data_8UWT
# 
_entry.id   8UWT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8UWT         pdb_00008uwt 10.2210/pdb8uwt/pdb 
WWPDB D_1000278870 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-13 
# 
_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_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8UWT 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 franz.j.st.john@usda.gov Franz 'St John' J 'principal investigator/group leader' 0000-0003-3458-5628 
3 zui@affrc.go.jp          Zui   Fujimoto  ? 'principal investigator/group leader' 0000-0002-3551-6854 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'St John, F.J.' 1 0000-0003-3458-5628 
'Fujimoto, Z.'  2 0000-0002-3551-6854 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;A X-ray Crystallographic Structure Model of a Glycoside Hydrolase (GH) Family 39 (GH39)-like Enzyme Encoded within a Xylan Utilization Locus of the pSOL1 Megaplasmid of Clostridium acetobutylicum
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'St John, F.J.' 1 0000-0003-3458-5628 
primary 'Fujimoto, Z.'  2 0000-0002-3551-6854 
# 
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 
'Possible beta-xylosidase diverged, family 5/39 of glycosyl hydrolases and alpha-amylase C (Greek key) C-terminal domain' 
45427.793 2   ? ? ? 
;The translated genomic DNA sequence was cloned for expression in pET28. The N-terminal secretion signal sequence was determined using Signal-P and replaced with an initiation codon and the C-terminal was in-line fused with the vector encoded His tag.
;
2 non-polymer syn GLYCEROL 92.094    3   ? ? ? ? 
3 non-polymer syn 'FORMIC ACID' 46.025    31  ? ? ? ? 
4 non-polymer syn 'TRIETHYLENE GLYCOL' 150.173   1   ? ? ? ? 
5 non-polymer syn BICINE 163.172   1   ? ? ? ? 
6 non-polymer syn 'SODIUM ION' 22.990    1   ? ? ? ? 
7 water       nat water 18.015    872 ? ? ? ? 
# 
_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       
;MATTLTVDCRATLRGVTHCASGSLYGVTESKPFDINQFVAPLKPNVFTNPALAGFNHQQPIGAAIPTAGRLKNTTGKVMI
RLADIFPRWPYGFTNMNDWLGKVTSVINQKKASGYSNFYGYEIWNEPDGTFKNNNVSFNDMWLQTYKLIRRLDPNSQIIG
PSYSYYNHYNMNAFLNFCRANNCLPDVICWHELGGSQNISGNIRDLKTLERSLGIPERKIAINEYSDSNHYAEGQPGASA
PFIAKFERNKVDSACISWWWTNAPGRLGSLMASDTQKGAGWWFYKWYGDMTGNMVNVIPQNDNSNLADGFACVDSNAKYI
SVLLGGVNDGTVNVNIKNIPAFIGSSATVKVEKVDWNGKDTPVNGTNTVFSKRYTVSNGTINVSIPGTNNTSGYRVYVSR
LEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MATTLTVDCRATLRGVTHCASGSLYGVTESKPFDINQFVAPLKPNVFTNPALAGFNHQQPIGAAIPTAGRLKNTTGKVMI
RLADIFPRWPYGFTNMNDWLGKVTSVINQKKASGYSNFYGYEIWNEPDGTFKNNNVSFNDMWLQTYKLIRRLDPNSQIIG
PSYSYYNHYNMNAFLNFCRANNCLPDVICWHELGGSQNISGNIRDLKTLERSLGIPERKIAINEYSDSNHYAEGQPGASA
PFIAKFERNKVDSACISWWWTNAPGRLGSLMASDTQKGAGWWFYKWYGDMTGNMVNVIPQNDNSNLADGFACVDSNAKYI
SVLLGGVNDGTVNVNIKNIPAFIGSSATVKVEKVDWNGKDTPVNGTNTVFSKRYTVSNGTINVSIPGTNNTSGYRVYVSR
LEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCEROL             GOL 
3 'FORMIC ACID'        FMT 
4 'TRIETHYLENE GLYCOL' PGE 
5 BICINE               BCN 
6 'SODIUM ION'         NA  
7 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   THR n 
1 5   LEU n 
1 6   THR n 
1 7   VAL n 
1 8   ASP n 
1 9   CYS n 
1 10  ARG n 
1 11  ALA n 
1 12  THR n 
1 13  LEU n 
1 14  ARG n 
1 15  GLY n 
1 16  VAL n 
1 17  THR n 
1 18  HIS n 
1 19  CYS n 
1 20  ALA n 
1 21  SER n 
1 22  GLY n 
1 23  SER n 
1 24  LEU n 
1 25  TYR n 
1 26  GLY n 
1 27  VAL n 
1 28  THR n 
1 29  GLU n 
1 30  SER n 
1 31  LYS n 
1 32  PRO n 
1 33  PHE n 
1 34  ASP n 
1 35  ILE n 
1 36  ASN n 
1 37  GLN n 
1 38  PHE n 
1 39  VAL n 
1 40  ALA n 
1 41  PRO n 
1 42  LEU n 
1 43  LYS n 
1 44  PRO n 
1 45  ASN n 
1 46  VAL n 
1 47  PHE n 
1 48  THR n 
1 49  ASN n 
1 50  PRO n 
1 51  ALA n 
1 52  LEU n 
1 53  ALA n 
1 54  GLY n 
1 55  PHE n 
1 56  ASN n 
1 57  HIS n 
1 58  GLN n 
1 59  GLN n 
1 60  PRO n 
1 61  ILE n 
1 62  GLY n 
1 63  ALA n 
1 64  ALA n 
1 65  ILE n 
1 66  PRO n 
1 67  THR n 
1 68  ALA n 
1 69  GLY n 
1 70  ARG n 
1 71  LEU n 
1 72  LYS n 
1 73  ASN n 
1 74  THR n 
1 75  THR n 
1 76  GLY n 
1 77  LYS n 
1 78  VAL n 
1 79  MET n 
1 80  ILE n 
1 81  ARG n 
1 82  LEU n 
1 83  ALA n 
1 84  ASP n 
1 85  ILE n 
1 86  PHE n 
1 87  PRO n 
1 88  ARG n 
1 89  TRP n 
1 90  PRO n 
1 91  TYR n 
1 92  GLY n 
1 93  PHE n 
1 94  THR n 
1 95  ASN n 
1 96  MET n 
1 97  ASN n 
1 98  ASP n 
1 99  TRP n 
1 100 LEU n 
1 101 GLY n 
1 102 LYS n 
1 103 VAL n 
1 104 THR n 
1 105 SER n 
1 106 VAL n 
1 107 ILE n 
1 108 ASN n 
1 109 GLN n 
1 110 LYS n 
1 111 LYS n 
1 112 ALA n 
1 113 SER n 
1 114 GLY n 
1 115 TYR n 
1 116 SER n 
1 117 ASN n 
1 118 PHE n 
1 119 TYR n 
1 120 GLY n 
1 121 TYR n 
1 122 GLU n 
1 123 ILE n 
1 124 TRP n 
1 125 ASN n 
1 126 GLU n 
1 127 PRO n 
1 128 ASP n 
1 129 GLY n 
1 130 THR n 
1 131 PHE n 
1 132 LYS n 
1 133 ASN n 
1 134 ASN n 
1 135 ASN n 
1 136 VAL n 
1 137 SER n 
1 138 PHE n 
1 139 ASN n 
1 140 ASP n 
1 141 MET n 
1 142 TRP n 
1 143 LEU n 
1 144 GLN n 
1 145 THR n 
1 146 TYR n 
1 147 LYS n 
1 148 LEU n 
1 149 ILE n 
1 150 ARG n 
1 151 ARG n 
1 152 LEU n 
1 153 ASP n 
1 154 PRO n 
1 155 ASN n 
1 156 SER n 
1 157 GLN n 
1 158 ILE n 
1 159 ILE n 
1 160 GLY n 
1 161 PRO n 
1 162 SER n 
1 163 TYR n 
1 164 SER n 
1 165 TYR n 
1 166 TYR n 
1 167 ASN n 
1 168 HIS n 
1 169 TYR n 
1 170 ASN n 
1 171 MET n 
1 172 ASN n 
1 173 ALA n 
1 174 PHE n 
1 175 LEU n 
1 176 ASN n 
1 177 PHE n 
1 178 CYS n 
1 179 ARG n 
1 180 ALA n 
1 181 ASN n 
1 182 ASN n 
1 183 CYS n 
1 184 LEU n 
1 185 PRO n 
1 186 ASP n 
1 187 VAL n 
1 188 ILE n 
1 189 CYS n 
1 190 TRP n 
1 191 HIS n 
1 192 GLU n 
1 193 LEU n 
1 194 GLY n 
1 195 GLY n 
1 196 SER n 
1 197 GLN n 
1 198 ASN n 
1 199 ILE n 
1 200 SER n 
1 201 GLY n 
1 202 ASN n 
1 203 ILE n 
1 204 ARG n 
1 205 ASP n 
1 206 LEU n 
1 207 LYS n 
1 208 THR n 
1 209 LEU n 
1 210 GLU n 
1 211 ARG n 
1 212 SER n 
1 213 LEU n 
1 214 GLY n 
1 215 ILE n 
1 216 PRO n 
1 217 GLU n 
1 218 ARG n 
1 219 LYS n 
1 220 ILE n 
1 221 ALA n 
1 222 ILE n 
1 223 ASN n 
1 224 GLU n 
1 225 TYR n 
1 226 SER n 
1 227 ASP n 
1 228 SER n 
1 229 ASN n 
1 230 HIS n 
1 231 TYR n 
1 232 ALA n 
1 233 GLU n 
1 234 GLY n 
1 235 GLN n 
1 236 PRO n 
1 237 GLY n 
1 238 ALA n 
1 239 SER n 
1 240 ALA n 
1 241 PRO n 
1 242 PHE n 
1 243 ILE n 
1 244 ALA n 
1 245 LYS n 
1 246 PHE n 
1 247 GLU n 
1 248 ARG n 
1 249 ASN n 
1 250 LYS n 
1 251 VAL n 
1 252 ASP n 
1 253 SER n 
1 254 ALA n 
1 255 CYS n 
1 256 ILE n 
1 257 SER n 
1 258 TRP n 
1 259 TRP n 
1 260 TRP n 
1 261 THR n 
1 262 ASN n 
1 263 ALA n 
1 264 PRO n 
1 265 GLY n 
1 266 ARG n 
1 267 LEU n 
1 268 GLY n 
1 269 SER n 
1 270 LEU n 
1 271 MET n 
1 272 ALA n 
1 273 SER n 
1 274 ASP n 
1 275 THR n 
1 276 GLN n 
1 277 LYS n 
1 278 GLY n 
1 279 ALA n 
1 280 GLY n 
1 281 TRP n 
1 282 TRP n 
1 283 PHE n 
1 284 TYR n 
1 285 LYS n 
1 286 TRP n 
1 287 TYR n 
1 288 GLY n 
1 289 ASP n 
1 290 MET n 
1 291 THR n 
1 292 GLY n 
1 293 ASN n 
1 294 MET n 
1 295 VAL n 
1 296 ASN n 
1 297 VAL n 
1 298 ILE n 
1 299 PRO n 
1 300 GLN n 
1 301 ASN n 
1 302 ASP n 
1 303 ASN n 
1 304 SER n 
1 305 ASN n 
1 306 LEU n 
1 307 ALA n 
1 308 ASP n 
1 309 GLY n 
1 310 PHE n 
1 311 ALA n 
1 312 CYS n 
1 313 VAL n 
1 314 ASP n 
1 315 SER n 
1 316 ASN n 
1 317 ALA n 
1 318 LYS n 
1 319 TYR n 
1 320 ILE n 
1 321 SER n 
1 322 VAL n 
1 323 LEU n 
1 324 LEU n 
1 325 GLY n 
1 326 GLY n 
1 327 VAL n 
1 328 ASN n 
1 329 ASP n 
1 330 GLY n 
1 331 THR n 
1 332 VAL n 
1 333 ASN n 
1 334 VAL n 
1 335 ASN n 
1 336 ILE n 
1 337 LYS n 
1 338 ASN n 
1 339 ILE n 
1 340 PRO n 
1 341 ALA n 
1 342 PHE n 
1 343 ILE n 
1 344 GLY n 
1 345 SER n 
1 346 SER n 
1 347 ALA n 
1 348 THR n 
1 349 VAL n 
1 350 LYS n 
1 351 VAL n 
1 352 GLU n 
1 353 LYS n 
1 354 VAL n 
1 355 ASP n 
1 356 TRP n 
1 357 ASN n 
1 358 GLY n 
1 359 LYS n 
1 360 ASP n 
1 361 THR n 
1 362 PRO n 
1 363 VAL n 
1 364 ASN n 
1 365 GLY n 
1 366 THR n 
1 367 ASN n 
1 368 THR n 
1 369 VAL n 
1 370 PHE n 
1 371 SER n 
1 372 LYS n 
1 373 ARG n 
1 374 TYR n 
1 375 THR n 
1 376 VAL n 
1 377 SER n 
1 378 ASN n 
1 379 GLY n 
1 380 THR n 
1 381 ILE n 
1 382 ASN n 
1 383 VAL n 
1 384 SER n 
1 385 ILE n 
1 386 PRO n 
1 387 GLY n 
1 388 THR n 
1 389 ASN n 
1 390 ASN n 
1 391 THR n 
1 392 SER n 
1 393 GLY n 
1 394 TYR n 
1 395 ARG n 
1 396 VAL n 
1 397 TYR n 
1 398 VAL n 
1 399 SER n 
1 400 ARG n 
1 401 LEU n 
1 402 GLU n 
1 403 HIS n 
1 404 HIS n 
1 405 HIS n 
1 406 HIS n 
1 407 HIS n 
1 408 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   408 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA_P0117 
_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                   'Mega plasmid pSOL1' 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Clostridium acetobutylicum ATCC 824' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     272562 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              Rosetta 
_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                   pET27 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE              ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE             ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE           ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'      ?                               'C4 H7 N O4'     133.103 
BCN non-polymer         . BICINE               ?                               'C6 H13 N O4'    163.172 
CYS 'L-peptide linking' y CYSTEINE             ?                               'C3 H7 N O2 S'   121.158 
FMT non-polymer         . 'FORMIC ACID'        ?                               'C H2 O2'        46.025  
GLN 'L-peptide linking' y GLUTAMINE            ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'      ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE              ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL             'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE            ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE           ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE              ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE               ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE           ?                               'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'         ?                               'Na 1'           22.990  
PGE non-polymer         . 'TRIETHYLENE GLYCOL' ?                               'C6 H14 O4'      150.173 
PHE 'L-peptide linking' y PHENYLALANINE        ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE              ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE               ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE            ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN           ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE             ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE               ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   THR 3   3   3   THR THR A . n 
A 1 4   THR 4   4   4   THR THR A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   ASP 8   8   8   ASP ASP A . n 
A 1 9   CYS 9   9   9   CYS CYS A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  THR 12  12  12  THR THR A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  THR 17  17  17  THR THR A . n 
A 1 18  HIS 18  18  18  HIS HIS A . n 
A 1 19  CYS 19  19  19  CYS CYS A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  THR 28  28  28  THR THR A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  SER 30  30  30  SER SER A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  ASN 36  36  36  ASN ASN A . n 
A 1 37  GLN 37  37  37  GLN GLN A . n 
A 1 38  PHE 38  38  38  PHE PHE A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  PRO 41  41  41  PRO PRO A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  ASN 45  45  45  ASN ASN A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  PHE 47  47  47  PHE PHE A . n 
A 1 48  THR 48  48  48  THR THR A . n 
A 1 49  ASN 49  49  49  ASN ASN A . n 
A 1 50  PRO 50  50  50  PRO PRO A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  PHE 55  55  55  PHE PHE A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  HIS 57  57  57  HIS HIS A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  GLN 59  59  59  GLN GLN A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  LYS 72  72  72  LYS LYS A . n 
A 1 73  ASN 73  73  73  ASN ASN A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  MET 79  79  79  MET MET A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  PHE 86  86  86  PHE PHE A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  TRP 89  89  89  TRP TRP A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  THR 94  94  94  THR THR A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  MET 96  96  96  MET MET A . n 
A 1 97  ASN 97  97  97  ASN ASN A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  TRP 99  99  99  TRP TRP 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 LYS 102 102 102 LYS LYS A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 THR 104 104 104 THR THR A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 GLN 109 109 109 GLN GLN A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 PHE 118 118 118 PHE PHE A . n 
A 1 119 TYR 119 119 119 TYR TYR A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 TRP 124 124 124 TRP TRP A . n 
A 1 125 ASN 125 125 125 ASN ASN A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 THR 130 130 130 THR THR A . n 
A 1 131 PHE 131 131 131 PHE PHE A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 ASN 135 135 135 ASN ASN A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 SER 137 137 137 SER SER A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 MET 141 141 141 MET MET A . n 
A 1 142 TRP 142 142 142 TRP TRP A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 GLN 144 144 144 GLN GLN A . n 
A 1 145 THR 145 145 145 THR THR A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 ARG 150 150 150 ARG ARG A . n 
A 1 151 ARG 151 151 151 ARG ARG A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 ASN 155 155 155 ASN ASN A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 PRO 161 161 161 PRO PRO A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 TYR 163 163 163 TYR TYR A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 TYR 165 165 165 TYR TYR A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 HIS 168 168 168 HIS HIS A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 ASN 170 170 170 ASN ASN A . n 
A 1 171 MET 171 171 171 MET MET A . n 
A 1 172 ASN 172 172 172 ASN ASN A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 PHE 174 174 174 PHE PHE A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 CYS 178 178 178 CYS CYS A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 ASN 181 181 181 ASN ASN A . n 
A 1 182 ASN 182 182 182 ASN ASN A . n 
A 1 183 CYS 183 183 183 CYS CYS A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 CYS 189 189 189 CYS CYS A . n 
A 1 190 TRP 190 190 190 TRP TRP A . n 
A 1 191 HIS 191 191 191 HIS HIS A . n 
A 1 192 GLU 192 192 192 GLU GLU A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 GLN 197 197 197 GLN GLN A . n 
A 1 198 ASN 198 198 198 ASN ASN A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 GLY 201 201 201 GLY GLY A . n 
A 1 202 ASN 202 202 202 ASN ASN A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 ASP 205 205 205 ASP ASP A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 THR 208 208 208 THR THR A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 ARG 211 211 211 ARG ARG A . n 
A 1 212 SER 212 212 212 SER SER A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 PRO 216 216 216 PRO PRO A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 ARG 218 218 218 ARG ARG A . n 
A 1 219 LYS 219 219 219 LYS LYS A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 ASN 223 223 223 ASN ASN A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 TYR 225 225 225 TYR TYR A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 ASP 227 227 227 ASP ASP A . n 
A 1 228 SER 228 228 228 SER SER A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 HIS 230 230 230 HIS HIS A . n 
A 1 231 TYR 231 231 231 TYR TYR A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 GLN 235 235 235 GLN GLN A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 ALA 238 238 238 ALA ALA A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 PHE 242 242 242 PHE PHE A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 LYS 245 245 245 LYS LYS A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 ARG 248 248 248 ARG ARG A . n 
A 1 249 ASN 249 249 249 ASN ASN A . n 
A 1 250 LYS 250 250 250 LYS LYS 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 SER 253 253 253 SER SER A . n 
A 1 254 ALA 254 254 254 ALA ALA A . n 
A 1 255 CYS 255 255 255 CYS CYS A . n 
A 1 256 ILE 256 256 256 ILE ILE A . n 
A 1 257 SER 257 257 257 SER SER A . n 
A 1 258 TRP 258 258 258 TRP TRP A . n 
A 1 259 TRP 259 259 259 TRP TRP A . n 
A 1 260 TRP 260 260 260 TRP TRP A . n 
A 1 261 THR 261 261 261 THR THR A . n 
A 1 262 ASN 262 262 262 ASN ASN A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 PRO 264 264 264 PRO PRO A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 ARG 266 266 266 ARG ARG A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 GLY 268 268 268 GLY GLY A . n 
A 1 269 SER 269 269 269 SER SER A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 MET 271 271 271 MET MET A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 SER 273 273 273 SER SER A . n 
A 1 274 ASP 274 274 274 ASP ASP A . n 
A 1 275 THR 275 275 275 THR THR A . n 
A 1 276 GLN 276 276 276 GLN GLN A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ALA 279 279 279 ALA ALA A . n 
A 1 280 GLY 280 280 280 GLY GLY A . n 
A 1 281 TRP 281 281 281 TRP TRP A . n 
A 1 282 TRP 282 282 282 TRP TRP A . n 
A 1 283 PHE 283 283 283 PHE PHE A . n 
A 1 284 TYR 284 284 284 TYR TYR A . n 
A 1 285 LYS 285 285 285 LYS LYS A . n 
A 1 286 TRP 286 286 286 TRP TRP A . n 
A 1 287 TYR 287 287 287 TYR TYR A . n 
A 1 288 GLY 288 288 288 GLY GLY A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 MET 290 290 290 MET MET A . n 
A 1 291 THR 291 291 291 THR THR A . n 
A 1 292 GLY 292 292 292 GLY GLY A . n 
A 1 293 ASN 293 293 293 ASN ASN A . n 
A 1 294 MET 294 294 294 MET MET A . n 
A 1 295 VAL 295 295 295 VAL VAL A . n 
A 1 296 ASN 296 296 296 ASN ASN A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ILE 298 298 298 ILE ILE A . n 
A 1 299 PRO 299 299 299 PRO PRO A . n 
A 1 300 GLN 300 300 300 GLN GLN A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 ASP 302 302 302 ASP ASP A . n 
A 1 303 ASN 303 303 303 ASN ASN A . n 
A 1 304 SER 304 304 304 SER SER A . n 
A 1 305 ASN 305 305 305 ASN ASN A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 ALA 307 307 307 ALA ALA A . n 
A 1 308 ASP 308 308 308 ASP ASP A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 PHE 310 310 310 PHE PHE A . n 
A 1 311 ALA 311 311 311 ALA ALA A . n 
A 1 312 CYS 312 312 312 CYS CYS A . n 
A 1 313 VAL 313 313 313 VAL VAL A . n 
A 1 314 ASP 314 314 314 ASP ASP 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 ALA 317 317 317 ALA ALA A . n 
A 1 318 LYS 318 318 318 LYS LYS A . n 
A 1 319 TYR 319 319 319 TYR TYR A . n 
A 1 320 ILE 320 320 320 ILE ILE A . n 
A 1 321 SER 321 321 321 SER SER A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
A 1 323 LEU 323 323 323 LEU LEU A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 GLY 325 325 325 GLY GLY A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 ASN 328 328 328 ASN ASN A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 GLY 330 330 330 GLY GLY A . n 
A 1 331 THR 331 331 331 THR THR A . n 
A 1 332 VAL 332 332 332 VAL VAL A . n 
A 1 333 ASN 333 333 333 ASN ASN A . n 
A 1 334 VAL 334 334 334 VAL VAL A . n 
A 1 335 ASN 335 335 335 ASN ASN A . n 
A 1 336 ILE 336 336 336 ILE ILE A . n 
A 1 337 LYS 337 337 337 LYS LYS A . n 
A 1 338 ASN 338 338 338 ASN ASN A . n 
A 1 339 ILE 339 339 339 ILE ILE A . n 
A 1 340 PRO 340 340 340 PRO PRO A . n 
A 1 341 ALA 341 341 341 ALA ALA A . n 
A 1 342 PHE 342 342 342 PHE PHE A . n 
A 1 343 ILE 343 343 343 ILE ILE A . n 
A 1 344 GLY 344 344 344 GLY GLY A . n 
A 1 345 SER 345 345 345 SER SER A . n 
A 1 346 SER 346 346 346 SER SER A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 THR 348 348 348 THR THR A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 LYS 350 350 350 LYS LYS A . n 
A 1 351 VAL 351 351 351 VAL VAL A . n 
A 1 352 GLU 352 352 352 GLU GLU A . n 
A 1 353 LYS 353 353 353 LYS LYS A . n 
A 1 354 VAL 354 354 354 VAL VAL A . n 
A 1 355 ASP 355 355 355 ASP ASP A . n 
A 1 356 TRP 356 356 356 TRP TRP A . n 
A 1 357 ASN 357 357 357 ASN ASN A . n 
A 1 358 GLY 358 358 358 GLY GLY A . n 
A 1 359 LYS 359 359 359 LYS LYS A . n 
A 1 360 ASP 360 360 360 ASP ASP A . n 
A 1 361 THR 361 361 361 THR THR A . n 
A 1 362 PRO 362 362 362 PRO PRO A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 ASN 364 364 364 ASN ASN A . n 
A 1 365 GLY 365 365 365 GLY GLY A . n 
A 1 366 THR 366 366 366 THR THR A . n 
A 1 367 ASN 367 367 367 ASN ASN A . n 
A 1 368 THR 368 368 368 THR THR A . n 
A 1 369 VAL 369 369 369 VAL VAL A . n 
A 1 370 PHE 370 370 370 PHE PHE A . n 
A 1 371 SER 371 371 371 SER SER A . n 
A 1 372 LYS 372 372 372 LYS LYS A . n 
A 1 373 ARG 373 373 373 ARG ARG A . n 
A 1 374 TYR 374 374 374 TYR TYR A . n 
A 1 375 THR 375 375 375 THR THR A . n 
A 1 376 VAL 376 376 376 VAL VAL A . n 
A 1 377 SER 377 377 377 SER SER A . n 
A 1 378 ASN 378 378 378 ASN ASN A . n 
A 1 379 GLY 379 379 379 GLY GLY A . n 
A 1 380 THR 380 380 380 THR THR A . n 
A 1 381 ILE 381 381 381 ILE ILE A . n 
A 1 382 ASN 382 382 382 ASN ASN A . n 
A 1 383 VAL 383 383 383 VAL VAL A . n 
A 1 384 SER 384 384 384 SER SER A . n 
A 1 385 ILE 385 385 385 ILE ILE A . n 
A 1 386 PRO 386 386 386 PRO PRO A . n 
A 1 387 GLY 387 387 387 GLY GLY A . n 
A 1 388 THR 388 388 388 THR THR A . n 
A 1 389 ASN 389 389 389 ASN ASN A . n 
A 1 390 ASN 390 390 390 ASN ASN A . n 
A 1 391 THR 391 391 391 THR THR A . n 
A 1 392 SER 392 392 392 SER SER A . n 
A 1 393 GLY 393 393 393 GLY GLY A . n 
A 1 394 TYR 394 394 394 TYR TYR A . n 
A 1 395 ARG 395 395 395 ARG ARG A . n 
A 1 396 VAL 396 396 396 VAL VAL A . n 
A 1 397 TYR 397 397 397 TYR TYR A . n 
A 1 398 VAL 398 398 398 VAL VAL A . n 
A 1 399 SER 399 399 399 SER SER A . n 
A 1 400 ARG 400 400 400 ARG ARG A . n 
A 1 401 LEU 401 401 401 LEU LEU A . n 
A 1 402 GLU 402 402 ?   ?   ?   A . n 
A 1 403 HIS 403 403 ?   ?   ?   A . n 
A 1 404 HIS 404 404 ?   ?   ?   A . n 
A 1 405 HIS 405 405 ?   ?   ?   A . n 
A 1 406 HIS 406 406 ?   ?   ?   A . n 
A 1 407 HIS 407 407 ?   ?   ?   A . n 
A 1 408 HIS 408 408 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ALA 2   2   2   ALA ALA B . n 
B 1 3   THR 3   3   3   THR THR B . n 
B 1 4   THR 4   4   4   THR THR B . n 
B 1 5   LEU 5   5   5   LEU LEU B . n 
B 1 6   THR 6   6   6   THR THR B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   ASP 8   8   8   ASP ASP B . n 
B 1 9   CYS 9   9   9   CYS CYS B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  ALA 11  11  11  ALA ALA B . n 
B 1 12  THR 12  12  12  THR THR B . n 
B 1 13  LEU 13  13  13  LEU LEU B . n 
B 1 14  ARG 14  14  14  ARG ARG B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  THR 17  17  17  THR THR B . n 
B 1 18  HIS 18  18  18  HIS HIS B . n 
B 1 19  CYS 19  19  19  CYS CYS B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  SER 23  23  23  SER SER B . n 
B 1 24  LEU 24  24  24  LEU LEU B . n 
B 1 25  TYR 25  25  25  TYR TYR B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  VAL 27  27  27  VAL VAL B . n 
B 1 28  THR 28  28  28  THR THR B . n 
B 1 29  GLU 29  29  29  GLU GLU B . n 
B 1 30  SER 30  30  30  SER SER B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  PHE 33  33  33  PHE PHE B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  ASN 36  36  36  ASN ASN B . n 
B 1 37  GLN 37  37  37  GLN GLN B . n 
B 1 38  PHE 38  38  38  PHE PHE B . n 
B 1 39  VAL 39  39  39  VAL VAL B . n 
B 1 40  ALA 40  40  40  ALA ALA B . n 
B 1 41  PRO 41  41  41  PRO PRO B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  LYS 43  43  43  LYS LYS B . n 
B 1 44  PRO 44  44  44  PRO PRO B . n 
B 1 45  ASN 45  45  45  ASN ASN B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  PHE 47  47  47  PHE PHE B . n 
B 1 48  THR 48  48  48  THR THR B . n 
B 1 49  ASN 49  49  49  ASN ASN B . n 
B 1 50  PRO 50  50  50  PRO PRO B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  ALA 53  53  53  ALA ALA B . n 
B 1 54  GLY 54  54  54  GLY GLY B . n 
B 1 55  PHE 55  55  55  PHE PHE B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  HIS 57  57  57  HIS HIS B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  GLN 59  59  59  GLN GLN B . n 
B 1 60  PRO 60  60  60  PRO PRO B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  GLY 62  62  62  GLY GLY B . n 
B 1 63  ALA 63  63  63  ALA ALA B . n 
B 1 64  ALA 64  64  64  ALA ALA B . n 
B 1 65  ILE 65  65  65  ILE ILE B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  THR 67  67  67  THR THR B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  GLY 69  69  69  GLY GLY B . n 
B 1 70  ARG 70  70  70  ARG ARG B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  LYS 72  72  72  LYS LYS B . n 
B 1 73  ASN 73  73  73  ASN ASN B . n 
B 1 74  THR 74  74  74  THR THR B . n 
B 1 75  THR 75  75  75  THR THR B . n 
B 1 76  GLY 76  76  76  GLY GLY B . n 
B 1 77  LYS 77  77  77  LYS LYS B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  MET 79  79  79  MET MET B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  ARG 81  81  81  ARG ARG B . n 
B 1 82  LEU 82  82  82  LEU LEU B . n 
B 1 83  ALA 83  83  83  ALA ALA B . n 
B 1 84  ASP 84  84  84  ASP ASP B . n 
B 1 85  ILE 85  85  85  ILE ILE B . n 
B 1 86  PHE 86  86  86  PHE PHE B . n 
B 1 87  PRO 87  87  87  PRO PRO B . n 
B 1 88  ARG 88  88  88  ARG ARG B . n 
B 1 89  TRP 89  89  89  TRP TRP B . n 
B 1 90  PRO 90  90  90  PRO PRO B . n 
B 1 91  TYR 91  91  91  TYR TYR B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  PHE 93  93  93  PHE PHE B . n 
B 1 94  THR 94  94  94  THR THR B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  MET 96  96  96  MET MET B . n 
B 1 97  ASN 97  97  97  ASN ASN B . n 
B 1 98  ASP 98  98  98  ASP ASP B . n 
B 1 99  TRP 99  99  99  TRP TRP 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 LYS 102 102 102 LYS LYS B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 THR 104 104 104 THR THR B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 VAL 106 106 106 VAL VAL B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 ASN 108 108 108 ASN ASN B . n 
B 1 109 GLN 109 109 109 GLN GLN B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 TYR 115 115 115 TYR TYR B . n 
B 1 116 SER 116 116 116 SER SER B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 PHE 118 118 118 PHE PHE B . n 
B 1 119 TYR 119 119 119 TYR TYR B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 GLU 122 122 122 GLU GLU B . n 
B 1 123 ILE 123 123 123 ILE ILE B . n 
B 1 124 TRP 124 124 124 TRP TRP B . n 
B 1 125 ASN 125 125 125 ASN ASN B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 THR 130 130 130 THR THR B . n 
B 1 131 PHE 131 131 131 PHE PHE B . n 
B 1 132 LYS 132 132 132 LYS LYS B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 ASN 135 135 135 ASN ASN B . n 
B 1 136 VAL 136 136 136 VAL VAL B . n 
B 1 137 SER 137 137 137 SER SER B . n 
B 1 138 PHE 138 138 138 PHE PHE B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ASP 140 140 140 ASP ASP B . n 
B 1 141 MET 141 141 141 MET MET B . n 
B 1 142 TRP 142 142 142 TRP TRP B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 GLN 144 144 144 GLN GLN B . n 
B 1 145 THR 145 145 145 THR THR B . n 
B 1 146 TYR 146 146 146 TYR TYR B . n 
B 1 147 LYS 147 147 147 LYS LYS B . n 
B 1 148 LEU 148 148 148 LEU LEU B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 ARG 150 150 150 ARG ARG B . n 
B 1 151 ARG 151 151 151 ARG ARG B . n 
B 1 152 LEU 152 152 152 LEU LEU B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 PRO 154 154 154 PRO PRO B . n 
B 1 155 ASN 155 155 155 ASN ASN B . n 
B 1 156 SER 156 156 156 SER SER B . n 
B 1 157 GLN 157 157 157 GLN GLN B . n 
B 1 158 ILE 158 158 158 ILE ILE B . n 
B 1 159 ILE 159 159 159 ILE ILE B . n 
B 1 160 GLY 160 160 160 GLY GLY B . n 
B 1 161 PRO 161 161 161 PRO PRO B . n 
B 1 162 SER 162 162 162 SER SER B . n 
B 1 163 TYR 163 163 163 TYR TYR B . n 
B 1 164 SER 164 164 164 SER SER B . n 
B 1 165 TYR 165 165 165 TYR TYR B . n 
B 1 166 TYR 166 166 166 TYR TYR B . n 
B 1 167 ASN 167 167 167 ASN ASN B . n 
B 1 168 HIS 168 168 168 HIS HIS B . n 
B 1 169 TYR 169 169 169 TYR TYR B . n 
B 1 170 ASN 170 170 170 ASN ASN B . n 
B 1 171 MET 171 171 171 MET MET B . n 
B 1 172 ASN 172 172 172 ASN ASN B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 PHE 174 174 174 PHE PHE B . n 
B 1 175 LEU 175 175 175 LEU LEU B . n 
B 1 176 ASN 176 176 176 ASN ASN B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 CYS 178 178 178 CYS CYS B . n 
B 1 179 ARG 179 179 179 ARG ARG B . n 
B 1 180 ALA 180 180 180 ALA ALA B . n 
B 1 181 ASN 181 181 181 ASN ASN B . n 
B 1 182 ASN 182 182 182 ASN ASN B . n 
B 1 183 CYS 183 183 183 CYS CYS B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 PRO 185 185 185 PRO PRO B . n 
B 1 186 ASP 186 186 186 ASP ASP B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 ILE 188 188 188 ILE ILE B . n 
B 1 189 CYS 189 189 189 CYS CYS B . n 
B 1 190 TRP 190 190 190 TRP TRP B . n 
B 1 191 HIS 191 191 191 HIS HIS B . n 
B 1 192 GLU 192 192 192 GLU GLU B . n 
B 1 193 LEU 193 193 193 LEU LEU B . n 
B 1 194 GLY 194 194 194 GLY GLY B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 GLN 197 197 197 GLN GLN B . n 
B 1 198 ASN 198 198 198 ASN ASN B . n 
B 1 199 ILE 199 199 199 ILE ILE B . n 
B 1 200 SER 200 200 200 SER SER B . n 
B 1 201 GLY 201 201 201 GLY GLY B . n 
B 1 202 ASN 202 202 202 ASN ASN B . n 
B 1 203 ILE 203 203 203 ILE ILE B . n 
B 1 204 ARG 204 204 204 ARG ARG B . n 
B 1 205 ASP 205 205 205 ASP ASP B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 LYS 207 207 207 LYS LYS B . n 
B 1 208 THR 208 208 208 THR THR B . n 
B 1 209 LEU 209 209 209 LEU LEU B . n 
B 1 210 GLU 210 210 210 GLU GLU B . n 
B 1 211 ARG 211 211 211 ARG ARG B . n 
B 1 212 SER 212 212 212 SER SER B . n 
B 1 213 LEU 213 213 213 LEU LEU B . n 
B 1 214 GLY 214 214 214 GLY GLY B . n 
B 1 215 ILE 215 215 215 ILE ILE B . n 
B 1 216 PRO 216 216 216 PRO PRO B . n 
B 1 217 GLU 217 217 217 GLU GLU B . n 
B 1 218 ARG 218 218 218 ARG ARG B . n 
B 1 219 LYS 219 219 219 LYS LYS B . n 
B 1 220 ILE 220 220 220 ILE ILE B . n 
B 1 221 ALA 221 221 221 ALA ALA B . n 
B 1 222 ILE 222 222 222 ILE ILE B . n 
B 1 223 ASN 223 223 223 ASN ASN B . n 
B 1 224 GLU 224 224 224 GLU GLU B . n 
B 1 225 TYR 225 225 225 TYR TYR B . n 
B 1 226 SER 226 226 226 SER SER B . n 
B 1 227 ASP 227 227 227 ASP ASP B . n 
B 1 228 SER 228 228 228 SER SER B . n 
B 1 229 ASN 229 229 229 ASN ASN B . n 
B 1 230 HIS 230 230 230 HIS HIS B . n 
B 1 231 TYR 231 231 231 TYR TYR B . n 
B 1 232 ALA 232 232 232 ALA ALA B . n 
B 1 233 GLU 233 233 233 GLU GLU B . n 
B 1 234 GLY 234 234 234 GLY GLY B . n 
B 1 235 GLN 235 235 235 GLN GLN B . n 
B 1 236 PRO 236 236 236 PRO PRO B . n 
B 1 237 GLY 237 237 237 GLY GLY B . n 
B 1 238 ALA 238 238 238 ALA ALA B . n 
B 1 239 SER 239 239 239 SER SER B . n 
B 1 240 ALA 240 240 240 ALA ALA B . n 
B 1 241 PRO 241 241 241 PRO PRO B . n 
B 1 242 PHE 242 242 242 PHE PHE B . n 
B 1 243 ILE 243 243 243 ILE ILE B . n 
B 1 244 ALA 244 244 244 ALA ALA B . n 
B 1 245 LYS 245 245 245 LYS LYS B . n 
B 1 246 PHE 246 246 246 PHE PHE B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 ARG 248 248 248 ARG ARG B . n 
B 1 249 ASN 249 249 249 ASN ASN B . n 
B 1 250 LYS 250 250 250 LYS LYS 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 SER 253 253 253 SER SER B . n 
B 1 254 ALA 254 254 254 ALA ALA B . n 
B 1 255 CYS 255 255 255 CYS CYS B . n 
B 1 256 ILE 256 256 256 ILE ILE B . n 
B 1 257 SER 257 257 257 SER SER B . n 
B 1 258 TRP 258 258 258 TRP TRP B . n 
B 1 259 TRP 259 259 259 TRP TRP B . n 
B 1 260 TRP 260 260 260 TRP TRP B . n 
B 1 261 THR 261 261 261 THR THR B . n 
B 1 262 ASN 262 262 262 ASN ASN B . n 
B 1 263 ALA 263 263 263 ALA ALA B . n 
B 1 264 PRO 264 264 264 PRO PRO B . n 
B 1 265 GLY 265 265 265 GLY GLY B . n 
B 1 266 ARG 266 266 266 ARG ARG B . n 
B 1 267 LEU 267 267 267 LEU LEU B . n 
B 1 268 GLY 268 268 268 GLY GLY B . n 
B 1 269 SER 269 269 269 SER SER B . n 
B 1 270 LEU 270 270 270 LEU LEU B . n 
B 1 271 MET 271 271 271 MET MET B . n 
B 1 272 ALA 272 272 272 ALA ALA B . n 
B 1 273 SER 273 273 273 SER SER B . n 
B 1 274 ASP 274 274 274 ASP ASP B . n 
B 1 275 THR 275 275 275 THR THR B . n 
B 1 276 GLN 276 276 276 GLN GLN B . n 
B 1 277 LYS 277 277 277 LYS LYS B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 ALA 279 279 279 ALA ALA B . n 
B 1 280 GLY 280 280 280 GLY GLY B . n 
B 1 281 TRP 281 281 281 TRP TRP B . n 
B 1 282 TRP 282 282 282 TRP TRP B . n 
B 1 283 PHE 283 283 283 PHE PHE B . n 
B 1 284 TYR 284 284 284 TYR TYR B . n 
B 1 285 LYS 285 285 285 LYS LYS B . n 
B 1 286 TRP 286 286 286 TRP TRP B . n 
B 1 287 TYR 287 287 287 TYR TYR B . n 
B 1 288 GLY 288 288 288 GLY GLY B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 MET 290 290 290 MET MET B . n 
B 1 291 THR 291 291 291 THR THR B . n 
B 1 292 GLY 292 292 292 GLY GLY B . n 
B 1 293 ASN 293 293 293 ASN ASN B . n 
B 1 294 MET 294 294 294 MET MET B . n 
B 1 295 VAL 295 295 295 VAL VAL B . n 
B 1 296 ASN 296 296 296 ASN ASN B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 ILE 298 298 298 ILE ILE B . n 
B 1 299 PRO 299 299 299 PRO PRO B . n 
B 1 300 GLN 300 300 300 GLN GLN B . n 
B 1 301 ASN 301 301 301 ASN ASN B . n 
B 1 302 ASP 302 302 302 ASP ASP B . n 
B 1 303 ASN 303 303 303 ASN ASN B . n 
B 1 304 SER 304 304 304 SER SER B . n 
B 1 305 ASN 305 305 305 ASN ASN B . n 
B 1 306 LEU 306 306 306 LEU LEU B . n 
B 1 307 ALA 307 307 307 ALA ALA B . n 
B 1 308 ASP 308 308 308 ASP ASP B . n 
B 1 309 GLY 309 309 309 GLY GLY B . n 
B 1 310 PHE 310 310 310 PHE PHE B . n 
B 1 311 ALA 311 311 311 ALA ALA B . n 
B 1 312 CYS 312 312 312 CYS CYS B . n 
B 1 313 VAL 313 313 313 VAL VAL B . n 
B 1 314 ASP 314 314 314 ASP ASP 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 ALA 317 317 317 ALA ALA B . n 
B 1 318 LYS 318 318 318 LYS LYS B . n 
B 1 319 TYR 319 319 319 TYR TYR B . n 
B 1 320 ILE 320 320 320 ILE ILE B . n 
B 1 321 SER 321 321 321 SER SER B . n 
B 1 322 VAL 322 322 322 VAL VAL B . n 
B 1 323 LEU 323 323 323 LEU LEU B . n 
B 1 324 LEU 324 324 324 LEU LEU B . n 
B 1 325 GLY 325 325 325 GLY GLY B . n 
B 1 326 GLY 326 326 326 GLY GLY B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 ASN 328 328 328 ASN ASN B . n 
B 1 329 ASP 329 329 329 ASP ASP B . n 
B 1 330 GLY 330 330 330 GLY GLY B . n 
B 1 331 THR 331 331 331 THR THR B . n 
B 1 332 VAL 332 332 332 VAL VAL B . n 
B 1 333 ASN 333 333 333 ASN ASN B . n 
B 1 334 VAL 334 334 334 VAL VAL B . n 
B 1 335 ASN 335 335 335 ASN ASN B . n 
B 1 336 ILE 336 336 336 ILE ILE B . n 
B 1 337 LYS 337 337 337 LYS LYS B . n 
B 1 338 ASN 338 338 338 ASN ASN B . n 
B 1 339 ILE 339 339 339 ILE ILE B . n 
B 1 340 PRO 340 340 340 PRO PRO B . n 
B 1 341 ALA 341 341 341 ALA ALA B . n 
B 1 342 PHE 342 342 342 PHE PHE B . n 
B 1 343 ILE 343 343 343 ILE ILE B . n 
B 1 344 GLY 344 344 344 GLY GLY B . n 
B 1 345 SER 345 345 345 SER SER B . n 
B 1 346 SER 346 346 346 SER SER B . n 
B 1 347 ALA 347 347 347 ALA ALA B . n 
B 1 348 THR 348 348 348 THR THR B . n 
B 1 349 VAL 349 349 349 VAL VAL B . n 
B 1 350 LYS 350 350 350 LYS LYS B . n 
B 1 351 VAL 351 351 351 VAL VAL B . n 
B 1 352 GLU 352 352 352 GLU GLU B . n 
B 1 353 LYS 353 353 353 LYS LYS B . n 
B 1 354 VAL 354 354 354 VAL VAL B . n 
B 1 355 ASP 355 355 355 ASP ASP B . n 
B 1 356 TRP 356 356 356 TRP TRP B . n 
B 1 357 ASN 357 357 357 ASN ASN B . n 
B 1 358 GLY 358 358 358 GLY GLY B . n 
B 1 359 LYS 359 359 359 LYS LYS B . n 
B 1 360 ASP 360 360 360 ASP ASP B . n 
B 1 361 THR 361 361 361 THR THR B . n 
B 1 362 PRO 362 362 362 PRO PRO B . n 
B 1 363 VAL 363 363 363 VAL VAL B . n 
B 1 364 ASN 364 364 364 ASN ASN B . n 
B 1 365 GLY 365 365 365 GLY GLY B . n 
B 1 366 THR 366 366 366 THR THR B . n 
B 1 367 ASN 367 367 367 ASN ASN B . n 
B 1 368 THR 368 368 368 THR THR B . n 
B 1 369 VAL 369 369 369 VAL VAL B . n 
B 1 370 PHE 370 370 370 PHE PHE B . n 
B 1 371 SER 371 371 371 SER SER B . n 
B 1 372 LYS 372 372 372 LYS LYS B . n 
B 1 373 ARG 373 373 373 ARG ARG B . n 
B 1 374 TYR 374 374 374 TYR TYR B . n 
B 1 375 THR 375 375 375 THR THR B . n 
B 1 376 VAL 376 376 376 VAL VAL B . n 
B 1 377 SER 377 377 377 SER SER B . n 
B 1 378 ASN 378 378 378 ASN ASN B . n 
B 1 379 GLY 379 379 379 GLY GLY B . n 
B 1 380 THR 380 380 380 THR THR B . n 
B 1 381 ILE 381 381 381 ILE ILE B . n 
B 1 382 ASN 382 382 382 ASN ASN B . n 
B 1 383 VAL 383 383 383 VAL VAL B . n 
B 1 384 SER 384 384 384 SER SER B . n 
B 1 385 ILE 385 385 385 ILE ILE B . n 
B 1 386 PRO 386 386 386 PRO PRO B . n 
B 1 387 GLY 387 387 387 GLY GLY B . n 
B 1 388 THR 388 388 388 THR THR B . n 
B 1 389 ASN 389 389 389 ASN ASN B . n 
B 1 390 ASN 390 390 390 ASN ASN B . n 
B 1 391 THR 391 391 391 THR THR B . n 
B 1 392 SER 392 392 392 SER SER B . n 
B 1 393 GLY 393 393 393 GLY GLY B . n 
B 1 394 TYR 394 394 394 TYR TYR B . n 
B 1 395 ARG 395 395 395 ARG ARG B . n 
B 1 396 VAL 396 396 396 VAL VAL B . n 
B 1 397 TYR 397 397 397 TYR TYR B . n 
B 1 398 VAL 398 398 398 VAL VAL B . n 
B 1 399 SER 399 399 399 SER SER B . n 
B 1 400 ARG 400 400 400 ARG ARG B . n 
B 1 401 LEU 401 401 401 LEU LEU B . n 
B 1 402 GLU 402 402 ?   ?   ?   B . n 
B 1 403 HIS 403 403 ?   ?   ?   B . n 
B 1 404 HIS 404 404 ?   ?   ?   B . n 
B 1 405 HIS 405 405 ?   ?   ?   B . n 
B 1 406 HIS 406 406 ?   ?   ?   B . n 
B 1 407 HIS 407 407 ?   ?   ?   B . n 
B 1 408 HIS 408 408 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C  2 GOL 1   501  1   GOL GOL A . 
D  3 FMT 1   502  2   FMT FMT A . 
E  3 FMT 1   503  5   FMT FMT A . 
F  3 FMT 1   504  7   FMT FMT A . 
G  3 FMT 1   505  8   FMT FMT A . 
H  3 FMT 1   506  10  FMT FMT A . 
I  3 FMT 1   507  11  FMT FMT A . 
J  3 FMT 1   508  13  FMT FMT A . 
K  3 FMT 1   509  14  FMT FMT A . 
L  3 FMT 1   510  16  FMT FMT A . 
M  3 FMT 1   511  18  FMT FMT A . 
N  3 FMT 1   512  22  FMT FMT A . 
O  3 FMT 1   513  24  FMT FMT A . 
P  3 FMT 1   514  25  FMT FMT A . 
Q  3 FMT 1   515  27  FMT FMT A . 
R  3 FMT 1   516  29  FMT FMT A . 
S  3 FMT 1   517  31  FMT FMT A . 
T  4 PGE 1   501  501 PGE PGE B . 
U  2 GOL 1   502  2   GOL GOL B . 
V  2 GOL 1   503  3   GOL GOL B . 
W  5 BCN 1   504  1   BCN BCN B . 
X  3 FMT 1   505  1   FMT FMT B . 
Y  3 FMT 1   506  3   FMT FMT B . 
Z  3 FMT 1   507  4   FMT FMT B . 
AA 3 FMT 1   508  6   FMT FMT B . 
BA 3 FMT 1   509  9   FMT FMT B . 
CA 3 FMT 1   510  12  FMT FMT B . 
DA 3 FMT 1   511  15  FMT FMT B . 
EA 3 FMT 1   512  17  FMT FMT B . 
FA 3 FMT 1   513  19  FMT FMT B . 
GA 3 FMT 1   514  20  FMT FMT B . 
HA 3 FMT 1   515  21  FMT FMT B . 
IA 3 FMT 1   516  23  FMT FMT B . 
JA 3 FMT 1   517  26  FMT FMT B . 
KA 3 FMT 1   518  28  FMT FMT B . 
LA 3 FMT 1   519  30  FMT FMT B . 
MA 6 NA  1   520  1   NA  NA  B . 
NA 7 HOH 1   601  810 HOH HOH A . 
NA 7 HOH 2   602  787 HOH HOH A . 
NA 7 HOH 3   603  320 HOH HOH A . 
NA 7 HOH 4   604  752 HOH HOH A . 
NA 7 HOH 5   605  63  HOH HOH A . 
NA 7 HOH 6   606  318 HOH HOH A . 
NA 7 HOH 7   607  774 HOH HOH A . 
NA 7 HOH 8   608  808 HOH HOH A . 
NA 7 HOH 9   609  800 HOH HOH A . 
NA 7 HOH 10  610  644 HOH HOH A . 
NA 7 HOH 11  611  456 HOH HOH A . 
NA 7 HOH 12  612  606 HOH HOH A . 
NA 7 HOH 13  613  306 HOH HOH A . 
NA 7 HOH 14  614  169 HOH HOH A . 
NA 7 HOH 15  615  39  HOH HOH A . 
NA 7 HOH 16  616  768 HOH HOH A . 
NA 7 HOH 17  617  603 HOH HOH A . 
NA 7 HOH 18  618  702 HOH HOH A . 
NA 7 HOH 19  619  93  HOH HOH A . 
NA 7 HOH 20  620  669 HOH HOH A . 
NA 7 HOH 21  621  670 HOH HOH A . 
NA 7 HOH 22  622  634 HOH HOH A . 
NA 7 HOH 23  623  757 HOH HOH A . 
NA 7 HOH 24  624  687 HOH HOH A . 
NA 7 HOH 25  625  487 HOH HOH A . 
NA 7 HOH 26  626  617 HOH HOH A . 
NA 7 HOH 27  627  756 HOH HOH A . 
NA 7 HOH 28  628  759 HOH HOH A . 
NA 7 HOH 29  629  340 HOH HOH A . 
NA 7 HOH 30  630  57  HOH HOH A . 
NA 7 HOH 31  631  525 HOH HOH A . 
NA 7 HOH 32  632  511 HOH HOH A . 
NA 7 HOH 33  633  430 HOH HOH A . 
NA 7 HOH 34  634  130 HOH HOH A . 
NA 7 HOH 35  635  467 HOH HOH A . 
NA 7 HOH 36  636  5   HOH HOH A . 
NA 7 HOH 37  637  515 HOH HOH A . 
NA 7 HOH 38  638  868 HOH HOH A . 
NA 7 HOH 39  639  558 HOH HOH A . 
NA 7 HOH 40  640  107 HOH HOH A . 
NA 7 HOH 41  641  89  HOH HOH A . 
NA 7 HOH 42  642  478 HOH HOH A . 
NA 7 HOH 43  643  862 HOH HOH A . 
NA 7 HOH 44  644  494 HOH HOH A . 
NA 7 HOH 45  645  51  HOH HOH A . 
NA 7 HOH 46  646  296 HOH HOH A . 
NA 7 HOH 47  647  580 HOH HOH A . 
NA 7 HOH 48  648  227 HOH HOH A . 
NA 7 HOH 49  649  572 HOH HOH A . 
NA 7 HOH 50  650  685 HOH HOH A . 
NA 7 HOH 51  651  743 HOH HOH A . 
NA 7 HOH 52  652  119 HOH HOH A . 
NA 7 HOH 53  653  188 HOH HOH A . 
NA 7 HOH 54  654  528 HOH HOH A . 
NA 7 HOH 55  655  636 HOH HOH A . 
NA 7 HOH 56  656  650 HOH HOH A . 
NA 7 HOH 57  657  697 HOH HOH A . 
NA 7 HOH 58  658  858 HOH HOH A . 
NA 7 HOH 59  659  73  HOH HOH A . 
NA 7 HOH 60  660  624 HOH HOH A . 
NA 7 HOH 61  661  87  HOH HOH A . 
NA 7 HOH 62  662  235 HOH HOH A . 
NA 7 HOH 63  663  816 HOH HOH A . 
NA 7 HOH 64  664  648 HOH HOH A . 
NA 7 HOH 65  665  394 HOH HOH A . 
NA 7 HOH 66  666  203 HOH HOH A . 
NA 7 HOH 67  667  123 HOH HOH A . 
NA 7 HOH 68  668  491 HOH HOH A . 
NA 7 HOH 69  669  374 HOH HOH A . 
NA 7 HOH 70  670  472 HOH HOH A . 
NA 7 HOH 71  671  632 HOH HOH A . 
NA 7 HOH 72  672  139 HOH HOH A . 
NA 7 HOH 73  673  263 HOH HOH A . 
NA 7 HOH 74  674  76  HOH HOH A . 
NA 7 HOH 75  675  55  HOH HOH A . 
NA 7 HOH 76  676  23  HOH HOH A . 
NA 7 HOH 77  677  684 HOH HOH A . 
NA 7 HOH 78  678  331 HOH HOH A . 
NA 7 HOH 79  679  25  HOH HOH A . 
NA 7 HOH 80  680  112 HOH HOH A . 
NA 7 HOH 81  681  424 HOH HOH A . 
NA 7 HOH 82  682  542 HOH HOH A . 
NA 7 HOH 83  683  191 HOH HOH A . 
NA 7 HOH 84  684  778 HOH HOH A . 
NA 7 HOH 85  685  231 HOH HOH A . 
NA 7 HOH 86  686  479 HOH HOH A . 
NA 7 HOH 87  687  751 HOH HOH A . 
NA 7 HOH 88  688  270 HOH HOH A . 
NA 7 HOH 89  689  168 HOH HOH A . 
NA 7 HOH 90  690  613 HOH HOH A . 
NA 7 HOH 91  691  441 HOH HOH A . 
NA 7 HOH 92  692  597 HOH HOH A . 
NA 7 HOH 93  693  471 HOH HOH A . 
NA 7 HOH 94  694  527 HOH HOH A . 
NA 7 HOH 95  695  299 HOH HOH A . 
NA 7 HOH 96  696  740 HOH HOH A . 
NA 7 HOH 97  697  147 HOH HOH A . 
NA 7 HOH 98  698  240 HOH HOH A . 
NA 7 HOH 99  699  557 HOH HOH A . 
NA 7 HOH 100 700  408 HOH HOH A . 
NA 7 HOH 101 701  503 HOH HOH A . 
NA 7 HOH 102 702  91  HOH HOH A . 
NA 7 HOH 103 703  410 HOH HOH A . 
NA 7 HOH 104 704  750 HOH HOH A . 
NA 7 HOH 105 705  71  HOH HOH A . 
NA 7 HOH 106 706  9   HOH HOH A . 
NA 7 HOH 107 707  709 HOH HOH A . 
NA 7 HOH 108 708  167 HOH HOH A . 
NA 7 HOH 109 709  439 HOH HOH A . 
NA 7 HOH 110 710  546 HOH HOH A . 
NA 7 HOH 111 711  608 HOH HOH A . 
NA 7 HOH 112 712  548 HOH HOH A . 
NA 7 HOH 113 713  727 HOH HOH A . 
NA 7 HOH 114 714  532 HOH HOH A . 
NA 7 HOH 115 715  497 HOH HOH A . 
NA 7 HOH 116 716  545 HOH HOH A . 
NA 7 HOH 117 717  177 HOH HOH A . 
NA 7 HOH 118 718  719 HOH HOH A . 
NA 7 HOH 119 719  443 HOH HOH A . 
NA 7 HOH 120 720  56  HOH HOH A . 
NA 7 HOH 121 721  232 HOH HOH A . 
NA 7 HOH 122 722  559 HOH HOH A . 
NA 7 HOH 123 723  124 HOH HOH A . 
NA 7 HOH 124 724  594 HOH HOH A . 
NA 7 HOH 125 725  4   HOH HOH A . 
NA 7 HOH 126 726  397 HOH HOH A . 
NA 7 HOH 127 727  279 HOH HOH A . 
NA 7 HOH 128 728  290 HOH HOH A . 
NA 7 HOH 129 729  145 HOH HOH A . 
NA 7 HOH 130 730  432 HOH HOH A . 
NA 7 HOH 131 731  507 HOH HOH A . 
NA 7 HOH 132 732  790 HOH HOH A . 
NA 7 HOH 133 733  209 HOH HOH A . 
NA 7 HOH 134 734  245 HOH HOH A . 
NA 7 HOH 135 735  267 HOH HOH A . 
NA 7 HOH 136 736  534 HOH HOH A . 
NA 7 HOH 137 737  246 HOH HOH A . 
NA 7 HOH 138 738  861 HOH HOH A . 
NA 7 HOH 139 739  683 HOH HOH A . 
NA 7 HOH 140 740  413 HOH HOH A . 
NA 7 HOH 141 741  706 HOH HOH A . 
NA 7 HOH 142 742  414 HOH HOH A . 
NA 7 HOH 143 743  710 HOH HOH A . 
NA 7 HOH 144 744  600 HOH HOH A . 
NA 7 HOH 145 745  686 HOH HOH A . 
NA 7 HOH 146 746  238 HOH HOH A . 
NA 7 HOH 147 747  325 HOH HOH A . 
NA 7 HOH 148 748  536 HOH HOH A . 
NA 7 HOH 149 749  605 HOH HOH A . 
NA 7 HOH 150 750  666 HOH HOH A . 
NA 7 HOH 151 751  452 HOH HOH A . 
NA 7 HOH 152 752  126 HOH HOH A . 
NA 7 HOH 153 753  391 HOH HOH A . 
NA 7 HOH 154 754  423 HOH HOH A . 
NA 7 HOH 155 755  222 HOH HOH A . 
NA 7 HOH 156 756  387 HOH HOH A . 
NA 7 HOH 157 757  183 HOH HOH A . 
NA 7 HOH 158 758  22  HOH HOH A . 
NA 7 HOH 159 759  257 HOH HOH A . 
NA 7 HOH 160 760  278 HOH HOH A . 
NA 7 HOH 161 761  571 HOH HOH A . 
NA 7 HOH 162 762  193 HOH HOH A . 
NA 7 HOH 163 763  2   HOH HOH A . 
NA 7 HOH 164 764  164 HOH HOH A . 
NA 7 HOH 165 765  671 HOH HOH A . 
NA 7 HOH 166 766  36  HOH HOH A . 
NA 7 HOH 167 767  365 HOH HOH A . 
NA 7 HOH 168 768  434 HOH HOH A . 
NA 7 HOH 169 769  258 HOH HOH A . 
NA 7 HOH 170 770  854 HOH HOH A . 
NA 7 HOH 171 771  393 HOH HOH A . 
NA 7 HOH 172 772  476 HOH HOH A . 
NA 7 HOH 173 773  451 HOH HOH A . 
NA 7 HOH 174 774  495 HOH HOH A . 
NA 7 HOH 175 775  596 HOH HOH A . 
NA 7 HOH 176 776  659 HOH HOH A . 
NA 7 HOH 177 777  477 HOH HOH A . 
NA 7 HOH 178 778  131 HOH HOH A . 
NA 7 HOH 179 779  70  HOH HOH A . 
NA 7 HOH 180 780  199 HOH HOH A . 
NA 7 HOH 181 781  292 HOH HOH A . 
NA 7 HOH 182 782  744 HOH HOH A . 
NA 7 HOH 183 783  132 HOH HOH A . 
NA 7 HOH 184 784  412 HOH HOH A . 
NA 7 HOH 185 785  143 HOH HOH A . 
NA 7 HOH 186 786  777 HOH HOH A . 
NA 7 HOH 187 787  260 HOH HOH A . 
NA 7 HOH 188 788  215 HOH HOH A . 
NA 7 HOH 189 789  593 HOH HOH A . 
NA 7 HOH 190 790  573 HOH HOH A . 
NA 7 HOH 191 791  224 HOH HOH A . 
NA 7 HOH 192 792  425 HOH HOH A . 
NA 7 HOH 193 793  7   HOH HOH A . 
NA 7 HOH 194 794  513 HOH HOH A . 
NA 7 HOH 195 795  178 HOH HOH A . 
NA 7 HOH 196 796  386 HOH HOH A . 
NA 7 HOH 197 797  388 HOH HOH A . 
NA 7 HOH 198 798  544 HOH HOH A . 
NA 7 HOH 199 799  392 HOH HOH A . 
NA 7 HOH 200 800  426 HOH HOH A . 
NA 7 HOH 201 801  856 HOH HOH A . 
NA 7 HOH 202 802  739 HOH HOH A . 
NA 7 HOH 203 803  38  HOH HOH A . 
NA 7 HOH 204 804  541 HOH HOH A . 
NA 7 HOH 205 805  149 HOH HOH A . 
NA 7 HOH 206 806  111 HOH HOH A . 
NA 7 HOH 207 807  90  HOH HOH A . 
NA 7 HOH 208 808  213 HOH HOH A . 
NA 7 HOH 209 809  464 HOH HOH A . 
NA 7 HOH 210 810  206 HOH HOH A . 
NA 7 HOH 211 811  120 HOH HOH A . 
NA 7 HOH 212 812  274 HOH HOH A . 
NA 7 HOH 213 813  773 HOH HOH A . 
NA 7 HOH 214 814  501 HOH HOH A . 
NA 7 HOH 215 815  485 HOH HOH A . 
NA 7 HOH 216 816  24  HOH HOH A . 
NA 7 HOH 217 817  672 HOH HOH A . 
NA 7 HOH 218 818  159 HOH HOH A . 
NA 7 HOH 219 819  623 HOH HOH A . 
NA 7 HOH 220 820  309 HOH HOH A . 
NA 7 HOH 221 821  255 HOH HOH A . 
NA 7 HOH 222 822  661 HOH HOH A . 
NA 7 HOH 223 823  136 HOH HOH A . 
NA 7 HOH 224 824  269 HOH HOH A . 
NA 7 HOH 225 825  233 HOH HOH A . 
NA 7 HOH 226 826  307 HOH HOH A . 
NA 7 HOH 227 827  335 HOH HOH A . 
NA 7 HOH 228 828  415 HOH HOH A . 
NA 7 HOH 229 829  212 HOH HOH A . 
NA 7 HOH 230 830  433 HOH HOH A . 
NA 7 HOH 231 831  34  HOH HOH A . 
NA 7 HOH 232 832  755 HOH HOH A . 
NA 7 HOH 233 833  550 HOH HOH A . 
NA 7 HOH 234 834  170 HOH HOH A . 
NA 7 HOH 235 835  599 HOH HOH A . 
NA 7 HOH 236 836  530 HOH HOH A . 
NA 7 HOH 237 837  303 HOH HOH A . 
NA 7 HOH 238 838  465 HOH HOH A . 
NA 7 HOH 239 839  259 HOH HOH A . 
NA 7 HOH 240 840  35  HOH HOH A . 
NA 7 HOH 241 841  869 HOH HOH A . 
NA 7 HOH 242 842  389 HOH HOH A . 
NA 7 HOH 243 843  616 HOH HOH A . 
NA 7 HOH 244 844  83  HOH HOH A . 
NA 7 HOH 245 845  137 HOH HOH A . 
NA 7 HOH 246 846  745 HOH HOH A . 
NA 7 HOH 247 847  241 HOH HOH A . 
NA 7 HOH 248 848  758 HOH HOH A . 
NA 7 HOH 249 849  803 HOH HOH A . 
NA 7 HOH 250 850  496 HOH HOH A . 
NA 7 HOH 251 851  543 HOH HOH A . 
NA 7 HOH 252 852  286 HOH HOH A . 
NA 7 HOH 253 853  668 HOH HOH A . 
NA 7 HOH 254 854  427 HOH HOH A . 
NA 7 HOH 255 855  418 HOH HOH A . 
NA 7 HOH 256 856  219 HOH HOH A . 
NA 7 HOH 257 857  355 HOH HOH A . 
NA 7 HOH 258 858  277 HOH HOH A . 
NA 7 HOH 259 859  181 HOH HOH A . 
NA 7 HOH 260 860  310 HOH HOH A . 
NA 7 HOH 261 861  179 HOH HOH A . 
NA 7 HOH 262 862  64  HOH HOH A . 
NA 7 HOH 263 863  488 HOH HOH A . 
NA 7 HOH 264 864  870 HOH HOH A . 
NA 7 HOH 265 865  180 HOH HOH A . 
NA 7 HOH 266 866  229 HOH HOH A . 
NA 7 HOH 267 867  490 HOH HOH A . 
NA 7 HOH 268 868  598 HOH HOH A . 
NA 7 HOH 269 869  12  HOH HOH A . 
NA 7 HOH 270 870  629 HOH HOH A . 
NA 7 HOH 271 871  555 HOH HOH A . 
NA 7 HOH 272 872  688 HOH HOH A . 
NA 7 HOH 273 873  788 HOH HOH A . 
NA 7 HOH 274 874  398 HOH HOH A . 
NA 7 HOH 275 875  121 HOH HOH A . 
NA 7 HOH 276 876  37  HOH HOH A . 
NA 7 HOH 277 877  381 HOH HOH A . 
NA 7 HOH 278 878  151 HOH HOH A . 
NA 7 HOH 279 879  734 HOH HOH A . 
NA 7 HOH 280 880  419 HOH HOH A . 
NA 7 HOH 281 881  457 HOH HOH A . 
NA 7 HOH 282 882  458 HOH HOH A . 
NA 7 HOH 283 883  81  HOH HOH A . 
NA 7 HOH 284 884  872 HOH HOH A . 
NA 7 HOH 285 885  442 HOH HOH A . 
NA 7 HOH 286 886  67  HOH HOH A . 
NA 7 HOH 287 887  567 HOH HOH A . 
NA 7 HOH 288 888  422 HOH HOH A . 
NA 7 HOH 289 889  294 HOH HOH A . 
NA 7 HOH 290 890  547 HOH HOH A . 
NA 7 HOH 291 891  522 HOH HOH A . 
NA 7 HOH 292 892  321 HOH HOH A . 
NA 7 HOH 293 893  863 HOH HOH A . 
NA 7 HOH 294 894  483 HOH HOH A . 
NA 7 HOH 295 895  509 HOH HOH A . 
NA 7 HOH 296 896  265 HOH HOH A . 
NA 7 HOH 297 897  730 HOH HOH A . 
NA 7 HOH 298 898  377 HOH HOH A . 
NA 7 HOH 299 899  848 HOH HOH A . 
NA 7 HOH 300 900  853 HOH HOH A . 
NA 7 HOH 301 901  289 HOH HOH A . 
NA 7 HOH 302 902  13  HOH HOH A . 
NA 7 HOH 303 903  592 HOH HOH A . 
NA 7 HOH 304 904  622 HOH HOH A . 
NA 7 HOH 305 905  529 HOH HOH A . 
NA 7 HOH 306 906  444 HOH HOH A . 
NA 7 HOH 307 907  266 HOH HOH A . 
NA 7 HOH 308 908  125 HOH HOH A . 
NA 7 HOH 309 909  737 HOH HOH A . 
NA 7 HOH 310 910  673 HOH HOH A . 
NA 7 HOH 311 911  186 HOH HOH A . 
NA 7 HOH 312 912  280 HOH HOH A . 
NA 7 HOH 313 913  570 HOH HOH A . 
NA 7 HOH 314 914  162 HOH HOH A . 
NA 7 HOH 315 915  724 HOH HOH A . 
NA 7 HOH 316 916  844 HOH HOH A . 
NA 7 HOH 317 917  486 HOH HOH A . 
NA 7 HOH 318 918  459 HOH HOH A . 
NA 7 HOH 319 919  539 HOH HOH A . 
NA 7 HOH 320 920  821 HOH HOH A . 
NA 7 HOH 321 921  308 HOH HOH A . 
NA 7 HOH 322 922  820 HOH HOH A . 
NA 7 HOH 323 923  218 HOH HOH A . 
NA 7 HOH 324 924  855 HOH HOH A . 
NA 7 HOH 325 925  30  HOH HOH A . 
NA 7 HOH 326 926  329 HOH HOH A . 
NA 7 HOH 327 927  237 HOH HOH A . 
NA 7 HOH 328 928  300 HOH HOH A . 
NA 7 HOH 329 929  217 HOH HOH A . 
NA 7 HOH 330 930  689 HOH HOH A . 
NA 7 HOH 331 931  86  HOH HOH A . 
NA 7 HOH 332 932  721 HOH HOH A . 
NA 7 HOH 333 933  714 HOH HOH A . 
NA 7 HOH 334 934  690 HOH HOH A . 
NA 7 HOH 335 935  674 HOH HOH A . 
NA 7 HOH 336 936  211 HOH HOH A . 
NA 7 HOH 337 937  366 HOH HOH A . 
NA 7 HOH 338 938  440 HOH HOH A . 
NA 7 HOH 339 939  304 HOH HOH A . 
NA 7 HOH 340 940  801 HOH HOH A . 
NA 7 HOH 341 941  637 HOH HOH A . 
NA 7 HOH 342 942  368 HOH HOH A . 
NA 7 HOH 343 943  678 HOH HOH A . 
NA 7 HOH 344 944  342 HOH HOH A . 
NA 7 HOH 345 945  117 HOH HOH A . 
NA 7 HOH 346 946  828 HOH HOH A . 
NA 7 HOH 347 947  113 HOH HOH A . 
NA 7 HOH 348 948  562 HOH HOH A . 
NA 7 HOH 349 949  353 HOH HOH A . 
NA 7 HOH 350 950  72  HOH HOH A . 
NA 7 HOH 351 951  604 HOH HOH A . 
NA 7 HOH 352 952  323 HOH HOH A . 
NA 7 HOH 353 953  332 HOH HOH A . 
NA 7 HOH 354 954  78  HOH HOH A . 
NA 7 HOH 355 955  328 HOH HOH A . 
NA 7 HOH 356 956  450 HOH HOH A . 
NA 7 HOH 357 957  866 HOH HOH A . 
NA 7 HOH 358 958  549 HOH HOH A . 
NA 7 HOH 359 959  786 HOH HOH A . 
NA 7 HOH 360 960  254 HOH HOH A . 
NA 7 HOH 361 961  799 HOH HOH A . 
NA 7 HOH 362 962  103 HOH HOH A . 
NA 7 HOH 363 963  316 HOH HOH A . 
NA 7 HOH 364 964  359 HOH HOH A . 
NA 7 HOH 365 965  635 HOH HOH A . 
NA 7 HOH 366 966  846 HOH HOH A . 
NA 7 HOH 367 967  764 HOH HOH A . 
NA 7 HOH 368 968  156 HOH HOH A . 
NA 7 HOH 369 969  336 HOH HOH A . 
NA 7 HOH 370 970  194 HOH HOH A . 
NA 7 HOH 371 971  192 HOH HOH A . 
NA 7 HOH 372 972  802 HOH HOH A . 
NA 7 HOH 373 973  351 HOH HOH A . 
NA 7 HOH 374 974  346 HOH HOH A . 
NA 7 HOH 375 975  205 HOH HOH A . 
NA 7 HOH 376 976  371 HOH HOH A . 
NA 7 HOH 377 977  707 HOH HOH A . 
NA 7 HOH 378 978  313 HOH HOH A . 
NA 7 HOH 379 979  806 HOH HOH A . 
NA 7 HOH 380 980  717 HOH HOH A . 
NA 7 HOH 381 981  805 HOH HOH A . 
NA 7 HOH 382 982  809 HOH HOH A . 
NA 7 HOH 383 983  88  HOH HOH A . 
NA 7 HOH 384 984  794 HOH HOH A . 
NA 7 HOH 385 985  364 HOH HOH A . 
NA 7 HOH 386 986  102 HOH HOH A . 
NA 7 HOH 387 987  97  HOH HOH A . 
NA 7 HOH 388 988  185 HOH HOH A . 
NA 7 HOH 389 989  110 HOH HOH A . 
NA 7 HOH 390 990  795 HOH HOH A . 
NA 7 HOH 391 991  220 HOH HOH A . 
NA 7 HOH 392 992  95  HOH HOH A . 
NA 7 HOH 393 993  348 HOH HOH A . 
NA 7 HOH 394 994  77  HOH HOH A . 
NA 7 HOH 395 995  595 HOH HOH A . 
NA 7 HOH 396 996  713 HOH HOH A . 
NA 7 HOH 397 997  578 HOH HOH A . 
NA 7 HOH 398 998  819 HOH HOH A . 
NA 7 HOH 399 999  831 HOH HOH A . 
NA 7 HOH 400 1000 298 HOH HOH A . 
NA 7 HOH 401 1001 109 HOH HOH A . 
NA 7 HOH 402 1002 830 HOH HOH A . 
NA 7 HOH 403 1003 781 HOH HOH A . 
NA 7 HOH 404 1004 609 HOH HOH A . 
NA 7 HOH 405 1005 242 HOH HOH A . 
NA 7 HOH 406 1006 370 HOH HOH A . 
NA 7 HOH 407 1007 815 HOH HOH A . 
NA 7 HOH 408 1008 382 HOH HOH A . 
NA 7 HOH 409 1009 349 HOH HOH A . 
NA 7 HOH 410 1010 698 HOH HOH A . 
NA 7 HOH 411 1011 118 HOH HOH A . 
NA 7 HOH 412 1012 369 HOH HOH A . 
NA 7 HOH 413 1013 343 HOH HOH A . 
NA 7 HOH 414 1014 765 HOH HOH A . 
NA 7 HOH 415 1015 312 HOH HOH A . 
NA 7 HOH 416 1016 172 HOH HOH A . 
NA 7 HOH 417 1017 645 HOH HOH A . 
NA 7 HOH 418 1018 276 HOH HOH A . 
NA 7 HOH 419 1019 104 HOH HOH A . 
NA 7 HOH 420 1020 796 HOH HOH A . 
NA 7 HOH 421 1021 345 HOH HOH A . 
NA 7 HOH 422 1022 98  HOH HOH A . 
NA 7 HOH 423 1023 519 HOH HOH A . 
NA 7 HOH 424 1024 358 HOH HOH A . 
NA 7 HOH 425 1025 354 HOH HOH A . 
NA 7 HOH 426 1026 865 HOH HOH A . 
NA 7 HOH 427 1027 250 HOH HOH A . 
NA 7 HOH 428 1028 202 HOH HOH A . 
NA 7 HOH 429 1029 776 HOH HOH A . 
NA 7 HOH 430 1030 344 HOH HOH A . 
NA 7 HOH 431 1031 262 HOH HOH A . 
NA 7 HOH 432 1032 352 HOH HOH A . 
NA 7 HOH 433 1033 766 HOH HOH A . 
NA 7 HOH 434 1034 341 HOH HOH A . 
NA 7 HOH 435 1035 100 HOH HOH A . 
OA 7 HOH 1   601  857 HOH HOH B . 
OA 7 HOH 2   602  334 HOH HOH B . 
OA 7 HOH 3   603  295 HOH HOH B . 
OA 7 HOH 4   604  319 HOH HOH B . 
OA 7 HOH 5   605  85  HOH HOH B . 
OA 7 HOH 6   606  747 HOH HOH B . 
OA 7 HOH 7   607  705 HOH HOH B . 
OA 7 HOH 8   608  797 HOH HOH B . 
OA 7 HOH 9   609  80  HOH HOH B . 
OA 7 HOH 10  610  326 HOH HOH B . 
OA 7 HOH 11  611  322 HOH HOH B . 
OA 7 HOH 12  612  223 HOH HOH B . 
OA 7 HOH 13  613  663 HOH HOH B . 
OA 7 HOH 14  614  762 HOH HOH B . 
OA 7 HOH 15  615  533 HOH HOH B . 
OA 7 HOH 16  616  474 HOH HOH B . 
OA 7 HOH 17  617  696 HOH HOH B . 
OA 7 HOH 18  618  48  HOH HOH B . 
OA 7 HOH 19  619  116 HOH HOH B . 
OA 7 HOH 20  620  626 HOH HOH B . 
OA 7 HOH 21  621  760 HOH HOH B . 
OA 7 HOH 22  622  842 HOH HOH B . 
OA 7 HOH 23  623  579 HOH HOH B . 
OA 7 HOH 24  624  305 HOH HOH B . 
OA 7 HOH 25  625  293 HOH HOH B . 
OA 7 HOH 26  626  317 HOH HOH B . 
OA 7 HOH 27  627  282 HOH HOH B . 
OA 7 HOH 28  628  284 HOH HOH B . 
OA 7 HOH 29  629  144 HOH HOH B . 
OA 7 HOH 30  630  176 HOH HOH B . 
OA 7 HOH 31  631  171 HOH HOH B . 
OA 7 HOH 32  632  66  HOH HOH B . 
OA 7 HOH 33  633  157 HOH HOH B . 
OA 7 HOH 34  634  461 HOH HOH B . 
OA 7 HOH 35  635  625 HOH HOH B . 
OA 7 HOH 36  636  153 HOH HOH B . 
OA 7 HOH 37  637  641 HOH HOH B . 
OA 7 HOH 38  638  615 HOH HOH B . 
OA 7 HOH 39  639  268 HOH HOH B . 
OA 7 HOH 40  640  664 HOH HOH B . 
OA 7 HOH 41  641  208 HOH HOH B . 
OA 7 HOH 42  642  196 HOH HOH B . 
OA 7 HOH 43  643  665 HOH HOH B . 
OA 7 HOH 44  644  249 HOH HOH B . 
OA 7 HOH 45  645  234 HOH HOH B . 
OA 7 HOH 46  646  272 HOH HOH B . 
OA 7 HOH 47  647  500 HOH HOH B . 
OA 7 HOH 48  648  556 HOH HOH B . 
OA 7 HOH 49  649  19  HOH HOH B . 
OA 7 HOH 50  650  161 HOH HOH B . 
OA 7 HOH 51  651  660 HOH HOH B . 
OA 7 HOH 52  652  421 HOH HOH B . 
OA 7 HOH 53  653  493 HOH HOH B . 
OA 7 HOH 54  654  428 HOH HOH B . 
OA 7 HOH 55  655  568 HOH HOH B . 
OA 7 HOH 56  656  138 HOH HOH B . 
OA 7 HOH 57  657  53  HOH HOH B . 
OA 7 HOH 58  658  723 HOH HOH B . 
OA 7 HOH 59  659  867 HOH HOH B . 
OA 7 HOH 60  660  736 HOH HOH B . 
OA 7 HOH 61  661  512 HOH HOH B . 
OA 7 HOH 62  662  402 HOH HOH B . 
OA 7 HOH 63  663  807 HOH HOH B . 
OA 7 HOH 64  664  482 HOH HOH B . 
OA 7 HOH 65  665  538 HOH HOH B . 
OA 7 HOH 66  666  449 HOH HOH B . 
OA 7 HOH 67  667  469 HOH HOH B . 
OA 7 HOH 68  668  521 HOH HOH B . 
OA 7 HOH 69  669  148 HOH HOH B . 
OA 7 HOH 70  670  404 HOH HOH B . 
OA 7 HOH 71  671  189 HOH HOH B . 
OA 7 HOH 72  672  720 HOH HOH B . 
OA 7 HOH 73  673  96  HOH HOH B . 
OA 7 HOH 74  674  411 HOH HOH B . 
OA 7 HOH 75  675  560 HOH HOH B . 
OA 7 HOH 76  676  436 HOH HOH B . 
OA 7 HOH 77  677  253 HOH HOH B . 
OA 7 HOH 78  678  682 HOH HOH B . 
OA 7 HOH 79  679  68  HOH HOH B . 
OA 7 HOH 80  680  742 HOH HOH B . 
OA 7 HOH 81  681  761 HOH HOH B . 
OA 7 HOH 82  682  225 HOH HOH B . 
OA 7 HOH 83  683  535 HOH HOH B . 
OA 7 HOH 84  684  611 HOH HOH B . 
OA 7 HOH 85  685  62  HOH HOH B . 
OA 7 HOH 86  686  447 HOH HOH B . 
OA 7 HOH 87  687  204 HOH HOH B . 
OA 7 HOH 88  688  463 HOH HOH B . 
OA 7 HOH 89  689  333 HOH HOH B . 
OA 7 HOH 90  690  58  HOH HOH B . 
OA 7 HOH 91  691  492 HOH HOH B . 
OA 7 HOH 92  692  589 HOH HOH B . 
OA 7 HOH 93  693  642 HOH HOH B . 
OA 7 HOH 94  694  462 HOH HOH B . 
OA 7 HOH 95  695  827 HOH HOH B . 
OA 7 HOH 96  696  619 HOH HOH B . 
OA 7 HOH 97  697  643 HOH HOH B . 
OA 7 HOH 98  698  28  HOH HOH B . 
OA 7 HOH 99  699  627 HOH HOH B . 
OA 7 HOH 100 700  417 HOH HOH B . 
OA 7 HOH 101 701  448 HOH HOH B . 
OA 7 HOH 102 702  399 HOH HOH B . 
OA 7 HOH 103 703  230 HOH HOH B . 
OA 7 HOH 104 704  429 HOH HOH B . 
OA 7 HOH 105 705  173 HOH HOH B . 
OA 7 HOH 106 706  409 HOH HOH B . 
OA 7 HOH 107 707  575 HOH HOH B . 
OA 7 HOH 108 708  32  HOH HOH B . 
OA 7 HOH 109 709  6   HOH HOH B . 
OA 7 HOH 110 710  45  HOH HOH B . 
OA 7 HOH 111 711  871 HOH HOH B . 
OA 7 HOH 112 712  396 HOH HOH B . 
OA 7 HOH 113 713  174 HOH HOH B . 
OA 7 HOH 114 714  480 HOH HOH B . 
OA 7 HOH 115 715  587 HOH HOH B . 
OA 7 HOH 116 716  244 HOH HOH B . 
OA 7 HOH 117 717  475 HOH HOH B . 
OA 7 HOH 118 718  201 HOH HOH B . 
OA 7 HOH 119 719  746 HOH HOH B . 
OA 7 HOH 120 720  187 HOH HOH B . 
OA 7 HOH 121 721  134 HOH HOH B . 
OA 7 HOH 122 722  822 HOH HOH B . 
OA 7 HOH 123 723  271 HOH HOH B . 
OA 7 HOH 124 724  505 HOH HOH B . 
OA 7 HOH 125 725  401 HOH HOH B . 
OA 7 HOH 126 726  407 HOH HOH B . 
OA 7 HOH 127 727  711 HOH HOH B . 
OA 7 HOH 128 728  691 HOH HOH B . 
OA 7 HOH 129 729  564 HOH HOH B . 
OA 7 HOH 130 730  517 HOH HOH B . 
OA 7 HOH 131 731  551 HOH HOH B . 
OA 7 HOH 132 732  518 HOH HOH B . 
OA 7 HOH 133 733  566 HOH HOH B . 
OA 7 HOH 134 734  42  HOH HOH B . 
OA 7 HOH 135 735  275 HOH HOH B . 
OA 7 HOH 136 736  537 HOH HOH B . 
OA 7 HOH 137 737  630 HOH HOH B . 
OA 7 HOH 138 738  638 HOH HOH B . 
OA 7 HOH 139 739  453 HOH HOH B . 
OA 7 HOH 140 740  26  HOH HOH B . 
OA 7 HOH 141 741  214 HOH HOH B . 
OA 7 HOH 142 742  420 HOH HOH B . 
OA 7 HOH 143 743  29  HOH HOH B . 
OA 7 HOH 144 744  693 HOH HOH B . 
OA 7 HOH 145 745  302 HOH HOH B . 
OA 7 HOH 146 746  591 HOH HOH B . 
OA 7 HOH 147 747  190 HOH HOH B . 
OA 7 HOH 148 748  510 HOH HOH B . 
OA 7 HOH 149 749  699 HOH HOH B . 
OA 7 HOH 150 750  163 HOH HOH B . 
OA 7 HOH 151 751  105 HOH HOH B . 
OA 7 HOH 152 752  84  HOH HOH B . 
OA 7 HOH 153 753  792 HOH HOH B . 
OA 7 HOH 154 754  251 HOH HOH B . 
OA 7 HOH 155 755  405 HOH HOH B . 
OA 7 HOH 156 756  455 HOH HOH B . 
OA 7 HOH 157 757  129 HOH HOH B . 
OA 7 HOH 158 758  197 HOH HOH B . 
OA 7 HOH 159 759  283 HOH HOH B . 
OA 7 HOH 160 760  264 HOH HOH B . 
OA 7 HOH 161 761  675 HOH HOH B . 
OA 7 HOH 162 762  715 HOH HOH B . 
OA 7 HOH 163 763  8   HOH HOH B . 
OA 7 HOH 164 764  140 HOH HOH B . 
OA 7 HOH 165 765  252 HOH HOH B . 
OA 7 HOH 166 766  400 HOH HOH B . 
OA 7 HOH 167 767  621 HOH HOH B . 
OA 7 HOH 168 768  216 HOH HOH B . 
OA 7 HOH 169 769  390 HOH HOH B . 
OA 7 HOH 170 770  701 HOH HOH B . 
OA 7 HOH 171 771  531 HOH HOH B . 
OA 7 HOH 172 772  155 HOH HOH B . 
OA 7 HOH 173 773  601 HOH HOH B . 
OA 7 HOH 174 774  330 HOH HOH B . 
OA 7 HOH 175 775  502 HOH HOH B . 
OA 7 HOH 176 776  122 HOH HOH B . 
OA 7 HOH 177 777  59  HOH HOH B . 
OA 7 HOH 178 778  639 HOH HOH B . 
OA 7 HOH 179 779  523 HOH HOH B . 
OA 7 HOH 180 780  823 HOH HOH B . 
OA 7 HOH 181 781  446 HOH HOH B . 
OA 7 HOH 182 782  708 HOH HOH B . 
OA 7 HOH 183 783  716 HOH HOH B . 
OA 7 HOH 184 784  584 HOH HOH B . 
OA 7 HOH 185 785  561 HOH HOH B . 
OA 7 HOH 186 786  783 HOH HOH B . 
OA 7 HOH 187 787  859 HOH HOH B . 
OA 7 HOH 188 788  775 HOH HOH B . 
OA 7 HOH 189 789  798 HOH HOH B . 
OA 7 HOH 190 790  677 HOH HOH B . 
OA 7 HOH 191 791  614 HOH HOH B . 
OA 7 HOH 192 792  826 HOH HOH B . 
OA 7 HOH 193 793  445 HOH HOH B . 
OA 7 HOH 194 794  437 HOH HOH B . 
OA 7 HOH 195 795  395 HOH HOH B . 
OA 7 HOH 196 796  514 HOH HOH B . 
OA 7 HOH 197 797  40  HOH HOH B . 
OA 7 HOH 198 798  226 HOH HOH B . 
OA 7 HOH 199 799  748 HOH HOH B . 
OA 7 HOH 200 800  281 HOH HOH B . 
OA 7 HOH 201 801  288 HOH HOH B . 
OA 7 HOH 202 802  248 HOH HOH B . 
OA 7 HOH 203 803  44  HOH HOH B . 
OA 7 HOH 204 804  158 HOH HOH B . 
OA 7 HOH 205 805  239 HOH HOH B . 
OA 7 HOH 206 806  154 HOH HOH B . 
OA 7 HOH 207 807  484 HOH HOH B . 
OA 7 HOH 208 808  466 HOH HOH B . 
OA 7 HOH 209 809  454 HOH HOH B . 
OA 7 HOH 210 810  504 HOH HOH B . 
OA 7 HOH 211 811  301 HOH HOH B . 
OA 7 HOH 212 812  207 HOH HOH B . 
OA 7 HOH 213 813  838 HOH HOH B . 
OA 7 HOH 214 814  749 HOH HOH B . 
OA 7 HOH 215 815  704 HOH HOH B . 
OA 7 HOH 216 816  754 HOH HOH B . 
OA 7 HOH 217 817  221 HOH HOH B . 
OA 7 HOH 218 818  835 HOH HOH B . 
OA 7 HOH 219 819  470 HOH HOH B . 
OA 7 HOH 220 820  27  HOH HOH B . 
OA 7 HOH 221 821  640 HOH HOH B . 
OA 7 HOH 222 822  725 HOH HOH B . 
OA 7 HOH 223 823  106 HOH HOH B . 
OA 7 HOH 224 824  553 HOH HOH B . 
OA 7 HOH 225 825  694 HOH HOH B . 
OA 7 HOH 226 826  836 HOH HOH B . 
OA 7 HOH 227 827  11  HOH HOH B . 
OA 7 HOH 228 828  3   HOH HOH B . 
OA 7 HOH 229 829  135 HOH HOH B . 
OA 7 HOH 230 830  569 HOH HOH B . 
OA 7 HOH 231 831  406 HOH HOH B . 
OA 7 HOH 232 832  438 HOH HOH B . 
OA 7 HOH 233 833  128 HOH HOH B . 
OA 7 HOH 234 834  726 HOH HOH B . 
OA 7 HOH 235 835  498 HOH HOH B . 
OA 7 HOH 236 836  837 HOH HOH B . 
OA 7 HOH 237 837  273 HOH HOH B . 
OA 7 HOH 238 838  236 HOH HOH B . 
OA 7 HOH 239 839  738 HOH HOH B . 
OA 7 HOH 240 840  499 HOH HOH B . 
OA 7 HOH 241 841  228 HOH HOH B . 
OA 7 HOH 242 842  385 HOH HOH B . 
OA 7 HOH 243 843  261 HOH HOH B . 
OA 7 HOH 244 844  247 HOH HOH B . 
OA 7 HOH 245 845  435 HOH HOH B . 
OA 7 HOH 246 846  655 HOH HOH B . 
OA 7 HOH 247 847  516 HOH HOH B . 
OA 7 HOH 248 848  520 HOH HOH B . 
OA 7 HOH 249 849  574 HOH HOH B . 
OA 7 HOH 250 850  658 HOH HOH B . 
OA 7 HOH 251 851  847 HOH HOH B . 
OA 7 HOH 252 852  667 HOH HOH B . 
OA 7 HOH 253 853  146 HOH HOH B . 
OA 7 HOH 254 854  49  HOH HOH B . 
OA 7 HOH 255 855  602 HOH HOH B . 
OA 7 HOH 256 856  612 HOH HOH B . 
OA 7 HOH 257 857  833 HOH HOH B . 
OA 7 HOH 258 858  607 HOH HOH B . 
OA 7 HOH 259 859  256 HOH HOH B . 
OA 7 HOH 260 860  291 HOH HOH B . 
OA 7 HOH 261 861  403 HOH HOH B . 
OA 7 HOH 262 862  468 HOH HOH B . 
OA 7 HOH 263 863  20  HOH HOH B . 
OA 7 HOH 264 864  165 HOH HOH B . 
OA 7 HOH 265 865  338 HOH HOH B . 
OA 7 HOH 266 866  43  HOH HOH B . 
OA 7 HOH 267 867  297 HOH HOH B . 
OA 7 HOH 268 868  460 HOH HOH B . 
OA 7 HOH 269 869  733 HOH HOH B . 
OA 7 HOH 270 870  565 HOH HOH B . 
OA 7 HOH 271 871  41  HOH HOH B . 
OA 7 HOH 272 872  21  HOH HOH B . 
OA 7 HOH 273 873  590 HOH HOH B . 
OA 7 HOH 274 874  628 HOH HOH B . 
OA 7 HOH 275 875  1   HOH HOH B . 
OA 7 HOH 276 876  184 HOH HOH B . 
OA 7 HOH 277 877  753 HOH HOH B . 
OA 7 HOH 278 878  152 HOH HOH B . 
OA 7 HOH 279 879  647 HOH HOH B . 
OA 7 HOH 280 880  582 HOH HOH B . 
OA 7 HOH 281 881  577 HOH HOH B . 
OA 7 HOH 282 882  508 HOH HOH B . 
OA 7 HOH 283 883  285 HOH HOH B . 
OA 7 HOH 284 884  150 HOH HOH B . 
OA 7 HOH 285 885  586 HOH HOH B . 
OA 7 HOH 286 886  526 HOH HOH B . 
OA 7 HOH 287 887  50  HOH HOH B . 
OA 7 HOH 288 888  94  HOH HOH B . 
OA 7 HOH 289 889  849 HOH HOH B . 
OA 7 HOH 290 890  585 HOH HOH B . 
OA 7 HOH 291 891  175 HOH HOH B . 
OA 7 HOH 292 892  850 HOH HOH B . 
OA 7 HOH 293 893  431 HOH HOH B . 
OA 7 HOH 294 894  841 HOH HOH B . 
OA 7 HOH 295 895  243 HOH HOH B . 
OA 7 HOH 296 896  832 HOH HOH B . 
OA 7 HOH 297 897  700 HOH HOH B . 
OA 7 HOH 298 898  52  HOH HOH B . 
OA 7 HOH 299 899  31  HOH HOH B . 
OA 7 HOH 300 900  825 HOH HOH B . 
OA 7 HOH 301 901  195 HOH HOH B . 
OA 7 HOH 302 902  864 HOH HOH B . 
OA 7 HOH 303 903  198 HOH HOH B . 
OA 7 HOH 304 904  540 HOH HOH B . 
OA 7 HOH 305 905  662 HOH HOH B . 
OA 7 HOH 306 906  82  HOH HOH B . 
OA 7 HOH 307 907  127 HOH HOH B . 
OA 7 HOH 308 908  489 HOH HOH B . 
OA 7 HOH 309 909  524 HOH HOH B . 
OA 7 HOH 310 910  311 HOH HOH B . 
OA 7 HOH 311 911  654 HOH HOH B . 
OA 7 HOH 312 912  722 HOH HOH B . 
OA 7 HOH 313 913  339 HOH HOH B . 
OA 7 HOH 314 914  692 HOH HOH B . 
OA 7 HOH 315 915  473 HOH HOH B . 
OA 7 HOH 316 916  17  HOH HOH B . 
OA 7 HOH 317 917  416 HOH HOH B . 
OA 7 HOH 318 918  133 HOH HOH B . 
OA 7 HOH 319 919  141 HOH HOH B . 
OA 7 HOH 320 920  703 HOH HOH B . 
OA 7 HOH 321 921  287 HOH HOH B . 
OA 7 HOH 322 922  10  HOH HOH B . 
OA 7 HOH 323 923  46  HOH HOH B . 
OA 7 HOH 324 924  380 HOH HOH B . 
OA 7 HOH 325 925  681 HOH HOH B . 
OA 7 HOH 326 926  843 HOH HOH B . 
OA 7 HOH 327 927  860 HOH HOH B . 
OA 7 HOH 328 928  618 HOH HOH B . 
OA 7 HOH 329 929  115 HOH HOH B . 
OA 7 HOH 330 930  834 HOH HOH B . 
OA 7 HOH 331 931  840 HOH HOH B . 
OA 7 HOH 332 932  772 HOH HOH B . 
OA 7 HOH 333 933  791 HOH HOH B . 
OA 7 HOH 334 934  656 HOH HOH B . 
OA 7 HOH 335 935  362 HOH HOH B . 
OA 7 HOH 336 936  676 HOH HOH B . 
OA 7 HOH 337 937  200 HOH HOH B . 
OA 7 HOH 338 938  33  HOH HOH B . 
OA 7 HOH 339 939  69  HOH HOH B . 
OA 7 HOH 340 940  481 HOH HOH B . 
OA 7 HOH 341 941  101 HOH HOH B . 
OA 7 HOH 342 942  784 HOH HOH B . 
OA 7 HOH 343 943  789 HOH HOH B . 
OA 7 HOH 344 944  160 HOH HOH B . 
OA 7 HOH 345 945  839 HOH HOH B . 
OA 7 HOH 346 946  576 HOH HOH B . 
OA 7 HOH 347 947  61  HOH HOH B . 
OA 7 HOH 348 948  651 HOH HOH B . 
OA 7 HOH 349 949  47  HOH HOH B . 
OA 7 HOH 350 950  114 HOH HOH B . 
OA 7 HOH 351 951  15  HOH HOH B . 
OA 7 HOH 352 952  337 HOH HOH B . 
OA 7 HOH 353 953  60  HOH HOH B . 
OA 7 HOH 354 954  729 HOH HOH B . 
OA 7 HOH 355 955  360 HOH HOH B . 
OA 7 HOH 356 956  620 HOH HOH B . 
OA 7 HOH 357 957  315 HOH HOH B . 
OA 7 HOH 358 958  851 HOH HOH B . 
OA 7 HOH 359 959  631 HOH HOH B . 
OA 7 HOH 360 960  356 HOH HOH B . 
OA 7 HOH 361 961  367 HOH HOH B . 
OA 7 HOH 362 962  506 HOH HOH B . 
OA 7 HOH 363 963  65  HOH HOH B . 
OA 7 HOH 364 964  583 HOH HOH B . 
OA 7 HOH 365 965  680 HOH HOH B . 
OA 7 HOH 366 966  852 HOH HOH B . 
OA 7 HOH 367 967  767 HOH HOH B . 
OA 7 HOH 368 968  373 HOH HOH B . 
OA 7 HOH 369 969  384 HOH HOH B . 
OA 7 HOH 370 970  657 HOH HOH B . 
OA 7 HOH 371 971  74  HOH HOH B . 
OA 7 HOH 372 972  581 HOH HOH B . 
OA 7 HOH 373 973  361 HOH HOH B . 
OA 7 HOH 374 974  99  HOH HOH B . 
OA 7 HOH 375 975  92  HOH HOH B . 
OA 7 HOH 376 976  75  HOH HOH B . 
OA 7 HOH 377 977  324 HOH HOH B . 
OA 7 HOH 378 978  770 HOH HOH B . 
OA 7 HOH 379 979  728 HOH HOH B . 
OA 7 HOH 380 980  182 HOH HOH B . 
OA 7 HOH 381 981  16  HOH HOH B . 
OA 7 HOH 382 982  108 HOH HOH B . 
OA 7 HOH 383 983  829 HOH HOH B . 
OA 7 HOH 384 984  79  HOH HOH B . 
OA 7 HOH 385 985  142 HOH HOH B . 
OA 7 HOH 386 986  782 HOH HOH B . 
OA 7 HOH 387 987  780 HOH HOH B . 
OA 7 HOH 388 988  812 HOH HOH B . 
OA 7 HOH 389 989  646 HOH HOH B . 
OA 7 HOH 390 990  811 HOH HOH B . 
OA 7 HOH 391 991  383 HOH HOH B . 
OA 7 HOH 392 992  652 HOH HOH B . 
OA 7 HOH 393 993  14  HOH HOH B . 
OA 7 HOH 394 994  771 HOH HOH B . 
OA 7 HOH 395 995  712 HOH HOH B . 
OA 7 HOH 396 996  769 HOH HOH B . 
OA 7 HOH 397 997  793 HOH HOH B . 
OA 7 HOH 398 998  610 HOH HOH B . 
OA 7 HOH 399 999  375 HOH HOH B . 
OA 7 HOH 400 1000 552 HOH HOH B . 
OA 7 HOH 401 1001 785 HOH HOH B . 
OA 7 HOH 402 1002 363 HOH HOH B . 
OA 7 HOH 403 1003 818 HOH HOH B . 
OA 7 HOH 404 1004 327 HOH HOH B . 
OA 7 HOH 405 1005 314 HOH HOH B . 
OA 7 HOH 406 1006 166 HOH HOH B . 
OA 7 HOH 407 1007 732 HOH HOH B . 
OA 7 HOH 408 1008 845 HOH HOH B . 
OA 7 HOH 409 1009 695 HOH HOH B . 
OA 7 HOH 410 1010 735 HOH HOH B . 
OA 7 HOH 411 1011 741 HOH HOH B . 
OA 7 HOH 412 1012 817 HOH HOH B . 
OA 7 HOH 413 1013 18  HOH HOH B . 
OA 7 HOH 414 1014 633 HOH HOH B . 
OA 7 HOH 415 1015 653 HOH HOH B . 
OA 7 HOH 416 1016 554 HOH HOH B . 
OA 7 HOH 417 1017 54  HOH HOH B . 
OA 7 HOH 418 1018 718 HOH HOH B . 
OA 7 HOH 419 1019 804 HOH HOH B . 
OA 7 HOH 420 1020 814 HOH HOH B . 
OA 7 HOH 421 1021 376 HOH HOH B . 
OA 7 HOH 422 1022 649 HOH HOH B . 
OA 7 HOH 423 1023 350 HOH HOH B . 
OA 7 HOH 424 1024 372 HOH HOH B . 
OA 7 HOH 425 1025 679 HOH HOH B . 
OA 7 HOH 426 1026 588 HOH HOH B . 
OA 7 HOH 427 1027 763 HOH HOH B . 
OA 7 HOH 428 1028 563 HOH HOH B . 
OA 7 HOH 429 1029 357 HOH HOH B . 
OA 7 HOH 430 1030 379 HOH HOH B . 
OA 7 HOH 431 1031 210 HOH HOH B . 
OA 7 HOH 432 1032 779 HOH HOH B . 
OA 7 HOH 433 1033 378 HOH HOH B . 
OA 7 HOH 434 1034 824 HOH HOH B . 
OA 7 HOH 435 1035 347 HOH HOH B . 
OA 7 HOH 436 1036 731 HOH HOH B . 
OA 7 HOH 437 1037 813 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 B PGE 501 ? O4 ? T PGE 1 O4 
2 1 N 1 B PGE 501 ? C6 ? T PGE 1 C6 
3 1 N 1 B PGE 501 ? C5 ? T PGE 1 C5 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC    ? ? ? 5.8.0238 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8UWT 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     75.407 
_cell.length_a_esd                 ? 
_cell.length_b                     88.245 
_cell.length_b_esd                 ? 
_cell.length_c                     106.593 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8UWT 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8UWT 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.95 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          36.98 
_exptl_crystal.description                  'Thin 2D plates no more than a few microns thick growing as a rosette' 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Hampton Research PEGRx HT: Condition 80 (G8): 0.2 M Sodium Formate, 0.1 M BICINE pH 8.5, 20% PEG5000 MME. This condition was extensively refined and the crystal which generated the data for this deposit consisted of the same, but had pH adjusted to 8.3.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     105 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      'Rhodium coated silicon single crystal' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-03-12 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Numerical link type Si(111) double crystal monochromator' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PHOTON FACTORY BEAMLINE BL-5A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL-5A 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8UWT 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.55 
_reflns.d_resolution_low                               100.00 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     96886 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           94.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.955 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.162 
_reflns.pdbx_Rpim_I_all                                0.047 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1062381 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.155 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.55 1.61   ? ? ? ? ? ? 6167  ? ? ? ? ? ? ? ? ? ? ? 3.8  0.833 ? ? 1.720 0.751 ? 1  1 0.277 0.658 ? 60.6  ? 1.530 ? ? ? ? ? ? ? ? 
? 
1.61 1.67   ? ? ? ? ? ? 8785  ? ? ? ? ? ? ? ? ? ? ? 5.7  1.002 ? ? 1.472 0.551 ? 2  1 0.072 0.368 ? 86.7  ? 1.354 ? ? ? ? ? ? ? ? 
? 
1.67 1.75   ? ? ? ? ? ? 9713  ? ? ? ? ? ? ? ? ? ? ? 8.8  0.905 ? ? 1.303 0.421 ? 3  1 0.511 0.823 ? 95.5  ? 1.228 ? ? ? ? ? ? ? ? 
? 
1.75 1.84   ? ? ? ? ? ? 10164 ? ? ? ? ? ? ? ? ? ? ? 11.4 0.901 ? ? 1.051 0.307 ? 4  1 0.799 0.942 ? 99.6  ? 1.004 ? ? ? ? ? ? ? ? 
? 
1.84 1.95   ? ? ? ? ? ? 10151 ? ? ? ? ? ? ? ? ? ? ? 12.0 0.940 ? ? 0.736 0.211 ? 5  1 0.917 0.978 ? 100.0 ? 0.704 ? ? ? ? ? ? ? ? 
? 
1.95 2.10   ? ? ? ? ? ? 10264 ? ? ? ? ? ? ? ? ? ? ? 12.3 0.985 ? ? 0.446 0.126 ? 6  1 0.961 0.990 ? 100.0 ? 0.427 ? ? ? ? ? ? ? ? 
? 
2.10 2.32   ? ? ? ? ? ? 10246 ? ? ? ? ? ? ? ? ? ? ? 13.3 1.036 ? ? 0.294 0.080 ? 7  1 0.982 0.995 ? 100.0 ? 0.282 ? ? ? ? ? ? ? ? 
? 
2.32 2.65   ? ? ? ? ? ? 10303 ? ? ? ? ? ? ? ? ? ? ? 12.9 1.067 ? ? 0.190 0.053 ? 8  1 0.992 0.998 ? 100.0 ? 0.183 ? ? ? ? ? ? ? ? 
? 
2.65 3.34   ? ? ? ? ? ? 10369 ? ? ? ? ? ? ? ? ? ? ? 12.7 1.015 ? ? 0.109 0.030 ? 9  1 0.997 0.999 ? 100.0 ? 0.105 ? ? ? ? ? ? ? ? 
? 
3.34 100.00 ? ? ? ? ? ? 10724 ? ? ? ? ? ? ? ? ? ? ? 13.0 0.774 ? ? 0.061 0.017 ? 10 1 0.999 1.000 ? 99.8  ? 0.059 ? ? ? ? ? ? ? ? 
? 
# 
_refine.aniso_B[1][1]                            -0.31 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.25 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.56 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               17.324 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.976 
_refine.correlation_coeff_Fo_to_Fc_free          0.960 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8UWT 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.55 
_refine.ls_d_res_low                             35.89 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     78644 
_refine.ls_number_reflns_R_free                  4294 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    80.48 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.14429 
_refine.ls_R_factor_R_free                       0.17987 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.14238 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.095 
_refine.pdbx_overall_ESU_R_Free                  0.094 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.089 
_refine.overall_SU_ML                            0.069 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        35.89 
_refine_hist.number_atoms_solvent             872 
_refine_hist.number_atoms_total               7252 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        6250 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         130 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  0.012  6735  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  5897  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.539  1.641  9137  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.458  1.579  13732 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.997  5.000  849   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 36.596 23.029 350   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.399 15.000 1037  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 19.689 15.000 35    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.080  0.200  861   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  7791  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  1490  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.304  1.617  3312  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.304  1.617  3313  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.919  2.420  4174  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.920  2.421  4175  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.196  1.893  3423  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.058  1.848  3358  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.193  2.705  4959  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.726  20.930 8125  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.576  20.231 7927  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.553 
_refine_ls_shell.d_res_low                        1.594 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             26 
_refine_ls_shell.number_reflns_R_work             562 
_refine_ls_shell.percent_reflns_obs               7.77 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.310 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.394 
# 
_struct.entry_id                     8UWT 
_struct.title                        
;A X-ray Crystallographic Structure Model of a Glycoside Hydrolase (GH) Family 39 (GH39)-like Enzyme Encoded within a Xylan Utilization Locus of the pSOL1 Megaplasmid of Clostridium acetobutylicum
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8UWT 
_struct_keywords.text            'Glycoside Hydrolase Family 39, Clostridium acetobutylicum, pSOL1, Xylan, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 2 ? 
D  N N 3 ? 
E  N N 3 ? 
F  N N 3 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 3 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 3 ? 
S  N N 3 ? 
T  N N 4 ? 
U  N N 2 ? 
V  N N 2 ? 
W  N N 5 ? 
X  N N 3 ? 
Y  N N 3 ? 
Z  N N 3 ? 
AA N N 3 ? 
BA N N 3 ? 
CA N N 3 ? 
DA N N 3 ? 
EA N N 3 ? 
FA N N 3 ? 
GA N N 3 ? 
HA N N 3 ? 
IA N N 3 ? 
JA N N 3 ? 
KA N N 3 ? 
LA N N 3 ? 
MA N N 6 ? 
NA N N 7 ? 
OA N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q97TI4_CLOAB 
_struct_ref.pdbx_db_accession          Q97TI4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATTLTVDCRATLRGVTHCASGSLYGVTESKPFDINQFVAPLKPNVFTNPALAGFNHQQPIGAAIPTAGRLKNTTGKVMIR
LADIFPRWPYGFTNMNDWLGKVTSVINQKKASGYSNFYGYEIWNEPDGTFKNNNVSFNDMWLQTYKLIRRLDPNSQIIGP
SYSYYNHYNMNAFLNFCRANNCLPDVICWHELGGSQNISGNIRDLKTLERSLGIPERKIAINEYSDSNHYAEGQPGASAP
FIAKFERNKVDSACISWWWTNAPGRLGSLMASDTQKGAGWWFYKWYGDMTGNMVNVIPQNDNSNLADGFACVDSNAKYIS
VLLGGVNDGTVNVNIKNIPAFIGSSATVKVEKVDWNGKDTPVNGTNTVFSKRYTVSNGTINVSIPGTNNTSGYRVYVSR
;
_struct_ref.pdbx_align_begin           29 
# 
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 8UWT A 2 ? 400 ? Q97TI4 29 ? 427 ? 2 400 
2 1 8UWT B 2 ? 400 ? Q97TI4 29 ? 427 ? 2 400 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8UWT MET A 1   ? UNP Q97TI4 ? ? 'initiating methionine' 1   1  
1 8UWT LEU A 401 ? UNP Q97TI4 ? ? 'expression tag'        401 2  
1 8UWT GLU A 402 ? UNP Q97TI4 ? ? 'expression tag'        402 3  
1 8UWT HIS A 403 ? UNP Q97TI4 ? ? 'expression tag'        403 4  
1 8UWT HIS A 404 ? UNP Q97TI4 ? ? 'expression tag'        404 5  
1 8UWT HIS A 405 ? UNP Q97TI4 ? ? 'expression tag'        405 6  
1 8UWT HIS A 406 ? UNP Q97TI4 ? ? 'expression tag'        406 7  
1 8UWT HIS A 407 ? UNP Q97TI4 ? ? 'expression tag'        407 8  
1 8UWT HIS A 408 ? UNP Q97TI4 ? ? 'expression tag'        408 9  
2 8UWT MET B 1   ? UNP Q97TI4 ? ? 'initiating methionine' 1   10 
2 8UWT LEU B 401 ? UNP Q97TI4 ? ? 'expression tag'        401 11 
2 8UWT GLU B 402 ? UNP Q97TI4 ? ? 'expression tag'        402 12 
2 8UWT HIS B 403 ? UNP Q97TI4 ? ? 'expression tag'        403 13 
2 8UWT HIS B 404 ? UNP Q97TI4 ? ? 'expression tag'        404 14 
2 8UWT HIS B 405 ? UNP Q97TI4 ? ? 'expression tag'        405 15 
2 8UWT HIS B 406 ? UNP Q97TI4 ? ? 'expression tag'        406 16 
2 8UWT HIS B 407 ? UNP Q97TI4 ? ? 'expression tag'        407 17 
2 8UWT HIS B 408 ? UNP Q97TI4 ? ? 'expression tag'        408 18 
# 
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,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,NA                    
2 1 B,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,OA 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 34  ? VAL A 39  ? ASP A 34  VAL A 39  1 ? 6  
HELX_P HELX_P2  AA2 ALA A 40  ? LYS A 43  ? ALA A 40  LYS A 43  5 ? 4  
HELX_P HELX_P3  AA3 ALA A 63  ? LYS A 72  ? ALA A 63  LYS A 72  1 ? 10 
HELX_P HELX_P4  AA4 ALA A 83  ? PHE A 86  ? ALA A 83  PHE A 86  5 ? 4  
HELX_P HELX_P5  AA5 ASN A 95  ? SER A 113 ? ASN A 95  SER A 113 1 ? 19 
HELX_P HELX_P6  AA6 GLU A 126 ? PHE A 131 ? GLU A 126 PHE A 131 1 ? 6  
HELX_P HELX_P7  AA7 SER A 137 ? ASP A 153 ? SER A 137 ASP A 153 1 ? 17 
HELX_P HELX_P8  AA8 ASN A 167 ? ASN A 181 ? ASN A 167 ASN A 181 1 ? 15 
HELX_P HELX_P9  AA9 ASN A 198 ? GLY A 214 ? ASN A 198 GLY A 214 1 ? 17 
HELX_P HELX_P10 AB1 ASN A 229 ? GLU A 233 ? ASN A 229 GLU A 233 5 ? 5  
HELX_P HELX_P11 AB2 GLN A 235 ? ASN A 249 ? GLN A 235 ASN A 249 1 ? 15 
HELX_P HELX_P12 AB3 GLY A 278 ? MET A 290 ? GLY A 278 MET A 290 1 ? 13 
HELX_P HELX_P13 AB4 PRO A 340 ? GLY A 344 ? PRO A 340 GLY A 344 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 34  ? VAL B 39  ? ASP B 34  VAL B 39  1 ? 6  
HELX_P HELX_P15 AB6 ALA B 40  ? LYS B 43  ? ALA B 40  LYS B 43  5 ? 4  
HELX_P HELX_P16 AB7 ALA B 63  ? LYS B 72  ? ALA B 63  LYS B 72  1 ? 10 
HELX_P HELX_P17 AB8 ALA B 83  ? PHE B 86  ? ALA B 83  PHE B 86  5 ? 4  
HELX_P HELX_P18 AB9 ASN B 95  ? GLY B 114 ? ASN B 95  GLY B 114 1 ? 20 
HELX_P HELX_P19 AC1 GLU B 126 ? PHE B 131 ? GLU B 126 PHE B 131 1 ? 6  
HELX_P HELX_P20 AC2 SER B 137 ? ASP B 153 ? SER B 137 ASP B 153 1 ? 17 
HELX_P HELX_P21 AC3 ASN B 167 ? ASN B 182 ? ASN B 167 ASN B 182 1 ? 16 
HELX_P HELX_P22 AC4 ASN B 198 ? GLY B 214 ? ASN B 198 GLY B 214 1 ? 17 
HELX_P HELX_P23 AC5 ASN B 229 ? GLU B 233 ? ASN B 229 GLU B 233 5 ? 5  
HELX_P HELX_P24 AC6 GLN B 235 ? ASN B 249 ? GLN B 235 ASN B 249 1 ? 15 
HELX_P HELX_P25 AC7 GLY B 278 ? MET B 290 ? GLY B 278 MET B 290 1 ? 13 
HELX_P HELX_P26 AC8 PRO B 340 ? GLY B 344 ? PRO B 340 GLY B 344 5 ? 5  
# 
_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 
_struct_conn.pdbx_role 
metalc1 metalc ? ? NA HOH .   O   ? ? ? 1_555 MA NA  . NA ? ? A HOH 984 B NA  520 1_555 ? ? ? ? ? ? ? 2.378 ? ? 
metalc2 metalc ? ? B  GLN 235 OE1 ? ? ? 1_555 MA NA  . NA ? ? B GLN 235 B NA  520 1_555 ? ? ? ? ? ? ? 3.186 ? ? 
metalc3 metalc ? ? MA NA  .   NA  ? ? ? 1_555 OA HOH . O  ? ? B NA  520 B HOH 704 1_555 ? ? ? ? ? ? ? 3.047 ? ? 
metalc4 metalc ? ? MA NA  .   NA  ? ? ? 1_555 OA HOH . O  ? ? B NA  520 B HOH 796 1_555 ? ? ? ? ? ? ? 2.895 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 O   ? NA HOH .   ? A HOH 984 ? 1_555 NA ? MA NA . ? B NA 520 ? 1_555 OE1 ? B  GLN 235 ? B GLN 235 ? 1_555 96.1  ? 
2 O   ? NA HOH .   ? A HOH 984 ? 1_555 NA ? MA NA . ? B NA 520 ? 1_555 O   ? OA HOH .   ? B HOH 704 ? 1_555 110.9 ? 
3 OE1 ? B  GLN 235 ? B GLN 235 ? 1_555 NA ? MA NA . ? B NA 520 ? 1_555 O   ? OA HOH .   ? B HOH 704 ? 1_555 132.6 ? 
4 O   ? NA HOH .   ? A HOH 984 ? 1_555 NA ? MA NA . ? B NA 520 ? 1_555 O   ? OA HOH .   ? B HOH 796 ? 1_555 142.2 ? 
5 OE1 ? B  GLN 235 ? B GLN 235 ? 1_555 NA ? MA NA . ? B NA 520 ? 1_555 O   ? OA HOH .   ? B HOH 796 ? 1_555 76.6  ? 
6 O   ? OA HOH .   ? B HOH 704 ? 1_555 NA ? MA NA . ? B NA 520 ? 1_555 O   ? OA HOH .   ? B HOH 796 ? 1_555 100.4 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LYS 31  A . ? LYS 31  A PRO 32  A ? PRO 32  A 1 -13.29 
2 TRP 89  A . ? TRP 89  A PRO 90  A ? PRO 90  A 1 -7.38  
3 GLY 160 A . ? GLY 160 A PRO 161 A ? PRO 161 A 1 6.23   
4 LYS 31  B . ? LYS 31  B PRO 32  B ? PRO 32  B 1 -13.41 
5 TRP 89  B . ? TRP 89  B PRO 90  B ? PRO 90  B 1 1.62   
6 GLY 160 B . ? GLY 160 B PRO 161 B ? PRO 161 B 1 5.53   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 7 ? 
AA3 ? 9 ? 
AA4 ? 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 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
AA1 8 9 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? parallel      
AA3 8 9 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA4 6 7 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASN A 367 ? THR A 375 ? ASN A 367 THR A 375 
AA1 2 SER A 346 ? VAL A 354 ? SER A 346 VAL A 354 
AA1 3 GLY A 393 ? ARG A 400 ? GLY A 393 ARG A 400 
AA1 4 TYR A 319 ? GLY A 325 ? TYR A 319 GLY A 325 
AA1 5 ASP A 308 ? ASP A 314 ? ASP A 308 ASP A 314 
AA1 6 ASN A 293 ? ILE A 298 ? ASN A 293 ILE A 298 
AA1 7 THR A 3   ? GLY A 15  ? THR A 3   GLY A 15  
AA1 8 VAL A 332 ? LYS A 337 ? VAL A 332 LYS A 337 
AA1 9 ILE A 381 ? ILE A 385 ? ILE A 381 ILE A 385 
AA2 1 VAL A 46  ? PRO A 50  ? VAL A 46  PRO A 50  
AA2 2 LYS A 77  ? ARG A 81  ? LYS A 77  ARG A 81  
AA2 3 PHE A 118 ? GLU A 122 ? PHE A 118 GLU A 122 
AA2 4 ILE A 158 ? TYR A 163 ? ILE A 158 TYR A 163 
AA2 5 VAL A 187 ? TRP A 190 ? VAL A 187 TRP A 190 
AA2 6 LYS A 219 ? TYR A 225 ? LYS A 219 TYR A 225 
AA2 7 SER A 253 ? ILE A 256 ? SER A 253 ILE A 256 
AA3 1 ASN B 367 ? THR B 375 ? ASN B 367 THR B 375 
AA3 2 SER B 346 ? VAL B 354 ? SER B 346 VAL B 354 
AA3 3 GLY B 393 ? ARG B 400 ? GLY B 393 ARG B 400 
AA3 4 TYR B 319 ? GLY B 325 ? TYR B 319 GLY B 325 
AA3 5 ASP B 308 ? ASP B 314 ? ASP B 308 ASP B 314 
AA3 6 ASN B 293 ? ILE B 298 ? ASN B 293 ILE B 298 
AA3 7 THR B 3   ? GLY B 15  ? THR B 3   GLY B 15  
AA3 8 THR B 331 ? LYS B 337 ? THR B 331 LYS B 337 
AA3 9 ILE B 381 ? PRO B 386 ? ILE B 381 PRO B 386 
AA4 1 VAL B 46  ? PRO B 50  ? VAL B 46  PRO B 50  
AA4 2 LYS B 77  ? ARG B 81  ? LYS B 77  ARG B 81  
AA4 3 PHE B 118 ? GLU B 122 ? PHE B 118 GLU B 122 
AA4 4 ILE B 158 ? TYR B 163 ? ILE B 158 TYR B 163 
AA4 5 VAL B 187 ? TRP B 190 ? VAL B 187 TRP B 190 
AA4 6 LYS B 219 ? TYR B 225 ? LYS B 219 TYR B 225 
AA4 7 SER B 253 ? ILE B 256 ? SER B 253 ILE B 256 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O PHE A 370 ? O PHE A 370 N VAL A 351 ? N VAL A 351 
AA1 2 3 N LYS A 350 ? N LYS A 350 O TYR A 397 ? O TYR A 397 
AA1 3 4 O VAL A 398 ? O VAL A 398 N ILE A 320 ? N ILE A 320 
AA1 4 5 O LEU A 323 ? O LEU A 323 N PHE A 310 ? N PHE A 310 
AA1 5 6 O ALA A 311 ? O ALA A 311 N VAL A 295 ? N VAL A 295 
AA1 6 7 O ILE A 298 ? O ILE A 298 N THR A 6   ? N THR A 6   
AA1 7 8 N VAL A 7   ? N VAL A 7   O ASN A 335 ? O ASN A 335 
AA1 8 9 N VAL A 334 ? N VAL A 334 O VAL A 383 ? O VAL A 383 
AA2 1 2 N PHE A 47  ? N PHE A 47  O MET A 79  ? O MET A 79  
AA2 2 3 N ILE A 80  ? N ILE A 80  O GLU A 122 ? O GLU A 122 
AA2 3 4 N TYR A 121 ? N TYR A 121 O ILE A 159 ? O ILE A 159 
AA2 4 5 N GLY A 160 ? N GLY A 160 O VAL A 187 ? O VAL A 187 
AA2 5 6 N ILE A 188 ? N ILE A 188 O LYS A 219 ? O LYS A 219 
AA2 6 7 N ILE A 222 ? N ILE A 222 O SER A 253 ? O SER A 253 
AA3 1 2 O PHE B 370 ? O PHE B 370 N VAL B 351 ? N VAL B 351 
AA3 2 3 N LYS B 350 ? N LYS B 350 O TYR B 397 ? O TYR B 397 
AA3 3 4 O VAL B 398 ? O VAL B 398 N ILE B 320 ? N ILE B 320 
AA3 4 5 O LEU B 323 ? O LEU B 323 N PHE B 310 ? N PHE B 310 
AA3 5 6 O VAL B 313 ? O VAL B 313 N ASN B 293 ? N ASN B 293 
AA3 6 7 O MET B 294 ? O MET B 294 N LEU B 13  ? N LEU B 13  
AA3 7 8 N VAL B 7   ? N VAL B 7   O LYS B 337 ? O LYS B 337 
AA3 8 9 N VAL B 332 ? N VAL B 332 O ILE B 385 ? O ILE B 385 
AA4 1 2 N PHE B 47  ? N PHE B 47  O MET B 79  ? O MET B 79  
AA4 2 3 N ILE B 80  ? N ILE B 80  O GLU B 122 ? O GLU B 122 
AA4 3 4 N TYR B 121 ? N TYR B 121 O ILE B 159 ? O ILE B 159 
AA4 4 5 N GLY B 160 ? N GLY B 160 O VAL B 187 ? O VAL B 187 
AA4 5 6 N ILE B 188 ? N ILE B 188 O LYS B 219 ? O LYS B 219 
AA4 6 7 N ILE B 222 ? N ILE B 222 O SER B 253 ? O SER B 253 
# 
_pdbx_entry_details.entry_id                   8UWT 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 OH  B TYR 163  ? ? O B HOH 601  ? ? 1.98 
2 1 NE2 B GLN 109  ? ? O B HOH 602  ? ? 2.15 
3 1 O   B HOH 1020 ? ? O B HOH 1037 ? ? 2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              248 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              248 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              248 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                116.70 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.60 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_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 ARG A 14  ? ? 179.83  173.09 
2  1 ASN A 45  ? ? -98.50  -85.84 
3  1 ARG A 88  ? ? 80.58   162.42 
4  1 THR A 94  ? ? -93.06  -85.59 
5  1 SER A 257 ? ? -55.14  170.38 
6  1 ASN A 303 ? ? -90.56  51.54  
7  1 LYS A 318 ? ? 61.15   64.01  
8  1 ARG B 14  ? ? 177.82  174.24 
9  1 ASN B 45  ? ? -97.45  -88.12 
10 1 ARG B 88  ? A 84.71   163.45 
11 1 ARG B 88  ? B 83.17   155.61 
12 1 THR B 94  ? ? -97.61  -85.18 
13 1 GLU B 192 ? ? -119.80 79.42  
14 1 ASN B 303 ? ? -97.19  49.30  
15 1 LYS B 318 ? ? 73.88   55.41  
16 1 ASN B 357 ? B -140.14 39.07  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A GLU 402 ? A GLU 402 
3  1 Y 1 A HIS 403 ? A HIS 403 
4  1 Y 1 A HIS 404 ? A HIS 404 
5  1 Y 1 A HIS 405 ? A HIS 405 
6  1 Y 1 A HIS 406 ? A HIS 406 
7  1 Y 1 A HIS 407 ? A HIS 407 
8  1 Y 1 A HIS 408 ? A HIS 408 
9  1 Y 1 B MET 1   ? B MET 1   
10 1 Y 1 B GLU 402 ? B GLU 402 
11 1 Y 1 B HIS 403 ? B HIS 403 
12 1 Y 1 B HIS 404 ? B HIS 404 
13 1 Y 1 B HIS 405 ? B HIS 405 
14 1 Y 1 B HIS 406 ? B HIS 406 
15 1 Y 1 B HIS 407 ? B HIS 407 
16 1 Y 1 B HIS 408 ? B HIS 408 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
FMT C    C  N N 112 
FMT O1   O  N N 113 
FMT O2   O  N N 114 
FMT H    H  N N 115 
FMT HO2  H  N N 116 
GLN N    N  N N 117 
GLN CA   C  N S 118 
GLN C    C  N N 119 
GLN O    O  N N 120 
GLN CB   C  N N 121 
GLN CG   C  N N 122 
GLN CD   C  N N 123 
GLN OE1  O  N N 124 
GLN NE2  N  N N 125 
GLN OXT  O  N N 126 
GLN H    H  N N 127 
GLN H2   H  N N 128 
GLN HA   H  N N 129 
GLN HB2  H  N N 130 
GLN HB3  H  N N 131 
GLN HG2  H  N N 132 
GLN HG3  H  N N 133 
GLN HE21 H  N N 134 
GLN HE22 H  N N 135 
GLN HXT  H  N N 136 
GLU N    N  N N 137 
GLU CA   C  N S 138 
GLU C    C  N N 139 
GLU O    O  N N 140 
GLU CB   C  N N 141 
GLU CG   C  N N 142 
GLU CD   C  N N 143 
GLU OE1  O  N N 144 
GLU OE2  O  N N 145 
GLU OXT  O  N N 146 
GLU H    H  N N 147 
GLU H2   H  N N 148 
GLU HA   H  N N 149 
GLU HB2  H  N N 150 
GLU HB3  H  N N 151 
GLU HG2  H  N N 152 
GLU HG3  H  N N 153 
GLU HE2  H  N N 154 
GLU HXT  H  N N 155 
GLY N    N  N N 156 
GLY CA   C  N N 157 
GLY C    C  N N 158 
GLY O    O  N N 159 
GLY OXT  O  N N 160 
GLY H    H  N N 161 
GLY H2   H  N N 162 
GLY HA2  H  N N 163 
GLY HA3  H  N N 164 
GLY HXT  H  N N 165 
GOL C1   C  N N 166 
GOL O1   O  N N 167 
GOL C2   C  N N 168 
GOL O2   O  N N 169 
GOL C3   C  N N 170 
GOL O3   O  N N 171 
GOL H11  H  N N 172 
GOL H12  H  N N 173 
GOL HO1  H  N N 174 
GOL H2   H  N N 175 
GOL HO2  H  N N 176 
GOL H31  H  N N 177 
GOL H32  H  N N 178 
GOL HO3  H  N N 179 
HIS N    N  N N 180 
HIS CA   C  N S 181 
HIS C    C  N N 182 
HIS O    O  N N 183 
HIS CB   C  N N 184 
HIS CG   C  Y N 185 
HIS ND1  N  Y N 186 
HIS CD2  C  Y N 187 
HIS CE1  C  Y N 188 
HIS NE2  N  Y N 189 
HIS OXT  O  N N 190 
HIS H    H  N N 191 
HIS H2   H  N N 192 
HIS HA   H  N N 193 
HIS HB2  H  N N 194 
HIS HB3  H  N N 195 
HIS HD1  H  N N 196 
HIS HD2  H  N N 197 
HIS HE1  H  N N 198 
HIS HE2  H  N N 199 
HIS HXT  H  N N 200 
HOH O    O  N N 201 
HOH H1   H  N N 202 
HOH H2   H  N N 203 
ILE N    N  N N 204 
ILE CA   C  N S 205 
ILE C    C  N N 206 
ILE O    O  N N 207 
ILE CB   C  N S 208 
ILE CG1  C  N N 209 
ILE CG2  C  N N 210 
ILE CD1  C  N N 211 
ILE OXT  O  N N 212 
ILE H    H  N N 213 
ILE H2   H  N N 214 
ILE HA   H  N N 215 
ILE HB   H  N N 216 
ILE HG12 H  N N 217 
ILE HG13 H  N N 218 
ILE HG21 H  N N 219 
ILE HG22 H  N N 220 
ILE HG23 H  N N 221 
ILE HD11 H  N N 222 
ILE HD12 H  N N 223 
ILE HD13 H  N N 224 
ILE HXT  H  N N 225 
LEU N    N  N N 226 
LEU CA   C  N S 227 
LEU C    C  N N 228 
LEU O    O  N N 229 
LEU CB   C  N N 230 
LEU CG   C  N N 231 
LEU CD1  C  N N 232 
LEU CD2  C  N N 233 
LEU OXT  O  N N 234 
LEU H    H  N N 235 
LEU H2   H  N N 236 
LEU HA   H  N N 237 
LEU HB2  H  N N 238 
LEU HB3  H  N N 239 
LEU HG   H  N N 240 
LEU HD11 H  N N 241 
LEU HD12 H  N N 242 
LEU HD13 H  N N 243 
LEU HD21 H  N N 244 
LEU HD22 H  N N 245 
LEU HD23 H  N N 246 
LEU HXT  H  N N 247 
LYS N    N  N N 248 
LYS CA   C  N S 249 
LYS C    C  N N 250 
LYS O    O  N N 251 
LYS CB   C  N N 252 
LYS CG   C  N N 253 
LYS CD   C  N N 254 
LYS CE   C  N N 255 
LYS NZ   N  N N 256 
LYS OXT  O  N N 257 
LYS H    H  N N 258 
LYS H2   H  N N 259 
LYS HA   H  N N 260 
LYS HB2  H  N N 261 
LYS HB3  H  N N 262 
LYS HG2  H  N N 263 
LYS HG3  H  N N 264 
LYS HD2  H  N N 265 
LYS HD3  H  N N 266 
LYS HE2  H  N N 267 
LYS HE3  H  N N 268 
LYS HZ1  H  N N 269 
LYS HZ2  H  N N 270 
LYS HZ3  H  N N 271 
LYS HXT  H  N N 272 
MET N    N  N N 273 
MET CA   C  N S 274 
MET C    C  N N 275 
MET O    O  N N 276 
MET CB   C  N N 277 
MET CG   C  N N 278 
MET SD   S  N N 279 
MET CE   C  N N 280 
MET OXT  O  N N 281 
MET H    H  N N 282 
MET H2   H  N N 283 
MET HA   H  N N 284 
MET HB2  H  N N 285 
MET HB3  H  N N 286 
MET HG2  H  N N 287 
MET HG3  H  N N 288 
MET HE1  H  N N 289 
MET HE2  H  N N 290 
MET HE3  H  N N 291 
MET HXT  H  N N 292 
NA  NA   NA N N 293 
PGE C1   C  N N 294 
PGE O1   O  N N 295 
PGE C2   C  N N 296 
PGE O2   O  N N 297 
PGE C3   C  N N 298 
PGE C4   C  N N 299 
PGE O4   O  N N 300 
PGE C6   C  N N 301 
PGE C5   C  N N 302 
PGE O3   O  N N 303 
PGE H1   H  N N 304 
PGE H12  H  N N 305 
PGE HO1  H  N N 306 
PGE H2   H  N N 307 
PGE H22  H  N N 308 
PGE H3   H  N N 309 
PGE H32  H  N N 310 
PGE H4   H  N N 311 
PGE H42  H  N N 312 
PGE HO4  H  N N 313 
PGE H6   H  N N 314 
PGE H62  H  N N 315 
PGE H5   H  N N 316 
PGE H52  H  N N 317 
PHE N    N  N N 318 
PHE CA   C  N S 319 
PHE C    C  N N 320 
PHE O    O  N N 321 
PHE CB   C  N N 322 
PHE CG   C  Y N 323 
PHE CD1  C  Y N 324 
PHE CD2  C  Y N 325 
PHE CE1  C  Y N 326 
PHE CE2  C  Y N 327 
PHE CZ   C  Y N 328 
PHE OXT  O  N N 329 
PHE H    H  N N 330 
PHE H2   H  N N 331 
PHE HA   H  N N 332 
PHE HB2  H  N N 333 
PHE HB3  H  N N 334 
PHE HD1  H  N N 335 
PHE HD2  H  N N 336 
PHE HE1  H  N N 337 
PHE HE2  H  N N 338 
PHE HZ   H  N N 339 
PHE HXT  H  N N 340 
PRO N    N  N N 341 
PRO CA   C  N S 342 
PRO C    C  N N 343 
PRO O    O  N N 344 
PRO CB   C  N N 345 
PRO CG   C  N N 346 
PRO CD   C  N N 347 
PRO OXT  O  N N 348 
PRO H    H  N N 349 
PRO HA   H  N N 350 
PRO HB2  H  N N 351 
PRO HB3  H  N N 352 
PRO HG2  H  N N 353 
PRO HG3  H  N N 354 
PRO HD2  H  N N 355 
PRO HD3  H  N N 356 
PRO HXT  H  N N 357 
SER N    N  N N 358 
SER CA   C  N S 359 
SER C    C  N N 360 
SER O    O  N N 361 
SER CB   C  N N 362 
SER OG   O  N N 363 
SER OXT  O  N N 364 
SER H    H  N N 365 
SER H2   H  N N 366 
SER HA   H  N N 367 
SER HB2  H  N N 368 
SER HB3  H  N N 369 
SER HG   H  N N 370 
SER HXT  H  N N 371 
THR N    N  N N 372 
THR CA   C  N S 373 
THR C    C  N N 374 
THR O    O  N N 375 
THR CB   C  N R 376 
THR OG1  O  N N 377 
THR CG2  C  N N 378 
THR OXT  O  N N 379 
THR H    H  N N 380 
THR H2   H  N N 381 
THR HA   H  N N 382 
THR HB   H  N N 383 
THR HG1  H  N N 384 
THR HG21 H  N N 385 
THR HG22 H  N N 386 
THR HG23 H  N N 387 
THR HXT  H  N N 388 
TRP N    N  N N 389 
TRP CA   C  N S 390 
TRP C    C  N N 391 
TRP O    O  N N 392 
TRP CB   C  N N 393 
TRP CG   C  Y N 394 
TRP CD1  C  Y N 395 
TRP CD2  C  Y N 396 
TRP NE1  N  Y N 397 
TRP CE2  C  Y N 398 
TRP CE3  C  Y N 399 
TRP CZ2  C  Y N 400 
TRP CZ3  C  Y N 401 
TRP CH2  C  Y N 402 
TRP OXT  O  N N 403 
TRP H    H  N N 404 
TRP H2   H  N N 405 
TRP HA   H  N N 406 
TRP HB2  H  N N 407 
TRP HB3  H  N N 408 
TRP HD1  H  N N 409 
TRP HE1  H  N N 410 
TRP HE3  H  N N 411 
TRP HZ2  H  N N 412 
TRP HZ3  H  N N 413 
TRP HH2  H  N N 414 
TRP HXT  H  N N 415 
TYR N    N  N N 416 
TYR CA   C  N S 417 
TYR C    C  N N 418 
TYR O    O  N N 419 
TYR CB   C  N N 420 
TYR CG   C  Y N 421 
TYR CD1  C  Y N 422 
TYR CD2  C  Y N 423 
TYR CE1  C  Y N 424 
TYR CE2  C  Y N 425 
TYR CZ   C  Y N 426 
TYR OH   O  N N 427 
TYR OXT  O  N N 428 
TYR H    H  N N 429 
TYR H2   H  N N 430 
TYR HA   H  N N 431 
TYR HB2  H  N N 432 
TYR HB3  H  N N 433 
TYR HD1  H  N N 434 
TYR HD2  H  N N 435 
TYR HE1  H  N N 436 
TYR HE2  H  N N 437 
TYR HH   H  N N 438 
TYR HXT  H  N N 439 
VAL N    N  N N 440 
VAL CA   C  N S 441 
VAL C    C  N N 442 
VAL O    O  N N 443 
VAL CB   C  N N 444 
VAL CG1  C  N N 445 
VAL CG2  C  N N 446 
VAL OXT  O  N N 447 
VAL H    H  N N 448 
VAL H2   H  N N 449 
VAL HA   H  N N 450 
VAL HB   H  N N 451 
VAL HG11 H  N N 452 
VAL HG12 H  N N 453 
VAL HG13 H  N N 454 
VAL HG21 H  N N 455 
VAL HG22 H  N N 456 
VAL HG23 H  N N 457 
VAL HXT  H  N N 458 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
FMT C   O1   doub N N 106 
FMT C   O2   sing N N 107 
FMT C   H    sing N N 108 
FMT O2  HO2  sing N N 109 
GLN N   CA   sing N N 110 
GLN N   H    sing N N 111 
GLN N   H2   sing N N 112 
GLN CA  C    sing N N 113 
GLN CA  CB   sing N N 114 
GLN CA  HA   sing N N 115 
GLN C   O    doub N N 116 
GLN C   OXT  sing N N 117 
GLN CB  CG   sing N N 118 
GLN CB  HB2  sing N N 119 
GLN CB  HB3  sing N N 120 
GLN CG  CD   sing N N 121 
GLN CG  HG2  sing N N 122 
GLN CG  HG3  sing N N 123 
GLN CD  OE1  doub N N 124 
GLN CD  NE2  sing N N 125 
GLN NE2 HE21 sing N N 126 
GLN NE2 HE22 sing N N 127 
GLN OXT HXT  sing N N 128 
GLU N   CA   sing N N 129 
GLU N   H    sing N N 130 
GLU N   H2   sing N N 131 
GLU CA  C    sing N N 132 
GLU CA  CB   sing N N 133 
GLU CA  HA   sing N N 134 
GLU C   O    doub N N 135 
GLU C   OXT  sing N N 136 
GLU CB  CG   sing N N 137 
GLU CB  HB2  sing N N 138 
GLU CB  HB3  sing N N 139 
GLU CG  CD   sing N N 140 
GLU CG  HG2  sing N N 141 
GLU CG  HG3  sing N N 142 
GLU CD  OE1  doub N N 143 
GLU CD  OE2  sing N N 144 
GLU OE2 HE2  sing N N 145 
GLU OXT HXT  sing N N 146 
GLY N   CA   sing N N 147 
GLY N   H    sing N N 148 
GLY N   H2   sing N N 149 
GLY CA  C    sing N N 150 
GLY CA  HA2  sing N N 151 
GLY CA  HA3  sing N N 152 
GLY C   O    doub N N 153 
GLY C   OXT  sing N N 154 
GLY OXT HXT  sing N N 155 
GOL C1  O1   sing N N 156 
GOL C1  C2   sing N N 157 
GOL C1  H11  sing N N 158 
GOL C1  H12  sing N N 159 
GOL O1  HO1  sing N N 160 
GOL C2  O2   sing N N 161 
GOL C2  C3   sing N N 162 
GOL C2  H2   sing N N 163 
GOL O2  HO2  sing N N 164 
GOL C3  O3   sing N N 165 
GOL C3  H31  sing N N 166 
GOL C3  H32  sing N N 167 
GOL O3  HO3  sing N N 168 
HIS N   CA   sing N N 169 
HIS N   H    sing N N 170 
HIS N   H2   sing N N 171 
HIS CA  C    sing N N 172 
HIS CA  CB   sing N N 173 
HIS CA  HA   sing N N 174 
HIS C   O    doub N N 175 
HIS C   OXT  sing N N 176 
HIS CB  CG   sing N N 177 
HIS CB  HB2  sing N N 178 
HIS CB  HB3  sing N N 179 
HIS CG  ND1  sing Y N 180 
HIS CG  CD2  doub Y N 181 
HIS ND1 CE1  doub Y N 182 
HIS ND1 HD1  sing N N 183 
HIS CD2 NE2  sing Y N 184 
HIS CD2 HD2  sing N N 185 
HIS CE1 NE2  sing Y N 186 
HIS CE1 HE1  sing N N 187 
HIS NE2 HE2  sing N N 188 
HIS OXT HXT  sing N N 189 
HOH O   H1   sing N N 190 
HOH O   H2   sing N N 191 
ILE N   CA   sing N N 192 
ILE N   H    sing N N 193 
ILE N   H2   sing N N 194 
ILE CA  C    sing N N 195 
ILE CA  CB   sing N N 196 
ILE CA  HA   sing N N 197 
ILE C   O    doub N N 198 
ILE C   OXT  sing N N 199 
ILE CB  CG1  sing N N 200 
ILE CB  CG2  sing N N 201 
ILE CB  HB   sing N N 202 
ILE CG1 CD1  sing N N 203 
ILE CG1 HG12 sing N N 204 
ILE CG1 HG13 sing N N 205 
ILE CG2 HG21 sing N N 206 
ILE CG2 HG22 sing N N 207 
ILE CG2 HG23 sing N N 208 
ILE CD1 HD11 sing N N 209 
ILE CD1 HD12 sing N N 210 
ILE CD1 HD13 sing N N 211 
ILE OXT HXT  sing N N 212 
LEU N   CA   sing N N 213 
LEU N   H    sing N N 214 
LEU N   H2   sing N N 215 
LEU CA  C    sing N N 216 
LEU CA  CB   sing N N 217 
LEU CA  HA   sing N N 218 
LEU C   O    doub N N 219 
LEU C   OXT  sing N N 220 
LEU CB  CG   sing N N 221 
LEU CB  HB2  sing N N 222 
LEU CB  HB3  sing N N 223 
LEU CG  CD1  sing N N 224 
LEU CG  CD2  sing N N 225 
LEU CG  HG   sing N N 226 
LEU CD1 HD11 sing N N 227 
LEU CD1 HD12 sing N N 228 
LEU CD1 HD13 sing N N 229 
LEU CD2 HD21 sing N N 230 
LEU CD2 HD22 sing N N 231 
LEU CD2 HD23 sing N N 232 
LEU OXT HXT  sing N N 233 
LYS N   CA   sing N N 234 
LYS N   H    sing N N 235 
LYS N   H2   sing N N 236 
LYS CA  C    sing N N 237 
LYS CA  CB   sing N N 238 
LYS CA  HA   sing N N 239 
LYS C   O    doub N N 240 
LYS C   OXT  sing N N 241 
LYS CB  CG   sing N N 242 
LYS CB  HB2  sing N N 243 
LYS CB  HB3  sing N N 244 
LYS CG  CD   sing N N 245 
LYS CG  HG2  sing N N 246 
LYS CG  HG3  sing N N 247 
LYS CD  CE   sing N N 248 
LYS CD  HD2  sing N N 249 
LYS CD  HD3  sing N N 250 
LYS CE  NZ   sing N N 251 
LYS CE  HE2  sing N N 252 
LYS CE  HE3  sing N N 253 
LYS NZ  HZ1  sing N N 254 
LYS NZ  HZ2  sing N N 255 
LYS NZ  HZ3  sing N N 256 
LYS OXT HXT  sing N N 257 
MET N   CA   sing N N 258 
MET N   H    sing N N 259 
MET N   H2   sing N N 260 
MET CA  C    sing N N 261 
MET CA  CB   sing N N 262 
MET CA  HA   sing N N 263 
MET C   O    doub N N 264 
MET C   OXT  sing N N 265 
MET CB  CG   sing N N 266 
MET CB  HB2  sing N N 267 
MET CB  HB3  sing N N 268 
MET CG  SD   sing N N 269 
MET CG  HG2  sing N N 270 
MET CG  HG3  sing N N 271 
MET SD  CE   sing N N 272 
MET CE  HE1  sing N N 273 
MET CE  HE2  sing N N 274 
MET CE  HE3  sing N N 275 
MET OXT HXT  sing N N 276 
PGE C1  O1   sing N N 277 
PGE C1  C2   sing N N 278 
PGE C1  H1   sing N N 279 
PGE C1  H12  sing N N 280 
PGE O1  HO1  sing N N 281 
PGE C2  O2   sing N N 282 
PGE C2  H2   sing N N 283 
PGE C2  H22  sing N N 284 
PGE O2  C3   sing N N 285 
PGE C3  C4   sing N N 286 
PGE C3  H3   sing N N 287 
PGE C3  H32  sing N N 288 
PGE C4  O3   sing N N 289 
PGE C4  H4   sing N N 290 
PGE C4  H42  sing N N 291 
PGE O4  C6   sing N N 292 
PGE O4  HO4  sing N N 293 
PGE C6  C5   sing N N 294 
PGE C6  H6   sing N N 295 
PGE C6  H62  sing N N 296 
PGE C5  O3   sing N N 297 
PGE C5  H5   sing N N 298 
PGE C5  H52  sing N N 299 
PHE N   CA   sing N N 300 
PHE N   H    sing N N 301 
PHE N   H2   sing N N 302 
PHE CA  C    sing N N 303 
PHE CA  CB   sing N N 304 
PHE CA  HA   sing N N 305 
PHE C   O    doub N N 306 
PHE C   OXT  sing N N 307 
PHE CB  CG   sing N N 308 
PHE CB  HB2  sing N N 309 
PHE CB  HB3  sing N N 310 
PHE CG  CD1  doub Y N 311 
PHE CG  CD2  sing Y N 312 
PHE CD1 CE1  sing Y N 313 
PHE CD1 HD1  sing N N 314 
PHE CD2 CE2  doub Y N 315 
PHE CD2 HD2  sing N N 316 
PHE CE1 CZ   doub Y N 317 
PHE CE1 HE1  sing N N 318 
PHE CE2 CZ   sing Y N 319 
PHE CE2 HE2  sing N N 320 
PHE CZ  HZ   sing N N 321 
PHE OXT HXT  sing N N 322 
PRO N   CA   sing N N 323 
PRO N   CD   sing N N 324 
PRO N   H    sing N N 325 
PRO CA  C    sing N N 326 
PRO CA  CB   sing N N 327 
PRO CA  HA   sing N N 328 
PRO C   O    doub N N 329 
PRO C   OXT  sing N N 330 
PRO CB  CG   sing N N 331 
PRO CB  HB2  sing N N 332 
PRO CB  HB3  sing N N 333 
PRO CG  CD   sing N N 334 
PRO CG  HG2  sing N N 335 
PRO CG  HG3  sing N N 336 
PRO CD  HD2  sing N N 337 
PRO CD  HD3  sing N N 338 
PRO OXT HXT  sing N N 339 
SER N   CA   sing N N 340 
SER N   H    sing N N 341 
SER N   H2   sing N N 342 
SER CA  C    sing N N 343 
SER CA  CB   sing N N 344 
SER CA  HA   sing N N 345 
SER C   O    doub N N 346 
SER C   OXT  sing N N 347 
SER CB  OG   sing N N 348 
SER CB  HB2  sing N N 349 
SER CB  HB3  sing N N 350 
SER OG  HG   sing N N 351 
SER OXT HXT  sing N N 352 
THR N   CA   sing N N 353 
THR N   H    sing N N 354 
THR N   H2   sing N N 355 
THR CA  C    sing N N 356 
THR CA  CB   sing N N 357 
THR CA  HA   sing N N 358 
THR C   O    doub N N 359 
THR C   OXT  sing N N 360 
THR CB  OG1  sing N N 361 
THR CB  CG2  sing N N 362 
THR CB  HB   sing N N 363 
THR OG1 HG1  sing N N 364 
THR CG2 HG21 sing N N 365 
THR CG2 HG22 sing N N 366 
THR CG2 HG23 sing N N 367 
THR OXT HXT  sing N N 368 
TRP N   CA   sing N N 369 
TRP N   H    sing N N 370 
TRP N   H2   sing N N 371 
TRP CA  C    sing N N 372 
TRP CA  CB   sing N N 373 
TRP CA  HA   sing N N 374 
TRP C   O    doub N N 375 
TRP C   OXT  sing N N 376 
TRP CB  CG   sing N N 377 
TRP CB  HB2  sing N N 378 
TRP CB  HB3  sing N N 379 
TRP CG  CD1  doub Y N 380 
TRP CG  CD2  sing Y N 381 
TRP CD1 NE1  sing Y N 382 
TRP CD1 HD1  sing N N 383 
TRP CD2 CE2  doub Y N 384 
TRP CD2 CE3  sing Y N 385 
TRP NE1 CE2  sing Y N 386 
TRP NE1 HE1  sing N N 387 
TRP CE2 CZ2  sing Y N 388 
TRP CE3 CZ3  doub Y N 389 
TRP CE3 HE3  sing N N 390 
TRP CZ2 CH2  doub Y N 391 
TRP CZ2 HZ2  sing N N 392 
TRP CZ3 CH2  sing Y N 393 
TRP CZ3 HZ3  sing N N 394 
TRP CH2 HH2  sing N N 395 
TRP OXT HXT  sing N N 396 
TYR N   CA   sing N N 397 
TYR N   H    sing N N 398 
TYR N   H2   sing N N 399 
TYR CA  C    sing N N 400 
TYR CA  CB   sing N N 401 
TYR CA  HA   sing N N 402 
TYR C   O    doub N N 403 
TYR C   OXT  sing N N 404 
TYR CB  CG   sing N N 405 
TYR CB  HB2  sing N N 406 
TYR CB  HB3  sing N N 407 
TYR CG  CD1  doub Y N 408 
TYR CG  CD2  sing Y N 409 
TYR CD1 CE1  sing Y N 410 
TYR CD1 HD1  sing N N 411 
TYR CD2 CE2  doub Y N 412 
TYR CD2 HD2  sing N N 413 
TYR CE1 CZ   doub Y N 414 
TYR CE1 HE1  sing N N 415 
TYR CE2 CZ   sing Y N 416 
TYR CE2 HE2  sing N N 417 
TYR CZ  OH   sing N N 418 
TYR OH  HH   sing N N 419 
TYR OXT HXT  sing N N 420 
VAL N   CA   sing N N 421 
VAL N   H    sing N N 422 
VAL N   H2   sing N N 423 
VAL CA  C    sing N N 424 
VAL CA  CB   sing N N 425 
VAL CA  HA   sing N N 426 
VAL C   O    doub N N 427 
VAL C   OXT  sing N N 428 
VAL CB  CG1  sing N N 429 
VAL CB  CG2  sing N N 430 
VAL CB  HB   sing N N 431 
VAL CG1 HG11 sing N N 432 
VAL CG1 HG12 sing N N 433 
VAL CG1 HG13 sing N N 434 
VAL CG2 HG21 sing N N 435 
VAL CG2 HG22 sing N N 436 
VAL CG2 HG23 sing N N 437 
VAL OXT HXT  sing N N 438 
# 
_pdbx_audit_support.funding_organization   'Japan Society for the Promotion of Science (JSPS)' 
_pdbx_audit_support.country                Japan 
_pdbx_audit_support.grant_number           L17552 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5U22 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8UWT 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.013261 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011332 
_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]   0.009381 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A  1 2   ? -38.761 -13.737 -23.753 1.00 24.08 ? 2    ALA A N   1 
ATOM   2    C  CA  . ALA A  1 2   ? -38.050 -12.837 -22.822 1.00 25.12 ? 2    ALA A CA  1 
ATOM   3    C  C   . ALA A  1 2   ? -38.267 -13.329 -21.393 1.00 22.28 ? 2    ALA A C   1 
ATOM   4    O  O   . ALA A  1 2   ? -39.342 -13.891 -21.084 1.00 26.69 ? 2    ALA A O   1 
ATOM   5    C  CB  . ALA A  1 2   ? -38.545 -11.423 -22.963 1.00 23.84 ? 2    ALA A CB  1 
ATOM   6    N  N   . THR A  1 3   ? -37.266 -13.115 -20.560 1.00 19.76 ? 3    THR A N   1 
ATOM   7    C  CA  . THR A  1 3   ? -37.359 -13.254 -19.092 1.00 18.13 ? 3    THR A CA  1 
ATOM   8    C  C   . THR A  1 3   ? -37.770 -11.872 -18.569 1.00 19.30 ? 3    THR A C   1 
ATOM   9    O  O   . THR A  1 3   ? -37.041 -10.918 -18.895 1.00 20.57 ? 3    THR A O   1 
ATOM   10   C  CB  . THR A  1 3   ? -36.010 -13.752 -18.573 1.00 18.16 ? 3    THR A CB  1 
ATOM   11   O  OG1 . THR A  1 3   ? -35.733 -14.964 -19.270 1.00 17.67 ? 3    THR A OG1 1 
ATOM   12   C  CG2 . THR A  1 3   ? -35.990 -14.036 -17.100 1.00 19.45 ? 3    THR A CG2 1 
ATOM   13   N  N   . THR A  1 4   ? -38.834 -11.793 -17.775 1.00 18.66 ? 4    THR A N   1 
ATOM   14   C  CA  . THR A  1 4   ? -39.466 -10.521 -17.338 1.00 18.64 ? 4    THR A CA  1 
ATOM   15   C  C   . THR A  1 4   ? -39.322 -10.271 -15.829 1.00 17.11 ? 4    THR A C   1 
ATOM   16   O  O   . THR A  1 4   ? -39.582 -11.197 -15.013 1.00 16.92 ? 4    THR A O   1 
ATOM   17   C  CB  . THR A  1 4   ? -40.937 -10.482 -17.763 1.00 20.86 ? 4    THR A CB  1 
ATOM   18   O  OG1 . THR A  1 4   ? -40.877 -10.630 -19.191 1.00 20.93 ? 4    THR A OG1 1 
ATOM   19   C  CG2 . THR A  1 4   ? -41.615 -9.186  -17.366 1.00 22.33 ? 4    THR A CG2 1 
ATOM   20   N  N   . LEU A  1 5   ? -38.951 -9.031  -15.502 1.00 15.53 ? 5    LEU A N   1 
ATOM   21   C  CA  . LEU A  1 5   ? -38.945 -8.460  -14.138 1.00 15.78 ? 5    LEU A CA  1 
ATOM   22   C  C   . LEU A  1 5   ? -39.864 -7.242  -14.128 1.00 14.83 ? 5    LEU A C   1 
ATOM   23   O  O   . LEU A  1 5   ? -39.835 -6.483  -15.119 1.00 15.34 ? 5    LEU A O   1 
ATOM   24   C  CB  . LEU A  1 5   ? -37.542 -7.989  -13.778 1.00 18.48 ? 5    LEU A CB  1 
ATOM   25   C  CG  . LEU A  1 5   ? -36.445 -9.010  -13.967 1.00 22.35 ? 5    LEU A CG  1 
ATOM   26   C  CD1 . LEU A  1 5   ? -35.140 -8.383  -13.541 1.00 23.00 ? 5    LEU A CD1 1 
ATOM   27   C  CD2 . LEU A  1 5   ? -36.757 -10.289 -13.171 1.00 25.77 ? 5    LEU A CD2 1 
ATOM   28   N  N   . THR A  1 6   ? -40.638 -7.063  -13.066 1.00 13.87 ? 6    THR A N   1 
ATOM   29   C  CA  . THR A  1 6   ? -41.490 -5.880  -12.905 1.00 14.13 ? 6    THR A CA  1 
ATOM   30   C  C   . THR A  1 6   ? -41.026 -5.100  -11.687 1.00 14.13 ? 6    THR A C   1 
ATOM   31   O  O   . THR A  1 6   ? -41.008 -5.662  -10.588 1.00 16.16 ? 6    THR A O   1 
ATOM   32   C  CB  . THR A  1 6   ? -42.968 -6.250  -12.819 1.00 16.50 ? 6    THR A CB  1 
ATOM   33   O  OG1 . THR A  1 6   ? -43.295 -6.949  -14.021 1.00 16.83 ? 6    THR A OG1 1 
ATOM   34   C  CG2 . THR A  1 6   ? -43.843 -5.030  -12.640 1.00 17.15 ? 6    THR A CG2 1 
ATOM   35   N  N   . VAL A  1 7   ? -40.675 -3.829  -11.893 1.00 12.81 ? 7    VAL A N   1 
ATOM   36   C  CA  . VAL A  1 7   ? -40.230 -2.951  -10.794 1.00 12.81 ? 7    VAL A CA  1 
ATOM   37   C  C   . VAL A  1 7   ? -41.429 -2.124  -10.342 1.00 13.03 ? 7    VAL A C   1 
ATOM   38   O  O   . VAL A  1 7   ? -41.953 -1.356  -11.147 1.00 12.73 ? 7    VAL A O   1 
ATOM   39   C  CB  . VAL A  1 7   ? -39.065 -2.062  -11.246 1.00 12.67 ? 7    VAL A CB  1 
ATOM   40   C  CG1 . VAL A  1 7   ? -38.658 -1.061  -10.177 1.00 14.37 ? 7    VAL A CG1 1 
ATOM   41   C  CG2 . VAL A  1 7   ? -37.903 -2.945  -11.658 1.00 12.58 ? 7    VAL A CG2 1 
ATOM   42   N  N   . ASP A  1 8   ? -41.790 -2.218  -9.076  1.00 12.26 ? 8    ASP A N   1 
ATOM   43   C  CA  . ASP A  1 8   ? -43.003 -1.528  -8.575  1.00 12.52 ? 8    ASP A CA  1 
ATOM   44   C  C   . ASP A  1 8   ? -42.557 -0.372  -7.695  1.00 11.85 ? 8    ASP A C   1 
ATOM   45   O  O   . ASP A  1 8   ? -42.255 -0.581  -6.477  1.00 11.24 ? 8    ASP A O   1 
ATOM   46   C  CB  . ASP A  1 8   ? -43.913 -2.498  -7.825  1.00 15.03 ? 8    ASP A CB  1 
ATOM   47   C  CG  . ASP A  1 8   ? -45.192 -1.822  -7.372  1.00 16.75 ? 8    ASP A CG  1 
ATOM   48   O  OD1 . ASP A  1 8   ? -45.329 -0.603  -7.619  1.00 15.36 ? 8    ASP A OD1 1 
ATOM   49   O  OD2 . ASP A  1 8   ? -46.039 -2.558  -6.821  1.00 19.38 ? 8    ASP A OD2 1 
ATOM   50   N  N   . CYS A  1 9   ? -42.519 0.825   -8.260  1.00 11.56 ? 9    CYS A N   1 
ATOM   51   C  CA  . CYS A  1 9   ? -42.002 1.996   -7.539  1.00 12.92 ? 9    CYS A CA  1 
ATOM   52   C  C   . CYS A  1 9   ? -42.908 2.351   -6.357  1.00 12.22 ? 9    CYS A C   1 
ATOM   53   O  O   . CYS A  1 9   ? -42.457 3.110   -5.495  1.00 12.29 ? 9    CYS A O   1 
ATOM   54   C  CB  . CYS A  1 9   ? -41.824 3.195   -8.457  1.00 13.85 ? 9    CYS A CB  1 
ATOM   55   S  SG  . CYS A  1 9   ? -40.718 2.885   -9.864  1.00 14.06 ? 9    CYS A SG  1 
ATOM   56   N  N   . ARG A  1 10  ? -44.132 1.831   -6.293  1.00 12.42 ? 10   ARG A N   1 
ATOM   57   C  CA  . ARG A  1 10  ? -45.045 2.105   -5.155  1.00 12.93 ? 10   ARG A CA  1 
ATOM   58   C  C   . ARG A  1 10  ? -44.672 1.253   -3.944  1.00 13.03 ? 10   ARG A C   1 
ATOM   59   O  O   . ARG A  1 10  ? -44.902 1.711   -2.819  1.00 13.15 ? 10   ARG A O   1 
ATOM   60   C  CB  . ARG A  1 10  ? -46.495 1.825   -5.583  1.00 13.20 ? 10   ARG A CB  1 
ATOM   61   C  CG  . ARG A  1 10  ? -47.508 1.916   -4.457  1.00 13.93 ? 10   ARG A CG  1 
ATOM   62   C  CD  . ARG A  1 10  ? -47.833 0.574   -3.831  1.00 14.06 ? 10   ARG A CD  1 
ATOM   63   N  NE  . ARG A  1 10  ? -48.767 0.657   -2.701  1.00 14.21 ? 10   ARG A NE  1 
ATOM   64   C  CZ  . ARG A  1 10  ? -48.430 0.697   -1.417  1.00 14.56 ? 10   ARG A CZ  1 
ATOM   65   N  NH1 . ARG A  1 10  ? -49.384 0.690   -0.502  1.00 15.07 ? 10   ARG A NH1 1 
ATOM   66   N  NH2 . ARG A  1 10  ? -47.149 0.763   -1.052  1.00 15.63 ? 10   ARG A NH2 1 
ATOM   67   N  N   . ALA A  1 11  ? -44.064 0.090   -4.165  1.00 13.96 ? 11   ALA A N   1 
ATOM   68   C  CA  . ALA A  1 11  ? -43.836 -0.941  -3.128  1.00 14.19 ? 11   ALA A CA  1 
ATOM   69   C  C   . ALA A  1 11  ? -42.522 -0.641  -2.390  1.00 14.67 ? 11   ALA A C   1 
ATOM   70   O  O   . ALA A  1 11  ? -41.555 -1.422  -2.560  1.00 14.71 ? 11   ALA A O   1 
ATOM   71   C  CB  . ALA A  1 11  ? -43.842 -2.311  -3.778  1.00 14.84 ? 11   ALA A CB  1 
ATOM   72   N  N   . THR A  1 12  ? -42.454 0.440   -1.606  1.00 14.61 ? 12   THR A N   1 
ATOM   73   C  CA  . THR A  1 12  ? -41.227 0.810   -0.844  1.00 16.94 ? 12   THR A CA  1 
ATOM   74   C  C   . THR A  1 12  ? -40.899 -0.301  0.158   1.00 17.10 ? 12   THR A C   1 
ATOM   75   O  O   . THR A  1 12  ? -41.796 -0.710  0.906   1.00 17.17 ? 12   THR A O   1 
ATOM   76   C  CB  . THR A  1 12  ? -41.393 2.134   -0.096  1.00 19.58 ? 12   THR A CB  1 
ATOM   77   O  OG1 . THR A  1 12  ? -41.833 3.075   -1.069  1.00 25.11 ? 12   THR A OG1 1 
ATOM   78   C  CG2 . THR A  1 12  ? -40.112 2.631   0.536   1.00 20.74 ? 12   THR A CG2 1 
ATOM   79   N  N   . LEU A  1 13  ? -39.673 -0.815  0.141   1.00 14.36 ? 13   LEU A N   1 
ATOM   80   C  CA  . LEU A  1 13  ? -39.228 -1.865  1.086   1.00 15.80 ? 13   LEU A CA  1 
ATOM   81   C  C   . LEU A  1 13  ? -38.666 -1.197  2.333   1.00 14.99 ? 13   LEU A C   1 
ATOM   82   O  O   . LEU A  1 13  ? -39.159 -1.490  3.431   1.00 16.63 ? 13   LEU A O   1 
ATOM   83   C  CB  . LEU A  1 13  ? -38.190 -2.754  0.394   1.00 15.59 ? 13   LEU A CB  1 
ATOM   84   C  CG  . LEU A  1 13  ? -38.772 -3.674  -0.669  1.00 17.22 ? 13   LEU A CG  1 
ATOM   85   C  CD1 . LEU A  1 13  ? -37.656 -4.370  -1.435  1.00 16.10 ? 13   LEU A CD1 1 
ATOM   86   C  CD2 . LEU A  1 13  ? -39.758 -4.665  -0.023  1.00 19.81 ? 13   LEU A CD2 1 
ATOM   87   N  N   . ARG A  1 14  ? -37.670 -0.342  2.158   1.00 15.10 ? 14   ARG A N   1 
ATOM   88   C  CA  . ARG A  1 14  ? -36.908 0.320   3.241   1.00 14.64 ? 14   ARG A CA  1 
ATOM   89   C  C   . ARG A  1 14  ? -35.867 1.205   2.579   1.00 14.76 ? 14   ARG A C   1 
ATOM   90   O  O   . ARG A  1 14  ? -35.744 1.151   1.339   1.00 14.94 ? 14   ARG A O   1 
ATOM   91   C  CB  . ARG A  1 14  ? -36.222 -0.706  4.160   1.00 15.87 ? 14   ARG A CB  1 
ATOM   92   C  CG  . ARG A  1 14  ? -35.409 -1.768  3.429   1.00 15.69 ? 14   ARG A CG  1 
ATOM   93   C  CD  . ARG A  1 14  ? -34.628 -2.665  4.367   1.00 15.85 ? 14   ARG A CD  1 
ATOM   94   N  NE  . ARG A  1 14  ? -33.901 -3.638  3.551   1.00 15.30 ? 14   ARG A NE  1 
ATOM   95   C  CZ  . ARG A  1 14  ? -32.978 -4.452  4.011   1.00 15.98 ? 14   ARG A CZ  1 
ATOM   96   N  NH1 . ARG A  1 14  ? -32.753 -4.518  5.309   1.00 15.59 ? 14   ARG A NH1 1 
ATOM   97   N  NH2 . ARG A  1 14  ? -32.332 -5.236  3.184   1.00 14.32 ? 14   ARG A NH2 1 
ATOM   98   N  N   . GLY A  1 15  ? -35.169 1.997   3.376   1.00 14.47 ? 15   GLY A N   1 
ATOM   99   C  CA  . GLY A  1 15  ? -33.960 2.718   2.963   1.00 14.88 ? 15   GLY A CA  1 
ATOM   100  C  C   . GLY A  1 15  ? -32.914 1.788   2.403   1.00 15.71 ? 15   GLY A C   1 
ATOM   101  O  O   . GLY A  1 15  ? -32.869 0.557   2.753   1.00 18.10 ? 15   GLY A O   1 
ATOM   102  N  N   . VAL A  1 16  ? -32.144 2.299   1.464   1.00 13.84 ? 16   VAL A N   1 
ATOM   103  C  CA  . VAL A  1 16  ? -30.994 1.553   0.888   1.00 12.59 ? 16   VAL A CA  1 
ATOM   104  C  C   . VAL A  1 16  ? -30.052 1.177   2.020   1.00 13.44 ? 16   VAL A C   1 
ATOM   105  O  O   . VAL A  1 16  ? -29.667 2.075   2.823   1.00 13.96 ? 16   VAL A O   1 
ATOM   106  C  CB  . VAL A  1 16  ? -30.308 2.385   -0.203  1.00 13.03 ? 16   VAL A CB  1 
ATOM   107  C  CG1 . VAL A  1 16  ? -28.973 1.778   -0.636  1.00 14.47 ? 16   VAL A CG1 1 
ATOM   108  C  CG2 . VAL A  1 16  ? -31.215 2.583   -1.399  1.00 13.43 ? 16   VAL A CG2 1 
ATOM   109  N  N   . THR A  1 17  ? -29.628 -0.086  2.082   1.00 12.22 ? 17   THR A N   1 
ATOM   110  C  CA  . THR A  1 17  ? -28.634 -0.553  3.064   1.00 13.37 ? 17   THR A CA  1 
ATOM   111  C  C   . THR A  1 17  ? -27.461 -1.272  2.397   1.00 13.43 ? 17   THR A C   1 
ATOM   112  O  O   . THR A  1 17  ? -26.540 -1.626  3.160   1.00 14.28 ? 17   THR A O   1 
ATOM   113  C  CB  . THR A  1 17  ? -29.245 -1.440  4.157   1.00 14.04 ? 17   THR A CB  1 
ATOM   114  O  OG1 . THR A  1 17  ? -29.665 -2.653  3.549   1.00 15.30 ? 17   THR A OG1 1 
ATOM   115  C  CG2 . THR A  1 17  ? -30.393 -0.773  4.891   1.00 14.23 ? 17   THR A CG2 1 
ATOM   116  N  N   . HIS A  1 18  ? -27.490 -1.531  1.082   1.00 11.93 ? 18   HIS A N   1 
ATOM   117  C  CA  . HIS A  1 18  ? -26.474 -2.395  0.428   1.00 12.48 ? 18   HIS A CA  1 
ATOM   118  C  C   . HIS A  1 18  ? -26.304 -3.698  1.222   1.00 10.87 ? 18   HIS A C   1 
ATOM   119  O  O   . HIS A  1 18  ? -25.163 -4.137  1.433   1.00 11.51 ? 18   HIS A O   1 
ATOM   120  C  CB  . HIS A  1 18  ? -25.147 -1.631  0.320   1.00 12.72 ? 18   HIS A CB  1 
ATOM   121  C  CG  . HIS A  1 18  ? -25.294 -0.280  -0.304  1.00 14.14 ? 18   HIS A CG  1 
ATOM   122  N  ND1 . HIS A  1 18  ? -24.939 0.871   0.350   1.00 19.64 ? 18   HIS A ND1 1 
ATOM   123  C  CD2 . HIS A  1 18  ? -25.942 0.120   -1.427  1.00 16.23 ? 18   HIS A CD2 1 
ATOM   124  C  CE1 . HIS A  1 18  ? -25.233 1.918   -0.426  1.00 16.93 ? 18   HIS A CE1 1 
ATOM   125  N  NE2 . HIS A  1 18  ? -25.847 1.480   -1.513  1.00 14.87 ? 18   HIS A NE2 1 
ATOM   126  N  N   . CYS A  1 19  ? -27.396 -4.337  1.616   1.00 11.76 ? 19   CYS A N   1 
ATOM   127  C  CA  . CYS A  1 19  ? -27.383 -5.386  2.677   1.00 11.43 ? 19   CYS A CA  1 
ATOM   128  C  C   . CYS A  1 19  ? -26.457 -6.549  2.263   1.00 11.24 ? 19   CYS A C   1 
ATOM   129  O  O   . CYS A  1 19  ? -25.840 -7.129  3.162   1.00 11.17 ? 19   CYS A O   1 
ATOM   130  C  CB  . CYS A  1 19  ? -28.802 -5.851  3.014   1.00 11.79 ? 19   CYS A CB  1 
ATOM   131  S  SG  . CYS A  1 19  ? -29.574 -6.872  1.737   1.00 13.35 ? 19   CYS A SG  1 
ATOM   132  N  N   . ALA A  1 20  ? -26.343 -6.859  0.973   1.00 11.30 ? 20   ALA A N   1 
ATOM   133  C  CA  . ALA A  1 20  ? -25.638 -8.067  0.468   1.00 11.30 ? 20   ALA A CA  1 
ATOM   134  C  C   . ALA A  1 20  ? -24.227 -7.705  -0.000  1.00 11.02 ? 20   ALA A C   1 
ATOM   135  O  O   . ALA A  1 20  ? -23.559 -8.550  -0.619  1.00 9.98  ? 20   ALA A O   1 
ATOM   136  C  CB  . ALA A  1 20  ? -26.427 -8.713  -0.637  1.00 11.68 ? 20   ALA A CB  1 
ATOM   137  N  N   . SER A  1 21  ? -23.784 -6.471  0.226   1.00 10.28 ? 21   SER A N   1 
ATOM   138  C  CA  . SER A  1 21  ? -22.428 -6.071  -0.237  1.00 9.93  ? 21   SER A CA  1 
ATOM   139  C  C   . SER A  1 21  ? -21.425 -6.362  0.893   1.00 10.10 ? 21   SER A C   1 
ATOM   140  O  O   . SER A  1 21  ? -21.147 -5.529  1.760   1.00 10.98 ? 21   SER A O   1 
ATOM   141  C  CB  . SER A  1 21  ? -22.393 -4.631  -0.702  1.00 9.71  ? 21   SER A CB  1 
ATOM   142  O  OG  . SER A  1 21  ? -21.085 -4.335  -1.154  1.00 9.80  ? 21   SER A OG  1 
ATOM   143  N  N   . GLY A  1 22  ? -20.851 -7.552  0.871   1.00 10.52 ? 22   GLY A N   1 
ATOM   144  C  CA  . GLY A  1 22  ? -19.851 -7.967  1.847   1.00 10.50 ? 22   GLY A CA  1 
ATOM   145  C  C   . GLY A  1 22  ? -19.404 -9.361  1.536   1.00 10.24 ? 22   GLY A C   1 
ATOM   146  O  O   . GLY A  1 22  ? -19.919 -9.962  0.602   1.00 9.41  ? 22   GLY A O   1 
ATOM   147  N  N   . SER A  1 23  ? -18.410 -9.840  2.275   1.00 10.01 ? 23   SER A N   1 
ATOM   148  C  CA  . SER A  1 23  ? -17.740 -11.120 1.941   1.00 9.44  ? 23   SER A CA  1 
ATOM   149  C  C   . SER A  1 23  ? -17.064 -11.724 3.161   1.00 9.54  ? 23   SER A C   1 
ATOM   150  O  O   . SER A  1 23  ? -16.742 -11.046 4.150   1.00 10.51 ? 23   SER A O   1 
ATOM   151  C  CB  . SER A  1 23  ? -16.780 -10.911 0.804   1.00 9.72  ? 23   SER A CB  1 
ATOM   152  O  OG  . SER A  1 23  ? -15.996 -9.733  1.031   1.00 8.97  ? 23   SER A OG  1 
ATOM   153  N  N   . LEU A  1 24  ? -16.930 -13.034 3.122   1.00 10.57 ? 24   LEU A N   1 
ATOM   154  C  CA  . LEU A  1 24  ? -16.174 -13.835 4.093   1.00 9.97  ? 24   LEU A CA  1 
ATOM   155  C  C   . LEU A  1 24  ? -14.695 -13.806 3.676   1.00 10.71 ? 24   LEU A C   1 
ATOM   156  O  O   . LEU A  1 24  ? -14.409 -14.152 2.524   1.00 10.45 ? 24   LEU A O   1 
ATOM   157  C  CB  . LEU A  1 24  ? -16.747 -15.254 4.061   1.00 9.97  ? 24   LEU A CB  1 
ATOM   158  C  CG  . LEU A  1 24  ? -15.955 -16.315 4.827   1.00 9.67  ? 24   LEU A CG  1 
ATOM   159  C  CD1 . LEU A  1 24  ? -15.889 -16.039 6.316   1.00 9.77  ? 24   LEU A CD1 1 
ATOM   160  C  CD2 . LEU A  1 24  ? -16.508 -17.693 4.545   1.00 9.82  ? 24   LEU A CD2 1 
ATOM   161  N  N   . TYR A  1 25  ? -13.809 -13.403 4.573   1.00 11.45 ? 25   TYR A N   1 
ATOM   162  C  CA  . TYR A  1 25  ? -12.365 -13.209 4.279   1.00 11.53 ? 25   TYR A CA  1 
ATOM   163  C  C   . TYR A  1 25  ? -12.201 -12.398 2.978   1.00 11.91 ? 25   TYR A C   1 
ATOM   164  O  O   . TYR A  1 25  ? -11.216 -12.559 2.286   1.00 12.56 ? 25   TYR A O   1 
ATOM   165  C  CB  . TYR A  1 25  ? -11.692 -14.566 4.122   1.00 11.44 ? 25   TYR A CB  1 
ATOM   166  C  CG  . TYR A  1 25  ? -11.409 -15.338 5.393   1.00 11.46 ? 25   TYR A CG  1 
ATOM   167  C  CD1 . TYR A  1 25  ? -12.381 -16.102 6.021   1.00 12.07 ? 25   TYR A CD1 1 
ATOM   168  C  CD2 . TYR A  1 25  ? -10.114 -15.451 5.877   1.00 12.30 ? 25   TYR A CD2 1 
ATOM   169  C  CE1 . TYR A  1 25  ? -12.110 -16.840 7.164   1.00 12.97 ? 25   TYR A CE1 1 
ATOM   170  C  CE2 . TYR A  1 25  ? -9.818  -16.216 7.008   1.00 12.01 ? 25   TYR A CE2 1 
ATOM   171  C  CZ  . TYR A  1 25  ? -10.807 -16.963 7.629   1.00 13.01 ? 25   TYR A CZ  1 
ATOM   172  O  OH  . TYR A  1 25  ? -10.511 -17.720 8.745   1.00 12.20 ? 25   TYR A OH  1 
ATOM   173  N  N   . GLY A  1 26  ? -13.145 -11.513 2.661   1.00 11.69 ? 26   GLY A N   1 
ATOM   174  C  CA  . GLY A  1 26  ? -13.039 -10.623 1.495   1.00 11.29 ? 26   GLY A CA  1 
ATOM   175  C  C   . GLY A  1 26  ? -12.156 -9.408  1.734   1.00 11.76 ? 26   GLY A C   1 
ATOM   176  O  O   . GLY A  1 26  ? -11.690 -8.813  0.755   1.00 11.34 ? 26   GLY A O   1 
ATOM   177  N  N   . VAL A  1 27  ? -11.952 -9.041  3.003   1.00 11.92 ? 27   VAL A N   1 
ATOM   178  C  CA  . VAL A  1 27  ? -10.947 -8.047  3.459   1.00 11.57 ? 27   VAL A CA  1 
ATOM   179  C  C   . VAL A  1 27  ? -10.144 -8.698  4.583   1.00 12.17 ? 27   VAL A C   1 
ATOM   180  O  O   . VAL A  1 27  ? -10.717 -9.410  5.404   1.00 11.91 ? 27   VAL A O   1 
ATOM   181  C  CB  . VAL A  1 27  ? -11.629 -6.745  3.924   1.00 12.30 ? 27   VAL A CB  1 
ATOM   182  C  CG1 . VAL A  1 27  ? -10.618 -5.665  4.273   1.00 12.01 ? 27   VAL A CG1 1 
ATOM   183  C  CG2 . VAL A  1 27  ? -12.600 -6.236  2.904   1.00 12.69 ? 27   VAL A CG2 1 
ATOM   184  N  N   . THR A  1 28  ? -8.840  -8.458  4.603   1.00 13.19 ? 28   THR A N   1 
ATOM   185  C  CA  . THR A  1 28  ? -7.923  -9.003  5.637   1.00 13.10 ? 28   THR A CA  1 
ATOM   186  C  C   . THR A  1 28  ? -7.083  -7.866  6.189   1.00 15.58 ? 28   THR A C   1 
ATOM   187  O  O   . THR A  1 28  ? -7.389  -6.693  5.900   1.00 13.81 ? 28   THR A O   1 
ATOM   188  C  CB  . THR A  1 28  ? -7.052  -10.119 5.049   1.00 13.62 ? 28   THR A CB  1 
ATOM   189  O  OG1 . THR A  1 28  ? -6.072  -9.512  4.210   1.00 14.01 ? 28   THR A OG1 1 
ATOM   190  C  CG2 . THR A  1 28  ? -7.849  -11.147 4.278   1.00 13.43 ? 28   THR A CG2 1 
ATOM   191  N  N   . GLU A  1 29  ? -6.011  -8.198  6.902   1.00 16.58 ? 29   GLU A N   1 
ATOM   192  C  CA  . GLU A  1 29  ? -5.082  -7.175  7.434   1.00 17.39 ? 29   GLU A CA  1 
ATOM   193  C  C   . GLU A  1 29  ? -4.277  -6.531  6.308   1.00 18.99 ? 29   GLU A C   1 
ATOM   194  O  O   . GLU A  1 29  ? -3.698  -5.483  6.533   1.00 23.68 ? 29   GLU A O   1 
ATOM   195  C  CB  . GLU A  1 29  ? -4.060  -7.789  8.395   1.00 20.08 ? 29   GLU A CB  1 
ATOM   196  C  CG  . GLU A  1 29  ? -4.672  -8.678  9.419   1.00 18.92 ? 29   GLU A CG  1 
ATOM   197  C  CD  . GLU A  1 29  ? -4.768  -10.164 9.088   1.00 17.97 ? 29   GLU A CD  1 
ATOM   198  O  OE1 . GLU A  1 29  ? -4.964  -10.567 7.860   1.00 14.19 ? 29   GLU A OE1 1 
ATOM   199  O  OE2 . GLU A  1 29  ? -4.710  -10.930 10.053  1.00 16.81 ? 29   GLU A OE2 1 
ATOM   200  N  N   A SER A  1 30  ? -4.217  -7.183  5.148   0.50 18.68 ? 30   SER A N   1 
ATOM   201  N  N   B SER A  1 30  ? -4.215  -7.109  5.112   0.50 17.52 ? 30   SER A N   1 
ATOM   202  C  CA  A SER A  1 30  ? -3.291  -6.868  4.038   0.50 18.55 ? 30   SER A CA  1 
ATOM   203  C  CA  B SER A  1 30  ? -3.335  -6.586  4.040   0.50 16.78 ? 30   SER A CA  1 
ATOM   204  C  C   A SER A  1 30  ? -4.050  -6.495  2.757   0.50 17.32 ? 30   SER A C   1 
ATOM   205  C  C   B SER A  1 30  ? -4.019  -6.529  2.675   0.50 16.44 ? 30   SER A C   1 
ATOM   206  O  O   A SER A  1 30  ? -3.533  -5.678  1.995   0.50 16.56 ? 30   SER A O   1 
ATOM   207  O  O   B SER A  1 30  ? -3.375  -6.010  1.741   0.50 15.59 ? 30   SER A O   1 
ATOM   208  C  CB  A SER A  1 30  ? -2.362  -8.053  3.805   0.50 19.54 ? 30   SER A CB  1 
ATOM   209  C  CB  B SER A  1 30  ? -2.080  -7.422  3.967   0.50 17.14 ? 30   SER A CB  1 
ATOM   210  O  OG  A SER A  1 30  ? -1.979  -8.658  5.039   0.50 20.64 ? 30   SER A OG  1 
ATOM   211  O  OG  B SER A  1 30  ? -2.406  -8.785  3.715   0.50 15.44 ? 30   SER A OG  1 
ATOM   212  N  N   . LYS A  1 31  ? -5.231  -7.088  2.523   1.00 16.65 ? 31   LYS A N   1 
ATOM   213  C  CA  . LYS A  1 31  ? -5.876  -7.140  1.188   1.00 16.06 ? 31   LYS A CA  1 
ATOM   214  C  C   . LYS A  1 31  ? -7.350  -6.770  1.307   1.00 14.55 ? 31   LYS A C   1 
ATOM   215  O  O   . LYS A  1 31  ? -8.004  -7.146  2.287   1.00 14.94 ? 31   LYS A O   1 
ATOM   216  C  CB  . LYS A  1 31  ? -5.701  -8.539  0.613   1.00 17.47 ? 31   LYS A CB  1 
ATOM   217  C  CG  . LYS A  1 31  ? -4.249  -8.893  0.303   1.00 19.06 ? 31   LYS A CG  1 
ATOM   218  C  CD  . LYS A  1 31  ? -4.119  -10.311 -0.136  1.00 23.41 ? 31   LYS A CD  1 
ATOM   219  C  CE  . LYS A  1 31  ? -2.717  -10.718 -0.546  1.00 24.86 ? 31   LYS A CE  1 
ATOM   220  N  NZ  . LYS A  1 31  ? -2.742  -12.149 -0.920  1.00 27.40 ? 31   LYS A NZ  1 
ATOM   221  N  N   . PRO A  1 32  ? -7.915  -6.031  0.335   1.00 13.84 ? 32   PRO A N   1 
ATOM   222  C  CA  . PRO A  1 32  ? -7.145  -5.325  -0.687  1.00 14.40 ? 32   PRO A CA  1 
ATOM   223  C  C   . PRO A  1 32  ? -6.172  -4.333  -0.068  1.00 15.27 ? 32   PRO A C   1 
ATOM   224  O  O   . PRO A  1 32  ? -6.395  -3.892  1.067   1.00 14.12 ? 32   PRO A O   1 
ATOM   225  C  CB  . PRO A  1 32  ? -8.186  -4.520  -1.453  1.00 14.47 ? 32   PRO A CB  1 
ATOM   226  C  CG  . PRO A  1 32  ? -9.449  -5.341  -1.274  1.00 14.24 ? 32   PRO A CG  1 
ATOM   227  C  CD  . PRO A  1 32  ? -9.373  -5.869  0.144   1.00 13.06 ? 32   PRO A CD  1 
ATOM   228  N  N   . PHE A  1 33  ? -5.044  -4.092  -0.748  1.00 15.24 ? 33   PHE A N   1 
ATOM   229  C  CA  . PHE A  1 33  ? -4.020  -3.195  -0.168  1.00 16.25 ? 33   PHE A CA  1 
ATOM   230  C  C   . PHE A  1 33  ? -4.558  -1.768  -0.143  1.00 16.79 ? 33   PHE A C   1 
ATOM   231  O  O   . PHE A  1 33  ? -4.295  -1.057  0.878   1.00 17.67 ? 33   PHE A O   1 
ATOM   232  C  CB  . PHE A  1 33  ? -2.697  -3.335  -0.921  1.00 16.28 ? 33   PHE A CB  1 
ATOM   233  C  CG  . PHE A  1 33  ? -1.602  -2.428  -0.396  1.00 16.76 ? 33   PHE A CG  1 
ATOM   234  C  CD1 . PHE A  1 33  ? -1.096  -2.586  0.889   1.00 17.91 ? 33   PHE A CD1 1 
ATOM   235  C  CD2 . PHE A  1 33  ? -1.176  -1.339  -1.140  1.00 18.52 ? 33   PHE A CD2 1 
ATOM   236  C  CE1 . PHE A  1 33  ? -0.115  -1.720  1.373   1.00 18.98 ? 33   PHE A CE1 1 
ATOM   237  C  CE2 . PHE A  1 33  ? -0.155  -0.510  -0.679  1.00 18.31 ? 33   PHE A CE2 1 
ATOM   238  C  CZ  . PHE A  1 33  ? 0.363   -0.701  0.584   1.00 18.89 ? 33   PHE A CZ  1 
ATOM   239  N  N   . ASP A  1 34  ? -5.280  -1.373  -1.186  1.00 15.68 ? 34   ASP A N   1 
ATOM   240  C  CA  . ASP A  1 34  ? -5.791  0.002   -1.395  1.00 16.61 ? 34   ASP A CA  1 
ATOM   241  C  C   . ASP A  1 34  ? -7.285  0.024   -1.052  1.00 16.39 ? 34   ASP A C   1 
ATOM   242  O  O   . ASP A  1 34  ? -8.110  -0.153  -1.976  1.00 17.07 ? 34   ASP A O   1 
ATOM   243  C  CB  . ASP A  1 34  ? -5.514  0.487   -2.823  1.00 16.54 ? 34   ASP A CB  1 
ATOM   244  C  CG  . ASP A  1 34  ? -5.789  1.979   -2.973  1.00 19.39 ? 34   ASP A CG  1 
ATOM   245  O  OD1 . ASP A  1 34  ? -6.437  2.530   -2.085  1.00 18.42 ? 34   ASP A OD1 1 
ATOM   246  O  OD2 . ASP A  1 34  ? -5.330  2.563   -3.955  1.00 22.65 ? 34   ASP A OD2 1 
ATOM   247  N  N   . ILE A  1 35  ? -7.592  0.287   0.215   1.00 16.93 ? 35   ILE A N   1 
ATOM   248  C  CA  . ILE A  1 35  ? -8.996  0.298   0.740   1.00 17.16 ? 35   ILE A CA  1 
ATOM   249  C  C   . ILE A  1 35  ? -9.817  1.359   0.005   1.00 16.90 ? 35   ILE A C   1 
ATOM   250  O  O   . ILE A  1 35  ? -10.946 1.089   -0.399  1.00 14.86 ? 35   ILE A O   1 
ATOM   251  C  CB  . ILE A  1 35  ? -9.007  0.525   2.259   1.00 17.29 ? 35   ILE A CB  1 
ATOM   252  C  CG1 . ILE A  1 35  ? -8.383  -0.648  3.014   1.00 17.55 ? 35   ILE A CG1 1 
ATOM   253  C  CG2 . ILE A  1 35  ? -10.410 0.794   2.763   1.00 16.88 ? 35   ILE A CG2 1 
ATOM   254  C  CD1 . ILE A  1 35  ? -9.201  -1.946  2.968   1.00 18.19 ? 35   ILE A CD1 1 
ATOM   255  N  N   . ASN A  1 36  ? -9.272  2.561   -0.184  1.00 18.58 ? 36   ASN A N   1 
ATOM   256  C  CA  . ASN A  1 36  ? -10.012 3.687   -0.788  1.00 19.61 ? 36   ASN A CA  1 
ATOM   257  C  C   . ASN A  1 36  ? -10.343 3.362   -2.249  1.00 17.99 ? 36   ASN A C   1 
ATOM   258  O  O   . ASN A  1 36  ? -11.410 3.768   -2.720  1.00 17.16 ? 36   ASN A O   1 
ATOM   259  C  CB  . ASN A  1 36  ? -9.214  4.987   -0.683  1.00 24.18 ? 36   ASN A CB  1 
ATOM   260  C  CG  . ASN A  1 36  ? -10.044 6.197   -1.060  1.00 31.73 ? 36   ASN A CG  1 
ATOM   261  O  OD1 . ASN A  1 36  ? -10.951 6.588   -0.317  1.00 38.27 ? 36   ASN A OD1 1 
ATOM   262  N  ND2 . ASN A  1 36  ? -9.787  6.755   -2.233  1.00 33.18 ? 36   ASN A ND2 1 
ATOM   263  N  N   . GLN A  1 37  ? -9.430  2.690   -2.959  1.00 16.70 ? 37   GLN A N   1 
ATOM   264  C  CA  . GLN A  1 37  ? -9.629  2.355   -4.397  1.00 18.02 ? 37   GLN A CA  1 
ATOM   265  C  C   . GLN A  1 37  ? -10.678 1.240   -4.529  1.00 15.52 ? 37   GLN A C   1 
ATOM   266  O  O   . GLN A  1 37  ? -11.535 1.318   -5.428  1.00 16.53 ? 37   GLN A O   1 
ATOM   267  C  CB  . GLN A  1 37  ? -8.314  1.911   -5.049  1.00 19.05 ? 37   GLN A CB  1 
ATOM   268  C  CG  . GLN A  1 37  ? -8.417  1.609   -6.542  1.00 20.88 ? 37   GLN A CG  1 
ATOM   269  C  CD  . GLN A  1 37  ? -7.071  1.435   -7.226  1.00 24.27 ? 37   GLN A CD  1 
ATOM   270  O  OE1 . GLN A  1 37  ? -5.998  1.527   -6.620  1.00 27.38 ? 37   GLN A OE1 1 
ATOM   271  N  NE2 . GLN A  1 37  ? -7.130  1.114   -8.502  1.00 22.95 ? 37   GLN A NE2 1 
ATOM   272  N  N   . PHE A  1 38  ? -10.529 0.161   -3.762  1.00 14.76 ? 38   PHE A N   1 
ATOM   273  C  CA  . PHE A  1 38  ? -11.250 -1.112  -4.044  1.00 14.19 ? 38   PHE A CA  1 
ATOM   274  C  C   . PHE A  1 38  ? -12.412 -1.351  -3.081  1.00 13.67 ? 38   PHE A C   1 
ATOM   275  O  O   . PHE A  1 38  ? -13.375 -1.995  -3.516  1.00 13.87 ? 38   PHE A O   1 
ATOM   276  C  CB  . PHE A  1 38  ? -10.289 -2.297  -4.036  1.00 14.84 ? 38   PHE A CB  1 
ATOM   277  C  CG  . PHE A  1 38  ? -9.319  -2.226  -5.179  1.00 15.13 ? 38   PHE A CG  1 
ATOM   278  C  CD1 . PHE A  1 38  ? -9.732  -2.449  -6.476  1.00 17.40 ? 38   PHE A CD1 1 
ATOM   279  C  CD2 . PHE A  1 38  ? -7.985  -1.927  -4.950  1.00 15.52 ? 38   PHE A CD2 1 
ATOM   280  C  CE1 . PHE A  1 38  ? -8.836  -2.374  -7.533  1.00 18.56 ? 38   PHE A CE1 1 
ATOM   281  C  CE2 . PHE A  1 38  ? -7.088  -1.858  -6.001  1.00 16.90 ? 38   PHE A CE2 1 
ATOM   282  C  CZ  . PHE A  1 38  ? -7.516  -2.072  -7.294  1.00 18.49 ? 38   PHE A CZ  1 
ATOM   283  N  N   . VAL A  1 39  ? -12.366 -0.852  -1.844  1.00 13.45 ? 39   VAL A N   1 
ATOM   284  C  CA  . VAL A  1 39  ? -13.421 -1.185  -0.837  1.00 13.59 ? 39   VAL A CA  1 
ATOM   285  C  C   . VAL A  1 39  ? -14.389 0.002   -0.692  1.00 13.14 ? 39   VAL A C   1 
ATOM   286  O  O   . VAL A  1 39  ? -15.588 -0.192  -0.794  1.00 12.69 ? 39   VAL A O   1 
ATOM   287  C  CB  . VAL A  1 39  ? -12.821 -1.604  0.516   1.00 13.41 ? 39   VAL A CB  1 
ATOM   288  C  CG1 . VAL A  1 39  ? -13.915 -2.008  1.507   1.00 14.57 ? 39   VAL A CG1 1 
ATOM   289  C  CG2 . VAL A  1 39  ? -11.771 -2.706  0.342   1.00 12.86 ? 39   VAL A CG2 1 
ATOM   290  N  N   . ALA A  1 40  ? -13.896 1.201   -0.403  1.00 13.42 ? 40   ALA A N   1 
ATOM   291  C  CA  . ALA A  1 40  ? -14.751 2.360   -0.028  1.00 14.59 ? 40   ALA A CA  1 
ATOM   292  C  C   . ALA A  1 40  ? -15.841 2.581   -1.082  1.00 14.67 ? 40   ALA A C   1 
ATOM   293  O  O   . ALA A  1 40  ? -16.988 2.822   -0.730  1.00 14.98 ? 40   ALA A O   1 
ATOM   294  C  CB  . ALA A  1 40  ? -13.883 3.587   0.137   1.00 15.15 ? 40   ALA A CB  1 
ATOM   295  N  N   . PRO A  1 41  ? -15.559 2.538   -2.404  1.00 14.79 ? 41   PRO A N   1 
ATOM   296  C  CA  . PRO A  1 41  ? -16.564 2.881   -3.414  1.00 14.41 ? 41   PRO A CA  1 
ATOM   297  C  C   . PRO A  1 41  ? -17.768 1.934   -3.430  1.00 14.56 ? 41   PRO A C   1 
ATOM   298  O  O   . PRO A  1 41  ? -18.832 2.317   -3.910  1.00 15.70 ? 41   PRO A O   1 
ATOM   299  C  CB  . PRO A  1 41  ? -15.811 2.790   -4.760  1.00 15.58 ? 41   PRO A CB  1 
ATOM   300  C  CG  . PRO A  1 41  ? -14.363 2.969   -4.371  1.00 16.02 ? 41   PRO A CG  1 
ATOM   301  C  CD  . PRO A  1 41  ? -14.246 2.282   -3.017  1.00 16.82 ? 41   PRO A CD  1 
ATOM   302  N  N   . LEU A  1 42  ? -17.608 0.726   -2.892  1.00 12.84 ? 42   LEU A N   1 
ATOM   303  C  CA  . LEU A  1 42  ? -18.712 -0.237  -2.860  1.00 13.02 ? 42   LEU A CA  1 
ATOM   304  C  C   . LEU A  1 42  ? -19.698 0.133   -1.755  1.00 12.52 ? 42   LEU A C   1 
ATOM   305  O  O   . LEU A  1 42  ? -20.767 -0.475  -1.741  1.00 13.31 ? 42   LEU A O   1 
ATOM   306  C  CB  . LEU A  1 42  ? -18.151 -1.650  -2.662  1.00 12.55 ? 42   LEU A CB  1 
ATOM   307  C  CG  . LEU A  1 42  ? -17.199 -2.162  -3.733  1.00 13.36 ? 42   LEU A CG  1 
ATOM   308  C  CD1 . LEU A  1 42  ? -16.836 -3.618  -3.463  1.00 14.96 ? 42   LEU A CD1 1 
ATOM   309  C  CD2 . LEU A  1 42  ? -17.771 -2.021  -5.140  1.00 13.52 ? 42   LEU A CD2 1 
ATOM   310  N  N   . LYS A  1 43  ? -19.338 1.003   -0.795  1.00 13.17 ? 43   LYS A N   1 
ATOM   311  C  CA  . LYS A  1 43  ? -20.248 1.300   0.334   1.00 14.18 ? 43   LYS A CA  1 
ATOM   312  C  C   . LYS A  1 43  ? -20.733 -0.012  0.944   1.00 13.51 ? 43   LYS A C   1 
ATOM   313  O  O   . LYS A  1 43  ? -21.947 -0.252  1.110   1.00 12.91 ? 43   LYS A O   1 
ATOM   314  C  CB  . LYS A  1 43  ? -21.404 2.193   -0.139  1.00 15.73 ? 43   LYS A CB  1 
ATOM   315  C  CG  . LYS A  1 43  ? -20.945 3.462   -0.844  1.00 18.47 ? 43   LYS A CG  1 
ATOM   316  C  CD  . LYS A  1 43  ? -20.322 4.446   0.064   1.00 22.77 ? 43   LYS A CD  1 
ATOM   317  C  CE  . LYS A  1 43  ? -19.735 5.631   -0.671  1.00 27.68 ? 43   LYS A CE  1 
ATOM   318  N  NZ  . LYS A  1 43  ? -20.677 6.120   -1.698  1.00 31.41 ? 43   LYS A NZ  1 
ATOM   319  N  N   . PRO A  1 44  ? -19.788 -0.889  1.346   1.00 12.27 ? 44   PRO A N   1 
ATOM   320  C  CA  . PRO A  1 44  ? -20.151 -2.228  1.813   1.00 12.23 ? 44   PRO A CA  1 
ATOM   321  C  C   . PRO A  1 44  ? -20.879 -2.228  3.161   1.00 12.44 ? 44   PRO A C   1 
ATOM   322  O  O   . PRO A  1 44  ? -20.842 -1.242  3.898   1.00 12.60 ? 44   PRO A O   1 
ATOM   323  C  CB  . PRO A  1 44  ? -18.794 -2.912  1.945   1.00 12.01 ? 44   PRO A CB  1 
ATOM   324  C  CG  . PRO A  1 44  ? -17.885 -1.756  2.359   1.00 11.84 ? 44   PRO A CG  1 
ATOM   325  C  CD  . PRO A  1 44  ? -18.329 -0.652  1.422   1.00 11.74 ? 44   PRO A CD  1 
ATOM   326  N  N   . ASN A  1 45  ? -21.563 -3.338  3.439   1.00 12.57 ? 45   ASN A N   1 
ATOM   327  C  CA  . ASN A  1 45  ? -22.344 -3.501  4.680   1.00 12.26 ? 45   ASN A CA  1 
ATOM   328  C  C   . ASN A  1 45  ? -21.507 -4.299  5.683   1.00 12.72 ? 45   ASN A C   1 
ATOM   329  O  O   . ASN A  1 45  ? -20.826 -3.668  6.525   1.00 14.85 ? 45   ASN A O   1 
ATOM   330  C  CB  . ASN A  1 45  ? -23.716 -4.093  4.340   1.00 12.72 ? 45   ASN A CB  1 
ATOM   331  C  CG  . ASN A  1 45  ? -24.559 -4.259  5.575   1.00 14.85 ? 45   ASN A CG  1 
ATOM   332  O  OD1 . ASN A  1 45  ? -24.445 -3.460  6.512   1.00 15.21 ? 45   ASN A OD1 1 
ATOM   333  N  ND2 . ASN A  1 45  ? -25.400 -5.286  5.573   1.00 14.13 ? 45   ASN A ND2 1 
ATOM   334  N  N   . VAL A  1 46  ? -21.551 -5.633  5.624   1.00 11.79 ? 46   VAL A N   1 
ATOM   335  C  CA  . VAL A  1 46  ? -20.934 -6.510  6.664   1.00 11.98 ? 46   VAL A CA  1 
ATOM   336  C  C   . VAL A  1 46  ? -19.942 -7.483  6.020   1.00 11.52 ? 46   VAL A C   1 
ATOM   337  O  O   . VAL A  1 46  ? -20.265 -8.087  4.971   1.00 12.27 ? 46   VAL A O   1 
ATOM   338  C  CB  . VAL A  1 46  ? -21.999 -7.301  7.447   1.00 11.67 ? 46   VAL A CB  1 
ATOM   339  C  CG1 . VAL A  1 46  ? -21.336 -8.333  8.332   1.00 12.67 ? 46   VAL A CG1 1 
ATOM   340  C  CG2 . VAL A  1 46  ? -22.870 -6.397  8.274   1.00 11.70 ? 46   VAL A CG2 1 
ATOM   341  N  N   . PHE A  1 47  ? -18.760 -7.587  6.597   1.00 11.33 ? 47   PHE A N   1 
ATOM   342  C  CA  . PHE A  1 47  ? -17.720 -8.586  6.263   1.00 11.25 ? 47   PHE A CA  1 
ATOM   343  C  C   . PHE A  1 47  ? -17.659 -9.590  7.411   1.00 10.89 ? 47   PHE A C   1 
ATOM   344  O  O   . PHE A  1 47  ? -17.777 -9.180  8.596   1.00 12.90 ? 47   PHE A O   1 
ATOM   345  C  CB  . PHE A  1 47  ? -16.363 -7.904  6.108   1.00 10.94 ? 47   PHE A CB  1 
ATOM   346  C  CG  . PHE A  1 47  ? -16.312 -6.978  4.929   1.00 10.24 ? 47   PHE A CG  1 
ATOM   347  C  CD1 . PHE A  1 47  ? -16.091 -7.454  3.659   1.00 10.93 ? 47   PHE A CD1 1 
ATOM   348  C  CD2 . PHE A  1 47  ? -16.620 -5.622  5.078   1.00 10.50 ? 47   PHE A CD2 1 
ATOM   349  C  CE1 . PHE A  1 47  ? -16.056 -6.599  2.568   1.00 11.40 ? 47   PHE A CE1 1 
ATOM   350  C  CE2 . PHE A  1 47  ? -16.556 -4.761  3.985   1.00 10.86 ? 47   PHE A CE2 1 
ATOM   351  C  CZ  . PHE A  1 47  ? -16.285 -5.255  2.726   1.00 11.23 ? 47   PHE A CZ  1 
ATOM   352  N  N   . THR A  1 48  ? -17.442 -10.860 7.101   1.00 9.83  ? 48   THR A N   1 
ATOM   353  C  CA  . THR A  1 48  ? -17.239 -11.885 8.134   1.00 9.80  ? 48   THR A CA  1 
ATOM   354  C  C   . THR A  1 48  ? -15.758 -12.237 8.152   1.00 10.46 ? 48   THR A C   1 
ATOM   355  O  O   . THR A  1 48  ? -15.226 -12.580 7.085   1.00 9.77  ? 48   THR A O   1 
ATOM   356  C  CB  . THR A  1 48  ? -18.122 -13.110 7.886   1.00 10.03 ? 48   THR A CB  1 
ATOM   357  O  OG1 . THR A  1 48  ? -19.476 -12.666 8.000   1.00 10.09 ? 48   THR A OG1 1 
ATOM   358  C  CG2 . THR A  1 48  ? -17.916 -14.224 8.878   1.00 9.84  ? 48   THR A CG2 1 
ATOM   359  N  N   . ASN A  1 49  ? -15.180 -12.201 9.338   1.00 10.11 ? 49   ASN A N   1 
ATOM   360  C  CA  . ASN A  1 49  ? -13.728 -12.416 9.522   1.00 10.76 ? 49   ASN A CA  1 
ATOM   361  C  C   . ASN A  1 49  ? -13.479 -13.280 10.748  1.00 10.36 ? 49   ASN A C   1 
ATOM   362  O  O   . ASN A  1 49  ? -14.189 -13.202 11.735  1.00 9.46  ? 49   ASN A O   1 
ATOM   363  C  CB  . ASN A  1 49  ? -13.009 -11.087 9.681   1.00 10.80 ? 49   ASN A CB  1 
ATOM   364  C  CG  . ASN A  1 49  ? -12.812 -10.421 8.343   1.00 11.02 ? 49   ASN A CG  1 
ATOM   365  O  OD1 . ASN A  1 49  ? -13.770 -9.863  7.782   1.00 11.54 ? 49   ASN A OD1 1 
ATOM   366  N  ND2 . ASN A  1 49  ? -11.603 -10.517 7.812   1.00 10.76 ? 49   ASN A ND2 1 
ATOM   367  N  N   . PRO A  1 50  ? -12.422 -14.121 10.705  1.00 11.71 ? 50   PRO A N   1 
ATOM   368  C  CA  . PRO A  1 50  ? -12.071 -14.970 11.834  1.00 10.87 ? 50   PRO A CA  1 
ATOM   369  C  C   . PRO A  1 50  ? -11.688 -14.135 13.064  1.00 10.90 ? 50   PRO A C   1 
ATOM   370  O  O   . PRO A  1 50  ? -11.051 -13.075 12.928  1.00 10.97 ? 50   PRO A O   1 
ATOM   371  C  CB  . PRO A  1 50  ? -10.816 -15.724 11.336  1.00 10.70 ? 50   PRO A CB  1 
ATOM   372  C  CG  . PRO A  1 50  ? -10.250 -14.790 10.292  1.00 11.31 ? 50   PRO A CG  1 
ATOM   373  C  CD  . PRO A  1 50  ? -11.470 -14.225 9.593   1.00 11.67 ? 50   PRO A CD  1 
ATOM   374  N  N   . ALA A  1 51  ? -12.029 -14.620 14.249  1.00 11.26 ? 51   ALA A N   1 
ATOM   375  C  CA  . ALA A  1 51  ? -11.723 -13.917 15.503  1.00 11.47 ? 51   ALA A CA  1 
ATOM   376  C  C   . ALA A  1 51  ? -10.216 -13.739 15.576  1.00 12.32 ? 51   ALA A C   1 
ATOM   377  O  O   . ALA A  1 51  ? -9.772  -12.729 16.104  1.00 13.30 ? 51   ALA A O   1 
ATOM   378  C  CB  . ALA A  1 51  ? -12.221 -14.641 16.717  1.00 11.78 ? 51   ALA A CB  1 
ATOM   379  N  N   . LEU A  1 52  ? -9.479  -14.787 15.208  1.00 12.74 ? 52   LEU A N   1 
ATOM   380  C  CA  . LEU A  1 52  ? -7.992  -14.795 15.290  1.00 13.24 ? 52   LEU A CA  1 
ATOM   381  C  C   . LEU A  1 52  ? -7.431  -15.427 14.021  1.00 13.77 ? 52   LEU A C   1 
ATOM   382  O  O   . LEU A  1 52  ? -8.130  -16.261 13.377  1.00 13.84 ? 52   LEU A O   1 
ATOM   383  C  CB  . LEU A  1 52  ? -7.503  -15.562 16.526  1.00 13.90 ? 52   LEU A CB  1 
ATOM   384  C  CG  . LEU A  1 52  ? -7.951  -15.025 17.884  1.00 15.20 ? 52   LEU A CG  1 
ATOM   385  C  CD1 . LEU A  1 52  ? -7.608  -15.991 18.997  1.00 16.11 ? 52   LEU A CD1 1 
ATOM   386  C  CD2 . LEU A  1 52  ? -7.371  -13.644 18.171  1.00 16.17 ? 52   LEU A CD2 1 
ATOM   387  N  N   . ALA A  1 53  ? -6.183  -15.101 13.712  1.00 14.19 ? 53   ALA A N   1 
ATOM   388  C  CA  . ALA A  1 53  ? -5.507  -15.678 12.537  1.00 14.96 ? 53   ALA A CA  1 
ATOM   389  C  C   . ALA A  1 53  ? -4.067  -16.049 12.923  1.00 16.21 ? 53   ALA A C   1 
ATOM   390  O  O   . ALA A  1 53  ? -3.462  -15.335 13.759  1.00 16.15 ? 53   ALA A O   1 
ATOM   391  C  CB  . ALA A  1 53  ? -5.587  -14.728 11.371  1.00 15.48 ? 53   ALA A CB  1 
ATOM   392  N  N   . GLY A  1 54  ? -3.569  -17.134 12.342  1.00 16.21 ? 54   GLY A N   1 
ATOM   393  C  CA  . GLY A  1 54  ? -2.187  -17.609 12.511  1.00 16.97 ? 54   GLY A CA  1 
ATOM   394  C  C   . GLY A  1 54  ? -2.095  -19.108 12.618  1.00 16.87 ? 54   GLY A C   1 
ATOM   395  O  O   . GLY A  1 54  ? -3.100  -19.804 12.439  1.00 14.34 ? 54   GLY A O   1 
ATOM   396  N  N   . PHE A  1 55  ? -0.907  -19.615 12.954  1.00 18.19 ? 55   PHE A N   1 
ATOM   397  C  CA  . PHE A  1 55  ? -0.646  -21.075 12.963  1.00 18.94 ? 55   PHE A CA  1 
ATOM   398  C  C   . PHE A  1 55  ? -1.550  -21.812 13.962  1.00 17.96 ? 55   PHE A C   1 
ATOM   399  O  O   . PHE A  1 55  ? -1.797  -23.020 13.789  1.00 18.72 ? 55   PHE A O   1 
ATOM   400  C  CB  . PHE A  1 55  ? 0.861   -21.262 13.202  1.00 21.60 ? 55   PHE A CB  1 
ATOM   401  C  CG  . PHE A  1 55  ? 1.779   -20.865 12.057  1.00 28.07 ? 55   PHE A CG  1 
ATOM   402  C  CD1 . PHE A  1 55  ? 1.302   -20.272 10.886  1.00 29.11 ? 55   PHE A CD1 1 
ATOM   403  C  CD2 . PHE A  1 55  ? 3.154   -21.094 12.155  1.00 31.12 ? 55   PHE A CD2 1 
ATOM   404  C  CE1 . PHE A  1 55  ? 2.170   -19.918 9.863   1.00 31.77 ? 55   PHE A CE1 1 
ATOM   405  C  CE2 . PHE A  1 55  ? 4.014   -20.766 11.113  1.00 28.49 ? 55   PHE A CE2 1 
ATOM   406  C  CZ  . PHE A  1 55  ? 3.524   -20.162 9.980   1.00 30.04 ? 55   PHE A CZ  1 
ATOM   407  N  N   . ASN A  1 56  ? -2.035  -21.164 15.013  1.00 16.64 ? 56   ASN A N   1 
ATOM   408  C  CA  . ASN A  1 56  ? -2.848  -21.850 16.045  1.00 18.20 ? 56   ASN A CA  1 
ATOM   409  C  C   . ASN A  1 56  ? -4.338  -21.813 15.668  1.00 16.18 ? 56   ASN A C   1 
ATOM   410  O  O   . ASN A  1 56  ? -5.118  -22.375 16.445  1.00 17.22 ? 56   ASN A O   1 
ATOM   411  C  CB  . ASN A  1 56  ? -2.648  -21.287 17.451  1.00 19.93 ? 56   ASN A CB  1 
ATOM   412  C  CG  . ASN A  1 56  ? -1.259  -21.597 17.967  1.00 24.39 ? 56   ASN A CG  1 
ATOM   413  O  OD1 . ASN A  1 56  ? -0.604  -20.747 18.550  1.00 32.61 ? 56   ASN A OD1 1 
ATOM   414  N  ND2 . ASN A  1 56  ? -0.790  -22.781 17.676  1.00 22.99 ? 56   ASN A ND2 1 
ATOM   415  N  N   . HIS A  1 57  ? -4.689  -21.227 14.526  1.00 14.96 ? 57   HIS A N   1 
ATOM   416  C  CA  . HIS A  1 57  ? -6.090  -20.845 14.177  1.00 13.86 ? 57   HIS A CA  1 
ATOM   417  C  C   . HIS A  1 57  ? -6.468  -21.422 12.803  1.00 13.82 ? 57   HIS A C   1 
ATOM   418  O  O   . HIS A  1 57  ? -5.670  -22.171 12.175  1.00 14.00 ? 57   HIS A O   1 
ATOM   419  C  CB  . HIS A  1 57  ? -6.249  -19.315 14.306  1.00 14.25 ? 57   HIS A CB  1 
ATOM   420  C  CG  . HIS A  1 57  ? -5.771  -18.817 15.622  1.00 13.43 ? 57   HIS A CG  1 
ATOM   421  N  ND1 . HIS A  1 57  ? -6.323  -19.224 16.798  1.00 14.70 ? 57   HIS A ND1 1 
ATOM   422  C  CD2 . HIS A  1 57  ? -4.710  -18.043 15.946  1.00 15.74 ? 57   HIS A CD2 1 
ATOM   423  C  CE1 . HIS A  1 57  ? -5.648  -18.715 17.828  1.00 14.97 ? 57   HIS A CE1 1 
ATOM   424  N  NE2 . HIS A  1 57  ? -4.662  -17.961 17.329  1.00 15.72 ? 57   HIS A NE2 1 
ATOM   425  N  N   . GLN A  1 58  ? -7.710  -21.183 12.389  1.00 14.77 ? 58   GLN A N   1 
ATOM   426  C  CA  . GLN A  1 58  ? -8.274  -21.779 11.150  1.00 14.40 ? 58   GLN A CA  1 
ATOM   427  C  C   . GLN A  1 58  ? -7.464  -21.370 9.926   1.00 14.80 ? 58   GLN A C   1 
ATOM   428  O  O   . GLN A  1 58  ? -7.237  -22.239 9.052   1.00 14.31 ? 58   GLN A O   1 
ATOM   429  C  CB  . GLN A  1 58  ? -9.753  -21.404 11.001  1.00 14.29 ? 58   GLN A CB  1 
ATOM   430  C  CG  . GLN A  1 58  ? -10.414 -22.091 9.825   1.00 14.58 ? 58   GLN A CG  1 
ATOM   431  C  CD  . GLN A  1 58  ? -10.533 -23.588 9.936   1.00 16.40 ? 58   GLN A CD  1 
ATOM   432  O  OE1 . GLN A  1 58  ? -10.442 -24.225 11.009  1.00 16.66 ? 58   GLN A OE1 1 
ATOM   433  N  NE2 . GLN A  1 58  ? -10.761 -24.178 8.787   1.00 15.69 ? 58   GLN A NE2 1 
ATOM   434  N  N   . GLN A  1 59  ? -7.065  -20.105 9.824   1.00 13.51 ? 59   GLN A N   1 
ATOM   435  C  CA  . GLN A  1 59  ? -6.340  -19.571 8.658   1.00 15.16 ? 59   GLN A CA  1 
ATOM   436  C  C   . GLN A  1 59  ? -5.206  -18.661 9.122   1.00 14.33 ? 59   GLN A C   1 
ATOM   437  O  O   . GLN A  1 59  ? -5.220  -18.147 10.240  1.00 14.29 ? 59   GLN A O   1 
ATOM   438  C  CB  . GLN A  1 59  ? -7.295  -18.799 7.745   1.00 16.43 ? 59   GLN A CB  1 
ATOM   439  C  CG  . GLN A  1 59  ? -8.368  -19.679 7.098   1.00 17.01 ? 59   GLN A CG  1 
ATOM   440  C  CD  . GLN A  1 59  ? -7.809  -20.632 6.073   1.00 18.76 ? 59   GLN A CD  1 
ATOM   441  O  OE1 . GLN A  1 59  ? -6.710  -20.465 5.569   1.00 20.99 ? 59   GLN A OE1 1 
ATOM   442  N  NE2 . GLN A  1 59  ? -8.585  -21.643 5.739   1.00 20.04 ? 59   GLN A NE2 1 
ATOM   443  N  N   . PRO A  1 60  ? -4.168  -18.480 8.288   1.00 17.92 ? 60   PRO A N   1 
ATOM   444  C  CA  . PRO A  1 60  ? -3.056  -17.608 8.655   1.00 17.81 ? 60   PRO A CA  1 
ATOM   445  C  C   . PRO A  1 60  ? -3.334  -16.112 8.477   1.00 17.09 ? 60   PRO A C   1 
ATOM   446  O  O   . PRO A  1 60  ? -2.489  -15.342 8.868   1.00 16.20 ? 60   PRO A O   1 
ATOM   447  C  CB  . PRO A  1 60  ? -1.966  -18.009 7.675   1.00 19.17 ? 60   PRO A CB  1 
ATOM   448  C  CG  . PRO A  1 60  ? -2.700  -18.516 6.483   1.00 21.08 ? 60   PRO A CG  1 
ATOM   449  C  CD  . PRO A  1 60  ? -3.954  -19.189 7.013   1.00 18.53 ? 60   PRO A CD  1 
ATOM   450  N  N   . ILE A  1 61  ? -4.472  -15.752 7.880   1.00 15.96 ? 61   ILE A N   1 
ATOM   451  C  CA  . ILE A  1 61  ? -4.830  -14.334 7.588   1.00 15.08 ? 61   ILE A CA  1 
ATOM   452  C  C   . ILE A  1 61  ? -6.274  -14.073 8.017   1.00 13.85 ? 61   ILE A C   1 
ATOM   453  O  O   . ILE A  1 61  ? -7.017  -15.061 8.278   1.00 13.56 ? 61   ILE A O   1 
ATOM   454  C  CB  . ILE A  1 61  ? -4.642  -13.980 6.094   1.00 17.76 ? 61   ILE A CB  1 
ATOM   455  C  CG1 . ILE A  1 61  ? -5.774  -14.477 5.177   1.00 18.96 ? 61   ILE A CG1 1 
ATOM   456  C  CG2 . ILE A  1 61  ? -3.256  -14.339 5.584   1.00 20.32 ? 61   ILE A CG2 1 
ATOM   457  C  CD1 . ILE A  1 61  ? -6.025  -15.963 5.062   1.00 20.30 ? 61   ILE A CD1 1 
ATOM   458  N  N   . GLY A  1 62  ? -6.634  -12.785 8.075   1.00 13.27 ? 62   GLY A N   1 
ATOM   459  C  CA  . GLY A  1 62  ? -8.035  -12.319 8.111   1.00 13.19 ? 62   GLY A CA  1 
ATOM   460  C  C   . GLY A  1 62  ? -8.479  -11.835 9.480   1.00 12.65 ? 62   GLY A C   1 
ATOM   461  O  O   . GLY A  1 62  ? -9.694  -11.629 9.638   1.00 13.22 ? 62   GLY A O   1 
ATOM   462  N  N   . ALA A  1 63  ? -7.590  -11.698 10.470  1.00 12.11 ? 63   ALA A N   1 
ATOM   463  C  CA  . ALA A  1 63  ? -7.977  -11.402 11.868  1.00 11.77 ? 63   ALA A CA  1 
ATOM   464  C  C   . ALA A  1 63  ? -8.992  -10.248 11.907  1.00 11.53 ? 63   ALA A C   1 
ATOM   465  O  O   . ALA A  1 63  ? -8.749  -9.184  11.276  1.00 12.41 ? 63   ALA A O   1 
ATOM   466  C  CB  . ALA A  1 63  ? -6.760  -11.118 12.719  1.00 13.54 ? 63   ALA A CB  1 
ATOM   467  N  N   . ALA A  1 64  ? -10.101 -10.450 12.602  1.00 10.83 ? 64   ALA A N   1 
ATOM   468  C  CA  . ALA A  1 64  ? -11.256 -9.526  12.565  1.00 12.04 ? 64   ALA A CA  1 
ATOM   469  C  C   . ALA A  1 64  ? -10.884 -8.127  13.083  1.00 12.92 ? 64   ALA A C   1 
ATOM   470  O  O   . ALA A  1 64  ? -11.389 -7.110  12.538  1.00 12.90 ? 64   ALA A O   1 
ATOM   471  C  CB  . ALA A  1 64  ? -12.385 -10.105 13.366  1.00 12.01 ? 64   ALA A CB  1 
ATOM   472  N  N   . ILE A  1 65  ? -10.141 -8.050  14.172  1.00 14.08 ? 65   ILE A N   1 
ATOM   473  C  CA  . ILE A  1 65  ? -9.946  -6.743  14.844  1.00 13.96 ? 65   ILE A CA  1 
ATOM   474  C  C   . ILE A  1 65  ? -9.101  -5.841  13.955  1.00 13.72 ? 65   ILE A C   1 
ATOM   475  O  O   . ILE A  1 65  ? -9.534  -4.730  13.638  1.00 13.42 ? 65   ILE A O   1 
ATOM   476  C  CB  . ILE A  1 65  ? -9.406  -6.929  16.268  1.00 16.59 ? 65   ILE A CB  1 
ATOM   477  C  CG1 . ILE A  1 65  ? -10.455 -7.583  17.168  1.00 18.83 ? 65   ILE A CG1 1 
ATOM   478  C  CG2 . ILE A  1 65  ? -8.958  -5.578  16.802  1.00 18.07 ? 65   ILE A CG2 1 
ATOM   479  C  CD1 . ILE A  1 65  ? -9.871  -8.189  18.415  1.00 22.52 ? 65   ILE A CD1 1 
ATOM   480  N  N   . PRO A  1 66  ? -7.896  -6.226  13.472  1.00 12.61 ? 66   PRO A N   1 
ATOM   481  C  CA  . PRO A  1 66  ? -7.184  -5.369  12.528  1.00 13.34 ? 66   PRO A CA  1 
ATOM   482  C  C   . PRO A  1 66  ? -7.906  -5.119  11.202  1.00 12.69 ? 66   PRO A C   1 
ATOM   483  O  O   . PRO A  1 66  ? -7.758  -4.059  10.632  1.00 12.57 ? 66   PRO A O   1 
ATOM   484  C  CB  . PRO A  1 66  ? -5.859  -6.076  12.242  1.00 14.23 ? 66   PRO A CB  1 
ATOM   485  C  CG  . PRO A  1 66  ? -6.035  -7.451  12.778  1.00 14.58 ? 66   PRO A CG  1 
ATOM   486  C  CD  . PRO A  1 66  ? -7.147  -7.451  13.796  1.00 14.01 ? 66   PRO A CD  1 
ATOM   487  N  N   . THR A  1 67  ? -8.712  -6.078  10.739  1.00 12.61 ? 67   THR A N   1 
ATOM   488  C  CA  . THR A  1 67  ? -9.538  -5.873  9.523   1.00 11.51 ? 67   THR A CA  1 
ATOM   489  C  C   . THR A  1 67  ? -10.560 -4.745  9.778   1.00 10.94 ? 67   THR A C   1 
ATOM   490  O  O   . THR A  1 67  ? -10.703 -3.858  8.925   1.00 12.25 ? 67   THR A O   1 
ATOM   491  C  CB  . THR A  1 67  ? -10.206 -7.179  9.092   1.00 11.24 ? 67   THR A CB  1 
ATOM   492  O  OG1 . THR A  1 67  ? -9.171  -8.124  8.814   1.00 10.42 ? 67   THR A OG1 1 
ATOM   493  C  CG2 . THR A  1 67  ? -11.073 -6.992  7.867   1.00 11.47 ? 67   THR A CG2 1 
ATOM   494  N  N   . ALA A  1 68  ? -11.213 -4.735  10.925  1.00 11.85 ? 68   ALA A N   1 
ATOM   495  C  CA  . ALA A  1 68  ? -12.194 -3.686  11.288  1.00 11.48 ? 68   ALA A CA  1 
ATOM   496  C  C   . ALA A  1 68  ? -11.470 -2.343  11.255  1.00 13.01 ? 68   ALA A C   1 
ATOM   497  O  O   . ALA A  1 68  ? -11.988 -1.345  10.683  1.00 12.90 ? 68   ALA A O   1 
ATOM   498  C  CB  . ALA A  1 68  ? -12.783 -3.972  12.644  1.00 12.33 ? 68   ALA A CB  1 
ATOM   499  N  N   . GLY A  1 69  ? -10.252 -2.323  11.792  1.00 12.20 ? 69   GLY A N   1 
ATOM   500  C  CA  . GLY A  1 69  ? -9.425  -1.096  11.800  1.00 13.11 ? 69   GLY A CA  1 
ATOM   501  C  C   . GLY A  1 69  ? -9.183  -0.556  10.403  1.00 13.86 ? 69   GLY A C   1 
ATOM   502  O  O   . GLY A  1 69  ? -9.388  0.674   10.185  1.00 15.29 ? 69   GLY A O   1 
ATOM   503  N  N   . ARG A  1 70  ? -8.833  -1.429  9.465   1.00 14.46 ? 70   ARG A N   1 
ATOM   504  C  CA  . ARG A  1 70  ? -8.572  -1.039  8.055   1.00 14.91 ? 70   ARG A CA  1 
ATOM   505  C  C   . ARG A  1 70  ? -9.846  -0.508  7.396   1.00 14.85 ? 70   ARG A C   1 
ATOM   506  O  O   . ARG A  1 70  ? -9.720  0.260   6.441   1.00 15.10 ? 70   ARG A O   1 
ATOM   507  C  CB  . ARG A  1 70  ? -8.019  -2.250  7.313   1.00 18.16 ? 70   ARG A CB  1 
ATOM   508  C  CG  . ARG A  1 70  ? -6.683  -2.722  7.862   1.00 20.99 ? 70   ARG A CG  1 
ATOM   509  C  CD  . ARG A  1 70  ? -6.015  -3.629  6.871   1.00 22.51 ? 70   ARG A CD  1 
ATOM   510  N  NE  . ARG A  1 70  ? -5.600  -2.900  5.681   1.00 19.70 ? 70   ARG A NE  1 
ATOM   511  C  CZ  . ARG A  1 70  ? -5.843  -3.255  4.431   1.00 20.92 ? 70   ARG A CZ  1 
ATOM   512  N  NH1 . ARG A  1 70  ? -6.631  -4.302  4.149   1.00 20.57 ? 70   ARG A NH1 1 
ATOM   513  N  NH2 . ARG A  1 70  ? -5.353  -2.484  3.470   1.00 19.44 ? 70   ARG A NH2 1 
ATOM   514  N  N   . LEU A  1 71  ? -11.024 -0.941  7.846   1.00 13.98 ? 71   LEU A N   1 
ATOM   515  C  CA  . LEU A  1 71  ? -12.343 -0.575  7.263   1.00 13.02 ? 71   LEU A CA  1 
ATOM   516  C  C   . LEU A  1 71  ? -12.992 0.637   7.931   1.00 13.72 ? 71   LEU A C   1 
ATOM   517  O  O   . LEU A  1 71  ? -14.103 1.051   7.487   1.00 12.50 ? 71   LEU A O   1 
ATOM   518  C  CB  . LEU A  1 71  ? -13.250 -1.803  7.382   1.00 12.82 ? 71   LEU A CB  1 
ATOM   519  C  CG  . LEU A  1 71  ? -12.889 -2.931  6.446   1.00 13.02 ? 71   LEU A CG  1 
ATOM   520  C  CD1 . LEU A  1 71  ? -13.730 -4.177  6.755   1.00 14.52 ? 71   LEU A CD1 1 
ATOM   521  C  CD2 . LEU A  1 71  ? -13.024 -2.525  4.985   1.00 13.74 ? 71   LEU A CD2 1 
ATOM   522  N  N   . LYS A  1 72  ? -12.371 1.216   8.955   1.00 14.24 ? 72   LYS A N   1 
ATOM   523  C  CA  . LYS A  1 72  ? -13.043 2.201   9.849   1.00 17.16 ? 72   LYS A CA  1 
ATOM   524  C  C   . LYS A  1 72  ? -13.528 3.457   9.092   1.00 15.33 ? 72   LYS A C   1 
ATOM   525  O  O   . LYS A  1 72  ? -14.466 4.063   9.588   1.00 14.81 ? 72   LYS A O   1 
ATOM   526  C  CB  . LYS A  1 72  ? -12.129 2.566   11.020  1.00 22.88 ? 72   LYS A CB  1 
ATOM   527  C  CG  . LYS A  1 72  ? -11.030 3.560   10.719  1.00 28.47 ? 72   LYS A CG  1 
ATOM   528  C  CD  . LYS A  1 72  ? -10.224 3.878   11.982  1.00 34.87 ? 72   LYS A CD  1 
ATOM   529  C  CE  . LYS A  1 72  ? -8.866  4.503   11.717  1.00 40.54 ? 72   LYS A CE  1 
ATOM   530  N  NZ  . LYS A  1 72  ? -7.876  4.099   12.749  1.00 42.85 ? 72   LYS A NZ  1 
ATOM   531  N  N   . ASN A  1 73  ? -12.904 3.833   7.979   1.00 15.79 ? 73   ASN A N   1 
ATOM   532  C  CA  . ASN A  1 73  ? -13.297 5.035   7.195   1.00 16.85 ? 73   ASN A CA  1 
ATOM   533  C  C   . ASN A  1 73  ? -14.337 4.665   6.125   1.00 18.77 ? 73   ASN A C   1 
ATOM   534  O  O   . ASN A  1 73  ? -14.855 5.597   5.438   1.00 21.85 ? 73   ASN A O   1 
ATOM   535  C  CB  . ASN A  1 73  ? -12.072 5.745   6.618   1.00 16.80 ? 73   ASN A CB  1 
ATOM   536  C  CG  . ASN A  1 73  ? -11.193 6.245   7.745   1.00 17.55 ? 73   ASN A CG  1 
ATOM   537  O  OD1 . ASN A  1 73  ? -11.687 6.710   8.767   1.00 17.36 ? 73   ASN A OD1 1 
ATOM   538  N  ND2 . ASN A  1 73  ? -9.882  6.089   7.618   1.00 19.61 ? 73   ASN A ND2 1 
ATOM   539  N  N   . THR A  1 74  ? -14.652 3.373   5.963   1.00 16.05 ? 74   THR A N   1 
ATOM   540  C  CA  . THR A  1 74  ? -15.641 2.885   4.973   1.00 14.80 ? 74   THR A CA  1 
ATOM   541  C  C   . THR A  1 74  ? -16.967 2.712   5.701   1.00 14.02 ? 74   THR A C   1 
ATOM   542  O  O   . THR A  1 74  ? -16.998 2.904   6.935   1.00 13.99 ? 74   THR A O   1 
ATOM   543  C  CB  . THR A  1 74  ? -15.233 1.549   4.309   1.00 14.21 ? 74   THR A CB  1 
ATOM   544  O  OG1 . THR A  1 74  ? -15.471 0.518   5.268   1.00 13.76 ? 74   THR A OG1 1 
ATOM   545  C  CG2 . THR A  1 74  ? -13.793 1.554   3.818   1.00 15.67 ? 74   THR A CG2 1 
ATOM   546  N  N   . THR A  1 75  ? -18.020 2.322   4.990   1.00 12.45 ? 75   THR A N   1 
ATOM   547  C  CA  . THR A  1 75  ? -19.318 1.965   5.618   1.00 13.76 ? 75   THR A CA  1 
ATOM   548  C  C   . THR A  1 75  ? -19.268 0.548   6.244   1.00 13.26 ? 75   THR A C   1 
ATOM   549  O  O   . THR A  1 75  ? -20.261 0.138   6.868   1.00 13.44 ? 75   THR A O   1 
ATOM   550  C  CB  . THR A  1 75  ? -20.438 2.096   4.583   1.00 14.92 ? 75   THR A CB  1 
ATOM   551  O  OG1 . THR A  1 75  ? -20.085 1.301   3.452   1.00 14.03 ? 75   THR A OG1 1 
ATOM   552  C  CG2 . THR A  1 75  ? -20.609 3.531   4.147   1.00 16.99 ? 75   THR A CG2 1 
ATOM   553  N  N   . GLY A  1 76  ? -18.169 -0.182  6.053   1.00 12.62 ? 76   GLY A N   1 
ATOM   554  C  CA  . GLY A  1 76  ? -18.118 -1.623  6.350   1.00 12.81 ? 76   GLY A CA  1 
ATOM   555  C  C   . GLY A  1 76  ? -18.024 -1.920  7.843   1.00 13.40 ? 76   GLY A C   1 
ATOM   556  O  O   . GLY A  1 76  ? -17.263 -1.200  8.560   1.00 13.94 ? 76   GLY A O   1 
ATOM   557  N  N   . LYS A  1 77  ? -18.667 -3.012  8.260   1.00 12.09 ? 77   LYS A N   1 
ATOM   558  C  CA  . LYS A  1 77  ? -18.653 -3.542  9.633   1.00 12.17 ? 77   LYS A CA  1 
ATOM   559  C  C   . LYS A  1 77  ? -18.168 -4.986  9.558   1.00 12.15 ? 77   LYS A C   1 
ATOM   560  O  O   . LYS A  1 77  ? -18.248 -5.595  8.452   1.00 12.34 ? 77   LYS A O   1 
ATOM   561  C  CB  . LYS A  1 77  ? -20.050 -3.474  10.238  1.00 14.63 ? 77   LYS A CB  1 
ATOM   562  C  CG  . LYS A  1 77  ? -20.590 -2.078  10.503  1.00 16.75 ? 77   LYS A CG  1 
ATOM   563  C  CD  . LYS A  1 77  ? -21.951 -2.142  11.135  1.00 21.55 ? 77   LYS A CD  1 
ATOM   564  C  CE  . LYS A  1 77  ? -22.585 -0.794  11.397  1.00 26.64 ? 77   LYS A CE  1 
ATOM   565  N  NZ  . LYS A  1 77  ? -22.701 -0.045  10.129  1.00 31.51 ? 77   LYS A NZ  1 
ATOM   566  N  N   . VAL A  1 78  ? -17.654 -5.477  10.673  1.00 11.59 ? 78   VAL A N   1 
ATOM   567  C  CA  . VAL A  1 78  ? -17.027 -6.817  10.736  1.00 10.97 ? 78   VAL A CA  1 
ATOM   568  C  C   . VAL A  1 78  ? -17.797 -7.690  11.719  1.00 11.47 ? 78   VAL A C   1 
ATOM   569  O  O   . VAL A  1 78  ? -17.907 -7.343  12.902  1.00 11.11 ? 78   VAL A O   1 
ATOM   570  C  CB  . VAL A  1 78  ? -15.529 -6.731  11.049  1.00 10.69 ? 78   VAL A CB  1 
ATOM   571  C  CG1 . VAL A  1 78  ? -14.964 -8.139  11.149  1.00 9.75  ? 78   VAL A CG1 1 
ATOM   572  C  CG2 . VAL A  1 78  ? -14.788 -5.950  9.991   1.00 11.18 ? 78   VAL A CG2 1 
ATOM   573  N  N   . MET A  1 79  ? -18.258 -8.846  11.223  1.00 11.26 ? 79   MET A N   1 
ATOM   574  C  CA  . MET A  1 79  ? -18.804 -9.940  12.058  1.00 11.03 ? 79   MET A CA  1 
ATOM   575  C  C   . MET A  1 79  ? -17.644 -10.843 12.479  1.00 10.33 ? 79   MET A C   1 
ATOM   576  O  O   . MET A  1 79  ? -16.854 -11.231 11.604  1.00 10.83 ? 79   MET A O   1 
ATOM   577  C  CB  . MET A  1 79  ? -19.825 -10.770 11.298  1.00 11.62 ? 79   MET A CB  1 
ATOM   578  C  CG  . MET A  1 79  ? -20.595 -11.666 12.245  1.00 12.68 ? 79   MET A CG  1 
ATOM   579  S  SD  . MET A  1 79  ? -21.533 -12.966 11.447  1.00 14.13 ? 79   MET A SD  1 
ATOM   580  C  CE  . MET A  1 79  ? -22.451 -12.004 10.239  1.00 14.23 ? 79   MET A CE  1 
ATOM   581  N  N   . ILE A  1 80  ? -17.545 -11.143 13.776  1.00 10.78 ? 80   ILE A N   1 
ATOM   582  C  CA  . ILE A  1 80  ? -16.446 -11.971 14.325  1.00 10.39 ? 80   ILE A CA  1 
ATOM   583  C  C   . ILE A  1 80  ? -16.846 -13.444 14.287  1.00 10.87 ? 80   ILE A C   1 
ATOM   584  O  O   . ILE A  1 80  ? -17.782 -13.836 14.996  1.00 11.99 ? 80   ILE A O   1 
ATOM   585  C  CB  . ILE A  1 80  ? -16.048 -11.459 15.726  1.00 10.95 ? 80   ILE A CB  1 
ATOM   586  C  CG1 . ILE A  1 80  ? -15.527 -10.028 15.636  1.00 12.20 ? 80   ILE A CG1 1 
ATOM   587  C  CG2 . ILE A  1 80  ? -15.013 -12.373 16.328  1.00 11.37 ? 80   ILE A CG2 1 
ATOM   588  C  CD1 . ILE A  1 80  ? -15.455 -9.367  16.972  1.00 13.62 ? 80   ILE A CD1 1 
ATOM   589  N  N   . ARG A  1 81  ? -16.150 -14.237 13.468  1.00 10.68 ? 81   ARG A N   1 
ATOM   590  C  CA  . ARG A  1 81  ? -16.336 -15.714 13.418  1.00 10.58 ? 81   ARG A CA  1 
ATOM   591  C  C   . ARG A  1 81  ? -15.472 -16.354 14.512  1.00 10.72 ? 81   ARG A C   1 
ATOM   592  O  O   . ARG A  1 81  ? -14.240 -16.547 14.310  1.00 9.76  ? 81   ARG A O   1 
ATOM   593  C  CB  . ARG A  1 81  ? -16.043 -16.248 12.023  1.00 10.52 ? 81   ARG A CB  1 
ATOM   594  C  CG  . ARG A  1 81  ? -15.941 -17.760 11.940  1.00 9.82  ? 81   ARG A CG  1 
ATOM   595  C  CD  . ARG A  1 81  ? -16.098 -18.225 10.491  1.00 10.13 ? 81   ARG A CD  1 
ATOM   596  N  NE  . ARG A  1 81  ? -17.501 -18.053 10.062  1.00 10.51 ? 81   ARG A NE  1 
ATOM   597  C  CZ  . ARG A  1 81  ? -17.953 -18.330 8.854   1.00 11.29 ? 81   ARG A CZ  1 
ATOM   598  N  NH1 . ARG A  1 81  ? -19.230 -18.133 8.569   1.00 11.17 ? 81   ARG A NH1 1 
ATOM   599  N  NH2 . ARG A  1 81  ? -17.137 -18.820 7.939   1.00 11.51 ? 81   ARG A NH2 1 
ATOM   600  N  N   . LEU A  1 82  ? -16.093 -16.622 15.659  1.00 10.51 ? 82   LEU A N   1 
ATOM   601  C  CA  . LEU A  1 82  ? -15.383 -17.170 16.850  1.00 11.00 ? 82   LEU A CA  1 
ATOM   602  C  C   . LEU A  1 82  ? -14.880 -18.596 16.560  1.00 11.37 ? 82   LEU A C   1 
ATOM   603  O  O   . LEU A  1 82  ? -13.815 -18.966 17.088  1.00 11.47 ? 82   LEU A O   1 
ATOM   604  C  CB  . LEU A  1 82  ? -16.315 -17.102 18.059  1.00 10.69 ? 82   LEU A CB  1 
ATOM   605  C  CG  . LEU A  1 82  ? -16.542 -15.708 18.641  1.00 11.42 ? 82   LEU A CG  1 
ATOM   606  C  CD1 . LEU A  1 82  ? -17.568 -15.728 19.755  1.00 12.30 ? 82   LEU A CD1 1 
ATOM   607  C  CD2 . LEU A  1 82  ? -15.249 -15.133 19.188  1.00 12.04 ? 82   LEU A CD2 1 
ATOM   608  N  N   . ALA A  1 83  ? -15.580 -19.395 15.741  1.00 11.51 ? 83   ALA A N   1 
ATOM   609  C  CA  . ALA A  1 83  ? -15.167 -20.809 15.532  1.00 11.20 ? 83   ALA A CA  1 
ATOM   610  C  C   . ALA A  1 83  ? -13.731 -20.863 14.975  1.00 11.79 ? 83   ALA A C   1 
ATOM   611  O  O   . ALA A  1 83  ? -13.029 -21.870 15.209  1.00 11.09 ? 83   ALA A O   1 
ATOM   612  C  CB  . ALA A  1 83  ? -16.130 -21.559 14.644  1.00 10.88 ? 83   ALA A CB  1 
ATOM   613  N  N   . ASP A  1 84  ? -13.308 -19.848 14.192  1.00 11.66 ? 84   ASP A N   1 
ATOM   614  C  CA  . ASP A  1 84  ? -11.996 -19.818 13.504  1.00 11.52 ? 84   ASP A CA  1 
ATOM   615  C  C   . ASP A  1 84  ? -10.849 -19.642 14.518  1.00 11.23 ? 84   ASP A C   1 
ATOM   616  O  O   . ASP A  1 84  ? -9.664  -19.737 14.103  1.00 11.02 ? 84   ASP A O   1 
ATOM   617  C  CB  . ASP A  1 84  ? -12.017 -18.818 12.352  1.00 11.64 ? 84   ASP A CB  1 
ATOM   618  C  CG  . ASP A  1 84  ? -12.701 -19.325 11.090  1.00 11.91 ? 84   ASP A CG  1 
ATOM   619  O  OD1 . ASP A  1 84  ? -13.263 -20.434 11.119  1.00 12.58 ? 84   ASP A OD1 1 
ATOM   620  O  OD2 . ASP A  1 84  ? -12.669 -18.594 10.069  1.00 12.79 ? 84   ASP A OD2 1 
ATOM   621  N  N   . ILE A  1 85  ? -11.160 -19.506 15.806  1.00 11.56 ? 85   ILE A N   1 
ATOM   622  C  CA  . ILE A  1 85  ? -10.142 -19.698 16.870  1.00 12.78 ? 85   ILE A CA  1 
ATOM   623  C  C   . ILE A  1 85  ? -9.472  -21.056 16.660  1.00 13.14 ? 85   ILE A C   1 
ATOM   624  O  O   . ILE A  1 85  ? -8.237  -21.192 16.907  1.00 12.52 ? 85   ILE A O   1 
ATOM   625  C  CB  . ILE A  1 85  ? -10.801 -19.563 18.248  1.00 13.89 ? 85   ILE A CB  1 
ATOM   626  C  CG1 . ILE A  1 85  ? -11.161 -18.114 18.583  1.00 13.65 ? 85   ILE A CG1 1 
ATOM   627  C  CG2 . ILE A  1 85  ? -9.941  -20.192 19.320  1.00 14.96 ? 85   ILE A CG2 1 
ATOM   628  C  CD1 . ILE A  1 85  ? -12.152 -17.979 19.729  1.00 14.58 ? 85   ILE A CD1 1 
ATOM   629  N  N   . PHE A  1 86  ? -10.234 -22.061 16.258  1.00 12.59 ? 86   PHE A N   1 
ATOM   630  C  CA  . PHE A  1 86  ? -9.687  -23.433 16.115  1.00 13.21 ? 86   PHE A CA  1 
ATOM   631  C  C   . PHE A  1 86  ? -9.206  -23.739 14.707  1.00 13.96 ? 86   PHE A C   1 
ATOM   632  O  O   . PHE A  1 86  ? -9.847  -23.415 13.713  1.00 13.52 ? 86   PHE A O   1 
ATOM   633  C  CB  . PHE A  1 86  ? -10.728 -24.481 16.510  1.00 13.19 ? 86   PHE A CB  1 
ATOM   634  C  CG  . PHE A  1 86  ? -11.099 -24.428 17.975  1.00 13.37 ? 86   PHE A CG  1 
ATOM   635  C  CD1 . PHE A  1 86  ? -10.144 -24.687 18.940  1.00 13.92 ? 86   PHE A CD1 1 
ATOM   636  C  CD2 . PHE A  1 86  ? -12.378 -24.121 18.380  1.00 13.15 ? 86   PHE A CD2 1 
ATOM   637  C  CE1 . PHE A  1 86  ? -10.475 -24.687 20.285  1.00 14.50 ? 86   PHE A CE1 1 
ATOM   638  C  CE2 . PHE A  1 86  ? -12.707 -24.124 19.724  1.00 13.34 ? 86   PHE A CE2 1 
ATOM   639  C  CZ  . PHE A  1 86  ? -11.772 -24.426 20.669  1.00 14.12 ? 86   PHE A CZ  1 
ATOM   640  N  N   . PRO A  1 87  ? -8.102  -24.513 14.601  1.00 15.05 ? 87   PRO A N   1 
ATOM   641  C  CA  . PRO A  1 87  ? -7.667  -25.053 13.327  1.00 14.88 ? 87   PRO A CA  1 
ATOM   642  C  C   . PRO A  1 87  ? -8.438  -26.326 12.923  1.00 15.97 ? 87   PRO A C   1 
ATOM   643  O  O   . PRO A  1 87  ? -9.167  -26.885 13.739  1.00 15.26 ? 87   PRO A O   1 
ATOM   644  C  CB  . PRO A  1 87  ? -6.191  -25.405 13.631  1.00 16.69 ? 87   PRO A CB  1 
ATOM   645  C  CG  . PRO A  1 87  ? -6.227  -25.851 15.081  1.00 17.46 ? 87   PRO A CG  1 
ATOM   646  C  CD  . PRO A  1 87  ? -7.283  -24.983 15.733  1.00 16.22 ? 87   PRO A CD  1 
ATOM   647  N  N   . ARG A  1 88  ? -8.256  -26.703 11.656  1.00 17.65 ? 88   ARG A N   1 
ATOM   648  C  CA  . ARG A  1 88  ? -8.680  -27.979 11.015  1.00 20.28 ? 88   ARG A CA  1 
ATOM   649  C  C   . ARG A  1 88  ? -10.157 -27.942 10.628  1.00 19.73 ? 88   ARG A C   1 
ATOM   650  O  O   . ARG A  1 88  ? -10.867 -27.051 11.081  1.00 17.28 ? 88   ARG A O   1 
ATOM   651  C  CB  . ARG A  1 88  ? -8.366  -29.152 11.932  1.00 22.10 ? 88   ARG A CB  1 
ATOM   652  C  CG  . ARG A  1 88  ? -6.866  -29.315 12.140  1.00 27.18 ? 88   ARG A CG  1 
ATOM   653  C  CD  . ARG A  1 88  ? -6.552  -30.719 12.588  1.00 29.77 ? 88   ARG A CD  1 
ATOM   654  N  NE  . ARG A  1 88  ? -7.135  -30.947 13.899  1.00 31.80 ? 88   ARG A NE  1 
ATOM   655  C  CZ  . ARG A  1 88  ? -6.615  -30.532 15.052  1.00 39.00 ? 88   ARG A CZ  1 
ATOM   656  N  NH1 . ARG A  1 88  ? -7.252  -30.787 16.185  1.00 40.93 ? 88   ARG A NH1 1 
ATOM   657  N  NH2 . ARG A  1 88  ? -5.481  -29.847 15.082  1.00 37.71 ? 88   ARG A NH2 1 
ATOM   658  N  N   . TRP A  1 89  ? -10.558 -28.860 9.735   1.00 20.30 ? 89   TRP A N   1 
ATOM   659  C  CA  . TRP A  1 89  ? -11.944 -28.952 9.212   1.00 20.61 ? 89   TRP A CA  1 
ATOM   660  C  C   . TRP A  1 89  ? -12.421 -30.391 9.292   1.00 23.59 ? 89   TRP A C   1 
ATOM   661  O  O   . TRP A  1 89  ? -11.756 -31.265 8.748   1.00 25.74 ? 89   TRP A O   1 
ATOM   662  C  CB  . TRP A  1 89  ? -12.040 -28.410 7.787   1.00 22.67 ? 89   TRP A CB  1 
ATOM   663  C  CG  . TRP A  1 89  ? -13.461 -28.151 7.409   1.00 23.67 ? 89   TRP A CG  1 
ATOM   664  C  CD1 . TRP A  1 89  ? -14.294 -28.999 6.741   1.00 23.80 ? 89   TRP A CD1 1 
ATOM   665  C  CD2 . TRP A  1 89  ? -14.246 -27.006 7.769   1.00 20.92 ? 89   TRP A CD2 1 
ATOM   666  N  NE1 . TRP A  1 89  ? -15.542 -28.447 6.644   1.00 24.28 ? 89   TRP A NE1 1 
ATOM   667  C  CE2 . TRP A  1 89  ? -15.536 -27.209 7.244   1.00 22.11 ? 89   TRP A CE2 1 
ATOM   668  C  CE3 . TRP A  1 89  ? -13.998 -25.843 8.497   1.00 19.90 ? 89   TRP A CE3 1 
ATOM   669  C  CZ2 . TRP A  1 89  ? -16.561 -26.287 7.412   1.00 20.75 ? 89   TRP A CZ2 1 
ATOM   670  C  CZ3 . TRP A  1 89  ? -15.000 -24.922 8.640   1.00 20.33 ? 89   TRP A CZ3 1 
ATOM   671  C  CH2 . TRP A  1 89  ? -16.266 -25.131 8.100   1.00 20.18 ? 89   TRP A CH2 1 
ATOM   672  N  N   . PRO A  1 90  ? -13.501 -30.695 10.046  1.00 23.33 ? 90   PRO A N   1 
ATOM   673  C  CA  . PRO A  1 90  ? -14.164 -29.735 10.930  1.00 20.52 ? 90   PRO A CA  1 
ATOM   674  C  C   . PRO A  1 90  ? -13.270 -29.244 12.085  1.00 18.71 ? 90   PRO A C   1 
ATOM   675  O  O   . PRO A  1 90  ? -12.250 -29.836 12.409  1.00 17.12 ? 90   PRO A O   1 
ATOM   676  C  CB  . PRO A  1 90  ? -15.356 -30.539 11.505  1.00 21.35 ? 90   PRO A CB  1 
ATOM   677  C  CG  . PRO A  1 90  ? -14.858 -31.966 11.470  1.00 24.30 ? 90   PRO A CG  1 
ATOM   678  C  CD  . PRO A  1 90  ? -14.123 -32.033 10.139  1.00 24.81 ? 90   PRO A CD  1 
ATOM   679  N  N   . TYR A  1 91  ? -13.683 -28.140 12.685  1.00 16.26 ? 91   TYR A N   1 
ATOM   680  C  CA  . TYR A  1 91  ? -12.907 -27.442 13.737  1.00 15.66 ? 91   TYR A CA  1 
ATOM   681  C  C   . TYR A  1 91  ? -12.406 -28.430 14.788  1.00 15.53 ? 91   TYR A C   1 
ATOM   682  O  O   . TYR A  1 91  ? -13.218 -29.242 15.318  1.00 16.30 ? 91   TYR A O   1 
ATOM   683  C  CB  . TYR A  1 91  ? -13.805 -26.402 14.402  1.00 15.14 ? 91   TYR A CB  1 
ATOM   684  C  CG  . TYR A  1 91  ? -14.189 -25.308 13.441  1.00 13.32 ? 91   TYR A CG  1 
ATOM   685  C  CD1 . TYR A  1 91  ? -13.257 -24.346 13.073  1.00 12.97 ? 91   TYR A CD1 1 
ATOM   686  C  CD2 . TYR A  1 91  ? -15.476 -25.214 12.930  1.00 13.29 ? 91   TYR A CD2 1 
ATOM   687  C  CE1 . TYR A  1 91  ? -13.609 -23.309 12.229  1.00 12.97 ? 91   TYR A CE1 1 
ATOM   688  C  CE2 . TYR A  1 91  ? -15.832 -24.199 12.047  1.00 13.18 ? 91   TYR A CE2 1 
ATOM   689  C  CZ  . TYR A  1 91  ? -14.897 -23.230 11.718  1.00 12.86 ? 91   TYR A CZ  1 
ATOM   690  O  OH  . TYR A  1 91  ? -15.207 -22.209 10.860  1.00 13.33 ? 91   TYR A OH  1 
ATOM   691  N  N   . GLY A  1 92  ? -11.133 -28.321 15.143  1.00 16.09 ? 92   GLY A N   1 
ATOM   692  C  CA  . GLY A  1 92  ? -10.518 -29.048 16.269  1.00 17.73 ? 92   GLY A CA  1 
ATOM   693  C  C   . GLY A  1 92  ? -10.936 -28.475 17.610  1.00 18.43 ? 92   GLY A C   1 
ATOM   694  O  O   . GLY A  1 92  ? -10.064 -28.077 18.387  1.00 18.24 ? 92   GLY A O   1 
ATOM   695  N  N   . PHE A  1 93  ? -12.231 -28.489 17.917  1.00 18.50 ? 93   PHE A N   1 
ATOM   696  C  CA  . PHE A  1 93  ? -12.752 -28.063 19.233  1.00 18.35 ? 93   PHE A CA  1 
ATOM   697  C  C   . PHE A  1 93  ? -12.034 -28.859 20.311  1.00 20.04 ? 93   PHE A C   1 
ATOM   698  O  O   . PHE A  1 93  ? -11.925 -30.092 20.144  1.00 18.59 ? 93   PHE A O   1 
ATOM   699  C  CB  . PHE A  1 93  ? -14.256 -28.269 19.323  1.00 17.96 ? 93   PHE A CB  1 
ATOM   700  C  CG  . PHE A  1 93  ? -14.847 -27.804 20.624  1.00 18.99 ? 93   PHE A CG  1 
ATOM   701  C  CD1 . PHE A  1 93  ? -15.230 -26.482 20.797  1.00 19.26 ? 93   PHE A CD1 1 
ATOM   702  C  CD2 . PHE A  1 93  ? -15.054 -28.695 21.663  1.00 19.88 ? 93   PHE A CD2 1 
ATOM   703  C  CE1 . PHE A  1 93  ? -15.758 -26.050 21.998  1.00 19.34 ? 93   PHE A CE1 1 
ATOM   704  C  CE2 . PHE A  1 93  ? -15.585 -28.259 22.865  1.00 20.39 ? 93   PHE A CE2 1 
ATOM   705  C  CZ  . PHE A  1 93  ? -15.947 -26.941 23.026  1.00 19.81 ? 93   PHE A CZ  1 
ATOM   706  N  N   . THR A  1 94  ? -11.568 -28.170 21.350  1.00 19.02 ? 94   THR A N   1 
ATOM   707  C  CA  . THR A  1 94  ? -10.828 -28.749 22.490  1.00 18.77 ? 94   THR A CA  1 
ATOM   708  C  C   . THR A  1 94  ? -11.818 -29.087 23.605  1.00 18.26 ? 94   THR A C   1 
ATOM   709  O  O   . THR A  1 94  ? -12.349 -30.234 23.655  1.00 18.47 ? 94   THR A O   1 
ATOM   710  C  CB  . THR A  1 94  ? -9.720  -27.775 22.893  1.00 19.81 ? 94   THR A CB  1 
ATOM   711  O  OG1 . THR A  1 94  ? -10.309 -26.489 23.086  1.00 19.45 ? 94   THR A OG1 1 
ATOM   712  C  CG2 . THR A  1 94  ? -8.652  -27.693 21.837  1.00 21.10 ? 94   THR A CG2 1 
ATOM   713  N  N   . ASN A  1 95  ? -12.133 -28.117 24.445  1.00 15.46 ? 95   ASN A N   1 
ATOM   714  C  CA  . ASN A  1 95  ? -13.078 -28.294 25.562  1.00 16.16 ? 95   ASN A CA  1 
ATOM   715  C  C   . ASN A  1 95  ? -13.669 -26.925 25.936  1.00 15.80 ? 95   ASN A C   1 
ATOM   716  O  O   . ASN A  1 95  ? -13.145 -25.872 25.480  1.00 16.29 ? 95   ASN A O   1 
ATOM   717  C  CB  . ASN A  1 95  ? -12.369 -28.982 26.731  1.00 16.16 ? 95   ASN A CB  1 
ATOM   718  C  CG  . ASN A  1 95  ? -11.193 -28.178 27.232  1.00 16.47 ? 95   ASN A CG  1 
ATOM   719  O  OD1 . ASN A  1 95  ? -11.371 -27.073 27.729  1.00 17.48 ? 95   ASN A OD1 1 
ATOM   720  N  ND2 . ASN A  1 95  ? -9.994  -28.732 27.129  1.00 18.08 ? 95   ASN A ND2 1 
ATOM   721  N  N   . MET A  1 96  ? -14.745 -26.925 26.696  1.00 16.47 ? 96   MET A N   1 
ATOM   722  C  CA  . MET A  1 96  ? -15.447 -25.655 27.030  1.00 17.04 ? 96   MET A CA  1 
ATOM   723  C  C   . MET A  1 96  ? -14.530 -24.711 27.824  1.00 17.36 ? 96   MET A C   1 
ATOM   724  O  O   . MET A  1 96  ? -14.625 -23.471 27.627  1.00 16.33 ? 96   MET A O   1 
ATOM   725  C  CB  . MET A  1 96  ? -16.754 -25.913 27.782  1.00 17.15 ? 96   MET A CB  1 
ATOM   726  C  CG  . MET A  1 96  ? -17.856 -26.498 26.907  1.00 19.16 ? 96   MET A CG  1 
ATOM   727  S  SD  . MET A  1 96  ? -18.309 -25.375 25.524  1.00 18.40 ? 96   MET A SD  1 
ATOM   728  C  CE  . MET A  1 96  ? -18.962 -23.954 26.401  1.00 18.05 ? 96   MET A CE  1 
ATOM   729  N  N   . ASN A  1 97  ? -13.653 -25.218 28.696  1.00 18.56 ? 97   ASN A N   1 
ATOM   730  C  CA  . ASN A  1 97  ? -12.745 -24.326 29.468  1.00 18.61 ? 97   ASN A CA  1 
ATOM   731  C  C   . ASN A  1 97  ? -11.836 -23.584 28.487  1.00 16.96 ? 97   ASN A C   1 
ATOM   732  O  O   . ASN A  1 97  ? -11.712 -22.325 28.588  1.00 17.59 ? 97   ASN A O   1 
ATOM   733  C  CB  . ASN A  1 97  ? -11.901 -25.089 30.486  1.00 19.41 ? 97   ASN A CB  1 
ATOM   734  C  CG  . ASN A  1 97  ? -12.760 -25.641 31.602  1.00 24.09 ? 97   ASN A CG  1 
ATOM   735  O  OD1 . ASN A  1 97  ? -13.695 -24.986 32.043  1.00 25.07 ? 97   ASN A OD1 1 
ATOM   736  N  ND2 . ASN A  1 97  ? -12.477 -26.851 32.054  1.00 20.54 ? 97   ASN A ND2 1 
ATOM   737  N  N   . ASP A  1 98  ? -11.229 -24.321 27.574  1.00 16.27 ? 98   ASP A N   1 
ATOM   738  C  CA  . ASP A  1 98  ? -10.251 -23.764 26.601  1.00 17.50 ? 98   ASP A CA  1 
ATOM   739  C  C   . ASP A  1 98  ? -10.981 -22.733 25.721  1.00 16.47 ? 98   ASP A C   1 
ATOM   740  O  O   . ASP A  1 98  ? -10.516 -21.595 25.582  1.00 14.55 ? 98   ASP A O   1 
ATOM   741  C  CB  . ASP A  1 98  ? -9.618  -24.884 25.788  1.00 18.70 ? 98   ASP A CB  1 
ATOM   742  C  CG  . ASP A  1 98  ? -8.516  -24.385 24.886  1.00 20.95 ? 98   ASP A CG  1 
ATOM   743  O  OD1 . ASP A  1 98  ? -7.667  -23.622 25.392  1.00 23.28 ? 98   ASP A OD1 1 
ATOM   744  O  OD2 . ASP A  1 98  ? -8.538  -24.715 23.686  1.00 21.36 ? 98   ASP A OD2 1 
ATOM   745  N  N   . TRP A  1 99  ? -12.118 -23.137 25.155  1.00 15.92 ? 99   TRP A N   1 
ATOM   746  C  CA  . TRP A  1 99  ? -12.954 -22.294 24.258  1.00 14.48 ? 99   TRP A CA  1 
ATOM   747  C  C   . TRP A  1 99  ? -13.338 -20.982 24.947  1.00 15.48 ? 99   TRP A C   1 
ATOM   748  O  O   . TRP A  1 99  ? -13.146 -19.932 24.355  1.00 15.81 ? 99   TRP A O   1 
ATOM   749  C  CB  . TRP A  1 99  ? -14.169 -23.108 23.861  1.00 14.34 ? 99   TRP A CB  1 
ATOM   750  C  CG  . TRP A  1 99  ? -15.288 -22.366 23.215  1.00 14.30 ? 99   TRP A CG  1 
ATOM   751  C  CD1 . TRP A  1 99  ? -16.553 -22.235 23.695  1.00 15.21 ? 99   TRP A CD1 1 
ATOM   752  C  CD2 . TRP A  1 99  ? -15.285 -21.745 21.916  1.00 14.13 ? 99   TRP A CD2 1 
ATOM   753  N  NE1 . TRP A  1 99  ? -17.322 -21.543 22.804  1.00 14.73 ? 99   TRP A NE1 1 
ATOM   754  C  CE2 . TRP A  1 99  ? -16.585 -21.267 21.694  1.00 13.76 ? 99   TRP A CE2 1 
ATOM   755  C  CE3 . TRP A  1 99  ? -14.326 -21.548 20.923  1.00 14.98 ? 99   TRP A CE3 1 
ATOM   756  C  CZ2 . TRP A  1 99  ? -16.945 -20.610 20.518  1.00 13.71 ? 99   TRP A CZ2 1 
ATOM   757  C  CZ3 . TRP A  1 99  ? -14.672 -20.907 19.755  1.00 14.00 ? 99   TRP A CZ3 1 
ATOM   758  C  CH2 . TRP A  1 99  ? -15.981 -20.459 19.557  1.00 13.99 ? 99   TRP A CH2 1 
ATOM   759  N  N   . LEU A  1 100 ? -13.946 -21.053 26.126  1.00 15.12 ? 100  LEU A N   1 
ATOM   760  C  CA  . LEU A  1 100 ? -14.457 -19.845 26.813  1.00 14.91 ? 100  LEU A CA  1 
ATOM   761  C  C   . LEU A  1 100 ? -13.282 -18.926 27.169  1.00 14.40 ? 100  LEU A C   1 
ATOM   762  O  O   . LEU A  1 100 ? -13.446 -17.704 27.100  1.00 14.90 ? 100  LEU A O   1 
ATOM   763  C  CB  . LEU A  1 100 ? -15.263 -20.244 28.042  1.00 15.55 ? 100  LEU A CB  1 
ATOM   764  C  CG  . LEU A  1 100 ? -16.564 -20.971 27.729  1.00 15.85 ? 100  LEU A CG  1 
ATOM   765  C  CD1 . LEU A  1 100 ? -17.235 -21.452 29.004  1.00 16.79 ? 100  LEU A CD1 1 
ATOM   766  C  CD2 . LEU A  1 100 ? -17.518 -20.096 26.933  1.00 16.92 ? 100  LEU A CD2 1 
ATOM   767  N  N   . GLY A  1 101 ? -12.110 -19.480 27.479  1.00 15.59 ? 101  GLY A N   1 
ATOM   768  C  CA  . GLY A  1 101 ? -10.940 -18.632 27.752  1.00 15.14 ? 101  GLY A CA  1 
ATOM   769  C  C   . GLY A  1 101 ? -10.541 -17.886 26.489  1.00 15.99 ? 101  GLY A C   1 
ATOM   770  O  O   . GLY A  1 101 ? -10.266 -16.693 26.564  1.00 13.92 ? 101  GLY A O   1 
ATOM   771  N  N   . LYS A  1 102 ? -10.536 -18.583 25.346  1.00 14.08 ? 102  LYS A N   1 
ATOM   772  C  CA  . LYS A  1 102 ? -10.131 -17.971 24.065  1.00 15.02 ? 102  LYS A CA  1 
ATOM   773  C  C   . LYS A  1 102 ? -11.175 -16.926 23.661  1.00 13.26 ? 102  LYS A C   1 
ATOM   774  O  O   . LYS A  1 102 ? -10.799 -15.887 23.186  1.00 13.51 ? 102  LYS A O   1 
ATOM   775  C  CB  . LYS A  1 102 ? -9.879  -19.073 23.038  1.00 16.15 ? 102  LYS A CB  1 
ATOM   776  C  CG  . LYS A  1 102 ? -8.606  -19.864 23.331  1.00 17.60 ? 102  LYS A CG  1 
ATOM   777  C  CD  . LYS A  1 102 ? -8.431  -21.108 22.497  1.00 20.59 ? 102  LYS A CD  1 
ATOM   778  C  CE  . LYS A  1 102 ? -7.054  -21.717 22.701  1.00 22.78 ? 102  LYS A CE  1 
ATOM   779  N  NZ  . LYS A  1 102 ? -6.939  -23.019 22.004  1.00 26.53 ? 102  LYS A NZ  1 
ATOM   780  N  N   . VAL A  1 103 ? -12.455 -17.213 23.850  1.00 14.52 ? 103  VAL A N   1 
ATOM   781  C  CA  . VAL A  1 103 ? -13.530 -16.262 23.482  1.00 14.05 ? 103  VAL A CA  1 
ATOM   782  C  C   . VAL A  1 103 ? -13.378 -15.025 24.366  1.00 14.10 ? 103  VAL A C   1 
ATOM   783  O  O   . VAL A  1 103 ? -13.486 -13.914 23.837  1.00 13.19 ? 103  VAL A O   1 
ATOM   784  C  CB  . VAL A  1 103 ? -14.925 -16.900 23.590  1.00 13.33 ? 103  VAL A CB  1 
ATOM   785  C  CG1 . VAL A  1 103 ? -16.032 -15.864 23.394  1.00 13.53 ? 103  VAL A CG1 1 
ATOM   786  C  CG2 . VAL A  1 103 ? -15.057 -18.058 22.616  1.00 13.74 ? 103  VAL A CG2 1 
ATOM   787  N  N   . THR A  1 104 ? -13.129 -15.217 25.670  1.00 15.18 ? 104  THR A N   1 
ATOM   788  C  CA  . THR A  1 104 ? -12.874 -14.108 26.622  1.00 14.98 ? 104  THR A CA  1 
ATOM   789  C  C   . THR A  1 104 ? -11.765 -13.226 26.058  1.00 13.83 ? 104  THR A C   1 
ATOM   790  O  O   . THR A  1 104 ? -11.928 -11.990 25.990  1.00 14.12 ? 104  THR A O   1 
ATOM   791  C  CB  . THR A  1 104 ? -12.562 -14.617 28.037  1.00 15.29 ? 104  THR A CB  1 
ATOM   792  O  OG1 . THR A  1 104 ? -13.677 -15.351 28.530  1.00 16.20 ? 104  THR A OG1 1 
ATOM   793  C  CG2 . THR A  1 104 ? -12.271 -13.498 29.008  1.00 17.04 ? 104  THR A CG2 1 
ATOM   794  N  N   A SER A  1 105 ? -10.654 -13.822 25.633  0.60 13.96 ? 105  SER A N   1 
ATOM   795  N  N   B SER A  1 105 ? -10.649 -13.817 25.621  0.40 13.58 ? 105  SER A N   1 
ATOM   796  C  CA  A SER A  1 105 ? -9.498  -13.062 25.094  0.60 14.04 ? 105  SER A CA  1 
ATOM   797  C  CA  B SER A  1 105 ? -9.474  -13.059 25.111  0.40 13.38 ? 105  SER A CA  1 
ATOM   798  C  C   A SER A  1 105 ? -9.954  -12.228 23.889  0.60 13.07 ? 105  SER A C   1 
ATOM   799  C  C   B SER A  1 105 ? -9.862  -12.271 23.848  0.40 13.04 ? 105  SER A C   1 
ATOM   800  O  O   A SER A  1 105 ? -9.669  -11.011 23.814  0.60 12.56 ? 105  SER A O   1 
ATOM   801  O  O   B SER A  1 105 ? -9.404  -11.117 23.687  0.40 13.25 ? 105  SER A O   1 
ATOM   802  C  CB  A SER A  1 105 ? -8.382  -13.978 24.719  0.60 15.34 ? 105  SER A CB  1 
ATOM   803  C  CB  B SER A  1 105 ? -8.297  -13.964 24.865  0.40 13.75 ? 105  SER A CB  1 
ATOM   804  O  OG  A SER A  1 105 ? -7.220  -13.234 24.436  0.60 16.15 ? 105  SER A OG  1 
ATOM   805  O  OG  B SER A  1 105 ? -7.904  -14.625 26.063  0.40 12.99 ? 105  SER A OG  1 
ATOM   806  N  N   . VAL A  1 106 ? -10.693 -12.856 22.987  1.00 13.28 ? 106  VAL A N   1 
ATOM   807  C  CA  . VAL A  1 106 ? -11.189 -12.153 21.776  1.00 13.49 ? 106  VAL A CA  1 
ATOM   808  C  C   . VAL A  1 106 ? -12.050 -10.955 22.189  1.00 12.26 ? 106  VAL A C   1 
ATOM   809  O  O   . VAL A  1 106 ? -11.835 -9.837  21.613  1.00 11.03 ? 106  VAL A O   1 
ATOM   810  C  CB  . VAL A  1 106 ? -11.906 -13.092 20.806  1.00 13.52 ? 106  VAL A CB  1 
ATOM   811  C  CG1 . VAL A  1 106 ? -12.681 -12.293 19.761  1.00 13.29 ? 106  VAL A CG1 1 
ATOM   812  C  CG2 . VAL A  1 106 ? -10.904 -14.042 20.182  1.00 15.19 ? 106  VAL A CG2 1 
ATOM   813  N  N   . ILE A  1 107 ? -12.990 -11.158 23.105  1.00 12.11 ? 107  ILE A N   1 
ATOM   814  C  CA  . ILE A  1 107 ? -13.916 -10.074 23.528  1.00 13.30 ? 107  ILE A CA  1 
ATOM   815  C  C   . ILE A  1 107 ? -13.079 -8.926  24.108  1.00 13.10 ? 107  ILE A C   1 
ATOM   816  O  O   . ILE A  1 107 ? -13.296 -7.760  23.702  1.00 12.81 ? 107  ILE A O   1 
ATOM   817  C  CB  . ILE A  1 107 ? -14.965 -10.580 24.523  1.00 13.94 ? 107  ILE A CB  1 
ATOM   818  C  CG1 . ILE A  1 107 ? -15.936 -11.583 23.899  1.00 14.70 ? 107  ILE A CG1 1 
ATOM   819  C  CG2 . ILE A  1 107 ? -15.701 -9.398  25.119  1.00 14.71 ? 107  ILE A CG2 1 
ATOM   820  C  CD1 . ILE A  1 107 ? -16.715 -12.381 24.928  1.00 15.93 ? 107  ILE A CD1 1 
ATOM   821  N  N   . ASN A  1 108 ? -12.109 -9.249  24.972  1.00 13.42 ? 108  ASN A N   1 
ATOM   822  C  CA  . ASN A  1 108 ? -11.174 -8.230  25.527  1.00 14.84 ? 108  ASN A CA  1 
ATOM   823  C  C   . ASN A  1 108 ? -10.461 -7.472  24.401  1.00 14.82 ? 108  ASN A C   1 
ATOM   824  O  O   . ASN A  1 108 ? -10.408 -6.237  24.477  1.00 15.10 ? 108  ASN A O   1 
ATOM   825  C  CB  . ASN A  1 108 ? -10.223 -8.853  26.542  1.00 15.68 ? 108  ASN A CB  1 
ATOM   826  C  CG  . ASN A  1 108 ? -10.924 -9.292  27.817  1.00 16.39 ? 108  ASN A CG  1 
ATOM   827  O  OD1 . ASN A  1 108 ? -11.969 -8.758  28.178  1.00 18.74 ? 108  ASN A OD1 1 
ATOM   828  N  ND2 . ASN A  1 108 ? -10.374 -10.284 28.484  1.00 19.57 ? 108  ASN A ND2 1 
ATOM   829  N  N   . GLN A  1 109 ? -9.909  -8.154  23.402  1.00 14.32 ? 109  GLN A N   1 
ATOM   830  C  CA  . GLN A  1 109 ? -9.158  -7.527  22.292  1.00 15.35 ? 109  GLN A CA  1 
ATOM   831  C  C   . GLN A  1 109 ? -10.098 -6.676  21.442  1.00 14.44 ? 109  GLN A C   1 
ATOM   832  O  O   . GLN A  1 109 ? -9.707  -5.581  21.074  1.00 13.74 ? 109  GLN A O   1 
ATOM   833  C  CB  . GLN A  1 109 ? -8.467  -8.588  21.458  1.00 17.47 ? 109  GLN A CB  1 
ATOM   834  C  CG  . GLN A  1 109 ? -7.366  -9.311  22.223  1.00 20.46 ? 109  GLN A CG  1 
ATOM   835  C  CD  . GLN A  1 109 ? -6.813  -10.430 21.366  1.00 25.07 ? 109  GLN A CD  1 
ATOM   836  O  OE1 . GLN A  1 109 ? -6.539  -10.235 20.182  1.00 30.77 ? 109  GLN A OE1 1 
ATOM   837  N  NE2 . GLN A  1 109 ? -6.758  -11.628 21.927  1.00 26.48 ? 109  GLN A NE2 1 
ATOM   838  N  N   . LYS A  1 110 ? -11.335 -7.127  21.244  1.00 12.76 ? 110  LYS A N   1 
ATOM   839  C  CA  . LYS A  1 110 ? -12.325 -6.395  20.438  1.00 14.12 ? 110  LYS A CA  1 
ATOM   840  C  C   . LYS A  1 110 ? -12.648 -5.070  21.135  1.00 14.07 ? 110  LYS A C   1 
ATOM   841  O  O   . LYS A  1 110 ? -12.600 -3.986  20.495  1.00 14.76 ? 110  LYS A O   1 
ATOM   842  C  CB  . LYS A  1 110 ? -13.530 -7.315  20.262  1.00 14.91 ? 110  LYS A CB  1 
ATOM   843  C  CG  . LYS A  1 110 ? -14.696 -6.744  19.489  1.00 16.19 ? 110  LYS A CG  1 
ATOM   844  C  CD  . LYS A  1 110 ? -15.565 -5.831  20.317  1.00 17.95 ? 110  LYS A CD  1 
ATOM   845  C  CE  . LYS A  1 110 ? -16.964 -5.698  19.750  1.00 19.79 ? 110  LYS A CE  1 
ATOM   846  N  NZ  . LYS A  1 110 ? -17.876 -4.970  20.647  1.00 18.56 ? 110  LYS A NZ  1 
ATOM   847  N  N   . LYS A  1 111 ? -12.978 -5.141  22.416  1.00 14.19 ? 111  LYS A N   1 
ATOM   848  C  CA  . LYS A  1 111 ? -13.295 -3.935  23.217  1.00 16.05 ? 111  LYS A CA  1 
ATOM   849  C  C   . LYS A  1 111 ? -12.073 -3.011  23.304  1.00 16.09 ? 111  LYS A C   1 
ATOM   850  O  O   . LYS A  1 111 ? -12.268 -1.790  23.183  1.00 16.64 ? 111  LYS A O   1 
ATOM   851  C  CB  . LYS A  1 111 ? -13.848 -4.326  24.582  1.00 17.33 ? 111  LYS A CB  1 
ATOM   852  C  CG  . LYS A  1 111 ? -15.230 -4.973  24.469  1.00 20.26 ? 111  LYS A CG  1 
ATOM   853  C  CD  . LYS A  1 111 ? -15.741 -5.519  25.773  1.00 23.50 ? 111  LYS A CD  1 
ATOM   854  C  CE  . LYS A  1 111 ? -15.828 -4.472  26.858  1.00 28.30 ? 111  LYS A CE  1 
ATOM   855  N  NZ  . LYS A  1 111 ? -16.202 -5.107  28.147  1.00 30.99 ? 111  LYS A NZ  1 
ATOM   856  N  N   . ALA A  1 112 ? -10.878 -3.555  23.510  1.00 15.07 ? 112  ALA A N   1 
ATOM   857  C  CA  . ALA A  1 112 ? -9.641  -2.766  23.677  1.00 15.58 ? 112  ALA A CA  1 
ATOM   858  C  C   . ALA A  1 112 ? -9.270  -2.014  22.397  1.00 16.97 ? 112  ALA A C   1 
ATOM   859  O  O   . ALA A  1 112 ? -8.605  -0.957  22.509  1.00 16.32 ? 112  ALA A O   1 
ATOM   860  C  CB  . ALA A  1 112 ? -8.521  -3.643  24.131  1.00 16.25 ? 112  ALA A CB  1 
ATOM   861  N  N   . SER A  1 113 ? -9.625  -2.538  21.218  1.00 15.78 ? 113  SER A N   1 
ATOM   862  C  CA  . SER A  1 113 ? -9.243  -1.945  19.916  1.00 15.82 ? 113  SER A CA  1 
ATOM   863  C  C   . SER A  1 113 ? -9.787  -0.522  19.820  1.00 17.16 ? 113  SER A C   1 
ATOM   864  O  O   . SER A  1 113 ? -9.205  0.241   19.073  1.00 18.72 ? 113  SER A O   1 
ATOM   865  C  CB  . SER A  1 113 ? -9.701  -2.772  18.736  1.00 16.09 ? 113  SER A CB  1 
ATOM   866  O  OG  . SER A  1 113 ? -11.112 -2.740  18.599  1.00 15.49 ? 113  SER A OG  1 
ATOM   867  N  N   . GLY A  1 114 ? -10.909 -0.266  20.473  1.00 18.55 ? 114  GLY A N   1 
ATOM   868  C  CA  . GLY A  1 114 ? -11.661 0.993   20.362  1.00 22.31 ? 114  GLY A CA  1 
ATOM   869  C  C   . GLY A  1 114 ? -12.428 1.107   19.054  1.00 24.12 ? 114  GLY A C   1 
ATOM   870  O  O   . GLY A  1 114 ? -13.192 2.081   18.936  1.00 25.98 ? 114  GLY A O   1 
ATOM   871  N  N   . TYR A  1 115 ? -12.282 0.187   18.090  1.00 18.95 ? 115  TYR A N   1 
ATOM   872  C  CA  . TYR A  1 115 ? -13.021 0.307   16.799  1.00 18.40 ? 115  TYR A CA  1 
ATOM   873  C  C   . TYR A  1 115 ? -14.519 0.119   17.057  1.00 18.32 ? 115  TYR A C   1 
ATOM   874  O  O   . TYR A  1 115 ? -14.894 -0.706  17.941  1.00 18.75 ? 115  TYR A O   1 
ATOM   875  C  CB  . TYR A  1 115 ? -12.526 -0.686  15.744  1.00 18.05 ? 115  TYR A CB  1 
ATOM   876  C  CG  . TYR A  1 115 ? -11.062 -0.598  15.443  1.00 17.34 ? 115  TYR A CG  1 
ATOM   877  C  CD1 . TYR A  1 115 ? -10.441 0.627   15.219  1.00 18.62 ? 115  TYR A CD1 1 
ATOM   878  C  CD2 . TYR A  1 115 ? -10.279 -1.737  15.383  1.00 16.75 ? 115  TYR A CD2 1 
ATOM   879  C  CE1 . TYR A  1 115 ? -9.088  0.708   14.947  1.00 19.72 ? 115  TYR A CE1 1 
ATOM   880  C  CE2 . TYR A  1 115 ? -8.924  -1.669  15.113  1.00 17.86 ? 115  TYR A CE2 1 
ATOM   881  C  CZ  . TYR A  1 115 ? -8.316  -0.441  14.914  1.00 19.83 ? 115  TYR A CZ  1 
ATOM   882  O  OH  . TYR A  1 115 ? -6.973  -0.367  14.656  1.00 21.18 ? 115  TYR A OH  1 
ATOM   883  N  N   . SER A  1 116 ? -15.343 0.887   16.338  1.00 18.45 ? 116  SER A N   1 
ATOM   884  C  CA  . SER A  1 116 ? -16.812 0.934   16.555  1.00 19.25 ? 116  SER A CA  1 
ATOM   885  C  C   . SER A  1 116 ? -17.579 0.291   15.394  1.00 18.84 ? 116  SER A C   1 
ATOM   886  O  O   . SER A  1 116 ? -18.811 0.466   15.358  1.00 21.74 ? 116  SER A O   1 
ATOM   887  C  CB  . SER A  1 116 ? -17.287 2.337   16.822  1.00 21.57 ? 116  SER A CB  1 
ATOM   888  O  OG  . SER A  1 116 ? -16.624 3.283   16.005  1.00 23.05 ? 116  SER A OG  1 
ATOM   889  N  N   . ASN A  1 117 ? -16.918 -0.473  14.534  1.00 14.45 ? 117  ASN A N   1 
ATOM   890  C  CA  . ASN A  1 117 ? -17.532 -1.015  13.303  1.00 13.46 ? 117  ASN A CA  1 
ATOM   891  C  C   . ASN A  1 117 ? -17.611 -2.550  13.382  1.00 12.24 ? 117  ASN A C   1 
ATOM   892  O  O   . ASN A  1 117 ? -17.391 -3.193  12.381  1.00 13.25 ? 117  ASN A O   1 
ATOM   893  C  CB  . ASN A  1 117 ? -16.844 -0.525  12.026  1.00 12.89 ? 117  ASN A CB  1 
ATOM   894  C  CG  . ASN A  1 117 ? -15.376 -0.872  11.905  1.00 12.94 ? 117  ASN A CG  1 
ATOM   895  O  OD1 . ASN A  1 117 ? -14.670 -0.941  12.909  1.00 13.70 ? 117  ASN A OD1 1 
ATOM   896  N  ND2 . ASN A  1 117 ? -14.886 -1.048  10.679  1.00 13.14 ? 117  ASN A ND2 1 
ATOM   897  N  N   . PHE A  1 118 ? -17.934 -3.102  14.540  1.00 12.69 ? 118  PHE A N   1 
ATOM   898  C  CA  . PHE A  1 118 ? -18.221 -4.544  14.700  1.00 12.62 ? 118  PHE A CA  1 
ATOM   899  C  C   . PHE A  1 118 ? -19.722 -4.766  14.555  1.00 13.19 ? 118  PHE A C   1 
ATOM   900  O  O   . PHE A  1 118 ? -20.550 -4.008  15.125  1.00 16.20 ? 118  PHE A O   1 
ATOM   901  C  CB  . PHE A  1 118 ? -17.670 -5.047  16.034  1.00 12.59 ? 118  PHE A CB  1 
ATOM   902  C  CG  . PHE A  1 118 ? -16.163 -5.010  16.090  1.00 12.51 ? 118  PHE A CG  1 
ATOM   903  C  CD1 . PHE A  1 118 ? -15.392 -5.931  15.385  1.00 12.82 ? 118  PHE A CD1 1 
ATOM   904  C  CD2 . PHE A  1 118 ? -15.517 -4.000  16.785  1.00 14.24 ? 118  PHE A CD2 1 
ATOM   905  C  CE1 . PHE A  1 118 ? -14.007 -5.871  15.427  1.00 13.53 ? 118  PHE A CE1 1 
ATOM   906  C  CE2 . PHE A  1 118 ? -14.132 -3.944  16.822  1.00 13.89 ? 118  PHE A CE2 1 
ATOM   907  C  CZ  . PHE A  1 118 ? -13.381 -4.877  16.144  1.00 13.79 ? 118  PHE A CZ  1 
ATOM   908  N  N   . TYR A  1 119 ? -20.071 -5.794  13.805  1.00 12.65 ? 119  TYR A N   1 
ATOM   909  C  CA  . TYR A  1 119 ? -21.477 -6.227  13.627  1.00 12.77 ? 119  TYR A CA  1 
ATOM   910  C  C   . TYR A  1 119 ? -21.919 -7.134  14.765  1.00 14.07 ? 119  TYR A C   1 
ATOM   911  O  O   . TYR A  1 119 ? -23.128 -7.126  15.075  1.00 15.24 ? 119  TYR A O   1 
ATOM   912  C  CB  . TYR A  1 119 ? -21.617 -6.900  12.280  1.00 12.44 ? 119  TYR A CB  1 
ATOM   913  C  CG  . TYR A  1 119 ? -23.001 -7.318  11.873  1.00 12.65 ? 119  TYR A CG  1 
ATOM   914  C  CD1 . TYR A  1 119 ? -23.936 -6.402  11.449  1.00 12.78 ? 119  TYR A CD1 1 
ATOM   915  C  CD2 . TYR A  1 119 ? -23.332 -8.665  11.809  1.00 11.57 ? 119  TYR A CD2 1 
ATOM   916  C  CE1 . TYR A  1 119 ? -25.188 -6.804  11.009  1.00 12.03 ? 119  TYR A CE1 1 
ATOM   917  C  CE2 . TYR A  1 119 ? -24.562 -9.079  11.325  1.00 11.85 ? 119  TYR A CE2 1 
ATOM   918  C  CZ  . TYR A  1 119 ? -25.484 -8.146  10.897  1.00 12.45 ? 119  TYR A CZ  1 
ATOM   919  O  OH  . TYR A  1 119 ? -26.690 -8.543  10.393  1.00 12.37 ? 119  TYR A OH  1 
ATOM   920  N  N   . GLY A  1 120 ? -21.006 -7.888  15.354  1.00 13.46 ? 120  GLY A N   1 
ATOM   921  C  CA  . GLY A  1 120 ? -21.316 -8.771  16.488  1.00 13.45 ? 120  GLY A CA  1 
ATOM   922  C  C   . GLY A  1 120 ? -20.512 -10.043 16.409  1.00 12.62 ? 120  GLY A C   1 
ATOM   923  O  O   . GLY A  1 120 ? -19.539 -10.103 15.630  1.00 12.58 ? 120  GLY A O   1 
ATOM   924  N  N   . TYR A  1 121 ? -20.853 -10.986 17.268  1.00 12.25 ? 121  TYR A N   1 
ATOM   925  C  CA  . TYR A  1 121 ? -20.146 -12.273 17.427  1.00 12.39 ? 121  TYR A CA  1 
ATOM   926  C  C   . TYR A  1 121 ? -20.976 -13.401 16.811  1.00 11.92 ? 121  TYR A C   1 
ATOM   927  O  O   . TYR A  1 121 ? -22.164 -13.595 17.197  1.00 13.76 ? 121  TYR A O   1 
ATOM   928  C  CB  . TYR A  1 121 ? -19.910 -12.585 18.899  1.00 11.73 ? 121  TYR A CB  1 
ATOM   929  C  CG  . TYR A  1 121 ? -19.059 -11.563 19.609  1.00 11.82 ? 121  TYR A CG  1 
ATOM   930  C  CD1 . TYR A  1 121 ? -17.677 -11.621 19.571  1.00 12.65 ? 121  TYR A CD1 1 
ATOM   931  C  CD2 . TYR A  1 121 ? -19.638 -10.512 20.280  1.00 12.09 ? 121  TYR A CD2 1 
ATOM   932  C  CE1 . TYR A  1 121 ? -16.907 -10.677 20.211  1.00 13.37 ? 121  TYR A CE1 1 
ATOM   933  C  CE2 . TYR A  1 121 ? -18.877 -9.546  20.917  1.00 13.03 ? 121  TYR A CE2 1 
ATOM   934  C  CZ  . TYR A  1 121 ? -17.502 -9.642  20.910  1.00 12.34 ? 121  TYR A CZ  1 
ATOM   935  O  OH  . TYR A  1 121 ? -16.727 -8.713  21.556  1.00 13.38 ? 121  TYR A OH  1 
ATOM   936  N  N   . GLU A  1 122 ? -20.345 -14.173 15.925  1.00 11.66 ? 122  GLU A N   1 
ATOM   937  C  CA  . GLU A  1 122 ? -20.886 -15.458 15.442  1.00 11.30 ? 122  GLU A CA  1 
ATOM   938  C  C   . GLU A  1 122 ? -20.350 -16.558 16.366  1.00 11.57 ? 122  GLU A C   1 
ATOM   939  O  O   . GLU A  1 122 ? -19.127 -16.773 16.365  1.00 10.52 ? 122  GLU A O   1 
ATOM   940  C  CB  . GLU A  1 122 ? -20.515 -15.689 13.983  1.00 11.16 ? 122  GLU A CB  1 
ATOM   941  C  CG  . GLU A  1 122 ? -21.070 -17.000 13.432  1.00 11.68 ? 122  GLU A CG  1 
ATOM   942  C  CD  . GLU A  1 122 ? -20.356 -17.438 12.171  1.00 12.23 ? 122  GLU A CD  1 
ATOM   943  O  OE1 . GLU A  1 122 ? -19.121 -17.670 12.246  1.00 11.92 ? 122  GLU A OE1 1 
ATOM   944  O  OE2 . GLU A  1 122 ? -21.017 -17.573 11.118  1.00 12.84 ? 122  GLU A OE2 1 
ATOM   945  N  N   . ILE A  1 123 ? -21.209 -17.177 17.167  1.00 11.36 ? 123  ILE A N   1 
ATOM   946  C  CA  . ILE A  1 123 ? -20.763 -18.172 18.189  1.00 12.27 ? 123  ILE A CA  1 
ATOM   947  C  C   . ILE A  1 123 ? -20.106 -19.371 17.497  1.00 11.99 ? 123  ILE A C   1 
ATOM   948  O  O   . ILE A  1 123 ? -19.031 -19.800 17.965  1.00 12.81 ? 123  ILE A O   1 
ATOM   949  C  CB  . ILE A  1 123 ? -21.923 -18.552 19.127  1.00 12.80 ? 123  ILE A CB  1 
ATOM   950  C  CG1 . ILE A  1 123 ? -22.216 -17.389 20.086  1.00 13.30 ? 123  ILE A CG1 1 
ATOM   951  C  CG2 . ILE A  1 123 ? -21.612 -19.850 19.881  1.00 12.62 ? 123  ILE A CG2 1 
ATOM   952  C  CD1 . ILE A  1 123 ? -23.350 -17.604 21.055  1.00 13.58 ? 123  ILE A CD1 1 
ATOM   953  N  N   . TRP A  1 124 ? -20.696 -19.890 16.421  1.00 11.42 ? 124  TRP A N   1 
ATOM   954  C  CA  . TRP A  1 124 ? -20.184 -21.081 15.725  1.00 11.02 ? 124  TRP A CA  1 
ATOM   955  C  C   . TRP A  1 124 ? -20.559 -21.029 14.248  1.00 11.43 ? 124  TRP A C   1 
ATOM   956  O  O   . TRP A  1 124 ? -21.372 -20.171 13.835  1.00 11.85 ? 124  TRP A O   1 
ATOM   957  C  CB  . TRP A  1 124 ? -20.658 -22.389 16.368  1.00 12.10 ? 124  TRP A CB  1 
ATOM   958  C  CG  . TRP A  1 124 ? -19.731 -23.523 16.066  1.00 11.93 ? 124  TRP A CG  1 
ATOM   959  C  CD1 . TRP A  1 124 ? -19.905 -24.510 15.133  1.00 12.31 ? 124  TRP A CD1 1 
ATOM   960  C  CD2 . TRP A  1 124 ? -18.454 -23.776 16.680  1.00 12.35 ? 124  TRP A CD2 1 
ATOM   961  N  NE1 . TRP A  1 124 ? -18.812 -25.325 15.101  1.00 12.93 ? 124  TRP A NE1 1 
ATOM   962  C  CE2 . TRP A  1 124 ? -17.911 -24.911 16.045  1.00 12.51 ? 124  TRP A CE2 1 
ATOM   963  C  CE3 . TRP A  1 124 ? -17.702 -23.136 17.668  1.00 12.23 ? 124  TRP A CE3 1 
ATOM   964  C  CZ2 . TRP A  1 124 ? -16.674 -25.451 16.396  1.00 12.50 ? 124  TRP A CZ2 1 
ATOM   965  C  CZ3 . TRP A  1 124 ? -16.483 -23.667 18.020  1.00 12.82 ? 124  TRP A CZ3 1 
ATOM   966  C  CH2 . TRP A  1 124 ? -15.982 -24.814 17.399  1.00 13.21 ? 124  TRP A CH2 1 
ATOM   967  N  N   . ASN A  1 125 ? -19.819 -21.807 13.491  1.00 10.84 ? 125  ASN A N   1 
ATOM   968  C  CA  . ASN A  1 125 ? -19.909 -21.841 12.018  1.00 10.57 ? 125  ASN A CA  1 
ATOM   969  C  C   . ASN A  1 125 ? -20.315 -23.251 11.584  1.00 10.60 ? 125  ASN A C   1 
ATOM   970  O  O   . ASN A  1 125 ? -19.542 -24.226 11.755  1.00 9.77  ? 125  ASN A O   1 
ATOM   971  C  CB  . ASN A  1 125 ? -18.617 -21.376 11.366  1.00 9.81  ? 125  ASN A CB  1 
ATOM   972  C  CG  . ASN A  1 125 ? -18.699 -21.440 9.861   1.00 10.04 ? 125  ASN A CG  1 
ATOM   973  O  OD1 . ASN A  1 125 ? -19.763 -21.127 9.325   1.00 10.45 ? 125  ASN A OD1 1 
ATOM   974  N  ND2 . ASN A  1 125 ? -17.610 -21.808 9.185   1.00 10.01 ? 125  ASN A ND2 1 
ATOM   975  N  N   . GLU A  1 126 ? -21.488 -23.329 10.958  1.00 10.69 ? 126  GLU A N   1 
ATOM   976  C  CA  . GLU A  1 126 ? -22.020 -24.577 10.362  1.00 11.04 ? 126  GLU A CA  1 
ATOM   977  C  C   . GLU A  1 126 ? -22.037 -25.732 11.374  1.00 11.30 ? 126  GLU A C   1 
ATOM   978  O  O   . GLU A  1 126 ? -21.504 -26.820 11.075  1.00 9.71  ? 126  GLU A O   1 
ATOM   979  C  CB  . GLU A  1 126 ? -21.247 -24.909 9.077   1.00 11.28 ? 126  GLU A CB  1 
ATOM   980  C  CG  . GLU A  1 126 ? -21.338 -23.817 8.020   1.00 11.29 ? 126  GLU A CG  1 
ATOM   981  C  CD  . GLU A  1 126 ? -20.842 -24.207 6.635   1.00 13.21 ? 126  GLU A CD  1 
ATOM   982  O  OE1 . GLU A  1 126 ? -20.086 -25.226 6.555   1.00 14.63 ? 126  GLU A OE1 1 
ATOM   983  O  OE2 . GLU A  1 126 ? -21.188 -23.516 5.652   1.00 13.70 ? 126  GLU A OE2 1 
ATOM   984  N  N   . PRO A  1 127 ? -22.636 -25.553 12.574  1.00 11.81 ? 127  PRO A N   1 
ATOM   985  C  CA  . PRO A  1 127 ? -22.618 -26.588 13.613  1.00 11.69 ? 127  PRO A CA  1 
ATOM   986  C  C   . PRO A  1 127 ? -23.342 -27.856 13.169  1.00 12.85 ? 127  PRO A C   1 
ATOM   987  O  O   . PRO A  1 127 ? -23.043 -28.931 13.708  1.00 13.46 ? 127  PRO A O   1 
ATOM   988  C  CB  . PRO A  1 127 ? -23.332 -25.935 14.808  1.00 12.67 ? 127  PRO A CB  1 
ATOM   989  C  CG  . PRO A  1 127 ? -24.263 -24.925 14.157  1.00 12.65 ? 127  PRO A CG  1 
ATOM   990  C  CD  . PRO A  1 127 ? -23.405 -24.376 13.024  1.00 12.61 ? 127  PRO A CD  1 
ATOM   991  N  N   . ASP A  1 128 ? -24.269 -27.724 12.213  1.00 12.33 ? 128  ASP A N   1 
ATOM   992  C  CA  . ASP A  1 128 ? -24.984 -28.864 11.591  1.00 12.18 ? 128  ASP A CA  1 
ATOM   993  C  C   . ASP A  1 128 ? -23.984 -29.820 10.938  1.00 12.60 ? 128  ASP A C   1 
ATOM   994  O  O   . ASP A  1 128 ? -24.285 -31.021 10.894  1.00 13.58 ? 128  ASP A O   1 
ATOM   995  C  CB  . ASP A  1 128 ? -26.082 -28.418 10.616  1.00 12.70 ? 128  ASP A CB  1 
ATOM   996  C  CG  . ASP A  1 128 ? -25.651 -27.455 9.520   1.00 12.65 ? 128  ASP A CG  1 
ATOM   997  O  OD1 . ASP A  1 128 ? -24.719 -26.611 9.776   1.00 12.02 ? 128  ASP A OD1 1 
ATOM   998  O  OD2 . ASP A  1 128 ? -26.237 -27.555 8.403   1.00 12.45 ? 128  ASP A OD2 1 
ATOM   999  N  N   . GLY A  1 129 ? -22.871 -29.309 10.438  1.00 12.23 ? 129  GLY A N   1 
ATOM   1000 C  CA  . GLY A  1 129 ? -21.790 -30.095 9.817   1.00 12.90 ? 129  GLY A CA  1 
ATOM   1001 C  C   . GLY A  1 129 ? -20.554 -30.232 10.696  1.00 12.17 ? 129  GLY A C   1 
ATOM   1002 O  O   . GLY A  1 129 ? -19.802 -31.156 10.420  1.00 13.34 ? 129  GLY A O   1 
ATOM   1003 N  N   . THR A  1 130 ? -20.263 -29.273 11.588  1.00 12.47 ? 130  THR A N   1 
ATOM   1004 C  CA  . THR A  1 130 ? -18.916 -29.145 12.200  1.00 12.29 ? 130  THR A CA  1 
ATOM   1005 C  C   . THR A  1 130 ? -18.920 -29.367 13.713  1.00 14.53 ? 130  THR A C   1 
ATOM   1006 O  O   . THR A  1 130 ? -17.827 -29.289 14.270  1.00 16.95 ? 130  THR A O   1 
ATOM   1007 C  CB  . THR A  1 130 ? -18.226 -27.811 11.902  1.00 11.39 ? 130  THR A CB  1 
ATOM   1008 O  OG1 . THR A  1 130 ? -18.928 -26.814 12.646  1.00 12.00 ? 130  THR A OG1 1 
ATOM   1009 C  CG2 . THR A  1 130 ? -18.161 -27.529 10.414  1.00 11.69 ? 130  THR A CG2 1 
ATOM   1010 N  N   . PHE A  1 131 ? -20.057 -29.570 14.361  1.00 16.16 ? 131  PHE A N   1 
ATOM   1011 C  CA  . PHE A  1 131 ? -20.087 -29.682 15.836  1.00 17.78 ? 131  PHE A CA  1 
ATOM   1012 C  C   . PHE A  1 131 ? -20.668 -31.041 16.226  1.00 22.88 ? 131  PHE A C   1 
ATOM   1013 O  O   . PHE A  1 131 ? -21.834 -31.052 16.567  1.00 25.20 ? 131  PHE A O   1 
ATOM   1014 C  CB  . PHE A  1 131 ? -20.826 -28.513 16.480  1.00 17.53 ? 131  PHE A CB  1 
ATOM   1015 C  CG  . PHE A  1 131 ? -20.321 -28.260 17.879  1.00 18.19 ? 131  PHE A CG  1 
ATOM   1016 C  CD1 . PHE A  1 131 ? -19.240 -27.418 18.086  1.00 16.84 ? 131  PHE A CD1 1 
ATOM   1017 C  CD2 . PHE A  1 131 ? -20.847 -28.937 18.968  1.00 17.66 ? 131  PHE A CD2 1 
ATOM   1018 C  CE1 . PHE A  1 131 ? -18.742 -27.208 19.361  1.00 18.26 ? 131  PHE A CE1 1 
ATOM   1019 C  CE2 . PHE A  1 131 ? -20.330 -28.742 20.245  1.00 16.76 ? 131  PHE A CE2 1 
ATOM   1020 C  CZ  . PHE A  1 131 ? -19.297 -27.855 20.438  1.00 17.98 ? 131  PHE A CZ  1 
ATOM   1021 N  N   . LYS A  1 132 ? -19.865 -32.103 16.143  1.00 31.62 ? 132  LYS A N   1 
ATOM   1022 C  CA  . LYS A  1 132 ? -20.229 -33.491 16.575  1.00 40.28 ? 132  LYS A CA  1 
ATOM   1023 C  C   . LYS A  1 132 ? -19.085 -34.122 17.378  1.00 39.90 ? 132  LYS A C   1 
ATOM   1024 O  O   . LYS A  1 132 ? -17.903 -33.760 17.157  1.00 40.17 ? 132  LYS A O   1 
ATOM   1025 C  CB  . LYS A  1 132 ? -20.543 -34.393 15.384  1.00 47.63 ? 132  LYS A CB  1 
ATOM   1026 C  CG  . LYS A  1 132 ? -21.547 -33.824 14.401  1.00 55.27 ? 132  LYS A CG  1 
ATOM   1027 C  CD  . LYS A  1 132 ? -22.894 -33.483 14.999  1.00 63.18 ? 132  LYS A CD  1 
ATOM   1028 C  CE  . LYS A  1 132 ? -23.566 -32.342 14.255  1.00 70.37 ? 132  LYS A CE  1 
ATOM   1029 N  NZ  . LYS A  1 132 ? -25.020 -32.258 14.541  1.00 73.48 ? 132  LYS A NZ  1 
ATOM   1030 N  N   . ASN A  1 133 ? -19.423 -35.018 18.308  1.00 46.24 ? 133  ASN A N   1 
ATOM   1031 C  CA  . ASN A  1 133 ? -18.428 -35.800 19.096  1.00 46.86 ? 133  ASN A CA  1 
ATOM   1032 C  C   . ASN A  1 133 ? -17.451 -34.843 19.787  1.00 45.29 ? 133  ASN A C   1 
ATOM   1033 O  O   . ASN A  1 133 ? -16.219 -35.106 19.761  1.00 44.44 ? 133  ASN A O   1 
ATOM   1034 C  CB  . ASN A  1 133 ? -17.707 -36.824 18.214  1.00 51.70 ? 133  ASN A CB  1 
ATOM   1035 C  CG  . ASN A  1 133 ? -18.688 -37.827 17.656  1.00 54.14 ? 133  ASN A CG  1 
ATOM   1036 O  OD1 . ASN A  1 133 ? -19.405 -38.468 18.422  1.00 59.55 ? 133  ASN A OD1 1 
ATOM   1037 N  ND2 . ASN A  1 133 ? -18.779 -37.912 16.339  1.00 58.16 ? 133  ASN A ND2 1 
ATOM   1038 N  N   . ASN A  1 134 ? -17.985 -33.795 20.420  1.00 37.03 ? 134  ASN A N   1 
ATOM   1039 C  CA  . ASN A  1 134 ? -17.157 -32.738 21.052  1.00 37.30 ? 134  ASN A CA  1 
ATOM   1040 C  C   . ASN A  1 134 ? -17.259 -32.791 22.580  1.00 37.38 ? 134  ASN A C   1 
ATOM   1041 O  O   . ASN A  1 134 ? -16.673 -31.887 23.231  1.00 43.28 ? 134  ASN A O   1 
ATOM   1042 C  CB  . ASN A  1 134 ? -17.524 -31.376 20.487  1.00 30.72 ? 134  ASN A CB  1 
ATOM   1043 C  CG  . ASN A  1 134 ? -16.742 -31.047 19.235  1.00 32.50 ? 134  ASN A CG  1 
ATOM   1044 O  OD1 . ASN A  1 134 ? -15.662 -31.606 18.999  1.00 31.07 ? 134  ASN A OD1 1 
ATOM   1045 N  ND2 . ASN A  1 134 ? -17.261 -30.115 18.447  1.00 24.23 ? 134  ASN A ND2 1 
ATOM   1046 N  N   . ASN A  1 135 ? -17.936 -33.808 23.129  1.00 39.03 ? 135  ASN A N   1 
ATOM   1047 C  CA  . ASN A  1 135 ? -18.082 -34.058 24.593  1.00 37.34 ? 135  ASN A CA  1 
ATOM   1048 C  C   . ASN A  1 135 ? -18.971 -32.988 25.240  1.00 35.46 ? 135  ASN A C   1 
ATOM   1049 O  O   . ASN A  1 135 ? -19.184 -33.042 26.459  1.00 40.02 ? 135  ASN A O   1 
ATOM   1050 C  CB  . ASN A  1 135 ? -16.727 -34.120 25.302  1.00 41.44 ? 135  ASN A CB  1 
ATOM   1051 C  CG  . ASN A  1 135 ? -16.642 -35.256 26.300  1.00 46.20 ? 135  ASN A CG  1 
ATOM   1052 O  OD1 . ASN A  1 135 ? -17.648 -35.681 26.866  1.00 42.23 ? 135  ASN A OD1 1 
ATOM   1053 N  ND2 . ASN A  1 135 ? -15.441 -35.769 26.511  1.00 50.47 ? 135  ASN A ND2 1 
ATOM   1054 N  N   . VAL A  1 136 ? -19.468 -32.032 24.459  1.00 27.65 ? 136  VAL A N   1 
ATOM   1055 C  CA  . VAL A  1 136 ? -20.528 -31.079 24.888  1.00 22.36 ? 136  VAL A CA  1 
ATOM   1056 C  C   . VAL A  1 136 ? -21.459 -30.998 23.689  1.00 19.76 ? 136  VAL A C   1 
ATOM   1057 O  O   . VAL A  1 136 ? -20.960 -31.107 22.558  1.00 19.98 ? 136  VAL A O   1 
ATOM   1058 C  CB  . VAL A  1 136 ? -19.954 -29.712 25.314  1.00 22.07 ? 136  VAL A CB  1 
ATOM   1059 C  CG1 . VAL A  1 136 ? -19.253 -29.011 24.169  1.00 21.19 ? 136  VAL A CG1 1 
ATOM   1060 C  CG2 . VAL A  1 136 ? -21.000 -28.786 25.904  1.00 22.71 ? 136  VAL A CG2 1 
ATOM   1061 N  N   . SER A  1 137 ? -22.747 -30.869 23.922  1.00 18.73 ? 137  SER A N   1 
ATOM   1062 C  CA  . SER A  1 137 ? -23.737 -30.653 22.842  1.00 20.12 ? 137  SER A CA  1 
ATOM   1063 C  C   . SER A  1 137 ? -23.551 -29.238 22.251  1.00 18.22 ? 137  SER A C   1 
ATOM   1064 O  O   . SER A  1 137 ? -23.078 -28.325 22.956  1.00 16.13 ? 137  SER A O   1 
ATOM   1065 C  CB  . SER A  1 137 ? -25.138 -30.865 23.354  1.00 19.93 ? 137  SER A CB  1 
ATOM   1066 O  OG  . SER A  1 137 ? -25.576 -29.772 24.137  1.00 20.99 ? 137  SER A OG  1 
ATOM   1067 N  N   . PHE A  1 138 ? -23.881 -29.064 20.978  1.00 17.42 ? 138  PHE A N   1 
ATOM   1068 C  CA  . PHE A  1 138 ? -23.925 -27.715 20.359  1.00 16.93 ? 138  PHE A CA  1 
ATOM   1069 C  C   . PHE A  1 138 ? -24.807 -26.800 21.208  1.00 16.03 ? 138  PHE A C   1 
ATOM   1070 O  O   . PHE A  1 138 ? -24.365 -25.707 21.526  1.00 16.74 ? 138  PHE A O   1 
ATOM   1071 C  CB  . PHE A  1 138 ? -24.413 -27.738 18.909  1.00 16.43 ? 138  PHE A CB  1 
ATOM   1072 C  CG  . PHE A  1 138 ? -24.687 -26.364 18.375  1.00 15.93 ? 138  PHE A CG  1 
ATOM   1073 C  CD1 . PHE A  1 138 ? -23.643 -25.497 18.167  1.00 16.86 ? 138  PHE A CD1 1 
ATOM   1074 C  CD2 . PHE A  1 138 ? -25.980 -25.920 18.146  1.00 18.03 ? 138  PHE A CD2 1 
ATOM   1075 C  CE1 . PHE A  1 138 ? -23.875 -24.217 17.709  1.00 16.11 ? 138  PHE A CE1 1 
ATOM   1076 C  CE2 . PHE A  1 138 ? -26.210 -24.638 17.678  1.00 16.81 ? 138  PHE A CE2 1 
ATOM   1077 C  CZ  . PHE A  1 138 ? -25.155 -23.800 17.454  1.00 16.38 ? 138  PHE A CZ  1 
ATOM   1078 N  N   . ASN A  1 139 ? -26.005 -27.213 21.612  1.00 17.15 ? 139  ASN A N   1 
ATOM   1079 C  CA  . ASN A  1 139 ? -26.912 -26.335 22.410  1.00 18.40 ? 139  ASN A CA  1 
ATOM   1080 C  C   . ASN A  1 139 ? -26.215 -25.838 23.689  1.00 17.83 ? 139  ASN A C   1 
ATOM   1081 O  O   . ASN A  1 139 ? -26.349 -24.615 24.059  1.00 16.72 ? 139  ASN A O   1 
ATOM   1082 C  CB  . ASN A  1 139 ? -28.207 -27.071 22.765  1.00 18.63 ? 139  ASN A CB  1 
ATOM   1083 C  CG  . ASN A  1 139 ? -29.163 -27.230 21.600  1.00 21.51 ? 139  ASN A CG  1 
ATOM   1084 O  OD1 . ASN A  1 139 ? -28.987 -26.607 20.551  1.00 20.43 ? 139  ASN A OD1 1 
ATOM   1085 N  ND2 . ASN A  1 139 ? -30.204 -28.042 21.794  1.00 18.59 ? 139  ASN A ND2 1 
ATOM   1086 N  N   . ASP A  1 140 ? -25.531 -26.745 24.387  1.00 19.37 ? 140  ASP A N   1 
ATOM   1087 C  CA  . ASP A  1 140 ? -24.879 -26.427 25.680  1.00 21.11 ? 140  ASP A CA  1 
ATOM   1088 C  C   . ASP A  1 140 ? -23.714 -25.478 25.435  1.00 17.44 ? 140  ASP A C   1 
ATOM   1089 O  O   . ASP A  1 140 ? -23.571 -24.515 26.191  1.00 18.39 ? 140  ASP A O   1 
ATOM   1090 C  CB  . ASP A  1 140 ? -24.495 -27.706 26.420  1.00 22.20 ? 140  ASP A CB  1 
ATOM   1091 C  CG  . ASP A  1 140 ? -25.715 -28.352 27.042  1.00 27.80 ? 140  ASP A CG  1 
ATOM   1092 O  OD1 . ASP A  1 140 ? -26.623 -27.591 27.506  1.00 33.94 ? 140  ASP A OD1 1 
ATOM   1093 O  OD2 . ASP A  1 140 ? -25.756 -29.575 27.042  1.00 29.50 ? 140  ASP A OD2 1 
ATOM   1094 N  N   . MET A  1 141 ? -22.944 -25.706 24.369  1.00 16.03 ? 141  MET A N   1 
ATOM   1095 C  CA  . MET A  1 141 ? -21.814 -24.812 24.037  1.00 15.31 ? 141  MET A CA  1 
ATOM   1096 C  C   . MET A  1 141 ? -22.411 -23.435 23.721  1.00 14.10 ? 141  MET A C   1 
ATOM   1097 O  O   . MET A  1 141 ? -21.901 -22.429 24.215  1.00 14.16 ? 141  MET A O   1 
ATOM   1098 C  CB  . MET A  1 141 ? -21.014 -25.371 22.865  1.00 16.89 ? 141  MET A CB  1 
ATOM   1099 C  CG  . MET A  1 141 ? -19.884 -24.518 22.449  1.00 18.47 ? 141  MET A CG  1 
ATOM   1100 S  SD  . MET A  1 141 ? -20.363 -23.176 21.287  1.00 17.87 ? 141  MET A SD  1 
ATOM   1101 C  CE  . MET A  1 141 ? -20.997 -24.130 19.917  1.00 17.61 ? 141  MET A CE  1 
ATOM   1102 N  N   . TRP A  1 142 ? -23.489 -23.407 22.953  1.00 14.00 ? 142  TRP A N   1 
ATOM   1103 C  CA  . TRP A  1 142 ? -24.155 -22.149 22.540  1.00 13.95 ? 142  TRP A CA  1 
ATOM   1104 C  C   . TRP A  1 142 ? -24.579 -21.371 23.796  1.00 14.65 ? 142  TRP A C   1 
ATOM   1105 O  O   . TRP A  1 142 ? -24.283 -20.185 23.912  1.00 14.57 ? 142  TRP A O   1 
ATOM   1106 C  CB  . TRP A  1 142 ? -25.328 -22.427 21.602  1.00 13.67 ? 142  TRP A CB  1 
ATOM   1107 C  CG  . TRP A  1 142 ? -26.138 -21.208 21.364  1.00 13.43 ? 142  TRP A CG  1 
ATOM   1108 C  CD1 . TRP A  1 142 ? -27.107 -20.709 22.183  1.00 14.09 ? 142  TRP A CD1 1 
ATOM   1109 C  CD2 . TRP A  1 142 ? -26.034 -20.301 20.248  1.00 13.08 ? 142  TRP A CD2 1 
ATOM   1110 N  NE1 . TRP A  1 142 ? -27.576 -19.529 21.682  1.00 14.22 ? 142  TRP A NE1 1 
ATOM   1111 C  CE2 . TRP A  1 142 ? -26.962 -19.262 20.491  1.00 13.90 ? 142  TRP A CE2 1 
ATOM   1112 C  CE3 . TRP A  1 142 ? -25.247 -20.233 19.090  1.00 13.45 ? 142  TRP A CE3 1 
ATOM   1113 C  CZ2 . TRP A  1 142 ? -27.124 -18.187 19.626  1.00 13.97 ? 142  TRP A CZ2 1 
ATOM   1114 C  CZ3 . TRP A  1 142 ? -25.444 -19.187 18.203  1.00 13.05 ? 142  TRP A CZ3 1 
ATOM   1115 C  CH2 . TRP A  1 142 ? -26.357 -18.167 18.481  1.00 13.86 ? 142  TRP A CH2 1 
ATOM   1116 N  N   . LEU A  1 143 ? -25.328 -22.008 24.681  1.00 15.14 ? 143  LEU A N   1 
ATOM   1117 C  CA  . LEU A  1 143 ? -25.828 -21.323 25.897  1.00 15.93 ? 143  LEU A CA  1 
ATOM   1118 C  C   . LEU A  1 143 ? -24.652 -20.738 26.687  1.00 15.73 ? 143  LEU A C   1 
ATOM   1119 O  O   . LEU A  1 143 ? -24.730 -19.568 27.132  1.00 15.80 ? 143  LEU A O   1 
ATOM   1120 C  CB  . LEU A  1 143 ? -26.643 -22.324 26.727  1.00 17.13 ? 143  LEU A CB  1 
ATOM   1121 C  CG  . LEU A  1 143 ? -27.142 -21.814 28.080  1.00 18.83 ? 143  LEU A CG  1 
ATOM   1122 C  CD1 . LEU A  1 143 ? -27.883 -20.488 27.952  1.00 19.87 ? 143  LEU A CD1 1 
ATOM   1123 C  CD2 . LEU A  1 143 ? -28.006 -22.885 28.770  1.00 18.92 ? 143  LEU A CD2 1 
ATOM   1124 N  N   . GLN A  1 144 ? -23.612 -21.516 26.925  1.00 17.33 ? 144  GLN A N   1 
ATOM   1125 C  CA  . GLN A  1 144 ? -22.516 -21.071 27.811  1.00 18.06 ? 144  GLN A CA  1 
ATOM   1126 C  C   . GLN A  1 144 ? -21.766 -19.911 27.129  1.00 17.07 ? 144  GLN A C   1 
ATOM   1127 O  O   . GLN A  1 144 ? -21.406 -18.928 27.807  1.00 17.45 ? 144  GLN A O   1 
ATOM   1128 C  CB  . GLN A  1 144 ? -21.647 -22.268 28.220  1.00 19.48 ? 144  GLN A CB  1 
ATOM   1129 C  CG  . GLN A  1 144 ? -22.354 -23.246 29.160  1.00 20.60 ? 144  GLN A CG  1 
ATOM   1130 C  CD  . GLN A  1 144 ? -23.087 -22.606 30.325  1.00 24.29 ? 144  GLN A CD  1 
ATOM   1131 O  OE1 . GLN A  1 144 ? -22.518 -21.779 31.033  1.00 29.29 ? 144  GLN A OE1 1 
ATOM   1132 N  NE2 . GLN A  1 144 ? -24.344 -22.991 30.582  1.00 25.53 ? 144  GLN A NE2 1 
ATOM   1133 N  N   . THR A  1 145 ? -21.600 -19.969 25.820  1.00 15.73 ? 145  THR A N   1 
ATOM   1134 C  CA  . THR A  1 145 ? -20.865 -18.924 25.074  1.00 15.85 ? 145  THR A CA  1 
ATOM   1135 C  C   . THR A  1 145 ? -21.726 -17.659 25.035  1.00 13.73 ? 145  THR A C   1 
ATOM   1136 O  O   . THR A  1 145 ? -21.175 -16.523 25.182  1.00 15.04 ? 145  THR A O   1 
ATOM   1137 C  CB  . THR A  1 145 ? -20.482 -19.374 23.657  1.00 14.67 ? 145  THR A CB  1 
ATOM   1138 O  OG1 . THR A  1 145 ? -19.884 -20.666 23.690  1.00 14.08 ? 145  THR A OG1 1 
ATOM   1139 C  CG2 . THR A  1 145 ? -19.476 -18.442 23.036  1.00 15.76 ? 145  THR A CG2 1 
ATOM   1140 N  N   . TYR A  1 146 ? -23.024 -17.840 24.854  1.00 14.50 ? 146  TYR A N   1 
ATOM   1141 C  CA  . TYR A  1 146 ? -24.017 -16.744 24.803  1.00 15.54 ? 146  TYR A CA  1 
ATOM   1142 C  C   . TYR A  1 146 ? -23.976 -15.955 26.114  1.00 16.50 ? 146  TYR A C   1 
ATOM   1143 O  O   . TYR A  1 146 ? -23.912 -14.720 26.104  1.00 15.70 ? 146  TYR A O   1 
ATOM   1144 C  CB  . TYR A  1 146 ? -25.382 -17.351 24.562  1.00 15.13 ? 146  TYR A CB  1 
ATOM   1145 C  CG  . TYR A  1 146 ? -26.499 -16.361 24.386  1.00 15.88 ? 146  TYR A CG  1 
ATOM   1146 C  CD1 . TYR A  1 146 ? -27.101 -15.748 25.473  1.00 17.40 ? 146  TYR A CD1 1 
ATOM   1147 C  CD2 . TYR A  1 146 ? -27.001 -16.109 23.113  1.00 17.64 ? 146  TYR A CD2 1 
ATOM   1148 C  CE1 . TYR A  1 146 ? -28.154 -14.858 25.299  1.00 18.42 ? 146  TYR A CE1 1 
ATOM   1149 C  CE2 . TYR A  1 146 ? -28.070 -15.249 22.927  1.00 17.30 ? 146  TYR A CE2 1 
ATOM   1150 C  CZ  . TYR A  1 146 ? -28.654 -14.644 24.021  1.00 19.49 ? 146  TYR A CZ  1 
ATOM   1151 O  OH  . TYR A  1 146 ? -29.728 -13.818 23.799  1.00 21.57 ? 146  TYR A OH  1 
ATOM   1152 N  N   . LYS A  1 147 ? -23.973 -16.682 27.237  1.00 17.75 ? 147  LYS A N   1 
ATOM   1153 C  CA  . LYS A  1 147 ? -23.952 -16.044 28.580  1.00 19.17 ? 147  LYS A CA  1 
ATOM   1154 C  C   . LYS A  1 147 ? -22.643 -15.244 28.757  1.00 16.65 ? 147  LYS A C   1 
ATOM   1155 O  O   . LYS A  1 147 ? -22.673 -14.112 29.254  1.00 17.29 ? 147  LYS A O   1 
ATOM   1156 C  CB  . LYS A  1 147 ? -24.183 -17.107 29.664  1.00 21.52 ? 147  LYS A CB  1 
ATOM   1157 C  CG  . LYS A  1 147 ? -25.592 -17.681 29.726  1.00 23.71 ? 147  LYS A CG  1 
ATOM   1158 C  CD  . LYS A  1 147 ? -25.694 -18.849 30.688  1.00 28.54 ? 147  LYS A CD  1 
ATOM   1159 C  CE  . LYS A  1 147 ? -25.546 -18.383 32.118  1.00 35.70 ? 147  LYS A CE  1 
ATOM   1160 N  NZ  . LYS A  1 147 ? -25.940 -19.455 33.061  1.00 42.15 ? 147  LYS A NZ  1 
ATOM   1161 N  N   . LEU A  1 148 ? -21.512 -15.798 28.345  1.00 16.06 ? 148  LEU A N   1 
ATOM   1162 C  CA  . LEU A  1 148 ? -20.206 -15.105 28.419  1.00 16.69 ? 148  LEU A CA  1 
ATOM   1163 C  C   . LEU A  1 148 ? -20.265 -13.799 27.628  1.00 16.20 ? 148  LEU A C   1 
ATOM   1164 O  O   . LEU A  1 148 ? -19.846 -12.755 28.136  1.00 16.36 ? 148  LEU A O   1 
ATOM   1165 C  CB  . LEU A  1 148 ? -19.129 -16.029 27.858  1.00 16.65 ? 148  LEU A CB  1 
ATOM   1166 C  CG  . LEU A  1 148 ? -17.744 -15.405 27.759  1.00 17.85 ? 148  LEU A CG  1 
ATOM   1167 C  CD1 . LEU A  1 148 ? -17.246 -15.006 29.140  1.00 19.01 ? 148  LEU A CD1 1 
ATOM   1168 C  CD2 . LEU A  1 148 ? -16.791 -16.396 27.127  1.00 18.07 ? 148  LEU A CD2 1 
ATOM   1169 N  N   . ILE A  1 149 ? -20.723 -13.848 26.380  1.00 16.12 ? 149  ILE A N   1 
ATOM   1170 C  CA  . ILE A  1 149 ? -20.778 -12.626 25.523  1.00 16.93 ? 149  ILE A CA  1 
ATOM   1171 C  C   . ILE A  1 149 ? -21.722 -11.603 26.145  1.00 16.45 ? 149  ILE A C   1 
ATOM   1172 O  O   . ILE A  1 149 ? -21.394 -10.423 26.137  1.00 17.58 ? 149  ILE A O   1 
ATOM   1173 C  CB  . ILE A  1 149 ? -21.206 -12.972 24.076  1.00 17.59 ? 149  ILE A CB  1 
ATOM   1174 C  CG1 . ILE A  1 149 ? -20.169 -13.882 23.414  1.00 17.68 ? 149  ILE A CG1 1 
ATOM   1175 C  CG2 . ILE A  1 149 ? -21.421 -11.708 23.265  1.00 17.10 ? 149  ILE A CG2 1 
ATOM   1176 C  CD1 . ILE A  1 149 ? -20.664 -14.610 22.157  1.00 16.05 ? 149  ILE A CD1 1 
ATOM   1177 N  N   . ARG A  1 150 ? -22.873 -12.037 26.648  1.00 17.79 ? 150  ARG A N   1 
ATOM   1178 C  CA  . ARG A  1 150 ? -23.836 -11.123 27.302  1.00 18.19 ? 150  ARG A CA  1 
ATOM   1179 C  C   . ARG A  1 150 ? -23.173 -10.476 28.526  1.00 19.71 ? 150  ARG A C   1 
ATOM   1180 O  O   . ARG A  1 150 ? -23.391 -9.284  28.733  1.00 19.38 ? 150  ARG A O   1 
ATOM   1181 C  CB  . ARG A  1 150 ? -25.123 -11.863 27.675  1.00 18.07 ? 150  ARG A CB  1 
ATOM   1182 C  CG  . ARG A  1 150 ? -26.022 -12.183 26.486  1.00 18.95 ? 150  ARG A CG  1 
ATOM   1183 C  CD  . ARG A  1 150 ? -26.432 -10.964 25.670  1.00 18.29 ? 150  ARG A CD  1 
ATOM   1184 N  NE  . ARG A  1 150 ? -27.601 -11.277 24.858  1.00 18.43 ? 150  ARG A NE  1 
ATOM   1185 C  CZ  . ARG A  1 150 ? -27.818 -10.856 23.609  1.00 20.23 ? 150  ARG A CZ  1 
ATOM   1186 N  NH1 . ARG A  1 150 ? -26.927 -10.109 22.977  1.00 18.89 ? 150  ARG A NH1 1 
ATOM   1187 N  NH2 . ARG A  1 150 ? -28.943 -11.196 22.996  1.00 19.31 ? 150  ARG A NH2 1 
ATOM   1188 N  N   . ARG A  1 151 ? -22.352 -11.216 29.271  1.00 22.95 ? 151  ARG A N   1 
ATOM   1189 C  CA  . ARG A  1 151 ? -21.691 -10.698 30.501  1.00 24.64 ? 151  ARG A CA  1 
ATOM   1190 C  C   . ARG A  1 151 ? -20.603 -9.684  30.117  1.00 24.11 ? 151  ARG A C   1 
ATOM   1191 O  O   . ARG A  1 151 ? -20.547 -8.617  30.732  1.00 20.48 ? 151  ARG A O   1 
ATOM   1192 C  CB  . ARG A  1 151 ? -21.156 -11.878 31.303  1.00 30.32 ? 151  ARG A CB  1 
ATOM   1193 C  CG  . ARG A  1 151 ? -20.728 -11.547 32.726  1.00 40.24 ? 151  ARG A CG  1 
ATOM   1194 C  CD  . ARG A  1 151 ? -20.295 -12.795 33.498  1.00 47.76 ? 151  ARG A CD  1 
ATOM   1195 N  NE  . ARG A  1 151 ? -21.188 -13.956 33.375  1.00 52.12 ? 151  ARG A NE  1 
ATOM   1196 C  CZ  . ARG A  1 151 ? -20.872 -15.146 32.841  1.00 53.55 ? 151  ARG A CZ  1 
ATOM   1197 N  NH1 . ARG A  1 151 ? -19.659 -15.380 32.362  1.00 56.81 ? 151  ARG A NH1 1 
ATOM   1198 N  NH2 . ARG A  1 151 ? -21.777 -16.116 32.804  1.00 52.04 ? 151  ARG A NH2 1 
ATOM   1199 N  N   . LEU A  1 152 ? -19.761 -9.983  29.136  1.00 19.48 ? 152  LEU A N   1 
ATOM   1200 C  CA  . LEU A  1 152 ? -18.555 -9.166  28.862  1.00 20.84 ? 152  LEU A CA  1 
ATOM   1201 C  C   . LEU A  1 152 ? -18.784 -8.113  27.775  1.00 20.59 ? 152  LEU A C   1 
ATOM   1202 O  O   . LEU A  1 152 ? -18.024 -7.143  27.775  1.00 19.94 ? 152  LEU A O   1 
ATOM   1203 C  CB  . LEU A  1 152 ? -17.392 -10.062 28.454  1.00 23.32 ? 152  LEU A CB  1 
ATOM   1204 C  CG  . LEU A  1 152 ? -16.895 -11.070 29.478  1.00 26.62 ? 152  LEU A CG  1 
ATOM   1205 C  CD1 . LEU A  1 152 ? -15.605 -11.679 28.962  1.00 27.88 ? 152  LEU A CD1 1 
ATOM   1206 C  CD2 . LEU A  1 152 ? -16.695 -10.435 30.861  1.00 28.44 ? 152  LEU A CD2 1 
ATOM   1207 N  N   . ASP A  1 153 ? -19.800 -8.267  26.924  1.00 19.99 ? 153  ASP A N   1 
ATOM   1208 C  CA  . ASP A  1 153 ? -20.071 -7.328  25.802  1.00 17.65 ? 153  ASP A CA  1 
ATOM   1209 C  C   . ASP A  1 153 ? -21.584 -7.267  25.570  1.00 19.26 ? 153  ASP A C   1 
ATOM   1210 O  O   . ASP A  1 153 ? -22.101 -7.661  24.522  1.00 16.70 ? 153  ASP A O   1 
ATOM   1211 C  CB  . ASP A  1 153 ? -19.202 -7.693  24.598  1.00 17.64 ? 153  ASP A CB  1 
ATOM   1212 C  CG  . ASP A  1 153 ? -18.953 -6.565  23.611  1.00 18.31 ? 153  ASP A CG  1 
ATOM   1213 O  OD1 . ASP A  1 153 ? -19.504 -5.442  23.824  1.00 18.37 ? 153  ASP A OD1 1 
ATOM   1214 O  OD2 . ASP A  1 153 ? -18.248 -6.799  22.606  1.00 16.27 ? 153  ASP A OD2 1 
ATOM   1215 N  N   . PRO A  1 154 ? -22.354 -6.757  26.561  1.00 21.55 ? 154  PRO A N   1 
ATOM   1216 C  CA  . PRO A  1 154 ? -23.816 -6.840  26.506  1.00 20.79 ? 154  PRO A CA  1 
ATOM   1217 C  C   . PRO A  1 154 ? -24.504 -6.112  25.334  1.00 20.78 ? 154  PRO A C   1 
ATOM   1218 O  O   . PRO A  1 154 ? -25.614 -6.524  24.944  1.00 23.59 ? 154  PRO A O   1 
ATOM   1219 C  CB  . PRO A  1 154 ? -24.241 -6.218  27.855  1.00 23.07 ? 154  PRO A CB  1 
ATOM   1220 C  CG  . PRO A  1 154 ? -23.084 -5.366  28.276  1.00 22.77 ? 154  PRO A CG  1 
ATOM   1221 C  CD  . PRO A  1 154 ? -21.855 -6.122  27.794  1.00 22.12 ? 154  PRO A CD  1 
ATOM   1222 N  N   . ASN A  1 155 ? -23.875 -5.082  24.771  1.00 20.85 ? 155  ASN A N   1 
ATOM   1223 C  CA  . ASN A  1 155 ? -24.491 -4.275  23.688  1.00 24.51 ? 155  ASN A CA  1 
ATOM   1224 C  C   . ASN A  1 155 ? -24.183 -4.865  22.314  1.00 24.63 ? 155  ASN A C   1 
ATOM   1225 O  O   . ASN A  1 155 ? -24.640 -4.272  21.316  1.00 23.93 ? 155  ASN A O   1 
ATOM   1226 C  CB  . ASN A  1 155 ? -24.046 -2.823  23.755  1.00 28.90 ? 155  ASN A CB  1 
ATOM   1227 C  CG  . ASN A  1 155 ? -24.496 -2.201  25.060  1.00 31.50 ? 155  ASN A CG  1 
ATOM   1228 O  OD1 . ASN A  1 155 ? -25.507 -2.615  25.637  1.00 35.59 ? 155  ASN A OD1 1 
ATOM   1229 N  ND2 . ASN A  1 155 ? -23.730 -1.236  25.532  1.00 35.75 ? 155  ASN A ND2 1 
ATOM   1230 N  N   . SER A  1 156 ? -23.426 -5.960  22.245  1.00 21.01 ? 156  SER A N   1 
ATOM   1231 C  CA  . SER A  1 156 ? -23.035 -6.557  20.941  1.00 19.72 ? 156  SER A CA  1 
ATOM   1232 C  C   . SER A  1 156 ? -24.138 -7.498  20.458  1.00 17.87 ? 156  SER A C   1 
ATOM   1233 O  O   . SER A  1 156 ? -24.808 -8.142  21.296  1.00 20.22 ? 156  SER A O   1 
ATOM   1234 C  CB  . SER A  1 156 ? -21.714 -7.283  21.041  1.00 21.81 ? 156  SER A CB  1 
ATOM   1235 O  OG  . SER A  1 156 ? -21.799 -8.284  22.055  1.00 22.49 ? 156  SER A OG  1 
ATOM   1236 N  N   . GLN A  1 157 ? -24.248 -7.663  19.143  1.00 15.12 ? 157  GLN A N   1 
ATOM   1237 C  CA  . GLN A  1 157 ? -25.175 -8.658  18.549  1.00 14.06 ? 157  GLN A CA  1 
ATOM   1238 C  C   . GLN A  1 157 ? -24.539 -10.041 18.623  1.00 13.67 ? 157  GLN A C   1 
ATOM   1239 O  O   . GLN A  1 157 ? -23.314 -10.162 18.434  1.00 13.53 ? 157  GLN A O   1 
ATOM   1240 C  CB  . GLN A  1 157 ? -25.482 -8.328  17.092  1.00 15.76 ? 157  GLN A CB  1 
ATOM   1241 C  CG  . GLN A  1 157 ? -26.244 -7.031  16.947  1.00 15.81 ? 157  GLN A CG  1 
ATOM   1242 C  CD  . GLN A  1 157 ? -26.788 -6.799  15.562  1.00 16.70 ? 157  GLN A CD  1 
ATOM   1243 O  OE1 . GLN A  1 157 ? -27.993 -6.611  15.398  1.00 20.49 ? 157  GLN A OE1 1 
ATOM   1244 N  NE2 . GLN A  1 157 ? -25.909 -6.808  14.571  1.00 15.01 ? 157  GLN A NE2 1 
ATOM   1245 N  N   . ILE A  1 158 ? -25.373 -11.046 18.848  1.00 13.24 ? 158  ILE A N   1 
ATOM   1246 C  CA  . ILE A  1 158 ? -24.995 -12.484 18.794  1.00 13.51 ? 158  ILE A CA  1 
ATOM   1247 C  C   . ILE A  1 158 ? -25.685 -13.095 17.588  1.00 13.12 ? 158  ILE A C   1 
ATOM   1248 O  O   . ILE A  1 158 ? -26.912 -12.935 17.480  1.00 13.11 ? 158  ILE A O   1 
ATOM   1249 C  CB  . ILE A  1 158 ? -25.400 -13.203 20.087  1.00 13.72 ? 158  ILE A CB  1 
ATOM   1250 C  CG1 . ILE A  1 158 ? -24.609 -12.629 21.258  1.00 14.60 ? 158  ILE A CG1 1 
ATOM   1251 C  CG2 . ILE A  1 158 ? -25.194 -14.700 19.925  1.00 13.84 ? 158  ILE A CG2 1 
ATOM   1252 C  CD1 . ILE A  1 158 ? -24.991 -13.152 22.600  1.00 14.49 ? 158  ILE A CD1 1 
ATOM   1253 N  N   . ILE A  1 159 ? -24.896 -13.728 16.725  1.00 13.27 ? 159  ILE A N   1 
ATOM   1254 C  CA  . ILE A  1 159 ? -25.339 -14.220 15.400  1.00 12.66 ? 159  ILE A CA  1 
ATOM   1255 C  C   . ILE A  1 159 ? -25.248 -15.749 15.380  1.00 12.00 ? 159  ILE A C   1 
ATOM   1256 O  O   . ILE A  1 159 ? -24.201 -16.305 15.726  1.00 12.00 ? 159  ILE A O   1 
ATOM   1257 C  CB  . ILE A  1 159 ? -24.514 -13.587 14.269  1.00 13.94 ? 159  ILE A CB  1 
ATOM   1258 C  CG1 . ILE A  1 159 ? -24.660 -12.059 14.232  1.00 15.44 ? 159  ILE A CG1 1 
ATOM   1259 C  CG2 . ILE A  1 159 ? -24.914 -14.207 12.952  1.00 14.45 ? 159  ILE A CG2 1 
ATOM   1260 C  CD1 . ILE A  1 159 ? -23.579 -11.328 14.930  1.00 18.23 ? 159  ILE A CD1 1 
ATOM   1261 N  N   . GLY A  1 160 ? -26.309 -16.420 14.932  1.00 11.20 ? 160  GLY A N   1 
ATOM   1262 C  CA  . GLY A  1 160 ? -26.248 -17.855 14.662  1.00 10.58 ? 160  GLY A CA  1 
ATOM   1263 C  C   . GLY A  1 160 ? -27.597 -18.424 14.265  1.00 9.82  ? 160  GLY A C   1 
ATOM   1264 O  O   . GLY A  1 160 ? -28.572 -17.706 14.147  1.00 10.11 ? 160  GLY A O   1 
ATOM   1265 N  N   . PRO A  1 161 ? -27.697 -19.741 14.034  1.00 10.85 ? 161  PRO A N   1 
ATOM   1266 C  CA  . PRO A  1 161 ? -26.595 -20.680 14.275  1.00 12.47 ? 161  PRO A CA  1 
ATOM   1267 C  C   . PRO A  1 161 ? -25.598 -20.889 13.125  1.00 11.90 ? 161  PRO A C   1 
ATOM   1268 O  O   . PRO A  1 161 ? -24.676 -21.676 13.257  1.00 11.48 ? 161  PRO A O   1 
ATOM   1269 C  CB  . PRO A  1 161 ? -27.382 -21.973 14.530  1.00 12.02 ? 161  PRO A CB  1 
ATOM   1270 C  CG  . PRO A  1 161 ? -28.591 -21.851 13.632  1.00 11.49 ? 161  PRO A CG  1 
ATOM   1271 C  CD  . PRO A  1 161 ? -28.957 -20.386 13.648  1.00 11.20 ? 161  PRO A CD  1 
ATOM   1272 N  N   . SER A  1 162 ? -25.793 -20.188 12.001  1.00 11.47 ? 162  SER A N   1 
ATOM   1273 C  CA  . SER A  1 162 ? -24.895 -20.220 10.833  1.00 10.72 ? 162  SER A CA  1 
ATOM   1274 C  C   . SER A  1 162 ? -24.824 -21.616 10.216  1.00 10.36 ? 162  SER A C   1 
ATOM   1275 O  O   . SER A  1 162 ? -23.744 -22.061 9.877   1.00 10.13 ? 162  SER A O   1 
ATOM   1276 C  CB  . SER A  1 162 ? -23.521 -19.715 11.204  1.00 11.46 ? 162  SER A CB  1 
ATOM   1277 O  OG  . SER A  1 162 ? -23.595 -18.335 11.577  1.00 11.46 ? 162  SER A OG  1 
ATOM   1278 N  N   . TYR A  1 163 ? -25.954 -22.270 10.004  1.00 10.50 ? 163  TYR A N   1 
ATOM   1279 C  CA  . TYR A  1 163 ? -25.961 -23.611 9.395   1.00 11.18 ? 163  TYR A CA  1 
ATOM   1280 C  C   . TYR A  1 163 ? -25.373 -23.602 7.990   1.00 11.98 ? 163  TYR A C   1 
ATOM   1281 O  O   . TYR A  1 163 ? -25.502 -22.591 7.254   1.00 12.34 ? 163  TYR A O   1 
ATOM   1282 C  CB  . TYR A  1 163 ? -27.402 -24.098 9.238   1.00 11.64 ? 163  TYR A CB  1 
ATOM   1283 C  CG  . TYR A  1 163 ? -28.117 -24.394 10.516  1.00 12.06 ? 163  TYR A CG  1 
ATOM   1284 C  CD1 . TYR A  1 163 ? -27.494 -25.042 11.558  1.00 12.88 ? 163  TYR A CD1 1 
ATOM   1285 C  CD2 . TYR A  1 163 ? -29.467 -24.096 10.643  1.00 13.39 ? 163  TYR A CD2 1 
ATOM   1286 C  CE1 . TYR A  1 163 ? -28.165 -25.350 12.731  1.00 13.83 ? 163  TYR A CE1 1 
ATOM   1287 C  CE2 . TYR A  1 163 ? -30.139 -24.367 11.823  1.00 14.45 ? 163  TYR A CE2 1 
ATOM   1288 C  CZ  . TYR A  1 163 ? -29.490 -24.996 12.861  1.00 14.25 ? 163  TYR A CZ  1 
ATOM   1289 O  OH  . TYR A  1 163 ? -30.205 -25.317 13.959  1.00 18.30 ? 163  TYR A OH  1 
ATOM   1290 N  N   . SER A  1 164 ? -24.794 -24.748 7.623   1.00 12.33 ? 164  SER A N   1 
ATOM   1291 C  CA  A SER A  1 164 ? -24.319 -25.084 6.267   0.80 13.42 ? 164  SER A CA  1 
ATOM   1292 C  CA  B SER A  1 164 ? -24.296 -25.014 6.253   0.20 12.33 ? 164  SER A CA  1 
ATOM   1293 C  C   . SER A  1 164 ? -25.451 -24.807 5.265   1.00 12.91 ? 164  SER A C   1 
ATOM   1294 O  O   . SER A  1 164 ? -25.219 -24.189 4.224   1.00 13.22 ? 164  SER A O   1 
ATOM   1295 C  CB  A SER A  1 164 ? -23.869 -26.549 6.314   0.80 14.62 ? 164  SER A CB  1 
ATOM   1296 C  CB  B SER A  1 164 ? -23.677 -26.390 6.157   0.20 12.17 ? 164  SER A CB  1 
ATOM   1297 O  OG  A SER A  1 164 ? -23.448 -27.037 5.057   0.80 19.49 ? 164  SER A OG  1 
ATOM   1298 O  OG  B SER A  1 164 ? -24.665 -27.403 6.229   0.20 11.86 ? 164  SER A OG  1 
ATOM   1299 N  N   . TYR A  1 165 ? -26.653 -25.271 5.611   1.00 12.35 ? 165  TYR A N   1 
ATOM   1300 C  CA  . TYR A  1 165 ? -27.906 -25.128 4.836   1.00 12.80 ? 165  TYR A CA  1 
ATOM   1301 C  C   . TYR A  1 165 ? -29.027 -24.817 5.807   1.00 12.83 ? 165  TYR A C   1 
ATOM   1302 O  O   . TYR A  1 165 ? -29.100 -25.410 6.910   1.00 11.89 ? 165  TYR A O   1 
ATOM   1303 C  CB  . TYR A  1 165 ? -28.215 -26.415 4.052   1.00 12.98 ? 165  TYR A CB  1 
ATOM   1304 C  CG  . TYR A  1 165 ? -27.500 -26.567 2.729   1.00 12.99 ? 165  TYR A CG  1 
ATOM   1305 C  CD1 . TYR A  1 165 ? -26.191 -26.999 2.662   1.00 12.83 ? 165  TYR A CD1 1 
ATOM   1306 C  CD2 . TYR A  1 165 ? -28.164 -26.353 1.519   1.00 15.28 ? 165  TYR A CD2 1 
ATOM   1307 C  CE1 . TYR A  1 165 ? -25.532 -27.157 1.455   1.00 13.67 ? 165  TYR A CE1 1 
ATOM   1308 C  CE2 . TYR A  1 165 ? -27.519 -26.507 0.299   1.00 14.58 ? 165  TYR A CE2 1 
ATOM   1309 C  CZ  . TYR A  1 165 ? -26.200 -26.922 0.267   1.00 13.73 ? 165  TYR A CZ  1 
ATOM   1310 O  OH  . TYR A  1 165 ? -25.517 -27.054 -0.907  1.00 18.44 ? 165  TYR A OH  1 
ATOM   1311 N  N   . TYR A  1 166 ? -29.989 -24.008 5.368   1.00 13.11 ? 166  TYR A N   1 
ATOM   1312 C  CA  . TYR A  1 166 ? -31.261 -23.901 6.103   1.00 12.71 ? 166  TYR A CA  1 
ATOM   1313 C  C   . TYR A  1 166 ? -31.908 -25.286 6.170   1.00 13.10 ? 166  TYR A C   1 
ATOM   1314 O  O   . TYR A  1 166 ? -31.950 -26.011 5.189   1.00 13.07 ? 166  TYR A O   1 
ATOM   1315 C  CB  . TYR A  1 166 ? -32.202 -22.884 5.468   1.00 13.50 ? 166  TYR A CB  1 
ATOM   1316 C  CG  . TYR A  1 166 ? -33.416 -22.687 6.325   1.00 14.03 ? 166  TYR A CG  1 
ATOM   1317 C  CD1 . TYR A  1 166 ? -33.356 -21.844 7.432   1.00 13.53 ? 166  TYR A CD1 1 
ATOM   1318 C  CD2 . TYR A  1 166 ? -34.580 -23.396 6.100   1.00 13.48 ? 166  TYR A CD2 1 
ATOM   1319 C  CE1 . TYR A  1 166 ? -34.429 -21.696 8.277   1.00 14.73 ? 166  TYR A CE1 1 
ATOM   1320 C  CE2 . TYR A  1 166 ? -35.670 -23.235 6.932   1.00 14.34 ? 166  TYR A CE2 1 
ATOM   1321 C  CZ  . TYR A  1 166 ? -35.596 -22.399 8.035   1.00 15.08 ? 166  TYR A CZ  1 
ATOM   1322 O  OH  . TYR A  1 166 ? -36.685 -22.268 8.850   1.00 15.19 ? 166  TYR A OH  1 
ATOM   1323 N  N   . ASN A  1 167 ? -32.367 -25.646 7.357   1.00 11.99 ? 167  ASN A N   1 
ATOM   1324 C  CA  . ASN A  1 167 ? -33.203 -26.850 7.526   1.00 12.75 ? 167  ASN A CA  1 
ATOM   1325 C  C   . ASN A  1 167 ? -34.240 -26.516 8.582   1.00 11.74 ? 167  ASN A C   1 
ATOM   1326 O  O   . ASN A  1 167 ? -33.875 -26.130 9.676   1.00 11.73 ? 167  ASN A O   1 
ATOM   1327 C  CB  . ASN A  1 167 ? -32.400 -28.103 7.863   1.00 12.64 ? 167  ASN A CB  1 
ATOM   1328 C  CG  . ASN A  1 167 ? -33.357 -29.274 7.987   1.00 13.17 ? 167  ASN A CG  1 
ATOM   1329 O  OD1 . ASN A  1 167 ? -33.846 -29.523 9.070   1.00 13.92 ? 167  ASN A OD1 1 
ATOM   1330 N  ND2 . ASN A  1 167 ? -33.676 -29.929 6.877   1.00 14.12 ? 167  ASN A ND2 1 
ATOM   1331 N  N   . HIS A  1 168 ? -35.506 -26.710 8.246   1.00 11.49 ? 168  HIS A N   1 
ATOM   1332 C  CA  . HIS A  1 168 ? -36.627 -26.401 9.144   1.00 12.30 ? 168  HIS A CA  1 
ATOM   1333 C  C   . HIS A  1 168 ? -36.469 -27.126 10.478  1.00 12.02 ? 168  HIS A C   1 
ATOM   1334 O  O   . HIS A  1 168 ? -36.739 -26.514 11.528  1.00 11.80 ? 168  HIS A O   1 
ATOM   1335 C  CB  . HIS A  1 168 ? -37.938 -26.743 8.446   1.00 13.62 ? 168  HIS A CB  1 
ATOM   1336 C  CG  . HIS A  1 168 ? -39.096 -26.645 9.367   1.00 14.93 ? 168  HIS A CG  1 
ATOM   1337 N  ND1 . HIS A  1 168 ? -39.728 -25.451 9.597   1.00 13.80 ? 168  HIS A ND1 1 
ATOM   1338 C  CD2 . HIS A  1 168 ? -39.662 -27.569 10.171  1.00 16.26 ? 168  HIS A CD2 1 
ATOM   1339 C  CE1 . HIS A  1 168 ? -40.728 -25.657 10.445  1.00 16.03 ? 168  HIS A CE1 1 
ATOM   1340 N  NE2 . HIS A  1 168 ? -40.689 -26.959 10.840  1.00 15.89 ? 168  HIS A NE2 1 
ATOM   1341 N  N   . TYR A  1 169 ? -36.124 -28.406 10.433  1.00 11.97 ? 169  TYR A N   1 
ATOM   1342 C  CA  . TYR A  1 169 ? -36.134 -29.285 11.625  1.00 13.14 ? 169  TYR A CA  1 
ATOM   1343 C  C   . TYR A  1 169 ? -34.965 -28.895 12.536  1.00 13.17 ? 169  TYR A C   1 
ATOM   1344 O  O   . TYR A  1 169 ? -35.173 -28.747 13.760  1.00 13.71 ? 169  TYR A O   1 
ATOM   1345 C  CB  . TYR A  1 169 ? -36.213 -30.761 11.206  1.00 13.12 ? 169  TYR A CB  1 
ATOM   1346 C  CG  . TYR A  1 169 ? -37.542 -31.009 10.550  1.00 14.77 ? 169  TYR A CG  1 
ATOM   1347 C  CD1 . TYR A  1 169 ? -38.692 -31.108 11.319  1.00 15.98 ? 169  TYR A CD1 1 
ATOM   1348 C  CD2 . TYR A  1 169 ? -37.672 -31.000 9.168   1.00 13.65 ? 169  TYR A CD2 1 
ATOM   1349 C  CE1 . TYR A  1 169 ? -39.940 -31.218 10.727  1.00 15.99 ? 169  TYR A CE1 1 
ATOM   1350 C  CE2 . TYR A  1 169 ? -38.912 -31.080 8.562   1.00 14.61 ? 169  TYR A CE2 1 
ATOM   1351 C  CZ  . TYR A  1 169 ? -40.039 -31.216 9.342   1.00 16.01 ? 169  TYR A CZ  1 
ATOM   1352 O  OH  . TYR A  1 169 ? -41.242 -31.277 8.711   1.00 18.09 ? 169  TYR A OH  1 
ATOM   1353 N  N   . ASN A  1 170 ? -33.786 -28.666 11.957  1.00 13.53 ? 170  ASN A N   1 
ATOM   1354 C  CA  . ASN A  1 170 ? -32.640 -28.183 12.757  1.00 14.75 ? 170  ASN A CA  1 
ATOM   1355 C  C   . ASN A  1 170 ? -33.030 -26.855 13.392  1.00 13.17 ? 170  ASN A C   1 
ATOM   1356 O  O   . ASN A  1 170 ? -32.813 -26.653 14.593  1.00 13.65 ? 170  ASN A O   1 
ATOM   1357 C  CB  . ASN A  1 170 ? -31.365 -28.044 11.924  1.00 14.67 ? 170  ASN A CB  1 
ATOM   1358 C  CG  . ASN A  1 170 ? -30.547 -29.304 11.815  1.00 16.32 ? 170  ASN A CG  1 
ATOM   1359 O  OD1 . ASN A  1 170 ? -30.629 -30.179 12.692  1.00 16.06 ? 170  ASN A OD1 1 
ATOM   1360 N  ND2 . ASN A  1 170 ? -29.739 -29.378 10.761  1.00 14.05 ? 170  ASN A ND2 1 
ATOM   1361 N  N   . MET A  1 171 ? -33.518 -25.920 12.586  1.00 13.93 ? 171  MET A N   1 
ATOM   1362 C  CA  . MET A  1 171 ? -33.823 -24.559 13.090  1.00 14.24 ? 171  MET A CA  1 
ATOM   1363 C  C   . MET A  1 171 ? -34.922 -24.644 14.163  1.00 13.60 ? 171  MET A C   1 
ATOM   1364 O  O   . MET A  1 171 ? -34.809 -23.934 15.157  1.00 12.89 ? 171  MET A O   1 
ATOM   1365 C  CB  . MET A  1 171 ? -34.197 -23.609 11.954  1.00 14.25 ? 171  MET A CB  1 
ATOM   1366 C  CG  . MET A  1 171 ? -34.342 -22.175 12.408  1.00 14.78 ? 171  MET A CG  1 
ATOM   1367 S  SD  . MET A  1 171 ? -32.749 -21.478 12.826  1.00 15.82 ? 171  MET A SD  1 
ATOM   1368 C  CE  . MET A  1 171 ? -32.090 -21.148 11.187  1.00 16.14 ? 171  MET A CE  1 
ATOM   1369 N  N   . ASN A  1 172 ? -35.934 -25.499 14.003  1.00 15.13 ? 172  ASN A N   1 
ATOM   1370 C  CA  . ASN A  1 172 ? -37.004 -25.668 15.023  1.00 16.76 ? 172  ASN A CA  1 
ATOM   1371 C  C   . ASN A  1 172 ? -36.389 -26.121 16.359  1.00 15.74 ? 172  ASN A C   1 
ATOM   1372 O  O   . ASN A  1 172 ? -36.665 -25.501 17.388  1.00 16.25 ? 172  ASN A O   1 
ATOM   1373 C  CB  . ASN A  1 172 ? -38.087 -26.644 14.552  1.00 18.44 ? 172  ASN A CB  1 
ATOM   1374 C  CG  . ASN A  1 172 ? -39.107 -26.907 15.646  1.00 20.26 ? 172  ASN A CG  1 
ATOM   1375 O  OD1 . ASN A  1 172 ? -39.805 -25.983 16.056  1.00 22.94 ? 172  ASN A OD1 1 
ATOM   1376 N  ND2 . ASN A  1 172 ? -39.101 -28.126 16.178  1.00 21.79 ? 172  ASN A ND2 1 
ATOM   1377 N  N   . ALA A  1 173 ? -35.551 -27.156 16.349  1.00 14.80 ? 173  ALA A N   1 
ATOM   1378 C  CA  . ALA A  1 173 ? -34.868 -27.717 17.546  1.00 16.12 ? 173  ALA A CA  1 
ATOM   1379 C  C   . ALA A  1 173 ? -34.040 -26.629 18.239  1.00 15.70 ? 173  ALA A C   1 
ATOM   1380 O  O   . ALA A  1 173 ? -34.142 -26.445 19.457  1.00 16.84 ? 173  ALA A O   1 
ATOM   1381 C  CB  . ALA A  1 173 ? -33.995 -28.861 17.135  1.00 15.91 ? 173  ALA A CB  1 
ATOM   1382 N  N   . PHE A  1 174 ? -33.296 -25.852 17.460  1.00 16.64 ? 174  PHE A N   1 
ATOM   1383 C  CA  . PHE A  1 174 ? -32.401 -24.793 17.966  1.00 15.43 ? 174  PHE A CA  1 
ATOM   1384 C  C   . PHE A  1 174 ? -33.223 -23.678 18.614  1.00 15.10 ? 174  PHE A C   1 
ATOM   1385 O  O   . PHE A  1 174 ? -32.899 -23.274 19.767  1.00 16.05 ? 174  PHE A O   1 
ATOM   1386 C  CB  . PHE A  1 174 ? -31.494 -24.285 16.837  1.00 15.35 ? 174  PHE A CB  1 
ATOM   1387 C  CG  . PHE A  1 174 ? -30.581 -23.153 17.248  1.00 14.32 ? 174  PHE A CG  1 
ATOM   1388 C  CD1 . PHE A  1 174 ? -29.584 -23.356 18.194  1.00 14.81 ? 174  PHE A CD1 1 
ATOM   1389 C  CD2 . PHE A  1 174 ? -30.763 -21.873 16.741  1.00 14.98 ? 174  PHE A CD2 1 
ATOM   1390 C  CE1 . PHE A  1 174 ? -28.771 -22.305 18.586  1.00 13.40 ? 174  PHE A CE1 1 
ATOM   1391 C  CE2 . PHE A  1 174 ? -29.940 -20.831 17.141  1.00 14.65 ? 174  PHE A CE2 1 
ATOM   1392 C  CZ  . PHE A  1 174 ? -28.959 -21.051 18.078  1.00 13.86 ? 174  PHE A CZ  1 
ATOM   1393 N  N   . LEU A  1 175 ? -34.242 -23.164 17.919  1.00 15.26 ? 175  LEU A N   1 
ATOM   1394 C  CA  . LEU A  1 175 ? -35.023 -22.010 18.417  1.00 16.41 ? 175  LEU A CA  1 
ATOM   1395 C  C   . LEU A  1 175 ? -35.830 -22.455 19.637  1.00 16.37 ? 175  LEU A C   1 
ATOM   1396 O  O   . LEU A  1 175 ? -36.012 -21.638 20.536  1.00 17.50 ? 175  LEU A O   1 
ATOM   1397 C  CB  . LEU A  1 175 ? -35.885 -21.410 17.303  1.00 16.39 ? 175  LEU A CB  1 
ATOM   1398 C  CG  . LEU A  1 175 ? -35.088 -20.756 16.178  1.00 17.26 ? 175  LEU A CG  1 
ATOM   1399 C  CD1 . LEU A  1 175 ? -36.008 -20.190 15.124  1.00 18.10 ? 175  LEU A CD1 1 
ATOM   1400 C  CD2 . LEU A  1 175 ? -34.129 -19.693 16.690  1.00 17.72 ? 175  LEU A CD2 1 
ATOM   1401 N  N   . ASN A  1 176 ? -36.309 -23.691 19.645  1.00 17.81 ? 176  ASN A N   1 
ATOM   1402 C  CA  . ASN A  1 176 ? -37.017 -24.257 20.814  1.00 18.91 ? 176  ASN A CA  1 
ATOM   1403 C  C   . ASN A  1 176 ? -36.076 -24.257 22.016  1.00 18.93 ? 176  ASN A C   1 
ATOM   1404 O  O   . ASN A  1 176 ? -36.493 -23.799 23.099  1.00 18.16 ? 176  ASN A O   1 
ATOM   1405 C  CB  . ASN A  1 176 ? -37.570 -25.660 20.551  1.00 21.52 ? 176  ASN A CB  1 
ATOM   1406 C  CG  . ASN A  1 176 ? -39.032 -25.603 20.164  1.00 24.18 ? 176  ASN A CG  1 
ATOM   1407 O  OD1 . ASN A  1 176 ? -39.881 -25.381 21.005  1.00 25.64 ? 176  ASN A OD1 1 
ATOM   1408 N  ND2 . ASN A  1 176 ? -39.337 -25.810 18.900  1.00 27.49 ? 176  ASN A ND2 1 
ATOM   1409 N  N   . PHE A  1 177 ? -34.835 -24.718 21.836  1.00 17.76 ? 177  PHE A N   1 
ATOM   1410 C  CA  . PHE A  1 177 ? -33.824 -24.715 22.917  1.00 18.23 ? 177  PHE A CA  1 
ATOM   1411 C  C   . PHE A  1 177 ? -33.568 -23.275 23.363  1.00 17.78 ? 177  PHE A C   1 
ATOM   1412 O  O   . PHE A  1 177 ? -33.518 -22.993 24.561  1.00 19.89 ? 177  PHE A O   1 
ATOM   1413 C  CB  . PHE A  1 177 ? -32.511 -25.345 22.468  1.00 17.60 ? 177  PHE A CB  1 
ATOM   1414 C  CG  . PHE A  1 177 ? -31.434 -25.212 23.505  1.00 18.74 ? 177  PHE A CG  1 
ATOM   1415 C  CD1 . PHE A  1 177 ? -31.377 -26.086 24.583  1.00 20.70 ? 177  PHE A CD1 1 
ATOM   1416 C  CD2 . PHE A  1 177 ? -30.506 -24.196 23.426  1.00 19.31 ? 177  PHE A CD2 1 
ATOM   1417 C  CE1 . PHE A  1 177 ? -30.389 -25.951 25.544  1.00 20.36 ? 177  PHE A CE1 1 
ATOM   1418 C  CE2 . PHE A  1 177 ? -29.530 -24.065 24.395  1.00 20.04 ? 177  PHE A CE2 1 
ATOM   1419 C  CZ  . PHE A  1 177 ? -29.478 -24.927 25.457  1.00 19.86 ? 177  PHE A CZ  1 
ATOM   1420 N  N   . CYS A  1 178 ? -33.362 -22.371 22.406  1.00 18.38 ? 178  CYS A N   1 
ATOM   1421 C  CA  . CYS A  1 178 ? -33.007 -20.963 22.683  1.00 18.47 ? 178  CYS A CA  1 
ATOM   1422 C  C   . CYS A  1 178 ? -34.161 -20.283 23.432  1.00 19.39 ? 178  CYS A C   1 
ATOM   1423 O  O   . CYS A  1 178 ? -33.906 -19.498 24.356  1.00 19.98 ? 178  CYS A O   1 
ATOM   1424 C  CB  . CYS A  1 178 ? -32.650 -20.210 21.401  1.00 18.24 ? 178  CYS A CB  1 
ATOM   1425 S  SG  . CYS A  1 178 ? -31.037 -20.682 20.731  1.00 17.33 ? 178  CYS A SG  1 
ATOM   1426 N  N   . ARG A  1 179 ? -35.403 -20.550 23.042  1.00 18.91 ? 179  ARG A N   1 
ATOM   1427 C  CA  . ARG A  1 179 ? -36.570 -19.912 23.677  1.00 21.59 ? 179  ARG A CA  1 
ATOM   1428 C  C   . ARG A  1 179 ? -36.673 -20.411 25.132  1.00 21.43 ? 179  ARG A C   1 
ATOM   1429 O  O   . ARG A  1 179 ? -36.810 -19.550 26.028  1.00 21.58 ? 179  ARG A O   1 
ATOM   1430 C  CB  . ARG A  1 179 ? -37.825 -20.192 22.853  1.00 25.47 ? 179  ARG A CB  1 
ATOM   1431 C  CG  . ARG A  1 179 ? -39.100 -19.743 23.539  1.00 28.13 ? 179  ARG A CG  1 
ATOM   1432 C  CD  . ARG A  1 179 ? -40.294 -20.224 22.756  1.00 31.14 ? 179  ARG A CD  1 
ATOM   1433 N  NE  . ARG A  1 179 ? -40.491 -21.670 22.850  1.00 35.58 ? 179  ARG A NE  1 
ATOM   1434 C  CZ  . ARG A  1 179 ? -41.620 -22.304 22.523  1.00 34.24 ? 179  ARG A CZ  1 
ATOM   1435 N  NH1 . ARG A  1 179 ? -41.707 -23.614 22.659  1.00 38.65 ? 179  ARG A NH1 1 
ATOM   1436 N  NH2 . ARG A  1 179 ? -42.677 -21.634 22.093  1.00 35.06 ? 179  ARG A NH2 1 
ATOM   1437 N  N   . ALA A  1 180 ? -36.546 -21.721 25.345  1.00 21.32 ? 180  ALA A N   1 
ATOM   1438 C  CA  . ALA A  1 180 ? -36.573 -22.377 26.671  1.00 24.14 ? 180  ALA A CA  1 
ATOM   1439 C  C   . ALA A  1 180 ? -35.477 -21.809 27.590  1.00 26.84 ? 180  ALA A C   1 
ATOM   1440 O  O   . ALA A  1 180 ? -35.710 -21.742 28.816  1.00 28.17 ? 180  ALA A O   1 
ATOM   1441 C  CB  . ALA A  1 180 ? -36.434 -23.870 26.529  1.00 25.05 ? 180  ALA A CB  1 
ATOM   1442 N  N   . ASN A  1 181 ? -34.323 -21.408 27.047  1.00 24.18 ? 181  ASN A N   1 
ATOM   1443 C  CA  . ASN A  1 181 ? -33.130 -21.054 27.854  1.00 22.92 ? 181  ASN A CA  1 
ATOM   1444 C  C   . ASN A  1 181 ? -32.748 -19.573 27.737  1.00 21.47 ? 181  ASN A C   1 
ATOM   1445 O  O   . ASN A  1 181 ? -31.631 -19.229 28.153  1.00 23.46 ? 181  ASN A O   1 
ATOM   1446 C  CB  . ASN A  1 181 ? -31.961 -21.963 27.474  1.00 22.20 ? 181  ASN A CB  1 
ATOM   1447 C  CG  . ASN A  1 181 ? -32.161 -23.389 27.928  1.00 23.18 ? 181  ASN A CG  1 
ATOM   1448 O  OD1 . ASN A  1 181 ? -31.810 -23.733 29.060  1.00 21.92 ? 181  ASN A OD1 1 
ATOM   1449 N  ND2 . ASN A  1 181 ? -32.665 -24.236 27.042  1.00 22.42 ? 181  ASN A ND2 1 
ATOM   1450 N  N   A ASN A  1 182 ? -33.615 -18.747 27.146  0.50 21.05 ? 182  ASN A N   1 
ATOM   1451 N  N   B ASN A  1 182 ? -33.632 -18.725 27.202  0.50 19.98 ? 182  ASN A N   1 
ATOM   1452 C  CA  A ASN A  1 182 ? -33.443 -17.271 27.044  0.50 22.49 ? 182  ASN A CA  1 
ATOM   1453 C  CA  B ASN A  1 182 ? -33.400 -17.261 27.038  0.50 20.60 ? 182  ASN A CA  1 
ATOM   1454 C  C   A ASN A  1 182 ? -32.118 -16.941 26.329  0.50 20.62 ? 182  ASN A C   1 
ATOM   1455 C  C   B ASN A  1 182 ? -32.009 -17.052 26.418  0.50 19.38 ? 182  ASN A C   1 
ATOM   1456 O  O   A ASN A  1 182 ? -31.452 -15.978 26.756  0.50 19.58 ? 182  ASN A O   1 
ATOM   1457 O  O   B ASN A  1 182 ? -31.166 -16.347 27.008  0.50 17.38 ? 182  ASN A O   1 
ATOM   1458 C  CB  A ASN A  1 182 ? -33.505 -16.606 28.425  0.50 24.22 ? 182  ASN A CB  1 
ATOM   1459 C  CB  B ASN A  1 182 ? -33.588 -16.502 28.356  0.50 20.96 ? 182  ASN A CB  1 
ATOM   1460 C  CG  A ASN A  1 182 ? -33.805 -15.126 28.346  0.50 26.20 ? 182  ASN A CG  1 
ATOM   1461 C  CG  B ASN A  1 182 ? -34.964 -16.734 28.938  0.50 21.20 ? 182  ASN A CG  1 
ATOM   1462 O  OD1 A ASN A  1 182 ? -34.446 -14.672 27.404  0.50 28.47 ? 182  ASN A OD1 1 
ATOM   1463 O  OD1 B ASN A  1 182 ? -35.963 -16.606 28.240  0.50 20.85 ? 182  ASN A OD1 1 
ATOM   1464 N  ND2 A ASN A  1 182 ? -33.342 -14.365 29.327  0.50 29.59 ? 182  ASN A ND2 1 
ATOM   1465 N  ND2 B ASN A  1 182 ? -35.019 -17.134 30.196  0.50 24.35 ? 182  ASN A ND2 1 
ATOM   1466 N  N   . CYS A  1 183 ? -31.751 -17.699 25.283  1.00 18.40 ? 183  CYS A N   1 
ATOM   1467 C  CA  . CYS A  1 183 ? -30.485 -17.480 24.529  1.00 17.47 ? 183  CYS A CA  1 
ATOM   1468 C  C   . CYS A  1 183 ? -30.777 -17.392 23.017  1.00 17.21 ? 183  CYS A C   1 
ATOM   1469 O  O   . CYS A  1 183 ? -30.007 -17.949 22.236  1.00 15.81 ? 183  CYS A O   1 
ATOM   1470 C  CB  . CYS A  1 183 ? -29.436 -18.531 24.893  1.00 17.85 ? 183  CYS A CB  1 
ATOM   1471 S  SG  . CYS A  1 183 ? -29.928 -20.253 24.641  1.00 19.01 ? 183  CYS A SG  1 
ATOM   1472 N  N   . LEU A  1 184 ? -31.820 -16.667 22.619  1.00 17.23 ? 184  LEU A N   1 
ATOM   1473 C  CA  . LEU A  1 184 ? -32.112 -16.481 21.178  1.00 17.56 ? 184  LEU A CA  1 
ATOM   1474 C  C   . LEU A  1 184 ? -31.028 -15.575 20.610  1.00 16.88 ? 184  LEU A C   1 
ATOM   1475 O  O   . LEU A  1 184 ? -30.640 -14.579 21.230  1.00 17.76 ? 184  LEU A O   1 
ATOM   1476 C  CB  . LEU A  1 184 ? -33.499 -15.881 20.942  1.00 18.37 ? 184  LEU A CB  1 
ATOM   1477 C  CG  . LEU A  1 184 ? -34.651 -16.850 21.190  1.00 17.98 ? 184  LEU A CG  1 
ATOM   1478 C  CD1 . LEU A  1 184 ? -35.923 -16.112 21.541  1.00 19.04 ? 184  LEU A CD1 1 
ATOM   1479 C  CD2 . LEU A  1 184 ? -34.854 -17.771 19.999  1.00 18.69 ? 184  LEU A CD2 1 
ATOM   1480 N  N   . PRO A  1 185 ? -30.549 -15.892 19.400  1.00 15.13 ? 185  PRO A N   1 
ATOM   1481 C  CA  . PRO A  1 185 ? -29.670 -14.975 18.681  1.00 15.99 ? 185  PRO A CA  1 
ATOM   1482 C  C   . PRO A  1 185 ? -30.372 -13.643 18.416  1.00 14.45 ? 185  PRO A C   1 
ATOM   1483 O  O   . PRO A  1 185 ? -31.599 -13.624 18.294  1.00 15.42 ? 185  PRO A O   1 
ATOM   1484 C  CB  . PRO A  1 185 ? -29.354 -15.647 17.328  1.00 16.17 ? 185  PRO A CB  1 
ATOM   1485 C  CG  . PRO A  1 185 ? -30.110 -16.958 17.321  1.00 17.51 ? 185  PRO A CG  1 
ATOM   1486 C  CD  . PRO A  1 185 ? -30.901 -17.082 18.611  1.00 16.54 ? 185  PRO A CD  1 
ATOM   1487 N  N   . ASP A  1 186 ? -29.604 -12.551 18.424  1.00 13.86 ? 186  ASP A N   1 
ATOM   1488 C  CA  . ASP A  1 186 ? -30.088 -11.230 17.945  1.00 14.14 ? 186  ASP A CA  1 
ATOM   1489 C  C   . ASP A  1 186 ? -30.293 -11.293 16.421  1.00 13.89 ? 186  ASP A C   1 
ATOM   1490 O  O   . ASP A  1 186 ? -31.188 -10.599 15.871  1.00 14.20 ? 186  ASP A O   1 
ATOM   1491 C  CB  . ASP A  1 186 ? -29.112 -10.134 18.316  1.00 14.18 ? 186  ASP A CB  1 
ATOM   1492 C  CG  . ASP A  1 186 ? -28.898 -10.094 19.816  1.00 15.84 ? 186  ASP A CG  1 
ATOM   1493 O  OD1 . ASP A  1 186 ? -29.911 -10.016 20.517  1.00 15.94 ? 186  ASP A OD1 1 
ATOM   1494 O  OD2 . ASP A  1 186 ? -27.766 -10.151 20.246  1.00 14.62 ? 186  ASP A OD2 1 
ATOM   1495 N  N   . VAL A  1 187 ? -29.456 -12.062 15.740  1.00 12.32 ? 187  VAL A N   1 
ATOM   1496 C  CA  . VAL A  1 187 ? -29.508 -12.176 14.262  1.00 12.38 ? 187  VAL A CA  1 
ATOM   1497 C  C   . VAL A  1 187 ? -29.480 -13.655 13.909  1.00 12.77 ? 187  VAL A C   1 
ATOM   1498 O  O   . VAL A  1 187 ? -28.503 -14.329 14.260  1.00 14.22 ? 187  VAL A O   1 
ATOM   1499 C  CB  . VAL A  1 187 ? -28.310 -11.456 13.623  1.00 11.59 ? 187  VAL A CB  1 
ATOM   1500 C  CG1 . VAL A  1 187 ? -28.376 -11.550 12.111  1.00 11.78 ? 187  VAL A CG1 1 
ATOM   1501 C  CG2 . VAL A  1 187 ? -28.190 -10.003 14.088  1.00 12.05 ? 187  VAL A CG2 1 
ATOM   1502 N  N   . ILE A  1 188 ? -30.514 -14.148 13.252  1.00 12.13 ? 188  ILE A N   1 
ATOM   1503 C  CA  . ILE A  1 188 ? -30.589 -15.560 12.831  1.00 12.89 ? 188  ILE A CA  1 
ATOM   1504 C  C   . ILE A  1 188 ? -29.869 -15.696 11.502  1.00 12.60 ? 188  ILE A C   1 
ATOM   1505 O  O   . ILE A  1 188 ? -30.006 -14.816 10.662  1.00 11.83 ? 188  ILE A O   1 
ATOM   1506 C  CB  . ILE A  1 188 ? -32.055 -16.031 12.814  1.00 13.47 ? 188  ILE A CB  1 
ATOM   1507 C  CG1 . ILE A  1 188 ? -32.634 -15.963 14.233  1.00 14.37 ? 188  ILE A CG1 1 
ATOM   1508 C  CG2 . ILE A  1 188 ? -32.152 -17.418 12.186  1.00 13.43 ? 188  ILE A CG2 1 
ATOM   1509 C  CD1 . ILE A  1 188 ? -34.065 -16.445 14.364  1.00 14.95 ? 188  ILE A CD1 1 
ATOM   1510 N  N   . CYS A  1 189 ? -29.041 -16.721 11.369  1.00 11.55 ? 189  CYS A N   1 
ATOM   1511 C  CA  . CYS A  1 189 ? -28.066 -16.803 10.256  1.00 11.04 ? 189  CYS A CA  1 
ATOM   1512 C  C   . CYS A  1 189 ? -27.984 -18.229 9.713   1.00 10.60 ? 189  CYS A C   1 
ATOM   1513 O  O   . CYS A  1 189 ? -28.009 -19.156 10.515  1.00 11.30 ? 189  CYS A O   1 
ATOM   1514 C  CB  . CYS A  1 189 ? -26.708 -16.349 10.767  1.00 13.20 ? 189  CYS A CB  1 
ATOM   1515 S  SG  . CYS A  1 189 ? -25.420 -16.293 9.485   1.00 13.19 ? 189  CYS A SG  1 
ATOM   1516 N  N   . TRP A  1 190 ? -27.884 -18.375 8.395   1.00 10.07 ? 190  TRP A N   1 
ATOM   1517 C  CA  . TRP A  1 190 ? -27.481 -19.632 7.729   1.00 9.75  ? 190  TRP A CA  1 
ATOM   1518 C  C   . TRP A  1 190 ? -26.835 -19.280 6.408   1.00 10.14 ? 190  TRP A C   1 
ATOM   1519 O  O   . TRP A  1 190 ? -26.766 -18.072 6.069   1.00 10.42 ? 190  TRP A O   1 
ATOM   1520 C  CB  . TRP A  1 190 ? -28.668 -20.557 7.519   1.00 10.51 ? 190  TRP A CB  1 
ATOM   1521 C  CG  . TRP A  1 190 ? -29.711 -20.016 6.606   1.00 10.25 ? 190  TRP A CG  1 
ATOM   1522 C  CD1 . TRP A  1 190 ? -29.815 -20.231 5.261   1.00 10.77 ? 190  TRP A CD1 1 
ATOM   1523 C  CD2 . TRP A  1 190 ? -30.849 -19.214 6.968   1.00 11.13 ? 190  TRP A CD2 1 
ATOM   1524 N  NE1 . TRP A  1 190 ? -30.928 -19.624 4.770   1.00 11.26 ? 190  TRP A NE1 1 
ATOM   1525 C  CE2 . TRP A  1 190 ? -31.573 -18.972 5.784   1.00 10.69 ? 190  TRP A CE2 1 
ATOM   1526 C  CE3 . TRP A  1 190 ? -31.276 -18.624 8.157   1.00 10.98 ? 190  TRP A CE3 1 
ATOM   1527 C  CZ2 . TRP A  1 190 ? -32.757 -18.225 5.768   1.00 10.82 ? 190  TRP A CZ2 1 
ATOM   1528 C  CZ3 . TRP A  1 190 ? -32.439 -17.884 8.147   1.00 11.62 ? 190  TRP A CZ3 1 
ATOM   1529 C  CH2 . TRP A  1 190 ? -33.164 -17.684 6.964   1.00 10.98 ? 190  TRP A CH2 1 
ATOM   1530 N  N   . HIS A  1 191 ? -26.358 -20.300 5.709   1.00 10.30 ? 191  HIS A N   1 
ATOM   1531 C  CA  . HIS A  1 191 ? -25.605 -20.125 4.458   1.00 10.06 ? 191  HIS A CA  1 
ATOM   1532 C  C   . HIS A  1 191 ? -26.482 -20.530 3.299   1.00 10.41 ? 191  HIS A C   1 
ATOM   1533 O  O   . HIS A  1 191 ? -27.305 -21.458 3.461   1.00 10.91 ? 191  HIS A O   1 
ATOM   1534 C  CB  . HIS A  1 191 ? -24.290 -20.895 4.576   1.00 11.31 ? 191  HIS A CB  1 
ATOM   1535 C  CG  . HIS A  1 191 ? -23.460 -20.413 5.715   1.00 10.88 ? 191  HIS A CG  1 
ATOM   1536 N  ND1 . HIS A  1 191 ? -22.400 -21.136 6.228   1.00 10.77 ? 191  HIS A ND1 1 
ATOM   1537 C  CD2 . HIS A  1 191 ? -23.506 -19.248 6.399   1.00 11.23 ? 191  HIS A CD2 1 
ATOM   1538 C  CE1 . HIS A  1 191 ? -21.871 -20.428 7.197   1.00 10.95 ? 191  HIS A CE1 1 
ATOM   1539 N  NE2 . HIS A  1 191 ? -22.499 -19.253 7.288   1.00 10.94 ? 191  HIS A NE2 1 
ATOM   1540 N  N   . GLU A  1 192 ? -26.280 -19.878 2.170   1.00 9.91  ? 192  GLU A N   1 
ATOM   1541 C  CA  . GLU A  1 192 ? -26.951 -20.254 0.903   1.00 10.77 ? 192  GLU A CA  1 
ATOM   1542 C  C   . GLU A  1 192 ? -25.854 -20.490 -0.143  1.00 11.59 ? 192  GLU A C   1 
ATOM   1543 O  O   . GLU A  1 192 ? -25.552 -19.568 -0.935  1.00 11.02 ? 192  GLU A O   1 
ATOM   1544 C  CB  . GLU A  1 192 ? -27.938 -19.175 0.515   1.00 10.88 ? 192  GLU A CB  1 
ATOM   1545 C  CG  . GLU A  1 192 ? -29.129 -19.025 1.452   1.00 11.21 ? 192  GLU A CG  1 
ATOM   1546 C  CD  . GLU A  1 192 ? -30.239 -20.038 1.307   1.00 12.87 ? 192  GLU A CD  1 
ATOM   1547 O  OE1 . GLU A  1 192 ? -30.079 -20.991 0.504   1.00 11.88 ? 192  GLU A OE1 1 
ATOM   1548 O  OE2 . GLU A  1 192 ? -31.225 -19.883 2.009   1.00 12.39 ? 192  GLU A OE2 1 
ATOM   1549 N  N   . LEU A  1 193 ? -25.206 -21.652 -0.075  1.00 12.29 ? 193  LEU A N   1 
ATOM   1550 C  CA  . LEU A  1 193 ? -24.083 -22.043 -0.945  1.00 13.51 ? 193  LEU A CA  1 
ATOM   1551 C  C   . LEU A  1 193 ? -24.507 -23.062 -1.997  1.00 13.74 ? 193  LEU A C   1 
ATOM   1552 O  O   . LEU A  1 193 ? -23.602 -23.572 -2.704  1.00 13.72 ? 193  LEU A O   1 
ATOM   1553 C  CB  . LEU A  1 193 ? -22.984 -22.587 -0.029  1.00 14.41 ? 193  LEU A CB  1 
ATOM   1554 C  CG  . LEU A  1 193 ? -22.460 -21.551 0.968   1.00 15.04 ? 193  LEU A CG  1 
ATOM   1555 C  CD1 . LEU A  1 193 ? -21.608 -22.222 2.018   1.00 16.32 ? 193  LEU A CD1 1 
ATOM   1556 C  CD2 . LEU A  1 193 ? -21.704 -20.462 0.233   1.00 17.00 ? 193  LEU A CD2 1 
ATOM   1557 N  N   . GLY A  1 194 ? -25.808 -23.303 -2.131  1.00 14.13 ? 194  GLY A N   1 
ATOM   1558 C  CA  . GLY A  1 194 ? -26.345 -24.238 -3.126  1.00 14.49 ? 194  GLY A CA  1 
ATOM   1559 C  C   . GLY A  1 194 ? -27.124 -23.539 -4.227  1.00 14.55 ? 194  GLY A C   1 
ATOM   1560 O  O   . GLY A  1 194 ? -27.974 -24.199 -4.829  1.00 13.09 ? 194  GLY A O   1 
ATOM   1561 N  N   . GLY A  1 195 ? -26.878 -22.251 -4.477  1.00 13.66 ? 195  GLY A N   1 
ATOM   1562 C  CA  . GLY A  1 195 ? -27.661 -21.460 -5.446  1.00 13.11 ? 195  GLY A CA  1 
ATOM   1563 C  C   . GLY A  1 195 ? -28.750 -20.635 -4.778  1.00 12.36 ? 195  GLY A C   1 
ATOM   1564 O  O   . GLY A  1 195 ? -28.938 -20.714 -3.530  1.00 11.75 ? 195  GLY A O   1 
ATOM   1565 N  N   . SER A  1 196 ? -29.432 -19.841 -5.580  1.00 11.86 ? 196  SER A N   1 
ATOM   1566 C  CA  . SER A  1 196 ? -30.374 -18.808 -5.105  1.00 10.93 ? 196  SER A CA  1 
ATOM   1567 C  C   . SER A  1 196 ? -31.825 -19.297 -5.061  1.00 11.01 ? 196  SER A C   1 
ATOM   1568 O  O   . SER A  1 196 ? -32.652 -18.555 -4.540  1.00 12.16 ? 196  SER A O   1 
ATOM   1569 C  CB  . SER A  1 196 ? -30.239 -17.576 -5.942  1.00 11.48 ? 196  SER A CB  1 
ATOM   1570 O  OG  . SER A  1 196 ? -30.421 -17.925 -7.303  1.00 11.55 ? 196  SER A OG  1 
ATOM   1571 N  N   . GLN A  1 197 ? -32.100 -20.509 -5.536  1.00 12.15 ? 197  GLN A N   1 
ATOM   1572 C  CA  . GLN A  1 197 ? -33.476 -20.960 -5.897  1.00 13.55 ? 197  GLN A CA  1 
ATOM   1573 C  C   . GLN A  1 197 ? -34.317 -21.239 -4.650  1.00 13.73 ? 197  GLN A C   1 
ATOM   1574 O  O   . GLN A  1 197 ? -35.548 -21.370 -4.821  1.00 15.44 ? 197  GLN A O   1 
ATOM   1575 C  CB  . GLN A  1 197 ? -33.423 -22.167 -6.848  1.00 14.32 ? 197  GLN A CB  1 
ATOM   1576 C  CG  . GLN A  1 197 ? -32.814 -23.405 -6.223  1.00 15.37 ? 197  GLN A CG  1 
ATOM   1577 C  CD  . GLN A  1 197 ? -31.319 -23.476 -6.366  1.00 14.99 ? 197  GLN A CD  1 
ATOM   1578 O  OE1 . GLN A  1 197 ? -30.656 -22.559 -6.864  1.00 14.30 ? 197  GLN A OE1 1 
ATOM   1579 N  NE2 . GLN A  1 197 ? -30.779 -24.626 -5.985  1.00 15.89 ? 197  GLN A NE2 1 
ATOM   1580 N  N   . ASN A  1 198 ? -33.741 -21.373 -3.459  1.00 13.45 ? 198  ASN A N   1 
ATOM   1581 C  CA  . ASN A  1 198 ? -34.508 -21.705 -2.228  1.00 13.85 ? 198  ASN A CA  1 
ATOM   1582 C  C   . ASN A  1 198 ? -34.496 -20.564 -1.204  1.00 13.71 ? 198  ASN A C   1 
ATOM   1583 O  O   . ASN A  1 198 ? -35.106 -20.758 -0.122  1.00 13.58 ? 198  ASN A O   1 
ATOM   1584 C  CB  . ASN A  1 198 ? -33.957 -23.003 -1.621  1.00 15.00 ? 198  ASN A CB  1 
ATOM   1585 C  CG  . ASN A  1 198 ? -34.134 -24.162 -2.574  1.00 14.97 ? 198  ASN A CG  1 
ATOM   1586 O  OD1 . ASN A  1 198 ? -33.172 -24.807 -2.967  1.00 21.36 ? 198  ASN A OD1 1 
ATOM   1587 N  ND2 . ASN A  1 198 ? -35.355 -24.353 -3.004  1.00 16.09 ? 198  ASN A ND2 1 
ATOM   1588 N  N   . ILE A  1 199 ? -33.829 -19.426 -1.474  1.00 12.62 ? 199  ILE A N   1 
ATOM   1589 C  CA  . ILE A  1 199 ? -33.660 -18.337 -0.475  1.00 12.77 ? 199  ILE A CA  1 
ATOM   1590 C  C   . ILE A  1 199 ? -35.038 -17.911 0.014   1.00 13.28 ? 199  ILE A C   1 
ATOM   1591 O  O   . ILE A  1 199 ? -35.239 -17.812 1.199   1.00 13.07 ? 199  ILE A O   1 
ATOM   1592 C  CB  . ILE A  1 199 ? -32.900 -17.126 -1.061  1.00 13.20 ? 199  ILE A CB  1 
ATOM   1593 C  CG1 . ILE A  1 199 ? -31.455 -17.493 -1.411  1.00 14.97 ? 199  ILE A CG1 1 
ATOM   1594 C  CG2 . ILE A  1 199 ? -32.984 -15.969 -0.094  1.00 13.35 ? 199  ILE A CG2 1 
ATOM   1595 C  CD1 . ILE A  1 199 ? -30.706 -16.458 -2.183  1.00 15.64 ? 199  ILE A CD1 1 
ATOM   1596 N  N   . SER A  1 200 ? -35.924 -17.562 -0.905  1.00 13.60 ? 200  SER A N   1 
ATOM   1597 C  CA  . SER A  1 200 ? -37.199 -16.921 -0.547  1.00 14.91 ? 200  SER A CA  1 
ATOM   1598 C  C   . SER A  1 200 ? -38.035 -17.910 0.275   1.00 14.71 ? 200  SER A C   1 
ATOM   1599 O  O   . SER A  1 200 ? -38.563 -17.527 1.326   1.00 14.10 ? 200  SER A O   1 
ATOM   1600 C  CB  . SER A  1 200 ? -37.885 -16.380 -1.762  1.00 17.65 ? 200  SER A CB  1 
ATOM   1601 O  OG  . SER A  1 200 ? -37.136 -15.239 -2.213  1.00 18.97 ? 200  SER A OG  1 
ATOM   1602 N  N   . GLY A  1 201 ? -38.072 -19.157 -0.143  1.00 14.67 ? 201  GLY A N   1 
ATOM   1603 C  CA  . GLY A  1 201 ? -38.769 -20.185 0.641   1.00 14.01 ? 201  GLY A CA  1 
ATOM   1604 C  C   . GLY A  1 201 ? -38.180 -20.376 2.032   1.00 13.28 ? 201  GLY A C   1 
ATOM   1605 O  O   . GLY A  1 201 ? -38.958 -20.588 3.011   1.00 12.64 ? 201  GLY A O   1 
ATOM   1606 N  N   . ASN A  1 202 ? -36.849 -20.373 2.135   1.00 12.09 ? 202  ASN A N   1 
ATOM   1607 C  CA  . ASN A  1 202 ? -36.184 -20.619 3.429   1.00 12.66 ? 202  ASN A CA  1 
ATOM   1608 C  C   . ASN A  1 202 ? -36.520 -19.469 4.369   1.00 12.60 ? 202  ASN A C   1 
ATOM   1609 O  O   . ASN A  1 202 ? -36.777 -19.728 5.547   1.00 11.57 ? 202  ASN A O   1 
ATOM   1610 C  CB  . ASN A  1 202 ? -34.671 -20.810 3.270   1.00 13.16 ? 202  ASN A CB  1 
ATOM   1611 C  CG  . ASN A  1 202 ? -34.280 -22.086 2.547   1.00 14.71 ? 202  ASN A CG  1 
ATOM   1612 O  OD1 . ASN A  1 202 ? -35.082 -23.034 2.476   1.00 13.09 ? 202  ASN A OD1 1 
ATOM   1613 N  ND2 . ASN A  1 202 ? -33.042 -22.138 2.031   1.00 14.57 ? 202  ASN A ND2 1 
ATOM   1614 N  N   . ILE A  1 203 ? -36.472 -18.225 3.873   1.00 12.74 ? 203  ILE A N   1 
ATOM   1615 C  CA  . ILE A  1 203 ? -36.747 -17.042 4.730   1.00 14.02 ? 203  ILE A CA  1 
ATOM   1616 C  C   . ILE A  1 203 ? -38.223 -17.094 5.159   1.00 14.85 ? 203  ILE A C   1 
ATOM   1617 O  O   . ILE A  1 203 ? -38.499 -16.938 6.384   1.00 14.12 ? 203  ILE A O   1 
ATOM   1618 C  CB  . ILE A  1 203 ? -36.386 -15.728 4.015   1.00 14.06 ? 203  ILE A CB  1 
ATOM   1619 C  CG1 . ILE A  1 203 ? -34.866 -15.647 3.794   1.00 14.40 ? 203  ILE A CG1 1 
ATOM   1620 C  CG2 . ILE A  1 203 ? -36.922 -14.558 4.812   1.00 13.66 ? 203  ILE A CG2 1 
ATOM   1621 C  CD1 . ILE A  1 203 ? -34.455 -14.539 2.799   1.00 14.23 ? 203  ILE A CD1 1 
ATOM   1622 N  N   . ARG A  1 204 ? -39.119 -17.414 4.246   1.00 15.82 ? 204  ARG A N   1 
ATOM   1623 C  CA  A ARG A  1 204 ? -40.571 -17.574 4.576   0.80 18.01 ? 204  ARG A CA  1 
ATOM   1624 C  CA  B ARG A  1 204 ? -40.559 -17.550 4.601   0.20 16.37 ? 204  ARG A CA  1 
ATOM   1625 C  C   . ARG A  1 204 ? -40.700 -18.625 5.682   1.00 16.43 ? 204  ARG A C   1 
ATOM   1626 O  O   . ARG A  1 204 ? -41.464 -18.402 6.662   1.00 16.14 ? 204  ARG A O   1 
ATOM   1627 C  CB  A ARG A  1 204 ? -41.368 -18.046 3.356   0.80 20.24 ? 204  ARG A CB  1 
ATOM   1628 C  CB  B ARG A  1 204 ? -41.383 -17.890 3.361   0.20 16.89 ? 204  ARG A CB  1 
ATOM   1629 C  CG  A ARG A  1 204 ? -42.886 -18.096 3.537   0.80 23.55 ? 204  ARG A CG  1 
ATOM   1630 C  CG  B ARG A  1 204 ? -41.362 -16.778 2.328   0.20 17.40 ? 204  ARG A CG  1 
ATOM   1631 C  CD  A ARG A  1 204 ? -43.653 -18.638 2.319   0.80 28.50 ? 204  ARG A CD  1 
ATOM   1632 C  CD  B ARG A  1 204 ? -42.619 -15.941 2.298   0.20 18.54 ? 204  ARG A CD  1 
ATOM   1633 N  NE  A ARG A  1 204 ? -42.894 -18.830 1.074   0.80 34.98 ? 204  ARG A NE  1 
ATOM   1634 N  NE  B ARG A  1 204 ? -43.316 -16.202 1.053   0.20 19.28 ? 204  ARG A NE  1 
ATOM   1635 C  CZ  A ARG A  1 204 ? -42.338 -17.864 0.322   0.80 37.89 ? 204  ARG A CZ  1 
ATOM   1636 C  CZ  B ARG A  1 204 ? -42.951 -15.699 -0.121  0.20 19.35 ? 204  ARG A CZ  1 
ATOM   1637 N  NH1 A ARG A  1 204 ? -42.432 -16.586 0.665   0.80 42.31 ? 204  ARG A NH1 1 
ATOM   1638 N  NH1 B ARG A  1 204 ? -43.627 -16.010 -1.214  0.20 19.77 ? 204  ARG A NH1 1 
ATOM   1639 N  NH2 A ARG A  1 204 ? -41.670 -18.184 -0.776  0.80 38.77 ? 204  ARG A NH2 1 
ATOM   1640 N  NH2 B ARG A  1 204 ? -41.914 -14.887 -0.194  0.20 19.53 ? 204  ARG A NH2 1 
ATOM   1641 N  N   . ASP A  1 205 ? -39.990 -19.738 5.523   1.00 15.50 ? 205  ASP A N   1 
ATOM   1642 C  CA  . ASP A  1 205 ? -40.079 -20.861 6.493   1.00 15.15 ? 205  ASP A CA  1 
ATOM   1643 C  C   . ASP A  1 205 ? -39.645 -20.351 7.873   1.00 15.62 ? 205  ASP A C   1 
ATOM   1644 O  O   . ASP A  1 205 ? -40.337 -20.605 8.883   1.00 14.38 ? 205  ASP A O   1 
ATOM   1645 C  CB  . ASP A  1 205 ? -39.228 -22.048 6.062   1.00 15.35 ? 205  ASP A CB  1 
ATOM   1646 C  CG  . ASP A  1 205 ? -39.508 -23.277 6.903   1.00 17.20 ? 205  ASP A CG  1 
ATOM   1647 O  OD1 . ASP A  1 205 ? -38.960 -23.399 8.013   1.00 15.31 ? 205  ASP A OD1 1 
ATOM   1648 O  OD2 . ASP A  1 205 ? -40.397 -24.019 6.485   1.00 24.66 ? 205  ASP A OD2 1 
ATOM   1649 N  N   . LEU A  1 206 ? -38.505 -19.644 7.927   1.00 14.85 ? 206  LEU A N   1 
ATOM   1650 C  CA  . LEU A  1 206 ? -37.993 -19.142 9.211   1.00 15.14 ? 206  LEU A CA  1 
ATOM   1651 C  C   . LEU A  1 206 ? -39.031 -18.207 9.846   1.00 15.48 ? 206  LEU A C   1 
ATOM   1652 O  O   . LEU A  1 206 ? -39.255 -18.314 11.062  1.00 15.01 ? 206  LEU A O   1 
ATOM   1653 C  CB  . LEU A  1 206 ? -36.677 -18.398 9.060   1.00 15.31 ? 206  LEU A CB  1 
ATOM   1654 C  CG  . LEU A  1 206 ? -36.335 -17.697 10.372  1.00 19.22 ? 206  LEU A CG  1 
ATOM   1655 C  CD1 . LEU A  1 206 ? -35.869 -18.707 11.386  1.00 19.00 ? 206  LEU A CD1 1 
ATOM   1656 C  CD2 . LEU A  1 206 ? -35.420 -16.542 10.216  1.00 21.21 ? 206  LEU A CD2 1 
ATOM   1657 N  N   . LYS A  1 207 ? -39.602 -17.281 9.087   1.00 16.33 ? 207  LYS A N   1 
ATOM   1658 C  CA  . LYS A  1 207 ? -40.542 -16.284 9.667   1.00 17.38 ? 207  LYS A CA  1 
ATOM   1659 C  C   . LYS A  1 207 ? -41.781 -17.020 10.195  1.00 18.07 ? 207  LYS A C   1 
ATOM   1660 O  O   . LYS A  1 207 ? -42.243 -16.696 11.314  1.00 17.52 ? 207  LYS A O   1 
ATOM   1661 C  CB  . LYS A  1 207 ? -40.802 -15.194 8.632   1.00 18.55 ? 207  LYS A CB  1 
ATOM   1662 C  CG  . LYS A  1 207 ? -39.564 -14.323 8.457   1.00 19.87 ? 207  LYS A CG  1 
ATOM   1663 C  CD  . LYS A  1 207 ? -39.762 -13.132 7.580   1.00 19.95 ? 207  LYS A CD  1 
ATOM   1664 C  CE  . LYS A  1 207 ? -38.493 -12.356 7.308   1.00 21.19 ? 207  LYS A CE  1 
ATOM   1665 N  NZ  . LYS A  1 207 ? -37.904 -11.702 8.513   1.00 20.03 ? 207  LYS A NZ  1 
ATOM   1666 N  N   . THR A  1 208 ? -42.276 -17.990 9.444   1.00 18.34 ? 208  THR A N   1 
ATOM   1667 C  CA  . THR A  1 208 ? -43.432 -18.805 9.890   1.00 19.99 ? 208  THR A CA  1 
ATOM   1668 C  C   . THR A  1 208 ? -43.076 -19.545 11.185  1.00 20.21 ? 208  THR A C   1 
ATOM   1669 O  O   . THR A  1 208 ? -43.900 -19.590 12.118  1.00 19.01 ? 208  THR A O   1 
ATOM   1670 C  CB  . THR A  1 208 ? -43.855 -19.777 8.795   1.00 21.38 ? 208  THR A CB  1 
ATOM   1671 O  OG1 . THR A  1 208 ? -44.183 -18.929 7.690   1.00 21.64 ? 208  THR A OG1 1 
ATOM   1672 C  CG2 . THR A  1 208 ? -45.027 -20.639 9.208   1.00 22.62 ? 208  THR A CG2 1 
ATOM   1673 N  N   . LEU A  1 209 ? -41.885 -20.134 11.239  1.00 18.19 ? 209  LEU A N   1 
ATOM   1674 C  CA  . LEU A  1 209 ? -41.398 -20.821 12.461  1.00 18.35 ? 209  LEU A CA  1 
ATOM   1675 C  C   . LEU A  1 209 ? -41.318 -19.855 13.647  1.00 19.01 ? 209  LEU A C   1 
ATOM   1676 O  O   . LEU A  1 209 ? -41.767 -20.245 14.763  1.00 19.44 ? 209  LEU A O   1 
ATOM   1677 C  CB  . LEU A  1 209 ? -40.042 -21.435 12.130  1.00 18.96 ? 209  LEU A CB  1 
ATOM   1678 C  CG  . LEU A  1 209 ? -39.370 -22.261 13.213  1.00 20.61 ? 209  LEU A CG  1 
ATOM   1679 C  CD1 . LEU A  1 209 ? -40.293 -23.368 13.725  1.00 19.84 ? 209  LEU A CD1 1 
ATOM   1680 C  CD2 . LEU A  1 209 ? -38.084 -22.842 12.645  1.00 19.48 ? 209  LEU A CD2 1 
ATOM   1681 N  N   . GLU A  1 210 ? -40.769 -18.650 13.472  1.00 17.37 ? 210  GLU A N   1 
ATOM   1682 C  CA  . GLU A  1 210 ? -40.668 -17.693 14.603  1.00 19.47 ? 210  GLU A CA  1 
ATOM   1683 C  C   . GLU A  1 210 ? -42.093 -17.424 15.128  1.00 23.09 ? 210  GLU A C   1 
ATOM   1684 O  O   . GLU A  1 210 ? -42.310 -17.435 16.358  1.00 23.15 ? 210  GLU A O   1 
ATOM   1685 C  CB  . GLU A  1 210 ? -40.058 -16.368 14.185  1.00 19.09 ? 210  GLU A CB  1 
ATOM   1686 C  CG  . GLU A  1 210 ? -38.585 -16.432 13.824  1.00 20.16 ? 210  GLU A CG  1 
ATOM   1687 C  CD  . GLU A  1 210 ? -38.093 -15.086 13.310  1.00 20.32 ? 210  GLU A CD  1 
ATOM   1688 O  OE1 . GLU A  1 210 ? -38.755 -14.526 12.377  1.00 22.99 ? 210  GLU A OE1 1 
ATOM   1689 O  OE2 . GLU A  1 210 ? -37.131 -14.531 13.909  1.00 19.74 ? 210  GLU A OE2 1 
ATOM   1690 N  N   . ARG A  1 211 ? -43.025 -17.122 14.233  1.00 21.72 ? 211  ARG A N   1 
ATOM   1691 C  CA  . ARG A  1 211 ? -44.422 -16.819 14.666  1.00 23.33 ? 211  ARG A CA  1 
ATOM   1692 C  C   . ARG A  1 211 ? -44.965 -18.037 15.421  1.00 23.63 ? 211  ARG A C   1 
ATOM   1693 O  O   . ARG A  1 211 ? -45.641 -17.857 16.453  1.00 23.93 ? 211  ARG A O   1 
ATOM   1694 C  CB  . ARG A  1 211 ? -45.277 -16.413 13.465  1.00 23.83 ? 211  ARG A CB  1 
ATOM   1695 C  CG  . ARG A  1 211 ? -44.922 -15.020 12.970  1.00 26.96 ? 211  ARG A CG  1 
ATOM   1696 C  CD  . ARG A  1 211 ? -45.845 -14.519 11.894  1.00 30.28 ? 211  ARG A CD  1 
ATOM   1697 N  NE  . ARG A  1 211 ? -45.893 -15.419 10.739  1.00 34.17 ? 211  ARG A NE  1 
ATOM   1698 C  CZ  . ARG A  1 211 ? -45.162 -15.287 9.621   1.00 35.08 ? 211  ARG A CZ  1 
ATOM   1699 N  NH1 . ARG A  1 211 ? -44.292 -14.297 9.492   1.00 35.17 ? 211  ARG A NH1 1 
ATOM   1700 N  NH2 . ARG A  1 211 ? -45.315 -16.144 8.628   1.00 35.52 ? 211  ARG A NH2 1 
ATOM   1701 N  N   . SER A  1 212 ? -44.676 -19.227 14.928  1.00 24.50 ? 212  SER A N   1 
ATOM   1702 C  CA  . SER A  1 212 ? -45.161 -20.488 15.526  1.00 28.31 ? 212  SER A CA  1 
ATOM   1703 C  C   . SER A  1 212 ? -44.661 -20.621 16.976  1.00 27.37 ? 212  SER A C   1 
ATOM   1704 O  O   . SER A  1 212 ? -45.425 -21.148 17.795  1.00 26.81 ? 212  SER A O   1 
ATOM   1705 C  CB  . SER A  1 212 ? -44.781 -21.642 14.666  1.00 31.07 ? 212  SER A CB  1 
ATOM   1706 O  OG  . SER A  1 212 ? -45.100 -22.842 15.318  1.00 38.49 ? 212  SER A OG  1 
ATOM   1707 N  N   . LEU A  1 213 ? -43.449 -20.154 17.302  1.00 23.26 ? 213  LEU A N   1 
ATOM   1708 C  CA  . LEU A  1 213 ? -42.842 -20.308 18.648  1.00 23.67 ? 213  LEU A CA  1 
ATOM   1709 C  C   . LEU A  1 213 ? -43.044 -19.035 19.451  1.00 23.94 ? 213  LEU A C   1 
ATOM   1710 O  O   . LEU A  1 213 ? -42.585 -19.006 20.604  1.00 26.38 ? 213  LEU A O   1 
ATOM   1711 C  CB  . LEU A  1 213 ? -41.349 -20.633 18.506  1.00 23.15 ? 213  LEU A CB  1 
ATOM   1712 C  CG  . LEU A  1 213 ? -41.035 -21.890 17.707  1.00 24.23 ? 213  LEU A CG  1 
ATOM   1713 C  CD1 . LEU A  1 213 ? -39.532 -22.074 17.574  1.00 24.00 ? 213  LEU A CD1 1 
ATOM   1714 C  CD2 . LEU A  1 213 ? -41.687 -23.125 18.316  1.00 26.27 ? 213  LEU A CD2 1 
ATOM   1715 N  N   . GLY A  1 214 ? -43.657 -18.012 18.860  1.00 23.37 ? 214  GLY A N   1 
ATOM   1716 C  CA  . GLY A  1 214 ? -43.907 -16.720 19.521  1.00 25.62 ? 214  GLY A CA  1 
ATOM   1717 C  C   . GLY A  1 214 ? -42.614 -15.975 19.750  1.00 28.52 ? 214  GLY A C   1 
ATOM   1718 O  O   . GLY A  1 214 ? -42.472 -15.267 20.769  1.00 29.71 ? 214  GLY A O   1 
ATOM   1719 N  N   . ILE A  1 215 ? -41.676 -16.119 18.825  1.00 26.57 ? 215  ILE A N   1 
ATOM   1720 C  CA  . ILE A  1 215 ? -40.387 -15.392 18.882  1.00 24.33 ? 215  ILE A CA  1 
ATOM   1721 C  C   . ILE A  1 215 ? -40.590 -14.105 18.101  1.00 23.92 ? 215  ILE A C   1 
ATOM   1722 O  O   . ILE A  1 215 ? -40.937 -14.149 16.916  1.00 25.92 ? 215  ILE A O   1 
ATOM   1723 C  CB  . ILE A  1 215 ? -39.236 -16.230 18.298  1.00 23.94 ? 215  ILE A CB  1 
ATOM   1724 C  CG1 . ILE A  1 215 ? -39.015 -17.507 19.103  1.00 26.08 ? 215  ILE A CG1 1 
ATOM   1725 C  CG2 . ILE A  1 215 ? -37.983 -15.390 18.195  1.00 25.37 ? 215  ILE A CG2 1 
ATOM   1726 C  CD1 . ILE A  1 215 ? -38.225 -18.569 18.365  1.00 23.40 ? 215  ILE A CD1 1 
ATOM   1727 N  N   . PRO A  1 216 ? -40.346 -12.924 18.702  1.00 24.20 ? 216  PRO A N   1 
ATOM   1728 C  CA  . PRO A  1 216 ? -40.343 -11.678 17.932  1.00 24.72 ? 216  PRO A CA  1 
ATOM   1729 C  C   . PRO A  1 216 ? -39.348 -11.759 16.762  1.00 26.01 ? 216  PRO A C   1 
ATOM   1730 O  O   . PRO A  1 216 ? -38.231 -12.249 16.955  1.00 24.31 ? 216  PRO A O   1 
ATOM   1731 C  CB  . PRO A  1 216 ? -39.944 -10.599 18.948  1.00 25.17 ? 216  PRO A CB  1 
ATOM   1732 C  CG  . PRO A  1 216 ? -40.289 -11.213 20.295  1.00 26.78 ? 216  PRO A CG  1 
ATOM   1733 C  CD  . PRO A  1 216 ? -40.099 -12.703 20.130  1.00 25.42 ? 216  PRO A CD  1 
ATOM   1734 N  N   . GLU A  1 217 ? -39.792 -11.309 15.595  1.00 23.69 ? 217  GLU A N   1 
ATOM   1735 C  CA  . GLU A  1 217 ? -39.083 -11.454 14.299  1.00 23.64 ? 217  GLU A CA  1 
ATOM   1736 C  C   . GLU A  1 217 ? -37.663 -10.931 14.457  1.00 21.68 ? 217  GLU A C   1 
ATOM   1737 O  O   . GLU A  1 217 ? -37.467 -9.772  14.889  1.00 21.91 ? 217  GLU A O   1 
ATOM   1738 C  CB  . GLU A  1 217 ? -39.842 -10.691 13.221  1.00 28.28 ? 217  GLU A CB  1 
ATOM   1739 C  CG  . GLU A  1 217 ? -39.191 -10.729 11.847  1.00 29.17 ? 217  GLU A CG  1 
ATOM   1740 C  CD  . GLU A  1 217 ? -39.927 -9.911  10.803  1.00 32.89 ? 217  GLU A CD  1 
ATOM   1741 O  OE1 . GLU A  1 217 ? -40.590 -8.907  11.200  1.00 36.30 ? 217  GLU A OE1 1 
ATOM   1742 O  OE2 . GLU A  1 217 ? -39.853 -10.263 9.606   1.00 29.07 ? 217  GLU A OE2 1 
ATOM   1743 N  N   . ARG A  1 218 ? -36.685 -11.765 14.126  1.00 19.21 ? 218  ARG A N   1 
ATOM   1744 C  CA  . ARG A  1 218 ? -35.265 -11.400 14.237  1.00 18.28 ? 218  ARG A CA  1 
ATOM   1745 C  C   . ARG A  1 218 ? -34.741 -10.896 12.883  1.00 15.71 ? 218  ARG A C   1 
ATOM   1746 O  O   . ARG A  1 218 ? -35.175 -11.377 11.839  1.00 14.06 ? 218  ARG A O   1 
ATOM   1747 C  CB  . ARG A  1 218 ? -34.436 -12.620 14.659  1.00 19.61 ? 218  ARG A CB  1 
ATOM   1748 C  CG  . ARG A  1 218 ? -34.736 -13.132 16.067  1.00 22.47 ? 218  ARG A CG  1 
ATOM   1749 C  CD  . ARG A  1 218 ? -34.645 -12.028 17.080  1.00 23.82 ? 218  ARG A CD  1 
ATOM   1750 N  NE  . ARG A  1 218 ? -34.309 -12.346 18.471  1.00 23.00 ? 218  ARG A NE  1 
ATOM   1751 C  CZ  . ARG A  1 218 ? -35.156 -12.341 19.498  1.00 23.35 ? 218  ARG A CZ  1 
ATOM   1752 N  NH1 . ARG A  1 218 ? -36.468 -12.201 19.311  1.00 22.75 ? 218  ARG A NH1 1 
ATOM   1753 N  NH2 . ARG A  1 218 ? -34.685 -12.509 20.719  1.00 22.61 ? 218  ARG A NH2 1 
ATOM   1754 N  N   . LYS A  1 219 ? -33.739 -10.042 12.954  1.00 15.12 ? 219  LYS A N   1 
ATOM   1755 C  CA  . LYS A  1 219 ? -32.816 -9.750  11.838  1.00 15.29 ? 219  LYS A CA  1 
ATOM   1756 C  C   . LYS A  1 219 ? -32.263 -11.074 11.300  1.00 12.76 ? 219  LYS A C   1 
ATOM   1757 O  O   . LYS A  1 219 ? -32.014 -12.021 12.103  1.00 13.58 ? 219  LYS A O   1 
ATOM   1758 C  CB  . LYS A  1 219 ? -31.669 -8.887  12.338  1.00 16.39 ? 219  LYS A CB  1 
ATOM   1759 C  CG  . LYS A  1 219 ? -31.993 -7.421  12.588  1.00 19.06 ? 219  LYS A CG  1 
ATOM   1760 C  CD  . LYS A  1 219 ? -30.822 -6.750  13.248  1.00 22.77 ? 219  LYS A CD  1 
ATOM   1761 C  CE  . LYS A  1 219 ? -31.017 -5.282  13.524  1.00 27.15 ? 219  LYS A CE  1 
ATOM   1762 N  NZ  . LYS A  1 219 ? -29.815 -4.744  14.201  1.00 30.59 ? 219  LYS A NZ  1 
ATOM   1763 N  N   . ILE A  1 220 ? -32.050 -11.127 9.992   1.00 12.09 ? 220  ILE A N   1 
ATOM   1764 C  CA  . ILE A  1 220 ? -31.482 -12.291 9.260   1.00 11.26 ? 220  ILE A CA  1 
ATOM   1765 C  C   . ILE A  1 220 ? -30.137 -11.885 8.665   1.00 11.22 ? 220  ILE A C   1 
ATOM   1766 O  O   . ILE A  1 220 ? -30.043 -10.800 7.998   1.00 10.02 ? 220  ILE A O   1 
ATOM   1767 C  CB  . ILE A  1 220 ? -32.449 -12.787 8.169   1.00 12.84 ? 220  ILE A CB  1 
ATOM   1768 C  CG1 . ILE A  1 220 ? -33.762 -13.264 8.798   1.00 13.94 ? 220  ILE A CG1 1 
ATOM   1769 C  CG2 . ILE A  1 220 ? -31.804 -13.863 7.309   1.00 12.28 ? 220  ILE A CG2 1 
ATOM   1770 C  CD1 . ILE A  1 220 ? -34.825 -13.652 7.817   1.00 15.08 ? 220  ILE A CD1 1 
ATOM   1771 N  N   . ALA A  1 221 ? -29.134 -12.763 8.826   1.00 11.11 ? 221  ALA A N   1 
ATOM   1772 C  CA  . ALA A  1 221 ? -27.825 -12.672 8.155   1.00 11.49 ? 221  ALA A CA  1 
ATOM   1773 C  C   . ALA A  1 221 ? -27.609 -13.943 7.341   1.00 10.58 ? 221  ALA A C   1 
ATOM   1774 O  O   . ALA A  1 221 ? -27.878 -15.027 7.863   1.00 11.45 ? 221  ALA A O   1 
ATOM   1775 C  CB  . ALA A  1 221 ? -26.715 -12.502 9.128   1.00 12.20 ? 221  ALA A CB  1 
ATOM   1776 N  N   . ILE A  1 222 ? -27.260 -13.776 6.079   1.00 10.53 ? 222  ILE A N   1 
ATOM   1777 C  CA  . ILE A  1 222 ? -26.847 -14.912 5.224   1.00 10.90 ? 222  ILE A CA  1 
ATOM   1778 C  C   . ILE A  1 222 ? -25.353 -14.760 4.971   1.00 10.04 ? 222  ILE A C   1 
ATOM   1779 O  O   . ILE A  1 222 ? -25.002 -14.170 3.933   1.00 10.41 ? 222  ILE A O   1 
ATOM   1780 C  CB  . ILE A  1 222 ? -27.708 -15.000 3.959   1.00 11.36 ? 222  ILE A CB  1 
ATOM   1781 C  CG1 . ILE A  1 222 ? -29.197 -14.986 4.311   1.00 12.38 ? 222  ILE A CG1 1 
ATOM   1782 C  CG2 . ILE A  1 222 ? -27.298 -16.235 3.164   1.00 10.88 ? 222  ILE A CG2 1 
ATOM   1783 C  CD1 . ILE A  1 222 ? -29.683 -16.226 5.027   1.00 12.32 ? 222  ILE A CD1 1 
ATOM   1784 N  N   . ASN A  1 223 ? -24.510 -15.178 5.923   1.00 9.57  ? 223  ASN A N   1 
ATOM   1785 C  CA  . ASN A  1 223 ? -23.105 -14.697 5.932   1.00 10.32 ? 223  ASN A CA  1 
ATOM   1786 C  C   . ASN A  1 223 ? -22.179 -15.560 5.072   1.00 10.79 ? 223  ASN A C   1 
ATOM   1787 O  O   . ASN A  1 223 ? -20.985 -15.264 5.075   1.00 11.26 ? 223  ASN A O   1 
ATOM   1788 C  CB  . ASN A  1 223 ? -22.621 -14.389 7.348   1.00 11.39 ? 223  ASN A CB  1 
ATOM   1789 C  CG  . ASN A  1 223 ? -22.270 -15.602 8.163   1.00 12.00 ? 223  ASN A CG  1 
ATOM   1790 O  OD1 . ASN A  1 223 ? -22.787 -16.681 7.899   1.00 11.06 ? 223  ASN A OD1 1 
ATOM   1791 N  ND2 . ASN A  1 223 ? -21.427 -15.399 9.174   1.00 13.15 ? 223  ASN A ND2 1 
ATOM   1792 N  N   . GLU A  1 224 ? -22.702 -16.483 4.268   1.00 10.78 ? 224  GLU A N   1 
ATOM   1793 C  CA  . GLU A  1 224 ? -22.001 -17.038 3.078   1.00 11.06 ? 224  GLU A CA  1 
ATOM   1794 C  C   . GLU A  1 224 ? -23.024 -17.325 1.988   1.00 10.68 ? 224  GLU A C   1 
ATOM   1795 O  O   . GLU A  1 224 ? -23.992 -18.032 2.288   1.00 11.35 ? 224  GLU A O   1 
ATOM   1796 C  CB  . GLU A  1 224 ? -21.193 -18.306 3.379   1.00 11.20 ? 224  GLU A CB  1 
ATOM   1797 C  CG  . GLU A  1 224 ? -20.308 -18.203 4.603   1.00 11.00 ? 224  GLU A CG  1 
ATOM   1798 C  CD  . GLU A  1 224 ? -19.474 -19.466 4.844   1.00 10.59 ? 224  GLU A CD  1 
ATOM   1799 O  OE1 . GLU A  1 224 ? -19.181 -20.201 3.851   1.00 10.83 ? 224  GLU A OE1 1 
ATOM   1800 O  OE2 . GLU A  1 224 ? -19.093 -19.722 6.041   1.00 10.10 ? 224  GLU A OE2 1 
ATOM   1801 N  N   . TYR A  1 225 ? -22.836 -16.787 0.778   1.00 10.73 ? 225  TYR A N   1 
ATOM   1802 C  CA  . TYR A  1 225 ? -23.755 -17.106 -0.328  1.00 10.17 ? 225  TYR A CA  1 
ATOM   1803 C  C   . TYR A  1 225 ? -22.974 -17.288 -1.612  1.00 10.29 ? 225  TYR A C   1 
ATOM   1804 O  O   . TYR A  1 225 ? -22.029 -16.551 -1.880  1.00 9.61  ? 225  TYR A O   1 
ATOM   1805 C  CB  . TYR A  1 225 ? -24.850 -16.041 -0.449  1.00 9.58  ? 225  TYR A CB  1 
ATOM   1806 C  CG  . TYR A  1 225 ? -24.470 -14.649 -0.894  1.00 8.86  ? 225  TYR A CG  1 
ATOM   1807 C  CD1 . TYR A  1 225 ? -24.384 -14.325 -2.241  1.00 9.68  ? 225  TYR A CD1 1 
ATOM   1808 C  CD2 . TYR A  1 225 ? -24.299 -13.621 0.021   1.00 9.23  ? 225  TYR A CD2 1 
ATOM   1809 C  CE1 . TYR A  1 225 ? -24.152 -13.024 -2.658  1.00 9.76  ? 225  TYR A CE1 1 
ATOM   1810 C  CE2 . TYR A  1 225 ? -24.003 -12.324 -0.382  1.00 9.07  ? 225  TYR A CE2 1 
ATOM   1811 C  CZ  . TYR A  1 225 ? -23.997 -12.015 -1.735  1.00 9.29  ? 225  TYR A CZ  1 
ATOM   1812 O  OH  . TYR A  1 225 ? -23.748 -10.727 -2.163  1.00 9.55  ? 225  TYR A OH  1 
ATOM   1813 N  N   A SER A  1 226 ? -23.369 -18.283 -2.404  0.75 10.42 ? 226  SER A N   1 
ATOM   1814 N  N   B SER A  1 226 ? -23.406 -18.247 -2.423  0.25 10.64 ? 226  SER A N   1 
ATOM   1815 C  CA  A SER A  1 226 ? -22.820 -18.505 -3.758  0.75 10.59 ? 226  SER A CA  1 
ATOM   1816 C  CA  B SER A  1 226 ? -22.787 -18.531 -3.733  0.25 11.01 ? 226  SER A CA  1 
ATOM   1817 C  C   A SER A  1 226 ? -23.680 -19.505 -4.505  0.75 11.09 ? 226  SER A C   1 
ATOM   1818 C  C   B SER A  1 226 ? -23.647 -19.522 -4.499  0.25 11.54 ? 226  SER A C   1 
ATOM   1819 O  O   A SER A  1 226 ? -24.397 -20.332 -3.865  0.75 11.26 ? 226  SER A O   1 
ATOM   1820 O  O   B SER A  1 226 ? -24.367 -20.328 -3.864  0.25 11.65 ? 226  SER A O   1 
ATOM   1821 C  CB  A SER A  1 226 ? -21.407 -19.003 -3.734  0.75 11.10 ? 226  SER A CB  1 
ATOM   1822 C  CB  B SER A  1 226 ? -21.396 -19.063 -3.568  0.25 11.12 ? 226  SER A CB  1 
ATOM   1823 O  OG  A SER A  1 226 ? -21.357 -20.343 -3.268  0.75 11.11 ? 226  SER A OG  1 
ATOM   1824 O  OG  B SER A  1 226 ? -20.851 -19.414 -4.826  0.25 10.92 ? 226  SER A OG  1 
ATOM   1825 N  N   . ASP A  1 227 ? -23.549 -19.451 -5.822  1.00 12.71 ? 227  ASP A N   1 
ATOM   1826 C  CA  . ASP A  1 227 ? -23.963 -20.553 -6.720  1.00 12.77 ? 227  ASP A CA  1 
ATOM   1827 C  C   . ASP A  1 227 ? -23.265 -21.835 -6.260  1.00 13.57 ? 227  ASP A C   1 
ATOM   1828 O  O   . ASP A  1 227 ? -22.151 -21.747 -5.740  1.00 13.85 ? 227  ASP A O   1 
ATOM   1829 C  CB  . ASP A  1 227 ? -23.580 -20.144 -8.135  1.00 14.80 ? 227  ASP A CB  1 
ATOM   1830 C  CG  . ASP A  1 227 ? -24.249 -20.972 -9.207  1.00 17.92 ? 227  ASP A CG  1 
ATOM   1831 O  OD1 . ASP A  1 227 ? -25.436 -20.763 -9.426  1.00 19.18 ? 227  ASP A OD1 1 
ATOM   1832 O  OD2 . ASP A  1 227 ? -23.585 -21.852 -9.754  1.00 17.12 ? 227  ASP A OD2 1 
ATOM   1833 N  N   . SER A  1 228 ? -23.823 -23.016 -6.574  1.00 14.27 ? 228  SER A N   1 
ATOM   1834 C  CA  . SER A  1 228 ? -23.114 -24.316 -6.387  1.00 17.04 ? 228  SER A CA  1 
ATOM   1835 C  C   . SER A  1 228 ? -21.788 -24.331 -7.150  1.00 16.65 ? 228  SER A C   1 
ATOM   1836 O  O   . SER A  1 228 ? -20.869 -24.966 -6.639  1.00 16.27 ? 228  SER A O   1 
ATOM   1837 C  CB  . SER A  1 228 ? -23.966 -25.481 -6.813  1.00 17.39 ? 228  SER A CB  1 
ATOM   1838 O  OG  . SER A  1 228 ? -25.121 -25.486 -6.009  1.00 23.61 ? 228  SER A OG  1 
ATOM   1839 N  N   . ASN A  1 229 ? -21.708 -23.663 -8.302  1.00 15.68 ? 229  ASN A N   1 
ATOM   1840 C  CA  . ASN A  1 229 ? -20.468 -23.590 -9.104  1.00 16.69 ? 229  ASN A CA  1 
ATOM   1841 C  C   . ASN A  1 229 ? -19.559 -22.532 -8.466  1.00 15.43 ? 229  ASN A C   1 
ATOM   1842 O  O   . ASN A  1 229 ? -19.880 -21.362 -8.594  1.00 14.13 ? 229  ASN A O   1 
ATOM   1843 C  CB  . ASN A  1 229 ? -20.722 -23.257 -10.566 1.00 18.70 ? 229  ASN A CB  1 
ATOM   1844 C  CG  . ASN A  1 229 ? -19.435 -23.244 -11.365 1.00 19.44 ? 229  ASN A CG  1 
ATOM   1845 O  OD1 . ASN A  1 229 ? -18.334 -23.448 -10.845 1.00 19.91 ? 229  ASN A OD1 1 
ATOM   1846 N  ND2 . ASN A  1 229 ? -19.561 -22.997 -12.655 1.00 29.52 ? 229  ASN A ND2 1 
ATOM   1847 N  N   . HIS A  1 230 ? -18.475 -22.941 -7.811  1.00 16.61 ? 230  HIS A N   1 
ATOM   1848 C  CA  . HIS A  1 230 ? -17.589 -22.012 -7.052  1.00 18.09 ? 230  HIS A CA  1 
ATOM   1849 C  C   . HIS A  1 230 ? -16.896 -21.033 -8.007  1.00 16.73 ? 230  HIS A C   1 
ATOM   1850 O  O   . HIS A  1 230 ? -16.520 -19.925 -7.557  1.00 14.33 ? 230  HIS A O   1 
ATOM   1851 C  CB  . HIS A  1 230 ? -16.601 -22.785 -6.198  1.00 18.42 ? 230  HIS A CB  1 
ATOM   1852 C  CG  . HIS A  1 230 ? -17.311 -23.631 -5.199  1.00 20.71 ? 230  HIS A CG  1 
ATOM   1853 N  ND1 . HIS A  1 230 ? -16.689 -24.654 -4.522  1.00 23.01 ? 230  HIS A ND1 1 
ATOM   1854 C  CD2 . HIS A  1 230 ? -18.602 -23.637 -4.799  1.00 24.97 ? 230  HIS A CD2 1 
ATOM   1855 C  CE1 . HIS A  1 230 ? -17.571 -25.251 -3.747  1.00 20.39 ? 230  HIS A CE1 1 
ATOM   1856 N  NE2 . HIS A  1 230 ? -18.750 -24.656 -3.892  1.00 24.15 ? 230  HIS A NE2 1 
ATOM   1857 N  N   . TYR A  1 231 ? -16.801 -21.366 -9.290  1.00 15.55 ? 231  TYR A N   1 
ATOM   1858 C  CA  . TYR A  1 231 ? -16.222 -20.451 -10.296 1.00 17.31 ? 231  TYR A CA  1 
ATOM   1859 C  C   . TYR A  1 231 ? -17.134 -19.230 -10.484 1.00 15.68 ? 231  TYR A C   1 
ATOM   1860 O  O   . TYR A  1 231 ? -16.671 -18.221 -11.020 1.00 14.56 ? 231  TYR A O   1 
ATOM   1861 C  CB  . TYR A  1 231 ? -15.962 -21.186 -11.611 1.00 19.88 ? 231  TYR A CB  1 
ATOM   1862 C  CG  . TYR A  1 231 ? -14.838 -22.196 -11.535 1.00 26.27 ? 231  TYR A CG  1 
ATOM   1863 C  CD1 . TYR A  1 231 ? -13.517 -21.784 -11.574 1.00 27.24 ? 231  TYR A CD1 1 
ATOM   1864 C  CD2 . TYR A  1 231 ? -15.094 -23.559 -11.399 1.00 30.30 ? 231  TYR A CD2 1 
ATOM   1865 C  CE1 . TYR A  1 231 ? -12.472 -22.690 -11.494 1.00 31.28 ? 231  TYR A CE1 1 
ATOM   1866 C  CE2 . TYR A  1 231 ? -14.059 -24.480 -11.322 1.00 33.38 ? 231  TYR A CE2 1 
ATOM   1867 C  CZ  . TYR A  1 231 ? -12.746 -24.040 -11.364 1.00 34.14 ? 231  TYR A CZ  1 
ATOM   1868 O  OH  . TYR A  1 231 ? -11.722 -24.946 -11.323 1.00 41.42 ? 231  TYR A OH  1 
ATOM   1869 N  N   . ALA A  1 232 ? -18.403 -19.310 -10.081 1.00 13.60 ? 232  ALA A N   1 
ATOM   1870 C  CA  . ALA A  1 232 ? -19.407 -18.233 -10.239 1.00 13.87 ? 232  ALA A CA  1 
ATOM   1871 C  C   . ALA A  1 232 ? -19.485 -17.328 -9.001  1.00 12.61 ? 232  ALA A C   1 
ATOM   1872 O  O   . ALA A  1 232 ? -20.292 -16.399 -8.998  1.00 12.64 ? 232  ALA A O   1 
ATOM   1873 C  CB  . ALA A  1 232 ? -20.772 -18.830 -10.514 1.00 14.66 ? 232  ALA A CB  1 
ATOM   1874 N  N   . GLU A  1 233 ? -18.696 -17.587 -7.983  1.00 12.98 ? 233  GLU A N   1 
ATOM   1875 C  CA  . GLU A  1 233 ? -18.540 -16.632 -6.855  1.00 13.00 ? 233  GLU A CA  1 
ATOM   1876 C  C   . GLU A  1 233 ? -18.183 -15.252 -7.425  1.00 13.03 ? 233  GLU A C   1 
ATOM   1877 O  O   . GLU A  1 233 ? -17.285 -15.165 -8.241  1.00 11.72 ? 233  GLU A O   1 
ATOM   1878 C  CB  . GLU A  1 233 ? -17.424 -17.107 -5.932  1.00 13.15 ? 233  GLU A CB  1 
ATOM   1879 C  CG  . GLU A  1 233 ? -17.263 -16.271 -4.695  1.00 12.89 ? 233  GLU A CG  1 
ATOM   1880 C  CD  . GLU A  1 233 ? -16.129 -16.741 -3.800  1.00 12.56 ? 233  GLU A CD  1 
ATOM   1881 O  OE1 . GLU A  1 233 ? -16.320 -17.741 -3.081  1.00 12.59 ? 233  GLU A OE1 1 
ATOM   1882 O  OE2 . GLU A  1 233 ? -15.054 -16.083 -3.825  1.00 14.47 ? 233  GLU A OE2 1 
ATOM   1883 N  N   . GLY A  1 234 ? -18.860 -14.192 -7.006  1.00 12.60 ? 234  GLY A N   1 
ATOM   1884 C  CA  . GLY A  1 234 ? -18.548 -12.838 -7.492  1.00 13.05 ? 234  GLY A CA  1 
ATOM   1885 C  C   . GLY A  1 234 ? -18.942 -12.611 -8.951  1.00 12.32 ? 234  GLY A C   1 
ATOM   1886 O  O   . GLY A  1 234 ? -18.637 -11.527 -9.475  1.00 13.06 ? 234  GLY A O   1 
ATOM   1887 N  N   . GLN A  1 235 ? -19.597 -13.576 -9.609  1.00 11.74 ? 235  GLN A N   1 
ATOM   1888 C  CA  . GLN A  1 235 ? -20.032 -13.398 -11.021 1.00 11.73 ? 235  GLN A CA  1 
ATOM   1889 C  C   . GLN A  1 235 ? -21.267 -12.505 -11.025 1.00 11.26 ? 235  GLN A C   1 
ATOM   1890 O  O   . GLN A  1 235 ? -22.174 -12.734 -10.229 1.00 12.38 ? 235  GLN A O   1 
ATOM   1891 C  CB  . GLN A  1 235 ? -20.402 -14.732 -11.654 1.00 12.10 ? 235  GLN A CB  1 
ATOM   1892 C  CG  . GLN A  1 235 ? -20.765 -14.603 -13.121 1.00 12.02 ? 235  GLN A CG  1 
ATOM   1893 C  CD  . GLN A  1 235 ? -21.458 -15.856 -13.557 1.00 13.14 ? 235  GLN A CD  1 
ATOM   1894 O  OE1 . GLN A  1 235 ? -22.678 -15.987 -13.427 1.00 13.48 ? 235  GLN A OE1 1 
ATOM   1895 N  NE2 . GLN A  1 235 ? -20.664 -16.830 -13.979 1.00 12.69 ? 235  GLN A NE2 1 
ATOM   1896 N  N   . PRO A  1 236 ? -21.357 -11.453 -11.861 1.00 11.95 ? 236  PRO A N   1 
ATOM   1897 C  CA  . PRO A  1 236 ? -22.531 -10.568 -11.832 1.00 11.60 ? 236  PRO A CA  1 
ATOM   1898 C  C   . PRO A  1 236 ? -23.864 -11.291 -12.029 1.00 12.16 ? 236  PRO A C   1 
ATOM   1899 O  O   . PRO A  1 236 ? -24.753 -11.124 -11.203 1.00 12.30 ? 236  PRO A O   1 
ATOM   1900 C  CB  . PRO A  1 236 ? -22.283 -9.567  -12.961 1.00 12.32 ? 236  PRO A CB  1 
ATOM   1901 C  CG  . PRO A  1 236 ? -20.754 -9.549  -13.084 1.00 12.89 ? 236  PRO A CG  1 
ATOM   1902 C  CD  . PRO A  1 236 ? -20.291 -10.952 -12.729 1.00 12.77 ? 236  PRO A CD  1 
ATOM   1903 N  N   . GLY A  1 237 ? -23.977 -12.112 -13.076 1.00 11.34 ? 237  GLY A N   1 
ATOM   1904 C  CA  . GLY A  1 237 ? -25.238 -12.807 -13.385 1.00 11.97 ? 237  GLY A CA  1 
ATOM   1905 C  C   . GLY A  1 237 ? -25.671 -13.724 -12.245 1.00 12.04 ? 237  GLY A C   1 
ATOM   1906 O  O   . GLY A  1 237 ? -26.838 -13.645 -11.786 1.00 11.41 ? 237  GLY A O   1 
ATOM   1907 N  N   . ALA A  1 238 ? -24.799 -14.623 -11.812 1.00 12.22 ? 238  ALA A N   1 
ATOM   1908 C  CA  . ALA A  1 238 ? -25.113 -15.555 -10.698 1.00 12.53 ? 238  ALA A CA  1 
ATOM   1909 C  C   . ALA A  1 238 ? -25.417 -14.768 -9.414  1.00 12.24 ? 238  ALA A C   1 
ATOM   1910 O  O   . ALA A  1 238 ? -26.247 -15.207 -8.617  1.00 13.49 ? 238  ALA A O   1 
ATOM   1911 C  CB  . ALA A  1 238 ? -23.967 -16.501 -10.468 1.00 13.82 ? 238  ALA A CB  1 
ATOM   1912 N  N   . SER A  1 239 ? -24.763 -13.628 -9.197  1.00 11.41 ? 239  SER A N   1 
ATOM   1913 C  CA  . SER A  1 239 ? -24.892 -12.860 -7.928  1.00 10.78 ? 239  SER A CA  1 
ATOM   1914 C  C   . SER A  1 239 ? -26.247 -12.131 -7.896  1.00 10.54 ? 239  SER A C   1 
ATOM   1915 O  O   . SER A  1 239 ? -26.809 -11.944 -6.807  1.00 10.53 ? 239  SER A O   1 
ATOM   1916 C  CB  . SER A  1 239 ? -23.766 -11.879 -7.752  1.00 11.30 ? 239  SER A CB  1 
ATOM   1917 O  OG  . SER A  1 239 ? -22.523 -12.570 -7.646  1.00 12.96 ? 239  SER A OG  1 
ATOM   1918 N  N   . ALA A  1 240 ? -26.751 -11.648 -9.023  1.00 10.12 ? 240  ALA A N   1 
ATOM   1919 C  CA  . ALA A  1 240 ? -27.917 -10.744 -8.969  1.00 10.70 ? 240  ALA A CA  1 
ATOM   1920 C  C   . ALA A  1 240 ? -29.132 -11.388 -8.284  1.00 10.82 ? 240  ALA A C   1 
ATOM   1921 O  O   . ALA A  1 240 ? -29.813 -10.711 -7.492  1.00 11.37 ? 240  ALA A O   1 
ATOM   1922 C  CB  . ALA A  1 240 ? -28.205 -10.192 -10.338 1.00 11.08 ? 240  ALA A CB  1 
ATOM   1923 N  N   . PRO A  1 241 ? -29.507 -12.651 -8.546  1.00 11.63 ? 241  PRO A N   1 
ATOM   1924 C  CA  . PRO A  1 241 ? -30.675 -13.222 -7.879  1.00 11.04 ? 241  PRO A CA  1 
ATOM   1925 C  C   . PRO A  1 241 ? -30.489 -13.336 -6.352  1.00 10.81 ? 241  PRO A C   1 
ATOM   1926 O  O   . PRO A  1 241 ? -31.466 -13.255 -5.620  1.00 10.72 ? 241  PRO A O   1 
ATOM   1927 C  CB  . PRO A  1 241 ? -30.837 -14.582 -8.561  1.00 12.30 ? 241  PRO A CB  1 
ATOM   1928 C  CG  . PRO A  1 241 ? -30.280 -14.342 -9.949  1.00 11.62 ? 241  PRO A CG  1 
ATOM   1929 C  CD  . PRO A  1 241 ? -29.039 -13.519 -9.648  1.00 11.35 ? 241  PRO A CD  1 
ATOM   1930 N  N   . PHE A  1 242 ? -29.272 -13.557 -5.895  1.00 9.73  ? 242  PHE A N   1 
ATOM   1931 C  CA  . PHE A  1 242 ? -28.989 -13.574 -4.436  1.00 9.40  ? 242  PHE A CA  1 
ATOM   1932 C  C   . PHE A  1 242 ? -29.361 -12.208 -3.862  1.00 9.91  ? 242  PHE A C   1 
ATOM   1933 O  O   . PHE A  1 242 ? -30.194 -12.064 -2.943  1.00 10.83 ? 242  PHE A O   1 
ATOM   1934 C  CB  . PHE A  1 242 ? -27.517 -13.914 -4.156  1.00 9.53  ? 242  PHE A CB  1 
ATOM   1935 C  CG  . PHE A  1 242 ? -27.193 -15.358 -4.378  1.00 9.85  ? 242  PHE A CG  1 
ATOM   1936 C  CD1 . PHE A  1 242 ? -27.339 -16.281 -3.361  1.00 9.95  ? 242  PHE A CD1 1 
ATOM   1937 C  CD2 . PHE A  1 242 ? -26.764 -15.805 -5.614  1.00 10.71 ? 242  PHE A CD2 1 
ATOM   1938 C  CE1 . PHE A  1 242 ? -26.982 -17.603 -3.574  1.00 10.29 ? 242  PHE A CE1 1 
ATOM   1939 C  CE2 . PHE A  1 242 ? -26.460 -17.137 -5.839  1.00 10.45 ? 242  PHE A CE2 1 
ATOM   1940 C  CZ  . PHE A  1 242 ? -26.579 -18.032 -4.809  1.00 10.02 ? 242  PHE A CZ  1 
ATOM   1941 N  N   . ILE A  1 243 ? -28.725 -11.169 -4.385  1.00 9.65  ? 243  ILE A N   1 
ATOM   1942 C  CA  . ILE A  1 243 ? -28.931 -9.784  -3.907  1.00 9.71  ? 243  ILE A CA  1 
ATOM   1943 C  C   . ILE A  1 243 ? -30.421 -9.431  -3.985  1.00 9.59  ? 243  ILE A C   1 
ATOM   1944 O  O   . ILE A  1 243 ? -30.959 -8.850  -3.006  1.00 9.44  ? 243  ILE A O   1 
ATOM   1945 C  CB  . ILE A  1 243 ? -28.086 -8.782  -4.705  1.00 9.98  ? 243  ILE A CB  1 
ATOM   1946 C  CG1 . ILE A  1 243 ? -26.591 -9.103  -4.620  1.00 9.87  ? 243  ILE A CG1 1 
ATOM   1947 C  CG2 . ILE A  1 243 ? -28.377 -7.372  -4.231  1.00 9.70  ? 243  ILE A CG2 1 
ATOM   1948 C  CD1 . ILE A  1 243 ? -25.778 -8.408  -5.650  1.00 10.42 ? 243  ILE A CD1 1 
ATOM   1949 N  N   . ALA A  1 244 ? -31.047 -9.752  -5.106  1.00 9.79  ? 244  ALA A N   1 
ATOM   1950 C  CA  . ALA A  1 244 ? -32.485 -9.475  -5.354  1.00 9.77  ? 244  ALA A CA  1 
ATOM   1951 C  C   . ALA A  1 244 ? -33.342 -10.075 -4.239  1.00 9.78  ? 244  ALA A C   1 
ATOM   1952 O  O   . ALA A  1 244 ? -34.201 -9.350  -3.672  1.00 9.41  ? 244  ALA A O   1 
ATOM   1953 C  CB  . ALA A  1 244 ? -32.909 -10.031 -6.686  1.00 10.52 ? 244  ALA A CB  1 
ATOM   1954 N  N   . LYS A  1 245 ? -33.074 -11.322 -3.903  1.00 10.56 ? 245  LYS A N   1 
ATOM   1955 C  CA  . LYS A  1 245 ? -33.894 -12.060 -2.917  1.00 10.49 ? 245  LYS A CA  1 
ATOM   1956 C  C   . LYS A  1 245 ? -33.606 -11.543 -1.505  1.00 10.08 ? 245  LYS A C   1 
ATOM   1957 O  O   . LYS A  1 245 ? -34.545 -11.440 -0.706  1.00 11.64 ? 245  LYS A O   1 
ATOM   1958 C  CB  . LYS A  1 245 ? -33.719 -13.553 -3.117  1.00 10.97 ? 245  LYS A CB  1 
ATOM   1959 C  CG  . LYS A  1 245 ? -34.269 -14.043 -4.452  1.00 11.94 ? 245  LYS A CG  1 
ATOM   1960 C  CD  . LYS A  1 245 ? -33.961 -15.464 -4.757  1.00 12.69 ? 245  LYS A CD  1 
ATOM   1961 C  CE  . LYS A  1 245 ? -33.920 -15.716 -6.256  1.00 13.64 ? 245  LYS A CE  1 
ATOM   1962 N  NZ  . LYS A  1 245 ? -35.155 -15.255 -6.945  1.00 13.43 ? 245  LYS A NZ  1 
ATOM   1963 N  N   . PHE A  1 246 ? -32.345 -11.223 -1.205  1.00 9.63  ? 246  PHE A N   1 
ATOM   1964 C  CA  . PHE A  1 246 ? -31.962 -10.653 0.106   1.00 10.28 ? 246  PHE A CA  1 
ATOM   1965 C  C   . PHE A  1 246 ? -32.678 -9.302  0.267   1.00 9.90  ? 246  PHE A C   1 
ATOM   1966 O  O   . PHE A  1 246 ? -33.212 -8.981  1.344   1.00 11.43 ? 246  PHE A O   1 
ATOM   1967 C  CB  . PHE A  1 246 ? -30.447 -10.553 0.201   1.00 10.17 ? 246  PHE A CB  1 
ATOM   1968 C  CG  . PHE A  1 246 ? -29.726 -11.870 0.159   1.00 10.46 ? 246  PHE A CG  1 
ATOM   1969 C  CD1 . PHE A  1 246 ? -30.302 -13.025 0.671   1.00 11.18 ? 246  PHE A CD1 1 
ATOM   1970 C  CD2 . PHE A  1 246 ? -28.431 -11.931 -0.333  1.00 10.68 ? 246  PHE A CD2 1 
ATOM   1971 C  CE1 . PHE A  1 246 ? -29.607 -14.217 0.652   1.00 11.61 ? 246  PHE A CE1 1 
ATOM   1972 C  CE2 . PHE A  1 246 ? -27.760 -13.143 -0.376  1.00 11.86 ? 246  PHE A CE2 1 
ATOM   1973 C  CZ  . PHE A  1 246 ? -28.340 -14.273 0.123   1.00 11.66 ? 246  PHE A CZ  1 
ATOM   1974 N  N   . GLU A  1 247 ? -32.671 -8.478  -0.778  1.00 10.09 ? 247  GLU A N   1 
ATOM   1975 C  CA  . GLU A  1 247 ? -33.297 -7.141  -0.708  1.00 10.30 ? 247  GLU A CA  1 
ATOM   1976 C  C   . GLU A  1 247 ? -34.815 -7.331  -0.593  1.00 11.12 ? 247  GLU A C   1 
ATOM   1977 O  O   . GLU A  1 247 ? -35.427 -6.672  0.245   1.00 11.37 ? 247  GLU A O   1 
ATOM   1978 C  CB  . GLU A  1 247 ? -32.868 -6.287  -1.906  1.00 10.39 ? 247  GLU A CB  1 
ATOM   1979 C  CG  . GLU A  1 247 ? -31.424 -5.823  -1.800  1.00 10.39 ? 247  GLU A CG  1 
ATOM   1980 C  CD  . GLU A  1 247 ? -31.133 -4.694  -0.830  1.00 10.78 ? 247  GLU A CD  1 
ATOM   1981 O  OE1 . GLU A  1 247 ? -32.087 -4.205  -0.153  1.00 11.44 ? 247  GLU A OE1 1 
ATOM   1982 O  OE2 . GLU A  1 247 ? -29.916 -4.341  -0.688  1.00 11.83 ? 247  GLU A OE2 1 
ATOM   1983 N  N   . ARG A  1 248 ? -35.392 -8.229  -1.384  1.00 11.56 ? 248  ARG A N   1 
ATOM   1984 C  CA  . ARG A  1 248 ? -36.869 -8.434  -1.388  1.00 13.06 ? 248  ARG A CA  1 
ATOM   1985 C  C   . ARG A  1 248 ? -37.337 -8.838  0.013   1.00 13.32 ? 248  ARG A C   1 
ATOM   1986 O  O   . ARG A  1 248 ? -38.418 -8.398  0.454   1.00 12.57 ? 248  ARG A O   1 
ATOM   1987 C  CB  . ARG A  1 248 ? -37.239 -9.503  -2.407  1.00 14.25 ? 248  ARG A CB  1 
ATOM   1988 C  CG  . ARG A  1 248 ? -38.739 -9.795  -2.512  1.00 15.98 ? 248  ARG A CG  1 
ATOM   1989 C  CD  . ARG A  1 248 ? -38.989 -10.906 -3.559  1.00 16.59 ? 248  ARG A CD  1 
ATOM   1990 N  NE  . ARG A  1 248 ? -38.611 -10.331 -4.803  1.00 17.31 ? 248  ARG A NE  1 
ATOM   1991 C  CZ  . ARG A  1 248 ? -37.630 -10.724 -5.593  1.00 16.87 ? 248  ARG A CZ  1 
ATOM   1992 N  NH1 . ARG A  1 248 ? -37.018 -11.890 -5.450  1.00 15.69 ? 248  ARG A NH1 1 
ATOM   1993 N  NH2 . ARG A  1 248 ? -37.359 -9.957  -6.623  1.00 16.46 ? 248  ARG A NH2 1 
ATOM   1994 N  N   . ASN A  1 249 ? -36.556 -9.669  0.698   1.00 13.62 ? 249  ASN A N   1 
ATOM   1995 C  CA  . ASN A  1 249 ? -36.895 -10.207 2.036   1.00 12.92 ? 249  ASN A CA  1 
ATOM   1996 C  C   . ASN A  1 249 ? -36.327 -9.362  3.177   1.00 12.66 ? 249  ASN A C   1 
ATOM   1997 O  O   . ASN A  1 249 ? -36.477 -9.784  4.327   1.00 12.77 ? 249  ASN A O   1 
ATOM   1998 C  CB  . ASN A  1 249 ? -36.416 -11.651 2.099   1.00 13.16 ? 249  ASN A CB  1 
ATOM   1999 C  CG  . ASN A  1 249 ? -37.269 -12.554 1.243   1.00 15.15 ? 249  ASN A CG  1 
ATOM   2000 O  OD1 . ASN A  1 249 ? -38.363 -12.904 1.661   1.00 15.71 ? 249  ASN A OD1 1 
ATOM   2001 N  ND2 . ASN A  1 249 ? -36.817 -12.907 0.043   1.00 13.97 ? 249  ASN A ND2 1 
ATOM   2002 N  N   A LYS A  1 250 ? -35.731 -8.203  2.877   0.50 11.93 ? 250  LYS A N   1 
ATOM   2003 N  N   B LYS A  1 250 ? -35.695 -8.227  2.867   0.50 12.03 ? 250  LYS A N   1 
ATOM   2004 C  CA  A LYS A  1 250 ? -35.225 -7.202  3.861   0.50 12.66 ? 250  LYS A CA  1 
ATOM   2005 C  CA  B LYS A  1 250 ? -35.223 -7.211  3.847   0.50 12.87 ? 250  LYS A CA  1 
ATOM   2006 C  C   A LYS A  1 250 ? -34.231 -7.882  4.807   0.50 12.26 ? 250  LYS A C   1 
ATOM   2007 C  C   B LYS A  1 250 ? -34.234 -7.880  4.805   0.50 12.38 ? 250  LYS A C   1 
ATOM   2008 O  O   A LYS A  1 250 ? -34.300 -7.658  6.032   0.50 12.69 ? 250  LYS A O   1 
ATOM   2009 O  O   B LYS A  1 250 ? -34.306 -7.648  6.028   0.50 12.82 ? 250  LYS A O   1 
ATOM   2010 C  CB  A LYS A  1 250 ? -36.387 -6.522  4.588   0.50 13.43 ? 250  LYS A CB  1 
ATOM   2011 C  CB  B LYS A  1 250 ? -36.440 -6.543  4.489   0.50 13.84 ? 250  LYS A CB  1 
ATOM   2012 C  CG  A LYS A  1 250 ? -37.244 -5.632  3.692   0.50 13.99 ? 250  LYS A CG  1 
ATOM   2013 C  CG  B LYS A  1 250 ? -37.357 -5.895  3.458   0.50 14.45 ? 250  LYS A CG  1 
ATOM   2014 C  CD  A LYS A  1 250 ? -38.338 -4.884  4.425   0.50 14.42 ? 250  LYS A CD  1 
ATOM   2015 C  CD  B LYS A  1 250 ? -38.689 -5.393  3.980   0.50 15.41 ? 250  LYS A CD  1 
ATOM   2016 C  CE  A LYS A  1 250 ? -39.202 -5.815  5.249   0.50 15.89 ? 250  LYS A CE  1 
ATOM   2017 C  CE  B LYS A  1 250 ? -38.554 -4.616  5.261   0.50 16.01 ? 250  LYS A CE  1 
ATOM   2018 N  NZ  A LYS A  1 250 ? -40.418 -5.155  5.788   0.50 17.18 ? 250  LYS A NZ  1 
ATOM   2019 N  NZ  B LYS A  1 250 ? -39.822 -3.914  5.571   0.50 17.23 ? 250  LYS A NZ  1 
ATOM   2020 N  N   . VAL A  1 251 ? -33.344 -8.687  4.233   1.00 12.47 ? 251  VAL A N   1 
ATOM   2021 C  CA  . VAL A  1 251 ? -32.248 -9.355  4.972   1.00 12.97 ? 251  VAL A CA  1 
ATOM   2022 C  C   . VAL A  1 251 ? -31.344 -8.269  5.556   1.00 12.01 ? 251  VAL A C   1 
ATOM   2023 O  O   . VAL A  1 251 ? -31.107 -7.205  4.871   1.00 11.23 ? 251  VAL A O   1 
ATOM   2024 C  CB  . VAL A  1 251 ? -31.524 -10.332 4.032   1.00 14.66 ? 251  VAL A CB  1 
ATOM   2025 C  CG1 . VAL A  1 251 ? -30.178 -10.715 4.556   1.00 16.23 ? 251  VAL A CG1 1 
ATOM   2026 C  CG2 . VAL A  1 251 ? -32.376 -11.566 3.756   1.00 14.70 ? 251  VAL A CG2 1 
ATOM   2027 N  N   . ASP A  1 252 ? -30.941 -8.440  6.809   1.00 11.57 ? 252  ASP A N   1 
ATOM   2028 C  CA  . ASP A  1 252 ? -30.110 -7.425  7.526   1.00 12.10 ? 252  ASP A CA  1 
ATOM   2029 C  C   . ASP A  1 252 ? -28.726 -7.377  6.882   1.00 11.32 ? 252  ASP A C   1 
ATOM   2030 O  O   . ASP A  1 252 ? -28.222 -6.252  6.618   1.00 11.24 ? 252  ASP A O   1 
ATOM   2031 C  CB  . ASP A  1 252 ? -29.987 -7.705  9.014   1.00 12.12 ? 252  ASP A CB  1 
ATOM   2032 C  CG  . ASP A  1 252 ? -29.443 -6.500  9.763   1.00 15.04 ? 252  ASP A CG  1 
ATOM   2033 O  OD1 . ASP A  1 252 ? -30.136 -5.446  9.796   1.00 16.54 ? 252  ASP A OD1 1 
ATOM   2034 O  OD2 . ASP A  1 252 ? -28.325 -6.586  10.289  1.00 15.90 ? 252  ASP A OD2 1 
ATOM   2035 N  N   . SER A  1 253 ? -28.136 -8.534  6.610   1.00 10.73 ? 253  SER A N   1 
ATOM   2036 C  CA  . SER A  1 253 ? -26.804 -8.597  5.962   1.00 11.03 ? 253  SER A CA  1 
ATOM   2037 C  C   . SER A  1 253 ? -26.629 -9.931  5.256   1.00 10.27 ? 253  SER A C   1 
ATOM   2038 O  O   . SER A  1 253 ? -27.306 -10.920 5.611   1.00 10.34 ? 253  SER A O   1 
ATOM   2039 C  CB  . SER A  1 253 ? -25.682 -8.355  6.916   1.00 11.18 ? 253  SER A CB  1 
ATOM   2040 O  OG  . SER A  1 253 ? -25.617 -9.367  7.908   1.00 11.50 ? 253  SER A OG  1 
ATOM   2041 N  N   . ALA A  1 254 ? -25.812 -9.915  4.208   1.00 10.23 ? 254  ALA A N   1 
ATOM   2042 C  CA  . ALA A  1 254 ? -25.369 -11.140 3.523   1.00 10.32 ? 254  ALA A CA  1 
ATOM   2043 C  C   . ALA A  1 254 ? -23.920 -10.957 3.049   1.00 10.46 ? 254  ALA A C   1 
ATOM   2044 O  O   . ALA A  1 254 ? -23.563 -9.870  2.604   1.00 10.86 ? 254  ALA A O   1 
ATOM   2045 C  CB  . ALA A  1 254 ? -26.334 -11.522 2.415   1.00 11.29 ? 254  ALA A CB  1 
ATOM   2046 N  N   . CYS A  1 255 ? -23.136 -12.023 3.115   1.00 10.89 ? 255  CYS A N   1 
ATOM   2047 C  CA  . CYS A  1 255 ? -21.710 -12.019 2.730   1.00 11.05 ? 255  CYS A CA  1 
ATOM   2048 C  C   . CYS A  1 255 ? -21.448 -13.080 1.666   1.00 10.89 ? 255  CYS A C   1 
ATOM   2049 O  O   . CYS A  1 255 ? -21.899 -14.240 1.831   1.00 9.68  ? 255  CYS A O   1 
ATOM   2050 C  CB  . CYS A  1 255 ? -20.787 -12.303 3.897   1.00 12.13 ? 255  CYS A CB  1 
ATOM   2051 S  SG  . CYS A  1 255 ? -21.062 -11.292 5.375   1.00 12.39 ? 255  CYS A SG  1 
ATOM   2052 N  N   . ILE A  1 256 ? -20.709 -12.698 0.627   1.00 10.54 ? 256  ILE A N   1 
ATOM   2053 C  CA  . ILE A  1 256 ? -20.228 -13.645 -0.419  1.00 10.60 ? 256  ILE A CA  1 
ATOM   2054 C  C   . ILE A  1 256 ? -19.353 -14.690 0.275   1.00 10.91 ? 256  ILE A C   1 
ATOM   2055 O  O   . ILE A  1 256 ? -18.650 -14.354 1.264   1.00 10.29 ? 256  ILE A O   1 
ATOM   2056 C  CB  . ILE A  1 256 ? -19.500 -12.884 -1.550  1.00 11.07 ? 256  ILE A CB  1 
ATOM   2057 C  CG1 . ILE A  1 256 ? -20.428 -11.856 -2.208  1.00 10.00 ? 256  ILE A CG1 1 
ATOM   2058 C  CG2 . ILE A  1 256 ? -18.951 -13.841 -2.579  1.00 11.08 ? 256  ILE A CG2 1 
ATOM   2059 C  CD1 . ILE A  1 256 ? -19.708 -10.825 -3.092  1.00 10.81 ? 256  ILE A CD1 1 
ATOM   2060 N  N   . SER A  1 257 ? -19.415 -15.918 -0.254  1.00 11.13 ? 257  SER A N   1 
ATOM   2061 C  CA  . SER A  1 257 ? -18.554 -17.058 0.099   1.00 10.89 ? 257  SER A CA  1 
ATOM   2062 C  C   . SER A  1 257 ? -17.065 -16.720 -0.051  1.00 10.40 ? 257  SER A C   1 
ATOM   2063 O  O   . SER A  1 257 ? -16.650 -15.731 -0.696  1.00 10.45 ? 257  SER A O   1 
ATOM   2064 C  CB  . SER A  1 257 ? -18.947 -18.214 -0.771  1.00 11.04 ? 257  SER A CB  1 
ATOM   2065 O  OG  . SER A  1 257 ? -18.788 -17.868 -2.156  1.00 12.41 ? 257  SER A OG  1 
ATOM   2066 N  N   . TRP A  1 258 ? -16.264 -17.639 0.443   1.00 10.02 ? 258  TRP A N   1 
ATOM   2067 C  CA  . TRP A  1 258 ? -14.798 -17.651 0.260   1.00 10.69 ? 258  TRP A CA  1 
ATOM   2068 C  C   . TRP A  1 258 ? -14.369 -19.051 -0.171  1.00 11.68 ? 258  TRP A C   1 
ATOM   2069 O  O   . TRP A  1 258 ? -13.908 -19.813 0.698   1.00 12.42 ? 258  TRP A O   1 
ATOM   2070 C  CB  . TRP A  1 258 ? -14.095 -17.229 1.546   1.00 10.84 ? 258  TRP A CB  1 
ATOM   2071 C  CG  . TRP A  1 258 ? -12.598 -17.156 1.417   1.00 11.38 ? 258  TRP A CG  1 
ATOM   2072 C  CD1 . TRP A  1 258 ? -11.881 -16.615 0.391   1.00 12.88 ? 258  TRP A CD1 1 
ATOM   2073 C  CD2 . TRP A  1 258 ? -11.641 -17.689 2.342   1.00 12.06 ? 258  TRP A CD2 1 
ATOM   2074 N  NE1 . TRP A  1 258 ? -10.532 -16.751 0.630   1.00 13.58 ? 258  TRP A NE1 1 
ATOM   2075 C  CE2 . TRP A  1 258 ? -10.357 -17.385 1.828   1.00 13.44 ? 258  TRP A CE2 1 
ATOM   2076 C  CE3 . TRP A  1 258 ? -11.742 -18.372 3.562   1.00 12.99 ? 258  TRP A CE3 1 
ATOM   2077 C  CZ2 . TRP A  1 258 ? -9.183  -17.774 2.480   1.00 14.50 ? 258  TRP A CZ2 1 
ATOM   2078 C  CZ3 . TRP A  1 258 ? -10.574 -18.759 4.206   1.00 14.07 ? 258  TRP A CZ3 1 
ATOM   2079 C  CH2 . TRP A  1 258 ? -9.323  -18.439 3.687   1.00 14.85 ? 258  TRP A CH2 1 
ATOM   2080 N  N   . TRP A  1 259 ? -14.561 -19.372 -1.450  1.00 12.27 ? 259  TRP A N   1 
ATOM   2081 C  CA  . TRP A  1 259 ? -14.248 -20.720 -1.985  1.00 13.50 ? 259  TRP A CA  1 
ATOM   2082 C  C   . TRP A  1 259 ? -12.767 -20.798 -2.340  1.00 14.82 ? 259  TRP A C   1 
ATOM   2083 O  O   . TRP A  1 259 ? -12.236 -21.934 -2.292  1.00 16.02 ? 259  TRP A O   1 
ATOM   2084 C  CB  . TRP A  1 259 ? -15.123 -21.054 -3.189  1.00 14.38 ? 259  TRP A CB  1 
ATOM   2085 C  CG  . TRP A  1 259 ? -16.543 -21.355 -2.806  1.00 16.29 ? 259  TRP A CG  1 
ATOM   2086 C  CD1 . TRP A  1 259 ? -17.705 -20.696 -3.137  1.00 17.80 ? 259  TRP A CD1 1 
ATOM   2087 C  CD2 . TRP A  1 259 ? -16.939 -22.415 -1.920  1.00 18.92 ? 259  TRP A CD2 1 
ATOM   2088 N  NE1 . TRP A  1 259 ? -18.780 -21.301 -2.525  1.00 18.95 ? 259  TRP A NE1 1 
ATOM   2089 C  CE2 . TRP A  1 259 ? -18.346 -22.349 -1.772  1.00 19.83 ? 259  TRP A CE2 1 
ATOM   2090 C  CE3 . TRP A  1 259 ? -16.242 -23.452 -1.294  1.00 20.06 ? 259  TRP A CE3 1 
ATOM   2091 C  CZ2 . TRP A  1 259 ? -19.059 -23.304 -1.040  1.00 21.83 ? 259  TRP A CZ2 1 
ATOM   2092 C  CZ3 . TRP A  1 259 ? -16.936 -24.365 -0.532  1.00 21.64 ? 259  TRP A CZ3 1 
ATOM   2093 C  CH2 . TRP A  1 259 ? -18.325 -24.279 -0.400  1.00 23.30 ? 259  TRP A CH2 1 
ATOM   2094 N  N   . TRP A  1 260 ? -12.123 -19.672 -2.635  1.00 14.21 ? 260  TRP A N   1 
ATOM   2095 C  CA  . TRP A  1 260 ? -10.757 -19.656 -3.234  1.00 14.95 ? 260  TRP A CA  1 
ATOM   2096 C  C   . TRP A  1 260 ? -9.749  -19.254 -2.152  1.00 14.16 ? 260  TRP A C   1 
ATOM   2097 O  O   . TRP A  1 260 ? -9.386  -18.062 -2.050  1.00 13.94 ? 260  TRP A O   1 
ATOM   2098 C  CB  . TRP A  1 260 ? -10.750 -18.820 -4.516  1.00 15.55 ? 260  TRP A CB  1 
ATOM   2099 C  CG  . TRP A  1 260 ? -11.799 -19.327 -5.460  1.00 15.72 ? 260  TRP A CG  1 
ATOM   2100 C  CD1 . TRP A  1 260 ? -13.066 -18.821 -5.654  1.00 16.72 ? 260  TRP A CD1 1 
ATOM   2101 C  CD2 . TRP A  1 260 ? -11.731 -20.543 -6.227  1.00 17.31 ? 260  TRP A CD2 1 
ATOM   2102 N  NE1 . TRP A  1 260 ? -13.760 -19.619 -6.534  1.00 16.67 ? 260  TRP A NE1 1 
ATOM   2103 C  CE2 . TRP A  1 260 ? -12.969 -20.682 -6.899  1.00 18.46 ? 260  TRP A CE2 1 
ATOM   2104 C  CE3 . TRP A  1 260 ? -10.736 -21.522 -6.440  1.00 19.18 ? 260  TRP A CE3 1 
ATOM   2105 C  CZ2 . TRP A  1 260 ? -13.229 -21.761 -7.756  1.00 19.29 ? 260  TRP A CZ2 1 
ATOM   2106 C  CZ3 . TRP A  1 260 ? -10.989 -22.567 -7.311  1.00 21.64 ? 260  TRP A CZ3 1 
ATOM   2107 C  CH2 . TRP A  1 260 ? -12.223 -22.681 -7.955  1.00 20.90 ? 260  TRP A CH2 1 
ATOM   2108 N  N   . THR A  1 261 ? -9.348  -20.256 -1.358  1.00 15.53 ? 261  THR A N   1 
ATOM   2109 C  CA  A THR A  1 261 ? -8.615  -20.001 -0.091  0.80 17.08 ? 261  THR A CA  1 
ATOM   2110 C  CA  B THR A  1 261 ? -8.550  -20.142 -0.112  0.20 15.34 ? 261  THR A CA  1 
ATOM   2111 C  C   . THR A  1 261 ? -7.183  -19.517 -0.395  1.00 15.54 ? 261  THR A C   1 
ATOM   2112 O  O   . THR A  1 261 ? -6.603  -18.934 0.519   1.00 15.23 ? 261  THR A O   1 
ATOM   2113 C  CB  A THR A  1 261 ? -8.705  -21.172 0.895   0.80 19.13 ? 261  THR A CB  1 
ATOM   2114 C  CB  B THR A  1 261 ? -8.317  -21.521 0.518   0.20 15.03 ? 261  THR A CB  1 
ATOM   2115 O  OG1 A THR A  1 261 ? -8.201  -22.319 0.220   0.80 21.50 ? 261  THR A OG1 1 
ATOM   2116 O  OG1 B THR A  1 261 ? -9.516  -22.295 0.432   0.20 14.60 ? 261  THR A OG1 1 
ATOM   2117 C  CG2 A THR A  1 261 ? -10.126 -21.412 1.372   0.80 19.40 ? 261  THR A CG2 1 
ATOM   2118 C  CG2 B THR A  1 261 ? -7.870  -21.407 1.954   0.20 14.67 ? 261  THR A CG2 1 
ATOM   2119 N  N   . ASN A  1 262 ? -6.695  -19.640 -1.627  1.00 16.64 ? 262  ASN A N   1 
ATOM   2120 C  CA  . ASN A  1 262 ? -5.366  -19.065 -2.000  1.00 17.92 ? 262  ASN A CA  1 
ATOM   2121 C  C   . ASN A  1 262 ? -5.531  -17.576 -2.350  1.00 18.25 ? 262  ASN A C   1 
ATOM   2122 O  O   . ASN A  1 262 ? -4.512  -16.881 -2.564  1.00 17.15 ? 262  ASN A O   1 
ATOM   2123 C  CB  . ASN A  1 262 ? -4.661  -19.881 -3.098  1.00 19.37 ? 262  ASN A CB  1 
ATOM   2124 C  CG  . ASN A  1 262 ? -3.844  -21.033 -2.538  1.00 22.44 ? 262  ASN A CG  1 
ATOM   2125 O  OD1 . ASN A  1 262 ? -3.182  -20.868 -1.518  1.00 27.60 ? 262  ASN A OD1 1 
ATOM   2126 N  ND2 . ASN A  1 262 ? -3.898  -22.194 -3.176  1.00 22.68 ? 262  ASN A ND2 1 
ATOM   2127 N  N   . ALA A  1 263 ? -6.766  -17.059 -2.374  1.00 16.16 ? 263  ALA A N   1 
ATOM   2128 C  CA  . ALA A  1 263 ? -7.075  -15.674 -2.802  1.00 16.32 ? 263  ALA A CA  1 
ATOM   2129 C  C   . ALA A  1 263 ? -7.983  -14.991 -1.780  1.00 15.35 ? 263  ALA A C   1 
ATOM   2130 O  O   . ALA A  1 263 ? -9.020  -14.409 -2.123  1.00 15.55 ? 263  ALA A O   1 
ATOM   2131 C  CB  . ALA A  1 263 ? -7.682  -15.695 -4.188  1.00 15.74 ? 263  ALA A CB  1 
ATOM   2132 N  N   . PRO A  1 264 ? -7.557  -14.901 -0.510  1.00 15.92 ? 264  PRO A N   1 
ATOM   2133 C  CA  . PRO A  1 264 ? -8.297  -14.102 0.465   1.00 15.33 ? 264  PRO A CA  1 
ATOM   2134 C  C   . PRO A  1 264 ? -8.211  -12.645 0.024   1.00 14.65 ? 264  PRO A C   1 
ATOM   2135 O  O   . PRO A  1 264 ? -7.283  -12.278 -0.730  1.00 12.67 ? 264  PRO A O   1 
ATOM   2136 C  CB  . PRO A  1 264 ? -7.556  -14.322 1.773   1.00 16.74 ? 264  PRO A CB  1 
ATOM   2137 C  CG  . PRO A  1 264 ? -6.143  -14.594 1.320   1.00 16.09 ? 264  PRO A CG  1 
ATOM   2138 C  CD  . PRO A  1 264 ? -6.281  -15.398 0.040   1.00 15.45 ? 264  PRO A CD  1 
ATOM   2139 N  N   . GLY A  1 265 ? -9.166  -11.831 0.472   1.00 13.54 ? 265  GLY A N   1 
ATOM   2140 C  CA  . GLY A  1 265 ? -9.010  -10.371 0.344   1.00 12.74 ? 265  GLY A CA  1 
ATOM   2141 C  C   . GLY A  1 265 ? -9.403  -9.859  -1.035  1.00 12.24 ? 265  GLY A C   1 
ATOM   2142 O  O   . GLY A  1 265 ? -8.909  -8.732  -1.380  1.00 12.10 ? 265  GLY A O   1 
ATOM   2143 N  N   . ARG A  1 266 ? -10.248 -10.587 -1.790  1.00 11.07 ? 266  ARG A N   1 
ATOM   2144 C  CA  . ARG A  1 266 ? -10.710 -10.126 -3.125  1.00 11.73 ? 266  ARG A CA  1 
ATOM   2145 C  C   . ARG A  1 266 ? -12.208 -9.798  -3.090  1.00 10.90 ? 266  ARG A C   1 
ATOM   2146 O  O   . ARG A  1 266 ? -12.810 -9.778  -4.167  1.00 12.05 ? 266  ARG A O   1 
ATOM   2147 C  CB  . ARG A  1 266 ? -10.372 -11.128 -4.226  1.00 12.50 ? 266  ARG A CB  1 
ATOM   2148 C  CG  . ARG A  1 266 ? -8.863  -11.221 -4.420  1.00 13.70 ? 266  ARG A CG  1 
ATOM   2149 C  CD  . ARG A  1 266 ? -8.554  -11.999 -5.666  1.00 14.30 ? 266  ARG A CD  1 
ATOM   2150 N  NE  . ARG A  1 266 ? -7.119  -12.269 -5.690  1.00 15.97 ? 266  ARG A NE  1 
ATOM   2151 C  CZ  . ARG A  1 266 ? -6.577  -13.214 -6.447  1.00 16.43 ? 266  ARG A CZ  1 
ATOM   2152 N  NH1 . ARG A  1 266 ? -7.306  -13.908 -7.303  1.00 16.39 ? 266  ARG A NH1 1 
ATOM   2153 N  NH2 . ARG A  1 266 ? -5.269  -13.418 -6.396  1.00 19.05 ? 266  ARG A NH2 1 
ATOM   2154 N  N   . LEU A  1 267 ? -12.728 -9.484  -1.906  1.00 11.41 ? 267  LEU A N   1 
ATOM   2155 C  CA  . LEU A  1 267 ? -14.081 -8.907  -1.736  1.00 11.19 ? 267  LEU A CA  1 
ATOM   2156 C  C   . LEU A  1 267 ? -15.147 -9.903  -2.216  1.00 11.21 ? 267  LEU A C   1 
ATOM   2157 O  O   . LEU A  1 267 ? -16.304 -9.473  -2.499  1.00 11.90 ? 267  LEU A O   1 
ATOM   2158 C  CB  . LEU A  1 267 ? -14.142 -7.564  -2.484  1.00 11.64 ? 267  LEU A CB  1 
ATOM   2159 C  CG  . LEU A  1 267 ? -13.310 -6.444  -1.848  1.00 12.95 ? 267  LEU A CG  1 
ATOM   2160 C  CD1 . LEU A  1 267 ? -13.177 -5.256  -2.795  1.00 14.31 ? 267  LEU A CD1 1 
ATOM   2161 C  CD2 . LEU A  1 267 ? -13.894 -6.011  -0.515  1.00 13.32 ? 267  LEU A CD2 1 
ATOM   2162 N  N   . GLY A  1 268 ? -14.851 -11.195 -2.174  1.00 11.17 ? 268  GLY A N   1 
ATOM   2163 C  CA  . GLY A  1 268 ? -15.785 -12.219 -2.670  1.00 11.25 ? 268  GLY A CA  1 
ATOM   2164 C  C   . GLY A  1 268 ? -15.623 -12.438 -4.165  1.00 10.93 ? 268  GLY A C   1 
ATOM   2165 O  O   . GLY A  1 268 ? -16.619 -12.573 -4.881  1.00 11.22 ? 268  GLY A O   1 
ATOM   2166 N  N   . SER A  1 269 ? -14.386 -12.546 -4.635  1.00 10.41 ? 269  SER A N   1 
ATOM   2167 C  CA  . SER A  1 269 ? -14.090 -12.708 -6.079  1.00 10.65 ? 269  SER A CA  1 
ATOM   2168 C  C   . SER A  1 269 ? -14.641 -11.523 -6.892  1.00 10.37 ? 269  SER A C   1 
ATOM   2169 O  O   . SER A  1 269 ? -14.820 -11.671 -8.115  1.00 10.81 ? 269  SER A O   1 
ATOM   2170 C  CB  . SER A  1 269 ? -14.569 -14.058 -6.617  1.00 11.78 ? 269  SER A CB  1 
ATOM   2171 O  OG  . SER A  1 269 ? -13.843 -15.113 -5.985  1.00 12.27 ? 269  SER A OG  1 
ATOM   2172 N  N   . LEU A  1 270 ? -14.838 -10.363 -6.272  1.00 9.98  ? 270  LEU A N   1 
ATOM   2173 C  CA  . LEU A  1 270 ? -15.136 -9.117  -7.019  1.00 11.13 ? 270  LEU A CA  1 
ATOM   2174 C  C   . LEU A  1 270 ? -13.866 -8.594  -7.681  1.00 11.63 ? 270  LEU A C   1 
ATOM   2175 O  O   . LEU A  1 270 ? -13.966 -7.998  -8.769  1.00 11.91 ? 270  LEU A O   1 
ATOM   2176 C  CB  . LEU A  1 270 ? -15.766 -8.088  -6.083  1.00 11.32 ? 270  LEU A CB  1 
ATOM   2177 C  CG  . LEU A  1 270 ? -17.069 -8.565  -5.415  1.00 12.56 ? 270  LEU A CG  1 
ATOM   2178 C  CD1 . LEU A  1 270 ? -17.718 -7.411  -4.708  1.00 12.25 ? 270  LEU A CD1 1 
ATOM   2179 C  CD2 . LEU A  1 270 ? -18.050 -9.255  -6.373  1.00 12.40 ? 270  LEU A CD2 1 
ATOM   2180 N  N   A MET A  1 271 ? -12.712 -8.813  -7.043  0.60 13.69 ? 271  MET A N   1 
ATOM   2181 N  N   B MET A  1 271 ? -12.699 -8.794  -7.063  0.40 10.50 ? 271  MET A N   1 
ATOM   2182 C  CA  A MET A  1 271 ? -11.375 -8.530  -7.612  0.60 14.46 ? 271  MET A CA  1 
ATOM   2183 C  CA  B MET A  1 271 ? -11.402 -8.461  -7.697  0.40 9.61  ? 271  MET A CA  1 
ATOM   2184 C  C   A MET A  1 271 ? -10.934 -9.762  -8.421  0.60 13.49 ? 271  MET A C   1 
ATOM   2185 C  C   B MET A  1 271 ? -10.858 -9.722  -8.380  0.40 10.56 ? 271  MET A C   1 
ATOM   2186 O  O   A MET A  1 271 ? -11.179 -10.884 -7.951  0.60 13.45 ? 271  MET A O   1 
ATOM   2187 O  O   B MET A  1 271 ? -10.935 -10.804 -7.774  0.40 10.57 ? 271  MET A O   1 
ATOM   2188 C  CB  A MET A  1 271 ? -10.349 -8.241  -6.510  0.60 16.68 ? 271  MET A CB  1 
ATOM   2189 C  CB  B MET A  1 271 ? -10.381 -7.931  -6.688  0.40 8.17  ? 271  MET A CB  1 
ATOM   2190 C  CG  A MET A  1 271 ? -10.727 -7.080  -5.585  0.60 19.33 ? 271  MET A CG  1 
ATOM   2191 C  CG  B MET A  1 271 ? -10.805 -6.618  -6.060  0.40 7.39  ? 271  MET A CG  1 
ATOM   2192 S  SD  A MET A  1 271 ? -10.438 -5.523  -6.386  0.60 26.58 ? 271  MET A SD  1 
ATOM   2193 S  SD  B MET A  1 271 ? -9.821  -6.210  -4.608  0.40 6.27  ? 271  MET A SD  1 
ATOM   2194 C  CE  A MET A  1 271 ? -8.644  -5.469  -6.278  0.60 24.33 ? 271  MET A CE  1 
ATOM   2195 C  CE  B MET A  1 271 ? -8.170  -6.030  -5.278  0.40 6.40  ? 271  MET A CE  1 
ATOM   2196 N  N   . ALA A  1 272 ? -10.338 -9.538  -9.592  1.00 11.70 ? 272  ALA A N   1 
ATOM   2197 C  CA  . ALA A  1 272 ? -9.755  -10.560 -10.478 1.00 12.46 ? 272  ALA A CA  1 
ATOM   2198 C  C   . ALA A  1 272 ? -8.384  -11.021 -9.970  1.00 12.95 ? 272  ALA A C   1 
ATOM   2199 O  O   . ALA A  1 272 ? -7.960  -12.136 -10.288 1.00 14.13 ? 272  ALA A O   1 
ATOM   2200 C  CB  . ALA A  1 272 ? -9.645  -9.960  -11.877 1.00 12.90 ? 272  ALA A CB  1 
ATOM   2201 N  N   . SER A  1 273 ? -7.698  -10.133 -9.252  1.00 13.19 ? 273  SER A N   1 
ATOM   2202 C  CA  . SER A  1 273 ? -6.336  -10.317 -8.702  1.00 13.01 ? 273  SER A CA  1 
ATOM   2203 C  C   . SER A  1 273 ? -6.215  -9.419  -7.478  1.00 14.22 ? 273  SER A C   1 
ATOM   2204 O  O   . SER A  1 273 ? -7.210  -8.779  -7.107  1.00 15.32 ? 273  SER A O   1 
ATOM   2205 C  CB  . SER A  1 273 ? -5.331  -9.949  -9.769  1.00 13.60 ? 273  SER A CB  1 
ATOM   2206 O  OG  . SER A  1 273 ? -5.254  -8.545  -9.916  1.00 12.23 ? 273  SER A OG  1 
ATOM   2207 N  N   . ASP A  1 274 ? -5.024  -9.298  -6.893  1.00 14.06 ? 274  ASP A N   1 
ATOM   2208 C  CA  . ASP A  1 274 ? -4.812  -8.346  -5.767  1.00 14.40 ? 274  ASP A CA  1 
ATOM   2209 C  C   . ASP A  1 274 ? -4.557  -6.929  -6.290  1.00 14.26 ? 274  ASP A C   1 
ATOM   2210 O  O   . ASP A  1 274 ? -4.483  -6.001  -5.454  1.00 14.20 ? 274  ASP A O   1 
ATOM   2211 C  CB  . ASP A  1 274 ? -3.661  -8.816  -4.886  1.00 14.83 ? 274  ASP A CB  1 
ATOM   2212 C  CG  . ASP A  1 274 ? -3.933  -10.138 -4.201  1.00 17.74 ? 274  ASP A CG  1 
ATOM   2213 O  OD1 . ASP A  1 274 ? -5.133  -10.424 -3.906  1.00 16.71 ? 274  ASP A OD1 1 
ATOM   2214 O  OD2 . ASP A  1 274 ? -2.953  -10.884 -3.958  1.00 18.92 ? 274  ASP A OD2 1 
ATOM   2215 N  N   . THR A  1 275 ? -4.518  -6.728  -7.615  1.00 13.59 ? 275  THR A N   1 
ATOM   2216 C  CA  . THR A  1 275 ? -4.261  -5.396  -8.200  1.00 14.61 ? 275  THR A CA  1 
ATOM   2217 C  C   . THR A  1 275 ? -5.383  -4.945  -9.132  1.00 13.83 ? 275  THR A C   1 
ATOM   2218 O  O   . THR A  1 275 ? -5.371  -3.777  -9.521  1.00 14.08 ? 275  THR A O   1 
ATOM   2219 C  CB  . THR A  1 275 ? -2.904  -5.366  -8.926  1.00 15.01 ? 275  THR A CB  1 
ATOM   2220 O  OG1 . THR A  1 275 ? -3.043  -6.148  -10.116 1.00 14.33 ? 275  THR A OG1 1 
ATOM   2221 C  CG2 . THR A  1 275 ? -1.766  -5.897  -8.071  1.00 15.73 ? 275  THR A CG2 1 
ATOM   2222 N  N   . GLN A  1 276 ? -6.353  -5.797  -9.459  1.00 14.63 ? 276  GLN A N   1 
ATOM   2223 C  CA  . GLN A  1 276 ? -7.308  -5.460  -10.530 1.00 14.25 ? 276  GLN A CA  1 
ATOM   2224 C  C   . GLN A  1 276 ? -8.727  -5.851  -10.154 1.00 13.81 ? 276  GLN A C   1 
ATOM   2225 O  O   . GLN A  1 276 ? -8.965  -6.969  -9.679  1.00 13.44 ? 276  GLN A O   1 
ATOM   2226 C  CB  . GLN A  1 276 ? -6.961  -6.190  -11.819 1.00 16.78 ? 276  GLN A CB  1 
ATOM   2227 C  CG  . GLN A  1 276 ? -5.570  -5.850  -12.348 1.00 18.78 ? 276  GLN A CG  1 
ATOM   2228 C  CD  . GLN A  1 276 ? -4.932  -7.022  -13.064 1.00 23.96 ? 276  GLN A CD  1 
ATOM   2229 O  OE1 . GLN A  1 276 ? -4.726  -8.122  -12.511 1.00 23.02 ? 276  GLN A OE1 1 
ATOM   2230 N  NE2 . GLN A  1 276 ? -4.630  -6.782  -14.335 1.00 21.20 ? 276  GLN A NE2 1 
ATOM   2231 N  N   . LYS A  1 277 ? -9.636  -4.992  -10.556 1.00 13.83 ? 277  LYS A N   1 
ATOM   2232 C  CA  . LYS A  1 277 ? -11.081 -5.290  -10.544 1.00 13.43 ? 277  LYS A CA  1 
ATOM   2233 C  C   . LYS A  1 277 ? -11.449 -6.426  -11.496 1.00 13.68 ? 277  LYS A C   1 
ATOM   2234 O  O   . LYS A  1 277 ? -10.921 -6.489  -12.617 1.00 13.62 ? 277  LYS A O   1 
ATOM   2235 C  CB  . LYS A  1 277 ? -11.848 -4.032  -10.938 1.00 14.14 ? 277  LYS A CB  1 
ATOM   2236 C  CG  . LYS A  1 277 ? -11.730 -2.880  -9.964  1.00 14.39 ? 277  LYS A CG  1 
ATOM   2237 C  CD  . LYS A  1 277 ? -12.174 -1.549  -10.527 1.00 15.17 ? 277  LYS A CD  1 
ATOM   2238 C  CE  . LYS A  1 277 ? -12.006 -0.428  -9.519  1.00 15.17 ? 277  LYS A CE  1 
ATOM   2239 N  NZ  . LYS A  1 277 ? -12.371 0.885   -10.101 1.00 15.21 ? 277  LYS A NZ  1 
ATOM   2240 N  N   . GLY A  1 278 ? -12.435 -7.239  -11.088 1.00 12.21 ? 278  GLY A N   1 
ATOM   2241 C  CA  . GLY A  1 278 ? -13.126 -8.187  -11.971 1.00 13.07 ? 278  GLY A CA  1 
ATOM   2242 C  C   . GLY A  1 278 ? -14.528 -7.685  -12.289 1.00 12.18 ? 278  GLY A C   1 
ATOM   2243 O  O   . GLY A  1 278 ? -14.903 -6.592  -11.816 1.00 11.31 ? 278  GLY A O   1 
ATOM   2244 N  N   . ALA A  1 279 ? -15.245 -8.404  -13.135 1.00 11.61 ? 279  ALA A N   1 
ATOM   2245 C  CA  . ALA A  1 279 ? -16.628 -8.038  -13.542 1.00 12.00 ? 279  ALA A CA  1 
ATOM   2246 C  C   . ALA A  1 279 ? -17.505 -7.734  -12.321 1.00 12.09 ? 279  ALA A C   1 
ATOM   2247 O  O   . ALA A  1 279 ? -18.250 -6.711  -12.325 1.00 11.70 ? 279  ALA A O   1 
ATOM   2248 C  CB  . ALA A  1 279 ? -17.209 -9.162  -14.348 1.00 11.50 ? 279  ALA A CB  1 
ATOM   2249 N  N   . GLY A  1 280 ? -17.514 -8.598  -11.315 1.00 11.86 ? 280  GLY A N   1 
ATOM   2250 C  CA  . GLY A  1 280 ? -18.395 -8.398  -10.145 1.00 12.20 ? 280  GLY A CA  1 
ATOM   2251 C  C   . GLY A  1 280 ? -18.152 -7.075  -9.441  1.00 10.55 ? 280  GLY A C   1 
ATOM   2252 O  O   . GLY A  1 280 ? -19.105 -6.501  -8.862  1.00 10.70 ? 280  GLY A O   1 
ATOM   2253 N  N   . TRP A  1 281 ? -16.919 -6.584  -9.408  1.00 9.94  ? 281  TRP A N   1 
ATOM   2254 C  CA  . TRP A  1 281 ? -16.651 -5.299  -8.712  1.00 10.69 ? 281  TRP A CA  1 
ATOM   2255 C  C   . TRP A  1 281 ? -17.576 -4.226  -9.310  1.00 10.60 ? 281  TRP A C   1 
ATOM   2256 O  O   . TRP A  1 281 ? -18.164 -3.446  -8.561  1.00 10.43 ? 281  TRP A O   1 
ATOM   2257 C  CB  . TRP A  1 281 ? -15.155 -4.893  -8.783  1.00 10.87 ? 281  TRP A CB  1 
ATOM   2258 C  CG  . TRP A  1 281 ? -14.810 -3.750  -7.886  1.00 10.98 ? 281  TRP A CG  1 
ATOM   2259 C  CD1 . TRP A  1 281 ? -14.323 -3.855  -6.618  1.00 11.42 ? 281  TRP A CD1 1 
ATOM   2260 C  CD2 . TRP A  1 281 ? -14.961 -2.340  -8.143  1.00 10.70 ? 281  TRP A CD2 1 
ATOM   2261 N  NE1 . TRP A  1 281 ? -14.171 -2.620  -6.062  1.00 12.28 ? 281  TRP A NE1 1 
ATOM   2262 C  CE2 . TRP A  1 281 ? -14.545 -1.668  -6.967  1.00 12.32 ? 281  TRP A CE2 1 
ATOM   2263 C  CE3 . TRP A  1 281 ? -15.445 -1.582  -9.214  1.00 11.38 ? 281  TRP A CE3 1 
ATOM   2264 C  CZ2 . TRP A  1 281 ? -14.596 -0.278  -6.839  1.00 12.28 ? 281  TRP A CZ2 1 
ATOM   2265 C  CZ3 . TRP A  1 281 ? -15.504 -0.209  -9.086  1.00 11.73 ? 281  TRP A CZ3 1 
ATOM   2266 C  CH2 . TRP A  1 281 ? -15.066 0.431   -7.927  1.00 12.37 ? 281  TRP A CH2 1 
ATOM   2267 N  N   . TRP A  1 282 ? -17.646 -4.164  -10.646 1.00 11.99 ? 282  TRP A N   1 
ATOM   2268 C  CA  . TRP A  1 282 ? -18.389 -3.090  -11.350 1.00 11.10 ? 282  TRP A CA  1 
ATOM   2269 C  C   . TRP A  1 282 ? -19.879 -3.252  -11.050 1.00 10.70 ? 282  TRP A C   1 
ATOM   2270 O  O   . TRP A  1 282 ? -20.583 -2.227  -10.869 1.00 11.31 ? 282  TRP A O   1 
ATOM   2271 C  CB  . TRP A  1 282 ? -18.107 -3.130  -12.851 1.00 11.75 ? 282  TRP A CB  1 
ATOM   2272 C  CG  . TRP A  1 282 ? -16.671 -2.817  -13.132 1.00 12.02 ? 282  TRP A CG  1 
ATOM   2273 C  CD1 . TRP A  1 282 ? -15.673 -3.718  -13.319 1.00 12.52 ? 282  TRP A CD1 1 
ATOM   2274 C  CD2 . TRP A  1 282 ? -16.059 -1.523  -13.136 1.00 12.92 ? 282  TRP A CD2 1 
ATOM   2275 N  NE1 . TRP A  1 282 ? -14.494 -3.063  -13.509 1.00 13.94 ? 282  TRP A NE1 1 
ATOM   2276 C  CE2 . TRP A  1 282 ? -14.690 -1.728  -13.376 1.00 13.23 ? 282  TRP A CE2 1 
ATOM   2277 C  CE3 . TRP A  1 282 ? -16.540 -0.214  -12.971 1.00 14.51 ? 282  TRP A CE3 1 
ATOM   2278 C  CZ2 . TRP A  1 282 ? -13.798 -0.658  -13.482 1.00 14.01 ? 282  TRP A CZ2 1 
ATOM   2279 C  CZ3 . TRP A  1 282 ? -15.657 0.839   -13.065 1.00 14.21 ? 282  TRP A CZ3 1 
ATOM   2280 C  CH2 . TRP A  1 282 ? -14.300 0.601   -13.297 1.00 14.11 ? 282  TRP A CH2 1 
ATOM   2281 N  N   . PHE A  1 283 ? -20.344 -4.483  -10.951 1.00 10.70 ? 283  PHE A N   1 
ATOM   2282 C  CA  . PHE A  1 283 ? -21.775 -4.723  -10.654 1.00 10.31 ? 283  PHE A CA  1 
ATOM   2283 C  C   . PHE A  1 283 ? -22.076 -4.283  -9.210  1.00 10.67 ? 283  PHE A C   1 
ATOM   2284 O  O   . PHE A  1 283 ? -23.058 -3.601  -8.954  1.00 11.08 ? 283  PHE A O   1 
ATOM   2285 C  CB  . PHE A  1 283 ? -22.113 -6.187  -10.822 1.00 9.97  ? 283  PHE A CB  1 
ATOM   2286 C  CG  . PHE A  1 283 ? -23.593 -6.466  -10.759 1.00 10.06 ? 283  PHE A CG  1 
ATOM   2287 C  CD1 . PHE A  1 283 ? -24.435 -6.043  -11.760 1.00 10.95 ? 283  PHE A CD1 1 
ATOM   2288 C  CD2 . PHE A  1 283 ? -24.132 -7.177  -9.708  1.00 10.71 ? 283  PHE A CD2 1 
ATOM   2289 C  CE1 . PHE A  1 283 ? -25.798 -6.290  -11.685 1.00 11.13 ? 283  PHE A CE1 1 
ATOM   2290 C  CE2 . PHE A  1 283 ? -25.492 -7.443  -9.645  1.00 11.35 ? 283  PHE A CE2 1 
ATOM   2291 C  CZ  . PHE A  1 283 ? -26.320 -6.993  -10.632 1.00 11.51 ? 283  PHE A CZ  1 
ATOM   2292 N  N   . TYR A  1 284 ? -21.230 -4.667  -8.263  1.00 11.40 ? 284  TYR A N   1 
ATOM   2293 C  CA  . TYR A  1 284 ? -21.377 -4.242  -6.850  1.00 10.73 ? 284  TYR A CA  1 
ATOM   2294 C  C   . TYR A  1 284 ? -21.108 -2.735  -6.699  1.00 11.02 ? 284  TYR A C   1 
ATOM   2295 O  O   . TYR A  1 284 ? -21.613 -2.174  -5.697  1.00 11.32 ? 284  TYR A O   1 
ATOM   2296 C  CB  . TYR A  1 284 ? -20.577 -5.123  -5.884  1.00 10.76 ? 284  TYR A CB  1 
ATOM   2297 C  CG  . TYR A  1 284 ? -21.211 -6.464  -5.561  1.00 10.02 ? 284  TYR A CG  1 
ATOM   2298 C  CD1 . TYR A  1 284 ? -21.240 -7.483  -6.492  1.00 10.45 ? 284  TYR A CD1 1 
ATOM   2299 C  CD2 . TYR A  1 284 ? -21.681 -6.754  -4.284  1.00 10.22 ? 284  TYR A CD2 1 
ATOM   2300 C  CE1 . TYR A  1 284 ? -21.784 -8.714  -6.179  1.00 9.99  ? 284  TYR A CE1 1 
ATOM   2301 C  CE2 . TYR A  1 284 ? -22.227 -7.985  -3.948  1.00 10.03 ? 284  TYR A CE2 1 
ATOM   2302 C  CZ  . TYR A  1 284 ? -22.239 -8.986  -4.897  1.00 10.11 ? 284  TYR A CZ  1 
ATOM   2303 O  OH  . TYR A  1 284 ? -22.747 -10.236 -4.652  1.00 10.51 ? 284  TYR A OH  1 
ATOM   2304 N  N   . LYS A  1 285 ? -20.318 -2.113  -7.570  1.00 11.36 ? 285  LYS A N   1 
ATOM   2305 C  CA  . LYS A  1 285 ? -20.157 -0.644  -7.519  1.00 10.74 ? 285  LYS A CA  1 
ATOM   2306 C  C   . LYS A  1 285 ? -21.512 0.005   -7.833  1.00 11.16 ? 285  LYS A C   1 
ATOM   2307 O  O   . LYS A  1 285 ? -21.899 0.942   -7.109  1.00 10.96 ? 285  LYS A O   1 
ATOM   2308 C  CB  . LYS A  1 285 ? -19.057 -0.142  -8.454  1.00 11.78 ? 285  LYS A CB  1 
ATOM   2309 C  CG  . LYS A  1 285 ? -18.961 1.377   -8.549  1.00 12.48 ? 285  LYS A CG  1 
ATOM   2310 C  CD  . LYS A  1 285 ? -18.599 2.016   -7.255  1.00 13.82 ? 285  LYS A CD  1 
ATOM   2311 C  CE  . LYS A  1 285 ? -18.148 3.461   -7.359  1.00 16.65 ? 285  LYS A CE  1 
ATOM   2312 N  NZ  . LYS A  1 285 ? -19.029 4.240   -8.255  1.00 17.15 ? 285  LYS A NZ  1 
ATOM   2313 N  N   . TRP A  1 286 ? -22.193 -0.440  -8.882  1.00 10.99 ? 286  TRP A N   1 
ATOM   2314 C  CA  . TRP A  1 286 ? -23.563 0.070   -9.174  1.00 11.04 ? 286  TRP A CA  1 
ATOM   2315 C  C   . TRP A  1 286 ? -24.471 -0.100  -7.965  1.00 11.64 ? 286  TRP A C   1 
ATOM   2316 O  O   . TRP A  1 286 ? -25.284 0.794   -7.687  1.00 12.01 ? 286  TRP A O   1 
ATOM   2317 C  CB  . TRP A  1 286 ? -24.144 -0.621  -10.392 1.00 11.37 ? 286  TRP A CB  1 
ATOM   2318 C  CG  . TRP A  1 286 ? -23.607 -0.127  -11.697 1.00 12.59 ? 286  TRP A CG  1 
ATOM   2319 C  CD1 . TRP A  1 286 ? -23.181 1.128   -12.029 1.00 13.26 ? 286  TRP A CD1 1 
ATOM   2320 C  CD2 . TRP A  1 286 ? -23.562 -0.896  -12.908 1.00 12.39 ? 286  TRP A CD2 1 
ATOM   2321 N  NE1 . TRP A  1 286 ? -22.839 1.177   -13.367 1.00 13.65 ? 286  TRP A NE1 1 
ATOM   2322 C  CE2 . TRP A  1 286 ? -23.066 -0.050  -13.927 1.00 12.71 ? 286  TRP A CE2 1 
ATOM   2323 C  CE3 . TRP A  1 286 ? -23.881 -2.228  -13.221 1.00 13.12 ? 286  TRP A CE3 1 
ATOM   2324 C  CZ2 . TRP A  1 286 ? -22.887 -0.504  -15.238 1.00 13.20 ? 286  TRP A CZ2 1 
ATOM   2325 C  CZ3 . TRP A  1 286 ? -23.723 -2.662  -14.526 1.00 13.82 ? 286  TRP A CZ3 1 
ATOM   2326 C  CH2 . TRP A  1 286 ? -23.237 -1.806  -15.516 1.00 13.59 ? 286  TRP A CH2 1 
ATOM   2327 N  N   . TYR A  1 287 ? -24.381 -1.255  -7.299  1.00 10.67 ? 287  TYR A N   1 
ATOM   2328 C  CA  . TYR A  1 287 ? -25.185 -1.518  -6.081  1.00 10.98 ? 287  TYR A CA  1 
ATOM   2329 C  C   . TYR A  1 287 ? -24.834 -0.484  -5.002  1.00 10.90 ? 287  TYR A C   1 
ATOM   2330 O  O   . TYR A  1 287 ? -25.728 0.114   -4.390  1.00 11.23 ? 287  TYR A O   1 
ATOM   2331 C  CB  . TYR A  1 287 ? -24.904 -2.959  -5.667  1.00 11.03 ? 287  TYR A CB  1 
ATOM   2332 C  CG  . TYR A  1 287 ? -25.630 -3.507  -4.467  1.00 10.98 ? 287  TYR A CG  1 
ATOM   2333 C  CD1 . TYR A  1 287 ? -26.868 -3.049  -4.060  1.00 10.99 ? 287  TYR A CD1 1 
ATOM   2334 C  CD2 . TYR A  1 287 ? -25.101 -4.606  -3.808  1.00 10.82 ? 287  TYR A CD2 1 
ATOM   2335 C  CE1 . TYR A  1 287 ? -27.549 -3.648  -2.997  1.00 10.65 ? 287  TYR A CE1 1 
ATOM   2336 C  CE2 . TYR A  1 287 ? -25.757 -5.196  -2.736  1.00 11.49 ? 287  TYR A CE2 1 
ATOM   2337 C  CZ  . TYR A  1 287 ? -27.006 -4.759  -2.359  1.00 11.08 ? 287  TYR A CZ  1 
ATOM   2338 O  OH  . TYR A  1 287 ? -27.647 -5.385  -1.324  1.00 11.88 ? 287  TYR A OH  1 
ATOM   2339 N  N   . GLY A  1 288 ? -23.530 -0.218  -4.796  1.00 9.97  ? 288  GLY A N   1 
ATOM   2340 C  CA  . GLY A  1 288 ? -23.099 0.760   -3.775  1.00 11.13 ? 288  GLY A CA  1 
ATOM   2341 C  C   . GLY A  1 288 ? -23.556 2.170   -4.121  1.00 10.87 ? 288  GLY A C   1 
ATOM   2342 O  O   . GLY A  1 288 ? -23.788 2.966   -3.220  1.00 13.85 ? 288  GLY A O   1 
ATOM   2343 N  N   . ASP A  1 289 ? -23.724 2.461   -5.403  1.00 10.96 ? 289  ASP A N   1 
ATOM   2344 C  CA  . ASP A  1 289 ? -24.172 3.790   -5.890  1.00 11.16 ? 289  ASP A CA  1 
ATOM   2345 C  C   . ASP A  1 289 ? -25.645 4.016   -5.535  1.00 12.33 ? 289  ASP A C   1 
ATOM   2346 O  O   . ASP A  1 289 ? -26.076 5.216   -5.537  1.00 11.58 ? 289  ASP A O   1 
ATOM   2347 C  CB  . ASP A  1 289 ? -23.997 3.920   -7.409  1.00 11.35 ? 289  ASP A CB  1 
ATOM   2348 C  CG  . ASP A  1 289 ? -22.566 4.055   -7.871  1.00 13.94 ? 289  ASP A CG  1 
ATOM   2349 O  OD1 . ASP A  1 289 ? -21.718 4.327   -7.020  1.00 13.21 ? 289  ASP A OD1 1 
ATOM   2350 O  OD2 . ASP A  1 289 ? -22.335 3.837   -9.087  1.00 16.39 ? 289  ASP A OD2 1 
ATOM   2351 N  N   . MET A  1 290 ? -26.415 2.946   -5.303  1.00 12.28 ? 290  MET A N   1 
ATOM   2352 C  CA  . MET A  1 290 ? -27.868 3.068   -5.031  1.00 12.49 ? 290  MET A CA  1 
ATOM   2353 C  C   . MET A  1 290 ? -28.076 3.935   -3.794  1.00 12.90 ? 290  MET A C   1 
ATOM   2354 O  O   . MET A  1 290 ? -27.290 3.824   -2.834  1.00 13.53 ? 290  MET A O   1 
ATOM   2355 C  CB  . MET A  1 290 ? -28.548 1.713   -4.848  1.00 11.72 ? 290  MET A CB  1 
ATOM   2356 C  CG  . MET A  1 290 ? -28.610 0.921   -6.142  1.00 12.09 ? 290  MET A CG  1 
ATOM   2357 S  SD  . MET A  1 290 ? -29.512 -0.602  -5.914  1.00 13.19 ? 290  MET A SD  1 
ATOM   2358 C  CE  . MET A  1 290 ? -30.360 -0.768  -7.485  1.00 12.75 ? 290  MET A CE  1 
ATOM   2359 N  N   . THR A  1 291 ? -29.083 4.811   -3.869  1.00 13.07 ? 291  THR A N   1 
ATOM   2360 C  CA  . THR A  1 291 ? -29.466 5.768   -2.804  1.00 13.16 ? 291  THR A CA  1 
ATOM   2361 C  C   . THR A  1 291 ? -30.980 5.835   -2.773  1.00 12.83 ? 291  THR A C   1 
ATOM   2362 O  O   . THR A  1 291 ? -31.573 5.498   -3.773  1.00 12.89 ? 291  THR A O   1 
ATOM   2363 C  CB  . THR A  1 291 ? -28.849 7.153   -3.044  1.00 13.38 ? 291  THR A CB  1 
ATOM   2364 O  OG1 . THR A  1 291 ? -29.189 7.587   -4.362  1.00 13.06 ? 291  THR A OG1 1 
ATOM   2365 C  CG2 . THR A  1 291 ? -27.347 7.135   -2.870  1.00 14.88 ? 291  THR A CG2 1 
ATOM   2366 N  N   . GLY A  1 292 ? -31.532 6.344   -1.688  1.00 13.06 ? 292  GLY A N   1 
ATOM   2367 C  CA  . GLY A  1 292 ? -32.983 6.516   -1.543  1.00 13.01 ? 292  GLY A CA  1 
ATOM   2368 C  C   . GLY A  1 292 ? -33.578 5.301   -0.877  1.00 13.58 ? 292  GLY A C   1 
ATOM   2369 O  O   . GLY A  1 292 ? -33.076 4.916   0.219   1.00 13.64 ? 292  GLY A O   1 
ATOM   2370 N  N   . ASN A  1 293 ? -34.658 4.762   -1.461  1.00 12.37 ? 293  ASN A N   1 
ATOM   2371 C  CA  . ASN A  1 293 ? -35.394 3.586   -0.943  1.00 12.65 ? 293  ASN A CA  1 
ATOM   2372 C  C   . ASN A  1 293 ? -35.269 2.431   -1.930  1.00 12.26 ? 293  ASN A C   1 
ATOM   2373 O  O   . ASN A  1 293 ? -35.470 2.646   -3.157  1.00 11.36 ? 293  ASN A O   1 
ATOM   2374 C  CB  . ASN A  1 293 ? -36.868 3.900   -0.754  1.00 12.89 ? 293  ASN A CB  1 
ATOM   2375 C  CG  . ASN A  1 293 ? -37.091 4.874   0.382   1.00 14.98 ? 293  ASN A CG  1 
ATOM   2376 O  OD1 . ASN A  1 293 ? -36.349 4.844   1.359   1.00 16.36 ? 293  ASN A OD1 1 
ATOM   2377 N  ND2 . ASN A  1 293 ? -38.111 5.712   0.242   1.00 17.13 ? 293  ASN A ND2 1 
ATOM   2378 N  N   . MET A  1 294 ? -35.142 1.214   -1.403  1.00 11.49 ? 294  MET A N   1 
ATOM   2379 C  CA  . MET A  1 294 ? -35.334 -0.012  -2.219  1.00 11.81 ? 294  MET A CA  1 
ATOM   2380 C  C   . MET A  1 294 ? -36.827 -0.181  -2.460  1.00 11.31 ? 294  MET A C   1 
ATOM   2381 O  O   . MET A  1 294 ? -37.623 0.152   -1.559  1.00 12.79 ? 294  MET A O   1 
ATOM   2382 C  CB  . MET A  1 294 ? -34.758 -1.222  -1.493  1.00 11.94 ? 294  MET A CB  1 
ATOM   2383 C  CG  . MET A  1 294 ? -33.243 -1.069  -1.210  1.00 12.88 ? 294  MET A CG  1 
ATOM   2384 S  SD  . MET A  1 294 ? -32.204 -0.750  -2.678  1.00 12.70 ? 294  MET A SD  1 
ATOM   2385 C  CE  . MET A  1 294 ? -32.337 -2.281  -3.598  1.00 11.14 ? 294  MET A CE  1 
ATOM   2386 N  N   . VAL A  1 295 ? -37.198 -0.662  -3.636  1.00 11.71 ? 295  VAL A N   1 
ATOM   2387 C  CA  . VAL A  1 295 ? -38.608 -0.947  -3.992  1.00 11.92 ? 295  VAL A CA  1 
ATOM   2388 C  C   . VAL A  1 295 ? -38.695 -2.381  -4.473  1.00 12.62 ? 295  VAL A C   1 
ATOM   2389 O  O   . VAL A  1 295 ? -37.702 -2.913  -4.938  1.00 13.32 ? 295  VAL A O   1 
ATOM   2390 C  CB  . VAL A  1 295 ? -39.145 0.069   -5.013  1.00 12.01 ? 295  VAL A CB  1 
ATOM   2391 C  CG1 . VAL A  1 295 ? -39.055 1.475   -4.460  1.00 13.06 ? 295  VAL A CG1 1 
ATOM   2392 C  CG2 . VAL A  1 295 ? -38.457 -0.024  -6.361  1.00 12.02 ? 295  VAL A CG2 1 
ATOM   2393 N  N   . ASN A  1 296 ? -39.889 -2.948  -4.354  1.00 13.18 ? 296  ASN A N   1 
ATOM   2394 C  CA  . ASN A  1 296 ? -40.125 -4.360  -4.685  1.00 14.74 ? 296  ASN A CA  1 
ATOM   2395 C  C   . ASN A  1 296 ? -39.901 -4.557  -6.174  1.00 13.83 ? 296  ASN A C   1 
ATOM   2396 O  O   . ASN A  1 296 ? -40.353 -3.742  -7.000  1.00 14.24 ? 296  ASN A O   1 
ATOM   2397 C  CB  . ASN A  1 296 ? -41.511 -4.866  -4.272  1.00 16.21 ? 296  ASN A CB  1 
ATOM   2398 C  CG  . ASN A  1 296 ? -41.563 -6.377  -4.335  1.00 18.50 ? 296  ASN A CG  1 
ATOM   2399 O  OD1 . ASN A  1 296 ? -40.628 -7.055  -3.890  1.00 20.75 ? 296  ASN A OD1 1 
ATOM   2400 N  ND2 . ASN A  1 296 ? -42.599 -6.906  -4.951  1.00 23.68 ? 296  ASN A ND2 1 
ATOM   2401 N  N   . VAL A  1 297 ? -39.263 -5.671  -6.483  1.00 13.95 ? 297  VAL A N   1 
ATOM   2402 C  CA  . VAL A  1 297 ? -39.148 -6.223  -7.861  1.00 14.13 ? 297  VAL A CA  1 
ATOM   2403 C  C   . VAL A  1 297 ? -39.840 -7.576  -7.876  1.00 13.81 ? 297  VAL A C   1 
ATOM   2404 O  O   . VAL A  1 297 ? -39.584 -8.422  -6.987  1.00 14.28 ? 297  VAL A O   1 
ATOM   2405 C  CB  . VAL A  1 297 ? -37.697 -6.338  -8.323  1.00 13.33 ? 297  VAL A CB  1 
ATOM   2406 C  CG1 . VAL A  1 297 ? -37.580 -7.006  -9.695  1.00 13.69 ? 297  VAL A CG1 1 
ATOM   2407 C  CG2 . VAL A  1 297 ? -37.005 -4.981  -8.291  1.00 12.52 ? 297  VAL A CG2 1 
ATOM   2408 N  N   . ILE A  1 298 ? -40.789 -7.731  -8.795  1.00 14.88 ? 298  ILE A N   1 
ATOM   2409 C  CA  . ILE A  1 298 ? -41.505 -9.012  -8.990  1.00 15.88 ? 298  ILE A CA  1 
ATOM   2410 C  C   . ILE A  1 298 ? -40.698 -9.823  -9.989  1.00 15.95 ? 298  ILE A C   1 
ATOM   2411 O  O   . ILE A  1 298 ? -40.648 -9.475  -11.168 1.00 15.27 ? 298  ILE A O   1 
ATOM   2412 C  CB  . ILE A  1 298 ? -42.966 -8.809  -9.446  1.00 17.63 ? 298  ILE A CB  1 
ATOM   2413 C  CG1 . ILE A  1 298 ? -43.760 -7.995  -8.419  1.00 20.82 ? 298  ILE A CG1 1 
ATOM   2414 C  CG2 . ILE A  1 298 ? -43.607 -10.187 -9.672  1.00 18.70 ? 298  ILE A CG2 1 
ATOM   2415 C  CD1 . ILE A  1 298 ? -43.631 -6.496  -8.528  1.00 25.15 ? 298  ILE A CD1 1 
ATOM   2416 N  N   . PRO A  1 299 ? -40.082 -10.937 -9.521  1.00 14.97 ? 299  PRO A N   1 
ATOM   2417 C  CA  . PRO A  1 299 ? -39.219 -11.759 -10.351 1.00 16.42 ? 299  PRO A CA  1 
ATOM   2418 C  C   . PRO A  1 299 ? -40.011 -12.609 -11.354 1.00 16.81 ? 299  PRO A C   1 
ATOM   2419 O  O   . PRO A  1 299 ? -41.168 -12.903 -11.117 1.00 16.58 ? 299  PRO A O   1 
ATOM   2420 C  CB  . PRO A  1 299 ? -38.527 -12.674 -9.318  1.00 15.67 ? 299  PRO A CB  1 
ATOM   2421 C  CG  . PRO A  1 299 ? -39.540 -12.836 -8.234  1.00 16.02 ? 299  PRO A CG  1 
ATOM   2422 C  CD  . PRO A  1 299 ? -40.236 -11.494 -8.153  1.00 15.31 ? 299  PRO A CD  1 
ATOM   2423 N  N   . GLN A  1 300 ? -39.331 -13.033 -12.417 1.00 17.48 ? 300  GLN A N   1 
ATOM   2424 C  CA  . GLN A  1 300 ? -39.830 -14.071 -13.351 1.00 19.65 ? 300  GLN A CA  1 
ATOM   2425 C  C   . GLN A  1 300 ? -40.346 -15.261 -12.531 1.00 18.10 ? 300  GLN A C   1 
ATOM   2426 O  O   . GLN A  1 300 ? -41.489 -15.705 -12.757 1.00 18.50 ? 300  GLN A O   1 
ATOM   2427 C  CB  . GLN A  1 300 ? -38.701 -14.420 -14.322 1.00 22.45 ? 300  GLN A CB  1 
ATOM   2428 C  CG  . GLN A  1 300 ? -39.021 -15.551 -15.286 1.00 26.20 ? 300  GLN A CG  1 
ATOM   2429 C  CD  . GLN A  1 300 ? -40.134 -15.253 -16.264 1.00 27.57 ? 300  GLN A CD  1 
ATOM   2430 O  OE1 . GLN A  1 300 ? -40.137 -14.253 -16.997 1.00 23.06 ? 300  GLN A OE1 1 
ATOM   2431 N  NE2 . GLN A  1 300 ? -41.088 -16.165 -16.303 1.00 28.46 ? 300  GLN A NE2 1 
ATOM   2432 N  N   A ASN A  1 301 ? -39.511 -15.749 -11.598 0.70 17.33 ? 301  ASN A N   1 
ATOM   2433 N  N   B ASN A  1 301 ? -39.539 -15.782 -11.594 0.30 16.90 ? 301  ASN A N   1 
ATOM   2434 C  CA  A ASN A  1 301 ? -39.868 -16.879 -10.710 0.70 16.14 ? 301  ASN A CA  1 
ATOM   2435 C  CA  B ASN A  1 301 ? -39.948 -16.895 -10.693 0.30 15.74 ? 301  ASN A CA  1 
ATOM   2436 C  C   A ASN A  1 301 ? -39.006 -16.854 -9.450  0.70 16.19 ? 301  ASN A C   1 
ATOM   2437 C  C   B ASN A  1 301 ? -39.042 -16.902 -9.459  0.30 15.82 ? 301  ASN A C   1 
ATOM   2438 O  O   A ASN A  1 301 ? -37.827 -17.142 -9.572  0.70 14.50 ? 301  ASN A O   1 
ATOM   2439 O  O   B ASN A  1 301 ? -37.876 -17.279 -9.612  0.30 14.98 ? 301  ASN A O   1 
ATOM   2440 C  CB  A ASN A  1 301 ? -39.692 -18.213 -11.440 0.70 17.18 ? 301  ASN A CB  1 
ATOM   2441 C  CB  B ASN A  1 301 ? -39.899 -18.248 -11.416 0.30 15.39 ? 301  ASN A CB  1 
ATOM   2442 C  CG  A ASN A  1 301 ? -40.309 -19.356 -10.678 0.70 18.07 ? 301  ASN A CG  1 
ATOM   2443 C  CG  B ASN A  1 301 ? -40.788 -19.308 -10.798 0.30 15.35 ? 301  ASN A CG  1 
ATOM   2444 O  OD1 A ASN A  1 301 ? -40.270 -19.369 -9.443  0.70 18.33 ? 301  ASN A OD1 1 
ATOM   2445 O  OD1 B ASN A  1 301 ? -41.857 -19.001 -10.253 0.30 14.03 ? 301  ASN A OD1 1 
ATOM   2446 N  ND2 A ASN A  1 301 ? -40.944 -20.269 -11.402 0.70 20.02 ? 301  ASN A ND2 1 
ATOM   2447 N  ND2 B ASN A  1 301 ? -40.350 -20.560 -10.891 0.30 14.29 ? 301  ASN A ND2 1 
ATOM   2448 N  N   . ASP A  1 302 ? -39.566 -16.510 -8.291  1.00 15.69 ? 302  ASP A N   1 
ATOM   2449 C  CA  . ASP A  1 302 ? -38.758 -16.288 -7.068  1.00 16.61 ? 302  ASP A CA  1 
ATOM   2450 C  C   . ASP A  1 302 ? -38.025 -17.576 -6.664  1.00 16.79 ? 302  ASP A C   1 
ATOM   2451 O  O   . ASP A  1 302 ? -36.903 -17.483 -6.144  1.00 16.68 ? 302  ASP A O   1 
ATOM   2452 C  CB  . ASP A  1 302 ? -39.639 -15.817 -5.923  1.00 16.53 ? 302  ASP A CB  1 
ATOM   2453 C  CG  . ASP A  1 302 ? -38.921 -15.036 -4.848  1.00 19.37 ? 302  ASP A CG  1 
ATOM   2454 O  OD1 . ASP A  1 302 ? -37.747 -14.716 -5.051  1.00 20.19 ? 302  ASP A OD1 1 
ATOM   2455 O  OD2 . ASP A  1 302 ? -39.544 -14.772 -3.823  1.00 22.34 ? 302  ASP A OD2 1 
ATOM   2456 N  N   . ASN A  1 303 ? -38.657 -18.725 -6.906  1.00 15.77 ? 303  ASN A N   1 
ATOM   2457 C  CA  . ASN A  1 303 ? -38.153 -20.067 -6.523  1.00 17.19 ? 303  ASN A CA  1 
ATOM   2458 C  C   . ASN A  1 303 ? -37.316 -20.639 -7.658  1.00 16.81 ? 303  ASN A C   1 
ATOM   2459 O  O   . ASN A  1 303 ? -37.574 -21.791 -8.071  1.00 19.34 ? 303  ASN A O   1 
ATOM   2460 C  CB  . ASN A  1 303 ? -39.312 -21.011 -6.203  1.00 19.11 ? 303  ASN A CB  1 
ATOM   2461 C  CG  . ASN A  1 303 ? -40.225 -20.478 -5.118  1.00 24.50 ? 303  ASN A CG  1 
ATOM   2462 O  OD1 . ASN A  1 303 ? -41.441 -20.677 -5.197  1.00 29.76 ? 303  ASN A OD1 1 
ATOM   2463 N  ND2 . ASN A  1 303 ? -39.688 -19.808 -4.110  1.00 21.57 ? 303  ASN A ND2 1 
ATOM   2464 N  N   . SER A  1 304 ? -36.342 -19.878 -8.151  1.00 13.74 ? 304  SER A N   1 
ATOM   2465 C  CA  . SER A  1 304 ? -35.496 -20.289 -9.285  1.00 12.57 ? 304  SER A CA  1 
ATOM   2466 C  C   . SER A  1 304 ? -34.195 -19.501 -9.243  1.00 12.71 ? 304  SER A C   1 
ATOM   2467 O  O   . SER A  1 304 ? -34.098 -18.529 -8.468  1.00 12.13 ? 304  SER A O   1 
ATOM   2468 C  CB  . SER A  1 304 ? -36.200 -20.067 -10.596 1.00 12.68 ? 304  SER A CB  1 
ATOM   2469 O  OG  . SER A  1 304 ? -36.161 -18.692 -10.976 1.00 12.46 ? 304  SER A OG  1 
ATOM   2470 N  N   . ASN A  1 305 ? -33.290 -19.841 -10.138 1.00 13.71 ? 305  ASN A N   1 
ATOM   2471 C  CA  . ASN A  1 305 ? -32.058 -19.047 -10.348 1.00 14.92 ? 305  ASN A CA  1 
ATOM   2472 C  C   . ASN A  1 305 ? -32.223 -18.204 -11.627 1.00 14.82 ? 305  ASN A C   1 
ATOM   2473 O  O   . ASN A  1 305 ? -31.213 -17.745 -12.177 1.00 14.55 ? 305  ASN A O   1 
ATOM   2474 C  CB  . ASN A  1 305 ? -30.846 -19.970 -10.436 1.00 17.07 ? 305  ASN A CB  1 
ATOM   2475 C  CG  . ASN A  1 305 ? -30.891 -20.859 -11.663 1.00 19.98 ? 305  ASN A CG  1 
ATOM   2476 O  OD1 . ASN A  1 305 ? -31.898 -20.916 -12.391 1.00 20.95 ? 305  ASN A OD1 1 
ATOM   2477 N  ND2 . ASN A  1 305 ? -29.795 -21.567 -11.915 1.00 23.05 ? 305  ASN A ND2 1 
ATOM   2478 N  N   . LEU A  1 306 ? -33.456 -17.996 -12.105 1.00 13.22 ? 306  LEU A N   1 
ATOM   2479 C  CA  . LEU A  1 306 ? -33.678 -17.167 -13.304 1.00 13.73 ? 306  LEU A CA  1 
ATOM   2480 C  C   . LEU A  1 306 ? -33.396 -15.715 -12.934 1.00 14.00 ? 306  LEU A C   1 
ATOM   2481 O  O   . LEU A  1 306 ? -33.335 -15.371 -11.727 1.00 13.50 ? 306  LEU A O   1 
ATOM   2482 C  CB  . LEU A  1 306 ? -35.112 -17.312 -13.808 1.00 14.81 ? 306  LEU A CB  1 
ATOM   2483 C  CG  . LEU A  1 306 ? -35.496 -18.703 -14.290 1.00 15.82 ? 306  LEU A CG  1 
ATOM   2484 C  CD1 . LEU A  1 306 ? -36.946 -18.697 -14.711 1.00 15.92 ? 306  LEU A CD1 1 
ATOM   2485 C  CD2 . LEU A  1 306 ? -34.586 -19.136 -15.427 1.00 17.54 ? 306  LEU A CD2 1 
ATOM   2486 N  N   . ALA A  1 307 ? -33.233 -14.905 -13.953 1.00 15.04 ? 307  ALA A N   1 
ATOM   2487 C  CA  . ALA A  1 307 ? -32.883 -13.482 -13.816 1.00 14.22 ? 307  ALA A CA  1 
ATOM   2488 C  C   . ALA A  1 307 ? -33.844 -12.843 -12.818 1.00 14.28 ? 307  ALA A C   1 
ATOM   2489 O  O   . ALA A  1 307 ? -35.063 -13.163 -12.774 1.00 13.78 ? 307  ALA A O   1 
ATOM   2490 C  CB  . ALA A  1 307 ? -32.932 -12.777 -15.141 1.00 14.67 ? 307  ALA A CB  1 
ATOM   2491 N  N   . ASP A  1 308 ? -33.276 -11.974 -11.992 1.00 13.79 ? 308  ASP A N   1 
ATOM   2492 C  CA  . ASP A  1 308 ? -33.998 -11.306 -10.896 1.00 13.46 ? 308  ASP A CA  1 
ATOM   2493 C  C   . ASP A  1 308 ? -33.303 -9.964  -10.714 1.00 12.05 ? 308  ASP A C   1 
ATOM   2494 O  O   . ASP A  1 308 ? -32.166 -9.795  -11.189 1.00 13.69 ? 308  ASP A O   1 
ATOM   2495 C  CB  . ASP A  1 308 ? -34.024 -12.170 -9.627  1.00 12.91 ? 308  ASP A CB  1 
ATOM   2496 C  CG  . ASP A  1 308 ? -35.042 -11.796 -8.550  1.00 13.71 ? 308  ASP A CG  1 
ATOM   2497 O  OD1 . ASP A  1 308 ? -35.729 -10.773 -8.705  1.00 11.82 ? 308  ASP A OD1 1 
ATOM   2498 O  OD2 . ASP A  1 308 ? -35.194 -12.595 -7.576  1.00 12.54 ? 308  ASP A OD2 1 
ATOM   2499 N  N   . GLY A  1 309 ? -33.953 -9.051  -10.027 1.00 11.13 ? 309  GLY A N   1 
ATOM   2500 C  CA  . GLY A  1 309 ? -33.358 -7.718  -9.870  1.00 11.04 ? 309  GLY A CA  1 
ATOM   2501 C  C   . GLY A  1 309 ? -33.751 -7.049  -8.583  1.00 10.58 ? 309  GLY A C   1 
ATOM   2502 O  O   . GLY A  1 309 ? -34.612 -7.566  -7.838  1.00 11.43 ? 309  GLY A O   1 
ATOM   2503 N  N   . PHE A  1 310 ? -33.053 -5.956  -8.322  1.00 10.12 ? 310  PHE A N   1 
ATOM   2504 C  CA  . PHE A  1 310 ? -33.252 -5.101  -7.143  1.00 10.32 ? 310  PHE A CA  1 
ATOM   2505 C  C   . PHE A  1 310 ? -33.192 -3.662  -7.638  1.00 11.04 ? 310  PHE A C   1 
ATOM   2506 O  O   . PHE A  1 310 ? -32.541 -3.372  -8.690  1.00 11.14 ? 310  PHE A O   1 
ATOM   2507 C  CB  . PHE A  1 310 ? -32.240 -5.440  -6.053  1.00 10.30 ? 310  PHE A CB  1 
ATOM   2508 C  CG  . PHE A  1 310 ? -30.798 -5.522  -6.487  1.00 10.13 ? 310  PHE A CG  1 
ATOM   2509 C  CD1 . PHE A  1 310 ? -30.317 -6.655  -7.136  1.00 11.15 ? 310  PHE A CD1 1 
ATOM   2510 C  CD2 . PHE A  1 310 ? -29.921 -4.487  -6.251  1.00 10.87 ? 310  PHE A CD2 1 
ATOM   2511 C  CE1 . PHE A  1 310 ? -28.990 -6.748  -7.532  1.00 11.70 ? 310  PHE A CE1 1 
ATOM   2512 C  CE2 . PHE A  1 310 ? -28.591 -4.593  -6.620  1.00 10.03 ? 310  PHE A CE2 1 
ATOM   2513 C  CZ  . PHE A  1 310 ? -28.130 -5.715  -7.279  1.00 10.92 ? 310  PHE A CZ  1 
ATOM   2514 N  N   . ALA A  1 311 ? -33.940 -2.787  -6.980  1.00 10.29 ? 311  ALA A N   1 
ATOM   2515 C  CA  . ALA A  1 311 ? -34.189 -1.443  -7.521  1.00 10.43 ? 311  ALA A CA  1 
ATOM   2516 C  C   . ALA A  1 311 ? -34.312 -0.438  -6.394  1.00 11.08 ? 311  ALA A C   1 
ATOM   2517 O  O   . ALA A  1 311 ? -34.827 -0.774  -5.292  1.00 11.72 ? 311  ALA A O   1 
ATOM   2518 C  CB  . ALA A  1 311 ? -35.437 -1.487  -8.370  1.00 11.00 ? 311  ALA A CB  1 
ATOM   2519 N  N   . CYS A  1 312 ? -33.822 0.757   -6.680  1.00 10.09 ? 312  CYS A N   1 
ATOM   2520 C  CA  . CYS A  1 312 ? -33.963 1.934   -5.798  1.00 11.47 ? 312  CYS A CA  1 
ATOM   2521 C  C   . CYS A  1 312 ? -34.630 3.068   -6.562  1.00 12.17 ? 312  CYS A C   1 
ATOM   2522 O  O   . CYS A  1 312 ? -34.558 3.142   -7.834  1.00 10.94 ? 312  CYS A O   1 
ATOM   2523 C  CB  . CYS A  1 312 ? -32.650 2.357   -5.179  1.00 12.13 ? 312  CYS A CB  1 
ATOM   2524 S  SG  . CYS A  1 312 ? -31.479 3.112   -6.336  1.00 12.56 ? 312  CYS A SG  1 
ATOM   2525 N  N   . VAL A  1 313 ? -35.319 3.881   -5.767  1.00 12.46 ? 313  VAL A N   1 
ATOM   2526 C  CA  . VAL A  1 313 ? -35.975 5.128   -6.211  1.00 13.00 ? 313  VAL A CA  1 
ATOM   2527 C  C   . VAL A  1 313 ? -35.456 6.206   -5.276  1.00 12.35 ? 313  VAL A C   1 
ATOM   2528 O  O   . VAL A  1 313 ? -35.603 6.073   -4.058  1.00 12.81 ? 313  VAL A O   1 
ATOM   2529 C  CB  . VAL A  1 313 ? -37.505 5.033   -6.211  1.00 12.91 ? 313  VAL A CB  1 
ATOM   2530 C  CG1 . VAL A  1 313 ? -38.099 6.390   -6.581  1.00 14.03 ? 313  VAL A CG1 1 
ATOM   2531 C  CG2 . VAL A  1 313 ? -37.990 3.935   -7.138  1.00 14.04 ? 313  VAL A CG2 1 
ATOM   2532 N  N   . ASP A  1 314 ? -34.828 7.222   -5.862  1.00 14.30 ? 314  ASP A N   1 
ATOM   2533 C  CA  . ASP A  1 314 ? -34.283 8.386   -5.125  1.00 15.53 ? 314  ASP A CA  1 
ATOM   2534 C  C   . ASP A  1 314 ? -35.042 9.638   -5.570  1.00 16.47 ? 314  ASP A C   1 
ATOM   2535 O  O   . ASP A  1 314 ? -34.829 10.092  -6.691  1.00 15.67 ? 314  ASP A O   1 
ATOM   2536 C  CB  . ASP A  1 314 ? -32.758 8.513   -5.295  1.00 16.16 ? 314  ASP A CB  1 
ATOM   2537 C  CG  . ASP A  1 314 ? -32.145 9.539   -4.346  1.00 17.38 ? 314  ASP A CG  1 
ATOM   2538 O  OD1 . ASP A  1 314 ? -32.863 10.535  -4.040  1.00 16.49 ? 314  ASP A OD1 1 
ATOM   2539 O  OD2 . ASP A  1 314 ? -30.945 9.387   -3.934  1.00 16.14 ? 314  ASP A OD2 1 
ATOM   2540 N  N   A SER A  1 315 ? -35.943 10.162  -4.740  0.70 18.57 ? 315  SER A N   1 
ATOM   2541 N  N   B SER A  1 315 ? -35.901 10.149  -4.680  0.30 17.26 ? 315  SER A N   1 
ATOM   2542 C  CA  A SER A  1 315 ? -36.749 11.368  -5.076  0.70 20.04 ? 315  SER A CA  1 
ATOM   2543 C  CA  B SER A  1 315 ? -36.801 11.316  -4.889  0.30 18.03 ? 315  SER A CA  1 
ATOM   2544 C  C   A SER A  1 315 ? -35.921 12.649  -4.916  0.70 21.36 ? 315  SER A C   1 
ATOM   2545 C  C   B SER A  1 315 ? -36.080 12.640  -4.585  0.30 19.18 ? 315  SER A C   1 
ATOM   2546 O  O   A SER A  1 315 ? -36.319 13.687  -5.469  0.70 21.12 ? 315  SER A O   1 
ATOM   2547 O  O   B SER A  1 315 ? -36.739 13.683  -4.649  0.30 18.32 ? 315  SER A O   1 
ATOM   2548 C  CB  A SER A  1 315 ? -37.983 11.445  -4.228  0.70 21.11 ? 315  SER A CB  1 
ATOM   2549 C  CB  B SER A  1 315 ? -38.041 11.186  -4.034  0.30 17.87 ? 315  SER A CB  1 
ATOM   2550 O  OG  A SER A  1 315 ? -37.620 11.518  -2.866  0.70 22.13 ? 315  SER A OG  1 
ATOM   2551 O  OG  B SER A  1 315 ? -38.857 10.099  -4.453  0.30 17.21 ? 315  SER A OG  1 
ATOM   2552 N  N   . ASN A  1 316 ? -34.804 12.584  -4.195  1.00 20.39 ? 316  ASN A N   1 
ATOM   2553 C  CA  . ASN A  1 316 ? -33.939 13.763  -3.976  1.00 22.02 ? 316  ASN A CA  1 
ATOM   2554 C  C   . ASN A  1 316 ? -33.083 13.900  -5.234  1.00 21.58 ? 316  ASN A C   1 
ATOM   2555 O  O   . ASN A  1 316 ? -33.178 14.925  -5.898  1.00 22.18 ? 316  ASN A O   1 
ATOM   2556 C  CB  . ASN A  1 316 ? -33.180 13.632  -2.665  1.00 24.38 ? 316  ASN A CB  1 
ATOM   2557 C  CG  . ASN A  1 316 ? -32.177 14.741  -2.448  1.00 29.76 ? 316  ASN A CG  1 
ATOM   2558 O  OD1 . ASN A  1 316 ? -30.995 14.478  -2.251  1.00 42.98 ? 316  ASN A OD1 1 
ATOM   2559 N  ND2 . ASN A  1 316 ? -32.625 15.974  -2.510  1.00 32.37 ? 316  ASN A ND2 1 
ATOM   2560 N  N   . ALA A  1 317 ? -32.324 12.864  -5.611  1.00 18.44 ? 317  ALA A N   1 
ATOM   2561 C  CA  . ALA A  1 317 ? -31.492 12.878  -6.831  1.00 19.10 ? 317  ALA A CA  1 
ATOM   2562 C  C   . ALA A  1 317 ? -32.359 12.669  -8.080  1.00 19.66 ? 317  ALA A C   1 
ATOM   2563 O  O   . ALA A  1 317 ? -31.825 12.836  -9.167  1.00 19.35 ? 317  ALA A O   1 
ATOM   2564 C  CB  . ALA A  1 317 ? -30.404 11.820  -6.738  1.00 19.22 ? 317  ALA A CB  1 
ATOM   2565 N  N   . LYS A  1 318 ? -33.614 12.226  -7.925  1.00 17.40 ? 318  LYS A N   1 
ATOM   2566 C  CA  . LYS A  1 318 ? -34.590 12.018  -9.016  1.00 18.71 ? 318  LYS A CA  1 
ATOM   2567 C  C   . LYS A  1 318 ? -34.093 10.984  -10.006 1.00 15.81 ? 318  LYS A C   1 
ATOM   2568 O  O   . LYS A  1 318 ? -33.989 11.268  -11.205 1.00 15.63 ? 318  LYS A O   1 
ATOM   2569 C  CB  . LYS A  1 318 ? -34.969 13.363  -9.635  1.00 21.90 ? 318  LYS A CB  1 
ATOM   2570 C  CG  . LYS A  1 318 ? -35.836 14.136  -8.646  1.00 26.55 ? 318  LYS A CG  1 
ATOM   2571 C  CD  . LYS A  1 318 ? -36.071 15.560  -8.941  1.00 30.11 ? 318  LYS A CD  1 
ATOM   2572 C  CE  . LYS A  1 318 ? -36.661 16.228  -7.715  1.00 32.46 ? 318  LYS A CE  1 
ATOM   2573 N  NZ  . LYS A  1 318 ? -37.248 17.541  -8.069  1.00 37.75 ? 318  LYS A NZ  1 
ATOM   2574 N  N   . TYR A  1 319 ? -33.934 9.747   -9.547  1.00 13.73 ? 319  TYR A N   1 
ATOM   2575 C  CA  . TYR A  1 319 ? -33.683 8.657   -10.498 1.00 13.36 ? 319  TYR A CA  1 
ATOM   2576 C  C   . TYR A  1 319 ? -34.262 7.351   -9.987  1.00 12.64 ? 319  TYR A C   1 
ATOM   2577 O  O   . TYR A  1 319 ? -34.634 7.224   -8.793  1.00 11.30 ? 319  TYR A O   1 
ATOM   2578 C  CB  . TYR A  1 319 ? -32.186 8.529   -10.802 1.00 13.28 ? 319  TYR A CB  1 
ATOM   2579 C  CG  . TYR A  1 319 ? -31.396 7.917   -9.684  1.00 12.83 ? 319  TYR A CG  1 
ATOM   2580 C  CD1 . TYR A  1 319 ? -30.835 8.700   -8.691  1.00 13.00 ? 319  TYR A CD1 1 
ATOM   2581 C  CD2 . TYR A  1 319 ? -31.204 6.537   -9.615  1.00 12.62 ? 319  TYR A CD2 1 
ATOM   2582 C  CE1 . TYR A  1 319 ? -30.107 8.147   -7.650  1.00 13.55 ? 319  TYR A CE1 1 
ATOM   2583 C  CE2 . TYR A  1 319 ? -30.517 5.969   -8.561  1.00 13.23 ? 319  TYR A CE2 1 
ATOM   2584 C  CZ  . TYR A  1 319 ? -29.952 6.766   -7.577  1.00 13.31 ? 319  TYR A CZ  1 
ATOM   2585 O  OH  . TYR A  1 319 ? -29.222 6.172   -6.579  1.00 12.89 ? 319  TYR A OH  1 
ATOM   2586 N  N   . ILE A  1 320 ? -34.323 6.411   -10.910 1.00 12.82 ? 320  ILE A N   1 
ATOM   2587 C  CA  . ILE A  1 320 ? -34.611 4.990   -10.599 1.00 11.66 ? 320  ILE A CA  1 
ATOM   2588 C  C   . ILE A  1 320 ? -33.425 4.171   -11.118 1.00 11.98 ? 320  ILE A C   1 
ATOM   2589 O  O   . ILE A  1 320 ? -33.070 4.296   -12.336 1.00 11.01 ? 320  ILE A O   1 
ATOM   2590 C  CB  . ILE A  1 320 ? -35.933 4.554   -11.251 1.00 13.18 ? 320  ILE A CB  1 
ATOM   2591 C  CG1 . ILE A  1 320 ? -37.077 5.482   -10.859 1.00 13.78 ? 320  ILE A CG1 1 
ATOM   2592 C  CG2 . ILE A  1 320 ? -36.238 3.089   -10.962 1.00 13.33 ? 320  ILE A CG2 1 
ATOM   2593 C  CD1 . ILE A  1 320 ? -38.321 5.292   -11.701 1.00 15.27 ? 320  ILE A CD1 1 
ATOM   2594 N  N   . SER A  1 321 ? -32.908 3.274   -10.298 1.00 11.73 ? 321  SER A N   1 
ATOM   2595 C  CA  . SER A  1 321 ? -31.875 2.329   -10.761 1.00 11.40 ? 321  SER A CA  1 
ATOM   2596 C  C   . SER A  1 321 ? -32.335 0.886   -10.522 1.00 12.16 ? 321  SER A C   1 
ATOM   2597 O  O   . SER A  1 321 ? -32.752 0.569   -9.372  1.00 11.24 ? 321  SER A O   1 
ATOM   2598 C  CB  . SER A  1 321 ? -30.588 2.597   -10.078 1.00 12.66 ? 321  SER A CB  1 
ATOM   2599 O  OG  . SER A  1 321 ? -29.631 1.645   -10.495 1.00 12.81 ? 321  SER A OG  1 
ATOM   2600 N  N   . VAL A  1 322 ? -32.217 0.058   -11.561 1.00 10.58 ? 322  VAL A N   1 
ATOM   2601 C  CA  . VAL A  1 322 ? -32.584 -1.376  -11.526 1.00 11.70 ? 322  VAL A CA  1 
ATOM   2602 C  C   . VAL A  1 322 ? -31.321 -2.150  -11.904 1.00 11.74 ? 322  VAL A C   1 
ATOM   2603 O  O   . VAL A  1 322 ? -30.771 -1.877  -12.970 1.00 12.42 ? 322  VAL A O   1 
ATOM   2604 C  CB  . VAL A  1 322 ? -33.739 -1.742  -12.475 1.00 11.71 ? 322  VAL A CB  1 
ATOM   2605 C  CG1 . VAL A  1 322 ? -34.232 -3.146  -12.165 1.00 12.14 ? 322  VAL A CG1 1 
ATOM   2606 C  CG2 . VAL A  1 322 ? -34.871 -0.736  -12.422 1.00 13.61 ? 322  VAL A CG2 1 
ATOM   2607 N  N   . LEU A  1 323 ? -30.909 -3.061  -11.036 1.00 10.55 ? 323  LEU A N   1 
ATOM   2608 C  CA  . LEU A  1 323 ? -29.767 -3.986  -11.243 1.00 11.28 ? 323  LEU A CA  1 
ATOM   2609 C  C   . LEU A  1 323 ? -30.291 -5.410  -11.342 1.00 11.82 ? 323  LEU A C   1 
ATOM   2610 O  O   . LEU A  1 323 ? -31.160 -5.821  -10.538 1.00 11.80 ? 323  LEU A O   1 
ATOM   2611 C  CB  . LEU A  1 323 ? -28.769 -3.821  -10.098 1.00 10.80 ? 323  LEU A CB  1 
ATOM   2612 C  CG  . LEU A  1 323 ? -27.934 -2.554  -10.199 1.00 10.95 ? 323  LEU A CG  1 
ATOM   2613 C  CD1 . LEU A  1 323 ? -27.166 -2.288  -8.912  1.00 11.06 ? 323  LEU A CD1 1 
ATOM   2614 C  CD2 . LEU A  1 323 ? -26.947 -2.654  -11.368 1.00 11.40 ? 323  LEU A CD2 1 
ATOM   2615 N  N   . LEU A  1 324 ? -29.768 -6.166  -12.294 1.00 12.04 ? 324  LEU A N   1 
ATOM   2616 C  CA  . LEU A  1 324 ? -30.343 -7.489  -12.578 1.00 11.41 ? 324  LEU A CA  1 
ATOM   2617 C  C   . LEU A  1 324 ? -29.349 -8.396  -13.289 1.00 12.15 ? 324  LEU A C   1 
ATOM   2618 O  O   . LEU A  1 324 ? -28.330 -7.940  -13.824 1.00 12.27 ? 324  LEU A O   1 
ATOM   2619 C  CB  . LEU A  1 324 ? -31.602 -7.266  -13.415 1.00 13.33 ? 324  LEU A CB  1 
ATOM   2620 C  CG  . LEU A  1 324 ? -31.317 -6.669  -14.786 1.00 15.04 ? 324  LEU A CG  1 
ATOM   2621 C  CD1 . LEU A  1 324 ? -31.807 -7.589  -15.877 1.00 19.45 ? 324  LEU A CD1 1 
ATOM   2622 C  CD2 . LEU A  1 324 ? -31.910 -5.274  -14.923 1.00 17.47 ? 324  LEU A CD2 1 
ATOM   2623 N  N   . GLY A  1 325 ? -29.686 -9.675  -13.272 1.00 10.73 ? 325  GLY A N   1 
ATOM   2624 C  CA  . GLY A  1 325 ? -28.859 -10.728 -13.879 1.00 12.41 ? 325  GLY A CA  1 
ATOM   2625 C  C   . GLY A  1 325 ? -29.413 -12.071 -13.533 1.00 12.77 ? 325  GLY A C   1 
ATOM   2626 O  O   . GLY A  1 325 ? -30.207 -12.158 -12.593 1.00 13.11 ? 325  GLY A O   1 
ATOM   2627 N  N   . GLY A  1 326 ? -28.955 -13.097 -14.236 1.00 13.47 ? 326  GLY A N   1 
ATOM   2628 C  CA  . GLY A  1 326 ? -29.276 -14.483 -13.877 1.00 13.55 ? 326  GLY A CA  1 
ATOM   2629 C  C   . GLY A  1 326 ? -29.782 -15.188 -15.110 1.00 13.58 ? 326  GLY A C   1 
ATOM   2630 O  O   . GLY A  1 326 ? -29.731 -14.584 -16.201 1.00 14.01 ? 326  GLY A O   1 
ATOM   2631 N  N   . VAL A  1 327 ? -30.270 -16.409 -14.949 1.00 13.48 ? 327  VAL A N   1 
ATOM   2632 C  CA  . VAL A  1 327 ? -30.524 -17.286 -16.126 1.00 14.60 ? 327  VAL A CA  1 
ATOM   2633 C  C   . VAL A  1 327 ? -31.701 -16.694 -16.900 1.00 14.61 ? 327  VAL A C   1 
ATOM   2634 O  O   . VAL A  1 327 ? -32.726 -16.317 -16.297 1.00 13.73 ? 327  VAL A O   1 
ATOM   2635 C  CB  . VAL A  1 327 ? -30.756 -18.737 -15.683 1.00 14.61 ? 327  VAL A CB  1 
ATOM   2636 C  CG1 . VAL A  1 327 ? -31.270 -19.595 -16.822 1.00 15.97 ? 327  VAL A CG1 1 
ATOM   2637 C  CG2 . VAL A  1 327 ? -29.474 -19.331 -15.093 1.00 15.98 ? 327  VAL A CG2 1 
ATOM   2638 N  N   . ASN A  1 328 ? -31.577 -16.607 -18.214 1.00 15.09 ? 328  ASN A N   1 
ATOM   2639 C  CA  . ASN A  1 328 ? -32.652 -16.024 -19.034 1.00 15.86 ? 328  ASN A CA  1 
ATOM   2640 C  C   . ASN A  1 328 ? -32.632 -16.638 -20.427 1.00 16.54 ? 328  ASN A C   1 
ATOM   2641 O  O   . ASN A  1 328 ? -31.684 -17.358 -20.759 1.00 18.67 ? 328  ASN A O   1 
ATOM   2642 C  CB  . ASN A  1 328 ? -32.538 -14.500 -19.092 1.00 14.62 ? 328  ASN A CB  1 
ATOM   2643 C  CG  . ASN A  1 328 ? -31.240 -14.032 -19.705 1.00 14.40 ? 328  ASN A CG  1 
ATOM   2644 O  OD1 . ASN A  1 328 ? -31.065 -14.051 -20.936 1.00 14.82 ? 328  ASN A OD1 1 
ATOM   2645 N  ND2 . ASN A  1 328 ? -30.285 -13.683 -18.863 1.00 14.34 ? 328  ASN A ND2 1 
ATOM   2646 N  N   . ASP A  1 329 ? -33.641 -16.313 -21.220 1.00 17.10 ? 329  ASP A N   1 
ATOM   2647 C  CA  . ASP A  1 329 ? -33.832 -16.943 -22.542 1.00 19.27 ? 329  ASP A CA  1 
ATOM   2648 C  C   . ASP A  1 329 ? -33.208 -16.107 -23.656 1.00 19.73 ? 329  ASP A C   1 
ATOM   2649 O  O   . ASP A  1 329 ? -33.516 -16.413 -24.799 1.00 21.97 ? 329  ASP A O   1 
ATOM   2650 C  CB  . ASP A  1 329 ? -35.309 -17.219 -22.784 1.00 19.43 ? 329  ASP A CB  1 
ATOM   2651 C  CG  . ASP A  1 329 ? -36.145 -15.992 -23.062 1.00 21.82 ? 329  ASP A CG  1 
ATOM   2652 O  OD1 . ASP A  1 329 ? -35.576 -14.878 -23.212 1.00 23.09 ? 329  ASP A OD1 1 
ATOM   2653 O  OD2 . ASP A  1 329 ? -37.382 -16.160 -23.111 1.00 24.16 ? 329  ASP A OD2 1 
ATOM   2654 N  N   . GLY A  1 330 ? -32.357 -15.120 -23.361 1.00 19.57 ? 330  GLY A N   1 
ATOM   2655 C  CA  . GLY A  1 330 ? -31.623 -14.344 -24.376 1.00 17.93 ? 330  GLY A CA  1 
ATOM   2656 C  C   . GLY A  1 330 ? -32.156 -12.941 -24.547 1.00 17.68 ? 330  GLY A C   1 
ATOM   2657 O  O   . GLY A  1 330 ? -31.490 -12.135 -25.233 1.00 18.04 ? 330  GLY A O   1 
ATOM   2658 N  N   . THR A  1 331 ? -33.304 -12.644 -23.938 1.00 17.44 ? 331  THR A N   1 
ATOM   2659 C  CA  . THR A  1 331 ? -33.860 -11.279 -23.835 1.00 17.26 ? 331  THR A CA  1 
ATOM   2660 C  C   . THR A  1 331 ? -34.286 -11.073 -22.391 1.00 17.75 ? 331  THR A C   1 
ATOM   2661 O  O   . THR A  1 331 ? -34.817 -12.044 -21.806 1.00 16.81 ? 331  THR A O   1 
ATOM   2662 C  CB  . THR A  1 331 ? -35.081 -11.067 -24.719 1.00 19.64 ? 331  THR A CB  1 
ATOM   2663 O  OG1 . THR A  1 331 ? -34.684 -11.436 -26.036 1.00 23.13 ? 331  THR A OG1 1 
ATOM   2664 C  CG2 . THR A  1 331 ? -35.597 -9.649  -24.684 1.00 22.23 ? 331  THR A CG2 1 
ATOM   2665 N  N   . VAL A  1 332 ? -34.072 -9.883  -21.842 1.00 16.27 ? 332  VAL A N   1 
ATOM   2666 C  CA  . VAL A  1 332 ? -34.647 -9.561  -20.503 1.00 16.48 ? 332  VAL A CA  1 
ATOM   2667 C  C   . VAL A  1 332 ? -35.495 -8.300  -20.630 1.00 15.74 ? 332  VAL A C   1 
ATOM   2668 O  O   . VAL A  1 332 ? -34.987 -7.265  -21.097 1.00 18.00 ? 332  VAL A O   1 
ATOM   2669 C  CB  . VAL A  1 332 ? -33.588 -9.442  -19.392 1.00 17.57 ? 332  VAL A CB  1 
ATOM   2670 C  CG1 . VAL A  1 332 ? -34.213 -9.031  -18.059 1.00 17.70 ? 332  VAL A CG1 1 
ATOM   2671 C  CG2 . VAL A  1 332 ? -32.798 -10.734 -19.246 1.00 16.25 ? 332  VAL A CG2 1 
ATOM   2672 N  N   . ASN A  1 333 ? -36.761 -8.408  -20.230 1.00 15.84 ? 333  ASN A N   1 
ATOM   2673 C  CA  . ASN A  1 333 ? -37.696 -7.255  -20.203 1.00 15.26 ? 333  ASN A CA  1 
ATOM   2674 C  C   . ASN A  1 333 ? -37.800 -6.727  -18.773 1.00 15.83 ? 333  ASN A C   1 
ATOM   2675 O  O   . ASN A  1 333 ? -38.025 -7.530  -17.837 1.00 16.08 ? 333  ASN A O   1 
ATOM   2676 C  CB  . ASN A  1 333 ? -39.063 -7.631  -20.745 1.00 16.95 ? 333  ASN A CB  1 
ATOM   2677 C  CG  . ASN A  1 333 ? -38.998 -7.873  -22.236 1.00 18.09 ? 333  ASN A CG  1 
ATOM   2678 O  OD1 . ASN A  1 333 ? -37.995 -7.577  -22.883 1.00 21.64 ? 333  ASN A OD1 1 
ATOM   2679 N  ND2 . ASN A  1 333 ? -40.012 -8.513  -22.764 1.00 18.50 ? 333  ASN A ND2 1 
ATOM   2680 N  N   . VAL A  1 334 ? -37.656 -5.425  -18.608 1.00 14.21 ? 334  VAL A N   1 
ATOM   2681 C  CA  . VAL A  1 334 ? -37.757 -4.772  -17.277 1.00 15.52 ? 334  VAL A CA  1 
ATOM   2682 C  C   . VAL A  1 334 ? -38.933 -3.801  -17.394 1.00 15.02 ? 334  VAL A C   1 
ATOM   2683 O  O   . VAL A  1 334 ? -38.839 -2.799  -18.124 1.00 16.43 ? 334  VAL A O   1 
ATOM   2684 C  CB  . VAL A  1 334 ? -36.452 -4.082  -16.841 1.00 15.75 ? 334  VAL A CB  1 
ATOM   2685 C  CG1 . VAL A  1 334 ? -36.616 -3.349  -15.527 1.00 16.85 ? 334  VAL A CG1 1 
ATOM   2686 C  CG2 . VAL A  1 334 ? -35.260 -5.040  -16.769 1.00 16.36 ? 334  VAL A CG2 1 
ATOM   2687 N  N   . ASN A  1 335 ? -40.043 -4.148  -16.770 1.00 15.31 ? 335  ASN A N   1 
ATOM   2688 C  CA  . ASN A  1 335 ? -41.245 -3.276  -16.755 1.00 15.63 ? 335  ASN A CA  1 
ATOM   2689 C  C   . ASN A  1 335 ? -41.223 -2.475  -15.474 1.00 16.14 ? 335  ASN A C   1 
ATOM   2690 O  O   . ASN A  1 335 ? -41.177 -3.089  -14.408 1.00 18.97 ? 335  ASN A O   1 
ATOM   2691 C  CB  . ASN A  1 335 ? -42.507 -4.097  -16.894 1.00 17.19 ? 335  ASN A CB  1 
ATOM   2692 C  CG  . ASN A  1 335 ? -42.522 -4.835  -18.214 1.00 18.74 ? 335  ASN A CG  1 
ATOM   2693 O  OD1 . ASN A  1 335 ? -41.996 -4.357  -19.223 1.00 22.06 ? 335  ASN A OD1 1 
ATOM   2694 N  ND2 . ASN A  1 335 ? -43.124 -6.002  -18.217 1.00 22.53 ? 335  ASN A ND2 1 
ATOM   2695 N  N   . ILE A  1 336 ? -41.191 -1.155  -15.593 1.00 13.30 ? 336  ILE A N   1 
ATOM   2696 C  CA  . ILE A  1 336 ? -41.158 -0.270  -14.408 1.00 13.65 ? 336  ILE A CA  1 
ATOM   2697 C  C   . ILE A  1 336 ? -42.535 0.364   -14.287 1.00 14.06 ? 336  ILE A C   1 
ATOM   2698 O  O   . ILE A  1 336 ? -42.951 1.001   -15.263 1.00 14.93 ? 336  ILE A O   1 
ATOM   2699 C  CB  . ILE A  1 336 ? -40.029 0.753   -14.523 1.00 14.35 ? 336  ILE A CB  1 
ATOM   2700 C  CG1 . ILE A  1 336 ? -38.719 0.007   -14.819 1.00 15.24 ? 336  ILE A CG1 1 
ATOM   2701 C  CG2 . ILE A  1 336 ? -39.999 1.573   -13.245 1.00 13.27 ? 336  ILE A CG2 1 
ATOM   2702 C  CD1 . ILE A  1 336 ? -37.553 0.925   -15.114 1.00 15.87 ? 336  ILE A CD1 1 
ATOM   2703 N  N   . LYS A  1 337 ? -43.214 0.138   -13.177 1.00 12.77 ? 337  LYS A N   1 
ATOM   2704 C  CA  . LYS A  1 337 ? -44.597 0.626   -12.995 1.00 13.48 ? 337  LYS A CA  1 
ATOM   2705 C  C   . LYS A  1 337 ? -44.726 1.551   -11.781 1.00 12.18 ? 337  LYS A C   1 
ATOM   2706 O  O   . LYS A  1 337 ? -43.853 1.629   -10.948 1.00 11.58 ? 337  LYS A O   1 
ATOM   2707 C  CB  . LYS A  1 337 ? -45.580 -0.550  -12.962 1.00 14.62 ? 337  LYS A CB  1 
ATOM   2708 C  CG  . LYS A  1 337 ? -45.514 -1.433  -11.743 1.00 16.84 ? 337  LYS A CG  1 
ATOM   2709 C  CD  . LYS A  1 337 ? -46.574 -2.515  -11.771 1.00 19.00 ? 337  LYS A CD  1 
ATOM   2710 C  CE  . LYS A  1 337 ? -46.734 -3.192  -10.422 1.00 22.61 ? 337  LYS A CE  1 
ATOM   2711 N  NZ  . LYS A  1 337 ? -47.879 -4.139  -10.401 1.00 25.41 ? 337  LYS A NZ  1 
ATOM   2712 N  N   . ASN A  1 338 ? -45.869 2.227   -11.684 1.00 13.20 ? 338  ASN A N   1 
ATOM   2713 C  CA  . ASN A  1 338 ? -46.171 3.177   -10.599 1.00 12.90 ? 338  ASN A CA  1 
ATOM   2714 C  C   . ASN A  1 338 ? -45.042 4.215   -10.546 1.00 12.99 ? 338  ASN A C   1 
ATOM   2715 O  O   . ASN A  1 338 ? -44.660 4.624   -9.455  1.00 12.31 ? 338  ASN A O   1 
ATOM   2716 C  CB  . ASN A  1 338 ? -46.438 2.398   -9.304  1.00 14.73 ? 338  ASN A CB  1 
ATOM   2717 C  CG  . ASN A  1 338 ? -47.744 1.628   -9.344  1.00 14.95 ? 338  ASN A CG  1 
ATOM   2718 O  OD1 . ASN A  1 338 ? -48.737 2.062   -9.958  1.00 15.34 ? 338  ASN A OD1 1 
ATOM   2719 N  ND2 . ASN A  1 338 ? -47.732 0.463   -8.714  1.00 14.14 ? 338  ASN A ND2 1 
ATOM   2720 N  N   . ILE A  1 339 ? -44.576 4.671   -11.698 1.00 12.77 ? 339  ILE A N   1 
ATOM   2721 C  CA  . ILE A  1 339 ? -43.440 5.624   -11.794 1.00 13.41 ? 339  ILE A CA  1 
ATOM   2722 C  C   . ILE A  1 339 ? -43.868 6.946   -11.167 1.00 14.22 ? 339  ILE A C   1 
ATOM   2723 O  O   . ILE A  1 339 ? -44.961 7.451   -11.422 1.00 13.90 ? 339  ILE A O   1 
ATOM   2724 C  CB  . ILE A  1 339 ? -43.010 5.772   -13.263 1.00 14.30 ? 339  ILE A CB  1 
ATOM   2725 C  CG1 . ILE A  1 339 ? -42.379 4.457   -13.722 1.00 15.47 ? 339  ILE A CG1 1 
ATOM   2726 C  CG2 . ILE A  1 339 ? -42.066 6.951   -13.472 1.00 14.75 ? 339  ILE A CG2 1 
ATOM   2727 C  CD1 . ILE A  1 339 ? -42.029 4.400   -15.187 1.00 15.60 ? 339  ILE A CD1 1 
ATOM   2728 N  N   . PRO A  1 340 ? -43.024 7.513   -10.290 1.00 13.56 ? 340  PRO A N   1 
ATOM   2729 C  CA  . PRO A  1 340 ? -43.276 8.810   -9.690  1.00 12.84 ? 340  PRO A CA  1 
ATOM   2730 C  C   . PRO A  1 340 ? -43.458 9.907   -10.747 1.00 13.86 ? 340  PRO A C   1 
ATOM   2731 O  O   . PRO A  1 340 ? -42.857 9.884   -11.814 1.00 12.67 ? 340  PRO A O   1 
ATOM   2732 C  CB  . PRO A  1 340 ? -42.033 9.123   -8.868  1.00 14.31 ? 340  PRO A CB  1 
ATOM   2733 C  CG  . PRO A  1 340 ? -41.390 7.787   -8.624  1.00 14.15 ? 340  PRO A CG  1 
ATOM   2734 C  CD  . PRO A  1 340 ? -41.750 6.938   -9.818  1.00 13.95 ? 340  PRO A CD  1 
ATOM   2735 N  N   . ALA A  1 341 ? -44.326 10.874  -10.427 1.00 12.66 ? 341  ALA A N   1 
ATOM   2736 C  CA  . ALA A  1 341 ? -44.581 12.031  -11.305 1.00 12.45 ? 341  ALA A CA  1 
ATOM   2737 C  C   . ALA A  1 341 ? -43.266 12.778  -11.597 1.00 12.69 ? 341  ALA A C   1 
ATOM   2738 O  O   . ALA A  1 341 ? -43.222 13.385  -12.656 1.00 13.52 ? 341  ALA A O   1 
ATOM   2739 C  CB  . ALA A  1 341 ? -45.605 12.937  -10.665 1.00 12.09 ? 341  ALA A CB  1 
ATOM   2740 N  N   . PHE A  1 342 ? -42.240 12.717  -10.740 1.00 13.87 ? 342  PHE A N   1 
ATOM   2741 C  CA  . PHE A  1 342 ? -40.973 13.478  -10.943 1.00 15.05 ? 342  PHE A CA  1 
ATOM   2742 C  C   . PHE A  1 342 ? -40.295 13.047  -12.246 1.00 15.39 ? 342  PHE A C   1 
ATOM   2743 O  O   . PHE A  1 342 ? -39.491 13.813  -12.825 1.00 16.77 ? 342  PHE A O   1 
ATOM   2744 C  CB  . PHE A  1 342 ? -40.061 13.494  -9.708  1.00 14.65 ? 342  PHE A CB  1 
ATOM   2745 C  CG  . PHE A  1 342 ? -39.290 12.249  -9.376  1.00 14.92 ? 342  PHE A CG  1 
ATOM   2746 C  CD1 . PHE A  1 342 ? -38.289 11.781  -10.216 1.00 14.27 ? 342  PHE A CD1 1 
ATOM   2747 C  CD2 . PHE A  1 342 ? -39.539 11.559  -8.193  1.00 14.65 ? 342  PHE A CD2 1 
ATOM   2748 C  CE1 . PHE A  1 342 ? -37.616 10.604  -9.916  1.00 14.95 ? 342  PHE A CE1 1 
ATOM   2749 C  CE2 . PHE A  1 342 ? -38.807 10.428  -7.860  1.00 15.34 ? 342  PHE A CE2 1 
ATOM   2750 C  CZ  . PHE A  1 342 ? -37.851 9.952   -8.721  1.00 15.03 ? 342  PHE A CZ  1 
ATOM   2751 N  N   . ILE A  1 343 ? -40.546 11.832  -12.715 1.00 15.64 ? 343  ILE A N   1 
ATOM   2752 C  CA  . ILE A  1 343 ? -39.976 11.366  -14.015 1.00 15.96 ? 343  ILE A CA  1 
ATOM   2753 C  C   . ILE A  1 343 ? -40.637 12.080  -15.191 1.00 17.99 ? 343  ILE A C   1 
ATOM   2754 O  O   . ILE A  1 343 ? -40.010 12.159  -16.274 1.00 19.63 ? 343  ILE A O   1 
ATOM   2755 C  CB  . ILE A  1 343 ? -40.084 9.833   -14.088 1.00 16.13 ? 343  ILE A CB  1 
ATOM   2756 C  CG1 . ILE A  1 343 ? -39.167 9.205   -13.030 1.00 17.23 ? 343  ILE A CG1 1 
ATOM   2757 C  CG2 . ILE A  1 343 ? -39.828 9.303   -15.488 1.00 16.68 ? 343  ILE A CG2 1 
ATOM   2758 C  CD1 . ILE A  1 343 ? -37.666 9.349   -13.311 1.00 16.88 ? 343  ILE A CD1 1 
ATOM   2759 N  N   . GLY A  1 344 ? -41.895 12.512  -15.049 1.00 17.07 ? 344  GLY A N   1 
ATOM   2760 C  CA  . GLY A  1 344 ? -42.599 13.158  -16.158 1.00 17.16 ? 344  GLY A CA  1 
ATOM   2761 C  C   . GLY A  1 344 ? -43.167 12.184  -17.166 1.00 18.08 ? 344  GLY A C   1 
ATOM   2762 O  O   . GLY A  1 344 ? -43.499 11.046  -16.787 1.00 18.78 ? 344  GLY A O   1 
ATOM   2763 N  N   . SER A  1 345 ? -43.420 12.635  -18.401 1.00 17.83 ? 345  SER A N   1 
ATOM   2764 C  CA  . SER A  1 345 ? -44.069 11.779  -19.427 1.00 21.30 ? 345  SER A CA  1 
ATOM   2765 C  C   . SER A  1 345 ? -43.019 11.168  -20.354 1.00 21.78 ? 345  SER A C   1 
ATOM   2766 O  O   . SER A  1 345 ? -43.388 10.315  -21.159 1.00 21.97 ? 345  SER A O   1 
ATOM   2767 C  CB  . SER A  1 345 ? -45.102 12.534  -20.213 1.00 25.12 ? 345  SER A CB  1 
ATOM   2768 O  OG  . SER A  1 345 ? -44.498 13.660  -20.759 1.00 25.45 ? 345  SER A OG  1 
ATOM   2769 N  N   . SER A  1 346 ? -41.776 11.587  -20.194 1.00 22.28 ? 346  SER A N   1 
ATOM   2770 C  CA  . SER A  1 346 ? -40.635 11.169  -21.047 1.00 25.05 ? 346  SER A CA  1 
ATOM   2771 C  C   . SER A  1 346 ? -39.433 10.936  -20.153 1.00 21.55 ? 346  SER A C   1 
ATOM   2772 O  O   . SER A  1 346 ? -39.205 11.750  -19.271 1.00 23.77 ? 346  SER A O   1 
ATOM   2773 C  CB  . SER A  1 346 ? -40.336 12.188  -22.085 1.00 25.05 ? 346  SER A CB  1 
ATOM   2774 O  OG  . SER A  1 346 ? -40.843 11.741  -23.308 1.00 35.27 ? 346  SER A OG  1 
ATOM   2775 N  N   . ALA A  1 347 ? -38.701 9.851   -20.373 1.00 21.04 ? 347  ALA A N   1 
ATOM   2776 C  CA  . ALA A  1 347 ? -37.550 9.546   -19.506 1.00 19.97 ? 347  ALA A CA  1 
ATOM   2777 C  C   . ALA A  1 347 ? -36.336 9.248   -20.372 1.00 17.94 ? 347  ALA A C   1 
ATOM   2778 O  O   . ALA A  1 347 ? -36.509 8.651   -21.402 1.00 16.91 ? 347  ALA A O   1 
ATOM   2779 C  CB  . ALA A  1 347 ? -37.881 8.375   -18.614 1.00 20.10 ? 347  ALA A CB  1 
ATOM   2780 N  N   . THR A  1 348 ? -35.157 9.559   -19.872 1.00 18.30 ? 348  THR A N   1 
ATOM   2781 C  CA  . THR A  1 348 ? -33.902 8.988   -20.408 1.00 18.65 ? 348  THR A CA  1 
ATOM   2782 C  C   . THR A  1 348 ? -33.678 7.643   -19.727 1.00 16.07 ? 348  THR A C   1 
ATOM   2783 O  O   . THR A  1 348 ? -33.651 7.624   -18.501 1.00 14.53 ? 348  THR A O   1 
ATOM   2784 C  CB  . THR A  1 348 ? -32.748 9.961   -20.239 1.00 20.88 ? 348  THR A CB  1 
ATOM   2785 O  OG1 . THR A  1 348 ? -33.128 11.090  -21.026 1.00 21.87 ? 348  THR A OG1 1 
ATOM   2786 C  CG2 . THR A  1 348 ? -31.433 9.379   -20.711 1.00 21.10 ? 348  THR A CG2 1 
ATOM   2787 N  N   . VAL A  1 349 ? -33.552 6.582   -20.509 1.00 16.14 ? 349  VAL A N   1 
ATOM   2788 C  CA  . VAL A  1 349 ? -33.285 5.212   -19.980 1.00 15.76 ? 349  VAL A CA  1 
ATOM   2789 C  C   . VAL A  1 349 ? -31.888 4.844   -20.472 1.00 15.29 ? 349  VAL A C   1 
ATOM   2790 O  O   . VAL A  1 349 ? -31.684 4.789   -21.723 1.00 14.97 ? 349  VAL A O   1 
ATOM   2791 C  CB  . VAL A  1 349 ? -34.366 4.224   -20.440 1.00 16.16 ? 349  VAL A CB  1 
ATOM   2792 C  CG1 . VAL A  1 349 ? -34.045 2.786   -20.048 1.00 17.13 ? 349  VAL A CG1 1 
ATOM   2793 C  CG2 . VAL A  1 349 ? -35.742 4.653   -19.925 1.00 18.45 ? 349  VAL A CG2 1 
ATOM   2794 N  N   A LYS A  1 350 ? -30.954 4.670   -19.535 0.50 14.82 ? 350  LYS A N   1 
ATOM   2795 N  N   B LYS A  1 350 ? -30.966 4.576   -19.541 0.50 14.49 ? 350  LYS A N   1 
ATOM   2796 C  CA  A LYS A  1 350 ? -29.597 4.188   -19.871 0.50 14.62 ? 350  LYS A CA  1 
ATOM   2797 C  CA  B LYS A  1 350 ? -29.551 4.238   -19.843 0.50 14.19 ? 350  LYS A CA  1 
ATOM   2798 C  C   A LYS A  1 350 ? -29.487 2.740   -19.405 0.50 13.75 ? 350  LYS A C   1 
ATOM   2799 C  C   B LYS A  1 350 ? -29.323 2.793   -19.393 0.50 13.69 ? 350  LYS A C   1 
ATOM   2800 O  O   A LYS A  1 350 ? -29.719 2.448   -18.227 0.50 12.50 ? 350  LYS A O   1 
ATOM   2801 O  O   B LYS A  1 350 ? -29.300 2.574   -18.173 0.50 13.18 ? 350  LYS A O   1 
ATOM   2802 C  CB  A LYS A  1 350 ? -28.516 5.091   -19.286 0.50 14.97 ? 350  LYS A CB  1 
ATOM   2803 C  CB  B LYS A  1 350 ? -28.655 5.270   -19.152 0.50 14.06 ? 350  LYS A CB  1 
ATOM   2804 C  CG  A LYS A  1 350 ? -27.113 4.689   -19.721 0.50 16.79 ? 350  LYS A CG  1 
ATOM   2805 C  CG  B LYS A  1 350 ? -27.156 5.021   -19.233 0.50 15.33 ? 350  LYS A CG  1 
ATOM   2806 C  CD  A LYS A  1 350 ? -26.099 5.778   -19.529 0.50 17.68 ? 350  LYS A CD  1 
ATOM   2807 C  CD  B LYS A  1 350 ? -26.359 6.030   -18.446 0.50 15.65 ? 350  LYS A CD  1 
ATOM   2808 C  CE  A LYS A  1 350 ? -24.813 5.503   -20.274 0.50 19.54 ? 350  LYS A CE  1 
ATOM   2809 C  CE  B LYS A  1 350 ? -26.616 5.986   -16.954 0.50 16.44 ? 350  LYS A CE  1 
ATOM   2810 N  NZ  A LYS A  1 350 ? -23.978 6.718   -20.327 0.50 20.70 ? 350  LYS A NZ  1 
ATOM   2811 N  NZ  B LYS A  1 350 ? -25.703 6.911   -16.251 0.50 18.79 ? 350  LYS A NZ  1 
ATOM   2812 N  N   . VAL A  1 351 ? -29.197 1.854   -20.333 1.00 12.72 ? 351  VAL A N   1 
ATOM   2813 C  CA  . VAL A  1 351 ? -28.953 0.430   -20.006 1.00 14.11 ? 351  VAL A CA  1 
ATOM   2814 C  C   . VAL A  1 351 ? -27.469 0.158   -20.219 1.00 15.22 ? 351  VAL A C   1 
ATOM   2815 O  O   . VAL A  1 351 ? -26.969 0.453   -21.308 1.00 14.99 ? 351  VAL A O   1 
ATOM   2816 C  CB  . VAL A  1 351 ? -29.828 -0.514  -20.828 1.00 15.27 ? 351  VAL A CB  1 
ATOM   2817 C  CG1 . VAL A  1 351 ? -29.535 -1.985  -20.553 1.00 15.81 ? 351  VAL A CG1 1 
ATOM   2818 C  CG2 . VAL A  1 351 ? -31.288 -0.170  -20.597 1.00 15.21 ? 351  VAL A CG2 1 
ATOM   2819 N  N   . GLU A  1 352 ? -26.841 -0.368  -19.186 1.00 14.37 ? 352  GLU A N   1 
ATOM   2820 C  CA  . GLU A  1 352 ? -25.388 -0.656  -19.178 1.00 14.94 ? 352  GLU A CA  1 
ATOM   2821 C  C   . GLU A  1 352 ? -25.204 -2.100  -18.752 1.00 14.98 ? 352  GLU A C   1 
ATOM   2822 O  O   . GLU A  1 352 ? -26.151 -2.715  -18.196 1.00 14.50 ? 352  GLU A O   1 
ATOM   2823 C  CB  . GLU A  1 352 ? -24.642 0.283   -18.247 1.00 14.99 ? 352  GLU A CB  1 
ATOM   2824 C  CG  . GLU A  1 352 ? -24.643 1.711   -18.730 1.00 15.82 ? 352  GLU A CG  1 
ATOM   2825 C  CD  . GLU A  1 352 ? -24.170 2.684   -17.672 1.00 17.09 ? 352  GLU A CD  1 
ATOM   2826 O  OE1 . GLU A  1 352 ? -24.997 3.241   -16.926 1.00 18.01 ? 352  GLU A OE1 1 
ATOM   2827 O  OE2 . GLU A  1 352 ? -22.968 2.884   -17.605 1.00 19.00 ? 352  GLU A OE2 1 
ATOM   2828 N  N   . LYS A  1 353 ? -24.057 -2.670  -19.106 1.00 14.65 ? 353  LYS A N   1 
ATOM   2829 C  CA  . LYS A  1 353 ? -23.772 -4.056  -18.710 1.00 14.77 ? 353  LYS A CA  1 
ATOM   2830 C  C   . LYS A  1 353 ? -22.325 -4.186  -18.278 1.00 14.62 ? 353  LYS A C   1 
ATOM   2831 O  O   . LYS A  1 353 ? -21.504 -3.301  -18.569 1.00 14.19 ? 353  LYS A O   1 
ATOM   2832 C  CB  . LYS A  1 353 ? -24.039 -5.008  -19.872 1.00 15.94 ? 353  LYS A CB  1 
ATOM   2833 C  CG  . LYS A  1 353 ? -23.114 -4.762  -21.046 1.00 16.42 ? 353  LYS A CG  1 
ATOM   2834 C  CD  . LYS A  1 353 ? -23.330 -5.712  -22.176 1.00 19.60 ? 353  LYS A CD  1 
ATOM   2835 C  CE  . LYS A  1 353 ? -22.273 -5.509  -23.237 1.00 23.28 ? 353  LYS A CE  1 
ATOM   2836 N  NZ  . LYS A  1 353 ? -22.649 -6.242  -24.454 1.00 27.58 ? 353  LYS A NZ  1 
ATOM   2837 N  N   . VAL A  1 354 ? -22.059 -5.271  -17.562 1.00 13.14 ? 354  VAL A N   1 
ATOM   2838 C  CA  . VAL A  1 354 ? -20.673 -5.683  -17.289 1.00 13.49 ? 354  VAL A CA  1 
ATOM   2839 C  C   . VAL A  1 354 ? -20.607 -7.144  -17.702 1.00 14.36 ? 354  VAL A C   1 
ATOM   2840 O  O   . VAL A  1 354 ? -21.473 -7.920  -17.268 1.00 14.06 ? 354  VAL A O   1 
ATOM   2841 C  CB  . VAL A  1 354 ? -20.219 -5.368  -15.846 1.00 13.37 ? 354  VAL A CB  1 
ATOM   2842 C  CG1 . VAL A  1 354 ? -21.053 -6.020  -14.770 1.00 14.24 ? 354  VAL A CG1 1 
ATOM   2843 C  CG2 . VAL A  1 354 ? -18.740 -5.682  -15.654 1.00 13.16 ? 354  VAL A CG2 1 
ATOM   2844 N  N   . ASP A  1 355 ? -19.684 -7.477  -18.604 1.00 15.23 ? 355  ASP A N   1 
ATOM   2845 C  CA  . ASP A  1 355 ? -19.516 -8.868  -19.090 1.00 15.48 ? 355  ASP A CA  1 
ATOM   2846 C  C   . ASP A  1 355 ? -18.496 -9.586  -18.217 1.00 15.04 ? 355  ASP A C   1 
ATOM   2847 O  O   . ASP A  1 355 ? -17.555 -8.946  -17.707 1.00 16.10 ? 355  ASP A O   1 
ATOM   2848 C  CB  . ASP A  1 355 ? -19.091 -8.888  -20.555 1.00 18.18 ? 355  ASP A CB  1 
ATOM   2849 C  CG  . ASP A  1 355 ? -20.187 -8.381  -21.480 1.00 20.33 ? 355  ASP A CG  1 
ATOM   2850 O  OD1 . ASP A  1 355 ? -21.415 -8.562  -21.150 1.00 19.50 ? 355  ASP A OD1 1 
ATOM   2851 O  OD2 . ASP A  1 355 ? -19.809 -7.774  -22.514 1.00 21.92 ? 355  ASP A OD2 1 
ATOM   2852 N  N   . TRP A  1 356 ? -18.672 -10.886 -18.098 1.00 15.08 ? 356  TRP A N   1 
ATOM   2853 C  CA  . TRP A  1 356 ? -17.814 -11.779 -17.293 1.00 16.29 ? 356  TRP A CA  1 
ATOM   2854 C  C   . TRP A  1 356 ? -17.236 -12.863 -18.196 1.00 17.81 ? 356  TRP A C   1 
ATOM   2855 O  O   . TRP A  1 356 ? -17.976 -13.464 -18.972 1.00 17.11 ? 356  TRP A O   1 
ATOM   2856 C  CB  . TRP A  1 356 ? -18.661 -12.352 -16.163 1.00 15.81 ? 356  TRP A CB  1 
ATOM   2857 C  CG  . TRP A  1 356 ? -18.016 -13.361 -15.270 1.00 14.37 ? 356  TRP A CG  1 
ATOM   2858 C  CD1 . TRP A  1 356 ? -17.415 -13.155 -14.067 1.00 13.52 ? 356  TRP A CD1 1 
ATOM   2859 C  CD2 . TRP A  1 356 ? -17.975 -14.778 -15.505 1.00 15.00 ? 356  TRP A CD2 1 
ATOM   2860 N  NE1 . TRP A  1 356 ? -17.017 -14.346 -13.526 1.00 15.00 ? 356  TRP A NE1 1 
ATOM   2861 C  CE2 . TRP A  1 356 ? -17.377 -15.361 -14.371 1.00 13.87 ? 356  TRP A CE2 1 
ATOM   2862 C  CE3 . TRP A  1 356 ? -18.453 -15.597 -16.532 1.00 15.11 ? 356  TRP A CE3 1 
ATOM   2863 C  CZ2 . TRP A  1 356 ? -17.178 -16.736 -14.262 1.00 14.90 ? 356  TRP A CZ2 1 
ATOM   2864 C  CZ3 . TRP A  1 356 ? -18.248 -16.957 -16.435 1.00 15.27 ? 356  TRP A CZ3 1 
ATOM   2865 C  CH2 . TRP A  1 356 ? -17.617 -17.509 -15.312 1.00 15.36 ? 356  TRP A CH2 1 
ATOM   2866 N  N   A ASN A  1 357 ? -15.929 -13.117 -18.079 0.50 21.00 ? 357  ASN A N   1 
ATOM   2867 N  N   B ASN A  1 357 ? -15.935 -13.085 -18.037 0.50 19.44 ? 357  ASN A N   1 
ATOM   2868 C  CA  A ASN A  1 357 ? -15.212 -14.226 -18.775 0.50 21.96 ? 357  ASN A CA  1 
ATOM   2869 C  CA  B ASN A  1 357 ? -15.138 -14.098 -18.771 0.50 19.71 ? 357  ASN A CA  1 
ATOM   2870 C  C   A ASN A  1 357 ? -14.777 -15.273 -17.747 0.50 20.29 ? 357  ASN A C   1 
ATOM   2871 C  C   B ASN A  1 357 ? -14.191 -14.771 -17.775 0.50 18.86 ? 357  ASN A C   1 
ATOM   2872 O  O   A ASN A  1 357 ? -14.681 -16.462 -18.111 0.50 19.89 ? 357  ASN A O   1 
ATOM   2873 O  O   B ASN A  1 357 ? -13.060 -15.092 -18.200 0.50 19.68 ? 357  ASN A O   1 
ATOM   2874 C  CB  A ASN A  1 357 ? -14.000 -13.700 -19.553 0.50 25.84 ? 357  ASN A CB  1 
ATOM   2875 C  CB  B ASN A  1 357 ? -14.390 -13.422 -19.928 0.50 20.41 ? 357  ASN A CB  1 
ATOM   2876 C  CG  A ASN A  1 357 ? -13.503 -14.659 -20.615 0.50 27.75 ? 357  ASN A CG  1 
ATOM   2877 C  CG  B ASN A  1 357 ? -15.317 -12.873 -20.987 0.50 21.19 ? 357  ASN A CG  1 
ATOM   2878 O  OD1 A ASN A  1 357 ? -14.257 -15.502 -21.096 0.50 31.94 ? 357  ASN A OD1 1 
ATOM   2879 O  OD1 B ASN A  1 357 ? -15.865 -13.627 -21.788 0.50 24.02 ? 357  ASN A OD1 1 
ATOM   2880 N  ND2 A ASN A  1 357 ? -12.244 -14.518 -21.011 0.50 32.83 ? 357  ASN A ND2 1 
ATOM   2881 N  ND2 B ASN A  1 357 ? -15.526 -11.568 -20.990 0.50 21.60 ? 357  ASN A ND2 1 
ATOM   2882 N  N   . GLY A  1 358 ? -14.592 -14.860 -16.494 1.00 17.55 ? 358  GLY A N   1 
ATOM   2883 C  CA  . GLY A  1 358 ? -13.933 -15.655 -15.452 1.00 16.82 ? 358  GLY A CA  1 
ATOM   2884 C  C   . GLY A  1 358 ? -13.605 -14.832 -14.224 1.00 15.02 ? 358  GLY A C   1 
ATOM   2885 O  O   . GLY A  1 358 ? -13.434 -13.612 -14.360 1.00 14.64 ? 358  GLY A O   1 
ATOM   2886 N  N   . LYS A  1 359 ? -13.501 -15.474 -13.055 1.00 16.70 ? 359  LYS A N   1 
ATOM   2887 C  CA  . LYS A  1 359 ? -13.335 -14.749 -11.771 1.00 17.44 ? 359  LYS A CA  1 
ATOM   2888 C  C   . LYS A  1 359 ? -11.978 -14.046 -11.743 1.00 16.56 ? 359  LYS A C   1 
ATOM   2889 O  O   . LYS A  1 359 ? -11.846 -13.027 -11.035 1.00 15.71 ? 359  LYS A O   1 
ATOM   2890 C  CB  . LYS A  1 359 ? -13.501 -15.677 -10.571 1.00 20.47 ? 359  LYS A CB  1 
ATOM   2891 C  CG  . LYS A  1 359 ? -12.407 -16.680 -10.357 1.00 23.66 ? 359  LYS A CG  1 
ATOM   2892 C  CD  . LYS A  1 359 ? -12.569 -17.412 -9.055  1.00 23.49 ? 359  LYS A CD  1 
ATOM   2893 C  CE  . LYS A  1 359 ? -11.258 -18.042 -8.678  1.00 25.23 ? 359  LYS A CE  1 
ATOM   2894 N  NZ  . LYS A  1 359 ? -10.285 -17.089 -8.079  1.00 24.56 ? 359  LYS A NZ  1 
ATOM   2895 N  N   . ASP A  1 360 ? -10.988 -14.579 -12.458 1.00 14.90 ? 360  ASP A N   1 
ATOM   2896 C  CA  . ASP A  1 360 ? -9.625  -13.997 -12.394 1.00 16.45 ? 360  ASP A CA  1 
ATOM   2897 C  C   . ASP A  1 360 ? -9.315  -13.146 -13.632 1.00 17.53 ? 360  ASP A C   1 
ATOM   2898 O  O   . ASP A  1 360 ? -8.110  -12.782 -13.821 1.00 17.10 ? 360  ASP A O   1 
ATOM   2899 C  CB  . ASP A  1 360 ? -8.596  -15.102 -12.145 1.00 17.96 ? 360  ASP A CB  1 
ATOM   2900 C  CG  . ASP A  1 360 ? -8.822  -15.913 -10.884 1.00 20.79 ? 360  ASP A CG  1 
ATOM   2901 O  OD1 . ASP A  1 360 ? -9.318  -15.361 -9.882  1.00 20.07 ? 360  ASP A OD1 1 
ATOM   2902 O  OD2 . ASP A  1 360 ? -8.503  -17.122 -10.909 1.00 23.45 ? 360  ASP A OD2 1 
ATOM   2903 N  N   . THR A  1 361 ? -10.319 -12.787 -14.426 1.00 16.07 ? 361  THR A N   1 
ATOM   2904 C  CA  . THR A  1 361 ? -10.137 -11.971 -15.649 1.00 17.83 ? 361  THR A CA  1 
ATOM   2905 C  C   . THR A  1 361 ? -10.310 -10.508 -15.268 1.00 15.92 ? 361  THR A C   1 
ATOM   2906 O  O   . THR A  1 361 ? -11.409 -10.096 -14.871 1.00 13.56 ? 361  THR A O   1 
ATOM   2907 C  CB  . THR A  1 361 ? -11.112 -12.357 -16.765 1.00 18.83 ? 361  THR A CB  1 
ATOM   2908 O  OG1 . THR A  1 361 ? -10.836 -13.702 -17.133 1.00 21.89 ? 361  THR A OG1 1 
ATOM   2909 C  CG2 . THR A  1 361 ? -11.019 -11.444 -17.972 1.00 20.68 ? 361  THR A CG2 1 
ATOM   2910 N  N   . PRO A  1 362 ? -9.274  -9.671  -15.419 1.00 16.14 ? 362  PRO A N   1 
ATOM   2911 C  CA  . PRO A  1 362 ? -9.414  -8.256  -15.117 1.00 17.14 ? 362  PRO A CA  1 
ATOM   2912 C  C   . PRO A  1 362 ? -10.480 -7.644  -16.019 1.00 15.83 ? 362  PRO A C   1 
ATOM   2913 O  O   . PRO A  1 362 ? -10.582 -8.017  -17.185 1.00 17.48 ? 362  PRO A O   1 
ATOM   2914 C  CB  . PRO A  1 362 ? -8.029  -7.673  -15.412 1.00 18.14 ? 362  PRO A CB  1 
ATOM   2915 C  CG  . PRO A  1 362 ? -7.122  -8.865  -15.214 1.00 19.17 ? 362  PRO A CG  1 
ATOM   2916 C  CD  . PRO A  1 362 ? -7.890  -10.015 -15.818 1.00 18.41 ? 362  PRO A CD  1 
ATOM   2917 N  N   . VAL A  1 363 ? -11.259 -6.733  -15.452 1.00 15.65 ? 363  VAL A N   1 
ATOM   2918 C  CA  . VAL A  1 363 ? -12.289 -5.937  -16.175 1.00 15.92 ? 363  VAL A CA  1 
ATOM   2919 C  C   . VAL A  1 363 ? -12.074 -4.473  -15.838 1.00 16.36 ? 363  VAL A C   1 
ATOM   2920 O  O   . VAL A  1 363 ? -12.074 -4.117  -14.644 1.00 15.41 ? 363  VAL A O   1 
ATOM   2921 C  CB  . VAL A  1 363 ? -13.718 -6.409  -15.817 1.00 14.64 ? 363  VAL A CB  1 
ATOM   2922 C  CG1 . VAL A  1 363 ? -14.777 -5.506  -16.443 1.00 14.24 ? 363  VAL A CG1 1 
ATOM   2923 C  CG2 . VAL A  1 363 ? -13.922 -7.846  -16.216 1.00 15.73 ? 363  VAL A CG2 1 
ATOM   2924 N  N   . ASN A  1 364 ? -11.934 -3.625  -16.847 1.00 18.87 ? 364  ASN A N   1 
ATOM   2925 C  CA  . ASN A  1 364 ? -11.503 -2.226  -16.595 1.00 21.51 ? 364  ASN A CA  1 
ATOM   2926 C  C   . ASN A  1 364 ? -12.681 -1.270  -16.734 1.00 19.43 ? 364  ASN A C   1 
ATOM   2927 O  O   . ASN A  1 364 ? -12.473 -0.062  -16.585 1.00 18.76 ? 364  ASN A O   1 
ATOM   2928 C  CB  . ASN A  1 364 ? -10.321 -1.822  -17.477 1.00 26.33 ? 364  ASN A CB  1 
ATOM   2929 C  CG  . ASN A  1 364 ? -10.582 -2.010  -18.952 1.00 31.02 ? 364  ASN A CG  1 
ATOM   2930 O  OD1 . ASN A  1 364 ? -11.730 -1.970  -19.403 1.00 42.18 ? 364  ASN A OD1 1 
ATOM   2931 N  ND2 . ASN A  1 364 ? -9.519  -2.205  -19.720 1.00 42.54 ? 364  ASN A ND2 1 
ATOM   2932 N  N   . GLY A  1 365 ? -13.895 -1.774  -16.928 1.00 19.44 ? 365  GLY A N   1 
ATOM   2933 C  CA  . GLY A  1 365 ? -15.082 -0.894  -16.950 1.00 18.53 ? 365  GLY A CA  1 
ATOM   2934 C  C   . GLY A  1 365 ? -16.300 -1.622  -17.480 1.00 17.23 ? 365  GLY A C   1 
ATOM   2935 O  O   . GLY A  1 365 ? -16.250 -2.862  -17.616 1.00 18.32 ? 365  GLY A O   1 
ATOM   2936 N  N   . THR A  1 366 ? -17.353 -0.857  -17.732 1.00 16.32 ? 366  THR A N   1 
ATOM   2937 C  CA  . THR A  1 366 ? -18.692 -1.323  -18.147 1.00 16.63 ? 366  THR A CA  1 
ATOM   2938 C  C   . THR A  1 366 ? -18.974 -0.770  -19.555 1.00 17.03 ? 366  THR A C   1 
ATOM   2939 O  O   . THR A  1 366 ? -18.186 0.006   -20.038 1.00 17.60 ? 366  THR A O   1 
ATOM   2940 C  CB  . THR A  1 366 ? -19.729 -0.937  -17.097 1.00 16.05 ? 366  THR A CB  1 
ATOM   2941 O  OG1 . THR A  1 366 ? -19.761 0.483   -17.033 1.00 16.53 ? 366  THR A OG1 1 
ATOM   2942 C  CG2 . THR A  1 366 ? -19.408 -1.444  -15.706 1.00 15.72 ? 366  THR A CG2 1 
ATOM   2943 N  N   . ASN A  1 367 ? -20.035 -1.223  -20.203 1.00 18.21 ? 367  ASN A N   1 
ATOM   2944 C  CA  A ASN A  1 367 ? -20.388 -0.869  -21.603 0.90 20.08 ? 367  ASN A CA  1 
ATOM   2945 C  CA  B ASN A  1 367 ? -20.375 -0.814  -21.588 0.10 17.75 ? 367  ASN A CA  1 
ATOM   2946 C  C   . ASN A  1 367 ? -21.825 -0.341  -21.594 1.00 18.90 ? 367  ASN A C   1 
ATOM   2947 O  O   . ASN A  1 367 ? -22.645 -0.891  -20.819 1.00 15.77 ? 367  ASN A O   1 
ATOM   2948 C  CB  A ASN A  1 367 ? -20.337 -2.077  -22.546 0.90 24.83 ? 367  ASN A CB  1 
ATOM   2949 C  CB  B ASN A  1 367 ? -20.147 -1.937  -22.602 0.10 17.60 ? 367  ASN A CB  1 
ATOM   2950 C  CG  A ASN A  1 367 ? -19.090 -2.922  -22.375 0.90 30.32 ? 367  ASN A CG  1 
ATOM   2951 C  CG  B ASN A  1 367 ? -18.700 -2.065  -23.029 0.10 17.24 ? 367  ASN A CG  1 
ATOM   2952 O  OD1 A ASN A  1 367 ? -17.997 -2.459  -22.694 0.90 31.20 ? 367  ASN A OD1 1 
ATOM   2953 O  OD1 B ASN A  1 367 ? -18.140 -3.159  -23.013 0.10 16.65 ? 367  ASN A OD1 1 
ATOM   2954 N  ND2 A ASN A  1 367 ? -19.226 -4.133  -21.840 0.90 36.33 ? 367  ASN A ND2 1 
ATOM   2955 N  ND2 B ASN A  1 367 ? -18.089 -0.957  -23.414 0.10 16.48 ? 367  ASN A ND2 1 
ATOM   2956 N  N   . THR A  1 368 ? -22.114 0.652   -22.420 1.00 18.85 ? 368  THR A N   1 
ATOM   2957 C  CA  . THR A  1 368 ? -23.496 1.126   -22.602 1.00 18.46 ? 368  THR A CA  1 
ATOM   2958 C  C   . THR A  1 368 ? -24.145 0.183   -23.618 1.00 18.76 ? 368  THR A C   1 
ATOM   2959 O  O   . THR A  1 368 ? -23.548 -0.034  -24.718 1.00 21.35 ? 368  THR A O   1 
ATOM   2960 C  CB  . THR A  1 368 ? -23.520 2.618   -22.976 1.00 20.50 ? 368  THR A CB  1 
ATOM   2961 O  OG1 . THR A  1 368 ? -23.028 3.402   -21.890 1.00 24.17 ? 368  THR A OG1 1 
ATOM   2962 C  CG2 . THR A  1 368 ? -24.920 3.087   -23.283 1.00 20.23 ? 368  THR A CG2 1 
ATOM   2963 N  N   . VAL A  1 369 ? -25.327 -0.361  -23.312 1.00 16.69 ? 369  VAL A N   1 
ATOM   2964 C  CA  . VAL A  1 369 ? -26.107 -1.136  -24.307 1.00 17.87 ? 369  VAL A CA  1 
ATOM   2965 C  C   . VAL A  1 369 ? -26.894 -0.111  -25.130 1.00 18.05 ? 369  VAL A C   1 
ATOM   2966 O  O   . VAL A  1 369 ? -26.786 -0.102  -26.363 1.00 17.25 ? 369  VAL A O   1 
ATOM   2967 C  CB  . VAL A  1 369 ? -27.014 -2.164  -23.621 1.00 17.71 ? 369  VAL A CB  1 
ATOM   2968 C  CG1 . VAL A  1 369 ? -27.806 -2.974  -24.647 1.00 19.57 ? 369  VAL A CG1 1 
ATOM   2969 C  CG2 . VAL A  1 369 ? -26.210 -3.071  -22.697 1.00 18.92 ? 369  VAL A CG2 1 
ATOM   2970 N  N   . PHE A  1 370 ? -27.643 0.760   -24.470 1.00 17.54 ? 370  PHE A N   1 
ATOM   2971 C  CA  . PHE A  1 370 ? -28.234 1.961   -25.120 1.00 16.60 ? 370  PHE A CA  1 
ATOM   2972 C  C   . PHE A  1 370 ? -28.628 2.991   -24.069 1.00 16.32 ? 370  PHE A C   1 
ATOM   2973 O  O   . PHE A  1 370 ? -28.887 2.632   -22.909 1.00 15.09 ? 370  PHE A O   1 
ATOM   2974 C  CB  . PHE A  1 370 ? -29.465 1.670   -25.983 1.00 15.81 ? 370  PHE A CB  1 
ATOM   2975 C  CG  . PHE A  1 370 ? -30.547 0.865   -25.309 1.00 17.49 ? 370  PHE A CG  1 
ATOM   2976 C  CD1 . PHE A  1 370 ? -31.455 1.480   -24.470 1.00 18.73 ? 370  PHE A CD1 1 
ATOM   2977 C  CD2 . PHE A  1 370 ? -30.675 -0.493  -25.531 1.00 17.42 ? 370  PHE A CD2 1 
ATOM   2978 C  CE1 . PHE A  1 370 ? -32.469 0.752   -23.873 1.00 17.67 ? 370  PHE A CE1 1 
ATOM   2979 C  CE2 . PHE A  1 370 ? -31.673 -1.229  -24.893 1.00 17.65 ? 370  PHE A CE2 1 
ATOM   2980 C  CZ  . PHE A  1 370 ? -32.550 -0.603  -24.057 1.00 17.33 ? 370  PHE A CZ  1 
ATOM   2981 N  N   . SER A  1 371 ? -28.640 4.243   -24.512 1.00 16.39 ? 371  SER A N   1 
ATOM   2982 C  CA  . SER A  1 371 ? -29.330 5.368   -23.841 1.00 15.64 ? 371  SER A CA  1 
ATOM   2983 C  C   . SER A  1 371 ? -30.354 5.915   -24.833 1.00 17.51 ? 371  SER A C   1 
ATOM   2984 O  O   . SER A  1 371 ? -29.967 6.275   -25.986 1.00 17.24 ? 371  SER A O   1 
ATOM   2985 C  CB  . SER A  1 371 ? -28.367 6.395   -23.343 1.00 16.24 ? 371  SER A CB  1 
ATOM   2986 O  OG  . SER A  1 371 ? -29.074 7.532   -22.878 1.00 18.73 ? 371  SER A OG  1 
ATOM   2987 N  N   . LYS A  1 372 ? -31.632 5.834   -24.487 1.00 17.93 ? 372  LYS A N   1 
ATOM   2988 C  CA  . LYS A  1 372 ? -32.731 6.233   -25.414 1.00 20.61 ? 372  LYS A CA  1 
ATOM   2989 C  C   . LYS A  1 372 ? -33.823 6.921   -24.600 1.00 21.17 ? 372  LYS A C   1 
ATOM   2990 O  O   . LYS A  1 372 ? -33.961 6.638   -23.410 1.00 18.40 ? 372  LYS A O   1 
ATOM   2991 C  CB  . LYS A  1 372 ? -33.421 5.043   -26.084 1.00 24.41 ? 372  LYS A CB  1 
ATOM   2992 C  CG  . LYS A  1 372 ? -32.588 4.252   -27.068 1.00 31.47 ? 372  LYS A CG  1 
ATOM   2993 C  CD  . LYS A  1 372 ? -33.386 3.171   -27.771 1.00 33.88 ? 372  LYS A CD  1 
ATOM   2994 C  CE  . LYS A  1 372 ? -33.781 2.033   -26.859 1.00 38.81 ? 372  LYS A CE  1 
ATOM   2995 N  NZ  . LYS A  1 372 ? -33.891 0.747   -27.599 1.00 42.67 ? 372  LYS A NZ  1 
ATOM   2996 N  N   . ARG A  1 373 ? -34.604 7.749   -25.270 1.00 22.08 ? 373  ARG A N   1 
ATOM   2997 C  CA  . ARG A  1 373 ? -35.831 8.345   -24.695 1.00 23.19 ? 373  ARG A CA  1 
ATOM   2998 C  C   . ARG A  1 373 ? -36.927 7.284   -24.656 1.00 21.44 ? 373  ARG A C   1 
ATOM   2999 O  O   . ARG A  1 373 ? -37.117 6.574   -25.638 1.00 20.97 ? 373  ARG A O   1 
ATOM   3000 C  CB  . ARG A  1 373 ? -36.263 9.522   -25.556 1.00 25.65 ? 373  ARG A CB  1 
ATOM   3001 C  CG  . ARG A  1 373 ? -37.612 10.094  -25.160 1.00 31.84 ? 373  ARG A CG  1 
ATOM   3002 C  CD  . ARG A  1 373 ? -37.877 11.322  -26.010 1.00 37.92 ? 373  ARG A CD  1 
ATOM   3003 N  NE  . ARG A  1 373 ? -39.233 11.836  -25.864 1.00 44.13 ? 373  ARG A NE  1 
ATOM   3004 C  CZ  . ARG A  1 373 ? -40.330 11.250  -26.330 1.00 48.21 ? 373  ARG A CZ  1 
ATOM   3005 N  NH1 . ARG A  1 373 ? -40.261 10.096  -26.980 1.00 49.03 ? 373  ARG A NH1 1 
ATOM   3006 N  NH2 . ARG A  1 373 ? -41.502 11.835  -26.138 1.00 55.04 ? 373  ARG A NH2 1 
ATOM   3007 N  N   . TYR A  1 374 ? -37.626 7.158   -23.532 1.00 21.01 ? 374  TYR A N   1 
ATOM   3008 C  CA  . TYR A  1 374 ? -38.863 6.352   -23.435 1.00 21.40 ? 374  TYR A CA  1 
ATOM   3009 C  C   . TYR A  1 374 ? -40.001 7.280   -23.034 1.00 22.66 ? 374  TYR A C   1 
ATOM   3010 O  O   . TYR A  1 374 ? -39.771 8.233   -22.262 1.00 24.80 ? 374  TYR A O   1 
ATOM   3011 C  CB  . TYR A  1 374 ? -38.749 5.199   -22.431 1.00 19.57 ? 374  TYR A CB  1 
ATOM   3012 C  CG  . TYR A  1 374 ? -37.962 4.011   -22.915 1.00 19.29 ? 374  TYR A CG  1 
ATOM   3013 C  CD1 . TYR A  1 374 ? -36.590 4.101   -23.087 1.00 18.88 ? 374  TYR A CD1 1 
ATOM   3014 C  CD2 . TYR A  1 374 ? -38.581 2.816   -23.219 1.00 17.74 ? 374  TYR A CD2 1 
ATOM   3015 C  CE1 . TYR A  1 374 ? -35.859 3.015   -23.521 1.00 19.44 ? 374  TYR A CE1 1 
ATOM   3016 C  CE2 . TYR A  1 374 ? -37.863 1.726   -23.661 1.00 18.98 ? 374  TYR A CE2 1 
ATOM   3017 C  CZ  . TYR A  1 374 ? -36.495 1.818   -23.793 1.00 18.24 ? 374  TYR A CZ  1 
ATOM   3018 O  OH  . TYR A  1 374 ? -35.755 0.737   -24.192 1.00 20.01 ? 374  TYR A OH  1 
ATOM   3019 N  N   . THR A  1 375 ? -41.180 7.033   -23.588 1.00 24.90 ? 375  THR A N   1 
ATOM   3020 C  CA  . THR A  1 375 ? -42.414 7.715   -23.133 1.00 25.86 ? 375  THR A CA  1 
ATOM   3021 C  C   . THR A  1 375 ? -43.046 6.863   -22.033 1.00 23.93 ? 375  THR A C   1 
ATOM   3022 O  O   . THR A  1 375 ? -43.032 5.630   -22.125 1.00 23.47 ? 375  THR A O   1 
ATOM   3023 C  CB  . THR A  1 375 ? -43.403 7.965   -24.271 1.00 33.62 ? 375  THR A CB  1 
ATOM   3024 O  OG1 . THR A  1 375 ? -43.648 6.661   -24.788 1.00 37.53 ? 375  THR A OG1 1 
ATOM   3025 C  CG2 . THR A  1 375 ? -42.880 8.930   -25.312 1.00 33.94 ? 375  THR A CG2 1 
ATOM   3026 N  N   . VAL A  1 376 ? -43.533 7.527   -20.995 1.00 23.09 ? 376  VAL A N   1 
ATOM   3027 C  CA  . VAL A  1 376 ? -44.207 6.870   -19.843 1.00 22.57 ? 376  VAL A CA  1 
ATOM   3028 C  C   . VAL A  1 376 ? -45.649 6.661   -20.264 1.00 23.96 ? 376  VAL A C   1 
ATOM   3029 O  O   . VAL A  1 376 ? -46.306 7.632   -20.623 1.00 25.25 ? 376  VAL A O   1 
ATOM   3030 C  CB  . VAL A  1 376 ? -44.089 7.711   -18.565 1.00 22.41 ? 376  VAL A CB  1 
ATOM   3031 C  CG1 . VAL A  1 376 ? -44.839 7.064   -17.403 1.00 24.65 ? 376  VAL A CG1 1 
ATOM   3032 C  CG2 . VAL A  1 376 ? -42.638 7.968   -18.212 1.00 25.70 ? 376  VAL A CG2 1 
ATOM   3033 N  N   . SER A  1 377 ? -46.075 5.425   -20.368 1.00 23.75 ? 377  SER A N   1 
ATOM   3034 C  CA  . SER A  1 377 ? -47.476 5.122   -20.695 1.00 27.67 ? 377  SER A CA  1 
ATOM   3035 C  C   . SER A  1 377 ? -48.096 4.482   -19.459 1.00 25.91 ? 377  SER A C   1 
ATOM   3036 O  O   . SER A  1 377 ? -47.552 3.476   -18.984 1.00 25.40 ? 377  SER A O   1 
ATOM   3037 C  CB  . SER A  1 377 ? -47.542 4.251   -21.917 1.00 29.17 ? 377  SER A CB  1 
ATOM   3038 O  OG  . SER A  1 377 ? -48.774 3.560   -21.914 1.00 38.06 ? 377  SER A OG  1 
ATOM   3039 N  N   . ASN A  1 378 ? -49.174 5.062   -18.930 1.00 23.87 ? 378  ASN A N   1 
ATOM   3040 C  CA  A ASN A  1 378 ? -49.874 4.451   -17.778 0.70 23.80 ? 378  ASN A CA  1 
ATOM   3041 C  CA  B ASN A  1 378 ? -49.901 4.542   -17.740 0.30 24.01 ? 378  ASN A CA  1 
ATOM   3042 C  C   . ASN A  1 378 ? -48.880 4.207   -16.644 1.00 21.85 ? 378  ASN A C   1 
ATOM   3043 O  O   . ASN A  1 378 ? -48.923 3.092   -16.088 1.00 21.56 ? 378  ASN A O   1 
ATOM   3044 C  CB  A ASN A  1 378 ? -50.534 3.124   -18.149 0.70 23.02 ? 378  ASN A CB  1 
ATOM   3045 C  CB  B ASN A  1 378 ? -50.886 3.422   -18.103 0.30 24.52 ? 378  ASN A CB  1 
ATOM   3046 C  CG  A ASN A  1 378 ? -51.472 2.620   -17.065 0.70 23.17 ? 378  ASN A CG  1 
ATOM   3047 C  CG  B ASN A  1 378 ? -50.329 2.353   -19.017 0.30 24.78 ? 378  ASN A CG  1 
ATOM   3048 O  OD1 A ASN A  1 378 ? -52.179 3.398   -16.405 0.70 18.00 ? 378  ASN A OD1 1 
ATOM   3049 O  OD1 B ASN A  1 378 ? -50.560 2.380   -20.230 0.30 23.22 ? 378  ASN A OD1 1 
ATOM   3050 N  ND2 A ASN A  1 378 ? -51.455 1.316   -16.878 0.70 21.94 ? 378  ASN A ND2 1 
ATOM   3051 N  ND2 B ASN A  1 378 ? -49.621 1.398   -18.438 0.30 23.90 ? 378  ASN A ND2 1 
ATOM   3052 N  N   . GLY A  1 379 ? -48.026 5.187   -16.347 1.00 21.51 ? 379  GLY A N   1 
ATOM   3053 C  CA  . GLY A  1 379 ? -47.055 5.136   -15.238 1.00 21.35 ? 379  GLY A CA  1 
ATOM   3054 C  C   . GLY A  1 379 ? -45.999 4.063   -15.429 1.00 20.67 ? 379  GLY A C   1 
ATOM   3055 O  O   . GLY A  1 379 ? -45.366 3.727   -14.434 1.00 19.16 ? 379  GLY A O   1 
ATOM   3056 N  N   . THR A  1 380 ? -45.810 3.579   -16.659 1.00 21.49 ? 380  THR A N   1 
ATOM   3057 C  CA  . THR A  1 380 ? -45.055 2.348   -16.987 1.00 21.81 ? 380  THR A CA  1 
ATOM   3058 C  C   . THR A  1 380 ? -44.065 2.671   -18.109 1.00 21.72 ? 380  THR A C   1 
ATOM   3059 O  O   . THR A  1 380 ? -44.401 3.449   -19.067 1.00 22.35 ? 380  THR A O   1 
ATOM   3060 C  CB  . THR A  1 380 ? -46.016 1.202   -17.335 1.00 24.39 ? 380  THR A CB  1 
ATOM   3061 O  OG1 . THR A  1 380 ? -46.752 0.858   -16.151 1.00 26.32 ? 380  THR A OG1 1 
ATOM   3062 C  CG2 . THR A  1 380 ? -45.334 -0.046  -17.839 1.00 26.17 ? 380  THR A CG2 1 
ATOM   3063 N  N   . ILE A  1 381 ? -42.865 2.124   -17.968 1.00 19.11 ? 381  ILE A N   1 
ATOM   3064 C  CA  . ILE A  1 381 ? -41.843 2.068   -19.034 1.00 18.83 ? 381  ILE A CA  1 
ATOM   3065 C  C   . ILE A  1 381 ? -41.542 0.587   -19.229 1.00 18.13 ? 381  ILE A C   1 
ATOM   3066 O  O   . ILE A  1 381 ? -41.293 -0.083  -18.215 1.00 17.83 ? 381  ILE A O   1 
ATOM   3067 C  CB  . ILE A  1 381 ? -40.621 2.877   -18.578 1.00 20.10 ? 381  ILE A CB  1 
ATOM   3068 C  CG1 . ILE A  1 381 ? -40.963 4.367   -18.586 1.00 22.64 ? 381  ILE A CG1 1 
ATOM   3069 C  CG2 . ILE A  1 381 ? -39.384 2.573   -19.388 1.00 23.90 ? 381  ILE A CG2 1 
ATOM   3070 C  CD1 . ILE A  1 381 ? -39.869 5.233   -18.039 1.00 23.23 ? 381  ILE A CD1 1 
ATOM   3071 N  N   . ASN A  1 382 ? -41.562 0.109   -20.455 1.00 17.18 ? 382  ASN A N   1 
ATOM   3072 C  CA  . ASN A  1 382 ? -41.211 -1.300  -20.773 1.00 19.99 ? 382  ASN A CA  1 
ATOM   3073 C  C   . ASN A  1 382 ? -39.862 -1.318  -21.499 1.00 18.99 ? 382  ASN A C   1 
ATOM   3074 O  O   . ASN A  1 382 ? -39.804 -0.905  -22.688 1.00 17.31 ? 382  ASN A O   1 
ATOM   3075 C  CB  . ASN A  1 382 ? -42.313 -1.976  -21.594 1.00 21.83 ? 382  ASN A CB  1 
ATOM   3076 C  CG  . ASN A  1 382 ? -43.691 -1.717  -21.016 1.00 30.24 ? 382  ASN A CG  1 
ATOM   3077 O  OD1 . ASN A  1 382 ? -44.462 -0.931  -21.573 1.00 33.91 ? 382  ASN A OD1 1 
ATOM   3078 N  ND2 . ASN A  1 382 ? -43.979 -2.299  -19.863 1.00 26.92 ? 382  ASN A ND2 1 
ATOM   3079 N  N   . VAL A  1 383 ? -38.803 -1.727  -20.805 1.00 17.82 ? 383  VAL A N   1 
ATOM   3080 C  CA  . VAL A  1 383 ? -37.428 -1.730  -21.373 1.00 16.94 ? 383  VAL A CA  1 
ATOM   3081 C  C   . VAL A  1 383 ? -37.128 -3.167  -21.796 1.00 18.90 ? 383  VAL A C   1 
ATOM   3082 O  O   . VAL A  1 383 ? -37.213 -4.072  -20.943 1.00 19.80 ? 383  VAL A O   1 
ATOM   3083 C  CB  . VAL A  1 383 ? -36.386 -1.212  -20.372 1.00 17.69 ? 383  VAL A CB  1 
ATOM   3084 C  CG1 . VAL A  1 383 ? -34.997 -1.138  -20.990 1.00 18.06 ? 383  VAL A CG1 1 
ATOM   3085 C  CG2 . VAL A  1 383 ? -36.769 0.118   -19.746 1.00 17.48 ? 383  VAL A CG2 1 
ATOM   3086 N  N   . SER A  1 384 ? -36.767 -3.393  -23.051 1.00 18.28 ? 384  SER A N   1 
ATOM   3087 C  CA  . SER A  1 384 ? -36.314 -4.724  -23.516 1.00 18.51 ? 384  SER A CA  1 
ATOM   3088 C  C   . SER A  1 384 ? -34.811 -4.675  -23.746 1.00 18.40 ? 384  SER A C   1 
ATOM   3089 O  O   . SER A  1 384 ? -34.338 -3.815  -24.541 1.00 18.19 ? 384  SER A O   1 
ATOM   3090 C  CB  . SER A  1 384 ? -37.103 -5.162  -24.726 1.00 20.66 ? 384  SER A CB  1 
ATOM   3091 O  OG  . SER A  1 384 ? -36.675 -6.421  -25.197 1.00 23.14 ? 384  SER A OG  1 
ATOM   3092 N  N   . ILE A  1 385 ? -34.071 -5.544  -23.060 1.00 16.16 ? 385  ILE A N   1 
ATOM   3093 C  CA  . ILE A  1 385 ? -32.590 -5.683  -23.184 1.00 16.76 ? 385  ILE A CA  1 
ATOM   3094 C  C   . ILE A  1 385 ? -32.301 -6.868  -24.091 1.00 17.93 ? 385  ILE A C   1 
ATOM   3095 O  O   . ILE A  1 385 ? -32.591 -7.994  -23.726 1.00 17.14 ? 385  ILE A O   1 
ATOM   3096 C  CB  . ILE A  1 385 ? -31.891 -5.847  -21.831 1.00 16.38 ? 385  ILE A CB  1 
ATOM   3097 C  CG1 . ILE A  1 385 ? -32.356 -4.809  -20.812 1.00 16.12 ? 385  ILE A CG1 1 
ATOM   3098 C  CG2 . ILE A  1 385 ? -30.391 -5.813  -22.042 1.00 16.82 ? 385  ILE A CG2 1 
ATOM   3099 C  CD1 . ILE A  1 385 ? -31.801 -5.011  -19.436 1.00 16.73 ? 385  ILE A CD1 1 
ATOM   3100 N  N   . PRO A  1 386 ? -31.784 -6.597  -25.308 1.00 19.31 ? 386  PRO A N   1 
ATOM   3101 C  CA  . PRO A  1 386 ? -31.579 -7.622  -26.324 1.00 20.17 ? 386  PRO A CA  1 
ATOM   3102 C  C   . PRO A  1 386 ? -30.252 -8.340  -26.093 1.00 17.35 ? 386  PRO A C   1 
ATOM   3103 O  O   . PRO A  1 386 ? -29.358 -7.770  -25.479 1.00 19.91 ? 386  PRO A O   1 
ATOM   3104 C  CB  . PRO A  1 386 ? -31.565 -6.812  -27.634 1.00 22.42 ? 386  PRO A CB  1 
ATOM   3105 C  CG  . PRO A  1 386 ? -30.963 -5.474  -27.220 1.00 24.28 ? 386  PRO A CG  1 
ATOM   3106 C  CD  . PRO A  1 386 ? -31.374 -5.252  -25.773 1.00 22.14 ? 386  PRO A CD  1 
ATOM   3107 N  N   . GLY A  1 387 ? -30.152 -9.567  -26.588 1.00 19.41 ? 387  GLY A N   1 
ATOM   3108 C  CA  . GLY A  1 387 ? -28.887 -10.324 -26.609 1.00 18.43 ? 387  GLY A CA  1 
ATOM   3109 C  C   . GLY A  1 387 ? -28.291 -10.508 -25.223 1.00 18.70 ? 387  GLY A C   1 
ATOM   3110 O  O   . GLY A  1 387 ? -27.055 -10.382 -25.070 1.00 18.39 ? 387  GLY A O   1 
ATOM   3111 N  N   . THR A  1 388 ? -29.117 -10.884 -24.254 1.00 17.86 ? 388  THR A N   1 
ATOM   3112 C  CA  . THR A  1 388 ? -28.659 -11.073 -22.860 1.00 17.05 ? 388  THR A CA  1 
ATOM   3113 C  C   . THR A  1 388 ? -28.087 -12.475 -22.693 1.00 16.96 ? 388  THR A C   1 
ATOM   3114 O  O   . THR A  1 388 ? -28.372 -13.371 -23.540 1.00 17.17 ? 388  THR A O   1 
ATOM   3115 C  CB  . THR A  1 388 ? -29.762 -10.798 -21.846 1.00 16.41 ? 388  THR A CB  1 
ATOM   3116 O  OG1 . THR A  1 388 ? -30.895 -11.588 -22.175 1.00 15.29 ? 388  THR A OG1 1 
ATOM   3117 C  CG2 . THR A  1 388 ? -30.135 -9.339  -21.824 1.00 16.48 ? 388  THR A CG2 1 
ATOM   3118 N  N   . ASN A  1 389 ? -27.293 -12.643 -21.645 1.00 15.31 ? 389  ASN A N   1 
ATOM   3119 C  CA  . ASN A  1 389 ? -26.663 -13.932 -21.308 1.00 15.37 ? 389  ASN A CA  1 
ATOM   3120 C  C   . ASN A  1 389 ? -26.812 -14.142 -19.787 1.00 15.45 ? 389  ASN A C   1 
ATOM   3121 O  O   . ASN A  1 389 ? -27.349 -13.270 -19.095 1.00 14.75 ? 389  ASN A O   1 
ATOM   3122 C  CB  . ASN A  1 389 ? -25.220 -13.968 -21.821 1.00 15.90 ? 389  ASN A CB  1 
ATOM   3123 C  CG  . ASN A  1 389 ? -24.362 -12.935 -21.139 1.00 15.19 ? 389  ASN A CG  1 
ATOM   3124 O  OD1 . ASN A  1 389 ? -24.157 -13.057 -19.939 1.00 15.06 ? 389  ASN A OD1 1 
ATOM   3125 N  ND2 . ASN A  1 389 ? -23.919 -11.919 -21.863 1.00 14.36 ? 389  ASN A ND2 1 
ATOM   3126 N  N   . ASN A  1 390 ? -26.321 -15.262 -19.284 1.00 14.26 ? 390  ASN A N   1 
ATOM   3127 C  CA  . ASN A  1 390 ? -26.577 -15.686 -17.888 1.00 14.23 ? 390  ASN A CA  1 
ATOM   3128 C  C   . ASN A  1 390 ? -25.529 -15.161 -16.905 1.00 14.66 ? 390  ASN A C   1 
ATOM   3129 O  O   . ASN A  1 390 ? -25.747 -15.359 -15.688 1.00 14.23 ? 390  ASN A O   1 
ATOM   3130 C  CB  . ASN A  1 390 ? -26.683 -17.212 -17.838 1.00 15.49 ? 390  ASN A CB  1 
ATOM   3131 C  CG  . ASN A  1 390 ? -27.806 -17.774 -18.693 1.00 16.23 ? 390  ASN A CG  1 
ATOM   3132 O  OD1 . ASN A  1 390 ? -28.724 -17.064 -19.081 1.00 15.34 ? 390  ASN A OD1 1 
ATOM   3133 N  ND2 . ASN A  1 390 ? -27.783 -19.086 -18.919 1.00 16.40 ? 390  ASN A ND2 1 
ATOM   3134 N  N   . THR A  1 391 ? -24.424 -14.558 -17.365 1.00 13.86 ? 391  THR A N   1 
ATOM   3135 C  CA  . THR A  1 391 ? -23.223 -14.238 -16.537 1.00 13.68 ? 391  THR A CA  1 
ATOM   3136 C  C   . THR A  1 391 ? -22.996 -12.729 -16.449 1.00 13.59 ? 391  THR A C   1 
ATOM   3137 O  O   . THR A  1 391 ? -22.419 -12.292 -15.432 1.00 12.64 ? 391  THR A O   1 
ATOM   3138 C  CB  . THR A  1 391 ? -21.976 -14.990 -17.018 1.00 14.03 ? 391  THR A CB  1 
ATOM   3139 O  OG1 . THR A  1 391 ? -21.686 -14.562 -18.351 1.00 13.61 ? 391  THR A OG1 1 
ATOM   3140 C  CG2 . THR A  1 391 ? -22.197 -16.481 -16.960 1.00 14.27 ? 391  THR A CG2 1 
ATOM   3141 N  N   . SER A  1 392 ? -23.444 -11.952 -17.450 1.00 13.74 ? 392  SER A N   1 
ATOM   3142 C  CA  . SER A  1 392 ? -23.345 -10.480 -17.422 1.00 13.32 ? 392  SER A CA  1 
ATOM   3143 C  C   . SER A  1 392 ? -24.223 -9.927  -16.285 1.00 12.58 ? 392  SER A C   1 
ATOM   3144 O  O   . SER A  1 392 ? -25.220 -10.608 -15.856 1.00 12.20 ? 392  SER A O   1 
ATOM   3145 C  CB  . SER A  1 392 ? -23.712 -9.888  -18.761 1.00 14.69 ? 392  SER A CB  1 
ATOM   3146 O  OG  . SER A  1 392 ? -22.726 -10.199 -19.754 1.00 14.86 ? 392  SER A OG  1 
ATOM   3147 N  N   . GLY A  1 393 ? -23.888 -8.733  -15.812 1.00 12.54 ? 393  GLY A N   1 
ATOM   3148 C  CA  . GLY A  1 393 ? -24.801 -7.923  -14.987 1.00 12.61 ? 393  GLY A CA  1 
ATOM   3149 C  C   . GLY A  1 393 ? -25.293 -6.739  -15.795 1.00 13.07 ? 393  GLY A C   1 
ATOM   3150 O  O   . GLY A  1 393 ? -24.529 -6.216  -16.596 1.00 12.95 ? 393  GLY A O   1 
ATOM   3151 N  N   . TYR A  1 394 ? -26.525 -6.296  -15.558 1.00 11.98 ? 394  TYR A N   1 
ATOM   3152 C  CA  . TYR A  1 394 ? -27.194 -5.218  -16.303 1.00 12.13 ? 394  TYR A CA  1 
ATOM   3153 C  C   . TYR A  1 394 ? -27.726 -4.194  -15.312 1.00 11.54 ? 394  TYR A C   1 
ATOM   3154 O  O   . TYR A  1 394 ? -28.116 -4.559  -14.202 1.00 10.85 ? 394  TYR A O   1 
ATOM   3155 C  CB  . TYR A  1 394 ? -28.318 -5.809  -17.147 1.00 12.71 ? 394  TYR A CB  1 
ATOM   3156 C  CG  . TYR A  1 394 ? -27.845 -6.867  -18.105 1.00 13.05 ? 394  TYR A CG  1 
ATOM   3157 C  CD1 . TYR A  1 394 ? -27.368 -6.541  -19.363 1.00 13.74 ? 394  TYR A CD1 1 
ATOM   3158 C  CD2 . TYR A  1 394 ? -27.911 -8.207  -17.767 1.00 13.82 ? 394  TYR A CD2 1 
ATOM   3159 C  CE1 . TYR A  1 394 ? -26.931 -7.513  -20.251 1.00 13.60 ? 394  TYR A CE1 1 
ATOM   3160 C  CE2 . TYR A  1 394 ? -27.445 -9.189  -18.625 1.00 13.46 ? 394  TYR A CE2 1 
ATOM   3161 C  CZ  . TYR A  1 394 ? -26.985 -8.845  -19.883 1.00 14.42 ? 394  TYR A CZ  1 
ATOM   3162 O  OH  . TYR A  1 394 ? -26.566 -9.853  -20.716 1.00 15.69 ? 394  TYR A OH  1 
ATOM   3163 N  N   . ARG A  1 395 ? -27.739 -2.939  -15.726 1.00 11.99 ? 395  ARG A N   1 
ATOM   3164 C  CA  . ARG A  1 395 ? -28.413 -1.849  -14.988 1.00 12.38 ? 395  ARG A CA  1 
ATOM   3165 C  C   . ARG A  1 395 ? -29.329 -1.116  -15.963 1.00 12.93 ? 395  ARG A C   1 
ATOM   3166 O  O   . ARG A  1 395 ? -28.936 -0.874  -17.136 1.00 11.74 ? 395  ARG A O   1 
ATOM   3167 C  CB  . ARG A  1 395 ? -27.407 -0.882  -14.365 1.00 12.94 ? 395  ARG A CB  1 
ATOM   3168 C  CG  . ARG A  1 395 ? -28.083 0.126   -13.458 1.00 12.68 ? 395  ARG A CG  1 
ATOM   3169 C  CD  . ARG A  1 395 ? -27.164 1.048   -12.706 1.00 13.08 ? 395  ARG A CD  1 
ATOM   3170 N  NE  . ARG A  1 395 ? -26.532 2.005   -13.598 1.00 13.45 ? 395  ARG A NE  1 
ATOM   3171 C  CZ  . ARG A  1 395 ? -25.833 3.046   -13.170 1.00 15.91 ? 395  ARG A CZ  1 
ATOM   3172 N  NH1 . ARG A  1 395 ? -25.720 3.290   -11.873 1.00 14.85 ? 395  ARG A NH1 1 
ATOM   3173 N  NH2 . ARG A  1 395 ? -25.262 3.865   -14.041 1.00 16.87 ? 395  ARG A NH2 1 
ATOM   3174 N  N   . VAL A  1 396 ? -30.530 -0.798  -15.478 1.00 12.48 ? 396  VAL A N   1 
ATOM   3175 C  CA  . VAL A  1 396 ? -31.473 0.132   -16.143 1.00 13.13 ? 396  VAL A CA  1 
ATOM   3176 C  C   . VAL A  1 396 ? -31.539 1.369   -15.256 1.00 12.98 ? 396  VAL A C   1 
ATOM   3177 O  O   . VAL A  1 396 ? -31.951 1.242   -14.080 1.00 12.13 ? 396  VAL A O   1 
ATOM   3178 C  CB  . VAL A  1 396 ? -32.846 -0.537  -16.350 1.00 12.89 ? 396  VAL A CB  1 
ATOM   3179 C  CG1 . VAL A  1 396 ? -33.801 0.408   -17.051 1.00 14.14 ? 396  VAL A CG1 1 
ATOM   3180 C  CG2 . VAL A  1 396 ? -32.749 -1.852  -17.082 1.00 13.98 ? 396  VAL A CG2 1 
ATOM   3181 N  N   . TYR A  1 397 ? -31.073 2.513   -15.763 1.00 12.26 ? 397  TYR A N   1 
ATOM   3182 C  CA  . TYR A  1 397 ? -30.996 3.767   -14.993 1.00 14.29 ? 397  TYR A CA  1 
ATOM   3183 C  C   . TYR A  1 397 ? -31.973 4.739   -15.655 1.00 13.89 ? 397  TYR A C   1 
ATOM   3184 O  O   . TYR A  1 397 ? -31.896 4.914   -16.865 1.00 14.07 ? 397  TYR A O   1 
ATOM   3185 C  CB  . TYR A  1 397 ? -29.555 4.258   -14.950 1.00 14.40 ? 397  TYR A CB  1 
ATOM   3186 C  CG  . TYR A  1 397 ? -29.349 5.431   -14.051 1.00 16.94 ? 397  TYR A CG  1 
ATOM   3187 C  CD1 . TYR A  1 397 ? -29.670 6.707   -14.496 1.00 17.36 ? 397  TYR A CD1 1 
ATOM   3188 C  CD2 . TYR A  1 397 ? -28.890 5.265   -12.747 1.00 18.43 ? 397  TYR A CD2 1 
ATOM   3189 C  CE1 . TYR A  1 397 ? -29.500 7.797   -13.673 1.00 19.35 ? 397  TYR A CE1 1 
ATOM   3190 C  CE2 . TYR A  1 397 ? -28.724 6.355   -11.911 1.00 18.81 ? 397  TYR A CE2 1 
ATOM   3191 C  CZ  . TYR A  1 397 ? -29.027 7.619   -12.387 1.00 20.96 ? 397  TYR A CZ  1 
ATOM   3192 O  OH  . TYR A  1 397 ? -28.868 8.740   -11.610 1.00 25.06 ? 397  TYR A OH  1 
ATOM   3193 N  N   . VAL A  1 398 ? -32.937 5.248   -14.906 1.00 14.45 ? 398  VAL A N   1 
ATOM   3194 C  CA  . VAL A  1 398 ? -34.056 6.069   -15.455 1.00 14.86 ? 398  VAL A CA  1 
ATOM   3195 C  C   . VAL A  1 398 ? -34.025 7.434   -14.774 1.00 15.41 ? 398  VAL A C   1 
ATOM   3196 O  O   . VAL A  1 398 ? -33.995 7.514   -13.517 1.00 12.87 ? 398  VAL A O   1 
ATOM   3197 C  CB  . VAL A  1 398 ? -35.416 5.393   -15.223 1.00 15.42 ? 398  VAL A CB  1 
ATOM   3198 C  CG1 . VAL A  1 398 ? -36.553 6.187   -15.861 1.00 18.19 ? 398  VAL A CG1 1 
ATOM   3199 C  CG2 . VAL A  1 398 ? -35.432 3.957   -15.686 1.00 15.98 ? 398  VAL A CG2 1 
ATOM   3200 N  N   . SER A  1 399 ? -34.057 8.493   -15.572 1.00 16.90 ? 399  SER A N   1 
ATOM   3201 C  CA  . SER A  1 399 ? -34.101 9.874   -15.032 1.00 19.02 ? 399  SER A CA  1 
ATOM   3202 C  C   . SER A  1 399 ? -34.920 10.752  -15.980 1.00 20.27 ? 399  SER A C   1 
ATOM   3203 O  O   . SER A  1 399 ? -35.295 10.285  -17.041 1.00 16.95 ? 399  SER A O   1 
ATOM   3204 C  CB  . SER A  1 399 ? -32.726 10.418  -14.841 1.00 21.73 ? 399  SER A CB  1 
ATOM   3205 O  OG  . SER A  1 399 ? -32.032 10.347  -16.058 1.00 22.43 ? 399  SER A OG  1 
ATOM   3206 N  N   . ARG A  1 400 ? -35.263 11.963  -15.575 1.00 25.87 ? 400  ARG A N   1 
ATOM   3207 C  CA  . ARG A  1 400 ? -36.161 12.803  -16.417 1.00 32.57 ? 400  ARG A CA  1 
ATOM   3208 C  C   . ARG A  1 400 ? -35.341 13.309  -17.620 1.00 31.16 ? 400  ARG A C   1 
ATOM   3209 O  O   . ARG A  1 400 ? -34.119 13.491  -17.473 1.00 29.19 ? 400  ARG A O   1 
ATOM   3210 C  CB  . ARG A  1 400 ? -36.830 13.882  -15.555 1.00 40.72 ? 400  ARG A CB  1 
ATOM   3211 C  CG  . ARG A  1 400 ? -36.118 15.227  -15.523 1.00 54.74 ? 400  ARG A CG  1 
ATOM   3212 C  CD  . ARG A  1 400 ? -36.959 16.300  -14.823 1.00 62.87 ? 400  ARG A CD  1 
ATOM   3213 N  NE  . ARG A  1 400 ? -37.947 17.001  -15.661 1.00 69.40 ? 400  ARG A NE  1 
ATOM   3214 C  CZ  . ARG A  1 400 ? -39.266 16.765  -15.714 1.00 64.69 ? 400  ARG A CZ  1 
ATOM   3215 N  NH1 . ARG A  1 400 ? -39.827 15.811  -14.986 1.00 65.44 ? 400  ARG A NH1 1 
ATOM   3216 N  NH2 . ARG A  1 400 ? -40.026 17.502  -16.507 1.00 61.74 ? 400  ARG A NH2 1 
ATOM   3217 N  N   . LEU A  1 401 ? -35.989 13.479  -18.776 1.00 32.96 ? 401  LEU A N   1 
ATOM   3218 C  CA  . LEU A  1 401 ? -35.330 13.761  -20.084 1.00 37.87 ? 401  LEU A CA  1 
ATOM   3219 C  C   . LEU A  1 401 ? -34.542 15.078  -20.049 1.00 39.89 ? 401  LEU A C   1 
ATOM   3220 O  O   . LEU A  1 401 ? -34.700 15.974  -19.234 1.00 48.88 ? 401  LEU A O   1 
ATOM   3221 C  CB  . LEU A  1 401 ? -36.390 13.794  -21.189 1.00 39.46 ? 401  LEU A CB  1 
ATOM   3222 C  CG  . LEU A  1 401 ? -35.881 13.673  -22.633 1.00 44.81 ? 401  LEU A CG  1 
ATOM   3223 C  CD1 . LEU A  1 401 ? -34.367 13.882  -22.760 1.00 49.74 ? 401  LEU A CD1 1 
ATOM   3224 C  CD2 . LEU A  1 401 ? -36.259 12.334  -23.236 1.00 45.08 ? 401  LEU A CD2 1 
ATOM   3225 N  N   . ALA B  1 2   ? -49.264 21.396  -26.299 1.00 25.75 ? 2    ALA B N   1 
ATOM   3226 C  CA  . ALA B  1 2   ? -50.033 21.698  -25.081 1.00 26.07 ? 2    ALA B CA  1 
ATOM   3227 C  C   . ALA B  1 2   ? -50.689 20.412  -24.588 1.00 23.71 ? 2    ALA B C   1 
ATOM   3228 O  O   . ALA B  1 2   ? -50.936 19.494  -25.379 1.00 28.16 ? 2    ALA B O   1 
ATOM   3229 C  CB  . ALA B  1 2   ? -51.077 22.758  -25.321 1.00 26.98 ? 2    ALA B CB  1 
ATOM   3230 N  N   . THR B  1 3   ? -50.924 20.362  -23.295 1.00 23.11 ? 3    THR B N   1 
ATOM   3231 C  CA  . THR B  1 3   ? -51.710 19.302  -22.639 1.00 22.07 ? 3    THR B CA  1 
ATOM   3232 C  C   . THR B  1 3   ? -53.116 19.859  -22.441 1.00 19.78 ? 3    THR B C   1 
ATOM   3233 O  O   . THR B  1 3   ? -53.244 20.921  -21.834 1.00 21.83 ? 3    THR B O   1 
ATOM   3234 C  CB  . THR B  1 3   ? -51.032 18.883  -21.341 1.00 22.30 ? 3    THR B CB  1 
ATOM   3235 O  OG1 . THR B  1 3   ? -49.663 18.607  -21.648 1.00 21.93 ? 3    THR B OG1 1 
ATOM   3236 C  CG2 . THR B  1 3   ? -51.679 17.657  -20.744 1.00 23.14 ? 3    THR B CG2 1 
ATOM   3237 N  N   . THR B  1 4   ? -54.115 19.159  -22.946 1.00 21.59 ? 4    THR B N   1 
ATOM   3238 C  CA  . THR B  1 4   ? -55.482 19.697  -23.106 1.00 21.37 ? 4    THR B CA  1 
ATOM   3239 C  C   . THR B  1 4   ? -56.455 18.976  -22.177 1.00 21.34 ? 4    THR B C   1 
ATOM   3240 O  O   . THR B  1 4   ? -56.354 17.758  -22.013 1.00 19.80 ? 4    THR B O   1 
ATOM   3241 C  CB  . THR B  1 4   ? -55.906 19.607  -24.575 1.00 24.10 ? 4    THR B CB  1 
ATOM   3242 O  OG1 . THR B  1 4   ? -54.970 20.419  -25.281 1.00 25.70 ? 4    THR B OG1 1 
ATOM   3243 C  CG2 . THR B  1 4   ? -57.304 20.113  -24.826 1.00 26.23 ? 4    THR B CG2 1 
ATOM   3244 N  N   . LEU B  1 5   ? -57.354 19.735  -21.559 1.00 20.56 ? 5    LEU B N   1 
ATOM   3245 C  CA  . LEU B  1 5   ? -58.581 19.158  -20.981 1.00 20.88 ? 5    LEU B CA  1 
ATOM   3246 C  C   . LEU B  1 5   ? -59.806 19.954  -21.440 1.00 19.46 ? 5    LEU B C   1 
ATOM   3247 O  O   . LEU B  1 5   ? -59.660 21.103  -21.904 1.00 19.89 ? 5    LEU B O   1 
ATOM   3248 C  CB  . LEU B  1 5   ? -58.498 19.108  -19.457 1.00 23.82 ? 5    LEU B CB  1 
ATOM   3249 C  CG  . LEU B  1 5   ? -57.967 20.331  -18.743 1.00 23.73 ? 5    LEU B CG  1 
ATOM   3250 C  CD1 . LEU B  1 5   ? -58.719 20.556  -17.438 1.00 27.76 ? 5    LEU B CD1 1 
ATOM   3251 C  CD2 . LEU B  1 5   ? -56.474 20.196  -18.462 1.00 24.15 ? 5    LEU B CD2 1 
ATOM   3252 N  N   . THR B  1 6   ? -60.951 19.288  -21.407 1.00 21.09 ? 6    THR B N   1 
ATOM   3253 C  CA  . THR B  1 6   ? -62.234 19.860  -21.847 1.00 20.31 ? 6    THR B CA  1 
ATOM   3254 C  C   . THR B  1 6   ? -63.196 19.816  -20.669 1.00 21.15 ? 6    THR B C   1 
ATOM   3255 O  O   . THR B  1 6   ? -63.300 18.770  -20.015 1.00 19.78 ? 6    THR B O   1 
ATOM   3256 C  CB  . THR B  1 6   ? -62.781 19.094  -23.048 1.00 22.83 ? 6    THR B CB  1 
ATOM   3257 O  OG1 . THR B  1 6   ? -61.757 19.085  -24.041 1.00 23.73 ? 6    THR B OG1 1 
ATOM   3258 C  CG2 . THR B  1 6   ? -64.043 19.736  -23.576 1.00 22.59 ? 6    THR B CG2 1 
ATOM   3259 N  N   . VAL B  1 7   ? -63.868 20.928  -20.428 1.00 18.72 ? 7    VAL B N   1 
ATOM   3260 C  CA  . VAL B  1 7   ? -64.854 21.086  -19.326 1.00 19.88 ? 7    VAL B CA  1 
ATOM   3261 C  C   . VAL B  1 7   ? -66.219 21.218  -19.982 1.00 19.17 ? 7    VAL B C   1 
ATOM   3262 O  O   . VAL B  1 7   ? -66.386 22.184  -20.744 1.00 19.72 ? 7    VAL B O   1 
ATOM   3263 C  CB  . VAL B  1 7   ? -64.512 22.315  -18.480 1.00 18.82 ? 7    VAL B CB  1 
ATOM   3264 C  CG1 . VAL B  1 7   ? -65.497 22.499  -17.333 1.00 19.41 ? 7    VAL B CG1 1 
ATOM   3265 C  CG2 . VAL B  1 7   ? -63.079 22.273  -17.996 1.00 19.68 ? 7    VAL B CG2 1 
ATOM   3266 N  N   . ASP B  1 8   ? -67.100 20.248  -19.738 1.00 20.04 ? 8    ASP B N   1 
ATOM   3267 C  CA  . ASP B  1 8   ? -68.485 20.258  -20.254 1.00 20.10 ? 8    ASP B CA  1 
ATOM   3268 C  C   . ASP B  1 8   ? -69.389 20.803  -19.140 1.00 20.08 ? 8    ASP B C   1 
ATOM   3269 O  O   . ASP B  1 8   ? -69.758 20.032  -18.240 1.00 17.21 ? 8    ASP B O   1 
ATOM   3270 C  CB  . ASP B  1 8   ? -68.890 18.865  -20.740 1.00 21.59 ? 8    ASP B CB  1 
ATOM   3271 C  CG  . ASP B  1 8   ? -70.259 18.873  -21.396 1.00 22.09 ? 8    ASP B CG  1 
ATOM   3272 O  OD1 . ASP B  1 8   ? -70.923 19.915  -21.292 1.00 20.78 ? 8    ASP B OD1 1 
ATOM   3273 O  OD2 . ASP B  1 8   ? -70.617 17.863  -22.045 1.00 25.10 ? 8    ASP B OD2 1 
ATOM   3274 N  N   . CYS B  1 9   ? -69.747 22.085  -19.203 1.00 20.90 ? 9    CYS B N   1 
ATOM   3275 C  CA  . CYS B  1 9   ? -70.480 22.789  -18.128 1.00 20.99 ? 9    CYS B CA  1 
ATOM   3276 C  C   . CYS B  1 9   ? -71.889 22.226  -17.969 1.00 20.59 ? 9    CYS B C   1 
ATOM   3277 O  O   . CYS B  1 9   ? -72.472 22.409  -16.888 1.00 18.34 ? 9    CYS B O   1 
ATOM   3278 C  CB  . CYS B  1 9   ? -70.582 24.271  -18.429 1.00 20.96 ? 9    CYS B CB  1 
ATOM   3279 S  SG  . CYS B  1 9   ? -68.957 25.058  -18.516 1.00 21.16 ? 9    CYS B SG  1 
ATOM   3280 N  N   . ARG B  1 10  ? -72.392 21.551  -18.995 1.00 19.42 ? 10   ARG B N   1 
ATOM   3281 C  CA  . ARG B  1 10  ? -73.763 20.979  -18.976 1.00 23.53 ? 10   ARG B CA  1 
ATOM   3282 C  C   . ARG B  1 10  ? -73.754 19.598  -18.325 1.00 21.97 ? 10   ARG B C   1 
ATOM   3283 O  O   . ARG B  1 10  ? -74.844 19.130  -17.922 1.00 22.73 ? 10   ARG B O   1 
ATOM   3284 C  CB  . ARG B  1 10  ? -74.266 20.874  -20.416 1.00 28.96 ? 10   ARG B CB  1 
ATOM   3285 C  CG  . ARG B  1 10  ? -75.725 20.472  -20.561 1.00 37.97 ? 10   ARG B CG  1 
ATOM   3286 C  CD  . ARG B  1 10  ? -76.000 20.396  -22.057 1.00 43.52 ? 10   ARG B CD  1 
ATOM   3287 N  NE  . ARG B  1 10  ? -75.439 19.189  -22.660 1.00 50.67 ? 10   ARG B NE  1 
ATOM   3288 C  CZ  . ARG B  1 10  ? -75.167 19.029  -23.961 1.00 52.51 ? 10   ARG B CZ  1 
ATOM   3289 N  NH1 . ARG B  1 10  ? -74.665 17.888  -24.402 1.00 50.97 ? 10   ARG B NH1 1 
ATOM   3290 N  NH2 . ARG B  1 10  ? -75.392 20.003  -24.821 1.00 57.37 ? 10   ARG B NH2 1 
ATOM   3291 N  N   . ALA B  1 11  ? -72.602 18.932  -18.248 1.00 19.60 ? 11   ALA B N   1 
ATOM   3292 C  CA  . ALA B  1 11  ? -72.551 17.508  -17.831 1.00 18.98 ? 11   ALA B CA  1 
ATOM   3293 C  C   . ALA B  1 11  ? -72.362 17.455  -16.319 1.00 18.75 ? 11   ALA B C   1 
ATOM   3294 O  O   . ALA B  1 11  ? -71.261 17.174  -15.826 1.00 18.84 ? 11   ALA B O   1 
ATOM   3295 C  CB  . ALA B  1 11  ? -71.494 16.772  -18.587 1.00 18.49 ? 11   ALA B CB  1 
ATOM   3296 N  N   . THR B  1 12  ? -73.430 17.707  -15.590 1.00 18.15 ? 12   THR B N   1 
ATOM   3297 C  CA  . THR B  1 12  ? -73.465 17.624  -14.115 1.00 17.34 ? 12   THR B CA  1 
ATOM   3298 C  C   . THR B  1 12  ? -73.067 16.214  -13.685 1.00 17.55 ? 12   THR B C   1 
ATOM   3299 O  O   . THR B  1 12  ? -73.633 15.255  -14.233 1.00 17.83 ? 12   THR B O   1 
ATOM   3300 C  CB  . THR B  1 12  ? -74.852 17.999  -13.587 1.00 17.79 ? 12   THR B CB  1 
ATOM   3301 O  OG1 . THR B  1 12  ? -75.058 19.334  -14.028 1.00 21.71 ? 12   THR B OG1 1 
ATOM   3302 C  CG2 . THR B  1 12  ? -74.945 17.876  -12.084 1.00 18.52 ? 12   THR B CG2 1 
ATOM   3303 N  N   . LEU B  1 13  ? -72.151 16.085  -12.725 1.00 17.04 ? 13   LEU B N   1 
ATOM   3304 C  CA  . LEU B  1 13  ? -71.840 14.774  -12.106 1.00 17.16 ? 13   LEU B CA  1 
ATOM   3305 C  C   . LEU B  1 13  ? -72.713 14.610  -10.887 1.00 16.92 ? 13   LEU B C   1 
ATOM   3306 O  O   . LEU B  1 13  ? -73.401 13.588  -10.816 1.00 17.33 ? 13   LEU B O   1 
ATOM   3307 C  CB  . LEU B  1 13  ? -70.353 14.678  -11.762 1.00 17.80 ? 13   LEU B CB  1 
ATOM   3308 C  CG  . LEU B  1 13  ? -69.406 14.896  -12.937 1.00 20.07 ? 13   LEU B CG  1 
ATOM   3309 C  CD1 . LEU B  1 13  ? -67.956 14.982  -12.461 1.00 21.12 ? 13   LEU B CD1 1 
ATOM   3310 C  CD2 . LEU B  1 13  ? -69.607 13.798  -13.987 1.00 21.41 ? 13   LEU B CD2 1 
ATOM   3311 N  N   . ARG B  1 14  ? -72.706 15.614  -10.014 1.00 15.46 ? 14   ARG B N   1 
ATOM   3312 C  CA  . ARG B  1 14  ? -73.374 15.638  -8.703  1.00 15.19 ? 14   ARG B CA  1 
ATOM   3313 C  C   . ARG B  1 14  ? -73.051 16.964  -8.027  1.00 15.26 ? 14   ARG B C   1 
ATOM   3314 O  O   . ARG B  1 14  ? -72.191 17.703  -8.543  1.00 15.74 ? 14   ARG B O   1 
ATOM   3315 C  CB  . ARG B  1 14  ? -72.915 14.461  -7.826  1.00 15.07 ? 14   ARG B CB  1 
ATOM   3316 C  CG  . ARG B  1 14  ? -71.410 14.398  -7.604  1.00 14.51 ? 14   ARG B CG  1 
ATOM   3317 C  CD  . ARG B  1 14  ? -70.989 13.267  -6.719  1.00 15.82 ? 14   ARG B CD  1 
ATOM   3318 N  NE  . ARG B  1 14  ? -69.540 13.302  -6.605  1.00 14.82 ? 14   ARG B NE  1 
ATOM   3319 C  CZ  . ARG B  1 14  ? -68.824 12.680  -5.677  1.00 15.93 ? 14   ARG B CZ  1 
ATOM   3320 N  NH1 . ARG B  1 14  ? -69.404 11.876  -4.814  1.00 17.47 ? 14   ARG B NH1 1 
ATOM   3321 N  NH2 . ARG B  1 14  ? -67.509 12.812  -5.669  1.00 15.70 ? 14   ARG B NH2 1 
ATOM   3322 N  N   . GLY B  1 15  ? -73.666 17.216  -6.878  1.00 15.64 ? 15   GLY B N   1 
ATOM   3323 C  CA  . GLY B  1 15  ? -73.366 18.369  -6.023  1.00 15.50 ? 15   GLY B CA  1 
ATOM   3324 C  C   . GLY B  1 15  ? -71.930 18.334  -5.548  1.00 15.19 ? 15   GLY B C   1 
ATOM   3325 O  O   . GLY B  1 15  ? -71.370 17.225  -5.367  1.00 17.76 ? 15   GLY B O   1 
ATOM   3326 N  N   . VAL B  1 16  ? -71.311 19.491  -5.370  1.00 13.78 ? 16   VAL B N   1 
ATOM   3327 C  CA  . VAL B  1 16  ? -69.964 19.572  -4.737  1.00 14.01 ? 16   VAL B CA  1 
ATOM   3328 C  C   . VAL B  1 16  ? -69.983 18.836  -3.395  1.00 14.26 ? 16   VAL B C   1 
ATOM   3329 O  O   . VAL B  1 16  ? -70.869 19.131  -2.625  1.00 14.39 ? 16   VAL B O   1 
ATOM   3330 C  CB  . VAL B  1 16  ? -69.572 21.051  -4.575  1.00 14.95 ? 16   VAL B CB  1 
ATOM   3331 C  CG1 . VAL B  1 16  ? -68.360 21.238  -3.674  1.00 16.98 ? 16   VAL B CG1 1 
ATOM   3332 C  CG2 . VAL B  1 16  ? -69.368 21.682  -5.956  1.00 15.26 ? 16   VAL B CG2 1 
ATOM   3333 N  N   . THR B  1 17  ? -69.009 17.953  -3.115  1.00 13.49 ? 17   THR B N   1 
ATOM   3334 C  CA  . THR B  1 17  ? -68.800 17.310  -1.803  1.00 14.06 ? 17   THR B CA  1 
ATOM   3335 C  C   . THR B  1 17  ? -67.354 17.430  -1.325  1.00 13.43 ? 17   THR B C   1 
ATOM   3336 O  O   . THR B  1 17  ? -67.066 16.942  -0.213  1.00 13.93 ? 17   THR B O   1 
ATOM   3337 C  CB  . THR B  1 17  ? -69.176 15.824  -1.876  1.00 16.37 ? 17   THR B CB  1 
ATOM   3338 O  OG1 . THR B  1 17  ? -68.283 15.160  -2.761  1.00 16.13 ? 17   THR B OG1 1 
ATOM   3339 C  CG2 . THR B  1 17  ? -70.607 15.607  -2.348  1.00 18.35 ? 17   THR B CG2 1 
ATOM   3340 N  N   . HIS B  1 18  ? -66.485 18.054  -2.105  1.00 12.16 ? 18   HIS B N   1 
ATOM   3341 C  CA  . HIS B  1 18  ? -65.018 18.130  -1.837  1.00 12.71 ? 18   HIS B CA  1 
ATOM   3342 C  C   . HIS B  1 18  ? -64.500 16.723  -1.485  1.00 12.24 ? 18   HIS B C   1 
ATOM   3343 O  O   . HIS B  1 18  ? -63.832 16.547  -0.424  1.00 11.04 ? 18   HIS B O   1 
ATOM   3344 C  CB  . HIS B  1 18  ? -64.721 19.151  -0.734  1.00 13.78 ? 18   HIS B CB  1 
ATOM   3345 C  CG  . HIS B  1 18  ? -65.339 20.491  -0.997  1.00 16.09 ? 18   HIS B CG  1 
ATOM   3346 N  ND1 . HIS B  1 18  ? -66.237 21.072  -0.131  1.00 20.21 ? 18   HIS B ND1 1 
ATOM   3347 C  CD2 . HIS B  1 18  ? -65.316 21.289  -2.078  1.00 17.54 ? 18   HIS B CD2 1 
ATOM   3348 C  CE1 . HIS B  1 18  ? -66.634 22.241  -0.639  1.00 21.03 ? 18   HIS B CE1 1 
ATOM   3349 N  NE2 . HIS B  1 18  ? -66.113 22.374  -1.812  1.00 16.83 ? 18   HIS B NE2 1 
ATOM   3350 N  N   . CYS B  1 19  ? -64.881 15.717  -2.273  1.00 13.01 ? 19   CYS B N   1 
ATOM   3351 C  CA  . CYS B  1 19  ? -64.811 14.294  -1.831  1.00 12.89 ? 19   CYS B CA  1 
ATOM   3352 C  C   . CYS B  1 19  ? -63.393 13.887  -1.427  1.00 13.21 ? 19   CYS B C   1 
ATOM   3353 O  O   . CYS B  1 19  ? -63.266 13.023  -0.535  1.00 12.71 ? 19   CYS B O   1 
ATOM   3354 C  CB  . CYS B  1 19  ? -65.318 13.337  -2.894  1.00 13.57 ? 19   CYS B CB  1 
ATOM   3355 S  SG  . CYS B  1 19  ? -64.283 13.188  -4.375  1.00 14.92 ? 19   CYS B SG  1 
ATOM   3356 N  N   . ALA B  1 20  ? -62.374 14.504  -2.023  1.00 12.33 ? 20   ALA B N   1 
ATOM   3357 C  CA  . ALA B  1 20  ? -60.945 14.151  -1.841  1.00 12.42 ? 20   ALA B CA  1 
ATOM   3358 C  C   . ALA B  1 20  ? -60.204 15.119  -0.890  1.00 12.61 ? 20   ALA B C   1 
ATOM   3359 O  O   . ALA B  1 20  ? -58.929 15.028  -0.757  1.00 12.03 ? 20   ALA B O   1 
ATOM   3360 C  CB  . ALA B  1 20  ? -60.302 14.112  -3.198  1.00 12.18 ? 20   ALA B CB  1 
ATOM   3361 N  N   . SER B  1 21  ? -60.921 15.974  -0.178  1.00 11.99 ? 21   SER B N   1 
ATOM   3362 C  CA  . SER B  1 21  ? -60.319 16.909  0.801   1.00 12.41 ? 21   SER B CA  1 
ATOM   3363 C  C   . SER B  1 21  ? -60.358 16.300  2.199   1.00 12.75 ? 21   SER B C   1 
ATOM   3364 O  O   . SER B  1 21  ? -61.363 16.422  2.912   1.00 13.70 ? 21   SER B O   1 
ATOM   3365 C  CB  . SER B  1 21  ? -61.026 18.254  0.766   1.00 12.35 ? 21   SER B CB  1 
ATOM   3366 O  OG  . SER B  1 21  ? -60.317 19.137  1.598   1.00 12.35 ? 21   SER B OG  1 
ATOM   3367 N  N   . GLY B  1 22  ? -59.270 15.661  2.595   1.00 12.62 ? 22   GLY B N   1 
ATOM   3368 C  CA  . GLY B  1 22  ? -59.154 14.977  3.885   1.00 11.83 ? 22   GLY B CA  1 
ATOM   3369 C  C   . GLY B  1 22  ? -57.860 14.195  3.908   1.00 11.87 ? 22   GLY B C   1 
ATOM   3370 O  O   . GLY B  1 22  ? -57.182 14.176  2.897   1.00 11.80 ? 22   GLY B O   1 
ATOM   3371 N  N   . SER B  1 23  ? -57.536 13.612  5.046   1.00 11.38 ? 23   SER B N   1 
ATOM   3372 C  CA  . SER B  1 23  ? -56.197 13.079  5.291   1.00 12.35 ? 23   SER B CA  1 
ATOM   3373 C  C   . SER B  1 23  ? -56.221 12.082  6.432   1.00 12.79 ? 23   SER B C   1 
ATOM   3374 O  O   . SER B  1 23  ? -57.092 12.140  7.313   1.00 12.44 ? 23   SER B O   1 
ATOM   3375 C  CB  . SER B  1 23  ? -55.219 14.206  5.542   1.00 12.81 ? 23   SER B CB  1 
ATOM   3376 O  OG  . SER B  1 23  ? -55.775 15.188  6.410   1.00 13.45 ? 23   SER B OG  1 
ATOM   3377 N  N   . LEU B  1 24  ? -55.269 11.164  6.354   1.00 12.47 ? 24   LEU B N   1 
ATOM   3378 C  CA  . LEU B  1 24  ? -54.944 10.197  7.411   1.00 12.70 ? 24   LEU B CA  1 
ATOM   3379 C  C   . LEU B  1 24  ? -54.084 10.894  8.467   1.00 12.90 ? 24   LEU B C   1 
ATOM   3380 O  O   . LEU B  1 24  ? -53.027 11.451  8.117   1.00 11.97 ? 24   LEU B O   1 
ATOM   3381 C  CB  . LEU B  1 24  ? -54.239 9.004   6.777   1.00 12.53 ? 24   LEU B CB  1 
ATOM   3382 C  CG  . LEU B  1 24  ? -53.691 7.996   7.775   1.00 13.36 ? 24   LEU B CG  1 
ATOM   3383 C  CD1 . LEU B  1 24  ? -54.799 7.323   8.571   1.00 13.54 ? 24   LEU B CD1 1 
ATOM   3384 C  CD2 . LEU B  1 24  ? -52.838 6.967   7.088   1.00 13.98 ? 24   LEU B CD2 1 
ATOM   3385 N  N   . TYR B  1 25  ? -54.558 10.910  9.711   1.00 12.65 ? 25   TYR B N   1 
ATOM   3386 C  CA  . TYR B  1 25  ? -53.903 11.627  10.838  1.00 13.30 ? 25   TYR B CA  1 
ATOM   3387 C  C   . TYR B  1 25  ? -53.599 13.091  10.455  1.00 14.72 ? 25   TYR B C   1 
ATOM   3388 O  O   . TYR B  1 25  ? -52.600 13.652  10.938  1.00 16.64 ? 25   TYR B O   1 
ATOM   3389 C  CB  . TYR B  1 25  ? -52.606 10.900  11.221  1.00 13.70 ? 25   TYR B CB  1 
ATOM   3390 C  CG  . TYR B  1 25  ? -52.730 9.635   12.041  1.00 12.92 ? 25   TYR B CG  1 
ATOM   3391 C  CD1 . TYR B  1 25  ? -53.000 8.394   11.467  1.00 12.99 ? 25   TYR B CD1 1 
ATOM   3392 C  CD2 . TYR B  1 25  ? -52.424 9.643   13.388  1.00 14.01 ? 25   TYR B CD2 1 
ATOM   3393 C  CE1 . TYR B  1 25  ? -53.026 7.229   12.220  1.00 12.81 ? 25   TYR B CE1 1 
ATOM   3394 C  CE2 . TYR B  1 25  ? -52.405 8.487   14.147  1.00 13.18 ? 25   TYR B CE2 1 
ATOM   3395 C  CZ  . TYR B  1 25  ? -52.702 7.270   13.564  1.00 12.86 ? 25   TYR B CZ  1 
ATOM   3396 O  OH  . TYR B  1 25  ? -52.674 6.127   14.313  1.00 12.88 ? 25   TYR B OH  1 
ATOM   3397 N  N   . GLY B  1 26  ? -54.395 13.694  9.586   1.00 13.90 ? 26   GLY B N   1 
ATOM   3398 C  CA  . GLY B  1 26  ? -54.180 15.063  9.114   1.00 13.58 ? 26   GLY B CA  1 
ATOM   3399 C  C   . GLY B  1 26  ? -54.660 16.076  10.145  1.00 13.81 ? 26   GLY B C   1 
ATOM   3400 O  O   . GLY B  1 26  ? -54.198 17.228  10.104  1.00 14.73 ? 26   GLY B O   1 
ATOM   3401 N  N   . VAL B  1 27  ? -55.547 15.657  11.040  1.00 14.45 ? 27   VAL B N   1 
ATOM   3402 C  CA  . VAL B  1 27  ? -56.009 16.454  12.215  1.00 15.22 ? 27   VAL B CA  1 
ATOM   3403 C  C   . VAL B  1 27  ? -55.889 15.562  13.433  1.00 16.31 ? 27   VAL B C   1 
ATOM   3404 O  O   . VAL B  1 27  ? -56.224 14.373  13.336  1.00 16.83 ? 27   VAL B O   1 
ATOM   3405 C  CB  . VAL B  1 27  ? -57.446 16.991  12.049  1.00 15.58 ? 27   VAL B CB  1 
ATOM   3406 C  CG1 . VAL B  1 27  ? -57.883 17.829  13.244  1.00 17.34 ? 27   VAL B CG1 1 
ATOM   3407 C  CG2 . VAL B  1 27  ? -57.578 17.799  10.781  1.00 16.81 ? 27   VAL B CG2 1 
ATOM   3408 N  N   . THR B  1 28  ? -55.396 16.100  14.549  1.00 14.94 ? 28   THR B N   1 
ATOM   3409 C  CA  . THR B  1 28  ? -55.296 15.341  15.811  1.00 15.74 ? 28   THR B CA  1 
ATOM   3410 C  C   . THR B  1 28  ? -55.969 16.145  16.927  1.00 16.19 ? 28   THR B C   1 
ATOM   3411 O  O   . THR B  1 28  ? -56.626 17.141  16.631  1.00 16.48 ? 28   THR B O   1 
ATOM   3412 C  CB  . THR B  1 28  ? -53.820 15.084  16.137  1.00 16.60 ? 28   THR B CB  1 
ATOM   3413 O  OG1 . THR B  1 28  ? -53.233 16.352  16.485  1.00 17.68 ? 28   THR B OG1 1 
ATOM   3414 C  CG2 . THR B  1 28  ? -53.093 14.424  14.985  1.00 16.90 ? 28   THR B CG2 1 
ATOM   3415 N  N   . GLU B  1 29  ? -55.818 15.680  18.156  1.00 20.00 ? 29   GLU B N   1 
ATOM   3416 C  CA  . GLU B  1 29  ? -56.322 16.394  19.353  1.00 21.76 ? 29   GLU B CA  1 
ATOM   3417 C  C   . GLU B  1 29  ? -55.745 17.820  19.365  1.00 22.90 ? 29   GLU B C   1 
ATOM   3418 O  O   . GLU B  1 29  ? -56.438 18.702  19.832  1.00 24.81 ? 29   GLU B O   1 
ATOM   3419 C  CB  . GLU B  1 29  ? -55.974 15.622  20.630  1.00 22.68 ? 29   GLU B CB  1 
ATOM   3420 C  CG  . GLU B  1 29  ? -56.452 14.184  20.652  1.00 22.62 ? 29   GLU B CG  1 
ATOM   3421 C  CD  . GLU B  1 29  ? -55.413 13.170  20.177  1.00 23.34 ? 29   GLU B CD  1 
ATOM   3422 O  OE1 . GLU B  1 29  ? -54.492 13.587  19.407  1.00 20.84 ? 29   GLU B OE1 1 
ATOM   3423 O  OE2 . GLU B  1 29  ? -55.478 11.980  20.622  1.00 21.35 ? 29   GLU B OE2 1 
ATOM   3424 N  N   . SER B  1 30  ? -54.520 18.071  18.901  1.00 21.21 ? 30   SER B N   1 
ATOM   3425 C  CA  . SER B  1 30  ? -53.827 19.367  19.158  1.00 23.37 ? 30   SER B CA  1 
ATOM   3426 C  C   . SER B  1 30  ? -53.361 20.028  17.862  1.00 20.71 ? 30   SER B C   1 
ATOM   3427 O  O   . SER B  1 30  ? -53.014 21.210  17.899  1.00 19.20 ? 30   SER B O   1 
ATOM   3428 C  CB  . SER B  1 30  ? -52.685 19.173  20.117  1.00 24.69 ? 30   SER B CB  1 
ATOM   3429 O  OG  . SER B  1 30  ? -51.869 18.121  19.649  1.00 28.86 ? 30   SER B OG  1 
ATOM   3430 N  N   . LYS B  1 31  ? -53.371 19.329  16.725  1.00 20.08 ? 31   LYS B N   1 
ATOM   3431 C  CA  . LYS B  1 31  ? -52.832 19.886  15.459  1.00 19.26 ? 31   LYS B CA  1 
ATOM   3432 C  C   . LYS B  1 31  ? -53.792 19.685  14.297  1.00 20.25 ? 31   LYS B C   1 
ATOM   3433 O  O   . LYS B  1 31  ? -54.468 18.665  14.235  1.00 18.08 ? 31   LYS B O   1 
ATOM   3434 C  CB  . LYS B  1 31  ? -51.506 19.200  15.142  1.00 21.17 ? 31   LYS B CB  1 
ATOM   3435 C  CG  . LYS B  1 31  ? -50.390 19.483  16.133  1.00 22.90 ? 31   LYS B CG  1 
ATOM   3436 C  CD  . LYS B  1 31  ? -49.216 18.541  15.975  1.00 23.92 ? 31   LYS B CD  1 
ATOM   3437 C  CE  . LYS B  1 31  ? -48.046 18.930  16.841  1.00 24.17 ? 31   LYS B CE  1 
ATOM   3438 N  NZ  . LYS B  1 31  ? -46.888 18.061  16.551  1.00 25.69 ? 31   LYS B NZ  1 
ATOM   3439 N  N   . PRO B  1 32  ? -53.944 20.657  13.377  1.00 17.74 ? 32   PRO B N   1 
ATOM   3440 C  CA  . PRO B  1 32  ? -53.455 22.026  13.564  1.00 19.48 ? 32   PRO B CA  1 
ATOM   3441 C  C   . PRO B  1 32  ? -54.007 22.664  14.848  1.00 22.48 ? 32   PRO B C   1 
ATOM   3442 O  O   . PRO B  1 32  ? -55.096 22.295  15.312  1.00 20.41 ? 32   PRO B O   1 
ATOM   3443 C  CB  . PRO B  1 32  ? -53.986 22.762  12.329  1.00 18.35 ? 32   PRO B CB  1 
ATOM   3444 C  CG  . PRO B  1 32  ? -54.158 21.662  11.285  1.00 19.12 ? 32   PRO B CG  1 
ATOM   3445 C  CD  . PRO B  1 32  ? -54.619 20.476  12.088  1.00 19.00 ? 32   PRO B CD  1 
ATOM   3446 N  N   . PHE B  1 33  ? -53.235 23.600  15.424  1.00 22.88 ? 33   PHE B N   1 
ATOM   3447 C  CA  . PHE B  1 33  ? -53.623 24.317  16.658  1.00 23.64 ? 33   PHE B CA  1 
ATOM   3448 C  C   . PHE B  1 33  ? -54.905 25.107  16.396  1.00 23.80 ? 33   PHE B C   1 
ATOM   3449 O  O   . PHE B  1 33  ? -55.716 25.196  17.307  1.00 23.75 ? 33   PHE B O   1 
ATOM   3450 C  CB  . PHE B  1 33  ? -52.480 25.207  17.145  1.00 27.56 ? 33   PHE B CB  1 
ATOM   3451 C  CG  . PHE B  1 33  ? -52.282 26.511  16.413  1.00 33.63 ? 33   PHE B CG  1 
ATOM   3452 C  CD1 . PHE B  1 33  ? -51.528 26.572  15.249  1.00 37.25 ? 33   PHE B CD1 1 
ATOM   3453 C  CD2 . PHE B  1 33  ? -52.810 27.699  16.911  1.00 37.01 ? 33   PHE B CD2 1 
ATOM   3454 C  CE1 . PHE B  1 33  ? -51.297 27.786  14.610  1.00 37.87 ? 33   PHE B CE1 1 
ATOM   3455 C  CE2 . PHE B  1 33  ? -52.596 28.908  16.255  1.00 39.75 ? 33   PHE B CE2 1 
ATOM   3456 C  CZ  . PHE B  1 33  ? -51.839 28.948  15.103  1.00 36.65 ? 33   PHE B CZ  1 
ATOM   3457 N  N   . ASP B  1 34  ? -55.070 25.664  15.199  1.00 21.23 ? 34   ASP B N   1 
ATOM   3458 C  CA  . ASP B  1 34  ? -56.176 26.597  14.895  1.00 22.95 ? 34   ASP B CA  1 
ATOM   3459 C  C   . ASP B  1 34  ? -57.080 25.987  13.816  1.00 20.90 ? 34   ASP B C   1 
ATOM   3460 O  O   . ASP B  1 34  ? -56.748 26.090  12.626  1.00 20.88 ? 34   ASP B O   1 
ATOM   3461 C  CB  . ASP B  1 34  ? -55.624 27.952  14.493  1.00 24.13 ? 34   ASP B CB  1 
ATOM   3462 C  CG  . ASP B  1 34  ? -56.688 29.028  14.366  1.00 25.37 ? 34   ASP B CG  1 
ATOM   3463 O  OD1 . ASP B  1 34  ? -57.888 28.690  14.246  1.00 24.97 ? 34   ASP B OD1 1 
ATOM   3464 O  OD2 . ASP B  1 34  ? -56.292 30.198  14.374  1.00 28.97 ? 34   ASP B OD2 1 
ATOM   3465 N  N   . ILE B  1 35  ? -58.194 25.379  14.247  1.00 20.81 ? 35   ILE B N   1 
ATOM   3466 C  CA  . ILE B  1 35  ? -59.165 24.689  13.343  1.00 19.81 ? 35   ILE B CA  1 
ATOM   3467 C  C   . ILE B  1 35  ? -59.790 25.714  12.400  1.00 21.07 ? 35   ILE B C   1 
ATOM   3468 O  O   . ILE B  1 35  ? -59.844 25.486  11.186  1.00 18.46 ? 35   ILE B O   1 
ATOM   3469 C  CB  . ILE B  1 35  ? -60.246 23.942  14.147  1.00 19.75 ? 35   ILE B CB  1 
ATOM   3470 C  CG1 . ILE B  1 35  ? -59.641 22.792  14.944  1.00 20.33 ? 35   ILE B CG1 1 
ATOM   3471 C  CG2 . ILE B  1 35  ? -61.379 23.480  13.238  1.00 18.68 ? 35   ILE B CG2 1 
ATOM   3472 C  CD1 . ILE B  1 35  ? -59.022 21.702  14.082  1.00 21.12 ? 35   ILE B CD1 1 
ATOM   3473 N  N   . ASN B  1 36  ? -60.248 26.842  12.933  1.00 23.36 ? 36   ASN B N   1 
ATOM   3474 C  CA  . ASN B  1 36  ? -60.889 27.899  12.115  1.00 25.20 ? 36   ASN B CA  1 
ATOM   3475 C  C   . ASN B  1 36  ? -59.935 28.443  11.055  1.00 21.22 ? 36   ASN B C   1 
ATOM   3476 O  O   . ASN B  1 36  ? -60.418 28.767  9.974   1.00 21.45 ? 36   ASN B O   1 
ATOM   3477 C  CB  . ASN B  1 36  ? -61.447 29.030  12.987  1.00 30.64 ? 36   ASN B CB  1 
ATOM   3478 C  CG  . ASN B  1 36  ? -62.822 28.695  13.526  1.00 38.67 ? 36   ASN B CG  1 
ATOM   3479 O  OD1 . ASN B  1 36  ? -63.540 27.875  12.941  1.00 47.45 ? 36   ASN B OD1 1 
ATOM   3480 N  ND2 . ASN B  1 36  ? -63.193 29.314  14.641  1.00 42.62 ? 36   ASN B ND2 1 
ATOM   3481 N  N   . GLN B  1 37  ? -58.655 28.609  11.361  1.00 20.73 ? 37   GLN B N   1 
ATOM   3482 C  CA  . GLN B  1 37  ? -57.694 29.209  10.413  1.00 21.04 ? 37   GLN B CA  1 
ATOM   3483 C  C   . GLN B  1 37  ? -57.297 28.190  9.326   1.00 19.53 ? 37   GLN B C   1 
ATOM   3484 O  O   . GLN B  1 37  ? -57.264 28.562  8.145   1.00 20.00 ? 37   GLN B O   1 
ATOM   3485 C  CB  . GLN B  1 37  ? -56.483 29.731  11.173  1.00 23.43 ? 37   GLN B CB  1 
ATOM   3486 C  CG  . GLN B  1 37  ? -55.511 30.470  10.276  1.00 25.72 ? 37   GLN B CG  1 
ATOM   3487 C  CD  . GLN B  1 37  ? -54.355 31.058  11.046  1.00 27.75 ? 37   GLN B CD  1 
ATOM   3488 O  OE1 . GLN B  1 37  ? -54.308 31.014  12.279  1.00 29.97 ? 37   GLN B OE1 1 
ATOM   3489 N  NE2 . GLN B  1 37  ? -53.390 31.557  10.298  1.00 26.43 ? 37   GLN B NE2 1 
ATOM   3490 N  N   . PHE B  1 38  ? -57.010 26.943  9.698   1.00 19.48 ? 38   PHE B N   1 
ATOM   3491 C  CA  . PHE B  1 38  ? -56.290 25.995  8.811   1.00 18.35 ? 38   PHE B CA  1 
ATOM   3492 C  C   . PHE B  1 38  ? -57.188 24.870  8.309   1.00 17.78 ? 38   PHE B C   1 
ATOM   3493 O  O   . PHE B  1 38  ? -56.918 24.406  7.205   1.00 15.99 ? 38   PHE B O   1 
ATOM   3494 C  CB  . PHE B  1 38  ? -55.062 25.408  9.499   1.00 19.11 ? 38   PHE B CB  1 
ATOM   3495 C  CG  . PHE B  1 38  ? -54.024 26.451  9.826   1.00 18.65 ? 38   PHE B CG  1 
ATOM   3496 C  CD1 . PHE B  1 38  ? -53.357 27.117  8.820   1.00 20.09 ? 38   PHE B CD1 1 
ATOM   3497 C  CD2 . PHE B  1 38  ? -53.769 26.778  11.140  1.00 20.91 ? 38   PHE B CD2 1 
ATOM   3498 C  CE1 . PHE B  1 38  ? -52.389 28.056  9.131   1.00 22.07 ? 38   PHE B CE1 1 
ATOM   3499 C  CE2 . PHE B  1 38  ? -52.799 27.716  11.447  1.00 21.13 ? 38   PHE B CE2 1 
ATOM   3500 C  CZ  . PHE B  1 38  ? -52.120 28.350  10.444  1.00 20.53 ? 38   PHE B CZ  1 
ATOM   3501 N  N   . VAL B  1 39  ? -58.266 24.534  9.005   1.00 17.83 ? 39   VAL B N   1 
ATOM   3502 C  CA  . VAL B  1 39  ? -59.111 23.363  8.624   1.00 17.59 ? 39   VAL B CA  1 
ATOM   3503 C  C   . VAL B  1 39  ? -60.437 23.834  8.014   1.00 16.61 ? 39   VAL B C   1 
ATOM   3504 O  O   . VAL B  1 39  ? -60.767 23.413  6.891   1.00 14.84 ? 39   VAL B O   1 
ATOM   3505 C  CB  . VAL B  1 39  ? -59.340 22.462  9.838   1.00 17.40 ? 39   VAL B CB  1 
ATOM   3506 C  CG1 . VAL B  1 39  ? -60.155 21.230  9.453   1.00 17.55 ? 39   VAL B CG1 1 
ATOM   3507 C  CG2 . VAL B  1 39  ? -57.996 22.084  10.449  1.00 17.34 ? 39   VAL B CG2 1 
ATOM   3508 N  N   . ALA B  1 40  ? -61.184 24.665  8.731   1.00 16.41 ? 40   ALA B N   1 
ATOM   3509 C  CA  . ALA B  1 40  ? -62.559 25.059  8.343   1.00 17.07 ? 40   ALA B CA  1 
ATOM   3510 C  C   . ALA B  1 40  ? -62.600 25.580  6.909   1.00 17.46 ? 40   ALA B C   1 
ATOM   3511 O  O   . ALA B  1 40  ? -63.491 25.204  6.144   1.00 16.64 ? 40   ALA B O   1 
ATOM   3512 C  CB  . ALA B  1 40  ? -63.131 26.048  9.341   1.00 19.03 ? 40   ALA B CB  1 
ATOM   3513 N  N   . PRO B  1 41  ? -61.684 26.487  6.484   1.00 16.44 ? 41   PRO B N   1 
ATOM   3514 C  CA  . PRO B  1 41  ? -61.733 27.042  5.125   1.00 16.47 ? 41   PRO B CA  1 
ATOM   3515 C  C   . PRO B  1 41  ? -61.601 26.034  3.969   1.00 16.47 ? 41   PRO B C   1 
ATOM   3516 O  O   . PRO B  1 41  ? -61.970 26.323  2.831   1.00 16.21 ? 41   PRO B O   1 
ATOM   3517 C  CB  . PRO B  1 41  ? -60.516 27.988  5.109   1.00 17.49 ? 41   PRO B CB  1 
ATOM   3518 C  CG  . PRO B  1 41  ? -60.287 28.352  6.541   1.00 18.05 ? 41   PRO B CG  1 
ATOM   3519 C  CD  . PRO B  1 41  ? -60.595 27.074  7.292   1.00 18.74 ? 41   PRO B CD  1 
ATOM   3520 N  N   . LEU B  1 42  ? -61.048 24.859  4.252   1.00 16.71 ? 42   LEU B N   1 
ATOM   3521 C  CA  . LEU B  1 42  ? -60.891 23.799  3.232   1.00 15.71 ? 42   LEU B CA  1 
ATOM   3522 C  C   . LEU B  1 42  ? -62.242 23.118  2.996   1.00 14.94 ? 42   LEU B C   1 
ATOM   3523 O  O   . LEU B  1 42  ? -62.372 22.444  1.992   1.00 15.71 ? 42   LEU B O   1 
ATOM   3524 C  CB  . LEU B  1 42  ? -59.846 22.777  3.708   1.00 15.37 ? 42   LEU B CB  1 
ATOM   3525 C  CG  . LEU B  1 42  ? -58.435 23.317  3.960   1.00 15.42 ? 42   LEU B CG  1 
ATOM   3526 C  CD1 . LEU B  1 42  ? -57.493 22.173  4.269   1.00 16.29 ? 42   LEU B CD1 1 
ATOM   3527 C  CD2 . LEU B  1 42  ? -57.911 24.144  2.795   1.00 16.41 ? 42   LEU B CD2 1 
ATOM   3528 N  N   . LYS B  1 43  ? -63.211 23.283  3.877   1.00 16.27 ? 43   LYS B N   1 
ATOM   3529 C  CA  . LYS B  1 43  ? -64.536 22.615  3.710   1.00 15.94 ? 43   LYS B CA  1 
ATOM   3530 C  C   . LYS B  1 43  ? -64.295 21.118  3.476   1.00 15.62 ? 43   LYS B C   1 
ATOM   3531 O  O   . LYS B  1 43  ? -64.783 20.521  2.496   1.00 13.77 ? 43   LYS B O   1 
ATOM   3532 C  CB  . LYS B  1 43  ? -65.347 23.247  2.577   1.00 19.23 ? 43   LYS B CB  1 
ATOM   3533 C  CG  . LYS B  1 43  ? -65.661 24.741  2.750   1.00 21.88 ? 43   LYS B CG  1 
ATOM   3534 C  CD  . LYS B  1 43  ? -66.315 25.056  4.078   1.00 25.66 ? 43   LYS B CD  1 
ATOM   3535 C  CE  . LYS B  1 43  ? -66.608 26.529  4.269   1.00 29.36 ? 43   LYS B CE  1 
ATOM   3536 N  NZ  . LYS B  1 43  ? -67.220 27.105  3.052   1.00 32.35 ? 43   LYS B NZ  1 
ATOM   3537 N  N   . PRO B  1 44  ? -63.536 20.477  4.391   1.00 13.91 ? 44   PRO B N   1 
ATOM   3538 C  CA  . PRO B  1 44  ? -63.104 19.096  4.199   1.00 13.71 ? 44   PRO B CA  1 
ATOM   3539 C  C   . PRO B  1 44  ? -64.267 18.099  4.274   1.00 13.15 ? 44   PRO B C   1 
ATOM   3540 O  O   . PRO B  1 44  ? -65.367 18.393  4.784   1.00 13.26 ? 44   PRO B O   1 
ATOM   3541 C  CB  . PRO B  1 44  ? -62.139 18.821  5.350   1.00 13.79 ? 44   PRO B CB  1 
ATOM   3542 C  CG  . PRO B  1 44  ? -62.639 19.767  6.435   1.00 14.61 ? 44   PRO B CG  1 
ATOM   3543 C  CD  . PRO B  1 44  ? -63.040 21.018  5.665   1.00 14.96 ? 44   PRO B CD  1 
ATOM   3544 N  N   . ASN B  1 45  ? -64.007 16.939  3.686   1.00 12.53 ? 45   ASN B N   1 
ATOM   3545 C  CA  . ASN B  1 45  ? -64.976 15.835  3.578   1.00 12.84 ? 45   ASN B CA  1 
ATOM   3546 C  C   . ASN B  1 45  ? -64.674 14.867  4.709   1.00 13.32 ? 45   ASN B C   1 
ATOM   3547 O  O   . ASN B  1 45  ? -65.276 15.008  5.780   1.00 14.98 ? 45   ASN B O   1 
ATOM   3548 C  CB  . ASN B  1 45  ? -64.953 15.212  2.178   1.00 13.80 ? 45   ASN B CB  1 
ATOM   3549 C  CG  . ASN B  1 45  ? -65.954 14.087  2.055   1.00 15.17 ? 45   ASN B CG  1 
ATOM   3550 O  OD1 . ASN B  1 45  ? -67.058 14.181  2.623   1.00 15.38 ? 45   ASN B OD1 1 
ATOM   3551 N  ND2 . ASN B  1 45  ? -65.597 13.071  1.265   1.00 14.95 ? 45   ASN B ND2 1 
ATOM   3552 N  N   . VAL B  1 46  ? -63.778 13.905  4.493   1.00 12.38 ? 46   VAL B N   1 
ATOM   3553 C  CA  . VAL B  1 46  ? -63.525 12.829  5.488   1.00 11.84 ? 46   VAL B CA  1 
ATOM   3554 C  C   . VAL B  1 46  ? -62.049 12.768  5.880   1.00 12.38 ? 46   VAL B C   1 
ATOM   3555 O  O   . VAL B  1 46  ? -61.176 12.784  4.984   1.00 12.33 ? 46   VAL B O   1 
ATOM   3556 C  CB  . VAL B  1 46  ? -63.989 11.473  4.906   1.00 12.76 ? 46   VAL B CB  1 
ATOM   3557 C  CG1 . VAL B  1 46  ? -63.597 10.309  5.779   1.00 12.70 ? 46   VAL B CG1 1 
ATOM   3558 C  CG2 . VAL B  1 46  ? -65.492 11.511  4.715   1.00 12.26 ? 46   VAL B CG2 1 
ATOM   3559 N  N   . PHE B  1 47  ? -61.811 12.678  7.187   1.00 11.51 ? 47   PHE B N   1 
ATOM   3560 C  CA  . PHE B  1 47  ? -60.498 12.367  7.788   1.00 12.12 ? 47   PHE B CA  1 
ATOM   3561 C  C   . PHE B  1 47  ? -60.505 10.945  8.319   1.00 12.24 ? 47   PHE B C   1 
ATOM   3562 O  O   . PHE B  1 47  ? -61.547 10.491  8.762   1.00 13.69 ? 47   PHE B O   1 
ATOM   3563 C  CB  . PHE B  1 47  ? -60.243 13.346  8.935   1.00 11.99 ? 47   PHE B CB  1 
ATOM   3564 C  CG  . PHE B  1 47  ? -60.111 14.766  8.473   1.00 13.00 ? 47   PHE B CG  1 
ATOM   3565 C  CD1 . PHE B  1 47  ? -58.904 15.240  7.977   1.00 12.89 ? 47   PHE B CD1 1 
ATOM   3566 C  CD2 . PHE B  1 47  ? -61.189 15.632  8.535   1.00 14.20 ? 47   PHE B CD2 1 
ATOM   3567 C  CE1 . PHE B  1 47  ? -58.800 16.540  7.523   1.00 14.36 ? 47   PHE B CE1 1 
ATOM   3568 C  CE2 . PHE B  1 47  ? -61.066 16.940  8.101   1.00 14.20 ? 47   PHE B CE2 1 
ATOM   3569 C  CZ  . PHE B  1 47  ? -59.857 17.401  7.632   1.00 13.77 ? 47   PHE B CZ  1 
ATOM   3570 N  N   . THR B  1 48  ? -59.379 10.250  8.237   1.00 12.53 ? 48   THR B N   1 
ATOM   3571 C  CA  . THR B  1 48  ? -59.198 8.922   8.831   1.00 12.50 ? 48   THR B CA  1 
ATOM   3572 C  C   . THR B  1 48  ? -58.301 9.075   10.061  1.00 13.28 ? 48   THR B C   1 
ATOM   3573 O  O   . THR B  1 48  ? -57.173 9.649   9.952   1.00 13.06 ? 48   THR B O   1 
ATOM   3574 C  CB  . THR B  1 48  ? -58.675 7.907   7.806   1.00 12.94 ? 48   THR B CB  1 
ATOM   3575 O  OG1 . THR B  1 48  ? -59.563 7.837   6.684   1.00 11.69 ? 48   THR B OG1 1 
ATOM   3576 C  CG2 . THR B  1 48  ? -58.545 6.532   8.416   1.00 12.06 ? 48   THR B CG2 1 
ATOM   3577 N  N   . ASN B  1 49  ? -58.779 8.569   11.193  1.00 13.24 ? 49   ASN B N   1 
ATOM   3578 C  CA  . ASN B  1 49  ? -58.114 8.735   12.506  1.00 12.94 ? 49   ASN B CA  1 
ATOM   3579 C  C   . ASN B  1 49  ? -58.171 7.406   13.240  1.00 13.10 ? 49   ASN B C   1 
ATOM   3580 O  O   . ASN B  1 49  ? -59.191 6.729   13.186  1.00 12.87 ? 49   ASN B O   1 
ATOM   3581 C  CB  . ASN B  1 49  ? -58.761 9.852   13.318  1.00 12.49 ? 49   ASN B CB  1 
ATOM   3582 C  CG  . ASN B  1 49  ? -58.333 11.205  12.836  1.00 12.35 ? 49   ASN B CG  1 
ATOM   3583 O  OD1 . ASN B  1 49  ? -58.876 11.683  11.832  1.00 12.81 ? 49   ASN B OD1 1 
ATOM   3584 N  ND2 . ASN B  1 49  ? -57.354 11.822  13.540  1.00 12.61 ? 49   ASN B ND2 1 
ATOM   3585 N  N   . PRO B  1 50  ? -57.121 7.053   13.994  1.00 14.06 ? 50   PRO B N   1 
ATOM   3586 C  CA  . PRO B  1 50  ? -57.111 5.833   14.802  1.00 14.22 ? 50   PRO B CA  1 
ATOM   3587 C  C   . PRO B  1 50  ? -58.232 5.856   15.847  1.00 14.74 ? 50   PRO B C   1 
ATOM   3588 O  O   . PRO B  1 50  ? -58.524 6.911   16.405  1.00 14.83 ? 50   PRO B O   1 
ATOM   3589 C  CB  . PRO B  1 50  ? -55.748 5.884   15.491  1.00 13.32 ? 50   PRO B CB  1 
ATOM   3590 C  CG  . PRO B  1 50  ? -55.492 7.352   15.598  1.00 14.29 ? 50   PRO B CG  1 
ATOM   3591 C  CD  . PRO B  1 50  ? -55.924 7.884   14.251  1.00 13.23 ? 50   PRO B CD  1 
ATOM   3592 N  N   . ALA B  1 51  ? -58.811 4.701   16.115  1.00 14.73 ? 51   ALA B N   1 
ATOM   3593 C  CA  . ALA B  1 51  ? -59.865 4.519   17.130  1.00 15.73 ? 51   ALA B CA  1 
ATOM   3594 C  C   . ALA B  1 51  ? -59.350 5.000   18.484  1.00 16.73 ? 51   ALA B C   1 
ATOM   3595 O  O   . ALA B  1 51  ? -60.135 5.621   19.203  1.00 18.83 ? 51   ALA B O   1 
ATOM   3596 C  CB  . ALA B  1 51  ? -60.294 3.070   17.217  1.00 14.01 ? 51   ALA B CB  1 
ATOM   3597 N  N   . LEU B  1 52  ? -58.121 4.638   18.836  1.00 16.78 ? 52   LEU B N   1 
ATOM   3598 C  CA  . LEU B  1 52  ? -57.478 4.999   20.119  1.00 17.66 ? 52   LEU B CA  1 
ATOM   3599 C  C   . LEU B  1 52  ? -56.050 5.455   19.831  1.00 18.80 ? 52   LEU B C   1 
ATOM   3600 O  O   . LEU B  1 52  ? -55.488 5.066   18.777  1.00 15.48 ? 52   LEU B O   1 
ATOM   3601 C  CB  . LEU B  1 52  ? -57.473 3.793   21.046  1.00 17.73 ? 52   LEU B CB  1 
ATOM   3602 C  CG  . LEU B  1 52  ? -58.848 3.256   21.475  1.00 19.76 ? 52   LEU B CG  1 
ATOM   3603 C  CD1 . LEU B  1 52  ? -58.676 1.920   22.193  1.00 20.89 ? 52   LEU B CD1 1 
ATOM   3604 C  CD2 . LEU B  1 52  ? -59.571 4.256   22.367  1.00 21.76 ? 52   LEU B CD2 1 
ATOM   3605 N  N   . ALA B  1 53  ? -55.485 6.267   20.718  1.00 16.88 ? 53   ALA B N   1 
ATOM   3606 C  CA  . ALA B  1 53  ? -54.096 6.732   20.591  1.00 17.79 ? 53   ALA B CA  1 
ATOM   3607 C  C   . ALA B  1 53  ? -53.487 6.774   21.986  1.00 19.97 ? 53   ALA B C   1 
ATOM   3608 O  O   . ALA B  1 53  ? -54.256 6.960   22.963  1.00 20.29 ? 53   ALA B O   1 
ATOM   3609 C  CB  . ALA B  1 53  ? -54.076 8.069   19.909  1.00 18.50 ? 53   ALA B CB  1 
ATOM   3610 N  N   . GLY B  1 54  ? -52.193 6.499   22.058  1.00 20.94 ? 54   GLY B N   1 
ATOM   3611 C  CA  . GLY B  1 54  ? -51.440 6.470   23.322  1.00 23.38 ? 54   GLY B CA  1 
ATOM   3612 C  C   . GLY B  1 54  ? -50.433 5.350   23.328  1.00 26.80 ? 54   GLY B C   1 
ATOM   3613 O  O   . GLY B  1 54  ? -50.231 4.742   22.275  1.00 22.37 ? 54   GLY B O   1 
ATOM   3614 N  N   . PHE B  1 55  ? -49.826 5.103   24.490  1.00 30.27 ? 55   PHE B N   1 
ATOM   3615 C  CA  . PHE B  1 55  ? -48.626 4.247   24.649  1.00 33.89 ? 55   PHE B CA  1 
ATOM   3616 C  C   . PHE B  1 55  ? -48.920 2.858   24.079  1.00 30.39 ? 55   PHE B C   1 
ATOM   3617 O  O   . PHE B  1 55  ? -48.021 2.309   23.406  1.00 34.39 ? 55   PHE B O   1 
ATOM   3618 C  CB  . PHE B  1 55  ? -48.174 4.181   26.117  1.00 42.54 ? 55   PHE B CB  1 
ATOM   3619 C  CG  . PHE B  1 55  ? -47.069 3.182   26.397  1.00 50.60 ? 55   PHE B CG  1 
ATOM   3620 C  CD1 . PHE B  1 55  ? -45.821 3.304   25.791  1.00 58.25 ? 55   PHE B CD1 1 
ATOM   3621 C  CD2 . PHE B  1 55  ? -47.283 2.097   27.244  1.00 57.78 ? 55   PHE B CD2 1 
ATOM   3622 C  CE1 . PHE B  1 55  ? -44.815 2.377   26.035  1.00 58.77 ? 55   PHE B CE1 1 
ATOM   3623 C  CE2 . PHE B  1 55  ? -46.275 1.171   27.489  1.00 60.59 ? 55   PHE B CE2 1 
ATOM   3624 C  CZ  . PHE B  1 55  ? -45.042 1.316   26.886  1.00 59.99 ? 55   PHE B CZ  1 
ATOM   3625 N  N   . ASN B  1 56  ? -50.108 2.310   24.348  1.00 28.22 ? 56   ASN B N   1 
ATOM   3626 C  CA  . ASN B  1 56  ? -50.426 0.897   24.008  1.00 28.44 ? 56   ASN B CA  1 
ATOM   3627 C  C   . ASN B  1 56  ? -51.022 0.785   22.593  1.00 23.23 ? 56   ASN B C   1 
ATOM   3628 O  O   . ASN B  1 56  ? -51.408 -0.316  22.238  1.00 22.21 ? 56   ASN B O   1 
ATOM   3629 C  CB  . ASN B  1 56  ? -51.427 0.268   24.981  1.00 35.09 ? 56   ASN B CB  1 
ATOM   3630 C  CG  . ASN B  1 56  ? -51.064 0.448   26.442  1.00 38.04 ? 56   ASN B CG  1 
ATOM   3631 O  OD1 . ASN B  1 56  ? -49.902 0.345   26.826  1.00 42.40 ? 56   ASN B OD1 1 
ATOM   3632 N  ND2 . ASN B  1 56  ? -52.066 0.703   27.264  1.00 43.11 ? 56   ASN B ND2 1 
ATOM   3633 N  N   . HIS B  1 57  ? -51.097 1.869   21.825  1.00 21.71 ? 57   HIS B N   1 
ATOM   3634 C  CA  . HIS B  1 57  ? -51.853 1.912   20.541  1.00 19.57 ? 57   HIS B CA  1 
ATOM   3635 C  C   . HIS B  1 57  ? -50.862 2.105   19.399  1.00 18.68 ? 57   HIS B C   1 
ATOM   3636 O  O   . HIS B  1 57  ? -49.639 2.153   19.656  1.00 20.06 ? 57   HIS B O   1 
ATOM   3637 C  CB  . HIS B  1 57  ? -52.997 2.938   20.646  1.00 18.98 ? 57   HIS B CB  1 
ATOM   3638 C  CG  . HIS B  1 57  ? -53.908 2.653   21.795  1.00 20.46 ? 57   HIS B CG  1 
ATOM   3639 N  ND1 . HIS B  1 57  ? -54.543 1.431   21.938  1.00 19.54 ? 57   HIS B ND1 1 
ATOM   3640 C  CD2 . HIS B  1 57  ? -54.232 3.384   22.895  1.00 20.00 ? 57   HIS B CD2 1 
ATOM   3641 C  CE1 . HIS B  1 57  ? -55.233 1.428   23.066  1.00 19.90 ? 57   HIS B CE1 1 
ATOM   3642 N  NE2 . HIS B  1 57  ? -55.073 2.611   23.648  1.00 18.34 ? 57   HIS B NE2 1 
ATOM   3643 N  N   . GLN B  1 58  ? -51.354 2.185   18.160  1.00 17.39 ? 58   GLN B N   1 
ATOM   3644 C  CA  . GLN B  1 58  ? -50.482 2.351   16.968  1.00 16.52 ? 58   GLN B CA  1 
ATOM   3645 C  C   . GLN B  1 58  ? -49.663 3.648   17.079  1.00 17.27 ? 58   GLN B C   1 
ATOM   3646 O  O   . GLN B  1 58  ? -48.466 3.614   16.761  1.00 17.65 ? 58   GLN B O   1 
ATOM   3647 C  CB  . GLN B  1 58  ? -51.312 2.283   15.685  1.00 15.36 ? 58   GLN B CB  1 
ATOM   3648 C  CG  . GLN B  1 58  ? -50.464 2.327   14.436  1.00 15.61 ? 58   GLN B CG  1 
ATOM   3649 C  CD  . GLN B  1 58  ? -49.551 1.139   14.250  1.00 15.97 ? 58   GLN B CD  1 
ATOM   3650 O  OE1 . GLN B  1 58  ? -48.566 1.247   13.526  1.00 18.75 ? 58   GLN B OE1 1 
ATOM   3651 N  NE2 . GLN B  1 58  ? -49.847 0.007   14.853  1.00 14.74 ? 58   GLN B NE2 1 
ATOM   3652 N  N   . GLN B  1 59  ? -50.255 4.751   17.503  1.00 17.92 ? 59   GLN B N   1 
ATOM   3653 C  CA  . GLN B  1 59  ? -49.554 6.058   17.595  1.00 17.96 ? 59   GLN B CA  1 
ATOM   3654 C  C   . GLN B  1 59  ? -49.946 6.710   18.907  1.00 19.43 ? 59   GLN B C   1 
ATOM   3655 O  O   . GLN B  1 59  ? -50.955 6.345   19.508  1.00 18.50 ? 59   GLN B O   1 
ATOM   3656 C  CB  . GLN B  1 59  ? -49.924 6.968   16.423  1.00 19.57 ? 59   GLN B CB  1 
ATOM   3657 C  CG  . GLN B  1 59  ? -49.397 6.480   15.088  1.00 19.91 ? 59   GLN B CG  1 
ATOM   3658 C  CD  . GLN B  1 59  ? -47.900 6.686   14.957  1.00 22.47 ? 59   GLN B CD  1 
ATOM   3659 O  OE1 . GLN B  1 59  ? -47.313 7.564   15.611  1.00 22.58 ? 59   GLN B OE1 1 
ATOM   3660 N  NE2 . GLN B  1 59  ? -47.313 5.949   14.033  1.00 20.10 ? 59   GLN B NE2 1 
ATOM   3661 N  N   . PRO B  1 60  ? -49.130 7.659   19.402  1.00 19.22 ? 60   PRO B N   1 
ATOM   3662 C  CA  . PRO B  1 60  ? -49.449 8.357   20.648  1.00 19.86 ? 60   PRO B CA  1 
ATOM   3663 C  C   . PRO B  1 60  ? -50.497 9.460   20.507  1.00 19.12 ? 60   PRO B C   1 
ATOM   3664 O  O   . PRO B  1 60  ? -50.983 9.908   21.512  1.00 20.08 ? 60   PRO B O   1 
ATOM   3665 C  CB  . PRO B  1 60  ? -48.084 8.904   21.073  1.00 20.33 ? 60   PRO B CB  1 
ATOM   3666 C  CG  . PRO B  1 60  ? -47.368 9.156   19.759  1.00 20.48 ? 60   PRO B CG  1 
ATOM   3667 C  CD  . PRO B  1 60  ? -47.802 8.009   18.871  1.00 21.05 ? 60   PRO B CD  1 
ATOM   3668 N  N   . ILE B  1 61  ? -50.868 9.829   19.278  1.00 17.65 ? 61   ILE B N   1 
ATOM   3669 C  CA  . ILE B  1 61  ? -51.765 10.975  18.981  1.00 18.23 ? 61   ILE B CA  1 
ATOM   3670 C  C   . ILE B  1 61  ? -52.829 10.558  17.955  1.00 17.52 ? 61   ILE B C   1 
ATOM   3671 O  O   . ILE B  1 61  ? -52.651 9.508   17.304  1.00 15.70 ? 61   ILE B O   1 
ATOM   3672 C  CB  . ILE B  1 61  ? -50.900 12.145  18.466  1.00 22.90 ? 61   ILE B CB  1 
ATOM   3673 C  CG1 . ILE B  1 61  ? -49.881 11.681  17.424  1.00 27.06 ? 61   ILE B CG1 1 
ATOM   3674 C  CG2 . ILE B  1 61  ? -50.170 12.803  19.634  1.00 22.53 ? 61   ILE B CG2 1 
ATOM   3675 C  CD1 . ILE B  1 61  ? -50.407 11.460  16.078  1.00 28.46 ? 61   ILE B CD1 1 
ATOM   3676 N  N   . GLY B  1 62  ? -53.880 11.357  17.822  1.00 16.37 ? 62   GLY B N   1 
ATOM   3677 C  CA  . GLY B  1 62  ? -54.821 11.317  16.684  1.00 16.82 ? 62   GLY B CA  1 
ATOM   3678 C  C   . GLY B  1 62  ? -56.159 10.662  16.999  1.00 16.01 ? 62   GLY B C   1 
ATOM   3679 O  O   . GLY B  1 62  ? -56.920 10.449  16.046  1.00 14.47 ? 62   GLY B O   1 
ATOM   3680 N  N   . ALA B  1 63  ? -56.486 10.413  18.272  1.00 15.42 ? 63   ALA B N   1 
ATOM   3681 C  CA  . ALA B  1 63  ? -57.712 9.669   18.654  1.00 15.90 ? 63   ALA B CA  1 
ATOM   3682 C  C   . ALA B  1 63  ? -58.944 10.242  17.946  1.00 16.10 ? 63   ALA B C   1 
ATOM   3683 O  O   . ALA B  1 63  ? -59.166 11.463  17.945  1.00 15.97 ? 63   ALA B O   1 
ATOM   3684 C  CB  . ALA B  1 63  ? -57.878 9.592   20.147  1.00 16.47 ? 63   ALA B CB  1 
ATOM   3685 N  N   . ALA B  1 64  ? -59.731 9.349   17.334  1.00 15.00 ? 64   ALA B N   1 
ATOM   3686 C  CA  . ALA B  1 64  ? -60.833 9.713   16.412  1.00 15.87 ? 64   ALA B CA  1 
ATOM   3687 C  C   . ALA B  1 64  ? -61.920 10.521  17.129  1.00 15.14 ? 64   ALA B C   1 
ATOM   3688 O  O   . ALA B  1 64  ? -62.444 11.449  16.546  1.00 14.80 ? 64   ALA B O   1 
ATOM   3689 C  CB  . ALA B  1 64  ? -61.450 8.462   15.809  1.00 15.45 ? 64   ALA B CB  1 
ATOM   3690 N  N   . ILE B  1 65  ? -62.288 10.149  18.342  1.00 15.83 ? 65   ILE B N   1 
ATOM   3691 C  CA  . ILE B  1 65  ? -63.461 10.796  18.992  1.00 16.82 ? 65   ILE B CA  1 
ATOM   3692 C  C   . ILE B  1 65  ? -63.131 12.238  19.361  1.00 15.84 ? 65   ILE B C   1 
ATOM   3693 O  O   . ILE B  1 65  ? -63.839 13.161  18.946  1.00 16.04 ? 65   ILE B O   1 
ATOM   3694 C  CB  . ILE B  1 65  ? -63.963 9.935   20.159  1.00 18.54 ? 65   ILE B CB  1 
ATOM   3695 C  CG1 . ILE B  1 65  ? -64.597 8.659   19.602  1.00 19.06 ? 65   ILE B CG1 1 
ATOM   3696 C  CG2 . ILE B  1 65  ? -64.950 10.739  21.003  1.00 18.97 ? 65   ILE B CG2 1 
ATOM   3697 C  CD1 . ILE B  1 65  ? -64.698 7.533   20.588  1.00 21.84 ? 65   ILE B CD1 1 
ATOM   3698 N  N   . PRO B  1 66  ? -62.009 12.499  20.065  1.00 17.20 ? 66   PRO B N   1 
ATOM   3699 C  CA  . PRO B  1 66  ? -61.608 13.876  20.331  1.00 17.55 ? 66   PRO B CA  1 
ATOM   3700 C  C   . PRO B  1 66  ? -61.425 14.654  19.021  1.00 18.12 ? 66   PRO B C   1 
ATOM   3701 O  O   . PRO B  1 66  ? -61.769 15.816  19.000  1.00 17.20 ? 66   PRO B O   1 
ATOM   3702 C  CB  . PRO B  1 66  ? -60.292 13.790  21.120  1.00 19.90 ? 66   PRO B CB  1 
ATOM   3703 C  CG  . PRO B  1 66  ? -60.181 12.342  21.561  1.00 18.73 ? 66   PRO B CG  1 
ATOM   3704 C  CD  . PRO B  1 66  ? -61.168 11.519  20.758  1.00 17.12 ? 66   PRO B CD  1 
ATOM   3705 N  N   . THR B  1 67  ? -60.907 14.015  17.960  1.00 17.07 ? 67   THR B N   1 
ATOM   3706 C  CA  . THR B  1 67  ? -60.666 14.705  16.672  1.00 16.20 ? 67   THR B CA  1 
ATOM   3707 C  C   . THR B  1 67  ? -62.017 15.116  16.077  1.00 15.92 ? 67   THR B C   1 
ATOM   3708 O  O   . THR B  1 67  ? -62.143 16.250  15.570  1.00 17.08 ? 67   THR B O   1 
ATOM   3709 C  CB  . THR B  1 67  ? -59.753 13.898  15.733  1.00 16.57 ? 67   THR B CB  1 
ATOM   3710 O  OG1 . THR B  1 67  ? -58.510 13.669  16.399  1.00 17.82 ? 67   THR B OG1 1 
ATOM   3711 C  CG2 . THR B  1 67  ? -59.519 14.639  14.443  1.00 17.95 ? 67   THR B CG2 1 
ATOM   3712 N  N   . ALA B  1 68  ? -62.997 14.219  16.076  1.00 15.54 ? 68   ALA B N   1 
ATOM   3713 C  CA  . ALA B  1 68  ? -64.360 14.512  15.589  1.00 14.76 ? 68   ALA B CA  1 
ATOM   3714 C  C   . ALA B  1 68  ? -64.894 15.715  16.375  1.00 15.05 ? 68   ALA B C   1 
ATOM   3715 O  O   . ALA B  1 68  ? -65.502 16.604  15.770  1.00 14.34 ? 68   ALA B O   1 
ATOM   3716 C  CB  . ALA B  1 68  ? -65.250 13.306  15.747  1.00 15.40 ? 68   ALA B CB  1 
ATOM   3717 N  N   . GLY B  1 69  ? -64.732 15.676  17.689  1.00 17.42 ? 69   GLY B N   1 
ATOM   3718 C  CA  . GLY B  1 69  ? -65.107 16.811  18.555  1.00 18.65 ? 69   GLY B CA  1 
ATOM   3719 C  C   . GLY B  1 69  ? -64.601 18.127  18.022  1.00 18.44 ? 69   GLY B C   1 
ATOM   3720 O  O   . GLY B  1 69  ? -65.409 19.093  17.876  1.00 19.82 ? 69   GLY B O   1 
ATOM   3721 N  N   . ARG B  1 70  ? -63.301 18.209  17.737  1.00 17.56 ? 70   ARG B N   1 
ATOM   3722 C  CA  . ARG B  1 70  ? -62.656 19.468  17.293  1.00 18.93 ? 70   ARG B CA  1 
ATOM   3723 C  C   . ARG B  1 70  ? -63.216 19.923  15.956  1.00 18.69 ? 70   ARG B C   1 
ATOM   3724 O  O   . ARG B  1 70  ? -63.139 21.109  15.682  1.00 17.83 ? 70   ARG B O   1 
ATOM   3725 C  CB  . ARG B  1 70  ? -61.150 19.291  17.099  1.00 20.19 ? 70   ARG B CB  1 
ATOM   3726 C  CG  . ARG B  1 70  ? -60.402 18.939  18.356  1.00 23.51 ? 70   ARG B CG  1 
ATOM   3727 C  CD  . ARG B  1 70  ? -58.916 19.044  18.077  1.00 22.53 ? 70   ARG B CD  1 
ATOM   3728 N  NE  . ARG B  1 70  ? -58.487 20.435  18.031  1.00 24.25 ? 70   ARG B NE  1 
ATOM   3729 C  CZ  . ARG B  1 70  ? -57.472 20.906  17.292  1.00 23.82 ? 70   ARG B CZ  1 
ATOM   3730 N  NH1 . ARG B  1 70  ? -56.776 20.100  16.495  1.00 23.34 ? 70   ARG B NH1 1 
ATOM   3731 N  NH2 . ARG B  1 70  ? -57.178 22.191  17.331  1.00 21.92 ? 70   ARG B NH2 1 
ATOM   3732 N  N   . LEU B  1 71  ? -63.684 18.986  15.127  1.00 18.22 ? 71   LEU B N   1 
ATOM   3733 C  CA  . LEU B  1 71  ? -64.119 19.234  13.725  1.00 18.24 ? 71   LEU B CA  1 
ATOM   3734 C  C   . LEU B  1 71  ? -65.624 19.481  13.647  1.00 19.30 ? 71   LEU B C   1 
ATOM   3735 O  O   . LEU B  1 71  ? -66.123 19.744  12.543  1.00 19.05 ? 71   LEU B O   1 
ATOM   3736 C  CB  . LEU B  1 71  ? -63.747 18.014  12.877  1.00 17.38 ? 71   LEU B CB  1 
ATOM   3737 C  CG  . LEU B  1 71  ? -62.252 17.795  12.693  1.00 18.41 ? 71   LEU B CG  1 
ATOM   3738 C  CD1 . LEU B  1 71  ? -61.972 16.470  12.008  1.00 18.90 ? 71   LEU B CD1 1 
ATOM   3739 C  CD2 . LEU B  1 71  ? -61.646 18.949  11.912  1.00 19.99 ? 71   LEU B CD2 1 
ATOM   3740 N  N   . LYS B  1 72  ? -66.327 19.411  14.770  1.00 22.70 ? 72   LYS B N   1 
ATOM   3741 C  CA  . LYS B  1 72  ? -67.802 19.276  14.763  1.00 26.33 ? 72   LYS B CA  1 
ATOM   3742 C  C   . LYS B  1 72  ? -68.464 20.532  14.191  1.00 26.32 ? 72   LYS B C   1 
ATOM   3743 O  O   . LYS B  1 72  ? -69.580 20.378  13.702  1.00 27.17 ? 72   LYS B O   1 
ATOM   3744 C  CB  . LYS B  1 72  ? -68.305 18.968  16.169  1.00 30.19 ? 72   LYS B CB  1 
ATOM   3745 C  CG  . LYS B  1 72  ? -68.533 20.196  17.028  1.00 34.06 ? 72   LYS B CG  1 
ATOM   3746 C  CD  . LYS B  1 72  ? -68.981 19.811  18.415  1.00 39.79 ? 72   LYS B CD  1 
ATOM   3747 C  CE  . LYS B  1 72  ? -68.502 20.786  19.458  1.00 43.03 ? 72   LYS B CE  1 
ATOM   3748 N  NZ  . LYS B  1 72  ? -68.864 20.276  20.795  1.00 50.36 ? 72   LYS B NZ  1 
ATOM   3749 N  N   . ASN B  1 73  ? -67.803 21.691  14.179  1.00 24.24 ? 73   ASN B N   1 
ATOM   3750 C  CA  . ASN B  1 73  ? -68.358 22.915  13.533  1.00 29.01 ? 73   ASN B CA  1 
ATOM   3751 C  C   . ASN B  1 73  ? -67.745 23.172  12.151  1.00 30.53 ? 73   ASN B C   1 
ATOM   3752 O  O   . ASN B  1 73  ? -68.057 24.232  11.547  1.00 31.13 ? 73   ASN B O   1 
ATOM   3753 C  CB  . ASN B  1 73  ? -68.191 24.131  14.441  1.00 31.50 ? 73   ASN B CB  1 
ATOM   3754 C  CG  . ASN B  1 73  ? -69.056 23.980  15.671  1.00 33.17 ? 73   ASN B CG  1 
ATOM   3755 O  OD1 . ASN B  1 73  ? -68.574 24.095  16.788  1.00 39.87 ? 73   ASN B OD1 1 
ATOM   3756 N  ND2 . ASN B  1 73  ? -70.323 23.669  15.475  1.00 37.94 ? 73   ASN B ND2 1 
ATOM   3757 N  N   . THR B  1 74  ? -66.934 22.257  11.631  1.00 23.74 ? 74   THR B N   1 
ATOM   3758 C  CA  . THR B  1 74  ? -66.528 22.277  10.205  1.00 21.45 ? 74   THR B CA  1 
ATOM   3759 C  C   . THR B  1 74  ? -67.439 21.321  9.420   1.00 18.52 ? 74   THR B C   1 
ATOM   3760 O  O   . THR B  1 74  ? -68.263 20.619  10.042  1.00 19.62 ? 74   THR B O   1 
ATOM   3761 C  CB  . THR B  1 74  ? -65.059 21.864  10.072  1.00 20.43 ? 74   THR B CB  1 
ATOM   3762 O  OG1 . THR B  1 74  ? -64.981 20.458  10.294  1.00 18.26 ? 74   THR B OG1 1 
ATOM   3763 C  CG2 . THR B  1 74  ? -64.173 22.567  11.074  1.00 22.33 ? 74   THR B CG2 1 
ATOM   3764 N  N   . THR B  1 75  ? -67.220 21.200  8.117   1.00 17.96 ? 75   THR B N   1 
ATOM   3765 C  CA  . THR B  1 75  ? -67.847 20.176  7.252   1.00 17.04 ? 75   THR B CA  1 
ATOM   3766 C  C   . THR B  1 75  ? -67.237 18.781  7.466   1.00 17.35 ? 75   THR B C   1 
ATOM   3767 O  O   . THR B  1 75  ? -67.797 17.820  6.920   1.00 17.81 ? 75   THR B O   1 
ATOM   3768 C  CB  . THR B  1 75  ? -67.747 20.587  5.781   1.00 16.79 ? 75   THR B CB  1 
ATOM   3769 O  OG1 . THR B  1 75  ? -66.367 20.685  5.412   1.00 15.40 ? 75   THR B OG1 1 
ATOM   3770 C  CG2 . THR B  1 75  ? -68.425 21.913  5.510   1.00 16.99 ? 75   THR B CG2 1 
ATOM   3771 N  N   . GLY B  1 76  ? -66.161 18.653  8.222   1.00 16.78 ? 76   GLY B N   1 
ATOM   3772 C  CA  . GLY B  1 76  ? -65.346 17.424  8.295   1.00 17.83 ? 76   GLY B CA  1 
ATOM   3773 C  C   . GLY B  1 76  ? -65.998 16.297  9.069   1.00 17.19 ? 76   GLY B C   1 
ATOM   3774 O  O   . GLY B  1 76  ? -66.579 16.522  10.154  1.00 16.78 ? 76   GLY B O   1 
ATOM   3775 N  N   . LYS B  1 77  ? -65.885 15.082  8.542   1.00 16.21 ? 77   LYS B N   1 
ATOM   3776 C  CA  . LYS B  1 77  ? -66.296 13.847  9.232   1.00 15.58 ? 77   LYS B CA  1 
ATOM   3777 C  C   . LYS B  1 77  ? -65.068 12.980  9.464   1.00 13.79 ? 77   LYS B C   1 
ATOM   3778 O  O   . LYS B  1 77  ? -64.065 13.209  8.781   1.00 13.23 ? 77   LYS B O   1 
ATOM   3779 C  CB  . LYS B  1 77  ? -67.301 13.086  8.369   1.00 16.85 ? 77   LYS B CB  1 
ATOM   3780 C  CG  . LYS B  1 77  ? -68.579 13.846  8.076   1.00 19.80 ? 77   LYS B CG  1 
ATOM   3781 C  CD  . LYS B  1 77  ? -69.402 13.077  7.079   1.00 25.55 ? 77   LYS B CD  1 
ATOM   3782 C  CE  . LYS B  1 77  ? -70.388 13.943  6.330   1.00 32.34 ? 77   LYS B CE  1 
ATOM   3783 N  NZ  . LYS B  1 77  ? -71.733 13.843  6.933   1.00 36.55 ? 77   LYS B NZ  1 
ATOM   3784 N  N   . VAL B  1 78  ? -65.179 12.005  10.355  1.00 13.27 ? 78   VAL B N   1 
ATOM   3785 C  CA  . VAL B  1 78  ? -64.038 11.171  10.810  1.00 12.79 ? 78   VAL B CA  1 
ATOM   3786 C  C   . VAL B  1 78  ? -64.393 9.708   10.589  1.00 12.94 ? 78   VAL B C   1 
ATOM   3787 O  O   . VAL B  1 78  ? -65.400 9.213   11.158  1.00 11.79 ? 78   VAL B O   1 
ATOM   3788 C  CB  . VAL B  1 78  ? -63.665 11.440  12.278  1.00 12.78 ? 78   VAL B CB  1 
ATOM   3789 C  CG1 . VAL B  1 78  ? -62.639 10.452  12.803  1.00 13.77 ? 78   VAL B CG1 1 
ATOM   3790 C  CG2 . VAL B  1 78  ? -63.157 12.869  12.444  1.00 13.80 ? 78   VAL B CG2 1 
ATOM   3791 N  N   . MET B  1 79  ? -63.531 9.055   9.820   1.00 12.25 ? 79   MET B N   1 
ATOM   3792 C  CA  . MET B  1 79  ? -63.584 7.584   9.671   1.00 12.91 ? 79   MET B CA  1 
ATOM   3793 C  C   . MET B  1 79  ? -62.719 6.986   10.778  1.00 12.89 ? 79   MET B C   1 
ATOM   3794 O  O   . MET B  1 79  ? -61.559 7.414   10.938  1.00 11.20 ? 79   MET B O   1 
ATOM   3795 C  CB  . MET B  1 79  ? -63.061 7.155   8.299   1.00 14.09 ? 79   MET B CB  1 
ATOM   3796 C  CG  . MET B  1 79  ? -63.220 5.657   8.116   1.00 15.00 ? 79   MET B CG  1 
ATOM   3797 S  SD  . MET B  1 79  ? -62.358 4.955   6.726   1.00 14.39 ? 79   MET B SD  1 
ATOM   3798 C  CE  . MET B  1 79  ? -62.759 6.019   5.345   1.00 15.00 ? 79   MET B CE  1 
ATOM   3799 N  N   . ILE B  1 80  ? -63.237 5.984   11.487  1.00 12.49 ? 80   ILE B N   1 
ATOM   3800 C  CA  . ILE B  1 80  ? -62.556 5.344   12.647  1.00 11.83 ? 80   ILE B CA  1 
ATOM   3801 C  C   . ILE B  1 80  ? -61.737 4.143   12.165  1.00 11.31 ? 80   ILE B C   1 
ATOM   3802 O  O   . ILE B  1 80  ? -62.302 3.147   11.759  1.00 11.98 ? 80   ILE B O   1 
ATOM   3803 C  CB  . ILE B  1 80  ? -63.544 4.977   13.767  1.00 12.72 ? 80   ILE B CB  1 
ATOM   3804 C  CG1 . ILE B  1 80  ? -64.268 6.203   14.324  1.00 12.65 ? 80   ILE B CG1 1 
ATOM   3805 C  CG2 . ILE B  1 80  ? -62.829 4.213   14.867  1.00 13.06 ? 80   ILE B CG2 1 
ATOM   3806 C  CD1 . ILE B  1 80  ? -65.525 5.842   15.122  1.00 13.58 ? 80   ILE B CD1 1 
ATOM   3807 N  N   . ARG B  1 81  ? -60.417 4.265   12.206  1.00 11.88 ? 81   ARG B N   1 
ATOM   3808 C  CA  . ARG B  1 81  ? -59.487 3.151   11.905  1.00 11.56 ? 81   ARG B CA  1 
ATOM   3809 C  C   . ARG B  1 81  ? -59.347 2.274   13.146  1.00 12.92 ? 81   ARG B C   1 
ATOM   3810 O  O   . ARG B  1 81  ? -58.533 2.616   14.047  1.00 12.17 ? 81   ARG B O   1 
ATOM   3811 C  CB  . ARG B  1 81  ? -58.150 3.702   11.409  1.00 11.87 ? 81   ARG B CB  1 
ATOM   3812 C  CG  . ARG B  1 81  ? -57.053 2.657   11.274  1.00 11.41 ? 81   ARG B CG  1 
ATOM   3813 C  CD  . ARG B  1 81  ? -55.980 3.176   10.367  1.00 11.57 ? 81   ARG B CD  1 
ATOM   3814 N  NE  . ARG B  1 81  ? -56.420 3.143   8.984   1.00 11.76 ? 81   ARG B NE  1 
ATOM   3815 C  CZ  . ARG B  1 81  ? -55.713 3.522   7.918   1.00 12.08 ? 81   ARG B CZ  1 
ATOM   3816 N  NH1 . ARG B  1 81  ? -56.272 3.442   6.719   1.00 12.05 ? 81   ARG B NH1 1 
ATOM   3817 N  NH2 . ARG B  1 81  ? -54.460 3.956   8.035   1.00 12.29 ? 81   ARG B NH2 1 
ATOM   3818 N  N   . LEU B  1 82  ? -60.090 1.169   13.191  1.00 12.25 ? 82   LEU B N   1 
ATOM   3819 C  CA  . LEU B  1 82  ? -60.111 0.272   14.377  1.00 12.97 ? 82   LEU B CA  1 
ATOM   3820 C  C   . LEU B  1 82  ? -58.769 -0.465  14.541  1.00 13.91 ? 82   LEU B C   1 
ATOM   3821 O  O   . LEU B  1 82  ? -58.423 -0.813  15.693  1.00 14.68 ? 82   LEU B O   1 
ATOM   3822 C  CB  . LEU B  1 82  ? -61.279 -0.710  14.295  1.00 13.66 ? 82   LEU B CB  1 
ATOM   3823 C  CG  . LEU B  1 82  ? -62.661 -0.097  14.495  1.00 13.73 ? 82   LEU B CG  1 
ATOM   3824 C  CD1 . LEU B  1 82  ? -63.732 -1.091  14.128  1.00 13.65 ? 82   LEU B CD1 1 
ATOM   3825 C  CD2 . LEU B  1 82  ? -62.871 0.415   15.915  1.00 14.12 ? 82   LEU B CD2 1 
ATOM   3826 N  N   . ALA B  1 83  ? -58.015 -0.700  13.471  1.00 13.76 ? 83   ALA B N   1 
ATOM   3827 C  CA  . ALA B  1 83  ? -56.784 -1.528  13.565  1.00 13.67 ? 83   ALA B CA  1 
ATOM   3828 C  C   . ALA B  1 83  ? -55.745 -0.829  14.458  1.00 14.17 ? 83   ALA B C   1 
ATOM   3829 O  O   . ALA B  1 83  ? -54.990 -1.524  15.152  1.00 13.69 ? 83   ALA B O   1 
ATOM   3830 C  CB  . ALA B  1 83  ? -56.194 -1.837  12.213  1.00 14.78 ? 83   ALA B CB  1 
ATOM   3831 N  N   . ASP B  1 84  ? -55.793 0.489   14.530  1.00 14.46 ? 84   ASP B N   1 
ATOM   3832 C  CA  . ASP B  1 84  ? -54.781 1.282   15.263  1.00 13.83 ? 84   ASP B CA  1 
ATOM   3833 C  C   . ASP B  1 84  ? -54.994 1.164   16.785  1.00 15.05 ? 84   ASP B C   1 
ATOM   3834 O  O   . ASP B  1 84  ? -54.157 1.690   17.552  1.00 15.74 ? 84   ASP B O   1 
ATOM   3835 C  CB  . ASP B  1 84  ? -54.763 2.722   14.765  1.00 14.60 ? 84   ASP B CB  1 
ATOM   3836 C  CG  . ASP B  1 84  ? -54.004 2.892   13.445  1.00 14.02 ? 84   ASP B CG  1 
ATOM   3837 O  OD1 . ASP B  1 84  ? -53.712 1.868   12.827  1.00 14.69 ? 84   ASP B OD1 1 
ATOM   3838 O  OD2 . ASP B  1 84  ? -53.757 4.032   13.034  1.00 14.21 ? 84   ASP B OD2 1 
ATOM   3839 N  N   . ILE B  1 85  ? -56.030 0.457   17.226  1.00 14.41 ? 85   ILE B N   1 
ATOM   3840 C  CA  . ILE B  1 85  ? -56.118 -0.050  18.624  1.00 15.72 ? 85   ILE B CA  1 
ATOM   3841 C  C   . ILE B  1 85  ? -54.796 -0.769  18.931  1.00 17.16 ? 85   ILE B C   1 
ATOM   3842 O  O   . ILE B  1 85  ? -54.315 -0.659  20.094  1.00 17.09 ? 85   ILE B O   1 
ATOM   3843 C  CB  . ILE B  1 85  ? -57.346 -0.956  18.802  1.00 16.09 ? 85   ILE B CB  1 
ATOM   3844 C  CG1 . ILE B  1 85  ? -58.641 -0.129  18.785  1.00 15.89 ? 85   ILE B CG1 1 
ATOM   3845 C  CG2 . ILE B  1 85  ? -57.256 -1.834  20.057  1.00 18.42 ? 85   ILE B CG2 1 
ATOM   3846 C  CD1 . ILE B  1 85  ? -59.909 -0.949  18.649  1.00 16.04 ? 85   ILE B CD1 1 
ATOM   3847 N  N   . PHE B  1 86  ? -54.212 -1.454  17.943  1.00 16.24 ? 86   PHE B N   1 
ATOM   3848 C  CA  . PHE B  1 86  ? -53.016 -2.299  18.198  1.00 16.80 ? 86   PHE B CA  1 
ATOM   3849 C  C   . PHE B  1 86  ? -51.755 -1.542  17.846  1.00 17.11 ? 86   PHE B C   1 
ATOM   3850 O  O   . PHE B  1 86  ? -51.695 -0.797  16.860  1.00 16.46 ? 86   PHE B O   1 
ATOM   3851 C  CB  . PHE B  1 86  ? -53.060 -3.625  17.445  1.00 17.72 ? 86   PHE B CB  1 
ATOM   3852 C  CG  . PHE B  1 86  ? -54.086 -4.585  17.961  1.00 17.39 ? 86   PHE B CG  1 
ATOM   3853 C  CD1 . PHE B  1 86  ? -54.041 -5.031  19.277  1.00 18.20 ? 86   PHE B CD1 1 
ATOM   3854 C  CD2 . PHE B  1 86  ? -55.094 -5.053  17.133  1.00 19.59 ? 86   PHE B CD2 1 
ATOM   3855 C  CE1 . PHE B  1 86  ? -54.999 -5.902  19.758  1.00 19.26 ? 86   PHE B CE1 1 
ATOM   3856 C  CE2 . PHE B  1 86  ? -56.037 -5.947  17.615  1.00 19.21 ? 86   PHE B CE2 1 
ATOM   3857 C  CZ  . PHE B  1 86  ? -55.991 -6.366  18.925  1.00 20.83 ? 86   PHE B CZ  1 
ATOM   3858 N  N   . PRO B  1 87  ? -50.697 -1.754  18.654  1.00 18.66 ? 87   PRO B N   1 
ATOM   3859 C  CA  . PRO B  1 87  ? -49.377 -1.240  18.332  1.00 19.61 ? 87   PRO B CA  1 
ATOM   3860 C  C   . PRO B  1 87  ? -48.659 -2.140  17.311  1.00 19.81 ? 87   PRO B C   1 
ATOM   3861 O  O   . PRO B  1 87  ? -49.118 -3.251  17.046  1.00 17.93 ? 87   PRO B O   1 
ATOM   3862 C  CB  . PRO B  1 87  ? -48.709 -1.234  19.708  1.00 19.71 ? 87   PRO B CB  1 
ATOM   3863 C  CG  . PRO B  1 87  ? -49.252 -2.481  20.379  1.00 19.28 ? 87   PRO B CG  1 
ATOM   3864 C  CD  . PRO B  1 87  ? -50.698 -2.563  19.892  1.00 18.95 ? 87   PRO B CD  1 
ATOM   3865 N  N   A ARG B  1 88  ? -47.657 -1.528  16.679  0.60 20.05 ? 88   ARG B N   1 
ATOM   3866 N  N   B ARG B  1 88  ? -47.510 -1.694  16.798  0.40 20.00 ? 88   ARG B N   1 
ATOM   3867 C  CA  A ARG B  1 88  ? -46.597 -2.158  15.852  0.60 20.02 ? 88   ARG B CA  1 
ATOM   3868 C  CA  B ARG B  1 88  ? -46.593 -2.472  15.910  0.40 19.94 ? 88   ARG B CA  1 
ATOM   3869 C  C   A ARG B  1 88  ? -47.093 -2.358  14.417  0.60 21.05 ? 88   ARG B C   1 
ATOM   3870 C  C   B ARG B  1 88  ? -47.076 -2.397  14.452  0.40 20.85 ? 88   ARG B C   1 
ATOM   3871 O  O   A ARG B  1 88  ? -48.320 -2.300  14.161  0.60 19.52 ? 88   ARG B O   1 
ATOM   3872 O  O   B ARG B  1 88  ? -48.287 -2.190  14.213  0.40 20.14 ? 88   ARG B O   1 
ATOM   3873 C  CB  A ARG B  1 88  ? -46.105 -3.473  16.469  0.60 20.73 ? 88   ARG B CB  1 
ATOM   3874 C  CB  B ARG B  1 88  ? -46.459 -3.957  16.298  0.40 20.17 ? 88   ARG B CB  1 
ATOM   3875 C  CG  A ARG B  1 88  ? -45.513 -3.312  17.859  0.60 21.95 ? 88   ARG B CG  1 
ATOM   3876 C  CG  B ARG B  1 88  ? -45.905 -4.253  17.688  0.40 19.95 ? 88   ARG B CG  1 
ATOM   3877 C  CD  A ARG B  1 88  ? -44.852 -4.577  18.341  0.60 23.61 ? 88   ARG B CD  1 
ATOM   3878 C  CD  B ARG B  1 88  ? -45.183 -5.603  17.744  0.40 20.74 ? 88   ARG B CD  1 
ATOM   3879 N  NE  A ARG B  1 88  ? -45.819 -5.577  18.744  0.60 24.89 ? 88   ARG B NE  1 
ATOM   3880 N  NE  B ARG B  1 88  ? -45.962 -6.742  18.240  0.40 21.84 ? 88   ARG B NE  1 
ATOM   3881 C  CZ  A ARG B  1 88  ? -46.437 -5.635  19.922  0.60 25.74 ? 88   ARG B CZ  1 
ATOM   3882 C  CZ  B ARG B  1 88  ? -46.284 -7.839  17.547  0.40 22.26 ? 88   ARG B CZ  1 
ATOM   3883 N  NH1 A ARG B  1 88  ? -46.242 -4.705  20.841  0.60 27.55 ? 88   ARG B NH1 1 
ATOM   3884 N  NH1 B ARG B  1 88  ? -46.987 -8.796  18.126  0.40 23.22 ? 88   ARG B NH1 1 
ATOM   3885 N  NH2 A ARG B  1 88  ? -47.296 -6.612  20.157  0.60 25.92 ? 88   ARG B NH2 1 
ATOM   3886 N  NH2 B ARG B  1 88  ? -45.929 -7.976  16.288  0.40 21.55 ? 88   ARG B NH2 1 
ATOM   3887 N  N   . TRP B  1 89  ? -46.146 -2.588  13.513  1.00 20.29 ? 89   TRP B N   1 
ATOM   3888 C  CA  . TRP B  1 89  ? -46.435 -2.697  12.069  1.00 21.28 ? 89   TRP B CA  1 
ATOM   3889 C  C   . TRP B  1 89  ? -45.633 -3.856  11.509  1.00 24.63 ? 89   TRP B C   1 
ATOM   3890 O  O   . TRP B  1 89  ? -44.399 -3.818  11.563  1.00 27.40 ? 89   TRP B O   1 
ATOM   3891 C  CB  . TRP B  1 89  ? -46.124 -1.383  11.392  1.00 20.95 ? 89   TRP B CB  1 
ATOM   3892 C  CG  . TRP B  1 89  ? -46.530 -1.386  9.962   1.00 23.43 ? 89   TRP B CG  1 
ATOM   3893 C  CD1 . TRP B  1 89  ? -45.748 -1.702  8.892   1.00 26.84 ? 89   TRP B CD1 1 
ATOM   3894 C  CD2 . TRP B  1 89  ? -47.820 -1.028  9.428   1.00 23.04 ? 89   TRP B CD2 1 
ATOM   3895 N  NE1 . TRP B  1 89  ? -46.471 -1.599  7.729   1.00 28.02 ? 89   TRP B NE1 1 
ATOM   3896 C  CE2 . TRP B  1 89  ? -47.746 -1.189  8.029   1.00 25.50 ? 89   TRP B CE2 1 
ATOM   3897 C  CE3 . TRP B  1 89  ? -49.038 -0.660  9.996   1.00 21.96 ? 89   TRP B CE3 1 
ATOM   3898 C  CZ2 . TRP B  1 89  ? -48.836 -0.955  7.190   1.00 25.47 ? 89   TRP B CZ2 1 
ATOM   3899 C  CZ3 . TRP B  1 89  ? -50.107 -0.410  9.169   1.00 22.70 ? 89   TRP B CZ3 1 
ATOM   3900 C  CH2 . TRP B  1 89  ? -50.003 -0.536  7.784   1.00 23.53 ? 89   TRP B CH2 1 
ATOM   3901 N  N   . PRO B  1 90  ? -46.287 -4.961  11.072  1.00 24.80 ? 90   PRO B N   1 
ATOM   3902 C  CA  . PRO B  1 90  ? -47.746 -5.075  11.084  1.00 22.39 ? 90   PRO B CA  1 
ATOM   3903 C  C   . PRO B  1 90  ? -48.342 -5.136  12.496  1.00 21.25 ? 90   PRO B C   1 
ATOM   3904 O  O   . PRO B  1 90  ? -47.653 -5.497  13.460  1.00 21.21 ? 90   PRO B O   1 
ATOM   3905 C  CB  . PRO B  1 90  ? -48.008 -6.387  10.318  1.00 23.50 ? 90   PRO B CB  1 
ATOM   3906 C  CG  . PRO B  1 90  ? -46.771 -7.213  10.558  1.00 26.17 ? 90   PRO B CG  1 
ATOM   3907 C  CD  . PRO B  1 90  ? -45.647 -6.205  10.605  1.00 25.78 ? 90   PRO B CD  1 
ATOM   3908 N  N   . TYR B  1 91  ? -49.649 -4.870  12.595  1.00 18.76 ? 91   TYR B N   1 
ATOM   3909 C  CA  . TYR B  1 91  ? -50.388 -4.762  13.883  1.00 17.72 ? 91   TYR B CA  1 
ATOM   3910 C  C   . TYR B  1 91  ? -50.118 -5.970  14.777  1.00 18.31 ? 91   TYR B C   1 
ATOM   3911 O  O   . TYR B  1 91  ? -50.199 -7.111  14.291  1.00 18.28 ? 91   TYR B O   1 
ATOM   3912 C  CB  . TYR B  1 91  ? -51.889 -4.639  13.606  1.00 16.91 ? 91   TYR B CB  1 
ATOM   3913 C  CG  . TYR B  1 91  ? -52.224 -3.371  12.858  1.00 15.50 ? 91   TYR B CG  1 
ATOM   3914 C  CD1 . TYR B  1 91  ? -52.198 -2.152  13.502  1.00 15.02 ? 91   TYR B CD1 1 
ATOM   3915 C  CD2 . TYR B  1 91  ? -52.542 -3.386  11.515  1.00 13.67 ? 91   TYR B CD2 1 
ATOM   3916 C  CE1 . TYR B  1 91  ? -52.516 -0.974  12.843  1.00 13.69 ? 91   TYR B CE1 1 
ATOM   3917 C  CE2 . TYR B  1 91  ? -52.828 -2.218  10.830  1.00 13.32 ? 91   TYR B CE2 1 
ATOM   3918 C  CZ  . TYR B  1 91  ? -52.820 -1.007  11.497  1.00 12.99 ? 91   TYR B CZ  1 
ATOM   3919 O  OH  . TYR B  1 91  ? -53.108 0.163   10.837  1.00 13.58 ? 91   TYR B OH  1 
ATOM   3920 N  N   . GLY B  1 92  ? -49.876 -5.716  16.068  1.00 17.59 ? 92   GLY B N   1 
ATOM   3921 C  CA  . GLY B  1 92  ? -49.771 -6.771  17.091  1.00 19.79 ? 92   GLY B CA  1 
ATOM   3922 C  C   . GLY B  1 92  ? -51.140 -7.273  17.505  1.00 20.18 ? 92   GLY B C   1 
ATOM   3923 O  O   . GLY B  1 92  ? -51.501 -7.155  18.718  1.00 21.59 ? 92   GLY B O   1 
ATOM   3924 N  N   . PHE B  1 93  ? -51.852 -7.939  16.595  1.00 19.60 ? 93   PHE B N   1 
ATOM   3925 C  CA  . PHE B  1 93  ? -53.154 -8.547  16.914  1.00 20.00 ? 93   PHE B CA  1 
ATOM   3926 C  C   . PHE B  1 93  ? -52.933 -9.548  18.056  1.00 21.50 ? 93   PHE B C   1 
ATOM   3927 O  O   . PHE B  1 93  ? -51.910 -10.269 18.021  1.00 22.41 ? 93   PHE B O   1 
ATOM   3928 C  CB  . PHE B  1 93  ? -53.747 -9.203  15.675  1.00 20.47 ? 93   PHE B CB  1 
ATOM   3929 C  CG  . PHE B  1 93  ? -55.076 -9.853  15.914  1.00 20.47 ? 93   PHE B CG  1 
ATOM   3930 C  CD1 . PHE B  1 93  ? -56.235 -9.098  15.852  1.00 20.08 ? 93   PHE B CD1 1 
ATOM   3931 C  CD2 . PHE B  1 93  ? -55.161 -11.194 16.267  1.00 21.95 ? 93   PHE B CD2 1 
ATOM   3932 C  CE1 . PHE B  1 93  ? -57.471 -9.681  16.048  1.00 22.21 ? 93   PHE B CE1 1 
ATOM   3933 C  CE2 . PHE B  1 93  ? -56.399 -11.770 16.490  1.00 22.99 ? 93   PHE B CE2 1 
ATOM   3934 C  CZ  . PHE B  1 93  ? -57.547 -11.019 16.370  1.00 22.95 ? 93   PHE B CZ  1 
ATOM   3935 N  N   . THR B  1 94  ? -53.857 -9.574  19.010  1.00 21.48 ? 94   THR B N   1 
ATOM   3936 C  CA  . THR B  1 94  ? -53.836 -10.424 20.235  1.00 22.31 ? 94   THR B CA  1 
ATOM   3937 C  C   . THR B  1 94  ? -54.698 -11.668 19.990  1.00 21.96 ? 94   THR B C   1 
ATOM   3938 O  O   . THR B  1 94  ? -54.159 -12.709 19.542  1.00 23.18 ? 94   THR B O   1 
ATOM   3939 C  CB  . THR B  1 94  ? -54.268 -9.572  21.435  1.00 22.49 ? 94   THR B CB  1 
ATOM   3940 O  OG1 . THR B  1 94  ? -55.491 -8.902  21.111  1.00 23.29 ? 94   THR B OG1 1 
ATOM   3941 C  CG2 . THR B  1 94  ? -53.235 -8.531  21.796  1.00 23.36 ? 94   THR B CG2 1 
ATOM   3942 N  N   . ASN B  1 95  ? -56.003 -11.551 20.216  1.00 19.68 ? 95   ASN B N   1 
ATOM   3943 C  CA  . ASN B  1 95  ? -56.967 -12.648 19.987  1.00 21.24 ? 95   ASN B CA  1 
ATOM   3944 C  C   . ASN B  1 95  ? -58.332 -11.996 19.808  1.00 20.64 ? 95   ASN B C   1 
ATOM   3945 O  O   . ASN B  1 95  ? -58.470 -10.796 20.144  1.00 21.98 ? 95   ASN B O   1 
ATOM   3946 C  CB  . ASN B  1 95  ? -56.978 -13.653 21.136  1.00 22.19 ? 95   ASN B CB  1 
ATOM   3947 C  CG  . ASN B  1 95  ? -57.254 -12.953 22.449  1.00 24.88 ? 95   ASN B CG  1 
ATOM   3948 O  OD1 . ASN B  1 95  ? -58.377 -12.541 22.731  1.00 24.77 ? 95   ASN B OD1 1 
ATOM   3949 N  ND2 . ASN B  1 95  ? -56.207 -12.750 23.221  1.00 23.27 ? 95   ASN B ND2 1 
ATOM   3950 N  N   A MET B  1 96  ? -59.288 -12.757 19.290  0.60 19.39 ? 96   MET B N   1 
ATOM   3951 N  N   B MET B  1 96  ? -59.319 -12.779 19.354  0.40 21.25 ? 96   MET B N   1 
ATOM   3952 C  CA  A MET B  1 96  ? -60.607 -12.214 18.889  0.60 19.15 ? 96   MET B CA  1 
ATOM   3953 C  CA  B MET B  1 96  ? -60.704 -12.317 19.052  0.40 21.91 ? 96   MET B CA  1 
ATOM   3954 C  C   A MET B  1 96  ? -61.335 -11.635 20.099  0.60 20.55 ? 96   MET B C   1 
ATOM   3955 C  C   B MET B  1 96  ? -61.372 -11.781 20.330  0.40 22.83 ? 96   MET B C   1 
ATOM   3956 O  O   A MET B  1 96  ? -61.933 -10.574 19.968  0.60 19.43 ? 96   MET B O   1 
ATOM   3957 O  O   B MET B  1 96  ? -61.951 -10.686 20.265  0.40 20.33 ? 96   MET B O   1 
ATOM   3958 C  CB  A MET B  1 96  ? -61.448 -13.306 18.234  0.60 18.22 ? 96   MET B CB  1 
ATOM   3959 C  CB  B MET B  1 96  ? -61.537 -13.452 18.439  0.40 22.55 ? 96   MET B CB  1 
ATOM   3960 C  CG  A MET B  1 96  ? -61.072 -13.505 16.805  0.60 17.83 ? 96   MET B CG  1 
ATOM   3961 C  CG  B MET B  1 96  ? -62.783 -12.989 17.678  0.40 22.72 ? 96   MET B CG  1 
ATOM   3962 S  SD  A MET B  1 96  ? -61.137 -11.949 15.856  0.60 16.86 ? 96   MET B SD  1 
ATOM   3963 S  SD  B MET B  1 96  ? -62.452 -12.440 15.960  0.40 24.43 ? 96   MET B SD  1 
ATOM   3964 C  CE  A MET B  1 96  ? -62.860 -11.494 16.036  0.60 17.03 ? 96   MET B CE  1 
ATOM   3965 C  CE  B MET B  1 96  ? -60.779 -11.825 16.138  0.40 23.44 ? 96   MET B CE  1 
ATOM   3966 N  N   A ASN B  1 97  ? -61.297 -12.314 21.249  0.50 21.02 ? 97   ASN B N   1 
ATOM   3967 N  N   B ASN B  1 97  ? -61.303 -12.484 21.466  0.50 23.34 ? 97   ASN B N   1 
ATOM   3968 C  CA  A ASN B  1 97  ? -62.006 -11.852 22.477  0.50 21.93 ? 97   ASN B CA  1 
ATOM   3969 C  CA  B ASN B  1 97  ? -61.909 -11.971 22.727  0.50 24.67 ? 97   ASN B CA  1 
ATOM   3970 C  C   A ASN B  1 97  ? -61.462 -10.482 22.917  0.50 21.22 ? 97   ASN B C   1 
ATOM   3971 C  C   B ASN B  1 97  ? -61.449 -10.529 22.981  0.50 22.75 ? 97   ASN B C   1 
ATOM   3972 O  O   A ASN B  1 97  ? -62.289 -9.584  23.241  0.50 23.06 ? 97   ASN B O   1 
ATOM   3973 O  O   B ASN B  1 97  ? -62.314 -9.645  23.229  0.50 24.96 ? 97   ASN B O   1 
ATOM   3974 C  CB  A ASN B  1 97  ? -61.943 -12.895 23.600  0.50 21.93 ? 97   ASN B CB  1 
ATOM   3975 C  CB  B ASN B  1 97  ? -61.603 -12.898 23.900  0.50 25.87 ? 97   ASN B CB  1 
ATOM   3976 C  CG  A ASN B  1 97  ? -62.508 -12.371 24.906  0.50 22.74 ? 97   ASN B CG  1 
ATOM   3977 C  CG  B ASN B  1 97  ? -62.519 -14.096 23.875  0.50 27.57 ? 97   ASN B CG  1 
ATOM   3978 O  OD1 A ASN B  1 97  ? -61.884 -11.552 25.571  0.50 26.02 ? 97   ASN B OD1 1 
ATOM   3979 O  OD1 B ASN B  1 97  ? -63.454 -14.123 23.076  0.50 31.88 ? 97   ASN B OD1 1 
ATOM   3980 N  ND2 A ASN B  1 97  ? -63.702 -12.798 25.257  0.50 21.60 ? 97   ASN B ND2 1 
ATOM   3981 N  ND2 B ASN B  1 97  ? -62.261 -15.071 24.734  0.50 30.05 ? 97   ASN B ND2 1 
ATOM   3982 N  N   . ASP B  1 98  ? -60.140 -10.303 22.921  1.00 20.86 ? 98   ASP B N   1 
ATOM   3983 C  CA  . ASP B  1 98  ? -59.505 -9.021  23.292  1.00 20.77 ? 98   ASP B CA  1 
ATOM   3984 C  C   . ASP B  1 98  ? -59.921 -7.947  22.274  1.00 19.32 ? 98   ASP B C   1 
ATOM   3985 O  O   . ASP B  1 98  ? -60.372 -6.879  22.668  1.00 18.54 ? 98   ASP B O   1 
ATOM   3986 C  CB  . ASP B  1 98  ? -57.989 -9.177  23.347  1.00 21.04 ? 98   ASP B CB  1 
ATOM   3987 C  CG  . ASP B  1 98  ? -57.296 -7.935  23.875  1.00 24.35 ? 98   ASP B CG  1 
ATOM   3988 O  OD1 . ASP B  1 98  ? -57.723 -7.441  24.936  1.00 25.04 ? 98   ASP B OD1 1 
ATOM   3989 O  OD2 . ASP B  1 98  ? -56.363 -7.453  23.214  1.00 24.48 ? 98   ASP B OD2 1 
ATOM   3990 N  N   . TRP B  1 99  ? -59.803 -8.266  20.984  1.00 18.62 ? 99   TRP B N   1 
ATOM   3991 C  CA  . TRP B  1 99  ? -60.153 -7.340  19.876  1.00 17.94 ? 99   TRP B CA  1 
ATOM   3992 C  C   . TRP B  1 99  ? -61.610 -6.890  19.960  1.00 17.11 ? 99   TRP B C   1 
ATOM   3993 O  O   . TRP B  1 99  ? -61.850 -5.677  19.902  1.00 17.88 ? 99   TRP B O   1 
ATOM   3994 C  CB  . TRP B  1 99  ? -59.859 -8.024  18.545  1.00 17.27 ? 99   TRP B CB  1 
ATOM   3995 C  CG  . TRP B  1 99  ? -60.412 -7.374  17.316  1.00 17.33 ? 99   TRP B CG  1 
ATOM   3996 C  CD1 . TRP B  1 99  ? -61.388 -7.905  16.526  1.00 16.23 ? 99   TRP B CD1 1 
ATOM   3997 C  CD2 . TRP B  1 99  ? -60.025 -6.127  16.696  1.00 16.56 ? 99   TRP B CD2 1 
ATOM   3998 N  NE1 . TRP B  1 99  ? -61.651 -7.065  15.484  1.00 15.60 ? 99   TRP B NE1 1 
ATOM   3999 C  CE2 . TRP B  1 99  ? -60.816 -5.991  15.534  1.00 15.47 ? 99   TRP B CE2 1 
ATOM   4000 C  CE3 . TRP B  1 99  ? -59.141 -5.088  17.020  1.00 16.17 ? 99   TRP B CE3 1 
ATOM   4001 C  CZ2 . TRP B  1 99  ? -60.704 -4.912  14.668  1.00 14.78 ? 99   TRP B CZ2 1 
ATOM   4002 C  CZ3 . TRP B  1 99  ? -59.010 -4.027  16.148  1.00 16.47 ? 99   TRP B CZ3 1 
ATOM   4003 C  CH2 . TRP B  1 99  ? -59.773 -3.945  14.980  1.00 15.57 ? 99   TRP B CH2 1 
ATOM   4004 N  N   . LEU B  1 100 ? -62.543 -7.827  20.050  1.00 18.22 ? 100  LEU B N   1 
ATOM   4005 C  CA  . LEU B  1 100 ? -63.993 -7.494  20.055  1.00 18.72 ? 100  LEU B CA  1 
ATOM   4006 C  C   . LEU B  1 100 ? -64.320 -6.680  21.308  1.00 19.71 ? 100  LEU B C   1 
ATOM   4007 O  O   . LEU B  1 100 ? -65.161 -5.793  21.186  1.00 18.57 ? 100  LEU B O   1 
ATOM   4008 C  CB  . LEU B  1 100 ? -64.836 -8.768  19.979  1.00 19.19 ? 100  LEU B CB  1 
ATOM   4009 C  CG  . LEU B  1 100 ? -64.710 -9.560  18.675  1.00 19.75 ? 100  LEU B CG  1 
ATOM   4010 C  CD1 . LEU B  1 100 ? -65.449 -10.881 18.810  1.00 21.34 ? 100  LEU B CD1 1 
ATOM   4011 C  CD2 . LEU B  1 100 ? -65.218 -8.784  17.472  1.00 20.66 ? 100  LEU B CD2 1 
ATOM   4012 N  N   . GLY B  1 101 ? -63.645 -6.967  22.427  1.00 20.90 ? 101  GLY B N   1 
ATOM   4013 C  CA  . GLY B  1 101 ? -63.746 -6.186  23.681  1.00 20.70 ? 101  GLY B CA  1 
ATOM   4014 C  C   . GLY B  1 101 ? -63.334 -4.732  23.465  1.00 19.49 ? 101  GLY B C   1 
ATOM   4015 O  O   . GLY B  1 101 ? -64.056 -3.825  23.908  1.00 19.54 ? 101  GLY B O   1 
ATOM   4016 N  N   . LYS B  1 102 ? -62.218 -4.522  22.782  1.00 19.06 ? 102  LYS B N   1 
ATOM   4017 C  CA  . LYS B  1 102 ? -61.671 -3.178  22.525  1.00 20.10 ? 102  LYS B CA  1 
ATOM   4018 C  C   . LYS B  1 102 ? -62.594 -2.461  21.529  1.00 17.96 ? 102  LYS B C   1 
ATOM   4019 O  O   . LYS B  1 102 ? -62.892 -1.271  21.744  1.00 17.57 ? 102  LYS B O   1 
ATOM   4020 C  CB  . LYS B  1 102 ? -60.205 -3.331  22.120  1.00 22.08 ? 102  LYS B CB  1 
ATOM   4021 C  CG  . LYS B  1 102 ? -59.309 -3.698  23.297  1.00 23.89 ? 102  LYS B CG  1 
ATOM   4022 C  CD  . LYS B  1 102 ? -57.920 -4.154  22.913  1.00 26.96 ? 102  LYS B CD  1 
ATOM   4023 C  CE  . LYS B  1 102 ? -56.989 -4.184  24.110  1.00 29.46 ? 102  LYS B CE  1 
ATOM   4024 N  NZ  . LYS B  1 102 ? -55.692 -4.800  23.750  1.00 33.92 ? 102  LYS B NZ  1 
ATOM   4025 N  N   . VAL B  1 103 ? -63.060 -3.165  20.483  1.00 17.02 ? 103  VAL B N   1 
ATOM   4026 C  CA  . VAL B  1 103 ? -63.943 -2.532  19.464  1.00 16.07 ? 103  VAL B CA  1 
ATOM   4027 C  C   . VAL B  1 103 ? -65.245 -2.130  20.167  1.00 15.75 ? 103  VAL B C   1 
ATOM   4028 O  O   . VAL B  1 103 ? -65.707 -1.031  19.952  1.00 16.15 ? 103  VAL B O   1 
ATOM   4029 C  CB  . VAL B  1 103 ? -64.164 -3.433  18.230  1.00 15.34 ? 103  VAL B CB  1 
ATOM   4030 C  CG1 . VAL B  1 103 ? -65.176 -2.847  17.278  1.00 16.05 ? 103  VAL B CG1 1 
ATOM   4031 C  CG2 . VAL B  1 103 ? -62.849 -3.656  17.501  1.00 15.92 ? 103  VAL B CG2 1 
ATOM   4032 N  N   . THR B  1 104 ? -65.782 -2.989  21.024  1.00 17.38 ? 104  THR B N   1 
ATOM   4033 C  CA  . THR B  1 104 ? -67.029 -2.692  21.775  1.00 18.01 ? 104  THR B CA  1 
ATOM   4034 C  C   . THR B  1 104 ? -66.840 -1.379  22.542  1.00 18.22 ? 104  THR B C   1 
ATOM   4035 O  O   . THR B  1 104 ? -67.701 -0.495  22.493  1.00 18.86 ? 104  THR B O   1 
ATOM   4036 C  CB  . THR B  1 104 ? -67.389 -3.826  22.743  1.00 19.15 ? 104  THR B CB  1 
ATOM   4037 O  OG1 . THR B  1 104 ? -67.588 -5.038  22.011  1.00 19.21 ? 104  THR B OG1 1 
ATOM   4038 C  CG2 . THR B  1 104 ? -68.628 -3.494  23.551  1.00 19.26 ? 104  THR B CG2 1 
ATOM   4039 N  N   . SER B  1 105 ? -65.706 -1.227  23.197  1.00 21.49 ? 105  SER B N   1 
ATOM   4040 C  CA  . SER B  1 105 ? -65.429 -0.040  24.036  1.00 22.28 ? 105  SER B CA  1 
ATOM   4041 C  C   . SER B  1 105 ? -65.375 1.206   23.150  1.00 21.19 ? 105  SER B C   1 
ATOM   4042 O  O   . SER B  1 105 ? -65.978 2.229   23.521  1.00 20.45 ? 105  SER B O   1 
ATOM   4043 C  CB  . SER B  1 105 ? -64.173 -0.270  24.814  1.00 23.25 ? 105  SER B CB  1 
ATOM   4044 O  OG  . SER B  1 105 ? -63.818 0.929   25.446  1.00 26.41 ? 105  SER B OG  1 
ATOM   4045 N  N   . VAL B  1 106 ? -64.725 1.123   21.983  1.00 18.66 ? 106  VAL B N   1 
ATOM   4046 C  CA  . VAL B  1 106 ? -64.641 2.270   21.033  1.00 17.52 ? 106  VAL B CA  1 
ATOM   4047 C  C   . VAL B  1 106 ? -66.056 2.654   20.590  1.00 16.79 ? 106  VAL B C   1 
ATOM   4048 O  O   . VAL B  1 106 ? -66.372 3.864   20.453  1.00 17.06 ? 106  VAL B O   1 
ATOM   4049 C  CB  . VAL B  1 106 ? -63.729 1.921   19.835  1.00 16.49 ? 106  VAL B CB  1 
ATOM   4050 C  CG1 . VAL B  1 106 ? -63.910 2.889   18.699  1.00 16.20 ? 106  VAL B CG1 1 
ATOM   4051 C  CG2 . VAL B  1 106 ? -62.273 1.873   20.233  1.00 16.64 ? 106  VAL B CG2 1 
ATOM   4052 N  N   . ILE B  1 107 ? -66.847 1.659   20.216  1.00 16.83 ? 107  ILE B N   1 
ATOM   4053 C  CA  . ILE B  1 107 ? -68.219 1.892   19.696  1.00 15.87 ? 107  ILE B CA  1 
ATOM   4054 C  C   . ILE B  1 107 ? -69.004 2.627   20.778  1.00 16.88 ? 107  ILE B C   1 
ATOM   4055 O  O   . ILE B  1 107 ? -69.699 3.572   20.484  1.00 16.62 ? 107  ILE B O   1 
ATOM   4056 C  CB  . ILE B  1 107 ? -68.909 0.577   19.297  1.00 16.90 ? 107  ILE B CB  1 
ATOM   4057 C  CG1 . ILE B  1 107 ? -68.284 -0.043  18.039  1.00 17.03 ? 107  ILE B CG1 1 
ATOM   4058 C  CG2 . ILE B  1 107 ? -70.392 0.828   19.106  1.00 16.62 ? 107  ILE B CG2 1 
ATOM   4059 C  CD1 . ILE B  1 107 ? -68.642 -1.514  17.839  1.00 18.77 ? 107  ILE B CD1 1 
ATOM   4060 N  N   . ASN B  1 108 ? -68.914 2.132   21.991  1.00 17.94 ? 108  ASN B N   1 
ATOM   4061 C  CA  . ASN B  1 108 ? -69.630 2.730   23.146  1.00 20.41 ? 108  ASN B CA  1 
ATOM   4062 C  C   . ASN B  1 108 ? -69.170 4.177   23.350  1.00 19.86 ? 108  ASN B C   1 
ATOM   4063 O  O   . ASN B  1 108 ? -70.022 5.023   23.640  1.00 19.59 ? 108  ASN B O   1 
ATOM   4064 C  CB  . ASN B  1 108 ? -69.435 1.837   24.364  1.00 21.43 ? 108  ASN B CB  1 
ATOM   4065 C  CG  . ASN B  1 108 ? -70.356 0.638   24.273  1.00 22.32 ? 108  ASN B CG  1 
ATOM   4066 O  OD1 . ASN B  1 108 ? -71.359 0.696   23.583  1.00 25.87 ? 108  ASN B OD1 1 
ATOM   4067 N  ND2 . ASN B  1 108 ? -70.039 -0.440  24.942  1.00 25.58 ? 108  ASN B ND2 1 
ATOM   4068 N  N   . GLN B  1 109 ? -67.877 4.460   23.223  1.00 19.75 ? 109  GLN B N   1 
ATOM   4069 C  CA  . GLN B  1 109 ? -67.346 5.832   23.424  1.00 20.48 ? 109  GLN B CA  1 
ATOM   4070 C  C   . GLN B  1 109 ? -67.813 6.716   22.268  1.00 19.44 ? 109  GLN B C   1 
ATOM   4071 O  O   . GLN B  1 109 ? -68.131 7.871   22.480  1.00 17.91 ? 109  GLN B O   1 
ATOM   4072 C  CB  . GLN B  1 109 ? -65.822 5.857   23.492  1.00 22.63 ? 109  GLN B CB  1 
ATOM   4073 C  CG  . GLN B  1 109 ? -65.237 5.191   24.718  1.00 27.25 ? 109  GLN B CG  1 
ATOM   4074 C  CD  . GLN B  1 109 ? -63.772 4.909   24.477  1.00 32.03 ? 109  GLN B CD  1 
ATOM   4075 O  OE1 . GLN B  1 109 ? -63.062 5.685   23.843  1.00 41.95 ? 109  GLN B OE1 1 
ATOM   4076 N  NE2 . GLN B  1 109 ? -63.318 3.756   24.920  1.00 35.59 ? 109  GLN B NE2 1 
ATOM   4077 N  N   . LYS B  1 110 ? -67.866 6.165   21.058  1.00 17.20 ? 110  LYS B N   1 
ATOM   4078 C  CA  . LYS B  1 110 ? -68.280 6.906   19.857  1.00 16.91 ? 110  LYS B CA  1 
ATOM   4079 C  C   . LYS B  1 110 ? -69.731 7.366   20.043  1.00 16.25 ? 110  LYS B C   1 
ATOM   4080 O  O   . LYS B  1 110 ? -70.069 8.533   19.716  1.00 16.42 ? 110  LYS B O   1 
ATOM   4081 C  CB  . LYS B  1 110 ? -68.088 5.973   18.657  1.00 16.17 ? 110  LYS B CB  1 
ATOM   4082 C  CG  . LYS B  1 110 ? -68.499 6.538   17.309  1.00 16.42 ? 110  LYS B CG  1 
ATOM   4083 C  CD  . LYS B  1 110 ? -69.977 6.319   16.987  1.00 17.58 ? 110  LYS B CD  1 
ATOM   4084 C  CE  . LYS B  1 110 ? -70.357 6.559   15.545  1.00 17.87 ? 110  LYS B CE  1 
ATOM   4085 N  NZ  . LYS B  1 110 ? -71.765 6.166   15.246  1.00 19.09 ? 110  LYS B NZ  1 
ATOM   4086 N  N   . LYS B  1 111 ? -70.590 6.416   20.412  1.00 16.58 ? 111  LYS B N   1 
ATOM   4087 C  CA  . LYS B  1 111 ? -72.032 6.713   20.603  1.00 18.06 ? 111  LYS B CA  1 
ATOM   4088 C  C   . LYS B  1 111 ? -72.202 7.694   21.777  1.00 18.84 ? 111  LYS B C   1 
ATOM   4089 O  O   . LYS B  1 111 ? -73.013 8.644   21.630  1.00 18.26 ? 111  LYS B O   1 
ATOM   4090 C  CB  . LYS B  1 111 ? -72.805 5.416   20.822  1.00 19.09 ? 111  LYS B CB  1 
ATOM   4091 C  CG  . LYS B  1 111 ? -72.828 4.490   19.627  1.00 21.14 ? 111  LYS B CG  1 
ATOM   4092 C  CD  . LYS B  1 111 ? -73.901 3.425   19.728  1.00 23.67 ? 111  LYS B CD  1 
ATOM   4093 C  CE  . LYS B  1 111 ? -73.933 2.689   21.042  1.00 25.97 ? 111  LYS B CE  1 
ATOM   4094 N  NZ  . LYS B  1 111 ? -74.895 1.547   20.985  1.00 26.50 ? 111  LYS B NZ  1 
ATOM   4095 N  N   . ALA B  1 112 ? -71.467 7.493   22.867  1.00 19.41 ? 112  ALA B N   1 
ATOM   4096 C  CA  . ALA B  1 112 ? -71.555 8.339   24.088  1.00 21.25 ? 112  ALA B CA  1 
ATOM   4097 C  C   . ALA B  1 112 ? -71.094 9.759   23.782  1.00 22.20 ? 112  ALA B C   1 
ATOM   4098 O  O   . ALA B  1 112 ? -71.597 10.671  24.424  1.00 22.35 ? 112  ALA B O   1 
ATOM   4099 C  CB  . ALA B  1 112 ? -70.772 7.736   25.235  1.00 21.91 ? 112  ALA B CB  1 
ATOM   4100 N  N   . SER B  1 113 ? -70.187 9.976   22.826  1.00 20.20 ? 113  SER B N   1 
ATOM   4101 C  CA  . SER B  1 113 ? -69.628 11.322  22.528  1.00 20.12 ? 113  SER B CA  1 
ATOM   4102 C  C   . SER B  1 113 ? -70.738 12.281  22.081  1.00 22.01 ? 113  SER B C   1 
ATOM   4103 O  O   . SER B  1 113 ? -70.581 13.505  22.288  1.00 23.00 ? 113  SER B O   1 
ATOM   4104 C  CB  . SER B  1 113 ? -68.533 11.228  21.470  1.00 20.10 ? 113  SER B CB  1 
ATOM   4105 O  OG  . SER B  1 113 ? -69.113 11.081  20.181  1.00 18.73 ? 113  SER B OG  1 
ATOM   4106 N  N   . GLY B  1 114 ? -71.759 11.739  21.418  1.00 21.92 ? 114  GLY B N   1 
ATOM   4107 C  CA  . GLY B  1 114 ? -72.900 12.456  20.829  1.00 23.95 ? 114  GLY B CA  1 
ATOM   4108 C  C   . GLY B  1 114 ? -72.570 13.127  19.508  1.00 23.14 ? 114  GLY B C   1 
ATOM   4109 O  O   . GLY B  1 114 ? -73.484 13.760  18.933  1.00 24.68 ? 114  GLY B O   1 
ATOM   4110 N  N   . TYR B  1 115 ? -71.321 13.073  19.033  1.00 21.43 ? 115  TYR B N   1 
ATOM   4111 C  CA  . TYR B  1 115 ? -70.963 13.752  17.770  1.00 20.61 ? 115  TYR B CA  1 
ATOM   4112 C  C   . TYR B  1 115 ? -71.644 13.016  16.619  1.00 18.98 ? 115  TYR B C   1 
ATOM   4113 O  O   . TYR B  1 115 ? -71.743 11.786  16.666  1.00 18.25 ? 115  TYR B O   1 
ATOM   4114 C  CB  . TYR B  1 115 ? -69.445 13.821  17.607  1.00 21.73 ? 115  TYR B CB  1 
ATOM   4115 C  CG  . TYR B  1 115 ? -68.710 14.439  18.774  1.00 22.30 ? 115  TYR B CG  1 
ATOM   4116 C  CD1 . TYR B  1 115 ? -69.225 15.536  19.441  1.00 23.70 ? 115  TYR B CD1 1 
ATOM   4117 C  CD2 . TYR B  1 115 ? -67.480 13.958  19.182  1.00 22.23 ? 115  TYR B CD2 1 
ATOM   4118 C  CE1 . TYR B  1 115 ? -68.531 16.134  20.482  1.00 23.91 ? 115  TYR B CE1 1 
ATOM   4119 C  CE2 . TYR B  1 115 ? -66.757 14.555  20.201  1.00 22.05 ? 115  TYR B CE2 1 
ATOM   4120 C  CZ  . TYR B  1 115 ? -67.299 15.643  20.864  1.00 23.75 ? 115  TYR B CZ  1 
ATOM   4121 O  OH  . TYR B  1 115 ? -66.631 16.231  21.899  1.00 23.85 ? 115  TYR B OH  1 
ATOM   4122 N  N   . SER B  1 116 ? -72.117 13.768  15.642  1.00 18.53 ? 116  SER B N   1 
ATOM   4123 C  CA  . SER B  1 116 ? -72.853 13.230  14.485  1.00 19.73 ? 116  SER B CA  1 
ATOM   4124 C  C   . SER B  1 116 ? -71.987 13.316  13.221  1.00 19.18 ? 116  SER B C   1 
ATOM   4125 O  O   . SER B  1 116 ? -72.531 13.165  12.130  1.00 20.53 ? 116  SER B O   1 
ATOM   4126 C  CB  . SER B  1 116 ? -74.161 13.976  14.346  1.00 21.00 ? 116  SER B CB  1 
ATOM   4127 O  OG  . SER B  1 116 ? -73.931 15.321  13.994  1.00 26.21 ? 116  SER B OG  1 
ATOM   4128 N  N   . ASN B  1 117 ? -70.671 13.538  13.359  1.00 18.77 ? 117  ASN B N   1 
ATOM   4129 C  CA  . ASN B  1 117 ? -69.785 13.688  12.170  1.00 16.64 ? 117  ASN B CA  1 
ATOM   4130 C  C   . ASN B  1 117 ? -68.851 12.470  12.030  1.00 16.99 ? 117  ASN B C   1 
ATOM   4131 O  O   . ASN B  1 117 ? -67.717 12.650  11.575  1.00 16.57 ? 117  ASN B O   1 
ATOM   4132 C  CB  . ASN B  1 117 ? -69.014 15.005  12.217  1.00 16.46 ? 117  ASN B CB  1 
ATOM   4133 C  CG  . ASN B  1 117 ? -68.134 15.186  13.424  1.00 17.41 ? 117  ASN B CG  1 
ATOM   4134 O  OD1 . ASN B  1 117 ? -68.376 14.606  14.462  1.00 17.31 ? 117  ASN B OD1 1 
ATOM   4135 N  ND2 . ASN B  1 117 ? -67.075 15.972  13.284  1.00 15.39 ? 117  ASN B ND2 1 
ATOM   4136 N  N   . PHE B  1 118 ? -69.307 11.276  12.394  1.00 14.72 ? 118  PHE B N   1 
ATOM   4137 C  CA  . PHE B  1 118 ? -68.526 10.033  12.142  1.00 14.69 ? 118  PHE B CA  1 
ATOM   4138 C  C   . PHE B  1 118 ? -68.953 9.489   10.777  1.00 15.57 ? 118  PHE B C   1 
ATOM   4139 O  O   . PHE B  1 118 ? -70.164 9.483   10.448  1.00 17.50 ? 118  PHE B O   1 
ATOM   4140 C  CB  . PHE B  1 118 ? -68.695 9.025   13.267  1.00 14.45 ? 118  PHE B CB  1 
ATOM   4141 C  CG  . PHE B  1 118 ? -68.106 9.478   14.577  1.00 14.95 ? 118  PHE B CG  1 
ATOM   4142 C  CD1 . PHE B  1 118 ? -66.724 9.512   14.754  1.00 15.27 ? 118  PHE B CD1 1 
ATOM   4143 C  CD2 . PHE B  1 118 ? -68.929 9.894   15.613  1.00 14.98 ? 118  PHE B CD2 1 
ATOM   4144 C  CE1 . PHE B  1 118 ? -66.181 9.955   15.950  1.00 16.33 ? 118  PHE B CE1 1 
ATOM   4145 C  CE2 . PHE B  1 118 ? -68.384 10.314  16.824  1.00 15.44 ? 118  PHE B CE2 1 
ATOM   4146 C  CZ  . PHE B  1 118 ? -67.015 10.381  16.973  1.00 15.41 ? 118  PHE B CZ  1 
ATOM   4147 N  N   . TYR B  1 119 ? -67.982 9.096   9.967   1.00 15.06 ? 119  TYR B N   1 
ATOM   4148 C  CA  . TYR B  1 119 ? -68.208 8.592   8.589   1.00 14.01 ? 119  TYR B CA  1 
ATOM   4149 C  C   . TYR B  1 119 ? -68.490 7.098   8.683   1.00 14.70 ? 119  TYR B C   1 
ATOM   4150 O  O   . TYR B  1 119 ? -69.258 6.573   7.833   1.00 17.07 ? 119  TYR B O   1 
ATOM   4151 C  CB  . TYR B  1 119 ? -66.973 8.850   7.730   1.00 12.96 ? 119  TYR B CB  1 
ATOM   4152 C  CG  . TYR B  1 119 ? -67.041 8.385   6.302   1.00 12.23 ? 119  TYR B CG  1 
ATOM   4153 C  CD1 . TYR B  1 119 ? -67.798 9.043   5.365   1.00 12.15 ? 119  TYR B CD1 1 
ATOM   4154 C  CD2 . TYR B  1 119 ? -66.287 7.313   5.868   1.00 11.63 ? 119  TYR B CD2 1 
ATOM   4155 C  CE1 . TYR B  1 119 ? -67.794 8.695   4.025   1.00 12.74 ? 119  TYR B CE1 1 
ATOM   4156 C  CE2 . TYR B  1 119 ? -66.289 6.934   4.537   1.00 12.50 ? 119  TYR B CE2 1 
ATOM   4157 C  CZ  . TYR B  1 119 ? -67.045 7.613   3.607   1.00 11.96 ? 119  TYR B CZ  1 
ATOM   4158 O  OH  . TYR B  1 119 ? -67.022 7.289   2.272   1.00 13.86 ? 119  TYR B OH  1 
ATOM   4159 N  N   . GLY B  1 120 ? -67.880 6.433   9.670   1.00 13.77 ? 120  GLY B N   1 
ATOM   4160 C  CA  . GLY B  1 120 ? -68.119 5.003   9.906   1.00 12.96 ? 120  GLY B CA  1 
ATOM   4161 C  C   . GLY B  1 120 ? -66.890 4.335   10.440  1.00 12.70 ? 120  GLY B C   1 
ATOM   4162 O  O   . GLY B  1 120 ? -65.925 5.035   10.790  1.00 11.15 ? 120  GLY B O   1 
ATOM   4163 N  N   . TYR B  1 121 ? -66.886 3.015   10.454  1.00 11.90 ? 121  TYR B N   1 
ATOM   4164 C  CA  . TYR B  1 121 ? -65.799 2.227   11.064  1.00 12.41 ? 121  TYR B CA  1 
ATOM   4165 C  C   . TYR B  1 121 ? -65.045 1.479   9.974   1.00 12.15 ? 121  TYR B C   1 
ATOM   4166 O  O   . TYR B  1 121 ? -65.668 0.783   9.180   1.00 12.39 ? 121  TYR B O   1 
ATOM   4167 C  CB  . TYR B  1 121 ? -66.395 1.175   12.002  1.00 12.74 ? 121  TYR B CB  1 
ATOM   4168 C  CG  . TYR B  1 121 ? -67.162 1.732   13.163  1.00 13.20 ? 121  TYR B CG  1 
ATOM   4169 C  CD1 . TYR B  1 121 ? -66.535 1.995   14.367  1.00 13.67 ? 121  TYR B CD1 1 
ATOM   4170 C  CD2 . TYR B  1 121 ? -68.538 1.923   13.080  1.00 13.53 ? 121  TYR B CD2 1 
ATOM   4171 C  CE1 . TYR B  1 121 ? -67.234 2.518   15.446  1.00 13.38 ? 121  TYR B CE1 1 
ATOM   4172 C  CE2 . TYR B  1 121 ? -69.255 2.404   14.156  1.00 13.42 ? 121  TYR B CE2 1 
ATOM   4173 C  CZ  . TYR B  1 121 ? -68.603 2.714   15.339  1.00 13.32 ? 121  TYR B CZ  1 
ATOM   4174 O  OH  . TYR B  1 121 ? -69.298 3.170   16.414  1.00 14.62 ? 121  TYR B OH  1 
ATOM   4175 N  N   . GLU B  1 122 ? -63.730 1.647   9.924   1.00 12.04 ? 122  GLU B N   1 
ATOM   4176 C  CA  . GLU B  1 122 ? -62.839 0.785   9.105   1.00 12.08 ? 122  GLU B CA  1 
ATOM   4177 C  C   . GLU B  1 122 ? -62.430 -0.411  9.978   1.00 11.91 ? 122  GLU B C   1 
ATOM   4178 O  O   . GLU B  1 122 ? -61.717 -0.220  10.962  1.00 11.69 ? 122  GLU B O   1 
ATOM   4179 C  CB  . GLU B  1 122 ? -61.659 1.636   8.611   1.00 11.88 ? 122  GLU B CB  1 
ATOM   4180 C  CG  . GLU B  1 122 ? -60.685 0.865   7.751   1.00 11.99 ? 122  GLU B CG  1 
ATOM   4181 C  CD  . GLU B  1 122 ? -59.343 1.559   7.646   1.00 12.01 ? 122  GLU B CD  1 
ATOM   4182 O  OE1 . GLU B  1 122 ? -58.717 1.741   8.729   1.00 13.06 ? 122  GLU B OE1 1 
ATOM   4183 O  OE2 . GLU B  1 122 ? -58.939 1.911   6.503   1.00 12.70 ? 122  GLU B OE2 1 
ATOM   4184 N  N   . ILE B  1 123 ? -62.892 -1.613  9.658   1.00 11.85 ? 123  ILE B N   1 
ATOM   4185 C  CA  . ILE B  1 123 ? -62.599 -2.832  10.468  1.00 11.72 ? 123  ILE B CA  1 
ATOM   4186 C  C   . ILE B  1 123 ? -61.089 -3.099  10.535  1.00 11.64 ? 123  ILE B C   1 
ATOM   4187 O  O   . ILE B  1 123 ? -60.606 -3.401  11.635  1.00 11.53 ? 123  ILE B O   1 
ATOM   4188 C  CB  . ILE B  1 123 ? -63.389 -4.030  9.928   1.00 12.24 ? 123  ILE B CB  1 
ATOM   4189 C  CG1 . ILE B  1 123 ? -64.879 -3.848  10.235  1.00 12.27 ? 123  ILE B CG1 1 
ATOM   4190 C  CG2 . ILE B  1 123 ? -62.856 -5.345  10.489  1.00 12.86 ? 123  ILE B CG2 1 
ATOM   4191 C  CD1 . ILE B  1 123 ? -65.795 -4.912  9.668   1.00 12.71 ? 123  ILE B CD1 1 
ATOM   4192 N  N   . TRP B  1 124 ? -60.383 -2.971  9.418   1.00 11.81 ? 124  TRP B N   1 
ATOM   4193 C  CA  . TRP B  1 124 ? -58.932 -3.231  9.370   1.00 12.28 ? 124  TRP B CA  1 
ATOM   4194 C  C   . TRP B  1 124 ? -58.260 -2.363  8.313   1.00 11.98 ? 124  TRP B C   1 
ATOM   4195 O  O   . TRP B  1 124 ? -58.949 -1.748  7.468   1.00 13.75 ? 124  TRP B O   1 
ATOM   4196 C  CB  . TRP B  1 124 ? -58.662 -4.738  9.162   1.00 12.32 ? 124  TRP B CB  1 
ATOM   4197 C  CG  . TRP B  1 124 ? -57.318 -5.135  9.707   1.00 12.99 ? 124  TRP B CG  1 
ATOM   4198 C  CD1 . TRP B  1 124 ? -56.162 -5.306  9.001   1.00 13.49 ? 124  TRP B CD1 1 
ATOM   4199 C  CD2 . TRP B  1 124 ? -56.984 -5.365  11.094  1.00 13.52 ? 124  TRP B CD2 1 
ATOM   4200 N  NE1 . TRP B  1 124 ? -55.136 -5.614  9.855   1.00 12.69 ? 124  TRP B NE1 1 
ATOM   4201 C  CE2 . TRP B  1 124 ? -55.595 -5.632  11.147  1.00 12.94 ? 124  TRP B CE2 1 
ATOM   4202 C  CE3 . TRP B  1 124 ? -57.711 -5.345  12.305  1.00 14.29 ? 124  TRP B CE3 1 
ATOM   4203 C  CZ2 . TRP B  1 124 ? -54.939 -5.948  12.338  1.00 14.44 ? 124  TRP B CZ2 1 
ATOM   4204 C  CZ3 . TRP B  1 124 ? -57.063 -5.638  13.489  1.00 14.47 ? 124  TRP B CZ3 1 
ATOM   4205 C  CH2 . TRP B  1 124 ? -55.689 -5.941  13.505  1.00 14.64 ? 124  TRP B CH2 1 
ATOM   4206 N  N   . ASN B  1 125 ? -56.932 -2.302  8.392   1.00 12.08 ? 125  ASN B N   1 
ATOM   4207 C  CA  . ASN B  1 125 ? -56.103 -1.450  7.515   1.00 12.05 ? 125  ASN B CA  1 
ATOM   4208 C  C   . ASN B  1 125 ? -55.075 -2.331  6.808   1.00 11.84 ? 125  ASN B C   1 
ATOM   4209 O  O   . ASN B  1 125 ? -54.316 -3.028  7.506   1.00 13.58 ? 125  ASN B O   1 
ATOM   4210 C  CB  . ASN B  1 125 ? -55.452 -0.339  8.335   1.00 12.18 ? 125  ASN B CB  1 
ATOM   4211 C  CG  . ASN B  1 125 ? -54.522 0.463   7.480   1.00 12.73 ? 125  ASN B CG  1 
ATOM   4212 O  OD1 . ASN B  1 125 ? -54.863 0.694   6.311   1.00 12.03 ? 125  ASN B OD1 1 
ATOM   4213 N  ND2 . ASN B  1 125 ? -53.338 0.779   8.028   1.00 12.78 ? 125  ASN B ND2 1 
ATOM   4214 N  N   . GLU B  1 126 ? -55.090 -2.344  5.474   1.00 12.08 ? 126  GLU B N   1 
ATOM   4215 C  CA  . GLU B  1 126 ? -54.105 -3.086  4.636   1.00 12.00 ? 126  GLU B CA  1 
ATOM   4216 C  C   . GLU B  1 126 ? -53.956 -4.540  5.095   1.00 12.34 ? 126  GLU B C   1 
ATOM   4217 O  O   . GLU B  1 126 ? -52.831 -5.006  5.321   1.00 13.00 ? 126  GLU B O   1 
ATOM   4218 C  CB  . GLU B  1 126 ? -52.768 -2.339  4.643   1.00 11.76 ? 126  GLU B CB  1 
ATOM   4219 C  CG  . GLU B  1 126 ? -52.873 -0.934  4.095   1.00 11.98 ? 126  GLU B CG  1 
ATOM   4220 C  CD  . GLU B  1 126 ? -51.628 -0.255  3.562   1.00 11.77 ? 126  GLU B CD  1 
ATOM   4221 O  OE1 . GLU B  1 126 ? -50.546 -0.768  3.786   1.00 14.01 ? 126  GLU B OE1 1 
ATOM   4222 O  OE2 . GLU B  1 126 ? -51.774 0.787   2.899   1.00 14.21 ? 126  GLU B OE2 1 
ATOM   4223 N  N   . PRO B  1 127 ? -55.047 -5.314  5.230   1.00 11.69 ? 127  PRO B N   1 
ATOM   4224 C  CA  . PRO B  1 127 ? -54.939 -6.698  5.697   1.00 12.08 ? 127  PRO B CA  1 
ATOM   4225 C  C   . PRO B  1 127 ? -54.096 -7.575  4.770   1.00 13.26 ? 127  PRO B C   1 
ATOM   4226 O  O   . PRO B  1 127 ? -53.531 -8.558  5.232   1.00 14.13 ? 127  PRO B O   1 
ATOM   4227 C  CB  . PRO B  1 127 ? -56.385 -7.194  5.700   1.00 12.22 ? 127  PRO B CB  1 
ATOM   4228 C  CG  . PRO B  1 127 ? -57.082 -6.287  4.732   1.00 12.13 ? 127  PRO B CG  1 
ATOM   4229 C  CD  . PRO B  1 127 ? -56.441 -4.936  4.955   1.00 11.37 ? 127  PRO B CD  1 
ATOM   4230 N  N   . ASP B  1 128 ? -53.980 -7.200  3.505   1.00 13.03 ? 128  ASP B N   1 
ATOM   4231 C  CA  . ASP B  1 128 ? -53.132 -7.905  2.516   1.00 15.17 ? 128  ASP B CA  1 
ATOM   4232 C  C   . ASP B  1 128 ? -51.671 -7.867  2.993   1.00 17.87 ? 128  ASP B C   1 
ATOM   4233 O  O   . ASP B  1 128 ? -50.938 -8.794  2.680   1.00 19.13 ? 128  ASP B O   1 
ATOM   4234 C  CB  . ASP B  1 128 ? -53.341 -7.309  1.119   1.00 15.58 ? 128  ASP B CB  1 
ATOM   4235 C  CG  . ASP B  1 128 ? -53.047 -5.826  0.989   1.00 15.57 ? 128  ASP B CG  1 
ATOM   4236 O  OD1 . ASP B  1 128 ? -53.552 -5.063  1.815   1.00 13.18 ? 128  ASP B OD1 1 
ATOM   4237 O  OD2 . ASP B  1 128 ? -52.313 -5.457  0.056   1.00 18.23 ? 128  ASP B OD2 1 
ATOM   4238 N  N   . GLY B  1 129 ? -51.281 -6.841  3.750   1.00 17.12 ? 129  GLY B N   1 
ATOM   4239 C  CA  . GLY B  1 129 ? -49.926 -6.692  4.322   1.00 18.27 ? 129  GLY B CA  1 
ATOM   4240 C  C   . GLY B  1 129 ? -49.894 -7.011  5.804   1.00 18.84 ? 129  GLY B C   1 
ATOM   4241 O  O   . GLY B  1 129 ? -48.811 -7.395  6.280   1.00 20.51 ? 129  GLY B O   1 
ATOM   4242 N  N   . THR B  1 130 ? -50.996 -6.826  6.540   1.00 17.71 ? 130  THR B N   1 
ATOM   4243 C  CA  . THR B  1 130 ? -50.942 -6.768  8.019   1.00 16.91 ? 130  THR B CA  1 
ATOM   4244 C  C   . THR B  1 130 ? -51.812 -7.832  8.703   1.00 19.78 ? 130  THR B C   1 
ATOM   4245 O  O   . THR B  1 130 ? -51.792 -7.809  9.924   1.00 20.38 ? 130  THR B O   1 
ATOM   4246 C  CB  . THR B  1 130 ? -51.289 -5.371  8.552   1.00 16.73 ? 130  THR B CB  1 
ATOM   4247 O  OG1 . THR B  1 130 ? -52.694 -5.177  8.335   1.00 15.71 ? 130  THR B OG1 1 
ATOM   4248 C  CG2 . THR B  1 130 ? -50.437 -4.258  7.965   1.00 15.95 ? 130  THR B CG2 1 
ATOM   4249 N  N   . PHE B  1 131 ? -52.588 -8.667  7.998   1.00 19.62 ? 131  PHE B N   1 
ATOM   4250 C  CA  . PHE B  1 131 ? -53.441 -9.722  8.608   1.00 22.15 ? 131  PHE B CA  1 
ATOM   4251 C  C   . PHE B  1 131 ? -53.292 -11.043 7.836   1.00 25.47 ? 131  PHE B C   1 
ATOM   4252 O  O   . PHE B  1 131 ? -54.291 -11.582 7.290   1.00 25.19 ? 131  PHE B O   1 
ATOM   4253 C  CB  . PHE B  1 131 ? -54.918 -9.315  8.689   1.00 19.17 ? 131  PHE B CB  1 
ATOM   4254 C  CG  . PHE B  1 131 ? -55.610 -9.889  9.900   1.00 19.15 ? 131  PHE B CG  1 
ATOM   4255 C  CD1 . PHE B  1 131 ? -55.890 -11.245 9.977   1.00 18.91 ? 131  PHE B CD1 1 
ATOM   4256 C  CD2 . PHE B  1 131 ? -55.896 -9.105  11.010  1.00 19.05 ? 131  PHE B CD2 1 
ATOM   4257 C  CE1 . PHE B  1 131 ? -56.513 -11.786 11.096  1.00 18.25 ? 131  PHE B CE1 1 
ATOM   4258 C  CE2 . PHE B  1 131 ? -56.539 -9.645  12.118  1.00 18.76 ? 131  PHE B CE2 1 
ATOM   4259 C  CZ  . PHE B  1 131 ? -56.836 -10.985 12.162  1.00 18.51 ? 131  PHE B CZ  1 
ATOM   4260 N  N   . LYS B  1 132 ? -52.068 -11.540 7.810   1.00 30.99 ? 132  LYS B N   1 
ATOM   4261 C  CA  . LYS B  1 132 ? -51.651 -12.720 7.011   1.00 37.72 ? 132  LYS B CA  1 
ATOM   4262 C  C   . LYS B  1 132 ? -51.395 -13.927 7.924   1.00 40.99 ? 132  LYS B C   1 
ATOM   4263 O  O   . LYS B  1 132 ? -51.631 -15.074 7.429   1.00 40.12 ? 132  LYS B O   1 
ATOM   4264 C  CB  . LYS B  1 132 ? -50.407 -12.393 6.178   1.00 41.91 ? 132  LYS B CB  1 
ATOM   4265 C  CG  . LYS B  1 132 ? -50.681 -11.916 4.756   1.00 46.55 ? 132  LYS B CG  1 
ATOM   4266 C  CD  . LYS B  1 132 ? -49.416 -11.663 3.951   1.00 50.08 ? 132  LYS B CD  1 
ATOM   4267 C  CE  . LYS B  1 132 ? -48.696 -10.399 4.372   1.00 52.06 ? 132  LYS B CE  1 
ATOM   4268 N  NZ  . LYS B  1 132 ? -47.231 -10.538 4.232   1.00 56.20 ? 132  LYS B NZ  1 
ATOM   4269 N  N   . ASN B  1 133 ? -51.002 -13.698 9.190   1.00 40.55 ? 133  ASN B N   1 
ATOM   4270 C  CA  . ASN B  1 133 ? -50.242 -14.685 10.005  1.00 46.82 ? 133  ASN B CA  1 
ATOM   4271 C  C   . ASN B  1 133 ? -50.883 -14.984 11.371  1.00 44.99 ? 133  ASN B C   1 
ATOM   4272 O  O   . ASN B  1 133 ? -50.277 -15.741 12.145  1.00 47.71 ? 133  ASN B O   1 
ATOM   4273 C  CB  . ASN B  1 133 ? -48.813 -14.170 10.160  1.00 50.05 ? 133  ASN B CB  1 
ATOM   4274 C  CG  . ASN B  1 133 ? -48.155 -13.954 8.808   1.00 53.92 ? 133  ASN B CG  1 
ATOM   4275 O  OD1 . ASN B  1 133 ? -48.359 -14.748 7.892   1.00 50.84 ? 133  ASN B OD1 1 
ATOM   4276 N  ND2 . ASN B  1 133 ? -47.384 -12.886 8.659   1.00 53.90 ? 133  ASN B ND2 1 
ATOM   4277 N  N   . ASN B  1 134 ? -52.072 -14.464 11.660  1.00 37.44 ? 134  ASN B N   1 
ATOM   4278 C  CA  . ASN B  1 134 ? -52.641 -14.431 13.037  1.00 34.58 ? 134  ASN B CA  1 
ATOM   4279 C  C   . ASN B  1 134 ? -53.313 -15.767 13.392  1.00 32.63 ? 134  ASN B C   1 
ATOM   4280 O  O   . ASN B  1 134 ? -53.450 -16.627 12.512  1.00 34.09 ? 134  ASN B O   1 
ATOM   4281 C  CB  . ASN B  1 134 ? -53.549 -13.202 13.180  1.00 31.17 ? 134  ASN B CB  1 
ATOM   4282 C  CG  . ASN B  1 134 ? -52.756 -11.910 13.093  1.00 31.46 ? 134  ASN B CG  1 
ATOM   4283 O  OD1 . ASN B  1 134 ? -51.625 -11.853 13.546  1.00 34.32 ? 134  ASN B OD1 1 
ATOM   4284 N  ND2 . ASN B  1 134 ? -53.303 -10.878 12.485  1.00 24.83 ? 134  ASN B ND2 1 
ATOM   4285 N  N   . ASN B  1 135 ? -53.769 -15.900 14.644  1.00 34.61 ? 135  ASN B N   1 
ATOM   4286 C  CA  . ASN B  1 135 ? -54.385 -17.137 15.217  1.00 36.99 ? 135  ASN B CA  1 
ATOM   4287 C  C   . ASN B  1 135 ? -55.800 -17.340 14.647  1.00 32.66 ? 135  ASN B C   1 
ATOM   4288 O  O   . ASN B  1 135 ? -56.387 -18.395 14.866  1.00 34.54 ? 135  ASN B O   1 
ATOM   4289 C  CB  . ASN B  1 135 ? -54.427 -17.079 16.753  1.00 43.55 ? 135  ASN B CB  1 
ATOM   4290 C  CG  . ASN B  1 135 ? -55.046 -15.805 17.317  1.00 49.18 ? 135  ASN B CG  1 
ATOM   4291 O  OD1 . ASN B  1 135 ? -56.084 -15.341 16.841  1.00 49.67 ? 135  ASN B OD1 1 
ATOM   4292 N  ND2 . ASN B  1 135 ? -54.436 -15.244 18.355  1.00 43.49 ? 135  ASN B ND2 1 
ATOM   4293 N  N   . VAL B  1 136 ? -56.333 -16.319 13.975  1.00 29.84 ? 136  VAL B N   1 
ATOM   4294 C  CA  . VAL B  1 136 ? -57.657 -16.312 13.292  1.00 26.54 ? 136  VAL B CA  1 
ATOM   4295 C  C   . VAL B  1 136 ? -57.392 -15.831 11.863  1.00 21.44 ? 136  VAL B C   1 
ATOM   4296 O  O   . VAL B  1 136 ? -56.401 -15.141 11.644  1.00 21.33 ? 136  VAL B O   1 
ATOM   4297 C  CB  . VAL B  1 136 ? -58.632 -15.400 14.059  1.00 29.72 ? 136  VAL B CB  1 
ATOM   4298 C  CG1 . VAL B  1 136 ? -58.077 -13.994 14.238  1.00 29.94 ? 136  VAL B CG1 1 
ATOM   4299 C  CG2 . VAL B  1 136 ? -59.994 -15.329 13.399  1.00 32.80 ? 136  VAL B CG2 1 
ATOM   4300 N  N   . SER B  1 137 ? -58.239 -16.172 10.912  1.00 18.36 ? 137  SER B N   1 
ATOM   4301 C  CA  . SER B  1 137 ? -58.114 -15.663 9.529   1.00 17.93 ? 137  SER B CA  1 
ATOM   4302 C  C   . SER B  1 137 ? -58.614 -14.214 9.505   1.00 15.82 ? 137  SER B C   1 
ATOM   4303 O  O   . SER B  1 137 ? -59.425 -13.848 10.370  1.00 16.18 ? 137  SER B O   1 
ATOM   4304 C  CB  . SER B  1 137 ? -58.901 -16.522 8.572   1.00 17.30 ? 137  SER B CB  1 
ATOM   4305 O  OG  . SER B  1 137 ? -60.288 -16.450 8.851   1.00 17.05 ? 137  SER B OG  1 
ATOM   4306 N  N   . PHE B  1 138 ? -58.204 -13.464 8.493   1.00 17.03 ? 138  PHE B N   1 
ATOM   4307 C  CA  . PHE B  1 138 ? -58.744 -12.117 8.206   1.00 15.03 ? 138  PHE B CA  1 
ATOM   4308 C  C   . PHE B  1 138 ? -60.255 -12.213 8.027   1.00 15.56 ? 138  PHE B C   1 
ATOM   4309 O  O   . PHE B  1 138 ? -61.003 -11.436 8.662   1.00 14.10 ? 138  PHE B O   1 
ATOM   4310 C  CB  . PHE B  1 138 ? -58.062 -11.496 6.998   1.00 15.76 ? 138  PHE B CB  1 
ATOM   4311 C  CG  . PHE B  1 138 ? -58.776 -10.254 6.560   1.00 17.04 ? 138  PHE B CG  1 
ATOM   4312 C  CD1 . PHE B  1 138 ? -58.804 -9.136  7.384   1.00 16.41 ? 138  PHE B CD1 1 
ATOM   4313 C  CD2 . PHE B  1 138 ? -59.469 -10.221 5.366   1.00 17.55 ? 138  PHE B CD2 1 
ATOM   4314 C  CE1 . PHE B  1 138 ? -59.532 -8.018  7.017   1.00 15.94 ? 138  PHE B CE1 1 
ATOM   4315 C  CE2 . PHE B  1 138 ? -60.133 -9.069  4.974   1.00 18.35 ? 138  PHE B CE2 1 
ATOM   4316 C  CZ  . PHE B  1 138 ? -60.155 -7.974  5.801   1.00 16.39 ? 138  PHE B CZ  1 
ATOM   4317 N  N   . ASN B  1 139 ? -60.702 -13.191 7.230   1.00 14.67 ? 139  ASN B N   1 
ATOM   4318 C  CA  . ASN B  1 139 ? -62.141 -13.365 6.911   1.00 15.30 ? 139  ASN B CA  1 
ATOM   4319 C  C   . ASN B  1 139 ? -62.968 -13.530 8.188   1.00 15.22 ? 139  ASN B C   1 
ATOM   4320 O  O   . ASN B  1 139 ? -64.072 -12.939 8.263   1.00 15.66 ? 139  ASN B O   1 
ATOM   4321 C  CB  . ASN B  1 139 ? -62.335 -14.487 5.887   1.00 16.96 ? 139  ASN B CB  1 
ATOM   4322 C  CG  . ASN B  1 139 ? -61.988 -14.043 4.477   1.00 16.84 ? 139  ASN B CG  1 
ATOM   4323 O  OD1 . ASN B  1 139 ? -61.733 -12.876 4.196   1.00 21.65 ? 139  ASN B OD1 1 
ATOM   4324 N  ND2 . ASN B  1 139 ? -61.964 -14.993 3.572   1.00 24.10 ? 139  ASN B ND2 1 
ATOM   4325 N  N   A ASP B  1 140 ? -62.492 -14.338 9.132   0.50 15.42 ? 140  ASP B N   1 
ATOM   4326 N  N   B ASP B  1 140 ? -62.486 -14.342 9.130   0.50 15.58 ? 140  ASP B N   1 
ATOM   4327 C  CA  A ASP B  1 140 ? -63.226 -14.625 10.391  0.50 16.59 ? 140  ASP B CA  1 
ATOM   4328 C  CA  B ASP B  1 140 ? -63.200 -14.663 10.396  0.50 16.87 ? 140  ASP B CA  1 
ATOM   4329 C  C   A ASP B  1 140 ? -63.244 -13.376 11.275  0.50 15.40 ? 140  ASP B C   1 
ATOM   4330 C  C   B ASP B  1 140 ? -63.225 -13.418 11.297  0.50 15.56 ? 140  ASP B C   1 
ATOM   4331 O  O   A ASP B  1 140 ? -64.316 -13.030 11.800  0.50 15.44 ? 140  ASP B O   1 
ATOM   4332 O  O   B ASP B  1 140 ? -64.290 -13.110 11.854  0.50 15.74 ? 140  ASP B O   1 
ATOM   4333 C  CB  A ASP B  1 140 ? -62.604 -15.802 11.126  0.50 17.24 ? 140  ASP B CB  1 
ATOM   4334 C  CB  B ASP B  1 140 ? -62.552 -15.866 11.078  0.50 17.77 ? 140  ASP B CB  1 
ATOM   4335 C  CG  A ASP B  1 140 ? -62.863 -17.103 10.399  0.50 18.46 ? 140  ASP B CG  1 
ATOM   4336 C  CG  B ASP B  1 140 ? -63.216 -16.330 12.366  0.50 19.51 ? 140  ASP B CG  1 
ATOM   4337 O  OD1 A ASP B  1 140 ? -64.036 -17.341 10.004  0.50 20.15 ? 140  ASP B OD1 1 
ATOM   4338 O  OD1 B ASP B  1 140 ? -64.437 -16.141 12.533  0.50 20.61 ? 140  ASP B OD1 1 
ATOM   4339 O  OD2 A ASP B  1 140 ? -61.895 -17.856 10.229  0.50 20.32 ? 140  ASP B OD2 1 
ATOM   4340 O  OD2 B ASP B  1 140 ? -62.489 -16.877 13.197  0.50 20.45 ? 140  ASP B OD2 1 
ATOM   4341 N  N   . MET B  1 141 ? -62.097 -12.717 11.412  1.00 15.06 ? 141  MET B N   1 
ATOM   4342 C  CA  . MET B  1 141 ? -62.005 -11.449 12.169  1.00 15.20 ? 141  MET B CA  1 
ATOM   4343 C  C   . MET B  1 141 ? -62.987 -10.460 11.524  1.00 13.61 ? 141  MET B C   1 
ATOM   4344 O  O   . MET B  1 141 ? -63.799 -9.847  12.253  1.00 13.04 ? 141  MET B O   1 
ATOM   4345 C  CB  . MET B  1 141 ? -60.571 -10.908 12.129  1.00 14.95 ? 141  MET B CB  1 
ATOM   4346 C  CG  . MET B  1 141 ? -60.338 -9.621  12.886  1.00 15.91 ? 141  MET B CG  1 
ATOM   4347 S  SD  . MET B  1 141 ? -60.911 -8.131  12.046  1.00 16.08 ? 141  MET B SD  1 
ATOM   4348 C  CE  . MET B  1 141 ? -59.834 -8.209  10.623  1.00 16.79 ? 141  MET B CE  1 
ATOM   4349 N  N   . TRP B  1 142 ? -62.951 -10.329 10.200  1.00 13.00 ? 142  TRP B N   1 
ATOM   4350 C  CA  . TRP B  1 142 ? -63.847 -9.387  9.482   1.00 11.83 ? 142  TRP B CA  1 
ATOM   4351 C  C   . TRP B  1 142 ? -65.306 -9.728  9.832   1.00 12.69 ? 142  TRP B C   1 
ATOM   4352 O  O   . TRP B  1 142 ? -66.085 -8.812  10.229  1.00 12.20 ? 142  TRP B O   1 
ATOM   4353 C  CB  . TRP B  1 142 ? -63.609 -9.419  7.954   1.00 11.28 ? 142  TRP B CB  1 
ATOM   4354 C  CG  . TRP B  1 142 ? -64.636 -8.608  7.233   1.00 11.36 ? 142  TRP B CG  1 
ATOM   4355 C  CD1 . TRP B  1 142 ? -65.889 -9.007  6.890   1.00 11.45 ? 142  TRP B CD1 1 
ATOM   4356 C  CD2 . TRP B  1 142 ? -64.539 -7.224  6.860   1.00 10.92 ? 142  TRP B CD2 1 
ATOM   4357 N  NE1 . TRP B  1 142 ? -66.573 -7.994  6.276   1.00 11.00 ? 142  TRP B NE1 1 
ATOM   4358 C  CE2 . TRP B  1 142 ? -65.771 -6.871  6.259   1.00 11.36 ? 142  TRP B CE2 1 
ATOM   4359 C  CE3 . TRP B  1 142 ? -63.533 -6.261  6.940   1.00 12.05 ? 142  TRP B CE3 1 
ATOM   4360 C  CZ2 . TRP B  1 142 ? -66.015 -5.595  5.750   1.00 11.37 ? 142  TRP B CZ2 1 
ATOM   4361 C  CZ3 . TRP B  1 142 ? -63.774 -4.994  6.452   1.00 11.68 ? 142  TRP B CZ3 1 
ATOM   4362 C  CH2 . TRP B  1 142 ? -65.002 -4.673  5.864   1.00 12.36 ? 142  TRP B CH2 1 
ATOM   4363 N  N   . LEU B  1 143 ? -65.692 -10.996 9.683   1.00 12.61 ? 143  LEU B N   1 
ATOM   4364 C  CA  . LEU B  1 143 ? -67.117 -11.380 9.833   1.00 14.15 ? 143  LEU B CA  1 
ATOM   4365 C  C   . LEU B  1 143 ? -67.564 -11.064 11.273  1.00 13.15 ? 143  LEU B C   1 
ATOM   4366 O  O   . LEU B  1 143 ? -68.649 -10.526 11.428  1.00 13.07 ? 143  LEU B O   1 
ATOM   4367 C  CB  . LEU B  1 143 ? -67.266 -12.861 9.510   1.00 14.52 ? 143  LEU B CB  1 
ATOM   4368 C  CG  . LEU B  1 143 ? -68.659 -13.439 9.721   1.00 16.06 ? 143  LEU B CG  1 
ATOM   4369 C  CD1 . LEU B  1 143 ? -69.712 -12.634 8.968   1.00 16.28 ? 143  LEU B CD1 1 
ATOM   4370 C  CD2 . LEU B  1 143 ? -68.669 -14.889 9.254   1.00 17.00 ? 143  LEU B CD2 1 
ATOM   4371 N  N   . GLN B  1 144 ? -66.774 -11.437 12.278  1.00 14.67 ? 144  GLN B N   1 
ATOM   4372 C  CA  . GLN B  1 144 ? -67.216 -11.288 13.687  1.00 14.81 ? 144  GLN B CA  1 
ATOM   4373 C  C   . GLN B  1 144 ? -67.237 -9.794  14.038  1.00 14.65 ? 144  GLN B C   1 
ATOM   4374 O  O   . GLN B  1 144 ? -68.143 -9.371  14.754  1.00 15.11 ? 144  GLN B O   1 
ATOM   4375 C  CB  . GLN B  1 144 ? -66.301 -12.066 14.616  1.00 16.81 ? 144  GLN B CB  1 
ATOM   4376 C  CG  . GLN B  1 144 ? -66.291 -13.555 14.337  1.00 19.86 ? 144  GLN B CG  1 
ATOM   4377 C  CD  . GLN B  1 144 ? -65.610 -14.247 15.489  1.00 26.82 ? 144  GLN B CD  1 
ATOM   4378 O  OE1 . GLN B  1 144 ? -65.865 -13.930 16.663  1.00 31.44 ? 144  GLN B OE1 1 
ATOM   4379 N  NE2 . GLN B  1 144 ? -64.706 -15.161 15.163  1.00 32.57 ? 144  GLN B NE2 1 
ATOM   4380 N  N   . THR B  1 145 ? -66.295 -9.010  13.516  1.00 13.13 ? 145  THR B N   1 
ATOM   4381 C  CA  . THR B  1 145 ? -66.237 -7.551  13.814  1.00 13.19 ? 145  THR B CA  1 
ATOM   4382 C  C   . THR B  1 145 ? -67.417 -6.876  13.122  1.00 13.43 ? 145  THR B C   1 
ATOM   4383 O  O   . THR B  1 145 ? -68.077 -5.970  13.681  1.00 14.24 ? 145  THR B O   1 
ATOM   4384 C  CB  . THR B  1 145 ? -64.908 -6.948  13.392  1.00 11.94 ? 145  THR B CB  1 
ATOM   4385 O  OG1 . THR B  1 145 ? -63.813 -7.725  13.895  1.00 12.99 ? 145  THR B OG1 1 
ATOM   4386 C  CG2 . THR B  1 145 ? -64.792 -5.506  13.866  1.00 12.41 ? 145  THR B CG2 1 
ATOM   4387 N  N   . TYR B  1 146 ? -67.704 -7.297  11.892  1.00 12.60 ? 146  TYR B N   1 
ATOM   4388 C  CA  . TYR B  1 146 ? -68.873 -6.800  11.142  1.00 14.17 ? 146  TYR B CA  1 
ATOM   4389 C  C   . TYR B  1 146 ? -70.173 -7.012  11.947  1.00 14.32 ? 146  TYR B C   1 
ATOM   4390 O  O   . TYR B  1 146 ? -70.985 -6.095  12.082  1.00 13.15 ? 146  TYR B O   1 
ATOM   4391 C  CB  . TYR B  1 146 ? -68.906 -7.472  9.773   1.00 13.46 ? 146  TYR B CB  1 
ATOM   4392 C  CG  . TYR B  1 146 ? -70.029 -7.042  8.895   1.00 14.78 ? 146  TYR B CG  1 
ATOM   4393 C  CD1 . TYR B  1 146 ? -71.305 -7.541  9.072   1.00 15.56 ? 146  TYR B CD1 1 
ATOM   4394 C  CD2 . TYR B  1 146 ? -69.782 -6.201  7.819   1.00 16.04 ? 146  TYR B CD2 1 
ATOM   4395 C  CE1 . TYR B  1 146 ? -72.334 -7.181  8.212   1.00 17.72 ? 146  TYR B CE1 1 
ATOM   4396 C  CE2 . TYR B  1 146 ? -70.804 -5.810  6.977   1.00 18.51 ? 146  TYR B CE2 1 
ATOM   4397 C  CZ  . TYR B  1 146 ? -72.080 -6.284  7.187   1.00 18.30 ? 146  TYR B CZ  1 
ATOM   4398 O  OH  . TYR B  1 146 ? -73.053 -5.914  6.318   1.00 25.51 ? 146  TYR B OH  1 
ATOM   4399 N  N   A LYS B  1 147 ? -70.403 -8.234  12.424  0.50 14.28 ? 147  LYS B N   1 
ATOM   4400 N  N   B LYS B  1 147 ? -70.391 -8.227  12.461  0.50 15.21 ? 147  LYS B N   1 
ATOM   4401 C  CA  A LYS B  1 147 ? -71.613 -8.574  13.222  0.50 14.33 ? 147  LYS B CA  1 
ATOM   4402 C  CA  B LYS B  1 147 ? -71.625 -8.586  13.220  0.50 15.84 ? 147  LYS B CA  1 
ATOM   4403 C  C   A LYS B  1 147 ? -71.704 -7.633  14.429  0.50 14.50 ? 147  LYS B C   1 
ATOM   4404 C  C   B LYS B  1 147 ? -71.717 -7.745  14.502  0.50 15.60 ? 147  LYS B C   1 
ATOM   4405 O  O   A LYS B  1 147 ? -72.796 -7.047  14.643  0.50 13.75 ? 147  LYS B O   1 
ATOM   4406 O  O   B LYS B  1 147 ? -72.840 -7.383  14.888  0.50 16.16 ? 147  LYS B O   1 
ATOM   4407 C  CB  A LYS B  1 147 ? -71.544 -10.050 13.609  0.50 14.48 ? 147  LYS B CB  1 
ATOM   4408 C  CB  B LYS B  1 147 ? -71.646 -10.089 13.515  0.50 16.98 ? 147  LYS B CB  1 
ATOM   4409 C  CG  A LYS B  1 147 ? -71.821 -10.981 12.442  0.50 15.07 ? 147  LYS B CG  1 
ATOM   4410 C  CG  B LYS B  1 147 ? -71.613 -10.967 12.273  0.50 18.40 ? 147  LYS B CG  1 
ATOM   4411 C  CD  A LYS B  1 147 ? -71.699 -12.434 12.800  0.50 15.51 ? 147  LYS B CD  1 
ATOM   4412 C  CD  B LYS B  1 147 ? -72.744 -11.969 12.150  0.50 20.73 ? 147  LYS B CD  1 
ATOM   4413 C  CE  A LYS B  1 147 ? -72.285 -13.326 11.732  0.50 17.90 ? 147  LYS B CE  1 
ATOM   4414 C  CE  B LYS B  1 147 ? -72.979 -12.814 13.384  0.50 21.30 ? 147  LYS B CE  1 
ATOM   4415 N  NZ  A LYS B  1 147 ? -71.662 -14.671 11.739  0.50 20.44 ? 147  LYS B NZ  1 
ATOM   4416 N  NZ  B LYS B  1 147 ? -72.006 -13.926 13.459  0.50 22.35 ? 147  LYS B NZ  1 
ATOM   4417 N  N   . LEU B  1 148 ? -70.579 -7.422  15.119  1.00 14.81 ? 148  LEU B N   1 
ATOM   4418 C  CA  . LEU B  1 148 ? -70.519 -6.590  16.355  1.00 14.69 ? 148  LEU B CA  1 
ATOM   4419 C  C   . LEU B  1 148 ? -70.943 -5.153  16.032  1.00 14.38 ? 148  LEU B C   1 
ATOM   4420 O  O   . LEU B  1 148 ? -71.837 -4.604  16.708  1.00 16.18 ? 148  LEU B O   1 
ATOM   4421 C  CB  . LEU B  1 148 ? -69.113 -6.666  16.951  1.00 15.94 ? 148  LEU B CB  1 
ATOM   4422 C  CG  . LEU B  1 148 ? -68.897 -5.727  18.135  1.00 16.37 ? 148  LEU B CG  1 
ATOM   4423 C  CD1 . LEU B  1 148 ? -69.748 -6.160  19.335  1.00 17.03 ? 148  LEU B CD1 1 
ATOM   4424 C  CD2 . LEU B  1 148 ? -67.438 -5.647  18.508  1.00 15.82 ? 148  LEU B CD2 1 
ATOM   4425 N  N   . ILE B  1 149 ? -70.361 -4.566  14.995  1.00 13.34 ? 149  ILE B N   1 
ATOM   4426 C  CA  . ILE B  1 149 ? -70.707 -3.183  14.562  1.00 14.42 ? 149  ILE B CA  1 
ATOM   4427 C  C   . ILE B  1 149 ? -72.193 -3.158  14.198  1.00 14.59 ? 149  ILE B C   1 
ATOM   4428 O  O   . ILE B  1 149 ? -72.872 -2.223  14.596  1.00 14.66 ? 149  ILE B O   1 
ATOM   4429 C  CB  . ILE B  1 149 ? -69.790 -2.702  13.417  1.00 14.19 ? 149  ILE B CB  1 
ATOM   4430 C  CG1 . ILE B  1 149 ? -68.333 -2.593  13.880  1.00 14.78 ? 149  ILE B CG1 1 
ATOM   4431 C  CG2 . ILE B  1 149 ? -70.315 -1.395  12.847  1.00 14.87 ? 149  ILE B CG2 1 
ATOM   4432 C  CD1 . ILE B  1 149 ? -67.305 -2.620  12.764  1.00 14.85 ? 149  ILE B CD1 1 
ATOM   4433 N  N   . ARG B  1 150 ? -72.708 -4.146  13.468  1.00 13.52 ? 150  ARG B N   1 
ATOM   4434 C  CA  . ARG B  1 150 ? -74.133 -4.085  13.058  1.00 14.59 ? 150  ARG B CA  1 
ATOM   4435 C  C   . ARG B  1 150 ? -75.000 -4.165  14.312  1.00 14.59 ? 150  ARG B C   1 
ATOM   4436 O  O   . ARG B  1 150 ? -76.074 -3.520  14.316  1.00 14.69 ? 150  ARG B O   1 
ATOM   4437 C  CB  . ARG B  1 150 ? -74.509 -5.214  12.095  1.00 15.11 ? 150  ARG B CB  1 
ATOM   4438 C  CG  . ARG B  1 150 ? -73.956 -5.063  10.683  1.00 15.99 ? 150  ARG B CG  1 
ATOM   4439 C  CD  . ARG B  1 150 ? -74.313 -3.738  10.045  1.00 15.55 ? 150  ARG B CD  1 
ATOM   4440 N  NE  . ARG B  1 150 ? -74.135 -3.834  8.611   1.00 16.43 ? 150  ARG B NE  1 
ATOM   4441 C  CZ  . ARG B  1 150 ? -73.741 -2.840  7.808   1.00 16.01 ? 150  ARG B CZ  1 
ATOM   4442 N  NH1 . ARG B  1 150 ? -73.489 -1.631  8.279   1.00 15.10 ? 150  ARG B NH1 1 
ATOM   4443 N  NH2 . ARG B  1 150 ? -73.585 -3.073  6.518   1.00 18.45 ? 150  ARG B NH2 1 
ATOM   4444 N  N   . ARG B  1 151 ? -74.597 -4.951  15.306  1.00 15.63 ? 151  ARG B N   1 
ATOM   4445 C  CA  . ARG B  1 151 ? -75.416 -5.179  16.526  1.00 19.82 ? 151  ARG B CA  1 
ATOM   4446 C  C   . ARG B  1 151 ? -75.459 -3.899  17.361  1.00 21.13 ? 151  ARG B C   1 
ATOM   4447 O  O   . ARG B  1 151 ? -76.576 -3.513  17.801  1.00 18.30 ? 151  ARG B O   1 
ATOM   4448 C  CB  . ARG B  1 151 ? -74.878 -6.340  17.357  1.00 22.85 ? 151  ARG B CB  1 
ATOM   4449 C  CG  . ARG B  1 151 ? -75.786 -6.697  18.524  1.00 30.41 ? 151  ARG B CG  1 
ATOM   4450 C  CD  . ARG B  1 151 ? -75.635 -8.165  18.895  1.00 35.27 ? 151  ARG B CD  1 
ATOM   4451 N  NE  . ARG B  1 151 ? -74.217 -8.528  18.947  1.00 41.08 ? 151  ARG B NE  1 
ATOM   4452 C  CZ  . ARG B  1 151 ? -73.366 -8.169  19.918  1.00 45.18 ? 151  ARG B CZ  1 
ATOM   4453 N  NH1 . ARG B  1 151 ? -72.099 -8.547  19.849  1.00 49.84 ? 151  ARG B NH1 1 
ATOM   4454 N  NH2 . ARG B  1 151 ? -73.773 -7.432  20.944  1.00 43.86 ? 151  ARG B NH2 1 
ATOM   4455 N  N   . LEU B  1 152 ? -74.315 -3.226  17.530  1.00 19.47 ? 152  LEU B N   1 
ATOM   4456 C  CA  . LEU B  1 152 ? -74.180 -2.116  18.522  1.00 19.49 ? 152  LEU B CA  1 
ATOM   4457 C  C   . LEU B  1 152 ? -74.366 -0.746  17.870  1.00 19.80 ? 152  LEU B C   1 
ATOM   4458 O  O   . LEU B  1 152 ? -74.723 0.221   18.595  1.00 21.28 ? 152  LEU B O   1 
ATOM   4459 C  CB  . LEU B  1 152 ? -72.808 -2.199  19.176  1.00 20.31 ? 152  LEU B CB  1 
ATOM   4460 C  CG  . LEU B  1 152 ? -72.551 -3.392  20.082  1.00 23.60 ? 152  LEU B CG  1 
ATOM   4461 C  CD1 . LEU B  1 152 ? -71.261 -3.158  20.854  1.00 26.90 ? 152  LEU B CD1 1 
ATOM   4462 C  CD2 . LEU B  1 152 ? -73.704 -3.652  21.029  1.00 25.32 ? 152  LEU B CD2 1 
ATOM   4463 N  N   . ASP B  1 153 ? -74.113 -0.616  16.569  1.00 17.37 ? 153  ASP B N   1 
ATOM   4464 C  CA  . ASP B  1 153 ? -74.221 0.694   15.877  1.00 16.76 ? 153  ASP B CA  1 
ATOM   4465 C  C   . ASP B  1 153 ? -74.786 0.453   14.489  1.00 16.44 ? 153  ASP B C   1 
ATOM   4466 O  O   . ASP B  1 153 ? -74.116 0.651   13.472  1.00 14.78 ? 153  ASP B O   1 
ATOM   4467 C  CB  . ASP B  1 153 ? -72.856 1.383   15.839  1.00 16.36 ? 153  ASP B CB  1 
ATOM   4468 C  CG  . ASP B  1 153 ? -72.955 2.890   15.757  1.00 16.38 ? 153  ASP B CG  1 
ATOM   4469 O  OD1 . ASP B  1 153 ? -74.082 3.391   15.612  1.00 17.30 ? 153  ASP B OD1 1 
ATOM   4470 O  OD2 . ASP B  1 153 ? -71.912 3.553   15.820  1.00 17.09 ? 153  ASP B OD2 1 
ATOM   4471 N  N   . PRO B  1 154 ? -76.052 0.004   14.401  1.00 17.64 ? 154  PRO B N   1 
ATOM   4472 C  CA  . PRO B  1 154 ? -76.630 -0.365  13.117  1.00 18.35 ? 154  PRO B CA  1 
ATOM   4473 C  C   . PRO B  1 154 ? -76.712 0.759   12.078  1.00 20.40 ? 154  PRO B C   1 
ATOM   4474 O  O   . PRO B  1 154 ? -76.670 0.451   10.919  1.00 22.84 ? 154  PRO B O   1 
ATOM   4475 C  CB  . PRO B  1 154 ? -78.037 -0.869  13.492  1.00 18.99 ? 154  PRO B CB  1 
ATOM   4476 C  CG  . PRO B  1 154 ? -78.299 -0.299  14.865  1.00 18.18 ? 154  PRO B CG  1 
ATOM   4477 C  CD  . PRO B  1 154 ? -76.946 -0.252  15.543  1.00 18.95 ? 154  PRO B CD  1 
ATOM   4478 N  N   . ASN B  1 155 ? -76.778 2.020   12.487  1.00 21.82 ? 155  ASN B N   1 
ATOM   4479 C  CA  . ASN B  1 155 ? -76.910 3.147   11.519  1.00 23.35 ? 155  ASN B CA  1 
ATOM   4480 C  C   . ASN B  1 155 ? -75.541 3.530   10.933  1.00 21.10 ? 155  ASN B C   1 
ATOM   4481 O  O   . ASN B  1 155 ? -75.508 4.392   10.067  1.00 22.19 ? 155  ASN B O   1 
ATOM   4482 C  CB  . ASN B  1 155 ? -77.520 4.398   12.159  1.00 25.41 ? 155  ASN B CB  1 
ATOM   4483 C  CG  . ASN B  1 155 ? -78.871 4.133   12.781  1.00 29.38 ? 155  ASN B CG  1 
ATOM   4484 O  OD1 . ASN B  1 155 ? -79.620 3.295   12.275  1.00 31.42 ? 155  ASN B OD1 1 
ATOM   4485 N  ND2 . ASN B  1 155 ? -79.168 4.830   13.874  1.00 29.55 ? 155  ASN B ND2 1 
ATOM   4486 N  N   . SER B  1 156 ? -74.448 2.940   11.379  1.00 18.07 ? 156  SER B N   1 
ATOM   4487 C  CA  . SER B  1 156 ? -73.099 3.403   10.972  1.00 17.42 ? 156  SER B CA  1 
ATOM   4488 C  C   . SER B  1 156 ? -72.638 2.676   9.695   1.00 18.47 ? 156  SER B C   1 
ATOM   4489 O  O   . SER B  1 156 ? -73.154 1.595   9.371   1.00 18.61 ? 156  SER B O   1 
ATOM   4490 C  CB  . SER B  1 156 ? -72.142 3.257   12.127  1.00 19.13 ? 156  SER B CB  1 
ATOM   4491 O  OG  . SER B  1 156 ? -71.966 1.882   12.455  1.00 24.35 ? 156  SER B OG  1 
ATOM   4492 N  N   . GLN B  1 157 ? -71.679 3.244   8.973   1.00 13.97 ? 157  GLN B N   1 
ATOM   4493 C  CA  . GLN B  1 157 ? -71.146 2.645   7.734   1.00 13.90 ? 157  GLN B CA  1 
ATOM   4494 C  C   . GLN B  1 157 ? -69.954 1.790   8.106   1.00 13.61 ? 157  GLN B C   1 
ATOM   4495 O  O   . GLN B  1 157 ? -69.248 2.147   9.095   1.00 13.13 ? 157  GLN B O   1 
ATOM   4496 C  CB  . GLN B  1 157 ? -70.684 3.720   6.750   1.00 15.16 ? 157  GLN B CB  1 
ATOM   4497 C  CG  . GLN B  1 157 ? -71.836 4.507   6.190   1.00 17.82 ? 157  GLN B CG  1 
ATOM   4498 C  CD  . GLN B  1 157 ? -71.398 5.367   5.040   1.00 18.53 ? 157  GLN B CD  1 
ATOM   4499 O  OE1 . GLN B  1 157 ? -71.995 5.285   3.975   1.00 21.80 ? 157  GLN B OE1 1 
ATOM   4500 N  NE2 . GLN B  1 157 ? -70.369 6.187   5.256   1.00 17.93 ? 157  GLN B NE2 1 
ATOM   4501 N  N   . ILE B  1 158 ? -69.769 0.691   7.381   1.00 12.18 ? 158  ILE B N   1 
ATOM   4502 C  CA  . ILE B  1 158 ? -68.584 -0.177  7.546   1.00 11.74 ? 158  ILE B CA  1 
ATOM   4503 C  C   . ILE B  1 158 ? -67.745 -0.062  6.268   1.00 12.12 ? 158  ILE B C   1 
ATOM   4504 O  O   . ILE B  1 158 ? -68.312 -0.158  5.153   1.00 11.53 ? 158  ILE B O   1 
ATOM   4505 C  CB  . ILE B  1 158 ? -68.992 -1.624  7.878   1.00 12.48 ? 158  ILE B CB  1 
ATOM   4506 C  CG1 . ILE B  1 158 ? -69.756 -1.654  9.214   1.00 12.41 ? 158  ILE B CG1 1 
ATOM   4507 C  CG2 . ILE B  1 158 ? -67.769 -2.561  7.851   1.00 12.45 ? 158  ILE B CG2 1 
ATOM   4508 C  CD1 . ILE B  1 158 ? -70.347 -2.992  9.599   1.00 13.24 ? 158  ILE B CD1 1 
ATOM   4509 N  N   . ILE B  1 159 ? -66.457 0.206   6.441   1.00 11.99 ? 159  ILE B N   1 
ATOM   4510 C  CA  . ILE B  1 159 ? -65.517 0.499   5.332   1.00 12.45 ? 159  ILE B CA  1 
ATOM   4511 C  C   . ILE B  1 159 ? -64.444 -0.596  5.281   1.00 12.07 ? 159  ILE B C   1 
ATOM   4512 O  O   . ILE B  1 159 ? -63.812 -0.914  6.304   1.00 11.85 ? 159  ILE B O   1 
ATOM   4513 C  CB  . ILE B  1 159 ? -64.880 1.899   5.493   1.00 13.52 ? 159  ILE B CB  1 
ATOM   4514 C  CG1 . ILE B  1 159 ? -65.896 3.047   5.480   1.00 16.00 ? 159  ILE B CG1 1 
ATOM   4515 C  CG2 . ILE B  1 159 ? -63.835 2.117   4.405   1.00 13.33 ? 159  ILE B CG2 1 
ATOM   4516 C  CD1 . ILE B  1 159 ? -66.507 3.367   6.832   1.00 16.91 ? 159  ILE B CD1 1 
ATOM   4517 N  N   . GLY B  1 160 ? -64.208 -1.124  4.099   1.00 10.98 ? 160  GLY B N   1 
ATOM   4518 C  CA  . GLY B  1 160 ? -63.129 -2.101  3.919   1.00 10.94 ? 160  GLY B CA  1 
ATOM   4519 C  C   . GLY B  1 160 ? -63.081 -2.569  2.480   1.00 10.82 ? 160  GLY B C   1 
ATOM   4520 O  O   . GLY B  1 160 ? -63.900 -2.177  1.672   1.00 10.68 ? 160  GLY B O   1 
ATOM   4521 N  N   . PRO B  1 161 ? -62.087 -3.404  2.119   1.00 10.05 ? 161  PRO B N   1 
ATOM   4522 C  CA  . PRO B  1 161 ? -61.148 -3.950  3.090   1.00 11.02 ? 161  PRO B CA  1 
ATOM   4523 C  C   . PRO B  1 161 ? -59.871 -3.130  3.334   1.00 11.00 ? 161  PRO B C   1 
ATOM   4524 O  O   . PRO B  1 161 ? -59.045 -3.568  4.105   1.00 11.45 ? 161  PRO B O   1 
ATOM   4525 C  CB  . PRO B  1 161 ? -60.782 -5.262  2.395   1.00 10.22 ? 161  PRO B CB  1 
ATOM   4526 C  CG  . PRO B  1 161 ? -60.796 -4.928  0.950   1.00 10.99 ? 161  PRO B CG  1 
ATOM   4527 C  CD  . PRO B  1 161 ? -61.941 -3.952  0.776   1.00 11.02 ? 161  PRO B CD  1 
ATOM   4528 N  N   . SER B  1 162 ? -59.766 -1.953  2.689   1.00 11.26 ? 162  SER B N   1 
ATOM   4529 C  CA  . SER B  1 162 ? -58.647 -0.992  2.845   1.00 11.77 ? 162  SER B CA  1 
ATOM   4530 C  C   . SER B  1 162 ? -57.341 -1.691  2.435   1.00 11.53 ? 162  SER B C   1 
ATOM   4531 O  O   . SER B  1 162 ? -56.344 -1.543  3.094   1.00 11.02 ? 162  SER B O   1 
ATOM   4532 C  CB  . SER B  1 162 ? -58.577 -0.398  4.227   1.00 11.48 ? 162  SER B CB  1 
ATOM   4533 O  OG  . SER B  1 162 ? -59.764 0.330   4.534   1.00 11.65 ? 162  SER B OG  1 
ATOM   4534 N  N   . TYR B  1 163 ? -57.356 -2.404  1.314   1.00 11.49 ? 163  TYR B N   1 
ATOM   4535 C  CA  . TYR B  1 163 ? -56.121 -2.997  0.750   1.00 12.06 ? 163  TYR B CA  1 
ATOM   4536 C  C   . TYR B  1 163 ? -55.063 -1.945  0.449   1.00 11.39 ? 163  TYR B C   1 
ATOM   4537 O  O   . TYR B  1 163 ? -55.378 -0.824  0.041   1.00 12.57 ? 163  TYR B O   1 
ATOM   4538 C  CB  . TYR B  1 163 ? -56.376 -3.748  -0.542  1.00 12.63 ? 163  TYR B CB  1 
ATOM   4539 C  CG  . TYR B  1 163 ? -57.151 -5.007  -0.368  1.00 14.71 ? 163  TYR B CG  1 
ATOM   4540 C  CD1 . TYR B  1 163 ? -56.872 -5.878  0.670   1.00 14.89 ? 163  TYR B CD1 1 
ATOM   4541 C  CD2 . TYR B  1 163 ? -58.044 -5.395  -1.340  1.00 17.07 ? 163  TYR B CD2 1 
ATOM   4542 C  CE1 . TYR B  1 163 ? -57.518 -7.088  0.781   1.00 18.35 ? 163  TYR B CE1 1 
ATOM   4543 C  CE2 . TYR B  1 163 ? -58.732 -6.570  -1.213  1.00 18.38 ? 163  TYR B CE2 1 
ATOM   4544 C  CZ  . TYR B  1 163 ? -58.483 -7.403  -0.150  1.00 16.94 ? 163  TYR B CZ  1 
ATOM   4545 O  OH  . TYR B  1 163 ? -59.149 -8.579  -0.088  1.00 22.41 ? 163  TYR B OH  1 
ATOM   4546 N  N   . SER B  1 164 ? -53.797 -2.359  0.587   1.00 11.35 ? 164  SER B N   1 
ATOM   4547 C  CA  . SER B  1 164 ? -52.629 -1.483  0.323   1.00 11.49 ? 164  SER B CA  1 
ATOM   4548 C  C   . SER B  1 164 ? -52.645 -1.034  -1.144  1.00 11.56 ? 164  SER B C   1 
ATOM   4549 O  O   . SER B  1 164 ? -52.065 0.016   -1.454  1.00 11.43 ? 164  SER B O   1 
ATOM   4550 C  CB  . SER B  1 164 ? -51.322 -2.152  0.726   1.00 12.38 ? 164  SER B CB  1 
ATOM   4551 O  OG  . SER B  1 164 ? -50.997 -3.217  -0.145  1.00 13.16 ? 164  SER B OG  1 
ATOM   4552 N  N   . TYR B  1 165 ? -53.231 -1.818  -2.031  1.00 12.44 ? 165  TYR B N   1 
ATOM   4553 C  CA  . TYR B  1 165 ? -53.380 -1.455  -3.454  1.00 12.15 ? 165  TYR B CA  1 
ATOM   4554 C  C   . TYR B  1 165 ? -54.518 -2.281  -4.029  1.00 12.26 ? 165  TYR B C   1 
ATOM   4555 O  O   . TYR B  1 165 ? -54.807 -3.373  -3.523  1.00 12.29 ? 165  TYR B O   1 
ATOM   4556 C  CB  . TYR B  1 165 ? -52.076 -1.643  -4.221  1.00 14.04 ? 165  TYR B CB  1 
ATOM   4557 C  CG  . TYR B  1 165 ? -51.662 -3.081  -4.372  1.00 16.21 ? 165  TYR B CG  1 
ATOM   4558 C  CD1 . TYR B  1 165 ? -51.041 -3.738  -3.333  1.00 19.34 ? 165  TYR B CD1 1 
ATOM   4559 C  CD2 . TYR B  1 165 ? -51.881 -3.767  -5.551  1.00 18.64 ? 165  TYR B CD2 1 
ATOM   4560 C  CE1 . TYR B  1 165 ? -50.634 -5.063  -3.457  1.00 21.61 ? 165  TYR B CE1 1 
ATOM   4561 C  CE2 . TYR B  1 165 ? -51.505 -5.099  -5.684  1.00 19.95 ? 165  TYR B CE2 1 
ATOM   4562 C  CZ  . TYR B  1 165 ? -50.920 -5.751  -4.615  1.00 20.39 ? 165  TYR B CZ  1 
ATOM   4563 O  OH  . TYR B  1 165 ? -50.494 -7.051  -4.730  1.00 24.38 ? 165  TYR B OH  1 
ATOM   4564 N  N   . TYR B  1 166 ? -55.062 -1.823  -5.127  1.00 12.04 ? 166  TYR B N   1 
ATOM   4565 C  CA  . TYR B  1 166 ? -56.153 -2.557  -5.804  1.00 13.01 ? 166  TYR B CA  1 
ATOM   4566 C  C   . TYR B  1 166 ? -55.558 -3.808  -6.460  1.00 13.40 ? 166  TYR B C   1 
ATOM   4567 O  O   . TYR B  1 166 ? -54.650 -3.711  -7.295  1.00 14.10 ? 166  TYR B O   1 
ATOM   4568 C  CB  . TYR B  1 166 ? -56.857 -1.725  -6.860  1.00 13.41 ? 166  TYR B CB  1 
ATOM   4569 C  CG  . TYR B  1 166 ? -58.086 -2.438  -7.339  1.00 12.27 ? 166  TYR B CG  1 
ATOM   4570 C  CD1 . TYR B  1 166 ? -59.281 -2.369  -6.658  1.00 13.12 ? 166  TYR B CD1 1 
ATOM   4571 C  CD2 . TYR B  1 166 ? -58.051 -3.212  -8.481  1.00 13.30 ? 166  TYR B CD2 1 
ATOM   4572 C  CE1 . TYR B  1 166 ? -60.394 -3.089  -7.053  1.00 11.80 ? 166  TYR B CE1 1 
ATOM   4573 C  CE2 . TYR B  1 166 ? -59.163 -3.901  -8.924  1.00 12.68 ? 166  TYR B CE2 1 
ATOM   4574 C  CZ  . TYR B  1 166 ? -60.353 -3.812  -8.232  1.00 12.33 ? 166  TYR B CZ  1 
ATOM   4575 O  OH  . TYR B  1 166 ? -61.440 -4.531  -8.626  1.00 13.17 ? 166  TYR B OH  1 
ATOM   4576 N  N   . ASN B  1 167 ? -56.061 -4.961  -6.077  1.00 13.64 ? 167  ASN B N   1 
ATOM   4577 C  CA  . ASN B  1 167 ? -55.620 -6.272  -6.608  1.00 15.06 ? 167  ASN B CA  1 
ATOM   4578 C  C   . ASN B  1 167 ? -56.890 -7.019  -6.990  1.00 14.38 ? 167  ASN B C   1 
ATOM   4579 O  O   . ASN B  1 167 ? -57.693 -7.224  -6.093  1.00 13.47 ? 167  ASN B O   1 
ATOM   4580 C  CB  . ASN B  1 167 ? -54.805 -6.996  -5.538  1.00 16.39 ? 167  ASN B CB  1 
ATOM   4581 C  CG  . ASN B  1 167 ? -54.303 -8.339  -6.004  1.00 18.42 ? 167  ASN B CG  1 
ATOM   4582 O  OD1 . ASN B  1 167 ? -55.087 -9.244  -6.204  1.00 18.69 ? 167  ASN B OD1 1 
ATOM   4583 N  ND2 . ASN B  1 167 ? -52.997 -8.453  -6.242  1.00 22.51 ? 167  ASN B ND2 1 
ATOM   4584 N  N   . HIS B  1 168 ? -57.087 -7.335  -8.260  1.00 14.40 ? 168  HIS B N   1 
ATOM   4585 C  CA  . HIS B  1 168 ? -58.309 -8.015  -8.752  1.00 15.04 ? 168  HIS B CA  1 
ATOM   4586 C  C   . HIS B  1 168 ? -58.482 -9.344  -8.019  1.00 14.83 ? 168  HIS B C   1 
ATOM   4587 O  O   . HIS B  1 168 ? -59.620 -9.638  -7.585  1.00 13.65 ? 168  HIS B O   1 
ATOM   4588 C  CB  . HIS B  1 168 ? -58.240 -8.254  -10.257 1.00 17.85 ? 168  HIS B CB  1 
ATOM   4589 C  CG  . HIS B  1 168 ? -59.423 -8.984  -10.751 1.00 19.43 ? 168  HIS B CG  1 
ATOM   4590 N  ND1 . HIS B  1 168 ? -60.652 -8.363  -10.930 1.00 18.84 ? 168  HIS B ND1 1 
ATOM   4591 C  CD2 . HIS B  1 168 ? -59.590 -10.301 -11.019 1.00 20.38 ? 168  HIS B CD2 1 
ATOM   4592 C  CE1 . HIS B  1 168 ? -61.519 -9.275  -11.320 1.00 21.71 ? 168  HIS B CE1 1 
ATOM   4593 N  NE2 . HIS B  1 168 ? -60.888 -10.477 -11.368 1.00 21.01 ? 168  HIS B NE2 1 
ATOM   4594 N  N   . TYR B  1 169 ? -57.414 -10.130 -7.876  1.00 13.61 ? 169  TYR B N   1 
ATOM   4595 C  CA  . TYR B  1 169 ? -57.561 -11.461 -7.259  1.00 12.98 ? 169  TYR B CA  1 
ATOM   4596 C  C   . TYR B  1 169 ? -58.109 -11.319 -5.824  1.00 11.59 ? 169  TYR B C   1 
ATOM   4597 O  O   . TYR B  1 169 ? -59.082 -11.999 -5.457  1.00 11.14 ? 169  TYR B O   1 
ATOM   4598 C  CB  . TYR B  1 169 ? -56.243 -12.247 -7.310  1.00 13.48 ? 169  TYR B CB  1 
ATOM   4599 C  CG  . TYR B  1 169 ? -56.405 -13.582 -6.655  1.00 13.82 ? 169  TYR B CG  1 
ATOM   4600 C  CD1 . TYR B  1 169 ? -56.866 -14.667 -7.377  1.00 15.92 ? 169  TYR B CD1 1 
ATOM   4601 C  CD2 . TYR B  1 169 ? -56.232 -13.729 -5.291  1.00 15.27 ? 169  TYR B CD2 1 
ATOM   4602 C  CE1 . TYR B  1 169 ? -57.109 -15.886 -6.772  1.00 15.75 ? 169  TYR B CE1 1 
ATOM   4603 C  CE2 . TYR B  1 169 ? -56.499 -14.932 -4.666  1.00 17.38 ? 169  TYR B CE2 1 
ATOM   4604 C  CZ  . TYR B  1 169 ? -56.933 -16.011 -5.410  1.00 17.13 ? 169  TYR B CZ  1 
ATOM   4605 O  OH  . TYR B  1 169 ? -57.176 -17.215 -4.809  1.00 17.94 ? 169  TYR B OH  1 
ATOM   4606 N  N   A ASN B  1 170 ? -57.471 -10.445 -5.048  0.80 11.36 ? 170  ASN B N   1 
ATOM   4607 N  N   B ASN B  1 170 ? -57.512 -10.461 -4.992  0.20 11.22 ? 170  ASN B N   1 
ATOM   4608 C  CA  A ASN B  1 170 ? -57.787 -10.222 -3.613  0.80 12.28 ? 170  ASN B CA  1 
ATOM   4609 C  CA  B ASN B  1 170 ? -57.890 -10.417 -3.551  0.20 11.15 ? 170  ASN B CA  1 
ATOM   4610 C  C   A ASN B  1 170 ? -59.237 -9.735  -3.505  0.80 12.01 ? 170  ASN B C   1 
ATOM   4611 C  C   B ASN B  1 170 ? -59.203 -9.631  -3.378  0.20 11.36 ? 170  ASN B C   1 
ATOM   4612 O  O   A ASN B  1 170 ? -60.000 -10.274 -2.698  0.80 11.45 ? 170  ASN B O   1 
ATOM   4613 O  O   B ASN B  1 170 ? -59.901 -9.901  -2.380  0.20 11.23 ? 170  ASN B O   1 
ATOM   4614 C  CB  A ASN B  1 170 ? -56.811 -9.225  -2.971  0.80 13.82 ? 170  ASN B CB  1 
ATOM   4615 C  CB  B ASN B  1 170 ? -56.730 -9.995  -2.636  0.20 11.02 ? 170  ASN B CB  1 
ATOM   4616 C  CG  A ASN B  1 170 ? -55.414 -9.807  -2.847  0.80 16.56 ? 170  ASN B CG  1 
ATOM   4617 C  CG  B ASN B  1 170 ? -56.297 -8.551  -2.779  0.20 10.97 ? 170  ASN B CG  1 
ATOM   4618 O  OD1 A ASN B  1 170 ? -55.253 -11.017 -3.002  0.80 17.19 ? 170  ASN B OD1 1 
ATOM   4619 O  OD1 B ASN B  1 170 ? -56.913 -7.785  -3.505  0.20 11.44 ? 170  ASN B OD1 1 
ATOM   4620 N  ND2 A ASN B  1 170 ? -54.406 -8.975  -2.577  0.80 15.65 ? 170  ASN B ND2 1 
ATOM   4621 N  ND2 B ASN B  1 170 ? -55.236 -8.168  -2.083  0.20 10.93 ? 170  ASN B ND2 1 
ATOM   4622 N  N   . MET B  1 171 ? -59.569 -8.735  -4.303  1.00 11.40 ? 171  MET B N   1 
ATOM   4623 C  CA  . MET B  1 171 ? -60.921 -8.110  -4.246  1.00 11.68 ? 171  MET B CA  1 
ATOM   4624 C  C   . MET B  1 171 ? -61.993 -9.118  -4.655  1.00 10.89 ? 171  MET B C   1 
ATOM   4625 O  O   . MET B  1 171 ? -63.049 -9.154  -3.997  1.00 10.78 ? 171  MET B O   1 
ATOM   4626 C  CB  . MET B  1 171 ? -60.988 -6.845  -5.100  1.00 12.41 ? 171  MET B CB  1 
ATOM   4627 C  CG  . MET B  1 171 ? -62.255 -6.061  -4.833  1.00 13.12 ? 171  MET B CG  1 
ATOM   4628 S  SD  . MET B  1 171 ? -62.278 -5.368  -3.134  1.00 15.90 ? 171  MET B SD  1 
ATOM   4629 C  CE  . MET B  1 171 ? -61.134 -4.014  -3.339  1.00 16.11 ? 171  MET B CE  1 
ATOM   4630 N  N   . ASN B  1 172 ? -61.747 -9.964  -5.652  1.00 10.68 ? 172  ASN B N   1 
ATOM   4631 C  CA  . ASN B  1 172 ? -62.731 -10.979 -6.075  1.00 11.18 ? 172  ASN B CA  1 
ATOM   4632 C  C   . ASN B  1 172 ? -62.955 -11.942 -4.896  1.00 11.59 ? 172  ASN B C   1 
ATOM   4633 O  O   . ASN B  1 172 ? -64.099 -12.308 -4.634  1.00 11.85 ? 172  ASN B O   1 
ATOM   4634 C  CB  . ASN B  1 172 ? -62.282 -11.717 -7.344  1.00 11.53 ? 172  ASN B CB  1 
ATOM   4635 C  CG  . ASN B  1 172 ? -63.238 -12.819 -7.732  1.00 11.65 ? 172  ASN B CG  1 
ATOM   4636 O  OD1 . ASN B  1 172 ? -64.375 -12.538 -8.151  1.00 13.22 ? 172  ASN B OD1 1 
ATOM   4637 N  ND2 . ASN B  1 172 ? -62.836 -14.055 -7.473  1.00 11.94 ? 172  ASN B ND2 1 
ATOM   4638 N  N   . ALA B  1 173 ? -61.888 -12.365 -4.217  1.00 12.15 ? 173  ALA B N   1 
ATOM   4639 C  CA  . ALA B  1 173 ? -61.989 -13.353 -3.110  1.00 12.44 ? 173  ALA B CA  1 
ATOM   4640 C  C   . ALA B  1 173 ? -62.727 -12.699 -1.927  1.00 11.92 ? 173  ALA B C   1 
ATOM   4641 O  O   . ALA B  1 173 ? -63.638 -13.333 -1.358  1.00 11.63 ? 173  ALA B O   1 
ATOM   4642 C  CB  . ALA B  1 173 ? -60.617 -13.785 -2.706  1.00 13.52 ? 173  ALA B CB  1 
ATOM   4643 N  N   . PHE B  1 174 ? -62.397 -11.438 -1.612  1.00 11.60 ? 174  PHE B N   1 
ATOM   4644 C  CA  . PHE B  1 174 ? -62.964 -10.719 -0.442  1.00 11.47 ? 174  PHE B CA  1 
ATOM   4645 C  C   . PHE B  1 174 ? -64.464 -10.495 -0.671  1.00 11.60 ? 174  PHE B C   1 
ATOM   4646 O  O   . PHE B  1 174 ? -65.323 -10.827 0.213   1.00 11.72 ? 174  PHE B O   1 
ATOM   4647 C  CB  . PHE B  1 174 ? -62.246 -9.407  -0.195  1.00 11.85 ? 174  PHE B CB  1 
ATOM   4648 C  CG  . PHE B  1 174 ? -62.861 -8.620  0.925   1.00 11.48 ? 174  PHE B CG  1 
ATOM   4649 C  CD1 . PHE B  1 174 ? -62.768 -9.082  2.233   1.00 12.83 ? 174  PHE B CD1 1 
ATOM   4650 C  CD2 . PHE B  1 174 ? -63.567 -7.469  0.668   1.00 11.74 ? 174  PHE B CD2 1 
ATOM   4651 C  CE1 . PHE B  1 174 ? -63.337 -8.348  3.267   1.00 12.64 ? 174  PHE B CE1 1 
ATOM   4652 C  CE2 . PHE B  1 174 ? -64.100 -6.719  1.712   1.00 11.87 ? 174  PHE B CE2 1 
ATOM   4653 C  CZ  . PHE B  1 174 ? -63.957 -7.155  3.006   1.00 12.50 ? 174  PHE B CZ  1 
ATOM   4654 N  N   . LEU B  1 175 ? -64.807 -10.016 -1.861  1.00 11.67 ? 175  LEU B N   1 
ATOM   4655 C  CA  . LEU B  1 175 ? -66.221 -9.674  -2.160  1.00 11.20 ? 175  LEU B CA  1 
ATOM   4656 C  C   . LEU B  1 175 ? -67.037 -10.957 -2.209  1.00 11.62 ? 175  LEU B C   1 
ATOM   4657 O  O   . LEU B  1 175 ? -68.204 -10.921 -1.797  1.00 11.12 ? 175  LEU B O   1 
ATOM   4658 C  CB  . LEU B  1 175 ? -66.302 -8.869  -3.464  1.00 11.37 ? 175  LEU B CB  1 
ATOM   4659 C  CG  . LEU B  1 175 ? -65.735 -7.447  -3.352  1.00 11.70 ? 175  LEU B CG  1 
ATOM   4660 C  CD1 . LEU B  1 175 ? -65.967 -6.720  -4.651  1.00 11.29 ? 175  LEU B CD1 1 
ATOM   4661 C  CD2 . LEU B  1 175 ? -66.372 -6.705  -2.208  1.00 12.42 ? 175  LEU B CD2 1 
ATOM   4662 N  N   . ASN B  1 176 ? -66.480 -12.059 -2.722  1.00 11.40 ? 176  ASN B N   1 
ATOM   4663 C  CA  . ASN B  1 176 ? -67.232 -13.335 -2.747  1.00 11.78 ? 176  ASN B CA  1 
ATOM   4664 C  C   . ASN B  1 176 ? -67.416 -13.829 -1.313  1.00 11.89 ? 176  ASN B C   1 
ATOM   4665 O  O   . ASN B  1 176 ? -68.536 -14.253 -0.972  1.00 11.81 ? 176  ASN B O   1 
ATOM   4666 C  CB  . ASN B  1 176 ? -66.540 -14.403 -3.594  1.00 11.53 ? 176  ASN B CB  1 
ATOM   4667 C  CG  . ASN B  1 176 ? -66.983 -14.411 -5.042  1.00 11.60 ? 176  ASN B CG  1 
ATOM   4668 O  OD1 . ASN B  1 176 ? -68.173 -14.631 -5.342  1.00 14.84 ? 176  ASN B OD1 1 
ATOM   4669 N  ND2 . ASN B  1 176 ? -66.036 -14.204 -5.941  1.00 11.93 ? 176  ASN B ND2 1 
ATOM   4670 N  N   . PHE B  1 177 ? -66.370 -13.804 -0.500  1.00 10.83 ? 177  PHE B N   1 
ATOM   4671 C  CA  . PHE B  1 177 ? -66.527 -14.220 0.921   1.00 11.83 ? 177  PHE B CA  1 
ATOM   4672 C  C   . PHE B  1 177 ? -67.630 -13.371 1.568   1.00 11.79 ? 177  PHE B C   1 
ATOM   4673 O  O   . PHE B  1 177 ? -68.518 -13.915 2.255   1.00 11.72 ? 177  PHE B O   1 
ATOM   4674 C  CB  . PHE B  1 177 ? -65.211 -14.071 1.678   1.00 12.29 ? 177  PHE B CB  1 
ATOM   4675 C  CG  . PHE B  1 177 ? -65.383 -14.379 3.150   1.00 13.72 ? 177  PHE B CG  1 
ATOM   4676 C  CD1 . PHE B  1 177 ? -65.343 -15.683 3.620   1.00 14.65 ? 177  PHE B CD1 1 
ATOM   4677 C  CD2 . PHE B  1 177 ? -65.696 -13.376 4.046   1.00 15.02 ? 177  PHE B CD2 1 
ATOM   4678 C  CE1 . PHE B  1 177 ? -65.570 -15.965 4.963   1.00 16.59 ? 177  PHE B CE1 1 
ATOM   4679 C  CE2 . PHE B  1 177 ? -65.923 -13.663 5.384   1.00 15.64 ? 177  PHE B CE2 1 
ATOM   4680 C  CZ  . PHE B  1 177 ? -65.865 -14.947 5.839   1.00 16.30 ? 177  PHE B CZ  1 
ATOM   4681 N  N   . CYS B  1 178 ? -67.595 -12.055 1.327   1.00 12.47 ? 178  CYS B N   1 
ATOM   4682 C  CA  . CYS B  1 178 ? -68.525 -11.123 2.006   1.00 12.76 ? 178  CYS B CA  1 
ATOM   4683 C  C   . CYS B  1 178 ? -69.946 -11.349 1.485   1.00 12.57 ? 178  CYS B C   1 
ATOM   4684 O  O   . CYS B  1 178 ? -70.910 -11.292 2.282   1.00 12.30 ? 178  CYS B O   1 
ATOM   4685 C  CB  . CYS B  1 178 ? -68.111 -9.663  1.834   1.00 12.06 ? 178  CYS B CB  1 
ATOM   4686 S  SG  . CYS B  1 178 ? -66.642 -9.223  2.798   1.00 13.02 ? 178  CYS B SG  1 
ATOM   4687 N  N   . ARG B  1 179 ? -70.098 -11.600 0.182   1.00 12.39 ? 179  ARG B N   1 
ATOM   4688 C  CA  . ARG B  1 179 ? -71.432 -11.854 -0.392  1.00 12.59 ? 179  ARG B CA  1 
ATOM   4689 C  C   . ARG B  1 179 ? -71.958 -13.171 0.198   1.00 13.00 ? 179  ARG B C   1 
ATOM   4690 O  O   . ARG B  1 179 ? -73.113 -13.183 0.678   1.00 13.04 ? 179  ARG B O   1 
ATOM   4691 C  CB  . ARG B  1 179 ? -71.394 -11.905 -1.916  1.00 14.93 ? 179  ARG B CB  1 
ATOM   4692 C  CG  . ARG B  1 179 ? -72.745 -12.233 -2.525  1.00 16.29 ? 179  ARG B CG  1 
ATOM   4693 C  CD  . ARG B  1 179 ? -72.709 -12.186 -4.053  1.00 19.54 ? 179  ARG B CD  1 
ATOM   4694 N  NE  . ARG B  1 179 ? -74.035 -12.537 -4.527  1.00 24.88 ? 179  ARG B NE  1 
ATOM   4695 C  CZ  . ARG B  1 179 ? -74.439 -13.779 -4.720  1.00 26.24 ? 179  ARG B CZ  1 
ATOM   4696 N  NH1 . ARG B  1 179 ? -75.678 -14.022 -5.104  1.00 28.62 ? 179  ARG B NH1 1 
ATOM   4697 N  NH2 . ARG B  1 179 ? -73.600 -14.777 -4.525  1.00 27.55 ? 179  ARG B NH2 1 
ATOM   4698 N  N   . ALA B  1 180 ? -71.121 -14.217 0.247   1.00 12.43 ? 180  ALA B N   1 
ATOM   4699 C  CA  . ALA B  1 180 ? -71.552 -15.554 0.717   1.00 12.82 ? 180  ALA B CA  1 
ATOM   4700 C  C   . ALA B  1 180 ? -71.887 -15.499 2.215   1.00 13.72 ? 180  ALA B C   1 
ATOM   4701 O  O   . ALA B  1 180 ? -72.755 -16.270 2.646   1.00 14.96 ? 180  ALA B O   1 
ATOM   4702 C  CB  . ALA B  1 180 ? -70.483 -16.573 0.420   1.00 12.41 ? 180  ALA B CB  1 
ATOM   4703 N  N   . ASN B  1 181 ? -71.287 -14.595 2.987   1.00 12.50 ? 181  ASN B N   1 
ATOM   4704 C  CA  . ASN B  1 181 ? -71.493 -14.573 4.458   1.00 13.18 ? 181  ASN B CA  1 
ATOM   4705 C  C   . ASN B  1 181 ? -72.221 -13.303 4.918   1.00 12.38 ? 181  ASN B C   1 
ATOM   4706 O  O   . ASN B  1 181 ? -72.275 -13.072 6.140   1.00 11.59 ? 181  ASN B O   1 
ATOM   4707 C  CB  . ASN B  1 181 ? -70.151 -14.811 5.136   1.00 13.57 ? 181  ASN B CB  1 
ATOM   4708 C  CG  . ASN B  1 181 ? -69.607 -16.189 4.822   1.00 15.73 ? 181  ASN B CG  1 
ATOM   4709 O  OD1 . ASN B  1 181 ? -70.101 -17.189 5.363   1.00 16.34 ? 181  ASN B OD1 1 
ATOM   4710 N  ND2 . ASN B  1 181 ? -68.571 -16.251 3.996   1.00 15.16 ? 181  ASN B ND2 1 
ATOM   4711 N  N   . ASN B  1 182 ? -72.808 -12.546 3.994   1.00 12.56 ? 182  ASN B N   1 
ATOM   4712 C  CA  . ASN B  1 182 ? -73.657 -11.347 4.252   1.00 13.61 ? 182  ASN B CA  1 
ATOM   4713 C  C   . ASN B  1 182 ? -72.891 -10.353 5.127   1.00 12.50 ? 182  ASN B C   1 
ATOM   4714 O  O   . ASN B  1 182 ? -73.420 -9.862  6.162   1.00 13.18 ? 182  ASN B O   1 
ATOM   4715 C  CB  . ASN B  1 182 ? -75.004 -11.756 4.846   1.00 15.32 ? 182  ASN B CB  1 
ATOM   4716 C  CG  . ASN B  1 182 ? -75.749 -12.667 3.901   1.00 16.59 ? 182  ASN B CG  1 
ATOM   4717 O  OD1 . ASN B  1 182 ? -76.199 -12.210 2.862   1.00 21.36 ? 182  ASN B OD1 1 
ATOM   4718 N  ND2 . ASN B  1 182 ? -75.811 -13.936 4.240   1.00 17.64 ? 182  ASN B ND2 1 
ATOM   4719 N  N   . CYS B  1 183 ? -71.653 -10.065 4.759   1.00 12.24 ? 183  CYS B N   1 
ATOM   4720 C  CA  . CYS B  1 183 ? -70.802 -9.109  5.508   1.00 12.49 ? 183  CYS B CA  1 
ATOM   4721 C  C   . CYS B  1 183 ? -70.079 -8.172  4.552   1.00 12.41 ? 183  CYS B C   1 
ATOM   4722 O  O   . CYS B  1 183 ? -68.908 -7.851  4.786   1.00 11.89 ? 183  CYS B O   1 
ATOM   4723 C  CB  . CYS B  1 183 ? -69.860 -9.827  6.461   1.00 12.47 ? 183  CYS B CB  1 
ATOM   4724 S  SG  . CYS B  1 183 ? -68.788 -11.089 5.719   1.00 12.62 ? 183  CYS B SG  1 
ATOM   4725 N  N   . LEU B  1 184 ? -70.763 -7.712  3.525   1.00 12.87 ? 184  LEU B N   1 
ATOM   4726 C  CA  . LEU B  1 184 ? -70.168 -6.757  2.571   1.00 12.76 ? 184  LEU B CA  1 
ATOM   4727 C  C   . LEU B  1 184 ? -70.031 -5.423  3.262   1.00 12.30 ? 184  LEU B C   1 
ATOM   4728 O  O   . LEU B  1 184 ? -70.955 -4.943  3.921   1.00 11.45 ? 184  LEU B O   1 
ATOM   4729 C  CB  . LEU B  1 184 ? -71.070 -6.591  1.350   1.00 12.54 ? 184  LEU B CB  1 
ATOM   4730 C  CG  . LEU B  1 184 ? -71.012 -7.747  0.359   1.00 13.19 ? 184  LEU B CG  1 
ATOM   4731 C  CD1 . LEU B  1 184 ? -72.273 -7.790  -0.473  1.00 14.31 ? 184  LEU B CD1 1 
ATOM   4732 C  CD2 . LEU B  1 184 ? -69.766 -7.679  -0.502  1.00 14.12 ? 184  LEU B CD2 1 
ATOM   4733 N  N   . PRO B  1 185 ? -68.943 -4.701  2.983   1.00 12.18 ? 185  PRO B N   1 
ATOM   4734 C  CA  . PRO B  1 185 ? -68.848 -3.332  3.472   1.00 12.98 ? 185  PRO B CA  1 
ATOM   4735 C  C   . PRO B  1 185 ? -69.899 -2.454  2.799   1.00 11.29 ? 185  PRO B C   1 
ATOM   4736 O  O   . PRO B  1 185 ? -70.292 -2.732  1.656   1.00 11.06 ? 185  PRO B O   1 
ATOM   4737 C  CB  . PRO B  1 185 ? -67.443 -2.869  3.099   1.00 13.11 ? 185  PRO B CB  1 
ATOM   4738 C  CG  . PRO B  1 185 ? -66.960 -3.858  2.072   1.00 14.79 ? 185  PRO B CG  1 
ATOM   4739 C  CD  . PRO B  1 185 ? -67.795 -5.115  2.180   1.00 13.44 ? 185  PRO B CD  1 
ATOM   4740 N  N   . ASP B  1 186 ? -70.298 -1.381  3.484   1.00 10.29 ? 186  ASP B N   1 
ATOM   4741 C  CA  . ASP B  1 186 ? -71.123 -0.313  2.886   1.00 11.11 ? 186  ASP B CA  1 
ATOM   4742 C  C   . ASP B  1 186 ? -70.282 0.524   1.921   1.00 10.64 ? 186  ASP B C   1 
ATOM   4743 O  O   . ASP B  1 186 ? -70.833 1.029   0.910   1.00 11.25 ? 186  ASP B O   1 
ATOM   4744 C  CB  . ASP B  1 186 ? -71.736 0.579   3.956   1.00 11.38 ? 186  ASP B CB  1 
ATOM   4745 C  CG  . ASP B  1 186 ? -72.491 -0.250  4.959   1.00 11.40 ? 186  ASP B CG  1 
ATOM   4746 O  OD1 . ASP B  1 186 ? -73.387 -1.013  4.527   1.00 12.55 ? 186  ASP B OD1 1 
ATOM   4747 O  OD2 . ASP B  1 186 ? -72.127 -0.178  6.159   1.00 13.19 ? 186  ASP B OD2 1 
ATOM   4748 N  N   . VAL B  1 187 ? -68.988 0.671   2.223   1.00 10.66 ? 187  VAL B N   1 
ATOM   4749 C  CA  . VAL B  1 187 ? -68.039 1.494   1.440   1.00 10.78 ? 187  VAL B CA  1 
ATOM   4750 C  C   . VAL B  1 187 ? -66.820 0.640   1.132   1.00 9.99  ? 187  VAL B C   1 
ATOM   4751 O  O   . VAL B  1 187 ? -66.169 0.200   2.083   1.00 10.82 ? 187  VAL B O   1 
ATOM   4752 C  CB  . VAL B  1 187 ? -67.628 2.751   2.217   1.00 11.28 ? 187  VAL B CB  1 
ATOM   4753 C  CG1 . VAL B  1 187 ? -66.784 3.640   1.344   1.00 11.23 ? 187  VAL B CG1 1 
ATOM   4754 C  CG2 . VAL B  1 187 ? -68.850 3.479   2.746   1.00 11.11 ? 187  VAL B CG2 1 
ATOM   4755 N  N   . ILE B  1 188 ? -66.611 0.339   -0.140  1.00 9.88  ? 188  ILE B N   1 
ATOM   4756 C  CA  . ILE B  1 188 ? -65.429 -0.436  -0.589  1.00 10.09 ? 188  ILE B CA  1 
ATOM   4757 C  C   . ILE B  1 188 ? -64.217 0.494   -0.654  1.00 10.81 ? 188  ILE B C   1 
ATOM   4758 O  O   . ILE B  1 188 ? -64.308 1.566   -1.263  1.00 10.85 ? 188  ILE B O   1 
ATOM   4759 C  CB  . ILE B  1 188 ? -65.703 -1.180  -1.916  1.00 10.84 ? 188  ILE B CB  1 
ATOM   4760 C  CG1 . ILE B  1 188 ? -66.835 -2.190  -1.690  1.00 11.41 ? 188  ILE B CG1 1 
ATOM   4761 C  CG2 . ILE B  1 188 ? -64.427 -1.877  -2.414  1.00 10.77 ? 188  ILE B CG2 1 
ATOM   4762 C  CD1 . ILE B  1 188 ? -67.308 -2.908  -2.961  1.00 11.81 ? 188  ILE B CD1 1 
ATOM   4763 N  N   . CYS B  1 189 ? -63.116 0.058   -0.077  1.00 10.49 ? 189  CYS B N   1 
ATOM   4764 C  CA  . CYS B  1 189 ? -61.945 0.929   0.199   1.00 10.46 ? 189  CYS B CA  1 
ATOM   4765 C  C   . CYS B  1 189 ? -60.626 0.241   -0.143  1.00 11.15 ? 189  CYS B C   1 
ATOM   4766 O  O   . CYS B  1 189 ? -60.429 -0.968  0.150   1.00 11.68 ? 189  CYS B O   1 
ATOM   4767 C  CB  . CYS B  1 189 ? -61.976 1.413   1.633   1.00 11.47 ? 189  CYS B CB  1 
ATOM   4768 S  SG  . CYS B  1 189 ? -60.602 2.534   2.006   1.00 12.99 ? 189  CYS B SG  1 
ATOM   4769 N  N   . TRP B  1 190 ? -59.736 0.999   -0.776  1.00 10.04 ? 190  TRP B N   1 
ATOM   4770 C  CA  . TRP B  1 190 ? -58.335 0.574   -1.020  1.00 10.86 ? 190  TRP B CA  1 
ATOM   4771 C  C   . TRP B  1 190 ? -57.493 1.832   -1.121  1.00 10.71 ? 190  TRP B C   1 
ATOM   4772 O  O   . TRP B  1 190 ? -58.059 2.975   -1.159  1.00 11.15 ? 190  TRP B O   1 
ATOM   4773 C  CB  . TRP B  1 190 ? -58.186 -0.325  -2.254  1.00 10.47 ? 190  TRP B CB  1 
ATOM   4774 C  CG  . TRP B  1 190 ? -58.468 0.323   -3.567  1.00 10.78 ? 190  TRP B CG  1 
ATOM   4775 C  CD1 . TRP B  1 190 ? -57.587 0.989   -4.368  1.00 11.32 ? 190  TRP B CD1 1 
ATOM   4776 C  CD2 . TRP B  1 190 ? -59.752 0.454   -4.214  1.00 10.35 ? 190  TRP B CD2 1 
ATOM   4777 N  NE1 . TRP B  1 190 ? -58.208 1.444   -5.496  1.00 11.91 ? 190  TRP B NE1 1 
ATOM   4778 C  CE2 . TRP B  1 190 ? -59.532 1.126   -5.434  1.00 11.00 ? 190  TRP B CE2 1 
ATOM   4779 C  CE3 . TRP B  1 190 ? -61.049 0.020   -3.924  1.00 11.28 ? 190  TRP B CE3 1 
ATOM   4780 C  CZ2 . TRP B  1 190 ? -60.550 1.410   -6.335  1.00 11.70 ? 190  TRP B CZ2 1 
ATOM   4781 C  CZ3 . TRP B  1 190 ? -62.061 0.278   -4.826  1.00 11.93 ? 190  TRP B CZ3 1 
ATOM   4782 C  CH2 . TRP B  1 190 ? -61.821 1.007   -5.992  1.00 11.63 ? 190  TRP B CH2 1 
ATOM   4783 N  N   . HIS B  1 191 ? -56.171 1.656   -1.174  1.00 10.56 ? 191  HIS B N   1 
ATOM   4784 C  CA  . HIS B  1 191 ? -55.185 2.762   -1.135  1.00 10.80 ? 191  HIS B CA  1 
ATOM   4785 C  C   . HIS B  1 191 ? -54.591 2.948   -2.536  1.00 10.66 ? 191  HIS B C   1 
ATOM   4786 O  O   . HIS B  1 191 ? -54.375 1.933   -3.249  1.00 9.73  ? 191  HIS B O   1 
ATOM   4787 C  CB  . HIS B  1 191 ? -54.159 2.466   -0.070  1.00 10.62 ? 191  HIS B CB  1 
ATOM   4788 C  CG  . HIS B  1 191 ? -54.777 2.356   1.277   1.00 11.20 ? 191  HIS B CG  1 
ATOM   4789 N  ND1 . HIS B  1 191 ? -54.132 1.804   2.342   1.00 11.45 ? 191  HIS B ND1 1 
ATOM   4790 C  CD2 . HIS B  1 191 ? -56.014 2.733   1.715   1.00 10.66 ? 191  HIS B CD2 1 
ATOM   4791 C  CE1 . HIS B  1 191 ? -54.944 1.852   3.414   1.00 11.94 ? 191  HIS B CE1 1 
ATOM   4792 N  NE2 . HIS B  1 191 ? -56.095 2.424   3.048   1.00 10.90 ? 191  HIS B NE2 1 
ATOM   4793 N  N   . GLU B  1 192 ? -54.388 4.190   -2.939  1.00 10.37 ? 192  GLU B N   1 
ATOM   4794 C  CA  . GLU B  1 192 ? -53.791 4.576   -4.240  1.00 10.33 ? 192  GLU B CA  1 
ATOM   4795 C  C   . GLU B  1 192 ? -52.522 5.377   -3.908  1.00 10.17 ? 192  GLU B C   1 
ATOM   4796 O  O   . GLU B  1 192 ? -52.561 6.597   -3.925  1.00 10.37 ? 192  GLU B O   1 
ATOM   4797 C  CB  . GLU B  1 192 ? -54.803 5.348   -5.064  1.00 10.39 ? 192  GLU B CB  1 
ATOM   4798 C  CG  . GLU B  1 192 ? -55.966 4.500   -5.589  1.00 11.02 ? 192  GLU B CG  1 
ATOM   4799 C  CD  . GLU B  1 192 ? -55.649 3.617   -6.778  1.00 12.12 ? 192  GLU B CD  1 
ATOM   4800 O  OE1 . GLU B  1 192 ? -54.461 3.582   -7.242  1.00 11.68 ? 192  GLU B OE1 1 
ATOM   4801 O  OE2 . GLU B  1 192 ? -56.590 2.941   -7.231  1.00 12.83 ? 192  GLU B OE2 1 
ATOM   4802 N  N   . LEU B  1 193 ? -51.455 4.664   -3.575  1.00 11.55 ? 193  LEU B N   1 
ATOM   4803 C  CA  . LEU B  1 193 ? -50.173 5.183   -3.028  1.00 11.77 ? 193  LEU B CA  1 
ATOM   4804 C  C   . LEU B  1 193 ? -49.067 5.053   -4.080  1.00 11.56 ? 193  LEU B C   1 
ATOM   4805 O  O   . LEU B  1 193 ? -47.887 5.325   -3.723  1.00 11.55 ? 193  LEU B O   1 
ATOM   4806 C  CB  . LEU B  1 193 ? -49.865 4.438   -1.726  1.00 12.65 ? 193  LEU B CB  1 
ATOM   4807 C  CG  . LEU B  1 193 ? -50.829 4.767   -0.575  1.00 12.97 ? 193  LEU B CG  1 
ATOM   4808 C  CD1 . LEU B  1 193 ? -50.693 3.802   0.572   1.00 12.81 ? 193  LEU B CD1 1 
ATOM   4809 C  CD2 . LEU B  1 193 ? -50.668 6.206   -0.127  1.00 12.82 ? 193  LEU B CD2 1 
ATOM   4810 N  N   . GLY B  1 194 ? -49.413 4.778   -5.340  1.00 11.27 ? 194  GLY B N   1 
ATOM   4811 C  CA  . GLY B  1 194 ? -48.449 4.577   -6.438  1.00 11.82 ? 194  GLY B CA  1 
ATOM   4812 C  C   . GLY B  1 194 ? -48.672 5.525   -7.586  1.00 12.14 ? 194  GLY B C   1 
ATOM   4813 O  O   . GLY B  1 194 ? -48.224 5.234   -8.667  1.00 11.74 ? 194  GLY B O   1 
ATOM   4814 N  N   . GLY B  1 195 ? -49.407 6.614   -7.371  1.00 11.55 ? 195  GLY B N   1 
ATOM   4815 C  CA  . GLY B  1 195 ? -49.705 7.578   -8.436  1.00 12.05 ? 195  GLY B CA  1 
ATOM   4816 C  C   . GLY B  1 195 ? -51.152 7.553   -8.877  1.00 11.76 ? 195  GLY B C   1 
ATOM   4817 O  O   . GLY B  1 195 ? -51.916 6.637   -8.498  1.00 13.67 ? 195  GLY B O   1 
ATOM   4818 N  N   . SER B  1 196 ? -51.525 8.540   -9.681  1.00 12.61 ? 196  SER B N   1 
ATOM   4819 C  CA  . SER B  1 196 ? -52.920 8.763   -10.128 1.00 14.08 ? 196  SER B CA  1 
ATOM   4820 C  C   . SER B  1 196 ? -53.277 7.934   -11.371 1.00 13.56 ? 196  SER B C   1 
ATOM   4821 O  O   . SER B  1 196 ? -54.464 7.888   -11.725 1.00 13.71 ? 196  SER B O   1 
ATOM   4822 C  CB  . SER B  1 196 ? -53.120 10.236  -10.384 1.00 14.67 ? 196  SER B CB  1 
ATOM   4823 O  OG  . SER B  1 196 ? -52.169 10.695  -11.345 1.00 14.04 ? 196  SER B OG  1 
ATOM   4824 N  N   . GLN B  1 197 ? -52.322 7.264   -12.031 1.00 13.14 ? 197  GLN B N   1 
ATOM   4825 C  CA  . GLN B  1 197 ? -52.510 6.736   -13.403 1.00 13.58 ? 197  GLN B CA  1 
ATOM   4826 C  C   . GLN B  1 197 ? -53.454 5.523   -13.426 1.00 15.67 ? 197  GLN B C   1 
ATOM   4827 O  O   . GLN B  1 197 ? -53.873 5.167   -14.547 1.00 15.97 ? 197  GLN B O   1 
ATOM   4828 C  CB  . GLN B  1 197 ? -51.157 6.402   -14.072 1.00 13.78 ? 197  GLN B CB  1 
ATOM   4829 C  CG  . GLN B  1 197 ? -50.406 5.267   -13.401 1.00 13.37 ? 197  GLN B CG  1 
ATOM   4830 C  CD  . GLN B  1 197 ? -49.734 5.679   -12.122 1.00 12.76 ? 197  GLN B CD  1 
ATOM   4831 O  OE1 . GLN B  1 197 ? -49.556 6.875   -11.835 1.00 13.53 ? 197  GLN B OE1 1 
ATOM   4832 N  NE2 . GLN B  1 197 ? -49.305 4.678   -11.356 1.00 13.66 ? 197  GLN B NE2 1 
ATOM   4833 N  N   . ASN B  1 198 ? -53.746 4.861   -12.297 1.00 14.68 ? 198  ASN B N   1 
ATOM   4834 C  CA  . ASN B  1 198 ? -54.569 3.617   -12.353 1.00 15.73 ? 198  ASN B CA  1 
ATOM   4835 C  C   . ASN B  1 198 ? -55.919 3.817   -11.684 1.00 14.87 ? 198  ASN B C   1 
ATOM   4836 O  O   . ASN B  1 198 ? -56.702 2.865   -11.720 1.00 15.50 ? 198  ASN B O   1 
ATOM   4837 C  CB  . ASN B  1 198 ? -53.874 2.374   -11.786 1.00 17.63 ? 198  ASN B CB  1 
ATOM   4838 C  CG  . ASN B  1 198 ? -52.705 1.974   -12.659 1.00 20.69 ? 198  ASN B CG  1 
ATOM   4839 O  OD1 . ASN B  1 198 ? -52.860 1.818   -13.881 1.00 23.55 ? 198  ASN B OD1 1 
ATOM   4840 N  ND2 . ASN B  1 198 ? -51.531 1.926   -12.055 1.00 21.23 ? 198  ASN B ND2 1 
ATOM   4841 N  N   . ILE B  1 199 ? -56.182 4.988   -11.108 1.00 13.04 ? 199  ILE B N   1 
ATOM   4842 C  CA  . ILE B  1 199 ? -57.440 5.242   -10.343 1.00 13.76 ? 199  ILE B CA  1 
ATOM   4843 C  C   . ILE B  1 199 ? -58.654 4.902   -11.185 1.00 14.33 ? 199  ILE B C   1 
ATOM   4844 O  O   . ILE B  1 199 ? -59.511 4.141   -10.719 1.00 13.51 ? 199  ILE B O   1 
ATOM   4845 C  CB  . ILE B  1 199 ? -57.547 6.681   -9.841  1.00 14.53 ? 199  ILE B CB  1 
ATOM   4846 C  CG1 . ILE B  1 199 ? -56.462 6.992   -8.839  1.00 15.06 ? 199  ILE B CG1 1 
ATOM   4847 C  CG2 . ILE B  1 199 ? -58.919 6.913   -9.242  1.00 15.13 ? 199  ILE B CG2 1 
ATOM   4848 C  CD1 . ILE B  1 199 ? -56.273 8.452   -8.625  1.00 15.34 ? 199  ILE B CD1 1 
ATOM   4849 N  N   . SER B  1 200 ? -58.744 5.416   -12.403 1.00 15.18 ? 200  SER B N   1 
ATOM   4850 C  CA  . SER B  1 200 ? -59.991 5.292   -13.198 1.00 15.88 ? 200  SER B CA  1 
ATOM   4851 C  C   . SER B  1 200 ? -60.177 3.823   -13.612 1.00 15.44 ? 200  SER B C   1 
ATOM   4852 O  O   . SER B  1 200 ? -61.292 3.299   -13.532 1.00 15.35 ? 200  SER B O   1 
ATOM   4853 C  CB  . SER B  1 200 ? -59.983 6.235   -14.352 1.00 16.80 ? 200  SER B CB  1 
ATOM   4854 O  OG  . SER B  1 200 ? -60.212 7.566   -13.864 1.00 18.28 ? 200  SER B OG  1 
ATOM   4855 N  N   . GLY B  1 201 ? -59.103 3.173   -14.029 1.00 14.38 ? 201  GLY B N   1 
ATOM   4856 C  CA  . GLY B  1 201 ? -59.111 1.744   -14.403 1.00 14.37 ? 201  GLY B CA  1 
ATOM   4857 C  C   . GLY B  1 201 ? -59.448 0.879   -13.203 1.00 13.53 ? 201  GLY B C   1 
ATOM   4858 O  O   . GLY B  1 201 ? -60.232 -0.071  -13.372 1.00 16.06 ? 201  GLY B O   1 
ATOM   4859 N  N   . ASN B  1 202 ? -58.905 1.191   -12.031 1.00 13.50 ? 202  ASN B N   1 
ATOM   4860 C  CA  . ASN B  1 202 ? -59.175 0.389   -10.794 1.00 12.88 ? 202  ASN B CA  1 
ATOM   4861 C  C   . ASN B  1 202 ? -60.667 0.486   -10.458 1.00 12.78 ? 202  ASN B C   1 
ATOM   4862 O  O   . ASN B  1 202 ? -61.294 -0.560  -10.141 1.00 12.71 ? 202  ASN B O   1 
ATOM   4863 C  CB  . ASN B  1 202 ? -58.263 0.774   -9.622  1.00 12.87 ? 202  ASN B CB  1 
ATOM   4864 C  CG  . ASN B  1 202 ? -56.820 0.355   -9.828  1.00 12.98 ? 202  ASN B CG  1 
ATOM   4865 O  OD1 . ASN B  1 202 ? -56.525 -0.592  -10.583 1.00 13.40 ? 202  ASN B OD1 1 
ATOM   4866 N  ND2 . ASN B  1 202 ? -55.905 1.048   -9.177  1.00 14.16 ? 202  ASN B ND2 1 
ATOM   4867 N  N   . ILE B  1 203 ? -61.211 1.696   -10.488 1.00 12.89 ? 203  ILE B N   1 
ATOM   4868 C  CA  . ILE B  1 203 ? -62.637 1.938   -10.166 1.00 13.92 ? 203  ILE B CA  1 
ATOM   4869 C  C   . ILE B  1 203 ? -63.512 1.218   -11.201 1.00 15.41 ? 203  ILE B C   1 
ATOM   4870 O  O   . ILE B  1 203 ? -64.502 0.567   -10.780 1.00 14.68 ? 203  ILE B O   1 
ATOM   4871 C  CB  . ILE B  1 203 ? -62.968 3.428   -10.004 1.00 12.72 ? 203  ILE B CB  1 
ATOM   4872 C  CG1 . ILE B  1 203 ? -62.302 3.970   -8.740  1.00 12.88 ? 203  ILE B CG1 1 
ATOM   4873 C  CG2 . ILE B  1 203 ? -64.461 3.617   -9.981  1.00 13.74 ? 203  ILE B CG2 1 
ATOM   4874 C  CD1 . ILE B  1 203 ? -62.322 5.485   -8.643  1.00 13.37 ? 203  ILE B CD1 1 
ATOM   4875 N  N   A ARG B  1 204 ? -63.179 1.314   -12.493 0.60 16.00 ? 204  ARG B N   1 
ATOM   4876 N  N   B ARG B  1 204 ? -63.189 1.297   -12.497 0.40 15.87 ? 204  ARG B N   1 
ATOM   4877 C  CA  A ARG B  1 204 ? -63.902 0.590   -13.575 0.60 18.60 ? 204  ARG B CA  1 
ATOM   4878 C  CA  B ARG B  1 204 ? -63.980 0.604   -13.552 0.40 17.75 ? 204  ARG B CA  1 
ATOM   4879 C  C   A ARG B  1 204 ? -63.921 -0.898  -13.239 0.60 17.30 ? 204  ARG B C   1 
ATOM   4880 C  C   B ARG B  1 204 ? -63.916 -0.911  -13.296 0.40 16.86 ? 204  ARG B C   1 
ATOM   4881 O  O   A ARG B  1 204 ? -65.011 -1.512  -13.313 0.60 17.59 ? 204  ARG B O   1 
ATOM   4882 O  O   B ARG B  1 204 ? -64.970 -1.567  -13.438 0.40 17.04 ? 204  ARG B O   1 
ATOM   4883 C  CB  A ARG B  1 204 ? -63.267 0.793   -14.959 0.60 20.90 ? 204  ARG B CB  1 
ATOM   4884 C  CB  B ARG B  1 204 ? -63.542 1.003   -14.972 0.40 19.35 ? 204  ARG B CB  1 
ATOM   4885 C  CG  A ARG B  1 204 ? -63.851 -0.098  -16.049 0.60 23.62 ? 204  ARG B CG  1 
ATOM   4886 C  CG  B ARG B  1 204 ? -63.866 2.448   -15.340 0.40 21.33 ? 204  ARG B CG  1 
ATOM   4887 C  CD  A ARG B  1 204 ? -63.390 0.213   -17.466 0.60 26.24 ? 204  ARG B CD  1 
ATOM   4888 C  CD  B ARG B  1 204 ? -63.519 2.858   -16.765 0.40 23.31 ? 204  ARG B CD  1 
ATOM   4889 N  NE  A ARG B  1 204 ? -63.073 1.631   -17.568 0.60 30.22 ? 204  ARG B NE  1 
ATOM   4890 N  NE  B ARG B  1 204 ? -62.923 4.185   -16.918 0.40 25.40 ? 204  ARG B NE  1 
ATOM   4891 C  CZ  A ARG B  1 204 ? -61.838 2.140   -17.607 0.60 31.33 ? 204  ARG B CZ  1 
ATOM   4892 C  CZ  B ARG B  1 204 ? -61.622 4.419   -17.135 0.40 26.31 ? 204  ARG B CZ  1 
ATOM   4893 N  NH1 A ARG B  1 204 ? -60.781 1.342   -17.633 0.60 33.25 ? 204  ARG B NH1 1 
ATOM   4894 N  NH1 B ARG B  1 204 ? -60.754 3.426   -17.225 0.40 27.46 ? 204  ARG B NH1 1 
ATOM   4895 N  NH2 A ARG B  1 204 ? -61.670 3.453   -17.657 0.60 31.85 ? 204  ARG B NH2 1 
ATOM   4896 N  NH2 B ARG B  1 204 ? -61.182 5.655   -17.280 0.40 29.08 ? 204  ARG B NH2 1 
ATOM   4897 N  N   . ASP B  1 205 ? -62.759 -1.440  -12.875 1.00 15.72 ? 205  ASP B N   1 
ATOM   4898 C  CA  . ASP B  1 205 ? -62.566 -2.885  -12.636 1.00 16.07 ? 205  ASP B CA  1 
ATOM   4899 C  C   . ASP B  1 205 ? -63.392 -3.300  -11.419 1.00 15.55 ? 205  ASP B C   1 
ATOM   4900 O  O   . ASP B  1 205 ? -64.070 -4.350  -11.494 1.00 14.85 ? 205  ASP B O   1 
ATOM   4901 C  CB  . ASP B  1 205 ? -61.085 -3.211  -12.559 1.00 18.90 ? 205  ASP B CB  1 
ATOM   4902 C  CG  . ASP B  1 205 ? -60.418 -3.036  -13.928 1.00 25.15 ? 205  ASP B CG  1 
ATOM   4903 O  OD1 . ASP B  1 205 ? -61.154 -2.783  -14.955 1.00 26.34 ? 205  ASP B OD1 1 
ATOM   4904 O  OD2 . ASP B  1 205 ? -59.176 -3.149  -13.975 1.00 25.87 ? 205  ASP B OD2 1 
ATOM   4905 N  N   . LEU B  1 206 ? -63.391 -2.472  -10.376 1.00 12.98 ? 206  LEU B N   1 
ATOM   4906 C  CA  . LEU B  1 206 ? -64.198 -2.773  -9.154  1.00 13.45 ? 206  LEU B CA  1 
ATOM   4907 C  C   . LEU B  1 206 ? -65.692 -2.806  -9.533  1.00 12.77 ? 206  LEU B C   1 
ATOM   4908 O  O   . LEU B  1 206 ? -66.418 -3.694  -9.111  1.00 11.86 ? 206  LEU B O   1 
ATOM   4909 C  CB  . LEU B  1 206 ? -63.901 -1.704  -8.113  1.00 13.80 ? 206  LEU B CB  1 
ATOM   4910 C  CG  . LEU B  1 206 ? -64.471 -1.932  -6.716  1.00 15.56 ? 206  LEU B CG  1 
ATOM   4911 C  CD1 . LEU B  1 206 ? -65.814 -1.291  -6.594  1.00 16.23 ? 206  LEU B CD1 1 
ATOM   4912 C  CD2 . LEU B  1 206 ? -64.539 -3.386  -6.309  1.00 15.05 ? 206  LEU B CD2 1 
ATOM   4913 N  N   . LYS B  1 207 ? -66.164 -1.831  -10.292 1.00 12.66 ? 207  LYS B N   1 
ATOM   4914 C  CA  . LYS B  1 207 ? -67.607 -1.776  -10.629 1.00 13.31 ? 207  LYS B CA  1 
ATOM   4915 C  C   . LYS B  1 207 ? -67.971 -2.954  -11.542 1.00 14.43 ? 207  LYS B C   1 
ATOM   4916 O  O   . LYS B  1 207 ? -69.087 -3.487  -11.379 1.00 14.68 ? 207  LYS B O   1 
ATOM   4917 C  CB  . LYS B  1 207 ? -67.908 -0.399  -11.211 1.00 14.14 ? 207  LYS B CB  1 
ATOM   4918 C  CG  . LYS B  1 207 ? -67.908 0.676   -10.139 1.00 14.62 ? 207  LYS B CG  1 
ATOM   4919 C  CD  . LYS B  1 207 ? -68.319 2.020   -10.638 1.00 16.49 ? 207  LYS B CD  1 
ATOM   4920 C  CE  . LYS B  1 207 ? -68.103 3.105   -9.616  1.00 17.43 ? 207  LYS B CE  1 
ATOM   4921 N  NZ  . LYS B  1 207 ? -69.067 3.007   -8.498  1.00 18.98 ? 207  LYS B NZ  1 
ATOM   4922 N  N   . THR B  1 208 ? -67.075 -3.362  -12.439 1.00 14.72 ? 208  THR B N   1 
ATOM   4923 C  CA  . THR B  1 208 ? -67.258 -4.554  -13.292 1.00 15.24 ? 208  THR B CA  1 
ATOM   4924 C  C   . THR B  1 208 ? -67.352 -5.778  -12.388 1.00 14.93 ? 208  THR B C   1 
ATOM   4925 O  O   . THR B  1 208 ? -68.232 -6.680  -12.623 1.00 14.05 ? 208  THR B O   1 
ATOM   4926 C  CB  . THR B  1 208 ? -66.175 -4.654  -14.372 1.00 17.71 ? 208  THR B CB  1 
ATOM   4927 O  OG1 . THR B  1 208 ? -66.309 -3.450  -15.135 1.00 18.43 ? 208  THR B OG1 1 
ATOM   4928 C  CG2 . THR B  1 208 ? -66.328 -5.919  -15.186 1.00 18.12 ? 208  THR B CG2 1 
ATOM   4929 N  N   . LEU B  1 209 ? -66.483 -5.845  -11.399 1.00 13.92 ? 209  LEU B N   1 
ATOM   4930 C  CA  . LEU B  1 209 ? -66.416 -7.003  -10.488 1.00 13.78 ? 209  LEU B CA  1 
ATOM   4931 C  C   . LEU B  1 209 ? -67.698 -7.076  -9.651  1.00 13.77 ? 209  LEU B C   1 
ATOM   4932 O  O   . LEU B  1 209 ? -68.305 -8.177  -9.578  1.00 13.29 ? 209  LEU B O   1 
ATOM   4933 C  CB  . LEU B  1 209 ? -65.160 -6.863  -9.644  1.00 14.66 ? 209  LEU B CB  1 
ATOM   4934 C  CG  . LEU B  1 209 ? -64.959 -7.889  -8.552  1.00 15.49 ? 209  LEU B CG  1 
ATOM   4935 C  CD1 . LEU B  1 209 ? -64.858 -9.275  -9.163  1.00 16.52 ? 209  LEU B CD1 1 
ATOM   4936 C  CD2 . LEU B  1 209 ? -63.675 -7.543  -7.787  1.00 15.54 ? 209  LEU B CD2 1 
ATOM   4937 N  N   . GLU B  1 210 ? -68.156 -5.972  -9.068  1.00 12.36 ? 210  GLU B N   1 
ATOM   4938 C  CA  . GLU B  1 210 ? -69.476 -5.961  -8.385  1.00 13.20 ? 210  GLU B CA  1 
ATOM   4939 C  C   . GLU B  1 210 ? -70.529 -6.533  -9.344  1.00 13.39 ? 210  GLU B C   1 
ATOM   4940 O  O   . GLU B  1 210 ? -71.343 -7.397  -8.914  1.00 12.50 ? 210  GLU B O   1 
ATOM   4941 C  CB  . GLU B  1 210 ? -69.877 -4.562  -7.939  1.00 13.02 ? 210  GLU B CB  1 
ATOM   4942 C  CG  . GLU B  1 210 ? -69.051 -3.983  -6.830  1.00 14.41 ? 210  GLU B CG  1 
ATOM   4943 C  CD  . GLU B  1 210 ? -69.432 -2.531  -6.558  1.00 14.53 ? 210  GLU B CD  1 
ATOM   4944 O  OE1 . GLU B  1 210 ? -69.575 -1.765  -7.547  1.00 15.82 ? 210  GLU B OE1 1 
ATOM   4945 O  OE2 . GLU B  1 210 ? -69.722 -2.211  -5.424  1.00 14.78 ? 210  GLU B OE2 1 
ATOM   4946 N  N   . ARG B  1 211 ? -70.588 -6.048  -10.588 1.00 13.08 ? 211  ARG B N   1 
ATOM   4947 C  CA  . ARG B  1 211 ? -71.670 -6.504  -11.488 1.00 15.01 ? 211  ARG B CA  1 
ATOM   4948 C  C   . ARG B  1 211 ? -71.531 -8.002  -11.750 1.00 13.86 ? 211  ARG B C   1 
ATOM   4949 O  O   . ARG B  1 211 ? -72.569 -8.708  -11.797 1.00 13.74 ? 211  ARG B O   1 
ATOM   4950 C  CB  . ARG B  1 211 ? -71.709 -5.727  -12.795 1.00 17.66 ? 211  ARG B CB  1 
ATOM   4951 C  CG  . ARG B  1 211 ? -72.199 -4.299  -12.615 1.00 18.91 ? 211  ARG B CG  1 
ATOM   4952 C  CD  . ARG B  1 211 ? -72.476 -3.643  -13.978 1.00 24.17 ? 211  ARG B CD  1 
ATOM   4953 N  NE  . ARG B  1 211 ? -71.317 -3.559  -14.853 1.00 27.78 ? 211  ARG B NE  1 
ATOM   4954 C  CZ  . ARG B  1 211 ? -70.395 -2.571  -14.866 1.00 32.76 ? 211  ARG B CZ  1 
ATOM   4955 N  NH1 . ARG B  1 211 ? -70.445 -1.552  -14.023 1.00 32.55 ? 211  ARG B NH1 1 
ATOM   4956 N  NH2 . ARG B  1 211 ? -69.402 -2.620  -15.734 1.00 34.19 ? 211  ARG B NH2 1 
ATOM   4957 N  N   . SER B  1 212 ? -70.313 -8.484  -11.911 1.00 13.94 ? 212  SER B N   1 
ATOM   4958 C  CA  . SER B  1 212 ? -70.050 -9.897  -12.252 1.00 14.79 ? 212  SER B CA  1 
ATOM   4959 C  C   . SER B  1 212 ? -70.547 -10.787 -11.102 1.00 14.26 ? 212  SER B C   1 
ATOM   4960 O  O   . SER B  1 212 ? -70.928 -11.943 -11.385 1.00 14.69 ? 212  SER B O   1 
ATOM   4961 C  CB  . SER B  1 212 ? -68.565 -10.142 -12.560 1.00 16.97 ? 212  SER B CB  1 
ATOM   4962 O  OG  . SER B  1 212 ? -67.800 -10.246 -11.363 1.00 18.81 ? 212  SER B OG  1 
ATOM   4963 N  N   . LEU B  1 213 ? -70.504 -10.294 -9.853  1.00 13.09 ? 213  LEU B N   1 
ATOM   4964 C  CA  . LEU B  1 213 ? -70.845 -11.079 -8.632  1.00 12.73 ? 213  LEU B CA  1 
ATOM   4965 C  C   . LEU B  1 213 ? -72.306 -10.849 -8.204  1.00 12.55 ? 213  LEU B C   1 
ATOM   4966 O  O   . LEU B  1 213 ? -72.737 -11.459 -7.213  1.00 12.40 ? 213  LEU B O   1 
ATOM   4967 C  CB  . LEU B  1 213 ? -69.855 -10.707 -7.526  1.00 12.98 ? 213  LEU B CB  1 
ATOM   4968 C  CG  . LEU B  1 213 ? -68.387 -11.081 -7.804  1.00 13.26 ? 213  LEU B CG  1 
ATOM   4969 C  CD1 . LEU B  1 213 ? -67.528 -10.769 -6.585  1.00 13.67 ? 213  LEU B CD1 1 
ATOM   4970 C  CD2 . LEU B  1 213 ? -68.209 -12.565 -8.181  1.00 13.76 ? 213  LEU B CD2 1 
ATOM   4971 N  N   . GLY B  1 214 ? -72.998 -9.937  -8.873  1.00 12.08 ? 214  GLY B N   1 
ATOM   4972 C  CA  . GLY B  1 214 ? -74.393 -9.605  -8.524  1.00 11.80 ? 214  GLY B CA  1 
ATOM   4973 C  C   . GLY B  1 214 ? -74.478 -8.761  -7.248  1.00 12.81 ? 214  GLY B C   1 
ATOM   4974 O  O   . GLY B  1 214 ? -75.502 -8.867  -6.513  1.00 14.48 ? 214  GLY B O   1 
ATOM   4975 N  N   . ILE B  1 215 ? -73.449 -7.975  -6.941  1.00 11.77 ? 215  ILE B N   1 
ATOM   4976 C  CA  . ILE B  1 215 ? -73.400 -7.130  -5.700  1.00 11.65 ? 215  ILE B CA  1 
ATOM   4977 C  C   . ILE B  1 215 ? -73.918 -5.741  -6.017  1.00 12.23 ? 215  ILE B C   1 
ATOM   4978 O  O   . ILE B  1 215 ? -73.378 -5.101  -6.903  1.00 12.24 ? 215  ILE B O   1 
ATOM   4979 C  CB  . ILE B  1 215 ? -71.960 -7.075  -5.164  1.00 11.86 ? 215  ILE B CB  1 
ATOM   4980 C  CG1 . ILE B  1 215 ? -71.529 -8.477  -4.716  1.00 12.45 ? 215  ILE B CG1 1 
ATOM   4981 C  CG2 . ILE B  1 215 ? -71.834 -6.036  -4.063  1.00 11.59 ? 215  ILE B CG2 1 
ATOM   4982 C  CD1 . ILE B  1 215 ? -70.067 -8.628  -4.497  1.00 13.16 ? 215  ILE B CD1 1 
ATOM   4983 N  N   . PRO B  1 216 ? -74.961 -5.243  -5.307  1.00 12.24 ? 216  PRO B N   1 
ATOM   4984 C  CA  . PRO B  1 216 ? -75.392 -3.854  -5.425  1.00 12.60 ? 216  PRO B CA  1 
ATOM   4985 C  C   . PRO B  1 216 ? -74.215 -2.877  -5.276  1.00 13.45 ? 216  PRO B C   1 
ATOM   4986 O  O   . PRO B  1 216 ? -73.399 -3.028  -4.373  1.00 12.99 ? 216  PRO B O   1 
ATOM   4987 C  CB  . PRO B  1 216 ? -76.379 -3.711  -4.255  1.00 12.64 ? 216  PRO B CB  1 
ATOM   4988 C  CG  . PRO B  1 216 ? -76.982 -5.091  -4.127  1.00 12.45 ? 216  PRO B CG  1 
ATOM   4989 C  CD  . PRO B  1 216 ? -75.797 -6.005  -4.365  1.00 12.96 ? 216  PRO B CD  1 
ATOM   4990 N  N   . GLU B  1 217 ? -74.138 -1.932  -6.214  1.00 13.15 ? 217  GLU B N   1 
ATOM   4991 C  CA  . GLU B  1 217 ? -73.014 -0.987  -6.335  1.00 13.25 ? 217  GLU B CA  1 
ATOM   4992 C  C   . GLU B  1 217 ? -72.821 -0.279  -4.981  1.00 12.27 ? 217  GLU B C   1 
ATOM   4993 O  O   . GLU B  1 217 ? -73.806 0.281   -4.411  1.00 13.52 ? 217  GLU B O   1 
ATOM   4994 C  CB  . GLU B  1 217 ? -73.307 -0.024  -7.474  1.00 14.28 ? 217  GLU B CB  1 
ATOM   4995 C  CG  . GLU B  1 217 ? -72.249 1.014   -7.697  1.00 16.81 ? 217  GLU B CG  1 
ATOM   4996 C  CD  . GLU B  1 217 ? -72.634 2.010   -8.773  1.00 20.33 ? 217  GLU B CD  1 
ATOM   4997 O  OE1 . GLU B  1 217 ? -73.854 2.134   -9.033  1.00 21.93 ? 217  GLU B OE1 1 
ATOM   4998 O  OE2 . GLU B  1 217 ? -71.735 2.676   -9.301  1.00 22.11 ? 217  GLU B OE2 1 
ATOM   4999 N  N   . ARG B  1 218 ? -71.576 -0.286  -4.501  1.00 12.43 ? 218  ARG B N   1 
ATOM   5000 C  CA  . ARG B  1 218 ? -71.195 0.273   -3.182  1.00 12.58 ? 218  ARG B CA  1 
ATOM   5001 C  C   . ARG B  1 218 ? -70.561 1.650   -3.410  1.00 11.64 ? 218  ARG B C   1 
ATOM   5002 O  O   . ARG B  1 218 ? -69.890 1.904   -4.415  1.00 10.80 ? 218  ARG B O   1 
ATOM   5003 C  CB  . ARG B  1 218 ? -70.216 -0.626  -2.413  1.00 12.69 ? 218  ARG B CB  1 
ATOM   5004 C  CG  . ARG B  1 218 ? -70.766 -1.959  -1.928  1.00 13.51 ? 218  ARG B CG  1 
ATOM   5005 C  CD  . ARG B  1 218 ? -72.126 -1.843  -1.287  1.00 13.19 ? 218  ARG B CD  1 
ATOM   5006 N  NE  . ARG B  1 218 ? -72.414 -2.864  -0.284  1.00 13.05 ? 218  ARG B NE  1 
ATOM   5007 C  CZ  . ARG B  1 218 ? -73.331 -3.813  -0.416  1.00 13.44 ? 218  ARG B CZ  1 
ATOM   5008 N  NH1 . ARG B  1 218 ? -73.896 -4.041  -1.588  1.00 14.10 ? 218  ARG B NH1 1 
ATOM   5009 N  NH2 . ARG B  1 218 ? -73.603 -4.599  0.595   1.00 14.41 ? 218  ARG B NH2 1 
ATOM   5010 N  N   . LYS B  1 219 ? -70.670 2.497   -2.415  1.00 12.15 ? 219  LYS B N   1 
ATOM   5011 C  CA  . LYS B  1 219 ? -69.801 3.690   -2.320  1.00 12.14 ? 219  LYS B CA  1 
ATOM   5012 C  C   . LYS B  1 219 ? -68.336 3.272   -2.288  1.00 11.58 ? 219  LYS B C   1 
ATOM   5013 O  O   . LYS B  1 219 ? -68.018 2.192   -1.825  1.00 10.60 ? 219  LYS B O   1 
ATOM   5014 C  CB  . LYS B  1 219 ? -70.103 4.396   -1.008  1.00 13.30 ? 219  LYS B CB  1 
ATOM   5015 C  CG  . LYS B  1 219 ? -71.418 5.152   -0.994  1.00 14.82 ? 219  LYS B CG  1 
ATOM   5016 C  CD  . LYS B  1 219 ? -71.779 5.602   0.394   1.00 15.52 ? 219  LYS B CD  1 
ATOM   5017 C  CE  . LYS B  1 219 ? -73.021 6.462   0.436   1.00 18.09 ? 219  LYS B CE  1 
ATOM   5018 N  NZ  . LYS B  1 219 ? -73.247 6.921   1.826   1.00 19.38 ? 219  LYS B NZ  1 
ATOM   5019 N  N   . ILE B  1 220 ? -67.464 4.164   -2.712  1.00 11.13 ? 220  ILE B N   1 
ATOM   5020 C  CA  . ILE B  1 220 ? -66.001 3.920   -2.739  1.00 11.12 ? 220  ILE B CA  1 
ATOM   5021 C  C   . ILE B  1 220 ? -65.317 4.958   -1.847  1.00 10.45 ? 220  ILE B C   1 
ATOM   5022 O  O   . ILE B  1 220 ? -65.605 6.144   -1.962  1.00 10.77 ? 220  ILE B O   1 
ATOM   5023 C  CB  . ILE B  1 220 ? -65.487 3.961   -4.196  1.00 11.35 ? 220  ILE B CB  1 
ATOM   5024 C  CG1 . ILE B  1 220 ? -66.094 2.831   -5.012  1.00 11.90 ? 220  ILE B CG1 1 
ATOM   5025 C  CG2 . ILE B  1 220 ? -63.967 3.882   -4.244  1.00 11.31 ? 220  ILE B CG2 1 
ATOM   5026 C  CD1 . ILE B  1 220 ? -65.855 2.936   -6.509  1.00 12.87 ? 220  ILE B CD1 1 
ATOM   5027 N  N   . ALA B  1 221 ? -64.371 4.508   -1.041  1.00 10.02 ? 221  ALA B N   1 
ATOM   5028 C  CA  . ALA B  1 221 ? -63.453 5.377   -0.314  1.00 9.90  ? 221  ALA B CA  1 
ATOM   5029 C  C   . ALA B  1 221 ? -62.045 4.970   -0.708  1.00 9.87  ? 221  ALA B C   1 
ATOM   5030 O  O   . ALA B  1 221 ? -61.716 3.793   -0.668  1.00 11.86 ? 221  ALA B O   1 
ATOM   5031 C  CB  . ALA B  1 221 ? -63.650 5.294   1.182   1.00 10.25 ? 221  ALA B CB  1 
ATOM   5032 N  N   . ILE B  1 222 ? -61.216 5.952   -0.953  1.00 10.08 ? 222  ILE B N   1 
ATOM   5033 C  CA  . ILE B  1 222 ? -59.759 5.750   -1.200  1.00 10.09 ? 222  ILE B CA  1 
ATOM   5034 C  C   . ILE B  1 222 ? -59.057 6.488   -0.061  1.00 9.69  ? 222  ILE B C   1 
ATOM   5035 O  O   . ILE B  1 222 ? -58.679 7.649   -0.242  1.00 10.01 ? 222  ILE B O   1 
ATOM   5036 C  CB  . ILE B  1 222 ? -59.356 6.230   -2.611  1.00 9.87  ? 222  ILE B CB  1 
ATOM   5037 C  CG1 . ILE B  1 222 ? -60.197 5.594   -3.724  1.00 11.36 ? 222  ILE B CG1 1 
ATOM   5038 C  CG2 . ILE B  1 222 ? -57.875 5.991   -2.825  1.00 10.08 ? 222  ILE B CG2 1 
ATOM   5039 C  CD1 . ILE B  1 222 ? -60.048 4.123   -3.858  1.00 11.64 ? 222  ILE B CD1 1 
ATOM   5040 N  N   . ASN B  1 223 ? -58.927 5.851   1.111   1.00 10.59 ? 223  ASN B N   1 
ATOM   5041 C  CA  . ASN B  1 223 ? -58.614 6.612   2.346   1.00 11.00 ? 223  ASN B CA  1 
ATOM   5042 C  C   . ASN B  1 223 ? -57.109 6.773   2.567   1.00 10.34 ? 223  ASN B C   1 
ATOM   5043 O  O   . ASN B  1 223 ? -56.741 7.295   3.617   1.00 10.69 ? 223  ASN B O   1 
ATOM   5044 C  CB  . ASN B  1 223 ? -59.374 6.107   3.566   1.00 11.10 ? 223  ASN B CB  1 
ATOM   5045 C  CG  . ASN B  1 223 ? -58.922 4.785   4.118   1.00 12.36 ? 223  ASN B CG  1 
ATOM   5046 O  OD1 . ASN B  1 223 ? -58.260 4.029   3.415   1.00 12.07 ? 223  ASN B OD1 1 
ATOM   5047 N  ND2 . ASN B  1 223 ? -59.313 4.520   5.366   1.00 12.42 ? 223  ASN B ND2 1 
ATOM   5048 N  N   . GLU B  1 224 ? -56.269 6.421   1.589   1.00 9.70  ? 224  GLU B N   1 
ATOM   5049 C  CA  . GLU B  1 224 ? -54.851 6.879   1.558   1.00 9.85  ? 224  GLU B CA  1 
ATOM   5050 C  C   . GLU B  1 224 ? -54.458 7.051   0.093   1.00 9.73  ? 224  GLU B C   1 
ATOM   5051 O  O   . GLU B  1 224 ? -54.634 6.089   -0.695  1.00 9.40  ? 224  GLU B O   1 
ATOM   5052 C  CB  . GLU B  1 224 ? -53.890 5.916   2.228   1.00 10.12 ? 224  GLU B CB  1 
ATOM   5053 C  CG  . GLU B  1 224 ? -54.209 5.556   3.647   1.00 10.26 ? 224  GLU B CG  1 
ATOM   5054 C  CD  . GLU B  1 224 ? -53.231 4.619   4.343   1.00 11.06 ? 224  GLU B CD  1 
ATOM   5055 O  OE1 . GLU B  1 224 ? -52.014 4.688   4.034   1.00 11.91 ? 224  GLU B OE1 1 
ATOM   5056 O  OE2 . GLU B  1 224 ? -53.674 3.894   5.284   1.00 11.78 ? 224  GLU B OE2 1 
ATOM   5057 N  N   . TYR B  1 225 ? -54.033 8.239   -0.302  1.00 10.25 ? 225  TYR B N   1 
ATOM   5058 C  CA  . TYR B  1 225 ? -53.596 8.463   -1.689  1.00 10.34 ? 225  TYR B CA  1 
ATOM   5059 C  C   . TYR B  1 225 ? -52.346 9.337   -1.736  1.00 11.10 ? 225  TYR B C   1 
ATOM   5060 O  O   . TYR B  1 225 ? -52.242 10.377  -1.011  1.00 10.76 ? 225  TYR B O   1 
ATOM   5061 C  CB  . TYR B  1 225 ? -54.721 8.987   -2.582  1.00 10.76 ? 225  TYR B CB  1 
ATOM   5062 C  CG  . TYR B  1 225 ? -55.205 10.394  -2.377  1.00 10.57 ? 225  TYR B CG  1 
ATOM   5063 C  CD1 . TYR B  1 225 ? -54.600 11.464  -3.034  1.00 10.78 ? 225  TYR B CD1 1 
ATOM   5064 C  CD2 . TYR B  1 225 ? -56.345 10.655  -1.628  1.00 10.43 ? 225  TYR B CD2 1 
ATOM   5065 C  CE1 . TYR B  1 225 ? -55.101 12.749  -2.892  1.00 11.76 ? 225  TYR B CE1 1 
ATOM   5066 C  CE2 . TYR B  1 225 ? -56.883 11.927  -1.518  1.00 10.88 ? 225  TYR B CE2 1 
ATOM   5067 C  CZ  . TYR B  1 225 ? -56.229 12.996  -2.130  1.00 11.70 ? 225  TYR B CZ  1 
ATOM   5068 O  OH  . TYR B  1 225 ? -56.729 14.278  -2.010  1.00 11.90 ? 225  TYR B OH  1 
ATOM   5069 N  N   . SER B  1 226 ? -51.449 8.953   -2.637  1.00 10.07 ? 226  SER B N   1 
ATOM   5070 C  CA  . SER B  1 226 ? -50.222 9.737   -2.939  1.00 11.03 ? 226  SER B CA  1 
ATOM   5071 C  C   . SER B  1 226 ? -49.524 9.202   -4.174  1.00 11.63 ? 226  SER B C   1 
ATOM   5072 O  O   . SER B  1 226 ? -49.742 8.047   -4.585  1.00 10.25 ? 226  SER B O   1 
ATOM   5073 C  CB  . SER B  1 226 ? -49.235 9.742   -1.800  1.00 11.88 ? 226  SER B CB  1 
ATOM   5074 O  OG  . SER B  1 226 ? -48.568 8.486   -1.719  1.00 12.97 ? 226  SER B OG  1 
ATOM   5075 N  N   . ASP B  1 227 ? -48.648 10.047  -4.691  1.00 11.87 ? 227  ASP B N   1 
ATOM   5076 C  CA  . ASP B  1 227 ? -47.590 9.660   -5.650  1.00 12.76 ? 227  ASP B CA  1 
ATOM   5077 C  C   . ASP B  1 227 ? -46.677 8.628   -4.994  1.00 11.67 ? 227  ASP B C   1 
ATOM   5078 O  O   . ASP B  1 227 ? -46.619 8.539   -3.741  1.00 11.29 ? 227  ASP B O   1 
ATOM   5079 C  CB  . ASP B  1 227 ? -46.790 10.894  -6.053  1.00 12.78 ? 227  ASP B CB  1 
ATOM   5080 C  CG  . ASP B  1 227 ? -45.917 10.707  -7.279  1.00 12.66 ? 227  ASP B CG  1 
ATOM   5081 O  OD1 . ASP B  1 227 ? -46.467 10.685  -8.385  1.00 13.35 ? 227  ASP B OD1 1 
ATOM   5082 O  OD2 . ASP B  1 227 ? -44.678 10.622  -7.100  1.00 13.41 ? 227  ASP B OD2 1 
ATOM   5083 N  N   . SER B  1 228 ? -45.962 7.850   -5.810  1.00 12.91 ? 228  SER B N   1 
ATOM   5084 C  CA  . SER B  1 228 ? -44.923 6.900   -5.352  1.00 12.56 ? 228  SER B CA  1 
ATOM   5085 C  C   . SER B  1 228 ? -43.794 7.630   -4.616  1.00 13.30 ? 228  SER B C   1 
ATOM   5086 O  O   . SER B  1 228 ? -43.145 7.036   -3.721  1.00 14.17 ? 228  SER B O   1 
ATOM   5087 C  CB  . SER B  1 228 ? -44.393 6.083   -6.519  1.00 12.11 ? 228  SER B CB  1 
ATOM   5088 O  OG  . SER B  1 228 ? -45.378 5.116   -6.875  1.00 11.40 ? 228  SER B OG  1 
ATOM   5089 N  N   . ASN B  1 229 ? -43.607 8.893   -4.952  1.00 12.62 ? 229  ASN B N   1 
ATOM   5090 C  CA  . ASN B  1 229 ? -42.658 9.783   -4.252  1.00 12.97 ? 229  ASN B CA  1 
ATOM   5091 C  C   . ASN B  1 229 ? -43.360 10.391  -3.044  1.00 12.22 ? 229  ASN B C   1 
ATOM   5092 O  O   . ASN B  1 229 ? -44.262 11.241  -3.238  1.00 12.68 ? 229  ASN B O   1 
ATOM   5093 C  CB  . ASN B  1 229 ? -42.183 10.884  -5.191  1.00 13.01 ? 229  ASN B CB  1 
ATOM   5094 C  CG  . ASN B  1 229 ? -41.406 11.955  -4.449  1.00 12.85 ? 229  ASN B CG  1 
ATOM   5095 O  OD1 . ASN B  1 229 ? -41.003 11.749  -3.302  1.00 13.47 ? 229  ASN B OD1 1 
ATOM   5096 N  ND2 . ASN B  1 229 ? -41.218 13.085  -5.093  1.00 13.28 ? 229  ASN B ND2 1 
ATOM   5097 N  N   . HIS B  1 230 ? -43.016 9.950   -1.848  1.00 12.71 ? 230  HIS B N   1 
ATOM   5098 C  CA  . HIS B  1 230 ? -43.704 10.351  -0.609  1.00 12.57 ? 230  HIS B CA  1 
ATOM   5099 C  C   . HIS B  1 230 ? -43.503 11.850  -0.348  1.00 12.86 ? 230  HIS B C   1 
ATOM   5100 O  O   . HIS B  1 230 ? -44.344 12.440  0.331   1.00 11.72 ? 230  HIS B O   1 
ATOM   5101 C  CB  . HIS B  1 230 ? -43.281 9.440   0.545   1.00 13.72 ? 230  HIS B CB  1 
ATOM   5102 C  CG  . HIS B  1 230 ? -43.561 8.008   0.268   1.00 15.13 ? 230  HIS B CG  1 
ATOM   5103 N  ND1 . HIS B  1 230 ? -43.024 6.986   1.024   1.00 16.29 ? 230  HIS B ND1 1 
ATOM   5104 C  CD2 . HIS B  1 230 ? -44.357 7.427   -0.666  1.00 16.66 ? 230  HIS B CD2 1 
ATOM   5105 C  CE1 . HIS B  1 230 ? -43.440 5.834   0.544   1.00 17.31 ? 230  HIS B CE1 1 
ATOM   5106 N  NE2 . HIS B  1 230 ? -44.252 6.073   -0.506  1.00 16.15 ? 230  HIS B NE2 1 
ATOM   5107 N  N   . TYR B  1 231 ? -42.439 12.460  -0.871  1.00 13.50 ? 231  TYR B N   1 
ATOM   5108 C  CA  . TYR B  1 231 ? -42.234 13.919  -0.716  1.00 14.50 ? 231  TYR B CA  1 
ATOM   5109 C  C   . TYR B  1 231 ? -43.253 14.712  -1.542  1.00 15.27 ? 231  TYR B C   1 
ATOM   5110 O  O   . TYR B  1 231 ? -43.353 15.942  -1.289  1.00 15.35 ? 231  TYR B O   1 
ATOM   5111 C  CB  . TYR B  1 231 ? -40.789 14.303  -1.043  1.00 15.11 ? 231  TYR B CB  1 
ATOM   5112 C  CG  . TYR B  1 231 ? -39.849 13.965  0.078   1.00 16.16 ? 231  TYR B CG  1 
ATOM   5113 C  CD1 . TYR B  1 231 ? -39.770 14.785  1.191   1.00 17.88 ? 231  TYR B CD1 1 
ATOM   5114 C  CD2 . TYR B  1 231 ? -39.034 12.847  0.035   1.00 18.17 ? 231  TYR B CD2 1 
ATOM   5115 C  CE1 . TYR B  1 231 ? -38.898 14.515  2.230   1.00 20.00 ? 231  TYR B CE1 1 
ATOM   5116 C  CE2 . TYR B  1 231 ? -38.177 12.547  1.084   1.00 20.76 ? 231  TYR B CE2 1 
ATOM   5117 C  CZ  . TYR B  1 231 ? -38.090 13.402  2.175   1.00 19.99 ? 231  TYR B CZ  1 
ATOM   5118 O  OH  . TYR B  1 231 ? -37.268 13.126  3.230   1.00 21.48 ? 231  TYR B OH  1 
ATOM   5119 N  N   . ALA B  1 232 ? -44.036 14.073  -2.435  1.00 13.59 ? 232  ALA B N   1 
ATOM   5120 C  CA  . ALA B  1 232 ? -45.041 14.783  -3.254  1.00 13.26 ? 232  ALA B CA  1 
ATOM   5121 C  C   . ALA B  1 232 ? -46.421 14.671  -2.592  1.00 13.36 ? 232  ALA B C   1 
ATOM   5122 O  O   . ALA B  1 232 ? -47.404 15.128  -3.169  1.00 12.98 ? 232  ALA B O   1 
ATOM   5123 C  CB  . ALA B  1 232 ? -45.028 14.256  -4.660  1.00 13.65 ? 232  ALA B CB  1 
ATOM   5124 N  N   . GLU B  1 233 ? -46.483 14.141  -1.374  1.00 12.00 ? 233  GLU B N   1 
ATOM   5125 C  CA  . GLU B  1 233 ? -47.751 14.156  -0.588  1.00 12.10 ? 233  GLU B CA  1 
ATOM   5126 C  C   . GLU B  1 233 ? -48.133 15.629  -0.413  1.00 12.52 ? 233  GLU B C   1 
ATOM   5127 O  O   . GLU B  1 233 ? -47.236 16.417  -0.082  1.00 12.35 ? 233  GLU B O   1 
ATOM   5128 C  CB  . GLU B  1 233 ? -47.501 13.513  0.763   1.00 11.88 ? 233  GLU B CB  1 
ATOM   5129 C  CG  . GLU B  1 233 ? -48.733 13.402  1.621   1.00 11.69 ? 233  GLU B CG  1 
ATOM   5130 C  CD  . GLU B  1 233 ? -48.421 12.819  2.973   1.00 11.94 ? 233  GLU B CD  1 
ATOM   5131 O  OE1 . GLU B  1 233 ? -48.284 11.584  3.051   1.00 11.72 ? 233  GLU B OE1 1 
ATOM   5132 O  OE2 . GLU B  1 233 ? -48.299 13.623  3.951   1.00 14.27 ? 233  GLU B OE2 1 
ATOM   5133 N  N   . GLY B  1 234 ? -49.376 16.009  -0.695  1.00 11.65 ? 234  GLY B N   1 
ATOM   5134 C  CA  . GLY B  1 234 ? -49.829 17.406  -0.513  1.00 12.82 ? 234  GLY B CA  1 
ATOM   5135 C  C   . GLY B  1 234 ? -49.341 18.342  -1.613  1.00 13.07 ? 234  GLY B C   1 
ATOM   5136 O  O   . GLY B  1 234 ? -49.663 19.547  -1.543  1.00 15.25 ? 234  GLY B O   1 
ATOM   5137 N  N   . GLN B  1 235 ? -48.611 17.860  -2.616  1.00 13.04 ? 235  GLN B N   1 
ATOM   5138 C  CA  . GLN B  1 235 ? -48.106 18.736  -3.702  1.00 13.10 ? 235  GLN B CA  1 
ATOM   5139 C  C   . GLN B  1 235 ? -49.265 19.070  -4.631  1.00 13.79 ? 235  GLN B C   1 
ATOM   5140 O  O   . GLN B  1 235 ? -49.950 18.162  -5.086  1.00 12.33 ? 235  GLN B O   1 
ATOM   5141 C  CB  . GLN B  1 235 ? -46.950 18.089  -4.436  1.00 13.66 ? 235  GLN B CB  1 
ATOM   5142 C  CG  . GLN B  1 235 ? -46.430 18.920  -5.584  1.00 14.00 ? 235  GLN B CG  1 
ATOM   5143 C  CD  . GLN B  1 235 ? -45.619 18.052  -6.500  1.00 14.00 ? 235  GLN B CD  1 
ATOM   5144 O  OE1 . GLN B  1 235 ? -44.446 17.726  -6.204  1.00 20.12 ? 235  GLN B OE1 1 
ATOM   5145 N  NE2 . GLN B  1 235 ? -46.198 17.735  -7.635  1.00 12.25 ? 235  GLN B NE2 1 
ATOM   5146 N  N   . PRO B  1 236 ? -49.528 20.367  -4.950  1.00 13.53 ? 236  PRO B N   1 
ATOM   5147 C  CA  . PRO B  1 236 ? -50.654 20.717  -5.819  1.00 14.10 ? 236  PRO B CA  1 
ATOM   5148 C  C   . PRO B  1 236 ? -50.675 19.956  -7.166  1.00 13.80 ? 236  PRO B C   1 
ATOM   5149 O  O   . PRO B  1 236 ? -51.717 19.366  -7.581  1.00 13.71 ? 236  PRO B O   1 
ATOM   5150 C  CB  . PRO B  1 236 ? -50.458 22.234  -6.068  1.00 14.29 ? 236  PRO B CB  1 
ATOM   5151 C  CG  . PRO B  1 236 ? -49.617 22.717  -4.910  1.00 15.04 ? 236  PRO B CG  1 
ATOM   5152 C  CD  . PRO B  1 236 ? -48.737 21.537  -4.516  1.00 15.01 ? 236  PRO B CD  1 
ATOM   5153 N  N   . GLY B  1 237 ? -49.529 19.939  -7.875  1.00 13.21 ? 237  GLY B N   1 
ATOM   5154 C  CA  . GLY B  1 237 ? -49.475 19.334  -9.220  1.00 12.26 ? 237  GLY B CA  1 
ATOM   5155 C  C   . GLY B  1 237 ? -49.725 17.822  -9.193  1.00 13.76 ? 237  GLY B C   1 
ATOM   5156 O  O   . GLY B  1 237 ? -50.598 17.340  -9.943  1.00 14.77 ? 237  GLY B O   1 
ATOM   5157 N  N   . ALA B  1 238 ? -48.984 17.082  -8.386  1.00 14.58 ? 238  ALA B N   1 
ATOM   5158 C  CA  . ALA B  1 238 ? -49.184 15.618  -8.220  1.00 14.38 ? 238  ALA B CA  1 
ATOM   5159 C  C   . ALA B  1 238 ? -50.612 15.342  -7.694  1.00 14.70 ? 238  ALA B C   1 
ATOM   5160 O  O   . ALA B  1 238 ? -51.197 14.315  -8.110  1.00 15.05 ? 238  ALA B O   1 
ATOM   5161 C  CB  . ALA B  1 238 ? -48.121 15.063  -7.312  1.00 14.34 ? 238  ALA B CB  1 
ATOM   5162 N  N   . SER B  1 239 ? -51.164 16.210  -6.842  1.00 12.77 ? 239  SER B N   1 
ATOM   5163 C  CA  . SER B  1 239 ? -52.490 15.973  -6.201  1.00 13.86 ? 239  SER B CA  1 
ATOM   5164 C  C   . SER B  1 239 ? -53.628 16.156  -7.213  1.00 13.46 ? 239  SER B C   1 
ATOM   5165 O  O   . SER B  1 239 ? -54.655 15.489  -7.096  1.00 11.88 ? 239  SER B O   1 
ATOM   5166 C  CB  . SER B  1 239 ? -52.688 16.854  -4.976  1.00 14.52 ? 239  SER B CB  1 
ATOM   5167 O  OG  . SER B  1 239 ? -51.734 16.619  -3.983  1.00 14.17 ? 239  SER B OG  1 
ATOM   5168 N  N   . ALA B  1 240 ? -53.505 17.051  -8.181  1.00 13.25 ? 240  ALA B N   1 
ATOM   5169 C  CA  . ALA B  1 240 ? -54.652 17.461  -9.008  1.00 13.05 ? 240  ALA B CA  1 
ATOM   5170 C  C   . ALA B  1 240 ? -55.241 16.285  -9.780  1.00 13.19 ? 240  ALA B C   1 
ATOM   5171 O  O   . ALA B  1 240 ? -56.460 16.149  -9.792  1.00 12.71 ? 240  ALA B O   1 
ATOM   5172 C  CB  . ALA B  1 240 ? -54.265 18.595  -9.921  1.00 14.04 ? 240  ALA B CB  1 
ATOM   5173 N  N   . PRO B  1 241 ? -54.446 15.395  -10.433 1.00 11.98 ? 241  PRO B N   1 
ATOM   5174 C  CA  . PRO B  1 241 ? -55.030 14.264  -11.141 1.00 12.31 ? 241  PRO B CA  1 
ATOM   5175 C  C   . PRO B  1 241 ? -55.700 13.238  -10.225 1.00 11.21 ? 241  PRO B C   1 
ATOM   5176 O  O   . PRO B  1 241 ? -56.625 12.607  -10.668 1.00 13.22 ? 241  PRO B O   1 
ATOM   5177 C  CB  . PRO B  1 241 ? -53.839 13.695  -11.924 1.00 12.08 ? 241  PRO B CB  1 
ATOM   5178 C  CG  . PRO B  1 241 ? -52.880 14.858  -12.047 1.00 11.94 ? 241  PRO B CG  1 
ATOM   5179 C  CD  . PRO B  1 241 ? -52.993 15.502  -10.681 1.00 11.95 ? 241  PRO B CD  1 
ATOM   5180 N  N   . PHE B  1 242 ? -55.324 13.153  -8.950  1.00 11.51 ? 242  PHE B N   1 
ATOM   5181 C  CA  . PHE B  1 242 ? -56.035 12.263  -8.007  1.00 11.30 ? 242  PHE B CA  1 
ATOM   5182 C  C   . PHE B  1 242 ? -57.432 12.844  -7.785  1.00 11.11 ? 242  PHE B C   1 
ATOM   5183 O  O   . PHE B  1 242 ? -58.397 12.145  -8.002  1.00 12.16 ? 242  PHE B O   1 
ATOM   5184 C  CB  . PHE B  1 242 ? -55.361 12.217  -6.653  1.00 11.67 ? 242  PHE B CB  1 
ATOM   5185 C  CG  . PHE B  1 242 ? -54.107 11.389  -6.612  1.00 11.78 ? 242  PHE B CG  1 
ATOM   5186 C  CD1 . PHE B  1 242 ? -54.164 10.051  -6.277  1.00 11.04 ? 242  PHE B CD1 1 
ATOM   5187 C  CD2 . PHE B  1 242 ? -52.866 11.956  -6.842  1.00 11.48 ? 242  PHE B CD2 1 
ATOM   5188 C  CE1 . PHE B  1 242 ? -53.002 9.288   -6.204  1.00 11.98 ? 242  PHE B CE1 1 
ATOM   5189 C  CE2 . PHE B  1 242 ? -51.713 11.184  -6.767  1.00 12.59 ? 242  PHE B CE2 1 
ATOM   5190 C  CZ  . PHE B  1 242 ? -51.782 9.851   -6.464  1.00 11.83 ? 242  PHE B CZ  1 
ATOM   5191 N  N   . ILE B  1 243 ? -57.492 14.122  -7.393  1.00 11.39 ? 243  ILE B N   1 
ATOM   5192 C  CA  . ILE B  1 243 ? -58.794 14.802  -7.150  1.00 11.54 ? 243  ILE B CA  1 
ATOM   5193 C  C   . ILE B  1 243 ? -59.647 14.722  -8.421  1.00 12.29 ? 243  ILE B C   1 
ATOM   5194 O  O   . ILE B  1 243 ? -60.843 14.394  -8.318  1.00 12.38 ? 243  ILE B O   1 
ATOM   5195 C  CB  . ILE B  1 243 ? -58.589 16.262  -6.712  1.00 11.91 ? 243  ILE B CB  1 
ATOM   5196 C  CG1 . ILE B  1 243 ? -57.719 16.362  -5.459  1.00 12.61 ? 243  ILE B CG1 1 
ATOM   5197 C  CG2 . ILE B  1 243 ? -59.967 16.924  -6.517  1.00 11.41 ? 243  ILE B CG2 1 
ATOM   5198 C  CD1 . ILE B  1 243 ? -57.139 17.758  -5.263  1.00 13.00 ? 243  ILE B CD1 1 
ATOM   5199 N  N   . ALA B  1 244 ? -59.063 15.038  -9.584  1.00 12.92 ? 244  ALA B N   1 
ATOM   5200 C  CA  . ALA B  1 244 ? -59.763 15.022  -10.891 1.00 12.39 ? 244  ALA B CA  1 
ATOM   5201 C  C   . ALA B  1 244 ? -60.469 13.661  -11.081 1.00 13.23 ? 244  ALA B C   1 
ATOM   5202 O  O   . ALA B  1 244 ? -61.658 13.632  -11.433 1.00 13.68 ? 244  ALA B O   1 
ATOM   5203 C  CB  . ALA B  1 244 ? -58.786 15.300  -11.992 1.00 13.29 ? 244  ALA B CB  1 
ATOM   5204 N  N   . LYS B  1 245 ? -59.757 12.567  -10.827 1.00 12.43 ? 245  LYS B N   1 
ATOM   5205 C  CA  . LYS B  1 245 ? -60.254 11.203  -11.136 1.00 12.05 ? 245  LYS B CA  1 
ATOM   5206 C  C   . LYS B  1 245 ? -61.226 10.743  -10.055 1.00 11.74 ? 245  LYS B C   1 
ATOM   5207 O  O   . LYS B  1 245 ? -62.204 10.065  -10.395 1.00 11.26 ? 245  LYS B O   1 
ATOM   5208 C  CB  . LYS B  1 245 ? -59.070 10.255  -11.309 1.00 12.14 ? 245  LYS B CB  1 
ATOM   5209 C  CG  . LYS B  1 245 ? -58.230 10.670  -12.501 1.00 12.75 ? 245  LYS B CG  1 
ATOM   5210 C  CD  . LYS B  1 245 ? -56.953 9.889   -12.649 1.00 13.46 ? 245  LYS B CD  1 
ATOM   5211 C  CE  . LYS B  1 245 ? -55.902 10.595  -13.470 1.00 14.84 ? 245  LYS B CE  1 
ATOM   5212 N  NZ  . LYS B  1 245 ? -56.420 11.005  -14.789 1.00 15.78 ? 245  LYS B NZ  1 
ATOM   5213 N  N   . PHE B  1 246 ? -60.984 11.124  -8.804  1.00 11.21 ? 246  PHE B N   1 
ATOM   5214 C  CA  . PHE B  1 246 ? -61.944 10.818  -7.730  1.00 10.85 ? 246  PHE B CA  1 
ATOM   5215 C  C   . PHE B  1 246 ? -63.255 11.538  -8.039  1.00 11.64 ? 246  PHE B C   1 
ATOM   5216 O  O   . PHE B  1 246 ? -64.311 10.913  -7.960  1.00 10.49 ? 246  PHE B O   1 
ATOM   5217 C  CB  . PHE B  1 246 ? -61.395 11.224  -6.370  1.00 11.08 ? 246  PHE B CB  1 
ATOM   5218 C  CG  . PHE B  1 246 ? -60.171 10.467  -5.931  1.00 11.40 ? 246  PHE B CG  1 
ATOM   5219 C  CD1 . PHE B  1 246 ? -59.976 9.126   -6.242  1.00 11.75 ? 246  PHE B CD1 1 
ATOM   5220 C  CD2 . PHE B  1 246 ? -59.206 11.099  -5.162  1.00 11.08 ? 246  PHE B CD2 1 
ATOM   5221 C  CE1 . PHE B  1 246 ? -58.841 8.450   -5.812  1.00 11.36 ? 246  PHE B CE1 1 
ATOM   5222 C  CE2 . PHE B  1 246 ? -58.087 10.418  -4.705  1.00 11.89 ? 246  PHE B CE2 1 
ATOM   5223 C  CZ  . PHE B  1 246 ? -57.900 9.099   -5.021  1.00 11.55 ? 246  PHE B CZ  1 
ATOM   5224 N  N   . GLU B  1 247 ? -63.212 12.811  -8.402  1.00 10.88 ? 247  GLU B N   1 
ATOM   5225 C  CA  . GLU B  1 247 ? -64.459 13.548  -8.743  1.00 12.69 ? 247  GLU B CA  1 
ATOM   5226 C  C   . GLU B  1 247 ? -65.119 12.950  -9.991  1.00 12.12 ? 247  GLU B C   1 
ATOM   5227 O  O   . GLU B  1 247 ? -66.364 12.754  -9.947  1.00 11.79 ? 247  GLU B O   1 
ATOM   5228 C  CB  . GLU B  1 247 ? -64.148 15.037  -8.894  1.00 12.87 ? 247  GLU B CB  1 
ATOM   5229 C  CG  . GLU B  1 247 ? -63.796 15.686  -7.583  1.00 13.86 ? 247  GLU B CG  1 
ATOM   5230 C  CD  . GLU B  1 247 ? -64.946 15.975  -6.641  1.00 14.83 ? 247  GLU B CD  1 
ATOM   5231 O  OE1 . GLU B  1 247 ? -66.134 15.678  -7.003  1.00 15.04 ? 247  GLU B OE1 1 
ATOM   5232 O  OE2 . GLU B  1 247 ? -64.671 16.520  -5.533  1.00 15.11 ? 247  GLU B OE2 1 
ATOM   5233 N  N   . ARG B  1 248 ? -64.336 12.642  -11.027 1.00 12.45 ? 248  ARG B N   1 
ATOM   5234 C  CA  . ARG B  1 248 ? -64.823 12.064  -12.307 1.00 13.76 ? 248  ARG B CA  1 
ATOM   5235 C  C   . ARG B  1 248 ? -65.627 10.792  -12.022 1.00 12.49 ? 248  ARG B C   1 
ATOM   5236 O  O   . ARG B  1 248 ? -66.676 10.580  -12.662 1.00 14.03 ? 248  ARG B O   1 
ATOM   5237 C  CB  . ARG B  1 248 ? -63.663 11.758  -13.254 1.00 14.67 ? 248  ARG B CB  1 
ATOM   5238 C  CG  . ARG B  1 248 ? -64.078 11.142  -14.590 1.00 15.62 ? 248  ARG B CG  1 
ATOM   5239 C  CD  . ARG B  1 248 ? -62.892 10.971  -15.537 1.00 16.35 ? 248  ARG B CD  1 
ATOM   5240 N  NE  . ARG B  1 248 ? -62.471 12.310  -15.853 1.00 17.05 ? 248  ARG B NE  1 
ATOM   5241 C  CZ  . ARG B  1 248 ? -61.306 12.850  -15.530 1.00 15.32 ? 248  ARG B CZ  1 
ATOM   5242 N  NH1 . ARG B  1 248 ? -61.112 14.140  -15.739 1.00 14.87 ? 248  ARG B NH1 1 
ATOM   5243 N  NH2 . ARG B  1 248 ? -60.344 12.120  -15.009 1.00 15.27 ? 248  ARG B NH2 1 
ATOM   5244 N  N   . ASN B  1 249 ? -65.109 9.959   -11.124 1.00 13.19 ? 249  ASN B N   1 
ATOM   5245 C  CA  . ASN B  1 249 ? -65.676 8.631   -10.786 1.00 13.21 ? 249  ASN B CA  1 
ATOM   5246 C  C   . ASN B  1 249 ? -66.695 8.737   -9.642  1.00 14.18 ? 249  ASN B C   1 
ATOM   5247 O  O   . ASN B  1 249 ? -67.193 7.692   -9.243  1.00 14.75 ? 249  ASN B O   1 
ATOM   5248 C  CB  . ASN B  1 249 ? -64.521 7.662   -10.533 1.00 13.33 ? 249  ASN B CB  1 
ATOM   5249 C  CG  . ASN B  1 249 ? -63.872 7.307   -11.850 1.00 14.79 ? 249  ASN B CG  1 
ATOM   5250 O  OD1 . ASN B  1 249 ? -64.453 6.510   -12.579 1.00 16.59 ? 249  ASN B OD1 1 
ATOM   5251 N  ND2 . ASN B  1 249 ? -62.717 7.879   -12.165 1.00 14.71 ? 249  ASN B ND2 1 
ATOM   5252 N  N   . LYS B  1 250 ? -67.030 9.939   -9.163  1.00 13.98 ? 250  LYS B N   1 
ATOM   5253 C  CA  . LYS B  1 250 ? -67.969 10.165  -8.032  1.00 14.71 ? 250  LYS B CA  1 
ATOM   5254 C  C   . LYS B  1 250 ? -67.629 9.267   -6.835  1.00 13.94 ? 250  LYS B C   1 
ATOM   5255 O  O   . LYS B  1 250 ? -68.520 8.657   -6.225  1.00 14.64 ? 250  LYS B O   1 
ATOM   5256 C  CB  . LYS B  1 250 ? -69.404 9.975   -8.505  1.00 16.02 ? 250  LYS B CB  1 
ATOM   5257 C  CG  . LYS B  1 250 ? -69.733 10.854  -9.708  1.00 18.91 ? 250  LYS B CG  1 
ATOM   5258 C  CD  . LYS B  1 250 ? -71.204 10.838  -10.053 1.00 22.88 ? 250  LYS B CD  1 
ATOM   5259 C  CE  . LYS B  1 250 ? -71.699 9.474   -10.465 1.00 29.37 ? 250  LYS B CE  1 
ATOM   5260 N  NZ  . LYS B  1 250 ? -73.122 9.580   -10.858 1.00 34.96 ? 250  LYS B NZ  1 
ATOM   5261 N  N   . VAL B  1 251 ? -66.358 9.247   -6.478  1.00 12.60 ? 251  VAL B N   1 
ATOM   5262 C  CA  . VAL B  1 251 ? -65.874 8.573   -5.268  1.00 12.47 ? 251  VAL B CA  1 
ATOM   5263 C  C   . VAL B  1 251 ? -66.506 9.251   -4.057  1.00 12.17 ? 251  VAL B C   1 
ATOM   5264 O  O   . VAL B  1 251 ? -66.659 10.487  -4.051  1.00 13.23 ? 251  VAL B O   1 
ATOM   5265 C  CB  . VAL B  1 251 ? -64.334 8.602   -5.256  1.00 14.01 ? 251  VAL B CB  1 
ATOM   5266 C  CG1 . VAL B  1 251 ? -63.762 8.351   -3.881  1.00 15.99 ? 251  VAL B CG1 1 
ATOM   5267 C  CG2 . VAL B  1 251 ? -63.786 7.618   -6.289  1.00 13.07 ? 251  VAL B CG2 1 
ATOM   5268 N  N   . ASP B  1 252 ? -66.917 8.473   -3.073  1.00 11.95 ? 252  ASP B N   1 
ATOM   5269 C  CA  . ASP B  1 252 ? -67.603 9.016   -1.870  1.00 12.33 ? 252  ASP B CA  1 
ATOM   5270 C  C   . ASP B  1 252 ? -66.608 9.807   -1.015  1.00 11.83 ? 252  ASP B C   1 
ATOM   5271 O  O   . ASP B  1 252 ? -66.973 10.885  -0.509  1.00 11.60 ? 252  ASP B O   1 
ATOM   5272 C  CB  . ASP B  1 252 ? -68.254 7.880   -1.076  1.00 12.71 ? 252  ASP B CB  1 
ATOM   5273 C  CG  . ASP B  1 252 ? -69.272 8.404   -0.087  1.00 14.25 ? 252  ASP B CG  1 
ATOM   5274 O  OD1 . ASP B  1 252 ? -70.276 8.953   -0.547  1.00 14.96 ? 252  ASP B OD1 1 
ATOM   5275 O  OD2 . ASP B  1 252 ? -69.042 8.271   1.104   1.00 13.76 ? 252  ASP B OD2 1 
ATOM   5276 N  N   . SER B  1 253 ? -65.399 9.290   -0.837  1.00 12.00 ? 253  SER B N   1 
ATOM   5277 C  CA  . SER B  1 253 ? -64.363 10.002  -0.063  1.00 11.87 ? 253  SER B CA  1 
ATOM   5278 C  C   . SER B  1 253 ? -62.979 9.515   -0.474  1.00 11.71 ? 253  SER B C   1 
ATOM   5279 O  O   . SER B  1 253 ? -62.828 8.378   -0.929  1.00 10.98 ? 253  SER B O   1 
ATOM   5280 C  CB  . SER B  1 253 ? -64.552 9.838   1.424   1.00 11.87 ? 253  SER B CB  1 
ATOM   5281 O  OG  . SER B  1 253 ? -64.392 8.486   1.834   1.00 13.37 ? 253  SER B OG  1 
ATOM   5282 N  N   . ALA B  1 254 ? -61.998 10.365  -0.228  1.00 12.46 ? 254  ALA B N   1 
ATOM   5283 C  CA  . ALA B  1 254 ? -60.580 10.004  -0.382  1.00 10.69 ? 254  ALA B CA  1 
ATOM   5284 C  C   . ALA B  1 254 ? -59.774 10.858  0.582   1.00 11.39 ? 254  ALA B C   1 
ATOM   5285 O  O   . ALA B  1 254 ? -60.134 12.022  0.788   1.00 11.24 ? 254  ALA B O   1 
ATOM   5286 C  CB  . ALA B  1 254 ? -60.138 10.179  -1.816  1.00 11.29 ? 254  ALA B CB  1 
ATOM   5287 N  N   . CYS B  1 255 ? -58.749 10.256  1.182   1.00 11.62 ? 255  CYS B N   1 
ATOM   5288 C  CA  . CYS B  1 255 ? -57.895 10.878  2.204   1.00 10.42 ? 255  CYS B CA  1 
ATOM   5289 C  C   . CYS B  1 255 ? -56.437 10.811  1.743   1.00 10.12 ? 255  CYS B C   1 
ATOM   5290 O  O   . CYS B  1 255 ? -55.986 9.747   1.299   1.00 9.86  ? 255  CYS B O   1 
ATOM   5291 C  CB  . CYS B  1 255 ? -58.005 10.196  3.554   1.00 10.91 ? 255  CYS B CB  1 
ATOM   5292 S  SG  . CYS B  1 255 ? -59.703 10.021  4.140   1.00 12.42 ? 255  CYS B SG  1 
ATOM   5293 N  N   . ILE B  1 256 ? -55.774 11.958  1.839   1.00 10.52 ? 256  ILE B N   1 
ATOM   5294 C  CA  . ILE B  1 256 ? -54.328 12.025  1.592   1.00 10.68 ? 256  ILE B CA  1 
ATOM   5295 C  C   . ILE B  1 256 ? -53.647 11.054  2.565   1.00 10.97 ? 256  ILE B C   1 
ATOM   5296 O  O   . ILE B  1 256 ? -54.040 10.870  3.738   1.00 10.76 ? 256  ILE B O   1 
ATOM   5297 C  CB  . ILE B  1 256 ? -53.842 13.473  1.705   1.00 10.30 ? 256  ILE B CB  1 
ATOM   5298 C  CG1 . ILE B  1 256 ? -54.575 14.402  0.728   1.00 10.67 ? 256  ILE B CG1 1 
ATOM   5299 C  CG2 . ILE B  1 256 ? -52.326 13.523  1.515   1.00 11.06 ? 256  ILE B CG2 1 
ATOM   5300 C  CD1 . ILE B  1 256 ? -54.433 15.870  1.115   1.00 11.48 ? 256  ILE B CD1 1 
ATOM   5301 N  N   . SER B  1 257 ? -52.565 10.465  2.080   1.00 11.76 ? 257  SER B N   1 
ATOM   5302 C  CA  . SER B  1 257 ? -51.645 9.607   2.845   1.00 12.27 ? 257  SER B CA  1 
ATOM   5303 C  C   . SER B  1 257 ? -51.063 10.306  4.088   1.00 11.96 ? 257  SER B C   1 
ATOM   5304 O  O   . SER B  1 257 ? -51.132 11.563  4.219   1.00 13.27 ? 257  SER B O   1 
ATOM   5305 C  CB  . SER B  1 257 ? -50.533 9.169   1.928   1.00 13.00 ? 257  SER B CB  1 
ATOM   5306 O  OG  . SER B  1 257 ? -49.893 10.302  1.340   1.00 13.09 ? 257  SER B OG  1 
ATOM   5307 N  N   . TRP B  1 258 ? -50.434 9.502   4.941   1.00 11.51 ? 258  TRP B N   1 
ATOM   5308 C  CA  . TRP B  1 258 ? -49.631 9.990   6.083   1.00 11.95 ? 258  TRP B CA  1 
ATOM   5309 C  C   . TRP B  1 258 ? -48.292 9.285   6.120   1.00 11.32 ? 258  TRP B C   1 
ATOM   5310 O  O   . TRP B  1 258 ? -48.097 8.337   6.916   1.00 12.68 ? 258  TRP B O   1 
ATOM   5311 C  CB  . TRP B  1 258 ? -50.398 9.819   7.386   1.00 12.48 ? 258  TRP B CB  1 
ATOM   5312 C  CG  . TRP B  1 258 ? -49.692 10.419  8.555   1.00 13.72 ? 258  TRP B CG  1 
ATOM   5313 C  CD1 . TRP B  1 258 ? -49.167 11.674  8.660   1.00 14.63 ? 258  TRP B CD1 1 
ATOM   5314 C  CD2 . TRP B  1 258 ? -49.515 9.797   9.826   1.00 13.99 ? 258  TRP B CD2 1 
ATOM   5315 N  NE1 . TRP B  1 258 ? -48.678 11.868  9.923   1.00 15.02 ? 258  TRP B NE1 1 
ATOM   5316 C  CE2 . TRP B  1 258 ? -48.841 10.724  10.647  1.00 15.03 ? 258  TRP B CE2 1 
ATOM   5317 C  CE3 . TRP B  1 258 ? -49.851 8.547   10.342  1.00 14.68 ? 258  TRP B CE3 1 
ATOM   5318 C  CZ2 . TRP B  1 258 ? -48.513 10.428  11.968  1.00 14.92 ? 258  TRP B CZ2 1 
ATOM   5319 C  CZ3 . TRP B  1 258 ? -49.528 8.260   11.652  1.00 15.17 ? 258  TRP B CZ3 1 
ATOM   5320 C  CH2 . TRP B  1 258 ? -48.833 9.181   12.439  1.00 15.24 ? 258  TRP B CH2 1 
ATOM   5321 N  N   . TRP B  1 259 ? -47.425 9.688   5.216   1.00 12.87 ? 259  TRP B N   1 
ATOM   5322 C  CA  . TRP B  1 259 ? -46.075 9.078   5.090   1.00 12.41 ? 259  TRP B CA  1 
ATOM   5323 C  C   . TRP B  1 259 ? -45.153 9.621   6.172   1.00 12.18 ? 259  TRP B C   1 
ATOM   5324 O  O   . TRP B  1 259 ? -44.178 8.936   6.477   1.00 13.06 ? 259  TRP B O   1 
ATOM   5325 C  CB  . TRP B  1 259 ? -45.483 9.364   3.717   1.00 12.74 ? 259  TRP B CB  1 
ATOM   5326 C  CG  . TRP B  1 259 ? -46.124 8.549   2.641   1.00 13.12 ? 259  TRP B CG  1 
ATOM   5327 C  CD1 . TRP B  1 259 ? -46.848 9.007   1.582   1.00 13.54 ? 259  TRP B CD1 1 
ATOM   5328 C  CD2 . TRP B  1 259 ? -46.094 7.121   2.528   1.00 13.78 ? 259  TRP B CD2 1 
ATOM   5329 N  NE1 . TRP B  1 259 ? -47.264 7.966   0.805   1.00 13.17 ? 259  TRP B NE1 1 
ATOM   5330 C  CE2 . TRP B  1 259 ? -46.852 6.795   1.385   1.00 13.62 ? 259  TRP B CE2 1 
ATOM   5331 C  CE3 . TRP B  1 259 ? -45.523 6.088   3.302   1.00 14.63 ? 259  TRP B CE3 1 
ATOM   5332 C  CZ2 . TRP B  1 259 ? -47.011 5.474   0.982   1.00 13.97 ? 259  TRP B CZ2 1 
ATOM   5333 C  CZ3 . TRP B  1 259 ? -45.711 4.784   2.912   1.00 16.02 ? 259  TRP B CZ3 1 
ATOM   5334 C  CH2 . TRP B  1 259 ? -46.420 4.497   1.746   1.00 14.81 ? 259  TRP B CH2 1 
ATOM   5335 N  N   . TRP B  1 260 ? -45.428 10.802  6.699   1.00 12.37 ? 260  TRP B N   1 
ATOM   5336 C  CA  . TRP B  1 260 ? -44.440 11.496  7.575   1.00 13.40 ? 260  TRP B CA  1 
ATOM   5337 C  C   . TRP B  1 260 ? -44.950 11.426  9.006   1.00 13.49 ? 260  TRP B C   1 
ATOM   5338 O  O   . TRP B  1 260 ? -45.572 12.386  9.518   1.00 14.40 ? 260  TRP B O   1 
ATOM   5339 C  CB  . TRP B  1 260 ? -44.182 12.888  7.011   1.00 13.69 ? 260  TRP B CB  1 
ATOM   5340 C  CG  . TRP B  1 260 ? -43.789 12.800  5.573   1.00 13.72 ? 260  TRP B CG  1 
ATOM   5341 C  CD1 . TRP B  1 260 ? -44.528 13.143  4.489   1.00 13.89 ? 260  TRP B CD1 1 
ATOM   5342 C  CD2 . TRP B  1 260 ? -42.594 12.193  5.064   1.00 13.53 ? 260  TRP B CD2 1 
ATOM   5343 N  NE1 . TRP B  1 260 ? -43.874 12.807  3.329   1.00 14.74 ? 260  TRP B NE1 1 
ATOM   5344 C  CE2 . TRP B  1 260 ? -42.672 12.235  3.653   1.00 14.59 ? 260  TRP B CE2 1 
ATOM   5345 C  CE3 . TRP B  1 260 ? -41.471 11.625  5.661   1.00 15.29 ? 260  TRP B CE3 1 
ATOM   5346 C  CZ2 . TRP B  1 260 ? -41.637 11.761  2.843   1.00 14.57 ? 260  TRP B CZ2 1 
ATOM   5347 C  CZ3 . TRP B  1 260 ? -40.447 11.148  4.868   1.00 13.94 ? 260  TRP B CZ3 1 
ATOM   5348 C  CH2 . TRP B  1 260 ? -40.543 11.213  3.471   1.00 14.73 ? 260  TRP B CH2 1 
ATOM   5349 N  N   . THR B  1 261 ? -44.704 10.290  9.634   1.00 14.91 ? 261  THR B N   1 
ATOM   5350 C  CA  . THR B  1 261 ? -45.279 9.968   10.944  1.00 16.20 ? 261  THR B CA  1 
ATOM   5351 C  C   . THR B  1 261 ? -44.702 10.831  12.066  1.00 15.52 ? 261  THR B C   1 
ATOM   5352 O  O   . THR B  1 261 ? -45.273 10.763  13.131  1.00 15.64 ? 261  THR B O   1 
ATOM   5353 C  CB  . THR B  1 261 ? -45.246 8.470   11.212  1.00 17.64 ? 261  THR B CB  1 
ATOM   5354 O  OG1 . THR B  1 261 ? -43.874 8.073   11.211  1.00 20.29 ? 261  THR B OG1 1 
ATOM   5355 C  CG2 . THR B  1 261 ? -46.053 7.713   10.186  1.00 18.58 ? 261  THR B CG2 1 
ATOM   5356 N  N   . ASN B  1 262 ? -43.638 11.610  11.866  1.00 16.02 ? 262  ASN B N   1 
ATOM   5357 C  CA  . ASN B  1 262 ? -43.181 12.580  12.894  1.00 16.77 ? 262  ASN B CA  1 
ATOM   5358 C  C   . ASN B  1 262 ? -43.876 13.925  12.681  1.00 17.12 ? 262  ASN B C   1 
ATOM   5359 O  O   . ASN B  1 262 ? -43.636 14.816  13.489  1.00 18.01 ? 262  ASN B O   1 
ATOM   5360 C  CB  . ASN B  1 262 ? -41.652 12.711  12.913  1.00 17.76 ? 262  ASN B CB  1 
ATOM   5361 C  CG  . ASN B  1 262 ? -40.994 11.397  13.270  1.00 19.04 ? 262  ASN B CG  1 
ATOM   5362 O  OD1 . ASN B  1 262 ? -41.397 10.752  14.235  1.00 19.55 ? 262  ASN B OD1 1 
ATOM   5363 N  ND2 . ASN B  1 262 ? -39.980 10.981  12.510  1.00 19.69 ? 262  ASN B ND2 1 
ATOM   5364 N  N   . ALA B  1 263 ? -44.762 14.041  11.689  1.00 15.26 ? 263  ALA B N   1 
ATOM   5365 C  CA  . ALA B  1 263 ? -45.493 15.292  11.389  1.00 13.15 ? 263  ALA B CA  1 
ATOM   5366 C  C   . ALA B  1 263 ? -46.998 15.015  11.304  1.00 13.21 ? 263  ALA B C   1 
ATOM   5367 O  O   . ALA B  1 263 ? -47.628 15.348  10.302  1.00 13.37 ? 263  ALA B O   1 
ATOM   5368 C  CB  . ALA B  1 263 ? -44.990 15.914  10.116  1.00 13.16 ? 263  ALA B CB  1 
ATOM   5369 N  N   . PRO B  1 264 ? -47.614 14.499  12.371  1.00 14.63 ? 264  PRO B N   1 
ATOM   5370 C  CA  . PRO B  1 264 ? -49.075 14.367  12.399  1.00 15.50 ? 264  PRO B CA  1 
ATOM   5371 C  C   . PRO B  1 264 ? -49.711 15.760  12.371  1.00 16.03 ? 264  PRO B C   1 
ATOM   5372 O  O   . PRO B  1 264 ? -49.072 16.772  12.793  1.00 17.31 ? 264  PRO B O   1 
ATOM   5373 C  CB  . PRO B  1 264 ? -49.329 13.654  13.726  1.00 16.39 ? 264  PRO B CB  1 
ATOM   5374 C  CG  . PRO B  1 264 ? -48.212 14.134  14.606  1.00 16.95 ? 264  PRO B CG  1 
ATOM   5375 C  CD  . PRO B  1 264 ? -47.024 14.163  13.673  1.00 16.19 ? 264  PRO B CD  1 
ATOM   5376 N  N   . GLY B  1 265 ? -50.944 15.831  11.866  1.00 15.18 ? 265  GLY B N   1 
ATOM   5377 C  CA  . GLY B  1 265 ? -51.765 17.040  11.984  1.00 14.19 ? 265  GLY B CA  1 
ATOM   5378 C  C   . GLY B  1 265 ? -51.373 18.107  11.000  1.00 14.82 ? 265  GLY B C   1 
ATOM   5379 O  O   . GLY B  1 265 ? -51.628 19.263  11.305  1.00 14.49 ? 265  GLY B O   1 
ATOM   5380 N  N   . ARG B  1 266 ? -50.855 17.743  9.829   1.00 14.75 ? 266  ARG B N   1 
ATOM   5381 C  CA  . ARG B  1 266 ? -50.532 18.713  8.757   1.00 14.95 ? 266  ARG B CA  1 
ATOM   5382 C  C   . ARG B  1 266 ? -51.440 18.565  7.540   1.00 13.83 ? 266  ARG B C   1 
ATOM   5383 O  O   . ARG B  1 266 ? -51.098 19.070  6.460   1.00 13.01 ? 266  ARG B O   1 
ATOM   5384 C  CB  . ARG B  1 266 ? -49.051 18.570  8.433   1.00 15.42 ? 266  ARG B CB  1 
ATOM   5385 C  CG  . ARG B  1 266 ? -48.185 19.094  9.574   1.00 17.43 ? 266  ARG B CG  1 
ATOM   5386 C  CD  . ARG B  1 266 ? -46.814 19.404  9.048   1.00 18.12 ? 266  ARG B CD  1 
ATOM   5387 N  NE  . ARG B  1 266 ? -45.885 19.567  10.144  1.00 17.96 ? 266  ARG B NE  1 
ATOM   5388 C  CZ  . ARG B  1 266 ? -44.573 19.483  9.992   1.00 19.11 ? 266  ARG B CZ  1 
ATOM   5389 N  NH1 . ARG B  1 266 ? -44.048 19.256  8.794   1.00 19.61 ? 266  ARG B NH1 1 
ATOM   5390 N  NH2 . ARG B  1 266 ? -43.798 19.568  11.057  1.00 20.84 ? 266  ARG B NH2 1 
ATOM   5391 N  N   . LEU B  1 267 ? -52.637 18.006  7.733   1.00 14.67 ? 267  LEU B N   1 
ATOM   5392 C  CA  . LEU B  1 267 ? -53.725 17.989  6.726   1.00 13.88 ? 267  LEU B CA  1 
ATOM   5393 C  C   . LEU B  1 267 ? -53.298 17.266  5.452   1.00 13.67 ? 267  LEU B C   1 
ATOM   5394 O  O   . LEU B  1 267 ? -53.889 17.512  4.431   1.00 14.03 ? 267  LEU B O   1 
ATOM   5395 C  CB  . LEU B  1 267 ? -54.190 19.416  6.455   1.00 13.59 ? 267  LEU B CB  1 
ATOM   5396 C  CG  . LEU B  1 267 ? -54.861 20.046  7.667   1.00 13.92 ? 267  LEU B CG  1 
ATOM   5397 C  CD1 . LEU B  1 267 ? -55.034 21.539  7.470   1.00 13.88 ? 267  LEU B CD1 1 
ATOM   5398 C  CD2 . LEU B  1 267 ? -56.210 19.369  7.896   1.00 13.54 ? 267  LEU B CD2 1 
ATOM   5399 N  N   . GLY B  1 268 ? -52.358 16.341  5.562   1.00 12.77 ? 268  GLY B N   1 
ATOM   5400 C  CA  . GLY B  1 268 ? -51.849 15.603  4.393   1.00 13.23 ? 268  GLY B CA  1 
ATOM   5401 C  C   . GLY B  1 268 ? -50.721 16.366  3.707   1.00 12.26 ? 268  GLY B C   1 
ATOM   5402 O  O   . GLY B  1 268 ? -50.718 16.466  2.464   1.00 11.74 ? 268  GLY B O   1 
ATOM   5403 N  N   . SER B  1 269 ? -49.795 16.895  4.491   1.00 12.32 ? 269  SER B N   1 
ATOM   5404 C  CA  . SER B  1 269 ? -48.675 17.729  3.993   1.00 12.78 ? 269  SER B CA  1 
ATOM   5405 C  C   . SER B  1 269 ? -49.227 18.941  3.223   1.00 13.92 ? 269  SER B C   1 
ATOM   5406 O  O   . SER B  1 269 ? -48.500 19.523  2.394   1.00 12.87 ? 269  SER B O   1 
ATOM   5407 C  CB  . SER B  1 269 ? -47.711 16.923  3.162   1.00 13.54 ? 269  SER B CB  1 
ATOM   5408 O  OG  . SER B  1 269 ? -47.085 15.925  3.963   1.00 13.58 ? 269  SER B OG  1 
ATOM   5409 N  N   . LEU B  1 270 ? -50.455 19.375  3.526   1.00 12.59 ? 270  LEU B N   1 
ATOM   5410 C  CA  . LEU B  1 270 ? -50.941 20.691  3.036   1.00 13.40 ? 270  LEU B CA  1 
ATOM   5411 C  C   . LEU B  1 270 ? -50.296 21.828  3.862   1.00 13.30 ? 270  LEU B C   1 
ATOM   5412 O  O   . LEU B  1 270 ? -50.105 22.914  3.317   1.00 14.32 ? 270  LEU B O   1 
ATOM   5413 C  CB  . LEU B  1 270 ? -52.464 20.740  3.090   1.00 13.34 ? 270  LEU B CB  1 
ATOM   5414 C  CG  . LEU B  1 270 ? -53.201 19.690  2.266   1.00 13.81 ? 270  LEU B CG  1 
ATOM   5415 C  CD1 . LEU B  1 270 ? -54.700 19.996  2.286   1.00 13.95 ? 270  LEU B CD1 1 
ATOM   5416 C  CD2 . LEU B  1 270 ? -52.706 19.584  0.845   1.00 14.90 ? 270  LEU B CD2 1 
ATOM   5417 N  N   A MET B  1 271 ? -49.983 21.566  5.119   0.75 14.82 ? 271  MET B N   1 
ATOM   5418 N  N   B MET B  1 271 ? -49.965 21.572  5.126   0.25 14.36 ? 271  MET B N   1 
ATOM   5419 C  CA  A MET B  1 271 ? -49.246 22.497  6.013   0.75 14.89 ? 271  MET B CA  1 
ATOM   5420 C  CA  B MET B  1 271 ? -49.244 22.533  6.003   0.25 14.66 ? 271  MET B CA  1 
ATOM   5421 C  C   A MET B  1 271 ? -47.755 22.192  5.842   0.75 15.59 ? 271  MET B C   1 
ATOM   5422 C  C   B MET B  1 271 ? -47.750 22.209  5.954   0.25 15.28 ? 271  MET B C   1 
ATOM   5423 O  O   A MET B  1 271 ? -47.415 21.010  5.757   0.75 14.57 ? 271  MET B O   1 
ATOM   5424 O  O   B MET B  1 271 ? -47.403 21.030  6.153   0.25 15.26 ? 271  MET B O   1 
ATOM   5425 C  CB  A MET B  1 271 ? -49.653 22.297  7.474   0.75 15.34 ? 271  MET B CB  1 
ATOM   5426 C  CB  B MET B  1 271 ? -49.733 22.444  7.449   0.25 14.72 ? 271  MET B CB  1 
ATOM   5427 C  CG  A MET B  1 271 ? -51.132 22.528  7.727   0.75 15.90 ? 271  MET B CG  1 
ATOM   5428 C  CG  B MET B  1 271 ? -51.231 22.350  7.550   0.25 14.92 ? 271  MET B CG  1 
ATOM   5429 S  SD  A MET B  1 271 ? -51.547 24.255  7.620   0.75 16.88 ? 271  MET B SD  1 
ATOM   5430 S  SD  B MET B  1 271 ? -51.858 23.039  9.079   0.25 14.99 ? 271  MET B SD  1 
ATOM   5431 C  CE  A MET B  1 271 ? -50.906 24.743  9.224   0.75 16.93 ? 271  MET B CE  1 
ATOM   5432 C  CE  B MET B  1 271 ? -50.992 22.093  10.331  0.25 14.70 ? 271  MET B CE  1 
ATOM   5433 N  N   . ALA B  1 272 ? -46.917 23.224  5.693   1.00 15.69 ? 272  ALA B N   1 
ATOM   5434 C  CA  . ALA B  1 272 ? -45.448 23.097  5.541   1.00 16.18 ? 272  ALA B CA  1 
ATOM   5435 C  C   . ALA B  1 272 ? -44.792 22.846  6.901   1.00 18.27 ? 272  ALA B C   1 
ATOM   5436 O  O   . ALA B  1 272 ? -43.701 22.174  6.952   1.00 19.18 ? 272  ALA B O   1 
ATOM   5437 C  CB  . ALA B  1 272 ? -44.946 24.355  4.867   1.00 16.70 ? 272  ALA B CB  1 
ATOM   5438 N  N   . SER B  1 273 ? -45.424 23.304  7.978   1.00 17.02 ? 273  SER B N   1 
ATOM   5439 C  CA  . SER B  1 273 ? -45.014 23.022  9.381   1.00 17.57 ? 273  SER B CA  1 
ATOM   5440 C  C   . SER B  1 273 ? -46.255 22.886  10.247  1.00 17.89 ? 273  SER B C   1 
ATOM   5441 O  O   . SER B  1 273 ? -47.343 23.020  9.703   1.00 18.46 ? 273  SER B O   1 
ATOM   5442 C  CB  . SER B  1 273 ? -44.148 24.139  9.909   1.00 18.77 ? 273  SER B CB  1 
ATOM   5443 O  OG  . SER B  1 273 ? -44.933 25.293  10.116  1.00 16.35 ? 273  SER B OG  1 
ATOM   5444 N  N   . ASP B  1 274 ? -46.101 22.747  11.568  1.00 19.65 ? 274  ASP B N   1 
ATOM   5445 C  CA  . ASP B  1 274 ? -47.268 22.655  12.467  1.00 20.51 ? 274  ASP B CA  1 
ATOM   5446 C  C   . ASP B  1 274 ? -48.101 23.926  12.349  1.00 23.67 ? 274  ASP B C   1 
ATOM   5447 O  O   . ASP B  1 274 ? -49.350 23.787  12.516  1.00 23.44 ? 274  ASP B O   1 
ATOM   5448 C  CB  . ASP B  1 274 ? -46.872 22.313  13.904  1.00 21.24 ? 274  ASP B CB  1 
ATOM   5449 C  CG  . ASP B  1 274 ? -46.309 20.919  14.005  1.00 21.40 ? 274  ASP B CG  1 
ATOM   5450 O  OD1 . ASP B  1 274 ? -46.279 20.238  12.961  1.00 23.38 ? 274  ASP B OD1 1 
ATOM   5451 O  OD2 . ASP B  1 274 ? -45.907 20.515  15.108  1.00 23.58 ? 274  ASP B OD2 1 
ATOM   5452 N  N   . THR B  1 275 ? -47.490 25.057  11.968  1.00 22.16 ? 275  THR B N   1 
ATOM   5453 C  CA  . THR B  1 275 ? -48.096 26.405  12.090  1.00 23.17 ? 275  THR B CA  1 
ATOM   5454 C  C   . THR B  1 275 ? -48.151 27.161  10.758  1.00 21.41 ? 275  THR B C   1 
ATOM   5455 O  O   . THR B  1 275 ? -48.614 28.295  10.782  1.00 22.95 ? 275  THR B O   1 
ATOM   5456 C  CB  . THR B  1 275 ? -47.313 27.198  13.148  1.00 25.10 ? 275  THR B CB  1 
ATOM   5457 O  OG1 . THR B  1 275 ? -45.987 27.403  12.670  1.00 24.68 ? 275  THR B OG1 1 
ATOM   5458 C  CG2 . THR B  1 275 ? -47.296 26.476  14.478  1.00 27.64 ? 275  THR B CG2 1 
ATOM   5459 N  N   . GLN B  1 276 ? -47.660 26.624  9.637   1.00 20.17 ? 276  GLN B N   1 
ATOM   5460 C  CA  . GLN B  1 276 ? -47.551 27.402  8.383   1.00 18.69 ? 276  GLN B CA  1 
ATOM   5461 C  C   . GLN B  1 276 ? -48.170 26.623  7.223   1.00 17.70 ? 276  GLN B C   1 
ATOM   5462 O  O   . GLN B  1 276 ? -47.883 25.431  7.101   1.00 16.37 ? 276  GLN B O   1 
ATOM   5463 C  CB  . GLN B  1 276 ? -46.083 27.709  8.103   1.00 20.95 ? 276  GLN B CB  1 
ATOM   5464 C  CG  . GLN B  1 276 ? -45.457 28.541  9.210   1.00 22.19 ? 276  GLN B CG  1 
ATOM   5465 C  CD  . GLN B  1 276 ? -43.957 28.510  9.088   1.00 25.92 ? 276  GLN B CD  1 
ATOM   5466 O  OE1 . GLN B  1 276 ? -43.322 27.519  9.455   1.00 27.71 ? 276  GLN B OE1 1 
ATOM   5467 N  NE2 . GLN B  1 276 ? -43.402 29.588  8.546   1.00 27.01 ? 276  GLN B NE2 1 
ATOM   5468 N  N   . LYS B  1 277 ? -48.893 27.321  6.360   1.00 17.44 ? 277  LYS B N   1 
ATOM   5469 C  CA  . LYS B  1 277 ? -49.461 26.753  5.122   1.00 17.44 ? 277  LYS B CA  1 
ATOM   5470 C  C   . LYS B  1 277 ? -48.323 26.406  4.171   1.00 17.96 ? 277  LYS B C   1 
ATOM   5471 O  O   . LYS B  1 277 ? -47.352 27.181  4.081   1.00 16.14 ? 277  LYS B O   1 
ATOM   5472 C  CB  . LYS B  1 277 ? -50.445 27.712  4.468   1.00 17.61 ? 277  LYS B CB  1 
ATOM   5473 C  CG  . LYS B  1 277 ? -51.667 28.033  5.300   1.00 17.99 ? 277  LYS B CG  1 
ATOM   5474 C  CD  . LYS B  1 277 ? -52.412 29.232  4.762   1.00 17.65 ? 277  LYS B CD  1 
ATOM   5475 C  CE  . LYS B  1 277 ? -53.621 29.590  5.592   1.00 18.62 ? 277  LYS B CE  1 
ATOM   5476 N  NZ  . LYS B  1 277 ? -54.267 30.782  4.991   1.00 20.46 ? 277  LYS B NZ  1 
ATOM   5477 N  N   . GLY B  1 278 ? -48.449 25.264  3.498   1.00 15.55 ? 278  GLY B N   1 
ATOM   5478 C  CA  . GLY B  1 278 ? -47.648 24.905  2.320   1.00 15.30 ? 278  GLY B CA  1 
ATOM   5479 C  C   . GLY B  1 278 ? -48.410 25.200  1.050   1.00 13.86 ? 278  GLY B C   1 
ATOM   5480 O  O   . GLY B  1 278 ? -49.571 25.611  1.158   1.00 15.59 ? 278  GLY B O   1 
ATOM   5481 N  N   . ALA B  1 279 ? -47.840 24.907  -0.119  1.00 13.16 ? 279  ALA B N   1 
ATOM   5482 C  CA  . ALA B  1 279 ? -48.458 25.169  -1.437  1.00 13.22 ? 279  ALA B CA  1 
ATOM   5483 C  C   . ALA B  1 279 ? -49.791 24.412  -1.525  1.00 13.53 ? 279  ALA B C   1 
ATOM   5484 O  O   . ALA B  1 279 ? -50.767 24.953  -2.009  1.00 14.82 ? 279  ALA B O   1 
ATOM   5485 C  CB  . ALA B  1 279 ? -47.550 24.746  -2.548  1.00 12.85 ? 279  ALA B CB  1 
ATOM   5486 N  N   . GLY B  1 280 ? -49.804 23.154  -1.093  1.00 13.16 ? 280  GLY B N   1 
ATOM   5487 C  CA  . GLY B  1 280 ? -51.023 22.319  -1.155  1.00 13.37 ? 280  GLY B CA  1 
ATOM   5488 C  C   . GLY B  1 280 ? -52.196 22.958  -0.436  1.00 13.41 ? 280  GLY B C   1 
ATOM   5489 O  O   . GLY B  1 280 ? -53.348 22.818  -0.937  1.00 13.28 ? 280  GLY B O   1 
ATOM   5490 N  N   . TRP B  1 281 ? -51.954 23.672  0.674   1.00 14.37 ? 281  TRP B N   1 
ATOM   5491 C  CA  . TRP B  1 281 ? -53.065 24.297  1.425   1.00 14.34 ? 281  TRP B CA  1 
ATOM   5492 C  C   . TRP B  1 281 ? -53.870 25.220  0.492   1.00 14.80 ? 281  TRP B C   1 
ATOM   5493 O  O   . TRP B  1 281 ? -55.132 25.106  0.429   1.00 12.09 ? 281  TRP B O   1 
ATOM   5494 C  CB  . TRP B  1 281 ? -52.584 25.008  2.696   1.00 14.03 ? 281  TRP B CB  1 
ATOM   5495 C  CG  . TRP B  1 281 ? -53.724 25.407  3.568   1.00 14.26 ? 281  TRP B CG  1 
ATOM   5496 C  CD1 . TRP B  1 281 ? -54.211 24.715  4.642   1.00 13.97 ? 281  TRP B CD1 1 
ATOM   5497 C  CD2 . TRP B  1 281 ? -54.573 26.563  3.411   1.00 14.72 ? 281  TRP B CD2 1 
ATOM   5498 N  NE1 . TRP B  1 281 ? -55.295 25.360  5.162   1.00 14.37 ? 281  TRP B NE1 1 
ATOM   5499 C  CE2 . TRP B  1 281 ? -55.557 26.478  4.417   1.00 14.94 ? 281  TRP B CE2 1 
ATOM   5500 C  CE3 . TRP B  1 281 ? -54.584 27.657  2.541   1.00 14.78 ? 281  TRP B CE3 1 
ATOM   5501 C  CZ2 . TRP B  1 281 ? -56.549 27.450  4.577   1.00 15.48 ? 281  TRP B CZ2 1 
ATOM   5502 C  CZ3 . TRP B  1 281 ? -55.575 28.602  2.691   1.00 17.25 ? 281  TRP B CZ3 1 
ATOM   5503 C  CH2 . TRP B  1 281 ? -56.531 28.503  3.698   1.00 15.01 ? 281  TRP B CH2 1 
ATOM   5504 N  N   . TRP B  1 282 ? -53.197 26.079  -0.262  1.00 15.63 ? 282  TRP B N   1 
ATOM   5505 C  CA  . TRP B  1 282 ? -53.831 27.087  -1.157  1.00 15.38 ? 282  TRP B CA  1 
ATOM   5506 C  C   . TRP B  1 282 ? -54.605 26.387  -2.268  1.00 14.12 ? 282  TRP B C   1 
ATOM   5507 O  O   . TRP B  1 282 ? -55.706 26.808  -2.613  1.00 15.14 ? 282  TRP B O   1 
ATOM   5508 C  CB  . TRP B  1 282 ? -52.753 28.017  -1.724  1.00 16.71 ? 282  TRP B CB  1 
ATOM   5509 C  CG  . TRP B  1 282 ? -52.074 28.797  -0.643  1.00 16.12 ? 282  TRP B CG  1 
ATOM   5510 C  CD1 . TRP B  1 282 ? -50.901 28.502  0.003   1.00 15.56 ? 282  TRP B CD1 1 
ATOM   5511 C  CD2 . TRP B  1 282 ? -52.607 29.962  0.024   1.00 17.91 ? 282  TRP B CD2 1 
ATOM   5512 N  NE1 . TRP B  1 282 ? -50.667 29.424  0.992   1.00 17.03 ? 282  TRP B NE1 1 
ATOM   5513 C  CE2 . TRP B  1 282 ? -51.694 30.317  1.037   1.00 16.99 ? 282  TRP B CE2 1 
ATOM   5514 C  CE3 . TRP B  1 282 ? -53.786 30.705  -0.110  1.00 19.86 ? 282  TRP B CE3 1 
ATOM   5515 C  CZ2 . TRP B  1 282 ? -51.896 31.420  1.864   1.00 19.45 ? 282  TRP B CZ2 1 
ATOM   5516 C  CZ3 . TRP B  1 282 ? -53.978 31.809  0.698   1.00 20.35 ? 282  TRP B CZ3 1 
ATOM   5517 C  CH2 . TRP B  1 282 ? -53.049 32.146  1.682   1.00 19.91 ? 282  TRP B CH2 1 
ATOM   5518 N  N   . PHE B  1 283 ? -54.076 25.286  -2.778  1.00 13.44 ? 283  PHE B N   1 
ATOM   5519 C  CA  . PHE B  1 283 ? -54.752 24.533  -3.858  1.00 13.39 ? 283  PHE B CA  1 
ATOM   5520 C  C   . PHE B  1 283 ? -56.018 23.898  -3.285  1.00 12.86 ? 283  PHE B C   1 
ATOM   5521 O  O   . PHE B  1 283 ? -57.124 24.029  -3.913  1.00 13.74 ? 283  PHE B O   1 
ATOM   5522 C  CB  . PHE B  1 283 ? -53.837 23.498  -4.510  1.00 13.16 ? 283  PHE B CB  1 
ATOM   5523 C  CG  . PHE B  1 283 ? -54.411 22.869  -5.755  1.00 13.15 ? 283  PHE B CG  1 
ATOM   5524 C  CD1 . PHE B  1 283 ? -54.474 23.584  -6.931  1.00 13.46 ? 283  PHE B CD1 1 
ATOM   5525 C  CD2 . PHE B  1 283 ? -54.840 21.538  -5.762  1.00 13.01 ? 283  PHE B CD2 1 
ATOM   5526 C  CE1 . PHE B  1 283 ? -55.011 23.019  -8.078  1.00 14.22 ? 283  PHE B CE1 1 
ATOM   5527 C  CE2 . PHE B  1 283 ? -55.317 20.954  -6.922  1.00 13.09 ? 283  PHE B CE2 1 
ATOM   5528 C  CZ  . PHE B  1 283 ? -55.433 21.699  -8.073  1.00 14.23 ? 283  PHE B CZ  1 
ATOM   5529 N  N   . TYR B  1 284 ? -55.925 23.271  -2.104  1.00 12.56 ? 284  TYR B N   1 
ATOM   5530 C  CA  . TYR B  1 284 ? -57.125 22.625  -1.537  1.00 13.16 ? 284  TYR B CA  1 
ATOM   5531 C  C   . TYR B  1 284 ? -58.107 23.687  -1.027  1.00 13.42 ? 284  TYR B C   1 
ATOM   5532 O  O   . TYR B  1 284 ? -59.304 23.370  -0.868  1.00 13.11 ? 284  TYR B O   1 
ATOM   5533 C  CB  . TYR B  1 284 ? -56.751 21.570  -0.501  1.00 11.94 ? 284  TYR B CB  1 
ATOM   5534 C  CG  . TYR B  1 284 ? -56.330 20.235  -1.058  1.00 12.14 ? 284  TYR B CG  1 
ATOM   5535 C  CD1 . TYR B  1 284 ? -55.085 20.044  -1.644  1.00 11.81 ? 284  TYR B CD1 1 
ATOM   5536 C  CD2 . TYR B  1 284 ? -57.128 19.105  -0.888  1.00 12.80 ? 284  TYR B CD2 1 
ATOM   5537 C  CE1 . TYR B  1 284 ? -54.682 18.791  -2.110  1.00 12.29 ? 284  TYR B CE1 1 
ATOM   5538 C  CE2 . TYR B  1 284 ? -56.728 17.854  -1.315  1.00 11.89 ? 284  TYR B CE2 1 
ATOM   5539 C  CZ  . TYR B  1 284 ? -55.497 17.691  -1.937  1.00 12.47 ? 284  TYR B CZ  1 
ATOM   5540 O  OH  . TYR B  1 284 ? -55.091 16.437  -2.335  1.00 12.47 ? 284  TYR B OH  1 
ATOM   5541 N  N   . LYS B  1 285 ? -57.636 24.908  -0.766  1.00 14.20 ? 285  LYS B N   1 
ATOM   5542 C  CA  . LYS B  1 285 ? -58.523 26.042  -0.390  1.00 14.34 ? 285  LYS B CA  1 
ATOM   5543 C  C   . LYS B  1 285 ? -59.378 26.431  -1.591  1.00 14.19 ? 285  LYS B C   1 
ATOM   5544 O  O   . LYS B  1 285 ? -60.611 26.602  -1.434  1.00 14.11 ? 285  LYS B O   1 
ATOM   5545 C  CB  . LYS B  1 285 ? -57.685 27.227  0.108   1.00 16.18 ? 285  LYS B CB  1 
ATOM   5546 C  CG  . LYS B  1 285 ? -58.484 28.495  0.372   1.00 17.02 ? 285  LYS B CG  1 
ATOM   5547 C  CD  . LYS B  1 285 ? -59.581 28.319  1.407   1.00 18.34 ? 285  LYS B CD  1 
ATOM   5548 C  CE  . LYS B  1 285 ? -60.217 29.633  1.836   1.00 19.94 ? 285  LYS B CE  1 
ATOM   5549 N  NZ  . LYS B  1 285 ? -60.606 30.432  0.665   1.00 20.16 ? 285  LYS B NZ  1 
ATOM   5550 N  N   . TRP B  1 286 ? -58.791 26.525  -2.774  1.00 13.93 ? 286  TRP B N   1 
ATOM   5551 C  CA  . TRP B  1 286 ? -59.578 26.734  -4.002  1.00 13.81 ? 286  TRP B CA  1 
ATOM   5552 C  C   . TRP B  1 286 ? -60.585 25.600  -4.134  1.00 13.74 ? 286  TRP B C   1 
ATOM   5553 O  O   . TRP B  1 286 ? -61.737 25.865  -4.521  1.00 13.43 ? 286  TRP B O   1 
ATOM   5554 C  CB  . TRP B  1 286 ? -58.698 26.817  -5.240  1.00 14.65 ? 286  TRP B CB  1 
ATOM   5555 C  CG  . TRP B  1 286 ? -57.980 28.118  -5.438  1.00 15.37 ? 286  TRP B CG  1 
ATOM   5556 C  CD1 . TRP B  1 286 ? -58.390 29.373  -5.064  1.00 17.77 ? 286  TRP B CD1 1 
ATOM   5557 C  CD2 . TRP B  1 286 ? -56.729 28.295  -6.128  1.00 16.66 ? 286  TRP B CD2 1 
ATOM   5558 N  NE1 . TRP B  1 286 ? -57.457 30.308  -5.459  1.00 16.84 ? 286  TRP B NE1 1 
ATOM   5559 C  CE2 . TRP B  1 286 ? -56.447 29.687  -6.138  1.00 17.55 ? 286  TRP B CE2 1 
ATOM   5560 C  CE3 . TRP B  1 286 ? -55.818 27.430  -6.743  1.00 16.91 ? 286  TRP B CE3 1 
ATOM   5561 C  CZ2 . TRP B  1 286 ? -55.287 30.200  -6.714  1.00 18.79 ? 286  TRP B CZ2 1 
ATOM   5562 C  CZ3 . TRP B  1 286 ? -54.673 27.941  -7.315  1.00 17.91 ? 286  TRP B CZ3 1 
ATOM   5563 C  CH2 . TRP B  1 286 ? -54.426 29.316  -7.323  1.00 17.59 ? 286  TRP B CH2 1 
ATOM   5564 N  N   . TYR B  1 287 ? -60.165 24.366  -3.862  1.00 12.51 ? 287  TYR B N   1 
ATOM   5565 C  CA  . TYR B  1 287 ? -61.089 23.201  -3.918  1.00 13.04 ? 287  TYR B CA  1 
ATOM   5566 C  C   . TYR B  1 287 ? -62.256 23.429  -2.947  1.00 12.90 ? 287  TYR B C   1 
ATOM   5567 O  O   . TYR B  1 287 ? -63.432 23.247  -3.350  1.00 12.81 ? 287  TYR B O   1 
ATOM   5568 C  CB  . TYR B  1 287 ? -60.308 21.925  -3.581  1.00 12.15 ? 287  TYR B CB  1 
ATOM   5569 C  CG  . TYR B  1 287 ? -60.996 20.584  -3.711  1.00 12.03 ? 287  TYR B CG  1 
ATOM   5570 C  CD1 . TYR B  1 287 ? -62.121 20.362  -4.489  1.00 11.76 ? 287  TYR B CD1 1 
ATOM   5571 C  CD2 . TYR B  1 287 ? -60.405 19.488  -3.113  1.00 12.98 ? 287  TYR B CD2 1 
ATOM   5572 C  CE1 . TYR B  1 287 ? -62.669 19.088  -4.608  1.00 12.21 ? 287  TYR B CE1 1 
ATOM   5573 C  CE2 . TYR B  1 287 ? -60.919 18.204  -3.238  1.00 12.16 ? 287  TYR B CE2 1 
ATOM   5574 C  CZ  . TYR B  1 287 ? -62.049 18.002  -4.001  1.00 12.33 ? 287  TYR B CZ  1 
ATOM   5575 O  OH  . TYR B  1 287 ? -62.522 16.715  -4.089  1.00 11.72 ? 287  TYR B OH  1 
ATOM   5576 N  N   . GLY B  1 288 ? -61.952 23.824  -1.706  1.00 13.46 ? 288  GLY B N   1 
ATOM   5577 C  CA  . GLY B  1 288 ? -62.923 24.100  -0.632  1.00 14.56 ? 288  GLY B CA  1 
ATOM   5578 C  C   . GLY B  1 288 ? -63.897 25.210  -0.990  1.00 14.18 ? 288  GLY B C   1 
ATOM   5579 O  O   . GLY B  1 288 ? -65.093 25.138  -0.606  1.00 14.69 ? 288  GLY B O   1 
ATOM   5580 N  N   . ASP B  1 289 ? -63.443 26.161  -1.802  1.00 14.29 ? 289  ASP B N   1 
ATOM   5581 C  CA  . ASP B  1 289 ? -64.276 27.304  -2.263  1.00 14.97 ? 289  ASP B CA  1 
ATOM   5582 C  C   . ASP B  1 289 ? -65.321 26.834  -3.273  1.00 15.37 ? 289  ASP B C   1 
ATOM   5583 O  O   . ASP B  1 289 ? -66.307 27.533  -3.450  1.00 15.19 ? 289  ASP B O   1 
ATOM   5584 C  CB  . ASP B  1 289 ? -63.420 28.409  -2.898  1.00 16.98 ? 289  ASP B CB  1 
ATOM   5585 C  CG  . ASP B  1 289 ? -62.506 29.141  -1.930  1.00 19.62 ? 289  ASP B CG  1 
ATOM   5586 O  OD1 . ASP B  1 289 ? -62.775 29.110  -0.725  1.00 18.47 ? 289  ASP B OD1 1 
ATOM   5587 O  OD2 . ASP B  1 289 ? -61.538 29.795  -2.417  1.00 20.04 ? 289  ASP B OD2 1 
ATOM   5588 N  N   . MET B  1 290 ? -65.100 25.712  -3.947  1.00 14.81 ? 290  MET B N   1 
ATOM   5589 C  CA  . MET B  1 290 ? -66.032 25.197  -4.975  1.00 14.02 ? 290  MET B CA  1 
ATOM   5590 C  C   . MET B  1 290 ? -67.404 24.940  -4.335  1.00 12.89 ? 290  MET B C   1 
ATOM   5591 O  O   . MET B  1 290 ? -67.505 24.463  -3.154  1.00 13.43 ? 290  MET B O   1 
ATOM   5592 C  CB  . MET B  1 290 ? -65.519 23.908  -5.612  1.00 14.88 ? 290  MET B CB  1 
ATOM   5593 C  CG  . MET B  1 290 ? -64.293 24.114  -6.437  1.00 14.98 ? 290  MET B CG  1 
ATOM   5594 S  SD  . MET B  1 290 ? -63.896 22.607  -7.349  1.00 14.65 ? 290  MET B SD  1 
ATOM   5595 C  CE  . MET B  1 290 ? -63.302 23.324  -8.875  1.00 14.81 ? 290  MET B CE  1 
ATOM   5596 N  N   . THR B  1 291 ? -68.413 25.373  -5.069  1.00 14.41 ? 291  THR B N   1 
ATOM   5597 C  CA  . THR B  1 291 ? -69.842 25.318  -4.720  1.00 14.09 ? 291  THR B CA  1 
ATOM   5598 C  C   . THR B  1 291 ? -70.629 25.003  -5.981  1.00 13.97 ? 291  THR B C   1 
ATOM   5599 O  O   . THR B  1 291 ? -70.128 25.170  -7.125  1.00 13.56 ? 291  THR B O   1 
ATOM   5600 C  CB  . THR B  1 291 ? -70.291 26.641  -4.081  1.00 14.56 ? 291  THR B CB  1 
ATOM   5601 O  OG1 . THR B  1 291 ? -70.049 27.727  -4.992  1.00 16.11 ? 291  THR B OG1 1 
ATOM   5602 C  CG2 . THR B  1 291 ? -69.625 26.897  -2.757  1.00 15.23 ? 291  THR B CG2 1 
ATOM   5603 N  N   . GLY B  1 292 ? -71.884 24.604  -5.807  1.00 14.28 ? 292  GLY B N   1 
ATOM   5604 C  CA  . GLY B  1 292 ? -72.726 24.285  -6.966  1.00 15.00 ? 292  GLY B CA  1 
ATOM   5605 C  C   . GLY B  1 292 ? -72.616 22.807  -7.316  1.00 14.47 ? 292  GLY B C   1 
ATOM   5606 O  O   . GLY B  1 292 ? -72.716 21.967  -6.409  1.00 15.27 ? 292  GLY B O   1 
ATOM   5607 N  N   . ASN B  1 293 ? -72.465 22.511  -8.586  1.00 14.98 ? 293  ASN B N   1 
ATOM   5608 C  CA  . ASN B  1 293 ? -72.317 21.140  -9.110  1.00 15.86 ? 293  ASN B CA  1 
ATOM   5609 C  C   . ASN B  1 293 ? -70.917 20.935  -9.693  1.00 15.08 ? 293  ASN B C   1 
ATOM   5610 O  O   . ASN B  1 293 ? -70.392 21.777  -10.464 1.00 14.74 ? 293  ASN B O   1 
ATOM   5611 C  CB  . ASN B  1 293 ? -73.330 20.797  -10.190 1.00 17.05 ? 293  ASN B CB  1 
ATOM   5612 C  CG  . ASN B  1 293 ? -74.734 20.724  -9.627  1.00 19.36 ? 293  ASN B CG  1 
ATOM   5613 O  OD1 . ASN B  1 293 ? -74.931 20.180  -8.529  1.00 17.62 ? 293  ASN B OD1 1 
ATOM   5614 N  ND2 . ASN B  1 293 ? -75.674 21.368  -10.313 1.00 20.68 ? 293  ASN B ND2 1 
ATOM   5615 N  N   . MET B  1 294 ? -70.419 19.729  -9.484  1.00 14.77 ? 294  MET B N   1 
ATOM   5616 C  CA  . MET B  1 294 ? -69.233 19.240  -10.211 1.00 14.05 ? 294  MET B CA  1 
ATOM   5617 C  C   . MET B  1 294 ? -69.673 18.819  -11.601 1.00 15.31 ? 294  MET B C   1 
ATOM   5618 O  O   . MET B  1 294 ? -70.802 18.296  -11.761 1.00 15.33 ? 294  MET B O   1 
ATOM   5619 C  CB  . MET B  1 294 ? -68.611 18.048  -9.485  1.00 13.88 ? 294  MET B CB  1 
ATOM   5620 C  CG  . MET B  1 294 ? -68.116 18.398  -8.101  1.00 13.45 ? 294  MET B CG  1 
ATOM   5621 S  SD  . MET B  1 294 ? -66.960 19.794  -8.004  1.00 13.77 ? 294  MET B SD  1 
ATOM   5622 C  CE  . MET B  1 294 ? -65.512 19.151  -8.851  1.00 14.46 ? 294  MET B CE  1 
ATOM   5623 N  N   . VAL B  1 295 ? -68.843 19.082  -12.591 1.00 15.17 ? 295  VAL B N   1 
ATOM   5624 C  CA  . VAL B  1 295 ? -69.193 18.773  -14.003 1.00 15.82 ? 295  VAL B CA  1 
ATOM   5625 C  C   . VAL B  1 295 ? -68.082 17.931  -14.621 1.00 18.51 ? 295  VAL B C   1 
ATOM   5626 O  O   . VAL B  1 295 ? -66.943 17.867  -14.042 1.00 17.96 ? 295  VAL B O   1 
ATOM   5627 C  CB  . VAL B  1 295 ? -69.465 20.061  -14.794 1.00 16.91 ? 295  VAL B CB  1 
ATOM   5628 C  CG1 . VAL B  1 295 ? -70.610 20.869  -14.177 1.00 17.95 ? 295  VAL B CG1 1 
ATOM   5629 C  CG2 . VAL B  1 295 ? -68.221 20.916  -14.907 1.00 17.59 ? 295  VAL B CG2 1 
ATOM   5630 N  N   . ASN B  1 296 ? -68.407 17.321  -15.764 1.00 17.83 ? 296  ASN B N   1 
ATOM   5631 C  CA  . ASN B  1 296 ? -67.521 16.364  -16.449 1.00 19.23 ? 296  ASN B CA  1 
ATOM   5632 C  C   . ASN B  1 296 ? -66.332 17.133  -16.995 1.00 19.08 ? 296  ASN B C   1 
ATOM   5633 O  O   . ASN B  1 296 ? -66.514 18.129  -17.663 1.00 20.85 ? 296  ASN B O   1 
ATOM   5634 C  CB  . ASN B  1 296 ? -68.218 15.600  -17.572 1.00 21.21 ? 296  ASN B CB  1 
ATOM   5635 C  CG  . ASN B  1 296 ? -67.382 14.464  -18.111 1.00 23.63 ? 296  ASN B CG  1 
ATOM   5636 O  OD1 . ASN B  1 296 ? -66.757 13.731  -17.341 1.00 24.58 ? 296  ASN B OD1 1 
ATOM   5637 N  ND2 . ASN B  1 296 ? -67.467 14.254  -19.418 1.00 24.39 ? 296  ASN B ND2 1 
ATOM   5638 N  N   . VAL B  1 297 ? -65.149 16.614  -16.738 1.00 17.41 ? 297  VAL B N   1 
ATOM   5639 C  CA  . VAL B  1 297 ? -63.894 17.101  -17.353 1.00 18.12 ? 297  VAL B CA  1 
ATOM   5640 C  C   . VAL B  1 297 ? -63.304 15.915  -18.110 1.00 18.87 ? 297  VAL B C   1 
ATOM   5641 O  O   . VAL B  1 297 ? -63.135 14.830  -17.504 1.00 17.92 ? 297  VAL B O   1 
ATOM   5642 C  CB  . VAL B  1 297 ? -62.937 17.639  -16.289 1.00 18.28 ? 297  VAL B CB  1 
ATOM   5643 C  CG1 . VAL B  1 297 ? -61.598 18.007  -16.899 1.00 16.81 ? 297  VAL B CG1 1 
ATOM   5644 C  CG2 . VAL B  1 297 ? -63.525 18.793  -15.499 1.00 19.60 ? 297  VAL B CG2 1 
ATOM   5645 N  N   . ILE B  1 298 ? -63.073 16.101  -19.401 1.00 18.12 ? 298  ILE B N   1 
ATOM   5646 C  CA  . ILE B  1 298 ? -62.520 15.050  -20.292 1.00 19.20 ? 298  ILE B CA  1 
ATOM   5647 C  C   . ILE B  1 298 ? -61.011 15.248  -20.357 1.00 19.14 ? 298  ILE B C   1 
ATOM   5648 O  O   . ILE B  1 298 ? -60.530 16.264  -20.869 1.00 16.44 ? 298  ILE B O   1 
ATOM   5649 C  CB  . ILE B  1 298 ? -63.177 15.099  -21.686 1.00 22.63 ? 298  ILE B CB  1 
ATOM   5650 C  CG1 . ILE B  1 298 ? -64.698 14.997  -21.594 1.00 25.50 ? 298  ILE B CG1 1 
ATOM   5651 C  CG2 . ILE B  1 298 ? -62.596 14.019  -22.582 1.00 21.90 ? 298  ILE B CG2 1 
ATOM   5652 C  CD1 . ILE B  1 298 ? -65.397 15.620  -22.762 1.00 30.00 ? 298  ILE B CD1 1 
ATOM   5653 N  N   . PRO B  1 299 ? -60.226 14.297  -19.806 1.00 19.05 ? 299  PRO B N   1 
ATOM   5654 C  CA  . PRO B  1 299 ? -58.775 14.447  -19.741 1.00 18.21 ? 299  PRO B CA  1 
ATOM   5655 C  C   . PRO B  1 299 ? -58.104 13.999  -21.044 1.00 19.89 ? 299  PRO B C   1 
ATOM   5656 O  O   . PRO B  1 299 ? -58.705 13.279  -21.810 1.00 19.67 ? 299  PRO B O   1 
ATOM   5657 C  CB  . PRO B  1 299 ? -58.439 13.494  -18.595 1.00 17.99 ? 299  PRO B CB  1 
ATOM   5658 C  CG  . PRO B  1 299 ? -59.388 12.375  -18.786 1.00 18.01 ? 299  PRO B CG  1 
ATOM   5659 C  CD  . PRO B  1 299 ? -60.686 13.036  -19.215 1.00 19.66 ? 299  PRO B CD  1 
ATOM   5660 N  N   . GLN B  1 300 ? -56.859 14.431  -21.248 1.00 20.32 ? 300  GLN B N   1 
ATOM   5661 C  CA  . GLN B  1 300 ? -56.059 13.975  -22.402 1.00 21.98 ? 300  GLN B CA  1 
ATOM   5662 C  C   . GLN B  1 300 ? -55.870 12.467  -22.297 1.00 20.74 ? 300  GLN B C   1 
ATOM   5663 O  O   . GLN B  1 300 ? -56.038 11.769  -23.301 1.00 20.33 ? 300  GLN B O   1 
ATOM   5664 C  CB  . GLN B  1 300 ? -54.682 14.631  -22.436 1.00 24.82 ? 300  GLN B CB  1 
ATOM   5665 C  CG  . GLN B  1 300 ? -53.922 14.317  -23.720 1.00 25.20 ? 300  GLN B CG  1 
ATOM   5666 C  CD  . GLN B  1 300 ? -52.924 15.406  -24.013 1.00 27.29 ? 300  GLN B CD  1 
ATOM   5667 O  OE1 . GLN B  1 300 ? -53.292 16.558  -24.226 1.00 24.27 ? 300  GLN B OE1 1 
ATOM   5668 N  NE2 . GLN B  1 300 ? -51.652 15.047  -23.989 1.00 26.55 ? 300  GLN B NE2 1 
ATOM   5669 N  N   . ASN B  1 301 ? -55.511 11.990  -21.108 1.00 19.39 ? 301  ASN B N   1 
ATOM   5670 C  CA  . ASN B  1 301 ? -55.285 10.539  -20.893 1.00 18.20 ? 301  ASN B CA  1 
ATOM   5671 C  C   . ASN B  1 301 ? -55.669 10.203  -19.450 1.00 16.75 ? 301  ASN B C   1 
ATOM   5672 O  O   . ASN B  1 301 ? -54.872 10.432  -18.532 1.00 17.98 ? 301  ASN B O   1 
ATOM   5673 C  CB  . ASN B  1 301 ? -53.845 10.155  -21.223 1.00 19.66 ? 301  ASN B CB  1 
ATOM   5674 C  CG  . ASN B  1 301 ? -53.630 8.655   -21.155 1.00 22.90 ? 301  ASN B CG  1 
ATOM   5675 O  OD1 . ASN B  1 301 ? -54.465 7.896   -20.660 1.00 24.07 ? 301  ASN B OD1 1 
ATOM   5676 N  ND2 . ASN B  1 301 ? -52.483 8.212   -21.631 1.00 27.26 ? 301  ASN B ND2 1 
ATOM   5677 N  N   . ASP B  1 302 ? -56.856 9.643   -19.276 1.00 17.29 ? 302  ASP B N   1 
ATOM   5678 C  CA  . ASP B  1 302 ? -57.390 9.328   -17.927 1.00 17.14 ? 302  ASP B CA  1 
ATOM   5679 C  C   . ASP B  1 302 ? -56.448 8.347   -17.217 1.00 16.81 ? 302  ASP B C   1 
ATOM   5680 O  O   . ASP B  1 302 ? -56.318 8.406   -15.975 1.00 16.26 ? 302  ASP B O   1 
ATOM   5681 C  CB  . ASP B  1 302 ? -58.824 8.832   -18.068 1.00 18.21 ? 302  ASP B CB  1 
ATOM   5682 C  CG  . ASP B  1 302 ? -59.599 8.871   -16.768 1.00 19.53 ? 302  ASP B CG  1 
ATOM   5683 O  OD1 . ASP B  1 302 ? -59.180 9.621   -15.847 1.00 20.48 ? 302  ASP B OD1 1 
ATOM   5684 O  OD2 . ASP B  1 302 ? -60.634 8.179   -16.721 1.00 21.80 ? 302  ASP B OD2 1 
ATOM   5685 N  N   . ASN B  1 303 ? -55.766 7.487   -17.975 1.00 16.22 ? 303  ASN B N   1 
ATOM   5686 C  CA  . ASN B  1 303 ? -54.947 6.391   -17.415 1.00 16.66 ? 303  ASN B CA  1 
ATOM   5687 C  C   . ASN B  1 303 ? -53.488 6.857   -17.363 1.00 16.55 ? 303  ASN B C   1 
ATOM   5688 O  O   . ASN B  1 303 ? -52.615 6.098   -17.759 1.00 17.64 ? 303  ASN B O   1 
ATOM   5689 C  CB  . ASN B  1 303 ? -55.176 5.115   -18.211 1.00 18.86 ? 303  ASN B CB  1 
ATOM   5690 C  CG  . ASN B  1 303 ? -56.647 4.860   -18.471 1.00 22.95 ? 303  ASN B CG  1 
ATOM   5691 O  OD1 . ASN B  1 303 ? -57.089 4.825   -19.636 1.00 28.08 ? 303  ASN B OD1 1 
ATOM   5692 N  ND2 . ASN B  1 303 ? -57.433 4.697   -17.415 1.00 20.68 ? 303  ASN B ND2 1 
ATOM   5693 N  N   . SER B  1 304 ? -53.249 8.040   -16.818 1.00 16.47 ? 304  SER B N   1 
ATOM   5694 C  CA  . SER B  1 304 ? -51.916 8.680   -16.751 1.00 15.02 ? 304  SER B CA  1 
ATOM   5695 C  C   . SER B  1 304 ? -51.890 9.633   -15.571 1.00 15.50 ? 304  SER B C   1 
ATOM   5696 O  O   . SER B  1 304 ? -52.958 9.913   -15.026 1.00 13.89 ? 304  SER B O   1 
ATOM   5697 C  CB  . SER B  1 304 ? -51.611 9.405   -18.026 1.00 15.25 ? 304  SER B CB  1 
ATOM   5698 O  OG  . SER B  1 304 ? -52.292 10.663  -18.042 1.00 14.45 ? 304  SER B OG  1 
ATOM   5699 N  N   . ASN B  1 305 ? -50.722 10.210  -15.313 1.00 14.90 ? 305  ASN B N   1 
ATOM   5700 C  CA  . ASN B  1 305 ? -50.545 11.281  -14.302 1.00 15.06 ? 305  ASN B CA  1 
ATOM   5701 C  C   . ASN B  1 305 ? -50.452 12.626  -15.032 1.00 14.17 ? 305  ASN B C   1 
ATOM   5702 O  O   . ASN B  1 305 ? -49.989 13.583  -14.423 1.00 14.04 ? 305  ASN B O   1 
ATOM   5703 C  CB  . ASN B  1 305 ? -49.330 11.001  -13.420 1.00 15.33 ? 305  ASN B CB  1 
ATOM   5704 C  CG  . ASN B  1 305 ? -48.030 10.953  -14.187 1.00 15.74 ? 305  ASN B CG  1 
ATOM   5705 O  OD1 . ASN B  1 305 ? -48.010 11.268  -15.374 1.00 14.31 ? 305  ASN B OD1 1 
ATOM   5706 N  ND2 . ASN B  1 305 ? -46.959 10.538  -13.526 1.00 17.26 ? 305  ASN B ND2 1 
ATOM   5707 N  N   . LEU B  1 306 ? -50.856 12.681  -16.301 1.00 13.50 ? 306  LEU B N   1 
ATOM   5708 C  CA  . LEU B  1 306 ? -50.851 13.959  -17.051 1.00 14.39 ? 306  LEU B CA  1 
ATOM   5709 C  C   . LEU B  1 306 ? -51.853 14.914  -16.420 1.00 15.39 ? 306  LEU B C   1 
ATOM   5710 O  O   . LEU B  1 306 ? -52.794 14.460  -15.740 1.00 14.26 ? 306  LEU B O   1 
ATOM   5711 C  CB  . LEU B  1 306 ? -51.203 13.755  -18.521 1.00 15.31 ? 306  LEU B CB  1 
ATOM   5712 C  CG  . LEU B  1 306 ? -50.249 12.897  -19.348 1.00 16.83 ? 306  LEU B CG  1 
ATOM   5713 C  CD1 . LEU B  1 306 ? -50.706 12.898  -20.801 1.00 17.69 ? 306  LEU B CD1 1 
ATOM   5714 C  CD2 . LEU B  1 306 ? -48.811 13.358  -19.211 1.00 16.88 ? 306  LEU B CD2 1 
ATOM   5715 N  N   . ALA B  1 307 ? -51.673 16.190  -16.702 1.00 15.49 ? 307  ALA B N   1 
ATOM   5716 C  CA  . ALA B  1 307 ? -52.509 17.274  -16.162 1.00 15.58 ? 307  ALA B CA  1 
ATOM   5717 C  C   . ALA B  1 307 ? -53.965 16.876  -16.373 1.00 14.04 ? 307  ALA B C   1 
ATOM   5718 O  O   . ALA B  1 307 ? -54.353 16.381  -17.442 1.00 13.98 ? 307  ALA B O   1 
ATOM   5719 C  CB  . ALA B  1 307 ? -52.171 18.584  -16.808 1.00 18.15 ? 307  ALA B CB  1 
ATOM   5720 N  N   . ASP B  1 308 ? -54.744 17.048  -15.330 1.00 14.08 ? 308  ASP B N   1 
ATOM   5721 C  CA  . ASP B  1 308 ? -56.184 16.678  -15.316 1.00 13.89 ? 308  ASP B CA  1 
ATOM   5722 C  C   . ASP B  1 308 ? -56.844 17.728  -14.446 1.00 14.26 ? 308  ASP B C   1 
ATOM   5723 O  O   . ASP B  1 308 ? -56.154 18.396  -13.657 1.00 13.92 ? 308  ASP B O   1 
ATOM   5724 C  CB  . ASP B  1 308 ? -56.361 15.242  -14.808 1.00 14.91 ? 308  ASP B CB  1 
ATOM   5725 C  CG  . ASP B  1 308 ? -57.712 14.593  -15.059 1.00 15.41 ? 308  ASP B CG  1 
ATOM   5726 O  OD1 . ASP B  1 308 ? -58.628 15.297  -15.542 1.00 15.49 ? 308  ASP B OD1 1 
ATOM   5727 O  OD2 . ASP B  1 308 ? -57.847 13.368  -14.739 1.00 14.50 ? 308  ASP B OD2 1 
ATOM   5728 N  N   . GLY B  1 309 ? -58.161 17.788  -14.475 1.00 13.79 ? 309  GLY B N   1 
ATOM   5729 C  CA  . GLY B  1 309 ? -58.845 18.851  -13.741 1.00 14.24 ? 309  GLY B CA  1 
ATOM   5730 C  C   . GLY B  1 309 ? -60.219 18.418  -13.278 1.00 13.51 ? 309  GLY B C   1 
ATOM   5731 O  O   . GLY B  1 309 ? -60.743 17.371  -13.684 1.00 13.86 ? 309  GLY B O   1 
ATOM   5732 N  N   . PHE B  1 310 ? -60.719 19.193  -12.347 1.00 13.75 ? 310  PHE B N   1 
ATOM   5733 C  CA  . PHE B  1 310 ? -62.057 19.023  -11.770 1.00 12.20 ? 310  PHE B CA  1 
ATOM   5734 C  C   . PHE B  1 310 ? -62.651 20.417  -11.798 1.00 12.27 ? 310  PHE B C   1 
ATOM   5735 O  O   . PHE B  1 310 ? -61.916 21.429  -11.664 1.00 14.35 ? 310  PHE B O   1 
ATOM   5736 C  CB  . PHE B  1 310 ? -62.025 18.418  -10.361 1.00 12.92 ? 310  PHE B CB  1 
ATOM   5737 C  CG  . PHE B  1 310 ? -61.000 19.011  -9.436  1.00 12.91 ? 310  PHE B CG  1 
ATOM   5738 C  CD1 . PHE B  1 310 ? -59.654 18.732  -9.621  1.00 13.78 ? 310  PHE B CD1 1 
ATOM   5739 C  CD2 . PHE B  1 310 ? -61.367 19.835  -8.370  1.00 12.67 ? 310  PHE B CD2 1 
ATOM   5740 C  CE1 . PHE B  1 310 ? -58.688 19.261  -8.781  1.00 13.23 ? 310  PHE B CE1 1 
ATOM   5741 C  CE2 . PHE B  1 310 ? -60.415 20.305  -7.486  1.00 12.72 ? 310  PHE B CE2 1 
ATOM   5742 C  CZ  . PHE B  1 310 ? -59.069 20.046  -7.709  1.00 14.46 ? 310  PHE B CZ  1 
ATOM   5743 N  N   . ALA B  1 311 ? -63.968 20.486  -11.972 1.00 12.73 ? 311  ALA B N   1 
ATOM   5744 C  CA  . ALA B  1 311 ? -64.627 21.779  -12.241 1.00 13.05 ? 311  ALA B CA  1 
ATOM   5745 C  C   . ALA B  1 311 ? -66.021 21.826  -11.615 1.00 13.51 ? 311  ALA B C   1 
ATOM   5746 O  O   . ALA B  1 311 ? -66.705 20.792  -11.586 1.00 13.92 ? 311  ALA B O   1 
ATOM   5747 C  CB  . ALA B  1 311 ? -64.694 21.998  -13.731 1.00 12.99 ? 311  ALA B CB  1 
ATOM   5748 N  N   . CYS B  1 312 ? -66.389 23.027  -11.156 1.00 14.00 ? 312  CYS B N   1 
ATOM   5749 C  CA  . CYS B  1 312 ? -67.750 23.287  -10.643 1.00 13.40 ? 312  CYS B CA  1 
ATOM   5750 C  C   . CYS B  1 312 ? -68.401 24.427  -11.428 1.00 14.38 ? 312  CYS B C   1 
ATOM   5751 O  O   . CYS B  1 312 ? -67.712 25.237  -12.030 1.00 13.19 ? 312  CYS B O   1 
ATOM   5752 C  CB  . CYS B  1 312 ? -67.738 23.526  -9.136  1.00 13.18 ? 312  CYS B CB  1 
ATOM   5753 S  SG  . CYS B  1 312 ? -67.024 25.113  -8.650  1.00 14.51 ? 312  CYS B SG  1 
ATOM   5754 N  N   . VAL B  1 313 ? -69.718 24.348  -11.523 1.00 14.26 ? 313  VAL B N   1 
ATOM   5755 C  CA  . VAL B  1 313 ? -70.572 25.405  -12.111 1.00 15.67 ? 313  VAL B CA  1 
ATOM   5756 C  C   . VAL B  1 313 ? -71.592 25.751  -11.033 1.00 15.63 ? 313  VAL B C   1 
ATOM   5757 O  O   . VAL B  1 313 ? -72.215 24.800  -10.495 1.00 15.09 ? 313  VAL B O   1 
ATOM   5758 C  CB  . VAL B  1 313 ? -71.258 24.951  -13.404 1.00 16.77 ? 313  VAL B CB  1 
ATOM   5759 C  CG1 . VAL B  1 313 ? -72.117 26.071  -13.968 1.00 18.60 ? 313  VAL B CG1 1 
ATOM   5760 C  CG2 . VAL B  1 313 ? -70.282 24.448  -14.442 1.00 18.30 ? 313  VAL B CG2 1 
ATOM   5761 N  N   . ASP B  1 314 ? -71.678 27.027  -10.662 1.00 15.75 ? 314  ASP B N   1 
ATOM   5762 C  CA  . ASP B  1 314 ? -72.587 27.515  -9.589  1.00 15.74 ? 314  ASP B CA  1 
ATOM   5763 C  C   . ASP B  1 314 ? -73.403 28.665  -10.187 1.00 15.11 ? 314  ASP B C   1 
ATOM   5764 O  O   . ASP B  1 314 ? -72.855 29.784  -10.318 1.00 14.99 ? 314  ASP B O   1 
ATOM   5765 C  CB  . ASP B  1 314 ? -71.820 27.933  -8.335  1.00 16.68 ? 314  ASP B CB  1 
ATOM   5766 C  CG  . ASP B  1 314 ? -72.693 28.317  -7.161  1.00 16.38 ? 314  ASP B CG  1 
ATOM   5767 O  OD1 . ASP B  1 314 ? -73.874 28.721  -7.416  1.00 17.24 ? 314  ASP B OD1 1 
ATOM   5768 O  OD2 . ASP B  1 314 ? -72.230 28.188  -5.998  1.00 15.25 ? 314  ASP B OD2 1 
ATOM   5769 N  N   . SER B  1 315 ? -74.651 28.408  -10.544 1.00 16.01 ? 315  SER B N   1 
ATOM   5770 C  CA  . SER B  1 315 ? -75.529 29.459  -11.149 1.00 16.15 ? 315  SER B CA  1 
ATOM   5771 C  C   . SER B  1 315 ? -76.131 30.337  -10.048 1.00 16.01 ? 315  SER B C   1 
ATOM   5772 O  O   . SER B  1 315 ? -76.718 31.348  -10.385 1.00 17.40 ? 315  SER B O   1 
ATOM   5773 C  CB  . SER B  1 315 ? -76.585 28.860  -12.001 1.00 15.81 ? 315  SER B CB  1 
ATOM   5774 O  OG  . SER B  1 315 ? -77.451 28.059  -11.213 1.00 16.99 ? 315  SER B OG  1 
ATOM   5775 N  N   . ASN B  1 316 ? -76.014 29.973  -8.772  1.00 15.61 ? 316  ASN B N   1 
ATOM   5776 C  CA  . ASN B  1 316 ? -76.406 30.865  -7.648  1.00 15.51 ? 316  ASN B CA  1 
ATOM   5777 C  C   . ASN B  1 316 ? -75.383 32.009  -7.533  1.00 15.73 ? 316  ASN B C   1 
ATOM   5778 O  O   . ASN B  1 316 ? -75.747 33.219  -7.587  1.00 17.45 ? 316  ASN B O   1 
ATOM   5779 C  CB  . ASN B  1 316 ? -76.492 30.118  -6.313  1.00 15.30 ? 316  ASN B CB  1 
ATOM   5780 C  CG  . ASN B  1 316 ? -77.378 28.888  -6.304  1.00 16.44 ? 316  ASN B CG  1 
ATOM   5781 O  OD1 . ASN B  1 316 ? -76.972 27.832  -5.802  1.00 18.72 ? 316  ASN B OD1 1 
ATOM   5782 N  ND2 . ASN B  1 316 ? -78.564 28.994  -6.843  1.00 13.58 ? 316  ASN B ND2 1 
ATOM   5783 N  N   . ALA B  1 317 ? -74.120 31.629  -7.346  1.00 16.89 ? 317  ALA B N   1 
ATOM   5784 C  CA  . ALA B  1 317 ? -72.974 32.544  -7.148  1.00 17.19 ? 317  ALA B CA  1 
ATOM   5785 C  C   . ALA B  1 317 ? -72.477 33.056  -8.499  1.00 16.97 ? 317  ALA B C   1 
ATOM   5786 O  O   . ALA B  1 317 ? -71.793 34.096  -8.506  1.00 18.74 ? 317  ALA B O   1 
ATOM   5787 C  CB  . ALA B  1 317 ? -71.890 31.856  -6.344  1.00 17.75 ? 317  ALA B CB  1 
ATOM   5788 N  N   . LYS B  1 318 ? -72.848 32.412  -9.593  1.00 17.21 ? 318  LYS B N   1 
ATOM   5789 C  CA  . LYS B  1 318 ? -72.645 32.872  -10.988 1.00 18.38 ? 318  LYS B CA  1 
ATOM   5790 C  C   . LYS B  1 318 ? -71.171 32.733  -11.416 1.00 18.63 ? 318  LYS B C   1 
ATOM   5791 O  O   . LYS B  1 318 ? -70.568 33.709  -11.853 1.00 18.46 ? 318  LYS B O   1 
ATOM   5792 C  CB  . LYS B  1 318 ? -73.152 34.302  -11.123 1.00 21.06 ? 318  LYS B CB  1 
ATOM   5793 C  CG  . LYS B  1 318 ? -74.654 34.382  -10.919 1.00 23.89 ? 318  LYS B CG  1 
ATOM   5794 C  CD  . LYS B  1 318 ? -75.167 35.769  -10.998 1.00 29.27 ? 318  LYS B CD  1 
ATOM   5795 C  CE  . LYS B  1 318 ? -74.693 36.593  -9.831  1.00 34.54 ? 318  LYS B CE  1 
ATOM   5796 N  NZ  . LYS B  1 318 ? -75.696 37.632  -9.487  1.00 42.63 ? 318  LYS B NZ  1 
ATOM   5797 N  N   . TYR B  1 319 ? -70.599 31.539  -11.310 1.00 17.01 ? 319  TYR B N   1 
ATOM   5798 C  CA  . TYR B  1 319 ? -69.194 31.336  -11.754 1.00 16.84 ? 319  TYR B CA  1 
ATOM   5799 C  C   . TYR B  1 319 ? -68.974 29.889  -12.174 1.00 16.32 ? 319  TYR B C   1 
ATOM   5800 O  O   . TYR B  1 319 ? -69.770 29.004  -11.840 1.00 16.93 ? 319  TYR B O   1 
ATOM   5801 C  CB  . TYR B  1 319 ? -68.210 31.757  -10.660 1.00 15.34 ? 319  TYR B CB  1 
ATOM   5802 C  CG  . TYR B  1 319 ? -68.090 30.778  -9.523  1.00 15.91 ? 319  TYR B CG  1 
ATOM   5803 C  CD1 . TYR B  1 319 ? -67.167 29.738  -9.566  1.00 15.45 ? 319  TYR B CD1 1 
ATOM   5804 C  CD2 . TYR B  1 319 ? -68.925 30.841  -8.412  1.00 14.42 ? 319  TYR B CD2 1 
ATOM   5805 C  CE1 . TYR B  1 319 ? -67.079 28.812  -8.537  1.00 15.64 ? 319  TYR B CE1 1 
ATOM   5806 C  CE2 . TYR B  1 319 ? -68.840 29.928  -7.375  1.00 14.38 ? 319  TYR B CE2 1 
ATOM   5807 C  CZ  . TYR B  1 319 ? -67.925 28.885  -7.445  1.00 16.38 ? 319  TYR B CZ  1 
ATOM   5808 O  OH  . TYR B  1 319 ? -67.843 27.988  -6.423  1.00 15.47 ? 319  TYR B OH  1 
ATOM   5809 N  N   . ILE B  1 320 ? -67.878 29.693  -12.902 1.00 16.79 ? 320  ILE B N   1 
ATOM   5810 C  CA  . ILE B  1 320 ? -67.288 28.370  -13.230 1.00 16.28 ? 320  ILE B CA  1 
ATOM   5811 C  C   . ILE B  1 320 ? -65.887 28.374  -12.646 1.00 16.91 ? 320  ILE B C   1 
ATOM   5812 O  O   . ILE B  1 320 ? -65.125 29.313  -12.932 1.00 17.36 ? 320  ILE B O   1 
ATOM   5813 C  CB  . ILE B  1 320 ? -67.268 28.124  -14.748 1.00 17.15 ? 320  ILE B CB  1 
ATOM   5814 C  CG1 . ILE B  1 320 ? -68.661 28.291  -15.362 1.00 18.63 ? 320  ILE B CG1 1 
ATOM   5815 C  CG2 . ILE B  1 320 ? -66.673 26.762  -15.075 1.00 17.15 ? 320  ILE B CG2 1 
ATOM   5816 C  CD1 . ILE B  1 320 ? -68.647 28.407  -16.858 1.00 19.18 ? 320  ILE B CD1 1 
ATOM   5817 N  N   . SER B  1 321 ? -65.526 27.350  -11.883 1.00 16.14 ? 321  SER B N   1 
ATOM   5818 C  CA  . SER B  1 321 ? -64.132 27.191  -11.418 1.00 15.54 ? 321  SER B CA  1 
ATOM   5819 C  C   . SER B  1 321 ? -63.543 25.881  -11.935 1.00 16.17 ? 321  SER B C   1 
ATOM   5820 O  O   . SER B  1 321 ? -64.191 24.825  -11.775 1.00 15.53 ? 321  SER B O   1 
ATOM   5821 C  CB  . SER B  1 321 ? -64.073 27.270  -9.924  1.00 14.86 ? 321  SER B CB  1 
ATOM   5822 O  OG  . SER B  1 321 ? -62.725 27.045  -9.535  1.00 15.44 ? 321  SER B OG  1 
ATOM   5823 N  N   . VAL B  1 322 ? -62.359 25.942  -12.563 1.00 15.68 ? 322  VAL B N   1 
ATOM   5824 C  CA  . VAL B  1 322 ? -61.628 24.745  -13.047 1.00 15.19 ? 322  VAL B CA  1 
ATOM   5825 C  C   . VAL B  1 322 ? -60.311 24.687  -12.280 1.00 14.79 ? 322  VAL B C   1 
ATOM   5826 O  O   . VAL B  1 322 ? -59.541 25.670  -12.322 1.00 14.50 ? 322  VAL B O   1 
ATOM   5827 C  CB  . VAL B  1 322 ? -61.403 24.790  -14.568 1.00 15.90 ? 322  VAL B CB  1 
ATOM   5828 C  CG1 . VAL B  1 322 ? -60.811 23.485  -15.066 1.00 15.32 ? 322  VAL B CG1 1 
ATOM   5829 C  CG2 . VAL B  1 322 ? -62.661 25.109  -15.357 1.00 15.56 ? 322  VAL B CG2 1 
ATOM   5830 N  N   . LEU B  1 323 ? -60.054 23.584  -11.581 1.00 14.16 ? 323  LEU B N   1 
ATOM   5831 C  CA  . LEU B  1 323 ? -58.773 23.363  -10.893 1.00 13.73 ? 323  LEU B CA  1 
ATOM   5832 C  C   . LEU B  1 323 ? -58.010 22.229  -11.575 1.00 14.32 ? 323  LEU B C   1 
ATOM   5833 O  O   . LEU B  1 323 ? -58.614 21.218  -11.926 1.00 15.31 ? 323  LEU B O   1 
ATOM   5834 C  CB  . LEU B  1 323 ? -59.023 23.055  -9.428  1.00 13.54 ? 323  LEU B CB  1 
ATOM   5835 C  CG  . LEU B  1 323 ? -59.433 24.266  -8.610  1.00 14.53 ? 323  LEU B CG  1 
ATOM   5836 C  CD1 . LEU B  1 323 ? -60.032 23.855  -7.279  1.00 15.08 ? 323  LEU B CD1 1 
ATOM   5837 C  CD2 . LEU B  1 323 ? -58.235 25.207  -8.464  1.00 15.01 ? 323  LEU B CD2 1 
ATOM   5838 N  N   . LEU B  1 324 ? -56.701 22.400  -11.747 1.00 13.86 ? 324  LEU B N   1 
ATOM   5839 C  CA  . LEU B  1 324 ? -55.949 21.423  -12.566 1.00 13.81 ? 324  LEU B CA  1 
ATOM   5840 C  C   . LEU B  1 324 ? -54.462 21.468  -12.235 1.00 14.04 ? 324  LEU B C   1 
ATOM   5841 O  O   . LEU B  1 324 ? -53.999 22.372  -11.540 1.00 14.00 ? 324  LEU B O   1 
ATOM   5842 C  CB  . LEU B  1 324 ? -56.174 21.738  -14.041 1.00 15.06 ? 324  LEU B CB  1 
ATOM   5843 C  CG  . LEU B  1 324 ? -55.574 23.063  -14.516 1.00 16.83 ? 324  LEU B CG  1 
ATOM   5844 C  CD1 . LEU B  1 324 ? -54.160 22.856  -15.041 1.00 18.52 ? 324  LEU B CD1 1 
ATOM   5845 C  CD2 . LEU B  1 324 ? -56.439 23.693  -15.582 1.00 18.57 ? 324  LEU B CD2 1 
ATOM   5846 N  N   . GLY B  1 325 ? -53.786 20.413  -12.670 1.00 14.11 ? 325  GLY B N   1 
ATOM   5847 C  CA  . GLY B  1 325 ? -52.356 20.240  -12.448 1.00 12.74 ? 325  GLY B CA  1 
ATOM   5848 C  C   . GLY B  1 325 ? -51.952 18.844  -12.825 1.00 13.21 ? 325  GLY B C   1 
ATOM   5849 O  O   . GLY B  1 325 ? -52.850 17.995  -13.008 1.00 13.57 ? 325  GLY B O   1 
ATOM   5850 N  N   . GLY B  1 326 ? -50.651 18.619  -12.907 1.00 13.06 ? 326  GLY B N   1 
ATOM   5851 C  CA  . GLY B  1 326 ? -50.060 17.321  -13.284 1.00 13.28 ? 326  GLY B CA  1 
ATOM   5852 C  C   . GLY B  1 326 ? -49.061 17.467  -14.396 1.00 14.11 ? 326  GLY B C   1 
ATOM   5853 O  O   . GLY B  1 326 ? -48.662 18.597  -14.725 1.00 14.77 ? 326  GLY B O   1 
ATOM   5854 N  N   . VAL B  1 327 ? -48.617 16.336  -14.942 1.00 14.60 ? 327  VAL B N   1 
ATOM   5855 C  CA  . VAL B  1 327 ? -47.478 16.289  -15.890 1.00 14.00 ? 327  VAL B CA  1 
ATOM   5856 C  C   . VAL B  1 327 ? -47.962 16.901  -17.197 1.00 14.34 ? 327  VAL B C   1 
ATOM   5857 O  O   . VAL B  1 327 ? -49.029 16.531  -17.690 1.00 14.44 ? 327  VAL B O   1 
ATOM   5858 C  CB  . VAL B  1 327 ? -46.989 14.842  -16.053 1.00 14.74 ? 327  VAL B CB  1 
ATOM   5859 C  CG1 . VAL B  1 327 ? -45.969 14.717  -17.167 1.00 15.65 ? 327  VAL B CG1 1 
ATOM   5860 C  CG2 . VAL B  1 327 ? -46.450 14.338  -14.734 1.00 14.58 ? 327  VAL B CG2 1 
ATOM   5861 N  N   . ASN B  1 328 ? -47.197 17.835  -17.759 1.00 15.51 ? 328  ASN B N   1 
ATOM   5862 C  CA  . ASN B  1 328 ? -47.627 18.481  -19.019 1.00 16.49 ? 328  ASN B CA  1 
ATOM   5863 C  C   . ASN B  1 328 ? -46.397 18.918  -19.817 1.00 18.44 ? 328  ASN B C   1 
ATOM   5864 O  O   . ASN B  1 328 ? -45.279 18.790  -19.288 1.00 17.19 ? 328  ASN B O   1 
ATOM   5865 C  CB  . ASN B  1 328 ? -48.558 19.652  -18.716 1.00 16.91 ? 328  ASN B CB  1 
ATOM   5866 C  CG  . ASN B  1 328 ? -47.848 20.718  -17.919 1.00 17.10 ? 328  ASN B CG  1 
ATOM   5867 O  OD1 . ASN B  1 328 ? -47.114 21.519  -18.497 1.00 16.82 ? 328  ASN B OD1 1 
ATOM   5868 N  ND2 . ASN B  1 328 ? -48.078 20.748  -16.608 1.00 15.37 ? 328  ASN B ND2 1 
ATOM   5869 N  N   . ASP B  1 329 ? -46.641 19.384  -21.039 1.00 19.93 ? 329  ASP B N   1 
ATOM   5870 C  CA  . ASP B  1 329 ? -45.571 19.698  -22.016 1.00 21.68 ? 329  ASP B CA  1 
ATOM   5871 C  C   . ASP B  1 329 ? -45.196 21.170  -21.904 1.00 22.91 ? 329  ASP B C   1 
ATOM   5872 O  O   . ASP B  1 329 ? -44.407 21.609  -22.732 1.00 23.93 ? 329  ASP B O   1 
ATOM   5873 C  CB  . ASP B  1 329 ? -45.966 19.266  -23.419 1.00 23.50 ? 329  ASP B CB  1 
ATOM   5874 C  CG  . ASP B  1 329 ? -47.042 20.124  -24.067 1.00 24.14 ? 329  ASP B CG  1 
ATOM   5875 O  OD1 . ASP B  1 329 ? -47.402 21.163  -23.480 1.00 26.70 ? 329  ASP B OD1 1 
ATOM   5876 O  OD2 . ASP B  1 329 ? -47.483 19.749  -25.158 1.00 26.36 ? 329  ASP B OD2 1 
ATOM   5877 N  N   . GLY B  1 330 ? -45.654 21.879  -20.875 1.00 21.08 ? 330  GLY B N   1 
ATOM   5878 C  CA  . GLY B  1 330 ? -45.237 23.270  -20.622 1.00 20.99 ? 330  GLY B CA  1 
ATOM   5879 C  C   . GLY B  1 330 ? -46.276 24.289  -21.050 1.00 19.47 ? 330  GLY B C   1 
ATOM   5880 O  O   . GLY B  1 330 ? -46.061 25.508  -20.803 1.00 19.91 ? 330  GLY B O   1 
ATOM   5881 N  N   . THR B  1 331 ? -47.391 23.826  -21.604 1.00 20.61 ? 331  THR B N   1 
ATOM   5882 C  CA  . THR B  1 331 ? -48.618 24.627  -21.853 1.00 21.08 ? 331  THR B CA  1 
ATOM   5883 C  C   . THR B  1 331 ? -49.830 23.767  -21.493 1.00 19.99 ? 331  THR B C   1 
ATOM   5884 O  O   . THR B  1 331 ? -49.813 22.572  -21.822 1.00 20.30 ? 331  THR B O   1 
ATOM   5885 C  CB  . THR B  1 331 ? -48.738 25.075  -23.318 1.00 22.43 ? 331  THR B CB  1 
ATOM   5886 O  OG1 . THR B  1 331 ? -47.549 25.782  -23.679 1.00 23.15 ? 331  THR B OG1 1 
ATOM   5887 C  CG2 . THR B  1 331 ? -49.942 25.965  -23.562 1.00 24.70 ? 331  THR B CG2 1 
ATOM   5888 N  N   . VAL B  1 332 ? -50.845 24.364  -20.877 1.00 20.53 ? 332  VAL B N   1 
ATOM   5889 C  CA  . VAL B  1 332 ? -52.113 23.632  -20.611 1.00 19.02 ? 332  VAL B CA  1 
ATOM   5890 C  C   . VAL B  1 332 ? -53.253 24.406  -21.263 1.00 19.91 ? 332  VAL B C   1 
ATOM   5891 O  O   . VAL B  1 332 ? -53.403 25.619  -20.981 1.00 20.85 ? 332  VAL B O   1 
ATOM   5892 C  CB  . VAL B  1 332 ? -52.348 23.407  -19.111 1.00 19.16 ? 332  VAL B CB  1 
ATOM   5893 C  CG1 . VAL B  1 332 ? -53.697 22.729  -18.858 1.00 18.97 ? 332  VAL B CG1 1 
ATOM   5894 C  CG2 . VAL B  1 332 ? -51.226 22.611  -18.503 1.00 18.47 ? 332  VAL B CG2 1 
ATOM   5895 N  N   . ASN B  1 333 ? -53.982 23.724  -22.133 1.00 20.83 ? 333  ASN B N   1 
ATOM   5896 C  CA  . ASN B  1 333 ? -55.189 24.277  -22.781 1.00 21.25 ? 333  ASN B CA  1 
ATOM   5897 C  C   . ASN B  1 333 ? -56.424 23.720  -22.064 1.00 22.06 ? 333  ASN B C   1 
ATOM   5898 O  O   . ASN B  1 333 ? -56.483 22.504  -21.772 1.00 22.06 ? 333  ASN B O   1 
ATOM   5899 C  CB  . ASN B  1 333 ? -55.171 24.031  -24.287 1.00 22.44 ? 333  ASN B CB  1 
ATOM   5900 C  CG  . ASN B  1 333 ? -54.111 24.846  -24.982 1.00 21.82 ? 333  ASN B CG  1 
ATOM   5901 O  OD1 . ASN B  1 333 ? -53.458 25.701  -24.378 1.00 25.30 ? 333  ASN B OD1 1 
ATOM   5902 N  ND2 . ASN B  1 333 ? -53.906 24.546  -26.249 1.00 23.29 ? 333  ASN B ND2 1 
ATOM   5903 N  N   . VAL B  1 334 ? -57.353 24.623  -21.758 1.00 21.43 ? 334  VAL B N   1 
ATOM   5904 C  CA  . VAL B  1 334 ? -58.635 24.301  -21.079 1.00 21.39 ? 334  VAL B CA  1 
ATOM   5905 C  C   . VAL B  1 334 ? -59.738 24.782  -22.020 1.00 23.06 ? 334  VAL B C   1 
ATOM   5906 O  O   . VAL B  1 334 ? -59.867 26.017  -22.185 1.00 23.20 ? 334  VAL B O   1 
ATOM   5907 C  CB  . VAL B  1 334 ? -58.701 24.946  -19.689 1.00 20.44 ? 334  VAL B CB  1 
ATOM   5908 C  CG1 . VAL B  1 334 ? -59.999 24.548  -19.000 1.00 21.67 ? 334  VAL B CG1 1 
ATOM   5909 C  CG2 . VAL B  1 334 ? -57.486 24.616  -18.837 1.00 21.03 ? 334  VAL B CG2 1 
ATOM   5910 N  N   . ASN B  1 335 ? -60.379 23.834  -22.702 1.00 23.67 ? 335  ASN B N   1 
ATOM   5911 C  CA  . ASN B  1 335 ? -61.540 24.046  -23.591 1.00 24.00 ? 335  ASN B CA  1 
ATOM   5912 C  C   . ASN B  1 335 ? -62.780 23.953  -22.706 1.00 23.05 ? 335  ASN B C   1 
ATOM   5913 O  O   . ASN B  1 335 ? -62.998 22.892  -22.133 1.00 22.00 ? 335  ASN B O   1 
ATOM   5914 C  CB  . ASN B  1 335 ? -61.561 23.034  -24.731 1.00 26.20 ? 335  ASN B CB  1 
ATOM   5915 C  CG  . ASN B  1 335 ? -60.341 23.142  -25.627 1.00 30.70 ? 335  ASN B CG  1 
ATOM   5916 O  OD1 . ASN B  1 335 ? -59.679 24.182  -25.664 1.00 32.77 ? 335  ASN B OD1 1 
ATOM   5917 N  ND2 . ASN B  1 335 ? -60.071 22.078  -26.373 1.00 32.40 ? 335  ASN B ND2 1 
ATOM   5918 N  N   . ILE B  1 336 ? -63.498 25.053  -22.538 1.00 23.03 ? 336  ILE B N   1 
ATOM   5919 C  CA  . ILE B  1 336 ? -64.736 25.098  -21.711 1.00 22.17 ? 336  ILE B CA  1 
ATOM   5920 C  C   . ILE B  1 336 ? -65.909 25.168  -22.677 1.00 22.60 ? 336  ILE B C   1 
ATOM   5921 O  O   . ILE B  1 336 ? -65.962 26.142  -23.411 1.00 26.38 ? 336  ILE B O   1 
ATOM   5922 C  CB  . ILE B  1 336 ? -64.691 26.301  -20.759 1.00 21.10 ? 336  ILE B CB  1 
ATOM   5923 C  CG1 . ILE B  1 336 ? -63.362 26.340  -19.992 1.00 21.99 ? 336  ILE B CG1 1 
ATOM   5924 C  CG2 . ILE B  1 336 ? -65.920 26.281  -19.856 1.00 21.60 ? 336  ILE B CG2 1 
ATOM   5925 C  CD1 . ILE B  1 336 ? -63.269 27.375  -18.897 1.00 23.12 ? 336  ILE B CD1 1 
ATOM   5926 N  N   . LYS B  1 337 ? -66.772 24.160  -22.712 1.00 22.14 ? 337  LYS B N   1 
ATOM   5927 C  CA  . LYS B  1 337 ? -67.867 24.121  -23.705 1.00 24.60 ? 337  LYS B CA  1 
ATOM   5928 C  C   . LYS B  1 337 ? -69.213 24.072  -22.977 1.00 25.40 ? 337  LYS B C   1 
ATOM   5929 O  O   . LYS B  1 337 ? -69.229 23.902  -21.741 1.00 21.96 ? 337  LYS B O   1 
ATOM   5930 C  CB  . LYS B  1 337 ? -67.696 22.966  -24.688 1.00 27.95 ? 337  LYS B CB  1 
ATOM   5931 C  CG  . LYS B  1 337 ? -67.766 21.573  -24.091 1.00 32.54 ? 337  LYS B CG  1 
ATOM   5932 C  CD  . LYS B  1 337 ? -67.676 20.473  -25.154 1.00 34.38 ? 337  LYS B CD  1 
ATOM   5933 C  CE  . LYS B  1 337 ? -67.508 19.093  -24.546 1.00 38.86 ? 337  LYS B CE  1 
ATOM   5934 N  NZ  . LYS B  1 337 ? -67.926 18.007  -25.465 1.00 39.65 ? 337  LYS B NZ  1 
ATOM   5935 N  N   . ASN B  1 338 ? -70.296 24.288  -23.727 1.00 22.71 ? 338  ASN B N   1 
ATOM   5936 C  CA  . ASN B  1 338 ? -71.687 24.227  -23.202 1.00 24.17 ? 338  ASN B CA  1 
ATOM   5937 C  C   . ASN B  1 338 ? -71.783 25.205  -22.030 1.00 25.00 ? 338  ASN B C   1 
ATOM   5938 O  O   . ASN B  1 338 ? -72.468 24.910  -21.035 1.00 24.82 ? 338  ASN B O   1 
ATOM   5939 C  CB  . ASN B  1 338 ? -72.104 22.790  -22.855 1.00 25.68 ? 338  ASN B CB  1 
ATOM   5940 C  CG  . ASN B  1 338 ? -72.270 21.907  -24.084 1.00 30.76 ? 338  ASN B CG  1 
ATOM   5941 O  OD1 . ASN B  1 338 ? -72.801 22.345  -25.112 1.00 33.04 ? 338  ASN B OD1 1 
ATOM   5942 N  ND2 . ASN B  1 338 ? -71.825 20.662  -23.997 1.00 29.98 ? 338  ASN B ND2 1 
ATOM   5943 N  N   . ILE B  1 339 ? -71.144 26.359  -22.165 1.00 22.81 ? 339  ILE B N   1 
ATOM   5944 C  CA  . ILE B  1 339 ? -71.128 27.391  -21.104 1.00 21.82 ? 339  ILE B CA  1 
ATOM   5945 C  C   . ILE B  1 339 ? -72.578 27.778  -20.821 1.00 26.34 ? 339  ILE B C   1 
ATOM   5946 O  O   . ILE B  1 339 ? -73.373 27.929  -21.745 1.00 26.51 ? 339  ILE B O   1 
ATOM   5947 C  CB  . ILE B  1 339 ? -70.259 28.580  -21.548 1.00 22.19 ? 339  ILE B CB  1 
ATOM   5948 C  CG1 . ILE B  1 339 ? -68.780 28.188  -21.496 1.00 23.06 ? 339  ILE B CG1 1 
ATOM   5949 C  CG2 . ILE B  1 339 ? -70.543 29.801  -20.701 1.00 21.20 ? 339  ILE B CG2 1 
ATOM   5950 C  CD1 . ILE B  1 339 ? -67.839 29.189  -22.103 1.00 22.45 ? 339  ILE B CD1 1 
ATOM   5951 N  N   . PRO B  1 340 ? -72.987 27.923  -19.543 1.00 25.99 ? 340  PRO B N   1 
ATOM   5952 C  CA  . PRO B  1 340 ? -74.350 28.353  -19.238 1.00 24.45 ? 340  PRO B CA  1 
ATOM   5953 C  C   . PRO B  1 340 ? -74.660 29.790  -19.677 1.00 25.00 ? 340  PRO B C   1 
ATOM   5954 O  O   . PRO B  1 340 ? -73.786 30.612  -19.820 1.00 24.25 ? 340  PRO B O   1 
ATOM   5955 C  CB  . PRO B  1 340 ? -74.466 28.246  -17.708 1.00 26.61 ? 340  PRO B CB  1 
ATOM   5956 C  CG  . PRO B  1 340 ? -73.028 28.199  -17.213 1.00 26.04 ? 340  PRO B CG  1 
ATOM   5957 C  CD  . PRO B  1 340 ? -72.220 27.580  -18.335 1.00 25.78 ? 340  PRO B CD  1 
ATOM   5958 N  N   . ALA B  1 341 ? -75.950 30.054  -19.852 1.00 25.76 ? 341  ALA B N   1 
ATOM   5959 C  CA  . ALA B  1 341 ? -76.482 31.364  -20.258 1.00 24.93 ? 341  ALA B CA  1 
ATOM   5960 C  C   . ALA B  1 341 ? -76.032 32.437  -19.267 1.00 24.35 ? 341  ALA B C   1 
ATOM   5961 O  O   . ALA B  1 341 ? -75.722 33.577  -19.699 1.00 23.55 ? 341  ALA B O   1 
ATOM   5962 C  CB  . ALA B  1 341 ? -77.982 31.253  -20.338 1.00 28.07 ? 341  ALA B CB  1 
ATOM   5963 N  N   . PHE B  1 342 ? -75.986 32.137  -17.968 1.00 23.23 ? 342  PHE B N   1 
ATOM   5964 C  CA  . PHE B  1 342 ? -75.710 33.189  -16.961 1.00 23.76 ? 342  PHE B CA  1 
ATOM   5965 C  C   . PHE B  1 342 ? -74.347 33.868  -17.205 1.00 26.22 ? 342  PHE B C   1 
ATOM   5966 O  O   . PHE B  1 342 ? -74.122 34.979  -16.669 1.00 23.47 ? 342  PHE B O   1 
ATOM   5967 C  CB  . PHE B  1 342 ? -75.848 32.652  -15.538 1.00 23.29 ? 342  PHE B CB  1 
ATOM   5968 C  CG  . PHE B  1 342 ? -74.734 31.761  -15.044 1.00 22.98 ? 342  PHE B CG  1 
ATOM   5969 C  CD1 . PHE B  1 342 ? -73.518 32.300  -14.635 1.00 24.28 ? 342  PHE B CD1 1 
ATOM   5970 C  CD2 . PHE B  1 342 ? -74.918 30.388  -14.967 1.00 22.61 ? 342  PHE B CD2 1 
ATOM   5971 C  CE1 . PHE B  1 342 ? -72.505 31.476  -14.176 1.00 20.86 ? 342  PHE B CE1 1 
ATOM   5972 C  CE2 . PHE B  1 342 ? -73.913 29.572  -14.472 1.00 20.87 ? 342  PHE B CE2 1 
ATOM   5973 C  CZ  . PHE B  1 342 ? -72.721 30.122  -14.071 1.00 21.09 ? 342  PHE B CZ  1 
ATOM   5974 N  N   . ILE B  1 343 ? -73.453 33.247  -17.978 1.00 25.45 ? 343  ILE B N   1 
ATOM   5975 C  CA  . ILE B  1 343 ? -72.122 33.855  -18.287 1.00 27.19 ? 343  ILE B CA  1 
ATOM   5976 C  C   . ILE B  1 343 ? -72.314 34.976  -19.316 1.00 29.15 ? 343  ILE B C   1 
ATOM   5977 O  O   . ILE B  1 343 ? -71.603 36.008  -19.225 1.00 28.00 ? 343  ILE B O   1 
ATOM   5978 C  CB  . ILE B  1 343 ? -71.113 32.781  -18.754 1.00 24.84 ? 343  ILE B CB  1 
ATOM   5979 C  CG1 . ILE B  1 343 ? -70.669 31.887  -17.588 1.00 25.37 ? 343  ILE B CG1 1 
ATOM   5980 C  CG2 . ILE B  1 343 ? -69.926 33.411  -19.459 1.00 27.91 ? 343  ILE B CG2 1 
ATOM   5981 C  CD1 . ILE B  1 343 ? -70.051 32.635  -16.408 1.00 25.77 ? 343  ILE B CD1 1 
ATOM   5982 N  N   . GLY B  1 344 ? -73.227 34.786  -20.263 1.00 33.14 ? 344  GLY B N   1 
ATOM   5983 C  CA  . GLY B  1 344 ? -73.485 35.796  -21.305 1.00 33.34 ? 344  GLY B CA  1 
ATOM   5984 C  C   . GLY B  1 344 ? -72.608 35.539  -22.509 1.00 35.50 ? 344  GLY B C   1 
ATOM   5985 O  O   . GLY B  1 344 ? -72.135 34.385  -22.668 1.00 37.27 ? 344  GLY B O   1 
ATOM   5986 N  N   . SER B  1 345 ? -72.406 36.557  -23.348 1.00 35.33 ? 345  SER B N   1 
ATOM   5987 C  CA  . SER B  1 345 ? -71.669 36.442  -24.634 1.00 35.96 ? 345  SER B CA  1 
ATOM   5988 C  C   . SER B  1 345 ? -70.168 36.665  -24.408 1.00 32.63 ? 345  SER B C   1 
ATOM   5989 O  O   . SER B  1 345 ? -69.395 36.308  -25.308 1.00 35.38 ? 345  SER B O   1 
ATOM   5990 C  CB  . SER B  1 345 ? -72.207 37.434  -25.616 1.00 39.84 ? 345  SER B CB  1 
ATOM   5991 O  OG  . SER B  1 345 ? -72.176 38.726  -25.025 1.00 43.38 ? 345  SER B OG  1 
ATOM   5992 N  N   . SER B  1 346 ? -69.808 37.289  -23.286 1.00 32.19 ? 346  SER B N   1 
ATOM   5993 C  CA  . SER B  1 346 ? -68.426 37.650  -22.891 1.00 37.64 ? 346  SER B CA  1 
ATOM   5994 C  C   . SER B  1 346 ? -68.163 37.290  -21.431 1.00 36.10 ? 346  SER B C   1 
ATOM   5995 O  O   . SER B  1 346 ? -68.994 37.596  -20.555 1.00 32.73 ? 346  SER B O   1 
ATOM   5996 C  CB  . SER B  1 346 ? -68.148 39.104  -23.111 1.00 43.64 ? 346  SER B CB  1 
ATOM   5997 O  OG  . SER B  1 346 ? -67.801 39.319  -24.469 1.00 54.70 ? 346  SER B OG  1 
ATOM   5998 N  N   . ALA B  1 347 ? -66.980 36.736  -21.175 1.00 31.33 ? 347  ALA B N   1 
ATOM   5999 C  CA  . ALA B  1 347 ? -66.582 36.245  -19.842 1.00 30.86 ? 347  ALA B CA  1 
ATOM   6000 C  C   . ALA B  1 347 ? -65.292 36.941  -19.404 1.00 27.80 ? 347  ALA B C   1 
ATOM   6001 O  O   . ALA B  1 347 ? -64.449 37.222  -20.255 1.00 31.52 ? 347  ALA B O   1 
ATOM   6002 C  CB  . ALA B  1 347 ? -66.411 34.745  -19.926 1.00 31.49 ? 347  ALA B CB  1 
ATOM   6003 N  N   . THR B  1 348 ? -65.147 37.207  -18.114 1.00 26.19 ? 348  THR B N   1 
ATOM   6004 C  CA  . THR B  1 348 ? -63.829 37.456  -17.492 1.00 27.89 ? 348  THR B CA  1 
ATOM   6005 C  C   . THR B  1 348 ? -63.261 36.117  -17.027 1.00 25.59 ? 348  THR B C   1 
ATOM   6006 O  O   . THR B  1 348 ? -63.954 35.391  -16.277 1.00 21.66 ? 348  THR B O   1 
ATOM   6007 C  CB  . THR B  1 348 ? -63.927 38.436  -16.329 1.00 29.26 ? 348  THR B CB  1 
ATOM   6008 O  OG1 . THR B  1 348 ? -64.427 39.621  -16.943 1.00 34.32 ? 348  THR B OG1 1 
ATOM   6009 C  CG2 . THR B  1 348 ? -62.595 38.689  -15.661 1.00 31.33 ? 348  THR B CG2 1 
ATOM   6010 N  N   . VAL B  1 349 ? -62.040 35.823  -17.455 1.00 21.95 ? 349  VAL B N   1 
ATOM   6011 C  CA  . VAL B  1 349 ? -61.334 34.556  -17.122 1.00 22.30 ? 349  VAL B CA  1 
ATOM   6012 C  C   . VAL B  1 349 ? -60.094 34.965  -16.351 1.00 23.46 ? 349  VAL B C   1 
ATOM   6013 O  O   . VAL B  1 349 ? -59.242 35.710  -16.943 1.00 22.28 ? 349  VAL B O   1 
ATOM   6014 C  CB  . VAL B  1 349 ? -60.964 33.775  -18.381 1.00 24.15 ? 349  VAL B CB  1 
ATOM   6015 C  CG1 . VAL B  1 349 ? -60.117 32.556  -18.058 1.00 25.03 ? 349  VAL B CG1 1 
ATOM   6016 C  CG2 . VAL B  1 349 ? -62.195 33.382  -19.161 1.00 24.03 ? 349  VAL B CG2 1 
ATOM   6017 N  N   . LYS B  1 350 ? -60.058 34.609  -15.074 1.00 20.63 ? 350  LYS B N   1 
ATOM   6018 C  CA  . LYS B  1 350 ? -58.895 34.813  -14.192 1.00 20.20 ? 350  LYS B CA  1 
ATOM   6019 C  C   . LYS B  1 350 ? -58.160 33.474  -14.031 1.00 21.37 ? 350  LYS B C   1 
ATOM   6020 O  O   . LYS B  1 350 ? -58.765 32.554  -13.484 1.00 18.12 ? 350  LYS B O   1 
ATOM   6021 C  CB  . LYS B  1 350 ? -59.340 35.342  -12.839 1.00 24.17 ? 350  LYS B CB  1 
ATOM   6022 C  CG  . LYS B  1 350 ? -58.179 35.793  -11.986 1.00 27.62 ? 350  LYS B CG  1 
ATOM   6023 C  CD  . LYS B  1 350 ? -58.559 36.460  -10.699 1.00 32.96 ? 350  LYS B CD  1 
ATOM   6024 C  CE  . LYS B  1 350 ? -57.406 37.330  -10.234 1.00 36.99 ? 350  LYS B CE  1 
ATOM   6025 N  NZ  . LYS B  1 350 ? -57.619 37.884  -8.880  1.00 42.75 ? 350  LYS B NZ  1 
ATOM   6026 N  N   . VAL B  1 351 ? -56.889 33.409  -14.430 1.00 19.31 ? 351  VAL B N   1 
ATOM   6027 C  CA  . VAL B  1 351 ? -56.012 32.209  -14.270 1.00 18.95 ? 351  VAL B CA  1 
ATOM   6028 C  C   . VAL B  1 351 ? -55.030 32.511  -13.146 1.00 18.11 ? 351  VAL B C   1 
ATOM   6029 O  O   . VAL B  1 351 ? -54.369 33.583  -13.199 1.00 17.97 ? 351  VAL B O   1 
ATOM   6030 C  CB  . VAL B  1 351 ? -55.285 31.863  -15.572 1.00 19.36 ? 351  VAL B CB  1 
ATOM   6031 C  CG1 . VAL B  1 351 ? -54.287 30.731  -15.382 1.00 18.78 ? 351  VAL B CG1 1 
ATOM   6032 C  CG2 . VAL B  1 351 ? -56.265 31.593  -16.708 1.00 19.60 ? 351  VAL B CG2 1 
ATOM   6033 N  N   . GLU B  1 352 ? -54.998 31.671  -12.110 1.00 15.71 ? 352  GLU B N   1 
ATOM   6034 C  CA  . GLU B  1 352 ? -54.106 31.813  -10.943 1.00 14.94 ? 352  GLU B CA  1 
ATOM   6035 C  C   . GLU B  1 352 ? -53.312 30.514  -10.774 1.00 16.13 ? 352  GLU B C   1 
ATOM   6036 O  O   . GLU B  1 352 ? -53.719 29.498  -11.347 1.00 15.02 ? 352  GLU B O   1 
ATOM   6037 C  CB  . GLU B  1 352 ? -54.891 32.108  -9.687  1.00 16.22 ? 352  GLU B CB  1 
ATOM   6038 C  CG  . GLU B  1 352 ? -55.609 33.443  -9.741  1.00 16.66 ? 352  GLU B CG  1 
ATOM   6039 C  CD  . GLU B  1 352 ? -56.614 33.661  -8.628  1.00 17.49 ? 352  GLU B CD  1 
ATOM   6040 O  OE1 . GLU B  1 352 ? -56.205 33.911  -7.475  1.00 18.97 ? 352  GLU B OE1 1 
ATOM   6041 O  OE2 . GLU B  1 352 ? -57.804 33.501  -8.911  1.00 18.83 ? 352  GLU B OE2 1 
ATOM   6042 N  N   . LYS B  1 353 ? -52.202 30.579  -10.065 1.00 15.63 ? 353  LYS B N   1 
ATOM   6043 C  CA  . LYS B  1 353 ? -51.355 29.398  -9.818  1.00 17.64 ? 353  LYS B CA  1 
ATOM   6044 C  C   . LYS B  1 353 ? -50.873 29.450  -8.383  1.00 16.73 ? 353  LYS B C   1 
ATOM   6045 O  O   . LYS B  1 353 ? -50.803 30.528  -7.793  1.00 17.24 ? 353  LYS B O   1 
ATOM   6046 C  CB  . LYS B  1 353 ? -50.213 29.336  -10.833 1.00 18.11 ? 353  LYS B CB  1 
ATOM   6047 C  CG  . LYS B  1 353 ? -49.187 30.447  -10.704 1.00 19.88 ? 353  LYS B CG  1 
ATOM   6048 C  CD  . LYS B  1 353 ? -48.024 30.302  -11.665 1.00 21.26 ? 353  LYS B CD  1 
ATOM   6049 C  CE  . LYS B  1 353 ? -46.985 31.375  -11.434 1.00 24.36 ? 353  LYS B CE  1 
ATOM   6050 N  NZ  . LYS B  1 353 ? -45.917 31.319  -12.456 1.00 25.34 ? 353  LYS B NZ  1 
ATOM   6051 N  N   . VAL B  1 354 ? -50.526 28.289  -7.843  1.00 15.57 ? 354  VAL B N   1 
ATOM   6052 C  CA  . VAL B  1 354 ? -49.761 28.204  -6.584  1.00 15.86 ? 354  VAL B CA  1 
ATOM   6053 C  C   . VAL B  1 354 ? -48.545 27.340  -6.902  1.00 15.71 ? 354  VAL B C   1 
ATOM   6054 O  O   . VAL B  1 354 ? -48.702 26.236  -7.528  1.00 15.66 ? 354  VAL B O   1 
ATOM   6055 C  CB  . VAL B  1 354 ? -50.580 27.684  -5.409  1.00 16.49 ? 354  VAL B CB  1 
ATOM   6056 C  CG1 . VAL B  1 354 ? -51.188 26.313  -5.689  1.00 16.64 ? 354  VAL B CG1 1 
ATOM   6057 C  CG2 . VAL B  1 354 ? -49.748 27.686  -4.147  1.00 17.42 ? 354  VAL B CG2 1 
ATOM   6058 N  N   . ASP B  1 355 ? -47.373 27.848  -6.537  1.00 15.56 ? 355  ASP B N   1 
ATOM   6059 C  CA  . ASP B  1 355 ? -46.099 27.185  -6.874  1.00 16.31 ? 355  ASP B CA  1 
ATOM   6060 C  C   . ASP B  1 355 ? -45.627 26.345  -5.693  1.00 15.60 ? 355  ASP B C   1 
ATOM   6061 O  O   . ASP B  1 355 ? -45.863 26.710  -4.538  1.00 15.94 ? 355  ASP B O   1 
ATOM   6062 C  CB  . ASP B  1 355 ? -45.053 28.212  -7.325  1.00 19.47 ? 355  ASP B CB  1 
ATOM   6063 C  CG  . ASP B  1 355 ? -45.387 28.873  -8.658  1.00 22.80 ? 355  ASP B CG  1 
ATOM   6064 O  OD1 . ASP B  1 355 ? -46.028 28.219  -9.496  1.00 20.96 ? 355  ASP B OD1 1 
ATOM   6065 O  OD2 . ASP B  1 355 ? -45.000 30.072  -8.853  1.00 25.73 ? 355  ASP B OD2 1 
ATOM   6066 N  N   . TRP B  1 356 ? -44.889 25.274  -5.987  1.00 15.79 ? 356  TRP B N   1 
ATOM   6067 C  CA  . TRP B  1 356 ? -44.410 24.316  -4.978  1.00 15.61 ? 356  TRP B CA  1 
ATOM   6068 C  C   . TRP B  1 356 ? -42.909 24.181  -5.132  1.00 15.22 ? 356  TRP B C   1 
ATOM   6069 O  O   . TRP B  1 356 ? -42.461 24.024  -6.255  1.00 15.21 ? 356  TRP B O   1 
ATOM   6070 C  CB  . TRP B  1 356 ? -45.082 22.955  -5.200  1.00 17.04 ? 356  TRP B CB  1 
ATOM   6071 C  CG  . TRP B  1 356 ? -44.644 21.858  -4.283  1.00 16.82 ? 356  TRP B CG  1 
ATOM   6072 C  CD1 . TRP B  1 356 ? -45.232 21.497  -3.108  1.00 17.91 ? 356  TRP B CD1 1 
ATOM   6073 C  CD2 . TRP B  1 356 ? -43.569 20.923  -4.484  1.00 18.35 ? 356  TRP B CD2 1 
ATOM   6074 N  NE1 . TRP B  1 356 ? -44.612 20.401  -2.574  1.00 16.96 ? 356  TRP B NE1 1 
ATOM   6075 C  CE2 . TRP B  1 356 ? -43.575 20.043  -3.378  1.00 17.60 ? 356  TRP B CE2 1 
ATOM   6076 C  CE3 . TRP B  1 356 ? -42.595 20.757  -5.473  1.00 19.01 ? 356  TRP B CE3 1 
ATOM   6077 C  CZ2 . TRP B  1 356 ? -42.673 18.979  -3.271  1.00 17.95 ? 356  TRP B CZ2 1 
ATOM   6078 C  CZ3 . TRP B  1 356 ? -41.696 19.714  -5.361  1.00 19.23 ? 356  TRP B CZ3 1 
ATOM   6079 C  CH2 . TRP B  1 356 ? -41.714 18.872  -4.254  1.00 18.18 ? 356  TRP B CH2 1 
ATOM   6080 N  N   A ASN B  1 357 ? -42.188 24.208  -4.023  0.70 16.89 ? 357  ASN B N   1 
ATOM   6081 N  N   B ASN B  1 357 ? -42.181 24.310  -4.027  0.30 16.46 ? 357  ASN B N   1 
ATOM   6082 C  CA  A ASN B  1 357 ? -40.711 24.017  -3.987  0.70 18.15 ? 357  ASN B CA  1 
ATOM   6083 C  CA  B ASN B  1 357 ? -40.717 24.058  -3.948  0.30 17.36 ? 357  ASN B CA  1 
ATOM   6084 C  C   A ASN B  1 357 ? -40.353 22.838  -3.070  0.70 18.82 ? 357  ASN B C   1 
ATOM   6085 C  C   B ASN B  1 357 ? -40.404 23.345  -2.628  0.30 17.96 ? 357  ASN B C   1 
ATOM   6086 O  O   A ASN B  1 357 ? -39.272 22.245  -3.232  0.70 18.25 ? 357  ASN B O   1 
ATOM   6087 O  O   B ASN B  1 357 ? -39.414 23.729  -1.980  0.30 19.02 ? 357  ASN B O   1 
ATOM   6088 C  CB  A ASN B  1 357 ? -40.041 25.338  -3.612  0.70 20.95 ? 357  ASN B CB  1 
ATOM   6089 C  CB  B ASN B  1 357 ? -39.912 25.351  -4.084  0.30 18.58 ? 357  ASN B CB  1 
ATOM   6090 C  CG  A ASN B  1 357 ? -40.177 26.333  -4.750  0.70 23.31 ? 357  ASN B CG  1 
ATOM   6091 C  CG  B ASN B  1 357 ? -38.423 25.135  -3.930  0.30 18.90 ? 357  ASN B CG  1 
ATOM   6092 O  OD1 A ASN B  1 357 ? -39.541 26.172  -5.794  0.70 26.20 ? 357  ASN B OD1 1 
ATOM   6093 O  OD1 B ASN B  1 357 ? -37.879 25.336  -2.848  0.30 20.76 ? 357  ASN B OD1 1 
ATOM   6094 N  ND2 A ASN B  1 357 ? -41.061 27.313  -4.596  0.70 24.09 ? 357  ASN B ND2 1 
ATOM   6095 N  ND2 B ASN B  1 357 ? -37.759 24.733  -4.998  0.30 19.30 ? 357  ASN B ND2 1 
ATOM   6096 N  N   . GLY B  1 358 ? -41.271 22.415  -2.215  1.00 17.63 ? 358  GLY B N   1 
ATOM   6097 C  CA  . GLY B  1 358 ? -40.969 21.408  -1.196  1.00 16.62 ? 358  GLY B CA  1 
ATOM   6098 C  C   . GLY B  1 358 ? -42.156 21.232  -0.289  1.00 16.54 ? 358  GLY B C   1 
ATOM   6099 O  O   . GLY B  1 358 ? -42.890 22.216  -0.072  1.00 16.36 ? 358  GLY B O   1 
ATOM   6100 N  N   . LYS B  1 359 ? -42.324 20.016  0.230   1.00 15.46 ? 359  LYS B N   1 
ATOM   6101 C  CA  . LYS B  1 359 ? -43.351 19.640  1.223   1.00 16.46 ? 359  LYS B CA  1 
ATOM   6102 C  C   . LYS B  1 359 ? -43.351 20.601  2.436   1.00 16.79 ? 359  LYS B C   1 
ATOM   6103 O  O   . LYS B  1 359 ? -44.424 20.938  2.965   1.00 15.58 ? 359  LYS B O   1 
ATOM   6104 C  CB  . LYS B  1 359 ? -42.985 18.221  1.659   1.00 17.73 ? 359  LYS B CB  1 
ATOM   6105 C  CG  . LYS B  1 359 ? -43.960 17.561  2.606   1.00 18.25 ? 359  LYS B CG  1 
ATOM   6106 C  CD  . LYS B  1 359 ? -43.605 16.122  2.908   1.00 16.24 ? 359  LYS B CD  1 
ATOM   6107 C  CE  . LYS B  1 359 ? -42.502 15.939  3.933   1.00 14.31 ? 359  LYS B CE  1 
ATOM   6108 N  NZ  . LYS B  1 359 ? -42.871 16.445  5.274   1.00 14.83 ? 359  LYS B NZ  1 
ATOM   6109 N  N   . ASP B  1 360 ? -42.163 20.983  2.909   1.00 16.76 ? 360  ASP B N   1 
ATOM   6110 C  CA  . ASP B  1 360 ? -41.997 21.684  4.210   1.00 17.88 ? 360  ASP B CA  1 
ATOM   6111 C  C   . ASP B  1 360 ? -41.692 23.177  3.974   1.00 16.83 ? 360  ASP B C   1 
ATOM   6112 O  O   . ASP B  1 360 ? -41.309 23.862  4.918   1.00 20.70 ? 360  ASP B O   1 
ATOM   6113 C  CB  . ASP B  1 360 ? -40.945 20.950  5.037   1.00 19.11 ? 360  ASP B CB  1 
ATOM   6114 C  CG  . ASP B  1 360 ? -41.371 19.565  5.480   1.00 19.14 ? 360  ASP B CG  1 
ATOM   6115 O  OD1 . ASP B  1 360 ? -42.576 19.218  5.318   1.00 19.03 ? 360  ASP B OD1 1 
ATOM   6116 O  OD2 . ASP B  1 360 ? -40.507 18.836  6.013   1.00 21.64 ? 360  ASP B OD2 1 
ATOM   6117 N  N   . THR B  1 361 ? -41.879 23.671  2.767   1.00 16.95 ? 361  THR B N   1 
ATOM   6118 C  CA  . THR B  1 361 ? -41.614 25.088  2.398   1.00 17.25 ? 361  THR B CA  1 
ATOM   6119 C  C   . THR B  1 361 ? -42.879 25.927  2.598   1.00 17.01 ? 361  THR B C   1 
ATOM   6120 O  O   . THR B  1 361 ? -43.910 25.689  1.954   1.00 16.38 ? 361  THR B O   1 
ATOM   6121 C  CB  . THR B  1 361 ? -41.094 25.188  0.963   1.00 18.57 ? 361  THR B CB  1 
ATOM   6122 O  OG1 . THR B  1 361 ? -39.933 24.356  0.883   1.00 18.40 ? 361  THR B OG1 1 
ATOM   6123 C  CG2 . THR B  1 361 ? -40.730 26.603  0.577   1.00 18.75 ? 361  THR B CG2 1 
ATOM   6124 N  N   . PRO B  1 362 ? -42.872 26.905  3.536   1.00 18.84 ? 362  PRO B N   1 
ATOM   6125 C  CA  . PRO B  1 362 ? -44.035 27.766  3.743   1.00 19.32 ? 362  PRO B CA  1 
ATOM   6126 C  C   . PRO B  1 362 ? -44.374 28.543  2.470   1.00 19.38 ? 362  PRO B C   1 
ATOM   6127 O  O   . PRO B  1 362 ? -43.478 28.975  1.764   1.00 18.71 ? 362  PRO B O   1 
ATOM   6128 C  CB  . PRO B  1 362 ? -43.645 28.662  4.937   1.00 20.41 ? 362  PRO B CB  1 
ATOM   6129 C  CG  . PRO B  1 362 ? -42.548 27.871  5.648   1.00 21.25 ? 362  PRO B CG  1 
ATOM   6130 C  CD  . PRO B  1 362 ? -41.808 27.174  4.527   1.00 21.57 ? 362  PRO B CD  1 
ATOM   6131 N  N   . VAL B  1 363 ? -45.673 28.644  2.176   1.00 18.45 ? 363  VAL B N   1 
ATOM   6132 C  CA  . VAL B  1 363 ? -46.213 29.429  1.047   1.00 20.29 ? 363  VAL B CA  1 
ATOM   6133 C  C   . VAL B  1 363 ? -47.247 30.386  1.646   1.00 21.68 ? 363  VAL B C   1 
ATOM   6134 O  O   . VAL B  1 363 ? -48.129 29.921  2.388   1.00 20.45 ? 363  VAL B O   1 
ATOM   6135 C  CB  . VAL B  1 363 ? -46.801 28.510  -0.035  1.00 19.02 ? 363  VAL B CB  1 
ATOM   6136 C  CG1 . VAL B  1 363 ? -47.474 29.284  -1.154  1.00 18.12 ? 363  VAL B CG1 1 
ATOM   6137 C  CG2 . VAL B  1 363 ? -45.724 27.571  -0.562  1.00 20.37 ? 363  VAL B CG2 1 
ATOM   6138 N  N   A ASN B  1 364 ? -47.124 31.674  1.305   0.70 23.41 ? 364  ASN B N   1 
ATOM   6139 N  N   B ASN B  1 364 ? -47.145 31.683  1.353   0.30 22.30 ? 364  ASN B N   1 
ATOM   6140 C  CA  A ASN B  1 364 ? -47.902 32.788  1.917   0.70 25.20 ? 364  ASN B CA  1 
ATOM   6141 C  CA  B ASN B  1 364 ? -48.029 32.708  1.972   0.30 23.09 ? 364  ASN B CA  1 
ATOM   6142 C  C   A ASN B  1 364 ? -49.086 33.196  1.025   0.70 24.59 ? 364  ASN B C   1 
ATOM   6143 C  C   B ASN B  1 364 ? -48.952 33.333  0.919   0.30 23.19 ? 364  ASN B C   1 
ATOM   6144 O  O   A ASN B  1 364 ? -49.848 34.035  1.457   0.70 24.79 ? 364  ASN B O   1 
ATOM   6145 O  O   B ASN B  1 364 ? -49.378 34.475  1.127   0.30 23.16 ? 364  ASN B O   1 
ATOM   6146 C  CB  A ASN B  1 364 ? -47.008 33.990  2.254   0.70 27.65 ? 364  ASN B CB  1 
ATOM   6147 C  CB  B ASN B  1 364 ? -47.217 33.739  2.756   0.30 23.91 ? 364  ASN B CB  1 
ATOM   6148 C  CG  A ASN B  1 364 ? -46.195 34.507  1.088   0.70 28.61 ? 364  ASN B CG  1 
ATOM   6149 C  CG  B ASN B  1 364 ? -47.041 33.321  4.198   0.30 23.84 ? 364  ASN B CG  1 
ATOM   6150 O  OD1 A ASN B  1 364 ? -46.584 34.370  -0.064  0.70 35.12 ? 364  ASN B OD1 1 
ATOM   6151 O  OD1 B ASN B  1 364 ? -46.320 32.369  4.491   0.30 23.06 ? 364  ASN B OD1 1 
ATOM   6152 N  ND2 A ASN B  1 364 ? -45.047 35.099  1.373   0.70 34.42 ? 364  ASN B ND2 1 
ATOM   6153 N  ND2 B ASN B  1 364 ? -47.721 34.010  5.102   0.30 25.93 ? 364  ASN B ND2 1 
ATOM   6154 N  N   . GLY B  1 365 ? -49.259 32.611  -0.160  1.00 22.98 ? 365  GLY B N   1 
ATOM   6155 C  CA  . GLY B  1 365 ? -50.346 32.994  -1.070  1.00 23.08 ? 365  GLY B CA  1 
ATOM   6156 C  C   . GLY B  1 365 ? -50.117 32.495  -2.477  1.00 22.55 ? 365  GLY B C   1 
ATOM   6157 O  O   . GLY B  1 365 ? -49.203 31.689  -2.683  1.00 21.84 ? 365  GLY B O   1 
ATOM   6158 N  N   . THR B  1 366 ? -50.925 32.980  -3.409  1.00 21.47 ? 366  THR B N   1 
ATOM   6159 C  CA  . THR B  1 366 ? -51.006 32.515  -4.809  1.00 21.11 ? 366  THR B CA  1 
ATOM   6160 C  C   . THR B  1 366 ? -50.619 33.634  -5.765  1.00 21.52 ? 366  THR B C   1 
ATOM   6161 O  O   . THR B  1 366 ? -50.403 34.757  -5.321  1.00 21.81 ? 366  THR B O   1 
ATOM   6162 C  CB  . THR B  1 366 ? -52.408 31.955  -5.062  1.00 23.35 ? 366  THR B CB  1 
ATOM   6163 O  OG1 . THR B  1 366 ? -53.335 33.037  -4.964  1.00 23.13 ? 366  THR B OG1 1 
ATOM   6164 C  CG2 . THR B  1 366 ? -52.771 30.876  -4.069  1.00 22.84 ? 366  THR B CG2 1 
ATOM   6165 N  N   . ASN B  1 367 ? -50.489 33.301  -7.036  1.00 20.42 ? 367  ASN B N   1 
ATOM   6166 C  CA  . ASN B  1 367 ? -50.013 34.228  -8.089  1.00 25.64 ? 367  ASN B CA  1 
ATOM   6167 C  C   . ASN B  1 367 ? -51.097 34.330  -9.140  1.00 24.98 ? 367  ASN B C   1 
ATOM   6168 O  O   . ASN B  1 367 ? -51.709 33.291  -9.465  1.00 24.42 ? 367  ASN B O   1 
ATOM   6169 C  CB  . ASN B  1 367 ? -48.735 33.757  -8.790  1.00 29.22 ? 367  ASN B CB  1 
ATOM   6170 C  CG  . ASN B  1 367 ? -47.589 33.586  -7.828  1.00 36.68 ? 367  ASN B CG  1 
ATOM   6171 O  OD1 . ASN B  1 367 ? -46.857 32.599  -7.909  1.00 49.63 ? 367  ASN B OD1 1 
ATOM   6172 N  ND2 . ASN B  1 367 ? -47.464 34.508  -6.888  1.00 38.18 ? 367  ASN B ND2 1 
ATOM   6173 N  N   . THR B  1 368 ? -51.328 35.532  -9.647  1.00 21.24 ? 368  THR B N   1 
ATOM   6174 C  CA  . THR B  1 368 ? -52.228 35.736  -10.792 1.00 20.53 ? 368  THR B CA  1 
ATOM   6175 C  C   . THR B  1 368 ? -51.400 35.600  -12.057 1.00 22.08 ? 368  THR B C   1 
ATOM   6176 O  O   . THR B  1 368 ? -50.429 36.354  -12.195 1.00 25.10 ? 368  THR B O   1 
ATOM   6177 C  CB  . THR B  1 368 ? -52.971 37.066  -10.655 1.00 20.31 ? 368  THR B CB  1 
ATOM   6178 O  OG1 . THR B  1 368 ? -53.670 37.002  -9.422  1.00 21.15 ? 368  THR B OG1 1 
ATOM   6179 C  CG2 . THR B  1 368 ? -53.933 37.311  -11.793 1.00 21.70 ? 368  THR B CG2 1 
ATOM   6180 N  N   . VAL B  1 369 ? -51.759 34.679  -12.937 1.00 20.84 ? 369  VAL B N   1 
ATOM   6181 C  CA  . VAL B  1 369 ? -51.134 34.519  -14.280 1.00 20.84 ? 369  VAL B CA  1 
ATOM   6182 C  C   . VAL B  1 369 ? -51.687 35.583  -15.236 1.00 22.87 ? 369  VAL B C   1 
ATOM   6183 O  O   . VAL B  1 369 ? -50.886 36.350  -15.784 1.00 25.89 ? 369  VAL B O   1 
ATOM   6184 C  CB  . VAL B  1 369 ? -51.332 33.101  -14.833 1.00 20.89 ? 369  VAL B CB  1 
ATOM   6185 C  CG1 . VAL B  1 369 ? -50.632 32.962  -16.173 1.00 21.74 ? 369  VAL B CG1 1 
ATOM   6186 C  CG2 . VAL B  1 369 ? -50.867 32.038  -13.855 1.00 20.25 ? 369  VAL B CG2 1 
ATOM   6187 N  N   . PHE B  1 370 ? -53.000 35.677  -15.404 1.00 21.63 ? 370  PHE B N   1 
ATOM   6188 C  CA  . PHE B  1 370 ? -53.628 36.778  -16.175 1.00 22.83 ? 370  PHE B CA  1 
ATOM   6189 C  C   . PHE B  1 370 ? -55.118 36.814  -15.869 1.00 27.50 ? 370  PHE B C   1 
ATOM   6190 O  O   . PHE B  1 370 ? -55.652 35.832  -15.324 1.00 21.49 ? 370  PHE B O   1 
ATOM   6191 C  CB  . PHE B  1 370 ? -53.433 36.596  -17.688 1.00 24.05 ? 370  PHE B CB  1 
ATOM   6192 C  CG  . PHE B  1 370 ? -53.995 35.352  -18.333 1.00 22.64 ? 370  PHE B CG  1 
ATOM   6193 C  CD1 . PHE B  1 370 ? -55.359 35.187  -18.537 1.00 25.74 ? 370  PHE B CD1 1 
ATOM   6194 C  CD2 . PHE B  1 370 ? -53.166 34.325  -18.746 1.00 25.15 ? 370  PHE B CD2 1 
ATOM   6195 C  CE1 . PHE B  1 370 ? -55.867 34.038  -19.131 1.00 24.93 ? 370  PHE B CE1 1 
ATOM   6196 C  CE2 . PHE B  1 370 ? -53.673 33.177  -19.333 1.00 25.33 ? 370  PHE B CE2 1 
ATOM   6197 C  CZ  . PHE B  1 370 ? -55.028 33.033  -19.528 1.00 25.33 ? 370  PHE B CZ  1 
ATOM   6198 N  N   A SER B  1 371 ? -55.753 37.949  -16.170 0.80 27.06 ? 371  SER B N   1 
ATOM   6199 N  N   B SER B  1 371 ? -55.777 37.914  -16.253 0.20 25.46 ? 371  SER B N   1 
ATOM   6200 C  CA  A SER B  1 371 ? -57.215 38.053  -16.388 0.80 29.05 ? 371  SER B CA  1 
ATOM   6201 C  CA  B SER B  1 371 ? -57.256 38.038  -16.355 0.20 26.05 ? 371  SER B CA  1 
ATOM   6202 C  C   A SER B  1 371 ? -57.411 38.586  -17.804 0.80 30.31 ? 371  SER B C   1 
ATOM   6203 C  C   B SER B  1 371 ? -57.617 38.707  -17.684 0.20 28.62 ? 371  SER B C   1 
ATOM   6204 O  O   A SER B  1 371 ? -56.663 39.489  -18.203 0.80 27.80 ? 371  SER B O   1 
ATOM   6205 O  O   B SER B  1 371 ? -57.288 39.897  -17.844 0.20 28.25 ? 371  SER B O   1 
ATOM   6206 C  CB  A SER B  1 371 ? -57.881 38.904  -15.368 0.80 31.69 ? 371  SER B CB  1 
ATOM   6207 C  CB  B SER B  1 371 ? -57.842 38.800  -15.207 0.20 24.91 ? 371  SER B CB  1 
ATOM   6208 O  OG  A SER B  1 371 ? -57.391 38.600  -14.062 0.80 35.75 ? 371  SER B OG  1 
ATOM   6209 O  OG  B SER B  1 371 ? -59.251 38.919  -15.356 0.20 21.73 ? 371  SER B OG  1 
ATOM   6210 N  N   . LYS B  1 372 ? -58.309 37.980  -18.566 1.00 31.50 ? 372  LYS B N   1 
ATOM   6211 C  CA  . LYS B  1 372 ? -58.617 38.421  -19.948 1.00 34.43 ? 372  LYS B CA  1 
ATOM   6212 C  C   . LYS B  1 372 ? -60.132 38.343  -20.129 1.00 36.88 ? 372  LYS B C   1 
ATOM   6213 O  O   . LYS B  1 372 ? -60.757 37.516  -19.421 1.00 29.88 ? 372  LYS B O   1 
ATOM   6214 C  CB  . LYS B  1 372 ? -57.922 37.526  -20.981 1.00 40.42 ? 372  LYS B CB  1 
ATOM   6215 C  CG  . LYS B  1 372 ? -56.453 37.817  -21.242 1.00 46.26 ? 372  LYS B CG  1 
ATOM   6216 C  CD  . LYS B  1 372 ? -55.767 36.711  -22.023 1.00 50.00 ? 372  LYS B CD  1 
ATOM   6217 C  CE  . LYS B  1 372 ? -54.257 36.855  -22.041 1.00 55.86 ? 372  LYS B CE  1 
ATOM   6218 N  NZ  . LYS B  1 372 ? -53.589 35.615  -22.517 1.00 57.28 ? 372  LYS B NZ  1 
ATOM   6219 N  N   . ARG B  1 373 ? -60.678 39.177  -21.020 1.00 33.75 ? 373  ARG B N   1 
ATOM   6220 C  CA  . ARG B  1 373 ? -62.017 38.991  -21.626 1.00 35.75 ? 373  ARG B CA  1 
ATOM   6221 C  C   . ARG B  1 373 ? -61.905 37.882  -22.656 1.00 32.05 ? 373  ARG B C   1 
ATOM   6222 O  O   . ARG B  1 373 ? -60.899 37.872  -23.406 1.00 32.99 ? 373  ARG B O   1 
ATOM   6223 C  CB  . ARG B  1 373 ? -62.495 40.211  -22.420 1.00 42.44 ? 373  ARG B CB  1 
ATOM   6224 C  CG  . ARG B  1 373 ? -62.718 41.498  -21.641 1.00 51.93 ? 373  ARG B CG  1 
ATOM   6225 C  CD  . ARG B  1 373 ? -63.291 42.524  -22.620 1.00 59.40 ? 373  ARG B CD  1 
ATOM   6226 N  NE  . ARG B  1 373 ? -63.634 43.828  -22.041 1.00 67.97 ? 373  ARG B NE  1 
ATOM   6227 C  CZ  . ARG B  1 373 ? -64.548 44.676  -22.534 1.00 69.57 ? 373  ARG B CZ  1 
ATOM   6228 N  NH1 . ARG B  1 373 ? -64.776 45.833  -21.929 1.00 69.75 ? 373  ARG B NH1 1 
ATOM   6229 N  NH2 . ARG B  1 373 ? -65.237 44.366  -23.622 1.00 71.14 ? 373  ARG B NH2 1 
ATOM   6230 N  N   . TYR B  1 374 ? -62.899 37.002  -22.726 1.00 30.46 ? 374  TYR B N   1 
ATOM   6231 C  CA  . TYR B  1 374 ? -63.074 36.065  -23.857 1.00 30.65 ? 374  TYR B CA  1 
ATOM   6232 C  C   . TYR B  1 374 ? -64.497 36.239  -24.384 1.00 33.23 ? 374  TYR B C   1 
ATOM   6233 O  O   . TYR B  1 374 ? -65.399 36.474  -23.590 1.00 32.54 ? 374  TYR B O   1 
ATOM   6234 C  CB  . TYR B  1 374 ? -62.832 34.615  -23.413 1.00 30.22 ? 374  TYR B CB  1 
ATOM   6235 C  CG  . TYR B  1 374 ? -61.396 34.267  -23.101 1.00 29.78 ? 374  TYR B CG  1 
ATOM   6236 C  CD1 . TYR B  1 374 ? -60.782 34.741  -21.947 1.00 30.19 ? 374  TYR B CD1 1 
ATOM   6237 C  CD2 . TYR B  1 374 ? -60.657 33.457  -23.947 1.00 29.50 ? 374  TYR B CD2 1 
ATOM   6238 C  CE1 . TYR B  1 374 ? -59.463 34.432  -21.654 1.00 29.30 ? 374  TYR B CE1 1 
ATOM   6239 C  CE2 . TYR B  1 374 ? -59.335 33.143  -23.667 1.00 27.10 ? 374  TYR B CE2 1 
ATOM   6240 C  CZ  . TYR B  1 374 ? -58.744 33.619  -22.509 1.00 29.37 ? 374  TYR B CZ  1 
ATOM   6241 O  OH  . TYR B  1 374 ? -57.442 33.318  -22.216 1.00 28.85 ? 374  TYR B OH  1 
ATOM   6242 N  N   . THR B  1 375 ? -64.683 36.061  -25.683 1.00 35.62 ? 375  THR B N   1 
ATOM   6243 C  CA  . THR B  1 375 ? -66.021 35.979  -26.306 1.00 36.24 ? 375  THR B CA  1 
ATOM   6244 C  C   . THR B  1 375 ? -66.447 34.515  -26.339 1.00 34.90 ? 375  THR B C   1 
ATOM   6245 O  O   . THR B  1 375 ? -65.698 33.673  -26.859 1.00 37.00 ? 375  THR B O   1 
ATOM   6246 C  CB  . THR B  1 375 ? -66.018 36.584  -27.711 1.00 38.20 ? 375  THR B CB  1 
ATOM   6247 O  OG1 . THR B  1 375 ? -65.650 37.945  -27.506 1.00 41.08 ? 375  THR B OG1 1 
ATOM   6248 C  CG2 . THR B  1 375 ? -67.359 36.487  -28.403 1.00 40.29 ? 375  THR B CG2 1 
ATOM   6249 N  N   . VAL B  1 376 ? -67.633 34.229  -25.833 1.00 31.97 ? 376  VAL B N   1 
ATOM   6250 C  CA  . VAL B  1 376 ? -68.223 32.874  -25.927 1.00 32.41 ? 376  VAL B CA  1 
ATOM   6251 C  C   . VAL B  1 376 ? -68.646 32.660  -27.378 1.00 37.94 ? 376  VAL B C   1 
ATOM   6252 O  O   . VAL B  1 376 ? -69.391 33.512  -27.909 1.00 40.08 ? 376  VAL B O   1 
ATOM   6253 C  CB  . VAL B  1 376 ? -69.394 32.745  -24.946 1.00 32.05 ? 376  VAL B CB  1 
ATOM   6254 C  CG1 . VAL B  1 376 ? -70.071 31.392  -25.072 1.00 30.10 ? 376  VAL B CG1 1 
ATOM   6255 C  CG2 . VAL B  1 376 ? -68.935 33.044  -23.530 1.00 30.27 ? 376  VAL B CG2 1 
ATOM   6256 N  N   . SER B  1 377 ? -68.206 31.559  -27.973 1.00 39.05 ? 377  SER B N   1 
ATOM   6257 C  CA  . SER B  1 377 ? -68.449 31.198  -29.386 1.00 37.68 ? 377  SER B CA  1 
ATOM   6258 C  C   . SER B  1 377 ? -69.064 29.796  -29.440 1.00 39.14 ? 377  SER B C   1 
ATOM   6259 O  O   . SER B  1 377 ? -68.371 28.832  -29.056 1.00 34.92 ? 377  SER B O   1 
ATOM   6260 C  CB  . SER B  1 377 ? -67.147 31.303  -30.130 1.00 43.91 ? 377  SER B CB  1 
ATOM   6261 O  OG  . SER B  1 377 ? -67.347 31.260  -31.530 1.00 49.48 ? 377  SER B OG  1 
ATOM   6262 N  N   . ASN B  1 378 ? -70.335 29.682  -29.842 1.00 35.66 ? 378  ASN B N   1 
ATOM   6263 C  CA  . ASN B  1 378 ? -71.095 28.407  -29.798 1.00 35.76 ? 378  ASN B CA  1 
ATOM   6264 C  C   . ASN B  1 378 ? -70.927 27.773  -28.401 1.00 29.98 ? 378  ASN B C   1 
ATOM   6265 O  O   . ASN B  1 378 ? -70.775 26.552  -28.314 1.00 33.75 ? 378  ASN B O   1 
ATOM   6266 C  CB  . ASN B  1 378 ? -70.659 27.449  -30.915 1.00 38.64 ? 378  ASN B CB  1 
ATOM   6267 C  CG  . ASN B  1 378 ? -71.074 27.896  -32.302 1.00 41.76 ? 378  ASN B CG  1 
ATOM   6268 O  OD1 . ASN B  1 378 ? -71.856 28.832  -32.445 1.00 40.27 ? 378  ASN B OD1 1 
ATOM   6269 N  ND2 . ASN B  1 378 ? -70.563 27.229  -33.329 1.00 42.17 ? 378  ASN B ND2 1 
ATOM   6270 N  N   . GLY B  1 379 ? -70.993 28.583  -27.356 1.00 30.45 ? 379  GLY B N   1 
ATOM   6271 C  CA  . GLY B  1 379 ? -70.955 28.146  -25.947 1.00 29.40 ? 379  GLY B CA  1 
ATOM   6272 C  C   . GLY B  1 379 ? -69.563 27.712  -25.496 1.00 26.59 ? 379  GLY B C   1 
ATOM   6273 O  O   . GLY B  1 379 ? -69.489 27.142  -24.399 1.00 24.85 ? 379  GLY B O   1 
ATOM   6274 N  N   . THR B  1 380 ? -68.506 28.019  -26.266 1.00 27.95 ? 380  THR B N   1 
ATOM   6275 C  CA  . THR B  1 380 ? -67.102 27.571  -26.011 1.00 27.90 ? 380  THR B CA  1 
ATOM   6276 C  C   . THR B  1 380 ? -66.169 28.756  -25.777 1.00 28.61 ? 380  THR B C   1 
ATOM   6277 O  O   . THR B  1 380 ? -66.234 29.739  -26.547 1.00 31.57 ? 380  THR B O   1 
ATOM   6278 C  CB  . THR B  1 380 ? -66.575 26.740  -27.185 1.00 29.96 ? 380  THR B CB  1 
ATOM   6279 O  OG1 . THR B  1 380 ? -67.335 25.533  -27.252 1.00 31.59 ? 380  THR B OG1 1 
ATOM   6280 C  CG2 . THR B  1 380 ? -65.111 26.387  -27.079 1.00 31.15 ? 380  THR B CG2 1 
ATOM   6281 N  N   . ILE B  1 381 ? -65.280 28.650  -24.787 1.00 27.67 ? 381  ILE B N   1 
ATOM   6282 C  CA  . ILE B  1 381 ? -64.044 29.478  -24.726 1.00 27.13 ? 381  ILE B CA  1 
ATOM   6283 C  C   . ILE B  1 381 ? -62.861 28.518  -24.604 1.00 28.48 ? 381  ILE B C   1 
ATOM   6284 O  O   . ILE B  1 381 ? -63.020 27.419  -23.980 1.00 26.84 ? 381  ILE B O   1 
ATOM   6285 C  CB  . ILE B  1 381 ? -64.067 30.566  -23.628 1.00 28.95 ? 381  ILE B CB  1 
ATOM   6286 C  CG1 . ILE B  1 381 ? -63.845 30.034  -22.216 1.00 30.26 ? 381  ILE B CG1 1 
ATOM   6287 C  CG2 . ILE B  1 381 ? -65.348 31.381  -23.684 1.00 32.02 ? 381  ILE B CG2 1 
ATOM   6288 C  CD1 . ILE B  1 381 ? -63.278 31.067  -21.283 1.00 32.57 ? 381  ILE B CD1 1 
ATOM   6289 N  N   . ASN B  1 382 ? -61.744 28.905  -25.214 1.00 25.74 ? 382  ASN B N   1 
ATOM   6290 C  CA  . ASN B  1 382 ? -60.490 28.116  -25.273 1.00 26.77 ? 382  ASN B CA  1 
ATOM   6291 C  C   . ASN B  1 382 ? -59.411 28.920  -24.562 1.00 26.35 ? 382  ASN B C   1 
ATOM   6292 O  O   . ASN B  1 382 ? -58.970 29.946  -25.091 1.00 28.25 ? 382  ASN B O   1 
ATOM   6293 C  CB  . ASN B  1 382 ? -60.129 27.738  -26.697 1.00 27.21 ? 382  ASN B CB  1 
ATOM   6294 C  CG  . ASN B  1 382 ? -61.260 27.002  -27.379 1.00 28.85 ? 382  ASN B CG  1 
ATOM   6295 O  OD1 . ASN B  1 382 ? -61.775 27.461  -28.395 1.00 34.79 ? 382  ASN B OD1 1 
ATOM   6296 N  ND2 . ASN B  1 382 ? -61.695 25.901  -26.804 1.00 30.81 ? 382  ASN B ND2 1 
ATOM   6297 N  N   . VAL B  1 383 ? -59.088 28.511  -23.347 1.00 23.62 ? 383  VAL B N   1 
ATOM   6298 C  CA  . VAL B  1 383 ? -58.113 29.200  -22.480 1.00 22.57 ? 383  VAL B CA  1 
ATOM   6299 C  C   . VAL B  1 383 ? -56.782 28.453  -22.619 1.00 24.95 ? 383  VAL B C   1 
ATOM   6300 O  O   . VAL B  1 383 ? -56.762 27.207  -22.547 1.00 23.61 ? 383  VAL B O   1 
ATOM   6301 C  CB  . VAL B  1 383 ? -58.565 29.253  -21.013 1.00 23.21 ? 383  VAL B CB  1 
ATOM   6302 C  CG1 . VAL B  1 383 ? -57.541 29.971  -20.170 1.00 23.46 ? 383  VAL B CG1 1 
ATOM   6303 C  CG2 . VAL B  1 383 ? -59.932 29.893  -20.829 1.00 23.80 ? 383  VAL B CG2 1 
ATOM   6304 N  N   . SER B  1 384 ? -55.708 29.199  -22.786 1.00 23.86 ? 384  SER B N   1 
ATOM   6305 C  CA  . SER B  1 384 ? -54.347 28.626  -22.861 1.00 24.99 ? 384  SER B CA  1 
ATOM   6306 C  C   . SER B  1 384 ? -53.517 29.185  -21.720 1.00 24.06 ? 384  SER B C   1 
ATOM   6307 O  O   . SER B  1 384 ? -53.378 30.432  -21.630 1.00 23.97 ? 384  SER B O   1 
ATOM   6308 C  CB  . SER B  1 384 ? -53.716 28.921  -24.174 1.00 26.56 ? 384  SER B CB  1 
ATOM   6309 O  OG  . SER B  1 384 ? -52.420 28.346  -24.199 1.00 29.47 ? 384  SER B OG  1 
ATOM   6310 N  N   . ILE B  1 385 ? -52.950 28.305  -20.896 1.00 23.10 ? 385  ILE B N   1 
ATOM   6311 C  CA  . ILE B  1 385 ? -52.123 28.713  -19.734 1.00 21.58 ? 385  ILE B CA  1 
ATOM   6312 C  C   . ILE B  1 385 ? -50.683 28.520  -20.166 1.00 22.13 ? 385  ILE B C   1 
ATOM   6313 O  O   . ILE B  1 385 ? -50.262 27.396  -20.421 1.00 23.06 ? 385  ILE B O   1 
ATOM   6314 C  CB  . ILE B  1 385 ? -52.459 27.902  -18.476 1.00 21.07 ? 385  ILE B CB  1 
ATOM   6315 C  CG1 . ILE B  1 385 ? -53.962 27.906  -18.180 1.00 22.36 ? 385  ILE B CG1 1 
ATOM   6316 C  CG2 . ILE B  1 385 ? -51.653 28.400  -17.298 1.00 20.50 ? 385  ILE B CG2 1 
ATOM   6317 C  CD1 . ILE B  1 385 ? -54.357 26.990  -17.052 1.00 21.45 ? 385  ILE B CD1 1 
ATOM   6318 N  N   . PRO B  1 386 ? -49.898 29.608  -20.320 1.00 23.22 ? 386  PRO B N   1 
ATOM   6319 C  CA  . PRO B  1 386 ? -48.528 29.454  -20.806 1.00 22.27 ? 386  PRO B CA  1 
ATOM   6320 C  C   . PRO B  1 386 ? -47.554 29.140  -19.667 1.00 20.60 ? 386  PRO B C   1 
ATOM   6321 O  O   . PRO B  1 386 ? -47.875 29.431  -18.534 1.00 21.51 ? 386  PRO B O   1 
ATOM   6322 C  CB  . PRO B  1 386 ? -48.313 30.859  -21.376 1.00 23.93 ? 386  PRO B CB  1 
ATOM   6323 C  CG  . PRO B  1 386 ? -48.967 31.755  -20.346 1.00 24.53 ? 386  PRO B CG  1 
ATOM   6324 C  CD  . PRO B  1 386 ? -50.264 31.024  -20.051 1.00 23.61 ? 386  PRO B CD  1 
ATOM   6325 N  N   . GLY B  1 387 ? -46.383 28.568  -19.977 1.00 20.88 ? 387  GLY B N   1 
ATOM   6326 C  CA  . GLY B  1 387 ? -45.292 28.452  -18.987 1.00 20.11 ? 387  GLY B CA  1 
ATOM   6327 C  C   . GLY B  1 387 ? -45.636 27.530  -17.819 1.00 18.42 ? 387  GLY B C   1 
ATOM   6328 O  O   . GLY B  1 387 ? -45.195 27.810  -16.661 1.00 17.96 ? 387  GLY B O   1 
ATOM   6329 N  N   . THR B  1 388 ? -46.400 26.469  -18.078 1.00 18.82 ? 388  THR B N   1 
ATOM   6330 C  CA  . THR B  1 388 ? -46.848 25.526  -17.003 1.00 18.43 ? 388  THR B CA  1 
ATOM   6331 C  C   . THR B  1 388 ? -45.747 24.530  -16.649 1.00 17.71 ? 388  THR B C   1 
ATOM   6332 O  O   . THR B  1 388 ? -44.810 24.325  -17.440 1.00 18.60 ? 388  THR B O   1 
ATOM   6333 C  CB  . THR B  1 388 ? -48.149 24.804  -17.364 1.00 16.73 ? 388  THR B CB  1 
ATOM   6334 O  OG1 . THR B  1 388 ? -47.957 24.148  -18.610 1.00 17.09 ? 388  THR B OG1 1 
ATOM   6335 C  CG2 . THR B  1 388 ? -49.326 25.747  -17.479 1.00 18.94 ? 388  THR B CG2 1 
ATOM   6336 N  N   . ASN B  1 389 ? -45.832 24.007  -15.432 1.00 17.98 ? 389  ASN B N   1 
ATOM   6337 C  CA  . ASN B  1 389 ? -44.901 22.977  -14.916 1.00 16.62 ? 389  ASN B CA  1 
ATOM   6338 C  C   . ASN B  1 389 ? -45.730 21.873  -14.254 1.00 15.27 ? 389  ASN B C   1 
ATOM   6339 O  O   . ASN B  1 389 ? -46.981 21.994  -14.212 1.00 13.65 ? 389  ASN B O   1 
ATOM   6340 C  CB  . ASN B  1 389 ? -43.893 23.592  -13.951 1.00 16.77 ? 389  ASN B CB  1 
ATOM   6341 C  CG  . ASN B  1 389 ? -44.528 24.139  -12.687 1.00 16.98 ? 389  ASN B CG  1 
ATOM   6342 O  OD1 . ASN B  1 389 ? -45.007 23.369  -11.855 1.00 16.74 ? 389  ASN B OD1 1 
ATOM   6343 N  ND2 . ASN B  1 389 ? -44.525 25.471  -12.521 1.00 15.93 ? 389  ASN B ND2 1 
ATOM   6344 N  N   . ASN B  1 390 ? -45.062 20.842  -13.726 1.00 15.05 ? 390  ASN B N   1 
ATOM   6345 C  CA  . ASN B  1 390 ? -45.740 19.618  -13.225 1.00 14.49 ? 390  ASN B CA  1 
ATOM   6346 C  C   . ASN B  1 390 ? -46.072 19.669  -11.722 1.00 15.42 ? 390  ASN B C   1 
ATOM   6347 O  O   . ASN B  1 390 ? -46.762 18.751  -11.226 1.00 15.96 ? 390  ASN B O   1 
ATOM   6348 C  CB  . ASN B  1 390 ? -44.828 18.432  -13.493 1.00 15.07 ? 390  ASN B CB  1 
ATOM   6349 C  CG  . ASN B  1 390 ? -44.564 18.226  -14.970 1.00 15.78 ? 390  ASN B CG  1 
ATOM   6350 O  OD1 . ASN B  1 390 ? -45.193 18.849  -15.810 1.00 17.69 ? 390  ASN B OD1 1 
ATOM   6351 N  ND2 . ASN B  1 390 ? -43.621 17.349  -15.283 1.00 14.90 ? 390  ASN B ND2 1 
ATOM   6352 N  N   . THR B  1 391 ? -45.597 20.662  -10.984 1.00 14.71 ? 391  THR B N   1 
ATOM   6353 C  CA  . THR B  1 391 ? -45.734 20.707  -9.506  1.00 14.51 ? 391  THR B CA  1 
ATOM   6354 C  C   . THR B  1 391 ? -46.734 21.789  -9.089  1.00 14.07 ? 391  THR B C   1 
ATOM   6355 O  O   . THR B  1 391 ? -47.257 21.679  -7.970  1.00 12.89 ? 391  THR B O   1 
ATOM   6356 C  CB  . THR B  1 391 ? -44.378 20.858  -8.807  1.00 15.54 ? 391  THR B CB  1 
ATOM   6357 O  OG1 . THR B  1 391 ? -43.707 22.048  -9.249  1.00 15.61 ? 391  THR B OG1 1 
ATOM   6358 C  CG2 . THR B  1 391 ? -43.491 19.659  -9.037  1.00 15.90 ? 391  THR B CG2 1 
ATOM   6359 N  N   . SER B  1 392 ? -46.893 22.861  -9.867  1.00 13.61 ? 392  SER B N   1 
ATOM   6360 C  CA  . SER B  1 392 ? -47.822 23.962  -9.527  1.00 13.05 ? 392  SER B CA  1 
ATOM   6361 C  C   . SER B  1 392 ? -49.259 23.436  -9.605  1.00 13.28 ? 392  SER B C   1 
ATOM   6362 O  O   . SER B  1 392 ? -49.537 22.473  -10.350 1.00 14.80 ? 392  SER B O   1 
ATOM   6363 C  CB  . SER B  1 392 ? -47.644 25.188  -10.445 1.00 13.87 ? 392  SER B CB  1 
ATOM   6364 O  OG  . SER B  1 392 ? -46.392 25.832  -10.250 1.00 14.21 ? 392  SER B OG  1 
ATOM   6365 N  N   . GLY B  1 393 ? -50.156 24.112  -8.910  1.00 13.64 ? 393  GLY B N   1 
ATOM   6366 C  CA  . GLY B  1 393 ? -51.597 23.999  -9.166  1.00 13.53 ? 393  GLY B CA  1 
ATOM   6367 C  C   . GLY B  1 393 ? -52.138 25.236  -9.856  1.00 14.98 ? 393  GLY B C   1 
ATOM   6368 O  O   . GLY B  1 393 ? -51.655 26.355  -9.539  1.00 16.45 ? 393  GLY B O   1 
ATOM   6369 N  N   . TYR B  1 394 ? -53.174 25.066  -10.677 1.00 13.63 ? 394  TYR B N   1 
ATOM   6370 C  CA  . TYR B  1 394 ? -53.743 26.163  -11.482 1.00 12.91 ? 394  TYR B CA  1 
ATOM   6371 C  C   . TYR B  1 394 ? -55.241 26.204  -11.300 1.00 14.55 ? 394  TYR B C   1 
ATOM   6372 O  O   . TYR B  1 394 ? -55.864 25.129  -11.112 1.00 15.83 ? 394  TYR B O   1 
ATOM   6373 C  CB  . TYR B  1 394 ? -53.422 25.955  -12.965 1.00 13.43 ? 394  TYR B CB  1 
ATOM   6374 C  CG  . TYR B  1 394 ? -51.944 25.855  -13.235 1.00 13.32 ? 394  TYR B CG  1 
ATOM   6375 C  CD1 . TYR B  1 394 ? -51.176 26.993  -13.416 1.00 14.89 ? 394  TYR B CD1 1 
ATOM   6376 C  CD2 . TYR B  1 394 ? -51.297 24.631  -13.227 1.00 14.95 ? 394  TYR B CD2 1 
ATOM   6377 C  CE1 . TYR B  1 394 ? -49.810 26.916  -13.622 1.00 14.48 ? 394  TYR B CE1 1 
ATOM   6378 C  CE2 . TYR B  1 394 ? -49.928 24.537  -13.398 1.00 14.85 ? 394  TYR B CE2 1 
ATOM   6379 C  CZ  . TYR B  1 394 ? -49.186 25.683  -13.635 1.00 14.73 ? 394  TYR B CZ  1 
ATOM   6380 O  OH  . TYR B  1 394 ? -47.831 25.619  -13.835 1.00 16.08 ? 394  TYR B OH  1 
ATOM   6381 N  N   . ARG B  1 395 ? -55.787 27.419  -11.382 1.00 14.75 ? 395  ARG B N   1 
ATOM   6382 C  CA  . ARG B  1 395 ? -57.249 27.663  -11.356 1.00 15.08 ? 395  ARG B CA  1 
ATOM   6383 C  C   . ARG B  1 395 ? -57.592 28.537  -12.562 1.00 16.58 ? 395  ARG B C   1 
ATOM   6384 O  O   . ARG B  1 395 ? -56.873 29.539  -12.837 1.00 14.32 ? 395  ARG B O   1 
ATOM   6385 C  CB  . ARG B  1 395 ? -57.739 28.296  -10.057 1.00 16.07 ? 395  ARG B CB  1 
ATOM   6386 C  CG  . ARG B  1 395 ? -59.255 28.375  -10.062 1.00 15.29 ? 395  ARG B CG  1 
ATOM   6387 C  CD  . ARG B  1 395 ? -59.845 28.784  -8.767  1.00 16.36 ? 395  ARG B CD  1 
ATOM   6388 N  NE  . ARG B  1 395 ? -59.668 30.207  -8.566  1.00 15.83 ? 395  ARG B NE  1 
ATOM   6389 C  CZ  . ARG B  1 395 ? -60.218 30.883  -7.588  1.00 18.03 ? 395  ARG B CZ  1 
ATOM   6390 N  NH1 . ARG B  1 395 ? -61.087 30.301  -6.767  1.00 18.19 ? 395  ARG B NH1 1 
ATOM   6391 N  NH2 . ARG B  1 395 ? -59.971 32.183  -7.496  1.00 18.73 ? 395  ARG B NH2 1 
ATOM   6392 N  N   . VAL B  1 396 ? -58.660 28.158  -13.243 1.00 16.48 ? 396  VAL B N   1 
ATOM   6393 C  CA  . VAL B  1 396 ? -59.299 28.987  -14.288 1.00 15.70 ? 396  VAL B CA  1 
ATOM   6394 C  C   . VAL B  1 396 ? -60.680 29.335  -13.739 1.00 16.88 ? 396  VAL B C   1 
ATOM   6395 O  O   . VAL B  1 396 ? -61.497 28.424  -13.555 1.00 14.66 ? 396  VAL B O   1 
ATOM   6396 C  CB  . VAL B  1 396 ? -59.342 28.274  -15.645 1.00 17.21 ? 396  VAL B CB  1 
ATOM   6397 C  CG1 . VAL B  1 396 ? -60.021 29.131  -16.699 1.00 17.53 ? 396  VAL B CG1 1 
ATOM   6398 C  CG2 . VAL B  1 396 ? -57.959 27.854  -16.143 1.00 16.86 ? 396  VAL B CG2 1 
ATOM   6399 N  N   . TYR B  1 397 ? -60.889 30.619  -13.453 1.00 17.22 ? 397  TYR B N   1 
ATOM   6400 C  CA  . TYR B  1 397 ? -62.136 31.137  -12.849 1.00 18.51 ? 397  TYR B CA  1 
ATOM   6401 C  C   . TYR B  1 397 ? -62.852 31.982  -13.898 1.00 18.88 ? 397  TYR B C   1 
ATOM   6402 O  O   . TYR B  1 397 ? -62.245 32.956  -14.398 1.00 17.95 ? 397  TYR B O   1 
ATOM   6403 C  CB  . TYR B  1 397 ? -61.815 31.905  -11.581 1.00 18.97 ? 397  TYR B CB  1 
ATOM   6404 C  CG  . TYR B  1 397 ? -63.013 32.189  -10.711 1.00 19.51 ? 397  TYR B CG  1 
ATOM   6405 C  CD1 . TYR B  1 397 ? -63.823 33.285  -10.958 1.00 19.69 ? 397  TYR B CD1 1 
ATOM   6406 C  CD2 . TYR B  1 397 ? -63.304 31.403  -9.596  1.00 21.45 ? 397  TYR B CD2 1 
ATOM   6407 C  CE1 . TYR B  1 397 ? -64.902 33.578  -10.141 1.00 22.12 ? 397  TYR B CE1 1 
ATOM   6408 C  CE2 . TYR B  1 397 ? -64.378 31.691  -8.762  1.00 23.42 ? 397  TYR B CE2 1 
ATOM   6409 C  CZ  . TYR B  1 397 ? -65.172 32.790  -9.032  1.00 23.23 ? 397  TYR B CZ  1 
ATOM   6410 O  OH  . TYR B  1 397 ? -66.259 33.094  -8.253  1.00 30.95 ? 397  TYR B OH  1 
ATOM   6411 N  N   . VAL B  1 398 ? -64.098 31.612  -14.221 1.00 19.27 ? 398  VAL B N   1 
ATOM   6412 C  CA  . VAL B  1 398 ? -64.896 32.258  -15.301 1.00 19.20 ? 398  VAL B CA  1 
ATOM   6413 C  C   . VAL B  1 398 ? -66.127 32.909  -14.671 1.00 21.01 ? 398  VAL B C   1 
ATOM   6414 O  O   . VAL B  1 398 ? -66.832 32.260  -13.896 1.00 19.13 ? 398  VAL B O   1 
ATOM   6415 C  CB  . VAL B  1 398 ? -65.270 31.248  -16.402 1.00 20.32 ? 398  VAL B CB  1 
ATOM   6416 C  CG1 . VAL B  1 398 ? -65.913 31.937  -17.591 1.00 21.05 ? 398  VAL B CG1 1 
ATOM   6417 C  CG2 . VAL B  1 398 ? -64.062 30.420  -16.837 1.00 19.80 ? 398  VAL B CG2 1 
ATOM   6418 N  N   . SER B  1 399 ? -66.335 34.202  -14.939 1.00 22.61 ? 399  SER B N   1 
ATOM   6419 C  CA  . SER B  1 399 ? -67.530 34.940  -14.488 1.00 24.07 ? 399  SER B CA  1 
ATOM   6420 C  C   . SER B  1 399 ? -67.991 35.878  -15.612 1.00 27.27 ? 399  SER B C   1 
ATOM   6421 O  O   . SER B  1 399 ? -67.279 36.012  -16.624 1.00 23.77 ? 399  SER B O   1 
ATOM   6422 C  CB  . SER B  1 399 ? -67.262 35.638  -13.179 1.00 25.69 ? 399  SER B CB  1 
ATOM   6423 O  OG  . SER B  1 399 ? -66.193 36.569  -13.321 1.00 30.57 ? 399  SER B OG  1 
ATOM   6424 N  N   . ARG B  1 400 ? -69.205 36.410  -15.475 1.00 31.41 ? 400  ARG B N   1 
ATOM   6425 C  CA  . ARG B  1 400 ? -69.800 37.405  -16.409 1.00 39.05 ? 400  ARG B CA  1 
ATOM   6426 C  C   . ARG B  1 400 ? -68.923 38.660  -16.411 1.00 36.67 ? 400  ARG B C   1 
ATOM   6427 O  O   . ARG B  1 400 ? -68.543 39.126  -15.325 1.00 35.72 ? 400  ARG B O   1 
ATOM   6428 C  CB  . ARG B  1 400 ? -71.234 37.700  -15.958 1.00 45.10 ? 400  ARG B CB  1 
ATOM   6429 C  CG  . ARG B  1 400 ? -71.917 38.858  -16.670 1.00 51.49 ? 400  ARG B CG  1 
ATOM   6430 C  CD  . ARG B  1 400 ? -73.391 38.892  -16.307 1.00 55.45 ? 400  ARG B CD  1 
ATOM   6431 N  NE  . ARG B  1 400 ? -74.157 38.128  -17.277 1.00 61.98 ? 400  ARG B NE  1 
ATOM   6432 C  CZ  . ARG B  1 400 ? -74.835 38.641  -18.298 1.00 67.45 ? 400  ARG B CZ  1 
ATOM   6433 N  NH1 . ARG B  1 400 ? -74.880 39.951  -18.492 1.00 71.36 ? 400  ARG B NH1 1 
ATOM   6434 N  NH2 . ARG B  1 400 ? -75.486 37.835  -19.120 1.00 69.03 ? 400  ARG B NH2 1 
ATOM   6435 N  N   . LEU B  1 401 ? -68.630 39.204  -17.589 1.00 45.48 ? 401  LEU B N   1 
ATOM   6436 C  CA  . LEU B  1 401 ? -67.698 40.360  -17.736 1.00 51.53 ? 401  LEU B CA  1 
ATOM   6437 C  C   . LEU B  1 401 ? -68.248 41.603  -17.014 1.00 55.95 ? 401  LEU B C   1 
ATOM   6438 O  O   . LEU B  1 401 ? -69.324 42.118  -17.317 1.00 62.17 ? 401  LEU B O   1 
ATOM   6439 C  CB  . LEU B  1 401 ? -67.487 40.591  -19.232 1.00 51.79 ? 401  LEU B CB  1 
ATOM   6440 C  CG  . LEU B  1 401 ? -66.660 41.811  -19.623 1.00 53.47 ? 401  LEU B CG  1 
ATOM   6441 C  CD1 . LEU B  1 401 ? -65.507 42.075  -18.662 1.00 52.73 ? 401  LEU B CD1 1 
ATOM   6442 C  CD2 . LEU B  1 401 ? -66.149 41.636  -21.045 1.00 55.26 ? 401  LEU B CD2 1 
HETATM 6443 C  C1  A GOL C  2 .   ? -13.646 -20.893 8.051   0.70 25.42 ? 501  GOL A C1  1 
HETATM 6444 C  C1  B GOL C  2 .   ? -14.168 -20.766 7.840   0.30 15.09 ? 501  GOL A C1  1 
HETATM 6445 O  O1  A GOL C  2 .   ? -14.223 -19.588 7.948   0.70 19.09 ? 501  GOL A O1  1 
HETATM 6446 O  O1  B GOL C  2 .   ? -14.364 -19.502 8.475   0.30 12.41 ? 501  GOL A O1  1 
HETATM 6447 C  C2  A GOL C  2 .   ? -13.677 -21.683 6.758   0.70 27.15 ? 501  GOL A C2  1 
HETATM 6448 C  C2  B GOL C  2 .   ? -13.557 -20.607 6.466   0.30 15.84 ? 501  GOL A C2  1 
HETATM 6449 O  O2  A GOL C  2 .   ? -14.875 -21.416 6.024   0.70 28.49 ? 501  GOL A O2  1 
HETATM 6450 O  O2  B GOL C  2 .   ? -12.513 -19.644 6.545   0.30 16.18 ? 501  GOL A O2  1 
HETATM 6451 C  C3  A GOL C  2 .   ? -12.461 -21.421 5.884   0.70 28.14 ? 501  GOL A C3  1 
HETATM 6452 C  C3  B GOL C  2 .   ? -13.009 -21.903 5.900   0.30 16.73 ? 501  GOL A C3  1 
HETATM 6453 O  O3  A GOL C  2 .   ? -11.244 -21.887 6.481   0.70 29.57 ? 501  GOL A O3  1 
HETATM 6454 O  O3  B GOL C  2 .   ? -12.143 -22.547 6.833   0.30 18.06 ? 501  GOL A O3  1 
HETATM 6455 C  C   . FMT D  3 .   ? -28.311 -6.566  21.471  1.00 50.78 ? 502  FMT A C   1 
HETATM 6456 O  O1  . FMT D  3 .   ? -27.293 -6.207  22.023  1.00 48.36 ? 502  FMT A O1  1 
HETATM 6457 O  O2  . FMT D  3 .   ? -29.267 -7.215  22.068  1.00 50.50 ? 502  FMT A O2  1 
HETATM 6458 C  C   . FMT E  3 .   ? -48.852 -1.439  -6.630  1.00 35.23 ? 503  FMT A C   1 
HETATM 6459 O  O1  . FMT E  3 .   ? -48.562 -2.407  -5.940  1.00 33.43 ? 503  FMT A O1  1 
HETATM 6460 O  O2  . FMT E  3 .   ? -50.025 -1.155  -7.225  1.00 33.66 ? 503  FMT A O2  1 
HETATM 6461 C  C   . FMT F  3 .   ? -37.317 -2.607  7.755   1.00 49.40 ? 504  FMT A C   1 
HETATM 6462 O  O1  . FMT F  3 .   ? -36.466 -3.458  7.593   1.00 45.19 ? 504  FMT A O1  1 
HETATM 6463 O  O2  . FMT F  3 .   ? -38.585 -2.726  7.445   1.00 46.24 ? 504  FMT A O2  1 
HETATM 6464 C  C   . FMT G  3 .   ? -5.644  -2.932  15.029  1.00 29.46 ? 505  FMT A C   1 
HETATM 6465 O  O1  . FMT G  3 .   ? -5.649  -2.429  13.925  1.00 25.33 ? 505  FMT A O1  1 
HETATM 6466 O  O2  . FMT G  3 .   ? -4.940  -3.974  15.380  1.00 37.51 ? 505  FMT A O2  1 
HETATM 6467 C  C   . FMT H  3 .   ? -20.224 -4.729  18.422  1.00 28.86 ? 506  FMT A C   1 
HETATM 6468 O  O1  . FMT H  3 .   ? -20.447 -5.895  18.191  1.00 33.22 ? 506  FMT A O1  1 
HETATM 6469 O  O2  . FMT H  3 .   ? -20.553 -4.113  19.484  1.00 32.94 ? 506  FMT A O2  1 
HETATM 6470 C  C   . FMT I  3 .   ? -15.286 -0.616  -21.266 1.00 52.27 ? 507  FMT A C   1 
HETATM 6471 O  O1  . FMT I  3 .   ? -14.686 -1.664  -21.142 1.00 54.79 ? 507  FMT A O1  1 
HETATM 6472 O  O2  . FMT I  3 .   ? -15.222 0.387   -20.438 1.00 49.02 ? 507  FMT A O2  1 
HETATM 6473 C  C   . FMT J  3 .   ? -26.327 -3.416  9.234   1.00 46.99 ? 508  FMT A C   1 
HETATM 6474 O  O1  . FMT J  3 .   ? -25.193 -2.976  9.198   1.00 46.67 ? 508  FMT A O1  1 
HETATM 6475 O  O2  . FMT J  3 .   ? -26.795 -4.360  8.472   1.00 42.05 ? 508  FMT A O2  1 
HETATM 6476 C  C   . FMT K  3 .   ? -8.280  -14.525 28.919  1.00 48.86 ? 509  FMT A C   1 
HETATM 6477 O  O1  . FMT K  3 .   ? -7.087  -14.370 28.745  1.00 51.36 ? 509  FMT A O1  1 
HETATM 6478 O  O2  . FMT K  3 .   ? -8.890  -15.678 28.954  1.00 37.98 ? 509  FMT A O2  1 
HETATM 6479 C  C   . FMT L  3 .   ? -24.922 -0.612  5.281   1.00 53.72 ? 510  FMT A C   1 
HETATM 6480 O  O1  . FMT L  3 .   ? -26.071 -0.414  5.625   1.00 53.39 ? 510  FMT A O1  1 
HETATM 6481 O  O2  . FMT L  3 .   ? -23.914 0.175   5.512   1.00 52.62 ? 510  FMT A O2  1 
HETATM 6482 C  C   . FMT M  3 .   ? -13.539 -24.398 -4.394  1.00 43.04 ? 511  FMT A C   1 
HETATM 6483 O  O1  . FMT M  3 .   ? -14.274 -25.190 -4.944  1.00 39.67 ? 511  FMT A O1  1 
HETATM 6484 O  O2  . FMT M  3 .   ? -12.319 -24.134 -4.766  1.00 52.29 ? 511  FMT A O2  1 
HETATM 6485 C  C   . FMT N  3 .   ? -10.341 -16.949 -14.409 1.00 28.16 ? 512  FMT A C   1 
HETATM 6486 O  O1  . FMT N  3 .   ? -10.549 -16.081 -15.220 1.00 28.23 ? 512  FMT A O1  1 
HETATM 6487 O  O2  . FMT N  3 .   ? -11.221 -17.699 -13.838 1.00 38.24 ? 512  FMT A O2  1 
HETATM 6488 C  C   . FMT O  3 .   ? -46.795 9.795   -17.827 1.00 41.45 ? 513  FMT A C   1 
HETATM 6489 O  O1  . FMT O  3 .   ? -47.626 9.697   -18.716 1.00 39.62 ? 513  FMT A O1  1 
HETATM 6490 O  O2  . FMT O  3 .   ? -46.346 10.896  -17.270 1.00 31.59 ? 513  FMT A O2  1 
HETATM 6491 C  C   . FMT P  3 .   ? -16.692 -2.276  20.603  1.00 42.50 ? 514  FMT A C   1 
HETATM 6492 O  O1  . FMT P  3 .   ? -17.405 -1.582  19.899  1.00 48.84 ? 514  FMT A O1  1 
HETATM 6493 O  O2  . FMT P  3 .   ? -16.684 -2.296  21.918  1.00 38.05 ? 514  FMT A O2  1 
HETATM 6494 C  C   . FMT Q  3 .   ? -9.981  -11.712 31.707  1.00 52.54 ? 515  FMT A C   1 
HETATM 6495 O  O1  . FMT Q  3 .   ? -10.963 -11.167 31.240  1.00 48.99 ? 515  FMT A O1  1 
HETATM 6496 O  O2  . FMT Q  3 .   ? -8.989  -12.187 31.011  1.00 58.36 ? 515  FMT A O2  1 
HETATM 6497 C  C   . FMT R  3 .   ? -20.021 1.091   -24.887 1.00 49.31 ? 516  FMT A C   1 
HETATM 6498 O  O1  . FMT R  3 .   ? -19.860 1.756   -23.885 1.00 42.28 ? 516  FMT A O1  1 
HETATM 6499 O  O2  . FMT R  3 .   ? -19.431 -0.039  -25.134 1.00 58.79 ? 516  FMT A O2  1 
HETATM 6500 C  C   . FMT S  3 .   ? -5.660  -22.623 -5.511  1.00 44.24 ? 517  FMT A C   1 
HETATM 6501 O  O1  . FMT S  3 .   ? -6.789  -23.077 -5.537  1.00 50.79 ? 517  FMT A O1  1 
HETATM 6502 O  O2  . FMT S  3 .   ? -5.271  -21.498 -6.067  1.00 40.34 ? 517  FMT A O2  1 
HETATM 6503 C  C1  . PGE T  4 .   ? -40.940 22.475  -8.366  1.00 39.86 ? 501  PGE B C1  1 
HETATM 6504 O  O1  . PGE T  4 .   ? -40.018 23.303  -7.674  1.00 39.90 ? 501  PGE B O1  1 
HETATM 6505 C  C2  . PGE T  4 .   ? -40.980 22.754  -9.860  1.00 43.82 ? 501  PGE B C2  1 
HETATM 6506 O  O2  . PGE T  4 .   ? -41.655 21.703  -10.556 1.00 39.85 ? 501  PGE B O2  1 
HETATM 6507 C  C3  . PGE T  4 .   ? -41.572 21.773  -11.979 1.00 35.13 ? 501  PGE B C3  1 
HETATM 6508 C  C4  . PGE T  4 .   ? -41.671 20.385  -12.599 1.00 30.21 ? 501  PGE B C4  1 
HETATM 6509 O  O3  . PGE T  4 .   ? -42.006 20.497  -13.978 1.00 21.26 ? 501  PGE B O3  1 
HETATM 6510 C  C1  . GOL U  2 .   ? -49.163 4.446   11.992  1.00 42.45 ? 502  GOL B C1  1 
HETATM 6511 O  O1  . GOL U  2 .   ? -48.098 3.705   12.575  1.00 35.81 ? 502  GOL B O1  1 
HETATM 6512 C  C2  . GOL U  2 .   ? -49.610 3.796   10.714  1.00 46.27 ? 502  GOL B C2  1 
HETATM 6513 O  O2  . GOL U  2 .   ? -50.365 4.749   9.969   1.00 39.00 ? 502  GOL B O2  1 
HETATM 6514 C  C3  . GOL U  2 .   ? -48.445 3.219   9.921   1.00 50.70 ? 502  GOL B C3  1 
HETATM 6515 O  O3  . GOL U  2 .   ? -47.209 3.905   10.141  1.00 51.61 ? 502  GOL B O3  1 
HETATM 6516 C  C1  . GOL V  2 .   ? -46.647 14.837  -21.911 1.00 45.61 ? 503  GOL B C1  1 
HETATM 6517 O  O1  . GOL V  2 .   ? -46.365 15.982  -21.110 1.00 39.25 ? 503  GOL B O1  1 
HETATM 6518 C  C2  . GOL V  2 .   ? -47.636 15.109  -23.024 1.00 47.44 ? 503  GOL B C2  1 
HETATM 6519 O  O2  . GOL V  2 .   ? -48.029 13.850  -23.588 1.00 51.51 ? 503  GOL B O2  1 
HETATM 6520 C  C3  . GOL V  2 .   ? -48.850 15.896  -22.563 1.00 44.31 ? 503  GOL B C3  1 
HETATM 6521 O  O3  . GOL V  2 .   ? -49.341 16.770  -23.575 1.00 45.01 ? 503  GOL B O3  1 
HETATM 6522 N  N1  . BCN W  5 .   ? -49.577 3.877   5.055   1.00 21.97 ? 504  BCN B N1  1 
HETATM 6523 C  C1  . BCN W  5 .   ? -49.038 2.892   4.111   1.00 24.56 ? 504  BCN B C1  1 
HETATM 6524 C  C2  . BCN W  5 .   ? -47.640 2.344   4.471   1.00 29.30 ? 504  BCN B C2  1 
HETATM 6525 O  O21 . BCN W  5 .   ? -47.145 1.475   3.698   1.00 27.26 ? 504  BCN B O21 1 
HETATM 6526 O  O22 . BCN W  5 .   ? -47.081 2.772   5.548   1.00 27.98 ? 504  BCN B O22 1 
HETATM 6527 C  C3  . BCN W  5 .   ? -49.664 3.368   6.439   1.00 23.00 ? 504  BCN B C3  1 
HETATM 6528 C  C4  . BCN W  5 .   ? -51.074 3.298   6.983   1.00 22.39 ? 504  BCN B C4  1 
HETATM 6529 O  O4  . BCN W  5 .   ? -51.802 2.350   6.249   1.00 17.59 ? 504  BCN B O4  1 
HETATM 6530 C  C5  . BCN W  5 .   ? -48.859 5.159   5.068   1.00 20.09 ? 504  BCN B C5  1 
HETATM 6531 C  C6  . BCN W  5 .   ? -49.225 6.134   3.979   1.00 19.23 ? 504  BCN B C6  1 
HETATM 6532 O  O6  . BCN W  5 .   ? -50.488 6.719   4.207   1.00 16.39 ? 504  BCN B O6  1 
HETATM 6533 C  C   A FMT X  3 .   ? -64.361 14.497  22.951  0.80 25.49 ? 505  FMT B C   1 
HETATM 6534 C  C   B FMT X  3 .   ? -64.368 13.741  23.090  0.20 8.78  ? 505  FMT B C   1 
HETATM 6535 O  O1  A FMT X  3 .   ? -64.522 15.587  22.430  0.80 24.89 ? 505  FMT B O1  1 
HETATM 6536 O  O1  B FMT X  3 .   ? -63.954 14.868  22.913  0.20 8.86  ? 505  FMT B O1  1 
HETATM 6537 O  O2  A FMT X  3 .   ? -63.214 13.974  23.276  0.80 24.86 ? 505  FMT B O2  1 
HETATM 6538 O  O2  B FMT X  3 .   ? -65.502 13.424  23.653  0.20 8.54  ? 505  FMT B O2  1 
HETATM 6539 C  C   A FMT Y  3 .   ? -54.974 -14.977 6.740   0.80 46.00 ? 506  FMT B C   1 
HETATM 6540 C  C   B FMT Y  3 .   ? -55.959 -15.260 6.141   0.20 7.57  ? 506  FMT B C   1 
HETATM 6541 O  O1  A FMT Y  3 .   ? -55.396 -16.107 6.570   0.80 49.04 ? 506  FMT B O1  1 
HETATM 6542 O  O1  B FMT Y  3 .   ? -55.844 -16.473 6.085   0.20 7.31  ? 506  FMT B O1  1 
HETATM 6543 O  O2  A FMT Y  3 .   ? -55.651 -13.984 7.249   0.80 32.93 ? 506  FMT B O2  1 
HETATM 6544 O  O2  B FMT Y  3 .   ? -55.832 -14.518 7.217   0.20 7.12  ? 506  FMT B O2  1 
HETATM 6545 C  C   . FMT Z  3 .   ? -56.692 -1.214  -14.023 1.00 55.92 ? 507  FMT B C   1 
HETATM 6546 O  O1  . FMT Z  3 .   ? -57.232 -1.776  -13.090 1.00 50.71 ? 507  FMT B O1  1 
HETATM 6547 O  O2  . FMT Z  3 .   ? -55.963 -0.144  -13.916 1.00 50.31 ? 507  FMT B O2  1 
HETATM 6548 C  C   . FMT AA 3 .   ? -49.620 -6.871  0.173   1.00 47.28 ? 508  FMT B C   1 
HETATM 6549 O  O1  . FMT AA 3 .   ? -48.414 -6.765  0.316   1.00 51.60 ? 508  FMT B O1  1 
HETATM 6550 O  O2  . FMT AA 3 .   ? -50.242 -7.251  -0.921  1.00 42.79 ? 508  FMT B O2  1 
HETATM 6551 C  C   . FMT BA 3 .   ? -71.566 6.977   12.085  1.00 24.07 ? 509  FMT B C   1 
HETATM 6552 O  O1  . FMT BA 3 .   ? -72.703 6.907   12.473  1.00 35.27 ? 509  FMT B O1  1 
HETATM 6553 O  O2  . FMT BA 3 .   ? -70.740 5.991   12.062  1.00 39.83 ? 509  FMT B O2  1 
HETATM 6554 C  C   . FMT CA 3 .   ? -40.671 23.244  8.002   1.00 47.89 ? 510  FMT B C   1 
HETATM 6555 O  O1  . FMT CA 3 .   ? -41.032 24.291  7.500   1.00 51.84 ? 510  FMT B O1  1 
HETATM 6556 O  O2  . FMT CA 3 .   ? -41.437 22.222  8.289   1.00 40.81 ? 510  FMT B O2  1 
HETATM 6557 C  C   . FMT DA 3 .   ? -45.293 23.533  -24.721 1.00 52.27 ? 511  FMT B C   1 
HETATM 6558 O  O1  . FMT DA 3 .   ? -46.439 23.368  -25.083 1.00 46.82 ? 511  FMT B O1  1 
HETATM 6559 O  O2  . FMT DA 3 .   ? -44.871 24.520  -23.983 1.00 57.34 ? 511  FMT B O2  1 
HETATM 6560 C  C   . FMT EA 3 .   ? -72.018 7.015   8.973   1.00 44.51 ? 512  FMT B C   1 
HETATM 6561 O  O1  . FMT EA 3 .   ? -73.213 7.210   8.820   1.00 46.37 ? 512  FMT B O1  1 
HETATM 6562 O  O2  . FMT EA 3 .   ? -71.446 6.064   9.711   1.00 30.60 ? 512  FMT B O2  1 
HETATM 6563 C  C   . FMT FA 3 .   ? -56.812 4.279   25.234  1.00 44.82 ? 513  FMT B C   1 
HETATM 6564 O  O1  . FMT FA 3 .   ? -55.937 3.728   25.874  1.00 48.06 ? 513  FMT B O1  1 
HETATM 6565 O  O2  . FMT FA 3 .   ? -57.001 5.567   25.163  1.00 44.44 ? 513  FMT B O2  1 
HETATM 6566 C  C   . FMT GA 3 .   ? -55.729 31.712  -24.737 1.00 43.38 ? 514  FMT B C   1 
HETATM 6567 O  O1  . FMT GA 3 .   ? -56.541 31.485  -25.620 1.00 45.47 ? 514  FMT B O1  1 
HETATM 6568 O  O2  . FMT GA 3 .   ? -55.992 32.057  -23.503 1.00 37.24 ? 514  FMT B O2  1 
HETATM 6569 C  C   . FMT HA 3 .   ? -66.237 -18.199 8.107   1.00 47.38 ? 515  FMT B C   1 
HETATM 6570 O  O1  . FMT HA 3 .   ? -66.726 -18.239 9.219   1.00 56.31 ? 515  FMT B O1  1 
HETATM 6571 O  O2  . FMT HA 3 .   ? -64.981 -18.374 7.846   1.00 46.13 ? 515  FMT B O2  1 
HETATM 6572 C  C   . FMT IA 3 .   ? -72.760 11.466  -3.727  1.00 49.15 ? 516  FMT B C   1 
HETATM 6573 O  O1  . FMT IA 3 .   ? -72.769 12.659  -3.491  1.00 44.30 ? 516  FMT B O1  1 
HETATM 6574 O  O2  . FMT IA 3 .   ? -72.098 10.866  -4.695  1.00 43.52 ? 516  FMT B O2  1 
HETATM 6575 C  C   . FMT JA 3 .   ? -78.181 -16.746 2.545   1.00 54.14 ? 517  FMT B C   1 
HETATM 6576 O  O1  . FMT JA 3 .   ? -78.829 -17.774 2.482   1.00 50.73 ? 517  FMT B O1  1 
HETATM 6577 O  O2  . FMT JA 3 .   ? -78.053 -15.858 1.590   1.00 47.33 ? 517  FMT B O2  1 
HETATM 6578 C  C   . FMT KA 3 .   ? -73.756 -13.611 8.535   1.00 53.62 ? 518  FMT B C   1 
HETATM 6579 O  O1  . FMT KA 3 .   ? -74.043 -12.855 9.442   1.00 59.12 ? 518  FMT B O1  1 
HETATM 6580 O  O2  . FMT KA 3 .   ? -72.960 -14.636 8.632   1.00 49.48 ? 518  FMT B O2  1 
HETATM 6581 C  C   . FMT LA 3 .   ? -41.922 26.277  -8.606  1.00 44.77 ? 519  FMT B C   1 
HETATM 6582 O  O1  . FMT LA 3 .   ? -42.045 26.063  -9.796  1.00 40.69 ? 519  FMT B O1  1 
HETATM 6583 O  O2  . FMT LA 3 .   ? -40.808 26.610  -8.007  1.00 53.25 ? 519  FMT B O2  1 
HETATM 6584 NA NA  . NA  MA 6 .   ? -42.799 15.537  -7.830  1.00 25.78 ? 520  NA  B NA  1 
HETATM 6585 O  O   . HOH NA 7 .   ? -17.146 -11.803 -22.382 0.70 31.83 ? 601  HOH A O   1 
HETATM 6586 O  O   . HOH NA 7 .   ? -19.641 -34.438 21.880  1.00 38.62 ? 602  HOH A O   1 
HETATM 6587 O  O   . HOH NA 7 .   ? -2.657  -17.329 18.151  1.00 26.73 ? 603  HOH A O   1 
HETATM 6588 O  O   . HOH NA 7 .   ? -16.237 -17.714 -19.212 1.00 46.77 ? 604  HOH A O   1 
HETATM 6589 O  O   . HOH NA 7 .   ? -2.798  -12.959 -4.924  1.00 35.51 ? 605  HOH A O   1 
HETATM 6590 O  O   . HOH NA 7 .   ? -2.900  -10.554 5.946   1.00 21.12 ? 606  HOH A O   1 
HETATM 6591 O  O   . HOH NA 7 .   ? -9.780  -19.086 -12.679 1.00 45.79 ? 607  HOH A O   1 
HETATM 6592 O  O   . HOH NA 7 .   ? -22.717 -5.806  17.733  1.00 26.10 ? 608  HOH A O   1 
HETATM 6593 O  O   . HOH NA 7 .   ? -41.338 -3.439  3.838   1.00 42.14 ? 609  HOH A O   1 
HETATM 6594 O  O   . HOH NA 7 .   ? -34.109 -3.545  7.582   1.00 38.30 ? 610  HOH A O   1 
HETATM 6595 O  O   . HOH NA 7 .   ? -26.184 -32.662 12.491  1.00 28.69 ? 611  HOH A O   1 
HETATM 6596 O  O   . HOH NA 7 .   ? -29.590 14.235  -4.221  1.00 30.97 ? 612  HOH A O   1 
HETATM 6597 O  O   . HOH NA 7 .   ? -14.800 -18.793 -17.375 1.00 38.65 ? 613  HOH A O   1 
HETATM 6598 O  O   . HOH NA 7 .   ? -25.183 7.446   -6.028  1.00 25.74 ? 614  HOH A O   1 
HETATM 6599 O  O   . HOH NA 7 .   ? -13.001 -16.839 -2.692  1.00 12.79 ? 615  HOH A O   1 
HETATM 6600 O  O   . HOH NA 7 .   ? -22.452 -25.310 3.609   1.00 32.47 ? 616  HOH A O   1 
HETATM 6601 O  O   . HOH NA 7 .   ? -15.484 7.988   5.326   1.00 41.54 ? 617  HOH A O   1 
HETATM 6602 O  O   . HOH NA 7 .   ? -41.995 -9.633  -21.172 1.00 26.42 ? 618  HOH A O   1 
HETATM 6603 O  O   . HOH NA 7 .   ? -14.914 -31.499 24.967  1.00 43.10 ? 619  HOH A O   1 
HETATM 6604 O  O   . HOH NA 7 .   ? -1.528  -4.353  6.006   1.00 33.75 ? 620  HOH A O   1 
HETATM 6605 O  O   . HOH NA 7 .   ? -34.542 -2.340  -26.560 1.00 30.47 ? 621  HOH A O   1 
HETATM 6606 O  O   . HOH NA 7 .   ? -44.244 2.857   -0.408  1.00 31.20 ? 622  HOH A O   1 
HETATM 6607 O  O   . HOH NA 7 .   ? -42.959 4.358   -2.939  1.00 33.56 ? 623  HOH A O   1 
HETATM 6608 O  O   . HOH NA 7 .   ? -0.904  -6.384  1.325   1.00 34.02 ? 624  HOH A O   1 
HETATM 6609 O  O   . HOH NA 7 .   ? -5.707  -2.481  11.392  1.00 15.80 ? 625  HOH A O   1 
HETATM 6610 O  O   . HOH NA 7 .   ? -32.002 6.031   2.234   1.00 45.05 ? 626  HOH A O   1 
HETATM 6611 O  O   . HOH NA 7 .   ? -34.409 17.047  -5.199  1.00 45.18 ? 627  HOH A O   1 
HETATM 6612 O  O   . HOH NA 7 .   ? -42.493 -28.067 12.267  1.00 34.27 ? 628  HOH A O   1 
HETATM 6613 O  O   . HOH NA 7 .   ? -2.826  0.954   1.455   1.00 42.82 ? 629  HOH A O   1 
HETATM 6614 O  O   . HOH NA 7 .   ? -45.090 -6.296  -15.720 1.00 47.04 ? 630  HOH A O   1 
HETATM 6615 O  O   . HOH NA 7 .   ? -34.683 -28.489 20.899  1.00 26.60 ? 631  HOH A O   1 
HETATM 6616 O  O   . HOH NA 7 .   ? -4.818  -6.145  -2.917  1.00 18.46 ? 632  HOH A O   1 
HETATM 6617 O  O   . HOH NA 7 .   ? -37.497 -20.141 -2.809  1.00 13.56 ? 633  HOH A O   1 
HETATM 6618 O  O   . HOH NA 7 .   ? -17.503 1.276   9.221   1.00 18.26 ? 634  HOH A O   1 
HETATM 6619 O  O   . HOH NA 7 .   ? -13.717 -11.312 -10.606 1.00 14.30 ? 635  HOH A O   1 
HETATM 6620 O  O   . HOH NA 7 .   ? -28.879 -26.827 15.569  1.00 20.43 ? 636  HOH A O   1 
HETATM 6621 O  O   . HOH NA 7 .   ? -39.826 -15.085 1.305   1.00 28.68 ? 637  HOH A O   1 
HETATM 6622 O  O   . HOH NA 7 .   ? -21.716 -16.168 -20.369 1.00 39.14 ? 638  HOH A O   1 
HETATM 6623 O  O   . HOH NA 7 .   ? -29.728 11.427  -2.916  1.00 30.99 ? 639  HOH A O   1 
HETATM 6624 O  O   . HOH NA 7 .   ? -39.361 -13.242 -1.748  1.00 35.19 ? 640  HOH A O   1 
HETATM 6625 O  O   . HOH NA 7 .   ? -42.790 15.006  -19.358 1.00 34.15 ? 641  HOH A O   1 
HETATM 6626 O  O   . HOH NA 7 .   ? -21.082 1.791   -18.999 1.00 21.37 ? 642  HOH A O   1 
HETATM 6627 O  O   . HOH NA 7 .   ? -32.637 -4.939  9.363   1.00 28.10 ? 643  HOH A O   1 
HETATM 6628 O  O   . HOH NA 7 .   ? -21.215 -12.872 -5.431  1.00 15.55 ? 644  HOH A O   1 
HETATM 6629 O  O   . HOH NA 7 .   ? -50.048 -1.451  -9.798  1.00 37.89 ? 645  HOH A O   1 
HETATM 6630 O  O   . HOH NA 7 .   ? -42.155 -26.602 16.953  1.00 37.95 ? 646  HOH A O   1 
HETATM 6631 O  O   . HOH NA 7 .   ? -28.433 -2.450  7.843   1.00 37.62 ? 647  HOH A O   1 
HETATM 6632 O  O   . HOH NA 7 .   ? -20.484 4.180   -4.636  1.00 20.60 ? 648  HOH A O   1 
HETATM 6633 O  O   . HOH NA 7 .   ? -14.203 -15.454 31.068  1.00 31.15 ? 649  HOH A O   1 
HETATM 6634 O  O   . HOH NA 7 .   ? -26.057 -23.124 32.526  1.00 45.93 ? 650  HOH A O   1 
HETATM 6635 O  O   . HOH NA 7 .   ? -13.640 -9.241  30.105  1.00 40.94 ? 651  HOH A O   1 
HETATM 6636 O  O   . HOH NA 7 .   ? -30.106 -27.212 18.287  1.00 23.06 ? 652  HOH A O   1 
HETATM 6637 O  O   . HOH NA 7 .   ? -1.764  -4.905  -12.006 1.00 31.97 ? 653  HOH A O   1 
HETATM 6638 O  O   . HOH NA 7 .   ? -17.535 -21.794 6.241   1.00 16.44 ? 654  HOH A O   1 
HETATM 6639 O  O   . HOH NA 7 .   ? -28.283 -13.769 -26.108 1.00 33.19 ? 655  HOH A O   1 
HETATM 6640 O  O   . HOH NA 7 .   ? -27.639 -7.579  26.195  1.00 31.30 ? 656  HOH A O   1 
HETATM 6641 O  O   . HOH NA 7 .   ? -4.681  -24.051 18.390  1.00 36.92 ? 657  HOH A O   1 
HETATM 6642 O  O   . HOH NA 7 .   ? -24.877 5.009   -2.017  1.00 34.60 ? 658  HOH A O   1 
HETATM 6643 O  O   . HOH NA 7 .   ? -27.876 8.838   -20.963 1.00 25.52 ? 659  HOH A O   1 
HETATM 6644 O  O   . HOH NA 7 .   ? -39.073 -23.418 -9.456  1.00 33.12 ? 660  HOH A O   1 
HETATM 6645 O  O   . HOH NA 7 .   ? -44.378 -0.917  0.573   1.00 48.74 ? 661  HOH A O   1 
HETATM 6646 O  O   . HOH NA 7 .   ? -27.837 -5.192  12.443  1.00 20.89 ? 662  HOH A O   1 
HETATM 6647 O  O   . HOH NA 7 .   ? -51.227 2.495   -9.296  1.00 21.27 ? 663  HOH A O   1 
HETATM 6648 O  O   . HOH NA 7 .   ? -12.585 -22.668 32.527  1.00 43.15 ? 664  HOH A O   1 
HETATM 6649 O  O   . HOH NA 7 .   ? -21.816 -2.598  -2.969  1.00 12.54 ? 665  HOH A O   1 
HETATM 6650 O  O   . HOH NA 7 .   ? -16.077 -7.376  -19.192 1.00 30.66 ? 666  HOH A O   1 
HETATM 6651 O  O   . HOH NA 7 .   ? -24.032 -14.854 33.240  1.00 41.78 ? 667  HOH A O   1 
HETATM 6652 O  O   . HOH NA 7 .   ? -22.829 -9.048  -23.304 1.00 18.92 ? 668  HOH A O   1 
HETATM 6653 O  O   . HOH NA 7 .   ? -22.992 -27.724 -0.676  1.00 44.23 ? 669  HOH A O   1 
HETATM 6654 O  O   . HOH NA 7 .   ? -25.549 -8.968  -22.966 1.00 16.64 ? 670  HOH A O   1 
HETATM 6655 O  O   . HOH NA 7 .   ? -11.106 -32.194 12.547  1.00 33.41 ? 671  HOH A O   1 
HETATM 6656 O  O   . HOH NA 7 .   ? -15.961 -29.014 16.095  1.00 20.49 ? 672  HOH A O   1 
HETATM 6657 O  O   . HOH NA 7 .   ? -35.269 12.865  -12.851 1.00 36.74 ? 673  HOH A O   1 
HETATM 6658 O  O   . HOH NA 7 .   ? -13.254 -11.709 32.413  1.00 38.45 ? 674  HOH A O   1 
HETATM 6659 O  O   . HOH NA 7 .   ? -12.478 -23.865 -0.523  1.00 35.60 ? 675  HOH A O   1 
HETATM 6660 O  O   . HOH NA 7 .   ? -17.548 -20.010 1.796   1.00 15.31 ? 676  HOH A O   1 
HETATM 6661 O  O   . HOH NA 7 .   ? -18.009 -32.797 11.430  1.00 30.09 ? 677  HOH A O   1 
HETATM 6662 O  O   . HOH NA 7 .   ? -39.775 -8.034  2.681   1.00 36.69 ? 678  HOH A O   1 
HETATM 6663 O  O   . HOH NA 7 .   ? -23.728 0.825   2.966   1.00 24.80 ? 679  HOH A O   1 
HETATM 6664 O  O   . HOH NA 7 .   ? -20.212 -3.523  22.031  1.00 38.64 ? 680  HOH A O   1 
HETATM 6665 O  O   . HOH NA 7 .   ? -11.184 -14.791 -3.590  1.00 12.98 ? 681  HOH A O   1 
HETATM 6666 O  O   . HOH NA 7 .   ? -5.671  -13.444 -10.465 1.00 19.43 ? 682  HOH A O   1 
HETATM 6667 O  O   . HOH NA 7 .   ? -0.426  -10.142 -4.177  1.00 23.75 ? 683  HOH A O   1 
HETATM 6668 O  O   . HOH NA 7 .   ? -16.078 2.923   11.346  1.00 31.65 ? 684  HOH A O   1 
HETATM 6669 O  O   . HOH NA 7 .   ? -3.195  -10.288 12.123  1.00 25.85 ? 685  HOH A O   1 
HETATM 6670 O  O   . HOH NA 7 .   ? -29.673 -4.102  6.090   1.00 17.96 ? 686  HOH A O   1 
HETATM 6671 O  O   . HOH NA 7 .   ? -27.755 -30.607 25.388  1.00 42.75 ? 687  HOH A O   1 
HETATM 6672 O  O   . HOH NA 7 .   ? -34.693 -16.088 -9.568  1.00 12.58 ? 688  HOH A O   1 
HETATM 6673 O  O   . HOH NA 7 .   ? -41.342 -14.005 12.137  1.00 20.76 ? 689  HOH A O   1 
HETATM 6674 O  O   . HOH NA 7 .   ? -42.254 15.758  -13.330 1.00 25.11 ? 690  HOH A O   1 
HETATM 6675 O  O   . HOH NA 7 .   ? -11.209 -15.216 -6.261  1.00 11.84 ? 691  HOH A O   1 
HETATM 6676 O  O   . HOH NA 7 .   ? -26.850 -17.013 -13.934 1.00 26.96 ? 692  HOH A O   1 
HETATM 6677 O  O   . HOH NA 7 .   ? -5.253  -12.781 -2.362  1.00 16.27 ? 693  HOH A O   1 
HETATM 6678 O  O   . HOH NA 7 .   ? -50.604 1.271   -6.318  1.00 25.81 ? 694  HOH A O   1 
HETATM 6679 O  O   . HOH NA 7 .   ? -24.613 -17.703 -14.026 1.00 32.24 ? 695  HOH A O   1 
HETATM 6680 O  O   . HOH NA 7 .   ? -31.731 -26.444 2.577   1.00 42.64 ? 696  HOH A O   1 
HETATM 6681 O  O   . HOH NA 7 .   ? -19.421 1.882   -14.800 1.00 31.37 ? 697  HOH A O   1 
HETATM 6682 O  O   . HOH NA 7 .   ? -13.838 2.219   -16.592 1.00 31.77 ? 698  HOH A O   1 
HETATM 6683 O  O   . HOH NA 7 .   ? -7.123  -5.065  20.705  1.00 22.22 ? 699  HOH A O   1 
HETATM 6684 O  O   . HOH NA 7 .   ? -27.270 1.949   -16.419 1.00 15.18 ? 700  HOH A O   1 
HETATM 6685 O  O   . HOH NA 7 .   ? -7.488  -27.415 18.233  1.00 23.52 ? 701  HOH A O   1 
HETATM 6686 O  O   . HOH NA 7 .   ? -19.089 -20.646 -13.817 1.00 43.63 ? 702  HOH A O   1 
HETATM 6687 O  O   . HOH NA 7 .   ? -24.189 -9.322  23.606  1.00 18.21 ? 703  HOH A O   1 
HETATM 6688 O  O   . HOH NA 7 .   ? -38.374 -12.986 -26.283 1.00 35.94 ? 704  HOH A O   1 
HETATM 6689 O  O   . HOH NA 7 .   ? -30.787 7.289   -28.318 1.00 19.78 ? 705  HOH A O   1 
HETATM 6690 O  O   . HOH NA 7 .   ? -14.332 4.233   16.997  1.00 36.65 ? 706  HOH A O   1 
HETATM 6691 O  O   . HOH NA 7 .   ? -5.338  -4.423  -15.373 1.00 41.71 ? 707  HOH A O   1 
HETATM 6692 O  O   . HOH NA 7 .   ? -5.543  -12.606 -13.083 1.00 28.94 ? 708  HOH A O   1 
HETATM 6693 O  O   . HOH NA 7 .   ? -28.602 -17.377 -11.716 1.00 14.23 ? 709  HOH A O   1 
HETATM 6694 O  O   . HOH NA 7 .   ? -20.814 -26.945 -4.834  1.00 29.55 ? 710  HOH A O   1 
HETATM 6695 O  O   . HOH NA 7 .   ? -35.731 -10.538 6.792   1.00 26.49 ? 711  HOH A O   1 
HETATM 6696 O  O   . HOH NA 7 .   ? -34.895 -6.746  -27.179 1.00 33.49 ? 712  HOH A O   1 
HETATM 6697 O  O   . HOH NA 7 .   ? -12.989 5.941   -2.759  1.00 36.30 ? 713  HOH A O   1 
HETATM 6698 O  O   . HOH NA 7 .   ? -11.972 2.645   -7.723  1.00 18.08 ? 714  HOH A O   1 
HETATM 6699 O  O   . HOH NA 7 .   ? -6.700  -8.220  -2.825  1.00 15.43 ? 715  HOH A O   1 
HETATM 6700 O  O   . HOH NA 7 .   ? -4.368  -11.475 3.522   1.00 15.82 ? 716  HOH A O   1 
HETATM 6701 O  O   . HOH NA 7 .   ? -18.209 -15.653 -20.521 1.00 25.69 ? 717  HOH A O   1 
HETATM 6702 O  O   . HOH NA 7 .   ? -45.793 1.334   -20.985 1.00 40.55 ? 718  HOH A O   1 
HETATM 6703 O  O   . HOH NA 7 .   ? -20.884 -12.229 -19.431 1.00 14.26 ? 719  HOH A O   1 
HETATM 6704 O  O   . HOH NA 7 .   ? -8.922  0.283   -10.336 1.00 43.82 ? 720  HOH A O   1 
HETATM 6705 O  O   . HOH NA 7 .   ? -44.486 -19.282 -9.729  1.00 25.67 ? 721  HOH A O   1 
HETATM 6706 O  O   . HOH NA 7 .   ? -4.816  0.197   -9.539  1.00 34.88 ? 722  HOH A O   1 
HETATM 6707 O  O   . HOH NA 7 .   ? -21.330 -4.034  25.224  1.00 28.54 ? 723  HOH A O   1 
HETATM 6708 O  O   . HOH NA 7 .   ? -6.492  1.789   12.914  1.00 37.31 ? 724  HOH A O   1 
HETATM 6709 O  O   . HOH NA 7 .   ? -34.573 -4.090  0.892   1.00 14.89 ? 725  HOH A O   1 
HETATM 6710 O  O   . HOH NA 7 .   ? -27.316 -12.269 -16.588 1.00 14.60 ? 726  HOH A O   1 
HETATM 6711 O  O   . HOH NA 7 .   ? -21.004 -32.434 20.207  1.00 31.76 ? 727  HOH A O   1 
HETATM 6712 O  O   . HOH NA 7 .   ? -41.392 -13.521 -19.273 1.00 37.62 ? 728  HOH A O   1 
HETATM 6713 O  O   . HOH NA 7 .   ? -33.243 -8.849  15.745  1.00 21.64 ? 729  HOH A O   1 
HETATM 6714 O  O   . HOH NA 7 .   ? -13.912 -10.837 -14.165 1.00 15.67 ? 730  HOH A O   1 
HETATM 6715 O  O   . HOH NA 7 .   ? -31.798 -12.130 21.274  1.00 17.57 ? 731  HOH A O   1 
HETATM 6716 O  O   . HOH NA 7 .   ? -22.113 -35.281 18.497  1.00 42.32 ? 732  HOH A O   1 
HETATM 6717 O  O   . HOH NA 7 .   ? -37.009 -1.498  -25.076 1.00 22.27 ? 733  HOH A O   1 
HETATM 6718 O  O   . HOH NA 7 .   ? -24.876 -11.923 -24.580 1.00 24.74 ? 734  HOH A O   1 
HETATM 6719 O  O   . HOH NA 7 .   ? -29.615 -1.644  -0.761  1.00 11.34 ? 735  HOH A O   1 
HETATM 6720 O  O   . HOH NA 7 .   ? -42.413 -13.502 14.729  1.00 22.77 ? 736  HOH A O   1 
HETATM 6721 O  O   . HOH NA 7 .   ? -24.611 -29.569 15.838  1.00 30.13 ? 737  HOH A O   1 
HETATM 6722 O  O   . HOH NA 7 .   ? -26.403 -17.998 35.314  1.00 38.49 ? 738  HOH A O   1 
HETATM 6723 O  O   . HOH NA 7 .   ? -6.358  -18.069 -12.293 1.00 33.69 ? 739  HOH A O   1 
HETATM 6724 O  O   . HOH NA 7 .   ? -31.254 -21.040 -2.136  1.00 15.68 ? 740  HOH A O   1 
HETATM 6725 O  O   . HOH NA 7 .   ? -37.114 -30.201 14.998  1.00 27.48 ? 741  HOH A O   1 
HETATM 6726 O  O   . HOH NA 7 .   ? -16.759 -15.445 -10.898 1.00 16.11 ? 742  HOH A O   1 
HETATM 6727 O  O   . HOH NA 7 .   ? -20.213 -18.824 30.253  1.00 32.73 ? 743  HOH A O   1 
HETATM 6728 O  O   . HOH NA 7 .   ? -18.211 6.844   -8.295  1.00 44.06 ? 744  HOH A O   1 
HETATM 6729 O  O   . HOH NA 7 .   ? -26.688 -20.869 -11.850 1.00 36.38 ? 745  HOH A O   1 
HETATM 6730 O  O   . HOH NA 7 .   ? -22.412 -1.379  7.609   1.00 24.80 ? 746  HOH A O   1 
HETATM 6731 O  O   . HOH NA 7 .   ? -32.191 -22.484 -14.614 1.00 29.48 ? 747  HOH A O   1 
HETATM 6732 O  O   . HOH NA 7 .   ? -24.003 5.172   -10.868 1.00 22.15 ? 748  HOH A O   1 
HETATM 6733 O  O   . HOH NA 7 .   ? -12.580 -33.417 7.267   1.00 41.45 ? 749  HOH A O   1 
HETATM 6734 O  O   . HOH NA 7 .   ? -4.500  -11.394 18.756  1.00 35.82 ? 750  HOH A O   1 
HETATM 6735 O  O   . HOH NA 7 .   ? -10.202 -13.444 -8.127  1.00 14.09 ? 751  HOH A O   1 
HETATM 6736 O  O   . HOH NA 7 .   ? -14.082 -1.663  20.384  1.00 19.84 ? 752  HOH A O   1 
HETATM 6737 O  O   . HOH NA 7 .   ? -14.120 -10.214 5.080   1.00 12.24 ? 753  HOH A O   1 
HETATM 6738 O  O   . HOH NA 7 .   ? -27.682 -19.749 -8.212  1.00 14.53 ? 754  HOH A O   1 
HETATM 6739 O  O   . HOH NA 7 .   ? -35.112 -14.149 -26.095 1.00 26.38 ? 755  HOH A O   1 
HETATM 6740 O  O   . HOH NA 7 .   ? -28.970 -27.849 8.403   1.00 13.32 ? 756  HOH A O   1 
HETATM 6741 O  O   . HOH NA 7 .   ? -20.409 3.399   -11.000 1.00 31.76 ? 757  HOH A O   1 
HETATM 6742 O  O   . HOH NA 7 .   ? -28.367 -22.265 -1.331  1.00 13.67 ? 758  HOH A O   1 
HETATM 6743 O  O   . HOH NA 7 .   ? -28.208 -30.961 13.741  1.00 33.11 ? 759  HOH A O   1 
HETATM 6744 O  O   . HOH NA 7 .   ? -23.367 5.864   -17.261 1.00 33.80 ? 760  HOH A O   1 
HETATM 6745 O  O   . HOH NA 7 .   ? -39.083 15.127  -4.645  1.00 23.49 ? 761  HOH A O   1 
HETATM 6746 O  O   . HOH NA 7 .   ? -10.710 1.539   -12.197 1.00 26.39 ? 762  HOH A O   1 
HETATM 6747 O  O   . HOH NA 7 .   ? -31.672 -2.213  1.715   1.00 15.73 ? 763  HOH A O   1 
HETATM 6748 O  O   . HOH NA 7 .   ? -19.795 -21.918 31.422  1.00 35.66 ? 764  HOH A O   1 
HETATM 6749 O  O   . HOH NA 7 .   ? -11.383 -31.926 18.161  1.00 45.42 ? 765  HOH A O   1 
HETATM 6750 O  O   . HOH NA 7 .   ? -11.173 2.556   5.984   1.00 18.11 ? 766  HOH A O   1 
HETATM 6751 O  O   . HOH NA 7 .   ? -30.910 -21.956 30.965  1.00 40.84 ? 767  HOH A O   1 
HETATM 6752 O  O   . HOH NA 7 .   ? -17.408 -7.920  -0.500  1.00 12.41 ? 768  HOH A O   1 
HETATM 6753 O  O   . HOH NA 7 .   ? -25.737 -3.234  11.893  1.00 34.29 ? 769  HOH A O   1 
HETATM 6754 O  O   . HOH NA 7 .   ? -34.507 -25.458 1.283   1.00 24.51 ? 770  HOH A O   1 
HETATM 6755 O  O   . HOH NA 7 .   ? -37.026 -13.195 10.668  1.00 14.64 ? 771  HOH A O   1 
HETATM 6756 O  O   . HOH NA 7 .   ? -10.954 -4.708  26.717  1.00 14.07 ? 772  HOH A O   1 
HETATM 6757 O  O   . HOH NA 7 .   ? -8.704  -10.220 15.621  1.00 11.11 ? 773  HOH A O   1 
HETATM 6758 O  O   . HOH NA 7 .   ? -41.467 -22.903 -9.922  1.00 21.01 ? 774  HOH A O   1 
HETATM 6759 O  O   . HOH NA 7 .   ? -6.111  -1.800  -11.316 1.00 33.79 ? 775  HOH A O   1 
HETATM 6760 O  O   . HOH NA 7 .   ? -32.471 -10.543 -27.750 1.00 32.81 ? 776  HOH A O   1 
HETATM 6761 O  O   . HOH NA 7 .   ? -14.337 -11.185 -16.804 1.00 19.53 ? 777  HOH A O   1 
HETATM 6762 O  O   . HOH NA 7 .   ? -18.565 -5.400  -0.694  1.00 16.78 ? 778  HOH A O   1 
HETATM 6763 O  O   . HOH NA 7 .   ? -30.400 4.712   3.286   1.00 39.36 ? 779  HOH A O   1 
HETATM 6764 O  O   . HOH NA 7 .   ? -35.897 -9.751  9.708   1.00 19.38 ? 780  HOH A O   1 
HETATM 6765 O  O   . HOH NA 7 .   ? -26.662 4.782   -0.305  1.00 44.56 ? 781  HOH A O   1 
HETATM 6766 O  O   . HOH NA 7 .   ? -44.226 12.574  -23.300 1.00 48.21 ? 782  HOH A O   1 
HETATM 6767 O  O   . HOH NA 7 .   ? -12.891 -6.137  28.220  1.00 21.12 ? 783  HOH A O   1 
HETATM 6768 O  O   . HOH NA 7 .   ? -17.353 3.103   2.011   1.00 15.23 ? 784  HOH A O   1 
HETATM 6769 O  O   . HOH NA 7 .   ? -47.442 -5.846  -12.551 1.00 32.27 ? 785  HOH A O   1 
HETATM 6770 O  O   . HOH NA 7 .   ? -7.573  2.664   9.488   1.00 48.28 ? 786  HOH A O   1 
HETATM 6771 O  O   . HOH NA 7 .   ? -21.393 -25.263 -2.659  1.00 37.93 ? 787  HOH A O   1 
HETATM 6772 O  O   . HOH NA 7 .   ? -37.467 -17.073 -18.729 1.00 28.17 ? 788  HOH A O   1 
HETATM 6773 O  O   . HOH NA 7 .   ? -28.690 -22.021 -8.761  1.00 24.97 ? 789  HOH A O   1 
HETATM 6774 O  O   . HOH NA 7 .   ? -13.732 -31.938 17.017  1.00 41.36 ? 790  HOH A O   1 
HETATM 6775 O  O   . HOH NA 7 .   ? -7.315  1.612   6.039   1.00 25.61 ? 791  HOH A O   1 
HETATM 6776 O  O   . HOH NA 7 .   ? -35.223 -4.153  -4.636  1.00 12.12 ? 792  HOH A O   1 
HETATM 6777 O  O   . HOH NA 7 .   ? -30.951 8.063   -17.238 1.00 19.78 ? 793  HOH A O   1 
HETATM 6778 O  O   . HOH NA 7 .   ? -4.763  -22.874 7.930   1.00 20.99 ? 794  HOH A O   1 
HETATM 6779 O  O   . HOH NA 7 .   ? -12.376 -20.743 30.790  1.00 25.74 ? 795  HOH A O   1 
HETATM 6780 O  O   . HOH NA 7 .   ? -18.224 -18.794 14.641  1.00 10.58 ? 796  HOH A O   1 
HETATM 6781 O  O   . HOH NA 7 .   ? -23.038 -7.495  3.981   1.00 13.43 ? 797  HOH A O   1 
HETATM 6782 O  O   . HOH NA 7 .   ? -29.080 -16.293 -21.744 1.00 23.58 ? 798  HOH A O   1 
HETATM 6783 O  O   . HOH NA 7 .   ? -23.404 -19.031 15.380  1.00 11.75 ? 799  HOH A O   1 
HETATM 6784 O  O   . HOH NA 7 .   ? -14.439 -14.007 -0.268  1.00 11.96 ? 800  HOH A O   1 
HETATM 6785 O  O   . HOH NA 7 .   ? -36.679 8.204   -2.600  1.00 35.19 ? 801  HOH A O   1 
HETATM 6786 O  O   . HOH NA 7 .   ? -14.812 -38.063 27.983  1.00 35.70 ? 802  HOH A O   1 
HETATM 6787 O  O   . HOH NA 7 .   ? -26.179 -23.718 1.639   1.00 14.96 ? 803  HOH A O   1 
HETATM 6788 O  O   . HOH NA 7 .   ? -39.155 -24.250 23.834  1.00 33.81 ? 804  HOH A O   1 
HETATM 6789 O  O   . HOH NA 7 .   ? -34.434 -19.562 31.458  1.00 49.12 ? 805  HOH A O   1 
HETATM 6790 O  O   . HOH NA 7 .   ? -17.587 6.213   5.387   1.00 46.56 ? 806  HOH A O   1 
HETATM 6791 O  O   . HOH NA 7 .   ? -3.327  -14.341 -2.632  1.00 37.62 ? 807  HOH A O   1 
HETATM 6792 O  O   . HOH NA 7 .   ? -18.987 -23.068 3.972   1.00 30.24 ? 808  HOH A O   1 
HETATM 6793 O  O   . HOH NA 7 .   ? -16.517 -11.220 -11.377 1.00 12.60 ? 809  HOH A O   1 
HETATM 6794 O  O   . HOH NA 7 .   ? -30.185 -19.710 -20.436 1.00 27.64 ? 810  HOH A O   1 
HETATM 6795 O  O   . HOH NA 7 .   ? -44.203 10.000  -14.278 1.00 15.02 ? 811  HOH A O   1 
HETATM 6796 O  O   . HOH NA 7 .   ? -30.828 9.183   -24.324 1.00 26.20 ? 812  HOH A O   1 
HETATM 6797 O  O   . HOH NA 7 .   ? -2.683  -0.719  3.155   1.00 40.00 ? 813  HOH A O   1 
HETATM 6798 O  O   . HOH NA 7 .   ? -29.896 -11.872 26.367  1.00 30.18 ? 814  HOH A O   1 
HETATM 6799 O  O   . HOH NA 7 .   ? -28.259 -17.137 -8.993  1.00 11.53 ? 815  HOH A O   1 
HETATM 6800 O  O   . HOH NA 7 .   ? -35.483 -18.331 -3.866  1.00 14.32 ? 816  HOH A O   1 
HETATM 6801 O  O   . HOH NA 7 .   ? -10.543 0.920   -14.785 1.00 37.16 ? 817  HOH A O   1 
HETATM 6802 O  O   . HOH NA 7 .   ? -14.091 2.043   14.093  1.00 21.96 ? 818  HOH A O   1 
HETATM 6803 O  O   . HOH NA 7 .   ? -43.242 -13.613 -9.338  1.00 26.00 ? 819  HOH A O   1 
HETATM 6804 O  O   . HOH NA 7 .   ? -43.453 -16.387 6.517   1.00 35.65 ? 820  HOH A O   1 
HETATM 6805 O  O   . HOH NA 7 .   ? -30.254 -29.729 24.065  1.00 30.17 ? 821  HOH A O   1 
HETATM 6806 O  O   . HOH NA 7 .   ? -17.649 -26.177 -10.544 1.00 28.09 ? 822  HOH A O   1 
HETATM 6807 O  O   . HOH NA 7 .   ? -24.833 -13.641 31.028  1.00 27.32 ? 823  HOH A O   1 
HETATM 6808 O  O   . HOH NA 7 .   ? -36.785 -15.018 -11.329 1.00 12.78 ? 824  HOH A O   1 
HETATM 6809 O  O   . HOH NA 7 .   ? -37.801 -6.790  -4.326  1.00 24.89 ? 825  HOH A O   1 
HETATM 6810 O  O   . HOH NA 7 .   ? -29.883 -6.771  17.508  1.00 38.84 ? 826  HOH A O   1 
HETATM 6811 O  O   . HOH NA 7 .   ? -2.551  -12.695 10.594  1.00 45.20 ? 827  HOH A O   1 
HETATM 6812 O  O   . HOH NA 7 .   ? -27.047 2.305   -9.325  1.00 12.01 ? 828  HOH A O   1 
HETATM 6813 O  O   . HOH NA 7 .   ? -40.906 -29.544 17.854  1.00 35.81 ? 829  HOH A O   1 
HETATM 6814 O  O   . HOH NA 7 .   ? -23.402 -31.135 26.710  1.00 26.51 ? 830  HOH A O   1 
HETATM 6815 O  O   . HOH NA 7 .   ? -35.292 -7.143  -5.109  1.00 10.84 ? 831  HOH A O   1 
HETATM 6816 O  O   . HOH NA 7 .   ? -37.004 -23.700 -5.557  1.00 29.95 ? 832  HOH A O   1 
HETATM 6817 O  O   . HOH NA 7 .   ? -7.862  6.616   9.550   1.00 43.92 ? 833  HOH A O   1 
HETATM 6818 O  O   . HOH NA 7 .   ? -21.484 -19.471 -14.649 1.00 30.58 ? 834  HOH A O   1 
HETATM 6819 O  O   . HOH NA 7 .   ? -46.304 -3.255  -18.528 1.00 33.53 ? 835  HOH A O   1 
HETATM 6820 O  O   . HOH NA 7 .   ? -45.189 -5.063  -5.763  1.00 26.99 ? 836  HOH A O   1 
HETATM 6821 O  O   . HOH NA 7 .   ? -30.033 -25.883 29.643  1.00 42.91 ? 837  HOH A O   1 
HETATM 6822 O  O   . HOH NA 7 .   ? -2.618  -25.273 15.331  1.00 22.58 ? 838  HOH A O   1 
HETATM 6823 O  O   . HOH NA 7 .   ? -20.276 3.275   -21.149 1.00 36.07 ? 839  HOH A O   1 
HETATM 6824 O  O   . HOH NA 7 .   ? -29.507 -23.054 2.598   1.00 13.05 ? 840  HOH A O   1 
HETATM 6825 O  O   A HOH NA 7 .   ? -48.636 7.971   -16.545 0.70 12.98 ? 841  HOH A O   1 
HETATM 6826 O  O   B HOH NA 7 .   ? -48.383 8.039   -14.533 0.30 6.20  ? 841  HOH A O   1 
HETATM 6827 O  O   . HOH NA 7 .   ? -8.564  -18.033 11.176  1.00 12.74 ? 842  HOH A O   1 
HETATM 6828 O  O   . HOH NA 7 .   ? -33.523 -26.860 27.797  1.00 31.37 ? 843  HOH A O   1 
HETATM 6829 O  O   . HOH NA 7 .   ? -41.238 -0.088  -25.030 1.00 41.12 ? 844  HOH A O   1 
HETATM 6830 O  O   . HOH NA 7 .   ? -42.364 -10.046 15.574  1.00 28.70 ? 845  HOH A O   1 
HETATM 6831 O  O   . HOH NA 7 .   ? -4.245  -10.707 -13.651 1.00 40.04 ? 846  HOH A O   1 
HETATM 6832 O  O   . HOH NA 7 .   ? -8.501  -8.370  -19.124 1.00 36.44 ? 847  HOH A O   1 
HETATM 6833 O  O   . HOH NA 7 .   ? -38.695 16.262  -11.565 1.00 36.44 ? 848  HOH A O   1 
HETATM 6834 O  O   . HOH NA 7 .   ? -42.004 -10.669 -13.395 1.00 33.61 ? 849  HOH A O   1 
HETATM 6835 O  O   . HOH NA 7 .   ? -33.562 -9.063  8.423   1.00 14.99 ? 850  HOH A O   1 
HETATM 6836 O  O   . HOH NA 7 .   ? -45.820 7.794   -14.140 1.00 23.56 ? 851  HOH A O   1 
HETATM 6837 O  O   . HOH NA 7 .   ? 1.183   -17.732 13.531  1.00 30.03 ? 852  HOH A O   1 
HETATM 6838 O  O   . HOH NA 7 .   ? -5.737  -15.917 -8.630  1.00 38.36 ? 853  HOH A O   1 
HETATM 6839 O  O   . HOH NA 7 .   ? -39.663 -12.231 4.138   1.00 25.71 ? 854  HOH A O   1 
HETATM 6840 O  O   . HOH NA 7 .   ? -21.794 3.368   -15.023 1.00 17.41 ? 855  HOH A O   1 
HETATM 6841 O  O   . HOH NA 7 .   ? -12.018 -4.830  -19.569 1.00 30.79 ? 856  HOH A O   1 
HETATM 6842 O  O   . HOH NA 7 .   ? -29.917 -18.654 30.395  1.00 38.02 ? 857  HOH A O   1 
HETATM 6843 O  O   . HOH NA 7 .   ? -7.751  -11.099 27.614  1.00 42.87 ? 858  HOH A O   1 
HETATM 6844 O  O   . HOH NA 7 .   ? -24.726 -31.325 19.404  1.00 34.77 ? 859  HOH A O   1 
HETATM 6845 O  O   . HOH NA 7 .   ? -42.680 -12.326 10.842  1.00 35.12 ? 860  HOH A O   1 
HETATM 6846 O  O   . HOH NA 7 .   ? -23.154 -21.081 -12.498 1.00 29.71 ? 861  HOH A O   1 
HETATM 6847 O  O   . HOH NA 7 .   ? -2.881  -12.511 13.788  1.00 36.28 ? 862  HOH A O   1 
HETATM 6848 O  O   . HOH NA 7 .   ? -18.573 -1.908  17.281  1.00 28.42 ? 863  HOH A O   1 
HETATM 6849 O  O   . HOH NA 7 .   ? -42.428 -16.138 -8.274  1.00 22.90 ? 864  HOH A O   1 
HETATM 6850 O  O   . HOH NA 7 .   ? -6.861  -22.326 19.180  1.00 21.82 ? 865  HOH A O   1 
HETATM 6851 O  O   . HOH NA 7 .   ? -14.335 -18.239 -12.836 1.00 23.90 ? 866  HOH A O   1 
HETATM 6852 O  O   . HOH NA 7 .   ? -33.834 8.698   -27.898 1.00 29.57 ? 867  HOH A O   1 
HETATM 6853 O  O   . HOH NA 7 .   ? -14.499 -9.639  -19.086 1.00 33.87 ? 868  HOH A O   1 
HETATM 6854 O  O   . HOH NA 7 .   ? -6.433  -0.200  24.282  1.00 45.98 ? 869  HOH A O   1 
HETATM 6855 O  O   . HOH NA 7 .   ? -46.764 -20.097 12.149  1.00 34.05 ? 870  HOH A O   1 
HETATM 6856 O  O   . HOH NA 7 .   ? -41.258 4.895   -25.561 1.00 33.12 ? 871  HOH A O   1 
HETATM 6857 O  O   . HOH NA 7 .   ? -35.575 2.203   6.254   1.00 29.69 ? 872  HOH A O   1 
HETATM 6858 O  O   . HOH NA 7 .   ? -17.569 -13.360 32.582  1.00 43.82 ? 873  HOH A O   1 
HETATM 6859 O  O   . HOH NA 7 .   ? -24.099 -11.578 6.760   1.00 12.00 ? 874  HOH A O   1 
HETATM 6860 O  O   . HOH NA 7 .   ? -42.154 2.032   -22.574 1.00 28.03 ? 875  HOH A O   1 
HETATM 6861 O  O   . HOH NA 7 .   ? -19.872 0.329   -12.095 1.00 17.68 ? 876  HOH A O   1 
HETATM 6862 O  O   . HOH NA 7 .   ? -9.610  2.959   18.077  1.00 37.65 ? 877  HOH A O   1 
HETATM 6863 O  O   . HOH NA 7 .   ? -33.130 10.272  -1.138  1.00 33.69 ? 878  HOH A O   1 
HETATM 6864 O  O   . HOH NA 7 .   ? -33.258 10.154  -23.798 1.00 36.72 ? 879  HOH A O   1 
HETATM 6865 O  O   . HOH NA 7 .   ? -22.301 -16.993 -6.943  1.00 13.72 ? 880  HOH A O   1 
HETATM 6866 O  O   . HOH NA 7 .   ? -4.956  -13.071 15.440  1.00 19.68 ? 881  HOH A O   1 
HETATM 6867 O  O   . HOH NA 7 .   ? -12.494 -12.929 -1.904  1.00 11.23 ? 882  HOH A O   1 
HETATM 6868 O  O   . HOH NA 7 .   ? -25.142 -21.816 34.618  1.00 36.98 ? 883  HOH A O   1 
HETATM 6869 O  O   A HOH NA 7 .   ? -17.624 -5.051  -19.015 0.90 23.08 ? 884  HOH A O   1 
HETATM 6870 O  O   B HOH NA 7 .   ? -18.862 -5.269  -20.467 0.10 0.50  ? 884  HOH A O   1 
HETATM 6871 O  O   . HOH NA 7 .   ? -48.352 2.229   -13.265 1.00 13.04 ? 885  HOH A O   1 
HETATM 6872 O  O   . HOH NA 7 .   ? -21.231 -1.241  14.386  1.00 44.77 ? 886  HOH A O   1 
HETATM 6873 O  O   . HOH NA 7 .   ? -8.699  -26.134 8.010   1.00 42.92 ? 887  HOH A O   1 
HETATM 6874 O  O   . HOH NA 7 .   ? -33.538 -14.958 24.296  1.00 22.84 ? 888  HOH A O   1 
HETATM 6875 O  O   . HOH NA 7 .   ? -36.298 -16.414 25.318  1.00 40.96 ? 889  HOH A O   1 
HETATM 6876 O  O   . HOH NA 7 .   ? -8.265  -20.687 27.258  1.00 32.72 ? 890  HOH A O   1 
HETATM 6877 O  O   . HOH NA 7 .   ? -42.094 -22.932 9.342   1.00 21.40 ? 891  HOH A O   1 
HETATM 6878 O  O   . HOH NA 7 .   ? -1.865  -8.836  -10.454 1.00 23.42 ? 892  HOH A O   1 
HETATM 6879 O  O   . HOH NA 7 .   ? -37.893 -23.932 2.743   1.00 34.24 ? 893  HOH A O   1 
HETATM 6880 O  O   . HOH NA 7 .   ? -1.097  -18.516 15.959  1.00 23.89 ? 894  HOH A O   1 
HETATM 6881 O  O   . HOH NA 7 .   ? -4.929  -3.033  -3.620  1.00 14.80 ? 895  HOH A O   1 
HETATM 6882 O  O   . HOH NA 7 .   ? 1.200   -21.411 15.949  1.00 42.37 ? 896  HOH A O   1 
HETATM 6883 O  O   . HOH NA 7 .   ? -39.648 -16.798 -20.549 1.00 42.55 ? 897  HOH A O   1 
HETATM 6884 O  O   . HOH NA 7 .   ? -15.923 -26.900 31.589  1.00 36.02 ? 898  HOH A O   1 
HETATM 6885 O  O   . HOH NA 7 .   ? -15.890 -29.597 27.320  1.00 24.98 ? 899  HOH A O   1 
HETATM 6886 O  O   A HOH NA 7 .   ? -6.729  3.346   1.143   0.50 16.53 ? 900  HOH A O   1 
HETATM 6887 O  O   B HOH NA 7 .   ? -5.528  1.498   2.026   0.50 9.16  ? 900  HOH A O   1 
HETATM 6888 O  O   . HOH NA 7 .   ? -7.689  -27.287 28.334  1.00 32.51 ? 901  HOH A O   1 
HETATM 6889 O  O   . HOH NA 7 .   ? -1.636  -15.280 16.109  1.00 41.70 ? 902  HOH A O   1 
HETATM 6890 O  O   . HOH NA 7 .   ? -27.295 9.537   -5.581  1.00 33.43 ? 903  HOH A O   1 
HETATM 6891 O  O   . HOH NA 7 .   ? -37.357 -11.772 22.123  1.00 36.94 ? 904  HOH A O   1 
HETATM 6892 O  O   . HOH NA 7 .   ? -31.606 -24.568 1.070   1.00 18.47 ? 905  HOH A O   1 
HETATM 6893 O  O   . HOH NA 7 .   ? -16.628 1.985   -17.181 1.00 28.23 ? 906  HOH A O   1 
HETATM 6894 O  O   . HOH NA 7 .   ? -40.123 -4.731  -21.525 1.00 27.14 ? 907  HOH A O   1 
HETATM 6895 O  O   . HOH NA 7 .   ? -24.938 -17.433 -20.811 1.00 19.93 ? 908  HOH A O   1 
HETATM 6896 O  O   . HOH NA 7 .   ? -3.105  -8.672  -16.085 1.00 42.84 ? 909  HOH A O   1 
HETATM 6897 O  O   . HOH NA 7 .   ? -25.086 -25.459 29.047  1.00 38.08 ? 910  HOH A O   1 
HETATM 6898 O  O   . HOH NA 7 .   ? -26.985 -6.671  -24.004 1.00 23.59 ? 911  HOH A O   1 
HETATM 6899 O  O   . HOH NA 7 .   ? -3.691  -1.825  -7.968  1.00 23.45 ? 912  HOH A O   1 
HETATM 6900 O  O   . HOH NA 7 .   ? -8.513  5.530   -4.674  1.00 38.88 ? 913  HOH A O   1 
HETATM 6901 O  O   . HOH NA 7 .   ? -27.338 -29.739 20.613  1.00 20.15 ? 914  HOH A O   1 
HETATM 6902 O  O   . HOH NA 7 .   ? -36.361 -6.676  8.032   1.00 36.31 ? 915  HOH A O   1 
HETATM 6903 O  O   . HOH NA 7 .   ? -54.047 1.430   -18.449 1.00 49.34 ? 916  HOH A O   1 
HETATM 6904 O  O   . HOH NA 7 .   ? -21.414 -15.487 -4.654  1.00 13.18 ? 917  HOH A O   1 
HETATM 6905 O  O   . HOH NA 7 .   ? -29.621 6.729   0.638   1.00 24.66 ? 918  HOH A O   1 
HETATM 6906 O  O   . HOH NA 7 .   ? -0.052  -9.091  1.811   1.00 20.36 ? 919  HOH A O   1 
HETATM 6907 O  O   . HOH NA 7 .   ? -8.679  -2.346  -11.718 1.00 16.09 ? 920  HOH A O   1 
HETATM 6908 O  O   . HOH NA 7 .   ? -41.260 -7.704  -0.981  1.00 39.94 ? 921  HOH A O   1 
HETATM 6909 O  O   . HOH NA 7 .   ? -9.117  -4.355  -13.928 1.00 24.51 ? 922  HOH A O   1 
HETATM 6910 O  O   . HOH NA 7 .   ? -6.969  -10.179 25.278  1.00 35.15 ? 923  HOH A O   1 
HETATM 6911 O  O   . HOH NA 7 .   ? -39.701 5.603   -2.366  1.00 28.37 ? 924  HOH A O   1 
HETATM 6912 O  O   . HOH NA 7 .   ? -27.245 4.792   -8.463  1.00 11.80 ? 925  HOH A O   1 
HETATM 6913 O  O   . HOH NA 7 .   ? -9.817  -31.559 25.953  1.00 32.07 ? 926  HOH A O   1 
HETATM 6914 O  O   . HOH NA 7 .   ? -25.360 -5.675  -25.773 1.00 33.67 ? 927  HOH A O   1 
HETATM 6915 O  O   . HOH NA 7 .   ? 0.095   -16.046 10.368  1.00 37.01 ? 928  HOH A O   1 
HETATM 6916 O  O   . HOH NA 7 .   ? -11.711 5.406   2.419   1.00 33.79 ? 929  HOH A O   1 
HETATM 6917 O  O   . HOH NA 7 .   ? -38.306 3.935   3.554   1.00 38.87 ? 930  HOH A O   1 
HETATM 6918 O  O   . HOH NA 7 .   ? -19.835 -5.621  30.860  1.00 44.63 ? 931  HOH A O   1 
HETATM 6919 O  O   . HOH NA 7 .   ? -32.326 16.609  -8.341  1.00 37.97 ? 932  HOH A O   1 
HETATM 6920 O  O   . HOH NA 7 .   ? -39.237 8.119   1.821   1.00 33.68 ? 933  HOH A O   1 
HETATM 6921 O  O   . HOH NA 7 .   ? -5.672  1.830   16.401  1.00 33.82 ? 934  HOH A O   1 
HETATM 6922 O  O   . HOH NA 7 .   ? -6.012  -7.412  19.010  1.00 30.99 ? 935  HOH A O   1 
HETATM 6923 O  O   . HOH NA 7 .   ? -2.908  1.213   -6.596  1.00 43.38 ? 936  HOH A O   1 
HETATM 6924 O  O   . HOH NA 7 .   ? -37.697 -23.744 30.128  1.00 35.77 ? 937  HOH A O   1 
HETATM 6925 O  O   . HOH NA 7 .   ? -7.679  -20.275 -4.517  1.00 22.48 ? 938  HOH A O   1 
HETATM 6926 O  O   . HOH NA 7 .   ? -25.636 -20.651 -17.283 1.00 37.83 ? 939  HOH A O   1 
HETATM 6927 O  O   . HOH NA 7 .   ? -6.248  -17.122 25.183  1.00 45.67 ? 940  HOH A O   1 
HETATM 6928 O  O   . HOH NA 7 .   ? -38.093 3.732   -26.495 1.00 44.24 ? 941  HOH A O   1 
HETATM 6929 O  O   . HOH NA 7 .   ? -47.470 -2.817  -3.041  1.00 36.50 ? 942  HOH A O   1 
HETATM 6930 O  O   . HOH NA 7 .   ? -19.821 1.519   12.587  1.00 42.18 ? 943  HOH A O   1 
HETATM 6931 O  O   . HOH NA 7 .   ? -11.371 -11.553 -21.559 1.00 44.33 ? 944  HOH A O   1 
HETATM 6932 O  O   . HOH NA 7 .   ? -37.994 -22.840 -2.206  1.00 37.82 ? 945  HOH A O   1 
HETATM 6933 O  O   . HOH NA 7 .   ? -29.777 11.574  -12.675 1.00 44.12 ? 946  HOH A O   1 
HETATM 6934 O  O   . HOH NA 7 .   ? -3.734  -14.925 17.309  1.00 38.49 ? 947  HOH A O   1 
HETATM 6935 O  O   . HOH NA 7 .   ? -19.945 1.531   10.185  1.00 32.17 ? 948  HOH A O   1 
HETATM 6936 O  O   . HOH NA 7 .   ? -33.213 1.040   5.873   1.00 30.69 ? 949  HOH A O   1 
HETATM 6937 O  O   . HOH NA 7 .   ? -41.417 -11.849 -1.018  1.00 32.63 ? 950  HOH A O   1 
HETATM 6938 O  O   . HOH NA 7 .   ? -30.447 -24.453 -1.352  1.00 26.50 ? 951  HOH A O   1 
HETATM 6939 O  O   . HOH NA 7 .   ? -42.293 -10.093 -5.248  1.00 28.15 ? 952  HOH A O   1 
HETATM 6940 O  O   . HOH NA 7 .   ? -28.691 -20.609 31.823  1.00 44.05 ? 953  HOH A O   1 
HETATM 6941 O  O   . HOH NA 7 .   ? -39.618 -9.502  5.030   1.00 36.51 ? 954  HOH A O   1 
HETATM 6942 O  O   . HOH NA 7 .   ? -8.156  -30.980 9.305   1.00 32.36 ? 955  HOH A O   1 
HETATM 6943 O  O   . HOH NA 7 .   ? -7.817  -18.683 -6.727  1.00 26.08 ? 956  HOH A O   1 
HETATM 6944 O  O   . HOH NA 7 .   ? -14.704 3.109   -10.409 1.00 24.37 ? 957  HOH A O   1 
HETATM 6945 O  O   . HOH NA 7 .   ? -38.681 -8.110  -27.097 1.00 42.24 ? 958  HOH A O   1 
HETATM 6946 O  O   . HOH NA 7 .   ? -41.889 -5.757  2.959   1.00 42.96 ? 959  HOH A O   1 
HETATM 6947 O  O   . HOH NA 7 .   ? -10.600 -24.441 -14.345 1.00 39.15 ? 960  HOH A O   1 
HETATM 6948 O  O   . HOH NA 7 .   ? -32.610 -12.304 24.041  1.00 38.63 ? 961  HOH A O   1 
HETATM 6949 O  O   . HOH NA 7 .   ? -43.952 -21.071 -3.145  1.00 44.79 ? 962  HOH A O   1 
HETATM 6950 O  O   . HOH NA 7 .   ? -24.181 3.247   2.508   1.00 42.66 ? 963  HOH A O   1 
HETATM 6951 O  O   . HOH NA 7 .   ? -9.811  4.439   15.415  1.00 37.73 ? 964  HOH A O   1 
HETATM 6952 O  O   . HOH NA 7 .   ? -32.289 -30.083 20.099  1.00 36.33 ? 965  HOH A O   1 
HETATM 6953 O  O   . HOH NA 7 .   ? -44.259 -13.810 17.449  1.00 46.57 ? 966  HOH A O   1 
HETATM 6954 O  O   . HOH NA 7 .   ? -2.110  1.951   -3.120  1.00 36.81 ? 967  HOH A O   1 
HETATM 6955 O  O   . HOH NA 7 .   ? -22.308 5.496   -13.678 1.00 39.19 ? 968  HOH A O   1 
HETATM 6956 O  O   . HOH NA 7 .   ? -40.359 17.358  -9.422  1.00 38.30 ? 969  HOH A O   1 
HETATM 6957 O  O   . HOH NA 7 .   ? -6.526  -25.324 19.528  1.00 26.39 ? 970  HOH A O   1 
HETATM 6958 O  O   . HOH NA 7 .   ? -30.258 -17.902 -23.809 1.00 36.17 ? 971  HOH A O   1 
HETATM 6959 O  O   . HOH NA 7 .   ? -3.609  -21.328 1.845   1.00 47.58 ? 972  HOH A O   1 
HETATM 6960 O  O   . HOH NA 7 .   ? -26.412 -20.566 36.349  1.00 27.23 ? 973  HOH A O   1 
HETATM 6961 O  O   . HOH NA 7 .   ? -5.950  0.137   10.769  1.00 30.27 ? 974  HOH A O   1 
HETATM 6962 O  O   . HOH NA 7 .   ? -17.127 3.598   -11.157 1.00 29.24 ? 975  HOH A O   1 
HETATM 6963 O  O   . HOH NA 7 .   ? -43.849 -12.379 19.165  1.00 43.36 ? 976  HOH A O   1 
HETATM 6964 O  O   . HOH NA 7 .   ? -42.877 -21.821 25.695  1.00 39.05 ? 977  HOH A O   1 
HETATM 6965 O  O   . HOH NA 7 .   ? -23.877 7.585   -3.922  1.00 40.55 ? 978  HOH A O   1 
HETATM 6966 O  O   . HOH NA 7 .   ? -34.283 -8.967  -28.666 1.00 39.12 ? 979  HOH A O   1 
HETATM 6967 O  O   . HOH NA 7 .   ? -21.135 -11.075 -24.035 1.00 40.55 ? 980  HOH A O   1 
HETATM 6968 O  O   . HOH NA 7 .   ? -7.634  -34.414 16.295  1.00 44.91 ? 981  HOH A O   1 
HETATM 6969 O  O   . HOH NA 7 .   ? -19.796 -12.325 -21.941 1.00 35.12 ? 982  HOH A O   1 
HETATM 6970 O  O   . HOH NA 7 .   ? -9.851  -1.301  -13.861 1.00 45.09 ? 983  HOH A O   1 
HETATM 6971 O  O   . HOH NA 7 .   ? -40.647 16.275  -7.138  1.00 41.77 ? 984  HOH A O   1 
HETATM 6972 O  O   . HOH NA 7 .   ? -36.932 0.635   7.541   1.00 41.74 ? 985  HOH A O   1 
HETATM 6973 O  O   . HOH NA 7 .   ? -28.411 -31.504 22.391  1.00 45.94 ? 986  HOH A O   1 
HETATM 6974 O  O   . HOH NA 7 .   ? -47.383 -2.179  1.275   1.00 36.92 ? 987  HOH A O   1 
HETATM 6975 O  O   . HOH NA 7 .   ? -9.784  4.379   4.269   1.00 28.52 ? 988  HOH A O   1 
HETATM 6976 O  O   . HOH NA 7 .   ? -9.199  -32.901 10.975  1.00 36.45 ? 989  HOH A O   1 
HETATM 6977 O  O   . HOH NA 7 .   ? -28.214 -34.153 15.238  1.00 42.98 ? 990  HOH A O   1 
HETATM 6978 O  O   . HOH NA 7 .   ? -24.014 -19.378 -19.016 1.00 36.04 ? 991  HOH A O   1 
HETATM 6979 O  O   . HOH NA 7 .   ? -39.540 -16.159 22.986  1.00 41.73 ? 992  HOH A O   1 
HETATM 6980 O  O   . HOH NA 7 .   ? -43.548 -23.557 11.415  1.00 22.91 ? 993  HOH A O   1 
HETATM 6981 O  O   . HOH NA 7 .   ? -45.554 -16.865 4.777   1.00 43.65 ? 994  HOH A O   1 
HETATM 6982 O  O   . HOH NA 7 .   ? -25.421 -11.047 31.558  1.00 37.02 ? 995  HOH A O   1 
HETATM 6983 O  O   . HOH NA 7 .   ? -6.978  -18.663 26.857  1.00 33.56 ? 996  HOH A O   1 
HETATM 6984 O  O   . HOH NA 7 .   ? -26.901 -28.486 14.918  1.00 33.33 ? 997  HOH A O   1 
HETATM 6985 O  O   . HOH NA 7 .   ? -42.846 -7.222  -25.061 1.00 39.56 ? 998  HOH A O   1 
HETATM 6986 O  O   . HOH NA 7 .   ? -24.184 -3.337  13.923  1.00 46.95 ? 999  HOH A O   1 
HETATM 6987 O  O   . HOH NA 7 .   ? -31.883 -31.997 15.932  1.00 39.62 ? 1000 HOH A O   1 
HETATM 6988 O  O   . HOH NA 7 .   ? -36.531 17.314  -11.920 1.00 35.73 ? 1001 HOH A O   1 
HETATM 6989 O  O   . HOH NA 7 .   ? -42.855 -11.263 -22.727 1.00 43.27 ? 1002 HOH A O   1 
HETATM 6990 O  O   . HOH NA 7 .   ? -2.681  2.272   -0.557  1.00 42.12 ? 1003 HOH A O   1 
HETATM 6991 O  O   . HOH NA 7 .   ? -24.612 -33.586 26.183  1.00 39.97 ? 1004 HOH A O   1 
HETATM 6992 O  O   . HOH NA 7 .   ? -5.799  -10.474 16.249  1.00 30.20 ? 1005 HOH A O   1 
HETATM 6993 O  O   . HOH NA 7 .   ? -27.207 -33.146 25.578  1.00 48.11 ? 1006 HOH A O   1 
HETATM 6994 O  O   . HOH NA 7 .   ? -22.609 -26.643 29.531  1.00 43.73 ? 1007 HOH A O   1 
HETATM 6995 O  O   . HOH NA 7 .   ? -14.805 -24.834 3.774   1.00 41.52 ? 1008 HOH A O   1 
HETATM 6996 O  O   . HOH NA 7 .   ? -15.463 -35.983 30.599  1.00 27.08 ? 1009 HOH A O   1 
HETATM 6997 O  O   . HOH NA 7 .   ? -42.481 17.045  -10.974 1.00 32.97 ? 1010 HOH A O   1 
HETATM 6998 O  O   . HOH NA 7 .   ? -17.874 5.760   2.665   1.00 29.47 ? 1011 HOH A O   1 
HETATM 6999 O  O   . HOH NA 7 .   ? -8.942  -21.191 -11.267 1.00 34.44 ? 1012 HOH A O   1 
HETATM 7000 O  O   . HOH NA 7 .   ? -3.422  -1.527  -5.613  1.00 16.94 ? 1013 HOH A O   1 
HETATM 7001 O  O   . HOH NA 7 .   ? -36.110 -25.533 -7.130  1.00 42.99 ? 1014 HOH A O   1 
HETATM 7002 O  O   . HOH NA 7 .   ? -20.921 6.985   2.345   1.00 43.46 ? 1015 HOH A O   1 
HETATM 7003 O  O   . HOH NA 7 .   ? -25.856 6.907   -9.418  1.00 24.67 ? 1016 HOH A O   1 
HETATM 7004 O  O   . HOH NA 7 .   ? -14.688 -19.807 -14.893 1.00 32.29 ? 1017 HOH A O   1 
HETATM 7005 O  O   . HOH NA 7 .   ? -28.613 9.021   -18.464 1.00 23.26 ? 1018 HOH A O   1 
HETATM 7006 O  O   . HOH NA 7 .   ? -12.792 -26.565 4.034   1.00 36.50 ? 1019 HOH A O   1 
HETATM 7007 O  O   . HOH NA 7 .   ? -43.536 -5.100  -1.237  1.00 39.07 ? 1020 HOH A O   1 
HETATM 7008 O  O   . HOH NA 7 .   ? -46.000 -5.207  -3.040  1.00 28.42 ? 1021 HOH A O   1 
HETATM 7009 O  O   . HOH NA 7 .   ? -22.400 -30.796 29.364  1.00 47.48 ? 1022 HOH A O   1 
HETATM 7010 O  O   . HOH NA 7 .   ? -0.016  -3.153  -10.503 1.00 20.60 ? 1023 HOH A O   1 
HETATM 7011 O  O   . HOH NA 7 .   ? -35.337 15.471  -12.594 1.00 38.15 ? 1024 HOH A O   1 
HETATM 7012 O  O   . HOH NA 7 .   ? -2.396  -6.068  10.629  1.00 32.70 ? 1025 HOH A O   1 
HETATM 7013 O  O   . HOH NA 7 .   ? -14.564 4.019   -8.017  1.00 19.95 ? 1026 HOH A O   1 
HETATM 7014 O  O   . HOH NA 7 .   ? -22.548 -10.614 -25.833 1.00 48.80 ? 1027 HOH A O   1 
HETATM 7015 O  O   . HOH NA 7 .   ? 0.536   -8.949  -2.021  1.00 20.68 ? 1028 HOH A O   1 
HETATM 7016 O  O   . HOH NA 7 .   ? -1.805  1.602   3.556   1.00 46.60 ? 1029 HOH A O   1 
HETATM 7017 O  O   . HOH NA 7 .   ? -5.610  -5.761  23.073  1.00 24.08 ? 1030 HOH A O   1 
HETATM 7018 O  O   . HOH NA 7 .   ? -24.044 -19.633 -15.948 1.00 29.66 ? 1031 HOH A O   1 
HETATM 7019 O  O   . HOH NA 7 .   ? -46.253 -3.764  -15.560 1.00 37.81 ? 1032 HOH A O   1 
HETATM 7020 O  O   . HOH NA 7 .   ? -4.405  -10.653 -17.036 1.00 43.74 ? 1033 HOH A O   1 
HETATM 7021 O  O   . HOH NA 7 .   ? -18.034 -29.158 29.310  1.00 38.57 ? 1034 HOH A O   1 
HETATM 7022 O  O   . HOH NA 7 .   ? -3.959  -9.455  14.701  1.00 39.75 ? 1035 HOH A O   1 
HETATM 7023 O  O   . HOH OA 7 .   ? -58.764 -9.925  1.309   1.00 31.85 ? 601  HOH B O   1 
HETATM 7024 O  O   . HOH OA 7 .   ? -61.757 2.284   24.846  1.00 39.84 ? 602  HOH B O   1 
HETATM 7025 O  O   . HOH OA 7 .   ? -62.471 -20.045 10.418  1.00 31.30 ? 603  HOH B O   1 
HETATM 7026 O  O   . HOH OA 7 .   ? -60.330 -18.191 11.869  1.00 23.62 ? 604  HOH B O   1 
HETATM 7027 O  O   . HOH OA 7 .   ? -73.955 29.007  -31.512 1.00 39.12 ? 605  HOH B O   1 
HETATM 7028 O  O   . HOH OA 7 .   ? -73.061 -10.751 8.937   1.00 40.05 ? 606  HOH B O   1 
HETATM 7029 O  O   . HOH OA 7 .   ? -45.487 -6.682  14.315  1.00 29.82 ? 607  HOH B O   1 
HETATM 7030 O  O   . HOH OA 7 .   ? -73.132 32.268  -22.042 1.00 31.22 ? 608  HOH B O   1 
HETATM 7031 O  O   . HOH OA 7 .   ? -61.743 7.470   -18.807 1.00 41.30 ? 609  HOH B O   1 
HETATM 7032 O  O   . HOH OA 7 .   ? -62.974 11.965  24.655  1.00 29.19 ? 610  HOH B O   1 
HETATM 7033 O  O   . HOH OA 7 .   ? -55.437 1.710   -15.454 1.00 27.35 ? 611  HOH B O   1 
HETATM 7034 O  O   . HOH OA 7 .   ? -48.581 0.194   2.155   1.00 25.59 ? 612  HOH B O   1 
HETATM 7035 O  O   . HOH OA 7 .   ? -60.072 39.243  -13.049 1.00 35.09 ? 613  HOH B O   1 
HETATM 7036 O  O   . HOH OA 7 .   ? -80.942 -18.886 3.116   1.00 37.30 ? 614  HOH B O   1 
HETATM 7037 O  O   . HOH OA 7 .   ? -56.695 4.136   -15.120 1.00 18.41 ? 615  HOH B O   1 
HETATM 7038 O  O   . HOH OA 7 .   ? -64.058 -20.670 7.924   1.00 21.38 ? 616  HOH B O   1 
HETATM 7039 O  O   . HOH OA 7 .   ? -71.251 35.407  -6.474  1.00 43.76 ? 617  HOH B O   1 
HETATM 7040 O  O   . HOH OA 7 .   ? -74.979 -15.235 6.184   1.00 38.14 ? 618  HOH B O   1 
HETATM 7041 O  O   . HOH OA 7 .   ? -36.566 10.808  3.785   1.00 39.63 ? 619  HOH B O   1 
HETATM 7042 O  O   . HOH OA 7 .   ? -44.191 31.755  -7.209  1.00 44.62 ? 620  HOH B O   1 
HETATM 7043 O  O   . HOH OA 7 .   ? -42.520 29.643  -0.434  1.00 40.22 ? 621  HOH B O   1 
HETATM 7044 O  O   . HOH OA 7 .   ? -73.051 17.371  -22.285 1.00 41.28 ? 622  HOH B O   1 
HETATM 7045 O  O   . HOH OA 7 .   ? -78.167 -4.666  13.583  1.00 30.21 ? 623  HOH B O   1 
HETATM 7046 O  O   . HOH OA 7 .   ? -75.216 -8.181  6.588   1.00 35.73 ? 624  HOH B O   1 
HETATM 7047 O  O   . HOH OA 7 .   ? -74.529 24.929  -19.618 1.00 31.26 ? 625  HOH B O   1 
HETATM 7048 O  O   . HOH OA 7 .   ? -50.498 23.354  14.708  1.00 30.38 ? 626  HOH B O   1 
HETATM 7049 O  O   . HOH OA 7 .   ? -66.583 19.450  21.486  1.00 43.12 ? 627  HOH B O   1 
HETATM 7050 O  O   . HOH OA 7 .   ? -45.506 31.765  6.818   1.00 47.49 ? 628  HOH B O   1 
HETATM 7051 O  O   . HOH OA 7 .   ? -52.079 -8.315  12.404  1.00 19.58 ? 629  HOH B O   1 
HETATM 7052 O  O   . HOH OA 7 .   ? -60.055 11.177  -22.325 1.00 27.76 ? 630  HOH B O   1 
HETATM 7053 O  O   . HOH OA 7 .   ? -55.095 38.950  -8.586  1.00 26.83 ? 631  HOH B O   1 
HETATM 7054 O  O   . HOH OA 7 .   ? -71.604 9.088   -2.728  1.00 38.10 ? 632  HOH B O   1 
HETATM 7055 O  O   . HOH OA 7 .   ? -72.302 10.263  0.301   1.00 30.09 ? 633  HOH B O   1 
HETATM 7056 O  O   . HOH OA 7 .   ? -43.857 19.024  15.489  1.00 29.90 ? 634  HOH B O   1 
HETATM 7057 O  O   . HOH OA 7 .   ? -48.332 36.499  -15.969 1.00 41.28 ? 635  HOH B O   1 
HETATM 7058 O  O   . HOH OA 7 .   ? -72.910 2.021   -0.227  1.00 17.43 ? 636  HOH B O   1 
HETATM 7059 O  O   . HOH OA 7 .   ? -63.581 28.038  1.465   1.00 23.11 ? 637  HOH B O   1 
HETATM 7060 O  O   . HOH OA 7 .   ? -50.545 7.013   -20.445 1.00 35.93 ? 638  HOH B O   1 
HETATM 7061 O  O   . HOH OA 7 .   ? -45.567 16.586  5.930   1.00 14.16 ? 639  HOH B O   1 
HETATM 7062 O  O   . HOH OA 7 .   ? -62.671 29.749  9.199   1.00 38.97 ? 640  HOH B O   1 
HETATM 7063 O  O   . HOH OA 7 .   ? -66.802 30.051  -3.179  1.00 29.82 ? 641  HOH B O   1 
HETATM 7064 O  O   . HOH OA 7 .   ? -48.685 6.240   8.301   1.00 26.00 ? 642  HOH B O   1 
HETATM 7065 O  O   . HOH OA 7 .   ? -74.124 21.507  -15.117 1.00 36.36 ? 643  HOH B O   1 
HETATM 7066 O  O   . HOH OA 7 .   ? -55.333 22.536  -27.051 1.00 41.40 ? 644  HOH B O   1 
HETATM 7067 O  O   . HOH OA 7 .   ? -65.341 -3.877  26.159  1.00 31.24 ? 645  HOH B O   1 
HETATM 7068 O  O   . HOH OA 7 .   ? -71.023 -12.610 -13.889 1.00 22.32 ? 646  HOH B O   1 
HETATM 7069 O  O   . HOH OA 7 .   ? -54.254 12.344  -16.086 1.00 13.47 ? 647  HOH B O   1 
HETATM 7070 O  O   . HOH OA 7 .   ? -44.951 8.258   16.430  1.00 36.84 ? 648  HOH B O   1 
HETATM 7071 O  O   . HOH OA 7 .   ? -60.652 21.325  0.244   1.00 15.84 ? 649  HOH B O   1 
HETATM 7072 O  O   . HOH OA 7 .   ? -63.292 -6.421  -12.859 1.00 19.43 ? 650  HOH B O   1 
HETATM 7073 O  O   . HOH OA 7 .   ? -38.562 19.793  7.448   1.00 30.64 ? 651  HOH B O   1 
HETATM 7074 O  O   . HOH OA 7 .   ? -52.217 15.351  -1.749  1.00 12.60 ? 652  HOH B O   1 
HETATM 7075 O  O   . HOH OA 7 .   ? -76.097 0.813   -9.276  1.00 21.66 ? 653  HOH B O   1 
HETATM 7076 O  O   . HOH OA 7 .   ? -48.856 10.444  -9.427  1.00 18.40 ? 654  HOH B O   1 
HETATM 7077 O  O   . HOH OA 7 .   ? -45.247 29.914  12.698  1.00 39.22 ? 655  HOH B O   1 
HETATM 7078 O  O   . HOH OA 7 .   ? -57.375 33.190  -5.245  1.00 19.62 ? 656  HOH B O   1 
HETATM 7079 O  O   . HOH OA 7 .   ? -45.016 29.109  -3.913  1.00 40.47 ? 657  HOH B O   1 
HETATM 7080 O  O   A HOH OA 7 .   ? -64.640 12.341  -18.012 0.50 14.99 ? 658  HOH B O   1 
HETATM 7081 O  O   B HOH OA 7 .   ? -64.299 11.517  -19.811 0.50 24.29 ? 658  HOH B O   1 
HETATM 7082 O  O   . HOH OA 7 .   ? -42.102 16.928  13.740  1.00 34.01 ? 659  HOH B O   1 
HETATM 7083 O  O   . HOH OA 7 .   ? -60.765 -6.540  25.242  1.00 31.67 ? 660  HOH B O   1 
HETATM 7084 O  O   . HOH OA 7 .   ? -54.038 -5.844  -2.329  1.00 18.06 ? 661  HOH B O   1 
HETATM 7085 O  O   . HOH OA 7 .   ? -67.965 14.435  -8.719  1.00 17.27 ? 662  HOH B O   1 
HETATM 7086 O  O   . HOH OA 7 .   ? -52.850 4.084   10.498  1.00 14.55 ? 663  HOH B O   1 
HETATM 7087 O  O   . HOH OA 7 .   ? -70.227 24.621  -26.617 1.00 29.50 ? 664  HOH B O   1 
HETATM 7088 O  O   . HOH OA 7 .   ? -68.690 18.091  10.626  1.00 21.17 ? 665  HOH B O   1 
HETATM 7089 O  O   . HOH OA 7 .   ? -53.478 4.849   -9.635  1.00 19.51 ? 666  HOH B O   1 
HETATM 7090 O  O   . HOH OA 7 .   ? -46.708 17.485  13.717  1.00 20.02 ? 667  HOH B O   1 
HETATM 7091 O  O   . HOH OA 7 .   ? -79.228 29.439  -9.357  1.00 17.15 ? 668  HOH B O   1 
HETATM 7092 O  O   . HOH OA 7 .   ? -78.398 -13.128 1.728   1.00 23.66 ? 669  HOH B O   1 
HETATM 7093 O  O   . HOH OA 7 .   ? -61.090 -5.728  -10.953 1.00 20.10 ? 670  HOH B O   1 
HETATM 7094 O  O   . HOH OA 7 .   ? -53.370 18.156  -26.328 1.00 32.27 ? 671  HOH B O   1 
HETATM 7095 O  O   . HOH OA 7 .   ? -41.148 30.157  2.169   1.00 33.37 ? 672  HOH B O   1 
HETATM 7096 O  O   . HOH OA 7 .   ? -73.256 10.142  -6.959  1.00 42.35 ? 673  HOH B O   1 
HETATM 7097 O  O   . HOH OA 7 .   ? -47.404 12.689  6.257   1.00 14.29 ? 674  HOH B O   1 
HETATM 7098 O  O   . HOH OA 7 .   ? -70.601 18.021  13.071  1.00 34.78 ? 675  HOH B O   1 
HETATM 7099 O  O   . HOH OA 7 .   ? -47.495 15.214  7.663   1.00 13.11 ? 676  HOH B O   1 
HETATM 7100 O  O   . HOH OA 7 .   ? -67.156 -18.242 2.973   1.00 22.57 ? 677  HOH B O   1 
HETATM 7101 O  O   . HOH OA 7 .   ? -63.476 4.741   -14.291 1.00 28.24 ? 678  HOH B O   1 
HETATM 7102 O  O   . HOH OA 7 .   ? -71.615 11.546  9.638   1.00 40.93 ? 679  HOH B O   1 
HETATM 7103 O  O   . HOH OA 7 .   ? -50.307 33.933  4.065   1.00 38.47 ? 680  HOH B O   1 
HETATM 7104 O  O   . HOH OA 7 .   ? -53.084 32.731  -22.915 1.00 33.71 ? 681  HOH B O   1 
HETATM 7105 O  O   . HOH OA 7 .   ? -44.996 28.594  -11.915 1.00 22.92 ? 682  HOH B O   1 
HETATM 7106 O  O   . HOH OA 7 .   ? -53.638 34.553  -7.218  1.00 29.64 ? 683  HOH B O   1 
HETATM 7107 O  O   . HOH OA 7 .   ? -71.454 -17.374 7.644   1.00 28.37 ? 684  HOH B O   1 
HETATM 7108 O  O   . HOH OA 7 .   ? -48.056 23.789  -27.152 1.00 41.44 ? 685  HOH B O   1 
HETATM 7109 O  O   . HOH OA 7 .   ? -68.790 12.413  -1.718  1.00 17.46 ? 686  HOH B O   1 
HETATM 7110 O  O   . HOH OA 7 .   ? -72.139 9.825   18.426  1.00 22.65 ? 687  HOH B O   1 
HETATM 7111 O  O   . HOH OA 7 .   ? -70.971 8.251   2.943   1.00 17.86 ? 688  HOH B O   1 
HETATM 7112 O  O   . HOH OA 7 .   ? -64.910 -10.040 23.705  1.00 36.93 ? 689  HOH B O   1 
HETATM 7113 O  O   . HOH OA 7 .   ? -47.254 1.663   20.755  1.00 37.66 ? 690  HOH B O   1 
HETATM 7114 O  O   . HOH OA 7 .   ? -50.482 12.642  -10.067 1.00 14.51 ? 691  HOH B O   1 
HETATM 7115 O  O   . HOH OA 7 .   ? -73.799 3.443   3.269   1.00 38.98 ? 692  HOH B O   1 
HETATM 7116 O  O   . HOH OA 7 .   ? -42.800 8.507   13.854  1.00 36.85 ? 693  HOH B O   1 
HETATM 7117 O  O   . HOH OA 7 .   ? -46.918 21.657  2.073   1.00 15.39 ? 694  HOH B O   1 
HETATM 7118 O  O   . HOH OA 7 .   ? -59.571 31.649  -27.066 1.00 46.63 ? 695  HOH B O   1 
HETATM 7119 O  O   . HOH OA 7 .   ? -46.744 10.394  15.337  1.00 29.82 ? 696  HOH B O   1 
HETATM 7120 O  O   . HOH OA 7 .   ? -73.212 11.304  -12.908 1.00 46.05 ? 697  HOH B O   1 
HETATM 7121 O  O   . HOH OA 7 .   ? -65.122 17.769  -12.078 1.00 13.56 ? 698  HOH B O   1 
HETATM 7122 O  O   . HOH OA 7 .   ? -73.237 13.999  -16.568 1.00 33.55 ? 699  HOH B O   1 
HETATM 7123 O  O   . HOH OA 7 .   ? -41.362 7.463   3.074   1.00 28.84 ? 700  HOH B O   1 
HETATM 7124 O  O   . HOH OA 7 .   ? -75.130 -8.422  13.954  1.00 21.46 ? 701  HOH B O   1 
HETATM 7125 O  O   . HOH OA 7 .   ? -62.153 12.991  2.266   1.00 14.02 ? 702  HOH B O   1 
HETATM 7126 O  O   . HOH OA 7 .   ? -57.161 12.617  -25.586 1.00 39.28 ? 703  HOH B O   1 
HETATM 7127 O  O   . HOH OA 7 .   ? -42.931 12.494  -7.904  1.00 16.09 ? 704  HOH B O   1 
HETATM 7128 O  O   . HOH OA 7 .   ? -75.098 -7.816  -11.677 1.00 31.80 ? 705  HOH B O   1 
HETATM 7129 O  O   . HOH OA 7 .   ? -51.909 4.346   -6.902  1.00 11.17 ? 706  HOH B O   1 
HETATM 7130 O  O   . HOH OA 7 .   ? -67.269 26.582  0.021   1.00 28.80 ? 707  HOH B O   1 
HETATM 7131 O  O   . HOH OA 7 .   ? -63.622 35.798  -13.456 1.00 23.78 ? 708  HOH B O   1 
HETATM 7132 O  O   . HOH OA 7 .   ? -58.229 -15.509 18.452  1.00 25.50 ? 709  HOH B O   1 
HETATM 7133 O  O   . HOH OA 7 .   ? -49.478 31.977  5.024   1.00 38.94 ? 710  HOH B O   1 
HETATM 7134 O  O   . HOH OA 7 .   ? -50.190 20.948  12.831  1.00 47.49 ? 711  HOH B O   1 
HETATM 7135 O  O   . HOH OA 7 .   ? -58.436 31.687  -10.800 1.00 15.69 ? 712  HOH B O   1 
HETATM 7136 O  O   . HOH OA 7 .   ? -50.449 -6.071  20.950  1.00 29.08 ? 713  HOH B O   1 
HETATM 7137 O  O   . HOH OA 7 .   ? -55.293 -18.353 8.057   1.00 21.69 ? 714  HOH B O   1 
HETATM 7138 O  O   . HOH OA 7 .   ? -60.576 -12.064 1.900   1.00 35.45 ? 715  HOH B O   1 
HETATM 7139 O  O   . HOH OA 7 .   ? -65.125 22.635  14.682  1.00 28.75 ? 716  HOH B O   1 
HETATM 7140 O  O   . HOH OA 7 .   ? -44.978 24.080  0.070   1.00 17.75 ? 717  HOH B O   1 
HETATM 7141 O  O   . HOH OA 7 .   ? -76.499 0.171   -4.538  1.00 24.44 ? 718  HOH B O   1 
HETATM 7142 O  O   . HOH OA 7 .   ? -69.678 -5.194  -16.502 1.00 42.61 ? 719  HOH B O   1 
HETATM 7143 O  O   . HOH OA 7 .   ? -41.164 18.260  8.569   1.00 36.02 ? 720  HOH B O   1 
HETATM 7144 O  O   . HOH OA 7 .   ? -70.494 -14.981 -4.002  1.00 18.64 ? 721  HOH B O   1 
HETATM 7145 O  O   . HOH OA 7 .   ? -52.188 3.275   25.780  1.00 37.02 ? 722  HOH B O   1 
HETATM 7146 O  O   . HOH OA 7 .   ? -72.340 -9.695  17.390  1.00 34.19 ? 723  HOH B O   1 
HETATM 7147 O  O   . HOH OA 7 .   ? -45.133 19.260  6.198   1.00 13.48 ? 724  HOH B O   1 
HETATM 7148 O  O   . HOH OA 7 .   ? -68.362 16.059  -5.313  1.00 16.00 ? 725  HOH B O   1 
HETATM 7149 O  O   . HOH OA 7 .   ? -57.089 12.854  10.168  1.00 15.14 ? 726  HOH B O   1 
HETATM 7150 O  O   . HOH OA 7 .   ? -61.926 31.047  -26.861 1.00 35.81 ? 727  HOH B O   1 
HETATM 7151 O  O   . HOH OA 7 .   ? -43.511 26.255  -21.326 1.00 36.55 ? 728  HOH B O   1 
HETATM 7152 O  O   . HOH OA 7 .   ? -62.223 31.413  -4.480  1.00 27.08 ? 729  HOH B O   1 
HETATM 7153 O  O   . HOH OA 7 .   ? -46.521 27.959  -14.226 1.00 17.38 ? 730  HOH B O   1 
HETATM 7154 O  O   . HOH OA 7 .   ? -56.094 16.434  -19.520 1.00 23.41 ? 731  HOH B O   1 
HETATM 7155 O  O   . HOH OA 7 .   ? -45.743 4.499   -2.280  1.00 16.15 ? 732  HOH B O   1 
HETATM 7156 O  O   . HOH OA 7 .   ? -73.432 15.186  -4.225  1.00 24.49 ? 733  HOH B O   1 
HETATM 7157 O  O   . HOH OA 7 .   ? -68.143 15.878  5.056   1.00 20.27 ? 734  HOH B O   1 
HETATM 7158 O  O   . HOH OA 7 .   ? -48.364 -3.176  -0.803  1.00 35.58 ? 735  HOH B O   1 
HETATM 7159 O  O   . HOH OA 7 .   ? -47.099 16.065  -11.432 1.00 15.68 ? 736  HOH B O   1 
HETATM 7160 O  O   . HOH OA 7 .   ? -74.061 2.433   -2.774  1.00 25.38 ? 737  HOH B O   1 
HETATM 7161 O  O   . HOH OA 7 .   ? -66.814 12.037  -20.845 1.00 37.08 ? 738  HOH B O   1 
HETATM 7162 O  O   . HOH OA 7 .   ? -71.036 -1.979  -9.828  1.00 14.02 ? 739  HOH B O   1 
HETATM 7163 O  O   . HOH OA 7 .   ? -56.709 17.123  4.745   1.00 13.77 ? 740  HOH B O   1 
HETATM 7164 O  O   . HOH OA 7 .   ? -69.486 -10.553 16.801  1.00 21.69 ? 741  HOH B O   1 
HETATM 7165 O  O   . HOH OA 7 .   ? -43.235 25.406  -1.771  1.00 19.19 ? 742  HOH B O   1 
HETATM 7166 O  O   . HOH OA 7 .   ? -51.595 13.126  6.519   1.00 10.83 ? 743  HOH B O   1 
HETATM 7167 O  O   . HOH OA 7 .   ? -46.305 22.567  16.852  1.00 35.71 ? 744  HOH B O   1 
HETATM 7168 O  O   . HOH OA 7 .   ? -75.700 -0.103  5.642   1.00 33.18 ? 745  HOH B O   1 
HETATM 7169 O  O   . HOH OA 7 .   ? -56.824 30.838  6.713   1.00 25.28 ? 746  HOH B O   1 
HETATM 7170 O  O   . HOH OA 7 .   ? -69.627 -6.694  22.746  1.00 27.72 ? 747  HOH B O   1 
HETATM 7171 O  O   . HOH OA 7 .   ? -71.180 35.662  -13.658 1.00 28.13 ? 748  HOH B O   1 
HETATM 7172 O  O   . HOH OA 7 .   ? -58.867 -11.650 -0.558  1.00 35.56 ? 749  HOH B O   1 
HETATM 7173 O  O   . HOH OA 7 .   ? -61.110 8.029   20.040  1.00 17.82 ? 750  HOH B O   1 
HETATM 7174 O  O   . HOH OA 7 .   ? -60.291 -4.882  6.153   1.00 35.81 ? 751  HOH B O   1 
HETATM 7175 O  O   . HOH OA 7 .   ? -54.802 -4.798  26.336  1.00 45.48 ? 752  HOH B O   1 
HETATM 7176 O  O   . HOH OA 7 .   ? -68.993 9.134   -12.835 1.00 41.66 ? 753  HOH B O   1 
HETATM 7177 O  O   . HOH OA 7 .   ? -66.854 9.227   24.485  1.00 27.33 ? 754  HOH B O   1 
HETATM 7178 O  O   . HOH OA 7 .   ? -68.836 0.814   -6.695  1.00 13.70 ? 755  HOH B O   1 
HETATM 7179 O  O   . HOH OA 7 .   ? -44.314 24.678  -8.785  1.00 14.68 ? 756  HOH B O   1 
HETATM 7180 O  O   . HOH OA 7 .   ? -45.269 18.009  -1.130  1.00 14.23 ? 757  HOH B O   1 
HETATM 7181 O  O   . HOH OA 7 .   ? -74.430 27.880  -4.395  1.00 23.23 ? 758  HOH B O   1 
HETATM 7182 O  O   . HOH OA 7 .   ? -62.863 7.651   -15.217 1.00 40.85 ? 759  HOH B O   1 
HETATM 7183 O  O   . HOH OA 7 .   ? -47.031 29.846  5.290   1.00 26.74 ? 760  HOH B O   1 
HETATM 7184 O  O   . HOH OA 7 .   ? -69.362 15.395  -21.036 1.00 32.73 ? 761  HOH B O   1 
HETATM 7185 O  O   . HOH OA 7 .   ? -75.865 20.919  -6.056  1.00 40.60 ? 762  HOH B O   1 
HETATM 7186 O  O   . HOH OA 7 .   ? -50.676 6.919   26.366  1.00 39.74 ? 763  HOH B O   1 
HETATM 7187 O  O   . HOH OA 7 .   ? -67.363 19.587  2.380   1.00 23.37 ? 764  HOH B O   1 
HETATM 7188 O  O   . HOH OA 7 .   ? -64.852 14.944  -14.577 1.00 18.07 ? 765  HOH B O   1 
HETATM 7189 O  O   . HOH OA 7 .   ? -49.182 21.084  -12.697 1.00 14.52 ? 766  HOH B O   1 
HETATM 7190 O  O   . HOH OA 7 .   ? -52.448 15.349  19.950  1.00 24.09 ? 767  HOH B O   1 
HETATM 7191 O  O   . HOH OA 7 .   ? -46.173 27.935  -22.649 1.00 25.38 ? 768  HOH B O   1 
HETATM 7192 O  O   . HOH OA 7 .   ? -66.316 18.668  -5.014  1.00 12.66 ? 769  HOH B O   1 
HETATM 7193 O  O   . HOH OA 7 .   ? -41.862 8.426   7.879   1.00 39.44 ? 770  HOH B O   1 
HETATM 7194 O  O   . HOH OA 7 .   ? -70.065 4.231   -5.881  1.00 18.71 ? 771  HOH B O   1 
HETATM 7195 O  O   . HOH OA 7 .   ? -73.167 -3.480  3.169   1.00 17.17 ? 772  HOH B O   1 
HETATM 7196 O  O   . HOH OA 7 .   ? -74.730 5.718   14.283  1.00 32.23 ? 773  HOH B O   1 
HETATM 7197 O  O   . HOH OA 7 .   ? -49.878 9.795   24.036  1.00 36.42 ? 774  HOH B O   1 
HETATM 7198 O  O   . HOH OA 7 .   ? -73.201 -3.775  -9.317  1.00 16.50 ? 775  HOH B O   1 
HETATM 7199 O  O   . HOH OA 7 .   ? -46.002 0.742   14.423  1.00 28.74 ? 776  HOH B O   1 
HETATM 7200 O  O   . HOH OA 7 .   ? -55.476 32.340  -3.361  1.00 42.87 ? 777  HOH B O   1 
HETATM 7201 O  O   . HOH OA 7 .   ? -68.036 5.786   -7.427  1.00 29.87 ? 778  HOH B O   1 
HETATM 7202 O  O   . HOH OA 7 .   ? -77.917 34.069  -9.074  1.00 17.46 ? 779  HOH B O   1 
HETATM 7203 O  O   . HOH OA 7 .   ? -39.677 20.175  -9.373  1.00 43.93 ? 780  HOH B O   1 
HETATM 7204 O  O   . HOH OA 7 .   ? -49.080 14.174  -11.879 1.00 13.65 ? 781  HOH B O   1 
HETATM 7205 O  O   . HOH OA 7 .   ? -49.103 35.974  -3.203  1.00 33.74 ? 782  HOH B O   1 
HETATM 7206 O  O   . HOH OA 7 .   ? -44.522 2.016   6.281   1.00 40.27 ? 783  HOH B O   1 
HETATM 7207 O  O   . HOH OA 7 .   ? -60.221 16.677  -23.593 1.00 31.52 ? 784  HOH B O   1 
HETATM 7208 O  O   . HOH OA 7 .   ? -42.884 25.602  -18.974 1.00 38.04 ? 785  HOH B O   1 
HETATM 7209 O  O   . HOH OA 7 .   ? -74.688 4.212   -10.670 1.00 43.07 ? 786  HOH B O   1 
HETATM 7210 O  O   . HOH OA 7 .   ? -45.542 1.266   1.442   1.00 30.64 ? 787  HOH B O   1 
HETATM 7211 O  O   . HOH OA 7 .   ? -49.822 -10.469 15.139  1.00 49.27 ? 788  HOH B O   1 
HETATM 7212 O  O   . HOH OA 7 .   ? -55.402 5.457   -21.748 1.00 44.85 ? 789  HOH B O   1 
HETATM 7213 O  O   . HOH OA 7 .   ? -68.364 -13.021 17.470  1.00 33.76 ? 790  HOH B O   1 
HETATM 7214 O  O   . HOH OA 7 .   ? -57.621 16.454  -24.118 1.00 29.12 ? 791  HOH B O   1 
HETATM 7215 O  O   . HOH OA 7 .   ? -53.773 -13.955 22.614  1.00 46.97 ? 792  HOH B O   1 
HETATM 7216 O  O   . HOH OA 7 .   ? -56.345 6.786   -13.711 1.00 13.75 ? 793  HOH B O   1 
HETATM 7217 O  O   . HOH OA 7 .   ? -77.780 -9.789  -7.827  1.00 16.76 ? 794  HOH B O   1 
HETATM 7218 O  O   . HOH OA 7 .   ? -61.505 -2.458  6.613   1.00 11.07 ? 795  HOH B O   1 
HETATM 7219 O  O   . HOH OA 7 .   ? -44.978 16.198  -9.617  1.00 17.95 ? 796  HOH B O   1 
HETATM 7220 O  O   A HOH OA 7 .   ? -74.019 -17.420 -5.314  0.80 13.09 ? 797  HOH B O   1 
HETATM 7221 O  O   B HOH OA 7 .   ? -76.245 -18.296 -4.758  0.20 7.48  ? 797  HOH B O   1 
HETATM 7222 O  O   . HOH OA 7 .   ? -73.304 -10.333 -13.944 1.00 35.05 ? 798  HOH B O   1 
HETATM 7223 O  O   . HOH OA 7 .   ? -69.379 -7.548  -15.016 1.00 27.13 ? 799  HOH B O   1 
HETATM 7224 O  O   . HOH OA 7 .   ? -44.676 32.359  -0.404  1.00 32.41 ? 800  HOH B O   1 
HETATM 7225 O  O   . HOH OA 7 .   ? -63.594 -3.420  -16.159 1.00 35.02 ? 801  HOH B O   1 
HETATM 7226 O  O   . HOH OA 7 .   ? -43.119 17.159  -18.029 1.00 26.55 ? 802  HOH B O   1 
HETATM 7227 O  O   A HOH OA 7 .   ? -59.154 31.067  -1.688  0.60 25.11 ? 803  HOH B O   1 
HETATM 7228 O  O   B HOH OA 7 .   ? -57.446 31.468  -1.412  0.40 16.05 ? 803  HOH B O   1 
HETATM 7229 O  O   . HOH OA 7 .   ? -49.331 -3.281  3.993   1.00 21.10 ? 804  HOH B O   1 
HETATM 7230 O  O   . HOH OA 7 .   ? -42.874 27.997  -2.575  1.00 31.08 ? 805  HOH B O   1 
HETATM 7231 O  O   . HOH OA 7 .   ? -51.730 -9.624  -2.069  1.00 32.29 ? 806  HOH B O   1 
HETATM 7232 O  O   . HOH OA 7 .   ? -73.416 -0.641  11.086  1.00 17.10 ? 807  HOH B O   1 
HETATM 7233 O  O   . HOH OA 7 .   ? -76.823 3.048   15.127  1.00 24.59 ? 808  HOH B O   1 
HETATM 7234 O  O   . HOH OA 7 .   ? -54.384 -14.509 9.800   1.00 24.07 ? 809  HOH B O   1 
HETATM 7235 O  O   . HOH OA 7 .   ? -54.982 -6.662  -9.988  1.00 24.74 ? 810  HOH B O   1 
HETATM 7236 O  O   . HOH OA 7 .   ? -57.372 26.175  -25.086 1.00 37.36 ? 811  HOH B O   1 
HETATM 7237 O  O   . HOH OA 7 .   ? -46.429 4.746   7.577   1.00 28.04 ? 812  HOH B O   1 
HETATM 7238 O  O   . HOH OA 7 .   ? -69.093 12.305  3.114   1.00 32.31 ? 813  HOH B O   1 
HETATM 7239 O  O   . HOH OA 7 .   ? -75.482 -15.004 0.840   1.00 37.72 ? 814  HOH B O   1 
HETATM 7240 O  O   . HOH OA 7 .   ? -52.451 32.852  5.556   1.00 42.49 ? 815  HOH B O   1 
HETATM 7241 O  O   . HOH OA 7 .   ? -74.137 24.668  -17.072 1.00 39.33 ? 816  HOH B O   1 
HETATM 7242 O  O   . HOH OA 7 .   ? -68.358 17.109  2.288   1.00 31.29 ? 817  HOH B O   1 
HETATM 7243 O  O   . HOH OA 7 .   ? -50.719 15.729  17.601  1.00 21.30 ? 818  HOH B O   1 
HETATM 7244 O  O   . HOH OA 7 .   ? -62.903 15.782  -12.771 1.00 11.99 ? 819  HOH B O   1 
HETATM 7245 O  O   . HOH OA 7 .   ? -47.533 21.508  -0.758  1.00 13.71 ? 820  HOH B O   1 
HETATM 7246 O  O   . HOH OA 7 .   ? -43.999 25.566  13.486  1.00 33.45 ? 821  HOH B O   1 
HETATM 7247 O  O   . HOH OA 7 .   ? -40.875 24.654  -11.950 1.00 38.93 ? 822  HOH B O   1 
HETATM 7248 O  O   . HOH OA 7 .   ? -40.980 5.420   -4.566  1.00 38.75 ? 823  HOH B O   1 
HETATM 7249 O  O   . HOH OA 7 .   ? -77.862 19.078  -14.340 1.00 45.34 ? 824  HOH B O   1 
HETATM 7250 O  O   . HOH OA 7 .   ? -62.404 23.025  17.635  1.00 34.38 ? 825  HOH B O   1 
HETATM 7251 O  O   A HOH OA 7 .   ? -72.620 4.373   24.572  0.70 23.51 ? 826  HOH B O   1 
HETATM 7252 O  O   B HOH OA 7 .   ? -73.696 2.672   24.495  0.30 13.34 ? 826  HOH B O   1 
HETATM 7253 O  O   . HOH OA 7 .   ? -39.190 26.157  8.585   1.00 35.69 ? 827  HOH B O   1 
HETATM 7254 O  O   . HOH OA 7 .   ? -58.894 -0.364  10.695  1.00 11.15 ? 828  HOH B O   1 
HETATM 7255 O  O   . HOH OA 7 .   ? -46.869 1.110   17.373  1.00 23.57 ? 829  HOH B O   1 
HETATM 7256 O  O   . HOH OA 7 .   ? -44.204 6.148   7.018   1.00 26.75 ? 830  HOH B O   1 
HETATM 7257 O  O   . HOH OA 7 .   ? -60.107 -14.460 -6.442  1.00 13.43 ? 831  HOH B O   1 
HETATM 7258 O  O   . HOH OA 7 .   ? -43.631 22.569  12.965  1.00 23.65 ? 832  HOH B O   1 
HETATM 7259 O  O   . HOH OA 7 .   ? -48.193 29.815  -15.734 1.00 26.50 ? 833  HOH B O   1 
HETATM 7260 O  O   . HOH OA 7 .   ? -44.014 13.851  16.138  1.00 41.21 ? 834  HOH B O   1 
HETATM 7261 O  O   . HOH OA 7 .   ? -58.449 9.065   -21.568 1.00 20.43 ? 835  HOH B O   1 
HETATM 7262 O  O   . HOH OA 7 .   ? -56.822 11.118  22.985  1.00 34.91 ? 836  HOH B O   1 
HETATM 7263 O  O   . HOH OA 7 .   ? -52.653 -13.947 16.398  1.00 31.92 ? 837  HOH B O   1 
HETATM 7264 O  O   . HOH OA 7 .   ? -56.188 29.618  -2.519  1.00 19.64 ? 838  HOH B O   1 
HETATM 7265 O  O   . HOH OA 7 .   ? -58.740 31.605  13.965  1.00 42.63 ? 839  HOH B O   1 
HETATM 7266 O  O   . HOH OA 7 .   ? -61.284 16.044  23.641  1.00 20.65 ? 840  HOH B O   1 
HETATM 7267 O  O   . HOH OA 7 .   ? -72.039 -0.562  -11.873 1.00 26.93 ? 841  HOH B O   1 
HETATM 7268 O  O   . HOH OA 7 .   ? -53.086 4.934   17.177  1.00 16.65 ? 842  HOH B O   1 
HETATM 7269 O  O   . HOH OA 7 .   ? -66.864 4.999   -12.323 1.00 29.84 ? 843  HOH B O   1 
HETATM 7270 O  O   . HOH OA 7 .   ? -60.429 27.307  15.746  1.00 31.74 ? 844  HOH B O   1 
HETATM 7271 O  O   . HOH OA 7 .   ? -73.381 20.443  -2.989  1.00 32.06 ? 845  HOH B O   1 
HETATM 7272 O  O   . HOH OA 7 .   ? -53.373 11.259  22.415  1.00 32.54 ? 846  HOH B O   1 
HETATM 7273 O  O   . HOH OA 7 .   ? -65.601 23.662  7.304   1.00 17.11 ? 847  HOH B O   1 
HETATM 7274 O  O   . HOH OA 7 .   ? -58.768 18.840  3.984   1.00 17.85 ? 848  HOH B O   1 
HETATM 7275 O  O   . HOH OA 7 .   ? -75.016 35.542  -6.082  1.00 32.02 ? 849  HOH B O   1 
HETATM 7276 O  O   . HOH OA 7 .   ? -58.916 41.076  -22.239 1.00 36.08 ? 850  HOH B O   1 
HETATM 7277 O  O   . HOH OA 7 .   ? -65.635 -12.337 -10.714 1.00 16.50 ? 851  HOH B O   1 
HETATM 7278 O  O   . HOH OA 7 .   ? -44.928 18.363  18.619  1.00 43.42 ? 852  HOH B O   1 
HETATM 7279 O  O   . HOH OA 7 .   ? -47.592 8.880   -11.248 1.00 18.66 ? 853  HOH B O   1 
HETATM 7280 O  O   . HOH OA 7 .   ? -67.555 11.288  -15.298 1.00 33.20 ? 854  HOH B O   1 
HETATM 7281 O  O   . HOH OA 7 .   ? -77.901 27.953  -19.779 1.00 31.21 ? 855  HOH B O   1 
HETATM 7282 O  O   . HOH OA 7 .   ? -57.361 7.139   22.791  1.00 24.63 ? 856  HOH B O   1 
HETATM 7283 O  O   . HOH OA 7 .   ? -49.062 12.792  -3.953  1.00 13.38 ? 857  HOH B O   1 
HETATM 7284 O  O   . HOH OA 7 .   ? -72.099 15.824  21.493  1.00 33.80 ? 858  HOH B O   1 
HETATM 7285 O  O   . HOH OA 7 .   ? -54.144 -2.540  22.275  1.00 30.47 ? 859  HOH B O   1 
HETATM 7286 O  O   . HOH OA 7 .   ? -59.138 35.629  -7.490  1.00 35.93 ? 860  HOH B O   1 
HETATM 7287 O  O   . HOH OA 7 .   ? -61.564 8.052   2.233   1.00 13.77 ? 861  HOH B O   1 
HETATM 7288 O  O   . HOH OA 7 .   ? -62.463 27.630  -6.716  1.00 12.95 ? 862  HOH B O   1 
HETATM 7289 O  O   . HOH OA 7 .   ? -54.051 0.727   -6.046  1.00 14.55 ? 863  HOH B O   1 
HETATM 7290 O  O   . HOH OA 7 .   ? -59.047 25.634  17.000  1.00 29.87 ? 864  HOH B O   1 
HETATM 7291 O  O   . HOH OA 7 .   ? -41.873 12.125  16.737  1.00 36.24 ? 865  HOH B O   1 
HETATM 7292 O  O   . HOH OA 7 .   ? -51.043 32.169  11.877  1.00 42.74 ? 866  HOH B O   1 
HETATM 7293 O  O   . HOH OA 7 .   ? -70.605 17.544  6.258   1.00 40.52 ? 867  HOH B O   1 
HETATM 7294 O  O   . HOH OA 7 .   ? -51.064 12.873  -1.904  1.00 12.42 ? 868  HOH B O   1 
HETATM 7295 O  O   . HOH OA 7 .   ? -49.650 29.902  12.964  1.00 35.08 ? 869  HOH B O   1 
HETATM 7296 O  O   . HOH OA 7 .   ? -74.292 -17.855 0.763   1.00 29.76 ? 870  HOH B O   1 
HETATM 7297 O  O   . HOH OA 7 .   ? -42.005 12.092  9.516   1.00 17.82 ? 871  HOH B O   1 
HETATM 7298 O  O   . HOH OA 7 .   ? -46.445 7.640   -8.664  1.00 15.07 ? 872  HOH B O   1 
HETATM 7299 O  O   . HOH OA 7 .   ? -51.816 25.616  -27.955 1.00 34.93 ? 873  HOH B O   1 
HETATM 7300 O  O   . HOH OA 7 .   ? -51.323 -13.184 19.140  1.00 40.79 ? 874  HOH B O   1 
HETATM 7301 O  O   . HOH OA 7 .   ? -51.363 1.688   -3.740  1.00 9.64  ? 875  HOH B O   1 
HETATM 7302 O  O   . HOH OA 7 .   ? -72.834 23.997  -3.113  1.00 24.39 ? 876  HOH B O   1 
HETATM 7303 O  O   . HOH OA 7 .   ? -42.589 6.263   9.313   1.00 42.01 ? 877  HOH B O   1 
HETATM 7304 O  O   . HOH OA 7 .   ? -39.137 21.769  1.985   1.00 26.14 ? 878  HOH B O   1 
HETATM 7305 O  O   . HOH OA 7 .   ? -77.632 -1.940  9.539   1.00 34.80 ? 879  HOH B O   1 
HETATM 7306 O  O   . HOH OA 7 .   ? -52.633 35.073  -2.287  1.00 24.84 ? 880  HOH B O   1 
HETATM 7307 O  O   . HOH OA 7 .   ? -44.107 20.944  -17.543 1.00 24.71 ? 881  HOH B O   1 
HETATM 7308 O  O   . HOH OA 7 .   ? -75.529 -6.412  -1.040  1.00 19.29 ? 882  HOH B O   1 
HETATM 7309 O  O   . HOH OA 7 .   ? -49.170 -9.730  8.015   1.00 38.42 ? 883  HOH B O   1 
HETATM 7310 O  O   . HOH OA 7 .   ? -54.799 -9.797  -9.170  1.00 25.89 ? 884  HOH B O   1 
HETATM 7311 O  O   . HOH OA 7 .   ? -42.497 28.292  -11.656 1.00 35.81 ? 885  HOH B O   1 
HETATM 7312 O  O   . HOH OA 7 .   ? -43.164 26.983  -14.698 1.00 24.30 ? 886  HOH B O   1 
HETATM 7313 O  O   . HOH OA 7 .   ? -58.709 -12.771 25.648  1.00 40.27 ? 887  HOH B O   1 
HETATM 7314 O  O   . HOH OA 7 .   ? -38.986 8.365   13.434  1.00 32.71 ? 888  HOH B O   1 
HETATM 7315 O  O   . HOH OA 7 .   ? -76.238 16.009  -6.091  1.00 26.58 ? 889  HOH B O   1 
HETATM 7316 O  O   . HOH OA 7 .   ? -46.979 32.152  -15.082 1.00 31.68 ? 890  HOH B O   1 
HETATM 7317 O  O   . HOH OA 7 .   ? -60.278 -15.257 21.479  1.00 26.15 ? 891  HOH B O   1 
HETATM 7318 O  O   . HOH OA 7 .   ? -52.779 -1.885  -8.680  1.00 35.94 ? 892  HOH B O   1 
HETATM 7319 O  O   . HOH OA 7 .   ? -73.722 -7.791  3.421   1.00 15.98 ? 893  HOH B O   1 
HETATM 7320 O  O   . HOH OA 7 .   ? -43.981 33.251  -11.319 1.00 44.08 ? 894  HOH B O   1 
HETATM 7321 O  O   . HOH OA 7 .   ? -70.923 21.483  11.039  1.00 41.20 ? 895  HOH B O   1 
HETATM 7322 O  O   . HOH OA 7 .   ? -68.641 6.212   -4.523  1.00 14.43 ? 896  HOH B O   1 
HETATM 7323 O  O   . HOH OA 7 .   ? -72.986 29.924  -23.922 1.00 30.06 ? 897  HOH B O   1 
HETATM 7324 O  O   . HOH OA 7 .   ? -64.541 30.363  -28.917 1.00 41.98 ? 898  HOH B O   1 
HETATM 7325 O  O   . HOH OA 7 .   ? -50.235 15.449  7.461   1.00 14.89 ? 899  HOH B O   1 
HETATM 7326 O  O   . HOH OA 7 .   ? -77.760 29.972  -16.926 1.00 25.78 ? 900  HOH B O   1 
HETATM 7327 O  O   . HOH OA 7 .   ? -73.303 7.908   17.128  1.00 29.38 ? 901  HOH B O   1 
HETATM 7328 O  O   . HOH OA 7 .   ? -40.665 8.132   -1.473  1.00 22.74 ? 902  HOH B O   1 
HETATM 7329 O  O   . HOH OA 7 .   ? -67.567 35.700  -8.944  1.00 38.25 ? 903  HOH B O   1 
HETATM 7330 O  O   . HOH OA 7 .   ? -54.806 13.510  -18.623 1.00 20.41 ? 904  HOH B O   1 
HETATM 7331 O  O   . HOH OA 7 .   ? -78.074 -1.220  19.021  1.00 36.68 ? 905  HOH B O   1 
HETATM 7332 O  O   . HOH OA 7 .   ? -73.506 25.164  -25.855 1.00 41.29 ? 906  HOH B O   1 
HETATM 7333 O  O   . HOH OA 7 .   ? -49.532 30.126  7.211   1.00 20.14 ? 907  HOH B O   1 
HETATM 7334 O  O   . HOH OA 7 .   ? -75.520 25.606  -9.916  1.00 23.51 ? 908  HOH B O   1 
HETATM 7335 O  O   . HOH OA 7 .   ? -48.030 4.777   20.231  1.00 25.63 ? 909  HOH B O   1 
HETATM 7336 O  O   . HOH OA 7 .   ? -75.020 10.520  22.869  1.00 37.24 ? 910  HOH B O   1 
HETATM 7337 O  O   . HOH OA 7 .   ? -53.095 -12.101 -4.808  1.00 33.38 ? 911  HOH B O   1 
HETATM 7338 O  O   . HOH OA 7 .   ? -52.344 32.504  14.019  1.00 44.05 ? 912  HOH B O   1 
HETATM 7339 O  O   . HOH OA 7 .   ? -68.347 14.221  24.294  1.00 39.60 ? 913  HOH B O   1 
HETATM 7340 O  O   . HOH OA 7 .   ? -43.345 -2.566  14.661  1.00 33.98 ? 914  HOH B O   1 
HETATM 7341 O  O   . HOH OA 7 .   ? -76.312 -1.834  -8.333  1.00 13.54 ? 915  HOH B O   1 
HETATM 7342 O  O   . HOH OA 7 .   ? -76.719 -12.105 8.210   1.00 38.12 ? 916  HOH B O   1 
HETATM 7343 O  O   . HOH OA 7 .   ? -58.837 -14.738 5.390   1.00 16.60 ? 917  HOH B O   1 
HETATM 7344 O  O   . HOH OA 7 .   ? -74.883 -10.768 0.122   1.00 20.84 ? 918  HOH B O   1 
HETATM 7345 O  O   . HOH OA 7 .   ? -71.915 10.162  13.508  1.00 22.47 ? 919  HOH B O   1 
HETATM 7346 O  O   . HOH OA 7 .   ? -67.403 -0.376  -14.837 1.00 29.92 ? 920  HOH B O   1 
HETATM 7347 O  O   . HOH OA 7 .   ? -74.708 22.117  -4.103  1.00 24.86 ? 921  HOH B O   1 
HETATM 7348 O  O   . HOH OA 7 .   ? -43.658 30.168  -15.482 1.00 42.25 ? 922  HOH B O   1 
HETATM 7349 O  O   . HOH OA 7 .   ? -50.923 34.275  -21.869 1.00 46.25 ? 923  HOH B O   1 
HETATM 7350 O  O   . HOH OA 7 .   ? -44.302 4.057   11.068  1.00 38.80 ? 924  HOH B O   1 
HETATM 7351 O  O   . HOH OA 7 .   ? -75.824 -6.187  7.638   1.00 33.39 ? 925  HOH B O   1 
HETATM 7352 O  O   . HOH OA 7 .   ? -47.921 -7.050  -3.079  1.00 51.97 ? 926  HOH B O   1 
HETATM 7353 O  O   . HOH OA 7 .   ? -47.545 30.539  -5.065  1.00 31.46 ? 927  HOH B O   1 
HETATM 7354 O  O   . HOH OA 7 .   ? -71.088 16.660  15.459  1.00 34.94 ? 928  HOH B O   1 
HETATM 7355 O  O   . HOH OA 7 .   ? -65.707 -12.077 22.594  1.00 44.74 ? 929  HOH B O   1 
HETATM 7356 O  O   . HOH OA 7 .   ? -52.905 0.386   -8.928  1.00 19.57 ? 930  HOH B O   1 
HETATM 7357 O  O   . HOH OA 7 .   ? -41.091 23.105  11.225  1.00 43.33 ? 931  HOH B O   1 
HETATM 7358 O  O   . HOH OA 7 .   ? -55.468 -10.852 4.502   1.00 37.35 ? 932  HOH B O   1 
HETATM 7359 O  O   . HOH OA 7 .   ? -47.868 7.496   24.559  1.00 41.19 ? 933  HOH B O   1 
HETATM 7360 O  O   . HOH OA 7 .   ? -61.394 -13.976 0.701   1.00 37.34 ? 934  HOH B O   1 
HETATM 7361 O  O   . HOH OA 7 .   ? -51.407 11.965  -24.381 1.00 37.64 ? 935  HOH B O   1 
HETATM 7362 O  O   . HOH OA 7 .   ? -69.119 6.500   -11.388 1.00 35.32 ? 936  HOH B O   1 
HETATM 7363 O  O   . HOH OA 7 .   ? -50.205 -10.488 10.157  1.00 29.30 ? 937  HOH B O   1 
HETATM 7364 O  O   . HOH OA 7 .   ? -64.848 28.796  -6.023  1.00 15.78 ? 938  HOH B O   1 
HETATM 7365 O  O   . HOH OA 7 .   ? -55.563 40.958  -13.093 1.00 43.02 ? 939  HOH B O   1 
HETATM 7366 O  O   . HOH OA 7 .   ? -48.075 15.475  17.880  1.00 23.79 ? 940  HOH B O   1 
HETATM 7367 O  O   . HOH OA 7 .   ? -62.146 35.507  -27.452 1.00 44.87 ? 941  HOH B O   1 
HETATM 7368 O  O   . HOH OA 7 .   ? -74.477 38.815  -22.645 1.00 43.64 ? 942  HOH B O   1 
HETATM 7369 O  O   . HOH OA 7 .   ? -52.765 -4.874  22.601  1.00 37.02 ? 943  HOH B O   1 
HETATM 7370 O  O   . HOH OA 7 .   ? -69.603 30.681  -3.997  1.00 32.42 ? 944  HOH B O   1 
HETATM 7371 O  O   . HOH OA 7 .   ? -75.192 2.003   7.001   1.00 43.15 ? 945  HOH B O   1 
HETATM 7372 O  O   . HOH OA 7 .   ? -59.786 23.328  18.693  1.00 41.10 ? 946  HOH B O   1 
HETATM 7373 O  O   . HOH OA 7 .   ? -45.926 -1.485  4.624   1.00 45.79 ? 947  HOH B O   1 
HETATM 7374 O  O   . HOH OA 7 .   ? -71.243 7.255   -6.983  1.00 39.52 ? 948  HOH B O   1 
HETATM 7375 O  O   . HOH OA 7 .   ? -41.756 20.277  -23.823 1.00 39.98 ? 949  HOH B O   1 
HETATM 7376 O  O   . HOH OA 7 .   ? -66.809 27.112  11.167  1.00 46.78 ? 950  HOH B O   1 
HETATM 7377 O  O   . HOH OA 7 .   ? -65.246 31.131  -0.751  1.00 43.82 ? 951  HOH B O   1 
HETATM 7378 O  O   . HOH OA 7 .   ? -63.875 28.794  6.832   1.00 42.71 ? 952  HOH B O   1 
HETATM 7379 O  O   . HOH OA 7 .   ? -66.318 2.418   26.791  1.00 42.77 ? 953  HOH B O   1 
HETATM 7380 O  O   . HOH OA 7 .   ? -74.725 25.847  -23.777 1.00 36.10 ? 954  HOH B O   1 
HETATM 7381 O  O   . HOH OA 7 .   ? -52.713 -11.515 -7.161  1.00 39.75 ? 955  HOH B O   1 
HETATM 7382 O  O   . HOH OA 7 .   ? -74.251 -11.278 20.620  1.00 49.67 ? 956  HOH B O   1 
HETATM 7383 O  O   . HOH OA 7 .   ? -48.880 -15.105 14.997  1.00 41.04 ? 957  HOH B O   1 
HETATM 7384 O  O   A HOH OA 7 .   ? -49.656 -0.388  -13.330 0.80 25.52 ? 958  HOH B O   1 
HETATM 7385 O  O   B HOH OA 7 .   ? -49.672 -0.035  -11.525 0.20 6.55  ? 958  HOH B O   1 
HETATM 7386 O  O   . HOH OA 7 .   ? -74.495 23.207  -12.710 1.00 35.44 ? 959  HOH B O   1 
HETATM 7387 O  O   . HOH OA 7 .   ? -64.425 25.183  14.594  1.00 36.70 ? 960  HOH B O   1 
HETATM 7388 O  O   . HOH OA 7 .   ? -75.147 -5.126  3.910   1.00 21.68 ? 961  HOH B O   1 
HETATM 7389 O  O   . HOH OA 7 .   ? -56.523 32.206  3.069   1.00 29.70 ? 962  HOH B O   1 
HETATM 7390 O  O   . HOH OA 7 .   ? -57.802 32.131  0.976   1.00 32.82 ? 963  HOH B O   1 
HETATM 7391 O  O   . HOH OA 7 .   ? -59.706 3.771   25.848  1.00 42.17 ? 964  HOH B O   1 
HETATM 7392 O  O   . HOH OA 7 .   ? -46.984 -3.745  5.222   1.00 34.25 ? 965  HOH B O   1 
HETATM 7393 O  O   . HOH OA 7 .   ? -39.683 18.131  -0.564  1.00 19.85 ? 966  HOH B O   1 
HETATM 7394 O  O   . HOH OA 7 .   ? -75.291 11.412  17.344  1.00 43.19 ? 967  HOH B O   1 
HETATM 7395 O  O   . HOH OA 7 .   ? -56.833 -13.449 -1.250  1.00 39.37 ? 968  HOH B O   1 
HETATM 7396 O  O   . HOH OA 7 .   ? -59.093 -17.451 -1.990  1.00 39.39 ? 969  HOH B O   1 
HETATM 7397 O  O   . HOH OA 7 .   ? -70.650 16.941  8.684   1.00 39.28 ? 970  HOH B O   1 
HETATM 7398 O  O   . HOH OA 7 .   ? -68.276 4.654   26.663  1.00 34.49 ? 971  HOH B O   1 
HETATM 7399 O  O   . HOH OA 7 .   ? -62.266 -6.070  -15.388 1.00 34.71 ? 972  HOH B O   1 
HETATM 7400 O  O   . HOH OA 7 .   ? -43.159 -5.656  14.274  1.00 39.64 ? 973  HOH B O   1 
HETATM 7401 O  O   . HOH OA 7 .   ? -74.627 6.440   23.960  1.00 36.55 ? 974  HOH B O   1 
HETATM 7402 O  O   . HOH OA 7 .   ? -72.523 4.416   -6.359  1.00 41.87 ? 975  HOH B O   1 
HETATM 7403 O  O   . HOH OA 7 .   ? -69.200 21.406  1.776   1.00 42.04 ? 976  HOH B O   1 
HETATM 7404 O  O   . HOH OA 7 .   ? -38.631 26.152  4.433   1.00 30.28 ? 977  HOH B O   1 
HETATM 7405 O  O   . HOH OA 7 .   ? -42.437 20.990  -19.628 1.00 37.77 ? 978  HOH B O   1 
HETATM 7406 O  O   . HOH OA 7 .   ? -71.749 -8.600  -15.265 1.00 40.59 ? 979  HOH B O   1 
HETATM 7407 O  O   . HOH OA 7 .   ? -65.463 31.226  -5.300  1.00 29.18 ? 980  HOH B O   1 
HETATM 7408 O  O   . HOH OA 7 .   ? -46.783 5.766   22.478  1.00 44.71 ? 981  HOH B O   1 
HETATM 7409 O  O   . HOH OA 7 .   ? -70.512 6.288   -9.171  1.00 45.16 ? 982  HOH B O   1 
HETATM 7410 O  O   . HOH OA 7 .   ? -70.957 12.580  -0.333  1.00 35.89 ? 983  HOH B O   1 
HETATM 7411 O  O   . HOH OA 7 .   ? -69.864 2.054   -14.114 1.00 42.03 ? 984  HOH B O   1 
HETATM 7412 O  O   . HOH OA 7 .   ? -64.872 -8.848  -13.060 1.00 22.13 ? 985  HOH B O   1 
HETATM 7413 O  O   . HOH OA 7 .   ? -39.329 18.735  2.223   1.00 40.98 ? 986  HOH B O   1 
HETATM 7414 O  O   . HOH OA 7 .   ? -54.722 -10.736 0.648   1.00 46.21 ? 987  HOH B O   1 
HETATM 7415 O  O   . HOH OA 7 .   ? -67.277 -17.755 15.844  1.00 49.88 ? 988  HOH B O   1 
HETATM 7416 O  O   . HOH OA 7 .   ? -64.017 9.329   24.083  1.00 32.41 ? 989  HOH B O   1 
HETATM 7417 O  O   . HOH OA 7 .   ? -71.646 10.048  6.765   1.00 41.52 ? 990  HOH B O   1 
HETATM 7418 O  O   . HOH OA 7 .   ? -66.144 -0.894  -17.977 1.00 46.99 ? 991  HOH B O   1 
HETATM 7419 O  O   . HOH OA 7 .   ? -58.037 -13.522 3.422   1.00 39.11 ? 992  HOH B O   1 
HETATM 7420 O  O   . HOH OA 7 .   ? -74.674 -10.677 15.573  1.00 37.52 ? 993  HOH B O   1 
HETATM 7421 O  O   . HOH OA 7 .   ? -56.428 -10.011 2.566   1.00 36.20 ? 994  HOH B O   1 
HETATM 7422 O  O   . HOH OA 7 .   ? -77.201 -1.827  7.105   1.00 33.43 ? 995  HOH B O   1 
HETATM 7423 O  O   . HOH OA 7 .   ? -61.133 -1.766  26.228  1.00 33.71 ? 996  HOH B O   1 
HETATM 7424 O  O   . HOH OA 7 .   ? -40.977 25.557  11.889  1.00 45.95 ? 997  HOH B O   1 
HETATM 7425 O  O   . HOH OA 7 .   ? -66.551 28.895  6.470   1.00 43.69 ? 998  HOH B O   1 
HETATM 7426 O  O   . HOH OA 7 .   ? -41.959 3.719   2.999   1.00 38.97 ? 999  HOH B O   1 
HETATM 7427 O  O   . HOH OA 7 .   ? -46.776 -7.060  -6.145  1.00 43.75 ? 1000 HOH B O   1 
HETATM 7428 O  O   . HOH OA 7 .   ? -43.958 1.325   8.722   1.00 45.87 ? 1001 HOH B O   1 
HETATM 7429 O  O   . HOH OA 7 .   ? -70.825 13.279  -17.356 1.00 30.23 ? 1002 HOH B O   1 
HETATM 7430 O  O   . HOH OA 7 .   ? -41.514 23.409  -20.439 1.00 42.19 ? 1003 HOH B O   1 
HETATM 7431 O  O   . HOH OA 7 .   ? -70.698 10.933  4.223   1.00 29.70 ? 1004 HOH B O   1 
HETATM 7432 O  O   . HOH OA 7 .   ? -50.315 29.668  -27.495 1.00 39.76 ? 1005 HOH B O   1 
HETATM 7433 O  O   . HOH OA 7 .   ? -75.899 29.222  -33.282 1.00 35.40 ? 1006 HOH B O   1 
HETATM 7434 O  O   . HOH OA 7 .   ? -73.866 -6.735  -15.680 1.00 45.67 ? 1007 HOH B O   1 
HETATM 7435 O  O   . HOH OA 7 .   ? -44.883 -6.151  6.831   1.00 52.01 ? 1008 HOH B O   1 
HETATM 7436 O  O   . HOH OA 7 .   ? -65.253 8.038   -16.387 1.00 42.41 ? 1009 HOH B O   1 
HETATM 7437 O  O   . HOH OA 7 .   ? -62.912 25.502  16.336  1.00 41.91 ? 1010 HOH B O   1 
HETATM 7438 O  O   . HOH OA 7 .   ? -77.724 -7.248  13.326  1.00 45.94 ? 1011 HOH B O   1 
HETATM 7439 O  O   . HOH OA 7 .   ? -35.200 15.986  0.954   1.00 38.20 ? 1012 HOH B O   1 
HETATM 7440 O  O   . HOH OA 7 .   ? -77.176 -10.401 16.596  1.00 42.12 ? 1013 HOH B O   1 
HETATM 7441 O  O   . HOH OA 7 .   ? -51.885 14.872  22.489  1.00 37.64 ? 1014 HOH B O   1 
HETATM 7442 O  O   . HOH OA 7 .   ? -67.976 25.298  7.236   1.00 35.16 ? 1015 HOH B O   1 
HETATM 7443 O  O   . HOH OA 7 .   ? -71.384 17.490  1.286   1.00 42.95 ? 1016 HOH B O   1 
HETATM 7444 O  O   . HOH OA 7 .   ? -69.840 23.711  2.959   1.00 40.10 ? 1017 HOH B O   1 
HETATM 7445 O  O   . HOH OA 7 .   ? -78.442 -3.860  10.744  1.00 34.49 ? 1018 HOH B O   1 
HETATM 7446 O  O   . HOH OA 7 .   ? -45.984 12.259  17.117  1.00 37.89 ? 1019 HOH B O   1 
HETATM 7447 O  O   . HOH OA 7 .   ? -55.088 17.500  23.774  1.00 37.01 ? 1020 HOH B O   1 
HETATM 7448 O  O   . HOH OA 7 .   ? -70.024 10.952  -16.615 1.00 34.54 ? 1021 HOH B O   1 
HETATM 7449 O  O   . HOH OA 7 .   ? -74.458 -8.777  10.900  1.00 40.33 ? 1022 HOH B O   1 
HETATM 7450 O  O   . HOH OA 7 .   ? -75.514 26.377  -14.741 1.00 27.80 ? 1023 HOH B O   1 
HETATM 7451 O  O   . HOH OA 7 .   ? -43.129 -1.122  16.914  1.00 43.57 ? 1024 HOH B O   1 
HETATM 7452 O  O   . HOH OA 7 .   ? -75.605 -6.090  -13.662 1.00 43.16 ? 1025 HOH B O   1 
HETATM 7453 O  O   . HOH OA 7 .   ? -77.682 27.598  -15.617 1.00 29.43 ? 1026 HOH B O   1 
HETATM 7454 O  O   . HOH OA 7 .   ? -61.253 31.782  4.844   1.00 38.62 ? 1027 HOH B O   1 
HETATM 7455 O  O   . HOH OA 7 .   ? -74.609 -1.343  -12.355 1.00 30.20 ? 1028 HOH B O   1 
HETATM 7456 O  O   . HOH OA 7 .   ? -42.832 4.272   5.418   1.00 33.02 ? 1029 HOH B O   1 
HETATM 7457 O  O   . HOH OA 7 .   ? -74.519 16.493  -1.864  1.00 41.88 ? 1030 HOH B O   1 
HETATM 7458 O  O   . HOH OA 7 .   ? -58.888 31.210  4.853   1.00 24.74 ? 1031 HOH B O   1 
HETATM 7459 O  O   . HOH OA 7 .   ? -74.140 26.648  -2.185  1.00 36.92 ? 1032 HOH B O   1 
HETATM 7460 O  O   . HOH OA 7 .   ? -76.518 14.460  -1.462  1.00 39.85 ? 1033 HOH B O   1 
HETATM 7461 O  O   . HOH OA 7 .   ? -61.415 38.682  -6.231  1.00 45.33 ? 1034 HOH B O   1 
HETATM 7462 O  O   . HOH OA 7 .   ? -67.661 2.225   -14.356 1.00 34.53 ? 1035 HOH B O   1 
HETATM 7463 O  O   . HOH OA 7 .   ? -47.732 15.935  20.721  1.00 41.71 ? 1036 HOH B O   1 
HETATM 7464 O  O   . HOH OA 7 .   ? -54.726 15.345  23.971  1.00 43.65 ? 1037 HOH B O   1 
# 
