data_9CJG
# 
_entry.id   9CJG 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9CJG         pdb_00009cjg 10.2210/pdb9cjg/pdb 
WWPDB D_1000272929 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-12 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CJG 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-06 
_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 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              katherine.davis@emory.edu 
_pdbx_contact_author.name_first         Katherine 
_pdbx_contact_author.name_last          Davis 
_pdbx_contact_author.name_mi            M 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0258-8907 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ireland, K.A.' 1 0000-0003-0986-5142 
'Davis, K.M.'   2 0000-0002-0258-8907 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Non-Canonical Cytochrome P450 Enzymes in Nature.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2024.12.22.630014 
_citation.pdbx_database_id_PubMed   39763895 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nguy, A.K.L.'         1 ? 
primary 'Ireland, K.A.'        2 ? 
primary 'Kayrouz, C.M.'        3 ? 
primary 'Caceres, J.C.'        4 ? 
primary 'Greene, B.L.'         5 ? 
primary 'Davis, K.M.'          6 ? 
primary 'Seyedsayamdost, M.R.' 7 ? 
# 
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 'Cytochrome P450-G9'              44429.207 2   1.14.-.- ? ? ? 
2 non-polymer nat 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   2   ?        ? ? ? 
3 non-polymer syn 'FORMIC ACID'                     46.025    2   ?        ? ? ? 
4 non-polymer syn 1-BUTANOL                         74.122    2   ?        ? ? ? 
5 water       nat water                             18.015    489 ?        ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMSELFGRAFHVDPYPIYARLRAGGGIRQVSTPDGAAAWVVTRYDDVRAGLADPRLSVDRS
NAGAGYRGFSLPPALDANLLNLDPPDHTRLRTLIAGEFTPRRVHELVPAIEAAARELLAGLPSGEPVDLIAGFAAPLPLR
VIGDLLGVPPADRARFRGWTTTLLTPGPDQPPTAARDAVVAMHGFLVDLVAAKRAEPGHDLLSGLIAVRDDEDRLSEAEL
VSMAFLALWAGYENLVHLIGNGVRALLAAPDQLADLRSDEALLPRAIEELTRFDQPLQWAIRRFPTRELDIAGVEVPAGD
TVLLGIASANHDETVFDLPDTLDLRRDPNPHLSYGHGIHRSFGSRLSQAEAAAAFSALLARGFRAAVDLADLQWQPSFRN
RGLTELPLLLG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMSELFGRAFHVDPYPIYARLRAGGGIRQVSTPDGAAAWVVTRYDDVRAGLADPRLSVDRS
NAGAGYRGFSLPPALDANLLNLDPPDHTRLRTLIAGEFTPRRVHELVPAIEAAARELLAGLPSGEPVDLIAGFAAPLPLR
VIGDLLGVPPADRARFRGWTTTLLTPGPDQPPTAARDAVVAMHGFLVDLVAAKRAEPGHDLLSGLIAVRDDEDRLSEAEL
VSMAFLALWAGYENLVHLIGNGVRALLAAPDQLADLRSDEALLPRAIEELTRFDQPLQWAIRRFPTRELDIAGVEVPAGD
TVLLGIASANHDETVFDLPDTLDLRRDPNPHLSYGHGIHRSFGSRLSQAEAAAAFSALLARGFRAAVDLADLQWQPSFRN
RGLTELPLLLG
;
_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 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
3 'FORMIC ACID'                     FMT 
4 1-BUTANOL                         1BO 
5 water                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  SER n 
1 23  GLU n 
1 24  LEU n 
1 25  PHE n 
1 26  GLY n 
1 27  ARG n 
1 28  ALA n 
1 29  PHE n 
1 30  HIS n 
1 31  VAL n 
1 32  ASP n 
1 33  PRO n 
1 34  TYR n 
1 35  PRO n 
1 36  ILE n 
1 37  TYR n 
1 38  ALA n 
1 39  ARG n 
1 40  LEU n 
1 41  ARG n 
1 42  ALA n 
1 43  GLY n 
1 44  GLY n 
1 45  GLY n 
1 46  ILE n 
1 47  ARG n 
1 48  GLN n 
1 49  VAL n 
1 50  SER n 
1 51  THR n 
1 52  PRO n 
1 53  ASP n 
1 54  GLY n 
1 55  ALA n 
1 56  ALA n 
1 57  ALA n 
1 58  TRP n 
1 59  VAL n 
1 60  VAL n 
1 61  THR n 
1 62  ARG n 
1 63  TYR n 
1 64  ASP n 
1 65  ASP n 
1 66  VAL n 
1 67  ARG n 
1 68  ALA n 
1 69  GLY n 
1 70  LEU n 
1 71  ALA n 
1 72  ASP n 
1 73  PRO n 
1 74  ARG n 
1 75  LEU n 
1 76  SER n 
1 77  VAL n 
1 78  ASP n 
1 79  ARG n 
1 80  SER n 
1 81  ASN n 
1 82  ALA n 
1 83  GLY n 
1 84  ALA n 
1 85  GLY n 
1 86  TYR n 
1 87  ARG n 
1 88  GLY n 
1 89  PHE n 
1 90  SER n 
1 91  LEU n 
1 92  PRO n 
1 93  PRO n 
1 94  ALA n 
1 95  LEU n 
1 96  ASP n 
1 97  ALA n 
1 98  ASN n 
1 99  LEU n 
1 100 LEU n 
1 101 ASN n 
1 102 LEU n 
1 103 ASP n 
1 104 PRO n 
1 105 PRO n 
1 106 ASP n 
1 107 HIS n 
1 108 THR n 
1 109 ARG n 
1 110 LEU n 
1 111 ARG n 
1 112 THR n 
1 113 LEU n 
1 114 ILE n 
1 115 ALA n 
1 116 GLY n 
1 117 GLU n 
1 118 PHE n 
1 119 THR n 
1 120 PRO n 
1 121 ARG n 
1 122 ARG n 
1 123 VAL n 
1 124 HIS n 
1 125 GLU n 
1 126 LEU n 
1 127 VAL n 
1 128 PRO n 
1 129 ALA n 
1 130 ILE n 
1 131 GLU n 
1 132 ALA n 
1 133 ALA n 
1 134 ALA n 
1 135 ARG n 
1 136 GLU n 
1 137 LEU n 
1 138 LEU n 
1 139 ALA n 
1 140 GLY n 
1 141 LEU n 
1 142 PRO n 
1 143 SER n 
1 144 GLY n 
1 145 GLU n 
1 146 PRO n 
1 147 VAL n 
1 148 ASP n 
1 149 LEU n 
1 150 ILE n 
1 151 ALA n 
1 152 GLY n 
1 153 PHE n 
1 154 ALA n 
1 155 ALA n 
1 156 PRO n 
1 157 LEU n 
1 158 PRO n 
1 159 LEU n 
1 160 ARG n 
1 161 VAL n 
1 162 ILE n 
1 163 GLY n 
1 164 ASP n 
1 165 LEU n 
1 166 LEU n 
1 167 GLY n 
1 168 VAL n 
1 169 PRO n 
1 170 PRO n 
1 171 ALA n 
1 172 ASP n 
1 173 ARG n 
1 174 ALA n 
1 175 ARG n 
1 176 PHE n 
1 177 ARG n 
1 178 GLY n 
1 179 TRP n 
1 180 THR n 
1 181 THR n 
1 182 THR n 
1 183 LEU n 
1 184 LEU n 
1 185 THR n 
1 186 PRO n 
1 187 GLY n 
1 188 PRO n 
1 189 ASP n 
1 190 GLN n 
1 191 PRO n 
1 192 PRO n 
1 193 THR n 
1 194 ALA n 
1 195 ALA n 
1 196 ARG n 
1 197 ASP n 
1 198 ALA n 
1 199 VAL n 
1 200 VAL n 
1 201 ALA n 
1 202 MET n 
1 203 HIS n 
1 204 GLY n 
1 205 PHE n 
1 206 LEU n 
1 207 VAL n 
1 208 ASP n 
1 209 LEU n 
1 210 VAL n 
1 211 ALA n 
1 212 ALA n 
1 213 LYS n 
1 214 ARG n 
1 215 ALA n 
1 216 GLU n 
1 217 PRO n 
1 218 GLY n 
1 219 HIS n 
1 220 ASP n 
1 221 LEU n 
1 222 LEU n 
1 223 SER n 
1 224 GLY n 
1 225 LEU n 
1 226 ILE n 
1 227 ALA n 
1 228 VAL n 
1 229 ARG n 
1 230 ASP n 
1 231 ASP n 
1 232 GLU n 
1 233 ASP n 
1 234 ARG n 
1 235 LEU n 
1 236 SER n 
1 237 GLU n 
1 238 ALA n 
1 239 GLU n 
1 240 LEU n 
1 241 VAL n 
1 242 SER n 
1 243 MET n 
1 244 ALA n 
1 245 PHE n 
1 246 LEU n 
1 247 ALA n 
1 248 LEU n 
1 249 TRP n 
1 250 ALA n 
1 251 GLY n 
1 252 TYR n 
1 253 GLU n 
1 254 ASN n 
1 255 LEU n 
1 256 VAL n 
1 257 HIS n 
1 258 LEU n 
1 259 ILE n 
1 260 GLY n 
1 261 ASN n 
1 262 GLY n 
1 263 VAL n 
1 264 ARG n 
1 265 ALA n 
1 266 LEU n 
1 267 LEU n 
1 268 ALA n 
1 269 ALA n 
1 270 PRO n 
1 271 ASP n 
1 272 GLN n 
1 273 LEU n 
1 274 ALA n 
1 275 ASP n 
1 276 LEU n 
1 277 ARG n 
1 278 SER n 
1 279 ASP n 
1 280 GLU n 
1 281 ALA n 
1 282 LEU n 
1 283 LEU n 
1 284 PRO n 
1 285 ARG n 
1 286 ALA n 
1 287 ILE n 
1 288 GLU n 
1 289 GLU n 
1 290 LEU n 
1 291 THR n 
1 292 ARG n 
1 293 PHE n 
1 294 ASP n 
1 295 GLN n 
1 296 PRO n 
1 297 LEU n 
1 298 GLN n 
1 299 TRP n 
1 300 ALA n 
1 301 ILE n 
1 302 ARG n 
1 303 ARG n 
1 304 PHE n 
1 305 PRO n 
1 306 THR n 
1 307 ARG n 
1 308 GLU n 
1 309 LEU n 
1 310 ASP n 
1 311 ILE n 
1 312 ALA n 
1 313 GLY n 
1 314 VAL n 
1 315 GLU n 
1 316 VAL n 
1 317 PRO n 
1 318 ALA n 
1 319 GLY n 
1 320 ASP n 
1 321 THR n 
1 322 VAL n 
1 323 LEU n 
1 324 LEU n 
1 325 GLY n 
1 326 ILE n 
1 327 ALA n 
1 328 SER n 
1 329 ALA n 
1 330 ASN n 
1 331 HIS n 
1 332 ASP n 
1 333 GLU n 
1 334 THR n 
1 335 VAL n 
1 336 PHE n 
1 337 ASP n 
1 338 LEU n 
1 339 PRO n 
1 340 ASP n 
1 341 THR n 
1 342 LEU n 
1 343 ASP n 
1 344 LEU n 
1 345 ARG n 
1 346 ARG n 
1 347 ASP n 
1 348 PRO n 
1 349 ASN n 
1 350 PRO n 
1 351 HIS n 
1 352 LEU n 
1 353 SER n 
1 354 TYR n 
1 355 GLY n 
1 356 HIS n 
1 357 GLY n 
1 358 ILE n 
1 359 HIS n 
1 360 ARG n 
1 361 SER n 
1 362 PHE n 
1 363 GLY n 
1 364 SER n 
1 365 ARG n 
1 366 LEU n 
1 367 SER n 
1 368 GLN n 
1 369 ALA n 
1 370 GLU n 
1 371 ALA n 
1 372 ALA n 
1 373 ALA n 
1 374 ALA n 
1 375 PHE n 
1 376 SER n 
1 377 ALA n 
1 378 LEU n 
1 379 LEU n 
1 380 ALA n 
1 381 ARG n 
1 382 GLY n 
1 383 PHE n 
1 384 ARG n 
1 385 ALA n 
1 386 ALA n 
1 387 VAL n 
1 388 ASP n 
1 389 LEU n 
1 390 ALA n 
1 391 ASP n 
1 392 LEU n 
1 393 GLN n 
1 394 TRP n 
1 395 GLN n 
1 396 PRO n 
1 397 SER n 
1 398 PHE n 
1 399 ARG n 
1 400 ASN n 
1 401 ARG n 
1 402 GLY n 
1 403 LEU n 
1 404 THR n 
1 405 GLU n 
1 406 LEU n 
1 407 PRO n 
1 408 LEU n 
1 409 LEU n 
1 410 LEU n 
1 411 GLY 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                   411 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SAMN04487818_101238 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Actinokineospora terrae' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     155974 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
1BO non-polymer         . 1-BUTANOL                         BUTAN-1-OL 'C4 H10 O'         74.122  
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 
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  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME       'C34 H32 Fe N4 O4' 616.487 
HIS 'L-peptide linking' y HISTIDINE                         ?          'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                             ?          'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                        ?          'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                           ?          'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                            ?          'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                        ?          'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                     ?          'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                           ?          'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                            ?          'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                         ?          'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ?          'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                          ?          'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                            ?          'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  LEU 14  -6  ?   ?   ?   A . n 
A 1 15  VAL 15  -5  ?   ?   ?   A . n 
A 1 16  PRO 16  -4  ?   ?   ?   A . n 
A 1 17  ARG 17  -3  ?   ?   ?   A . n 
A 1 18  GLY 18  -2  ?   ?   ?   A . n 
A 1 19  SER 19  -1  ?   ?   ?   A . n 
A 1 20  HIS 20  0   ?   ?   ?   A . n 
A 1 21  MET 21  1   ?   ?   ?   A . n 
A 1 22  SER 22  2   ?   ?   ?   A . n 
A 1 23  GLU 23  3   ?   ?   ?   A . n 
A 1 24  LEU 24  4   4   LEU LEU A . n 
A 1 25  PHE 25  5   5   PHE PHE A . n 
A 1 26  GLY 26  6   6   GLY GLY A . n 
A 1 27  ARG 27  7   7   ARG ARG A . n 
A 1 28  ALA 28  8   8   ALA ALA A . n 
A 1 29  PHE 29  9   9   PHE PHE A . n 
A 1 30  HIS 30  10  10  HIS HIS A . n 
A 1 31  VAL 31  11  11  VAL VAL A . n 
A 1 32  ASP 32  12  12  ASP ASP A . n 
A 1 33  PRO 33  13  13  PRO PRO A . n 
A 1 34  TYR 34  14  14  TYR TYR A . n 
A 1 35  PRO 35  15  15  PRO PRO A . n 
A 1 36  ILE 36  16  16  ILE ILE A . n 
A 1 37  TYR 37  17  17  TYR TYR A . n 
A 1 38  ALA 38  18  18  ALA ALA A . n 
A 1 39  ARG 39  19  19  ARG ARG A . n 
A 1 40  LEU 40  20  20  LEU LEU A . n 
A 1 41  ARG 41  21  21  ARG ARG A . n 
A 1 42  ALA 42  22  22  ALA ALA A . n 
A 1 43  GLY 43  23  23  GLY GLY A . n 
A 1 44  GLY 44  24  24  GLY GLY A . n 
A 1 45  GLY 45  25  25  GLY GLY A . n 
A 1 46  ILE 46  26  26  ILE ILE A . n 
A 1 47  ARG 47  27  27  ARG ARG A . n 
A 1 48  GLN 48  28  28  GLN GLN A . n 
A 1 49  VAL 49  29  29  VAL VAL A . n 
A 1 50  SER 50  30  30  SER SER A . n 
A 1 51  THR 51  31  31  THR THR A . n 
A 1 52  PRO 52  32  32  PRO PRO A . n 
A 1 53  ASP 53  33  33  ASP ASP A . n 
A 1 54  GLY 54  34  34  GLY GLY A . n 
A 1 55  ALA 55  35  35  ALA ALA A . n 
A 1 56  ALA 56  36  36  ALA ALA A . n 
A 1 57  ALA 57  37  37  ALA ALA A . n 
A 1 58  TRP 58  38  38  TRP TRP A . n 
A 1 59  VAL 59  39  39  VAL VAL A . n 
A 1 60  VAL 60  40  40  VAL VAL A . n 
A 1 61  THR 61  41  41  THR THR A . n 
A 1 62  ARG 62  42  42  ARG ARG A . n 
A 1 63  TYR 63  43  43  TYR TYR A . n 
A 1 64  ASP 64  44  44  ASP ASP A . n 
A 1 65  ASP 65  45  45  ASP ASP A . n 
A 1 66  VAL 66  46  46  VAL VAL A . n 
A 1 67  ARG 67  47  47  ARG ARG A . n 
A 1 68  ALA 68  48  48  ALA ALA A . n 
A 1 69  GLY 69  49  49  GLY GLY A . n 
A 1 70  LEU 70  50  50  LEU LEU A . n 
A 1 71  ALA 71  51  51  ALA ALA A . n 
A 1 72  ASP 72  52  52  ASP ASP A . n 
A 1 73  PRO 73  53  53  PRO PRO A . n 
A 1 74  ARG 74  54  54  ARG ARG A . n 
A 1 75  LEU 75  55  55  LEU LEU A . n 
A 1 76  SER 76  56  56  SER SER A . n 
A 1 77  VAL 77  57  57  VAL VAL A . n 
A 1 78  ASP 78  58  58  ASP ASP A . n 
A 1 79  ARG 79  59  59  ARG ARG A . n 
A 1 80  SER 80  60  60  SER SER A . n 
A 1 81  ASN 81  61  61  ASN ASN A . n 
A 1 82  ALA 82  62  62  ALA ALA A . n 
A 1 83  GLY 83  63  63  GLY GLY A . n 
A 1 84  ALA 84  64  64  ALA ALA A . n 
A 1 85  GLY 85  65  65  GLY GLY A . n 
A 1 86  TYR 86  66  66  TYR TYR A . n 
A 1 87  ARG 87  67  67  ARG ARG A . n 
A 1 88  GLY 88  68  68  GLY GLY A . n 
A 1 89  PHE 89  69  69  PHE PHE A . n 
A 1 90  SER 90  70  70  SER SER A . n 
A 1 91  LEU 91  71  71  LEU LEU A . n 
A 1 92  PRO 92  72  72  PRO PRO A . n 
A 1 93  PRO 93  73  73  PRO PRO A . n 
A 1 94  ALA 94  74  74  ALA ALA A . n 
A 1 95  LEU 95  75  75  LEU LEU A . n 
A 1 96  ASP 96  76  76  ASP ASP A . n 
A 1 97  ALA 97  77  77  ALA ALA A . n 
A 1 98  ASN 98  78  78  ASN ASN A . n 
A 1 99  LEU 99  79  79  LEU LEU A . n 
A 1 100 LEU 100 80  80  LEU LEU A . n 
A 1 101 ASN 101 81  81  ASN ASN A . n 
A 1 102 LEU 102 82  82  LEU LEU A . n 
A 1 103 ASP 103 83  83  ASP ASP A . n 
A 1 104 PRO 104 84  84  PRO PRO A . n 
A 1 105 PRO 105 85  85  PRO PRO A . n 
A 1 106 ASP 106 86  86  ASP ASP A . n 
A 1 107 HIS 107 87  87  HIS HIS A . n 
A 1 108 THR 108 88  88  THR THR A . n 
A 1 109 ARG 109 89  89  ARG ARG A . n 
A 1 110 LEU 110 90  90  LEU LEU A . n 
A 1 111 ARG 111 91  91  ARG ARG A . n 
A 1 112 THR 112 92  92  THR THR A . n 
A 1 113 LEU 113 93  93  LEU LEU A . n 
A 1 114 ILE 114 94  94  ILE ILE A . n 
A 1 115 ALA 115 95  95  ALA ALA A . n 
A 1 116 GLY 116 96  96  GLY GLY A . n 
A 1 117 GLU 117 97  97  GLU GLU A . n 
A 1 118 PHE 118 98  98  PHE PHE A . n 
A 1 119 THR 119 99  99  THR THR A . n 
A 1 120 PRO 120 100 100 PRO PRO A . n 
A 1 121 ARG 121 101 101 ARG ARG A . n 
A 1 122 ARG 122 102 102 ARG ARG A . n 
A 1 123 VAL 123 103 103 VAL VAL A . n 
A 1 124 HIS 124 104 104 HIS HIS A . n 
A 1 125 GLU 125 105 105 GLU GLU A . n 
A 1 126 LEU 126 106 106 LEU LEU A . n 
A 1 127 VAL 127 107 107 VAL VAL A . n 
A 1 128 PRO 128 108 108 PRO PRO A . n 
A 1 129 ALA 129 109 109 ALA ALA A . n 
A 1 130 ILE 130 110 110 ILE ILE A . n 
A 1 131 GLU 131 111 111 GLU GLU A . n 
A 1 132 ALA 132 112 112 ALA ALA A . n 
A 1 133 ALA 133 113 113 ALA ALA A . n 
A 1 134 ALA 134 114 114 ALA ALA A . n 
A 1 135 ARG 135 115 115 ARG ARG A . n 
A 1 136 GLU 136 116 116 GLU GLU A . n 
A 1 137 LEU 137 117 117 LEU LEU A . n 
A 1 138 LEU 138 118 118 LEU LEU A . n 
A 1 139 ALA 139 119 119 ALA ALA A . n 
A 1 140 GLY 140 120 120 GLY GLY A . n 
A 1 141 LEU 141 121 121 LEU LEU A . n 
A 1 142 PRO 142 122 122 PRO PRO A . n 
A 1 143 SER 143 123 123 SER SER A . n 
A 1 144 GLY 144 124 124 GLY GLY A . n 
A 1 145 GLU 145 125 125 GLU GLU A . n 
A 1 146 PRO 146 126 126 PRO PRO A . n 
A 1 147 VAL 147 127 127 VAL VAL A . n 
A 1 148 ASP 148 128 128 ASP ASP A . n 
A 1 149 LEU 149 129 129 LEU LEU A . n 
A 1 150 ILE 150 130 130 ILE ILE A . n 
A 1 151 ALA 151 131 131 ALA ALA A . n 
A 1 152 GLY 152 132 132 GLY GLY A . n 
A 1 153 PHE 153 133 133 PHE PHE A . n 
A 1 154 ALA 154 134 134 ALA ALA A . n 
A 1 155 ALA 155 135 135 ALA ALA A . n 
A 1 156 PRO 156 136 136 PRO PRO A . n 
A 1 157 LEU 157 137 137 LEU LEU A . n 
A 1 158 PRO 158 138 138 PRO PRO A . n 
A 1 159 LEU 159 139 139 LEU LEU A . n 
A 1 160 ARG 160 140 140 ARG ARG A . n 
A 1 161 VAL 161 141 141 VAL VAL A . n 
A 1 162 ILE 162 142 142 ILE ILE A . n 
A 1 163 GLY 163 143 143 GLY GLY A . n 
A 1 164 ASP 164 144 144 ASP ASP A . n 
A 1 165 LEU 165 145 145 LEU LEU A . n 
A 1 166 LEU 166 146 146 LEU LEU A . n 
A 1 167 GLY 167 147 147 GLY GLY A . n 
A 1 168 VAL 168 148 148 VAL VAL A . n 
A 1 169 PRO 169 149 149 PRO PRO A . n 
A 1 170 PRO 170 150 150 PRO PRO A . n 
A 1 171 ALA 171 151 151 ALA ALA A . n 
A 1 172 ASP 172 152 152 ASP ASP A . n 
A 1 173 ARG 173 153 153 ARG ARG A . n 
A 1 174 ALA 174 154 154 ALA ALA A . n 
A 1 175 ARG 175 155 155 ARG ARG A . n 
A 1 176 PHE 176 156 156 PHE PHE A . n 
A 1 177 ARG 177 157 157 ARG ARG A . n 
A 1 178 GLY 178 158 158 GLY GLY A . n 
A 1 179 TRP 179 159 159 TRP TRP A . n 
A 1 180 THR 180 160 160 THR THR A . n 
A 1 181 THR 181 161 161 THR THR A . n 
A 1 182 THR 182 162 162 THR THR A . n 
A 1 183 LEU 183 163 163 LEU LEU A . n 
A 1 184 LEU 184 164 164 LEU LEU A . n 
A 1 185 THR 185 165 165 THR THR A . n 
A 1 186 PRO 186 166 166 PRO PRO A . n 
A 1 187 GLY 187 167 167 GLY GLY A . n 
A 1 188 PRO 188 168 168 PRO PRO A . n 
A 1 189 ASP 189 169 169 ASP ASP A . n 
A 1 190 GLN 190 170 170 GLN GLN A . n 
A 1 191 PRO 191 171 171 PRO PRO A . n 
A 1 192 PRO 192 172 172 PRO PRO A . n 
A 1 193 THR 193 173 173 THR THR A . n 
A 1 194 ALA 194 174 174 ALA ALA A . n 
A 1 195 ALA 195 175 175 ALA ALA A . n 
A 1 196 ARG 196 176 176 ARG ARG A . n 
A 1 197 ASP 197 177 177 ASP ASP A . n 
A 1 198 ALA 198 178 178 ALA ALA A . n 
A 1 199 VAL 199 179 179 VAL VAL A . n 
A 1 200 VAL 200 180 180 VAL VAL A . n 
A 1 201 ALA 201 181 181 ALA ALA A . n 
A 1 202 MET 202 182 182 MET MET A . n 
A 1 203 HIS 203 183 183 HIS HIS A . n 
A 1 204 GLY 204 184 184 GLY GLY A . n 
A 1 205 PHE 205 185 185 PHE PHE A . n 
A 1 206 LEU 206 186 186 LEU LEU A . n 
A 1 207 VAL 207 187 187 VAL VAL A . n 
A 1 208 ASP 208 188 188 ASP ASP A . n 
A 1 209 LEU 209 189 189 LEU LEU A . n 
A 1 210 VAL 210 190 190 VAL VAL A . n 
A 1 211 ALA 211 191 191 ALA ALA A . n 
A 1 212 ALA 212 192 192 ALA ALA A . n 
A 1 213 LYS 213 193 193 LYS LYS A . n 
A 1 214 ARG 214 194 194 ARG ARG A . n 
A 1 215 ALA 215 195 195 ALA ALA A . n 
A 1 216 GLU 216 196 196 GLU GLU A . n 
A 1 217 PRO 217 197 197 PRO PRO A . n 
A 1 218 GLY 218 198 198 GLY GLY A . n 
A 1 219 HIS 219 199 199 HIS HIS A . n 
A 1 220 ASP 220 200 200 ASP ASP A . n 
A 1 221 LEU 221 201 201 LEU LEU A . n 
A 1 222 LEU 222 202 202 LEU LEU A . n 
A 1 223 SER 223 203 203 SER SER A . n 
A 1 224 GLY 224 204 204 GLY GLY A . n 
A 1 225 LEU 225 205 205 LEU LEU A . n 
A 1 226 ILE 226 206 206 ILE ILE A . n 
A 1 227 ALA 227 207 207 ALA ALA A . n 
A 1 228 VAL 228 208 208 VAL VAL A . n 
A 1 229 ARG 229 209 209 ARG ARG A . n 
A 1 230 ASP 230 210 210 ASP ASP A . n 
A 1 231 ASP 231 211 211 ASP ASP A . n 
A 1 232 GLU 232 212 212 GLU GLU A . n 
A 1 233 ASP 233 213 213 ASP ASP A . n 
A 1 234 ARG 234 214 214 ARG ARG A . n 
A 1 235 LEU 235 215 215 LEU LEU A . n 
A 1 236 SER 236 216 216 SER SER A . n 
A 1 237 GLU 237 217 217 GLU GLU A . n 
A 1 238 ALA 238 218 218 ALA ALA A . n 
A 1 239 GLU 239 219 219 GLU GLU A . n 
A 1 240 LEU 240 220 220 LEU LEU A . n 
A 1 241 VAL 241 221 221 VAL VAL A . n 
A 1 242 SER 242 222 222 SER SER A . n 
A 1 243 MET 243 223 223 MET MET A . n 
A 1 244 ALA 244 224 224 ALA ALA A . n 
A 1 245 PHE 245 225 225 PHE PHE A . n 
A 1 246 LEU 246 226 226 LEU LEU A . n 
A 1 247 ALA 247 227 227 ALA ALA A . n 
A 1 248 LEU 248 228 228 LEU LEU A . n 
A 1 249 TRP 249 229 229 TRP TRP A . n 
A 1 250 ALA 250 230 230 ALA ALA A . n 
A 1 251 GLY 251 231 231 GLY GLY A . n 
A 1 252 TYR 252 232 232 TYR TYR A . n 
A 1 253 GLU 253 233 233 GLU GLU A . n 
A 1 254 ASN 254 234 234 ASN ASN A . n 
A 1 255 LEU 255 235 235 LEU LEU A . n 
A 1 256 VAL 256 236 236 VAL VAL A . n 
A 1 257 HIS 257 237 237 HIS HIS A . n 
A 1 258 LEU 258 238 238 LEU LEU A . n 
A 1 259 ILE 259 239 239 ILE ILE A . n 
A 1 260 GLY 260 240 240 GLY GLY A . n 
A 1 261 ASN 261 241 241 ASN ASN A . n 
A 1 262 GLY 262 242 242 GLY GLY A . n 
A 1 263 VAL 263 243 243 VAL VAL A . n 
A 1 264 ARG 264 244 244 ARG ARG A . n 
A 1 265 ALA 265 245 245 ALA ALA A . n 
A 1 266 LEU 266 246 246 LEU LEU A . n 
A 1 267 LEU 267 247 247 LEU LEU A . n 
A 1 268 ALA 268 248 248 ALA ALA A . n 
A 1 269 ALA 269 249 249 ALA ALA A . n 
A 1 270 PRO 270 250 250 PRO PRO A . n 
A 1 271 ASP 271 251 251 ASP ASP A . n 
A 1 272 GLN 272 252 252 GLN GLN A . n 
A 1 273 LEU 273 253 253 LEU LEU A . n 
A 1 274 ALA 274 254 254 ALA ALA A . n 
A 1 275 ASP 275 255 255 ASP ASP A . n 
A 1 276 LEU 276 256 256 LEU LEU A . n 
A 1 277 ARG 277 257 257 ARG ARG A . n 
A 1 278 SER 278 258 258 SER SER A . n 
A 1 279 ASP 279 259 259 ASP ASP A . n 
A 1 280 GLU 280 260 260 GLU GLU A . n 
A 1 281 ALA 281 261 261 ALA ALA A . n 
A 1 282 LEU 282 262 262 LEU LEU A . n 
A 1 283 LEU 283 263 263 LEU LEU A . n 
A 1 284 PRO 284 264 264 PRO PRO A . n 
A 1 285 ARG 285 265 265 ARG ARG A . n 
A 1 286 ALA 286 266 266 ALA ALA A . n 
A 1 287 ILE 287 267 267 ILE ILE A . n 
A 1 288 GLU 288 268 268 GLU GLU A . n 
A 1 289 GLU 289 269 269 GLU GLU A . n 
A 1 290 LEU 290 270 270 LEU LEU A . n 
A 1 291 THR 291 271 271 THR THR A . n 
A 1 292 ARG 292 272 272 ARG ARG A . n 
A 1 293 PHE 293 273 273 PHE PHE A . n 
A 1 294 ASP 294 274 274 ASP ASP A . n 
A 1 295 GLN 295 275 275 GLN GLN A . n 
A 1 296 PRO 296 276 276 PRO PRO A . n 
A 1 297 LEU 297 277 277 LEU LEU A . n 
A 1 298 GLN 298 278 278 GLN GLN A . n 
A 1 299 TRP 299 279 279 TRP TRP A . n 
A 1 300 ALA 300 280 280 ALA ALA A . n 
A 1 301 ILE 301 281 281 ILE ILE A . n 
A 1 302 ARG 302 282 282 ARG ARG A . n 
A 1 303 ARG 303 283 283 ARG ARG A . n 
A 1 304 PHE 304 284 284 PHE PHE A . n 
A 1 305 PRO 305 285 285 PRO PRO A . n 
A 1 306 THR 306 286 286 THR THR A . n 
A 1 307 ARG 307 287 287 ARG ARG A . n 
A 1 308 GLU 308 288 288 GLU GLU A . n 
A 1 309 LEU 309 289 289 LEU LEU A . n 
A 1 310 ASP 310 290 290 ASP ASP A . n 
A 1 311 ILE 311 291 291 ILE ILE A . n 
A 1 312 ALA 312 292 292 ALA ALA A . n 
A 1 313 GLY 313 293 293 GLY GLY A . n 
A 1 314 VAL 314 294 294 VAL VAL A . n 
A 1 315 GLU 315 295 295 GLU GLU A . n 
A 1 316 VAL 316 296 296 VAL VAL A . n 
A 1 317 PRO 317 297 297 PRO PRO A . n 
A 1 318 ALA 318 298 298 ALA ALA A . n 
A 1 319 GLY 319 299 299 GLY GLY A . n 
A 1 320 ASP 320 300 300 ASP ASP A . n 
A 1 321 THR 321 301 301 THR THR A . n 
A 1 322 VAL 322 302 302 VAL VAL A . n 
A 1 323 LEU 323 303 303 LEU LEU A . n 
A 1 324 LEU 324 304 304 LEU LEU A . n 
A 1 325 GLY 325 305 305 GLY GLY A . n 
A 1 326 ILE 326 306 306 ILE ILE A . n 
A 1 327 ALA 327 307 307 ALA ALA A . n 
A 1 328 SER 328 308 308 SER SER A . n 
A 1 329 ALA 329 309 309 ALA ALA A . n 
A 1 330 ASN 330 310 310 ASN ASN A . n 
A 1 331 HIS 331 311 311 HIS HIS A . n 
A 1 332 ASP 332 312 312 ASP ASP A . n 
A 1 333 GLU 333 313 313 GLU GLU A . n 
A 1 334 THR 334 314 314 THR THR A . n 
A 1 335 VAL 335 315 315 VAL VAL A . n 
A 1 336 PHE 336 316 316 PHE PHE A . n 
A 1 337 ASP 337 317 317 ASP ASP A . n 
A 1 338 LEU 338 318 318 LEU LEU A . n 
A 1 339 PRO 339 319 319 PRO PRO A . n 
A 1 340 ASP 340 320 320 ASP ASP A . n 
A 1 341 THR 341 321 321 THR THR A . n 
A 1 342 LEU 342 322 322 LEU LEU A . n 
A 1 343 ASP 343 323 323 ASP ASP A . n 
A 1 344 LEU 344 324 324 LEU LEU A . n 
A 1 345 ARG 345 325 325 ARG ARG A . n 
A 1 346 ARG 346 326 326 ARG ARG A . n 
A 1 347 ASP 347 327 327 ASP ASP A . n 
A 1 348 PRO 348 328 328 PRO PRO A . n 
A 1 349 ASN 349 329 329 ASN ASN A . n 
A 1 350 PRO 350 330 330 PRO PRO A . n 
A 1 351 HIS 351 331 331 HIS HIS A . n 
A 1 352 LEU 352 332 332 LEU LEU A . n 
A 1 353 SER 353 333 333 SER SER A . n 
A 1 354 TYR 354 334 334 TYR TYR A . n 
A 1 355 GLY 355 335 335 GLY GLY A . n 
A 1 356 HIS 356 336 336 HIS HIS A . n 
A 1 357 GLY 357 337 337 GLY GLY A . n 
A 1 358 ILE 358 338 338 ILE ILE A . n 
A 1 359 HIS 359 339 339 HIS HIS A . n 
A 1 360 ARG 360 340 340 ARG ARG A . n 
A 1 361 SER 361 341 341 SER SER A . n 
A 1 362 PHE 362 342 342 PHE PHE A . n 
A 1 363 GLY 363 343 343 GLY GLY A . n 
A 1 364 SER 364 344 344 SER SER A . n 
A 1 365 ARG 365 345 345 ARG ARG A . n 
A 1 366 LEU 366 346 346 LEU LEU A . n 
A 1 367 SER 367 347 347 SER SER A . n 
A 1 368 GLN 368 348 348 GLN GLN A . n 
A 1 369 ALA 369 349 349 ALA ALA A . n 
A 1 370 GLU 370 350 350 GLU GLU A . n 
A 1 371 ALA 371 351 351 ALA ALA A . n 
A 1 372 ALA 372 352 352 ALA ALA A . n 
A 1 373 ALA 373 353 353 ALA ALA A . n 
A 1 374 ALA 374 354 354 ALA ALA A . n 
A 1 375 PHE 375 355 355 PHE PHE A . n 
A 1 376 SER 376 356 356 SER SER A . n 
A 1 377 ALA 377 357 357 ALA ALA A . n 
A 1 378 LEU 378 358 358 LEU LEU A . n 
A 1 379 LEU 379 359 359 LEU LEU A . n 
A 1 380 ALA 380 360 360 ALA ALA A . n 
A 1 381 ARG 381 361 361 ARG ARG A . n 
A 1 382 GLY 382 362 362 GLY GLY A . n 
A 1 383 PHE 383 363 363 PHE PHE A . n 
A 1 384 ARG 384 364 364 ARG ARG A . n 
A 1 385 ALA 385 365 365 ALA ALA A . n 
A 1 386 ALA 386 366 366 ALA ALA A . n 
A 1 387 VAL 387 367 367 VAL VAL A . n 
A 1 388 ASP 388 368 368 ASP ASP A . n 
A 1 389 LEU 389 369 369 LEU LEU A . n 
A 1 390 ALA 390 370 370 ALA ALA A . n 
A 1 391 ASP 391 371 371 ASP ASP A . n 
A 1 392 LEU 392 372 372 LEU LEU A . n 
A 1 393 GLN 393 373 373 GLN GLN A . n 
A 1 394 TRP 394 374 374 TRP TRP A . n 
A 1 395 GLN 395 375 375 GLN GLN A . n 
A 1 396 PRO 396 376 376 PRO PRO A . n 
A 1 397 SER 397 377 377 SER SER A . n 
A 1 398 PHE 398 378 378 PHE PHE A . n 
A 1 399 ARG 399 379 379 ARG ARG A . n 
A 1 400 ASN 400 380 380 ASN ASN A . n 
A 1 401 ARG 401 381 381 ARG ARG A . n 
A 1 402 GLY 402 382 382 GLY GLY A . n 
A 1 403 LEU 403 383 383 LEU LEU A . n 
A 1 404 THR 404 384 384 THR THR A . n 
A 1 405 GLU 405 385 385 GLU GLU A . n 
A 1 406 LEU 406 386 386 LEU LEU A . n 
A 1 407 PRO 407 387 387 PRO PRO A . n 
A 1 408 LEU 408 388 388 LEU LEU A . n 
A 1 409 LEU 409 389 389 LEU LEU A . n 
A 1 410 LEU 410 390 390 LEU LEU A . n 
A 1 411 GLY 411 391 391 GLY GLY A . n 
B 1 1   MET 1   -19 ?   ?   ?   B . n 
B 1 2   GLY 2   -18 ?   ?   ?   B . n 
B 1 3   SER 3   -17 ?   ?   ?   B . n 
B 1 4   SER 4   -16 ?   ?   ?   B . n 
B 1 5   HIS 5   -15 ?   ?   ?   B . n 
B 1 6   HIS 6   -14 ?   ?   ?   B . n 
B 1 7   HIS 7   -13 ?   ?   ?   B . n 
B 1 8   HIS 8   -12 ?   ?   ?   B . n 
B 1 9   HIS 9   -11 ?   ?   ?   B . n 
B 1 10  HIS 10  -10 ?   ?   ?   B . n 
B 1 11  SER 11  -9  ?   ?   ?   B . n 
B 1 12  SER 12  -8  ?   ?   ?   B . n 
B 1 13  GLY 13  -7  ?   ?   ?   B . n 
B 1 14  LEU 14  -6  ?   ?   ?   B . n 
B 1 15  VAL 15  -5  ?   ?   ?   B . n 
B 1 16  PRO 16  -4  ?   ?   ?   B . n 
B 1 17  ARG 17  -3  ?   ?   ?   B . n 
B 1 18  GLY 18  -2  ?   ?   ?   B . n 
B 1 19  SER 19  -1  ?   ?   ?   B . n 
B 1 20  HIS 20  0   ?   ?   ?   B . n 
B 1 21  MET 21  1   ?   ?   ?   B . n 
B 1 22  SER 22  2   ?   ?   ?   B . n 
B 1 23  GLU 23  3   ?   ?   ?   B . n 
B 1 24  LEU 24  4   ?   ?   ?   B . n 
B 1 25  PHE 25  5   ?   ?   ?   B . n 
B 1 26  GLY 26  6   ?   ?   ?   B . n 
B 1 27  ARG 27  7   ?   ?   ?   B . n 
B 1 28  ALA 28  8   8   ALA ALA B . n 
B 1 29  PHE 29  9   9   PHE PHE B . n 
B 1 30  HIS 30  10  10  HIS HIS B . n 
B 1 31  VAL 31  11  11  VAL VAL B . n 
B 1 32  ASP 32  12  12  ASP ASP B . n 
B 1 33  PRO 33  13  13  PRO PRO B . n 
B 1 34  TYR 34  14  14  TYR TYR B . n 
B 1 35  PRO 35  15  15  PRO PRO B . n 
B 1 36  ILE 36  16  16  ILE ILE B . n 
B 1 37  TYR 37  17  17  TYR TYR B . n 
B 1 38  ALA 38  18  18  ALA ALA B . n 
B 1 39  ARG 39  19  19  ARG ARG B . n 
B 1 40  LEU 40  20  20  LEU LEU B . n 
B 1 41  ARG 41  21  21  ARG ARG B . n 
B 1 42  ALA 42  22  22  ALA ALA B . n 
B 1 43  GLY 43  23  23  GLY GLY B . n 
B 1 44  GLY 44  24  24  GLY GLY B . n 
B 1 45  GLY 45  25  25  GLY GLY B . n 
B 1 46  ILE 46  26  26  ILE ILE B . n 
B 1 47  ARG 47  27  27  ARG ARG B . n 
B 1 48  GLN 48  28  28  GLN GLN B . n 
B 1 49  VAL 49  29  29  VAL VAL B . n 
B 1 50  SER 50  30  30  SER SER B . n 
B 1 51  THR 51  31  31  THR THR B . n 
B 1 52  PRO 52  32  32  PRO PRO B . n 
B 1 53  ASP 53  33  33  ASP ASP B . n 
B 1 54  GLY 54  34  34  GLY GLY B . n 
B 1 55  ALA 55  35  35  ALA ALA B . n 
B 1 56  ALA 56  36  36  ALA ALA B . n 
B 1 57  ALA 57  37  37  ALA ALA B . n 
B 1 58  TRP 58  38  38  TRP TRP B . n 
B 1 59  VAL 59  39  39  VAL VAL B . n 
B 1 60  VAL 60  40  40  VAL VAL B . n 
B 1 61  THR 61  41  41  THR THR B . n 
B 1 62  ARG 62  42  42  ARG ARG B . n 
B 1 63  TYR 63  43  43  TYR TYR B . n 
B 1 64  ASP 64  44  44  ASP ASP B . n 
B 1 65  ASP 65  45  45  ASP ASP B . n 
B 1 66  VAL 66  46  46  VAL VAL B . n 
B 1 67  ARG 67  47  47  ARG ARG B . n 
B 1 68  ALA 68  48  48  ALA ALA B . n 
B 1 69  GLY 69  49  49  GLY GLY B . n 
B 1 70  LEU 70  50  50  LEU LEU B . n 
B 1 71  ALA 71  51  51  ALA ALA B . n 
B 1 72  ASP 72  52  52  ASP ASP B . n 
B 1 73  PRO 73  53  53  PRO PRO B . n 
B 1 74  ARG 74  54  54  ARG ARG B . n 
B 1 75  LEU 75  55  55  LEU LEU B . n 
B 1 76  SER 76  56  56  SER SER B . n 
B 1 77  VAL 77  57  57  VAL VAL B . n 
B 1 78  ASP 78  58  58  ASP ASP B . n 
B 1 79  ARG 79  59  59  ARG ARG B . n 
B 1 80  SER 80  60  60  SER SER B . n 
B 1 81  ASN 81  61  61  ASN ASN B . n 
B 1 82  ALA 82  62  62  ALA ALA B . n 
B 1 83  GLY 83  63  63  GLY GLY B . n 
B 1 84  ALA 84  64  64  ALA ALA B . n 
B 1 85  GLY 85  65  65  GLY GLY B . n 
B 1 86  TYR 86  66  66  TYR TYR B . n 
B 1 87  ARG 87  67  67  ARG ARG B . n 
B 1 88  GLY 88  68  68  GLY GLY B . n 
B 1 89  PHE 89  69  69  PHE PHE B . n 
B 1 90  SER 90  70  70  SER SER B . n 
B 1 91  LEU 91  71  71  LEU LEU B . n 
B 1 92  PRO 92  72  72  PRO PRO B . n 
B 1 93  PRO 93  73  73  PRO PRO B . n 
B 1 94  ALA 94  74  74  ALA ALA B . n 
B 1 95  LEU 95  75  75  LEU LEU B . n 
B 1 96  ASP 96  76  76  ASP ASP B . n 
B 1 97  ALA 97  77  77  ALA ALA B . n 
B 1 98  ASN 98  78  78  ASN ASN B . n 
B 1 99  LEU 99  79  79  LEU LEU B . n 
B 1 100 LEU 100 80  80  LEU LEU B . n 
B 1 101 ASN 101 81  81  ASN ASN B . n 
B 1 102 LEU 102 82  82  LEU LEU B . n 
B 1 103 ASP 103 83  83  ASP ASP B . n 
B 1 104 PRO 104 84  84  PRO PRO B . n 
B 1 105 PRO 105 85  85  PRO PRO B . n 
B 1 106 ASP 106 86  86  ASP ASP B . n 
B 1 107 HIS 107 87  87  HIS HIS B . n 
B 1 108 THR 108 88  88  THR THR B . n 
B 1 109 ARG 109 89  89  ARG ARG B . n 
B 1 110 LEU 110 90  90  LEU LEU B . n 
B 1 111 ARG 111 91  91  ARG ARG B . n 
B 1 112 THR 112 92  92  THR THR B . n 
B 1 113 LEU 113 93  93  LEU LEU B . n 
B 1 114 ILE 114 94  94  ILE ILE B . n 
B 1 115 ALA 115 95  95  ALA ALA B . n 
B 1 116 GLY 116 96  96  GLY GLY B . n 
B 1 117 GLU 117 97  97  GLU GLU B . n 
B 1 118 PHE 118 98  98  PHE PHE B . n 
B 1 119 THR 119 99  99  THR THR B . n 
B 1 120 PRO 120 100 100 PRO PRO B . n 
B 1 121 ARG 121 101 101 ARG ARG B . n 
B 1 122 ARG 122 102 102 ARG ARG B . n 
B 1 123 VAL 123 103 103 VAL VAL B . n 
B 1 124 HIS 124 104 104 HIS HIS B . n 
B 1 125 GLU 125 105 105 GLU GLU B . n 
B 1 126 LEU 126 106 106 LEU LEU B . n 
B 1 127 VAL 127 107 107 VAL VAL B . n 
B 1 128 PRO 128 108 108 PRO PRO B . n 
B 1 129 ALA 129 109 109 ALA ALA B . n 
B 1 130 ILE 130 110 110 ILE ILE B . n 
B 1 131 GLU 131 111 111 GLU GLU B . n 
B 1 132 ALA 132 112 112 ALA ALA B . n 
B 1 133 ALA 133 113 113 ALA ALA B . n 
B 1 134 ALA 134 114 114 ALA ALA B . n 
B 1 135 ARG 135 115 115 ARG ARG B . n 
B 1 136 GLU 136 116 116 GLU GLU B . n 
B 1 137 LEU 137 117 117 LEU LEU B . n 
B 1 138 LEU 138 118 118 LEU LEU B . n 
B 1 139 ALA 139 119 119 ALA ALA B . n 
B 1 140 GLY 140 120 120 GLY GLY B . n 
B 1 141 LEU 141 121 121 LEU LEU B . n 
B 1 142 PRO 142 122 122 PRO PRO B . n 
B 1 143 SER 143 123 123 SER SER B . n 
B 1 144 GLY 144 124 124 GLY GLY B . n 
B 1 145 GLU 145 125 125 GLU GLU B . n 
B 1 146 PRO 146 126 126 PRO PRO B . n 
B 1 147 VAL 147 127 127 VAL VAL B . n 
B 1 148 ASP 148 128 128 ASP ASP B . n 
B 1 149 LEU 149 129 129 LEU LEU B . n 
B 1 150 ILE 150 130 130 ILE ILE B . n 
B 1 151 ALA 151 131 131 ALA ALA B . n 
B 1 152 GLY 152 132 132 GLY GLY B . n 
B 1 153 PHE 153 133 133 PHE PHE B . n 
B 1 154 ALA 154 134 134 ALA ALA B . n 
B 1 155 ALA 155 135 135 ALA ALA B . n 
B 1 156 PRO 156 136 136 PRO PRO B . n 
B 1 157 LEU 157 137 137 LEU LEU B . n 
B 1 158 PRO 158 138 138 PRO PRO B . n 
B 1 159 LEU 159 139 139 LEU LEU B . n 
B 1 160 ARG 160 140 140 ARG ARG B . n 
B 1 161 VAL 161 141 141 VAL VAL B . n 
B 1 162 ILE 162 142 142 ILE ILE B . n 
B 1 163 GLY 163 143 143 GLY GLY B . n 
B 1 164 ASP 164 144 144 ASP ASP B . n 
B 1 165 LEU 165 145 145 LEU LEU B . n 
B 1 166 LEU 166 146 146 LEU LEU B . n 
B 1 167 GLY 167 147 147 GLY GLY B . n 
B 1 168 VAL 168 148 148 VAL VAL B . n 
B 1 169 PRO 169 149 149 PRO PRO B . n 
B 1 170 PRO 170 150 150 PRO PRO B . n 
B 1 171 ALA 171 151 151 ALA ALA B . n 
B 1 172 ASP 172 152 152 ASP ASP B . n 
B 1 173 ARG 173 153 153 ARG ARG B . n 
B 1 174 ALA 174 154 154 ALA ALA B . n 
B 1 175 ARG 175 155 155 ARG ARG B . n 
B 1 176 PHE 176 156 156 PHE PHE B . n 
B 1 177 ARG 177 157 157 ARG ARG B . n 
B 1 178 GLY 178 158 158 GLY GLY B . n 
B 1 179 TRP 179 159 159 TRP TRP B . n 
B 1 180 THR 180 160 160 THR THR B . n 
B 1 181 THR 181 161 161 THR THR B . n 
B 1 182 THR 182 162 162 THR THR B . n 
B 1 183 LEU 183 163 163 LEU LEU B . n 
B 1 184 LEU 184 164 164 LEU LEU B . n 
B 1 185 THR 185 165 165 THR THR B . n 
B 1 186 PRO 186 166 166 PRO PRO B . n 
B 1 187 GLY 187 167 167 GLY GLY B . n 
B 1 188 PRO 188 168 168 PRO PRO B . n 
B 1 189 ASP 189 169 169 ASP ASP B . n 
B 1 190 GLN 190 170 170 GLN GLN B . n 
B 1 191 PRO 191 171 171 PRO PRO B . n 
B 1 192 PRO 192 172 172 PRO PRO B . n 
B 1 193 THR 193 173 173 THR THR B . n 
B 1 194 ALA 194 174 174 ALA ALA B . n 
B 1 195 ALA 195 175 175 ALA ALA B . n 
B 1 196 ARG 196 176 176 ARG ARG B . n 
B 1 197 ASP 197 177 177 ASP ASP B . n 
B 1 198 ALA 198 178 178 ALA ALA B . n 
B 1 199 VAL 199 179 179 VAL VAL B . n 
B 1 200 VAL 200 180 180 VAL VAL B . n 
B 1 201 ALA 201 181 181 ALA ALA B . n 
B 1 202 MET 202 182 182 MET MET B . n 
B 1 203 HIS 203 183 183 HIS HIS B . n 
B 1 204 GLY 204 184 184 GLY GLY B . n 
B 1 205 PHE 205 185 185 PHE PHE B . n 
B 1 206 LEU 206 186 186 LEU LEU B . n 
B 1 207 VAL 207 187 187 VAL VAL B . n 
B 1 208 ASP 208 188 188 ASP ASP B . n 
B 1 209 LEU 209 189 189 LEU LEU B . n 
B 1 210 VAL 210 190 190 VAL VAL B . n 
B 1 211 ALA 211 191 191 ALA ALA B . n 
B 1 212 ALA 212 192 192 ALA ALA B . n 
B 1 213 LYS 213 193 193 LYS LYS B . n 
B 1 214 ARG 214 194 194 ARG ARG B . n 
B 1 215 ALA 215 195 195 ALA ALA B . n 
B 1 216 GLU 216 196 196 GLU GLU B . n 
B 1 217 PRO 217 197 197 PRO PRO B . n 
B 1 218 GLY 218 198 198 GLY GLY B . n 
B 1 219 HIS 219 199 199 HIS HIS B . n 
B 1 220 ASP 220 200 200 ASP ASP B . n 
B 1 221 LEU 221 201 201 LEU LEU B . n 
B 1 222 LEU 222 202 202 LEU LEU B . n 
B 1 223 SER 223 203 203 SER SER B . n 
B 1 224 GLY 224 204 204 GLY GLY B . n 
B 1 225 LEU 225 205 205 LEU LEU B . n 
B 1 226 ILE 226 206 206 ILE ILE B . n 
B 1 227 ALA 227 207 207 ALA ALA B . n 
B 1 228 VAL 228 208 208 VAL VAL B . n 
B 1 229 ARG 229 209 209 ARG ARG B . n 
B 1 230 ASP 230 210 210 ASP ASP B . n 
B 1 231 ASP 231 211 211 ASP ASP B . n 
B 1 232 GLU 232 212 212 GLU GLU B . n 
B 1 233 ASP 233 213 213 ASP ASP B . n 
B 1 234 ARG 234 214 214 ARG ARG B . n 
B 1 235 LEU 235 215 215 LEU LEU B . n 
B 1 236 SER 236 216 216 SER SER B . n 
B 1 237 GLU 237 217 217 GLU GLU B . n 
B 1 238 ALA 238 218 218 ALA ALA B . n 
B 1 239 GLU 239 219 219 GLU GLU B . n 
B 1 240 LEU 240 220 220 LEU LEU B . n 
B 1 241 VAL 241 221 221 VAL VAL B . n 
B 1 242 SER 242 222 222 SER SER B . n 
B 1 243 MET 243 223 223 MET MET B . n 
B 1 244 ALA 244 224 224 ALA ALA B . n 
B 1 245 PHE 245 225 225 PHE PHE B . n 
B 1 246 LEU 246 226 226 LEU LEU B . n 
B 1 247 ALA 247 227 227 ALA ALA B . n 
B 1 248 LEU 248 228 228 LEU LEU B . n 
B 1 249 TRP 249 229 229 TRP TRP B . n 
B 1 250 ALA 250 230 230 ALA ALA B . n 
B 1 251 GLY 251 231 231 GLY GLY B . n 
B 1 252 TYR 252 232 232 TYR TYR B . n 
B 1 253 GLU 253 233 233 GLU GLU B . n 
B 1 254 ASN 254 234 234 ASN ASN B . n 
B 1 255 LEU 255 235 235 LEU LEU B . n 
B 1 256 VAL 256 236 236 VAL VAL B . n 
B 1 257 HIS 257 237 237 HIS HIS B . n 
B 1 258 LEU 258 238 238 LEU LEU B . n 
B 1 259 ILE 259 239 239 ILE ILE B . n 
B 1 260 GLY 260 240 240 GLY GLY B . n 
B 1 261 ASN 261 241 241 ASN ASN B . n 
B 1 262 GLY 262 242 242 GLY GLY B . n 
B 1 263 VAL 263 243 243 VAL VAL B . n 
B 1 264 ARG 264 244 244 ARG ARG B . n 
B 1 265 ALA 265 245 245 ALA ALA B . n 
B 1 266 LEU 266 246 246 LEU LEU B . n 
B 1 267 LEU 267 247 247 LEU LEU B . n 
B 1 268 ALA 268 248 248 ALA ALA B . n 
B 1 269 ALA 269 249 249 ALA ALA B . n 
B 1 270 PRO 270 250 250 PRO PRO B . n 
B 1 271 ASP 271 251 251 ASP ASP B . n 
B 1 272 GLN 272 252 252 GLN GLN B . n 
B 1 273 LEU 273 253 253 LEU LEU B . n 
B 1 274 ALA 274 254 254 ALA ALA B . n 
B 1 275 ASP 275 255 255 ASP ASP B . n 
B 1 276 LEU 276 256 256 LEU LEU B . n 
B 1 277 ARG 277 257 257 ARG ARG B . n 
B 1 278 SER 278 258 258 SER SER B . n 
B 1 279 ASP 279 259 259 ASP ASP B . n 
B 1 280 GLU 280 260 260 GLU GLU B . n 
B 1 281 ALA 281 261 261 ALA ALA B . n 
B 1 282 LEU 282 262 262 LEU LEU B . n 
B 1 283 LEU 283 263 263 LEU LEU B . n 
B 1 284 PRO 284 264 264 PRO PRO B . n 
B 1 285 ARG 285 265 265 ARG ARG B . n 
B 1 286 ALA 286 266 266 ALA ALA B . n 
B 1 287 ILE 287 267 267 ILE ILE B . n 
B 1 288 GLU 288 268 268 GLU GLU B . n 
B 1 289 GLU 289 269 269 GLU GLU B . n 
B 1 290 LEU 290 270 270 LEU LEU B . n 
B 1 291 THR 291 271 271 THR THR B . n 
B 1 292 ARG 292 272 272 ARG ARG B . n 
B 1 293 PHE 293 273 273 PHE PHE B . n 
B 1 294 ASP 294 274 274 ASP ASP B . n 
B 1 295 GLN 295 275 275 GLN GLN B . n 
B 1 296 PRO 296 276 276 PRO PRO B . n 
B 1 297 LEU 297 277 277 LEU LEU B . n 
B 1 298 GLN 298 278 278 GLN GLN B . n 
B 1 299 TRP 299 279 279 TRP TRP B . n 
B 1 300 ALA 300 280 280 ALA ALA B . n 
B 1 301 ILE 301 281 281 ILE ILE B . n 
B 1 302 ARG 302 282 282 ARG ARG B . n 
B 1 303 ARG 303 283 283 ARG ARG B . n 
B 1 304 PHE 304 284 284 PHE PHE B . n 
B 1 305 PRO 305 285 285 PRO PRO B . n 
B 1 306 THR 306 286 286 THR THR B . n 
B 1 307 ARG 307 287 287 ARG ARG B . n 
B 1 308 GLU 308 288 288 GLU GLU B . n 
B 1 309 LEU 309 289 289 LEU LEU B . n 
B 1 310 ASP 310 290 290 ASP ASP B . n 
B 1 311 ILE 311 291 291 ILE ILE B . n 
B 1 312 ALA 312 292 292 ALA ALA B . n 
B 1 313 GLY 313 293 293 GLY GLY B . n 
B 1 314 VAL 314 294 294 VAL VAL B . n 
B 1 315 GLU 315 295 295 GLU GLU B . n 
B 1 316 VAL 316 296 296 VAL VAL B . n 
B 1 317 PRO 317 297 297 PRO PRO B . n 
B 1 318 ALA 318 298 298 ALA ALA B . n 
B 1 319 GLY 319 299 299 GLY GLY B . n 
B 1 320 ASP 320 300 300 ASP ASP B . n 
B 1 321 THR 321 301 301 THR THR B . n 
B 1 322 VAL 322 302 302 VAL VAL B . n 
B 1 323 LEU 323 303 303 LEU LEU B . n 
B 1 324 LEU 324 304 304 LEU LEU B . n 
B 1 325 GLY 325 305 305 GLY GLY B . n 
B 1 326 ILE 326 306 306 ILE ILE B . n 
B 1 327 ALA 327 307 307 ALA ALA B . n 
B 1 328 SER 328 308 308 SER SER B . n 
B 1 329 ALA 329 309 309 ALA ALA B . n 
B 1 330 ASN 330 310 310 ASN ASN B . n 
B 1 331 HIS 331 311 311 HIS HIS B . n 
B 1 332 ASP 332 312 312 ASP ASP B . n 
B 1 333 GLU 333 313 313 GLU GLU B . n 
B 1 334 THR 334 314 314 THR THR B . n 
B 1 335 VAL 335 315 315 VAL VAL B . n 
B 1 336 PHE 336 316 316 PHE PHE B . n 
B 1 337 ASP 337 317 317 ASP ASP B . n 
B 1 338 LEU 338 318 318 LEU LEU B . n 
B 1 339 PRO 339 319 319 PRO PRO B . n 
B 1 340 ASP 340 320 320 ASP ASP B . n 
B 1 341 THR 341 321 321 THR THR B . n 
B 1 342 LEU 342 322 322 LEU LEU B . n 
B 1 343 ASP 343 323 323 ASP ASP B . n 
B 1 344 LEU 344 324 324 LEU LEU B . n 
B 1 345 ARG 345 325 325 ARG ARG B . n 
B 1 346 ARG 346 326 326 ARG ARG B . n 
B 1 347 ASP 347 327 327 ASP ASP B . n 
B 1 348 PRO 348 328 328 PRO PRO B . n 
B 1 349 ASN 349 329 329 ASN ASN B . n 
B 1 350 PRO 350 330 330 PRO PRO B . n 
B 1 351 HIS 351 331 331 HIS HIS B . n 
B 1 352 LEU 352 332 332 LEU LEU B . n 
B 1 353 SER 353 333 333 SER SER B . n 
B 1 354 TYR 354 334 334 TYR TYR B . n 
B 1 355 GLY 355 335 335 GLY GLY B . n 
B 1 356 HIS 356 336 336 HIS HIS B . n 
B 1 357 GLY 357 337 337 GLY GLY B . n 
B 1 358 ILE 358 338 338 ILE ILE B . n 
B 1 359 HIS 359 339 339 HIS HIS B . n 
B 1 360 ARG 360 340 340 ARG ARG B . n 
B 1 361 SER 361 341 341 SER SER B . n 
B 1 362 PHE 362 342 342 PHE PHE B . n 
B 1 363 GLY 363 343 343 GLY GLY B . n 
B 1 364 SER 364 344 344 SER SER B . n 
B 1 365 ARG 365 345 345 ARG ARG B . n 
B 1 366 LEU 366 346 346 LEU LEU B . n 
B 1 367 SER 367 347 347 SER SER B . n 
B 1 368 GLN 368 348 348 GLN GLN B . n 
B 1 369 ALA 369 349 349 ALA ALA B . n 
B 1 370 GLU 370 350 350 GLU GLU B . n 
B 1 371 ALA 371 351 351 ALA ALA B . n 
B 1 372 ALA 372 352 352 ALA ALA B . n 
B 1 373 ALA 373 353 353 ALA ALA B . n 
B 1 374 ALA 374 354 354 ALA ALA B . n 
B 1 375 PHE 375 355 355 PHE PHE B . n 
B 1 376 SER 376 356 356 SER SER B . n 
B 1 377 ALA 377 357 357 ALA ALA B . n 
B 1 378 LEU 378 358 358 LEU LEU B . n 
B 1 379 LEU 379 359 359 LEU LEU B . n 
B 1 380 ALA 380 360 360 ALA ALA B . n 
B 1 381 ARG 381 361 361 ARG ARG B . n 
B 1 382 GLY 382 362 362 GLY GLY B . n 
B 1 383 PHE 383 363 363 PHE PHE B . n 
B 1 384 ARG 384 364 364 ARG ARG B . n 
B 1 385 ALA 385 365 365 ALA ALA B . n 
B 1 386 ALA 386 366 366 ALA ALA B . n 
B 1 387 VAL 387 367 367 VAL VAL B . n 
B 1 388 ASP 388 368 368 ASP ASP B . n 
B 1 389 LEU 389 369 369 LEU LEU B . n 
B 1 390 ALA 390 370 370 ALA ALA B . n 
B 1 391 ASP 391 371 371 ASP ASP B . n 
B 1 392 LEU 392 372 372 LEU LEU B . n 
B 1 393 GLN 393 373 373 GLN GLN B . n 
B 1 394 TRP 394 374 374 TRP TRP B . n 
B 1 395 GLN 395 375 375 GLN GLN B . n 
B 1 396 PRO 396 376 376 PRO PRO B . n 
B 1 397 SER 397 377 377 SER SER B . n 
B 1 398 PHE 398 378 378 PHE PHE B . n 
B 1 399 ARG 399 379 379 ARG ARG B . n 
B 1 400 ASN 400 380 380 ASN ASN B . n 
B 1 401 ARG 401 381 381 ARG ARG B . n 
B 1 402 GLY 402 382 382 GLY GLY B . n 
B 1 403 LEU 403 383 383 LEU LEU B . n 
B 1 404 THR 404 384 384 THR THR B . n 
B 1 405 GLU 405 385 385 GLU GLU B . n 
B 1 406 LEU 406 386 386 LEU LEU B . n 
B 1 407 PRO 407 387 387 PRO PRO B . n 
B 1 408 LEU 408 388 388 LEU LEU B . n 
B 1 409 LEU 409 389 389 LEU LEU B . n 
B 1 410 LEU 410 390 390 LEU LEU B . n 
B 1 411 GLY 411 391 391 GLY GLY B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HEM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HEM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HEM 1   401 481 HEM HEM A . 
D 3 FMT 1   402 482 FMT FMT A . 
E 4 1BO 1   403 483 1BO 1BO A . 
F 4 1BO 1   404 484 1BO 1BO A . 
G 3 FMT 1   405 485 FMT FMT A . 
H 2 HEM 1   401 481 HEM HEM B . 
I 5 HOH 1   501 259 HOH HOH A . 
I 5 HOH 2   502 306 HOH HOH A . 
I 5 HOH 3   503 16  HOH HOH A . 
I 5 HOH 4   504 61  HOH HOH A . 
I 5 HOH 5   505 50  HOH HOH A . 
I 5 HOH 6   506 154 HOH HOH A . 
I 5 HOH 7   507 206 HOH HOH A . 
I 5 HOH 8   508 188 HOH HOH A . 
I 5 HOH 9   509 164 HOH HOH A . 
I 5 HOH 10  510 418 HOH HOH A . 
I 5 HOH 11  511 194 HOH HOH A . 
I 5 HOH 12  512 46  HOH HOH A . 
I 5 HOH 13  513 36  HOH HOH A . 
I 5 HOH 14  514 381 HOH HOH A . 
I 5 HOH 15  515 102 HOH HOH A . 
I 5 HOH 16  516 29  HOH HOH A . 
I 5 HOH 17  517 119 HOH HOH A . 
I 5 HOH 18  518 17  HOH HOH A . 
I 5 HOH 19  519 456 HOH HOH A . 
I 5 HOH 20  520 92  HOH HOH A . 
I 5 HOH 21  521 214 HOH HOH A . 
I 5 HOH 22  522 252 HOH HOH A . 
I 5 HOH 23  523 143 HOH HOH A . 
I 5 HOH 24  524 134 HOH HOH A . 
I 5 HOH 25  525 74  HOH HOH A . 
I 5 HOH 26  526 365 HOH HOH A . 
I 5 HOH 27  527 184 HOH HOH A . 
I 5 HOH 28  528 38  HOH HOH A . 
I 5 HOH 29  529 410 HOH HOH A . 
I 5 HOH 30  530 2   HOH HOH A . 
I 5 HOH 31  531 141 HOH HOH A . 
I 5 HOH 32  532 7   HOH HOH A . 
I 5 HOH 33  533 23  HOH HOH A . 
I 5 HOH 34  534 340 HOH HOH A . 
I 5 HOH 35  535 191 HOH HOH A . 
I 5 HOH 36  536 351 HOH HOH A . 
I 5 HOH 37  537 226 HOH HOH A . 
I 5 HOH 38  538 213 HOH HOH A . 
I 5 HOH 39  539 302 HOH HOH A . 
I 5 HOH 40  540 138 HOH HOH A . 
I 5 HOH 41  541 292 HOH HOH A . 
I 5 HOH 42  542 247 HOH HOH A . 
I 5 HOH 43  543 21  HOH HOH A . 
I 5 HOH 44  544 14  HOH HOH A . 
I 5 HOH 45  545 43  HOH HOH A . 
I 5 HOH 46  546 39  HOH HOH A . 
I 5 HOH 47  547 53  HOH HOH A . 
I 5 HOH 48  548 173 HOH HOH A . 
I 5 HOH 49  549 190 HOH HOH A . 
I 5 HOH 50  550 240 HOH HOH A . 
I 5 HOH 51  551 33  HOH HOH A . 
I 5 HOH 52  552 185 HOH HOH A . 
I 5 HOH 53  553 278 HOH HOH A . 
I 5 HOH 54  554 30  HOH HOH A . 
I 5 HOH 55  555 96  HOH HOH A . 
I 5 HOH 56  556 144 HOH HOH A . 
I 5 HOH 57  557 98  HOH HOH A . 
I 5 HOH 58  558 9   HOH HOH A . 
I 5 HOH 59  559 6   HOH HOH A . 
I 5 HOH 60  560 201 HOH HOH A . 
I 5 HOH 61  561 283 HOH HOH A . 
I 5 HOH 62  562 1   HOH HOH A . 
I 5 HOH 63  563 484 HOH HOH A . 
I 5 HOH 64  564 382 HOH HOH A . 
I 5 HOH 65  565 123 HOH HOH A . 
I 5 HOH 66  566 15  HOH HOH A . 
I 5 HOH 67  567 44  HOH HOH A . 
I 5 HOH 68  568 31  HOH HOH A . 
I 5 HOH 69  569 69  HOH HOH A . 
I 5 HOH 70  570 5   HOH HOH A . 
I 5 HOH 71  571 192 HOH HOH A . 
I 5 HOH 72  572 557 HOH HOH A . 
I 5 HOH 73  573 473 HOH HOH A . 
I 5 HOH 74  574 42  HOH HOH A . 
I 5 HOH 75  575 255 HOH HOH A . 
I 5 HOH 76  576 41  HOH HOH A . 
I 5 HOH 77  577 450 HOH HOH A . 
I 5 HOH 78  578 129 HOH HOH A . 
I 5 HOH 79  579 343 HOH HOH A . 
I 5 HOH 80  580 179 HOH HOH A . 
I 5 HOH 81  581 295 HOH HOH A . 
I 5 HOH 82  582 305 HOH HOH A . 
I 5 HOH 83  583 34  HOH HOH A . 
I 5 HOH 84  584 63  HOH HOH A . 
I 5 HOH 85  585 79  HOH HOH A . 
I 5 HOH 86  586 231 HOH HOH A . 
I 5 HOH 87  587 235 HOH HOH A . 
I 5 HOH 88  588 133 HOH HOH A . 
I 5 HOH 89  589 75  HOH HOH A . 
I 5 HOH 90  590 112 HOH HOH A . 
I 5 HOH 91  591 56  HOH HOH A . 
I 5 HOH 92  592 251 HOH HOH A . 
I 5 HOH 93  593 233 HOH HOH A . 
I 5 HOH 94  594 197 HOH HOH A . 
I 5 HOH 95  595 105 HOH HOH A . 
I 5 HOH 96  596 22  HOH HOH A . 
I 5 HOH 97  597 26  HOH HOH A . 
I 5 HOH 98  598 19  HOH HOH A . 
I 5 HOH 99  599 12  HOH HOH A . 
I 5 HOH 100 600 250 HOH HOH A . 
I 5 HOH 101 601 73  HOH HOH A . 
I 5 HOH 102 602 55  HOH HOH A . 
I 5 HOH 103 603 487 HOH HOH A . 
I 5 HOH 104 604 95  HOH HOH A . 
I 5 HOH 105 605 298 HOH HOH A . 
I 5 HOH 106 606 296 HOH HOH A . 
I 5 HOH 107 607 48  HOH HOH A . 
I 5 HOH 108 608 325 HOH HOH A . 
I 5 HOH 109 609 116 HOH HOH A . 
I 5 HOH 110 610 357 HOH HOH A . 
I 5 HOH 111 611 18  HOH HOH A . 
I 5 HOH 112 612 8   HOH HOH A . 
I 5 HOH 113 613 52  HOH HOH A . 
I 5 HOH 114 614 182 HOH HOH A . 
I 5 HOH 115 615 286 HOH HOH A . 
I 5 HOH 116 616 229 HOH HOH A . 
I 5 HOH 117 617 70  HOH HOH A . 
I 5 HOH 118 618 109 HOH HOH A . 
I 5 HOH 119 619 84  HOH HOH A . 
I 5 HOH 120 620 254 HOH HOH A . 
I 5 HOH 121 621 137 HOH HOH A . 
I 5 HOH 122 622 11  HOH HOH A . 
I 5 HOH 123 623 4   HOH HOH A . 
I 5 HOH 124 624 477 HOH HOH A . 
I 5 HOH 125 625 265 HOH HOH A . 
I 5 HOH 126 626 333 HOH HOH A . 
I 5 HOH 127 627 25  HOH HOH A . 
I 5 HOH 128 628 10  HOH HOH A . 
I 5 HOH 129 629 275 HOH HOH A . 
I 5 HOH 130 630 99  HOH HOH A . 
I 5 HOH 131 631 91  HOH HOH A . 
I 5 HOH 132 632 472 HOH HOH A . 
I 5 HOH 133 633 177 HOH HOH A . 
I 5 HOH 134 634 3   HOH HOH A . 
I 5 HOH 135 635 85  HOH HOH A . 
I 5 HOH 136 636 258 HOH HOH A . 
I 5 HOH 137 637 13  HOH HOH A . 
I 5 HOH 138 638 558 HOH HOH A . 
I 5 HOH 139 639 132 HOH HOH A . 
I 5 HOH 140 640 93  HOH HOH A . 
I 5 HOH 141 641 110 HOH HOH A . 
I 5 HOH 142 642 187 HOH HOH A . 
I 5 HOH 143 643 199 HOH HOH A . 
I 5 HOH 144 644 209 HOH HOH A . 
I 5 HOH 145 645 37  HOH HOH A . 
I 5 HOH 146 646 81  HOH HOH A . 
I 5 HOH 147 647 89  HOH HOH A . 
I 5 HOH 148 648 35  HOH HOH A . 
I 5 HOH 149 649 202 HOH HOH A . 
I 5 HOH 150 650 135 HOH HOH A . 
I 5 HOH 151 651 152 HOH HOH A . 
I 5 HOH 152 652 438 HOH HOH A . 
I 5 HOH 153 653 256 HOH HOH A . 
I 5 HOH 154 654 158 HOH HOH A . 
I 5 HOH 155 655 28  HOH HOH A . 
I 5 HOH 156 656 24  HOH HOH A . 
I 5 HOH 157 657 67  HOH HOH A . 
I 5 HOH 158 658 203 HOH HOH A . 
I 5 HOH 159 659 111 HOH HOH A . 
I 5 HOH 160 660 300 HOH HOH A . 
I 5 HOH 161 661 385 HOH HOH A . 
I 5 HOH 162 662 40  HOH HOH A . 
I 5 HOH 163 663 376 HOH HOH A . 
I 5 HOH 164 664 183 HOH HOH A . 
I 5 HOH 165 665 157 HOH HOH A . 
I 5 HOH 166 666 327 HOH HOH A . 
I 5 HOH 167 667 228 HOH HOH A . 
I 5 HOH 168 668 338 HOH HOH A . 
I 5 HOH 169 669 501 HOH HOH A . 
I 5 HOH 170 670 150 HOH HOH A . 
I 5 HOH 171 671 369 HOH HOH A . 
I 5 HOH 172 672 264 HOH HOH A . 
I 5 HOH 173 673 370 HOH HOH A . 
I 5 HOH 174 674 317 HOH HOH A . 
I 5 HOH 175 675 548 HOH HOH A . 
I 5 HOH 176 676 211 HOH HOH A . 
I 5 HOH 177 677 66  HOH HOH A . 
I 5 HOH 178 678 394 HOH HOH A . 
I 5 HOH 179 679 491 HOH HOH A . 
I 5 HOH 180 680 208 HOH HOH A . 
I 5 HOH 181 681 27  HOH HOH A . 
I 5 HOH 182 682 181 HOH HOH A . 
I 5 HOH 183 683 204 HOH HOH A . 
I 5 HOH 184 684 140 HOH HOH A . 
I 5 HOH 185 685 285 HOH HOH A . 
I 5 HOH 186 686 60  HOH HOH A . 
I 5 HOH 187 687 328 HOH HOH A . 
I 5 HOH 188 688 273 HOH HOH A . 
I 5 HOH 189 689 107 HOH HOH A . 
I 5 HOH 190 690 216 HOH HOH A . 
I 5 HOH 191 691 481 HOH HOH A . 
I 5 HOH 192 692 149 HOH HOH A . 
I 5 HOH 193 693 172 HOH HOH A . 
I 5 HOH 194 694 449 HOH HOH A . 
I 5 HOH 195 695 464 HOH HOH A . 
I 5 HOH 196 696 62  HOH HOH A . 
I 5 HOH 197 697 480 HOH HOH A . 
I 5 HOH 198 698 207 HOH HOH A . 
I 5 HOH 199 699 353 HOH HOH A . 
I 5 HOH 200 700 482 HOH HOH A . 
I 5 HOH 201 701 277 HOH HOH A . 
I 5 HOH 202 702 468 HOH HOH A . 
I 5 HOH 203 703 299 HOH HOH A . 
I 5 HOH 204 704 166 HOH HOH A . 
I 5 HOH 205 705 261 HOH HOH A . 
I 5 HOH 206 706 115 HOH HOH A . 
I 5 HOH 207 707 293 HOH HOH A . 
I 5 HOH 208 708 554 HOH HOH A . 
I 5 HOH 209 709 68  HOH HOH A . 
I 5 HOH 210 710 502 HOH HOH A . 
I 5 HOH 211 711 349 HOH HOH A . 
I 5 HOH 212 712 297 HOH HOH A . 
I 5 HOH 213 713 245 HOH HOH A . 
I 5 HOH 214 714 49  HOH HOH A . 
I 5 HOH 215 715 476 HOH HOH A . 
I 5 HOH 216 716 471 HOH HOH A . 
I 5 HOH 217 717 475 HOH HOH A . 
I 5 HOH 218 718 424 HOH HOH A . 
I 5 HOH 219 719 352 HOH HOH A . 
I 5 HOH 220 720 488 HOH HOH A . 
I 5 HOH 221 721 210 HOH HOH A . 
I 5 HOH 222 722 469 HOH HOH A . 
I 5 HOH 223 723 64  HOH HOH A . 
I 5 HOH 224 724 71  HOH HOH A . 
I 5 HOH 225 725 372 HOH HOH A . 
I 5 HOH 226 726 421 HOH HOH A . 
I 5 HOH 227 727 538 HOH HOH A . 
I 5 HOH 228 728 225 HOH HOH A . 
I 5 HOH 229 729 268 HOH HOH A . 
I 5 HOH 230 730 218 HOH HOH A . 
I 5 HOH 231 731 217 HOH HOH A . 
I 5 HOH 232 732 58  HOH HOH A . 
I 5 HOH 233 733 348 HOH HOH A . 
I 5 HOH 234 734 308 HOH HOH A . 
I 5 HOH 235 735 329 HOH HOH A . 
I 5 HOH 236 736 466 HOH HOH A . 
I 5 HOH 237 737 313 HOH HOH A . 
I 5 HOH 238 738 561 HOH HOH A . 
I 5 HOH 239 739 507 HOH HOH A . 
I 5 HOH 240 740 470 HOH HOH A . 
I 5 HOH 241 741 103 HOH HOH A . 
I 5 HOH 242 742 467 HOH HOH A . 
I 5 HOH 243 743 196 HOH HOH A . 
I 5 HOH 244 744 175 HOH HOH A . 
I 5 HOH 245 745 160 HOH HOH A . 
I 5 HOH 246 746 378 HOH HOH A . 
I 5 HOH 247 747 249 HOH HOH A . 
I 5 HOH 248 748 136 HOH HOH A . 
I 5 HOH 249 749 272 HOH HOH A . 
I 5 HOH 250 750 444 HOH HOH A . 
I 5 HOH 251 751 402 HOH HOH A . 
I 5 HOH 252 752 564 HOH HOH A . 
I 5 HOH 253 753 417 HOH HOH A . 
I 5 HOH 254 754 383 HOH HOH A . 
I 5 HOH 255 755 391 HOH HOH A . 
I 5 HOH 256 756 534 HOH HOH A . 
I 5 HOH 257 757 504 HOH HOH A . 
I 5 HOH 258 758 399 HOH HOH A . 
I 5 HOH 259 759 411 HOH HOH A . 
I 5 HOH 260 760 451 HOH HOH A . 
I 5 HOH 261 761 222 HOH HOH A . 
I 5 HOH 262 762 503 HOH HOH A . 
I 5 HOH 263 763 270 HOH HOH A . 
I 5 HOH 264 764 559 HOH HOH A . 
I 5 HOH 265 765 371 HOH HOH A . 
I 5 HOH 266 766 121 HOH HOH A . 
I 5 HOH 267 767 544 HOH HOH A . 
I 5 HOH 268 768 366 HOH HOH A . 
I 5 HOH 269 769 533 HOH HOH A . 
I 5 HOH 270 770 373 HOH HOH A . 
I 5 HOH 271 771 189 HOH HOH A . 
I 5 HOH 272 772 355 HOH HOH A . 
I 5 HOH 273 773 289 HOH HOH A . 
I 5 HOH 274 774 350 HOH HOH A . 
I 5 HOH 275 775 239 HOH HOH A . 
I 5 HOH 276 776 153 HOH HOH A . 
I 5 HOH 277 777 428 HOH HOH A . 
I 5 HOH 278 778 542 HOH HOH A . 
I 5 HOH 279 779 356 HOH HOH A . 
I 5 HOH 280 780 412 HOH HOH A . 
I 5 HOH 281 781 543 HOH HOH A . 
I 5 HOH 282 782 562 HOH HOH A . 
I 5 HOH 283 783 174 HOH HOH A . 
I 5 HOH 284 784 106 HOH HOH A . 
I 5 HOH 285 785 420 HOH HOH A . 
I 5 HOH 286 786 236 HOH HOH A . 
I 5 HOH 287 787 505 HOH HOH A . 
I 5 HOH 288 788 524 HOH HOH A . 
I 5 HOH 289 789 532 HOH HOH A . 
I 5 HOH 290 790 212 HOH HOH A . 
I 5 HOH 291 791 127 HOH HOH A . 
I 5 HOH 292 792 500 HOH HOH A . 
I 5 HOH 293 793 363 HOH HOH A . 
I 5 HOH 294 794 118 HOH HOH A . 
I 5 HOH 295 795 546 HOH HOH A . 
I 5 HOH 296 796 198 HOH HOH A . 
I 5 HOH 297 797 499 HOH HOH A . 
I 5 HOH 298 798 315 HOH HOH A . 
I 5 HOH 299 799 446 HOH HOH A . 
I 5 HOH 300 800 290 HOH HOH A . 
I 5 HOH 301 801 539 HOH HOH A . 
I 5 HOH 302 802 540 HOH HOH A . 
I 5 HOH 303 803 426 HOH HOH A . 
I 5 HOH 304 804 266 HOH HOH A . 
I 5 HOH 305 805 535 HOH HOH A . 
I 5 HOH 306 806 537 HOH HOH A . 
I 5 HOH 307 807 126 HOH HOH A . 
I 5 HOH 308 808 556 HOH HOH A . 
I 5 HOH 309 809 334 HOH HOH A . 
I 5 HOH 310 810 526 HOH HOH A . 
I 5 HOH 311 811 529 HOH HOH A . 
I 5 HOH 312 812 531 HOH HOH A . 
I 5 HOH 313 813 163 HOH HOH A . 
I 5 HOH 314 814 274 HOH HOH A . 
I 5 HOH 315 815 465 HOH HOH A . 
I 5 HOH 316 816 309 HOH HOH A . 
I 5 HOH 317 817 219 HOH HOH A . 
I 5 HOH 318 818 342 HOH HOH A . 
I 5 HOH 319 819 145 HOH HOH A . 
I 5 HOH 320 820 167 HOH HOH A . 
I 5 HOH 321 821 536 HOH HOH A . 
I 5 HOH 322 822 335 HOH HOH A . 
I 5 HOH 323 823 269 HOH HOH A . 
I 5 HOH 324 824 545 HOH HOH A . 
I 5 HOH 325 825 458 HOH HOH A . 
I 5 HOH 326 826 131 HOH HOH A . 
I 5 HOH 327 827 347 HOH HOH A . 
I 5 HOH 328 828 332 HOH HOH A . 
I 5 HOH 329 829 419 HOH HOH A . 
I 5 HOH 330 830 336 HOH HOH A . 
I 5 HOH 331 831 321 HOH HOH A . 
I 5 HOH 332 832 430 HOH HOH A . 
I 5 HOH 333 833 171 HOH HOH A . 
I 5 HOH 334 834 291 HOH HOH A . 
I 5 HOH 335 835 100 HOH HOH A . 
I 5 HOH 336 836 221 HOH HOH A . 
I 5 HOH 337 837 494 HOH HOH A . 
I 5 HOH 338 838 441 HOH HOH A . 
I 5 HOH 339 839 397 HOH HOH A . 
I 5 HOH 340 840 512 HOH HOH A . 
I 5 HOH 341 841 530 HOH HOH A . 
I 5 HOH 342 842 560 HOH HOH A . 
J 5 HOH 1   501 243 HOH HOH B . 
J 5 HOH 2   502 248 HOH HOH B . 
J 5 HOH 3   503 479 HOH HOH B . 
J 5 HOH 4   504 148 HOH HOH B . 
J 5 HOH 5   505 319 HOH HOH B . 
J 5 HOH 6   506 101 HOH HOH B . 
J 5 HOH 7   507 368 HOH HOH B . 
J 5 HOH 8   508 117 HOH HOH B . 
J 5 HOH 9   509 124 HOH HOH B . 
J 5 HOH 10  510 51  HOH HOH B . 
J 5 HOH 11  511 260 HOH HOH B . 
J 5 HOH 12  512 311 HOH HOH B . 
J 5 HOH 13  513 178 HOH HOH B . 
J 5 HOH 14  514 326 HOH HOH B . 
J 5 HOH 15  515 76  HOH HOH B . 
J 5 HOH 16  516 552 HOH HOH B . 
J 5 HOH 17  517 358 HOH HOH B . 
J 5 HOH 18  518 176 HOH HOH B . 
J 5 HOH 19  519 139 HOH HOH B . 
J 5 HOH 20  520 262 HOH HOH B . 
J 5 HOH 21  521 72  HOH HOH B . 
J 5 HOH 22  522 57  HOH HOH B . 
J 5 HOH 23  523 271 HOH HOH B . 
J 5 HOH 24  524 125 HOH HOH B . 
J 5 HOH 25  525 45  HOH HOH B . 
J 5 HOH 26  526 47  HOH HOH B . 
J 5 HOH 27  527 128 HOH HOH B . 
J 5 HOH 28  528 416 HOH HOH B . 
J 5 HOH 29  529 549 HOH HOH B . 
J 5 HOH 30  530 205 HOH HOH B . 
J 5 HOH 31  531 220 HOH HOH B . 
J 5 HOH 32  532 318 HOH HOH B . 
J 5 HOH 33  533 374 HOH HOH B . 
J 5 HOH 34  534 87  HOH HOH B . 
J 5 HOH 35  535 146 HOH HOH B . 
J 5 HOH 36  536 32  HOH HOH B . 
J 5 HOH 37  537 83  HOH HOH B . 
J 5 HOH 38  538 485 HOH HOH B . 
J 5 HOH 39  539 130 HOH HOH B . 
J 5 HOH 40  540 288 HOH HOH B . 
J 5 HOH 41  541 88  HOH HOH B . 
J 5 HOH 42  542 104 HOH HOH B . 
J 5 HOH 43  543 395 HOH HOH B . 
J 5 HOH 44  544 180 HOH HOH B . 
J 5 HOH 45  545 169 HOH HOH B . 
J 5 HOH 46  546 97  HOH HOH B . 
J 5 HOH 47  547 94  HOH HOH B . 
J 5 HOH 48  548 354 HOH HOH B . 
J 5 HOH 49  549 234 HOH HOH B . 
J 5 HOH 50  550 461 HOH HOH B . 
J 5 HOH 51  551 339 HOH HOH B . 
J 5 HOH 52  552 54  HOH HOH B . 
J 5 HOH 53  553 238 HOH HOH B . 
J 5 HOH 54  554 284 HOH HOH B . 
J 5 HOH 55  555 113 HOH HOH B . 
J 5 HOH 56  556 65  HOH HOH B . 
J 5 HOH 57  557 401 HOH HOH B . 
J 5 HOH 58  558 242 HOH HOH B . 
J 5 HOH 59  559 86  HOH HOH B . 
J 5 HOH 60  560 170 HOH HOH B . 
J 5 HOH 61  561 82  HOH HOH B . 
J 5 HOH 62  562 384 HOH HOH B . 
J 5 HOH 63  563 224 HOH HOH B . 
J 5 HOH 64  564 122 HOH HOH B . 
J 5 HOH 65  565 344 HOH HOH B . 
J 5 HOH 66  566 257 HOH HOH B . 
J 5 HOH 67  567 120 HOH HOH B . 
J 5 HOH 68  568 287 HOH HOH B . 
J 5 HOH 69  569 316 HOH HOH B . 
J 5 HOH 70  570 406 HOH HOH B . 
J 5 HOH 71  571 253 HOH HOH B . 
J 5 HOH 72  572 156 HOH HOH B . 
J 5 HOH 73  573 90  HOH HOH B . 
J 5 HOH 74  574 108 HOH HOH B . 
J 5 HOH 75  575 379 HOH HOH B . 
J 5 HOH 76  576 301 HOH HOH B . 
J 5 HOH 77  577 241 HOH HOH B . 
J 5 HOH 78  578 337 HOH HOH B . 
J 5 HOH 79  579 489 HOH HOH B . 
J 5 HOH 80  580 193 HOH HOH B . 
J 5 HOH 81  581 408 HOH HOH B . 
J 5 HOH 82  582 280 HOH HOH B . 
J 5 HOH 83  583 151 HOH HOH B . 
J 5 HOH 84  584 388 HOH HOH B . 
J 5 HOH 85  585 244 HOH HOH B . 
J 5 HOH 86  586 263 HOH HOH B . 
J 5 HOH 87  587 303 HOH HOH B . 
J 5 HOH 88  588 453 HOH HOH B . 
J 5 HOH 89  589 367 HOH HOH B . 
J 5 HOH 90  590 246 HOH HOH B . 
J 5 HOH 91  591 77  HOH HOH B . 
J 5 HOH 92  592 276 HOH HOH B . 
J 5 HOH 93  593 323 HOH HOH B . 
J 5 HOH 94  594 114 HOH HOH B . 
J 5 HOH 95  595 515 HOH HOH B . 
J 5 HOH 96  596 281 HOH HOH B . 
J 5 HOH 97  597 215 HOH HOH B . 
J 5 HOH 98  598 495 HOH HOH B . 
J 5 HOH 99  599 200 HOH HOH B . 
J 5 HOH 100 600 508 HOH HOH B . 
J 5 HOH 101 601 380 HOH HOH B . 
J 5 HOH 102 602 330 HOH HOH B . 
J 5 HOH 103 603 398 HOH HOH B . 
J 5 HOH 104 604 307 HOH HOH B . 
J 5 HOH 105 605 142 HOH HOH B . 
J 5 HOH 106 606 541 HOH HOH B . 
J 5 HOH 107 607 454 HOH HOH B . 
J 5 HOH 108 608 478 HOH HOH B . 
J 5 HOH 109 609 423 HOH HOH B . 
J 5 HOH 110 610 511 HOH HOH B . 
J 5 HOH 111 611 267 HOH HOH B . 
J 5 HOH 112 612 168 HOH HOH B . 
J 5 HOH 113 613 486 HOH HOH B . 
J 5 HOH 114 614 429 HOH HOH B . 
J 5 HOH 115 615 521 HOH HOH B . 
J 5 HOH 116 616 516 HOH HOH B . 
J 5 HOH 117 617 377 HOH HOH B . 
J 5 HOH 118 618 528 HOH HOH B . 
J 5 HOH 119 619 525 HOH HOH B . 
J 5 HOH 120 620 312 HOH HOH B . 
J 5 HOH 121 621 320 HOH HOH B . 
J 5 HOH 122 622 310 HOH HOH B . 
J 5 HOH 123 623 341 HOH HOH B . 
J 5 HOH 124 624 405 HOH HOH B . 
J 5 HOH 125 625 360 HOH HOH B . 
J 5 HOH 126 626 523 HOH HOH B . 
J 5 HOH 127 627 522 HOH HOH B . 
J 5 HOH 128 628 445 HOH HOH B . 
J 5 HOH 129 629 506 HOH HOH B . 
J 5 HOH 130 630 414 HOH HOH B . 
J 5 HOH 131 631 553 HOH HOH B . 
J 5 HOH 132 632 563 HOH HOH B . 
J 5 HOH 133 633 387 HOH HOH B . 
J 5 HOH 134 634 403 HOH HOH B . 
J 5 HOH 135 635 474 HOH HOH B . 
J 5 HOH 136 636 513 HOH HOH B . 
J 5 HOH 137 637 509 HOH HOH B . 
J 5 HOH 138 638 460 HOH HOH B . 
J 5 HOH 139 639 165 HOH HOH B . 
J 5 HOH 140 640 514 HOH HOH B . 
J 5 HOH 141 641 510 HOH HOH B . 
J 5 HOH 142 642 392 HOH HOH B . 
J 5 HOH 143 643 434 HOH HOH B . 
J 5 HOH 144 644 520 HOH HOH B . 
J 5 HOH 145 645 439 HOH HOH B . 
J 5 HOH 146 646 518 HOH HOH B . 
J 5 HOH 147 647 517 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LEU 4   ? CG  ? A LEU 24  CG  
2   1 Y 1 A LEU 4   ? CD1 ? A LEU 24  CD1 
3   1 Y 1 A LEU 4   ? CD2 ? A LEU 24  CD2 
4   1 Y 1 A ARG 7   ? CG  ? A ARG 27  CG  
5   1 Y 1 A ARG 7   ? CD  ? A ARG 27  CD  
6   1 Y 1 A ARG 7   ? NE  ? A ARG 27  NE  
7   1 Y 1 A ARG 7   ? CZ  ? A ARG 27  CZ  
8   1 Y 1 A ARG 7   ? NH1 ? A ARG 27  NH1 
9   1 Y 1 A ARG 7   ? NH2 ? A ARG 27  NH2 
10  1 Y 1 A ASP 33  ? OD1 ? A ASP 53  OD1 
11  1 Y 1 A ASP 33  ? OD2 ? A ASP 53  OD2 
12  1 Y 1 A LEU 129 ? CD1 ? A LEU 149 CD1 
13  1 Y 1 A LEU 129 ? CD2 ? A LEU 149 CD2 
14  1 Y 1 A ASP 169 ? CG  ? A ASP 189 CG  
15  1 Y 1 A ASP 169 ? OD1 ? A ASP 189 OD1 
16  1 Y 1 A ASP 169 ? OD2 ? A ASP 189 OD2 
17  1 Y 1 A ARG 194 ? CD  ? A ARG 214 CD  
18  1 Y 1 A ARG 194 ? NE  ? A ARG 214 NE  
19  1 Y 1 A ARG 194 ? CZ  ? A ARG 214 CZ  
20  1 Y 1 A ARG 194 ? NH1 ? A ARG 214 NH1 
21  1 Y 1 A ARG 194 ? NH2 ? A ARG 214 NH2 
22  1 Y 1 A GLU 196 ? CG  ? A GLU 216 CG  
23  1 Y 1 A GLU 196 ? CD  ? A GLU 216 CD  
24  1 Y 1 A GLU 196 ? OE1 ? A GLU 216 OE1 
25  1 Y 1 A GLU 196 ? OE2 ? A GLU 216 OE2 
26  1 Y 1 A ASP 211 ? CG  ? A ASP 231 CG  
27  1 Y 1 A ASP 211 ? OD1 ? A ASP 231 OD1 
28  1 Y 1 A ASP 211 ? OD2 ? A ASP 231 OD2 
29  1 Y 1 A GLU 212 ? CG  ? A GLU 232 CG  
30  1 Y 1 A GLU 212 ? CD  ? A GLU 232 CD  
31  1 Y 1 A GLU 212 ? OE1 ? A GLU 232 OE1 
32  1 Y 1 A GLU 212 ? OE2 ? A GLU 232 OE2 
33  1 Y 1 A ARG 214 ? CD  ? A ARG 234 CD  
34  1 Y 1 A ARG 214 ? NE  ? A ARG 234 NE  
35  1 Y 1 A ARG 214 ? CZ  ? A ARG 234 CZ  
36  1 Y 1 A ARG 214 ? NH1 ? A ARG 234 NH1 
37  1 Y 1 A ARG 214 ? NH2 ? A ARG 234 NH2 
38  1 Y 1 A GLU 260 ? CG  ? A GLU 280 CG  
39  1 Y 1 A GLU 260 ? CD  ? A GLU 280 CD  
40  1 Y 1 A GLU 260 ? OE1 ? A GLU 280 OE1 
41  1 Y 1 A GLU 260 ? OE2 ? A GLU 280 OE2 
42  1 Y 1 A ARG 345 ? NE  ? A ARG 365 NE  
43  1 Y 1 A ARG 345 ? CZ  ? A ARG 365 CZ  
44  1 Y 1 A ARG 345 ? NH1 ? A ARG 365 NH1 
45  1 Y 1 A ARG 345 ? NH2 ? A ARG 365 NH2 
46  1 Y 1 A GLN 373 ? CD  ? A GLN 393 CD  
47  1 Y 1 A GLN 373 ? OE1 ? A GLN 393 OE1 
48  1 Y 1 A GLN 373 ? NE2 ? A GLN 393 NE2 
49  1 Y 1 A GLN 375 ? CG  ? A GLN 395 CG  
50  1 Y 1 A GLN 375 ? CD  ? A GLN 395 CD  
51  1 Y 1 A GLN 375 ? OE1 ? A GLN 395 OE1 
52  1 Y 1 A GLN 375 ? NE2 ? A GLN 395 NE2 
53  1 Y 1 B TYR 14  ? O   ? B TYR 34  O   
54  1 Y 1 B ILE 16  ? CG1 ? B ILE 36  CG1 
55  1 Y 1 B ILE 16  ? CG2 ? B ILE 36  CG2 
56  1 Y 1 B ILE 16  ? CD1 ? B ILE 36  CD1 
57  1 Y 1 B ARG 19  ? CB  ? B ARG 39  CB  
58  1 Y 1 B ARG 19  ? CG  ? B ARG 39  CG  
59  1 Y 1 B ARG 19  ? CD  ? B ARG 39  CD  
60  1 Y 1 B ARG 19  ? NE  ? B ARG 39  NE  
61  1 Y 1 B ARG 19  ? CZ  ? B ARG 39  CZ  
62  1 Y 1 B ARG 19  ? NH1 ? B ARG 39  NH1 
63  1 Y 1 B ARG 19  ? NH2 ? B ARG 39  NH2 
64  1 Y 1 B LEU 20  ? CG  ? B LEU 40  CG  
65  1 Y 1 B LEU 20  ? CD1 ? B LEU 40  CD1 
66  1 Y 1 B LEU 20  ? CD2 ? B LEU 40  CD2 
67  1 Y 1 B ARG 21  ? CD  ? B ARG 41  CD  
68  1 Y 1 B ARG 21  ? NE  ? B ARG 41  NE  
69  1 Y 1 B ARG 21  ? CZ  ? B ARG 41  CZ  
70  1 Y 1 B ARG 21  ? NH1 ? B ARG 41  NH1 
71  1 Y 1 B ARG 21  ? NH2 ? B ARG 41  NH2 
72  1 Y 1 B ALA 22  ? CA  ? B ALA 42  CA  
73  1 Y 1 B ALA 22  ? CB  ? B ALA 42  CB  
74  1 Y 1 B ARG 27  ? NE  ? B ARG 47  NE  
75  1 Y 1 B ARG 27  ? CZ  ? B ARG 47  CZ  
76  1 Y 1 B ARG 27  ? NH1 ? B ARG 47  NH1 
77  1 Y 1 B ARG 27  ? NH2 ? B ARG 47  NH2 
78  1 Y 1 B ASP 33  ? OD1 ? B ASP 53  OD1 
79  1 Y 1 B ASP 33  ? OD2 ? B ASP 53  OD2 
80  1 Y 1 B LEU 75  ? CD1 ? B LEU 95  CD1 
81  1 Y 1 B GLU 97  ? CG  ? B GLU 117 CG  
82  1 Y 1 B GLU 97  ? CD  ? B GLU 117 CD  
83  1 Y 1 B GLU 97  ? OE1 ? B GLU 117 OE1 
84  1 Y 1 B GLU 97  ? OE2 ? B GLU 117 OE2 
85  1 Y 1 B ARG 101 ? CG  ? B ARG 121 CG  
86  1 Y 1 B ARG 101 ? CD  ? B ARG 121 CD  
87  1 Y 1 B ARG 101 ? NE  ? B ARG 121 NE  
88  1 Y 1 B ARG 101 ? CZ  ? B ARG 121 CZ  
89  1 Y 1 B ARG 101 ? NH1 ? B ARG 121 NH1 
90  1 Y 1 B ARG 101 ? NH2 ? B ARG 121 NH2 
91  1 Y 1 B GLU 105 ? CD  ? B GLU 125 CD  
92  1 Y 1 B GLU 105 ? OE1 ? B GLU 125 OE1 
93  1 Y 1 B GLU 105 ? OE2 ? B GLU 125 OE2 
94  1 Y 1 B GLU 125 ? CD  ? B GLU 145 CD  
95  1 Y 1 B GLU 125 ? OE1 ? B GLU 145 OE1 
96  1 Y 1 B GLU 125 ? OE2 ? B GLU 145 OE2 
97  1 Y 1 B ASP 169 ? CG  ? B ASP 189 CG  
98  1 Y 1 B ASP 169 ? OD1 ? B ASP 189 OD1 
99  1 Y 1 B ASP 169 ? OD2 ? B ASP 189 OD2 
100 1 Y 1 B ARG 194 ? NE  ? B ARG 214 NE  
101 1 Y 1 B ARG 194 ? CZ  ? B ARG 214 CZ  
102 1 Y 1 B ARG 194 ? NH1 ? B ARG 214 NH1 
103 1 Y 1 B ARG 194 ? NH2 ? B ARG 214 NH2 
104 1 Y 1 B HIS 199 ? CG  ? B HIS 219 CG  
105 1 Y 1 B HIS 199 ? ND1 ? B HIS 219 ND1 
106 1 Y 1 B HIS 199 ? CD2 ? B HIS 219 CD2 
107 1 Y 1 B HIS 199 ? CE1 ? B HIS 219 CE1 
108 1 Y 1 B HIS 199 ? NE2 ? B HIS 219 NE2 
109 1 Y 1 B LEU 201 ? CG  ? B LEU 221 CG  
110 1 Y 1 B LEU 201 ? CD1 ? B LEU 221 CD1 
111 1 Y 1 B LEU 201 ? CD2 ? B LEU 221 CD2 
112 1 Y 1 B VAL 208 ? CG1 ? B VAL 228 CG1 
113 1 Y 1 B VAL 208 ? CG2 ? B VAL 228 CG2 
114 1 Y 1 B ASP 210 ? OD1 ? B ASP 230 OD1 
115 1 Y 1 B ASP 210 ? OD2 ? B ASP 230 OD2 
116 1 Y 1 B GLU 212 ? CG  ? B GLU 232 CG  
117 1 Y 1 B GLU 212 ? CD  ? B GLU 232 CD  
118 1 Y 1 B GLU 212 ? OE1 ? B GLU 232 OE1 
119 1 Y 1 B GLU 212 ? OE2 ? B GLU 232 OE2 
120 1 Y 1 B ARG 214 ? CZ  ? B ARG 234 CZ  
121 1 Y 1 B ARG 214 ? NH1 ? B ARG 234 NH1 
122 1 Y 1 B ARG 214 ? NH2 ? B ARG 234 NH2 
123 1 Y 1 B ASP 251 ? CG  ? B ASP 271 CG  
124 1 Y 1 B ASP 251 ? OD1 ? B ASP 271 OD1 
125 1 Y 1 B ASP 251 ? OD2 ? B ASP 271 OD2 
126 1 Y 1 B ASP 255 ? OD1 ? B ASP 275 OD1 
127 1 Y 1 B ASP 255 ? OD2 ? B ASP 275 OD2 
128 1 Y 1 B ARG 257 ? CG  ? B ARG 277 CG  
129 1 Y 1 B ARG 257 ? CD  ? B ARG 277 CD  
130 1 Y 1 B ARG 257 ? NE  ? B ARG 277 NE  
131 1 Y 1 B ARG 257 ? CZ  ? B ARG 277 CZ  
132 1 Y 1 B ARG 257 ? NH1 ? B ARG 277 NH1 
133 1 Y 1 B ARG 257 ? NH2 ? B ARG 277 NH2 
134 1 Y 1 B GLU 260 ? CG  ? B GLU 280 CG  
135 1 Y 1 B GLU 260 ? CD  ? B GLU 280 CD  
136 1 Y 1 B GLU 260 ? OE1 ? B GLU 280 OE1 
137 1 Y 1 B GLU 260 ? OE2 ? B GLU 280 OE2 
138 1 Y 1 B LEU 263 ? CD1 ? B LEU 283 CD1 
139 1 Y 1 B LEU 263 ? CD2 ? B LEU 283 CD2 
140 1 Y 1 B ARG 265 ? CD  ? B ARG 285 CD  
141 1 Y 1 B ARG 265 ? NE  ? B ARG 285 NE  
142 1 Y 1 B ARG 265 ? CZ  ? B ARG 285 CZ  
143 1 Y 1 B ARG 265 ? NH1 ? B ARG 285 NH1 
144 1 Y 1 B ARG 265 ? NH2 ? B ARG 285 NH2 
145 1 Y 1 B ARG 287 ? CD  ? B ARG 307 CD  
146 1 Y 1 B ARG 287 ? NE  ? B ARG 307 NE  
147 1 Y 1 B ARG 287 ? CZ  ? B ARG 307 CZ  
148 1 Y 1 B ARG 287 ? NH1 ? B ARG 307 NH1 
149 1 Y 1 B ARG 287 ? NH2 ? B ARG 307 NH2 
150 1 Y 1 B GLU 288 ? CG  ? B GLU 308 CG  
151 1 Y 1 B GLU 288 ? CD  ? B GLU 308 CD  
152 1 Y 1 B GLU 288 ? OE1 ? B GLU 308 OE1 
153 1 Y 1 B GLU 288 ? OE2 ? B GLU 308 OE2 
154 1 Y 1 B LEU 289 ? CD1 ? B LEU 309 CD1 
155 1 Y 1 B LEU 289 ? CD2 ? B LEU 309 CD2 
156 1 Y 1 B ASP 290 ? CG  ? B ASP 310 CG  
157 1 Y 1 B ASP 290 ? OD1 ? B ASP 310 OD1 
158 1 Y 1 B ASP 290 ? OD2 ? B ASP 310 OD2 
159 1 Y 1 B ALA 292 ? CB  ? B ALA 312 CB  
160 1 Y 1 B VAL 294 ? CG1 ? B VAL 314 CG1 
161 1 Y 1 B VAL 294 ? CG2 ? B VAL 314 CG2 
162 1 Y 1 B GLU 295 ? CG  ? B GLU 315 CG  
163 1 Y 1 B GLU 295 ? CD  ? B GLU 315 CD  
164 1 Y 1 B GLU 295 ? OE1 ? B GLU 315 OE1 
165 1 Y 1 B GLU 295 ? OE2 ? B GLU 315 OE2 
166 1 Y 1 B ASP 312 ? CG  ? B ASP 332 CG  
167 1 Y 1 B ASP 312 ? OD1 ? B ASP 332 OD1 
168 1 Y 1 B ASP 312 ? OD2 ? B ASP 332 OD2 
169 1 Y 1 B GLU 313 ? OE2 ? B GLU 333 OE2 
170 1 Y 1 B THR 314 ? OG1 ? B THR 334 OG1 
171 1 Y 1 B THR 314 ? CG2 ? B THR 334 CG2 
172 1 Y 1 B ASP 317 ? CG  ? B ASP 337 CG  
173 1 Y 1 B ASP 317 ? OD1 ? B ASP 337 OD1 
174 1 Y 1 B ASP 317 ? OD2 ? B ASP 337 OD2 
175 1 Y 1 B PRO 319 ? CG  ? B PRO 339 CG  
176 1 Y 1 B ASP 320 ? OD1 ? B ASP 340 OD1 
177 1 Y 1 B ASP 323 ? CG  ? B ASP 343 CG  
178 1 Y 1 B ASP 323 ? OD1 ? B ASP 343 OD1 
179 1 Y 1 B ASP 323 ? OD2 ? B ASP 343 OD2 
180 1 Y 1 B ASP 327 ? CG  ? B ASP 347 CG  
181 1 Y 1 B ASP 327 ? OD1 ? B ASP 347 OD1 
182 1 Y 1 B ASP 327 ? OD2 ? B ASP 347 OD2 
183 1 Y 1 B ARG 345 ? CG  ? B ARG 365 CG  
184 1 Y 1 B ARG 345 ? CD  ? B ARG 365 CD  
185 1 Y 1 B ARG 345 ? NE  ? B ARG 365 NE  
186 1 Y 1 B ARG 345 ? CZ  ? B ARG 365 CZ  
187 1 Y 1 B ARG 345 ? NH1 ? B ARG 365 NH1 
188 1 Y 1 B ARG 345 ? NH2 ? B ARG 365 NH2 
189 1 Y 1 B ARG 364 ? CG  ? B ARG 384 CG  
190 1 Y 1 B ARG 364 ? CD  ? B ARG 384 CD  
191 1 Y 1 B ARG 364 ? NE  ? B ARG 384 NE  
192 1 Y 1 B ARG 364 ? CZ  ? B ARG 384 CZ  
193 1 Y 1 B ARG 364 ? NH1 ? B ARG 384 NH1 
194 1 Y 1 B ARG 364 ? NH2 ? B ARG 384 NH2 
195 1 Y 1 B VAL 367 ? CG1 ? B VAL 387 CG1 
196 1 Y 1 B VAL 367 ? CG2 ? B VAL 387 CG2 
197 1 Y 1 B ALA 370 ? CB  ? B ALA 390 CB  
198 1 Y 1 B GLN 373 ? OE1 ? B GLN 393 OE1 
199 1 Y 1 B GLN 373 ? NE2 ? B GLN 393 NE2 
200 1 Y 1 B GLN 375 ? OE1 ? B GLN 395 OE1 
201 1 Y 1 B GLN 375 ? NE2 ? B GLN 395 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM  ? ? ? 7.4.0       1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.7       2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot    ? ? ? 0.9.8.4     4 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CJG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     53.130 
_cell.length_a_esd                 ? 
_cell.length_b                     59.650 
_cell.length_b_esd                 ? 
_cell.length_c                     233.800 
_cell.length_c_esd                 ? 
_cell.volume                       740960.012 
_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                         9CJG 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_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                   9CJG 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.00 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.6 
_exptl_crystal.description                  'Colored rods' 
_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              7 
_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    '60% (v/v) tacsimate pH 7, 0.7% (v/v) 1-butanol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RAYONIX MX-300' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-02-18 
_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                    'C(111)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97872 
_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                        'APS BEAMLINE 21-ID-F' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97872 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-F 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          23.77 
_reflns.entry_id                                       9CJG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.85 
_reflns.d_resolution_low                               57.8 
_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                                     64200 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.59 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.05494 
_reflns.pdbx_Rpim_I_all                                0.03885 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.03885 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.85 
_reflns_shell.d_res_low                                     1.916 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.77 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6334 
_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                               2.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.5253 
_reflns_shell.pdbx_Rpim_I_all                               0.3714 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.68 
_reflns_shell.pdbx_CC_star                                  0.9 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.73 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.3714 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               30.59 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9CJG 
_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                            1.85 
_refine.ls_d_res_low                             57.8 
_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                     64161 
_refine.ls_number_reflns_R_free                  1999 
_refine.ls_number_reflns_R_work                  62162 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.30 
_refine.ls_percent_reflns_R_free                 3.12 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2152 
_refine.ls_R_factor_R_free                       0.2425 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2143 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 25.0595 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2577 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        57.8 
_refine_hist.number_atoms_solvent             489 
_refine_hist.number_atoms_total               6282 
_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        5691 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         102 
_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' ? 0.0084  ? 5941 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9436  ? 8148 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0556  ? 914  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0127  ? 1075 ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.3106 ? 2085 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.85 1.90 . . 141 4396 99.76 . . . . 0.3047 . . . . . . . . . . . 0.3558 
'X-RAY DIFFRACTION' 1.90 1.95 . . 142 4379 99.76 . . . . 0.2866 . . . . . . . . . . . 0.3397 
'X-RAY DIFFRACTION' 1.95 2.00 . . 141 4395 99.58 . . . . 0.2695 . . . . . . . . . . . 0.3094 
'X-RAY DIFFRACTION' 2.00 2.07 . . 141 4375 99.54 . . . . 0.2536 . . . . . . . . . . . 0.2956 
'X-RAY DIFFRACTION' 2.07 2.14 . . 142 4418 99.41 . . . . 0.2370 . . . . . . . . . . . 0.2829 
'X-RAY DIFFRACTION' 2.14 2.23 . . 141 4380 99.47 . . . . 0.2284 . . . . . . . . . . . 0.2631 
'X-RAY DIFFRACTION' 2.23 2.33 . . 142 4406 99.34 . . . . 0.2248 . . . . . . . . . . . 0.2736 
'X-RAY DIFFRACTION' 2.33 2.45 . . 141 4400 99.52 . . . . 0.2243 . . . . . . . . . . . 0.2613 
'X-RAY DIFFRACTION' 2.45 2.61 . . 141 4408 98.93 . . . . 0.2244 . . . . . . . . . . . 0.2588 
'X-RAY DIFFRACTION' 2.61 2.81 . . 143 4453 99.31 . . . . 0.2124 . . . . . . . . . . . 0.2772 
'X-RAY DIFFRACTION' 2.81 3.09 . . 143 4410 98.53 . . . . 0.2140 . . . . . . . . . . . 0.2490 
'X-RAY DIFFRACTION' 3.09 3.54 . . 142 4443 98.12 . . . . 0.1976 . . . . . . . . . . . 0.2430 
'X-RAY DIFFRACTION' 3.54 4.46 . . 145 4525 99.11 . . . . 0.1779 . . . . . . . . . . . 0.1909 
'X-RAY DIFFRACTION' 4.46 57.8 . . 154 4774 99.90 . . . . 0.2035 . . . . . . . . . . . 0.1952 
# 
_struct.entry_id                     9CJG 
_struct.title                        
'P450-G9 from Actinokineospora terrae, a non-canonical, serine-ligated cytochrome P450 in the ligand-free, closed conformation' 
_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        9CJG 
_struct_keywords.text            'P450, cytochrome, serine, P411, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 4 ? 
F N N 4 ? 
G N N 3 ? 
H N N 2 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1H9KM06_9PSEU 
_struct_ref.pdbx_db_accession          A0A1H9KM06 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSELFGRAFHVDPYPIYARLRAGGGIRQVSTPDGAAAWVVTRYDDVRAGLADPRLSVDRSNAGAGYRGFSLPPALDANLL
NLDPPDHTRLRTLIAGEFTPRRVHELVPAIEAAARELLAGLPSGEPVDLIAGFAAPLPLRVIGDLLGVPPADRARFRGWT
TTLLTPGPDQPPTAARDAVVAMHGFLVDLVAAKRAEPGHDLLSGLIAVRDDEDRLSEAELVSMAFLALWAGYENLVHLIG
NGVRALLAAPDQLADLRSDEALLPRAIEELTRFDQPLQWAIRRFPTRELDIAGVEVPAGDTVLLGIASANHDETVFDLPD
TLDLRRDPNPHLSYGHGIHRSFGSRLSQAEAAAAFSALLARGFRAAVDLADLQWQPSFRNRGLTELPLLLG
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CJG A 21 ? 411 ? A0A1H9KM06 1 ? 391 ? 1 391 
2 1 9CJG B 21 ? 411 ? A0A1H9KM06 1 ? 391 ? 1 391 
# 
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 9CJG MET A 1  ? UNP A0A1H9KM06 ? ? 'initiating methionine' -19 1  
1 9CJG GLY A 2  ? UNP A0A1H9KM06 ? ? 'expression tag'        -18 2  
1 9CJG SER A 3  ? UNP A0A1H9KM06 ? ? 'expression tag'        -17 3  
1 9CJG SER A 4  ? UNP A0A1H9KM06 ? ? 'expression tag'        -16 4  
1 9CJG HIS A 5  ? UNP A0A1H9KM06 ? ? 'expression tag'        -15 5  
1 9CJG HIS A 6  ? UNP A0A1H9KM06 ? ? 'expression tag'        -14 6  
1 9CJG HIS A 7  ? UNP A0A1H9KM06 ? ? 'expression tag'        -13 7  
1 9CJG HIS A 8  ? UNP A0A1H9KM06 ? ? 'expression tag'        -12 8  
1 9CJG HIS A 9  ? UNP A0A1H9KM06 ? ? 'expression tag'        -11 9  
1 9CJG HIS A 10 ? UNP A0A1H9KM06 ? ? 'expression tag'        -10 10 
1 9CJG SER A 11 ? UNP A0A1H9KM06 ? ? 'expression tag'        -9  11 
1 9CJG SER A 12 ? UNP A0A1H9KM06 ? ? 'expression tag'        -8  12 
1 9CJG GLY A 13 ? UNP A0A1H9KM06 ? ? 'expression tag'        -7  13 
1 9CJG LEU A 14 ? UNP A0A1H9KM06 ? ? 'expression tag'        -6  14 
1 9CJG VAL A 15 ? UNP A0A1H9KM06 ? ? 'expression tag'        -5  15 
1 9CJG PRO A 16 ? UNP A0A1H9KM06 ? ? 'expression tag'        -4  16 
1 9CJG ARG A 17 ? UNP A0A1H9KM06 ? ? 'expression tag'        -3  17 
1 9CJG GLY A 18 ? UNP A0A1H9KM06 ? ? 'expression tag'        -2  18 
1 9CJG SER A 19 ? UNP A0A1H9KM06 ? ? 'expression tag'        -1  19 
1 9CJG HIS A 20 ? UNP A0A1H9KM06 ? ? 'expression tag'        0   20 
2 9CJG MET B 1  ? UNP A0A1H9KM06 ? ? 'initiating methionine' -19 21 
2 9CJG GLY B 2  ? UNP A0A1H9KM06 ? ? 'expression tag'        -18 22 
2 9CJG SER B 3  ? UNP A0A1H9KM06 ? ? 'expression tag'        -17 23 
2 9CJG SER B 4  ? UNP A0A1H9KM06 ? ? 'expression tag'        -16 24 
2 9CJG HIS B 5  ? UNP A0A1H9KM06 ? ? 'expression tag'        -15 25 
2 9CJG HIS B 6  ? UNP A0A1H9KM06 ? ? 'expression tag'        -14 26 
2 9CJG HIS B 7  ? UNP A0A1H9KM06 ? ? 'expression tag'        -13 27 
2 9CJG HIS B 8  ? UNP A0A1H9KM06 ? ? 'expression tag'        -12 28 
2 9CJG HIS B 9  ? UNP A0A1H9KM06 ? ? 'expression tag'        -11 29 
2 9CJG HIS B 10 ? UNP A0A1H9KM06 ? ? 'expression tag'        -10 30 
2 9CJG SER B 11 ? UNP A0A1H9KM06 ? ? 'expression tag'        -9  31 
2 9CJG SER B 12 ? UNP A0A1H9KM06 ? ? 'expression tag'        -8  32 
2 9CJG GLY B 13 ? UNP A0A1H9KM06 ? ? 'expression tag'        -7  33 
2 9CJG LEU B 14 ? UNP A0A1H9KM06 ? ? 'expression tag'        -6  34 
2 9CJG VAL B 15 ? UNP A0A1H9KM06 ? ? 'expression tag'        -5  35 
2 9CJG PRO B 16 ? UNP A0A1H9KM06 ? ? 'expression tag'        -4  36 
2 9CJG ARG B 17 ? UNP A0A1H9KM06 ? ? 'expression tag'        -3  37 
2 9CJG GLY B 18 ? UNP A0A1H9KM06 ? ? 'expression tag'        -2  38 
2 9CJG SER B 19 ? UNP A0A1H9KM06 ? ? 'expression tag'        -1  39 
2 9CJG HIS B 20 ? UNP A0A1H9KM06 ? ? 'expression tag'        0   40 
# 
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_defined_assembly ? monomeric 1 
2 author_defined_assembly ? 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,I 
2 1 B,H,J         
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 26  ? ASP A 32  ? GLY A 6   ASP A 12  1 ? 7  
HELX_P HELX_P2  AA2 PRO A 33  ? GLY A 43  ? PRO A 13  GLY A 23  1 ? 11 
HELX_P HELX_P3  AA3 ARG A 62  ? ASP A 72  ? ARG A 42  ASP A 52  1 ? 11 
HELX_P HELX_P4  AA4 ASP A 78  ? ALA A 82  ? ASP A 58  ALA A 62  5 ? 5  
HELX_P HELX_P5  AA5 ASN A 98  ? LEU A 102 ? ASN A 78  LEU A 82  5 ? 5  
HELX_P HELX_P6  AA6 PRO A 105 ? GLY A 116 ? PRO A 85  GLY A 96  1 ? 12 
HELX_P HELX_P7  AA7 THR A 119 ? GLY A 140 ? THR A 99  GLY A 120 1 ? 22 
HELX_P HELX_P8  AA8 LEU A 149 ? PHE A 153 ? LEU A 129 PHE A 133 1 ? 5  
HELX_P HELX_P9  AA9 ALA A 155 ? GLY A 167 ? ALA A 135 GLY A 147 1 ? 13 
HELX_P HELX_P10 AB1 PRO A 169 ? ALA A 171 ? PRO A 149 ALA A 151 5 ? 3  
HELX_P HELX_P11 AB2 ASP A 172 ? THR A 185 ? ASP A 152 THR A 165 1 ? 14 
HELX_P HELX_P12 AB3 THR A 193 ? GLU A 216 ? THR A 173 GLU A 196 1 ? 24 
HELX_P HELX_P13 AB4 ASP A 220 ? VAL A 228 ? ASP A 200 VAL A 208 1 ? 9  
HELX_P HELX_P14 AB5 SER A 236 ? TYR A 252 ? SER A 216 TYR A 232 1 ? 17 
HELX_P HELX_P15 AB6 TYR A 252 ? ALA A 269 ? TYR A 232 ALA A 249 1 ? 18 
HELX_P HELX_P16 AB7 ALA A 269 ? ASP A 279 ? ALA A 249 ASP A 259 1 ? 11 
HELX_P HELX_P17 AB8 LEU A 282 ? GLN A 295 ? LEU A 262 GLN A 275 1 ? 14 
HELX_P HELX_P18 AB9 GLY A 325 ? HIS A 331 ? GLY A 305 HIS A 311 1 ? 7  
HELX_P HELX_P19 AC1 GLY A 363 ? GLY A 382 ? GLY A 343 GLY A 362 1 ? 20 
HELX_P HELX_P20 AC2 ASP A 388 ? LEU A 392 ? ASP A 368 LEU A 372 5 ? 5  
HELX_P HELX_P21 AC3 PRO B 35  ? ARG B 41  ? PRO B 15  ARG B 21  1 ? 7  
HELX_P HELX_P22 AC4 ARG B 62  ? ASP B 72  ? ARG B 42  ASP B 52  1 ? 11 
HELX_P HELX_P23 AC5 ASP B 78  ? ALA B 82  ? ASP B 58  ALA B 62  5 ? 5  
HELX_P HELX_P24 AC6 ASN B 98  ? LEU B 102 ? ASN B 78  LEU B 82  5 ? 5  
HELX_P HELX_P25 AC7 PRO B 105 ? PHE B 118 ? PRO B 85  PHE B 98  1 ? 14 
HELX_P HELX_P26 AC8 THR B 119 ? GLY B 140 ? THR B 99  GLY B 120 1 ? 22 
HELX_P HELX_P27 AC9 LEU B 149 ? PHE B 153 ? LEU B 129 PHE B 133 1 ? 5  
HELX_P HELX_P28 AD1 ALA B 155 ? GLY B 167 ? ALA B 135 GLY B 147 1 ? 13 
HELX_P HELX_P29 AD2 PRO B 169 ? ALA B 171 ? PRO B 149 ALA B 151 5 ? 3  
HELX_P HELX_P30 AD3 ASP B 172 ? THR B 185 ? ASP B 152 THR B 165 1 ? 14 
HELX_P HELX_P31 AD4 THR B 193 ? GLU B 216 ? THR B 173 GLU B 196 1 ? 24 
HELX_P HELX_P32 AD5 ASP B 220 ? VAL B 228 ? ASP B 200 VAL B 208 1 ? 9  
HELX_P HELX_P33 AD6 SER B 236 ? TYR B 252 ? SER B 216 TYR B 232 1 ? 17 
HELX_P HELX_P34 AD7 TYR B 252 ? ALA B 269 ? TYR B 232 ALA B 249 1 ? 18 
HELX_P HELX_P35 AD8 ALA B 269 ? ASP B 279 ? ALA B 249 ASP B 259 1 ? 11 
HELX_P HELX_P36 AD9 LEU B 282 ? GLN B 295 ? LEU B 262 GLN B 275 1 ? 14 
HELX_P HELX_P37 AE1 GLY B 325 ? ASN B 330 ? GLY B 305 ASN B 310 1 ? 6  
HELX_P HELX_P38 AE2 GLY B 363 ? GLY B 382 ? GLY B 343 GLY B 362 1 ? 20 
HELX_P HELX_P39 AE3 ASP B 388 ? LEU B 392 ? ASP B 368 LEU B 372 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 ? ? A SER 361 OG ? ? ? 1_555 C HEM . FE ? ? A SER 341 A HEM 401 1_555 ? ? ? ? ? ? ? 2.369 ? ? 
metalc2 metalc ? ? B SER 361 OG ? ? ? 1_555 H HEM . FE ? ? B SER 341 B HEM 401 1_555 ? ? ? ? ? ? ? 2.430 ? ? 
# 
_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  OG ? A SER 361 ? A SER 341 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NA ? C HEM . ? A HEM 401 ? 1_555 88.4  ? 
2  OG ? A SER 361 ? A SER 341 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NB ? C HEM . ? A HEM 401 ? 1_555 81.9  ? 
3  NA ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NB ? C HEM . ? A HEM 401 ? 1_555 87.8  ? 
4  OG ? A SER 361 ? A SER 341 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NC ? C HEM . ? A HEM 401 ? 1_555 89.4  ? 
5  NA ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NC ? C HEM . ? A HEM 401 ? 1_555 173.7 ? 
6  NB ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NC ? C HEM . ? A HEM 401 ? 1_555 86.0  ? 
7  OG ? A SER 361 ? A SER 341 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND ? C HEM . ? A HEM 401 ? 1_555 99.2  ? 
8  NA ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND ? C HEM . ? A HEM 401 ? 1_555 93.8  ? 
9  NB ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND ? C HEM . ? A HEM 401 ? 1_555 178.1 ? 
10 NC ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND ? C HEM . ? A HEM 401 ? 1_555 92.4  ? 
11 OG ? B SER 361 ? B SER 341 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 NA ? H HEM . ? B HEM 401 ? 1_555 90.9  ? 
12 OG ? B SER 361 ? B SER 341 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 NB ? H HEM . ? B HEM 401 ? 1_555 78.6  ? 
13 NA ? H HEM .   ? B HEM 401 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 NB ? H HEM . ? B HEM 401 ? 1_555 87.7  ? 
14 OG ? B SER 361 ? B SER 341 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 NC ? H HEM . ? B HEM 401 ? 1_555 83.7  ? 
15 NA ? H HEM .   ? B HEM 401 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 NC ? H HEM . ? B HEM 401 ? 1_555 172.6 ? 
16 NB ? H HEM .   ? B HEM 401 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 NC ? H HEM . ? B HEM 401 ? 1_555 86.1  ? 
17 OG ? B SER 361 ? B SER 341 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 ND ? H HEM . ? B HEM 401 ? 1_555 100.1 ? 
18 NA ? H HEM .   ? B HEM 401 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 ND ? H HEM . ? B HEM 401 ? 1_555 93.7  ? 
19 NB ? H HEM .   ? B HEM 401 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 ND ? H HEM . ? B HEM 401 ? 1_555 178.1 ? 
20 NC ? H HEM .   ? B HEM 401 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 ND ? H HEM . ? B HEM 401 ? 1_555 92.3  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 104 A . ? PRO 84  A PRO 105 A ? PRO 85  A 1 4.72  
2 ASP 347 A . ? ASP 327 A PRO 348 A ? PRO 328 A 1 0.20  
3 PRO 104 B . ? PRO 84  B PRO 105 B ? PRO 85  B 1 27.52 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 3 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 46  ? SER A 50  ? ILE A 26  SER A 30  
AA1 2 ALA A 56  ? VAL A 60  ? ALA A 36  VAL A 40  
AA1 3 VAL A 322 ? LEU A 324 ? VAL A 302 LEU A 304 
AA2 1 LEU A 75  ? SER A 76  ? LEU A 55  SER A 56  
AA2 2 PHE A 304 ? PRO A 305 ? PHE A 284 PRO A 285 
AA3 1 VAL A 147 ? ASP A 148 ? VAL A 127 ASP A 128 
AA3 2 PRO A 407 ? LEU A 410 ? PRO A 387 LEU A 390 
AA3 3 PHE A 383 ? ALA A 385 ? PHE A 363 ALA A 365 
AA4 1 LEU A 309 ? ILE A 311 ? LEU A 289 ILE A 291 
AA4 2 VAL A 314 ? VAL A 316 ? VAL A 294 VAL A 296 
AA5 1 ILE B 46  ? SER B 50  ? ILE B 26  SER B 30  
AA5 2 ALA B 56  ? VAL B 60  ? ALA B 36  VAL B 40  
AA5 3 VAL B 322 ? LEU B 324 ? VAL B 302 LEU B 304 
AA6 1 LEU B 75  ? SER B 76  ? LEU B 55  SER B 56  
AA6 2 PHE B 304 ? PRO B 305 ? PHE B 284 PRO B 285 
AA7 1 PRO B 146 ? ASP B 148 ? PRO B 126 ASP B 128 
AA7 2 PRO B 407 ? LEU B 410 ? PRO B 387 LEU B 390 
AA7 3 PHE B 383 ? ALA B 385 ? PHE B 363 ALA B 365 
AA8 1 ARG B 229 ? ASP B 230 ? ARG B 209 ASP B 210 
AA8 2 ASP B 233 ? ARG B 234 ? ASP B 213 ARG B 214 
AA9 1 LEU B 309 ? ILE B 311 ? LEU B 289 ILE B 291 
AA9 2 VAL B 314 ? VAL B 316 ? VAL B 294 VAL B 296 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 49  ? N VAL A 29  O ALA A 57  ? O ALA A 37  
AA1 2 3 N TRP A 58  ? N TRP A 38  O LEU A 323 ? O LEU A 303 
AA2 1 2 N SER A 76  ? N SER A 56  O PHE A 304 ? O PHE A 284 
AA3 1 2 N VAL A 147 ? N VAL A 127 O LEU A 408 ? O LEU A 388 
AA3 2 3 O LEU A 409 ? O LEU A 389 N ARG A 384 ? N ARG A 364 
AA4 1 2 N LEU A 309 ? N LEU A 289 O VAL A 316 ? O VAL A 296 
AA5 1 2 N VAL B 49  ? N VAL B 29  O ALA B 57  ? O ALA B 37  
AA5 2 3 N TRP B 58  ? N TRP B 38  O LEU B 323 ? O LEU B 303 
AA6 1 2 N SER B 76  ? N SER B 56  O PHE B 304 ? O PHE B 284 
AA7 1 2 N VAL B 147 ? N VAL B 127 O LEU B 408 ? O LEU B 388 
AA7 2 3 O LEU B 409 ? O LEU B 389 N ARG B 384 ? N ARG B 364 
AA8 1 2 N ASP B 230 ? N ASP B 210 O ASP B 233 ? O ASP B 213 
AA9 1 2 N LEU B 309 ? N LEU B 289 O VAL B 316 ? O VAL B 296 
# 
_pdbx_entry_details.entry_id                   9CJG 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 76  ? ? 63.09   -177.26 
2  1 PHE A 133 ? ? -143.36 -57.88  
3  1 GLU A 212 ? ? 77.37   -10.95  
4  1 TYR A 232 ? ? -121.13 -62.48  
5  1 ASP A 274 ? ? -150.91 33.57   
6  1 PRO B 32  ? ? -67.67  0.14    
7  1 ASP B 76  ? ? 70.60   177.99  
8  1 PHE B 133 ? ? -151.21 -57.75  
9  1 ASP B 211 ? ? 58.11   -123.73 
10 1 ALA B 249 ? ? -111.88 79.25   
11 1 ASP B 274 ? ? -155.58 27.14   
12 1 GLN B 275 ? ? -49.21  154.06  
13 1 ARG B 326 ? ? -57.73  102.44  
14 1 PRO B 330 ? ? -82.84  48.60   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? B HOH 645 ? 6.17 . 
2 1 O ? B HOH 646 ? 6.27 . 
3 1 O ? B HOH 647 ? 6.37 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -19 ? A MET 1  
2  1 Y 1 A GLY -18 ? A GLY 2  
3  1 Y 1 A SER -17 ? A SER 3  
4  1 Y 1 A SER -16 ? A SER 4  
5  1 Y 1 A HIS -15 ? A HIS 5  
6  1 Y 1 A HIS -14 ? A HIS 6  
7  1 Y 1 A HIS -13 ? A HIS 7  
8  1 Y 1 A HIS -12 ? A HIS 8  
9  1 Y 1 A HIS -11 ? A HIS 9  
10 1 Y 1 A HIS -10 ? A HIS 10 
11 1 Y 1 A SER -9  ? A SER 11 
12 1 Y 1 A SER -8  ? A SER 12 
13 1 Y 1 A GLY -7  ? A GLY 13 
14 1 Y 1 A LEU -6  ? A LEU 14 
15 1 Y 1 A VAL -5  ? A VAL 15 
16 1 Y 1 A PRO -4  ? A PRO 16 
17 1 Y 1 A ARG -3  ? A ARG 17 
18 1 Y 1 A GLY -2  ? A GLY 18 
19 1 Y 1 A SER -1  ? A SER 19 
20 1 Y 1 A HIS 0   ? A HIS 20 
21 1 Y 1 A MET 1   ? A MET 21 
22 1 Y 1 A SER 2   ? A SER 22 
23 1 Y 1 A GLU 3   ? A GLU 23 
24 1 Y 1 B MET -19 ? B MET 1  
25 1 Y 1 B GLY -18 ? B GLY 2  
26 1 Y 1 B SER -17 ? B SER 3  
27 1 Y 1 B SER -16 ? B SER 4  
28 1 Y 1 B HIS -15 ? B HIS 5  
29 1 Y 1 B HIS -14 ? B HIS 6  
30 1 Y 1 B HIS -13 ? B HIS 7  
31 1 Y 1 B HIS -12 ? B HIS 8  
32 1 Y 1 B HIS -11 ? B HIS 9  
33 1 Y 1 B HIS -10 ? B HIS 10 
34 1 Y 1 B SER -9  ? B SER 11 
35 1 Y 1 B SER -8  ? B SER 12 
36 1 Y 1 B GLY -7  ? B GLY 13 
37 1 Y 1 B LEU -6  ? B LEU 14 
38 1 Y 1 B VAL -5  ? B VAL 15 
39 1 Y 1 B PRO -4  ? B PRO 16 
40 1 Y 1 B ARG -3  ? B ARG 17 
41 1 Y 1 B GLY -2  ? B GLY 18 
42 1 Y 1 B SER -1  ? B SER 19 
43 1 Y 1 B HIS 0   ? B HIS 20 
44 1 Y 1 B MET 1   ? B MET 21 
45 1 Y 1 B SER 2   ? B SER 22 
46 1 Y 1 B GLU 3   ? B GLU 23 
47 1 Y 1 B LEU 4   ? B LEU 24 
48 1 Y 1 B PHE 5   ? B PHE 25 
49 1 Y 1 B GLY 6   ? B GLY 26 
50 1 Y 1 B ARG 7   ? B ARG 27 
# 
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 
1BO C1   C  N N 1   
1BO C2   C  N N 2   
1BO C3   C  N N 3   
1BO C4   C  N N 4   
1BO OH   O  N N 5   
1BO H11  H  N N 6   
1BO H12  H  N N 7   
1BO H13  H  N N 8   
1BO H21  H  N N 9   
1BO H22  H  N N 10  
1BO H31  H  N N 11  
1BO H32  H  N N 12  
1BO H41  H  N N 13  
1BO H42  H  N N 14  
1BO HO   H  N N 15  
ALA N    N  N N 16  
ALA CA   C  N S 17  
ALA C    C  N N 18  
ALA O    O  N N 19  
ALA CB   C  N N 20  
ALA OXT  O  N N 21  
ALA H    H  N N 22  
ALA H2   H  N N 23  
ALA HA   H  N N 24  
ALA HB1  H  N N 25  
ALA HB2  H  N N 26  
ALA HB3  H  N N 27  
ALA HXT  H  N N 28  
ARG N    N  N N 29  
ARG CA   C  N S 30  
ARG C    C  N N 31  
ARG O    O  N N 32  
ARG CB   C  N N 33  
ARG CG   C  N N 34  
ARG CD   C  N N 35  
ARG NE   N  N N 36  
ARG CZ   C  N N 37  
ARG NH1  N  N N 38  
ARG NH2  N  N N 39  
ARG OXT  O  N N 40  
ARG H    H  N N 41  
ARG H2   H  N N 42  
ARG HA   H  N N 43  
ARG HB2  H  N N 44  
ARG HB3  H  N N 45  
ARG HG2  H  N N 46  
ARG HG3  H  N N 47  
ARG HD2  H  N N 48  
ARG HD3  H  N N 49  
ARG HE   H  N N 50  
ARG HH11 H  N N 51  
ARG HH12 H  N N 52  
ARG HH21 H  N N 53  
ARG HH22 H  N N 54  
ARG HXT  H  N N 55  
ASN N    N  N N 56  
ASN CA   C  N S 57  
ASN C    C  N N 58  
ASN O    O  N N 59  
ASN CB   C  N N 60  
ASN CG   C  N N 61  
ASN OD1  O  N N 62  
ASN ND2  N  N N 63  
ASN OXT  O  N N 64  
ASN H    H  N N 65  
ASN H2   H  N N 66  
ASN HA   H  N N 67  
ASN HB2  H  N N 68  
ASN HB3  H  N N 69  
ASN HD21 H  N N 70  
ASN HD22 H  N N 71  
ASN HXT  H  N N 72  
ASP N    N  N N 73  
ASP CA   C  N S 74  
ASP C    C  N N 75  
ASP O    O  N N 76  
ASP CB   C  N N 77  
ASP CG   C  N N 78  
ASP OD1  O  N N 79  
ASP OD2  O  N N 80  
ASP OXT  O  N N 81  
ASP H    H  N N 82  
ASP H2   H  N N 83  
ASP HA   H  N N 84  
ASP HB2  H  N N 85  
ASP HB3  H  N N 86  
ASP HD2  H  N N 87  
ASP HXT  H  N N 88  
FMT C    C  N N 89  
FMT O1   O  N N 90  
FMT O2   O  N N 91  
FMT H    H  N N 92  
FMT HO2  H  N N 93  
GLN N    N  N N 94  
GLN CA   C  N S 95  
GLN C    C  N N 96  
GLN O    O  N N 97  
GLN CB   C  N N 98  
GLN CG   C  N N 99  
GLN CD   C  N N 100 
GLN OE1  O  N N 101 
GLN NE2  N  N N 102 
GLN OXT  O  N N 103 
GLN H    H  N N 104 
GLN H2   H  N N 105 
GLN HA   H  N N 106 
GLN HB2  H  N N 107 
GLN HB3  H  N N 108 
GLN HG2  H  N N 109 
GLN HG3  H  N N 110 
GLN HE21 H  N N 111 
GLN HE22 H  N N 112 
GLN HXT  H  N N 113 
GLU N    N  N N 114 
GLU CA   C  N S 115 
GLU C    C  N N 116 
GLU O    O  N N 117 
GLU CB   C  N N 118 
GLU CG   C  N N 119 
GLU CD   C  N N 120 
GLU OE1  O  N N 121 
GLU OE2  O  N N 122 
GLU OXT  O  N N 123 
GLU H    H  N N 124 
GLU H2   H  N N 125 
GLU HA   H  N N 126 
GLU HB2  H  N N 127 
GLU HB3  H  N N 128 
GLU HG2  H  N N 129 
GLU HG3  H  N N 130 
GLU HE2  H  N N 131 
GLU HXT  H  N N 132 
GLY N    N  N N 133 
GLY CA   C  N N 134 
GLY C    C  N N 135 
GLY O    O  N N 136 
GLY OXT  O  N N 137 
GLY H    H  N N 138 
GLY H2   H  N N 139 
GLY HA2  H  N N 140 
GLY HA3  H  N N 141 
GLY HXT  H  N N 142 
HEM CHA  C  N N 143 
HEM CHB  C  N N 144 
HEM CHC  C  N N 145 
HEM CHD  C  N N 146 
HEM C1A  C  Y N 147 
HEM C2A  C  Y N 148 
HEM C3A  C  Y N 149 
HEM C4A  C  Y N 150 
HEM CMA  C  N N 151 
HEM CAA  C  N N 152 
HEM CBA  C  N N 153 
HEM CGA  C  N N 154 
HEM O1A  O  N N 155 
HEM O2A  O  N N 156 
HEM C1B  C  N N 157 
HEM C2B  C  N N 158 
HEM C3B  C  N N 159 
HEM C4B  C  N N 160 
HEM CMB  C  N N 161 
HEM CAB  C  N N 162 
HEM CBB  C  N N 163 
HEM C1C  C  Y N 164 
HEM C2C  C  Y N 165 
HEM C3C  C  Y N 166 
HEM C4C  C  Y N 167 
HEM CMC  C  N N 168 
HEM CAC  C  N N 169 
HEM CBC  C  N N 170 
HEM C1D  C  N N 171 
HEM C2D  C  N N 172 
HEM C3D  C  N N 173 
HEM C4D  C  N N 174 
HEM CMD  C  N N 175 
HEM CAD  C  N N 176 
HEM CBD  C  N N 177 
HEM CGD  C  N N 178 
HEM O1D  O  N N 179 
HEM O2D  O  N N 180 
HEM NA   N  Y N 181 
HEM NB   N  N N 182 
HEM NC   N  Y N 183 
HEM ND   N  N N 184 
HEM FE   FE N N 185 
HEM HHB  H  N N 186 
HEM HHC  H  N N 187 
HEM HHD  H  N N 188 
HEM HMA  H  N N 189 
HEM HMAA H  N N 190 
HEM HMAB H  N N 191 
HEM HAA  H  N N 192 
HEM HAAA H  N N 193 
HEM HBA  H  N N 194 
HEM HBAA H  N N 195 
HEM HMB  H  N N 196 
HEM HMBA H  N N 197 
HEM HMBB H  N N 198 
HEM HAB  H  N N 199 
HEM HBB  H  N N 200 
HEM HBBA H  N N 201 
HEM HMC  H  N N 202 
HEM HMCA H  N N 203 
HEM HMCB H  N N 204 
HEM HAC  H  N N 205 
HEM HBC  H  N N 206 
HEM HBCA H  N N 207 
HEM HMD  H  N N 208 
HEM HMDA H  N N 209 
HEM HMDB H  N N 210 
HEM HAD  H  N N 211 
HEM HADA H  N N 212 
HEM HBD  H  N N 213 
HEM HBDA H  N N 214 
HEM H2A  H  N N 215 
HEM H2D  H  N N 216 
HEM HHA  H  N N 217 
HIS N    N  N N 218 
HIS CA   C  N S 219 
HIS C    C  N N 220 
HIS O    O  N N 221 
HIS CB   C  N N 222 
HIS CG   C  Y N 223 
HIS ND1  N  Y N 224 
HIS CD2  C  Y N 225 
HIS CE1  C  Y N 226 
HIS NE2  N  Y N 227 
HIS OXT  O  N N 228 
HIS H    H  N N 229 
HIS H2   H  N N 230 
HIS HA   H  N N 231 
HIS HB2  H  N N 232 
HIS HB3  H  N N 233 
HIS HD1  H  N N 234 
HIS HD2  H  N N 235 
HIS HE1  H  N N 236 
HIS HE2  H  N N 237 
HIS HXT  H  N N 238 
HOH O    O  N N 239 
HOH H1   H  N N 240 
HOH H2   H  N N 241 
ILE N    N  N N 242 
ILE CA   C  N S 243 
ILE C    C  N N 244 
ILE O    O  N N 245 
ILE CB   C  N S 246 
ILE CG1  C  N N 247 
ILE CG2  C  N N 248 
ILE CD1  C  N N 249 
ILE OXT  O  N N 250 
ILE H    H  N N 251 
ILE H2   H  N N 252 
ILE HA   H  N N 253 
ILE HB   H  N N 254 
ILE HG12 H  N N 255 
ILE HG13 H  N N 256 
ILE HG21 H  N N 257 
ILE HG22 H  N N 258 
ILE HG23 H  N N 259 
ILE HD11 H  N N 260 
ILE HD12 H  N N 261 
ILE HD13 H  N N 262 
ILE HXT  H  N N 263 
LEU N    N  N N 264 
LEU CA   C  N S 265 
LEU C    C  N N 266 
LEU O    O  N N 267 
LEU CB   C  N N 268 
LEU CG   C  N N 269 
LEU CD1  C  N N 270 
LEU CD2  C  N N 271 
LEU OXT  O  N N 272 
LEU H    H  N N 273 
LEU H2   H  N N 274 
LEU HA   H  N N 275 
LEU HB2  H  N N 276 
LEU HB3  H  N N 277 
LEU HG   H  N N 278 
LEU HD11 H  N N 279 
LEU HD12 H  N N 280 
LEU HD13 H  N N 281 
LEU HD21 H  N N 282 
LEU HD22 H  N N 283 
LEU HD23 H  N N 284 
LEU HXT  H  N N 285 
LYS N    N  N N 286 
LYS CA   C  N S 287 
LYS C    C  N N 288 
LYS O    O  N N 289 
LYS CB   C  N N 290 
LYS CG   C  N N 291 
LYS CD   C  N N 292 
LYS CE   C  N N 293 
LYS NZ   N  N N 294 
LYS OXT  O  N N 295 
LYS H    H  N N 296 
LYS H2   H  N N 297 
LYS HA   H  N N 298 
LYS HB2  H  N N 299 
LYS HB3  H  N N 300 
LYS HG2  H  N N 301 
LYS HG3  H  N N 302 
LYS HD2  H  N N 303 
LYS HD3  H  N N 304 
LYS HE2  H  N N 305 
LYS HE3  H  N N 306 
LYS HZ1  H  N N 307 
LYS HZ2  H  N N 308 
LYS HZ3  H  N N 309 
LYS HXT  H  N N 310 
MET N    N  N N 311 
MET CA   C  N S 312 
MET C    C  N N 313 
MET O    O  N N 314 
MET CB   C  N N 315 
MET CG   C  N N 316 
MET SD   S  N N 317 
MET CE   C  N N 318 
MET OXT  O  N N 319 
MET H    H  N N 320 
MET H2   H  N N 321 
MET HA   H  N N 322 
MET HB2  H  N N 323 
MET HB3  H  N N 324 
MET HG2  H  N N 325 
MET HG3  H  N N 326 
MET HE1  H  N N 327 
MET HE2  H  N N 328 
MET HE3  H  N N 329 
MET HXT  H  N N 330 
PHE N    N  N N 331 
PHE CA   C  N S 332 
PHE C    C  N N 333 
PHE O    O  N N 334 
PHE CB   C  N N 335 
PHE CG   C  Y N 336 
PHE CD1  C  Y N 337 
PHE CD2  C  Y N 338 
PHE CE1  C  Y N 339 
PHE CE2  C  Y N 340 
PHE CZ   C  Y N 341 
PHE OXT  O  N N 342 
PHE H    H  N N 343 
PHE H2   H  N N 344 
PHE HA   H  N N 345 
PHE HB2  H  N N 346 
PHE HB3  H  N N 347 
PHE HD1  H  N N 348 
PHE HD2  H  N N 349 
PHE HE1  H  N N 350 
PHE HE2  H  N N 351 
PHE HZ   H  N N 352 
PHE HXT  H  N N 353 
PRO N    N  N N 354 
PRO CA   C  N S 355 
PRO C    C  N N 356 
PRO O    O  N N 357 
PRO CB   C  N N 358 
PRO CG   C  N N 359 
PRO CD   C  N N 360 
PRO OXT  O  N N 361 
PRO H    H  N N 362 
PRO HA   H  N N 363 
PRO HB2  H  N N 364 
PRO HB3  H  N N 365 
PRO HG2  H  N N 366 
PRO HG3  H  N N 367 
PRO HD2  H  N N 368 
PRO HD3  H  N N 369 
PRO HXT  H  N N 370 
SER N    N  N N 371 
SER CA   C  N S 372 
SER C    C  N N 373 
SER O    O  N N 374 
SER CB   C  N N 375 
SER OG   O  N N 376 
SER OXT  O  N N 377 
SER H    H  N N 378 
SER H2   H  N N 379 
SER HA   H  N N 380 
SER HB2  H  N N 381 
SER HB3  H  N N 382 
SER HG   H  N N 383 
SER HXT  H  N N 384 
THR N    N  N N 385 
THR CA   C  N S 386 
THR C    C  N N 387 
THR O    O  N N 388 
THR CB   C  N R 389 
THR OG1  O  N N 390 
THR CG2  C  N N 391 
THR OXT  O  N N 392 
THR H    H  N N 393 
THR H2   H  N N 394 
THR HA   H  N N 395 
THR HB   H  N N 396 
THR HG1  H  N N 397 
THR HG21 H  N N 398 
THR HG22 H  N N 399 
THR HG23 H  N N 400 
THR HXT  H  N N 401 
TRP N    N  N N 402 
TRP CA   C  N S 403 
TRP C    C  N N 404 
TRP O    O  N N 405 
TRP CB   C  N N 406 
TRP CG   C  Y N 407 
TRP CD1  C  Y N 408 
TRP CD2  C  Y N 409 
TRP NE1  N  Y N 410 
TRP CE2  C  Y N 411 
TRP CE3  C  Y N 412 
TRP CZ2  C  Y N 413 
TRP CZ3  C  Y N 414 
TRP CH2  C  Y N 415 
TRP OXT  O  N N 416 
TRP H    H  N N 417 
TRP H2   H  N N 418 
TRP HA   H  N N 419 
TRP HB2  H  N N 420 
TRP HB3  H  N N 421 
TRP HD1  H  N N 422 
TRP HE1  H  N N 423 
TRP HE3  H  N N 424 
TRP HZ2  H  N N 425 
TRP HZ3  H  N N 426 
TRP HH2  H  N N 427 
TRP HXT  H  N N 428 
TYR N    N  N N 429 
TYR CA   C  N S 430 
TYR C    C  N N 431 
TYR O    O  N N 432 
TYR CB   C  N N 433 
TYR CG   C  Y N 434 
TYR CD1  C  Y N 435 
TYR CD2  C  Y N 436 
TYR CE1  C  Y N 437 
TYR CE2  C  Y N 438 
TYR CZ   C  Y N 439 
TYR OH   O  N N 440 
TYR OXT  O  N N 441 
TYR H    H  N N 442 
TYR H2   H  N N 443 
TYR HA   H  N N 444 
TYR HB2  H  N N 445 
TYR HB3  H  N N 446 
TYR HD1  H  N N 447 
TYR HD2  H  N N 448 
TYR HE1  H  N N 449 
TYR HE2  H  N N 450 
TYR HH   H  N N 451 
TYR HXT  H  N N 452 
VAL N    N  N N 453 
VAL CA   C  N S 454 
VAL C    C  N N 455 
VAL O    O  N N 456 
VAL CB   C  N N 457 
VAL CG1  C  N N 458 
VAL CG2  C  N N 459 
VAL OXT  O  N N 460 
VAL H    H  N N 461 
VAL H2   H  N N 462 
VAL HA   H  N N 463 
VAL HB   H  N N 464 
VAL HG11 H  N N 465 
VAL HG12 H  N N 466 
VAL HG13 H  N N 467 
VAL HG21 H  N N 468 
VAL HG22 H  N N 469 
VAL HG23 H  N N 470 
VAL HXT  H  N N 471 
# 
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 
1BO C1  C2   sing N N 1   
1BO C1  H11  sing N N 2   
1BO C1  H12  sing N N 3   
1BO C1  H13  sing N N 4   
1BO C2  C3   sing N N 5   
1BO C2  H21  sing N N 6   
1BO C2  H22  sing N N 7   
1BO C3  C4   sing N N 8   
1BO C3  H31  sing N N 9   
1BO C3  H32  sing N N 10  
1BO C4  OH   sing N N 11  
1BO C4  H41  sing N N 12  
1BO C4  H42  sing N N 13  
1BO OH  HO   sing N N 14  
ALA N   CA   sing N N 15  
ALA N   H    sing N N 16  
ALA N   H2   sing N N 17  
ALA CA  C    sing N N 18  
ALA CA  CB   sing N N 19  
ALA CA  HA   sing N N 20  
ALA C   O    doub N N 21  
ALA C   OXT  sing N N 22  
ALA CB  HB1  sing N N 23  
ALA CB  HB2  sing N N 24  
ALA CB  HB3  sing N N 25  
ALA OXT HXT  sing N N 26  
ARG N   CA   sing N N 27  
ARG N   H    sing N N 28  
ARG N   H2   sing N N 29  
ARG CA  C    sing N N 30  
ARG CA  CB   sing N N 31  
ARG CA  HA   sing N N 32  
ARG C   O    doub N N 33  
ARG C   OXT  sing N N 34  
ARG CB  CG   sing N N 35  
ARG CB  HB2  sing N N 36  
ARG CB  HB3  sing N N 37  
ARG CG  CD   sing N N 38  
ARG CG  HG2  sing N N 39  
ARG CG  HG3  sing N N 40  
ARG CD  NE   sing N N 41  
ARG CD  HD2  sing N N 42  
ARG CD  HD3  sing N N 43  
ARG NE  CZ   sing N N 44  
ARG NE  HE   sing N N 45  
ARG CZ  NH1  sing N N 46  
ARG CZ  NH2  doub N N 47  
ARG NH1 HH11 sing N N 48  
ARG NH1 HH12 sing N N 49  
ARG NH2 HH21 sing N N 50  
ARG NH2 HH22 sing N N 51  
ARG OXT HXT  sing N N 52  
ASN N   CA   sing N N 53  
ASN N   H    sing N N 54  
ASN N   H2   sing N N 55  
ASN CA  C    sing N N 56  
ASN CA  CB   sing N N 57  
ASN CA  HA   sing N N 58  
ASN C   O    doub N N 59  
ASN C   OXT  sing N N 60  
ASN CB  CG   sing N N 61  
ASN CB  HB2  sing N N 62  
ASN CB  HB3  sing N N 63  
ASN CG  OD1  doub N N 64  
ASN CG  ND2  sing N N 65  
ASN ND2 HD21 sing N N 66  
ASN ND2 HD22 sing N N 67  
ASN OXT HXT  sing N N 68  
ASP N   CA   sing N N 69  
ASP N   H    sing N N 70  
ASP N   H2   sing N N 71  
ASP CA  C    sing N N 72  
ASP CA  CB   sing N N 73  
ASP CA  HA   sing N N 74  
ASP C   O    doub N N 75  
ASP C   OXT  sing N N 76  
ASP CB  CG   sing N N 77  
ASP CB  HB2  sing N N 78  
ASP CB  HB3  sing N N 79  
ASP CG  OD1  doub N N 80  
ASP CG  OD2  sing N N 81  
ASP OD2 HD2  sing N N 82  
ASP OXT HXT  sing N N 83  
FMT C   O1   doub N N 84  
FMT C   O2   sing N N 85  
FMT C   H    sing N N 86  
FMT O2  HO2  sing N N 87  
GLN N   CA   sing N N 88  
GLN N   H    sing N N 89  
GLN N   H2   sing N N 90  
GLN CA  C    sing N N 91  
GLN CA  CB   sing N N 92  
GLN CA  HA   sing N N 93  
GLN C   O    doub N N 94  
GLN C   OXT  sing N N 95  
GLN CB  CG   sing N N 96  
GLN CB  HB2  sing N N 97  
GLN CB  HB3  sing N N 98  
GLN CG  CD   sing N N 99  
GLN CG  HG2  sing N N 100 
GLN CG  HG3  sing N N 101 
GLN CD  OE1  doub N N 102 
GLN CD  NE2  sing N N 103 
GLN NE2 HE21 sing N N 104 
GLN NE2 HE22 sing N N 105 
GLN OXT HXT  sing N N 106 
GLU N   CA   sing N N 107 
GLU N   H    sing N N 108 
GLU N   H2   sing N N 109 
GLU CA  C    sing N N 110 
GLU CA  CB   sing N N 111 
GLU CA  HA   sing N N 112 
GLU C   O    doub N N 113 
GLU C   OXT  sing N N 114 
GLU CB  CG   sing N N 115 
GLU CB  HB2  sing N N 116 
GLU CB  HB3  sing N N 117 
GLU CG  CD   sing N N 118 
GLU CG  HG2  sing N N 119 
GLU CG  HG3  sing N N 120 
GLU CD  OE1  doub N N 121 
GLU CD  OE2  sing N N 122 
GLU OE2 HE2  sing N N 123 
GLU OXT HXT  sing N N 124 
GLY N   CA   sing N N 125 
GLY N   H    sing N N 126 
GLY N   H2   sing N N 127 
GLY CA  C    sing N N 128 
GLY CA  HA2  sing N N 129 
GLY CA  HA3  sing N N 130 
GLY C   O    doub N N 131 
GLY C   OXT  sing N N 132 
GLY OXT HXT  sing N N 133 
HEM CHA C1A  sing N N 134 
HEM CHA C4D  doub N N 135 
HEM CHA HHA  sing N N 136 
HEM CHB C4A  sing N N 137 
HEM CHB C1B  doub N N 138 
HEM CHB HHB  sing N N 139 
HEM CHC C4B  sing N N 140 
HEM CHC C1C  doub N N 141 
HEM CHC HHC  sing N N 142 
HEM CHD C4C  doub N N 143 
HEM CHD C1D  sing N N 144 
HEM CHD HHD  sing N N 145 
HEM C1A C2A  doub Y N 146 
HEM C1A NA   sing Y N 147 
HEM C2A C3A  sing Y N 148 
HEM C2A CAA  sing N N 149 
HEM C3A C4A  doub Y N 150 
HEM C3A CMA  sing N N 151 
HEM C4A NA   sing Y N 152 
HEM CMA HMA  sing N N 153 
HEM CMA HMAA sing N N 154 
HEM CMA HMAB sing N N 155 
HEM CAA CBA  sing N N 156 
HEM CAA HAA  sing N N 157 
HEM CAA HAAA sing N N 158 
HEM CBA CGA  sing N N 159 
HEM CBA HBA  sing N N 160 
HEM CBA HBAA sing N N 161 
HEM CGA O1A  doub N N 162 
HEM CGA O2A  sing N N 163 
HEM C1B C2B  sing N N 164 
HEM C1B NB   sing N N 165 
HEM C2B C3B  doub N N 166 
HEM C2B CMB  sing N N 167 
HEM C3B C4B  sing N N 168 
HEM C3B CAB  sing N N 169 
HEM C4B NB   doub N N 170 
HEM CMB HMB  sing N N 171 
HEM CMB HMBA sing N N 172 
HEM CMB HMBB sing N N 173 
HEM CAB CBB  doub N N 174 
HEM CAB HAB  sing N N 175 
HEM CBB HBB  sing N N 176 
HEM CBB HBBA sing N N 177 
HEM C1C C2C  sing Y N 178 
HEM C1C NC   sing Y N 179 
HEM C2C C3C  doub Y N 180 
HEM C2C CMC  sing N N 181 
HEM C3C C4C  sing Y N 182 
HEM C3C CAC  sing N N 183 
HEM C4C NC   sing Y N 184 
HEM CMC HMC  sing N N 185 
HEM CMC HMCA sing N N 186 
HEM CMC HMCB sing N N 187 
HEM CAC CBC  doub N N 188 
HEM CAC HAC  sing N N 189 
HEM CBC HBC  sing N N 190 
HEM CBC HBCA sing N N 191 
HEM C1D C2D  sing N N 192 
HEM C1D ND   doub N N 193 
HEM C2D C3D  doub N N 194 
HEM C2D CMD  sing N N 195 
HEM C3D C4D  sing N N 196 
HEM C3D CAD  sing N N 197 
HEM C4D ND   sing N N 198 
HEM CMD HMD  sing N N 199 
HEM CMD HMDA sing N N 200 
HEM CMD HMDB sing N N 201 
HEM CAD CBD  sing N N 202 
HEM CAD HAD  sing N N 203 
HEM CAD HADA sing N N 204 
HEM CBD CGD  sing N N 205 
HEM CBD HBD  sing N N 206 
HEM CBD HBDA sing N N 207 
HEM CGD O1D  doub N N 208 
HEM CGD O2D  sing N N 209 
HEM O2A H2A  sing N N 210 
HEM O2D H2D  sing N N 211 
HEM FE  NA   sing N N 212 
HEM FE  NB   sing N N 213 
HEM FE  NC   sing N N 214 
HEM FE  ND   sing N N 215 
HIS N   CA   sing N N 216 
HIS N   H    sing N N 217 
HIS N   H2   sing N N 218 
HIS CA  C    sing N N 219 
HIS CA  CB   sing N N 220 
HIS CA  HA   sing N N 221 
HIS C   O    doub N N 222 
HIS C   OXT  sing N N 223 
HIS CB  CG   sing N N 224 
HIS CB  HB2  sing N N 225 
HIS CB  HB3  sing N N 226 
HIS CG  ND1  sing Y N 227 
HIS CG  CD2  doub Y N 228 
HIS ND1 CE1  doub Y N 229 
HIS ND1 HD1  sing N N 230 
HIS CD2 NE2  sing Y N 231 
HIS CD2 HD2  sing N N 232 
HIS CE1 NE2  sing Y N 233 
HIS CE1 HE1  sing N N 234 
HIS NE2 HE2  sing N N 235 
HIS OXT HXT  sing N N 236 
HOH O   H1   sing N N 237 
HOH O   H2   sing N N 238 
ILE N   CA   sing N N 239 
ILE N   H    sing N N 240 
ILE N   H2   sing N N 241 
ILE CA  C    sing N N 242 
ILE CA  CB   sing N N 243 
ILE CA  HA   sing N N 244 
ILE C   O    doub N N 245 
ILE C   OXT  sing N N 246 
ILE CB  CG1  sing N N 247 
ILE CB  CG2  sing N N 248 
ILE CB  HB   sing N N 249 
ILE CG1 CD1  sing N N 250 
ILE CG1 HG12 sing N N 251 
ILE CG1 HG13 sing N N 252 
ILE CG2 HG21 sing N N 253 
ILE CG2 HG22 sing N N 254 
ILE CG2 HG23 sing N N 255 
ILE CD1 HD11 sing N N 256 
ILE CD1 HD12 sing N N 257 
ILE CD1 HD13 sing N N 258 
ILE OXT HXT  sing N N 259 
LEU N   CA   sing N N 260 
LEU N   H    sing N N 261 
LEU N   H2   sing N N 262 
LEU CA  C    sing N N 263 
LEU CA  CB   sing N N 264 
LEU CA  HA   sing N N 265 
LEU C   O    doub N N 266 
LEU C   OXT  sing N N 267 
LEU CB  CG   sing N N 268 
LEU CB  HB2  sing N N 269 
LEU CB  HB3  sing N N 270 
LEU CG  CD1  sing N N 271 
LEU CG  CD2  sing N N 272 
LEU CG  HG   sing N N 273 
LEU CD1 HD11 sing N N 274 
LEU CD1 HD12 sing N N 275 
LEU CD1 HD13 sing N N 276 
LEU CD2 HD21 sing N N 277 
LEU CD2 HD22 sing N N 278 
LEU CD2 HD23 sing N N 279 
LEU OXT HXT  sing N N 280 
LYS N   CA   sing N N 281 
LYS N   H    sing N N 282 
LYS N   H2   sing N N 283 
LYS CA  C    sing N N 284 
LYS CA  CB   sing N N 285 
LYS CA  HA   sing N N 286 
LYS C   O    doub N N 287 
LYS C   OXT  sing N N 288 
LYS CB  CG   sing N N 289 
LYS CB  HB2  sing N N 290 
LYS CB  HB3  sing N N 291 
LYS CG  CD   sing N N 292 
LYS CG  HG2  sing N N 293 
LYS CG  HG3  sing N N 294 
LYS CD  CE   sing N N 295 
LYS CD  HD2  sing N N 296 
LYS CD  HD3  sing N N 297 
LYS CE  NZ   sing N N 298 
LYS CE  HE2  sing N N 299 
LYS CE  HE3  sing N N 300 
LYS NZ  HZ1  sing N N 301 
LYS NZ  HZ2  sing N N 302 
LYS NZ  HZ3  sing N N 303 
LYS OXT HXT  sing N N 304 
MET N   CA   sing N N 305 
MET N   H    sing N N 306 
MET N   H2   sing N N 307 
MET CA  C    sing N N 308 
MET CA  CB   sing N N 309 
MET CA  HA   sing N N 310 
MET C   O    doub N N 311 
MET C   OXT  sing N N 312 
MET CB  CG   sing N N 313 
MET CB  HB2  sing N N 314 
MET CB  HB3  sing N N 315 
MET CG  SD   sing N N 316 
MET CG  HG2  sing N N 317 
MET CG  HG3  sing N N 318 
MET SD  CE   sing N N 319 
MET CE  HE1  sing N N 320 
MET CE  HE2  sing N N 321 
MET CE  HE3  sing N N 322 
MET OXT HXT  sing N N 323 
PHE N   CA   sing N N 324 
PHE N   H    sing N N 325 
PHE N   H2   sing N N 326 
PHE CA  C    sing N N 327 
PHE CA  CB   sing N N 328 
PHE CA  HA   sing N N 329 
PHE C   O    doub N N 330 
PHE C   OXT  sing N N 331 
PHE CB  CG   sing N N 332 
PHE CB  HB2  sing N N 333 
PHE CB  HB3  sing N N 334 
PHE CG  CD1  doub Y N 335 
PHE CG  CD2  sing Y N 336 
PHE CD1 CE1  sing Y N 337 
PHE CD1 HD1  sing N N 338 
PHE CD2 CE2  doub Y N 339 
PHE CD2 HD2  sing N N 340 
PHE CE1 CZ   doub Y N 341 
PHE CE1 HE1  sing N N 342 
PHE CE2 CZ   sing Y N 343 
PHE CE2 HE2  sing N N 344 
PHE CZ  HZ   sing N N 345 
PHE OXT HXT  sing N N 346 
PRO N   CA   sing N N 347 
PRO N   CD   sing N N 348 
PRO N   H    sing N N 349 
PRO CA  C    sing N N 350 
PRO CA  CB   sing N N 351 
PRO CA  HA   sing N N 352 
PRO C   O    doub N N 353 
PRO C   OXT  sing N N 354 
PRO CB  CG   sing N N 355 
PRO CB  HB2  sing N N 356 
PRO CB  HB3  sing N N 357 
PRO CG  CD   sing N N 358 
PRO CG  HG2  sing N N 359 
PRO CG  HG3  sing N N 360 
PRO CD  HD2  sing N N 361 
PRO CD  HD3  sing N N 362 
PRO OXT HXT  sing N N 363 
SER N   CA   sing N N 364 
SER N   H    sing N N 365 
SER N   H2   sing N N 366 
SER CA  C    sing N N 367 
SER CA  CB   sing N N 368 
SER CA  HA   sing N N 369 
SER C   O    doub N N 370 
SER C   OXT  sing N N 371 
SER CB  OG   sing N N 372 
SER CB  HB2  sing N N 373 
SER CB  HB3  sing N N 374 
SER OG  HG   sing N N 375 
SER OXT HXT  sing N N 376 
THR N   CA   sing N N 377 
THR N   H    sing N N 378 
THR N   H2   sing N N 379 
THR CA  C    sing N N 380 
THR CA  CB   sing N N 381 
THR CA  HA   sing N N 382 
THR C   O    doub N N 383 
THR C   OXT  sing N N 384 
THR CB  OG1  sing N N 385 
THR CB  CG2  sing N N 386 
THR CB  HB   sing N N 387 
THR OG1 HG1  sing N N 388 
THR CG2 HG21 sing N N 389 
THR CG2 HG22 sing N N 390 
THR CG2 HG23 sing N N 391 
THR OXT HXT  sing N N 392 
TRP N   CA   sing N N 393 
TRP N   H    sing N N 394 
TRP N   H2   sing N N 395 
TRP CA  C    sing N N 396 
TRP CA  CB   sing N N 397 
TRP CA  HA   sing N N 398 
TRP C   O    doub N N 399 
TRP C   OXT  sing N N 400 
TRP CB  CG   sing N N 401 
TRP CB  HB2  sing N N 402 
TRP CB  HB3  sing N N 403 
TRP CG  CD1  doub Y N 404 
TRP CG  CD2  sing Y N 405 
TRP CD1 NE1  sing Y N 406 
TRP CD1 HD1  sing N N 407 
TRP CD2 CE2  doub Y N 408 
TRP CD2 CE3  sing Y N 409 
TRP NE1 CE2  sing Y N 410 
TRP NE1 HE1  sing N N 411 
TRP CE2 CZ2  sing Y N 412 
TRP CE3 CZ3  doub Y N 413 
TRP CE3 HE3  sing N N 414 
TRP CZ2 CH2  doub Y N 415 
TRP CZ2 HZ2  sing N N 416 
TRP CZ3 CH2  sing Y N 417 
TRP CZ3 HZ3  sing N N 418 
TRP CH2 HH2  sing N N 419 
TRP OXT HXT  sing N N 420 
TYR N   CA   sing N N 421 
TYR N   H    sing N N 422 
TYR N   H2   sing N N 423 
TYR CA  C    sing N N 424 
TYR CA  CB   sing N N 425 
TYR CA  HA   sing N N 426 
TYR C   O    doub N N 427 
TYR C   OXT  sing N N 428 
TYR CB  CG   sing N N 429 
TYR CB  HB2  sing N N 430 
TYR CB  HB3  sing N N 431 
TYR CG  CD1  doub Y N 432 
TYR CG  CD2  sing Y N 433 
TYR CD1 CE1  sing Y N 434 
TYR CD1 HD1  sing N N 435 
TYR CD2 CE2  doub Y N 436 
TYR CD2 HD2  sing N N 437 
TYR CE1 CZ   doub Y N 438 
TYR CE1 HE1  sing N N 439 
TYR CE2 CZ   sing Y N 440 
TYR CE2 HE2  sing N N 441 
TYR CZ  OH   sing N N 442 
TYR OH  HH   sing N N 443 
TYR OXT HXT  sing N N 444 
VAL N   CA   sing N N 445 
VAL N   H    sing N N 446 
VAL N   H2   sing N N 447 
VAL CA  C    sing N N 448 
VAL CA  CB   sing N N 449 
VAL CA  HA   sing N N 450 
VAL C   O    doub N N 451 
VAL C   OXT  sing N N 452 
VAL CB  CG1  sing N N 453 
VAL CB  CG2  sing N N 454 
VAL CB  HB   sing N N 455 
VAL CG1 HG11 sing N N 456 
VAL CG1 HG12 sing N N 457 
VAL CG1 HG13 sing N N 458 
VAL CG2 HG21 sing N N 459 
VAL CG2 HG22 sing N N 460 
VAL CG2 HG23 sing N N 461 
VAL OXT HXT  sing N N 462 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/John E. Fogarty International Center (NIH/FIC)' 'United States' R35-GM147557 1 
'National Science Foundation (NSF, United States)'                             'United States' 1937971      2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9CJG 
_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]   0.018822 
_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]   0.016764 
_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]   0.004277 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
FE  ? ? 20.90327 4.99816 ? ? 2.55100  38.46870 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366  3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . LEU A 1 24  ? -16.81000 11.97500  -6.41000  1.000 43.92168 ?  4   LEU A N   1 
ATOM   2    C  CA  . LEU A 1 24  ? -16.84900 10.52400  -6.28000  1.000 48.39342 ?  4   LEU A CA  1 
ATOM   3    C  C   . LEU A 1 24  ? -15.65300 9.88500   -6.97400  1.000 44.17222 ?  4   LEU A C   1 
ATOM   4    O  O   . LEU A 1 24  ? -14.59000 9.72300   -6.37800  1.000 44.76366 ?  4   LEU A O   1 
ATOM   5    C  CB  . LEU A 1 24  ? -18.15200 9.96900   -6.85500  1.000 42.63072 ?  4   LEU A CB  1 
ATOM   6    N  N   . PHE A 1 25  ? -15.82600 9.52400   -8.24300  1.000 42.97593 ?  5   PHE A N   1 
ATOM   7    C  CA  . PHE A 1 25  ? -14.76000 8.91200   -9.02400  1.000 46.32508 ?  5   PHE A CA  1 
ATOM   8    C  C   . PHE A 1 25  ? -14.23200 9.86100   -10.09800 1.000 50.33090 ?  5   PHE A C   1 
ATOM   9    O  O   . PHE A 1 25  ? -13.77700 9.42600   -11.16000 1.000 44.26850 ?  5   PHE A O   1 
ATOM   10   C  CB  . PHE A 1 25  ? -15.24200 7.59400   -9.62900  1.000 43.83705 ?  5   PHE A CB  1 
ATOM   11   C  CG  . PHE A 1 25  ? -15.32500 6.47100   -8.62600  1.000 42.40550 ?  5   PHE A CG  1 
ATOM   12   C  CD1 . PHE A 1 25  ? -14.24000 6.16600   -7.81700  1.000 39.78598 ?  5   PHE A CD1 1 
ATOM   13   C  CD2 . PHE A 1 25  ? -16.49400 5.74300   -8.46800  1.000 41.23924 ?  5   PHE A CD2 1 
ATOM   14   C  CE1 . PHE A 1 25  ? -14.31300 5.14100   -6.88300  1.000 32.89728 ?  5   PHE A CE1 1 
ATOM   15   C  CE2 . PHE A 1 25  ? -16.57300 4.71700   -7.53400  1.000 37.90178 ?  5   PHE A CE2 1 
ATOM   16   C  CZ  . PHE A 1 25  ? -15.48300 4.41800   -6.74300  1.000 33.62726 ?  5   PHE A CZ  1 
ATOM   17   N  N   . GLY A 1 26  ? -14.27300 11.16500  -9.81900  1.000 43.42753 ?  6   GLY A N   1 
ATOM   18   C  CA  . GLY A 1 26  ? -13.81200 12.17500  -10.75100 1.000 42.92051 ?  6   GLY A CA  1 
ATOM   19   C  C   . GLY A 1 26  ? -12.48400 12.79800  -10.37400 1.000 38.54586 ?  6   GLY A C   1 
ATOM   20   O  O   . GLY A 1 26  ? -11.53300 12.08300  -10.04900 1.000 38.28146 ?  6   GLY A O   1 
ATOM   21   N  N   . ARG A 1 27  ? -12.41900 14.13400  -10.39600 1.000 41.52142 ?  7   ARG A N   1 
ATOM   22   C  CA  . ARG A 1 27  ? -11.14500 14.83300  -10.23600 1.000 36.81711 ?  7   ARG A CA  1 
ATOM   23   C  C   . ARG A 1 27  ? -10.47800 14.48800  -8.91000  1.000 35.21683 ?  7   ARG A C   1 
ATOM   24   O  O   . ARG A 1 27  ? -9.28500  14.16600  -8.86900  1.000 34.52545 ?  7   ARG A O   1 
ATOM   25   C  CB  . ARG A 1 27  ? -11.35800 16.34400  -10.35500 1.000 36.40051 ?  7   ARG A CB  1 
ATOM   26   N  N   . ALA A 1 28  ? -11.23100 14.55800  -7.81000  1.000 33.79317 ?  8   ALA A N   1 
ATOM   27   C  CA  . ALA A 1 28  ? -10.66300 14.21500  -6.51000  1.000 33.99981 ?  8   ALA A CA  1 
ATOM   28   C  C   . ALA A 1 28  ? -10.11800 12.79200  -6.50600  1.000 33.49815 ?  8   ALA A C   1 
ATOM   29   O  O   . ALA A 1 28  ? -9.04100  12.53300  -5.95700  1.000 31.80192 ?  8   ALA A O   1 
ATOM   30   C  CB  . ALA A 1 28  ? -11.71200 14.39000  -5.41400  1.000 29.86661 ?  8   ALA A CB  1 
ATOM   31   N  N   . PHE A 1 29  ? -10.84700 11.86100  -7.12900  1.000 30.02306 ?  9   PHE A N   1 
ATOM   32   C  CA  . PHE A 1 29  ? -10.40700 10.47000  -7.18700  1.000 33.49291 ?  9   PHE A CA  1 
ATOM   33   C  C   . PHE A 1 29  ? -9.11500  10.32400  -7.97900  1.000 27.45818 ?  9   PHE A C   1 
ATOM   34   O  O   . PHE A 1 29  ? -8.26200  9.49500   -7.64100  1.000 26.03595 ?  9   PHE A O   1 
ATOM   35   C  CB  . PHE A 1 29  ? -11.50800 9.61000   -7.80500  1.000 32.31995 ?  9   PHE A CB  1 
ATOM   36   C  CG  . PHE A 1 29  ? -11.15500 8.15200   -7.93200  1.000 25.98773 ?  9   PHE A CG  1 
ATOM   37   C  CD1 . PHE A 1 29  ? -11.17700 7.31700   -6.82700  1.000 26.58279 ?  9   PHE A CD1 1 
ATOM   38   C  CD2 . PHE A 1 29  ? -10.81000 7.61600   -9.16200  1.000 28.79547 ?  9   PHE A CD2 1 
ATOM   39   C  CE1 . PHE A 1 29  ? -10.86200 5.97100   -6.95000  1.000 19.93924 ?  9   PHE A CE1 1 
ATOM   40   C  CE2 . PHE A 1 29  ? -10.48800 6.27700   -9.28600  1.000 24.87577 ?  9   PHE A CE2 1 
ATOM   41   C  CZ  . PHE A 1 29  ? -10.51700 5.45500   -8.17700  1.000 20.44410 ?  9   PHE A CZ  1 
ATOM   42   N  N   . HIS A 1 30  ? -8.95400  11.11200  -9.04400  1.000 28.77973 ?  10  HIS A N   1 
ATOM   43   C  CA  . HIS A 1 30  ? -7.76300  10.98100  -9.87700  1.000 30.53868 ?  10  HIS A CA  1 
ATOM   44   C  C   . HIS A 1 30  ? -6.54300  11.59000  -9.19800  1.000 34.08554 ?  10  HIS A C   1 
ATOM   45   O  O   . HIS A 1 30  ? -5.43100  11.06100  -9.31500  1.000 30.41427 ?  10  HIS A O   1 
ATOM   46   C  CB  . HIS A 1 30  ? -8.00600  11.62900  -11.23900 1.000 44.90914 ?  10  HIS A CB  1 
ATOM   47   C  CG  . HIS A 1 30  ? -8.94700  10.85700  -12.11100 1.000 42.16889 ?  10  HIS A CG  1 
ATOM   48   N  ND1 . HIS A 1 30  ? -10.04700 11.43200  -12.70900 1.000 44.14012 ?  10  HIS A ND1 1 
ATOM   49   C  CD2 . HIS A 1 30  ? -8.95600  9.55400   -12.48100 1.000 45.79692 ?  10  HIS A CD2 1 
ATOM   50   C  CE1 . HIS A 1 30  ? -10.69300 10.51800  -13.41100 1.000 45.71103 ?  10  HIS A CE1 1 
ATOM   51   N  NE2 . HIS A 1 30  ? -10.05200 9.37000   -13.28900 1.000 40.76523 ?  10  HIS A NE2 1 
ATOM   52   N  N   . VAL A 1 31  ? -6.73100  12.69500  -8.47400  1.000 28.55425 ?  11  VAL A N   1 
ATOM   53   C  CA  . VAL A 1 31  ? -5.61500  13.31500  -7.76600  1.000 29.30115 ?  11  VAL A CA  1 
ATOM   54   C  C   . VAL A 1 31  ? -5.22600  12.48200  -6.55100  1.000 32.66360 ?  11  VAL A C   1 
ATOM   55   O  O   . VAL A 1 31  ? -4.04300  12.21900  -6.31200  1.000 28.78658 ?  11  VAL A O   1 
ATOM   56   C  CB  . VAL A 1 31  ? -5.97000  14.75900  -7.37200  1.000 34.12461 ?  11  VAL A CB  1 
ATOM   57   C  CG1 . VAL A 1 31  ? -4.84300  15.37800  -6.55900  1.000 32.52260 ?  11  VAL A CG1 1 
ATOM   58   C  CG2 . VAL A 1 31  ? -6.26400  15.58600  -8.61700  1.000 29.94014 ?  11  VAL A CG2 1 
ATOM   59   N  N   . ASP A 1 32  ? -6.21500  12.05700  -5.76100  1.000 28.54674 ?  12  ASP A N   1 
ATOM   60   C  CA  . ASP A 1 32  ? -5.95000  11.19100  -4.61700  1.000 25.19753 ?  12  ASP A CA  1 
ATOM   61   C  C   . ASP A 1 32  ? -7.19500  10.37400  -4.29000  1.000 26.89635 ?  12  ASP A C   1 
ATOM   62   O  O   . ASP A 1 32  ? -8.19000  10.91700  -3.79400  1.000 23.74600 ?  12  ASP A O   1 
ATOM   63   C  CB  . ASP A 1 32  ? -5.49300  12.00900  -3.40600  1.000 26.53785 ?  12  ASP A CB  1 
ATOM   64   C  CG  . ASP A 1 32  ? -5.22300  11.14700  -2.18400  1.000 25.39555 ?  12  ASP A CG  1 
ATOM   65   O  OD1 . ASP A 1 32  ? -5.01700  9.92400   -2.34100  1.000 29.79772 ?  12  ASP A OD1 1 
ATOM   66   O  OD2 . ASP A 1 32  ? -5.19300  11.69600  -1.06200  1.000 33.21730 -1 12  ASP A OD2 1 
ATOM   67   N  N   . PRO A 1 33  ? -7.16800  9.06300   -4.54000  1.000 27.50136 ?  13  PRO A N   1 
ATOM   68   C  CA  . PRO A 1 33  ? -8.37400  8.25000   -4.34100  1.000 20.05039 ?  13  PRO A CA  1 
ATOM   69   C  C   . PRO A 1 33  ? -8.59400  7.79600   -2.90800  1.000 23.91726 ?  13  PRO A C   1 
ATOM   70   O  O   . PRO A 1 33  ? -9.70800  7.36500   -2.57900  1.000 18.13299 ?  13  PRO A O   1 
ATOM   71   C  CB  . PRO A 1 33  ? -8.12100  7.05200   -5.26200  1.000 16.82680 ?  13  PRO A CB  1 
ATOM   72   C  CG  . PRO A 1 33  ? -6.62500  6.85300   -5.13400  1.000 19.65288 ?  13  PRO A CG  1 
ATOM   73   C  CD  . PRO A 1 33  ? -6.04100  8.25500   -5.04100  1.000 18.57156 ?  13  PRO A CD  1 
ATOM   74   N  N   . TYR A 1 34  ? -7.58900  7.87900   -2.05000  1.000 19.03596 ?  14  TYR A N   1 
ATOM   75   C  CA  . TYR A 1 34  ? -7.68500  7.28300   -0.72500  1.000 20.57440 ?  14  TYR A CA  1 
ATOM   76   C  C   . TYR A 1 34  ? -8.68700  7.95100   0.22000   1.000 20.04093 ?  14  TYR A C   1 
ATOM   77   O  O   . TYR A 1 34  ? -9.24600  7.25200   1.07400   1.000 20.20823 ?  14  TYR A O   1 
ATOM   78   C  CB  . TYR A 1 34  ? -6.27700  7.21800   -0.12900  1.000 24.79212 ?  14  TYR A CB  1 
ATOM   79   C  CG  . TYR A 1 34  ? -5.43100  6.26600   -0.94600  1.000 19.60375 ?  14  TYR A CG  1 
ATOM   80   C  CD1 . TYR A 1 34  ? -5.73100  4.91200   -0.96000  1.000 19.86420 ?  14  TYR A CD1 1 
ATOM   81   C  CD2 . TYR A 1 34  ? -4.41300  6.72000   -1.77200  1.000 21.73877 ?  14  TYR A CD2 1 
ATOM   82   C  CE1 . TYR A 1 34  ? -5.01200  4.02700   -1.72100  1.000 19.64563 ?  14  TYR A CE1 1 
ATOM   83   C  CE2 . TYR A 1 34  ? -3.67700  5.83100   -2.54600  1.000 19.74438 ?  14  TYR A CE2 1 
ATOM   84   C  CZ  . TYR A 1 34  ? -3.98800  4.48100   -2.51100  1.000 20.84116 ?  14  TYR A CZ  1 
ATOM   85   O  OH  . TYR A 1 34  ? -3.28600  3.56200   -3.26100  1.000 19.32819 ?  14  TYR A OH  1 
ATOM   86   N  N   . PRO A 1 35  ? -8.96700  9.25800   0.12300   1.000 22.57814 ?  15  PRO A N   1 
ATOM   87   C  CA  . PRO A 1 35  ? -10.08400 9.79500   0.92000   1.000 23.99990 ?  15  PRO A CA  1 
ATOM   88   C  C   . PRO A 1 35  ? -11.43500 9.24000   0.49700   1.000 21.39708 ?  15  PRO A C   1 
ATOM   89   O  O   . PRO A 1 35  ? -12.31300 9.05800   1.34800   1.000 22.99415 ?  15  PRO A O   1 
ATOM   90   C  CB  . PRO A 1 35  ? -9.99700  11.30800  0.68100   1.000 27.66009 ?  15  PRO A CB  1 
ATOM   91   C  CG  . PRO A 1 35  ? -8.58500  11.54200  0.30200   1.000 27.41533 ?  15  PRO A CG  1 
ATOM   92   C  CD  . PRO A 1 35  ? -8.21800  10.34800  -0.53000  1.000 24.70781 ?  15  PRO A CD  1 
ATOM   93   N  N   . ILE A 1 36  ? -11.62200 8.95800   -0.79400  1.000 21.10208 ?  16  ILE A N   1 
ATOM   94   C  CA  . ILE A 1 36  ? -12.86700 8.35100   -1.25300  1.000 19.92177 ?  16  ILE A CA  1 
ATOM   95   C  C   . ILE A 1 36  ? -12.96200 6.90800   -0.78000  1.000 20.87617 ?  16  ILE A C   1 
ATOM   96   O  O   . ILE A 1 36  ? -14.01700 6.46700   -0.31400  1.000 19.73082 ?  16  ILE A O   1 
ATOM   97   C  CB  . ILE A 1 36  ? -12.96900 8.46100   -2.78400  1.000 26.38566 ?  16  ILE A CB  1 
ATOM   98   C  CG1 . ILE A 1 36  ? -12.87000 9.92800   -3.19300  1.000 30.58807 ?  16  ILE A CG1 1 
ATOM   99   C  CG2 . ILE A 1 36  ? -14.27600 7.85300   -3.28400  1.000 28.40594 ?  16  ILE A CG2 1 
ATOM   100  C  CD1 . ILE A 1 36  ? -13.92900 10.79000  -2.59400  1.000 39.50591 ?  16  ILE A CD1 1 
ATOM   101  N  N   . TYR A 1 37  ? -11.86300 6.14900   -0.89100  1.000 16.36491 ?  17  TYR A N   1 
ATOM   102  C  CA  . TYR A 1 37  ? -11.85100 4.79900   -0.33400  1.000 15.24152 ?  17  TYR A CA  1 
ATOM   103  C  C   . TYR A 1 37  ? -12.18600 4.80900   1.15400   1.000 16.58837 ?  17  TYR A C   1 
ATOM   104  O  O   . TYR A 1 37  ? -12.90700 3.92900   1.64000   1.000 16.89521 ?  17  TYR A O   1 
ATOM   105  C  CB  . TYR A 1 37  ? -10.49000 4.13100   -0.56100  1.000 13.57714 ?  17  TYR A CB  1 
ATOM   106  C  CG  . TYR A 1 37  ? -10.11100 3.90500   -2.00800  1.000 14.78977 ?  17  TYR A CG  1 
ATOM   107  C  CD1 . TYR A 1 37  ? -11.07000 3.58700   -2.96000  1.000 15.91366 ?  17  TYR A CD1 1 
ATOM   108  C  CD2 . TYR A 1 37  ? -8.78400  3.97400   -2.41600  1.000 14.02954 ?  17  TYR A CD2 1 
ATOM   109  C  CE1 . TYR A 1 37  ? -10.72100 3.36700   -4.28400  1.000 16.90852 ?  17  TYR A CE1 1 
ATOM   110  C  CE2 . TYR A 1 37  ? -8.42700  3.75800   -3.72900  1.000 14.41947 ?  17  TYR A CE2 1 
ATOM   111  C  CZ  . TYR A 1 37  ? -9.39200  3.45700   -4.66300  1.000 14.90485 ?  17  TYR A CZ  1 
ATOM   112  O  OH  . TYR A 1 37  ? -9.03200  3.23900   -5.97800  1.000 16.47602 ?  17  TYR A OH  1 
ATOM   113  N  N   . ALA A 1 38  ? -11.66700 5.79000   1.89600   1.000 17.09924 ?  18  ALA A N   1 
ATOM   114  C  CA  . ALA A 1 38  ? -11.96700 5.86000   3.32400   1.000 18.33895 ?  18  ALA A CA  1 
ATOM   115  C  C   . ALA A 1 38  ? -13.46200 6.04100   3.56800   1.000 16.81157 ?  18  ALA A C   1 
ATOM   116  O  O   . ALA A 1 38  ? -14.02500 5.42800   4.48200   1.000 18.58473 ?  18  ALA A O   1 
ATOM   117  C  CB  . ALA A 1 38  ? -11.17200 6.98900   3.97600   1.000 20.19211 ?  18  ALA A CB  1 
ATOM   118  N  N   . ARG A 1 39  ? -14.12200 6.87100   2.75400   1.000 19.02979 ?  19  ARG A N   1 
ATOM   119  C  CA  . ARG A 1 39  ? -15.57300 7.03300   2.87600   1.000 17.77720 ?  19  ARG A CA  1 
ATOM   120  C  C   . ARG A 1 39  ? -16.30100 5.73500   2.56000   1.000 22.16200 ?  19  ARG A C   1 
ATOM   121  O  O   . ARG A 1 39  ? -17.30800 5.40100   3.20100   1.000 20.14714 ?  19  ARG A O   1 
ATOM   122  C  CB  . ARG A 1 39  ? -16.06800 8.13100   1.93600   1.000 23.24011 ?  19  ARG A CB  1 
ATOM   123  C  CG  . ARG A 1 39  ? -15.52800 9.53000   2.17900   1.000 30.13016 ?  19  ARG A CG  1 
ATOM   124  C  CD  . ARG A 1 39  ? -15.92200 10.37800  0.99100   1.000 35.13456 ?  19  ARG A CD  1 
ATOM   125  N  NE  . ARG A 1 39  ? -16.78200 11.48800  1.37500   1.000 43.57390 ?  19  ARG A NE  1 
ATOM   126  C  CZ  . ARG A 1 39  ? -17.93900 11.75900  0.78700   1.000 43.32551 ?  19  ARG A CZ  1 
ATOM   127  N  NH1 . ARG A 1 39  ? -18.45900 10.94800  -0.11400  1.000 55.47996 ?  19  ARG A NH1 1 
ATOM   128  N  NH2 . ARG A 1 39  ? -18.60500 12.85500  1.13200   1.000 45.66911 ?  19  ARG A NH2 1 
ATOM   129  N  N   . LEU A 1 40  ? -15.82800 5.00900   1.54800   1.000 15.68446 ?  20  LEU A N   1 
ATOM   130  C  CA  . LEU A 1 40  ? -16.47000 3.75800   1.16300   1.000 18.29575 ?  20  LEU A CA  1 
ATOM   131  C  C   . LEU A 1 40  ? -16.32200 2.70300   2.25300   1.000 21.43137 ?  20  LEU A C   1 
ATOM   132  O  O   . LEU A 1 40  ? -17.27300 1.97100   2.54600   1.000 16.49355 ?  20  LEU A O   1 
ATOM   133  C  CB  . LEU A 1 40  ? -15.88500 3.26300   -0.15800  1.000 13.59386 ?  20  LEU A CB  1 
ATOM   134  C  CG  . LEU A 1 40  ? -16.24000 4.06500   -1.40800  1.000 15.82020 ?  20  LEU A CG  1 
ATOM   135  C  CD1 . LEU A 1 40  ? -15.50000 3.52700   -2.62900  1.000 16.43869 ?  20  LEU A CD1 1 
ATOM   136  C  CD2 . LEU A 1 40  ? -17.75300 4.06400   -1.64500  1.000 15.41059 ?  20  LEU A CD2 1 
ATOM   137  N  N   . ARG A 1 41  ? -15.13500 2.59700   2.86000   1.000 13.75352 ?  21  ARG A N   1 
ATOM   138  C  CA  . ARG A 1 41  ? -14.98600 1.67100   3.97900   1.000 16.73093 ?  21  ARG A CA  1 
ATOM   139  C  C   . ARG A 1 41  ? -15.82400 2.11400   5.17400   1.000 15.36487 ?  21  ARG A C   1 
ATOM   140  O  O   . ARG A 1 41  ? -16.41800 1.27800   5.86300   1.000 19.52951 ?  21  ARG A O   1 
ATOM   141  C  CB  . ARG A 1 41  ? -13.51700 1.53400   4.38200   1.000 13.29383 ?  21  ARG A CB  1 
ATOM   142  C  CG  . ARG A 1 41  ? -12.60100 1.03500   3.27400   1.000 12.05381 ?  21  ARG A CG  1 
ATOM   143  C  CD  . ARG A 1 41  ? -11.20800 0.74000   3.81000   1.000 13.29586 ?  21  ARG A CD  1 
ATOM   144  N  NE  . ARG A 1 41  ? -10.64900 1.89000   4.51700   1.000 18.86603 ?  21  ARG A NE  1 
ATOM   145  C  CZ  . ARG A 1 41  ? -9.89200  2.81900   3.94700   1.000 17.99494 ?  21  ARG A CZ  1 
ATOM   146  N  NH1 . ARG A 1 41  ? -9.58100  2.76400   2.66400   1.000 14.02463 ?  21  ARG A NH1 1 
ATOM   147  N  NH2 . ARG A 1 41  ? -9.44900  3.83800   4.68000   1.000 19.37607 ?  21  ARG A NH2 1 
ATOM   148  N  N   . ALA A 1 42  ? -15.88700 3.42400   5.42900   1.000 18.64231 ?  22  ALA A N   1 
ATOM   149  C  CA  . ALA A 1 42  ? -16.68800 3.92900   6.54100   1.000 25.37114 ?  22  ALA A CA  1 
ATOM   150  C  C   . ALA A 1 42  ? -18.17300 3.67100   6.32600   1.000 21.84494 ?  22  ALA A C   1 
ATOM   151  O  O   . ALA A 1 42  ? -18.92800 3.55200   7.29700   1.000 22.08973 ?  22  ALA A O   1 
ATOM   152  C  CB  . ALA A 1 42  ? -16.44300 5.42400   6.74000   1.000 22.56869 ?  22  ALA A CB  1 
ATOM   153  N  N   . GLY A 1 43  ? -18.60700 3.58900   5.07000   1.000 22.09846 ?  23  GLY A N   1 
ATOM   154  C  CA  . GLY A 1 43  ? -19.98300 3.30000   4.73400   1.000 25.71026 ?  23  GLY A CA  1 
ATOM   155  C  C   . GLY A 1 43  ? -20.35000 1.83700   4.75600   1.000 26.43907 ?  23  GLY A C   1 
ATOM   156  O  O   . GLY A 1 43  ? -21.45300 1.48200   4.33300   1.000 26.05295 ?  23  GLY A O   1 
ATOM   157  N  N   . GLY A 1 44  ? -19.46100 0.96700   5.23600   1.000 24.12904 ?  24  GLY A N   1 
ATOM   158  C  CA  . GLY A 1 44  ? -19.72600 -0.45500  5.30000   1.000 20.65791 ?  24  GLY A CA  1 
ATOM   159  C  C   . GLY A 1 44  ? -18.85600 -1.30700  4.40800   1.000 19.45452 ?  24  GLY A C   1 
ATOM   160  O  O   . GLY A 1 44  ? -18.82000 -2.52700  4.59600   1.000 16.37009 ?  24  GLY A O   1 
ATOM   161  N  N   . GLY A 1 45  ? -18.16300 -0.72000  3.43900   1.000 16.63348 ?  25  GLY A N   1 
ATOM   162  C  CA  . GLY A 1 45  ? -17.24200 -1.47500  2.61500   1.000 17.07064 ?  25  GLY A CA  1 
ATOM   163  C  C   . GLY A 1 45  ? -17.83400 -2.12800  1.38300   1.000 13.95704 ?  25  GLY A C   1 
ATOM   164  O  O   . GLY A 1 45  ? -17.12100 -2.86000  0.69000   1.000 12.59878 ?  25  GLY A O   1 
ATOM   165  N  N   . ILE A 1 46  ? -19.11100 -1.90400  1.08400   1.000 13.34117 ?  26  ILE A N   1 
ATOM   166  C  CA  . ILE A 1 46  ? -19.68600 -2.37700  -0.17300  1.000 13.46499 ?  26  ILE A CA  1 
ATOM   167  C  C   . ILE A 1 46  ? -20.76100 -1.39600  -0.61800  1.000 16.46458 ?  26  ILE A C   1 
ATOM   168  O  O   . ILE A 1 46  ? -21.60600 -0.97200  0.17700   1.000 18.98052 ?  26  ILE A O   1 
ATOM   169  C  CB  . ILE A 1 46  ? -20.24800 -3.81500  -0.07500  1.000 20.14884 ?  26  ILE A CB  1 
ATOM   170  C  CG1 . ILE A 1 46  ? -20.73400 -4.29200  -1.45200  1.000 15.30362 ?  26  ILE A CG1 1 
ATOM   171  C  CG2 . ILE A 1 46  ? -21.34100 -3.92500  0.98900   1.000 17.24123 ?  26  ILE A CG2 1 
ATOM   172  C  CD1 . ILE A 1 46  ? -20.74700 -5.79800  -1.62500  1.000 18.31853 ?  26  ILE A CD1 1 
ATOM   173  N  N   . ARG A 1 47  ? -20.70400 -1.00900  -1.88800  1.000 14.24297 ?  27  ARG A N   1 
ATOM   174  C  CA  . ARG A 1 47  ? -21.67100 -0.08400  -2.45200  1.000 21.43016 ?  27  ARG A CA  1 
ATOM   175  C  C   . ARG A 1 47  ? -21.83200 -0.39800  -3.92900  1.000 16.92426 ?  27  ARG A C   1 
ATOM   176  O  O   . ARG A 1 47  ? -20.86400 -0.75600  -4.60200  1.000 16.02975 ?  27  ARG A O   1 
ATOM   177  C  CB  . ARG A 1 47  ? -21.22500 1.37100   -2.25900  1.000 16.58306 ?  27  ARG A CB  1 
ATOM   178  C  CG  . ARG A 1 47  ? -22.24300 2.41800   -2.69200  1.000 35.04489 ?  27  ARG A CG  1 
ATOM   179  C  CD  . ARG A 1 47  ? -21.54200 3.69200   -3.14200  1.000 31.63817 ?  27  ARG A CD  1 
ATOM   180  N  NE  . ARG A 1 47  ? -22.35300 4.88600   -2.93000  1.000 50.77167 ?  27  ARG A NE  1 
ATOM   181  C  CZ  . ARG A 1 47  ? -23.21000 5.38300   -3.81300  1.000 56.43648 ?  27  ARG A CZ  1 
ATOM   182  N  NH1 . ARG A 1 47  ? -23.40700 4.80700   -4.98900  1.000 46.56001 ?  27  ARG A NH1 1 
ATOM   183  N  NH2 . ARG A 1 47  ? -23.88600 6.48800   -3.50800  1.000 61.67546 ?  27  ARG A NH2 1 
ATOM   184  N  N   . GLN A 1 48  ? -23.06000 -0.27900  -4.42900  1.000 19.04352 ?  28  GLN A N   1 
ATOM   185  C  CA  . GLN A 1 48  ? -23.30000 -0.36500  -5.86100  1.000 16.63619 ?  28  GLN A CA  1 
ATOM   186  C  C   . GLN A 1 48  ? -23.15400 1.02900   -6.45600  1.000 21.59491 ?  28  GLN A C   1 
ATOM   187  O  O   . GLN A 1 48  ? -23.86600 1.95800   -6.05700  1.000 24.98889 ?  28  GLN A O   1 
ATOM   188  C  CB  . GLN A 1 48  ? -24.68100 -0.94400  -6.16700  1.000 16.32276 ?  28  GLN A CB  1 
ATOM   189  C  CG  . GLN A 1 48  ? -24.96100 -1.01400  -7.65600  1.000 22.10127 ?  28  GLN A CG  1 
ATOM   190  C  CD  . GLN A 1 48  ? -26.21300 -1.80600  -7.98000  1.000 18.04474 ?  28  GLN A CD  1 
ATOM   191  O  OE1 . GLN A 1 48  ? -27.32400 -1.28400  -7.93300  1.000 28.09007 ?  28  GLN A OE1 1 
ATOM   192  N  NE2 . GLN A 1 48  ? -26.03600 -3.07900  -8.30100  1.000 22.30258 ?  28  GLN A NE2 1 
ATOM   193  N  N   . VAL A 1 49  ? -22.22200 1.17600   -7.39400  1.000 19.01597 ?  29  VAL A N   1 
ATOM   194  C  CA  . VAL A 1 49  ? -21.96000 2.44800   -8.04600  1.000 18.86644 ?  29  VAL A CA  1 
ATOM   195  C  C   . VAL A 1 49  ? -22.44000 2.34700   -9.48700  1.000 18.76962 ?  29  VAL A C   1 
ATOM   196  O  O   . VAL A 1 49  ? -22.53600 1.26100   -10.06000 1.000 20.52816 ?  29  VAL A O   1 
ATOM   197  C  CB  . VAL A 1 49  ? -20.46600 2.82600   -7.99300  1.000 21.14684 ?  29  VAL A CB  1 
ATOM   198  C  CG1 . VAL A 1 49  ? -20.03400 3.05800   -6.55100  1.000 24.45196 ?  29  VAL A CG1 1 
ATOM   199  C  CG2 . VAL A 1 49  ? -19.62200 1.75300   -8.65500  1.000 20.93588 ?  29  VAL A CG2 1 
ATOM   200  N  N   . SER A 1 50  ? -22.74700 3.50100   -10.08000 1.000 23.14223 ?  30  SER A N   1 
ATOM   201  C  CA  . SER A 1 50  ? -23.30700 3.53100   -11.42300 1.000 25.99259 ?  30  SER A CA  1 
ATOM   202  C  C   . SER A 1 50  ? -22.67100 4.64100   -12.24600 1.000 28.35448 ?  30  SER A C   1 
ATOM   203  O  O   . SER A 1 50  ? -22.40000 5.73000   -11.73300 1.000 31.42658 ?  30  SER A O   1 
ATOM   204  C  CB  . SER A 1 50  ? -24.83200 3.71900   -11.39100 1.000 23.48537 ?  30  SER A CB  1 
ATOM   205  O  OG  . SER A 1 50  ? -25.17600 5.07800   -11.18500 1.000 36.28289 ?  30  SER A OG  1 
ATOM   206  N  N   . THR A 1 51  ? -22.43900 4.35300   -13.52500 1.000 26.15137 ?  31  THR A N   1 
ATOM   207  C  CA  . THR A 1 51  ? -21.95700 5.34600   -14.47200 1.000 25.50951 ?  31  THR A CA  1 
ATOM   208  C  C   . THR A 1 51  ? -23.11400 6.23200   -14.91200 1.000 32.15939 ?  31  THR A C   1 
ATOM   209  O  O   . THR A 1 51  ? -24.28300 5.92000   -14.66200 1.000 25.32189 ?  31  THR A O   1 
ATOM   210  C  CB  . THR A 1 51  ? -21.31800 4.65500   -15.67600 1.000 24.94380 ?  31  THR A CB  1 
ATOM   211  O  OG1 . THR A 1 51  ? -22.30800 3.89500   -16.37900 1.000 27.65873 ?  31  THR A OG1 1 
ATOM   212  C  CG2 . THR A 1 51  ? -20.19500 3.73900   -15.23500 1.000 29.70352 ?  31  THR A CG2 1 
ATOM   213  N  N   . PRO A 1 52  ? -22.82500 7.35900   -15.57300 1.000 27.16171 ?  32  PRO A N   1 
ATOM   214  C  CA  . PRO A 1 52  ? -23.92200 8.19400   -16.09300 1.000 31.79837 ?  32  PRO A CA  1 
ATOM   215  C  C   . PRO A 1 52  ? -24.78200 7.50000   -17.13600 1.000 27.78913 ?  32  PRO A C   1 
ATOM   216  O  O   . PRO A 1 52  ? -25.89200 7.97400   -17.40900 1.000 31.36174 ?  32  PRO A O   1 
ATOM   217  C  CB  . PRO A 1 52  ? -23.18800 9.40700   -16.68400 1.000 30.77839 ?  32  PRO A CB  1 
ATOM   218  C  CG  . PRO A 1 52  ? -21.89700 9.45600   -15.93000 1.000 34.69159 ?  32  PRO A CG  1 
ATOM   219  C  CD  . PRO A 1 52  ? -21.51800 8.02100   -15.73800 1.000 34.45151 ?  32  PRO A CD  1 
ATOM   220  N  N   . ASP A 1 53  ? -24.31500 6.39800   -17.72500 1.000 27.56317 ?  33  ASP A N   1 
ATOM   221  C  CA  . ASP A 1 53  ? -25.10700 5.62600   -18.67200 1.000 26.57109 ?  33  ASP A CA  1 
ATOM   222  C  C   . ASP A 1 53  ? -25.91200 4.51000   -18.01500 1.000 26.36089 ?  33  ASP A C   1 
ATOM   223  O  O   . ASP A 1 53  ? -26.67200 3.82600   -18.71000 1.000 28.15330 ?  33  ASP A O   1 
ATOM   224  C  CB  . ASP A 1 53  ? -24.20100 5.02100   -19.75100 1.000 30.97043 ?  33  ASP A CB  1 
ATOM   225  C  CG  . ASP A 1 53  ? -23.75400 3.61200   -19.41200 1.000 36.07337 ?  33  ASP A CG  1 
ATOM   226  N  N   . GLY A 1 54  ? -25.75800 4.29900   -16.71000 1.000 24.90564 ?  34  GLY A N   1 
ATOM   227  C  CA  . GLY A 1 54  ? -26.51000 3.28300   -16.00200 1.000 22.09853 ?  34  GLY A CA  1 
ATOM   228  C  C   . GLY A 1 54  ? -25.79100 1.96700   -15.79500 1.000 22.75568 ?  34  GLY A C   1 
ATOM   229  O  O   . GLY A 1 54  ? -26.40400 1.02400   -15.28200 1.000 17.32665 ?  34  GLY A O   1 
ATOM   230  N  N   . ALA A 1 55  ? -24.52200 1.86700   -16.19100 1.000 15.94728 ?  35  ALA A N   1 
ATOM   231  C  CA  . ALA A 1 55  ? -23.73100 0.67500   -15.90000 1.000 21.25330 ?  35  ALA A CA  1 
ATOM   232  C  C   . ALA A 1 55  ? -23.39800 0.62200   -14.41400 1.000 18.45162 ?  35  ALA A C   1 
ATOM   233  O  O   . ALA A 1 55  ? -22.94200 1.61200   -13.83800 1.000 19.14981 ?  35  ALA A O   1 
ATOM   234  C  CB  . ALA A 1 55  ? -22.44500 0.68000   -16.72700 1.000 23.08224 ?  35  ALA A CB  1 
ATOM   235  N  N   . ALA A 1 56  ? -23.59400 -0.54100  -13.79400 1.000 13.37351 ?  36  ALA A N   1 
ATOM   236  C  CA  . ALA A 1 56  ? -23.45100 -0.66400  -12.35000 1.000 16.00079 ?  36  ALA A CA  1 
ATOM   237  C  C   . ALA A 1 56  ? -22.46800 -1.76500  -11.97000 1.000 14.22902 ?  36  ALA A C   1 
ATOM   238  O  O   . ALA A 1 56  ? -22.32700 -2.77500  -12.66700 1.000 16.24111 ?  36  ALA A O   1 
ATOM   239  C  CB  . ALA A 1 56  ? -24.80800 -0.93200  -11.68100 1.000 16.53718 ?  36  ALA A CB  1 
ATOM   240  N  N   . ALA A 1 57  ? -21.79300 -1.55100  -10.84200 1.000 12.54127 ?  37  ALA A N   1 
ATOM   241  C  CA  . ALA A 1 57  ? -20.87700 -2.52700  -10.27200 1.000 11.32501 ?  37  ALA A CA  1 
ATOM   242  C  C   . ALA A 1 57  ? -20.82400 -2.32400  -8.76500  1.000 10.49051 ?  37  ALA A C   1 
ATOM   243  O  O   . ALA A 1 57  ? -21.08700 -1.22900  -8.26300  1.000 17.30231 ?  37  ALA A O   1 
ATOM   244  C  CB  . ALA A 1 57  ? -19.46900 -2.39800  -10.87000 1.000 14.53426 ?  37  ALA A CB  1 
ATOM   245  N  N   . TRP A 1 58  ? -20.48500 -3.39200  -8.04600  1.000 10.87756 ?  38  TRP A N   1 
ATOM   246  C  CA  . TRP A 1 58  ? -20.26800 -3.32000  -6.60600  1.000 11.05848 ?  38  TRP A CA  1 
ATOM   247  C  C   . TRP A 1 58  ? -18.79200 -3.05100  -6.34800  1.000 11.73930 ?  38  TRP A C   1 
ATOM   248  O  O   . TRP A 1 58  ? -17.93800 -3.77700  -6.85900  1.000 15.75083 ?  38  TRP A O   1 
ATOM   249  C  CB  . TRP A 1 58  ? -20.66400 -4.62400  -5.91200  1.000 12.07839 ?  38  TRP A CB  1 
ATOM   250  C  CG  . TRP A 1 58  ? -22.10500 -5.00600  -6.03700  1.000 11.47524 ?  38  TRP A CG  1 
ATOM   251  C  CD1 . TRP A 1 58  ? -22.66700 -5.79900  -6.99500  1.000 10.59842 ?  38  TRP A CD1 1 
ATOM   252  C  CD2 . TRP A 1 58  ? -23.16900 -4.60600  -5.16900  1.000 16.17312 ?  38  TRP A CD2 1 
ATOM   253  N  NE1 . TRP A 1 58  ? -24.02100 -5.92500  -6.77300  1.000 12.26270 ?  38  TRP A NE1 1 
ATOM   254  C  CE2 . TRP A 1 58  ? -24.35300 -5.20100  -5.65600  1.000 18.70535 ?  38  TRP A CE2 1 
ATOM   255  C  CE3 . TRP A 1 58  ? -23.23400 -3.81200  -4.02200  1.000 12.96411 ?  38  TRP A CE3 1 
ATOM   256  C  CZ2 . TRP A 1 58  ? -25.59100 -5.01400  -5.03900  1.000 16.37188 ?  38  TRP A CZ2 1 
ATOM   257  C  CZ3 . TRP A 1 58  ? -24.46900 -3.62800  -3.40900  1.000 14.51568 ?  38  TRP A CZ3 1 
ATOM   258  C  CH2 . TRP A 1 58  ? -25.62600 -4.22800  -3.92100  1.000 16.85715 ?  38  TRP A CH2 1 
ATOM   259  N  N   . VAL A 1 59  ? -18.49900 -2.01600  -5.56300  1.000 12.20316 ?  39  VAL A N   1 
ATOM   260  C  CA  . VAL A 1 59  ? -17.13200 -1.71500  -5.14000  1.000 15.01272 ?  39  VAL A CA  1 
ATOM   261  C  C   . VAL A 1 59  ? -16.95600 -2.19800  -3.70400  1.000 14.23815 ?  39  VAL A C   1 
ATOM   262  O  O   . VAL A 1 59  ? -17.73600 -1.83700  -2.81200  1.000 12.82843 ?  39  VAL A O   1 
ATOM   263  C  CB  . VAL A 1 59  ? -16.81100 -0.21700  -5.28100  1.000 12.17036 ?  39  VAL A CB  1 
ATOM   264  C  CG1 . VAL A 1 59  ? -16.63000 0.13000   -6.75100  1.000 13.38351 ?  39  VAL A CG1 1 
ATOM   265  C  CG2 . VAL A 1 59  ? -17.90500 0.63900   -4.65700  1.000 18.98504 ?  39  VAL A CG2 1 
ATOM   266  N  N   . VAL A 1 60  ? -15.94200 -3.03600  -3.49200  1.000 11.77826 ?  40  VAL A N   1 
ATOM   267  C  CA  . VAL A 1 60  ? -15.63900 -3.63800  -2.19900  1.000 12.60367 ?  40  VAL A CA  1 
ATOM   268  C  C   . VAL A 1 60  ? -14.31000 -3.06800  -1.73300  1.000 14.40596 ?  40  VAL A C   1 
ATOM   269  O  O   . VAL A 1 60  ? -13.32200 -3.12100  -2.47100  1.000 13.53763 ?  40  VAL A O   1 
ATOM   270  C  CB  . VAL A 1 60  ? -15.57500 -5.17200  -2.30400  1.000 11.40467 ?  40  VAL A CB  1 
ATOM   271  C  CG1 . VAL A 1 60  ? -15.25200 -5.78100  -0.95000  1.000 12.42657 ?  40  VAL A CG1 1 
ATOM   272  C  CG2 . VAL A 1 60  ? -16.87800 -5.72400  -2.85700  1.000 14.20634 ?  40  VAL A CG2 1 
ATOM   273  N  N   . THR A 1 61  ? -14.27900 -2.52100  -0.51600  1.000 14.94958 ?  41  THR A N   1 
ATOM   274  C  CA  . THR A 1 61  ? -13.17800 -1.65100  -0.12400  1.000 11.23878 ?  41  THR A CA  1 
ATOM   275  C  C   . THR A 1 61  ? -12.46300 -2.00700  1.17400   1.000 14.62703 ?  41  THR A C   1 
ATOM   276  O  O   . THR A 1 61  ? -11.37200 -1.47200  1.40800   1.000 9.79426  ?  41  THR A O   1 
ATOM   277  C  CB  . THR A 1 61  ? -13.66600 -0.19900  -0.03500  1.000 14.75490 ?  41  THR A CB  1 
ATOM   278  O  OG1 . THR A 1 61  ? -14.89900 -0.14900  0.70700   1.000 12.47574 ?  41  THR A OG1 1 
ATOM   279  C  CG2 . THR A 1 61  ? -13.86700 0.36600   -1.43800  1.000 14.68725 ?  41  THR A CG2 1 
ATOM   280  N  N   . ARG A 1 62  ? -13.01000 -2.88200  2.01200   1.000 16.03697 ?  42  ARG A N   1 
ATOM   281  C  CA  . ARG A 1 62  ? -12.33900 -3.26500  3.25100   1.000 15.28941 ?  42  ARG A CA  1 
ATOM   282  C  C   . ARG A 1 62  ? -11.38400 -4.43200  3.03600   1.000 13.27769 ?  42  ARG A C   1 
ATOM   283  O  O   . ARG A 1 62  ? -11.67800 -5.35800  2.27900   1.000 12.46642 ?  42  ARG A O   1 
ATOM   284  C  CB  . ARG A 1 62  ? -13.36400 -3.61600  4.33200   1.000 17.96760 ?  42  ARG A CB  1 
ATOM   285  C  CG  . ARG A 1 62  ? -14.18800 -2.43100  4.79600   1.000 16.67295 ?  42  ARG A CG  1 
ATOM   286  C  CD  . ARG A 1 62  ? -15.19000 -2.84900  5.84900   1.000 18.60685 ?  42  ARG A CD  1 
ATOM   287  N  NE  . ARG A 1 62  ? -16.02200 -1.72500  6.25500   1.000 23.89044 ?  42  ARG A NE  1 
ATOM   288  C  CZ  . ARG A 1 62  ? -16.83500 -1.73500  7.30400   1.000 29.01066 ?  42  ARG A CZ  1 
ATOM   289  N  NH1 . ARG A 1 62  ? -17.05400 -2.83900  7.99900   1.000 31.20026 ?  42  ARG A NH1 1 
ATOM   290  N  NH2 . ARG A 1 62  ? -17.43400 -0.60400  7.67000   1.000 24.95772 ?  42  ARG A NH2 1 
ATOM   291  N  N   . TYR A 1 63  ? -10.24000 -4.37700  3.73100   1.000 15.07191 ?  43  TYR A N   1 
ATOM   292  C  CA  . TYR A 1 63  ? -9.19500  -5.39000  3.58900   1.000 11.71548 ?  43  TYR A CA  1 
ATOM   293  C  C   . TYR A 1 63  ? -9.73800  -6.81000  3.69500   1.000 15.71191 ?  43  TYR A C   1 
ATOM   294  O  O   . TYR A 1 63  ? -9.45500  -7.65700  2.83900   1.000 12.08715 ?  43  TYR A O   1 
ATOM   295  C  CB  . TYR A 1 63  ? -8.10700  -5.16800  4.64400   1.000 15.82001 ?  43  TYR A CB  1 
ATOM   296  C  CG  . TYR A 1 63  ? -6.90300  -6.07300  4.49100   1.000 14.11211 ?  43  TYR A CG  1 
ATOM   297  C  CD1 . TYR A 1 63  ? -6.90600  -7.35800  5.02500   1.000 16.39718 ?  43  TYR A CD1 1 
ATOM   298  C  CD2 . TYR A 1 63  ? -5.75500  -5.63700  3.84000   1.000 11.87102 ?  43  TYR A CD2 1 
ATOM   299  C  CE1 . TYR A 1 63  ? -5.80900  -8.19200  4.89500   1.000 17.59321 ?  43  TYR A CE1 1 
ATOM   300  C  CE2 . TYR A 1 63  ? -4.65200  -6.46100  3.71000   1.000 12.33212 ?  43  TYR A CE2 1 
ATOM   301  C  CZ  . TYR A 1 63  ? -4.68400  -7.73700  4.23900   1.000 18.43250 ?  43  TYR A CZ  1 
ATOM   302  O  OH  . TYR A 1 63  ? -3.59500  -8.56800  4.11300   1.000 14.69131 ?  43  TYR A OH  1 
ATOM   303  N  N   . ASP A 1 64  ? -10.49100 -7.09600  4.76400   1.000 15.60189 ?  44  ASP A N   1 
ATOM   304  C  CA  . ASP A 1 64  ? -10.96900 -8.45300  5.00500   1.000 16.58816 ?  44  ASP A CA  1 
ATOM   305  C  C   . ASP A 1 64  ? -11.79400 -8.96700  3.83500   1.000 15.33758 ?  44  ASP A C   1 
ATOM   306  O  O   . ASP A 1 64  ? -11.65900 -10.12800 3.43000   1.000 16.82391 ?  44  ASP A O   1 
ATOM   307  C  CB  . ASP A 1 64  ? -11.79800 -8.50300  6.29200   1.000 21.35010 ?  44  ASP A CB  1 
ATOM   308  C  CG  . ASP A 1 64  ? -10.97500 -8.19700  7.53400   1.000 27.71597 ?  44  ASP A CG  1 
ATOM   309  O  OD1 . ASP A 1 64  ? -9.75600  -8.44600  7.52200   1.000 24.82134 ?  44  ASP A OD1 1 
ATOM   310  O  OD2 . ASP A 1 64  ? -11.55600 -7.70300  8.52400   1.000 31.54708 -1 44  ASP A OD2 1 
ATOM   311  N  N   . ASP A 1 65  ? -12.66200 -8.11800  3.28200   1.000 14.23766 ?  45  ASP A N   1 
ATOM   312  C  CA  . ASP A 1 65  ? -13.52600 -8.56200  2.19400   1.000 11.88474 ?  45  ASP A CA  1 
ATOM   313  C  C   . ASP A 1 65  ? -12.78400 -8.61900  0.86700   1.000 13.65329 ?  45  ASP A C   1 
ATOM   314  O  O   . ASP A 1 65  ? -13.05600 -9.50100  0.04000   1.000 14.02320 ?  45  ASP A O   1 
ATOM   315  C  CB  . ASP A 1 65  ? -14.75700 -7.65700  2.08600   1.000 15.43635 ?  45  ASP A CB  1 
ATOM   316  C  CG  . ASP A 1 65  ? -15.50000 -7.54200  3.39800   1.000 17.36224 ?  45  ASP A CG  1 
ATOM   317  O  OD1 . ASP A 1 65  ? -15.88800 -8.60200  3.92900   1.000 22.04984 -1 45  ASP A OD1 1 
ATOM   318  O  OD2 . ASP A 1 65  ? -15.60200 -6.42600  3.95800   1.000 17.86204 -1 45  ASP A OD2 1 
ATOM   319  N  N   . VAL A 1 66  ? -11.84100 -7.69900  0.65300   1.000 12.29722 ?  46  VAL A N   1 
ATOM   320  C  CA  . VAL A 1 66  ? -11.01900 -7.74900  -0.55200  1.000 12.09047 ?  46  VAL A CA  1 
ATOM   321  C  C   . VAL A 1 66  ? -10.13600 -8.99000  -0.54700  1.000 12.27503 ?  46  VAL A C   1 
ATOM   322  O  O   . VAL A 1 66  ? -10.02700 -9.69600  -1.55600  1.000 12.41619 ?  46  VAL A O   1 
ATOM   323  C  CB  . VAL A 1 66  ? -10.18800 -6.46400  -0.68200  1.000 12.06854 ?  46  VAL A CB  1 
ATOM   324  C  CG1 . VAL A 1 66  ? -9.16900  -6.60900  -1.80500  1.000 15.59977 ?  46  VAL A CG1 1 
ATOM   325  C  CG2 . VAL A 1 66  ? -11.09400 -5.27700  -0.94200  1.000 9.66607  ?  46  VAL A CG2 1 
ATOM   326  N  N   . ARG A 1 67  ? -9.50600  -9.28500  0.59100   1.000 12.68186 ?  47  ARG A N   1 
ATOM   327  C  CA  . ARG A 1 67  ? -8.65700  -10.46800 0.67800   1.000 14.60944 ?  47  ARG A CA  1 
ATOM   328  C  C   . ARG A 1 67  ? -9.46000  -11.74300 0.45700   1.000 14.61303 ?  47  ARG A C   1 
ATOM   329  O  O   . ARG A 1 67  ? -9.09000  -12.58900 -0.36700  1.000 15.04580 ?  47  ARG A O   1 
ATOM   330  C  CB  . ARG A 1 67  ? -7.94300  -10.51000 2.03000   1.000 15.50917 ?  47  ARG A CB  1 
ATOM   331  C  CG  . ARG A 1 67  ? -6.80200  -11.51000 2.05600   1.000 20.49851 ?  47  ARG A CG  1 
ATOM   332  C  CD  . ARG A 1 67  ? -6.19800  -11.67300 3.44300   1.000 26.66376 ?  47  ARG A CD  1 
ATOM   333  N  NE  . ARG A 1 67  ? -5.70400  -13.03000 3.65700   1.000 25.74880 ?  47  ARG A NE  1 
ATOM   334  C  CZ  . ARG A 1 67  ? -6.47800  -14.08700 3.87100   1.000 32.83460 ?  47  ARG A CZ  1 
ATOM   335  N  NH1 . ARG A 1 67  ? -7.79600  -13.97700 3.94700   1.000 32.01723 ?  47  ARG A NH1 1 
ATOM   336  N  NH2 . ARG A 1 67  ? -5.91700  -15.28400 4.02300   1.000 37.11131 ?  47  ARG A NH2 1 
ATOM   337  N  N   . ALA A 1 68  ? -10.56300 -11.90300 1.19000   1.000 13.00217 ?  48  ALA A N   1 
ATOM   338  C  CA  . ALA A 1 68  ? -11.40000 -13.08300 1.00100   1.000 15.52107 ?  48  ALA A CA  1 
ATOM   339  C  C   . ALA A 1 68  ? -11.92400 -13.16100 -0.42800  1.000 16.45857 ?  48  ALA A C   1 
ATOM   340  O  O   . ALA A 1 68  ? -11.93100 -14.23700 -1.03800  1.000 13.31029 ?  48  ALA A O   1 
ATOM   341  C  CB  . ALA A 1 68  ? -12.56100 -13.06800 1.99600   1.000 19.20459 ?  48  ALA A CB  1 
ATOM   342  N  N   . GLY A 1 69  ? -12.35000 -12.02500 -0.98500  1.000 15.23580 ?  49  GLY A N   1 
ATOM   343  C  CA  . GLY A 1 69  ? -12.89300 -12.03600 -2.33400  1.000 15.52447 ?  49  GLY A CA  1 
ATOM   344  C  C   . GLY A 1 69  ? -11.89100 -12.51300 -3.36800  1.000 11.12052 ?  49  GLY A C   1 
ATOM   345  O  O   . GLY A 1 69  ? -12.21500 -13.33200 -4.23200  1.000 16.75477 ?  49  GLY A O   1 
ATOM   346  N  N   . LEU A 1 70  ? -10.65200 -12.00800 -3.28600  1.000 14.07453 ?  50  LEU A N   1 
ATOM   347  C  CA  . LEU A 1 70  ? -9.63900  -12.32400 -4.29000  1.000 11.34261 ?  50  LEU A CA  1 
ATOM   348  C  C   . LEU A 1 70  ? -9.51100  -13.82600 -4.51100  1.000 14.95479 ?  50  LEU A C   1 
ATOM   349  O  O   . LEU A 1 70  ? -9.38900  -14.28900 -5.65300  1.000 15.01205 ?  50  LEU A O   1 
ATOM   350  C  CB  . LEU A 1 70  ? -8.28800  -11.73100 -3.86800  1.000 8.23146  ?  50  LEU A CB  1 
ATOM   351  C  CG  . LEU A 1 70  ? -8.14800  -10.22600 -4.09500  1.000 10.16237 ?  50  LEU A CG  1 
ATOM   352  C  CD1 . LEU A 1 70  ? -6.88300  -9.69100  -3.42900  1.000 13.84670 ?  50  LEU A CD1 1 
ATOM   353  C  CD2 . LEU A 1 70  ? -8.14700  -9.91600  -5.58600  1.000 15.90155 ?  50  LEU A CD2 1 
ATOM   354  N  N   . ALA A 1 71  ? -9.56300  -14.60200 -3.43200  1.000 11.66096 ?  51  ALA A N   1 
ATOM   355  C  CA  . ALA A 1 71  ? -9.31600  -16.03500 -3.49100  1.000 15.13469 ?  51  ALA A CA  1 
ATOM   356  C  C   . ALA A 1 71  ? -10.58700 -16.87400 -3.53800  1.000 23.08863 ?  51  ALA A C   1 
ATOM   357  O  O   . ALA A 1 71  ? -10.49400 -18.08400 -3.76700  1.000 22.84643 ?  51  ALA A O   1 
ATOM   358  C  CB  . ALA A 1 71  ? -8.47900  -16.46900 -2.28200  1.000 16.80906 ?  51  ALA A CB  1 
ATOM   359  N  N   . ASP A 1 72  ? -11.75300 -16.26700 -3.33500  1.000 18.01186 ?  52  ASP A N   1 
ATOM   360  C  CA  . ASP A 1 72  ? -13.01100 -16.99900 -3.21000  1.000 18.73922 ?  52  ASP A CA  1 
ATOM   361  C  C   . ASP A 1 72  ? -13.32100 -17.79100 -4.47700  1.000 18.88159 ?  52  ASP A C   1 
ATOM   362  O  O   . ASP A 1 72  ? -13.49000 -17.19300 -5.55100  1.000 19.98381 ?  52  ASP A O   1 
ATOM   363  C  CB  . ASP A 1 72  ? -14.14300 -16.01900 -2.89400  1.000 19.09963 ?  52  ASP A CB  1 
ATOM   364  C  CG  . ASP A 1 72  ? -15.39400 -16.70900 -2.35400  1.000 25.45904 ?  52  ASP A CG  1 
ATOM   365  O  OD1 . ASP A 1 72  ? -15.69700 -17.84400 -2.77200  1.000 22.02790 ?  52  ASP A OD1 1 
ATOM   366  O  OD2 . ASP A 1 72  ? -16.07300 -16.10900 -1.49600  1.000 30.29811 -1 52  ASP A OD2 1 
ATOM   367  N  N   . PRO A 1 73  ? -13.41600 -19.12200 -4.40200  1.000 18.95887 ?  53  PRO A N   1 
ATOM   368  C  CA  . PRO A 1 73  ? -13.76900 -19.91000 -5.59500  1.000 16.37835 ?  53  PRO A CA  1 
ATOM   369  C  C   . PRO A 1 73  ? -15.16000 -19.62000 -6.13300  1.000 22.07545 ?  53  PRO A C   1 
ATOM   370  O  O   . PRO A 1 73  ? -15.46800 -20.03600 -7.25700  1.000 24.55103 ?  53  PRO A O   1 
ATOM   371  C  CB  . PRO A 1 73  ? -13.66400 -21.35900 -5.10100  1.000 24.26525 ?  53  PRO A CB  1 
ATOM   372  C  CG  . PRO A 1 73  ? -13.83900 -21.25900 -3.61000  1.000 23.66412 ?  53  PRO A CG  1 
ATOM   373  C  CD  . PRO A 1 73  ? -13.17200 -19.97100 -3.22600  1.000 20.71956 ?  53  PRO A CD  1 
ATOM   374  N  N   . ARG A 1 74  ? -16.00700 -18.93400 -5.37500  1.000 14.66612 ?  54  ARG A N   1 
ATOM   375  C  CA  . ARG A 1 74  ? -17.34900 -18.60100 -5.82700  1.000 17.15220 ?  54  ARG A CA  1 
ATOM   376  C  C   . ARG A 1 74  ? -17.40300 -17.26400 -6.54900  1.000 18.01403 ?  54  ARG A C   1 
ATOM   377  O  O   . ARG A 1 74  ? -18.49000 -16.82600 -6.93500  1.000 15.39976 ?  54  ARG A O   1 
ATOM   378  C  CB  . ARG A 1 74  ? -18.30800 -18.60100 -4.63800  1.000 20.08547 ?  54  ARG A CB  1 
ATOM   379  C  CG  . ARG A 1 74  ? -18.39200 -19.96000 -3.97400  1.000 20.35607 ?  54  ARG A CG  1 
ATOM   380  C  CD  . ARG A 1 74  ? -18.95800 -19.88000 -2.57600  1.000 23.32146 ?  54  ARG A CD  1 
ATOM   381  N  NE  . ARG A 1 74  ? -18.15100 -19.02600 -1.71500  1.000 21.99654 ?  54  ARG A NE  1 
ATOM   382  C  CZ  . ARG A 1 74  ? -18.47300 -18.70800 -0.46900  1.000 29.31748 ?  54  ARG A CZ  1 
ATOM   383  N  NH1 . ARG A 1 74  ? -19.56100 -19.19300 0.10900   1.000 25.00457 ?  54  ARG A NH1 1 
ATOM   384  N  NH2 . ARG A 1 74  ? -17.68200 -17.88700 0.21700   1.000 25.17288 ?  54  ARG A NH2 1 
ATOM   385  N  N   . LEU A 1 75  ? -16.25500 -16.62100 -6.75200  1.000 15.36506 ?  55  LEU A N   1 
ATOM   386  C  CA  . LEU A 1 75  ? -16.16000 -15.34400 -7.45100  1.000 12.72270 ?  55  LEU A CA  1 
ATOM   387  C  C   . LEU A 1 75  ? -15.36600 -15.60000 -8.72700  1.000 19.54125 ?  55  LEU A C   1 
ATOM   388  O  O   . LEU A 1 75  ? -14.14100 -15.77000 -8.68000  1.000 18.27804 ?  55  LEU A O   1 
ATOM   389  C  CB  . LEU A 1 75  ? -15.48700 -14.29700 -6.56500  1.000 16.17047 ?  55  LEU A CB  1 
ATOM   390  C  CG  . LEU A 1 75  ? -16.37200 -13.44700 -5.64300  1.000 17.07914 ?  55  LEU A CG  1 
ATOM   391  C  CD1 . LEU A 1 75  ? -15.53900 -12.42400 -4.87900  1.000 13.95618 ?  55  LEU A CD1 1 
ATOM   392  C  CD2 . LEU A 1 75  ? -17.49600 -12.76100 -6.41300  1.000 12.60663 ?  55  LEU A CD2 1 
ATOM   393  N  N   . SER A 1 76  ? -16.05900 -15.63800 -9.86100  1.000 15.95870 ?  56  SER A N   1 
ATOM   394  C  CA  . SER A 1 76  ? -15.46200 -16.07900 -11.11400 1.000 15.85852 ?  56  SER A CA  1 
ATOM   395  C  C   . SER A 1 76  ? -14.93100 -14.90000 -11.92600 1.000 11.46364 ?  56  SER A C   1 
ATOM   396  O  O   . SER A 1 76  ? -15.40800 -13.77000 -11.80500 1.000 11.54372 ?  56  SER A O   1 
ATOM   397  C  CB  . SER A 1 76  ? -16.48500 -16.86000 -11.94300 1.000 18.96282 ?  56  SER A CB  1 
ATOM   398  O  OG  . SER A 1 76  ? -17.57800 -16.04500 -12.33300 1.000 41.57317 ?  56  SER A OG  1 
ATOM   399  N  N   . VAL A 1 77  ? -13.92100 -15.17000 -12.75500 1.000 13.31200 ?  57  VAL A N   1 
ATOM   400  C  CA  . VAL A 1 77  ? -13.43400 -14.16900 -13.70000 1.000 11.62689 ?  57  VAL A CA  1 
ATOM   401  C  C   . VAL A 1 77  ? -13.96200 -14.42600 -15.10600 1.000 12.88222 ?  57  VAL A C   1 
ATOM   402  O  O   . VAL A 1 77  ? -13.60500 -13.71000 -16.04000 1.000 13.96510 ?  57  VAL A O   1 
ATOM   403  C  CB  . VAL A 1 77  ? -11.89600 -14.08800 -13.70200 1.000 10.76238 ?  57  VAL A CB  1 
ATOM   404  C  CG1 . VAL A 1 77  ? -11.40600 -13.42600 -12.42400 1.000 10.69768 ?  57  VAL A CG1 1 
ATOM   405  C  CG2 . VAL A 1 77  ? -11.28300 -15.46500 -13.91000 1.000 9.43553  ?  57  VAL A CG2 1 
ATOM   406  N  N   . ASP A 1 78  ? -14.82100 -15.43200 -15.27200 1.000 12.97242 ?  58  ASP A N   1 
ATOM   407  C  CA  . ASP A 1 78  ? -15.29200 -15.88900 -16.57500 1.000 15.59328 ?  58  ASP A CA  1 
ATOM   408  C  C   . ASP A 1 78  ? -16.61000 -15.19500 -16.89700 1.000 19.14330 ?  58  ASP A C   1 
ATOM   409  O  O   . ASP A 1 78  ? -17.60700 -15.39400 -16.19100 1.000 14.63486 ?  58  ASP A O   1 
ATOM   410  C  CB  . ASP A 1 78  ? -15.44400 -17.41000 -16.55600 1.000 18.60199 ?  58  ASP A CB  1 
ATOM   411  C  CG  . ASP A 1 78  ? -15.78100 -18.00200 -17.91600 1.000 26.04832 ?  58  ASP A CG  1 
ATOM   412  O  OD1 . ASP A 1 78  ? -16.36200 -17.30700 -18.77700 1.000 24.07232 ?  58  ASP A OD1 1 
ATOM   413  O  OD2 . ASP A 1 78  ? -15.43400 -19.18200 -18.12600 1.000 29.63005 -1 58  ASP A OD2 1 
ATOM   414  N  N   . ARG A 1 79  ? -16.61600 -14.38800 -17.96700 1.000 18.93264 ?  59  ARG A N   1 
ATOM   415  C  CA  . ARG A 1 79  ? -17.80800 -13.61800 -18.31000 1.000 17.67322 ?  59  ARG A CA  1 
ATOM   416  C  C   . ARG A 1 79  ? -19.01900 -14.49900 -18.59600 1.000 17.40269 ?  59  ARG A C   1 
ATOM   417  O  O   . ARG A 1 79  ? -20.14200 -13.98500 -18.59900 1.000 19.60151 ?  59  ARG A O   1 
ATOM   418  C  CB  . ARG A 1 79  ? -17.54100 -12.70400 -19.51400 1.000 22.18986 ?  59  ARG A CB  1 
ATOM   419  C  CG  . ARG A 1 79  ? -17.28600 -13.43500 -20.82300 1.000 19.47279 ?  59  ARG A CG  1 
ATOM   420  C  CD  . ARG A 1 79  ? -16.92500 -12.46100 -21.93800 1.000 22.39355 ?  59  ARG A CD  1 
ATOM   421  N  NE  . ARG A 1 79  ? -16.81900 -13.13100 -23.22900 1.000 25.82720 ?  59  ARG A NE  1 
ATOM   422  C  CZ  . ARG A 1 79  ? -15.75100 -13.79300 -23.65300 1.000 23.20472 ?  59  ARG A CZ  1 
ATOM   423  N  NH1 . ARG A 1 79  ? -14.62100 -13.79800 -22.96400 1.000 26.88369 ?  59  ARG A NH1 1 
ATOM   424  N  NH2 . ARG A 1 79  ? -15.81600 -14.45700 -24.80200 1.000 22.64890 ?  59  ARG A NH2 1 
ATOM   425  N  N   . SER A 1 80  ? -18.82600 -15.80400 -18.82100 1.000 17.75368 ?  60  SER A N   1 
ATOM   426  C  CA  . SER A 1 80  ? -19.97000 -16.69900 -18.97200 1.000 21.88232 ?  60  SER A CA  1 
ATOM   427  C  C   . SER A 1 80  ? -20.86600 -16.67300 -17.73800 1.000 24.13491 ?  60  SER A C   1 
ATOM   428  O  O   . SER A 1 80  ? -22.06700 -16.94800 -17.83900 1.000 16.50575 ?  60  SER A O   1 
ATOM   429  C  CB  . SER A 1 80  ? -19.49600 -18.12600 -19.24800 1.000 18.04902 ?  60  SER A CB  1 
ATOM   430  O  OG  . SER A 1 80  ? -18.90100 -18.69900 -18.09700 1.000 29.50455 ?  60  SER A OG  1 
ATOM   431  N  N   . ASN A 1 81  ? -20.31100 -16.33100 -16.57500 1.000 20.74764 ?  61  ASN A N   1 
ATOM   432  C  CA  . ASN A 1 81  ? -21.07100 -16.25400 -15.33300 1.000 23.53533 ?  61  ASN A CA  1 
ATOM   433  C  C   . ASN A 1 81  ? -21.59600 -14.85400 -15.02900 1.000 17.34800 ?  61  ASN A C   1 
ATOM   434  O  O   . ASN A 1 81  ? -22.17300 -14.64900 -13.95700 1.000 17.91873 ?  61  ASN A O   1 
ATOM   435  C  CB  . ASN A 1 81  ? -20.21900 -16.75400 -14.15900 1.000 19.98856 ?  61  ASN A CB  1 
ATOM   436  C  CG  . ASN A 1 81  ? -19.83400 -18.21200 -14.29900 1.000 28.19847 ?  61  ASN A CG  1 
ATOM   437  O  OD1 . ASN A 1 81  ? -20.68300 -19.06600 -14.56800 1.000 21.18203 ?  61  ASN A OD1 1 
ATOM   438  N  ND2 . ASN A 1 81  ? -18.55600 -18.50900 -14.10100 1.000 17.40823 ?  61  ASN A ND2 1 
ATOM   439  N  N   . ALA A 1 82  ? -21.41800 -13.89000 -15.92900 1.000 14.48053 ?  62  ALA A N   1 
ATOM   440  C  CA  . ALA A 1 82  ? -21.95100 -12.55500 -15.69900 1.000 14.64981 ?  62  ALA A CA  1 
ATOM   441  C  C   . ALA A 1 82  ? -23.42400 -12.48700 -16.08900 1.000 15.10601 ?  62  ALA A C   1 
ATOM   442  O  O   . ALA A 1 82  ? -23.87200 -13.17100 -17.01100 1.000 16.31675 ?  62  ALA A O   1 
ATOM   443  C  CB  . ALA A 1 82  ? -21.17800 -11.50000 -16.48500 1.000 15.72612 ?  62  ALA A CB  1 
ATOM   444  N  N   . GLY A 1 83  ? -24.16900 -11.63700 -15.38300 1.000 17.43928 ?  63  GLY A N   1 
ATOM   445  C  CA  . GLY A 1 83  ? -25.58600 -11.46500 -15.62300 1.000 18.31458 ?  63  GLY A CA  1 
ATOM   446  C  C   . GLY A 1 83  ? -25.88400 -10.37300 -16.63500 1.000 17.06382 ?  63  GLY A C   1 
ATOM   447  O  O   . GLY A 1 83  ? -24.99500 -9.78800  -17.25400 1.000 14.89966 ?  63  GLY A O   1 
ATOM   448  N  N   . ALA A 1 84  ? -27.18100 -10.08200 -16.78100 1.000 17.65493 ?  64  ALA A N   1 
ATOM   449  C  CA  . ALA A 1 84  ? -27.63400 -9.20400  -17.85700 1.000 15.30798 ?  64  ALA A CA  1 
ATOM   450  C  C   . ALA A 1 84  ? -27.14100 -7.77200  -17.68000 1.000 17.02934 ?  64  ALA A C   1 
ATOM   451  O  O   . ALA A 1 84  ? -27.03100 -7.03400  -18.66600 1.000 17.75790 ?  64  ALA A O   1 
ATOM   452  C  CB  . ALA A 1 84  ? -29.16400 -9.23200  -17.95100 1.000 15.88285 ?  64  ALA A CB  1 
ATOM   453  N  N   . GLY A 1 85  ? -26.85300 -7.35700  -16.44600 1.000 13.89009 ?  65  GLY A N   1 
ATOM   454  C  CA  . GLY A 1 85  ? -26.34800 -6.02300  -16.20300 1.000 11.17973 ?  65  GLY A CA  1 
ATOM   455  C  C   . GLY A 1 85  ? -24.87400 -5.82600  -16.48900 1.000 16.37075 ?  65  GLY A C   1 
ATOM   456  O  O   . GLY A 1 85  ? -24.34400 -4.75100  -16.20300 1.000 16.86149 ?  65  GLY A O   1 
ATOM   457  N  N   . TYR A 1 86  ? -24.20000 -6.82600  -17.05500 1.000 15.07998 ?  66  TYR A N   1 
ATOM   458  C  CA  . TYR A 1 86  ? -22.75800 -6.74300  -17.27100 1.000 15.07885 ?  66  TYR A CA  1 
ATOM   459  C  C   . TYR A 1 86  ? -22.43100 -5.69500  -18.32500 1.000 19.37990 ?  66  TYR A C   1 
ATOM   460  O  O   . TYR A 1 86  ? -23.01100 -5.69300  -19.41500 1.000 15.87832 ?  66  TYR A O   1 
ATOM   461  C  CB  . TYR A 1 86  ? -22.21100 -8.10400  -17.69300 1.000 14.19873 ?  66  TYR A CB  1 
ATOM   462  C  CG  . TYR A 1 86  ? -20.71200 -8.12100  -17.92400 1.000 12.99298 ?  66  TYR A CG  1 
ATOM   463  C  CD1 . TYR A 1 86  ? -19.83200 -7.75200  -16.92100 1.000 16.43606 ?  66  TYR A CD1 1 
ATOM   464  C  CD2 . TYR A 1 86  ? -20.18600 -8.51200  -19.15000 1.000 16.05501 ?  66  TYR A CD2 1 
ATOM   465  C  CE1 . TYR A 1 86  ? -18.44900 -7.77000  -17.13300 1.000 16.40154 ?  66  TYR A CE1 1 
ATOM   466  C  CE2 . TYR A 1 86  ? -18.81400 -8.53800  -19.37000 1.000 17.30044 ?  66  TYR A CE2 1 
ATOM   467  C  CZ  . TYR A 1 86  ? -17.95400 -8.16500  -18.35500 1.000 14.55106 ?  66  TYR A CZ  1 
ATOM   468  O  OH  . TYR A 1 86  ? -16.58700 -8.18000  -18.56900 1.000 12.72703 ?  66  TYR A OH  1 
ATOM   469  N  N   . ARG A 1 87  ? -21.49300 -4.80300  -18.00000 1.000 17.09830 ?  67  ARG A N   1 
ATOM   470  C  CA  . ARG A 1 87  ? -21.11200 -3.72300  -18.89900 1.000 17.14469 ?  67  ARG A CA  1 
ATOM   471  C  C   . ARG A 1 87  ? -19.60300 -3.57700  -19.05800 1.000 22.75933 ?  67  ARG A C   1 
ATOM   472  O  O   . ARG A 1 87  ? -19.15500 -2.63200  -19.71600 1.000 21.56264 ?  67  ARG A O   1 
ATOM   473  C  CB  . ARG A 1 87  ? -21.71200 -2.39500  -18.41300 1.000 14.90346 ?  67  ARG A CB  1 
ATOM   474  C  CG  . ARG A 1 87  ? -23.24000 -2.40900  -18.32800 1.000 23.91043 ?  67  ARG A CG  1 
ATOM   475  C  CD  . ARG A 1 87  ? -23.89400 -2.33800  -19.70900 1.000 27.79231 ?  67  ARG A CD  1 
ATOM   476  N  NE  . ARG A 1 87  ? -23.35300 -1.24800  -20.51400 1.000 26.95520 ?  67  ARG A NE  1 
ATOM   477  C  CZ  . ARG A 1 87  ? -23.84700 -0.01700  -20.52800 1.000 31.87046 ?  67  ARG A CZ  1 
ATOM   478  N  NH1 . ARG A 1 87  ? -24.90700 0.31300   -19.80400 1.000 27.39758 ?  67  ARG A NH1 1 
ATOM   479  N  NH2 . ARG A 1 87  ? -23.26200 0.90900   -21.28100 1.000 36.49823 ?  67  ARG A NH2 1 
ATOM   480  N  N   . GLY A 1 88  ? -18.80900 -4.47200  -18.47500 1.000 19.52116 ?  68  GLY A N   1 
ATOM   481  C  CA  . GLY A 1 88  ? -17.38200 -4.49500  -18.73800 1.000 18.60496 ?  68  GLY A CA  1 
ATOM   482  C  C   . GLY A 1 88  ? -16.49800 -3.60800  -17.88600 1.000 25.80791 ?  68  GLY A C   1 
ATOM   483  O  O   . GLY A 1 88  ? -15.56500 -2.98700  -18.41000 1.000 22.42160 ?  68  GLY A O   1 
ATOM   484  N  N   . PHE A 1 89  ? -16.76000 -3.54300  -16.58000 1.000 21.79320 ?  69  PHE A N   1 
ATOM   485  C  CA  . PHE A 1 89  ? -15.82400 -2.91300  -15.66000 1.000 19.06073 ?  69  PHE A CA  1 
ATOM   486  C  C   . PHE A 1 89  ? -14.59600 -3.79200  -15.47200 1.000 17.71977 ?  69  PHE A C   1 
ATOM   487  O  O   . PHE A 1 89  ? -14.68300 -5.02100  -15.49500 1.000 21.39067 ?  69  PHE A O   1 
ATOM   488  C  CB  . PHE A 1 89  ? -16.45300 -2.68900  -14.28200 1.000 14.25679 ?  69  PHE A CB  1 
ATOM   489  C  CG  . PHE A 1 89  ? -17.47500 -1.59500  -14.22800 1.000 17.66129 ?  69  PHE A CG  1 
ATOM   490  C  CD1 . PHE A 1 89  ? -18.81500 -1.85900  -14.49700 1.000 20.68118 ?  69  PHE A CD1 1 
ATOM   491  C  CD2 . PHE A 1 89  ? -17.10800 -0.30700  -13.87500 1.000 18.09713 ?  69  PHE A CD2 1 
ATOM   492  C  CE1 . PHE A 1 89  ? -19.75700 -0.85100  -14.42600 1.000 19.61119 ?  69  PHE A CE1 1 
ATOM   493  C  CE2 . PHE A 1 89  ? -18.05000 0.70500   -13.80900 1.000 30.93770 ?  69  PHE A CE2 1 
ATOM   494  C  CZ  . PHE A 1 89  ? -19.37500 0.43100   -14.08500 1.000 12.78463 ?  69  PHE A CZ  1 
ATOM   495  N  N   . SER A 1 90  ? -13.45200 -3.13700  -15.27000 1.000 18.71447 ?  70  SER A N   1 
ATOM   496  C  CA  . SER A 1 90  ? -12.17700 -3.76400  -14.88400 1.000 18.95209 ?  70  SER A CA  1 
ATOM   497  C  C   . SER A 1 90  ? -11.95200 -5.08300  -15.62000 1.000 18.25021 ?  70  SER A C   1 
ATOM   498  O  O   . SER A 1 90  ? -11.88000 -6.16500  -15.02500 1.000 15.22829 ?  70  SER A O   1 
ATOM   499  C  CB  . SER A 1 90  ? -12.10800 -3.96000  -13.37100 1.000 17.02409 ?  70  SER A CB  1 
ATOM   500  O  OG  . SER A 1 90  ? -10.82400 -4.40800  -12.95900 1.000 14.63922 ?  70  SER A OG  1 
ATOM   501  N  N   . LEU A 1 91  ? -11.84800 -4.97000  -16.93800 1.000 14.03092 ?  71  LEU A N   1 
ATOM   502  C  CA  . LEU A 1 91  ? -11.78300 -6.13300  -17.80500 1.000 18.18576 ?  71  LEU A CA  1 
ATOM   503  C  C   . LEU A 1 91  ? -10.44800 -6.85500  -17.65300 1.000 16.34785 ?  71  LEU A C   1 
ATOM   504  O  O   . LEU A 1 91  ? -9.44000  -6.25900  -17.25800 1.000 16.28769 ?  71  LEU A O   1 
ATOM   505  C  CB  . LEU A 1 91  ? -11.96100 -5.73000  -19.26800 1.000 18.41375 ?  71  LEU A CB  1 
ATOM   506  C  CG  . LEU A 1 91  ? -13.22500 -4.97700  -19.65600 1.000 19.14609 ?  71  LEU A CG  1 
ATOM   507  C  CD1 . LEU A 1 91  ? -12.91700 -4.08400  -20.85400 1.000 27.51181 ?  71  LEU A CD1 1 
ATOM   508  C  CD2 . LEU A 1 91  ? -14.31200 -5.98800  -19.96200 1.000 18.40301 ?  71  LEU A CD2 1 
ATOM   509  N  N   . PRO A 1 92  ? -10.42100 -8.14400  -17.97900 1.000 14.57264 ?  72  PRO A N   1 
ATOM   510  C  CA  . PRO A 1 92  ? -9.15100  -8.85400  -18.04200 1.000 12.85921 ?  72  PRO A CA  1 
ATOM   511  C  C   . PRO A 1 92  ? -8.23700  -8.19100  -19.04900 1.000 19.50850 ?  72  PRO A C   1 
ATOM   512  O  O   . PRO A 1 92  ? -8.69900  -7.66100  -20.07600 1.000 17.33091 ?  72  PRO A O   1 
ATOM   513  C  CB  . PRO A 1 92  ? -9.55500  -10.26000 -18.50200 1.000 15.56802 ?  72  PRO A CB  1 
ATOM   514  C  CG  . PRO A 1 92  ? -11.01000 -10.37900 -18.12100 1.000 17.04223 ?  72  PRO A CG  1 
ATOM   515  C  CD  . PRO A 1 92  ? -11.56300 -9.01300  -18.30100 1.000 13.94918 ?  72  PRO A CD  1 
ATOM   516  N  N   . PRO A 1 93  ? -6.92800  -8.18100  -18.78700 1.000 17.65935 ?  73  PRO A N   1 
ATOM   517  C  CA  . PRO A 1 93  ? -6.00500  -7.37600  -19.59900 1.000 23.88924 ?  73  PRO A CA  1 
ATOM   518  C  C   . PRO A 1 93  ? -5.58100  -8.02900  -20.90400 1.000 25.94624 ?  73  PRO A C   1 
ATOM   519  O  O   . PRO A 1 93  ? -4.47400  -7.76900  -21.38200 1.000 33.96499 ?  73  PRO A O   1 
ATOM   520  C  CB  . PRO A 1 93  ? -4.79700  -7.19500  -18.67000 1.000 23.71836 ?  73  PRO A CB  1 
ATOM   521  C  CG  . PRO A 1 93  ? -5.28200  -7.60400  -17.29600 1.000 27.01378 ?  73  PRO A CG  1 
ATOM   522  C  CD  . PRO A 1 93  ? -6.27800  -8.67700  -17.56200 1.000 21.33561 ?  73  PRO A CD  1 
ATOM   523  N  N   . ALA A 1 94  ? -6.42500  -8.86600  -21.49600 1.000 20.73846 ?  74  ALA A N   1 
ATOM   524  C  CA  . ALA A 1 94  ? -6.04700  -9.48900  -22.75600 1.000 27.87181 ?  74  ALA A CA  1 
ATOM   525  C  C   . ALA A 1 94  ? -7.28300  -10.01900 -23.45900 1.000 31.26494 ?  74  ALA A C   1 
ATOM   526  O  O   . ALA A 1 94  ? -8.27900  -10.36500 -22.81800 1.000 23.93221 ?  74  ALA A O   1 
ATOM   527  C  CB  . ALA A 1 94  ? -5.03500  -10.62300 -22.54900 1.000 24.35398 ?  74  ALA A CB  1 
ATOM   528  N  N   . LEU A 1 95  ? -7.20200  -10.06100 -24.78700 1.000 32.16874 ?  75  LEU A N   1 
ATOM   529  C  CA  . LEU A 1 95  ? -8.19900  -10.70300 -25.62400 1.000 34.48213 ?  75  LEU A CA  1 
ATOM   530  C  C   . LEU A 1 95  ? -8.01300  -12.21500 -25.56900 1.000 31.43528 ?  75  LEU A C   1 
ATOM   531  O  O   . LEU A 1 95  ? -6.94900  -12.71800 -25.19000 1.000 40.14815 ?  75  LEU A O   1 
ATOM   532  C  CB  . LEU A 1 95  ? -8.07500  -10.22300 -27.07200 1.000 37.12387 ?  75  LEU A CB  1 
ATOM   533  C  CG  . LEU A 1 95  ? -8.36300  -8.75100  -27.37400 1.000 35.63911 ?  75  LEU A CG  1 
ATOM   534  C  CD1 . LEU A 1 95  ? -7.57000  -8.31500  -28.59200 1.000 46.66542 ?  75  LEU A CD1 1 
ATOM   535  C  CD2 . LEU A 1 95  ? -9.84900  -8.53100  -27.59100 1.000 39.30563 ?  75  LEU A CD2 1 
ATOM   536  N  N   . ASP A 1 96  ? -9.06300  -12.94000 -25.95700 1.000 31.76842 ?  76  ASP A N   1 
ATOM   537  C  CA  . ASP A 1 96  ? -9.02500  -14.40000 -25.98600 1.000 31.59193 ?  76  ASP A CA  1 
ATOM   538  C  C   . ASP A 1 96  ? -8.82200  -14.98100 -24.59200 1.000 33.86227 ?  76  ASP A C   1 
ATOM   539  O  O   . ASP A 1 96  ? -8.75100  -14.24400 -23.60300 1.000 32.09817 ?  76  ASP A O   1 
ATOM   540  C  CB  . ASP A 1 96  ? -7.91700  -14.90000 -26.92100 1.000 35.94775 ?  76  ASP A CB  1 
ATOM   541  C  CG  . ASP A 1 96  ? -8.39500  -15.97100 -27.87700 1.000 46.08908 ?  76  ASP A CG  1 
ATOM   542  O  OD1 . ASP A 1 96  ? -9.29600  -16.75200 -27.49800 1.000 47.55249 -1 76  ASP A OD1 1 
ATOM   543  O  OD2 . ASP A 1 96  ? -7.85300  -16.04200 -29.00100 1.000 45.04579 ?  76  ASP A OD2 1 
ATOM   544  N  N   . ALA A 1 97  ? -8.71600  -16.30500 -24.51300 1.000 33.45816 ?  77  ALA A N   1 
ATOM   545  C  CA  . ALA A 1 97  ? -8.58700  -16.97200 -23.22700 1.000 31.35450 ?  77  ALA A CA  1 
ATOM   546  C  C   . ALA A 1 97  ? -7.22100  -16.69100 -22.61600 1.000 26.34604 ?  77  ALA A C   1 
ATOM   547  O  O   . ALA A 1 97  ? -6.18600  -16.83900 -23.27500 1.000 24.88820 ?  77  ALA A O   1 
ATOM   548  C  CB  . ALA A 1 97  ? -8.80200  -18.47600 -23.38400 1.000 29.62074 ?  77  ALA A CB  1 
ATOM   549  N  N   . ASN A 1 98  ? -7.22400  -16.27800 -21.35300 1.000 18.59125 ?  78  ASN A N   1 
ATOM   550  C  CA  . ASN A 1 98  ? -5.99900  -15.97800 -20.63700 1.000 20.79087 ?  78  ASN A CA  1 
ATOM   551  C  C   . ASN A 1 98  ? -6.21800  -16.28500 -19.16300 1.000 17.93360 ?  78  ASN A C   1 
ATOM   552  O  O   . ASN A 1 98  ? -7.33500  -16.56600 -18.72200 1.000 20.68017 ?  78  ASN A O   1 
ATOM   553  C  CB  . ASN A 1 98  ? -5.56600  -14.52100 -20.86000 1.000 17.34722 ?  78  ASN A CB  1 
ATOM   554  C  CG  . ASN A 1 98  ? -6.57000  -13.52100 -20.31400 1.000 22.59754 ?  78  ASN A CG  1 
ATOM   555  O  OD1 . ASN A 1 98  ? -6.53100  -13.15900 -19.13800 1.000 21.34708 ?  78  ASN A OD1 1 
ATOM   556  N  ND2 . ASN A 1 98  ? -7.47500  -13.06000 -21.17700 1.000 25.45492 ?  78  ASN A ND2 1 
ATOM   557  N  N   . LEU A 1 99  ? -5.12400  -16.22800 -18.40100 1.000 15.38784 ?  79  LEU A N   1 
ATOM   558  C  CA  . LEU A 1 99  ? -5.17700  -16.56900 -16.98200 1.000 13.96615 ?  79  LEU A CA  1 
ATOM   559  C  C   . LEU A 1 99  ? -6.25200  -15.78300 -16.23600 1.000 16.98838 ?  79  LEU A C   1 
ATOM   560  O  O   . LEU A 1 99  ? -6.86400  -16.30000 -15.29300 1.000 12.43297 ?  79  LEU A O   1 
ATOM   561  C  CB  . LEU A 1 99  ? -3.80800  -16.33900 -16.34300 1.000 17.56342 ?  79  LEU A CB  1 
ATOM   562  C  CG  . LEU A 1 99  ? -2.73700  -17.38400 -16.65400 1.000 16.68041 ?  79  LEU A CG  1 
ATOM   563  C  CD1 . LEU A 1 99  ? -1.36700  -16.92600 -16.17900 1.000 16.85764 ?  79  LEU A CD1 1 
ATOM   564  C  CD2 . LEU A 1 99  ? -3.10100  -18.69000 -15.99200 1.000 15.53872 ?  79  LEU A CD2 1 
ATOM   565  N  N   . LEU A 1 100 ? -6.50300  -14.53600 -16.63800 1.000 11.23386 ?  80  LEU A N   1 
ATOM   566  C  CA  . LEU A 1 100 ? -7.37900  -13.65400 -15.87400 1.000 18.32494 ?  80  LEU A CA  1 
ATOM   567  C  C   . LEU A 1 100 ? -8.80900  -13.58700 -16.40600 1.000 15.47397 ?  80  LEU A C   1 
ATOM   568  O  O   . LEU A 1 100 ? -9.57500  -12.72400 -15.96600 1.000 15.89363 ?  80  LEU A O   1 
ATOM   569  C  CB  . LEU A 1 100 ? -6.77500  -12.24700 -15.78900 1.000 12.97341 ?  80  LEU A CB  1 
ATOM   570  C  CG  . LEU A 1 100 ? -5.61400  -12.09300 -14.80200 1.000 11.22268 ?  80  LEU A CG  1 
ATOM   571  C  CD1 . LEU A 1 100 ? -4.96600  -10.71400 -14.90100 1.000 15.49844 ?  80  LEU A CD1 1 
ATOM   572  C  CD2 . LEU A 1 100 ? -6.10400  -12.35100 -13.37600 1.000 13.31899 ?  80  LEU A CD2 1 
ATOM   573  N  N   . ASN A 1 101 ? -9.19600  -14.47200 -17.33000 1.000 15.11908 ?  81  ASN A N   1 
ATOM   574  C  CA  . ASN A 1 101 ? -10.60200 -14.59600 -17.70200 1.000 15.60660 ?  81  ASN A CA  1 
ATOM   575  C  C   . ASN A 1 101 ? -11.07900 -16.04600 -17.65600 1.000 15.22074 ?  81  ASN A C   1 
ATOM   576  O  O   . ASN A 1 101 ? -12.12200 -16.37000 -18.23500 1.000 17.55421 ?  81  ASN A O   1 
ATOM   577  C  CB  . ASN A 1 101 ? -10.87000 -13.96700 -19.07600 1.000 14.90199 ?  81  ASN A CB  1 
ATOM   578  C  CG  . ASN A 1 101 ? -10.28800 -14.76200 -20.24200 1.000 16.73160 ?  81  ASN A CG  1 
ATOM   579  O  OD1 . ASN A 1 101 ? -9.73800  -15.85200 -20.08400 1.000 20.95612 ?  81  ASN A OD1 1 
ATOM   580  N  ND2 . ASN A 1 101 ? -10.40600 -14.19500 -21.43500 1.000 22.94827 ?  81  ASN A ND2 1 
ATOM   581  N  N   . LEU A 1 102 ? -10.34500 -16.91400 -16.96400 1.000 18.31764 ?  82  LEU A N   1 
ATOM   582  C  CA  . LEU A 1 102 ? -10.64100 -18.33700 -16.88300 1.000 21.08025 ?  82  LEU A CA  1 
ATOM   583  C  C   . LEU A 1 102 ? -10.65600 -18.77400 -15.42400 1.000 20.23757 ?  82  LEU A C   1 
ATOM   584  O  O   . LEU A 1 102 ? -9.83500  -18.31600 -14.62100 1.000 16.62125 ?  82  LEU A O   1 
ATOM   585  C  CB  . LEU A 1 102 ? -9.59400  -19.16200 -17.64700 1.000 21.09967 ?  82  LEU A CB  1 
ATOM   586  C  CG  . LEU A 1 102 ? -9.60200  -19.06300 -19.17400 1.000 22.84871 ?  82  LEU A CG  1 
ATOM   587  C  CD1 . LEU A 1 102 ? -8.49500  -19.93200 -19.76500 1.000 26.55069 ?  82  LEU A CD1 1 
ATOM   588  C  CD2 . LEU A 1 102 ? -10.95500 -19.47000 -19.72500 1.000 20.67447 ?  82  LEU A CD2 1 
ATOM   589  N  N   . ASP A 1 103 ? -11.57300 -19.66800 -15.09400 1.000 15.69822 ?  83  ASP A N   1 
ATOM   590  C  CA  . ASP A 1 103 ? -11.63900 -20.32300 -13.79800 1.000 16.42693 ?  83  ASP A CA  1 
ATOM   591  C  C   . ASP A 1 103 ? -11.07600 -21.72900 -13.89700 1.000 15.42494 ?  83  ASP A C   1 
ATOM   592  O  O   . ASP A 1 103 ? -10.88000 -22.25900 -14.99400 1.000 17.44822 ?  83  ASP A O   1 
ATOM   593  C  CB  . ASP A 1 103 ? -13.08800 -20.38600 -13.30000 1.000 16.16903 ?  83  ASP A CB  1 
ATOM   594  C  CG  . ASP A 1 103 ? -13.74100 -19.02700 -13.20500 1.000 22.91353 ?  83  ASP A CG  1 
ATOM   595  O  OD1 . ASP A 1 103 ? -13.07100 -18.07200 -12.76800 1.000 18.19207 ?  83  ASP A OD1 1 
ATOM   596  O  OD2 . ASP A 1 103 ? -14.94300 -18.93200 -13.52800 1.000 18.46755 -1 83  ASP A OD2 1 
ATOM   597  N  N   . PRO A 1 104 ? -10.80600 -22.37400 -12.76100 1.000 18.29675 ?  84  PRO A N   1 
ATOM   598  C  CA  . PRO A 1 104 ? -10.47200 -23.79400 -12.79600 1.000 20.09353 ?  84  PRO A CA  1 
ATOM   599  C  C   . PRO A 1 104 ? -11.59200 -24.58600 -13.44100 1.000 20.98544 ?  84  PRO A C   1 
ATOM   600  O  O   . PRO A 1 104 ? -12.77900 -24.23400 -13.31000 1.000 17.83787 ?  84  PRO A O   1 
ATOM   601  C  CB  . PRO A 1 104 ? -10.31500 -24.15400 -11.31300 1.000 19.40123 ?  84  PRO A CB  1 
ATOM   602  C  CG  . PRO A 1 104 ? -9.87200  -22.88000 -10.69000 1.000 23.78390 ?  84  PRO A CG  1 
ATOM   603  C  CD  . PRO A 1 104 ? -10.66700 -21.82100 -11.39900 1.000 22.70777 ?  84  PRO A CD  1 
ATOM   604  N  N   . PRO A 1 105 ? -11.26200 -25.67300 -14.14400 1.000 22.70652 ?  85  PRO A N   1 
ATOM   605  C  CA  . PRO A 1 105 ? -9.94500  -26.28400 -14.31500 1.000 19.67030 ?  85  PRO A CA  1 
ATOM   606  C  C   . PRO A 1 105 ? -9.12800  -25.67900 -15.45200 1.000 23.92817 ?  85  PRO A C   1 
ATOM   607  O  O   . PRO A 1 105 ? -7.93100  -25.92800 -15.54100 1.000 23.17875 ?  85  PRO A O   1 
ATOM   608  C  CB  . PRO A 1 105 ? -10.30600 -27.74300 -14.60000 1.000 21.02681 ?  85  PRO A CB  1 
ATOM   609  C  CG  . PRO A 1 105 ? -11.53500 -27.61700 -15.45200 1.000 27.75659 ?  85  PRO A CG  1 
ATOM   610  C  CD  . PRO A 1 105 ? -12.30000 -26.44100 -14.86100 1.000 26.94277 ?  85  PRO A CD  1 
ATOM   611  N  N   . ASP A 1 106 ? -9.74700  -24.89300 -16.33700 1.000 21.28821 ?  86  ASP A N   1 
ATOM   612  C  CA  . ASP A 1 106 ? -9.00600  -24.31900 -17.45600 1.000 21.21175 ?  86  ASP A CA  1 
ATOM   613  C  C   . ASP A 1 106 ? -7.89300  -23.40000 -16.96900 1.000 20.22282 ?  86  ASP A C   1 
ATOM   614  O  O   . ASP A 1 106 ? -6.79800  -23.38200 -17.54500 1.000 24.72773 ?  86  ASP A O   1 
ATOM   615  C  CB  . ASP A 1 106 ? -9.95500  -23.56300 -18.38300 1.000 24.14906 ?  86  ASP A CB  1 
ATOM   616  C  CG  . ASP A 1 106 ? -10.91200 -24.48600 -19.11700 1.000 33.59695 ?  86  ASP A CG  1 
ATOM   617  O  OD1 . ASP A 1 106 ? -10.81100 -25.71800 -18.93900 1.000 39.98572 ?  86  ASP A OD1 1 
ATOM   618  O  OD2 . ASP A 1 106 ? -11.76400 -23.97800 -19.87600 1.000 41.33229 -1 86  ASP A OD2 1 
ATOM   619  N  N   . HIS A 1 107 ? -8.15700  -22.62700 -15.91100 1.000 20.26508 ?  87  HIS A N   1 
ATOM   620  C  CA  . HIS A 1 107 ? -7.11600  -21.77400 -15.34800 1.000 19.94990 ?  87  HIS A CA  1 
ATOM   621  C  C   . HIS A 1 107 ? -5.95300  -22.60000 -14.81800 1.000 17.79403 ?  87  HIS A C   1 
ATOM   622  O  O   . HIS A 1 107 ? -4.78700  -22.23000 -14.99100 1.000 19.31169 ?  87  HIS A O   1 
ATOM   623  C  CB  . HIS A 1 107 ? -7.68200  -20.91100 -14.22200 1.000 15.17993 ?  87  HIS A CB  1 
ATOM   624  C  CG  . HIS A 1 107 ? -6.62900  -20.13900 -13.49500 1.000 18.25845 ?  87  HIS A CG  1 
ATOM   625  N  ND1 . HIS A 1 107 ? -6.09800  -20.55900 -12.29600 1.000 17.63868 ?  87  HIS A ND1 1 
ATOM   626  C  CD2 . HIS A 1 107 ? -5.99600  -18.98100 -13.80300 1.000 13.97363 ?  87  HIS A CD2 1 
ATOM   627  C  CE1 . HIS A 1 107 ? -5.18300  -19.69400 -11.89500 1.000 13.83682 ?  87  HIS A CE1 1 
ATOM   628  N  NE2 . HIS A 1 107 ? -5.10600  -18.72500 -12.78900 1.000 13.58768 ?  87  HIS A NE2 1 
ATOM   629  N  N   . THR A 1 108 ? -6.25500  -23.72100 -14.15800 1.000 21.06654 ?  88  THR A N   1 
ATOM   630  C  CA  . THR A 1 108 ? -5.20000  -24.54300 -13.57300 1.000 22.42128 ?  88  THR A CA  1 
ATOM   631  C  C   . THR A 1 108 ? -4.24600  -25.07100 -14.63800 1.000 23.50632 ?  88  THR A C   1 
ATOM   632  O  O   . THR A 1 108 ? -3.03700  -25.17000 -14.40100 1.000 23.09223 ?  88  THR A O   1 
ATOM   633  C  CB  . THR A 1 108 ? -5.81500  -25.69500 -12.78100 1.000 27.45234 ?  88  THR A CB  1 
ATOM   634  O  OG1 . THR A 1 108 ? -6.62100  -25.16500 -11.71800 1.000 29.97709 ?  88  THR A OG1 1 
ATOM   635  C  CG2 . THR A 1 108 ? -4.72300  -26.58000 -12.19900 1.000 30.83073 ?  88  THR A CG2 1 
ATOM   636  N  N   . ARG A 1 109 ? -4.76700  -25.40300 -15.82000 1.000 25.31244 ?  89  ARG A N   1 
ATOM   637  C  CA  . ARG A 1 109 ? -3.90500  -25.88600 -16.89500 1.000 26.04509 ?  89  ARG A CA  1 
ATOM   638  C  C   . ARG A 1 109 ? -2.94400  -24.80000 -17.36400 1.000 24.05855 ?  89  ARG A C   1 
ATOM   639  O  O   . ARG A 1 109 ? -1.73000  -25.02500 -17.43800 1.000 19.99878 ?  89  ARG A O   1 
ATOM   640  C  CB  . ARG A 1 109 ? -4.74600  -26.39300 -18.06600 1.000 24.75394 ?  89  ARG A CB  1 
ATOM   641  C  CG  . ARG A 1 109 ? -3.90400  -26.77800 -19.27000 1.000 33.28858 ?  89  ARG A CG  1 
ATOM   642  C  CD  . ARG A 1 109 ? -4.74700  -27.23600 -20.44800 1.000 37.09324 ?  89  ARG A CD  1 
ATOM   643  N  NE  . ARG A 1 109 ? -4.03400  -27.04300 -21.70600 1.000 36.44090 ?  89  ARG A NE  1 
ATOM   644  C  CZ  . ARG A 1 109 ? -4.01200  -25.90600 -22.38800 1.000 35.76579 ?  89  ARG A CZ  1 
ATOM   645  N  NH1 . ARG A 1 109 ? -4.70700  -24.85100 -21.99500 1.000 35.35606 ?  89  ARG A NH1 1 
ATOM   646  N  NH2 . ARG A 1 109 ? -3.27900  -25.82800 -23.49600 1.000 34.90011 ?  89  ARG A NH2 1 
ATOM   647  N  N   . LEU A 1 110 ? -3.47400  -23.61800 -17.69700 1.000 22.48345 ?  90  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 110 ? -2.62400  -22.51700 -18.14800 1.000 22.54552 ?  90  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 110 ? -1.58300  -22.15800 -17.09800 1.000 19.37603 ?  90  LEU A C   1 
ATOM   650  O  O   . LEU A 1 110 ? -0.40400  -21.95600 -17.41500 1.000 20.95705 ?  90  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 110 ? -3.47600  -21.29300 -18.47700 1.000 20.01025 ?  90  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 110 ? -4.18600  -21.25600 -19.82300 1.000 30.56851 ?  90  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 110 ? -4.71200  -19.85200 -20.08000 1.000 33.27227 ?  90  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 110 ? -3.23800  -21.68800 -20.91700 1.000 31.07141 ?  90  LEU A CD2 1 
ATOM   655  N  N   . ARG A 1 111 ? -2.01200  -22.04900 -15.83900 1.000 19.54404 ?  91  ARG A N   1 
ATOM   656  C  CA  . ARG A 1 111 ? -1.09100  -21.66300 -14.77700 1.000 19.32148 ?  91  ARG A CA  1 
ATOM   657  C  C   . ARG A 1 111 ? 0.04700   -22.66600 -14.64900 1.000 21.39760 ?  91  ARG A C   1 
ATOM   658  O  O   . ARG A 1 111 ? 1.21800   -22.28700 -14.54400 1.000 20.19493 ?  91  ARG A O   1 
ATOM   659  C  CB  . ARG A 1 111 ? -1.84100  -21.53100 -13.45400 1.000 15.15753 ?  91  ARG A CB  1 
ATOM   660  C  CG  . ARG A 1 111 ? -0.95400  -21.06500 -12.31700 1.000 22.42215 ?  91  ARG A CG  1 
ATOM   661  C  CD  . ARG A 1 111 ? -1.24800  -19.63400 -11.93400 1.000 22.02751 ?  91  ARG A CD  1 
ATOM   662  N  NE  . ARG A 1 111 ? -0.36500  -19.16600 -10.87100 1.000 19.35777 ?  91  ARG A NE  1 
ATOM   663  C  CZ  . ARG A 1 111 ? -0.32800  -17.91700 -10.42400 1.000 22.67997 ?  91  ARG A CZ  1 
ATOM   664  N  NH1 . ARG A 1 111 ? -1.14900  -16.99300 -10.89200 1.000 16.58914 ?  91  ARG A NH1 1 
ATOM   665  N  NH2 . ARG A 1 111 ? 0.55300   -17.58900 -9.48100  1.000 17.88236 ?  91  ARG A NH2 1 
ATOM   666  N  N   . THR A 1 112 ? -0.28300  -23.95800 -14.66300 1.000 19.37510 ?  92  THR A N   1 
ATOM   667  C  CA  . THR A 1 112 ? 0.74600   -24.98300 -14.53500 1.000 22.65757 ?  92  THR A CA  1 
ATOM   668  C  C   . THR A 1 112 ? 1.71600   -24.93300 -15.70900 1.000 23.35396 ?  92  THR A C   1 
ATOM   669  O  O   . THR A 1 112 ? 2.93400   -25.05100 -15.52600 1.000 24.57786 ?  92  THR A O   1 
ATOM   670  C  CB  . THR A 1 112 ? 0.09400   -26.36300 -14.42600 1.000 30.13297 ?  92  THR A CB  1 
ATOM   671  O  OG1 . THR A 1 112 ? -0.68600  -26.43400 -13.22500 1.000 26.18681 ?  92  THR A OG1 1 
ATOM   672  C  CG2 . THR A 1 112 ? 1.14900   -27.45100 -14.39400 1.000 28.42014 ?  92  THR A CG2 1 
ATOM   673  N  N   . LEU A 1 113 ? 1.19500   -24.72800 -16.92100 1.000 24.08924 ?  93  LEU A N   1 
ATOM   674  C  CA  . LEU A 1 113 ? 2.05300   -24.65300 -18.09900 1.000 28.14562 ?  93  LEU A CA  1 
ATOM   675  C  C   . LEU A 1 113 ? 2.97700   -23.44400 -18.03700 1.000 28.26050 ?  93  LEU A C   1 
ATOM   676  O  O   . LEU A 1 113 ? 4.18500   -23.56200 -18.27500 1.000 26.12761 ?  93  LEU A O   1 
ATOM   677  C  CB  . LEU A 1 113 ? 1.19900   -24.61300 -19.36200 1.000 26.98744 ?  93  LEU A CB  1 
ATOM   678  C  CG  . LEU A 1 113 ? 0.50200   -25.93200 -19.69600 1.000 25.17709 ?  93  LEU A CG  1 
ATOM   679  C  CD1 . LEU A 1 113 ? -0.27900  -25.82100 -20.99100 1.000 33.42247 ?  93  LEU A CD1 1 
ATOM   680  C  CD2 . LEU A 1 113 ? 1.52100   -27.06000 -19.77300 1.000 35.16666 ?  93  LEU A CD2 1 
ATOM   681  N  N   . ILE A 1 114 ? 2.42800   -22.27000 -17.72200 1.000 23.98096 ?  94  ILE A N   1 
ATOM   682  C  CA  . ILE A 1 114 ? 3.24400   -21.05900 -17.72200 1.000 25.32963 ?  94  ILE A CA  1 
ATOM   683  C  C   . ILE A 1 114 ? 4.22500   -21.06600 -16.55400 1.000 23.26216 ?  94  ILE A C   1 
ATOM   684  O  O   . ILE A 1 114 ? 5.37100   -20.61700 -16.68800 1.000 26.00289 ?  94  ILE A O   1 
ATOM   685  C  CB  . ILE A 1 114 ? 2.34500   -19.80800 -17.71700 1.000 22.48556 ?  94  ILE A CB  1 
ATOM   686  C  CG1 . ILE A 1 114 ? 1.63700   -19.66400 -19.07000 1.000 18.71558 ?  94  ILE A CG1 1 
ATOM   687  C  CG2 . ILE A 1 114 ? 3.16200   -18.55600 -17.41800 1.000 26.11820 ?  94  ILE A CG2 1 
ATOM   688  C  CD1 . ILE A 1 114 ? 0.20500   -19.20300 -18.97700 1.000 22.80189 ?  94  ILE A CD1 1 
ATOM   689  N  N   . ALA A 1 115 ? 3.80900   -21.59300 -15.39800 1.000 21.67993 ?  95  ALA A N   1 
ATOM   690  C  CA  . ALA A 1 115 ? 4.70500   -21.63100 -14.24500 1.000 28.12138 ?  95  ALA A CA  1 
ATOM   691  C  C   . ALA A 1 115 ? 5.94100   -22.48600 -14.49900 1.000 30.63454 ?  95  ALA A C   1 
ATOM   692  O  O   . ALA A 1 115 ? 6.93900   -22.33900 -13.78500 1.000 29.14917 ?  95  ALA A O   1 
ATOM   693  C  CB  . ALA A 1 115 ? 3.96500   -22.14800 -13.00900 1.000 25.91104 ?  95  ALA A CB  1 
ATOM   694  N  N   . GLY A 1 116 ? 5.89900   -23.37600 -15.49400 1.000 29.28367 ?  96  GLY A N   1 
ATOM   695  C  CA  . GLY A 1 116 ? 7.04700   -24.21100 -15.79800 1.000 30.00419 ?  96  GLY A CA  1 
ATOM   696  C  C   . GLY A 1 116 ? 8.22000   -23.45500 -16.38300 1.000 35.39098 ?  96  GLY A C   1 
ATOM   697  O  O   . GLY A 1 116 ? 9.34600   -23.96200 -16.35200 1.000 29.30761 ?  96  GLY A O   1 
ATOM   698  N  N   . GLU A 1 117 ? 7.98400   -22.25700 -16.91500 1.000 31.69909 ?  97  GLU A N   1 
ATOM   699  C  CA  . GLU A 1 117 ? 9.04500   -21.41300 -17.44800 1.000 30.33980 ?  97  GLU A CA  1 
ATOM   700  C  C   . GLU A 1 117 ? 9.15000   -20.06200 -16.75600 1.000 29.20282 ?  97  GLU A C   1 
ATOM   701  O  O   . GLU A 1 117 ? 10.25300  -19.52200 -16.64900 1.000 27.67902 ?  97  GLU A O   1 
ATOM   702  C  CB  . GLU A 1 117 ? 8.84300   -21.19500 -18.95600 1.000 34.45939 ?  97  GLU A CB  1 
ATOM   703  C  CG  . GLU A 1 117 ? 8.97100   -22.46600 -19.79200 1.000 43.91372 ?  97  GLU A CG  1 
ATOM   704  C  CD  . GLU A 1 117 ? 10.31500  -23.15400 -19.63200 1.000 43.83639 ?  97  GLU A CD  1 
ATOM   705  O  OE1 . GLU A 1 117 ? 11.34700  -22.45000 -19.56600 1.000 41.45175 ?  97  GLU A OE1 1 
ATOM   706  O  OE2 . GLU A 1 117 ? 10.34100  -24.40100 -19.57500 1.000 50.97204 -1 97  GLU A OE2 1 
ATOM   707  N  N   . PHE A 1 118 ? 8.03500   -19.50400 -16.28500 1.000 29.71949 ?  98  PHE A N   1 
ATOM   708  C  CA  . PHE A 1 118 ? 8.02900   -18.27400 -15.49300 1.000 21.40649 ?  98  PHE A CA  1 
ATOM   709  C  C   . PHE A 1 118 ? 8.38500   -18.63900 -14.05300 1.000 30.88746 ?  98  PHE A C   1 
ATOM   710  O  O   . PHE A 1 118 ? 7.52400   -18.82800 -13.19100 1.000 30.63921 ?  98  PHE A O   1 
ATOM   711  C  CB  . PHE A 1 118 ? 6.66700   -17.59400 -15.59000 1.000 28.65898 ?  98  PHE A CB  1 
ATOM   712  C  CG  . PHE A 1 118 ? 6.70800   -16.10200 -15.40900 1.000 29.90517 ?  98  PHE A CG  1 
ATOM   713  C  CD1 . PHE A 1 118 ? 7.56000   -15.51700 -14.48400 1.000 32.66806 ?  98  PHE A CD1 1 
ATOM   714  C  CD2 . PHE A 1 118 ? 5.88800   -15.28300 -16.16600 1.000 28.45483 ?  98  PHE A CD2 1 
ATOM   715  C  CE1 . PHE A 1 118 ? 7.59400   -14.14400 -14.31800 1.000 34.49283 ?  98  PHE A CE1 1 
ATOM   716  C  CE2 . PHE A 1 118 ? 5.91600   -13.91300 -16.00500 1.000 33.16387 ?  98  PHE A CE2 1 
ATOM   717  C  CZ  . PHE A 1 118 ? 6.77200   -13.34200 -15.07900 1.000 30.06086 ?  98  PHE A CZ  1 
ATOM   718  N  N   . THR A 1 119 ? 9.68600   -18.73200 -13.78800 1.000 23.60889 ?  99  THR A N   1 
ATOM   719  C  CA  . THR A 1 119 ? 10.19200  -19.26200 -12.53100 1.000 27.62040 ?  99  THR A CA  1 
ATOM   720  C  C   . THR A 1 119 ? 10.99800  -18.21700 -11.76800 1.000 27.82855 ?  99  THR A C   1 
ATOM   721  O  O   . THR A 1 119 ? 11.53700  -17.27300 -12.36000 1.000 26.20311 ?  99  THR A O   1 
ATOM   722  C  CB  . THR A 1 119 ? 11.07900  -20.49400 -12.77000 1.000 28.89339 ?  99  THR A CB  1 
ATOM   723  O  OG1 . THR A 1 119 ? 12.17000  -20.14900 -13.63800 1.000 24.85530 ?  99  THR A OG1 1 
ATOM   724  C  CG2 . THR A 1 119 ? 10.26900  -21.60400 -13.41300 1.000 29.92667 ?  99  THR A CG2 1 
ATOM   725  N  N   . PRO A 1 120 ? 11.09400  -18.35600 -10.44300 1.000 22.39387 ?  100 PRO A N   1 
ATOM   726  C  CA  . PRO A 1 120 ? 11.98500  -17.47200 -9.67400  1.000 23.90460 ?  100 PRO A CA  1 
ATOM   727  C  C   . PRO A 1 120 ? 13.42900  -17.51800 -10.14000 1.000 24.46602 ?  100 PRO A C   1 
ATOM   728  O  O   . PRO A 1 120 ? 14.14500  -16.51700 -10.01000 1.000 23.42273 ?  100 PRO A O   1 
ATOM   729  C  CB  . PRO A 1 120 ? 11.84300  -18.00500 -8.24400  1.000 24.07616 ?  100 PRO A CB  1 
ATOM   730  C  CG  . PRO A 1 120 ? 10.44400  -18.57600 -8.21200  1.000 18.87646 ?  100 PRO A CG  1 
ATOM   731  C  CD  . PRO A 1 120 ? 10.25800  -19.20100 -9.56700  1.000 27.68153 ?  100 PRO A CD  1 
ATOM   732  N  N   . ARG A 1 121 ? 13.88400  -18.65700 -10.66800 1.000 22.52024 ?  101 ARG A N   1 
ATOM   733  C  CA  . ARG A 1 121 ? 15.25000  -18.73400 -11.17500 1.000 25.84558 ?  101 ARG A CA  1 
ATOM   734  C  C   . ARG A 1 121 ? 15.41400  -17.88300 -12.42700 1.000 24.38392 ?  101 ARG A C   1 
ATOM   735  O  O   . ARG A 1 121 ? 16.44500  -17.22300 -12.60100 1.000 24.73489 ?  101 ARG A O   1 
ATOM   736  C  CB  . ARG A 1 121 ? 15.62800  -20.18700 -11.45700 1.000 25.24039 ?  101 ARG A CB  1 
ATOM   737  C  CG  . ARG A 1 121 ? 17.00400  -20.37300 -12.09300 1.000 27.20728 ?  101 ARG A CG  1 
ATOM   738  C  CD  . ARG A 1 121 ? 18.05700  -20.73800 -11.05600 1.000 34.14751 ?  101 ARG A CD  1 
ATOM   739  N  NE  . ARG A 1 121 ? 17.59300  -21.78400 -10.15100 1.000 26.64457 ?  101 ARG A NE  1 
ATOM   740  C  CZ  . ARG A 1 121 ? 17.83500  -23.07800 -10.30800 1.000 26.21862 ?  101 ARG A CZ  1 
ATOM   741  N  NH1 . ARG A 1 121 ? 18.55200  -23.52900 -11.32400 1.000 24.93573 ?  101 ARG A NH1 1 
ATOM   742  N  NH2 . ARG A 1 121 ? 17.33000  -23.94500 -9.43200  1.000 24.36603 ?  101 ARG A NH2 1 
ATOM   743  N  N   . ARG A 1 122 ? 14.40800  -17.88300 -13.30800 1.000 26.94066 ?  102 ARG A N   1 
ATOM   744  C  CA  . ARG A 1 122 ? 14.44600  -17.00200 -14.47300 1.000 22.30523 ?  102 ARG A CA  1 
ATOM   745  C  C   . ARG A 1 122 ? 14.60400  -15.54700 -14.05300 1.000 24.55225 ?  102 ARG A C   1 
ATOM   746  O  O   . ARG A 1 122 ? 15.42500  -14.81200 -14.61200 1.000 20.51485 ?  102 ARG A O   1 
ATOM   747  C  CB  . ARG A 1 122 ? 13.18300  -17.16000 -15.31800 1.000 27.08375 ?  102 ARG A CB  1 
ATOM   748  C  CG  . ARG A 1 122 ? 13.32500  -16.56000 -16.71400 1.000 28.92899 ?  102 ARG A CG  1 
ATOM   749  C  CD  . ARG A 1 122 ? 12.12800  -16.87000 -17.61000 1.000 26.10020 ?  102 ARG A CD  1 
ATOM   750  N  NE  . ARG A 1 122 ? 12.23700  -18.16100 -18.28000 1.000 27.62238 ?  102 ARG A NE  1 
ATOM   751  C  CZ  . ARG A 1 122 ? 12.90200  -18.37000 -19.40800 1.000 31.66526 ?  102 ARG A CZ  1 
ATOM   752  N  NH1 . ARG A 1 122 ? 13.60500  -17.40700 -19.98600 1.000 26.43222 ?  102 ARG A NH1 1 
ATOM   753  N  NH2 . ARG A 1 122 ? 12.86800  -19.57600 -19.96700 1.000 31.03709 ?  102 ARG A NH2 1 
ATOM   754  N  N   . VAL A 1 123 ? 13.81900  -15.11100 -13.06700 1.000 20.82058 ?  103 VAL A N   1 
ATOM   755  C  CA  . VAL A 1 123 ? 13.90500  -13.72900 -12.61000 1.000 23.63401 ?  103 VAL A CA  1 
ATOM   756  C  C   . VAL A 1 123 ? 15.27300  -13.46000 -11.99900 1.000 22.51110 ?  103 VAL A C   1 
ATOM   757  O  O   . VAL A 1 123 ? 15.91400  -12.44500 -12.29300 1.000 20.61249 ?  103 VAL A O   1 
ATOM   758  C  CB  . VAL A 1 123 ? 12.77000  -13.41800 -11.61700 1.000 21.78089 ?  103 VAL A CB  1 
ATOM   759  C  CG1 . VAL A 1 123 ? 12.95700  -12.03200 -11.02000 1.000 26.84334 ?  103 VAL A CG1 1 
ATOM   760  C  CG2 . VAL A 1 123 ? 11.41900  -13.52400 -12.31400 1.000 21.95787 ?  103 VAL A CG2 1 
ATOM   761  N  N   . HIS A 1 124 ? 15.73800  -14.37300 -11.13900 1.000 22.11680 ?  104 HIS A N   1 
ATOM   762  C  CA  . HIS A 1 124 ? 17.05300  -14.23000 -10.52200 1.000 29.60880 ?  104 HIS A CA  1 
ATOM   763  C  C   . HIS A 1 124 ? 18.14000  -14.03900 -11.56900 1.000 23.08163 ?  104 HIS A C   1 
ATOM   764  O  O   . HIS A 1 124 ? 19.02100  -13.18600 -11.41600 1.000 24.10662 ?  104 HIS A O   1 
ATOM   765  C  CB  . HIS A 1 124 ? 17.35600  -15.45600 -9.65900  1.000 25.43110 ?  104 HIS A CB  1 
ATOM   766  C  CG  . HIS A 1 124 ? 18.74800  -15.48200 -9.10800  1.000 27.45201 ?  104 HIS A CG  1 
ATOM   767  N  ND1 . HIS A 1 124 ? 19.11300  -14.79300 -7.97100  1.000 33.47313 ?  104 HIS A ND1 1 
ATOM   768  C  CD2 . HIS A 1 124 ? 19.86600  -16.11500 -9.53900  1.000 33.38033 ?  104 HIS A CD2 1 
ATOM   769  C  CE1 . HIS A 1 124 ? 20.39400  -15.00200 -7.72400  1.000 30.42676 ?  104 HIS A CE1 1 
ATOM   770  N  NE2 . HIS A 1 124 ? 20.87500  -15.80000 -8.66100  1.000 30.68428 ?  104 HIS A NE2 1 
ATOM   771  N  N   . GLU A 1 125 ? 18.08800  -14.81800 -12.64600 1.000 22.63033 ?  105 GLU A N   1 
ATOM   772  C  CA  . GLU A 1 125 ? 19.13600  -14.76400 -13.65900 1.000 24.19091 ?  105 GLU A CA  1 
ATOM   773  C  C   . GLU A 1 125 ? 19.04900  -13.51400 -14.52600 1.000 21.14861 ?  105 GLU A C   1 
ATOM   774  O  O   . GLU A 1 125 ? 20.01500  -13.19700 -15.22700 1.000 20.53214 ?  105 GLU A O   1 
ATOM   775  C  CB  . GLU A 1 125 ? 19.07000  -16.03500 -14.50900 1.000 24.29131 ?  105 GLU A CB  1 
ATOM   776  C  CG  . GLU A 1 125 ? 19.44100  -17.27200 -13.69500 1.000 27.96031 ?  105 GLU A CG  1 
ATOM   777  C  CD  . GLU A 1 125 ? 19.32900  -18.57200 -14.46200 1.000 32.61984 ?  105 GLU A CD  1 
ATOM   778  O  OE1 . GLU A 1 125 ? 18.60100  -18.61500 -15.47600 1.000 41.27257 ?  105 GLU A OE1 1 
ATOM   779  O  OE2 . GLU A 1 125 ? 19.96300  -19.56200 -14.03300 1.000 35.30204 -1 105 GLU A OE2 1 
ATOM   780  N  N   . LEU A 1 126 ? 17.93200  -12.79000 -14.47800 1.000 15.83468 ?  106 LEU A N   1 
ATOM   781  C  CA  . LEU A 1 126 ? 17.78900  -11.53300 -15.19900 1.000 15.36159 ?  106 LEU A CA  1 
ATOM   782  C  C   . LEU A 1 126 ? 18.27800  -10.33600 -14.39900 1.000 13.91809 ?  106 LEU A C   1 
ATOM   783  O  O   . LEU A 1 126 ? 18.52500  -9.27900  -14.99100 1.000 14.85029 ?  106 LEU A O   1 
ATOM   784  C  CB  . LEU A 1 126 ? 16.31600  -11.30700 -15.57100 1.000 17.78976 ?  106 LEU A CB  1 
ATOM   785  C  CG  . LEU A 1 126 ? 15.76900  -12.11900 -16.74400 1.000 24.19081 ?  106 LEU A CG  1 
ATOM   786  C  CD1 . LEU A 1 126 ? 14.24400  -12.03700 -16.79400 1.000 27.54500 ?  106 LEU A CD1 1 
ATOM   787  C  CD2 . LEU A 1 126 ? 16.38500  -11.66200 -18.06300 1.000 25.41066 ?  106 LEU A CD2 1 
ATOM   788  N  N   . VAL A 1 127 ? 18.42300  -10.48800 -13.07600 1.000 15.73579 ?  107 VAL A N   1 
ATOM   789  C  CA  . VAL A 1 127 ? 18.73100  -9.34100  -12.21500 1.000 18.06362 ?  107 VAL A CA  1 
ATOM   790  C  C   . VAL A 1 127 ? 19.98700  -8.59000  -12.64500 1.000 18.39822 ?  107 VAL A C   1 
ATOM   791  O  O   . VAL A 1 127 ? 19.95200  -7.35000  -12.68500 1.000 17.26416 ?  107 VAL A O   1 
ATOM   792  C  CB  . VAL A 1 127 ? 18.79800  -9.79100  -10.74400 1.000 21.98596 ?  107 VAL A CB  1 
ATOM   793  C  CG1 . VAL A 1 127 ? 19.37400  -8.68500  -9.87100  1.000 18.44483 ?  107 VAL A CG1 1 
ATOM   794  C  CG2 . VAL A 1 127 ? 17.41500  -10.18200 -10.25100 1.000 16.65329 ?  107 VAL A CG2 1 
ATOM   795  N  N   . PRO A 1 128 ? 21.11400  -9.24200  -12.95300 1.000 16.65646 ?  108 PRO A N   1 
ATOM   796  C  CA  . PRO A 1 128 ? 22.28300  -8.44800  -13.37500 1.000 15.25943 ?  108 PRO A CA  1 
ATOM   797  C  C   . PRO A 1 128 ? 22.02000  -7.61200  -14.61700 1.000 17.94265 ?  108 PRO A C   1 
ATOM   798  O  O   . PRO A 1 128 ? 22.47400  -6.46400  -14.69500 1.000 16.32272 ?  108 PRO A O   1 
ATOM   799  C  CB  . PRO A 1 128 ? 23.36300  -9.51300  -13.60800 1.000 21.77999 ?  108 PRO A CB  1 
ATOM   800  C  CG  . PRO A 1 128 ? 22.96200  -10.62900 -12.71900 1.000 22.04181 ?  108 PRO A CG  1 
ATOM   801  C  CD  . PRO A 1 128 ? 21.46500  -10.66900 -12.81500 1.000 21.67901 ?  108 PRO A CD  1 
ATOM   802  N  N   . ALA A 1 129 ? 21.26300  -8.14300  -15.58200 1.000 17.91921 ?  109 ALA A N   1 
ATOM   803  C  CA  . ALA A 1 129 ? 20.91700  -7.35000  -16.75900 1.000 17.44937 ?  109 ALA A CA  1 
ATOM   804  C  C   . ALA A 1 129 ? 19.96400  -6.21300  -16.40300 1.000 16.77771 ?  109 ALA A C   1 
ATOM   805  O  O   . ALA A 1 129 ? 20.10700  -5.09400  -16.91400 1.000 14.66687 ?  109 ALA A O   1 
ATOM   806  C  CB  . ALA A 1 129 ? 20.31500  -8.24700  -17.84100 1.000 19.53948 ?  109 ALA A CB  1 
ATOM   807  N  N   . ILE A 1 130 ? 18.99200  -6.47200  -15.52200 1.000 13.22768 ?  110 ILE A N   1 
ATOM   808  C  CA  . ILE A 1 130 ? 18.07400  -5.41500  -15.10400 1.000 14.84345 ?  110 ILE A CA  1 
ATOM   809  C  C   . ILE A 1 130 ? 18.83300  -4.27500  -14.43900 1.000 14.16896 ?  110 ILE A C   1 
ATOM   810  O  O   . ILE A 1 130 ? 18.60600  -3.09700  -14.73500 1.000 13.89907 ?  110 ILE A O   1 
ATOM   811  C  CB  . ILE A 1 130 ? 16.98200  -5.97500  -14.17300 1.000 14.64102 ?  110 ILE A CB  1 
ATOM   812  C  CG1 . ILE A 1 130 ? 16.12200  -7.00800  -14.90600 1.000 14.55070 ?  110 ILE A CG1 1 
ATOM   813  C  CG2 . ILE A 1 130 ? 16.15700  -4.83800  -13.58200 1.000 16.15216 ?  110 ILE A CG2 1 
ATOM   814  C  CD1 . ILE A 1 130 ? 15.13500  -7.74600  -13.99200 1.000 13.59173 ?  110 ILE A CD1 1 
ATOM   815  N  N   . GLU A 1 131 ? 19.74800  -4.60800  -13.52600 1.000 16.59393 ?  111 GLU A N   1 
ATOM   816  C  CA  . GLU A 1 131 ? 20.45100  -3.56200  -12.79400 1.000 17.46668 ?  111 GLU A CA  1 
ATOM   817  C  C   . GLU A 1 131 ? 21.34200  -2.74400  -13.72000 1.000 15.54111 ?  111 GLU A C   1 
ATOM   818  O  O   . GLU A 1 131 ? 21.36100  -1.51200  -13.63300 1.000 14.02081 ?  111 GLU A O   1 
ATOM   819  C  CB  . GLU A 1 131 ? 21.24500  -4.17500  -11.64000 1.000 18.01753 ?  111 GLU A CB  1 
ATOM   820  C  CG  . GLU A 1 131 ? 20.32800  -4.89200  -10.65200 1.000 19.23194 ?  111 GLU A CG  1 
ATOM   821  C  CD  . GLU A 1 131 ? 20.99600  -5.26900  -9.35000  1.000 33.77218 ?  111 GLU A CD  1 
ATOM   822  O  OE1 . GLU A 1 131 ? 22.20700  -5.57500  -9.35400  1.000 39.26666 ?  111 GLU A OE1 1 
ATOM   823  O  OE2 . GLU A 1 131 ? 20.29000  -5.27500  -8.31800  1.000 45.68991 -1 111 GLU A OE2 1 
ATOM   824  N  N   . ALA A 1 132 ? 22.05100  -3.40400  -14.63900 1.000 14.37626 ?  112 ALA A N   1 
ATOM   825  C  CA  . ALA A 1 132 ? 22.86700  -2.66900  -15.60200 1.000 18.78220 ?  112 ALA A CA  1 
ATOM   826  C  C   . ALA A 1 132 ? 22.01300  -1.77800  -16.50100 1.000 17.93124 ?  112 ALA A C   1 
ATOM   827  O  O   . ALA A 1 132 ? 22.39400  -0.64100  -16.79900 1.000 15.37535 ?  112 ALA A O   1 
ATOM   828  C  CB  . ALA A 1 132 ? 23.69200  -3.64200  -16.44400 1.000 20.35815 ?  112 ALA A CB  1 
ATOM   829  N  N   . ALA A 1 133 ? 20.85600  -2.27800  -16.94800 1.000 16.82440 ?  113 ALA A N   1 
ATOM   830  C  CA  . ALA A 1 133 ? 19.99300  -1.46800  -17.80500 1.000 15.67649 ?  113 ALA A CA  1 
ATOM   831  C  C   . ALA A 1 133 ? 19.52600  -0.20800  -17.08700 1.000 13.24362 ?  113 ALA A C   1 
ATOM   832  O  O   . ALA A 1 133 ? 19.47700  0.87400   -17.68500 1.000 15.63570 ?  113 ALA A O   1 
ATOM   833  C  CB  . ALA A 1 133 ? 18.79800  -2.29200  -18.28100 1.000 18.81658 ?  113 ALA A CB  1 
ATOM   834  N  N   . ALA A 1 134 ? 19.17800  -0.32700  -15.80300 1.000 14.75727 ?  114 ALA A N   1 
ATOM   835  C  CA  . ALA A 1 134 ? 18.76700  0.84400   -15.03300 1.000 15.60766 ?  114 ALA A CA  1 
ATOM   836  C  C   . ALA A 1 134 ? 19.89400  1.86500   -14.92500 1.000 12.61963 ?  114 ALA A C   1 
ATOM   837  O  O   . ALA A 1 134 ? 19.67100  3.06800   -15.11100 1.000 17.03042 ?  114 ALA A O   1 
ATOM   838  C  CB  . ALA A 1 134 ? 18.29100  0.41400   -13.64300 1.000 13.12150 ?  114 ALA A CB  1 
ATOM   839  N  N   . ARG A 1 135 ? 21.11500  1.40900   -14.62200 1.000 19.02706 ?  115 ARG A N   1 
ATOM   840  C  CA  . ARG A 1 135 ? 22.24000  2.33900   -14.54900 1.000 14.69288 ?  115 ARG A CA  1 
ATOM   841  C  C   . ARG A 1 135 ? 22.47900  3.01800   -15.89200 1.000 15.11549 ?  115 ARG A C   1 
ATOM   842  O  O   . ARG A 1 135 ? 22.67700  4.23400   -15.95300 1.000 16.09322 ?  115 ARG A O   1 
ATOM   843  C  CB  . ARG A 1 135 ? 23.51300  1.61400   -14.09700 1.000 14.23179 ?  115 ARG A CB  1 
ATOM   844  C  CG  . ARG A 1 135 ? 23.46300  1.04500   -12.68800 1.000 15.97172 ?  115 ARG A CG  1 
ATOM   845  C  CD  . ARG A 1 135 ? 24.84400  0.56700   -12.24000 1.000 18.18787 ?  115 ARG A CD  1 
ATOM   846  N  NE  . ARG A 1 135 ? 25.30000  -0.57000  -13.02900 1.000 13.77745 ?  115 ARG A NE  1 
ATOM   847  C  CZ  . ARG A 1 135 ? 25.10500  -1.83800  -12.69600 1.000 14.98353 ?  115 ARG A CZ  1 
ATOM   848  N  NH1 . ARG A 1 135 ? 24.42500  -2.17000  -11.61100 1.000 15.73704 ?  115 ARG A NH1 1 
ATOM   849  N  NH2 . ARG A 1 135 ? 25.58700  -2.79800  -13.48300 1.000 18.13975 ?  115 ARG A NH2 1 
ATOM   850  N  N   . GLU A 1 136 ? 22.44200  2.24400   -16.98000 1.000 15.18096 ?  116 GLU A N   1 
ATOM   851  C  CA  . GLU A 1 136 ? 22.70700  2.79400   -18.30700 1.000 14.14211 ?  116 GLU A CA  1 
ATOM   852  C  C   . GLU A 1 136 ? 21.64700  3.80400   -18.72300 1.000 19.84933 ?  116 GLU A C   1 
ATOM   853  O  O   . GLU A 1 136 ? 21.96500  4.84100   -19.31900 1.000 18.86775 ?  116 GLU A O   1 
ATOM   854  C  CB  . GLU A 1 136 ? 22.78500  1.65200   -19.31800 1.000 15.42331 ?  116 GLU A CB  1 
ATOM   855  C  CG  . GLU A 1 136 ? 24.02900  0.80700   -19.14700 1.000 20.75430 ?  116 GLU A CG  1 
ATOM   856  C  CD  . GLU A 1 136 ? 23.86400  -0.59100  -19.69200 1.000 23.41452 ?  116 GLU A CD  1 
ATOM   857  O  OE1 . GLU A 1 136 ? 22.91900  -0.82100  -20.47600 1.000 21.07979 ?  116 GLU A OE1 1 
ATOM   858  O  OE2 . GLU A 1 136 ? 24.68800  -1.45900  -19.33400 1.000 25.07646 -1 116 GLU A OE2 1 
ATOM   859  N  N   . LEU A 1 137 ? 20.37800  3.50700   -18.44200 1.000 15.84473 ?  117 LEU A N   1 
ATOM   860  C  CA  . LEU A 1 137 ? 19.30500  4.41800   -18.82400 1.000 17.85784 ?  117 LEU A CA  1 
ATOM   861  C  C   . LEU A 1 137 ? 19.41300  5.73300   -18.06600 1.000 15.85542 ?  117 LEU A C   1 
ATOM   862  O  O   . LEU A 1 137 ? 19.35200  6.81200   -18.66400 1.000 19.27126 ?  117 LEU A O   1 
ATOM   863  C  CB  . LEU A 1 137 ? 17.95000  3.75100   -18.58400 1.000 16.21907 ?  117 LEU A CB  1 
ATOM   864  C  CG  . LEU A 1 137 ? 17.56500  2.75700   -19.68000 1.000 18.86450 ?  117 LEU A CG  1 
ATOM   865  C  CD1 . LEU A 1 137 ? 16.35900  1.91700   -19.26600 1.000 17.20468 ?  117 LEU A CD1 1 
ATOM   866  C  CD2 . LEU A 1 137 ? 17.29000  3.49600   -20.98900 1.000 22.17781 ?  117 LEU A CD2 1 
ATOM   867  N  N   . LEU A 1 138 ? 19.59600  5.65900   -16.74500 1.000 14.09648 ?  118 LEU A N   1 
ATOM   868  C  CA  . LEU A 1 138 ? 19.73600  6.87400   -15.94800 1.000 19.64153 ?  118 LEU A CA  1 
ATOM   869  C  C   . LEU A 1 138 ? 20.97900  7.65800   -16.35100 1.000 18.38559 ?  118 LEU A C   1 
ATOM   870  O  O   . LEU A 1 138 ? 20.96700  8.89400   -16.36700 1.000 25.36616 ?  118 LEU A O   1 
ATOM   871  C  CB  . LEU A 1 138 ? 19.77800  6.51900   -14.46200 1.000 18.72801 ?  118 LEU A CB  1 
ATOM   872  C  CG  . LEU A 1 138 ? 19.36600  7.61200   -13.47600 1.000 21.26344 ?  118 LEU A CG  1 
ATOM   873  C  CD1 . LEU A 1 138 ? 17.90700  7.99700   -13.69100 1.000 17.27559 ?  118 LEU A CD1 1 
ATOM   874  C  CD2 . LEU A 1 138 ? 19.60200  7.14500   -12.04900 1.000 18.09174 ?  118 LEU A CD2 1 
ATOM   875  N  N   . ALA A 1 139 ? 22.06700  6.95400   -16.67500 1.000 25.40614 ?  119 ALA A N   1 
ATOM   876  C  CA  . ALA A 1 139 ? 23.29600  7.61900   -17.09000 1.000 20.83656 ?  119 ALA A CA  1 
ATOM   877  C  C   . ALA A 1 139 ? 23.14000  8.35900   -18.41100 1.000 25.02135 ?  119 ALA A C   1 
ATOM   878  O  O   . ALA A 1 139 ? 23.91900  9.27700   -18.68600 1.000 30.25856 ?  119 ALA A O   1 
ATOM   879  C  CB  . ALA A 1 139 ? 24.43400  6.60400   -17.19600 1.000 23.36532 ?  119 ALA A CB  1 
ATOM   880  N  N   . GLY A 1 140 ? 22.16500  7.97800   -19.23400 1.000 28.64849 ?  120 GLY A N   1 
ATOM   881  C  CA  . GLY A 1 140 ? 21.87400  8.71400   -20.44500 1.000 28.85436 ?  120 GLY A CA  1 
ATOM   882  C  C   . GLY A 1 140 ? 21.08300  9.97900   -20.23500 1.000 25.89882 ?  120 GLY A C   1 
ATOM   883  O  O   . GLY A 1 140 ? 20.77200  10.68000  -21.19900 1.000 26.87706 ?  120 GLY A O   1 
ATOM   884  N  N   . LEU A 1 141 ? 20.74500  10.29300  -18.99400 1.000 27.13481 ?  121 LEU A N   1 
ATOM   885  C  CA  . LEU A 1 141 ? 19.95900  11.47400  -18.66600 1.000 28.25763 ?  121 LEU A CA  1 
ATOM   886  C  C   . LEU A 1 141 ? 20.86300  12.53900  -18.07200 1.000 27.41696 ?  121 LEU A C   1 
ATOM   887  O  O   . LEU A 1 141 ? 21.70800  12.22200  -17.21700 1.000 28.81717 ?  121 LEU A O   1 
ATOM   888  C  CB  . LEU A 1 141 ? 18.84900  11.11500  -17.68000 1.000 24.23027 ?  121 LEU A CB  1 
ATOM   889  C  CG  . LEU A 1 141 ? 17.75700  10.19000  -18.23500 1.000 22.96864 ?  121 LEU A CG  1 
ATOM   890  C  CD1 . LEU A 1 141 ? 16.65000  9.96300   -17.20900 1.000 14.94000 ?  121 LEU A CD1 1 
ATOM   891  C  CD2 . LEU A 1 141 ? 17.18500  10.72900  -19.53800 1.000 21.59913 ?  121 LEU A CD2 1 
ATOM   892  N  N   . PRO A 1 142 ? 20.73800  13.79300  -18.49700 1.000 23.43573 ?  122 PRO A N   1 
ATOM   893  C  CA  . PRO A 1 142 ? 21.66700  14.82700  -18.02800 1.000 28.54292 ?  122 PRO A CA  1 
ATOM   894  C  C   . PRO A 1 142 ? 21.40500  15.21100  -16.58000 1.000 31.94785 ?  122 PRO A C   1 
ATOM   895  O  O   . PRO A 1 142 ? 20.31900  15.00200  -16.03300 1.000 32.24504 ?  122 PRO A O   1 
ATOM   896  C  CB  . PRO A 1 142 ? 21.39000  16.00200  -18.96800 1.000 29.85452 ?  122 PRO A CB  1 
ATOM   897  C  CG  . PRO A 1 142 ? 19.96500  15.80200  -19.38200 1.000 34.17153 ?  122 PRO A CG  1 
ATOM   898  C  CD  . PRO A 1 142 ? 19.80300  14.31000  -19.51000 1.000 28.19193 ?  122 PRO A CD  1 
ATOM   899  N  N   . SER A 1 143 ? 22.43200  15.78500  -15.95800 1.000 25.27203 ?  123 SER A N   1 
ATOM   900  C  CA  . SER A 1 143 ? 22.34000  16.31500  -14.60500 1.000 28.59835 ?  123 SER A CA  1 
ATOM   901  C  C   . SER A 1 143 ? 22.12200  17.82300  -14.63600 1.000 37.56523 ?  123 SER A C   1 
ATOM   902  O  O   . SER A 1 143 ? 22.55400  18.51400  -15.56200 1.000 36.94469 ?  123 SER A O   1 
ATOM   903  C  CB  . SER A 1 143 ? 23.59900  16.00500  -13.79800 1.000 29.88854 ?  123 SER A CB  1 
ATOM   904  O  OG  . SER A 1 143 ? 23.94900  14.63800  -13.88400 1.000 37.34596 ?  123 SER A OG  1 
ATOM   905  N  N   . GLY A 1 144 ? 21.45100  18.32700  -13.60500 1.000 39.85249 ?  124 GLY A N   1 
ATOM   906  C  CA  . GLY A 1 144 ? 21.23900  19.76000  -13.47100 1.000 39.29314 ?  124 GLY A CA  1 
ATOM   907  C  C   . GLY A 1 144 ? 20.31300  20.36800  -14.50400 1.000 42.19141 ?  124 GLY A C   1 
ATOM   908  O  O   . GLY A 1 144 ? 20.54400  21.49600  -14.95300 1.000 46.52304 ?  124 GLY A O   1 
ATOM   909  N  N   . GLU A 1 145 ? 19.40100  19.55100  -14.99900 1.000 35.52377 ?  125 GLU A N   1 
ATOM   910  C  CA  . GLU A 1 145 ? 18.49200  19.97600  -16.07800 1.000 37.85127 ?  125 GLU A CA  1 
ATOM   911  C  C   . GLU A 1 145 ? 17.18400  19.21500  -15.87600 1.000 29.56207 ?  125 GLU A C   1 
ATOM   912  O  O   . GLU A 1 145 ? 17.22300  18.01200  -15.66000 1.000 31.38198 ?  125 GLU A O   1 
ATOM   913  C  CB  . GLU A 1 145 ? 19.13800  19.61600  -17.40900 1.000 33.96982 ?  125 GLU A CB  1 
ATOM   914  C  CG  . GLU A 1 145 ? 18.23800  19.72200  -18.62000 1.000 43.14110 ?  125 GLU A CG  1 
ATOM   915  C  CD  . GLU A 1 145 ? 19.01300  19.47500  -19.90300 1.000 49.52671 ?  125 GLU A CD  1 
ATOM   916  O  OE1 . GLU A 1 145 ? 20.18600  19.88200  -19.96300 1.000 46.11422 ?  125 GLU A OE1 1 
ATOM   917  O  OE2 . GLU A 1 145 ? 18.45300  18.86100  -20.82500 1.000 56.24270 -1 125 GLU A OE2 1 
ATOM   918  N  N   . PRO A 1 146 ? 16.02800  19.89000  -15.92700 1.000 39.08413 ?  126 PRO A N   1 
ATOM   919  C  CA  . PRO A 1 146 ? 14.75700  19.21000  -15.76800 1.000 29.82804 ?  126 PRO A CA  1 
ATOM   920  C  C   . PRO A 1 146 ? 14.66300  18.00200  -16.71300 1.000 33.11853 ?  126 PRO A C   1 
ATOM   921  O  O   . PRO A 1 146 ? 14.81500  18.17800  -17.90000 1.000 28.42052 ?  126 PRO A O   1 
ATOM   922  C  CB  . PRO A 1 146 ? 13.73600  20.28900  -16.12400 1.000 35.09887 ?  126 PRO A CB  1 
ATOM   923  C  CG  . PRO A 1 146 ? 14.53100  21.37800  -16.80300 1.000 43.01718 ?  126 PRO A CG  1 
ATOM   924  C  CD  . PRO A 1 146 ? 15.88400  21.32300  -16.13900 1.000 39.91087 ?  126 PRO A CD  1 
ATOM   925  N  N   . VAL A 1 147 ? 14.41300  16.81800  -16.14600 1.000 28.79906 ?  127 VAL A N   1 
ATOM   926  C  CA  . VAL A 1 147 ? 14.27000  15.57100  -16.94700 1.000 24.00819 ?  127 VAL A CA  1 
ATOM   927  C  C   . VAL A 1 147 ? 12.97500  14.87100  -16.51100 1.000 23.08861 ?  127 VAL A C   1 
ATOM   928  O  O   . VAL A 1 147 ? 12.70700  14.85800  -15.31400 1.000 25.24763 ?  127 VAL A O   1 
ATOM   929  C  CB  . VAL A 1 147 ? 15.49400  14.65300  -16.77500 1.000 25.13426 ?  127 VAL A CB  1 
ATOM   930  C  CG1 . VAL A 1 147 ? 16.75900  15.29800  -17.31200 1.000 30.42010 ?  127 VAL A CG1 1 
ATOM   931  C  CG2 . VAL A 1 147 ? 15.68600  14.22400  -15.33200 1.000 27.91213 ?  127 VAL A CG2 1 
ATOM   932  N  N   . ASP A 1 148 ? 12.23100  14.30700  -17.46200 1.000 24.37729 ?  128 ASP A N   1 
ATOM   933  C  CA  . ASP A 1 148 ? 11.01300  13.59400  -17.09800 1.000 25.55973 ?  128 ASP A CA  1 
ATOM   934  C  C   . ASP A 1 148 ? 11.37000  12.16500  -16.72100 1.000 20.38553 ?  128 ASP A C   1 
ATOM   935  O  O   . ASP A 1 148 ? 11.84500  11.39400  -17.56200 1.000 26.14881 ?  128 ASP A O   1 
ATOM   936  C  CB  . ASP A 1 148 ? 9.99500   13.61100  -18.23500 1.000 25.98081 ?  128 ASP A CB  1 
ATOM   937  C  CG  . ASP A 1 148 ? 8.80100   12.71200  -17.95600 1.000 29.99166 ?  128 ASP A CG  1 
ATOM   938  O  OD1 . ASP A 1 148 ? 8.43500   12.58400  -16.77300 1.000 27.52908 -1 128 ASP A OD1 1 
ATOM   939  O  OD2 . ASP A 1 148 ? 8.20900   12.15800  -18.90800 1.000 26.61243 -1 128 ASP A OD2 1 
ATOM   940  N  N   . LEU A 1 149 ? 11.13500  11.82500  -15.45100 1.000 22.93336 ?  129 LEU A N   1 
ATOM   941  C  CA  . LEU A 1 149 ? 11.44300  10.48900  -14.95200 1.000 20.33552 ?  129 LEU A CA  1 
ATOM   942  C  C   . LEU A 1 149 ? 10.66600  9.41400   -15.70100 1.000 18.35249 ?  129 LEU A C   1 
ATOM   943  O  O   . LEU A 1 149 ? 11.18600  8.31700   -15.92700 1.000 20.69903 ?  129 LEU A O   1 
ATOM   944  C  CB  . LEU A 1 149 ? 11.14800  10.41900  -13.45200 1.000 24.50810 ?  129 LEU A CB  1 
ATOM   945  C  CG  . LEU A 1 149 ? 11.33800  9.07300   -12.73500 1.000 37.49425 ?  129 LEU A CG  1 
ATOM   946  N  N   . ILE A 1 150 ? 9.42000   9.70400   -16.08600 1.000 21.54951 ?  130 ILE A N   1 
ATOM   947  C  CA  . ILE A 1 150 ? 8.58300   8.68900   -16.72900 1.000 18.97364 ?  130 ILE A CA  1 
ATOM   948  C  C   . ILE A 1 150 ? 9.13400   8.32000   -18.10100 1.000 19.78352 ?  130 ILE A C   1 
ATOM   949  O  O   . ILE A 1 150 ? 9.47700   7.16100   -18.35700 1.000 20.03741 ?  130 ILE A O   1 
ATOM   950  C  CB  . ILE A 1 150 ? 7.12400   9.16200   -16.82400 1.000 24.51301 ?  130 ILE A CB  1 
ATOM   951  C  CG1 . ILE A 1 150 ? 6.68200   9.81100   -15.51100 1.000 20.88306 ?  130 ILE A CG1 1 
ATOM   952  C  CG2 . ILE A 1 150 ? 6.22000   8.00800   -17.22700 1.000 25.24940 ?  130 ILE A CG2 1 
ATOM   953  C  CD1 . ILE A 1 150 ? 6.54300   8.83200   -14.36200 1.000 23.02924 ?  130 ILE A CD1 1 
ATOM   954  N  N   . ALA A 1 151 ? 9.21500   9.29500   -19.00900 1.000 17.29319 ?  131 ALA A N   1 
ATOM   955  C  CA  . ALA A 1 151 ? 9.67400   8.98000   -20.35800 1.000 18.07262 ?  131 ALA A CA  1 
ATOM   956  C  C   . ALA A 1 151 ? 11.15700  8.64600   -20.39900 1.000 18.08684 ?  131 ALA A C   1 
ATOM   957  O  O   . ALA A 1 151 ? 11.59000  7.92100   -21.29900 1.000 18.18006 ?  131 ALA A O   1 
ATOM   958  C  CB  . ALA A 1 151 ? 9.37900   10.13900  -21.31100 1.000 28.62501 ?  131 ALA A CB  1 
ATOM   959  N  N   . GLY A 1 152 ? 11.93600  9.13800   -19.44300 1.000 24.03457 ?  132 GLY A N   1 
ATOM   960  C  CA  . GLY A 1 152 ? 13.37000  8.94500   -19.48300 1.000 20.53796 ?  132 GLY A CA  1 
ATOM   961  C  C   . GLY A 1 152 ? 13.87200  7.71200   -18.76100 1.000 22.15959 ?  132 GLY A C   1 
ATOM   962  O  O   . GLY A 1 152 ? 14.95200  7.20500   -19.07600 1.000 19.94817 ?  132 GLY A O   1 
ATOM   963  N  N   . PHE A 1 153 ? 13.10200  7.20800   -17.79800 1.000 19.28191 ?  133 PHE A N   1 
ATOM   964  C  CA  . PHE A 1 153 ? 13.60000  6.12600   -16.95700 1.000 14.82980 ?  133 PHE A CA  1 
ATOM   965  C  C   . PHE A 1 153 ? 12.52200  5.11300   -16.58800 1.000 17.98664 ?  133 PHE A C   1 
ATOM   966  O  O   . PHE A 1 153 ? 12.65800  3.91700   -16.87800 1.000 17.04768 ?  133 PHE A O   1 
ATOM   967  C  CB  . PHE A 1 153 ? 14.21800  6.70800   -15.68700 1.000 16.63017 ?  133 PHE A CB  1 
ATOM   968  C  CG  . PHE A 1 153 ? 14.95200  5.69900   -14.85900 1.000 20.70218 ?  133 PHE A CG  1 
ATOM   969  C  CD1 . PHE A 1 153 ? 15.92300  4.89000   -15.43200 1.000 18.46146 ?  133 PHE A CD1 1 
ATOM   970  C  CD2 . PHE A 1 153 ? 14.67200  5.55400   -13.51200 1.000 19.62446 ?  133 PHE A CD2 1 
ATOM   971  C  CE1 . PHE A 1 153 ? 16.60400  3.95600   -14.67300 1.000 17.05419 ?  133 PHE A CE1 1 
ATOM   972  C  CE2 . PHE A 1 153 ? 15.36000  4.61600   -12.74300 1.000 23.92710 ?  133 PHE A CE2 1 
ATOM   973  C  CZ  . PHE A 1 153 ? 16.31900  3.81700   -13.32900 1.000 14.08170 ?  133 PHE A CZ  1 
ATOM   974  N  N   . ALA A 1 154 ? 11.44800  5.58400   -15.95000 1.000 15.80461 ?  134 ALA A N   1 
ATOM   975  C  CA  . ALA A 1 154 ? 10.44700  4.67000   -15.40600 1.000 15.27594 ?  134 ALA A CA  1 
ATOM   976  C  C   . ALA A 1 154 ? 9.73200   3.88500   -16.49500 1.000 14.77758 ?  134 ALA A C   1 
ATOM   977  O  O   . ALA A 1 154 ? 9.24900   2.78000   -16.23500 1.000 16.90886 ?  134 ALA A O   1 
ATOM   978  C  CB  . ALA A 1 154 ? 9.43800   5.43600   -14.55100 1.000 15.03442 ?  134 ALA A CB  1 
ATOM   979  N  N   . ALA A 1 155 ? 9.63600   4.42600   -17.70600 1.000 15.46796 ?  135 ALA A N   1 
ATOM   980  C  CA  . ALA A 1 155 ? 9.03300   3.65400   -18.78600 1.000 17.21630 ?  135 ALA A CA  1 
ATOM   981  C  C   . ALA A 1 155 ? 10.08000  2.85600   -19.56500 1.000 13.92378 ?  135 ALA A C   1 
ATOM   982  O  O   . ALA A 1 155 ? 9.85900   1.66800   -19.83400 1.000 17.93102 ?  135 ALA A O   1 
ATOM   983  C  CB  . ALA A 1 155 ? 8.23200   4.56600   -19.72600 1.000 17.42954 ?  135 ALA A CB  1 
ATOM   984  N  N   . PRO A 1 156 ? 11.22200  3.44600   -19.95000 1.000 14.58613 ?  136 PRO A N   1 
ATOM   985  C  CA  . PRO A 1 156 ? 12.19800  2.66000   -20.72200 1.000 17.94503 ?  136 PRO A CA  1 
ATOM   986  C  C   . PRO A 1 156 ? 12.67900  1.40900   -20.01100 1.000 17.27815 ?  136 PRO A C   1 
ATOM   987  O  O   . PRO A 1 156 ? 12.90500  0.38600   -20.66800 1.000 18.88926 ?  136 PRO A O   1 
ATOM   988  C  CB  . PRO A 1 156 ? 13.34600  3.65600   -20.93000 1.000 20.11751 ?  136 PRO A CB  1 
ATOM   989  C  CG  . PRO A 1 156 ? 12.68400  4.95500   -20.93800 1.000 22.74191 ?  136 PRO A CG  1 
ATOM   990  C  CD  . PRO A 1 156 ? 11.64100  4.85800   -19.87000 1.000 15.37549 ?  136 PRO A CD  1 
ATOM   991  N  N   . LEU A 1 157 ? 12.85000  1.45400   -18.68600 1.000 16.18408 ?  137 LEU A N   1 
ATOM   992  C  CA  . LEU A 1 157 ? 13.42100  0.30000   -17.99100 1.000 17.08584 ?  137 LEU A CA  1 
ATOM   993  C  C   . LEU A 1 157 ? 12.51100  -0.91800  -18.07500 1.000 15.62126 ?  137 LEU A C   1 
ATOM   994  O  O   . LEU A 1 157 ? 12.95700  -1.96000  -18.58500 1.000 18.72161 ?  137 LEU A O   1 
ATOM   995  C  CB  . LEU A 1 157 ? 13.77100  0.68200   -16.54900 1.000 14.84317 ?  137 LEU A CB  1 
ATOM   996  C  CG  . LEU A 1 157 ? 14.15000  -0.49800  -15.64900 1.000 17.65472 ?  137 LEU A CG  1 
ATOM   997  C  CD1 . LEU A 1 157 ? 15.36800  -1.21700  -16.22000 1.000 16.49494 ?  137 LEU A CD1 1 
ATOM   998  C  CD2 . LEU A 1 157 ? 14.40500  -0.03300  -14.22200 1.000 16.93998 ?  137 LEU A CD2 1 
ATOM   999  N  N   . PRO A 1 158 ? 11.24200  -0.86700  -17.62900 1.000 17.75479 ?  138 PRO A N   1 
ATOM   1000 C  CA  . PRO A 1 158 ? 10.37300  -2.04500  -17.80900 1.000 17.45400 ?  138 PRO A CA  1 
ATOM   1001 C  C   . PRO A 1 158 ? 10.18600  -2.43300  -19.26600 1.000 16.75846 ?  138 PRO A C   1 
ATOM   1002 O  O   . PRO A 1 158 ? 10.10600  -3.62600  -19.58300 1.000 14.88117 ?  138 PRO A O   1 
ATOM   1003 C  CB  . PRO A 1 158 ? 9.04500   -1.60300  -17.17100 1.000 18.96857 ?  138 PRO A CB  1 
ATOM   1004 C  CG  . PRO A 1 158 ? 9.41600   -0.53500  -16.22100 1.000 23.78719 ?  138 PRO A CG  1 
ATOM   1005 C  CD  . PRO A 1 158 ? 10.54100  0.20100   -16.89800 1.000 16.49945 ?  138 PRO A CD  1 
ATOM   1006 N  N   . LEU A 1 159 ? 10.10600  -1.45000  -20.16400 1.000 16.62672 ?  139 LEU A N   1 
ATOM   1007 C  CA  . LEU A 1 159 ? 9.98400   -1.75200  -21.58600 1.000 17.11760 ?  139 LEU A CA  1 
ATOM   1008 C  C   . LEU A 1 159 ? 11.16900  -2.57800  -22.07200 1.000 21.98118 ?  139 LEU A C   1 
ATOM   1009 O  O   . LEU A 1 159 ? 11.00200  -3.55000  -22.82200 1.000 16.02253 ?  139 LEU A O   1 
ATOM   1010 C  CB  . LEU A 1 159 ? 9.87300   -0.44900  -22.37700 1.000 21.15990 ?  139 LEU A CB  1 
ATOM   1011 C  CG  . LEU A 1 159 ? 9.22600   -0.50200  -23.76000 1.000 28.90604 ?  139 LEU A CG  1 
ATOM   1012 C  CD1 . LEU A 1 159 ? 7.99900   -1.39400  -23.73200 1.000 22.58684 ?  139 LEU A CD1 1 
ATOM   1013 C  CD2 . LEU A 1 159 ? 8.87100   0.90500   -24.22500 1.000 32.46419 ?  139 LEU A CD2 1 
ATOM   1014 N  N   . ARG A 1 160 ? 12.37500  -2.21100  -21.64300 1.000 19.35686 ?  140 ARG A N   1 
ATOM   1015 C  CA  . ARG A 1 160 ? 13.55800  -2.98300  -21.99800 1.000 17.27253 ?  140 ARG A CA  1 
ATOM   1016 C  C   . ARG A 1 160 ? 13.49300  -4.39100  -21.42200 1.000 20.60362 ?  140 ARG A C   1 
ATOM   1017 O  O   . ARG A 1 160 ? 13.78200  -5.37200  -22.12000 1.000 16.70605 ?  140 ARG A O   1 
ATOM   1018 C  CB  . ARG A 1 160 ? 14.80700  -2.24200  -21.51400 1.000 21.58902 ?  140 ARG A CB  1 
ATOM   1019 C  CG  . ARG A 1 160 ? 16.07300  -3.07800  -21.44800 1.000 23.44999 ?  140 ARG A CG  1 
ATOM   1020 C  CD  . ARG A 1 160 ? 16.58500  -3.46100  -22.82900 1.000 26.37489 ?  140 ARG A CD  1 
ATOM   1021 N  NE  . ARG A 1 160 ? 17.46700  -4.62000  -22.75400 1.000 28.20216 ?  140 ARG A NE  1 
ATOM   1022 C  CZ  . ARG A 1 160 ? 18.65800  -4.62600  -22.16800 1.000 29.33113 ?  140 ARG A CZ  1 
ATOM   1023 N  NH1 . ARG A 1 160 ? 19.22200  -3.51200  -21.72500 1.000 24.17224 ?  140 ARG A NH1 1 
ATOM   1024 N  NH2 . ARG A 1 160 ? 19.31300  -5.77800  -22.04400 1.000 28.63382 ?  140 ARG A NH2 1 
ATOM   1025 N  N   . VAL A 1 161 ? 13.09100  -4.51500  -20.15400 1.000 18.27631 ?  141 VAL A N   1 
ATOM   1026 C  CA  . VAL A 1 161 ? 13.06900  -5.82400  -19.50400 1.000 15.54185 ?  141 VAL A CA  1 
ATOM   1027 C  C   . VAL A 1 161 ? 12.01700  -6.72600  -20.13700 1.000 21.12796 ?  141 VAL A C   1 
ATOM   1028 O  O   . VAL A 1 161 ? 12.27400  -7.90500  -20.41100 1.000 22.30062 ?  141 VAL A O   1 
ATOM   1029 C  CB  . VAL A 1 161 ? 12.84400  -5.66200  -17.99100 1.000 23.71570 ?  141 VAL A CB  1 
ATOM   1030 C  CG1 . VAL A 1 161 ? 12.73700  -7.02200  -17.31600 1.000 20.34895 ?  141 VAL A CG1 1 
ATOM   1031 C  CG2 . VAL A 1 161 ? 13.98700  -4.85800  -17.38100 1.000 21.70611 ?  141 VAL A CG2 1 
ATOM   1032 N  N   . ILE A 1 162 ? 10.81400  -6.19300  -20.37700 1.000 19.16449 ?  142 ILE A N   1 
ATOM   1033 C  CA  . ILE A 1 162 ? 9.77200   -7.02400  -20.96900 1.000 17.67638 ?  142 ILE A CA  1 
ATOM   1034 C  C   . ILE A 1 162 ? 10.12300  -7.38200  -22.40800 1.000 19.85775 ?  142 ILE A C   1 
ATOM   1035 O  O   . ILE A 1 162 ? 9.73700   -8.44900  -22.89800 1.000 17.23960 ?  142 ILE A O   1 
ATOM   1036 C  CB  . ILE A 1 162 ? 8.39700   -6.33400  -20.86600 1.000 20.37863 ?  142 ILE A CB  1 
ATOM   1037 C  CG1 . ILE A 1 162 ? 7.27600   -7.37600  -20.92500 1.000 19.45327 ?  142 ILE A CG1 1 
ATOM   1038 C  CG2 . ILE A 1 162 ? 8.21300   -5.30500  -21.96600 1.000 22.46884 ?  142 ILE A CG2 1 
ATOM   1039 C  CD1 . ILE A 1 162 ? 7.36200   -8.42100  -19.83500 1.000 24.84962 ?  142 ILE A CD1 1 
ATOM   1040 N  N   . GLY A 1 163 ? 10.86200  -6.51500  -23.10500 1.000 19.68752 ?  143 GLY A N   1 
ATOM   1041 C  CA  . GLY A 1 163 ? 11.34600  -6.87400  -24.42700 1.000 21.05349 ?  143 GLY A CA  1 
ATOM   1042 C  C   . GLY A 1 163 ? 12.32100  -8.03400  -24.38300 1.000 21.59004 ?  143 GLY A C   1 
ATOM   1043 O  O   . GLY A 1 163 ? 12.22300  -8.96700  -25.18500 1.000 26.15490 ?  143 GLY A O   1 
ATOM   1044 N  N   . ASP A 1 164 ? 13.27600  -7.99000  -23.44300 1.000 22.50179 ?  144 ASP A N   1 
ATOM   1045 C  CA  . ASP A 1 164 ? 14.17600  -9.12100  -23.22500 1.000 21.13950 ?  144 ASP A CA  1 
ATOM   1046 C  C   . ASP A 1 164 ? 13.40700  -10.37800 -22.84900 1.000 27.42703 ?  144 ASP A C   1 
ATOM   1047 O  O   . ASP A 1 164 ? 13.72200  -11.47500 -23.32700 1.000 19.88912 ?  144 ASP A O   1 
ATOM   1048 C  CB  . ASP A 1 164 ? 15.19000  -8.78500  -22.12900 1.000 19.49951 ?  144 ASP A CB  1 
ATOM   1049 C  CG  . ASP A 1 164 ? 16.19000  -7.72300  -22.55300 1.000 26.80931 ?  144 ASP A CG  1 
ATOM   1050 O  OD1 . ASP A 1 164 ? 16.01000  -7.11400  -23.63000 1.000 26.52466 ?  144 ASP A OD1 1 
ATOM   1051 O  OD2 . ASP A 1 164 ? 17.15500  -7.49500  -21.79300 1.000 28.53226 -1 144 ASP A OD2 1 
ATOM   1052 N  N   . LEU A 1 165 ? 12.40000  -10.24100 -21.98100 1.000 22.47563 ?  145 LEU A N   1 
ATOM   1053 C  CA  . LEU A 1 165 ? 11.64500  -11.40800 -21.53500 1.000 20.82296 ?  145 LEU A CA  1 
ATOM   1054 C  C   . LEU A 1 165 ? 10.90500  -12.06200 -22.69600 1.000 23.66760 ?  145 LEU A C   1 
ATOM   1055 O  O   . LEU A 1 165 ? 10.84100  -13.29400 -22.78900 1.000 25.23125 ?  145 LEU A O   1 
ATOM   1056 C  CB  . LEU A 1 165 ? 10.67100  -11.00400 -20.42800 1.000 24.44214 ?  145 LEU A CB  1 
ATOM   1057 C  CG  . LEU A 1 165 ? 10.08000  -12.11900 -19.55700 1.000 27.78101 ?  145 LEU A CG  1 
ATOM   1058 C  CD1 . LEU A 1 165 ? 11.16400  -12.76000 -18.70400 1.000 20.93344 ?  145 LEU A CD1 1 
ATOM   1059 C  CD2 . LEU A 1 165 ? 8.94700   -11.59000 -18.68200 1.000 24.63854 ?  145 LEU A CD2 1 
ATOM   1060 N  N   . LEU A 1 166 ? 10.35700  -11.25400 -23.60000 1.000 18.93074 ?  146 LEU A N   1 
ATOM   1061 C  CA  . LEU A 1 166 ? 9.61700   -11.74900 -24.75000 1.000 21.70850 ?  146 LEU A CA  1 
ATOM   1062 C  C   . LEU A 1 166 ? 10.50400  -12.02000 -25.95800 1.000 24.73689 ?  146 LEU A C   1 
ATOM   1063 O  O   . LEU A 1 166 ? 9.99400   -12.45700 -26.99500 1.000 26.04607 ?  146 LEU A O   1 
ATOM   1064 C  CB  . LEU A 1 166 ? 8.51200   -10.75400 -25.12500 1.000 27.46319 ?  146 LEU A CB  1 
ATOM   1065 C  CG  . LEU A 1 166 ? 7.45300   -10.56200 -24.03600 1.000 22.18404 ?  146 LEU A CG  1 
ATOM   1066 C  CD1 . LEU A 1 166 ? 6.35900   -9.59200  -24.46900 1.000 20.30886 ?  146 LEU A CD1 1 
ATOM   1067 C  CD2 . LEU A 1 166 ? 6.85400   -11.90200 -23.65300 1.000 25.86009 ?  146 LEU A CD2 1 
ATOM   1068 N  N   . GLY A 1 167 ? 11.80700  -11.77200 -25.85300 1.000 24.84234 ?  147 GLY A N   1 
ATOM   1069 C  CA  . GLY A 1 167 ? 12.72300  -12.06100 -26.94300 1.000 25.54026 ?  147 GLY A CA  1 
ATOM   1070 C  C   . GLY A 1 167 ? 12.55800  -11.18000 -28.16100 1.000 21.96019 ?  147 GLY A C   1 
ATOM   1071 O  O   . GLY A 1 167 ? 12.72700  -11.65600 -29.29100 1.000 22.95060 ?  147 GLY A O   1 
ATOM   1072 N  N   . VAL A 1 168 ? 12.23100  -9.90700  -27.96600 1.000 20.49363 ?  148 VAL A N   1 
ATOM   1073 C  CA  . VAL A 1 168 ? 12.04700  -8.99000  -29.08600 1.000 22.04243 ?  148 VAL A CA  1 
ATOM   1074 C  C   . VAL A 1 168 ? 13.39700  -8.74700  -29.75200 1.000 21.95013 ?  148 VAL A C   1 
ATOM   1075 O  O   . VAL A 1 168 ? 14.35200  -8.33700  -29.08000 1.000 21.49917 ?  148 VAL A O   1 
ATOM   1076 C  CB  . VAL A 1 168 ? 11.40500  -7.67100  -28.63100 1.000 21.76320 ?  148 VAL A CB  1 
ATOM   1077 C  CG1 . VAL A 1 168 ? 11.22900  -6.73900  -29.81200 1.000 22.78487 ?  148 VAL A CG1 1 
ATOM   1078 C  CG2 . VAL A 1 168 ? 10.05700  -7.95000  -27.96200 1.000 18.76812 ?  148 VAL A CG2 1 
ATOM   1079 N  N   . PRO A 1 169 ? 13.52200  -8.99200  -31.05900 1.000 25.69469 ?  149 PRO A N   1 
ATOM   1080 C  CA  . PRO A 1 169 ? 14.81000  -8.78400  -31.71800 1.000 28.68500 ?  149 PRO A CA  1 
ATOM   1081 C  C   . PRO A 1 169 ? 15.12100  -7.30400  -31.83100 1.000 27.10911 ?  149 PRO A C   1 
ATOM   1082 O  O   . PRO A 1 169 ? 14.20400  -6.46400  -31.86600 1.000 27.23671 ?  149 PRO A O   1 
ATOM   1083 C  CB  . PRO A 1 169 ? 14.60500  -9.42200  -33.10500 1.000 25.26216 ?  149 PRO A CB  1 
ATOM   1084 C  CG  . PRO A 1 169 ? 13.35400  -10.25400 -32.97500 1.000 31.40885 ?  149 PRO A CG  1 
ATOM   1085 C  CD  . PRO A 1 169 ? 12.51200  -9.51700  -31.98800 1.000 23.93554 ?  149 PRO A CD  1 
ATOM   1086 N  N   . PRO A 1 170 ? 16.40300  -6.93100  -31.89200 1.000 31.14419 ?  150 PRO A N   1 
ATOM   1087 C  CA  . PRO A 1 170 ? 16.75200  -5.50000  -31.92400 1.000 27.25322 ?  150 PRO A CA  1 
ATOM   1088 C  C   . PRO A 1 170 ? 16.11100  -4.73000  -33.06700 1.000 26.47271 ?  150 PRO A C   1 
ATOM   1089 O  O   . PRO A 1 170 ? 15.80500  -3.54200  -32.90200 1.000 33.26924 ?  150 PRO A O   1 
ATOM   1090 C  CB  . PRO A 1 170 ? 18.28400  -5.52500  -32.04700 1.000 32.42471 ?  150 PRO A CB  1 
ATOM   1091 C  CG  . PRO A 1 170 ? 18.67400  -6.82500  -31.40000 1.000 33.77542 ?  150 PRO A CG  1 
ATOM   1092 C  CD  . PRO A 1 170 ? 17.60500  -7.78500  -31.84900 1.000 33.77435 ?  150 PRO A CD  1 
ATOM   1093 N  N   . ALA A 1 171 ? 15.88900  -5.36700  -34.22000 1.000 28.04937 ?  151 ALA A N   1 
ATOM   1094 C  CA  . ALA A 1 171 ? 15.25000  -4.67900  -35.33600 1.000 28.32998 ?  151 ALA A CA  1 
ATOM   1095 C  C   . ALA A 1 171 ? 13.79400  -4.34200  -35.05400 1.000 31.35152 ?  151 ALA A C   1 
ATOM   1096 O  O   . ALA A 1 171 ? 13.25400  -3.42000  -35.67400 1.000 29.52122 ?  151 ALA A O   1 
ATOM   1097 C  CB  . ALA A 1 171 ? 15.34200  -5.52500  -36.60600 1.000 34.52607 ?  151 ALA A CB  1 
ATOM   1098 N  N   . ASP A 1 172 ? 13.15400  -5.06100  -34.13400 1.000 31.24753 ?  152 ASP A N   1 
ATOM   1099 C  CA  . ASP A 1 172 ? 11.75100  -4.85900  -33.80400 1.000 29.01322 ?  152 ASP A CA  1 
ATOM   1100 C  C   . ASP A 1 172 ? 11.54500  -4.03000  -32.54300 1.000 28.08309 ?  152 ASP A C   1 
ATOM   1101 O  O   . ASP A 1 172 ? 10.39600  -3.78400  -32.16200 1.000 27.89851 ?  152 ASP A O   1 
ATOM   1102 C  CB  . ASP A 1 172 ? 11.05300  -6.21500  -33.64300 1.000 29.79133 ?  152 ASP A CB  1 
ATOM   1103 C  CG  . ASP A 1 172 ? 11.03500  -7.02100  -34.92800 1.000 39.34403 ?  152 ASP A CG  1 
ATOM   1104 O  OD1 . ASP A 1 172 ? 10.69400  -6.45400  -35.98900 1.000 37.59743 ?  152 ASP A OD1 1 
ATOM   1105 O  OD2 . ASP A 1 172 ? 11.37000  -8.22500  -34.87700 1.000 41.83067 -1 152 ASP A OD2 1 
ATOM   1106 N  N   . ARG A 1 173 ? 12.62100  -3.59100  -31.88600 1.000 27.07295 ?  153 ARG A N   1 
ATOM   1107 C  CA  . ARG A 1 173 ? 12.45300  -2.90700  -30.60700 1.000 29.38633 ?  153 ARG A CA  1 
ATOM   1108 C  C   . ARG A 1 173 ? 11.78300  -1.55000  -30.78200 1.000 27.69575 ?  153 ARG A C   1 
ATOM   1109 O  O   . ARG A 1 173 ? 10.98800  -1.13400  -29.93300 1.000 26.76597 ?  153 ARG A O   1 
ATOM   1110 C  CB  . ARG A 1 173 ? 13.79600  -2.74800  -29.89900 1.000 28.48850 ?  153 ARG A CB  1 
ATOM   1111 C  CG  . ARG A 1 173 ? 14.41000  -4.05500  -29.43300 1.000 28.55526 ?  153 ARG A CG  1 
ATOM   1112 C  CD  . ARG A 1 173 ? 14.08000  -4.32300  -27.97400 1.000 26.50628 ?  153 ARG A CD  1 
ATOM   1113 N  NE  . ARG A 1 173 ? 14.35900  -5.70600  -27.61200 1.000 24.15440 ?  153 ARG A NE  1 
ATOM   1114 C  CZ  . ARG A 1 173 ? 14.65900  -6.11300  -26.38700 1.000 27.07998 ?  153 ARG A CZ  1 
ATOM   1115 N  NH1 . ARG A 1 173 ? 14.62400  -5.28500  -25.35500 1.000 21.42243 ?  153 ARG A NH1 1 
ATOM   1116 N  NH2 . ARG A 1 173 ? 14.99100  -7.38600  -26.18900 1.000 32.58221 ?  153 ARG A NH2 1 
ATOM   1117 N  N   . ALA A 1 174 ? 12.07800  -0.85300  -31.88100 1.000 27.73593 ?  154 ALA A N   1 
ATOM   1118 C  CA  . ALA A 1 174 ? 11.52000  0.48100   -32.08200 1.000 22.17624 ?  154 ALA A CA  1 
ATOM   1119 C  C   . ALA A 1 174 ? 10.00500  0.42400   -32.24100 1.000 25.79942 ?  154 ALA A C   1 
ATOM   1120 O  O   . ALA A 1 174 ? 9.27000   1.18700   -31.60200 1.000 21.34677 ?  154 ALA A O   1 
ATOM   1121 C  CB  . ALA A 1 174 ? 12.16700  1.14000   -33.30000 1.000 26.75041 ?  154 ALA A CB  1 
ATOM   1122 N  N   . ARG A 1 175 ? 9.51900   -0.47100  -33.10300 1.000 25.01285 ?  155 ARG A N   1 
ATOM   1123 C  CA  . ARG A 1 175 ? 8.08000   -0.58500  -33.30700 1.000 26.69287 ?  155 ARG A CA  1 
ATOM   1124 C  C   . ARG A 1 175 ? 7.39800   -1.07200  -32.03800 1.000 21.51925 ?  155 ARG A C   1 
ATOM   1125 O  O   . ARG A 1 175 ? 6.32300   -0.58300  -31.67600 1.000 24.35590 ?  155 ARG A O   1 
ATOM   1126 C  CB  . ARG A 1 175 ? 7.78800   -1.54300  -34.45600 1.000 33.01843 ?  155 ARG A CB  1 
ATOM   1127 C  CG  . ARG A 1 175 ? 8.08100   -2.98900  -34.10500 1.000 42.41205 ?  155 ARG A CG  1 
ATOM   1128 C  CD  . ARG A 1 175 ? 7.57800   -3.92800  -35.17800 1.000 48.08867 ?  155 ARG A CD  1 
ATOM   1129 N  NE  . ARG A 1 175 ? 8.29800   -3.72000  -36.42400 1.000 43.53321 ?  155 ARG A NE  1 
ATOM   1130 C  CZ  . ARG A 1 175 ? 7.86100   -4.11500  -37.61000 1.000 49.18183 ?  155 ARG A CZ  1 
ATOM   1131 N  NH1 . ARG A 1 175 ? 6.65700   -4.64400  -37.76200 1.000 55.99682 ?  155 ARG A NH1 1 
ATOM   1132 N  NH2 . ARG A 1 175 ? 8.65100   -3.97700  -38.66900 1.000 49.27169 ?  155 ARG A NH2 1 
ATOM   1133 N  N   . PHE A 1 176 ? 8.02100   -2.03800  -31.35800 1.000 21.40413 ?  156 PHE A N   1 
ATOM   1134 C  CA  . PHE A 1 176 ? 7.52200   -2.54000  -30.08400 1.000 18.80424 ?  156 PHE A CA  1 
ATOM   1135 C  C   . PHE A 1 176 ? 7.35500   -1.41500  -29.06800 1.000 22.36084 ?  156 PHE A C   1 
ATOM   1136 O  O   . PHE A 1 176 ? 6.29200   -1.27600  -28.45100 1.000 28.25202 ?  156 PHE A O   1 
ATOM   1137 C  CB  . PHE A 1 176 ? 8.48100   -3.61000  -29.56300 1.000 20.39605 ?  156 PHE A CB  1 
ATOM   1138 C  CG  . PHE A 1 176 ? 8.10900   -4.17700  -28.22400 1.000 20.46753 ?  156 PHE A CG  1 
ATOM   1139 C  CD1 . PHE A 1 176 ? 7.01300   -5.00800  -28.08500 1.000 18.07279 ?  156 PHE A CD1 1 
ATOM   1140 C  CD2 . PHE A 1 176 ? 8.87400   -3.88300  -27.10300 1.000 18.67697 ?  156 PHE A CD2 1 
ATOM   1141 C  CE1 . PHE A 1 176 ? 6.68100   -5.53700  -26.85000 1.000 23.32093 ?  156 PHE A CE1 1 
ATOM   1142 C  CE2 . PHE A 1 176 ? 8.54900   -4.40600  -25.86700 1.000 24.34561 ?  156 PHE A CE2 1 
ATOM   1143 C  CZ  . PHE A 1 176 ? 7.45100   -5.23200  -25.74100 1.000 20.79361 ?  156 PHE A CZ  1 
ATOM   1144 N  N   . ARG A 1 177 ? 8.39700   -0.60500  -28.87500 1.000 17.82735 ?  157 ARG A N   1 
ATOM   1145 C  CA  . ARG A 1 177 ? 8.31000   0.51800   -27.94400 1.000 20.33118 ?  157 ARG A CA  1 
ATOM   1146 C  C   . ARG A 1 177 ? 7.17600   1.46400   -28.32100 1.000 22.98242 ?  157 ARG A C   1 
ATOM   1147 O  O   . ARG A 1 177 ? 6.37500   1.86000   -27.46700 1.000 18.76802 ?  157 ARG A O   1 
ATOM   1148 C  CB  . ARG A 1 177 ? 9.64700   1.26200   -27.89600 1.000 28.87200 ?  157 ARG A CB  1 
ATOM   1149 C  CG  . ARG A 1 177 ? 10.80600  0.42500   -27.37100 1.000 35.04019 ?  157 ARG A CG  1 
ATOM   1150 C  CD  . ARG A 1 177 ? 11.95600  1.30100   -26.89100 1.000 46.30255 ?  157 ARG A CD  1 
ATOM   1151 N  NE  . ARG A 1 177 ? 12.23200  2.38300   -27.82800 1.000 43.88169 ?  157 ARG A NE  1 
ATOM   1152 C  CZ  . ARG A 1 177 ? 13.20700  2.35900   -28.72700 1.000 51.97685 ?  157 ARG A CZ  1 
ATOM   1153 N  NH1 . ARG A 1 177 ? 14.01000  1.31400   -28.84900 1.000 47.11682 ?  157 ARG A NH1 1 
ATOM   1154 N  NH2 . ARG A 1 177 ? 13.37300  3.40600   -29.53200 1.000 53.90614 ?  157 ARG A NH2 1 
ATOM   1155 N  N   . GLY A 1 178 ? 7.08600   1.82900   -29.60100 1.000 21.92678 ?  158 GLY A N   1 
ATOM   1156 C  CA  . GLY A 1 178 ? 6.06400   2.77700   -30.01800 1.000 22.44093 ?  158 GLY A CA  1 
ATOM   1157 C  C   . GLY A 1 178 ? 4.65500   2.27900   -29.76200 1.000 20.18098 ?  158 GLY A C   1 
ATOM   1158 O  O   . GLY A 1 178 ? 3.79300   3.03300   -29.30100 1.000 19.75206 ?  158 GLY A O   1 
ATOM   1159 N  N   . TRP A 1 179 ? 4.40200   1.00400   -30.04700 1.000 16.85495 ?  159 TRP A N   1 
ATOM   1160 C  CA  . TRP A 1 179 ? 3.04800   0.49000   -29.88800 1.000 22.66179 ?  159 TRP A CA  1 
ATOM   1161 C  C   . TRP A 1 179 ? 2.72600   0.17400   -28.43300 1.000 23.57909 ?  159 TRP A C   1 
ATOM   1162 O  O   . TRP A 1 179 ? 1.61600   0.45800   -27.97100 1.000 19.60242 ?  159 TRP A O   1 
ATOM   1163 C  CB  . TRP A 1 179 ? 2.84700   -0.72800  -30.78700 1.000 21.86941 ?  159 TRP A CB  1 
ATOM   1164 C  CG  . TRP A 1 179 ? 2.54700   -0.34300  -32.22000 1.000 24.46401 ?  159 TRP A CG  1 
ATOM   1165 C  CD1 . TRP A 1 179 ? 3.18500   -0.78400  -33.33900 1.000 26.58281 ?  159 TRP A CD1 1 
ATOM   1166 C  CD2 . TRP A 1 179 ? 1.52400   0.56200   -32.67200 1.000 33.58403 ?  159 TRP A CD2 1 
ATOM   1167 N  NE1 . TRP A 1 179 ? 2.63200   -0.20700  -34.46000 1.000 23.16739 ?  159 TRP A NE1 1 
ATOM   1168 C  CE2 . TRP A 1 179 ? 1.60900   0.62200   -34.07600 1.000 33.51774 ?  159 TRP A CE2 1 
ATOM   1169 C  CE3 . TRP A 1 179 ? 0.54500   1.32700   -32.02300 1.000 36.74081 ?  159 TRP A CE3 1 
ATOM   1170 C  CZ2 . TRP A 1 179 ? 0.74500   1.41100   -34.84400 1.000 34.05375 ?  159 TRP A CZ2 1 
ATOM   1171 C  CZ3 . TRP A 1 179 ? -0.30500  2.11300   -32.78600 1.000 31.91387 ?  159 TRP A CZ3 1 
ATOM   1172 C  CH2 . TRP A 1 179 ? -0.20100  2.14800   -34.18000 1.000 37.33542 ?  159 TRP A CH2 1 
ATOM   1173 N  N   . THR A 1 180 ? 3.67800   -0.39700  -27.69100 1.000 18.36887 ?  160 THR A N   1 
ATOM   1174 C  CA  . THR A 1 180 ? 3.45500   -0.61200  -26.26100 1.000 21.01672 ?  160 THR A CA  1 
ATOM   1175 C  C   . THR A 1 180 ? 3.13000   0.69200   -25.54300 1.000 20.17820 ?  160 THR A C   1 
ATOM   1176 O  O   . THR A 1 180 ? 2.20600   0.73900   -24.72200 1.000 20.15627 ?  160 THR A O   1 
ATOM   1177 C  CB  . THR A 1 180 ? 4.67300   -1.27700  -25.62300 1.000 21.00563 ?  160 THR A CB  1 
ATOM   1178 O  OG1 . THR A 1 180 ? 5.02000   -2.45100  -26.36300 1.000 21.72978 ?  160 THR A OG1 1 
ATOM   1179 C  CG2 . THR A 1 180 ? 4.39100   -1.64400  -24.17300 1.000 22.89914 ?  160 THR A CG2 1 
ATOM   1180 N  N   . THR A 1 181 ? 3.87400   1.76100   -25.84000 1.000 16.79352 ?  161 THR A N   1 
ATOM   1181 C  CA  . THR A 1 181 ? 3.62400   3.04100   -25.18200 1.000 18.44317 ?  161 THR A CA  1 
ATOM   1182 C  C   . THR A 1 181 ? 2.27000   3.61800   -25.57800 1.000 23.10188 ?  161 THR A C   1 
ATOM   1183 O  O   . THR A 1 181 ? 1.53700   4.13400   -24.72800 1.000 21.15388 ?  161 THR A O   1 
ATOM   1184 C  CB  . THR A 1 181 ? 4.73600   4.03100   -25.51600 1.000 22.38624 ?  161 THR A CB  1 
ATOM   1185 O  OG1 . THR A 1 181 ? 4.90900   4.09300   -26.93500 1.000 28.90527 ?  161 THR A OG1 1 
ATOM   1186 C  CG2 . THR A 1 181 ? 6.04200   3.59900   -24.86600 1.000 21.08074 ?  161 THR A CG2 1 
ATOM   1187 N  N   . THR A 1 182 ? 1.92900   3.54600   -26.86500 1.000 18.08863 ?  162 THR A N   1 
ATOM   1188 C  CA  . THR A 1 182 ? 0.62600   4.02200   -27.30900 1.000 18.53395 ?  162 THR A CA  1 
ATOM   1189 C  C   . THR A 1 182 ? -0.49700  3.17200   -26.73100 1.000 20.12086 ?  162 THR A C   1 
ATOM   1190 O  O   . THR A 1 182 ? -1.58300  3.68900   -26.44300 1.000 20.37766 ?  162 THR A O   1 
ATOM   1191 C  CB  . THR A 1 182 ? 0.57200   4.01800   -28.83800 1.000 19.10511 ?  162 THR A CB  1 
ATOM   1192 O  OG1 . THR A 1 182 ? 1.56100   4.91900   -29.35000 1.000 20.39288 ?  162 THR A OG1 1 
ATOM   1193 C  CG2 . THR A 1 182 ? -0.79400  4.45900   -29.33800 1.000 18.11496 ?  162 THR A CG2 1 
ATOM   1194 N  N   . LEU A 1 183 ? -0.24500  1.87500   -26.53600 1.000 18.54735 ?  163 LEU A N   1 
ATOM   1195 C  CA  . LEU A 1 183 ? -1.26900  0.97500   -26.02300 1.000 23.79480 ?  163 LEU A CA  1 
ATOM   1196 C  C   . LEU A 1 183 ? -1.52100  1.19500   -24.53600 1.000 22.68160 ?  163 LEU A C   1 
ATOM   1197 O  O   . LEU A 1 183 ? -2.67700  1.21200   -24.09000 1.000 20.38969 ?  163 LEU A O   1 
ATOM   1198 C  CB  . LEU A 1 183 ? -0.85700  -0.47400  -26.28300 1.000 17.48175 ?  163 LEU A CB  1 
ATOM   1199 C  CG  . LEU A 1 183 ? -1.80100  -1.55200  -25.75500 1.000 20.18069 ?  163 LEU A CG  1 
ATOM   1200 C  CD1 . LEU A 1 183 ? -3.11100  -1.48800  -26.52200 1.000 19.63038 ?  163 LEU A CD1 1 
ATOM   1201 C  CD2 . LEU A 1 183 ? -1.16600  -2.92800  -25.88100 1.000 20.36351 ?  163 LEU A CD2 1 
ATOM   1202 N  N   . LEU A 1 184 ? -0.45700  1.36200   -23.75300 1.000 22.86509 ?  164 LEU A N   1 
ATOM   1203 C  CA  . LEU A 1 184 ? -0.53900  1.22200   -22.30500 1.000 23.29203 ?  164 LEU A CA  1 
ATOM   1204 C  C   . LEU A 1 184 ? -0.18800  2.47900   -21.52300 1.000 19.77861 ?  164 LEU A C   1 
ATOM   1205 O  O   . LEU A 1 184 ? -0.71100  2.66200   -20.42200 1.000 25.27452 ?  164 LEU A O   1 
ATOM   1206 C  CB  . LEU A 1 184 ? 0.37500   0.08000   -21.84100 1.000 17.04184 ?  164 LEU A CB  1 
ATOM   1207 C  CG  . LEU A 1 184 ? -0.00800  -1.30700  -22.35700 1.000 18.15471 ?  164 LEU A CG  1 
ATOM   1208 C  CD1 . LEU A 1 184 ? 1.02000   -2.34000  -21.91000 1.000 19.45892 ?  164 LEU A CD1 1 
ATOM   1209 C  CD2 . LEU A 1 184 ? -1.40600  -1.68300  -21.87500 1.000 21.28615 ?  164 LEU A CD2 1 
ATOM   1210 N  N   . THR A 1 185 ? 0.68200   3.34600   -22.04000 1.000 28.68305 ?  165 THR A N   1 
ATOM   1211 C  CA  . THR A 1 185 ? 0.99500   4.62500   -21.40300 1.000 26.91577 ?  165 THR A CA  1 
ATOM   1212 C  C   . THR A 1 185 ? 0.69200   5.76800   -22.36800 1.000 29.14391 ?  165 THR A C   1 
ATOM   1213 O  O   . THR A 1 185 ? 1.60700   6.47200   -22.81900 1.000 26.36029 ?  165 THR A O   1 
ATOM   1214 C  CB  . THR A 1 185 ? 2.45000   4.68300   -20.94200 1.000 27.69039 ?  165 THR A CB  1 
ATOM   1215 O  OG1 . THR A 1 185 ? 3.31700   4.27100   -22.00900 1.000 25.31701 ?  165 THR A OG1 1 
ATOM   1216 C  CG2 . THR A 1 185 ? 2.65600   3.79700   -19.73000 1.000 30.32649 ?  165 THR A CG2 1 
ATOM   1217 N  N   . PRO A 1 186 ? -0.58100  5.98700   -22.69700 1.000 29.11958 ?  166 PRO A N   1 
ATOM   1218 C  CA  . PRO A 1 186 ? -0.91800  7.05600   -23.64000 1.000 35.23063 ?  166 PRO A CA  1 
ATOM   1219 C  C   . PRO A 1 186 ? -0.63500  8.42600   -23.04800 1.000 40.07759 ?  166 PRO A C   1 
ATOM   1220 O  O   . PRO A 1 186 ? -0.71600  8.63700   -21.83500 1.000 41.43333 ?  166 PRO A O   1 
ATOM   1221 C  CB  . PRO A 1 186 ? -2.42400  6.86300   -23.87300 1.000 31.67874 ?  166 PRO A CB  1 
ATOM   1222 C  CG  . PRO A 1 186 ? -2.71000  5.45900   -23.42200 1.000 29.58996 ?  166 PRO A CG  1 
ATOM   1223 C  CD  . PRO A 1 186 ? -1.79000  5.27300   -22.25400 1.000 33.03637 ?  166 PRO A CD  1 
ATOM   1224 N  N   . GLY A 1 187 ? -0.29900  9.36600   -23.92400 1.000 41.88096 ?  167 GLY A N   1 
ATOM   1225 C  CA  . GLY A 1 187 ? -0.25200  10.75500  -23.54100 1.000 47.80645 ?  167 GLY A CA  1 
ATOM   1226 C  C   . GLY A 1 187 ? -1.64900  11.25500  -23.23300 1.000 54.53057 ?  167 GLY A C   1 
ATOM   1227 O  O   . GLY A 1 187 ? -2.63900  10.77300  -23.79700 1.000 50.51824 ?  167 GLY A O   1 
ATOM   1228 N  N   . PRO A 1 188 ? -1.76300  12.22100  -22.31700 1.000 59.03064 ?  168 PRO A N   1 
ATOM   1229 C  CA  . PRO A 1 188 ? -3.10000  12.72800  -21.96200 1.000 58.91300 ?  168 PRO A CA  1 
ATOM   1230 C  C   . PRO A 1 188 ? -3.84800  13.30800  -23.14600 1.000 57.71217 ?  168 PRO A C   1 
ATOM   1231 O  O   . PRO A 1 188 ? -5.08400  13.24600  -23.17900 1.000 58.55626 ?  168 PRO A O   1 
ATOM   1232 C  CB  . PRO A 1 188 ? -2.80100  13.80100  -20.90300 1.000 54.76948 ?  168 PRO A CB  1 
ATOM   1233 C  CG  . PRO A 1 188 ? -1.35000  14.14400  -21.10400 1.000 55.93456 ?  168 PRO A CG  1 
ATOM   1234 C  CD  . PRO A 1 188 ? -0.70400  12.86400  -21.52400 1.000 53.27048 ?  168 PRO A CD  1 
ATOM   1235 N  N   . ASP A 1 189 ? -3.13100  13.86700  -24.12400 1.000 54.90336 ?  169 ASP A N   1 
ATOM   1236 C  CA  . ASP A 1 189 ? -3.72000  14.38100  -25.35400 1.000 53.13789 ?  169 ASP A CA  1 
ATOM   1237 C  C   . ASP A 1 189 ? -3.42300  13.47000  -26.54400 1.000 55.20514 ?  169 ASP A C   1 
ATOM   1238 O  O   . ASP A 1 189 ? -3.27000  13.94000  -27.67400 1.000 55.17384 ?  169 ASP A O   1 
ATOM   1239 C  CB  . ASP A 1 189 ? -3.23100  15.80200  -25.63000 1.000 60.59114 ?  169 ASP A CB  1 
ATOM   1240 N  N   . GLN A 1 190 ? -3.31900  12.16900  -26.29500 1.000 48.83570 ?  170 GLN A N   1 
ATOM   1241 C  CA  . GLN A 1 190 ? -3.25500  11.20400  -27.38100 1.000 45.04173 ?  170 GLN A CA  1 
ATOM   1242 C  C   . GLN A 1 190 ? -4.64500  11.06000  -27.99500 1.000 31.75623 ?  170 GLN A C   1 
ATOM   1243 O  O   . GLN A 1 190 ? -5.64400  11.10200  -27.26900 1.000 34.78713 ?  170 GLN A O   1 
ATOM   1244 C  CB  . GLN A 1 190 ? -2.77500  9.84800   -26.86100 1.000 40.77519 ?  170 GLN A CB  1 
ATOM   1245 C  CG  . GLN A 1 190 ? -2.66400  8.76200   -27.91800 1.000 36.00717 ?  170 GLN A CG  1 
ATOM   1246 C  CD  . GLN A 1 190 ? -1.92300  7.53400   -27.42100 1.000 36.47686 ?  170 GLN A CD  1 
ATOM   1247 O  OE1 . GLN A 1 190 ? -0.69200  7.50500   -27.39200 1.000 32.54560 ?  170 GLN A OE1 1 
ATOM   1248 N  NE2 . GLN A 1 190 ? -2.67200  6.49700   -27.06400 1.000 32.04732 ?  170 GLN A NE2 1 
ATOM   1249 N  N   . PRO A 1 191 ? -4.74600  10.90700  -29.31400 1.000 33.30807 ?  171 PRO A N   1 
ATOM   1250 C  CA  . PRO A 1 191 ? -6.05300  10.65100  -29.93400 1.000 33.99285 ?  171 PRO A CA  1 
ATOM   1251 C  C   . PRO A 1 191 ? -6.72600  9.44700   -29.30000 1.000 30.37587 ?  171 PRO A C   1 
ATOM   1252 O  O   . PRO A 1 191 ? -6.08600  8.40500   -29.09200 1.000 30.58690 ?  171 PRO A O   1 
ATOM   1253 C  CB  . PRO A 1 191 ? -5.70000  10.38700  -31.40500 1.000 36.35175 ?  171 PRO A CB  1 
ATOM   1254 C  CG  . PRO A 1 191 ? -4.44200  11.15500  -31.61800 1.000 38.27468 ?  171 PRO A CG  1 
ATOM   1255 C  CD  . PRO A 1 191 ? -3.68200  11.07600  -30.32100 1.000 38.00747 ?  171 PRO A CD  1 
ATOM   1256 N  N   . PRO A 1 192 ? -8.01900  9.54600   -28.97800 1.000 30.51742 ?  172 PRO A N   1 
ATOM   1257 C  CA  . PRO A 1 192 ? -8.68200  8.44000   -28.26800 1.000 29.71470 ?  172 PRO A CA  1 
ATOM   1258 C  C   . PRO A 1 192 ? -8.72400  7.14700   -29.06000 1.000 25.65427 ?  172 PRO A C   1 
ATOM   1259 O  O   . PRO A 1 192 ? -8.97400  6.08700   -28.47300 1.000 27.56634 ?  172 PRO A O   1 
ATOM   1260 C  CB  . PRO A 1 192 ? -10.09100 8.98900   -28.00500 1.000 36.23204 ?  172 PRO A CB  1 
ATOM   1261 C  CG  . PRO A 1 192 ? -10.29500 9.98900   -29.10700 1.000 34.42463 ?  172 PRO A CG  1 
ATOM   1262 C  CD  . PRO A 1 192 ? -8.95200  10.64700  -29.26900 1.000 33.81276 ?  172 PRO A CD  1 
ATOM   1263 N  N   . THR A 1 193 ? -8.46800  7.19100   -30.36500 1.000 20.40174 ?  173 THR A N   1 
ATOM   1264 C  CA  . THR A 1 193 ? -8.46300  5.98900   -31.18800 1.000 22.84997 ?  173 THR A CA  1 
ATOM   1265 C  C   . THR A 1 193 ? -7.10000  5.31500   -31.26000 1.000 20.58923 ?  173 THR A C   1 
ATOM   1266 O  O   . THR A 1 193 ? -7.02100  4.15400   -31.67400 1.000 22.33641 ?  173 THR A O   1 
ATOM   1267 C  CB  . THR A 1 193 ? -8.92400  6.32400   -32.60900 1.000 25.00382 ?  173 THR A CB  1 
ATOM   1268 O  OG1 . THR A 1 193 ? -8.18600  7.45100   -33.09300 1.000 31.67001 ?  173 THR A OG1 1 
ATOM   1269 C  CG2 . THR A 1 193 ? -10.41000 6.65000   -32.62500 1.000 30.93627 ?  173 THR A CG2 1 
ATOM   1270 N  N   . ALA A 1 194 ? -6.03500  6.01100   -30.85700 1.000 25.01303 ?  174 ALA A N   1 
ATOM   1271 C  CA  . ALA A 1 194 ? -4.68600  5.49000   -31.05000 1.000 24.84621 ?  174 ALA A CA  1 
ATOM   1272 C  C   . ALA A 1 194 ? -4.45500  4.21000   -30.25700 1.000 22.93584 ?  174 ALA A C   1 
ATOM   1273 O  O   . ALA A 1 194 ? -3.84800  3.25800   -30.76500 1.000 22.63805 ?  174 ALA A O   1 
ATOM   1274 C  CB  . ALA A 1 194 ? -3.65800  6.55300   -30.66000 1.000 27.69398 ?  174 ALA A CB  1 
ATOM   1275 N  N   . ALA A 1 195 ? -4.91700  4.17100   -29.00300 1.000 24.13254 ?  175 ALA A N   1 
ATOM   1276 C  CA  . ALA A 1 195 ? -4.72300  2.97800   -28.18400 1.000 18.83380 ?  175 ALA A CA  1 
ATOM   1277 C  C   . ALA A 1 195 ? -5.52000  1.80200   -28.73300 1.000 20.20914 ?  175 ALA A C   1 
ATOM   1278 O  O   . ALA A 1 195 ? -5.05200  0.65800   -28.69900 1.000 16.06123 ?  175 ALA A O   1 
ATOM   1279 C  CB  . ALA A 1 195 ? -5.10500  3.26400   -26.73200 1.000 18.30573 ?  175 ALA A CB  1 
ATOM   1280 N  N   . ARG A 1 196 ? -6.72300  2.06600   -29.25100 1.000 22.63143 ?  176 ARG A N   1 
ATOM   1281 C  CA  . ARG A 1 196 ? -7.49400  1.01900   -29.91600 1.000 17.82267 ?  176 ARG A CA  1 
ATOM   1282 C  C   . ARG A 1 196 ? -6.71400  0.43300   -31.08600 1.000 15.40091 ?  176 ARG A C   1 
ATOM   1283 O  O   . ARG A 1 196 ? -6.58300  -0.79000  -31.21300 1.000 20.73854 ?  176 ARG A O   1 
ATOM   1284 C  CB  . ARG A 1 196 ? -8.82800  1.58200   -30.40400 1.000 15.89827 ?  176 ARG A CB  1 
ATOM   1285 C  CG  . ARG A 1 196 ? -9.61900  0.63400   -31.28700 1.000 19.32286 ?  176 ARG A CG  1 
ATOM   1286 C  CD  . ARG A 1 196 ? -10.64600 1.39100   -32.12900 1.000 20.87006 ?  176 ARG A CD  1 
ATOM   1287 N  NE  . ARG A 1 196 ? -9.99700  2.28200   -33.08100 1.000 20.73041 ?  176 ARG A NE  1 
ATOM   1288 C  CZ  . ARG A 1 196 ? -10.62900 3.13900   -33.87100 1.000 26.29251 ?  176 ARG A CZ  1 
ATOM   1289 N  NH1 . ARG A 1 196 ? -11.93700 3.31900   -33.79200 1.000 26.45023 ?  176 ARG A NH1 1 
ATOM   1290 N  NH2 . ARG A 1 196 ? -9.93000  3.83400   -34.76300 1.000 30.65470 ?  176 ARG A NH2 1 
ATOM   1291 N  N   . ASP A 1 197 ? -6.19800  1.29700   -31.96200 1.000 16.42334 ?  177 ASP A N   1 
ATOM   1292 C  CA  . ASP A 1 197 ? -5.39700  0.82200   -33.08700 1.000 22.01680 ?  177 ASP A CA  1 
ATOM   1293 C  C   . ASP A 1 197 ? -4.16700  0.05700   -32.60800 1.000 21.98781 ?  177 ASP A C   1 
ATOM   1294 O  O   . ASP A 1 197 ? -3.71400  -0.87200  -33.28200 1.000 20.78745 ?  177 ASP A O   1 
ATOM   1295 C  CB  . ASP A 1 197 ? -4.97700  1.99800   -33.97600 1.000 25.08076 ?  177 ASP A CB  1 
ATOM   1296 C  CG  . ASP A 1 197 ? -6.16400  2.79100   -34.51300 1.000 31.03083 ?  177 ASP A CG  1 
ATOM   1297 O  OD1 . ASP A 1 197 ? -7.30100  2.27400   -34.49500 1.000 28.42735 ?  177 ASP A OD1 1 
ATOM   1298 O  OD2 . ASP A 1 197 ? -5.95400  3.94400   -34.95700 1.000 32.69438 -1 177 ASP A OD2 1 
ATOM   1299 N  N   . ALA A 1 198 ? -3.61700  0.43000   -31.44600 1.000 20.70566 ?  178 ALA A N   1 
ATOM   1300 C  CA  . ALA A 1 198 ? -2.44100  -0.26800  -30.93200 1.000 24.34854 ?  178 ALA A CA  1 
ATOM   1301 C  C   . ALA A 1 198 ? -2.75700  -1.70900  -30.54800 1.000 21.42002 ?  178 ALA A C   1 
ATOM   1302 O  O   . ALA A 1 198 ? -1.86800  -2.56700  -30.58900 1.000 20.69597 ?  178 ALA A O   1 
ATOM   1303 C  CB  . ALA A 1 198 ? -1.86100  0.48700   -29.73700 1.000 21.68415 ?  178 ALA A CB  1 
ATOM   1304 N  N   . VAL A 1 199 ? -4.00100  -1.99300  -30.15900 1.000 18.97794 ?  179 VAL A N   1 
ATOM   1305 C  CA  . VAL A 1 199 ? -4.40200  -3.37700  -29.91200 1.000 19.60710 ?  179 VAL A CA  1 
ATOM   1306 C  C   . VAL A 1 199 ? -4.21300  -4.20800  -31.17300 1.000 19.99145 ?  179 VAL A C   1 
ATOM   1307 O  O   . VAL A 1 199 ? -3.62700  -5.29800  -31.14100 1.000 21.18440 ?  179 VAL A O   1 
ATOM   1308 C  CB  . VAL A 1 199 ? -5.85900  -3.44000  -29.42000 1.000 19.62514 ?  179 VAL A CB  1 
ATOM   1309 C  CG1 . VAL A 1 199 ? -6.29100  -4.88700  -29.23700 1.000 24.27757 ?  179 VAL A CG1 1 
ATOM   1310 C  CG2 . VAL A 1 199 ? -6.02400  -2.66600  -28.12400 1.000 19.74461 ?  179 VAL A CG2 1 
ATOM   1311 N  N   . VAL A 1 200 ? -4.72200  -3.70300  -32.30000 1.000 19.58637 ?  180 VAL A N   1 
ATOM   1312 C  CA  . VAL A 1 200 ? -4.59200  -4.40600  -33.57300 1.000 19.32748 ?  180 VAL A CA  1 
ATOM   1313 C  C   . VAL A 1 200 ? -3.12300  -4.57200  -33.93300 1.000 18.35521 ?  180 VAL A C   1 
ATOM   1314 O  O   . VAL A 1 200 ? -2.66800  -5.66300  -34.29700 1.000 18.81434 ?  180 VAL A O   1 
ATOM   1315 C  CB  . VAL A 1 200 ? -5.34900  -3.64800  -34.68100 1.000 25.87998 ?  180 VAL A CB  1 
ATOM   1316 C  CG1 . VAL A 1 200 ? -5.29800  -4.43000  -35.99200 1.000 27.37647 ?  180 VAL A CG1 1 
ATOM   1317 C  CG2 . VAL A 1 200 ? -6.78300  -3.33700  -34.25500 1.000 24.62496 ?  180 VAL A CG2 1 
ATOM   1318 N  N   . ALA A 1 201 ? -2.36600  -3.47800  -33.85600 1.000 20.51372 ?  181 ALA A N   1 
ATOM   1319 C  CA  . ALA A 1 201 ? -0.95700  -3.52800  -34.22500 1.000 21.74812 ?  181 ALA A CA  1 
ATOM   1320 C  C   . ALA A 1 201 ? -0.18700  -4.50900  -33.35100 1.000 19.10176 ?  181 ALA A C   1 
ATOM   1321 O  O   . ALA A 1 201 ? 0.63000   -5.28900  -33.85500 1.000 23.22300 ?  181 ALA A O   1 
ATOM   1322 C  CB  . ALA A 1 201 ? -0.34900  -2.13100  -34.13600 1.000 17.78299 ?  181 ALA A CB  1 
ATOM   1323 N  N   . MET A 1 202 ? -0.44200  -4.50100  -32.04000 1.000 20.59027 ?  182 MET A N   1 
ATOM   1324 C  CA  . MET A 1 202 ? 0.34900   -5.35400  -31.16100 1.000 21.92827 ?  182 MET A CA  1 
ATOM   1325 C  C   . MET A 1 202 ? -0.07100  -6.81500  -31.27600 1.000 20.68344 ?  182 MET A C   1 
ATOM   1326 O  O   . MET A 1 202 ? 0.76800   -7.70900  -31.12800 1.000 19.86162 ?  182 MET A O   1 
ATOM   1327 C  CB  . MET A 1 202 ? 0.24700   -4.87900  -29.71100 1.000 21.10012 ?  182 MET A CB  1 
ATOM   1328 C  CG  . MET A 1 202 ? 0.99400   -5.77900  -28.72700 1.000 19.48744 ?  182 MET A CG  1 
ATOM   1329 S  SD  . MET A 1 202 ? 2.79500   -5.66300  -28.92100 1.000 25.49303 ?  182 MET A SD  1 
ATOM   1330 C  CE  . MET A 1 202 ? 3.10600   -3.97600  -28.42100 1.000 23.99079 ?  182 MET A CE  1 
ATOM   1331 N  N   . HIS A 1 203 ? -1.34900  -7.08500  -31.55700 1.000 22.24713 ?  183 HIS A N   1 
ATOM   1332 C  CA  . HIS A 1 203 ? -1.77400  -8.46700  -31.77200 1.000 22.05343 ?  183 HIS A CA  1 
ATOM   1333 C  C   . HIS A 1 203 ? -1.01900  -9.09600  -32.93500 1.000 24.23277 ?  183 HIS A C   1 
ATOM   1334 O  O   . HIS A 1 203 ? -0.53700  -10.22900 -32.83800 1.000 21.54092 ?  183 HIS A O   1 
ATOM   1335 C  CB  . HIS A 1 203 ? -3.28000  -8.52700  -32.02700 1.000 22.19153 ?  183 HIS A CB  1 
ATOM   1336 C  CG  . HIS A 1 203 ? -3.82600  -9.92200  -32.09300 1.000 26.25949 ?  183 HIS A CG  1 
ATOM   1337 N  ND1 . HIS A 1 203 ? -4.12100  -10.55200 -33.28400 1.000 33.60070 ?  183 HIS A ND1 1 
ATOM   1338 C  CD2 . HIS A 1 203 ? -4.14500  -10.80400 -31.11500 1.000 29.27430 ?  183 HIS A CD2 1 
ATOM   1339 C  CE1 . HIS A 1 203 ? -4.58500  -11.76400 -33.03800 1.000 35.60280 ?  183 HIS A CE1 1 
ATOM   1340 N  NE2 . HIS A 1 203 ? -4.61200  -11.94100 -31.72900 1.000 30.48843 ?  183 HIS A NE2 1 
ATOM   1341 N  N   . GLY A 1 204 ? -0.91700  -8.37500  -34.05400 1.000 27.05924 ?  184 GLY A N   1 
ATOM   1342 C  CA  . GLY A 1 204 ? -0.15300  -8.88600  -35.18000 1.000 27.34262 ?  184 GLY A CA  1 
ATOM   1343 C  C   . GLY A 1 204 ? 1.32600   -9.00900  -34.86900 1.000 23.21272 ?  184 GLY A C   1 
ATOM   1344 O  O   . GLY A 1 204 ? 1.97000   -9.98900  -35.25300 1.000 30.23040 ?  184 GLY A O   1 
ATOM   1345 N  N   . PHE A 1 205 ? 1.88600   -8.01600  -34.17000 1.000 24.56379 ?  185 PHE A N   1 
ATOM   1346 C  CA  . PHE A 1 205 ? 3.28000   -8.10100  -33.73900 1.000 21.96863 ?  185 PHE A CA  1 
ATOM   1347 C  C   . PHE A 1 205 ? 3.51700   -9.35100  -32.90000 1.000 28.06242 ?  185 PHE A C   1 
ATOM   1348 O  O   . PHE A 1 205 ? 4.48300   -10.08900 -33.12300 1.000 23.76227 ?  185 PHE A O   1 
ATOM   1349 C  CB  . PHE A 1 205 ? 3.66700   -6.85000  -32.95000 1.000 22.07089 ?  185 PHE A CB  1 
ATOM   1350 C  CG  . PHE A 1 205 ? 5.09600   -6.85000  -32.46300 1.000 24.77834 ?  185 PHE A CG  1 
ATOM   1351 C  CD1 . PHE A 1 205 ? 6.11100   -6.32900  -33.24500 1.000 28.24968 ?  185 PHE A CD1 1 
ATOM   1352 C  CD2 . PHE A 1 205 ? 5.42000   -7.37400  -31.21700 1.000 29.01474 ?  185 PHE A CD2 1 
ATOM   1353 C  CE1 . PHE A 1 205 ? 7.42400   -6.33100  -32.79300 1.000 30.21974 ?  185 PHE A CE1 1 
ATOM   1354 C  CE2 . PHE A 1 205 ? 6.72400   -7.38000  -30.76500 1.000 24.40924 ?  185 PHE A CE2 1 
ATOM   1355 C  CZ  . PHE A 1 205 ? 7.72700   -6.85600  -31.55200 1.000 27.02180 ?  185 PHE A CZ  1 
ATOM   1356 N  N   . LEU A 1 206 ? 2.63500   -9.60600  -31.92800 1.000 21.62804 ?  186 LEU A N   1 
ATOM   1357 C  CA  . LEU A 1 206 ? 2.83800   -10.72700 -31.01600 1.000 25.15628 ?  186 LEU A CA  1 
ATOM   1358 C  C   . LEU A 1 206 ? 2.64900   -12.06000 -31.72900 1.000 24.55493 ?  186 LEU A C   1 
ATOM   1359 O  O   . LEU A 1 206 ? 3.38600   -13.01800 -31.46800 1.000 24.71203 ?  186 LEU A O   1 
ATOM   1360 C  CB  . LEU A 1 206 ? 1.88600   -10.60100 -29.82600 1.000 23.60736 ?  186 LEU A CB  1 
ATOM   1361 C  CG  . LEU A 1 206 ? 2.26900   -9.52300  -28.81000 1.000 20.60922 ?  186 LEU A CG  1 
ATOM   1362 C  CD1 . LEU A 1 206 ? 1.27600   -9.47400  -27.66700 1.000 22.39833 ?  186 LEU A CD1 1 
ATOM   1363 C  CD2 . LEU A 1 206 ? 3.68700   -9.74900  -28.28200 1.000 20.49802 ?  186 LEU A CD2 1 
ATOM   1364 N  N   . VAL A 1 207 ? 1.66400   -12.14100 -32.62800 1.000 22.13409 ?  187 VAL A N   1 
ATOM   1365 C  CA  . VAL A 1 207 ? 1.51100   -13.33400 -33.45800 1.000 28.28305 ?  187 VAL A CA  1 
ATOM   1366 C  C   . VAL A 1 207 ? 2.77200   -13.56600 -34.28100 1.000 28.00592 ?  187 VAL A C   1 
ATOM   1367 O  O   . VAL A 1 207 ? 3.28900   -14.68600 -34.36200 1.000 33.50640 ?  187 VAL A O   1 
ATOM   1368 C  CB  . VAL A 1 207 ? 0.26900   -13.20500 -34.35700 1.000 28.07535 ?  187 VAL A CB  1 
ATOM   1369 C  CG1 . VAL A 1 207 ? 0.37400   -14.14800 -35.54300 1.000 33.25035 ?  187 VAL A CG1 1 
ATOM   1370 C  CG2 . VAL A 1 207 ? -0.99300  -13.48300 -33.55900 1.000 31.22699 ?  187 VAL A CG2 1 
ATOM   1371 N  N   . ASP A 1 208 ? 3.29100   -12.50100 -34.89500 1.000 29.77982 ?  188 ASP A N   1 
ATOM   1372 C  CA  . ASP A 1 208 ? 4.51500   -12.62400 -35.68000 1.000 26.12767 ?  188 ASP A CA  1 
ATOM   1373 C  C   . ASP A 1 208 ? 5.69600   -13.01700 -34.80200 1.000 27.77376 ?  188 ASP A C   1 
ATOM   1374 O  O   . ASP A 1 208 ? 6.53700   -13.82400 -35.21100 1.000 30.64490 ?  188 ASP A O   1 
ATOM   1375 C  CB  . ASP A 1 208 ? 4.79700   -11.31400 -36.41600 1.000 25.28350 ?  188 ASP A CB  1 
ATOM   1376 C  CG  . ASP A 1 208 ? 3.75300   -11.00500 -37.47900 1.000 34.63335 ?  188 ASP A CG  1 
ATOM   1377 O  OD1 . ASP A 1 208 ? 2.92800   -11.89500 -37.78200 1.000 34.98186 -1 188 ASP A OD1 1 
ATOM   1378 O  OD2 . ASP A 1 208 ? 3.74300   -9.86700  -38.00000 1.000 33.26944 -1 188 ASP A OD2 1 
ATOM   1379 N  N   . LEU A 1 209 ? 5.76900   -12.46500 -33.58500 1.000 25.99767 ?  189 LEU A N   1 
ATOM   1380 C  CA  . LEU A 1 209 ? 6.86600   -12.79600 -32.67900 1.000 32.48559 ?  189 LEU A CA  1 
ATOM   1381 C  C   . LEU A 1 209 ? 6.83200   -14.26500 -32.27400 1.000 30.83196 ?  189 LEU A C   1 
ATOM   1382 O  O   . LEU A 1 209 ? 7.87600   -14.92300 -32.20700 1.000 28.44887 ?  189 LEU A O   1 
ATOM   1383 C  CB  . LEU A 1 209 ? 6.81400   -11.90300 -31.43800 1.000 24.97411 ?  189 LEU A CB  1 
ATOM   1384 C  CG  . LEU A 1 209 ? 7.96000   -12.04800 -30.43100 1.000 29.45319 ?  189 LEU A CG  1 
ATOM   1385 C  CD1 . LEU A 1 209 ? 9.31600   -11.76900 -31.08300 1.000 25.24240 ?  189 LEU A CD1 1 
ATOM   1386 C  CD2 . LEU A 1 209 ? 7.73700   -11.14100 -29.22800 1.000 25.08976 ?  189 LEU A CD2 1 
ATOM   1387 N  N   . VAL A 1 210 ? 5.63900   -14.79300 -31.99100 1.000 26.28910 ?  190 VAL A N   1 
ATOM   1388 C  CA  . VAL A 1 210 ? 5.52100   -16.20500 -31.64000 1.000 30.68236 ?  190 VAL A CA  1 
ATOM   1389 C  C   . VAL A 1 210 ? 5.98000   -17.07800 -32.80100 1.000 36.36631 ?  190 VAL A C   1 
ATOM   1390 O  O   . VAL A 1 210 ? 6.68800   -18.07600 -32.60700 1.000 36.48334 ?  190 VAL A O   1 
ATOM   1391 C  CB  . VAL A 1 210 ? 4.07500   -16.52600 -31.21800 1.000 31.09348 ?  190 VAL A CB  1 
ATOM   1392 C  CG1 . VAL A 1 210 ? 3.82500   -18.02300 -31.24400 1.000 38.93388 ?  190 VAL A CG1 1 
ATOM   1393 C  CG2 . VAL A 1 210 ? 3.79100   -15.95600 -29.83600 1.000 30.80410 ?  190 VAL A CG2 1 
ATOM   1394 N  N   . ALA A 1 211 ? 5.59500   -16.71000 -34.02700 1.000 36.65653 ?  191 ALA A N   1 
ATOM   1395 C  CA  . ALA A 1 211 ? 6.03700   -17.44900 -35.20500 1.000 34.35076 ?  191 ALA A CA  1 
ATOM   1396 C  C   . ALA A 1 211 ? 7.55400   -17.43400 -35.33700 1.000 40.59239 ?  191 ALA A C   1 
ATOM   1397 O  O   . ALA A 1 211 ? 8.16800   -18.46400 -35.64000 1.000 43.64619 ?  191 ALA A O   1 
ATOM   1398 C  CB  . ALA A 1 211 ? 5.38700   -16.86600 -36.45800 1.000 35.17928 ?  191 ALA A CB  1 
ATOM   1399 N  N   . ALA A 1 212 ? 8.17700   -16.27500 -35.11100 1.000 36.83042 ?  192 ALA A N   1 
ATOM   1400 C  CA  . ALA A 1 212 ? 9.63100   -16.18500 -35.18500 1.000 35.36286 ?  192 ALA A CA  1 
ATOM   1401 C  C   . ALA A 1 212 ? 10.28900  -17.10800 -34.16800 1.000 44.71085 ?  192 ALA A C   1 
ATOM   1402 O  O   . ALA A 1 212 ? 11.22900  -17.84400 -34.49500 1.000 40.06370 ?  192 ALA A O   1 
ATOM   1403 C  CB  . ALA A 1 212 ? 10.07800  -14.73900 -34.96500 1.000 36.88770 ?  192 ALA A CB  1 
ATOM   1404 N  N   . LYS A 1 213 ? 9.80500   -17.08200 -32.92400 1.000 35.28014 ?  193 LYS A N   1 
ATOM   1405 C  CA  . LYS A 1 213 ? 10.37300  -17.93800 -31.88900 1.000 38.53183 ?  193 LYS A CA  1 
ATOM   1406 C  C   . LYS A 1 213 ? 10.06500  -19.40600 -32.14700 1.000 34.25830 ?  193 LYS A C   1 
ATOM   1407 O  O   . LYS A 1 213 ? 10.86800  -20.27700 -31.79700 1.000 44.56599 ?  193 LYS A O   1 
ATOM   1408 C  CB  . LYS A 1 213 ? 9.85000   -17.51600 -30.51800 1.000 33.13383 ?  193 LYS A CB  1 
ATOM   1409 C  CG  . LYS A 1 213 ? 10.34100  -16.15000 -30.08600 1.000 32.61486 ?  193 LYS A CG  1 
ATOM   1410 C  CD  . LYS A 1 213 ? 11.83200  -16.00200 -30.33000 1.000 34.66882 ?  193 LYS A CD  1 
ATOM   1411 C  CE  . LYS A 1 213 ? 12.37400  -14.76900 -29.63800 1.000 29.27760 ?  193 LYS A CE  1 
ATOM   1412 N  NZ  . LYS A 1 213 ? 12.92800  -13.79200 -30.61200 1.000 38.39303 ?  193 LYS A NZ  1 
ATOM   1413 N  N   . ARG A 1 214 ? 8.91200   -19.69700 -32.75200 1.000 39.98878 ?  194 ARG A N   1 
ATOM   1414 C  CA  . ARG A 1 214 ? 8.60000   -21.07300 -33.12000 1.000 40.97134 ?  194 ARG A CA  1 
ATOM   1415 C  C   . ARG A 1 214 ? 9.58100   -21.60600 -34.15500 1.000 48.55130 ?  194 ARG A C   1 
ATOM   1416 O  O   . ARG A 1 214 ? 9.87300   -22.80700 -34.17200 1.000 54.24188 ?  194 ARG A O   1 
ATOM   1417 C  CB  . ARG A 1 214 ? 7.16600   -21.16300 -33.64600 1.000 42.86461 ?  194 ARG A CB  1 
ATOM   1418 C  CG  . ARG A 1 214 ? 6.55300   -22.54800 -33.54300 1.000 39.30376 ?  194 ARG A CG  1 
ATOM   1419 N  N   . ALA A 1 215 ? 10.10700  -20.73100 -35.01100 1.000 45.96562 ?  195 ALA A N   1 
ATOM   1420 C  CA  . ALA A 1 215 ? 11.08200  -21.11600 -36.02400 1.000 47.70421 ?  195 ALA A CA  1 
ATOM   1421 C  C   . ALA A 1 215 ? 12.51200  -21.06600 -35.49500 1.000 55.71606 ?  195 ALA A C   1 
ATOM   1422 O  O   . ALA A 1 215 ? 13.26600  -22.03200 -35.65000 1.000 60.45628 ?  195 ALA A O   1 
ATOM   1423 C  CB  . ALA A 1 215 ? 10.94200  -20.21300 -37.25300 1.000 47.37215 ?  195 ALA A CB  1 
ATOM   1424 N  N   . GLU A 1 216 ? 12.90100  -19.95200 -34.86900 1.000 47.29532 ?  196 GLU A N   1 
ATOM   1425 C  CA  . GLU A 1 216 ? 14.26400  -19.73200 -34.38600 1.000 44.62285 ?  196 GLU A CA  1 
ATOM   1426 C  C   . GLU A 1 216 ? 14.23500  -19.50500 -32.87900 1.000 47.07906 ?  196 GLU A C   1 
ATOM   1427 O  O   . GLU A 1 216 ? 14.17900  -18.35500 -32.41400 1.000 43.29671 ?  196 GLU A O   1 
ATOM   1428 C  CB  . GLU A 1 216 ? 14.91000  -18.54900 -35.10500 1.000 50.54078 ?  196 GLU A CB  1 
ATOM   1429 N  N   . PRO A 1 217 ? 14.28900  -20.56800 -32.08000 1.000 42.47633 ?  197 PRO A N   1 
ATOM   1430 C  CA  . PRO A 1 217 ? 14.13400  -20.41300 -30.63000 1.000 42.20550 ?  197 PRO A CA  1 
ATOM   1431 C  C   . PRO A 1 217 ? 15.33600  -19.75100 -29.97600 1.000 40.55891 ?  197 PRO A C   1 
ATOM   1432 O  O   . PRO A 1 217 ? 16.48000  -19.89200 -30.42000 1.000 54.11476 ?  197 PRO A O   1 
ATOM   1433 C  CB  . PRO A 1 217 ? 13.97200  -21.85800 -30.14100 1.000 43.23454 ?  197 PRO A CB  1 
ATOM   1434 C  CG  . PRO A 1 217 ? 13.49000  -22.60300 -31.36000 1.000 51.56373 ?  197 PRO A CG  1 
ATOM   1435 C  CD  . PRO A 1 217 ? 14.28300  -21.98600 -32.46900 1.000 45.00934 ?  197 PRO A CD  1 
ATOM   1436 N  N   . GLY A 1 218 ? 15.05700  -19.02500 -28.89700 1.000 36.73501 ?  198 GLY A N   1 
ATOM   1437 C  CA  . GLY A 1 218 ? 16.09100  -18.45100 -28.05800 1.000 32.01924 ?  198 GLY A CA  1 
ATOM   1438 C  C   . GLY A 1 218 ? 15.98000  -18.92900 -26.62400 1.000 32.19385 ?  198 GLY A C   1 
ATOM   1439 O  O   . GLY A 1 218 ? 15.46800  -20.02300 -26.36800 1.000 36.78134 ?  198 GLY A O   1 
ATOM   1440 N  N   . HIS A 1 219 ? 16.45200  -18.12200 -25.67400 1.000 29.83788 ?  199 HIS A N   1 
ATOM   1441 C  CA  . HIS A 1 219 ? 16.40100  -18.47300 -24.26000 1.000 34.74033 ?  199 HIS A CA  1 
ATOM   1442 C  C   . HIS A 1 219 ? 15.42600  -17.59500 -23.48600 1.000 31.70585 ?  199 HIS A C   1 
ATOM   1443 O  O   . HIS A 1 219 ? 15.48900  -17.53500 -22.25300 1.000 25.45769 ?  199 HIS A O   1 
ATOM   1444 C  CB  . HIS A 1 219 ? 17.79800  -18.39900 -23.64800 1.000 39.23363 ?  199 HIS A CB  1 
ATOM   1445 C  CG  . HIS A 1 219 ? 18.74700  -19.40800 -24.21100 1.000 45.82804 ?  199 HIS A CG  1 
ATOM   1446 N  ND1 . HIS A 1 219 ? 18.60200  -20.76200 -24.00000 1.000 44.67397 ?  199 HIS A ND1 1 
ATOM   1447 C  CD2 . HIS A 1 219 ? 19.84300  -19.26400 -24.99300 1.000 51.14064 ?  199 HIS A CD2 1 
ATOM   1448 C  CE1 . HIS A 1 219 ? 19.57400  -21.40800 -24.61800 1.000 51.46506 ?  199 HIS A CE1 1 
ATOM   1449 N  NE2 . HIS A 1 219 ? 20.34100  -20.52200 -25.22800 1.000 46.89992 ?  199 HIS A NE2 1 
ATOM   1450 N  N   . ASP A 1 220 ? 14.52300  -16.92400 -24.19300 1.000 31.91363 ?  200 ASP A N   1 
ATOM   1451 C  CA  . ASP A 1 220 ? 13.53500  -16.03700 -23.60500 1.000 28.60579 ?  200 ASP A CA  1 
ATOM   1452 C  C   . ASP A 1 220 ? 12.33200  -16.83200 -23.10000 1.000 30.04073 ?  200 ASP A C   1 
ATOM   1453 O  O   . ASP A 1 220 ? 12.22200  -18.04400 -23.30100 1.000 24.82009 ?  200 ASP A O   1 
ATOM   1454 C  CB  . ASP A 1 220 ? 13.09300  -15.00500 -24.63500 1.000 27.42201 ?  200 ASP A CB  1 
ATOM   1455 C  CG  . ASP A 1 220 ? 12.51500  -15.64800 -25.87600 1.000 30.68183 ?  200 ASP A CG  1 
ATOM   1456 O  OD1 . ASP A 1 220 ? 13.30500  -16.14600 -26.70900 1.000 33.20257 ?  200 ASP A OD1 1 
ATOM   1457 O  OD2 . ASP A 1 220 ? 11.27300  -15.66100 -26.01500 1.000 26.95580 -1 200 ASP A OD2 1 
ATOM   1458 N  N   . LEU A 1 221 ? 11.41000  -16.11900 -22.44400 1.000 28.02556 ?  201 LEU A N   1 
ATOM   1459 C  CA  . LEU A 1 221 ? 10.21000  -16.75500 -21.90400 1.000 24.00423 ?  201 LEU A CA  1 
ATOM   1460 C  C   . LEU A 1 221 ? 9.31500   -17.29800 -23.01100 1.000 26.06493 ?  201 LEU A C   1 
ATOM   1461 O  O   . LEU A 1 221 ? 8.80200   -18.42000 -22.91300 1.000 25.58259 ?  201 LEU A O   1 
ATOM   1462 C  CB  . LEU A 1 221 ? 9.43900   -15.76200 -21.03800 1.000 24.04378 ?  201 LEU A CB  1 
ATOM   1463 C  CG  . LEU A 1 221 ? 8.24500   -16.31200 -20.25100 1.000 25.09083 ?  201 LEU A CG  1 
ATOM   1464 C  CD1 . LEU A 1 221 ? 8.63500   -17.49700 -19.37400 1.000 27.71353 ?  201 LEU A CD1 1 
ATOM   1465 C  CD2 . LEU A 1 221 ? 7.62900   -15.20000 -19.41500 1.000 23.24718 ?  201 LEU A CD2 1 
ATOM   1466 N  N   . LEU A 1 222 ? 9.10200   -16.50800 -24.06700 1.000 26.26135 ?  202 LEU A N   1 
ATOM   1467 C  CA  . LEU A 1 222 ? 8.24600   -16.94800 -25.16500 1.000 27.02244 ?  202 LEU A CA  1 
ATOM   1468 C  C   . LEU A 1 222 ? 8.76000   -18.24500 -25.77400 1.000 26.67832 ?  202 LEU A C   1 
ATOM   1469 O  O   . LEU A 1 222 ? 7.99000   -19.18700 -26.00000 1.000 31.71380 ?  202 LEU A O   1 
ATOM   1470 C  CB  . LEU A 1 222 ? 8.15500   -15.85300 -26.22600 1.000 30.34831 ?  202 LEU A CB  1 
ATOM   1471 C  CG  . LEU A 1 222 ? 6.76400   -15.54200 -26.77700 1.000 35.31272 ?  202 LEU A CG  1 
ATOM   1472 C  CD1 . LEU A 1 222 ? 5.74400   -15.44400 -25.64700 1.000 34.89649 ?  202 LEU A CD1 1 
ATOM   1473 C  CD2 . LEU A 1 222 ? 6.80200   -14.25900 -27.58900 1.000 30.88442 ?  202 LEU A CD2 1 
ATOM   1474 N  N   . SER A 1 223 ? 10.06700  -18.31400 -26.04300 1.000 29.77466 ?  203 SER A N   1 
ATOM   1475 C  CA  . SER A 1 223 ? 10.65600  -19.54200 -26.56500 1.000 30.47661 ?  203 SER A CA  1 
ATOM   1476 C  C   . SER A 1 223 ? 10.44200  -20.70400 -25.60300 1.000 29.02891 ?  203 SER A C   1 
ATOM   1477 O  O   . SER A 1 223 ? 10.03900  -21.79900 -26.01200 1.000 34.79570 ?  203 SER A O   1 
ATOM   1478 C  CB  . SER A 1 223 ? 12.14800  -19.33400 -26.83300 1.000 28.78189 ?  203 SER A CB  1 
ATOM   1479 O  OG  . SER A 1 223 ? 12.36000  -18.32300 -27.80400 1.000 29.89862 ?  203 SER A OG  1 
ATOM   1480 N  N   . GLY A 1 224 ? 10.70600  -20.48300 -24.31400 1.000 26.67731 ?  204 GLY A N   1 
ATOM   1481 C  CA  . GLY A 1 224 ? 10.49700  -21.54300 -23.34200 1.000 29.08097 ?  204 GLY A CA  1 
ATOM   1482 C  C   . GLY A 1 224 ? 9.04600   -21.97700 -23.26000 1.000 32.11539 ?  204 GLY A C   1 
ATOM   1483 O  O   . GLY A 1 224 ? 8.75100   -23.16300 -23.09800 1.000 35.99123 ?  204 GLY A O   1 
ATOM   1484 N  N   . LEU A 1 225 ? 8.12000   -21.02100 -23.38300 1.000 28.05509 ?  205 LEU A N   1 
ATOM   1485 C  CA  . LEU A 1 225 ? 6.69800   -21.34800 -23.32600 1.000 30.21696 ?  205 LEU A CA  1 
ATOM   1486 C  C   . LEU A 1 225 ? 6.26400   -22.17600 -24.53000 1.000 36.92668 ?  205 LEU A C   1 
ATOM   1487 O  O   . LEU A 1 225 ? 5.36900   -23.02200 -24.40900 1.000 34.15654 ?  205 LEU A O   1 
ATOM   1488 C  CB  . LEU A 1 225 ? 5.87000   -20.06500 -23.23200 1.000 28.74217 ?  205 LEU A CB  1 
ATOM   1489 C  CG  . LEU A 1 225 ? 5.86900   -19.32800 -21.88800 1.000 30.57236 ?  205 LEU A CG  1 
ATOM   1490 C  CD1 . LEU A 1 225 ? 4.97500   -18.09900 -21.94900 1.000 29.81611 ?  205 LEU A CD1 1 
ATOM   1491 C  CD2 . LEU A 1 225 ? 5.44300   -20.25000 -20.75200 1.000 29.45811 ?  205 LEU A CD2 1 
ATOM   1492 N  N   . ILE A 1 226 ? 6.88000   -21.94600 -25.69300 1.000 30.57997 ?  206 ILE A N   1 
ATOM   1493 C  CA  . ILE A 1 226 ? 6.59500   -22.76400 -26.86900 1.000 34.01873 ?  206 ILE A CA  1 
ATOM   1494 C  C   . ILE A 1 226 ? 7.11800   -24.18100 -26.67100 1.000 36.15710 ?  206 ILE A C   1 
ATOM   1495 O  O   . ILE A 1 226 ? 6.49800   -25.15700 -27.11000 1.000 41.18495 ?  206 ILE A O   1 
ATOM   1496 C  CB  . ILE A 1 226 ? 7.19400   -22.10400 -28.12600 1.000 37.80893 ?  206 ILE A CB  1 
ATOM   1497 C  CG1 . ILE A 1 226 ? 6.39300   -20.85700 -28.50800 1.000 39.32066 ?  206 ILE A CG1 1 
ATOM   1498 C  CG2 . ILE A 1 226 ? 7.24900   -23.08400 -29.28900 1.000 38.62020 ?  206 ILE A CG2 1 
ATOM   1499 C  CD1 . ILE A 1 226 ? 7.21800   -19.79800 -29.20400 1.000 34.67999 ?  206 ILE A CD1 1 
ATOM   1500 N  N   . ALA A 1 227 ? 8.24300   -24.30300 -25.98100 1.000 38.44199 ?  207 ALA A N   1 
ATOM   1501 C  CA  . ALA A 1 227 ? 8.85600   -25.62700 -25.74100 1.000 39.57701 ?  207 ALA A CA  1 
ATOM   1502 C  C   . ALA A 1 227 ? 8.10400   -26.38700 -24.64700 1.000 42.96014 ?  207 ALA A C   1 
ATOM   1503 O  O   . ALA A 1 227 ? 8.19000   -27.61500 -24.62800 1.000 44.98590 ?  207 ALA A O   1 
ATOM   1504 C  CB  . ALA A 1 227 ? 10.28600  -25.42200 -25.36300 1.000 32.72889 ?  207 ALA A CB  1 
ATOM   1505 N  N   . VAL A 1 228 ? 7.37700   -25.67400 -23.79300 1.000 42.51845 ?  208 VAL A N   1 
ATOM   1506 C  CA  . VAL A 1 228 ? 6.66800   -26.30700 -22.64100 1.000 43.87810 ?  208 VAL A CA  1 
ATOM   1507 C  C   . VAL A 1 228 ? 5.76900   -27.44200 -23.13000 1.000 48.80151 ?  208 VAL A C   1 
ATOM   1508 O  O   . VAL A 1 228 ? 5.00300   -27.21900 -24.07900 1.000 51.17659 ?  208 VAL A O   1 
ATOM   1509 C  CB  . VAL A 1 228 ? 5.87500   -25.25900 -21.84200 1.000 40.18385 ?  208 VAL A CB  1 
ATOM   1510 C  CG1 . VAL A 1 228 ? 4.55500   -25.80100 -21.32200 1.000 45.76426 ?  208 VAL A CG1 1 
ATOM   1511 C  CG2 . VAL A 1 228 ? 6.69200   -24.69900 -20.69600 1.000 40.49793 ?  208 VAL A CG2 1 
ATOM   1512 N  N   . ARG A 1 229 ? 5.85500   -28.60200 -22.47200 1.000 48.11255 ?  209 ARG A N   1 
ATOM   1513 C  CA  . ARG A 1 229 ? 5.01700   -29.76300 -22.84200 1.000 53.66390 ?  209 ARG A CA  1 
ATOM   1514 C  C   . ARG A 1 229 ? 4.54500   -30.49600 -21.58800 1.000 55.31926 ?  209 ARG A C   1 
ATOM   1515 O  O   . ARG A 1 229 ? 5.36600   -30.69400 -20.68800 1.000 57.27732 ?  209 ARG A O   1 
ATOM   1516 C  CB  . ARG A 1 229 ? 5.82200   -30.76400 -23.67300 1.000 54.55613 ?  209 ARG A CB  1 
ATOM   1517 C  CG  . ARG A 1 229 ? 6.31900   -30.24200 -25.01000 1.000 60.00512 ?  209 ARG A CG  1 
ATOM   1518 C  CD  . ARG A 1 229 ? 5.18300   -29.94600 -25.96200 1.000 53.13891 ?  209 ARG A CD  1 
ATOM   1519 N  NE  . ARG A 1 229 ? 5.64200   -29.92900 -27.34000 1.000 56.08153 ?  209 ARG A NE  1 
ATOM   1520 C  CZ  . ARG A 1 229 ? 5.91100   -28.83100 -28.03500 1.000 58.87954 ?  209 ARG A CZ  1 
ATOM   1521 N  NH1 . ARG A 1 229 ? 5.67000   -27.63900 -27.52000 1.000 51.46179 ?  209 ARG A NH1 1 
ATOM   1522 N  NH2 . ARG A 1 229 ? 6.41000   -28.93500 -29.25400 1.000 60.04335 ?  209 ARG A NH2 1 
ATOM   1523 N  N   . ASP A 1 230 ? 3.26100   -30.84200 -21.52000 1.000 58.79417 ?  210 ASP A N   1 
ATOM   1524 C  CA  . ASP A 1 230 ? 2.77600   -31.69800 -20.40900 1.000 60.52329 ?  210 ASP A CA  1 
ATOM   1525 C  C   . ASP A 1 230 ? 2.18100   -32.93500 -21.06900 1.000 62.27897 ?  210 ASP A C   1 
ATOM   1526 O  O   . ASP A 1 230 ? 1.01000   -32.89000 -21.44800 1.000 61.05716 ?  210 ASP A O   1 
ATOM   1527 C  CB  . ASP A 1 230 ? 1.76800   -31.02400 -19.48500 1.000 58.80465 ?  210 ASP A CB  1 
ATOM   1528 C  CG  . ASP A 1 230 ? 1.00900   -32.01400 -18.62000 1.000 64.03272 ?  210 ASP A CG  1 
ATOM   1529 O  OD1 . ASP A 1 230 ? 1.65900   -32.70800 -17.82400 1.000 68.44240 ?  210 ASP A OD1 1 
ATOM   1530 O  OD2 . ASP A 1 230 ? -0.22200  -32.09400 -18.76900 1.000 63.11385 -1 210 ASP A OD2 1 
ATOM   1531 N  N   . ASP A 1 231 ? 3.00100   -33.96200 -21.26300 1.000 63.50969 ?  211 ASP A N   1 
ATOM   1532 C  CA  . ASP A 1 231 ? 2.51800   -35.19700 -21.87200 1.000 66.43588 ?  211 ASP A CA  1 
ATOM   1533 C  C   . ASP A 1 231 ? 1.60800   -34.90300 -23.05900 1.000 68.40177 ?  211 ASP A C   1 
ATOM   1534 O  O   . ASP A 1 231 ? 0.40400   -35.17800 -23.00000 1.000 71.39608 ?  211 ASP A O   1 
ATOM   1535 C  CB  . ASP A 1 231 ? 1.78500   -36.05500 -20.83700 1.000 61.66608 ?  211 ASP A CB  1 
ATOM   1536 N  N   . GLU A 1 232 ? 2.18100   -34.30300 -24.10900 1.000 66.30829 ?  212 GLU A N   1 
ATOM   1537 C  CA  . GLU A 1 232 ? 1.51100   -33.91300 -25.35000 1.000 66.38602 ?  212 GLU A CA  1 
ATOM   1538 C  C   . GLU A 1 232 ? 0.67700   -32.64000 -25.22400 1.000 63.30586 ?  212 GLU A C   1 
ATOM   1539 O  O   . GLU A 1 232 ? 0.23300   -32.09600 -26.24100 1.000 64.40873 ?  212 GLU A O   1 
ATOM   1540 C  CB  . GLU A 1 232 ? 0.56200   -35.01000 -25.84700 1.000 66.47775 ?  212 GLU A CB  1 
ATOM   1541 N  N   . ASP A 1 233 ? 0.45300   -32.14700 -24.00600 1.000 62.79963 ?  213 ASP A N   1 
ATOM   1542 C  CA  . ASP A 1 233 ? -0.28700  -30.89900 -23.84400 1.000 60.02891 ?  213 ASP A CA  1 
ATOM   1543 C  C   . ASP A 1 233 ? 0.69600   -29.75400 -24.05900 1.000 50.96041 ?  213 ASP A C   1 
ATOM   1544 O  O   . ASP A 1 233 ? 1.81300   -29.76900 -23.53300 1.000 54.69963 ?  213 ASP A O   1 
ATOM   1545 C  CB  . ASP A 1 233 ? -0.92300  -30.78800 -22.45800 1.000 58.07064 ?  213 ASP A CB  1 
ATOM   1546 C  CG  . ASP A 1 233 ? -1.92400  -29.64600 -22.36500 1.000 46.80607 ?  213 ASP A CG  1 
ATOM   1547 O  OD1 . ASP A 1 233 ? -2.27900  -29.07300 -23.41900 1.000 45.38738 ?  213 ASP A OD1 1 
ATOM   1548 O  OD2 . ASP A 1 233 ? -2.34700  -29.31400 -21.23700 1.000 47.01028 -1 213 ASP A OD2 1 
ATOM   1549 N  N   . ARG A 1 234 ? 0.26900   -28.75400 -24.82800 1.000 49.61316 ?  214 ARG A N   1 
ATOM   1550 C  CA  . ARG A 1 234 ? 1.09900   -27.60500 -25.15500 1.000 44.80885 ?  214 ARG A CA  1 
ATOM   1551 C  C   . ARG A 1 234 ? 0.25400   -26.34100 -25.09300 1.000 37.72118 ?  214 ARG A C   1 
ATOM   1552 O  O   . ARG A 1 234 ? -0.97700  -26.39000 -25.01800 1.000 35.35871 ?  214 ARG A O   1 
ATOM   1553 C  CB  . ARG A 1 234 ? 1.73300   -27.74400 -26.54500 1.000 46.44503 ?  214 ARG A CB  1 
ATOM   1554 C  CG  . ARG A 1 234 ? 0.83300   -28.41500 -27.57000 1.000 42.23665 ?  214 ARG A CG  1 
ATOM   1555 N  N   . LEU A 1 235 ? 0.93600   -25.19900 -25.13200 1.000 39.35925 ?  215 LEU A N   1 
ATOM   1556 C  CA  . LEU A 1 235 ? 0.27800   -23.90200 -25.19600 1.000 31.98471 ?  215 LEU A CA  1 
ATOM   1557 C  C   . LEU A 1 235 ? 0.00800   -23.53300 -26.65000 1.000 31.50270 ?  215 LEU A C   1 
ATOM   1558 O  O   . LEU A 1 235 ? 0.86400   -23.72300 -27.52000 1.000 32.94798 ?  215 LEU A O   1 
ATOM   1559 C  CB  . LEU A 1 235 ? 1.14000   -22.82400 -24.53500 1.000 30.24917 ?  215 LEU A CB  1 
ATOM   1560 C  CG  . LEU A 1 235 ? 1.22900   -22.81800 -23.00700 1.000 28.51861 ?  215 LEU A CG  1 
ATOM   1561 C  CD1 . LEU A 1 235 ? 2.36700   -21.92200 -22.53900 1.000 23.79609 ?  215 LEU A CD1 1 
ATOM   1562 C  CD2 . LEU A 1 235 ? -0.08600  -22.37900 -22.38600 1.000 29.43706 ?  215 LEU A CD2 1 
ATOM   1563 N  N   . SER A 1 236 ? -1.18400  -23.00600 -26.90900 1.000 33.39502 ?  216 SER A N   1 
ATOM   1564 C  CA  . SER A 1 236 ? -1.57300  -22.64400 -28.26300 1.000 34.17582 ?  216 SER A CA  1 
ATOM   1565 C  C   . SER A 1 236 ? -1.05000  -21.25600 -28.62600 1.000 36.89839 ?  216 SER A C   1 
ATOM   1566 O  O   . SER A 1 236 ? -0.63300  -20.47800 -27.76400 1.000 32.96294 ?  216 SER A O   1 
ATOM   1567 C  CB  . SER A 1 236 ? -3.09300  -22.68500 -28.40700 1.000 31.14771 ?  216 SER A CB  1 
ATOM   1568 O  OG  . SER A 1 236 ? -3.67400  -21.46700 -27.97500 1.000 38.50404 ?  216 SER A OG  1 
ATOM   1569 N  N   . GLU A 1 237 ? -1.07800  -20.95400 -29.93100 1.000 35.88184 ?  217 GLU A N   1 
ATOM   1570 C  CA  . GLU A 1 237 ? -0.71500  -19.61600 -30.39700 1.000 37.26220 ?  217 GLU A CA  1 
ATOM   1571 C  C   . GLU A 1 237 ? -1.53300  -18.54500 -29.69300 1.000 29.86273 ?  217 GLU A C   1 
ATOM   1572 O  O   . GLU A 1 237 ? -0.98300  -17.56100 -29.18300 1.000 31.78754 ?  217 GLU A O   1 
ATOM   1573 C  CB  . GLU A 1 237 ? -0.91000  -19.49500 -31.91100 1.000 44.29731 ?  217 GLU A CB  1 
ATOM   1574 C  CG  . GLU A 1 237 ? -0.25500  -18.24100 -32.49700 1.000 50.66521 ?  217 GLU A CG  1 
ATOM   1575 C  CD  . GLU A 1 237 ? -0.41600  -18.12300 -34.00300 1.000 49.78425 ?  217 GLU A CD  1 
ATOM   1576 O  OE1 . GLU A 1 237 ? -1.48400  -18.51500 -34.51800 1.000 52.70420 ?  217 GLU A OE1 1 
ATOM   1577 O  OE2 . GLU A 1 237 ? 0.51500   -17.61900 -34.66700 1.000 55.13410 -1 217 GLU A OE2 1 
ATOM   1578 N  N   . ALA A 1 238 ? -2.85900  -18.71200 -29.67800 1.000 29.39251 ?  218 ALA A N   1 
ATOM   1579 C  CA  . ALA A 1 238 ? -3.72000  -17.74600 -29.00400 1.000 33.57446 ?  218 ALA A CA  1 
ATOM   1580 C  C   . ALA A 1 238 ? -3.36200  -17.62800 -27.52900 1.000 29.22671 ?  218 ALA A C   1 
ATOM   1581 O  O   . ALA A 1 238 ? -3.34300  -16.52300 -26.97300 1.000 25.14953 ?  218 ALA A O   1 
ATOM   1582 C  CB  . ALA A 1 238 ? -5.18800  -18.14100 -29.17000 1.000 35.91212 ?  218 ALA A CB  1 
ATOM   1583 N  N   . GLU A 1 239 ? -3.06400  -18.75800 -26.88300 1.000 26.81835 ?  219 GLU A N   1 
ATOM   1584 C  CA  . GLU A 1 239 ? -2.69300  -18.73600 -25.47300 1.000 26.22071 ?  219 GLU A CA  1 
ATOM   1585 C  C   . GLU A 1 239 ? -1.35700  -18.03200 -25.26900 1.000 25.93566 ?  219 GLU A C   1 
ATOM   1586 O  O   . GLU A 1 239 ? -1.18500  -17.28200 -24.30200 1.000 26.11786 ?  219 GLU A O   1 
ATOM   1587 C  CB  . GLU A 1 239 ? -2.64200  -20.16500 -24.93200 1.000 26.16788 ?  219 GLU A CB  1 
ATOM   1588 C  CG  . GLU A 1 239 ? -4.00600  -20.82800 -24.83400 1.000 32.84951 ?  219 GLU A CG  1 
ATOM   1589 C  CD  . GLU A 1 239 ? -3.92800  -22.30700 -24.50200 1.000 34.27222 ?  219 GLU A CD  1 
ATOM   1590 O  OE1 . GLU A 1 239 ? -2.88300  -22.93000 -24.78500 1.000 34.60156 ?  219 GLU A OE1 1 
ATOM   1591 O  OE2 . GLU A 1 239 ? -4.92100  -22.85000 -23.97300 1.000 39.30779 -1 219 GLU A OE2 1 
ATOM   1592 N  N   . LEU A 1 240 ? -0.40000  -18.26100 -26.17200 1.000 26.76756 ?  220 LEU A N   1 
ATOM   1593 C  CA  . LEU A 1 240 ? 0.89500   -17.59700 -26.07200 1.000 26.58749 ?  220 LEU A CA  1 
ATOM   1594 C  C   . LEU A 1 240 ? 0.75500   -16.09500 -26.28100 1.000 21.73271 ?  220 LEU A C   1 
ATOM   1595 O  O   . LEU A 1 240 ? 1.29200   -15.29700 -25.50600 1.000 24.66229 ?  220 LEU A O   1 
ATOM   1596 C  CB  . LEU A 1 240 ? 1.86600   -18.19100 -27.09300 1.000 34.33196 ?  220 LEU A CB  1 
ATOM   1597 C  CG  . LEU A 1 240 ? 2.32500   -19.62900 -26.84300 1.000 32.90916 ?  220 LEU A CG  1 
ATOM   1598 C  CD1 . LEU A 1 240 ? 2.76200   -20.28700 -28.14300 1.000 34.57330 ?  220 LEU A CD1 1 
ATOM   1599 C  CD2 . LEU A 1 240 ? 3.44400   -19.67300 -25.82100 1.000 35.41528 ?  220 LEU A CD2 1 
ATOM   1600 N  N   . VAL A 1 241 ? 0.02400   -15.69600 -27.32400 1.000 24.45339 ?  221 VAL A N   1 
ATOM   1601 C  CA  . VAL A 1 241 ? -0.17400  -14.27800 -27.60600 1.000 20.45812 ?  221 VAL A CA  1 
ATOM   1602 C  C   . VAL A 1 241 ? -0.93500  -13.60700 -26.47000 1.000 25.13877 ?  221 VAL A C   1 
ATOM   1603 O  O   . VAL A 1 241 ? -0.59900  -12.49200 -26.05400 1.000 15.14299 ?  221 VAL A O   1 
ATOM   1604 C  CB  . VAL A 1 241 ? -0.89400  -14.10600 -28.95800 1.000 22.64063 ?  221 VAL A CB  1 
ATOM   1605 C  CG1 . VAL A 1 241 ? -1.35900  -12.66700 -29.14500 1.000 22.77511 ?  221 VAL A CG1 1 
ATOM   1606 C  CG2 . VAL A 1 241 ? 0.02400   -14.52900 -30.09500 1.000 23.81261 ?  221 VAL A CG2 1 
ATOM   1607 N  N   . SER A 1 242 ? -1.97500  -14.27300 -25.95300 1.000 25.06246 ?  222 SER A N   1 
ATOM   1608 C  CA  . SER A 1 242 ? -2.71500  -13.71900 -24.82200 1.000 23.89852 ?  222 SER A CA  1 
ATOM   1609 C  C   . SER A 1 242 ? -1.81400  -13.53900 -23.60800 1.000 18.65209 ?  222 SER A C   1 
ATOM   1610 O  O   . SER A 1 242 ? -1.89300  -12.51800 -22.91300 1.000 20.22357 ?  222 SER A O   1 
ATOM   1611 C  CB  . SER A 1 242 ? -3.90200  -14.61500 -24.47100 1.000 22.60087 ?  222 SER A CB  1 
ATOM   1612 O  OG  . SER A 1 242 ? -4.81100  -14.69900 -25.55000 1.000 32.79600 ?  222 SER A OG  1 
ATOM   1613 N  N   . MET A 1 243 ? -0.95400  -14.52100 -23.33500 1.000 19.72352 ?  223 MET A N   1 
ATOM   1614 C  CA  . MET A 1 243 ? -0.03500  -14.40300 -22.20800 1.000 22.95110 ?  223 MET A CA  1 
ATOM   1615 C  C   . MET A 1 243 ? 0.93300   -13.24400 -22.40600 1.000 18.14532 ?  223 MET A C   1 
ATOM   1616 O  O   . MET A 1 243 ? 1.26400   -12.53100 -21.45100 1.000 15.70702 ?  223 MET A O   1 
ATOM   1617 C  CB  . MET A 1 243 ? 0.72300   -15.71400 -22.00700 1.000 16.41274 ?  223 MET A CB  1 
ATOM   1618 C  CG  . MET A 1 243 ? 1.86000   -15.61100 -21.01200 1.000 30.23711 ?  223 MET A CG  1 
ATOM   1619 S  SD  . MET A 1 243 ? 1.22400   -15.46300 -19.33000 1.000 30.42453 ?  223 MET A SD  1 
ATOM   1620 C  CE  . MET A 1 243 ? 2.53300   -14.50700 -18.56800 1.000 27.98007 ?  223 MET A CE  1 
ATOM   1621 N  N   . ALA A 1 244 ? 1.38400   -13.03100 -23.64700 1.000 18.32983 ?  224 ALA A N   1 
ATOM   1622 C  CA  . ALA A 1 244 ? 2.25000   -11.89100 -23.93700 1.000 19.60003 ?  224 ALA A CA  1 
ATOM   1623 C  C   . ALA A 1 244 ? 1.54700   -10.57500 -23.64000 1.000 16.78650 ?  224 ALA A C   1 
ATOM   1624 O  O   . ALA A 1 244 ? 2.15700   -9.64800  -23.09100 1.000 17.21414 ?  224 ALA A O   1 
ATOM   1625 C  CB  . ALA A 1 244 ? 2.70800   -11.93900 -25.39500 1.000 24.37318 ?  224 ALA A CB  1 
ATOM   1626 N  N   . PHE A 1 245 ? 0.26300   -10.47100 -24.00300 1.000 19.41168 ?  225 PHE A N   1 
ATOM   1627 C  CA  . PHE A 1 245 ? -0.50500  -9.27300  -23.67600 1.000 16.84667 ?  225 PHE A CA  1 
ATOM   1628 C  C   . PHE A 1 245 ? -0.58200  -9.06300  -22.17200 1.000 15.87509 ?  225 PHE A C   1 
ATOM   1629 O  O   . PHE A 1 245 ? -0.43200  -7.93700  -21.68500 1.000 16.71710 ?  225 PHE A O   1 
ATOM   1630 C  CB  . PHE A 1 245 ? -1.91200  -9.37400  -24.26900 1.000 18.11432 ?  225 PHE A CB  1 
ATOM   1631 C  CG  . PHE A 1 245 ? -2.06200  -8.69300  -25.60200 1.000 19.41612 ?  225 PHE A CG  1 
ATOM   1632 C  CD1 . PHE A 1 245 ? -1.83100  -7.33300  -25.73500 1.000 21.21314 ?  225 PHE A CD1 1 
ATOM   1633 C  CD2 . PHE A 1 245 ? -2.44500  -9.41700  -26.72200 1.000 23.46825 ?  225 PHE A CD2 1 
ATOM   1634 C  CE1 . PHE A 1 245 ? -1.97100  -6.70700  -26.96400 1.000 24.29582 ?  225 PHE A CE1 1 
ATOM   1635 C  CE2 . PHE A 1 245 ? -2.58700  -8.80100  -27.95200 1.000 20.99655 ?  225 PHE A CE2 1 
ATOM   1636 C  CZ  . PHE A 1 245 ? -2.35000  -7.44600  -28.07700 1.000 23.13528 ?  225 PHE A CZ  1 
ATOM   1637 N  N   . LEU A 1 246 ? -0.83300  -10.13900 -21.42200 1.000 18.88980 ?  226 LEU A N   1 
ATOM   1638 C  CA  . LEU A 1 246 ? -0.85700  -10.05100 -19.96600 1.000 18.32650 ?  226 LEU A CA  1 
ATOM   1639 C  C   . LEU A 1 246 ? 0.47500   -9.55500  -19.42800 1.000 16.57915 ?  226 LEU A C   1 
ATOM   1640 O  O   . LEU A 1 246 ? 0.51700   -8.71000  -18.52600 1.000 19.30078 ?  226 LEU A O   1 
ATOM   1641 C  CB  . LEU A 1 246 ? -1.18300  -11.41900 -19.37300 1.000 20.51095 ?  226 LEU A CB  1 
ATOM   1642 C  CG  . LEU A 1 246 ? -2.63700  -11.87900 -19.39800 1.000 29.31970 ?  226 LEU A CG  1 
ATOM   1643 C  CD1 . LEU A 1 246 ? -2.80100  -13.11900 -18.53300 1.000 18.37040 ?  226 LEU A CD1 1 
ATOM   1644 C  CD2 . LEU A 1 246 ? -3.55800  -10.76500 -18.93900 1.000 24.71343 ?  226 LEU A CD2 1 
ATOM   1645 N  N   . ALA A 1 247 ? 1.57600   -10.08000 -19.96700 1.000 16.98948 ?  227 ALA A N   1 
ATOM   1646 C  CA  . ALA A 1 247 ? 2.89300   -9.64700  -19.51500 1.000 15.64475 ?  227 ALA A CA  1 
ATOM   1647 C  C   . ALA A 1 247 ? 3.12300   -8.17100  -19.81100 1.000 18.10919 ?  227 ALA A C   1 
ATOM   1648 O  O   . ALA A 1 247 ? 3.72600   -7.46100  -18.99900 1.000 18.71604 ?  227 ALA A O   1 
ATOM   1649 C  CB  . ALA A 1 247 ? 3.97600   -10.50500 -20.16600 1.000 23.17228 ?  227 ALA A CB  1 
ATOM   1650 N  N   . LEU A 1 248 ? 2.65100   -7.68800  -20.96600 1.000 17.75948 ?  228 LEU A N   1 
ATOM   1651 C  CA  . LEU A 1 248 ? 2.79900   -6.27100  -21.28500 1.000 18.38232 ?  228 LEU A CA  1 
ATOM   1652 C  C   . LEU A 1 248 ? 2.02800   -5.39800  -20.30400 1.000 18.60749 ?  228 LEU A C   1 
ATOM   1653 O  O   . LEU A 1 248 ? 2.54100   -4.37100  -19.84300 1.000 19.21785 ?  228 LEU A O   1 
ATOM   1654 C  CB  . LEU A 1 248 ? 2.32700   -5.99300  -22.71000 1.000 18.22383 ?  228 LEU A CB  1 
ATOM   1655 C  CG  . LEU A 1 248 ? 3.25300   -6.38600  -23.85400 1.000 19.98145 ?  228 LEU A CG  1 
ATOM   1656 C  CD1 . LEU A 1 248 ? 2.53100   -6.27800  -25.19100 1.000 19.97304 ?  228 LEU A CD1 1 
ATOM   1657 C  CD2 . LEU A 1 248 ? 4.52500   -5.54400  -23.83700 1.000 25.71733 ?  228 LEU A CD2 1 
ATOM   1658 N  N   . TRP A 1 249 ? 0.78500   -5.78100  -19.99100 1.000 16.84473 ?  229 TRP A N   1 
ATOM   1659 C  CA  . TRP A 1 249 ? -0.03400  -5.01300  -19.05700 1.000 19.39910 ?  229 TRP A CA  1 
ATOM   1660 C  C   . TRP A 1 249 ? 0.66400   -4.85700  -17.71300 1.000 21.05511 ?  229 TRP A C   1 
ATOM   1661 O  O   . TRP A 1 249 ? 0.85000   -3.74200  -17.21400 1.000 19.91507 ?  229 TRP A O   1 
ATOM   1662 C  CB  . TRP A 1 249 ? -1.39600  -5.69200  -18.87300 1.000 22.00296 ?  229 TRP A CB  1 
ATOM   1663 C  CG  . TRP A 1 249 ? -2.09400  -5.33800  -17.57900 1.000 23.82751 ?  229 TRP A CG  1 
ATOM   1664 C  CD1 . TRP A 1 249 ? -2.69400  -4.15000  -17.26400 1.000 25.04370 ?  229 TRP A CD1 1 
ATOM   1665 C  CD2 . TRP A 1 249 ? -2.27200  -6.19000  -16.43300 1.000 18.99996 ?  229 TRP A CD2 1 
ATOM   1666 N  NE1 . TRP A 1 249 ? -3.22400  -4.20800  -15.99600 1.000 21.93464 ?  229 TRP A NE1 1 
ATOM   1667 C  CE2 . TRP A 1 249 ? -2.98100  -5.44800  -15.46500 1.000 21.56011 ?  229 TRP A CE2 1 
ATOM   1668 C  CE3 . TRP A 1 249 ? -1.90400  -7.50700  -16.13600 1.000 21.16797 ?  229 TRP A CE3 1 
ATOM   1669 C  CZ2 . TRP A 1 249 ? -3.32400  -5.97700  -14.21500 1.000 17.10255 ?  229 TRP A CZ2 1 
ATOM   1670 C  CZ3 . TRP A 1 249 ? -2.24800  -8.03200  -14.89500 1.000 20.39018 ?  229 TRP A CZ3 1 
ATOM   1671 C  CH2 . TRP A 1 249 ? -2.94800  -7.26700  -13.95100 1.000 16.96425 ?  229 TRP A CH2 1 
ATOM   1672 N  N   . ALA A 1 250 ? 1.05100   -5.97100  -17.10400 1.000 17.80528 ?  230 ALA A N   1 
ATOM   1673 C  CA  . ALA A 1 250 ? 1.59700   -5.89900  -15.75700 1.000 20.05317 ?  230 ALA A CA  1 
ATOM   1674 C  C   . ALA A 1 250 ? 3.08500   -5.56900  -15.76700 1.000 18.77823 ?  230 ALA A C   1 
ATOM   1675 O  O   . ALA A 1 250 ? 3.57100   -4.84100  -14.89200 1.000 22.74693 ?  230 ALA A O   1 
ATOM   1676 C  CB  . ALA A 1 250 ? 1.33800   -7.21600  -15.03400 1.000 20.71383 ?  230 ALA A CB  1 
ATOM   1677 N  N   . GLY A 1 251 ? 3.82000   -6.09600  -16.74000 1.000 23.60144 ?  231 GLY A N   1 
ATOM   1678 C  CA  . GLY A 1 251 ? 5.24400   -5.83900  -16.82700 1.000 21.48727 ?  231 GLY A CA  1 
ATOM   1679 C  C   . GLY A 1 251 ? 5.62000   -4.46600  -17.32900 1.000 24.82212 ?  231 GLY A C   1 
ATOM   1680 O  O   . GLY A 1 251 ? 6.78100   -4.06700  -17.19200 1.000 24.87125 ?  231 GLY A O   1 
ATOM   1681 N  N   . TYR A 1 252 ? 4.67300   -3.73100  -17.91000 1.000 21.91423 ?  232 TYR A N   1 
ATOM   1682 C  CA  . TYR A 1 252 ? 4.93000   -2.35700  -18.31600 1.000 18.44247 ?  232 TYR A CA  1 
ATOM   1683 C  C   . TYR A 1 252 ? 3.98200   -1.37900  -17.63800 1.000 18.78916 ?  232 TYR A C   1 
ATOM   1684 O  O   . TYR A 1 252 ? 4.44000   -0.52700  -16.87300 1.000 21.57513 ?  232 TYR A O   1 
ATOM   1685 C  CB  . TYR A 1 252 ? 4.85300   -2.23400  -19.84300 1.000 19.93924 ?  232 TYR A CB  1 
ATOM   1686 C  CG  . TYR A 1 252 ? 5.07300   -0.82600  -20.33000 1.000 26.16480 ?  232 TYR A CG  1 
ATOM   1687 C  CD1 . TYR A 1 252 ? 6.33400   -0.23900  -20.28100 1.000 21.78238 ?  232 TYR A CD1 1 
ATOM   1688 C  CD2 . TYR A 1 252 ? 4.02000   -0.07700  -20.82900 1.000 20.48492 ?  232 TYR A CD2 1 
ATOM   1689 C  CE1 . TYR A 1 252 ? 6.53200   1.05200   -20.72800 1.000 22.99247 ?  232 TYR A CE1 1 
ATOM   1690 C  CE2 . TYR A 1 252 ? 4.20800   1.20700   -21.27500 1.000 23.91049 ?  232 TYR A CE2 1 
ATOM   1691 C  CZ  . TYR A 1 252 ? 5.46000   1.77300   -21.22000 1.000 27.01615 ?  232 TYR A CZ  1 
ATOM   1692 O  OH  . TYR A 1 252 ? 5.63200   3.06400   -21.66800 1.000 29.38533 ?  232 TYR A OH  1 
ATOM   1693 N  N   . GLU A 1 253 ? 2.67200   -1.47900  -17.87400 1.000 16.67778 ?  233 GLU A N   1 
ATOM   1694 C  CA  . GLU A 1 253 ? 1.76000   -0.46700  -17.34600 1.000 19.74754 ?  233 GLU A CA  1 
ATOM   1695 C  C   . GLU A 1 253 ? 1.81700   -0.40200  -15.82300 1.000 17.15336 ?  233 GLU A C   1 
ATOM   1696 O  O   . GLU A 1 253 ? 1.91400   0.68500   -15.24200 1.000 26.68261 ?  233 GLU A O   1 
ATOM   1697 C  CB  . GLU A 1 253 ? 0.33200   -0.73400  -17.81800 1.000 24.23210 ?  233 GLU A CB  1 
ATOM   1698 C  CG  . GLU A 1 253 ? -0.60900  0.41400   -17.51900 1.000 25.11044 ?  233 GLU A CG  1 
ATOM   1699 C  CD  . GLU A 1 253 ? -2.04800  0.08600   -17.83800 1.000 26.16383 ?  233 GLU A CD  1 
ATOM   1700 O  OE1 . GLU A 1 253 ? -2.29400  -0.95400  -18.48200 1.000 28.99608 ?  233 GLU A OE1 1 
ATOM   1701 O  OE2 . GLU A 1 253 ? -2.93400  0.86900   -17.44100 1.000 39.35263 -1 233 GLU A OE2 1 
ATOM   1702 N  N   . ASN A 1 254 ? 1.76200   -1.55700  -15.15500 1.000 20.59204 ?  234 ASN A N   1 
ATOM   1703 C  CA  . ASN A 1 254 ? 1.83800   -1.55400  -13.69700 1.000 21.20527 ?  234 ASN A CA  1 
ATOM   1704 C  C   . ASN A 1 254 ? 3.21600   -1.11200  -13.21200 1.000 16.60468 ?  234 ASN A C   1 
ATOM   1705 O  O   . ASN A 1 254 ? 3.32600   -0.30600  -12.28300 1.000 17.45533 ?  234 ASN A O   1 
ATOM   1706 C  CB  . ASN A 1 254 ? 1.49900   -2.93800  -13.13800 1.000 19.42437 ?  234 ASN A CB  1 
ATOM   1707 C  CG  . ASN A 1 254 ? 0.04000   -3.30500  -13.32800 1.000 22.72142 ?  234 ASN A CG  1 
ATOM   1708 O  OD1 . ASN A 1 254 ? -0.77700  -2.46100  -13.67600 1.000 27.40027 ?  234 ASN A OD1 1 
ATOM   1709 N  ND2 . ASN A 1 254 ? -0.29400  -4.57100  -13.08700 1.000 19.42243 ?  234 ASN A ND2 1 
ATOM   1710 N  N   . LEU A 1 255 ? 4.27700   -1.62500  -13.83100 1.000 18.30227 ?  235 LEU A N   1 
ATOM   1711 C  CA  . LEU A 1 255 ? 5.61400   -1.37500  -13.30600 1.000 17.12841 ?  235 LEU A CA  1 
ATOM   1712 C  C   . LEU A 1 255 ? 6.04200   0.07000   -13.52500 1.000 17.62326 ?  235 LEU A C   1 
ATOM   1713 O  O   . LEU A 1 255 ? 6.72700   0.65200   -12.67500 1.000 18.79034 ?  235 LEU A O   1 
ATOM   1714 C  CB  . LEU A 1 255 ? 6.62200   -2.32800  -13.94400 1.000 22.36744 ?  235 LEU A CB  1 
ATOM   1715 C  CG  . LEU A 1 255 ? 7.25600   -3.32100  -12.97100 1.000 29.18705 ?  235 LEU A CG  1 
ATOM   1716 C  CD1 . LEU A 1 255 ? 8.24700   -4.21700  -13.69600 1.000 20.99733 ?  235 LEU A CD1 1 
ATOM   1717 C  CD2 . LEU A 1 255 ? 7.92200   -2.59700  -11.80100 1.000 26.67042 ?  235 LEU A CD2 1 
ATOM   1718 N  N   . VAL A 1 256 ? 5.65500   0.66400   -14.65900 1.000 15.04835 ?  236 VAL A N   1 
ATOM   1719 C  CA  . VAL A 1 256 ? 6.04300   2.04400   -14.94700 1.000 14.76347 ?  236 VAL A CA  1 
ATOM   1720 C  C   . VAL A 1 256 ? 5.55700   2.97800   -13.85000 1.000 19.59080 ?  236 VAL A C   1 
ATOM   1721 O  O   . VAL A 1 256 ? 6.26900   3.90100   -13.43400 1.000 14.21453 ?  236 VAL A O   1 
ATOM   1722 C  CB  . VAL A 1 256 ? 5.51000   2.47900   -16.32400 1.000 17.77785 ?  236 VAL A CB  1 
ATOM   1723 C  CG1 . VAL A 1 256 ? 5.59400   3.99200   -16.46900 1.000 18.92651 ?  236 VAL A CG1 1 
ATOM   1724 C  CG2 . VAL A 1 256 ? 6.30700   1.81500   -17.41400 1.000 22.10243 ?  236 VAL A CG2 1 
ATOM   1725 N  N   . HIS A 1 257 ? 4.34200   2.76100   -13.36200 1.000 13.86315 ?  237 HIS A N   1 
ATOM   1726 C  CA  . HIS A 1 257 ? 3.79700   3.67800   -12.37500 1.000 15.58944 ?  237 HIS A CA  1 
ATOM   1727 C  C   . HIS A 1 257 ? 4.08600   3.25300   -10.94700 1.000 15.81571 ?  237 HIS A C   1 
ATOM   1728 O  O   . HIS A 1 257 ? 4.03600   4.09300   -10.04500 1.000 17.35326 ?  237 HIS A O   1 
ATOM   1729 C  CB  . HIS A 1 257 ? 2.30000   3.84200   -12.61700 1.000 15.12312 ?  237 HIS A CB  1 
ATOM   1730 C  CG  . HIS A 1 257 ? 2.00400   4.47200   -13.93900 1.000 20.78380 ?  237 HIS A CG  1 
ATOM   1731 N  ND1 . HIS A 1 257 ? 2.52900   5.69200   -14.30600 1.000 25.71150 ?  237 HIS A ND1 1 
ATOM   1732 C  CD2 . HIS A 1 257 ? 1.29900   4.02900   -15.00500 1.000 25.43790 ?  237 HIS A CD2 1 
ATOM   1733 C  CE1 . HIS A 1 257 ? 2.13300   5.98800   -15.53100 1.000 23.48477 ?  237 HIS A CE1 1 
ATOM   1734 N  NE2 . HIS A 1 257 ? 1.38600   4.99400   -15.97700 1.000 29.07697 ?  237 HIS A NE2 1 
ATOM   1735 N  N   . LEU A 1 258 ? 4.41300   1.98100   -10.71700 1.000 14.26433 ?  238 LEU A N   1 
ATOM   1736 C  CA  . LEU A 1 258 ? 4.99700   1.62100   -9.43100  1.000 17.20541 ?  238 LEU A CA  1 
ATOM   1737 C  C   . LEU A 1 258 ? 6.26700   2.43200   -9.18000  1.000 17.82430 ?  238 LEU A C   1 
ATOM   1738 O  O   . LEU A 1 258 ? 6.47900   2.95300   -8.07800  1.000 17.18317 ?  238 LEU A O   1 
ATOM   1739 C  CB  . LEU A 1 258 ? 5.28400   0.11900   -9.39000  1.000 19.64442 ?  238 LEU A CB  1 
ATOM   1740 C  CG  . LEU A 1 258 ? 5.78800   -0.41700  -8.05200  1.000 22.53228 ?  238 LEU A CG  1 
ATOM   1741 C  CD1 . LEU A 1 258 ? 4.78400   -0.13700  -6.95700  1.000 19.27486 ?  238 LEU A CD1 1 
ATOM   1742 C  CD2 . LEU A 1 258 ? 6.08400   -1.90100  -8.14500  1.000 27.52422 ?  238 LEU A CD2 1 
ATOM   1743 N  N   . ILE A 1 259 ? 7.09700   2.59000   -10.21100 1.000 17.92845 ?  239 ILE A N   1 
ATOM   1744 C  CA  . ILE A 1 259 ? 8.31700   3.38100   -10.07700 1.000 13.54433 ?  239 ILE A CA  1 
ATOM   1745 C  C   . ILE A 1 259 ? 7.99000   4.86300   -9.95900  1.000 16.52955 ?  239 ILE A C   1 
ATOM   1746 O  O   . ILE A 1 259 ? 8.50000   5.55300   -9.07100  1.000 18.13421 ?  239 ILE A O   1 
ATOM   1747 C  CB  . ILE A 1 259 ? 9.27700   3.11800   -11.24800 1.000 18.51825 ?  239 ILE A CB  1 
ATOM   1748 C  CG1 . ILE A 1 259 ? 9.69500   1.64500   -11.28200 1.000 21.69385 ?  239 ILE A CG1 1 
ATOM   1749 C  CG2 . ILE A 1 259 ? 10.49200  4.02100   -11.15500 1.000 16.57228 ?  239 ILE A CG2 1 
ATOM   1750 C  CD1 . ILE A 1 259 ? 10.27600  1.21300   -12.61800 1.000 17.72582 ?  239 ILE A CD1 1 
ATOM   1751 N  N   . GLY A 1 260 ? 7.15600   5.38000   -10.86600 1.000 13.47255 ?  240 GLY A N   1 
ATOM   1752 C  CA  . GLY A 1 260 ? 6.81800   6.79700   -10.83300 1.000 17.75644 ?  240 GLY A CA  1 
ATOM   1753 C  C   . GLY A 1 260 ? 6.17100   7.20700   -9.52900  1.000 15.17991 ?  240 GLY A C   1 
ATOM   1754 O  O   . GLY A 1 260 ? 6.63800   8.12600   -8.85000  1.000 15.67050 ?  240 GLY A O   1 
ATOM   1755 N  N   . ASN A 1 261 ? 5.09900   6.50600   -9.14700  1.000 18.46739 ?  241 ASN A N   1 
ATOM   1756 C  CA  . ASN A 1 261 ? 4.41900   6.83000   -7.90000  1.000 15.18325 ?  241 ASN A CA  1 
ATOM   1757 C  C   . ASN A 1 261 ? 5.34200   6.66000   -6.70300  1.000 14.53614 ?  241 ASN A C   1 
ATOM   1758 O  O   . ASN A 1 261 ? 5.23600   7.41100   -5.72700  1.000 17.21620 ?  241 ASN A O   1 
ATOM   1759 C  CB  . ASN A 1 261 ? 3.17400   5.96200   -7.72600  1.000 15.09268 ?  241 ASN A CB  1 
ATOM   1760 C  CG  . ASN A 1 261 ? 2.17200   6.13300   -8.86100  1.000 18.48971 ?  241 ASN A CG  1 
ATOM   1761 O  OD1 . ASN A 1 261 ? 2.36000   6.95500   -9.76100  1.000 19.09993 ?  241 ASN A OD1 1 
ATOM   1762 N  ND2 . ASN A 1 261 ? 1.10200   5.34800   -8.82200  1.000 17.61033 ?  241 ASN A ND2 1 
ATOM   1763 N  N   . GLY A 1 262 ? 6.26000   5.69300   -6.76200  1.000 17.96165 ?  242 GLY A N   1 
ATOM   1764 C  CA  . GLY A 1 262 ? 7.18500   5.49900   -5.65900  1.000 14.49534 ?  242 GLY A CA  1 
ATOM   1765 C  C   . GLY A 1 262 ? 8.14100   6.66300   -5.48100  1.000 19.72408 ?  242 GLY A C   1 
ATOM   1766 O  O   . GLY A 1 262 ? 8.38400   7.11200   -4.35700  1.000 21.78834 ?  242 GLY A O   1 
ATOM   1767 N  N   . VAL A 1 263 ? 8.69600   7.17000   -6.58500  1.000 19.13651 ?  243 VAL A N   1 
ATOM   1768 C  CA  . VAL A 1 263 ? 9.61100   8.30700   -6.49500  1.000 18.65457 ?  243 VAL A CA  1 
ATOM   1769 C  C   . VAL A 1 263 ? 8.88300   9.53100   -5.95700  1.000 14.57524 ?  243 VAL A C   1 
ATOM   1770 O  O   . VAL A 1 263 ? 9.38600   10.23600  -5.07500  1.000 18.84422 ?  243 VAL A O   1 
ATOM   1771 C  CB  . VAL A 1 263 ? 10.25900  8.59800   -7.86000  1.000 21.41578 ?  243 VAL A CB  1 
ATOM   1772 C  CG1 . VAL A 1 263 ? 11.16800  9.82300   -7.75400  1.000 17.18706 ?  243 VAL A CG1 1 
ATOM   1773 C  CG2 . VAL A 1 263 ? 11.05800  7.39300   -8.33700  1.000 20.22003 ?  243 VAL A CG2 1 
ATOM   1774 N  N   . ARG A 1 264 ? 7.68400   9.80300   -6.48200  1.000 17.75543 ?  244 ARG A N   1 
ATOM   1775 C  CA  . ARG A 1 264 ? 6.91200   10.94000  -5.98800  1.000 19.81851 ?  244 ARG A CA  1 
ATOM   1776 C  C   . ARG A 1 264 ? 6.63400   10.80700  -4.49400  1.000 18.90002 ?  244 ARG A C   1 
ATOM   1777 O  O   . ARG A 1 264 ? 6.74900   11.78400  -3.74500  1.000 17.31198 ?  244 ARG A O   1 
ATOM   1778 C  CB  . ARG A 1 264 ? 5.59500   11.05700  -6.75500  1.000 19.48915 ?  244 ARG A CB  1 
ATOM   1779 C  CG  . ARG A 1 264 ? 4.86400   12.37900  -6.54900  1.000 17.32343 ?  244 ARG A CG  1 
ATOM   1780 C  CD  . ARG A 1 264 ? 3.36200   12.18300  -6.72800  1.000 19.96925 ?  244 ARG A CD  1 
ATOM   1781 N  NE  . ARG A 1 264 ? 2.82000   11.50100  -5.56000  1.000 23.17236 ?  244 ARG A NE  1 
ATOM   1782 C  CZ  . ARG A 1 264 ? 2.69900   12.04700  -4.35500  1.000 21.26559 ?  244 ARG A CZ  1 
ATOM   1783 N  NH1 . ARG A 1 264 ? 2.82700   13.35100  -4.16600  1.000 23.05630 ?  244 ARG A NH1 1 
ATOM   1784 N  NH2 . ARG A 1 264 ? 2.42900   11.26400  -3.31400  1.000 19.98965 ?  244 ARG A NH2 1 
ATOM   1785 N  N   . ALA A 1 265 ? 6.25600   9.60300   -4.04200  1.000 21.15387 ?  245 ALA A N   1 
ATOM   1786 C  CA  . ALA A 1 265 ? 5.99500   9.38700   -2.62100  1.000 18.11767 ?  245 ALA A CA  1 
ATOM   1787 C  C   . ALA A 1 265 ? 7.23700   9.63400   -1.78100  1.000 14.94214 ?  245 ALA A C   1 
ATOM   1788 O  O   . ALA A 1 265 ? 7.13700   10.13100  -0.65500  1.000 20.13716 ?  245 ALA A O   1 
ATOM   1789 C  CB  . ALA A 1 265 ? 5.48500   7.96400   -2.38700  1.000 16.55874 ?  245 ALA A CB  1 
ATOM   1790 N  N   . LEU A 1 266 ? 8.41200   9.28100   -2.30900  1.000 15.10650 ?  246 LEU A N   1 
ATOM   1791 C  CA  . LEU A 1 266 ? 9.66400   9.54300   -1.61000  1.000 18.99493 ?  246 LEU A CA  1 
ATOM   1792 C  C   . LEU A 1 266 ? 9.92900   11.03700  -1.52500  1.000 18.61616 ?  246 LEU A C   1 
ATOM   1793 O  O   . LEU A 1 266 ? 10.33700  11.54700  -0.47400  1.000 22.52113 ?  246 LEU A O   1 
ATOM   1794 C  CB  . LEU A 1 266 ? 10.80500  8.83700   -2.34200  1.000 16.76871 ?  246 LEU A CB  1 
ATOM   1795 C  CG  . LEU A 1 266 ? 10.90200  7.33200   -2.09300  1.000 13.94434 ?  246 LEU A CG  1 
ATOM   1796 C  CD1 . LEU A 1 266 ? 12.05200  6.74000   -2.89400  1.000 15.78429 ?  246 LEU A CD1 1 
ATOM   1797 C  CD2 . LEU A 1 266 ? 11.07500  7.04100   -0.61100  1.000 14.45639 ?  246 LEU A CD2 1 
ATOM   1798 N  N   . LEU A 1 267 ? 9.70000   11.74700  -2.63100  1.000 19.18411 ?  247 LEU A N   1 
ATOM   1799 C  CA  . LEU A 1 267 ? 9.90400   13.18900  -2.67000  1.000 21.80256 ?  247 LEU A CA  1 
ATOM   1800 C  C   . LEU A 1 267 ? 8.90500   13.92200  -1.78300  1.000 25.02349 ?  247 LEU A C   1 
ATOM   1801 O  O   . LEU A 1 267 ? 9.22100   14.99100  -1.24800  1.000 21.61590 ?  247 LEU A O   1 
ATOM   1802 C  CB  . LEU A 1 267 ? 9.78800   13.67900  -4.11100  1.000 18.57763 ?  247 LEU A CB  1 
ATOM   1803 C  CG  . LEU A 1 267 ? 10.91700  13.26900  -5.05900  1.000 21.31859 ?  247 LEU A CG  1 
ATOM   1804 C  CD1 . LEU A 1 267 ? 10.59900  13.71400  -6.47000  1.000 21.38994 ?  247 LEU A CD1 1 
ATOM   1805 C  CD2 . LEU A 1 267 ? 12.25900  13.82500  -4.59700  1.000 28.02491 ?  247 LEU A CD2 1 
ATOM   1806 N  N   . ALA A 1 268 ? 7.70200   13.36600  -1.61900  1.000 23.27231 ?  248 ALA A N   1 
ATOM   1807 C  CA  . ALA A 1 268 ? 6.68300   13.97200  -0.77300  1.000 23.23352 ?  248 ALA A CA  1 
ATOM   1808 C  C   . ALA A 1 268 ? 6.92400   13.73500  0.71300   1.000 27.21295 ?  248 ALA A C   1 
ATOM   1809 O  O   . ALA A 1 268 ? 6.32500   14.43100  1.54000   1.000 30.16507 ?  248 ALA A O   1 
ATOM   1810 C  CB  . ALA A 1 268 ? 5.30200   13.44000  -1.15800  1.000 22.17090 ?  248 ALA A CB  1 
ATOM   1811 N  N   . ALA A 1 269 ? 7.77700   12.77500  1.07000   1.000 24.89918 ?  249 ALA A N   1 
ATOM   1812 C  CA  . ALA A 1 269 ? 8.10100   12.46700  2.46300   1.000 26.49481 ?  249 ALA A CA  1 
ATOM   1813 C  C   . ALA A 1 269 ? 9.61500   12.49200  2.62000   1.000 22.62469 ?  249 ALA A C   1 
ATOM   1814 O  O   . ALA A 1 269 ? 10.26000  11.43600  2.69300   1.000 28.10722 ?  249 ALA A O   1 
ATOM   1815 C  CB  . ALA A 1 269 ? 7.52700   11.11500  2.88200   1.000 24.63179 ?  249 ALA A CB  1 
ATOM   1816 N  N   . PRO A 1 270 ? 10.21500  13.68600  2.68600   1.000 27.99245 ?  250 PRO A N   1 
ATOM   1817 C  CA  . PRO A 1 270 ? 11.68800  13.77300  2.70500   1.000 25.71543 ?  250 PRO A CA  1 
ATOM   1818 C  C   . PRO A 1 270 ? 12.34700  12.96200  3.81000   1.000 24.62343 ?  250 PRO A C   1 
ATOM   1819 O  O   . PRO A 1 270 ? 13.41700  12.38100  3.58800   1.000 27.45980 ?  250 PRO A O   1 
ATOM   1820 C  CB  . PRO A 1 270 ? 11.92700  15.27900  2.88700   1.000 31.09699 ?  250 PRO A CB  1 
ATOM   1821 C  CG  . PRO A 1 270 ? 10.72900  15.90200  2.24700   1.000 33.73838 ?  250 PRO A CG  1 
ATOM   1822 C  CD  . PRO A 1 270 ? 9.59800   15.02200  2.70700   1.000 28.98124 ?  250 PRO A CD  1 
ATOM   1823 N  N   . ASP A 1 271 ? 11.73400  12.90100  4.99600   1.000 22.62830 ?  251 ASP A N   1 
ATOM   1824 C  CA  . ASP A 1 271 ? 12.33500  12.16200  6.10200   1.000 25.27334 ?  251 ASP A CA  1 
ATOM   1825 C  C   . ASP A 1 271 ? 12.44500  10.67300  5.78900   1.000 26.50214 ?  251 ASP A C   1 
ATOM   1826 O  O   . ASP A 1 271 ? 13.43700  10.03000  6.15100   1.000 23.93990 ?  251 ASP A O   1 
ATOM   1827 C  CB  . ASP A 1 271 ? 11.53100  12.38600  7.38300   1.000 32.94046 ?  251 ASP A CB  1 
ATOM   1828 C  CG  . ASP A 1 271 ? 11.70400  13.78700  7.94400   1.000 42.26286 ?  251 ASP A CG  1 
ATOM   1829 O  OD1 . ASP A 1 271 ? 12.30100  14.64300  7.25700   1.000 37.31269 ?  251 ASP A OD1 1 
ATOM   1830 O  OD2 . ASP A 1 271 ? 11.23700  14.03400  9.07600   1.000 46.23502 -1 251 ASP A OD2 1 
ATOM   1831 N  N   . GLN A 1 272 ? 11.43400  10.10000  5.12800   1.000 22.99674 ?  252 GLN A N   1 
ATOM   1832 C  CA  . GLN A 1 272 ? 11.54900  8.70800   4.69800   1.000 20.47655 ?  252 GLN A CA  1 
ATOM   1833 C  C   . GLN A 1 272 ? 12.67400  8.54900   3.68600   1.000 22.49863 ?  252 GLN A C   1 
ATOM   1834 O  O   . GLN A 1 272 ? 13.45300  7.59000   3.75500   1.000 21.87182 ?  252 GLN A O   1 
ATOM   1835 C  CB  . GLN A 1 272 ? 10.22600  8.20900   4.11100   1.000 20.11108 ?  252 GLN A CB  1 
ATOM   1836 C  CG  . GLN A 1 272 ? 9.04500   8.29500   5.06600   1.000 18.57098 ?  252 GLN A CG  1 
ATOM   1837 C  CD  . GLN A 1 272 ? 9.25700   7.50200   6.34000   1.000 18.67125 ?  252 GLN A CD  1 
ATOM   1838 O  OE1 . GLN A 1 272 ? 9.53400   6.30100   6.30600   1.000 18.23603 ?  252 GLN A OE1 1 
ATOM   1839 N  NE2 . GLN A 1 272 ? 9.11300   8.17000   7.47800   1.000 24.84485 ?  252 GLN A NE2 1 
ATOM   1840 N  N   . LEU A 1 273 ? 12.77900  9.48500   2.74200   1.000 21.67383 ?  253 LEU A N   1 
ATOM   1841 C  CA  . LEU A 1 273 ? 13.86100  9.43500   1.76600   1.000 26.68296 ?  253 LEU A CA  1 
ATOM   1842 C  C   . LEU A 1 273 ? 15.22400  9.51500   2.44400   1.000 25.18146 ?  253 LEU A C   1 
ATOM   1843 O  O   . LEU A 1 273 ? 16.15000  8.77700   2.08500   1.000 25.03861 ?  253 LEU A O   1 
ATOM   1844 C  CB  . LEU A 1 273 ? 13.70000  10.56500  0.74800   1.000 22.94473 ?  253 LEU A CB  1 
ATOM   1845 C  CG  . LEU A 1 273 ? 14.67600  10.55800  -0.43400  1.000 25.99144 ?  253 LEU A CG  1 
ATOM   1846 C  CD1 . LEU A 1 273 ? 14.85600  9.15400   -0.99400  1.000 21.18029 ?  253 LEU A CD1 1 
ATOM   1847 C  CD2 . LEU A 1 273 ? 14.20200  11.51500  -1.51600  1.000 29.47623 ?  253 LEU A CD2 1 
ATOM   1848 N  N   . ALA A 1 274 ? 15.36300  10.40200  3.43300   1.000 28.69477 ?  254 ALA A N   1 
ATOM   1849 C  CA  . ALA A 1 274 ? 16.63800  10.54200  4.12900   1.000 27.20467 ?  254 ALA A CA  1 
ATOM   1850 C  C   . ALA A 1 274 ? 17.00300  9.26700   4.88000   1.000 27.87485 ?  254 ALA A C   1 
ATOM   1851 O  O   . ALA A 1 274 ? 18.17400  8.86900   4.91000   1.000 26.77941 ?  254 ALA A O   1 
ATOM   1852 C  CB  . ALA A 1 274 ? 16.58400  11.73400  5.08500   1.000 31.41868 ?  254 ALA A CB  1 
ATOM   1853 N  N   . ASP A 1 275 ? 16.01500  8.61100   5.49200   1.000 24.49804 ?  255 ASP A N   1 
ATOM   1854 C  CA  . ASP A 1 275 ? 16.27500  7.33300   6.15100   1.000 30.11003 ?  255 ASP A CA  1 
ATOM   1855 C  C   . ASP A 1 275 ? 16.72600  6.27900   5.14600   1.000 27.08024 ?  255 ASP A C   1 
ATOM   1856 O  O   . ASP A 1 275 ? 17.69000  5.54400   5.39100   1.000 26.79013 ?  255 ASP A O   1 
ATOM   1857 C  CB  . ASP A 1 275 ? 15.02500  6.86900   6.90400   1.000 23.67857 ?  255 ASP A CB  1 
ATOM   1858 C  CG  . ASP A 1 275 ? 15.28900  5.66000   7.78400   1.000 36.30046 ?  255 ASP A CG  1 
ATOM   1859 O  OD1 . ASP A 1 275 ? 16.47300  5.32000   7.99700   1.000 31.54568 -1 255 ASP A OD1 1 
ATOM   1860 O  OD2 . ASP A 1 275 ? 14.30800  5.04300   8.25600   1.000 36.48721 -1 255 ASP A OD2 1 
ATOM   1861 N  N   . LEU A 1 276 ? 16.03700  6.19000   4.00400   1.000 20.85260 ?  256 LEU A N   1 
ATOM   1862 C  CA  . LEU A 1 276 ? 16.42300  5.22200   2.98000   1.000 24.55882 ?  256 LEU A CA  1 
ATOM   1863 C  C   . LEU A 1 276 ? 17.81500  5.52000   2.43500   1.000 26.18847 ?  256 LEU A C   1 
ATOM   1864 O  O   . LEU A 1 276 ? 18.59700  4.60100   2.16300   1.000 25.00120 ?  256 LEU A O   1 
ATOM   1865 C  CB  . LEU A 1 276 ? 15.39600  5.22300   1.84800   1.000 20.92562 ?  256 LEU A CB  1 
ATOM   1866 C  CG  . LEU A 1 276 ? 15.67900  4.29500   0.66500   1.000 23.60558 ?  256 LEU A CG  1 
ATOM   1867 C  CD1 . LEU A 1 276 ? 15.99500  2.87500   1.12600   1.000 20.55147 ?  256 LEU A CD1 1 
ATOM   1868 C  CD2 . LEU A 1 276 ? 14.51100  4.30700   -0.31400  1.000 17.59894 ?  256 LEU A CD2 1 
ATOM   1869 N  N   . ARG A 1 277 ? 18.14100  6.80300   2.26600   1.000 20.59170 ?  257 ARG A N   1 
ATOM   1870 C  CA  . ARG A 1 277 ? 19.46700  7.16800   1.78300   1.000 26.91193 ?  257 ARG A CA  1 
ATOM   1871 C  C   . ARG A 1 277 ? 20.55300  6.82500   2.79600   1.000 27.42966 ?  257 ARG A C   1 
ATOM   1872 O  O   . ARG A 1 277 ? 21.70800  6.60800   2.41400   1.000 32.63549 ?  257 ARG A O   1 
ATOM   1873 C  CB  . ARG A 1 277 ? 19.50100  8.65600   1.44300   1.000 26.82894 ?  257 ARG A CB  1 
ATOM   1874 C  CG  . ARG A 1 277 ? 18.95900  8.95900   0.06200   1.000 30.57031 ?  257 ARG A CG  1 
ATOM   1875 C  CD  . ARG A 1 277 ? 18.93400  10.44800  -0.22800  1.000 35.70501 ?  257 ARG A CD  1 
ATOM   1876 N  NE  . ARG A 1 277 ? 18.57900  10.70300  -1.61900  1.000 33.67934 ?  257 ARG A NE  1 
ATOM   1877 C  CZ  . ARG A 1 277 ? 17.95200  11.78500  -2.05300  1.000 38.86877 ?  257 ARG A CZ  1 
ATOM   1878 N  NH1 . ARG A 1 277 ? 17.56400  12.73900  -1.22100  1.000 47.58058 ?  257 ARG A NH1 1 
ATOM   1879 N  NH2 . ARG A 1 277 ? 17.71300  11.91700  -3.35500  1.000 35.27702 ?  257 ARG A NH2 1 
ATOM   1880 N  N   . SER A 1 278 ? 20.20500  6.76200   4.07800   1.000 29.35298 ?  258 SER A N   1 
ATOM   1881 C  CA  . SER A 1 278 ? 21.16500  6.47300   5.13500   1.000 31.84756 ?  258 SER A CA  1 
ATOM   1882 C  C   . SER A 1 278 ? 21.28500  4.98800   5.44800   1.000 33.20160 ?  258 SER A C   1 
ATOM   1883 O  O   . SER A 1 278 ? 22.20300  4.59700   6.17600   1.000 34.58576 ?  258 SER A O   1 
ATOM   1884 C  CB  . SER A 1 278 ? 20.77700  7.22700   6.41000   1.000 35.14093 ?  258 SER A CB  1 
ATOM   1885 O  OG  . SER A 1 278 ? 19.69800  6.58300   7.07100   1.000 37.78246 ?  258 SER A OG  1 
ATOM   1886 N  N   . ASP A 1 279 ? 20.38500  4.15700   4.92400   1.000 35.35452 ?  259 ASP A N   1 
ATOM   1887 C  CA  . ASP A 1 279 ? 20.32300  2.73100   5.25500   1.000 34.41606 ?  259 ASP A CA  1 
ATOM   1888 C  C   . ASP A 1 279 ? 20.00400  1.97200   3.96800   1.000 33.12311 ?  259 ASP A C   1 
ATOM   1889 O  O   . ASP A 1 279 ? 18.83500  1.76200   3.63000   1.000 27.64386 ?  259 ASP A O   1 
ATOM   1890 C  CB  . ASP A 1 279 ? 19.29000  2.47800   6.35300   1.000 27.82349 ?  259 ASP A CB  1 
ATOM   1891 C  CG  . ASP A 1 279 ? 19.40400  1.09200   6.97000   1.000 31.82658 ?  259 ASP A CG  1 
ATOM   1892 O  OD1 . ASP A 1 279 ? 20.32700  0.34100   6.59900   1.000 29.70129 -1 259 ASP A OD1 1 
ATOM   1893 O  OD2 . ASP A 1 279 ? 18.58100  0.76700   7.85800   1.000 35.20587 -1 259 ASP A OD2 1 
ATOM   1894 N  N   . GLU A 1 280 ? 21.05700  1.56800   3.25400   1.000 25.61538 ?  260 GLU A N   1 
ATOM   1895 C  CA  . GLU A 1 280 ? 20.87300  0.82800   2.01000   1.000 27.71315 ?  260 GLU A CA  1 
ATOM   1896 C  C   . GLU A 1 280 ? 20.11500  -0.47200  2.23600   1.000 24.71527 ?  260 GLU A C   1 
ATOM   1897 O  O   . GLU A 1 280 ? 19.37400  -0.92300  1.35200   1.000 26.57320 ?  260 GLU A O   1 
ATOM   1898 C  CB  . GLU A 1 280 ? 22.23000  0.54600   1.36400   1.000 24.77407 ?  260 GLU A CB  1 
ATOM   1899 N  N   . ALA A 1 281 ? 20.27600  -1.08200  3.41300   1.000 21.47879 ?  261 ALA A N   1 
ATOM   1900 C  CA  . ALA A 1 281 ? 19.59700  -2.33200  3.72500   1.000 22.98620 ?  261 ALA A CA  1 
ATOM   1901 C  C   . ALA A 1 281 ? 18.09100  -2.16600  3.86200   1.000 16.74866 ?  261 ALA A C   1 
ATOM   1902 O  O   . ALA A 1 281 ? 17.37800  -3.17500  3.86900   1.000 22.77693 ?  261 ALA A O   1 
ATOM   1903 C  CB  . ALA A 1 281 ? 20.16600  -2.93100  5.01200   1.000 21.30382 ?  261 ALA A CB  1 
ATOM   1904 N  N   . LEU A 1 282 ? 17.60100  -0.93200  3.98900   1.000 16.94232 ?  262 LEU A N   1 
ATOM   1905 C  CA  . LEU A 1 282 ? 16.17100  -0.66100  4.09900   1.000 19.45165 ?  262 LEU A CA  1 
ATOM   1906 C  C   . LEU A 1 282 ? 15.42600  -0.83900  2.77600   1.000 19.85320 ?  262 LEU A C   1 
ATOM   1907 O  O   . LEU A 1 282 ? 14.19000  -0.92300  2.78600   1.000 15.52824 ?  262 LEU A O   1 
ATOM   1908 C  CB  . LEU A 1 282 ? 15.95900  0.76600   4.62500   1.000 20.56176 ?  262 LEU A CB  1 
ATOM   1909 C  CG  . LEU A 1 282 ? 14.52500  1.22500   4.90600   1.000 21.77694 ?  262 LEU A CG  1 
ATOM   1910 C  CD1 . LEU A 1 282 ? 13.83600  0.24500   5.85100   1.000 21.07611 ?  262 LEU A CD1 1 
ATOM   1911 C  CD2 . LEU A 1 282 ? 14.47800  2.65200   5.43900   1.000 26.46950 ?  262 LEU A CD2 1 
ATOM   1912 N  N   . LEU A 1 283 ? 16.13600  -0.90700  1.64900   1.000 18.82174 ?  263 LEU A N   1 
ATOM   1913 C  CA  . LEU A 1 283 ? 15.48500  -0.90700  0.33700   1.000 16.88278 ?  263 LEU A CA  1 
ATOM   1914 C  C   . LEU A 1 283 ? 14.42300  -1.98500  0.15300   1.000 19.97170 ?  263 LEU A C   1 
ATOM   1915 O  O   . LEU A 1 283 ? 13.33500  -1.65600  -0.34900  1.000 19.38107 ?  263 LEU A O   1 
ATOM   1916 C  CB  . LEU A 1 283 ? 16.54800  -1.01300  -0.76500  1.000 21.05078 ?  263 LEU A CB  1 
ATOM   1917 C  CG  . LEU A 1 283 ? 16.00300  -0.83100  -2.18400  1.000 27.00232 ?  263 LEU A CG  1 
ATOM   1918 C  CD1 . LEU A 1 283 ? 15.32700  0.53000   -2.36100  1.000 18.08076 ?  263 LEU A CD1 1 
ATOM   1919 C  CD2 . LEU A 1 283 ? 17.11100  -1.02500  -3.20300  1.000 27.96026 ?  263 LEU A CD2 1 
ATOM   1920 N  N   . PRO A 1 284 ? 14.65800  -3.26200  0.49000   1.000 21.92503 ?  264 PRO A N   1 
ATOM   1921 C  CA  . PRO A 1 284 ? 13.60900  -4.26800  0.22900   1.000 24.28867 ?  264 PRO A CA  1 
ATOM   1922 C  C   . PRO A 1 284 ? 12.30900  -3.96700  0.95000   1.000 19.14086 ?  264 PRO A C   1 
ATOM   1923 O  O   . PRO A 1 284 ? 11.23400  -4.00400  0.33400   1.000 16.56097 ?  264 PRO A O   1 
ATOM   1924 C  CB  . PRO A 1 284 ? 14.25400  -5.56700  0.72400   1.000 20.35638 ?  264 PRO A CB  1 
ATOM   1925 C  CG  . PRO A 1 284 ? 15.71000  -5.33300  0.53400   1.000 27.41596 ?  264 PRO A CG  1 
ATOM   1926 C  CD  . PRO A 1 284 ? 15.90400  -3.90500  0.95400   1.000 25.63376 ?  264 PRO A CD  1 
ATOM   1927 N  N   . ARG A 1 285 ? 12.38100  -3.64900  2.24500   1.000 20.47797 ?  265 ARG A N   1 
ATOM   1928 C  CA  . ARG A 1 285 ? 11.17000  -3.29500  2.97700   1.000 22.81435 ?  265 ARG A CA  1 
ATOM   1929 C  C   . ARG A 1 285 ? 10.60700  -1.95400  2.51700   1.000 19.56569 ?  265 ARG A C   1 
ATOM   1930 O  O   . ARG A 1 285 ? 9.38800   -1.75000  2.55300   1.000 19.10604 ?  265 ARG A O   1 
ATOM   1931 C  CB  . ARG A 1 285 ? 11.44700  -3.28200  4.48500   1.000 23.20785 ?  265 ARG A CB  1 
ATOM   1932 C  CG  . ARG A 1 285 ? 10.22600  -2.88900  5.31400   1.000 33.46328 ?  265 ARG A CG  1 
ATOM   1933 C  CD  . ARG A 1 285 ? 10.31000  -3.29900  6.78200   1.000 34.77035 ?  265 ARG A CD  1 
ATOM   1934 N  NE  . ARG A 1 285 ? 10.61000  -4.71500  6.96200   1.000 45.30886 ?  265 ARG A NE  1 
ATOM   1935 C  CZ  . ARG A 1 285 ? 11.25900  -5.21700  8.00500   1.000 40.84670 ?  265 ARG A CZ  1 
ATOM   1936 N  NH1 . ARG A 1 285 ? 11.68200  -4.44500  8.99300   1.000 34.47063 ?  265 ARG A NH1 1 
ATOM   1937 N  NH2 . ARG A 1 285 ? 11.47100  -6.52800  8.06600   1.000 32.00679 ?  265 ARG A NH2 1 
ATOM   1938 N  N   . ALA A 1 286 ? 11.47100  -1.03500  2.08000   1.000 17.77544 ?  266 ALA A N   1 
ATOM   1939 C  CA  . ALA A 1 286 ? 10.99300  0.25100   1.57900   1.000 16.44148 ?  266 ALA A CA  1 
ATOM   1940 C  C   . ALA A 1 286 ? 10.14900  0.07700   0.32100   1.000 19.29525 ?  266 ALA A C   1 
ATOM   1941 O  O   . ALA A 1 286 ? 9.12100   0.74500   0.15600   1.000 13.98148 ?  266 ALA A O   1 
ATOM   1942 C  CB  . ALA A 1 286 ? 12.17700  1.18400   1.31000   1.000 16.03615 ?  266 ALA A CB  1 
ATOM   1943 N  N   . ILE A 1 287 ? 10.56100  -0.82100  -0.57700  1.000 17.98488 ?  267 ILE A N   1 
ATOM   1944 C  CA  . ILE A 1 287 ? 9.79400   -1.03900  -1.80200  1.000 19.01500 ?  267 ILE A CA  1 
ATOM   1945 C  C   . ILE A 1 287 ? 8.42300   -1.61700  -1.47900  1.000 15.60898 ?  267 ILE A C   1 
ATOM   1946 O  O   . ILE A 1 287 ? 7.42200   -1.28200  -2.12500  1.000 16.25445 ?  267 ILE A O   1 
ATOM   1947 C  CB  . ILE A 1 287 ? 10.57400  -1.94200  -2.77300  1.000 18.27658 ?  267 ILE A CB  1 
ATOM   1948 C  CG1 . ILE A 1 287 ? 11.82400  -1.22200  -3.28300  1.000 15.80140 ?  267 ILE A CG1 1 
ATOM   1949 C  CG2 . ILE A 1 287 ? 9.70400   -2.36500  -3.93600  1.000 12.57089 ?  267 ILE A CG2 1 
ATOM   1950 C  CD1 . ILE A 1 287 ? 12.88800  -2.16500  -3.76300  1.000 20.92883 ?  267 ILE A CD1 1 
ATOM   1951 N  N   . GLU A 1 288 ? 8.34800   -2.48700  -0.47300  1.000 15.57053 ?  268 GLU A N   1 
ATOM   1952 C  CA  . GLU A 1 288 ? 7.05000   -3.05500  -0.11800  1.000 19.04412 ?  268 GLU A CA  1 
ATOM   1953 C  C   . GLU A 1 288 ? 6.11000   -1.98400  0.42500   1.000 16.80115 ?  268 GLU A C   1 
ATOM   1954 O  O   . GLU A 1 288 ? 4.90800   -1.99900  0.12500   1.000 15.74329 ?  268 GLU A O   1 
ATOM   1955 C  CB  . GLU A 1 288 ? 7.22300   -4.19600  0.88600   1.000 20.86750 ?  268 GLU A CB  1 
ATOM   1956 C  CG  . GLU A 1 288 ? 7.89700   -5.43700  0.31100   1.000 21.40122 ?  268 GLU A CG  1 
ATOM   1957 C  CD  . GLU A 1 288 ? 7.25600   -5.90700  -0.98600  1.000 29.11807 ?  268 GLU A CD  1 
ATOM   1958 O  OE1 . GLU A 1 288 ? 6.13100   -6.45300  -0.94100  1.000 20.09727 ?  268 GLU A OE1 1 
ATOM   1959 O  OE2 . GLU A 1 288 ? 7.88300   -5.74200  -2.05800  1.000 29.97543 -1 268 GLU A OE2 1 
ATOM   1960 N  N   . GLU A 1 289 ? 6.63500   -1.04000  1.21900   1.000 13.85644 ?  269 GLU A N   1 
ATOM   1961 C  CA  . GLU A 1 289 ? 5.81000   0.06900   1.69200   1.000 17.19471 ?  269 GLU A CA  1 
ATOM   1962 C  C   . GLU A 1 289 ? 5.44600   1.01200   0.55500   1.000 16.11457 ?  269 GLU A C   1 
ATOM   1963 O  O   . GLU A 1 289 ? 4.30900   1.49200   0.48200   1.000 13.83904 ?  269 GLU A O   1 
ATOM   1964 C  CB  . GLU A 1 289 ? 6.51800   0.84000   2.80800   1.000 13.56195 ?  269 GLU A CB  1 
ATOM   1965 C  CG  . GLU A 1 289 ? 5.84000   2.15900   3.18600   1.000 19.16284 ?  269 GLU A CG  1 
ATOM   1966 C  CD  . GLU A 1 289 ? 4.53100   1.99400   3.95000   1.000 17.04961 ?  269 GLU A CD  1 
ATOM   1967 O  OE1 . GLU A 1 289 ? 3.98400   0.87600   3.97500   1.000 19.63158 ?  269 GLU A OE1 1 
ATOM   1968 O  OE2 . GLU A 1 289 ? 4.03600   3.00200   4.51200   1.000 18.77913 -1 269 GLU A OE2 1 
ATOM   1969 N  N   . LEU A 1 290 ? 6.40100   1.29800   -0.33500  1.000 15.28963 ?  270 LEU A N   1 
ATOM   1970 C  CA  . LEU A 1 290 ? 6.10600   2.11000   -1.51300  1.000 12.78335 ?  270 LEU A CA  1 
ATOM   1971 C  C   . LEU A 1 290 ? 5.03200   1.45200   -2.36600  1.000 14.24182 ?  270 LEU A C   1 
ATOM   1972 O  O   . LEU A 1 290 ? 4.15600   2.13300   -2.91300  1.000 18.68208 ?  270 LEU A O   1 
ATOM   1973 C  CB  . LEU A 1 290 ? 7.38400   2.32600   -2.32500  1.000 14.16487 ?  270 LEU A CB  1 
ATOM   1974 C  CG  . LEU A 1 290 ? 8.41000   3.28100   -1.71600  1.000 13.82251 ?  270 LEU A CG  1 
ATOM   1975 C  CD1 . LEU A 1 290 ? 9.71100   3.27800   -2.53200  1.000 12.58811 ?  270 LEU A CD1 1 
ATOM   1976 C  CD2 . LEU A 1 290 ? 7.85600   4.68800   -1.59100  1.000 16.53773 ?  270 LEU A CD2 1 
ATOM   1977 N  N   . THR A 1 291 ? 5.07600   0.12300   -2.47700  1.000 15.40015 ?  271 THR A N   1 
ATOM   1978 C  CA  . THR A 1 291 ? 4.01400   -0.59400  -3.17700  1.000 10.90072 ?  271 THR A CA  1 
ATOM   1979 C  C   . THR A 1 291 ? 2.67900   -0.43700  -2.45700  1.000 14.78414 ?  271 THR A C   1 
ATOM   1980 O  O   . THR A 1 291 ? 1.67800   -0.05400  -3.06600  1.000 12.82433 ?  271 THR A O   1 
ATOM   1981 C  CB  . THR A 1 291 ? 4.39400   -2.06900  -3.32400  1.000 15.45668 ?  271 THR A CB  1 
ATOM   1982 O  OG1 . THR A 1 291 ? 5.73400   -2.16300  -3.82900  1.000 14.00052 ?  271 THR A OG1 1 
ATOM   1983 C  CG2 . THR A 1 291 ? 3.44600   -2.77400  -4.28600  1.000 12.54813 ?  271 THR A CG2 1 
ATOM   1984 N  N   . ARG A 1 292 ? 2.65000   -0.69300  -1.14700  1.000 13.33600 ?  272 ARG A N   1 
ATOM   1985 C  CA  . ARG A 1 292 ? 1.39900   -0.54200  -0.40700  1.000 13.10341 ?  272 ARG A CA  1 
ATOM   1986 C  C   . ARG A 1 292 ? 0.86200   0.87800   -0.51900  1.000 17.51677 ?  272 ARG A C   1 
ATOM   1987 O  O   . ARG A 1 292 ? -0.34300  1.08200   -0.69900  1.000 15.17066 ?  272 ARG A O   1 
ATOM   1988 C  CB  . ARG A 1 292 ? 1.60000   -0.92600  1.06200   1.000 11.86391 ?  272 ARG A CB  1 
ATOM   1989 C  CG  . ARG A 1 292 ? 0.34100   -0.75600  1.92800   1.000 15.57695 ?  272 ARG A CG  1 
ATOM   1990 C  CD  . ARG A 1 292 ? 0.67700   -0.42400  3.38600   1.000 16.23404 ?  272 ARG A CD  1 
ATOM   1991 N  NE  . ARG A 1 292 ? 1.23400   0.91200   3.55500   1.000 14.01877 ?  272 ARG A NE  1 
ATOM   1992 C  CZ  . ARG A 1 292 ? 0.51300   2.01800   3.67700   1.000 16.80514 ?  272 ARG A CZ  1 
ATOM   1993 N  NH1 . ARG A 1 292 ? -0.81300  1.99000   3.64200   1.000 14.75085 ?  272 ARG A NH1 1 
ATOM   1994 N  NH2 . ARG A 1 292 ? 1.13700   3.18100   3.84000   1.000 16.91913 ?  272 ARG A NH2 1 
ATOM   1995 N  N   . PHE A 1 293 ? 1.75600   1.87000   -0.47200  1.000 11.45424 ?  273 PHE A N   1 
ATOM   1996 C  CA  . PHE A 1 293 ? 1.33700   3.26600   -0.38200  1.000 17.67818 ?  273 PHE A CA  1 
ATOM   1997 C  C   . PHE A 1 293 ? 0.66400   3.76000   -1.66000  1.000 16.88978 ?  273 PHE A C   1 
ATOM   1998 O  O   . PHE A 1 293 ? -0.38600  4.41200   -1.60300  1.000 16.20136 ?  273 PHE A O   1 
ATOM   1999 C  CB  . PHE A 1 293 ? 2.53800   4.14000   -0.03400  1.000 15.08382 ?  273 PHE A CB  1 
ATOM   2000 C  CG  . PHE A 1 293 ? 2.19000   5.57700   0.21100   1.000 14.63721 ?  273 PHE A CG  1 
ATOM   2001 C  CD1 . PHE A 1 293 ? 1.52300   5.95800   1.36500   1.000 19.41164 ?  273 PHE A CD1 1 
ATOM   2002 C  CD2 . PHE A 1 293 ? 2.54200   6.55100   -0.70900  1.000 19.65633 ?  273 PHE A CD2 1 
ATOM   2003 C  CE1 . PHE A 1 293 ? 1.20500   7.28800   1.59100   1.000 24.36532 ?  273 PHE A CE1 1 
ATOM   2004 C  CE2 . PHE A 1 293 ? 2.23100   7.87700   -0.49000  1.000 22.00258 ?  273 PHE A CE2 1 
ATOM   2005 C  CZ  . PHE A 1 293 ? 1.56400   8.24900   0.66200   1.000 20.15980 ?  273 PHE A CZ  1 
ATOM   2006 N  N   . ASP A 1 294 ? 1.27400   3.51200   -2.83000  1.000 15.28595 ?  274 ASP A N   1 
ATOM   2007 C  CA  . ASP A 1 294 ? 0.72300   4.11000   -4.04600  1.000 14.46364 ?  274 ASP A CA  1 
ATOM   2008 C  C   . ASP A 1 294 ? 0.97900   3.28900   -5.29900  1.000 13.68129 ?  274 ASP A C   1 
ATOM   2009 O  O   . ASP A 1 294 ? 1.14300   3.86300   -6.37900  1.000 17.05827 ?  274 ASP A O   1 
ATOM   2010 C  CB  . ASP A 1 294 ? 1.26900   5.53200   -4.25800  1.000 18.76542 ?  274 ASP A CB  1 
ATOM   2011 C  CG  . ASP A 1 294 ? 0.26300   6.45200   -4.93500  1.000 26.00119 ?  274 ASP A CG  1 
ATOM   2012 O  OD1 . ASP A 1 294 ? -0.93800  6.10100   -4.99900  1.000 20.86670 -1 274 ASP A OD1 1 
ATOM   2013 O  OD2 . ASP A 1 294 ? 0.68300   7.53100   -5.40700  1.000 24.32239 -1 274 ASP A OD2 1 
ATOM   2014 N  N   . GLN A 1 295 ? 1.00300   1.96300   -5.19200  1.000 15.35040 ?  275 GLN A N   1 
ATOM   2015 C  CA  . GLN A 1 295 ? 1.04000   1.14100   -6.38800  1.000 14.25590 ?  275 GLN A CA  1 
ATOM   2016 C  C   . GLN A 1 295 ? -0.17600  1.44900   -7.26500  1.000 15.22238 ?  275 GLN A C   1 
ATOM   2017 O  O   . GLN A 1 295 ? -1.23900  1.82800   -6.76100  1.000 12.31492 ?  275 GLN A O   1 
ATOM   2018 C  CB  . GLN A 1 295 ? 1.06800   -0.34300  -6.02100  1.000 13.51195 ?  275 GLN A CB  1 
ATOM   2019 C  CG  . GLN A 1 295 ? -0.16300  -0.81300  -5.25800  1.000 13.63717 ?  275 GLN A CG  1 
ATOM   2020 C  CD  . GLN A 1 295 ? -1.23200  -1.39100  -6.15300  1.000 16.54485 ?  275 GLN A CD  1 
ATOM   2021 O  OE1 . GLN A 1 295 ? -0.96400  -1.79200  -7.28300  1.000 15.28078 ?  275 GLN A OE1 1 
ATOM   2022 N  NE2 . GLN A 1 295 ? -2.47300  -1.39800  -5.66000  1.000 17.49481 ?  275 GLN A NE2 1 
ATOM   2023 N  N   . PRO A 1 296 ? -0.04900  1.28300   -8.58400  1.000 15.21627 ?  276 PRO A N   1 
ATOM   2024 C  CA  . PRO A 1 296 ? -1.05600  1.83900   -9.50600  1.000 15.00419 ?  276 PRO A CA  1 
ATOM   2025 C  C   . PRO A 1 296 ? -2.40300  1.12200   -9.56500  1.000 17.86827 ?  276 PRO A C   1 
ATOM   2026 O  O   . PRO A 1 296 ? -3.41800  1.75400   -9.88700  1.000 13.51216 ?  276 PRO A O   1 
ATOM   2027 C  CB  . PRO A 1 296 ? -0.34200  1.75500   -10.86100 1.000 18.37983 ?  276 PRO A CB  1 
ATOM   2028 C  CG  . PRO A 1 296 ? 0.57700   0.57100   -10.70900 1.000 16.82893 ?  276 PRO A CG  1 
ATOM   2029 C  CD  . PRO A 1 296 ? 1.09100   0.68900   -9.30700  1.000 16.03661 ?  276 PRO A CD  1 
ATOM   2030 N  N   . LEU A 1 297 ? -2.44900  -0.17600  -9.26200  1.000 15.50386 ?  277 LEU A N   1 
ATOM   2031 C  CA  . LEU A 1 297 ? -3.63400  -0.99100  -9.53700  1.000 17.98710 ?  277 LEU A CA  1 
ATOM   2032 C  C   . LEU A 1 297 ? -4.71000  -0.75800  -8.48300  1.000 17.34562 ?  277 LEU A C   1 
ATOM   2033 O  O   . LEU A 1 297 ? -4.57000  -1.18800  -7.33400  1.000 16.83383 ?  277 LEU A O   1 
ATOM   2034 C  CB  . LEU A 1 297 ? -3.24000  -2.46100  -9.60800  1.000 18.40898 ?  277 LEU A CB  1 
ATOM   2035 C  CG  . LEU A 1 297 ? -4.22600  -3.38100  -10.32400 1.000 21.56965 ?  277 LEU A CG  1 
ATOM   2036 C  CD1 . LEU A 1 297 ? -4.53600  -2.87800  -11.72800 1.000 27.84196 ?  277 LEU A CD1 1 
ATOM   2037 C  CD2 . LEU A 1 297 ? -3.66000  -4.78700  -10.37400 1.000 21.12898 ?  277 LEU A CD2 1 
ATOM   2038 N  N   . GLN A 1 298 ? -5.81000  -0.11300  -8.88000  1.000 15.85454 ?  278 GLN A N   1 
ATOM   2039 C  CA  . GLN A 1 298 ? -6.85300  0.22700   -7.91400  1.000 14.73189 ?  278 GLN A CA  1 
ATOM   2040 C  C   . GLN A 1 298 ? -7.84500  -0.90700  -7.69000  1.000 13.42258 ?  278 GLN A C   1 
ATOM   2041 O  O   . GLN A 1 298 ? -8.34700  -1.07000  -6.57000  1.000 14.26312 ?  278 GLN A O   1 
ATOM   2042 C  CB  . GLN A 1 298 ? -7.59200  1.49000   -8.36000  1.000 14.69518 ?  278 GLN A CB  1 
ATOM   2043 C  CG  . GLN A 1 298 ? -6.67100  2.67100   -8.63700  1.000 13.80981 ?  278 GLN A CG  1 
ATOM   2044 C  CD  . GLN A 1 298 ? -5.92400  3.10800   -7.38600  1.000 18.99242 ?  278 GLN A CD  1 
ATOM   2045 O  OE1 . GLN A 1 298 ? -6.53400  3.52200   -6.39500  1.000 15.09876 ?  278 GLN A OE1 1 
ATOM   2046 N  NE2 . GLN A 1 298 ? -4.59900  3.00600   -7.42200  1.000 16.09706 ?  278 GLN A NE2 1 
ATOM   2047 N  N   . TRP A 1 299 ? -8.15800  -1.68200  -8.72300  1.000 12.80591 ?  279 TRP A N   1 
ATOM   2048 C  CA  . TRP A 1 299 ? -9.13400  -2.75700  -8.61800  1.000 14.67409 ?  279 TRP A CA  1 
ATOM   2049 C  C   . TRP A 1 299 ? -8.57600  -4.03800  -9.21400  1.000 12.08257 ?  279 TRP A C   1 
ATOM   2050 O  O   . TRP A 1 299 ? -7.82300  -4.00900  -10.18700 1.000 15.68863 ?  279 TRP A O   1 
ATOM   2051 C  CB  . TRP A 1 299 ? -10.45500 -2.40200  -9.33400  1.000 12.63480 ?  279 TRP A CB  1 
ATOM   2052 C  CG  . TRP A 1 299 ? -10.91700 -0.99900  -9.07400  1.000 14.41426 ?  279 TRP A CG  1 
ATOM   2053 C  CD1 . TRP A 1 299 ? -10.68500 0.10600   -9.84500  1.000 18.59629 ?  279 TRP A CD1 1 
ATOM   2054 C  CD2 . TRP A 1 299 ? -11.67900 -0.55000  -7.95000  1.000 12.58113 ?  279 TRP A CD2 1 
ATOM   2055 N  NE1 . TRP A 1 299 ? -11.26500 1.21600   -9.26900  1.000 16.28888 ?  279 TRP A NE1 1 
ATOM   2056 C  CE2 . TRP A 1 299 ? -11.87900 0.83700   -8.10400  1.000 14.76109 ?  279 TRP A CE2 1 
ATOM   2057 C  CE3 . TRP A 1 299 ? -12.20900 -1.18700  -6.82600  1.000 13.99403 ?  279 TRP A CE3 1 
ATOM   2058 C  CZ2 . TRP A 1 299 ? -12.58700 1.59400   -7.17200  1.000 15.81792 ?  279 TRP A CZ2 1 
ATOM   2059 C  CZ3 . TRP A 1 299 ? -12.90900 -0.43700  -5.90600  1.000 13.94507 ?  279 TRP A CZ3 1 
ATOM   2060 C  CH2 . TRP A 1 299 ? -13.09100 0.94100   -6.08200  1.000 13.71802 ?  279 TRP A CH2 1 
ATOM   2061 N  N   . ALA A 1 300 ? -8.97100  -5.16700  -8.62900  1.000 9.14802  ?  280 ALA A N   1 
ATOM   2062 C  CA  . ALA A 1 300 ? -8.71500  -6.45400  -9.25500  1.000 13.28922 ?  280 ALA A CA  1 
ATOM   2063 C  C   . ALA A 1 300 ? -9.55100  -6.59100  -10.52800 1.000 13.97296 ?  280 ALA A C   1 
ATOM   2064 O  O   . ALA A 1 300 ? -10.43300 -5.77300  -10.81300 1.000 13.81432 ?  280 ALA A O   1 
ATOM   2065 C  CB  . ALA A 1 300 ? -9.03300  -7.59000  -8.28500  1.000 12.30204 ?  280 ALA A CB  1 
ATOM   2066 N  N   . ILE A 1 301 ? -9.32900  -7.68600  -11.26000 1.000 10.64659 ?  281 ILE A N   1 
ATOM   2067 C  CA  . ILE A 1 301 ? -10.17800 -7.95800  -12.45800 1.000 11.08141 ?  281 ILE A CA  1 
ATOM   2068 C  C   . ILE A 1 301 ? -11.61000 -8.18200  -11.96200 1.000 12.53972 ?  281 ILE A C   1 
ATOM   2069 O  O   . ILE A 1 301 ? -11.77000 -8.82600  -10.90500 1.000 10.57755 ?  281 ILE A O   1 
ATOM   2070 C  CB  . ILE A 1 301 ? -9.64800  -9.17800  -13.23700 1.000 13.66444 ?  281 ILE A CB  1 
ATOM   2071 C  CG1 . ILE A 1 301 ? -8.16400  -9.03000  -13.57800 1.000 22.26703 ?  281 ILE A CG1 1 
ATOM   2072 C  CG2 . ILE A 1 301 ? -10.48600 -9.44000  -14.47800 1.000 14.69306 ?  281 ILE A CG2 1 
ATOM   2073 C  CD1 . ILE A 1 301 ? -7.83800  -7.77900  -14.35500 1.000 19.36854 ?  281 ILE A CD1 1 
ATOM   2074 N  N   . ARG A 1 302 ? -12.60900 -7.67800  -12.69300 1.000 12.28594 ?  282 ARG A N   1 
ATOM   2075 C  CA  . ARG A 1 302 ? -14.02700 -7.80100  -12.25300 1.000 13.95338 ?  282 ARG A CA  1 
ATOM   2076 C  C   . ARG A 1 302 ? -14.34700 -9.26300  -11.91300 1.000 15.79916 ?  282 ARG A C   1 
ATOM   2077 O  O   . ARG A 1 302 ? -13.82400 -10.17300 -12.59600 1.000 11.10455 ?  282 ARG A O   1 
ATOM   2078 C  CB  . ARG A 1 302 ? -14.97300 -7.22800  -13.31500 1.000 14.68632 ?  282 ARG A CB  1 
ATOM   2079 C  CG  . ARG A 1 302 ? -15.37300 -8.19700  -14.41900 1.000 16.38211 ?  282 ARG A CG  1 
ATOM   2080 C  CD  . ARG A 1 302 ? -14.37100 -8.28400  -15.55500 1.000 11.34681 ?  282 ARG A CD  1 
ATOM   2081 N  NE  . ARG A 1 302 ? -14.69900 -9.32400  -16.51900 1.000 12.35151 ?  282 ARG A NE  1 
ATOM   2082 C  CZ  . ARG A 1 302 ? -14.27600 -10.58000 -16.44200 1.000 13.20817 ?  282 ARG A CZ  1 
ATOM   2083 N  NH1 . ARG A 1 302 ? -13.56700 -10.97700 -15.40000 1.000 13.72970 ?  282 ARG A NH1 1 
ATOM   2084 N  NH2 . ARG A 1 302 ? -14.56600 -11.43700 -17.40600 1.000 11.52050 ?  282 ARG A NH2 1 
ATOM   2085 N  N   . ARG A 1 303 ? -15.16000 -9.53700  -11.02800 1.000 15.77058 ?  283 ARG A N   1 
ATOM   2086 C  CA  . ARG A 1 303 ? -15.53000 -10.87600 -10.59600 1.000 9.09277  ?  283 ARG A CA  1 
ATOM   2087 C  C   . ARG A 1 303 ? -17.05000 -10.99800 -10.58000 1.000 9.91373  ?  283 ARG A C   1 
ATOM   2088 O  O   . ARG A 1 303 ? -17.76100 -10.00400 -10.40400 1.000 10.55831 ?  283 ARG A O   1 
ATOM   2089 C  CB  . ARG A 1 303 ? -14.96900 -11.19700 -9.19100  1.000 13.11235 ?  283 ARG A CB  1 
ATOM   2090 C  CG  . ARG A 1 303 ? -13.45200 -11.03000 -9.06700  1.000 18.91657 ?  283 ARG A CG  1 
ATOM   2091 C  CD  . ARG A 1 303 ? -12.71900 -12.36200 -9.06800  1.000 21.16139 ?  283 ARG A CD  1 
ATOM   2092 N  NE  . ARG A 1 303 ? -11.49400 -12.38000 -8.26500  1.000 11.56584 ?  283 ARG A NE  1 
ATOM   2093 C  CZ  . ARG A 1 303 ? -10.31400 -11.94200 -8.68500  1.000 12.19961 ?  283 ARG A CZ  1 
ATOM   2094 N  NH1 . ARG A 1 303 ? -10.19900 -11.19700 -9.76900  1.000 19.63991 ?  283 ARG A NH1 1 
ATOM   2095 N  NH2 . ARG A 1 303 ? -9.22100  -12.24500 -7.99000  1.000 11.44857 ?  283 ARG A NH2 1 
ATOM   2096 N  N   . PHE A 1 304 ? -17.50000 -12.27400 -10.74100 1.000 10.81493 ?  284 PHE A N   1 
ATOM   2097 C  CA  . PHE A 1 304 ? -18.95700 -12.56000 -10.78300 1.000 11.63828 ?  284 PHE A CA  1 
ATOM   2098 C  C   . PHE A 1 304 ? -19.28900 -13.68000 -9.79800  1.000 14.96717 ?  284 PHE A C   1 
ATOM   2099 O  O   . PHE A 1 304 ? -18.75800 -14.79700 -9.95400  1.000 14.08336 ?  284 PHE A O   1 
ATOM   2100 C  CB  . PHE A 1 304 ? -19.39800 -12.97600 -12.18700 1.000 10.63291 ?  284 PHE A CB  1 
ATOM   2101 C  CG  . PHE A 1 304 ? -18.75400 -12.19200 -13.29900 1.000 16.65315 ?  284 PHE A CG  1 
ATOM   2102 C  CD1 . PHE A 1 304 ? -19.06400 -10.85700 -13.49300 1.000 11.80005 ?  284 PHE A CD1 1 
ATOM   2103 C  CD2 . PHE A 1 304 ? -17.83200 -12.78900 -14.14300 1.000 12.67880 ?  284 PHE A CD2 1 
ATOM   2104 C  CE1 . PHE A 1 304 ? -18.46700 -10.13500 -14.51200 1.000 17.09064 ?  284 PHE A CE1 1 
ATOM   2105 C  CE2 . PHE A 1 304 ? -17.23600 -12.06500 -15.16100 1.000 13.35995 ?  284 PHE A CE2 1 
ATOM   2106 C  CZ  . PHE A 1 304 ? -17.56100 -10.74300 -15.34800 1.000 12.39410 ?  284 PHE A CZ  1 
ATOM   2107 N  N   . PRO A 1 305 ? -20.15100 -13.43600 -8.78800  1.000 15.96928 ?  285 PRO A N   1 
ATOM   2108 C  CA  . PRO A 1 305 ? -20.56100 -14.50100 -7.88500  1.000 16.62930 ?  285 PRO A CA  1 
ATOM   2109 C  C   . PRO A 1 305 ? -21.28600 -15.58700 -8.68800  1.000 15.84512 ?  285 PRO A C   1 
ATOM   2110 O  O   . PRO A 1 305 ? -22.17900 -15.27400 -9.41800  1.000 15.36714 ?  285 PRO A O   1 
ATOM   2111 C  CB  . PRO A 1 305 ? -21.48400 -13.78500 -6.88700  1.000 14.98132 ?  285 PRO A CB  1 
ATOM   2112 C  CG  . PRO A 1 305 ? -21.17800 -12.31500 -7.03700  1.000 17.06013 ?  285 PRO A CG  1 
ATOM   2113 C  CD  . PRO A 1 305 ? -20.75400 -12.14500 -8.47800  1.000 14.45398 ?  285 PRO A CD  1 
ATOM   2114 N  N   . THR A 1 306 ? -20.81000 -16.81500 -8.58900  1.000 12.75660 ?  286 THR A N   1 
ATOM   2115 C  CA  . THR A 1 306 ? -21.52000 -17.92200 -9.21800  1.000 18.07781 ?  286 THR A CA  1 
ATOM   2116 C  C   . THR A 1 306 ? -22.79600 -18.28600 -8.47200  1.000 14.97113 ?  286 THR A C   1 
ATOM   2117 O  O   . THR A 1 306 ? -23.58700 -19.08600 -8.98000  1.000 12.86060 ?  286 THR A O   1 
ATOM   2118 C  CB  . THR A 1 306 ? -20.61600 -19.15300 -9.31900  1.000 14.60717 ?  286 THR A CB  1 
ATOM   2119 O  OG1 . THR A 1 306 ? -20.21300 -19.56600 -8.00700  1.000 17.77889 ?  286 THR A OG1 1 
ATOM   2120 C  CG2 . THR A 1 306 ? -19.38800 -18.84400 -10.15800 1.000 20.52234 ?  286 THR A CG2 1 
ATOM   2121 N  N   . ARG A 1 307 ? -22.99500 -17.72800 -7.28100  1.000 12.35268 ?  287 ARG A N   1 
ATOM   2122 C  CA  . ARG A 1 307 ? -24.21000 -17.88000 -6.49500  1.000 23.63022 ?  287 ARG A CA  1 
ATOM   2123 C  C   . ARG A 1 307 ? -24.40900 -16.57100 -5.74900  1.000 20.30972 ?  287 ARG A C   1 
ATOM   2124 O  O   . ARG A 1 307 ? -23.50100 -15.73700 -5.69200  1.000 18.41077 ?  287 ARG A O   1 
ATOM   2125 C  CB  . ARG A 1 307 ? -24.10000 -19.06100 -5.52400  1.000 16.84352 ?  287 ARG A CB  1 
ATOM   2126 C  CG  . ARG A 1 307 ? -22.88600 -18.94200 -4.59900  1.000 17.48889 ?  287 ARG A CG  1 
ATOM   2127 C  CD  . ARG A 1 307 ? -23.04300 -19.75200 -3.32400  1.000 15.41039 ?  287 ARG A CD  1 
ATOM   2128 N  NE  . ARG A 1 307 ? -24.13000 -19.23800 -2.49900  1.000 19.99559 ?  287 ARG A NE  1 
ATOM   2129 C  CZ  . ARG A 1 307 ? -24.77100 -19.94200 -1.57600  1.000 22.90330 ?  287 ARG A CZ  1 
ATOM   2130 N  NH1 . ARG A 1 307 ? -24.34700 -21.14000 -1.20100  1.000 13.48792 ?  287 ARG A NH1 1 
ATOM   2131 N  NH2 . ARG A 1 307 ? -25.86000 -19.42800 -1.00700  1.000 20.88188 ?  287 ARG A NH2 1 
ATOM   2132 N  N   . GLU A 1 308 ? -25.59400 -16.38000 -5.16800  1.000 15.74264 ?  288 GLU A N   1 
ATOM   2133 C  CA  . GLU A 1 308 ? -25.75700 -15.22800 -4.28500  1.000 20.28994 ?  288 GLU A CA  1 
ATOM   2134 C  C   . GLU A 1 308 ? -24.78000 -15.34900 -3.12300  1.000 19.87723 ?  288 GLU A C   1 
ATOM   2135 O  O   . GLU A 1 308 ? -24.68200 -16.40000 -2.48400  1.000 20.82137 ?  288 GLU A O   1 
ATOM   2136 C  CB  . GLU A 1 308 ? -27.19600 -15.09800 -3.77100  1.000 21.46537 ?  288 GLU A CB  1 
ATOM   2137 C  CG  . GLU A 1 308 ? -27.47400 -13.71000 -3.16900  1.000 24.25445 ?  288 GLU A CG  1 
ATOM   2138 C  CD  . GLU A 1 308 ? -28.95500 -13.34100 -3.06900  1.000 34.64596 ?  288 GLU A CD  1 
ATOM   2139 O  OE1 . GLU A 1 308 ? -29.79500 -14.23700 -2.82300  1.000 33.40206 ?  288 GLU A OE1 1 
ATOM   2140 O  OE2 . GLU A 1 308 ? -29.27600 -12.13700 -3.21700  1.000 34.87522 -1 288 GLU A OE2 1 
ATOM   2141 N  N   . LEU A 1 309 ? -24.03100 -14.27800 -2.87200  1.000 19.61902 ?  289 LEU A N   1 
ATOM   2142 C  CA  . LEU A 1 309 ? -22.90400 -14.31200 -1.95400  1.000 15.99679 ?  289 LEU A CA  1 
ATOM   2143 C  C   . LEU A 1 309 ? -22.97400 -13.12300 -1.01100  1.000 19.61792 ?  289 LEU A C   1 
ATOM   2144 O  O   . LEU A 1 309 ? -23.21300 -11.99200 -1.44500  1.000 20.18003 ?  289 LEU A O   1 
ATOM   2145 C  CB  . LEU A 1 309 ? -21.57900 -14.29800 -2.72600  1.000 19.94056 ?  289 LEU A CB  1 
ATOM   2146 C  CG  . LEU A 1 309 ? -20.40300 -15.09100 -2.16200  1.000 23.29135 ?  289 LEU A CG  1 
ATOM   2147 C  CD1 . LEU A 1 309 ? -20.75300 -16.55700 -1.98700  1.000 22.98498 ?  289 LEU A CD1 1 
ATOM   2148 C  CD2 . LEU A 1 309 ? -19.19700 -14.93900 -3.08900  1.000 29.07953 ?  289 LEU A CD2 1 
ATOM   2149 N  N   . ASP A 1 310 ? -22.77400 -13.38200 0.27500   1.000 18.31117 ?  290 ASP A N   1 
ATOM   2150 C  CA  . ASP A 1 310 ? -22.71500 -12.31100 1.25800   1.000 18.91532 ?  290 ASP A CA  1 
ATOM   2151 C  C   . ASP A 1 310 ? -21.31700 -11.71200 1.20400   1.000 19.16971 ?  290 ASP A C   1 
ATOM   2152 O  O   . ASP A 1 310 ? -20.33400 -12.37500 1.54700   1.000 22.47056 ?  290 ASP A O   1 
ATOM   2153 C  CB  . ASP A 1 310 ? -23.04600 -12.83400 2.65200   1.000 21.96185 ?  290 ASP A CB  1 
ATOM   2154 C  CG  . ASP A 1 310 ? -23.18600 -11.72200 3.67300   1.000 26.59231 ?  290 ASP A CG  1 
ATOM   2155 O  OD1 . ASP A 1 310 ? -23.02500 -10.54000 3.30400   1.000 37.78095 -1 290 ASP A OD1 1 
ATOM   2156 O  OD2 . ASP A 1 310 ? -23.46500 -12.03000 4.84700   1.000 27.34151 -1 290 ASP A OD2 1 
ATOM   2157 N  N   . ILE A 1 311 ? -21.22700 -10.47500 0.73600   1.000 17.91922 ?  291 ILE A N   1 
ATOM   2158 C  CA  . ILE A 1 311 ? -19.97400 -9.73700  0.67200   1.000 19.85672 ?  291 ILE A CA  1 
ATOM   2159 C  C   . ILE A 1 311 ? -20.12900 -8.49800  1.53500   1.000 18.95253 ?  291 ILE A C   1 
ATOM   2160 O  O   . ILE A 1 311 ? -21.02500 -7.68000  1.29900   1.000 21.11244 ?  291 ILE A O   1 
ATOM   2161 C  CB  . ILE A 1 311 ? -19.59600 -9.36800  -0.77000  1.000 18.00923 ?  291 ILE A CB  1 
ATOM   2162 C  CG1 . ILE A 1 311 ? -19.45200 -10.63900 -1.61200  1.000 16.48608 ?  291 ILE A CG1 1 
ATOM   2163 C  CG2 . ILE A 1 311 ? -18.30400 -8.55100  -0.79000  1.000 20.73095 ?  291 ILE A CG2 1 
ATOM   2164 C  CD1 . ILE A 1 311 ? -19.24200 -10.37900 -3.09000  1.000 15.87457 ?  291 ILE A CD1 1 
ATOM   2165 N  N   . ALA A 1 312 ? -19.27900 -8.37900  2.55400   1.000 24.73257 ?  292 ALA A N   1 
ATOM   2166 C  CA  . ALA A 1 312 ? -19.26000 -7.21600  3.44000   1.000 23.38013 ?  292 ALA A CA  1 
ATOM   2167 C  C   . ALA A 1 312 ? -20.63000 -6.93700  4.05200   1.000 25.26608 ?  292 ALA A C   1 
ATOM   2168 O  O   . ALA A 1 312 ? -20.95500 -5.79200  4.36900   1.000 28.45385 ?  292 ALA A O   1 
ATOM   2169 C  CB  . ALA A 1 312 ? -18.73700 -5.97600  2.70800   1.000 18.26413 ?  292 ALA A CB  1 
ATOM   2170 N  N   . GLY A 1 313 ? -21.45300 -7.97400  4.21000   1.000 23.31936 ?  293 GLY A N   1 
ATOM   2171 C  CA  . GLY A 1 313 ? -22.75300 -7.84000  4.83700   1.000 21.40614 ?  293 GLY A CA  1 
ATOM   2172 C  C   . GLY A 1 313 ? -23.92100 -7.64400  3.89400   1.000 23.92474 ?  293 GLY A C   1 
ATOM   2173 O  O   . GLY A 1 313 ? -25.05600 -7.50300  4.36700   1.000 28.56811 ?  293 GLY A O   1 
ATOM   2174 N  N   . VAL A 1 314 ? -23.69100 -7.62700  2.58400   1.000 21.62734 ?  294 VAL A N   1 
ATOM   2175 C  CA  . VAL A 1 314 ? -24.75300 -7.50000  1.59300   1.000 24.69591 ?  294 VAL A CA  1 
ATOM   2176 C  C   . VAL A 1 314 ? -24.78100 -8.77700  0.76300   1.000 23.42558 ?  294 VAL A C   1 
ATOM   2177 O  O   . VAL A 1 314 ? -23.73300 -9.25200  0.30800   1.000 19.07766 ?  294 VAL A O   1 
ATOM   2178 C  CB  . VAL A 1 314 ? -24.55400 -6.25900  0.70300   1.000 22.73113 ?  294 VAL A CB  1 
ATOM   2179 C  CG1 . VAL A 1 314 ? -25.42600 -6.33500  -0.53600  1.000 24.22173 ?  294 VAL A CG1 1 
ATOM   2180 C  CG2 . VAL A 1 314 ? -24.86200 -4.99800  1.48700   1.000 30.02593 ?  294 VAL A CG2 1 
ATOM   2181 N  N   . GLU A 1 315 ? -25.97100 -9.35000  0.59300   1.000 15.56261 ?  295 GLU A N   1 
ATOM   2182 C  CA  . GLU A 1 315 ? -26.11900 -10.51600 -0.26800  1.000 15.37748 ?  295 GLU A CA  1 
ATOM   2183 C  C   . GLU A 1 315 ? -26.11600 -10.05600 -1.72100  1.000 18.22094 ?  295 GLU A C   1 
ATOM   2184 O  O   . GLU A 1 315 ? -27.08800 -9.46700  -2.20600  1.000 16.60221 ?  295 GLU A O   1 
ATOM   2185 C  CB  . GLU A 1 315 ? -27.37700 -11.30500 0.08600   1.000 19.39634 ?  295 GLU A CB  1 
ATOM   2186 C  CG  . GLU A 1 315 ? -27.20400 -12.13900 1.35400   1.000 17.87887 ?  295 GLU A CG  1 
ATOM   2187 C  CD  . GLU A 1 315 ? -28.40600 -13.00700 1.66300   1.000 21.91221 ?  295 GLU A CD  1 
ATOM   2188 O  OE1 . GLU A 1 315 ? -29.44100 -12.44900 2.06400   1.000 20.69364 ?  295 GLU A OE1 1 
ATOM   2189 O  OE2 . GLU A 1 315 ? -28.32000 -14.24200 1.48300   1.000 28.25164 -1 295 GLU A OE2 1 
ATOM   2190 N  N   . VAL A 1 316 ? -25.01300 -10.32100 -2.41000  1.000 12.00468 ?  296 VAL A N   1 
ATOM   2191 C  CA  . VAL A 1 316 ? -24.80600 -9.86500  -3.78000  1.000 10.24092 ?  296 VAL A CA  1 
ATOM   2192 C  C   . VAL A 1 316 ? -25.36000 -10.89200 -4.75700  1.000 14.37047 ?  296 VAL A C   1 
ATOM   2193 O  O   . VAL A 1 316 ? -25.02000 -12.08200 -4.66700  1.000 14.63934 ?  296 VAL A O   1 
ATOM   2194 C  CB  . VAL A 1 316 ? -23.31400 -9.59600  -4.04000  1.000 14.57891 ?  296 VAL A CB  1 
ATOM   2195 C  CG1 . VAL A 1 316 ? -23.06400 -9.41600  -5.51900  1.000 15.29528 ?  296 VAL A CG1 1 
ATOM   2196 C  CG2 . VAL A 1 316 ? -22.87200 -8.36300  -3.26300  1.000 10.77024 ?  296 VAL A CG2 1 
ATOM   2197 N  N   . PRO A 1 317 ? -26.20600 -10.47500 -5.70100  1.000 15.42200 ?  297 PRO A N   1 
ATOM   2198 C  CA  . PRO A 1 317 ? -26.84700 -11.43500 -6.60500  1.000 21.16414 ?  297 PRO A CA  1 
ATOM   2199 C  C   . PRO A 1 317 ? -25.84400 -12.15200 -7.49500  1.000 17.93893 ?  297 PRO A C   1 
ATOM   2200 O  O   . PRO A 1 317 ? -24.81000 -11.60100 -7.87400  1.000 14.37337 ?  297 PRO A O   1 
ATOM   2201 C  CB  . PRO A 1 317 ? -27.78700 -10.55300 -7.43800  1.000 16.19129 ?  297 PRO A CB  1 
ATOM   2202 C  CG  . PRO A 1 317 ? -28.05800 -9.37800  -6.55900  1.000 24.01698 ?  297 PRO A CG  1 
ATOM   2203 C  CD  . PRO A 1 317 ? -26.73800 -9.11400  -5.89000  1.000 19.60058 ?  297 PRO A CD  1 
ATOM   2204 N  N   . ALA A 1 318 ? -26.17400 -13.39400 -7.83700  1.000 18.63527 ?  298 ALA A N   1 
ATOM   2205 C  CA  . ALA A 1 318 ? -25.36200 -14.15800 -8.77600  1.000 20.84710 ?  298 ALA A CA  1 
ATOM   2206 C  C   . ALA A 1 318 ? -25.23000 -13.40700 -10.09700 1.000 17.96657 ?  298 ALA A C   1 
ATOM   2207 O  O   . ALA A 1 318 ? -26.21900 -12.91300 -10.64600 1.000 16.57077 ?  298 ALA A O   1 
ATOM   2208 C  CB  . ALA A 1 318 ? -25.98800 -15.53400 -9.00800  1.000 16.15904 ?  298 ALA A CB  1 
ATOM   2209 N  N   . GLY A 1 319 ? -24.00100 -13.31400 -10.60300 1.000 14.63271 ?  299 GLY A N   1 
ATOM   2210 C  CA  . GLY A 1 319 ? -23.75400 -12.69900 -11.88700 1.000 12.85287 ?  299 GLY A CA  1 
ATOM   2211 C  C   . GLY A 1 319 ? -23.52400 -11.20500 -11.86300 1.000 13.62915 ?  299 GLY A C   1 
ATOM   2212 O  O   . GLY A 1 319 ? -23.18700 -10.63600 -12.90900 1.000 13.70945 ?  299 GLY A O   1 
ATOM   2213 N  N   . ASP A 1 320 ? -23.69600 -10.55300 -10.71300 1.000 9.12861  ?  300 ASP A N   1 
ATOM   2214 C  CA  . ASP A 1 320 ? -23.43400 -9.12700  -10.58800 1.000 10.52501 ?  300 ASP A CA  1 
ATOM   2215 C  C   . ASP A 1 320 ? -21.92400 -8.89100  -10.69900 1.000 12.84563 ?  300 ASP A C   1 
ATOM   2216 O  O   . ASP A 1 320 ? -21.12000 -9.79200  -10.45700 1.000 15.97412 ?  300 ASP A O   1 
ATOM   2217 C  CB  . ASP A 1 320 ? -23.97500 -8.61300  -9.25000  1.000 12.40165 ?  300 ASP A CB  1 
ATOM   2218 C  CG  . ASP A 1 320 ? -25.40500 -8.08400  -9.36200  1.000 16.44811 ?  300 ASP A CG  1 
ATOM   2219 O  OD1 . ASP A 1 320 ? -26.07900 -8.50300  -10.32000 1.000 17.92920 -1 300 ASP A OD1 1 
ATOM   2220 O  OD2 . ASP A 1 320 ? -25.85000 -7.27700  -8.51300  1.000 16.66375 -1 300 ASP A OD2 1 
ATOM   2221 N  N   . THR A 1 321 ? -21.54000 -7.67800  -11.10300 1.000 10.83873 ?  301 THR A N   1 
ATOM   2222 C  CA  . THR A 1 321 ? -20.12800 -7.31300  -11.23500 1.000 8.03021  ?  301 THR A CA  1 
ATOM   2223 C  C   . THR A 1 321 ? -19.58500 -6.78800  -9.91300  1.000 11.17104 ?  301 THR A C   1 
ATOM   2224 O  O   . THR A 1 321 ? -20.14900 -5.85500  -9.33000  1.000 11.77983 ?  301 THR A O   1 
ATOM   2225 C  CB  . THR A 1 321 ? -19.93300 -6.26200  -12.33000 1.000 9.55515  ?  301 THR A CB  1 
ATOM   2226 O  OG1 . THR A 1 321 ? -20.43300 -6.76800  -13.57000 1.000 14.54318 ?  301 THR A OG1 1 
ATOM   2227 C  CG2 . THR A 1 321 ? -18.44100 -5.90200  -12.47900 1.000 16.88656 ?  301 THR A CG2 1 
ATOM   2228 N  N   . VAL A 1 322 ? -18.47100 -7.36800  -9.46000  1.000 12.24855 ?  302 VAL A N   1 
ATOM   2229 C  CA  . VAL A 1 322 ? -17.88600 -7.05900  -8.16000  1.000 10.66526 ?  302 VAL A CA  1 
ATOM   2230 C  C   . VAL A 1 322 ? -16.45700 -6.58500  -8.38300  1.000 8.25760  ?  302 VAL A C   1 
ATOM   2231 O  O   . VAL A 1 322 ? -15.65900 -7.28600  -9.01400  1.000 12.78396 ?  302 VAL A O   1 
ATOM   2232 C  CB  . VAL A 1 322 ? -17.91300 -8.28000  -7.22000  1.000 15.11061 ?  302 VAL A CB  1 
ATOM   2233 C  CG1 . VAL A 1 322 ? -17.02900 -8.03200  -5.98700  1.000 13.58497 ?  302 VAL A CG1 1 
ATOM   2234 C  CG2 . VAL A 1 322 ? -19.34200 -8.62600  -6.82300  1.000 13.62427 ?  302 VAL A CG2 1 
ATOM   2235 N  N   . LEU A 1 323 ? -16.14000 -5.40200  -7.87700  1.000 8.88453  ?  303 LEU A N   1 
ATOM   2236 C  CA  . LEU A 1 323 ? -14.80800 -4.82400  -8.00800  1.000 10.39458 ?  303 LEU A CA  1 
ATOM   2237 C  C   . LEU A 1 323 ? -14.15200 -4.84600  -6.63700  1.000 12.46853 ?  303 LEU A C   1 
ATOM   2238 O  O   . LEU A 1 323 ? -14.63500 -4.18900  -5.70600  1.000 10.68229 ?  303 LEU A O   1 
ATOM   2239 C  CB  . LEU A 1 323 ? -14.88300 -3.39700  -8.54800  1.000 14.37305 ?  303 LEU A CB  1 
ATOM   2240 C  CG  . LEU A 1 323 ? -15.56500 -3.26200  -9.91300  1.000 21.19654 ?  303 LEU A CG  1 
ATOM   2241 C  CD1 . LEU A 1 323 ? -15.42600 -1.84700  -10.45100 1.000 20.94179 ?  303 LEU A CD1 1 
ATOM   2242 C  CD2 . LEU A 1 323 ? -14.97900 -4.27100  -10.89900 1.000 16.56764 ?  303 LEU A CD2 1 
ATOM   2243 N  N   . LEU A 1 324 ? -13.05700 -5.59400  -6.51200  1.000 10.42664 ?  304 LEU A N   1 
ATOM   2244 C  CA  . LEU A 1 324 ? -12.36100 -5.71400  -5.24100  1.000 10.10673 ?  304 LEU A CA  1 
ATOM   2245 C  C   . LEU A 1 324 ? -11.27900 -4.64200  -5.19000  1.000 12.01162 ?  304 LEU A C   1 
ATOM   2246 O  O   . LEU A 1 324 ? -10.40600 -4.59900  -6.05800  1.000 11.21314 ?  304 LEU A O   1 
ATOM   2247 C  CB  . LEU A 1 324 ? -11.77300 -7.11700  -5.06900  1.000 12.55546 ?  304 LEU A CB  1 
ATOM   2248 C  CG  . LEU A 1 324 ? -12.81500 -8.24800  -5.12700  1.000 15.56851 ?  304 LEU A CG  1 
ATOM   2249 C  CD1 . LEU A 1 324 ? -12.14500 -9.62100  -5.18500  1.000 12.87331 ?  304 LEU A CD1 1 
ATOM   2250 C  CD2 . LEU A 1 324 ? -13.80900 -8.18200  -3.96700  1.000 12.46523 ?  304 LEU A CD2 1 
ATOM   2251 N  N   . GLY A 1 325 ? -11.37100 -3.75500  -4.20400  1.000 11.78090 ?  305 GLY A N   1 
ATOM   2252 C  CA  . GLY A 1 325 ? -10.51400 -2.59000  -4.13900  1.000 8.99568  ?  305 GLY A CA  1 
ATOM   2253 C  C   . GLY A 1 325 ? -9.17300  -2.87500  -3.49900  1.000 10.03813 ?  305 GLY A C   1 
ATOM   2254 O  O   . GLY A 1 325 ? -9.02000  -2.76300  -2.28000  1.000 10.87780 ?  305 GLY A O   1 
ATOM   2255 N  N   . ILE A 1 326 ? -8.19900  -3.25600  -4.32700  1.000 9.39716  ?  306 ILE A N   1 
ATOM   2256 C  CA  . ILE A 1 326 ? -6.85900  -3.56100  -3.82400  1.000 12.14410 ?  306 ILE A CA  1 
ATOM   2257 C  C   . ILE A 1 326 ? -6.23700  -2.33700  -3.16600  1.000 11.99484 ?  306 ILE A C   1 
ATOM   2258 O  O   . ILE A 1 326 ? -5.69000  -2.42100  -2.06100  1.000 11.40697 ?  306 ILE A O   1 
ATOM   2259 C  CB  . ILE A 1 326 ? -5.97500  -4.10900  -4.95800  1.000 13.68122 ?  306 ILE A CB  1 
ATOM   2260 C  CG1 . ILE A 1 326 ? -6.45200  -5.50600  -5.36300  1.000 11.49827 ?  306 ILE A CG1 1 
ATOM   2261 C  CG2 . ILE A 1 326 ? -4.48400  -4.08000  -4.56400  1.000 15.16046 ?  306 ILE A CG2 1 
ATOM   2262 C  CD1 . ILE A 1 326 ? -5.99100  -5.94400  -6.73300  1.000 16.63581 ?  306 ILE A CD1 1 
ATOM   2263 N  N   . ALA A 1 327 ? -6.31600  -1.17800  -3.82900  1.000 9.77282  ?  307 ALA A N   1 
ATOM   2264 C  CA  . ALA A 1 327 ? -5.70900  0.03200   -3.27600  1.000 10.95968 ?  307 ALA A CA  1 
ATOM   2265 C  C   . ALA A 1 327 ? -6.36900  0.43500   -1.96400  1.000 12.79900 ?  307 ALA A C   1 
ATOM   2266 O  O   . ALA A 1 327 ? -5.68400  0.76800   -0.99200  1.000 9.76796  ?  307 ALA A O   1 
ATOM   2267 C  CB  . ALA A 1 327 ? -5.78100  1.17500   -4.28600  1.000 11.60021 ?  307 ALA A CB  1 
ATOM   2268 N  N   . SER A 1 328 ? -7.70500  0.41300   -1.92000  1.000 10.17708 ?  308 SER A N   1 
ATOM   2269 C  CA  . SER A 1 328 ? -8.41500  0.69300   -0.67600  1.000 9.74251  ?  308 SER A CA  1 
ATOM   2270 C  C   . SER A 1 328 ? -7.96500  -0.23500  0.44400   1.000 9.74301  ?  308 SER A C   1 
ATOM   2271 O  O   . SER A 1 328 ? -7.71200  0.21100   1.57000   1.000 12.43112 ?  308 SER A O   1 
ATOM   2272 C  CB  . SER A 1 328 ? -9.92500  0.56500   -0.88900  1.000 12.33440 ?  308 SER A CB  1 
ATOM   2273 O  OG  . SER A 1 328 ? -10.62300 0.95000   0.28700   1.000 14.13273 ?  308 SER A OG  1 
ATOM   2274 N  N   . ALA A 1 329 ? -7.88300  -1.53900  0.15800   1.000 11.25927 ?  309 ALA A N   1 
ATOM   2275 C  CA  . ALA A 1 329 ? -7.46100  -2.49200  1.18000   1.000 11.30960 ?  309 ALA A CA  1 
ATOM   2276 C  C   . ALA A 1 329 ? -6.08200  -2.14400  1.71800   1.000 13.31812 ?  309 ALA A C   1 
ATOM   2277 O  O   . ALA A 1 329 ? -5.84400  -2.20600  2.93200   1.000 12.40938 ?  309 ALA A O   1 
ATOM   2278 C  CB  . ALA A 1 329 ? -7.47000  -3.91200  0.61200   1.000 9.08857  ?  309 ALA A CB  1 
ATOM   2279 N  N   . ASN A 1 330 ? -5.16300  -1.76100  0.82800   1.000 9.52932  ?  310 ASN A N   1 
ATOM   2280 C  CA  . ASN A 1 330 ? -3.81400  -1.38200  1.24100   1.000 12.57450 ?  310 ASN A CA  1 
ATOM   2281 C  C   . ASN A 1 330 ? -3.79700  -0.16600  2.15500   1.000 16.96424 ?  310 ASN A C   1 
ATOM   2282 O  O   . ASN A 1 330 ? -2.77600  0.09500   2.80200   1.000 13.44945 ?  310 ASN A O   1 
ATOM   2283 C  CB  . ASN A 1 330 ? -2.95300  -1.11000  0.00400   1.000 12.56871 ?  310 ASN A CB  1 
ATOM   2284 C  CG  . ASN A 1 330 ? -2.56100  -2.37900  -0.72700  1.000 14.30402 ?  310 ASN A CG  1 
ATOM   2285 O  OD1 . ASN A 1 330 ? -2.75200  -3.48800  -0.22300  1.000 16.17589 ?  310 ASN A OD1 1 
ATOM   2286 N  ND2 . ASN A 1 330 ? -2.04100  -2.22300  -1.94400  1.000 11.33929 ?  310 ASN A ND2 1 
ATOM   2287 N  N   . HIS A 1 331 ? -4.89400  0.59200   2.22400   1.000 12.98562 ?  311 HIS A N   1 
ATOM   2288 C  CA  . HIS A 1 331 ? -4.96400  1.75400   3.10000   1.000 14.20638 ?  311 HIS A CA  1 
ATOM   2289 C  C   . HIS A 1 331 ? -6.01200  1.58100   4.20000   1.000 15.82101 ?  311 HIS A C   1 
ATOM   2290 O  O   . HIS A 1 331 ? -6.46500  2.57000   4.78000   1.000 18.70811 ?  311 HIS A O   1 
ATOM   2291 C  CB  . HIS A 1 331 ? -5.23400  3.01600   2.27900   1.000 13.22173 ?  311 HIS A CB  1 
ATOM   2292 C  CG  . HIS A 1 331 ? -4.02600  3.52900   1.55200   1.000 19.96404 ?  311 HIS A CG  1 
ATOM   2293 N  ND1 . HIS A 1 331 ? -3.50000  4.78500   1.77100   1.000 16.71994 ?  311 HIS A ND1 1 
ATOM   2294 C  CD2 . HIS A 1 331 ? -3.23100  2.94700   0.62200   1.000 16.93705 ?  311 HIS A CD2 1 
ATOM   2295 C  CE1 . HIS A 1 331 ? -2.44200  4.95900   1.00000   1.000 17.37872 ?  311 HIS A CE1 1 
ATOM   2296 N  NE2 . HIS A 1 331 ? -2.26200  3.86300   0.28600   1.000 16.63855 ?  311 HIS A NE2 1 
ATOM   2297 N  N   . ASP A 1 332 ? -6.38600  0.33900   4.50500   1.000 13.94062 ?  312 ASP A N   1 
ATOM   2298 C  CA  . ASP A 1 332 ? -7.37200  0.03700   5.54000   1.000 13.74842 ?  312 ASP A CA  1 
ATOM   2299 C  C   . ASP A 1 332 ? -6.76100  0.27200   6.91800   1.000 16.99464 ?  312 ASP A C   1 
ATOM   2300 O  O   . ASP A 1 332 ? -5.84200  -0.44400  7.33000   1.000 19.09968 ?  312 ASP A O   1 
ATOM   2301 C  CB  . ASP A 1 332 ? -7.85200  -1.40600  5.38700   1.000 14.49587 ?  312 ASP A CB  1 
ATOM   2302 C  CG  . ASP A 1 332 ? -9.13300  -1.69000  6.17300   1.000 15.39602 ?  312 ASP A CG  1 
ATOM   2303 O  OD1 . ASP A 1 332 ? -9.36400  -1.02900  7.21000   1.000 15.49626 ?  312 ASP A OD1 1 
ATOM   2304 O  OD2 . ASP A 1 332 ? -9.90500  -2.58200  5.75500   1.000 15.71869 -1 312 ASP A OD2 1 
ATOM   2305 N  N   . GLU A 1 333 ? -7.29300  1.25800   7.64300   1.000 15.91514 ?  313 GLU A N   1 
ATOM   2306 C  CA  . GLU A 1 333 ? -6.75300  1.61300   8.95300   1.000 21.64852 ?  313 GLU A CA  1 
ATOM   2307 C  C   . GLU A 1 333 ? -6.91100  0.49400   9.97900   1.000 22.74285 ?  313 GLU A C   1 
ATOM   2308 O  O   . GLU A 1 333 ? -6.20900  0.50500   10.99700  1.000 22.11496 ?  313 GLU A O   1 
ATOM   2309 C  CB  . GLU A 1 333 ? -7.43700  2.87400   9.48100   1.000 25.72005 ?  313 GLU A CB  1 
ATOM   2310 C  CG  . GLU A 1 333 ? -8.90400  2.66300   9.83300   1.000 27.03466 ?  313 GLU A CG  1 
ATOM   2311 C  CD  . GLU A 1 333 ? -9.82500  2.73000   8.63100   1.000 30.62131 ?  313 GLU A CD  1 
ATOM   2312 O  OE1 . GLU A 1 333 ? -9.32800  2.94000   7.50600   1.000 20.50201 ?  313 GLU A OE1 1 
ATOM   2313 O  OE2 . GLU A 1 333 ? -11.04800 2.56100   8.81700   1.000 35.81980 -1 313 GLU A OE2 1 
ATOM   2314 N  N   . THR A 1 334 ? -7.82000  -0.45500  9.75400   1.000 17.21917 ?  314 THR A N   1 
ATOM   2315 C  CA  . THR A 1 334 ? -7.96700  -1.56000  10.69200  1.000 21.31148 ?  314 THR A CA  1 
ATOM   2316 C  C   . THR A 1 334 ? -6.86300  -2.59300  10.53900  1.000 16.41371 ?  314 THR A C   1 
ATOM   2317 O  O   . THR A 1 334 ? -6.80600  -3.53800  11.33300  1.000 19.10883 ?  314 THR A O   1 
ATOM   2318 C  CB  . THR A 1 334 ? -9.32100  -2.26100  10.52000  1.000 18.99203 ?  314 THR A CB  1 
ATOM   2319 O  OG1 . THR A 1 334 ? -9.30400  -3.07100  9.33800   1.000 17.91619 ?  314 THR A OG1 1 
ATOM   2320 C  CG2 . THR A 1 334 ? -10.43100 -1.23500  10.40200  1.000 17.99423 ?  314 THR A CG2 1 
ATOM   2321 N  N   . VAL A 1 335 ? -5.99800  -2.43600  9.53700   1.000 18.43139 ?  315 VAL A N   1 
ATOM   2322 C  CA  . VAL A 1 335 ? -4.86400  -3.32200  9.30800   1.000 16.49168 ?  315 VAL A CA  1 
ATOM   2323 C  C   . VAL A 1 335 ? -3.54100  -2.57700  9.44800   1.000 15.44847 ?  315 VAL A C   1 
ATOM   2324 O  O   . VAL A 1 335 ? -2.61700  -3.05100  10.11500  1.000 18.41243 ?  315 VAL A O   1 
ATOM   2325 C  CB  . VAL A 1 335 ? -4.95700  -4.00800  7.92500   1.000 14.85223 ?  315 VAL A CB  1 
ATOM   2326 C  CG1 . VAL A 1 335 ? -3.76200  -4.92600  7.69700   1.000 16.61026 ?  315 VAL A CG1 1 
ATOM   2327 C  CG2 . VAL A 1 335 ? -6.27000  -4.77500  7.79100   1.000 16.90130 ?  315 VAL A CG2 1 
ATOM   2328 N  N   . PHE A 1 336 ? -3.43800  -1.40100  8.83300   1.000 16.93743 ?  316 PHE A N   1 
ATOM   2329 C  CA  . PHE A 1 336 ? -2.21900  -0.60000  8.82800   1.000 19.02657 ?  316 PHE A CA  1 
ATOM   2330 C  C   . PHE A 1 336 ? -2.42600  0.66300   9.65300   1.000 19.12884 ?  316 PHE A C   1 
ATOM   2331 O  O   . PHE A 1 336 ? -3.37300  1.41800   9.41400   1.000 22.92390 ?  316 PHE A O   1 
ATOM   2332 C  CB  . PHE A 1 336 ? -1.80500  -0.21600  7.40300   1.000 19.89938 ?  316 PHE A CB  1 
ATOM   2333 C  CG  . PHE A 1 336 ? -1.83400  -1.35300  6.42100   1.000 14.68153 ?  316 PHE A CG  1 
ATOM   2334 C  CD1 . PHE A 1 336 ? -0.70400  -2.13200  6.21600   1.000 16.19309 ?  316 PHE A CD1 1 
ATOM   2335 C  CD2 . PHE A 1 336 ? -2.97200  -1.62200  5.67600   1.000 12.52948 ?  316 PHE A CD2 1 
ATOM   2336 C  CE1 . PHE A 1 336 ? -0.71200  -3.17100  5.30400   1.000 15.65884 ?  316 PHE A CE1 1 
ATOM   2337 C  CE2 . PHE A 1 336 ? -2.99300  -2.66300  4.76100   1.000 11.84115 ?  316 PHE A CE2 1 
ATOM   2338 C  CZ  . PHE A 1 336 ? -1.85800  -3.44300  4.57400   1.000 14.74917 ?  316 PHE A CZ  1 
ATOM   2339 N  N   . ASP A 1 337 ? -1.53400  0.89600   10.61000  1.000 21.76894 ?  317 ASP A N   1 
ATOM   2340 C  CA  . ASP A 1 337 ? -1.57400  2.13100   11.38000  1.000 19.43147 ?  317 ASP A CA  1 
ATOM   2341 C  C   . ASP A 1 337 ? -1.16200  3.31400   10.51600  1.000 23.63192 ?  317 ASP A C   1 
ATOM   2342 O  O   . ASP A 1 337 ? -0.16900  3.24900   9.78600   1.000 23.80965 ?  317 ASP A O   1 
ATOM   2343 C  CB  . ASP A 1 337 ? -0.65200  2.03200   12.59400  1.000 23.92439 ?  317 ASP A CB  1 
ATOM   2344 C  CG  . ASP A 1 337 ? -0.66700  3.29200   13.44400  1.000 35.66168 ?  317 ASP A CG  1 
ATOM   2345 O  OD1 . ASP A 1 337 ? -1.71600  3.59400   14.05400  1.000 40.98809 -1 317 ASP A OD1 1 
ATOM   2346 O  OD2 . ASP A 1 337 ? 0.37600   3.98000   13.50900  1.000 37.07229 ?  317 ASP A OD2 1 
ATOM   2347 N  N   . LEU A 1 338 ? -1.92500  4.40000   10.61500  1.000 18.89932 ?  318 LEU A N   1 
ATOM   2348 C  CA  . LEU A 1 338 ? -1.70400  5.60000   9.81700   1.000 25.21585 ?  318 LEU A CA  1 
ATOM   2349 C  C   . LEU A 1 338 ? -1.50300  5.22000   8.34800   1.000 26.27116 ?  318 LEU A C   1 
ATOM   2350 O  O   . LEU A 1 338 ? -0.43500  5.46300   7.77700   1.000 19.13511 ?  318 LEU A O   1 
ATOM   2351 C  CB  . LEU A 1 338 ? -0.51800  6.39600   10.34500  1.000 22.95652 ?  318 LEU A CB  1 
ATOM   2352 C  CG  . LEU A 1 338 ? -0.67900  6.87800   11.79100  1.000 31.29397 ?  318 LEU A CG  1 
ATOM   2353 C  CD1 . LEU A 1 338 ? 0.49900   7.74000   12.22600  1.000 28.81219 ?  318 LEU A CD1 1 
ATOM   2354 C  CD2 . LEU A 1 338 ? -1.98600  7.65200   11.94500  1.000 25.00954 ?  318 LEU A CD2 1 
ATOM   2355 N  N   . PRO A 1 339 ? -2.50900  4.60700   7.71700   1.000 17.44040 ?  319 PRO A N   1 
ATOM   2356 C  CA  . PRO A 1 339 ? -2.29100  4.00700   6.39200   1.000 19.06152 ?  319 PRO A CA  1 
ATOM   2357 C  C   . PRO A 1 339 ? -2.00400  5.01200   5.29500   1.000 22.94361 ?  319 PRO A C   1 
ATOM   2358 O  O   . PRO A 1 339 ? -1.41600  4.63400   4.27400   1.000 20.95414 ?  319 PRO A O   1 
ATOM   2359 C  CB  . PRO A 1 339 ? -3.60700  3.26600   6.13200   1.000 18.85532 ?  319 PRO A CB  1 
ATOM   2360 C  CG  . PRO A 1 339 ? -4.61800  4.07500   6.89600   1.000 23.46755 ?  319 PRO A CG  1 
ATOM   2361 C  CD  . PRO A 1 339 ? -3.91000  4.47000   8.15900   1.000 20.49380 ?  319 PRO A CD  1 
ATOM   2362 N  N   . ASP A 1 340 ? -2.39600  6.27100   5.46300   1.000 20.92633 ?  320 ASP A N   1 
ATOM   2363 C  CA  . ASP A 1 340 ? -2.17700  7.28800   4.44600   1.000 26.71771 ?  320 ASP A CA  1 
ATOM   2364 C  C   . ASP A 1 340 ? -0.85600  8.02100   4.63700   1.000 26.46260 ?  320 ASP A C   1 
ATOM   2365 O  O   . ASP A 1 340 ? -0.59700  9.00600   3.94100   1.000 27.91075 ?  320 ASP A O   1 
ATOM   2366 C  CB  . ASP A 1 340 ? -3.35000  8.26600   4.43700   1.000 27.96150 ?  320 ASP A CB  1 
ATOM   2367 C  CG  . ASP A 1 340 ? -4.68300  7.55800   4.30300   1.000 33.29567 ?  320 ASP A CG  1 
ATOM   2368 O  OD1 . ASP A 1 340 ? -4.76700  6.60400   3.49900   1.000 33.01687 ?  320 ASP A OD1 1 
ATOM   2369 O  OD2 . ASP A 1 340 ? -5.63800  7.93400   5.01400   1.000 39.08234 -1 320 ASP A OD2 1 
ATOM   2370 N  N   . THR A 1 341 ? -0.02200  7.55300   5.56000   1.000 24.36145 ?  321 THR A N   1 
ATOM   2371 C  CA  . THR A 1 341 ? 1.32500   8.05700   5.76900   1.000 25.86404 ?  321 THR A CA  1 
ATOM   2372 C  C   . THR A 1 341 ? 2.32000   7.00200   5.30400   1.000 27.43850 ?  321 THR A C   1 
ATOM   2373 O  O   . THR A 1 341 ? 2.10800   5.80300   5.51500   1.000 20.57071 ?  321 THR A O   1 
ATOM   2374 C  CB  . THR A 1 341 ? 1.54700   8.39700   7.24900   1.000 26.64008 ?  321 THR A CB  1 
ATOM   2375 O  OG1 . THR A 1 341 ? 0.62000   9.41600   7.64600   1.000 38.64823 ?  321 THR A OG1 1 
ATOM   2376 C  CG2 . THR A 1 341 ? 2.97000   8.87700   7.50700   1.000 37.89234 ?  321 THR A CG2 1 
ATOM   2377 N  N   . LEU A 1 342 ? 3.39000   7.45100   4.64800   1.000 24.47915 ?  322 LEU A N   1 
ATOM   2378 C  CA  . LEU A 1 342 ? 4.45800   6.56400   4.20400   1.000 22.40857 ?  322 LEU A CA  1 
ATOM   2379 C  C   . LEU A 1 342 ? 5.40000   6.27400   5.36600   1.000 19.28037 ?  322 LEU A C   1 
ATOM   2380 O  O   . LEU A 1 342 ? 5.96900   7.19800   5.95500   1.000 18.36463 ?  322 LEU A O   1 
ATOM   2381 C  CB  . LEU A 1 342 ? 5.22000   7.19200   3.03800   1.000 22.99910 ?  322 LEU A CB  1 
ATOM   2382 C  CG  . LEU A 1 342 ? 6.29100   6.32500   2.37900   1.000 19.40214 ?  322 LEU A CG  1 
ATOM   2383 C  CD1 . LEU A 1 342 ? 5.67000   5.33200   1.41800   1.000 21.53462 ?  322 LEU A CD1 1 
ATOM   2384 C  CD2 . LEU A 1 342 ? 7.33400   7.19500   1.66700   1.000 17.83434 ?  322 LEU A CD2 1 
ATOM   2385 N  N   . ASP A 1 343 ? 5.55800   4.99400   5.69700   1.000 18.11617 ?  323 ASP A N   1 
ATOM   2386 C  CA  . ASP A 1 343 ? 6.45300   4.53800   6.76000   1.000 22.54760 ?  323 ASP A CA  1 
ATOM   2387 C  C   . ASP A 1 343 ? 7.26700   3.37900   6.19700   1.000 17.13525 ?  323 ASP A C   1 
ATOM   2388 O  O   . ASP A 1 343 ? 6.80300   2.23500   6.18500   1.000 20.87347 ?  323 ASP A O   1 
ATOM   2389 C  CB  . ASP A 1 343 ? 5.67600   4.11500   8.00400   1.000 21.37561 ?  323 ASP A CB  1 
ATOM   2390 C  CG  . ASP A 1 343 ? 6.58200   3.64100   9.12000   1.000 22.23714 ?  323 ASP A CG  1 
ATOM   2391 O  OD1 . ASP A 1 343 ? 7.81100   3.59900   8.91200   1.000 19.45308 -1 323 ASP A OD1 1 
ATOM   2392 O  OD2 . ASP A 1 343 ? 6.06700   3.29800   10.20300  1.000 25.51316 -1 323 ASP A OD2 1 
ATOM   2393 N  N   . LEU A 1 344 ? 8.48500   3.67300   5.73400   1.000 17.65628 ?  324 LEU A N   1 
ATOM   2394 C  CA  . LEU A 1 344 ? 9.28300   2.66800   5.04200   1.000 14.57717 ?  324 LEU A CA  1 
ATOM   2395 C  C   . LEU A 1 344 ? 9.72300   1.52800   5.95400   1.000 19.36656 ?  324 LEU A C   1 
ATOM   2396 O  O   . LEU A 1 344 ? 10.10200  0.46800   5.44800   1.000 19.80999 ?  324 LEU A O   1 
ATOM   2397 C  CB  . LEU A 1 344 ? 10.49500  3.33400   4.38900   1.000 15.29336 ?  324 LEU A CB  1 
ATOM   2398 C  CG  . LEU A 1 344 ? 10.15400  4.41700   3.36100   1.000 13.95029 ?  324 LEU A CG  1 
ATOM   2399 C  CD1 . LEU A 1 344 ? 11.41500  5.03000   2.76500   1.000 24.48067 ?  324 LEU A CD1 1 
ATOM   2400 C  CD2 . LEU A 1 344 ? 9.25400   3.85800   2.24700   1.000 15.68787 ?  324 LEU A CD2 1 
ATOM   2401 N  N   . ARG A 1 345 ? 9.67300   1.71200   7.27600   1.000 14.06630 ?  325 ARG A N   1 
ATOM   2402 C  CA  . ARG A 1 345 ? 9.96800   0.65100   8.22900   1.000 16.52070 ?  325 ARG A CA  1 
ATOM   2403 C  C   . ARG A 1 345 ? 8.71000   -0.04100  8.74100   1.000 20.12351 ?  325 ARG A C   1 
ATOM   2404 O  O   . ARG A 1 345 ? 8.75500   -0.71000  9.77700   1.000 18.71217 ?  325 ARG A O   1 
ATOM   2405 C  CB  . ARG A 1 345 ? 10.78600  1.20000   9.40000   1.000 18.60297 ?  325 ARG A CB  1 
ATOM   2406 C  CG  . ARG A 1 345 ? 12.00000  2.00100   8.95800   1.000 21.44632 ?  325 ARG A CG  1 
ATOM   2407 C  CD  . ARG A 1 345 ? 12.94100  2.28800   10.11100  1.000 24.68577 ?  325 ARG A CD  1 
ATOM   2408 N  NE  . ARG A 1 345 ? 14.24700  2.71900   9.63100   1.000 24.62112 ?  325 ARG A NE  1 
ATOM   2409 C  CZ  . ARG A 1 345 ? 15.25600  1.90000   9.37200   1.000 30.81799 ?  325 ARG A CZ  1 
ATOM   2410 N  NH1 . ARG A 1 345 ? 15.15900  0.59700   9.57900   1.000 27.19786 ?  325 ARG A NH1 1 
ATOM   2411 N  NH2 . ARG A 1 345 ? 16.39500  2.40200   8.90500   1.000 25.71782 ?  325 ARG A NH2 1 
ATOM   2412 N  N   . ARG A 1 346 ? 7.59000   0.10900   8.03600   1.000 22.29263 ?  326 ARG A N   1 
ATOM   2413 C  CA  . ARG A 1 346 ? 6.34900   -0.54200  8.43900   1.000 21.62938 ?  326 ARG A CA  1 
ATOM   2414 C  C   . ARG A 1 346 ? 6.52000   -2.05600  8.47300   1.000 21.21942 ?  326 ARG A C   1 
ATOM   2415 O  O   . ARG A 1 346 ? 7.01100   -2.65800  7.51500   1.000 23.75828 ?  326 ARG A O   1 
ATOM   2416 C  CB  . ARG A 1 346 ? 5.22600   -0.16900  7.47000   1.000 20.31734 ?  326 ARG A CB  1 
ATOM   2417 C  CG  . ARG A 1 346 ? 3.92100   -0.84300  7.78200   1.000 18.22036 ?  326 ARG A CG  1 
ATOM   2418 C  CD  . ARG A 1 346 ? 2.80200   -0.36400  6.86000   1.000 18.18397 ?  326 ARG A CD  1 
ATOM   2419 N  NE  . ARG A 1 346 ? 2.77300   1.08600   6.69200   1.000 13.90937 ?  326 ARG A NE  1 
ATOM   2420 C  CZ  . ARG A 1 346 ? 1.95900   1.89600   7.35700   1.000 18.01004 ?  326 ARG A CZ  1 
ATOM   2421 N  NH1 . ARG A 1 346 ? 1.17800   1.44800   8.32700   1.000 18.09082 ?  326 ARG A NH1 1 
ATOM   2422 N  NH2 . ARG A 1 346 ? 1.93300   3.18900   7.04900   1.000 19.00967 ?  326 ARG A NH2 1 
ATOM   2423 N  N   . ASP A 1 347 ? 6.08800   -2.67500  9.57000   1.000 24.52284 ?  327 ASP A N   1 
ATOM   2424 C  CA  . ASP A 1 347 ? 6.27200   -4.10900  9.75600   1.000 27.66143 ?  327 ASP A CA  1 
ATOM   2425 C  C   . ASP A 1 347 ? 5.29600   -4.62500  10.80800  1.000 27.70082 ?  327 ASP A C   1 
ATOM   2426 O  O   . ASP A 1 347 ? 5.29200   -4.12900  11.94100  1.000 36.68055 ?  327 ASP A O   1 
ATOM   2427 C  CB  . ASP A 1 347 ? 7.71500   -4.40600  10.17200  1.000 28.14879 ?  327 ASP A CB  1 
ATOM   2428 C  CG  . ASP A 1 347 ? 8.13800   -5.82800  9.85400   1.000 36.83477 ?  327 ASP A CG  1 
ATOM   2429 O  OD1 . ASP A 1 347 ? 7.64200   -6.39500  8.85800   1.000 36.72909 ?  327 ASP A OD1 1 
ATOM   2430 O  OD2 . ASP A 1 347 ? 8.97300   -6.37800  10.60300  1.000 47.99995 -1 327 ASP A OD2 1 
ATOM   2431 N  N   . PRO A 1 348 ? 4.44600   -5.61100  10.48100  1.000 24.36367 ?  328 PRO A N   1 
ATOM   2432 C  CA  . PRO A 1 348 ? 4.31500   -6.30400  9.19100   1.000 21.82282 ?  328 PRO A CA  1 
ATOM   2433 C  C   . PRO A 1 348 ? 3.71000   -5.41100  8.11400   1.000 16.51842 ?  328 PRO A C   1 
ATOM   2434 O  O   . PRO A 1 348 ? 3.28700   -4.29300  8.38300   1.000 18.22932 ?  328 PRO A O   1 
ATOM   2435 C  CB  . PRO A 1 348 ? 3.40700   -7.49200  9.54000   1.000 22.13778 ?  328 PRO A CB  1 
ATOM   2436 C  CG  . PRO A 1 348 ? 2.53400   -6.95200  10.63100  1.000 22.44585 ?  328 PRO A CG  1 
ATOM   2437 C  CD  . PRO A 1 348 ? 3.46900   -6.11400  11.46400  1.000 24.54602 ?  328 PRO A CD  1 
ATOM   2438 N  N   . ASN A 1 349 ? 3.68000   -5.87400  6.87100   1.000 18.06517 ?  329 ASN A N   1 
ATOM   2439 C  CA  . ASN A 1 349 ? 3.11900   -5.10700  5.75900   1.000 13.80715 ?  329 ASN A CA  1 
ATOM   2440 C  C   . ASN A 1 349 ? 2.42600   -6.09400  4.83500   1.000 15.79887 ?  329 ASN A C   1 
ATOM   2441 O  O   . ASN A 1 349 ? 2.97300   -6.50000  3.80200   1.000 14.37678 ?  329 ASN A O   1 
ATOM   2442 C  CB  . ASN A 1 349 ? 4.20500   -4.30400  5.03400   1.000 17.54319 ?  329 ASN A CB  1 
ATOM   2443 C  CG  . ASN A 1 349 ? 3.64000   -3.38300  3.96800   1.000 20.90120 ?  329 ASN A CG  1 
ATOM   2444 O  OD1 . ASN A 1 349 ? 2.42900   -3.32900  3.74700   1.000 17.05702 ?  329 ASN A OD1 1 
ATOM   2445 N  ND2 . ASN A 1 349 ? 4.51600   -2.63400  3.31600   1.000 18.93710 ?  329 ASN A ND2 1 
ATOM   2446 N  N   . PRO A 1 350 ? 1.20800   -6.52900  5.20000   1.000 14.13265 ?  330 PRO A N   1 
ATOM   2447 C  CA  . PRO A 1 350 ? 0.45800   -7.51600  4.41300   1.000 16.44082 ?  330 PRO A CA  1 
ATOM   2448 C  C   . PRO A 1 350 ? -0.35700  -6.90500  3.27600   1.000 16.19262 ?  330 PRO A C   1 
ATOM   2449 O  O   . PRO A 1 350 ? -1.55300  -7.16400  3.13400   1.000 15.86145 ?  330 PRO A O   1 
ATOM   2450 C  CB  . PRO A 1 350 ? -0.43700  -8.17000  5.47000   1.000 14.54199 ?  330 PRO A CB  1 
ATOM   2451 C  CG  . PRO A 1 350 ? -0.75800  -7.04000  6.39300   1.000 14.52007 ?  330 PRO A CG  1 
ATOM   2452 C  CD  . PRO A 1 350 ? 0.51300   -6.19900  6.46000   1.000 17.98094 ?  330 PRO A CD  1 
ATOM   2453 N  N   . HIS A 1 351 ? 0.30300   -6.09300  2.45400   1.000 14.80481 ?  331 HIS A N   1 
ATOM   2454 C  CA  . HIS A 1 351 ? -0.37300  -5.44400  1.34100   1.000 14.77225 ?  331 HIS A CA  1 
ATOM   2455 C  C   . HIS A 1 351 ? -0.78100  -6.46200  0.27900   1.000 12.80081 ?  331 HIS A C   1 
ATOM   2456 O  O   . HIS A 1 351 ? -0.13800  -7.49900  0.09300   1.000 11.03407 ?  331 HIS A O   1 
ATOM   2457 C  CB  . HIS A 1 351 ? 0.51900   -4.34600  0.76000   1.000 13.26910 ?  331 HIS A CB  1 
ATOM   2458 C  CG  . HIS A 1 351 ? 1.69000   -4.85300  -0.02300  1.000 14.81940 ?  331 HIS A CG  1 
ATOM   2459 N  ND1 . HIS A 1 351 ? 1.59100   -5.25900  -1.33600  1.000 15.68870 ?  331 HIS A ND1 1 
ATOM   2460 C  CD2 . HIS A 1 351 ? 2.98500   -5.03100  0.33000   1.000 15.73012 ?  331 HIS A CD2 1 
ATOM   2461 C  CE1 . HIS A 1 351 ? 2.77700   -5.65800  -1.76100  1.000 15.55420 ?  331 HIS A CE1 1 
ATOM   2462 N  NE2 . HIS A 1 351 ? 3.64000   -5.53300  -0.76800  1.000 15.76963 ?  331 HIS A NE2 1 
ATOM   2463 N  N   . LEU A 1 352 ? -1.89500  -6.16700  -0.39700  1.000 8.93940  ?  332 LEU A N   1 
ATOM   2464 C  CA  . LEU A 1 352 ? -2.53700  -7.08400  -1.32800  1.000 14.42102 ?  332 LEU A CA  1 
ATOM   2465 C  C   . LEU A 1 352 ? -2.25600  -6.73400  -2.78200  1.000 15.78006 ?  332 LEU A C   1 
ATOM   2466 O  O   . LEU A 1 352 ? -3.00500  -7.15400  -3.67000  1.000 12.07222 ?  332 LEU A O   1 
ATOM   2467 C  CB  . LEU A 1 352 ? -4.04900  -7.10000  -1.07300  1.000 10.52239 ?  332 LEU A CB  1 
ATOM   2468 C  CG  . LEU A 1 352 ? -4.51800  -7.61700  0.29300   1.000 17.04989 ?  332 LEU A CG  1 
ATOM   2469 C  CD1 . LEU A 1 352 ? -6.04300  -7.61500  0.39600   1.000 12.58641 ?  332 LEU A CD1 1 
ATOM   2470 C  CD2 . LEU A 1 352 ? -3.96500  -9.00800  0.55600   1.000 14.14616 ?  332 LEU A CD2 1 
ATOM   2471 N  N   . SER A 1 353 ? -1.17200  -5.99800  -3.04400  1.000 15.80294 ?  333 SER A N   1 
ATOM   2472 C  CA  . SER A 1 353 ? -0.94900  -5.42400  -4.36600  1.000 14.74166 ?  333 SER A CA  1 
ATOM   2473 C  C   . SER A 1 353 ? -0.76500  -6.49300  -5.43800  1.000 18.87284 ?  333 SER A C   1 
ATOM   2474 O  O   . SER A 1 353 ? -1.05000  -6.24600  -6.61500  1.000 20.65718 ?  333 SER A O   1 
ATOM   2475 C  CB  . SER A 1 353 ? 0.27600   -4.51000  -4.32900  1.000 12.18936 ?  333 SER A CB  1 
ATOM   2476 O  OG  . SER A 1 353 ? 0.18900   -3.58800  -3.25700  1.000 12.90828 ?  333 SER A OG  1 
ATOM   2477 N  N   . TYR A 1 354 ? -0.28200  -7.67600  -5.06400  1.000 15.75127 ?  334 TYR A N   1 
ATOM   2478 C  CA  . TYR A 1 354 ? -0.02700  -8.74300  -6.02200  1.000 12.09469 ?  334 TYR A CA  1 
ATOM   2479 C  C   . TYR A 1 354 ? -1.09600  -9.82100  -5.98400  1.000 12.89614 ?  334 TYR A C   1 
ATOM   2480 O  O   . TYR A 1 354 ? -0.84700  -10.95400 -6.41800  1.000 15.37137 ?  334 TYR A O   1 
ATOM   2481 C  CB  . TYR A 1 354 ? 1.35400   -9.34700  -5.77600  1.000 12.72246 ?  334 TYR A CB  1 
ATOM   2482 C  CG  . TYR A 1 354 ? 2.47700   -8.37400  -6.05000  1.000 13.30919 ?  334 TYR A CG  1 
ATOM   2483 C  CD1 . TYR A 1 354 ? 2.81400   -8.02000  -7.35200  1.000 14.84161 ?  334 TYR A CD1 1 
ATOM   2484 C  CD2 . TYR A 1 354 ? 3.19300   -7.80000  -5.01100  1.000 16.63380 ?  334 TYR A CD2 1 
ATOM   2485 C  CE1 . TYR A 1 354 ? 3.84900   -7.12800  -7.61200  1.000 16.61963 ?  334 TYR A CE1 1 
ATOM   2486 C  CE2 . TYR A 1 354 ? 4.23100   -6.90800  -5.26000  1.000 12.89399 ?  334 TYR A CE2 1 
ATOM   2487 C  CZ  . TYR A 1 354 ? 4.55000   -6.57300  -6.56000  1.000 17.50387 ?  334 TYR A CZ  1 
ATOM   2488 O  OH  . TYR A 1 354 ? 5.57700   -5.67600  -6.80400  1.000 18.61615 ?  334 TYR A OH  1 
ATOM   2489 N  N   . GLY A 1 355 ? -2.27400  -9.49700  -5.47000  1.000 13.17762 ?  335 GLY A N   1 
ATOM   2490 C  CA  . GLY A 1 355 ? -3.36200  -10.44300 -5.44400  1.000 16.83933 ?  335 GLY A CA  1 
ATOM   2491 C  C   . GLY A 1 355 ? -3.22800  -11.47000 -4.33800  1.000 16.93250 ?  335 GLY A C   1 
ATOM   2492 O  O   . GLY A 1 355 ? -2.36700  -11.39800 -3.45000  1.000 17.37731 ?  335 GLY A O   1 
ATOM   2493 N  N   . HIS A 1 356 ? -4.10300  -12.46700 -4.42000  1.000 12.72681 ?  336 HIS A N   1 
ATOM   2494 C  CA  . HIS A 1 356 ? -4.22300  -13.49500 -3.40000  1.000 14.18779 ?  336 HIS A CA  1 
ATOM   2495 C  C   . HIS A 1 356 ? -5.09700  -14.59800 -3.96900  1.000 14.72667 ?  336 HIS A C   1 
ATOM   2496 O  O   . HIS A 1 356 ? -6.08200  -14.31300 -4.65000  1.000 15.82901 ?  336 HIS A O   1 
ATOM   2497 C  CB  . HIS A 1 356 ? -4.83400  -12.91900 -2.11300  1.000 15.65361 ?  336 HIS A CB  1 
ATOM   2498 C  CG  . HIS A 1 356 ? -5.14300  -13.95000 -1.07200  1.000 17.04603 ?  336 HIS A CG  1 
ATOM   2499 N  ND1 . HIS A 1 356 ? -6.41300  -14.15100 -0.57400  1.000 24.23576 ?  336 HIS A ND1 1 
ATOM   2500 C  CD2 . HIS A 1 356 ? -4.34100  -14.82300 -0.42000  1.000 17.14894 ?  336 HIS A CD2 1 
ATOM   2501 C  CE1 . HIS A 1 356 ? -6.38200  -15.10800 0.33500   1.000 19.23591 ?  336 HIS A CE1 1 
ATOM   2502 N  NE2 . HIS A 1 356 ? -5.13600  -15.53600 0.44500   1.000 27.94118 ?  336 HIS A NE2 1 
ATOM   2503 N  N   . GLY A 1 357 ? -4.72400  -15.84200 -3.71300  1.000 17.24499 ?  337 GLY A N   1 
ATOM   2504 C  CA  . GLY A 1 357 ? -5.44200  -16.96000 -4.28300  1.000 14.68898 ?  337 GLY A CA  1 
ATOM   2505 C  C   . GLY A 1 357 ? -4.82100  -17.43200 -5.58200  1.000 18.96964 ?  337 GLY A C   1 
ATOM   2506 O  O   . GLY A 1 357 ? -3.64700  -17.19000 -5.87500  1.000 15.27318 ?  337 GLY A O   1 
ATOM   2507 N  N   . ILE A 1 358 ? -5.64600  -18.10800 -6.38800  1.000 14.84230 ?  338 ILE A N   1 
ATOM   2508 C  CA  . ILE A 1 358 ? -5.12900  -18.80200 -7.56200  1.000 17.64239 ?  338 ILE A CA  1 
ATOM   2509 C  C   . ILE A 1 358 ? -4.67200  -17.85200 -8.66100  1.000 16.61730 ?  338 ILE A C   1 
ATOM   2510 O  O   . ILE A 1 358 ? -3.86200  -18.24800 -9.50700  1.000 14.60698 ?  338 ILE A O   1 
ATOM   2511 C  CB  . ILE A 1 358 ? -6.17700  -19.78800 -8.11000  1.000 18.60804 ?  338 ILE A CB  1 
ATOM   2512 C  CG1 . ILE A 1 358 ? -7.45700  -19.04700 -8.51100  1.000 16.84181 ?  338 ILE A CG1 1 
ATOM   2513 C  CG2 . ILE A 1 358 ? -6.45800  -20.88800 -7.09500  1.000 22.01792 ?  338 ILE A CG2 1 
ATOM   2514 C  CD1 . ILE A 1 358 ? -8.35500  -19.84700 -9.41600  1.000 17.89211 ?  338 ILE A CD1 1 
ATOM   2515 N  N   . HIS A 1 359 ? -5.15100  -16.60800 -8.67500  1.000 11.99298 ?  339 HIS A N   1 
ATOM   2516 C  CA  . HIS A 1 359 ? -4.77300  -15.65600 -9.71000  1.000 10.84962 ?  339 HIS A CA  1 
ATOM   2517 C  C   . HIS A 1 359 ? -3.63900  -14.73200 -9.28000  1.000 17.29121 ?  339 HIS A C   1 
ATOM   2518 O  O   . HIS A 1 359 ? -3.31300  -13.79500 -10.01200 1.000 13.54990 ?  339 HIS A O   1 
ATOM   2519 C  CB  . HIS A 1 359 ? -5.98200  -14.82200 -10.13100 1.000 12.36208 ?  339 HIS A CB  1 
ATOM   2520 C  CG  . HIS A 1 359 ? -7.02300  -15.60400 -10.86700 1.000 15.43722 ?  339 HIS A CG  1 
ATOM   2521 N  ND1 . HIS A 1 359 ? -6.84200  -16.05300 -12.15900 1.000 13.33956 ?  339 HIS A ND1 1 
ATOM   2522 C  CD2 . HIS A 1 359 ? -8.25100  -16.03000 -10.48800 1.000 12.87197 ?  339 HIS A CD2 1 
ATOM   2523 C  CE1 . HIS A 1 359 ? -7.92000  -16.71300 -12.54600 1.000 11.81745 ?  339 HIS A CE1 1 
ATOM   2524 N  NE2 . HIS A 1 359 ? -8.78700  -16.71800 -11.54900 1.000 13.50687 ?  339 HIS A NE2 1 
ATOM   2525 N  N   . ARG A 1 360 ? -3.03600  -14.96900 -8.11500  1.000 13.65356 ?  340 ARG A N   1 
ATOM   2526 C  CA  . ARG A 1 360 ? -2.00600  -14.06100 -7.61900  1.000 16.35398 ?  340 ARG A CA  1 
ATOM   2527 C  C   . ARG A 1 360 ? -0.86600  -13.93200 -8.62400  1.000 11.22196 ?  340 ARG A C   1 
ATOM   2528 O  O   . ARG A 1 360 ? -0.57000  -14.85300 -9.39400  1.000 16.33911 ?  340 ARG A O   1 
ATOM   2529 C  CB  . ARG A 1 360 ? -1.47800  -14.53200 -6.26400  1.000 20.62956 ?  340 ARG A CB  1 
ATOM   2530 C  CG  . ARG A 1 360 ? -0.63900  -15.79700 -6.30300  1.000 14.94857 ?  340 ARG A CG  1 
ATOM   2531 C  CD  . ARG A 1 360 ? -0.29600  -16.24200 -4.88000  1.000 21.42207 ?  340 ARG A CD  1 
ATOM   2532 N  NE  . ARG A 1 360 ? 0.36200   -17.54500 -4.84200  1.000 21.96787 ?  340 ARG A NE  1 
ATOM   2533 C  CZ  . ARG A 1 360 ? -0.26700  -18.70900 -4.93600  1.000 25.22045 ?  340 ARG A CZ  1 
ATOM   2534 N  NH1 . ARG A 1 360 ? -1.58000  -18.77700 -5.08700  1.000 24.02185 ?  340 ARG A NH1 1 
ATOM   2535 N  NH2 . ARG A 1 360 ? 0.44100   -19.83400 -4.88800  1.000 21.78055 ?  340 ARG A NH2 1 
ATOM   2536 N  N   . SER A 1 361 ? -0.23900  -12.76300 -8.61100  1.000 13.52379 ?  341 SER A N   1 
ATOM   2537 C  CA  . SER A 1 361 ? 0.62000   -12.34100 -9.70500  1.000 20.38958 ?  341 SER A CA  1 
ATOM   2538 C  C   . SER A 1 361 ? 1.77300   -13.31000 -9.90200  1.000 15.59272 ?  341 SER A C   1 
ATOM   2539 O  O   . SER A 1 361 ? 2.32400   -13.84400 -8.93700  1.000 17.20336 ?  341 SER A O   1 
ATOM   2540 C  CB  . SER A 1 361 ? 1.16900   -10.94200 -9.42200  1.000 17.73383 ?  341 SER A CB  1 
ATOM   2541 O  OG  . SER A 1 361 ? 2.06300   -10.52400 -10.43700 1.000 22.73239 ?  341 SER A OG  1 
ATOM   2542 N  N   . PHE A 1 362 ? 2.11100   -13.55600 -11.17200 1.000 15.60141 ?  342 PHE A N   1 
ATOM   2543 C  CA  . PHE A 1 362 ? 3.37000   -14.22200 -11.50400 1.000 23.83232 ?  342 PHE A CA  1 
ATOM   2544 C  C   . PHE A 1 362 ? 4.56900   -13.30000 -11.33900 1.000 25.86461 ?  342 PHE A C   1 
ATOM   2545 O  O   . PHE A 1 362 ? 5.71000   -13.78100 -11.32600 1.000 30.87627 ?  342 PHE A O   1 
ATOM   2546 C  CB  . PHE A 1 362 ? 3.34800   -14.73000 -12.95100 1.000 20.00366 ?  342 PHE A CB  1 
ATOM   2547 C  CG  . PHE A 1 362 ? 2.85800   -16.14700 -13.11000 1.000 25.44900 ?  342 PHE A CG  1 
ATOM   2548 C  CD1 . PHE A 1 362 ? 3.61900   -17.21900 -12.66900 1.000 23.71108 ?  342 PHE A CD1 1 
ATOM   2549 C  CD2 . PHE A 1 362 ? 1.64400   -16.40700 -13.72800 1.000 22.79889 ?  342 PHE A CD2 1 
ATOM   2550 C  CE1 . PHE A 1 362 ? 3.16800   -18.52400 -12.83200 1.000 27.59789 ?  342 PHE A CE1 1 
ATOM   2551 C  CE2 . PHE A 1 362 ? 1.18900   -17.70800 -13.89300 1.000 20.81456 ?  342 PHE A CE2 1 
ATOM   2552 C  CZ  . PHE A 1 362 ? 1.95000   -18.76600 -13.44500 1.000 25.17086 ?  342 PHE A CZ  1 
ATOM   2553 N  N   . GLY A 1 363 ? 4.34600   -11.99200 -11.23000 1.000 21.16912 ?  343 GLY A N   1 
ATOM   2554 C  CA  . GLY A 1 363 ? 5.44400   -11.05600 -11.39100 1.000 23.15905 ?  343 GLY A CA  1 
ATOM   2555 C  C   . GLY A 1 363 ? 5.88400   -10.34600 -10.13400 1.000 25.60166 ?  343 GLY A C   1 
ATOM   2556 O  O   . GLY A 1 363 ? 6.56700   -9.31500  -10.21500 1.000 21.49967 ?  343 GLY A O   1 
ATOM   2557 N  N   . SER A 1 364 ? 5.47500   -10.86300 -8.97400  1.000 16.44339 ?  344 SER A N   1 
ATOM   2558 C  CA  . SER A 1 364 ? 5.82500   -10.20100 -7.69200  1.000 17.95546 ?  344 SER A CA  1 
ATOM   2559 C  C   . SER A 1 364 ? 7.33800   -9.97300  -7.63600  1.000 24.81227 ?  344 SER A C   1 
ATOM   2560 O  O   . SER A 1 364 ? 7.75300   -8.80900  -7.47300  1.000 24.42683 ?  344 SER A O   1 
ATOM   2561 C  CB  . SER A 1 364 ? 5.35100   -11.01100 -6.51800  1.000 23.82465 ?  344 SER A CB  1 
ATOM   2562 O  OG  . SER A 1 364 ? 5.87900   -12.32800 -6.57200  1.000 37.69940 ?  344 SER A OG  1 
ATOM   2563 N  N   . ARG A 1 365 ? 8.12400   -11.04200 -7.78700  1.000 18.69680 ?  345 ARG A N   1 
ATOM   2564 C  CA  . ARG A 1 365 ? 9.60600   -10.93600 -7.69300  1.000 21.72252 ?  345 ARG A CA  1 
ATOM   2565 C  C   . ARG A 1 365 ? 10.13800  -10.01900 -8.79900  1.000 21.00776 ?  345 ARG A C   1 
ATOM   2566 O  O   . ARG A 1 365 ? 10.90300  -9.09400  -8.47700  1.000 19.44305 ?  345 ARG A O   1 
ATOM   2567 C  CB  . ARG A 1 365 ? 10.23400  -12.32900 -7.78600  1.000 22.40710 ?  345 ARG A CB  1 
ATOM   2568 C  CG  . ARG A 1 365 ? 9.46100   -13.39800 -7.02700  1.000 31.20025 ?  345 ARG A CG  1 
ATOM   2569 C  CD  . ARG A 1 365 ? 10.22300  -14.70200 -6.89800  1.000 39.78425 ?  345 ARG A CD  1 
ATOM   2570 N  N   . LEU A 1 366 ? 9.76600   -10.28700 -10.05300 1.000 15.53761 ?  346 LEU A N   1 
ATOM   2571 C  CA  . LEU A 1 366 ? 10.26200  -9.46700  -11.19000 1.000 17.43999 ?  346 LEU A CA  1 
ATOM   2572 C  C   . LEU A 1 366 ? 10.04700  -7.98700  -10.86100 1.000 16.35463 ?  346 LEU A C   1 
ATOM   2573 O  O   . LEU A 1 366 ? 11.01700  -7.21200  -10.96200 1.000 14.56643 ?  346 LEU A O   1 
ATOM   2574 C  CB  . LEU A 1 366 ? 9.50600   -9.87100  -12.45800 1.000 13.87346 ?  346 LEU A CB  1 
ATOM   2575 C  CG  . LEU A 1 366 ? 10.12300  -9.39200  -13.77100 1.000 15.31442 ?  346 LEU A CG  1 
ATOM   2576 C  CD1 . LEU A 1 366 ? 11.63600  -9.54900  -13.75100 1.000 14.34152 ?  346 LEU A CD1 1 
ATOM   2577 C  CD2 . LEU A 1 366 ? 9.52600   -10.14200 -14.95200 1.000 18.83299 ?  346 LEU A CD2 1 
ATOM   2578 N  N   . SER A 1 367 ? 8.82400   -7.61800  -10.47600 1.000 16.99065 ?  347 SER A N   1 
ATOM   2579 C  CA  . SER A 1 367 ? 8.53300   -6.23600  -10.11800 1.000 14.34776 ?  347 SER A CA  1 
ATOM   2580 C  C   . SER A 1 367 ? 9.45300   -5.75400  -9.00100  1.000 15.33645 ?  347 SER A C   1 
ATOM   2581 O  O   . SER A 1 367 ? 10.00400  -4.64800  -9.06200  1.000 12.98994 ?  347 SER A O   1 
ATOM   2582 C  CB  . SER A 1 367 ? 7.06200   -6.11600  -9.70900  1.000 16.09766 ?  347 SER A CB  1 
ATOM   2583 O  OG  . SER A 1 367 ? 6.83100   -4.90100  -9.02700  1.000 24.99174 ?  347 SER A OG  1 
ATOM   2584 N  N   . GLN A 1 368 ? 9.63900   -6.58400  -7.97300  1.000 14.44990 ?  348 GLN A N   1 
ATOM   2585 C  CA  . GLN A 1 368 ? 10.49700  -6.20100  -6.85900  1.000 17.34325 ?  348 GLN A CA  1 
ATOM   2586 C  C   . GLN A 1 368 ? 11.93700  -5.99000  -7.32300  1.000 13.37609 ?  348 GLN A C   1 
ATOM   2587 O  O   . GLN A 1 368 ? 12.63100  -5.09400  -6.83100  1.000 16.36411 ?  348 GLN A O   1 
ATOM   2588 C  CB  . GLN A 1 368 ? 10.41100  -7.26400  -5.76200  1.000 16.64818 ?  348 GLN A CB  1 
ATOM   2589 C  CG  . GLN A 1 368 ? 9.12500   -7.14600  -4.93000  1.000 25.85848 ?  348 GLN A CG  1 
ATOM   2590 C  CD  . GLN A 1 368 ? 8.66700   -8.47100  -4.32800  1.000 29.83950 ?  348 GLN A CD  1 
ATOM   2591 O  OE1 . GLN A 1 368 ? 9.29900   -9.51000  -4.52300  1.000 28.82131 ?  348 GLN A OE1 1 
ATOM   2592 N  NE2 . GLN A 1 368 ? 7.54600   -8.43800  -3.60900  1.000 23.73796 ?  348 GLN A NE2 1 
ATOM   2593 N  N   . ALA A 1 369 ? 12.39100  -6.78600  -8.29500  1.000 14.36367 ?  349 ALA A N   1 
ATOM   2594 C  CA  . ALA A 1 369 ? 13.76100  -6.64800  -8.79000  1.000 15.32546 ?  349 ALA A CA  1 
ATOM   2595 C  C   . ALA A 1 369 ? 13.92100  -5.39800  -9.64800  1.000 15.00106 ?  349 ALA A C   1 
ATOM   2596 O  O   . ALA A 1 369 ? 14.90600  -4.66100  -9.51400  1.000 17.82429 ?  349 ALA A O   1 
ATOM   2597 C  CB  . ALA A 1 369 ? 14.16100  -7.89400  -9.57900  1.000 14.85182 ?  349 ALA A CB  1 
ATOM   2598 N  N   . GLU A 1 370 ? 12.97100  -5.14900  -10.55200 1.000 14.66042 ?  350 GLU A N   1 
ATOM   2599 C  CA  . GLU A 1 370 ? 13.01700  -3.92500  -11.34700 1.000 15.19627 ?  350 GLU A CA  1 
ATOM   2600 C  C   . GLU A 1 370 ? 12.89000  -2.68300  -10.47300 1.000 16.39138 ?  350 GLU A C   1 
ATOM   2601 O  O   . GLU A 1 370 ? 13.60200  -1.69300  -10.68500 1.000 16.65668 ?  350 GLU A O   1 
ATOM   2602 C  CB  . GLU A 1 370 ? 11.92500  -3.95100  -12.42200 1.000 12.34480 ?  350 GLU A CB  1 
ATOM   2603 C  CG  . GLU A 1 370 ? 12.08600  -5.08400  -13.42400 1.000 19.52260 ?  350 GLU A CG  1 
ATOM   2604 C  CD  . GLU A 1 370 ? 11.31400  -4.82400  -14.70200 1.000 24.41325 ?  350 GLU A CD  1 
ATOM   2605 O  OE1 . GLU A 1 370 ? 11.45200  -3.71400  -15.25700 1.000 20.89351 ?  350 GLU A OE1 1 
ATOM   2606 O  OE2 . GLU A 1 370 ? 10.59500  -5.73600  -15.17000 1.000 21.15655 -1 350 GLU A OE2 1 
ATOM   2607 N  N   . ALA A 1 371 ? 11.98500  -2.70900  -9.48800  1.000 14.43947 ?  351 ALA A N   1 
ATOM   2608 C  CA  . ALA A 1 371 ? 11.87500  -1.58400  -8.56000  1.000 14.24868 ?  351 ALA A CA  1 
ATOM   2609 C  C   . ALA A 1 371 ? 13.18400  -1.35000  -7.81100  1.000 14.55190 ?  351 ALA A C   1 
ATOM   2610 O  O   . ALA A 1 371 ? 13.63000  -0.20500  -7.66400  1.000 15.22327 ?  351 ALA A O   1 
ATOM   2611 C  CB  . ALA A 1 371 ? 10.73000  -1.82500  -7.57600  1.000 16.11837 ?  351 ALA A CB  1 
ATOM   2612 N  N   . ALA A 1 372 ? 13.81600  -2.42200  -7.33200  1.000 13.44844 ?  352 ALA A N   1 
ATOM   2613 C  CA  . ALA A 1 372 ? 15.06400  -2.26400  -6.58900  1.000 16.00617 ?  352 ALA A CA  1 
ATOM   2614 C  C   . ALA A 1 372 ? 16.16500  -1.70000  -7.47400  1.000 17.65614 ?  352 ALA A C   1 
ATOM   2615 O  O   . ALA A 1 372 ? 16.91100  -0.81000  -7.05100  1.000 20.41166 ?  352 ALA A O   1 
ATOM   2616 C  CB  . ALA A 1 372 ? 15.48500  -3.60100  -5.97800  1.000 17.32474 ?  352 ALA A CB  1 
ATOM   2617 N  N   . ALA A 1 373 ? 16.27000  -2.18700  -8.71300  1.000 17.13870 ?  353 ALA A N   1 
ATOM   2618 C  CA  . ALA A 1 373 ? 17.24600  -1.62900  -9.64100  1.000 19.44468 ?  353 ALA A CA  1 
ATOM   2619 C  C   . ALA A 1 373 ? 16.96300  -0.15900  -9.91800  1.000 18.51239 ?  353 ALA A C   1 
ATOM   2620 O  O   . ALA A 1 373 ? 17.88300  0.66400   -9.93700  1.000 18.30109 ?  353 ALA A O   1 
ATOM   2621 C  CB  . ALA A 1 373 ? 17.24600  -2.42800  -10.94300 1.000 16.89105 ?  353 ALA A CB  1 
ATOM   2622 N  N   . ALA A 1 374 ? 15.69200  0.19300   -10.11900 1.000 16.40947 ?  354 ALA A N   1 
ATOM   2623 C  CA  . ALA A 1 374 ? 15.35100  1.57400   -10.45100 1.000 17.49624 ?  354 ALA A CA  1 
ATOM   2624 C  C   . ALA A 1 374 ? 15.64200  2.51400   -9.28900  1.000 18.50244 ?  354 ALA A C   1 
ATOM   2625 O  O   . ALA A 1 374 ? 16.23900  3.58400   -9.47500  1.000 16.97858 ?  354 ALA A O   1 
ATOM   2626 C  CB  . ALA A 1 374 ? 13.87900  1.66800   -10.86300 1.000 13.48548 ?  354 ALA A CB  1 
ATOM   2627 N  N   . PHE A 1 375 ? 15.22400  2.13500   -8.08000  1.000 14.36664 ?  355 PHE A N   1 
ATOM   2628 C  CA  . PHE A 1 375 ? 15.42400  3.00600   -6.92800  1.000 16.70070 ?  355 PHE A CA  1 
ATOM   2629 C  C   . PHE A 1 375 ? 16.89400  3.06100   -6.52300  1.000 16.42651 ?  355 PHE A C   1 
ATOM   2630 O  O   . PHE A 1 375 ? 17.38600  4.11500   -6.10600  1.000 18.24552 ?  355 PHE A O   1 
ATOM   2631 C  CB  . PHE A 1 375 ? 14.55600  2.53200   -5.76400  1.000 13.78031 ?  355 PHE A CB  1 
ATOM   2632 C  CG  . PHE A 1 375 ? 13.07700  2.62700   -6.03100  1.000 15.98477 ?  355 PHE A CG  1 
ATOM   2633 C  CD1 . PHE A 1 375 ? 12.56600  3.62200   -6.84200  1.000 28.54353 ?  355 PHE A CD1 1 
ATOM   2634 C  CD2 . PHE A 1 375 ? 12.20000  1.70400   -5.48000  1.000 26.69375 ?  355 PHE A CD2 1 
ATOM   2635 C  CE1 . PHE A 1 375 ? 11.19700  3.70400   -7.09300  1.000 24.97084 ?  355 PHE A CE1 1 
ATOM   2636 C  CE2 . PHE A 1 375 ? 10.83800  1.78200   -5.72900  1.000 21.97226 ?  355 PHE A CE2 1 
ATOM   2637 C  CZ  . PHE A 1 375 ? 10.34100  2.78400   -6.53300  1.000 20.72333 ?  355 PHE A CZ  1 
ATOM   2638 N  N   . SER A 1 376 ? 17.60700  1.93800   -6.63100  1.000 16.17037 ?  356 SER A N   1 
ATOM   2639 C  CA  . SER A 1 376 ? 19.03600  1.93300   -6.30900  1.000 20.29425 ?  356 SER A CA  1 
ATOM   2640 C  C   . SER A 1 376 ? 19.81700  2.89200   -7.19700  1.000 17.63773 ?  356 SER A C   1 
ATOM   2641 O  O   . SER A 1 376 ? 20.69400  3.62200   -6.71700  1.000 18.74386 ?  356 SER A O   1 
ATOM   2642 C  CB  . SER A 1 376 ? 19.60900  0.52300   -6.44600  1.000 20.42761 ?  356 SER A CB  1 
ATOM   2643 O  OG  . SER A 1 376 ? 19.08200  -0.34700  -5.46400  1.000 26.45213 ?  356 SER A OG  1 
ATOM   2644 N  N   . ALA A 1 377 ? 19.53700  2.88400   -8.50100  1.000 15.50138 ?  357 ALA A N   1 
ATOM   2645 C  CA  . ALA A 1 377 ? 20.24800  3.77900   -9.40700  1.000 17.25968 ?  357 ALA A CA  1 
ATOM   2646 C  C   . ALA A 1 377 ? 19.89900  5.23300   -9.12800  1.000 22.00576 ?  357 ALA A C   1 
ATOM   2647 O  O   . ALA A 1 377 ? 20.78500  6.09700   -9.11700  1.000 18.63963 ?  357 ALA A O   1 
ATOM   2648 C  CB  . ALA A 1 377 ? 19.94200  3.41300   -10.86100 1.000 17.27119 ?  357 ALA A CB  1 
ATOM   2649 N  N   . LEU A 1 378 ? 18.61500  5.51900   -8.88600  1.000 15.75241 ?  358 LEU A N   1 
ATOM   2650 C  CA  . LEU A 1 378 ? 18.20000  6.88200   -8.56900  1.000 20.90832 ?  358 LEU A CA  1 
ATOM   2651 C  C   . LEU A 1 378 ? 18.86700  7.36600   -7.28900  1.000 21.32974 ?  358 LEU A C   1 
ATOM   2652 O  O   . LEU A 1 378 ? 19.39700  8.48200   -7.23200  1.000 25.29831 ?  358 LEU A O   1 
ATOM   2653 C  CB  . LEU A 1 378 ? 16.67600  6.94700   -8.43400  1.000 20.06292 ?  358 LEU A CB  1 
ATOM   2654 C  CG  . LEU A 1 378 ? 15.90400  7.01300   -9.75300  1.000 23.99534 ?  358 LEU A CG  1 
ATOM   2655 C  CD1 . LEU A 1 378 ? 14.45300  6.57600   -9.55800  1.000 25.06910 ?  358 LEU A CD1 1 
ATOM   2656 C  CD2 . LEU A 1 378 ? 15.98400  8.40900   -10.35400 1.000 18.62861 ?  358 LEU A CD2 1 
ATOM   2657 N  N   . LEU A 1 379 ? 18.85600  6.52500   -6.25200  1.000 15.68661 ?  359 LEU A N   1 
ATOM   2658 C  CA  . LEU A 1 379 ? 19.44700  6.89900   -4.97100  1.000 16.80832 ?  359 LEU A CA  1 
ATOM   2659 C  C   . LEU A 1 379 ? 20.93400  7.18600   -5.11200  1.000 23.99406 ?  359 LEU A C   1 
ATOM   2660 O  O   . LEU A 1 379 ? 21.46400  8.09600   -4.46400  1.000 24.05385 ?  359 LEU A O   1 
ATOM   2661 C  CB  . LEU A 1 379 ? 19.22000  5.78200   -3.95600  1.000 20.23310 ?  359 LEU A CB  1 
ATOM   2662 C  CG  . LEU A 1 379 ? 17.80000  5.69400   -3.39400  1.000 25.54974 ?  359 LEU A CG  1 
ATOM   2663 C  CD1 . LEU A 1 379 ? 17.63700  4.41900   -2.58100  1.000 20.75507 ?  359 LEU A CD1 1 
ATOM   2664 C  CD2 . LEU A 1 379 ? 17.47100  6.92600   -2.56900  1.000 21.54343 ?  359 LEU A CD2 1 
ATOM   2665 N  N   . ALA A 1 380 ? 21.62300  6.41500   -5.95100  1.000 22.75391 ?  360 ALA A N   1 
ATOM   2666 C  CA  . ALA A 1 380 ? 23.05900  6.60300   -6.12800  1.000 22.91795 ?  360 ALA A CA  1 
ATOM   2667 C  C   . ALA A 1 380 ? 23.36200  7.85200   -6.94300  1.000 22.01833 ?  360 ALA A C   1 
ATOM   2668 O  O   . ALA A 1 380 ? 24.34500  8.55100   -6.67100  1.000 30.34783 ?  360 ALA A O   1 
ATOM   2669 C  CB  . ALA A 1 380 ? 23.66400  5.36900   -6.79400  1.000 20.94470 ?  360 ALA A CB  1 
ATOM   2670 N  N   . ARG A 1 381 ? 22.52700  8.15000   -7.93900  1.000 23.08405 ?  361 ARG A N   1 
ATOM   2671 C  CA  . ARG A 1 381 ? 22.73400  9.33900   -8.75600  1.000 22.46218 ?  361 ARG A CA  1 
ATOM   2672 C  C   . ARG A 1 381 ? 22.37600  10.60800  -7.99000  1.000 25.24444 ?  361 ARG A C   1 
ATOM   2673 O  O   . ARG A 1 381 ? 23.05700  11.63300  -8.12100  1.000 28.95651 ?  361 ARG A O   1 
ATOM   2674 C  CB  . ARG A 1 381 ? 21.91000  9.22500   -10.04000 1.000 18.84856 ?  361 ARG A CB  1 
ATOM   2675 C  CG  . ARG A 1 381 ? 21.87000  10.48400  -10.88800 1.000 21.22606 ?  361 ARG A CG  1 
ATOM   2676 C  CD  . ARG A 1 381 ? 23.16200  10.65000  -11.67500 1.000 26.77748 ?  361 ARG A CD  1 
ATOM   2677 N  NE  . ARG A 1 381 ? 23.04000  11.69000  -12.68800 1.000 20.59363 ?  361 ARG A NE  1 
ATOM   2678 C  CZ  . ARG A 1 381 ? 22.57000  11.48200  -13.91100 1.000 21.68872 ?  361 ARG A CZ  1 
ATOM   2679 N  NH1 . ARG A 1 381 ? 22.21200  10.27500  -14.31900 1.000 28.48341 ?  361 ARG A NH1 1 
ATOM   2680 N  NH2 . ARG A 1 381 ? 22.46300  12.51000  -14.74800 1.000 28.79379 ?  361 ARG A NH2 1 
ATOM   2681 N  N   . GLY A 1 382 ? 21.33000  10.55300  -7.17400  1.000 22.47918 ?  362 GLY A N   1 
ATOM   2682 C  CA  . GLY A 1 382 ? 20.79000  11.74400  -6.55700  1.000 21.25052 ?  362 GLY A CA  1 
ATOM   2683 C  C   . GLY A 1 382 ? 19.66300  12.31400  -7.39100  1.000 23.92141 ?  362 GLY A C   1 
ATOM   2684 O  O   . GLY A 1 382 ? 19.75400  12.37100  -8.62200  1.000 21.66617 ?  362 GLY A O   1 
ATOM   2685 N  N   . PHE A 1 383 ? 18.58300  12.72900  -6.73800  1.000 22.71910 ?  363 PHE A N   1 
ATOM   2686 C  CA  . PHE A 1 383 ? 17.43800  13.24000  -7.47100  1.000 20.19772 ?  363 PHE A CA  1 
ATOM   2687 C  C   . PHE A 1 383 ? 16.61800  14.14400  -6.56500  1.000 23.24971 ?  363 PHE A C   1 
ATOM   2688 O  O   . PHE A 1 383 ? 16.55100  13.93900  -5.35000  1.000 27.38676 ?  363 PHE A O   1 
ATOM   2689 C  CB  . PHE A 1 383 ? 16.56900  12.09900  -8.02600  1.000 27.11178 ?  363 PHE A CB  1 
ATOM   2690 C  CG  . PHE A 1 383 ? 15.95300  11.23500  -6.96400  1.000 21.45448 ?  363 PHE A CG  1 
ATOM   2691 C  CD1 . PHE A 1 383 ? 16.66600  10.18200  -6.41400  1.000 26.25906 ?  363 PHE A CD1 1 
ATOM   2692 C  CD2 . PHE A 1 383 ? 14.66300  11.47400  -6.51400  1.000 23.13417 ?  363 PHE A CD2 1 
ATOM   2693 C  CE1 . PHE A 1 383 ? 16.10600  9.38500   -5.43100  1.000 27.59846 ?  363 PHE A CE1 1 
ATOM   2694 C  CE2 . PHE A 1 383 ? 14.09800  10.67900  -5.53200  1.000 23.69743 ?  363 PHE A CE2 1 
ATOM   2695 C  CZ  . PHE A 1 383 ? 14.82400  9.63300   -4.99100  1.000 24.68678 ?  363 PHE A CZ  1 
ATOM   2696 N  N   . ARG A 1 384 ? 16.00000  15.14700  -7.18200  1.000 26.64175 ?  364 ARG A N   1 
ATOM   2697 C  CA  . ARG A 1 384 ? 15.07500  16.03900  -6.50400  1.000 24.49205 ?  364 ARG A CA  1 
ATOM   2698 C  C   . ARG A 1 384 ? 14.04200  16.49300  -7.52000  1.000 28.47581 ?  364 ARG A C   1 
ATOM   2699 O  O   . ARG A 1 384 ? 14.28100  16.46200  -8.73000  1.000 28.33702 ?  364 ARG A O   1 
ATOM   2700 C  CB  . ARG A 1 384 ? 15.79500  17.24400  -5.88400  1.000 30.50727 ?  364 ARG A CB  1 
ATOM   2701 C  CG  . ARG A 1 384 ? 16.50900  18.11000  -6.91300  1.000 37.62980 ?  364 ARG A CG  1 
ATOM   2702 C  CD  . ARG A 1 384 ? 17.04100  19.42000  -6.33600  1.000 40.52283 ?  364 ARG A CD  1 
ATOM   2703 N  NE  . ARG A 1 384 ? 18.11100  19.19800  -5.37000  1.000 47.81928 ?  364 ARG A NE  1 
ATOM   2704 C  CZ  . ARG A 1 384 ? 18.60200  20.13000  -4.56400  1.000 32.80911 ?  364 ARG A CZ  1 
ATOM   2705 N  NH1 . ARG A 1 384 ? 18.20900  21.39000  -4.64500  1.000 34.29412 ?  364 ARG A NH1 1 
ATOM   2706 N  NH2 . ARG A 1 384 ? 19.52300  19.79300  -3.66500  1.000 43.21827 ?  364 ARG A NH2 1 
ATOM   2707 N  N   . ALA A 1 385 ? 12.88200  16.90400  -7.01700  1.000 24.32737 ?  365 ALA A N   1 
ATOM   2708 C  CA  . ALA A 1 385 ? 11.83300  17.38600  -7.90000  1.000 21.41423 ?  365 ALA A CA  1 
ATOM   2709 C  C   . ALA A 1 385 ? 12.27300  18.67400  -8.58000  1.000 26.65832 ?  365 ALA A C   1 
ATOM   2710 O  O   . ALA A 1 385 ? 12.88200  19.54700  -7.95800  1.000 27.73143 ?  365 ALA A O   1 
ATOM   2711 C  CB  . ALA A 1 385 ? 10.54100  17.61700  -7.11600  1.000 28.52461 ?  365 ALA A CB  1 
ATOM   2712 N  N   . ALA A 1 386 ? 11.98000  18.77900  -9.87400  1.000 25.96882 ?  366 ALA A N   1 
ATOM   2713 C  CA  . ALA A 1 386 ? 12.23800  20.00000  -10.62400 1.000 27.44795 ?  366 ALA A CA  1 
ATOM   2714 C  C   . ALA A 1 386 ? 11.05600  20.95700  -10.59800 1.000 33.47745 ?  366 ALA A C   1 
ATOM   2715 O  O   . ALA A 1 386 ? 11.18700  22.09700  -11.05600 1.000 33.08507 ?  366 ALA A O   1 
ATOM   2716 C  CB  . ALA A 1 386 ? 12.59300  19.66800  -12.07600 1.000 29.03628 ?  366 ALA A CB  1 
ATOM   2717 N  N   . VAL A 1 387 ? 9.91400   20.52100  -10.06800 1.000 25.38065 ?  367 VAL A N   1 
ATOM   2718 C  CA  . VAL A 1 387 ? 8.71200   21.33700  -9.97500  1.000 28.33455 ?  367 VAL A CA  1 
ATOM   2719 C  C   . VAL A 1 387 ? 8.12300   21.15800  -8.58200  1.000 28.05045 ?  367 VAL A C   1 
ATOM   2720 O  O   . VAL A 1 387 ? 8.50400   20.26000  -7.82900  1.000 28.70150 ?  367 VAL A O   1 
ATOM   2721 C  CB  . VAL A 1 387 ? 7.66100   20.95900  -11.04000 1.000 27.48648 ?  367 VAL A CB  1 
ATOM   2722 C  CG1 . VAL A 1 387 ? 8.13600   21.35400  -12.42800 1.000 34.90084 ?  367 VAL A CG1 1 
ATOM   2723 C  CG2 . VAL A 1 387 ? 7.34700   19.47200  -10.96600 1.000 29.14904 ?  367 VAL A CG2 1 
ATOM   2724 N  N   . ASP A 1 388 ? 7.18100   22.03200  -8.24500  1.000 33.63157 ?  368 ASP A N   1 
ATOM   2725 C  CA  . ASP A 1 388 ? 6.37300   21.83000  -7.05300  1.000 33.70475 ?  368 ASP A CA  1 
ATOM   2726 C  C   . ASP A 1 388 ? 5.51800   20.58100  -7.24500  1.000 27.77885 ?  368 ASP A C   1 
ATOM   2727 O  O   . ASP A 1 388 ? 4.87300   20.41700  -8.28500  1.000 29.81764 ?  368 ASP A O   1 
ATOM   2728 C  CB  . ASP A 1 388 ? 5.50500   23.06300  -6.80100  1.000 31.50698 ?  368 ASP A CB  1 
ATOM   2729 C  CG  . ASP A 1 388 ? 4.64700   22.94000  -5.56000  1.000 40.99476 ?  368 ASP A CG  1 
ATOM   2730 O  OD1 . ASP A 1 388 ? 4.91900   22.05500  -4.72300  1.000 49.96986 ?  368 ASP A OD1 1 
ATOM   2731 O  OD2 . ASP A 1 388 ? 3.70000   23.74200  -5.42100  1.000 47.70598 -1 368 ASP A OD2 1 
ATOM   2732 N  N   . LEU A 1 389 ? 5.53400   19.68500  -6.25200  1.000 30.01531 ?  369 LEU A N   1 
ATOM   2733 C  CA  . LEU A 1 389 ? 4.80600   18.42500  -6.39300  1.000 29.00395 ?  369 LEU A CA  1 
ATOM   2734 C  C   . LEU A 1 389 ? 3.30600   18.65300  -6.53900  1.000 30.01673 ?  369 LEU A C   1 
ATOM   2735 O  O   . LEU A 1 389 ? 2.61700   17.85000  -7.18000  1.000 31.56386 ?  369 LEU A O   1 
ATOM   2736 C  CB  . LEU A 1 389 ? 5.08800   17.50600  -5.20300  1.000 29.08070 ?  369 LEU A CB  1 
ATOM   2737 C  CG  . LEU A 1 389 ? 6.49800   16.92000  -5.05800  1.000 32.87569 ?  369 LEU A CG  1 
ATOM   2738 C  CD1 . LEU A 1 389 ? 6.51900   15.88400  -3.95000  1.000 34.26986 ?  369 LEU A CD1 1 
ATOM   2739 C  CD2 . LEU A 1 389 ? 6.98900   16.31700  -6.36200  1.000 25.16806 ?  369 LEU A CD2 1 
ATOM   2740 N  N   . ALA A 1 390 ? 2.78200   19.73800  -5.96200  1.000 33.81272 ?  370 ALA A N   1 
ATOM   2741 C  CA  . ALA A 1 390 ? 1.36700   20.06400  -6.09800  1.000 32.37266 ?  370 ALA A CA  1 
ATOM   2742 C  C   . ALA A 1 390 ? 0.96500   20.37500  -7.53300  1.000 36.37389 ?  370 ALA A C   1 
ATOM   2743 O  O   . ALA A 1 390 ? -0.23400  20.39600  -7.83000  1.000 37.56600 ?  370 ALA A O   1 
ATOM   2744 C  CB  . ALA A 1 390 ? 1.01100   21.25000  -5.19600  1.000 34.44554 ?  370 ALA A CB  1 
ATOM   2745 N  N   . ASP A 1 391 ? 1.92600   20.61900  -8.42300  1.000 32.14628 ?  371 ASP A N   1 
ATOM   2746 C  CA  . ASP A 1 391 ? 1.64900   20.91900  -9.81900  1.000 35.54613 ?  371 ASP A CA  1 
ATOM   2747 C  C   . ASP A 1 391 ? 1.71300   19.68700  -10.71000 1.000 31.25651 ?  371 ASP A C   1 
ATOM   2748 O  O   . ASP A 1 391 ? 1.51000   19.80200  -11.92200 1.000 28.76706 ?  371 ASP A O   1 
ATOM   2749 C  CB  . ASP A 1 391 ? 2.62600   21.98600  -10.32400 1.000 41.32362 ?  371 ASP A CB  1 
ATOM   2750 C  CG  . ASP A 1 391 ? 2.33200   23.35900  -9.75000  1.000 47.16488 ?  371 ASP A CG  1 
ATOM   2751 O  OD1 . ASP A 1 391 ? 1.17600   23.59000  -9.33300  1.000 42.51249 -1 371 ASP A OD1 1 
ATOM   2752 O  OD2 . ASP A 1 391 ? 3.25600   24.19800  -9.70000  1.000 49.77661 -1 371 ASP A OD2 1 
ATOM   2753 N  N   . LEU A 1 392 ? 1.98700   18.51700  -10.14000 1.000 30.41152 ?  372 LEU A N   1 
ATOM   2754 C  CA  . LEU A 1 392 ? 2.00700   17.28500  -10.91300 1.000 30.29917 ?  372 LEU A CA  1 
ATOM   2755 C  C   . LEU A 1 392 ? 0.59100   16.90300  -11.33500 1.000 28.35451 ?  372 LEU A C   1 
ATOM   2756 O  O   . LEU A 1 392 ? -0.38000  17.13200  -10.61000 1.000 31.17310 ?  372 LEU A O   1 
ATOM   2757 C  CB  . LEU A 1 392 ? 2.62700   16.16100  -10.08900 1.000 29.24940 ?  372 LEU A CB  1 
ATOM   2758 C  CG  . LEU A 1 392 ? 4.14800   16.19800  -9.92700  1.000 26.27133 ?  372 LEU A CG  1 
ATOM   2759 C  CD1 . LEU A 1 392 ? 4.59600   15.10700  -8.97400  1.000 29.36339 ?  372 LEU A CD1 1 
ATOM   2760 C  CD2 . LEU A 1 392 ? 4.84100   16.05600  -11.27200 1.000 24.42231 ?  372 LEU A CD2 1 
ATOM   2761 N  N   . GLN A 1 393 ? 0.47800   16.31300  -12.52100 1.000 26.46168 ?  373 GLN A N   1 
ATOM   2762 C  CA  . GLN A 1 393 ? -0.81000  15.91000  -13.07300 1.000 28.87157 ?  373 GLN A CA  1 
ATOM   2763 C  C   . GLN A 1 393 ? -0.88400  14.39300  -13.18400 1.000 27.34428 ?  373 GLN A C   1 
ATOM   2764 O  O   . GLN A 1 393 ? 0.10400   13.73500  -13.52600 1.000 26.91686 ?  373 GLN A O   1 
ATOM   2765 C  CB  . GLN A 1 393 ? -1.04700  16.55100  -14.44400 1.000 32.33937 ?  373 GLN A CB  1 
ATOM   2766 C  CG  . GLN A 1 393 ? -0.47400  17.95400  -14.57600 1.000 31.18222 ?  373 GLN A CG  1 
ATOM   2767 N  N   . TRP A 1 394 ? -2.06000  13.84300  -12.88500 1.000 33.16857 ?  374 TRP A N   1 
ATOM   2768 C  CA  . TRP A 1 394 ? -2.29700  12.40700  -12.89200 1.000 28.85448 ?  374 TRP A CA  1 
ATOM   2769 C  C   . TRP A 1 394 ? -3.13100  12.00400  -14.10200 1.000 28.68422 ?  374 TRP A C   1 
ATOM   2770 O  O   . TRP A 1 394 ? -3.98000  12.76400  -14.57400 1.000 34.17892 ?  374 TRP A O   1 
ATOM   2771 C  CB  . TRP A 1 394 ? -3.00600  11.96000  -11.61000 1.000 23.74913 ?  374 TRP A CB  1 
ATOM   2772 C  CG  . TRP A 1 394 ? -2.23000  12.23400  -10.36200 1.000 29.56160 ?  374 TRP A CG  1 
ATOM   2773 C  CD1 . TRP A 1 394 ? -2.20500  13.39700  -9.64600  1.000 29.22716 ?  374 TRP A CD1 1 
ATOM   2774 C  CD2 . TRP A 1 394 ? -1.36700  11.32100  -9.67400  1.000 23.23847 ?  374 TRP A CD2 1 
ATOM   2775 N  NE1 . TRP A 1 394 ? -1.37700  13.26400  -8.55800  1.000 33.10704 ?  374 TRP A NE1 1 
ATOM   2776 C  CE2 . TRP A 1 394 ? -0.85200  11.99800  -8.55100  1.000 22.86755 ?  374 TRP A CE2 1 
ATOM   2777 C  CE3 . TRP A 1 394 ? -0.98400  9.99400   -9.89800  1.000 23.44118 ?  374 TRP A CE3 1 
ATOM   2778 C  CZ2 . TRP A 1 394 ? 0.03400   11.39600  -7.65500  1.000 24.92552 ?  374 TRP A CZ2 1 
ATOM   2779 C  CZ3 . TRP A 1 394 ? -0.10500  9.39500   -9.00600  1.000 22.71935 ?  374 TRP A CZ3 1 
ATOM   2780 C  CH2 . TRP A 1 394 ? 0.39400   10.09700  -7.89800  1.000 24.96365 ?  374 TRP A CH2 1 
ATOM   2781 N  N   . GLN A 1 395 ? -2.88500  10.79200  -14.59000 1.000 25.51701 ?  375 GLN A N   1 
ATOM   2782 C  CA  . GLN A 1 395 ? -3.59000  10.30900  -15.76500 1.000 32.33945 ?  375 GLN A CA  1 
ATOM   2783 C  C   . GLN A 1 395 ? -5.04400  10.00500  -15.41100 1.000 34.03558 ?  375 GLN A C   1 
ATOM   2784 O  O   . GLN A 1 395 ? -5.32700  9.49400   -14.32000 1.000 28.73954 ?  375 GLN A O   1 
ATOM   2785 C  CB  . GLN A 1 395 ? -2.91200  9.05600   -16.32100 1.000 32.33572 ?  375 GLN A CB  1 
ATOM   2786 N  N   . PRO A 1 396 ? -5.98900  10.29500  -16.30500 1.000 37.19002 ?  376 PRO A N   1 
ATOM   2787 C  CA  . PRO A 1 396 ? -7.39800  10.02100  -15.98900 1.000 39.52629 ?  376 PRO A CA  1 
ATOM   2788 C  C   . PRO A 1 396 ? -7.76700  8.55800   -16.20300 1.000 43.40137 ?  376 PRO A C   1 
ATOM   2789 O  O   . PRO A 1 396 ? -8.23800  8.17500   -17.27900 1.000 45.67931 ?  376 PRO A O   1 
ATOM   2790 C  CB  . PRO A 1 396 ? -8.14700  10.93700  -16.96000 1.000 37.48864 ?  376 PRO A CB  1 
ATOM   2791 C  CG  . PRO A 1 396 ? -7.25000  10.97300  -18.15400 1.000 38.75083 ?  376 PRO A CG  1 
ATOM   2792 C  CD  . PRO A 1 396 ? -5.82900  10.92100  -17.62900 1.000 36.15215 ?  376 PRO A CD  1 
ATOM   2793 N  N   . SER A 1 397 ? -7.55700  7.72800   -15.18200 1.000 39.72599 ?  377 SER A N   1 
ATOM   2794 C  CA  . SER A 1 397 ? -7.87400  6.30900   -15.24900 1.000 35.91741 ?  377 SER A CA  1 
ATOM   2795 C  C   . SER A 1 397 ? -8.64700  5.89900   -14.00500 1.000 37.32446 ?  377 SER A C   1 
ATOM   2796 O  O   . SER A 1 397 ? -8.52400  6.52000   -12.94800 1.000 42.82352 ?  377 SER A O   1 
ATOM   2797 C  CB  . SER A 1 397 ? -6.60500  5.45400   -15.38500 1.000 37.19985 ?  377 SER A CB  1 
ATOM   2798 O  OG  . SER A 1 397 ? -6.91600  4.07400   -15.49000 1.000 37.07070 ?  377 SER A OG  1 
ATOM   2799 N  N   . PHE A 1 398 ? -9.44800  4.84400   -14.14700 1.000 24.78402 ?  378 PHE A N   1 
ATOM   2800 C  CA  . PHE A 1 398 ? -10.20400 4.29500   -13.03100 1.000 27.00840 ?  378 PHE A CA  1 
ATOM   2801 C  C   . PHE A 1 398 ? -9.44300  3.17400   -12.33400 1.000 24.50449 ?  378 PHE A C   1 
ATOM   2802 O  O   . PHE A 1 398 ? -9.58400  3.00000   -11.11700 1.000 24.44847 ?  378 PHE A O   1 
ATOM   2803 C  CB  . PHE A 1 398 ? -11.56800 3.79500   -13.53400 1.000 26.94132 ?  378 PHE A CB  1 
ATOM   2804 C  CG  . PHE A 1 398 ? -12.45500 3.19700   -12.46300 1.000 28.42256 ?  378 PHE A CG  1 
ATOM   2805 C  CD1 . PHE A 1 398 ? -12.91800 3.96700   -11.40500 1.000 27.01178 ?  378 PHE A CD1 1 
ATOM   2806 C  CD2 . PHE A 1 398 ? -12.85200 1.86800   -12.53900 1.000 27.99206 ?  378 PHE A CD2 1 
ATOM   2807 C  CE1 . PHE A 1 398 ? -13.74400 3.42300   -10.43500 1.000 27.64242 ?  378 PHE A CE1 1 
ATOM   2808 C  CE2 . PHE A 1 398 ? -13.67800 1.31500   -11.57000 1.000 21.13002 ?  378 PHE A CE2 1 
ATOM   2809 C  CZ  . PHE A 1 398 ? -14.12300 2.09700   -10.51400 1.000 26.58317 ?  378 PHE A CZ  1 
ATOM   2810 N  N   . ARG A 1 399 ? -8.60700  2.44200   -13.07300 1.000 25.65234 ?  379 ARG A N   1 
ATOM   2811 C  CA  . ARG A 1 399 ? -7.90900  1.27800   -12.54300 1.000 20.50626 ?  379 ARG A CA  1 
ATOM   2812 C  C   . ARG A 1 399 ? -6.41700  1.47400   -12.34600 1.000 20.25594 ?  379 ARG A C   1 
ATOM   2813 O  O   . ARG A 1 399 ? -5.84200  0.82200   -11.47700 1.000 21.46649 ?  379 ARG A O   1 
ATOM   2814 C  CB  . ARG A 1 399 ? -8.11000  0.06200   -13.45600 1.000 23.97986 ?  379 ARG A CB  1 
ATOM   2815 C  CG  . ARG A 1 399 ? -7.70600  -1.25900  -12.79500 1.000 30.05419 ?  379 ARG A CG  1 
ATOM   2816 C  CD  . ARG A 1 399 ? -8.32200  -2.46400  -13.48800 1.000 28.78690 ?  379 ARG A CD  1 
ATOM   2817 N  NE  . ARG A 1 399 ? -7.68900  -2.77900  -14.76500 1.000 32.20375 ?  379 ARG A NE  1 
ATOM   2818 C  CZ  . ARG A 1 399 ? -7.97900  -3.85600  -15.48400 1.000 33.47814 ?  379 ARG A CZ  1 
ATOM   2819 N  NH1 . ARG A 1 399 ? -8.92700  -4.70100  -15.10900 1.000 23.91956 ?  379 ARG A NH1 1 
ATOM   2820 N  NH2 . ARG A 1 399 ? -7.30600  -4.08800  -16.60800 1.000 31.43236 ?  379 ARG A NH2 1 
ATOM   2821 N  N   . ASN A 1 400 ? -5.76700  2.33500   -13.12300 1.000 21.50933 ?  380 ASN A N   1 
ATOM   2822 C  CA  . ASN A 1 400 ? -4.30500  2.40400   -13.13100 1.000 21.54698 ?  380 ASN A CA  1 
ATOM   2823 C  C   . ASN A 1 400 ? -3.87100  3.83400   -12.83100 1.000 22.35564 ?  380 ASN A C   1 
ATOM   2824 O  O   . ASN A 1 400 ? -3.92300  4.70800   -13.70200 1.000 26.08524 ?  380 ASN A O   1 
ATOM   2825 C  CB  . ASN A 1 400 ? -3.75300  1.90600   -14.46100 1.000 22.57703 ?  380 ASN A CB  1 
ATOM   2826 C  CG  . ASN A 1 400 ? -2.45100  1.14800   -14.29700 1.000 36.49079 ?  380 ASN A CG  1 
ATOM   2827 O  OD1 . ASN A 1 400 ? -1.37100  1.73600   -14.27500 1.000 29.86146 ?  380 ASN A OD1 1 
ATOM   2828 N  ND2 . ASN A 1 400 ? -2.55300  -0.17100  -14.15300 1.000 35.11122 ?  380 ASN A ND2 1 
ATOM   2829 N  N   . ARG A 1 401 ? -3.43200  4.06400   -11.59800 1.000 14.38410 ?  381 ARG A N   1 
ATOM   2830 C  CA  . ARG A 1 401 ? -3.03800  5.38900   -11.14400 1.000 19.33504 ?  381 ARG A CA  1 
ATOM   2831 C  C   . ARG A 1 401 ? -1.58600  5.63700   -11.53200 1.000 20.42590 ?  381 ARG A C   1 
ATOM   2832 O  O   . ARG A 1 401 ? -0.70500  4.84100   -11.19400 1.000 19.48540 ?  381 ARG A O   1 
ATOM   2833 C  CB  . ARG A 1 401 ? -3.23300  5.50500   -9.63400  1.000 20.49559 ?  381 ARG A CB  1 
ATOM   2834 C  CG  . ARG A 1 401 ? -2.74700  6.79400   -9.01200  1.000 22.91499 ?  381 ARG A CG  1 
ATOM   2835 C  CD  . ARG A 1 401 ? -3.13000  6.82200   -7.55000  1.000 16.80988 ?  381 ARG A CD  1 
ATOM   2836 N  NE  . ARG A 1 401 ? -2.51700  7.92600   -6.82600  1.000 21.10279 ?  381 ARG A NE  1 
ATOM   2837 C  CZ  . ARG A 1 401 ? -2.95800  9.17600   -6.85300  1.000 26.75345 ?  381 ARG A CZ  1 
ATOM   2838 N  NH1 . ARG A 1 401 ? -3.97200  9.53300   -7.62200  1.000 23.63677 ?  381 ARG A NH1 1 
ATOM   2839 N  NH2 . ARG A 1 401 ? -2.36100  10.09100  -6.09500  1.000 29.21021 ?  381 ARG A NH2 1 
ATOM   2840 N  N   . GLY A 1 402 ? -1.34100  6.73700   -12.23500 1.000 18.58462 ?  382 GLY A N   1 
ATOM   2841 C  CA  . GLY A 1 402 ? -0.00200  7.05700   -12.68800 1.000 19.86522 ?  382 GLY A CA  1 
ATOM   2842 C  C   . GLY A 1 402 ? 0.09900   8.50100   -13.11600 1.000 23.72590 ?  382 GLY A C   1 
ATOM   2843 O  O   . GLY A 1 402 ? -0.90000  9.14500   -13.45600 1.000 25.49197 ?  382 GLY A O   1 
ATOM   2844 N  N   . LEU A 1 403 ? 1.32900   9.00100   -13.10600 1.000 24.16782 ?  383 LEU A N   1 
ATOM   2845 C  CA  . LEU A 1 403 ? 1.61500   10.39600  -13.40800 1.000 21.04425 ?  383 LEU A CA  1 
ATOM   2846 C  C   . LEU A 1 403 ? 1.79200   10.60100  -14.91000 1.000 22.42921 ?  383 LEU A C   1 
ATOM   2847 O  O   . LEU A 1 403 ? 2.28300   9.71900   -15.62100 1.000 19.21055 ?  383 LEU A O   1 
ATOM   2848 C  CB  . LEU A 1 403 ? 2.88500   10.84000  -12.67800 1.000 18.67333 ?  383 LEU A CB  1 
ATOM   2849 C  CG  . LEU A 1 403 ? 2.78700   11.02100  -11.16400 1.000 19.08850 ?  383 LEU A CG  1 
ATOM   2850 C  CD1 . LEU A 1 403 ? 4.17900   10.98500  -10.53500 1.000 20.71738 ?  383 LEU A CD1 1 
ATOM   2851 C  CD2 . LEU A 1 403 ? 2.08100   12.32000  -10.81200 1.000 21.43406 ?  383 LEU A CD2 1 
ATOM   2852 N  N   . THR A 1 404 ? 1.39000   11.78400  -15.39200 1.000 20.55719 ?  384 THR A N   1 
ATOM   2853 C  CA  . THR A 1 404 ? 1.64100   12.11600  -16.79300 1.000 20.32596 ?  384 THR A CA  1 
ATOM   2854 C  C   . THR A 1 404 ? 3.12300   12.34700  -17.04700 1.000 24.20370 ?  384 THR A C   1 
ATOM   2855 O  O   . THR A 1 404 ? 3.62200   12.03600  -18.13500 1.000 22.18541 ?  384 THR A O   1 
ATOM   2856 C  CB  . THR A 1 404 ? 0.85800   13.36300  -17.20800 1.000 21.93271 ?  384 THR A CB  1 
ATOM   2857 O  OG1 . THR A 1 404 ? 1.22500   14.46200  -16.36700 1.000 25.81363 ?  384 THR A OG1 1 
ATOM   2858 C  CG2 . THR A 1 404 ? -0.64100  13.12300  -17.06600 1.000 24.00322 ?  384 THR A CG2 1 
ATOM   2859 N  N   . GLU A 1 405 ? 3.82700   12.88900  -16.05700 1.000 23.21061 ?  385 GLU A N   1 
ATOM   2860 C  CA  . GLU A 1 405 ? 5.24600   13.21400  -16.11400 1.000 25.11692 ?  385 GLU A CA  1 
ATOM   2861 C  C   . GLU A 1 405 ? 5.69800   13.55100  -14.69900 1.000 25.36550 ?  385 GLU A C   1 
ATOM   2862 O  O   . GLU A 1 405 ? 4.88500   13.89500  -13.83800 1.000 24.98524 ?  385 GLU A O   1 
ATOM   2863 C  CB  . GLU A 1 405 ? 5.52500   14.38700  -17.06300 1.000 29.24590 ?  385 GLU A CB  1 
ATOM   2864 C  CG  . GLU A 1 405 ? 5.31500   15.75500  -16.42200 1.000 39.81025 ?  385 GLU A CG  1 
ATOM   2865 C  CD  . GLU A 1 405 ? 5.31800   16.89300  -17.43000 1.000 49.63542 ?  385 GLU A CD  1 
ATOM   2866 O  OE1 . GLU A 1 405 ? 4.87400   16.67600  -18.57600 1.000 52.54721 ?  385 GLU A OE1 1 
ATOM   2867 O  OE2 . GLU A 1 405 ? 5.75600   18.00700  -17.07100 1.000 58.45869 -1 385 GLU A OE2 1 
ATOM   2868 N  N   . LEU A 1 406 ? 7.01000   13.43700  -14.44300 1.000 21.21611 ?  386 LEU A N   1 
ATOM   2869 C  CA  . LEU A 1 406 ? 7.58700   13.80600  -13.15100 1.000 24.10694 ?  386 LEU A CA  1 
ATOM   2870 C  C   . LEU A 1 406 ? 8.93600   14.46100  -13.39700 1.000 24.53156 ?  386 LEU A C   1 
ATOM   2871 O  O   . LEU A 1 406 ? 9.96500   13.78100  -13.50100 1.000 23.09380 ?  386 LEU A O   1 
ATOM   2872 C  CB  . LEU A 1 406 ? 7.71300   12.59700  -12.22100 1.000 25.23002 ?  386 LEU A CB  1 
ATOM   2873 C  CG  . LEU A 1 406 ? 8.36700   12.80400  -10.84700 1.000 38.19446 ?  386 LEU A CG  1 
ATOM   2874 C  CD1 . LEU A 1 406 ? 7.91700   14.10200  -10.18900 1.000 28.13769 ?  386 LEU A CD1 1 
ATOM   2875 C  CD2 . LEU A 1 406 ? 8.05800   11.61700  -9.94100  1.000 33.37136 ?  386 LEU A CD2 1 
ATOM   2876 N  N   . PRO A 1 407 ? 8.96200   15.79800  -13.51300 1.000 24.70506 ?  387 PRO A N   1 
ATOM   2877 C  CA  . PRO A 1 407 ? 10.22900  16.49400  -13.77700 1.000 26.45112 ?  387 PRO A CA  1 
ATOM   2878 C  C   . PRO A 1 407 ? 11.15800  16.40300  -12.57800 1.000 25.41364 ?  387 PRO A C   1 
ATOM   2879 O  O   . PRO A 1 407 ? 10.78300  16.74900  -11.45500 1.000 24.28005 ?  387 PRO A O   1 
ATOM   2880 C  CB  . PRO A 1 407 ? 9.79300   17.94200  -14.04500 1.000 26.86056 ?  387 PRO A CB  1 
ATOM   2881 C  CG  . PRO A 1 407 ? 8.31700   17.84800  -14.36100 1.000 29.46530 ?  387 PRO A CG  1 
ATOM   2882 C  CD  . PRO A 1 407 ? 7.82200   16.72900  -13.50000 1.000 27.02823 ?  387 PRO A CD  1 
ATOM   2883 N  N   . LEU A 1 408 ? 12.37900  15.94000  -12.83000 1.000 25.64525 ?  388 LEU A N   1 
ATOM   2884 C  CA  . LEU A 1 408 ? 13.38200  15.73000  -11.80100 1.000 24.39418 ?  388 LEU A CA  1 
ATOM   2885 C  C   . LEU A 1 408 ? 14.65800  16.48100  -12.15300 1.000 23.97810 ?  388 LEU A C   1 
ATOM   2886 O  O   . LEU A 1 408 ? 14.87100  16.89500  -13.29400 1.000 25.49058 ?  388 LEU A O   1 
ATOM   2887 C  CB  . LEU A 1 408 ? 13.71000  14.23700  -11.63300 1.000 26.59734 ?  388 LEU A CB  1 
ATOM   2888 C  CG  . LEU A 1 408 ? 12.65900  13.32500  -10.99700 1.000 24.50288 ?  388 LEU A CG  1 
ATOM   2889 C  CD1 . LEU A 1 408 ? 13.27000  11.96000  -10.70300 1.000 22.53167 ?  388 LEU A CD1 1 
ATOM   2890 C  CD2 . LEU A 1 408 ? 12.08700  13.94900  -9.73600  1.000 22.55193 ?  388 LEU A CD2 1 
ATOM   2891 N  N   . LEU A 1 409 ? 15.50300  16.65300  -11.14200 1.000 25.61912 ?  389 LEU A N   1 
ATOM   2892 C  CA  . LEU A 1 409 ? 16.87400  17.11300  -11.31900 1.000 26.35524 ?  389 LEU A CA  1 
ATOM   2893 C  C   . LEU A 1 409 ? 17.78800  16.01000  -10.81200 1.000 24.38946 ?  389 LEU A C   1 
ATOM   2894 O  O   . LEU A 1 409 ? 17.65600  15.56700  -9.66500  1.000 24.37935 ?  389 LEU A O   1 
ATOM   2895 C  CB  . LEU A 1 409 ? 17.13100  18.42400  -10.57100 1.000 26.34024 ?  389 LEU A CB  1 
ATOM   2896 C  CG  . LEU A 1 409 ? 16.40000  19.66700  -11.08600 1.000 29.86325 ?  389 LEU A CG  1 
ATOM   2897 C  CD1 . LEU A 1 409 ? 16.50300  20.80100  -10.08100 1.000 34.36081 ?  389 LEU A CD1 1 
ATOM   2898 C  CD2 . LEU A 1 409 ? 16.92500  20.10200  -12.44500 1.000 29.20768 ?  389 LEU A CD2 1 
ATOM   2899 N  N   . LEU A 1 410 ? 18.69400  15.55300  -11.66700 1.000 26.30539 ?  390 LEU A N   1 
ATOM   2900 C  CA  . LEU A 1 410 ? 19.57900  14.44800  -11.33800 1.000 25.09289 ?  390 LEU A CA  1 
ATOM   2901 C  C   . LEU A 1 410 ? 20.92400  14.97500  -10.85000 1.000 27.40997 ?  390 LEU A C   1 
ATOM   2902 O  O   . LEU A 1 410 ? 21.40500  16.01700  -11.30400 1.000 26.86203 ?  390 LEU A O   1 
ATOM   2903 C  CB  . LEU A 1 410 ? 19.77000  13.54000  -12.55400 1.000 24.76236 ?  390 LEU A CB  1 
ATOM   2904 C  CG  . LEU A 1 410 ? 18.46400  12.91800  -13.06400 1.000 25.83338 ?  390 LEU A CG  1 
ATOM   2905 C  CD1 . LEU A 1 410 ? 18.73100  11.93400  -14.18700 1.000 20.90526 ?  390 LEU A CD1 1 
ATOM   2906 C  CD2 . LEU A 1 410 ? 17.71900  12.24100  -11.92400 1.000 20.43795 ?  390 LEU A CD2 1 
ATOM   2907 N  N   . GLY A 1 411 ? 21.52100  14.25000  -9.90900  1.000 25.85863 ?  391 GLY A N   1 
ATOM   2908 C  CA  . GLY A 1 411 ? 22.82300  14.61500  -9.38000  1.000 33.99486 ?  391 GLY A CA  1 
ATOM   2909 C  C   . GLY A 1 411 ? 23.93700  14.39100  -10.38600 1.000 39.84177 ?  391 GLY A C   1 
ATOM   2910 O  O   . GLY A 1 411 ? 23.73100  13.76000  -11.42300 1.000 42.01610 ?  391 GLY A O   1 
ATOM   2911 O  OXT . GLY A 1 411 ? 25.07200  14.83400  -10.20100 1.000 50.20196 -1 391 GLY A OXT 1 
ATOM   2912 N  N   . ALA B 1 28  ? -5.27500  21.17900  -38.46500 1.000 55.03255 ?  8   ALA B N   1 
ATOM   2913 C  CA  . ALA B 1 28  ? -5.65400  21.69500  -39.80200 1.000 58.79308 ?  8   ALA B CA  1 
ATOM   2914 C  C   . ALA B 1 28  ? -6.21000  20.56300  -40.67200 1.000 59.73326 ?  8   ALA B C   1 
ATOM   2915 O  O   . ALA B 1 28  ? -7.33100  20.70900  -41.17200 1.000 57.22283 ?  8   ALA B O   1 
ATOM   2916 C  CB  . ALA B 1 28  ? -4.46800  22.35100  -40.45600 1.000 54.23760 ?  8   ALA B CB  1 
ATOM   2917 N  N   . PHE B 1 29  ? -5.45800  19.47300  -40.82300 1.000 53.17528 ?  9   PHE B N   1 
ATOM   2918 C  CA  . PHE B 1 29  ? -5.96300  18.30800  -41.59100 1.000 56.50364 ?  9   PHE B CA  1 
ATOM   2919 C  C   . PHE B 1 29  ? -7.30700  17.87200  -41.00100 1.000 54.46578 ?  9   PHE B C   1 
ATOM   2920 O  O   . PHE B 1 29  ? -8.18900  17.46900  -41.75900 1.000 55.45271 ?  9   PHE B O   1 
ATOM   2921 C  CB  . PHE B 1 29  ? -4.93400  17.17900  -41.54900 1.000 53.53085 ?  9   PHE B CB  1 
ATOM   2922 C  CG  . PHE B 1 29  ? -5.28500  15.90300  -42.27100 1.000 53.91467 ?  9   PHE B CG  1 
ATOM   2923 C  CD1 . PHE B 1 29  ? -4.92900  15.71700  -43.59600 1.000 50.22616 ?  9   PHE B CD1 1 
ATOM   2924 C  CD2 . PHE B 1 29  ? -5.91500  14.86100  -41.60900 1.000 55.91294 ?  9   PHE B CD2 1 
ATOM   2925 C  CE1 . PHE B 1 29  ? -5.23300  14.53500  -44.25300 1.000 46.38917 ?  9   PHE B CE1 1 
ATOM   2926 C  CE2 . PHE B 1 29  ? -6.22200  13.68300  -42.27000 1.000 47.79989 ?  9   PHE B CE2 1 
ATOM   2927 C  CZ  . PHE B 1 29  ? -5.87700  13.52000  -43.58900 1.000 45.64628 ?  9   PHE B CZ  1 
ATOM   2928 N  N   . HIS B 1 30  ? -7.43200  17.94400  -39.67700 1.000 52.23387 ?  10  HIS B N   1 
ATOM   2929 C  CA  . HIS B 1 30  ? -8.69700  17.55600  -39.00500 1.000 55.75704 ?  10  HIS B CA  1 
ATOM   2930 C  C   . HIS B 1 30  ? -9.81700  18.54000  -39.37700 1.000 52.96506 ?  10  HIS B C   1 
ATOM   2931 O  O   . HIS B 1 30  ? -10.95300 18.08700  -39.50900 1.000 50.81508 ?  10  HIS B O   1 
ATOM   2932 C  CB  . HIS B 1 30  ? -8.50300  17.43100  -37.48900 1.000 53.82475 ?  10  HIS B CB  1 
ATOM   2933 C  CG  . HIS B 1 30  ? -7.45500  16.46700  -37.05600 1.000 59.53529 ?  10  HIS B CG  1 
ATOM   2934 N  ND1 . HIS B 1 30  ? -6.95800  15.46400  -37.85600 1.000 59.61083 ?  10  HIS B ND1 1 
ATOM   2935 C  CD2 . HIS B 1 30  ? -6.81000  16.36600  -35.88900 1.000 58.93715 ?  10  HIS B CD2 1 
ATOM   2936 C  CE1 . HIS B 1 30  ? -6.04300  14.78500  -37.18100 1.000 60.14296 ?  10  HIS B CE1 1 
ATOM   2937 N  NE2 . HIS B 1 30  ? -5.93900  15.31400  -35.98300 1.000 56.68278 ?  10  HIS B NE2 1 
ATOM   2938 N  N   . VAL B 1 31  ? -9.51600  19.83200  -39.52800 1.000 52.11084 ?  11  VAL B N   1 
ATOM   2939 C  CA  . VAL B 1 31  ? -10.59000 20.78800  -39.79200 1.000 54.91862 ?  11  VAL B CA  1 
ATOM   2940 C  C   . VAL B 1 31  ? -10.90400 20.86000  -41.28300 1.000 56.97761 ?  11  VAL B C   1 
ATOM   2941 O  O   . VAL B 1 31  ? -12.07300 20.94300  -41.67800 1.000 57.55541 ?  11  VAL B O   1 
ATOM   2942 C  CB  . VAL B 1 31  ? -10.24600 22.17200  -39.20400 1.000 52.55947 ?  11  VAL B CB  1 
ATOM   2943 C  CG1 . VAL B 1 31  ? -11.29200 23.21700  -39.57000 1.000 58.45898 ?  11  VAL B CG1 1 
ATOM   2944 C  CG2 . VAL B 1 31  ? -10.08900 22.07500  -37.69500 1.000 61.24615 ?  11  VAL B CG2 1 
ATOM   2945 N  N   . ASP B 1 32  ? -9.88100  20.81700  -42.13100 1.000 58.12308 ?  12  ASP B N   1 
ATOM   2946 C  CA  . ASP B 1 32  ? -10.06300 20.74500  -43.57400 1.000 57.95785 ?  12  ASP B CA  1 
ATOM   2947 C  C   . ASP B 1 32  ? -8.80900  20.15500  -44.20800 1.000 58.42220 ?  12  ASP B C   1 
ATOM   2948 O  O   . ASP B 1 32  ? -7.79100  20.84600  -44.33800 1.000 59.52221 ?  12  ASP B O   1 
ATOM   2949 C  CB  . ASP B 1 32  ? -10.36500 22.12000  -44.17500 1.000 54.43800 ?  12  ASP B CB  1 
ATOM   2950 C  CG  . ASP B 1 32  ? -10.92300 22.02700  -45.58700 1.000 60.90598 ?  12  ASP B CG  1 
ATOM   2951 O  OD1 . ASP B 1 32  ? -11.06200 20.89400  -46.09900 1.000 56.67504 ?  12  ASP B OD1 1 
ATOM   2952 O  OD2 . ASP B 1 32  ? -11.20500 23.08100  -46.19600 1.000 64.98925 -1 12  ASP B OD2 1 
ATOM   2953 N  N   . PRO B 1 33  ? -8.84500  18.88200  -44.61100 1.000 60.40158 ?  13  PRO B N   1 
ATOM   2954 C  CA  . PRO B 1 33  ? -7.68600  18.26600  -45.26400 1.000 51.85244 ?  13  PRO B CA  1 
ATOM   2955 C  C   . PRO B 1 33  ? -7.56000  18.53100  -46.75900 1.000 56.36967 ?  13  PRO B C   1 
ATOM   2956 O  O   . PRO B 1 33  ? -6.48200  18.29200  -47.31800 1.000 55.96034 ?  13  PRO B O   1 
ATOM   2957 C  CB  . PRO B 1 33  ? -7.93300  16.77500  -45.01600 1.000 51.22327 ?  13  PRO B CB  1 
ATOM   2958 C  CG  . PRO B 1 33  ? -9.41700  16.66400  -45.10300 1.000 55.92617 ?  13  PRO B CG  1 
ATOM   2959 C  CD  . PRO B 1 33  ? -9.94500  17.91900  -44.43500 1.000 57.43081 ?  13  PRO B CD  1 
ATOM   2960 N  N   . TYR B 1 34  ? -8.62500  18.99100  -47.41700 1.000 51.38720 ?  14  TYR B N   1 
ATOM   2961 C  CA  . TYR B 1 34  ? -8.66100  19.12900  -48.87000 1.000 52.34621 ?  14  TYR B CA  1 
ATOM   2962 C  C   . TYR B 1 34  ? -7.70900  20.20200  -49.39800 1.000 54.66710 ?  14  TYR B C   1 
ATOM   2963 C  CB  . TYR B 1 34  ? -10.09800 19.39800  -49.32100 1.000 48.90395 ?  14  TYR B CB  1 
ATOM   2964 C  CG  . TYR B 1 34  ? -10.97500 18.17700  -49.17800 1.000 50.85249 ?  14  TYR B CG  1 
ATOM   2965 C  CD1 . TYR B 1 34  ? -10.80700 17.08400  -50.01700 1.000 48.59273 ?  14  TYR B CD1 1 
ATOM   2966 C  CD2 . TYR B 1 34  ? -11.95200 18.10600  -48.19400 1.000 55.17400 ?  14  TYR B CD2 1 
ATOM   2967 C  CE1 . TYR B 1 34  ? -11.58800 15.95800  -49.88700 1.000 48.38313 ?  14  TYR B CE1 1 
ATOM   2968 C  CE2 . TYR B 1 34  ? -12.74600 16.98000  -48.05700 1.000 50.34697 ?  14  TYR B CE2 1 
ATOM   2969 C  CZ  . TYR B 1 34  ? -12.55800 15.90900  -48.90700 1.000 49.21156 ?  14  TYR B CZ  1 
ATOM   2970 O  OH  . TYR B 1 34  ? -13.33300 14.77900  -48.78900 1.000 47.20725 ?  14  TYR B OH  1 
ATOM   2971 N  N   . PRO B 1 35  ? -7.46600  21.30100  -48.67100 1.000 58.65801 ?  15  PRO B N   1 
ATOM   2972 C  CA  . PRO B 1 35  ? -6.33300  22.16400  -49.04600 1.000 58.10917 ?  15  PRO B CA  1 
ATOM   2973 C  C   . PRO B 1 35  ? -5.00800  21.42300  -49.12600 1.000 63.41656 ?  15  PRO B C   1 
ATOM   2974 O  O   . PRO B 1 35  ? -4.31500  21.51000  -50.14800 1.000 61.78152 ?  15  PRO B O   1 
ATOM   2975 C  CB  . PRO B 1 35  ? -6.33300  23.21600  -47.93300 1.000 63.32188 ?  15  PRO B CB  1 
ATOM   2976 C  CG  . PRO B 1 35  ? -7.76600  23.38700  -47.61700 1.000 60.92710 ?  15  PRO B CG  1 
ATOM   2977 C  CD  . PRO B 1 35  ? -8.39800  22.01500  -47.77400 1.000 62.63915 ?  15  PRO B CD  1 
ATOM   2978 N  N   . ILE B 1 36  ? -4.63500  20.69700  -48.06800 1.000 57.68244 ?  16  ILE B N   1 
ATOM   2979 C  CA  . ILE B 1 36  ? -3.37400  19.96000  -48.07100 1.000 53.41221 ?  16  ILE B CA  1 
ATOM   2980 C  C   . ILE B 1 36  ? -3.35600  18.93700  -49.20000 1.000 50.53104 ?  16  ILE B C   1 
ATOM   2981 O  O   . ILE B 1 36  ? -2.32800  18.73700  -49.86000 1.000 55.03817 ?  16  ILE B O   1 
ATOM   2982 C  CB  . ILE B 1 36  ? -3.13900  19.29800  -46.70000 1.000 55.69194 ?  16  ILE B CB  1 
ATOM   2983 N  N   . TYR B 1 37  ? -4.49200  18.27700  -49.44400 1.000 54.61574 ?  17  TYR B N   1 
ATOM   2984 C  CA  . TYR B 1 37  ? -4.59300  17.34700  -50.56500 1.000 49.59321 ?  17  TYR B CA  1 
ATOM   2985 C  C   . TYR B 1 37  ? -4.27500  18.03400  -51.88700 1.000 55.93946 ?  17  TYR B C   1 
ATOM   2986 O  O   . TYR B 1 37  ? -3.68000  17.42600  -52.78300 1.000 52.26943 ?  17  TYR B O   1 
ATOM   2987 C  CB  . TYR B 1 37  ? -5.99700  16.74500  -50.63200 1.000 51.58577 ?  17  TYR B CB  1 
ATOM   2988 C  CG  . TYR B 1 37  ? -6.34500  15.75100  -49.54800 1.000 44.95820 ?  17  TYR B CG  1 
ATOM   2989 C  CD1 . TYR B 1 37  ? -5.37100  14.97100  -48.93800 1.000 44.12996 ?  17  TYR B CD1 1 
ATOM   2990 C  CD2 . TYR B 1 37  ? -7.66600  15.58100  -49.15000 1.000 48.93583 ?  17  TYR B CD2 1 
ATOM   2991 C  CE1 . TYR B 1 37  ? -5.70700  14.05700  -47.95000 1.000 45.68382 ?  17  TYR B CE1 1 
ATOM   2992 C  CE2 . TYR B 1 37  ? -8.00900  14.67800  -48.17100 1.000 41.40462 ?  17  TYR B CE2 1 
ATOM   2993 C  CZ  . TYR B 1 37  ? -7.03100  13.91800  -47.57300 1.000 45.52502 ?  17  TYR B CZ  1 
ATOM   2994 O  OH  . TYR B 1 37  ? -7.38600  13.01900  -46.59600 1.000 39.63325 ?  17  TYR B OH  1 
ATOM   2995 N  N   . ALA B 1 38  ? -4.67800  19.30100  -52.02900 1.000 56.63949 ?  18  ALA B N   1 
ATOM   2996 C  CA  . ALA B 1 38  ? -4.49700  20.00800  -53.29400 1.000 58.71909 ?  18  ALA B CA  1 
ATOM   2997 C  C   . ALA B 1 38  ? -3.02000  20.17700  -53.62700 1.000 55.61903 ?  18  ALA B C   1 
ATOM   2998 O  O   . ALA B 1 38  ? -2.59500  19.92700  -54.76200 1.000 53.23204 ?  18  ALA B O   1 
ATOM   2999 C  CB  . ALA B 1 38  ? -5.20100  21.36400  -53.24000 1.000 58.29473 ?  18  ALA B CB  1 
ATOM   3000 N  N   . ARG B 1 39  ? -2.22000  20.60700  -52.64700 1.000 62.26099 ?  19  ARG B N   1 
ATOM   3001 C  CA  . ARG B 1 39  ? -0.78100  20.73000  -52.86800 1.000 61.93600 ?  19  ARG B CA  1 
ATOM   3002 C  C   . ARG B 1 39  ? -0.15600  19.37700  -53.18500 1.000 61.06613 ?  19  ARG B C   1 
ATOM   3003 O  O   . ARG B 1 39  ? 0.70600   19.27400  -54.06800 1.000 59.43217 ?  19  ARG B O   1 
ATOM   3004 N  N   . LEU B 1 40  ? -0.58100  18.32600  -52.47800 1.000 54.95540 ?  20  LEU B N   1 
ATOM   3005 C  CA  . LEU B 1 40  ? -0.04100  16.99100  -52.72200 1.000 53.48037 ?  20  LEU B CA  1 
ATOM   3006 C  C   . LEU B 1 40  ? -0.34700  16.52600  -54.14000 1.000 54.68540 ?  20  LEU B C   1 
ATOM   3007 O  O   . LEU B 1 40  ? 0.52900   15.99900  -54.83500 1.000 53.21641 ?  20  LEU B O   1 
ATOM   3008 C  CB  . LEU B 1 40  ? -0.59900  16.00400  -51.69600 1.000 36.73048 ?  20  LEU B CB  1 
ATOM   3009 N  N   . ARG B 1 41  ? -1.58900  16.72100  -54.59000 1.000 47.62100 ?  21  ARG B N   1 
ATOM   3010 C  CA  . ARG B 1 41  ? -1.96200  16.31500  -55.94200 1.000 50.64746 ?  21  ARG B CA  1 
ATOM   3011 C  C   . ARG B 1 41  ? -1.18500  17.10600  -56.98400 1.000 57.27925 ?  21  ARG B C   1 
ATOM   3012 O  O   . ARG B 1 41  ? -0.63000  16.53600  -57.93000 1.000 55.39784 ?  21  ARG B O   1 
ATOM   3013 C  CB  . ARG B 1 41  ? -3.46600  16.49300  -56.14700 1.000 51.74790 ?  21  ARG B CB  1 
ATOM   3014 C  CG  . ARG B 1 41  ? -4.31600  15.57400  -55.29700 1.000 44.12648 ?  21  ARG B CG  1 
ATOM   3015 N  N   . ALA B 1 42  ? -1.21500  18.42600  -56.80600 1.000 54.11846 ?  22  ALA B N   1 
ATOM   3016 C  C   . ALA B 1 42  ? 1.38400   19.22900  -57.84400 1.000 57.50596 ?  22  ALA B C   1 
ATOM   3017 O  O   . ALA B 1 42  ? 1.61600   18.55900  -58.86400 1.000 53.65128 ?  22  ALA B O   1 
ATOM   3018 N  N   . GLY B 1 43  ? 1.77700   18.88500  -56.61100 1.000 57.72525 ?  23  GLY B N   1 
ATOM   3019 C  CA  . GLY B 1 43  ? 3.13500   18.40900  -56.28900 1.000 54.71404 ?  23  GLY B CA  1 
ATOM   3020 C  C   . GLY B 1 43  ? 3.49600   17.04000  -56.84200 1.000 56.81643 ?  23  GLY B C   1 
ATOM   3021 O  O   . GLY B 1 43  ? 4.60600   16.58200  -56.53300 1.000 58.30598 ?  23  GLY B O   1 
ATOM   3022 N  N   . GLY B 1 44  ? 2.62800   16.40500  -57.62900 1.000 51.65847 ?  24  GLY B N   1 
ATOM   3023 C  CA  . GLY B 1 44  ? 2.99900   15.12400  -58.25000 1.000 55.44436 ?  24  GLY B CA  1 
ATOM   3024 C  C   . GLY B 1 44  ? 2.05900   14.00900  -57.81700 1.000 55.53188 ?  24  GLY B C   1 
ATOM   3025 O  O   . GLY B 1 44  ? 1.91200   13.04000  -58.57200 1.000 52.00746 ?  24  GLY B O   1 
ATOM   3026 N  N   . GLY B 1 45  ? 1.45600   14.14100  -56.63300 1.000 56.01436 ?  25  GLY B N   1 
ATOM   3027 C  CA  . GLY B 1 45  ? 0.50800   13.12700  -56.13900 1.000 53.54098 ?  25  GLY B CA  1 
ATOM   3028 C  C   . GLY B 1 45  ? 1.18500   11.98300  -55.41000 1.000 52.43417 ?  25  GLY B C   1 
ATOM   3029 O  O   . GLY B 1 45  ? 0.48100   11.07000  -54.96900 1.000 50.17220 ?  25  GLY B O   1 
ATOM   3030 N  N   . ILE B 1 46  ? 2.50400   12.01700  -55.31000 1.000 48.23857 ?  26  ILE B N   1 
ATOM   3031 C  CA  . ILE B 1 46  ? 3.23000   10.99800  -54.56000 1.000 45.52683 ?  26  ILE B CA  1 
ATOM   3032 C  C   . ILE B 1 46  ? 4.32600   11.67300  -53.74700 1.000 49.07660 ?  26  ILE B C   1 
ATOM   3033 O  O   . ILE B 1 46  ? 5.06900   12.51400  -54.26500 1.000 54.50261 ?  26  ILE B O   1 
ATOM   3034 C  CB  . ILE B 1 46  ? 3.81500   9.90100   -55.47700 1.000 44.11515 ?  26  ILE B CB  1 
ATOM   3035 C  CG1 . ILE B 1 46  ? 4.45300   8.78500   -54.63800 1.000 45.79923 ?  26  ILE B CG1 1 
ATOM   3036 C  CG2 . ILE B 1 46  ? 4.76400   10.48600  -56.51900 1.000 46.55678 ?  26  ILE B CG2 1 
ATOM   3037 C  CD1 . ILE B 1 46  ? 4.43500   7.42900   -55.28900 1.000 47.25720 ?  26  ILE B CD1 1 
ATOM   3038 N  N   . ARG B 1 47  ? 4.41100   11.31800  -52.46800 1.000 47.63987 ?  27  ARG B N   1 
ATOM   3039 C  CA  . ARG B 1 47  ? 5.38700   11.90200  -51.56200 1.000 43.23872 ?  27  ARG B CA  1 
ATOM   3040 C  C   . ARG B 1 47  ? 5.46200   11.01900  -50.32500 1.000 47.86333 ?  27  ARG B C   1 
ATOM   3041 O  O   . ARG B 1 47  ? 4.43400   10.54900  -49.83300 1.000 43.41810 ?  27  ARG B O   1 
ATOM   3042 C  CB  . ARG B 1 47  ? 5.00600   13.34300  -51.19100 1.000 46.83991 ?  27  ARG B CB  1 
ATOM   3043 C  CG  . ARG B 1 47  ? 5.39700   13.77300  -49.78800 1.000 51.16829 ?  27  ARG B CG  1 
ATOM   3044 C  CD  . ARG B 1 47  ? 5.38600   15.28800  -49.66500 1.000 50.58309 ?  27  ARG B CD  1 
ATOM   3045 N  N   . GLN B 1 48  ? 6.67800   10.78000  -49.84200 1.000 41.43067 ?  28  GLN B N   1 
ATOM   3046 C  CA  . GLN B 1 48  ? 6.88900   9.96600   -48.65100 1.000 41.41740 ?  28  GLN B CA  1 
ATOM   3047 C  C   . GLN B 1 48  ? 6.86300   10.87900  -47.42800 1.000 44.21798 ?  28  GLN B C   1 
ATOM   3048 O  O   . GLN B 1 48  ? 7.76600   11.70100  -47.23700 1.000 53.58648 ?  28  GLN B O   1 
ATOM   3049 C  CB  . GLN B 1 48  ? 8.20400   9.19800   -48.75000 1.000 42.30203 ?  28  GLN B CB  1 
ATOM   3050 C  CG  . GLN B 1 48  ? 8.47600   8.28700   -47.56200 1.000 44.04513 ?  28  GLN B CG  1 
ATOM   3051 C  CD  . GLN B 1 48  ? 9.87400   7.69900   -47.57300 1.000 47.45248 ?  28  GLN B CD  1 
ATOM   3052 O  OE1 . GLN B 1 48  ? 10.84200  8.36700   -47.21300 1.000 45.71499 ?  28  GLN B OE1 1 
ATOM   3053 N  NE2 . GLN B 1 48  ? 9.98500   6.44000   -47.98300 1.000 46.63575 ?  28  GLN B NE2 1 
ATOM   3054 N  N   . VAL B 1 49  ? 5.82500   10.73800  -46.60300 1.000 37.73016 ?  29  VAL B N   1 
ATOM   3055 C  CA  . VAL B 1 49  ? 5.65600   11.55700  -45.40700 1.000 37.66493 ?  29  VAL B CA  1 
ATOM   3056 C  C   . VAL B 1 49  ? 6.27200   10.84300  -44.21300 1.000 39.17202 ?  29  VAL B C   1 
ATOM   3057 O  O   . VAL B 1 49  ? 6.56900   9.64800   -44.28200 1.000 45.73533 ?  29  VAL B O   1 
ATOM   3058 C  CB  . VAL B 1 49  ? 4.17100   11.86700  -45.15500 1.000 44.31036 ?  29  VAL B CB  1 
ATOM   3059 C  CG1 . VAL B 1 49  ? 3.60700   12.70800  -46.29200 1.000 43.59455 ?  29  VAL B CG1 1 
ATOM   3060 C  CG2 . VAL B 1 49  ? 3.38000   10.58300  -44.99000 1.000 37.23961 ?  29  VAL B CG2 1 
ATOM   3061 N  N   . SER B 1 50  ? 6.49200   11.58700  -43.13600 1.000 47.97451 ?  30  SER B N   1 
ATOM   3062 C  CA  . SER B 1 50  ? 7.11600   11.01000  -41.92400 1.000 44.57561 ?  30  SER B CA  1 
ATOM   3063 C  C   . SER B 1 50  ? 6.48200   11.61300  -40.67500 1.000 48.69187 ?  30  SER B C   1 
ATOM   3064 O  O   . SER B 1 50  ? 6.21000   12.81600  -40.67900 1.000 54.39624 ?  30  SER B O   1 
ATOM   3065 C  CB  . SER B 1 50  ? 8.59700   11.21700  -41.90600 1.000 44.08568 ?  30  SER B CB  1 
ATOM   3066 O  OG  . SER B 1 50  ? 8.91000   12.50500  -41.40400 1.000 51.50213 ?  30  SER B OG  1 
ATOM   3067 N  N   . THR B 1 51  ? 6.26700   10.79100  -39.65600 1.000 46.54697 ?  31  THR B N   1 
ATOM   3068 C  CA  . THR B 1 51  ? 5.72000   11.27900  -38.36700 1.000 48.06175 ?  31  THR B CA  1 
ATOM   3069 C  C   . THR B 1 51  ? 6.83400   11.91500  -37.54400 1.000 48.98298 ?  31  THR B C   1 
ATOM   3070 O  O   . THR B 1 51  ? 8.00000   11.74000  -37.90400 1.000 41.36413 ?  31  THR B O   1 
ATOM   3071 C  CB  . THR B 1 51  ? 5.14100   10.11300  -37.55800 1.000 45.18372 ?  31  THR B CB  1 
ATOM   3072 O  OG1 . THR B 1 51  ? 6.20200   9.20800   -37.25800 1.000 47.33827 ?  31  THR B OG1 1 
ATOM   3073 C  CG2 . THR B 1 51  ? 4.01800   9.40500   -38.28000 1.000 44.19792 ?  31  THR B CG2 1 
ATOM   3074 N  N   . PRO B 1 52  ? 6.52200   12.63300  -36.44700 1.000 52.26887 ?  32  PRO B N   1 
ATOM   3075 C  CA  . PRO B 1 52  ? 7.55800   13.13700  -35.55500 1.000 47.43726 ?  32  PRO B CA  1 
ATOM   3076 C  C   . PRO B 1 52  ? 8.30700   12.03700  -34.78700 1.000 50.90292 ?  32  PRO B C   1 
ATOM   3077 O  O   . PRO B 1 52  ? 9.18600   12.37900  -34.04100 1.000 53.62206 ?  32  PRO B O   1 
ATOM   3078 C  CB  . PRO B 1 52  ? 6.79000   14.01700  -34.55700 1.000 48.23204 ?  32  PRO B CB  1 
ATOM   3079 C  CG  . PRO B 1 52  ? 5.37500   13.50200  -34.61600 1.000 51.85069 ?  32  PRO B CG  1 
ATOM   3080 C  CD  . PRO B 1 52  ? 5.18600   13.09400  -36.06000 1.000 48.44166 ?  32  PRO B CD  1 
ATOM   3081 N  N   . ASP B 1 53  ? 7.95800   10.76800  -34.99900 1.000 47.19307 ?  33  ASP B N   1 
ATOM   3082 C  CA  . ASP B 1 53  ? 8.66000   9.65300   -34.31400 1.000 47.48327 ?  33  ASP B CA  1 
ATOM   3083 C  C   . ASP B 1 53  ? 9.54300   8.89400   -35.31000 1.000 36.66531 ?  33  ASP B C   1 
ATOM   3084 O  O   . ASP B 1 53  ? 10.33500  8.07200   -34.86600 1.000 43.32453 ?  33  ASP B O   1 
ATOM   3085 C  CB  . ASP B 1 53  ? 7.68200   8.70500   -33.61200 1.000 47.58216 ?  33  ASP B CB  1 
ATOM   3086 C  CG  . ASP B 1 53  ? 8.09300   8.34800   -32.19600 1.000 41.38011 ?  33  ASP B CG  1 
ATOM   3087 N  N   . GLY B 1 54  ? 9.38300   9.15700   -36.60000 1.000 42.54629 ?  34  GLY B N   1 
ATOM   3088 C  CA  . GLY B 1 54  ? 10.17300  8.47500   -37.60500 1.000 35.82890 ?  34  GLY B CA  1 
ATOM   3089 C  C   . GLY B 1 54  ? 9.40000   7.53400   -38.50300 1.000 36.11636 ?  34  GLY B C   1 
ATOM   3090 O  O   . GLY B 1 54  ? 10.00200  6.95000   -39.41100 1.000 32.30646 ?  34  GLY B O   1 
ATOM   3091 N  N   . ALA B 1 55  ? 8.09500   7.37100   -38.28900 1.000 34.12410 ?  35  ALA B N   1 
ATOM   3092 C  CA  . ALA B 1 55  ? 7.28800   6.47200   -39.10300 1.000 36.69814 ?  35  ALA B CA  1 
ATOM   3093 C  C   . ALA B 1 55  ? 6.98500   7.10500   -40.45600 1.000 36.38838 ?  35  ALA B C   1 
ATOM   3094 O  O   . ALA B 1 55  ? 6.43800   8.21100   -40.52500 1.000 39.77658 ?  35  ALA B O   1 
ATOM   3095 C  CB  . ALA B 1 55  ? 5.98500   6.12700   -38.37900 1.000 34.70803 ?  35  ALA B CB  1 
ATOM   3096 N  N   . ALA B 1 56  ? 7.31800   6.39600   -41.53000 1.000 29.74815 ?  36  ALA B N   1 
ATOM   3097 C  CA  . ALA B 1 56  ? 7.20500   6.92600   -42.88000 1.000 32.13587 ?  36  ALA B CA  1 
ATOM   3098 C  C   . ALA B 1 56  ? 6.19500   6.13400   -43.70200 1.000 36.00969 ?  36  ALA B C   1 
ATOM   3099 O  O   . ALA B 1 56  ? 5.98300   4.93700   -43.47900 1.000 31.71852 ?  36  ALA B O   1 
ATOM   3100 C  CB  . ALA B 1 56  ? 8.56200   6.92000   -43.59100 1.000 35.25673 ?  36  ALA B CB  1 
ATOM   3101 N  N   . ALA B 1 57  ? 5.58000   6.81700   -44.66500 1.000 28.22481 ?  37  ALA B N   1 
ATOM   3102 C  CA  . ALA B 1 57  ? 4.65500   6.17500   -45.58800 1.000 34.08111 ?  37  ALA B CA  1 
ATOM   3103 C  C   . ALA B 1 57  ? 4.55700   7.01300   -46.85200 1.000 28.57400 ?  37  ALA B C   1 
ATOM   3104 O  O   . ALA B 1 57  ? 4.86100   8.20800   -46.85400 1.000 37.18642 ?  37  ALA B O   1 
ATOM   3105 C  CB  . ALA B 1 57  ? 3.26900   5.98400   -44.96300 1.000 36.14014 ?  37  ALA B CB  1 
ATOM   3106 N  N   . TRP B 1 58  ? 4.11600   6.35800   -47.91400 1.000 32.39981 ?  38  TRP B N   1 
ATOM   3107 C  CA  . TRP B 1 58  ? 3.88200   7.04800   -49.19600 1.000 32.00787 ?  38  TRP B CA  1 
ATOM   3108 C  C   . TRP B 1 58  ? 2.40500   7.42200   -49.25900 1.000 38.50249 ?  38  TRP B C   1 
ATOM   3109 O  O   . TRP B 1 58  ? 1.57200   6.52000   -49.11100 1.000 38.22896 ?  38  TRP B O   1 
ATOM   3110 C  CB  . TRP B 1 58  ? 4.24900   6.13700   -50.36200 1.000 29.37852 ?  38  TRP B CB  1 
ATOM   3111 C  CG  . TRP B 1 58  ? 5.69100   5.74500   -50.38200 1.000 36.47533 ?  38  TRP B CG  1 
ATOM   3112 C  CD1 . TRP B 1 58  ? 6.27500   4.72300   -49.69600 1.000 34.56709 ?  38  TRP B CD1 1 
ATOM   3113 C  CD2 . TRP B 1 58  ? 6.74100   6.37800   -51.13000 1.000 40.65661 ?  38  TRP B CD2 1 
ATOM   3114 N  NE1 . TRP B 1 58  ? 7.61300   4.67700   -49.96500 1.000 40.30994 ?  38  TRP B NE1 1 
ATOM   3115 C  CE2 . TRP B 1 58  ? 7.92900   5.67600   -50.84400 1.000 41.96295 ?  38  TRP B CE2 1 
ATOM   3116 C  CE3 . TRP B 1 58  ? 6.79300   7.46000   -52.01200 1.000 40.96980 ?  38  TRP B CE3 1 
ATOM   3117 C  CZ2 . TRP B 1 58  ? 9.15500   6.02500   -51.40600 1.000 43.02380 ?  38  TRP B CZ2 1 
ATOM   3118 C  CZ3 . TRP B 1 58  ? 8.00400   7.80400   -52.56900 1.000 42.45389 ?  38  TRP B CZ3 1 
ATOM   3119 C  CH2 . TRP B 1 58  ? 9.16600   7.09500   -52.26800 1.000 41.54177 ?  38  TRP B CH2 1 
ATOM   3120 N  N   . VAL B 1 59  ? 2.10900   8.70000   -49.47200 1.000 39.22411 ?  39  VAL B N   1 
ATOM   3121 C  CA  . VAL B 1 59  ? 0.69300   9.12900   -49.63500 1.000 33.97935 ?  39  VAL B CA  1 
ATOM   3122 C  C   . VAL B 1 59  ? 0.42400   9.34500   -51.12600 1.000 36.65880 ?  39  VAL B C   1 
ATOM   3123 O  O   . VAL B 1 59  ? 1.10100   10.17000  -51.73000 1.000 45.36491 ?  39  VAL B O   1 
ATOM   3124 C  CB  . VAL B 1 59  ? 0.38600   10.36400  -48.77100 1.000 34.58903 ?  39  VAL B CB  1 
ATOM   3125 C  CG1 . VAL B 1 59  ? 0.25100   9.99400   -47.30500 1.000 29.12500 ?  39  VAL B CG1 1 
ATOM   3126 C  CG2 . VAL B 1 59  ? 1.41600   11.46700  -48.94600 1.000 33.87503 ?  39  VAL B CG2 1 
ATOM   3127 N  N   . VAL B 1 60  ? -0.50200  8.58100   -51.69700 1.000 35.12509 ?  40  VAL B N   1 
ATOM   3128 C  CA  . VAL B 1 60  ? -0.87100  8.69900   -53.13100 1.000 34.91649 ?  40  VAL B CA  1 
ATOM   3129 C  C   . VAL B 1 60  ? -2.17400  9.49800   -53.15200 1.000 43.38525 ?  40  VAL B C   1 
ATOM   3130 O  O   . VAL B 1 60  ? -3.11900  9.07100   -52.47700 1.000 35.98253 ?  40  VAL B O   1 
ATOM   3131 C  CB  . VAL B 1 60  ? -0.98700  7.30500   -53.76400 1.000 29.43195 ?  40  VAL B CB  1 
ATOM   3132 C  CG1 . VAL B 1 60  ? -1.51200  7.34500   -55.18400 1.000 40.03175 ?  40  VAL B CG1 1 
ATOM   3133 C  CG2 . VAL B 1 60  ? 0.32200   6.53900   -53.68100 1.000 36.82342 ?  40  VAL B CG2 1 
ATOM   3134 N  N   . THR B 1 61  ? -2.23600  10.59000  -53.91600 1.000 39.25004 ?  41  THR B N   1 
ATOM   3135 C  CA  . THR B 1 61  ? -3.40500  11.49700  -53.77900 1.000 41.02563 ?  41  THR B CA  1 
ATOM   3136 C  C   . THR B 1 61  ? -4.18500  11.69400  -55.08000 1.000 44.90359 ?  41  THR B C   1 
ATOM   3137 O  O   . THR B 1 61  ? -5.25100  12.31600  -55.00800 1.000 43.06853 ?  41  THR B O   1 
ATOM   3138 C  CB  . THR B 1 61  ? -2.91800  12.81300  -53.17300 1.000 41.54611 ?  41  THR B CB  1 
ATOM   3139 O  OG1 . THR B 1 61  ? -1.78200  13.25500  -53.91400 1.000 47.83539 ?  41  THR B OG1 1 
ATOM   3140 C  CG2 . THR B 1 61  ? -2.55700  12.68100  -51.71000 1.000 44.28555 ?  41  THR B CG2 1 
ATOM   3141 N  N   . ARG B 1 62  ? -3.67400  11.15700  -56.19600 1.000 45.43653 ?  42  ARG B N   1 
ATOM   3142 C  CA  . ARG B 1 62  ? -4.31800  11.36400  -57.52400 1.000 41.36385 ?  42  ARG B CA  1 
ATOM   3143 C  C   . ARG B 1 62  ? -5.29000  10.22200  -57.83600 1.000 39.26348 ?  42  ARG B C   1 
ATOM   3144 O  O   . ARG B 1 62  ? -4.93400  9.06000   -57.57100 1.000 42.97740 ?  42  ARG B O   1 
ATOM   3145 C  CB  . ARG B 1 62  ? -3.25000  11.51100  -58.61100 1.000 49.95686 ?  42  ARG B CB  1 
ATOM   3146 C  CG  . ARG B 1 62  ? -2.38200  12.75000  -58.44200 1.000 55.53110 ?  42  ARG B CG  1 
ATOM   3147 C  CD  . ARG B 1 62  ? -1.42400  12.96900  -59.59600 1.000 63.15237 ?  42  ARG B CD  1 
ATOM   3148 N  NE  . ARG B 1 62  ? -0.96600  14.34900  -59.66200 1.000 55.64224 ?  42  ARG B NE  1 
ATOM   3149 C  CZ  . ARG B 1 62  ? 0.00800   14.78100  -60.45400 1.000 61.73618 ?  42  ARG B CZ  1 
ATOM   3150 N  NH1 . ARG B 1 62  ? 0.70400   13.92100  -61.17700 1.000 61.50225 ?  42  ARG B NH1 1 
ATOM   3151 N  NH2 . ARG B 1 62  ? 0.29200   16.07000  -60.50900 1.000 62.19689 ?  42  ARG B NH2 1 
ATOM   3152 N  N   . TYR B 1 63  ? -6.44000  10.54400  -58.43000 1.000 41.86659 ?  43  TYR B N   1 
ATOM   3153 C  CA  . TYR B 1 63  ? -7.48500  9.56000   -58.71200 1.000 38.88239 ?  43  TYR B CA  1 
ATOM   3154 C  C   . TYR B 1 63  ? -6.95900  8.35000   -59.47400 1.000 43.00854 ?  43  TYR B C   1 
ATOM   3155 O  O   . TYR B 1 63  ? -7.09000  7.20700   -59.02000 1.000 41.59394 ?  43  TYR B O   1 
ATOM   3156 C  CB  . TYR B 1 63  ? -8.61800  10.23900  -59.49000 1.000 44.68238 ?  43  TYR B CB  1 
ATOM   3157 C  CG  . TYR B 1 63  ? -9.82100  9.36500   -59.80100 1.000 42.22521 ?  43  TYR B CG  1 
ATOM   3158 C  CD1 . TYR B 1 63  ? -9.77900  8.42900   -60.83000 1.000 43.91270 ?  43  TYR B CD1 1 
ATOM   3159 C  CD2 . TYR B 1 63  ? -11.00300 9.48900   -59.08000 1.000 46.60636 ?  43  TYR B CD2 1 
ATOM   3160 C  CE1 . TYR B 1 63  ? -10.86900 7.63600   -61.12400 1.000 41.53823 ?  43  TYR B CE1 1 
ATOM   3161 C  CE2 . TYR B 1 63  ? -12.10400 8.69600   -59.37100 1.000 42.67765 ?  43  TYR B CE2 1 
ATOM   3162 C  CZ  . TYR B 1 63  ? -12.02900 7.77300   -60.39400 1.000 41.28777 ?  43  TYR B CZ  1 
ATOM   3163 O  OH  . TYR B 1 63  ? -13.11500 6.98100   -60.69000 1.000 43.52907 ?  43  TYR B OH  1 
ATOM   3164 N  N   . ASP B 1 64  ? -6.38300  8.58500   -60.65700 1.000 42.50146 ?  44  ASP B N   1 
ATOM   3165 C  CA  . ASP B 1 64  ? -5.99300  7.47600   -61.52400 1.000 38.06495 ?  44  ASP B CA  1 
ATOM   3166 C  C   . ASP B 1 64  ? -5.01800  6.53600   -60.83500 1.000 38.89226 ?  44  ASP B C   1 
ATOM   3167 O  O   . ASP B 1 64  ? -5.04200  5.32500   -61.08200 1.000 42.13011 ?  44  ASP B O   1 
ATOM   3168 C  CB  . ASP B 1 64  ? -5.38700  8.01400   -62.81900 1.000 51.14563 ?  44  ASP B CB  1 
ATOM   3169 C  CG  . ASP B 1 64  ? -6.39500  8.76700   -63.66200 1.000 56.62231 ?  44  ASP B CG  1 
ATOM   3170 O  OD1 . ASP B 1 64  ? -6.60200  9.97400   -63.40800 1.000 62.92167 -1 44  ASP B OD1 1 
ATOM   3171 O  OD2 . ASP B 1 64  ? -6.98400  8.15200   -64.57500 1.000 64.22548 -1 44  ASP B OD2 1 
ATOM   3172 N  N   . ASP B 1 65  ? -4.15800  7.06900   -59.96800 1.000 43.69873 ?  45  ASP B N   1 
ATOM   3173 C  CA  . ASP B 1 65  ? -3.24600  6.21600   -59.21800 1.000 44.85566 ?  45  ASP B CA  1 
ATOM   3174 C  C   . ASP B 1 65  ? -3.97400  5.48900   -58.09500 1.000 37.64988 ?  45  ASP B C   1 
ATOM   3175 O  O   . ASP B 1 65  ? -3.78100  4.28400   -57.89900 1.000 39.79716 ?  45  ASP B O   1 
ATOM   3176 C  CB  . ASP B 1 65  ? -2.08800  7.04600   -58.66200 1.000 41.75044 ?  45  ASP B CB  1 
ATOM   3177 C  CG  . ASP B 1 65  ? -1.28200  7.72800   -59.75300 1.000 55.17831 ?  45  ASP B CG  1 
ATOM   3178 O  OD1 . ASP B 1 65  ? -0.88100  7.04200   -60.72100 1.000 45.08813 ?  45  ASP B OD1 1 
ATOM   3179 O  OD2 . ASP B 1 65  ? -1.05100  8.95100   -59.64200 1.000 52.85087 -1 45  ASP B OD2 1 
ATOM   3180 N  N   . VAL B 1 66  ? -4.81900  6.20600   -57.35100 1.000 42.18974 ?  46  VAL B N   1 
ATOM   3181 C  CA  . VAL B 1 66  ? -5.57900  5.57800   -56.27200 1.000 35.33643 ?  46  VAL B CA  1 
ATOM   3182 C  C   . VAL B 1 66  ? -6.46400  4.46900   -56.82700 1.000 35.17894 ?  46  VAL B C   1 
ATOM   3183 O  O   . VAL B 1 66  ? -6.44600  3.33500   -56.33600 1.000 40.02131 ?  46  VAL B O   1 
ATOM   3184 C  CB  . VAL B 1 66  ? -6.39900  6.63300   -55.50800 1.000 38.29627 ?  46  VAL B CB  1 
ATOM   3185 C  CG1 . VAL B 1 66  ? -7.34100  5.96400   -54.50900 1.000 28.43491 ?  46  VAL B CG1 1 
ATOM   3186 C  CG2 . VAL B 1 66  ? -5.46800  7.61000   -54.80200 1.000 35.49859 ?  46  VAL B CG2 1 
ATOM   3187 N  N   . ARG B 1 67  ? -7.23500  4.77500   -57.87500 1.000 36.27112 ?  47  ARG B N   1 
ATOM   3188 C  CA  . ARG B 1 67  ? -8.09400  3.76800   -58.49500 1.000 35.25264 ?  47  ARG B CA  1 
ATOM   3189 C  C   . ARG B 1 67  ? -7.29300  2.55600   -58.95500 1.000 33.65604 ?  47  ARG B C   1 
ATOM   3190 O  O   . ARG B 1 67  ? -7.68000  1.40900   -58.70200 1.000 36.94653 ?  47  ARG B O   1 
ATOM   3191 C  CB  . ARG B 1 67  ? -8.85100  4.37100   -59.67800 1.000 39.12755 ?  47  ARG B CB  1 
ATOM   3192 C  CG  . ARG B 1 67  ? -9.81200  3.38900   -60.33400 1.000 39.50270 ?  47  ARG B CG  1 
ATOM   3193 C  CD  . ARG B 1 67  ? -10.54800 4.01500   -61.50800 1.000 42.30484 ?  47  ARG B CD  1 
ATOM   3194 N  NE  . ARG B 1 67  ? -11.78400 3.31200   -61.83500 1.000 48.15166 ?  47  ARG B NE  1 
ATOM   3195 C  CZ  . ARG B 1 67  ? -11.86100 2.28000   -62.66500 1.000 51.54723 ?  47  ARG B CZ  1 
ATOM   3196 N  NH1 . ARG B 1 67  ? -10.77800 1.74100   -63.20100 1.000 55.83402 ?  47  ARG B NH1 1 
ATOM   3197 N  NH2 . ARG B 1 67  ? -13.05500 1.77000   -62.95900 1.000 46.68552 ?  47  ARG B NH2 1 
ATOM   3198 N  N   . ALA B 1 68  ? -6.18100  2.79000   -59.65300 1.000 34.30312 ?  48  ALA B N   1 
ATOM   3199 C  CA  . ALA B 1 68  ? -5.38800  1.67600   -60.16300 1.000 39.38709 ?  48  ALA B CA  1 
ATOM   3200 C  C   . ALA B 1 68  ? -4.72300  0.90300   -59.03000 1.000 37.48063 ?  48  ALA B C   1 
ATOM   3201 O  O   . ALA B 1 68  ? -4.61900  -0.32700  -59.08900 1.000 39.72675 ?  48  ALA B O   1 
ATOM   3202 C  CB  . ALA B 1 68  ? -4.34000  2.18500   -61.15200 1.000 37.08376 ?  48  ALA B CB  1 
ATOM   3203 N  N   . GLY B 1 69  ? -4.26200  1.60600   -57.99400 1.000 35.82060 ?  49  GLY B N   1 
ATOM   3204 C  CA  . GLY B 1 69  ? -3.64100  0.92000   -56.87300 1.000 37.84044 ?  49  GLY B CA  1 
ATOM   3205 C  C   . GLY B 1 69  ? -4.62500  0.08000   -56.08100 1.000 32.50113 ?  49  GLY B C   1 
ATOM   3206 O  O   . GLY B 1 69  ? -4.27400  -0.99000  -55.57800 1.000 39.25540 ?  49  GLY B O   1 
ATOM   3207 N  N   . LEU B 1 70  ? -5.87400  0.54700   -55.97100 1.000 33.30033 ?  50  LEU B N   1 
ATOM   3208 C  CA  . LEU B 1 70  ? -6.88400  -0.18300  -55.20900 1.000 39.09510 ?  50  LEU B CA  1 
ATOM   3209 C  C   . LEU B 1 70  ? -7.07500  -1.60000  -55.73200 1.000 40.17780 ?  50  LEU B C   1 
ATOM   3210 O  O   . LEU B 1 70  ? -7.42000  -2.50200  -54.96300 1.000 44.99321 ?  50  LEU B O   1 
ATOM   3211 C  CB  . LEU B 1 70  ? -8.21400  0.57500   -55.23900 1.000 31.18394 ?  50  LEU B CB  1 
ATOM   3212 C  CG  . LEU B 1 70  ? -8.35800  1.82700   -54.36800 1.000 31.45725 ?  50  LEU B CG  1 
ATOM   3213 C  CD1 . LEU B 1 70  ? -9.63400  2.57400   -54.72100 1.000 27.68090 ?  50  LEU B CD1 1 
ATOM   3214 C  CD2 . LEU B 1 70  ? -8.33600  1.47900   -52.88400 1.000 33.69279 ?  50  LEU B CD2 1 
ATOM   3215 N  N   . ALA B 1 71  ? -6.85100  -1.82000  -57.02900 1.000 38.89596 ?  51  ALA B N   1 
ATOM   3216 C  CA  . ALA B 1 71  ? -7.02600  -3.13100  -57.63300 1.000 40.39912 ?  51  ALA B CA  1 
ATOM   3217 C  C   . ALA B 1 71  ? -5.72200  -3.84500  -57.95200 1.000 45.72324 ?  51  ALA B C   1 
ATOM   3218 O  O   . ALA B 1 71  ? -5.73400  -5.07300  -58.08600 1.000 49.39404 ?  51  ALA B O   1 
ATOM   3219 C  CB  . ALA B 1 71  ? -7.84900  -3.01700  -58.92400 1.000 38.76564 ?  51  ALA B CB  1 
ATOM   3220 N  N   . ASP B 1 72  ? -4.61600  -3.11900  -58.08500 1.000 40.64625 ?  52  ASP B N   1 
ATOM   3221 C  CA  . ASP B 1 72  ? -3.33500  -3.72500  -58.42600 1.000 37.83904 ?  52  ASP B CA  1 
ATOM   3222 C  C   . ASP B 1 72  ? -2.93400  -4.73800  -57.36100 1.000 35.12146 ?  52  ASP B C   1 
ATOM   3223 O  O   . ASP B 1 72  ? -2.69300  -4.35300  -56.20600 1.000 36.23479 ?  52  ASP B O   1 
ATOM   3224 C  CB  . ASP B 1 72  ? -2.25600  -2.65000  -58.57100 1.000 43.02097 ?  52  ASP B CB  1 
ATOM   3225 C  CG  . ASP B 1 72  ? -0.88800  -3.22700  -58.91400 1.000 39.15999 ?  52  ASP B CG  1 
ATOM   3226 O  OD1 . ASP B 1 72  ? -0.80700  -4.40200  -59.33600 1.000 39.37602 ?  52  ASP B OD1 1 
ATOM   3227 O  OD2 . ASP B 1 72  ? 0.11200   -2.49500  -58.77000 1.000 46.17966 -1 52  ASP B OD2 1 
ATOM   3228 N  N   . PRO B 1 73  ? -2.85000  -6.02800  -57.69700 1.000 36.83814 ?  53  PRO B N   1 
ATOM   3229 C  CA  . PRO B 1 73  ? -2.48600  -7.03600  -56.69200 1.000 40.53191 ?  53  PRO B CA  1 
ATOM   3230 C  C   . PRO B 1 73  ? -1.02000  -7.01600  -56.29600 1.000 36.19319 ?  53  PRO B C   1 
ATOM   3231 O  O   . PRO B 1 73  ? -0.62100  -7.80300  -55.42900 1.000 38.16391 ?  53  PRO B O   1 
ATOM   3232 C  CB  . PRO B 1 73  ? -2.86900  -8.35100  -57.38200 1.000 38.99584 ?  53  PRO B CB  1 
ATOM   3233 C  CG  . PRO B 1 73  ? -2.70500  -8.05400  -58.83200 1.000 41.77733 ?  53  PRO B CG  1 
ATOM   3234 C  CD  . PRO B 1 73  ? -3.12700  -6.62800  -59.01300 1.000 40.91214 ?  53  PRO B CD  1 
ATOM   3235 N  N   . ARG B 1 74  ? -0.20500  -6.14800  -56.89500 1.000 36.92998 ?  54  ARG B N   1 
ATOM   3236 C  CA  . ARG B 1 74  ? 1.15400   -5.94700  -56.40600 1.000 37.29610 ?  54  ARG B CA  1 
ATOM   3237 C  C   . ARG B 1 74  ? 1.17000   -5.14200  -55.11300 1.000 33.29958 ?  54  ARG B C   1 
ATOM   3238 O  O   . ARG B 1 74  ? 2.21000   -5.07500  -54.44600 1.000 36.04474 ?  54  ARG B O   1 
ATOM   3239 C  CB  . ARG B 1 74  ? 1.99300   -5.24700  -57.47700 1.000 34.52503 ?  54  ARG B CB  1 
ATOM   3240 C  CG  . ARG B 1 74  ? 2.27000   -6.11900  -58.69300 1.000 45.34837 ?  54  ARG B CG  1 
ATOM   3241 C  CD  . ARG B 1 74  ? 2.86300   -5.33500  -59.85800 1.000 43.26616 ?  54  ARG B CD  1 
ATOM   3242 N  NE  . ARG B 1 74  ? 2.05200   -4.16600  -60.17600 1.000 50.97936 ?  54  ARG B NE  1 
ATOM   3243 C  CZ  . ARG B 1 74  ? 2.47300   -3.11800  -60.87100 1.000 52.54751 ?  54  ARG B CZ  1 
ATOM   3244 N  NH1 . ARG B 1 74  ? 3.62900   -3.13400  -61.51700 1.000 51.41153 ?  54  ARG B NH1 1 
ATOM   3245 N  NH2 . ARG B 1 74  ? 1.70800   -2.03000  -60.93300 1.000 53.04937 ?  54  ARG B NH2 1 
ATOM   3246 N  N   . LEU B 1 75  ? 0.03800   -4.54200  -54.75100 1.000 33.48889 ?  55  LEU B N   1 
ATOM   3247 C  CA  . LEU B 1 75  ? -0.12300  -3.76500  -53.52500 1.000 29.45697 ?  55  LEU B CA  1 
ATOM   3248 C  C   . LEU B 1 75  ? -0.88100  -4.64300  -52.53500 1.000 28.54719 ?  55  LEU B C   1 
ATOM   3249 O  O   . LEU B 1 75  ? -2.10900  -4.73400  -52.58500 1.000 30.58129 ?  55  LEU B O   1 
ATOM   3250 C  CB  . LEU B 1 75  ? -0.86700  -2.46700  -53.81500 1.000 30.33141 ?  55  LEU B CB  1 
ATOM   3251 C  CG  . LEU B 1 75  ? -0.03500  -1.28500  -54.31700 1.000 35.84518 ?  55  LEU B CG  1 
ATOM   3252 C  CD1 . LEU B 1 75  ? -0.87300  -0.01400  -54.36200 1.000 35.02006 ?  55  LEU B CD1 1 
ATOM   3253 C  CD2 . LEU B 1 75  ? 1.19600   -1.08400  -53.44200 1.000 28.31051 ?  55  LEU B CD2 1 
ATOM   3254 N  N   . SER B 1 76  ? -0.14600  -5.29800  -51.64500 1.000 27.61003 ?  56  SER B N   1 
ATOM   3255 C  CA  . SER B 1 76  ? -0.72100  -6.27400  -50.73500 1.000 28.21936 ?  56  SER B CA  1 
ATOM   3256 C  C   . SER B 1 76  ? -1.23500  -5.60000  -49.46800 1.000 23.38755 ?  56  SER B C   1 
ATOM   3257 O  O   . SER B 1 76  ? -0.71500  -4.56900  -49.03700 1.000 22.43913 ?  56  SER B O   1 
ATOM   3258 C  CB  . SER B 1 76  ? 0.31400   -7.34100  -50.37700 1.000 28.28052 ?  56  SER B CB  1 
ATOM   3259 O  OG  . SER B 1 76  ? 1.40800   -6.79000  -49.66900 1.000 49.73757 ?  56  SER B OG  1 
ATOM   3260 N  N   . VAL B 1 77  ? -2.28500  -6.18600  -48.88400 1.000 25.63679 ?  57  VAL B N   1 
ATOM   3261 C  CA  . VAL B 1 77  ? -2.78200  -5.76300  -47.57800 1.000 21.23839 ?  57  VAL B CA  1 
ATOM   3262 C  C   . VAL B 1 77  ? -2.24600  -6.63300  -46.45500 1.000 26.00996 ?  57  VAL B C   1 
ATOM   3263 O  O   . VAL B 1 77  ? -2.53200  -6.36600  -45.27900 1.000 28.78545 ?  57  VAL B O   1 
ATOM   3264 C  CB  . VAL B 1 77  ? -4.32500  -5.75900  -47.53600 1.000 23.01984 ?  57  VAL B CB  1 
ATOM   3265 C  CG1 . VAL B 1 77  ? -4.88200  -4.59100  -48.34700 1.000 23.90694 ?  57  VAL B CG1 1 
ATOM   3266 C  CG2 . VAL B 1 77  ? -4.87700  -7.10200  -48.02000 1.000 23.72022 ?  57  VAL B CG2 1 
ATOM   3267 N  N   . ASP B 1 78  ? -1.49000  -7.67500  -46.78600 1.000 24.38380 ?  58  ASP B N   1 
ATOM   3268 C  CA  . ASP B 1 78  ? -0.95900  -8.61300  -45.80600 1.000 30.51678 ?  58  ASP B CA  1 
ATOM   3269 C  C   . ASP B 1 78  ? 0.32100   -8.04800  -45.19800 1.000 29.00737 ?  58  ASP B C   1 
ATOM   3270 O  O   . ASP B 1 78  ? 1.26400   -7.72300  -45.92600 1.000 27.72443 ?  58  ASP B O   1 
ATOM   3271 C  CB  . ASP B 1 78  ? -0.69900  -9.95700  -46.48300 1.000 24.72395 ?  58  ASP B CB  1 
ATOM   3272 C  CG  . ASP B 1 78  ? -0.53400  -11.09500 -45.50100 1.000 30.37729 ?  58  ASP B CG  1 
ATOM   3273 O  OD1 . ASP B 1 78  ? 0.04600   -10.88300 -44.41600 1.000 33.13722 ?  58  ASP B OD1 1 
ATOM   3274 O  OD2 . ASP B 1 78  ? -0.97700  -12.21700 -45.82700 1.000 41.53496 -1 58  ASP B OD2 1 
ATOM   3275 N  N   . ARG B 1 79  ? 0.36000   -7.93800  -43.86600 1.000 26.58959 ?  59  ARG B N   1 
ATOM   3276 C  CA  . ARG B 1 79  ? 1.54400   -7.40200  -43.19800 1.000 25.67161 ?  59  ARG B CA  1 
ATOM   3277 C  C   . ARG B 1 79  ? 2.77200   -8.28600  -43.36400 1.000 24.60784 ?  59  ARG B C   1 
ATOM   3278 O  O   . ARG B 1 79  ? 3.88100   -7.83000  -43.06700 1.000 25.26261 ?  59  ARG B O   1 
ATOM   3279 C  CB  . ARG B 1 79  ? 1.27500   -7.19300  -41.70400 1.000 30.32836 ?  59  ARG B CB  1 
ATOM   3280 C  CG  . ARG B 1 79  ? 1.05500   -8.48500  -40.93700 1.000 30.27304 ?  59  ARG B CG  1 
ATOM   3281 C  CD  . ARG B 1 79  ? 0.76500   -8.22900  -39.46200 1.000 34.66074 ?  59  ARG B CD  1 
ATOM   3282 N  NE  . ARG B 1 79  ? 0.78000   -9.47400  -38.70500 1.000 26.40916 ?  59  ARG B NE  1 
ATOM   3283 C  CZ  . ARG B 1 79  ? -0.29100  -10.21100 -38.44400 1.000 29.36810 ?  59  ARG B CZ  1 
ATOM   3284 N  NH1 . ARG B 1 79  ? -1.50800  -9.80500  -38.77200 1.000 28.23184 ?  59  ARG B NH1 1 
ATOM   3285 N  NH2 . ARG B 1 79  ? -0.14000  -11.38100 -37.83000 1.000 27.11414 ?  59  ARG B NH2 1 
ATOM   3286 N  N   . SER B 1 80  ? 2.60700   -9.53100  -43.81700 1.000 26.46680 ?  60  SER B N   1 
ATOM   3287 C  CA  . SER B 1 80  ? 3.75700   -10.39000 -44.08100 1.000 28.58228 ?  60  SER B CA  1 
ATOM   3288 C  C   . SER B 1 80  ? 4.66400   -9.82200  -45.16400 1.000 28.71619 ?  60  SER B C   1 
ATOM   3289 O  O   . SER B 1 80  ? 5.84600   -10.18100 -45.22300 1.000 24.91630 ?  60  SER B O   1 
ATOM   3290 C  CB  . SER B 1 80  ? 3.28300   -11.79000 -44.47800 1.000 30.75904 ?  60  SER B CB  1 
ATOM   3291 O  OG  . SER B 1 80  ? 2.51900   -11.74500 -45.67000 1.000 38.73309 ?  60  SER B OG  1 
ATOM   3292 N  N   . ASN B 1 81  ? 4.14300   -8.94200  -46.01800 1.000 28.45383 ?  61  ASN B N   1 
ATOM   3293 C  CA  . ASN B 1 81  ? 4.91700   -8.32400  -47.08400 1.000 30.75602 ?  61  ASN B CA  1 
ATOM   3294 C  C   . ASN B 1 81  ? 5.40000   -6.92500  -46.72500 1.000 31.00162 ?  61  ASN B C   1 
ATOM   3295 O  O   . ASN B 1 81  ? 5.96200   -6.23600  -47.58300 1.000 25.60034 ?  61  ASN B O   1 
ATOM   3296 C  CB  . ASN B 1 81  ? 4.09200   -8.28600  -48.37200 1.000 31.54141 ?  61  ASN B CB  1 
ATOM   3297 C  CG  . ASN B 1 81  ? 3.66500   -9.66800  -48.82700 1.000 35.49115 ?  61  ASN B CG  1 
ATOM   3298 O  OD1 . ASN B 1 81  ? 4.48000   -10.58900 -48.90000 1.000 34.16390 ?  61  ASN B OD1 1 
ATOM   3299 N  ND2 . ASN B 1 81  ? 2.38100   -9.82400  -49.12300 1.000 28.71695 ?  61  ASN B ND2 1 
ATOM   3300 N  N   . ALA B 1 82  ? 5.20100   -6.49100  -45.48300 1.000 25.18464 ?  62  ALA B N   1 
ATOM   3301 C  CA  . ALA B 1 82  ? 5.67900   -5.18700  -45.05500 1.000 26.28981 ?  62  ALA B CA  1 
ATOM   3302 C  C   . ALA B 1 82  ? 7.13900   -5.26900  -44.62800 1.000 27.61521 ?  62  ALA B C   1 
ATOM   3303 O  O   . ALA B 1 82  ? 7.61600   -6.31300  -44.17600 1.000 20.24363 ?  62  ALA B O   1 
ATOM   3304 C  CB  . ALA B 1 82  ? 4.83400   -4.64900  -43.90300 1.000 25.72955 ?  62  ALA B CB  1 
ATOM   3305 N  N   . GLY B 1 83  ? 7.84300   -4.14100  -44.76900 1.000 25.99700 ?  63  GLY B N   1 
ATOM   3306 C  CA  . GLY B 1 83  ? 9.24500   -4.06200  -44.41700 1.000 26.94626 ?  63  GLY B CA  1 
ATOM   3307 C  C   . GLY B 1 83  ? 9.46600   -3.65100  -42.96900 1.000 32.00880 ?  63  GLY B C   1 
ATOM   3308 O  O   . GLY B 1 83  ? 8.53400   -3.47200  -42.18700 1.000 29.66931 ?  63  GLY B O   1 
ATOM   3309 N  N   . ALA B 1 84  ? 10.74600  -3.49400  -42.61900 1.000 28.43971 ?  64  ALA B N   1 
ATOM   3310 C  CA  . ALA B 1 84  ? 11.12300  -3.18500  -41.24200 1.000 29.78116 ?  64  ALA B CA  1 
ATOM   3311 C  C   . ALA B 1 84  ? 10.69300  -1.78900  -40.80700 1.000 27.21850 ?  64  ALA B C   1 
ATOM   3312 O  O   . ALA B 1 84  ? 10.62600  -1.52700  -39.60100 1.000 35.37326 ?  64  ALA B O   1 
ATOM   3313 C  CB  . ALA B 1 84  ? 12.63500  -3.33800  -41.06300 1.000 30.90133 ?  64  ALA B CB  1 
ATOM   3314 N  N   . GLY B 1 85  ? 10.41000  -0.89000  -41.74800 1.000 33.06909 ?  65  GLY B N   1 
ATOM   3315 C  CA  . GLY B 1 85  ? 9.92100   0.43200   -41.41400 1.000 29.81532 ?  65  GLY B CA  1 
ATOM   3316 C  C   . GLY B 1 85  ? 8.44200   0.51500   -41.12900 1.000 30.55694 ?  65  GLY B C   1 
ATOM   3317 O  O   . GLY B 1 85  ? 7.94200   1.59100   -40.78700 1.000 31.37421 ?  65  GLY B O   1 
ATOM   3318 N  N   . TYR B 1 86  ? 7.72900   -0.60000  -41.27500 1.000 30.89069 ?  66  TYR B N   1 
ATOM   3319 C  CA  . TYR B 1 86  ? 6.30100   -0.64400  -40.98600 1.000 32.17587 ?  66  TYR B CA  1 
ATOM   3320 C  C   . TYR B 1 86  ? 6.01300   -0.24300  -39.54600 1.000 30.49530 ?  66  TYR B C   1 
ATOM   3321 O  O   . TYR B 1 86  ? 6.62100   -0.76200  -38.60500 1.000 34.14835 ?  66  TYR B O   1 
ATOM   3322 C  CB  . TYR B 1 86  ? 5.76700   -2.04400  -41.27000 1.000 30.48102 ?  66  TYR B CB  1 
ATOM   3323 C  CG  . TYR B 1 86  ? 4.28100   -2.18100  -41.07800 1.000 32.97697 ?  66  TYR B CG  1 
ATOM   3324 C  CD1 . TYR B 1 86  ? 3.38700   -1.29900  -41.67100 1.000 32.42989 ?  66  TYR B CD1 1 
ATOM   3325 C  CD2 . TYR B 1 86  ? 3.77500   -3.20100  -40.29100 1.000 35.28778 ?  66  TYR B CD2 1 
ATOM   3326 C  CE1 . TYR B 1 86  ? 2.01800   -1.44100  -41.47400 1.000 29.09555 ?  66  TYR B CE1 1 
ATOM   3327 C  CE2 . TYR B 1 86  ? 2.42800   -3.35100  -40.09200 1.000 36.88787 ?  66  TYR B CE2 1 
ATOM   3328 C  CZ  . TYR B 1 86  ? 1.55000   -2.47700  -40.68100 1.000 33.31447 ?  66  TYR B CZ  1 
ATOM   3329 O  OH  . TYR B 1 86  ? 0.20700   -2.67600  -40.44500 1.000 29.20110 ?  66  TYR B OH  1 
ATOM   3330 N  N   . ARG B 1 87  ? 5.07800   0.69400   -39.37800 1.000 23.84757 ?  67  ARG B N   1 
ATOM   3331 C  CA  . ARG B 1 87  ? 4.73700   1.22200   -38.06300 1.000 30.90688 ?  67  ARG B CA  1 
ATOM   3332 C  C   . ARG B 1 87  ? 3.23300   1.32700   -37.83100 1.000 31.75582 ?  67  ARG B C   1 
ATOM   3333 O  O   . ARG B 1 87  ? 2.82000   1.89100   -36.81300 1.000 28.38765 ?  67  ARG B O   1 
ATOM   3334 C  CB  . ARG B 1 87  ? 5.39700   2.59000   -37.85200 1.000 30.99343 ?  67  ARG B CB  1 
ATOM   3335 C  CG  . ARG B 1 87  ? 6.91500   2.52000   -37.80000 1.000 32.77128 ?  67  ARG B CG  1 
ATOM   3336 C  CD  . ARG B 1 87  ? 7.39000   1.90100   -36.48900 1.000 36.83242 ?  67  ARG B CD  1 
ATOM   3337 N  NE  . ARG B 1 87  ? 7.01900   2.72600   -35.34600 1.000 36.81841 ?  67  ARG B NE  1 
ATOM   3338 C  CZ  . ARG B 1 87  ? 7.72300   3.76400   -34.91300 1.000 47.32636 ?  67  ARG B CZ  1 
ATOM   3339 N  NH1 . ARG B 1 87  ? 8.88100   4.09400   -35.46500 1.000 41.98982 ?  67  ARG B NH1 1 
ATOM   3340 N  NH2 . ARG B 1 87  ? 7.25900   4.48100   -33.89300 1.000 45.80526 ?  67  ARG B NH2 1 
ATOM   3341 N  N   . GLY B 1 88  ? 2.40800   0.81600   -38.74300 1.000 33.45060 ?  68  GLY B N   1 
ATOM   3342 C  CA  . GLY B 1 88  ? 0.98200   0.68900   -38.49000 1.000 25.92930 ?  68  GLY B CA  1 
ATOM   3343 C  C   . GLY B 1 88  ? 0.09400   1.81800   -38.97900 1.000 31.22382 ?  68  GLY B C   1 
ATOM   3344 O  O   . GLY B 1 88  ? -0.84400  2.21500   -38.28000 1.000 33.14587 ?  68  GLY B O   1 
ATOM   3345 N  N   . PHE B 1 89  ? 0.36300   2.33400   -40.17700 1.000 32.25661 ?  69  PHE B N   1 
ATOM   3346 C  CA  . PHE B 1 89  ? -0.51400  3.31900   -40.79800 1.000 32.38943 ?  69  PHE B CA  1 
ATOM   3347 C  C   . PHE B 1 89  ? -1.76900  2.64300   -41.33700 1.000 24.38219 ?  69  PHE B C   1 
ATOM   3348 O  O   . PHE B 1 89  ? -1.70600  1.52500   -41.85300 1.000 28.08677 ?  69  PHE B O   1 
ATOM   3349 C  CB  . PHE B 1 89  ? 0.20400   4.03500   -41.94200 1.000 27.74572 ?  69  PHE B CB  1 
ATOM   3350 C  CG  . PHE B 1 89  ? 1.12600   5.13300   -41.49500 1.000 40.07746 ?  69  PHE B CG  1 
ATOM   3351 C  CD1 . PHE B 1 89  ? 0.62700   6.37700   -41.14200 1.000 37.79915 ?  69  PHE B CD1 1 
ATOM   3352 C  CD2 . PHE B 1 89  ? 2.49700   4.92800   -41.44900 1.000 34.32884 ?  69  PHE B CD2 1 
ATOM   3353 C  CE1 . PHE B 1 89  ? 1.47900   7.39300   -40.74200 1.000 37.97997 ?  69  PHE B CE1 1 
ATOM   3354 C  CE2 . PHE B 1 89  ? 3.35300   5.93800   -41.05100 1.000 37.94002 ?  69  PHE B CE2 1 
ATOM   3355 C  CZ  . PHE B 1 89  ? 2.84500   7.17200   -40.69800 1.000 33.33788 ?  69  PHE B CZ  1 
ATOM   3356 N  N   . SER B 1 90  ? -2.90600  3.33700   -41.21500 1.000 25.55423 ?  70  SER B N   1 
ATOM   3357 C  CA  . SER B 1 90  ? -4.19900  2.91000   -41.75500 1.000 24.68992 ?  70  SER B CA  1 
ATOM   3358 C  C   . SER B 1 90  ? -4.51000  1.42500   -41.60600 1.000 23.53594 ?  70  SER B C   1 
ATOM   3359 O  O   . SER B 1 90  ? -4.78100  0.73500   -42.59400 1.000 24.40398 ?  70  SER B O   1 
ATOM   3360 C  CB  . SER B 1 90  ? -4.33300  3.33400   -43.22200 1.000 22.23974 ?  70  SER B CB  1 
ATOM   3361 O  OG  . SER B 1 90  ? -5.66100  3.15600   -43.69300 1.000 26.18224 ?  70  SER B OG  1 
ATOM   3362 N  N   . LEU B 1 91  ? -4.46900  0.93400   -40.37200 1.000 23.12432 ?  71  LEU B N   1 
ATOM   3363 C  CA  . LEU B 1 91  ? -4.56000  -0.49500  -40.12300 1.000 24.49707 ?  71  LEU B CA  1 
ATOM   3364 C  C   . LEU B 1 91  ? -5.85400  -1.13100  -40.62800 1.000 24.18483 ?  71  LEU B C   1 
ATOM   3365 O  O   . LEU B 1 91  ? -6.88400  -0.46000  -40.73600 1.000 25.91731 ?  71  LEU B O   1 
ATOM   3366 C  CB  . LEU B 1 91  ? -4.42900  -0.74900  -38.62500 1.000 23.12339 ?  71  LEU B CB  1 
ATOM   3367 C  CG  . LEU B 1 91  ? -3.03900  -0.62100  -38.01500 1.000 25.31220 ?  71  LEU B CG  1 
ATOM   3368 C  CD1 . LEU B 1 91  ? -3.16200  -0.50700  -36.50600 1.000 28.57631 ?  71  LEU B CD1 1 
ATOM   3369 C  CD2 . LEU B 1 91  ? -2.16200  -1.79900  -38.40600 1.000 31.94862 ?  71  LEU B CD2 1 
ATOM   3370 N  N   . PRO B 1 92  ? -5.84800  -2.46000  -40.91200 1.000 22.99617 ?  72  PRO B N   1 
ATOM   3371 C  CA  . PRO B 1 92  ? -7.08700  -3.15400  -41.19800 1.000 24.08912 ?  72  PRO B CA  1 
ATOM   3372 C  C   . PRO B 1 92  ? -7.98700  -2.99300  -39.96200 1.000 30.26874 ?  72  PRO B C   1 
ATOM   3373 O  O   . PRO B 1 92  ? -7.48600  -2.99700  -38.86400 1.000 22.89569 ?  72  PRO B O   1 
ATOM   3374 C  CB  . PRO B 1 92  ? -6.66400  -4.60600  -41.39900 1.000 24.82048 ?  72  PRO B CB  1 
ATOM   3375 C  CG  . PRO B 1 92  ? -5.25500  -4.51100  -41.88600 1.000 29.81756 ?  72  PRO B CG  1 
ATOM   3376 C  CD  . PRO B 1 92  ? -4.69800  -3.37700  -41.06200 1.000 25.25792 ?  72  PRO B CD  1 
ATOM   3377 N  N   . PRO B 1 93  ? -9.31400  -2.85900  -40.13600 1.000 23.12000 ?  73  PRO B N   1 
ATOM   3378 C  CA  . PRO B 1 93  ? -10.21500 -2.55900  -39.01900 1.000 25.51295 ?  73  PRO B CA  1 
ATOM   3379 C  C   . PRO B 1 93  ? -10.65600 -3.77400  -38.19600 1.000 36.31974 ?  73  PRO B C   1 
ATOM   3380 O  O   . PRO B 1 93  ? -11.71500 -3.72800  -37.62200 1.000 34.78030 ?  73  PRO B O   1 
ATOM   3381 C  CB  . PRO B 1 93  ? -11.42000 -1.94200  -39.74100 1.000 33.34205 ?  73  PRO B CB  1 
ATOM   3382 C  CG  . PRO B 1 93  ? -10.97400 -1.76000  -41.17900 1.000 33.44792 ?  73  PRO B CG  1 
ATOM   3383 C  CD  . PRO B 1 93  ? -9.99900  -2.88600  -41.41700 1.000 25.80355 ?  73  PRO B CD  1 
ATOM   3384 N  N   . ALA B 1 94  ? -9.84100  -4.81300  -38.16900 1.000 25.08051 ?  74  ALA B N   1 
ATOM   3385 C  CA  . ALA B 1 94  ? -10.16100 -5.96400  -37.30400 1.000 30.38506 ?  74  ALA B CA  1 
ATOM   3386 C  C   . ALA B 1 94  ? -8.89200  -6.72700  -36.96700 1.000 30.75702 ?  74  ALA B C   1 
ATOM   3387 O  O   . ALA B 1 94  ? -7.88900  -6.55800  -37.65700 1.000 32.59896 ?  74  ALA B O   1 
ATOM   3388 C  CB  . ALA B 1 94  ? -11.17600 -6.87600  -37.94400 1.000 32.76711 ?  74  ALA B CB  1 
ATOM   3389 N  N   . LEU B 1 95  ? -8.98700  -7.56300  -35.94400 1.000 34.38667 ?  75  LEU B N   1 
ATOM   3390 C  CA  . LEU B 1 95  ? -7.83900  -8.38300  -35.52900 1.000 35.43755 ?  75  LEU B CA  1 
ATOM   3391 C  C   . LEU B 1 95  ? -8.01400  -9.74800  -36.18600 1.000 41.16804 ?  75  LEU B C   1 
ATOM   3392 O  O   . LEU B 1 95  ? -9.14900  -10.08000 -36.54800 1.000 38.44302 ?  75  LEU B O   1 
ATOM   3393 C  CB  . LEU B 1 95  ? -7.84800  -8.48300  -34.00000 1.000 42.30821 ?  75  LEU B CB  1 
ATOM   3394 C  CG  . LEU B 1 95  ? -7.58500  -7.18800  -33.23800 1.000 35.57022 ?  75  LEU B CG  1 
ATOM   3395 C  CD2 . LEU B 1 95  ? -7.55600  -7.44500  -31.74500 1.000 35.48552 ?  75  LEU B CD2 1 
ATOM   3396 N  N   . ASP B 1 96  ? -6.93000  -10.47900 -36.35600 1.000 33.91616 ?  76  ASP B N   1 
ATOM   3397 C  CA  . ASP B 1 96  ? -6.98900  -11.84200 -36.93500 1.000 40.89021 ?  76  ASP B CA  1 
ATOM   3398 C  C   . ASP B 1 96  ? -7.32600  -11.79200 -38.42600 1.000 39.14687 ?  76  ASP B C   1 
ATOM   3399 O  O   . ASP B 1 96  ? -7.52400  -10.70100 -38.95600 1.000 42.85833 ?  76  ASP B O   1 
ATOM   3400 C  CB  . ASP B 1 96  ? -7.90900  -12.76800 -36.13800 1.000 43.94403 ?  76  ASP B CB  1 
ATOM   3401 C  CG  . ASP B 1 96  ? -7.23300  -14.06200 -35.73200 1.000 51.88219 ?  76  ASP B CG  1 
ATOM   3402 O  OD1 . ASP B 1 96  ? -6.25300  -14.43700 -36.39800 1.000 57.08740 -1 76  ASP B OD1 1 
ATOM   3403 O  OD2 . ASP B 1 96  ? -7.69000  -14.67500 -34.75300 1.000 50.80568 ?  76  ASP B OD2 1 
ATOM   3404 N  N   . ALA B 1 97  ? -7.36600  -12.95100 -39.06300 1.000 41.64446 ?  77  ALA B N   1 
ATOM   3405 C  CA  . ALA B 1 97  ? -7.60300  -13.03200 -40.51800 1.000 36.56976 ?  77  ALA B CA  1 
ATOM   3406 C  C   . ALA B 1 97  ? -8.93500  -12.38800 -40.91500 1.000 38.43261 ?  77  ALA B C   1 
ATOM   3407 O  O   . ALA B 1 97  ? -9.99300  -12.85600 -40.47000 1.000 42.07683 ?  77  ALA B O   1 
ATOM   3408 C  CB  . ALA B 1 97  ? -7.52400  -14.47200 -40.94500 1.000 42.22428 ?  77  ALA B CB  1 
ATOM   3409 N  N   . ASN B 1 98  ? -8.86000  -11.35100 -41.73700 1.000 33.68278 ?  78  ASN B N   1 
ATOM   3410 C  CA  . ASN B 1 98  ? -10.08300 -10.67600 -42.22000 1.000 29.31429 ?  78  ASN B CA  1 
ATOM   3411 C  C   . ASN B 1 98  ? -9.89700  -10.31700 -43.69500 1.000 32.97673 ?  78  ASN B C   1 
ATOM   3412 O  O   . ASN B 1 98  ? -8.77200  -10.40100 -44.20200 1.000 30.32866 ?  78  ASN B O   1 
ATOM   3413 C  CB  . ASN B 1 98  ? -10.44900 -9.44800  -41.38500 1.000 30.16790 ?  78  ASN B CB  1 
ATOM   3414 C  CG  . ASN B 1 98  ? -9.41200  -8.35000  -41.41900 1.000 31.17989 ?  78  ASN B CG  1 
ATOM   3415 O  OD1 . ASN B 1 98  ? -9.39600  -7.53600  -42.33600 1.000 32.29162 ?  78  ASN B OD1 1 
ATOM   3416 N  ND2 . ASN B 1 98  ? -8.56300  -8.30600  -40.41000 1.000 29.28895 ?  78  ASN B ND2 1 
ATOM   3417 N  N   . LEU B 1 99  ? -10.98300 -9.93800  -44.34600 1.000 27.89007 ?  79  LEU B N   1 
ATOM   3418 C  CA  . LEU B 1 99  ? -10.92700 -9.61200  -45.78600 1.000 31.63085 ?  79  LEU B CA  1 
ATOM   3419 C  C   . LEU B 1 99  ? -9.89400  -8.51300  -46.07200 1.000 25.61353 ?  79  LEU B C   1 
ATOM   3420 O  O   . LEU B 1 99  ? -9.30400  -8.57700  -47.13600 1.000 26.68793 ?  79  LEU B O   1 
ATOM   3421 C  CB  . LEU B 1 99  ? -12.32400 -9.15400  -46.19200 1.000 28.57208 ?  79  LEU B CB  1 
ATOM   3422 C  CG  . LEU B 1 99  ? -13.36100 -10.25200 -46.38500 1.000 24.96795 ?  79  LEU B CG  1 
ATOM   3423 C  CD1 . LEU B 1 99  ? -14.75700 -9.68400  -46.20900 1.000 27.48606 ?  79  LEU B CD1 1 
ATOM   3424 C  CD2 . LEU B 1 99  ? -13.21400 -10.87400 -47.75900 1.000 29.52653 ?  79  LEU B CD2 1 
ATOM   3425 N  N   . LEU B 1 100 ? -9.68000  -7.56200  -45.16300 1.000 26.01310 ?  80  LEU B N   1 
ATOM   3426 C  CA  . LEU B 1 100 ? -8.81600  -6.42800  -45.46700 1.000 28.22470 ?  80  LEU B CA  1 
ATOM   3427 C  C   . LEU B 1 100 ? -7.39100  -6.59500  -44.95400 1.000 25.70688 ?  80  LEU B C   1 
ATOM   3428 O  O   . LEU B 1 100 ? -6.62900  -5.62200  -44.95100 1.000 25.95612 ?  80  LEU B O   1 
ATOM   3429 C  CB  . LEU B 1 100 ? -9.42300  -5.13700  -44.91900 1.000 27.19154 ?  80  LEU B CB  1 
ATOM   3430 C  CG  . LEU B 1 100 ? -10.62300 -4.60300  -45.70600 1.000 21.14216 ?  80  LEU B CG  1 
ATOM   3431 C  CD1 . LEU B 1 100 ? -11.32000 -3.48700  -44.93900 1.000 25.33467 ?  80  LEU B CD1 1 
ATOM   3432 C  CD2 . LEU B 1 100 ? -10.17900 -4.11500  -47.07500 1.000 22.52189 ?  80  LEU B CD2 1 
ATOM   3433 N  N   . ASN B 1 101 ? -7.00800  -7.79700  -44.52300 1.000 25.36481 ?  81  ASN B N   1 
ATOM   3434 C  CA  . ASN B 1 101 ? -5.60700  -8.09100  -44.24100 1.000 29.76311 ?  81  ASN B CA  1 
ATOM   3435 C  C   . ASN B 1 101 ? -5.13200  -9.35300  -44.95500 1.000 28.26835 ?  81  ASN B C   1 
ATOM   3436 O  O   . ASN B 1 101 ? -4.11400  -9.94100  -44.56900 1.000 31.24459 ?  81  ASN B O   1 
ATOM   3437 C  CB  . ASN B 1 101 ? -5.36100  -8.15200  -42.72200 1.000 33.38338 ?  81  ASN B CB  1 
ATOM   3438 C  CG  . ASN B 1 101 ? -5.83000  -9.45000  -42.07000 1.000 35.26540 ?  81  ASN B CG  1 
ATOM   3439 O  OD1 . ASN B 1 101 ? -6.30800  -10.37900 -42.72300 1.000 36.20038 ?  81  ASN B OD1 1 
ATOM   3440 N  ND2 . ASN B 1 101 ? -5.68700  -9.50900  -40.75200 1.000 39.43169 ?  81  ASN B ND2 1 
ATOM   3441 N  N   . LEU B 1 102 ? -5.83100  -9.75600  -46.01400 1.000 30.86059 ?  82  LEU B N   1 
ATOM   3442 C  CA  . LEU B 1 102 ? -5.54700  -10.97600 -46.75200 1.000 30.02554 ?  82  LEU B CA  1 
ATOM   3443 C  C   . LEU B 1 102 ? -5.52800  -10.66900 -48.24200 1.000 30.16263 ?  82  LEU B C   1 
ATOM   3444 O  O   . LEU B 1 102 ? -6.37000  -9.91700  -48.74000 1.000 29.75214 ?  82  LEU B O   1 
ATOM   3445 C  CB  . LEU B 1 102 ? -6.60600  -12.04800 -46.46300 1.000 33.11724 ?  82  LEU B CB  1 
ATOM   3446 C  CG  . LEU B 1 102 ? -6.53700  -12.74100 -45.10100 1.000 32.55531 ?  82  LEU B CG  1 
ATOM   3447 C  CD1 . LEU B 1 102 ? -7.59700  -13.82600 -45.01000 1.000 35.85765 ?  82  LEU B CD1 1 
ATOM   3448 C  CD2 . LEU B 1 102 ? -5.15200  -13.31400 -44.85200 1.000 36.27897 ?  82  LEU B CD2 1 
ATOM   3449 N  N   . ASP B 1 103 ? -4.60300  -11.30300 -48.94200 1.000 30.81969 ?  83  ASP B N   1 
ATOM   3450 C  CA  . ASP B 1 103 ? -4.53200  -11.15400 -50.41000 1.000 29.39088 ?  83  ASP B CA  1 
ATOM   3451 C  C   . ASP B 1 103 ? -5.04900  -12.43900 -51.04300 1.000 33.47864 ?  83  ASP B C   1 
ATOM   3452 O  O   . ASP B 1 103 ? -5.06600  -13.46800 -50.36400 1.000 36.25437 ?  83  ASP B O   1 
ATOM   3453 C  CB  . ASP B 1 103 ? -3.10500  -10.91300 -50.90000 1.000 30.00645 ?  83  ASP B CB  1 
ATOM   3454 C  CG  . ASP B 1 103 ? -2.40100  -9.76400  -50.21500 1.000 32.89006 ?  83  ASP B CG  1 
ATOM   3455 O  OD1 . ASP B 1 103 ? -2.98400  -8.67500  -50.15000 1.000 32.44631 ?  83  ASP B OD1 1 
ATOM   3456 O  OD2 . ASP B 1 103 ? -1.27100  -9.98000  -49.77500 1.000 39.23272 -1 83  ASP B OD2 1 
ATOM   3457 N  N   . PRO B 1 104 ? -5.50600  -12.41100 -52.30500 1.000 32.78885 ?  84  PRO B N   1 
ATOM   3458 C  CA  . PRO B 1 104 ? -5.86700  -13.64300 -52.96700 1.000 31.45617 ?  84  PRO B CA  1 
ATOM   3459 C  C   . PRO B 1 104 ? -4.60900  -14.51700 -52.95900 1.000 38.38870 ?  84  PRO B C   1 
ATOM   3460 O  O   . PRO B 1 104 ? -3.55300  -14.03000 -53.25500 1.000 42.79751 ?  84  PRO B O   1 
ATOM   3461 C  CB  . PRO B 1 104 ? -6.26200  -13.16600 -54.35800 1.000 35.63426 ?  84  PRO B CB  1 
ATOM   3462 C  CG  . PRO B 1 104 ? -6.70500  -11.74800 -54.15400 1.000 34.56046 ?  84  PRO B CG  1 
ATOM   3463 C  CD  . PRO B 1 104 ? -5.75800  -11.21700 -53.10500 1.000 29.93329 ?  84  PRO B CD  1 
ATOM   3464 N  N   . PRO B 1 105 ? -4.69400  -15.79500 -52.55100 1.000 42.04122 ?  85  PRO B N   1 
ATOM   3465 C  CA  . PRO B 1 105 ? -5.92600  -16.58400 -52.66400 1.000 40.88296 ?  85  PRO B CA  1 
ATOM   3466 C  C   . PRO B 1 105 ? -6.85100  -16.69600 -51.43000 1.000 45.87178 ?  85  PRO B C   1 
ATOM   3467 O  O   . PRO B 1 105 ? -8.00500  -17.05100 -51.58600 1.000 41.84720 ?  85  PRO B O   1 
ATOM   3468 C  CB  . PRO B 1 105 ? -5.31300  -17.95300 -52.97500 1.000 40.87905 ?  85  PRO B CB  1 
ATOM   3469 C  CG  . PRO B 1 105 ? -4.04500  -18.00800 -52.16300 1.000 40.42998 ?  85  PRO B CG  1 
ATOM   3470 C  CD  . PRO B 1 105 ? -3.57400  -16.57700 -52.04000 1.000 44.75375 ?  85  PRO B CD  1 
ATOM   3471 N  N   . ASP B 1 106 ? -6.35200  -16.35900 -50.24600 1.000 40.21000 ?  86  ASP B N   1 
ATOM   3472 C  CA  . ASP B 1 106 ? -7.16200  -16.49500 -49.00800 1.000 38.30314 ?  86  ASP B CA  1 
ATOM   3473 C  C   . ASP B 1 106 ? -8.34600  -15.52400 -49.02200 1.000 35.89631 ?  86  ASP B C   1 
ATOM   3474 O  O   . ASP B 1 106 ? -9.41600  -15.90500 -48.54700 1.000 39.66684 ?  86  ASP B O   1 
ATOM   3475 C  CB  . ASP B 1 106 ? -6.28600  -16.35200 -47.76700 1.000 40.84671 ?  86  ASP B CB  1 
ATOM   3476 C  CG  . ASP B 1 106 ? -5.14100  -17.34500 -47.68300 1.000 50.12956 ?  86  ASP B CG  1 
ATOM   3477 O  OD1 . ASP B 1 106 ? -4.93700  -18.08900 -48.65000 1.000 60.48066 -1 86  ASP B OD1 1 
ATOM   3478 O  OD2 . ASP B 1 106 ? -4.44800  -17.34200 -46.65500 1.000 50.90541 -1 86  ASP B OD2 1 
ATOM   3479 N  N   . HIS B 1 107 ? -8.15500  -14.32100 -49.55000 1.000 30.92710 ?  87  HIS B N   1 
ATOM   3480 C  CA  . HIS B 1 107 ? -9.24700  -13.32200 -49.60900 1.000 33.92276 ?  87  HIS B CA  1 
ATOM   3481 C  C   . HIS B 1 107 ? -10.39700 -13.88600 -50.43700 1.000 34.40607 ?  87  HIS B C   1 
ATOM   3482 O  O   . HIS B 1 107 ? -11.57400 -13.66000 -50.12200 1.000 32.28945 ?  87  HIS B O   1 
ATOM   3483 C  CB  . HIS B 1 107 ? -8.76200  -11.99700 -50.19500 1.000 29.35431 ?  87  HIS B CB  1 
ATOM   3484 C  CG  . HIS B 1 107 ? -9.85600  -11.06500 -50.55400 1.000 31.40507 ?  87  HIS B CG  1 
ATOM   3485 N  ND1 . HIS B 1 107 ? -10.47100 -11.08800 -51.78300 1.000 27.69819 ?  87  HIS B ND1 1 
ATOM   3486 C  CD2 . HIS B 1 107 ? -10.45400 -10.10800 -49.85500 1.000 27.37341 ?  87  HIS B CD2 1 
ATOM   3487 C  CE1 . HIS B 1 107 ? -11.40300 -10.15700 -51.81600 1.000 36.83387 ?  87  HIS B CE1 1 
ATOM   3488 N  NE2 . HIS B 1 107 ? -11.40400 -9.54700  -50.65800 1.000 30.95680 ?  87  HIS B NE2 1 
ATOM   3489 N  N   . THR B 1 108 ? -10.04000 -14.58900 -51.50100 1.000 35.35987 ?  88  THR B N   1 
ATOM   3490 C  CA  . THR B 1 108 ? -11.06300 -15.17500 -52.40100 1.000 33.50734 ?  88  THR B CA  1 
ATOM   3491 C  C   . THR B 1 108 ? -12.00100 -16.09100 -51.60400 1.000 36.22339 ?  88  THR B C   1 
ATOM   3492 O  O   . THR B 1 108 ? -13.21100 -15.91100 -51.72000 1.000 33.70462 ?  88  THR B O   1 
ATOM   3493 C  CB  . THR B 1 108 ? -10.35800 -15.82300 -53.60200 1.000 43.03158 ?  88  THR B CB  1 
ATOM   3494 O  OG1 . THR B 1 108 ? -9.63000  -14.82000 -54.31100 1.000 34.90795 ?  88  THR B OG1 1 
ATOM   3495 C  CG2 . THR B 1 108 ? -11.33000 -16.50900 -54.53800 1.000 42.20595 ?  88  THR B CG2 1 
ATOM   3496 N  N   . ARG B 1 109 ? -11.45200 -17.01700 -50.82400 1.000 38.01247 ?  89  ARG B N   1 
ATOM   3497 C  CA  . ARG B 1 109 ? -12.27900 -17.90200 -49.96600 1.000 36.09192 ?  89  ARG B CA  1 
ATOM   3498 C  C   . ARG B 1 109 ? -13.20600 -17.07500 -49.07500 1.000 38.87687 ?  89  ARG B C   1 
ATOM   3499 O  O   . ARG B 1 109 ? -14.40900 -17.34000 -49.07600 1.000 40.27416 ?  89  ARG B O   1 
ATOM   3500 C  CB  . ARG B 1 109 ? -11.37000 -18.75400 -49.08700 1.000 41.07603 ?  89  ARG B CB  1 
ATOM   3501 C  CG  . ARG B 1 109 ? -12.09200 -19.54400 -48.01000 1.000 37.93025 ?  89  ARG B CG  1 
ATOM   3502 C  CD  . ARG B 1 109 ? -11.11400 -20.40800 -47.24500 1.000 42.64868 ?  89  ARG B CD  1 
ATOM   3503 N  NE  . ARG B 1 109 ? -11.73400 -20.95800 -46.05300 1.000 49.89609 ?  89  ARG B NE  1 
ATOM   3504 C  CZ  . ARG B 1 109 ? -11.87300 -20.29500 -44.91400 1.000 45.79837 ?  89  ARG B CZ  1 
ATOM   3505 N  NH1 . ARG B 1 109 ? -11.24700 -19.14600 -44.74400 1.000 47.20923 ?  89  ARG B NH1 1 
ATOM   3506 N  NH2 . ARG B 1 109 ? -12.62700 -20.78800 -43.94800 1.000 44.69343 ?  89  ARG B NH2 1 
ATOM   3507 N  N   . LEU B 1 110 ? -12.65900 -16.09700 -48.35900 1.000 40.33524 ?  90  LEU B N   1 
ATOM   3508 C  CA  . LEU B 1 110 ? -13.47800 -15.32500 -47.42900 1.000 38.38901 ?  90  LEU B CA  1 
ATOM   3509 C  C   . LEU B 1 110 ? -14.57000 -14.55700 -48.16000 1.000 35.20582 ?  90  LEU B C   1 
ATOM   3510 O  O   . LEU B 1 110 ? -15.73200 -14.55100 -47.73700 1.000 36.65461 ?  90  LEU B O   1 
ATOM   3511 C  CB  . LEU B 1 110 ? -12.59800 -14.36500 -46.62900 1.000 36.23481 ?  90  LEU B CB  1 
ATOM   3512 C  CG  . LEU B 1 110 ? -11.88300 -14.94200 -45.41300 1.000 38.98483 ?  90  LEU B CG  1 
ATOM   3513 C  CD1 . LEU B 1 110 ? -11.31500 -13.82000 -44.57000 1.000 34.40974 ?  90  LEU B CD1 1 
ATOM   3514 C  CD2 . LEU B 1 110 ? -12.83200 -15.79900 -44.59400 1.000 41.39531 ?  90  LEU B CD2 1 
ATOM   3515 N  N   . ARG B 1 111 ? -14.21100 -13.89200 -49.26000 1.000 32.35389 ?  91  ARG B N   1 
ATOM   3516 C  CA  . ARG B 1 111 ? -15.19500 -13.10500 -49.99400 1.000 29.10748 ?  91  ARG B CA  1 
ATOM   3517 C  C   . ARG B 1 111 ? -16.30000 -13.99700 -50.54300 1.000 37.56137 ?  91  ARG B C   1 
ATOM   3518 O  O   . ARG B 1 111 ? -17.47900 -13.62900 -50.50700 1.000 37.79366 ?  91  ARG B O   1 
ATOM   3519 C  CB  . ARG B 1 111 ? -14.50700 -12.32800 -51.11800 1.000 25.43924 ?  91  ARG B CB  1 
ATOM   3520 C  CG  . ARG B 1 111 ? -15.43700 -11.47500 -51.95900 1.000 34.92416 ?  91  ARG B CG  1 
ATOM   3521 C  CD  . ARG B 1 111 ? -15.13400 -10.00100 -51.74000 1.000 30.34000 ?  91  ARG B CD  1 
ATOM   3522 N  NE  . ARG B 1 111 ? -16.17800 -9.11900  -52.24700 1.000 32.91476 ?  91  ARG B NE  1 
ATOM   3523 C  CZ  . ARG B 1 111 ? -16.17700 -7.80000  -52.10400 1.000 35.73961 ?  91  ARG B CZ  1 
ATOM   3524 N  NH1 . ARG B 1 111 ? -15.21600 -7.17600  -51.44100 1.000 34.82689 ?  91  ARG B NH1 1 
ATOM   3525 N  NH2 . ARG B 1 111 ? -17.16700 -7.08900  -52.63700 1.000 43.64150 ?  91  ARG B NH2 1 
ATOM   3526 N  N   . THR B 1 112 ? -15.94000 -15.18800 -51.02400 1.000 34.62915 ?  92  THR B N   1 
ATOM   3527 C  CA  . THR B 1 112 ? -16.93700 -16.11300 -51.55300 1.000 41.93557 ?  92  THR B CA  1 
ATOM   3528 C  C   . THR B 1 112 ? -17.86200 -16.62300 -50.45200 1.000 39.89460 ?  92  THR B C   1 
ATOM   3529 O  O   . THR B 1 112 ? -19.07800 -16.73900 -50.65700 1.000 41.15925 ?  92  THR B O   1 
ATOM   3530 C  CB  . THR B 1 112 ? -16.23600 -17.27600 -52.25800 1.000 37.52970 ?  92  THR B CB  1 
ATOM   3531 O  OG1 . THR B 1 112 ? -15.68100 -16.81200 -53.49400 1.000 32.79134 ?  92  THR B OG1 1 
ATOM   3532 C  CG2 . THR B 1 112 ? -17.21000 -18.41300 -52.54000 1.000 39.53214 ?  92  THR B CG2 1 
ATOM   3533 N  N   . LEU B 1 113 ? -17.31000 -16.91500 -49.27200 1.000 37.10888 ?  93  LEU B N   1 
ATOM   3534 C  CA  . LEU B 1 113 ? -18.13400 -17.40800 -48.17300 1.000 38.83533 ?  93  LEU B CA  1 
ATOM   3535 C  C   . LEU B 1 113 ? -19.03700 -16.31300 -47.61700 1.000 40.01294 ?  93  LEU B C   1 
ATOM   3536 O  O   . LEU B 1 113 ? -20.20300 -16.56800 -47.28600 1.000 40.52412 ?  93  LEU B O   1 
ATOM   3537 C  CB  . LEU B 1 113 ? -17.24700 -17.98300 -47.07100 1.000 36.69029 ?  93  LEU B CB  1 
ATOM   3538 C  CG  . LEU B 1 113 ? -16.74400 -19.41400 -47.27900 1.000 41.75628 ?  93  LEU B CG  1 
ATOM   3539 C  CD1 . LEU B 1 113 ? -15.51100 -19.67800 -46.42400 1.000 44.33708 ?  93  LEU B CD1 1 
ATOM   3540 C  CD2 . LEU B 1 113 ? -17.83600 -20.42600 -46.97600 1.000 39.02532 ?  93  LEU B CD2 1 
ATOM   3541 N  N   . ILE B 1 114 ? -18.52500 -15.08600 -47.51200 1.000 38.61397 ?  94  ILE B N   1 
ATOM   3542 C  CA  . ILE B 1 114 ? -19.30800 -14.01500 -46.90500 1.000 38.50320 ?  94  ILE B CA  1 
ATOM   3543 C  C   . ILE B 1 114 ? -20.33800 -13.45900 -47.88400 1.000 40.35003 ?  94  ILE B C   1 
ATOM   3544 O  O   . ILE B 1 114 ? -21.47500 -13.16400 -47.49700 1.000 37.59442 ?  94  ILE B O   1 
ATOM   3545 C  CB  . ILE B 1 114 ? -18.38000 -12.91600 -46.35800 1.000 32.40798 ?  94  ILE B CB  1 
ATOM   3546 C  CG1 . ILE B 1 114 ? -17.60800 -13.44400 -45.14500 1.000 36.29534 ?  94  ILE B CG1 1 
ATOM   3547 C  CG2 . ILE B 1 114 ? -19.17100 -11.66800 -45.98900 1.000 30.72998 ?  94  ILE B CG2 1 
ATOM   3548 C  CD1 . ILE B 1 114 ? -16.21500 -12.88400 -45.00400 1.000 29.03218 ?  94  ILE B CD1 1 
ATOM   3549 N  N   . ALA B 1 115 ? -19.97500 -13.31700 -49.16200 1.000 38.98509 ?  95  ALA B N   1 
ATOM   3550 C  CA  . ALA B 1 115 ? -20.92300 -12.79500 -50.14400 1.000 43.12008 ?  95  ALA B CA  1 
ATOM   3551 C  C   . ALA B 1 115 ? -22.16100 -13.67200 -50.28800 1.000 40.40288 ?  95  ALA B C   1 
ATOM   3552 O  O   . ALA B 1 115 ? -23.21100 -13.17400 -50.70700 1.000 50.66587 ?  95  ALA B O   1 
ATOM   3553 C  CB  . ALA B 1 115 ? -20.25000 -12.63200 -51.50700 1.000 39.91175 ?  95  ALA B CB  1 
ATOM   3554 N  N   . GLY B 1 116 ? -22.06500 -14.96200 -49.95600 1.000 44.73391 ?  96  GLY B N   1 
ATOM   3555 C  CA  . GLY B 1 116 ? -23.22500 -15.83000 -50.07500 1.000 49.44480 ?  96  GLY B CA  1 
ATOM   3556 C  C   . GLY B 1 116 ? -24.36900 -15.40700 -49.17600 1.000 53.78913 ?  96  GLY B C   1 
ATOM   3557 O  O   . GLY B 1 116 ? -25.53600 -15.46800 -49.57000 1.000 58.99016 ?  96  GLY B O   1 
ATOM   3558 N  N   . GLU B 1 117 ? -24.02700 -14.95000 -47.96600 1.000 48.62952 ?  97  GLU B N   1 
ATOM   3559 C  CA  . GLU B 1 117 ? -25.07300 -14.54600 -46.98600 1.000 50.49716 ?  97  GLU B CA  1 
ATOM   3560 C  C   . GLU B 1 117 ? -25.26200 -13.02900 -47.00600 1.000 49.92587 ?  97  GLU B C   1 
ATOM   3561 O  O   . GLU B 1 117 ? -26.33500 -12.58400 -46.60100 1.000 52.34698 ?  97  GLU B O   1 
ATOM   3562 C  CB  . GLU B 1 117 ? -24.69000 -15.03600 -45.59800 1.000 45.21809 ?  97  GLU B CB  1 
ATOM   3563 N  N   . PHE B 1 118 ? -24.28000 -12.28200 -47.51600 1.000 46.37400 ?  98  PHE B N   1 
ATOM   3564 C  CA  . PHE B 1 118 ? -24.33800 -10.79900 -47.55000 1.000 44.11340 ?  98  PHE B CA  1 
ATOM   3565 C  C   . PHE B 1 118 ? -24.79200 -10.37100 -48.94600 1.000 50.64060 ?  98  PHE B C   1 
ATOM   3566 O  O   . PHE B 1 118 ? -24.01600 -9.70500  -49.63400 1.000 48.18619 ?  98  PHE B O   1 
ATOM   3567 C  CB  . PHE B 1 118 ? -22.97900 -10.24600 -47.11500 1.000 52.56466 ?  98  PHE B CB  1 
ATOM   3568 C  CG  . PHE B 1 118 ? -22.98400 -8.89000  -46.46400 1.000 44.26945 ?  98  PHE B CG  1 
ATOM   3569 C  CD1 . PHE B 1 118 ? -23.85500 -7.90200  -46.88300 1.000 54.17472 ?  98  PHE B CD1 1 
ATOM   3570 C  CD2 . PHE B 1 118 ? -22.10800 -8.60600  -45.43200 1.000 46.22928 ?  98  PHE B CD2 1 
ATOM   3571 C  CE1 . PHE B 1 118 ? -23.85600 -6.65700  -46.28200 1.000 50.40693 ?  98  PHE B CE1 1 
ATOM   3572 C  CE2 . PHE B 1 118 ? -22.10900 -7.36000  -44.83000 1.000 42.44229 ?  98  PHE B CE2 1 
ATOM   3573 C  CZ  . PHE B 1 118 ? -22.98200 -6.39200  -45.25800 1.000 44.43254 ?  98  PHE B CZ  1 
ATOM   3574 N  N   . THR B 1 119 ? -26.03900 -10.69000 -49.30500 1.000 54.66809 ?  99  THR B N   1 
ATOM   3575 C  CA  . THR B 1 119 ? -26.61900 -10.42000 -50.64100 1.000 54.23352 ?  99  THR B CA  1 
ATOM   3576 C  C   . THR B 1 119 ? -27.31300 -9.05900  -50.72200 1.000 53.78906 ?  99  THR B C   1 
ATOM   3577 O  O   . THR B 1 119 ? -27.78500 -8.57200  -49.69800 1.000 55.41473 ?  99  THR B O   1 
ATOM   3578 C  CB  . THR B 1 119 ? -27.70000 -11.47200 -50.87500 1.000 54.15396 ?  99  THR B CB  1 
ATOM   3579 O  OG1 . THR B 1 119 ? -28.72900 -11.21500 -49.92300 1.000 53.10117 ?  99  THR B OG1 1 
ATOM   3580 C  CG2 . THR B 1 119 ? -27.18700 -12.87900 -50.67900 1.000 53.22945 ?  99  THR B CG2 1 
ATOM   3581 N  N   . PRO B 1 120 ? -27.44400 -8.44500  -51.91000 1.000 51.13400 ?  100 PRO B N   1 
ATOM   3582 C  CA  . PRO B 1 120 ? -28.18100 -7.19200  -52.01500 1.000 48.74325 ?  100 PRO B CA  1 
ATOM   3583 C  C   . PRO B 1 120 ? -29.64800 -7.31800  -51.56000 1.000 58.00753 ?  100 PRO B C   1 
ATOM   3584 O  O   . PRO B 1 120 ? -30.17600 -6.37000  -51.03900 1.000 55.94972 ?  100 PRO B O   1 
ATOM   3585 C  CB  . PRO B 1 120 ? -28.12400 -6.86700  -53.51100 1.000 56.14079 ?  100 PRO B CB  1 
ATOM   3586 C  CG  . PRO B 1 120 ? -26.90000 -7.60700  -54.00900 1.000 55.36537 ?  100 PRO B CG  1 
ATOM   3587 C  CD  . PRO B 1 120 ? -26.83700 -8.86700  -53.17100 1.000 48.74065 ?  100 PRO B CD  1 
ATOM   3588 N  N   . ARG B 1 121 ? -30.26200 -8.48200  -51.74300 1.000 48.48447 ?  101 ARG B N   1 
ATOM   3589 C  CA  . ARG B 1 121 ? -31.63200 -8.67000  -51.27600 1.000 48.01740 ?  101 ARG B CA  1 
ATOM   3590 C  C   . ARG B 1 121 ? -31.73200 -8.53700  -49.76300 1.000 50.20292 ?  101 ARG B C   1 
ATOM   3591 O  O   . ARG B 1 121 ? -32.77000 -8.10600  -49.24900 1.000 47.15746 ?  101 ARG B O   1 
ATOM   3592 C  CB  . ARG B 1 121 ? -32.16000 -10.03300 -51.72300 1.000 51.19018 ?  101 ARG B CB  1 
ATOM   3593 N  N   . ARG B 1 122 ? -30.67600 -8.91400  -49.03700 1.000 47.43963 ?  102 ARG B N   1 
ATOM   3594 C  CA  . ARG B 1 122 ? -30.62800 -8.64500  -47.60400 1.000 43.66301 ?  102 ARG B CA  1 
ATOM   3595 C  C   . ARG B 1 122 ? -30.80600 -7.15900  -47.33200 1.000 48.05889 ?  102 ARG B C   1 
ATOM   3596 O  O   . ARG B 1 122 ? -31.58400 -6.76100  -46.45800 1.000 44.46421 ?  102 ARG B O   1 
ATOM   3597 C  CB  . ARG B 1 122 ? -29.30600 -9.14700  -47.03100 1.000 49.19860 ?  102 ARG B CB  1 
ATOM   3598 C  CG  . ARG B 1 122 ? -29.39800 -10.50000 -46.36300 1.000 45.90630 ?  102 ARG B CG  1 
ATOM   3599 C  CD  . ARG B 1 122 ? -28.60300 -10.53400 -45.07500 1.000 46.39223 ?  102 ARG B CD  1 
ATOM   3600 N  NE  . ARG B 1 122 ? -28.29700 -11.90800 -44.69800 1.000 47.15794 ?  102 ARG B NE  1 
ATOM   3601 C  CZ  . ARG B 1 122 ? -28.93300 -12.58600 -43.75400 1.000 47.52906 ?  102 ARG B CZ  1 
ATOM   3602 N  NH1 . ARG B 1 122 ? -29.85600 -12.01700 -42.99400 1.000 38.67879 ?  102 ARG B NH1 1 
ATOM   3603 N  NH2 . ARG B 1 122 ? -28.62700 -13.86600 -43.55800 1.000 43.44839 ?  102 ARG B NH2 1 
ATOM   3604 N  N   . VAL B 1 123 ? -30.10700 -6.34600  -48.11100 1.000 43.69196 ?  103 VAL B N   1 
ATOM   3605 C  CA  . VAL B 1 123 ? -30.23300 -4.87200  -47.94000 1.000 45.88355 ?  103 VAL B CA  1 
ATOM   3606 C  C   . VAL B 1 123 ? -31.65800 -4.45000  -48.30900 1.000 41.63124 ?  103 VAL B C   1 
ATOM   3607 O  O   . VAL B 1 123 ? -32.28100 -3.72700  -47.53400 1.000 38.35026 ?  103 VAL B O   1 
ATOM   3608 C  CB  . VAL B 1 123 ? -29.16400 -4.14900  -48.77800 1.000 39.03292 ?  103 VAL B CB  1 
ATOM   3609 C  CG1 . VAL B 1 123 ? -29.33800 -2.64200  -48.73000 1.000 39.25993 ?  103 VAL B CG1 1 
ATOM   3610 C  CG2 . VAL B 1 123 ? -27.76600 -4.55300  -48.34700 1.000 39.67056 ?  103 VAL B CG2 1 
ATOM   3611 N  N   . HIS B 1 124 ? -32.15500 -4.92500  -49.44700 1.000 47.53056 ?  104 HIS B N   1 
ATOM   3612 C  CA  . HIS B 1 124 ? -33.51300 -4.54100  -49.91900 1.000 39.72886 ?  104 HIS B CA  1 
ATOM   3613 C  C   . HIS B 1 124 ? -34.57600 -4.97000  -48.89300 1.000 36.94460 ?  104 HIS B C   1 
ATOM   3614 O  O   . HIS B 1 124 ? -35.49300 -4.19600  -48.64600 1.000 39.12106 ?  104 HIS B O   1 
ATOM   3615 C  CB  . HIS B 1 124 ? -33.73700 -5.04200  -51.35300 1.000 45.66372 ?  104 HIS B CB  1 
ATOM   3616 C  CG  . HIS B 1 124 ? -35.12800 -4.82900  -51.83600 1.000 50.90380 ?  104 HIS B CG  1 
ATOM   3617 N  ND1 . HIS B 1 124 ? -35.55700 -3.63000  -52.36000 1.000 53.74344 ?  104 HIS B ND1 1 
ATOM   3618 C  CD2 . HIS B 1 124 ? -36.18500 -5.64500  -51.86300 1.000 50.29221 ?  104 HIS B CD2 1 
ATOM   3619 C  CE1 . HIS B 1 124 ? -36.83300 -3.73400  -52.69300 1.000 49.54254 ?  104 HIS B CE1 1 
ATOM   3620 N  NE2 . HIS B 1 124 ? -37.23400 -4.94900  -52.40200 1.000 46.74936 ?  104 HIS B NE2 1 
ATOM   3621 N  N   . GLU B 1 125 ? -34.44400 -6.15500  -48.30900 1.000 35.41940 ?  105 GLU B N   1 
ATOM   3622 C  CA  . GLU B 1 125 ? -35.44300 -6.65500  -47.33100 1.000 38.86387 ?  105 GLU B CA  1 
ATOM   3623 C  C   . GLU B 1 125 ? -35.49000 -5.72400  -46.11800 1.000 44.54026 ?  105 GLU B C   1 
ATOM   3624 O  O   . GLU B 1 125 ? -36.56300 -5.59000  -45.51800 1.000 37.81968 ?  105 GLU B O   1 
ATOM   3625 C  CB  . GLU B 1 125 ? -35.09200 -8.07500  -46.88900 1.000 36.82730 ?  105 GLU B CB  1 
ATOM   3626 C  CG  . GLU B 1 125 ? -35.03700 -8.28000  -45.38600 1.000 40.08867 ?  105 GLU B CG  1 
ATOM   3627 N  N   . LEU B 1 126 ? -34.37100 -5.07400  -45.80400 1.000 36.09070 ?  106 LEU B N   1 
ATOM   3628 C  CA  . LEU B 1 126 ? -34.29800 -4.24900  -44.58400 1.000 28.09546 ?  106 LEU B CA  1 
ATOM   3629 C  C   . LEU B 1 126 ? -34.71300 -2.80900  -44.87900 1.000 27.02689 ?  106 LEU B C   1 
ATOM   3630 O  O   . LEU B 1 126 ? -34.92600 -2.07100  -43.92800 1.000 29.78268 ?  106 LEU B O   1 
ATOM   3631 C  CB  . LEU B 1 126 ? -32.84300 -4.32400  -44.12700 1.000 31.19673 ?  106 LEU B CB  1 
ATOM   3632 C  CG  . LEU B 1 126 ? -32.41000 -5.63500  -43.48000 1.000 35.84534 ?  106 LEU B CG  1 
ATOM   3633 C  CD1 . LEU B 1 126 ? -30.89700 -5.69500  -43.36800 1.000 44.68401 ?  106 LEU B CD1 1 
ATOM   3634 C  CD2 . LEU B 1 126 ? -33.05000 -5.79200  -42.11200 1.000 42.04784 ?  106 LEU B CD2 1 
ATOM   3635 N  N   . VAL B 1 127 ? -34.88900 -2.45000  -46.14900 1.000 30.52086 ?  107 VAL B N   1 
ATOM   3636 C  CA  . VAL B 1 127 ? -35.13500 -1.03700  -46.45700 1.000 32.39560 ?  107 VAL B CA  1 
ATOM   3637 C  C   . VAL B 1 127 ? -36.34600 -0.46900  -45.72300 1.000 32.76444 ?  107 VAL B C   1 
ATOM   3638 O  O   . VAL B 1 127 ? -36.22200 0.61200   -45.12400 1.000 32.39145 ?  107 VAL B O   1 
ATOM   3639 C  CB  . VAL B 1 127 ? -35.22300 -0.83500  -47.98000 1.000 30.18520 ?  107 VAL B CB  1 
ATOM   3640 C  CG1 . VAL B 1 127 ? -35.72700 0.56400   -48.29600 1.000 28.10665 ?  107 VAL B CG1 1 
ATOM   3641 C  CG2 . VAL B 1 127 ? -33.86200 -1.06100  -48.61600 1.000 28.01639 ?  107 VAL B CG2 1 
ATOM   3642 N  N   . PRO B 1 128 ? -37.52800 -1.10900  -45.73200 1.000 30.98990 ?  108 PRO B N   1 
ATOM   3643 C  CA  . PRO B 1 128 ? -38.65800 -0.51100  -44.99600 1.000 27.54024 ?  108 PRO B CA  1 
ATOM   3644 C  C   . PRO B 1 128 ? -38.36800 -0.30300  -43.52000 1.000 28.84054 ?  108 PRO B C   1 
ATOM   3645 O  O   . PRO B 1 128 ? -38.70900 0.75200   -42.96900 1.000 27.17175 ?  108 PRO B O   1 
ATOM   3646 C  CB  . PRO B 1 128 ? -39.79600 -1.51800  -45.21400 1.000 28.61943 ?  108 PRO B CB  1 
ATOM   3647 C  CG  . PRO B 1 128 ? -39.42600 -2.24300  -46.46000 1.000 37.23207 ?  108 PRO B CG  1 
ATOM   3648 C  CD  . PRO B 1 128 ? -37.93100 -2.34300  -46.43500 1.000 31.31412 ?  108 PRO B CD  1 
ATOM   3649 N  N   . ALA B 1 129 ? -37.73100 -1.27900  -42.86600 1.000 27.75499 ?  109 ALA B N   1 
ATOM   3650 C  CA  . ALA B 1 129 ? -37.37000 -1.11400  -41.46200 1.000 28.36216 ?  109 ALA B CA  1 
ATOM   3651 C  C   . ALA B 1 129 ? -36.39300 0.03800   -41.27700 1.000 28.63924 ?  109 ALA B C   1 
ATOM   3652 O  O   . ALA B 1 129 ? -36.52300 0.82200   -40.32900 1.000 23.66791 ?  109 ALA B O   1 
ATOM   3653 C  CB  . ALA B 1 129 ? -36.77900 -2.41200  -40.90900 1.000 25.61635 ?  109 ALA B CB  1 
ATOM   3654 N  N   . ILE B 1 130 ? -35.40800 0.15500   -42.17500 1.000 26.95658 ?  110 ILE B N   1 
ATOM   3655 C  CA  . ILE B 1 130 ? -34.44200 1.24800   -42.09000 1.000 23.10740 ?  110 ILE B CA  1 
ATOM   3656 C  C   . ILE B 1 130 ? -35.15000 2.59100   -42.19900 1.000 23.94977 ?  110 ILE B C   1 
ATOM   3657 O  O   . ILE B 1 130 ? -34.90600 3.51100   -41.40900 1.000 22.25899 ?  110 ILE B O   1 
ATOM   3658 C  CB  . ILE B 1 130 ? -33.35400 1.09700   -43.16900 1.000 24.73155 ?  110 ILE B CB  1 
ATOM   3659 C  CG1 . ILE B 1 130 ? -32.51100 -0.15300  -42.91200 1.000 22.71400 ?  110 ILE B CG1 1 
ATOM   3660 C  CG2 . ILE B 1 130 ? -32.48400 2.34400   -43.23800 1.000 27.93272 ?  110 ILE B CG2 1 
ATOM   3661 C  CD1 . ILE B 1 130 ? -31.59900 -0.52500  -44.06600 1.000 25.15950 ?  110 ILE B CD1 1 
ATOM   3662 N  N   . GLU B 1 131 ? -36.04700 2.72300   -43.17700 1.000 24.75882 ?  111 GLU B N   1 
ATOM   3663 C  CA  . GLU B 1 131 ? -36.74600 3.99200   -43.35500 1.000 27.47940 ?  111 GLU B CA  1 
ATOM   3664 C  C   . GLU B 1 131 ? -37.65400 4.29000   -42.16600 1.000 24.84275 ?  111 GLU B C   1 
ATOM   3665 O  O   . GLU B 1 131 ? -37.70400 5.42800   -41.68600 1.000 20.34141 ?  111 GLU B O   1 
ATOM   3666 C  CB  . GLU B 1 131 ? -37.52400 3.96600   -44.67000 1.000 26.75000 ?  111 GLU B CB  1 
ATOM   3667 C  CG  . GLU B 1 131 ? -36.61200 3.67400   -45.86100 1.000 29.48061 ?  111 GLU B CG  1 
ATOM   3668 C  CD  . GLU B 1 131 ? -37.17900 4.11900   -47.19100 1.000 48.37037 ?  111 GLU B CD  1 
ATOM   3669 O  OE1 . GLU B 1 131 ? -38.38800 3.91100   -47.43300 1.000 49.28469 ?  111 GLU B OE1 1 
ATOM   3670 O  OE2 . GLU B 1 131 ? -36.40200 4.67100   -48.00100 1.000 49.34959 -1 111 GLU B OE2 1 
ATOM   3671 N  N   . ALA B 1 132 ? -38.35100 3.27300   -41.65400 1.000 29.48657 ?  112 ALA B N   1 
ATOM   3672 C  CA  . ALA B 1 132 ? -39.18500 3.47400   -40.47300 1.000 27.52310 ?  112 ALA B CA  1 
ATOM   3673 C  C   . ALA B 1 132 ? -38.34400 3.82700   -39.25200 1.000 23.60448 ?  112 ALA B C   1 
ATOM   3674 O  O   . ALA B 1 132 ? -38.72700 4.69800   -38.46200 1.000 23.97861 ?  112 ALA B O   1 
ATOM   3675 C  CB  . ALA B 1 132 ? -40.02600 2.22700   -40.20000 1.000 31.88303 ?  112 ALA B CB  1 
ATOM   3676 N  N   . ALA B 1 133 ? -37.19400 3.16300   -39.08300 1.000 24.47781 ?  113 ALA B N   1 
ATOM   3677 C  CA  . ALA B 1 133 ? -36.29800 3.48900   -37.97600 1.000 24.08885 ?  113 ALA B CA  1 
ATOM   3678 C  C   . ALA B 1 133 ? -35.85300 4.94300   -38.04600 1.000 24.09082 ?  113 ALA B C   1 
ATOM   3679 O  O   . ALA B 1 133 ? -35.86500 5.65800   -37.03700 1.000 25.82298 ?  113 ALA B O   1 
ATOM   3680 C  CB  . ALA B 1 133 ? -35.08600 2.55500   -37.98200 1.000 22.43745 ?  113 ALA B CB  1 
ATOM   3681 N  N   . ALA B 1 134 ? -35.46400 5.40000   -39.24100 1.000 21.84624 ?  114 ALA B N   1 
ATOM   3682 C  CA  . ALA B 1 134 ? -35.08100 6.79700   -39.41700 1.000 24.23113 ?  114 ALA B CA  1 
ATOM   3683 C  C   . ALA B 1 134 ? -36.20100 7.73600   -38.98200 1.000 24.38056 ?  114 ALA B C   1 
ATOM   3684 O  O   . ALA B 1 134 ? -35.97900 8.66400   -38.19300 1.000 25.73331 ?  114 ALA B O   1 
ATOM   3685 C  CB  . ALA B 1 134 ? -34.69700 7.05300   -40.87500 1.000 21.46692 ?  114 ALA B CB  1 
ATOM   3686 N  N   . ARG B 1 135 ? -37.41800 7.50600   -39.48400 1.000 24.11559 ?  115 ARG B N   1 
ATOM   3687 C  CA  . ARG B 1 135 ? -38.54300 8.35800   -39.10700 1.000 23.76701 ?  115 ARG B CA  1 
ATOM   3688 C  C   . ARG B 1 135 ? -38.78900 8.31800   -37.60600 1.000 22.73834 ?  115 ARG B C   1 
ATOM   3689 O  O   . ARG B 1 135 ? -39.06100 9.35100   -36.98400 1.000 23.18795 ?  115 ARG B O   1 
ATOM   3690 C  CB  . ARG B 1 135 ? -39.80200 7.93100   -39.86000 1.000 28.45073 ?  115 ARG B CB  1 
ATOM   3691 C  CG  . ARG B 1 135 ? -39.93500 8.52000   -41.25500 1.000 28.31876 ?  115 ARG B CG  1 
ATOM   3692 C  CD  . ARG B 1 135 ? -41.33900 8.29300   -41.79400 1.000 27.84821 ?  115 ARG B CD  1 
ATOM   3693 N  NE  . ARG B 1 135 ? -41.70900 6.88600   -41.71400 1.000 25.30007 ?  115 ARG B NE  1 
ATOM   3694 C  CZ  . ARG B 1 135 ? -41.42000 5.97800   -42.63700 1.000 31.12209 ?  115 ARG B CZ  1 
ATOM   3695 N  NH1 . ARG B 1 135 ? -40.77900 6.30300   -43.74800 1.000 29.69180 ?  115 ARG B NH1 1 
ATOM   3696 N  NH2 . ARG B 1 135 ? -41.78900 4.71400   -42.44200 1.000 25.03901 ?  115 ARG B NH2 1 
ATOM   3697 N  N   . GLU B 1 136 ? -38.68700 7.13200   -37.00400 1.000 19.09785 ?  116 GLU B N   1 
ATOM   3698 C  CA  . GLU B 1 136 ? -38.96900 6.99100   -35.57900 1.000 20.86523 ?  116 GLU B CA  1 
ATOM   3699 C  C   . GLU B 1 136 ? -37.92000 7.69500   -34.72600 1.000 24.22301 ?  116 GLU B C   1 
ATOM   3700 O  O   . GLU B 1 136 ? -38.26300 8.37400   -33.75100 1.000 23.74465 ?  116 GLU B O   1 
ATOM   3701 C  CB  . GLU B 1 136 ? -39.05500 5.51000   -35.22300 1.000 25.95816 ?  116 GLU B CB  1 
ATOM   3702 C  CG  . GLU B 1 136 ? -40.36800 4.87400   -35.64100 1.000 29.22905 ?  116 GLU B CG  1 
ATOM   3703 C  CD  . GLU B 1 136 ? -40.22800 3.40400   -35.97500 1.000 33.19522 ?  116 GLU B CD  1 
ATOM   3704 O  OE1 . GLU B 1 136 ? -39.24500 2.77700   -35.52600 1.000 32.06985 ?  116 GLU B OE1 1 
ATOM   3705 O  OE2 . GLU B 1 136 ? -41.10800 2.87500   -36.68600 1.000 36.50536 -1 116 GLU B OE2 1 
ATOM   3706 N  N   . LEU B 1 137 ? -36.63700 7.54100   -35.07000 1.000 22.88742 ?  117 LEU B N   1 
ATOM   3707 C  CA  . LEU B 1 137 ? -35.58400 8.19800   -34.30200 1.000 23.27802 ?  117 LEU B CA  1 
ATOM   3708 C  C   . LEU B 1 137 ? -35.70300 9.71300   -34.38900 1.000 23.42656 ?  117 LEU B C   1 
ATOM   3709 O  O   . LEU B 1 137 ? -35.59800 10.41400  -33.37600 1.000 22.51782 ?  117 LEU B O   1 
ATOM   3710 C  CB  . LEU B 1 137 ? -34.20500 7.74400   -34.78700 1.000 21.19394 ?  117 LEU B CB  1 
ATOM   3711 C  CG  . LEU B 1 137 ? -33.81000 6.29700   -34.49800 1.000 20.96304 ?  117 LEU B CG  1 
ATOM   3712 C  CD1 . LEU B 1 137 ? -32.51900 5.97200   -35.21900 1.000 20.35567 ?  117 LEU B CD1 1 
ATOM   3713 C  CD2 . LEU B 1 137 ? -33.66300 6.07000   -33.00400 1.000 22.87564 ?  117 LEU B CD2 1 
ATOM   3714 N  N   . LEU B 1 138 ? -35.92200 10.23900  -35.59700 1.000 29.49901 ?  118 LEU B N   1 
ATOM   3715 C  CA  . LEU B 1 138 ? -36.05100 11.68500  -35.75400 1.000 24.52701 ?  118 LEU B CA  1 
ATOM   3716 C  C   . LEU B 1 138 ? -37.28000 12.21600  -35.02400 1.000 28.36634 ?  118 LEU B C   1 
ATOM   3717 O  O   . LEU B 1 138 ? -37.25700 13.32500  -34.47900 1.000 34.58165 ?  118 LEU B O   1 
ATOM   3718 C  CB  . LEU B 1 138 ? -36.10700 12.05000  -37.23600 1.000 30.14820 ?  118 LEU B CB  1 
ATOM   3719 C  CG  . LEU B 1 138 ? -35.80300 13.51500  -37.54900 1.000 35.36879 ?  118 LEU B CG  1 
ATOM   3720 C  CD1 . LEU B 1 138 ? -34.44100 13.89600  -36.99700 1.000 29.70760 ?  118 LEU B CD1 1 
ATOM   3721 C  CD2 . LEU B 1 138 ? -35.86600 13.76200  -39.04200 1.000 30.89104 ?  118 LEU B CD2 1 
ATOM   3722 N  N   . ALA B 1 139 ? -38.36300 11.43700  -35.00400 1.000 28.59299 ?  119 ALA B N   1 
ATOM   3723 C  CA  . ALA B 1 139 ? -39.57900 11.86100  -34.31900 1.000 31.28889 ?  119 ALA B CA  1 
ATOM   3724 C  C   . ALA B 1 139 ? -39.37700 12.01800  -32.81800 1.000 30.44980 ?  119 ALA B C   1 
ATOM   3725 O  O   . ALA B 1 139 ? -40.13900 12.74800  -32.17500 1.000 34.17238 ?  119 ALA B O   1 
ATOM   3726 C  CB  . ALA B 1 139 ? -40.70900 10.86600  -34.59000 1.000 31.21870 ?  119 ALA B CB  1 
ATOM   3727 N  N   . GLY B 1 140 ? -38.37200 11.36000  -32.24800 1.000 36.10562 ?  120 GLY B N   1 
ATOM   3728 C  CA  . GLY B 1 140 ? -38.08100 11.48100  -30.83500 1.000 30.88375 ?  120 GLY B CA  1 
ATOM   3729 C  C   . GLY B 1 140 ? -37.33600 12.72800  -30.43400 1.000 35.36151 ?  120 GLY B C   1 
ATOM   3730 O  O   . GLY B 1 140 ? -37.15100 12.97200  -29.23900 1.000 35.26272 ?  120 GLY B O   1 
ATOM   3731 N  N   . LEU B 1 141 ? -36.89700 13.53200  -31.40100 1.000 36.08236 ?  121 LEU B N   1 
ATOM   3732 C  CA  . LEU B 1 141 ? -36.12500 14.73400  -31.12300 1.000 32.85751 ?  121 LEU B CA  1 
ATOM   3733 C  C   . LEU B 1 141 ? -37.02500 15.96500  -31.14500 1.000 36.47475 ?  121 LEU B C   1 
ATOM   3734 O  O   . LEU B 1 141 ? -37.93500 16.05500  -31.97800 1.000 31.77248 ?  121 LEU B O   1 
ATOM   3735 C  CB  . LEU B 1 141 ? -35.00500 14.89800  -32.15200 1.000 35.45800 ?  121 LEU B CB  1 
ATOM   3736 C  CG  . LEU B 1 141 ? -34.02000 13.72300  -32.19900 1.000 33.73262 ?  121 LEU B CG  1 
ATOM   3737 C  CD1 . LEU B 1 141 ? -32.92900 13.95000  -33.23200 1.000 32.49105 ?  121 LEU B CD1 1 
ATOM   3738 C  CD2 . LEU B 1 141 ? -33.40900 13.47800  -30.82300 1.000 28.44514 ?  121 LEU B CD2 1 
ATOM   3739 N  N   . PRO B 1 142 ? -36.81100 16.91600  -30.24200 1.000 41.33408 ?  122 PRO B N   1 
ATOM   3740 C  CA  . PRO B 1 142 ? -37.69600 18.08200  -30.16900 1.000 39.66045 ?  122 PRO B CA  1 
ATOM   3741 C  C   . PRO B 1 142 ? -37.42600 19.07000  -31.29400 1.000 46.91702 ?  122 PRO B C   1 
ATOM   3742 O  O   . PRO B 1 142 ? -36.36700 19.07500  -31.92400 1.000 45.25717 ?  122 PRO B O   1 
ATOM   3743 C  CB  . PRO B 1 142 ? -37.35400 18.69900  -28.80700 1.000 44.93331 ?  122 PRO B CB  1 
ATOM   3744 C  CG  . PRO B 1 142 ? -35.93900 18.29200  -28.56400 1.000 41.71688 ?  122 PRO B CG  1 
ATOM   3745 C  CD  . PRO B 1 142 ? -35.79700 16.92000  -29.17200 1.000 37.58492 ?  122 PRO B CD  1 
ATOM   3746 N  N   . SER B 1 143 ? -38.42600 19.90900  -31.54600 1.000 44.12727 ?  123 SER B N   1 
ATOM   3747 C  CA  . SER B 1 143 ? -38.30600 21.03100  -32.46200 1.000 42.87363 ?  123 SER B CA  1 
ATOM   3748 C  C   . SER B 1 143 ? -38.20200 22.32600  -31.66700 1.000 50.05763 ?  123 SER B C   1 
ATOM   3749 O  O   . SER B 1 143 ? -38.62000 22.40600  -30.51000 1.000 50.33068 ?  123 SER B O   1 
ATOM   3750 C  CB  . SER B 1 143 ? -39.49600 21.08300  -33.42800 1.000 49.63908 ?  123 SER B CB  1 
ATOM   3751 O  OG  . SER B 1 143 ? -39.72000 19.81900  -34.03300 1.000 48.89339 ?  123 SER B OG  1 
ATOM   3752 N  N   . GLY B 1 144 ? -37.62000 23.34300  -32.29800 1.000 53.96356 ?  124 GLY B N   1 
ATOM   3753 C  CA  . GLY B 1 144 ? -37.40900 24.61400  -31.63100 1.000 50.34825 ?  124 GLY B CA  1 
ATOM   3754 C  C   . GLY B 1 144 ? -36.42500 24.58700  -30.48800 1.000 60.60366 ?  124 GLY B C   1 
ATOM   3755 O  O   . GLY B 1 144 ? -36.36700 25.54400  -29.71200 1.000 66.46174 ?  124 GLY B O   1 
ATOM   3756 N  N   . GLU B 1 145 ? -35.65400 23.51200  -30.37100 1.000 55.18784 ?  125 GLU B N   1 
ATOM   3757 C  CA  . GLU B 1 145 ? -34.67600 23.27000  -29.32500 1.000 51.99371 ?  125 GLU B CA  1 
ATOM   3758 C  C   . GLU B 1 145 ? -33.38700 22.79700  -29.98900 1.000 52.48530 ?  125 GLU B C   1 
ATOM   3759 O  O   . GLU B 1 145 ? -33.44900 22.01800  -30.94300 1.000 49.26895 ?  125 GLU B O   1 
ATOM   3760 C  CB  . GLU B 1 145 ? -35.20800 22.22100  -28.31200 1.000 50.79590 ?  125 GLU B CB  1 
ATOM   3761 C  CG  . GLU B 1 145 ? -34.18100 21.46100  -27.48100 1.000 51.25286 ?  125 GLU B CG  1 
ATOM   3762 N  N   . PRO B 1 146 ? -32.21600 23.26800  -29.55100 1.000 51.36769 ?  126 PRO B N   1 
ATOM   3763 C  CA  . PRO B 1 146 ? -30.97800 22.82900  -30.19300 1.000 49.32565 ?  126 PRO B CA  1 
ATOM   3764 C  C   . PRO B 1 146 ? -30.75500 21.35100  -29.94300 1.000 45.70440 ?  126 PRO B C   1 
ATOM   3765 O  O   . PRO B 1 146 ? -30.68300 20.89700  -28.79000 1.000 46.62526 ?  126 PRO B O   1 
ATOM   3766 C  CB  . PRO B 1 146 ? -29.91000 23.72200  -29.55200 1.000 46.98618 ?  126 PRO B CB  1 
ATOM   3767 C  CG  . PRO B 1 146 ? -30.55000 24.36300  -28.33600 1.000 56.63822 ?  126 PRO B CG  1 
ATOM   3768 C  CD  . PRO B 1 146 ? -31.96100 23.84800  -28.21900 1.000 54.27802 ?  126 PRO B CD  1 
ATOM   3769 N  N   . VAL B 1 147 ? -30.70100 20.58400  -31.03300 1.000 42.62125 ?  127 VAL B N   1 
ATOM   3770 C  CA  . VAL B 1 147 ? -30.49100 19.14300  -30.98200 1.000 40.31024 ?  127 VAL B CA  1 
ATOM   3771 C  C   . VAL B 1 147 ? -29.20800 18.81900  -31.73700 1.000 39.23858 ?  127 VAL B C   1 
ATOM   3772 O  O   . VAL B 1 147 ? -28.84900 19.46800  -32.72600 1.000 40.50349 ?  127 VAL B O   1 
ATOM   3773 C  CB  . VAL B 1 147 ? -31.67900 18.33400  -31.55500 1.000 36.51895 ?  127 VAL B CB  1 
ATOM   3774 C  CG1 . VAL B 1 147 ? -32.93000 18.55300  -30.70800 1.000 43.86683 ?  127 VAL B CG1 1 
ATOM   3775 C  CG2 . VAL B 1 147 ? -31.95100 18.70400  -33.01200 1.000 41.37120 ?  127 VAL B CG2 1 
ATOM   3776 N  N   . ASP B 1 148 ? -28.49700 17.80800  -31.24100 1.000 38.46773 ?  128 ASP B N   1 
ATOM   3777 C  CA  . ASP B 1 148 ? -27.25600 17.33600  -31.85100 1.000 29.48325 ?  128 ASP B CA  1 
ATOM   3778 C  C   . ASP B 1 148 ? -27.59600 16.19500  -32.80000 1.000 27.57294 ?  128 ASP B C   1 
ATOM   3779 O  O   . ASP B 1 148 ? -28.05300 15.13200  -32.36600 1.000 30.46125 ?  128 ASP B O   1 
ATOM   3780 C  CB  . ASP B 1 148 ? -26.26900 16.89500  -30.77400 1.000 36.33583 ?  128 ASP B CB  1 
ATOM   3781 C  CG  . ASP B 1 148 ? -25.06700 16.17200  -31.34600 1.000 29.02451 ?  128 ASP B CG  1 
ATOM   3782 O  OD1 . ASP B 1 148 ? -24.66800 16.48400  -32.49000 1.000 32.32540 ?  128 ASP B OD1 1 
ATOM   3783 O  OD2 . ASP B 1 148 ? -24.51500 15.29000  -30.65700 1.000 33.22263 -1 128 ASP B OD2 1 
ATOM   3784 N  N   . LEU B 1 149 ? -27.35800 16.41900  -34.09300 1.000 28.57197 ?  129 LEU B N   1 
ATOM   3785 C  CA  . LEU B 1 149 ? -27.70200 15.43100  -35.11000 1.000 29.12855 ?  129 LEU B CA  1 
ATOM   3786 C  C   . LEU B 1 149 ? -26.96600 14.11000  -34.90300 1.000 29.31525 ?  129 LEU B C   1 
ATOM   3787 O  O   . LEU B 1 149 ? -27.52200 13.03600  -35.16400 1.000 28.80877 ?  129 LEU B O   1 
ATOM   3788 C  CB  . LEU B 1 149 ? -27.40000 15.99700  -36.49500 1.000 32.11327 ?  129 LEU B CB  1 
ATOM   3789 C  CG  . LEU B 1 149 ? -27.64200 15.04900  -37.67400 1.000 37.65152 ?  129 LEU B CG  1 
ATOM   3790 C  CD1 . LEU B 1 149 ? -29.10700 14.66500  -37.77700 1.000 38.64595 ?  129 LEU B CD1 1 
ATOM   3791 C  CD2 . LEU B 1 149 ? -27.14600 15.66400  -38.97300 1.000 45.47492 ?  129 LEU B CD2 1 
ATOM   3792 N  N   . ILE B 1 150 ? -25.71500 14.16200  -34.44600 1.000 29.56185 ?  130 ILE B N   1 
ATOM   3793 C  CA  . ILE B 1 150 ? -24.90700 12.94700  -34.37600 1.000 29.02549 ?  130 ILE B CA  1 
ATOM   3794 C  C   . ILE B 1 150 ? -25.44100 12.00500  -33.30200 1.000 29.04758 ?  130 ILE B C   1 
ATOM   3795 O  O   . ILE B 1 150 ? -25.78100 10.84900  -33.58000 1.000 33.08196 ?  130 ILE B O   1 
ATOM   3796 C  CB  . ILE B 1 150 ? -23.42600 13.28900  -34.14100 1.000 35.55628 ?  130 ILE B CB  1 
ATOM   3797 C  CG1 . ILE B 1 150 ? -22.91500 14.21800  -35.24500 1.000 27.84406 ?  130 ILE B CG1 1 
ATOM   3798 C  CG2 . ILE B 1 150 ? -22.59400 12.01700  -34.04600 1.000 36.94433 ?  130 ILE B CG2 1 
ATOM   3799 C  CD1 . ILE B 1 150 ? -23.03300 13.64000  -36.64000 1.000 36.76139 ?  130 ILE B CD1 1 
ATOM   3800 N  N   . ALA B 1 151 ? -25.51700 12.48200  -32.05900 1.000 26.46255 ?  131 ALA B N   1 
ATOM   3801 C  CA  . ALA B 1 151 ? -25.92600 11.61300  -30.96100 1.000 28.00056 ?  131 ALA B CA  1 
ATOM   3802 C  C   . ALA B 1 151 ? -27.40800 11.25700  -31.01500 1.000 27.27526 ?  131 ALA B C   1 
ATOM   3803 O  O   . ALA B 1 151 ? -27.80500 10.22800  -30.46100 1.000 23.19801 ?  131 ALA B O   1 
ATOM   3804 C  CB  . ALA B 1 151 ? -25.59800 12.27200  -29.62000 1.000 32.98883 ?  131 ALA B CB  1 
ATOM   3805 N  N   . GLY B 1 152 ? -28.23000 12.07000  -31.66800 1.000 34.73276 ?  132 GLY B N   1 
ATOM   3806 C  CA  . GLY B 1 152 ? -29.65900 11.82600  -31.66400 1.000 26.79312 ?  132 GLY B CA  1 
ATOM   3807 C  C   . GLY B 1 152 ? -30.20000 11.08900  -32.87200 1.000 29.65908 ?  132 GLY B C   1 
ATOM   3808 O  O   . GLY B 1 152 ? -31.34000 10.61500  -32.84200 1.000 24.16558 ?  132 GLY B O   1 
ATOM   3809 N  N   . PHE B 1 153 ? -29.40700 10.97500  -33.93700 1.000 23.70753 ?  133 PHE B N   1 
ATOM   3810 C  CA  . PHE B 1 153 ? -29.93200 10.45100  -35.19200 1.000 24.68308 ?  133 PHE B CA  1 
ATOM   3811 C  C   . PHE B 1 153 ? -28.85900 9.75300   -36.01500 1.000 24.54620 ?  133 PHE B C   1 
ATOM   3812 O  O   . PHE B 1 153 ? -28.99800 8.57200   -36.34600 1.000 25.10428 ?  133 PHE B O   1 
ATOM   3813 C  CB  . PHE B 1 153 ? -30.55600 11.58400  -36.01200 1.000 25.15662 ?  133 PHE B CB  1 
ATOM   3814 C  CG  . PHE B 1 153 ? -31.31900 11.11500  -37.21500 1.000 30.44860 ?  133 PHE B CG  1 
ATOM   3815 C  CD1 . PHE B 1 153 ? -32.33600 10.17800  -37.08900 1.000 31.03066 ?  133 PHE B CD1 1 
ATOM   3816 C  CD2 . PHE B 1 153 ? -31.01900 11.60900  -38.47600 1.000 25.75523 ?  133 PHE B CD2 1 
ATOM   3817 C  CE1 . PHE B 1 153 ? -33.04500 9.74700   -38.19600 1.000 24.60992 ?  133 PHE B CE1 1 
ATOM   3818 C  CE2 . PHE B 1 153 ? -31.72400 11.17900  -39.58900 1.000 33.30739 ?  133 PHE B CE2 1 
ATOM   3819 C  CZ  . PHE B 1 153 ? -32.74000 10.24600  -39.44700 1.000 28.07909 ?  133 PHE B CZ  1 
ATOM   3820 N  N   . ALA B 1 154 ? -27.78400 10.47900  -36.34600 1.000 26.31728 ?  134 ALA B N   1 
ATOM   3821 C  CA  . ALA B 1 154 ? -26.78500 9.95800   -37.27400 1.000 25.59402 ?  134 ALA B CA  1 
ATOM   3822 C  C   . ALA B 1 154 ? -26.03100 8.77000   -36.69700 1.000 24.33888 ?  134 ALA B C   1 
ATOM   3823 O  O   . ALA B 1 154 ? -25.55200 7.92000   -37.45300 1.000 24.37806 ?  134 ALA B O   1 
ATOM   3824 C  CB  . ALA B 1 154 ? -25.80500 11.06200  -37.66800 1.000 27.71113 ?  134 ALA B CB  1 
ATOM   3825 N  N   . ALA B 1 155 ? -25.89700 8.69800   -35.37900 1.000 24.27592 ?  135 ALA B N   1 
ATOM   3826 C  CA  . ALA B 1 155 ? -25.26100 7.53900   -34.76900 1.000 22.84309 ?  135 ALA B CA  1 
ATOM   3827 C  C   . ALA B 1 155 ? -26.29100 6.45800   -34.44200 1.000 20.04589 ?  135 ALA B C   1 
ATOM   3828 O  O   . ALA B 1 155 ? -26.06100 5.29000   -34.77600 1.000 26.44303 ?  135 ALA B O   1 
ATOM   3829 C  CB  . ALA B 1 155 ? -24.47400 7.94300   -33.51800 1.000 25.31710 ?  135 ALA B CB  1 
ATOM   3830 N  N   . PRO B 1 156 ? -27.42700 6.78300   -33.80500 1.000 25.97502 ?  136 PRO B N   1 
ATOM   3831 C  CA  . PRO B 1 156 ? -28.37900 5.71500   -33.45400 1.000 22.94164 ?  136 PRO B CA  1 
ATOM   3832 C  C   . PRO B 1 156 ? -28.90200 4.93000   -34.64100 1.000 17.84612 ?  136 PRO B C   1 
ATOM   3833 O  O   . PRO B 1 156 ? -29.14400 3.72300   -34.50400 1.000 23.39764 ?  136 PRO B O   1 
ATOM   3834 C  CB  . PRO B 1 156 ? -29.50700 6.48100   -32.75100 1.000 21.73865 ?  136 PRO B CB  1 
ATOM   3835 C  CG  . PRO B 1 156 ? -28.82300 7.63400   -32.14800 1.000 29.20031 ?  136 PRO B CG  1 
ATOM   3836 C  CD  . PRO B 1 156 ? -27.85200 8.06500   -33.20900 1.000 24.25346 ?  136 PRO B CD  1 
ATOM   3837 N  N   . LEU B 1 157 ? -29.08900 5.56600   -35.80900 1.000 19.88189 ?  137 LEU B N   1 
ATOM   3838 C  CA  . LEU B 1 157 ? -29.68700 4.83800   -36.92900 1.000 19.46039 ?  137 LEU B CA  1 
ATOM   3839 C  C   . LEU B 1 157 ? -28.78200 3.71400   -37.41600 1.000 17.90490 ?  137 LEU B C   1 
ATOM   3840 O  O   . LEU B 1 157 ? -29.22800 2.55300   -37.43300 1.000 18.62044 ?  137 LEU B O   1 
ATOM   3841 C  CB  . LEU B 1 157 ? -30.08800 5.81200   -38.04300 1.000 18.89112 ?  137 LEU B CB  1 
ATOM   3842 C  CG  . LEU B 1 157 ? -30.46800 5.13700   -39.36900 1.000 20.37653 ?  137 LEU B CG  1 
ATOM   3843 C  CD1 . LEU B 1 157 ? -31.70500 4.26200   -39.20600 1.000 23.15078 ?  137 LEU B CD1 1 
ATOM   3844 C  CD2 . LEU B 1 157 ? -30.66900 6.16200   -40.47300 1.000 25.38812 ?  137 LEU B CD2 1 
ATOM   3845 N  N   . PRO B 1 158 ? -27.52700 3.96000   -37.82000 1.000 21.04455 ?  138 PRO B N   1 
ATOM   3846 C  CA  . PRO B 1 158 ? -26.67100 2.82600   -38.20000 1.000 17.99950 ?  138 PRO B CA  1 
ATOM   3847 C  C   . PRO B 1 158 ? -26.41700 1.86500   -37.05500 1.000 17.25284 ?  138 PRO B C   1 
ATOM   3848 O  O   . PRO B 1 158 ? -26.22100 0.66700   -37.29700 1.000 17.91036 ?  138 PRO B O   1 
ATOM   3849 C  CB  . PRO B 1 158 ? -25.37200 3.50100   -38.66400 1.000 24.59676 ?  138 PRO B CB  1 
ATOM   3850 C  CG  . PRO B 1 158 ? -25.42500 4.85300   -38.08700 1.000 23.16310 ?  138 PRO B CG  1 
ATOM   3851 C  CD  . PRO B 1 158 ? -26.86300 5.23000   -38.13700 1.000 21.52443 ?  138 PRO B CD  1 
ATOM   3852 N  N   . LEU B 1 159 ? -26.40900 2.35400   -35.81200 1.000 18.83252 ?  139 LEU B N   1 
ATOM   3853 C  CA  . LEU B 1 159 ? -26.25100 1.45100   -34.67500 1.000 21.03835 ?  139 LEU B CA  1 
ATOM   3854 C  C   . LEU B 1 159 ? -27.40500 0.46100   -34.60400 1.000 20.30448 ?  139 LEU B C   1 
ATOM   3855 O  O   . LEU B 1 159 ? -27.19300 -0.74100  -34.40600 1.000 20.01023 ?  139 LEU B O   1 
ATOM   3856 C  CB  . LEU B 1 159 ? -26.13900 2.25100   -33.37700 1.000 24.39466 ?  139 LEU B CB  1 
ATOM   3857 C  CG  . LEU B 1 159 ? -25.60500 1.51600   -32.14400 1.000 33.13497 ?  139 LEU B CG  1 
ATOM   3858 C  CD1 . LEU B 1 159 ? -24.17000 1.04800   -32.35500 1.000 27.17165 ?  139 LEU B CD1 1 
ATOM   3859 C  CD2 . LEU B 1 159 ? -25.69600 2.41000   -30.91400 1.000 39.36259 ?  139 LEU B CD2 1 
ATOM   3860 N  N   . ARG B 1 160 ? -28.63500 0.94700   -34.78300 1.000 17.05108 ?  140 ARG B N   1 
ATOM   3861 C  CA  . ARG B 1 160 ? -29.78400 0.04700   -34.79600 1.000 20.69310 ?  140 ARG B CA  1 
ATOM   3862 C  C   . ARG B 1 160 ? -29.70600 -0.94100  -35.95400 1.000 19.99527 ?  140 ARG B C   1 
ATOM   3863 O  O   . ARG B 1 160 ? -29.95800 -2.14000  -35.77300 1.000 21.46946 ?  140 ARG B O   1 
ATOM   3864 C  CB  . ARG B 1 160 ? -31.08000 0.86300   -34.84700 1.000 22.48973 ?  140 ARG B CB  1 
ATOM   3865 C  CG  . ARG B 1 160 ? -32.30700 0.07700   -35.27300 1.000 26.76317 ?  140 ARG B CG  1 
ATOM   3866 C  CD  . ARG B 1 160 ? -32.82400 -0.86200  -34.18900 1.000 29.34697 ?  140 ARG B CD  1 
ATOM   3867 N  NE  . ARG B 1 160 ? -33.90800 -1.70800  -34.68200 1.000 30.83204 ?  140 ARG B NE  1 
ATOM   3868 C  CZ  . ARG B 1 160 ? -35.02800 -1.27300  -35.25000 1.000 38.19737 ?  140 ARG B CZ  1 
ATOM   3869 N  NH1 . ARG B 1 160 ? -35.39500 -0.00100  -35.19200 1.000 32.82085 ?  140 ARG B NH1 1 
ATOM   3870 N  NH2 . ARG B 1 160 ? -35.82400 -2.14700  -35.86200 1.000 29.54901 ?  140 ARG B NH2 1 
ATOM   3871 N  N   . VAL B 1 161 ? -29.32800 -0.46300  -37.14100 1.000 18.88576 ?  141 VAL B N   1 
ATOM   3872 C  CA  . VAL B 1 161 ? -29.28200 -1.35300  -38.34800 1.000 18.21715 ?  141 VAL B CA  1 
ATOM   3873 C  C   . VAL B 1 161 ? -28.22800 -2.45200  -38.15600 1.000 21.74197 ?  141 VAL B C   1 
ATOM   3874 O  O   . VAL B 1 161 ? -28.55900 -3.61500  -38.36100 1.000 19.43422 ?  141 VAL B O   1 
ATOM   3875 C  CB  . VAL B 1 161 ? -29.06600 -0.57800  -39.66500 1.000 22.03820 ?  141 VAL B CB  1 
ATOM   3876 C  CG1 . VAL B 1 161 ? -29.07700 -1.51000  -40.86400 1.000 17.40208 ?  141 VAL B CG1 1 
ATOM   3877 C  CG2 . VAL B 1 161 ? -30.10100 0.52000   -39.83500 1.000 25.15289 ?  141 VAL B CG2 1 
ATOM   3878 N  N   . ILE B 1 162 ? -26.99600 -2.08900  -37.78200 1.000 19.56953 ?  142 ILE B N   1 
ATOM   3879 C  CA  . ILE B 1 162 ? -25.93400 -3.13500  -37.64800 1.000 19.11724 ?  142 ILE B CA  1 
ATOM   3880 C  C   . ILE B 1 162 ? -26.29700 -4.08200  -36.49500 1.000 16.63993 ?  142 ILE B C   1 
ATOM   3881 O  O   . ILE B 1 162 ? -26.01900 -5.25700  -36.60300 1.000 23.99887 ?  142 ILE B O   1 
ATOM   3882 C  CB  . ILE B 1 162 ? -24.52200 -2.53100  -37.50300 1.000 25.52167 ?  142 ILE B CB  1 
ATOM   3883 C  CG1 . ILE B 1 162 ? -23.44100 -3.52200  -37.93100 1.000 23.60850 ?  142 ILE B CG1 1 
ATOM   3884 C  CG2 . ILE B 1 162 ? -24.28600 -1.99400  -36.09900 1.000 25.92366 ?  142 ILE B CG2 1 
ATOM   3885 C  CD1 . ILE B 1 162 ? -23.42700 -3.77900  -39.40900 1.000 31.72253 ?  142 ILE B CD1 1 
ATOM   3886 N  N   . GLY B 1 163 ? -26.97100 -3.57900  -35.47200 1.000 18.93107 ?  143 GLY B N   1 
ATOM   3887 C  CA  . GLY B 1 163 ? -27.44300 -4.46700  -34.39800 1.000 22.64610 ?  143 GLY B CA  1 
ATOM   3888 C  C   . GLY B 1 163 ? -28.43700 -5.47900  -34.93100 1.000 20.48060 ?  143 GLY B C   1 
ATOM   3889 O  O   . GLY B 1 163 ? -28.32700 -6.64300  -34.58700 1.000 21.77022 ?  143 GLY B O   1 
ATOM   3890 N  N   . ASP B 1 164 ? -29.35600 -5.02000  -35.77300 1.000 22.07578 ?  144 ASP B N   1 
ATOM   3891 C  CA  . ASP B 1 164 ? -30.32500 -5.94400  -36.41300 1.000 23.44450 ?  144 ASP B CA  1 
ATOM   3892 C  C   . ASP B 1 164 ? -29.58100 -6.92400  -37.33400 1.000 23.83484 ?  144 ASP B C   1 
ATOM   3893 O  O   . ASP B 1 164 ? -29.93600 -8.10100  -37.33900 1.000 22.73278 ?  144 ASP B O   1 
ATOM   3894 C  CB  . ASP B 1 164 ? -31.42300 -5.17800  -37.15600 1.000 27.97188 ?  144 ASP B CB  1 
ATOM   3895 C  CG  . ASP B 1 164 ? -32.39800 -4.41200  -36.28000 1.000 26.89643 ?  144 ASP B CG  1 
ATOM   3896 O  OD1 . ASP B 1 164 ? -32.21000 -4.39700  -35.05800 1.000 29.36797 ?  144 ASP B OD1 1 
ATOM   3897 O  OD2 . ASP B 1 164 ? -33.34300 -3.83800  -36.83900 1.000 31.54712 -1 144 ASP B OD2 1 
ATOM   3898 N  N   . LEU B 1 165 ? -28.59300 -6.43700  -38.07300 1.000 23.42350 ?  145 LEU B N   1 
ATOM   3899 C  CA  . LEU B 1 165 ? -27.83600 -7.28900  -39.02400 1.000 27.73957 ?  145 LEU B CA  1 
ATOM   3900 C  C   . LEU B 1 165 ? -27.07800 -8.38800  -38.27800 1.000 24.87941 ?  145 LEU B C   1 
ATOM   3901 O  O   . LEU B 1 165 ? -27.02900 -9.50300  -38.78400 1.000 29.57998 ?  145 LEU B O   1 
ATOM   3902 C  CB  . LEU B 1 165 ? -26.87600 -6.40300  -39.82200 1.000 25.50830 ?  145 LEU B CB  1 
ATOM   3903 C  CG  . LEU B 1 165 ? -26.18700 -7.11000  -40.98700 1.000 41.23310 ?  145 LEU B CG  1 
ATOM   3904 C  CD1 . LEU B 1 165 ? -27.17000 -7.38700  -42.11000 1.000 34.72769 ?  145 LEU B CD1 1 
ATOM   3905 C  CD2 . LEU B 1 165 ? -24.99900 -6.31700  -41.49800 1.000 38.89435 ?  145 LEU B CD2 1 
ATOM   3906 N  N   . LEU B 1 166 ? -26.53800 -8.07000  -37.10900 1.000 23.56223 ?  146 LEU B N   1 
ATOM   3907 C  CA  . LEU B 1 166 ? -25.73800 -9.04100  -36.31900 1.000 25.42116 ?  146 LEU B CA  1 
ATOM   3908 C  C   . LEU B 1 166 ? -26.64200 -9.82400  -35.36300 1.000 22.59191 ?  146 LEU B C   1 
ATOM   3909 O  O   . LEU B 1 166 ? -26.13200 -10.71300 -34.69700 1.000 24.26059 ?  146 LEU B O   1 
ATOM   3910 C  CB  . LEU B 1 166 ? -24.69000 -8.24500  -35.53900 1.000 27.86256 ?  146 LEU B CB  1 
ATOM   3911 C  CG  . LEU B 1 166 ? -23.62900 -7.53500  -36.38000 1.000 26.39825 ?  146 LEU B CG  1 
ATOM   3912 C  CD1 . LEU B 1 166 ? -22.66700 -6.76100  -35.49500 1.000 21.03483 ?  146 LEU B CD1 1 
ATOM   3913 C  CD2 . LEU B 1 166 ? -22.87200 -8.52500  -37.24800 1.000 20.25351 ?  146 LEU B CD2 1 
ATOM   3914 N  N   . GLY B 1 167 ? -27.91800 -9.44500  -35.28400 1.000 24.25999 ?  147 GLY B N   1 
ATOM   3915 C  CA  . GLY B 1 167 ? -28.87900 -10.16200 -34.42700 1.000 23.22769 ?  147 GLY B CA  1 
ATOM   3916 C  C   . GLY B 1 167 ? -28.65000 -9.93900  -32.94200 1.000 22.10167 ?  147 GLY B C   1 
ATOM   3917 O  O   . GLY B 1 167 ? -28.79200 -10.88400 -32.17900 1.000 27.34653 ?  147 GLY B O   1 
ATOM   3918 N  N   . VAL B 1 168 ? -28.34600 -8.70600  -32.55300 1.000 23.41305 ?  148 VAL B N   1 
ATOM   3919 C  CA  . VAL B 1 168 ? -28.13500 -8.40100  -31.14000 1.000 18.02219 ?  148 VAL B CA  1 
ATOM   3920 C  C   . VAL B 1 168 ? -29.46000 -8.55700  -30.40300 1.000 20.28718 ?  148 VAL B C   1 
ATOM   3921 O  O   . VAL B 1 168 ? -30.42300 -7.84400  -30.71400 1.000 21.55778 ?  148 VAL B O   1 
ATOM   3922 C  CB  . VAL B 1 168 ? -27.55700 -6.99200  -30.95300 1.000 20.74522 ?  148 VAL B CB  1 
ATOM   3923 C  CG1 . VAL B 1 168 ? -27.34300 -6.70100  -29.47800 1.000 21.32198 ?  148 VAL B CG1 1 
ATOM   3924 C  CG2 . VAL B 1 168 ? -26.24400 -6.85900  -31.72600 1.000 23.43528 ?  148 VAL B CG2 1 
ATOM   3925 N  N   . PRO B 1 169 ? -29.55800 -9.47200  -29.43300 1.000 23.70922 ?  149 PRO B N   1 
ATOM   3926 C  CA  . PRO B 1 169 ? -30.83300 -9.66900  -28.74200 1.000 26.15338 ?  149 PRO B CA  1 
ATOM   3927 C  C   . PRO B 1 169 ? -31.21300 -8.43900  -27.93900 1.000 27.77426 ?  149 PRO B C   1 
ATOM   3928 O  O   . PRO B 1 169 ? -30.34500 -7.63800  -27.55000 1.000 22.53355 ?  149 PRO B O   1 
ATOM   3929 C  CB  . PRO B 1 169 ? -30.55700 -10.87800 -27.82800 1.000 23.23686 ?  149 PRO B CB  1 
ATOM   3930 C  CG  . PRO B 1 169 ? -29.36800 -11.55100 -28.44500 1.000 28.01579 ?  149 PRO B CG  1 
ATOM   3931 C  CD  . PRO B 1 169 ? -28.53800 -10.42900 -28.97900 1.000 27.44788 ?  149 PRO B CD  1 
ATOM   3932 N  N   . PRO B 1 170 ? -32.51000 -8.24100  -27.67000 1.000 26.36005 ?  150 PRO B N   1 
ATOM   3933 C  CA  . PRO B 1 170 ? -32.94400 -7.01800  -26.97300 1.000 27.33078 ?  150 PRO B CA  1 
ATOM   3934 C  C   . PRO B 1 170 ? -32.22200 -6.75500  -25.66200 1.000 24.20268 ?  150 PRO B C   1 
ATOM   3935 O  O   . PRO B 1 170 ? -31.92700 -5.59500  -25.35300 1.000 26.07722 ?  150 PRO B O   1 
ATOM   3936 C  CB  . PRO B 1 170 ? -34.44000 -7.27500  -26.74900 1.000 28.94150 ?  150 PRO B CB  1 
ATOM   3937 C  CG  . PRO B 1 170 ? -34.82900 -8.11900  -27.90500 1.000 33.96502 ?  150 PRO B CG  1 
ATOM   3938 C  CD  . PRO B 1 170 ? -33.65400 -9.03800  -28.14300 1.000 27.70032 ?  150 PRO B CD  1 
ATOM   3939 N  N   . ALA B 1 171 ? -31.92200 -7.79700  -24.88500 1.000 23.66003 ?  151 ALA B N   1 
ATOM   3940 C  CA  . ALA B 1 171 ? -31.26000 -7.62000  -23.59900 1.000 24.54897 ?  151 ALA B CA  1 
ATOM   3941 C  C   . ALA B 1 171 ? -29.79200 -7.24900  -23.73600 1.000 26.29489 ?  151 ALA B C   1 
ATOM   3942 O  O   . ALA B 1 171 ? -29.18900 -6.81800  -22.75000 1.000 22.82142 ?  151 ALA B O   1 
ATOM   3943 C  CB  . ALA B 1 171 ? -31.38800 -8.89300  -22.75900 1.000 32.04228 ?  151 ALA B CB  1 
ATOM   3944 N  N   . ASP B 1 172 ? -29.20800 -7.40300  -24.92200 1.000 21.38960 ?  152 ASP B N   1 
ATOM   3945 C  CA  . ASP B 1 172 ? -27.80700 -7.08400  -25.15100 1.000 30.03448 ?  152 ASP B CA  1 
ATOM   3946 C  C   . ASP B 1 172 ? -27.61000 -5.74900  -25.85500 1.000 22.39164 ?  152 ASP B C   1 
ATOM   3947 O  O   . ASP B 1 172 ? -26.46400 -5.35300  -26.08800 1.000 24.39795 ?  152 ASP B O   1 
ATOM   3948 C  CB  . ASP B 1 172 ? -27.13800 -8.19800  -25.96600 1.000 24.88453 ?  152 ASP B CB  1 
ATOM   3949 C  CG  . ASP B 1 172 ? -27.16200 -9.53800  -25.25400 1.000 33.05052 ?  152 ASP B CG  1 
ATOM   3950 O  OD1 . ASP B 1 172 ? -26.90800 -9.57800  -24.03200 1.000 31.43429 ?  152 ASP B OD1 1 
ATOM   3951 O  OD2 . ASP B 1 172 ? -27.44900 -10.55500 -25.91700 1.000 36.62268 -1 152 ASP B OD2 1 
ATOM   3952 N  N   . ARG B 1 173 ? -28.69500 -5.03700  -26.17900 1.000 25.06849 ?  153 ARG B N   1 
ATOM   3953 C  CA  . ARG B 1 173 ? -28.57400 -3.84300  -27.01200 1.000 25.48475 ?  153 ARG B CA  1 
ATOM   3954 C  C   . ARG B 1 173 ? -27.86900 -2.70800  -26.28200 1.000 25.03674 ?  153 ARG B C   1 
ATOM   3955 O  O   . ARG B 1 173 ? -27.03900 -2.00800  -26.87500 1.000 21.93113 ?  153 ARG B O   1 
ATOM   3956 C  CB  . ARG B 1 173 ? -29.95000 -3.39200  -27.49700 1.000 24.72877 ?  153 ARG B CB  1 
ATOM   3957 C  CG  . ARG B 1 173 ? -30.59000 -4.33500  -28.49900 1.000 25.68088 ?  153 ARG B CG  1 
ATOM   3958 C  CD  . ARG B 1 173 ? -30.19300 -3.95700  -29.92400 1.000 25.85679 ?  153 ARG B CD  1 
ATOM   3959 N  NE  . ARG B 1 173 ? -30.52600 -5.01200  -30.87500 1.000 24.47303 ?  153 ARG B NE  1 
ATOM   3960 C  CZ  . ARG B 1 173 ? -30.76000 -4.81900  -32.16700 1.000 26.97546 ?  153 ARG B CZ  1 
ATOM   3961 N  NH1 . ARG B 1 173 ? -30.69700 -3.61400  -32.71000 1.000 25.07694 ?  153 ARG B NH1 1 
ATOM   3962 N  NH2 . ARG B 1 173 ? -31.07700 -5.86000  -32.93100 1.000 21.76344 ?  153 ARG B NH2 1 
ATOM   3963 N  N   . ALA B 1 174 ? -28.19200 -2.49500  -25.00300 1.000 19.54523 ?  154 ALA B N   1 
ATOM   3964 C  CA  . ALA B 1 174 ? -27.55400 -1.40500  -24.26900 1.000 21.99358 ?  154 ALA B CA  1 
ATOM   3965 C  C   . ALA B 1 174 ? -26.05100 -1.63000  -24.14700 1.000 17.49885 ?  154 ALA B C   1 
ATOM   3966 O  O   . ALA B 1 174 ? -25.26100 -0.68800  -24.28800 1.000 21.61889 ?  154 ALA B O   1 
ATOM   3967 C  CB  . ALA B 1 174 ? -28.18600 -1.25200  -22.88700 1.000 24.12617 ?  154 ALA B CB  1 
ATOM   3968 N  N   . ARG B 1 175 ? -25.64200 -2.87600  -23.88600 1.000 19.60924 ?  155 ARG B N   1 
ATOM   3969 C  CA  . ARG B 1 175 ? -24.22000 -3.21600  -23.83200 1.000 21.54758 ?  155 ARG B CA  1 
ATOM   3970 C  C   . ARG B 1 175 ? -23.55900 -3.02700  -25.19200 1.000 19.74561 ?  155 ARG B C   1 
ATOM   3971 O  O   . ARG B 1 175 ? -22.45200 -2.48200  -25.29000 1.000 20.99446 ?  155 ARG B O   1 
ATOM   3972 C  CB  . ARG B 1 175 ? -24.07000 -4.66400  -23.35700 1.000 19.83252 ?  155 ARG B CB  1 
ATOM   3973 C  CG  . ARG B 1 175 ? -22.65500 -5.18900  -23.21100 1.000 29.85348 ?  155 ARG B CG  1 
ATOM   3974 C  CD  . ARG B 1 175 ? -22.69400 -6.64700  -22.75200 1.000 33.44662 ?  155 ARG B CD  1 
ATOM   3975 N  NE  . ARG B 1 175 ? -21.44800 -7.36400  -23.01100 1.000 40.16330 ?  155 ARG B NE  1 
ATOM   3976 C  CZ  . ARG B 1 175 ? -21.31800 -8.68400  -22.96300 1.000 33.59268 ?  155 ARG B CZ  1 
ATOM   3977 N  NH1 . ARG B 1 175 ? -22.35400 -9.47500  -22.72900 1.000 36.41491 ?  155 ARG B NH1 1 
ATOM   3978 N  NH2 . ARG B 1 175 ? -20.11700 -9.22700  -23.15400 1.000 27.41373 ?  155 ARG B NH2 1 
ATOM   3979 N  N   . PHE B 1 176 ? -24.23100 -3.47700  -26.25200 1.000 15.27602 ?  156 PHE B N   1 
ATOM   3980 C  CA  . PHE B 1 176 ? -23.72400 -3.30900  -27.61000 1.000 18.96790 ?  156 PHE B CA  1 
ATOM   3981 C  C   . PHE B 1 176 ? -23.55100 -1.83700  -27.96300 1.000 18.06265 ?  156 PHE B C   1 
ATOM   3982 O  O   . PHE B 1 176 ? -22.52800 -1.44400  -28.53800 1.000 20.71230 ?  156 PHE B O   1 
ATOM   3983 C  CB  . PHE B 1 176 ? -24.68600 -4.00000  -28.58000 1.000 20.25520 ?  156 PHE B CB  1 
ATOM   3984 C  CG  . PHE B 1 176 ? -24.30700 -3.87900  -30.02400 1.000 16.89465 ?  156 PHE B CG  1 
ATOM   3985 C  CD1 . PHE B 1 176 ? -23.16200 -4.49100  -30.50900 1.000 20.56129 ?  156 PHE B CD1 1 
ATOM   3986 C  CD2 . PHE B 1 176 ? -25.12300 -3.18400  -30.91100 1.000 20.63516 ?  156 PHE B CD2 1 
ATOM   3987 C  CE1 . PHE B 1 176 ? -22.82100 -4.38700  -31.85100 1.000 26.27168 ?  156 PHE B CE1 1 
ATOM   3988 C  CE2 . PHE B 1 176 ? -24.78500 -3.08300  -32.24900 1.000 18.92665 ?  156 PHE B CE2 1 
ATOM   3989 C  CZ  . PHE B 1 176 ? -23.63500 -3.68400  -32.71600 1.000 23.43918 ?  156 PHE B CZ  1 
ATOM   3990 N  N   . ARG B 1 177 ? -24.53800 -1.00800  -27.61000 1.000 17.90113 ?  157 ARG B N   1 
ATOM   3991 C  CA  . ARG B 1 177 ? -24.49700 0.41400   -27.94100 1.000 22.26576 ?  157 ARG B CA  1 
ATOM   3992 C  C   . ARG B 1 177 ? -23.33000 1.11200   -27.25400 1.000 24.07547 ?  157 ARG B C   1 
ATOM   3993 O  O   . ARG B 1 177 ? -22.56700 1.84600   -27.89100 1.000 21.32229 ?  157 ARG B O   1 
ATOM   3994 C  CB  . ARG B 1 177 ? -25.81700 1.07300   -27.53700 1.000 26.29722 ?  157 ARG B CB  1 
ATOM   3995 C  CG  . ARG B 1 177 ? -26.99800 0.70400   -28.41600 1.000 33.00967 ?  157 ARG B CG  1 
ATOM   3996 C  CD  . ARG B 1 177 ? -28.20600 1.56800   -28.10200 1.000 37.14674 ?  157 ARG B CD  1 
ATOM   3997 N  NE  . ARG B 1 177 ? -29.44600 0.93100   -28.52800 1.000 37.95098 ?  157 ARG B NE  1 
ATOM   3998 C  CZ  . ARG B 1 177 ? -30.34200 0.41000   -27.70000 1.000 38.90879 ?  157 ARG B CZ  1 
ATOM   3999 N  NH1 . ARG B 1 177 ? -30.16600 0.43200   -26.38600 1.000 33.04877 ?  157 ARG B NH1 1 
ATOM   4000 N  NH2 . ARG B 1 177 ? -31.44200 -0.14600  -28.20100 1.000 47.19528 ?  157 ARG B NH2 1 
ATOM   4001 N  N   . GLY B 1 178 ? -23.19000 0.91200   -25.94400 1.000 23.38847 ?  158 GLY B N   1 
ATOM   4002 C  CA  . GLY B 1 178 ? -22.16200 1.63000   -25.21000 1.000 26.24383 ?  158 GLY B CA  1 
ATOM   4003 C  C   . GLY B 1 178 ? -20.76400 1.27800   -25.66800 1.000 21.46775 ?  158 GLY B C   1 
ATOM   4004 O  O   . GLY B 1 178 ? -19.89200 2.14800   -25.75600 1.000 27.24039 ?  158 GLY B O   1 
ATOM   4005 N  N   . TRP B 1 179 ? -20.53100 0.00600   -25.98500 1.000 18.22421 ?  159 TRP B N   1 
ATOM   4006 C  CA  . TRP B 1 179 ? -19.19500 -0.39900  -26.39100 1.000 22.67096 ?  159 TRP B CA  1 
ATOM   4007 C  C   . TRP B 1 179 ? -18.91600 -0.07800  -27.85400 1.000 23.03618 ?  159 TRP B C   1 
ATOM   4008 O  O   . TRP B 1 179 ? -17.78300 0.27000   -28.18700 1.000 19.99399 ?  159 TRP B O   1 
ATOM   4009 C  CB  . TRP B 1 179 ? -18.99400 -1.88300  -26.09300 1.000 25.10086 ?  159 TRP B CB  1 
ATOM   4010 C  CG  . TRP B 1 179 ? -18.64800 -2.13600  -24.63700 1.000 28.11364 ?  159 TRP B CG  1 
ATOM   4011 C  CD1 . TRP B 1 179 ? -19.22100 -3.05500  -23.81200 1.000 25.94051 ?  159 TRP B CD1 1 
ATOM   4012 C  CD2 . TRP B 1 179 ? -17.62800 -1.48200  -23.85600 1.000 34.95763 ?  159 TRP B CD2 1 
ATOM   4013 N  NE1 . TRP B 1 179 ? -18.64600 -3.00400  -22.56500 1.000 23.87163 ?  159 TRP B NE1 1 
ATOM   4014 C  CE2 . TRP B 1 179 ? -17.66100 -2.05100  -22.56700 1.000 32.98013 ?  159 TRP B CE2 1 
ATOM   4015 C  CE3 . TRP B 1 179 ? -16.69200 -0.47200  -24.12200 1.000 32.12392 ?  159 TRP B CE3 1 
ATOM   4016 C  CZ2 . TRP B 1 179 ? -16.79200 -1.64400  -21.54300 1.000 31.30362 ?  159 TRP B CZ2 1 
ATOM   4017 C  CZ3 . TRP B 1 179 ? -15.83500 -0.06500  -23.10200 1.000 28.60550 ?  159 TRP B CZ3 1 
ATOM   4018 C  CH2 . TRP B 1 179 ? -15.89200 -0.65200  -21.83100 1.000 28.17030 ?  159 TRP B CH2 1 
ATOM   4019 N  N   . THR B 1 180 ? -19.92300 -0.15500  -28.73100 1.000 18.99759 ?  160 THR B N   1 
ATOM   4020 C  CA  . THR B 1 180 ? -19.72400 0.30600   -30.10400 1.000 18.17981 ?  160 THR B CA  1 
ATOM   4021 C  C   . THR B 1 180 ? -19.39600 1.79300   -30.14300 1.000 17.36601 ?  160 THR B C   1 
ATOM   4022 O  O   . THR B 1 180 ? -18.48600 2.21600   -30.86800 1.000 21.75329 ?  160 THR B O   1 
ATOM   4023 C  CB  . THR B 1 180 ? -20.96200 0.01600   -30.95400 1.000 19.39490 ?  160 THR B CB  1 
ATOM   4024 O  OG1 . THR B 1 180 ? -21.27900 -1.37700  -30.87700 1.000 15.50357 ?  160 THR B OG1 1 
ATOM   4025 C  CG2 . THR B 1 180 ? -20.71200 0.39700   -32.41100 1.000 18.84891 ?  160 THR B CG2 1 
ATOM   4026 N  N   . THR B 1 181 ? -20.12400 2.60200   -29.36600 1.000 17.71680 ?  161 THR B N   1 
ATOM   4027 C  CA  . THR B 1 181 ? -19.88200 4.04200   -29.35800 1.000 21.40101 ?  161 THR B CA  1 
ATOM   4028 C  C   . THR B 1 181 ? -18.50000 4.36900   -28.79800 1.000 23.01667 ?  161 THR B C   1 
ATOM   4029 O  O   . THR B 1 181 ? -17.77000 5.19400   -29.35800 1.000 24.84096 ?  161 THR B O   1 
ATOM   4030 C  CB  . THR B 1 181 ? -20.96700 4.75200   -28.55200 1.000 21.74627 ?  161 THR B CB  1 
ATOM   4031 O  OG1 . THR B 1 181 ? -21.10200 4.11800   -27.27400 1.000 31.89821 ?  161 THR B OG1 1 
ATOM   4032 C  CG2 . THR B 1 181 ? -22.30300 4.68300   -29.29500 1.000 22.14870 ?  161 THR B CG2 1 
ATOM   4033 N  N   . THR B 1 182 ? -18.12600 3.72900   -27.68800 1.000 23.23924 ?  162 THR B N   1 
ATOM   4034 C  CA  . THR B 1 182 ? -16.80100 3.95400   -27.11300 1.000 20.47008 ?  162 THR B CA  1 
ATOM   4035 C  C   . THR B 1 182 ? -15.69500 3.46400   -28.03800 1.000 21.78215 ?  162 THR B C   1 
ATOM   4036 O  O   . THR B 1 182 ? -14.60800 4.05300   -28.07800 1.000 21.88315 ?  162 THR B O   1 
ATOM   4037 C  CB  . THR B 1 182 ? -16.70300 3.26000   -25.75200 1.000 19.42392 ?  162 THR B CB  1 
ATOM   4038 O  OG1 . THR B 1 182 ? -17.73700 3.75000   -24.89200 1.000 22.47082 ?  162 THR B OG1 1 
ATOM   4039 C  CG2 . THR B 1 182 ? -15.34700 3.52000   -25.10000 1.000 17.20212 ?  162 THR B CG2 1 
ATOM   4040 N  N   . LEU B 1 183 ? -15.95400 2.39800   -28.79500 1.000 19.22390 ?  163 LEU B N   1 
ATOM   4041 C  CA  . LEU B 1 183 ? -14.92800 1.84200   -29.67000 1.000 21.90348 ?  163 LEU B CA  1 
ATOM   4042 C  C   . LEU B 1 183 ? -14.69400 2.71800   -30.89400 1.000 21.83193 ?  163 LEU B C   1 
ATOM   4043 O  O   . LEU B 1 183 ? -13.54600 2.89500   -31.32400 1.000 19.05746 ?  163 LEU B O   1 
ATOM   4044 C  CB  . LEU B 1 183 ? -15.32400 0.43100   -30.09400 1.000 18.38630 ?  163 LEU B CB  1 
ATOM   4045 C  CG  . LEU B 1 183 ? -14.42100 -0.31600  -31.07100 1.000 22.20314 ?  163 LEU B CG  1 
ATOM   4046 C  CD1 . LEU B 1 183 ? -13.11200 -0.68200  -30.40100 1.000 21.77076 ?  163 LEU B CD1 1 
ATOM   4047 C  CD2 . LEU B 1 183 ? -15.13400 -1.55900  -31.58900 1.000 17.32798 ?  163 LEU B CD2 1 
ATOM   4048 N  N   . LEU B 1 184 ? -15.76200 3.27400   -31.46700 1.000 20.31490 ?  164 LEU B N   1 
ATOM   4049 C  CA  . LEU B 1 184 ? -15.70300 3.84200   -32.80900 1.000 24.55654 ?  164 LEU B CA  1 
ATOM   4050 C  C   . LEU B 1 184 ? -16.10000 5.30700   -32.90000 1.000 22.94245 ?  164 LEU B C   1 
ATOM   4051 O  O   . LEU B 1 184 ? -15.60200 6.00100   -33.78900 1.000 26.71175 ?  164 LEU B O   1 
ATOM   4052 C  CB  . LEU B 1 184 ? -16.59100 3.03000   -33.76600 1.000 20.32676 ?  164 LEU B CB  1 
ATOM   4053 C  CG  . LEU B 1 184 ? -16.15100 1.57600   -33.91900 1.000 20.65473 ?  164 LEU B CG  1 
ATOM   4054 C  CD1 . LEU B 1 184 ? -17.19300 0.75100   -34.65200 1.000 22.84697 ?  164 LEU B CD1 1 
ATOM   4055 C  CD2 . LEU B 1 184 ? -14.79000 1.49500   -34.61700 1.000 20.98293 ?  164 LEU B CD2 1 
ATOM   4056 N  N   . THR B 1 185 ? -16.97000 5.80400   -32.02200 1.000 22.70760 ?  165 THR B N   1 
ATOM   4057 C  CA  . THR B 1 185 ? -17.36600 7.21300   -32.02000 1.000 31.15617 ?  165 THR B CA  1 
ATOM   4058 C  C   . THR B 1 185 ? -17.07700 7.84300   -30.66100 1.000 33.73418 ?  165 THR B C   1 
ATOM   4059 O  O   . THR B 1 185 ? -17.99600 8.29900   -29.97000 1.000 28.54914 ?  165 THR B O   1 
ATOM   4060 C  CB  . THR B 1 185 ? -18.84100 7.37500   -32.37400 1.000 32.98826 ?  165 THR B CB  1 
ATOM   4061 O  OG1 . THR B 1 185 ? -19.61800 6.38000   -31.69000 1.000 24.21681 ?  165 THR B OG1 1 
ATOM   4062 C  CG2 . THR B 1 185 ? -19.03500 7.24500   -33.88000 1.000 26.76326 ?  165 THR B CG2 1 
ATOM   4063 N  N   . PRO B 1 186 ? -15.81000 7.89700   -30.25100 1.000 33.00411 ?  166 PRO B N   1 
ATOM   4064 C  CA  . PRO B 1 186 ? -15.50200 8.43600   -28.92500 1.000 34.34461 ?  166 PRO B CA  1 
ATOM   4065 C  C   . PRO B 1 186 ? -15.73800 9.93500   -28.88400 1.000 39.98723 ?  166 PRO B C   1 
ATOM   4066 O  O   . PRO B 1 186 ? -15.46300 10.65300  -29.84900 1.000 44.43777 ?  166 PRO B O   1 
ATOM   4067 C  CB  . PRO B 1 186 ? -14.01300 8.10300   -28.73600 1.000 33.83294 ?  166 PRO B CB  1 
ATOM   4068 C  CG  . PRO B 1 186 ? -13.65300 7.17900   -29.86700 1.000 34.05468 ?  166 PRO B CG  1 
ATOM   4069 C  CD  . PRO B 1 186 ? -14.58300 7.53400   -30.97700 1.000 33.17525 ?  166 PRO B CD  1 
ATOM   4070 N  N   . GLY B 1 187 ? -16.21000 10.40500  -27.73800 1.000 38.64653 ?  167 GLY B N   1 
ATOM   4071 C  CA  . GLY B 1 187 ? -16.31900 11.85800  -27.54600 1.000 48.92536 ?  167 GLY B CA  1 
ATOM   4072 C  C   . GLY B 1 187 ? -14.93900 12.49000  -27.51800 1.000 58.01022 ?  167 GLY B C   1 
ATOM   4073 O  O   . GLY B 1 187 ? -13.94700 11.77000  -27.32900 1.000 52.94043 ?  167 GLY B O   1 
ATOM   4074 N  N   . PRO B 1 188 ? -14.81000 13.81900  -27.67900 1.000 62.00001 ?  168 PRO B N   1 
ATOM   4075 C  CA  . PRO B 1 188 ? -13.48500 14.41400  -27.77400 1.000 66.62318 ?  168 PRO B CA  1 
ATOM   4076 C  C   . PRO B 1 188 ? -12.70900 14.28500  -26.44800 1.000 63.78434 ?  168 PRO B C   1 
ATOM   4077 O  O   . PRO B 1 188 ? -11.51300 14.37600  -26.48400 1.000 66.09182 ?  168 PRO B O   1 
ATOM   4078 C  CB  . PRO B 1 188 ? -13.80000 15.86100  -28.19200 1.000 60.60687 ?  168 PRO B CB  1 
ATOM   4079 C  CG  . PRO B 1 188 ? -15.18900 16.11700  -27.65900 1.000 65.59157 ?  168 PRO B CG  1 
ATOM   4080 C  CD  . PRO B 1 188 ? -15.90400 14.78500  -27.75200 1.000 60.38946 ?  168 PRO B CD  1 
ATOM   4081 N  N   . ASP B 1 189 ? -13.40100 14.04600  -25.33300 1.000 63.63100 ?  169 ASP B N   1 
ATOM   4082 C  CA  . ASP B 1 189 ? -12.72200 13.99800  -24.01000 1.000 61.48158 ?  169 ASP B CA  1 
ATOM   4083 C  C   . ASP B 1 189 ? -12.72800 12.56900  -23.46000 1.000 57.83485 ?  169 ASP B C   1 
ATOM   4084 O  O   . ASP B 1 189 ? -12.46700 12.41200  -22.25800 1.000 58.19179 ?  169 ASP B O   1 
ATOM   4085 C  CB  . ASP B 1 189 ? -13.37700 14.95700  -23.01800 1.000 63.80348 ?  169 ASP B CB  1 
ATOM   4086 N  N   . GLN B 1 190 ? -13.06900 11.58500  -24.28800 1.000 50.67664 ?  170 GLN B N   1 
ATOM   4087 C  CA  . GLN B 1 190 ? -12.99800 10.20200  -23.84300 1.000 47.94362 ?  170 GLN B CA  1 
ATOM   4088 C  C   . GLN B 1 190 ? -11.55600 9.88000   -23.46200 1.000 28.52239 ?  170 GLN B C   1 
ATOM   4089 O  O   . GLN B 1 190 ? -10.63800 10.17700  -24.23900 1.000 42.87936 ?  170 GLN B O   1 
ATOM   4090 C  CB  . GLN B 1 190 ? -13.48300 9.24900   -24.93800 1.000 40.50551 ?  170 GLN B CB  1 
ATOM   4091 C  CG  . GLN B 1 190 ? -13.36600 7.77400   -24.57400 1.000 33.18497 ?  170 GLN B CG  1 
ATOM   4092 C  CD  . GLN B 1 190 ? -14.05400 6.85500   -25.57100 1.000 32.55673 ?  170 GLN B CD  1 
ATOM   4093 O  OE1 . GLN B 1 190 ? -15.27100 6.92300   -25.76300 1.000 30.76774 ?  170 GLN B OE1 1 
ATOM   4094 N  NE2 . GLN B 1 190 ? -13.27800 5.98100   -26.20300 1.000 24.71019 ?  170 GLN B NE2 1 
ATOM   4095 N  N   . PRO B 1 191 ? -11.31100 9.31400   -22.28100 1.000 37.74425 ?  171 PRO B N   1 
ATOM   4096 C  CA  . PRO B 1 191 ? -9.94100  8.95000   -21.90100 1.000 31.03127 ?  171 PRO B CA  1 
ATOM   4097 C  C   . PRO B 1 191 ? -9.31100  8.06800   -22.96300 1.000 29.18629 ?  171 PRO B C   1 
ATOM   4098 O  O   . PRO B 1 191 ? -10.00400 7.25900   -23.60000 1.000 26.34945 ?  171 PRO B O   1 
ATOM   4099 C  CB  . PRO B 1 191 ? -10.12200 8.19300   -20.57500 1.000 32.72960 ?  171 PRO B CB  1 
ATOM   4100 C  CG  . PRO B 1 191 ? -11.60100 7.90100   -20.47600 1.000 36.21319 ?  171 PRO B CG  1 
ATOM   4101 C  CD  . PRO B 1 191 ? -12.27500 9.00800   -21.21200 1.000 39.21026 ?  171 PRO B CD  1 
ATOM   4102 N  N   . PRO B 1 192 ? -8.00300  8.20400   -23.19800 1.000 28.98597 ?  172 PRO B N   1 
ATOM   4103 C  CA  . PRO B 1 192 ? -7.40100  7.55300   -24.37200 1.000 27.12018 ?  172 PRO B CA  1 
ATOM   4104 C  C   . PRO B 1 192 ? -7.43000  6.03700   -24.32400 1.000 25.73058 ?  172 PRO B C   1 
ATOM   4105 O  O   . PRO B 1 192 ? -7.27900  5.40500   -25.37600 1.000 25.29553 ?  172 PRO B O   1 
ATOM   4106 C  CB  . PRO B 1 192 ? -5.96000  8.08600   -24.36300 1.000 32.05391 ?  172 PRO B CB  1 
ATOM   4107 C  CG  . PRO B 1 192 ? -5.70500  8.42300   -22.92800 1.000 36.79224 ?  172 PRO B CG  1 
ATOM   4108 C  CD  . PRO B 1 192 ? -7.01200  8.97000   -22.42400 1.000 39.21533 ?  172 PRO B CD  1 
ATOM   4109 N  N   . THR B 1 193 ? -7.62200  5.43300   -23.15100 1.000 25.68257 ?  173 THR B N   1 
ATOM   4110 C  CA  . THR B 1 193 ? -7.61800  3.98200   -23.02400 1.000 24.35722 ?  173 THR B CA  1 
ATOM   4111 C  C   . THR B 1 193 ? -8.99600  3.35700   -23.18600 1.000 20.54854 ?  173 THR B C   1 
ATOM   4112 O  O   . THR B 1 193 ? -9.09200  2.13000   -23.28000 1.000 22.34686 ?  173 THR B O   1 
ATOM   4113 C  CB  . THR B 1 193 ? -7.05500  3.56900   -21.66100 1.000 28.01632 ?  173 THR B CB  1 
ATOM   4114 O  OG1 . THR B 1 193 ? -7.86900  4.12900   -20.62200 1.000 30.57889 ?  173 THR B OG1 1 
ATOM   4115 C  CG2 . THR B 1 193 ? -5.62100  4.06100   -21.50000 1.000 25.61342 ?  173 THR B CG2 1 
ATOM   4116 N  N   . ALA B 1 194 ? -10.06000 4.16300   -23.21200 1.000 22.52380 ?  174 ALA B N   1 
ATOM   4117 C  CA  . ALA B 1 194 ? -11.40700 3.60000   -23.20800 1.000 24.35460 ?  174 ALA B CA  1 
ATOM   4118 C  C   . ALA B 1 194 ? -11.69900 2.83600   -24.49300 1.000 18.16667 ?  174 ALA B C   1 
ATOM   4119 O  O   . ALA B 1 194 ? -12.28400 1.74700   -24.45300 1.000 19.69084 ?  174 ALA B O   1 
ATOM   4120 C  CB  . ALA B 1 194 ? -12.43900 4.70600   -22.99300 1.000 23.68838 ?  174 ALA B CB  1 
ATOM   4121 N  N   . ALA B 1 195 ? -11.30600 3.38900   -25.64500 1.000 19.84963 ?  175 ALA B N   1 
ATOM   4122 C  CA  . ALA B 1 195 ? -11.50800 2.66800   -26.89700 1.000 17.33320 ?  175 ALA B CA  1 
ATOM   4123 C  C   . ALA B 1 195 ? -10.67600 1.39400   -26.94100 1.000 20.25353 ?  175 ALA B C   1 
ATOM   4124 O  O   . ALA B 1 195 ? -11.10400 0.39600   -27.53400 1.000 15.88324 ?  175 ALA B O   1 
ATOM   4125 C  CB  . ALA B 1 195 ? -11.17500 3.56700   -28.09000 1.000 15.06150 ?  175 ALA B CB  1 
ATOM   4126 N  N   . ARG B 1 196 ? -9.48700  1.41500   -26.32600 1.000 18.63194 ?  176 ARG B N   1 
ATOM   4127 C  CA  . ARG B 1 196 ? -8.69500  0.19800   -26.16800 1.000 16.70915 ?  176 ARG B CA  1 
ATOM   4128 C  C   . ARG B 1 196 ? -9.47100  -0.85500  -25.39300 1.000 15.22403 ?  176 ARG B C   1 
ATOM   4129 O  O   . ARG B 1 196 ? -9.58600  -2.00800  -25.82500 1.000 17.95190 ?  176 ARG B O   1 
ATOM   4130 C  CB  . ARG B 1 196 ? -7.39000  0.51400   -25.43700 1.000 19.37089 ?  176 ARG B CB  1 
ATOM   4131 C  CG  . ARG B 1 196 ? -6.54800  -0.71300  -25.11600 1.000 18.58034 ?  176 ARG B CG  1 
ATOM   4132 C  CD  . ARG B 1 196 ? -5.54200  -0.41800  -24.01400 1.000 24.17978 ?  176 ARG B CD  1 
ATOM   4133 N  NE  . ARG B 1 196 ? -6.21800  -0.15100  -22.75100 1.000 22.02399 ?  176 ARG B NE  1 
ATOM   4134 C  CZ  . ARG B 1 196 ? -5.62800  0.30800   -21.65600 1.000 23.87142 ?  176 ARG B CZ  1 
ATOM   4135 N  NH1 . ARG B 1 196 ? -4.34800  0.65300   -21.64900 1.000 17.44135 ?  176 ARG B NH1 1 
ATOM   4136 N  NH2 . ARG B 1 196 ? -6.34000  0.42200   -20.53800 1.000 20.71272 ?  176 ARG B NH2 1 
ATOM   4137 N  N   . ASP B 1 197 ? -10.00200 -0.47200  -24.22800 1.000 16.32307 ?  177 ASP B N   1 
ATOM   4138 C  CA  . ASP B 1 197 ? -10.79600 -1.39500  -23.42500 1.000 21.54653 ?  177 ASP B CA  1 
ATOM   4139 C  C   . ASP B 1 197 ? -11.99700 -1.91500  -24.20200 1.000 18.11043 ?  177 ASP B C   1 
ATOM   4140 O  O   . ASP B 1 197 ? -12.42300 -3.05500  -23.99600 1.000 17.43301 ?  177 ASP B O   1 
ATOM   4141 C  CB  . ASP B 1 197 ? -11.25200 -0.70300  -22.13600 1.000 19.82689 ?  177 ASP B CB  1 
ATOM   4142 C  CG  . ASP B 1 197 ? -10.08200 -0.23300  -21.27600 1.000 26.96712 ?  177 ASP B CG  1 
ATOM   4143 O  OD1 . ASP B 1 197 ? -8.94100  -0.69100  -21.50500 1.000 23.20791 ?  177 ASP B OD1 1 
ATOM   4144 O  OD2 . ASP B 1 197 ? -10.30700 0.60200   -20.37100 1.000 28.61622 -1 177 ASP B OD2 1 
ATOM   4145 N  N   . ALA B 1 198 ? -12.53900 -1.10400  -25.11400 1.000 21.15566 ?  178 ALA B N   1 
ATOM   4146 C  CA  . ALA B 1 198 ? -13.71500 -1.51700  -25.87600 1.000 21.97272 ?  178 ALA B CA  1 
ATOM   4147 C  C   . ALA B 1 198 ? -13.39800 -2.63600  -26.86200 1.000 20.39837 ?  178 ALA B C   1 
ATOM   4148 O  O   . ALA B 1 198 ? -14.29100 -3.41500  -27.20900 1.000 18.84847 ?  178 ALA B O   1 
ATOM   4149 C  CB  . ALA B 1 198 ? -14.30800 -0.31600  -26.61100 1.000 18.42720 ?  178 ALA B CB  1 
ATOM   4150 N  N   . VAL B 1 199 ? -12.14900 -2.73800  -27.32500 1.000 20.17854 ?  179 VAL B N   1 
ATOM   4151 C  CA  . VAL B 1 199 ? -11.77100 -3.86700  -28.17400 1.000 22.00935 ?  179 VAL B CA  1 
ATOM   4152 C  C   . VAL B 1 199 ? -11.91300 -5.17400  -27.41000 1.000 20.51080 ?  179 VAL B C   1 
ATOM   4153 O  O   . VAL B 1 199 ? -12.45600 -6.16100  -27.92200 1.000 19.54679 ?  179 VAL B O   1 
ATOM   4154 C  CB  . VAL B 1 199 ? -10.33900 -3.69900  -28.71000 1.000 20.74480 ?  179 VAL B CB  1 
ATOM   4155 C  CG1 . VAL B 1 199 ? -10.02900 -4.80400  -29.70000 1.000 19.66879 ?  179 VAL B CG1 1 
ATOM   4156 C  CG2 . VAL B 1 199 ? -10.17000 -2.34600  -29.36800 1.000 20.83658 ?  179 VAL B CG2 1 
ATOM   4157 N  N   . VAL B 1 200 ? -11.40100 -5.20600  -26.17900 1.000 20.53496 ?  180 VAL B N   1 
ATOM   4158 C  CA  . VAL B 1 200 ? -11.49800 -6.41100  -25.36200 1.000 16.49031 ?  180 VAL B CA  1 
ATOM   4159 C  C   . VAL B 1 200 ? -12.96000 -6.74800  -25.10200 1.000 16.19065 ?  180 VAL B C   1 
ATOM   4160 O  O   . VAL B 1 200 ? -13.39400 -7.89100  -25.28100 1.000 21.90011 ?  180 VAL B O   1 
ATOM   4161 C  CB  . VAL B 1 200 ? -10.71900 -6.22900  -24.04800 1.000 16.54906 ?  180 VAL B CB  1 
ATOM   4162 C  CG1 . VAL B 1 200 ? -11.03900 -7.36500  -23.08200 1.000 22.71066 ?  180 VAL B CG1 1 
ATOM   4163 C  CG2 . VAL B 1 200 ? -9.22000  -6.14700  -24.32600 1.000 18.67310 ?  180 VAL B CG2 1 
ATOM   4164 N  N   . ALA B 1 201 ? -13.74400 -5.74400  -24.70500 1.000 18.26296 ?  181 ALA B N   1 
ATOM   4165 C  CA  . ALA B 1 201 ? -15.15300 -5.96800  -24.38600 1.000 19.37363 ?  181 ALA B CA  1 
ATOM   4166 C  C   . ALA B 1 201 ? -15.93400 -6.44000  -25.60700 1.000 20.21195 ?  181 ALA B C   1 
ATOM   4167 O  O   . ALA B 1 201 ? -16.72900 -7.38400  -25.52200 1.000 17.70087 ?  181 ALA B O   1 
ATOM   4168 C  CB  . ALA B 1 201 ? -15.76600 -4.68900  -23.81500 1.000 17.07829 ?  181 ALA B CB  1 
ATOM   4169 N  N   . MET B 1 202 ? -15.72400 -5.79500  -26.75700 1.000 20.40848 ?  182 MET B N   1 
ATOM   4170 C  CA  . MET B 1 202 ? -16.47600 -6.16700  -27.95500 1.000 14.98543 ?  182 MET B CA  1 
ATOM   4171 C  C   . MET B 1 202 ? -16.06100 -7.53500  -28.48200 1.000 17.51233 ?  182 MET B C   1 
ATOM   4172 O  O   . MET B 1 202 ? -16.90600 -8.29500  -28.97100 1.000 21.38222 ?  182 MET B O   1 
ATOM   4173 C  CB  . MET B 1 202 ? -16.31300 -5.10400  -29.04400 1.000 18.19170 ?  182 MET B CB  1 
ATOM   4174 C  CG  . MET B 1 202 ? -17.11300 -5.42200  -30.30600 1.000 18.31055 ?  182 MET B CG  1 
ATOM   4175 S  SD  . MET B 1 202 ? -18.90600 -5.38300  -30.07300 1.000 22.32506 ?  182 MET B SD  1 
ATOM   4176 C  CE  . MET B 1 202 ? -19.12800 -3.83300  -29.20800 1.000 23.46344 ?  182 MET B CE  1 
ATOM   4177 N  N   . HIS B 1 203 ? -14.77100 -7.86500  -28.40600 1.000 17.24832 ?  183 HIS B N   1 
ATOM   4178 C  CA  . HIS B 1 203 ? -14.32500 -9.18700  -28.83700 1.000 20.32032 ?  183 HIS B CA  1 
ATOM   4179 C  C   . HIS B 1 203 ? -15.00900 -10.28600 -28.03200 1.000 21.27021 ?  183 HIS B C   1 
ATOM   4180 O  O   . HIS B 1 203 ? -15.49600 -11.27400 -28.59400 1.000 19.08048 ?  183 HIS B O   1 
ATOM   4181 C  CB  . HIS B 1 203 ? -12.80600 -9.30000  -28.71400 1.000 18.02322 ?  183 HIS B CB  1 
ATOM   4182 C  CG  . HIS B 1 203 ? -12.25000 -10.56100 -29.29300 1.000 22.84347 ?  183 HIS B CG  1 
ATOM   4183 N  ND1 . HIS B 1 203 ? -11.92300 -11.65200 -28.51700 1.000 30.62199 ?  183 HIS B ND1 1 
ATOM   4184 C  CD2 . HIS B 1 203 ? -11.95700 -10.90700 -30.56900 1.000 23.69082 ?  183 HIS B CD2 1 
ATOM   4185 C  CE1 . HIS B 1 203 ? -11.46400 -12.61900 -29.29000 1.000 27.42784 ?  183 HIS B CE1 1 
ATOM   4186 N  NE2 . HIS B 1 203 ? -11.47300 -12.19200 -30.53900 1.000 28.30937 ?  183 HIS B NE2 1 
ATOM   4187 N  N   . GLY B 1 204 ? -15.03900 -10.13600 -26.70700 1.000 19.98025 ?  184 GLY B N   1 
ATOM   4188 C  CA  . GLY B 1 204 ? -15.79900 -11.06700 -25.89200 1.000 18.10060 ?  184 GLY B CA  1 
ATOM   4189 C  C   . GLY B 1 204 ? -17.27100 -11.08900 -26.25900 1.000 16.54504 ?  184 GLY B C   1 
ATOM   4190 O  O   . GLY B 1 204 ? -17.88200 -12.15600 -26.34000 1.000 21.30006 ?  184 GLY B O   1 
ATOM   4191 N  N   . PHE B 1 205 ? -17.85300 -9.91000  -26.49800 1.000 12.70432 ?  185 PHE B N   1 
ATOM   4192 C  CA  . PHE B 1 205 ? -19.26400 -9.82800  -26.87000 1.000 21.30388 ?  185 PHE B CA  1 
ATOM   4193 C  C   . PHE B 1 205 ? -19.53800 -10.56000 -28.17800 1.000 23.81487 ?  185 PHE B C   1 
ATOM   4194 O  O   . PHE B 1 205 ? -20.52700 -11.29300 -28.29100 1.000 18.27628 ?  185 PHE B O   1 
ATOM   4195 C  CB  . PHE B 1 205 ? -19.68400 -8.36000  -26.97600 1.000 21.28641 ?  185 PHE B CB  1 
ATOM   4196 C  CG  . PHE B 1 205 ? -21.11900 -8.16000  -27.38700 1.000 23.80948 ?  185 PHE B CG  1 
ATOM   4197 C  CD1 . PHE B 1 205 ? -21.47500 -8.10700  -28.72800 1.000 23.30652 ?  185 PHE B CD1 1 
ATOM   4198 C  CD2 . PHE B 1 205 ? -22.11100 -8.01100  -26.42900 1.000 24.27241 ?  185 PHE B CD2 1 
ATOM   4199 C  CE1 . PHE B 1 205 ? -22.79800 -7.92600  -29.10600 1.000 15.20543 ?  185 PHE B CE1 1 
ATOM   4200 C  CE2 . PHE B 1 205 ? -23.43300 -7.82300  -26.80000 1.000 25.82404 ?  185 PHE B CE2 1 
ATOM   4201 C  CZ  . PHE B 1 205 ? -23.77600 -7.78100  -28.14200 1.000 22.96229 ?  185 PHE B CZ  1 
ATOM   4202 N  N   . LEU B 1 206 ? -18.67600 -10.36700 -29.17900 1.000 17.88789 ?  186 LEU B N   1 
ATOM   4203 C  CA  . LEU B 1 206 ? -18.91100 -10.98100 -30.48100 1.000 17.81223 ?  186 LEU B CA  1 
ATOM   4204 C  C   . LEU B 1 206 ? -18.62100 -12.47400 -30.45700 1.000 20.53636 ?  186 LEU B C   1 
ATOM   4205 O  O   . LEU B 1 206 ? -19.30000 -13.24300 -31.14200 1.000 24.55335 ?  186 LEU B O   1 
ATOM   4206 C  CB  . LEU B 1 206 ? -18.06700 -10.27800 -31.54600 1.000 20.54676 ?  186 LEU B CB  1 
ATOM   4207 C  CG  . LEU B 1 206 ? -18.42200 -8.80800  -31.78900 1.000 20.19128 ?  186 LEU B CG  1 
ATOM   4208 C  CD1 . LEU B 1 206 ? -17.43200 -8.16500  -32.74800 1.000 21.68663 ?  186 LEU B CD1 1 
ATOM   4209 C  CD2 . LEU B 1 206 ? -19.85000 -8.65400  -32.30600 1.000 19.90234 ?  186 LEU B CD2 1 
ATOM   4210 N  N   . VAL B 1 207 ? -17.62700 -12.90000 -29.67700 1.000 18.16853 ?  187 VAL B N   1 
ATOM   4211 C  CA  . VAL B 1 207 ? -17.39800 -14.32900 -29.48200 1.000 22.54386 ?  187 VAL B CA  1 
ATOM   4212 C  C   . VAL B 1 207 ? -18.64800 -14.98000 -28.89900 1.000 23.04359 ?  187 VAL B C   1 
ATOM   4213 O  O   . VAL B 1 207 ? -19.11700 -16.01700 -29.38200 1.000 23.76721 ?  187 VAL B O   1 
ATOM   4214 C  CB  . VAL B 1 207 ? -16.16600 -14.55600 -28.58600 1.000 23.65967 ?  187 VAL B CB  1 
ATOM   4215 C  CG1 . VAL B 1 207 ? -16.21100 -15.93700 -27.94600 1.000 27.86244 ?  187 VAL B CG1 1 
ATOM   4216 C  CG2 . VAL B 1 207 ? -14.87800 -14.37100 -29.38400 1.000 25.52968 ?  187 VAL B CG2 1 
ATOM   4217 N  N   . ASP B 1 208 ? -19.21700 -14.36200 -27.86000 1.000 24.08021 ?  188 ASP B N   1 
ATOM   4218 C  CA  . ASP B 1 208 ? -20.41300 -14.91300 -27.23300 1.000 23.06035 ?  188 ASP B CA  1 
ATOM   4219 C  C   . ASP B 1 208 ? -21.62000 -14.82400 -28.16100 1.000 26.51859 ?  188 ASP B C   1 
ATOM   4220 O  O   . ASP B 1 208 ? -22.44600 -15.74500 -28.20000 1.000 29.09361 ?  188 ASP B O   1 
ATOM   4221 C  CB  . ASP B 1 208 ? -20.68900 -14.19300 -25.91300 1.000 22.89449 ?  188 ASP B CB  1 
ATOM   4222 C  CG  . ASP B 1 208 ? -19.57100 -14.37600 -24.90900 1.000 26.71664 ?  188 ASP B CG  1 
ATOM   4223 O  OD1 . ASP B 1 208 ? -18.70800 -15.25800 -25.12400 1.000 27.39461 ?  188 ASP B OD1 1 
ATOM   4224 O  OD2 . ASP B 1 208 ? -19.54800 -13.63300 -23.90400 1.000 28.39851 -1 188 ASP B OD2 1 
ATOM   4225 N  N   . LEU B 1 209 ? -21.74400 -13.72300 -28.91100 1.000 26.54141 ?  189 LEU B N   1 
ATOM   4226 C  CA  . LEU B 1 209 ? -22.83600 -13.59600 -29.87300 1.000 24.63517 ?  189 LEU B CA  1 
ATOM   4227 C  C   . LEU B 1 209 ? -22.79300 -14.71000 -30.91200 1.000 23.36153 ?  189 LEU B C   1 
ATOM   4228 O  O   . LEU B 1 209 ? -23.82800 -15.30100 -31.24200 1.000 28.29557 ?  189 LEU B O   1 
ATOM   4229 C  CB  . LEU B 1 209 ? -22.78300 -12.22800 -30.55600 1.000 24.26676 ?  189 LEU B CB  1 
ATOM   4230 C  CG  . LEU B 1 209 ? -23.98700 -11.83800 -31.41800 1.000 27.99807 ?  189 LEU B CG  1 
ATOM   4231 C  CD1 . LEU B 1 209 ? -25.28200 -11.88800 -30.61300 1.000 29.24224 ?  189 LEU B CD1 1 
ATOM   4232 C  CD2 . LEU B 1 209 ? -23.79000 -10.45800 -32.03900 1.000 25.52307 ?  189 LEU B CD2 1 
ATOM   4233 N  N   . VAL B 1 210 ? -21.60500 -15.00900 -31.43700 1.000 26.53462 ?  190 VAL B N   1 
ATOM   4234 C  CA  . VAL B 1 210 ? -21.47300 -16.07500 -32.42600 1.000 27.40883 ?  190 VAL B CA  1 
ATOM   4235 C  C   . VAL B 1 210 ? -21.88100 -17.41400 -31.82400 1.000 28.53094 ?  190 VAL B C   1 
ATOM   4236 O  O   . VAL B 1 210 ? -22.59700 -18.20300 -32.45200 1.000 31.20502 ?  190 VAL B O   1 
ATOM   4237 C  CB  . VAL B 1 210 ? -20.03500 -16.11400 -32.97800 1.000 24.89097 ?  190 VAL B CB  1 
ATOM   4238 C  CG1 . VAL B 1 210 ? -19.77200 -17.42900 -33.70400 1.000 38.25250 ?  190 VAL B CG1 1 
ATOM   4239 C  CG2 . VAL B 1 210 ? -19.78600 -14.93100 -33.90100 1.000 25.67397 ?  190 VAL B CG2 1 
ATOM   4240 N  N   . ALA B 1 211 ? -21.44000 -17.68600 -30.59300 1.000 32.03547 ?  191 ALA B N   1 
ATOM   4241 C  CA  . ALA B 1 211 ? -21.78100 -18.94900 -29.94700 1.000 30.52080 ?  191 ALA B CA  1 
ATOM   4242 C  C   . ALA B 1 211 ? -23.28200 -19.06600 -29.71800 1.000 32.18933 ?  191 ALA B C   1 
ATOM   4243 O  O   . ALA B 1 211 ? -23.86300 -20.14300 -29.89400 1.000 39.28830 ?  191 ALA B O   1 
ATOM   4244 C  CB  . ALA B 1 211 ? -21.02500 -19.08500 -28.62600 1.000 35.39792 ?  191 ALA B CB  1 
ATOM   4245 N  N   . ALA B 1 212 ? -23.92700 -17.96700 -29.32100 1.000 29.36421 ?  192 ALA B N   1 
ATOM   4246 C  CA  . ALA B 1 212 ? -25.37200 -17.98200 -29.11600 1.000 32.00024 ?  192 ALA B CA  1 
ATOM   4247 C  C   . ALA B 1 212 ? -26.10700 -18.32800 -30.40600 1.000 39.88009 ?  192 ALA B C   1 
ATOM   4248 O  O   . ALA B 1 212 ? -26.97100 -19.21300 -30.42500 1.000 40.79370 ?  192 ALA B O   1 
ATOM   4249 C  CB  . ALA B 1 212 ? -25.84000 -16.62800 -28.57900 1.000 24.71438 ?  192 ALA B CB  1 
ATOM   4250 N  N   . LYS B 1 213 ? -25.77800 -17.63300 -31.49800 1.000 36.07560 ?  193 LYS B N   1 
ATOM   4251 C  CA  . LYS B 1 213 ? -26.44200 -17.89700 -32.77000 1.000 33.92191 ?  193 LYS B CA  1 
ATOM   4252 C  C   . LYS B 1 213 ? -26.14800 -19.30400 -33.26800 1.000 36.79725 ?  193 LYS B C   1 
ATOM   4253 O  O   . LYS B 1 213 ? -27.00200 -19.92700 -33.90900 1.000 41.33724 ?  193 LYS B O   1 
ATOM   4254 C  CB  . LYS B 1 213 ? -26.01300 -16.86600 -33.81200 1.000 30.21911 ?  193 LYS B CB  1 
ATOM   4255 C  CG  . LYS B 1 213 ? -26.32100 -15.43700 -33.42300 1.000 29.03028 ?  193 LYS B CG  1 
ATOM   4256 C  CD  . LYS B 1 213 ? -27.81600 -15.20800 -33.32500 1.000 33.76707 ?  193 LYS B CD  1 
ATOM   4257 C  CE  . LYS B 1 213 ? -28.11500 -13.92000 -32.58900 1.000 34.25697 ?  193 LYS B CE  1 
ATOM   4258 N  NZ  . LYS B 1 213 ? -29.43700 -13.35400 -32.97400 1.000 34.00553 ?  193 LYS B NZ  1 
ATOM   4259 N  N   . ARG B 1 214 ? -24.95100 -19.82300 -32.98100 1.000 35.65607 ?  194 ARG B N   1 
ATOM   4260 C  CA  . ARG B 1 214 ? -24.63100 -21.19700 -33.35200 1.000 40.05159 ?  194 ARG B CA  1 
ATOM   4261 C  C   . ARG B 1 214 ? -25.52500 -22.19100 -32.62300 1.000 44.61735 ?  194 ARG B C   1 
ATOM   4262 O  O   . ARG B 1 214 ? -25.82500 -23.26500 -33.15800 1.000 49.21245 ?  194 ARG B O   1 
ATOM   4263 C  CB  . ARG B 1 214 ? -23.15900 -21.49100 -33.06000 1.000 34.92660 ?  194 ARG B CB  1 
ATOM   4264 C  CG  . ARG B 1 214 ? -22.60600 -22.69900 -33.79700 1.000 37.46873 ?  194 ARG B CG  1 
ATOM   4265 C  CD  . ARG B 1 214 ? -21.12800 -22.89500 -33.50200 1.000 38.17967 ?  194 ARG B CD  1 
ATOM   4266 N  N   . ALA B 1 215 ? -25.96300 -21.85200 -31.40900 1.000 42.06015 ?  195 ALA B N   1 
ATOM   4267 C  CA  . ALA B 1 215 ? -26.88800 -22.71100 -30.67800 1.000 44.31051 ?  195 ALA B CA  1 
ATOM   4268 C  C   . ALA B 1 215 ? -28.32900 -22.48500 -31.11700 1.000 48.05864 ?  195 ALA B C   1 
ATOM   4269 O  O   . ALA B 1 215 ? -29.09100 -23.44500 -31.27500 1.000 51.62395 ?  195 ALA B O   1 
ATOM   4270 C  CB  . ALA B 1 215 ? -26.75100 -22.47100 -29.17500 1.000 41.68408 ?  195 ALA B CB  1 
ATOM   4271 N  N   . GLU B 1 216 ? -28.71700 -21.22700 -31.32300 1.000 46.80478 ?  196 GLU B N   1 
ATOM   4272 C  CA  . GLU B 1 216 ? -30.09400 -20.86100 -31.64800 1.000 47.15732 ?  196 GLU B CA  1 
ATOM   4273 C  C   . GLU B 1 216 ? -30.05800 -19.86800 -32.80100 1.000 41.39730 ?  196 GLU B C   1 
ATOM   4274 O  O   . GLU B 1 216 ? -30.01500 -18.64600 -32.58700 1.000 37.86422 ?  196 GLU B O   1 
ATOM   4275 C  CB  . GLU B 1 216 ? -30.80300 -20.28600 -30.42400 1.000 50.26040 ?  196 GLU B CB  1 
ATOM   4276 C  CG  . GLU B 1 216 ? -31.07400 -21.33100 -29.35200 1.000 56.35792 ?  196 GLU B CG  1 
ATOM   4277 C  CD  . GLU B 1 216 ? -31.15300 -20.74000 -27.96000 1.000 59.70603 ?  196 GLU B CD  1 
ATOM   4278 O  OE1 . GLU B 1 216 ? -31.47100 -19.53900 -27.84200 1.000 54.46884 ?  196 GLU B OE1 1 
ATOM   4279 O  OE2 . GLU B 1 216 ? -30.88400 -21.47500 -26.98400 1.000 54.59829 -1 196 GLU B OE2 1 
ATOM   4280 N  N   . PRO B 1 217 ? -30.07600 -20.35600 -34.04000 1.000 37.06486 ?  197 PRO B N   1 
ATOM   4281 C  CA  . PRO B 1 217 ? -29.90600 -19.46100 -35.18700 1.000 34.74099 ?  197 PRO B CA  1 
ATOM   4282 C  C   . PRO B 1 217 ? -31.15600 -18.64400 -35.46400 1.000 41.24775 ?  197 PRO B C   1 
ATOM   4283 O  O   . PRO B 1 217 ? -32.27900 -19.04900 -35.15300 1.000 39.31828 ?  197 PRO B O   1 
ATOM   4284 C  CB  . PRO B 1 217 ? -29.60500 -20.42700 -36.34300 1.000 36.93522 ?  197 PRO B CB  1 
ATOM   4285 C  CG  . PRO B 1 217 ? -29.22900 -21.73600 -35.65800 1.000 40.01597 ?  197 PRO B CG  1 
ATOM   4286 C  CD  . PRO B 1 217 ? -30.13600 -21.75900 -34.47500 1.000 45.20489 ?  197 PRO B CD  1 
ATOM   4287 N  N   . GLY B 1 218 ? -30.94200 -17.46800 -36.05300 1.000 37.77036 ?  198 GLY B N   1 
ATOM   4288 C  CA  . GLY B 1 218 ? -32.02800 -16.62400 -36.51300 1.000 28.39351 ?  198 GLY B CA  1 
ATOM   4289 C  C   . GLY B 1 218 ? -31.89100 -16.27200 -37.98000 1.000 30.57997 ?  198 GLY B C   1 
ATOM   4290 O  O   . GLY B 1 218 ? -31.14600 -16.92800 -38.71400 1.000 36.39885 ?  198 GLY B O   1 
ATOM   4291 N  N   . HIS B 1 219 ? -32.60500 -15.23900 -38.42600 1.000 36.05929 ?  199 HIS B N   1 
ATOM   4292 C  CA  . HIS B 1 219 ? -32.51000 -14.76000 -39.79800 1.000 32.67117 ?  199 HIS B CA  1 
ATOM   4293 C  C   . HIS B 1 219 ? -31.47500 -13.65200 -39.95500 1.000 37.36421 ?  199 HIS B C   1 
ATOM   4294 O  O   . HIS B 1 219 ? -31.49500 -12.93000 -40.95900 1.000 38.27420 ?  199 HIS B O   1 
ATOM   4295 C  CB  . HIS B 1 219 ? -33.88000 -14.28300 -40.28700 1.000 38.70096 ?  199 HIS B CB  1 
ATOM   4296 N  N   . ASP B 1 220 ? -30.57300 -13.50800 -38.98700 1.000 37.19463 ?  200 ASP B N   1 
ATOM   4297 C  CA  . ASP B 1 220 ? -29.55000 -12.47600 -39.00700 1.000 32.82457 ?  200 ASP B CA  1 
ATOM   4298 C  C   . ASP B 1 220 ? -28.36900 -12.90800 -39.87000 1.000 30.53014 ?  200 ASP B C   1 
ATOM   4299 O  O   . ASP B 1 220 ? -28.19700 -14.08800 -40.19300 1.000 28.38163 ?  200 ASP B O   1 
ATOM   4300 C  CB  . ASP B 1 220 ? -29.06200 -12.17700 -37.59100 1.000 25.59087 ?  200 ASP B CB  1 
ATOM   4301 C  CG  . ASP B 1 220 ? -28.49600 -13.40200 -36.90500 1.000 32.88616 ?  200 ASP B CG  1 
ATOM   4302 O  OD1 . ASP B 1 220 ? -29.28200 -14.19100 -36.34000 1.000 31.48312 ?  200 ASP B OD1 1 
ATOM   4303 O  OD2 . ASP B 1 220 ? -27.25800 -13.57900 -36.93500 1.000 31.33027 -1 200 ASP B OD2 1 
ATOM   4304 N  N   . LEU B 1 221 ? -27.53300 -11.92800 -40.22300 1.000 32.87547 ?  201 LEU B N   1 
ATOM   4305 C  CA  . LEU B 1 221 ? -26.37800 -12.20300 -41.07200 1.000 29.33739 ?  201 LEU B CA  1 
ATOM   4306 C  C   . LEU B 1 221 ? -25.39400 -13.14400 -40.39000 1.000 27.65407 ?  201 LEU B C   1 
ATOM   4307 O  O   . LEU B 1 221 ? -24.78100 -13.99600 -41.04500 1.000 30.08172 ?  201 LEU B O   1 
ATOM   4308 C  CB  . LEU B 1 221 ? -25.68600 -10.89400 -41.45600 1.000 28.81295 ?  201 LEU B CB  1 
ATOM   4309 N  N   . LEU B 1 222 ? -25.22700 -13.00700 -39.07200 1.000 27.71032 ?  202 LEU B N   1 
ATOM   4310 C  CA  . LEU B 1 222 ? -24.26900 -13.85100 -38.36500 1.000 28.53738 ?  202 LEU B CA  1 
ATOM   4311 C  C   . LEU B 1 222 ? -24.71800 -15.30800 -38.36100 1.000 29.43164 ?  202 LEU B C   1 
ATOM   4312 O  O   . LEU B 1 222 ? -23.90100 -16.21400 -38.56100 1.000 33.36346 ?  202 LEU B O   1 
ATOM   4313 C  CB  . LEU B 1 222 ? -24.07000 -13.33500 -36.93900 1.000 29.76167 ?  202 LEU B CB  1 
ATOM   4314 C  CG  . LEU B 1 222 ? -22.69300 -13.52000 -36.30500 1.000 38.27786 ?  202 LEU B CG  1 
ATOM   4315 C  CD1 . LEU B 1 222 ? -21.61600 -12.87600 -37.16200 1.000 26.14343 ?  202 LEU B CD1 1 
ATOM   4316 C  CD2 . LEU B 1 222 ? -22.68200 -12.92900 -34.90000 1.000 31.95441 ?  202 LEU B CD2 1 
ATOM   4317 N  N   . SER B 1 223 ? -26.01500 -15.55200 -38.14500 1.000 33.92278 ?  203 SER B N   1 
ATOM   4318 C  CA  . SER B 1 223 ? -26.53700 -16.91200 -38.23600 1.000 29.51770 ?  203 SER B CA  1 
ATOM   4319 C  C   . SER B 1 223 ? -26.37300 -17.47200 -39.64300 1.000 28.63587 ?  203 SER B C   1 
ATOM   4320 O  O   . SER B 1 223 ? -26.01800 -18.64300 -39.81600 1.000 33.85405 ?  203 SER B O   1 
ATOM   4321 C  CB  . SER B 1 223 ? -28.01000 -16.94500 -37.82300 1.000 31.27701 ?  203 SER B CB  1 
ATOM   4322 O  OG  . SER B 1 223 ? -28.17900 -16.53100 -36.48100 1.000 35.84663 ?  203 SER B OG  1 
ATOM   4323 N  N   . GLY B 1 224 ? -26.63500 -16.65100 -40.66200 1.000 30.82505 ?  204 GLY B N   1 
ATOM   4324 C  CA  . GLY B 1 224 ? -26.45700 -17.11200 -42.03000 1.000 33.42255 ?  204 GLY B CA  1 
ATOM   4325 C  C   . GLY B 1 224 ? -25.00800 -17.41500 -42.35400 1.000 36.81123 ?  204 GLY B C   1 
ATOM   4326 O  O   . GLY B 1 224 ? -24.70500 -18.40200 -43.02800 1.000 35.77845 ?  204 GLY B O   1 
ATOM   4327 N  N   . LEU B 1 225 ? -24.09100 -16.57500 -41.86800 1.000 32.90911 ?  205 LEU B N   1 
ATOM   4328 C  CA  . LEU B 1 225 ? -22.67000 -16.82000 -42.09000 1.000 33.93267 ?  205 LEU B CA  1 
ATOM   4329 C  C   . LEU B 1 225 ? -22.20400 -18.06800 -41.35200 1.000 35.99132 ?  205 LEU B C   1 
ATOM   4330 O  O   . LEU B 1 225 ? -21.33300 -18.79400 -41.84300 1.000 36.51528 ?  205 LEU B O   1 
ATOM   4331 C  CB  . LEU B 1 225 ? -21.85500 -15.60400 -41.65600 1.000 31.95171 ?  205 LEU B CB  1 
ATOM   4332 C  CG  . LEU B 1 225 ? -21.93200 -14.37600 -42.56100 1.000 34.95933 ?  205 LEU B CG  1 
ATOM   4333 C  CD1 . LEU B 1 225 ? -21.25900 -13.18900 -41.88700 1.000 29.50459 ?  205 LEU B CD1 1 
ATOM   4334 C  CD2 . LEU B 1 225 ? -21.29700 -14.66900 -43.91500 1.000 34.63153 ?  205 LEU B CD2 1 
ATOM   4335 N  N   . ILE B 1 226 ? -22.76400 -18.32700 -40.16700 1.000 36.80410 ?  206 ILE B N   1 
ATOM   4336 C  CA  . ILE B 1 226 ? -22.48500 -19.58600 -39.47900 1.000 36.38459 ?  206 ILE B CA  1 
ATOM   4337 C  C   . ILE B 1 226 ? -22.93700 -20.76300 -40.33400 1.000 37.86050 ?  206 ILE B C   1 
ATOM   4338 O  O   . ILE B 1 226 ? -22.28200 -21.81300 -40.37400 1.000 44.59756 ?  206 ILE B O   1 
ATOM   4339 C  CB  . ILE B 1 226 ? -23.15600 -19.60000 -38.09100 1.000 38.86053 ?  206 ILE B CB  1 
ATOM   4340 C  CG1 . ILE B 1 226 ? -22.43800 -18.64700 -37.13400 1.000 35.43675 ?  206 ILE B CG1 1 
ATOM   4341 C  CG2 . ILE B 1 226 ? -23.17700 -21.00700 -37.51100 1.000 41.25280 ?  206 ILE B CG2 1 
ATOM   4342 C  CD1 . ILE B 1 226 ? -23.32800 -18.10300 -36.03500 1.000 33.86648 ?  206 ILE B CD1 1 
ATOM   4343 N  N   . ALA B 1 227 ? -24.04700 -20.59600 -41.05700 1.000 34.67773 ?  207 ALA B N   1 
ATOM   4344 C  CA  . ALA B 1 227 ? -24.61000 -21.67800 -41.85400 1.000 42.09129 ?  207 ALA B CA  1 
ATOM   4345 C  C   . ALA B 1 227 ? -23.90500 -21.87300 -43.19100 1.000 43.75235 ?  207 ALA B C   1 
ATOM   4346 O  O   . ALA B 1 227 ? -24.04300 -22.94400 -43.79200 1.000 49.03383 ?  207 ALA B O   1 
ATOM   4347 C  CB  . ALA B 1 227 ? -26.09900 -21.42400 -42.10300 1.000 42.22704 ?  207 ALA B CB  1 
ATOM   4348 N  N   . VAL B 1 228 ? -23.15200 -20.87500 -43.66400 1.000 40.49014 ?  208 VAL B N   1 
ATOM   4349 C  CA  . VAL B 1 228 ? -22.59600 -20.93400 -45.01300 1.000 42.89674 ?  208 VAL B CA  1 
ATOM   4350 C  C   . VAL B 1 228 ? -21.61300 -22.09000 -45.12900 1.000 47.74334 ?  208 VAL B C   1 
ATOM   4351 O  O   . VAL B 1 228 ? -20.73800 -22.27800 -44.27400 1.000 44.66247 ?  208 VAL B O   1 
ATOM   4352 C  CB  . VAL B 1 228 ? -21.93100 -19.59800 -45.37800 1.000 39.49428 ?  208 VAL B CB  1 
ATOM   4353 N  N   . ARG B 1 229 ? -21.75400 -22.87000 -46.20100 1.000 50.32665 ?  209 ARG B N   1 
ATOM   4354 C  CA  . ARG B 1 229 ? -20.89000 -24.01500 -46.46800 1.000 58.34015 ?  209 ARG B CA  1 
ATOM   4355 C  C   . ARG B 1 229 ? -20.52800 -24.02300 -47.94500 1.000 65.87713 ?  209 ARG B C   1 
ATOM   4356 O  O   . ARG B 1 229 ? -21.41500 -24.10300 -48.80000 1.000 66.00529 ?  209 ARG B O   1 
ATOM   4357 C  CB  . ARG B 1 229 ? -21.57900 -25.33200 -46.09400 1.000 55.33619 ?  209 ARG B CB  1 
ATOM   4358 C  CG  . ARG B 1 229 ? -21.77100 -25.58100 -44.60900 1.000 55.86407 ?  209 ARG B CG  1 
ATOM   4359 C  CD  . ARG B 1 229 ? -20.46300 -25.57700 -43.83400 1.000 55.84660 ?  209 ARG B CD  1 
ATOM   4360 N  NE  . ARG B 1 229 ? -20.68700 -25.78400 -42.40600 1.000 57.00057 ?  209 ARG B NE  1 
ATOM   4361 C  CZ  . ARG B 1 229 ? -21.34300 -24.94800 -41.61100 1.000 51.34133 ?  209 ARG B CZ  1 
ATOM   4362 N  NH1 . ARG B 1 229 ? -21.77200 -23.77300 -42.04200 1.000 47.87566 ?  209 ARG B NH1 1 
ATOM   4363 N  NH2 . ARG B 1 229 ? -21.56200 -25.29600 -40.34600 1.000 56.24725 ?  209 ARG B NH2 1 
ATOM   4364 N  N   . ASP B 1 230 ? -19.23200 -23.93900 -48.24500 1.000 67.63428 ?  210 ASP B N   1 
ATOM   4365 C  CA  . ASP B 1 230 ? -18.72400 -24.19700 -49.59300 1.000 68.96051 ?  210 ASP B CA  1 
ATOM   4366 C  C   . ASP B 1 230 ? -18.20700 -25.63200 -49.60100 1.000 71.59008 ?  210 ASP B C   1 
ATOM   4367 O  O   . ASP B 1 230 ? -17.01400 -25.89700 -49.44900 1.000 68.67977 ?  210 ASP B O   1 
ATOM   4368 C  CB  . ASP B 1 230 ? -17.64300 -23.19400 -49.97900 1.000 66.97527 ?  210 ASP B CB  1 
ATOM   4369 C  CG  . ASP B 1 230 ? -17.13000 -23.40800 -51.39100 1.000 63.66052 ?  210 ASP B CG  1 
ATOM   4370 N  N   . ASP B 1 231 ? -19.14000 -26.56700 -49.77900 1.000 73.80557 ?  211 ASP B N   1 
ATOM   4371 C  CA  . ASP B 1 231 ? -18.90600 -27.99600 -49.55400 1.000 71.66492 ?  211 ASP B CA  1 
ATOM   4372 C  C   . ASP B 1 231 ? -18.46100 -28.14500 -48.10500 1.000 73.03191 ?  211 ASP B C   1 
ATOM   4373 O  O   . ASP B 1 231 ? -19.19600 -27.69400 -47.20900 1.000 75.74051 ?  211 ASP B O   1 
ATOM   4374 C  CB  . ASP B 1 231 ? -17.94400 -28.54700 -50.60900 1.000 74.46010 ?  211 ASP B CB  1 
ATOM   4375 C  CG  . ASP B 1 231 ? -18.63500 -29.45200 -51.61100 1.000 79.63240 ?  211 ASP B CG  1 
ATOM   4376 O  OD1 . ASP B 1 231 ? -19.77600 -29.88100 -51.33800 1.000 73.59309 ?  211 ASP B OD1 1 
ATOM   4377 O  OD2 . ASP B 1 231 ? -18.03100 -29.73700 -52.66800 1.000 76.16251 ?  211 ASP B OD2 1 
ATOM   4378 N  N   . GLU B 1 232 ? -17.30200 -28.73600 -47.81900 1.000 72.27657 ?  212 GLU B N   1 
ATOM   4379 C  CA  . GLU B 1 232 ? -16.87000 -28.91400 -46.43800 1.000 72.38557 ?  212 GLU B CA  1 
ATOM   4380 C  C   . GLU B 1 232 ? -16.31900 -27.64000 -45.81100 1.000 75.13435 ?  212 GLU B C   1 
ATOM   4381 O  O   . GLU B 1 232 ? -16.07900 -27.62400 -44.59900 1.000 71.02766 ?  212 GLU B O   1 
ATOM   4382 C  CB  . GLU B 1 232 ? -15.81400 -30.01800 -46.35400 1.000 78.52249 ?  212 GLU B CB  1 
ATOM   4383 N  N   . ASP B 1 233 ? -16.11000 -26.58100 -46.59000 1.000 71.66929 ?  213 ASP B N   1 
ATOM   4384 C  CA  . ASP B 1 233 ? -15.52300 -25.36300 -46.04800 1.000 67.62180 ?  213 ASP B CA  1 
ATOM   4385 C  C   . ASP B 1 233 ? -16.55200 -24.58000 -45.24600 1.000 63.75640 ?  213 ASP B C   1 
ATOM   4386 O  O   . ASP B 1 233 ? -17.67800 -24.35800 -45.70200 1.000 60.04330 ?  213 ASP B O   1 
ATOM   4387 C  CB  . ASP B 1 233 ? -14.95000 -24.48600 -47.16000 1.000 68.13825 ?  213 ASP B CB  1 
ATOM   4388 C  CG  . ASP B 1 233 ? -13.81300 -23.60800 -46.67100 1.000 62.04005 ?  213 ASP B CG  1 
ATOM   4389 O  OD1 . ASP B 1 233 ? -13.34300 -23.83000 -45.53400 1.000 59.66121 ?  213 ASP B OD1 1 
ATOM   4390 O  OD2 . ASP B 1 233 ? -13.39500 -22.69400 -47.41400 1.000 61.81170 -1 213 ASP B OD2 1 
ATOM   4391 N  N   . ARG B 1 234 ? -16.15300 -24.15900 -44.05100 1.000 62.63567 ?  214 ARG B N   1 
ATOM   4392 C  CA  . ARG B 1 234 ? -16.98500 -23.37800 -43.15400 1.000 54.67065 ?  214 ARG B CA  1 
ATOM   4393 C  C   . ARG B 1 234 ? -16.16400 -22.21700 -42.61600 1.000 50.14931 ?  214 ARG B C   1 
ATOM   4394 O  O   . ARG B 1 234 ? -14.93400 -22.28800 -42.54400 1.000 51.96428 ?  214 ARG B O   1 
ATOM   4395 C  CB  . ARG B 1 234 ? -17.51800 -24.24800 -42.00000 1.000 50.22563 ?  214 ARG B CB  1 
ATOM   4396 C  CG  . ARG B 1 234 ? -16.56100 -24.37400 -40.82100 1.000 49.58400 ?  214 ARG B CG  1 
ATOM   4397 C  CD  . ARG B 1 234 ? -17.30100 -24.66300 -39.52500 1.000 52.74655 ?  214 ARG B CD  1 
ATOM   4398 N  NE  . ARG B 1 234 ? -18.53600 -25.40100 -39.75900 1.000 51.10572 ?  214 ARG B NE  1 
ATOM   4399 N  N   . LEU B 1 235 ? -16.84900 -21.13300 -42.26300 1.000 49.61065 ?  215 LEU B N   1 
ATOM   4400 C  CA  . LEU B 1 235 ? -16.17600 -19.99000 -41.66300 1.000 40.54163 ?  215 LEU B CA  1 
ATOM   4401 C  C   . LEU B 1 235 ? -15.86100 -20.29200 -40.20300 1.000 42.61722 ?  215 LEU B C   1 
ATOM   4402 O  O   . LEU B 1 235 ? -16.71200 -20.80000 -39.46700 1.000 41.01422 ?  215 LEU B O   1 
ATOM   4403 C  CB  . LEU B 1 235 ? -17.03900 -18.73400 -41.77500 1.000 40.33554 ?  215 LEU B CB  1 
ATOM   4404 C  CG  . LEU B 1 235 ? -17.13700 -18.09100 -43.15800 1.000 41.62602 ?  215 LEU B CG  1 
ATOM   4405 C  CD1 . LEU B 1 235 ? -18.35300 -17.18300 -43.24000 1.000 41.51417 ?  215 LEU B CD1 1 
ATOM   4406 C  CD2 . LEU B 1 235 ? -15.86600 -17.32600 -43.47500 1.000 36.42336 ?  215 LEU B CD2 1 
ATOM   4407 N  N   . SER B 1 236 ? -14.63400 -19.98700 -39.78700 1.000 38.57099 ?  216 SER B N   1 
ATOM   4408 C  CA  . SER B 1 236 ? -14.23900 -20.21100 -38.40800 1.000 41.85835 ?  216 SER B CA  1 
ATOM   4409 C  C   . SER B 1 236 ? -14.84000 -19.13700 -37.50400 1.000 37.27005 ?  216 SER B C   1 
ATOM   4410 O  O   . SER B 1 236 ? -15.34100 -18.10600 -37.96100 1.000 35.96036 ?  216 SER B O   1 
ATOM   4411 C  CB  . SER B 1 236 ? -12.71400 -20.22900 -38.28700 1.000 34.79457 ?  216 SER B CB  1 
ATOM   4412 O  OG  . SER B 1 236 ? -12.20100 -18.92100 -38.11600 1.000 41.01846 ?  216 SER B OG  1 
ATOM   4413 N  N   . GLU B 1 237 ? -14.79500 -19.39500 -36.19300 1.000 40.22430 ?  217 GLU B N   1 
ATOM   4414 C  CA  . GLU B 1 237 ? -15.30200 -18.41200 -35.23800 1.000 40.97876 ?  217 GLU B CA  1 
ATOM   4415 C  C   . GLU B 1 237 ? -14.46700 -17.13900 -35.27000 1.000 28.18549 ?  217 GLU B C   1 
ATOM   4416 O  O   . GLU B 1 237 ? -15.01100 -16.03200 -35.19300 1.000 30.73250 ?  217 GLU B O   1 
ATOM   4417 C  CB  . GLU B 1 237 ? -15.33000 -19.00100 -33.82500 1.000 43.69758 ?  217 GLU B CB  1 
ATOM   4418 C  CG  . GLU B 1 237 ? -15.06700 -17.97700 -32.72300 1.000 43.34101 ?  217 GLU B CG  1 
ATOM   4419 C  CD  . GLU B 1 237 ? -14.90600 -18.60800 -31.35300 1.000 50.76523 ?  217 GLU B CD  1 
ATOM   4420 O  OE1 . GLU B 1 237 ? -13.98300 -19.43200 -31.18300 1.000 60.44919 ?  217 GLU B OE1 1 
ATOM   4421 O  OE2 . GLU B 1 237 ? -15.69700 -18.27400 -30.44500 1.000 45.70750 -1 217 GLU B OE2 1 
ATOM   4422 N  N   . ALA B 1 238 ? -13.14400 -17.27600 -35.39000 1.000 34.88966 ?  218 ALA B N   1 
ATOM   4423 C  CA  . ALA B 1 238 ? -12.28600 -16.10600 -35.54600 1.000 35.45348 ?  218 ALA B CA  1 
ATOM   4424 C  C   . ALA B 1 238 ? -12.68900 -15.29600 -36.77000 1.000 28.23740 ?  218 ALA B C   1 
ATOM   4425 O  O   . ALA B 1 238 ? -12.81400 -14.06700 -36.70500 1.000 29.22994 ?  218 ALA B O   1 
ATOM   4426 C  CB  . ALA B 1 238 ? -10.82400 -16.54100 -35.64800 1.000 36.17163 ?  218 ALA B CB  1 
ATOM   4427 N  N   . GLU B 1 239 ? -12.90200 -15.97800 -37.89900 1.000 33.97999 ?  219 GLU B N   1 
ATOM   4428 C  CA  . GLU B 1 239 ? -13.32400 -15.29700 -39.12000 1.000 28.17801 ?  219 GLU B CA  1 
ATOM   4429 C  C   . GLU B 1 239 ? -14.66300 -14.60000 -38.92200 1.000 28.94281 ?  219 GLU B C   1 
ATOM   4430 O  O   . GLU B 1 239 ? -14.86000 -13.47100 -39.38800 1.000 27.23508 ?  219 GLU B O   1 
ATOM   4431 C  CB  . GLU B 1 239 ? -13.39900 -16.30600 -40.26800 1.000 33.89621 ?  219 GLU B CB  1 
ATOM   4432 C  CG  . GLU B 1 239 ? -12.02900 -16.73600 -40.78900 1.000 34.67271 ?  219 GLU B CG  1 
ATOM   4433 C  CD  . GLU B 1 239 ? -12.09100 -17.97500 -41.66500 1.000 43.07540 ?  219 GLU B CD  1 
ATOM   4434 O  OE1 . GLU B 1 239 ? -13.19400 -18.54300 -41.81900 1.000 45.32914 ?  219 GLU B OE1 1 
ATOM   4435 O  OE2 . GLU B 1 239 ? -11.03400 -18.38200 -42.19500 1.000 41.29076 -1 219 GLU B OE2 1 
ATOM   4436 N  N   . LEU B 1 240 ? -15.59100 -15.25300 -38.21700 1.000 30.71434 ?  220 LEU B N   1 
ATOM   4437 C  CA  . LEU B 1 240 ? -16.89600 -14.65300 -37.95900 1.000 28.45895 ?  220 LEU B CA  1 
ATOM   4438 C  C   . LEU B 1 240 ? -16.76400 -13.40900 -37.08800 1.000 22.74767 ?  220 LEU B C   1 
ATOM   4439 O  O   . LEU B 1 240 ? -17.37800 -12.37300 -37.36500 1.000 24.36738 ?  220 LEU B O   1 
ATOM   4440 C  CB  . LEU B 1 240 ? -17.81800 -15.68200 -37.30100 1.000 32.36271 ?  220 LEU B CB  1 
ATOM   4441 C  CG  . LEU B 1 240 ? -18.30900 -16.79900 -38.22600 1.000 34.23921 ?  220 LEU B CG  1 
ATOM   4442 C  CD1 . LEU B 1 240 ? -18.70000 -18.03200 -37.43300 1.000 33.86532 ?  220 LEU B CD1 1 
ATOM   4443 C  CD2 . LEU B 1 240 ? -19.46100 -16.32600 -39.08700 1.000 34.27462 ?  220 LEU B CD2 1 
ATOM   4444 N  N   . VAL B 1 241 ? -15.94800 -13.49000 -36.03400 1.000 25.64606 ?  221 VAL B N   1 
ATOM   4445 C  CA  . VAL B 1 241 ? -15.77300 -12.34500 -35.14700 1.000 22.79956 ?  221 VAL B CA  1 
ATOM   4446 C  C   . VAL B 1 241 ? -15.09000 -11.19700 -35.88200 1.000 21.23874 ?  221 VAL B C   1 
ATOM   4447 O  O   . VAL B 1 241 ? -15.50600 -10.03800 -35.76800 1.000 22.76795 ?  221 VAL B O   1 
ATOM   4448 C  CB  . VAL B 1 241 ? -14.99600 -12.76400 -33.88400 1.000 24.66975 ?  221 VAL B CB  1 
ATOM   4449 C  CG1 . VAL B 1 241 ? -14.62100 -11.54700 -33.06200 1.000 23.66007 ?  221 VAL B CG1 1 
ATOM   4450 C  CG2 . VAL B 1 241 ? -15.82300 -13.73300 -33.05400 1.000 22.99475 ?  221 VAL B CG2 1 
ATOM   4451 N  N   . SER B 1 242 ? -14.03700 -11.49700 -36.65000 1.000 24.89897 ?  222 SER B N   1 
ATOM   4452 C  CA  . SER B 1 242 ? -13.34700 -10.44800 -37.39700 1.000 28.53677 ?  222 SER B CA  1 
ATOM   4453 C  C   . SER B 1 242 ? -14.26100 -9.82000  -38.44200 1.000 21.54115 ?  222 SER B C   1 
ATOM   4454 O  O   . SER B 1 242 ? -14.20900 -8.60700  -38.67100 1.000 23.85512 ?  222 SER B O   1 
ATOM   4455 C  CB  . SER B 1 242 ? -12.08400 -11.00300 -38.06000 1.000 26.55996 ?  222 SER B CB  1 
ATOM   4456 O  OG  . SER B 1 242 ? -11.13100 -11.41700 -37.09600 1.000 34.83976 ?  222 SER B OG  1 
ATOM   4457 N  N   . MET B 1 243 ? -15.10300 -10.63000 -39.08900 1.000 23.53158 ?  223 MET B N   1 
ATOM   4458 C  CA  . MET B 1 243 ? -16.08200 -10.07900 -40.02300 1.000 24.10542 ?  223 MET B CA  1 
ATOM   4459 C  C   . MET B 1 243 ? -17.06500 -9.16100  -39.30800 1.000 25.34750 ?  223 MET B C   1 
ATOM   4460 O  O   . MET B 1 243 ? -17.47400 -8.12700  -39.85300 1.000 25.31728 ?  223 MET B O   1 
ATOM   4461 C  CB  . MET B 1 243 ? -16.82400 -11.21100 -40.73600 1.000 26.17834 ?  223 MET B CB  1 
ATOM   4462 C  CG  . MET B 1 243 ? -17.88200 -10.74800 -41.72200 1.000 32.10954 ?  223 MET B CG  1 
ATOM   4463 S  SD  . MET B 1 243 ? -17.25600 -9.59300  -42.96000 1.000 30.20107 ?  223 MET B SD  1 
ATOM   4464 C  CE  . MET B 1 243 ? -18.76800 -8.74700  -43.42600 1.000 33.12739 ?  223 MET B CE  1 
ATOM   4465 N  N   . ALA B 1 244 ? -17.45800 -9.52300  -38.08200 1.000 22.96594 ?  224 ALA B N   1 
ATOM   4466 C  CA  . ALA B 1 244 ? -18.35700 -8.66800  -37.31300 1.000 21.40754 ?  224 ALA B CA  1 
ATOM   4467 C  C   . ALA B 1 244 ? -17.70500 -7.33100  -36.98700 1.000 17.81278 ?  224 ALA B C   1 
ATOM   4468 O  O   . ALA B 1 244 ? -18.34900 -6.28000  -37.08700 1.000 21.36239 ?  224 ALA B O   1 
ATOM   4469 C  CB  . ALA B 1 244 ? -18.78700 -9.38100  -36.03200 1.000 22.04251 ?  224 ALA B CB  1 
ATOM   4470 N  N   . PHE B 1 245 ? -16.43100 -7.35500  -36.57600 1.000 20.14800 ?  225 PHE B N   1 
ATOM   4471 C  CA  . PHE B 1 245 ? -15.69900 -6.11400  -36.33800 1.000 18.99215 ?  225 PHE B CA  1 
ATOM   4472 C  C   . PHE B 1 245 ? -15.64700 -5.26500  -37.59600 1.000 16.31138 ?  225 PHE B C   1 
ATOM   4473 O  O   . PHE B 1 245 ? -15.80800 -4.04100  -37.53800 1.000 18.00871 ?  225 PHE B O   1 
ATOM   4474 C  CB  . PHE B 1 245 ? -14.27600 -6.41700  -35.86400 1.000 20.02849 ?  225 PHE B CB  1 
ATOM   4475 C  CG  . PHE B 1 245 ? -14.13000 -6.50600  -34.37100 1.000 18.26360 ?  225 PHE B CG  1 
ATOM   4476 C  CD1 . PHE B 1 245 ? -14.21400 -5.37100  -33.58200 1.000 24.72990 ?  225 PHE B CD1 1 
ATOM   4477 C  CD2 . PHE B 1 245 ? -13.87800 -7.72500  -33.76000 1.000 28.20706 ?  225 PHE B CD2 1 
ATOM   4478 C  CE1 . PHE B 1 245 ? -14.07200 -5.44900  -32.20300 1.000 21.81162 ?  225 PHE B CE1 1 
ATOM   4479 C  CE2 . PHE B 1 245 ? -13.72900 -7.81300  -32.38400 1.000 22.57316 ?  225 PHE B CE2 1 
ATOM   4480 C  CZ  . PHE B 1 245 ? -13.82600 -6.67400  -31.60600 1.000 23.78878 ?  225 PHE B CZ  1 
ATOM   4481 N  N   . LEU B 1 246 ? -15.39000 -5.90100  -38.74100 1.000 19.73373 ?  226 LEU B N   1 
ATOM   4482 C  CA  . LEU B 1 246 ? -15.38000 -5.18900  -40.01300 1.000 23.16364 ?  226 LEU B CA  1 
ATOM   4483 C  C   . LEU B 1 246 ? -16.72300 -4.52100  -40.28000 1.000 23.94216 ?  226 LEU B C   1 
ATOM   4484 O  O   . LEU B 1 246 ? -16.77700 -3.36500  -40.71400 1.000 22.57092 ?  226 LEU B O   1 
ATOM   4485 C  CB  . LEU B 1 246 ? -15.03700 -6.16500  -41.13700 1.000 27.11083 ?  226 LEU B CB  1 
ATOM   4486 C  CG  . LEU B 1 246 ? -13.56100 -6.26800  -41.51000 1.000 30.70685 ?  226 LEU B CG  1 
ATOM   4487 C  CD1 . LEU B 1 246 ? -13.40700 -6.81900  -42.91900 1.000 27.96777 ?  226 LEU B CD1 1 
ATOM   4488 C  CD2 . LEU B 1 246 ? -12.89000 -4.91600  -41.38600 1.000 31.70391 ?  226 LEU B CD2 1 
ATOM   4489 N  N   . ALA B 1 247 ? -17.82000 -5.23700  -40.02100 1.000 19.88964 ?  227 ALA B N   1 
ATOM   4490 C  CA  . ALA B 1 247 ? -19.14300 -4.65600  -40.21700 1.000 20.41932 ?  227 ALA B CA  1 
ATOM   4491 C  C   . ALA B 1 247 ? -19.38200 -3.47400  -39.28700 1.000 21.76610 ?  227 ALA B C   1 
ATOM   4492 O  O   . ALA B 1 247 ? -20.08900 -2.53100  -39.65100 1.000 22.82941 ?  227 ALA B O   1 
ATOM   4493 C  CB  . ALA B 1 247 ? -20.21900 -5.72000  -40.01100 1.000 26.82764 ?  227 ALA B CB  1 
ATOM   4494 N  N   . LEU B 1 248 ? -18.80100 -3.50300  -38.08600 1.000 24.83158 ?  228 LEU B N   1 
ATOM   4495 C  CA  . LEU B 1 248 ? -18.94700 -2.37800  -37.16700 1.000 21.55906 ?  228 LEU B CA  1 
ATOM   4496 C  C   . LEU B 1 248 ? -18.20000 -1.15100  -37.67700 1.000 21.11411 ?  228 LEU B C   1 
ATOM   4497 O  O   . LEU B 1 248 ? -18.75000 -0.04400  -37.70100 1.000 20.40150 ?  228 LEU B O   1 
ATOM   4498 C  CB  . LEU B 1 248 ? -18.45000 -2.77500  -35.77600 1.000 21.16275 ?  228 LEU B CB  1 
ATOM   4499 C  CG  . LEU B 1 248 ? -19.36100 -3.71600  -34.98800 1.000 25.36532 ?  228 LEU B CG  1 
ATOM   4500 C  CD1 . LEU B 1 248 ? -18.70600 -4.12900  -33.67800 1.000 23.39749 ?  228 LEU B CD1 1 
ATOM   4501 C  CD2 . LEU B 1 248 ? -20.70400 -3.04500  -34.73500 1.000 23.76251 ?  228 LEU B CD2 1 
ATOM   4502 N  N   . TRP B 1 249 ? -16.93400 -1.32800  -38.07000 1.000 25.04902 ?  229 TRP B N   1 
ATOM   4503 C  CA  . TRP B 1 249 ? -16.14900 -0.22700  -38.62500 1.000 24.44811 ?  229 TRP B CA  1 
ATOM   4504 C  C   . TRP B 1 249 ? -16.88500 0.45800   -39.76800 1.000 25.60190 ?  229 TRP B C   1 
ATOM   4505 O  O   . TRP B 1 249 ? -17.07500 1.68000   -39.76700 1.000 26.58632 ?  229 TRP B O   1 
ATOM   4506 C  CB  . TRP B 1 249 ? -14.79600 -0.74800  -39.11500 1.000 27.33245 ?  229 TRP B CB  1 
ATOM   4507 C  CG  . TRP B 1 249 ? -14.11000 0.15000   -40.11500 1.000 29.27038 ?  229 TRP B CG  1 
ATOM   4508 C  CD1 . TRP B 1 249 ? -13.54700 1.37000   -39.87300 1.000 36.40166 ?  229 TRP B CD1 1 
ATOM   4509 C  CD2 . TRP B 1 249 ? -13.91700 -0.10900  -41.51600 1.000 29.78691 ?  229 TRP B CD2 1 
ATOM   4510 N  NE1 . TRP B 1 249 ? -13.01300 1.88500   -41.03300 1.000 33.65447 ?  229 TRP B NE1 1 
ATOM   4511 C  CE2 . TRP B 1 249 ? -13.22700 0.99700   -42.05400 1.000 35.56838 ?  229 TRP B CE2 1 
ATOM   4512 C  CE3 . TRP B 1 249 ? -14.25700 -1.16800  -42.36300 1.000 26.42709 ?  229 TRP B CE3 1 
ATOM   4513 C  CZ2 . TRP B 1 249 ? -12.87300 1.07500   -43.40400 1.000 36.75620 ?  229 TRP B CZ2 1 
ATOM   4514 C  CZ3 . TRP B 1 249 ? -13.90400 -1.08900  -43.70700 1.000 28.43613 ?  229 TRP B CZ3 1 
ATOM   4515 C  CH2 . TRP B 1 249 ? -13.22200 0.02400   -44.21100 1.000 31.65265 ?  229 TRP B CH2 1 
ATOM   4516 N  N   . ALA B 1 250 ? -17.30800 -0.32200  -40.75400 1.000 21.50864 ?  230 ALA B N   1 
ATOM   4517 C  CA  . ALA B 1 250 ? -17.94600 0.24900   -41.93100 1.000 29.99872 ?  230 ALA B CA  1 
ATOM   4518 C  C   . ALA B 1 250 ? -19.41200 0.58900   -41.67100 1.000 28.94857 ?  230 ALA B C   1 
ATOM   4519 O  O   . ALA B 1 250 ? -19.87200 1.68700   -42.00400 1.000 28.48705 ?  230 ALA B O   1 
ATOM   4520 C  CB  . ALA B 1 250 ? -17.81300 -0.72700  -43.09600 1.000 26.75658 ?  230 ALA B CB  1 
ATOM   4521 N  N   . GLY B 1 251 ? -20.15700 -0.34200  -41.07100 1.000 29.96514 ?  231 GLY B N   1 
ATOM   4522 C  CA  . GLY B 1 251 ? -21.58400 -0.14800  -40.87700 1.000 28.07639 ?  231 GLY B CA  1 
ATOM   4523 C  C   . GLY B 1 251 ? -21.94000 0.88500   -39.83200 1.000 30.12267 ?  231 GLY B C   1 
ATOM   4524 O  O   . GLY B 1 251 ? -23.06800 1.38900   -39.83500 1.000 27.52692 ?  231 GLY B O   1 
ATOM   4525 N  N   . TYR B 1 252 ? -21.01200 1.20600   -38.93000 1.000 23.41631 ?  232 TYR B N   1 
ATOM   4526 C  CA  . TYR B 1 252 ? -21.24200 2.25100   -37.94300 1.000 25.72295 ?  232 TYR B CA  1 
ATOM   4527 C  C   . TYR B 1 252 ? -20.32000 3.44600   -38.13200 1.000 23.82141 ?  232 TYR B C   1 
ATOM   4528 O  O   . TYR B 1 252 ? -20.80800 4.55400   -38.36300 1.000 27.17756 ?  232 TYR B O   1 
ATOM   4529 C  CB  . TYR B 1 252 ? -21.10300 1.69000   -36.52200 1.000 22.43576 ?  232 TYR B CB  1 
ATOM   4530 C  CG  . TYR B 1 252 ? -21.33500 2.73100   -35.45900 1.000 22.95159 ?  232 TYR B CG  1 
ATOM   4531 C  CD1 . TYR B 1 252 ? -22.59700 3.27700   -35.25400 1.000 21.72119 ?  232 TYR B CD1 1 
ATOM   4532 C  CD2 . TYR B 1 252 ? -20.28800 3.18100   -34.66600 1.000 21.11784 ?  232 TYR B CD2 1 
ATOM   4533 C  CE1 . TYR B 1 252 ? -22.81000 4.23800   -34.27900 1.000 24.63756 ?  232 TYR B CE1 1 
ATOM   4534 C  CE2 . TYR B 1 252 ? -20.49100 4.13900   -33.69200 1.000 20.31827 ?  232 TYR B CE2 1 
ATOM   4535 C  CZ  . TYR B 1 252 ? -21.75500 4.66500   -33.50200 1.000 24.57230 ?  232 TYR B CZ  1 
ATOM   4536 O  OH  . TYR B 1 252 ? -21.95800 5.62000   -32.53200 1.000 27.65134 ?  232 TYR B OH  1 
ATOM   4537 N  N   . GLU B 1 253 ? -19.00100 3.26600   -38.03400 1.000 25.75477 ?  233 GLU B N   1 
ATOM   4538 C  CA  . GLU B 1 253 ? -18.11900 4.42900   -37.99100 1.000 23.98917 ?  233 GLU B CA  1 
ATOM   4539 C  C   . GLU B 1 253 ? -18.17700 5.22500   -39.29000 1.000 26.35499 ?  233 GLU B C   1 
ATOM   4540 O  O   . GLU B 1 253 ? -18.25300 6.45800   -39.26400 1.000 28.69752 ?  233 GLU B O   1 
ATOM   4541 C  CB  . GLU B 1 253 ? -16.68500 4.00200   -37.68400 1.000 23.09922 ?  233 GLU B CB  1 
ATOM   4542 C  CG  . GLU B 1 253 ? -15.81000 5.17000   -37.26700 1.000 28.64204 ?  233 GLU B CG  1 
ATOM   4543 C  CD  . GLU B 1 253 ? -14.33500 4.86800   -37.37100 1.000 35.75060 ?  233 GLU B CD  1 
ATOM   4544 O  OE1 . GLU B 1 253 ? -13.97400 3.68100   -37.50400 1.000 32.12486 ?  233 GLU B OE1 1 
ATOM   4545 O  OE2 . GLU B 1 253 ? -13.53800 5.82700   -37.30800 1.000 33.54366 -1 233 GLU B OE2 1 
ATOM   4546 N  N   . ASN B 1 254 ? -18.15600 4.54300   -40.43700 1.000 23.72736 ?  234 ASN B N   1 
ATOM   4547 C  CA  . ASN B 1 254 ? -18.22600 5.25800   -41.70900 1.000 24.39856 ?  234 ASN B CA  1 
ATOM   4548 C  C   . ASN B 1 254 ? -19.59800 5.88900   -41.92100 1.000 26.79778 ?  234 ASN B C   1 
ATOM   4549 O  O   . ASN B 1 254 ? -19.69300 7.03200   -42.38300 1.000 29.05042 ?  234 ASN B O   1 
ATOM   4550 C  CB  . ASN B 1 254 ? -17.88000 4.32200   -42.86700 1.000 26.70139 ?  234 ASN B CB  1 
ATOM   4551 C  CG  . ASN B 1 254 ? -16.44100 3.83500   -42.81700 1.000 28.67165 ?  234 ASN B CG  1 
ATOM   4552 O  OD1 . ASN B 1 254 ? -15.63600 4.32000   -42.02700 1.000 33.34341 ?  234 ASN B OD1 1 
ATOM   4553 N  ND2 . ASN B 1 254 ? -16.11100 2.87500   -43.67200 1.000 28.65026 ?  234 ASN B ND2 1 
ATOM   4554 N  N   . LEU B 1 255 ? -20.67100 5.17400   -41.57900 1.000 26.00570 ?  235 LEU B N   1 
ATOM   4555 C  CA  . LEU B 1 255 ? -22.00500 5.65500   -41.92900 1.000 22.57428 ?  235 LEU B CA  1 
ATOM   4556 C  C   . LEU B 1 255 ? -22.41200 6.86300   -41.09400 1.000 23.37669 ?  235 LEU B C   1 
ATOM   4557 O  O   . LEU B 1 255 ? -23.06500 7.78100   -41.60500 1.000 29.47445 ?  235 LEU B O   1 
ATOM   4558 C  CB  . LEU B 1 255 ? -23.03100 4.53700   -41.77900 1.000 27.84650 ?  235 LEU B CB  1 
ATOM   4559 C  CG  . LEU B 1 255 ? -23.42900 3.88400   -43.10200 1.000 34.95804 ?  235 LEU B CG  1 
ATOM   4560 C  CD1 . LEU B 1 255 ? -24.33500 2.69000   -42.86800 1.000 30.26558 ?  235 LEU B CD1 1 
ATOM   4561 C  CD2 . LEU B 1 255 ? -24.09200 4.90300   -44.02000 1.000 34.77555 ?  235 LEU B CD2 1 
ATOM   4562 N  N   . VAL B 1 256 ? -22.05700 6.87400   -39.80600 1.000 23.34777 ?  236 VAL B N   1 
ATOM   4563 C  CA  . VAL B 1 256 ? -22.43300 7.99000   -38.93700 1.000 26.43459 ?  236 VAL B CA  1 
ATOM   4564 C  C   . VAL B 1 256 ? -21.94700 9.30900   -39.52100 1.000 27.70800 ?  236 VAL B C   1 
ATOM   4565 O  O   . VAL B 1 256 ? -22.66100 10.31900  -39.50200 1.000 27.28313 ?  236 VAL B O   1 
ATOM   4566 C  CB  . VAL B 1 256 ? -21.88500 7.77600   -37.51400 1.000 25.46273 ?  236 VAL B CB  1 
ATOM   4567 C  CG1 . VAL B 1 256 ? -22.08600 9.02600   -36.66900 1.000 28.44501 ?  236 VAL B CG1 1 
ATOM   4568 C  CG2 . VAL B 1 256 ? -22.55600 6.59200   -36.86000 1.000 25.01308 ?  236 VAL B CG2 1 
ATOM   4569 N  N   . HIS B 1 257 ? -20.73000 9.31700   -40.06300 1.000 25.41455 ?  237 HIS B N   1 
ATOM   4570 C  CA  . HIS B 1 257 ? -20.12700 10.56200  -40.51100 1.000 28.75860 ?  237 HIS B CA  1 
ATOM   4571 C  C   . HIS B 1 257 ? -20.43800 10.88300  -41.96400 1.000 26.13762 ?  237 HIS B C   1 
ATOM   4572 O  O   . HIS B 1 257 ? -20.44600 12.06200  -42.33400 1.000 34.81298 ?  237 HIS B O   1 
ATOM   4573 C  CB  . HIS B 1 257 ? -18.61900 10.51200  -40.27200 1.000 24.21759 ?  237 HIS B CB  1 
ATOM   4574 C  CG  . HIS B 1 257 ? -18.26100 10.43700  -38.82100 1.000 30.74572 ?  237 HIS B CG  1 
ATOM   4575 N  ND1 . HIS B 1 257 ? -18.71200 11.35800  -37.90000 1.000 30.73503 ?  237 HIS B ND1 1 
ATOM   4576 C  CD2 . HIS B 1 257 ? -17.53700 9.53100   -38.12400 1.000 34.33906 ?  237 HIS B CD2 1 
ATOM   4577 C  CE1 . HIS B 1 257 ? -18.25900 11.03700  -36.70200 1.000 32.95080 ?  237 HIS B CE1 1 
ATOM   4578 N  NE2 . HIS B 1 257 ? -17.54300 9.93200   -36.81000 1.000 36.70440 ?  237 HIS B NE2 1 
ATOM   4579 N  N   . LEU B 1 258 ? -20.69800 9.87300   -42.79500 1.000 27.09037 ?  238 LEU B N   1 
ATOM   4580 C  CA  . LEU B 1 258 ? -21.31700 10.14200  -44.09000 1.000 28.64361 ?  238 LEU B CA  1 
ATOM   4581 C  C   . LEU B 1 258 ? -22.56000 11.00600  -43.91700 1.000 32.24493 ?  238 LEU B C   1 
ATOM   4582 O  O   . LEU B 1 258 ? -22.75900 11.99100  -44.63800 1.000 31.74705 ?  238 LEU B O   1 
ATOM   4583 C  CB  . LEU B 1 258 ? -21.67200 8.83100   -44.79500 1.000 27.67989 ?  238 LEU B CB  1 
ATOM   4584 C  CG  . LEU B 1 258 ? -22.10300 8.92900   -46.26400 1.000 34.94998 ?  238 LEU B CG  1 
ATOM   4585 C  CD1 . LEU B 1 258 ? -21.70300 7.68300   -47.03100 1.000 36.70529 ?  238 LEU B CD1 1 
ATOM   4586 C  CD2 . LEU B 1 258 ? -23.60300 9.15900   -46.39500 1.000 41.11199 ?  238 LEU B CD2 1 
ATOM   4587 N  N   . ILE B 1 259 ? -23.40600 10.65100  -42.94900 1.000 35.43644 ?  239 ILE B N   1 
ATOM   4588 C  CA  . ILE B 1 259 ? -24.63900 11.39600  -42.72100 1.000 24.84136 ?  239 ILE B CA  1 
ATOM   4589 C  C   . ILE B 1 259 ? -24.33600 12.75500  -42.10000 1.000 30.41624 ?  239 ILE B C   1 
ATOM   4590 O  O   . ILE B 1 259 ? -24.85600 13.78700  -42.54000 1.000 31.38580 ?  239 ILE B O   1 
ATOM   4591 C  CB  . ILE B 1 259 ? -25.59800 10.57300  -41.84300 1.000 35.26202 ?  239 ILE B CB  1 
ATOM   4592 C  CG1 . ILE B 1 259 ? -25.99600 9.27700   -42.55400 1.000 26.51432 ?  239 ILE B CG1 1 
ATOM   4593 C  CG2 . ILE B 1 259 ? -26.82500 11.39100  -41.48100 1.000 31.36498 ?  239 ILE B CG2 1 
ATOM   4594 C  CD1 . ILE B 1 259 ? -26.37500 8.15400   -41.60900 1.000 27.44829 ?  239 ILE B CD1 1 
ATOM   4595 N  N   . GLY B 1 260 ? -23.48400 12.77600  -41.07300 1.000 24.98529 ?  240 GLY B N   1 
ATOM   4596 C  CA  . GLY B 1 260 ? -23.20500 14.02300  -40.37700 1.000 30.07399 ?  240 GLY B CA  1 
ATOM   4597 C  C   . GLY B 1 260 ? -22.51600 15.05000  -41.25700 1.000 37.43692 ?  240 GLY B C   1 
ATOM   4598 O  O   . GLY B 1 260 ? -22.92400 16.21400  -41.30800 1.000 28.26017 ?  240 GLY B O   1 
ATOM   4599 N  N   . ASN B 1 261 ? -21.44800 14.63600  -41.95000 1.000 30.66001 ?  241 ASN B N   1 
ATOM   4600 C  CA  . ASN B 1 261 ? -20.78500 15.53900  -42.88600 1.000 29.78127 ?  241 ASN B CA  1 
ATOM   4601 C  C   . ASN B 1 261 ? -21.72300 15.96800  -44.00700 1.000 37.47864 ?  241 ASN B C   1 
ATOM   4602 O  O   . ASN B 1 261 ? -21.62700 17.10100  -44.49500 1.000 37.85696 ?  241 ASN B O   1 
ATOM   4603 C  CB  . ASN B 1 261 ? -19.53200 14.88100  -43.46900 1.000 31.61928 ?  241 ASN B CB  1 
ATOM   4604 C  CG  . ASN B 1 261 ? -18.55200 14.42700  -42.39900 1.000 25.96375 ?  241 ASN B CG  1 
ATOM   4605 O  OD1 . ASN B 1 261 ? -18.65500 14.81500  -41.23400 1.000 27.80232 ?  241 ASN B OD1 1 
ATOM   4606 N  ND2 . ASN B 1 261 ? -17.59500 13.59100  -42.79400 1.000 29.94722 ?  241 ASN B ND2 1 
ATOM   4607 N  N   . GLY B 1 262 ? -22.63600 15.08600  -44.42200 1.000 35.41847 ?  242 GLY B N   1 
ATOM   4608 C  CA  . GLY B 1 262 ? -23.56100 15.44100  -45.48700 1.000 39.12069 ?  242 GLY B CA  1 
ATOM   4609 C  C   . GLY B 1 262 ? -24.51500 16.55100  -45.08900 1.000 38.96595 ?  242 GLY B C   1 
ATOM   4610 O  O   . GLY B 1 262 ? -24.82600 17.43700  -45.89000 1.000 36.47897 ?  242 GLY B O   1 
ATOM   4611 N  N   . VAL B 1 263 ? -24.99100 16.52100  -43.84400 1.000 33.89687 ?  243 VAL B N   1 
ATOM   4612 C  CA  . VAL B 1 263 ? -25.90400 17.56000  -43.38300 1.000 32.34381 ?  243 VAL B CA  1 
ATOM   4613 C  C   . VAL B 1 263 ? -25.18200 18.89700  -43.27200 1.000 39.10255 ?  243 VAL B C   1 
ATOM   4614 O  O   . VAL B 1 263 ? -25.71700 19.93700  -43.67600 1.000 33.00471 ?  243 VAL B O   1 
ATOM   4615 C  CB  . VAL B 1 263 ? -26.55800 17.14700  -42.05300 1.000 34.55914 ?  243 VAL B CB  1 
ATOM   4616 C  CG1 . VAL B 1 263 ? -27.40100 18.28300  -41.50700 1.000 34.59730 ?  243 VAL B CG1 1 
ATOM   4617 C  CG2 . VAL B 1 263 ? -27.40600 15.89700  -42.25800 1.000 30.03696 ?  243 VAL B CG2 1 
ATOM   4618 N  N   . ARG B 1 264 ? -23.95700 18.89500  -42.72900 1.000 35.00272 ?  244 ARG B N   1 
ATOM   4619 C  CA  . ARG B 1 264 ? -23.14600 20.11000  -42.72400 1.000 37.66208 ?  244 ARG B CA  1 
ATOM   4620 C  C   . ARG B 1 264 ? -22.94900 20.63700  -44.13700 1.000 39.64658 ?  244 ARG B C   1 
ATOM   4621 O  O   . ARG B 1 264 ? -23.06900 21.84200  -44.38700 1.000 44.78532 ?  244 ARG B O   1 
ATOM   4622 C  CB  . ARG B 1 264 ? -21.78100 19.85000  -42.08600 1.000 35.23926 ?  244 ARG B CB  1 
ATOM   4623 C  CG  . ARG B 1 264 ? -21.08200 21.10700  -41.57100 1.000 40.40339 ?  244 ARG B CG  1 
ATOM   4624 C  CD  . ARG B 1 264 ? -19.57100 20.92400  -41.61400 1.000 42.68818 ?  244 ARG B CD  1 
ATOM   4625 N  NE  . ARG B 1 264 ? -19.13700 20.62800  -42.97400 1.000 43.05289 ?  244 ARG B NE  1 
ATOM   4626 C  CZ  . ARG B 1 264 ? -19.05600 21.52600  -43.94900 1.000 43.23949 ?  244 ARG B CZ  1 
ATOM   4627 N  NH1 . ARG B 1 264 ? -19.21900 22.81900  -43.71600 1.000 41.17750 ?  244 ARG B NH1 1 
ATOM   4628 N  NH2 . ARG B 1 264 ? -18.79600 21.11700  -45.18700 1.000 38.55406 ?  244 ARG B NH2 1 
ATOM   4629 N  N   . ALA B 1 265 ? -22.62600 19.74000  -45.07500 1.000 36.12363 ?  245 ALA B N   1 
ATOM   4630 C  CA  . ALA B 1 265 ? -22.42800 20.14000  -46.46300 1.000 38.35566 ?  245 ALA B CA  1 
ATOM   4631 C  C   . ALA B 1 265 ? -23.65400 20.86400  -47.00200 1.000 40.99089 ?  245 ALA B C   1 
ATOM   4632 O  O   . ALA B 1 265 ? -23.53900 21.90900  -47.65200 1.000 43.16840 ?  245 ALA B O   1 
ATOM   4633 C  CB  . ALA B 1 265 ? -22.10800 18.91400  -47.31700 1.000 34.11498 ?  245 ALA B CB  1 
ATOM   4634 N  N   . LEU B 1 266 ? -24.84100 20.32100  -46.72800 1.000 42.08206 ?  246 LEU B N   1 
ATOM   4635 C  CA  . LEU B 1 266 ? -26.07500 20.95500  -47.18100 1.000 34.20281 ?  246 LEU B CA  1 
ATOM   4636 C  C   . LEU B 1 266 ? -26.27600 22.30200  -46.49900 1.000 37.34742 ?  246 LEU B C   1 
ATOM   4637 O  O   . LEU B 1 266 ? -26.59700 23.30200  -47.15200 1.000 46.12669 ?  246 LEU B O   1 
ATOM   4638 C  CB  . LEU B 1 266 ? -27.25600 20.02500  -46.91300 1.000 40.37276 ?  246 LEU B CB  1 
ATOM   4639 C  CG  . LEU B 1 266 ? -27.25600 18.74900  -47.75900 1.000 38.51279 ?  246 LEU B CG  1 
ATOM   4640 C  CD1 . LEU B 1 266 ? -28.25600 17.74100  -47.21800 1.000 42.82261 ?  246 LEU B CD1 1 
ATOM   4641 C  CD2 . LEU B 1 266 ? -27.54700 19.06700  -49.21800 1.000 37.04035 ?  246 LEU B CD2 1 
ATOM   4642 N  N   . LEU B 1 267 ? -26.08400 22.34700  -45.17700 1.000 34.77445 ?  247 LEU B N   1 
ATOM   4643 C  CA  . LEU B 1 267 ? -26.18000 23.60800  -44.44800 1.000 42.05163 ?  247 LEU B CA  1 
ATOM   4644 C  C   . LEU B 1 267 ? -25.17000 24.62900  -44.96000 1.000 47.94280 ?  247 LEU B C   1 
ATOM   4645 O  O   . LEU B 1 267 ? -25.40200 25.84000  -44.85800 1.000 44.77206 ?  247 LEU B O   1 
ATOM   4646 C  CB  . LEU B 1 267 ? -25.97000 23.36500  -42.95100 1.000 46.43366 ?  247 LEU B CB  1 
ATOM   4647 C  CG  . LEU B 1 267 ? -27.02100 22.54000  -42.20000 1.000 45.61110 ?  247 LEU B CG  1 
ATOM   4648 C  CD1 . LEU B 1 267 ? -26.42300 21.98200  -40.91700 1.000 40.80614 ?  247 LEU B CD1 1 
ATOM   4649 C  CD2 . LEU B 1 267 ? -28.25800 23.37300  -41.89800 1.000 36.07221 ?  247 LEU B CD2 1 
ATOM   4650 N  N   . ALA B 1 268 ? -24.04700 24.16200  -45.51000 1.000 43.25500 ?  248 ALA B N   1 
ATOM   4651 C  CA  . ALA B 1 268 ? -23.05000 25.06800  -46.06400 1.000 46.42395 ?  248 ALA B CA  1 
ATOM   4652 C  C   . ALA B 1 268 ? -23.41600 25.53000  -47.46900 1.000 48.37921 ?  248 ALA B C   1 
ATOM   4653 O  O   . ALA B 1 268 ? -23.08100 26.65600  -47.85200 1.000 53.44601 ?  248 ALA B O   1 
ATOM   4654 C  CB  . ALA B 1 268 ? -21.67500 24.39700  -46.07200 1.000 42.86811 ?  248 ALA B CB  1 
ATOM   4655 N  N   . ALA B 1 269 ? -24.09700 24.68600  -48.24400 1.000 47.67410 ?  249 ALA B N   1 
ATOM   4656 C  CA  . ALA B 1 269 ? -24.52900 25.03500  -49.59100 1.000 45.80475 ?  249 ALA B CA  1 
ATOM   4657 C  C   . ALA B 1 269 ? -26.04800 25.14900  -49.63200 1.000 47.28873 ?  249 ALA B C   1 
ATOM   4658 O  O   . ALA B 1 269 ? -26.72800 24.22300  -50.09700 1.000 51.22656 ?  249 ALA B O   1 
ATOM   4659 C  CB  . ALA B 1 269 ? -24.03900 23.99500  -50.59900 1.000 41.14096 ?  249 ALA B CB  1 
ATOM   4660 N  N   . PRO B 1 270 ? -26.61400 26.26800  -49.17000 1.000 45.34565 ?  250 PRO B N   1 
ATOM   4661 C  CA  . PRO B 1 270 ? -28.07500 26.33600  -49.00400 1.000 45.55395 ?  250 PRO B CA  1 
ATOM   4662 C  C   . PRO B 1 270 ? -28.85300 26.20400  -50.30000 1.000 49.01433 ?  250 PRO B C   1 
ATOM   4663 O  O   . PRO B 1 270 ? -30.02000 25.79200  -50.26500 1.000 53.30775 ?  250 PRO B O   1 
ATOM   4664 C  CB  . PRO B 1 270 ? -28.28000 27.71300  -48.35600 1.000 52.29259 ?  250 PRO B CB  1 
ATOM   4665 C  CG  . PRO B 1 270 ? -27.07100 28.49800  -48.79100 1.000 49.70674 ?  250 PRO B CG  1 
ATOM   4666 C  CD  . PRO B 1 270 ? -25.96300 27.50100  -48.70100 1.000 47.70520 ?  250 PRO B CD  1 
ATOM   4667 N  N   . ASP B 1 271 ? -28.25200 26.53700  -51.44500 1.000 50.00267 ?  251 ASP B N   1 
ATOM   4668 C  CA  . ASP B 1 271 ? -28.96300 26.39300  -52.71200 1.000 52.50834 ?  251 ASP B CA  1 
ATOM   4669 C  C   . ASP B 1 271 ? -29.01400 24.94300  -53.17100 1.000 49.89821 ?  251 ASP B C   1 
ATOM   4670 O  O   . ASP B 1 271 ? -29.99900 24.52800  -53.79400 1.000 46.13097 ?  251 ASP B O   1 
ATOM   4671 C  CB  . ASP B 1 271 ? -28.31100 27.26500  -53.78600 1.000 57.36847 ?  251 ASP B CB  1 
ATOM   4672 N  N   . GLN B 1 272 ? -27.96300 24.17000  -52.88100 1.000 47.68991 ?  252 GLN B N   1 
ATOM   4673 C  CA  . GLN B 1 272 ? -27.98600 22.73600  -53.15100 1.000 47.80041 ?  252 GLN B CA  1 
ATOM   4674 C  C   . GLN B 1 272 ? -29.15500 22.06400  -52.44500 1.000 46.07211 ?  252 GLN B C   1 
ATOM   4675 O  O   . GLN B 1 272 ? -29.84000 21.21100  -53.02400 1.000 45.39206 ?  252 GLN B O   1 
ATOM   4676 C  CB  . GLN B 1 272 ? -26.66900 22.10400  -52.70100 1.000 43.72305 ?  252 GLN B CB  1 
ATOM   4677 C  CG  . GLN B 1 272 ? -25.48600 22.40000  -53.60100 1.000 48.63313 ?  252 GLN B CG  1 
ATOM   4678 C  CD  . GLN B 1 272 ? -25.83900 22.31100  -55.07000 1.000 46.20349 ?  252 GLN B CD  1 
ATOM   4679 O  OE1 . GLN B 1 272 ? -26.20400 21.24700  -55.57000 1.000 38.27153 ?  252 GLN B OE1 1 
ATOM   4680 N  NE2 . GLN B 1 272 ? -25.72200 23.43100  -55.77500 1.000 49.46883 ?  252 GLN B NE2 1 
ATOM   4681 N  N   . LEU B 1 273 ? -29.40900 22.46300  -51.20400 1.000 49.07783 ?  253 LEU B N   1 
ATOM   4682 C  CA  . LEU B 1 273 ? -30.49800 21.84800  -50.39900 1.000 48.26254 ?  253 LEU B CA  1 
ATOM   4683 C  C   . LEU B 1 273 ? -31.85400 22.23900  -50.99700 1.000 50.67667 ?  253 LEU B C   1 
ATOM   4684 O  O   . LEU B 1 273 ? -32.71100 21.35700  -51.12900 1.000 50.25210 ?  253 LEU B O   1 
ATOM   4685 C  CB  . LEU B 1 273 ? -30.34800 22.34300  -48.96200 1.000 45.21815 ?  253 LEU B CB  1 
ATOM   4686 C  CG  . LEU B 1 273 ? -31.34300 21.77600  -47.95400 1.000 41.84275 ?  253 LEU B CG  1 
ATOM   4687 C  CD1 . LEU B 1 273 ? -31.50500 20.27800  -48.14100 1.000 45.96531 ?  253 LEU B CD1 1 
ATOM   4688 C  CD2 . LEU B 1 273 ? -30.90100 22.09200  -46.53700 1.000 38.65166 ?  253 LEU B CD2 1 
ATOM   4689 N  N   . ALA B 1 274 ? -32.02000 23.51200  -51.35800 1.000 52.57823 ?  254 ALA B N   1 
ATOM   4690 C  CA  . ALA B 1 274 ? -33.26600 23.95500  -52.02900 1.000 52.04974 ?  254 ALA B CA  1 
ATOM   4691 C  C   . ALA B 1 274 ? -33.67400 22.97600  -53.13600 1.000 52.53688 ?  254 ALA B C   1 
ATOM   4692 O  O   . ALA B 1 274 ? -34.79600 22.46900  -53.08300 1.000 52.14991 ?  254 ALA B O   1 
ATOM   4693 C  CB  . ALA B 1 274 ? -33.05100 25.32700  -52.58000 1.000 46.11553 ?  254 ALA B CB  1 
ATOM   4694 N  N   . ASP B 1 275 ? -32.79200 22.71800  -54.09900 1.000 47.67981 ?  255 ASP B N   1 
ATOM   4695 C  CA  . ASP B 1 275 ? -33.15300 21.86000  -55.25700 1.000 56.13297 ?  255 ASP B CA  1 
ATOM   4696 C  C   . ASP B 1 275 ? -33.38500 20.41300  -54.82000 1.000 56.94618 ?  255 ASP B C   1 
ATOM   4697 O  O   . ASP B 1 275 ? -34.12500 19.69900  -55.51600 1.000 53.43397 ?  255 ASP B O   1 
ATOM   4698 C  CB  . ASP B 1 275 ? -32.09300 21.94600  -56.36500 1.000 55.97790 ?  255 ASP B CB  1 
ATOM   4699 C  CG  . ASP B 1 275 ? -30.69100 22.20800  -55.84800 1.000 49.82110 ?  255 ASP B CG  1 
ATOM   4700 N  N   . LEU B 1 276 ? -32.77800 19.99000  -53.70800 1.000 54.24011 ?  256 LEU B N   1 
ATOM   4701 C  CA  . LEU B 1 276 ? -33.07000 18.61700  -53.23000 1.000 53.40260 ?  256 LEU B CA  1 
ATOM   4702 C  C   . LEU B 1 276 ? -34.45500 18.61100  -52.58500 1.000 52.18666 ?  256 LEU B C   1 
ATOM   4703 O  O   . LEU B 1 276 ? -35.21900 17.66700  -52.83100 1.000 52.68968 ?  256 LEU B O   1 
ATOM   4704 C  CB  . LEU B 1 276 ? -31.98500 18.18100  -52.24400 1.000 48.59350 ?  256 LEU B CB  1 
ATOM   4705 C  CG  . LEU B 1 276 ? -32.15300 16.78800  -51.64900 1.000 47.62468 ?  256 LEU B CG  1 
ATOM   4706 C  CD1 . LEU B 1 276 ? -32.11500 15.73200  -52.73800 1.000 41.70744 ?  256 LEU B CD1 1 
ATOM   4707 C  CD2 . LEU B 1 276 ? -31.08500 16.52500  -50.60200 1.000 47.47925 ?  256 LEU B CD2 1 
ATOM   4708 N  N   . ARG B 1 277 ? -34.75900 19.63900  -51.80600 1.000 54.24310 ?  257 ARG B N   1 
ATOM   4709 C  CA  . ARG B 1 277 ? -36.04600 19.64900  -51.06400 1.000 54.75233 ?  257 ARG B CA  1 
ATOM   4710 C  C   . ARG B 1 277 ? -37.20000 19.61900  -52.06600 1.000 55.79025 ?  257 ARG B C   1 
ATOM   4711 O  O   . ARG B 1 277 ? -38.30000 19.24000  -51.67000 1.000 58.80767 ?  257 ARG B O   1 
ATOM   4712 C  CB  . ARG B 1 277 ? -36.07600 20.87200  -50.14900 1.000 50.22134 ?  257 ARG B CB  1 
ATOM   4713 N  N   . SER B 1 278 ? -36.93600 19.98700  -53.31500 1.000 60.31580 ?  258 SER B N   1 
ATOM   4714 C  CA  . SER B 1 278 ? -37.99100 20.09000  -54.31700 1.000 64.61708 ?  258 SER B CA  1 
ATOM   4715 C  C   . SER B 1 278 ? -38.09600 18.85900  -55.20700 1.000 64.65105 ?  258 SER B C   1 
ATOM   4716 O  O   . SER B 1 278 ? -39.20800 18.40500  -55.49500 1.000 58.66718 ?  258 SER B O   1 
ATOM   4717 C  CB  . SER B 1 278 ? -37.76800 21.32600  -55.19300 1.000 59.23535 ?  258 SER B CB  1 
ATOM   4718 O  OG  . SER B 1 278 ? -37.89000 22.51400  -54.43200 1.000 66.39105 ?  258 SER B OG  1 
ATOM   4719 N  N   . ASP B 1 279 ? -36.97000 18.31000  -55.65100 1.000 55.44044 ?  259 ASP B N   1 
ATOM   4720 C  CA  . ASP B 1 279 ? -36.95500 17.16500  -56.55700 1.000 59.18699 ?  259 ASP B CA  1 
ATOM   4721 C  C   . ASP B 1 279 ? -36.56700 15.93700  -55.73900 1.000 56.82942 ?  259 ASP B C   1 
ATOM   4722 O  O   . ASP B 1 279 ? -35.38300 15.69600  -55.48500 1.000 54.89781 ?  259 ASP B O   1 
ATOM   4723 C  CB  . ASP B 1 279 ? -35.99400 17.40600  -57.72000 1.000 62.35163 ?  259 ASP B CB  1 
ATOM   4724 C  CG  . ASP B 1 279 ? -35.98600 16.26400  -58.72100 1.000 60.62179 ?  259 ASP B CG  1 
ATOM   4725 O  OD1 . ASP B 1 279 ? -36.77500 15.31100  -58.54100 1.000 61.13647 -1 259 ASP B OD1 1 
ATOM   4726 O  OD2 . ASP B 1 279 ? -35.19700 16.32100  -59.69000 1.000 63.91964 -1 259 ASP B OD2 1 
ATOM   4727 N  N   . GLU B 1 280 ? -37.57400 15.16700  -55.31800 1.000 49.29611 ?  260 GLU B N   1 
ATOM   4728 C  CA  . GLU B 1 280 ? -37.33600 13.95000  -54.55000 1.000 58.93003 ?  260 GLU B CA  1 
ATOM   4729 C  C   . GLU B 1 280 ? -36.73400 12.83200  -55.39000 1.000 59.17226 ?  260 GLU B C   1 
ATOM   4730 O  O   . GLU B 1 280 ? -36.31900 11.81200  -54.82600 1.000 55.87590 ?  260 GLU B O   1 
ATOM   4731 C  CB  . GLU B 1 280 ? -38.63900 13.47000  -53.90600 1.000 61.57954 ?  260 GLU B CB  1 
ATOM   4732 N  N   . ALA B 1 281 ? -36.62400 13.05800  -56.69200 1.000 53.14357 ?  261 ALA B N   1 
ATOM   4733 C  CA  . ALA B 1 281 ? -35.97400 12.05700  -57.55900 1.000 57.82354 ?  261 ALA B CA  1 
ATOM   4734 C  C   . ALA B 1 281 ? -34.46000 12.28300  -57.53700 1.000 47.25168 ?  261 ALA B C   1 
ATOM   4735 O  O   . ALA B 1 281 ? -33.73200 11.44800  -58.07100 1.000 49.65491 ?  261 ALA B O   1 
ATOM   4736 C  CB  . ALA B 1 281 ? -36.52100 12.20000  -58.95000 1.000 50.62708 ?  261 ALA B CB  1 
ATOM   4737 N  N   . LEU B 1 282 ? -34.02400 13.39200  -56.95100 1.000 48.92532 ?  262 LEU B N   1 
ATOM   4738 C  CA  . LEU B 1 282 ? -32.58000 13.72900  -56.95700 1.000 50.51909 ?  262 LEU B CA  1 
ATOM   4739 C  C   . LEU B 1 282 ? -31.90300 13.05300  -55.76700 1.000 45.54100 ?  262 LEU B C   1 
ATOM   4740 O  O   . LEU B 1 282 ? -30.69100 12.84600  -55.83300 1.000 44.13181 ?  262 LEU B O   1 
ATOM   4741 C  CB  . LEU B 1 282 ? -32.43500 15.25300  -56.88000 1.000 45.88836 ?  262 LEU B CB  1 
ATOM   4742 C  CG  . LEU B 1 282 ? -31.01200 15.80400  -56.81600 1.000 50.48763 ?  262 LEU B CG  1 
ATOM   4743 C  CD1 . LEU B 1 282 ? -30.26400 15.53000  -58.10800 1.000 49.07207 ?  262 LEU B CD1 1 
ATOM   4744 C  CD2 . LEU B 1 282 ? -31.02000 17.29200  -56.50100 1.000 48.92054 ?  262 LEU B CD2 1 
ATOM   4745 N  N   . LEU B 1 283 ? -32.67500 12.70600  -54.73800 1.000 47.73553 ?  263 LEU B N   1 
ATOM   4746 C  CA  . LEU B 1 283 ? -32.06000 12.13800  -53.50200 1.000 46.29013 ?  263 LEU B CA  1 
ATOM   4747 C  C   . LEU B 1 283 ? -30.94000 11.14900  -53.84000 1.000 42.85638 ?  263 LEU B C   1 
ATOM   4748 O  O   . LEU B 1 283 ? -29.82800 11.38200  -53.36200 1.000 40.87772 ?  263 LEU B O   1 
ATOM   4749 C  CB  . LEU B 1 283 ? -33.11700 11.49200  -52.59600 1.000 43.43546 ?  263 LEU B CB  1 
ATOM   4750 C  CG  . LEU B 1 283 ? -32.67200 11.25900  -51.15400 1.000 39.94570 ?  263 LEU B CG  1 
ATOM   4751 N  N   . PRO B 1 284 ? -31.15200 10.05500  -54.59200 1.000 41.90657 ?  264 PRO B N   1 
ATOM   4752 C  CA  . PRO B 1 284 ? -30.04800 9.12300   -54.82600 1.000 42.12237 ?  264 PRO B CA  1 
ATOM   4753 C  C   . PRO B 1 284 ? -28.77800 9.80100   -55.37100 1.000 47.28879 ?  264 PRO B C   1 
ATOM   4754 O  O   . PRO B 1 284 ? -27.70800 9.44600   -54.91300 1.000 44.45825 ?  264 PRO B O   1 
ATOM   4755 C  CB  . PRO B 1 284 ? -30.64800 8.11000   -55.80600 1.000 39.96064 ?  264 PRO B CB  1 
ATOM   4756 C  CG  . PRO B 1 284 ? -32.12400 8.15600   -55.50100 1.000 43.82183 ?  264 PRO B CG  1 
ATOM   4757 C  CD  . PRO B 1 284 ? -32.39800 9.61800   -55.22400 1.000 38.81359 ?  264 PRO B CD  1 
ATOM   4758 N  N   . ARG B 1 285 ? -28.92200 10.80500  -56.23400 1.000 38.29005 ?  265 ARG B N   1 
ATOM   4759 C  CA  . ARG B 1 285 ? -27.75000 11.45500  -56.86500 1.000 37.68889 ?  265 ARG B CA  1 
ATOM   4760 C  C   . ARG B 1 285 ? -27.10600 12.40700  -55.86600 1.000 42.36651 ?  265 ARG B C   1 
ATOM   4761 O  O   . ARG B 1 285 ? -25.87100 12.45700  -55.81000 1.000 42.61993 ?  265 ARG B O   1 
ATOM   4762 C  CB  . ARG B 1 285 ? -28.20100 12.27000  -58.08000 1.000 44.37947 ?  265 ARG B CB  1 
ATOM   4763 C  CG  . ARG B 1 285 ? -27.07000 12.77200  -58.96400 1.000 43.39417 ?  265 ARG B CG  1 
ATOM   4764 N  N   . ALA B 1 286 ? -27.93100 13.12300  -55.10900 1.000 39.59500 ?  266 ALA B N   1 
ATOM   4765 C  CA  . ALA B 1 286 ? -27.41600 14.09900  -54.13000 1.000 40.11211 ?  266 ALA B CA  1 
ATOM   4766 C  C   . ALA B 1 286 ? -26.59000 13.35200  -53.07900 1.000 39.95773 ?  266 ALA B C   1 
ATOM   4767 O  O   . ALA B 1 286 ? -25.56800 13.88600  -52.65400 1.000 38.05572 ?  266 ALA B O   1 
ATOM   4768 C  CB  . ALA B 1 286 ? -28.57300 14.84000  -53.52500 1.000 43.60629 ?  266 ALA B CB  1 
ATOM   4769 N  N   . ILE B 1 287 ? -27.02500 12.15300  -52.70700 1.000 37.99821 ?  267 ILE B N   1 
ATOM   4770 C  CA  . ILE B 1 287 ? -26.27600 11.30400  -51.73500 1.000 40.75758 ?  267 ILE B CA  1 
ATOM   4771 C  C   . ILE B 1 287 ? -24.89900 10.96300  -52.31800 1.000 42.19435 ?  267 ILE B C   1 
ATOM   4772 O  O   . ILE B 1 287 ? -23.90500 11.16700  -51.61600 1.000 37.94758 ?  267 ILE B O   1 
ATOM   4773 C  CB  . ILE B 1 287 ? -27.09500 10.03800  -51.42000 1.000 36.27012 ?  267 ILE B CB  1 
ATOM   4774 C  CG1 . ILE B 1 287 ? -28.34400 10.36600  -50.60200 1.000 38.44712 ?  267 ILE B CG1 1 
ATOM   4775 C  CG2 . ILE B 1 287 ? -26.24200 8.98100   -50.73900 1.000 40.42944 ?  267 ILE B CG2 1 
ATOM   4776 C  CD1 . ILE B 1 287 ? -29.41800 9.32300   -50.72500 1.000 37.67451 ?  267 ILE B CD1 1 
ATOM   4777 N  N   . GLU B 1 288 ? -24.85700 10.50100  -53.57200 1.000 37.22191 ?  268 GLU B N   1 
ATOM   4778 C  CA  . GLU B 1 288 ? -23.55800 10.20500  -54.23100 1.000 37.68102 ?  268 GLU B CA  1 
ATOM   4779 C  C   . GLU B 1 288 ? -22.66200 11.44200  -54.21100 1.000 36.46441 ?  268 GLU B C   1 
ATOM   4780 O  O   . GLU B 1 288 ? -21.45300 11.29000  -54.03100 1.000 41.89087 ?  268 GLU B O   1 
ATOM   4781 C  CB  . GLU B 1 288 ? -23.75600 9.67500   -55.64800 1.000 36.35702 ?  268 GLU B CB  1 
ATOM   4782 C  CG  . GLU B 1 288 ? -24.50700 8.36500   -55.68400 1.000 41.44397 ?  268 GLU B CG  1 
ATOM   4783 C  CD  . GLU B 1 288 ? -23.81300 7.25100   -54.92700 1.000 51.14993 ?  268 GLU B CD  1 
ATOM   4784 O  OE1 . GLU B 1 288 ? -22.87600 6.66200   -55.48900 1.000 57.23912 ?  268 GLU B OE1 1 
ATOM   4785 O  OE2 . GLU B 1 288 ? -24.21400 6.97900   -53.78000 1.000 54.62582 -1 268 GLU B OE2 1 
ATOM   4786 N  N   . GLU B 1 289 ? -23.25200 12.61100  -54.36600 1.000 31.23867 ?  269 GLU B N   1 
ATOM   4787 C  CA  . GLU B 1 289 ? -22.44500 13.85400  -54.37700 1.000 42.38209 ?  269 GLU B CA  1 
ATOM   4788 C  C   . GLU B 1 289 ? -22.02500 14.25300  -52.95200 1.000 39.94380 ?  269 GLU B C   1 
ATOM   4789 O  O   . GLU B 1 289 ? -20.89500 14.72600  -52.78300 1.000 37.93692 ?  269 GLU B O   1 
ATOM   4790 C  CB  . GLU B 1 289 ? -23.18700 14.98800  -55.08600 1.000 42.54279 ?  269 GLU B CB  1 
ATOM   4791 C  CG  . GLU B 1 289 ? -22.51800 16.33900  -54.90700 1.000 41.16133 ?  269 GLU B CG  1 
ATOM   4792 C  CD  . GLU B 1 289 ? -21.17800 16.54500  -55.59300 1.000 44.88158 ?  269 GLU B CD  1 
ATOM   4793 O  OE1 . GLU B 1 289 ? -20.71400 15.63100  -56.29200 1.000 42.34909 ?  269 GLU B OE1 1 
ATOM   4794 O  OE2 . GLU B 1 289 ? -20.60300 17.63200  -55.42800 1.000 48.67092 -1 269 GLU B OE2 1 
ATOM   4795 N  N   . LEU B 1 290 ? -22.89100 14.03100  -51.96700 1.000 34.62388 ?  270 LEU B N   1 
ATOM   4796 C  CA  . LEU B 1 290 ? -22.53100 14.35800  -50.56400 1.000 35.34687 ?  270 LEU B CA  1 
ATOM   4797 C  C   . LEU B 1 290 ? -21.45500 13.36400  -50.10800 1.000 30.99938 ?  270 LEU B C   1 
ATOM   4798 O  O   . LEU B 1 290 ? -20.62600 13.73700  -49.28100 1.000 31.58721 ?  270 LEU B O   1 
ATOM   4799 C  CB  . LEU B 1 290 ? -23.78900 14.29900  -49.69400 1.000 37.82748 ?  270 LEU B CB  1 
ATOM   4800 C  CG  . LEU B 1 290 ? -24.80400 15.41800  -49.90500 1.000 39.39110 ?  270 LEU B CG  1 
ATOM   4801 C  CD1 . LEU B 1 290 ? -26.14500 15.03700  -49.30000 1.000 33.56460 ?  270 LEU B CD1 1 
ATOM   4802 C  CD2 . LEU B 1 290 ? -24.30100 16.72100  -49.31000 1.000 40.08344 ?  270 LEU B CD2 1 
ATOM   4803 N  N   . THR B 1 291 ? -21.48700 12.16100  -50.66200 1.000 27.88209 ?  271 THR B N   1 
ATOM   4804 C  CA  . THR B 1 291 ? -20.46300 11.14200  -50.35400 1.000 37.22159 ?  271 THR B CA  1 
ATOM   4805 C  C   . THR B 1 291 ? -19.12000 11.65000  -50.89900 1.000 39.06203 ?  271 THR B C   1 
ATOM   4806 O  O   . THR B 1 291 ? -18.22500 11.92900  -50.10400 1.000 32.59158 ?  271 THR B O   1 
ATOM   4807 C  CB  . THR B 1 291 ? -20.89600 9.78400   -50.91900 1.000 33.12076 ?  271 THR B CB  1 
ATOM   4808 O  OG1 . THR B 1 291 ? -22.16900 9.45600   -50.36600 1.000 33.60030 ?  271 THR B OG1 1 
ATOM   4809 C  CG2 . THR B 1 291 ? -19.91600 8.67400   -50.62000 1.000 34.20529 ?  271 THR B CG2 1 
ATOM   4810 N  N   . ARG B 1 292 ? -19.02900 11.82500  -52.21200 1.000 35.13927 ?  272 ARG B N   1 
ATOM   4811 C  CA  . ARG B 1 292 ? -17.78900 12.29900  -52.82000 1.000 38.81120 ?  272 ARG B CA  1 
ATOM   4812 C  C   . ARG B 1 292 ? -17.26400 13.55200  -52.12200 1.000 38.64997 ?  272 ARG B C   1 
ATOM   4813 O  O   . ARG B 1 292 ? -16.05400 13.70000  -51.92000 1.000 36.37385 ?  272 ARG B O   1 
ATOM   4814 C  CB  . ARG B 1 292 ? -18.01900 12.57300  -54.30700 1.000 40.48391 ?  272 ARG B CB  1 
ATOM   4815 C  CG  . ARG B 1 292 ? -16.85500 13.24800  -55.02100 1.000 46.85772 ?  272 ARG B CG  1 
ATOM   4816 C  CD  . ARG B 1 292 ? -17.33100 13.94300  -56.29300 1.000 39.33072 ?  272 ARG B CD  1 
ATOM   4817 N  NE  . ARG B 1 292 ? -17.87700 15.26200  -55.99600 1.000 33.73029 ?  272 ARG B NE  1 
ATOM   4818 C  CZ  . ARG B 1 292 ? -17.15700 16.31200  -55.62000 1.000 42.26511 ?  272 ARG B CZ  1 
ATOM   4819 N  NH1 . ARG B 1 292 ? -15.83300 16.26700  -55.57700 1.000 43.66672 ?  272 ARG B NH1 1 
ATOM   4820 N  NH2 . ARG B 1 292 ? -17.78000 17.44000  -55.29100 1.000 44.35879 ?  272 ARG B NH2 1 
ATOM   4821 N  N   . PHE B 1 293 ? -18.16600 14.44500  -51.70700 1.000 37.27326 ?  273 PHE B N   1 
ATOM   4822 C  CA  . PHE B 1 293 ? -17.74400 15.73800  -51.18000 1.000 35.12111 ?  273 PHE B CA  1 
ATOM   4823 C  C   . PHE B 1 293 ? -17.09600 15.60800  -49.80300 1.000 43.25410 ?  273 PHE B C   1 
ATOM   4824 O  O   . PHE B 1 293 ? -16.09300 16.27900  -49.52400 1.000 38.22366 ?  273 PHE B O   1 
ATOM   4825 C  CB  . PHE B 1 293 ? -18.93900 16.69400  -51.13500 1.000 37.10752 ?  273 PHE B CB  1 
ATOM   4826 C  CG  . PHE B 1 293 ? -18.57400 18.12200  -50.81500 1.000 38.90786 ?  273 PHE B CG  1 
ATOM   4827 C  CD1 . PHE B 1 293 ? -17.96500 18.93200  -51.76300 1.000 43.26143 ?  273 PHE B CD1 1 
ATOM   4828 C  CD2 . PHE B 1 293 ? -18.86400 18.66400  -49.57000 1.000 41.71415 ?  273 PHE B CD2 1 
ATOM   4829 C  CE1 . PHE B 1 293 ? -17.63100 20.24900  -51.46600 1.000 48.59327 ?  273 PHE B CE1 1 
ATOM   4830 C  CE2 . PHE B 1 293 ? -18.53500 19.97800  -49.26900 1.000 45.40888 ?  273 PHE B CE2 1 
ATOM   4831 C  CZ  . PHE B 1 293 ? -17.91800 20.77100  -50.21800 1.000 44.02365 ?  273 PHE B CZ  1 
ATOM   4832 N  N   . ASP B 1 294 ? -17.63400 14.75200  -48.92700 1.000 33.84013 ?  274 ASP B N   1 
ATOM   4833 C  CA  . ASP B 1 294 ? -17.12300 14.69500  -47.55600 1.000 35.42121 ?  274 ASP B CA  1 
ATOM   4834 C  C   . ASP B 1 294 ? -17.36500 13.35900  -46.84800 1.000 30.10285 ?  274 ASP B C   1 
ATOM   4835 O  O   . ASP B 1 294 ? -17.44600 13.30400  -45.61600 1.000 38.49561 ?  274 ASP B O   1 
ATOM   4836 C  CB  . ASP B 1 294 ? -17.65100 15.85800  -46.70700 1.000 29.42859 ?  274 ASP B CB  1 
ATOM   4837 C  CG  . ASP B 1 294 ? -16.62500 16.35600  -45.69900 1.000 44.11784 ?  274 ASP B CG  1 
ATOM   4838 O  OD1 . ASP B 1 294 ? -15.50500 15.80200  -45.68600 1.000 41.26771 -1 274 ASP B OD1 1 
ATOM   4839 O  OD2 . ASP B 1 294 ? -16.92500 17.29100  -44.93000 1.000 40.38814 -1 274 ASP B OD2 1 
ATOM   4840 N  N   . GLN B 1 295 ? -17.46800 12.26600  -47.60900 1.000 30.91691 ?  275 GLN B N   1 
ATOM   4841 C  CA  . GLN B 1 295 ? -17.40200 10.94500  -47.00000 1.000 30.57662 ?  275 GLN B CA  1 
ATOM   4842 C  C   . GLN B 1 295 ? -16.19900 10.82600  -46.06400 1.000 34.46453 ?  275 GLN B C   1 
ATOM   4843 O  O   . GLN B 1 295 ? -15.20600 11.53300  -46.23100 1.000 27.35802 ?  275 GLN B O   1 
ATOM   4844 C  CB  . GLN B 1 295 ? -17.38900 9.83800   -48.05600 1.000 31.11359 ?  275 GLN B CB  1 
ATOM   4845 C  CG  . GLN B 1 295 ? -16.11700 9.78800   -48.86600 1.000 39.39133 ?  275 GLN B CG  1 
ATOM   4846 C  CD  . GLN B 1 295 ? -15.16000 8.73200   -48.36200 1.000 39.70860 ?  275 GLN B CD  1 
ATOM   4847 O  OE1 . GLN B 1 295 ? -15.50000 7.93900   -47.48000 1.000 33.15748 ?  275 GLN B OE1 1 
ATOM   4848 N  NE2 . GLN B 1 295 ? -13.95300 8.71700   -48.91300 1.000 38.14832 ?  275 GLN B NE2 1 
ATOM   4849 N  N   . PRO B 1 296 ? -16.26700 9.93800   -45.05600 1.000 34.36772 ?  276 PRO B N   1 
ATOM   4850 C  CA  . PRO B 1 296 ? -15.27400 9.97700   -43.96900 1.000 35.11080 ?  276 PRO B CA  1 
ATOM   4851 C  C   . PRO B 1 296 ? -13.91500 9.37500   -44.30100 1.000 33.70517 ?  276 PRO B C   1 
ATOM   4852 O  O   . PRO B 1 296 ? -12.89600 9.83000   -43.76700 1.000 33.82994 ?  276 PRO B O   1 
ATOM   4853 C  CB  . PRO B 1 296 ? -15.95900 9.17400   -42.85000 1.000 31.83179 ?  276 PRO B CB  1 
ATOM   4854 C  CG  . PRO B 1 296 ? -17.38700 9.00100   -43.30200 1.000 37.02175 ?  276 PRO B CG  1 
ATOM   4855 C  CD  . PRO B 1 296 ? -17.28900 8.92100   -44.78200 1.000 33.84346 ?  276 PRO B CD  1 
ATOM   4856 N  N   . LEU B 1 297 ? -13.87500 8.35100   -45.15000 1.000 31.44276 ?  277 LEU B N   1 
ATOM   4857 C  CA  . LEU B 1 297 ? -12.65800 7.56100   -45.32900 1.000 32.67294 ?  277 LEU B CA  1 
ATOM   4858 C  C   . LEU B 1 297 ? -11.62900 8.33600   -46.14500 1.000 31.06715 ?  277 LEU B C   1 
ATOM   4859 O  O   . LEU B 1 297 ? -11.77000 8.47800   -47.36500 1.000 34.12967 ?  277 LEU B O   1 
ATOM   4860 C  CB  . LEU B 1 297 ? -12.99000 6.23200   -45.99700 1.000 24.34580 ?  277 LEU B CB  1 
ATOM   4861 C  CG  . LEU B 1 297 ? -12.17200 5.04600   -45.49100 1.000 38.36888 ?  277 LEU B CG  1 
ATOM   4862 C  CD1 . LEU B 1 297 ? -12.38000 4.83700   -43.99500 1.000 39.64213 ?  277 LEU B CD1 1 
ATOM   4863 C  CD2 . LEU B 1 297 ? -12.53500 3.79400   -46.25900 1.000 33.20310 ?  277 LEU B CD2 1 
ATOM   4864 N  N   . GLN B 1 298 ? -10.57600 8.81500   -45.47600 1.000 31.19071 ?  278 GLN B N   1 
ATOM   4865 C  CA  . GLN B 1 298 ? -9.55300  9.60100   -46.15700 1.000 28.21662 ?  278 GLN B CA  1 
ATOM   4866 C  C   . GLN B 1 298 ? -8.53800  8.71300   -46.86400 1.000 31.38371 ?  278 GLN B C   1 
ATOM   4867 O  O   . GLN B 1 298 ? -8.04500  9.06800   -47.94000 1.000 32.50079 ?  278 GLN B O   1 
ATOM   4868 C  CB  . GLN B 1 298 ? -8.84500  10.52300  -45.16200 1.000 34.38357 ?  278 GLN B CB  1 
ATOM   4869 C  CG  . GLN B 1 298 ? -9.77900  11.39700  -44.34400 1.000 35.34017 ?  278 GLN B CG  1 
ATOM   4870 C  CD  . GLN B 1 298 ? -10.60000 12.34100  -45.20800 1.000 42.50583 ?  278 GLN B CD  1 
ATOM   4871 O  OE1 . GLN B 1 298 ? -10.06000 13.24800  -45.84200 1.000 38.36931 ?  278 GLN B OE1 1 
ATOM   4872 N  NE2 . GLN B 1 298 ? -11.91300 12.13400  -45.23200 1.000 34.39680 ?  278 GLN B NE2 1 
ATOM   4873 N  N   . TRP B 1 299 ? -8.21100  7.56400   -46.28100 1.000 28.30469 ?  279 TRP B N   1 
ATOM   4874 C  CA  . TRP B 1 299 ? -7.22100  6.66000   -46.83900 1.000 27.61607 ?  279 TRP B CA  1 
ATOM   4875 C  C   . TRP B 1 299 ? -7.79600  5.25500   -46.90800 1.000 26.04358 ?  279 TRP B C   1 
ATOM   4876 O  O   . TRP B 1 299 ? -8.59600  4.84800   -46.06200 1.000 26.57991 ?  279 TRP B O   1 
ATOM   4877 C  CB  . TRP B 1 299 ? -5.92600  6.65900   -45.99500 1.000 21.69100 ?  279 TRP B CB  1 
ATOM   4878 C  CG  . TRP B 1 299 ? -5.43900  8.04000   -45.66600 1.000 29.54634 ?  279 TRP B CG  1 
ATOM   4879 C  CD1 . TRP B 1 299 ? -5.61400  8.71300   -44.49300 1.000 29.01391 ?  279 TRP B CD1 1 
ATOM   4880 C  CD2 . TRP B 1 299 ? -4.69500  8.91600   -46.52200 1.000 27.23907 ?  279 TRP B CD2 1 
ATOM   4881 N  NE1 . TRP B 1 299 ? -5.03200  9.95300   -44.56600 1.000 35.83505 ?  279 TRP B NE1 1 
ATOM   4882 C  CE2 . TRP B 1 299 ? -4.45700  10.10200  -45.80100 1.000 33.12170 ?  279 TRP B CE2 1 
ATOM   4883 C  CE3 . TRP B 1 299 ? -4.20700  8.81200   -47.82900 1.000 28.57286 ?  279 TRP B CE3 1 
ATOM   4884 C  CZ2 . TRP B 1 299 ? -3.75200  11.17500  -46.34100 1.000 32.07435 ?  279 TRP B CZ2 1 
ATOM   4885 C  CZ3 . TRP B 1 299 ? -3.51000  9.88000   -48.36400 1.000 32.65742 ?  279 TRP B CZ3 1 
ATOM   4886 C  CH2 . TRP B 1 299 ? -3.28900  11.04500  -47.62000 1.000 28.92425 ?  279 TRP B CH2 1 
ATOM   4887 N  N   . ALA B 1 300 ? -7.38600  4.51800   -47.93400 1.000 25.46500 ?  280 ALA B N   1 
ATOM   4888 C  CA  . ALA B 1 300 ? -7.64200  3.09000   -47.96000 1.000 17.26338 ?  280 ALA B CA  1 
ATOM   4889 C  C   . ALA B 1 300 ? -6.78200  2.39000   -46.90400 1.000 23.58937 ?  280 ALA B C   1 
ATOM   4890 O  O   . ALA B 1 300 ? -5.90200  2.99300   -46.28100 1.000 20.14931 ?  280 ALA B O   1 
ATOM   4891 C  CB  . ALA B 1 300 ? -7.35700  2.52600   -49.35000 1.000 16.70804 ?  280 ALA B CB  1 
ATOM   4892 N  N   . ILE B 1 301 ? -7.02900  1.09200   -46.72800 1.000 24.67734 ?  281 ILE B N   1 
ATOM   4893 C  CA  . ILE B 1 301 ? -6.20700  0.27700   -45.79200 1.000 27.36925 ?  281 ILE B CA  1 
ATOM   4894 C  C   . ILE B 1 301 ? -4.78000  0.24800   -46.35000 1.000 22.63378 ?  281 ILE B C   1 
ATOM   4895 O  O   . ILE B 1 301 ? -4.62200  0.17000   -47.56200 1.000 22.50802 ?  281 ILE B O   1 
ATOM   4896 C  CB  . ILE B 1 301 ? -6.79300  -1.13700  -45.61700 1.000 23.20728 ?  281 ILE B CB  1 
ATOM   4897 C  CG1 . ILE B 1 301 ? -8.22100  -1.09900  -45.06700 1.000 24.80051 ?  281 ILE B CG1 1 
ATOM   4898 C  CG2 . ILE B 1 301 ? -5.88500  -2.01600  -44.77300 1.000 27.13380 ?  281 ILE B CG2 1 
ATOM   4899 C  CD1 . ILE B 1 301 ? -8.36800  -0.31400  -43.80100 1.000 27.47307 ?  281 ILE B CD1 1 
ATOM   4900 N  N   . ARG B 1 302 ? -3.80100  0.32900   -45.46700 1.000 21.41700 ?  282 ARG B N   1 
ATOM   4901 C  CA  . ARG B 1 302 ? -2.38500  0.36600   -45.90000 1.000 20.76275 ?  282 ARG B CA  1 
ATOM   4902 C  C   . ARG B 1 302 ? -2.06800  -0.78100  -46.86600 1.000 22.92798 ?  282 ARG B C   1 
ATOM   4903 O  O   . ARG B 1 302 ? -2.56000  -1.88900  -46.68400 1.000 20.94770 ?  282 ARG B O   1 
ATOM   4904 C  CB  . ARG B 1 302 ? -1.44000  0.35600   -44.69400 1.000 23.98134 ?  282 ARG B CB  1 
ATOM   4905 C  CG  . ARG B 1 302 ? -1.03100  -1.02000  -44.19800 1.000 29.32210 ?  282 ARG B CG  1 
ATOM   4906 C  CD  . ARG B 1 302 ? -1.90700  -1.54500  -43.08300 1.000 17.36183 ?  282 ARG B CD  1 
ATOM   4907 N  NE  . ARG B 1 302 ? -1.48300  -2.86700  -42.65400 1.000 21.96458 ?  282 ARG B NE  1 
ATOM   4908 C  CZ  . ARG B 1 302 ? -1.83900  -3.99200  -43.25700 1.000 22.94876 ?  282 ARG B CZ  1 
ATOM   4909 N  NH1 . ARG B 1 302 ? -2.46700  -3.94900  -44.41500 1.000 25.54822 ?  282 ARG B NH1 1 
ATOM   4910 N  NH2 . ARG B 1 302 ? -1.57700  -5.15800  -42.69800 1.000 26.49092 ?  282 ARG B NH2 1 
ATOM   4911 N  N   . ARG B 1 303 ? -1.25600  -0.45900  -47.87700 1.000 20.70843 ?  283 ARG B N   1 
ATOM   4912 C  CA  . ARG B 1 303 ? -0.85300  -1.47700  -48.87900 1.000 19.09817 ?  283 ARG B CA  1 
ATOM   4913 C  C   . ARG B 1 303 ? 0.67500   -1.56300  -48.91000 1.000 22.47665 ?  283 ARG B C   1 
ATOM   4914 O  O   . ARG B 1 303 ? 1.33200   -0.55500  -48.58500 1.000 25.25974 ?  283 ARG B O   1 
ATOM   4915 C  CB  . ARG B 1 303 ? -1.42100  -1.12800  -50.25700 1.000 25.31056 ?  283 ARG B CB  1 
ATOM   4916 C  CG  . ARG B 1 303 ? -2.72300  -1.84600  -50.58300 1.000 30.80923 ?  283 ARG B CG  1 
ATOM   4917 C  CD  . ARG B 1 303 ? -3.73000  -0.92100  -51.23500 1.000 33.30382 ?  283 ARG B CD  1 
ATOM   4918 N  NE  . ARG B 1 303 ? -4.89300  -1.62300  -51.76000 1.000 29.17747 ?  283 ARG B NE  1 
ATOM   4919 C  CZ  . ARG B 1 303 ? -6.12900  -1.47700  -51.29900 1.000 38.72846 ?  283 ARG B CZ  1 
ATOM   4920 N  NH1 . ARG B 1 303 ? -6.33500  -0.86900  -50.14400 1.000 36.30271 ?  283 ARG B NH1 1 
ATOM   4921 N  NH2 . ARG B 1 303 ? -7.15500  -1.93800  -51.99400 1.000 30.86873 ?  283 ARG B NH2 1 
ATOM   4922 N  N   . PHE B 1 304 ? 1.21000   -2.72500  -49.28000 1.000 19.60924 ?  284 PHE B N   1 
ATOM   4923 C  CA  . PHE B 1 304 ? 2.66900   -2.94900  -49.33100 1.000 27.02194 ?  284 PHE B CA  1 
ATOM   4924 C  C   . PHE B 1 304 ? 3.04900   -3.45000  -50.72000 1.000 27.87278 ?  284 PHE B C   1 
ATOM   4925 O  O   . PHE B 1 304 ? 2.58900   -4.51500  -51.12700 1.000 28.75319 ?  284 PHE B O   1 
ATOM   4926 C  CB  . PHE B 1 304 ? 3.06400   -3.99300  -48.29100 1.000 25.47762 ?  284 PHE B CB  1 
ATOM   4927 C  CG  . PHE B 1 304 ? 2.54200   -3.69300  -46.91300 1.000 29.70132 ?  284 PHE B CG  1 
ATOM   4928 C  CD1 . PHE B 1 304 ? 2.96100   -2.56200  -46.23300 1.000 26.34876 ?  284 PHE B CD1 1 
ATOM   4929 C  CD2 . PHE B 1 304 ? 1.61400   -4.52400  -46.31200 1.000 27.35870 ?  284 PHE B CD2 1 
ATOM   4930 C  CE1 . PHE B 1 304 ? 2.47100   -2.27700  -44.97000 1.000 25.56875 ?  284 PHE B CE1 1 
ATOM   4931 C  CE2 . PHE B 1 304 ? 1.13000   -4.23900  -45.04800 1.000 23.11309 ?  284 PHE B CE2 1 
ATOM   4932 C  CZ  . PHE B 1 304 ? 1.56300   -3.12200  -44.38100 1.000 27.56442 ?  284 PHE B CZ  1 
ATOM   4933 N  N   . PRO B 1 305 ? 3.88200   -2.70600  -51.47300 1.000 27.59258 ?  285 PRO B N   1 
ATOM   4934 C  CA  . PRO B 1 305 ? 4.31900   -3.20800  -52.75000 1.000 26.04975 ?  285 PRO B CA  1 
ATOM   4935 C  C   . PRO B 1 305 ? 5.01200   -4.55800  -52.55400 1.000 28.15461 ?  285 PRO B C   1 
ATOM   4936 O  O   . PRO B 1 305 ? 5.85800   -4.65200  -51.70100 1.000 28.86688 ?  285 PRO B O   1 
ATOM   4937 C  CB  . PRO B 1 305 ? 5.27700   -2.12500  -53.26200 1.000 29.27825 ?  285 PRO B CB  1 
ATOM   4938 C  CG  . PRO B 1 305 ? 4.90200   -0.88600  -52.49000 1.000 28.65491 ?  285 PRO B CG  1 
ATOM   4939 C  CD  . PRO B 1 305 ? 4.40400   -1.38900  -51.15300 1.000 22.57241 ?  285 PRO B CD  1 
ATOM   4940 N  N   . THR B 1 306 ? 4.59300   -5.56800  -53.30600 1.000 26.99612 ?  286 THR B N   1 
ATOM   4941 C  CA  . THR B 1 306 ? 5.27100   -6.85700  -53.29700 1.000 24.98400 ?  286 THR B CA  1 
ATOM   4942 C  C   . THR B 1 306 ? 6.57100   -6.82500  -54.08500 1.000 31.23311 ?  286 THR B C   1 
ATOM   4943 O  O   . THR B 1 306 ? 7.34900   -7.78300  -54.02100 1.000 27.21897 ?  286 THR B O   1 
ATOM   4944 C  CB  . THR B 1 306 ? 4.36300   -7.93500  -53.88100 1.000 25.93166 ?  286 THR B CB  1 
ATOM   4945 O  OG1 . THR B 1 306 ? 3.92000   -7.52500  -55.18100 1.000 34.47168 ?  286 THR B OG1 1 
ATOM   4946 C  CG2 . THR B 1 306 ? 3.15100   -8.13500  -52.98400 1.000 29.46484 ?  286 THR B CG2 1 
ATOM   4947 N  N   . ARG B 1 307 ? 6.80100   -5.74800  -54.82600 1.000 29.62503 ?  287 ARG B N   1 
ATOM   4948 C  CA  . ARG B 1 307 ? 7.98500   -5.56100  -55.64500 1.000 36.76405 ?  287 ARG B CA  1 
ATOM   4949 C  C   . ARG B 1 307 ? 8.16800   -4.06300  -55.80700 1.000 38.38462 ?  287 ARG B C   1 
ATOM   4950 O  O   . ARG B 1 307 ? 7.24900   -3.28100  -55.54300 1.000 33.99084 ?  287 ARG B O   1 
ATOM   4951 C  CB  . ARG B 1 307 ? 7.84300   -6.24700  -57.00900 1.000 34.07759 ?  287 ARG B CB  1 
ATOM   4952 C  CG  . ARG B 1 307 ? 6.77800   -5.62500  -57.90600 1.000 36.79411 ?  287 ARG B CG  1 
ATOM   4953 N  N   . GLU B 1 308 ? 9.37000   -3.66600  -56.21700 1.000 30.74627 ?  288 GLU B N   1 
ATOM   4954 C  CA  . GLU B 1 308 ? 9.58100   -2.28200  -56.61200 1.000 28.87416 ?  288 GLU B CA  1 
ATOM   4955 C  C   . GLU B 1 308 ? 8.55600   -1.91000  -57.67200 1.000 34.48236 ?  288 GLU B C   1 
ATOM   4956 O  O   . GLU B 1 308 ? 8.34900   -2.64900  -58.63700 1.000 41.42213 ?  288 GLU B O   1 
ATOM   4957 C  CB  . GLU B 1 308 ? 11.00500  -2.08700  -57.14100 1.000 34.88023 ?  288 GLU B CB  1 
ATOM   4958 N  N   . LEU B 1 309 ? 7.88100   -0.78400  -57.47000 1.000 31.76724 ?  289 LEU B N   1 
ATOM   4959 C  CA  . LEU B 1 309 ? 6.78100   -0.41000  -58.34300 1.000 33.79566 ?  289 LEU B CA  1 
ATOM   4960 C  C   . LEU B 1 309 ? 6.79400   1.09000   -58.58400 1.000 35.37482 ?  289 LEU B C   1 
ATOM   4961 O  O   . LEU B 1 309 ? 7.23300   1.87200   -57.73700 1.000 39.84501 ?  289 LEU B O   1 
ATOM   4962 C  CB  . LEU B 1 309 ? 5.42500   -0.84400  -57.75700 1.000 37.10960 ?  289 LEU B CB  1 
ATOM   4963 C  CG  . LEU B 1 309 ? 5.00100   -0.21100  -56.43100 1.000 40.90554 ?  289 LEU B CG  1 
ATOM   4964 N  N   . ASP B 1 310 ? 6.28400   1.46200   -59.74800 1.000 39.37267 ?  290 ASP B N   1 
ATOM   4965 C  CA  . ASP B 1 310 ? 6.22400   2.88500   -60.12100 1.000 43.56438 ?  290 ASP B CA  1 
ATOM   4966 C  C   . ASP B 1 310 ? 4.81400   3.41000   -59.88900 1.000 46.75647 ?  290 ASP B C   1 
ATOM   4967 O  O   . ASP B 1 310 ? 3.87900   2.86200   -60.47600 1.000 50.78958 ?  290 ASP B O   1 
ATOM   4968 C  CB  . ASP B 1 310 ? 6.61400   3.07200   -61.58700 1.000 47.12578 ?  290 ASP B CB  1 
ATOM   4969 N  N   . ILE B 1 311 ? 4.69500   4.43900   -59.06700 1.000 49.99271 ?  291 ILE B N   1 
ATOM   4970 C  CA  . ILE B 1 311 ? 3.38500   5.09500   -58.84400 1.000 51.53681 ?  291 ILE B CA  1 
ATOM   4971 C  C   . ILE B 1 311 ? 3.52800   6.55200   -59.29300 1.000 54.10846 ?  291 ILE B C   1 
ATOM   4972 O  O   . ILE B 1 311 ? 4.44000   7.23400   -58.80600 1.000 54.84751 ?  291 ILE B O   1 
ATOM   4973 C  CB  . ILE B 1 311 ? 2.97500   4.97600   -57.36800 1.000 47.77462 ?  291 ILE B CB  1 
ATOM   4974 C  CG1 . ILE B 1 311 ? 2.90900   3.51300   -56.92200 1.000 44.84491 ?  291 ILE B CG1 1 
ATOM   4975 C  CG2 . ILE B 1 311 ? 1.66400   5.70500   -57.12200 1.000 49.22106 ?  291 ILE B CG2 1 
ATOM   4976 C  CD1 . ILE B 1 311 ? 2.48300   3.32500   -55.48600 1.000 50.49519 ?  291 ILE B CD1 1 
ATOM   4977 N  N   . ALA B 1 312 ? 2.64900   6.99200   -60.18700 1.000 56.85260 ?  292 ALA B N   1 
ATOM   4978 C  CA  . ALA B 1 312 ? 2.69600   8.38900   -60.66400 1.000 57.97913 ?  292 ALA B CA  1 
ATOM   4979 C  C   . ALA B 1 312 ? 4.12700   8.71400   -61.10100 1.000 57.15405 ?  292 ALA B C   1 
ATOM   4980 O  O   . ALA B 1 312 ? 4.53700   9.87200   -60.93000 1.000 56.89571 ?  292 ALA B O   1 
ATOM   4981 N  N   . GLY B 1 313 ? 4.85700   7.71900   -61.60700 1.000 54.43583 ?  293 GLY B N   1 
ATOM   4982 C  CA  . GLY B 1 313 ? 6.21700   7.94900   -62.11900 1.000 47.41469 ?  293 GLY B CA  1 
ATOM   4983 C  C   . GLY B 1 313 ? 7.28800   8.01000   -61.05000 1.000 54.63617 ?  293 GLY B C   1 
ATOM   4984 O  O   . GLY B 1 313 ? 8.33400   8.61000   -61.32000 1.000 52.91868 ?  293 GLY B O   1 
ATOM   4985 N  N   . VAL B 1 314 ? 7.06900   7.39500   -59.89300 1.000 52.65816 ?  294 VAL B N   1 
ATOM   4986 C  CA  . VAL B 1 314 ? 8.15500   7.34800   -58.87100 1.000 45.04748 ?  294 VAL B CA  1 
ATOM   4987 C  C   . VAL B 1 314 ? 8.29400   5.91500   -58.35500 1.000 44.88170 ?  294 VAL B C   1 
ATOM   4988 O  O   . VAL B 1 314 ? 7.27200   5.32000   -58.01500 1.000 52.19905 ?  294 VAL B O   1 
ATOM   4989 C  CB  . VAL B 1 314 ? 7.92400   8.36100   -57.73700 1.000 51.43582 ?  294 VAL B CB  1 
ATOM   4990 N  N   . GLU B 1 315 ? 9.51600   5.38900   -58.31900 1.000 45.86942 ?  295 GLU B N   1 
ATOM   4991 C  CA  . GLU B 1 315 ? 9.72900   4.00300   -57.92200 1.000 38.14755 ?  295 GLU B CA  1 
ATOM   4992 C  C   . GLU B 1 315 ? 9.59500   3.86100   -56.40900 1.000 45.17321 ?  295 GLU B C   1 
ATOM   4993 O  O   . GLU B 1 315 ? 10.35200  4.47500   -55.64900 1.000 43.71977 ?  295 GLU B O   1 
ATOM   4994 C  CB  . GLU B 1 315 ? 11.10300  3.52600   -58.38700 1.000 44.87798 ?  295 GLU B CB  1 
ATOM   4995 N  N   . VAL B 1 316 ? 8.64200   3.05000   -55.97500 1.000 39.93942 ?  296 VAL B N   1 
ATOM   4996 C  CA  . VAL B 1 316 ? 8.39400   2.79600   -54.55700 1.000 36.92809 ?  296 VAL B CA  1 
ATOM   4997 C  C   . VAL B 1 316 ? 9.02100   1.45400   -54.19600 1.000 28.34237 ?  296 VAL B C   1 
ATOM   4998 O  O   . VAL B 1 316 ? 8.79200   0.46900   -54.91000 1.000 31.79315 ?  296 VAL B O   1 
ATOM   4999 C  CB  . VAL B 1 316 ? 6.88700   2.79600   -54.23800 1.000 36.73551 ?  296 VAL B CB  1 
ATOM   5000 C  CG1 . VAL B 1 316 ? 6.65700   2.48000   -52.76800 1.000 37.34652 ?  296 VAL B CG1 1 
ATOM   5001 C  CG2 . VAL B 1 316 ? 6.26200   4.13000   -54.61500 1.000 40.16709 ?  296 VAL B CG2 1 
ATOM   5002 N  N   . PRO B 1 317 ? 9.80200   1.36900   -53.12200 1.000 31.17714 ?  297 PRO B N   1 
ATOM   5003 C  CA  . PRO B 1 317 ? 10.43400  0.09500   -52.76900 1.000 33.19375 ?  297 PRO B CA  1 
ATOM   5004 C  C   . PRO B 1 317 ? 9.41600   -0.93800  -52.30900 1.000 35.39470 ?  297 PRO B C   1 
ATOM   5005 O  O   . PRO B 1 317 ? 8.29400   -0.62200  -51.90700 1.000 30.20396 ?  297 PRO B O   1 
ATOM   5006 C  CB  . PRO B 1 317 ? 11.38400  0.47600   -51.62600 1.000 35.16945 ?  297 PRO B CB  1 
ATOM   5007 C  CG  . PRO B 1 317 ? 11.59700  1.95100   -51.78500 1.000 38.17409 ?  297 PRO B CG  1 
ATOM   5008 C  CD  . PRO B 1 317 ? 10.27500  2.46800   -52.26500 1.000 34.00524 ?  297 PRO B CD  1 
ATOM   5009 N  N   . ALA B 1 318 ? 9.83500   -2.19900  -52.36700 1.000 32.19036 ?  298 ALA B N   1 
ATOM   5010 C  CA  . ALA B 1 318 ? 8.99800   -3.28600  -51.87900 1.000 35.53568 ?  298 ALA B CA  1 
ATOM   5011 C  C   . ALA B 1 318 ? 8.91500   -3.24600  -50.35700 1.000 36.11992 ?  298 ALA B C   1 
ATOM   5012 O  O   . ALA B 1 318 ? 9.93100   -3.09700  -49.67100 1.000 30.49054 ?  298 ALA B O   1 
ATOM   5013 C  CB  . ALA B 1 318 ? 9.55100   -4.63100  -52.34600 1.000 35.65695 ?  298 ALA B CB  1 
ATOM   5014 N  N   . GLY B 1 319 ? 7.69700   -3.37500  -49.82900 1.000 29.93413 ?  299 GLY B N   1 
ATOM   5015 C  CA  . GLY B 1 319 ? 7.48200   -3.41400  -48.40000 1.000 25.81253 ?  299 GLY B CA  1 
ATOM   5016 C  C   . GLY B 1 319 ? 7.21200   -2.07500  -47.75200 1.000 26.07711 ?  299 GLY B C   1 
ATOM   5017 O  O   . GLY B 1 319 ? 6.84700   -2.04300  -46.57100 1.000 26.57459 ?  299 GLY B O   1 
ATOM   5018 N  N   . ASP B 1 320 ? 7.39100   -0.97200  -48.47500 1.000 23.39184 ?  300 ASP B N   1 
ATOM   5019 C  CA  . ASP B 1 320 ? 7.07400   0.33900   -47.93200 1.000 29.75932 ?  300 ASP B CA  1 
ATOM   5020 C  C   . ASP B 1 320 ? 5.56300   0.48000   -47.76300 1.000 24.21112 ?  300 ASP B C   1 
ATOM   5021 O  O   . ASP B 1 320 ? 4.77700   -0.19900  -48.42200 1.000 22.56493 ?  300 ASP B O   1 
ATOM   5022 C  CB  . ASP B 1 320 ? 7.61200   1.43900   -48.85000 1.000 25.58829 ?  300 ASP B CB  1 
ATOM   5023 C  CG  . ASP B 1 320 ? 9.08100   1.74100   -48.60300 1.000 32.54400 ?  300 ASP B CG  1 
ATOM   5024 O  OD1 . ASP B 1 320 ? 9.80100   0.85100   -48.10800 1.000 27.69790 ?  300 ASP B OD1 1 
ATOM   5025 O  OD2 . ASP B 1 320 ? 9.51800   2.86400   -48.92600 1.000 36.12991 -1 300 ASP B OD2 1 
ATOM   5026 N  N   . THR B 1 321 ? 5.15500   1.37100   -46.86500 1.000 29.58374 ?  301 THR B N   1 
ATOM   5027 C  CA  . THR B 1 321 ? 3.73100   1.57500   -46.61800 1.000 22.91546 ?  301 THR B CA  1 
ATOM   5028 C  C   . THR B 1 321 ? 3.17400   2.56200   -47.63800 1.000 30.61367 ?  301 THR B C   1 
ATOM   5029 O  O   . THR B 1 321 ? 3.67700   3.68400   -47.76100 1.000 26.49587 ?  301 THR B O   1 
ATOM   5030 C  CB  . THR B 1 321 ? 3.49000   2.07200   -45.19600 1.000 26.11317 ?  301 THR B CB  1 
ATOM   5031 O  OG1 . THR B 1 321 ? 4.01300   1.12100   -44.26200 1.000 27.78943 ?  301 THR B OG1 1 
ATOM   5032 C  CG2 . THR B 1 321 ? 1.99400   2.24800   -44.94700 1.000 24.39110 ?  301 THR B CG2 1 
ATOM   5033 N  N   . VAL B 1 322 ? 2.13700   2.14400   -48.36400 1.000 25.88322 ?  302 VAL B N   1 
ATOM   5034 C  CA  . VAL B 1 322 ? 1.50400   2.94800   -49.40700 1.000 24.88049 ?  302 VAL B CA  1 
ATOM   5035 C  C   . VAL B 1 322 ? 0.07800   3.26800   -48.97600 1.000 30.79088 ?  302 VAL B C   1 
ATOM   5036 O  O   . VAL B 1 322 ? -0.71700  2.35800   -48.70500 1.000 24.74822 ?  302 VAL B O   1 
ATOM   5037 C  CB  . VAL B 1 322 ? 1.51100   2.22700   -50.76200 1.000 26.04574 ?  302 VAL B CB  1 
ATOM   5038 C  CG1 . VAL B 1 322 ? 0.82700   3.08700   -51.81100 1.000 27.10929 ?  302 VAL B CG1 1 
ATOM   5039 C  CG2 . VAL B 1 322 ? 2.93500   1.91600   -51.18300 1.000 32.38223 ?  302 VAL B CG2 1 
ATOM   5040 N  N   . LEU B 1 323 ? -0.25100  4.56000   -48.93800 1.000 26.32146 ?  303 LEU B N   1 
ATOM   5041 C  CA  . LEU B 1 323 ? -1.54800  5.04100   -48.47400 1.000 28.65545 ?  303 LEU B CA  1 
ATOM   5042 C  C   . LEU B 1 323 ? -2.26400  5.70100   -49.64600 1.000 29.77861 ?  303 LEU B C   1 
ATOM   5043 O  O   . LEU B 1 323 ? -1.83800  6.75800   -50.12400 1.000 28.07155 ?  303 LEU B O   1 
ATOM   5044 C  CB  . LEU B 1 323 ? -1.37700  6.01100   -47.30800 1.000 27.24448 ?  303 LEU B CB  1 
ATOM   5045 C  CG  . LEU B 1 323 ? -0.79500  5.38300   -46.04000 1.000 26.71657 ?  303 LEU B CG  1 
ATOM   5046 C  CD1 . LEU B 1 323 ? -0.89100  6.33300   -44.85400 1.000 32.12569 ?  303 LEU B CD1 1 
ATOM   5047 C  CD2 . LEU B 1 323 ? -1.47300  4.05700   -45.72700 1.000 33.82334 ?  303 LEU B CD2 1 
ATOM   5048 N  N   . LEU B 1 324 ? -3.34500  5.07600   -50.10400 1.000 27.51090 ?  304 LEU B N   1 
ATOM   5049 C  CA  . LEU B 1 324 ? -4.11500  5.56700   -51.24200 1.000 33.63592 ?  304 LEU B CA  1 
ATOM   5050 C  C   . LEU B 1 324 ? -5.17900  6.53800   -50.74800 1.000 34.41712 ?  304 LEU B C   1 
ATOM   5051 O  O   . LEU B 1 324 ? -6.02000  6.17400   -49.91500 1.000 31.98121 ?  304 LEU B O   1 
ATOM   5052 C  CB  . LEU B 1 324 ? -4.76100  4.40600   -51.99500 1.000 27.88664 ?  304 LEU B CB  1 
ATOM   5053 C  CG  . LEU B 1 324 ? -3.82400  3.28200   -52.44300 1.000 29.41477 ?  304 LEU B CG  1 
ATOM   5054 C  CD1 . LEU B 1 324 ? -4.61600  2.12200   -53.03000 1.000 29.55649 ?  304 LEU B CD1 1 
ATOM   5055 C  CD2 . LEU B 1 324 ? -2.78300  3.79300   -53.43800 1.000 32.70933 ?  304 LEU B CD2 1 
ATOM   5056 N  N   . GLY B 1 325 ? -5.15100  7.76400   -51.26700 1.000 28.51425 ?  305 GLY B N   1 
ATOM   5057 C  CA  . GLY B 1 325 ? -6.04900  8.80600   -50.80800 1.000 29.59052 ?  305 GLY B CA  1 
ATOM   5058 C  C   . GLY B 1 325 ? -7.39500  8.82700   -51.50500 1.000 35.37030 ?  305 GLY B C   1 
ATOM   5059 O  O   . GLY B 1 325 ? -7.56500  9.51200   -52.51900 1.000 33.47174 ?  305 GLY B O   1 
ATOM   5060 N  N   . ILE B 1 326 ? -8.36500  8.08600   -50.96100 1.000 38.97110 ?  306 ILE B N   1 
ATOM   5061 C  CA  . ILE B 1 326 ? -9.69900  8.05100   -51.55900 1.000 32.73656 ?  306 ILE B CA  1 
ATOM   5062 C  C   . ILE B 1 326 ? -10.33300 9.43600   -51.52900 1.000 29.60436 ?  306 ILE B C   1 
ATOM   5063 O  O   . ILE B 1 326 ? -10.92400 9.89300   -52.51500 1.000 37.27826 ?  306 ILE B O   1 
ATOM   5064 C  CB  . ILE B 1 326 ? -10.58300 7.01600   -50.83800 1.000 37.84816 ?  306 ILE B CB  1 
ATOM   5065 C  CG1 . ILE B 1 326 ? -9.98900  5.61500   -50.97700 1.000 33.29485 ?  306 ILE B CG1 1 
ATOM   5066 C  CG2 . ILE B 1 326 ? -12.00500 7.05400   -51.38300 1.000 34.30171 ?  306 ILE B CG2 1 
ATOM   5067 C  CD1 . ILE B 1 326 ? -10.68400 4.57700   -50.11900 1.000 36.26683 ?  306 ILE B CD1 1 
ATOM   5068 N  N   . ALA B 1 327 ? -10.21800 10.12500  -50.39300 1.000 28.48496 ?  307 ALA B N   1 
ATOM   5069 C  CA  . ALA B 1 327 ? -10.84300 11.43600  -50.24800 1.000 34.69948 ?  307 ALA B CA  1 
ATOM   5070 C  C   . ALA B 1 327 ? -10.21200 12.45800  -51.18800 1.000 41.85105 ?  307 ALA B C   1 
ATOM   5071 O  O   . ALA B 1 327 ? -10.92000 13.20500  -51.87400 1.000 40.60844 ?  307 ALA B O   1 
ATOM   5072 C  CB  . ALA B 1 327 ? -10.74600 11.90600  -48.79700 1.000 37.48835 ?  307 ALA B CB  1 
ATOM   5073 N  N   . SER B 1 328 ? -8.87700  12.51000  -51.22900 1.000 42.11270 ?  308 SER B N   1 
ATOM   5074 C  CA  . SER B 1 328 ? -8.21100  13.42200  -52.15200 1.000 37.35846 ?  308 SER B CA  1 
ATOM   5075 C  C   . SER B 1 328 ? -8.56900  13.09000  -53.59400 1.000 33.05886 ?  308 SER B C   1 
ATOM   5076 O  O   . SER B 1 328 ? -8.81900  13.99200  -54.40300 1.000 40.56599 ?  308 SER B O   1 
ATOM   5077 C  CB  . SER B 1 328 ? -6.69500  13.36900  -51.94900 1.000 45.20907 ?  308 SER B CB  1 
ATOM   5078 O  OG  . SER B 1 328 ? -6.02200  14.14400  -52.93000 1.000 38.70584 ?  308 SER B OG  1 
ATOM   5079 N  N   . ALA B 1 329 ? -8.61200  11.79700  -53.92800 1.000 31.10004 ?  309 ALA B N   1 
ATOM   5080 C  CA  . ALA B 1 329 ? -8.99200  11.38500  -55.27600 1.000 31.08400 ?  309 ALA B CA  1 
ATOM   5081 C  C   . ALA B 1 329 ? -10.42200 11.79600  -55.59700 1.000 41.17074 ?  309 ALA B C   1 
ATOM   5082 O  O   . ALA B 1 329 ? -10.72100 12.19800  -56.72800 1.000 46.91159 ?  309 ALA B O   1 
ATOM   5083 C  CB  . ALA B 1 329 ? -8.82100  9.87600   -55.42800 1.000 32.58472 ?  309 ALA B CB  1 
ATOM   5084 N  N   . ASN B 1 330 ? -11.32200 11.70900  -54.61400 1.000 40.81565 ?  310 ASN B N   1 
ATOM   5085 C  CA  . ASN B 1 330 ? -12.69800 12.14700  -54.81400 1.000 40.45762 ?  310 ASN B CA  1 
ATOM   5086 C  C   . ASN B 1 330 ? -12.80900 13.64100  -55.08800 1.000 43.42599 ?  310 ASN B C   1 
ATOM   5087 O  O   . ASN B 1 330 ? -13.87700 14.09800  -55.50900 1.000 43.65711 ?  310 ASN B O   1 
ATOM   5088 C  CB  . ASN B 1 330 ? -13.54700 11.77600  -53.59500 1.000 39.94293 ?  310 ASN B CB  1 
ATOM   5089 C  CG  . ASN B 1 330 ? -13.98600 10.32300  -53.60700 1.000 40.90851 ?  310 ASN B CG  1 
ATOM   5090 O  OD1 . ASN B 1 330 ? -13.84100 9.62100   -54.60900 1.000 34.57095 ?  310 ASN B OD1 1 
ATOM   5091 N  ND2 . ASN B 1 330 ? -14.52300 9.86100   -52.48300 1.000 42.24045 ?  310 ASN B ND2 1 
ATOM   5092 N  N   . HIS B 1 331 ? -11.71400 14.36200  -54.87600 1.000 43.10347 ?  311 HIS B N   1 
ATOM   5093 C  CA  . HIS B 1 331 ? -11.68700 15.81900  -55.16100 1.000 45.16030 ?  311 HIS B CA  1 
ATOM   5094 C  C   . HIS B 1 331 ? -10.64200 16.09900  -56.25400 1.000 44.86595 ?  311 HIS B C   1 
ATOM   5095 O  O   . HIS B 1 331 ? -9.99500  17.15900  -56.20300 1.000 39.95262 ?  311 HIS B O   1 
ATOM   5096 C  CB  . HIS B 1 331 ? -11.45500 16.59000  -53.86300 1.000 43.69862 ?  311 HIS B CB  1 
ATOM   5097 C  CG  . HIS B 1 331 ? -12.68300 16.79500  -53.04700 1.000 49.09624 ?  311 HIS B CG  1 
ATOM   5098 N  ND1 . HIS B 1 331 ? -12.94600 17.97500  -52.38800 1.000 52.31920 ?  311 HIS B ND1 1 
ATOM   5099 C  CD2 . HIS B 1 331 ? -13.70600 15.98300  -52.77600 1.000 48.15245 ?  311 HIS B CD2 1 
ATOM   5100 C  CE1 . HIS B 1 331 ? -14.09400 17.86400  -51.73900 1.000 50.48609 ?  311 HIS B CE1 1 
ATOM   5101 N  NE2 . HIS B 1 331 ? -14.57000 16.66200  -51.96500 1.000 48.54881 ?  311 HIS B NE2 1 
ATOM   5102 N  N   . ASP B 1 332 ? -10.51300 15.18300  -57.21600 1.000 40.19642 ?  312 ASP B N   1 
ATOM   5103 C  CA  . ASP B 1 332 ? -9.51000  15.34400  -58.29700 1.000 52.87909 ?  312 ASP B CA  1 
ATOM   5104 C  C   . ASP B 1 332 ? -10.07100 16.23800  -59.40800 1.000 52.04611 ?  312 ASP B C   1 
ATOM   5105 O  O   . ASP B 1 332 ? -11.03900 15.82700  -60.05600 1.000 49.90172 ?  312 ASP B O   1 
ATOM   5106 C  CB  . ASP B 1 332 ? -9.09200  14.00800  -58.90300 1.000 48.97308 ?  312 ASP B CB  1 
ATOM   5107 N  N   . GLU B 1 333 ? -9.43000  17.38000  -59.64300 1.000 52.80854 ?  313 GLU B N   1 
ATOM   5108 C  CA  . GLU B 1 333 ? -9.89500  18.33500  -60.68800 1.000 58.00474 ?  313 GLU B CA  1 
ATOM   5109 C  C   . GLU B 1 333 ? -9.79100  17.70000  -62.08300 1.000 54.33001 ?  313 GLU B C   1 
ATOM   5110 O  O   . GLU B 1 333 ? -10.47000 18.19200  -62.98500 1.000 54.51743 ?  313 GLU B O   1 
ATOM   5111 C  CB  . GLU B 1 333 ? -9.11600  19.64200  -60.55500 1.000 48.95553 ?  313 GLU B CB  1 
ATOM   5112 C  CG  . GLU B 1 333 ? -9.01700  20.14100  -59.12800 1.000 53.64819 ?  313 GLU B CG  1 
ATOM   5113 C  CD  . GLU B 1 333 ? -7.69800  19.83200  -58.44100 1.000 52.42455 ?  313 GLU B CD  1 
ATOM   5114 O  OE1 . GLU B 1 333 ? -7.11300  18.78100  -58.74800 1.000 57.68330 ?  313 GLU B OE1 1 
ATOM   5115 N  N   . THR B 1 334 ? -9.03500  16.60900  -62.22400 1.000 57.41718 ?  314 THR B N   1 
ATOM   5116 C  CA  . THR B 1 334 ? -8.82200  15.92900  -63.52800 1.000 49.95472 ?  314 THR B CA  1 
ATOM   5117 C  C   . THR B 1 334 ? -10.00500 15.03300  -63.87900 1.000 51.60204 ?  314 THR B C   1 
ATOM   5118 O  O   . THR B 1 334 ? -10.04400 14.55200  -65.01100 1.000 48.92332 ?  314 THR B O   1 
ATOM   5119 C  CB  . THR B 1 334 ? -7.53900  15.09300  -63.48500 1.000 52.72017 ?  314 THR B CB  1 
ATOM   5120 N  N   . VAL B 1 335 ? -10.89900 14.78600  -62.91500 1.000 54.22646 ?  315 VAL B N   1 
ATOM   5121 C  CA  . VAL B 1 335 ? -12.09500 13.92100  -63.14200 1.000 55.63964 ?  315 VAL B CA  1 
ATOM   5122 C  C   . VAL B 1 335 ? -13.34500 14.67000  -62.66600 1.000 52.12527 ?  315 VAL B C   1 
ATOM   5123 O  O   . VAL B 1 335 ? -14.43900 14.36900  -63.16500 1.000 53.38940 ?  315 VAL B O   1 
ATOM   5124 C  CB  . VAL B 1 335 ? -11.93700 12.56700  -62.41000 1.000 54.04538 ?  315 VAL B CB  1 
ATOM   5125 C  CG1 . VAL B 1 335 ? -12.92200 11.51800  -62.90100 1.000 54.16958 ?  315 VAL B CG1 1 
ATOM   5126 C  CG2 . VAL B 1 335 ? -10.51600 12.03400  -62.48100 1.000 52.48360 ?  315 VAL B CG2 1 
ATOM   5127 N  N   . PHE B 1 336 ? -13.19100 15.58400  -61.71200 1.000 50.25982 ?  316 PHE B N   1 
ATOM   5128 C  CA  . PHE B 1 336 ? -14.33000 16.28900  -61.14100 1.000 52.48525 ?  316 PHE B CA  1 
ATOM   5129 C  C   . PHE B 1 336 ? -14.16800 17.77900  -61.39600 1.000 52.35425 ?  316 PHE B C   1 
ATOM   5130 O  O   . PHE B 1 336 ? -13.17200 18.37800  -60.97600 1.000 53.63146 ?  316 PHE B O   1 
ATOM   5131 C  CB  . PHE B 1 336 ? -14.44800 16.01600  -59.63900 1.000 49.34991 ?  316 PHE B CB  1 
ATOM   5132 C  CG  . PHE B 1 336 ? -14.57900 14.55900  -59.29700 1.000 53.91751 ?  316 PHE B CG  1 
ATOM   5133 C  CD1 . PHE B 1 336 ? -15.77900 13.88900  -59.48600 1.000 45.66376 ?  316 PHE B CD1 1 
ATOM   5134 C  CD2 . PHE B 1 336 ? -13.49700 13.85600  -58.78900 1.000 45.86176 ?  316 PHE B CD2 1 
ATOM   5135 C  CE1 . PHE B 1 336 ? -15.89600 12.54300  -59.17300 1.000 46.81460 ?  316 PHE B CE1 1 
ATOM   5136 C  CE2 . PHE B 1 336 ? -13.60700 12.51300  -58.47500 1.000 47.10059 ?  316 PHE B CE2 1 
ATOM   5137 C  CZ  . PHE B 1 336 ? -14.80600 11.85500  -58.66700 1.000 46.42026 ?  316 PHE B CZ  1 
ATOM   5138 N  N   . ASP B 1 337 ? -15.14200 18.37200  -62.08100 1.000 56.59312 ?  317 ASP B N   1 
ATOM   5139 C  CA  . ASP B 1 337 ? -15.15400 19.81400  -62.27400 1.000 49.98936 ?  317 ASP B CA  1 
ATOM   5140 C  C   . ASP B 1 337 ? -15.59700 20.50500  -60.99300 1.000 46.53830 ?  317 ASP B C   1 
ATOM   5141 O  O   . ASP B 1 337 ? -16.58000 20.10100  -60.36400 1.000 48.81350 ?  317 ASP B O   1 
ATOM   5142 C  CB  . ASP B 1 337 ? -16.08200 20.19700  -63.42600 1.000 49.60545 ?  317 ASP B CB  1 
ATOM   5143 N  N   . LEU B 1 338 ? -14.86600 21.55200  -60.61700 1.000 49.72268 ?  318 LEU B N   1 
ATOM   5144 C  CA  . LEU B 1 338 ? -15.08900 22.27900  -59.37200 1.000 50.94868 ?  318 LEU B CA  1 
ATOM   5145 C  C   . LEU B 1 338 ? -15.21000 21.30600  -58.19700 1.000 52.41301 ?  318 LEU B C   1 
ATOM   5146 O  O   . LEU B 1 338 ? -16.22400 21.30900  -57.48400 1.000 42.10809 ?  318 LEU B O   1 
ATOM   5147 C  CB  . LEU B 1 338 ? -16.32200 23.16600  -59.47300 1.000 47.16430 ?  318 LEU B CB  1 
ATOM   5148 C  CG  . LEU B 1 338 ? -16.29000 24.26500  -60.54200 1.000 49.35656 ?  318 LEU B CG  1 
ATOM   5149 C  CD1 . LEU B 1 338 ? -17.62800 24.98300  -60.62700 1.000 47.31806 ?  318 LEU B CD1 1 
ATOM   5150 C  CD2 . LEU B 1 338 ? -15.17500 25.26000  -60.26000 1.000 48.83871 ?  318 LEU B CD2 1 
ATOM   5151 N  N   . PRO B 1 339 ? -14.19800 20.46100  -57.96600 1.000 48.62675 ?  319 PRO B N   1 
ATOM   5152 C  CA  . PRO B 1 339 ? -14.36100 19.36500  -56.99900 1.000 47.37131 ?  319 PRO B CA  1 
ATOM   5153 C  C   . PRO B 1 339 ? -14.53700 19.83700  -55.57000 1.000 46.39985 ?  319 PRO B C   1 
ATOM   5154 O  O   . PRO B 1 339 ? -14.96000 19.04000  -54.72300 1.000 50.12081 ?  319 PRO B O   1 
ATOM   5155 C  CB  . PRO B 1 339 ? -13.06500 18.56300  -57.16600 1.000 49.40960 ?  319 PRO B CB  1 
ATOM   5156 C  CD  . PRO B 1 339 ? -12.82500 20.50400  -58.50400 1.000 48.75109 ?  319 PRO B CD  1 
ATOM   5157 N  N   . ASP B 1 340 ? -14.22600 21.09600  -55.27200 1.000 41.28095 ?  320 ASP B N   1 
ATOM   5158 C  CA  . ASP B 1 340 ? -14.43300 21.66400  -53.94800 1.000 50.14797 ?  320 ASP B CA  1 
ATOM   5159 C  C   . ASP B 1 340 ? -15.75000 22.42400  -53.83500 1.000 46.99091 ?  320 ASP B C   1 
ATOM   5160 O  O   . ASP B 1 340 ? -15.95200 23.15500  -52.85900 1.000 47.03510 ?  320 ASP B O   1 
ATOM   5161 C  CB  . ASP B 1 340 ? -13.26200 22.57800  -53.57700 1.000 49.44488 ?  320 ASP B CB  1 
ATOM   5162 C  CG  . ASP B 1 340 ? -11.92700 21.85200  -53.58300 1.000 43.53796 ?  320 ASP B CG  1 
ATOM   5163 O  OD2 . ASP B 1 340 ? -10.88200 22.53000  -53.48600 1.000 52.37006 -1 320 ASP B OD2 1 
ATOM   5164 N  N   . THR B 1 341 ? -16.65000 22.26600  -54.80400 1.000 48.20063 ?  321 THR B N   1 
ATOM   5165 C  CA  . THR B 1 341 ? -17.97200 22.87700  -54.76500 1.000 51.99084 ?  321 THR B CA  1 
ATOM   5166 C  C   . THR B 1 341 ? -19.01900 21.77200  -54.81400 1.000 50.78287 ?  321 THR B C   1 
ATOM   5167 O  O   . THR B 1 341 ? -18.93200 20.86500  -55.65000 1.000 51.38826 ?  321 THR B O   1 
ATOM   5168 C  CB  . THR B 1 341 ? -18.15900 23.86800  -55.92500 1.000 55.30531 ?  321 THR B CB  1 
ATOM   5169 O  OG1 . THR B 1 341 ? -17.18800 24.91800  -55.82000 1.000 59.75815 ?  321 THR B OG1 1 
ATOM   5170 C  CG2 . THR B 1 341 ? -19.55600 24.48700  -55.90900 1.000 53.18629 ?  321 THR B CG2 1 
ATOM   5171 N  N   . LEU B 1 342 ? -19.99900 21.84600  -53.90600 1.000 49.99039 ?  322 LEU B N   1 
ATOM   5172 C  CA  . LEU B 1 342 ? -21.05700 20.80600  -53.85100 1.000 51.08297 ?  322 LEU B CA  1 
ATOM   5173 C  C   . LEU B 1 342 ? -21.99500 20.99300  -55.04200 1.000 48.33034 ?  322 LEU B C   1 
ATOM   5174 O  O   . LEU B 1 342 ? -22.58800 22.07100  -55.15900 1.000 48.62219 ?  322 LEU B O   1 
ATOM   5175 C  CB  . LEU B 1 342 ? -21.81900 20.89800  -52.52300 1.000 48.09507 ?  322 LEU B CB  1 
ATOM   5176 C  CG  . LEU B 1 342 ? -22.73700 19.72000  -52.20000 1.000 49.52633 ?  322 LEU B CG  1 
ATOM   5177 C  CD1 . LEU B 1 342 ? -21.92700 18.46700  -51.93400 1.000 48.40147 ?  322 LEU B CD1 1 
ATOM   5178 C  CD2 . LEU B 1 342 ? -23.62900 20.03000  -51.00700 1.000 37.22824 ?  322 LEU B CD2 1 
ATOM   5179 N  N   . ASP B 1 343 ? -22.08600 19.98300  -55.89600 1.000 46.98610 ?  323 ASP B N   1 
ATOM   5180 C  CA  . ASP B 1 343 ? -23.02000 20.03800  -57.04200 1.000 45.76883 ?  323 ASP B CA  1 
ATOM   5181 C  C   . ASP B 1 343 ? -23.84800 18.76500  -56.99400 1.000 46.71315 ?  323 ASP B C   1 
ATOM   5182 O  O   . ASP B 1 343 ? -23.43100 17.78400  -57.59900 1.000 49.31165 ?  323 ASP B O   1 
ATOM   5183 C  CB  . ASP B 1 343 ? -22.25600 20.21800  -58.34900 1.000 47.01768 ?  323 ASP B CB  1 
ATOM   5184 N  N   . LEU B 1 344 ? -25.00600 18.81800  -56.33900 1.000 45.33253 ?  324 LEU B N   1 
ATOM   5185 C  CA  . LEU B 1 344 ? -25.80100 17.58300  -56.12400 1.000 47.63578 ?  324 LEU B CA  1 
ATOM   5186 C  C   . LEU B 1 344 ? -26.24400 16.96700  -57.45400 1.000 49.46826 ?  324 LEU B C   1 
ATOM   5187 O  O   . LEU B 1 344 ? -26.67600 15.80900  -57.42900 1.000 48.55343 ?  324 LEU B O   1 
ATOM   5188 C  CB  . LEU B 1 344 ? -26.99800 17.90600  -55.22000 1.000 43.23987 ?  324 LEU B CB  1 
ATOM   5189 C  CG  . LEU B 1 344 ? -26.65500 18.39500  -53.81600 1.000 45.07253 ?  324 LEU B CG  1 
ATOM   5190 C  CD1 . LEU B 1 344 ? -27.91300 18.52800  -52.97600 1.000 40.05666 ?  324 LEU B CD1 1 
ATOM   5191 C  CD2 . LEU B 1 344 ? -25.65600 17.46900  -53.14200 1.000 39.59682 ?  324 LEU B CD2 1 
ATOM   5192 N  N   . ARG B 1 345 ? -26.12500 17.70800  -58.55900 1.000 51.22171 ?  325 ARG B N   1 
ATOM   5193 C  CA  . ARG B 1 345 ? -26.62800 17.20300  -59.86600 1.000 54.11372 ?  325 ARG B CA  1 
ATOM   5194 C  C   . ARG B 1 345 ? -25.47400 16.59900  -60.67500 1.000 55.56904 ?  325 ARG B C   1 
ATOM   5195 O  O   . ARG B 1 345 ? -25.68700 16.29100  -61.85000 1.000 53.78840 ?  325 ARG B O   1 
ATOM   5196 C  CB  . ARG B 1 345 ? -27.37400 18.32300  -60.60000 1.000 57.10045 ?  325 ARG B CB  1 
ATOM   5197 C  CG  . ARG B 1 345 ? -28.35400 19.08400  -59.71900 1.000 62.84035 ?  325 ARG B CG  1 
ATOM   5198 C  CD  . ARG B 1 345 ? -29.35900 19.88900  -60.52300 1.000 61.51950 ?  325 ARG B CD  1 
ATOM   5199 N  NE  . ARG B 1 345 ? -30.73200 19.68100  -60.09200 1.000 60.41170 ?  325 ARG B NE  1 
ATOM   5200 C  CZ  . ARG B 1 345 ? -31.47200 18.63800  -60.44200 1.000 56.10107 ?  325 ARG B CZ  1 
ATOM   5201 N  NH1 . ARG B 1 345 ? -30.94100 17.67000  -61.16500 1.000 54.75704 ?  325 ARG B NH1 1 
ATOM   5202 N  NH2 . ARG B 1 345 ? -32.73500 18.56300  -60.06700 1.000 55.22885 ?  325 ARG B NH2 1 
ATOM   5203 N  N   . ARG B 1 346 ? -24.31900 16.39300  -60.02600 1.000 56.68241 ?  326 ARG B N   1 
ATOM   5204 C  CA  . ARG B 1 346 ? -23.19600 15.68000  -60.69100 1.000 54.13177 ?  326 ARG B CA  1 
ATOM   5205 C  C   . ARG B 1 346 ? -23.75200 14.31600  -61.09600 1.000 61.97023 ?  326 ARG B C   1 
ATOM   5206 O  O   . ARG B 1 346 ? -23.87300 13.45000  -60.21200 1.000 68.26261 ?  326 ARG B O   1 
ATOM   5207 C  CB  . ARG B 1 346 ? -22.01300 15.54500  -59.72900 1.000 52.26023 ?  326 ARG B CB  1 
ATOM   5208 C  CG  . ARG B 1 346 ? -20.76800 14.92200  -60.34200 1.000 49.96142 ?  326 ARG B CG  1 
ATOM   5209 C  CD  . ARG B 1 346 ? -19.55100 15.08400  -59.45200 1.000 49.50536 ?  326 ARG B CD  1 
ATOM   5210 N  NE  . ARG B 1 346 ? -19.63900 16.27200  -58.61500 1.000 40.52288 ?  326 ARG B NE  1 
ATOM   5211 C  CZ  . ARG B 1 346 ? -18.80000 17.30000  -58.66800 1.000 47.51122 ?  326 ARG B CZ  1 
ATOM   5212 N  NH1 . ARG B 1 346 ? -17.66500 17.19600  -59.33500 1.000 54.52173 ?  326 ARG B NH1 1 
ATOM   5213 N  NH2 . ARG B 1 346 ? -19.09900 18.42900  -58.04900 1.000 46.31023 ?  326 ARG B NH2 1 
ATOM   5214 N  N   . ASP B 1 347 ? -24.07900 14.13100  -62.37500 1.000 66.08383 ?  327 ASP B N   1 
ATOM   5215 C  CA  . ASP B 1 347 ? -24.77100 12.88300  -62.80500 1.000 64.92783 ?  327 ASP B CA  1 
ATOM   5216 C  C   . ASP B 1 347 ? -23.60100 11.89100  -62.88200 1.000 73.30970 ?  327 ASP B C   1 
ATOM   5217 O  O   . ASP B 1 347 ? -23.63000 10.91200  -62.11100 1.000 78.40561 ?  327 ASP B O   1 
ATOM   5218 C  CB  . ASP B 1 347 ? -25.60600 13.02100  -64.08500 1.000 61.54154 ?  327 ASP B CB  1 
ATOM   5219 N  N   . PRO B 1 348 ? -22.57000 12.06800  -63.74500 1.000 69.44165 ?  328 PRO B N   1 
ATOM   5220 C  CA  . PRO B 1 348 ? -21.40800 11.17000  -63.71600 1.000 68.64775 ?  328 PRO B CA  1 
ATOM   5221 C  C   . PRO B 1 348 ? -20.59600 11.35600  -62.42300 1.000 65.51775 ?  328 PRO B C   1 
ATOM   5222 O  O   . PRO B 1 348 ? -19.96500 12.37700  -62.29400 1.000 58.22674 ?  328 PRO B O   1 
ATOM   5223 C  CB  . PRO B 1 348 ? -20.54300 11.62100  -64.89500 1.000 65.31208 ?  328 PRO B CB  1 
ATOM   5224 C  CG  . PRO B 1 348 ? -20.95800 13.05400  -65.14500 1.000 65.33174 ?  328 PRO B CG  1 
ATOM   5225 C  CD  . PRO B 1 348 ? -22.42000 13.11400  -64.76200 1.000 64.21750 ?  328 PRO B CD  1 
ATOM   5226 N  N   . ASN B 1 349 ? -20.61500 10.36400  -61.51800 1.000 64.65177 ?  329 ASN B N   1 
ATOM   5227 C  CA  . ASN B 1 349 ? -19.87600 10.45500  -60.22700 1.000 58.47695 ?  329 ASN B CA  1 
ATOM   5228 C  C   . ASN B 1 349 ? -19.08600 9.17100   -60.00800 1.000 54.47998 ?  329 ASN B C   1 
ATOM   5229 O  O   . ASN B 1 349 ? -19.54000 8.34200   -59.21600 1.000 55.06682 ?  329 ASN B O   1 
ATOM   5230 C  CB  . ASN B 1 349 ? -20.77500 10.67900  -59.00900 1.000 56.47365 ?  329 ASN B CB  1 
ATOM   5231 C  CG  . ASN B 1 349 ? -20.14300 11.55400  -57.94900 1.000 49.86463 ?  329 ASN B CG  1 
ATOM   5232 O  OD1 . ASN B 1 349 ? -18.94300 11.47600  -57.70800 1.000 45.26591 ?  329 ASN B OD1 1 
ATOM   5233 N  ND2 . ASN B 1 349 ? -20.94600 12.38800  -57.31100 1.000 46.91036 ?  329 ASN B ND2 1 
ATOM   5234 N  N   . PRO B 1 350 ? -17.90700 9.01900   -60.64100 1.000 57.86001 ?  330 PRO B N   1 
ATOM   5235 C  CA  . PRO B 1 350 ? -17.12300 7.80700   -60.51800 1.000 53.38237 ?  330 PRO B CA  1 
ATOM   5236 C  C   . PRO B 1 350 ? -16.29100 7.86300   -59.23300 1.000 45.78248 ?  330 PRO B C   1 
ATOM   5237 O  O   . PRO B 1 350 ? -15.12700 7.60200   -59.28800 1.000 46.72230 ?  330 PRO B O   1 
ATOM   5238 C  CB  . PRO B 1 350 ? -16.23400 7.90500   -61.75600 1.000 47.82710 ?  330 PRO B CB  1 
ATOM   5239 C  CG  . PRO B 1 350 ? -15.95000 9.38000   -61.87300 1.000 53.36184 ?  330 PRO B CG  1 
ATOM   5240 C  CD  . PRO B 1 350 ? -17.24800 10.03800  -61.46200 1.000 55.03591 ?  330 PRO B CD  1 
ATOM   5241 N  N   . HIS B 1 351 ? -16.92400 8.20600   -58.11400 1.000 45.82642 ?  331 HIS B N   1 
ATOM   5242 C  CA  . HIS B 1 351 ? -16.17800 8.33000   -56.83500 1.000 45.19847 ?  331 HIS B CA  1 
ATOM   5243 C  C   . HIS B 1 351 ? -15.75900 6.92100   -56.39700 1.000 39.27436 ?  331 HIS B C   1 
ATOM   5244 O  O   . HIS B 1 351 ? -16.35900 5.93200   -56.83400 1.000 36.79327 ?  331 HIS B O   1 
ATOM   5245 C  CB  . HIS B 1 351 ? -16.95300 9.17000   -55.80900 1.000 42.41736 ?  331 HIS B CB  1 
ATOM   5246 C  CG  . HIS B 1 351 ? -18.17500 8.48600   -55.29800 1.000 48.85306 ?  331 HIS B CG  1 
ATOM   5247 N  ND1 . HIS B 1 351 ? -18.12800 7.40600   -54.44600 1.000 42.53390 ?  331 HIS B ND1 1 
ATOM   5248 C  CD2 . HIS B 1 351 ? -19.46900 8.71000   -55.53800 1.000 45.64876 ?  331 HIS B CD2 1 
ATOM   5249 C  CE1 . HIS B 1 351 ? -19.36000 7.00600   -54.18100 1.000 45.94767 ?  331 HIS B CE1 1 
ATOM   5250 N  NE2 . HIS B 1 351 ? -20.18800 7.78500   -54.83500 1.000 47.68295 ?  331 HIS B NE2 1 
ATOM   5251 N  N   . LEU B 1 352 ? -14.72900 6.84700   -55.55500 1.000 36.00704 ?  332 LEU B N   1 
ATOM   5252 C  CA  . LEU B 1 352 ? -14.19000 5.52500   -55.13900 1.000 39.39092 ?  332 LEU B CA  1 
ATOM   5253 C  C   . LEU B 1 352 ? -14.40800 5.33100   -53.63800 1.000 38.56365 ?  332 LEU B C   1 
ATOM   5254 O  O   . LEU B 1 352 ? -13.67900 4.54300   -53.04500 1.000 36.07828 ?  332 LEU B O   1 
ATOM   5255 C  CB  . LEU B 1 352 ? -12.69600 5.48700   -55.47200 1.000 40.92129 ?  332 LEU B CB  1 
ATOM   5256 C  CG  . LEU B 1 352 ? -12.31100 5.67900   -56.93600 1.000 38.20919 ?  332 LEU B CG  1 
ATOM   5257 C  CD1 . LEU B 1 352 ? -10.85700 6.10800   -57.03900 1.000 41.89421 ?  332 LEU B CD1 1 
ATOM   5258 C  CD2 . LEU B 1 352 ? -12.54200 4.39900   -57.72100 1.000 34.20828 ?  332 LEU B CD2 1 
ATOM   5259 N  N   . SER B 1 353 ? -15.39800 6.01800   -53.07700 1.000 37.94663 ?  333 SER B N   1 
ATOM   5260 C  CA  . SER B 1 353 ? -15.61700 5.97100   -51.63600 1.000 36.09336 ?  333 SER B CA  1 
ATOM   5261 C  C   . SER B 1 353 ? -15.81900 4.55400   -51.12300 1.000 33.97415 ?  333 SER B C   1 
ATOM   5262 O  O   . SER B 1 353 ? -15.58600 4.29700   -49.93700 1.000 35.05746 ?  333 SER B O   1 
ATOM   5263 C  CB  . SER B 1 353 ? -16.82400 6.83100   -51.26600 1.000 38.79941 ?  333 SER B CB  1 
ATOM   5264 O  OG  . SER B 1 353 ? -16.74200 8.10400   -51.88100 1.000 37.60416 ?  333 SER B OG  1 
ATOM   5265 N  N   . TYR B 1 354 ? -16.24100 3.63200   -51.98600 1.000 31.82790 ?  334 TYR B N   1 
ATOM   5266 C  CA  . TYR B 1 354 ? -16.47200 2.24600   -51.60700 1.000 32.34081 ?  334 TYR B CA  1 
ATOM   5267 C  C   . TYR B 1 354 ? -15.39100 1.31900   -52.15000 1.000 33.29510 ?  334 TYR B C   1 
ATOM   5268 O  O   . TYR B 1 354 ? -15.62100 0.11400   -52.27800 1.000 32.61206 ?  334 TYR B O   1 
ATOM   5269 C  CB  . TYR B 1 354 ? -17.85500 1.79400   -52.08200 1.000 34.76799 ?  334 TYR B CB  1 
ATOM   5270 C  CG  . TYR B 1 354 ? -18.99700 2.57100   -51.46100 1.000 35.22107 ?  334 TYR B CG  1 
ATOM   5271 C  CD1 . TYR B 1 354 ? -19.36700 2.36800   -50.13500 1.000 31.87065 ?  334 TYR B CD1 1 
ATOM   5272 C  CD2 . TYR B 1 354 ? -19.70100 3.51500   -52.20000 1.000 39.84535 ?  334 TYR B CD2 1 
ATOM   5273 C  CE1 . TYR B 1 354 ? -20.41000 3.08200   -49.56500 1.000 34.84397 ?  334 TYR B CE1 1 
ATOM   5274 C  CE2 . TYR B 1 354 ? -20.74200 4.23000   -51.64100 1.000 42.93168 ?  334 TYR B CE2 1 
ATOM   5275 C  CZ  . TYR B 1 354 ? -21.09500 4.01100   -50.32500 1.000 38.09618 ?  334 TYR B CZ  1 
ATOM   5276 O  OH  . TYR B 1 354 ? -22.13100 4.73000   -49.77200 1.000 36.65781 ?  334 TYR B OH  1 
ATOM   5277 N  N   . GLY B 1 355 ? -14.21800 1.85900   -52.47500 1.000 34.63194 ?  335 GLY B N   1 
ATOM   5278 C  CA  . GLY B 1 355 ? -13.12400 1.04700   -52.96300 1.000 31.46771 ?  335 GLY B CA  1 
ATOM   5279 C  C   . GLY B 1 355 ? -13.26600 0.67400   -54.42900 1.000 39.56647 ?  335 GLY B C   1 
ATOM   5280 O  O   . GLY B 1 355 ? -14.12900 1.16600   -55.16400 1.000 28.62993 ?  335 GLY B O   1 
ATOM   5281 N  N   . HIS B 1 356 ? -12.38600 -0.23300  -54.85100 1.000 31.66154 ?  336 HIS B N   1 
ATOM   5282 C  CA  . HIS B 1 356 ? -12.32200 -0.66000  -56.24100 1.000 39.62433 ?  336 HIS B CA  1 
ATOM   5283 C  C   . HIS B 1 356 ? -11.49100 -1.93200  -56.31500 1.000 36.51201 ?  336 HIS B C   1 
ATOM   5284 O  O   . HIS B 1 356 ? -10.43900 -2.02800  -55.67800 1.000 37.47125 ?  336 HIS B O   1 
ATOM   5285 C  CB  . HIS B 1 356 ? -11.71500 0.43300   -57.12900 1.000 36.55047 ?  336 HIS B CB  1 
ATOM   5286 C  CG  . HIS B 1 356 ? -11.45100 -0.00400  -58.53500 1.000 40.13520 ?  336 HIS B CG  1 
ATOM   5287 N  ND1 . HIS B 1 356 ? -12.46100 -0.30700  -59.42200 1.000 41.97074 ?  336 HIS B ND1 1 
ATOM   5288 C  CD2 . HIS B 1 356 ? -10.29000 -0.18300  -59.21000 1.000 39.38482 ?  336 HIS B CD2 1 
ATOM   5289 C  CE1 . HIS B 1 356 ? -11.93400 -0.65900  -60.58200 1.000 42.29707 ?  336 HIS B CE1 1 
ATOM   5290 N  NE2 . HIS B 1 356 ? -10.61900 -0.59100  -60.48000 1.000 46.32759 ?  336 HIS B NE2 1 
ATOM   5291 N  N   . GLY B 1 357 ? -11.97100 -2.90500  -57.08400 1.000 33.15150 ?  337 GLY B N   1 
ATOM   5292 C  CA  . GLY B 1 357 ? -11.27200 -4.16900  -57.20700 1.000 32.49839 ?  337 GLY B CA  1 
ATOM   5293 C  C   . GLY B 1 357 ? -11.80200 -5.24200  -56.28000 1.000 33.69236 ?  337 GLY B C   1 
ATOM   5294 O  O   . GLY B 1 357 ? -12.96500 -5.20100  -55.87200 1.000 30.36853 ?  337 GLY B O   1 
ATOM   5295 N  N   . ILE B 1 358 ? -10.94600 -6.20500  -55.92900 1.000 33.70552 ?  338 ILE B N   1 
ATOM   5296 C  CA  . ILE B 1 358 ? -11.39100 -7.35300  -55.14400 1.000 39.17637 ?  338 ILE B CA  1 
ATOM   5297 C  C   . ILE B 1 358 ? -11.82700 -6.94200  -53.74200 1.000 35.03245 ?  338 ILE B C   1 
ATOM   5298 O  O   . ILE B 1 358 ? -12.65400 -7.62100  -53.12300 1.000 35.97611 ?  338 ILE B O   1 
ATOM   5299 C  CB  . ILE B 1 358 ? -10.28200 -8.41900  -55.09000 1.000 35.85336 ?  338 ILE B CB  1 
ATOM   5300 C  CG1 . ILE B 1 358 ? -9.03300  -7.84400  -54.42100 1.000 35.00734 ?  338 ILE B CG1 1 
ATOM   5301 C  CG2 . ILE B 1 358 ? -9.96000  -8.93300  -56.48700 1.000 40.74432 ?  338 ILE B CG2 1 
ATOM   5302 C  CD1 . ILE B 1 358 ? -7.97600  -8.86900  -54.13200 1.000 35.11582 ?  338 ILE B CD1 1 
ATOM   5303 N  N   . HIS B 1 359 ? -11.28800 -5.84400  -53.21500 1.000 36.11387 ?  339 HIS B N   1 
ATOM   5304 C  CA  . HIS B 1 359 ? -11.62900 -5.38300  -51.87500 1.000 36.16537 ?  339 HIS B CA  1 
ATOM   5305 C  C   . HIS B 1 359 ? -12.76900 -4.37000  -51.86900 1.000 37.31358 ?  339 HIS B C   1 
ATOM   5306 O  O   . HIS B 1 359 ? -12.98700 -3.71000  -50.84800 1.000 29.20944 ?  339 HIS B O   1 
ATOM   5307 C  CB  . HIS B 1 359 ? -10.39300 -4.78800  -51.19500 1.000 30.22743 ?  339 HIS B CB  1 
ATOM   5308 C  CG  . HIS B 1 359 ? -9.35200  -5.80600  -50.84100 1.000 32.30358 ?  339 HIS B CG  1 
ATOM   5309 N  ND1 . HIS B 1 359 ? -9.57100  -6.80700  -49.91800 1.000 27.35016 ?  339 HIS B ND1 1 
ATOM   5310 C  CD2 . HIS B 1 359 ? -8.09100  -5.98900  -51.30100 1.000 30.59508 ?  339 HIS B CD2 1 
ATOM   5311 C  CE1 . HIS B 1 359 ? -8.48500  -7.55300  -49.81400 1.000 24.86761 ?  339 HIS B CE1 1 
ATOM   5312 N  NE2 . HIS B 1 359 ? -7.57400  -7.08000  -50.64400 1.000 28.26736 ?  339 HIS B NE2 1 
ATOM   5313 N  N   . ARG B 1 360 ? -13.49500 -4.24400  -52.98300 1.000 34.79597 ?  340 ARG B N   1 
ATOM   5314 C  CA  . ARG B 1 360 ? -14.63400 -3.33700  -53.07200 1.000 33.86965 ?  340 ARG B CA  1 
ATOM   5315 C  C   . ARG B 1 360 ? -15.61700 -3.58900  -51.93300 1.000 25.87006 ?  340 ARG B C   1 
ATOM   5316 O  O   . ARG B 1 360 ? -15.87100 -4.73400  -51.55300 1.000 28.85283 ?  340 ARG B O   1 
ATOM   5317 C  CB  . ARG B 1 360 ? -15.32800 -3.52100  -54.42600 1.000 34.94018 ?  340 ARG B CB  1 
ATOM   5318 C  CG  . ARG B 1 360 ? -16.63800 -2.77000  -54.59200 1.000 33.57307 ?  340 ARG B CG  1 
ATOM   5319 C  CD  . ARG B 1 360 ? -16.41800 -1.38200  -55.16500 1.000 36.87692 ?  340 ARG B CD  1 
ATOM   5320 N  NE  . ARG B 1 360 ? -17.67900 -0.72100  -55.47900 1.000 49.28478 ?  340 ARG B NE  1 
ATOM   5321 C  CZ  . ARG B 1 360 ? -17.82000 0.58700   -55.65000 1.000 48.68695 ?  340 ARG B CZ  1 
ATOM   5322 N  NH1 . ARG B 1 360 ? -16.78200 1.40800   -55.60500 1.000 43.33004 ?  340 ARG B NH1 1 
ATOM   5323 N  NH2 . ARG B 1 360 ? -19.03400 1.08400   -55.87600 1.000 45.30201 ?  340 ARG B NH2 1 
ATOM   5324 N  N   . SER B 1 361 ? -16.16500 -2.50200  -51.38800 1.000 28.21747 ?  341 SER B N   1 
ATOM   5325 C  CA  . SER B 1 361 ? -16.99600 -2.58500  -50.19100 1.000 28.98966 ?  341 SER B CA  1 
ATOM   5326 C  C   . SER B 1 361 ? -18.20400 -3.49000  -50.41000 1.000 32.98452 ?  341 SER B C   1 
ATOM   5327 O  O   . SER B 1 361 ? -18.80200 -3.51300  -51.49000 1.000 29.62372 ?  341 SER B O   1 
ATOM   5328 C  CB  . SER B 1 361 ? -17.45900 -1.18600  -49.77800 1.000 27.88660 ?  341 SER B CB  1 
ATOM   5329 O  OG  . SER B 1 361 ? -18.45100 -1.24300  -48.76600 1.000 30.84949 ?  341 SER B OG  1 
ATOM   5330 N  N   . PHE B 1 362 ? -18.55100 -4.25200  -49.37000 1.000 32.54576 ?  342 PHE B N   1 
ATOM   5331 C  CA  . PHE B 1 362 ? -19.75700 -5.07200  -49.37000 1.000 33.62379 ?  342 PHE B CA  1 
ATOM   5332 C  C   . PHE B 1 362 ? -21.01800 -4.26100  -49.10700 1.000 35.37865 ?  342 PHE B C   1 
ATOM   5333 O  O   . PHE B 1 362 ? -22.12200 -4.78400  -49.29600 1.000 42.01077 ?  342 PHE B O   1 
ATOM   5334 C  CB  . PHE B 1 362 ? -19.66200 -6.16800  -48.30200 1.000 35.95284 ?  342 PHE B CB  1 
ATOM   5335 C  CG  . PHE B 1 362 ? -19.13400 -7.48100  -48.80800 1.000 36.15938 ?  342 PHE B CG  1 
ATOM   5336 C  CD1 . PHE B 1 362 ? -19.74800 -8.14200  -49.85900 1.000 46.24508 ?  342 PHE B CD1 1 
ATOM   5337 C  CD2 . PHE B 1 362 ? -18.03800 -8.07300  -48.20300 1.000 37.19207 ?  342 PHE B CD2 1 
ATOM   5338 C  CE1 . PHE B 1 362 ? -19.26300 -9.35700  -50.30900 1.000 43.35732 ?  342 PHE B CE1 1 
ATOM   5339 C  CE2 . PHE B 1 362 ? -17.55100 -9.28500  -48.64500 1.000 38.24120 ?  342 PHE B CE2 1 
ATOM   5340 C  CZ  . PHE B 1 362 ? -18.16100 -9.92900  -49.70000 1.000 43.70244 ?  342 PHE B CZ  1 
ATOM   5341 N  N   . GLY B 1 363 ? -20.88500 -3.01100  -48.67000 1.000 35.38292 ?  343 GLY B N   1 
ATOM   5342 C  CA  . GLY B 1 363 ? -22.02700 -2.27500  -48.16600 1.000 34.93137 ?  343 GLY B CA  1 
ATOM   5343 C  C   . GLY B 1 363 ? -22.31300 -0.95500  -48.84900 1.000 31.50348 ?  343 GLY B C   1 
ATOM   5344 O  O   . GLY B 1 363 ? -22.80200 -0.01700  -48.21000 1.000 32.73773 ?  343 GLY B O   1 
ATOM   5345 N  N   . SER B 1 364 ? -22.01900 -0.86600  -50.14600 1.000 29.55664 ?  344 SER B N   1 
ATOM   5346 C  CA  . SER B 1 364 ? -22.42900 0.31100   -50.90200 1.000 30.83224 ?  344 SER B CA  1 
ATOM   5347 C  C   . SER B 1 364 ? -23.94400 0.46300   -50.88800 1.000 28.13094 ?  344 SER B C   1 
ATOM   5348 O  O   . SER B 1 364 ? -24.46100 1.55500   -50.63900 1.000 37.50458 ?  344 SER B O   1 
ATOM   5349 C  CB  . SER B 1 364 ? -21.91800 0.21800   -52.33800 1.000 34.82052 ?  344 SER B CB  1 
ATOM   5350 O  OG  . SER B 1 364 ? -22.51100 -0.88200  -53.00600 1.000 47.08754 ?  344 SER B OG  1 
ATOM   5351 N  N   . ARG B 1 365 ? -24.67200 -0.62900  -51.12700 1.000 23.54307 ?  345 ARG B N   1 
ATOM   5352 C  CA  . ARG B 1 365 ? -26.13100 -0.55600  -51.16200 1.000 29.23764 ?  345 ARG B CA  1 
ATOM   5353 C  C   . ARG B 1 365 ? -26.70200 -0.21700  -49.78900 1.000 24.08740 ?  345 ARG B C   1 
ATOM   5354 O  O   . ARG B 1 365 ? -27.56400 0.66100   -49.66500 1.000 34.04344 ?  345 ARG B O   1 
ATOM   5355 C  CB  . ARG B 1 365 ? -26.71000 -1.87500  -51.67300 1.000 31.03461 ?  345 ARG B CB  1 
ATOM   5356 N  N   . LEU B 1 366 ? -26.23900 -0.91600  -48.74800 1.000 27.85437 ?  346 LEU B N   1 
ATOM   5357 C  CA  . LEU B 1 366 ? -26.70500 -0.64000  -47.39200 1.000 24.97260 ?  346 LEU B CA  1 
ATOM   5358 C  C   . LEU B 1 366 ? -26.44500 0.81100   -47.00900 1.000 28.11389 ?  346 LEU B C   1 
ATOM   5359 O  O   . LEU B 1 366 ? -27.31800 1.48400   -46.45000 1.000 22.48272 ?  346 LEU B O   1 
ATOM   5360 C  CB  . LEU B 1 366 ? -26.02900 -1.59200  -46.40400 1.000 24.99244 ?  346 LEU B CB  1 
ATOM   5361 C  CG  . LEU B 1 366 ? -26.58100 -1.66000  -44.97600 1.000 28.34183 ?  346 LEU B CG  1 
ATOM   5362 C  CD1 . LEU B 1 366 ? -28.10600 -1.65900  -44.95800 1.000 27.12458 ?  346 LEU B CD1 1 
ATOM   5363 C  CD2 . LEU B 1 366 ? -26.03100 -2.87800  -44.25200 1.000 28.16503 ?  346 LEU B CD2 1 
ATOM   5364 N  N   . SER B 1 367 ? -25.25100 1.29100   -47.32900 1.000 23.48891 ?  347 SER B N   1 
ATOM   5365 C  CA  . SER B 1 367 ? -24.92000 2.70000   -47.03300 1.000 25.73268 ?  347 SER B CA  1 
ATOM   5366 C  C   . SER B 1 367 ? -25.92600 3.61600   -47.72600 1.000 24.29987 ?  347 SER B C   1 
ATOM   5367 O  O   . SER B 1 367 ? -26.46300 4.50100   -47.07500 1.000 29.70256 ?  347 SER B O   1 
ATOM   5368 C  CB  . SER B 1 367 ? -23.51000 3.00700   -47.44400 1.000 26.29324 ?  347 SER B CB  1 
ATOM   5369 O  OG  . SER B 1 367 ? -23.20800 4.37500   -47.23400 1.000 35.22240 ?  347 SER B OG  1 
ATOM   5370 N  N   . GLN B 1 368 ? -26.13300 3.40900   -49.01600 1.000 24.89997 ?  348 GLN B N   1 
ATOM   5371 C  CA  . GLN B 1 368 ? -27.04200 4.28400   -49.79900 1.000 31.11938 ?  348 GLN B CA  1 
ATOM   5372 C  C   . GLN B 1 368 ? -28.45300 4.27300   -49.19200 1.000 24.00575 ?  348 GLN B C   1 
ATOM   5373 O  O   . GLN B 1 368 ? -29.04100 5.35400   -49.07300 1.000 29.08135 ?  348 GLN B O   1 
ATOM   5374 C  CB  . GLN B 1 368 ? -27.02500 3.84300   -51.26300 1.000 28.63318 ?  348 GLN B CB  1 
ATOM   5375 C  CG  . GLN B 1 368 ? -25.71300 4.16700   -51.96600 1.000 39.54271 ?  348 GLN B CG  1 
ATOM   5376 C  CD  . GLN B 1 368 ? -25.50000 3.40100   -53.24900 1.000 45.67893 ?  348 GLN B CD  1 
ATOM   5377 O  OE1 . GLN B 1 368 ? -25.93500 2.26200   -53.40000 1.000 45.22120 ?  348 GLN B OE1 1 
ATOM   5378 N  NE2 . GLN B 1 368 ? -24.82000 4.02800   -54.19300 1.000 42.89167 ?  348 GLN B NE2 1 
ATOM   5379 N  N   . ALA B 1 369 ? -28.94900 3.10200   -48.81000 1.000 26.52020 ?  349 ALA B N   1 
ATOM   5380 C  CA  . ALA B 1 369 ? -30.31900 2.99100   -48.26400 1.000 23.84378 ?  349 ALA B CA  1 
ATOM   5381 C  C   . ALA B 1 369 ? -30.40300 3.72000   -46.92600 1.000 24.34384 ?  349 ALA B C   1 
ATOM   5382 O  O   . ALA B 1 369 ? -31.34200 4.48700   -46.72400 1.000 27.57019 ?  349 ALA B O   1 
ATOM   5383 C  CB  . ALA B 1 369 ? -30.68600 1.54700   -48.12600 1.000 24.40568 ?  349 ALA B CB  1 
ATOM   5384 N  N   . GLU B 1 370 ? -29.41600 3.48800   -46.06600 1.000 22.09241 ?  350 GLU B N   1 
ATOM   5385 C  CA  . GLU B 1 370 ? -29.42400 4.15400   -44.76800 1.000 26.07620 ?  350 GLU B CA  1 
ATOM   5386 C  C   . GLU B 1 370 ? -29.31600 5.66500   -44.93000 1.000 25.78020 ?  350 GLU B C   1 
ATOM   5387 O  O   . GLU B 1 370 ? -30.00200 6.42500   -44.23400 1.000 24.18259 ?  350 GLU B O   1 
ATOM   5388 C  CB  . GLU B 1 370 ? -28.28700 3.60900   -43.89100 1.000 19.33981 ?  350 GLU B CB  1 
ATOM   5389 C  CG  . GLU B 1 370 ? -28.46400 2.14300   -43.49800 1.000 22.01134 ?  350 GLU B CG  1 
ATOM   5390 C  CD  . GLU B 1 370 ? -27.63500 1.74800   -42.28000 1.000 26.20342 ?  350 GLU B CD  1 
ATOM   5391 O  OE1 . GLU B 1 370 ? -27.50400 2.57100   -41.35200 1.000 25.76438 ?  350 GLU B OE1 1 
ATOM   5392 O  OE2 . GLU B 1 370 ? -27.12900 0.60600   -42.24500 1.000 23.20162 -1 350 GLU B OE2 1 
ATOM   5393 N  N   . ALA B 1 371 ? -28.46300 6.11900   -45.85400 1.000 24.33804 ?  351 ALA B N   1 
ATOM   5394 C  CA  . ALA B 1 371 ? -28.31100 7.55200   -46.08800 1.000 24.23860 ?  351 ALA B CA  1 
ATOM   5395 C  C   . ALA B 1 371 ? -29.60700 8.16600   -46.60200 1.000 24.72856 ?  351 ALA B C   1 
ATOM   5396 O  O   . ALA B 1 371 ? -30.02900 9.23200   -46.13900 1.000 32.79572 ?  351 ALA B O   1 
ATOM   5397 C  CB  . ALA B 1 371 ? -27.17100 7.80600   -47.07600 1.000 21.95427 ?  351 ALA B CB  1 
ATOM   5398 N  N   . ALA B 1 372 ? -30.24800 7.50700   -47.57000 1.000 25.44224 ?  352 ALA B N   1 
ATOM   5399 C  CA  . ALA B 1 372 ? -31.51100 8.01300   -48.10200 1.000 28.53738 ?  352 ALA B CA  1 
ATOM   5400 C  C   . ALA B 1 372 ? -32.55800 8.15500   -47.00700 1.000 32.22505 ?  352 ALA B C   1 
ATOM   5401 O  O   . ALA B 1 372 ? -33.25400 9.17400   -46.93500 1.000 29.99673 ?  352 ALA B O   1 
ATOM   5402 C  CB  . ALA B 1 372 ? -32.01900 7.09300   -49.21200 1.000 27.25216 ?  352 ALA B CB  1 
ATOM   5403 N  N   . ALA B 1 373 ? -32.66900 7.15100   -46.13200 1.000 31.04170 ?  353 ALA B N   1 
ATOM   5404 C  CA  . ALA B 1 373 ? -33.63900 7.21400   -45.04200 1.000 29.40938 ?  353 ALA B CA  1 
ATOM   5405 C  C   . ALA B 1 373 ? -33.34700 8.37700   -44.10400 1.000 31.57301 ?  353 ALA B C   1 
ATOM   5406 O  O   . ALA B 1 373 ? -34.27000 9.05400   -43.63600 1.000 29.01913 ?  353 ALA B O   1 
ATOM   5407 C  CB  . ALA B 1 373 ? -33.64600 5.89400   -44.27200 1.000 30.46718 ?  353 ALA B CB  1 
ATOM   5408 N  N   . ALA B 1 374 ? -32.06800 8.62200   -43.81300 1.000 24.34377 ?  354 ALA B N   1 
ATOM   5409 C  CA  . ALA B 1 374 ? -31.70900 9.73000   -42.93300 1.000 27.19763 ?  354 ALA B CA  1 
ATOM   5410 C  C   . ALA B 1 374 ? -32.06300 11.07300  -43.55900 1.000 26.01831 ?  354 ALA B C   1 
ATOM   5411 O  O   . ALA B 1 374 ? -32.73600 11.90400  -42.94000 1.000 24.33676 ?  354 ALA B O   1 
ATOM   5412 C  CB  . ALA B 1 374 ? -30.21700 9.66700   -42.60000 1.000 21.90334 ?  354 ALA B CB  1 
ATOM   5413 N  N   . PHE B 1 375 ? -31.61000 11.30500  -44.79200 1.000 29.01418 ?  355 PHE B N   1 
ATOM   5414 C  CA  . PHE B 1 375 ? -31.83600 12.60100  -45.42300 1.000 32.37501 ?  355 PHE B CA  1 
ATOM   5415 C  C   . PHE B 1 375 ? -33.30700 12.81000  -45.75600 1.000 30.54190 ?  355 PHE B C   1 
ATOM   5416 O  O   . PHE B 1 375 ? -33.83500 13.91100  -45.56700 1.000 31.07216 ?  355 PHE B O   1 
ATOM   5417 C  CB  . PHE B 1 375 ? -30.96300 12.73300  -46.66900 1.000 31.44314 ?  355 PHE B CB  1 
ATOM   5418 C  CG  . PHE B 1 375 ? -29.48700 12.65200  -46.38100 1.000 36.40443 ?  355 PHE B CG  1 
ATOM   5419 C  CD1 . PHE B 1 375 ? -28.91600 13.45800  -45.40800 1.000 37.02725 ?  355 PHE B CD1 1 
ATOM   5420 C  CD2 . PHE B 1 375 ? -28.67700 11.76700  -47.07100 1.000 39.90422 ?  355 PHE B CD2 1 
ATOM   5421 C  CE1 . PHE B 1 375 ? -27.56400 13.38900  -45.13100 1.000 36.34625 ?  355 PHE B CE1 1 
ATOM   5422 C  CE2 . PHE B 1 375 ? -27.32200 11.69100  -46.79800 1.000 37.76409 ?  355 PHE B CE2 1 
ATOM   5423 C  CZ  . PHE B 1 375 ? -26.76600 12.50400  -45.82600 1.000 38.29953 ?  355 PHE B CZ  1 
ATOM   5424 N  N   . SER B 1 376 ? -33.98900 11.76700  -46.23600 1.000 26.23866 ?  356 SER B N   1 
ATOM   5425 C  CA  . SER B 1 376 ? -35.41600 11.89000  -46.52300 1.000 33.66708 ?  356 SER B CA  1 
ATOM   5426 C  C   . SER B 1 376 ? -36.19100 12.31900  -45.28200 1.000 36.63645 ?  356 SER B C   1 
ATOM   5427 O  O   . SER B 1 376 ? -37.00700 13.24700  -45.33600 1.000 38.61997 ?  356 SER B O   1 
ATOM   5428 C  CB  . SER B 1 376 ? -35.96300 10.57100  -47.07000 1.000 35.69988 ?  356 SER B CB  1 
ATOM   5429 O  OG  . SER B 1 376 ? -35.86800 9.54600   -46.09700 1.000 46.29286 ?  356 SER B OG  1 
ATOM   5430 N  N   . ALA B 1 377 ? -35.93300 11.66500  -44.14400 1.000 31.21627 ?  357 ALA B N   1 
ATOM   5431 C  CA  . ALA B 1 377 ? -36.63900 12.02600  -42.91700 1.000 26.87125 ?  357 ALA B CA  1 
ATOM   5432 C  C   . ALA B 1 377 ? -36.30700 13.44800  -42.48500 1.000 32.33694 ?  357 ALA B C   1 
ATOM   5433 O  O   . ALA B 1 377 ? -37.19900 14.20800  -42.09100 1.000 36.60555 ?  357 ALA B O   1 
ATOM   5434 C  CB  . ALA B 1 377 ? -36.30400 11.03400  -41.80300 1.000 27.99308 ?  357 ALA B CB  1 
ATOM   5435 N  N   . LEU B 1 378 ? -35.03400 13.82400  -42.56100 1.000 29.77576 ?  358 LEU B N   1 
ATOM   5436 C  CA  . LEU B 1 378 ? -34.64500 15.21700  -42.19900 1.000 32.18776 ?  358 LEU B CA  1 
ATOM   5437 C  C   . LEU B 1 378 ? -35.35300 16.22000  -43.11600 1.000 31.72096 ?  358 LEU B C   1 
ATOM   5438 O  O   . LEU B 1 378 ? -35.80500 17.25800  -42.61600 1.000 31.22755 ?  358 LEU B O   1 
ATOM   5439 C  CB  . LEU B 1 378 ? -33.12600 15.37500  -42.31300 1.000 34.30946 ?  358 LEU B CB  1 
ATOM   5440 C  CG  . LEU B 1 378 ? -32.32300 14.89200  -41.11000 1.000 31.50955 ?  358 LEU B CG  1 
ATOM   5441 C  CD1 . LEU B 1 378 ? -30.86000 14.73300  -41.48100 1.000 35.77684 ?  358 LEU B CD1 1 
ATOM   5442 C  CD2 . LEU B 1 378 ? -32.47600 15.84900  -39.94100 1.000 26.36600 ?  358 LEU B CD2 1 
ATOM   5443 N  N   . LEU B 1 379 ? -35.40000 15.91900  -44.40300 1.000 27.47078 ?  359 LEU B N   1 
ATOM   5444 C  CA  . LEU B 1 379 ? -36.00000 16.86000  -45.38000 1.000 34.71492 ?  359 LEU B CA  1 
ATOM   5445 C  C   . LEU B 1 379 ? -37.47200 17.11400  -45.03600 1.000 35.80424 ?  359 LEU B C   1 
ATOM   5446 O  O   . LEU B 1 379 ? -37.91300 18.25700  -45.21400 1.000 37.53880 ?  359 LEU B O   1 
ATOM   5447 C  CB  . LEU B 1 379 ? -35.85200 16.26000  -46.77600 1.000 30.47353 ?  359 LEU B CB  1 
ATOM   5448 C  CG  . LEU B 1 379 ? -34.45300 16.37200  -47.37800 1.000 43.15499 ?  359 LEU B CG  1 
ATOM   5449 C  CD1 . LEU B 1 379 ? -34.30500 15.48200  -48.59900 1.000 37.84040 ?  359 LEU B CD1 1 
ATOM   5450 C  CD2 . LEU B 1 379 ? -34.12300 17.81100  -47.72100 1.000 43.57094 ?  359 LEU B CD2 1 
ATOM   5451 N  N   . ALA B 1 380 ? -38.18500 16.09400  -44.55000 1.000 37.54298 ?  360 ALA B N   1 
ATOM   5452 C  CA  . ALA B 1 380 ? -39.62600 16.22200  -44.21200 1.000 32.39794 ?  360 ALA B CA  1 
ATOM   5453 C  C   . ALA B 1 380 ? -39.83900 16.97400  -42.89500 1.000 39.63391 ?  360 ALA B C   1 
ATOM   5454 O  O   . ALA B 1 380 ? -40.90300 17.57400  -42.73600 1.000 41.69691 ?  360 ALA B O   1 
ATOM   5455 C  CB  . ALA B 1 380 ? -40.24300 14.86100  -44.13100 1.000 31.59753 ?  360 ALA B CB  1 
ATOM   5456 N  N   . ARG B 1 381 ? -38.88000 16.91700  -41.98100 1.000 34.31208 ?  361 ARG B N   1 
ATOM   5457 C  CA  . ARG B 1 381 ? -39.03100 17.56900  -40.65700 1.000 39.55428 ?  361 ARG B CA  1 
ATOM   5458 C  C   . ARG B 1 381 ? -38.57000 19.02500  -40.74600 1.000 43.18257 ?  361 ARG B C   1 
ATOM   5459 O  O   . ARG B 1 381 ? -39.14000 19.86200  -40.04800 1.000 33.14246 ?  361 ARG B O   1 
ATOM   5460 C  CB  . ARG B 1 381 ? -38.22900 16.78900  -39.61300 1.000 35.02754 ?  361 ARG B CB  1 
ATOM   5461 C  CG  . ARG B 1 381 ? -38.21100 17.42000  -38.23300 1.000 39.14206 ?  361 ARG B CG  1 
ATOM   5462 C  CD  . ARG B 1 381 ? -39.52600 17.15500  -37.54200 1.000 35.58916 ?  361 ARG B CD  1 
ATOM   5463 N  NE  . ARG B 1 381 ? -39.43800 17.57400  -36.15800 1.000 38.12325 ?  361 ARG B NE  1 
ATOM   5464 C  CZ  . ARG B 1 381 ? -38.85400 16.87300  -35.20100 1.000 32.80821 ?  361 ARG B CZ  1 
ATOM   5465 N  NH1 . ARG B 1 381 ? -38.50800 15.62000  -35.41900 1.000 37.23578 ?  361 ARG B NH1 1 
ATOM   5466 N  NH2 . ARG B 1 381 ? -38.62500 17.42900  -34.02700 1.000 37.26117 ?  361 ARG B NH2 1 
ATOM   5467 N  N   . GLY B 1 382 ? -37.54700 19.29100  -41.56500 1.000 40.55822 ?  362 GLY B N   1 
ATOM   5468 C  CA  . GLY B 1 382 ? -36.98400 20.65200  -41.66100 1.000 39.19053 ?  362 GLY B CA  1 
ATOM   5469 C  C   . GLY B 1 382 ? -35.83800 20.83000  -40.67900 1.000 43.95850 ?  362 GLY B C   1 
ATOM   5470 O  O   . GLY B 1 382 ? -36.09900 20.78400  -39.46500 1.000 48.56500 ?  362 GLY B O   1 
ATOM   5471 N  N   . PHE B 1 383 ? -34.61300 21.01500  -41.18000 1.000 44.48403 ?  363 PHE B N   1 
ATOM   5472 C  CA  . PHE B 1 383 ? -33.43000 21.12300  -40.28400 1.000 47.43346 ?  363 PHE B CA  1 
ATOM   5473 C  C   . PHE B 1 383 ? -32.67700 22.42800  -40.56900 1.000 45.63179 ?  363 PHE B C   1 
ATOM   5474 O  O   . PHE B 1 383 ? -32.53500 22.79200  -41.75300 1.000 48.09669 ?  363 PHE B O   1 
ATOM   5475 C  CB  . PHE B 1 383 ? -32.53100 19.88900  -40.41900 1.000 44.11672 ?  363 PHE B CB  1 
ATOM   5476 C  CG  . PHE B 1 383 ? -32.01600 19.60500  -41.80900 1.000 40.45572 ?  363 PHE B CG  1 
ATOM   5477 C  CD1 . PHE B 1 383 ? -32.80500 18.95100  -42.74100 1.000 40.69196 ?  363 PHE B CD1 1 
ATOM   5478 C  CD2 . PHE B 1 383 ? -30.73500 19.97900  -42.18000 1.000 43.93180 ?  363 PHE B CD2 1 
ATOM   5479 C  CE1 . PHE B 1 383 ? -32.33000 18.68800  -44.01600 1.000 37.80265 ?  363 PHE B CE1 1 
ATOM   5480 C  CE2 . PHE B 1 383 ? -30.26000 19.71500  -43.45600 1.000 44.50314 ?  363 PHE B CE2 1 
ATOM   5481 C  CZ  . PHE B 1 383 ? -31.05800 19.06900  -44.37000 1.000 42.08461 ?  363 PHE B CZ  1 
ATOM   5482 N  N   . ARG B 1 384 ? -32.21900 23.10900  -39.51400 1.000 46.31640 ?  364 ARG B N   1 
ATOM   5483 C  CA  . ARG B 1 384 ? -31.47000 24.38500  -39.67400 1.000 48.09147 ?  364 ARG B CA  1 
ATOM   5484 C  C   . ARG B 1 384 ? -30.34800 24.42700  -38.63300 1.000 41.43132 ?  364 ARG B C   1 
ATOM   5485 O  O   . ARG B 1 384 ? -30.47100 23.72000  -37.62100 1.000 37.87537 ?  364 ARG B O   1 
ATOM   5486 C  CB  . ARG B 1 384 ? -32.41100 25.58000  -39.50200 1.000 47.02601 ?  364 ARG B CB  1 
ATOM   5487 N  N   . ALA B 1 385 ? -29.30200 25.22700  -38.86200 1.000 42.07218 ?  365 ALA B N   1 
ATOM   5488 C  CA  . ALA B 1 385 ? -28.18600 25.21900  -37.92700 1.000 35.71495 ?  365 ALA B CA  1 
ATOM   5489 C  C   . ALA B 1 385 ? -28.54900 25.94600  -36.63700 1.000 44.62007 ?  365 ALA B C   1 
ATOM   5490 O  O   . ALA B 1 385 ? -29.20100 26.99300  -36.65700 1.000 42.65047 ?  365 ALA B O   1 
ATOM   5491 C  CB  . ALA B 1 385 ? -26.96000 25.86700  -38.56600 1.000 45.84272 ?  365 ALA B CB  1 
ATOM   5492 N  N   . ALA B 1 386 ? -28.13200 25.37200  -35.50600 1.000 41.06543 ?  366 ALA B N   1 
ATOM   5493 C  CA  . ALA B 1 386 ? -28.25500 26.03100  -34.21100 1.000 40.79653 ?  366 ALA B CA  1 
ATOM   5494 C  C   . ALA B 1 386 ? -27.05300 26.89700  -33.88600 1.000 44.95887 ?  366 ALA B C   1 
ATOM   5495 O  O   . ALA B 1 386 ? -27.17300 27.84200  -33.09800 1.000 49.35979 ?  366 ALA B O   1 
ATOM   5496 C  CB  . ALA B 1 386 ? -28.42100 24.99800  -33.09200 1.000 41.21102 ?  366 ALA B CB  1 
ATOM   5497 N  N   . VAL B 1 387 ? -25.90500 26.58200  -34.46800 1.000 46.99227 ?  367 VAL B N   1 
ATOM   5498 C  CA  . VAL B 1 387 ? -24.64700 27.25100  -34.18800 1.000 52.52161 ?  367 VAL B CA  1 
ATOM   5499 C  C   . VAL B 1 387 ? -24.04000 27.67000  -35.51600 1.000 54.03926 ?  367 VAL B C   1 
ATOM   5500 O  O   . VAL B 1 387 ? -24.32000 27.07300  -36.56100 1.000 45.63062 ?  367 VAL B O   1 
ATOM   5501 C  CB  . VAL B 1 387 ? -23.66200 26.35200  -33.41900 1.000 47.50998 ?  367 VAL B CB  1 
ATOM   5502 N  N   . ASP B 1 388 ? -23.23800 28.73000  -35.48100 1.000 54.16761 ?  368 ASP B N   1 
ATOM   5503 C  CA  . ASP B 1 388 ? -22.46200 29.09600  -36.65600 1.000 53.06325 ?  368 ASP B CA  1 
ATOM   5504 C  C   . ASP B 1 388 ? -21.59000 27.91600  -37.06000 1.000 53.54878 ?  368 ASP B C   1 
ATOM   5505 O  O   . ASP B 1 388 ? -20.88200 27.34200  -36.22700 1.000 55.73722 ?  368 ASP B O   1 
ATOM   5506 C  CB  . ASP B 1 388 ? -21.60600 30.33100  -36.36600 1.000 59.51537 ?  368 ASP B CB  1 
ATOM   5507 C  CG  . ASP B 1 388 ? -20.98400 30.92200  -37.62200 1.000 63.32527 ?  368 ASP B CG  1 
ATOM   5508 O  OD1 . ASP B 1 388 ? -21.67600 30.98600  -38.65900 1.000 62.76949 -1 368 ASP B OD1 1 
ATOM   5509 O  OD2 . ASP B 1 388 ? -19.80200 31.32400  -37.57200 1.000 65.61020 -1 368 ASP B OD2 1 
ATOM   5510 N  N   . LEU B 1 389 ? -21.67200 27.53100  -38.33700 1.000 48.06361 ?  369 LEU B N   1 
ATOM   5511 C  CA  . LEU B 1 389 ? -20.90000 26.39200  -38.82300 1.000 41.46032 ?  369 LEU B CA  1 
ATOM   5512 C  C   . LEU B 1 389 ? -19.41700 26.54500  -38.51200 1.000 52.42773 ?  369 LEU B C   1 
ATOM   5513 O  O   . LEU B 1 389 ? -18.72100 25.54800  -38.28800 1.000 49.55028 ?  369 LEU B O   1 
ATOM   5514 C  CB  . LEU B 1 389 ? -21.10800 26.22200  -40.32800 1.000 49.22040 ?  369 LEU B CB  1 
ATOM   5515 C  CG  . LEU B 1 389 ? -22.55300 26.00400  -40.78300 1.000 43.33217 ?  369 LEU B CG  1 
ATOM   5516 C  CD1 . LEU B 1 389 ? -22.60300 25.73400  -42.27800 1.000 42.38563 ?  369 LEU B CD1 1 
ATOM   5517 C  CD2 . LEU B 1 389 ? -23.19700 24.86900  -40.00100 1.000 43.05369 ?  369 LEU B CD2 1 
ATOM   5518 N  N   . ALA B 1 390 ? -18.92200 27.78300  -38.47300 1.000 52.36362 ?  370 ALA B N   1 
ATOM   5519 C  CA  . ALA B 1 390 ? -17.53400 28.04400  -38.11800 1.000 50.98263 ?  370 ALA B CA  1 
ATOM   5520 C  C   . ALA B 1 390 ? -17.22500 27.74500  -36.65600 1.000 52.87466 ?  370 ALA B C   1 
ATOM   5521 O  O   . ALA B 1 390 ? -16.05600 27.82700  -36.26500 1.000 57.81499 ?  370 ALA B O   1 
ATOM   5522 N  N   . ASP B 1 391 ? -18.22800 27.41200  -35.84300 1.000 53.21226 ?  371 ASP B N   1 
ATOM   5523 C  CA  . ASP B 1 391 ? -18.01300 27.02200  -34.45500 1.000 57.07560 ?  371 ASP B CA  1 
ATOM   5524 C  C   . ASP B 1 391 ? -18.08100 25.51200  -34.25500 1.000 49.62835 ?  371 ASP B C   1 
ATOM   5525 O  O   . ASP B 1 391 ? -18.08300 25.04600  -33.11000 1.000 51.41297 ?  371 ASP B O   1 
ATOM   5526 C  CB  . ASP B 1 391 ? -19.02300 27.71900  -33.53800 1.000 61.60372 ?  371 ASP B CB  1 
ATOM   5527 C  CG  . ASP B 1 391 ? -18.99400 29.23100  -33.67900 1.000 63.87252 ?  371 ASP B CG  1 
ATOM   5528 O  OD1 . ASP B 1 391 ? -18.05000 29.75200  -34.31000 1.000 66.84163 -1 371 ASP B OD1 1 
ATOM   5529 O  OD2 . ASP B 1 391 ? -19.90900 29.89800  -33.15200 1.000 64.33751 -1 371 ASP B OD2 1 
ATOM   5530 N  N   . LEU B 1 392 ? -18.13700 24.75200  -35.34400 1.000 46.48706 ?  372 LEU B N   1 
ATOM   5531 C  CA  . LEU B 1 392 ? -18.17800 23.27000  -35.25800 1.000 43.96639 ?  372 LEU B CA  1 
ATOM   5532 C  C   . LEU B 1 392 ? -16.77100 22.70300  -35.03600 1.000 47.92071 ?  372 LEU B C   1 
ATOM   5533 O  O   . LEU B 1 392 ? -15.79700 23.37600  -35.41500 1.000 44.60089 ?  372 LEU B O   1 
ATOM   5534 C  CB  . LEU B 1 392 ? -18.79200 22.70700  -36.53700 1.000 36.53286 ?  372 LEU B CB  1 
ATOM   5535 C  CG  . LEU B 1 392 ? -20.29400 22.93300  -36.68600 1.000 46.15332 ?  372 LEU B CG  1 
ATOM   5536 C  CD1 . LEU B 1 392 ? -20.79500 22.39100  -38.01300 1.000 34.88384 ?  372 LEU B CD1 1 
ATOM   5537 C  CD2 . LEU B 1 392 ? -21.05400 22.30600  -35.52900 1.000 39.76392 ?  372 LEU B CD2 1 
ATOM   5538 N  N   . GLN B 1 393 ? -16.68700 21.50800  -34.44900 1.000 37.75859 ?  373 GLN B N   1 
ATOM   5539 C  CA  . GLN B 1 393 ? -15.37000 20.88200  -34.14600 1.000 43.38655 ?  373 GLN B CA  1 
ATOM   5540 C  C   . GLN B 1 393 ? -15.30000 19.50200  -34.79700 1.000 49.00380 ?  373 GLN B C   1 
ATOM   5541 O  O   . GLN B 1 393 ? -16.32500 18.81100  -34.80200 1.000 44.60825 ?  373 GLN B O   1 
ATOM   5542 C  CB  . GLN B 1 393 ? -15.11400 20.80100  -32.64200 1.000 43.87870 ?  373 GLN B CB  1 
ATOM   5543 C  CG  . GLN B 1 393 ? -14.73200 22.13100  -32.01300 1.000 48.91299 ?  373 GLN B CG  1 
ATOM   5544 C  CD  . GLN B 1 393 ? -14.36700 21.98600  -30.55600 1.000 44.72417 ?  373 GLN B CD  1 
ATOM   5545 N  N   . TRP B 1 394 ? -14.13100 19.15100  -35.33400 1.000 45.20092 ?  374 TRP B N   1 
ATOM   5546 C  CA  . TRP B 1 394 ? -13.94100 17.85500  -36.03300 1.000 43.45405 ?  374 TRP B CA  1 
ATOM   5547 C  C   . TRP B 1 394 ? -13.18600 16.85200  -35.15100 1.000 41.80734 ?  374 TRP B C   1 
ATOM   5548 O  O   . TRP B 1 394 ? -12.46600 17.28500  -34.24100 1.000 40.23479 ?  374 TRP B O   1 
ATOM   5549 C  CB  . TRP B 1 394 ? -13.22900 18.09900  -37.35300 1.000 41.43683 ?  374 TRP B CB  1 
ATOM   5550 C  CG  . TRP B 1 394 ? -14.01200 18.96400  -38.28400 1.000 46.40156 ?  374 TRP B CG  1 
ATOM   5551 C  CD1 . TRP B 1 394 ? -14.05400 20.32700  -38.30800 1.000 48.27426 ?  374 TRP B CD1 1 
ATOM   5552 C  CD2 . TRP B 1 394 ? -14.88200 18.51500  -39.33400 1.000 43.74148 ?  374 TRP B CD2 1 
ATOM   5553 N  NE1 . TRP B 1 394 ? -14.88900 20.75600  -39.30200 1.000 48.43557 ?  374 TRP B NE1 1 
ATOM   5554 C  CE2 . TRP B 1 394 ? -15.40900 19.66800  -39.94900 1.000 47.77244 ?  374 TRP B CE2 1 
ATOM   5555 C  CE3 . TRP B 1 394 ? -15.26400 17.25900  -39.81100 1.000 44.43084 ?  374 TRP B CE3 1 
ATOM   5556 C  CZ2 . TRP B 1 394 ? -16.29900 19.59700  -41.01700 1.000 44.93596 ?  374 TRP B CZ2 1 
ATOM   5557 C  CZ3 . TRP B 1 394 ? -16.14300 17.19100  -40.86800 1.000 41.56416 ?  374 TRP B CZ3 1 
ATOM   5558 C  CH2 . TRP B 1 394 ? -16.65200 18.34400  -41.46100 1.000 43.58690 ?  374 TRP B CH2 1 
ATOM   5559 N  N   . GLN B 1 395 ? -13.37900 15.56200  -35.41300 1.000 38.68914 ?  375 GLN B N   1 
ATOM   5560 C  CA  . GLN B 1 395 ? -12.72800 14.49500  -34.62200 1.000 39.95847 ?  375 GLN B CA  1 
ATOM   5561 C  C   . GLN B 1 395 ? -11.22400 14.50900  -34.85500 1.000 36.86279 ?  375 GLN B C   1 
ATOM   5562 O  O   . GLN B 1 395 ? -10.80800 14.72800  -35.99500 1.000 36.59882 ?  375 GLN B O   1 
ATOM   5563 C  CB  . GLN B 1 395 ? -13.25200 13.12800  -35.05700 1.000 36.23526 ?  375 GLN B CB  1 
ATOM   5564 C  CG  . GLN B 1 395 ? -14.67900 12.83600  -34.61500 1.000 40.59376 ?  375 GLN B CG  1 
ATOM   5565 C  CD  . GLN B 1 395 ? -14.92900 13.22500  -33.18000 1.000 42.79453 ?  375 GLN B CD  1 
ATOM   5566 N  N   . PRO B 1 396 ? -10.40500 14.26700  -33.81200 1.000 39.66977 ?  376 PRO B N   1 
ATOM   5567 C  CA  . PRO B 1 396 ? -8.96500  14.12900  -34.00000 1.000 45.72405 ?  376 PRO B CA  1 
ATOM   5568 C  C   . PRO B 1 396 ? -8.66600  12.76300  -34.63300 1.000 45.04026 ?  376 PRO B C   1 
ATOM   5569 O  O   . PRO B 1 396 ? -8.44200  11.83600  -33.90500 1.000 47.70632 ?  376 PRO B O   1 
ATOM   5570 C  CB  . PRO B 1 396 ? -8.40500  14.14100  -32.57600 1.000 43.56737 ?  376 PRO B CB  1 
ATOM   5571 C  CG  . PRO B 1 396 ? -9.55500  14.57300  -31.69200 1.000 46.05977 ?  376 PRO B CG  1 
ATOM   5572 C  CD  . PRO B 1 396 ? -10.81200 14.15200  -32.41900 1.000 38.73138 ?  376 PRO B CD  1 
ATOM   5573 N  N   . SER B 1 397 ? -8.73700  12.66300  -35.95200 1.000 41.10816 ?  377 SER B N   1 
ATOM   5574 C  CA  . SER B 1 397 ? -8.45500  11.41500  -36.64400 1.000 43.40321 ?  377 SER B CA  1 
ATOM   5575 C  C   . SER B 1 397 ? -7.76900  11.71600  -37.96700 1.000 49.00107 ?  377 SER B C   1 
ATOM   5576 O  O   . SER B 1 397 ? -7.96400  12.78000  -38.56100 1.000 49.09199 ?  377 SER B O   1 
ATOM   5577 C  CB  . SER B 1 397 ? -9.72900  10.59400  -36.88000 1.000 44.09070 ?  377 SER B CB  1 
ATOM   5578 O  OG  . SER B 1 397 ? -9.44600  9.40200   -37.59500 1.000 43.62164 ?  377 SER B OG  1 
ATOM   5579 N  N   . PHE B 1 398 ? -6.96700  10.75500  -38.42200 1.000 41.98155 ?  378 PHE B N   1 
ATOM   5580 C  CA  . PHE B 1 398 ? -6.20700  10.88100  -39.65500 1.000 45.83731 ?  378 PHE B CA  1 
ATOM   5581 C  C   . PHE B 1 398 ? -6.87800  10.17700  -40.82700 1.000 40.03361 ?  378 PHE B C   1 
ATOM   5582 O  O   . PHE B 1 398 ? -6.59700  10.51700  -41.98100 1.000 37.60081 ?  378 PHE B O   1 
ATOM   5583 C  CB  . PHE B 1 398 ? -4.78900  10.33000  -39.42400 1.000 43.38465 ?  378 PHE B CB  1 
ATOM   5584 C  CG  . PHE B 1 398 ? -3.92400  10.27100  -40.65700 1.000 46.00231 ?  378 PHE B CG  1 
ATOM   5585 C  CD1 . PHE B 1 398 ? -3.46400  11.43300  -41.25800 1.000 47.70031 ?  378 PHE B CD1 1 
ATOM   5586 C  CD2 . PHE B 1 398 ? -3.51900  9.04800   -41.17800 1.000 40.84335 ?  378 PHE B CD2 1 
ATOM   5587 C  CE1 . PHE B 1 398 ? -2.64900  11.38100  -42.37900 1.000 47.47434 ?  378 PHE B CE1 1 
ATOM   5588 C  CE2 . PHE B 1 398 ? -2.70200  8.98700   -42.29600 1.000 40.87592 ?  378 PHE B CE2 1 
ATOM   5589 C  CZ  . PHE B 1 398 ? -2.26600  10.15700  -42.89800 1.000 38.97402 ?  378 PHE B CZ  1 
ATOM   5590 N  N   . ARG B 1 399 ? -7.78700  9.24200   -40.56000 1.000 35.82263 ?  379 ARG B N   1 
ATOM   5591 C  CA  . ARG B 1 399 ? -8.43700  8.47400   -41.61100 1.000 40.79357 ?  379 ARG B CA  1 
ATOM   5592 C  C   . ARG B 1 399 ? -9.94300  8.68900   -41.69900 1.000 35.26766 ?  379 ARG B C   1 
ATOM   5593 O  O   . ARG B 1 399 ? -10.50100 8.54700   -42.78900 1.000 37.83956 ?  379 ARG B O   1 
ATOM   5594 C  CB  . ARG B 1 399 ? -8.14600  6.97300   -41.42400 1.000 35.27387 ?  379 ARG B CB  1 
ATOM   5595 C  CG  . ARG B 1 399 ? -8.71900  6.07400   -42.51700 1.000 35.05036 ?  379 ARG B CG  1 
ATOM   5596 C  CD  . ARG B 1 399 ? -8.17200  4.65700   -42.43300 1.000 34.19706 ?  379 ARG B CD  1 
ATOM   5597 N  NE  . ARG B 1 399 ? -8.91200  3.81200   -41.50200 1.000 40.72501 ?  379 ARG B NE  1 
ATOM   5598 C  CZ  . ARG B 1 399 ? -8.55200  2.57900   -41.17200 1.000 36.02755 ?  379 ARG B CZ  1 
ATOM   5599 N  NH1 . ARG B 1 399 ? -7.46400  2.02000   -41.67500 1.000 35.80170 ?  379 ARG B NH1 1 
ATOM   5600 N  NH2 . ARG B 1 399 ? -9.30100  1.88900   -40.31500 1.000 42.41642 ?  379 ARG B NH2 1 
ATOM   5601 N  N   . ASN B 1 400 ? -10.61400 9.04200   -40.60200 1.000 36.52064 ?  380 ASN B N   1 
ATOM   5602 C  CA  . ASN B 1 400 ? -12.07000 9.17500   -40.58900 1.000 36.14220 ?  380 ASN B CA  1 
ATOM   5603 C  C   . ASN B 1 400 ? -12.46300 10.57600  -40.13900 1.000 41.94992 ?  380 ASN B C   1 
ATOM   5604 O  O   . ASN B 1 400 ? -12.39000 10.90100  -38.95000 1.000 43.46278 ?  380 ASN B O   1 
ATOM   5605 C  CB  . ASN B 1 400 ? -12.70400 8.10800   -39.70200 1.000 44.38276 ?  380 ASN B CB  1 
ATOM   5606 C  CG  . ASN B 1 400 ? -12.83100 6.77500   -40.41100 1.000 41.25677 ?  380 ASN B CG  1 
ATOM   5607 O  OD1 . ASN B 1 400 ? -11.83500 6.10200   -40.67800 1.000 41.58905 ?  380 ASN B OD1 1 
ATOM   5608 N  ND2 . ASN B 1 400 ? -14.06100 6.39200   -40.72900 1.000 36.26388 ?  380 ASN B ND2 1 
ATOM   5609 N  N   . ARG B 1 401 ? -12.90600 11.38400  -41.10100 1.000 35.59421 ?  381 ARG B N   1 
ATOM   5610 C  CA  . ARG B 1 401 ? -13.31500 12.76000  -40.86300 1.000 34.59900 ?  381 ARG B CA  1 
ATOM   5611 C  C   . ARG B 1 401 ? -14.77000 12.80900  -40.40500 1.000 32.48377 ?  381 ARG B C   1 
ATOM   5612 O  O   . ARG B 1 401 ? -15.64800 12.21000  -41.03400 1.000 33.25177 ?  381 ARG B O   1 
ATOM   5613 C  CB  . ARG B 1 401 ? -13.12600 13.56400  -42.14900 1.000 39.12397 ?  381 ARG B CB  1 
ATOM   5614 C  CG  . ARG B 1 401 ? -13.50000 15.03300  -42.09000 1.000 44.25366 ?  381 ARG B CG  1 
ATOM   5615 C  CD  . ARG B 1 401 ? -12.97500 15.73100  -43.34500 1.000 45.58314 ?  381 ARG B CD  1 
ATOM   5616 N  NE  . ARG B 1 401 ? -13.55100 17.05400  -43.55100 1.000 40.80934 ?  381 ARG B NE  1 
ATOM   5617 C  CZ  . ARG B 1 401 ? -13.22600 18.13400  -42.85400 1.000 46.84888 ?  381 ARG B CZ  1 
ATOM   5618 N  NH1 . ARG B 1 401 ? -12.35100 18.08000  -41.86200 1.000 49.10060 ?  381 ARG B NH1 1 
ATOM   5619 N  NH2 . ARG B 1 401 ? -13.79600 19.29600  -43.15500 1.000 49.78360 ?  381 ARG B NH2 1 
ATOM   5620 N  N   . GLY B 1 402 ? -15.02200 13.52400  -39.31600 1.000 29.90876 ?  382 GLY B N   1 
ATOM   5621 C  CA  . GLY B 1 402 ? -16.37000 13.64000  -38.79400 1.000 31.99981 ?  382 GLY B CA  1 
ATOM   5622 C  C   . GLY B 1 402 ? -16.42900 14.66200  -37.68500 1.000 34.18400 ?  382 GLY B C   1 
ATOM   5623 O  O   . GLY B 1 402 ? -15.42400 14.95700  -37.03000 1.000 31.92068 ?  382 GLY B O   1 
ATOM   5624 N  N   . LEU B 1 403 ? -17.63000 15.19400  -37.47400 1.000 32.50766 ?  383 LEU B N   1 
ATOM   5625 C  CA  . LEU B 1 403 ? -17.82500 16.24800  -36.49200 1.000 33.11271 ?  383 LEU B CA  1 
ATOM   5626 C  C   . LEU B 1 403 ? -18.01100 15.66300  -35.09700 1.000 32.59978 ?  383 LEU B C   1 
ATOM   5627 O  O   . LEU B 1 403 ? -18.50000 14.54200  -34.92900 1.000 34.75057 ?  383 LEU B O   1 
ATOM   5628 C  CB  . LEU B 1 403 ? -19.04000 17.10500  -36.85600 1.000 36.72968 ?  383 LEU B CB  1 
ATOM   5629 C  CG  . LEU B 1 403 ? -18.94100 17.86800  -38.17700 1.000 35.70264 ?  383 LEU B CG  1 
ATOM   5630 C  CD1 . LEU B 1 403 ? -20.28700 17.90000  -38.88300 1.000 36.30608 ?  383 LEU B CD1 1 
ATOM   5631 C  CD2 . LEU B 1 403 ? -18.41300 19.28000  -37.94500 1.000 42.09763 ?  383 LEU B CD2 1 
ATOM   5632 N  N   . THR B 1 404 ? -17.60500 16.43900  -34.08700 1.000 31.18159 ?  384 THR B N   1 
ATOM   5633 C  CA  . THR B 1 404 ? -17.88800 16.04800  -32.71100 1.000 36.66211 ?  384 THR B CA  1 
ATOM   5634 C  C   . THR B 1 404 ? -19.38000 16.12300  -32.41700 1.000 37.22779 ?  384 THR B C   1 
ATOM   5635 O  O   . THR B 1 404 ? -19.90300 15.31300  -31.64400 1.000 39.56741 ?  384 THR B O   1 
ATOM   5636 C  CB  . THR B 1 404 ? -17.12900 16.94100  -31.72700 1.000 40.72341 ?  384 THR B CB  1 
ATOM   5637 O  OG1 . THR B 1 404 ? -17.65800 18.27100  -31.78200 1.000 38.68581 ?  384 THR B OG1 1 
ATOM   5638 C  CG2 . THR B 1 404 ? -15.65000 16.98100  -32.08000 1.000 40.89820 ?  384 THR B CG2 1 
ATOM   5639 N  N   . GLU B 1 405 ? -20.07000 17.07900  -33.03000 1.000 35.62069 ?  385 GLU B N   1 
ATOM   5640 C  CA  . GLU B 1 405 ? -21.48900 17.32200  -32.81900 1.000 34.71320 ?  385 GLU B CA  1 
ATOM   5641 C  C   . GLU B 1 405 ? -21.96800 18.22800  -33.94100 1.000 36.17900 ?  385 GLU B C   1 
ATOM   5642 O  O   . GLU B 1 405 ? -21.16300 18.84500  -34.64300 1.000 37.93880 ?  385 GLU B O   1 
ATOM   5643 C  CB  . GLU B 1 405 ? -21.75600 17.96000  -31.44900 1.000 39.19351 ?  385 GLU B CB  1 
ATOM   5644 C  CG  . GLU B 1 405 ? -21.44900 19.45200  -31.39300 1.000 42.91591 ?  385 GLU B CG  1 
ATOM   5645 C  CD  . GLU B 1 405 ? -21.45700 20.00200  -29.98000 1.000 47.44236 ?  385 GLU B CD  1 
ATOM   5646 O  OE1 . GLU B 1 405 ? -20.51600 19.69600  -29.21900 1.000 61.88431 ?  385 GLU B OE1 1 
ATOM   5647 O  OE2 . GLU B 1 405 ? -22.39800 20.74500  -29.63100 1.000 49.22614 -1 385 GLU B OE2 1 
ATOM   5648 N  N   . LEU B 1 406 ? -23.28700 18.29900  -34.11100 1.000 38.05421 ?  386 LEU B N   1 
ATOM   5649 C  CA  . LEU B 1 406 ? -23.88600 19.18400  -35.10900 1.000 36.92660 ?  386 LEU B CA  1 
ATOM   5650 C  C   . LEU B 1 406 ? -25.19100 19.71800  -34.53500 1.000 37.38355 ?  386 LEU B C   1 
ATOM   5651 O  O   . LEU B 1 406 ? -26.25800 19.11500  -34.71100 1.000 32.94514 ?  386 LEU B O   1 
ATOM   5652 C  CB  . LEU B 1 406 ? -24.10900 18.46000  -36.43800 1.000 29.60869 ?  386 LEU B CB  1 
ATOM   5653 C  CG  . LEU B 1 406 ? -24.79600 19.22800  -37.57500 1.000 42.45240 ?  386 LEU B CG  1 
ATOM   5654 C  CD1 . LEU B 1 406 ? -23.97000 20.43000  -38.02000 1.000 42.84385 ?  386 LEU B CD1 1 
ATOM   5655 C  CD2 . LEU B 1 406 ? -25.07300 18.30800  -38.75000 1.000 46.27662 ?  386 LEU B CD2 1 
ATOM   5656 N  N   . PRO B 1 407 ? -25.16800 20.86900  -33.81000 1.000 35.39808 ?  387 PRO B N   1 
ATOM   5657 C  CA  . PRO B 1 407 ? -26.36400 21.40900  -33.17800 1.000 37.23500 ?  387 PRO B CA  1 
ATOM   5658 C  C   . PRO B 1 407 ? -27.35300 21.86200  -34.25800 1.000 43.87213 ?  387 PRO B C   1 
ATOM   5659 O  O   . PRO B 1 407 ? -27.02900 22.74100  -35.02700 1.000 42.66331 ?  387 PRO B O   1 
ATOM   5660 C  CB  . PRO B 1 407 ? -25.88400 22.59500  -32.31700 1.000 44.59420 ?  387 PRO B CB  1 
ATOM   5661 C  CG  . PRO B 1 407 ? -24.39700 22.41100  -32.21200 1.000 39.27901 ?  387 PRO B CG  1 
ATOM   5662 C  CD  . PRO B 1 407 ? -24.03200 21.77400  -33.53200 1.000 39.14288 ?  387 PRO B CD  1 
ATOM   5663 N  N   . LEU B 1 408 ? -28.53000 21.24300  -34.28400 1.000 38.96697 ?  388 LEU B N   1 
ATOM   5664 C  CA  . LEU B 1 408 ? -29.52600 21.55800  -35.33100 1.000 38.84771 ?  388 LEU B CA  1 
ATOM   5665 C  C   . LEU B 1 408 ? -30.81600 22.07600  -34.71500 1.000 45.43473 ?  388 LEU B C   1 
ATOM   5666 O  O   . LEU B 1 408 ? -31.02600 21.87700  -33.51000 1.000 46.17531 ?  388 LEU B O   1 
ATOM   5667 C  CB  . LEU B 1 408 ? -29.84100 20.29200  -36.12200 1.000 42.84290 ?  388 LEU B CB  1 
ATOM   5668 C  CG  . LEU B 1 408 ? -28.81400 19.90800  -37.18300 1.000 40.78538 ?  388 LEU B CG  1 
ATOM   5669 C  CD1 . LEU B 1 408 ? -29.40500 18.90700  -38.16000 1.000 40.65562 ?  388 LEU B CD1 1 
ATOM   5670 C  CD2 . LEU B 1 408 ? -28.31800 21.13800  -37.91900 1.000 39.18873 ?  388 LEU B CD2 1 
ATOM   5671 N  N   . LEU B 1 409 ? -31.62700 22.72100  -35.53700 1.000 45.35879 ?  389 LEU B N   1 
ATOM   5672 C  CA  . LEU B 1 409 ? -32.96000 23.16800  -35.09000 1.000 45.11115 ?  389 LEU B CA  1 
ATOM   5673 C  C   . LEU B 1 409 ? -33.94700 22.46400  -36.01300 1.000 41.82895 ?  389 LEU B C   1 
ATOM   5674 O  O   . LEU B 1 409 ? -33.86000 22.68400  -37.22200 1.000 42.87149 ?  389 LEU B O   1 
ATOM   5675 C  CB  . LEU B 1 409 ? -33.04000 24.68800  -35.22700 1.000 44.43554 ?  389 LEU B CB  1 
ATOM   5676 C  CG  . LEU B 1 409 ? -32.31000 25.47900  -34.14800 1.000 49.89803 ?  389 LEU B CG  1 
ATOM   5677 C  CD1 . LEU B 1 409 ? -32.36400 26.96700  -34.45300 1.000 50.40815 ?  389 LEU B CD1 1 
ATOM   5678 C  CD2 . LEU B 1 409 ? -32.90300 25.19200  -32.78000 1.000 49.69459 ?  389 LEU B CD2 1 
ATOM   5679 N  N   . LEU B 1 410 ? -34.78100 21.58800  -35.45300 1.000 41.79148 ?  390 LEU B N   1 
ATOM   5680 C  CA  . LEU B 1 410 ? -35.74700 20.81600  -36.27100 1.000 42.57411 ?  390 LEU B CA  1 
ATOM   5681 C  C   . LEU B 1 410 ? -37.07700 21.57100  -36.37200 1.000 44.01501 ?  390 LEU B C   1 
ATOM   5682 O  O   . LEU B 1 410 ? -37.35300 22.40000  -35.50100 1.000 49.24904 ?  390 LEU B O   1 
ATOM   5683 C  CB  . LEU B 1 410 ? -35.94200 19.43400  -35.64800 1.000 39.35042 ?  390 LEU B CB  1 
ATOM   5684 C  CG  . LEU B 1 410 ? -34.71300 18.53200  -35.68200 1.000 42.35729 ?  390 LEU B CG  1 
ATOM   5685 C  CD1 . LEU B 1 410 ? -35.01200 17.18300  -35.05200 1.000 36.10694 ?  390 LEU B CD1 1 
ATOM   5686 C  CD2 . LEU B 1 410 ? -34.20600 18.36400  -37.10300 1.000 38.71078 ?  390 LEU B CD2 1 
ATOM   5687 N  N   . GLY B 1 411 ? -37.84700 21.29500  -37.41800 1.000 45.09335 ?  391 GLY B N   1 
ATOM   5688 C  CA  . GLY B 1 411 ? -39.14400 21.97300  -37.61200 1.000 54.93280 ?  391 GLY B CA  1 
ATOM   5689 C  C   . GLY B 1 411 ? -40.30800 21.01900  -37.42400 1.000 52.73714 ?  391 GLY B C   1 
ATOM   5690 O  O   . GLY B 1 411 ? -40.33400 20.31600  -36.43300 1.000 54.60849 ?  391 GLY B O   1 
ATOM   5691 O  OXT . GLY B 1 411 ? -41.18100 21.00800  -38.30000 1.000 59.78475 -1 391 GLY B OXT 1 
HETATM 5692 C  CHA . HEM C 2 .   ? -1.89400  -11.14700 -11.93100 1.000 14.15047 ?  401 HEM A CHA 1 
HETATM 5693 C  CHB . HEM C 2 .   ? 2.28600   -11.10300 -14.37300 1.000 20.38456 ?  401 HEM A CHB 1 
HETATM 5694 C  CHC . HEM C 2 .   ? 3.64200   -7.07700  -11.97900 1.000 14.27803 ?  401 HEM A CHC 1 
HETATM 5695 C  CHD . HEM C 2 .   ? -0.52100  -7.16800  -9.53100  1.000 13.48804 ?  401 HEM A CHD 1 
HETATM 5696 C  C1A . HEM C 2 .   ? -0.87600  -11.43100 -12.80500 1.000 16.91503 ?  401 HEM A C1A 1 
HETATM 5697 C  C2A . HEM C 2 .   ? -0.92700  -12.46900 -13.74800 1.000 17.16879 ?  401 HEM A C2A 1 
HETATM 5698 C  C3A . HEM C 2 .   ? 0.24000   -12.46700 -14.43400 1.000 21.66410 ?  401 HEM A C3A 1 
HETATM 5699 C  C4A . HEM C 2 .   ? 1.02700   -11.42200 -13.92200 1.000 16.52600 ?  401 HEM A C4A 1 
HETATM 5700 C  CMA . HEM C 2 .   ? 0.62600   -13.40400 -15.54500 1.000 22.13183 ?  401 HEM A CMA 1 
HETATM 5701 C  CAA . HEM C 2 .   ? -2.07100  -13.42000 -13.95200 1.000 11.55326 ?  401 HEM A CAA 1 
HETATM 5702 C  CBA . HEM C 2 .   ? -1.87700  -14.58400 -12.98400 1.000 10.84675 ?  401 HEM A CBA 1 
HETATM 5703 C  CGA . HEM C 2 .   ? -3.07400  -15.49100 -13.02300 1.000 18.61152 ?  401 HEM A CGA 1 
HETATM 5704 O  O1A . HEM C 2 .   ? -2.92500  -16.71400 -12.83000 1.000 18.95221 ?  401 HEM A O1A 1 
HETATM 5705 O  O2A . HEM C 2 .   ? -4.20900  -15.02800 -13.24900 1.000 14.11261 ?  401 HEM A O2A 1 
HETATM 5706 C  C1B . HEM C 2 .   ? 2.97800   -9.98700  -13.90100 1.000 16.58495 ?  401 HEM A C1B 1 
HETATM 5707 C  C2B . HEM C 2 .   ? 4.24900   -9.63700  -14.41700 1.000 19.90827 ?  401 HEM A C2B 1 
HETATM 5708 C  C3B . HEM C 2 .   ? 4.66000   -8.51900  -13.77000 1.000 22.16008 ?  401 HEM A C3B 1 
HETATM 5709 C  C4B . HEM C 2 .   ? 3.58000   -8.18300  -12.81900 1.000 14.22853 ?  401 HEM A C4B 1 
HETATM 5710 C  CMB . HEM C 2 .   ? 5.01200   -10.36800 -15.48400 1.000 23.30879 ?  401 HEM A CMB 1 
HETATM 5711 C  CAB . HEM C 2 .   ? 5.92700   -7.80200  -13.99000 1.000 26.32370 ?  401 HEM A CAB 1 
HETATM 5712 C  CBB . HEM C 2 .   ? 6.81200   -7.64900  -13.01900 1.000 29.04714 ?  401 HEM A CBB 1 
HETATM 5713 C  C1C . HEM C 2 .   ? 2.59300   -6.71800  -11.15900 1.000 16.10373 ?  401 HEM A C1C 1 
HETATM 5714 C  C2C . HEM C 2 .   ? 2.50500   -5.50500  -10.46900 1.000 17.24967 ?  401 HEM A C2C 1 
HETATM 5715 C  C3C . HEM C 2 .   ? 1.31300   -5.52600  -9.76600  1.000 17.38770 ?  401 HEM A C3C 1 
HETATM 5716 C  C4C . HEM C 2 .   ? 0.68200   -6.76900  -10.04500 1.000 15.38681 ?  401 HEM A C4C 1 
HETATM 5717 C  CMC . HEM C 2 .   ? 3.53300   -4.40100  -10.49900 1.000 19.72938 ?  401 HEM A CMC 1 
HETATM 5718 C  CAC . HEM C 2 .   ? 0.79500   -4.45900  -8.89100  1.000 17.41066 ?  401 HEM A CAC 1 
HETATM 5719 C  CBC . HEM C 2 .   ? 1.35200   -4.24600  -7.70300  1.000 32.80516 ?  401 HEM A CBC 1 
HETATM 5720 C  C1D . HEM C 2 .   ? -1.20600  -8.27700  -10.01800 1.000 14.35395 ?  401 HEM A C1D 1 
HETATM 5721 C  C2D . HEM C 2 .   ? -2.53600  -8.62900  -9.51200  1.000 11.25125 ?  401 HEM A C2D 1 
HETATM 5722 C  C3D . HEM C 2 .   ? -2.91800  -9.72900  -10.18200 1.000 11.44228 ?  401 HEM A C3D 1 
HETATM 5723 C  C4D . HEM C 2 .   ? -1.81800  -10.05100 -11.09000 1.000 12.42235 ?  401 HEM A C4D 1 
HETATM 5724 C  CMD . HEM C 2 .   ? -3.31400  -7.89200  -8.45600  1.000 13.44200 ?  401 HEM A CMD 1 
HETATM 5725 C  CAD . HEM C 2 .   ? -4.20200  -10.50300 -10.03100 1.000 15.34357 ?  401 HEM A CAD 1 
HETATM 5726 C  CBD . HEM C 2 .   ? -5.39300  -9.80300  -10.68400 1.000 9.53952  ?  401 HEM A CBD 1 
HETATM 5727 C  CGD . HEM C 2 .   ? -6.65900  -10.42400 -10.14700 1.000 18.33706 ?  401 HEM A CGD 1 
HETATM 5728 O  O1D . HEM C 2 .   ? -7.76500  -9.89400  -10.37800 1.000 12.99610 ?  401 HEM A O1D 1 
HETATM 5729 O  O2D . HEM C 2 .   ? -6.60700  -11.47300 -9.46700  1.000 16.82851 ?  401 HEM A O2D 1 
HETATM 5730 N  NA  . HEM C 2 .   ? 0.33200   -10.79300 -12.92600 1.000 17.45594 ?  401 HEM A NA  1 
HETATM 5731 N  NB  . HEM C 2 .   ? 2.61200   -9.10800  -12.95700 1.000 22.74043 ?  401 HEM A NB  1 
HETATM 5732 N  NC  . HEM C 2 .   ? 1.48500   -7.47300  -10.89800 1.000 14.82730 ?  401 HEM A NC  1 
HETATM 5733 N  ND  . HEM C 2 .   ? -0.82900  -9.15200  -10.96000 1.000 7.63087  ?  401 HEM A ND  1 
HETATM 5734 FE FE  . HEM C 2 .   ? 0.78900   -9.16400  -11.89900 1.000 15.95353 ?  401 HEM A FE  1 
HETATM 5735 C  C   . FMT D 3 .   ? 22.08300  -4.38700  -20.07500 1.000 30.41480 ?  402 FMT A C   1 
HETATM 5736 O  O1  . FMT D 3 .   ? 22.22700  -3.55600  -20.97800 1.000 23.25741 ?  402 FMT A O1  1 
HETATM 5737 O  O2  . FMT D 3 .   ? 22.52000  -5.53900  -20.11400 1.000 37.40443 ?  402 FMT A O2  1 
HETATM 5738 C  C1  . 1BO E 4 .   ? -13.09900 -16.71600 -21.56400 1.000 34.99961 ?  403 1BO A C1  1 
HETATM 5739 C  C2  . 1BO E 4 .   ? -14.36300 -17.54300 -21.33600 1.000 31.46544 ?  403 1BO A C2  1 
HETATM 5740 C  C3  . 1BO E 4 .   ? -15.59000 -16.77100 -21.81900 1.000 26.27992 ?  403 1BO A C3  1 
HETATM 5741 C  C4  . 1BO E 4 .   ? -16.75800 -17.74400 -21.98600 1.000 35.33987 ?  403 1BO A C4  1 
HETATM 5742 O  OH  . 1BO E 4 .   ? -17.72100 -17.20000 -22.84900 1.000 38.51457 ?  403 1BO A OH  1 
HETATM 5743 C  C1  . 1BO F 4 .   ? -2.83500  -5.14100  -22.40000 1.000 29.44499 ?  404 1BO A C1  1 
HETATM 5744 C  C2  . 1BO F 4 .   ? -3.92500  -4.36900  -21.69400 1.000 28.82252 ?  404 1BO A C2  1 
HETATM 5745 C  C3  . 1BO F 4 .   ? -5.04000  -3.94700  -22.61000 1.000 32.40073 ?  404 1BO A C3  1 
HETATM 5746 C  C4  . 1BO F 4 .   ? -4.74200  -4.15000  -24.07300 1.000 40.89402 ?  404 1BO A C4  1 
HETATM 5747 O  OH  . 1BO F 4 .   ? -5.35200  -5.31500  -24.58900 1.000 47.22921 ?  404 1BO A OH  1 
HETATM 5748 C  C   . FMT G 3 .   ? 11.31800  -9.05400  -0.16800  1.000 34.97513 ?  405 FMT A C   1 
HETATM 5749 O  O1  . FMT G 3 .   ? 12.53800  -9.20700  -0.10600  1.000 34.14586 ?  405 FMT A O1  1 
HETATM 5750 O  O2  . FMT G 3 .   ? 10.68600  -8.29500  0.56600   1.000 35.42265 ?  405 FMT A O2  1 
HETATM 5751 C  CHA . HEM H 2 .   ? -14.49400 -2.55400  -47.61600 1.000 25.62520 ?  401 HEM B CHA 1 
HETATM 5752 C  CHB . HEM H 2 .   ? -18.68300 -3.52000  -45.37500 1.000 26.13944 ?  401 HEM B CHB 1 
HETATM 5753 C  CHC . HEM H 2 .   ? -20.13600 1.05600   -46.17300 1.000 30.38553 ?  401 HEM B CHC 1 
HETATM 5754 C  CHD . HEM H 2 .   ? -15.75800 2.10600   -47.88300 1.000 29.40058 ?  401 HEM B CHD 1 
HETATM 5755 C  C1A . HEM H 2 .   ? -15.52200 -3.18200  -46.96000 1.000 30.50465 ?  401 HEM B C1A 1 
HETATM 5756 C  C2A . HEM H 2 .   ? -15.50600 -4.54100  -46.60700 1.000 27.80204 ?  401 HEM B C2A 1 
HETATM 5757 C  C3A . HEM H 2 .   ? -16.67500 -4.82000  -45.98200 1.000 29.73473 ?  401 HEM B C3A 1 
HETATM 5758 C  C4A . HEM H 2 .   ? -17.43000 -3.63500  -45.93600 1.000 34.34851 ?  401 HEM B C4A 1 
HETATM 5759 C  CMA . HEM H 2 .   ? -17.09100 -6.15300  -45.42700 1.000 33.67952 ?  401 HEM B CMA 1 
HETATM 5760 C  CAA . HEM H 2 .   ? -14.39200 -5.51100  -46.88700 1.000 25.26164 ?  401 HEM B CAA 1 
HETATM 5761 C  CBA . HEM H 2 .   ? -14.57400 -6.02600  -48.31400 1.000 28.10241 ?  401 HEM B CBA 1 
HETATM 5762 C  CGA . HEM H 2 .   ? -13.36200 -6.80600  -48.73700 1.000 33.96751 ?  401 HEM B CGA 1 
HETATM 5763 O  O1A . HEM H 2 .   ? -13.50200 -7.80400  -49.47300 1.000 33.66076 ?  401 HEM B O1A 1 
HETATM 5764 O  O2A . HEM H 2 .   ? -12.22300 -6.46300  -48.35700 1.000 31.44192 ?  401 HEM B O2A 1 
HETATM 5765 C  C1B . HEM H 2 .   ? -19.42400 -2.33700  -45.45500 1.000 30.08373 ?  401 HEM B C1B 1 
HETATM 5766 C  C2B . HEM H 2 .   ? -20.75400 -2.25700  -44.96500 1.000 27.67884 ?  401 HEM B C2B 1 
HETATM 5767 C  C3B . HEM H 2 .   ? -21.18700 -0.97500  -45.17200 1.000 33.83998 ?  401 HEM B C3B 1 
HETATM 5768 C  C4B . HEM H 2 .   ? -20.05700 -0.28100  -45.81400 1.000 23.06358 ?  401 HEM B C4B 1 
HETATM 5769 C  CMB . HEM H 2 .   ? -21.50200 -3.40500  -44.34600 1.000 36.63652 ?  401 HEM B CMB 1 
HETATM 5770 C  CAB . HEM H 2 .   ? -22.49000 -0.33800  -44.88600 1.000 34.39522 ?  401 HEM B CAB 1 
HETATM 5771 C  CBB . HEM H 2 .   ? -23.20300 -0.57300  -43.79300 1.000 32.57973 ?  401 HEM B CBB 1 
HETATM 5772 C  C1C . HEM H 2 .   ? -19.01700 1.75700   -46.56700 1.000 31.62992 ?  401 HEM B C1C 1 
HETATM 5773 C  C2C . HEM H 2 .   ? -18.87400 3.14400   -46.47800 1.000 31.06236 ?  401 HEM B C2C 1 
HETATM 5774 C  C3C . HEM H 2 .   ? -17.62000 3.44900   -46.97000 1.000 25.77870 ?  401 HEM B C3C 1 
HETATM 5775 C  C4C . HEM H 2 .   ? -17.00800 2.22300   -47.34700 1.000 32.94625 ?  401 HEM B C4C 1 
HETATM 5776 C  CMC . HEM H 2 .   ? -19.90900 4.10900   -45.95400 1.000 26.45080 ?  401 HEM B CMC 1 
HETATM 5777 C  CAC . HEM H 2 .   ? -17.03300 4.79400   -47.07600 1.000 35.19060 ?  401 HEM B CAC 1 
HETATM 5778 C  CBC . HEM H 2 .   ? -16.43400 5.33400   -46.02300 1.000 44.01187 ?  401 HEM B CBC 1 
HETATM 5779 C  C1D . HEM H 2 .   ? -15.09800 0.88800   -47.97000 1.000 23.57000 ?  401 HEM B C1D 1 
HETATM 5780 C  C2D . HEM H 2 .   ? -13.76000 0.79200   -48.55300 1.000 22.63569 ?  401 HEM B C2D 1 
HETATM 5781 C  C3D . HEM H 2 .   ? -13.40500 -0.50100  -48.47500 1.000 25.15908 ?  401 HEM B C3D 1 
HETATM 5782 C  C4D . HEM H 2 .   ? -14.53200 -1.19200  -47.84700 1.000 22.84961 ?  401 HEM B C4D 1 
HETATM 5783 C  CMD . HEM H 2 .   ? -12.95800 1.92700   -49.12600 1.000 28.26474 ?  401 HEM B CMD 1 
HETATM 5784 C  CAD . HEM H 2 .   ? -12.12200 -1.13400  -48.94500 1.000 28.33847 ?  401 HEM B CAD 1 
HETATM 5785 C  CBD . HEM H 2 .   ? -10.92400 -0.71900  -48.09100 1.000 16.77898 ?  401 HEM B CBD 1 
HETATM 5786 C  CGD . HEM H 2 .   ? -9.67200  -0.91000  -48.91000 1.000 31.78642 ?  401 HEM B CGD 1 
HETATM 5787 O  O1D . HEM H 2 .   ? -9.73000  -1.46400  -50.03000 1.000 25.96779 ?  401 HEM B O1D 1 
HETATM 5788 O  O2D . HEM H 2 .   ? -8.57200  -0.51600  -48.47000 1.000 23.42887 ?  401 HEM B O2D 1 
HETATM 5789 N  NA  . HEM H 2 .   ? -16.70800 -2.63900  -46.53300 1.000 25.64543 ?  401 HEM B NA  1 
HETATM 5790 N  NB  . HEM H 2 .   ? -19.04400 -1.15000  -45.94400 1.000 27.76346 ?  401 HEM B NB  1 
HETATM 5791 N  NC  . HEM H 2 .   ? -17.87900 1.20500   -47.08300 1.000 24.79818 ?  401 HEM B NC  1 
HETATM 5792 N  ND  . HEM H 2 .   ? -15.50700 -0.31600  -47.55600 1.000 21.19681 ?  401 HEM B ND  1 
HETATM 5793 FE FE  . HEM H 2 .   ? -17.15500 -0.72800  -46.77600 1.000 27.78070 ?  401 HEM B FE  1 
HETATM 5794 O  O   . HOH I 5 .   ? -13.46200 -8.59100  9.67600   1.000 31.00163 ?  501 HOH A O   1 
HETATM 5795 O  O   . HOH I 5 .   ? 5.59100   24.09500  -10.35700 1.000 36.45944 ?  502 HOH A O   1 
HETATM 5796 O  O   . HOH I 5 .   ? -2.41100  3.82900   -5.51200  1.000 23.49208 ?  503 HOH A O   1 
HETATM 5797 O  O   . HOH I 5 .   ? -5.55500  6.79000   -27.34500 1.000 25.54542 ?  504 HOH A O   1 
HETATM 5798 O  O   . HOH I 5 .   ? -23.83700 -3.74700  -9.20000  1.000 21.49891 ?  505 HOH A O   1 
HETATM 5799 O  O   . HOH I 5 .   ? -5.32200  1.23100   -17.97000 1.000 35.18280 ?  506 HOH A O   1 
HETATM 5800 O  O   . HOH I 5 .   ? -6.15700  -21.51800 -28.02300 1.000 45.13556 ?  507 HOH A O   1 
HETATM 5801 O  O   . HOH I 5 .   ? -27.89400 -5.91300  -8.14600  1.000 29.69459 ?  508 HOH A O   1 
HETATM 5802 O  O   . HOH I 5 .   ? 23.98600  5.27600   -20.71600 1.000 29.98104 ?  509 HOH A O   1 
HETATM 5803 O  O   . HOH I 5 .   ? -13.69100 -1.34200  -18.50200 1.000 30.67570 ?  510 HOH A O   1 
HETATM 5804 O  O   . HOH I 5 .   ? 21.26100  0.18500   -22.06000 1.000 28.52934 ?  511 HOH A O   1 
HETATM 5805 O  O   . HOH I 5 .   ? -22.19700 -3.38100  -15.09400 1.000 26.33642 ?  512 HOH A O   1 
HETATM 5806 O  O   . HOH I 5 .   ? -6.12300  -22.88400 -10.80100 1.000 21.45389 ?  513 HOH A O   1 
HETATM 5807 O  O   . HOH I 5 .   ? -9.18100  9.62000   -32.31600 1.000 35.35737 ?  514 HOH A O   1 
HETATM 5808 O  O   . HOH I 5 .   ? 2.08800   11.64600  -0.85100  1.000 31.86474 ?  515 HOH A O   1 
HETATM 5809 O  O   . HOH I 5 .   ? 8.42200   -8.60600  7.94300   1.000 25.23219 ?  516 HOH A O   1 
HETATM 5810 O  O   . HOH I 5 .   ? -11.36600 -16.44300 0.07400   1.000 24.99278 ?  517 HOH A O   1 
HETATM 5811 O  O   . HOH I 5 .   ? -25.42800 -2.62000  -15.35800 1.000 17.96413 ?  518 HOH A O   1 
HETATM 5812 O  O   . HOH I 5 .   ? 19.94400  -2.61100  -0.46800  1.000 38.99798 ?  519 HOH A O   1 
HETATM 5813 O  O   . HOH I 5 .   ? -3.18700  2.54100   -19.82400 1.000 29.08764 ?  520 HOH A O   1 
HETATM 5814 O  O   . HOH I 5 .   ? 20.08000  4.29400   0.10300   1.000 32.54121 ?  521 HOH A O   1 
HETATM 5815 O  O   . HOH I 5 .   ? 17.78900  -16.10400 -26.50800 1.000 39.83736 ?  522 HOH A O   1 
HETATM 5816 O  O   . HOH I 5 .   ? -1.58700  3.55200   -16.06800 1.000 33.84170 ?  523 HOH A O   1 
HETATM 5817 O  O   . HOH I 5 .   ? -6.04900  -17.46200 -25.75600 1.000 34.19764 ?  524 HOH A O   1 
HETATM 5818 O  O   . HOH I 5 .   ? -21.78300 -0.45900  2.69400   1.000 25.01483 ?  525 HOH A O   1 
HETATM 5819 O  O   . HOH I 5 .   ? -19.46200 -4.84300  6.22300   1.000 36.28082 ?  526 HOH A O   1 
HETATM 5820 O  O   . HOH I 5 .   ? 6.63200   20.37900  -3.81100  1.000 37.23431 ?  527 HOH A O   1 
HETATM 5821 O  O   . HOH I 5 .   ? -8.03900  5.20600   2.04400   1.000 17.69241 ?  528 HOH A O   1 
HETATM 5822 O  O   . HOH I 5 .   ? 18.89500  16.40500  -14.42000 1.000 31.63776 ?  529 HOH A O   1 
HETATM 5823 O  O   . HOH I 5 .   ? -11.11200 -17.97600 -11.10800 1.000 14.81664 ?  530 HOH A O   1 
HETATM 5824 O  O   . HOH I 5 .   ? 26.58500  8.20900   -5.44500  1.000 43.90637 ?  531 HOH A O   1 
HETATM 5825 O  O   . HOH I 5 .   ? -19.17700 1.51900   0.86100   1.000 14.99783 ?  532 HOH A O   1 
HETATM 5826 O  O   . HOH I 5 .   ? -2.53900  -20.38600 -8.91000  1.000 19.37036 ?  533 HOH A O   1 
HETATM 5827 O  O   . HOH I 5 .   ? 6.92600   -20.56600 -11.36900 1.000 35.92368 ?  534 HOH A O   1 
HETATM 5828 O  O   . HOH I 5 .   ? 16.26100  17.53700  -20.43600 1.000 41.07490 ?  535 HOH A O   1 
HETATM 5829 O  O   . HOH I 5 .   ? -5.48300  -7.70800  -25.57300 1.000 37.24566 ?  536 HOH A O   1 
HETATM 5830 O  O   . HOH I 5 .   ? 14.37900  -14.99600 -19.43600 1.000 34.85424 ?  537 HOH A O   1 
HETATM 5831 O  O   . HOH I 5 .   ? 23.38400  8.04200   -13.71500 1.000 26.21215 ?  538 HOH A O   1 
HETATM 5832 O  O   . HOH I 5 .   ? 3.20200   -2.12200  -36.12100 1.000 29.41339 ?  539 HOH A O   1 
HETATM 5833 O  O   . HOH I 5 .   ? -30.31800 -10.00400 1.88800   1.000 32.86412 ?  540 HOH A O   1 
HETATM 5834 O  O   . HOH I 5 .   ? 3.24500   25.17200  -3.29300  1.000 46.70133 ?  541 HOH A O   1 
HETATM 5835 O  O   . HOH I 5 .   ? 3.32100   -24.58800 -27.50700 1.000 42.97346 ?  542 HOH A O   1 
HETATM 5836 O  O   . HOH I 5 .   ? 10.68800  -5.36500  -1.82600  1.000 20.39405 ?  543 HOH A O   1 
HETATM 5837 O  O   . HOH I 5 .   ? 9.27800   -5.29600  -17.38400 1.000 20.02456 ?  544 HOH A O   1 
HETATM 5838 O  O   . HOH I 5 .   ? -17.05800 -10.61900 2.73200   1.000 20.74442 ?  545 HOH A O   1 
HETATM 5839 O  O   . HOH I 5 .   ? 21.21200  -11.16600 -16.37300 1.000 19.24252 ?  546 HOH A O   1 
HETATM 5840 O  O   . HOH I 5 .   ? -7.10800  5.10700   4.62600   1.000 23.66212 ?  547 HOH A O   1 
HETATM 5841 O  O   . HOH I 5 .   ? 14.63400  21.32000  -7.13300  1.000 37.96345 ?  548 HOH A O   1 
HETATM 5842 O  O   . HOH I 5 .   ? 4.12600   -25.93300 -13.35800 1.000 31.29972 ?  549 HOH A O   1 
HETATM 5843 O  O   . HOH I 5 .   ? -14.56700 -20.13000 -9.72800  1.000 33.46045 ?  550 HOH A O   1 
HETATM 5844 O  O   . HOH I 5 .   ? 2.76000   15.43000  -14.13300 1.000 28.91106 ?  551 HOH A O   1 
HETATM 5845 O  O   . HOH I 5 .   ? 24.43400  -4.48700  -10.26200 1.000 30.48349 ?  552 HOH A O   1 
HETATM 5846 O  O   . HOH I 5 .   ? 9.31700   20.28400  -5.31700  1.000 31.01763 ?  553 HOH A O   1 
HETATM 5847 O  O   . HOH I 5 .   ? 2.91400   8.91300   -5.03200  1.000 23.97087 ?  554 HOH A O   1 
HETATM 5848 O  O   . HOH I 5 .   ? 12.556    17.268    7.440     1.000 39.22601 ?  555 HOH A O   1 
HETATM 5849 O  O   . HOH I 5 .   ? -4.00000  8.14700   -12.46000 1.000 26.28342 ?  556 HOH A O   1 
HETATM 5850 O  O   . HOH I 5 .   ? 1.89900   15.50500  -6.16200  1.000 30.09182 ?  557 HOH A O   1 
HETATM 5851 O  O   . HOH I 5 .   ? -22.56500 -8.27000  -14.07900 1.000 15.28196 ?  558 HOH A O   1 
HETATM 5852 O  O   . HOH I 5 .   ? 6.62400   -4.55200  -4.58100  1.000 18.06529 ?  559 HOH A O   1 
HETATM 5853 O  O   . HOH I 5 .   ? 18.74700  7.32800   -21.20800 1.000 27.83504 ?  560 HOH A O   1 
HETATM 5854 O  O   . HOH I 5 .   ? -1.67900  -29.83300 -18.70800 1.000 40.85594 ?  561 HOH A O   1 
HETATM 5855 O  O   . HOH I 5 .   ? -15.55600 -4.46900  2.14700   1.000 12.04939 ?  562 HOH A O   1 
HETATM 5856 O  O   . HOH I 5 .   ? 23.26500  20.04500  -17.62800 1.000 38.19733 ?  563 HOH A O   1 
HETATM 5857 O  O   . HOH I 5 .   ? -7.20500  -3.65900  13.97400  1.000 40.19285 ?  564 HOH A O   1 
HETATM 5858 O  O   . HOH I 5 .   ? 11.48400  5.33900   7.86400   1.000 25.29828 ?  565 HOH A O   1 
HETATM 5859 O  O   . HOH I 5 .   ? 3.70100   7.60200   -11.99300 1.000 19.01860 ?  566 HOH A O   1 
HETATM 5860 O  O   . HOH I 5 .   ? -13.40000 -20.62200 -17.10700 1.000 19.52001 ?  567 HOH A O   1 
HETATM 5861 O  O   . HOH I 5 .   ? 22.48500  -3.58600  -23.65900 1.000 24.18792 ?  568 HOH A O   1 
HETATM 5862 O  O   . HOH I 5 .   ? 5.76300   10.99000  -19.40400 1.000 30.09310 ?  569 HOH A O   1 
HETATM 5863 O  O   . HOH I 5 .   ? -26.82000 -10.36500 -12.12900 1.000 17.14061 ?  570 HOH A O   1 
HETATM 5864 O  O   . HOH I 5 .   ? -8.92500  2.39000   -16.14300 1.000 37.96025 ?  571 HOH A O   1 
HETATM 5865 O  O   . HOH I 5 .   ? -20.20900 -20.80100 -16.58600 1.000 34.73034 ?  572 HOH A O   1 
HETATM 5866 O  O   . HOH I 5 .   ? 6.52700   -13.97000 -8.62100  1.000 39.98663 ?  573 HOH A O   1 
HETATM 5867 O  O   . HOH I 5 .   ? -6.87100  7.44900   -8.73700  1.000 25.45563 ?  574 HOH A O   1 
HETATM 5868 O  O   . HOH I 5 .   ? 10.22100  -8.67900  11.29000  1.000 33.35573 ?  575 HOH A O   1 
HETATM 5869 O  O   . HOH I 5 .   ? -15.91300 -13.62800 -0.42500  1.000 29.51970 ?  576 HOH A O   1 
HETATM 5870 O  O   . HOH I 5 .   ? -10.74900 -10.55400 -21.71200 1.000 34.06754 ?  577 HOH A O   1 
HETATM 5871 O  O   . HOH I 5 .   ? 26.50500  -1.14400  -17.33900 1.000 29.53640 ?  578 HOH A O   1 
HETATM 5872 O  O   . HOH I 5 .   ? -2.54600  5.84900   -15.75700 1.000 38.44597 ?  579 HOH A O   1 
HETATM 5873 O  O   . HOH I 5 .   ? 20.15600  10.71500  5.26100   1.000 29.13569 ?  580 HOH A O   1 
HETATM 5874 O  O   . HOH I 5 .   ? -14.112   -23.400   -11.072   1.000 33.25974 ?  581 HOH A O   1 
HETATM 5875 O  O   . HOH I 5 .   ? -12.35000 7.88200   -13.16700 1.000 43.43935 ?  582 HOH A O   1 
HETATM 5876 O  O   . HOH I 5 .   ? 14.37200  -1.30200  -33.57000 1.000 23.08680 ?  583 HOH A O   1 
HETATM 5877 O  O   . HOH I 5 .   ? 23.01800  5.52500   -10.60400 1.000 23.57046 ?  584 HOH A O   1 
HETATM 5878 O  O   . HOH I 5 .   ? -6.70600  -24.29100 -20.19800 1.000 28.78742 ?  585 HOH A O   1 
HETATM 5879 O  O   . HOH I 5 .   ? 20.88900  -1.47800  8.58000   1.000 29.25874 ?  586 HOH A O   1 
HETATM 5880 O  O   . HOH I 5 .   ? 5.52400   -7.09600  2.97100   1.000 27.06314 ?  587 HOH A O   1 
HETATM 5881 O  O   . HOH I 5 .   ? -5.25100  2.40500   12.73900  1.000 24.74548 ?  588 HOH A O   1 
HETATM 5882 O  O   . HOH I 5 .   ? -11.90100 0.03500   7.28800   1.000 24.49238 ?  589 HOH A O   1 
HETATM 5883 O  O   . HOH I 5 .   ? 11.96300  -3.44300  -25.39900 1.000 26.15917 ?  590 HOH A O   1 
HETATM 5884 O  O   . HOH I 5 .   ? 17.19800  -6.02600  -8.79500  1.000 23.63250 ?  591 HOH A O   1 
HETATM 5885 O  O   . HOH I 5 .   ? -6.74300  6.57300   -10.83400 1.000 39.76150 ?  592 HOH A O   1 
HETATM 5886 O  O   . HOH I 5 .   ? 16.90900  -17.60600 -17.41600 1.000 31.81919 ?  593 HOH A O   1 
HETATM 5887 O  O   . HOH I 5 .   ? 9.92300   5.01500   9.99900   1.000 29.62602 ?  594 HOH A O   1 
HETATM 5888 O  O   . HOH I 5 .   ? 4.75600   10.10700  0.75200   1.000 27.47761 ?  595 HOH A O   1 
HETATM 5889 O  O   . HOH I 5 .   ? 0.81100   -8.53800  -2.29200  1.000 17.92501 ?  596 HOH A O   1 
HETATM 5890 O  O   . HOH I 5 .   ? 24.66500  -5.69300  -13.17900 1.000 16.59794 ?  597 HOH A O   1 
HETATM 5891 O  O   . HOH I 5 .   ? 1.03600   -0.68400  10.09900  1.000 18.59872 ?  598 HOH A O   1 
HETATM 5892 O  O   . HOH I 5 .   ? -17.25500 0.10100   -0.88300  1.000 17.65869 ?  599 HOH A O   1 
HETATM 5893 O  O   . HOH I 5 .   ? 13.84400  1.08800   -23.18500 1.000 31.15689 ?  600 HOH A O   1 
HETATM 5894 O  O   . HOH I 5 .   ? -26.00300 -20.45200 -8.80900  1.000 21.23648 ?  601 HOH A O   1 
HETATM 5895 O  O   . HOH I 5 .   ? 8.16300   -12.62500 -10.71000 1.000 25.19236 ?  602 HOH A O   1 
HETATM 5896 O  O   . HOH I 5 .   ? 25.16700  17.60000  -10.47500 1.000 41.77932 ?  603 HOH A O   1 
HETATM 5897 O  O   . HOH I 5 .   ? -2.94900  -17.50800 -22.16300 1.000 28.08806 ?  604 HOH A O   1 
HETATM 5898 O  O   . HOH I 5 .   ? 7.44300   16.52600  -19.63300 1.000 41.02087 ?  605 HOH A O   1 
HETATM 5899 O  O   . HOH I 5 .   ? -12.256   10.711    3.585     1.000 31.56219 ?  606 HOH A O   1 
HETATM 5900 O  O   . HOH I 5 .   ? -26.26900 -8.31900  -13.89800 1.000 20.99041 ?  607 HOH A O   1 
HETATM 5901 O  O   . HOH I 5 .   ? 7.02200   1.52800   12.13200  1.000 37.32633 ?  608 HOH A O   1 
HETATM 5902 O  O   . HOH I 5 .   ? 18.76600  -0.82400  -22.32000 1.000 32.10064 ?  609 HOH A O   1 
HETATM 5903 O  O   . HOH I 5 .   ? 7.42900   -13.82500 -37.85600 1.000 43.39575 ?  610 HOH A O   1 
HETATM 5904 O  O   . HOH I 5 .   ? -7.13200  -15.43000 -6.98300  1.000 16.79713 ?  611 HOH A O   1 
HETATM 5905 O  O   . HOH I 5 .   ? -5.47200  -12.31800 -7.05600  1.000 12.99705 ?  612 HOH A O   1 
HETATM 5906 O  O   . HOH I 5 .   ? -29.06500 -12.00500 -16.00400 1.000 20.57104 ?  613 HOH A O   1 
HETATM 5907 O  O   . HOH I 5 .   ? -0.61200  -4.94300  9.59300   1.000 26.82340 ?  614 HOH A O   1 
HETATM 5908 O  O   . HOH I 5 .   ? -8.13400  -10.66300 6.95000   1.000 37.39510 ?  615 HOH A O   1 
HETATM 5909 O  O   . HOH I 5 .   ? 14.18100  -20.17500 -22.37700 1.000 31.79688 ?  616 HOH A O   1 
HETATM 5910 O  O   . HOH I 5 .   ? -8.05200  -18.72900 -5.00000  1.000 23.65967 ?  617 HOH A O   1 
HETATM 5911 O  O   . HOH I 5 .   ? 3.27900   3.24100   10.56300  1.000 29.42198 ?  618 HOH A O   1 
HETATM 5912 O  O   . HOH I 5 .   ? -28.95500 -13.17600 -10.04400 1.000 26.84187 ?  619 HOH A O   1 
HETATM 5913 O  O   . HOH I 5 .   ? -27.19000 9.33200   -15.30900 1.000 39.38378 ?  620 HOH A O   1 
HETATM 5914 O  O   . HOH I 5 .   ? 1.42600   -3.12300  10.14800  1.000 23.73377 ?  621 HOH A O   1 
HETATM 5915 O  O   . HOH I 5 .   ? -12.74100 -7.69500  -8.50600  1.000 15.31371 ?  622 HOH A O   1 
HETATM 5916 O  O   . HOH I 5 .   ? -9.27700  0.40200   -4.34600  1.000 10.44386 ?  623 HOH A O   1 
HETATM 5917 O  O   . HOH I 5 .   ? 13.40100  -1.10600  10.98900  1.000 38.69751 ?  624 HOH A O   1 
HETATM 5918 O  O   . HOH I 5 .   ? -6.43000  13.66000  -13.48200 1.000 39.88377 ?  625 HOH A O   1 
HETATM 5919 O  O   . HOH I 5 .   ? 3.63800   26.08700  -7.62400  1.000 41.14131 ?  626 HOH A O   1 
HETATM 5920 O  O   . HOH I 5 .   ? -9.69300  -16.42400 -7.49100  1.000 17.58380 ?  627 HOH A O   1 
HETATM 5921 O  O   . HOH I 5 .   ? -11.89500 -14.84100 -6.91600  1.000 17.26480 ?  628 HOH A O   1 
HETATM 5922 O  O   . HOH I 5 .   ? -20.83900 3.57100   -18.78200 1.000 33.31140 ?  629 HOH A O   1 
HETATM 5923 O  O   . HOH I 5 .   ? 16.33200  -15.36800 -17.24200 1.000 26.20625 ?  630 HOH A O   1 
HETATM 5924 O  O   . HOH I 5 .   ? 12.52900  17.35000  -4.23700  1.000 24.92359 ?  631 HOH A O   1 
HETATM 5925 O  O   . HOH I 5 .   ? 7.44000   -6.77500  6.05100   1.000 34.52620 ?  632 HOH A O   1 
HETATM 5926 O  O   . HOH I 5 .   ? 20.32200  -0.59900  -10.66300 1.000 30.73010 ?  633 HOH A O   1 
HETATM 5927 O  O   . HOH I 5 .   ? -2.12700  0.64600   -2.86700  1.000 13.77633 ?  634 HOH A O   1 
HETATM 5928 O  O   . HOH I 5 .   ? 1.32700   -5.74800  -36.57100 1.000 25.99199 ?  635 HOH A O   1 
HETATM 5929 O  O   . HOH I 5 .   ? -11.95900 -16.00200 -28.15900 1.000 33.19725 ?  636 HOH A O   1 
HETATM 5930 O  O   . HOH I 5 .   ? 4.978     -8.359    6.390     1.000 17.12751 ?  637 HOH A O   1 
HETATM 5931 O  O   . HOH I 5 .   ? -22.40300 -20.37100 -16.42600 1.000 38.92653 ?  638 HOH A O   1 
HETATM 5932 O  O   . HOH I 5 .   ? 16.22100  7.09400   -21.62400 1.000 29.26875 ?  639 HOH A O   1 
HETATM 5933 O  O   . HOH I 5 .   ? 7.21200   -2.83400  4.21700   1.000 23.33561 ?  640 HOH A O   1 
HETATM 5934 O  O   . HOH I 5 .   ? 12.61000  -5.47600  -4.00700  1.000 22.47910 ?  641 HOH A O   1 
HETATM 5935 O  O   . HOH I 5 .   ? 2.76600   -13.29000 -6.17200  1.000 29.42152 ?  642 HOH A O   1 
HETATM 5936 O  O   . HOH I 5 .   ? -10.38500 4.56300   -16.83000 1.000 40.57329 ?  643 HOH A O   1 
HETATM 5937 O  O   . HOH I 5 .   ? 18.20500  -5.89000  4.19200   1.000 31.25621 ?  644 HOH A O   1 
HETATM 5938 O  O   . HOH I 5 .   ? 5.16600   -8.45900  0.85300   1.000 21.35583 ?  645 HOH A O   1 
HETATM 5939 O  O   . HOH I 5 .   ? -4.15500  15.71600  -12.30400 1.000 33.18944 ?  646 HOH A O   1 
HETATM 5940 O  O   . HOH I 5 .   ? -23.30000 -16.56300 -12.13800 1.000 24.84062 ?  647 HOH A O   1 
HETATM 5941 O  O   . HOH I 5 .   ? -20.00800 -4.66000  -15.47300 1.000 19.80639 ?  648 HOH A O   1 
HETATM 5942 O  O   . HOH I 5 .   ? 11.14100  -2.03200  10.69200  1.000 35.46261 ?  649 HOH A O   1 
HETATM 5943 O  O   . HOH I 5 .   ? -25.98800 -15.85500 0.99400   1.000 28.22538 ?  650 HOH A O   1 
HETATM 5944 O  O   . HOH I 5 .   ? -28.33600 -8.18600  1.74700   1.000 24.61563 ?  651 HOH A O   1 
HETATM 5945 O  O   . HOH I 5 .   ? -4.96500  -1.92100  -15.12200 1.000 32.90561 ?  652 HOH A O   1 
HETATM 5946 O  O   . HOH I 5 .   ? 25.04100  15.79100  -17.18500 1.000 29.40102 ?  653 HOH A O   1 
HETATM 5947 O  O   . HOH I 5 .   ? -8.40900  -27.37900 -11.22300 1.000 27.97694 ?  654 HOH A O   1 
HETATM 5948 O  O   . HOH I 5 .   ? -28.86000 -14.31800 -7.27200  1.000 19.45195 ?  655 HOH A O   1 
HETATM 5949 O  O   . HOH I 5 .   ? -23.54200 -5.57400  -11.25800 1.000 19.03479 ?  656 HOH A O   1 
HETATM 5950 O  O   . HOH I 5 .   ? -3.08800  7.85800   7.80200   1.000 32.04621 ?  657 HOH A O   1 
HETATM 5951 O  O   . HOH I 5 .   ? -4.71200  -0.71700  13.17600  1.000 38.76518 ?  658 HOH A O   1 
HETATM 5952 O  O   . HOH I 5 .   ? -15.51300 -11.02000 0.44700   1.000 21.46359 ?  659 HOH A O   1 
HETATM 5953 O  O   . HOH I 5 .   ? -22.00600 -12.66100 -20.41100 1.000 31.49122 ?  660 HOH A O   1 
HETATM 5954 O  O   . HOH I 5 .   ? -3.23800  5.00400   -34.84200 1.000 36.28872 ?  661 HOH A O   1 
HETATM 5955 O  O   . HOH I 5 .   ? -14.24400 -14.20600 -19.65900 1.000 21.79650 ?  662 HOH A O   1 
HETATM 5956 O  O   . HOH I 5 .   ? -1.46500  17.21900  -7.89700  1.000 41.53293 ?  663 HOH A O   1 
HETATM 5957 O  O   . HOH I 5 .   ? 20.74800  -18.96900 -11.27500 1.000 43.43575 ?  664 HOH A O   1 
HETATM 5958 O  O   . HOH I 5 .   ? -1.51300  -24.59500 -11.09100 1.000 31.33742 ?  665 HOH A O   1 
HETATM 5959 O  O   . HOH I 5 .   ? 10.19900  24.85900  -11.18500 1.000 37.94448 ?  666 HOH A O   1 
HETATM 5960 O  O   . HOH I 5 .   ? -4.407    4.886     12.113    1.000 28.45240 ?  667 HOH A O   1 
HETATM 5961 O  O   . HOH I 5 .   ? -5.23500  14.98800  -16.03200 1.000 42.81637 ?  668 HOH A O   1 
HETATM 5962 O  O   . HOH I 5 .   ? -1.30700  23.45100  -10.91700 1.000 48.32303 ?  669 HOH A O   1 
HETATM 5963 O  O   . HOH I 5 .   ? 16.98900  -7.64800  -18.85100 1.000 23.90940 ?  670 HOH A O   1 
HETATM 5964 O  O   . HOH I 5 .   ? -23.945   1.982     5.837     1.000 37.85284 ?  671 HOH A O   1 
HETATM 5965 O  O   . HOH I 5 .   ? -23.96000 -10.36200 -19.96300 1.000 36.02896 ?  672 HOH A O   1 
HETATM 5966 O  O   . HOH I 5 .   ? 13.29800  -20.75300 -16.30900 1.000 38.25892 ?  673 HOH A O   1 
HETATM 5967 O  O   . HOH I 5 .   ? 7.11100   -16.37700 -11.00500 1.000 37.16705 ?  674 HOH A O   1 
HETATM 5968 O  O   . HOH I 5 .   ? 14.62800  -4.19900  4.31000   1.000 23.32601 ?  675 HOH A O   1 
HETATM 5969 O  O   . HOH I 5 .   ? 13.55100  14.27900  -20.12400 1.000 40.35350 ?  676 HOH A O   1 
HETATM 5970 O  O   . HOH I 5 .   ? -11.45800 -2.19400  -17.92700 1.000 22.24350 ?  677 HOH A O   1 
HETATM 5971 O  O   . HOH I 5 .   ? 8.43100   13.60600  -21.50000 1.000 39.25516 ?  678 HOH A O   1 
HETATM 5972 O  O   . HOH I 5 .   ? 3.17400   -2.89100  13.63300  1.000 39.11723 ?  679 HOH A O   1 
HETATM 5973 O  O   . HOH I 5 .   ? 19.47300  -3.24100  -6.07100  1.000 33.08686 ?  680 HOH A O   1 
HETATM 5974 O  O   . HOH I 5 .   ? -10.84100 -5.11600  7.02200   1.000 18.87922 ?  681 HOH A O   1 
HETATM 5975 O  O   . HOH I 5 .   ? 13.00400  -10.28600 -6.72000  1.000 25.51292 ?  682 HOH A O   1 
HETATM 5976 O  O   . HOH I 5 .   ? -1.53900  -23.17300 -31.88300 1.000 45.97599 ?  683 HOH A O   1 
HETATM 5977 O  O   . HOH I 5 .   ? 21.79400  3.02300   -3.99800  1.000 28.11754 ?  684 HOH A O   1 
HETATM 5978 O  O   . HOH I 5 .   ? 13.35900  -14.39600 -8.04900  1.000 34.36691 ?  685 HOH A O   1 
HETATM 5979 O  O   . HOH I 5 .   ? -25.38700 0.09200   -2.57600  1.000 23.75135 ?  686 HOH A O   1 
HETATM 5980 O  O   . HOH I 5 .   ? 12.03400  20.93200  -5.43800  1.000 33.71121 ?  687 HOH A O   1 
HETATM 5981 O  O   . HOH I 5 .   ? 19.90800  13.96100  -3.25500  1.000 39.30655 ?  688 HOH A O   1 
HETATM 5982 O  O   . HOH I 5 .   ? -13.47800 -0.14300  -15.58200 1.000 27.80120 ?  689 HOH A O   1 
HETATM 5983 O  O   . HOH I 5 .   ? 15.89500  14.97400  -2.36200  1.000 39.14210 ?  690 HOH A O   1 
HETATM 5984 O  O   . HOH I 5 .   ? 17.82500  -12.24300 -7.01100  1.000 43.55787 ?  691 HOH A O   1 
HETATM 5985 O  O   . HOH I 5 .   ? -4.87500  -14.59000 -28.71300 1.000 26.80683 ?  692 HOH A O   1 
HETATM 5986 O  O   . HOH I 5 .   ? 22.45600  -14.84300 -14.54800 1.000 41.02054 ?  693 HOH A O   1 
HETATM 5987 O  O   . HOH I 5 .   ? 13.56500  -22.53800 -14.87200 1.000 37.81387 ?  694 HOH A O   1 
HETATM 5988 O  O   . HOH I 5 .   ? -0.19500  13.80400  -24.86900 1.000 52.43921 ?  695 HOH A O   1 
HETATM 5989 O  O   . HOH I 5 .   ? -2.53300  -16.08500 -19.97200 1.000 25.44152 ?  696 HOH A O   1 
HETATM 5990 O  O   . HOH I 5 .   ? -27.766   4.184     -12.497   1.000 37.01722 ?  697 HOH A O   1 
HETATM 5991 O  O   . HOH I 5 .   ? -23.80300 -19.43600 -11.99900 1.000 32.10964 ?  698 HOH A O   1 
HETATM 5992 O  O   . HOH I 5 .   ? -4.70600  -12.54600 -27.70400 1.000 35.60732 ?  699 HOH A O   1 
HETATM 5993 O  O   . HOH I 5 .   ? 4.35100   18.68600  -14.45000 1.000 40.62586 ?  700 HOH A O   1 
HETATM 5994 O  O   . HOH I 5 .   ? -18.01100 -17.61500 3.24600   1.000 37.42788 ?  701 HOH A O   1 
HETATM 5995 O  O   . HOH I 5 .   ? -2.07400  -11.22800 4.03200   1.000 37.38232 ?  702 HOH A O   1 
HETATM 5996 O  O   . HOH I 5 .   ? -30.41100 -12.41900 -6.05100  1.000 35.53987 ?  703 HOH A O   1 
HETATM 5997 O  O   . HOH I 5 .   ? -12.46100 4.74700   7.03400   1.000 32.52341 ?  704 HOH A O   1 
HETATM 5998 O  O   . HOH I 5 .   ? -6.89500  -28.79700 -15.18900 1.000 32.18905 ?  705 HOH A O   1 
HETATM 5999 O  O   . HOH I 5 .   ? -9.76700  -11.93100 5.11500   1.000 30.46578 ?  706 HOH A O   1 
HETATM 6000 O  O   . HOH I 5 .   ? -26.34600 7.27500   -9.38000  1.000 46.36653 ?  707 HOH A O   1 
HETATM 6001 O  O   . HOH I 5 .   ? -6.14900  -25.16700 -25.59400 1.000 44.71593 ?  708 HOH A O   1 
HETATM 6002 O  O   . HOH I 5 .   ? -13.13100 -11.90200 -21.04300 1.000 21.59771 ?  709 HOH A O   1 
HETATM 6003 O  O   . HOH I 5 .   ? 9.031     14.059    5.946     1.000 40.78075 ?  710 HOH A O   1 
HETATM 6004 O  O   . HOH I 5 .   ? -7.59400  -21.71600 -22.87600 1.000 37.57828 ?  711 HOH A O   1 
HETATM 6005 O  O   . HOH I 5 .   ? -3.91500  -7.83500  -36.13300 1.000 38.57531 ?  712 HOH A O   1 
HETATM 6006 O  O   . HOH I 5 .   ? -13.13500 -5.03300  8.31500   1.000 31.85891 ?  713 HOH A O   1 
HETATM 6007 O  O   . HOH I 5 .   ? 3.56800   10.31800  3.44400   1.000 28.91724 ?  714 HOH A O   1 
HETATM 6008 O  O   . HOH I 5 .   ? 23.60400  -17.21800 -8.15200  1.000 42.81286 ?  715 HOH A O   1 
HETATM 6009 O  O   . HOH I 5 .   ? 15.389    -2.055    11.202    1.000 33.72597 ?  716 HOH A O   1 
HETATM 6010 O  O   . HOH I 5 .   ? -19.64000 -9.89000  5.89600   1.000 40.18516 ?  717 HOH A O   1 
HETATM 6011 O  O   . HOH I 5 .   ? 26.19500  11.54800  -8.33700  1.000 43.01718 ?  718 HOH A O   1 
HETATM 6012 O  O   . HOH I 5 .   ? 10.03700  -27.27600 -20.81900 1.000 37.43242 ?  719 HOH A O   1 
HETATM 6013 O  O   . HOH I 5 .   ? -5.12800  7.65000   -33.81300 1.000 39.10387 ?  720 HOH A O   1 
HETATM 6014 O  O   . HOH I 5 .   ? 19.56900  1.22400   -0.94900  1.000 36.90103 ?  721 HOH A O   1 
HETATM 6015 O  O   . HOH I 5 .   ? -27.84700 -18.22600 -6.37700  1.000 27.53616 ?  722 HOH A O   1 
HETATM 6016 O  O   . HOH I 5 .   ? 5.31400   -0.58900  11.81700  1.000 23.66397 ?  723 HOH A O   1 
HETATM 6017 O  O   . HOH I 5 .   ? 15.04600  -13.60900 -21.40500 1.000 25.36150 ?  724 HOH A O   1 
HETATM 6018 O  O   . HOH I 5 .   ? -24.68200 -0.58200  0.82400   1.000 39.20899 ?  725 HOH A O   1 
HETATM 6019 O  O   . HOH I 5 .   ? -5.41200  -11.69200 6.51700   1.000 36.16215 ?  726 HOH A O   1 
HETATM 6020 O  O   . HOH I 5 .   ? -29.01900 -7.26300  -3.41800  1.000 36.58407 ?  727 HOH A O   1 
HETATM 6021 O  O   . HOH I 5 .   ? 23.23200  5.77300   -13.22000 1.000 29.20609 ?  728 HOH A O   1 
HETATM 6022 O  O   . HOH I 5 .   ? -13.85400 -16.60700 0.74300   1.000 37.66889 ?  729 HOH A O   1 
HETATM 6023 O  O   . HOH I 5 .   ? 26.85000  13.00700  -12.12100 1.000 41.74402 ?  730 HOH A O   1 
HETATM 6024 O  O   . HOH I 5 .   ? -26.27200 -13.51300 -19.08900 1.000 37.86053 ?  731 HOH A O   1 
HETATM 6025 O  O   . HOH I 5 .   ? -12.19100 -18.29200 -8.90600  1.000 27.61445 ?  732 HOH A O   1 
HETATM 6026 O  O   . HOH I 5 .   ? 2.31200   7.85900   -18.24100 1.000 34.29288 ?  733 HOH A O   1 
HETATM 6027 O  O   . HOH I 5 .   ? -4.62500  -20.62500 -31.56200 1.000 37.40907 ?  734 HOH A O   1 
HETATM 6028 O  O   . HOH I 5 .   ? -28.86200 -7.07000  -1.00000  1.000 37.20833 ?  735 HOH A O   1 
HETATM 6029 O  O   . HOH I 5 .   ? -14.45200 -10.00700 -20.29300 1.000 21.90977 ?  736 HOH A O   1 
HETATM 6030 O  O   . HOH I 5 .   ? 9.82500   -7.25600  5.13600   1.000 31.98611 ?  737 HOH A O   1 
HETATM 6031 O  O   . HOH I 5 .   ? -5.43800  -1.33700  -17.79000 1.000 36.27947 ?  738 HOH A O   1 
HETATM 6032 O  O   . HOH I 5 .   ? -4.05900  -15.13900 -31.76300 1.000 36.75568 ?  739 HOH A O   1 
HETATM 6033 O  O   . HOH I 5 .   ? 23.79300  -8.32400  -10.05900 1.000 26.48844 ?  740 HOH A O   1 
HETATM 6034 O  O   . HOH I 5 .   ? 18.78900  -10.11200 -20.75000 1.000 30.87331 ?  741 HOH A O   1 
HETATM 6035 O  O   . HOH I 5 .   ? -8.14600  -4.43100  -20.22400 1.000 37.15601 ?  742 HOH A O   1 
HETATM 6036 O  O   . HOH I 5 .   ? -2.23000  8.58800   1.12000   1.000 29.82705 ?  743 HOH A O   1 
HETATM 6037 O  O   . HOH I 5 .   ? 8.39100   12.42400  9.62000   1.000 42.60208 ?  744 HOH A O   1 
HETATM 6038 O  O   . HOH I 5 .   ? -21.42900 2.57000   1.20100   1.000 29.11909 ?  745 HOH A O   1 
HETATM 6039 O  O   . HOH I 5 .   ? -20.32400 -21.64200 -12.51100 1.000 33.49672 ?  746 HOH A O   1 
HETATM 6040 O  O   . HOH I 5 .   ? -7.26100  -24.21200 -8.60600  1.000 33.31272 ?  747 HOH A O   1 
HETATM 6041 O  O   . HOH I 5 .   ? -24.37800 -6.66500  -13.47700 1.000 20.62534 ?  748 HOH A O   1 
HETATM 6042 O  O   . HOH I 5 .   ? 8.06100   11.26100  6.78400   1.000 35.67613 ?  749 HOH A O   1 
HETATM 6043 O  O   . HOH I 5 .   ? -19.11400 5.73100   -11.14200 1.000 39.17479 ?  750 HOH A O   1 
HETATM 6044 O  O   . HOH I 5 .   ? 27.12100  10.34600  -6.18600  1.000 49.88362 ?  751 HOH A O   1 
HETATM 6045 O  O   . HOH I 5 .   ? -26.27700 2.76700   -8.24100  1.000 43.75376 ?  752 HOH A O   1 
HETATM 6046 O  O   . HOH I 5 .   ? 1.13000   11.70900  2.94300   1.000 45.25767 ?  753 HOH A O   1 
HETATM 6047 O  O   . HOH I 5 .   ? -1.30300  -30.63000 -15.91700 1.000 43.75808 ?  754 HOH A O   1 
HETATM 6048 O  O   . HOH I 5 .   ? 8.28100   -28.54300 -20.10900 1.000 44.80965 ?  755 HOH A O   1 
HETATM 6049 O  O   . HOH I 5 .   ? -0.21500  10.21900  -29.37500 1.000 42.48045 ?  756 HOH A O   1 
HETATM 6050 O  O   . HOH I 5 .   ? 17.639    23.076    -7.537    1.000 43.34171 ?  757 HOH A O   1 
HETATM 6051 O  O   . HOH I 5 .   ? 8.58900   7.40200   10.74400  1.000 45.98162 ?  758 HOH A O   1 
HETATM 6052 O  O   . HOH I 5 .   ? -13.79800 -2.15900  8.79300   1.000 33.67361 ?  759 HOH A O   1 
HETATM 6053 O  O   . HOH I 5 .   ? 22.76300  4.85900   -3.14800  1.000 35.36169 ?  760 HOH A O   1 
HETATM 6054 O  O   . HOH I 5 .   ? 20.640    -20.921   -8.856    1.000 29.32667 ?  761 HOH A O   1 
HETATM 6055 O  O   . HOH I 5 .   ? -6.56400  7.07300   8.19400   1.000 35.18100 ?  762 HOH A O   1 
HETATM 6056 O  O   . HOH I 5 .   ? 4.66600   -25.24200 -30.00400 1.000 42.93931 ?  763 HOH A O   1 
HETATM 6057 O  O   . HOH I 5 .   ? -18.71100 8.01200   -9.35400  1.000 44.88020 ?  764 HOH A O   1 
HETATM 6058 O  O   . HOH I 5 .   ? 22.17800  4.97800   -0.58700  1.000 41.66029 ?  765 HOH A O   1 
HETATM 6059 O  O   . HOH I 5 .   ? 22.86900  0.16900   -9.59300  1.000 34.73166 ?  766 HOH A O   1 
HETATM 6060 O  O   . HOH I 5 .   ? 23.99800  12.00000  -21.08000 1.000 43.31361 ?  767 HOH A O   1 
HETATM 6061 O  O   . HOH I 5 .   ? -9.995    -20.841   -5.906    1.000 36.14048 ?  768 HOH A O   1 
HETATM 6062 O  O   . HOH I 5 .   ? 2.08100   14.87400  -1.07200  1.000 39.87641 ?  769 HOH A O   1 
HETATM 6063 O  O   . HOH I 5 .   ? -21.601   1.185     8.053     1.000 42.31658 ?  770 HOH A O   1 
HETATM 6064 O  O   . HOH I 5 .   ? 25.53300  7.39200   -21.22600 1.000 28.94854 ?  771 HOH A O   1 
HETATM 6065 O  O   . HOH I 5 .   ? -19.80000 0.56700   -22.05700 1.000 32.28853 ?  772 HOH A O   1 
HETATM 6066 O  O   . HOH I 5 .   ? 22.410    -14.216   -11.897   1.000 33.25656 ?  773 HOH A O   1 
HETATM 6067 O  O   . HOH I 5 .   ? -12.48100 -16.22200 -25.93700 1.000 41.69689 ?  774 HOH A O   1 
HETATM 6068 O  O   . HOH I 5 .   ? -1.95500  -27.20200 -9.93600  1.000 38.36815 ?  775 HOH A O   1 
HETATM 6069 O  O   . HOH I 5 .   ? -10.38900 -0.72900  -16.02200 1.000 36.12142 ?  776 HOH A O   1 
HETATM 6070 O  O   . HOH I 5 .   ? -17.488   2.768     10.545    1.000 44.90743 ?  777 HOH A O   1 
HETATM 6071 O  O   . HOH I 5 .   ? 20.59400  4.97700   -22.70300 1.000 31.49804 ?  778 HOH A O   1 
HETATM 6072 O  O   . HOH I 5 .   ? -22.66200 -2.54800  4.62200   1.000 38.26758 ?  779 HOH A O   1 
HETATM 6073 O  O   . HOH I 5 .   ? -8.01400  -26.68500 -8.67500  1.000 42.00927 ?  780 HOH A O   1 
HETATM 6074 O  O   . HOH I 5 .   ? 22.72400  9.23100   -23.98500 1.000 37.59983 ?  781 HOH A O   1 
HETATM 6075 O  O   . HOH I 5 .   ? 4.52300   -28.16900 -16.76900 1.000 38.53440 ?  782 HOH A O   1 
HETATM 6076 O  O   . HOH I 5 .   ? 13.86200  -1.65200  -25.21000 1.000 31.42005 ?  783 HOH A O   1 
HETATM 6077 O  O   . HOH I 5 .   ? 8.86800   -15.40300 -9.98800  1.000 36.63046 ?  784 HOH A O   1 
HETATM 6078 O  O   . HOH I 5 .   ? 21.11700  0.30400   10.56100  1.000 45.90032 ?  785 HOH A O   1 
HETATM 6079 O  O   . HOH I 5 .   ? 3.04900   0.93400   11.52200  1.000 33.62016 ?  786 HOH A O   1 
HETATM 6080 O  O   . HOH I 5 .   ? -8.14100  -28.32800 -18.52500 1.000 37.23979 ?  787 HOH A O   1 
HETATM 6081 O  O   . HOH I 5 .   ? 17.709    -1.293    -30.551   1.000 42.67082 ?  788 HOH A O   1 
HETATM 6082 O  O   . HOH I 5 .   ? -21.45100 -17.41800 -22.31800 1.000 44.10299 ?  789 HOH A O   1 
HETATM 6083 O  O   . HOH I 5 .   ? 1.48400   -12.95200 -4.21900  1.000 34.15749 ?  790 HOH A O   1 
HETATM 6084 O  O   . HOH I 5 .   ? 13.15800  12.26200  -21.23100 1.000 37.11838 ?  791 HOH A O   1 
HETATM 6085 O  O   . HOH I 5 .   ? -24.53600 -18.50000 -15.39100 1.000 35.82238 ?  792 HOH A O   1 
HETATM 6086 O  O   . HOH I 5 .   ? -3.84600  4.45900   -18.34300 1.000 39.28752 ?  793 HOH A O   1 
HETATM 6087 O  O   . HOH I 5 .   ? -28.43600 -13.39700 -18.18900 1.000 32.26804 ?  794 HOH A O   1 
HETATM 6088 O  O   . HOH I 5 .   ? -24.721   9.819     -20.571   1.000 37.62176 ?  795 HOH A O   1 
HETATM 6089 O  O   . HOH I 5 .   ? 20.51700  23.33400  -11.53700 1.000 34.21051 ?  796 HOH A O   1 
HETATM 6090 O  O   . HOH I 5 .   ? 17.42500  9.76400   8.96900   1.000 43.20837 ?  797 HOH A O   1 
HETATM 6091 O  O   . HOH I 5 .   ? 22.70700  -2.61600  7.67900   1.000 40.14634 ?  798 HOH A O   1 
HETATM 6092 O  O   . HOH I 5 .   ? -7.26700  -19.98200 -26.45300 1.000 44.82209 ?  799 HOH A O   1 
HETATM 6093 O  O   . HOH I 5 .   ? -5.03200  7.20400   -19.38500 1.000 47.49087 ?  800 HOH A O   1 
HETATM 6094 O  O   . HOH I 5 .   ? 21.762    -7.964    -5.739    1.000 37.22881 ?  801 HOH A O   1 
HETATM 6095 O  O   . HOH I 5 .   ? 9.82600   -15.98500 -38.76100 1.000 41.77588 ?  802 HOH A O   1 
HETATM 6096 O  O   . HOH I 5 .   ? 19.49400  10.73500  8.21400   1.000 43.50305 ?  803 HOH A O   1 
HETATM 6097 O  O   . HOH I 5 .   ? 2.53300   -25.38800 -11.05100 1.000 43.29878 ?  804 HOH A O   1 
HETATM 6098 O  O   . HOH I 5 .   ? -6.81300  15.79300  -20.58400 1.000 47.46464 ?  805 HOH A O   1 
HETATM 6099 O  O   . HOH I 5 .   ? 10.67300  18.01300  -18.04100 1.000 34.27078 ?  806 HOH A O   1 
HETATM 6100 O  O   . HOH I 5 .   ? 1.07500   -23.74100 -10.71900 1.000 33.57079 ?  807 HOH A O   1 
HETATM 6101 O  O   . HOH I 5 .   ? -21.99700 -22.91500 -15.02400 1.000 46.36872 ?  808 HOH A O   1 
HETATM 6102 O  O   . HOH I 5 .   ? 18.141    -10.815   -24.025   1.000 38.68795 ?  809 HOH A O   1 
HETATM 6103 O  O   . HOH I 5 .   ? 17.082    -11.405   -29.688   1.000 39.68899 ?  810 HOH A O   1 
HETATM 6104 O  O   . HOH I 5 .   ? -26.33800 -15.21700 -14.35700 1.000 36.64482 ?  811 HOH A O   1 
HETATM 6105 O  O   . HOH I 5 .   ? -20.61700 -20.06500 -21.97600 1.000 46.72320 ?  812 HOH A O   1 
HETATM 6106 O  O   . HOH I 5 .   ? 20.76700  -11.53000 -18.99000 1.000 37.61592 ?  813 HOH A O   1 
HETATM 6107 O  O   . HOH I 5 .   ? 14.89200  -12.27300 -7.61500  1.000 35.25091 ?  814 HOH A O   1 
HETATM 6108 O  O   . HOH I 5 .   ? 22.85500  9.96500   4.66400   1.000 41.93061 ?  815 HOH A O   1 
HETATM 6109 O  O   . HOH I 5 .   ? -10.14500 -22.10200 -23.26800 1.000 40.23554 ?  816 HOH A O   1 
HETATM 6110 O  O   . HOH I 5 .   ? 7.66300   -5.63700  4.09900   1.000 24.87930 ?  817 HOH A O   1 
HETATM 6111 O  O   . HOH I 5 .   ? 17.32400  -7.93800  -6.91000  1.000 35.84096 ?  818 HOH A O   1 
HETATM 6112 O  O   . HOH I 5 .   ? -3.51700  -22.84300 -9.81700  1.000 27.13067 ?  819 HOH A O   1 
HETATM 6113 O  O   . HOH I 5 .   ? 17.98000  24.04100  -12.70400 1.000 34.62903 ?  820 HOH A O   1 
HETATM 6114 O  O   . HOH I 5 .   ? 5.91400   7.93100   -21.36600 1.000 34.30660 ?  821 HOH A O   1 
HETATM 6115 O  O   . HOH I 5 .   ? 16.36900  -7.33500  3.69500   1.000 34.15653 ?  822 HOH A O   1 
HETATM 6116 O  O   . HOH I 5 .   ? 17.26200  -6.30400  6.85800   1.000 38.59807 ?  823 HOH A O   1 
HETATM 6117 O  O   . HOH I 5 .   ? 1.74800   -28.46200 -10.17700 1.000 46.23326 ?  824 HOH A O   1 
HETATM 6118 O  O   . HOH I 5 .   ? 6.67800   -12.92900 -39.86400 1.000 45.17682 ?  825 HOH A O   1 
HETATM 6119 O  O   . HOH I 5 .   ? 19.38600  12.85900  3.42900   1.000 37.20248 ?  826 HOH A O   1 
HETATM 6120 O  O   . HOH I 5 .   ? 4.45200   -20.65900 -36.69300 1.000 35.14797 ?  827 HOH A O   1 
HETATM 6121 O  O   . HOH I 5 .   ? -13.53900 6.41600   -15.12200 1.000 44.66225 ?  828 HOH A O   1 
HETATM 6122 O  O   . HOH I 5 .   ? -24.09500 -22.03500 -14.94100 1.000 45.14876 ?  829 HOH A O   1 
HETATM 6123 O  O   . HOH I 5 .   ? -7.79400  -29.49800 -12.61700 1.000 39.74574 ?  830 HOH A O   1 
HETATM 6124 O  O   . HOH I 5 .   ? -31.58900 -10.39400 -6.88700  1.000 33.72036 ?  831 HOH A O   1 
HETATM 6125 O  O   . HOH I 5 .   ? 0.33500   13.56800  4.75800   1.000 55.76740 ?  832 HOH A O   1 
HETATM 6126 O  O   . HOH I 5 .   ? -3.68000  -8.81600  8.91600   1.000 28.55771 ?  833 HOH A O   1 
HETATM 6127 O  O   . HOH I 5 .   ? -4.55600  -24.73500 -7.37800  1.000 38.09021 ?  834 HOH A O   1 
HETATM 6128 O  O   . HOH I 5 .   ? -27.468   -21.914   -10.026   1.000 34.41460 ?  835 HOH A O   1 
HETATM 6129 O  O   . HOH I 5 .   ? 16.82300  0.25500   -23.79300 1.000 30.34807 ?  836 HOH A O   1 
HETATM 6130 O  O   . HOH I 5 .   ? 1.54800   15.87100  -23.24000 1.000 39.96550 ?  837 HOH A O   1 
HETATM 6131 O  O   . HOH I 5 .   ? -17.55700 4.31000   -12.02600 1.000 38.95346 ?  838 HOH A O   1 
HETATM 6132 O  O   . HOH I 5 .   ? 9.86200   12.96800  -23.83800 1.000 43.21345 ?  839 HOH A O   1 
HETATM 6133 O  O   . HOH I 5 .   ? 17.330    -11.582   -34.363   1.000 47.22803 ?  840 HOH A O   1 
HETATM 6134 O  O   . HOH I 5 .   ? -27.39500 -16.66700 -19.81400 1.000 45.95781 ?  841 HOH A O   1 
HETATM 6135 O  O   . HOH I 5 .   ? 19.78500  8.05900   -26.16700 1.000 44.70204 ?  842 HOH A O   1 
HETATM 6136 O  O   . HOH J 5 .   ? -6.64000  -4.60300  -54.10200 1.000 37.66936 ?  501 HOH B O   1 
HETATM 6137 O  O   . HOH J 5 .   ? -18.25700 24.38800  -40.34700 1.000 43.98415 ?  502 HOH B O   1 
HETATM 6138 O  O   . HOH J 5 .   ? -31.59100 -16.89100 -32.00700 1.000 42.50693 ?  503 HOH B O   1 
HETATM 6139 O  O   . HOH J 5 .   ? -0.82600  10.13800  -56.79200 1.000 47.27702 ?  504 HOH B O   1 
HETATM 6140 O  O   . HOH J 5 .   ? -9.24900  13.65800  -40.44100 1.000 49.69435 ?  505 HOH B O   1 
HETATM 6141 O  O   . HOH J 5 .   ? -32.80500 16.22700  -61.83300 1.000 46.37668 ?  506 HOH B O   1 
HETATM 6142 O  O   . HOH J 5 .   ? -21.96000 14.29800  -30.74100 1.000 33.90101 ?  507 HOH B O   1 
HETATM 6143 O  O   . HOH J 5 .   ? 10.27000  -1.42700  -47.26600 1.000 30.97044 ?  508 HOH B O   1 
HETATM 6144 O  O   . HOH J 5 .   ? -10.21900 -12.41300 -54.34500 1.000 34.53807 ?  509 HOH B O   1 
HETATM 6145 O  O   . HOH J 5 .   ? -19.07500 18.42400  -44.41200 1.000 35.66110 ?  510 HOH B O   1 
HETATM 6146 O  O   . HOH J 5 .   ? -7.34400  6.49300   -20.06100 1.000 41.68188 ?  511 HOH B O   1 
HETATM 6147 O  O   . HOH J 5 .   ? -20.98400 -11.97200 -22.73000 1.000 37.94177 ?  512 HOH B O   1 
HETATM 6148 O  O   . HOH J 5 .   ? 3.54800   12.91000  -60.44800 1.000 55.58813 ?  513 HOH B O   1 
HETATM 6149 O  O   . HOH J 5 .   ? -38.27400 14.10600  -47.30400 1.000 32.17199 ?  514 HOH B O   1 
HETATM 6150 O  O   . HOH J 5 .   ? 9.01600   3.81900   -40.43200 1.000 31.93893 ?  515 HOH B O   1 
HETATM 6151 O  O   . HOH J 5 .   ? -2.56200  3.63600   -37.14400 1.000 35.94355 ?  516 HOH B O   1 
HETATM 6152 O  O   . HOH J 5 .   ? -13.10500 5.71700   -34.84500 1.000 38.27054 ?  517 HOH B O   1 
HETATM 6153 O  O   . HOH J 5 .   ? -23.95300 12.46000  -57.88900 1.000 41.20907 ?  518 HOH B O   1 
HETATM 6154 O  O   . HOH J 5 .   ? -19.76800 -20.75300 -42.49300 1.000 41.75709 ?  519 HOH B O   1 
HETATM 6155 O  O   . HOH J 5 .   ? -0.01800  -12.19500 -49.57700 1.000 36.06840 ?  520 HOH B O   1 
HETATM 6156 O  O   . HOH J 5 .   ? -7.16900  11.24800  -48.96200 1.000 29.02086 ?  521 HOH B O   1 
HETATM 6157 O  O   . HOH J 5 .   ? -27.35400 -5.00800  -22.62000 1.000 25.95107 ?  522 HOH B O   1 
HETATM 6158 O  O   . HOH J 5 .   ? -20.29800 29.35000  -40.10400 1.000 51.99082 ?  523 HOH B O   1 
HETATM 6159 O  O   . HOH J 5 .   ? -41.14000 5.03600   -45.96900 1.000 38.24771 ?  524 HOH B O   1 
HETATM 6160 O  O   . HOH J 5 .   ? 6.17500   -0.56000  -44.55400 1.000 24.68515 ?  525 HOH B O   1 
HETATM 6161 O  O   . HOH J 5 .   ? -25.44600 0.35100   -39.98800 1.000 23.00806 ?  526 HOH B O   1 
HETATM 6162 O  O   . HOH J 5 .   ? -9.30800  -4.03400  -54.04300 1.000 34.76183 ?  527 HOH B O   1 
HETATM 6163 O  O   . HOH J 5 .   ? -20.31900 4.78400   -24.88300 1.000 35.48935 ?  528 HOH B O   1 
HETATM 6164 O  O   . HOH J 5 .   ? -7.15800  16.30300  -60.32700 1.000 54.55201 ?  529 HOH B O   1 
HETATM 6165 O  O   . HOH J 5 .   ? 0.78800   12.71100  -52.29600 1.000 38.67790 ?  530 HOH B O   1 
HETATM 6166 O  O   . HOH J 5 .   ? 10.09900  4.32500   -37.78600 1.000 40.49817 ?  531 HOH B O   1 
HETATM 6167 O  O   . HOH J 5 .   ? -29.52500 -16.05700 -42.40500 1.000 44.25945 ?  532 HOH B O   1 
HETATM 6168 O  O   . HOH J 5 .   ? 8.77600   11.15100  -51.40000 1.000 42.71764 ?  533 HOH B O   1 
HETATM 6169 O  O   . HOH J 5 .   ? -37.58800 -4.45400  -43.36600 1.000 36.37804 ?  534 HOH B O   1 
HETATM 6170 O  O   . HOH J 5 .   ? -19.48500 -5.73700  -22.28600 1.000 28.77780 ?  535 HOH B O   1 
HETATM 6171 O  O   . HOH J 5 .   ? -10.64600 6.30800   -25.99200 1.000 23.25674 ?  536 HOH B O   1 
HETATM 6172 O  O   . HOH J 5 .   ? -23.23900 6.91800   -51.31100 1.000 37.39609 ?  537 HOH B O   1 
HETATM 6173 O  O   . HOH J 5 .   ? 2.50400   14.84700  -53.46800 1.000 46.47693 ?  538 HOH B O   1 
HETATM 6174 O  O   . HOH J 5 .   ? -2.98100  5.31000   -39.42200 1.000 28.97143 ?  539 HOH B O   1 
HETATM 6175 O  O   . HOH J 5 .   ? -37.61200 2.59600   -33.40100 1.000 40.24432 ?  540 HOH B O   1 
HETATM 6176 O  O   . HOH J 5 .   ? 6.95500   -6.84800  -50.01100 1.000 31.40045 ?  541 HOH B O   1 
HETATM 6177 O  O   . HOH J 5 .   ? -12.23700 15.04400  -38.26000 1.000 37.13856 ?  542 HOH B O   1 
HETATM 6178 O  O   . HOH J 5 .   ? -12.86700 12.03800  -29.79500 1.000 44.81316 ?  543 HOH B O   1 
HETATM 6179 O  O   . HOH J 5 .   ? -14.28100 -14.55200 -54.01200 1.000 34.46118 ?  544 HOH B O   1 
HETATM 6180 O  O   . HOH J 5 .   ? -30.02000 0.01600   -31.02100 1.000 38.08251 ?  545 HOH B O   1 
HETATM 6181 O  O   . HOH J 5 .   ? -3.59800  2.21900   -49.03500 1.000 24.66586 ?  546 HOH B O   1 
HETATM 6182 O  O   . HOH J 5 .   ? -24.92600 -3.25900  -49.22700 1.000 35.03950 ?  547 HOH B O   1 
HETATM 6183 O  O   . HOH J 5 .   ? -15.19100 10.26400  -32.53700 1.000 46.52016 ?  548 HOH B O   1 
HETATM 6184 O  O   . HOH J 5 .   ? -38.07100 -2.10800  -37.41900 1.000 37.32511 ?  549 HOH B O   1 
HETATM 6185 O  O   . HOH J 5 .   ? -37.49200 25.12500  -35.28500 1.000 42.75474 ?  550 HOH B O   1 
HETATM 6186 O  O   . HOH J 5 .   ? -39.95400 11.32100  -38.66400 1.000 37.43261 ?  551 HOH B O   1 
HETATM 6187 O  O   . HOH J 5 .   ? -5.15300  -7.77700  -51.72200 1.000 27.89694 ?  552 HOH B O   1 
HETATM 6188 O  O   . HOH J 5 .   ? 10.41600  0.01900   -37.34600 1.000 37.44179 ?  553 HOH B O   1 
HETATM 6189 O  O   . HOH J 5 .   ? -19.33700 -21.59600 -39.57700 1.000 42.31006 ?  554 HOH B O   1 
HETATM 6190 O  O   . HOH J 5 .   ? 3.73300   1.99700   -41.39300 1.000 31.27269 ?  555 HOH B O   1 
HETATM 6191 O  O   . HOH J 5 .   ? -10.82700 -1.32100  -52.56200 1.000 30.13064 ?  556 HOH B O   1 
HETATM 6192 O  O   . HOH J 5 .   ? -42.79600 13.06200  -31.44300 1.000 47.19050 ?  557 HOH B O   1 
HETATM 6193 O  O   . HOH J 5 .   ? -27.91300 -10.23800 -21.52600 1.000 32.93316 ?  558 HOH B O   1 
HETATM 6194 O  O   . HOH J 5 .   ? -19.08700 20.22800  -33.40500 1.000 39.49495 ?  559 HOH B O   1 
HETATM 6195 O  O   . HOH J 5 .   ? -40.94900 2.21200   -43.75300 1.000 33.51098 ?  560 HOH B O   1 
HETATM 6196 O  O   . HOH J 5 .   ? -14.41000 12.07000  -50.36900 1.000 36.30160 ?  561 HOH B O   1 
HETATM 6197 O  O   . HOH J 5 .   ? -18.28800 2.41500   -22.50600 1.000 40.37785 ?  562 HOH B O   1 
HETATM 6198 O  O   . HOH J 5 .   ? 5.74900   3.27900   -41.18800 1.000 35.88125 ?  563 HOH B O   1 
HETATM 6199 O  O   . HOH J 5 .   ? -17.34400 -8.80000  -23.18200 1.000 22.20369 ?  564 HOH B O   1 
HETATM 6200 O  O   . HOH J 5 .   ? -6.93900  12.04200  -61.54300 1.000 44.41657 ?  565 HOH B O   1 
HETATM 6201 O  O   . HOH J 5 .   ? -23.35800 -16.59700 -25.68500 1.000 36.79179 ?  566 HOH B O   1 
HETATM 6202 O  O   . HOH J 5 .   ? -4.50500  -3.51200  -53.84200 1.000 28.09253 ?  567 HOH B O   1 
HETATM 6203 O  O   . HOH J 5 .   ? -9.82700  -14.65600 -38.26500 1.000 36.47004 ?  568 HOH B O   1 
HETATM 6204 O  O   . HOH J 5 .   ? -19.75700 -5.82400  -24.71400 1.000 34.81835 ?  569 HOH B O   1 
HETATM 6205 O  O   . HOH J 5 .   ? -1.88400  -8.21300  -42.12300 1.000 30.81618 ?  570 HOH B O   1 
HETATM 6206 O  O   . HOH J 5 .   ? -29.83900 2.90300   -31.84900 1.000 27.08356 ?  571 HOH B O   1 
HETATM 6207 O  O   . HOH J 5 .   ? -2.83800  -13.23800 -47.78100 1.000 31.08262 ?  572 HOH B O   1 
HETATM 6208 O  O   . HOH J 5 .   ? -13.05300 -12.93200 -41.54700 1.000 29.40141 ?  573 HOH B O   1 
HETATM 6209 O  O   . HOH J 5 .   ? -4.85000  2.89200   -38.30100 1.000 26.69180 ?  574 HOH B O   1 
HETATM 6210 O  O   . HOH J 5 .   ? 12.55000  -2.65100  -53.25500 1.000 35.49605 ?  575 HOH B O   1 
HETATM 6211 O  O   . HOH J 5 .   ? -39.47600 8.76200   -44.53800 1.000 32.92894 ?  576 HOH B O   1 
HETATM 6212 O  O   . HOH J 5 .   ? -20.09100 13.84900  -38.90300 1.000 35.13461 ?  577 HOH B O   1 
HETATM 6213 O  O   . HOH J 5 .   ? -25.58200 -23.97800 -35.96600 1.000 44.42593 ?  578 HOH B O   1 
HETATM 6214 O  O   . HOH J 5 .   ? -25.91900 -12.12700 -23.04000 1.000 44.77096 ?  579 HOH B O   1 
HETATM 6215 O  O   . HOH J 5 .   ? -18.73800 -18.12500 -25.64700 1.000 32.87854 ?  580 HOH B O   1 
HETATM 6216 O  O   . HOH J 5 .   ? 7.24200   3.08700   -45.77200 1.000 32.20887 ?  581 HOH B O   1 
HETATM 6217 O  O   . HOH J 5 .   ? -16.07900 16.57400  -64.17900 1.000 45.44399 ?  582 HOH B O   1 
HETATM 6218 O  O   . HOH J 5 .   ? -31.73000 -1.41600  -24.74300 1.000 29.63408 ?  583 HOH B O   1 
HETATM 6219 O  O   . HOH J 5 .   ? -17.83200 16.21100  -62.09200 1.000 39.42202 ?  584 HOH B O   1 
HETATM 6220 O  O   . HOH J 5 .   ? -39.65000 13.54500  -37.15900 1.000 36.58818 ?  585 HOH B O   1 
HETATM 6221 O  O   . HOH J 5 .   ? -10.10200 15.23500  -41.80100 1.000 46.20957 ?  586 HOH B O   1 
HETATM 6222 O  O   . HOH J 5 .   ? -13.32600 -10.59200 -42.68600 1.000 25.23481 ?  587 HOH B O   1 
HETATM 6223 O  O   . HOH J 5 .   ? 9.36900   13.40700  -45.44100 1.000 45.03583 ?  588 HOH B O   1 
HETATM 6224 O  O   . HOH J 5 .   ? 6.96500   -9.87500  -51.96700 1.000 39.84823 ?  589 HOH B O   1 
HETATM 6225 O  O   . HOH J 5 .   ? -11.27300 -9.23900  -34.66500 1.000 34.04104 ?  590 HOH B O   1 
HETATM 6226 O  O   . HOH J 5 .   ? -28.30400 -1.82700  -31.87200 1.000 28.51611 ?  591 HOH B O   1 
HETATM 6227 O  O   . HOH J 5 .   ? -39.43100 12.69800  -40.83600 1.000 34.91610 ?  592 HOH B O   1 
HETATM 6228 O  O   . HOH J 5 .   ? -36.82700 7.40400   -43.73100 1.000 33.64147 ?  593 HOH B O   1 
HETATM 6229 O  O   . HOH J 5 .   ? -35.13300 2.32900   -33.31200 1.000 28.60538 ?  594 HOH B O   1 
HETATM 6230 O  O   . HOH J 5 .   ? -14.65300 8.62400   -37.26300 1.000 44.16788 ?  595 HOH B O   1 
HETATM 6231 O  O   . HOH J 5 .   ? -33.74100 3.17400   -47.99500 1.000 31.27496 ?  596 HOH B O   1 
HETATM 6232 O  O   . HOH J 5 .   ? -10.76200 3.04600   -37.92100 1.000 39.07554 ?  597 HOH B O   1 
HETATM 6233 O  O   . HOH J 5 .   ? -28.64500 -14.86800 -46.42300 1.000 48.62375 ?  598 HOH B O   1 
HETATM 6234 O  O   . HOH J 5 .   ? -11.65700 -19.81000 -34.55400 1.000 40.32269 ?  599 HOH B O   1 
HETATM 6235 O  O   . HOH J 5 .   ? -26.63600 -18.88000 -45.35200 1.000 43.30544 ?  600 HOH B O   1 
HETATM 6236 O  O   . HOH J 5 .   ? 9.59800   -0.52100  -44.67600 1.000 34.87759 ?  601 HOH B O   1 
HETATM 6237 O  O   . HOH J 5 .   ? -29.56000 -10.77300 -53.66100 1.000 43.88030 ?  602 HOH B O   1 
HETATM 6238 O  O   . HOH J 5 .   ? -35.88300 20.56200  -45.12500 1.000 43.35076 ?  603 HOH B O   1 
HETATM 6239 O  O   . HOH J 5 .   ? -40.92200 8.26400   -32.20400 1.000 38.53219 ?  604 HOH B O   1 
HETATM 6240 O  O   . HOH J 5 .   ? -32.94300 -10.69100 -25.12700 1.000 29.90862 ?  605 HOH B O   1 
HETATM 6241 O  O   . HOH J 5 .   ? 7.40900   -6.00200  -40.79300 1.000 39.81092 ?  606 HOH B O   1 
HETATM 6242 O  O   . HOH J 5 .   ? 5.95900   14.79100  -43.06500 1.000 47.25812 ?  607 HOH B O   1 
HETATM 6243 O  O   . HOH J 5 .   ? -11.30000 -13.10600 -34.15000 1.000 33.64862 ?  608 HOH B O   1 
HETATM 6244 O  O   . HOH J 5 .   ? 6.612     16.372    -58.959   1.000 42.84639 ?  609 HOH B O   1 
HETATM 6245 O  O   . HOH J 5 .   ? -32.43900 -8.60500  -33.68900 1.000 39.25942 ?  610 HOH B O   1 
HETATM 6246 O  O   . HOH J 5 .   ? -12.10200 -11.60600 -25.36200 1.000 35.04063 ?  611 HOH B O   1 
HETATM 6247 O  O   . HOH J 5 .   ? -11.91400 1.37100   -36.77100 1.000 36.39216 ?  612 HOH B O   1 
HETATM 6248 O  O   . HOH J 5 .   ? 12.98800  1.14400   -47.96400 1.000 36.99146 ?  613 HOH B O   1 
HETATM 6249 O  O   . HOH J 5 .   ? -21.81800 -26.67800 -51.57800 1.000 59.10139 ?  614 HOH B O   1 
HETATM 6250 O  O   . HOH J 5 .   ? -15.17000 -1.95800  -58.73400 1.000 46.24599 ?  615 HOH B O   1 
HETATM 6251 O  O   . HOH J 5 .   ? -7.99100  -0.42300  -36.94000 1.000 37.33873 ?  616 HOH B O   1 
HETATM 6252 O  O   . HOH J 5 .   ? -30.32300 -18.14500 -41.63600 1.000 43.51689 ?  617 HOH B O   1 
HETATM 6253 O  O   . HOH J 5 .   ? -15.26500 1.48200   -59.00500 1.000 41.16595 ?  618 HOH B O   1 
HETATM 6254 O  O   . HOH J 5 .   ? -14.17200 21.45900  -50.53700 1.000 44.43910 ?  619 HOH B O   1 
HETATM 6255 O  O   . HOH J 5 .   ? -38.79000 -0.07500  -37.98400 1.000 40.86554 ?  620 HOH B O   1 
HETATM 6256 O  O   . HOH J 5 .   ? -6.59600  18.69600  -55.34300 1.000 48.95857 ?  621 HOH B O   1 
HETATM 6257 O  O   . HOH J 5 .   ? 8.00900   1.19400   -44.22400 1.000 38.39722 ?  622 HOH B O   1 
HETATM 6258 O  O   . HOH J 5 .   ? -8.94800  -12.25000 -56.64700 1.000 40.34035 ?  623 HOH B O   1 
HETATM 6259 O  O   . HOH J 5 .   ? 0.88100   4.84700   -36.54900 1.000 35.46147 ?  624 HOH B O   1 
HETATM 6260 O  O   . HOH J 5 .   ? -12.95800 8.31800   -34.49800 1.000 42.19515 ?  625 HOH B O   1 
HETATM 6261 O  O   . HOH J 5 .   ? -34.33400 -3.13200  -26.50400 1.000 41.40732 ?  626 HOH B O   1 
HETATM 6262 O  O   . HOH J 5 .   ? -8.34600  22.30800  -56.11500 1.000 41.33715 ?  627 HOH B O   1 
HETATM 6263 O  O   . HOH J 5 .   ? -11.96900 -0.63600  -35.53400 1.000 39.19730 ?  628 HOH B O   1 
HETATM 6264 O  O   . HOH J 5 .   ? -11.55800 -15.93900 -31.37200 1.000 44.09777 ?  629 HOH B O   1 
HETATM 6265 O  O   . HOH J 5 .   ? 2.55900   5.57500   -37.88900 1.000 40.53856 ?  630 HOH B O   1 
HETATM 6266 O  O   . HOH J 5 .   ? -11.16000 -3.80600  -33.64100 1.000 36.93738 ?  631 HOH B O   1 
HETATM 6267 O  O   . HOH J 5 .   ? -26.09000 27.73100  -41.36500 1.000 50.05773 ?  632 HOH B O   1 
HETATM 6268 O  O   . HOH J 5 .   ? -12.56100 -11.81100 -55.15900 1.000 34.97989 ?  633 HOH B O   1 
HETATM 6269 O  O   . HOH J 5 .   ? -9.140    19.208    -66.738   1.000 46.95051 ?  634 HOH B O   1 
HETATM 6270 O  O   . HOH J 5 .   ? -18.71600 -20.67600 -32.01600 1.000 45.52213 ?  635 HOH B O   1 
HETATM 6271 O  O   . HOH J 5 .   ? -35.01800 -18.85800 -38.33300 1.000 44.86006 ?  636 HOH B O   1 
HETATM 6272 O  O   . HOH J 5 .   ? -33.55400 -12.07500 -44.99900 1.000 36.33592 ?  637 HOH B O   1 
HETATM 6273 O  O   . HOH J 5 .   ? 5.33900   -12.76200 -41.85900 1.000 42.89089 ?  638 HOH B O   1 
HETATM 6274 O  O   . HOH J 5 .   ? -33.36000 -10.90200 -31.65800 1.000 34.45660 ?  639 HOH B O   1 
HETATM 6275 O  O   . HOH J 5 .   ? -21.76400 10.33600  -30.85400 1.000 40.31101 ?  640 HOH B O   1 
HETATM 6276 O  O   . HOH J 5 .   ? -33.80500 -8.22600  -39.48000 1.000 37.24399 ?  641 HOH B O   1 
HETATM 6277 O  O   . HOH J 5 .   ? 13.90900  -1.04000  -54.20600 1.000 40.96091 ?  642 HOH B O   1 
HETATM 6278 O  O   . HOH J 5 .   ? -24.92200 -14.56200 -24.26600 1.000 41.09705 ?  643 HOH B O   1 
HETATM 6279 O  O   . HOH J 5 .   ? -0.47500  17.09200  -40.69600 1.000 52.09055 ?  644 HOH B O   1 
HETATM 6280 O  O   . HOH J 5 .   ? -1.51000  14.73500  -40.88800 1.000 44.12988 ?  645 HOH B O   1 
HETATM 6281 O  O   . HOH J 5 .   ? -0.61300  15.92800  -42.62300 1.000 47.49081 ?  646 HOH B O   1 
HETATM 6282 O  O   . HOH J 5 .   ? -0.90000  14.79100  -44.87800 1.000 51.95476 ?  647 HOH B O   1 
# 
