? 201  ALA B N   1 
ATOM   4911 C CA  . ALA B 1 201 ? 33.995  -23.180 16.374  1.00 30.04 ? 201  ALA B CA  1 
ATOM   4912 C C   . ALA B 1 201 ? 33.293  -24.028 17.445  1.00 29.77 ? 201  ALA B C   1 
ATOM   4913 O O   . ALA B 1 201 ? 32.330  -23.584 18.055  1.00 28.89 ? 201  ALA B O   1 
ATOM   4914 C CB  . ALA B 1 201 ? 33.578  -23.642 14.951  1.00 29.71 ? 201  ALA B CB  1 
ATOM   4915 N N   . ASP B 1 202 ? 33.783  -25.254 17.658  1.00 30.66 ? 202  ASP B N   1 
ATOM   4916 C CA  . ASP B 1 202 ? 33.323  -26.124 18.757  1.00 31.25 ? 202  ASP B CA  1 
ATOM   4917 C C   . ASP B 1 202 ? 33.391  -25.451 20.127  1.00 31.24 ? 202  ASP B C   1 
ATOM   4918 O O   . ASP B 1 202 ? 32.460  -25.531 20.950  1.00 30.97 ? 202  ASP B O   1 
ATOM   4919 C CB  . ASP B 1 202 ? 34.168  -27.379 18.803  1.00 31.83 ? 202  ASP B CB  1 
ATOM   4920 C CG  . ASP B 1 202 ? 33.889  -28.291 17.668  1.00 34.17 ? 202  ASP B CG  1 
ATOM   4921 O OD1 . ASP B 1 202 ? 32.738  -28.283 17.220  1.00 37.68 ? 202  ASP B OD1 1 
ATOM   4922 O OD2 . ASP B 1 202 ? 34.802  -29.031 17.235  1.00 38.37 ? 202  ASP B OD2 1 
ATOM   4923 N N   . THR B 1 203 ? 34.513  -24.798 20.389  1.00 31.58 ? 203  THR B N   1 
ATOM   4924 C CA  . THR B 1 203 ? 34.676  -24.150 21.686  1.00 31.36 ? 203  THR B CA  1 
ATOM   4925 C C   . THR B 1 203 ? 33.568  -23.131 21.889  1.00 31.33 ? 203  THR B C   1 
ATOM   4926 O O   . THR B 1 203 ? 32.810  -23.234 22.862  1.00 31.55 ? 203  THR B O   1 
ATOM   4927 C CB  . THR B 1 203 ? 36.093  -23.652 21.883  1.00 30.82 ? 203  THR B CB  1 
ATOM   4928 O OG1 . THR B 1 203 ? 36.940  -24.797 21.795  1.00 31.43 ? 203  THR B OG1 1 
ATOM   4929 C CG2 . THR B 1 203 ? 36.292  -23.082 23.275  1.00 31.77 ? 203  THR B CG2 1 
ATOM   4930 N N   . VAL B 1 204 ? 33.414  -22.218 20.928  1.00 31.30 ? 204  VAL B N   1 
ATOM   4931 C CA  . VAL B 1 204 ? 32.334  -21.212 20.962  1.00 30.82 ? 204  VAL B CA  1 
ATOM   4932 C C   . VAL B 1 204 ? 30.933  -21.820 20.987  1.00 30.33 ? 204  VAL B C   1 
ATOM   4933 O O   . VAL B 1 204 ? 30.040  -21.267 21.615  1.00 30.07 ? 204  VAL B O   1 
ATOM   4934 C CB  . VAL B 1 204 ? 32.398  -20.256 19.762  1.00 31.24 ? 204  VAL B CB  1 
ATOM   4935 C CG1 . VAL B 1 204 ? 31.349  -19.141 19.925  1.00 31.32 ? 204  VAL B CG1 1 
ATOM   4936 C CG2 . VAL B 1 204 ? 33.831  -19.672 19.579  1.00 30.19 ? 204  VAL B CG2 1 
ATOM   4937 N N   . GLU B 1 205 ? 30.738  -22.938 20.283  1.00 29.96 ? 205  GLU B N   1 
ATOM   4938 C CA  . GLU B 1 205 ? 29.429  -23.560 20.234  1.00 29.21 ? 205  GLU B CA  1 
ATOM   4939 C C   . GLU B 1 205 ? 29.147  -24.054 21.628  1.00 29.22 ? 205  GLU B C   1 
ATOM   4940 O O   . GLU B 1 205 ? 28.072  -23.795 22.150  1.00 29.21 ? 205  GLU B O   1 
ATOM   4941 C CB  . GLU B 1 205 ? 29.342  -24.712 19.222  1.00 28.96 ? 205  GLU B CB  1 
ATOM   4942 C CG  . GLU B 1 205 ? 27.989  -25.494 19.291  1.00 28.91 ? 205  GLU B CG  1 
ATOM   4943 C CD  . GLU B 1 205 ? 27.808  -26.658 18.258  1.00 29.24 ? 205  GLU B CD  1 
ATOM   4944 O OE1 . GLU B 1 205 ? 28.721  -27.009 17.482  1.00 30.35 ? 205  GLU B OE1 1 
ATOM   4945 O OE2 . GLU B 1 205 ? 26.699  -27.226 18.216  1.00 31.25 ? 205  GLU B OE2 1 
ATOM   4946 N N   . ALA B 1 206 ? 30.109  -24.739 22.253  1.00 29.20 ? 206  ALA B N   1 
ATOM   4947 C CA  . ALA B 1 206 ? 29.874  -25.274 23.621  1.00 28.88 ? 206  ALA B CA  1 
ATOM   4948 C C   . ALA B 1 206 ? 29.684  -24.148 24.619  1.00 28.85 ? 206  ALA B C   1 
ATOM   4949 O O   . ALA B 1 206 ? 28.714  -24.145 25.381  1.00 28.68 ? 206  ALA B O   1 
ATOM   4950 C CB  . ALA B 1 206 ? 30.978  -26.199 24.063  1.00 28.51 ? 206  ALA B CB  1 
ATOM   4951 N N   . ASN B 1 207 ? 30.569  -23.159 24.570  1.00 28.94 ? 207  ASN B N   1 
ATOM   4952 C CA  . ASN B 1 207 ? 30.469  -22.042 25.484  1.00 29.59 ? 207  ASN B CA  1 
ATOM   4953 C C   . ASN B 1 207 ? 29.133  -21.315 25.433  1.00 29.57 ? 207  ASN B C   1 
ATOM   4954 O O   . ASN B 1 207 ? 28.560  -21.031 26.486  1.00 29.78 ? 207  ASN B O   1 
ATOM   4955 C CB  . ASN B 1 207 ? 31.676  -21.102 25.357  1.00 29.87 ? 207  ASN B CB  1 
ATOM   4956 C CG  . ASN B 1 207 ? 32.993  -21.725 25.932  1.00 32.99 ? 207  ASN B CG  1 
ATOM   4957 O OD1 . ASN B 1 207 ? 33.088  -22.944 26.216  1.00 34.12 ? 207  ASN B OD1 1 
ATOM   4958 N ND2 . ASN B 1 207 ? 34.008  -20.874 26.109  1.00 33.51 ? 207  ASN B ND2 1 
ATOM   4959 N N   . PHE B 1 208 ? 28.609  -21.041 24.229  1.00 29.87 ? 208  PHE B N   1 
ATOM   4960 C CA  . PHE B 1 208 ? 27.368  -20.235 24.101  1.00 29.03 ? 208  PHE B CA  1 
ATOM   4961 C C   . PHE B 1 208 ? 26.140  -21.080 24.351  1.00 29.43 ? 208  PHE B C   1 
ATOM   4962 O O   . PHE B 1 208 ? 25.133  -20.558 24.810  1.00 28.80 ? 208  PHE B O   1 
ATOM   4963 C CB  . PHE B 1 208 ? 27.259  -19.499 22.757  1.00 29.03 ? 208  PHE B CB  1 
ATOM   4964 C CG  . PHE B 1 208 ? 25.973  -18.700 22.582  1.00 28.17 ? 208  PHE B CG  1 
ATOM   4965 C CD1 . PHE B 1 208 ? 25.835  -17.414 23.128  1.00 29.14 ? 208  PHE B CD1 1 
ATOM   4966 C CD2 . PHE B 1 208 ? 24.910  -19.216 21.849  1.00 27.44 ? 208  PHE B CD2 1 
ATOM   4967 C CE1 . PHE B 1 208 ? 24.652  -16.665 22.957  1.00 27.43 ? 208  PHE B CE1 1 
ATOM   4968 C CE2 . PHE B 1 208 ? 23.718  -18.484 21.669  1.00 25.85 ? 208  PHE B CE2 1 
ATOM   4969 C CZ  . PHE B 1 208 ? 23.596  -17.202 22.222  1.00 27.49 ? 208  PHE B CZ  1 
ATOM   4970 N N   . THR B 1 209 ? 26.225  -22.377 24.083  1.00 29.71 ? 209  THR B N   1 
ATOM   4971 C CA  . THR B 1 209 ? 25.095  -23.224 24.364  1.00 31.65 ? 209  THR B CA  1 
ATOM   4972 C C   . THR B 1 209 ? 24.904  -23.452 25.853  1.00 32.23 ? 209  THR B C   1 
ATOM   4973 O O   . THR B 1 209 ? 23.829  -23.875 26.285  1.00 33.21 ? 209  THR B O   1 
ATOM   4974 C CB  . THR B 1 209 ? 25.150  -24.615 23.695  1.00 31.40 ? 209  THR B CB  1 
ATOM   4975 O OG1 . THR B 1 209 ? 26.326  -25.289 24.097  1.00 35.14 ? 209  THR B OG1 1 
ATOM   4976 C CG2 . THR B 1 209 ? 25.120  -24.533 22.202  1.00 31.53 ? 209  THR B CG2 1 
ATOM   4977 N N   . ALA B 1 210 ? 25.942  -23.177 26.635  1.00 33.10 ? 210  ALA B N   1 
ATOM   4978 C CA  . ALA B 1 210 ? 25.887  -23.341 28.090  1.00 33.10 ? 210  ALA B CA  1 
ATOM   4979 C C   . ALA B 1 210 ? 25.141  -22.178 28.725  1.00 33.62 ? 210  ALA B C   1 
ATOM   4980 O O   . ALA B 1 210 ? 24.741  -22.241 29.891  1.00 33.61 ? 210  ALA B O   1 
ATOM   4981 C CB  . ALA B 1 210 ? 27.292  -23.476 28.677  1.00 32.82 ? 210  ALA B CB  1 
ATOM   4982 N N   . THR B 1 211 ? 24.942  -21.118 27.952  1.00 33.79 ? 211  THR B N   1 
ATOM   4983 C CA  . THR B 1 211 ? 24.306  -19.936 28.486  1.00 34.36 ? 211  THR B CA  1 
ATOM   4984 C C   . THR B 1 211 ? 22.789  -19.924 28.290  1.00 34.49 ? 211  THR B C   1 
ATOM   4985 O O   . THR B 1 211 ? 22.114  -19.032 28.838  1.00 34.40 ? 211  THR B O   1 
ATOM   4986 C CB  . THR B 1 211 ? 24.852  -18.660 27.821  1.00 34.89 ? 211  THR B CB  1 
ATOM   4987 O OG1 . THR B 1 211 ? 24.458  -18.643 26.445  1.00 35.76 ? 211  THR B OG1 1 
ATOM   4988 C CG2 . THR B 1 211 ? 26.401  -18.586 27.916  1.00 35.98 ? 211  THR B CG2 1 
ATOM   4989 N N   . PHE B 1 212 ? 22.254  -20.858 27.484  1.00 33.83 ? 212  PHE B N   1 
ATOM   4990 C CA  . PHE B 1 212 ? 20.823  -20.791 27.156  1.00 33.27 ? 212  PHE B CA  1 
ATOM   4991 C C   . PHE B 1 212 ? 20.092  -22.115 27.024  1.00 32.07 ? 212  PHE B C   1 
ATOM   4992 O O   . PHE B 1 212 ? 18.896  -22.176 27.292  1.00 31.65 ? 212  PHE B O   1 
ATOM   4993 C CB  . PHE B 1 212 ? 20.560  -19.902 25.928  1.00 33.54 ? 212  PHE B CB  1 
ATOM   4994 C CG  . PHE B 1 212 ? 20.655  -20.622 24.608  1.00 34.24 ? 212  PHE B CG  1 
ATOM   4995 C CD1 . PHE B 1 212 ? 21.861  -20.691 23.926  1.00 31.91 ? 212  PHE B CD1 1 
ATOM   4996 C CD2 . PHE B 1 212 ? 19.516  -21.186 24.030  1.00 34.67 ? 212  PHE B CD2 1 
ATOM   4997 C CE1 . PHE B 1 212 ? 21.939  -21.335 22.713  1.00 32.97 ? 212  PHE B CE1 1 
ATOM   4998 C CE2 . PHE B 1 212 ? 19.576  -21.827 22.807  1.00 34.42 ? 212  PHE B CE2 1 
ATOM   4999 C CZ  . PHE B 1 212 ? 20.794  -21.909 22.141  1.00 34.12 ? 212  PHE B CZ  1 
ATOM   5000 N N   . VAL B 1 213 ? 20.802  -23.156 26.617  1.00 31.26 ? 213  VAL B N   1 
ATOM   5001 C CA  . VAL B 1 213 ? 20.188  -24.477 26.492  1.00 31.05 ? 213  VAL B CA  1 
ATOM   5002 C C   . VAL B 1 213 ? 19.753  -25.186 27.806  1.00 31.04 ? 213  VAL B C   1 
ATOM   5003 O O   . VAL B 1 213 ? 18.680  -25.781 27.820  1.00 30.90 ? 213  VAL B O   1 
ATOM   5004 C CB  . VAL B 1 213 ? 20.998  -25.378 25.559  1.00 31.26 ? 213  VAL B CB  1 
ATOM   5005 C CG1 . VAL B 1 213 ? 20.506  -26.840 25.582  1.00 31.02 ? 213  VAL B CG1 1 
ATOM   5006 C CG2 . VAL B 1 213 ? 20.935  -24.815 24.162  1.00 31.14 ? 213  VAL B CG2 1 
ATOM   5007 N N   . PRO B 1 214 ? 20.557  -25.103 28.906  1.00 30.98 ? 214  PRO B N   1 
ATOM   5008 C CA  . PRO B 1 214 ? 20.140  -25.674 30.224  1.00 30.39 ? 214  PRO B CA  1 
ATOM   5009 C C   . PRO B 1 214 ? 18.694  -25.368 30.687  1.00 29.87 ? 214  PRO B C   1 
ATOM   5010 O O   . PRO B 1 214 ? 18.012  -26.257 31.153  1.00 29.42 ? 214  PRO B O   1 
ATOM   5011 C CB  . PRO B 1 214 ? 21.136  -25.047 31.211  1.00 30.00 ? 214  PRO B CB  1 
ATOM   5012 C CG  . PRO B 1 214 ? 22.400  -24.864 30.388  1.00 31.34 ? 214  PRO B CG  1 
ATOM   5013 C CD  . PRO B 1 214 ? 21.890  -24.452 28.997  1.00 31.30 ? 214  PRO B CD  1 
ATOM   5014 N N   . SER B 1 215 ? 18.243  -24.125 30.547  1.00 29.98 ? 215  SER B N   1 
ATOM   5015 C CA  . SER B 1 215 ? 16.897  -23.729 30.941  1.00 30.49 ? 215  SER B CA  1 
ATOM   5016 C C   . SER B 1 215 ? 15.868  -24.448 30.113  1.00 30.47 ? 215  SER B C   1 
ATOM   5017 O O   . SER B 1 215 ? 14.747  -24.633 30.558  1.00 30.72 ? 215  SER B O   1 
ATOM   5018 C CB  . SER B 1 215 ? 16.672  -22.235 30.706  1.00 30.57 ? 215  SER B CB  1 
ATOM   5019 O OG  . SER B 1 215 ? 17.728  -21.468 31.251  1.00 32.93 ? 215  SER B OG  1 
ATOM   5020 N N   . ILE B 1 216 ? 16.237  -24.801 28.891  1.00 30.19 ? 216  ILE B N   1 
ATOM   5021 C CA  . ILE B 1 216 ? 15.311  -25.444 27.982  1.00 30.36 ? 216  ILE B CA  1 
ATOM   5022 C C   . ILE B 1 216 ? 15.279  -26.898 28.377  1.00 30.32 ? 216  ILE B C   1 
ATOM   5023 O O   . ILE B 1 216 ? 14.195  -27.464 28.581  1.00 30.94 ? 216  ILE B O   1 
ATOM   5024 C CB  . ILE B 1 216 ? 15.713  -25.249 26.476  1.00 30.34 ? 216  ILE B CB  1 
ATOM   5025 C CG1 . ILE B 1 216 ? 15.768  -23.766 26.107  1.00 30.07 ? 216  ILE B CG1 1 
ATOM   5026 C CG2 . ILE B 1 216 ? 14.719  -25.920 25.566  1.00 29.83 ? 216  ILE B CG2 1 
ATOM   5027 C CD1 . ILE B 1 216 ? 16.497  -23.486 24.797  1.00 31.47 ? 216  ILE B CD1 1 
ATOM   5028 N N   . ARG B 1 217 ? 16.472  -27.479 28.540  1.00 29.92 ? 217  ARG B N   1 
ATOM   5029 C CA  . ARG B 1 217 ? 16.622  -28.845 29.043  1.00 29.76 ? 217  ARG B CA  1 
ATOM   5030 C C   . ARG B 1 217 ? 15.784  -29.097 30.303  1.00 29.65 ? 217  ARG B C   1 
ATOM   5031 O O   . ARG B 1 217 ? 15.091  -30.085 30.387  1.00 29.34 ? 217  ARG B O   1 
ATOM   5032 C CB  . ARG B 1 217 ? 18.089  -29.167 29.311  1.00 29.81 ? 217  ARG B CB  1 
ATOM   5033 C CG  . ARG B 1 217 ? 18.303  -30.640 29.728  1.00 31.61 ? 217  ARG B CG  1 
ATOM   5034 C CD  . ARG B 1 217 ? 19.572  -30.895 30.499  1.00 32.45 ? 217  ARG B CD  1 
ATOM   5035 N NE  . ARG B 1 217 ? 19.983  -29.817 31.416  1.00 34.43 ? 217  ARG B NE  1 
ATOM   5036 C CZ  . ARG B 1 217 ? 19.564  -29.669 32.682  1.00 30.65 ? 217  ARG B CZ  1 
ATOM   5037 N NH1 . ARG B 1 217 ? 18.691  -30.500 33.215  1.00 26.20 ? 217  ARG B NH1 1 
ATOM   5038 N NH2 . ARG B 1 217 ? 20.013  -28.653 33.410  1.00 27.80 ? 217  ARG B NH2 1 
ATOM   5039 N N   . GLN B 1 218 ? 15.843  -28.191 31.264  1.00 29.94 ? 218  GLN B N   1 
ATOM   5040 C CA  . GLN B 1 218 ? 15.138  -28.373 32.530  1.00 31.31 ? 218  GLN B CA  1 
ATOM   5041 C C   . GLN B 1 218 ? 13.658  -28.489 32.243  1.00 30.99 ? 218  GLN B C   1 
ATOM   5042 O O   . GLN B 1 218 ? 13.032  -29.505 32.572  1.00 30.29 ? 218  GLN B O   1 
ATOM   5043 C CB  . GLN B 1 218 ? 15.368  -27.181 33.444  1.00 31.34 ? 218  GLN B CB  1 
ATOM   5044 C CG  . GLN B 1 218 ? 15.289  -27.471 34.942  1.00 33.51 ? 218  GLN B CG  1 
ATOM   5045 C CD  . GLN B 1 218 ? 16.190  -26.495 35.722  1.00 35.96 ? 218  GLN B CD  1 
ATOM   5046 O OE1 . GLN B 1 218 ? 16.160  -25.272 35.510  1.00 35.62 ? 218  GLN B OE1 1 
ATOM   5047 N NE2 . GLN B 1 218 ? 17.039  -27.047 36.568  1.00 35.82 ? 218  GLN B NE2 1 
ATOM   5048 N N   . ARG B 1 219 ? 13.135  -27.451 31.585  1.00 31.10 ? 219  ARG B N   1 
ATOM   5049 C CA  . ARG B 1 219 ? 11.737  -27.395 31.199  1.00 31.42 ? 219  ARG B CA  1 
ATOM   5050 C C   . ARG B 1 219 ? 11.300  -28.650 30.466  1.00 31.95 ? 219  ARG B C   1 
ATOM   5051 O O   . ARG B 1 219 ? 10.277  -29.233 30.813  1.00 32.68 ? 219  ARG B O   1 
ATOM   5052 C CB  . ARG B 1 219 ? 11.404  -26.142 30.387  1.00 30.73 ? 219  ARG B CB  1 
ATOM   5053 C CG  . ARG B 1 219 ? 9.889   -25.979 30.210  1.00 31.03 ? 219  ARG B CG  1 
ATOM   5054 C CD  . ARG B 1 219 ? 9.487   -24.796 29.331  1.00 32.12 ? 219  ARG B CD  1 
ATOM   5055 N NE  . ARG B 1 219 ? 9.959   -24.892 27.944  1.00 31.33 ? 219  ARG B NE  1 
ATOM   5056 C CZ  . ARG B 1 219 ? 10.854  -24.077 27.390  1.00 31.67 ? 219  ARG B CZ  1 
ATOM   5057 N NH1 . ARG B 1 219 ? 11.416  -23.090 28.076  1.00 31.27 ? 219  ARG B NH1 1 
ATOM   5058 N NH2 . ARG B 1 219 ? 11.178  -24.235 26.126  1.00 32.19 ? 219  ARG B NH2 1 
ATOM   5059 N N   . LEU B 1 220 ? 12.080  -29.089 29.478  1.00 32.77 ? 220  LEU B N   1 
ATOM   5060 C CA  . LEU B 1 220 ? 11.716  -30.304 28.730  1.00 33.62 ? 220  LEU B CA  1 
ATOM   5061 C C   . LEU B 1 220 ? 11.735  -31.593 29.548  1.00 33.76 ? 220  LEU B C   1 
ATOM   5062 O O   . LEU B 1 220 ? 10.939  -32.473 29.294  1.00 34.04 ? 220  LEU B O   1 
ATOM   5063 C CB  . LEU B 1 220 ? 12.588  -30.487 27.487  1.00 33.68 ? 220  LEU B CB  1 
ATOM   5064 C CG  . LEU B 1 220 ? 12.570  -29.506 26.327  1.00 34.20 ? 220  LEU B CG  1 
ATOM   5065 C CD1 . LEU B 1 220 ? 13.620  -29.979 25.273  1.00 32.01 ? 220  LEU B CD1 1 
ATOM   5066 C CD2 . LEU B 1 220 ? 11.167  -29.405 25.766  1.00 32.83 ? 220  LEU B CD2 1 
ATOM   5067 N N   . GLU B 1 221 ? 12.663  -31.724 30.488  1.00 34.70 ? 221  GLU B N   1 
ATOM   5068 C CA  . GLU B 1 221 ? 12.676  -32.899 31.366  1.00 35.86 ? 221  GLU B CA  1 
ATOM   5069 C C   . GLU B 1 221 ? 11.532  -32.789 32.359  1.00 36.31 ? 221  GLU B C   1 
ATOM   5070 O O   . GLU B 1 221 ? 10.943  -33.788 32.742  1.00 36.27 ? 221  GLU B O   1 
ATOM   5071 C CB  . GLU B 1 221 ? 13.996  -33.036 32.120  1.00 35.70 ? 221  GLU B CB  1 
ATOM   5072 C CG  . GLU B 1 221 ? 15.158  -33.615 31.299  1.00 36.34 ? 221  GLU B CG  1 
ATOM   5073 C CD  . GLU B 1 221 ? 16.507  -33.471 31.991  1.00 36.52 ? 221  GLU B CD  1 
ATOM   5074 O OE1 . GLU B 1 221 ? 16.675  -32.587 32.842  1.00 39.25 ? 221  GLU B OE1 1 
ATOM   5075 O OE2 . GLU B 1 221 ? 17.414  -34.240 31.695  1.00 36.71 ? 221  GLU B OE2 1 
ATOM   5076 N N   . ASN B 1 222 ? 11.226  -31.560 32.750  1.00 36.99 ? 222  ASN B N   1 
ATOM   5077 C CA  . ASN B 1 222 ? 10.124  -31.275 33.637  1.00 38.22 ? 222  ASN B CA  1 
ATOM   5078 C C   . ASN B 1 222 ? 8.787   -31.689 33.062  1.00 38.20 ? 222  ASN B C   1 
ATOM   5079 O O   . ASN B 1 222 ? 7.958   -32.254 33.776  1.00 38.00 ? 222  ASN B O   1 
ATOM   5080 C CB  . ASN B 1 222 ? 10.076  -29.792 33.888  1.00 38.82 ? 222  ASN B CB  1 
ATOM   5081 C CG  . ASN B 1 222 ? 10.129  -29.464 35.351  1.00 43.11 ? 222  ASN B CG  1 
ATOM   5082 O OD1 . ASN B 1 222 ? 9.078   -29.217 35.986  1.00 46.69 ? 222  ASN B OD1 1 
ATOM   5083 N ND2 . ASN B 1 222 ? 11.350  -29.487 35.923  1.00 43.65 ? 222  ASN B ND2 1 
ATOM   5084 N N   . ASP B 1 223 ? 8.597   -31.391 31.770  1.00 38.10 ? 223  ASP B N   1 
ATOM   5085 C CA  . ASP B 1 223 ? 7.348   -31.638 31.059  1.00 38.08 ? 223  ASP B CA  1 
ATOM   5086 C C   . ASP B 1 223 ? 7.228   -33.087 30.599  1.00 37.94 ? 223  ASP B C   1 
ATOM   5087 O O   . ASP B 1 223 ? 6.135   -33.623 30.485  1.00 38.25 ? 223  ASP B O   1 
ATOM   5088 C CB  . ASP B 1 223 ? 7.244   -30.705 29.861  1.00 38.07 ? 223  ASP B CB  1 
ATOM   5089 C CG  . ASP B 1 223 ? 7.061   -29.252 30.264  1.00 39.22 ? 223  ASP B CG  1 
ATOM   5090 O OD1 . ASP B 1 223 ? 6.466   -29.002 31.327  1.00 41.10 ? 223  ASP B OD1 1 
ATOM   5091 O OD2 . ASP B 1 223 ? 7.487   -28.348 29.520  1.00 39.40 ? 223  ASP B OD2 1 
ATOM   5092 N N   . LEU B 1 224 ? 8.362   -33.712 30.328  1.00 37.65 ? 224  LEU B N   1 
ATOM   5093 C CA  . LEU B 1 224 ? 8.378   -35.082 29.857  1.00 37.46 ? 224  LEU B CA  1 
ATOM   5094 C C   . LEU B 1 224 ? 9.002   -35.981 30.937  1.00 37.51 ? 224  LEU B C   1 
ATOM   5095 O O   . LEU B 1 224 ? 10.175  -36.357 30.850  1.00 37.77 ? 224  LEU B O   1 
ATOM   5096 C CB  . LEU B 1 224 ? 9.138   -35.171 28.521  1.00 37.48 ? 224  LEU B CB  1 
ATOM   5097 C CG  . LEU B 1 224 ? 8.481   -34.626 27.232  1.00 37.35 ? 224  LEU B CG  1 
ATOM   5098 C CD1 . LEU B 1 224 ? 9.538   -34.057 26.265  1.00 36.03 ? 224  LEU B CD1 1 
ATOM   5099 C CD2 . LEU B 1 224 ? 7.619   -35.716 26.538  1.00 35.39 ? 224  LEU B CD2 1 
ATOM   5100 N N   . SER B 1 225 ? 8.202   -36.308 31.950  1.00 37.41 ? 225  SER B N   1 
ATOM   5101 C CA  . SER B 1 225 ? 8.610   -37.141 33.093  1.00 37.41 ? 225  SER B CA  1 
ATOM   5102 C C   . SER B 1 225 ? 9.225   -38.493 32.746  1.00 37.00 ? 225  SER B C   1 
ATOM   5103 O O   . SER B 1 225 ? 8.553   -39.374 32.182  1.00 37.48 ? 225  SER B O   1 
ATOM   5104 C CB  . SER B 1 225 ? 7.414   -37.368 34.013  1.00 37.59 ? 225  SER B CB  1 
ATOM   5105 O OG  . SER B 1 225 ? 7.237   -36.237 34.846  1.00 39.69 ? 225  SER B OG  1 
ATOM   5106 N N   . GLY B 1 226 ? 10.496  -38.670 33.097  1.00 36.44 ? 226  GLY B N   1 
ATOM   5107 C CA  . GLY B 1 226 ? 11.156  -39.965 32.882  1.00 36.43 ? 226  GLY B CA  1 
ATOM   5108 C C   . GLY B 1 226 ? 12.239  -39.866 31.824  1.00 35.91 ? 226  GLY B C   1 
ATOM   5109 O O   . GLY B 1 226 ? 12.971  -40.831 31.555  1.00 36.15 ? 226  GLY B O   1 
ATOM   5110 N N   . VAL B 1 227 ? 12.352  -38.664 31.264  1.00 34.94 ? 227  VAL B N   1 
ATOM   5111 C CA  . VAL B 1 227 ? 13.270  -38.371 30.172  1.00 33.88 ? 227  VAL B CA  1 
ATOM   5112 C C   . VAL B 1 227 ? 14.455  -37.605 30.706  1.00 33.16 ? 227  VAL B C   1 
ATOM   5113 O O   . VAL B 1 227 ? 14.275  -36.720 31.511  1.00 32.57 ? 227  VAL B O   1 
ATOM   5114 C CB  . VAL B 1 227 ? 12.533  -37.543 29.109  1.00 33.27 ? 227  VAL B CB  1 
ATOM   5115 C CG1 . VAL B 1 227 ? 13.442  -36.630 28.415  1.00 33.85 ? 227  VAL B CG1 1 
ATOM   5116 C CG2 . VAL B 1 227 ? 11.824  -38.483 28.141  1.00 33.10 ? 227  VAL B CG2 1 
ATOM   5117 N N   . THR B 1 228 ? 15.667  -37.929 30.260  1.00 32.85 ? 228  THR B N   1 
ATOM   5118 C CA  . THR B 1 228 ? 16.831  -37.192 30.729  1.00 32.65 ? 228  THR B CA  1 
ATOM   5119 C C   . THR B 1 228 ? 17.648  -36.797 29.509  1.00 32.25 ? 228  THR B C   1 
ATOM   5120 O O   . THR B 1 228 ? 18.021  -37.644 28.716  1.00 32.78 ? 228  THR B O   1 
ATOM   5121 C CB  . THR B 1 228 ? 17.658  -37.980 31.825  1.00 32.95 ? 228  THR B CB  1 
ATOM   5122 O OG1 . THR B 1 228 ? 18.800  -38.636 31.245  1.00 33.51 ? 228  THR B OG1 1 
ATOM   5123 C CG2 . THR B 1 228 ? 16.794  -39.033 32.547  1.00 33.10 ? 228  THR B CG2 1 
ATOM   5124 N N   . LEU B 1 229 ? 17.902  -35.504 29.343  1.00 31.90 ? 229  LEU B N   1 
ATOM   5125 C CA  . LEU B 1 229 ? 18.425  -34.959 28.068  1.00 31.85 ? 229  LEU B CA  1 
ATOM   5126 C C   . LEU B 1 229 ? 19.797  -34.289 28.197  1.00 32.03 ? 229  LEU B C   1 
ATOM   5127 O O   . LEU B 1 229 ? 20.075  -33.650 29.237  1.00 32.20 ? 229  LEU B O   1 
ATOM   5128 C CB  . LEU B 1 229 ? 17.429  -33.929 27.497  1.00 31.10 ? 229  LEU B CB  1 
ATOM   5129 C CG  . LEU B 1 229 ? 16.094  -34.435 26.932  1.00 31.21 ? 229  LEU B CG  1 
ATOM   5130 C CD1 . LEU B 1 229 ? 15.070  -33.299 26.745  1.00 29.63 ? 229  LEU B CD1 1 
ATOM   5131 C CD2 . LEU B 1 229 ? 16.272  -35.235 25.620  1.00 28.39 ? 229  LEU B CD2 1 
ATOM   5132 N N   . THR B 1 230 ? 20.644  -34.428 27.170  1.00 31.71 ? 230  THR B N   1 
ATOM   5133 C CA  . THR B 1 230 ? 21.888  -33.616 27.104  1.00 31.82 ? 230  THR B CA  1 
ATOM   5134 C C   . THR B 1 230 ? 21.641  -32.324 26.348  1.00 31.98 ? 230  THR B C   1 
ATOM   5135 O O   . THR B 1 230 ? 20.760  -32.253 25.518  1.00 32.59 ? 230  THR B O   1 
ATOM   5136 C CB  . THR B 1 230 ? 23.052  -34.321 26.405  1.00 31.67 ? 230  THR B CB  1 
ATOM   5137 O OG1 . THR B 1 230 ? 22.744  -34.490 25.010  1.00 30.77 ? 230  THR B OG1 1 
ATOM   5138 C CG2 . THR B 1 230 ? 23.394  -35.677 27.083  1.00 30.75 ? 230  THR B CG2 1 
ATOM   5139 N N   . ASP B 1 231 ? 22.421  -31.298 26.627  1.00 32.28 ? 231  ASP B N   1 
ATOM   5140 C CA  . ASP B 1 231 ? 22.278  -30.053 25.893  1.00 32.69 ? 231  ASP B CA  1 
ATOM   5141 C C   . ASP B 1 231 ? 22.290  -30.290 24.383  1.00 32.47 ? 231  ASP B C   1 
ATOM   5142 O O   . ASP B 1 231 ? 21.571  -29.614 23.621  1.00 33.21 ? 231  ASP B O   1 
ATOM   5143 C CB  . ASP B 1 231 ? 23.369  -29.084 26.304  1.00 33.03 ? 231  ASP B CB  1 
ATOM   5144 C CG  . ASP B 1 231 ? 23.225  -28.633 27.768  1.00 34.85 ? 231  ASP B CG  1 
ATOM   5145 O OD1 . ASP B 1 231 ? 22.133  -28.803 28.365  1.00 37.19 ? 231  ASP B OD1 1 
ATOM   5146 O OD2 . ASP B 1 231 ? 24.197  -28.092 28.334  1.00 35.78 ? 231  ASP B OD2 1 
ATOM   5147 N N   . THR B 1 232 ? 23.052  -31.287 23.947  1.00 31.03 ? 232  THR B N   1 
ATOM   5148 C CA  . THR B 1 232 ? 23.182  -31.509 22.521  1.00 29.90 ? 232  THR B CA  1 
ATOM   5149 C C   . THR B 1 232 ? 21.869  -32.020 21.985  1.00 29.11 ? 232  THR B C   1 
ATOM   5150 O O   . THR B 1 232 ? 21.353  -31.528 20.965  1.00 29.80 ? 232  THR B O   1 
ATOM   5151 C CB  . THR B 1 232 ? 24.397  -32.376 22.195  1.00 29.80 ? 232  THR B CB  1 
ATOM   5152 O OG1 . THR B 1 232 ? 25.580  -31.612 22.484  1.00 30.20 ? 232  THR B OG1 1 
ATOM   5153 C CG2 . THR B 1 232 ? 24.425  -32.728 20.731  1.00 30.22 ? 232  THR B CG2 1 
ATOM   5154 N N   . GLU B 1 233 ? 21.282  -32.951 22.724  1.00 27.61 ? 233  GLU B N   1 
ATOM   5155 C CA  . GLU B 1 233 ? 20.006  -33.506 22.337  1.00 26.50 ? 233  GLU B CA  1 
ATOM   5156 C C   . GLU B 1 233 ? 18.949  -32.424 22.227  1.00 25.77 ? 233  GLU B C   1 
ATOM   5157 O O   . GLU B 1 233 ? 18.122  -32.472 21.345  1.00 25.59 ? 233  GLU B O   1 
ATOM   5158 C CB  . GLU B 1 233 ? 19.606  -34.636 23.281  1.00 26.54 ? 233  GLU B CB  1 
ATOM   5159 C CG  . GLU B 1 233 ? 20.448  -35.929 22.989  1.00 28.26 ? 233  GLU B CG  1 
ATOM   5160 C CD  . GLU B 1 233 ? 20.504  -36.946 24.128  1.00 28.61 ? 233  GLU B CD  1 
ATOM   5161 O OE1 . GLU B 1 233 ? 20.056  -36.611 25.238  1.00 32.19 ? 233  GLU B OE1 1 
ATOM   5162 O OE2 . GLU B 1 233 ? 20.978  -38.083 23.906  1.00 27.81 ? 233  GLU B OE2 1 
ATOM   5163 N N   . VAL B 1 234 ? 19.017  -31.416 23.081  1.00 25.13 ? 234  VAL B N   1 
ATOM   5164 C CA  . VAL B 1 234 ? 18.048  -30.362 23.009  1.00 24.92 ? 234  VAL B CA  1 
ATOM   5165 C C   . VAL B 1 234 ? 18.233  -29.654 21.680  1.00 25.54 ? 234  VAL B C   1 
ATOM   5166 O O   . VAL B 1 234 ? 17.241  -29.400 20.990  1.00 25.23 ? 234  VAL B O   1 
ATOM   5167 C CB  . VAL B 1 234 ? 18.148  -29.349 24.177  1.00 25.32 ? 234  VAL B CB  1 
ATOM   5168 C CG1 . VAL B 1 234 ? 17.188  -28.219 23.937  1.00 24.82 ? 234  VAL B CG1 1 
ATOM   5169 C CG2 . VAL B 1 234 ? 17.856  -30.022 25.535  1.00 22.80 ? 234  VAL B CG2 1 
ATOM   5170 N N   . THR B 1 235 ? 19.479  -29.361 21.276  1.00 25.11 ? 235  THR B N   1 
ATOM   5171 C CA  . THR B 1 235 ? 19.611  -28.716 19.976  1.00 24.68 ? 235  THR B CA  1 
ATOM   5172 C C   . THR B 1 235 ? 19.095  -29.598 18.830  1.00 24.65 ? 235  THR B C   1 
ATOM   5173 O O   . THR B 1 235 ? 18.613  -29.068 17.833  1.00 24.52 ? 235  THR B O   1 
ATOM   5174 C CB  . THR B 1 235 ? 20.997  -28.156 19.671  1.00 24.45 ? 235  THR B CB  1 
ATOM   5175 O OG1 . THR B 1 235 ? 21.885  -29.219 19.360  1.00 24.54 ? 235  THR B OG1 1 
ATOM   5176 C CG2 . THR B 1 235 ? 21.503  -27.354 20.846  1.00 25.65 ? 235  THR B CG2 1 
ATOM   5177 N N   . TYR B 1 236 ? 19.131  -30.919 18.995  1.00 24.20 ? 236  TYR B N   1 
ATOM   5178 C CA  . TYR B 1 236 ? 18.545  -31.816 17.988  1.00 24.53 ? 236  TYR B CA  1 
ATOM   5179 C C   . TYR B 1 236 ? 17.040  -31.597 17.815  1.00 24.71 ? 236  TYR B C   1 
ATOM   5180 O O   . TYR B 1 236 ? 16.579  -31.443 16.684  1.00 24.97 ? 236  TYR B O   1 
ATOM   5181 C CB  . TYR B 1 236 ? 18.860  -33.303 18.251  1.00 24.71 ? 236  TYR B CB  1 
ATOM   5182 C CG  . TYR B 1 236 ? 20.339  -33.687 18.207  1.00 27.19 ? 236  TYR B CG  1 
ATOM   5183 C CD1 . TYR B 1 236 ? 21.301  -32.842 17.629  1.00 27.49 ? 236  TYR B CD1 1 
ATOM   5184 C CD2 . TYR B 1 236 ? 20.766  -34.928 18.703  1.00 29.25 ? 236  TYR B CD2 1 
ATOM   5185 C CE1 . TYR B 1 236 ? 22.656  -33.197 17.594  1.00 30.76 ? 236  TYR B CE1 1 
ATOM   5186 C CE2 . TYR B 1 236 ? 22.115  -35.315 18.658  1.00 30.08 ? 236  TYR B CE2 1 
ATOM   5187 C CZ  . TYR B 1 236 ? 23.060  -34.440 18.107  1.00 32.46 ? 236  TYR B CZ  1 
ATOM   5188 O OH  . TYR B 1 236 ? 24.399  -34.809 18.062  1.00 34.71 ? 236  TYR B OH  1 
ATOM   5189 N N   . LEU B 1 237 ? 16.283  -31.563 18.910  1.00 24.25 ? 237  LEU B N   1 
ATOM   5190 C CA  . LEU B 1 237 ? 14.840  -31.256 18.837  1.00 24.38 ? 237  LEU B CA  1 
ATOM   5191 C C   . LEU B 1 237 ? 14.597  -29.882 18.218  1.00 25.16 ? 237  LEU B C   1 
ATOM   5192 O O   . LEU B 1 237 ? 13.627  -29.682 17.501  1.00 25.57 ? 237  LEU B O   1 
ATOM   5193 C CB  . LEU B 1 237 ? 14.184  -31.320 20.212  1.00 23.61 ? 237  LEU B CB  1 
ATOM   5194 C CG  . LEU B 1 237 ? 14.200  -32.684 20.910  1.00 23.62 ? 237  LEU B CG  1 
ATOM   5195 C CD1 . LEU B 1 237 ? 13.687  -32.490 22.311  1.00 22.87 ? 237  LEU B CD1 1 
ATOM   5196 C CD2 . LEU B 1 237 ? 13.380  -33.766 20.172  1.00 17.93 ? 237  LEU B CD2 1 
ATOM   5197 N N   . MET B 1 238 ? 15.492  -28.937 18.483  1.00 25.26 ? 238  MET B N   1 
ATOM   5198 C CA  . MET B 1 238 ? 15.417  -27.662 17.800  1.00 25.72 ? 238  MET B CA  1 
ATOM   5199 C C   . MET B 1 238 ? 15.659  -27.821 16.279  1.00 26.15 ? 238  MET B C   1 
ATOM   5200 O O   . MET B 1 238 ? 14.837  -27.355 15.483  1.00 26.33 ? 238  MET B O   1 
ATOM   5201 C CB  . MET B 1 238 ? 16.317  -26.632 18.482  1.00 25.62 ? 238  MET B CB  1 
ATOM   5202 C CG  . MET B 1 238 ? 15.810  -26.299 19.918  1.00 25.04 ? 238  MET B CG  1 
ATOM   5203 S SD  . MET B 1 238 ? 16.745  -24.959 20.682  1.00 27.17 ? 238  MET B SD  1 
ATOM   5204 C CE  . MET B 1 238 ? 15.801  -23.530 20.175  1.00 22.36 ? 238  MET B CE  1 
ATOM   5205 N N   . ASP B 1 239 ? 16.729  -28.536 15.896  1.00 25.94 ? 239  ASP B N   1 
ATOM   5206 C CA  . ASP B 1 239 ? 17.040  -28.840 14.489  1.00 25.84 ? 239  ASP B CA  1 
ATOM   5207 C C   . ASP B 1 239 ? 15.792  -29.476 13.808  1.00 26.31 ? 239  ASP B C   1 
ATOM   5208 O O   . ASP B 1 239 ? 15.446  -29.112 12.690  1.00 25.93 ? 239  ASP B O   1 
ATOM   5209 C CB  . ASP B 1 239 ? 18.248  -29.814 14.330  1.00 25.28 ? 239  ASP B CB  1 
ATOM   5210 C CG  . ASP B 1 239 ? 19.635  -29.203 14.675  1.00 24.20 ? 239  ASP B CG  1 
ATOM   5211 O OD1 . ASP B 1 239 ? 19.829  -27.989 14.875  1.00 22.42 ? 239  ASP B OD1 1 
ATOM   5212 O OD2 . ASP B 1 239 ? 20.588  -29.999 14.757  1.00 25.23 ? 239  ASP B OD2 1 
ATOM   5213 N N   . MET B 1 240 ? 15.103  -30.393 14.498  1.00 27.18 ? 240  MET B N   1 
ATOM   5214 C CA  . MET B 1 240 ? 13.882  -31.046 13.954  1.00 27.38 ? 240  MET B CA  1 
ATOM   5215 C C   . MET B 1 240 ? 12.763  -30.116 13.515  1.00 27.94 ? 240  MET B C   1 
ATOM   5216 O O   . MET B 1 240 ? 11.980  -30.488 12.646  1.00 28.63 ? 240  MET B O   1 
ATOM   5217 C CB  . MET B 1 240 ? 13.313  -32.069 14.912  1.00 27.43 ? 240  MET B CB  1 
ATOM   5218 C CG  . MET B 1 240 ? 14.059  -33.386 14.873  1.00 28.78 ? 240  MET B CG  1 
ATOM   5219 S SD  . MET B 1 240 ? 14.193  -34.109 13.216  1.00 32.09 ? 240  MET B SD  1 
ATOM   5220 C CE  . MET B 1 240 ? 12.468  -34.560 13.000  1.00 28.62 ? 240  MET B CE  1 
ATOM   5221 N N   . CYS B 1 241 ? 12.701  -28.908 14.084  1.00 28.39 ? 241  CYS B N   1 
ATOM   5222 C CA  . CYS B 1 241 ? 11.671  -27.926 13.742  1.00 28.78 ? 241  CYS B CA  1 
ATOM   5223 C C   . CYS B 1 241 ? 11.864  -27.357 12.328  1.00 28.56 ? 241  CYS B C   1 
ATOM   5224 O O   . CYS B 1 241 ? 10.911  -27.004 11.652  1.00 29.21 ? 241  CYS B O   1 
ATOM   5225 C CB  . CYS B 1 241 ? 11.673  -26.833 14.791  1.00 28.63 ? 241  CYS B CB  1 
ATOM   5226 S SG  . CYS B 1 241 ? 11.040  -25.247 14.261  1.00 32.47 ? 241  CYS B SG  1 
ATOM   5227 N N   . SER B 1 242 ? 13.106  -27.280 11.869  1.00 28.17 ? 242  SER B N   1 
ATOM   5228 C CA  . SER B 1 242 ? 13.373  -26.904 10.499  1.00 26.82 ? 242  SER B CA  1 
ATOM   5229 C C   . SER B 1 242 ? 13.052  -28.105 9.595   1.00 26.94 ? 242  SER B C   1 
ATOM   5230 O O   . SER B 1 242 ? 12.256  -27.999 8.659   1.00 26.49 ? 242  SER B O   1 
ATOM   5231 C CB  . SER B 1 242 ? 14.837  -26.487 10.340  1.00 26.82 ? 242  SER B CB  1 
ATOM   5232 O OG  . SER B 1 242 ? 15.107  -25.971 9.049   1.00 25.22 ? 242  SER B OG  1 
ATOM   5233 N N   . PHE B 1 243 ? 13.645  -29.245 9.897   1.00 26.29 ? 243  PHE B N   1 
ATOM   5234 C CA  . PHE B 1 243 ? 13.532  -30.397 9.031   1.00 27.00 ? 243  PHE B CA  1 
ATOM   5235 C C   . PHE B 1 243 ? 12.140  -30.977 8.924   1.00 27.70 ? 243  PHE B C   1 
ATOM   5236 O O   . PHE B 1 243 ? 11.732  -31.379 7.841   1.00 28.24 ? 243  PHE B O   1 
ATOM   5237 C CB  . PHE B 1 243 ? 14.488  -31.475 9.489   1.00 27.13 ? 243  PHE B CB  1 
ATOM   5238 C CG  . PHE B 1 243 ? 15.918  -31.173 9.184   1.00 27.02 ? 243  PHE B CG  1 
ATOM   5239 C CD1 . PHE B 1 243 ? 16.389  -31.245 7.887   1.00 27.14 ? 243  PHE B CD1 1 
ATOM   5240 C CD2 . PHE B 1 243 ? 16.797  -30.830 10.196  1.00 26.19 ? 243  PHE B CD2 1 
ATOM   5241 C CE1 . PHE B 1 243 ? 17.735  -30.999 7.602   1.00 28.05 ? 243  PHE B CE1 1 
ATOM   5242 C CE2 . PHE B 1 243 ? 18.130  -30.575 9.923   1.00 27.51 ? 243  PHE B CE2 1 
ATOM   5243 C CZ  . PHE B 1 243 ? 18.602  -30.652 8.641   1.00 27.39 ? 243  PHE B CZ  1 
ATOM   5244 N N   . ASP B 1 244 ? 11.405  -31.045 10.034  1.00 28.54 ? 244  ASP B N   1 
ATOM   5245 C CA  . ASP B 1 244 ? 10.029  -31.558 10.007  1.00 29.12 ? 244  ASP B CA  1 
ATOM   5246 C C   . ASP B 1 244 ? 9.104   -30.595 9.258   1.00 30.02 ? 244  ASP B C   1 
ATOM   5247 O O   . ASP B 1 244 ? 8.069   -30.993 8.743   1.00 30.30 ? 244  ASP B O   1 
ATOM   5248 C CB  . ASP B 1 244 ? 9.500   -31.808 11.426  1.00 28.47 ? 244  ASP B CB  1 
ATOM   5249 C CG  . ASP B 1 244 ? 8.188   -32.604 11.437  1.00 28.39 ? 244  ASP B CG  1 
ATOM   5250 O OD1 . ASP B 1 244 ? 8.195   -33.784 11.036  1.00 27.31 ? 244  ASP B OD1 1 
ATOM   5251 O OD2 . ASP B 1 244 ? 7.145   -32.049 11.865  1.00 29.32 ? 244  ASP B OD2 1 
ATOM   5252 N N   . THR B 1 245 ? 9.464   -29.322 9.207   1.00 31.15 ? 245  THR B N   1 
ATOM   5253 C CA  . THR B 1 245 ? 8.631   -28.389 8.487   1.00 32.90 ? 245  THR B CA  1 
ATOM   5254 C C   . THR B 1 245 ? 8.846   -28.513 6.972   1.00 33.86 ? 245  THR B C   1 
ATOM   5255 O O   . THR B 1 245 ? 7.921   -28.825 6.218   1.00 34.07 ? 245  THR B O   1 
ATOM   5256 C CB  . THR B 1 245 ? 8.884   -26.959 8.943   1.00 32.36 ? 245  THR B CB  1 
ATOM   5257 O OG1 . THR B 1 245 ? 8.570   -26.880 10.319  1.00 34.05 ? 245  THR B OG1 1 
ATOM   5258 C CG2 . THR B 1 245 ? 7.980   -25.981 8.205   1.00 32.27 ? 245  THR B CG2 1 
ATOM   5259 N N   . ILE B 1 246 ? 10.078  -28.290 6.549   1.00 35.09 ? 246  ILE B N   1 
ATOM   5260 C CA  . ILE B 1 246 ? 10.369  -28.076 5.141   1.00 36.38 ? 246  ILE B CA  1 
ATOM   5261 C C   . ILE B 1 246 ? 10.731  -29.344 4.366   1.00 37.59 ? 246  ILE B C   1 
ATOM   5262 O O   . ILE B 1 246 ? 11.229  -29.272 3.245   1.00 38.55 ? 246  ILE B O   1 
ATOM   5263 C CB  . ILE B 1 246 ? 11.405  -26.932 4.967   1.00 35.90 ? 246  ILE B CB  1 
ATOM   5264 C CG1 . ILE B 1 246 ? 12.808  -27.365 5.381   1.00 34.49 ? 246  ILE B CG1 1 
ATOM   5265 C CG2 . ILE B 1 246 ? 10.978  -25.721 5.774   1.00 34.20 ? 246  ILE B CG2 1 
ATOM   5266 C CD1 . ILE B 1 246 ? 13.827  -26.253 5.178   1.00 32.37 ? 246  ILE B CD1 1 
ATOM   5267 N N   . SER B 1 247 ? 10.459  -30.498 4.971   1.00 39.44 ? 247  SER B N   1 
ATOM   5268 C CA  . SER B 1 247 ? 10.745  -31.802 4.370   1.00 41.16 ? 247  SER B CA  1 
ATOM   5269 C C   . SER B 1 247 ? 9.494   -32.447 3.856   1.00 42.14 ? 247  SER B C   1 
ATOM   5270 O O   . SER B 1 247 ? 9.569   -33.374 3.065   1.00 43.22 ? 247  SER B O   1 
ATOM   5271 C CB  . SER B 1 247 ? 11.371  -32.767 5.379   1.00 41.24 ? 247  SER B CB  1 
ATOM   5272 O OG  . SER B 1 247 ? 12.678  -32.354 5.748   1.00 42.37 ? 247  SER B OG  1 
ATOM   5273 N N   . THR B 1 248 ? 8.341   -31.979 4.294   1.00 43.45 ? 248  THR B N   1 
ATOM   5274 C CA  . THR B 1 248 ? 7.099   -32.611 3.858   1.00 45.01 ? 248  THR B CA  1 
ATOM   5275 C C   . THR B 1 248 ? 6.191   -31.745 2.996   1.00 44.93 ? 248  THR B C   1 
ATOM   5276 O O   . THR B 1 248 ? 6.491   -30.571 2.715   1.00 44.80 ? 248  THR B O   1 
ATOM   5277 C CB  . THR B 1 248 ? 6.250   -33.152 5.055   1.00 45.60 ? 248  THR B CB  1 
ATOM   5278 O OG1 . THR B 1 248 ? 4.879   -33.263 4.640   1.00 47.24 ? 248  THR B OG1 1 
ATOM   5279 C CG2 . THR B 1 248 ? 6.331   -32.194 6.266   1.00 45.90 ? 248  THR B CG2 1 
ATOM   5280 N N   . SER B 1 249 ? 5.089   -32.396 2.600   1.00 45.13 ? 249  SER B N   1 
ATOM   5281 C CA  . SER B 1 249 ? 3.925   -31.836 1.934   1.00 45.17 ? 249  SER B CA  1 
ATOM   5282 C C   . SER B 1 249 ? 3.630   -30.477 2.508   1.00 44.34 ? 249  SER B C   1 
ATOM   5283 O O   . SER B 1 249 ? 3.483   -29.505 1.761   1.00 44.38 ? 249  SER B O   1 
ATOM   5284 C CB  . SER B 1 249 ? 2.710   -32.782 2.148   1.00 45.73 ? 249  SER B CB  1 
ATOM   5285 O OG  . SER B 1 249 ? 1.493   -32.264 1.607   1.00 46.80 ? 249  SER B OG  1 
ATOM   5286 N N   . THR B 1 250 ? 3.595   -30.416 3.835   1.00 43.26 ? 250  THR B N   1 
ATOM   5287 C CA  . THR B 1 250 ? 3.062   -29.258 4.533   1.00 42.56 ? 250  THR B CA  1 
ATOM   5288 C C   . THR B 1 250 ? 3.967   -28.032 4.587   1.00 41.90 ? 250  THR B C   1 
ATOM   5289 O O   . THR B 1 250 ? 3.670   -27.108 5.350   1.00 41.30 ? 250  THR B O   1 
ATOM   5290 C CB  . THR B 1 250 ? 2.533   -29.597 5.980   1.00 42.98 ? 250  THR B CB  1 
ATOM   5291 O OG1 . THR B 1 250 ? 3.275   -30.690 6.553   1.00 42.63 ? 250  THR B OG1 1 
ATOM   5292 C CG2 . THR B 1 250 ? 1.037   -29.967 5.914   1.00 44.17 ? 250  THR B CG2 1 
ATOM   5293 N N   . VAL B 1 251 ? 5.039   -27.993 3.783   1.00 41.45 ? 251  VAL B N   1 
ATOM   5294 C CA  . VAL B 1 251 ? 5.970   -26.853 3.845   1.00 41.50 ? 251  VAL B CA  1 
ATOM   5295 C C   . VAL B 1 251 ? 5.253   -25.533 3.975   1.00 41.53 ? 251  VAL B C   1 
ATOM   5296 O O   . VAL B 1 251 ? 5.597   -24.710 4.832   1.00 40.62 ? 251  VAL B O   1 
ATOM   5297 C CB  . VAL B 1 251 ? 6.862   -26.619 2.614   1.00 41.42 ? 251  VAL B CB  1 
ATOM   5298 C CG1 . VAL B 1 251 ? 8.300   -26.541 2.987   1.00 41.97 ? 251  VAL B CG1 1 
ATOM   5299 C CG2 . VAL B 1 251 ? 6.547   -27.484 1.453   1.00 41.98 ? 251  VAL B CG2 1 
ATOM   5300 N N   . ASP B 1 252 ? 4.276   -25.336 3.088   1.00 42.16 ? 252  ASP B N   1 
ATOM   5301 C CA  . ASP B 1 252 ? 3.547   -24.069 2.962   1.00 42.48 ? 252  ASP B CA  1 
ATOM   5302 C C   . ASP B 1 252 ? 2.331   -23.912 3.901   1.00 42.02 ? 252  ASP B C   1 
ATOM   5303 O O   . ASP B 1 252 ? 1.886   -22.803 4.146   1.00 41.93 ? 252  ASP B O   1 
ATOM   5304 C CB  . ASP B 1 252 ? 3.142   -23.851 1.494   1.00 42.45 ? 252  ASP B CB  1 
ATOM   5305 C CG  . ASP B 1 252 ? 4.322   -23.404 0.616   1.00 44.92 ? 252  ASP B CG  1 
ATOM   5306 O OD1 . ASP B 1 252 ? 4.408   -22.202 0.314   1.00 47.65 ? 252  ASP B OD1 1 
ATOM   5307 O OD2 . ASP B 1 252 ? 5.182   -24.221 0.229   1.00 46.77 ? 252  ASP B OD2 1 
ATOM   5308 N N   . THR B 1 253 ? 1.805   -25.009 4.430   1.00 42.42 ? 253  THR B N   1 
ATOM   5309 C CA  . THR B 1 253 ? 0.548   -24.957 5.206   1.00 43.11 ? 253  THR B CA  1 
ATOM   5310 C C   . THR B 1 253 ? 0.699   -24.999 6.741   1.00 43.36 ? 253  THR B C   1 
ATOM   5311 O O   . THR B 1 253 ? -0.009  -24.268 7.453   1.00 43.53 ? 253  THR B O   1 
ATOM   5312 C CB  . THR B 1 253 ? -0.465  -26.040 4.730   1.00 43.31 ? 253  THR B CB  1 
ATOM   5313 O OG1 . THR B 1 253 ? 0.226   -27.273 4.450   1.00 43.72 ? 253  THR B OG1 1 
ATOM   5314 C CG2 . THR B 1 253 ? -1.196  -25.575 3.461   1.00 43.48 ? 253  THR B CG2 1 
ATOM   5315 N N   . LYS B 1 254 ? 1.614   -25.839 7.249   1.00 43.29 ? 254  LYS B N   1 
ATOM   5316 C CA  . LYS B 1 254 ? 1.819   -25.971 8.702   1.00 42.94 ? 254  LYS B CA  1 
ATOM   5317 C C   . LYS B 1 254 ? 3.283   -25.857 9.110   1.00 42.41 ? 254  LYS B C   1 
ATOM   5318 O O   . LYS B 1 254 ? 4.171   -26.459 8.483   1.00 42.17 ? 254  LYS B O   1 
ATOM   5319 C CB  . LYS B 1 254 ? 1.229   -27.293 9.243   1.00 43.03 ? 254  LYS B CB  1 
ATOM   5320 N N   . LEU B 1 255 ? 3.512   -25.077 10.170  1.00 41.83 ? 255  LEU B N   1 
ATOM   5321 C CA  . LEU B 1 255 ? 4.771   -25.106 10.933  1.00 41.37 ? 255  LEU B CA  1 
ATOM   5322 C C   . LEU B 1 255 ? 4.869   -26.411 11.761  1.00 40.89 ? 255  LEU B C   1 
ATOM   5323 O O   . LEU B 1 255 ? 3.882   -26.821 12.401  1.00 41.25 ? 255  LEU B O   1 
ATOM   5324 C CB  . LEU B 1 255 ? 4.844   -23.872 11.844  1.00 41.23 ? 255  LEU B CB  1 
ATOM   5325 C CG  . LEU B 1 255 ? 6.169   -23.490 12.505  1.00 40.38 ? 255  LEU B CG  1 
ATOM   5326 C CD1 . LEU B 1 255 ? 7.286   -23.377 11.460  1.00 39.18 ? 255  LEU B CD1 1 
ATOM   5327 C CD2 . LEU B 1 255 ? 6.009   -22.194 13.318  1.00 38.27 ? 255  LEU B CD2 1 
ATOM   5328 N N   . SER B 1 256 ? 6.030   -27.069 11.732  1.00 39.93 ? 256  SER B N   1 
ATOM   5329 C CA  . SER B 1 256 ? 6.225   -28.343 12.462  1.00 39.17 ? 256  SER B CA  1 
ATOM   5330 C C   . SER B 1 256 ? 5.826   -28.266 13.931  1.00 38.51 ? 256  SER B C   1 
ATOM   5331 O O   . SER B 1 256 ? 5.988   -27.209 14.557  1.00 38.06 ? 256  SER B O   1 
ATOM   5332 C CB  . SER B 1 256 ? 7.679   -28.814 12.395  1.00 39.17 ? 256  SER B CB  1 
ATOM   5333 O OG  . SER B 1 256 ? 7.847   -29.941 13.231  1.00 38.45 ? 256  SER B OG  1 
ATOM   5334 N N   . PRO B 1 257 ? 5.301   -29.386 14.488  1.00 38.23 ? 257  PRO B N   1 
ATOM   5335 C CA  . PRO B 1 257 ? 4.900   -29.397 15.916  1.00 37.51 ? 257  PRO B CA  1 
ATOM   5336 C C   . PRO B 1 257 ? 6.107   -29.168 16.873  1.00 36.69 ? 257  PRO B C   1 
ATOM   5337 O O   . PRO B 1 257 ? 5.957   -28.544 17.942  1.00 36.32 ? 257  PRO B O   1 
ATOM   5338 C CB  . PRO B 1 257 ? 4.288   -30.791 16.102  1.00 37.78 ? 257  PRO B CB  1 
ATOM   5339 C CG  . PRO B 1 257 ? 4.068   -31.356 14.721  1.00 37.74 ? 257  PRO B CG  1 
ATOM   5340 C CD  . PRO B 1 257 ? 5.062   -30.689 13.831  1.00 38.21 ? 257  PRO B CD  1 
ATOM   5341 N N   . PHE B 1 258 ? 7.289   -29.634 16.449  1.00 35.33 ? 258  PHE B N   1 
ATOM   5342 C CA  . PHE B 1 258 ? 8.558   -29.402 17.143  1.00 33.85 ? 258  PHE B CA  1 
ATOM   5343 C C   . PHE B 1 258 ? 8.848   -27.932 17.467  1.00 32.94 ? 258  PHE B C   1 
ATOM   5344 O O   . PHE B 1 258 ? 9.479   -27.626 18.483  1.00 32.54 ? 258  PHE B O   1 
ATOM   5345 C CB  . PHE B 1 258 ? 9.706   -29.959 16.311  1.00 34.03 ? 258  PHE B CB  1 
ATOM   5346 C CG  . PHE B 1 258 ? 9.845   -31.448 16.366  1.00 33.67 ? 258  PHE B CG  1 
ATOM   5347 C CD1 . PHE B 1 258 ? 10.258  -32.079 17.538  1.00 34.02 ? 258  PHE B CD1 1 
ATOM   5348 C CD2 . PHE B 1 258 ? 9.617   -32.225 15.234  1.00 34.35 ? 258  PHE B CD2 1 
ATOM   5349 C CE1 . PHE B 1 258 ? 10.426  -33.482 17.605  1.00 33.01 ? 258  PHE B CE1 1 
ATOM   5350 C CE2 . PHE B 1 258 ? 9.775   -33.651 15.275  1.00 34.55 ? 258  PHE B CE2 1 
ATOM   5351 C CZ  . PHE B 1 258 ? 10.189  -34.273 16.470  1.00 34.01 ? 258  PHE B CZ  1 
ATOM   5352 N N   . CYS B 1 259 ? 8.385   -27.026 16.621  1.00 32.00 ? 259  CYS B N   1 
ATOM   5353 C CA  . CYS B 1 259 ? 8.699   -25.601 16.773  1.00 31.89 ? 259  CYS B CA  1 
ATOM   5354 C C   . CYS B 1 259 ? 8.045   -24.945 17.964  1.00 31.99 ? 259  CYS B C   1 
ATOM   5355 O O   . CYS B 1 259 ? 8.566   -23.953 18.510  1.00 31.93 ? 259  CYS B O   1 
ATOM   5356 C CB  . CYS B 1 259 ? 8.330   -24.820 15.512  1.00 31.35 ? 259  CYS B CB  1 
ATOM   5357 S SG  . CYS B 1 259 ? 9.023   -25.565 14.063  1.00 30.47 ? 259  CYS B SG  1 
ATOM   5358 N N   . ASP B 1 260 ? 6.899   -25.488 18.351  1.00 32.07 ? 260  ASP B N   1 
ATOM   5359 C CA  . ASP B 1 260 ? 6.104   -24.917 19.437  1.00 32.74 ? 260  ASP B CA  1 
ATOM   5360 C C   . ASP B 1 260 ? 6.651   -25.315 20.820  1.00 31.75 ? 260  ASP B C   1 
ATOM   5361 O O   . ASP B 1 260 ? 6.242   -24.743 21.828  1.00 31.92 ? 260  ASP B O   1 
ATOM   5362 C CB  . ASP B 1 260 ? 4.619   -25.312 19.283  1.00 33.41 ? 260  ASP B CB  1 
ATOM   5363 C CG  . ASP B 1 260 ? 3.652   -24.381 20.073  1.00 37.94 ? 260  ASP B CG  1 
ATOM   5364 O OD1 . ASP B 1 260 ? 4.053   -23.234 20.468  1.00 40.36 ? 260  ASP B OD1 1 
ATOM   5365 O OD2 . ASP B 1 260 ? 2.472   -24.809 20.287  1.00 40.27 ? 260  ASP B OD2 1 
ATOM   5366 N N   . LEU B 1 261 ? 7.571   -26.286 20.865  1.00 30.53 ? 261  LEU B N   1 
ATOM   5367 C CA  . LEU B 1 261 ? 8.242   -26.681 22.112  1.00 29.22 ? 261  LEU B CA  1 
ATOM   5368 C C   . LEU B 1 261 ? 9.279   -25.658 22.559  1.00 28.67 ? 261  LEU B C   1 
ATOM   5369 O O   . LEU B 1 261 ? 9.824   -25.732 23.652  1.00 29.24 ? 261  LEU B O   1 
ATOM   5370 C CB  . LEU B 1 261 ? 8.889   -28.057 21.972  1.00 28.47 ? 261  LEU B CB  1 
ATOM   5371 C CG  . LEU B 1 261 ? 8.023   -29.227 21.466  1.00 28.00 ? 261  LEU B CG  1 
ATOM   5372 C CD1 . LEU B 1 261 ? 8.905   -30.412 21.185  1.00 26.03 ? 261  LEU B CD1 1 
ATOM   5373 C CD2 . LEU B 1 261 ? 6.893   -29.645 22.430  1.00 25.68 ? 261  LEU B CD2 1 
ATOM   5374 N N   . PHE B 1 262 ? 9.545   -24.680 21.727  1.00 27.78 ? 262  PHE B N   1 
ATOM   5375 C CA  . PHE B 1 262 ? 10.507  -23.660 22.084  1.00 27.58 ? 262  PHE B CA  1 
ATOM   5376 C C   . PHE B 1 262 ? 9.828   -22.297 21.991  1.00 27.91 ? 262  PHE B C   1 
ATOM   5377 O O   . PHE B 1 262 ? 8.793   -22.175 21.368  1.00 28.40 ? 262  PHE B O   1 
ATOM   5378 C CB  . PHE B 1 262 ? 11.753  -23.835 21.208  1.00 26.33 ? 262  PHE B CB  1 
ATOM   5379 C CG  . PHE B 1 262 ? 12.253  -25.253 21.211  1.00 25.16 ? 262  PHE B CG  1 
ATOM   5380 C CD1 . PHE B 1 262 ? 12.957  -25.754 22.298  1.00 25.48 ? 262  PHE B CD1 1 
ATOM   5381 C CD2 . PHE B 1 262 ? 11.960  -26.114 20.183  1.00 21.33 ? 262  PHE B CD2 1 
ATOM   5382 C CE1 . PHE B 1 262 ? 13.384  -27.105 22.345  1.00 23.56 ? 262  PHE B CE1 1 
ATOM   5383 C CE2 . PHE B 1 262 ? 12.402  -27.425 20.210  1.00 24.21 ? 262  PHE B CE2 1 
ATOM   5384 C CZ  . PHE B 1 262 ? 13.118  -27.925 21.310  1.00 23.47 ? 262  PHE B CZ  1 
ATOM   5385 N N   . THR B 1 263 ? 10.360  -21.287 22.656  1.00 28.32 ? 263  THR B N   1 
ATOM   5386 C CA  . THR B 1 263 ? 9.766   -19.974 22.577  1.00 28.16 ? 263  THR B CA  1 
ATOM   5387 C C   . THR B 1 263 ? 10.510  -19.122 21.558  1.00 29.29 ? 263  THR B C   1 
ATOM   5388 O O   . THR B 1 263 ? 11.667  -19.432 21.169  1.00 28.40 ? 263  THR B O   1 
ATOM   5389 C CB  . THR B 1 263 ? 9.889   -19.228 23.886  1.00 28.05 ? 263  THR B CB  1 
ATOM   5390 O OG1 . THR B 1 263 ? 11.275  -19.028 24.170  1.00 25.96 ? 263  THR B OG1 1 
ATOM   5391 C CG2 . THR B 1 263 ? 9.263   -19.999 25.004  1.00 29.04 ? 263  THR B CG2 1 
ATOM   5392 N N   . HIS B 1 264 ? 9.870   -18.011 21.179  1.00 30.01 ? 264  HIS B N   1 
ATOM   5393 C CA  . HIS B 1 264 ? 10.472  -17.063 20.266  1.00 31.22 ? 264  HIS B CA  1 
ATOM   5394 C C   . HIS B 1 264 ? 11.896  -16.696 20.682  1.00 31.66 ? 264  HIS B C   1 
ATOM   5395 O O   . HIS B 1 264 ? 12.821  -16.722 19.851  1.00 32.29 ? 264  HIS B O   1 
ATOM   5396 C CB  . HIS B 1 264 ? 9.611   -15.803 20.131  1.00 31.55 ? 264  HIS B CB  1 
ATOM   5397 C CG  . HIS B 1 264 ? 10.143  -14.812 19.135  1.00 33.15 ? 264  HIS B CG  1 
ATOM   5398 N ND1 . HIS B 1 264 ? 10.279  -15.104 17.793  1.00 34.05 ? 264  HIS B ND1 1 
ATOM   5399 C CD2 . HIS B 1 264 ? 10.554  -13.529 19.285  1.00 33.74 ? 264  HIS B CD2 1 
ATOM   5400 C CE1 . HIS B 1 264 ? 10.754  -14.044 17.160  1.00 33.05 ? 264  HIS B CE1 1 
ATOM   5401 N NE2 . HIS B 1 264 ? 10.921  -13.072 18.041  1.00 33.47 ? 264  HIS B NE2 1 
ATOM   5402 N N   . ASP B 1 265 ? 12.063  -16.358 21.963  1.00 31.43 ? 265  ASP B N   1 
ATOM   5403 C CA  . ASP B 1 265 ? 13.348  -15.896 22.488  1.00 31.32 ? 265  ASP B CA  1 
ATOM   5404 C C   . ASP B 1 265 ? 14.371  -17.030 22.438  1.00 30.44 ? 265  ASP B C   1 
ATOM   5405 O O   . ASP B 1 265 ? 15.546  -16.814 22.124  1.00 29.70 ? 265  ASP B O   1 
ATOM   5406 C CB  . ASP B 1 265 ? 13.204  -15.302 23.917  1.00 32.29 ? 265  ASP B CB  1 
ATOM   5407 N N   . GLU B 1 266 ? 13.902  -18.236 22.746  1.00 29.07 ? 266  GLU B N   1 
ATOM   5408 C CA  . GLU B 1 266 ? 14.665  -19.435 22.504  1.00 28.06 ? 266  GLU B CA  1 
ATOM   5409 C C   . GLU B 1 266 ? 15.032  -19.610 21.044  1.00 27.59 ? 266  GLU B C   1 
ATOM   5410 O O   . GLU B 1 266 ? 16.185  -19.981 20.760  1.00 27.67 ? 266  GLU B O   1 
ATOM   5411 C CB  . GLU B 1 266 ? 13.946  -20.647 23.022  1.00 28.00 ? 266  GLU B CB  1 
ATOM   5412 C CG  . GLU B 1 266 ? 14.104  -20.760 24.513  1.00 29.66 ? 266  GLU B CG  1 
ATOM   5413 C CD  . GLU B 1 266 ? 13.062  -21.620 25.182  1.00 31.48 ? 266  GLU B CD  1 
ATOM   5414 O OE1 . GLU B 1 266 ? 12.563  -22.587 24.576  1.00 29.19 ? 266  GLU B OE1 1 
ATOM   5415 O OE2 . GLU B 1 266 ? 12.750  -21.315 26.345  1.00 34.43 ? 266  GLU B OE2 1 
ATOM   5416 N N   . TRP B 1 267 ? 14.103  -19.320 20.117  1.00 25.91 ? 267  TRP B N   1 
ATOM   5417 C CA  . TRP B 1 267 ? 14.510  -19.241 18.696  1.00 24.53 ? 267  TRP B CA  1 
ATOM   5418 C C   . TRP B 1 267 ? 15.613  -18.215 18.373  1.00 24.79 ? 267  TRP B C   1 
ATOM   5419 O O   . TRP B 1 267 ? 16.533  -18.522 17.621  1.00 24.59 ? 267  TRP B O   1 
ATOM   5420 C CB  . TRP B 1 267 ? 13.321  -19.138 17.744  1.00 23.81 ? 267  TRP B CB  1 
ATOM   5421 C CG  . TRP B 1 267 ? 12.597  -20.458 17.699  1.00 21.37 ? 267  TRP B CG  1 
ATOM   5422 C CD1 . TRP B 1 267 ? 11.313  -20.728 18.131  1.00 18.76 ? 267  TRP B CD1 1 
ATOM   5423 C CD2 . TRP B 1 267 ? 13.149  -21.703 17.271  1.00 17.44 ? 267  TRP B CD2 1 
ATOM   5424 N NE1 . TRP B 1 267 ? 11.032  -22.059 17.945  1.00 17.73 ? 267  TRP B NE1 1 
ATOM   5425 C CE2 . TRP B 1 267 ? 12.150  -22.682 17.438  1.00 17.88 ? 267  TRP B CE2 1 
ATOM   5426 C CE3 . TRP B 1 267 ? 14.397  -22.082 16.745  1.00 19.08 ? 267  TRP B CE3 1 
ATOM   5427 C CZ2 . TRP B 1 267 ? 12.353  -24.022 17.088  1.00 17.95 ? 267  TRP B CZ2 1 
ATOM   5428 C CZ3 . TRP B 1 267 ? 14.609  -23.420 16.384  1.00 18.49 ? 267  TRP B CZ3 1 
ATOM   5429 C CH2 . TRP B 1 267 ? 13.597  -24.376 16.569  1.00 18.74 ? 267  TRP B CH2 1 
ATOM   5430 N N   . ILE B 1 268 ? 15.532  -17.020 18.949  1.00 24.54 ? 268  ILE B N   1 
ATOM   5431 C CA  . ILE B 1 268 ? 16.553  -15.997 18.741  1.00 24.81 ? 268  ILE B CA  1 
ATOM   5432 C C   . ILE B 1 268 ? 17.977  -16.503 19.075  1.00 25.23 ? 268  ILE B C   1 
ATOM   5433 O O   . ILE B 1 268 ? 18.942  -16.288 18.301  1.00 24.50 ? 268  ILE B O   1 
ATOM   5434 C CB  . ILE B 1 268 ? 16.239  -14.726 19.561  1.00 24.95 ? 268  ILE B CB  1 
ATOM   5435 C CG1 . ILE B 1 268 ? 15.058  -13.989 18.926  1.00 25.65 ? 268  ILE B CG1 1 
ATOM   5436 C CG2 . ILE B 1 268 ? 17.430  -13.793 19.621  1.00 24.81 ? 268  ILE B CG2 1 
ATOM   5437 C CD1 . ILE B 1 268 ? 14.590  -12.812 19.716  1.00 27.67 ? 268  ILE B CD1 1 
ATOM   5438 N N   . ASN B 1 269 ? 18.096  -17.162 20.230  1.00 24.04 ? 269  ASN B N   1 
ATOM   5439 C CA  . ASN B 1 269 ? 19.343  -17.710 20.655  1.00 23.15 ? 269  ASN B CA  1 
ATOM   5440 C C   . ASN B 1 269 ? 19.727  -18.757 19.645  1.00 22.92 ? 269  ASN B C   1 
ATOM   5441 O O   . ASN B 1 269 ? 20.840  -18.743 19.131  1.00 23.36 ? 269  ASN B O   1 
ATOM   5442 C CB  . ASN B 1 269 ? 19.239  -18.303 22.063  1.00 23.01 ? 269  ASN B CB  1 
ATOM   5443 C CG  . ASN B 1 269 ? 19.228  -17.242 23.148  1.00 24.95 ? 269  ASN B CG  1 
ATOM   5444 O OD1 . ASN B 1 269 ? 20.185  -16.489 23.305  1.00 27.48 ? 269  ASN B OD1 1 
ATOM   5445 N ND2 . ASN B 1 269 ? 18.153  -17.199 23.923  1.00 26.81 ? 269  ASN B ND2 1 
ATOM   5446 N N   . TYR B 1 270 ? 18.811  -19.661 19.326  1.00 22.20 ? 270  TYR B N   1 
ATOM   5447 C CA  . TYR B 1 270 ? 19.138  -20.650 18.308  1.00 21.50 ? 270  TYR B CA  1 
ATOM   5448 C C   . TYR B 1 270 ? 19.763  -20.000 17.052  1.00 20.90 ? 270  TYR B C   1 
ATOM   5449 O O   . TYR B 1 270 ? 20.834  -20.410 16.589  1.00 19.98 ? 270  TYR B O   1 
ATOM   5450 C CB  . TYR B 1 270 ? 17.919  -21.430 17.924  1.00 20.92 ? 270  TYR B CB  1 
ATOM   5451 C CG  . TYR B 1 270 ? 18.205  -22.572 16.988  1.00 22.48 ? 270  TYR B CG  1 
ATOM   5452 C CD1 . TYR B 1 270 ? 18.648  -23.803 17.468  1.00 21.01 ? 270  TYR B CD1 1 
ATOM   5453 C CD2 . TYR B 1 270 ? 18.001  -22.426 15.613  1.00 22.19 ? 270  TYR B CD2 1 
ATOM   5454 C CE1 . TYR B 1 270 ? 18.885  -24.861 16.601  1.00 20.63 ? 270  TYR B CE1 1 
ATOM   5455 C CE2 . TYR B 1 270 ? 18.239  -23.460 14.747  1.00 22.20 ? 270  TYR B CE2 1 
ATOM   5456 C CZ  . TYR B 1 270 ? 18.673  -24.689 15.238  1.00 23.18 ? 270  TYR B CZ  1 
ATOM   5457 O OH  . TYR B 1 270 ? 18.874  -25.731 14.340  1.00 22.09 ? 270  TYR B OH  1 
ATOM   5458 N N   . ASP B 1 271 ? 19.098  -18.985 16.521  1.00 19.99 ? 271  ASP B N   1 
ATOM   5459 C CA  . ASP B 1 271 ? 19.589  -18.340 15.324  1.00 20.09 ? 271  ASP B CA  1 
ATOM   5460 C C   . ASP B 1 271 ? 21.014  -17.864 15.542  1.00 19.90 ? 271  ASP B C   1 
ATOM   5461 O O   . ASP B 1 271 ? 21.898  -18.140 14.730  1.00 20.56 ? 271  ASP B O   1 
ATOM   5462 C CB  . ASP B 1 271 ? 18.681  -17.187 14.926  1.00 20.18 ? 271  ASP B CB  1 
ATOM   5463 C CG  . ASP B 1 271 ? 19.049  -16.583 13.562  1.00 20.47 ? 271  ASP B CG  1 
ATOM   5464 O OD1 . ASP B 1 271 ? 18.943  -17.294 12.536  1.00 15.63 ? 271  ASP B OD1 1 
ATOM   5465 O OD2 . ASP B 1 271 ? 19.406  -15.377 13.531  1.00 20.76 ? 271  ASP B OD2 1 
ATOM   5466 N N   . TYR B 1 272 ? 21.230  -17.194 16.667  1.00 18.95 ? 272  TYR B N   1 
ATOM   5467 C CA  . TYR B 1 272 ? 22.488  -16.565 16.962  1.00 18.36 ? 272  TYR B CA  1 
ATOM   5468 C C   . TYR B 1 272 ? 23.609  -17.561 17.115  1.00 18.31 ? 272  TYR B C   1 
ATOM   5469 O O   . TYR B 1 272 ? 24.715  -17.345 16.611  1.00 17.47 ? 272  TYR B O   1 
ATOM   5470 C CB  . TYR B 1 272 ? 22.368  -15.675 18.192  1.00 18.86 ? 272  TYR B CB  1 
ATOM   5471 C CG  . TYR B 1 272 ? 23.593  -14.832 18.407  1.00 19.41 ? 272  TYR B CG  1 
ATOM   5472 C CD1 . TYR B 1 272 ? 23.858  -13.737 17.601  1.00 20.04 ? 272  TYR B CD1 1 
ATOM   5473 C CD2 . TYR B 1 272 ? 24.488  -15.148 19.407  1.00 19.20 ? 272  TYR B CD2 1 
ATOM   5474 C CE1 . TYR B 1 272 ? 25.005  -12.989 17.793  1.00 22.37 ? 272  TYR B CE1 1 
ATOM   5475 C CE2 . TYR B 1 272 ? 25.612  -14.396 19.620  1.00 21.11 ? 272  TYR B CE2 1 
ATOM   5476 C CZ  . TYR B 1 272 ? 25.870  -13.316 18.820  1.00 21.34 ? 272  TYR B CZ  1 
ATOM   5477 O OH  . TYR B 1 272 ? 27.012  -12.591 19.038  1.00 23.48 ? 272  TYR B OH  1 
ATOM   5478 N N   . LEU B 1 273 ? 23.308  -18.666 17.805  1.00 18.27 ? 273  LEU B N   1 
ATOM   5479 C CA  . LEU B 1 273 ? 24.183  -19.820 17.817  1.00 18.21 ? 273  LEU B CA  1 
ATOM   5480 C C   . LEU B 1 273 ? 24.661  -20.145 16.418  1.00 18.39 ? 273  LEU B C   1 
ATOM   5481 O O   . LEU B 1 273 ? 25.875  -20.234 16.186  1.00 19.43 ? 273  LEU B O   1 
ATOM   5482 C CB  . LEU B 1 273 ? 23.518  -21.044 18.397  1.00 17.38 ? 273  LEU B CB  1 
ATOM   5483 C CG  . LEU B 1 273 ? 24.373  -22.309 18.244  1.00 19.12 ? 273  LEU B CG  1 
ATOM   5484 C CD1 . LEU B 1 273 ? 25.535  -22.459 19.265  1.00 20.55 ? 273  LEU B CD1 1 
ATOM   5485 C CD2 . LEU B 1 273 ? 23.492  -23.499 18.341  1.00 21.93 ? 273  LEU B CD2 1 
ATOM   5486 N N   . GLN B 1 274 ? 23.727  -20.347 15.486  1.00 18.17 ? 274  GLN B N   1 
ATOM   5487 C CA  . GLN B 1 274 ? 24.109  -20.657 14.095  1.00 17.32 ? 274  GLN B CA  1 
ATOM   5488 C C   . GLN B 1 274 ? 25.005  -19.544 13.512  1.00 17.03 ? 274  GLN B C   1 
ATOM   5489 O O   . GLN B 1 274 ? 25.989  -19.838 12.828  1.00 17.65 ? 274  GLN B O   1 
ATOM   5490 C CB  . GLN B 1 274 ? 22.898  -20.898 13.190  1.00 17.55 ? 274  GLN B CB  1 
ATOM   5491 C CG  . GLN B 1 274 ? 21.796  -21.858 13.710  1.00 16.47 ? 274  GLN B CG  1 
ATOM   5492 C CD  . GLN B 1 274 ? 22.308  -23.192 14.217  1.00 22.67 ? 274  GLN B CD  1 
ATOM   5493 O OE1 . GLN B 1 274 ? 23.317  -23.773 13.715  1.00 24.18 ? 274  GLN B OE1 1 
ATOM   5494 N NE2 . GLN B 1 274 ? 21.614  -23.709 15.228  1.00 23.87 ? 274  GLN B NE2 1 
ATOM   5495 N N   . SER B 1 275 ? 24.709  -18.276 13.788  1.00 15.50 ? 275  SER B N   1 
ATOM   5496 C CA  . SER B 1 275 ? 25.609  -17.253 13.302  1.00 15.50 ? 275  SER B CA  1 
ATOM   5497 C C   . SER B 1 275 ? 27.032  -17.474 13.820  1.00 15.94 ? 275  SER B C   1 
ATOM   5498 O O   . SER B 1 275 ? 27.993  -17.304 13.074  1.00 14.39 ? 275  SER B O   1 
ATOM   5499 C CB  . SER B 1 275 ? 25.080  -15.841 13.596  1.00 15.45 ? 275  SER B CB  1 
ATOM   5500 O OG  . SER B 1 275 ? 23.811  -15.653 12.986  1.00 15.95 ? 275  SER B OG  1 
ATOM   5501 N N   . LEU B 1 276 ? 27.156  -17.858 15.109  1.00 17.06 ? 276  LEU B N   1 
ATOM   5502 C CA  . LEU B 1 276 ? 28.479  -18.137 15.770  1.00 17.05 ? 276  LEU B CA  1 
ATOM   5503 C C   . LEU B 1 276 ? 29.237  -19.263 15.147  1.00 16.84 ? 276  LEU B C   1 
ATOM   5504 O O   . LEU B 1 276 ? 30.431  -19.093 14.826  1.00 16.75 ? 276  LEU B O   1 
ATOM   5505 C CB  . LEU B 1 276 ? 28.354  -18.418 17.277  1.00 17.35 ? 276  LEU B CB  1 
ATOM   5506 C CG  . LEU B 1 276 ? 28.006  -17.206 18.152  1.00 18.59 ? 276  LEU B CG  1 
ATOM   5507 C CD1 . LEU B 1 276 ? 27.546  -17.671 19.521  1.00 15.46 ? 276  LEU B CD1 1 
ATOM   5508 C CD2 . LEU B 1 276 ? 29.204  -16.268 18.230  1.00 20.15 ? 276  LEU B CD2 1 
ATOM   5509 N N   . LYS B 1 277 ? 28.566  -20.405 14.992  1.00 16.29 ? 277  LYS B N   1 
ATOM   5510 C CA  . LYS B 1 277 ? 29.139  -21.529 14.274  1.00 16.67 ? 277  LYS B CA  1 
ATOM   5511 C C   . LYS B 1 277 ? 29.777  -21.049 12.933  1.00 17.03 ? 277  LYS B C   1 
ATOM   5512 O O   . LYS B 1 277 ? 30.994  -21.350 12.622  1.00 16.33 ? 277  LYS B O   1 
ATOM   5513 C CB  . LYS B 1 277 ? 28.092  -22.595 13.983  1.00 17.11 ? 277  LYS B CB  1 
ATOM   5514 C CG  . LYS B 1 277 ? 27.421  -23.372 15.170  1.00 18.51 ? 277  LYS B CG  1 
ATOM   5515 C CD  . LYS B 1 277 ? 27.055  -24.831 14.637  1.00 21.06 ? 277  LYS B CD  1 
ATOM   5516 C CE  . LYS B 1 277 ? 25.820  -25.497 15.341  1.00 26.40 ? 277  LYS B CE  1 
ATOM   5517 N NZ  . LYS B 1 277 ? 25.000  -26.553 14.537  1.00 24.76 ? 277  LYS B NZ  1 
ATOM   5518 N N   . LYS B 1 278 ? 28.985  -20.303 12.138  1.00 16.55 ? 278  LYS B N   1 
ATOM   5519 C CA  . LYS B 1 278 ? 29.487  -19.835 10.838  1.00 16.39 ? 278  LYS B CA  1 
ATOM   5520 C C   . LYS B 1 278 ? 30.621  -18.812 10.977  1.00 17.15 ? 278  LYS B C   1 
ATOM   5521 O O   . LYS B 1 278 ? 31.721  -19.004 10.383  1.00 17.04 ? 278  LYS B O   1 
ATOM   5522 C CB  . LYS B 1 278 ? 28.369  -19.384 9.892   1.00 16.31 ? 278  LYS B CB  1 
ATOM   5523 C CG  . LYS B 1 278 ? 27.382  -20.507 9.515   1.00 16.50 ? 278  LYS B CG  1 
ATOM   5524 C CD  . LYS B 1 278 ? 28.016  -21.870 9.213   1.00 14.99 ? 278  LYS B CD  1 
ATOM   5525 C CE  . LYS B 1 278 ? 26.972  -22.869 8.691   1.00 15.44 ? 278  LYS B CE  1 
ATOM   5526 N NZ  . LYS B 1 278 ? 27.598  -24.184 8.316   1.00 13.58 ? 278  LYS B NZ  1 
ATOM   5527 N N   . TYR B 1 279 ? 30.394  -17.775 11.797  1.00 16.79 ? 279  TYR B N   1 
ATOM   5528 C CA  . TYR B 1 279 ? 31.409  -16.756 12.024  1.00 17.85 ? 279  TYR B CA  1 
ATOM   5529 C C   . TYR B 1 279 ? 32.751  -17.272 12.531  1.00 18.36 ? 279  TYR B C   1 
ATOM   5530 O O   . TYR B 1 279 ? 33.816  -16.856 12.017  1.00 18.34 ? 279  TYR B O   1 
ATOM   5531 C CB  . TYR B 1 279 ? 30.908  -15.661 12.947  1.00 18.49 ? 279  TYR B CB  1 
ATOM   5532 C CG  . TYR B 1 279 ? 31.809  -14.463 13.026  1.00 19.20 ? 279  TYR B CG  1 
ATOM   5533 C CD1 . TYR B 1 279 ? 31.736  -13.437 12.069  1.00 21.74 ? 279  TYR B CD1 1 
ATOM   5534 C CD2 . TYR B 1 279 ? 32.723  -14.340 14.045  1.00 20.51 ? 279  TYR B CD2 1 
ATOM   5535 C CE1 . TYR B 1 279 ? 32.589  -12.293 12.131  1.00 21.80 ? 279  TYR B CE1 1 
ATOM   5536 C CE2 . TYR B 1 279 ? 33.586  -13.212 14.122  1.00 21.43 ? 279  TYR B CE2 1 
ATOM   5537 C CZ  . TYR B 1 279 ? 33.511  -12.190 13.179  1.00 22.49 ? 279  TYR B CZ  1 
ATOM   5538 O OH  . TYR B 1 279 ? 34.357  -11.083 13.294  1.00 22.58 ? 279  TYR B OH  1 
ATOM   5539 N N   . TYR B 1 280 ? 32.716  -18.157 13.536  1.00 18.33 ? 280  TYR B N   1 
ATOM   5540 C CA  . TYR B 1 280 ? 33.966  -18.647 14.120  1.00 17.86 ? 280  TYR B CA  1 
ATOM   5541 C C   . TYR B 1 280 ? 34.523  -19.843 13.356  1.00 18.53 ? 280  TYR B C   1 
ATOM   5542 O O   . TYR B 1 280 ? 35.709  -20.148 13.485  1.00 18.53 ? 280  TYR B O   1 
ATOM   5543 C CB  . TYR B 1 280 ? 33.868  -18.855 15.670  1.00 17.66 ? 280  TYR B CB  1 
ATOM   5544 C CG  . TYR B 1 280 ? 33.840  -17.517 16.371  1.00 15.05 ? 280  TYR B CG  1 
ATOM   5545 C CD1 . TYR B 1 280 ? 34.993  -16.707 16.405  1.00 13.87 ? 280  TYR B CD1 1 
ATOM   5546 C CD2 . TYR B 1 280 ? 32.638  -17.018 16.939  1.00 13.71 ? 280  TYR B CD2 1 
ATOM   5547 C CE1 . TYR B 1 280 ? 34.960  -15.406 16.991  1.00 14.32 ? 280  TYR B CE1 1 
ATOM   5548 C CE2 . TYR B 1 280 ? 32.581  -15.756 17.528  1.00 10.04 ? 280  TYR B CE2 1 
ATOM   5549 C CZ  . TYR B 1 280 ? 33.746  -14.927 17.554  1.00 13.98 ? 280  TYR B CZ  1 
ATOM   5550 O OH  . TYR B 1 280 ? 33.714  -13.626 18.108  1.00 10.58 ? 280  TYR B OH  1 
ATOM   5551 N N   . GLY B 1 281 ? 33.671  -20.507 12.556  1.00 18.51 ? 281  GLY B N   1 
ATOM   5552 C CA  . GLY B 1 281 ? 34.089  -21.650 11.749  1.00 17.54 ? 281  GLY B CA  1 
ATOM   5553 C C   . GLY B 1 281 ? 34.805  -21.225 10.474  1.00 17.85 ? 281  GLY B C   1 
ATOM   5554 O O   . GLY B 1 281 ? 35.880  -21.730 10.152  1.00 16.85 ? 281  GLY B O   1 
ATOM   5555 N N   . HIS B 1 282 ? 34.208  -20.284 9.746   1.00 18.27 ? 282  HIS B N   1 
ATOM   5556 C CA  . HIS B 1 282 ? 34.644  -19.987 8.384   1.00 18.76 ? 282  HIS B CA  1 
ATOM   5557 C C   . HIS B 1 282 ? 34.768  -18.485 8.085   1.00 18.97 ? 282  HIS B C   1 
ATOM   5558 O O   . HIS B 1 282 ? 35.441  -18.068 7.112   1.00 18.54 ? 282  HIS B O   1 
ATOM   5559 C CB  . HIS B 1 282 ? 33.725  -20.706 7.392   1.00 18.63 ? 282  HIS B CB  1 
ATOM   5560 C CG  . HIS B 1 282 ? 33.704  -22.187 7.587   1.00 20.46 ? 282  HIS B CG  1 
ATOM   5561 N ND1 . HIS B 1 282 ? 34.569  -23.031 6.920   1.00 21.62 ? 282  HIS B ND1 1 
ATOM   5562 C CD2 . HIS B 1 282 ? 32.981  -22.970 8.431   1.00 21.76 ? 282  HIS B CD2 1 
ATOM   5563 C CE1 . HIS B 1 282 ? 34.366  -24.273 7.324   1.00 22.89 ? 282  HIS B CE1 1 
ATOM   5564 N NE2 . HIS B 1 282 ? 33.407  -24.264 8.241   1.00 25.23 ? 282  HIS B NE2 1 
ATOM   5565 N N   . GLY B 1 283 ? 34.118  -17.675 8.915   1.00 18.38 ? 283  GLY B N   1 
ATOM   5566 C CA  . GLY B 1 283 ? 34.182  -16.228 8.739   1.00 17.70 ? 283  GLY B CA  1 
ATOM   5567 C C   . GLY B 1 283 ? 35.369  -15.575 9.408   1.00 17.69 ? 283  GLY B C   1 
ATOM   5568 O O   . GLY B 1 283 ? 36.392  -16.222 9.721   1.00 17.31 ? 283  GLY B O   1 
ATOM   5569 N N   . ALA B 1 284 ? 35.222  -14.269 9.608   1.00 17.52 ? 284  ALA B N   1 
ATOM   5570 C CA  . ALA B 1 284 ? 36.263  -13.406 10.207  1.00 17.94 ? 284  ALA B CA  1 
ATOM   5571 C C   . ALA B 1 284 ? 36.733  -13.852 11.587  1.00 17.70 ? 284  ALA B C   1 
ATOM   5572 O O   . ALA B 1 284 ? 37.880  -13.629 11.951  1.00 17.43 ? 284  ALA B O   1 
ATOM   5573 C CB  . ALA B 1 284 ? 35.779  -11.952 10.289  1.00 17.33 ? 284  ALA B CB  1 
ATOM   5574 N N   . GLY B 1 285 ? 35.827  -14.436 12.363  1.00 17.74 ? 285  GLY B N   1 
ATOM   5575 C CA  . GLY B 1 285 ? 36.208  -14.949 13.672  1.00 18.10 ? 285  GLY B CA  1 
ATOM   5576 C C   . GLY B 1 285 ? 37.262  -16.052 13.690  1.00 17.64 ? 285  GLY B C   1 
ATOM   5577 O O   . GLY B 1 285 ? 37.839  -16.339 14.744  1.00 18.25 ? 285  GLY B O   1 
ATOM   5578 N N   . ASN B 1 286 ? 37.493  -16.705 12.557  1.00 17.11 ? 286  ASN B N   1 
ATOM   5579 C CA  . ASN B 1 286 ? 38.476  -17.783 12.526  1.00 16.86 ? 286  ASN B CA  1 
ATOM   5580 C C   . ASN B 1 286 ? 39.716  -17.329 11.750  1.00 17.03 ? 286  ASN B C   1 
ATOM   5581 O O   . ASN B 1 286 ? 39.599  -16.827 10.670  1.00 16.37 ? 286  ASN B O   1 
ATOM   5582 C CB  . ASN B 1 286 ? 37.866  -19.024 11.898  1.00 15.83 ? 286  ASN B CB  1 
ATOM   5583 C CG  . ASN B 1 286 ? 38.839  -20.146 11.815  1.00 17.86 ? 286  ASN B CG  1 
ATOM   5584 O OD1 . ASN B 1 286 ? 39.880  -20.062 11.108  1.00 23.28 ? 286  ASN B OD1 1 
ATOM   5585 N ND2 . ASN B 1 286 ? 38.564  -21.205 12.544  1.00 13.73 ? 286  ASN B ND2 1 
ATOM   5586 N N   . PRO B 1 287 ? 40.915  -17.536 12.292  1.00 18.06 ? 287  PRO B N   1 
ATOM   5587 C CA  . PRO B 1 287 ? 42.076  -16.861 11.669  1.00 18.37 ? 287  PRO B CA  1 
ATOM   5588 C C   . PRO B 1 287 ? 42.316  -17.278 10.246  1.00 18.32 ? 287  PRO B C   1 
ATOM   5589 O O   . PRO B 1 287 ? 42.997  -16.570 9.524   1.00 19.53 ? 287  PRO B O   1 
ATOM   5590 C CB  . PRO B 1 287 ? 43.263  -17.326 12.503  1.00 17.92 ? 287  PRO B CB  1 
ATOM   5591 C CG  . PRO B 1 287 ? 42.765  -18.521 13.287  1.00 18.72 ? 287  PRO B CG  1 
ATOM   5592 C CD  . PRO B 1 287 ? 41.297  -18.456 13.384  1.00 18.16 ? 287  PRO B CD  1 
ATOM   5593 N N   . LEU B 1 288 ? 41.789  -18.427 9.844   1.00 18.12 ? 288  LEU B N   1 
ATOM   5594 C CA  . LEU B 1 288 ? 42.066  -18.958 8.497   1.00 17.23 ? 288  LEU B CA  1 
ATOM   5595 C C   . LEU B 1 288 ? 40.799  -19.050 7.665   1.00 16.48 ? 288  LEU B C   1 
ATOM   5596 O O   . LEU B 1 288 ? 40.774  -19.632 6.581   1.00 17.48 ? 288  LEU B O   1 
ATOM   5597 C CB  . LEU B 1 288 ? 42.727  -20.330 8.604   1.00 17.43 ? 288  LEU B CB  1 
ATOM   5598 C CG  . LEU B 1 288 ? 44.229  -20.331 8.851   1.00 19.32 ? 288  LEU B CG  1 
ATOM   5599 C CD1 . LEU B 1 288 ? 44.776  -21.722 9.237   1.00 18.95 ? 288  LEU B CD1 1 
ATOM   5600 C CD2 . LEU B 1 288 ? 44.899  -19.812 7.560   1.00 21.71 ? 288  LEU B CD2 1 
ATOM   5601 N N   . GLY B 1 289 ? 39.719  -18.502 8.191   1.00 15.67 ? 289  GLY B N   1 
ATOM   5602 C CA  . GLY B 1 289 ? 38.414  -18.615 7.544   1.00 14.08 ? 289  GLY B CA  1 
ATOM   5603 C C   . GLY B 1 289 ? 38.383  -17.815 6.243   1.00 13.26 ? 289  GLY B C   1 
ATOM   5604 O O   . GLY B 1 289 ? 38.168  -18.401 5.191   1.00 12.63 ? 289  GLY B O   1 
ATOM   5605 N N   . PRO B 1 290 ? 38.603  -16.474 6.314   1.00 12.64 ? 290  PRO B N   1 
ATOM   5606 C CA  . PRO B 1 290 ? 38.572  -15.668 5.094   1.00 12.33 ? 290  PRO B CA  1 
ATOM   5607 C C   . PRO B 1 290 ? 39.671  -16.136 4.118   1.00 13.45 ? 290  PRO B C   1 
ATOM   5608 O O   . PRO B 1 290 ? 39.591  -15.899 2.888   1.00 11.88 ? 290  PRO B O   1 
ATOM   5609 C CB  . PRO B 1 290 ? 38.893  -14.236 5.581   1.00 11.39 ? 290  PRO B CB  1 
ATOM   5610 C CG  . PRO B 1 290 ? 38.713  -14.229 7.080   1.00 12.23 ? 290  PRO B CG  1 
ATOM   5611 C CD  . PRO B 1 290 ? 39.050  -15.677 7.485   1.00 12.55 ? 290  PRO B CD  1 
ATOM   5612 N N   . THR B 1 291 ? 40.679  -16.821 4.655   1.00 13.52 ? 291  THR B N   1 
ATOM   5613 C CA  . THR B 1 291 ? 41.717  -17.329 3.782   1.00 14.73 ? 291  THR B CA  1 
ATOM   5614 C C   . THR B 1 291 ? 41.135  -18.461 2.902   1.00 15.30 ? 291  THR B C   1 
ATOM   5615 O O   . THR B 1 291 ? 41.636  -18.740 1.811   1.00 15.73 ? 291  THR B O   1 
ATOM   5616 C CB  . THR B 1 291 ? 42.981  -17.749 4.570   1.00 14.77 ? 291  THR B CB  1 
ATOM   5617 O OG1 . THR B 1 291 ? 43.849  -16.606 4.716   1.00 13.87 ? 291  THR B OG1 1 
ATOM   5618 C CG2 . THR B 1 291 ? 43.713  -18.874 3.851   1.00 12.13 ? 291  THR B CG2 1 
ATOM   5619 N N   . GLN B 1 292 ? 40.063  -19.070 3.373   1.00 14.77 ? 292  GLN B N   1 
ATOM   5620 C CA  . GLN B 1 292 ? 39.433  -20.129 2.614   1.00 15.50 ? 292  GLN B CA  1 
ATOM   5621 C C   . GLN B 1 292 ? 38.764  -19.534 1.372   1.00 15.31 ? 292  GLN B C   1 
ATOM   5622 O O   . GLN B 1 292 ? 38.584  -20.222 0.393   1.00 13.73 ? 292  GLN B O   1 
ATOM   5623 C CB  . GLN B 1 292 ? 38.457  -20.961 3.490   1.00 15.19 ? 292  GLN B CB  1 
ATOM   5624 C CG  . GLN B 1 292 ? 39.180  -21.612 4.661   1.00 14.83 ? 292  GLN B CG  1 
ATOM   5625 C CD  . GLN B 1 292 ? 40.426  -22.407 4.211   1.00 13.94 ? 292  GLN B CD  1 
ATOM   5626 O OE1 . GLN B 1 292 ? 40.294  -23.443 3.548   1.00 16.23 ? 292  GLN B OE1 1 
ATOM   5627 N NE2 . GLN B 1 292 ? 41.609  -21.970 4.611   1.00 8.97  ? 292  GLN B NE2 1 
ATOM   5628 N N   . GLY B 1 293 ? 38.460  -18.229 1.417   1.00 16.34 ? 293  GLY B N   1 
ATOM   5629 C CA  . GLY B 1 293 ? 37.767  -17.543 0.308   1.00 15.39 ? 293  GLY B CA  1 
ATOM   5630 C C   . GLY B 1 293 ? 38.673  -16.851 -0.692  1.00 15.61 ? 293  GLY B C   1 
ATOM   5631 O O   . GLY B 1 293 ? 38.184  -16.194 -1.629  1.00 15.34 ? 293  GLY B O   1 
ATOM   5632 N N   . VAL B 1 294 ? 39.997  -16.946 -0.523  1.00 16.36 ? 294  VAL B N   1 
ATOM   5633 C CA  . VAL B 1 294 ? 40.836  -16.091 -1.368  1.00 16.15 ? 294  VAL B CA  1 
ATOM   5634 C C   . VAL B 1 294 ? 40.971  -16.601 -2.786  1.00 15.17 ? 294  VAL B C   1 
ATOM   5635 O O   . VAL B 1 294 ? 41.119  -15.808 -3.703  1.00 15.51 ? 294  VAL B O   1 
ATOM   5636 C CB  . VAL B 1 294 ? 42.195  -15.573 -0.721  1.00 16.98 ? 294  VAL B CB  1 
ATOM   5637 C CG1 . VAL B 1 294 ? 42.209  -15.778 0.752   1.00 17.24 ? 294  VAL B CG1 1 
ATOM   5638 C CG2 . VAL B 1 294 ? 43.412  -16.144 -1.413  1.00 15.63 ? 294  VAL B CG2 1 
ATOM   5639 N N   . GLY B 1 295 ? 40.840  -17.914 -2.973  1.00 15.64 ? 295  GLY B N   1 
ATOM   5640 C CA  . GLY B 1 295 ? 40.875  -18.533 -4.322  1.00 14.39 ? 295  GLY B CA  1 
ATOM   5641 C C   . GLY B 1 295 ? 39.745  -18.040 -5.222  1.00 14.06 ? 295  GLY B C   1 
ATOM   5642 O O   . GLY B 1 295 ? 39.972  -17.639 -6.372  1.00 15.02 ? 295  GLY B O   1 
ATOM   5643 N N   . TYR B 1 296 ? 38.534  -18.035 -4.693  1.00 12.49 ? 296  TYR B N   1 
ATOM   5644 C CA  . TYR B 1 296 ? 37.406  -17.610 -5.428  1.00 12.32 ? 296  TYR B CA  1 
ATOM   5645 C C   . TYR B 1 296 ? 37.462  -16.133 -5.658  1.00 12.77 ? 296  TYR B C   1 
ATOM   5646 O O   . TYR B 1 296 ? 37.051  -15.667 -6.719  1.00 14.05 ? 296  TYR B O   1 
ATOM   5647 C CB  . TYR B 1 296 ? 36.117  -17.944 -4.653  1.00 13.56 ? 296  TYR B CB  1 
ATOM   5648 C CG  . TYR B 1 296 ? 34.863  -17.828 -5.495  1.00 12.46 ? 296  TYR B CG  1 
ATOM   5649 C CD1 . TYR B 1 296 ? 34.509  -18.821 -6.400  1.00 14.13 ? 296  TYR B CD1 1 
ATOM   5650 C CD2 . TYR B 1 296 ? 34.047  -16.692 -5.396  1.00 16.13 ? 296  TYR B CD2 1 
ATOM   5651 C CE1 . TYR B 1 296 ? 33.348  -18.694 -7.178  1.00 17.42 ? 296  TYR B CE1 1 
ATOM   5652 C CE2 . TYR B 1 296 ? 32.899  -16.549 -6.147  1.00 17.22 ? 296  TYR B CE2 1 
ATOM   5653 C CZ  . TYR B 1 296 ? 32.540  -17.550 -7.049  1.00 19.41 ? 296  TYR B CZ  1 
ATOM   5654 O OH  . TYR B 1 296 ? 31.370  -17.386 -7.798  1.00 20.28 ? 296  TYR B OH  1 
ATOM   5655 N N   . ALA B 1 297 ? 37.940  -15.382 -4.674  1.00 12.51 ? 297  ALA B N   1 
ATOM   5656 C CA  . ALA B 1 297 ? 38.088  -13.943 -4.820  1.00 13.20 ? 297  ALA B CA  1 
ATOM   5657 C C   . ALA B 1 297 ? 39.043  -13.621 -5.924  1.00 14.03 ? 297  ALA B C   1 
ATOM   5658 O O   . ALA B 1 297 ? 38.847  -12.638 -6.591  1.00 15.01 ? 297  ALA B O   1 
ATOM   5659 C CB  . ALA B 1 297 ? 38.549  -13.237 -3.480  1.00 12.41 ? 297  ALA B CB  1 
ATOM   5660 N N   . ASN B 1 298 ? 40.090  -14.410 -6.130  1.00 14.85 ? 298  ASN B N   1 
ATOM   5661 C CA  . ASN B 1 298 ? 40.997  -14.106 -7.252  1.00 16.24 ? 298  ASN B CA  1 
ATOM   5662 C C   . ASN B 1 298 ? 40.404  -14.527 -8.610  1.00 17.37 ? 298  ASN B C   1 
ATOM   5663 O O   . ASN B 1 298 ? 40.783  -13.958 -9.660  1.00 18.03 ? 298  ASN B O   1 
ATOM   5664 C CB  . ASN B 1 298 ? 42.392  -14.727 -7.055  1.00 16.27 ? 298  ASN B CB  1 
ATOM   5665 C CG  . ASN B 1 298 ? 43.159  -14.084 -5.896  1.00 16.94 ? 298  ASN B CG  1 
ATOM   5666 O OD1 . ASN B 1 298 ? 43.305  -12.871 -5.835  1.00 15.12 ? 298  ASN B OD1 1 
ATOM   5667 N ND2 . ASN B 1 298 ? 43.625  -14.910 -4.958  1.00 15.32 ? 298  ASN B ND2 1 
ATOM   5668 N N   . GLU B 1 299 ? 39.471  -15.496 -8.603  1.00 16.75 ? 299  GLU B N   1 
ATOM   5669 C CA  . GLU B 1 299 ? 38.758  -15.868 -9.847  1.00 15.98 ? 299  GLU B CA  1 
ATOM   5670 C C   . GLU B 1 299 ? 37.757  -14.787 -10.175 1.00 16.70 ? 299  GLU B C   1 
ATOM   5671 O O   . GLU B 1 299 ? 37.640  -14.354 -11.340 1.00 16.59 ? 299  GLU B O   1 
ATOM   5672 C CB  . GLU B 1 299 ? 38.079  -17.223 -9.740  1.00 15.43 ? 299  GLU B CB  1 
ATOM   5673 C CG  . GLU B 1 299 ? 39.120  -18.346 -9.630  1.00 14.68 ? 299  GLU B CG  1 
ATOM   5674 C CD  . GLU B 1 299 ? 38.495  -19.691 -9.554  1.00 17.00 ? 299  GLU B CD  1 
ATOM   5675 O OE1 . GLU B 1 299 ? 37.441  -19.824 -8.874  1.00 16.66 ? 299  GLU B OE1 1 
ATOM   5676 O OE2 . GLU B 1 299 ? 39.045  -20.604 -10.207 1.00 18.28 ? 299  GLU B OE2 1 
ATOM   5677 N N   . LEU B 1 300 ? 37.066  -14.282 -9.156  1.00 16.77 ? 300  LEU B N   1 
ATOM   5678 C CA  . LEU B 1 300 ? 36.216  -13.151 -9.433  1.00 17.28 ? 300  LEU B CA  1 
ATOM   5679 C C   . LEU B 1 300 ? 37.021  -11.954 -9.974  1.00 17.32 ? 300  LEU B C   1 
ATOM   5680 O O   . LEU B 1 300 ? 36.540  -11.272 -10.865 1.00 19.32 ? 300  LEU B O   1 
ATOM   5681 C CB  . LEU B 1 300 ? 35.403  -12.746 -8.211  1.00 17.48 ? 300  LEU B CB  1 
ATOM   5682 C CG  . LEU B 1 300 ? 34.643  -11.450 -8.452  1.00 16.90 ? 300  LEU B CG  1 
ATOM   5683 C CD1 . LEU B 1 300 ? 33.531  -11.709 -9.462  1.00 16.04 ? 300  LEU B CD1 1 
ATOM   5684 C CD2 . LEU B 1 300 ? 34.076  -10.908 -7.132  1.00 14.64 ? 300  LEU B CD2 1 
ATOM   5685 N N   . ILE B 1 301 ? 38.242  -11.725 -9.493  1.00 16.98 ? 301  ILE B N   1 
ATOM   5686 C CA  . ILE B 1 301 ? 39.049  -10.598 -9.958  1.00 17.18 ? 301  ILE B CA  1 
ATOM   5687 C C   . ILE B 1 301 ? 39.413  -10.780 -11.439 1.00 17.54 ? 301  ILE B C   1 
ATOM   5688 O O   . ILE B 1 301 ? 39.199  -9.867  -12.253 1.00 18.52 ? 301  ILE B O   1 
ATOM   5689 C CB  . ILE B 1 301 ? 40.279  -10.330 -9.036  1.00 17.04 ? 301  ILE B CB  1 
ATOM   5690 C CG1 . ILE B 1 301 ? 39.872  -9.564  -7.788  1.00 16.23 ? 301  ILE B CG1 1 
ATOM   5691 C CG2 . ILE B 1 301 ? 41.426  -9.602  -9.760  1.00 16.47 ? 301  ILE B CG2 1 
ATOM   5692 C CD1 . ILE B 1 301 ? 40.913  -9.702  -6.649  1.00 18.68 ? 301  ILE B CD1 1 
ATOM   5693 N N   . ALA B 1 302 ? 39.914  -11.963 -11.784 1.00 17.71 ? 302  ALA B N   1 
ATOM   5694 C CA  . ALA B 1 302 ? 40.119  -12.369 -13.185 1.00 17.82 ? 302  ALA B CA  1 
ATOM   5695 C C   . ALA B 1 302 ? 38.931  -12.036 -14.105 1.00 18.18 ? 302  ALA B C   1 
ATOM   5696 O O   . ALA B 1 302 ? 39.100  -11.431 -15.169 1.00 17.93 ? 302  ALA B O   1 
ATOM   5697 C CB  . ALA B 1 302 ? 40.432  -13.842 -13.249 1.00 17.24 ? 302  ALA B CB  1 
ATOM   5698 N N   . ARG B 1 303 ? 37.737  -12.434 -13.671 1.00 19.07 ? 303  ARG B N   1 
ATOM   5699 C CA  . ARG B 1 303 ? 36.513  -12.257 -14.436 1.00 18.68 ? 303  ARG B CA  1 
ATOM   5700 C C   . ARG B 1 303 ? 36.132  -10.791 -14.590 1.00 19.62 ? 303  ARG B C   1 
ATOM   5701 O O   . ARG B 1 303 ? 35.671  -10.377 -15.643 1.00 20.38 ? 303  ARG B O   1 
ATOM   5702 C CB  . ARG B 1 303 ? 35.371  -13.044 -13.792 1.00 18.26 ? 303  ARG B CB  1 
ATOM   5703 C CG  . ARG B 1 303 ? 35.492  -14.500 -14.031 1.00 15.27 ? 303  ARG B CG  1 
ATOM   5704 C CD  . ARG B 1 303 ? 34.560  -15.338 -13.206 1.00 13.44 ? 303  ARG B CD  1 
ATOM   5705 N NE  . ARG B 1 303 ? 34.577  -16.753 -13.673 1.00 12.13 ? 303  ARG B NE  1 
ATOM   5706 C CZ  . ARG B 1 303 ? 33.901  -17.770 -13.110 1.00 14.64 ? 303  ARG B CZ  1 
ATOM   5707 N NH1 . ARG B 1 303 ? 33.127  -17.557 -12.036 1.00 15.61 ? 303  ARG B NH1 1 
ATOM   5708 N NH2 . ARG B 1 303 ? 33.939  -19.011 -13.659 1.00 9.33  ? 303  ARG B NH2 1 
ATOM   5709 N N   . LEU B 1 304 ? 36.315  -9.996  -13.545 1.00 20.59 ? 304  LEU B N   1 
ATOM   5710 C CA  . LEU B 1 304 ? 35.938  -8.587  -13.609 1.00 19.99 ? 304  LEU B CA  1 
ATOM   5711 C C   . LEU B 1 304 ? 36.917  -7.829  -14.467 1.00 20.73 ? 304  LEU B C   1 
ATOM   5712 O O   . LEU B 1 304 ? 36.540  -6.812  -15.074 1.00 20.85 ? 304  LEU B O   1 
ATOM   5713 C CB  . LEU B 1 304 ? 35.947  -7.954  -12.228 1.00 19.57 ? 304  LEU B CB  1 
ATOM   5714 C CG  . LEU B 1 304 ? 34.952  -8.303  -11.144 1.00 19.86 ? 304  LEU B CG  1 
ATOM   5715 C CD1 . LEU B 1 304 ? 35.314  -7.451  -9.929  1.00 16.61 ? 304  LEU B CD1 1 
ATOM   5716 C CD2 . LEU B 1 304 ? 33.488  -8.078  -11.573 1.00 20.43 ? 304  LEU B CD2 1 
ATOM   5717 N N   . THR B 1 305 ? 38.170  -8.305  -14.481 1.00 21.03 ? 305  THR B N   1 
ATOM   5718 C CA  . THR B 1 305 ? 39.255  -7.659  -15.234 1.00 22.00 ? 305  THR B CA  1 
ATOM   5719 C C   . THR B 1 305 ? 39.588  -8.381  -16.519 1.00 22.54 ? 305  THR B C   1 
ATOM   5720 O O   . THR B 1 305 ? 40.521  -7.970  -17.206 1.00 22.64 ? 305  THR B O   1 
ATOM   5721 C CB  . THR B 1 305 ? 40.601  -7.567  -14.431 1.00 21.65 ? 305  THR B CB  1 
ATOM   5722 O OG1 . THR B 1 305 ? 40.913  -8.856  -13.910 1.00 21.97 ? 305  THR B OG1 1 
ATOM   5723 C CG2 . THR B 1 305 ? 40.517  -6.555  -13.271 1.00 21.33 ? 305  THR B CG2 1 
ATOM   5724 N N   . HIS B 1 306 ? 38.866  -9.469  -16.830 1.00 23.34 ? 306  HIS B N   1 
ATOM   5725 C CA  . HIS B 1 306 ? 39.086  -10.217 -18.077 1.00 23.41 ? 306  HIS B CA  1 
ATOM   5726 C C   . HIS B 1 306 ? 40.550  -10.461 -18.296 1.00 24.19 ? 306  HIS B C   1 
ATOM   5727 O O   . HIS B 1 306 ? 41.017  -10.314 -19.442 1.00 23.45 ? 306  HIS B O   1 
ATOM   5728 C CB  . HIS B 1 306 ? 38.579  -9.424  -19.274 1.00 23.30 ? 306  HIS B CB  1 
ATOM   5729 C CG  . HIS B 1 306 ? 37.293  -8.728  -19.014 1.00 24.70 ? 306  HIS B CG  1 
ATOM   5730 N ND1 . HIS B 1 306 ? 36.092  -9.404  -18.912 1.00 25.44 ? 306  HIS B ND1 1 
ATOM   5731 C CD2 . HIS B 1 306 ? 37.019  -7.418  -18.787 1.00 25.62 ? 306  HIS B CD2 1 
ATOM   5732 C CE1 . HIS B 1 306 ? 35.129  -8.532  -18.648 1.00 26.55 ? 306  HIS B CE1 1 
ATOM   5733 N NE2 . HIS B 1 306 ? 35.663  -7.321  -18.566 1.00 25.47 ? 306  HIS B NE2 1 
ATOM   5734 N N   . SER B 1 307 ? 41.256  -10.804 -17.201 1.00 24.64 ? 307  SER B N   1 
ATOM   5735 C CA  . SER B 1 307 ? 42.707  -11.106 -17.203 1.00 24.87 ? 307  SER B CA  1 
ATOM   5736 C C   . SER B 1 307 ? 42.911  -12.471 -16.582 1.00 24.83 ? 307  SER B C   1 
ATOM   5737 O O   . SER B 1 307 ? 41.984  -12.992 -16.011 1.00 24.84 ? 307  SER B O   1 
ATOM   5738 C CB  . SER B 1 307 ? 43.470  -10.078 -16.359 1.00 25.08 ? 307  SER B CB  1 
ATOM   5739 O OG  . SER B 1 307 ? 43.210  -8.789  -16.844 1.00 25.01 ? 307  SER B OG  1 
ATOM   5740 N N   . PRO B 1 308 ? 44.116  -13.059 -16.701 1.00 25.20 ? 308  PRO B N   1 
ATOM   5741 C CA  . PRO B 1 308 ? 44.462  -14.326 -16.023 1.00 25.86 ? 308  PRO B CA  1 
ATOM   5742 C C   . PRO B 1 308 ? 44.299  -14.334 -14.486 1.00 26.60 ? 308  PRO B C   1 
ATOM   5743 O O   . PRO B 1 308 ? 44.484  -13.307 -13.836 1.00 26.93 ? 308  PRO B O   1 
ATOM   5744 C CB  . PRO B 1 308 ? 45.947  -14.511 -16.363 1.00 26.02 ? 308  PRO B CB  1 
ATOM   5745 C CG  . PRO B 1 308 ? 46.111  -13.800 -17.727 1.00 26.53 ? 308  PRO B CG  1 
ATOM   5746 C CD  . PRO B 1 308 ? 45.087  -12.695 -17.755 1.00 25.23 ? 308  PRO B CD  1 
ATOM   5747 N N   . VAL B 1 309 ? 43.974  -15.494 -13.919 1.00 27.11 ? 309  VAL B N   1 
ATOM   5748 C CA  . VAL B 1 309 ? 43.871  -15.676 -12.478 1.00 27.34 ? 309  VAL B CA  1 
ATOM   5749 C C   . VAL B 1 309 ? 45.270  -15.510 -11.902 1.00 28.28 ? 309  VAL B C   1 
ATOM   5750 O O   . VAL B 1 309 ? 46.233  -16.054 -12.429 1.00 28.70 ? 309  VAL B O   1 
ATOM   5751 C CB  . VAL B 1 309 ? 43.337  -17.088 -12.128 1.00 27.26 ? 309  VAL B CB  1 
ATOM   5752 C CG1 . VAL B 1 309 ? 42.976  -17.206 -10.667 1.00 25.18 ? 309  VAL B CG1 1 
ATOM   5753 C CG2 . VAL B 1 309 ? 42.130  -17.381 -12.966 1.00 26.76 ? 309  VAL B CG2 1 
ATOM   5754 N N   . HIS B 1 310 ? 45.378  -14.713 -10.847 1.00 28.97 ? 310  HIS B N   1 
ATOM   5755 C CA  . HIS B 1 310 ? 46.582  -14.704 -10.038 1.00 29.80 ? 310  HIS B CA  1 
ATOM   5756 C C   . HIS B 1 310 ? 46.235  -15.205 -8.640  1.00 29.21 ? 310  HIS B C   1 
ATOM   5757 O O   . HIS B 1 310 ? 45.599  -14.492 -7.829  1.00 29.35 ? 310  HIS B O   1 
ATOM   5758 C CB  . HIS B 1 310 ? 47.266  -13.344 -10.053 1.00 30.07 ? 310  HIS B CB  1 
ATOM   5759 C CG  . HIS B 1 310 ? 47.517  -12.852 -11.434 1.00 34.98 ? 310  HIS B CG  1 
ATOM   5760 N ND1 . HIS B 1 310 ? 46.828  -11.786 -11.984 1.00 37.97 ? 310  HIS B ND1 1 
ATOM   5761 C CD2 . HIS B 1 310 ? 48.329  -13.331 -12.413 1.00 37.56 ? 310  HIS B CD2 1 
ATOM   5762 C CE1 . HIS B 1 310 ? 47.229  -11.613 -13.237 1.00 39.44 ? 310  HIS B CE1 1 
ATOM   5763 N NE2 . HIS B 1 310 ? 48.135  -12.539 -13.522 1.00 39.22 ? 310  HIS B NE2 1 
ATOM   5764 N N   . ASP B 1 311 ? 46.639  -16.459 -8.408  1.00 28.47 ? 311  ASP B N   1 
ATOM   5765 C CA  . ASP B 1 311 ? 46.334  -17.193 -7.188  1.00 28.03 ? 311  ASP B CA  1 
ATOM   5766 C C   . ASP B 1 311 ? 47.205  -18.423 -7.003  1.00 27.69 ? 311  ASP B C   1 
ATOM   5767 O O   . ASP B 1 311 ? 47.334  -19.256 -7.900  1.00 28.13 ? 311  ASP B O   1 
ATOM   5768 C CB  . ASP B 1 311 ? 44.877  -17.653 -7.223  1.00 28.00 ? 311  ASP B CB  1 
ATOM   5769 C CG  . ASP B 1 311 ? 44.472  -18.383 -5.969  1.00 27.48 ? 311  ASP B CG  1 
ATOM   5770 O OD1 . ASP B 1 311 ? 44.172  -17.711 -4.964  1.00 28.10 ? 311  ASP B OD1 1 
ATOM   5771 O OD2 . ASP B 1 311 ? 44.470  -19.624 -5.986  1.00 27.33 ? 311  ASP B OD2 1 
ATOM   5772 N N   . ASP B 1 312 ? 47.783  -18.573 -5.826  1.00 27.57 ? 312  ASP B N   1 
ATOM   5773 C CA  A ASP B 1 312 ? 48.459  -19.849 -5.505  0.50 27.54 ? 312  ASP B CA  1 
ATOM   5774 C CA  B ASP B 1 312 ? 48.494  -19.801 -5.496  0.50 26.99 ? 312  ASP B CA  1 
ATOM   5775 C C   . ASP B 1 312 ? 47.951  -20.449 -4.201  1.00 26.80 ? 312  ASP B C   1 
ATOM   5776 O O   . ASP B 1 312 ? 48.661  -21.191 -3.525  1.00 26.70 ? 312  ASP B O   1 
ATOM   5777 C CB  A ASP B 1 312 ? 49.993  -19.758 -5.503  0.50 28.03 ? 312  ASP B CB  1 
ATOM   5778 C CB  B ASP B 1 312 ? 50.004  -19.532 -5.468  0.50 27.01 ? 312  ASP B CB  1 
ATOM   5779 C CG  A ASP B 1 312 ? 50.660  -21.144 -5.376  0.50 31.05 ? 312  ASP B CG  1 
ATOM   5780 C CG  B ASP B 1 312 ? 50.529  -19.031 -6.819  0.50 27.73 ? 312  ASP B CG  1 
ATOM   5781 O OD1 A ASP B 1 312 ? 50.131  -22.117 -5.962  0.50 33.62 ? 312  ASP B OD1 1 
ATOM   5782 O OD1 B ASP B 1 312 ? 50.522  -19.826 -7.784  0.50 29.47 ? 312  ASP B OD1 1 
ATOM   5783 O OD2 A ASP B 1 312 ? 51.694  -21.272 -4.672  0.50 33.93 ? 312  ASP B OD2 1 
ATOM   5784 O OD2 B ASP B 1 312 ? 50.911  -17.842 -6.929  0.50 27.55 ? 312  ASP B OD2 1 
ATOM   5785 N N   . THR B 1 313 ? 46.686  -20.167 -3.877  1.00 25.16 ? 313  THR B N   1 
ATOM   5786 C CA  . THR B 1 313 ? 46.057  -20.780 -2.714  1.00 23.30 ? 313  THR B CA  1 
ATOM   5787 C C   . THR B 1 313 ? 45.181  -22.017 -3.105  1.00 24.27 ? 313  THR B C   1 
ATOM   5788 O O   . THR B 1 313 ? 45.682  -23.167 -3.167  1.00 23.34 ? 313  THR B O   1 
ATOM   5789 C CB  . THR B 1 313 ? 45.227  -19.763 -1.945  1.00 22.82 ? 313  THR B CB  1 
ATOM   5790 O OG1 . THR B 1 313 ? 43.990  -19.541 -2.626  1.00 17.46 ? 313  THR B OG1 1 
ATOM   5791 C CG2 . THR B 1 313 ? 46.006  -18.448 -1.775  1.00 21.39 ? 313  THR B CG2 1 
ATOM   5792 N N   . SER B 1 314 ? 43.896  -21.764 -3.407  1.00 24.15 ? 314  SER B N   1 
ATOM   5793 C CA  . SER B 1 314 ? 42.916  -22.839 -3.569  1.00 23.99 ? 314  SER B CA  1 
ATOM   5794 C C   . SER B 1 314 ? 42.538  -23.153 -4.993  1.00 24.25 ? 314  SER B C   1 
ATOM   5795 O O   . SER B 1 314 ? 41.802  -24.125 -5.208  1.00 24.80 ? 314  SER B O   1 
ATOM   5796 C CB  . SER B 1 314 ? 41.642  -22.544 -2.785  1.00 23.41 ? 314  SER B CB  1 
ATOM   5797 O OG  . SER B 1 314 ? 40.984  -21.442 -3.351  1.00 22.74 ? 314  SER B OG  1 
ATOM   5798 N N   . SER B 1 315 ? 43.004  -22.359 -5.954  1.00 24.23 ? 315  SER B N   1 
ATOM   5799 C CA  . SER B 1 315 ? 42.650  -22.595 -7.360  1.00 25.08 ? 315  SER B CA  1 
ATOM   5800 C C   . SER B 1 315 ? 43.421  -23.722 -8.060  1.00 26.08 ? 315  SER B C   1 
ATOM   5801 O O   . SER B 1 315 ? 44.620  -23.952 -7.811  1.00 26.75 ? 315  SER B O   1 
ATOM   5802 C CB  . SER B 1 315 ? 42.791  -21.327 -8.191  1.00 24.50 ? 315  SER B CB  1 
ATOM   5803 O OG  . SER B 1 315 ? 44.156  -20.971 -8.320  1.00 26.89 ? 315  SER B OG  1 
ATOM   5804 N N   . ASN B 1 316 ? 42.731  -24.406 -8.961  1.00 26.65 ? 316  ASN B N   1 
ATOM   5805 C CA  . ASN B 1 316 ? 43.356  -25.366 -9.814  1.00 27.59 ? 316  ASN B CA  1 
ATOM   5806 C C   . ASN B 1 316 ? 43.884  -24.680 -11.090 1.00 28.07 ? 316  ASN B C   1 
ATOM   5807 O O   . ASN B 1 316 ? 43.106  -24.116 -11.871 1.00 28.85 ? 316  ASN B O   1 
ATOM   5808 C CB  . ASN B 1 316 ? 42.349  -26.462 -10.131 1.00 27.77 ? 316  ASN B CB  1 
ATOM   5809 C CG  . ASN B 1 316 ? 42.924  -27.544 -11.044 1.00 29.49 ? 316  ASN B CG  1 
ATOM   5810 O OD1 . ASN B 1 316 ? 43.710  -27.252 -11.945 1.00 29.41 ? 316  ASN B OD1 1 
ATOM   5811 N ND2 . ASN B 1 316 ? 42.522  -28.797 -10.807 1.00 30.69 ? 316  ASN B ND2 1 
ATOM   5812 N N   . HIS B 1 317 ? 45.205  -24.751 -11.308 1.00 28.15 ? 317  HIS B N   1 
ATOM   5813 C CA  . HIS B 1 317 ? 45.890  -24.083 -12.425 1.00 27.66 ? 317  HIS B CA  1 
ATOM   5814 C C   . HIS B 1 317 ? 45.610  -24.674 -13.810 1.00 27.37 ? 317  HIS B C   1 
ATOM   5815 O O   . HIS B 1 317 ? 45.564  -23.955 -14.812 1.00 26.99 ? 317  HIS B O   1 
ATOM   5816 C CB  . HIS B 1 317 ? 47.398  -24.072 -12.177 1.00 28.34 ? 317  HIS B CB  1 
ATOM   5817 C CG  . HIS B 1 317 ? 47.810  -23.132 -11.090 1.00 30.15 ? 317  HIS B CG  1 
ATOM   5818 N ND1 . HIS B 1 317 ? 48.156  -21.822 -11.333 1.00 33.97 ? 317  HIS B ND1 1 
ATOM   5819 C CD2 . HIS B 1 317 ? 47.860  -23.290 -9.746  1.00 33.02 ? 317  HIS B CD2 1 
ATOM   5820 C CE1 . HIS B 1 317 ? 48.434  -21.219 -10.188 1.00 34.07 ? 317  HIS B CE1 1 
ATOM   5821 N NE2 . HIS B 1 317 ? 48.259  -22.089 -9.209  1.00 34.36 ? 317  HIS B NE2 1 
ATOM   5822 N N   . THR B 1 318 ? 45.464  -25.991 -13.864 1.00 26.58 ? 318  THR B N   1 
ATOM   5823 C CA  . THR B 1 318 ? 44.992  -26.643 -15.053 1.00 26.06 ? 318  THR B CA  1 
ATOM   5824 C C   . THR B 1 318 ? 43.612  -26.058 -15.450 1.00 25.87 ? 318  THR B C   1 
ATOM   5825 O O   . THR B 1 318 ? 43.444  -25.547 -16.564 1.00 25.87 ? 318  THR B O   1 
ATOM   5826 C CB  . THR B 1 318 ? 44.826  -28.159 -14.816 1.00 25.92 ? 318  THR B CB  1 
ATOM   5827 O OG1 . THR B 1 318 ? 46.049  -28.720 -14.333 1.00 25.72 ? 318  THR B OG1 1 
ATOM   5828 C CG2 . THR B 1 318 ? 44.412  -28.846 -16.077 1.00 25.30 ? 318  THR B CG2 1 
ATOM   5829 N N   . LEU B 1 319 ? 42.648  -26.166 -14.528 1.00 25.16 ? 319  LEU B N   1 
ATOM   5830 C CA  . LEU B 1 319 ? 41.291  -25.674 -14.710 1.00 24.28 ? 319  LEU B CA  1 
ATOM   5831 C C   . LEU B 1 319 ? 41.233  -24.167 -15.079 1.00 24.66 ? 319  LEU B C   1 
ATOM   5832 O O   . LEU B 1 319 ? 40.494  -23.787 -15.995 1.00 25.16 ? 319  LEU B O   1 
ATOM   5833 C CB  . LEU B 1 319 ? 40.517  -25.951 -13.442 1.00 23.70 ? 319  LEU B CB  1 
ATOM   5834 C CG  . LEU B 1 319 ? 39.331  -26.918 -13.452 1.00 23.69 ? 319  LEU B CG  1 
ATOM   5835 C CD1 . LEU B 1 319 ? 39.480  -28.027 -14.495 1.00 24.83 ? 319  LEU B CD1 1 
ATOM   5836 C CD2 . LEU B 1 319 ? 38.991  -27.462 -12.030 1.00 21.42 ? 319  LEU B CD2 1 
ATOM   5837 N N   . ASP B 1 320 ? 42.047  -23.322 -14.421 1.00 23.95 ? 320  ASP B N   1 
ATOM   5838 C CA  . ASP B 1 320 ? 41.958  -21.887 -14.641 1.00 23.31 ? 320  ASP B CA  1 
ATOM   5839 C C   . ASP B 1 320 ? 42.770  -21.283 -15.779 1.00 23.82 ? 320  ASP B C   1 
ATOM   5840 O O   . ASP B 1 320 ? 42.465  -20.164 -16.194 1.00 23.54 ? 320  ASP B O   1 
ATOM   5841 C CB  . ASP B 1 320 ? 42.297  -21.121 -13.365 1.00 22.99 ? 320  ASP B CB  1 
ATOM   5842 C CG  . ASP B 1 320 ? 41.209  -21.143 -12.389 1.00 20.31 ? 320  ASP B CG  1 
ATOM   5843 O OD1 . ASP B 1 320 ? 40.281  -21.977 -12.506 1.00 22.47 ? 320  ASP B OD1 1 
ATOM   5844 O OD2 . ASP B 1 320 ? 41.287  -20.337 -11.472 1.00 15.99 ? 320  ASP B OD2 1 
ATOM   5845 N N   . SER B 1 321 ? 43.820  -21.949 -16.253 1.00 24.27 ? 321  SER B N   1 
ATOM   5846 C CA  . SER B 1 321 ? 44.696  -21.272 -17.240 1.00 25.47 ? 321  SER B CA  1 
ATOM   5847 C C   . SER B 1 321 ? 44.247  -21.545 -18.695 1.00 25.87 ? 321  SER B C   1 
ATOM   5848 O O   . SER B 1 321 ? 44.978  -21.283 -19.671 1.00 25.61 ? 321  SER B O   1 
ATOM   5849 C CB  . SER B 1 321 ? 46.186  -21.599 -17.002 1.00 25.49 ? 321  SER B CB  1 
ATOM   5850 O OG  . SER B 1 321 ? 46.423  -22.978 -17.221 1.00 26.88 ? 321  SER B OG  1 
ATOM   5851 N N   . SER B 1 322 ? 43.010  -22.028 -18.818 1.00 26.59 ? 322  SER B N   1 
ATOM   5852 C CA  . SER B 1 322 ? 42.475  -22.550 -20.052 1.00 26.95 ? 322  SER B CA  1 
ATOM   5853 C C   . SER B 1 322 ? 41.078  -21.990 -20.282 1.00 27.11 ? 322  SER B C   1 
ATOM   5854 O O   . SER B 1 322 ? 40.184  -22.248 -19.456 1.00 27.42 ? 322  SER B O   1 
ATOM   5855 C CB  . SER B 1 322 ? 42.433  -24.082 -19.977 1.00 26.88 ? 322  SER B CB  1 
ATOM   5856 O OG  . SER B 1 322 ? 41.305  -24.599 -20.670 1.00 29.22 ? 322  SER B OG  1 
ATOM   5857 N N   . PRO B 1 323 ? 40.863  -21.271 -21.427 1.00 26.70 ? 323  PRO B N   1 
ATOM   5858 C CA  . PRO B 1 323 ? 39.591  -20.602 -21.689 1.00 25.92 ? 323  PRO B CA  1 
ATOM   5859 C C   . PRO B 1 323 ? 38.399  -21.560 -21.624 1.00 25.88 ? 323  PRO B C   1 
ATOM   5860 O O   . PRO B 1 323 ? 37.355  -21.160 -21.132 1.00 26.95 ? 323  PRO B O   1 
ATOM   5861 C CB  . PRO B 1 323 ? 39.762  -20.022 -23.091 1.00 25.89 ? 323  PRO B CB  1 
ATOM   5862 C CG  . PRO B 1 323 ? 41.201  -20.003 -23.337 1.00 27.01 ? 323  PRO B CG  1 
ATOM   5863 C CD  . PRO B 1 323 ? 41.735  -21.218 -22.607 1.00 27.00 ? 323  PRO B CD  1 
ATOM   5864 N N   . ALA B 1 324 ? 38.566  -22.817 -22.053 1.00 25.05 ? 324  ALA B N   1 
ATOM   5865 C CA  . ALA B 1 324 ? 37.513  -23.854 -22.010 1.00 24.08 ? 324  ALA B CA  1 
ATOM   5866 C C   . ALA B 1 324 ? 36.913  -24.070 -20.630 1.00 23.81 ? 324  ALA B C   1 
ATOM   5867 O O   . ALA B 1 324 ? 35.708  -24.274 -20.502 1.00 24.28 ? 324  ALA B O   1 
ATOM   5868 C CB  . ALA B 1 324 ? 38.057  -25.223 -22.527 1.00 23.40 ? 324  ALA B CB  1 
ATOM   5869 N N   . THR B 1 325 ? 37.772  -24.069 -19.608 1.00 23.23 ? 325  THR B N   1 
ATOM   5870 C CA  . THR B 1 325 ? 37.377  -24.400 -18.238 1.00 22.27 ? 325  THR B CA  1 
ATOM   5871 C C   . THR B 1 325 ? 37.417  -23.160 -17.331 1.00 22.28 ? 325  THR B C   1 
ATOM   5872 O O   . THR B 1 325 ? 36.928  -23.185 -16.200 1.00 22.61 ? 325  THR B O   1 
ATOM   5873 C CB  . THR B 1 325 ? 38.245  -25.531 -17.649 1.00 22.02 ? 325  THR B CB  1 
ATOM   5874 O OG1 . THR B 1 325 ? 39.584  -25.421 -18.154 1.00 21.24 ? 325  THR B OG1 1 
ATOM   5875 C CG2 . THR B 1 325 ? 37.707  -26.894 -18.078 1.00 22.27 ? 325  THR B CG2 1 
ATOM   5876 N N   . PHE B 1 326 ? 38.003  -22.083 -17.826 1.00 20.90 ? 326  PHE B N   1 
ATOM   5877 C CA  . PHE B 1 326 ? 37.865  -20.808 -17.154 1.00 20.83 ? 326  PHE B CA  1 
ATOM   5878 C C   . PHE B 1 326 ? 37.807  -19.604 -18.129 1.00 20.60 ? 326  PHE B C   1 
ATOM   5879 O O   . PHE B 1 326 ? 38.790  -18.856 -18.227 1.00 20.95 ? 326  PHE B O   1 
ATOM   5880 C CB  . PHE B 1 326 ? 38.970  -20.614 -16.102 1.00 19.71 ? 326  PHE B CB  1 
ATOM   5881 C CG  . PHE B 1 326 ? 38.698  -19.470 -15.152 1.00 20.33 ? 326  PHE B CG  1 
ATOM   5882 C CD1 . PHE B 1 326 ? 37.899  -19.651 -14.024 1.00 19.57 ? 326  PHE B CD1 1 
ATOM   5883 C CD2 . PHE B 1 326 ? 39.205  -18.203 -15.402 1.00 19.34 ? 326  PHE B CD2 1 
ATOM   5884 C CE1 . PHE B 1 326 ? 37.650  -18.586 -13.160 1.00 18.38 ? 326  PHE B CE1 1 
ATOM   5885 C CE2 . PHE B 1 326 ? 38.942  -17.131 -14.543 1.00 19.56 ? 326  PHE B CE2 1 
ATOM   5886 C CZ  . PHE B 1 326 ? 38.161  -17.321 -13.435 1.00 19.78 ? 326  PHE B CZ  1 
ATOM   5887 N N   . PRO B 1 327 ? 36.657  -19.394 -18.824 1.00 19.84 ? 327  PRO B N   1 
ATOM   5888 C CA  . PRO B 1 327 ? 36.636  -18.313 -19.825 1.00 20.10 ? 327  PRO B CA  1 
ATOM   5889 C C   . PRO B 1 327 ? 36.506  -16.938 -19.165 1.00 19.77 ? 327  PRO B C   1 
ATOM   5890 O O   . PRO B 1 327 ? 35.812  -16.828 -18.161 1.00 19.58 ? 327  PRO B O   1 
ATOM   5891 C CB  . PRO B 1 327 ? 35.406  -18.650 -20.693 1.00 19.67 ? 327  PRO B CB  1 
ATOM   5892 C CG  . PRO B 1 327 ? 34.502  -19.381 -19.790 1.00 19.40 ? 327  PRO B CG  1 
ATOM   5893 C CD  . PRO B 1 327 ? 35.371  -20.112 -18.781 1.00 19.85 ? 327  PRO B CD  1 
ATOM   5894 N N   . LEU B 1 328 ? 37.179  -15.924 -19.709 1.00 19.88 ? 328  LEU B N   1 
ATOM   5895 C CA  . LEU B 1 328 ? 37.290  -14.597 -19.054 1.00 20.60 ? 328  LEU B CA  1 
ATOM   5896 C C   . LEU B 1 328 ? 36.331  -13.544 -19.568 1.00 20.93 ? 328  LEU B C   1 
ATOM   5897 O O   . LEU B 1 328 ? 36.307  -12.422 -19.076 1.00 21.25 ? 328  LEU B O   1 
ATOM   5898 C CB  . LEU B 1 328 ? 38.710  -14.056 -19.220 1.00 19.99 ? 328  LEU B CB  1 
ATOM   5899 C CG  . LEU B 1 328 ? 39.813  -15.010 -18.782 1.00 22.21 ? 328  LEU B CG  1 
ATOM   5900 C CD1 . LEU B 1 328 ? 41.175  -14.577 -19.315 1.00 20.32 ? 328  LEU B CD1 1 
ATOM   5901 C CD2 . LEU B 1 328 ? 39.777  -15.056 -17.254 1.00 21.21 ? 328  LEU B CD2 1 
ATOM   5902 N N   . ASN B 1 329 ? 35.568  -13.887 -20.591 1.00 22.00 ? 329  ASN B N   1 
ATOM   5903 C CA  . ASN B 1 329 ? 34.800  -12.887 -21.318 1.00 23.40 ? 329  ASN B CA  1 
ATOM   5904 C C   . ASN B 1 329 ? 33.403  -13.330 -21.550 1.00 22.85 ? 329  ASN B C   1 
ATOM   5905 O O   . ASN B 1 329 ? 32.753  -12.791 -22.455 1.00 23.12 ? 329  ASN B O   1 
ATOM   5906 C CB  . ASN B 1 329 ? 35.399  -12.611 -22.700 1.00 24.11 ? 329  ASN B CB  1 
ATOM   5907 C CG  . ASN B 1 329 ? 36.640  -11.771 -22.629 1.00 28.35 ? 329  ASN B CG  1 
ATOM   5908 O OD1 . ASN B 1 329 ? 36.651  -10.719 -21.980 1.00 33.12 ? 329  ASN B OD1 1 
ATOM   5909 N ND2 . ASN B 1 329 ? 37.715  -12.235 -23.292 1.00 31.21 ? 329  ASN B ND2 1 
ATOM   5910 N N   . SER B 1 330 ? 32.941  -14.312 -20.772 1.00 22.16 ? 330  SER B N   1 
ATOM   5911 C CA  . SER B 1 330 ? 31.545  -14.684 -20.812 1.00 21.70 ? 330  SER B CA  1 
ATOM   5912 C C   . SER B 1 330 ? 30.997  -13.441 -20.135 1.00 22.34 ? 330  SER B C   1 
ATOM   5913 O O   . SER B 1 330 ? 31.782  -12.487 -19.768 1.00 23.47 ? 330  SER B O   1 
ATOM   5914 C CB  . SER B 1 330 ? 31.270  -15.933 -19.966 1.00 21.86 ? 330  SER B CB  1 
ATOM   5915 O OG  . SER B 1 330 ? 32.251  -16.931 -20.215 1.00 20.50 ? 330  SER B OG  1 
ATOM   5916 N N   . THR B 1 331 ? 29.695  -13.392 -19.960 1.00 20.48 ? 331  THR B N   1 
ATOM   5917 C CA  . THR B 1 331 ? 29.169  -12.164 -19.381 1.00 19.71 ? 331  THR B CA  1 
ATOM   5918 C C   . THR B 1 331 ? 28.405  -12.520 -18.135 1.00 18.84 ? 331  THR B C   1 
ATOM   5919 O O   . THR B 1 331 ? 28.269  -11.684 -17.201 1.00 18.66 ? 331  THR B O   1 
ATOM   5920 C CB  . THR B 1 331 ? 28.301  -11.459 -20.434 1.00 20.02 ? 331  THR B CB  1 
ATOM   5921 O OG1 . THR B 1 331 ? 29.176  -10.741 -21.298 1.00 19.58 ? 331  THR B OG1 1 
ATOM   5922 C CG2 . THR B 1 331 ? 27.273  -10.547 -19.852 1.00 19.11 ? 331  THR B CG2 1 
ATOM   5923 N N   . LEU B 1 332 ? 27.962  -13.780 -18.130 1.00 16.77 ? 332  LEU B N   1 
ATOM   5924 C CA  . LEU B 1 332 ? 27.234  -14.374 -17.031 1.00 16.52 ? 332  LEU B CA  1 
ATOM   5925 C C   . LEU B 1 332 ? 27.907  -15.644 -16.562 1.00 15.71 ? 332  LEU B C   1 
ATOM   5926 O O   . LEU B 1 332 ? 28.385  -16.441 -17.369 1.00 16.23 ? 332  LEU B O   1 
ATOM   5927 C CB  . LEU B 1 332 ? 25.785  -14.699 -17.432 1.00 16.42 ? 332  LEU B CB  1 
ATOM   5928 C CG  . LEU B 1 332 ? 24.986  -13.621 -18.136 1.00 14.43 ? 332  LEU B CG  1 
ATOM   5929 C CD1 . LEU B 1 332 ? 23.919  -14.229 -18.978 1.00 13.75 ? 332  LEU B CD1 1 
ATOM   5930 C CD2 . LEU B 1 332 ? 24.451  -12.694 -17.159 1.00 13.57 ? 332  LEU B CD2 1 
ATOM   5931 N N   . TYR B 1 333 ? 27.884  -15.847 -15.252 1.00 14.92 ? 333  TYR B N   1 
ATOM   5932 C CA  . TYR B 1 333 ? 28.608  -16.926 -14.602 1.00 13.21 ? 333  TYR B CA  1 
ATOM   5933 C C   . TYR B 1 333 ? 27.723  -17.401 -13.456 1.00 14.16 ? 333  TYR B C   1 
ATOM   5934 O O   . TYR B 1 333 ? 27.039  -16.609 -12.805 1.00 13.27 ? 333  TYR B O   1 
ATOM   5935 C CB  . TYR B 1 333 ? 29.900  -16.425 -14.064 1.00 12.70 ? 333  TYR B CB  1 
ATOM   5936 C CG  . TYR B 1 333 ? 30.955  -16.058 -15.095 1.00 12.28 ? 333  TYR B CG  1 
ATOM   5937 C CD1 . TYR B 1 333 ? 31.832  -17.012 -15.601 1.00 11.10 ? 333  TYR B CD1 1 
ATOM   5938 C CD2 . TYR B 1 333 ? 31.099  -14.741 -15.522 1.00 10.96 ? 333  TYR B CD2 1 
ATOM   5939 C CE1 . TYR B 1 333 ? 32.850  -16.654 -16.532 1.00 11.49 ? 333  TYR B CE1 1 
ATOM   5940 C CE2 . TYR B 1 333 ? 32.072  -14.368 -16.434 1.00 10.54 ? 333  TYR B CE2 1 
ATOM   5941 C CZ  . TYR B 1 333 ? 32.949  -15.336 -16.943 1.00 13.35 ? 333  TYR B CZ  1 
ATOM   5942 O OH  . TYR B 1 333 ? 33.902  -14.954 -17.865 1.00 12.77 ? 333  TYR B OH  1 
ATOM   5943 N N   . ALA B 1 334 ? 27.683  -18.717 -13.257 1.00 14.10 ? 334  ALA B N   1 
ATOM   5944 C CA  . ALA B 1 334 ? 26.953  -19.260 -12.157 1.00 14.28 ? 334  ALA B CA  1 
ATOM   5945 C C   . ALA B 1 334 ? 27.843  -20.316 -11.492 1.00 15.40 ? 334  ALA B C   1 
ATOM   5946 O O   . ALA B 1 334 ? 28.469  -21.199 -12.179 1.00 14.35 ? 334  ALA B O   1 
ATOM   5947 C CB  . ALA B 1 334 ? 25.630  -19.827 -12.615 1.00 13.53 ? 334  ALA B CB  1 
ATOM   5948 N N   . ASP B 1 335 ? 27.916  -20.187 -10.153 1.00 15.96 ? 335  ASP B N   1 
ATOM   5949 C CA  . ASP B 1 335 ? 28.637  -21.125 -9.303  1.00 15.70 ? 335  ASP B CA  1 
ATOM   5950 C C   . ASP B 1 335 ? 27.758  -21.674 -8.197  1.00 16.13 ? 335  ASP B C   1 
ATOM   5951 O O   . ASP B 1 335 ? 26.900  -20.968 -7.660  1.00 16.95 ? 335  ASP B O   1 
ATOM   5952 C CB  . ASP B 1 335 ? 29.872  -20.459 -8.743  1.00 15.96 ? 335  ASP B CB  1 
ATOM   5953 C CG  . ASP B 1 335 ? 30.911  -20.153 -9.801  1.00 17.31 ? 335  ASP B CG  1 
ATOM   5954 O OD1 . ASP B 1 335 ? 31.219  -21.055 -10.620 1.00 15.87 ? 335  ASP B OD1 1 
ATOM   5955 O OD2 . ASP B 1 335 ? 31.428  -18.993 -9.802  1.00 18.07 ? 335  ASP B OD2 1 
ATOM   5956 N N   . PHE B 1 336 ? 27.972  -22.944 -7.858  1.00 16.28 ? 336  PHE B N   1 
ATOM   5957 C CA  . PHE B 1 336 ? 27.146  -23.645 -6.872  1.00 16.02 ? 336  PHE B CA  1 
ATOM   5958 C C   . PHE B 1 336 ? 28.008  -24.378 -5.853  1.00 16.50 ? 336  PHE B C   1 
ATOM   5959 O O   . PHE B 1 336 ? 28.888  -25.134 -6.239  1.00 17.69 ? 336  PHE B O   1 
ATOM   5960 C CB  . PHE B 1 336 ? 26.227  -24.656 -7.592  1.00 16.58 ? 336  PHE B CB  1 
ATOM   5961 C CG  . PHE B 1 336 ? 25.192  -24.006 -8.454  1.00 15.25 ? 336  PHE B CG  1 
ATOM   5962 C CD1 . PHE B 1 336 ? 25.502  -23.628 -9.748  1.00 11.31 ? 336  PHE B CD1 1 
ATOM   5963 C CD2 . PHE B 1 336 ? 23.898  -23.744 -7.937  1.00 14.36 ? 336  PHE B CD2 1 
ATOM   5964 C CE1 . PHE B 1 336 ? 24.574  -23.010 -10.530 1.00 13.08 ? 336  PHE B CE1 1 
ATOM   5965 C CE2 . PHE B 1 336 ? 22.950  -23.106 -8.713  1.00 12.32 ? 336  PHE B CE2 1 
ATOM   5966 C CZ  . PHE B 1 336 ? 23.295  -22.735 -10.021 1.00 15.48 ? 336  PHE B CZ  1 
ATOM   5967 N N   . SER B 1 337 ? 27.741  -24.198 -4.560  1.00 16.52 ? 337  SER B N   1 
ATOM   5968 C CA  . SER B 1 337 ? 28.674  -24.639 -3.523  1.00 15.82 ? 337  SER B CA  1 
ATOM   5969 C C   . SER B 1 337 ? 27.934  -24.832 -2.209  1.00 16.00 ? 337  SER B C   1 
ATOM   5970 O O   . SER B 1 337 ? 26.690  -24.854 -2.220  1.00 18.09 ? 337  SER B O   1 
ATOM   5971 C CB  . SER B 1 337 ? 29.768  -23.602 -3.361  1.00 15.36 ? 337  SER B CB  1 
ATOM   5972 O OG  . SER B 1 337 ? 30.851  -24.143 -2.634  1.00 17.87 ? 337  SER B OG  1 
ATOM   5973 N N   . HIS B 1 338 ? 28.666  -24.968 -1.092  1.00 15.59 ? 338  HIS B N   1 
ATOM   5974 C CA  . HIS B 1 338 ? 28.091  -25.081 0.267   1.00 14.33 ? 338  HIS B CA  1 
ATOM   5975 C C   . HIS B 1 338 ? 28.152  -23.807 1.048   1.00 14.65 ? 338  HIS B C   1 
ATOM   5976 O O   . HIS B 1 338 ? 28.976  -22.923 0.756   1.00 14.03 ? 338  HIS B O   1 
ATOM   5977 C CB  . HIS B 1 338 ? 28.849  -26.108 1.120   1.00 14.21 ? 338  HIS B CB  1 
ATOM   5978 C CG  . HIS B 1 338 ? 29.037  -27.433 0.463   1.00 12.59 ? 338  HIS B CG  1 
ATOM   5979 N ND1 . HIS B 1 338 ? 28.187  -28.490 0.681   1.00 10.96 ? 338  HIS B ND1 1 
ATOM   5980 C CD2 . HIS B 1 338 ? 29.990  -27.879 -0.388  1.00 13.98 ? 338  HIS B CD2 1 
ATOM   5981 C CE1 . HIS B 1 338 ? 28.592  -29.530 -0.022  1.00 14.89 ? 338  HIS B CE1 1 
ATOM   5982 N NE2 . HIS B 1 338 ? 29.692  -29.192 -0.674  1.00 16.12 ? 338  HIS B NE2 1 
ATOM   5983 N N   . ASP B 1 339 ? 27.334  -23.760 2.102   1.00 14.90 ? 339  ASP B N   1 
ATOM   5984 C CA  . ASP B 1 339 ? 27.337  -22.670 3.068   1.00 15.85 ? 339  ASP B CA  1 
ATOM   5985 C C   . ASP B 1 339 ? 28.737  -22.284 3.545   1.00 16.18 ? 339  ASP B C   1 
ATOM   5986 O O   . ASP B 1 339 ? 29.132  -21.103 3.500   1.00 17.29 ? 339  ASP B O   1 
ATOM   5987 C CB  . ASP B 1 339 ? 26.424  -22.967 4.286   1.00 15.17 ? 339  ASP B CB  1 
ATOM   5988 C CG  . ASP B 1 339 ? 26.789  -24.247 5.022   1.00 16.04 ? 339  ASP B CG  1 
ATOM   5989 O OD1 . ASP B 1 339 ? 27.829  -24.887 4.738   1.00 15.73 ? 339  ASP B OD1 1 
ATOM   5990 O OD2 . ASP B 1 339 ? 26.014  -24.656 5.901   1.00 17.89 ? 339  ASP B OD2 1 
ATOM   5991 N N   . ASN B 1 340 ? 29.494  -23.274 3.977   1.00 16.17 ? 340  ASN B N   1 
ATOM   5992 C CA  . ASN B 1 340 ? 30.766  -22.975 4.625   1.00 17.26 ? 340  ASN B CA  1 
ATOM   5993 C C   . ASN B 1 340 ? 31.695  -22.235 3.690   1.00 16.89 ? 340  ASN B C   1 
ATOM   5994 O O   . ASN B 1 340 ? 32.314  -21.255 4.097   1.00 16.57 ? 340  ASN B O   1 
ATOM   5995 C CB  . ASN B 1 340 ? 31.429  -24.246 5.209   1.00 16.59 ? 340  ASN B CB  1 
ATOM   5996 C CG  . ASN B 1 340 ? 30.618  -24.843 6.378   1.00 17.64 ? 340  ASN B CG  1 
ATOM   5997 O OD1 . ASN B 1 340 ? 29.852  -24.123 7.074   1.00 15.02 ? 340  ASN B OD1 1 
ATOM   5998 N ND2 . ASN B 1 340 ? 30.788  -26.152 6.607   1.00 15.54 ? 340  ASN B ND2 1 
ATOM   5999 N N   . GLY B 1 341 ? 31.782  -22.686 2.441   1.00 16.16 ? 341  GLY B N   1 
ATOM   6000 C CA  . GLY B 1 341 ? 32.703  -22.045 1.498   1.00 16.33 ? 341  GLY B CA  1 
ATOM   6001 C C   . GLY B 1 341 ? 32.195  -20.667 1.126   1.00 16.64 ? 341  GLY B C   1 
ATOM   6002 O O   . GLY B 1 341 ? 32.966  -19.790 0.755   1.00 16.79 ? 341  GLY B O   1 
ATOM   6003 N N   . ILE B 1 342 ? 30.885  -20.470 1.238   1.00 16.70 ? 342  ILE B N   1 
ATOM   6004 C CA  . ILE B 1 342 ? 30.250  -19.224 0.805   1.00 16.64 ? 342  ILE B CA  1 
ATOM   6005 C C   . ILE B 1 342 ? 30.484  -18.183 1.884   1.00 17.33 ? 342  ILE B C   1 
ATOM   6006 O O   . ILE B 1 342 ? 30.668  -17.010 1.575   1.00 17.74 ? 342  ILE B O   1 
ATOM   6007 C CB  . ILE B 1 342 ? 28.703  -19.416 0.528   1.00 17.07 ? 342  ILE B CB  1 
ATOM   6008 C CG1 . ILE B 1 342 ? 28.484  -20.183 -0.776  1.00 15.39 ? 342  ILE B CG1 1 
ATOM   6009 C CG2 . ILE B 1 342 ? 28.013  -18.121 0.399   1.00 14.33 ? 342  ILE B CG2 1 
ATOM   6010 C CD1 . ILE B 1 342 ? 27.090  -20.743 -0.901  1.00 17.21 ? 342  ILE B CD1 1 
ATOM   6011 N N   . ILE B 1 343 ? 30.467  -18.620 3.154   1.00 17.17 ? 343  ILE B N   1 
ATOM   6012 C CA  . ILE B 1 343 ? 30.805  -17.745 4.265   1.00 15.78 ? 343  ILE B CA  1 
ATOM   6013 C C   . ILE B 1 343 ? 32.208  -17.219 4.002   1.00 15.42 ? 343  ILE B C   1 
ATOM   6014 O O   . ILE B 1 343 ? 32.394  -16.006 3.903   1.00 16.15 ? 343  ILE B O   1 
ATOM   6015 C CB  . ILE B 1 343 ? 30.731  -18.475 5.639   1.00 15.69 ? 343  ILE B CB  1 
ATOM   6016 C CG1 . ILE B 1 343 ? 29.294  -18.815 6.019   1.00 14.36 ? 343  ILE B CG1 1 
ATOM   6017 C CG2 . ILE B 1 343 ? 31.386  -17.648 6.719   1.00 16.01 ? 343  ILE B CG2 1 
ATOM   6018 C CD1 . ILE B 1 343 ? 28.423  -17.623 6.376   1.00 7.87  ? 343  ILE B CD1 1 
ATOM   6019 N N   . SER B 1 344 ? 33.180  -18.122 3.851   1.00 14.78 ? 344  SER B N   1 
ATOM   6020 C CA  . SER B 1 344 ? 34.585  -17.755 3.636   1.00 14.96 ? 344  SER B CA  1 
ATOM   6021 C C   . SER B 1 344 ? 34.730  -16.769 2.495   1.00 15.58 ? 344  SER B C   1 
ATOM   6022 O O   . SER B 1 344 ? 35.490  -15.768 2.609   1.00 16.41 ? 344  SER B O   1 
ATOM   6023 C CB  . SER B 1 344 ? 35.480  -18.980 3.376   1.00 14.17 ? 344  SER B CB  1 
ATOM   6024 O OG  . SER B 1 344 ? 35.433  -19.877 4.472   1.00 15.28 ? 344  SER B OG  1 
ATOM   6025 N N   . ILE B 1 345 ? 33.983  -17.026 1.417   1.00 15.17 ? 345  ILE B N   1 
ATOM   6026 C CA  . ILE B 1 345 ? 34.028  -16.161 0.230   1.00 15.45 ? 345  ILE B CA  1 
ATOM   6027 C C   . ILE B 1 345 ? 33.508  -14.724 0.475   1.00 14.75 ? 345  ILE B C   1 
ATOM   6028 O O   . ILE B 1 345 ? 34.158  -13.738 0.090   1.00 13.75 ? 345  ILE B O   1 
ATOM   6029 C CB  . ILE B 1 345 ? 33.317  -16.834 -0.987  1.00 15.40 ? 345  ILE B CB  1 
ATOM   6030 C CG1 . ILE B 1 345 ? 34.102  -18.072 -1.436  1.00 14.40 ? 345  ILE B CG1 1 
ATOM   6031 C CG2 . ILE B 1 345 ? 33.151  -15.820 -2.129  1.00 14.05 ? 345  ILE B CG2 1 
ATOM   6032 C CD1 . ILE B 1 345 ? 33.391  -18.884 -2.532  1.00 14.53 ? 345  ILE B CD1 1 
ATOM   6033 N N   . LEU B 1 346 ? 32.327  -14.631 1.087   1.00 14.96 ? 346  LEU B N   1 
ATOM   6034 C CA  . LEU B 1 346 ? 31.743  -13.370 1.501   1.00 15.34 ? 346  LEU B CA  1 
ATOM   6035 C C   . LEU B 1 346 ? 32.740  -12.489 2.311   1.00 16.28 ? 346  LEU B C   1 
ATOM   6036 O O   . LEU B 1 346 ? 32.978  -11.300 1.961   1.00 17.08 ? 346  LEU B O   1 
ATOM   6037 C CB  . LEU B 1 346 ? 30.476  -13.627 2.313   1.00 15.79 ? 346  LEU B CB  1 
ATOM   6038 C CG  . LEU B 1 346 ? 29.293  -14.314 1.652   1.00 15.91 ? 346  LEU B CG  1 
ATOM   6039 C CD1 . LEU B 1 346 ? 28.080  -14.348 2.592   1.00 17.49 ? 346  LEU B CD1 1 
ATOM   6040 C CD2 . LEU B 1 346 ? 28.954  -13.599 0.396   1.00 16.44 ? 346  LEU B CD2 1 
ATOM   6041 N N   . PHE B 1 347 ? 33.335  -13.060 3.364   1.00 15.70 ? 347  PHE B N   1 
ATOM   6042 C CA  . PHE B 1 347 ? 34.354  -12.354 4.167   1.00 15.89 ? 347  PHE B CA  1 
ATOM   6043 C C   . PHE B 1 347 ? 35.653  -12.010 3.412   1.00 16.10 ? 347  PHE B C   1 
ATOM   6044 O O   . PHE B 1 347 ? 36.162  -10.919 3.595   1.00 17.29 ? 347  PHE B O   1 
ATOM   6045 C CB  . PHE B 1 347 ? 34.674  -13.111 5.467   1.00 15.07 ? 347  PHE B CB  1 
ATOM   6046 C CG  . PHE B 1 347 ? 33.638  -12.942 6.524   1.00 14.38 ? 347  PHE B CG  1 
ATOM   6047 C CD1 . PHE B 1 347 ? 33.715  -11.877 7.423   1.00 11.77 ? 347  PHE B CD1 1 
ATOM   6048 C CD2 . PHE B 1 347 ? 32.578  -13.855 6.647   1.00 10.18 ? 347  PHE B CD2 1 
ATOM   6049 C CE1 . PHE B 1 347 ? 32.701  -11.712 8.424   1.00 11.84 ? 347  PHE B CE1 1 
ATOM   6050 C CE2 . PHE B 1 347 ? 31.583  -13.698 7.643   1.00 10.93 ? 347  PHE B CE2 1 
ATOM   6051 C CZ  . PHE B 1 347 ? 31.652  -12.640 8.518   1.00 10.08 ? 347  PHE B CZ  1 
ATOM   6052 N N   . ALA B 1 348 ? 36.182  -12.893 2.570   1.00 16.10 ? 348  ALA B N   1 
ATOM   6053 C CA  . ALA B 1 348 ? 37.394  -12.540 1.766   1.00 16.27 ? 348  ALA B CA  1 
ATOM   6054 C C   . ALA B 1 348 ? 37.129  -11.409 0.757   1.00 16.50 ? 348  ALA B C   1 
ATOM   6055 O O   . ALA B 1 348 ? 38.064  -10.719 0.286   1.00 16.39 ? 348  ALA B O   1 
ATOM   6056 C CB  . ALA B 1 348 ? 37.925  -13.726 1.053   1.00 15.79 ? 348  ALA B CB  1 
ATOM   6057 N N   . LEU B 1 349 ? 35.863  -11.208 0.418   1.00 15.96 ? 349  LEU B N   1 
ATOM   6058 C CA  . LEU B 1 349 ? 35.527  -10.153 -0.538  1.00 16.06 ? 349  LEU B CA  1 
ATOM   6059 C C   . LEU B 1 349 ? 35.311  -8.841  0.197   1.00 16.47 ? 349  LEU B C   1 
ATOM   6060 O O   . LEU B 1 349 ? 34.998  -7.843  -0.425  1.00 16.75 ? 349  LEU B O   1 
ATOM   6061 C CB  . LEU B 1 349 ? 34.289  -10.507 -1.371  1.00 15.36 ? 349  LEU B CB  1 
ATOM   6062 C CG  . LEU B 1 349 ? 34.427  -11.692 -2.337  1.00 16.73 ? 349  LEU B CG  1 
ATOM   6063 C CD1 . LEU B 1 349 ? 33.065  -12.154 -2.884  1.00 14.35 ? 349  LEU B CD1 1 
ATOM   6064 C CD2 . LEU B 1 349 ? 35.419  -11.364 -3.463  1.00 16.12 ? 349  LEU B CD2 1 
ATOM   6065 N N   . GLY B 1 350 ? 35.435  -8.883  1.528   1.00 16.78 ? 350  GLY B N   1 
ATOM   6066 C CA  . GLY B 1 350 ? 35.297  -7.729  2.375   1.00 16.83 ? 350  GLY B CA  1 
ATOM   6067 C C   . GLY B 1 350 ? 33.879  -7.371  2.746   1.00 17.58 ? 350  GLY B C   1 
ATOM   6068 O O   . GLY B 1 350 ? 33.661  -6.412  3.452   1.00 18.27 ? 350  GLY B O   1 
ATOM   6069 N N   . LEU B 1 351 ? 32.907  -8.132  2.267   1.00 18.40 ? 351  LEU B N   1 
ATOM   6070 C CA  . LEU B 1 351 ? 31.493  -7.784  2.445   1.00 18.82 ? 351  LEU B CA  1 
ATOM   6071 C C   . LEU B 1 351 ? 31.069  -7.585  3.863   1.00 19.00 ? 351  LEU B C   1 
ATOM   6072 O O   . LEU B 1 351 ? 30.019  -6.993  4.121   1.00 20.80 ? 351  LEU B O   1 
ATOM   6073 C CB  . LEU B 1 351 ? 30.581  -8.810  1.768   1.00 19.05 ? 351  LEU B CB  1 
ATOM   6074 C CG  . LEU B 1 351 ? 30.959  -9.060  0.295   1.00 21.24 ? 351  LEU B CG  1 
ATOM   6075 C CD1 . LEU B 1 351 ? 30.045  -10.094 -0.299  1.00 19.99 ? 351  LEU B CD1 1 
ATOM   6076 C CD2 . LEU B 1 351 ? 30.943  -7.729  -0.507  1.00 20.51 ? 351  LEU B CD2 1 
ATOM   6077 N N   . TYR B 1 352 ? 31.850  -8.065  4.813   1.00 18.81 ? 352  TYR B N   1 
ATOM   6078 C CA  . TYR B 1 352 ? 31.435  -7.887  6.202   1.00 18.90 ? 352  TYR B CA  1 
ATOM   6079 C C   . TYR B 1 352 ? 32.461  -7.131  7.076   1.00 19.59 ? 352  TYR B C   1 
ATOM   6080 O O   . TYR B 1 352 ? 32.587  -7.348  8.284   1.00 19.36 ? 352  TYR B O   1 
ATOM   6081 C CB  . TYR B 1 352 ? 30.872  -9.189  6.775   1.00 17.91 ? 352  TYR B CB  1 
ATOM   6082 C CG  . TYR B 1 352 ? 29.540  -9.515  6.099   1.00 17.28 ? 352  TYR B CG  1 
ATOM   6083 C CD1 . TYR B 1 352 ? 28.323  -8.909  6.534   1.00 15.28 ? 352  TYR B CD1 1 
ATOM   6084 C CD2 . TYR B 1 352 ? 29.498  -10.405 5.006   1.00 12.53 ? 352  TYR B CD2 1 
ATOM   6085 C CE1 . TYR B 1 352 ? 27.096  -9.186  5.874   1.00 13.40 ? 352  TYR B CE1 1 
ATOM   6086 C CE2 . TYR B 1 352 ? 28.330  -10.687 4.350   1.00 13.88 ? 352  TYR B CE2 1 
ATOM   6087 C CZ  . TYR B 1 352 ? 27.119  -10.101 4.772   1.00 15.51 ? 352  TYR B CZ  1 
ATOM   6088 O OH  . TYR B 1 352 ? 25.982  -10.440 4.070   1.00 16.66 ? 352  TYR B OH  1 
ATOM   6089 N N   . ASN B 1 353 ? 33.128  -6.174  6.439   1.00 19.93 ? 353  ASN B N   1 
ATOM   6090 C CA  . ASN B 1 353 ? 34.213  -5.452  7.083   1.00 21.67 ? 353  ASN B CA  1 
ATOM   6091 C C   . ASN B 1 353 ? 33.751  -4.219  7.878   1.00 22.45 ? 353  ASN B C   1 
ATOM   6092 O O   . ASN B 1 353 ? 34.559  -3.363  8.230   1.00 22.39 ? 353  ASN B O   1 
ATOM   6093 C CB  . ASN B 1 353 ? 35.297  -5.091  6.061   1.00 21.43 ? 353  ASN B CB  1 
ATOM   6094 C CG  . ASN B 1 353 ? 36.366  -6.106  6.005   1.00 21.58 ? 353  ASN B CG  1 
ATOM   6095 O OD1 . ASN B 1 353 ? 36.158  -7.268  6.393   1.00 20.94 ? 353  ASN B OD1 1 
ATOM   6096 N ND2 . ASN B 1 353 ? 37.538  -5.692  5.549   1.00 20.62 ? 353  ASN B ND2 1 
ATOM   6097 N N   . GLY B 1 354 ? 32.451  -4.138  8.157   1.00 23.53 ? 354  GLY B N   1 
ATOM   6098 C CA  . GLY B 1 354 ? 31.921  -3.147  9.116   1.00 24.39 ? 354  GLY B CA  1 
ATOM   6099 C C   . GLY B 1 354 ? 31.239  -3.874  10.263  1.00 25.21 ? 354  GLY B C   1 
ATOM   6100 O O   . GLY B 1 354 ? 30.557  -3.251  11.047  1.00 25.58 ? 354  GLY B O   1 
ATOM   6101 N N   . THR B 1 355 ? 31.437  -5.199  10.331  1.00 25.73 ? 355  THR B N   1 
ATOM   6102 C CA  . THR B 1 355 ? 30.863  -6.103  11.342  1.00 25.78 ? 355  THR B CA  1 
ATOM   6103 C C   . THR B 1 355 ? 31.892  -6.431  12.469  1.00 26.80 ? 355  THR B C   1 
ATOM   6104 O O   . THR B 1 355 ? 32.995  -6.937  12.197  1.00 26.49 ? 355  THR B O   1 
ATOM   6105 C CB  . THR B 1 355 ? 30.384  -7.460  10.698  1.00 25.74 ? 355  THR B CB  1 
ATOM   6106 O OG1 . THR B 1 355 ? 29.224  -7.258  9.883   1.00 24.01 ? 355  THR B OG1 1 
ATOM   6107 C CG2 . THR B 1 355 ? 30.096  -8.551  11.769  1.00 23.96 ? 355  THR B CG2 1 
ATOM   6108 N N   . LYS B 1 356 ? 31.493  -6.182  13.728  1.00 27.16 ? 356  LYS B N   1 
ATOM   6109 C CA  . LYS B 1 356 ? 32.324  -6.468  14.897  1.00 27.49 ? 356  LYS B CA  1 
ATOM   6110 C C   . LYS B 1 356 ? 32.202  -7.918  15.368  1.00 26.90 ? 356  LYS B C   1 
ATOM   6111 O O   . LYS B 1 356 ? 31.097  -8.423  15.496  1.00 27.97 ? 356  LYS B O   1 
ATOM   6112 C CB  . LYS B 1 356 ? 32.024  -5.477  16.018  1.00 27.50 ? 356  LYS B CB  1 
ATOM   6113 C CG  . LYS B 1 356 ? 33.057  -4.349  16.043  1.00 30.72 ? 356  LYS B CG  1 
ATOM   6114 C CD  . LYS B 1 356 ? 32.445  -2.948  16.139  1.00 36.19 ? 356  LYS B CD  1 
ATOM   6115 C CE  . LYS B 1 356 ? 33.526  -1.884  15.752  1.00 42.36 ? 356  LYS B CE  1 
ATOM   6116 N NZ  . LYS B 1 356 ? 33.213  -0.393  15.939  1.00 44.84 ? 356  LYS B NZ  1 
ATOM   6117 N N   . PRO B 1 357 ? 33.338  -8.577  15.657  1.00 26.14 ? 357  PRO B N   1 
ATOM   6118 C CA  . PRO B 1 357 ? 33.356  -9.982  16.037  1.00 25.99 ? 357  PRO B CA  1 
ATOM   6119 C C   . PRO B 1 357 ? 32.226  -10.262 16.996  1.00 26.02 ? 357  PRO B C   1 
ATOM   6120 O O   . PRO B 1 357 ? 32.016  -9.505  17.941  1.00 26.57 ? 357  PRO B O   1 
ATOM   6121 C CB  . PRO B 1 357 ? 34.697  -10.128 16.751  1.00 26.45 ? 357  PRO B CB  1 
ATOM   6122 C CG  . PRO B 1 357 ? 35.556  -9.090  16.136  1.00 26.47 ? 357  PRO B CG  1 
ATOM   6123 C CD  . PRO B 1 357 ? 34.646  -7.930  15.858  1.00 26.11 ? 357  PRO B CD  1 
ATOM   6124 N N   . LEU B 1 358 ? 31.475  -11.318 16.755  1.00 25.48 ? 358  LEU B N   1 
ATOM   6125 C CA  . LEU B 1 358 ? 30.244  -11.476 17.475  1.00 25.80 ? 358  LEU B CA  1 
ATOM   6126 C C   . LEU B 1 358 ? 30.584  -11.882 18.881  1.00 27.69 ? 358  LEU B C   1 
ATOM   6127 O O   . LEU B 1 358 ? 31.557  -12.663 19.092  1.00 27.44 ? 358  LEU B O   1 
ATOM   6128 C CB  . LEU B 1 358 ? 29.340  -12.535 16.834  1.00 24.66 ? 358  LEU B CB  1 
ATOM   6129 C CG  . LEU B 1 358 ? 29.081  -12.538 15.326  1.00 24.86 ? 358  LEU B CG  1 
ATOM   6130 C CD1 . LEU B 1 358 ? 27.955  -13.513 14.977  1.00 22.22 ? 358  LEU B CD1 1 
ATOM   6131 C CD2 . LEU B 1 358 ? 28.816  -11.166 14.742  1.00 20.27 ? 358  LEU B CD2 1 
ATOM   6132 N N   . SER B 1 359 ? 29.779  -11.379 19.835  1.00 28.66 ? 359  SER B N   1 
ATOM   6133 C CA  . SER B 1 359 ? 29.939  -11.712 21.256  1.00 29.44 ? 359  SER B CA  1 
ATOM   6134 C C   . SER B 1 359 ? 29.763  -13.194 21.441  1.00 29.87 ? 359  SER B C   1 
ATOM   6135 O O   . SER B 1 359 ? 28.835  -13.775 20.875  1.00 30.35 ? 359  SER B O   1 
ATOM   6136 C CB  . SER B 1 359 ? 28.901  -10.978 22.121  1.00 29.84 ? 359  SER B CB  1 
ATOM   6137 O OG  . SER B 1 359 ? 28.632  -11.720 23.310  1.00 29.46 ? 359  SER B OG  1 
ATOM   6138 N N   . THR B 1 360 ? 30.628  -13.811 22.236  1.00 30.37 ? 360  THR B N   1 
ATOM   6139 C CA  . THR B 1 360 ? 30.484  -15.251 22.504  1.00 31.33 ? 360  THR B CA  1 
ATOM   6140 C C   . THR B 1 360 ? 29.437  -15.591 23.603  1.00 31.76 ? 360  THR B C   1 
ATOM   6141 O O   . THR B 1 360 ? 29.084  -16.736 23.798  1.00 31.21 ? 360  THR B O   1 
ATOM   6142 C CB  . THR B 1 360 ? 31.873  -15.929 22.778  1.00 31.45 ? 360  THR B CB  1 
ATOM   6143 O OG1 . THR B 1 360 ? 32.497  -15.301 23.902  1.00 30.30 ? 360  THR B OG1 1 
ATOM   6144 C CG2 . THR B 1 360 ? 32.806  -15.810 21.554  1.00 30.82 ? 360  THR B CG2 1 
ATOM   6145 N N   . THR B 1 361 ? 28.909  -14.567 24.268  1.00 33.62 ? 361  THR B N   1 
ATOM   6146 C CA  . THR B 1 361 ? 28.121  -14.707 25.520  1.00 34.64 ? 361  THR B CA  1 
ATOM   6147 C C   . THR B 1 361 ? 26.670  -14.167 25.428  1.00 35.24 ? 361  THR B C   1 
ATOM   6148 O O   . THR B 1 361 ? 25.751  -14.680 26.076  1.00 34.98 ? 361  THR B O   1 
ATOM   6149 C CB  . THR B 1 361 ? 28.820  -13.919 26.664  1.00 34.79 ? 361  THR B CB  1 
ATOM   6150 O OG1 . THR B 1 361 ? 28.716  -12.516 26.382  1.00 34.56 ? 361  THR B OG1 1 
ATOM   6151 C CG2 . THR B 1 361 ? 30.322  -14.296 26.809  1.00 34.31 ? 361  THR B CG2 1 
ATOM   6152 N N   . THR B 1 362 ? 26.482  -13.104 24.641  1.00 36.45 ? 362  THR B N   1 
ATOM   6153 C CA  . THR B 1 362 ? 25.168  -12.470 24.446  1.00 37.05 ? 362  THR B CA  1 
ATOM   6154 C C   . THR B 1 362 ? 24.730  -12.430 22.965  1.00 36.59 ? 362  THR B C   1 
ATOM   6155 O O   . THR B 1 362 ? 25.545  -12.147 22.092  1.00 36.48 ? 362  THR B O   1 
ATOM   6156 C CB  . THR B 1 362 ? 25.187  -10.974 24.901  1.00 37.81 ? 362  THR B CB  1 
ATOM   6157 O OG1 . THR B 1 362 ? 26.479  -10.615 25.437  1.00 39.48 ? 362  THR B OG1 1 
ATOM   6158 C CG2 . THR B 1 362 ? 24.042  -10.682 25.910  1.00 38.34 ? 362  THR B CG2 1 
ATOM   6159 N N   . VAL B 1 363 ? 23.439  -12.669 22.714  1.00 35.93 ? 363  VAL B N   1 
ATOM   6160 C CA  . VAL B 1 363 ? 22.767  -12.329 21.453  1.00 35.76 ? 363  VAL B CA  1 
ATOM   6161 C C   . VAL B 1 363 ? 23.048  -10.896 20.916  1.00 35.44 ? 363  VAL B C   1 
ATOM   6162 O O   . VAL B 1 363 ? 22.898  -9.899  21.650  1.00 34.79 ? 363  VAL B O   1 
ATOM   6163 C CB  . VAL B 1 363 ? 21.227  -12.430 21.609  1.00 36.04 ? 363  VAL B CB  1 
ATOM   6164 C CG1 . VAL B 1 363 ? 20.534  -12.078 20.300  1.00 36.80 ? 363  VAL B CG1 1 
ATOM   6165 C CG2 . VAL B 1 363 ? 20.811  -13.808 22.102  1.00 35.81 ? 363  VAL B CG2 1 
ATOM   6166 N N   . GLU B 1 364 ? 23.445  -10.817 19.638  1.00 34.50 ? 364  GLU B N   1 
ATOM   6167 C CA  . GLU B 1 364 ? 23.539  -9.547  18.908  1.00 34.14 ? 364  GLU B CA  1 
ATOM   6168 C C   . GLU B 1 364 ? 22.546  -9.543  17.746  1.00 33.66 ? 364  GLU B C   1 
ATOM   6169 O O   . GLU B 1 364 ? 22.604  -10.438 16.893  1.00 34.38 ? 364  GLU B O   1 
ATOM   6170 C CB  . GLU B 1 364 ? 24.967  -9.303  18.405  1.00 33.26 ? 364  GLU B CB  1 
ATOM   6171 C CG  . GLU B 1 364 ? 25.966  -9.228  19.536  1.00 34.25 ? 364  GLU B CG  1 
ATOM   6172 C CD  . GLU B 1 364 ? 27.396  -8.846  19.123  1.00 35.32 ? 364  GLU B CD  1 
ATOM   6173 O OE1 . GLU B 1 364 ? 28.069  -8.166  19.923  1.00 38.80 ? 364  GLU B OE1 1 
ATOM   6174 O OE2 . GLU B 1 364 ? 27.870  -9.213  18.037  1.00 33.30 ? 364  GLU B OE2 1 
ATOM   6175 N N   . ASN B 1 365 ? 21.649  -8.550  17.717  1.00 32.64 ? 365  ASN B N   1 
ATOM   6176 C CA  . ASN B 1 365 ? 20.664  -8.399  16.639  1.00 31.70 ? 365  ASN B CA  1 
ATOM   6177 C C   . ASN B 1 365 ? 21.290  -8.006  15.298  1.00 31.63 ? 365  ASN B C   1 
ATOM   6178 O O   . ASN B 1 365 ? 22.499  -7.740  15.215  1.00 31.26 ? 365  ASN B O   1 
ATOM   6179 C CB  . ASN B 1 365 ? 19.531  -7.438  17.039  1.00 31.31 ? 365  ASN B CB  1 
ATOM   6180 C CG  . ASN B 1 365 ? 20.004  -6.008  17.269  1.00 31.84 ? 365  ASN B CG  1 
ATOM   6181 O OD1 . ASN B 1 365 ? 20.630  -5.389  16.405  1.00 33.23 ? 365  ASN B OD1 1 
ATOM   6182 N ND2 . ASN B 1 365 ? 19.665  -5.459  18.426  1.00 32.06 ? 365  ASN B ND2 1 
ATOM   6183 N N   . ILE B 1 366 ? 20.465  -7.951  14.249  1.00 31.56 ? 366  ILE B N   1 
ATOM   6184 C CA  . ILE B 1 366 ? 20.996  -7.765  12.898  1.00 30.81 ? 366  ILE B CA  1 
ATOM   6185 C C   . ILE B 1 366 ? 21.626  -6.374  12.675  1.00 30.94 ? 366  ILE B C   1 
ATOM   6186 O O   . ILE B 1 366 ? 22.438  -6.215  11.761  1.00 30.83 ? 366  ILE B O   1 
ATOM   6187 C CB  . ILE B 1 366 ? 19.962  -8.162  11.776  1.00 30.76 ? 366  ILE B CB  1 
ATOM   6188 C CG1 . ILE B 1 366 ? 20.663  -8.343  10.425  1.00 29.97 ? 366  ILE B CG1 1 
ATOM   6189 C CG2 . ILE B 1 366 ? 18.852  -7.129  11.647  1.00 28.35 ? 366  ILE B CG2 1 
ATOM   6190 C CD1 . ILE B 1 366 ? 21.583  -9.558  10.339  1.00 28.55 ? 366  ILE B CD1 1 
ATOM   6191 N N   . THR B 1 367 ? 21.280  -5.395  13.524  1.00 30.87 ? 367  THR B N   1 
ATOM   6192 C CA  . THR B 1 367 ? 21.945  -4.069  13.529  1.00 30.75 ? 367  THR B CA  1 
ATOM   6193 C C   . THR B 1 367 ? 23.330  -4.150  14.143  1.00 30.65 ? 367  THR B C   1 
ATOM   6194 O O   . THR B 1 367 ? 24.327  -3.740  13.543  1.00 31.07 ? 367  THR B O   1 
ATOM   6195 C CB  . THR B 1 367 ? 21.165  -3.042  14.350  1.00 31.06 ? 367  THR B CB  1 
ATOM   6196 O OG1 . THR B 1 367 ? 19.779  -3.122  14.022  1.00 31.62 ? 367  THR B OG1 1 
ATOM   6197 C CG2 . THR B 1 367 ? 21.673  -1.605  14.080  1.00 32.26 ? 367  THR B CG2 1 
ATOM   6198 N N   . GLN B 1 368 ? 23.399  -4.690  15.352  1.00 30.49 ? 368  GLN B N   1 
ATOM   6199 C CA  . GLN B 1 368 ? 24.681  -4.856  16.027  1.00 29.77 ? 368  GLN B CA  1 
ATOM   6200 C C   . GLN B 1 368 ? 25.687  -5.594  15.126  1.00 28.92 ? 368  GLN B C   1 
ATOM   6201 O O   . GLN B 1 368 ? 26.840  -5.173  15.022  1.00 29.02 ? 368  GLN B O   1 
ATOM   6202 C CB  . GLN B 1 368 ? 24.489  -5.555  17.364  1.00 29.94 ? 368  GLN B CB  1 
ATOM   6203 C CG  . GLN B 1 368 ? 23.329  -4.957  18.185  1.00 31.36 ? 368  GLN B CG  1 
ATOM   6204 C CD  . GLN B 1 368 ? 23.110  -5.676  19.485  1.00 32.24 ? 368  GLN B CD  1 
ATOM   6205 O OE1 . GLN B 1 368 ? 22.199  -6.504  19.617  1.00 30.56 ? 368  GLN B OE1 1 
ATOM   6206 N NE2 . GLN B 1 368 ? 23.973  -5.388  20.463  1.00 34.19 ? 368  GLN B NE2 1 
ATOM   6207 N N   . THR B 1 369 ? 25.257  -6.646  14.437  1.00 27.45 ? 369  THR B N   1 
ATOM   6208 C CA  . THR B 1 369 ? 26.192  -7.356  13.530  1.00 26.79 ? 369  THR B CA  1 
ATOM   6209 C C   . THR B 1 369 ? 26.362  -6.714  12.125  1.00 26.22 ? 369  THR B C   1 
ATOM   6210 O O   . THR B 1 369 ? 26.983  -7.327  11.232  1.00 25.82 ? 369  THR B O   1 
ATOM   6211 C CB  . THR B 1 369 ? 25.840  -8.856  13.365  1.00 26.15 ? 369  THR B CB  1 
ATOM   6212 O OG1 . THR B 1 369 ? 24.588  -8.948  12.692  1.00 27.13 ? 369  THR B OG1 1 
ATOM   6213 C CG2 . THR B 1 369 ? 25.739  -9.541  14.681  1.00 24.38 ? 369  THR B CG2 1 
ATOM   6214 N N   . ASP B 1 370 ? 25.801  -5.500  11.935  1.00 26.44 ? 370  ASP B N   1 
ATOM   6215 C CA  . ASP B 1 370 ? 25.851  -4.754  10.654  1.00 25.13 ? 370  ASP B CA  1 
ATOM   6216 C C   . ASP B 1 370 ? 25.438  -5.669  9.477   1.00 24.20 ? 370  ASP B C   1 
ATOM   6217 O O   . ASP B 1 370 ? 26.121  -5.751  8.467   1.00 24.01 ? 370  ASP B O   1 
ATOM   6218 C CB  . ASP B 1 370 ? 27.253  -4.142  10.443  1.00 25.14 ? 370  ASP B CB  1 
ATOM   6219 C CG  . ASP B 1 370 ? 27.310  -3.137  9.288   1.00 27.59 ? 370  ASP B CG  1 
ATOM   6220 O OD1 . ASP B 1 370 ? 26.320  -2.410  9.092   1.00 30.11 ? 370  ASP B OD1 1 
ATOM   6221 O OD2 . ASP B 1 370 ? 28.360  -3.053  8.595   1.00 28.54 ? 370  ASP B OD2 1 
ATOM   6222 N N   . GLY B 1 371 ? 24.327  -6.379  9.638   1.00 22.87 ? 371  GLY B N   1 
ATOM   6223 C CA  . GLY B 1 371 ? 23.800  -7.223  8.567   1.00 21.91 ? 371  GLY B CA  1 
ATOM   6224 C C   . GLY B 1 371 ? 24.319  -8.646  8.422   1.00 20.75 ? 371  GLY B C   1 
ATOM   6225 O O   . GLY B 1 371 ? 23.930  -9.317  7.499   1.00 21.10 ? 371  GLY B O   1 
ATOM   6226 N N   . PHE B 1 372 ? 25.181  -9.115  9.317   1.00 20.13 ? 372  PHE B N   1 
ATOM   6227 C CA  . PHE B 1 372 ? 25.639  -10.507 9.245   1.00 19.02 ? 372  PHE B CA  1 
ATOM   6228 C C   . PHE B 1 372 ? 24.856  -11.490 10.076  1.00 18.64 ? 372  PHE B C   1 
ATOM   6229 O O   . PHE B 1 372 ? 24.641  -11.273 11.255  1.00 18.65 ? 372  PHE B O   1 
ATOM   6230 C CB  . PHE B 1 372 ? 27.112  -10.706 9.617   1.00 19.11 ? 372  PHE B CB  1 
ATOM   6231 C CG  . PHE B 1 372 ? 27.495  -12.152 9.598   1.00 18.18 ? 372  PHE B CG  1 
ATOM   6232 C CD1 . PHE B 1 372 ? 27.756  -12.793 8.392   1.00 18.48 ? 372  PHE B CD1 1 
ATOM   6233 C CD2 . PHE B 1 372 ? 27.451  -12.917 10.763  1.00 18.43 ? 372  PHE B CD2 1 
ATOM   6234 C CE1 . PHE B 1 372 ? 28.021  -14.167 8.341   1.00 17.96 ? 372  PHE B CE1 1 
ATOM   6235 C CE2 . PHE B 1 372 ? 27.719  -14.267 10.725  1.00 17.32 ? 372  PHE B CE2 1 
ATOM   6236 C CZ  . PHE B 1 372 ? 28.015  -14.898 9.517   1.00 17.57 ? 372  PHE B CZ  1 
ATOM   6237 N N   . SER B 1 373 ? 24.471  -12.601 9.465   1.00 17.93 ? 373  SER B N   1 
ATOM   6238 C CA  . SER B 1 373 ? 23.883  -13.703 10.205  1.00 17.88 ? 373  SER B CA  1 
ATOM   6239 C C   . SER B 1 373 ? 23.869  -14.869 9.250   1.00 17.37 ? 373  SER B C   1 
ATOM   6240 O O   . SER B 1 373 ? 23.927  -14.657 8.033   1.00 17.72 ? 373  SER B O   1 
ATOM   6241 C CB  . SER B 1 373 ? 22.466  -13.370 10.701  1.00 18.25 ? 373  SER B CB  1 
ATOM   6242 O OG  . SER B 1 373 ? 21.478  -13.628 9.699   1.00 18.14 ? 373  SER B OG  1 
ATOM   6243 N N   . SER B 1 374 ? 23.821  -16.088 9.770   1.00 16.27 ? 374  SER B N   1 
ATOM   6244 C CA  . SER B 1 374 ? 23.753  -17.244 8.887   1.00 16.71 ? 374  SER B CA  1 
ATOM   6245 C C   . SER B 1 374 ? 22.596  -17.093 7.974   1.00 16.08 ? 374  SER B C   1 
ATOM   6246 O O   . SER B 1 374 ? 22.759  -17.148 6.766   1.00 17.00 ? 374  SER B O   1 
ATOM   6247 C CB  . SER B 1 374 ? 23.545  -18.527 9.638   1.00 15.70 ? 374  SER B CB  1 
ATOM   6248 O OG  . SER B 1 374 ? 24.786  -18.923 10.067  1.00 21.48 ? 374  SER B OG  1 
ATOM   6249 N N   . ALA B 1 375 ? 21.436  -16.855 8.580   1.00 15.75 ? 375  ALA B N   1 
ATOM   6250 C CA  . ALA B 1 375 ? 20.166  -16.858 7.912   1.00 15.91 ? 375  ALA B CA  1 
ATOM   6251 C C   . ALA B 1 375 ? 20.103  -15.744 6.834   1.00 15.33 ? 375  ALA B C   1 
ATOM   6252 O O   . ALA B 1 375 ? 19.464  -15.951 5.784   1.00 15.87 ? 375  ALA B O   1 
ATOM   6253 C CB  . ALA B 1 375 ? 18.996  -16.730 8.965   1.00 15.78 ? 375  ALA B CB  1 
ATOM   6254 N N   . TRP B 1 376 ? 20.735  -14.594 7.095   1.00 13.83 ? 376  TRP B N   1 
ATOM   6255 C CA  . TRP B 1 376 ? 20.829  -13.517 6.093   1.00 14.43 ? 376  TRP B CA  1 
ATOM   6256 C C   . TRP B 1 376 ? 21.912  -13.781 5.031   1.00 14.98 ? 376  TRP B C   1 
ATOM   6257 O O   . TRP B 1 376 ? 21.975  -13.088 4.030   1.00 16.15 ? 376  TRP B O   1 
ATOM   6258 C CB  . TRP B 1 376 ? 21.048  -12.148 6.777   1.00 13.07 ? 376  TRP B CB  1 
ATOM   6259 C CG  . TRP B 1 376 ? 19.800  -11.594 7.386   1.00 14.56 ? 376  TRP B CG  1 
ATOM   6260 C CD1 . TRP B 1 376 ? 18.767  -12.312 7.990   1.00 15.40 ? 376  TRP B CD1 1 
ATOM   6261 C CD2 . TRP B 1 376 ? 19.412  -10.222 7.444   1.00 14.03 ? 376  TRP B CD2 1 
ATOM   6262 N NE1 . TRP B 1 376 ? 17.766  -11.455 8.373   1.00 15.98 ? 376  TRP B NE1 1 
ATOM   6263 C CE2 . TRP B 1 376 ? 18.133  -10.172 8.060   1.00 14.25 ? 376  TRP B CE2 1 
ATOM   6264 C CE3 . TRP B 1 376 ? 20.005  -9.036  7.013   1.00 13.98 ? 376  TRP B CE3 1 
ATOM   6265 C CZ2 . TRP B 1 376 ? 17.453  -8.981  8.268   1.00 14.52 ? 376  TRP B CZ2 1 
ATOM   6266 C CZ3 . TRP B 1 376 ? 19.330  -7.842  7.208   1.00 15.69 ? 376  TRP B CZ3 1 
ATOM   6267 C CH2 . TRP B 1 376 ? 18.061  -7.824  7.837   1.00 17.41 ? 376  TRP B CH2 1 
ATOM   6268 N N   . THR B 1 377 ? 22.759  -14.783 5.201   1.00 15.22 ? 377  THR B N   1 
ATOM   6269 C CA  . THR B 1 377 ? 23.827  -14.969 4.199   1.00 15.84 ? 377  THR B CA  1 
ATOM   6270 C C   . THR B 1 377 ? 23.792  -16.337 3.507   1.00 15.77 ? 377  THR B C   1 
ATOM   6271 O O   . THR B 1 377 ? 23.754  -16.421 2.269   1.00 16.19 ? 377  THR B O   1 
ATOM   6272 C CB  . THR B 1 377 ? 25.233  -14.635 4.763   1.00 15.54 ? 377  THR B CB  1 
ATOM   6273 O OG1 . THR B 1 377 ? 25.530  -15.530 5.816   1.00 17.64 ? 377  THR B OG1 1 
ATOM   6274 C CG2 . THR B 1 377 ? 25.232  -13.268 5.392   1.00 15.92 ? 377  THR B CG2 1 
ATOM   6275 N N   . VAL B 1 378 ? 23.804  -17.409 4.299   1.00 16.06 ? 378  VAL B N   1 
ATOM   6276 C CA  . VAL B 1 378 ? 23.776  -18.760 3.771   1.00 14.95 ? 378  VAL B CA  1 
ATOM   6277 C C   . VAL B 1 378 ? 22.563  -19.573 4.189   1.00 15.61 ? 378  VAL B C   1 
ATOM   6278 O O   . VAL B 1 378 ? 22.694  -20.667 4.737   1.00 15.31 ? 378  VAL B O   1 
ATOM   6279 C CB  . VAL B 1 378 ? 25.042  -19.495 4.140   1.00 15.91 ? 378  VAL B CB  1 
ATOM   6280 C CG1 . VAL B 1 378 ? 26.204  -18.766 3.541   1.00 13.32 ? 378  VAL B CG1 1 
ATOM   6281 C CG2 . VAL B 1 378 ? 25.184  -19.642 5.756   1.00 15.65 ? 378  VAL B CG2 1 
ATOM   6282 N N   . PRO B 1 379 ? 21.356  -19.073 3.902   1.00 16.28 ? 379  PRO B N   1 
ATOM   6283 C CA  . PRO B 1 379 ? 20.217  -19.945 4.135   1.00 16.84 ? 379  PRO B CA  1 
ATOM   6284 C C   . PRO B 1 379 ? 20.217  -21.041 3.082   1.00 17.91 ? 379  PRO B C   1 
ATOM   6285 O O   . PRO B 1 379 ? 21.089  -21.033 2.184   1.00 19.05 ? 379  PRO B O   1 
ATOM   6286 C CB  . PRO B 1 379 ? 19.045  -19.014 3.907   1.00 17.33 ? 379  PRO B CB  1 
ATOM   6287 C CG  . PRO B 1 379 ? 19.588  -17.955 3.018   1.00 16.92 ? 379  PRO B CG  1 
ATOM   6288 C CD  . PRO B 1 379 ? 20.943  -17.735 3.460   1.00 15.52 ? 379  PRO B CD  1 
ATOM   6289 N N   . PHE B 1 380 ? 19.301  -21.999 3.176   1.00 17.95 ? 380  PHE B N   1 
ATOM   6290 C CA  . PHE B 1 380 ? 19.142  -22.955 2.089   1.00 18.71 ? 380  PHE B CA  1 
ATOM   6291 C C   . PHE B 1 380 ? 18.875  -22.135 0.816   1.00 18.96 ? 380  PHE B C   1 
ATOM   6292 O O   . PHE B 1 380 ? 18.080  -21.172 0.857   1.00 18.69 ? 380  PHE B O   1 
ATOM   6293 C CB  . PHE B 1 380 ? 17.943  -23.878 2.334   1.00 18.75 ? 380  PHE B CB  1 
ATOM   6294 C CG  . PHE B 1 380 ? 18.211  -24.993 3.289   1.00 19.28 ? 380  PHE B CG  1 
ATOM   6295 C CD1 . PHE B 1 380 ? 19.371  -25.759 3.176   1.00 19.27 ? 380  PHE B CD1 1 
ATOM   6296 C CD2 . PHE B 1 380 ? 17.294  -25.298 4.280   1.00 20.22 ? 380  PHE B CD2 1 
ATOM   6297 C CE1 . PHE B 1 380 ? 19.632  -26.796 4.045   1.00 19.84 ? 380  PHE B CE1 1 
ATOM   6298 C CE2 . PHE B 1 380 ? 17.531  -26.339 5.163   1.00 22.74 ? 380  PHE B CE2 1 
ATOM   6299 C CZ  . PHE B 1 380 ? 18.710  -27.104 5.048   1.00 20.46 ? 380  PHE B CZ  1 
ATOM   6300 N N   . ALA B 1 381 ? 19.517  -22.527 -0.296  1.00 18.57 ? 381  ALA B N   1 
ATOM   6301 C CA  . ALA B 1 381 ? 19.336  -21.884 -1.606  1.00 17.95 ? 381  ALA B CA  1 
ATOM   6302 C C   . ALA B 1 381 ? 19.781  -20.409 -1.630  1.00 17.97 ? 381  ALA B C   1 
ATOM   6303 O O   . ALA B 1 381 ? 19.292  -19.614 -2.431  1.00 18.48 ? 381  ALA B O   1 
ATOM   6304 C CB  . ALA B 1 381 ? 17.901  -22.018 -2.048  1.00 17.10 ? 381  ALA B CB  1 
ATOM   6305 N N   . SER B 1 382 ? 20.678  -20.018 -0.730  1.00 17.32 ? 382  SER B N   1 
ATOM   6306 C CA  . SER B 1 382 ? 21.153  -18.644 -0.727  1.00 17.18 ? 382  SER B CA  1 
ATOM   6307 C C   . SER B 1 382 ? 21.741  -18.302 -2.083  1.00 17.01 ? 382  SER B C   1 
ATOM   6308 O O   . SER B 1 382 ? 22.204  -19.188 -2.810  1.00 16.71 ? 382  SER B O   1 
ATOM   6309 C CB  . SER B 1 382 ? 22.268  -18.464 0.282   1.00 17.21 ? 382  SER B CB  1 
ATOM   6310 O OG  . SER B 1 382 ? 23.486  -19.096 -0.176  1.00 19.87 ? 382  SER B OG  1 
ATOM   6311 N N   . ARG B 1 383 ? 21.744  -17.010 -2.397  1.00 17.16 ? 383  ARG B N   1 
ATOM   6312 C CA  . ARG B 1 383 ? 22.408  -16.495 -3.589  1.00 17.28 ? 383  ARG B CA  1 
ATOM   6313 C C   . ARG B 1 383 ? 23.213  -15.211 -3.333  1.00 17.28 ? 383  ARG B C   1 
ATOM   6314 O O   . ARG B 1 383 ? 22.805  -14.350 -2.552  1.00 17.13 ? 383  ARG B O   1 
ATOM   6315 C CB  . ARG B 1 383 ? 21.436  -16.390 -4.789  1.00 17.06 ? 383  ARG B CB  1 
ATOM   6316 C CG  . ARG B 1 383 ? 20.409  -15.304 -4.743  1.00 16.62 ? 383  ARG B CG  1 
ATOM   6317 C CD  . ARG B 1 383 ? 19.348  -15.511 -3.643  1.00 17.86 ? 383  ARG B CD  1 
ATOM   6318 N NE  . ARG B 1 383 ? 18.727  -16.842 -3.633  1.00 18.07 ? 383  ARG B NE  1 
ATOM   6319 C CZ  . ARG B 1 383 ? 17.561  -17.148 -4.191  1.00 16.61 ? 383  ARG B CZ  1 
ATOM   6320 N NH1 . ARG B 1 383 ? 16.874  -16.226 -4.842  1.00 16.72 ? 383  ARG B NH1 1 
ATOM   6321 N NH2 . ARG B 1 383 ? 17.079  -18.387 -4.094  1.00 14.29 ? 383  ARG B NH2 1 
ATOM   6322 N N   . LEU B 1 384 ? 24.379  -15.144 -3.968  1.00 16.80 ? 384  LEU B N   1 
ATOM   6323 C CA  . LEU B 1 384 ? 25.204  -13.946 -4.027  1.00 17.61 ? 384  LEU B CA  1 
ATOM   6324 C C   . LEU B 1 384 ? 25.173  -13.432 -5.463  1.00 17.38 ? 384  LEU B C   1 
ATOM   6325 O O   . LEU B 1 384 ? 25.494  -14.199 -6.361  1.00 18.06 ? 384  LEU B O   1 
ATOM   6326 C CB  . LEU B 1 384 ? 26.673  -14.300 -3.655  1.00 17.83 ? 384  LEU B CB  1 
ATOM   6327 C CG  . LEU B 1 384 ? 27.740  -13.224 -3.983  1.00 18.13 ? 384  LEU B CG  1 
ATOM   6328 C CD1 . LEU B 1 384 ? 27.688  -12.082 -2.921  1.00 19.48 ? 384  LEU B CD1 1 
ATOM   6329 C CD2 . LEU B 1 384 ? 29.147  -13.752 -4.149  1.00 11.82 ? 384  LEU B CD2 1 
ATOM   6330 N N   . TYR B 1 385 ? 24.821  -12.167 -5.701  1.00 16.63 ? 385  TYR B N   1 
ATOM   6331 C CA  . TYR B 1 385 ? 24.968  -11.596 -7.070  1.00 16.39 ? 385  TYR B CA  1 
ATOM   6332 C C   . TYR B 1 385 ? 26.090  -10.553 -7.117  1.00 16.41 ? 385  TYR B C   1 
ATOM   6333 O O   . TYR B 1 385 ? 26.064  -9.563  -6.383  1.00 16.37 ? 385  TYR B O   1 
ATOM   6334 C CB  . TYR B 1 385 ? 23.691  -10.906 -7.589  1.00 16.20 ? 385  TYR B CB  1 
ATOM   6335 C CG  . TYR B 1 385 ? 22.400  -11.719 -7.658  1.00 15.65 ? 385  TYR B CG  1 
ATOM   6336 C CD1 . TYR B 1 385 ? 22.398  -13.061 -8.029  1.00 14.28 ? 385  TYR B CD1 1 
ATOM   6337 C CD2 . TYR B 1 385 ? 21.181  -11.110 -7.401  1.00 15.82 ? 385  TYR B CD2 1 
ATOM   6338 C CE1 . TYR B 1 385 ? 21.214  -13.784 -8.087  1.00 14.81 ? 385  TYR B CE1 1 
ATOM   6339 C CE2 . TYR B 1 385 ? 19.968  -11.824 -7.460  1.00 17.63 ? 385  TYR B CE2 1 
ATOM   6340 C CZ  . TYR B 1 385 ? 19.994  -13.159 -7.816  1.00 16.41 ? 385  TYR B CZ  1 
ATOM   6341 O OH  . TYR B 1 385 ? 18.836  -13.867 -7.895  1.00 15.46 ? 385  TYR B OH  1 
ATOM   6342 N N   . VAL B 1 386 ? 27.082  -10.763 -7.964  1.00 16.20 ? 386  VAL B N   1 
ATOM   6343 C CA  . VAL B 1 386 ? 28.028  -9.691  -8.241  1.00 16.28 ? 386  VAL B CA  1 
ATOM   6344 C C   . VAL B 1 386 ? 27.587  -9.062  -9.575  1.00 17.73 ? 386  VAL B C   1 
ATOM   6345 O O   . VAL B 1 386 ? 27.433  -9.778  -10.562 1.00 18.50 ? 386  VAL B O   1 
ATOM   6346 C CB  . VAL B 1 386 ? 29.472  -10.268 -8.321  1.00 16.57 ? 386  VAL B CB  1 
ATOM   6347 C CG1 . VAL B 1 386 ? 30.508  -9.214  -8.755  1.00 14.55 ? 386  VAL B CG1 1 
ATOM   6348 C CG2 . VAL B 1 386 ? 29.858  -10.955 -6.977  1.00 14.42 ? 386  VAL B CG2 1 
ATOM   6349 N N   . GLU B 1 387 ? 27.333  -7.756  -9.619  1.00 18.29 ? 387  GLU B N   1 
ATOM   6350 C CA  . GLU B 1 387 ? 27.146  -7.081  -10.927 1.00 19.93 ? 387  GLU B CA  1 
ATOM   6351 C C   . GLU B 1 387 ? 28.192  -6.052  -11.205 1.00 20.30 ? 387  GLU B C   1 
ATOM   6352 O O   . GLU B 1 387 ? 28.846  -5.531  -10.306 1.00 20.89 ? 387  GLU B O   1 
ATOM   6353 C CB  . GLU B 1 387 ? 25.744  -6.512  -11.157 1.00 18.43 ? 387  GLU B CB  1 
ATOM   6354 C CG  . GLU B 1 387 ? 25.088  -6.349  -9.916  1.00 21.43 ? 387  GLU B CG  1 
ATOM   6355 C CD  . GLU B 1 387 ? 23.667  -5.879  -9.967  1.00 21.04 ? 387  GLU B CD  1 
ATOM   6356 O OE1 . GLU B 1 387 ? 22.777  -6.689  -10.331 1.00 17.53 ? 387  GLU B OE1 1 
ATOM   6357 O OE2 . GLU B 1 387 ? 23.471  -4.713  -9.524  1.00 19.95 ? 387  GLU B OE2 1 
ATOM   6358 N N   . MET B 1 388 ? 28.368  -5.805  -12.485 1.00 21.29 ? 388  MET B N   1 
ATOM   6359 C CA  . MET B 1 388 ? 29.174  -4.731  -12.963 1.00 22.43 ? 388  MET B CA  1 
ATOM   6360 C C   . MET B 1 388 ? 28.213  -3.983  -13.881 1.00 22.76 ? 388  MET B C   1 
ATOM   6361 O O   . MET B 1 388 ? 27.472  -4.595  -14.594 1.00 22.92 ? 388  MET B O   1 
ATOM   6362 C CB  . MET B 1 388 ? 30.358  -5.348  -13.667 1.00 22.23 ? 388  MET B CB  1 
ATOM   6363 C CG  . MET B 1 388 ? 31.511  -4.434  -13.936 1.00 24.32 ? 388  MET B CG  1 
ATOM   6364 S SD  . MET B 1 388 ? 33.084  -5.357  -13.907 1.00 24.43 ? 388  MET B SD  1 
ATOM   6365 C CE  . MET B 1 388 ? 32.866  -6.521  -15.269 1.00 24.62 ? 388  MET B CE  1 
ATOM   6366 N N   . MET B 1 389 ? 28.159  -2.663  -13.811 1.00 24.18 ? 389  MET B N   1 
ATOM   6367 C CA  . MET B 1 389 ? 27.255  -1.900  -14.648 1.00 25.32 ? 389  MET B CA  1 
ATOM   6368 C C   . MET B 1 389 ? 28.004  -0.736  -15.213 1.00 27.28 ? 389  MET B C   1 
ATOM   6369 O O   . MET B 1 389 ? 28.993  -0.298  -14.642 1.00 27.35 ? 389  MET B O   1 
ATOM   6370 C CB  . MET B 1 389 ? 26.035  -1.397  -13.841 1.00 25.22 ? 389  MET B CB  1 
ATOM   6371 C CG  . MET B 1 389 ? 26.378  -0.443  -12.703 1.00 22.46 ? 389  MET B CG  1 
ATOM   6372 S SD  . MET B 1 389 ? 24.961  0.100   -11.728 1.00 25.45 ? 389  MET B SD  1 
ATOM   6373 C CE  . MET B 1 389 ? 24.166  -1.421  -11.247 1.00 24.72 ? 389  MET B CE  1 
ATOM   6374 N N   . GLN B 1 390 ? 27.519  -0.239  -16.340 1.00 29.45 ? 390  GLN B N   1 
ATOM   6375 C CA  . GLN B 1 390 ? 28.060  0.939   -16.985 1.00 31.78 ? 390  GLN B CA  1 
ATOM   6376 C C   . GLN B 1 390 ? 27.033  2.045   -16.889 1.00 32.70 ? 390  GLN B C   1 
ATOM   6377 O O   . GLN B 1 390 ? 25.854  1.838   -17.167 1.00 32.92 ? 390  GLN B O   1 
ATOM   6378 C CB  . GLN B 1 390 ? 28.387  0.657   -18.439 1.00 31.80 ? 390  GLN B CB  1 
ATOM   6379 C CG  . GLN B 1 390 ? 29.586  1.418   -18.877 1.00 34.18 ? 390  GLN B CG  1 
ATOM   6380 C CD  . GLN B 1 390 ? 30.866  0.715   -18.509 1.00 37.98 ? 390  GLN B CD  1 
ATOM   6381 O OE1 . GLN B 1 390 ? 31.948  1.223   -18.773 1.00 41.91 ? 390  GLN B OE1 1 
ATOM   6382 N NE2 . GLN B 1 390 ? 30.756  -0.472  -17.909 1.00 38.70 ? 390  GLN B NE2 1 
ATOM   6383 N N   . CYS B 1 391 ? 27.473  3.212   -16.454 1.00 34.89 ? 391  CYS B N   1 
ATOM   6384 C CA  . CYS B 1 391 ? 26.520  4.248   -16.118 1.00 37.71 ? 391  CYS B CA  1 
ATOM   6385 C C   . CYS B 1 391 ? 26.780  5.491   -16.900 1.00 39.77 ? 391  CYS B C   1 
ATOM   6386 O O   . CYS B 1 391 ? 27.848  5.642   -17.479 1.00 40.24 ? 391  CYS B O   1 
ATOM   6387 C CB  . CYS B 1 391 ? 26.506  4.543   -14.623 1.00 37.21 ? 391  CYS B CB  1 
ATOM   6388 S SG  . CYS B 1 391 ? 25.830  3.195   -13.700 1.00 35.88 ? 391  CYS B SG  1 
ATOM   6389 N N   . GLN B 1 392 ? 25.782  6.374   -16.893 1.00 42.95 ? 392  GLN B N   1 
ATOM   6390 C CA  . GLN B 1 392 ? 25.752  7.562   -17.749 1.00 45.62 ? 392  GLN B CA  1 
ATOM   6391 C C   . GLN B 1 392 ? 26.846  8.535   -17.381 1.00 46.13 ? 392  GLN B C   1 
ATOM   6392 O O   . GLN B 1 392 ? 27.688  8.892   -18.215 1.00 47.17 ? 392  GLN B O   1 
ATOM   6393 C CB  . GLN B 1 392 ? 24.372  8.247   -17.728 1.00 46.12 ? 392  GLN B CB  1 
ATOM   6394 C CG  . GLN B 1 392 ? 23.932  8.739   -19.145 1.00 50.60 ? 392  GLN B CG  1 
ATOM   6395 C CD  . GLN B 1 392 ? 22.435  9.127   -19.231 1.00 56.12 ? 392  GLN B CD  1 
ATOM   6396 O OE1 . GLN B 1 392 ? 21.542  8.351   -18.839 1.00 56.93 ? 392  GLN B OE1 1 
ATOM   6397 N NE2 . GLN B 1 392 ? 22.162  10.333  -19.770 1.00 57.71 ? 392  GLN B NE2 1 
ATOM   6398 N N   . ALA B 1 393 ? 26.867  8.935   -16.119 1.00 46.62 ? 393  ALA B N   1 
ATOM   6399 C CA  . ALA B 1 393 ? 27.797  9.976   -15.689 1.00 46.84 ? 393  ALA B CA  1 
ATOM   6400 C C   . ALA B 1 393 ? 29.335  9.653   -15.721 1.00 46.71 ? 393  ALA B C   1 
ATOM   6401 O O   . ALA B 1 393 ? 30.147  10.583  -15.617 1.00 46.51 ? 393  ALA B O   1 
ATOM   6402 C CB  . ALA B 1 393 ? 27.352  10.518  -14.293 1.00 47.22 ? 393  ALA B CB  1 
ATOM   6403 N N   . GLU B 1 394 ? 29.723  8.373   -15.881 1.00 46.37 ? 394  GLU B N   1 
ATOM   6404 C CA  . GLU B 1 394 ? 31.088  7.885   -15.524 1.00 45.34 ? 394  GLU B CA  1 
ATOM   6405 C C   . GLU B 1 394 ? 31.716  6.938   -16.556 1.00 44.36 ? 394  GLU B C   1 
ATOM   6406 O O   . GLU B 1 394 ? 31.034  6.076   -17.082 1.00 44.43 ? 394  GLU B O   1 
ATOM   6407 C CB  . GLU B 1 394 ? 31.038  7.229   -14.126 1.00 45.44 ? 394  GLU B CB  1 
ATOM   6408 C CG  . GLU B 1 394 ? 32.143  6.215   -13.780 1.00 46.69 ? 394  GLU B CG  1 
ATOM   6409 C CD  . GLU B 1 394 ? 33.420  6.830   -13.197 1.00 49.38 ? 394  GLU B CD  1 
ATOM   6410 O OE1 . GLU B 1 394 ? 33.353  7.521   -12.148 1.00 49.02 ? 394  GLU B OE1 1 
ATOM   6411 O OE2 . GLU B 1 394 ? 34.506  6.589   -13.784 1.00 49.61 ? 394  GLU B OE2 1 
ATOM   6412 N N   . GLN B 1 395 ? 33.018  7.081   -16.815 1.00 43.02 ? 395  GLN B N   1 
ATOM   6413 C CA  . GLN B 1 395 ? 33.707  6.271   -17.841 1.00 41.89 ? 395  GLN B CA  1 
ATOM   6414 C C   . GLN B 1 395 ? 33.968  4.801   -17.458 1.00 40.19 ? 395  GLN B C   1 
ATOM   6415 O O   . GLN B 1 395 ? 34.077  3.951   -18.342 1.00 39.90 ? 395  GLN B O   1 
ATOM   6416 C CB  . GLN B 1 395 ? 35.032  6.913   -18.241 1.00 42.29 ? 395  GLN B CB  1 
ATOM   6417 C CG  . GLN B 1 395 ? 35.099  8.439   -18.014 1.00 47.48 ? 395  GLN B CG  1 
ATOM   6418 C CD  . GLN B 1 395 ? 36.550  9.006   -18.086 1.00 54.02 ? 395  GLN B CD  1 
ATOM   6419 O OE1 . GLN B 1 395 ? 37.493  8.290   -18.467 1.00 55.65 ? 395  GLN B OE1 1 
ATOM   6420 N NE2 . GLN B 1 395 ? 36.720  10.294  -17.721 1.00 55.00 ? 395  GLN B NE2 1 
ATOM   6421 N N   . GLU B 1 396 ? 34.055  4.518   -16.154 1.00 37.79 ? 396  GLU B N   1 
ATOM   6422 C CA  . GLU B 1 396 ? 34.464  3.200   -15.599 1.00 35.26 ? 396  GLU B CA  1 
ATOM   6423 C C   . GLU B 1 396 ? 33.303  2.284   -15.163 1.00 32.59 ? 396  GLU B C   1 
ATOM   6424 O O   . GLU B 1 396 ? 32.248  2.760   -14.716 1.00 32.86 ? 396  GLU B O   1 
ATOM   6425 C CB  . GLU B 1 396 ? 35.332  3.416   -14.358 1.00 35.56 ? 396  GLU B CB  1 
ATOM   6426 C CG  . GLU B 1 396 ? 36.845  3.511   -14.584 1.00 38.48 ? 396  GLU B CG  1 
ATOM   6427 C CD  . GLU B 1 396 ? 37.624  3.428   -13.255 1.00 42.12 ? 396  GLU B CD  1 
ATOM   6428 O OE1 . GLU B 1 396 ? 37.765  2.274   -12.717 1.00 43.71 ? 396  GLU B OE1 1 
ATOM   6429 O OE2 . GLU B 1 396 ? 38.068  4.511   -12.769 1.00 39.43 ? 396  GLU B OE2 1 
ATOM   6430 N N   . PRO B 1 397 ? 33.514  0.966   -15.224 1.00 29.24 ? 397  PRO B N   1 
ATOM   6431 C CA  . PRO B 1 397 ? 32.464  0.115   -14.702 1.00 27.06 ? 397  PRO B CA  1 
ATOM   6432 C C   . PRO B 1 397 ? 32.354  0.209   -13.175 1.00 25.02 ? 397  PRO B C   1 
ATOM   6433 O O   . PRO B 1 397 ? 33.346  0.309   -12.505 1.00 23.67 ? 397  PRO B O   1 
ATOM   6434 C CB  . PRO B 1 397 ? 32.913  -1.291  -15.114 1.00 27.06 ? 397  PRO B CB  1 
ATOM   6435 C CG  . PRO B 1 397 ? 34.313  -1.133  -15.773 1.00 27.24 ? 397  PRO B CG  1 
ATOM   6436 C CD  . PRO B 1 397 ? 34.772  0.234   -15.454 1.00 29.07 ? 397  PRO B CD  1 
ATOM   6437 N N   . LEU B 1 398 ? 31.139  0.195   -12.658 1.00 23.19 ? 398  LEU B N   1 
ATOM   6438 C CA  . LEU B 1 398 ? 30.871  0.214   -11.234 1.00 22.13 ? 398  LEU B CA  1 
ATOM   6439 C C   . LEU B 1 398 ? 30.445  -1.210  -10.759 1.00 21.93 ? 398  LEU B C   1 
ATOM   6440 O O   . LEU B 1 398 ? 29.553  -1.831  -11.366 1.00 22.14 ? 398  LEU B O   1 
ATOM   6441 C CB  . LEU B 1 398 ? 29.743  1.209   -10.935 1.00 21.73 ? 398  LEU B CB  1 
ATOM   6442 C CG  . LEU B 1 398 ? 29.907  2.699   -11.284 1.00 20.73 ? 398  LEU B CG  1 
ATOM   6443 C CD1 . LEU B 1 398 ? 28.901  3.486   -10.504 1.00 19.43 ? 398  LEU B CD1 1 
ATOM   6444 C CD2 . LEU B 1 398 ? 31.318  3.203   -11.005 1.00 19.27 ? 398  LEU B CD2 1 
ATOM   6445 N N   . VAL B 1 399 ? 31.051  -1.712  -9.674  1.00 19.90 ? 399  VAL B N   1 
ATOM   6446 C CA  . VAL B 1 399 ? 30.735  -3.020  -9.164  1.00 17.76 ? 399  VAL B CA  1 
ATOM   6447 C C   . VAL B 1 399 ? 29.667  -2.885  -8.105  1.00 18.51 ? 399  VAL B C   1 
ATOM   6448 O O   . VAL B 1 399 ? 29.769  -2.033  -7.220  1.00 18.33 ? 399  VAL B O   1 
ATOM   6449 C CB  . VAL B 1 399 ? 31.937  -3.600  -8.523  1.00 17.85 ? 399  VAL B CB  1 
ATOM   6450 C CG1 . VAL B 1 399 ? 31.589  -4.894  -7.786  1.00 17.48 ? 399  VAL B CG1 1 
ATOM   6451 C CG2 . VAL B 1 399 ? 33.063  -3.789  -9.545  1.00 16.10 ? 399  VAL B CG2 1 
ATOM   6452 N N   . ARG B 1 400 ? 28.629  -3.708  -8.153  1.00 18.17 ? 400  ARG B N   1 
ATOM   6453 C CA  . ARG B 1 400 ? 27.715  -3.735  -7.031  1.00 18.23 ? 400  ARG B CA  1 
ATOM   6454 C C   . ARG B 1 400 ? 27.519  -5.168  -6.569  1.00 18.61 ? 400  ARG B C   1 
ATOM   6455 O O   . ARG B 1 400 ? 27.724  -6.090  -7.369  1.00 19.09 ? 400  ARG B O   1 
ATOM   6456 C CB  . ARG B 1 400 ? 26.414  -3.071  -7.408  1.00 18.53 ? 400  ARG B CB  1 
ATOM   6457 C CG  . ARG B 1 400 ? 25.249  -3.406  -6.481  1.00 20.29 ? 400  ARG B CG  1 
ATOM   6458 C CD  . ARG B 1 400 ? 24.036  -2.513  -6.726  1.00 19.85 ? 400  ARG B CD  1 
ATOM   6459 N NE  . ARG B 1 400 ? 23.219  -3.089  -7.769  1.00 23.06 ? 400  ARG B NE  1 
ATOM   6460 C CZ  . ARG B 1 400 ? 21.976  -2.719  -8.060  1.00 23.26 ? 400  ARG B CZ  1 
ATOM   6461 N NH1 . ARG B 1 400 ? 21.385  -1.773  -7.355  1.00 23.55 ? 400  ARG B NH1 1 
ATOM   6462 N NH2 . ARG B 1 400 ? 21.318  -3.324  -9.064  1.00 21.54 ? 400  ARG B NH2 1 
ATOM   6463 N N   . VAL B 1 401 ? 27.155  -5.372  -5.293  1.00 18.24 ? 401  VAL B N   1 
ATOM   6464 C CA  . VAL B 1 401 ? 26.964  -6.730  -4.747  1.00 17.26 ? 401  VAL B CA  1 
ATOM   6465 C C   . VAL B 1 401 ? 25.607  -6.894  -4.045  1.00 17.32 ? 401  VAL B C   1 
ATOM   6466 O O   . VAL B 1 401 ? 25.276  -6.093  -3.181  1.00 16.41 ? 401  VAL B O   1 
ATOM   6467 C CB  . VAL B 1 401 ? 28.105  -7.094  -3.788  1.00 16.59 ? 401  VAL B CB  1 
ATOM   6468 C CG1 . VAL B 1 401 ? 27.690  -8.184  -2.836  1.00 18.03 ? 401  VAL B CG1 1 
ATOM   6469 C CG2 . VAL B 1 401 ? 29.345  -7.564  -4.553  1.00 16.98 ? 401  VAL B CG2 1 
ATOM   6470 N N   . LEU B 1 402 ? 24.816  -7.922  -4.377  1.00 17.04 ? 402  LEU B N   1 
ATOM   6471 C CA  . LEU B 1 402 ? 23.654  -8.213  -3.498  1.00 18.14 ? 402  LEU B CA  1 
ATOM   6472 C C   . LEU B 1 402 ? 23.796  -9.569  -2.845  1.00 18.81 ? 402  LEU B C   1 
ATOM   6473 O O   . LEU B 1 402 ? 24.283  -10.492 -3.472  1.00 20.27 ? 402  LEU B O   1 
ATOM   6474 C CB  . LEU B 1 402 ? 22.299  -8.086  -4.230  1.00 18.12 ? 402  LEU B CB  1 
ATOM   6475 C CG  . LEU B 1 402 ? 22.086  -6.792  -5.073  1.00 17.14 ? 402  LEU B CG  1 
ATOM   6476 C CD1 . LEU B 1 402 ? 22.855  -6.834  -6.436  1.00 10.26 ? 402  LEU B CD1 1 
ATOM   6477 C CD2 . LEU B 1 402 ? 20.620  -6.589  -5.291  1.00 13.44 ? 402  LEU B CD2 1 
ATOM   6478 N N   . VAL B 1 403 ? 23.377  -9.685  -1.584  1.00 19.41 ? 403  VAL B N   1 
ATOM   6479 C CA  . VAL B 1 403 ? 23.435  -10.943 -0.803  1.00 18.87 ? 403  VAL B CA  1 
ATOM   6480 C C   . VAL B 1 403 ? 22.001  -11.228 -0.346  1.00 18.81 ? 403  VAL B C   1 
ATOM   6481 O O   . VAL B 1 403 ? 21.456  -10.501 0.460   1.00 18.36 ? 403  VAL B O   1 
ATOM   6482 C CB  . VAL B 1 403 ? 24.409  -10.789 0.389   1.00 18.80 ? 403  VAL B CB  1 
ATOM   6483 C CG1 . VAL B 1 403 ? 24.355  -11.969 1.333   1.00 18.48 ? 403  VAL B CG1 1 
ATOM   6484 C CG2 . VAL B 1 403 ? 25.810  -10.596 -0.132  1.00 19.01 ? 403  VAL B CG2 1 
ATOM   6485 N N   . ASN B 1 404 ? 21.406  -12.261 -0.945  1.00 19.47 ? 404  ASN B N   1 
ATOM   6486 C CA  . ASN B 1 404 ? 19.977  -12.594 -0.859  1.00 19.68 ? 404  ASN B CA  1 
ATOM   6487 C C   . ASN B 1 404 ? 18.976  -11.462 -1.062  1.00 20.37 ? 404  ASN B C   1 
ATOM   6488 O O   . ASN B 1 404 ? 17.991  -11.372 -0.334  1.00 20.85 ? 404  ASN B O   1 
ATOM   6489 C CB  . ASN B 1 404 ? 19.662  -13.340 0.429   1.00 19.92 ? 404  ASN B CB  1 
ATOM   6490 C CG  . ASN B 1 404 ? 20.411  -14.638 0.543   1.00 19.42 ? 404  ASN B CG  1 
ATOM   6491 O OD1 . ASN B 1 404 ? 20.199  -15.589 -0.209  1.00 16.73 ? 404  ASN B OD1 1 
ATOM   6492 N ND2 . ASN B 1 404 ? 21.299  -14.680 1.482   1.00 21.61 ? 404  ASN B ND2 1 
ATOM   6493 N N   . ASP B 1 405 ? 19.235  -10.631 -2.073  1.00 21.24 ? 405  ASP B N   1 
ATOM   6494 C CA  . ASP B 1 405 ? 18.349  -9.524  -2.563  1.00 21.72 ? 405  ASP B CA  1 
ATOM   6495 C C   . ASP B 1 405 ? 18.519  -8.204  -1.845  1.00 22.51 ? 405  ASP B C   1 
ATOM   6496 O O   . ASP B 1 405 ? 17.746  -7.247  -2.077  1.00 23.18 ? 405  ASP B O   1 
ATOM   6497 C CB  . ASP B 1 405 ? 16.884  -9.931  -2.607  1.00 20.36 ? 405  ASP B CB  1 
ATOM   6498 C CG  . ASP B 1 405 ? 16.653  -11.160 -3.472  1.00 22.11 ? 405  ASP B CG  1 
ATOM   6499 O OD1 . ASP B 1 405 ? 17.550  -11.505 -4.299  1.00 23.72 ? 405  ASP B OD1 1 
ATOM   6500 O OD2 . ASP B 1 405 ? 15.585  -11.799 -3.317  1.00 17.83 ? 405  ASP B OD2 1 
ATOM   6501 N N   . ARG B 1 406 ? 19.530  -8.180  -0.967  1.00 23.20 ? 406  ARG B N   1 
ATOM   6502 C CA  . ARG B 1 406 ? 19.947  -7.008  -0.185  1.00 23.03 ? 406  ARG B CA  1 
ATOM   6503 C C   . ARG B 1 406 ? 21.259  -6.429  -0.755  1.00 22.34 ? 406  ARG B C   1 
ATOM   6504 O O   . ARG B 1 406 ? 22.264  -7.124  -0.875  1.00 22.20 ? 406  ARG B O   1 
ATOM   6505 C CB  . ARG B 1 406 ? 20.129  -7.404  1.306   1.00 23.10 ? 406  ARG B CB  1 
ATOM   6506 C CG  . ARG B 1 406 ? 20.598  -6.263  2.197   1.00 25.24 ? 406  ARG B CG  1 
ATOM   6507 C CD  . ARG B 1 406 ? 21.030  -6.710  3.592   1.00 28.18 ? 406  ARG B CD  1 
ATOM   6508 N NE  . ARG B 1 406 ? 21.587  -5.593  4.352   1.00 31.65 ? 406  ARG B NE  1 
ATOM   6509 C CZ  . ARG B 1 406 ? 22.868  -5.470  4.708   1.00 34.15 ? 406  ARG B CZ  1 
ATOM   6510 N NH1 . ARG B 1 406 ? 23.760  -6.411  4.408   1.00 32.52 ? 406  ARG B NH1 1 
ATOM   6511 N NH2 . ARG B 1 406 ? 23.252  -4.398  5.397   1.00 36.64 ? 406  ARG B NH2 1 
ATOM   6512 N N   . VAL B 1 407 ? 21.242  -5.161  -1.130  1.00 22.08 ? 407  VAL B N   1 
ATOM   6513 C CA  . VAL B 1 407 ? 22.476  -4.502  -1.536  1.00 20.57 ? 407  VAL B CA  1 
ATOM   6514 C C   . VAL B 1 407 ? 23.391  -4.380  -0.307  1.00 21.31 ? 407  VAL B C   1 
ATOM   6515 O O   . VAL B 1 407 ? 22.964  -3.919  0.757   1.00 21.24 ? 407  VAL B O   1 
ATOM   6516 C CB  . VAL B 1 407 ? 22.223  -3.121  -2.146  1.00 20.43 ? 407  VAL B CB  1 
ATOM   6517 C CG1 . VAL B 1 407 ? 23.506  -2.597  -2.747  1.00 18.28 ? 407  VAL B CG1 1 
ATOM   6518 C CG2 . VAL B 1 407 ? 21.135  -3.188  -3.214  1.00 16.69 ? 407  VAL B CG2 1 
ATOM   6519 N N   . VAL B 1 408 ? 24.642  -4.818  -0.460  1.00 20.93 ? 408  VAL B N   1 
ATOM   6520 C CA  . VAL B 1 408 ? 25.613  -4.793  0.614   1.00 20.33 ? 408  VAL B CA  1 
ATOM   6521 C C   . VAL B 1 408 ? 26.707  -3.850  0.135   1.00 20.71 ? 408  VAL B C   1 
ATOM   6522 O O   . VAL B 1 408 ? 27.336  -4.120  -0.907  1.00 21.12 ? 408  VAL B O   1 
ATOM   6523 C CB  . VAL B 1 408 ? 26.130  -6.238  0.978   1.00 20.53 ? 408  VAL B CB  1 
ATOM   6524 C CG1 . VAL B 1 408 ? 27.156  -6.204  2.108   1.00 20.52 ? 408  VAL B CG1 1 
ATOM   6525 C CG2 . VAL B 1 408 ? 24.989  -7.124  1.396   1.00 18.89 ? 408  VAL B CG2 1 
ATOM   6526 N N   . PRO B 1 409 ? 26.906  -2.724  0.852   1.00 20.27 ? 409  PRO B N   1 
ATOM   6527 C CA  . PRO B 1 409 ? 27.884  -1.733  0.438   1.00 20.44 ? 409  PRO B CA  1 
ATOM   6528 C C   . PRO B 1 409 ? 29.298  -2.295  0.450   1.00 20.98 ? 409  PRO B C   1 
ATOM   6529 O O   . PRO B 1 409 ? 29.745  -2.854  1.455   1.00 22.42 ? 409  PRO B O   1 
ATOM   6530 C CB  . PRO B 1 409 ? 27.761  -0.629  1.506   1.00 20.44 ? 409  PRO B CB  1 
ATOM   6531 C CG  . PRO B 1 409 ? 26.407  -0.778  2.067   1.00 21.67 ? 409  PRO B CG  1 
ATOM   6532 C CD  . PRO B 1 409 ? 26.081  -2.260  1.983   1.00 20.46 ? 409  PRO B CD  1 
ATOM   6533 N N   . LEU B 1 410 ? 30.017  -2.137  -0.643  1.00 20.55 ? 410  LEU B N   1 
ATOM   6534 C CA  . LEU B 1 410 ? 31.419  -2.569  -0.682  1.00 21.12 ? 410  LEU B CA  1 
ATOM   6535 C C   . LEU B 1 410 ? 32.321  -1.929  0.406   1.00 21.35 ? 410  LEU B C   1 
ATOM   6536 O O   . LEU B 1 410 ? 32.132  -0.743  0.811   1.00 20.70 ? 410  LEU B O   1 
ATOM   6537 C CB  . LEU B 1 410 ? 31.991  -2.290  -2.067  1.00 20.99 ? 410  LEU B CB  1 
ATOM   6538 C CG  . LEU B 1 410 ? 31.159  -2.871  -3.233  1.00 20.82 ? 410  LEU B CG  1 
ATOM   6539 C CD1 . LEU B 1 410 ? 32.024  -2.872  -4.504  1.00 20.05 ? 410  LEU B CD1 1 
ATOM   6540 C CD2 . LEU B 1 410 ? 30.658  -4.271  -2.913  1.00 16.56 ? 410  LEU B CD2 1 
ATOM   6541 N N   . HIS B 1 411 ? 33.284  -2.710  0.884   1.00 20.72 ? 411  HIS B N   1 
ATOM   6542 C CA  . HIS B 1 411 ? 34.291  -2.165  1.772   1.00 20.56 ? 411  HIS B CA  1 
ATOM   6543 C C   . HIS B 1 411 ? 35.634  -2.198  1.077   1.00 20.26 ? 411  HIS B C   1 
ATOM   6544 O O   . HIS B 1 411 ? 35.834  -2.982  0.130   1.00 19.67 ? 411  HIS B O   1 
ATOM   6545 C CB  . HIS B 1 411 ? 34.355  -2.955  3.059   1.00 20.71 ? 411  HIS B CB  1 
ATOM   6546 C CG  . HIS B 1 411 ? 33.243  -2.650  4.012   1.00 20.90 ? 411  HIS B CG  1 
ATOM   6547 N ND1 . HIS B 1 411 ? 32.028  -3.295  3.966   1.00 22.33 ? 411  HIS B ND1 1 
ATOM   6548 C CD2 . HIS B 1 411 ? 33.175  -1.792  5.055   1.00 21.28 ? 411  HIS B CD2 1 
ATOM   6549 C CE1 . HIS B 1 411 ? 31.252  -2.838  4.931   1.00 23.61 ? 411  HIS B CE1 1 
ATOM   6550 N NE2 . HIS B 1 411 ? 31.926  -1.923  5.605   1.00 24.47 ? 411  HIS B NE2 1 
ATOM   6551 N N   . GLY B 1 412 ? 36.541  -1.332  1.538   1.00 20.01 ? 412  GLY B N   1 
ATOM   6552 C CA  . GLY B 1 412 ? 37.924  -1.333  1.065   1.00 19.16 ? 412  GLY B CA  1 
ATOM   6553 C C   . GLY B 1 412 ? 38.112  -0.427  -0.133  1.00 19.49 ? 412  GLY B C   1 
ATOM   6554 O O   . GLY B 1 412 ? 39.180  -0.429  -0.756  1.00 17.75 ? 412  GLY B O   1 
ATOM   6555 N N   . CYS B 1 413 ? 37.062  0.355   -0.430  1.00 20.19 ? 413  CYS B N   1 
ATOM   6556 C CA  . CYS B 1 413 ? 37.056  1.265   -1.582  1.00 21.43 ? 413  CYS B CA  1 
ATOM   6557 C C   . CYS B 1 413 ? 36.057  2.410   -1.424  1.00 21.54 ? 413  CYS B C   1 
ATOM   6558 O O   . CYS B 1 413 ? 35.120  2.330   -0.585  1.00 22.24 ? 413  CYS B O   1 
ATOM   6559 C CB  . CYS B 1 413 ? 36.814  0.503   -2.887  1.00 21.44 ? 413  CYS B CB  1 
ATOM   6560 S SG  . CYS B 1 413 ? 35.366  -0.509  -2.871  1.00 21.98 ? 413  CYS B SG  1 
ATOM   6561 N N   . PRO B 1 414 ? 36.253  3.505   -2.198  1.00 22.25 ? 414  PRO B N   1 
ATOM   6562 C CA  . PRO B 1 414 ? 35.327  4.643   -1.973  1.00 22.22 ? 414  PRO B CA  1 
ATOM   6563 C C   . PRO B 1 414 ? 33.919  4.296   -2.443  1.00 22.50 ? 414  PRO B C   1 
ATOM   6564 O O   . PRO B 1 414 ? 33.621  4.541   -3.602  1.00 23.47 ? 414  PRO B O   1 
ATOM   6565 C CB  . PRO B 1 414 ? 35.927  5.794   -2.804  1.00 20.90 ? 414  PRO B CB  1 
ATOM   6566 C CG  . PRO B 1 414 ? 37.295  5.306   -3.297  1.00 21.81 ? 414  PRO B CG  1 
ATOM   6567 C CD  . PRO B 1 414 ? 37.294  3.800   -3.217  1.00 21.74 ? 414  PRO B CD  1 
ATOM   6568 N N   . VAL B 1 415 ? 33.087  3.684   -1.580  1.00 23.16 ? 415  VAL B N   1 
ATOM   6569 C CA  . VAL B 1 415 ? 31.674  3.419   -1.936  1.00 24.01 ? 415  VAL B CA  1 
ATOM   6570 C C   . VAL B 1 415 ? 30.923  4.680   -2.147  1.00 24.27 ? 415  VAL B C   1 
ATOM   6571 O O   . VAL B 1 415 ? 31.202  5.646   -1.460  1.00 25.77 ? 415  VAL B O   1 
ATOM   6572 C CB  . VAL B 1 415 ? 30.816  2.692   -0.858  1.00 24.57 ? 415  VAL B CB  1 
ATOM   6573 C CG1 . VAL B 1 415 ? 30.514  1.277   -1.296  1.00 23.44 ? 415  VAL B CG1 1 
ATOM   6574 C CG2 . VAL B 1 415 ? 31.359  2.824   0.585   1.00 23.85 ? 415  VAL B CG2 1 
ATOM   6575 N N   . ASP B 1 416 ? 29.972  4.662   -3.081  1.00 24.67 ? 416  ASP B N   1 
ATOM   6576 C CA  . ASP B 1 416 ? 28.997  5.746   -3.259  1.00 24.97 ? 416  ASP B CA  1 
ATOM   6577 C C   . ASP B 1 416 ? 27.719  5.412   -2.487  1.00 25.39 ? 416  ASP B C   1 
ATOM   6578 O O   . ASP B 1 416 ? 27.648  4.376   -1.850  1.00 26.16 ? 416  ASP B O   1 
ATOM   6579 C CB  . ASP B 1 416 ? 28.730  6.000   -4.734  1.00 24.94 ? 416  ASP B CB  1 
ATOM   6580 C CG  . ASP B 1 416 ? 28.150  4.760   -5.479  1.00 27.00 ? 416  ASP B CG  1 
ATOM   6581 O OD1 . ASP B 1 416 ? 27.363  3.976   -4.873  1.00 26.18 ? 416  ASP B OD1 1 
ATOM   6582 O OD2 . ASP B 1 416 ? 28.474  4.599   -6.692  1.00 26.72 ? 416  ASP B OD2 1 
ATOM   6583 N N   . ALA B 1 417 ? 26.720  6.281   -2.508  1.00 26.30 ? 417  ALA B N   1 
ATOM   6584 C CA  . ALA B 1 417 ? 25.508  6.075   -1.683  1.00 27.22 ? 417  ALA B CA  1 
ATOM   6585 C C   . ALA B 1 417 ? 24.626  4.918   -2.195  1.00 27.60 ? 417  ALA B C   1 
ATOM   6586 O O   . ALA B 1 417 ? 23.652  4.542   -1.527  1.00 28.38 ? 417  ALA B O   1 
ATOM   6587 C CB  . ALA B 1 417 ? 24.672  7.393   -1.583  1.00 27.28 ? 417  ALA B CB  1 
ATOM   6588 N N   . LEU B 1 418 ? 24.954  4.389   -3.385  1.00 26.88 ? 418  LEU B N   1 
ATOM   6589 C CA  . LEU B 1 418 ? 24.218  3.283   -3.977  1.00 26.19 ? 418  LEU B CA  1 
ATOM   6590 C C   . LEU B 1 418 ? 24.941  1.937   -3.745  1.00 25.68 ? 418  LEU B C   1 
ATOM   6591 O O   . LEU B 1 418 ? 24.593  0.934   -4.365  1.00 25.62 ? 418  LEU B O   1 
ATOM   6592 C CB  . LEU B 1 418 ? 23.895  3.542   -5.467  1.00 26.01 ? 418  LEU B CB  1 
ATOM   6593 C CG  . LEU B 1 418 ? 23.034  4.792   -5.792  1.00 26.82 ? 418  LEU B CG  1 
ATOM   6594 C CD1 . LEU B 1 418 ? 22.967  5.051   -7.264  1.00 24.86 ? 418  LEU B CD1 1 
ATOM   6595 C CD2 . LEU B 1 418 ? 21.617  4.801   -5.175  1.00 25.22 ? 418  LEU B CD2 1 
ATOM   6596 N N   . GLY B 1 419 ? 25.927  1.924   -2.844  1.00 24.20 ? 419  GLY B N   1 
ATOM   6597 C CA  . GLY B 1 419 ? 26.649  0.696   -2.523  1.00 23.48 ? 419  GLY B CA  1 
ATOM   6598 C C   . GLY B 1 419 ? 27.819  0.276   -3.414  1.00 22.91 ? 419  GLY B C   1 
ATOM   6599 O O   . GLY B 1 419 ? 28.419  -0.757  -3.168  1.00 21.77 ? 419  GLY B O   1 
ATOM   6600 N N   . ARG B 1 420 ? 28.147  1.080   -4.419  1.00 22.40 ? 420  ARG B N   1 
ATOM   6601 C CA  . ARG B 1 420 ? 29.030  0.655   -5.517  1.00 23.31 ? 420  ARG B CA  1 
ATOM   6602 C C   . ARG B 1 420 ? 30.436  1.205   -5.435  1.00 23.13 ? 420  ARG B C   1 
ATOM   6603 O O   . ARG B 1 420 ? 30.669  2.311   -4.953  1.00 24.96 ? 420  ARG B O   1 
ATOM   6604 C CB  . ARG B 1 420 ? 28.454  1.061   -6.905  1.00 23.20 ? 420  ARG B CB  1 
ATOM   6605 C CG  . ARG B 1 420 ? 26.920  0.892   -7.082  1.00 23.78 ? 420  ARG B CG  1 
ATOM   6606 C CD  . ARG B 1 420 ? 26.430  1.530   -8.391  1.00 24.64 ? 420  ARG B CD  1 
ATOM   6607 N NE  . ARG B 1 420 ? 26.547  2.994   -8.370  1.00 24.46 ? 420  ARG B NE  1 
ATOM   6608 C CZ  . ARG B 1 420 ? 25.859  3.826   -9.157  1.00 25.59 ? 420  ARG B CZ  1 
ATOM   6609 N NH1 . ARG B 1 420 ? 24.987  3.340   -10.048 1.00 26.03 ? 420  ARG B NH1 1 
ATOM   6610 N NH2 . ARG B 1 420 ? 26.031  5.144   -9.051  1.00 20.12 ? 420  ARG B NH2 1 
ATOM   6611 N N   . CYS B 1 421 ? 31.389  0.468   -5.949  1.00 23.27 ? 421  CYS B N   1 
ATOM   6612 C CA  . CYS B 1 421 ? 32.707  1.061   -6.174  1.00 23.92 ? 421  CYS B CA  1 
ATOM   6613 C C   . CYS B 1 421 ? 33.007  0.918   -7.631  1.00 23.58 ? 421  CYS B C   1 
ATOM   6614 O O   . CYS B 1 421 ? 32.494  0.007   -8.292  1.00 23.88 ? 421  CYS B O   1 
ATOM   6615 C CB  . CYS B 1 421 ? 33.814  0.346   -5.381  1.00 23.91 ? 421  CYS B CB  1 
ATOM   6616 S SG  . CYS B 1 421 ? 33.879  0.700   -3.569  1.00 28.13 ? 421  CYS B SG  1 
ATOM   6617 N N   . THR B 1 422 ? 33.848  1.802   -8.141  1.00 23.21 ? 422  THR B N   1 
ATOM   6618 C CA  . THR B 1 422 ? 34.460  1.575   -9.447  1.00 23.01 ? 422  THR B CA  1 
ATOM   6619 C C   . THR B 1 422 ? 35.266  0.267   -9.427  1.00 23.30 ? 422  THR B C   1 
ATOM   6620 O O   . THR B 1 422 ? 35.862  -0.074  -8.417  1.00 23.92 ? 422  THR B O   1 
ATOM   6621 C CB  . THR B 1 422 ? 35.426  2.706   -9.848  1.00 22.74 ? 422  THR B CB  1 
ATOM   6622 O OG1 . THR B 1 422 ? 36.612  2.554   -9.084  1.00 22.25 ? 422  THR B OG1 1 
ATOM   6623 C CG2 . THR B 1 422 ? 34.816  4.115   -9.605  1.00 21.09 ? 422  THR B CG2 1 
ATOM   6624 N N   . ARG B 1 423 ? 35.315  -0.430  -10.557 1.00 23.44 ? 423  ARG B N   1 
ATOM   6625 C CA  . ARG B 1 423 ? 35.917  -1.743  -10.633 1.00 23.87 ? 423  ARG B CA  1 
ATOM   6626 C C   . ARG B 1 423 ? 37.391  -1.730  -10.264 1.00 24.33 ? 423  ARG B C   1 
ATOM   6627 O O   . ARG B 1 423 ? 37.834  -2.619  -9.535  1.00 24.18 ? 423  ARG B O   1 
ATOM   6628 C CB  . ARG B 1 423 ? 35.686  -2.377  -12.003 1.00 23.64 ? 423  ARG B CB  1 
ATOM   6629 C CG  . ARG B 1 423 ? 36.281  -3.781  -12.203 1.00 25.36 ? 423  ARG B CG  1 
ATOM   6630 C CD  . ARG B 1 423 ? 37.683  -3.781  -12.880 1.00 27.91 ? 423  ARG B CD  1 
ATOM   6631 N NE  . ARG B 1 423 ? 37.773  -2.855  -14.011 1.00 27.48 ? 423  ARG B NE  1 
ATOM   6632 C CZ  . ARG B 1 423 ? 37.466  -3.144  -15.279 1.00 29.65 ? 423  ARG B CZ  1 
ATOM   6633 N NH1 . ARG B 1 423 ? 37.026  -4.352  -15.637 1.00 29.67 ? 423  ARG B NH1 1 
ATOM   6634 N NH2 . ARG B 1 423 ? 37.568  -2.196  -16.204 1.00 26.67 ? 423  ARG B NH2 1 
ATOM   6635 N N   . ASP B 1 424 ? 38.138  -0.733  -10.747 1.00 25.08 ? 424  ASP B N   1 
ATOM   6636 C CA  . ASP B 1 424 ? 39.581  -0.663  -10.465 1.00 25.86 ? 424  ASP B CA  1 
ATOM   6637 C C   . ASP B 1 424 ? 39.845  -0.491  -8.981  1.00 25.29 ? 424  ASP B C   1 
ATOM   6638 O O   . ASP B 1 424 ? 40.777  -1.093  -8.443  1.00 25.23 ? 424  ASP B O   1 
ATOM   6639 C CB  . ASP B 1 424 ? 40.294  0.467   -11.234 1.00 26.65 ? 424  ASP B CB  1 
ATOM   6640 C CG  . ASP B 1 424 ? 40.523  0.134   -12.698 1.00 30.08 ? 424  ASP B CG  1 
ATOM   6641 O OD1 . ASP B 1 424 ? 40.304  -1.024  -13.124 1.00 34.32 ? 424  ASP B OD1 1 
ATOM   6642 O OD2 . ASP B 1 424 ? 40.935  1.050   -13.434 1.00 34.76 ? 424  ASP B OD2 1 
ATOM   6643 N N   . SER B 1 425 ? 39.011  0.306   -8.316  1.00 24.39 ? 425  SER B N   1 
ATOM   6644 C CA  . SER B 1 425 ? 39.229  0.557   -6.897  1.00 23.94 ? 425  SER B CA  1 
ATOM   6645 C C   . SER B 1 425 ? 38.748  -0.637  -6.044  1.00 23.31 ? 425  SER B C   1 
ATOM   6646 O O   . SER B 1 425 ? 39.372  -0.963  -5.037  1.00 23.81 ? 425  SER B O   1 
ATOM   6647 C CB  . SER B 1 425 ? 38.564  1.863   -6.466  1.00 23.09 ? 425  SER B CB  1 
ATOM   6648 O OG  . SER B 1 425 ? 37.158  1.679   -6.346  1.00 23.72 ? 425  SER B OG  1 
ATOM   6649 N N   . PHE B 1 426 ? 37.648  -1.276  -6.442  1.00 22.76 ? 426  PHE B N   1 
ATOM   6650 C CA  . PHE B 1 426 ? 37.222  -2.531  -5.805  1.00 21.79 ? 426  PHE B CA  1 
ATOM   6651 C C   . PHE B 1 426 ? 38.301  -3.612  -5.877  1.00 21.86 ? 426  PHE B C   1 
ATOM   6652 O O   . PHE B 1 426 ? 38.515  -4.330  -4.906  1.00 21.57 ? 426  PHE B O   1 
ATOM   6653 C CB  . PHE B 1 426 ? 35.945  -3.062  -6.419  1.00 20.62 ? 426  PHE B CB  1 
ATOM   6654 C CG  . PHE B 1 426 ? 35.451  -4.313  -5.781  1.00 19.44 ? 426  PHE B CG  1 
ATOM   6655 C CD1 . PHE B 1 426 ? 35.062  -4.312  -4.447  1.00 21.20 ? 426  PHE B CD1 1 
ATOM   6656 C CD2 . PHE B 1 426 ? 35.383  -5.501  -6.504  1.00 19.47 ? 426  PHE B CD2 1 
ATOM   6657 C CE1 . PHE B 1 426 ? 34.588  -5.466  -3.835  1.00 22.34 ? 426  PHE B CE1 1 
ATOM   6658 C CE2 . PHE B 1 426 ? 34.943  -6.682  -5.916  1.00 20.00 ? 426  PHE B CE2 1 
ATOM   6659 C CZ  . PHE B 1 426 ? 34.522  -6.680  -4.600  1.00 21.62 ? 426  PHE B CZ  1 
ATOM   6660 N N   . VAL B 1 427 ? 38.977  -3.706  -7.021  1.00 22.23 ? 427  VAL B N   1 
ATOM   6661 C CA  . VAL B 1 427 ? 40.009  -4.731  -7.215  1.00 22.71 ? 427  VAL B CA  1 
ATOM   6662 C C   . VAL B 1 427 ? 41.182  -4.426  -6.316  1.00 22.86 ? 427  VAL B C   1 
ATOM   6663 O O   . VAL B 1 427 ? 41.593  -5.262  -5.499  1.00 23.89 ? 427  VAL B O   1 
ATOM   6664 C CB  . VAL B 1 427 ? 40.389  -4.945  -8.716  1.00 22.54 ? 427  VAL B CB  1 
ATOM   6665 C CG1 . VAL B 1 427 ? 41.740  -5.656  -8.857  1.00 22.21 ? 427  VAL B CG1 1 
ATOM   6666 C CG2 . VAL B 1 427 ? 39.324  -5.784  -9.421  1.00 21.31 ? 427  VAL B CG2 1 
ATOM   6667 N N   . ARG B 1 428 ? 41.660  -3.196  -6.397  1.00 23.78 ? 428  ARG B N   1 
ATOM   6668 C CA  . ARG B 1 428 ? 42.711  -2.689  -5.494  1.00 24.14 ? 428  ARG B CA  1 
ATOM   6669 C C   . ARG B 1 428 ? 42.400  -2.913  -4.007  1.00 23.74 ? 428  ARG B C   1 
ATOM   6670 O O   . ARG B 1 428 ? 43.309  -3.183  -3.247  1.00 24.29 ? 428  ARG B O   1 
ATOM   6671 C CB  . ARG B 1 428 ? 42.955  -1.217  -5.780  1.00 24.78 ? 428  ARG B CB  1 
ATOM   6672 C CG  . ARG B 1 428 ? 43.893  -0.485  -4.833  1.00 29.50 ? 428  ARG B CG  1 
ATOM   6673 C CD  . ARG B 1 428 ? 43.369  0.918   -4.636  1.00 37.11 ? 428  ARG B CD  1 
ATOM   6674 N NE  . ARG B 1 428 ? 44.430  1.907   -4.437  1.00 45.01 ? 428  ARG B NE  1 
ATOM   6675 C CZ  . ARG B 1 428 ? 44.405  3.146   -4.948  1.00 48.60 ? 428  ARG B CZ  1 
ATOM   6676 N NH1 . ARG B 1 428 ? 43.376  3.532   -5.714  1.00 49.09 ? 428  ARG B NH1 1 
ATOM   6677 N NH2 . ARG B 1 428 ? 45.420  3.989   -4.716  1.00 48.39 ? 428  ARG B NH2 1 
ATOM   6678 N N   . GLY B 1 429 ? 41.132  -2.826  -3.584  1.00 23.37 ? 429  GLY B N   1 
ATOM   6679 C CA  . GLY B 1 429 ? 40.781  -3.008  -2.159  1.00 22.13 ? 429  GLY B CA  1 
ATOM   6680 C C   . GLY B 1 429 ? 40.944  -4.452  -1.672  1.00 21.72 ? 429  GLY B C   1 
ATOM   6681 O O   . GLY B 1 429 ? 41.065  -4.697  -0.473  1.00 22.52 ? 429  GLY B O   1 
ATOM   6682 N N   . LEU B 1 430 ? 40.961  -5.400  -2.606  1.00 20.02 ? 430  LEU B N   1 
ATOM   6683 C CA  . LEU B 1 430 ? 41.066  -6.827  -2.287  1.00 18.41 ? 430  LEU B CA  1 
ATOM   6684 C C   . LEU B 1 430 ? 42.514  -7.302  -2.328  1.00 17.96 ? 430  LEU B C   1 
ATOM   6685 O O   . LEU B 1 430 ? 42.814  -8.389  -2.833  1.00 17.96 ? 430  LEU B O   1 
ATOM   6686 C CB  . LEU B 1 430 ? 40.184  -7.674  -3.237  1.00 17.82 ? 430  LEU B CB  1 
ATOM   6687 C CG  . LEU B 1 430 ? 38.673  -7.376  -3.446  1.00 14.84 ? 430  LEU B CG  1 
ATOM   6688 C CD1 . LEU B 1 430 ? 38.194  -8.246  -4.593  1.00 14.68 ? 430  LEU B CD1 1 
ATOM   6689 C CD2 . LEU B 1 430 ? 37.781  -7.585  -2.202  1.00 9.26  ? 430  LEU B CD2 1 
ATOM   6690 N N   . SER B 1 431 ? 43.397  -6.470  -1.779  1.00 18.02 ? 431  SER B N   1 
ATOM   6691 C CA  . SER B 1 431 ? 44.811  -6.796  -1.538  1.00 18.17 ? 431  SER B CA  1 
ATOM   6692 C C   . SER B 1 431 ? 44.984  -8.008  -0.667  1.00 18.39 ? 431  SER B C   1 
ATOM   6693 O O   . SER B 1 431 ? 45.974  -8.722  -0.811  1.00 18.20 ? 431  SER B O   1 
ATOM   6694 C CB  . SER B 1 431 ? 45.525  -5.622  -0.856  1.00 18.54 ? 431  SER B CB  1 
ATOM   6695 O OG  . SER B 1 431 ? 44.671  -4.979  0.074   1.00 17.71 ? 431  SER B OG  1 
ATOM   6696 N N   . PHE B 1 432 ? 44.029  -8.241  0.243   1.00 18.69 ? 432  PHE B N   1 
ATOM   6697 C CA  . PHE B 1 432 ? 44.120  -9.394  1.129   1.00 19.14 ? 432  PHE B CA  1 
ATOM   6698 C C   . PHE B 1 432 ? 44.120  -10.620 0.237   1.00 19.65 ? 432  PHE B C   1 
ATOM   6699 O O   . PHE B 1 432 ? 45.101  -11.339 0.212   1.00 20.19 ? 432  PHE B O   1 
ATOM   6700 C CB  . PHE B 1 432 ? 43.025  -9.415  2.201   1.00 19.54 ? 432  PHE B CB  1 
ATOM   6701 C CG  . PHE B 1 432 ? 42.939  -10.733 2.974   1.00 19.77 ? 432  PHE B CG  1 
ATOM   6702 C CD1 . PHE B 1 432 ? 43.809  -10.994 4.039   1.00 18.87 ? 432  PHE B CD1 1 
ATOM   6703 C CD2 . PHE B 1 432 ? 42.009  -11.695 2.623   1.00 19.77 ? 432  PHE B CD2 1 
ATOM   6704 C CE1 . PHE B 1 432 ? 43.759  -12.163 4.727   1.00 18.27 ? 432  PHE B CE1 1 
ATOM   6705 C CE2 . PHE B 1 432 ? 41.950  -12.911 3.290   1.00 20.84 ? 432  PHE B CE2 1 
ATOM   6706 C CZ  . PHE B 1 432 ? 42.834  -13.156 4.353   1.00 20.12 ? 432  PHE B CZ  1 
ATOM   6707 N N   . ALA B 1 433 ? 43.080  -10.811 -0.575  1.00 19.70 ? 433  ALA B N   1 
ATOM   6708 C CA  . ALA B 1 433 ? 43.052  -11.972 -1.507  1.00 19.11 ? 433  ALA B CA  1 
ATOM   6709 C C   . ALA B 1 433 ? 44.196  -11.890 -2.531  1.00 19.41 ? 433  ALA B C   1 
ATOM   6710 O O   . ALA B 1 433 ? 44.755  -12.915 -2.969  1.00 17.48 ? 433  ALA B O   1 
ATOM   6711 C CB  . ALA B 1 433 ? 41.703  -12.077 -2.200  1.00 17.78 ? 433  ALA B CB  1 
ATOM   6712 N N   . ARG B 1 434 ? 44.542  -10.656 -2.913  1.00 20.79 ? 434  ARG B N   1 
ATOM   6713 C CA  . ARG B 1 434 ? 45.457  -10.489 -4.043  1.00 22.40 ? 434  ARG B CA  1 
ATOM   6714 C C   . ARG B 1 434 ? 46.851  -10.960 -3.626  1.00 22.63 ? 434  ARG B C   1 
ATOM   6715 O O   . ARG B 1 434 ? 47.610  -11.447 -4.461  1.00 23.17 ? 434  ARG B O   1 
ATOM   6716 C CB  . ARG B 1 434 ? 45.469  -9.049  -4.600  1.00 22.13 ? 434  ARG B CB  1 
ATOM   6717 C CG  . ARG B 1 434 ? 44.539  -8.808  -5.774  1.00 24.41 ? 434  ARG B CG  1 
ATOM   6718 C CD  . ARG B 1 434 ? 44.747  -7.467  -6.539  1.00 25.24 ? 434  ARG B CD  1 
ATOM   6719 N NE  . ARG B 1 434 ? 44.732  -6.294  -5.646  1.00 28.97 ? 434  ARG B NE  1 
ATOM   6720 C CZ  . ARG B 1 434 ? 45.837  -5.651  -5.261  1.00 27.76 ? 434  ARG B CZ  1 
ATOM   6721 N NH1 . ARG B 1 434 ? 47.007  -6.049  -5.724  1.00 28.31 ? 434  ARG B NH1 1 
ATOM   6722 N NH2 . ARG B 1 434 ? 45.775  -4.616  -4.439  1.00 25.62 ? 434  ARG B NH2 1 
ATOM   6723 N N   . SER B 1 435 ? 47.158  -10.837 -2.329  1.00 23.12 ? 435  SER B N   1 
ATOM   6724 C CA  . SER B 1 435 ? 48.479  -11.225 -1.776  1.00 23.41 ? 435  SER B CA  1 
ATOM   6725 C C   . SER B 1 435 ? 48.545  -12.699 -1.423  1.00 23.14 ? 435  SER B C   1 
ATOM   6726 O O   . SER B 1 435 ? 49.612  -13.218 -1.071  1.00 23.50 ? 435  SER B O   1 
ATOM   6727 C CB  . SER B 1 435 ? 48.839  -10.377 -0.550  1.00 23.14 ? 435  SER B CB  1 
ATOM   6728 O OG  . SER B 1 435 ? 47.760  -10.354 0.391   1.00 23.74 ? 435  SER B OG  1 
ATOM   6729 N N   . GLY B 1 436 ? 47.407  -13.373 -1.535  1.00 22.91 ? 436  GLY B N   1 
ATOM   6730 C CA  . GLY B 1 436 ? 47.300  -14.773 -1.119  1.00 22.80 ? 436  GLY B CA  1 
ATOM   6731 C C   . GLY B 1 436 ? 46.746  -14.977 0.290   1.00 22.66 ? 436  GLY B C   1 
ATOM   6732 O O   . GLY B 1 436 ? 46.824  -16.083 0.826   1.00 22.04 ? 436  GLY B O   1 
ATOM   6733 N N   . GLY B 1 437 ? 46.187  -13.917 0.887   1.00 22.22 ? 437  GLY B N   1 
ATOM   6734 C CA  . GLY B 1 437 ? 45.667  -13.956 2.269   1.00 23.00 ? 437  GLY B CA  1 
ATOM   6735 C C   . GLY B 1 437 ? 46.683  -14.531 3.229   1.00 23.25 ? 437  GLY B C   1 
ATOM   6736 O O   . GLY B 1 437 ? 47.854  -14.201 3.116   1.00 24.76 ? 437  GLY B O   1 
ATOM   6737 N N   . ASP B 1 438 ? 46.258  -15.424 4.125   1.00 22.75 ? 438  ASP B N   1 
ATOM   6738 C CA  . ASP B 1 438 ? 47.171  -16.141 5.028   1.00 22.62 ? 438  ASP B CA  1 
ATOM   6739 C C   . ASP B 1 438 ? 47.347  -17.574 4.613   1.00 22.85 ? 438  ASP B C   1 
ATOM   6740 O O   . ASP B 1 438 ? 47.652  -18.435 5.436   1.00 22.73 ? 438  ASP B O   1 
ATOM   6741 C CB  . ASP B 1 438 ? 46.689  -16.074 6.489   1.00 21.57 ? 438  ASP B CB  1 
ATOM   6742 C CG  . ASP B 1 438 ? 46.489  -14.663 6.952   1.00 21.55 ? 438  ASP B CG  1 
ATOM   6743 O OD1 . ASP B 1 438 ? 47.369  -13.846 6.682   1.00 22.50 ? 438  ASP B OD1 1 
ATOM   6744 O OD2 . ASP B 1 438 ? 45.442  -14.349 7.575   1.00 21.66 ? 438  ASP B OD2 1 
ATOM   6745 N N   . TRP B 1 439 ? 47.179  -17.836 3.322   1.00 23.55 ? 439  TRP B N   1 
ATOM   6746 C CA  . TRP B 1 439 ? 47.349  -19.200 2.829   1.00 23.87 ? 439  TRP B CA  1 
ATOM   6747 C C   . TRP B 1 439 ? 48.666  -19.871 3.312   1.00 25.13 ? 439  TRP B C   1 
ATOM   6748 O O   . TRP B 1 439 ? 48.650  -21.066 3.589   1.00 24.89 ? 439  TRP B O   1 
ATOM   6749 C CB  . TRP B 1 439 ? 47.181  -19.294 1.303   1.00 22.39 ? 439  TRP B CB  1 
ATOM   6750 C CG  . TRP B 1 439 ? 47.004  -20.723 0.839   1.00 21.16 ? 439  TRP B CG  1 
ATOM   6751 C CD1 . TRP B 1 439 ? 47.991  -21.568 0.354   1.00 18.70 ? 439  TRP B CD1 1 
ATOM   6752 C CD2 . TRP B 1 439 ? 45.794  -21.506 0.874   1.00 18.90 ? 439  TRP B CD2 1 
ATOM   6753 N NE1 . TRP B 1 439 ? 47.450  -22.799 0.065   1.00 19.23 ? 439  TRP B NE1 1 
ATOM   6754 C CE2 . TRP B 1 439 ? 46.116  -22.796 0.385   1.00 18.15 ? 439  TRP B CE2 1 
ATOM   6755 C CE3 . TRP B 1 439 ? 44.465  -21.232 1.239   1.00 18.54 ? 439  TRP B CE3 1 
ATOM   6756 C CZ2 . TRP B 1 439 ? 45.163  -23.806 0.256   1.00 18.78 ? 439  TRP B CZ2 1 
ATOM   6757 C CZ3 . TRP B 1 439 ? 43.496  -22.248 1.098   1.00 18.17 ? 439  TRP B CZ3 1 
ATOM   6758 C CH2 . TRP B 1 439 ? 43.854  -23.516 0.593   1.00 18.22 ? 439  TRP B CH2 1 
ATOM   6759 N N   . ALA B 1 440 ? 49.777  -19.115 3.437   1.00 26.67 ? 440  ALA B N   1 
ATOM   6760 C CA  . ALA B 1 440 ? 51.091  -19.694 3.857   1.00 28.35 ? 440  ALA B CA  1 
ATOM   6761 C C   . ALA B 1 440 ? 51.030  -20.353 5.242   1.00 29.76 ? 440  ALA B C   1 
ATOM   6762 O O   . ALA B 1 440 ? 51.812  -21.252 5.552   1.00 29.98 ? 440  ALA B O   1 
ATOM   6763 C CB  . ALA B 1 440 ? 52.233  -18.651 3.793   1.00 27.87 ? 440  ALA B CB  1 
ATOM   6764 N N   . GLU B 1 441 ? 50.065  -19.927 6.056   1.00 31.61 ? 441  GLU B N   1 
ATOM   6765 C CA  . GLU B 1 441 ? 49.907  -20.417 7.427   1.00 33.20 ? 441  GLU B CA  1 
ATOM   6766 C C   . GLU B 1 441 ? 49.134  -21.715 7.486   1.00 33.37 ? 441  GLU B C   1 
ATOM   6767 O O   . GLU B 1 441 ? 48.871  -22.224 8.568   1.00 33.46 ? 441  GLU B O   1 
ATOM   6768 C CB  . GLU B 1 441 ? 49.214  -19.348 8.270   1.00 33.89 ? 441  GLU B CB  1 
ATOM   6769 C CG  . GLU B 1 441 ? 49.978  -18.012 8.242   1.00 37.41 ? 441  GLU B CG  1 
ATOM   6770 C CD  . GLU B 1 441 ? 49.565  -17.055 9.358   1.00 42.82 ? 441  GLU B CD  1 
ATOM   6771 O OE1 . GLU B 1 441 ? 48.877  -17.528 10.306  1.00 44.33 ? 441  GLU B OE1 1 
ATOM   6772 O OE2 . GLU B 1 441 ? 49.943  -15.839 9.286   1.00 43.83 ? 441  GLU B OE2 1 
ATOM   6773 N N   . CYS B 1 442 ? 48.786  -22.249 6.315   1.00 33.81 ? 442  CYS B N   1 
ATOM   6774 C CA  . CYS B 1 442 ? 48.055  -23.502 6.214   1.00 34.06 ? 442  CYS B CA  1 
ATOM   6775 C C   . CYS B 1 442 ? 48.950  -24.694 6.598   1.00 35.76 ? 442  CYS B C   1 
ATOM   6776 O O   . CYS B 1 442 ? 48.468  -25.824 6.851   1.00 35.46 ? 442  CYS B O   1 
ATOM   6777 C CB  . CYS B 1 442 ? 47.474  -23.678 4.799   1.00 33.36 ? 442  CYS B CB  1 
ATOM   6778 S SG  . CYS B 1 442 ? 46.025  -22.620 4.304   1.00 29.65 ? 442  CYS B SG  1 
ATOM   6779 N N   . PHE B 1 443 ? 50.250  -24.433 6.662   1.00 37.85 ? 443  PHE B N   1 
ATOM   6780 C CA  . PHE B 1 443 ? 51.232  -25.518 6.705   1.00 40.42 ? 443  PHE B CA  1 
ATOM   6781 C C   . PHE B 1 443 ? 52.208  -25.462 7.874   1.00 41.90 ? 443  PHE B C   1 
ATOM   6782 O O   . PHE B 1 443 ? 52.530  -26.484 8.456   1.00 42.61 ? 443  PHE B O   1 
ATOM   6783 C CB  . PHE B 1 443 ? 51.915  -25.643 5.341   1.00 40.50 ? 443  PHE B CB  1 
ATOM   6784 C CG  . PHE B 1 443 ? 50.928  -25.761 4.205   1.00 40.17 ? 443  PHE B CG  1 
ATOM   6785 C CD1 . PHE B 1 443 ? 50.187  -26.942 4.030   1.00 39.68 ? 443  PHE B CD1 1 
ATOM   6786 C CD2 . PHE B 1 443 ? 50.687  -24.677 3.360   1.00 40.69 ? 443  PHE B CD2 1 
ATOM   6787 C CE1 . PHE B 1 443 ? 49.252  -27.063 3.017   1.00 39.11 ? 443  PHE B CE1 1 
ATOM   6788 C CE2 . PHE B 1 443 ? 49.750  -24.782 2.328   1.00 41.53 ? 443  PHE B CE2 1 
ATOM   6789 C CZ  . PHE B 1 443 ? 49.030  -25.988 2.156   1.00 41.11 ? 443  PHE B CZ  1 
ATOM   6790 N N   . ALA B 1 444 ? 52.655  -24.273 8.237   1.00 44.13 ? 444  ALA B N   1 
ATOM   6791 C CA  . ALA B 1 444 ? 53.364  -24.091 9.516   1.00 46.35 ? 444  ALA B CA  1 
ATOM   6792 C C   . ALA B 1 444 ? 52.396  -23.722 10.696  1.00 47.28 ? 444  ALA B C   1 
ATOM   6793 O O   . ALA B 1 444 ? 51.964  -24.588 11.500  1.00 47.67 ? 444  ALA B O   1 
ATOM   6794 C CB  . ALA B 1 444 ? 54.526  -23.039 9.368   1.00 46.92 ? 444  ALA B CB  1 
ATOM   6795 O OXT . ALA B 1 444 ? 52.013  -22.543 10.882  1.00 47.45 ? 444  ALA B OXT 1 
HETATM 6796 C C1  . NAG C 2 .   ? 19.813  23.955  37.726  1.00 40.45 ? 1001 NAG A C1  1 
HETATM 6797 C C2  . NAG C 2 .   ? 19.193  22.908  38.662  1.00 37.03 ? 1001 NAG A C2  1 
HETATM 6798 C C3  . NAG C 2 .   ? 18.319  23.533  39.756  1.00 39.46 ? 1001 NAG A C3  1 
HETATM 6799 C C4  . NAG C 2 .   ? 19.155  24.541  40.503  1.00 40.74 ? 1001 NAG A C4  1 
HETATM 6800 C C5  . NAG C 2 .   ? 19.497  25.586  39.439  1.00 42.76 ? 1001 NAG A C5  1 
HETATM 6801 C C6  . NAG C 2 .   ? 20.109  26.876  39.999  1.00 43.97 ? 1001 NAG A C6  1 
HETATM 6802 C C7  . NAG C 2 .   ? 18.711  20.983  37.187  1.00 29.42 ? 1001 NAG A C7  1 
HETATM 6803 C C8  . NAG C 2 .   ? 17.551  20.207  36.607  1.00 25.82 ? 1001 NAG A C8  1 
HETATM 6804 N N2  . NAG C 2 .   ? 18.336  21.993  37.959  1.00 31.92 ? 1001 NAG A N2  1 
HETATM 6805 O O3  . NAG C 2 .   ? 17.804  22.587  40.674  1.00 38.84 ? 1001 NAG A O3  1 
HETATM 6806 O O4  . NAG C 2 .   ? 18.414  25.026  41.594  1.00 39.83 ? 1001 NAG A O4  1 
HETATM 6807 O O5  . NAG C 2 .   ? 20.396  24.945  38.536  1.00 42.19 ? 1001 NAG A O5  1 
HETATM 6808 O O6  . NAG C 2 .   ? 21.391  26.606  40.535  1.00 46.11 ? 1001 NAG A O6  1 
HETATM 6809 O O7  . NAG C 2 .   ? 19.887  20.696  36.932  1.00 28.73 ? 1001 NAG A O7  1 
HETATM 6810 C C1  . NAG D 2 .   ? -28.240 10.769  38.223  1.00 36.11 ? 1002 NAG A C1  1 
HETATM 6811 C C2  . NAG D 2 .   ? -27.598 11.951  38.985  1.00 41.25 ? 1002 NAG A C2  1 
HETATM 6812 C C3  . NAG D 2 .   ? -28.280 13.299  38.715  1.00 40.89 ? 1002 NAG A C3  1 
HETATM 6813 C C4  . NAG D 2 .   ? -28.436 13.558  37.206  1.00 41.68 ? 1002 NAG A C4  1 
HETATM 6814 C C5  . NAG D 2 .   ? -29.118 12.285  36.623  1.00 42.17 ? 1002 NAG A C5  1 
HETATM 6815 C C6  . NAG D 2 .   ? -29.577 12.321  35.150  1.00 41.54 ? 1002 NAG A C6  1 
HETATM 6816 C C7  . NAG D 2 .   ? -26.243 11.338  40.871  1.00 40.54 ? 1002 NAG A C7  1 
HETATM 6817 C C8  . NAG D 2 .   ? -26.098 11.121  42.344  1.00 41.86 ? 1002 NAG A C8  1 
HETATM 6818 N N2  . NAG D 2 .   ? -27.430 11.735  40.428  1.00 40.18 ? 1002 NAG A N2  1 
HETATM 6819 O O3  . NAG D 2 .   ? -27.382 14.203  39.293  1.00 43.81 ? 1002 NAG A O3  1 
HETATM 6820 O O4  . NAG D 2 .   ? -29.079 14.803  36.882  1.00 39.00 ? 1002 NAG A O4  1 
HETATM 6821 O O5  . NAG D 2 .   ? -28.288 11.136  36.855  1.00 38.34 ? 1002 NAG A O5  1 
HETATM 6822 O O6  . NAG D 2 .   ? -28.476 12.428  34.271  1.00 39.43 ? 1002 NAG A O6  1 
HETATM 6823 O O7  . NAG D 2 .   ? -25.287 11.150  40.120  1.00 38.21 ? 1002 NAG A O7  1 
HETATM 6824 C C1  . NAG E 2 .   ? -11.812 -12.800 43.870  1.00 24.56 ? 1003 NAG A C1  1 
HETATM 6825 C C2  . NAG E 2 .   ? -13.214 -13.150 44.331  1.00 25.38 ? 1003 NAG A C2  1 
HETATM 6826 C C3  . NAG E 2 .   ? -13.693 -12.253 45.459  1.00 27.98 ? 1003 NAG A C3  1 
HETATM 6827 C C4  . NAG E 2 .   ? -12.583 -12.083 46.512  1.00 29.88 ? 1003 NAG A C4  1 
HETATM 6828 C C5  . NAG E 2 .   ? -11.211 -11.826 45.863  1.00 30.62 ? 1003 NAG A C5  1 
HETATM 6829 C C6  . NAG E 2 .   ? -10.051 -11.759 46.855  1.00 30.64 ? 1003 NAG A C6  1 
HETATM 6830 C C7  . NAG E 2 .   ? -14.394 -14.026 42.457  1.00 29.94 ? 1003 NAG A C7  1 
HETATM 6831 C C8  . NAG E 2 .   ? -15.240 -13.660 41.285  1.00 29.91 ? 1003 NAG A C8  1 
HETATM 6832 N N2  . NAG E 2 .   ? -14.044 -12.987 43.188  1.00 27.84 ? 1003 NAG A N2  1 
HETATM 6833 O O3  . NAG E 2 .   ? -14.887 -12.816 46.005  1.00 28.57 ? 1003 NAG A O3  1 
HETATM 6834 O O4  . NAG E 2 .   ? -12.877 -11.010 47.386  1.00 32.26 ? 1003 NAG A O4  1 
HETATM 6835 O O5  . NAG E 2 .   ? -10.948 -12.869 44.960  1.00 28.39 ? 1003 NAG A O5  1 
HETATM 6836 O O6  . NAG E 2 .   ? -10.483 -10.948 47.889  1.00 30.29 ? 1003 NAG A O6  1 
HETATM 6837 O O7  . NAG E 2 .   ? -14.069 -15.197 42.716  1.00 30.83 ? 1003 NAG A O7  1 
HETATM 6838 C C1  . NAG F 2 .   ? 16.104  -43.506 28.308  1.00 44.88 ? 1001 NAG B C1  1 
HETATM 6839 C C2  . NAG F 2 .   ? 17.138  -42.371 28.359  1.00 44.69 ? 1001 NAG B C2  1 
HETATM 6840 C C3  . NAG F 2 .   ? 18.571  -42.903 28.280  1.00 46.31 ? 1001 NAG B C3  1 
HETATM 6841 C C4  . NAG F 2 .   ? 18.787  -43.937 29.379  1.00 47.44 ? 1001 NAG B C4  1 
HETATM 6842 C C5  . NAG F 2 .   ? 17.747  -45.055 29.184  1.00 49.07 ? 1001 NAG B C5  1 
HETATM 6843 C C6  . NAG F 2 .   ? 17.851  -46.110 30.285  1.00 50.52 ? 1001 NAG B C6  1 
HETATM 6844 C C7  . NAG F 2 .   ? 16.237  -40.312 27.339  1.00 39.78 ? 1001 NAG B C7  1 
HETATM 6845 C C8  . NAG F 2 .   ? 16.247  -39.434 26.107  1.00 35.59 ? 1001 NAG B C8  1 
HETATM 6846 N N2  . NAG F 2 .   ? 16.983  -41.409 27.278  1.00 41.70 ? 1001 NAG B N2  1 
HETATM 6847 O O3  . NAG F 2 .   ? 19.518  -41.857 28.391  1.00 46.18 ? 1001 NAG B O3  1 
HETATM 6848 O O4  . NAG F 2 .   ? 20.104  -44.444 29.301  1.00 46.66 ? 1001 NAG B O4  1 
HETATM 6849 O O5  . NAG F 2 .   ? 16.412  -44.553 29.195  1.00 46.66 ? 1001 NAG B O5  1 
HETATM 6850 O O6  . NAG F 2 .   ? 17.723  -45.467 31.540  1.00 51.12 ? 1001 NAG B O6  1 
HETATM 6851 O O7  . NAG F 2 .   ? 15.573  -40.024 28.346  1.00 40.98 ? 1001 NAG B O7  1 
HETATM 6852 C C1  . NAG G 2 .   ? 42.910  -29.948 -11.573 1.00 38.10 ? 1002 NAG B C1  1 
HETATM 6853 C C2  . NAG G 2 .   ? 43.144  -31.091 -10.576 1.00 42.57 ? 1002 NAG B C2  1 
HETATM 6854 C C3  . NAG G 2 .   ? 43.311  -32.425 -11.310 1.00 42.94 ? 1002 NAG B C3  1 
HETATM 6855 C C4  . NAG G 2 .   ? 42.087  -32.677 -12.191 1.00 43.00 ? 1002 NAG B C4  1 
HETATM 6856 C C5  . NAG G 2 .   ? 41.844  -31.455 -13.096 1.00 42.33 ? 1002 NAG B C5  1 
HETATM 6857 C C6  . NAG G 2 .   ? 40.582  -31.532 -13.972 1.00 41.81 ? 1002 NAG B C6  1 
HETATM 6858 C C7  . NAG G 2 .   ? 44.033  -30.454 -8.387  1.00 40.86 ? 1002 NAG B C7  1 
HETATM 6859 C C8  . NAG G 2 .   ? 45.267  -30.157 -7.576  1.00 38.90 ? 1002 NAG B C8  1 
HETATM 6860 N N2  . NAG G 2 .   ? 44.248  -30.797 -9.661  1.00 42.27 ? 1002 NAG B N2  1 
HETATM 6861 O O3  . NAG G 2 .   ? 43.357  -33.436 -10.332 1.00 45.08 ? 1002 NAG B O3  1 
HETATM 6862 O O4  . NAG G 2 .   ? 42.203  -33.883 -12.933 1.00 44.91 ? 1002 NAG B O4  1 
HETATM 6863 O O5  . NAG G 2 .   ? 41.749  -30.287 -12.301 1.00 39.29 ? 1002 NAG B O5  1 
HETATM 6864 O O6  . NAG G 2 .   ? 39.387  -31.581 -13.209 1.00 39.96 ? 1002 NAG B O6  1 
HETATM 6865 O O7  . NAG G 2 .   ? 42.897  -30.387 -7.893  1.00 38.66 ? 1002 NAG B O7  1 
HETATM 6866 C C1  . NAG H 2 .   ? 38.661  -6.553  5.478   1.00 23.37 ? 1003 NAG B C1  1 
HETATM 6867 C C2  . NAG H 2 .   ? 39.726  -6.161  4.441   1.00 24.62 ? 1003 NAG B C2  1 
HETATM 6868 C C3  . NAG H 2 .   ? 40.959  -7.025  4.482   1.00 26.31 ? 1003 NAG B C3  1 
HETATM 6869 C C4  . NAG H 2 .   ? 41.443  -7.225  5.915   1.00 27.25 ? 1003 NAG B C4  1 
HETATM 6870 C C5  . NAG H 2 .   ? 40.327  -7.636  6.867   1.00 26.27 ? 1003 NAG B C5  1 
HETATM 6871 C C6  . NAG H 2 .   ? 40.936  -7.727  8.273   1.00 26.29 ? 1003 NAG B C6  1 
HETATM 6872 C C7  . NAG H 2 .   ? 38.709  -5.238  2.533   1.00 27.35 ? 1003 NAG B C7  1 
HETATM 6873 C C8  . NAG H 2 .   ? 38.172  -5.468  1.161   1.00 25.75 ? 1003 NAG B C8  1 
HETATM 6874 N N2  . NAG H 2 .   ? 39.217  -6.308  3.118   1.00 25.30 ? 1003 NAG B N2  1 
HETATM 6875 O O3  . NAG H 2 .   ? 41.932  -6.348  3.698   1.00 31.21 ? 1003 NAG B O3  1 
HETATM 6876 O O4  . NAG H 2 .   ? 42.453  -8.227  5.939   1.00 31.14 ? 1003 NAG B O4  1 
HETATM 6877 O O5  . NAG H 2 .   ? 39.216  -6.735  6.784   1.00 25.16 ? 1003 NAG B O5  1 
HETATM 6878 O O6  . NAG H 2 .   ? 39.965  -8.168  9.215   1.00 25.44 ? 1003 NAG B O6  1 
HETATM 6879 O O7  . NAG H 2 .   ? 38.669  -4.134  3.089   1.00 26.42 ? 1003 NAG B O7  1 
HETATM 6880 O O   . HOH I 3 .   ? -7.055  8.136   32.310  1.00 29.96 ? 445  HOH A O   1 
HETATM 6881 O O   . HOH I 3 .   ? -5.608  4.881   45.191  1.00 26.35 ? 446  HOH A O   1 
HETATM 6882 O O   . HOH I 3 .   ? 18.435  11.948  44.966  1.00 29.92 ? 447  HOH A O   1 
HETATM 6883 O O   . HOH I 3 .   ? -11.694 -3.604  54.099  1.00 24.64 ? 448  HOH A O   1 
HETATM 6884 O O   . HOH I 3 .   ? -21.575 13.679  23.720  1.00 22.67 ? 449  HOH A O   1 
HETATM 6885 O O   . HOH I 3 .   ? -8.794  -4.097  29.160  1.00 13.99 ? 450  HOH A O   1 
HETATM 6886 O O   . HOH I 3 .   ? -9.563  17.033  25.747  1.00 34.81 ? 451  HOH A O   1 
HETATM 6887 O O   . HOH I 3 .   ? -10.291 -7.794  23.620  1.00 18.84 ? 452  HOH A O   1 
HETATM 6888 O O   . HOH I 3 .   ? -18.568 0.550   58.036  1.00 35.37 ? 453  HOH A O   1 
HETATM 6889 O O   . HOH I 3 .   ? -18.157 7.679   9.921   1.00 26.95 ? 454  HOH A O   1 
HETATM 6890 O O   . HOH I 3 .   ? 13.480  0.657   48.636  1.00 23.10 ? 455  HOH A O   1 
HETATM 6891 O O   . HOH I 3 .   ? 15.820  6.432   21.111  1.00 29.69 ? 456  HOH A O   1 
HETATM 6892 O O   . HOH I 3 .   ? -22.351 15.837  26.038  1.00 27.63 ? 457  HOH A O   1 
HETATM 6893 O O   . HOH I 3 .   ? -7.169  0.496   18.213  1.00 21.24 ? 458  HOH A O   1 
HETATM 6894 O O   . HOH I 3 .   ? -29.478 -2.421  20.827  1.00 17.58 ? 459  HOH A O   1 
HETATM 6895 O O   . HOH I 3 .   ? -32.589 -1.497  36.526  1.00 20.91 ? 460  HOH A O   1 
HETATM 6896 O O   . HOH I 3 .   ? 9.503   10.786  18.237  1.00 36.00 ? 461  HOH A O   1 
HETATM 6897 O O   . HOH I 3 .   ? -28.547 -7.525  27.734  1.00 27.16 ? 462  HOH A O   1 
HETATM 6898 O O   . HOH I 3 .   ? -27.482 -6.279  39.292  1.00 20.20 ? 463  HOH A O   1 
HETATM 6899 O O   . HOH I 3 .   ? -18.596 0.461   42.823  1.00 10.16 ? 464  HOH A O   1 
HETATM 6900 O O   . HOH I 3 .   ? -12.890 2.074   56.074  1.00 26.80 ? 465  HOH A O   1 
HETATM 6901 O O   . HOH I 3 .   ? -29.745 12.791  42.163  1.00 19.43 ? 466  HOH A O   1 
HETATM 6902 O O   . HOH I 3 .   ? -17.590 -9.945  42.409  1.00 20.60 ? 467  HOH A O   1 
HETATM 6903 O O   . HOH I 3 .   ? 14.516  -1.357  25.374  1.00 37.98 ? 468  HOH A O   1 
HETATM 6904 O O   . HOH I 3 .   ? -26.883 3.467   32.556  1.00 23.55 ? 469  HOH A O   1 
HETATM 6905 O O   . HOH I 3 .   ? -35.174 -2.687  28.999  1.00 17.13 ? 470  HOH A O   1 
HETATM 6906 O O   . HOH I 3 .   ? 18.983  20.839  42.492  1.00 17.22 ? 471  HOH A O   1 
HETATM 6907 O O   . HOH I 3 .   ? -33.638 -3.740  25.396  1.00 27.79 ? 472  HOH A O   1 
HETATM 6908 O O   . HOH I 3 .   ? 2.009   19.325  27.742  1.00 20.20 ? 473  HOH A O   1 
HETATM 6909 O O   . HOH I 3 .   ? 22.372  7.317   29.584  1.00 28.03 ? 474  HOH A O   1 
HETATM 6910 O O   . HOH I 3 .   ? -31.422 -6.331  20.876  1.00 14.53 ? 475  HOH A O   1 
HETATM 6911 O O   . HOH I 3 .   ? 16.410  18.879  40.055  1.00 20.08 ? 476  HOH A O   1 
HETATM 6912 O O   . HOH I 3 .   ? -16.516 -4.976  54.252  1.00 25.80 ? 477  HOH A O   1 
HETATM 6913 O O   . HOH I 3 .   ? 1.313   -8.745  21.132  1.00 20.50 ? 478  HOH A O   1 
HETATM 6914 O O   . HOH I 3 .   ? -18.191 1.069   39.203  1.00 16.26 ? 479  HOH A O   1 
HETATM 6915 O O   . HOH I 3 .   ? -22.922 5.611   36.853  1.00 19.27 ? 480  HOH A O   1 
HETATM 6916 O O   . HOH I 3 .   ? -28.726 7.688   43.525  1.00 36.19 ? 481  HOH A O   1 
HETATM 6917 O O   . HOH I 3 .   ? -17.896 11.212  41.229  1.00 29.83 ? 482  HOH A O   1 
HETATM 6918 O O   . HOH I 3 .   ? -12.226 -3.755  47.877  1.00 29.04 ? 483  HOH A O   1 
HETATM 6919 O O   . HOH I 3 .   ? -27.896 -15.618 25.902  1.00 29.15 ? 484  HOH A O   1 
HETATM 6920 O O   . HOH I 3 .   ? -17.657 -16.342 39.146  1.00 19.97 ? 485  HOH A O   1 
HETATM 6921 O O   . HOH I 3 .   ? 26.018  12.242  18.305  1.00 32.30 ? 486  HOH A O   1 
HETATM 6922 O O   . HOH I 3 .   ? 11.932  28.233  20.513  1.00 32.55 ? 487  HOH A O   1 
HETATM 6923 O O   . HOH I 3 .   ? -9.468  -5.601  19.994  1.00 14.75 ? 488  HOH A O   1 
HETATM 6924 O O   . HOH I 3 .   ? -4.074  20.709  23.539  1.00 31.23 ? 489  HOH A O   1 
HETATM 6925 O O   . HOH I 3 .   ? 21.871  -0.029  33.003  1.00 26.68 ? 490  HOH A O   1 
HETATM 6926 O O   . HOH I 3 .   ? -26.006 3.309   44.378  1.00 23.61 ? 491  HOH A O   1 
HETATM 6927 O O   . HOH I 3 .   ? -34.504 -5.156  22.276  1.00 29.03 ? 492  HOH A O   1 
HETATM 6928 O O   . HOH I 3 .   ? -10.185 12.410  11.327  1.00 32.21 ? 493  HOH A O   1 
HETATM 6929 O O   . HOH I 3 .   ? -10.867 -7.347  12.785  1.00 19.41 ? 494  HOH A O   1 
HETATM 6930 O O   . HOH I 3 .   ? -26.638 11.591  22.046  1.00 23.82 ? 495  HOH A O   1 
HETATM 6931 O O   . HOH I 3 .   ? -23.869 0.848   27.631  1.00 22.27 ? 496  HOH A O   1 
HETATM 6932 O O   . HOH I 3 .   ? -7.823  5.871   53.157  1.00 34.84 ? 497  HOH A O   1 
HETATM 6933 O O   . HOH I 3 .   ? 14.638  2.299   24.042  1.00 19.62 ? 498  HOH A O   1 
HETATM 6934 O O   . HOH I 3 .   ? -10.890 0.717   22.365  1.00 12.30 ? 499  HOH A O   1 
HETATM 6935 O O   . HOH I 3 .   ? -3.599  4.445   15.977  1.00 30.19 ? 500  HOH A O   1 
HETATM 6936 O O   . HOH I 3 .   ? -20.065 -3.332  52.256  1.00 25.83 ? 501  HOH A O   1 
HETATM 6937 O O   . HOH I 3 .   ? 7.591   -5.350  33.457  1.00 26.31 ? 502  HOH A O   1 
HETATM 6938 O O   . HOH I 3 .   ? -4.428  -8.826  28.788  1.00 17.83 ? 503  HOH A O   1 
HETATM 6939 O O   . HOH I 3 .   ? -22.964 7.130   13.146  1.00 39.55 ? 504  HOH A O   1 
HETATM 6940 O O   . HOH I 3 .   ? -14.126 -14.074 36.875  1.00 19.55 ? 505  HOH A O   1 
HETATM 6941 O O   . HOH I 3 .   ? -12.944 -19.705 24.080  1.00 25.08 ? 506  HOH A O   1 
HETATM 6942 O O   . HOH I 3 .   ? -34.835 1.611   25.809  1.00 30.61 ? 507  HOH A O   1 
HETATM 6943 O O   . HOH I 3 .   ? 5.974   7.708   35.790  1.00 40.37 ? 508  HOH A O   1 
HETATM 6944 O O   . HOH I 3 .   ? -12.680 -15.869 29.718  1.00 19.11 ? 509  HOH A O   1 
HETATM 6945 O O   . HOH I 3 .   ? -28.159 1.522   9.369   1.00 34.06 ? 510  HOH A O   1 
HETATM 6946 O O   . HOH I 3 .   ? -35.650 9.478   39.117  1.00 32.82 ? 511  HOH A O   1 
HETATM 6947 O O   . HOH I 3 .   ? -16.882 15.190  21.253  1.00 21.31 ? 512  HOH A O   1 
HETATM 6948 O O   . HOH I 3 .   ? 2.787   -2.361  32.948  1.00 19.27 ? 513  HOH A O   1 
HETATM 6949 O O   . HOH I 3 .   ? -20.149 -21.936 14.869  1.00 26.91 ? 514  HOH A O   1 
HETATM 6950 O O   . HOH I 3 .   ? -28.039 -10.352 14.149  1.00 18.71 ? 515  HOH A O   1 
HETATM 6951 O O   . HOH I 3 .   ? -16.795 3.918   4.884   1.00 33.98 ? 516  HOH A O   1 
HETATM 6952 O O   . HOH I 3 .   ? 26.326  22.480  25.899  1.00 38.61 ? 517  HOH A O   1 
HETATM 6953 O O   . HOH I 3 .   ? -15.997 -13.802 18.823  1.00 34.54 ? 518  HOH A O   1 
HETATM 6954 O O   . HOH I 3 .   ? -29.124 8.803   12.858  1.00 30.59 ? 519  HOH A O   1 
HETATM 6955 O O   . HOH I 3 .   ? -4.494  2.945   11.631  1.00 32.64 ? 520  HOH A O   1 
HETATM 6956 O O   . HOH I 3 .   ? 11.041  26.936  18.177  1.00 23.14 ? 521  HOH A O   1 
HETATM 6957 O O   . HOH I 3 .   ? 3.944   -5.784  30.975  1.00 30.51 ? 522  HOH A O   1 
HETATM 6958 O O   . HOH I 3 .   ? -2.764  1.696   16.561  1.00 24.33 ? 523  HOH A O   1 
HETATM 6959 O O   . HOH I 3 .   ? -18.093 15.361  33.480  1.00 19.24 ? 524  HOH A O   1 
HETATM 6960 O O   . HOH I 3 .   ? 30.483  11.056  24.147  1.00 28.14 ? 525  HOH A O   1 
HETATM 6961 O O   . HOH I 3 .   ? -24.239 -22.942 25.146  1.00 25.74 ? 526  HOH A O   1 
HETATM 6962 O O   . HOH I 3 .   ? 10.426  -7.027  20.908  1.00 38.24 ? 527  HOH A O   1 
HETATM 6963 O O   . HOH I 3 .   ? -19.999 -12.269 13.520  1.00 25.20 ? 528  HOH A O   1 
HETATM 6964 O O   . HOH I 3 .   ? 0.895   -18.408 35.002  1.00 34.71 ? 529  HOH A O   1 
HETATM 6965 O O   . HOH I 3 .   ? -8.312  -9.657  43.431  1.00 26.00 ? 530  HOH A O   1 
HETATM 6966 O O   . HOH I 3 .   ? 3.964   -8.231  35.139  1.00 19.06 ? 531  HOH A O   1 
HETATM 6967 O O   . HOH I 3 .   ? -30.392 -19.836 27.034  1.00 23.98 ? 532  HOH A O   1 
HETATM 6968 O O   . HOH I 3 .   ? -19.336 7.814   41.879  1.00 24.29 ? 533  HOH A O   1 
HETATM 6969 O O   . HOH I 3 .   ? -25.073 -0.211  6.066   1.00 31.50 ? 534  HOH A O   1 
HETATM 6970 O O   . HOH I 3 .   ? -5.125  -13.788 37.650  1.00 46.42 ? 535  HOH A O   1 
HETATM 6971 O O   . HOH I 3 .   ? -19.386 -11.708 6.895   1.00 25.46 ? 536  HOH A O   1 
HETATM 6972 O O   . HOH I 3 .   ? -29.810 -14.684 28.268  1.00 36.29 ? 537  HOH A O   1 
HETATM 6973 O O   . HOH I 3 .   ? -13.822 12.992  18.380  1.00 34.35 ? 538  HOH A O   1 
HETATM 6974 O O   . HOH I 3 .   ? -1.375  6.969   46.902  1.00 35.60 ? 539  HOH A O   1 
HETATM 6975 O O   . HOH I 3 .   ? 5.076   -7.403  32.840  1.00 27.39 ? 540  HOH A O   1 
HETATM 6976 O O   . HOH I 3 .   ? -2.298  -3.877  25.308  1.00 26.36 ? 541  HOH A O   1 
HETATM 6977 O O   . HOH I 3 .   ? -5.709  -14.049 34.416  1.00 35.56 ? 542  HOH A O   1 
HETATM 6978 O O   . HOH I 3 .   ? -6.578  -9.796  17.359  1.00 29.58 ? 543  HOH A O   1 
HETATM 6979 O O   . HOH I 3 .   ? 17.923  16.820  43.705  1.00 22.95 ? 544  HOH A O   1 
HETATM 6980 O O   . HOH I 3 .   ? -26.021 -20.847 40.734  1.00 25.73 ? 545  HOH A O   1 
HETATM 6981 O O   . HOH I 3 .   ? 0.708   6.756   43.154  1.00 37.37 ? 546  HOH A O   1 
HETATM 6982 O O   . HOH I 3 .   ? 0.527   -14.437 40.842  1.00 34.66 ? 547  HOH A O   1 
HETATM 6983 O O   . HOH I 3 .   ? 18.776  30.147  35.344  1.00 30.49 ? 548  HOH A O   1 
HETATM 6984 O O   . HOH I 3 .   ? -25.404 3.835   36.502  1.00 28.85 ? 549  HOH A O   1 
HETATM 6985 O O   . HOH I 3 .   ? -31.550 1.476   39.271  1.00 35.16 ? 550  HOH A O   1 
HETATM 6986 O O   . HOH I 3 .   ? 7.497   16.172  41.897  1.00 33.98 ? 551  HOH A O   1 
HETATM 6987 O O   . HOH I 3 .   ? 7.478   24.967  32.086  1.00 32.41 ? 552  HOH A O   1 
HETATM 6988 O O   . HOH I 3 .   ? -18.489 17.149  20.344  1.00 35.68 ? 553  HOH A O   1 
HETATM 6989 O O   . HOH I 3 .   ? 0.577   -18.190 32.302  1.00 30.75 ? 554  HOH A O   1 
HETATM 6990 O O   . HOH I 3 .   ? -26.549 4.524   20.426  1.00 36.27 ? 555  HOH A O   1 
HETATM 6991 O O   . HOH I 3 .   ? -25.656 2.375   7.953   1.00 24.85 ? 556  HOH A O   1 
HETATM 6992 O O   . HOH I 3 .   ? -10.454 -9.946  19.428  1.00 33.30 ? 557  HOH A O   1 
HETATM 6993 O O   . HOH I 3 .   ? 15.792  27.643  29.551  1.00 39.08 ? 558  HOH A O   1 
HETATM 6994 O O   . HOH I 3 .   ? -30.893 11.461  32.114  1.00 38.74 ? 559  HOH A O   1 
HETATM 6995 O O   . HOH I 3 .   ? -19.732 -20.183 40.703  1.00 18.03 ? 560  HOH A O   1 
HETATM 6996 O O   . HOH I 3 .   ? 28.396  6.943   32.282  1.00 27.78 ? 561  HOH A O   1 
HETATM 6997 O O   . HOH I 3 .   ? 11.411  -12.995 34.288  1.00 30.25 ? 562  HOH A O   1 
HETATM 6998 O O   . HOH I 3 .   ? -30.418 -1.227  42.271  1.00 26.51 ? 563  HOH A O   1 
HETATM 6999 O O   . HOH I 3 .   ? -20.095 -8.970  5.952   1.00 43.03 ? 564  HOH A O   1 
HETATM 7000 O O   . HOH I 3 .   ? 8.468   -1.717  49.774  1.00 31.04 ? 565  HOH A O   1 
HETATM 7001 O O   . HOH I 3 .   ? -21.914 -2.974  32.928  1.00 44.30 ? 566  HOH A O   1 
HETATM 7002 O O   . HOH I 3 .   ? -28.728 -12.817 20.831  1.00 24.92 ? 567  HOH A O   1 
HETATM 7003 O O   . HOH I 3 .   ? -36.563 -8.536  34.714  1.00 37.70 ? 568  HOH A O   1 
HETATM 7004 O O   . HOH I 3 .   ? 19.054  2.513   42.205  1.00 33.04 ? 569  HOH A O   1 
HETATM 7005 O O   . HOH I 3 .   ? -30.824 -1.883  16.834  1.00 25.53 ? 570  HOH A O   1 
HETATM 7006 O O   . HOH I 3 .   ? 4.073   -12.244 44.048  1.00 38.53 ? 571  HOH A O   1 
HETATM 7007 O O   . HOH I 3 .   ? -14.865 16.533  38.660  1.00 19.72 ? 572  HOH A O   1 
HETATM 7008 O O   . HOH I 3 .   ? -35.478 4.995   24.639  1.00 35.67 ? 573  HOH A O   1 
HETATM 7009 O O   . HOH I 3 .   ? -2.174  4.692   13.827  1.00 20.18 ? 574  HOH A O   1 
HETATM 7010 O O   . HOH I 3 .   ? -13.788 -28.101 29.566  1.00 25.17 ? 575  HOH A O   1 
HETATM 7011 O O   . HOH I 3 .   ? -29.759 -21.724 19.841  1.00 34.49 ? 576  HOH A O   1 
HETATM 7012 O O   . HOH I 3 .   ? 25.948  16.837  36.883  1.00 30.13 ? 577  HOH A O   1 
HETATM 7013 O O   . HOH I 3 .   ? -23.253 -14.158 16.405  1.00 32.13 ? 578  HOH A O   1 
HETATM 7014 O O   . HOH I 3 .   ? -15.724 11.576  15.687  1.00 29.11 ? 579  HOH A O   1 
HETATM 7015 O O   . HOH I 3 .   ? 2.104   8.764   50.617  1.00 26.35 ? 580  HOH A O   1 
HETATM 7016 O O   . HOH I 3 .   ? 29.556  24.189  26.864  1.00 28.99 ? 581  HOH A O   1 
HETATM 7017 O O   . HOH I 3 .   ? 0.182   -15.390 32.286  1.00 30.02 ? 582  HOH A O   1 
HETATM 7018 O O   . HOH I 3 .   ? -14.692 6.923   44.849  1.00 30.11 ? 583  HOH A O   1 
HETATM 7019 O O   . HOH I 3 .   ? -29.750 -20.128 32.411  1.00 34.73 ? 584  HOH A O   1 
HETATM 7020 O O   . HOH I 3 .   ? 7.789   -15.551 32.196  1.00 43.20 ? 585  HOH A O   1 
HETATM 7021 O O   . HOH I 3 .   ? -25.377 -1.617  14.104  1.00 27.34 ? 586  HOH A O   1 
HETATM 7022 O O   . HOH I 3 .   ? -25.644 -5.241  45.076  1.00 23.86 ? 587  HOH A O   1 
HETATM 7023 O O   . HOH I 3 .   ? -29.333 -13.035 25.245  1.00 39.35 ? 588  HOH A O   1 
HETATM 7024 O O   . HOH I 3 .   ? -5.419  -13.249 44.683  1.00 23.23 ? 589  HOH A O   1 
HETATM 7025 O O   . HOH I 3 .   ? -15.547 -23.450 40.338  1.00 28.61 ? 590  HOH A O   1 
HETATM 7026 O O   . HOH I 3 .   ? -0.242  7.051   36.023  1.00 36.52 ? 591  HOH A O   1 
HETATM 7027 O O   . HOH I 3 .   ? -29.501 0.945   41.191  1.00 38.36 ? 592  HOH A O   1 
HETATM 7028 O O   . HOH I 3 .   ? -14.578 -10.190 42.980  1.00 34.59 ? 593  HOH A O   1 
HETATM 7029 O O   . HOH I 3 .   ? -28.062 -1.035  30.019  1.00 22.59 ? 594  HOH A O   1 
HETATM 7030 O O   . HOH I 3 .   ? -18.476 -13.063 16.926  1.00 45.08 ? 595  HOH A O   1 
HETATM 7031 O O   . HOH I 3 .   ? 9.602   -5.908  25.303  1.00 46.14 ? 596  HOH A O   1 
HETATM 7032 O O   . HOH I 3 .   ? -30.536 -17.726 21.013  1.00 26.51 ? 597  HOH A O   1 
HETATM 7033 O O   . HOH I 3 .   ? -12.186 -8.569  47.413  1.00 36.89 ? 598  HOH A O   1 
HETATM 7034 O O   . HOH I 3 .   ? -33.723 -0.017  8.181   1.00 29.24 ? 599  HOH A O   1 
HETATM 7035 O O   . HOH I 3 .   ? -32.210 -16.830 30.051  1.00 29.57 ? 600  HOH A O   1 
HETATM 7036 O O   . HOH I 3 .   ? 10.382  -1.359  48.081  1.00 36.16 ? 601  HOH A O   1 
HETATM 7037 O O   . HOH I 3 .   ? -9.731  15.187  23.468  1.00 32.43 ? 602  HOH A O   1 
HETATM 7038 O O   . HOH I 3 .   ? -27.246 -6.199  48.496  1.00 34.30 ? 603  HOH A O   1 
HETATM 7039 O O   . HOH I 3 .   ? -27.994 -15.905 36.903  1.00 23.40 ? 604  HOH A O   1 
HETATM 7040 O O   . HOH I 3 .   ? 0.575   8.175   12.178  1.00 33.14 ? 605  HOH A O   1 
HETATM 7041 O O   . HOH I 3 .   ? -34.306 8.503   33.817  1.00 28.30 ? 606  HOH A O   1 
HETATM 7042 O O   . HOH I 3 .   ? -18.360 12.477  15.526  1.00 16.58 ? 607  HOH A O   1 
HETATM 7043 O O   . HOH I 3 .   ? -10.978 -10.137 16.364  1.00 29.52 ? 608  HOH A O   1 
HETATM 7044 O O   . HOH I 3 .   ? -12.933 -8.499  44.579  1.00 30.98 ? 609  HOH A O   1 
HETATM 7045 O O   . HOH I 3 .   ? 9.041   -3.923  51.710  1.00 27.07 ? 610  HOH A O   1 
HETATM 7046 O O   . HOH I 3 .   ? -10.662 15.775  21.077  1.00 20.62 ? 611  HOH A O   1 
HETATM 7047 O O   . HOH I 3 .   ? -31.745 -20.337 21.663  1.00 44.34 ? 612  HOH A O   1 
HETATM 7048 O O   . HOH I 3 .   ? -9.371  18.065  19.598  1.00 22.60 ? 613  HOH A O   1 
HETATM 7049 O O   . HOH J 3 .   ? 26.024  -26.780 3.263   1.00 29.52 ? 445  HOH B O   1 
HETATM 7050 O O   . HOH J 3 .   ? 10.622  -21.445 -2.121  1.00 21.34 ? 446  HOH B O   1 
HETATM 7051 O O   . HOH J 3 .   ? 23.435  -9.644  4.601   1.00 37.78 ? 447  HOH B O   1 
HETATM 7052 O O   . HOH J 3 .   ? 14.477  -19.785 -4.443  1.00 13.34 ? 448  HOH B O   1 
HETATM 7053 O O   . HOH J 3 .   ? 24.857  -15.429 -0.147  1.00 20.20 ? 449  HOH B O   1 
HETATM 7054 O O   . HOH J 3 .   ? 43.279  -11.455 -12.413 1.00 31.25 ? 450  HOH B O   1 
HETATM 7055 O O   . HOH J 3 .   ? 39.275  -9.108  2.568   1.00 30.17 ? 451  HOH B O   1 
HETATM 7056 O O   . HOH J 3 .   ? 22.616  -36.156 -2.893  1.00 30.61 ? 452  HOH B O   1 
HETATM 7057 O O   . HOH J 3 .   ? 13.527  -26.950 -18.324 1.00 23.66 ? 453  HOH B O   1 
HETATM 7058 O O   . HOH J 3 .   ? 43.742  -17.617 -16.226 1.00 19.98 ? 454  HOH B O   1 
HETATM 7059 O O   . HOH J 3 .   ? 0.308   -27.280 13.245  1.00 29.92 ? 455  HOH B O   1 
HETATM 7060 O O   . HOH J 3 .   ? 8.862   -18.182 17.534  1.00 28.77 ? 456  HOH B O   1 
HETATM 7061 O O   . HOH J 3 .   ? 12.164  -10.180 -17.285 1.00 25.68 ? 457  HOH B O   1 
HETATM 7062 O O   . HOH J 3 .   ? 47.122  -26.563 -9.062  1.00 29.15 ? 458  HOH B O   1 
HETATM 7063 O O   . HOH J 3 .   ? 37.112  -23.156 -13.555 1.00 25.13 ? 459  HOH B O   1 
HETATM 7064 O O   . HOH J 3 .   ? 15.660  -21.252 -25.483 1.00 24.75 ? 460  HOH B O   1 
HETATM 7065 O O   . HOH J 3 .   ? 41.627  -19.909 -0.883  1.00 2.05  ? 461  HOH B O   1 
HETATM 7066 O O   . HOH J 3 .   ? 20.979  -11.585 -4.360  1.00 13.83 ? 462  HOH B O   1 
HETATM 7067 O O   . HOH J 3 .   ? 15.199  -9.006  -8.813  1.00 21.56 ? 463  HOH B O   1 
HETATM 7068 O O   . HOH J 3 .   ? 2.796   -44.141 14.167  1.00 34.51 ? 464  HOH B O   1 
HETATM 7069 O O   . HOH J 3 .   ? 25.357  -20.885 -28.204 1.00 22.15 ? 465  HOH B O   1 
HETATM 7070 O O   . HOH J 3 .   ? 5.361   -29.992 9.960   1.00 21.93 ? 466  HOH B O   1 
HETATM 7071 O O   . HOH J 3 .   ? 35.940  -18.026 -15.958 1.00 13.50 ? 467  HOH B O   1 
HETATM 7072 O O   . HOH J 3 .   ? 7.931   -21.818 -10.063 1.00 17.05 ? 468  HOH B O   1 
HETATM 7073 O O   . HOH J 3 .   ? 31.178  -18.587 -21.615 1.00 19.24 ? 469  HOH B O   1 
HETATM 7074 O O   . HOH J 3 .   ? 45.316  -19.871 -10.724 1.00 25.88 ? 470  HOH B O   1 
HETATM 7075 O O   . HOH J 3 .   ? 43.760  -33.835 -7.464  1.00 27.59 ? 471  HOH B O   1 
HETATM 7076 O O   . HOH J 3 .   ? 29.472  -1.445  -22.763 1.00 26.79 ? 472  HOH B O   1 
HETATM 7077 O O   . HOH J 3 .   ? 34.068  -5.062  -0.481  1.00 19.48 ? 473  HOH B O   1 
HETATM 7078 O O   . HOH J 3 .   ? 25.276  -4.791  -22.209 1.00 29.21 ? 474  HOH B O   1 
HETATM 7079 O O   . HOH J 3 .   ? 40.998  -11.148 -21.868 1.00 32.35 ? 475  HOH B O   1 
HETATM 7080 O O   . HOH J 3 .   ? 39.648  -30.757 -1.003  1.00 31.02 ? 476  HOH B O   1 
HETATM 7081 O O   . HOH J 3 .   ? 13.841  -3.678  -2.442  1.00 24.51 ? 477  HOH B O   1 
HETATM 7082 O O   . HOH J 3 .   ? 46.238  -22.773 -6.271  1.00 17.84 ? 478  HOH B O   1 
HETATM 7083 O O   . HOH J 3 .   ? 28.081  -7.073  -21.713 1.00 30.03 ? 479  HOH B O   1 
HETATM 7084 O O   . HOH J 3 .   ? 19.940  -20.122 -5.416  1.00 10.48 ? 480  HOH B O   1 
HETATM 7085 O O   . HOH J 3 .   ? 31.143  -20.075 -13.198 1.00 26.86 ? 481  HOH B O   1 
HETATM 7086 O O   . HOH J 3 .   ? 26.643  -23.636 -19.423 1.00 23.51 ? 482  HOH B O   1 
HETATM 7087 O O   . HOH J 3 .   ? 18.861  -20.793 -27.285 1.00 32.72 ? 483  HOH B O   1 
HETATM 7088 O O   . HOH J 3 .   ? 21.180  -40.114 30.286  1.00 22.56 ? 484  HOH B O   1 
HETATM 7089 O O   . HOH J 3 .   ? 26.888  -33.148 -13.416 1.00 18.87 ? 485  HOH B O   1 
HETATM 7090 O O   . HOH J 3 .   ? 29.704  -5.453  8.003   1.00 34.11 ? 486  HOH B O   1 
HETATM 7091 O O   . HOH J 3 .   ? 42.357  -15.876 7.098   1.00 32.57 ? 487  HOH B O   1 
HETATM 7092 O O   . HOH J 3 .   ? 17.572  -9.619  -6.538  1.00 24.31 ? 488  HOH B O   1 
HETATM 7093 O O   . HOH J 3 .   ? 36.999  -31.196 0.497   1.00 18.25 ? 489  HOH B O   1 
HETATM 7094 O O   . HOH J 3 .   ? 36.658  -8.674  -23.130 1.00 28.68 ? 490  HOH B O   1 
HETATM 7095 O O   . HOH J 3 .   ? 47.790  -16.460 -4.165  1.00 16.18 ? 491  HOH B O   1 
HETATM 7096 O O   . HOH J 3 .   ? 30.691  4.371   -18.664 1.00 45.94 ? 492  HOH B O   1 
HETATM 7097 O O   . HOH J 3 .   ? 39.102  -25.036 -7.780  1.00 18.18 ? 493  HOH B O   1 
HETATM 7098 O O   . HOH J 3 .   ? 15.118  -29.719 4.570   1.00 24.91 ? 494  HOH B O   1 
HETATM 7099 O O   . HOH J 3 .   ? 50.398  -14.140 6.309   1.00 39.09 ? 495  HOH B O   1 
HETATM 7100 O O   . HOH J 3 .   ? 1.426   -23.483 11.870  1.00 24.43 ? 496  HOH B O   1 
HETATM 7101 O O   . HOH J 3 .   ? 40.745  -32.365 11.757  1.00 36.53 ? 497  HOH B O   1 
HETATM 7102 O O   . HOH J 3 .   ? 40.528  -9.169  -0.312  1.00 17.77 ? 498  HOH B O   1 
HETATM 7103 O O   . HOH J 3 .   ? 38.316  -19.918 -2.501  1.00 31.94 ? 499  HOH B O   1 
HETATM 7104 O O   . HOH J 3 .   ? 50.168  -16.463 3.174   1.00 29.15 ? 500  HOH B O   1 
HETATM 7105 O O   . HOH J 3 .   ? 9.289   -20.331 29.069  1.00 31.52 ? 501  HOH B O   1 
HETATM 7106 O O   . HOH J 3 .   ? 20.451  -21.892 30.302  1.00 32.71 ? 502  HOH B O   1 
HETATM 7107 O O   . HOH J 3 .   ? 21.736  -5.162  -18.852 1.00 27.64 ? 503  HOH B O   1 
HETATM 7108 O O   . HOH J 3 .   ? 16.170  1.351   -13.653 1.00 29.24 ? 504  HOH B O   1 
HETATM 7109 O O   . HOH J 3 .   ? 37.483  -3.286  -1.594  1.00 29.42 ? 505  HOH B O   1 
HETATM 7110 O O   . HOH J 3 .   ? 27.194  -3.412  -3.221  1.00 17.44 ? 506  HOH B O   1 
HETATM 7111 O O   . HOH J 3 .   ? 40.128  -23.217 -10.131 1.00 17.76 ? 507  HOH B O   1 
HETATM 7112 O O   . HOH J 3 .   ? 41.022  -26.061 3.643   1.00 20.96 ? 508  HOH B O   1 
HETATM 7113 O O   . HOH J 3 .   ? 30.124  -12.938 -23.468 1.00 21.53 ? 509  HOH B O   1 
HETATM 7114 O O   . HOH J 3 .   ? 29.852  6.371   -8.390  1.00 26.25 ? 510  HOH B O   1 
HETATM 7115 O O   . HOH J 3 .   ? 30.230  -25.546 15.662  1.00 40.68 ? 511  HOH B O   1 
HETATM 7116 O O   . HOH J 3 .   ? 35.754  -0.207  4.320   1.00 33.89 ? 512  HOH B O   1 
HETATM 7117 O O   . HOH J 3 .   ? 26.494  -17.387 -25.276 1.00 25.41 ? 513  HOH B O   1 
HETATM 7118 O O   . HOH J 3 .   ? 19.202  -44.518 14.517  1.00 22.24 ? 514  HOH B O   1 
HETATM 7119 O O   . HOH J 3 .   ? 48.096  -28.326 -16.248 1.00 35.85 ? 515  HOH B O   1 
HETATM 7120 O O   . HOH J 3 .   ? 0.986   -32.435 20.375  1.00 41.24 ? 516  HOH B O   1 
HETATM 7121 O O   . HOH J 3 .   ? 29.344  -20.440 28.884  1.00 25.46 ? 517  HOH B O   1 
HETATM 7122 O O   . HOH J 3 .   ? 9.721   -47.698 16.659  1.00 32.60 ? 518  HOH B O   1 
HETATM 7123 O O   . HOH J 3 .   ? 3.246   -33.275 7.575   1.00 30.24 ? 519  HOH B O   1 
HETATM 7124 O O   . HOH J 3 .   ? 35.618  -26.285 15.455  1.00 29.58 ? 520  HOH B O   1 
HETATM 7125 O O   . HOH J 3 .   ? 5.696   -25.666 29.323  1.00 34.67 ? 521  HOH B O   1 
HETATM 7126 O O   . HOH J 3 .   ? 11.399  -12.959 -18.354 1.00 56.00 ? 522  HOH B O   1 
HETATM 7127 O O   . HOH J 3 .   ? 36.511  -1.177  -18.599 1.00 30.24 ? 523  HOH B O   1 
HETATM 7128 O O   . HOH J 3 .   ? 9.679   -15.744 -19.763 1.00 27.97 ? 524  HOH B O   1 
HETATM 7129 O O   . HOH J 3 .   ? 4.682   -26.574 16.247  1.00 33.28 ? 525  HOH B O   1 
HETATM 7130 O O   . HOH J 3 .   ? 17.539  -15.476 3.331   1.00 18.37 ? 526  HOH B O   1 
HETATM 7131 O O   . HOH J 3 .   ? 20.988  -17.491 -21.989 1.00 16.68 ? 527  HOH B O   1 
HETATM 7132 O O   . HOH J 3 .   ? 48.002  -7.389  -2.356  1.00 40.40 ? 528  HOH B O   1 
HETATM 7133 O O   . HOH J 3 .   ? 7.033   -7.296  0.128   1.00 31.46 ? 529  HOH B O   1 
HETATM 7134 O O   . HOH J 3 .   ? 8.077   -26.483 26.072  1.00 25.28 ? 530  HOH B O   1 
HETATM 7135 O O   . HOH J 3 .   ? 41.368  -19.033 -18.635 1.00 24.53 ? 531  HOH B O   1 
HETATM 7136 O O   . HOH J 3 .   ? 43.954  -17.135 -18.831 1.00 27.52 ? 532  HOH B O   1 
HETATM 7137 O O   . HOH J 3 .   ? 43.669  -24.966 13.894  1.00 32.97 ? 533  HOH B O   1 
HETATM 7138 O O   . HOH J 3 .   ? 7.519   -21.874 -25.538 1.00 39.46 ? 534  HOH B O   1 
HETATM 7139 O O   . HOH J 3 .   ? 44.664  -31.907 1.239   1.00 48.70 ? 535  HOH B O   1 
HETATM 7140 O O   . HOH J 3 .   ? 22.202  0.329   -5.957  1.00 28.71 ? 536  HOH B O   1 
HETATM 7141 O O   . HOH J 3 .   ? 45.984  -30.095 -3.921  1.00 23.08 ? 537  HOH B O   1 
HETATM 7142 O O   . HOH J 3 .   ? 41.084  -26.941 -1.735  1.00 26.02 ? 538  HOH B O   1 
HETATM 7143 O O   . HOH J 3 .   ? 38.840  -16.498 -22.165 1.00 28.39 ? 539  HOH B O   1 
HETATM 7144 O O   . HOH J 3 .   ? 5.413   -34.290 11.503  1.00 29.53 ? 540  HOH B O   1 
HETATM 7145 O O   . HOH J 3 .   ? 22.841  -16.253 26.062  1.00 30.57 ? 541  HOH B O   1 
HETATM 7146 O O   . HOH J 3 .   ? 27.005  3.003   0.505   1.00 28.22 ? 542  HOH B O   1 
HETATM 7147 O O   . HOH J 3 .   ? 29.880  8.182   -19.362 1.00 43.35 ? 543  HOH B O   1 
HETATM 7148 O O   . HOH J 3 .   ? 19.562  -13.946 16.259  1.00 33.73 ? 544  HOH B O   1 
HETATM 7149 O O   . HOH J 3 .   ? 10.279  -5.030  7.239   1.00 34.30 ? 545  HOH B O   1 
HETATM 7150 O O   . HOH J 3 .   ? 44.194  -8.458  -13.131 1.00 46.13 ? 546  HOH B O   1 
HETATM 7151 O O   . HOH J 3 .   ? 12.828  -32.620 36.142  1.00 34.92 ? 547  HOH B O   1 
HETATM 7152 O O   . HOH J 3 .   ? 10.601  -3.191  5.537   1.00 32.12 ? 548  HOH B O   1 
HETATM 7153 O O   . HOH J 3 .   ? 37.708  -2.693  5.324   1.00 33.28 ? 549  HOH B O   1 
HETATM 7154 O O   . HOH J 3 .   ? 23.655  -35.284 -8.351  1.00 19.91 ? 550  HOH B O   1 
HETATM 7155 O O   . HOH J 3 .   ? 18.033  -6.886  -17.692 1.00 13.60 ? 551  HOH B O   1 
HETATM 7156 O O   . HOH J 3 .   ? 17.289  -13.733 -5.652  1.00 22.06 ? 552  HOH B O   1 
HETATM 7157 O O   . HOH J 3 .   ? 28.609  -7.734  16.434  1.00 37.68 ? 553  HOH B O   1 
HETATM 7158 O O   . HOH J 3 .   ? 11.688  -12.196 -10.748 1.00 27.89 ? 554  HOH B O   1 
HETATM 7159 O O   . HOH J 3 .   ? 13.221  -24.396 32.792  1.00 32.09 ? 555  HOH B O   1 
HETATM 7160 O O   . HOH J 3 .   ? 21.324  -16.792 11.746  1.00 21.16 ? 556  HOH B O   1 
HETATM 7161 O O   . HOH J 3 .   ? 12.133  -7.999  -21.150 1.00 33.12 ? 557  HOH B O   1 
HETATM 7162 O O   . HOH J 3 .   ? 9.425   -18.706 -15.424 1.00 31.30 ? 558  HOH B O   1 
HETATM 7163 O O   . HOH J 3 .   ? 14.730  -20.359 27.804  1.00 16.55 ? 559  HOH B O   1 
HETATM 7164 O O   . HOH J 3 .   ? 4.250   -29.599 32.835  1.00 36.95 ? 560  HOH B O   1 
HETATM 7165 O O   . HOH J 3 .   ? 18.495  2.582   -17.229 1.00 28.62 ? 561  HOH B O   1 
HETATM 7166 O O   . HOH J 3 .   ? 50.490  -12.759 10.527  1.00 28.52 ? 562  HOH B O   1 
HETATM 7167 O O   . HOH J 3 .   ? 44.370  -11.362 -8.088  1.00 38.32 ? 563  HOH B O   1 
HETATM 7168 O O   . HOH J 3 .   ? 32.336  -3.670  -17.388 1.00 28.94 ? 564  HOH B O   1 
HETATM 7169 O O   . HOH J 3 .   ? 6.528   -22.161 24.354  1.00 32.66 ? 565  HOH B O   1 
HETATM 7170 O O   . HOH J 3 .   ? 41.158  -3.628  -12.066 1.00 30.14 ? 566  HOH B O   1 
HETATM 7171 O O   . HOH J 3 .   ? 45.197  -9.107  -8.948  1.00 35.77 ? 567  HOH B O   1 
HETATM 7172 O O   . HOH J 3 .   ? 17.463  -19.910 27.331  1.00 24.79 ? 568  HOH B O   1 
HETATM 7173 O O   . HOH J 3 .   ? 9.860   -9.903  -4.948  1.00 36.55 ? 569  HOH B O   1 
HETATM 7174 O O   . HOH J 3 .   ? 48.914  -21.347 -14.076 1.00 39.18 ? 570  HOH B O   1 
HETATM 7175 O O   . HOH J 3 .   ? 24.277  6.533   -11.046 1.00 36.90 ? 571  HOH B O   1 
HETATM 7176 O O   . HOH J 3 .   ? 28.422  -3.314  4.060   1.00 27.05 ? 572  HOH B O   1 
HETATM 7177 O O   . HOH J 3 .   ? 5.001   -21.000 20.266  1.00 34.85 ? 573  HOH B O   1 
HETATM 7178 O O   . HOH J 3 .   ? 5.309   -29.216 7.535   1.00 36.51 ? 574  HOH B O   1 
HETATM 7179 O O   . HOH J 3 .   ? 29.950  3.683   -15.155 1.00 26.28 ? 575  HOH B O   1 
HETATM 7180 O O   . HOH J 3 .   ? 36.999  -12.387 -26.027 1.00 32.44 ? 576  HOH B O   1 
HETATM 7181 O O   . HOH J 3 .   ? 2.352   -37.351 15.604  1.00 37.75 ? 577  HOH B O   1 
HETATM 7182 O O   . HOH J 3 .   ? 7.393   -21.611 16.882  1.00 25.40 ? 578  HOH B O   1 
HETATM 7183 O O   . HOH J 3 .   ? 31.866  -26.057 -21.598 1.00 26.29 ? 579  HOH B O   1 
HETATM 7184 O O   . HOH J 3 .   ? 54.574  -19.880 7.223   1.00 40.16 ? 580  HOH B O   1 
HETATM 7185 O O   . HOH J 3 .   ? 6.093   -34.963 8.929   1.00 30.56 ? 581  HOH B O   1 
HETATM 7186 O O   . HOH J 3 .   ? 15.537  -7.269  -16.765 1.00 19.92 ? 582  HOH B O   1 
HETATM 7187 O O   . HOH J 3 .   ? 17.831  -45.283 20.720  1.00 39.39 ? 583  HOH B O   1 
HETATM 7188 O O   . HOH J 3 .   ? 17.837  -19.133 31.610  1.00 25.59 ? 584  HOH B O   1 
HETATM 7189 O O   . HOH J 3 .   ? 42.289  -28.148 20.390  1.00 35.89 ? 585  HOH B O   1 
HETATM 7190 O O   . HOH J 3 .   ? 43.465  -30.143 21.339  1.00 18.79 ? 586  HOH B O   1 
HETATM 7191 O O   . HOH J 3 .   ? 2.786   -34.585 14.321  1.00 29.54 ? 587  HOH B O   1 
HETATM 7192 O O   . HOH J 3 .   ? 3.784   -37.537 13.180  1.00 30.62 ? 588  HOH B O   1 
HETATM 7193 O O   . HOH J 3 .   ? 6.470   -19.044 -26.124 1.00 39.99 ? 589  HOH B O   1 
HETATM 7194 O O   . HOH J 3 .   ? 18.155  5.162   -19.138 1.00 39.68 ? 590  HOH B O   1 
HETATM 7195 O O   . HOH J 3 .   ? 54.766  -17.185 5.850   1.00 24.69 ? 591  HOH B O   1 
# 
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   ALA 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   ARG 3   3   ?   ?   ?   A . n 
A 1 4   ASN 4   4   ?   ?   ?   A . n 
A 1 5   GLN 5   5   ?   ?   ?   A . n 
A 1 6   SER 6   6   ?   ?   ?   A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   CYS 8   8   8   CYS CYS A . n 
A 1 9   ASP 9   9   9   ASP ASP A . n 
A 1 10  THR 10  10  10  THR THR A . n 
A 1 11  VAL 11  11  11  VAL VAL A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  GLN 13  13  13  GLN GLN A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  TYR 15  15  15  TYR TYR A . n 
A 1 16  GLN 16  16  16  GLN GLN A . n 
A 1 17  CYS 17  17  17  CYS CYS A . n 
A 1 18  PHE 18  18  18  PHE PHE A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  HIS 23  23  23  HIS HIS A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  TRP 25  25  25  TRP TRP A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  TYR 28  28  28  TYR TYR A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  ASN 36  36  36  ASN ASN A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  VAL 44  44  44  VAL VAL A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  CYS 48  48  48  CYS CYS A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  THR 51  51  51  THR THR A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  HIS 59  59  59  HIS HIS A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  ARG 62  62  62  ARG ARG A . n 
A 1 63  TYR 63  63  63  TYR TYR A . n 
A 1 64  PRO 64  64  64  PRO PRO A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  GLN 80  80  80  GLN GLN A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  ASN 82  82  82  ASN ASN A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  PHE 86  86  86  PHE PHE A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  TYR 90  90  90  TYR TYR A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  THR 95  95  95  THR THR A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  ASN 97  97  97  ASN ASN A . n 
A 1 98  TYR 98  98  98  TYR TYR A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 PRO 107 107 107 PRO PRO A . n 
A 1 108 PHE 108 108 108 PHE PHE A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 GLN 111 111 111 GLN GLN A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 PHE 120 120 120 PHE PHE A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 GLN 122 122 122 GLN GLN A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 TYR 124 124 124 TYR TYR A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 ARG 129 129 129 ARG ARG A . n 
A 1 130 ASN 130 130 130 ASN ASN A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 ILE 135 135 135 ILE ILE A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 SER 137 137 137 SER SER A . n 
A 1 138 SER 138 138 138 SER SER A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 SER 140 140 140 SER SER A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 ARG 142 142 142 ARG ARG A . n 
A 1 143 VAL 143 143 143 VAL VAL A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 PHE 154 154 154 PHE PHE A . n 
A 1 155 GLN 155 155 155 GLN GLN A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 LYS 160 160 160 LYS LYS A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 PRO 162 162 162 PRO PRO A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 GLN 165 165 165 GLN GLN A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 GLN 168 168 168 GLN GLN A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 SER 170 170 170 SER SER A . n 
A 1 171 PRO 171 171 171 PRO PRO A . n 
A 1 172 LYS 172 172 172 LYS LYS A . n 
A 1 173 ILE 173 173 173 ILE ILE 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 VAL 176 176 176 VAL VAL A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 GLU 179 179 179 GLU GLU A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 ASN 184 184 184 ASN ASN A . n 
A 1 185 ASN 185 185 185 ASN ASN A . n 
A 1 186 THR 186 186 186 THR THR A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 PRO 189 189 189 PRO PRO A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 CYS 192 192 192 CYS CYS A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 PHE 195 195 195 PHE PHE A . n 
A 1 196 GLU 196 196 196 GLU GLU A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 ASP 202 202 202 ASP ASP A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 ASN 207 207 207 ASN ASN A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 THR 211 211 211 THR THR A . n 
A 1 212 PHE 212 212 212 PHE PHE A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 ARG 219 219 219 ARG ARG A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 ASN 222 222 222 ASN ASN A . n 
A 1 223 ASP 223 223 223 ASP ASP A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 GLY 226 226 226 GLY GLY A . n 
A 1 227 VAL 227 227 227 VAL VAL A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 THR 230 230 230 THR THR A . n 
A 1 231 ASP 231 231 231 ASP ASP A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 THR 235 235 235 THR THR A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 MET 238 238 238 MET MET A . n 
A 1 239 ASP 239 239 239 ASP ASP A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 CYS 241 241 241 CYS CYS A . n 
A 1 242 SER 242 242 242 SER SER A . n 
A 1 243 PHE 243 243 243 PHE PHE A . n 
A 1 244 ASP 244 244 244 ASP ASP A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 THR 248 248 248 THR THR A . n 
A 1 249 SER 249 249 249 SER SER A . n 
A 1 250 THR 250 250 250 THR THR A . n 
A 1 251 VAL 251 251 251 VAL VAL A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 THR 253 253 253 THR THR A . n 
A 1 254 LYS 254 254 254 LYS LYS A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 PRO 257 257 257 PRO PRO A . n 
A 1 258 PHE 258 258 258 PHE PHE A . n 
A 1 259 CYS 259 259 259 CYS CYS A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 THR 263 263 263 THR THR A . n 
A 1 264 HIS 264 264 264 HIS HIS A . n 
A 1 265 ASP 265 265 265 ASP ASP A . n 
A 1 266 GLU 266 266 266 GLU GLU A . n 
A 1 267 TRP 267 267 267 TRP TRP A . n 
A 1 268 ILE 268 268 268 ILE ILE A . n 
A 1 269 ASN 269 269 269 ASN ASN A . n 
A 1 270 TYR 270 270 270 TYR TYR A . n 
A 1 271 ASP 271 271 271 ASP ASP A . n 
A 1 272 TYR 272 272 272 TYR TYR A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 GLN 274 274 274 GLN GLN A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 LYS 278 278 278 LYS LYS A . n 
A 1 279 TYR 279 279 279 TYR TYR A . n 
A 1 280 TYR 280 280 280 TYR TYR A . n 
A 1 281 GLY 281 281 281 GLY GLY A . n 
A 1 282 HIS 282 282 282 HIS HIS A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 ALA 284 284 284 ALA ALA A . n 
A 1 285 GLY 285 285 285 GLY GLY A . n 
A 1 286 ASN 286 286 286 ASN ASN A . n 
A 1 287 PRO 287 287 287 PRO PRO A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 GLY 289 289 289 GLY GLY A . n 
A 1 290 PRO 290 290 290 PRO PRO A . n 
A 1 291 THR 291 291 291 THR THR A . n 
A 1 292 GLN 292 292 292 GLN GLN A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 VAL 294 294 294 VAL VAL A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 TYR 296 296 296 TYR TYR A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 ASN 298 298 298 ASN ASN A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 ILE 301 301 301 ILE ILE A . n 
A 1 302 ALA 302 302 302 ALA ALA A . n 
A 1 303 ARG 303 303 303 ARG ARG A . n 
A 1 304 LEU 304 304 304 LEU LEU A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 HIS 306 306 306 HIS HIS A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 PRO 308 308 308 PRO PRO A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 HIS 310 310 310 HIS HIS A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 ASP 312 312 312 ASP ASP A . n 
A 1 313 THR 313 313 313 THR THR A . n 
A 1 314 SER 314 314 314 SER SER A . n 
A 1 315 SER 315 315 315 SER SER A . n 
A 1 316 ASN 316 316 316 ASN ASN A . n 
A 1 317 HIS 317 317 317 HIS HIS A . n 
A 1 318 THR 318 318 318 THR THR A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 ASP 320 320 320 ASP ASP A . n 
A 1 321 SER 321 321 321 SER SER A . n 
A 1 322 SER 322 322 322 SER SER A . n 
A 1 323 PRO 323 323 323 PRO PRO A . n 
A 1 324 ALA 324 324 324 ALA ALA A . n 
A 1 325 THR 325 325 325 THR THR A . n 
A 1 326 PHE 326 326 326 PHE PHE A . n 
A 1 327 PRO 327 327 327 PRO PRO A . n 
A 1 328 LEU 328 328 328 LEU LEU A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 SER 330 330 330 SER SER A . n 
A 1 331 THR 331 331 331 THR THR A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 TYR 333 333 333 TYR TYR A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 ASP 335 335 335 ASP ASP A . n 
A 1 336 PHE 336 336 336 PHE PHE A . n 
A 1 337 SER 337 337 337 SER SER A . n 
A 1 338 HIS 338 338 338 HIS HIS A . n 
A 1 339 ASP 339 339 339 ASP ASP A . n 
A 1 340 ASN 340 340 340 ASN ASN A . n 
A 1 341 GLY 341 341 341 GLY GLY A . n 
A 1 342 ILE 342 342 342 ILE ILE A . n 
A 1 343 ILE 343 343 343 ILE ILE A . n 
A 1 344 SER 344 344 344 SER SER A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 PHE 347 347 347 PHE PHE A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 TYR 352 352 352 TYR TYR A . n 
A 1 353 ASN 353 353 353 ASN ASN A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 THR 355 355 355 THR THR A . n 
A 1 356 LYS 356 356 356 LYS LYS A . n 
A 1 357 PRO 357 357 357 PRO PRO A . n 
A 1 358 LEU 358 358 358 LEU LEU A . n 
A 1 359 SER 359 359 359 SER SER A . n 
A 1 360 THR 360 360 360 THR THR A . n 
A 1 361 THR 361 361 361 THR THR A . n 
A 1 362 THR 362 362 362 THR THR A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 GLU 364 364 364 GLU GLU A . n 
A 1 365 ASN 365 365 365 ASN ASN A . n 
A 1 366 ILE 366 366 366 ILE ILE A . n 
A 1 367 THR 367 367 367 THR THR A . n 
A 1 368 GLN 368 368 368 GLN GLN A . n 
A 1 369 THR 369 369 369 THR THR A . n 
A 1 370 ASP 370 370 370 ASP ASP A . n 
A 1 371 GLY 371 371 371 GLY GLY A . n 
A 1 372 PHE 372 372 372 PHE PHE A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 SER 374 374 374 SER SER A . n 
A 1 375 ALA 375 375 375 ALA ALA A . n 
A 1 376 TRP 376 376 376 TRP TRP A . n 
A 1 377 THR 377 377 377 THR THR A . n 
A 1 378 VAL 378 378 378 VAL VAL A . n 
A 1 379 PRO 379 379 379 PRO PRO A . n 
A 1 380 PHE 380 380 380 PHE PHE A . n 
A 1 381 ALA 381 381 381 ALA ALA A . n 
A 1 382 SER 382 382 382 SER SER A . n 
A 1 383 ARG 383 383 383 ARG ARG A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 TYR 385 385 385 TYR TYR A . n 
A 1 386 VAL 386 386 386 VAL VAL A . n 
A 1 387 GLU 387 387 387 GLU GLU A . n 
A 1 388 MET 388 388 388 MET MET A . n 
A 1 389 MET 389 389 389 MET MET A . n 
A 1 390 GLN 390 390 390 GLN GLN A . n 
A 1 391 CYS 391 391 391 CYS CYS A . n 
A 1 392 GLN 392 392 392 GLN GLN A . n 
A 1 393 ALA 393 393 393 ALA ALA A . n 
A 1 394 GLU 394 394 394 GLU GLU A . n 
A 1 395 GLN 395 395 395 GLN GLN A . n 
A 1 396 GLU 396 396 396 GLU GLU A . n 
A 1 397 PRO 397 397 397 PRO PRO A . n 
A 1 398 LEU 398 398 398 LEU LEU A . n 
A 1 399 VAL 399 399 399 VAL VAL A . n 
A 1 400 ARG 400 400 400 ARG ARG A . n 
A 1 401 VAL 401 401 401 VAL VAL A . n 
A 1 402 LEU 402 402 402 LEU LEU A . n 
A 1 403 VAL 403 403 403 VAL VAL A . n 
A 1 404 ASN 404 404 404 ASN ASN A . n 
A 1 405 ASP 405 405 405 ASP ASP A . n 
A 1 406 ARG 406 406 406 ARG ARG A . n 
A 1 407 VAL 407 407 407 VAL VAL A . n 
A 1 408 VAL 408 408 408 VAL VAL A . n 
A 1 409 PRO 409 409 409 PRO PRO A . n 
A 1 410 LEU 410 410 410 LEU LEU A . n 
A 1 411 HIS 411 411 411 HIS HIS A . n 
A 1 412 GLY 412 412 412 GLY GLY A . n 
A 1 413 CYS 413 413 413 CYS CYS A . n 
A 1 414 PRO 414 414 414 PRO PRO A . n 
A 1 415 VAL 415 415 415 VAL VAL A . n 
A 1 416 ASP 416 416 416 ASP ASP A . n 
A 1 417 ALA 417 417 417 ALA ALA A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 GLY 419 419 419 GLY GLY A . n 
A 1 420 ARG 420 420 420 ARG ARG A . n 
A 1 421 CYS 421 421 421 CYS CYS A . n 
A 1 422 THR 422 422 422 THR THR A . n 
A 1 423 ARG 423 423 423 ARG ARG A . n 
A 1 424 ASP 424 424 424 ASP ASP A . n 
A 1 425 SER 425 425 425 SER SER A . n 
A 1 426 PHE 426 426 426 PHE PHE A . n 
A 1 427 VAL 427 427 427 VAL VAL A . n 
A 1 428 ARG 428 428 428 ARG ARG A . n 
A 1 429 GLY 429 429 429 GLY GLY A . n 
A 1 430 LEU 430 430 430 LEU LEU A . n 
A 1 431 SER 431 431 431 SER SER A . n 
A 1 432 PHE 432 432 432 PHE PHE A . n 
A 1 433 ALA 433 433 433 ALA ALA A . n 
A 1 434 ARG 434 434 434 ARG ARG A . n 
A 1 435 SER 435 435 435 SER SER A . n 
A 1 436 GLY 436 436 436 GLY GLY A . n 
A 1 437 GLY 437 437 437 GLY GLY A . n 
A 1 438 ASP 438 438 438 ASP ASP A . n 
A 1 439 TRP 439 439 439 TRP TRP A . n 
A 1 440 ALA 440 440 440 ALA ALA A . n 
A 1 441 GLU 441 441 441 GLU GLU A . n 
A 1 442 CYS 442 442 442 CYS CYS A . n 
A 1 443 PHE 443 443 443 PHE PHE A . n 
A 1 444 ALA 444 444 444 ALA ALA A . n 
B 1 1   ALA 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   ARG 3   3   ?   ?   ?   B . n 
B 1 4   ASN 4   4   ?   ?   ?   B . n 
B 1 5   GLN 5   5   ?   ?   ?   B . n 
B 1 6   SER 6   6   ?   ?   ?   B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   CYS 8   8   8   CYS CYS B . n 
B 1 9   ASP 9   9   9   ASP ASP B . n 
B 1 10  THR 10  10  10  THR THR B . n 
B 1 11  VAL 11  11  11  VAL VAL B . n 
B 1 12  ASP 12  12  12  ASP ASP B . n 
B 1 13  GLN 13  13  13  GLN GLN B . n 
B 1 14  GLY 14  14  14  GLY GLY B . n 
B 1 15  TYR 15  15  15  TYR TYR B . n 
B 1 16  GLN 16  16  16  GLN GLN B . n 
B 1 17  CYS 17  17  17  CYS CYS B . n 
B 1 18  PHE 18  18  18  PHE PHE B . n 
B 1 19  SER 19  19  19  SER SER B . n 
B 1 20  GLU 20  20  20  GLU GLU B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  SER 22  22  22  SER SER B . n 
B 1 23  HIS 23  23  23  HIS HIS B . n 
B 1 24  LEU 24  24  24  LEU LEU B . n 
B 1 25  TRP 25  25  25  TRP TRP B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  TYR 28  28  28  TYR TYR B . n 
B 1 29  ALA 29  29  29  ALA ALA B . n 
B 1 30  PRO 30  30  30  PRO PRO B . n 
B 1 31  PHE 31  31  31  PHE PHE B . n 
B 1 32  PHE 32  32  32  PHE PHE B . n 
B 1 33  SER 33  33  33  SER SER B . n 
B 1 34  LEU 34  34  34  LEU LEU B . n 
B 1 35  ALA 35  35  35  ALA ALA B . n 
B 1 36  ASN 36  36  36  ASN ASN B . n 
B 1 37  GLU 37  37  37  GLU GLU B . n 
B 1 38  SER 38  38  38  SER SER B . n 
B 1 39  VAL 39  39  39  VAL VAL B . n 
B 1 40  ILE 40  40  40  ILE ILE B . n 
B 1 41  SER 41  41  41  SER SER B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  VAL 44  44  44  VAL VAL B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  ALA 46  46  46  ALA ALA B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  CYS 48  48  48  CYS CYS B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  VAL 50  50  50  VAL VAL B . n 
B 1 51  THR 51  51  51  THR THR B . n 
B 1 52  PHE 52  52  52  PHE PHE B . n 
B 1 53  ALA 53  53  53  ALA ALA B . n 
B 1 54  GLN 54  54  54  GLN GLN B . n 
B 1 55  VAL 55  55  55  VAL VAL B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  SER 57  57  57  SER SER B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  HIS 59  59  59  HIS HIS B . n 
B 1 60  GLY 60  60  60  GLY GLY B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  ARG 62  62  62  ARG ARG B . n 
B 1 63  TYR 63  63  63  TYR TYR B . n 
B 1 64  PRO 64  64  64  PRO PRO B . n 
B 1 65  THR 65  65  65  THR THR B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  LYS 68  68  68  LYS LYS B . n 
B 1 69  GLY 69  69  69  GLY GLY B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  LYS 71  71  71  LYS LYS B . n 
B 1 72  TYR 72  72  72  TYR TYR B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  ALA 74  74  74  ALA ALA B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ILE 76  76  76  ILE ILE B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  GLN 80  80  80  GLN GLN B . n 
B 1 81  GLN 81  81  81  GLN GLN B . n 
B 1 82  ASN 82  82  82  ASN ASN B . n 
B 1 83  ALA 83  83  83  ALA ALA B . n 
B 1 84  THR 84  84  84  THR THR B . n 
B 1 85  THR 85  85  85  THR THR B . n 
B 1 86  PHE 86  86  86  PHE PHE B . n 
B 1 87  ASP 87  87  87  ASP ASP B . n 
B 1 88  GLY 88  88  88  GLY GLY B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  TYR 90  90  90  TYR TYR B . n 
B 1 91  ALA 91  91  91  ALA ALA B . n 
B 1 92  PHE 92  92  92  PHE PHE B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  THR 95  95  95  THR THR B . n 
B 1 96  TYR 96  96  96  TYR TYR B . n 
B 1 97  ASN 97  97  97  ASN ASN B . n 
B 1 98  TYR 98  98  98  TYR TYR B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 LEU 100 100 100 LEU LEU B . n 
B 1 101 GLY 101 101 101 GLY GLY B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 ASP 104 104 104 ASP ASP B . n 
B 1 105 LEU 105 105 105 LEU LEU B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 PRO 107 107 107 PRO PRO B . n 
B 1 108 PHE 108 108 108 PHE PHE B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLU 110 110 110 GLU GLU B . n 
B 1 111 GLN 111 111 111 GLN GLN B . n 
B 1 112 GLU 112 112 112 GLU GLU B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 SER 116 116 116 SER SER B . n 
B 1 117 GLY 117 117 117 GLY GLY B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 LYS 119 119 119 LYS LYS B . n 
B 1 120 PHE 120 120 120 PHE PHE B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 GLN 122 122 122 GLN GLN B . n 
B 1 123 ARG 123 123 123 ARG ARG B . n 
B 1 124 TYR 124 124 124 TYR TYR B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 SER 126 126 126 SER SER B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 THR 128 128 128 THR THR B . n 
B 1 129 ARG 129 129 129 ARG ARG B . n 
B 1 130 ASN 130 130 130 ASN ASN B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 VAL 132 132 132 VAL VAL B . n 
B 1 133 PRO 133 133 133 PRO PRO B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 ILE 135 135 135 ILE ILE B . n 
B 1 136 ARG 136 136 136 ARG ARG B . n 
B 1 137 SER 137 137 137 SER SER B . n 
B 1 138 SER 138 138 138 SER SER B . n 
B 1 139 GLY 139 139 139 GLY GLY B . n 
B 1 140 SER 140 140 140 SER SER B . n 
B 1 141 SER 141 141 141 SER SER B . n 
B 1 142 ARG 142 142 142 ARG ARG B . n 
B 1 143 VAL 143 143 143 VAL VAL B . n 
B 1 144 ILE 144 144 144 ILE ILE B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 SER 146 146 146 SER SER B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 LYS 149 149 149 LYS LYS B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 GLU 152 152 152 GLU GLU B . n 
B 1 153 GLY 153 153 153 GLY GLY B . n 
B 1 154 PHE 154 154 154 PHE PHE B . n 
B 1 155 GLN 155 155 155 GLN GLN B . n 
B 1 156 SER 156 156 156 SER SER B . n 
B 1 157 THR 157 157 157 THR THR B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 LEU 159 159 159 LEU LEU B . n 
B 1 160 LYS 160 160 160 LYS LYS B . n 
B 1 161 ASP 161 161 161 ASP ASP B . n 
B 1 162 PRO 162 162 162 PRO PRO B . n 
B 1 163 ARG 163 163 163 ARG ARG B . n 
B 1 164 ALA 164 164 164 ALA ALA B . n 
B 1 165 GLN 165 165 165 GLN GLN B . n 
B 1 166 PRO 166 166 166 PRO PRO B . n 
B 1 167 GLY 167 167 167 GLY GLY B . n 
B 1 168 GLN 168 168 168 GLN GLN B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 SER 170 170 170 SER SER B . n 
B 1 171 PRO 171 171 171 PRO PRO B . n 
B 1 172 LYS 172 172 172 LYS LYS B . n 
B 1 173 ILE 173 173 173 ILE ILE 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 VAL 176 176 176 VAL VAL B . n 
B 1 177 ILE 177 177 177 ILE ILE B . n 
B 1 178 SER 178 178 178 SER SER B . n 
B 1 179 GLU 179 179 179 GLU GLU B . n 
B 1 180 ALA 180 180 180 ALA ALA B . n 
B 1 181 SER 181 181 181 SER SER B . n 
B 1 182 SER 182 182 182 SER SER B . n 
B 1 183 SER 183 183 183 SER SER B . n 
B 1 184 ASN 184 184 184 ASN ASN B . n 
B 1 185 ASN 185 185 185 ASN ASN B . n 
B 1 186 THR 186 186 186 THR THR B . n 
B 1 187 LEU 187 187 187 LEU LEU B . n 
B 1 188 ASP 188 188 188 ASP ASP B . n 
B 1 189 PRO 189 189 189 PRO PRO B . n 
B 1 190 GLY 190 190 190 GLY GLY B . n 
B 1 191 THR 191 191 191 THR THR B . n 
B 1 192 CYS 192 192 192 CYS CYS B . n 
B 1 193 THR 193 193 193 THR THR B . n 
B 1 194 VAL 194 194 194 VAL VAL B . n 
B 1 195 PHE 195 195 195 PHE PHE B . n 
B 1 196 GLU 196 196 196 GLU GLU B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 SER 198 198 198 SER SER B . n 
B 1 199 GLU 199 199 199 GLU GLU B . n 
B 1 200 LEU 200 200 200 LEU LEU B . n 
B 1 201 ALA 201 201 201 ALA ALA B . n 
B 1 202 ASP 202 202 202 ASP ASP B . n 
B 1 203 THR 203 203 203 THR THR B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 GLU 205 205 205 GLU GLU B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 ASN 207 207 207 ASN ASN B . n 
B 1 208 PHE 208 208 208 PHE PHE B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 THR 211 211 211 THR THR B . n 
B 1 212 PHE 212 212 212 PHE PHE B . n 
B 1 213 VAL 213 213 213 VAL VAL B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 SER 215 215 215 SER SER B . n 
B 1 216 ILE 216 216 216 ILE ILE B . n 
B 1 217 ARG 217 217 217 ARG ARG B . n 
B 1 218 GLN 218 218 218 GLN GLN B . n 
B 1 219 ARG 219 219 219 ARG ARG B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 GLU 221 221 221 GLU GLU B . n 
B 1 222 ASN 222 222 222 ASN ASN B . n 
B 1 223 ASP 223 223 223 ASP ASP B . n 
B 1 224 LEU 224 224 224 LEU LEU B . n 
B 1 225 SER 225 225 225 SER SER B . n 
B 1 226 GLY 226 226 226 GLY GLY B . n 
B 1 227 VAL 227 227 227 VAL VAL B . n 
B 1 228 THR 228 228 228 THR THR B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 THR 230 230 230 THR THR B . n 
B 1 231 ASP 231 231 231 ASP ASP B . n 
B 1 232 THR 232 232 232 THR THR B . n 
B 1 233 GLU 233 233 233 GLU GLU B . n 
B 1 234 VAL 234 234 234 VAL VAL B . n 
B 1 235 THR 235 235 235 THR THR B . n 
B 1 236 TYR 236 236 236 TYR TYR B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 MET 238 238 238 MET MET B . n 
B 1 239 ASP 239 239 239 ASP ASP B . n 
B 1 240 MET 240 240 240 MET MET B . n 
B 1 241 CYS 241 241 241 CYS CYS B . n 
B 1 242 SER 242 242 242 SER SER B . n 
B 1 243 PHE 243 243 243 PHE PHE B . n 
B 1 244 ASP 244 244 244 ASP ASP B . n 
B 1 245 THR 245 245 245 THR THR B . n 
B 1 246 ILE 246 246 246 ILE ILE B . n 
B 1 247 SER 247 247 247 SER SER B . n 
B 1 248 THR 248 248 248 THR THR B . n 
B 1 249 SER 249 249 249 SER SER B . n 
B 1 250 THR 250 250 250 THR THR B . n 
B 1 251 VAL 251 251 251 VAL VAL B . n 
B 1 252 ASP 252 252 252 ASP ASP B . n 
B 1 253 THR 253 253 253 THR THR B . n 
B 1 254 LYS 254 254 254 LYS LYS B . n 
B 1 255 LEU 255 255 255 LEU LEU B . n 
B 1 256 SER 256 256 256 SER SER B . n 
B 1 257 PRO 257 257 257 PRO PRO B . n 
B 1 258 PHE 258 258 258 PHE PHE B . n 
B 1 259 CYS 259 259 259 CYS CYS B . n 
B 1 260 ASP 260 260 260 ASP ASP B . n 
B 1 261 LEU 261 261 261 LEU LEU B . n 
B 1 262 PHE 262 262 262 PHE PHE B . n 
B 1 263 THR 263 263 263 THR THR B . n 
B 1 264 HIS 264 264 264 HIS HIS B . n 
B 1 265 ASP 265 265 265 ASP ASP B . n 
B 1 266 GLU 266 266 266 GLU GLU B . n 
B 1 267 TRP 267 267 267 TRP TRP B . n 
B 1 268 ILE 268 268 268 ILE ILE B . n 
B 1 269 ASN 269 269 269 ASN ASN B . n 
B 1 270 TYR 270 270 270 TYR TYR B . n 
B 1 271 ASP 271 271 271 ASP ASP B . n 
B 1 272 TYR 272 272 272 TYR TYR B . n 
B 1 273 LEU 273 273 273 LEU LEU B . n 
B 1 274 GLN 274 274 274 GLN GLN B . n 
B 1 275 SER 275 275 275 SER SER B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 LYS 277 277 277 LYS LYS B . n 
B 1 278 LYS 278 278 278 LYS LYS B . n 
B 1 279 TYR 279 279 279 TYR TYR B . n 
B 1 280 TYR 280 280 280 TYR TYR B . n 
B 1 281 GLY 281 281 281 GLY GLY B . n 
B 1 282 HIS 282 282 282 HIS HIS B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 ALA 284 284 284 ALA ALA B . n 
B 1 285 GLY 285 285 285 GLY GLY B . n 
B 1 286 ASN 286 286 286 ASN ASN B . n 
B 1 287 PRO 287 287 287 PRO PRO B . n 
B 1 288 LEU 288 288 288 LEU LEU B . n 
B 1 289 GLY 289 289 289 GLY GLY B . n 
B 1 290 PRO 290 290 290 PRO PRO B . n 
B 1 291 THR 291 291 291 THR THR B . n 
B 1 292 GLN 292 292 292 GLN GLN B . n 
B 1 293 GLY 293 293 293 GLY GLY B . n 
B 1 294 VAL 294 294 294 VAL VAL B . n 
B 1 295 GLY 295 295 295 GLY GLY B . n 
B 1 296 TYR 296 296 296 TYR TYR B . n 
B 1 297 ALA 297 297 297 ALA ALA B . n 
B 1 298 ASN 298 298 298 ASN ASN B . n 
B 1 299 GLU 299 299 299 GLU GLU B . n 
B 1 300 LEU 300 300 300 LEU LEU B . n 
B 1 301 ILE 301 301 301 ILE ILE B . n 
B 1 302 ALA 302 302 302 ALA ALA B . n 
B 1 303 ARG 303 303 303 ARG ARG B . n 
B 1 304 LEU 304 304 304 LEU LEU B . n 
B 1 305 THR 305 305 305 THR THR B . n 
B 1 306 HIS 306 306 306 HIS HIS B . n 
B 1 307 SER 307 307 307 SER SER B . n 
B 1 308 PRO 308 308 308 PRO PRO B . n 
B 1 309 VAL 309 309 309 VAL VAL B . n 
B 1 310 HIS 310 310 310 HIS HIS B . n 
B 1 311 ASP 311 311 311 ASP ASP B . n 
B 1 312 ASP 312 312 312 ASP ASP B . n 
B 1 313 THR 313 313 313 THR THR B . n 
B 1 314 SER 314 314 314 SER SER B . n 
B 1 315 SER 315 315 315 SER SER B . n 
B 1 316 ASN 316 316 316 ASN ASN B . n 
B 1 317 HIS 317 317 317 HIS HIS B . n 
B 1 318 THR 318 318 318 THR THR B . n 
B 1 319 LEU 319 319 319 LEU LEU B . n 
B 1 320 ASP 320 320 320 ASP ASP B . n 
B 1 321 SER 321 321 321 SER SER B . n 
B 1 322 SER 322 322 322 SER SER B . n 
B 1 323 PRO 323 323 323 PRO PRO B . n 
B 1 324 ALA 324 324 324 ALA ALA B . n 
B 1 325 THR 325 325 325 THR THR B . n 
B 1 326 PHE 326 326 326 PHE PHE B . n 
B 1 327 PRO 327 327 327 PRO PRO B . n 
B 1 328 LEU 328 328 328 LEU LEU B . n 
B 1 329 ASN 329 329 329 ASN ASN B . n 
B 1 330 SER 330 330 330 SER SER B . n 
B 1 331 THR 331 331 331 THR THR B . n 
B 1 332 LEU 332 332 332 LEU LEU B . n 
B 1 333 TYR 333 333 333 TYR TYR B . n 
B 1 334 ALA 334 334 334 ALA ALA B . n 
B 1 335 ASP 335 335 335 ASP ASP B . n 
B 1 336 PHE 336 336 336 PHE PHE B . n 
B 1 337 SER 337 337 337 SER SER B . n 
B 1 338 HIS 338 338 338 HIS HIS B . n 
B 1 339 ASP 339 339 339 ASP ASP B . n 
B 1 340 ASN 340 340 340 ASN ASN B . n 
B 1 341 GLY 341 341 341 GLY GLY B . n 
B 1 342 ILE 342 342 342 ILE ILE B . n 
B 1 343 ILE 343 343 343 ILE ILE B . n 
B 1 344 SER 344 344 344 SER SER B . n 
B 1 345 ILE 345 345 345 ILE ILE B . n 
B 1 346 LEU 346 346 346 LEU LEU B . n 
B 1 347 PHE 347 347 347 PHE PHE B . n 
B 1 348 ALA 348 348 348 ALA ALA B . n 
B 1 349 LEU 349 349 349 LEU LEU B . n 
B 1 350 GLY 350 350 350 GLY GLY B . n 
B 1 351 LEU 351 351 351 LEU LEU B . n 
B 1 352 TYR 352 352 352 TYR TYR B . n 
B 1 353 ASN 353 353 353 ASN ASN B . n 
B 1 354 GLY 354 354 354 GLY GLY B . n 
B 1 355 THR 355 355 355 THR THR B . n 
B 1 356 LYS 356 356 356 LYS LYS B . n 
B 1 357 PRO 357 357 357 PRO PRO B . n 
B 1 358 LEU 358 358 358 LEU LEU B . n 
B 1 359 SER 359 359 359 SER SER B . n 
B 1 360 THR 360 360 360 THR THR B . n 
B 1 361 THR 361 361 361 THR THR B . n 
B 1 362 THR 362 362 362 THR THR B . n 
B 1 363 VAL 363 363 363 VAL VAL B . n 
B 1 364 GLU 364 364 364 GLU GLU B . n 
B 1 365 ASN 365 365 365 ASN ASN B . n 
B 1 366 ILE 366 366 366 ILE ILE B . n 
B 1 367 THR 367 367 367 THR THR B . n 
B 1 368 GLN 368 368 368 GLN GLN B . n 
B 1 369 THR 369 369 369 THR THR B . n 
B 1 370 ASP 370 370 370 ASP ASP B . n 
B 1 371 GLY 371 371 371 GLY GLY B . n 
B 1 372 PHE 372 372 372 PHE PHE B . n 
B 1 373 SER 373 373 373 SER SER B . n 
B 1 374 SER 374 374 374 SER SER B . n 
B 1 375 ALA 375 375 375 ALA ALA B . n 
B 1 376 TRP 376 376 376 TRP TRP B . n 
B 1 377 THR 377 377 377 THR THR B . n 
B 1 378 VAL 378 378 378 VAL VAL B . n 
B 1 379 PRO 379 379 379 PRO PRO B . n 
B 1 380 PHE 380 380 380 PHE PHE B . n 
B 1 381 ALA 381 381 381 ALA ALA B . n 
B 1 382 SER 382 382 382 SER SER B . n 
B 1 383 ARG 383 383 383 ARG ARG B . n 
B 1 384 LEU 384 384 384 LEU LEU B . n 
B 1 385 TYR 385 385 385 TYR TYR B . n 
B 1 386 VAL 386 386 386 VAL VAL B . n 
B 1 387 GLU 387 387 387 GLU GLU B . n 
B 1 388 MET 388 388 388 MET MET B . n 
B 1 389 MET 389 389 389 MET MET B . n 
B 1 390 GLN 390 390 390 GLN GLN B . n 
B 1 391 CYS 391 391 391 CYS CYS B . n 
B 1 392 GLN 392 392 392 GLN GLN B . n 
B 1 393 ALA 393 393 393 ALA ALA B . n 
B 1 394 GLU 394 394 394 GLU GLU B . n 
B 1 395 GLN 395 395 395 GLN GLN B . n 
B 1 396 GLU 396 396 396 GLU GLU B . n 
B 1 397 PRO 397 397 397 PRO PRO B . n 
B 1 398 LEU 398 398 398 LEU LEU B . n 
B 1 399 VAL 399 399 399 VAL VAL B . n 
B 1 400 ARG 400 400 400 ARG ARG B . n 
B 1 401 VAL 401 401 401 VAL VAL B . n 
B 1 402 LEU 402 402 402 LEU LEU B . n 
B 1 403 VAL 403 403 403 VAL VAL B . n 
B 1 404 ASN 404 404 404 ASN ASN B . n 
B 1 405 ASP 405 405 405 ASP ASP B . n 
B 1 406 ARG 406 406 406 ARG ARG B . n 
B 1 407 VAL 407 407 407 VAL VAL B . n 
B 1 408 VAL 408 408 408 VAL VAL B . n 
B 1 409 PRO 409 409 409 PRO PRO B . n 
B 1 410 LEU 410 410 410 LEU LEU B . n 
B 1 411 HIS 411 411 411 HIS HIS B . n 
B 1 412 GLY 412 412 412 GLY GLY B . n 
B 1 413 CYS 413 413 413 CYS CYS B . n 
B 1 414 PRO 414 414 414 PRO PRO B . n 
B 1 415 VAL 415 415 415 VAL VAL B . n 
B 1 416 ASP 416 416 416 ASP ASP B . n 
B 1 417 ALA 417 417 417 ALA ALA B . n 
B 1 418 LEU 418 418 418 LEU LEU B . n 
B 1 419 GLY 419 419 419 GLY GLY B . n 
B 1 420 ARG 420 420 420 ARG ARG B . n 
B 1 421 CYS 421 421 421 CYS CYS B . n 
B 1 422 THR 422 422 422 THR THR B . n 
B 1 423 ARG 423 423 423 ARG ARG B . n 
B 1 424 ASP 424 424 424 ASP ASP B . n 
B 1 425 SER 425 425 425 SER SER B . n 
B 1 426 PHE 426 426 426 PHE PHE B . n 
B 1 427 VAL 427 427 427 VAL VAL B . n 
B 1 428 ARG 428 428 428 ARG ARG B . n 
B 1 429 GLY 429 429 429 GLY GLY B . n 
B 1 430 LEU 430 430 430 LEU LEU B . n 
B 1 431 SER 431 431 431 SER SER B . n 
B 1 432 PHE 432 432 432 PHE PHE B . n 
B 1 433 ALA 433 433 433 ALA ALA B . n 
B 1 434 ARG 434 434 434 ARG ARG B . n 
B 1 435 SER 435 435 435 SER SER B . n 
B 1 436 GLY 436 436 436 GLY GLY B . n 
B 1 437 GLY 437 437 437 GLY GLY B . n 
B 1 438 ASP 438 438 438 ASP ASP B . n 
B 1 439 TRP 439 439 439 TRP TRP B . n 
B 1 440 ALA 440 440 440 ALA ALA B . n 
B 1 441 GLU 441 441 441 GLU GLU B . n 
B 1 442 CYS 442 442 442 CYS CYS B . n 
B 1 443 PHE 443 443 443 PHE PHE B . n 
B 1 444 ALA 444 444 444 ALA ALA B . n 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 82  A ASN 82  ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 316 A ASN 316 ? ASN 'GLYCOSYLATION SITE' 
3 A ASN 353 A ASN 353 ? ASN 'GLYCOSYLATION SITE' 
4 B ASN 82  B ASN 82  ? ASN 'GLYCOSYLATION SITE' 
5 B ASN 316 B ASN 316 ? ASN 'GLYCOSYLATION SITE' 
6 B ASN 353 B ASN 353 ? ASN 'GLYCOSYLATION SITE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,I 
2 1 B,F,G,H,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2010-06-30 
2 'Structure model' 1 1 2011-07-13 
# 
_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_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
Blu-Ice 'data collection' .        ? 1 
MOLREP  phasing           .        ? 2 
REFMAC  refinement        5.5.0102 ? 3 
MOSFLM  'data reduction'  .        ? 4 
SCALA   'data scaling'    .        ? 5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 ND2 A ASN 97  ? ? O  A HOH 521  ? ? 2.11 
2 1 ND2 A ASN 353 ? ? O5 A NAG 1003 ? ? 2.13 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              239 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              239 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              239 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                123.90 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            5.60 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                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 PHE A 31  ? ? -38.93  131.33 
2  1 SER A 67  ? ? -37.27  -70.94 
3  1 LEU A 100 ? ? -36.22  146.05 
4  1 ASP A 103 ? ? 71.54   -35.37 
5  1 ASN A 130 ? ? -146.32 14.05  
6  1 ASP A 188 ? ? -172.53 76.65  
7  1 PHE A 212 ? ? -145.94 -29.36 
8  1 LEU A 224 ? ? -111.10 79.22  
9  1 THR A 313 ? ? -95.62  -91.98 
10 1 THR A 377 ? ? -122.65 -57.03 
11 1 VAL A 378 ? ? -117.77 57.11  
12 1 ASP A 405 ? ? 85.69   6.03   
13 1 PRO A 414 ? ? -69.47  85.53  
14 1 LEU A 430 ? ? -94.77  40.36  
15 1 PHE B 31  ? ? -36.05  130.17 
16 1 TYR B 96  ? ? -39.66  129.58 
17 1 LEU B 100 ? ? -39.70  146.54 
18 1 ASP B 103 ? ? 73.53   -36.17 
19 1 ASN B 130 ? ? -147.14 13.18  
20 1 ASN B 184 ? ? -66.54  97.58  
21 1 ASP B 188 ? ? -170.45 77.99  
22 1 PHE B 212 ? ? -143.92 -29.51 
23 1 LEU B 224 ? ? -112.51 78.84  
24 1 THR B 313 ? ? -97.96  -89.20 
25 1 THR B 377 ? ? -120.80 -54.41 
26 1 VAL B 378 ? ? -118.40 56.69  
27 1 ASP B 405 ? ? 86.49   6.38   
28 1 PRO B 414 ? ? -69.14  87.56  
29 1 LEU B 430 ? ? -94.03  42.05  
# 
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 GLN 392 ? CG  ? A GLN 392 CG  
2  1 Y 1 A GLN 392 ? CD  ? A GLN 392 CD  
3  1 Y 1 A GLN 392 ? OE1 ? A GLN 392 OE1 
4  1 Y 1 A GLN 392 ? NE2 ? A GLN 392 NE2 
5  1 Y 1 A GLN 395 ? CG  ? A GLN 395 CG  
6  1 Y 1 A GLN 395 ? CD  ? A GLN 395 CD  
7  1 Y 1 A GLN 395 ? OE1 ? A GLN 395 OE1 
8  1 Y 1 A GLN 395 ? NE2 ? A GLN 395 NE2 
9  1 Y 1 B LYS 254 ? CG  ? B LYS 254 CG  
10 1 Y 1 B LYS 254 ? CD  ? B LYS 254 CD  
11 1 Y 1 B LYS 254 ? CE  ? B LYS 254 CE  
12 1 Y 1 B LYS 254 ? NZ  ? B LYS 254 NZ  
13 1 Y 1 B ASP 265 ? CG  ? B ASP 265 CG  
14 1 Y 1 B ASP 265 ? OD1 ? B ASP 265 OD1 
15 1 Y 1 B ASP 265 ? OD2 ? B ASP 265 OD2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ALA 1 ? A ALA 1 
2  1 Y 1 A SER 2 ? A SER 2 
3  1 Y 1 A ARG 3 ? A ARG 3 
4  1 Y 1 A ASN 4 ? A ASN 4 
5  1 Y 1 A GLN 5 ? A GLN 5 
6  1 Y 1 A SER 6 ? A SER 6 
7  1 Y 1 B ALA 1 ? B ALA 1 
8  1 Y 1 B SER 2 ? B SER 2 
9  1 Y 1 B ARG 3 ? B ARG 3 
10 1 Y 1 B ASN 4 ? B ASN 4 
11 1 Y 1 B GLN 5 ? B GLN 5 
12 1 Y 1 B SER 6 ? B SER 6 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 water                  HOH 
# 
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 NAG 1   1001 1001 NAG NAG A . 
D 2 NAG 1   1002 1002 NAG NAG A . 
E 2 NAG 1   1003 1003 NAG NAG A . 
F 2 NAG 1   1001 1001 NAG NAG B . 
G 2 NAG 1   1002 1002 NAG NAG B . 
H 2 NAG 1   1003 1003 NAG NAG B . 
I 3 HOH 1   445  2    HOH HOH A . 
I 3 HOH 2   446  3    HOH HOH A . 
I 3 HOH 3   447  5    HOH HOH A . 
I 3 HOH 4   448  8    HOH HOH A . 
I 3 HOH 5   449  9    HOH HOH A . 
I 3 HOH 6   450  10   HOH HOH A . 
I 3 HOH 7   451  12   HOH HOH A . 
I 3 HOH 8   452  15   HOH HOH A . 
I 3 HOH 9   453  18   HOH HOH A . 
I 3 HOH 10  454  20   HOH HOH A . 
I 3 HOH 11  455  22   HOH HOH A . 
I 3 HOH 12  456  26   HOH HOH A . 
I 3 HOH 13  457  27   HOH HOH A . 
I 3 HOH 14  458  28   HOH HOH A . 
I 3 HOH 15  459  32   HOH HOH A . 
I 3 HOH 16  460  33   HOH HOH A . 
I 3 HOH 17  461  37   HOH HOH A . 
I 3 HOH 18  462  39   HOH HOH A . 
I 3 HOH 19  463  41   HOH HOH A . 
I 3 HOH 20  464  43   HOH HOH A . 
I 3 HOH 21  465  44   HOH HOH A . 
I 3 HOH 22  466  47   HOH HOH A . 
I 3 HOH 23  467  48   HOH HOH A . 
I 3 HOH 24  468  51   HOH HOH A . 
I 3 HOH 25  469  55   HOH HOH A . 
I 3 HOH 26  470  56   HOH HOH A . 
I 3 HOH 27  471  59   HOH HOH A . 
I 3 HOH 28  472  60   HOH HOH A . 
I 3 HOH 29  473  64   HOH HOH A . 
I 3 HOH 30  474  66   HOH HOH A . 
I 3 HOH 31  475  67   HOH HOH A . 
I 3 HOH 32  476  68   HOH HOH A . 
I 3 HOH 33  477  71   HOH HOH A . 
I 3 HOH 34  478  72   HOH HOH A . 
I 3 HOH 35  479  74   HOH HOH A . 
I 3 HOH 36  480  77   HOH HOH A . 
I 3 HOH 37  481  81   HOH HOH A . 
I 3 HOH 38  482  83   HOH HOH A . 
I 3 HOH 39  483  87   HOH HOH A . 
I 3 HOH 40  484  88   HOH HOH A . 
I 3 HOH 41  485  89   HOH HOH A . 
I 3 HOH 42  486  90   HOH HOH A . 
I 3 HOH 43  487  94   HOH HOH A . 
I 3 HOH 44  488  96   HOH HOH A . 
I 3 HOH 45  489  97   HOH HOH A . 
I 3 HOH 46  490  98   HOH HOH A . 
I 3 HOH 47  491  100  HOH HOH A . 
I 3 HOH 48  492  101  HOH HOH A . 
I 3 HOH 49  493  102  HOH HOH A . 
I 3 HOH 50  494  103  HOH HOH A . 
I 3 HOH 51  495  104  HOH HOH A . 
I 3 HOH 52  496  105  HOH HOH A . 
I 3 HOH 53  497  106  HOH HOH A . 
I 3 HOH 54  498  107  HOH HOH A . 
I 3 HOH 55  499  108  HOH HOH A . 
I 3 HOH 56  500  111  HOH HOH A . 
I 3 HOH 57  501  113  HOH HOH A . 
I 3 HOH 58  502  115  HOH HOH A . 
I 3 HOH 59  503  119  HOH HOH A . 
I 3 HOH 60  504  120  HOH HOH A . 
I 3 HOH 61  505  121  HOH HOH A . 
I 3 HOH 62  506  122  HOH HOH A . 
I 3 HOH 63  507  123  HOH HOH A . 
I 3 HOH 64  508  124  HOH HOH A . 
I 3 HOH 65  509  125  HOH HOH A . 
I 3 HOH 66  510  127  HOH HOH A . 
I 3 HOH 67  511  128  HOH HOH A . 
I 3 HOH 68  512  129  HOH HOH A . 
I 3 HOH 69  513  130  HOH HOH A . 
I 3 HOH 70  514  132  HOH HOH A . 
I 3 HOH 71  515  133  HOH HOH A . 
I 3 HOH 72  516  136  HOH HOH A . 
I 3 HOH 73  517  138  HOH HOH A . 
I 3 HOH 74  518  140  HOH HOH A . 
I 3 HOH 75  519  141  HOH HOH A . 
I 3 HOH 76  520  143  HOH HOH A . 
I 3 HOH 77  521  144  HOH HOH A . 
I 3 HOH 78  522  146  HOH HOH A . 
I 3 HOH 79  523  147  HOH HOH A . 
I 3 HOH 80  524  148  HOH HOH A . 
I 3 HOH 81  525  149  HOH HOH A . 
I 3 HOH 82  526  150  HOH HOH A . 
I 3 HOH 83  527  152  HOH HOH A . 
I 3 HOH 84  528  155  HOH HOH A . 
I 3 HOH 85  529  157  HOH HOH A . 
I 3 HOH 86  530  161  HOH HOH A . 
I 3 HOH 87  531  162  HOH HOH A . 
I 3 HOH 88  532  167  HOH HOH A . 
I 3 HOH 89  533  168  HOH HOH A . 
I 3 HOH 90  534  170  HOH HOH A . 
I 3 HOH 91  535  174  HOH HOH A . 
I 3 HOH 92  536  175  HOH HOH A . 
I 3 HOH 93  537  177  HOH HOH A . 
I 3 HOH 94  538  180  HOH HOH A . 
I 3 HOH 95  539  181  HOH HOH A . 
I 3 HOH 96  540  182  HOH HOH A . 
I 3 HOH 97  541  183  HOH HOH A . 
I 3 HOH 98  542  184  HOH HOH A . 
I 3 HOH 99  543  185  HOH HOH A . 
I 3 HOH 100 544  187  HOH HOH A . 
I 3 HOH 101 545  192  HOH HOH A . 
I 3 HOH 102 546  194  HOH HOH A . 
I 3 HOH 103 547  197  HOH HOH A . 
I 3 HOH 104 548  198  HOH HOH A . 
I 3 HOH 105 549  199  HOH HOH A . 
I 3 HOH 106 550  200  HOH HOH A . 
I 3 HOH 107 551  201  HOH HOH A . 
I 3 HOH 108 552  203  HOH HOH A . 
I 3 HOH 109 553  204  HOH HOH A . 
I 3 HOH 110 554  205  HOH HOH A . 
I 3 HOH 111 555  207  HOH HOH A . 
I 3 HOH 112 556  208  HOH HOH A . 
I 3 HOH 113 557  209  HOH HOH A . 
I 3 HOH 114 558  210  HOH HOH A . 
I 3 HOH 115 559  215  HOH HOH A . 
I 3 HOH 116 560  220  HOH HOH A . 
I 3 HOH 117 561  221  HOH HOH A . 
I 3 HOH 118 562  225  HOH HOH A . 
I 3 HOH 119 563  228  HOH HOH A . 
I 3 HOH 120 564  229  HOH HOH A . 
I 3 HOH 121 565  230  HOH HOH A . 
I 3 HOH 122 566  231  HOH HOH A . 
I 3 HOH 123 567  232  HOH HOH A . 
I 3 HOH 124 568  237  HOH HOH A . 
I 3 HOH 125 569  238  HOH HOH A . 
I 3 HOH 126 570  240  HOH HOH A . 
I 3 HOH 127 571  242  HOH HOH A . 
I 3 HOH 128 572  243  HOH HOH A . 
I 3 HOH 129 573  244  HOH HOH A . 
I 3 HOH 130 574  245  HOH HOH A . 
I 3 HOH 131 575  246  HOH HOH A . 
I 3 HOH 132 576  248  HOH HOH A . 
I 3 HOH 133 577  249  HOH HOH A . 
I 3 HOH 134 578  251  HOH HOH A . 
I 3 HOH 135 579  252  HOH HOH A . 
I 3 HOH 136 580  253  HOH HOH A . 
I 3 HOH 137 581  254  HOH HOH A . 
I 3 HOH 138 582  256  HOH HOH A . 
I 3 HOH 139 583  259  HOH HOH A . 
I 3 HOH 140 584  261  HOH HOH A . 
I 3 HOH 141 585  262  HOH HOH A . 
I 3 HOH 142 586  263  HOH HOH A . 
I 3 HOH 143 587  265  HOH HOH A . 
I 3 HOH 144 588  267  HOH HOH A . 
I 3 HOH 145 589  269  HOH HOH A . 
I 3 HOH 146 590  273  HOH HOH A . 
I 3 HOH 147 591  274  HOH HOH A . 
I 3 HOH 148 592  278  HOH HOH A . 
I 3 HOH 149 593  280  HOH HOH A . 
I 3 HOH 150 594  281  HOH HOH A . 
I 3 HOH 151 595  283  HOH HOH A . 
I 3 HOH 152 596  286  HOH HOH A . 
I 3 HOH 153 597  289  HOH HOH A . 
I 3 HOH 154 598  290  HOH HOH A . 
I 3 HOH 155 599  292  HOH HOH A . 
I 3 HOH 156 600  297  HOH HOH A . 
I 3 HOH 157 601  298  HOH HOH A . 
I 3 HOH 158 602  299  HOH HOH A . 
I 3 HOH 159 603  300  HOH HOH A . 
I 3 HOH 160 604  301  HOH HOH A . 
I 3 HOH 161 605  302  HOH HOH A . 
I 3 HOH 162 606  304  HOH HOH A . 
I 3 HOH 163 607  306  HOH HOH A . 
I 3 HOH 164 608  307  HOH HOH A . 
I 3 HOH 165 609  311  HOH HOH A . 
I 3 HOH 166 610  312  HOH HOH A . 
I 3 HOH 167 611  315  HOH HOH A . 
I 3 HOH 168 612  316  HOH HOH A . 
I 3 HOH 169 613  317  HOH HOH A . 
J 3 HOH 1   445  1    HOH HOH B . 
J 3 HOH 2   446  4    HOH HOH B . 
J 3 HOH 3   447  6    HOH HOH B . 
J 3 HOH 4   448  7    HOH HOH B . 
J 3 HOH 5   449  11   HOH HOH B . 
J 3 HOH 6   450  13   HOH HOH B . 
J 3 HOH 7   451  14   HOH HOH B . 
J 3 HOH 8   452  16   HOH HOH B . 
J 3 HOH 9   453  17   HOH HOH B . 
J 3 HOH 10  454  19   HOH HOH B . 
J 3 HOH 11  455  21   HOH HOH B . 
J 3 HOH 12  456  23   HOH HOH B . 
J 3 HOH 13  457  24   HOH HOH B . 
J 3 HOH 14  458  25   HOH HOH B . 
J 3 HOH 15  459  29   HOH HOH B . 
J 3 HOH 16  460  30   HOH HOH B . 
J 3 HOH 17  461  31   HOH HOH B . 
J 3 HOH 18  462  34   HOH HOH B . 
J 3 HOH 19  463  35   HOH HOH B . 
J 3 HOH 20  464  36   HOH HOH B . 
J 3 HOH 21  465  38   HOH HOH B . 
J 3 HOH 22  466  40   HOH HOH B . 
J 3 HOH 23  467  42   HOH HOH B . 
J 3 HOH 24  468  45   HOH HOH B . 
J 3 HOH 25  469  46   HOH HOH B . 
J 3 HOH 26  470  49   HOH HOH B . 
J 3 HOH 27  471  50   HOH HOH B . 
J 3 HOH 28  472  52   HOH HOH B . 
J 3 HOH 29  473  53   HOH HOH B . 
J 3 HOH 30  474  54   HOH HOH B . 
J 3 HOH 31  475  57   HOH HOH B . 
J 3 HOH 32  476  58   HOH HOH B . 
J 3 HOH 33  477  61   HOH HOH B . 
J 3 HOH 34  478  62   HOH HOH B . 
J 3 HOH 35  479  63   HOH HOH B . 
J 3 HOH 36  480  65   HOH HOH B . 
J 3 HOH 37  481  69   HOH HOH B . 
J 3 HOH 38  482  70   HOH HOH B . 
J 3 HOH 39  483  73   HOH HOH B . 
J 3 HOH 40  484  75   HOH HOH B . 
J 3 HOH 41  485  76   HOH HOH B . 
J 3 HOH 42  486  78   HOH HOH B . 
J 3 HOH 43  487  79   HOH HOH B . 
J 3 HOH 44  488  80   HOH HOH B . 
J 3 HOH 45  489  82   HOH HOH B . 
J 3 HOH 46  490  84   HOH HOH B . 
J 3 HOH 47  491  85   HOH HOH B . 
J 3 HOH 48  492  86   HOH HOH B . 
J 3 HOH 49  493  91   HOH HOH B . 
J 3 HOH 50  494  92   HOH HOH B . 
J 3 HOH 51  495  93   HOH HOH B . 
J 3 HOH 52  496  95   HOH HOH B . 
J 3 HOH 53  497  99   HOH HOH B . 
J 3 HOH 54  498  109  HOH HOH B . 
J 3 HOH 55  499  110  HOH HOH B . 
J 3 HOH 56  500  112  HOH HOH B . 
J 3 HOH 57  501  114  HOH HOH B . 
J 3 HOH 58  502  116  HOH HOH B . 
J 3 HOH 59  503  117  HOH HOH B . 
J 3 HOH 60  504  118  HOH HOH B . 
J 3 HOH 61  505  126  HOH HOH B . 
J 3 HOH 62  506  131  HOH HOH B . 
J 3 HOH 63  507  134  HOH HOH B . 
J 3 HOH 64  508  135  HOH HOH B . 
J 3 HOH 65  509  137  HOH HOH B . 
J 3 HOH 66  510  139  HOH HOH B . 
J 3 HOH 67  511  142  HOH HOH B . 
J 3 HOH 68  512  145  HOH HOH B . 
J 3 HOH 69  513  151  HOH HOH B . 
J 3 HOH 70  514  153  HOH HOH B . 
J 3 HOH 71  515  154  HOH HOH B . 
J 3 HOH 72  516  156  HOH HOH B . 
J 3 HOH 73  517  158  HOH HOH B . 
J 3 HOH 74  518  159  HOH HOH B . 
J 3 HOH 75  519  160  HOH HOH B . 
J 3 HOH 76  520  163  HOH HOH B . 
J 3 HOH 77  521  164  HOH HOH B . 
J 3 HOH 78  522  165  HOH HOH B . 
J 3 HOH 79  523  166  HOH HOH B . 
J 3 HOH 80  524  169  HOH HOH B . 
J 3 HOH 81  525  171  HOH HOH B . 
J 3 HOH 82  526  172  HOH HOH B . 
J 3 HOH 83  527  173  HOH HOH B . 
J 3 HOH 84  528  176  HOH HOH B . 
J 3 HOH 85  529  178  HOH HOH B . 
J 3 HOH 86  530  179  HOH HOH B . 
J 3 HOH 87  531  186  HOH HOH B . 
J 3 HOH 88  532  188  HOH HOH B . 
J 3 HOH 89  533  189  HOH HOH B . 
J 3 HOH 90  534  190  HOH HOH B . 
J 3 HOH 91  535  191  HOH HOH B . 
J 3 HOH 92  536  193  HOH HOH B . 
J 3 HOH 93  537  195  HOH HOH B . 
J 3 HOH 94  538  196  HOH HOH B . 
J 3 HOH 95  539  202  HOH HOH B . 
J 3 HOH 96  540  206  HOH HOH B . 
J 3 HOH 97  541  211  HOH HOH B . 
J 3 HOH 98  542  212  HOH HOH B . 
J 3 HOH 99  543  213  HOH HOH B . 
J 3 HOH 100 544  214  HOH HOH B . 
J 3 HOH 101 545  216  HOH HOH B . 
J 3 HOH 102 546  217  HOH HOH B . 
J 3 HOH 103 547  218  HOH HOH B . 
J 3 HOH 104 548  219  HOH HOH B . 
J 3 HOH 105 549  222  HOH HOH B . 
J 3 HOH 106 550  223  HOH HOH B . 
J 3 HOH 107 551  224  HOH HOH B . 
J 3 HOH 108 552  227  HOH HOH B . 
J 3 HOH 109 553  233  HOH HOH B . 
J 3 HOH 110 554  234  HOH HOH B . 
J 3 HOH 111 555  235  HOH HOH B . 
J 3 HOH 112 556  236  HOH HOH B . 
J 3 HOH 113 557  239  HOH HOH B . 
J 3 HOH 114 558  241  HOH HOH B . 
J 3 HOH 115 559  247  HOH HOH B . 
J 3 HOH 116 560  250  HOH HOH B . 
J 3 HOH 117 561  255  HOH HOH B . 
J 3 HOH 118 562  257  HOH HOH B . 
J 3 HOH 119 563  258  HOH HOH B . 
J 3 HOH 120 564  260  HOH HOH B . 
J 3 HOH 121 565  264  HOH HOH B . 
J 3 HOH 122 566  266  HOH HOH B . 
J 3 HOH 123 567  268  HOH HOH B . 
J 3 HOH 124 568  270  HOH HOH B . 
J 3 HOH 125 569  271  HOH HOH B . 
J 3 HOH 126 570  272  HOH HOH B . 
J 3 HOH 127 571  275  HOH HOH B . 
J 3 HOH 128 572  276  HOH HOH B . 
J 3 HOH 129 573  277  HOH HOH B . 
J 3 HOH 130 574  279  HOH HOH B . 
J 3 HOH 131 575  282  HOH HOH B . 
J 3 HOH 132 576  284  HOH HOH B . 
J 3 HOH 133 577  285  HOH HOH B . 
J 3 HOH 134 578  287  HOH HOH B . 
J 3 HOH 135 579  288  HOH HOH B . 
J 3 HOH 136 580  291  HOH HOH B . 
J 3 HOH 137 581  293  HOH HOH B . 
J 3 HOH 138 582  294  HOH HOH B . 
J 3 HOH 139 583  295  HOH HOH B . 
J 3 HOH 140 584  296  HOH HOH B . 
J 3 HOH 141 585  303  HOH HOH B . 
J 3 HOH 142 586  305  HOH HOH B . 
J 3 HOH 143 587  308  HOH HOH B . 
J 3 HOH 144 588  309  HOH HOH B . 
J 3 HOH 145 589  310  HOH HOH B . 
J 3 HOH 146 590  313  HOH HOH B . 
J 3 HOH 147 591  314  HOH HOH B . 
# 
