data_8UYR
# 
_entry.id   8UYR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8UYR         pdb_00008uyr 10.2210/pdb8uyr/pdb 
WWPDB D_1000279185 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-27 
# 
_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                        8UYR 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-14 
_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                 2 
_pdbx_contact_author.email              rittle@berkeley.edu 
_pdbx_contact_author.name_first         Jonathan 
_pdbx_contact_author.name_last          Rittle 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6241-6253 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Liu, C.'    1 ? 
'Chen, S.'   2 ? 
'Rittle, J.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'A Widespread, Diiron-dependent Diterpenoid Hydroxylase' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, S.'   1 ? 
primary 'Liu, C.'    2 ? 
primary 'Rittle, J.' 3 ? 
# 
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 DitZ                 47305.555 2   ? ? ? ? 
2 non-polymer syn GLYCEROL             92.094    7   ? ? ? ? 
3 non-polymer syn 'MANGANESE (II) ION' 54.938    4   ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'      24.305    1   ? ? ? ? 
5 water       nat water                18.015    671 ? ? ? ? 
# 
_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       
;MKTEDMVMISIDDHVVEPADIFEKHFPKSLMDQAPKLTAHPRNPRVQAWQFQGTVVGSSGLNAVVSWPKHEWGMDPTGYA
EMRPAVYDMDMRVRDMDANGTLAATLFATFPGFAGTHLASLPDKKLSLAACRAFNDWVVGEVPDAHPGRFIPIGIIPFFD
ADESVAEVHRIAAMGCRSISIPETPYGVGEGFPDFKSGYWDPIFKACVEHNIVLSLHIGGGINLVKRPEGFDIDNMLMLT
PLISTIAATDMMLSGAFKKFPDLKVAMSEGGVGWVAPWLDRLDRHIVNQSWTGTSFLPKGMTPTDVWRKNFLACYITEPS
GLNNRHRLGVDTIAWECDYPHSDSTWPRSPETLKSELDAARCTDEEVDKITFANAAKFFDWDPFEHIPREEATVGALRAR
ATDVDISETSKEEYRRRYELTHS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKTEDMVMISIDDHVVEPADIFEKHFPKSLMDQAPKLTAHPRNPRVQAWQFQGTVVGSSGLNAVVSWPKHEWGMDPTGYA
EMRPAVYDMDMRVRDMDANGTLAATLFATFPGFAGTHLASLPDKKLSLAACRAFNDWVVGEVPDAHPGRFIPIGIIPFFD
ADESVAEVHRIAAMGCRSISIPETPYGVGEGFPDFKSGYWDPIFKACVEHNIVLSLHIGGGINLVKRPEGFDIDNMLMLT
PLISTIAATDMMLSGAFKKFPDLKVAMSEGGVGWVAPWLDRLDRHIVNQSWTGTSFLPKGMTPTDVWRKNFLACYITEPS
GLNNRHRLGVDTIAWECDYPHSDSTWPRSPETLKSELDAARCTDEEVDKITFANAAKFFDWDPFEHIPREEATVGALRAR
ATDVDISETSKEEYRRRYELTHS
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCEROL             GOL 
3 'MANGANESE (II) ION' MN  
4 'MAGNESIUM ION'      MG  
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   LYS n 
1 3   THR n 
1 4   GLU n 
1 5   ASP n 
1 6   MET n 
1 7   VAL n 
1 8   MET n 
1 9   ILE n 
1 10  SER n 
1 11  ILE n 
1 12  ASP n 
1 13  ASP n 
1 14  HIS n 
1 15  VAL n 
1 16  VAL n 
1 17  GLU n 
1 18  PRO n 
1 19  ALA n 
1 20  ASP n 
1 21  ILE n 
1 22  PHE n 
1 23  GLU n 
1 24  LYS n 
1 25  HIS n 
1 26  PHE n 
1 27  PRO n 
1 28  LYS n 
1 29  SER n 
1 30  LEU n 
1 31  MET n 
1 32  ASP n 
1 33  GLN n 
1 34  ALA n 
1 35  PRO n 
1 36  LYS n 
1 37  LEU n 
1 38  THR n 
1 39  ALA n 
1 40  HIS n 
1 41  PRO n 
1 42  ARG n 
1 43  ASN n 
1 44  PRO n 
1 45  ARG n 
1 46  VAL n 
1 47  GLN n 
1 48  ALA n 
1 49  TRP n 
1 50  GLN n 
1 51  PHE n 
1 52  GLN n 
1 53  GLY n 
1 54  THR n 
1 55  VAL n 
1 56  VAL n 
1 57  GLY n 
1 58  SER n 
1 59  SER n 
1 60  GLY n 
1 61  LEU n 
1 62  ASN n 
1 63  ALA n 
1 64  VAL n 
1 65  VAL n 
1 66  SER n 
1 67  TRP n 
1 68  PRO n 
1 69  LYS n 
1 70  HIS n 
1 71  GLU n 
1 72  TRP n 
1 73  GLY n 
1 74  MET n 
1 75  ASP n 
1 76  PRO n 
1 77  THR n 
1 78  GLY n 
1 79  TYR n 
1 80  ALA n 
1 81  GLU n 
1 82  MET n 
1 83  ARG n 
1 84  PRO n 
1 85  ALA n 
1 86  VAL n 
1 87  TYR n 
1 88  ASP n 
1 89  MET n 
1 90  ASP n 
1 91  MET n 
1 92  ARG n 
1 93  VAL n 
1 94  ARG n 
1 95  ASP n 
1 96  MET n 
1 97  ASP n 
1 98  ALA n 
1 99  ASN n 
1 100 GLY n 
1 101 THR n 
1 102 LEU n 
1 103 ALA n 
1 104 ALA n 
1 105 THR n 
1 106 LEU n 
1 107 PHE n 
1 108 ALA n 
1 109 THR n 
1 110 PHE n 
1 111 PRO n 
1 112 GLY n 
1 113 PHE n 
1 114 ALA n 
1 115 GLY n 
1 116 THR n 
1 117 HIS n 
1 118 LEU n 
1 119 ALA n 
1 120 SER n 
1 121 LEU n 
1 122 PRO n 
1 123 ASP n 
1 124 LYS n 
1 125 LYS n 
1 126 LEU n 
1 127 SER n 
1 128 LEU n 
1 129 ALA n 
1 130 ALA n 
1 131 CYS n 
1 132 ARG n 
1 133 ALA n 
1 134 PHE n 
1 135 ASN n 
1 136 ASP n 
1 137 TRP n 
1 138 VAL n 
1 139 VAL n 
1 140 GLY n 
1 141 GLU n 
1 142 VAL n 
1 143 PRO n 
1 144 ASP n 
1 145 ALA n 
1 146 HIS n 
1 147 PRO n 
1 148 GLY n 
1 149 ARG n 
1 150 PHE n 
1 151 ILE n 
1 152 PRO n 
1 153 ILE n 
1 154 GLY n 
1 155 ILE n 
1 156 ILE n 
1 157 PRO n 
1 158 PHE n 
1 159 PHE n 
1 160 ASP n 
1 161 ALA n 
1 162 ASP n 
1 163 GLU n 
1 164 SER n 
1 165 VAL n 
1 166 ALA n 
1 167 GLU n 
1 168 VAL n 
1 169 HIS n 
1 170 ARG n 
1 171 ILE n 
1 172 ALA n 
1 173 ALA n 
1 174 MET n 
1 175 GLY n 
1 176 CYS n 
1 177 ARG n 
1 178 SER n 
1 179 ILE n 
1 180 SER n 
1 181 ILE n 
1 182 PRO n 
1 183 GLU n 
1 184 THR n 
1 185 PRO n 
1 186 TYR n 
1 187 GLY n 
1 188 VAL n 
1 189 GLY n 
1 190 GLU n 
1 191 GLY n 
1 192 PHE n 
1 193 PRO n 
1 194 ASP n 
1 195 PHE n 
1 196 LYS n 
1 197 SER n 
1 198 GLY n 
1 199 TYR n 
1 200 TRP n 
1 201 ASP n 
1 202 PRO n 
1 203 ILE n 
1 204 PHE n 
1 205 LYS n 
1 206 ALA n 
1 207 CYS n 
1 208 VAL n 
1 209 GLU n 
1 210 HIS n 
1 211 ASN n 
1 212 ILE n 
1 213 VAL n 
1 214 LEU n 
1 215 SER n 
1 216 LEU n 
1 217 HIS n 
1 218 ILE n 
1 219 GLY n 
1 220 GLY n 
1 221 GLY n 
1 222 ILE n 
1 223 ASN n 
1 224 LEU n 
1 225 VAL n 
1 226 LYS n 
1 227 ARG n 
1 228 PRO n 
1 229 GLU n 
1 230 GLY n 
1 231 PHE n 
1 232 ASP n 
1 233 ILE n 
1 234 ASP n 
1 235 ASN n 
1 236 MET n 
1 237 LEU n 
1 238 MET n 
1 239 LEU n 
1 240 THR n 
1 241 PRO n 
1 242 LEU n 
1 243 ILE n 
1 244 SER n 
1 245 THR n 
1 246 ILE n 
1 247 ALA n 
1 248 ALA n 
1 249 THR n 
1 250 ASP n 
1 251 MET n 
1 252 MET n 
1 253 LEU n 
1 254 SER n 
1 255 GLY n 
1 256 ALA n 
1 257 PHE n 
1 258 LYS n 
1 259 LYS n 
1 260 PHE n 
1 261 PRO n 
1 262 ASP n 
1 263 LEU n 
1 264 LYS n 
1 265 VAL n 
1 266 ALA n 
1 267 MET n 
1 268 SER n 
1 269 GLU n 
1 270 GLY n 
1 271 GLY n 
1 272 VAL n 
1 273 GLY n 
1 274 TRP n 
1 275 VAL n 
1 276 ALA n 
1 277 PRO n 
1 278 TRP n 
1 279 LEU n 
1 280 ASP n 
1 281 ARG n 
1 282 LEU n 
1 283 ASP n 
1 284 ARG n 
1 285 HIS n 
1 286 ILE n 
1 287 VAL n 
1 288 ASN n 
1 289 GLN n 
1 290 SER n 
1 291 TRP n 
1 292 THR n 
1 293 GLY n 
1 294 THR n 
1 295 SER n 
1 296 PHE n 
1 297 LEU n 
1 298 PRO n 
1 299 LYS n 
1 300 GLY n 
1 301 MET n 
1 302 THR n 
1 303 PRO n 
1 304 THR n 
1 305 ASP n 
1 306 VAL n 
1 307 TRP n 
1 308 ARG n 
1 309 LYS n 
1 310 ASN n 
1 311 PHE n 
1 312 LEU n 
1 313 ALA n 
1 314 CYS n 
1 315 TYR n 
1 316 ILE n 
1 317 THR n 
1 318 GLU n 
1 319 PRO n 
1 320 SER n 
1 321 GLY n 
1 322 LEU n 
1 323 ASN n 
1 324 ASN n 
1 325 ARG n 
1 326 HIS n 
1 327 ARG n 
1 328 LEU n 
1 329 GLY n 
1 330 VAL n 
1 331 ASP n 
1 332 THR n 
1 333 ILE n 
1 334 ALA n 
1 335 TRP n 
1 336 GLU n 
1 337 CYS n 
1 338 ASP n 
1 339 TYR n 
1 340 PRO n 
1 341 HIS n 
1 342 SER n 
1 343 ASP n 
1 344 SER n 
1 345 THR n 
1 346 TRP n 
1 347 PRO n 
1 348 ARG n 
1 349 SER n 
1 350 PRO n 
1 351 GLU n 
1 352 THR n 
1 353 LEU n 
1 354 LYS n 
1 355 SER n 
1 356 GLU n 
1 357 LEU n 
1 358 ASP n 
1 359 ALA n 
1 360 ALA n 
1 361 ARG n 
1 362 CYS n 
1 363 THR n 
1 364 ASP n 
1 365 GLU n 
1 366 GLU n 
1 367 VAL n 
1 368 ASP n 
1 369 LYS n 
1 370 ILE n 
1 371 THR n 
1 372 PHE n 
1 373 ALA n 
1 374 ASN n 
1 375 ALA n 
1 376 ALA n 
1 377 LYS n 
1 378 PHE n 
1 379 PHE n 
1 380 ASP n 
1 381 TRP n 
1 382 ASP n 
1 383 PRO n 
1 384 PHE n 
1 385 GLU n 
1 386 HIS n 
1 387 ILE n 
1 388 PRO n 
1 389 ARG n 
1 390 GLU n 
1 391 GLU n 
1 392 ALA n 
1 393 THR n 
1 394 VAL n 
1 395 GLY n 
1 396 ALA n 
1 397 LEU n 
1 398 ARG n 
1 399 ALA n 
1 400 ARG n 
1 401 ALA n 
1 402 THR n 
1 403 ASP n 
1 404 VAL n 
1 405 ASP n 
1 406 ILE n 
1 407 SER n 
1 408 GLU n 
1 409 THR n 
1 410 SER n 
1 411 LYS n 
1 412 GLU n 
1 413 GLU n 
1 414 TYR n 
1 415 ARG n 
1 416 ARG n 
1 417 ARG n 
1 418 TYR n 
1 419 GLU n 
1 420 LEU n 
1 421 THR n 
1 422 HIS n 
1 423 SER 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                   423 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Rhodococcus rhodochrous' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1829 
_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 
ALA 'L-peptide linking' y ALANINE              ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE             ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE           ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'      ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE             ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE            ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'      ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE              ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL             'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE            ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE           ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE              ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE               ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE           ?                               'C5 H11 N O2 S'  149.211 
MG  non-polymer         . 'MAGNESIUM ION'      ?                               'Mg 2'           24.305  
MN  non-polymer         . 'MANGANESE (II) ION' ?                               'Mn 2'           54.938  
PHE 'L-peptide linking' y PHENYLALANINE        ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE              ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE               ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE            ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN           ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE             ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE               ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   THR 3   3   3   THR THR A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   ASP 5   5   5   ASP ASP A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   MET 8   8   8   MET MET A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  HIS 14  14  14  HIS HIS A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  PRO 18  18  18  PRO PRO A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  ASP 20  20  20  ASP ASP A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  HIS 25  25  25  HIS HIS A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  PRO 27  27  27  PRO PRO A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  MET 31  31  31  MET MET A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  GLN 33  33  33  GLN GLN A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  THR 38  38  38  THR THR A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  HIS 40  40  40  HIS HIS A . n 
A 1 41  PRO 41  41  41  PRO PRO A . n 
A 1 42  ARG 42  42  42  ARG ARG A . n 
A 1 43  ASN 43  43  43  ASN ASN A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  GLN 47  47  47  GLN GLN A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  TRP 49  49  49  TRP TRP A . n 
A 1 50  GLN 50  50  50  GLN GLN A . n 
A 1 51  PHE 51  51  51  PHE PHE A . n 
A 1 52  GLN 52  52  52  GLN GLN A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  TRP 67  67  67  TRP TRP A . n 
A 1 68  PRO 68  68  68  PRO PRO A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  HIS 70  70  70  HIS HIS A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  TRP 72  72  72  TRP TRP A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  MET 74  74  74  MET MET A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  TYR 79  79  79  TYR TYR A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  ALA 85  85  85  ALA ALA A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  ASP 88  88  88  ASP ASP A . n 
A 1 89  MET 89  89  89  MET MET A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  MET 91  91  91  MET MET A . n 
A 1 92  ARG 92  92  92  ARG ARG A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  ARG 94  94  94  ARG ARG A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  MET 96  96  96  MET MET A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 THR 101 101 101 THR THR A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 PHE 110 110 110 PHE PHE A . n 
A 1 111 PRO 111 111 111 PRO PRO A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 PHE 113 113 113 PHE PHE A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 ASP 123 123 123 ASP ASP A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 LYS 125 125 125 LYS LYS A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 CYS 131 131 131 CYS CYS A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 ASN 135 135 135 ASN ASN A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 TRP 137 137 137 TRP TRP A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 VAL 139 139 139 VAL VAL A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 HIS 146 146 146 HIS HIS A . n 
A 1 147 PRO 147 147 147 PRO PRO A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 ARG 149 149 149 ARG ARG A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 PRO 152 152 152 PRO PRO A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 PHE 158 158 158 PHE PHE A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 ASP 160 160 160 ASP ASP A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 HIS 169 169 169 HIS HIS A . n 
A 1 170 ARG 170 170 170 ARG ARG A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 MET 174 174 174 MET MET A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 CYS 176 176 176 CYS CYS A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 PRO 182 182 182 PRO PRO A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 GLU 190 190 190 GLU GLU A . n 
A 1 191 GLY 191 191 191 GLY GLY A . n 
A 1 192 PHE 192 192 192 PHE PHE A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 ASP 194 194 194 ASP ASP A . n 
A 1 195 PHE 195 195 195 PHE PHE A . n 
A 1 196 LYS 196 196 196 LYS LYS A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 TRP 200 200 200 TRP TRP A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 PHE 204 204 204 PHE PHE A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 CYS 207 207 207 CYS CYS A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 GLU 209 209 209 GLU GLU A . n 
A 1 210 HIS 210 210 210 HIS HIS A . n 
A 1 211 ASN 211 211 211 ASN ASN A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 HIS 217 217 217 HIS HIS A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 GLY 219 219 219 GLY GLY A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 ASN 223 223 223 ASN ASN A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 LYS 226 226 226 LYS LYS A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 PRO 228 228 228 PRO PRO A . n 
A 1 229 GLU 229 229 229 GLU GLU A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 PHE 231 231 231 PHE PHE A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 ILE 233 233 233 ILE ILE A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 MET 236 236 236 MET MET A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 MET 238 238 238 MET MET A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 THR 240 240 240 THR THR A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 ASP 250 250 250 ASP ASP A . n 
A 1 251 MET 251 251 251 MET MET A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 PHE 257 257 257 PHE PHE A . n 
A 1 258 LYS 258 258 258 LYS LYS A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 PHE 260 260 260 PHE PHE A . n 
A 1 261 PRO 261 261 261 PRO PRO A . n 
A 1 262 ASP 262 262 262 ASP ASP A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 LYS 264 264 264 LYS LYS A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 MET 267 267 267 MET MET A . n 
A 1 268 SER 268 268 268 SER SER A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 VAL 272 272 272 VAL VAL A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 TRP 274 274 274 TRP TRP A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 PRO 277 277 277 PRO PRO A . n 
A 1 278 TRP 278 278 278 TRP TRP A . n 
A 1 279 LEU 279 279 279 LEU LEU A . n 
A 1 280 ASP 280 280 280 ASP ASP A . n 
A 1 281 ARG 281 281 281 ARG ARG A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 ASP 283 283 283 ASP ASP A . n 
A 1 284 ARG 284 284 284 ARG ARG A . n 
A 1 285 HIS 285 285 285 HIS HIS A . n 
A 1 286 ILE 286 286 286 ILE ILE A . n 
A 1 287 VAL 287 287 287 VAL VAL A . n 
A 1 288 ASN 288 288 288 ASN ASN A . n 
A 1 289 GLN 289 289 289 GLN GLN A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 TRP 291 291 291 TRP TRP A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 THR 294 294 294 THR THR A . n 
A 1 295 SER 295 295 295 SER SER A . n 
A 1 296 PHE 296 296 296 PHE PHE A . n 
A 1 297 LEU 297 297 297 LEU LEU A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 LYS 299 299 299 LYS LYS A . n 
A 1 300 GLY 300 300 300 GLY GLY A . n 
A 1 301 MET 301 301 301 MET MET A . n 
A 1 302 THR 302 302 302 THR THR A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 ASP 305 305 305 ASP ASP A . n 
A 1 306 VAL 306 306 306 VAL VAL A . n 
A 1 307 TRP 307 307 307 TRP TRP A . n 
A 1 308 ARG 308 308 308 ARG ARG A . n 
A 1 309 LYS 309 309 309 LYS LYS A . n 
A 1 310 ASN 310 310 310 ASN ASN A . n 
A 1 311 PHE 311 311 311 PHE PHE A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 CYS 314 314 314 CYS CYS A . n 
A 1 315 TYR 315 315 315 TYR TYR A . n 
A 1 316 ILE 316 316 316 ILE ILE A . n 
A 1 317 THR 317 317 317 THR THR A . n 
A 1 318 GLU 318 318 318 GLU GLU A . n 
A 1 319 PRO 319 319 319 PRO PRO A . n 
A 1 320 SER 320 320 320 SER SER A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 LEU 322 322 322 LEU LEU A . n 
A 1 323 ASN 323 323 323 ASN ASN A . n 
A 1 324 ASN 324 324 324 ASN ASN A . n 
A 1 325 ARG 325 325 325 ARG ARG A . n 
A 1 326 HIS 326 326 326 HIS HIS A . n 
A 1 327 ARG 327 327 327 ARG ARG A . n 
A 1 328 LEU 328 328 328 LEU LEU A . n 
A 1 329 GLY 329 329 329 GLY GLY A . n 
A 1 330 VAL 330 330 330 VAL VAL A . n 
A 1 331 ASP 331 331 331 ASP ASP A . n 
A 1 332 THR 332 332 332 THR THR A . n 
A 1 333 ILE 333 333 333 ILE ILE A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 TRP 335 335 335 TRP TRP A . n 
A 1 336 GLU 336 336 336 GLU GLU A . n 
A 1 337 CYS 337 337 337 CYS CYS A . n 
A 1 338 ASP 338 338 338 ASP ASP A . n 
A 1 339 TYR 339 339 339 TYR TYR A . n 
A 1 340 PRO 340 340 340 PRO PRO A . n 
A 1 341 HIS 341 341 341 HIS HIS A . n 
A 1 342 SER 342 342 342 SER SER A . n 
A 1 343 ASP 343 343 343 ASP ASP A . n 
A 1 344 SER 344 344 344 SER SER A . n 
A 1 345 THR 345 345 345 THR THR A . n 
A 1 346 TRP 346 346 346 TRP TRP A . n 
A 1 347 PRO 347 347 347 PRO PRO A . n 
A 1 348 ARG 348 348 348 ARG ARG A . n 
A 1 349 SER 349 349 349 SER SER A . n 
A 1 350 PRO 350 350 350 PRO PRO A . n 
A 1 351 GLU 351 351 351 GLU GLU A . n 
A 1 352 THR 352 352 352 THR THR A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 LYS 354 354 354 LYS LYS A . n 
A 1 355 SER 355 355 355 SER SER A . n 
A 1 356 GLU 356 356 356 GLU GLU A . n 
A 1 357 LEU 357 357 357 LEU LEU A . n 
A 1 358 ASP 358 358 358 ASP ASP A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 ALA 360 360 360 ALA ALA A . n 
A 1 361 ARG 361 361 361 ARG ARG A . n 
A 1 362 CYS 362 362 362 CYS CYS A . n 
A 1 363 THR 363 363 363 THR THR A . n 
A 1 364 ASP 364 364 364 ASP ASP A . n 
A 1 365 GLU 365 365 365 GLU GLU A . n 
A 1 366 GLU 366 366 366 GLU GLU A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 ASP 368 368 368 ASP ASP A . n 
A 1 369 LYS 369 369 369 LYS LYS A . n 
A 1 370 ILE 370 370 370 ILE ILE A . n 
A 1 371 THR 371 371 371 THR THR A . n 
A 1 372 PHE 372 372 372 PHE PHE A . n 
A 1 373 ALA 373 373 373 ALA ALA A . n 
A 1 374 ASN 374 374 374 ASN ASN A . n 
A 1 375 ALA 375 375 375 ALA ALA A . n 
A 1 376 ALA 376 376 376 ALA ALA A . n 
A 1 377 LYS 377 377 377 LYS LYS A . n 
A 1 378 PHE 378 378 378 PHE PHE A . n 
A 1 379 PHE 379 379 379 PHE PHE A . n 
A 1 380 ASP 380 380 380 ASP ASP A . n 
A 1 381 TRP 381 381 381 TRP TRP A . n 
A 1 382 ASP 382 382 382 ASP ASP A . n 
A 1 383 PRO 383 383 383 PRO PRO A . n 
A 1 384 PHE 384 384 384 PHE PHE A . n 
A 1 385 GLU 385 385 385 GLU GLU A . n 
A 1 386 HIS 386 386 386 HIS HIS A . n 
A 1 387 ILE 387 387 387 ILE ILE A . n 
A 1 388 PRO 388 388 388 PRO PRO A . n 
A 1 389 ARG 389 389 389 ARG ARG A . n 
A 1 390 GLU 390 390 390 GLU GLU A . n 
A 1 391 GLU 391 391 391 GLU GLU A . n 
A 1 392 ALA 392 392 392 ALA ALA A . n 
A 1 393 THR 393 393 393 THR THR A . n 
A 1 394 VAL 394 394 394 VAL VAL A . n 
A 1 395 GLY 395 395 395 GLY GLY A . n 
A 1 396 ALA 396 396 396 ALA ALA A . n 
A 1 397 LEU 397 397 397 LEU LEU A . n 
A 1 398 ARG 398 398 398 ARG ARG A . n 
A 1 399 ALA 399 399 399 ALA ALA A . n 
A 1 400 ARG 400 400 400 ARG ARG A . n 
A 1 401 ALA 401 401 401 ALA ALA A . n 
A 1 402 THR 402 402 402 THR THR A . n 
A 1 403 ASP 403 403 403 ASP ASP A . n 
A 1 404 VAL 404 404 404 VAL VAL A . n 
A 1 405 ASP 405 405 405 ASP ASP A . n 
A 1 406 ILE 406 406 406 ILE ILE A . n 
A 1 407 SER 407 407 407 SER SER A . n 
A 1 408 GLU 408 408 408 GLU GLU A . n 
A 1 409 THR 409 409 409 THR THR A . n 
A 1 410 SER 410 410 410 SER SER A . n 
A 1 411 LYS 411 411 411 LYS LYS A . n 
A 1 412 GLU 412 412 412 GLU GLU A . n 
A 1 413 GLU 413 413 413 GLU GLU A . n 
A 1 414 TYR 414 414 414 TYR TYR A . n 
A 1 415 ARG 415 415 415 ARG ARG A . n 
A 1 416 ARG 416 416 416 ARG ARG A . n 
A 1 417 ARG 417 417 417 ARG ARG A . n 
A 1 418 TYR 418 418 418 TYR TYR A . n 
A 1 419 GLU 419 419 419 GLU GLU A . n 
A 1 420 LEU 420 420 420 LEU LEU A . n 
A 1 421 THR 421 421 421 THR THR A . n 
A 1 422 HIS 422 422 422 HIS HIS A . n 
A 1 423 SER 423 423 423 SER SER A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   LYS 2   2   2   LYS LYS B . n 
B 1 3   THR 3   3   3   THR THR B . n 
B 1 4   GLU 4   4   4   GLU GLU B . n 
B 1 5   ASP 5   5   5   ASP ASP B . n 
B 1 6   MET 6   6   6   MET MET B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   MET 8   8   8   MET MET B . n 
B 1 9   ILE 9   9   9   ILE ILE B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  ILE 11  11  11  ILE ILE B . n 
B 1 12  ASP 12  12  12  ASP ASP B . n 
B 1 13  ASP 13  13  13  ASP ASP B . n 
B 1 14  HIS 14  14  14  HIS HIS B . n 
B 1 15  VAL 15  15  15  VAL VAL B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  GLU 17  17  17  GLU GLU B . n 
B 1 18  PRO 18  18  18  PRO PRO B . n 
B 1 19  ALA 19  19  19  ALA ALA B . n 
B 1 20  ASP 20  20  20  ASP ASP B . n 
B 1 21  ILE 21  21  21  ILE ILE B . n 
B 1 22  PHE 22  22  22  PHE PHE B . n 
B 1 23  GLU 23  23  23  GLU GLU B . n 
B 1 24  LYS 24  24  24  LYS LYS B . n 
B 1 25  HIS 25  25  25  HIS HIS B . n 
B 1 26  PHE 26  26  26  PHE PHE B . n 
B 1 27  PRO 27  27  27  PRO PRO B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  MET 31  31  31  MET MET B . n 
B 1 32  ASP 32  32  32  ASP ASP B . n 
B 1 33  GLN 33  33  33  GLN GLN B . n 
B 1 34  ALA 34  34  34  ALA ALA B . n 
B 1 35  PRO 35  35  35  PRO PRO B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  THR 38  38  38  THR THR B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  HIS 40  40  40  HIS HIS B . n 
B 1 41  PRO 41  41  41  PRO PRO B . n 
B 1 42  ARG 42  42  42  ARG ARG B . n 
B 1 43  ASN 43  43  43  ASN ASN B . n 
B 1 44  PRO 44  44  44  PRO PRO B . n 
B 1 45  ARG 45  45  45  ARG ARG B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  GLN 47  47  47  GLN GLN B . n 
B 1 48  ALA 48  48  48  ALA ALA B . n 
B 1 49  TRP 49  49  49  TRP TRP B . n 
B 1 50  GLN 50  50  50  GLN GLN B . n 
B 1 51  PHE 51  51  51  PHE PHE B . n 
B 1 52  GLN 52  52  52  GLN GLN B . n 
B 1 53  GLY 53  53  53  GLY GLY B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  VAL 55  55  55  VAL VAL B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  GLY 57  57  57  GLY GLY B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  GLY 60  60  60  GLY GLY B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  ASN 62  62  62  ASN ASN B . n 
B 1 63  ALA 63  63  63  ALA ALA B . n 
B 1 64  VAL 64  64  64  VAL VAL B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  SER 66  66  66  SER SER B . n 
B 1 67  TRP 67  67  67  TRP TRP B . n 
B 1 68  PRO 68  68  68  PRO PRO B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  HIS 70  70  70  HIS HIS B . n 
B 1 71  GLU 71  71  71  GLU GLU B . n 
B 1 72  TRP 72  72  72  TRP TRP B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  MET 74  74  74  MET MET B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  PRO 76  76  76  PRO PRO B . n 
B 1 77  THR 77  77  77  THR THR B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  TYR 79  79  79  TYR TYR B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  GLU 81  81  81  GLU GLU B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  ARG 83  83  83  ARG ARG B . n 
B 1 84  PRO 84  84  84  PRO PRO B . n 
B 1 85  ALA 85  85  85  ALA ALA B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  TYR 87  87  87  TYR TYR B . n 
B 1 88  ASP 88  88  88  ASP ASP B . n 
B 1 89  MET 89  89  89  MET MET B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  MET 91  91  91  MET MET B . n 
B 1 92  ARG 92  92  92  ARG ARG B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  ARG 94  94  94  ARG ARG B . n 
B 1 95  ASP 95  95  95  ASP ASP B . n 
B 1 96  MET 96  96  96  MET MET B . n 
B 1 97  ASP 97  97  97  ASP ASP B . n 
B 1 98  ALA 98  98  98  ALA ALA B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 THR 101 101 101 THR THR B . n 
B 1 102 LEU 102 102 102 LEU LEU B . n 
B 1 103 ALA 103 103 103 ALA ALA B . n 
B 1 104 ALA 104 104 104 ALA ALA B . n 
B 1 105 THR 105 105 105 THR THR B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 PHE 107 107 107 PHE PHE B . n 
B 1 108 ALA 108 108 108 ALA ALA B . n 
B 1 109 THR 109 109 109 THR THR B . n 
B 1 110 PHE 110 110 110 PHE PHE B . n 
B 1 111 PRO 111 111 111 PRO PRO B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 PHE 113 113 113 PHE PHE B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLY 115 115 115 GLY GLY B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 HIS 117 117 117 HIS HIS B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 ALA 119 119 119 ALA ALA B . n 
B 1 120 SER 120 120 120 SER SER B . n 
B 1 121 LEU 121 121 121 LEU LEU B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 ASP 123 123 123 ASP ASP B . n 
B 1 124 LYS 124 124 124 LYS LYS B . n 
B 1 125 LYS 125 125 125 LYS LYS B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 SER 127 127 127 SER SER B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 CYS 131 131 131 CYS CYS B . n 
B 1 132 ARG 132 132 132 ARG ARG B . n 
B 1 133 ALA 133 133 133 ALA ALA B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 ASN 135 135 135 ASN ASN B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 TRP 137 137 137 TRP TRP B . n 
B 1 138 VAL 138 138 138 VAL VAL B . n 
B 1 139 VAL 139 139 139 VAL VAL B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 GLU 141 141 141 GLU GLU B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 PRO 143 143 143 PRO PRO B . n 
B 1 144 ASP 144 144 144 ASP ASP B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 HIS 146 146 146 HIS HIS B . n 
B 1 147 PRO 147 147 147 PRO PRO B . n 
B 1 148 GLY 148 148 148 GLY GLY B . n 
B 1 149 ARG 149 149 149 ARG ARG B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 PRO 152 152 152 PRO PRO B . n 
B 1 153 ILE 153 153 153 ILE ILE B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 ILE 155 155 155 ILE ILE B . n 
B 1 156 ILE 156 156 156 ILE ILE B . n 
B 1 157 PRO 157 157 157 PRO PRO B . n 
B 1 158 PHE 158 158 158 PHE PHE B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 ASP 160 160 160 ASP ASP B . n 
B 1 161 ALA 161 161 161 ALA ALA B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 GLU 163 163 163 GLU GLU B . n 
B 1 164 SER 164 164 164 SER SER B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 ALA 166 166 166 ALA ALA B . n 
B 1 167 GLU 167 167 167 GLU GLU B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 HIS 169 169 169 HIS HIS B . n 
B 1 170 ARG 170 170 170 ARG ARG B . n 
B 1 171 ILE 171 171 171 ILE ILE B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 MET 174 174 174 MET MET B . n 
B 1 175 GLY 175 175 175 GLY GLY B . n 
B 1 176 CYS 176 176 176 CYS CYS B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 SER 178 178 178 SER SER B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 SER 180 180 180 SER SER B . n 
B 1 181 ILE 181 181 181 ILE ILE B . n 
B 1 182 PRO 182 182 182 PRO PRO B . n 
B 1 183 GLU 183 183 183 GLU GLU B . n 
B 1 184 THR 184 184 184 THR THR B . n 
B 1 185 PRO 185 185 185 PRO PRO B . n 
B 1 186 TYR 186 186 186 TYR TYR B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 VAL 188 188 188 VAL VAL B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 GLU 190 190 190 GLU GLU B . n 
B 1 191 GLY 191 191 191 GLY GLY B . n 
B 1 192 PHE 192 192 192 PHE PHE B . n 
B 1 193 PRO 193 193 193 PRO PRO B . n 
B 1 194 ASP 194 194 194 ASP ASP B . n 
B 1 195 PHE 195 195 195 PHE PHE B . n 
B 1 196 LYS 196 196 196 LYS LYS B . n 
B 1 197 SER 197 197 197 SER SER B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 TYR 199 199 199 TYR TYR B . n 
B 1 200 TRP 200 200 200 TRP TRP B . n 
B 1 201 ASP 201 201 201 ASP ASP B . n 
B 1 202 PRO 202 202 202 PRO PRO B . n 
B 1 203 ILE 203 203 203 ILE ILE B . n 
B 1 204 PHE 204 204 204 PHE PHE B . n 
B 1 205 LYS 205 205 205 LYS LYS B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 CYS 207 207 207 CYS CYS B . n 
B 1 208 VAL 208 208 208 VAL VAL B . n 
B 1 209 GLU 209 209 209 GLU GLU B . n 
B 1 210 HIS 210 210 210 HIS HIS B . n 
B 1 211 ASN 211 211 211 ASN ASN B . n 
B 1 212 ILE 212 212 212 ILE ILE B . n 
B 1 213 VAL 213 213 213 VAL VAL B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 SER 215 215 215 SER SER B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 HIS 217 217 217 HIS HIS B . n 
B 1 218 ILE 218 218 218 ILE ILE B . n 
B 1 219 GLY 219 219 219 GLY GLY B . n 
B 1 220 GLY 220 220 220 GLY GLY B . n 
B 1 221 GLY 221 221 221 GLY GLY B . n 
B 1 222 ILE 222 222 222 ILE ILE B . n 
B 1 223 ASN 223 223 223 ASN ASN B . n 
B 1 224 LEU 224 224 224 LEU LEU B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 LYS 226 226 226 LYS LYS B . n 
B 1 227 ARG 227 227 227 ARG ARG B . n 
B 1 228 PRO 228 228 228 PRO PRO B . n 
B 1 229 GLU 229 229 229 GLU GLU B . n 
B 1 230 GLY 230 230 230 GLY GLY B . n 
B 1 231 PHE 231 231 231 PHE PHE B . n 
B 1 232 ASP 232 232 232 ASP ASP B . n 
B 1 233 ILE 233 233 233 ILE ILE B . n 
B 1 234 ASP 234 234 234 ASP ASP B . n 
B 1 235 ASN 235 235 235 ASN ASN B . n 
B 1 236 MET 236 236 236 MET MET B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 MET 238 238 238 MET MET B . n 
B 1 239 LEU 239 239 239 LEU LEU B . n 
B 1 240 THR 240 240 240 THR THR B . n 
B 1 241 PRO 241 241 241 PRO PRO B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 ILE 243 243 243 ILE ILE B . n 
B 1 244 SER 244 244 244 SER SER B . n 
B 1 245 THR 245 245 245 THR THR B . n 
B 1 246 ILE 246 246 246 ILE ILE B . n 
B 1 247 ALA 247 247 247 ALA ALA B . n 
B 1 248 ALA 248 248 248 ALA ALA B . n 
B 1 249 THR 249 249 249 THR THR B . n 
B 1 250 ASP 250 250 250 ASP ASP B . n 
B 1 251 MET 251 251 251 MET MET B . n 
B 1 252 MET 252 252 252 MET MET B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 GLY 255 255 255 GLY GLY B . n 
B 1 256 ALA 256 256 256 ALA ALA B . n 
B 1 257 PHE 257 257 257 PHE PHE B . n 
B 1 258 LYS 258 258 258 LYS LYS B . n 
B 1 259 LYS 259 259 259 LYS LYS B . n 
B 1 260 PHE 260 260 260 PHE PHE B . n 
B 1 261 PRO 261 261 261 PRO PRO B . n 
B 1 262 ASP 262 262 262 ASP ASP B . n 
B 1 263 LEU 263 263 263 LEU LEU B . n 
B 1 264 LYS 264 264 264 LYS LYS B . n 
B 1 265 VAL 265 265 265 VAL VAL B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 MET 267 267 267 MET MET B . n 
B 1 268 SER 268 268 268 SER SER B . n 
B 1 269 GLU 269 269 269 GLU GLU B . n 
B 1 270 GLY 270 270 270 GLY GLY B . n 
B 1 271 GLY 271 271 271 GLY GLY B . n 
B 1 272 VAL 272 272 272 VAL VAL B . n 
B 1 273 GLY 273 273 273 GLY GLY B . n 
B 1 274 TRP 274 274 274 TRP TRP B . n 
B 1 275 VAL 275 275 275 VAL VAL B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 PRO 277 277 277 PRO PRO B . n 
B 1 278 TRP 278 278 278 TRP TRP B . n 
B 1 279 LEU 279 279 279 LEU LEU B . n 
B 1 280 ASP 280 280 280 ASP ASP B . n 
B 1 281 ARG 281 281 281 ARG ARG B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 ASP 283 283 283 ASP ASP B . n 
B 1 284 ARG 284 284 284 ARG ARG B . n 
B 1 285 HIS 285 285 285 HIS HIS B . n 
B 1 286 ILE 286 286 286 ILE ILE B . n 
B 1 287 VAL 287 287 287 VAL VAL B . n 
B 1 288 ASN 288 288 288 ASN ASN B . n 
B 1 289 GLN 289 289 289 GLN GLN B . n 
B 1 290 SER 290 290 290 SER SER B . n 
B 1 291 TRP 291 291 291 TRP TRP B . n 
B 1 292 THR 292 292 292 THR THR B . n 
B 1 293 GLY 293 293 293 GLY GLY B . n 
B 1 294 THR 294 294 294 THR THR B . n 
B 1 295 SER 295 295 295 SER SER B . n 
B 1 296 PHE 296 296 296 PHE PHE B . n 
B 1 297 LEU 297 297 297 LEU LEU B . n 
B 1 298 PRO 298 298 298 PRO PRO B . n 
B 1 299 LYS 299 299 299 LYS LYS B . n 
B 1 300 GLY 300 300 300 GLY GLY B . n 
B 1 301 MET 301 301 301 MET MET B . n 
B 1 302 THR 302 302 302 THR THR B . n 
B 1 303 PRO 303 303 303 PRO PRO B . n 
B 1 304 THR 304 304 304 THR THR B . n 
B 1 305 ASP 305 305 305 ASP ASP B . n 
B 1 306 VAL 306 306 306 VAL VAL B . n 
B 1 307 TRP 307 307 307 TRP TRP B . n 
B 1 308 ARG 308 308 308 ARG ARG B . n 
B 1 309 LYS 309 309 309 LYS LYS B . n 
B 1 310 ASN 310 310 310 ASN ASN B . n 
B 1 311 PHE 311 311 311 PHE PHE B . n 
B 1 312 LEU 312 312 312 LEU LEU B . n 
B 1 313 ALA 313 313 313 ALA ALA B . n 
B 1 314 CYS 314 314 314 CYS CYS B . n 
B 1 315 TYR 315 315 315 TYR TYR B . n 
B 1 316 ILE 316 316 316 ILE ILE B . n 
B 1 317 THR 317 317 317 THR THR B . n 
B 1 318 GLU 318 318 318 GLU GLU B . n 
B 1 319 PRO 319 319 319 PRO PRO B . n 
B 1 320 SER 320 320 320 SER SER B . n 
B 1 321 GLY 321 321 321 GLY GLY B . n 
B 1 322 LEU 322 322 322 LEU LEU B . n 
B 1 323 ASN 323 323 323 ASN ASN B . n 
B 1 324 ASN 324 324 324 ASN ASN B . n 
B 1 325 ARG 325 325 325 ARG ARG B . n 
B 1 326 HIS 326 326 326 HIS HIS B . n 
B 1 327 ARG 327 327 327 ARG ARG B . n 
B 1 328 LEU 328 328 328 LEU LEU B . n 
B 1 329 GLY 329 329 329 GLY GLY B . n 
B 1 330 VAL 330 330 330 VAL VAL B . n 
B 1 331 ASP 331 331 331 ASP ASP B . n 
B 1 332 THR 332 332 332 THR THR B . n 
B 1 333 ILE 333 333 333 ILE ILE B . n 
B 1 334 ALA 334 334 334 ALA ALA B . n 
B 1 335 TRP 335 335 335 TRP TRP B . n 
B 1 336 GLU 336 336 336 GLU GLU B . n 
B 1 337 CYS 337 337 337 CYS CYS B . n 
B 1 338 ASP 338 338 338 ASP ASP B . n 
B 1 339 TYR 339 339 339 TYR TYR B . n 
B 1 340 PRO 340 340 340 PRO PRO B . n 
B 1 341 HIS 341 341 341 HIS HIS B . n 
B 1 342 SER 342 342 342 SER SER B . n 
B 1 343 ASP 343 343 343 ASP ASP B . n 
B 1 344 SER 344 344 344 SER SER B . n 
B 1 345 THR 345 345 345 THR THR B . n 
B 1 346 TRP 346 346 346 TRP TRP B . n 
B 1 347 PRO 347 347 347 PRO PRO B . n 
B 1 348 ARG 348 348 348 ARG ARG B . n 
B 1 349 SER 349 349 349 SER SER B . n 
B 1 350 PRO 350 350 350 PRO PRO B . n 
B 1 351 GLU 351 351 351 GLU GLU B . n 
B 1 352 THR 352 352 352 THR THR B . n 
B 1 353 LEU 353 353 353 LEU LEU B . n 
B 1 354 LYS 354 354 354 LYS LYS B . n 
B 1 355 SER 355 355 355 SER SER B . n 
B 1 356 GLU 356 356 356 GLU GLU B . n 
B 1 357 LEU 357 357 357 LEU LEU B . n 
B 1 358 ASP 358 358 358 ASP ASP B . n 
B 1 359 ALA 359 359 359 ALA ALA B . n 
B 1 360 ALA 360 360 360 ALA ALA B . n 
B 1 361 ARG 361 361 361 ARG ARG B . n 
B 1 362 CYS 362 362 362 CYS CYS B . n 
B 1 363 THR 363 363 363 THR THR B . n 
B 1 364 ASP 364 364 364 ASP ASP B . n 
B 1 365 GLU 365 365 365 GLU GLU B . n 
B 1 366 GLU 366 366 366 GLU GLU B . n 
B 1 367 VAL 367 367 367 VAL VAL B . n 
B 1 368 ASP 368 368 368 ASP ASP B . n 
B 1 369 LYS 369 369 369 LYS LYS B . n 
B 1 370 ILE 370 370 370 ILE ILE B . n 
B 1 371 THR 371 371 371 THR THR B . n 
B 1 372 PHE 372 372 372 PHE PHE B . n 
B 1 373 ALA 373 373 373 ALA ALA B . n 
B 1 374 ASN 374 374 374 ASN ASN B . n 
B 1 375 ALA 375 375 375 ALA ALA B . n 
B 1 376 ALA 376 376 376 ALA ALA B . n 
B 1 377 LYS 377 377 377 LYS LYS B . n 
B 1 378 PHE 378 378 378 PHE PHE B . n 
B 1 379 PHE 379 379 379 PHE PHE B . n 
B 1 380 ASP 380 380 380 ASP ASP B . n 
B 1 381 TRP 381 381 381 TRP TRP B . n 
B 1 382 ASP 382 382 382 ASP ASP B . n 
B 1 383 PRO 383 383 383 PRO PRO B . n 
B 1 384 PHE 384 384 384 PHE PHE B . n 
B 1 385 GLU 385 385 385 GLU GLU B . n 
B 1 386 HIS 386 386 386 HIS HIS B . n 
B 1 387 ILE 387 387 387 ILE ILE B . n 
B 1 388 PRO 388 388 388 PRO PRO B . n 
B 1 389 ARG 389 389 389 ARG ARG B . n 
B 1 390 GLU 390 390 390 GLU GLU B . n 
B 1 391 GLU 391 391 391 GLU GLU B . n 
B 1 392 ALA 392 392 392 ALA ALA B . n 
B 1 393 THR 393 393 393 THR THR B . n 
B 1 394 VAL 394 394 394 VAL VAL B . n 
B 1 395 GLY 395 395 395 GLY GLY B . n 
B 1 396 ALA 396 396 396 ALA ALA B . n 
B 1 397 LEU 397 397 397 LEU LEU B . n 
B 1 398 ARG 398 398 398 ARG ARG B . n 
B 1 399 ALA 399 399 399 ALA ALA B . n 
B 1 400 ARG 400 400 400 ARG ARG B . n 
B 1 401 ALA 401 401 401 ALA ALA B . n 
B 1 402 THR 402 402 402 THR THR B . n 
B 1 403 ASP 403 403 403 ASP ASP B . n 
B 1 404 VAL 404 404 404 VAL VAL B . n 
B 1 405 ASP 405 405 405 ASP ASP B . n 
B 1 406 ILE 406 406 406 ILE ILE B . n 
B 1 407 SER 407 407 407 SER SER B . n 
B 1 408 GLU 408 408 408 GLU GLU B . n 
B 1 409 THR 409 409 409 THR THR B . n 
B 1 410 SER 410 410 410 SER SER B . n 
B 1 411 LYS 411 411 411 LYS LYS B . n 
B 1 412 GLU 412 412 412 GLU GLU B . n 
B 1 413 GLU 413 413 413 GLU GLU B . n 
B 1 414 TYR 414 414 414 TYR TYR B . n 
B 1 415 ARG 415 415 415 ARG ARG B . n 
B 1 416 ARG 416 416 416 ARG ARG B . n 
B 1 417 ARG 417 417 417 ARG ARG B . n 
B 1 418 TYR 418 418 418 TYR TYR B . n 
B 1 419 GLU 419 419 419 GLU GLU B . n 
B 1 420 LEU 420 420 420 LEU LEU B . n 
B 1 421 THR 421 421 421 THR THR B . n 
B 1 422 HIS 422 422 422 HIS HIS B . n 
B 1 423 SER 423 423 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        MN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   MN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 GOL 1   501 501 GOL GOL A . 
D 2 GOL 1   502 601 GOL GOL A . 
E 2 GOL 1   503 701 GOL GOL A . 
F 3 MN  1   504 1   MN  MN  A . 
G 3 MN  1   505 2   MN  MN  A . 
H 4 MG  1   506 1   MG  MG  A . 
I 2 GOL 1   501 501 GOL GOL B . 
J 2 GOL 1   502 601 GOL GOL B . 
K 2 GOL 1   503 701 GOL GOL B . 
L 2 GOL 1   504 801 GOL GOL B . 
M 3 MN  1   505 3   MN  MN  B . 
N 3 MN  1   506 4   MN  MN  B . 
O 5 HOH 1   601 111 HOH HOH A . 
O 5 HOH 2   602 240 HOH HOH A . 
O 5 HOH 3   603 307 HOH HOH A . 
O 5 HOH 4   604 531 HOH HOH A . 
O 5 HOH 5   605 721 HOH HOH A . 
O 5 HOH 6   606 290 HOH HOH A . 
O 5 HOH 7   607 672 HOH HOH A . 
O 5 HOH 8   608 645 HOH HOH A . 
O 5 HOH 9   609 563 HOH HOH A . 
O 5 HOH 10  610 578 HOH HOH A . 
O 5 HOH 11  611 337 HOH HOH A . 
O 5 HOH 12  612 259 HOH HOH A . 
O 5 HOH 13  613 188 HOH HOH A . 
O 5 HOH 14  614 255 HOH HOH A . 
O 5 HOH 15  615 662 HOH HOH A . 
O 5 HOH 16  616 155 HOH HOH A . 
O 5 HOH 17  617 711 HOH HOH A . 
O 5 HOH 18  618 368 HOH HOH A . 
O 5 HOH 19  619 69  HOH HOH A . 
O 5 HOH 20  620 480 HOH HOH A . 
O 5 HOH 21  621 164 HOH HOH A . 
O 5 HOH 22  622 553 HOH HOH A . 
O 5 HOH 23  623 316 HOH HOH A . 
O 5 HOH 24  624 35  HOH HOH A . 
O 5 HOH 25  625 96  HOH HOH A . 
O 5 HOH 26  626 61  HOH HOH A . 
O 5 HOH 27  627 315 HOH HOH A . 
O 5 HOH 28  628 738 HOH HOH A . 
O 5 HOH 29  629 567 HOH HOH A . 
O 5 HOH 30  630 293 HOH HOH A . 
O 5 HOH 31  631 463 HOH HOH A . 
O 5 HOH 32  632 265 HOH HOH A . 
O 5 HOH 33  633 572 HOH HOH A . 
O 5 HOH 34  634 455 HOH HOH A . 
O 5 HOH 35  635 405 HOH HOH A . 
O 5 HOH 36  636 125 HOH HOH A . 
O 5 HOH 37  637 277 HOH HOH A . 
O 5 HOH 38  638 541 HOH HOH A . 
O 5 HOH 39  639 39  HOH HOH A . 
O 5 HOH 40  640 195 HOH HOH A . 
O 5 HOH 41  641 36  HOH HOH A . 
O 5 HOH 42  642 488 HOH HOH A . 
O 5 HOH 43  643 167 HOH HOH A . 
O 5 HOH 44  644 248 HOH HOH A . 
O 5 HOH 45  645 543 HOH HOH A . 
O 5 HOH 46  646 626 HOH HOH A . 
O 5 HOH 47  647 724 HOH HOH A . 
O 5 HOH 48  648 584 HOH HOH A . 
O 5 HOH 49  649 482 HOH HOH A . 
O 5 HOH 50  650 45  HOH HOH A . 
O 5 HOH 51  651 33  HOH HOH A . 
O 5 HOH 52  652 5   HOH HOH A . 
O 5 HOH 53  653 154 HOH HOH A . 
O 5 HOH 54  654 514 HOH HOH A . 
O 5 HOH 55  655 629 HOH HOH A . 
O 5 HOH 56  656 285 HOH HOH A . 
O 5 HOH 57  657 51  HOH HOH A . 
O 5 HOH 58  658 81  HOH HOH A . 
O 5 HOH 59  659 175 HOH HOH A . 
O 5 HOH 60  660 702 HOH HOH A . 
O 5 HOH 61  661 3   HOH HOH A . 
O 5 HOH 62  662 451 HOH HOH A . 
O 5 HOH 63  663 728 HOH HOH A . 
O 5 HOH 64  664 596 HOH HOH A . 
O 5 HOH 65  665 677 HOH HOH A . 
O 5 HOH 66  666 65  HOH HOH A . 
O 5 HOH 67  667 493 HOH HOH A . 
O 5 HOH 68  668 32  HOH HOH A . 
O 5 HOH 69  669 376 HOH HOH A . 
O 5 HOH 70  670 495 HOH HOH A . 
O 5 HOH 71  671 306 HOH HOH A . 
O 5 HOH 72  672 740 HOH HOH A . 
O 5 HOH 73  673 76  HOH HOH A . 
O 5 HOH 74  674 63  HOH HOH A . 
O 5 HOH 75  675 117 HOH HOH A . 
O 5 HOH 76  676 529 HOH HOH A . 
O 5 HOH 77  677 519 HOH HOH A . 
O 5 HOH 78  678 330 HOH HOH A . 
O 5 HOH 79  679 234 HOH HOH A . 
O 5 HOH 80  680 91  HOH HOH A . 
O 5 HOH 81  681 718 HOH HOH A . 
O 5 HOH 82  682 449 HOH HOH A . 
O 5 HOH 83  683 396 HOH HOH A . 
O 5 HOH 84  684 170 HOH HOH A . 
O 5 HOH 85  685 435 HOH HOH A . 
O 5 HOH 86  686 682 HOH HOH A . 
O 5 HOH 87  687 9   HOH HOH A . 
O 5 HOH 88  688 30  HOH HOH A . 
O 5 HOH 89  689 229 HOH HOH A . 
O 5 HOH 90  690 510 HOH HOH A . 
O 5 HOH 91  691 216 HOH HOH A . 
O 5 HOH 92  692 64  HOH HOH A . 
O 5 HOH 93  693 74  HOH HOH A . 
O 5 HOH 94  694 92  HOH HOH A . 
O 5 HOH 95  695 185 HOH HOH A . 
O 5 HOH 96  696 492 HOH HOH A . 
O 5 HOH 97  697 38  HOH HOH A . 
O 5 HOH 98  698 542 HOH HOH A . 
O 5 HOH 99  699 708 HOH HOH A . 
O 5 HOH 100 700 190 HOH HOH A . 
O 5 HOH 101 701 245 HOH HOH A . 
O 5 HOH 102 702 8   HOH HOH A . 
O 5 HOH 103 703 28  HOH HOH A . 
O 5 HOH 104 704 17  HOH HOH A . 
O 5 HOH 105 705 57  HOH HOH A . 
O 5 HOH 106 706 357 HOH HOH A . 
O 5 HOH 107 707 540 HOH HOH A . 
O 5 HOH 108 708 109 HOH HOH A . 
O 5 HOH 109 709 311 HOH HOH A . 
O 5 HOH 110 710 603 HOH HOH A . 
O 5 HOH 111 711 304 HOH HOH A . 
O 5 HOH 112 712 160 HOH HOH A . 
O 5 HOH 113 713 581 HOH HOH A . 
O 5 HOH 114 714 312 HOH HOH A . 
O 5 HOH 115 715 118 HOH HOH A . 
O 5 HOH 116 716 484 HOH HOH A . 
O 5 HOH 117 717 236 HOH HOH A . 
O 5 HOH 118 718 619 HOH HOH A . 
O 5 HOH 119 719 131 HOH HOH A . 
O 5 HOH 120 720 338 HOH HOH A . 
O 5 HOH 121 721 378 HOH HOH A . 
O 5 HOH 122 722 215 HOH HOH A . 
O 5 HOH 123 723 40  HOH HOH A . 
O 5 HOH 124 724 295 HOH HOH A . 
O 5 HOH 125 725 26  HOH HOH A . 
O 5 HOH 126 726 399 HOH HOH A . 
O 5 HOH 127 727 199 HOH HOH A . 
O 5 HOH 128 728 129 HOH HOH A . 
O 5 HOH 129 729 10  HOH HOH A . 
O 5 HOH 130 730 634 HOH HOH A . 
O 5 HOH 131 731 127 HOH HOH A . 
O 5 HOH 132 732 183 HOH HOH A . 
O 5 HOH 133 733 317 HOH HOH A . 
O 5 HOH 134 734 29  HOH HOH A . 
O 5 HOH 135 735 143 HOH HOH A . 
O 5 HOH 136 736 27  HOH HOH A . 
O 5 HOH 137 737 13  HOH HOH A . 
O 5 HOH 138 738 354 HOH HOH A . 
O 5 HOH 139 739 128 HOH HOH A . 
O 5 HOH 140 740 153 HOH HOH A . 
O 5 HOH 141 741 72  HOH HOH A . 
O 5 HOH 142 742 108 HOH HOH A . 
O 5 HOH 143 743 747 HOH HOH A . 
O 5 HOH 144 744 384 HOH HOH A . 
O 5 HOH 145 745 331 HOH HOH A . 
O 5 HOH 146 746 318 HOH HOH A . 
O 5 HOH 147 747 189 HOH HOH A . 
O 5 HOH 148 748 502 HOH HOH A . 
O 5 HOH 149 749 83  HOH HOH A . 
O 5 HOH 150 750 597 HOH HOH A . 
O 5 HOH 151 751 275 HOH HOH A . 
O 5 HOH 152 752 630 HOH HOH A . 
O 5 HOH 153 753 324 HOH HOH A . 
O 5 HOH 154 754 20  HOH HOH A . 
O 5 HOH 155 755 505 HOH HOH A . 
O 5 HOH 156 756 15  HOH HOH A . 
O 5 HOH 157 757 323 HOH HOH A . 
O 5 HOH 158 758 232 HOH HOH A . 
O 5 HOH 159 759 571 HOH HOH A . 
O 5 HOH 160 760 98  HOH HOH A . 
O 5 HOH 161 761 58  HOH HOH A . 
O 5 HOH 162 762 135 HOH HOH A . 
O 5 HOH 163 763 272 HOH HOH A . 
O 5 HOH 164 764 341 HOH HOH A . 
O 5 HOH 165 765 270 HOH HOH A . 
O 5 HOH 166 766 70  HOH HOH A . 
O 5 HOH 167 767 71  HOH HOH A . 
O 5 HOH 168 768 256 HOH HOH A . 
O 5 HOH 169 769 209 HOH HOH A . 
O 5 HOH 170 770 518 HOH HOH A . 
O 5 HOH 171 771 287 HOH HOH A . 
O 5 HOH 172 772 445 HOH HOH A . 
O 5 HOH 173 773 421 HOH HOH A . 
O 5 HOH 174 774 145 HOH HOH A . 
O 5 HOH 175 775 346 HOH HOH A . 
O 5 HOH 176 776 565 HOH HOH A . 
O 5 HOH 177 777 386 HOH HOH A . 
O 5 HOH 178 778 586 HOH HOH A . 
O 5 HOH 179 779 48  HOH HOH A . 
O 5 HOH 180 780 414 HOH HOH A . 
O 5 HOH 181 781 345 HOH HOH A . 
O 5 HOH 182 782 280 HOH HOH A . 
O 5 HOH 183 783 666 HOH HOH A . 
O 5 HOH 184 784 152 HOH HOH A . 
O 5 HOH 185 785 191 HOH HOH A . 
O 5 HOH 186 786 94  HOH HOH A . 
O 5 HOH 187 787 130 HOH HOH A . 
O 5 HOH 188 788 163 HOH HOH A . 
O 5 HOH 189 789 22  HOH HOH A . 
O 5 HOH 190 790 683 HOH HOH A . 
O 5 HOH 191 791 314 HOH HOH A . 
O 5 HOH 192 792 333 HOH HOH A . 
O 5 HOH 193 793 547 HOH HOH A . 
O 5 HOH 194 794 340 HOH HOH A . 
O 5 HOH 195 795 120 HOH HOH A . 
O 5 HOH 196 796 207 HOH HOH A . 
O 5 HOH 197 797 269 HOH HOH A . 
O 5 HOH 198 798 732 HOH HOH A . 
O 5 HOH 199 799 268 HOH HOH A . 
O 5 HOH 200 800 192 HOH HOH A . 
O 5 HOH 201 801 112 HOH HOH A . 
O 5 HOH 202 802 237 HOH HOH A . 
O 5 HOH 203 803 494 HOH HOH A . 
O 5 HOH 204 804 655 HOH HOH A . 
O 5 HOH 205 805 60  HOH HOH A . 
O 5 HOH 206 806 55  HOH HOH A . 
O 5 HOH 207 807 266 HOH HOH A . 
O 5 HOH 208 808 424 HOH HOH A . 
O 5 HOH 209 809 102 HOH HOH A . 
O 5 HOH 210 810 116 HOH HOH A . 
O 5 HOH 211 811 95  HOH HOH A . 
O 5 HOH 212 812 474 HOH HOH A . 
O 5 HOH 213 813 674 HOH HOH A . 
O 5 HOH 214 814 365 HOH HOH A . 
O 5 HOH 215 815 707 HOH HOH A . 
O 5 HOH 216 816 703 HOH HOH A . 
O 5 HOH 217 817 198 HOH HOH A . 
O 5 HOH 218 818 566 HOH HOH A . 
O 5 HOH 219 819 441 HOH HOH A . 
O 5 HOH 220 820 222 HOH HOH A . 
O 5 HOH 221 821 639 HOH HOH A . 
O 5 HOH 222 822 606 HOH HOH A . 
O 5 HOH 223 823 329 HOH HOH A . 
O 5 HOH 224 824 144 HOH HOH A . 
O 5 HOH 225 825 211 HOH HOH A . 
O 5 HOH 226 826 168 HOH HOH A . 
O 5 HOH 227 827 521 HOH HOH A . 
O 5 HOH 228 828 568 HOH HOH A . 
O 5 HOH 229 829 193 HOH HOH A . 
O 5 HOH 230 830 618 HOH HOH A . 
O 5 HOH 231 831 106 HOH HOH A . 
O 5 HOH 232 832 464 HOH HOH A . 
O 5 HOH 233 833 476 HOH HOH A . 
O 5 HOH 234 834 278 HOH HOH A . 
O 5 HOH 235 835 375 HOH HOH A . 
O 5 HOH 236 836 748 HOH HOH A . 
O 5 HOH 237 837 486 HOH HOH A . 
O 5 HOH 238 838 358 HOH HOH A . 
O 5 HOH 239 839 339 HOH HOH A . 
O 5 HOH 240 840 681 HOH HOH A . 
O 5 HOH 241 841 446 HOH HOH A . 
O 5 HOH 242 842 101 HOH HOH A . 
O 5 HOH 243 843 113 HOH HOH A . 
O 5 HOH 244 844 308 HOH HOH A . 
O 5 HOH 245 845 44  HOH HOH A . 
O 5 HOH 246 846 739 HOH HOH A . 
O 5 HOH 247 847 700 HOH HOH A . 
O 5 HOH 248 848 712 HOH HOH A . 
O 5 HOH 249 849 746 HOH HOH A . 
O 5 HOH 250 850 263 HOH HOH A . 
O 5 HOH 251 851 458 HOH HOH A . 
O 5 HOH 252 852 233 HOH HOH A . 
O 5 HOH 253 853 244 HOH HOH A . 
O 5 HOH 254 854 251 HOH HOH A . 
O 5 HOH 255 855 620 HOH HOH A . 
O 5 HOH 256 856 370 HOH HOH A . 
O 5 HOH 257 857 274 HOH HOH A . 
O 5 HOH 258 858 214 HOH HOH A . 
O 5 HOH 259 859 75  HOH HOH A . 
O 5 HOH 260 860 736 HOH HOH A . 
O 5 HOH 261 861 549 HOH HOH A . 
O 5 HOH 262 862 676 HOH HOH A . 
O 5 HOH 263 863 632 HOH HOH A . 
O 5 HOH 264 864 78  HOH HOH A . 
O 5 HOH 265 865 516 HOH HOH A . 
O 5 HOH 266 866 21  HOH HOH A . 
O 5 HOH 267 867 453 HOH HOH A . 
O 5 HOH 268 868 258 HOH HOH A . 
O 5 HOH 269 869 142 HOH HOH A . 
O 5 HOH 270 870 460 HOH HOH A . 
O 5 HOH 271 871 607 HOH HOH A . 
O 5 HOH 272 872 546 HOH HOH A . 
O 5 HOH 273 873 264 HOH HOH A . 
O 5 HOH 274 874 554 HOH HOH A . 
O 5 HOH 275 875 1   HOH HOH A . 
O 5 HOH 276 876 37  HOH HOH A . 
O 5 HOH 277 877 717 HOH HOH A . 
O 5 HOH 278 878 201 HOH HOH A . 
O 5 HOH 279 879 686 HOH HOH A . 
O 5 HOH 280 880 54  HOH HOH A . 
O 5 HOH 281 881 575 HOH HOH A . 
O 5 HOH 282 882 709 HOH HOH A . 
O 5 HOH 283 883 751 HOH HOH A . 
O 5 HOH 284 884 616 HOH HOH A . 
O 5 HOH 285 885 477 HOH HOH A . 
O 5 HOH 286 886 507 HOH HOH A . 
O 5 HOH 287 887 722 HOH HOH A . 
O 5 HOH 288 888 397 HOH HOH A . 
O 5 HOH 289 889 741 HOH HOH A . 
O 5 HOH 290 890 461 HOH HOH A . 
O 5 HOH 291 891 119 HOH HOH A . 
O 5 HOH 292 892 640 HOH HOH A . 
O 5 HOH 293 893 585 HOH HOH A . 
O 5 HOH 294 894 400 HOH HOH A . 
O 5 HOH 295 895 472 HOH HOH A . 
O 5 HOH 296 896 663 HOH HOH A . 
O 5 HOH 297 897 642 HOH HOH A . 
O 5 HOH 298 898 637 HOH HOH A . 
O 5 HOH 299 899 93  HOH HOH A . 
O 5 HOH 300 900 627 HOH HOH A . 
O 5 HOH 301 901 447 HOH HOH A . 
O 5 HOH 302 902 730 HOH HOH A . 
O 5 HOH 303 903 587 HOH HOH A . 
O 5 HOH 304 904 527 HOH HOH A . 
O 5 HOH 305 905 165 HOH HOH A . 
O 5 HOH 306 906 693 HOH HOH A . 
O 5 HOH 307 907 530 HOH HOH A . 
O 5 HOH 308 908 633 HOH HOH A . 
O 5 HOH 309 909 212 HOH HOH A . 
O 5 HOH 310 910 735 HOH HOH A . 
O 5 HOH 311 911 731 HOH HOH A . 
O 5 HOH 312 912 752 HOH HOH A . 
O 5 HOH 313 913 532 HOH HOH A . 
O 5 HOH 314 914 689 HOH HOH A . 
O 5 HOH 315 915 496 HOH HOH A . 
O 5 HOH 316 916 197 HOH HOH A . 
O 5 HOH 317 917 348 HOH HOH A . 
O 5 HOH 318 918 583 HOH HOH A . 
O 5 HOH 319 919 658 HOH HOH A . 
O 5 HOH 320 920 394 HOH HOH A . 
O 5 HOH 321 921 322 HOH HOH A . 
O 5 HOH 322 922 454 HOH HOH A . 
O 5 HOH 323 923 564 HOH HOH A . 
O 5 HOH 324 924 186 HOH HOH A . 
O 5 HOH 325 925 727 HOH HOH A . 
O 5 HOH 326 926 282 HOH HOH A . 
O 5 HOH 327 927 220 HOH HOH A . 
O 5 HOH 328 928 428 HOH HOH A . 
O 5 HOH 329 929 379 HOH HOH A . 
O 5 HOH 330 930 497 HOH HOH A . 
O 5 HOH 331 931 576 HOH HOH A . 
O 5 HOH 332 932 224 HOH HOH A . 
O 5 HOH 333 933 595 HOH HOH A . 
O 5 HOH 334 934 178 HOH HOH A . 
O 5 HOH 335 935 298 HOH HOH A . 
O 5 HOH 336 936 374 HOH HOH A . 
O 5 HOH 337 937 670 HOH HOH A . 
O 5 HOH 338 938 688 HOH HOH A . 
O 5 HOH 339 939 470 HOH HOH A . 
O 5 HOH 340 940 180 HOH HOH A . 
O 5 HOH 341 941 602 HOH HOH A . 
O 5 HOH 342 942 88  HOH HOH A . 
O 5 HOH 343 943 664 HOH HOH A . 
O 5 HOH 344 944 512 HOH HOH A . 
O 5 HOH 345 945 427 HOH HOH A . 
O 5 HOH 346 946 669 HOH HOH A . 
O 5 HOH 347 947 242 HOH HOH A . 
O 5 HOH 348 948 660 HOH HOH A . 
O 5 HOH 349 949 622 HOH HOH A . 
O 5 HOH 350 950 574 HOH HOH A . 
O 5 HOH 351 951 643 HOH HOH A . 
O 5 HOH 352 952 635 HOH HOH A . 
O 5 HOH 353 953 590 HOH HOH A . 
P 5 HOH 1   601 398 HOH HOH B . 
P 5 HOH 2   602 401 HOH HOH B . 
P 5 HOH 3   603 260 HOH HOH B . 
P 5 HOH 4   604 638 HOH HOH B . 
P 5 HOH 5   605 351 HOH HOH B . 
P 5 HOH 6   606 647 HOH HOH B . 
P 5 HOH 7   607 16  HOH HOH B . 
P 5 HOH 8   608 503 HOH HOH B . 
P 5 HOH 9   609 509 HOH HOH B . 
P 5 HOH 10  610 286 HOH HOH B . 
P 5 HOH 11  611 226 HOH HOH B . 
P 5 HOH 12  612 522 HOH HOH B . 
P 5 HOH 13  613 412 HOH HOH B . 
P 5 HOH 14  614 473 HOH HOH B . 
P 5 HOH 15  615 444 HOH HOH B . 
P 5 HOH 16  616 284 HOH HOH B . 
P 5 HOH 17  617 336 HOH HOH B . 
P 5 HOH 18  618 361 HOH HOH B . 
P 5 HOH 19  619 710 HOH HOH B . 
P 5 HOH 20  620 321 HOH HOH B . 
P 5 HOH 21  621 469 HOH HOH B . 
P 5 HOH 22  622 56  HOH HOH B . 
P 5 HOH 23  623 344 HOH HOH B . 
P 5 HOH 24  624 406 HOH HOH B . 
P 5 HOH 25  625 369 HOH HOH B . 
P 5 HOH 26  626 515 HOH HOH B . 
P 5 HOH 27  627 442 HOH HOH B . 
P 5 HOH 28  628 525 HOH HOH B . 
P 5 HOH 29  629 162 HOH HOH B . 
P 5 HOH 30  630 276 HOH HOH B . 
P 5 HOH 31  631 558 HOH HOH B . 
P 5 HOH 32  632 483 HOH HOH B . 
P 5 HOH 33  633 246 HOH HOH B . 
P 5 HOH 34  634 77  HOH HOH B . 
P 5 HOH 35  635 557 HOH HOH B . 
P 5 HOH 36  636 723 HOH HOH B . 
P 5 HOH 37  637 140 HOH HOH B . 
P 5 HOH 38  638 391 HOH HOH B . 
P 5 HOH 39  639 325 HOH HOH B . 
P 5 HOH 40  640 103 HOH HOH B . 
P 5 HOH 41  641 158 HOH HOH B . 
P 5 HOH 42  642 714 HOH HOH B . 
P 5 HOH 43  643 279 HOH HOH B . 
P 5 HOH 44  644 217 HOH HOH B . 
P 5 HOH 45  645 80  HOH HOH B . 
P 5 HOH 46  646 500 HOH HOH B . 
P 5 HOH 47  647 273 HOH HOH B . 
P 5 HOH 48  648 411 HOH HOH B . 
P 5 HOH 49  649 173 HOH HOH B . 
P 5 HOH 50  650 114 HOH HOH B . 
P 5 HOH 51  651 631 HOH HOH B . 
P 5 HOH 52  652 433 HOH HOH B . 
P 5 HOH 53  653 404 HOH HOH B . 
P 5 HOH 54  654 419 HOH HOH B . 
P 5 HOH 55  655 319 HOH HOH B . 
P 5 HOH 56  656 169 HOH HOH B . 
P 5 HOH 57  657 97  HOH HOH B . 
P 5 HOH 58  658 2   HOH HOH B . 
P 5 HOH 59  659 671 HOH HOH B . 
P 5 HOH 60  660 147 HOH HOH B . 
P 5 HOH 61  661 90  HOH HOH B . 
P 5 HOH 62  662 600 HOH HOH B . 
P 5 HOH 63  663 41  HOH HOH B . 
P 5 HOH 64  664 139 HOH HOH B . 
P 5 HOH 65  665 385 HOH HOH B . 
P 5 HOH 66  666 59  HOH HOH B . 
P 5 HOH 67  667 713 HOH HOH B . 
P 5 HOH 68  668 389 HOH HOH B . 
P 5 HOH 69  669 720 HOH HOH B . 
P 5 HOH 70  670 204 HOH HOH B . 
P 5 HOH 71  671 85  HOH HOH B . 
P 5 HOH 72  672 745 HOH HOH B . 
P 5 HOH 73  673 67  HOH HOH B . 
P 5 HOH 74  674 601 HOH HOH B . 
P 5 HOH 75  675 675 HOH HOH B . 
P 5 HOH 76  676 187 HOH HOH B . 
P 5 HOH 77  677 34  HOH HOH B . 
P 5 HOH 78  678 4   HOH HOH B . 
P 5 HOH 79  679 303 HOH HOH B . 
P 5 HOH 80  680 172 HOH HOH B . 
P 5 HOH 81  681 49  HOH HOH B . 
P 5 HOH 82  682 181 HOH HOH B . 
P 5 HOH 83  683 19  HOH HOH B . 
P 5 HOH 84  684 150 HOH HOH B . 
P 5 HOH 85  685 110 HOH HOH B . 
P 5 HOH 86  686 221 HOH HOH B . 
P 5 HOH 87  687 73  HOH HOH B . 
P 5 HOH 88  688 137 HOH HOH B . 
P 5 HOH 89  689 11  HOH HOH B . 
P 5 HOH 90  690 694 HOH HOH B . 
P 5 HOH 91  691 194 HOH HOH B . 
P 5 HOH 92  692 138 HOH HOH B . 
P 5 HOH 93  693 47  HOH HOH B . 
P 5 HOH 94  694 134 HOH HOH B . 
P 5 HOH 95  695 23  HOH HOH B . 
P 5 HOH 96  696 50  HOH HOH B . 
P 5 HOH 97  697 343 HOH HOH B . 
P 5 HOH 98  698 206 HOH HOH B . 
P 5 HOH 99  699 288 HOH HOH B . 
P 5 HOH 100 700 360 HOH HOH B . 
P 5 HOH 101 701 213 HOH HOH B . 
P 5 HOH 102 702 43  HOH HOH B . 
P 5 HOH 103 703 79  HOH HOH B . 
P 5 HOH 104 704 388 HOH HOH B . 
P 5 HOH 105 705 133 HOH HOH B . 
P 5 HOH 106 706 426 HOH HOH B . 
P 5 HOH 107 707 679 HOH HOH B . 
P 5 HOH 108 708 459 HOH HOH B . 
P 5 HOH 109 709 744 HOH HOH B . 
P 5 HOH 110 710 24  HOH HOH B . 
P 5 HOH 111 711 200 HOH HOH B . 
P 5 HOH 112 712 431 HOH HOH B . 
P 5 HOH 113 713 146 HOH HOH B . 
P 5 HOH 114 714 18  HOH HOH B . 
P 5 HOH 115 715 506 HOH HOH B . 
P 5 HOH 116 716 310 HOH HOH B . 
P 5 HOH 117 717 410 HOH HOH B . 
P 5 HOH 118 718 651 HOH HOH B . 
P 5 HOH 119 719 46  HOH HOH B . 
P 5 HOH 120 720 678 HOH HOH B . 
P 5 HOH 121 721 42  HOH HOH B . 
P 5 HOH 122 722 136 HOH HOH B . 
P 5 HOH 123 723 166 HOH HOH B . 
P 5 HOH 124 724 381 HOH HOH B . 
P 5 HOH 125 725 561 HOH HOH B . 
P 5 HOH 126 726 352 HOH HOH B . 
P 5 HOH 127 727 218 HOH HOH B . 
P 5 HOH 128 728 89  HOH HOH B . 
P 5 HOH 129 729 141 HOH HOH B . 
P 5 HOH 130 730 243 HOH HOH B . 
P 5 HOH 131 731 104 HOH HOH B . 
P 5 HOH 132 732 342 HOH HOH B . 
P 5 HOH 133 733 475 HOH HOH B . 
P 5 HOH 134 734 52  HOH HOH B . 
P 5 HOH 135 735 624 HOH HOH B . 
P 5 HOH 136 736 395 HOH HOH B . 
P 5 HOH 137 737 62  HOH HOH B . 
P 5 HOH 138 738 149 HOH HOH B . 
P 5 HOH 139 739 437 HOH HOH B . 
P 5 HOH 140 740 196 HOH HOH B . 
P 5 HOH 141 741 353 HOH HOH B . 
P 5 HOH 142 742 66  HOH HOH B . 
P 5 HOH 143 743 299 HOH HOH B . 
P 5 HOH 144 744 99  HOH HOH B . 
P 5 HOH 145 745 349 HOH HOH B . 
P 5 HOH 146 746 499 HOH HOH B . 
P 5 HOH 147 747 466 HOH HOH B . 
P 5 HOH 148 748 219 HOH HOH B . 
P 5 HOH 149 749 598 HOH HOH B . 
P 5 HOH 150 750 599 HOH HOH B . 
P 5 HOH 151 751 545 HOH HOH B . 
P 5 HOH 152 752 617 HOH HOH B . 
P 5 HOH 153 753 604 HOH HOH B . 
P 5 HOH 154 754 725 HOH HOH B . 
P 5 HOH 155 755 82  HOH HOH B . 
P 5 HOH 156 756 661 HOH HOH B . 
P 5 HOH 157 757 733 HOH HOH B . 
P 5 HOH 158 758 223 HOH HOH B . 
P 5 HOH 159 759 247 HOH HOH B . 
P 5 HOH 160 760 122 HOH HOH B . 
P 5 HOH 161 761 179 HOH HOH B . 
P 5 HOH 162 762 301 HOH HOH B . 
P 5 HOH 163 763 613 HOH HOH B . 
P 5 HOH 164 764 241 HOH HOH B . 
P 5 HOH 165 765 230 HOH HOH B . 
P 5 HOH 166 766 7   HOH HOH B . 
P 5 HOH 167 767 253 HOH HOH B . 
P 5 HOH 168 768 716 HOH HOH B . 
P 5 HOH 169 769 228 HOH HOH B . 
P 5 HOH 170 770 105 HOH HOH B . 
P 5 HOH 171 771 296 HOH HOH B . 
P 5 HOH 172 772 291 HOH HOH B . 
P 5 HOH 173 773 591 HOH HOH B . 
P 5 HOH 174 774 417 HOH HOH B . 
P 5 HOH 175 775 313 HOH HOH B . 
P 5 HOH 176 776 366 HOH HOH B . 
P 5 HOH 177 777 347 HOH HOH B . 
P 5 HOH 178 778 292 HOH HOH B . 
P 5 HOH 179 779 159 HOH HOH B . 
P 5 HOH 180 780 697 HOH HOH B . 
P 5 HOH 181 781 551 HOH HOH B . 
P 5 HOH 182 782 203 HOH HOH B . 
P 5 HOH 183 783 177 HOH HOH B . 
P 5 HOH 184 784 614 HOH HOH B . 
P 5 HOH 185 785 416 HOH HOH B . 
P 5 HOH 186 786 729 HOH HOH B . 
P 5 HOH 187 787 538 HOH HOH B . 
P 5 HOH 188 788 420 HOH HOH B . 
P 5 HOH 189 789 467 HOH HOH B . 
P 5 HOH 190 790 281 HOH HOH B . 
P 5 HOH 191 791 208 HOH HOH B . 
P 5 HOH 192 792 68  HOH HOH B . 
P 5 HOH 193 793 726 HOH HOH B . 
P 5 HOH 194 794 485 HOH HOH B . 
P 5 HOH 195 795 84  HOH HOH B . 
P 5 HOH 196 796 699 HOH HOH B . 
P 5 HOH 197 797 271 HOH HOH B . 
P 5 HOH 198 798 14  HOH HOH B . 
P 5 HOH 199 799 86  HOH HOH B . 
P 5 HOH 200 800 648 HOH HOH B . 
P 5 HOH 201 801 151 HOH HOH B . 
P 5 HOH 202 802 267 HOH HOH B . 
P 5 HOH 203 803 580 HOH HOH B . 
P 5 HOH 204 804 12  HOH HOH B . 
P 5 HOH 205 805 87  HOH HOH B . 
P 5 HOH 206 806 326 HOH HOH B . 
P 5 HOH 207 807 332 HOH HOH B . 
P 5 HOH 208 808 582 HOH HOH B . 
P 5 HOH 209 809 297 HOH HOH B . 
P 5 HOH 210 810 225 HOH HOH B . 
P 5 HOH 211 811 625 HOH HOH B . 
P 5 HOH 212 812 25  HOH HOH B . 
P 5 HOH 213 813 161 HOH HOH B . 
P 5 HOH 214 814 367 HOH HOH B . 
P 5 HOH 215 815 556 HOH HOH B . 
P 5 HOH 216 816 300 HOH HOH B . 
P 5 HOH 217 817 593 HOH HOH B . 
P 5 HOH 218 818 719 HOH HOH B . 
P 5 HOH 219 819 148 HOH HOH B . 
P 5 HOH 220 820 254 HOH HOH B . 
P 5 HOH 221 821 320 HOH HOH B . 
P 5 HOH 222 822 690 HOH HOH B . 
P 5 HOH 223 823 654 HOH HOH B . 
P 5 HOH 224 824 132 HOH HOH B . 
P 5 HOH 225 825 479 HOH HOH B . 
P 5 HOH 226 826 615 HOH HOH B . 
P 5 HOH 227 827 415 HOH HOH B . 
P 5 HOH 228 828 579 HOH HOH B . 
P 5 HOH 229 829 363 HOH HOH B . 
P 5 HOH 230 830 174 HOH HOH B . 
P 5 HOH 231 831 544 HOH HOH B . 
P 5 HOH 232 832 126 HOH HOH B . 
P 5 HOH 233 833 202 HOH HOH B . 
P 5 HOH 234 834 750 HOH HOH B . 
P 5 HOH 235 835 524 HOH HOH B . 
P 5 HOH 236 836 289 HOH HOH B . 
P 5 HOH 237 837 257 HOH HOH B . 
P 5 HOH 238 838 685 HOH HOH B . 
P 5 HOH 239 839 227 HOH HOH B . 
P 5 HOH 240 840 157 HOH HOH B . 
P 5 HOH 241 841 302 HOH HOH B . 
P 5 HOH 242 842 468 HOH HOH B . 
P 5 HOH 243 843 611 HOH HOH B . 
P 5 HOH 244 844 612 HOH HOH B . 
P 5 HOH 245 845 452 HOH HOH B . 
P 5 HOH 246 846 123 HOH HOH B . 
P 5 HOH 247 847 439 HOH HOH B . 
P 5 HOH 248 848 210 HOH HOH B . 
P 5 HOH 249 849 387 HOH HOH B . 
P 5 HOH 250 850 294 HOH HOH B . 
P 5 HOH 251 851 743 HOH HOH B . 
P 5 HOH 252 852 115 HOH HOH B . 
P 5 HOH 253 853 481 HOH HOH B . 
P 5 HOH 254 854 523 HOH HOH B . 
P 5 HOH 255 855 594 HOH HOH B . 
P 5 HOH 256 856 249 HOH HOH B . 
P 5 HOH 257 857 471 HOH HOH B . 
P 5 HOH 258 858 205 HOH HOH B . 
P 5 HOH 259 859 623 HOH HOH B . 
P 5 HOH 260 860 513 HOH HOH B . 
P 5 HOH 261 861 489 HOH HOH B . 
P 5 HOH 262 862 434 HOH HOH B . 
P 5 HOH 263 863 610 HOH HOH B . 
P 5 HOH 264 864 356 HOH HOH B . 
P 5 HOH 265 865 335 HOH HOH B . 
P 5 HOH 266 866 498 HOH HOH B . 
P 5 HOH 267 867 692 HOH HOH B . 
P 5 HOH 268 868 650 HOH HOH B . 
P 5 HOH 269 869 742 HOH HOH B . 
P 5 HOH 270 870 231 HOH HOH B . 
P 5 HOH 271 871 680 HOH HOH B . 
P 5 HOH 272 872 734 HOH HOH B . 
P 5 HOH 273 873 667 HOH HOH B . 
P 5 HOH 274 874 577 HOH HOH B . 
P 5 HOH 275 875 628 HOH HOH B . 
P 5 HOH 276 876 408 HOH HOH B . 
P 5 HOH 277 877 355 HOH HOH B . 
P 5 HOH 278 878 588 HOH HOH B . 
P 5 HOH 279 879 555 HOH HOH B . 
P 5 HOH 280 880 696 HOH HOH B . 
P 5 HOH 281 881 309 HOH HOH B . 
P 5 HOH 282 882 691 HOH HOH B . 
P 5 HOH 283 883 252 HOH HOH B . 
P 5 HOH 284 884 327 HOH HOH B . 
P 5 HOH 285 885 491 HOH HOH B . 
P 5 HOH 286 886 487 HOH HOH B . 
P 5 HOH 287 887 176 HOH HOH B . 
P 5 HOH 288 888 749 HOH HOH B . 
P 5 HOH 289 889 121 HOH HOH B . 
P 5 HOH 290 890 605 HOH HOH B . 
P 5 HOH 291 891 305 HOH HOH B . 
P 5 HOH 292 892 517 HOH HOH B . 
P 5 HOH 293 893 609 HOH HOH B . 
P 5 HOH 294 894 350 HOH HOH B . 
P 5 HOH 295 895 403 HOH HOH B . 
P 5 HOH 296 896 364 HOH HOH B . 
P 5 HOH 297 897 262 HOH HOH B . 
P 5 HOH 298 898 429 HOH HOH B . 
P 5 HOH 299 899 422 HOH HOH B . 
P 5 HOH 300 900 737 HOH HOH B . 
P 5 HOH 301 901 423 HOH HOH B . 
P 5 HOH 302 902 407 HOH HOH B . 
P 5 HOH 303 903 383 HOH HOH B . 
P 5 HOH 304 904 393 HOH HOH B . 
P 5 HOH 305 905 456 HOH HOH B . 
P 5 HOH 306 906 413 HOH HOH B . 
P 5 HOH 307 907 715 HOH HOH B . 
P 5 HOH 308 908 380 HOH HOH B . 
P 5 HOH 309 909 537 HOH HOH B . 
P 5 HOH 310 910 641 HOH HOH B . 
P 5 HOH 311 911 372 HOH HOH B . 
P 5 HOH 312 912 526 HOH HOH B . 
P 5 HOH 313 913 562 HOH HOH B . 
P 5 HOH 314 914 283 HOH HOH B . 
P 5 HOH 315 915 592 HOH HOH B . 
P 5 HOH 316 916 440 HOH HOH B . 
P 5 HOH 317 917 450 HOH HOH B . 
P 5 HOH 318 918 436 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 ARG 42  ? CG  ? A ARG 42  CG  
2  1 Y 1 A ARG 42  ? CD  ? A ARG 42  CD  
3  1 Y 1 A ARG 42  ? NE  ? A ARG 42  NE  
4  1 Y 1 A ARG 42  ? CZ  ? A ARG 42  CZ  
5  1 Y 1 A ARG 42  ? NH1 ? A ARG 42  NH1 
6  1 Y 1 A ARG 42  ? NH2 ? A ARG 42  NH2 
7  1 Y 1 A ARG 361 ? CG  ? A ARG 361 CG  
8  1 Y 1 A ARG 361 ? CD  ? A ARG 361 CD  
9  1 Y 1 A ARG 361 ? NE  ? A ARG 361 NE  
10 1 Y 1 A ARG 361 ? CZ  ? A ARG 361 CZ  
11 1 Y 1 A ARG 361 ? NH1 ? A ARG 361 NH1 
12 1 Y 1 A ARG 361 ? NH2 ? A ARG 361 NH2 
13 1 Y 1 B LYS 2   ? CG  ? B LYS 2   CG  
14 1 Y 1 B LYS 2   ? CD  ? B LYS 2   CD  
15 1 Y 1 B LYS 2   ? CE  ? B LYS 2   CE  
16 1 Y 1 B LYS 2   ? NZ  ? B LYS 2   NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.13_2998 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   99.944 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8UYR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     63.744 
_cell.length_a_esd                 ? 
_cell.length_b                     92.693 
_cell.length_b_esd                 ? 
_cell.length_c                     145.122 
_cell.length_c_esd                 ? 
_cell.volume                       844593.711 
_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                         8UYR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   8UYR 
_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             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.94 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.16 M MgCl2, 0.08 M Tris pH 8.5, 16.8% PEG 4000, 20% v/v glycerol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            300 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 12M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-28 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_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                        'ALS BEAMLINE 5.0.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   5.0.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          18.74 
_reflns.entry_id                                       8UYR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.82 
_reflns.d_resolution_low                               39.44 
_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                                     68822 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           92.44 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.83 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_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                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.82 
_reflns_shell.d_res_low                                     1.885 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4565 
_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                               5.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.625 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          61.37 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_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                               21.01 
_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                                 8UYR 
_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                            1.82 
_refine.ls_d_res_low                             39.44 
_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                     68822 
_refine.ls_number_reflns_R_free                  2033 
_refine.ls_number_reflns_R_work                  66789 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.45 
_refine.ls_percent_reflns_R_free                 2.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1625 
_refine.ls_R_factor_R_free                       0.1931 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1615 
_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' 
_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             1.1100 
_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                 19.9557 
_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                            0.1749 
_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                       1.82 
_refine_hist.d_res_low                        39.44 
_refine_hist.number_atoms_solvent             671 
_refine_hist.number_atoms_total               7347 
_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        6629 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         47 
_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' ? 0.0083  ? 6909 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9831  ? 9401 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0608  ? 1002 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0065  ? 1225 ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.0109 ? 2521 ? 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' 1.82 1.86  . . 82  2831 59.05 . . . . 0.2480 . . . . . . . . . . . 0.2837 
'X-RAY DIFFRACTION' 1.86 1.91  . . 113 3259 68.34 . . . . 0.2314 . . . . . . . . . . . 0.2519 
'X-RAY DIFFRACTION' 1.91 1.96  . . 121 3864 80.65 . . . . 0.2120 . . . . . . . . . . . 0.2651 
'X-RAY DIFFRACTION' 1.96 2.02  . . 130 4593 95.09 . . . . 0.2004 . . . . . . . . . . . 0.2400 
'X-RAY DIFFRACTION' 2.02 2.08  . . 147 4744 98.49 . . . . 0.1814 . . . . . . . . . . . 0.2354 
'X-RAY DIFFRACTION' 2.08 2.16  . . 136 4730 98.52 . . . . 0.1777 . . . . . . . . . . . 0.2099 
'X-RAY DIFFRACTION' 2.16 2.24  . . 139 4739 98.72 . . . . 0.1716 . . . . . . . . . . . 0.2185 
'X-RAY DIFFRACTION' 2.24 2.35  . . 140 4695 97.28 . . . . 0.1631 . . . . . . . . . . . 0.1997 
'X-RAY DIFFRACTION' 2.35 2.47  . . 144 4725 98.82 . . . . 0.1652 . . . . . . . . . . . 0.2259 
'X-RAY DIFFRACTION' 2.47 2.62  . . 145 4727 99.04 . . . . 0.1664 . . . . . . . . . . . 0.2078 
'X-RAY DIFFRACTION' 2.62 2.83  . . 148 4716 97.53 . . . . 0.1679 . . . . . . . . . . . 0.1922 
'X-RAY DIFFRACTION' 2.83 3.11  . . 148 4774 98.86 . . . . 0.1611 . . . . . . . . . . . 0.1650 
'X-RAY DIFFRACTION' 3.11 3.56  . . 141 4795 99.10 . . . . 0.1525 . . . . . . . . . . . 0.1793 
'X-RAY DIFFRACTION' 3.56 4.49  . . 148 4755 98.34 . . . . 0.1280 . . . . . . . . . . . 0.1561 
'X-RAY DIFFRACTION' 4.49 39.44 . . 151 4842 98.46 . . . . 0.1461 . . . . . . . . . . . 0.1723 
# 
_struct.entry_id                     8UYR 
_struct.title                        'Manganese-substituted DitZ from Rhodococcus Rhodochrous' 
_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        8UYR 
_struct_keywords.text            'Monooxygenase, diterpenoid, diiron, 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 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 3 ? 
N N N 3 ? 
O N N 5 ? 
P N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8UYR 
_struct_ref.pdbx_db_accession          8UYR 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8UYR A 1 ? 423 ? 8UYR 1 ? 423 ? 1 423 
2 1 8UYR B 1 ? 423 ? 8UYR 1 ? 423 ? 1 423 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6160  ? 
1 MORE         -42   ? 
1 'SSA (A^2)'  31050 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
_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 LYS A 2   ? MET A 6   ? LYS A 2   MET A 6   5 ? 5  
HELX_P HELX_P2  AA2 ASP A 20  ? PHE A 26  ? ASP A 20  PHE A 26  1 ? 7  
HELX_P HELX_P3  AA3 PRO A 27  ? ALA A 34  ? PRO A 27  ALA A 34  5 ? 8  
HELX_P HELX_P4  AA4 PRO A 68  ? TRP A 72  ? PRO A 68  TRP A 72  5 ? 5  
HELX_P HELX_P5  AA5 GLY A 78  ? MET A 82  ? GLY A 78  MET A 82  5 ? 5  
HELX_P HELX_P6  AA6 ARG A 83  ? TYR A 87  ? ARG A 83  TYR A 87  5 ? 5  
HELX_P HELX_P7  AA7 ASP A 88  ? GLY A 100 ? ASP A 88  GLY A 100 1 ? 13 
HELX_P HELX_P8  AA8 GLY A 115 ? SER A 120 ? GLY A 115 SER A 120 1 ? 6  
HELX_P HELX_P9  AA9 ASP A 123 ? VAL A 139 ? ASP A 123 VAL A 139 1 ? 17 
HELX_P HELX_P10 AB1 GLY A 140 ? HIS A 146 ? GLY A 140 HIS A 146 1 ? 7  
HELX_P HELX_P11 AB2 ASP A 160 ? ALA A 173 ? ASP A 160 ALA A 173 1 ? 14 
HELX_P HELX_P12 AB3 THR A 184 ? VAL A 188 ? THR A 184 VAL A 188 5 ? 5  
HELX_P HELX_P13 AB4 ASP A 194 ? GLY A 198 ? ASP A 194 GLY A 198 5 ? 5  
HELX_P HELX_P14 AB5 TRP A 200 ? HIS A 210 ? TRP A 200 HIS A 210 1 ? 11 
HELX_P HELX_P15 AB6 GLY A 220 ? VAL A 225 ? GLY A 220 VAL A 225 5 ? 6  
HELX_P HELX_P16 AB7 ASP A 232 ? THR A 240 ? ASP A 232 THR A 240 1 ? 9  
HELX_P HELX_P17 AB8 PRO A 241 ? ILE A 243 ? PRO A 241 ILE A 243 5 ? 3  
HELX_P HELX_P18 AB9 SER A 244 ? SER A 254 ? SER A 244 SER A 254 1 ? 11 
HELX_P HELX_P19 AC1 GLY A 255 ? PHE A 260 ? GLY A 255 PHE A 260 1 ? 6  
HELX_P HELX_P20 AC2 TRP A 274 ? GLN A 289 ? TRP A 274 GLN A 289 1 ? 16 
HELX_P HELX_P21 AC3 SER A 290 ? GLY A 293 ? SER A 290 GLY A 293 5 ? 4  
HELX_P HELX_P22 AC4 THR A 302 ? ASN A 310 ? THR A 302 ASN A 310 1 ? 9  
HELX_P HELX_P23 AC5 SER A 320 ? ASN A 323 ? SER A 320 ASN A 323 5 ? 4  
HELX_P HELX_P24 AC6 ASN A 324 ? GLY A 329 ? ASN A 324 GLY A 329 1 ? 6  
HELX_P HELX_P25 AC7 ARG A 348 ? ALA A 360 ? ARG A 348 ALA A 360 1 ? 13 
HELX_P HELX_P26 AC8 THR A 363 ? PHE A 372 ? THR A 363 PHE A 372 1 ? 10 
HELX_P HELX_P27 AC9 PHE A 372 ? PHE A 379 ? PHE A 372 PHE A 379 1 ? 8  
HELX_P HELX_P28 AD1 PRO A 388 ? ALA A 392 ? PRO A 388 ALA A 392 5 ? 5  
HELX_P HELX_P29 AD2 THR A 393 ? ALA A 399 ? THR A 393 ALA A 399 1 ? 7  
HELX_P HELX_P30 AD3 SER A 410 ? HIS A 422 ? SER A 410 HIS A 422 1 ? 13 
HELX_P HELX_P31 AD4 LYS B 2   ? MET B 6   ? LYS B 2   MET B 6   5 ? 5  
HELX_P HELX_P32 AD5 ASP B 20  ? PHE B 26  ? ASP B 20  PHE B 26  1 ? 7  
HELX_P HELX_P33 AD6 PRO B 27  ? ALA B 34  ? PRO B 27  ALA B 34  5 ? 8  
HELX_P HELX_P34 AD7 PRO B 68  ? TRP B 72  ? PRO B 68  TRP B 72  5 ? 5  
HELX_P HELX_P35 AD8 GLY B 78  ? MET B 82  ? GLY B 78  MET B 82  5 ? 5  
HELX_P HELX_P36 AD9 ARG B 83  ? TYR B 87  ? ARG B 83  TYR B 87  5 ? 5  
HELX_P HELX_P37 AE1 ASP B 88  ? ASN B 99  ? ASP B 88  ASN B 99  1 ? 12 
HELX_P HELX_P38 AE2 GLY B 115 ? SER B 120 ? GLY B 115 SER B 120 1 ? 6  
HELX_P HELX_P39 AE3 ASP B 123 ? GLY B 140 ? ASP B 123 GLY B 140 1 ? 18 
HELX_P HELX_P40 AE4 GLY B 140 ? HIS B 146 ? GLY B 140 HIS B 146 1 ? 7  
HELX_P HELX_P41 AE5 ASP B 160 ? ALA B 173 ? ASP B 160 ALA B 173 1 ? 14 
HELX_P HELX_P42 AE6 THR B 184 ? VAL B 188 ? THR B 184 VAL B 188 5 ? 5  
HELX_P HELX_P43 AE7 ASP B 194 ? GLY B 198 ? ASP B 194 GLY B 198 5 ? 5  
HELX_P HELX_P44 AE8 TRP B 200 ? HIS B 210 ? TRP B 200 HIS B 210 1 ? 11 
HELX_P HELX_P45 AE9 GLY B 220 ? VAL B 225 ? GLY B 220 VAL B 225 5 ? 6  
HELX_P HELX_P46 AF1 ASP B 232 ? THR B 240 ? ASP B 232 THR B 240 1 ? 9  
HELX_P HELX_P47 AF2 PRO B 241 ? ILE B 243 ? PRO B 241 ILE B 243 5 ? 3  
HELX_P HELX_P48 AF3 SER B 244 ? SER B 254 ? SER B 244 SER B 254 1 ? 11 
HELX_P HELX_P49 AF4 GLY B 255 ? PHE B 260 ? GLY B 255 PHE B 260 1 ? 6  
HELX_P HELX_P50 AF5 TRP B 274 ? GLN B 289 ? TRP B 274 GLN B 289 1 ? 16 
HELX_P HELX_P51 AF6 SER B 290 ? GLY B 293 ? SER B 290 GLY B 293 5 ? 4  
HELX_P HELX_P52 AF7 THR B 302 ? ASN B 310 ? THR B 302 ASN B 310 1 ? 9  
HELX_P HELX_P53 AF8 SER B 320 ? ASN B 323 ? SER B 320 ASN B 323 5 ? 4  
HELX_P HELX_P54 AF9 ASN B 324 ? GLY B 329 ? ASN B 324 GLY B 329 1 ? 6  
HELX_P HELX_P55 AG1 ARG B 348 ? ALA B 360 ? ARG B 348 ALA B 360 1 ? 13 
HELX_P HELX_P56 AG2 THR B 363 ? PHE B 372 ? THR B 363 PHE B 372 1 ? 10 
HELX_P HELX_P57 AG3 PHE B 372 ? PHE B 379 ? PHE B 372 PHE B 379 1 ? 8  
HELX_P HELX_P58 AG4 PRO B 388 ? ALA B 392 ? PRO B 388 ALA B 392 5 ? 5  
HELX_P HELX_P59 AG5 THR B 393 ? ALA B 399 ? THR B 393 ALA B 399 1 ? 7  
HELX_P HELX_P60 AG6 ARG B 400 ? THR B 402 ? ARG B 400 THR B 402 5 ? 3  
HELX_P HELX_P61 AG7 SER B 410 ? HIS B 422 ? SER B 410 HIS B 422 1 ? 13 
# 
_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 ASP 12  OD1 ? ? ? 1_555 F MN  . MN ? ? A ASP 12  A MN  504 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc2  metalc ? ? A ASP 12  OD2 ? ? ? 1_555 F MN  . MN ? ? A ASP 12  A MN  504 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
metalc3  metalc ? ? A HIS 14  NE2 ? ? ? 1_555 F MN  . MN ? ? A HIS 14  A MN  504 1_555 ? ? ? ? ? ? ? 2.221 ? ? 
metalc4  metalc ? ? A HIS 217 NE2 ? ? ? 1_555 F MN  . MN ? ? A HIS 217 A MN  504 1_555 ? ? ? ? ? ? ? 2.177 ? ? 
metalc5  metalc ? ? A GLU 269 OE1 ? ? ? 1_555 F MN  . MN ? ? A GLU 269 A MN  504 1_555 ? ? ? ? ? ? ? 2.167 ? ? 
metalc6  metalc ? ? A GLU 269 OE1 ? ? ? 1_555 G MN  . MN ? ? A GLU 269 A MN  505 1_555 ? ? ? ? ? ? ? 2.445 ? ? 
metalc7  metalc ? ? A GLU 269 OE2 ? ? ? 1_555 G MN  . MN ? ? A GLU 269 A MN  505 1_555 ? ? ? ? ? ? ? 2.198 ? ? 
metalc8  metalc ? ? A ASP 338 OD1 ? ? ? 1_555 F MN  . MN ? ? A ASP 338 A MN  504 1_555 ? ? ? ? ? ? ? 2.171 ? ? 
metalc9  metalc ? ? A ASP 338 OD2 ? ? ? 1_555 G MN  . MN ? ? A ASP 338 A MN  505 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
metalc10 metalc ? ? A HIS 341 ND1 ? ? ? 1_555 G MN  . MN ? ? A HIS 341 A MN  505 1_555 ? ? ? ? ? ? ? 2.176 ? ? 
metalc11 metalc ? ? G MN  .   MN  ? ? ? 1_555 O HOH . O  ? ? A MN  505 A HOH 624 1_555 ? ? ? ? ? ? ? 2.162 ? ? 
metalc12 metalc ? ? G MN  .   MN  ? ? ? 1_555 O HOH . O  ? ? A MN  505 A HOH 811 1_555 ? ? ? ? ? ? ? 2.122 ? ? 
metalc13 metalc ? ? H MG  .   MG  ? ? ? 1_555 O HOH . O  ? ? A MG  506 A HOH 651 2_655 ? ? ? ? ? ? ? 2.088 ? ? 
metalc14 metalc ? ? H MG  .   MG  ? ? ? 1_555 O HOH . O  ? ? A MG  506 A HOH 704 2_655 ? ? ? ? ? ? ? 2.211 ? ? 
metalc15 metalc ? ? H MG  .   MG  ? ? ? 1_555 O HOH . O  ? ? A MG  506 A HOH 755 1_555 ? ? ? ? ? ? ? 2.189 ? ? 
metalc16 metalc ? ? H MG  .   MG  ? ? ? 1_555 O HOH . O  ? ? A MG  506 A HOH 809 1_555 ? ? ? ? ? ? ? 2.007 ? ? 
metalc17 metalc ? ? H MG  .   MG  ? ? ? 1_555 O HOH . O  ? ? A MG  506 A HOH 899 2_655 ? ? ? ? ? ? ? 2.175 ? ? 
metalc18 metalc ? ? H MG  .   MG  ? ? ? 1_555 O HOH . O  ? ? A MG  506 A HOH 942 2_655 ? ? ? ? ? ? ? 2.036 ? ? 
metalc19 metalc ? ? B ASP 12  OD1 ? ? ? 1_555 M MN  . MN ? ? B ASP 12  B MN  505 1_555 ? ? ? ? ? ? ? 2.332 ? ? 
metalc20 metalc ? ? B ASP 12  OD2 ? ? ? 1_555 M MN  . MN ? ? B ASP 12  B MN  505 1_555 ? ? ? ? ? ? ? 2.223 ? ? 
metalc21 metalc ? ? B HIS 14  NE2 ? ? ? 1_555 M MN  . MN ? ? B HIS 14  B MN  505 1_555 ? ? ? ? ? ? ? 2.277 ? ? 
metalc22 metalc ? ? B HIS 217 NE2 ? ? ? 1_555 M MN  . MN ? ? B HIS 217 B MN  505 1_555 ? ? ? ? ? ? ? 2.247 ? ? 
metalc23 metalc ? ? B GLU 269 OE1 ? ? ? 1_555 M MN  . MN ? ? B GLU 269 B MN  505 1_555 ? ? ? ? ? ? ? 2.143 ? ? 
metalc24 metalc ? ? B GLU 269 OE1 ? ? ? 1_555 N MN  . MN ? ? B GLU 269 B MN  506 1_555 ? ? ? ? ? ? ? 2.343 ? ? 
metalc25 metalc ? ? B GLU 269 OE2 ? ? ? 1_555 N MN  . MN ? ? B GLU 269 B MN  506 1_555 ? ? ? ? ? ? ? 2.166 ? ? 
metalc26 metalc ? ? B ASP 338 OD1 ? ? ? 1_555 M MN  . MN ? ? B ASP 338 B MN  505 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
metalc27 metalc ? ? B ASP 338 OD2 ? ? ? 1_555 N MN  . MN ? ? B ASP 338 B MN  506 1_555 ? ? ? ? ? ? ? 2.131 ? ? 
metalc28 metalc ? ? B HIS 341 ND1 ? ? ? 1_555 N MN  . MN ? ? B HIS 341 B MN  506 1_555 ? ? ? ? ? ? ? 2.138 ? ? 
metalc29 metalc ? ? N MN  .   MN  ? ? ? 1_555 P HOH . O  ? ? B MN  506 B HOH 607 1_555 ? ? ? ? ? ? ? 2.182 ? ? 
metalc30 metalc ? ? N MN  .   MN  ? ? ? 1_555 P HOH . O  ? ? B MN  506 B HOH 804 1_555 ? ? ? ? ? ? ? 2.179 ? ? 
# 
_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  OD1 ? A ASP 12  ? A ASP 12  ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 OD2 ? A ASP 12  ? A ASP 12  ? 1_555 56.7  ? 
2  OD1 ? A ASP 12  ? A ASP 12  ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 NE2 ? A HIS 14  ? A HIS 14  ? 1_555 94.5  ? 
3  OD2 ? A ASP 12  ? A ASP 12  ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 NE2 ? A HIS 14  ? A HIS 14  ? 1_555 150.8 ? 
4  OD1 ? A ASP 12  ? A ASP 12  ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 NE2 ? A HIS 217 ? A HIS 217 ? 1_555 93.3  ? 
5  OD2 ? A ASP 12  ? A ASP 12  ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 NE2 ? A HIS 217 ? A HIS 217 ? 1_555 94.9  ? 
6  NE2 ? A HIS 14  ? A HIS 14  ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 NE2 ? A HIS 217 ? A HIS 217 ? 1_555 91.3  ? 
7  OD1 ? A ASP 12  ? A ASP 12  ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 OE1 ? A GLU 269 ? A GLU 269 ? 1_555 151.8 ? 
8  OD2 ? A ASP 12  ? A ASP 12  ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 OE1 ? A GLU 269 ? A GLU 269 ? 1_555 95.2  ? 
9  NE2 ? A HIS 14  ? A HIS 14  ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 OE1 ? A GLU 269 ? A GLU 269 ? 1_555 113.7 ? 
10 NE2 ? A HIS 217 ? A HIS 217 ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 OE1 ? A GLU 269 ? A GLU 269 ? 1_555 85.7  ? 
11 OD1 ? A ASP 12  ? A ASP 12  ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 OD1 ? A ASP 338 ? A ASP 338 ? 1_555 99.1  ? 
12 OD2 ? A ASP 12  ? A ASP 12  ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 OD1 ? A ASP 338 ? A ASP 338 ? 1_555 92.8  ? 
13 NE2 ? A HIS 14  ? A HIS 14  ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 OD1 ? A ASP 338 ? A ASP 338 ? 1_555 86.6  ? 
14 NE2 ? A HIS 217 ? A HIS 217 ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 OD1 ? A ASP 338 ? A ASP 338 ? 1_555 167.6 ? 
15 OE1 ? A GLU 269 ? A GLU 269 ? 1_555 MN ? F MN . ? A MN 504 ? 1_555 OD1 ? A ASP 338 ? A ASP 338 ? 1_555 83.9  ? 
16 OE1 ? A GLU 269 ? A GLU 269 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 OE2 ? A GLU 269 ? A GLU 269 ? 1_555 56.0  ? 
17 OE1 ? A GLU 269 ? A GLU 269 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 OD2 ? A ASP 338 ? A ASP 338 ? 1_555 84.8  ? 
18 OE2 ? A GLU 269 ? A GLU 269 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 OD2 ? A ASP 338 ? A ASP 338 ? 1_555 87.8  ? 
19 OE1 ? A GLU 269 ? A GLU 269 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 ND1 ? A HIS 341 ? A HIS 341 ? 1_555 116.3 ? 
20 OE2 ? A GLU 269 ? A GLU 269 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 ND1 ? A HIS 341 ? A HIS 341 ? 1_555 171.0 ? 
21 OD2 ? A ASP 338 ? A ASP 338 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 ND1 ? A HIS 341 ? A HIS 341 ? 1_555 96.3  ? 
22 OE1 ? A GLU 269 ? A GLU 269 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 O   ? O HOH .   ? A HOH 624 ? 1_555 149.2 ? 
23 OE2 ? A GLU 269 ? A GLU 269 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 O   ? O HOH .   ? A HOH 624 ? 1_555 93.2  ? 
24 OD2 ? A ASP 338 ? A ASP 338 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 O   ? O HOH .   ? A HOH 624 ? 1_555 95.4  ? 
25 ND1 ? A HIS 341 ? A HIS 341 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 O   ? O HOH .   ? A HOH 624 ? 1_555 94.4  ? 
26 OE1 ? A GLU 269 ? A GLU 269 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 O   ? O HOH .   ? A HOH 811 ? 1_555 81.6  ? 
27 OE2 ? A GLU 269 ? A GLU 269 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 O   ? O HOH .   ? A HOH 811 ? 1_555 84.6  ? 
28 OD2 ? A ASP 338 ? A ASP 338 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 O   ? O HOH .   ? A HOH 811 ? 1_555 166.4 ? 
29 ND1 ? A HIS 341 ? A HIS 341 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 O   ? O HOH .   ? A HOH 811 ? 1_555 89.8  ? 
30 O   ? O HOH .   ? A HOH 624 ? 1_555 MN ? G MN . ? A MN 505 ? 1_555 O   ? O HOH .   ? A HOH 811 ? 1_555 96.3  ? 
31 O   ? O HOH .   ? A HOH 651 ? 2_655 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 704 ? 2_655 91.4  ? 
32 O   ? O HOH .   ? A HOH 651 ? 2_655 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 755 ? 1_555 79.1  ? 
33 O   ? O HOH .   ? A HOH 704 ? 2_655 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 755 ? 1_555 89.1  ? 
34 O   ? O HOH .   ? A HOH 651 ? 2_655 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 809 ? 1_555 92.7  ? 
35 O   ? O HOH .   ? A HOH 704 ? 2_655 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 809 ? 1_555 174.1 ? 
36 O   ? O HOH .   ? A HOH 755 ? 1_555 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 809 ? 1_555 95.9  ? 
37 O   ? O HOH .   ? A HOH 651 ? 2_655 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 899 ? 2_655 90.2  ? 
38 O   ? O HOH .   ? A HOH 704 ? 2_655 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 899 ? 2_655 85.6  ? 
39 O   ? O HOH .   ? A HOH 755 ? 1_555 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 899 ? 2_655 167.9 ? 
40 O   ? O HOH .   ? A HOH 809 ? 1_555 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 899 ? 2_655 90.2  ? 
41 O   ? O HOH .   ? A HOH 651 ? 2_655 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 942 ? 2_655 174.5 ? 
42 O   ? O HOH .   ? A HOH 704 ? 2_655 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 942 ? 2_655 84.0  ? 
43 O   ? O HOH .   ? A HOH 755 ? 1_555 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 942 ? 2_655 103.8 ? 
44 O   ? O HOH .   ? A HOH 809 ? 1_555 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 942 ? 2_655 91.7  ? 
45 O   ? O HOH .   ? A HOH 899 ? 2_655 MG ? H MG . ? A MG 506 ? 1_555 O   ? O HOH .   ? A HOH 942 ? 2_655 86.4  ? 
46 OD1 ? B ASP 12  ? B ASP 12  ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 OD2 ? B ASP 12  ? B ASP 12  ? 1_555 57.0  ? 
47 OD1 ? B ASP 12  ? B ASP 12  ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 NE2 ? B HIS 14  ? B HIS 14  ? 1_555 93.0  ? 
48 OD2 ? B ASP 12  ? B ASP 12  ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 NE2 ? B HIS 14  ? B HIS 14  ? 1_555 149.3 ? 
49 OD1 ? B ASP 12  ? B ASP 12  ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 NE2 ? B HIS 217 ? B HIS 217 ? 1_555 96.0  ? 
50 OD2 ? B ASP 12  ? B ASP 12  ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 NE2 ? B HIS 217 ? B HIS 217 ? 1_555 96.9  ? 
51 NE2 ? B HIS 14  ? B HIS 14  ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 NE2 ? B HIS 217 ? B HIS 217 ? 1_555 92.0  ? 
52 OD1 ? B ASP 12  ? B ASP 12  ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 OE1 ? B GLU 269 ? B GLU 269 ? 1_555 152.8 ? 
53 OD2 ? B ASP 12  ? B ASP 12  ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 OE1 ? B GLU 269 ? B GLU 269 ? 1_555 95.8  ? 
54 NE2 ? B HIS 14  ? B HIS 14  ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 OE1 ? B GLU 269 ? B GLU 269 ? 1_555 114.2 ? 
55 NE2 ? B HIS 217 ? B HIS 217 ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 OE1 ? B GLU 269 ? B GLU 269 ? 1_555 85.7  ? 
56 OD1 ? B ASP 12  ? B ASP 12  ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 OD1 ? B ASP 338 ? B ASP 338 ? 1_555 98.3  ? 
57 OD2 ? B ASP 12  ? B ASP 12  ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 OD1 ? B ASP 338 ? B ASP 338 ? 1_555 91.7  ? 
58 NE2 ? B HIS 14  ? B HIS 14  ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 OD1 ? B ASP 338 ? B ASP 338 ? 1_555 86.3  ? 
59 NE2 ? B HIS 217 ? B HIS 217 ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 OD1 ? B ASP 338 ? B ASP 338 ? 1_555 165.7 ? 
60 OE1 ? B GLU 269 ? B GLU 269 ? 1_555 MN ? M MN . ? B MN 505 ? 1_555 OD1 ? B ASP 338 ? B ASP 338 ? 1_555 82.1  ? 
61 OE1 ? B GLU 269 ? B GLU 269 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 OE2 ? B GLU 269 ? B GLU 269 ? 1_555 57.9  ? 
62 OE1 ? B GLU 269 ? B GLU 269 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 OD2 ? B ASP 338 ? B ASP 338 ? 1_555 82.8  ? 
63 OE2 ? B GLU 269 ? B GLU 269 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 OD2 ? B ASP 338 ? B ASP 338 ? 1_555 88.8  ? 
64 OE1 ? B GLU 269 ? B GLU 269 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 ND1 ? B HIS 341 ? B HIS 341 ? 1_555 118.8 ? 
65 OE2 ? B GLU 269 ? B GLU 269 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 ND1 ? B HIS 341 ? B HIS 341 ? 1_555 173.9 ? 
66 OD2 ? B ASP 338 ? B ASP 338 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 ND1 ? B HIS 341 ? B HIS 341 ? 1_555 95.9  ? 
67 OE1 ? B GLU 269 ? B GLU 269 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 O   ? P HOH .   ? B HOH 607 ? 1_555 149.1 ? 
68 OE2 ? B GLU 269 ? B GLU 269 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 O   ? P HOH .   ? B HOH 607 ? 1_555 91.2  ? 
69 OD2 ? B ASP 338 ? B ASP 338 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 O   ? P HOH .   ? B HOH 607 ? 1_555 96.9  ? 
70 ND1 ? B HIS 341 ? B HIS 341 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 O   ? P HOH .   ? B HOH 607 ? 1_555 92.0  ? 
71 OE1 ? B GLU 269 ? B GLU 269 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 O   ? P HOH .   ? B HOH 804 ? 1_555 86.8  ? 
72 OE2 ? B GLU 269 ? B GLU 269 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 O   ? P HOH .   ? B HOH 804 ? 1_555 89.0  ? 
73 OD2 ? B ASP 338 ? B ASP 338 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 O   ? P HOH .   ? B HOH 804 ? 1_555 168.9 ? 
74 ND1 ? B HIS 341 ? B HIS 341 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 O   ? P HOH .   ? B HOH 804 ? 1_555 85.7  ? 
75 O   ? P HOH .   ? B HOH 607 ? 1_555 MN ? N MN . ? B MN 506 ? 1_555 O   ? P HOH .   ? B HOH 804 ? 1_555 94.1  ? 
# 
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 TYR 339 A . ? TYR 339 A PRO 340 A ? PRO 340 A 1 -0.41 
2 TRP 346 A . ? TRP 346 A PRO 347 A ? PRO 347 A 1 2.60  
3 TYR 339 B . ? TYR 339 B PRO 340 B ? PRO 340 B 1 2.75  
4 TRP 346 B . ? TRP 346 B PRO 347 B ? PRO 347 B 1 -1.00 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 6 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 3 ? 
AA9 ? 2 ? 
AB1 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA6 1 2 ? parallel      
AA7 1 2 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? parallel      
AB1 4 5 ? parallel      
AB1 5 6 ? 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 MET A 8   ? ILE A 9   ? MET A 8   ILE A 9   
AA1 2 THR A 101 ? ALA A 103 ? THR A 101 ALA A 103 
AA2 1 ASP A 13  ? HIS A 14  ? ASP A 13  HIS A 14  
AA2 2 LEU A 106 ? PHE A 107 ? LEU A 106 PHE A 107 
AA3 1 LYS A 36  ? HIS A 40  ? LYS A 36  HIS A 40  
AA3 2 ASN A 43  ? PHE A 51  ? ASN A 43  PHE A 51  
AA3 3 THR A 54  ? VAL A 56  ? THR A 54  VAL A 56  
AA4 1 SER A 58  ? SER A 59  ? SER A 58  SER A 59  
AA4 2 PRO A 76  ? THR A 77  ? PRO A 76  THR A 77  
AA5 1 ILE A 153 ? GLY A 154 ? ILE A 153 GLY A 154 
AA5 2 SER A 178 ? SER A 180 ? SER A 178 SER A 180 
AA5 3 VAL A 213 ? SER A 215 ? VAL A 213 SER A 215 
AA5 4 VAL A 265 ? MET A 267 ? VAL A 265 MET A 267 
AA5 5 PHE A 311 ? TYR A 315 ? PHE A 311 TYR A 315 
AA5 6 ILE A 333 ? TRP A 335 ? ILE A 333 TRP A 335 
AA6 1 MET B 8   ? ILE B 9   ? MET B 8   ILE B 9   
AA6 2 THR B 101 ? ALA B 103 ? THR B 101 ALA B 103 
AA7 1 ASP B 13  ? HIS B 14  ? ASP B 13  HIS B 14  
AA7 2 LEU B 106 ? PHE B 107 ? LEU B 106 PHE B 107 
AA8 1 LYS B 36  ? HIS B 40  ? LYS B 36  HIS B 40  
AA8 2 ASN B 43  ? PHE B 51  ? ASN B 43  PHE B 51  
AA8 3 THR B 54  ? VAL B 56  ? THR B 54  VAL B 56  
AA9 1 SER B 58  ? SER B 59  ? SER B 58  SER B 59  
AA9 2 PRO B 76  ? THR B 77  ? PRO B 76  THR B 77  
AB1 1 ILE B 153 ? GLY B 154 ? ILE B 153 GLY B 154 
AB1 2 SER B 178 ? SER B 180 ? SER B 178 SER B 180 
AB1 3 VAL B 213 ? SER B 215 ? VAL B 213 SER B 215 
AB1 4 VAL B 265 ? MET B 267 ? VAL B 265 MET B 267 
AB1 5 PHE B 311 ? TYR B 315 ? PHE B 311 TYR B 315 
AB1 6 ILE B 333 ? TRP B 335 ? ILE B 333 TRP B 335 
# 
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 MET A 8   ? N MET A 8   O LEU A 102 ? O LEU A 102 
AA2 1 2 N ASP A 13  ? N ASP A 13  O PHE A 107 ? O PHE A 107 
AA3 1 2 N THR A 38  ? N THR A 38  O ALA A 48  ? O ALA A 48  
AA3 2 3 N TRP A 49  ? N TRP A 49  O VAL A 56  ? O VAL A 56  
AA4 1 2 N SER A 58  ? N SER A 58  O THR A 77  ? O THR A 77  
AA5 1 2 N GLY A 154 ? N GLY A 154 O SER A 180 ? O SER A 180 
AA5 2 3 N ILE A 179 ? N ILE A 179 O SER A 215 ? O SER A 215 
AA5 3 4 N LEU A 214 ? N LEU A 214 O ALA A 266 ? O ALA A 266 
AA5 4 5 N MET A 267 ? N MET A 267 O LEU A 312 ? O LEU A 312 
AA5 5 6 N ALA A 313 ? N ALA A 313 O ALA A 334 ? O ALA A 334 
AA6 1 2 N MET B 8   ? N MET B 8   O LEU B 102 ? O LEU B 102 
AA7 1 2 N ASP B 13  ? N ASP B 13  O PHE B 107 ? O PHE B 107 
AA8 1 2 N LYS B 36  ? N LYS B 36  O GLN B 50  ? O GLN B 50  
AA8 2 3 N TRP B 49  ? N TRP B 49  O VAL B 56  ? O VAL B 56  
AA9 1 2 N SER B 58  ? N SER B 58  O THR B 77  ? O THR B 77  
AB1 1 2 N GLY B 154 ? N GLY B 154 O SER B 180 ? O SER B 180 
AB1 2 3 N ILE B 179 ? N ILE B 179 O SER B 215 ? O SER B 215 
AB1 3 4 N LEU B 214 ? N LEU B 214 O ALA B 266 ? O ALA B 266 
AB1 4 5 N MET B 267 ? N MET B 267 O LEU B 312 ? O LEU B 312 
AB1 5 6 N ALA B 313 ? N ALA B 313 O ALA B 334 ? O ALA B 334 
# 
_pdbx_entry_details.entry_id                   8UYR 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CE3 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            TRP 
_pdbx_validate_rmsd_bond.auth_seq_id_1             381 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CZ3 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            TRP 
_pdbx_validate_rmsd_bond.auth_seq_id_2             381 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.258 
_pdbx_validate_rmsd_bond.bond_target_value         1.380 
_pdbx_validate_rmsd_bond.bond_deviation            -0.122 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.017 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA A VAL 65 ? ? C A VAL 65 ? ? N A SER 66 ? ? 103.44 117.20 -13.76 2.20 Y 
2 1 O  A VAL 65 ? ? C A VAL 65 ? ? N A SER 66 ? ? 135.08 122.70 12.38  1.60 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 43  ? ? -175.29 85.23  
2  1 ALA A 63  ? ? -146.45 49.27  
3  1 SER A 66  ? ? 71.43   -7.61  
4  1 THR A 109 ? ? -102.94 -71.28 
5  1 GLU A 318 ? ? -166.77 81.69  
6  1 PHE A 372 ? ? -155.00 -31.67 
7  1 ASN B 43  ? ? -156.91 89.38  
8  1 ALA B 63  ? ? -145.56 48.82  
9  1 SER B 66  ? ? 76.53   -8.67  
10 1 THR B 109 ? ? -101.47 -67.55 
11 1 GLU B 269 ? ? 59.47   18.89  
12 1 ILE B 316 ? ? -91.83  -61.71 
13 1 GLU B 318 ? ? -167.37 80.84  
14 1 PHE B 372 ? ? -155.37 -34.15 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 ARG A 327 ? ? 10.75 
2 1 ARG B 327 ? ? 10.63 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 753 ? O HOH . 
2 1 A HOH 770 ? O HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       953 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.08 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     SER 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      423 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    B 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    SER 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     423 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
GOL C1   C  N N 137 
GOL O1   O  N N 138 
GOL C2   C  N N 139 
GOL O2   O  N N 140 
GOL C3   C  N N 141 
GOL O3   O  N N 142 
GOL H11  H  N N 143 
GOL H12  H  N N 144 
GOL HO1  H  N N 145 
GOL H2   H  N N 146 
GOL HO2  H  N N 147 
GOL H31  H  N N 148 
GOL H32  H  N N 149 
GOL HO3  H  N N 150 
HIS N    N  N N 151 
HIS CA   C  N S 152 
HIS C    C  N N 153 
HIS O    O  N N 154 
HIS CB   C  N N 155 
HIS CG   C  Y N 156 
HIS ND1  N  Y N 157 
HIS CD2  C  Y N 158 
HIS CE1  C  Y N 159 
HIS NE2  N  Y N 160 
HIS OXT  O  N N 161 
HIS H    H  N N 162 
HIS H2   H  N N 163 
HIS HA   H  N N 164 
HIS HB2  H  N N 165 
HIS HB3  H  N N 166 
HIS HD1  H  N N 167 
HIS HD2  H  N N 168 
HIS HE1  H  N N 169 
HIS HE2  H  N N 170 
HIS HXT  H  N N 171 
HOH O    O  N N 172 
HOH H1   H  N N 173 
HOH H2   H  N N 174 
ILE N    N  N N 175 
ILE CA   C  N S 176 
ILE C    C  N N 177 
ILE O    O  N N 178 
ILE CB   C  N S 179 
ILE CG1  C  N N 180 
ILE CG2  C  N N 181 
ILE CD1  C  N N 182 
ILE OXT  O  N N 183 
ILE H    H  N N 184 
ILE H2   H  N N 185 
ILE HA   H  N N 186 
ILE HB   H  N N 187 
ILE HG12 H  N N 188 
ILE HG13 H  N N 189 
ILE HG21 H  N N 190 
ILE HG22 H  N N 191 
ILE HG23 H  N N 192 
ILE HD11 H  N N 193 
ILE HD12 H  N N 194 
ILE HD13 H  N N 195 
ILE HXT  H  N N 196 
LEU N    N  N N 197 
LEU CA   C  N S 198 
LEU C    C  N N 199 
LEU O    O  N N 200 
LEU CB   C  N N 201 
LEU CG   C  N N 202 
LEU CD1  C  N N 203 
LEU CD2  C  N N 204 
LEU OXT  O  N N 205 
LEU H    H  N N 206 
LEU H2   H  N N 207 
LEU HA   H  N N 208 
LEU HB2  H  N N 209 
LEU HB3  H  N N 210 
LEU HG   H  N N 211 
LEU HD11 H  N N 212 
LEU HD12 H  N N 213 
LEU HD13 H  N N 214 
LEU HD21 H  N N 215 
LEU HD22 H  N N 216 
LEU HD23 H  N N 217 
LEU HXT  H  N N 218 
LYS N    N  N N 219 
LYS CA   C  N S 220 
LYS C    C  N N 221 
LYS O    O  N N 222 
LYS CB   C  N N 223 
LYS CG   C  N N 224 
LYS CD   C  N N 225 
LYS CE   C  N N 226 
LYS NZ   N  N N 227 
LYS OXT  O  N N 228 
LYS H    H  N N 229 
LYS H2   H  N N 230 
LYS HA   H  N N 231 
LYS HB2  H  N N 232 
LYS HB3  H  N N 233 
LYS HG2  H  N N 234 
LYS HG3  H  N N 235 
LYS HD2  H  N N 236 
LYS HD3  H  N N 237 
LYS HE2  H  N N 238 
LYS HE3  H  N N 239 
LYS HZ1  H  N N 240 
LYS HZ2  H  N N 241 
LYS HZ3  H  N N 242 
LYS HXT  H  N N 243 
MET N    N  N N 244 
MET CA   C  N S 245 
MET C    C  N N 246 
MET O    O  N N 247 
MET CB   C  N N 248 
MET CG   C  N N 249 
MET SD   S  N N 250 
MET CE   C  N N 251 
MET OXT  O  N N 252 
MET H    H  N N 253 
MET H2   H  N N 254 
MET HA   H  N N 255 
MET HB2  H  N N 256 
MET HB3  H  N N 257 
MET HG2  H  N N 258 
MET HG3  H  N N 259 
MET HE1  H  N N 260 
MET HE2  H  N N 261 
MET HE3  H  N N 262 
MET HXT  H  N N 263 
MG  MG   MG N N 264 
MN  MN   MN N N 265 
PHE N    N  N N 266 
PHE CA   C  N S 267 
PHE C    C  N N 268 
PHE O    O  N N 269 
PHE CB   C  N N 270 
PHE CG   C  Y N 271 
PHE CD1  C  Y N 272 
PHE CD2  C  Y N 273 
PHE CE1  C  Y N 274 
PHE CE2  C  Y N 275 
PHE CZ   C  Y N 276 
PHE OXT  O  N N 277 
PHE H    H  N N 278 
PHE H2   H  N N 279 
PHE HA   H  N N 280 
PHE HB2  H  N N 281 
PHE HB3  H  N N 282 
PHE HD1  H  N N 283 
PHE HD2  H  N N 284 
PHE HE1  H  N N 285 
PHE HE2  H  N N 286 
PHE HZ   H  N N 287 
PHE HXT  H  N N 288 
PRO N    N  N N 289 
PRO CA   C  N S 290 
PRO C    C  N N 291 
PRO O    O  N N 292 
PRO CB   C  N N 293 
PRO CG   C  N N 294 
PRO CD   C  N N 295 
PRO OXT  O  N N 296 
PRO H    H  N N 297 
PRO HA   H  N N 298 
PRO HB2  H  N N 299 
PRO HB3  H  N N 300 
PRO HG2  H  N N 301 
PRO HG3  H  N N 302 
PRO HD2  H  N N 303 
PRO HD3  H  N N 304 
PRO HXT  H  N N 305 
SER N    N  N N 306 
SER CA   C  N S 307 
SER C    C  N N 308 
SER O    O  N N 309 
SER CB   C  N N 310 
SER OG   O  N N 311 
SER OXT  O  N N 312 
SER H    H  N N 313 
SER H2   H  N N 314 
SER HA   H  N N 315 
SER HB2  H  N N 316 
SER HB3  H  N N 317 
SER HG   H  N N 318 
SER HXT  H  N N 319 
THR N    N  N N 320 
THR CA   C  N S 321 
THR C    C  N N 322 
THR O    O  N N 323 
THR CB   C  N R 324 
THR OG1  O  N N 325 
THR CG2  C  N N 326 
THR OXT  O  N N 327 
THR H    H  N N 328 
THR H2   H  N N 329 
THR HA   H  N N 330 
THR HB   H  N N 331 
THR HG1  H  N N 332 
THR HG21 H  N N 333 
THR HG22 H  N N 334 
THR HG23 H  N N 335 
THR HXT  H  N N 336 
TRP N    N  N N 337 
TRP CA   C  N S 338 
TRP C    C  N N 339 
TRP O    O  N N 340 
TRP CB   C  N N 341 
TRP CG   C  Y N 342 
TRP CD1  C  Y N 343 
TRP CD2  C  Y N 344 
TRP NE1  N  Y N 345 
TRP CE2  C  Y N 346 
TRP CE3  C  Y N 347 
TRP CZ2  C  Y N 348 
TRP CZ3  C  Y N 349 
TRP CH2  C  Y N 350 
TRP OXT  O  N N 351 
TRP H    H  N N 352 
TRP H2   H  N N 353 
TRP HA   H  N N 354 
TRP HB2  H  N N 355 
TRP HB3  H  N N 356 
TRP HD1  H  N N 357 
TRP HE1  H  N N 358 
TRP HE3  H  N N 359 
TRP HZ2  H  N N 360 
TRP HZ3  H  N N 361 
TRP HH2  H  N N 362 
TRP HXT  H  N N 363 
TYR N    N  N N 364 
TYR CA   C  N S 365 
TYR C    C  N N 366 
TYR O    O  N N 367 
TYR CB   C  N N 368 
TYR CG   C  Y N 369 
TYR CD1  C  Y N 370 
TYR CD2  C  Y N 371 
TYR CE1  C  Y N 372 
TYR CE2  C  Y N 373 
TYR CZ   C  Y N 374 
TYR OH   O  N N 375 
TYR OXT  O  N N 376 
TYR H    H  N N 377 
TYR H2   H  N N 378 
TYR HA   H  N N 379 
TYR HB2  H  N N 380 
TYR HB3  H  N N 381 
TYR HD1  H  N N 382 
TYR HD2  H  N N 383 
TYR HE1  H  N N 384 
TYR HE2  H  N N 385 
TYR HH   H  N N 386 
TYR HXT  H  N N 387 
VAL N    N  N N 388 
VAL CA   C  N S 389 
VAL C    C  N N 390 
VAL O    O  N N 391 
VAL CB   C  N N 392 
VAL CG1  C  N N 393 
VAL CG2  C  N N 394 
VAL OXT  O  N N 395 
VAL H    H  N N 396 
VAL H2   H  N N 397 
VAL HA   H  N N 398 
VAL HB   H  N N 399 
VAL HG11 H  N N 400 
VAL HG12 H  N N 401 
VAL HG13 H  N N 402 
VAL HG21 H  N N 403 
VAL HG22 H  N N 404 
VAL HG23 H  N N 405 
VAL HXT  H  N N 406 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   A0A2X4U804 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8UYR 
_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]   0.015688 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002750 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010788 
_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]   0.006996 
_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_b1 
_atom_type.scat_Cromer_Mann_b2 
_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.
;
? 
MG ? ? 9.41153  2.53737 2.59044  63.03566 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MN ? ? 20.23591 4.67902 2.76514  44.01191 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.
;
? 
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   . MET A 1 1   ? 13.13200  45.41100  17.29500 1.000 31.51000 ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 12.46900  44.45200  16.41000 1.000 32.94000 ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 11.15500  43.96500  17.02200 1.000 28.57000 ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 11.08300  43.70500  18.21900 1.000 28.17000 ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 13.39500  43.26100  16.11800 1.000 34.26000 ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 12.81900  42.23800  15.15900 1.000 31.28000 ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 13.63600  40.62200  15.21400 1.000 28.08000 ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 15.33700  41.10600  14.96300 1.000 22.16000 ? 1   MET A CE  1 
ATOM   9    N  N   . LYS A 1 2   ? 10.11700  43.85900  16.19500 1.000 25.92000 ? 2   LYS A N   1 
ATOM   10   C  CA  . LYS A 1 2   ? 8.83400   43.33600  16.64000 1.000 27.61000 ? 2   LYS A CA  1 
ATOM   11   C  C   . LYS A 1 2   ? 8.83500   41.81300  16.60800 1.000 23.09000 ? 2   LYS A C   1 
ATOM   12   O  O   . LYS A 1 2   ? 9.56600   41.19100  15.83600 1.000 21.07000 ? 2   LYS A O   1 
ATOM   13   C  CB  . LYS A 1 2   ? 7.70000   43.85200  15.75600 1.000 25.33000 ? 2   LYS A CB  1 
ATOM   14   C  CG  . LYS A 1 2   ? 7.48700   45.34800  15.84600 1.000 31.47000 ? 2   LYS A CG  1 
ATOM   15   C  CD  . LYS A 1 2   ? 6.22000   45.77600  15.13600 1.000 40.28000 ? 2   LYS A CD  1 
ATOM   16   C  CE  . LYS A 1 2   ? 6.46300   47.10400  14.43200 1.000 43.31000 ? 2   LYS A CE  1 
ATOM   17   N  NZ  . LYS A 1 2   ? 7.37100   47.99100  15.23800 1.000 48.10000 ? 2   LYS A NZ  1 
ATOM   18   N  N   . THR A 1 3   ? 7.97100   41.21800  17.43700 1.000 23.59000 ? 3   THR A N   1 
ATOM   19   C  CA  . THR A 1 3   ? 7.84400   39.76200  17.44900 1.000 24.48000 ? 3   THR A CA  1 
ATOM   20   C  C   . THR A 1 3   ? 7.61000   39.22200  16.04400 1.000 20.42000 ? 3   THR A C   1 
ATOM   21   O  O   . THR A 1 3   ? 8.25300   38.25100  15.62600 1.000 20.34000 ? 3   THR A O   1 
ATOM   22   C  CB  . THR A 1 3   ? 6.71300   39.34300  18.38600 1.000 23.34000 ? 3   THR A CB  1 
ATOM   23   O  OG1 . THR A 1 3   ? 7.03300   39.74900  19.72300 1.000 23.49000 ? 3   THR A OG1 1 
ATOM   24   C  CG2 . THR A 1 3   ? 6.50300   37.81800  18.35000 1.000 18.52000 ? 3   THR A CG2 1 
ATOM   25   N  N   . GLU A 1 4   ? 6.74700   39.89500  15.27500 1.000 20.55000 ? 4   GLU A N   1 
ATOM   26   C  CA  . GLU A 1 4   ? 6.33400   39.42000  13.95800 1.000 20.98000 ? 4   GLU A CA  1 
ATOM   27   C  C   . GLU A 1 4   ? 7.45800   39.45700  12.93500 1.000 20.96000 ? 4   GLU A C   1 
ATOM   28   O  O   . GLU A 1 4   ? 7.34100   38.82300  11.88300 1.000 17.63000 ? 4   GLU A O   1 
ATOM   29   C  CB  . GLU A 1 4   ? 5.16300   40.26200  13.44300 1.000 21.09000 ? 4   GLU A CB  1 
ATOM   30   C  CG  . GLU A 1 4   ? 5.55900   41.70000  13.14100 1.000 25.30000 ? 4   GLU A CG  1 
ATOM   31   C  CD  . GLU A 1 4   ? 4.43500   42.51200  12.51700 1.000 30.61000 ? 4   GLU A CD  1 
ATOM   32   O  OE1 . GLU A 1 4   ? 3.33800   41.95300  12.30300 1.000 37.23000 ? 4   GLU A OE1 1 
ATOM   33   O  OE2 . GLU A 1 4   ? 4.64600   43.71700  12.25400 1.000 28.53000 ? 4   GLU A OE2 1 
ATOM   34   N  N   . ASP A 1 5   ? 8.53900   40.18300  13.20400 1.000 21.33000 ? 5   ASP A N   1 
ATOM   35   C  CA  . ASP A 1 5   ? 9.62700   40.27300  12.24300 1.000 18.45000 ? 5   ASP A CA  1 
ATOM   36   C  C   . ASP A 1 5   ? 10.76200  39.31000  12.54700 1.000 17.51000 ? 5   ASP A C   1 
ATOM   37   O  O   . ASP A 1 5   ? 11.75700  39.30800  11.82500 1.000 18.20000 ? 5   ASP A O   1 
ATOM   38   C  CB  . ASP A 1 5   ? 10.16100  41.70500  12.17100 1.000 22.22000 ? 5   ASP A CB  1 
ATOM   39   C  CG  . ASP A 1 5   ? 9.24400   42.62200  11.38000 1.000 29.63000 ? 5   ASP A CG  1 
ATOM   40   O  OD1 . ASP A 1 5   ? 8.61600   42.15500  10.39800 1.000 28.42000 ? 5   ASP A OD1 1 
ATOM   41   O  OD2 . ASP A 1 5   ? 9.14500   43.80400  11.74700 1.000 30.29000 ? 5   ASP A OD2 1 
ATOM   42   N  N   . MET A 1 6   ? 10.64100  38.50100  13.59400 1.000 19.35000 ? 6   MET A N   1 
ATOM   43   C  CA  . MET A 1 6   ? 11.61700  37.44900  13.81500 1.000 19.99000 ? 6   MET A CA  1 
ATOM   44   C  C   . MET A 1 6   ? 11.53600  36.39800  12.71300 1.000 15.04000 ? 6   MET A C   1 
ATOM   45   O  O   . MET A 1 6   ? 10.48400  36.17100  12.10900 1.000 16.51000 ? 6   MET A O   1 
ATOM   46   C  CB  . MET A 1 6   ? 11.39500  36.79200  15.17700 1.000 17.79000 ? 6   MET A CB  1 
ATOM   47   C  CG  . MET A 1 6   ? 11.93200  37.62600  16.34300 1.000 17.81000 ? 6   MET A CG  1 
ATOM   48   S  SD  . MET A 1 6   ? 11.83000  36.71100  17.89700 1.000 32.47000 ? 6   MET A SD  1 
ATOM   49   C  CE  . MET A 1 6   ? 10.09000  36.53300  17.96900 1.000 13.23000 ? 6   MET A CE  1 
ATOM   50   N  N   . VAL A 1 7   ? 12.67300  35.77200  12.44000 1.000 14.72000 ? 7   VAL A N   1 
ATOM   51   C  CA  . VAL A 1 7   ? 12.74300  34.57000  11.62100 1.000 13.39000 ? 7   VAL A CA  1 
ATOM   52   C  C   . VAL A 1 7   ? 13.24600  33.45100  12.51800 1.000 17.09000 ? 7   VAL A C   1 
ATOM   53   O  O   . VAL A 1 7   ? 14.29700  33.59000  13.15500 1.000 15.46000 ? 7   VAL A O   1 
ATOM   54   C  CB  . VAL A 1 7   ? 13.66400  34.74500  10.39900 1.000 14.78000 ? 7   VAL A CB  1 
ATOM   55   C  CG1 . VAL A 1 7   ? 13.82600  33.42400  9.70400  1.000 14.27000 ? 7   VAL A CG1 1 
ATOM   56   C  CG2 . VAL A 1 7   ? 13.09400  35.79900  9.43800  1.000 15.25000 ? 7   VAL A CG2 1 
ATOM   57   N  N   . MET A 1 8   ? 12.50100  32.34800  12.57800 1.000 14.89000 ? 8   MET A N   1 
ATOM   58   C  CA  . MET A 1 8   ? 12.77400  31.30100  13.55800 1.000 15.16000 ? 8   MET A CA  1 
ATOM   59   C  C   . MET A 1 8   ? 12.99700  29.96700  12.86000 1.000 15.72000 ? 8   MET A C   1 
ATOM   60   O  O   . MET A 1 8   ? 12.08500  29.43700  12.22200 1.000 16.73000 ? 8   MET A O   1 
ATOM   61   C  CB  . MET A 1 8   ? 11.63400  31.20300  14.57700 1.000 14.79000 ? 8   MET A CB  1 
ATOM   62   C  CG  . MET A 1 8   ? 11.37300  32.51600  15.32300 1.000 14.68000 ? 8   MET A CG  1 
ATOM   63   S  SD  . MET A 1 8   ? 10.14300  32.33400  16.62900 1.000 16.69000 ? 8   MET A SD  1 
ATOM   64   C  CE  . MET A 1 8   ? 11.13100  31.59900  17.93400 1.000 13.71000 ? 8   MET A CE  1 
ATOM   65   N  N   . ILE A 1 9   ? 14.21300  29.43700  12.98000 1.000 15.35000 ? 9   ILE A N   1 
ATOM   66   C  CA  . ILE A 1 9   ? 14.54500  28.07100  12.58900 1.000 14.24000 ? 9   ILE A CA  1 
ATOM   67   C  C   . ILE A 1 9   ? 14.74200  27.26200  13.85500 1.000 14.19000 ? 9   ILE A C   1 
ATOM   68   O  O   . ILE A 1 9   ? 15.42100  27.71700  14.78400 1.000 16.33000 ? 9   ILE A O   1 
ATOM   69   C  CB  . ILE A 1 9   ? 15.81600  28.01300  11.72500 1.000 16.11000 ? 9   ILE A CB  1 
ATOM   70   C  CG1 . ILE A 1 9   ? 15.58200  28.67400  10.37200 1.000 16.07000 ? 9   ILE A CG1 1 
ATOM   71   C  CG2 . ILE A 1 9   ? 16.29300  26.56200  11.55000 1.000 15.43000 ? 9   ILE A CG2 1 
ATOM   72   C  CD1 . ILE A 1 9   ? 16.87500  28.85800  9.60400  1.000 19.48000 ? 9   ILE A CD1 1 
ATOM   73   N  N   . SER A 1 10  ? 14.15200  26.06800  13.89400 1.000 14.07000 ? 10  SER A N   1 
ATOM   74   C  CA  . SER A 1 10  ? 14.29000  25.16200  15.02800 1.000 13.05000 ? 10  SER A CA  1 
ATOM   75   C  C   . SER A 1 10  ? 15.24100  24.04800  14.61200 1.000 13.04000 ? 10  SER A C   1 
ATOM   76   O  O   . SER A 1 10  ? 15.01400  23.40200  13.58800 1.000 14.06000 ? 10  SER A O   1 
ATOM   77   C  CB  . SER A 1 10  ? 12.92100  24.60100  15.43800 1.000 12.78000 ? 10  SER A CB  1 
ATOM   78   O  OG  . SER A 1 10  ? 13.06600  23.48900  16.31000 1.000 12.14000 ? 10  SER A OG  1 
ATOM   79   N  N   . ILE A 1 11  ? 16.32100  23.84000  15.36700 1.000 11.22000 ? 11  ILE A N   1 
ATOM   80   C  CA  . ILE A 1 11  ? 17.25800  22.76200  15.02200 1.000 13.61000 ? 11  ILE A CA  1 
ATOM   81   C  C   . ILE A 1 11  ? 17.02700  21.51700  15.88900 1.000 13.89000 ? 11  ILE A C   1 
ATOM   82   O  O   . ILE A 1 11  ? 17.90100  20.66200  15.98800 1.000 14.43000 ? 11  ILE A O   1 
ATOM   83   C  CB  . ILE A 1 11  ? 18.73000  23.21700  15.05600 1.000 18.38000 ? 11  ILE A CB  1 
ATOM   84   C  CG1 . ILE A 1 11  ? 18.99200  24.19000  16.19800 1.000 17.48000 ? 11  ILE A CG1 1 
ATOM   85   C  CG2 . ILE A 1 11  ? 19.15500  23.82100  13.69400 1.000 20.30000 ? 11  ILE A CG2 1 
ATOM   86   C  CD1 . ILE A 1 11  ? 18.97400  23.52600  17.52600 1.000 15.53000 ? 11  ILE A CD1 1 
ATOM   87   N  N   . ASP A 1 12  ? 15.83900  21.38500  16.48600 1.000 11.07000 ? 12  ASP A N   1 
ATOM   88   C  CA  . ASP A 1 12  ? 15.50100  20.15200  17.18700 1.000 13.67000 ? 12  ASP A CA  1 
ATOM   89   C  C   . ASP A 1 12  ? 13.98300  20.06500  17.26400 1.000 13.95000 ? 12  ASP A C   1 
ATOM   90   O  O   . ASP A 1 12  ? 13.35800  20.80900  18.02700 1.000 13.32000 ? 12  ASP A O   1 
ATOM   91   C  CB  . ASP A 1 12  ? 16.13600  20.13100  18.57700 1.000 11.07000 ? 12  ASP A CB  1 
ATOM   92   C  CG  . ASP A 1 12  ? 15.60100  19.01000  19.45600 1.000 12.32000 ? 12  ASP A CG  1 
ATOM   93   O  OD1 . ASP A 1 12  ? 15.07700  18.01000  18.91800 1.000 12.68000 ? 12  ASP A OD1 1 
ATOM   94   O  OD2 . ASP A 1 12  ? 15.72900  19.11900  20.69600 1.000 12.94000 ? 12  ASP A OD2 1 
ATOM   95   N  N   . ASP A 1 13  ? 13.40400  19.17500  16.46500 1.000 14.16000 ? 13  ASP A N   1 
ATOM   96   C  CA  . ASP A 1 13  ? 12.01400  18.76500  16.60300 1.000 13.34000 ? 13  ASP A CA  1 
ATOM   97   C  C   . ASP A 1 13  ? 11.97100  17.25600  16.44900 1.000 14.00000 ? 13  ASP A C   1 
ATOM   98   O  O   . ASP A 1 13  ? 12.99500  16.61100  16.22600 1.000 14.34000 ? 13  ASP A O   1 
ATOM   99   C  CB  . ASP A 1 13  ? 11.12600  19.47000  15.57600 1.000 10.55000 ? 13  ASP A CB  1 
ATOM   100  C  CG  . ASP A 1 13  ? 11.23000  20.96900  15.67900 1.000 16.22000 ? 13  ASP A CG  1 
ATOM   101  O  OD1 . ASP A 1 13  ? 12.17200  21.53300  15.07600 1.000 15.40000 ? 13  ASP A OD1 1 
ATOM   102  O  OD2 . ASP A 1 13  ? 10.41000  21.57700  16.39900 1.000 14.98000 ? 13  ASP A OD2 1 
ATOM   103  N  N   . HIS A 1 14  ? 10.78000  16.69100  16.53600 1.000 12.78000 ? 14  HIS A N   1 
ATOM   104  C  CA  . HIS A 1 14  ? 10.61400  15.25100  16.49100 1.000 13.46000 ? 14  HIS A CA  1 
ATOM   105  C  C   . HIS A 1 14  ? 9.47500   14.90300  15.54300 1.000 15.90000 ? 14  HIS A C   1 
ATOM   106  O  O   . HIS A 1 14  ? 8.53600   15.67800  15.36000 1.000 13.43000 ? 14  HIS A O   1 
ATOM   107  C  CB  . HIS A 1 14  ? 10.37500  14.70800  17.90200 1.000 13.33000 ? 14  HIS A CB  1 
ATOM   108  C  CG  . HIS A 1 14  ? 11.53800  14.93000  18.81800 1.000 14.76000 ? 14  HIS A CG  1 
ATOM   109  N  ND1 . HIS A 1 14  ? 12.51400  13.98300  19.01600 1.000 14.45000 ? 14  HIS A ND1 1 
ATOM   110  C  CD2 . HIS A 1 14  ? 11.89700  16.00200  19.56200 1.000 14.71000 ? 14  HIS A CD2 1 
ATOM   111  C  CE1 . HIS A 1 14  ? 13.41700  14.45000  19.85900 1.000 17.10000 ? 14  HIS A CE1 1 
ATOM   112  N  NE2 . HIS A 1 14  ? 13.07000  15.67800  20.20000 1.000 16.22000 ? 14  HIS A NE2 1 
ATOM   113  N  N   . VAL A 1 15  ? 9.59200   13.75600  14.89000 1.000 14.61000 ? 15  VAL A N   1 
ATOM   114  C  CA  . VAL A 1 15  ? 8.56900   13.31500  13.95600 1.000 15.02000 ? 15  VAL A CA  1 
ATOM   115  C  C   . VAL A 1 15  ? 8.10700   11.92200  14.35300 1.000 18.72000 ? 15  VAL A C   1 
ATOM   116  O  O   . VAL A 1 15  ? 8.90300   11.08800  14.79700 1.000 17.48000 ? 15  VAL A O   1 
ATOM   117  C  CB  . VAL A 1 15  ? 9.07600   13.34700  12.49700 1.000 17.73000 ? 15  VAL A CB  1 
ATOM   118  C  CG1 . VAL A 1 15  ? 10.24900  12.39700  12.30300 1.000 15.65000 ? 15  VAL A CG1 1 
ATOM   119  C  CG2 . VAL A 1 15  ? 7.93800   13.02300  11.51400 1.000 19.79000 ? 15  VAL A CG2 1 
ATOM   120  N  N   . VAL A 1 16  ? 6.81000   11.69000  14.23000 1.000 15.11000 ? 16  VAL A N   1 
ATOM   121  C  CA  . VAL A 1 16  ? 6.23100   10.36300  14.35300 1.000 15.43000 ? 16  VAL A CA  1 
ATOM   122  C  C   . VAL A 1 16  ? 6.04400   9.84100   12.93800 1.000 15.69000 ? 16  VAL A C   1 
ATOM   123  O  O   . VAL A 1 16  ? 5.30200   10.43200  12.14600 1.000 17.76000 ? 16  VAL A O   1 
ATOM   124  C  CB  . VAL A 1 16  ? 4.90500   10.40200  15.12800 1.000 18.73000 ? 16  VAL A CB  1 
ATOM   125  C  CG1 . VAL A 1 16  ? 4.23900   9.02200   15.11000 1.000 16.63000 ? 16  VAL A CG1 1 
ATOM   126  C  CG2 . VAL A 1 16  ? 5.16600   10.87500  16.55900 1.000 18.00000 ? 16  VAL A CG2 1 
ATOM   127  N  N   . GLU A 1 17  ? 6.73400   8.75600   12.60400 1.000 12.14000 ? 17  GLU A N   1 
ATOM   128  C  CA  . GLU A 1 17  ? 6.73500   8.30400   11.22200 1.000 17.18000 ? 17  GLU A CA  1 
ATOM   129  C  C   . GLU A 1 17  ? 5.34000   7.80800   10.85900 1.000 14.88000 ? 17  GLU A C   1 
ATOM   130  O  O   . GLU A 1 17  ? 4.69900   7.13500   11.66900 1.000 17.25000 ? 17  GLU A O   1 
ATOM   131  C  CB  . GLU A 1 17  ? 7.76700   7.19300   11.00800 1.000 13.97000 ? 17  GLU A CB  1 
ATOM   132  C  CG  . GLU A 1 17  ? 9.22600   7.64000   11.26800 1.000 17.69000 ? 17  GLU A CG  1 
ATOM   133  C  CD  . GLU A 1 17  ? 9.60300   7.57300   12.73900 1.000 19.86000 ? 17  GLU A CD  1 
ATOM   134  O  OE1 . GLU A 1 17  ? 8.80200   7.02500   13.53600 1.000 16.68000 ? 17  GLU A OE1 1 
ATOM   135  O  OE2 . GLU A 1 17  ? 10.70300  8.04400   13.10100 1.000 16.59000 ? 17  GLU A OE2 1 
ATOM   136  N  N   . PRO A 1 18  ? 4.84400   8.13400   9.67000  1.000 18.27000 ? 18  PRO A N   1 
ATOM   137  C  CA  . PRO A 1 18  ? 3.48900   7.72800   9.28800  1.000 16.75000 ? 18  PRO A CA  1 
ATOM   138  C  C   . PRO A 1 18  ? 3.43900   6.24600   8.94700  1.000 23.25000 ? 18  PRO A C   1 
ATOM   139  O  O   . PRO A 1 18  ? 4.46000   5.56400   8.82900  1.000 21.16000 ? 18  PRO A O   1 
ATOM   140  C  CB  . PRO A 1 18  ? 3.20000   8.58800   8.06000  1.000 18.88000 ? 18  PRO A CB  1 
ATOM   141  C  CG  . PRO A 1 18  ? 4.54900   8.74700   7.42200  1.000 20.67000 ? 18  PRO A CG  1 
ATOM   142  C  CD  . PRO A 1 18  ? 5.52300   8.86200   8.58500  1.000 18.60000 ? 18  PRO A CD  1 
ATOM   143  N  N   . ALA A 1 19  ? 2.20700   5.76000   8.76400  1.000 20.20000 ? 19  ALA A N   1 
ATOM   144  C  CA  . ALA A 1 19  ? 1.96600   4.32500   8.72200  1.000 18.54000 ? 19  ALA A CA  1 
ATOM   145  C  C   . ALA A 1 19  ? 2.52600   3.65900   7.47100  1.000 20.04000 ? 19  ALA A C   1 
ATOM   146  O  O   . ALA A 1 19  ? 2.76700   2.44500   7.49400  1.000 22.72000 ? 19  ALA A O   1 
ATOM   147  C  CB  . ALA A 1 19  ? 0.46800   4.05100   8.82500  1.000 23.08000 ? 19  ALA A CB  1 
ATOM   148  N  N   . ASP A 1 20  ? 2.75700   4.41500   6.39700  1.000 22.42000 ? 20  ASP A N   1 
ATOM   149  C  CA  . ASP A 1 20  ? 3.15600   3.84200   5.11800  1.000 26.01000 ? 20  ASP A CA  1 
ATOM   150  C  C   . ASP A 1 20  ? 4.64700   3.97900   4.83200  1.000 22.95000 ? 20  ASP A C   1 
ATOM   151  O  O   . ASP A 1 20  ? 5.07800   3.66700   3.71700  1.000 21.13000 ? 20  ASP A O   1 
ATOM   152  C  CB  . ASP A 1 20  ? 2.35100   4.47300   3.98000  1.000 20.41000 ? 20  ASP A CB  1 
ATOM   153  C  CG  . ASP A 1 20  ? 2.53000   5.97900   3.88900  1.000 27.09000 ? 20  ASP A CG  1 
ATOM   154  O  OD1 . ASP A 1 20  ? 3.18600   6.57500   4.77200  1.000 26.28000 ? 20  ASP A OD1 1 
ATOM   155  O  OD2 . ASP A 1 20  ? 1.99700   6.57700   2.93000  1.000 31.69000 ? 20  ASP A OD2 1 
ATOM   156  N  N   . ILE A 1 21  ? 5.45100   4.40200   5.81100  1.000 19.31000 ? 21  ILE A N   1 
ATOM   157  C  CA  . ILE A 1 21  ? 6.84600   4.73100   5.51000  1.000 17.16000 ? 21  ILE A CA  1 
ATOM   158  C  C   . ILE A 1 21  ? 7.60600   3.49900   5.01900  1.000 19.12000 ? 21  ILE A C   1 
ATOM   159  O  O   . ILE A 1 21  ? 8.40700   3.57900   4.08100  1.000 18.71000 ? 21  ILE A O   1 
ATOM   160  C  CB  . ILE A 1 21  ? 7.52600   5.37500   6.73400  1.000 16.71000 ? 21  ILE A CB  1 
ATOM   161  C  CG1 . ILE A 1 21  ? 8.98800   5.68800   6.42500  1.000 16.97000 ? 21  ILE A CG1 1 
ATOM   162  C  CG2 . ILE A 1 21  ? 7.44500   4.47700   7.97400  1.000 20.61000 ? 21  ILE A CG2 1 
ATOM   163  C  CD1 . ILE A 1 21  ? 9.71100   6.32400   7.58100  1.000 18.50000 ? 21  ILE A CD1 1 
ATOM   164  N  N   . PHE A 1 22  ? 7.36200   2.34400   5.62000  1.000 19.80000 ? 22  PHE A N   1 
ATOM   165  C  CA  . PHE A 1 22  ? 8.09700   1.16800   5.17500  1.000 23.49000 ? 22  PHE A CA  1 
ATOM   166  C  C   . PHE A 1 22  ? 7.43300   0.48400   3.98400  1.000 21.42000 ? 22  PHE A C   1 
ATOM   167  O  O   . PHE A 1 22  ? 8.13900   -0.08000  3.14200  1.000 19.42000 ? 22  PHE A O   1 
ATOM   168  C  CB  . PHE A 1 22  ? 8.30200   0.20900   6.34900  1.000 21.01000 ? 22  PHE A CB  1 
ATOM   169  C  CG  . PHE A 1 22  ? 9.10100   0.81900   7.46100  1.000 19.12000 ? 22  PHE A CG  1 
ATOM   170  C  CD1 . PHE A 1 22  ? 10.41500  1.20600   7.24400  1.000 19.32000 ? 22  PHE A CD1 1 
ATOM   171  C  CD2 . PHE A 1 22  ? 8.53200   1.06300   8.70100  1.000 21.30000 ? 22  PHE A CD2 1 
ATOM   172  C  CE1 . PHE A 1 22  ? 11.15700  1.79700   8.25000  1.000 21.93000 ? 22  PHE A CE1 1 
ATOM   173  C  CE2 . PHE A 1 22  ? 9.27600   1.65600   9.72100  1.000 20.86000 ? 22  PHE A CE2 1 
ATOM   174  C  CZ  . PHE A 1 22  ? 10.59400  2.02400   9.48700  1.000 21.34000 ? 22  PHE A CZ  1 
ATOM   175  N  N   . GLU A 1 23  ? 6.10500   0.56300   3.85800  1.000 20.85000 ? 23  GLU A N   1 
ATOM   176  C  CA  . GLU A 1 23  ? 5.47300   0.19400   2.59500  1.000 21.58000 ? 23  GLU A CA  1 
ATOM   177  C  C   . GLU A 1 23  ? 6.10200   0.94200   1.42900  1.000 23.86000 ? 23  GLU A C   1 
ATOM   178  O  O   . GLU A 1 23  ? 6.27600   0.38200   0.34200  1.000 23.04000 ? 23  GLU A O   1 
ATOM   179  C  CB  . GLU A 1 23  ? 3.97100   0.48000   2.63900  1.000 19.76000 ? 23  GLU A CB  1 
ATOM   180  C  CG  . GLU A 1 23  ? 3.18600   -0.48700  3.47600  1.000 24.27000 ? 23  GLU A CG  1 
ATOM   181  C  CD  . GLU A 1 23  ? 1.85000   0.08700   3.93100  1.000 31.10000 ? 23  GLU A CD  1 
ATOM   182  O  OE1 . GLU A 1 23  ? 1.54500   1.24100   3.54500  1.000 34.27000 ? 23  GLU A OE1 1 
ATOM   183  O  OE2 . GLU A 1 23  ? 1.12100   -0.61200  4.68100  1.000 32.36000 ? 23  GLU A OE2 1 
ATOM   184  N  N   . LYS A 1 24  ? 6.46900   2.20700   1.63800  1.000 19.62000 ? 24  LYS A N   1 
ATOM   185  C  CA  . LYS A 1 24  ? 6.99900   3.01600   0.54800  1.000 19.45000 ? 24  LYS A CA  1 
ATOM   186  C  C   . LYS A 1 24  ? 8.49600   2.85400   0.34400  1.000 21.36000 ? 24  LYS A C   1 
ATOM   187  O  O   . LYS A 1 24  ? 8.97700   3.05800   -0.77300 1.000 23.84000 ? 24  LYS A O   1 
ATOM   188  C  CB  . LYS A 1 24  ? 6.70500   4.50300   0.78100  1.000 22.54000 ? 24  LYS A CB  1 
ATOM   189  C  CG  . LYS A 1 24  ? 5.25600   4.88800   0.60600  1.000 27.14000 ? 24  LYS A CG  1 
ATOM   190  C  CD  . LYS A 1 24  ? 4.91600   6.14900   1.40500  1.000 27.36000 ? 24  LYS A CD  1 
ATOM   191  C  CE  . LYS A 1 24  ? 5.54000   7.40600   0.80400  1.000 31.23000 ? 24  LYS A CE  1 
ATOM   192  N  NZ  . LYS A 1 24  ? 4.93700   8.65400   1.38900  1.000 29.16000 ? 24  LYS A NZ  1 
ATOM   193  N  N   . HIS A 1 25  ? 9.25800   2.52600   1.38700  1.000 18.65000 ? 25  HIS A N   1 
ATOM   194  C  CA  . HIS A 1 25  ? 10.70800  2.64700   1.30000  1.000 21.25000 ? 25  HIS A CA  1 
ATOM   195  C  C   . HIS A 1 25  ? 11.48500  1.39500   1.69300  1.000 18.65000 ? 25  HIS A C   1 
ATOM   196  O  O   . HIS A 1 25  ? 12.67300  1.30700   1.35000  1.000 20.15000 ? 25  HIS A O   1 
ATOM   197  C  CB  . HIS A 1 25  ? 11.18700  3.83900   2.15200  1.000 17.17000 ? 25  HIS A CB  1 
ATOM   198  C  CG  . HIS A 1 25  ? 10.72500  5.16700   1.62900  1.000 21.15000 ? 25  HIS A CG  1 
ATOM   199  N  ND1 . HIS A 1 25  ? 11.24500  5.73300   0.48500  1.000 20.09000 ? 25  HIS A ND1 1 
ATOM   200  C  CD2 . HIS A 1 25  ? 9.77300   6.02400   2.07100  1.000 19.38000 ? 25  HIS A CD2 1 
ATOM   201  C  CE1 . HIS A 1 25  ? 10.64600  6.88700   0.25200  1.000 20.04000 ? 25  HIS A CE1 1 
ATOM   202  N  NE2 . HIS A 1 25  ? 9.75000   7.08900   1.20100  1.000 18.74000 ? 25  HIS A NE2 1 
ATOM   203  N  N   . PHE A 1 26  ? 10.87400  0.42900   2.37500  1.000 17.72000 ? 26  PHE A N   1 
ATOM   204  C  CA  . PHE A 1 26  ? 11.56900  -0.82100  2.66100  1.000 17.75000 ? 26  PHE A CA  1 
ATOM   205  C  C   . PHE A 1 26  ? 11.78900  -1.61200  1.37000  1.000 20.95000 ? 26  PHE A C   1 
ATOM   206  O  O   . PHE A 1 26  ? 10.99000  -1.52200  0.43500  1.000 20.36000 ? 26  PHE A O   1 
ATOM   207  C  CB  . PHE A 1 26  ? 10.76800  -1.65000  3.64900  1.000 20.07000 ? 26  PHE A CB  1 
ATOM   208  C  CG  . PHE A 1 26  ? 11.60300  -2.42900  4.61500  1.000 18.18000 ? 26  PHE A CG  1 
ATOM   209  C  CD1 . PHE A 1 26  ? 12.34600  -1.78500  5.59300  1.000 19.04000 ? 26  PHE A CD1 1 
ATOM   210  C  CD2 . PHE A 1 26  ? 11.62400  -3.81700  4.56000  1.000 16.25000 ? 26  PHE A CD2 1 
ATOM   211  C  CE1 . PHE A 1 26  ? 13.10600  -2.51800  6.50300  1.000 15.36000 ? 26  PHE A CE1 1 
ATOM   212  C  CE2 . PHE A 1 26  ? 12.37200  -4.55600  5.46000  1.000 19.60000 ? 26  PHE A CE2 1 
ATOM   213  C  CZ  . PHE A 1 26  ? 13.12100  -3.90400  6.44000  1.000 21.33000 ? 26  PHE A CZ  1 
ATOM   214  N  N   . PRO A 1 27  ? 12.88300  -2.37300  1.27700  1.000 18.58000 ? 27  PRO A N   1 
ATOM   215  C  CA  . PRO A 1 27  ? 13.10300  -3.18500  0.07200  1.000 17.94000 ? 27  PRO A CA  1 
ATOM   216  C  C   . PRO A 1 27  ? 11.98700  -4.20300  -0.12200 1.000 19.94000 ? 27  PRO A C   1 
ATOM   217  O  O   . PRO A 1 27  ? 11.56000  -4.87300  0.82100  1.000 16.58000 ? 27  PRO A O   1 
ATOM   218  C  CB  . PRO A 1 27  ? 14.44300  -3.86900  0.34500  1.000 18.19000 ? 27  PRO A CB  1 
ATOM   219  C  CG  . PRO A 1 27  ? 15.15500  -2.93100  1.30100  1.000 20.45000 ? 27  PRO A CG  1 
ATOM   220  C  CD  . PRO A 1 27  ? 14.04400  -2.39800  2.18400  1.000 17.33000 ? 27  PRO A CD  1 
ATOM   221  N  N   . LYS A 1 28  ? 11.51900  -4.31200  -1.36600 1.000 22.41000 ? 28  LYS A N   1 
ATOM   222  C  CA  . LYS A 1 28  ? 10.38900  -5.19000  -1.65700 1.000 20.26000 ? 28  LYS A CA  1 
ATOM   223  C  C   . LYS A 1 28  ? 10.70400  -6.63300  -1.29800 1.000 23.49000 ? 28  LYS A C   1 
ATOM   224  O  O   . LYS A 1 28  ? 9.85500   -7.34000  -0.74500 1.000 23.03000 ? 28  LYS A O   1 
ATOM   225  C  CB  . LYS A 1 28  ? 9.99600   -5.06400  -3.12900 1.000 24.10000 ? 28  LYS A CB  1 
ATOM   226  C  CG  . LYS A 1 28  ? 8.75400   -5.85700  -3.50700 1.000 38.23000 ? 28  LYS A CG  1 
ATOM   227  C  CD  . LYS A 1 28  ? 8.43600   -5.74200  -5.00000 1.000 41.48000 ? 28  LYS A CD  1 
ATOM   228  C  CE  . LYS A 1 28  ? 9.09100   -6.86400  -5.79800 1.000 47.94000 ? 28  LYS A CE  1 
ATOM   229  N  NZ  . LYS A 1 28  ? 8.33200   -7.19900  -7.03800 1.000 56.93000 ? 28  LYS A NZ  1 
ATOM   230  N  N   . SER A 1 29  ? 11.93600  -7.07800  -1.55300 1.000 21.76000 ? 29  SER A N   1 
ATOM   231  C  CA  . SER A 1 29  ? 12.27200  -8.47100  -1.28000 1.000 24.32000 ? 29  SER A CA  1 
ATOM   232  C  C   . SER A 1 29  ? 12.31900  -8.78300  0.20700  1.000 26.33000 ? 29  SER A C   1 
ATOM   233  O  O   . SER A 1 29  ? 12.35900  -9.96400  0.56900  1.000 25.26000 ? 29  SER A O   1 
ATOM   234  C  CB  . SER A 1 29  ? 13.61000  -8.83500  -1.92900 1.000 26.08000 ? 29  SER A CB  1 
ATOM   235  O  OG  . SER A 1 29  ? 14.69200  -8.12500  -1.34600 1.000 24.12000 ? 29  SER A OG  1 
ATOM   236  N  N   . LEU A 1 30  ? 12.30700  -7.76400  1.06900  1.000 23.26000 ? 30  LEU A N   1 
ATOM   237  C  CA  . LEU A 1 30  ? 12.35100  -7.94600  2.51500  1.000 21.38000 ? 30  LEU A CA  1 
ATOM   238  C  C   . LEU A 1 30  ? 11.03400  -7.57600  3.18100  1.000 23.57000 ? 30  LEU A C   1 
ATOM   239  O  O   . LEU A 1 30  ? 10.97700  -7.50500  4.41400  1.000 23.22000 ? 30  LEU A O   1 
ATOM   240  C  CB  . LEU A 1 30  ? 13.47800  -7.10300  3.13000  1.000 17.15000 ? 30  LEU A CB  1 
ATOM   241  C  CG  . LEU A 1 30  ? 14.91000  -7.35500  2.64100  1.000 22.42000 ? 30  LEU A CG  1 
ATOM   242  C  CD1 . LEU A 1 30  ? 15.88600  -6.40200  3.31000  1.000 20.61000 ? 30  LEU A CD1 1 
ATOM   243  C  CD2 . LEU A 1 30  ? 15.30800  -8.78100  2.93100  1.000 19.26000 ? 30  LEU A CD2 1 
ATOM   244  N  N   . MET A 1 31  ? 9.98200   -7.31900  2.39800  1.000 21.72000 ? 31  MET A N   1 
ATOM   245  C  CA  . MET A 1 31  ? 8.81200   -6.63900  2.94800  1.000 24.22000 ? 31  MET A CA  1 
ATOM   246  C  C   . MET A 1 31  ? 8.12100   -7.47000  4.01600  1.000 25.68000 ? 31  MET A C   1 
ATOM   247  O  O   . MET A 1 31  ? 7.61300   -6.91600  4.99700  1.000 24.46000 ? 31  MET A O   1 
ATOM   248  C  CB  . MET A 1 31  ? 7.81700   -6.26800  1.85300  1.000 21.30000 ? 31  MET A CB  1 
ATOM   249  C  CG  . MET A 1 31  ? 6.70100   -5.35200  2.36800  1.000 24.47000 ? 31  MET A CG  1 
ATOM   250  S  SD  . MET A 1 31  ? 7.30500   -3.72400  2.90700  1.000 24.98000 ? 31  MET A SD  1 
ATOM   251  C  CE  . MET A 1 31  ? 7.85300   -3.07500  1.35000  1.000 18.34000 ? 31  MET A CE  1 
ATOM   252  N  N   . ASP A 1 32  ? 8.10200   -8.79700  3.86400  1.000 25.70000 ? 32  ASP A N   1 
ATOM   253  C  CA  . ASP A 1 32  ? 7.44200   -9.58900  4.89400  1.000 26.58000 ? 32  ASP A CA  1 
ATOM   254  C  C   . ASP A 1 32  ? 8.19500   -9.56300  6.21400  1.000 27.27000 ? 32  ASP A C   1 
ATOM   255  O  O   . ASP A 1 32  ? 7.66900   -10.05900 7.21200  1.000 29.26000 ? 32  ASP A O   1 
ATOM   256  C  CB  . ASP A 1 32  ? 7.22000   -11.03600 4.43400  1.000 28.89000 ? 32  ASP A CB  1 
ATOM   257  C  CG  . ASP A 1 32  ? 8.48200   -11.71100 3.94100  1.000 40.58000 ? 32  ASP A CG  1 
ATOM   258  O  OD1 . ASP A 1 32  ? 9.59600   -11.38200 4.40800  1.000 38.29000 ? 32  ASP A OD1 1 
ATOM   259  O  OD2 . ASP A 1 32  ? 8.34900   -12.59700 3.06900  1.000 51.12000 ? 32  ASP A OD2 1 
ATOM   260  N  N   . GLN A 1 33  ? 9.39200   -8.97300  6.25200  1.000 23.59000 ? 33  GLN A N   1 
ATOM   261  C  CA  . GLN A 1 33  ? 10.12100  -8.77700  7.50000  1.000 19.58000 ? 33  GLN A CA  1 
ATOM   262  C  C   . GLN A 1 33  ? 10.19000  -7.31000  7.90800  1.000 19.60000 ? 33  GLN A C   1 
ATOM   263  O  O   . GLN A 1 33  ? 10.90600  -6.97100  8.86000  1.000 19.30000 ? 33  GLN A O   1 
ATOM   264  C  CB  . GLN A 1 33  ? 11.53400  -9.34600  7.38400  1.000 22.54000 ? 33  GLN A CB  1 
ATOM   265  C  CG  . GLN A 1 33  ? 11.59200  -10.77200 6.86800  1.000 28.39000 ? 33  GLN A CG  1 
ATOM   266  C  CD  . GLN A 1 33  ? 13.01600  -11.21600 6.62200  1.000 32.35000 ? 33  GLN A CD  1 
ATOM   267  O  OE1 . GLN A 1 33  ? 13.69500  -11.69000 7.53700  1.000 40.23000 ? 33  GLN A OE1 1 
ATOM   268  N  NE2 . GLN A 1 33  ? 13.49000  -11.04100 5.38900  1.000 29.58000 ? 33  GLN A NE2 1 
ATOM   269  N  N   . ALA A 1 34  ? 9.50000   -6.43200  7.18800  1.000 19.81000 ? 34  ALA A N   1 
ATOM   270  C  CA  . ALA A 1 34  ? 9.52400   -5.01000  7.49200  1.000 19.09000 ? 34  ALA A CA  1 
ATOM   271  C  C   . ALA A 1 34  ? 8.88500   -4.74200  8.85200  1.000 23.19000 ? 34  ALA A C   1 
ATOM   272  O  O   . ALA A 1 34  ? 8.07700   -5.53900  9.34200  1.000 20.04000 ? 34  ALA A O   1 
ATOM   273  C  CB  . ALA A 1 34  ? 8.76900   -4.22800  6.41300  1.000 20.14000 ? 34  ALA A CB  1 
ATOM   274  N  N   . PRO A 1 35  ? 9.21600   -3.61300  9.47300  1.000 20.18000 ? 35  PRO A N   1 
ATOM   275  C  CA  . PRO A 1 35  ? 8.41200   -3.16000  10.61100 1.000 16.21000 ? 35  PRO A CA  1 
ATOM   276  C  C   . PRO A 1 35  ? 6.95000   -3.06100  10.19300 1.000 17.51000 ? 35  PRO A C   1 
ATOM   277  O  O   . PRO A 1 35  ? 6.63400   -2.55300  9.11600  1.000 20.29000 ? 35  PRO A O   1 
ATOM   278  C  CB  . PRO A 1 35  ? 9.01200   -1.78600  10.94600 1.000 19.17000 ? 35  PRO A CB  1 
ATOM   279  C  CG  . PRO A 1 35  ? 10.39600  -1.79900  10.33500 1.000 16.04000 ? 35  PRO A CG  1 
ATOM   280  C  CD  . PRO A 1 35  ? 10.24800  -2.62600  9.09100  1.000 16.02000 ? 35  PRO A CD  1 
ATOM   281  N  N   . LYS A 1 36  ? 6.05400   -3.57700  11.04500 1.000 20.34000 ? 36  LYS A N   1 
ATOM   282  C  CA  . LYS A 1 36  ? 4.61800   -3.55400  10.78100 1.000 22.01000 ? 36  LYS A CA  1 
ATOM   283  C  C   . LYS A 1 36  ? 3.87100   -3.03600  12.00100 1.000 19.04000 ? 36  LYS A C   1 
ATOM   284  O  O   . LYS A 1 36  ? 4.25200   -3.31100  13.14100 1.000 22.40000 ? 36  LYS A O   1 
ATOM   285  C  CB  . LYS A 1 36  ? 4.05700   -4.94900  10.42900 1.000 24.57000 ? 36  LYS A CB  1 
ATOM   286  C  CG  . LYS A 1 36  ? 4.90100   -5.75500  9.44300  1.000 29.59000 ? 36  LYS A CG  1 
ATOM   287  C  CD  . LYS A 1 36  ? 4.33500   -5.70200  8.02400  1.000 31.64000 ? 36  LYS A CD  1 
ATOM   288  C  CE  . LYS A 1 36  ? 5.19300   -6.53900  7.06700  1.000 28.59000 ? 36  LYS A CE  1 
ATOM   289  N  NZ  . LYS A 1 36  ? 4.65500   -6.49400  5.67400  1.000 31.12000 ? 36  LYS A NZ  1 
ATOM   290  N  N   . LEU A 1 37  ? 2.77400   -2.32400  11.74700 1.000 19.94000 ? 37  LEU A N   1 
ATOM   291  C  CA  . LEU A 1 37  ? 1.94500   -1.79300  12.82200 1.000 20.33000 ? 37  LEU A CA  1 
ATOM   292  C  C   . LEU A 1 37  ? 1.10200   -2.89100  13.45500 1.000 26.86000 ? 37  LEU A C   1 
ATOM   293  O  O   . LEU A 1 37  ? 0.41900   -3.64400  12.75400 1.000 27.50000 ? 37  LEU A O   1 
ATOM   294  C  CB  . LEU A 1 37  ? 1.03100   -0.69000  12.29500 1.000 24.65000 ? 37  LEU A CB  1 
ATOM   295  C  CG  . LEU A 1 37  ? 1.74900   0.61700   11.95200 1.000 21.43000 ? 37  LEU A CG  1 
ATOM   296  C  CD1 . LEU A 1 37  ? 0.81300   1.50900   11.18500 1.000 26.34000 ? 37  LEU A CD1 1 
ATOM   297  C  CD2 . LEU A 1 37  ? 2.23200   1.30300   13.21600 1.000 22.86000 ? 37  LEU A CD2 1 
ATOM   298  N  N   . THR A 1 38  ? 1.14600   -2.96700  14.78000 1.000 24.18000 ? 38  THR A N   1 
ATOM   299  C  CA  . THR A 1 38  ? 0.31300   -3.87300  15.55100 1.000 26.33000 ? 38  THR A CA  1 
ATOM   300  C  C   . THR A 1 38  ? -0.19100  -3.12500  16.77500 1.000 31.97000 ? 38  THR A C   1 
ATOM   301  O  O   . THR A 1 38  ? 0.27500   -2.02700  17.08700 1.000 25.22000 ? 38  THR A O   1 
ATOM   302  C  CB  . THR A 1 38  ? 1.08000   -5.13100  15.97900 1.000 24.79000 ? 38  THR A CB  1 
ATOM   303  O  OG1 . THR A 1 38  ? 0.17500   -6.05400  16.59900 1.000 36.26000 ? 38  THR A OG1 1 
ATOM   304  C  CG2 . THR A 1 38  ? 2.15700   -4.77400  16.96000 1.000 24.50000 ? 38  THR A CG2 1 
ATOM   305  N  N   . ALA A 1 39  ? -1.14500  -3.73100  17.47700 1.000 34.54000 ? 39  ALA A N   1 
ATOM   306  C  CA  . ALA A 1 39  ? -1.62300  -3.14700  18.72200 1.000 29.05000 ? 39  ALA A CA  1 
ATOM   307  C  C   . ALA A 1 39  ? -0.54600  -3.23900  19.79000 1.000 31.26000 ? 39  ALA A C   1 
ATOM   308  O  O   . ALA A 1 39  ? 0.11900   -4.26800  19.93800 1.000 37.78000 ? 39  ALA A O   1 
ATOM   309  C  CB  . ALA A 1 39  ? -2.89800  -3.85600  19.19400 1.000 32.76000 ? 39  ALA A CB  1 
ATOM   310  N  N   . HIS A 1 40  ? -0.35400  -2.15100  20.52500 1.000 31.24000 ? 40  HIS A N   1 
ATOM   311  C  CA  . HIS A 1 40  ? 0.60900   -2.17800  21.61200 1.000 34.80000 ? 40  HIS A CA  1 
ATOM   312  C  C   . HIS A 1 40  ? 0.17900   -3.21500  22.64400 1.000 43.53000 ? 40  HIS A C   1 
ATOM   313  O  O   . HIS A 1 40  ? -1.01500  -3.32100  22.95100 1.000 37.68000 ? 40  HIS A O   1 
ATOM   314  C  CB  . HIS A 1 40  ? 0.72700   -0.80500  22.27000 1.000 32.65000 ? 40  HIS A CB  1 
ATOM   315  C  CG  . HIS A 1 40  ? 2.05100   -0.56400  22.92900 1.000 34.89000 ? 40  HIS A CG  1 
ATOM   316  N  ND1 . HIS A 1 40  ? 2.44100   -1.21600  24.07900 1.000 41.15000 ? 40  HIS A ND1 1 
ATOM   317  C  CD2 . HIS A 1 40  ? 3.06900   0.26800   22.60600 1.000 29.87000 ? 40  HIS A CD2 1 
ATOM   318  C  CE1 . HIS A 1 40  ? 3.64800   -0.80600  24.42800 1.000 35.11000 ? 40  HIS A CE1 1 
ATOM   319  N  NE2 . HIS A 1 40  ? 4.05000   0.09800   23.55400 1.000 34.79000 ? 40  HIS A NE2 1 
ATOM   320  N  N   . PRO A 1 41  ? 1.11400   -4.00400  23.18100 1.000 46.20000 ? 41  PRO A N   1 
ATOM   321  C  CA  . PRO A 1 41  ? 0.74600   -4.99600  24.20800 1.000 45.43000 ? 41  PRO A CA  1 
ATOM   322  C  C   . PRO A 1 41  ? 0.09100   -4.39800  25.43700 1.000 47.74000 ? 41  PRO A C   1 
ATOM   323  O  O   . PRO A 1 41  ? -0.58500  -5.12600  26.17700 1.000 46.49000 ? 41  PRO A O   1 
ATOM   324  C  CB  . PRO A 1 41  ? 2.08800   -5.64900  24.56400 1.000 46.85000 ? 41  PRO A CB  1 
ATOM   325  C  CG  . PRO A 1 41  ? 2.94500   -5.46100  23.35500 1.000 40.87000 ? 41  PRO A CG  1 
ATOM   326  C  CD  . PRO A 1 41  ? 2.49500   -4.18000  22.69700 1.000 46.43000 ? 41  PRO A CD  1 
ATOM   327  N  N   . ARG A 1 42  ? 0.27600   -3.10400  25.69400 1.000 46.13000 ? 42  ARG A N   1 
ATOM   328  C  CA  . ARG A 1 42  ? -0.29400  -2.45300  26.86800 1.000 53.58000 ? 42  ARG A CA  1 
ATOM   329  C  C   . ARG A 1 42  ? -1.41000  -1.48200  26.51100 1.000 47.81000 ? 42  ARG A C   1 
ATOM   330  O  O   . ARG A 1 42  ? -1.77300  -0.63600  27.33500 1.000 51.09000 ? 42  ARG A O   1 
ATOM   331  C  CB  . ARG A 1 42  ? 0.79500   -1.72600  27.65600 1.000 47.06000 ? 42  ARG A CB  1 
ATOM   332  N  N   . ASN A 1 43  ? -1.96000  -1.58900  25.30400 1.000 37.32000 ? 43  ASN A N   1 
ATOM   333  C  CA  . ASN A 1 43  ? -2.95200  -0.64100  24.83200 1.000 36.29000 ? 43  ASN A CA  1 
ATOM   334  C  C   . ASN A 1 43  ? -3.47600  -1.08900  23.47400 1.000 31.37000 ? 43  ASN A C   1 
ATOM   335  O  O   . ASN A 1 43  ? -2.96500  -0.64400  22.43900 1.000 35.30000 ? 43  ASN A O   1 
ATOM   336  C  CB  . ASN A 1 43  ? -2.34400  0.76300   24.74700 1.000 42.25000 ? 43  ASN A CB  1 
ATOM   337  C  CG  . ASN A 1 43  ? -3.30600  1.84500   25.20200 1.000 37.74000 ? 43  ASN A CG  1 
ATOM   338  O  OD1 . ASN A 1 43  ? -4.51100  1.61600   25.30000 1.000 40.75000 ? 43  ASN A OD1 1 
ATOM   339  N  ND2 . ASN A 1 43  ? -2.77400  3.03000   25.48800 1.000 40.96000 ? 43  ASN A ND2 1 
ATOM   340  N  N   . PRO A 1 44  ? -4.47600  -1.97000  23.42500 1.000 33.25000 ? 44  PRO A N   1 
ATOM   341  C  CA  . PRO A 1 44  ? -5.06200  -2.32400  22.12300 1.000 31.92000 ? 44  PRO A CA  1 
ATOM   342  C  C   . PRO A 1 44  ? -5.65300  -1.12800  21.41500 1.000 33.78000 ? 44  PRO A C   1 
ATOM   343  O  O   . PRO A 1 44  ? -5.85900  -1.18100  20.19500 1.000 31.68000 ? 44  PRO A O   1 
ATOM   344  C  CB  . PRO A 1 44  ? -6.15000  -3.35400  22.48200 1.000 30.20000 ? 44  PRO A CB  1 
ATOM   345  C  CG  . PRO A 1 44  ? -6.50300  -3.03200  23.90800 1.000 35.29000 ? 44  PRO A CG  1 
ATOM   346  C  CD  . PRO A 1 44  ? -5.19900  -2.59900  24.54600 1.000 30.99000 ? 44  PRO A CD  1 
ATOM   347  N  N   . ARG A 1 45  ? -5.87100  -0.06200  22.17900 1.000 27.91000 ? 45  ARG A N   1 
ATOM   348  C  CA  . ARG A 1 45  ? -6.42000  1.13700   21.61200 1.000 32.64000 ? 45  ARG A CA  1 
ATOM   349  C  C   . ARG A 1 45  ? -5.37600  2.00300   20.87500 1.000 25.14000 ? 45  ARG A C   1 
ATOM   350  O  O   . ARG A 1 45  ? -5.73700  2.93400   20.30200 1.000 29.63000 ? 45  ARG A O   1 
ATOM   351  C  CB  . ARG A 1 45  ? -7.23500  1.94100   22.63900 1.000 33.96000 ? 45  ARG A CB  1 
ATOM   352  C  CG  . ARG A 1 45  ? -8.63200  1.36700   22.89400 1.000 37.25000 ? 45  ARG A CG  1 
ATOM   353  C  CD  . ARG A 1 45  ? -9.65400  2.37400   23.40800 1.000 35.99000 ? 45  ARG A CD  1 
ATOM   354  N  NE  . ARG A 1 45  ? -9.05000  3.36300   24.27500 1.000 40.23000 ? 45  ARG A NE  1 
ATOM   355  C  CZ  . ARG A 1 45  ? -9.47900  4.60100   24.42600 1.000 40.18000 ? 45  ARG A CZ  1 
ATOM   356  N  NH1 . ARG A 1 45  ? -10.57300 5.01600   23.81300 1.000 35.79000 ? 45  ARG A NH1 1 
ATOM   357  N  NH2 . ARG A 1 45  ? -8.81500  5.41500   25.21500 1.000 37.42000 ? 45  ARG A NH2 1 
ATOM   358  N  N   . VAL A 1 46  ? -4.09500  1.67400   20.93000 1.000 27.38000 ? 46  VAL A N   1 
ATOM   359  C  CA  . VAL A 1 46  ? -3.09700  2.38300   20.13700 1.000 26.45000 ? 46  VAL A CA  1 
ATOM   360  C  C   . VAL A 1 46  ? -2.14100  1.45100   19.40700 1.000 28.33000 ? 46  VAL A C   1 
ATOM   361  O  O   . VAL A 1 46  ? -1.76700  0.45700   19.92500 1.000 26.09000 ? 46  VAL A O   1 
ATOM   362  C  CB  . VAL A 1 46  ? -2.24500  3.39700   20.90100 1.000 24.25000 ? 46  VAL A CB  1 
ATOM   363  C  CG1 . VAL A 1 46  ? -3.10600  4.45500   21.50000 1.000 24.20000 ? 46  VAL A CG1 1 
ATOM   364  C  CG2 . VAL A 1 46  ? -1.36200  2.72800   21.91400 1.000 28.60000 ? 46  VAL A CG2 1 
ATOM   365  N  N   . GLN A 1 47  ? -1.73200  1.83500   18.22000 1.000 26.14000 ? 47  GLN A N   1 
ATOM   366  C  CA  . GLN A 1 47  ? -0.82200  0.98300   17.47700 1.000 25.73000 ? 47  GLN A CA  1 
ATOM   367  C  C   . GLN A 1 47  ? 0.63900   1.25200   17.80100 1.000 26.35000 ? 47  GLN A C   1 
ATOM   368  O  O   . GLN A 1 47  ? 1.00700   2.29200   18.27800 1.000 22.81000 ? 47  GLN A O   1 
ATOM   369  C  CB  . GLN A 1 47  ? -1.04400  1.09000   15.96900 1.000 25.16000 ? 47  GLN A CB  1 
ATOM   370  C  CG  . GLN A 1 47  ? -2.43800  0.83100   15.44200 1.000 28.52000 ? 47  GLN A CG  1 
ATOM   371  C  CD  . GLN A 1 47  ? -2.77600  -0.64300  15.26700 1.000 33.88000 ? 47  GLN A CD  1 
ATOM   372  O  OE1 . GLN A 1 47  ? -3.35100  -1.24500  16.12900 1.000 40.67000 ? 47  GLN A OE1 1 
ATOM   373  N  NE2 . GLN A 1 47  ? -2.46500  -1.19300  14.11600 1.000 34.12000 ? 47  GLN A NE2 1 
ATOM   374  N  N   . ALA A 1 48  ? 1.45900   0.26000   17.51200 1.000 26.61000 ? 48  ALA A N   1 
ATOM   375  C  CA  . ALA A 1 48  ? 2.89800   0.39700   17.67700 1.000 21.21000 ? 48  ALA A CA  1 
ATOM   376  C  C   . ALA A 1 48  ? 3.58700   -0.41400  16.58900 1.000 20.62000 ? 48  ALA A C   1 
ATOM   377  O  O   . ALA A 1 48  ? 2.94300   -1.15000  15.83500 1.000 23.45000 ? 48  ALA A O   1 
ATOM   378  C  CB  . ALA A 1 48  ? 3.34300   -0.05300  19.07000 1.000 23.05000 ? 48  ALA A CB  1 
ATOM   379  N  N   . TRP A 1 49  ? 4.91200   -0.29800  16.52800 1.000 18.16000 ? 49  TRP A N   1 
ATOM   380  C  CA  . TRP A 1 49  ? 5.70000   -0.92800  15.47200 1.000 18.94000 ? 49  TRP A CA  1 
ATOM   381  C  C   . TRP A 1 49  ? 6.31200   -2.23100  15.97000 1.000 20.41000 ? 49  TRP A C   1 
ATOM   382  O  O   . TRP A 1 49  ? 7.05300   -2.23900  16.95500 1.000 23.92000 ? 49  TRP A O   1 
ATOM   383  C  CB  . TRP A 1 49  ? 6.81600   -0.00600  14.97700 1.000 18.79000 ? 49  TRP A CB  1 
ATOM   384  C  CG  . TRP A 1 49  ? 6.38800   1.14900   14.13700 1.000 16.72000 ? 49  TRP A CG  1 
ATOM   385  C  CD1 . TRP A 1 49  ? 6.36200   2.45700   14.50900 1.000 18.10000 ? 49  TRP A CD1 1 
ATOM   386  C  CD2 . TRP A 1 49  ? 5.96200   1.11300   12.76600 1.000 17.60000 ? 49  TRP A CD2 1 
ATOM   387  N  NE1 . TRP A 1 49  ? 5.92800   3.23700   13.46900 1.000 17.20000 ? 49  TRP A NE1 1 
ATOM   388  C  CE2 . TRP A 1 49  ? 5.68500   2.43700   12.38300 1.000 16.55000 ? 49  TRP A CE2 1 
ATOM   389  C  CE3 . TRP A 1 49  ? 5.79500   0.08900   11.82600 1.000 15.44000 ? 49  TRP A CE3 1 
ATOM   390  C  CZ2 . TRP A 1 49  ? 5.24300   2.77000   11.10300 1.000 17.38000 ? 49  TRP A CZ2 1 
ATOM   391  C  CZ3 . TRP A 1 49  ? 5.34800   0.41600   10.56200 1.000 19.81000 ? 49  TRP A CZ3 1 
ATOM   392  C  CH2 . TRP A 1 49  ? 5.07600   1.74700   10.20900 1.000 19.29000 ? 49  TRP A CH2 1 
ATOM   393  N  N   . GLN A 1 50  ? 6.03400   -3.31400  15.26100 1.000 22.70000 ? 50  GLN A N   1 
ATOM   394  C  CA  . GLN A 1 50  ? 6.60700   -4.62300  15.54200 1.000 23.41000 ? 50  GLN A CA  1 
ATOM   395  C  C   . GLN A 1 50  ? 7.72800   -4.88100  14.54400 1.000 18.98000 ? 50  GLN A C   1 
ATOM   396  O  O   . GLN A 1 50  ? 7.50200   -4.84200  13.33200 1.000 18.87000 ? 50  GLN A O   1 
ATOM   397  C  CB  . GLN A 1 50  ? 5.54300   -5.71300  15.43600 1.000 25.68000 ? 50  GLN A CB  1 
ATOM   398  C  CG  . GLN A 1 50  ? 6.02700   -7.11000  15.77700 1.000 30.16000 ? 50  GLN A CG  1 
ATOM   399  C  CD  . GLN A 1 50  ? 4.86500   -8.04600  16.07100 1.000 38.07000 ? 50  GLN A CD  1 
ATOM   400  O  OE1 . GLN A 1 50  ? 3.96500   -8.20600  15.24300 1.000 38.80000 ? 50  GLN A OE1 1 
ATOM   401  N  NE2 . GLN A 1 50  ? 4.87800   -8.66700  17.24900 1.000 48.27000 ? 50  GLN A NE2 1 
ATOM   402  N  N   . PHE A 1 51  ? 8.92100   -5.16200  15.05200 1.000 20.93000 ? 51  PHE A N   1 
ATOM   403  C  CA  . PHE A 1 51  ? 10.09500  -5.34900  14.20600 1.000 22.80000 ? 51  PHE A CA  1 
ATOM   404  C  C   . PHE A 1 51  ? 11.04400  -6.28900  14.92800 1.000 19.00000 ? 51  PHE A C   1 
ATOM   405  O  O   . PHE A 1 51  ? 11.39400  -6.04200  16.08600 1.000 21.98000 ? 51  PHE A O   1 
ATOM   406  C  CB  . PHE A 1 51  ? 10.76900  -4.00200  13.90300 1.000 17.79000 ? 51  PHE A CB  1 
ATOM   407  C  CG  . PHE A 1 51  ? 11.84000  -4.07100  12.83900 1.000 19.47000 ? 51  PHE A CG  1 
ATOM   408  C  CD1 . PHE A 1 51  ? 11.64600  -4.80900  11.67800 1.000 21.53000 ? 51  PHE A CD1 1 
ATOM   409  C  CD2 . PHE A 1 51  ? 13.03100  -3.38000  12.99000 1.000 19.37000 ? 51  PHE A CD2 1 
ATOM   410  C  CE1 . PHE A 1 51  ? 12.63300  -4.86200  10.69900 1.000 20.48000 ? 51  PHE A CE1 1 
ATOM   411  C  CE2 . PHE A 1 51  ? 14.01800  -3.43700  12.01900 1.000 18.60000 ? 51  PHE A CE2 1 
ATOM   412  C  CZ  . PHE A 1 51  ? 13.81500  -4.16700  10.87100 1.000 16.73000 ? 51  PHE A CZ  1 
ATOM   413  N  N   . GLN A 1 52  ? 11.41800  -7.38200  14.26200 1.000 21.17000 ? 52  GLN A N   1 
ATOM   414  C  CA  . GLN A 1 52  ? 12.38400  -8.34700  14.79600 1.000 19.85000 ? 52  GLN A CA  1 
ATOM   415  C  C   . GLN A 1 52  ? 12.02800  -8.80500  16.21100 1.000 20.42000 ? 52  GLN A C   1 
ATOM   416  O  O   . GLN A 1 52  ? 12.88500  -8.89600  17.09000 1.000 23.58000 ? 52  GLN A O   1 
ATOM   417  C  CB  . GLN A 1 52  ? 13.80300  -7.78200  14.76200 1.000 18.84000 ? 52  GLN A CB  1 
ATOM   418  C  CG  . GLN A 1 52  ? 14.27900  -7.35900  13.38300 1.000 18.78000 ? 52  GLN A CG  1 
ATOM   419  C  CD  . GLN A 1 52  ? 15.78400  -7.22100  13.32400 1.000 24.40000 ? 52  GLN A CD  1 
ATOM   420  O  OE1 . GLN A 1 52  ? 16.51100  -8.11500  13.75700 1.000 21.94000 ? 52  GLN A OE1 1 
ATOM   421  N  NE2 . GLN A 1 52  ? 16.26600  -6.08900  12.80000 1.000 21.41000 ? 52  GLN A NE2 1 
ATOM   422  N  N   . GLY A 1 53  ? 10.75200  -9.09200  16.43900 1.000 23.98000 ? 53  GLY A N   1 
ATOM   423  C  CA  . GLY A 1 53  ? 10.34400  -9.60700  17.73500 1.000 27.08000 ? 53  GLY A CA  1 
ATOM   424  C  C   . GLY A 1 53  ? 10.28100  -8.58700  18.84800 1.000 27.60000 ? 53  GLY A C   1 
ATOM   425  O  O   . GLY A 1 53  ? 10.31100  -8.96300  20.02800 1.000 28.24000 ? 53  GLY A O   1 
ATOM   426  N  N   . THR A 1 54  ? 10.20500  -7.30200  18.51100 1.000 24.34000 ? 54  THR A N   1 
ATOM   427  C  CA  . THR A 1 54  ? 10.06200  -6.23300  19.48800 1.000 26.05000 ? 54  THR A CA  1 
ATOM   428  C  C   . THR A 1 54  ? 8.89400   -5.36000  19.07300 1.000 22.89000 ? 54  THR A C   1 
ATOM   429  O  O   . THR A 1 54  ? 8.56100   -5.27200  17.89100 1.000 25.38000 ? 54  THR A O   1 
ATOM   430  C  CB  . THR A 1 54  ? 11.31700  -5.34500  19.58700 1.000 27.98000 ? 54  THR A CB  1 
ATOM   431  O  OG1 . THR A 1 54  ? 11.52000  -4.67500  18.33100 1.000 23.98000 ? 54  THR A OG1 1 
ATOM   432  C  CG2 . THR A 1 54  ? 12.55200  -6.16200  19.96900 1.000 21.15000 ? 54  THR A CG2 1 
ATOM   433  N  N   . VAL A 1 55  ? 8.27200   -4.70800  20.04700 1.000 21.68000 ? 55  VAL A N   1 
ATOM   434  C  CA  . VAL A 1 55  ? 7.21000   -3.75300  19.77300 1.000 23.99000 ? 55  VAL A CA  1 
ATOM   435  C  C   . VAL A 1 55  ? 7.56700   -2.45200  20.47200 1.000 33.88000 ? 55  VAL A C   1 
ATOM   436  O  O   . VAL A 1 55  ? 7.91800   -2.46300  21.65700 1.000 26.69000 ? 55  VAL A O   1 
ATOM   437  C  CB  . VAL A 1 55  ? 5.83400   -4.27500  20.23600 1.000 32.49000 ? 55  VAL A CB  1 
ATOM   438  C  CG1 . VAL A 1 55  ? 4.75200   -3.24600  19.97200 1.000 25.82000 ? 55  VAL A CG1 1 
ATOM   439  C  CG2 . VAL A 1 55  ? 5.50300   -5.56800  19.51500 1.000 29.27000 ? 55  VAL A CG2 1 
ATOM   440  N  N   . VAL A 1 56  ? 7.51300   -1.34000  19.73200 1.000 29.85000 ? 56  VAL A N   1 
ATOM   441  C  CA  . VAL A 1 56  ? 7.79400   -0.01700  20.28200 1.000 28.86000 ? 56  VAL A CA  1 
ATOM   442  C  C   . VAL A 1 56  ? 6.80600   0.99300   19.70800 1.000 30.12000 ? 56  VAL A C   1 
ATOM   443  O  O   . VAL A 1 56  ? 6.43700   0.93100   18.52800 1.000 26.69000 ? 56  VAL A O   1 
ATOM   444  C  CB  . VAL A 1 56  ? 9.24600   0.44300   20.01300 1.000 29.97000 ? 56  VAL A CB  1 
ATOM   445  C  CG1 . VAL A 1 56  ? 10.25400  -0.52700  20.62100 1.000 27.76000 ? 56  VAL A CG1 1 
ATOM   446  C  CG2 . VAL A 1 56  ? 9.50700   0.64500   18.52300 1.000 26.26000 ? 56  VAL A CG2 1 
ATOM   447  N  N   . GLY A 1 57  ? 6.38100   1.93100   20.55400 1.000 31.44000 ? 57  GLY A N   1 
ATOM   448  C  CA  . GLY A 1 57  ? 5.50800   3.00800   20.13800 1.000 29.40000 ? 57  GLY A CA  1 
ATOM   449  C  C   . GLY A 1 57  ? 5.92100   4.31400   20.79000 1.000 29.49000 ? 57  GLY A C   1 
ATOM   450  O  O   . GLY A 1 57  ? 6.88100   4.36900   21.56600 1.000 28.61000 ? 57  GLY A O   1 
ATOM   451  N  N   . SER A 1 58  ? 5.17500   5.36600   20.46100 1.000 29.49000 ? 58  SER A N   1 
ATOM   452  C  CA  . SER A 1 58  ? 5.50400   6.69200   20.95900 1.000 29.25000 ? 58  SER A CA  1 
ATOM   453  C  C   . SER A 1 58  ? 5.18100   6.80100   22.44300 1.000 25.45000 ? 58  SER A C   1 
ATOM   454  O  O   . SER A 1 58  ? 4.17300   6.26600   22.91700 1.000 24.06000 ? 58  SER A O   1 
ATOM   455  C  CB  . SER A 1 58  ? 4.73900   7.76100   20.17700 1.000 24.60000 ? 58  SER A CB  1 
ATOM   456  O  OG  . SER A 1 58  ? 5.06800   7.72200   18.80000 1.000 27.90000 ? 58  SER A OG  1 
ATOM   457  N  N   . SER A 1 59  ? 6.05900   7.47800   23.18200 1.000 25.75000 ? 59  SER A N   1 
ATOM   458  C  CA  . SER A 1 59  ? 5.74900   7.85100   24.55400 1.000 26.29000 ? 59  SER A CA  1 
ATOM   459  C  C   . SER A 1 59  ? 4.74500   8.99400   24.57500 1.000 26.82000 ? 59  SER A C   1 
ATOM   460  O  O   . SER A 1 59  ? 4.72000   9.85300   23.68500 1.000 24.80000 ? 59  SER A O   1 
ATOM   461  C  CB  . SER A 1 59  ? 7.01100   8.26400   25.30800 1.000 29.18000 ? 59  SER A CB  1 
ATOM   462  O  OG  . SER A 1 59  ? 6.69600   9.17500   26.35700 1.000 31.23000 ? 59  SER A OG  1 
ATOM   463  N  N   . GLY A 1 60  ? 3.91600   9.00500   25.60800 1.000 25.34000 ? 60  GLY A N   1 
ATOM   464  C  CA  . GLY A 1 60  ? 2.92300   10.04300  25.72700 1.000 26.53000 ? 60  GLY A CA  1 
ATOM   465  C  C   . GLY A 1 60  ? 3.41800   11.37100  26.25200 1.000 22.86000 ? 60  GLY A C   1 
ATOM   466  O  O   . GLY A 1 60  ? 2.59300   12.23500  26.55600 1.000 25.28000 ? 60  GLY A O   1 
ATOM   467  N  N   . LEU A 1 61  ? 4.73000   11.55200  26.43400 1.000 24.15000 ? 61  LEU A N   1 
ATOM   468  C  CA  . LEU A 1 61  ? 5.28800   12.88200  26.66700 1.000 22.90000 ? 61  LEU A CA  1 
ATOM   469  C  C   . LEU A 1 61  ? 5.87300   13.48000  25.40300 1.000 22.38000 ? 61  LEU A C   1 
ATOM   470  O  O   . LEU A 1 61  ? 6.32800   14.63100  25.42500 1.000 19.01000 ? 61  LEU A O   1 
ATOM   471  C  CB  . LEU A 1 61  ? 6.37300   12.85100  27.74600 1.000 21.09000 ? 61  LEU A CB  1 
ATOM   472  C  CG  . LEU A 1 61  ? 5.96300   12.44900  29.16500 1.000 26.28000 ? 61  LEU A CG  1 
ATOM   473  C  CD1 . LEU A 1 61  ? 7.20000   12.40100  30.05400 1.000 31.77000 ? 61  LEU A CD1 1 
ATOM   474  C  CD2 . LEU A 1 61  ? 4.90000   13.39100  29.73000 1.000 23.55000 ? 61  LEU A CD2 1 
ATOM   475  N  N   . ASN A 1 62  ? 5.87600   12.72900  24.30600 1.000 17.38000 ? 62  ASN A N   1 
ATOM   476  C  CA  . ASN A 1 62  ? 6.59900   13.12900  23.11100 1.000 19.25000 ? 62  ASN A CA  1 
ATOM   477  C  C   . ASN A 1 62  ? 5.68700   13.54800  21.97100 1.000 18.76000 ? 62  ASN A C   1 
ATOM   478  O  O   . ASN A 1 62  ? 6.18100   13.90300  20.89600 1.000 18.09000 ? 62  ASN A O   1 
ATOM   479  C  CB  . ASN A 1 62  ? 7.51800   11.98800  22.66800 1.000 20.63000 ? 62  ASN A CB  1 
ATOM   480  C  CG  . ASN A 1 62  ? 8.70600   11.81700  23.59600 1.000 22.32000 ? 62  ASN A CG  1 
ATOM   481  O  OD1 . ASN A 1 62  ? 8.99500   12.69200  24.41500 1.000 24.06000 ? 62  ASN A OD1 1 
ATOM   482  N  ND2 . ASN A 1 62  ? 9.40800   10.69100  23.47000 1.000 24.62000 ? 62  ASN A ND2 1 
ATOM   483  N  N   . ALA A 1 63  ? 4.37600   13.53200  22.18000 1.000 16.73000 ? 63  ALA A N   1 
ATOM   484  C  CA  . ALA A 1 63  ? 3.42500   13.92300  21.14900 1.000 15.23000 ? 63  ALA A CA  1 
ATOM   485  C  C   . ALA A 1 63  ? 2.21900   14.59300  21.80300 1.000 18.16000 ? 63  ALA A C   1 
ATOM   486  O  O   . ALA A 1 63  ? 1.07000   14.27600  21.50200 1.000 22.68000 ? 63  ALA A O   1 
ATOM   487  C  CB  . ALA A 1 63  ? 2.99900   12.71600  20.31300 1.000 14.11000 ? 63  ALA A CB  1 
ATOM   488  N  N   . VAL A 1 64  ? 2.47300   15.56200  22.69300 1.000 19.66000 ? 64  VAL A N   1 
ATOM   489  C  CA  . VAL A 1 64  ? 1.42200   16.08900  23.56900 1.000 19.88000 ? 64  VAL A CA  1 
ATOM   490  C  C   . VAL A 1 64  ? 0.75900   17.33700  23.01800 1.000 20.33000 ? 64  VAL A C   1 
ATOM   491  O  O   . VAL A 1 64  ? -0.14100  17.89400  23.66200 1.000 18.59000 ? 64  VAL A O   1 
ATOM   492  C  CB  . VAL A 1 64  ? 1.95800   16.44000  24.97000 1.000 21.27000 ? 64  VAL A CB  1 
ATOM   493  C  CG1 . VAL A 1 64  ? 2.66100   15.26000  25.58200 1.000 20.85000 ? 64  VAL A CG1 1 
ATOM   494  C  CG2 . VAL A 1 64  ? 2.87500   17.66100  24.89000 1.000 20.61000 ? 64  VAL A CG2 1 
ATOM   495  N  N   . VAL A 1 65  ? 1.17700   17.97800  21.89100 1.000 17.10000 ? 65  VAL A N   1 
ATOM   496  C  CA  . VAL A 1 65  ? 0.66300   19.27000  21.47000 1.000 18.42000 ? 65  VAL A CA  1 
ATOM   497  C  C   . VAL A 1 65  ? -0.86700  19.23100  21.37600 1.000 17.27000 ? 65  VAL A C   1 
ATOM   498  O  O   . VAL A 1 65  ? -1.45200  18.33700  20.74900 1.000 19.44000 ? 65  VAL A O   1 
ATOM   499  C  CB  . VAL A 1 65  ? 1.40000   19.65500  20.17300 1.000 21.34000 ? 65  VAL A CB  1 
ATOM   500  C  CG1 . VAL A 1 65  ? 2.90700   19.86500  20.33900 1.000 23.03000 ? 65  VAL A CG1 1 
ATOM   501  C  CG2 . VAL A 1 65  ? 1.02700   18.77800  19.02900 1.000 18.57000 ? 65  VAL A CG2 1 
ATOM   502  N  N   . SER A 1 66  ? -1.23200  20.29900  21.99400 1.000 17.74000 ? 66  SER A N   1 
ATOM   503  C  CA  . SER A 1 66  ? -2.64700  20.66400  22.18500 1.000 17.73000 ? 66  SER A CA  1 
ATOM   504  C  C   . SER A 1 66  ? -3.41200  19.79800  23.18800 1.000 20.15000 ? 66  SER A C   1 
ATOM   505  O  O   . SER A 1 66  ? -4.55800  20.12100  23.53300 1.000 19.28000 ? 66  SER A O   1 
ATOM   506  C  CB  . SER A 1 66  ? -3.41100  20.67800  20.85300 1.000 19.06000 ? 66  SER A CB  1 
ATOM   507  O  OG  . SER A 1 66  ? -3.81100  19.38000  20.44300 1.000 17.42000 ? 66  SER A OG  1 
ATOM   508  N  N   . TRP A 1 67  ? -2.80900  18.71300  23.68200 1.000 15.56000 ? 67  TRP A N   1 
ATOM   509  C  CA  . TRP A 1 67  ? -3.47400  17.92200  24.71300 1.000 18.89000 ? 67  TRP A CA  1 
ATOM   510  C  C   . TRP A 1 67  ? -3.57600  18.71300  26.01800 1.000 19.11000 ? 67  TRP A C   1 
ATOM   511  O  O   . TRP A 1 67  ? -2.61100  19.38100  26.41700 1.000 18.49000 ? 67  TRP A O   1 
ATOM   512  C  CB  . TRP A 1 67  ? -2.70700  16.63700  25.02000 1.000 16.54000 ? 67  TRP A CB  1 
ATOM   513  C  CG  . TRP A 1 67  ? -2.73500  15.55300  24.02300 1.000 18.15000 ? 67  TRP A CG  1 
ATOM   514  C  CD1 . TRP A 1 67  ? -3.37200  15.52900  22.81800 1.000 16.11000 ? 67  TRP A CD1 1 
ATOM   515  C  CD2 . TRP A 1 67  ? -2.08200  14.29600  24.16800 1.000 15.85000 ? 67  TRP A CD2 1 
ATOM   516  N  NE1 . TRP A 1 67  ? -3.13000  14.31800  22.18800 1.000 16.62000 ? 67  TRP A NE1 1 
ATOM   517  C  CE2 . TRP A 1 67  ? -2.34300  13.55000  23.01100 1.000 15.94000 ? 67  TRP A CE2 1 
ATOM   518  C  CE3 . TRP A 1 67  ? -1.28700  13.73500  25.17500 1.000 17.44000 ? 67  TRP A CE3 1 
ATOM   519  C  CZ2 . TRP A 1 67  ? -1.84200  12.27000  22.83100 1.000 21.08000 ? 67  TRP A CZ2 1 
ATOM   520  C  CZ3 . TRP A 1 67  ? -0.79800  12.47400  24.99800 1.000 23.14000 ? 67  TRP A CZ3 1 
ATOM   521  C  CH2 . TRP A 1 67  ? -1.07300  11.74900  23.83100 1.000 22.58000 ? 67  TRP A CH2 1 
ATOM   522  N  N   . PRO A 1 68  ? -4.69600  18.60600  26.73600 1.000 18.20000 ? 68  PRO A N   1 
ATOM   523  C  CA  . PRO A 1 68  ? -4.72700  19.09500  28.12100 1.000 19.12000 ? 68  PRO A CA  1 
ATOM   524  C  C   . PRO A 1 68  ? -3.61200  18.45700  28.93900 1.000 21.56000 ? 68  PRO A C   1 
ATOM   525  O  O   . PRO A 1 68  ? -3.26700  17.28600  28.75200 1.000 16.35000 ? 68  PRO A O   1 
ATOM   526  C  CB  . PRO A 1 68  ? -6.11300  18.66900  28.63300 1.000 16.91000 ? 68  PRO A CB  1 
ATOM   527  C  CG  . PRO A 1 68  ? -6.92300  18.40300  27.42400 1.000 21.94000 ? 68  PRO A CG  1 
ATOM   528  C  CD  . PRO A 1 68  ? -5.97800  18.00600  26.31600 1.000 18.86000 ? 68  PRO A CD  1 
ATOM   529  N  N   . LYS A 1 69  ? -3.03800  19.24300  29.85400 1.000 21.19000 ? 69  LYS A N   1 
ATOM   530  C  CA  . LYS A 1 69  ? -1.85000  18.77400  30.56000 1.000 19.84000 ? 69  LYS A CA  1 
ATOM   531  C  C   . LYS A 1 69  ? -2.12200  17.52700  31.38800 1.000 21.02000 ? 69  LYS A C   1 
ATOM   532  O  O   . LYS A 1 69  ? -1.22100  16.69800  31.55900 1.000 18.01000 ? 69  LYS A O   1 
ATOM   533  C  CB  . LYS A 1 69  ? -1.27600  19.88900  31.43100 1.000 23.27000 ? 69  LYS A CB  1 
ATOM   534  C  CG  . LYS A 1 69  ? -0.61700  20.95800  30.59400 1.000 23.67000 ? 69  LYS A CG  1 
ATOM   535  C  CD  . LYS A 1 69  ? 0.20400   21.85600  31.45100 1.000 32.27000 ? 69  LYS A CD  1 
ATOM   536  C  CE  . LYS A 1 69  ? -0.66300  22.55600  32.46400 1.000 34.80000 ? 69  LYS A CE  1 
ATOM   537  N  NZ  . LYS A 1 69  ? -0.46800  24.03700  32.37800 1.000 34.08000 ? 69  LYS A NZ  1 
ATOM   538  N  N   . HIS A 1 70  ? -3.34700  17.35200  31.88800 1.000 18.79000 ? 70  HIS A N   1 
ATOM   539  C  CA  . HIS A 1 70  ? -3.59800  16.15300  32.67300 1.000 15.92000 ? 70  HIS A CA  1 
ATOM   540  C  C   . HIS A 1 70  ? -3.57200  14.88900  31.81900 1.000 18.84000 ? 70  HIS A C   1 
ATOM   541  O  O   . HIS A 1 70  ? -3.54200  13.78900  32.37100 1.000 18.36000 ? 70  HIS A O   1 
ATOM   542  C  CB  . HIS A 1 70  ? -4.93800  16.28700  33.41600 1.000 17.63000 ? 70  HIS A CB  1 
ATOM   543  C  CG  . HIS A 1 70  ? -6.13600  16.14900  32.52600 1.000 18.25000 ? 70  HIS A CG  1 
ATOM   544  N  ND1 . HIS A 1 70  ? -6.66700  17.21000  31.83100 1.000 15.95000 ? 70  HIS A ND1 1 
ATOM   545  C  CD2 . HIS A 1 70  ? -6.87600  15.06700  32.18100 1.000 16.45000 ? 70  HIS A CD2 1 
ATOM   546  C  CE1 . HIS A 1 70  ? -7.68800  16.79400  31.10300 1.000 16.52000 ? 70  HIS A CE1 1 
ATOM   547  N  NE2 . HIS A 1 70  ? -7.83700  15.49900  31.29800 1.000 20.85000 ? 70  HIS A NE2 1 
ATOM   548  N  N   . GLU A 1 71  ? -3.56200  15.01500  30.49100 1.000 16.40000 ? 71  GLU A N   1 
ATOM   549  C  CA  . GLU A 1 71  ? -3.48100  13.85300  29.62200 1.000 17.54000 ? 71  GLU A CA  1 
ATOM   550  C  C   . GLU A 1 71  ? -2.05200  13.46900  29.27100 1.000 16.98000 ? 71  GLU A C   1 
ATOM   551  O  O   . GLU A 1 71  ? -1.85000  12.40900  28.66400 1.000 21.42000 ? 71  GLU A O   1 
ATOM   552  C  CB  . GLU A 1 71  ? -4.29300  14.10000  28.33800 1.000 15.96000 ? 71  GLU A CB  1 
ATOM   553  C  CG  . GLU A 1 71  ? -5.79000  14.18800  28.60500 1.000 18.29000 ? 71  GLU A CG  1 
ATOM   554  C  CD  . GLU A 1 71  ? -6.62000  14.15600  27.33900 1.000 20.97000 ? 71  GLU A CD  1 
ATOM   555  O  OE1 . GLU A 1 71  ? -6.07700  14.45400  26.24500 1.000 20.77000 ? 71  GLU A OE1 1 
ATOM   556  O  OE2 . GLU A 1 71  ? -7.82600  13.83700  27.43700 1.000 20.87000 ? 71  GLU A OE2 1 
ATOM   557  N  N   . TRP A 1 72  ? -1.06300  14.29500  29.62100 1.000 18.27000 ? 72  TRP A N   1 
ATOM   558  C  CA  . TRP A 1 72  ? 0.33300   13.96200  29.34500 1.000 19.64000 ? 72  TRP A CA  1 
ATOM   559  C  C   . TRP A 1 72  ? 0.79700   12.83900  30.26600 1.000 20.65000 ? 72  TRP A C   1 
ATOM   560  O  O   . TRP A 1 72  ? 0.43800   12.80100  31.44300 1.000 22.69000 ? 72  TRP A O   1 
ATOM   561  C  CB  . TRP A 1 72  ? 1.23500   15.18300  29.55900 1.000 20.23000 ? 72  TRP A CB  1 
ATOM   562  C  CG  . TRP A 1 72  ? 0.88600   16.41800  28.77200 1.000 18.17000 ? 72  TRP A CG  1 
ATOM   563  C  CD1 . TRP A 1 72  ? -0.24500  16.64100  28.03800 1.000 21.07000 ? 72  TRP A CD1 1 
ATOM   564  C  CD2 . TRP A 1 72  ? 1.68200   17.60300  28.64400 1.000 18.11000 ? 72  TRP A CD2 1 
ATOM   565  N  NE1 . TRP A 1 72  ? -0.20400  17.89000  27.47400 1.000 19.24000 ? 72  TRP A NE1 1 
ATOM   566  C  CE2 . TRP A 1 72  ? 0.97100   18.49800  27.82600 1.000 18.45000 ? 72  TRP A CE2 1 
ATOM   567  C  CE3 . TRP A 1 72  ? 2.92400   17.99700  29.15300 1.000 21.69000 ? 72  TRP A CE3 1 
ATOM   568  C  CZ2 . TRP A 1 72  ? 1.45800   19.75900  27.50300 1.000 21.08000 ? 72  TRP A CZ2 1 
ATOM   569  C  CZ3 . TRP A 1 72  ? 3.41000   19.24900  28.82400 1.000 18.45000 ? 72  TRP A CZ3 1 
ATOM   570  C  CH2 . TRP A 1 72  ? 2.67900   20.11400  28.01000 1.000 22.53000 ? 72  TRP A CH2 1 
ATOM   571  N  N   . GLY A 1 73  ? 1.61300   11.92800  29.75100 1.000 18.44000 ? 73  GLY A N   1 
ATOM   572  C  CA  . GLY A 1 73  ? 2.08100   10.85300  30.61600 1.000 24.04000 ? 73  GLY A CA  1 
ATOM   573  C  C   . GLY A 1 73  ? 2.99200   9.90200   29.87900 1.000 24.41000 ? 73  GLY A C   1 
ATOM   574  O  O   . GLY A 1 73  ? 3.15000   9.97600   28.66300 1.000 24.28000 ? 73  GLY A O   1 
ATOM   575  N  N   . MET A 1 74  ? 3.57100   8.97600   30.64500 1.000 26.96000 ? 74  MET A N   1 
ATOM   576  C  CA  . MET A 1 74  ? 4.56300   8.04700   30.11400 1.000 30.62000 ? 74  MET A CA  1 
ATOM   577  C  C   . MET A 1 74  ? 3.95500   6.93800   29.26000 1.000 31.28000 ? 74  MET A C   1 
ATOM   578  O  O   . MET A 1 74  ? 4.65100   6.38500   28.40400 1.000 30.64000 ? 74  MET A O   1 
ATOM   579  C  CB  . MET A 1 74  ? 5.35200   7.41900   31.26600 1.000 34.29000 ? 74  MET A CB  1 
ATOM   580  C  CG  . MET A 1 74  ? 6.20900   8.39100   32.04600 1.000 42.64000 ? 74  MET A CG  1 
ATOM   581  S  SD  . MET A 1 74  ? 7.63100   8.88000   31.06600 1.000 65.33000 ? 74  MET A SD  1 
ATOM   582  C  CE  . MET A 1 74  ? 8.54300   7.33600   30.97900 1.000 55.81000 ? 74  MET A CE  1 
ATOM   583  N  N   . ASP A 1 75  ? 2.68600   6.58200   29.48100 1.000 30.39000 ? 75  ASP A N   1 
ATOM   584  C  CA  . ASP A 1 75  ? 2.04100   5.47800   28.76600 1.000 30.97000 ? 75  ASP A CA  1 
ATOM   585  C  C   . ASP A 1 75  ? 2.18300   5.62500   27.25300 1.000 34.76000 ? 75  ASP A C   1 
ATOM   586  O  O   . ASP A 1 75  ? 2.23300   6.75000   26.74200 1.000 27.10000 ? 75  ASP A O   1 
ATOM   587  C  CB  . ASP A 1 75  ? 0.55800   5.39600   29.12800 1.000 32.97000 ? 75  ASP A CB  1 
ATOM   588  C  CG  . ASP A 1 75  ? 0.32500   4.91800   30.55400 1.000 44.90000 ? 75  ASP A CG  1 
ATOM   589  O  OD1 . ASP A 1 75  ? 1.16600   4.15600   31.09000 1.000 40.88000 ? 75  ASP A OD1 1 
ATOM   590  O  OD2 . ASP A 1 75  ? -0.70600  5.31500   31.13900 1.000 44.87000 ? 75  ASP A OD2 1 
ATOM   591  N  N   . PRO A 1 76  ? 2.23900   4.52100   26.50600 1.000 28.06000 ? 76  PRO A N   1 
ATOM   592  C  CA  . PRO A 1 76  ? 2.33100   4.62600   25.04600 1.000 24.45000 ? 76  PRO A CA  1 
ATOM   593  C  C   . PRO A 1 76  ? 1.10000   5.30500   24.46000 1.000 25.38000 ? 76  PRO A C   1 
ATOM   594  O  O   . PRO A 1 76  ? -0.00000  5.22500   25.00400 1.000 24.69000 ? 76  PRO A O   1 
ATOM   595  C  CB  . PRO A 1 76  ? 2.43300   3.16600   24.58500 1.000 29.49000 ? 76  PRO A CB  1 
ATOM   596  C  CG  . PRO A 1 76  ? 2.73900   2.36500   25.82700 1.000 36.26000 ? 76  PRO A CG  1 
ATOM   597  C  CD  . PRO A 1 76  ? 2.15400   3.12500   26.96600 1.000 28.81000 ? 76  PRO A CD  1 
ATOM   598  N  N   . THR A 1 77  ? 1.30600   6.00200   23.34700 1.000 23.46000 ? 77  THR A N   1 
ATOM   599  C  CA  . THR A 1 77  ? 0.24800   6.65800   22.59200 1.000 14.48000 ? 77  THR A CA  1 
ATOM   600  C  C   . THR A 1 77  ? 0.42300   6.30000   21.12000 1.000 22.70000 ? 77  THR A C   1 
ATOM   601  O  O   . THR A 1 77  ? 1.41100   5.67800   20.72200 1.000 27.15000 ? 77  THR A O   1 
ATOM   602  C  CB  . THR A 1 77  ? 0.26900   8.18500   22.81600 1.000 21.96000 ? 77  THR A CB  1 
ATOM   603  O  OG1 . THR A 1 77  ? -0.86300  8.79400   22.17700 1.000 22.50000 ? 77  THR A OG1 1 
ATOM   604  C  CG2 . THR A 1 77  ? 1.55800   8.80900   22.27900 1.000 17.78000 ? 77  THR A CG2 1 
ATOM   605  N  N   . GLY A 1 78  ? -0.53700  6.68600   20.29400 1.000 18.76000 ? 78  GLY A N   1 
ATOM   606  C  CA  . GLY A 1 78  ? -0.49600  6.27700   18.90800 1.000 17.44000 ? 78  GLY A CA  1 
ATOM   607  C  C   . GLY A 1 78  ? -1.23400  7.26800   18.04300 1.000 19.04000 ? 78  GLY A C   1 
ATOM   608  O  O   . GLY A 1 78  ? -1.77600  8.26100   18.53500 1.000 18.84000 ? 78  GLY A O   1 
ATOM   609  N  N   . TYR A 1 79  ? -1.26400  6.96800   16.73500 1.000 13.64000 ? 79  TYR A N   1 
ATOM   610  C  CA  . TYR A 1 79  ? -1.79200  7.89600   15.74200 1.000 16.68000 ? 79  TYR A CA  1 
ATOM   611  C  C   . TYR A 1 79  ? -3.17600  8.40000   16.11100 1.000 14.50000 ? 79  TYR A C   1 
ATOM   612  O  O   . TYR A 1 79  ? -3.48600  9.57900   15.90100 1.000 17.61000 ? 79  TYR A O   1 
ATOM   613  C  CB  . TYR A 1 79  ? -1.88300  7.24000   14.36400 1.000 17.64000 ? 79  TYR A CB  1 
ATOM   614  C  CG  . TYR A 1 79  ? -0.60900  6.73900   13.74400 1.000 17.84000 ? 79  TYR A CG  1 
ATOM   615  C  CD1 . TYR A 1 79  ? 0.49100   7.57100   13.57700 1.000 17.79000 ? 79  TYR A CD1 1 
ATOM   616  C  CD2 . TYR A 1 79  ? -0.53400  5.43600   13.26600 1.000 21.15000 ? 79  TYR A CD2 1 
ATOM   617  C  CE1 . TYR A 1 79  ? 1.65200   7.09900   12.96800 1.000 19.32000 ? 79  TYR A CE1 1 
ATOM   618  C  CE2 . TYR A 1 79  ? 0.61800   4.95600   12.65400 1.000 21.94000 ? 79  TYR A CE2 1 
ATOM   619  C  CZ  . TYR A 1 79  ? 1.70800   5.78800   12.51500 1.000 20.17000 ? 79  TYR A CZ  1 
ATOM   620  O  OH  . TYR A 1 79  ? 2.85400   5.30200   11.91400 1.000 17.28000 ? 79  TYR A OH  1 
ATOM   621  N  N   . ALA A 1 80  ? -4.03700  7.51300   16.62800 1.000 14.50000 ? 80  ALA A N   1 
ATOM   622  C  CA  . ALA A 1 80  ? -5.43000  7.89600   16.82800 1.000 15.53000 ? 80  ALA A CA  1 
ATOM   623  C  C   . ALA A 1 80  ? -5.55600  9.04600   17.80900 1.000 15.79000 ? 80  ALA A C   1 
ATOM   624  O  O   . ALA A 1 80  ? -6.45500  9.88400   17.67500 1.000 19.72000 ? 80  ALA A O   1 
ATOM   625  C  CB  . ALA A 1 80  ? -6.25000  6.69400   17.31400 1.000 18.46000 ? 80  ALA A CB  1 
ATOM   626  N  N   . GLU A 1 81  ? -4.68100  9.09500   18.80500 1.000 16.44000 ? 81  GLU A N   1 
ATOM   627  C  CA  . GLU A 1 81  ? -4.74800  10.08900  19.86400 1.000 18.92000 ? 81  GLU A CA  1 
ATOM   628  C  C   . GLU A 1 81  ? -4.00200  11.36600  19.52400 1.000 17.86000 ? 81  GLU A C   1 
ATOM   629  O  O   . GLU A 1 81  ? -4.22600  12.38800  20.17600 1.000 15.81000 ? 81  GLU A O   1 
ATOM   630  C  CB  . GLU A 1 81  ? -4.19000  9.49400   21.16400 1.000 17.30000 ? 81  GLU A CB  1 
ATOM   631  C  CG  . GLU A 1 81  ? -5.12000  8.46400   21.76000 1.000 20.45000 ? 81  GLU A CG  1 
ATOM   632  C  CD  . GLU A 1 81  ? -4.54700  7.76200   22.96600 1.000 25.89000 ? 81  GLU A CD  1 
ATOM   633  O  OE1 . GLU A 1 81  ? -3.34500  7.93600   23.25400 1.000 21.82000 ? 81  GLU A OE1 1 
ATOM   634  O  OE2 . GLU A 1 81  ? -5.30800  7.02800   23.62600 1.000 25.72000 ? 81  GLU A OE2 1 
ATOM   635  N  N   . MET A 1 82  ? -3.14300  11.33800  18.51500 1.000 13.44000 ? 82  MET A N   1 
ATOM   636  C  CA  . MET A 1 82  ? -2.25000  12.44800  18.22900 1.000 15.59000 ? 82  MET A CA  1 
ATOM   637  C  C   . MET A 1 82  ? -2.92100  13.49800  17.36200 1.000 15.29000 ? 82  MET A C   1 
ATOM   638  O  O   . MET A 1 82  ? -3.70500  13.17900  16.46700 1.000 18.51000 ? 82  MET A O   1 
ATOM   639  C  CB  . MET A 1 82  ? -0.99300  11.94700  17.52100 1.000 15.42000 ? 82  MET A CB  1 
ATOM   640  C  CG  . MET A 1 82  ? -0.13500  11.03200  18.36200 1.000 22.32000 ? 82  MET A CG  1 
ATOM   641  S  SD  . MET A 1 82  ? 1.06300   10.20000  17.31300 1.000 18.01000 ? 82  MET A SD  1 
ATOM   642  C  CE  . MET A 1 82  ? 1.95400   9.23600   18.51000 1.000 16.92000 ? 82  MET A CE  1 
ATOM   643  N  N   . ARG A 1 83  ? -2.60600  14.75500  17.63000 1.000 15.59000 ? 83  ARG A N   1 
ATOM   644  C  CA  . ARG A 1 83  ? -2.91100  15.79400  16.66800 1.000 15.69000 ? 83  ARG A CA  1 
ATOM   645  C  C   . ARG A 1 83  ? -2.31000  15.39200  15.32600 1.000 15.83000 ? 83  ARG A C   1 
ATOM   646  O  O   . ARG A 1 83  ? -1.13900  14.98900  15.27800 1.000 15.77000 ? 83  ARG A O   1 
ATOM   647  C  CB  . ARG A 1 83  ? -2.34200  17.13300  17.13700 1.000 14.87000 ? 83  ARG A CB  1 
ATOM   648  C  CG  . ARG A 1 83  ? -2.59200  18.32400  16.20500 1.000 18.19000 ? 83  ARG A CG  1 
ATOM   649  C  CD  . ARG A 1 83  ? -2.16400  19.58000  16.92400 1.000 17.06000 ? 83  ARG A CD  1 
ATOM   650  N  NE  . ARG A 1 83  ? -2.23600  20.81200  16.14500 1.000 14.53000 ? 83  ARG A NE  1 
ATOM   651  C  CZ  . ARG A 1 83  ? -3.25200  21.67200  16.21200 1.000 20.89000 ? 83  ARG A CZ  1 
ATOM   652  N  NH1 . ARG A 1 83  ? -4.29800  21.40200  16.97800 1.000 17.64000 ? 83  ARG A NH1 1 
ATOM   653  N  NH2 . ARG A 1 83  ? -3.23000  22.79300  15.50100 1.000 18.48000 ? 83  ARG A NH2 1 
ATOM   654  N  N   . PRO A 1 84  ? -3.07500  15.44400  14.23400 1.000 18.84000 ? 84  PRO A N   1 
ATOM   655  C  CA  . PRO A 1 84  ? -2.57600  14.85900  12.98000 1.000 17.40000 ? 84  PRO A CA  1 
ATOM   656  C  C   . PRO A 1 84  ? -1.25000  15.44400  12.51600 1.000 17.81000 ? 84  PRO A C   1 
ATOM   657  O  O   . PRO A 1 84  ? -0.45300  14.72800  11.89300 1.000 18.58000 ? 84  PRO A O   1 
ATOM   658  C  CB  . PRO A 1 84  ? -3.71400  15.14800  11.99600 1.000 18.21000 ? 84  PRO A CB  1 
ATOM   659  C  CG  . PRO A 1 84  ? -4.94100  15.12900  12.85700 1.000 20.16000 ? 84  PRO A CG  1 
ATOM   660  C  CD  . PRO A 1 84  ? -4.51800  15.75700  14.16400 1.000 18.57000 ? 84  PRO A CD  1 
ATOM   661  N  N   . ALA A 1 85  ? -0.98100  16.71200  12.84000 1.000 17.35000 ? 85  ALA A N   1 
ATOM   662  C  CA  . ALA A 1 85  ? 0.27900   17.34100  12.47400 1.000 17.00000 ? 85  ALA A CA  1 
ATOM   663  C  C   . ALA A 1 85  ? 1.50100   16.64200  13.07000 1.000 16.57000 ? 85  ALA A C   1 
ATOM   664  O  O   . ALA A 1 85  ? 2.60500   16.83100  12.54500 1.000 16.29000 ? 85  ALA A O   1 
ATOM   665  C  CB  . ALA A 1 85  ? 0.26700   18.81600  12.88400 1.000 15.60000 ? 85  ALA A CB  1 
ATOM   666  N  N   . VAL A 1 86  ? 1.35800   15.82200  14.12200 1.000 14.34000 ? 86  VAL A N   1 
ATOM   667  C  CA  . VAL A 1 86  ? 2.58000   15.18500  14.61900 1.000 17.05000 ? 86  VAL A CA  1 
ATOM   668  C  C   . VAL A 1 86  ? 3.08700   14.12500  13.63600 1.000 14.67000 ? 86  VAL A C   1 
ATOM   669  O  O   . VAL A 1 86  ? 4.30000   13.91600  13.52700 1.000 16.03000 ? 86  VAL A O   1 
ATOM   670  C  CB  . VAL A 1 86  ? 2.43300   14.58400  16.03900 1.000 15.86000 ? 86  VAL A CB  1 
ATOM   671  C  CG1 . VAL A 1 86  ? 1.68200   15.51500  16.98500 1.000 15.47000 ? 86  VAL A CG1 1 
ATOM   672  C  CG2 . VAL A 1 86  ? 1.85800   13.21700  15.99600 1.000 26.53000 ? 86  VAL A CG2 1 
ATOM   673  N  N   . TYR A 1 87  ? 2.19500   13.46500  12.88400 1.000 17.07000 ? 87  TYR A N   1 
ATOM   674  C  CA  . TYR A 1 87  ? 2.59600   12.41500  11.95300 1.000 16.41000 ? 87  TYR A CA  1 
ATOM   675  C  C   . TYR A 1 87  ? 2.33500   12.74400  10.48700 1.000 19.43000 ? 87  TYR A C   1 
ATOM   676  O  O   . TYR A 1 87  ? 2.90600   12.08000  9.61300  1.000 19.40000 ? 87  TYR A O   1 
ATOM   677  C  CB  . TYR A 1 87  ? 1.89800   11.08000  12.29900 1.000 20.16000 ? 87  TYR A CB  1 
ATOM   678  C  CG  . TYR A 1 87  ? 0.37800   11.15600  12.36500 1.000 20.71000 ? 87  TYR A CG  1 
ATOM   679  C  CD1 . TYR A 1 87  ? -0.39500  11.01600  11.21300 1.000 20.73000 ? 87  TYR A CD1 1 
ATOM   680  C  CD2 . TYR A 1 87  ? -0.27800  11.35400  13.57500 1.000 17.66000 ? 87  TYR A CD2 1 
ATOM   681  C  CE1 . TYR A 1 87  ? -1.77100  11.09200  11.25000 1.000 16.12000 ? 87  TYR A CE1 1 
ATOM   682  C  CE2 . TYR A 1 87  ? -1.67000  11.43100  13.62800 1.000 19.91000 ? 87  TYR A CE2 1 
ATOM   683  C  CZ  . TYR A 1 87  ? -2.41000  11.30100  12.45800 1.000 18.70000 ? 87  TYR A CZ  1 
ATOM   684  O  OH  . TYR A 1 87  ? -3.78500  11.37700  12.49400 1.000 20.19000 ? 87  TYR A OH  1 
ATOM   685  N  N   . ASP A 1 88  ? 1.50300   13.73700  10.19000 1.000 17.39000 ? 88  ASP A N   1 
ATOM   686  C  CA  . ASP A 1 88  ? 1.14700   14.11300  8.82600  1.000 18.84000 ? 88  ASP A CA  1 
ATOM   687  C  C   . ASP A 1 88  ? 1.87100   15.41000  8.49800  1.000 16.39000 ? 88  ASP A C   1 
ATOM   688  O  O   . ASP A 1 88  ? 1.50300   16.48100  9.00100  1.000 17.92000 ? 88  ASP A O   1 
ATOM   689  C  CB  . ASP A 1 88  ? -0.36700  14.27700  8.68500  1.000 18.33000 ? 88  ASP A CB  1 
ATOM   690  C  CG  . ASP A 1 88  ? -0.80200  14.64100  7.26300  1.000 24.37000 ? 88  ASP A CG  1 
ATOM   691  O  OD1 . ASP A 1 88  ? -0.18800  15.51000  6.63900  1.000 24.05000 ? 88  ASP A OD1 1 
ATOM   692  O  OD2 . ASP A 1 88  ? -1.78700  14.06500  6.76900  1.000 30.84000 ? 88  ASP A OD2 1 
ATOM   693  N  N   . MET A 1 89  ? 2.87800   15.32700  7.62700  1.000 19.43000 ? 89  MET A N   1 
ATOM   694  C  CA  . MET A 1 89  ? 3.72800   16.49500  7.41200  1.000 14.48000 ? 89  MET A CA  1 
ATOM   695  C  C   . MET A 1 89  ? 3.00700   17.61300  6.67400  1.000 18.11000 ? 89  MET A C   1 
ATOM   696  O  O   . MET A 1 89  ? 3.41100   18.77300  6.79800  1.000 17.80000 ? 89  MET A O   1 
ATOM   697  C  CB  . MET A 1 89  ? 5.01100   16.08400  6.68300  1.000 19.21000 ? 89  MET A CB  1 
ATOM   698  C  CG  . MET A 1 89  ? 5.91400   15.20100  7.54000  1.000 22.20000 ? 89  MET A CG  1 
ATOM   699  S  SD  . MET A 1 89  ? 6.32400   15.84800  9.18500  1.000 21.26000 ? 89  MET A SD  1 
ATOM   700  C  CE  . MET A 1 89  ? 5.03100   15.13500  10.23100 1.000 14.62000 ? 89  MET A CE  1 
ATOM   701  N  N   . ASP A 1 90  ? 1.96200   17.29900  5.90800  1.000 19.09000 ? 90  ASP A N   1 
ATOM   702  C  CA  . ASP A 1 90  ? 1.14100   18.36400  5.34400  1.000 19.32000 ? 90  ASP A CA  1 
ATOM   703  C  C   . ASP A 1 90  ? 0.53600   19.21100  6.45400  1.000 20.78000 ? 90  ASP A C   1 
ATOM   704  O  O   . ASP A 1 90  ? 0.53800   20.44500  6.38100  1.000 20.22000 ? 90  ASP A O   1 
ATOM   705  C  CB  . ASP A 1 90  ? 0.04300   17.77900  4.44800  1.000 17.28000 ? 90  ASP A CB  1 
ATOM   706  C  CG  . ASP A 1 90  ? 0.57000   17.33700  3.08200  1.000 27.07000 ? 90  ASP A CG  1 
ATOM   707  O  OD1 . ASP A 1 90  ? 1.59800   17.88200  2.64100  1.000 26.93000 ? 90  ASP A OD1 1 
ATOM   708  O  OD2 . ASP A 1 90  ? -0.04800  16.45300  2.44800  1.000 33.94000 ? 90  ASP A OD2 1 
ATOM   709  N  N   . MET A 1 91  ? 0.03700   18.56400  7.50200  1.000 17.31000 ? 91  MET A N   1 
ATOM   710  C  CA  . MET A 1 91  ? -0.52400  19.29000  8.63200  1.000 17.93000 ? 91  MET A CA  1 
ATOM   711  C  C   . MET A 1 91  ? 0.56800   19.88300  9.51200  1.000 17.13000 ? 91  MET A C   1 
ATOM   712  O  O   . MET A 1 91  ? 0.36100   20.93100  10.13600 1.000 16.67000 ? 91  MET A O   1 
ATOM   713  C  CB  . MET A 1 91  ? -1.42500  18.35600  9.43900  1.000 18.02000 ? 91  MET A CB  1 
ATOM   714  C  CG  . MET A 1 91  ? -2.68100  17.89600  8.69100  1.000 25.24000 ? 91  MET A CG  1 
ATOM   715  S  SD  . MET A 1 91  ? -3.74600  19.29300  8.28100  1.000 30.44000 ? 91  MET A SD  1 
ATOM   716  C  CE  . MET A 1 91  ? -3.39200  19.49500  6.53500  1.000 33.97000 ? 91  MET A CE  1 
ATOM   717  N  N   . ARG A 1 92  ? 1.73800   19.24100  9.55300  1.000 18.36000 ? 92  ARG A N   1 
ATOM   718  C  CA  . ARG A 1 92  ? 2.84100   19.76600  10.34500 1.000 12.83000 ? 92  ARG A CA  1 
ATOM   719  C  C   . ARG A 1 92  ? 3.24100   21.16100  9.87900  1.000 14.08000 ? 92  ARG A C   1 
ATOM   720  O  O   . ARG A 1 92  ? 3.45700   22.05900  10.70100 1.000 15.75000 ? 92  ARG A O   1 
ATOM   721  C  CB  . ARG A 1 92  ? 4.03300   18.80600  10.27100 1.000 13.01000 ? 92  ARG A CB  1 
ATOM   722  C  CG  . ARG A 1 92  ? 5.30200   19.32700  10.95100 1.000 13.35000 ? 92  ARG A CG  1 
ATOM   723  C  CD  . ARG A 1 92  ? 5.18100   19.27900  12.45100 1.000 13.91000 ? 92  ARG A CD  1 
ATOM   724  N  NE  . ARG A 1 92  ? 5.17100   17.91300  12.95500 1.000 16.23000 ? 92  ARG A NE  1 
ATOM   725  C  CZ  . ARG A 1 92  ? 6.19800   17.32600  13.56800 1.000 14.66000 ? 92  ARG A CZ  1 
ATOM   726  N  NH1 . ARG A 1 92  ? 7.33200   17.98600  13.75900 1.000 14.27000 ? 92  ARG A NH1 1 
ATOM   727  N  NH2 . ARG A 1 92  ? 6.08800   16.07700  13.99700 1.000 14.66000 ? 92  ARG A NH2 1 
ATOM   728  N  N   . VAL A 1 93  ? 3.32900   21.38000  8.56600  1.000 13.95000 ? 93  VAL A N   1 
ATOM   729  C  CA  . VAL A 1 93  ? 3.77400   22.70600  8.14300  1.000 15.57000 ? 93  VAL A CA  1 
ATOM   730  C  C   . VAL A 1 93  ? 2.71500   23.75000  8.46600  1.000 16.88000 ? 93  VAL A C   1 
ATOM   731  O  O   . VAL A 1 93  ? 3.04500   24.92200  8.68400  1.000 17.92000 ? 93  VAL A O   1 
ATOM   732  C  CB  . VAL A 1 93  ? 4.18700   22.72300  6.65500  1.000 15.90000 ? 93  VAL A CB  1 
ATOM   733  C  CG1 . VAL A 1 93  ? 5.35400   21.76000  6.42900  1.000 16.48000 ? 93  VAL A CG1 1 
ATOM   734  C  CG2 . VAL A 1 93  ? 3.03200   22.38300  5.75700  1.000 21.35000 ? 93  VAL A CG2 1 
ATOM   735  N  N   . ARG A 1 94  ? 1.44300   23.34300  8.57300  1.000 14.83000 ? 94  ARG A N   1 
ATOM   736  C  CA  . ARG A 1 94  ? 0.41300   24.28500  8.99800  1.000 16.54000 ? 94  ARG A CA  1 
ATOM   737  C  C   . ARG A 1 94  ? 0.57500   24.65700  10.46600 1.000 14.84000 ? 94  ARG A C   1 
ATOM   738  O  O   . ARG A 1 94  ? 0.43600   25.82700  10.83000 1.000 15.10000 ? 94  ARG A O   1 
ATOM   739  C  CB  . ARG A 1 94  ? -0.98000  23.70800  8.73700  1.000 19.08000 ? 94  ARG A CB  1 
ATOM   740  C  CG  . ARG A 1 94  ? -1.22300  23.35600  7.28600  1.000 22.28000 ? 94  ARG A CG  1 
ATOM   741  C  CD  . ARG A 1 94  ? -2.65000  23.73500  6.86800  1.000 26.36000 ? 94  ARG A CD  1 
ATOM   742  N  NE  . ARG A 1 94  ? -2.78600  25.18100  6.69100  1.000 29.27000 ? 94  ARG A NE  1 
ATOM   743  C  CZ  . ARG A 1 94  ? -3.95000  25.82700  6.70100  1.000 32.49000 ? 94  ARG A CZ  1 
ATOM   744  N  NH1 . ARG A 1 94  ? -5.08000  25.15100  6.87700  1.000 23.08000 ? 94  ARG A NH1 1 
ATOM   745  N  NH2 . ARG A 1 94  ? -3.98800  27.14300  6.53700  1.000 33.19000 ? 94  ARG A NH2 1 
ATOM   746  N  N   . ASP A 1 95  ? 0.89800   23.68200  11.31600 1.000 15.12000 ? 95  ASP A N   1 
ATOM   747  C  CA  . ASP A 1 95  ? 1.21400   23.98400  12.70900 1.000 17.23000 ? 95  ASP A CA  1 
ATOM   748  C  C   . ASP A 1 95  ? 2.46800   24.83800  12.82000 1.000 16.62000 ? 95  ASP A C   1 
ATOM   749  O  O   . ASP A 1 95  ? 2.56900   25.67000  13.72800 1.000 15.86000 ? 95  ASP A O   1 
ATOM   750  C  CB  . ASP A 1 95  ? 1.39200   22.69200  13.50200 1.000 13.72000 ? 95  ASP A CB  1 
ATOM   751  C  CG  . ASP A 1 95  ? 0.09200   22.18000  14.08800 1.000 17.18000 ? 95  ASP A CG  1 
ATOM   752  O  OD1 . ASP A 1 95  ? -0.98300  22.67400  13.68900 1.000 16.11000 ? 95  ASP A OD1 1 
ATOM   753  O  OD2 . ASP A 1 95  ? 0.14700   21.27200  14.95500 1.000 14.58000 ? 95  ASP A OD2 1 
ATOM   754  N  N   . MET A 1 96  ? 3.44300   24.62700  11.93000 1.000 16.03000 ? 96  MET A N   1 
ATOM   755  C  CA  . MET A 1 96  ? 4.63000   25.47100  11.93000 1.000 14.09000 ? 96  MET A CA  1 
ATOM   756  C  C   . MET A 1 96  ? 4.27300   26.90200  11.53100 1.000 16.84000 ? 96  MET A C   1 
ATOM   757  O  O   . MET A 1 96  ? 4.71300   27.86000  12.18100 1.000 14.57000 ? 96  MET A O   1 
ATOM   758  C  CB  . MET A 1 96  ? 5.69400   24.87800  11.00600 1.000 15.05000 ? 96  MET A CB  1 
ATOM   759  C  CG  . MET A 1 96  ? 6.42700   23.64700  11.59400 1.000 16.66000 ? 96  MET A CG  1 
ATOM   760  S  SD  . MET A 1 96  ? 7.29800   22.67100  10.32700 1.000 16.51000 ? 96  MET A SD  1 
ATOM   761  C  CE  . MET A 1 96  ? 8.57700   23.82800  9.87100  1.000 14.17000 ? 96  MET A CE  1 
ATOM   762  N  N   . ASP A 1 97  ? 3.44100   27.06800  10.49200 1.000 15.21000 ? 97  ASP A N   1 
ATOM   763  C  CA  . ASP A 1 97  ? 2.95500   28.40500  10.14000 1.000 16.69000 ? 97  ASP A CA  1 
ATOM   764  C  C   . ASP A 1 97  ? 2.28500   29.06800  11.33900 1.000 16.07000 ? 97  ASP A C   1 
ATOM   765  O  O   . ASP A 1 97  ? 2.54400   30.23800  11.64400 1.000 16.25000 ? 97  ASP A O   1 
ATOM   766  C  CB  . ASP A 1 97  ? 1.96700   28.34100  8.95700  1.000 20.17000 ? 97  ASP A CB  1 
ATOM   767  C  CG  . ASP A 1 97  ? 2.61600   27.92800  7.64900  1.000 18.79000 ? 97  ASP A CG  1 
ATOM   768  O  OD1 . ASP A 1 97  ? 3.85400   27.98700  7.53300  1.000 21.34000 ? 97  ASP A OD1 1 
ATOM   769  O  OD2 . ASP A 1 97  ? 1.87600   27.55800  6.70700  1.000 23.22000 ? 97  ASP A OD2 1 
ATOM   770  N  N   . ALA A 1 98  ? 1.43100   28.32800  12.05100 1.000 15.31000 ? 98  ALA A N   1 
ATOM   771  C  CA  . ALA A 1 98  ? 0.70000   28.94400  13.15800 1.000 17.25000 ? 98  ALA A CA  1 
ATOM   772  C  C   . ALA A 1 98  ? 1.64100   29.38000  14.27500 1.000 16.37000 ? 98  ALA A C   1 
ATOM   773  O  O   . ALA A 1 98  ? 1.34600   30.33600  14.99600 1.000 15.93000 ? 98  ALA A O   1 
ATOM   774  C  CB  . ALA A 1 98  ? -0.35300  27.97700  13.70200 1.000 16.19000 ? 98  ALA A CB  1 
ATOM   775  N  N   . ASN A 1 99  ? 2.77000   28.69600  14.43300 1.000 16.41000 ? 99  ASN A N   1 
ATOM   776  C  CA  . ASN A 1 99  ? 3.76800   29.01600  15.44800 1.000 15.27000 ? 99  ASN A CA  1 
ATOM   777  C  C   . ASN A 1 99  ? 4.85300   29.96400  14.93900 1.000 16.68000 ? 99  ASN A C   1 
ATOM   778  O  O   . ASN A 1 99  ? 5.78000   30.29400  15.68700 1.000 17.22000 ? 99  ASN A O   1 
ATOM   779  C  CB  . ASN A 1 99  ? 4.40100   27.71300  15.95100 1.000 15.58000 ? 99  ASN A CB  1 
ATOM   780  C  CG  . ASN A 1 99  ? 5.09900   27.86700  17.29200 1.000 16.04000 ? 99  ASN A CG  1 
ATOM   781  O  OD1 . ASN A 1 99  ? 4.68100   28.65800  18.14200 1.000 14.31000 ? 99  ASN A OD1 1 
ATOM   782  N  ND2 . ASN A 1 99  ? 6.17300   27.11100  17.48500 1.000 14.13000 ? 99  ASN A ND2 1 
ATOM   783  N  N   . GLY A 1 100 ? 4.77300   30.40400  13.69000 1.000 13.98000 ? 100 GLY A N   1 
ATOM   784  C  CA  . GLY A 1 100 ? 5.78200   31.29900  13.15700 1.000 15.34000 ? 100 GLY A CA  1 
ATOM   785  C  C   . GLY A 1 100 ? 7.10900   30.64000  12.85900 1.000 18.93000 ? 100 GLY A C   1 
ATOM   786  O  O   . GLY A 1 100 ? 8.11900   31.33500  12.74100 1.000 19.12000 ? 100 GLY A O   1 
ATOM   787  N  N   . THR A 1 101 ? 7.13300   29.31700  12.72600 1.000 14.60000 ? 101 THR A N   1 
ATOM   788  C  CA  . THR A 1 101 ? 8.37700   28.56200  12.58100 1.000 15.37000 ? 101 THR A CA  1 
ATOM   789  C  C   . THR A 1 101 ? 8.68900   28.35200  11.10600 1.000 17.63000 ? 101 THR A C   1 
ATOM   790  O  O   . THR A 1 101 ? 7.92600   27.67700  10.39700 1.000 16.73000 ? 101 THR A O   1 
ATOM   791  C  CB  . THR A 1 101 ? 8.26200   27.21000  13.28000 1.000 14.94000 ? 101 THR A CB  1 
ATOM   792  O  OG1 . THR A 1 101 ? 7.92800   27.42300  14.64700 1.000 19.73000 ? 101 THR A OG1 1 
ATOM   793  C  CG2 . THR A 1 101 ? 9.58700   26.44200  13.19700 1.000 17.58000 ? 101 THR A CG2 1 
ATOM   794  N  N   . LEU A 1 102 ? 9.82300   28.91000  10.65300 1.000 14.42000 ? 102 LEU A N   1 
ATOM   795  C  CA  . LEU A 1 102 ? 10.22700  28.75100  9.25600  1.000 15.27000 ? 102 LEU A CA  1 
ATOM   796  C  C   . LEU A 1 102 ? 10.64400  27.31400  8.95200  1.000 16.31000 ? 102 LEU A C   1 
ATOM   797  O  O   . LEU A 1 102 ? 10.17100  26.71100  7.98000  1.000 15.63000 ? 102 LEU A O   1 
ATOM   798  C  CB  . LEU A 1 102 ? 11.36900  29.71100  8.92500  1.000 15.45000 ? 102 LEU A CB  1 
ATOM   799  C  CG  . LEU A 1 102 ? 11.97100  29.54400  7.52400  1.000 18.89000 ? 102 LEU A CG  1 
ATOM   800  C  CD1 . LEU A 1 102 ? 10.93400  29.80100  6.43400  1.000 15.52000 ? 102 LEU A CD1 1 
ATOM   801  C  CD2 . LEU A 1 102 ? 13.17100  30.47200  7.36300  1.000 15.57000 ? 102 LEU A CD2 1 
ATOM   802  N  N   . ALA A 1 103 ? 11.54600  26.75300  9.75700  1.000 13.27000 ? 103 ALA A N   1 
ATOM   803  C  CA  . ALA A 1 103 ? 12.07000  25.42800  9.47300  1.000 15.42000 ? 103 ALA A CA  1 
ATOM   804  C  C   . ALA A 1 103 ? 12.18000  24.62300  10.76100 1.000 13.77000 ? 103 ALA A C   1 
ATOM   805  O  O   . ALA A 1 103 ? 12.28600  25.17300  11.86400 1.000 14.14000 ? 103 ALA A O   1 
ATOM   806  C  CB  . ALA A 1 103 ? 13.43100  25.51400  8.76000  1.000 16.97000 ? 103 ALA A CB  1 
ATOM   807  N  N   . ALA A 1 104 ? 12.16100  23.29700  10.59600 1.000 15.86000 ? 104 ALA A N   1 
ATOM   808  C  CA  . ALA A 1 104 ? 12.26900  22.34400  11.68900 1.000 11.45000 ? 104 ALA A CA  1 
ATOM   809  C  C   . ALA A 1 104 ? 13.26000  21.24500  11.31000 1.000 12.55000 ? 104 ALA A C   1 
ATOM   810  O  O   . ALA A 1 104 ? 13.58200  21.04100  10.13500 1.000 16.14000 ? 104 ALA A O   1 
ATOM   811  C  CB  . ALA A 1 104 ? 10.89300  21.75000  12.04000 1.000 14.19000 ? 104 ALA A CB  1 
ATOM   812  N  N   . THR A 1 105 ? 13.75300  20.53800  12.32500 1.000 14.06000 ? 105 THR A N   1 
ATOM   813  C  CA  . THR A 1 105 ? 14.80500  19.53500  12.17100 1.000 13.62000 ? 105 THR A CA  1 
ATOM   814  C  C   . THR A 1 105 ? 14.29700  18.25200  12.82400 1.000 13.65000 ? 105 THR A C   1 
ATOM   815  O  O   . THR A 1 105 ? 14.23400  18.16900  14.05400 1.000 14.59000 ? 105 THR A O   1 
ATOM   816  C  CB  . THR A 1 105 ? 16.10400  20.02500  12.82000 1.000 15.04000 ? 105 THR A CB  1 
ATOM   817  O  OG1 . THR A 1 105 ? 16.46500  21.30500  12.27700 1.000 15.89000 ? 105 THR A OG1 1 
ATOM   818  C  CG2 . THR A 1 105 ? 17.24300  19.06700  12.58100 1.000 14.39000 ? 105 THR A CG2 1 
ATOM   819  N  N   . LEU A 1 106 ? 13.94800  17.25000  12.01000 1.000 14.66000 ? 106 LEU A N   1 
ATOM   820  C  CA  . LEU A 1 106 ? 13.10700  16.12800  12.44800 1.000 14.20000 ? 106 LEU A CA  1 
ATOM   821  C  C   . LEU A 1 106 ? 13.91300  14.94300  12.98700 1.000 14.52000 ? 106 LEU A C   1 
ATOM   822  O  O   . LEU A 1 106 ? 14.41000  14.11600  12.21600 1.000 12.69000 ? 106 LEU A O   1 
ATOM   823  C  CB  . LEU A 1 106 ? 12.23200  15.66700  11.28600 1.000 15.71000 ? 106 LEU A CB  1 
ATOM   824  C  CG  . LEU A 1 106 ? 11.23100  16.68400  10.73400 1.000 16.10000 ? 106 LEU A CG  1 
ATOM   825  C  CD1 . LEU A 1 106 ? 10.33000  16.05100  9.68100  1.000 15.22000 ? 106 LEU A CD1 1 
ATOM   826  C  CD2 . LEU A 1 106 ? 10.41300  17.25800  11.86800 1.000 14.71000 ? 106 LEU A CD2 1 
ATOM   827  N  N   . PHE A 1 107 ? 13.95400  14.78900  14.31500 1.000 14.45000 ? 107 PHE A N   1 
ATOM   828  C  CA  . PHE A 1 107 ? 14.53300  13.59600  14.92800 1.000 11.84000 ? 107 PHE A CA  1 
ATOM   829  C  C   . PHE A 1 107 ? 13.53600  12.43100  14.91400 1.000 15.55000 ? 107 PHE A C   1 
ATOM   830  O  O   . PHE A 1 107 ? 12.33500  12.61800  15.13800 1.000 16.60000 ? 107 PHE A O   1 
ATOM   831  C  CB  . PHE A 1 107 ? 14.96700  13.87900  16.37200 1.000 13.22000 ? 107 PHE A CB  1 
ATOM   832  C  CG  . PHE A 1 107 ? 16.26300  14.66100  16.48600 1.000 13.77000 ? 107 PHE A CG  1 
ATOM   833  C  CD1 . PHE A 1 107 ? 16.26600  16.04100  16.41700 1.000 16.44000 ? 107 PHE A CD1 1 
ATOM   834  C  CD2 . PHE A 1 107 ? 17.46600  14.00700  16.66000 1.000 12.52000 ? 107 PHE A CD2 1 
ATOM   835  C  CE1 . PHE A 1 107 ? 17.44800  16.75200  16.51200 1.000 13.69000 ? 107 PHE A CE1 1 
ATOM   836  C  CE2 . PHE A 1 107 ? 18.64300  14.71200  16.76400 1.000 12.64000 ? 107 PHE A CE2 1 
ATOM   837  C  CZ  . PHE A 1 107 ? 18.64100  16.08100  16.68700 1.000 11.59000 ? 107 PHE A CZ  1 
ATOM   838  N  N   . ALA A 1 108 ? 14.05900  11.21900  14.71800 1.000 14.00000 ? 108 ALA A N   1 
ATOM   839  C  CA  . ALA A 1 108 ? 13.25500  10.01800  14.50500 1.000 14.68000 ? 108 ALA A CA  1 
ATOM   840  C  C   . ALA A 1 108 ? 12.52800  9.56600   15.76800 1.000 16.11000 ? 108 ALA A C   1 
ATOM   841  O  O   . ALA A 1 108 ? 12.97400  9.81500   16.89200 1.000 17.00000 ? 108 ALA A O   1 
ATOM   842  C  CB  . ALA A 1 108 ? 14.14900  8.88000   14.02700 1.000 14.76000 ? 108 ALA A CB  1 
ATOM   843  N  N   . THR A 1 109 ? 11.40800  8.85500   15.57400 1.000 14.19000 ? 109 THR A N   1 
ATOM   844  C  CA  . THR A 1 109 ? 10.78000  8.13200   16.68000 1.000 15.86000 ? 109 THR A CA  1 
ATOM   845  C  C   . THR A 1 109 ? 11.06900  6.63100   16.61500 1.000 15.83000 ? 109 THR A C   1 
ATOM   846  O  O   . THR A 1 109 ? 11.82200  6.11600   17.44500 1.000 17.00000 ? 109 THR A O   1 
ATOM   847  C  CB  . THR A 1 109 ? 9.26800   8.37100   16.71200 1.000 19.30000 ? 109 THR A CB  1 
ATOM   848  O  OG1 . THR A 1 109 ? 9.03000   9.72900   17.07500 1.000 19.92000 ? 109 THR A OG1 1 
ATOM   849  C  CG2 . THR A 1 109 ? 8.59500   7.46800   17.74600 1.000 21.67000 ? 109 THR A CG2 1 
ATOM   850  N  N   . PHE A 1 110 ? 10.47500  5.91700   15.65600 1.000 16.17000 ? 110 PHE A N   1 
ATOM   851  C  CA  . PHE A 1 110 ? 10.58400  4.45600   15.64600 1.000 19.75000 ? 110 PHE A CA  1 
ATOM   852  C  C   . PHE A 1 110 ? 12.02000  3.92800   15.70000 1.000 17.24000 ? 110 PHE A C   1 
ATOM   853  O  O   . PHE A 1 110 ? 12.30000  3.06400   16.54600 1.000 17.48000 ? 110 PHE A O   1 
ATOM   854  C  CB  . PHE A 1 110 ? 9.86000   3.86600   14.42900 1.000 16.84000 ? 110 PHE A CB  1 
ATOM   855  C  CG  . PHE A 1 110 ? 10.25100  2.43700   14.15400 1.000 20.39000 ? 110 PHE A CG  1 
ATOM   856  C  CD1 . PHE A 1 110 ? 9.90600   1.43100   15.05100 1.000 21.79000 ? 110 PHE A CD1 1 
ATOM   857  C  CD2 . PHE A 1 110 ? 10.98100  2.10200   13.03400 1.000 20.98000 ? 110 PHE A CD2 1 
ATOM   858  C  CE1 . PHE A 1 110 ? 10.27400  0.11000   14.82100 1.000 20.88000 ? 110 PHE A CE1 1 
ATOM   859  C  CE2 . PHE A 1 110 ? 11.35900  0.77800   12.79900 1.000 25.01000 ? 110 PHE A CE2 1 
ATOM   860  C  CZ  . PHE A 1 110 ? 11.00800  -0.21000  13.69100 1.000 22.66000 ? 110 PHE A CZ  1 
ATOM   861  N  N   . PRO A 1 111 ? 12.97000  4.38300   14.87600 1.000 15.53000 ? 111 PRO A N   1 
ATOM   862  C  CA  . PRO A 1 111 ? 14.33200  3.83800   15.00200 1.000 14.26000 ? 111 PRO A CA  1 
ATOM   863  C  C   . PRO A 1 111 ? 15.07500  4.31700   16.23300 1.000 16.65000 ? 111 PRO A C   1 
ATOM   864  O  O   . PRO A 1 111 ? 16.17500  3.81800   16.48800 1.000 14.58000 ? 111 PRO A O   1 
ATOM   865  C  CB  . PRO A 1 111 ? 15.03000  4.30800   13.71400 1.000 15.37000 ? 111 PRO A CB  1 
ATOM   866  C  CG  . PRO A 1 111 ? 14.28700  5.48000   13.27700 1.000 14.71000 ? 111 PRO A CG  1 
ATOM   867  C  CD  . PRO A 1 111 ? 12.86800  5.35900   13.77500 1.000 15.04000 ? 111 PRO A CD  1 
ATOM   868  N  N   . GLY A 1 112 ? 14.50200  5.23600   17.01600 1.000 14.43000 ? 112 GLY A N   1 
ATOM   869  C  CA  . GLY A 1 112 ? 15.24500  5.91300   18.05900 1.000 16.28000 ? 112 GLY A CA  1 
ATOM   870  C  C   . GLY A 1 112 ? 15.77300  7.20600   17.47800 1.000 17.97000 ? 112 GLY A C   1 
ATOM   871  O  O   . GLY A 1 112 ? 16.18700  7.20800   16.31700 1.000 16.29000 ? 112 GLY A O   1 
ATOM   872  N  N   . PHE A 1 113 ? 15.76300  8.31400   18.23000 1.000 13.83000 ? 113 PHE A N   1 
ATOM   873  C  CA  . PHE A 1 113 ? 16.23300  9.55700   17.62100 1.000 17.59000 ? 113 PHE A CA  1 
ATOM   874  C  C   . PHE A 1 113 ? 17.70400  9.47600   17.22400 1.000 16.69000 ? 113 PHE A C   1 
ATOM   875  O  O   . PHE A 1 113 ? 18.15700  10.28500  16.40600 1.000 16.08000 ? 113 PHE A O   1 
ATOM   876  C  CB  . PHE A 1 113 ? 16.00900  10.74300  18.55800 1.000 18.39000 ? 113 PHE A CB  1 
ATOM   877  C  CG  . PHE A 1 113 ? 16.51500  10.51700  19.94700 1.000 20.65000 ? 113 PHE A CG  1 
ATOM   878  C  CD1 . PHE A 1 113 ? 17.87000  10.62600  20.23500 1.000 22.11000 ? 113 PHE A CD1 1 
ATOM   879  C  CD2 . PHE A 1 113 ? 15.64100  10.19100  20.96600 1.000 26.24000 ? 113 PHE A CD2 1 
ATOM   880  C  CE1 . PHE A 1 113 ? 18.35200  10.40400  21.52100 1.000 26.33000 ? 113 PHE A CE1 1 
ATOM   881  C  CE2 . PHE A 1 113 ? 16.11200  9.96800   22.25900 1.000 30.47000 ? 113 PHE A CE2 1 
ATOM   882  C  CZ  . PHE A 1 113 ? 17.47300  10.07700  22.53200 1.000 27.90000 ? 113 PHE A CZ  1 
ATOM   883  N  N   . ALA A 1 114 ? 18.45100  8.52300   17.78500 1.000 13.86000 ? 114 ALA A N   1 
ATOM   884  C  CA  . ALA A 1 114 ? 19.83600  8.28000   17.39300 1.000 15.46000 ? 114 ALA A CA  1 
ATOM   885  C  C   . ALA A 1 114 ? 20.02200  6.89300   16.79600 1.000 16.43000 ? 114 ALA A C   1 
ATOM   886  O  O   . ALA A 1 114 ? 21.16200  6.42100   16.70200 1.000 18.09000 ? 114 ALA A O   1 
ATOM   887  C  CB  . ALA A 1 114 ? 20.77500  8.46700   18.59000 1.000 16.81000 ? 114 ALA A CB  1 
ATOM   888  N  N   . GLY A 1 115 ? 18.93600  6.22300   16.41100 1.000 15.29000 ? 115 GLY A N   1 
ATOM   889  C  CA  . GLY A 1 115 ? 19.03400  4.92200   15.77200 1.000 14.92000 ? 115 GLY A CA  1 
ATOM   890  C  C   . GLY A 1 115 ? 19.28400  3.74400   16.68900 1.000 14.88000 ? 115 GLY A C   1 
ATOM   891  O  O   . GLY A 1 115 ? 19.49700  2.63500   16.18800 1.000 15.88000 ? 115 GLY A O   1 
ATOM   892  N  N   . THR A 1 116 ? 19.23200  3.92800   18.01200 1.000 16.94000 ? 116 THR A N   1 
ATOM   893  C  CA  . THR A 1 116 ? 19.62200  2.85400   18.92700 1.000 16.32000 ? 116 THR A CA  1 
ATOM   894  C  C   . THR A 1 116 ? 18.61900  1.70300   18.96400 1.000 16.04000 ? 116 THR A C   1 
ATOM   895  O  O   . THR A 1 116 ? 18.99500  0.59600   19.36100 1.000 19.04000 ? 116 THR A O   1 
ATOM   896  C  CB  . THR A 1 116 ? 19.83900  3.37900   20.36300 1.000 15.28000 ? 116 THR A CB  1 
ATOM   897  O  OG1 . THR A 1 116 ? 18.58900  3.73500   20.95800 1.000 20.56000 ? 116 THR A OG1 1 
ATOM   898  C  CG2 . THR A 1 116 ? 20.75800  4.60200   20.39200 1.000 15.20000 ? 116 THR A CG2 1 
ATOM   899  N  N   . HIS A 1 117 ? 17.35900  1.91700   18.58300 1.000 14.04000 ? 117 HIS A N   1 
ATOM   900  C  CA  . HIS A 1 117 ? 16.44200  0.77900   18.56000 1.000 15.16000 ? 117 HIS A CA  1 
ATOM   901  C  C   . HIS A 1 117 ? 16.83800  -0.20400  17.46500 1.000 18.32000 ? 117 HIS A C   1 
ATOM   902  O  O   . HIS A 1 117 ? 16.88900  -1.41400  17.70200 1.000 18.19000 ? 117 HIS A O   1 
ATOM   903  C  CB  . HIS A 1 117 ? 14.99200  1.23100   18.37200 1.000 15.67000 ? 117 HIS A CB  1 
ATOM   904  C  CG  . HIS A 1 117 ? 14.02000  0.08800   18.28700 1.000 21.14000 ? 117 HIS A CG  1 
ATOM   905  N  ND1 . HIS A 1 117 ? 13.93600  -0.89200  19.25300 1.000 19.19000 ? 117 HIS A ND1 1 
ATOM   906  C  CD2 . HIS A 1 117 ? 13.11600  -0.24700  17.33500 1.000 21.29000 ? 117 HIS A CD2 1 
ATOM   907  C  CE1 . HIS A 1 117 ? 13.01800  -1.77600  18.90600 1.000 21.66000 ? 117 HIS A CE1 1 
ATOM   908  N  NE2 . HIS A 1 117 ? 12.50300  -1.40800  17.74700 1.000 23.33000 ? 117 HIS A NE2 1 
ATOM   909  N  N   . LEU A 1 118 ? 17.15600  0.30900   16.27000 1.000 14.44000 ? 118 LEU A N   1 
ATOM   910  C  CA  . LEU A 1 118 ? 17.67500  -0.52900  15.19200 1.000 17.10000 ? 118 LEU A CA  1 
ATOM   911  C  C   . LEU A 1 118 ? 18.99200  -1.19300  15.57200 1.000 18.53000 ? 118 LEU A C   1 
ATOM   912  O  O   . LEU A 1 118 ? 19.24900  -2.33500  15.18100 1.000 19.93000 ? 118 LEU A O   1 
ATOM   913  C  CB  . LEU A 1 118 ? 17.86000  0.31200   13.92700 1.000 16.79000 ? 118 LEU A CB  1 
ATOM   914  C  CG  . LEU A 1 118 ? 16.64600  1.09000   13.40300 1.000 16.42000 ? 118 LEU A CG  1 
ATOM   915  C  CD1 . LEU A 1 118 ? 16.97900  1.72600   12.04700 1.000 17.33000 ? 118 LEU A CD1 1 
ATOM   916  C  CD2 . LEU A 1 118 ? 15.45000  0.17900   13.27200 1.000 18.10000 ? 118 LEU A CD2 1 
ATOM   917  N  N   . ALA A 1 119 ? 19.83700  -0.50600  16.33200 1.000 18.21000 ? 119 ALA A N   1 
ATOM   918  C  CA  . ALA A 1 119 ? 21.13300  -1.07400  16.68200 1.000 19.69000 ? 119 ALA A CA  1 
ATOM   919  C  C   . ALA A 1 119 ? 21.02200  -2.17800  17.72500 1.000 23.27000 ? 119 ALA A C   1 
ATOM   920  O  O   . ALA A 1 119 ? 21.96300  -2.96600  17.88300 1.000 26.84000 ? 119 ALA A O   1 
ATOM   921  C  CB  . ALA A 1 119 ? 22.06200  0.02400   17.19100 1.000 19.52000 ? 119 ALA A CB  1 
ATOM   922  N  N   . SER A 1 120 ? 19.89600  -2.25000  18.43200 1.000 25.51000 ? 120 SER A N   1 
ATOM   923  C  CA  . SER A 1 120 ? 19.68500  -3.24000  19.48100 1.000 27.31000 ? 120 SER A CA  1 
ATOM   924  C  C   . SER A 1 120 ? 19.22200  -4.58900  18.95000 1.000 30.41000 ? 120 SER A C   1 
ATOM   925  O  O   . SER A 1 120 ? 19.16100  -5.55100  19.72500 1.000 27.28000 ? 120 SER A O   1 
ATOM   926  C  CB  . SER A 1 120 ? 18.64700  -2.72600  20.48100 1.000 27.25000 ? 120 SER A CB  1 
ATOM   927  O  OG  . SER A 1 120 ? 17.31800  -2.96700  20.02400 1.000 25.70000 ? 120 SER A OG  1 
ATOM   928  N  N   . LEU A 1 121 ? 18.88600  -4.68400  17.66800 1.000 22.17000 ? 121 LEU A N   1 
ATOM   929  C  CA  . LEU A 1 121 ? 18.19500  -5.84800  17.14700 1.000 24.95000 ? 121 LEU A CA  1 
ATOM   930  C  C   . LEU A 1 121 ? 19.18400  -6.82600  16.52700 1.000 22.29000 ? 121 LEU A C   1 
ATOM   931  O  O   . LEU A 1 121 ? 20.29400  -6.44600  16.13100 1.000 24.75000 ? 121 LEU A O   1 
ATOM   932  C  CB  . LEU A 1 121 ? 17.14500  -5.40700  16.12500 1.000 17.85000 ? 121 LEU A CB  1 
ATOM   933  C  CG  . LEU A 1 121 ? 16.06800  -4.48000  16.71700 1.000 22.89000 ? 121 LEU A CG  1 
ATOM   934  C  CD1 . LEU A 1 121 ? 15.07400  -4.02100  15.66900 1.000 21.13000 ? 121 LEU A CD1 1 
ATOM   935  C  CD2 . LEU A 1 121 ? 15.32300  -5.13500  17.88700 1.000 22.51000 ? 121 LEU A CD2 1 
ATOM   936  N  N   . PRO A 1 122 ? 18.83700  -8.11500  16.45300 1.000 21.32000 ? 122 PRO A N   1 
ATOM   937  C  CA  . PRO A 1 122 ? 19.86000  -9.11900  16.11900 1.000 22.41000 ? 122 PRO A CA  1 
ATOM   938  C  C   . PRO A 1 122 ? 20.18700  -9.23700  14.63700 1.000 23.15000 ? 122 PRO A C   1 
ATOM   939  O  O   . PRO A 1 122 ? 21.31300  -9.60100  14.28100 1.000 24.10000 ? 122 PRO A O   1 
ATOM   940  C  CB  . PRO A 1 122 ? 19.25300  -10.42400 16.65600 1.000 28.82000 ? 122 PRO A CB  1 
ATOM   941  C  CG  . PRO A 1 122 ? 17.80300  -10.19800 16.64400 1.000 23.57000 ? 122 PRO A CG  1 
ATOM   942  C  CD  . PRO A 1 122 ? 17.59100  -8.73700  16.92700 1.000 22.24000 ? 122 PRO A CD  1 
ATOM   943  N  N   . ASP A 1 123 ? 19.22900  -8.97000  13.75700 1.000 20.54000 ? 123 ASP A N   1 
ATOM   944  C  CA  . ASP A 1 123 ? 19.47800  -9.09000  12.32200 1.000 23.41000 ? 123 ASP A CA  1 
ATOM   945  C  C   . ASP A 1 123 ? 19.90400  -7.72000  11.80100 1.000 22.08000 ? 123 ASP A C   1 
ATOM   946  O  O   . ASP A 1 123 ? 19.07100  -6.83200  11.59500 1.000 23.92000 ? 123 ASP A O   1 
ATOM   947  C  CB  . ASP A 1 123 ? 18.24300  -9.62500  11.60900 1.000 22.74000 ? 123 ASP A CB  1 
ATOM   948  C  CG  . ASP A 1 123 ? 18.50100  -9.95800  10.15100 1.000 27.44000 ? 123 ASP A CG  1 
ATOM   949  O  OD1 . ASP A 1 123 ? 19.31700  -9.27100  9.50400  1.000 23.34000 ? 123 ASP A OD1 1 
ATOM   950  O  OD2 . ASP A 1 123 ? 17.86700  -10.90400 9.64400  1.000 28.70000 ? 123 ASP A OD2 1 
ATOM   951  N  N   . LYS A 1 124 ? 21.21200  -7.55000  11.57900 1.000 21.86000 ? 124 LYS A N   1 
ATOM   952  C  CA  . LYS A 1 124 ? 21.72600  -6.24300  11.20200 1.000 19.33000 ? 124 LYS A CA  1 
ATOM   953  C  C   . LYS A 1 124 ? 21.47200  -5.91700  9.73600  1.000 20.18000 ? 124 LYS A C   1 
ATOM   954  O  O   . LYS A 1 124 ? 21.41100  -4.73500  9.37900  1.000 17.53000 ? 124 LYS A O   1 
ATOM   955  C  CB  . LYS A 1 124 ? 23.22100  -6.15800  11.52600 1.000 20.06000 ? 124 LYS A CB  1 
ATOM   956  C  CG  . LYS A 1 124 ? 23.52600  -6.24700  13.02000 1.000 22.10000 ? 124 LYS A CG  1 
ATOM   957  C  CD  . LYS A 1 124 ? 22.72900  -5.21300  13.80700 1.000 27.39000 ? 124 LYS A CD  1 
ATOM   958  C  CE  . LYS A 1 124 ? 23.31400  -4.97000  15.20000 1.000 28.08000 ? 124 LYS A CE  1 
ATOM   959  N  NZ  . LYS A 1 124 ? 23.04100  -6.11400  16.11900 1.000 26.98000 ? 124 LYS A NZ  1 
ATOM   960  N  N   . LYS A 1 125 ? 21.31500  -6.92700  8.87400  1.000 20.69000 ? 125 LYS A N   1 
ATOM   961  C  CA  . LYS A 1 125 ? 20.87200  -6.63400  7.51700  1.000 23.49000 ? 125 LYS A CA  1 
ATOM   962  C  C   . LYS A 1 125 ? 19.46300  -6.05900  7.53100  1.000 20.17000 ? 125 LYS A C   1 
ATOM   963  O  O   . LYS A 1 125 ? 19.16500  -5.11900  6.78400  1.000 19.42000 ? 125 LYS A O   1 
ATOM   964  C  CB  . LYS A 1 125 ? 20.95600  -7.88500  6.64000  1.000 27.23000 ? 125 LYS A CB  1 
ATOM   965  C  CG  . LYS A 1 125 ? 22.39300  -8.39800  6.46200  1.000 33.31000 ? 125 LYS A CG  1 
ATOM   966  C  CD  . LYS A 1 125 ? 22.64700  -8.93400  5.05300  1.000 44.81000 ? 125 LYS A CD  1 
ATOM   967  C  CE  . LYS A 1 125 ? 24.11800  -9.30900  4.82600  1.000 48.51000 ? 125 LYS A CE  1 
ATOM   968  N  NZ  . LYS A 1 125 ? 24.99400  -8.13400  4.53500  1.000 45.94000 ? 125 LYS A NZ  1 
ATOM   969  N  N   . LEU A 1 126 ? 18.59100  -6.59100  8.39800  1.000 17.05000 ? 126 LEU A N   1 
ATOM   970  C  CA  . LEU A 1 126 ? 17.25900  -6.01900  8.54500  1.000 20.24000 ? 126 LEU A CA  1 
ATOM   971  C  C   . LEU A 1 126 ? 17.32300  -4.62600  9.16200  1.000 19.72000 ? 126 LEU A C   1 
ATOM   972  O  O   . LEU A 1 126 ? 16.62700  -3.70900  8.71600  1.000 17.31000 ? 126 LEU A O   1 
ATOM   973  C  CB  . LEU A 1 126 ? 16.38000  -6.93300  9.40100  1.000 18.25000 ? 126 LEU A CB  1 
ATOM   974  C  CG  . LEU A 1 126 ? 15.72200  -8.11400  8.69300  1.000 19.43000 ? 126 LEU A CG  1 
ATOM   975  C  CD1 . LEU A 1 126 ? 14.70100  -8.81100  9.60000  1.000 15.65000 ? 126 LEU A CD1 1 
ATOM   976  C  CD2 . LEU A 1 126 ? 15.08300  -7.64400  7.39800  1.000 19.24000 ? 126 LEU A CD2 1 
ATOM   977  N  N   . SER A 1 127 ? 18.14000  -4.45000  10.19700 1.000 18.72000 ? 127 SER A N   1 
ATOM   978  C  CA  . SER A 1 127 ? 18.24900  -3.12800  10.80100 1.000 17.23000 ? 127 SER A CA  1 
ATOM   979  C  C   . SER A 1 127 ? 18.83700  -2.11900  9.82000  1.000 16.22000 ? 127 SER A C   1 
ATOM   980  O  O   . SER A 1 127 ? 18.41800  -0.95900  9.79200  1.000 16.06000 ? 127 SER A O   1 
ATOM   981  C  CB  . SER A 1 127 ? 19.08000  -3.20300  12.08000 1.000 15.47000 ? 127 SER A CB  1 
ATOM   982  O  OG  . SER A 1 127 ? 18.37100  -3.86700  13.10600 1.000 21.03000 ? 127 SER A OG  1 
ATOM   983  N  N   . LEU A 1 128 ? 19.80500  -2.54300  9.00300  1.000 15.52000 ? 128 LEU A N   1 
ATOM   984  C  CA  . LEU A 1 128 ? 20.37200  -1.64400  8.00100  1.000 16.01000 ? 128 LEU A CA  1 
ATOM   985  C  C   . LEU A 1 128 ? 19.32300  -1.22900  6.97700  1.000 19.50000 ? 128 LEU A C   1 
ATOM   986  O  O   . LEU A 1 128 ? 19.23900  -0.05300  6.59800  1.000 17.92000 ? 128 LEU A O   1 
ATOM   987  C  CB  . LEU A 1 128 ? 21.55700  -2.31800  7.31400  1.000 14.92000 ? 128 LEU A CB  1 
ATOM   988  C  CG  . LEU A 1 128 ? 22.19400  -1.52000  6.18100  1.000 19.60000 ? 128 LEU A CG  1 
ATOM   989  C  CD1 . LEU A 1 128 ? 22.71000  -0.20000  6.71200  1.000 19.82000 ? 128 LEU A CD1 1 
ATOM   990  C  CD2 . LEU A 1 128 ? 23.31700  -2.32000  5.54700  1.000 23.21000 ? 128 LEU A CD2 1 
ATOM   991  N  N   . ALA A 1 129 ? 18.51100  -2.18400  6.51200  1.000 14.62000 ? 129 ALA A N   1 
ATOM   992  C  CA  . ALA A 1 129 ? 17.44700  -1.84500  5.57600  1.000 16.19000 ? 129 ALA A CA  1 
ATOM   993  C  C   . ALA A 1 129 ? 16.48800  -0.83100  6.18100  1.000 15.83000 ? 129 ALA A C   1 
ATOM   994  O  O   . ALA A 1 129 ? 16.04900  0.10200   5.49900  1.000 17.95000 ? 129 ALA A O   1 
ATOM   995  C  CB  . ALA A 1 129 ? 16.69000  -3.10400  5.15900  1.000 17.84000 ? 129 ALA A CB  1 
ATOM   996  N  N   . ALA A 1 130 ? 16.15800  -0.99800  7.46700  1.000 15.92000 ? 130 ALA A N   1 
ATOM   997  C  CA  . ALA A 1 130 ? 15.24400  -0.07000  8.13100  1.000 14.50000 ? 130 ALA A CA  1 
ATOM   998  C  C   . ALA A 1 130 ? 15.87600  1.30900   8.29000  1.000 16.36000 ? 130 ALA A C   1 
ATOM   999  O  O   . ALA A 1 130 ? 15.19000  2.32800   8.18700  1.000 15.11000 ? 130 ALA A O   1 
ATOM   1000 C  CB  . ALA A 1 130 ? 14.83200  -0.62600  9.49800  1.000 14.31000 ? 130 ALA A CB  1 
ATOM   1001 N  N   . CYS A 1 131 ? 17.17900  1.36600   8.54800  1.000 14.71000 ? 131 CYS A N   1 
ATOM   1002 C  CA  . CYS A 1 131 ? 17.83600  2.67100   8.65500  1.000 14.97000 ? 131 CYS A CA  1 
ATOM   1003 C  C   . CYS A 1 131 ? 17.79700  3.40800   7.32200  1.000 14.81000 ? 131 CYS A C   1 
ATOM   1004 O  O   . CYS A 1 131 ? 17.46500  4.59900   7.25700  1.000 15.07000 ? 131 CYS A O   1 
ATOM   1005 C  CB  . CYS A 1 131 ? 19.28200  2.48100   9.13300  1.000 16.01000 ? 131 CYS A CB  1 
ATOM   1006 S  SG  . CYS A 1 131 ? 20.19700  4.01500   9.41800  1.000 17.46000 ? 131 CYS A SG  1 
ATOM   1007 N  N   . ARG A 1 132 ? 18.13400  2.71100   6.23700  1.000 16.95000 ? 132 ARG A N   1 
ATOM   1008 C  CA  . ARG A 1 132 ? 18.13000  3.35800   4.93200  1.000 17.45000 ? 132 ARG A CA  1 
ATOM   1009 C  C   . ARG A 1 132 ? 16.71900  3.76500   4.51500  1.000 16.17000 ? 132 ARG A C   1 
ATOM   1010 O  O   . ARG A 1 132 ? 16.53000  4.83400   3.93400  1.000 12.71000 ? 132 ARG A O   1 
ATOM   1011 C  CB  . ARG A 1 132 ? 18.78400  2.44000   3.89700  1.000 14.37000 ? 132 ARG A CB  1 
ATOM   1012 C  CG  . ARG A 1 132 ? 20.27900  2.24200   4.16600  1.000 14.35000 ? 132 ARG A CG  1 
ATOM   1013 C  CD  . ARG A 1 132 ? 21.00200  1.83200   2.92900  1.000 24.76000 ? 132 ARG A CD  1 
ATOM   1014 N  NE  . ARG A 1 132 ? 20.80700  0.41500   2.67900  1.000 27.38000 ? 132 ARG A NE  1 
ATOM   1015 C  CZ  . ARG A 1 132 ? 21.78700  -0.44100  2.41900  1.000 26.52000 ? 132 ARG A CZ  1 
ATOM   1016 N  NH1 . ARG A 1 132 ? 23.04000  -0.01600  2.35000  1.000 23.25000 ? 132 ARG A NH1 1 
ATOM   1017 N  NH2 . ARG A 1 132 ? 21.50100  -1.71600  2.20900  1.000 26.77000 ? 132 ARG A NH2 1 
ATOM   1018 N  N   . ALA A 1 133 ? 15.71000  2.94100   4.81600  1.000 16.55000 ? 133 ALA A N   1 
ATOM   1019 C  CA  . ALA A 1 133 ? 14.35000  3.31400   4.44700  1.000 15.74000 ? 133 ALA A CA  1 
ATOM   1020 C  C   . ALA A 1 133 ? 13.90200  4.54900   5.21300  1.000 17.16000 ? 133 ALA A C   1 
ATOM   1021 O  O   . ALA A 1 133 ? 13.26300  5.44400   4.64700  1.000 15.50000 ? 133 ALA A O   1 
ATOM   1022 C  CB  . ALA A 1 133 ? 13.38700  2.15000   4.71000  1.000 14.62000 ? 133 ALA A CB  1 
ATOM   1023 N  N   . PHE A 1 134 ? 14.22400  4.60800   6.50600  1.000 13.03000 ? 134 PHE A N   1 
ATOM   1024 C  CA  . PHE A 1 134 ? 13.90600  5.79900   7.27800  1.000 13.87000 ? 134 PHE A CA  1 
ATOM   1025 C  C   . PHE A 1 134 ? 14.58400  7.03200   6.69300  1.000 13.24000 ? 134 PHE A C   1 
ATOM   1026 O  O   . PHE A 1 134 ? 13.94400  8.07300   6.51200  1.000 13.77000 ? 134 PHE A O   1 
ATOM   1027 C  CB  . PHE A 1 134 ? 14.31100  5.62800   8.73500  1.000 15.79000 ? 134 PHE A CB  1 
ATOM   1028 C  CG  . PHE A 1 134 ? 14.16700  6.88700   9.50900  1.000 15.73000 ? 134 PHE A CG  1 
ATOM   1029 C  CD1 . PHE A 1 134 ? 12.92100  7.31100   9.92400  1.000 15.79000 ? 134 PHE A CD1 1 
ATOM   1030 C  CD2 . PHE A 1 134 ? 15.26300  7.69600   9.73900  1.000 17.82000 ? 134 PHE A CD2 1 
ATOM   1031 C  CE1 . PHE A 1 134 ? 12.77000  8.50600   10.60000 1.000 16.86000 ? 134 PHE A CE1 1 
ATOM   1032 C  CE2 . PHE A 1 134 ? 15.12200  8.87600   10.42500 1.000 16.53000 ? 134 PHE A CE2 1 
ATOM   1033 C  CZ  . PHE A 1 134 ? 13.86700  9.28800   10.83700 1.000 15.18000 ? 134 PHE A CZ  1 
ATOM   1034 N  N   . ASN A 1 135 ? 15.87900  6.93400   6.38400  1.000 15.02000 ? 135 ASN A N   1 
ATOM   1035 C  CA  . ASN A 1 135 ? 16.58100  8.08900   5.83000  1.000 12.76000 ? 135 ASN A CA  1 
ATOM   1036 C  C   . ASN A 1 135 ? 15.99300  8.50700   4.48900  1.000 11.61000 ? 135 ASN A C   1 
ATOM   1037 O  O   . ASN A 1 135 ? 15.82300  9.70100   4.23400  1.000 13.68000 ? 135 ASN A O   1 
ATOM   1038 C  CB  . ASN A 1 135 ? 18.08000  7.79700   5.69200  1.000 12.56000 ? 135 ASN A CB  1 
ATOM   1039 C  CG  . ASN A 1 135 ? 18.81600  7.87400   7.01200  1.000 12.32000 ? 135 ASN A CG  1 
ATOM   1040 O  OD1 . ASN A 1 135 ? 18.38300  8.56300   7.94200  1.000 14.24000 ? 135 ASN A OD1 1 
ATOM   1041 N  ND2 . ASN A 1 135 ? 19.95200  7.19000   7.09900  1.000 12.50000 ? 135 ASN A ND2 1 
ATOM   1042 N  N   . ASP A 1 136 ? 15.67700  7.53900   3.61700  1.000 13.19000 ? 136 ASP A N   1 
ATOM   1043 C  CA  . ASP A 1 136 ? 15.01500  7.86200   2.35300  1.000 12.95000 ? 136 ASP A CA  1 
ATOM   1044 C  C   . ASP A 1 136 ? 13.77300  8.71200   2.58200  1.000 14.97000 ? 136 ASP A C   1 
ATOM   1045 O  O   . ASP A 1 136 ? 13.49000  9.63400   1.81300  1.000 14.53000 ? 136 ASP A O   1 
ATOM   1046 C  CB  . ASP A 1 136 ? 14.64300  6.57700   1.60500  1.000 18.51000 ? 136 ASP A CB  1 
ATOM   1047 C  CG  . ASP A 1 136 ? 15.84700  5.92000   0.93100  1.000 20.34000 ? 136 ASP A CG  1 
ATOM   1048 O  OD1 . ASP A 1 136 ? 16.93900  6.52600   0.93200  1.000 16.63000 ? 136 ASP A OD1 1 
ATOM   1049 O  OD2 . ASP A 1 136 ? 15.70400  4.79300   0.40800  1.000 18.96000 ? 136 ASP A OD2 1 
ATOM   1050 N  N   . TRP A 1 137 ? 13.01600  8.41300   3.63400  1.000 16.22000 ? 137 TRP A N   1 
ATOM   1051 C  CA  . TRP A 1 137 ? 11.80900  9.18300   3.91100  1.000 14.86000 ? 137 TRP A CA  1 
ATOM   1052 C  C   . TRP A 1 137 ? 12.12900  10.54900  4.52100  1.000 14.82000 ? 137 TRP A C   1 
ATOM   1053 O  O   . TRP A 1 137 ? 11.65400  11.57800  4.03300  1.000 16.72000 ? 137 TRP A O   1 
ATOM   1054 C  CB  . TRP A 1 137 ? 10.88700  8.39900   4.83900  1.000 16.12000 ? 137 TRP A CB  1 
ATOM   1055 C  CG  . TRP A 1 137 ? 9.65000   9.17200   5.15900  1.000 17.32000 ? 137 TRP A CG  1 
ATOM   1056 C  CD1 . TRP A 1 137 ? 8.59900   9.42500   4.31300  1.000 18.47000 ? 137 TRP A CD1 1 
ATOM   1057 C  CD2 . TRP A 1 137 ? 9.33700   9.83300   6.39600  1.000 16.68000 ? 137 TRP A CD2 1 
ATOM   1058 N  NE1 . TRP A 1 137 ? 7.65500   10.18300  4.95700  1.000 19.42000 ? 137 TRP A NE1 1 
ATOM   1059 C  CE2 . TRP A 1 137 ? 8.08100   10.44400  6.23400  1.000 15.71000 ? 137 TRP A CE2 1 
ATOM   1060 C  CE3 . TRP A 1 137 ? 9.99600   9.95400   7.62800  1.000 17.49000 ? 137 TRP A CE3 1 
ATOM   1061 C  CZ2 . TRP A 1 137 ? 7.46900   11.17900  7.24900  1.000 16.10000 ? 137 TRP A CZ2 1 
ATOM   1062 C  CZ3 . TRP A 1 137 ? 9.38100   10.67900  8.64000  1.000 20.30000 ? 137 TRP A CZ3 1 
ATOM   1063 C  CH2 . TRP A 1 137 ? 8.12900   11.27600  8.44100  1.000 17.34000 ? 137 TRP A CH2 1 
ATOM   1064 N  N   . VAL A 1 138 ? 12.91700  10.57900  5.60000  1.000 13.73000 ? 138 VAL A N   1 
ATOM   1065 C  CA  . VAL A 1 138 ? 13.04300  11.81200  6.37300  1.000 13.55000 ? 138 VAL A CA  1 
ATOM   1066 C  C   . VAL A 1 138 ? 14.09700  12.73600  5.78400  1.000 15.85000 ? 138 VAL A C   1 
ATOM   1067 O  O   . VAL A 1 138 ? 14.03300  13.95600  5.98100  1.000 15.44000 ? 138 VAL A O   1 
ATOM   1068 C  CB  . VAL A 1 138 ? 13.34900  11.49700  7.84900  1.000 15.66000 ? 138 VAL A CB  1 
ATOM   1069 C  CG1 . VAL A 1 138 ? 14.84300  11.24400  8.05000  1.000 13.63000 ? 138 VAL A CG1 1 
ATOM   1070 C  CG2 . VAL A 1 138 ? 12.91200  12.64300  8.72700  1.000 16.40000 ? 138 VAL A CG2 1 
ATOM   1071 N  N   . VAL A 1 139 ? 15.08200  12.19400  5.07600  1.000 13.05000 ? 139 VAL A N   1 
ATOM   1072 C  CA  . VAL A 1 139 ? 16.08600  13.04100  4.43900  1.000 15.12000 ? 139 VAL A CA  1 
ATOM   1073 C  C   . VAL A 1 139 ? 15.67600  13.39500  3.01600  1.000 16.87000 ? 139 VAL A C   1 
ATOM   1074 O  O   . VAL A 1 139 ? 15.80600  14.54400  2.58900  1.000 19.41000 ? 139 VAL A O   1 
ATOM   1075 C  CB  . VAL A 1 139 ? 17.46200  12.35200  4.46900  1.000 15.42000 ? 139 VAL A CB  1 
ATOM   1076 C  CG1 . VAL A 1 139 ? 18.45500  13.10600  3.55200  1.000 14.91000 ? 139 VAL A CG1 1 
ATOM   1077 C  CG2 . VAL A 1 139 ? 17.98900  12.28700  5.88100  1.000 15.03000 ? 139 VAL A CG2 1 
ATOM   1078 N  N   . GLY A 1 140 ? 15.15900  12.42400  2.27200  1.000 15.10000 ? 140 GLY A N   1 
ATOM   1079 C  CA  . GLY A 1 140 ? 14.79600  12.66200  0.89000  1.000 21.95000 ? 140 GLY A CA  1 
ATOM   1080 C  C   . GLY A 1 140 ? 13.38600  13.17100  0.69400  1.000 23.65000 ? 140 GLY A C   1 
ATOM   1081 O  O   . GLY A 1 140 ? 13.18200  14.30400  0.23500  1.000 28.25000 ? 140 GLY A O   1 
ATOM   1082 N  N   . GLU A 1 141 ? 12.40400  12.34700  1.05700  1.000 15.70000 ? 141 GLU A N   1 
ATOM   1083 C  CA  . GLU A 1 141 ? 11.02400  12.62900  0.67500  1.000 18.52000 ? 141 GLU A CA  1 
ATOM   1084 C  C   . GLU A 1 141 ? 10.49500  13.88300  1.36500  1.000 20.40000 ? 141 GLU A C   1 
ATOM   1085 O  O   . GLU A 1 141 ? 9.98900   14.79600  0.70000  1.000 20.80000 ? 141 GLU A O   1 
ATOM   1086 C  CB  . GLU A 1 141 ? 10.13000  11.42700  0.98400  1.000 19.61000 ? 141 GLU A CB  1 
ATOM   1087 C  CG  . GLU A 1 141 ? 8.66600   11.64400  0.56700  1.000 22.20000 ? 141 GLU A CG  1 
ATOM   1088 C  CD  . GLU A 1 141 ? 7.80100   10.40700  0.73800  1.000 27.96000 ? 141 GLU A CD  1 
ATOM   1089 O  OE1 . GLU A 1 141 ? 8.35900   9.29800   0.79500  1.000 24.91000 ? 141 GLU A OE1 1 
ATOM   1090 O  OE2 . GLU A 1 141 ? 6.55800   10.54900  0.82800  1.000 30.47000 ? 141 GLU A OE2 1 
ATOM   1091 N  N   . VAL A 1 142 ? 10.59200  13.94800  2.69300  1.000 16.72000 ? 142 VAL A N   1 
ATOM   1092 C  CA  . VAL A 1 142 ? 9.95000   15.02600  3.45000  1.000 17.18000 ? 142 VAL A CA  1 
ATOM   1093 C  C   . VAL A 1 142 ? 10.52100  16.39500  3.08100  1.000 18.54000 ? 142 VAL A C   1 
ATOM   1094 O  O   . VAL A 1 142 ? 9.74400   17.28100  2.69700  1.000 17.77000 ? 142 VAL A O   1 
ATOM   1095 C  CB  . VAL A 1 142 ? 10.04400  14.77800  4.96300  1.000 14.33000 ? 142 VAL A CB  1 
ATOM   1096 C  CG1 . VAL A 1 142 ? 9.57000   16.02300  5.74100  1.000 14.92000 ? 142 VAL A CG1 1 
ATOM   1097 C  CG2 . VAL A 1 142 ? 9.20000   13.56900  5.34000  1.000 17.19000 ? 142 VAL A CG2 1 
ATOM   1098 N  N   . PRO A 1 143 ? 11.83900  16.63700  3.16400  1.000 18.64000 ? 143 PRO A N   1 
ATOM   1099 C  CA  . PRO A 1 143 ? 12.33400  17.98000  2.81100  1.000 21.27000 ? 143 PRO A CA  1 
ATOM   1100 C  C   . PRO A 1 143 ? 12.02300  18.37900  1.37600  1.000 22.19000 ? 143 PRO A C   1 
ATOM   1101 O  O   . PRO A 1 143 ? 11.83100  19.56900  1.10800  1.000 22.57000 ? 143 PRO A O   1 
ATOM   1102 C  CB  . PRO A 1 143 ? 13.85100  17.87900  3.05800  1.000 19.12000 ? 143 PRO A CB  1 
ATOM   1103 C  CG  . PRO A 1 143 ? 14.01100  16.74700  4.02000  1.000 16.68000 ? 143 PRO A CG  1 
ATOM   1104 C  CD  . PRO A 1 143 ? 12.95500  15.75400  3.55700  1.000 17.13000 ? 143 PRO A CD  1 
ATOM   1105 N  N   . ASP A 1 144 ? 11.96300  17.42100  0.44400  1.000 21.94000 ? 144 ASP A N   1 
ATOM   1106 C  CA  . ASP A 1 144 ? 11.65700  17.75300  -0.94400 1.000 19.58000 ? 144 ASP A CA  1 
ATOM   1107 C  C   . ASP A 1 144 ? 10.16800  18.03900  -1.14600 1.000 25.18000 ? 144 ASP A C   1 
ATOM   1108 O  O   . ASP A 1 144 ? 9.80000   18.78900  -2.05500 1.000 20.76000 ? 144 ASP A O   1 
ATOM   1109 C  CB  . ASP A 1 144 ? 12.10900  16.61800  -1.87800 1.000 28.83000 ? 144 ASP A CB  1 
ATOM   1110 C  CG  . ASP A 1 144 ? 13.62500  16.63400  -2.17100 1.000 36.81000 ? 144 ASP A CG  1 
ATOM   1111 O  OD1 . ASP A 1 144 ? 14.35400  17.56400  -1.74100 1.000 33.90000 ? 144 ASP A OD1 1 
ATOM   1112 O  OD2 . ASP A 1 144 ? 14.08600  15.69400  -2.85300 1.000 47.14000 ? 144 ASP A OD2 1 
ATOM   1113 N  N   . ALA A 1 145 ? 9.29300   17.45500  -0.32100 1.000 22.14000 ? 145 ALA A N   1 
ATOM   1114 C  CA  . ALA A 1 145 ? 7.87200   17.75900  -0.42400 1.000 21.14000 ? 145 ALA A CA  1 
ATOM   1115 C  C   . ALA A 1 145 ? 7.53000   19.11700  0.17100  1.000 23.50000 ? 145 ALA A C   1 
ATOM   1116 O  O   . ALA A 1 145 ? 6.49900   19.69100  -0.19800 1.000 20.20000 ? 145 ALA A O   1 
ATOM   1117 C  CB  . ALA A 1 145 ? 7.03600   16.67800  0.26000  1.000 21.47000 ? 145 ALA A CB  1 
ATOM   1118 N  N   . HIS A 1 146 ? 8.38300   19.65600  1.05000  1.000 16.33000 ? 146 HIS A N   1 
ATOM   1119 C  CA  . HIS A 1 146 ? 8.14400   20.93700  1.71700  1.000 18.51000 ? 146 HIS A CA  1 
ATOM   1120 C  C   . HIS A 1 146 ? 9.40800   21.79000  1.68000  1.000 24.36000 ? 146 HIS A C   1 
ATOM   1121 O  O   . HIS A 1 146 ? 10.04800  22.02800  2.71300  1.000 20.24000 ? 146 HIS A O   1 
ATOM   1122 C  CB  . HIS A 1 146 ? 7.67200   20.69700  3.15000  1.000 19.43000 ? 146 HIS A CB  1 
ATOM   1123 C  CG  . HIS A 1 146 ? 6.48400   19.79700  3.23300  1.000 21.65000 ? 146 HIS A CG  1 
ATOM   1124 N  ND1 . HIS A 1 146 ? 5.20200   20.24100  2.98800  1.000 22.11000 ? 146 HIS A ND1 1 
ATOM   1125 C  CD2 . HIS A 1 146 ? 6.38000   18.47700  3.51300  1.000 21.29000 ? 146 HIS A CD2 1 
ATOM   1126 C  CE1 . HIS A 1 146 ? 4.35800   19.23400  3.12300  1.000 20.94000 ? 146 HIS A CE1 1 
ATOM   1127 N  NE2 . HIS A 1 146 ? 5.04800   18.15000  3.43500  1.000 22.06000 ? 146 HIS A NE2 1 
ATOM   1128 N  N   . PRO A 1 147 ? 9.77300   22.30000  0.50100  1.000 24.69000 ? 147 PRO A N   1 
ATOM   1129 C  CA  . PRO A 1 147 ? 11.06600  22.97900  0.35000  1.000 20.26000 ? 147 PRO A CA  1 
ATOM   1130 C  C   . PRO A 1 147 ? 11.18900  24.16900  1.28600  1.000 20.01000 ? 147 PRO A C   1 
ATOM   1131 O  O   . PRO A 1 147 ? 10.28600  25.00400  1.38100  1.000 25.22000 ? 147 PRO A O   1 
ATOM   1132 C  CB  . PRO A 1 147 ? 11.05700  23.42100  -1.11800 1.000 22.43000 ? 147 PRO A CB  1 
ATOM   1133 C  CG  . PRO A 1 147 ? 10.11300  22.49600  -1.78900 1.000 24.24000 ? 147 PRO A CG  1 
ATOM   1134 C  CD  . PRO A 1 147 ? 9.03000   22.25200  -0.77000 1.000 24.68000 ? 147 PRO A CD  1 
ATOM   1135 N  N   . GLY A 1 148 ? 12.31000  24.23100  1.99100  1.000 19.69000 ? 148 GLY A N   1 
ATOM   1136 C  CA  . GLY A 1 148 ? 12.57300  25.31400  2.90600  1.000 20.33000 ? 148 GLY A CA  1 
ATOM   1137 C  C   . GLY A 1 148 ? 12.00500  25.13300  4.29500  1.000 16.20000 ? 148 GLY A C   1 
ATOM   1138 O  O   . GLY A 1 148 ? 12.26800  25.97200  5.16000  1.000 19.96000 ? 148 GLY A O   1 
ATOM   1139 N  N   . ARG A 1 149 ? 11.23600  24.07100  4.54200  1.000 14.92000 ? 149 ARG A N   1 
ATOM   1140 C  CA  . ARG A 1 149 ? 10.61100  23.88300  5.84300  1.000 19.96000 ? 149 ARG A CA  1 
ATOM   1141 C  C   . ARG A 1 149 ? 11.32400  22.86900  6.72600  1.000 15.53000 ? 149 ARG A C   1 
ATOM   1142 O  O   . ARG A 1 149 ? 11.07500  22.84900  7.93000  1.000 14.16000 ? 149 ARG A O   1 
ATOM   1143 C  CB  . ARG A 1 149 ? 9.14300   23.44800  5.68700  1.000 18.21000 ? 149 ARG A CB  1 
ATOM   1144 C  CG  . ARG A 1 149 ? 8.24100   24.37400  4.86300  1.000 17.67000 ? 149 ARG A CG  1 
ATOM   1145 C  CD  . ARG A 1 149 ? 8.42400   25.86800  5.15100  1.000 16.56000 ? 149 ARG A CD  1 
ATOM   1146 N  NE  . ARG A 1 149 ? 8.02000   26.27700  6.49300  1.000 16.40000 ? 149 ARG A NE  1 
ATOM   1147 C  CZ  . ARG A 1 149 ? 6.78500   26.64000  6.83700  1.000 20.35000 ? 149 ARG A CZ  1 
ATOM   1148 N  NH1 . ARG A 1 149 ? 5.79800   26.61400  5.95000  1.000 19.59000 ? 149 ARG A NH1 1 
ATOM   1149 N  NH2 . ARG A 1 149 ? 6.52700   27.01900  8.07600  1.000 14.79000 ? 149 ARG A NH2 1 
ATOM   1150 N  N   . PHE A 1 150 ? 12.19300  22.02500  6.17800  1.000 13.94000 ? 150 PHE A N   1 
ATOM   1151 C  CA  . PHE A 1 150 ? 12.83500  21.00200  6.99400  1.000 13.96000 ? 150 PHE A CA  1 
ATOM   1152 C  C   . PHE A 1 150 ? 14.32600  20.93600  6.70100  1.000 17.69000 ? 150 PHE A C   1 
ATOM   1153 O  O   . PHE A 1 150 ? 14.72200  20.81000  5.53900  1.000 13.47000 ? 150 PHE A O   1 
ATOM   1154 C  CB  . PHE A 1 150 ? 12.17600  19.64600  6.74900  1.000 15.51000 ? 150 PHE A CB  1 
ATOM   1155 C  CG  . PHE A 1 150 ? 10.73600  19.61500  7.17300  1.000 19.60000 ? 150 PHE A CG  1 
ATOM   1156 C  CD1 . PHE A 1 150 ? 10.40200  19.62800  8.52200  1.000 15.89000 ? 150 PHE A CD1 1 
ATOM   1157 C  CD2 . PHE A 1 150 ? 9.71600   19.60900  6.22800  1.000 17.29000 ? 150 PHE A CD2 1 
ATOM   1158 C  CE1 . PHE A 1 150 ? 9.08600   19.63100  8.92000  1.000 14.89000 ? 150 PHE A CE1 1 
ATOM   1159 C  CE2 . PHE A 1 150 ? 8.38500   19.59200  6.62600  1.000 15.86000 ? 150 PHE A CE2 1 
ATOM   1160 C  CZ  . PHE A 1 150 ? 8.07300   19.61000  7.97500  1.000 16.65000 ? 150 PHE A CZ  1 
ATOM   1161 N  N   . ILE A 1 151 ? 15.13800  21.04100  7.75200  1.000 13.90000 ? 151 ILE A N   1 
ATOM   1162 C  CA  . ILE A 1 151 ? 16.58500  20.86300  7.65800  1.000 13.70000 ? 151 ILE A CA  1 
ATOM   1163 C  C   . ILE A 1 151 ? 16.85700  19.36400  7.69100  1.000 15.72000 ? 151 ILE A C   1 
ATOM   1164 O  O   . ILE A 1 151 ? 16.53900  18.69800  8.69300  1.000 15.29000 ? 151 ILE A O   1 
ATOM   1165 C  CB  . ILE A 1 151 ? 17.32200  21.58800  8.79700  1.000 13.53000 ? 151 ILE A CB  1 
ATOM   1166 C  CG1 . ILE A 1 151 ? 17.04100  23.08500  8.76600  1.000 14.77000 ? 151 ILE A CG1 1 
ATOM   1167 C  CG2 . ILE A 1 151 ? 18.84300  21.37200  8.68800  1.000 14.52000 ? 151 ILE A CG2 1 
ATOM   1168 C  CD1 . ILE A 1 151 ? 17.81800  23.84700  9.80300  1.000 18.24000 ? 151 ILE A CD1 1 
ATOM   1169 N  N   . PRO A 1 152 ? 17.42700  18.79500  6.62900  1.000 13.05000 ? 152 PRO A N   1 
ATOM   1170 C  CA  . PRO A 1 152 ? 17.59000  17.33200  6.54000  1.000 13.80000 ? 152 PRO A CA  1 
ATOM   1171 C  C   . PRO A 1 152 ? 18.56400  16.79600  7.58400  1.000 16.57000 ? 152 PRO A C   1 
ATOM   1172 O  O   . PRO A 1 152 ? 19.73600  17.18900  7.63300  1.000 14.54000 ? 152 PRO A O   1 
ATOM   1173 C  CB  . PRO A 1 152 ? 18.12100  17.12100  5.11600  1.000 14.57000 ? 152 PRO A CB  1 
ATOM   1174 C  CG  . PRO A 1 152 ? 17.67000  18.35900  4.35600  1.000 18.41000 ? 152 PRO A CG  1 
ATOM   1175 C  CD  . PRO A 1 152 ? 17.74700  19.47700  5.36100  1.000 13.78000 ? 152 PRO A CD  1 
ATOM   1176 N  N   . ILE A 1 153 ? 18.08100  15.86000  8.39500  1.000 13.22000 ? 153 ILE A N   1 
ATOM   1177 C  CA  . ILE A 1 153 ? 18.89000  15.19700  9.40800  1.000 9.54000  ? 153 ILE A CA  1 
ATOM   1178 C  C   . ILE A 1 153 ? 18.56400  13.70400  9.35800  1.000 15.13000 ? 153 ILE A C   1 
ATOM   1179 O  O   . ILE A 1 153 ? 17.40100  13.31800  9.22700  1.000 13.86000 ? 153 ILE A O   1 
ATOM   1180 C  CB  . ILE A 1 153 ? 18.63000  15.81000  10.80500 1.000 12.31000 ? 153 ILE A CB  1 
ATOM   1181 C  CG1 . ILE A 1 153 ? 19.41900  15.08100  11.89600 1.000 14.94000 ? 153 ILE A CG1 1 
ATOM   1182 C  CG2 . ILE A 1 153 ? 17.13000  15.78400  11.15700 1.000 12.57000 ? 153 ILE A CG2 1 
ATOM   1183 C  CD1 . ILE A 1 153 ? 19.40900  15.85300  13.23600 1.000 12.29000 ? 153 ILE A CD1 1 
ATOM   1184 N  N   . GLY A 1 154 ? 19.58900  12.85700  9.42100  1.000 14.41000 ? 154 GLY A N   1 
ATOM   1185 C  CA  . GLY A 1 154 ? 19.34000  11.42500  9.37900  1.000 14.14000 ? 154 GLY A CA  1 
ATOM   1186 C  C   . GLY A 1 154 ? 19.98000  10.66500  10.52700 1.000 14.40000 ? 154 GLY A C   1 
ATOM   1187 O  O   . GLY A 1 154 ? 20.53000  11.27700  11.44600 1.000 14.23000 ? 154 GLY A O   1 
ATOM   1188 N  N   . ILE A 1 155 ? 19.92100  9.33400   10.48200 1.000 14.69000 ? 155 ILE A N   1 
ATOM   1189 C  CA  . ILE A 1 155 ? 20.58400  8.47900   11.45700 1.000 14.05000 ? 155 ILE A CA  1 
ATOM   1190 C  C   . ILE A 1 155 ? 21.51900  7.53800   10.69200 1.000 12.34000 ? 155 ILE A C   1 
ATOM   1191 O  O   . ILE A 1 155 ? 21.49800  7.48000   9.46500  1.000 11.80000 ? 155 ILE A O   1 
ATOM   1192 C  CB  . ILE A 1 155 ? 19.58500  7.69100   12.32000 1.000 12.98000 ? 155 ILE A CB  1 
ATOM   1193 C  CG1 . ILE A 1 155 ? 18.54600  7.00300   11.42700 1.000 14.49000 ? 155 ILE A CG1 1 
ATOM   1194 C  CG2 . ILE A 1 155 ? 18.88000  8.61300   13.32900 1.000 13.21000 ? 155 ILE A CG2 1 
ATOM   1195 C  CD1 . ILE A 1 155 ? 17.81500  5.88700   12.09600 1.000 14.25000 ? 155 ILE A CD1 1 
ATOM   1196 N  N   . ILE A 1 156 ? 22.35100  6.81000   11.43000 1.000 10.98000 ? 156 ILE A N   1 
ATOM   1197 C  CA  . ILE A 1 156 ? 23.29600  5.89100   10.79500 1.000 11.24000 ? 156 ILE A CA  1 
ATOM   1198 C  C   . ILE A 1 156 ? 23.19800  4.52000   11.45100 1.000 13.97000 ? 156 ILE A C   1 
ATOM   1199 O  O   . ILE A 1 156 ? 22.78200  4.38900   12.61200 1.000 14.49000 ? 156 ILE A O   1 
ATOM   1200 C  CB  . ILE A 1 156 ? 24.75200  6.42000   10.85300 1.000 13.46000 ? 156 ILE A CB  1 
ATOM   1201 C  CG1 . ILE A 1 156 ? 25.16500  6.83700   12.27800 1.000 12.19000 ? 156 ILE A CG1 1 
ATOM   1202 C  CG2 . ILE A 1 156 ? 24.99000  7.52000   9.79900  1.000 13.43000 ? 156 ILE A CG2 1 
ATOM   1203 C  CD1 . ILE A 1 156 ? 26.72600  6.89500   12.48300 1.000 10.35000 ? 156 ILE A CD1 1 
ATOM   1204 N  N   . PRO A 1 157 ? 23.61100  3.45600   10.71800 1.000 16.20000 ? 157 PRO A N   1 
ATOM   1205 C  CA  . PRO A 1 157 ? 23.75600  2.10500   11.29900 1.000 14.94000 ? 157 PRO A CA  1 
ATOM   1206 C  C   . PRO A 1 157 ? 25.05100  1.98800   12.09200 1.000 16.34000 ? 157 PRO A C   1 
ATOM   1207 O  O   . PRO A 1 157 ? 25.99200  1.28800   11.71200 1.000 16.35000 ? 157 PRO A O   1 
ATOM   1208 C  CB  . PRO A 1 157 ? 23.75000  1.21400   10.05300 1.000 17.08000 ? 157 PRO A CB  1 
ATOM   1209 C  CG  . PRO A 1 157 ? 24.46400  2.06100   9.01000  1.000 14.84000 ? 157 PRO A CG  1 
ATOM   1210 C  CD  . PRO A 1 157 ? 23.90700  3.46700   9.27000  1.000 13.94000 ? 157 PRO A CD  1 
ATOM   1211 N  N   . PHE A 1 158 ? 25.11500  2.68700   13.22900 1.000 16.68000 ? 158 PHE A N   1 
ATOM   1212 C  CA  . PHE A 1 158 ? 26.38700  2.90700   13.91900 1.000 15.16000 ? 158 PHE A CA  1 
ATOM   1213 C  C   . PHE A 1 158 ? 26.97400  1.64400   14.54000 1.000 17.23000 ? 158 PHE A C   1 
ATOM   1214 O  O   . PHE A 1 158 ? 28.10600  1.69500   15.03900 1.000 16.53000 ? 158 PHE A O   1 
ATOM   1215 C  CB  . PHE A 1 158 ? 26.21900  3.99600   14.99200 1.000 14.28000 ? 158 PHE A CB  1 
ATOM   1216 C  CG  . PHE A 1 158 ? 25.28000  3.62000   16.11100 1.000 16.39000 ? 158 PHE A CG  1 
ATOM   1217 C  CD1 . PHE A 1 158 ? 25.71100  2.81400   17.16400 1.000 16.01000 ? 158 PHE A CD1 1 
ATOM   1218 C  CD2 . PHE A 1 158 ? 23.97000  4.09600   16.12900 1.000 14.91000 ? 158 PHE A CD2 1 
ATOM   1219 C  CE1 . PHE A 1 158 ? 24.84200  2.46900   18.19800 1.000 13.24000 ? 158 PHE A CE1 1 
ATOM   1220 C  CE2 . PHE A 1 158 ? 23.10400  3.76200   17.15900 1.000 14.41000 ? 158 PHE A CE2 1 
ATOM   1221 C  CZ  . PHE A 1 158 ? 23.54500  2.94600   18.19900 1.000 13.87000 ? 158 PHE A CZ  1 
ATOM   1222 N  N   . PHE A 1 159 ? 26.24100  0.52300   14.52900 1.000 16.55000 ? 159 PHE A N   1 
ATOM   1223 C  CA  . PHE A 1 159 ? 26.78600  -0.77600  14.90500 1.000 19.21000 ? 159 PHE A CA  1 
ATOM   1224 C  C   . PHE A 1 159 ? 27.81700  -1.28400  13.90600 1.000 19.81000 ? 159 PHE A C   1 
ATOM   1225 O  O   . PHE A 1 159 ? 28.51400  -2.26200  14.19800 1.000 19.81000 ? 159 PHE A O   1 
ATOM   1226 C  CB  . PHE A 1 159 ? 25.64500  -1.79600  15.02500 1.000 18.02000 ? 159 PHE A CB  1 
ATOM   1227 C  CG  . PHE A 1 159 ? 24.69000  -1.78000  13.84900 1.000 19.81000 ? 159 PHE A CG  1 
ATOM   1228 C  CD1 . PHE A 1 159 ? 24.91300  -2.59000  12.74000 1.000 19.40000 ? 159 PHE A CD1 1 
ATOM   1229 C  CD2 . PHE A 1 159 ? 23.56800  -0.94700  13.85200 1.000 20.67000 ? 159 PHE A CD2 1 
ATOM   1230 C  CE1 . PHE A 1 159 ? 24.03800  -2.57500  11.65300 1.000 19.54000 ? 159 PHE A CE1 1 
ATOM   1231 C  CE2 . PHE A 1 159 ? 22.69400  -0.92800  12.77100 1.000 17.83000 ? 159 PHE A CE2 1 
ATOM   1232 C  CZ  . PHE A 1 159 ? 22.93200  -1.74000  11.67400 1.000 14.84000 ? 159 PHE A CZ  1 
ATOM   1233 N  N   . ASP A 1 160 ? 27.93700  -0.63800  12.74800 1.000 19.37000 ? 160 ASP A N   1 
ATOM   1234 C  CA  . ASP A 1 160 ? 28.81800  -1.09200  11.67700 1.000 19.23000 ? 160 ASP A CA  1 
ATOM   1235 C  C   . ASP A 1 160 ? 29.47600  0.14600   11.08000 1.000 15.76000 ? 160 ASP A C   1 
ATOM   1236 O  O   . ASP A 1 160 ? 28.82300  0.91700   10.36900 1.000 16.93000 ? 160 ASP A O   1 
ATOM   1237 C  CB  . ASP A 1 160 ? 28.01700  -1.88200  10.63500 1.000 18.97000 ? 160 ASP A CB  1 
ATOM   1238 C  CG  . ASP A 1 160 ? 28.89100  -2.53900  9.57200  1.000 29.10000 ? 160 ASP A CG  1 
ATOM   1239 O  OD1 . ASP A 1 160 ? 29.78000  -1.86400  9.00700  1.000 20.48000 ? 160 ASP A OD1 1 
ATOM   1240 O  OD2 . ASP A 1 160 ? 28.66100  -3.73400  9.28800  1.000 28.20000 ? 160 ASP A OD2 1 
ATOM   1241 N  N   . ALA A 1 161 ? 30.76100  0.34100   11.37100 1.000 15.91000 ? 161 ALA A N   1 
ATOM   1242 C  CA  . ALA A 1 161 ? 31.43900  1.57100   10.97300 1.000 17.70000 ? 161 ALA A CA  1 
ATOM   1243 C  C   . ALA A 1 161 ? 31.46700  1.73200   9.45600  1.000 14.72000 ? 161 ALA A C   1 
ATOM   1244 O  O   . ALA A 1 161 ? 31.16300  2.81100   8.93300  1.000 14.71000 ? 161 ALA A O   1 
ATOM   1245 C  CB  . ALA A 1 161 ? 32.86200  1.59100   11.54100 1.000 19.29000 ? 161 ALA A CB  1 
ATOM   1246 N  N   . ASP A 1 162 ? 31.85200  0.67500   8.73100  1.000 17.41000 ? 162 ASP A N   1 
ATOM   1247 C  CA  . ASP A 1 162 ? 31.90000  0.75300   7.27100  1.000 17.28000 ? 162 ASP A CA  1 
ATOM   1248 C  C   . ASP A 1 162 ? 30.52900  1.08400   6.69000  1.000 15.83000 ? 162 ASP A C   1 
ATOM   1249 O  O   . ASP A 1 162 ? 30.41300  1.90500   5.76800  1.000 12.62000 ? 162 ASP A O   1 
ATOM   1250 C  CB  . ASP A 1 162 ? 32.40000  -0.56900  6.68300  1.000 19.34000 ? 162 ASP A CB  1 
ATOM   1251 C  CG  . ASP A 1 162 ? 33.90300  -0.76100  6.82800  1.000 23.15000 ? 162 ASP A CG  1 
ATOM   1252 O  OD1 . ASP A 1 162 ? 34.60600  0.16400   7.28900  1.000 22.15000 ? 162 ASP A OD1 1 
ATOM   1253 O  OD2 . ASP A 1 162 ? 34.38300  -1.85500  6.46100  1.000 24.19000 ? 162 ASP A OD2 1 
ATOM   1254 N  N   . GLU A 1 163 ? 29.47500  0.44200   7.20100  1.000 14.60000 ? 163 GLU A N   1 
ATOM   1255 C  CA  . GLU A 1 163 ? 28.14400  0.74900   6.68100  1.000 16.91000 ? 163 GLU A CA  1 
ATOM   1256 C  C   . GLU A 1 163 ? 27.71300  2.16000   7.06700  1.000 18.43000 ? 163 GLU A C   1 
ATOM   1257 O  O   . GLU A 1 163 ? 26.98000  2.81400   6.31700  1.000 13.43000 ? 163 GLU A O   1 
ATOM   1258 C  CB  . GLU A 1 163 ? 27.11800  -0.27300  7.17800  1.000 17.91000 ? 163 GLU A CB  1 
ATOM   1259 C  CG  . GLU A 1 163 ? 27.33600  -1.69700  6.69200  1.000 25.50000 ? 163 GLU A CG  1 
ATOM   1260 C  CD  . GLU A 1 163 ? 26.96300  -1.90000  5.22900  1.000 30.10000 ? 163 GLU A CD  1 
ATOM   1261 O  OE1 . GLU A 1 163 ? 26.58100  -0.92300  4.55400  1.000 26.14000 ? 163 GLU A OE1 1 
ATOM   1262 O  OE2 . GLU A 1 163 ? 27.05400  -3.04900  4.74800  1.000 35.16000 ? 163 GLU A OE2 1 
ATOM   1263 N  N   . SER A 1 164 ? 28.15100  2.64200   8.23300  1.000 13.06000 ? 164 SER A N   1 
ATOM   1264 C  CA  . SER A 1 164 ? 27.84700  4.01700   8.60600  1.000 14.96000 ? 164 SER A CA  1 
ATOM   1265 C  C   . SER A 1 164 ? 28.51900  5.01100   7.66300  1.000 12.81000 ? 164 SER A C   1 
ATOM   1266 O  O   . SER A 1 164 ? 27.90400  6.00800   7.26800  1.000 12.16000 ? 164 SER A O   1 
ATOM   1267 C  CB  . SER A 1 164 ? 28.26900  4.26600   10.04900 1.000 13.82000 ? 164 SER A CB  1 
ATOM   1268 O  OG  . SER A 1 164 ? 27.43500  3.53500   10.92600 1.000 14.40000 ? 164 SER A OG  1 
ATOM   1269 N  N   . VAL A 1 165 ? 29.77200  4.76100   7.29100  1.000 11.98000 ? 165 VAL A N   1 
ATOM   1270 C  CA  . VAL A 1 165 ? 30.45800  5.65700   6.36600  1.000 13.75000 ? 165 VAL A CA  1 
ATOM   1271 C  C   . VAL A 1 165 ? 29.73200  5.68400   5.02800  1.000 12.87000 ? 165 VAL A C   1 
ATOM   1272 O  O   . VAL A 1 165 ? 29.46900  6.75000   4.46700  1.000 13.28000 ? 165 VAL A O   1 
ATOM   1273 C  CB  . VAL A 1 165 ? 31.93400  5.24100   6.21100  1.000 13.76000 ? 165 VAL A CB  1 
ATOM   1274 C  CG1 . VAL A 1 165 ? 32.59300  5.97500   5.04700  1.000 13.87000 ? 165 VAL A CG1 1 
ATOM   1275 C  CG2 . VAL A 1 165 ? 32.69600  5.52300   7.52000  1.000 14.73000 ? 165 VAL A CG2 1 
ATOM   1276 N  N   . ALA A 1 166 ? 29.39000  4.50600   4.50700  1.000 13.33000 ? 166 ALA A N   1 
ATOM   1277 C  CA  . ALA A 1 166 ? 28.64100  4.43300   3.25600  1.000 15.28000 ? 166 ALA A CA  1 
ATOM   1278 C  C   . ALA A 1 166 ? 27.31900  5.19000   3.34900  1.000 15.31000 ? 166 ALA A C   1 
ATOM   1279 O  O   . ALA A 1 166 ? 26.92400  5.89000   2.41500  1.000 13.07000 ? 166 ALA A O   1 
ATOM   1280 C  CB  . ALA A 1 166 ? 28.39200  2.97200   2.89900  1.000 14.20000 ? 166 ALA A CB  1 
ATOM   1281 N  N   . GLU A 1 167 ? 26.61500  5.05700   4.46900  1.000 12.67000 ? 167 GLU A N   1 
ATOM   1282 C  CA  . GLU A 1 167 ? 25.33000  5.73700   4.58800  1.000 15.31000 ? 167 GLU A CA  1 
ATOM   1283 C  C   . GLU A 1 167 ? 25.51600  7.24900   4.66100  1.000 14.08000 ? 167 GLU A C   1 
ATOM   1284 O  O   . GLU A 1 167 ? 24.72800  7.99900   4.07500  1.000 16.16000 ? 167 GLU A O   1 
ATOM   1285 C  CB  . GLU A 1 167 ? 24.56400  5.19700   5.80100  1.000 14.62000 ? 167 GLU A CB  1 
ATOM   1286 C  CG  . GLU A 1 167 ? 23.12300  5.71600   5.95500  1.000 11.34000 ? 167 GLU A CG  1 
ATOM   1287 C  CD  . GLU A 1 167 ? 22.18800  5.31500   4.82100  1.000 14.95000 ? 167 GLU A CD  1 
ATOM   1288 O  OE1 . GLU A 1 167 ? 22.61600  4.66400   3.85000  1.000 15.96000 ? 167 GLU A OE1 1 
ATOM   1289 O  OE2 . GLU A 1 167 ? 20.99100  5.65300   4.91500  1.000 14.98000 ? 167 GLU A OE2 1 
ATOM   1290 N  N   . VAL A 1 168 ? 26.58200  7.71900   5.32000  1.000 11.74000 ? 168 VAL A N   1 
ATOM   1291 C  CA  . VAL A 1 168 ? 26.86400  9.15400   5.33300  1.000 10.15000 ? 168 VAL A CA  1 
ATOM   1292 C  C   . VAL A 1 168 ? 27.05200  9.67500   3.90800  1.000 9.94000  ? 168 VAL A C   1 
ATOM   1293 O  O   . VAL A 1 168 ? 26.43100  10.66100  3.50100  1.000 12.17000 ? 168 VAL A O   1 
ATOM   1294 C  CB  . VAL A 1 168 ? 28.08200  9.45900   6.22900  1.000 13.31000 ? 168 VAL A CB  1 
ATOM   1295 C  CG1 . VAL A 1 168 ? 28.58100  10.89800  6.01500  1.000 12.91000 ? 168 VAL A CG1 1 
ATOM   1296 C  CG2 . VAL A 1 168 ? 27.74100  9.25700   7.71400  1.000 12.81000 ? 168 VAL A CG2 1 
ATOM   1297 N  N   . HIS A 1 169 ? 27.90000  9.01300   3.11700  1.000 12.88000 ? 169 HIS A N   1 
ATOM   1298 C  CA  . HIS A 1 169 ? 28.04300  9.41600   1.71900  1.000 13.94000 ? 169 HIS A CA  1 
ATOM   1299 C  C   . HIS A 1 169 ? 26.69800  9.41800   0.99900  1.000 13.56000 ? 169 HIS A C   1 
ATOM   1300 O  O   . HIS A 1 169 ? 26.38700  10.34600  0.24100  1.000 13.47000 ? 169 HIS A O   1 
ATOM   1301 C  CB  . HIS A 1 169 ? 29.00600  8.47900   0.99100  1.000 11.32000 ? 169 HIS A CB  1 
ATOM   1302 C  CG  . HIS A 1 169 ? 30.41800  8.55000   1.47400  1.000 13.61000 ? 169 HIS A CG  1 
ATOM   1303 N  ND1 . HIS A 1 169 ? 31.08900  9.74000   1.64300  1.000 15.71000 ? 169 HIS A ND1 1 
ATOM   1304 C  CD2 . HIS A 1 169 ? 31.30400  7.57100   1.77700  1.000 15.55000 ? 169 HIS A CD2 1 
ATOM   1305 C  CE1 . HIS A 1 169 ? 32.32300  9.49400   2.04900  1.000 16.59000 ? 169 HIS A CE1 1 
ATOM   1306 N  NE2 . HIS A 1 169 ? 32.47800  8.18600   2.14100  1.000 16.20000 ? 169 HIS A NE2 1 
ATOM   1307 N  N   . ARG A 1 170 ? 25.89400  8.37700   1.20600  1.000 13.26000 ? 170 ARG A N   1 
ATOM   1308 C  CA  . ARG A 1 170 ? 24.64900  8.23900   0.45600  1.000 14.32000 ? 170 ARG A CA  1 
ATOM   1309 C  C   . ARG A 1 170 ? 23.66000  9.34900   0.80400  1.000 15.44000 ? 170 ARG A C   1 
ATOM   1310 O  O   . ARG A 1 170 ? 23.04000  9.94100   -0.08900 1.000 14.02000 ? 170 ARG A O   1 
ATOM   1311 C  CB  . ARG A 1 170 ? 24.02700  6.86700   0.71800  1.000 13.52000 ? 170 ARG A CB  1 
ATOM   1312 C  CG  . ARG A 1 170 ? 22.90800  6.50900   -0.25300 1.000 12.69000 ? 170 ARG A CG  1 
ATOM   1313 C  CD  . ARG A 1 170 ? 22.25400  5.18500   0.12300  1.000 16.61000 ? 170 ARG A CD  1 
ATOM   1314 N  NE  . ARG A 1 170 ? 21.45300  5.31600   1.33600  1.000 16.51000 ? 170 ARG A NE  1 
ATOM   1315 C  CZ  . ARG A 1 170 ? 20.14900  5.57700   1.34200  1.000 17.88000 ? 170 ARG A CZ  1 
ATOM   1316 N  NH1 . ARG A 1 170 ? 19.48400  5.73300   0.20400  1.000 16.10000 ? 170 ARG A NH1 1 
ATOM   1317 N  NH2 . ARG A 1 170 ? 19.51000  5.69800   2.49200  1.000 12.97000 ? 170 ARG A NH2 1 
ATOM   1318 N  N   . ILE A 1 171 ? 23.48500  9.63900   2.09600  1.000 12.08000 ? 171 ILE A N   1 
ATOM   1319 C  CA  . ILE A 1 171 ? 22.52500  10.68100  2.46400  1.000 14.91000 ? 171 ILE A CA  1 
ATOM   1320 C  C   . ILE A 1 171 ? 23.11000  12.08000  2.32600  1.000 12.19000 ? 171 ILE A C   1 
ATOM   1321 O  O   . ILE A 1 171 ? 22.34400  13.04400  2.16500  1.000 12.78000 ? 171 ILE A O   1 
ATOM   1322 C  CB  . ILE A 1 171 ? 21.96100  10.43700  3.87400  1.000 13.94000 ? 171 ILE A CB  1 
ATOM   1323 C  CG1 . ILE A 1 171 ? 23.03000  10.65500  4.96000  1.000 14.83000 ? 171 ILE A CG1 1 
ATOM   1324 C  CG2 . ILE A 1 171 ? 21.36000  9.03200   3.94700  1.000 11.44000 ? 171 ILE A CG2 1 
ATOM   1325 C  CD1 . ILE A 1 171 ? 22.53100  10.32700  6.35500  1.000 16.87000 ? 171 ILE A CD1 1 
ATOM   1326 N  N   . ALA A 1 172 ? 24.44200  12.23500  2.35800  1.000 13.42000 ? 172 ALA A N   1 
ATOM   1327 C  CA  . ALA A 1 172 ? 25.02400  13.52500  1.98900  1.000 10.95000 ? 172 ALA A CA  1 
ATOM   1328 C  C   . ALA A 1 172 ? 24.53100  13.96300  0.61200  1.000 14.89000 ? 172 ALA A C   1 
ATOM   1329 O  O   . ALA A 1 172 ? 24.12800  15.11400  0.41600  1.000 15.89000 ? 172 ALA A O   1 
ATOM   1330 C  CB  . ALA A 1 172 ? 26.55700  13.46500  1.99200  1.000 13.60000 ? 172 ALA A CB  1 
ATOM   1331 N  N   . ALA A 1 173 ? 24.54300  13.04300  -0.35300 1.000 13.86000 ? 173 ALA A N   1 
ATOM   1332 C  CA  . ALA A 1 173 ? 24.12000  13.36700  -1.70900 1.000 16.94000 ? 173 ALA A CA  1 
ATOM   1333 C  C   . ALA A 1 173 ? 22.62400  13.62300  -1.81700 1.000 17.59000 ? 173 ALA A C   1 
ATOM   1334 O  O   . ALA A 1 173 ? 22.17400  14.11200  -2.85600 1.000 20.16000 ? 173 ALA A O   1 
ATOM   1335 C  CB  . ALA A 1 173 ? 24.54600  12.24200  -2.67000 1.000 14.76000 ? 173 ALA A CB  1 
ATOM   1336 N  N   . MET A 1 174 ? 21.84700  13.29800  -0.79100 1.000 13.56000 ? 174 MET A N   1 
ATOM   1337 C  CA  . MET A 1 174 ? 20.43600  13.64500  -0.74200 1.000 16.30000 ? 174 MET A CA  1 
ATOM   1338 C  C   . MET A 1 174 ? 20.18300  14.96700  -0.02900 1.000 17.34000 ? 174 MET A C   1 
ATOM   1339 O  O   . MET A 1 174 ? 19.01900  15.35600  0.12600  1.000 20.13000 ? 174 MET A O   1 
ATOM   1340 C  CB  . MET A 1 174 ? 19.64400  12.51200  -0.06600 1.000 14.96000 ? 174 MET A CB  1 
ATOM   1341 C  CG  . MET A 1 174 ? 19.75900  11.18500  -0.81600 1.000 19.50000 ? 174 MET A CG  1 
ATOM   1342 S  SD  . MET A 1 174 ? 19.24000  9.72800   0.13600  1.000 30.51000 ? 174 MET A SD  1 
ATOM   1343 C  CE  . MET A 1 174 ? 17.70600  10.35500  0.70500  1.000 14.20000 ? 174 MET A CE  1 
ATOM   1344 N  N   . GLY A 1 175 ? 21.23900  15.66100  0.39800  1.000 14.81000 ? 175 GLY A N   1 
ATOM   1345 C  CA  . GLY A 1 175 ? 21.13100  16.93000  1.09100  1.000 15.74000 ? 175 GLY A CA  1 
ATOM   1346 C  C   . GLY A 1 175 ? 21.19700  16.86600  2.60200  1.000 15.92000 ? 175 GLY A C   1 
ATOM   1347 O  O   . GLY A 1 175 ? 20.90600  17.87300  3.25600  1.000 17.21000 ? 175 GLY A O   1 
ATOM   1348 N  N   . CYS A 1 176 ? 21.55700  15.72100  3.17600  1.000 14.85000 ? 176 CYS A N   1 
ATOM   1349 C  CA  . CYS A 1 176 ? 21.63600  15.59900  4.62900  1.000 15.22000 ? 176 CYS A CA  1 
ATOM   1350 C  C   . CYS A 1 176 ? 22.60200  16.62600  5.20800  1.000 16.45000 ? 176 CYS A C   1 
ATOM   1351 O  O   . CYS A 1 176 ? 23.73300  16.77200  4.73100  1.000 16.72000 ? 176 CYS A O   1 
ATOM   1352 C  CB  . CYS A 1 176 ? 22.08300  14.18700  5.00700  1.000 14.86000 ? 176 CYS A CB  1 
ATOM   1353 S  SG  . CYS A 1 176 ? 22.25100  13.94500  6.77500  1.000 15.90000 ? 176 CYS A SG  1 
ATOM   1354 N  N   . ARG A 1 177 ? 22.13400  17.36500  6.22100  1.000 12.50000 ? 177 ARG A N   1 
ATOM   1355 C  CA  . ARG A 1 177 ? 22.93700  18.37200  6.90700  1.000 12.79000 ? 177 ARG A CA  1 
ATOM   1356 C  C   . ARG A 1 177 ? 23.46700  17.90400  8.25900  1.000 12.50000 ? 177 ARG A C   1 
ATOM   1357 O  O   . ARG A 1 177 ? 24.42200  18.49600  8.77100  1.000 12.49000 ? 177 ARG A O   1 
ATOM   1358 C  CB  . ARG A 1 177 ? 22.11200  19.65100  7.12000  1.000 17.48000 ? 177 ARG A CB  1 
ATOM   1359 C  CG  . ARG A 1 177 ? 21.61100  20.29500  5.83500  1.000 13.99000 ? 177 ARG A CG  1 
ATOM   1360 C  CD  . ARG A 1 177 ? 22.77300  20.56500  4.85700  1.000 16.45000 ? 177 ARG A CD  1 
ATOM   1361 N  NE  . ARG A 1 177 ? 22.49600  21.71400  4.00200  1.000 20.45000 ? 177 ARG A NE  1 
ATOM   1362 C  CZ  . ARG A 1 177 ? 21.61000  21.74400  2.99800  1.000 22.56000 ? 177 ARG A CZ  1 
ATOM   1363 N  NH1 . ARG A 1 177 ? 20.87500  20.67400  2.68400  1.000 20.13000 ? 177 ARG A NH1 1 
ATOM   1364 N  NH2 . ARG A 1 177 ? 21.45500  22.86500  2.30000  1.000 19.61000 ? 177 ARG A NH2 1 
ATOM   1365 N  N   . SER A 1 178 ? 22.87900  16.86700  8.84200  1.000 12.67000 ? 178 SER A N   1 
ATOM   1366 C  CA  . SER A 1 178 ? 23.27700  16.40500  10.16200 1.000 11.51000 ? 178 SER A CA  1 
ATOM   1367 C  C   . SER A 1 178 ? 22.94200  14.92400  10.29000 1.000 12.65000 ? 178 SER A C   1 
ATOM   1368 O  O   . SER A 1 178 ? 21.99800  14.43100  9.66800  1.000 12.99000 ? 178 SER A O   1 
ATOM   1369 C  CB  . SER A 1 178 ? 22.56800  17.22900  11.25100 1.000 10.98000 ? 178 SER A CB  1 
ATOM   1370 O  OG  . SER A 1 178 ? 22.92900  16.78000  12.55200 1.000 14.16000 ? 178 SER A OG  1 
ATOM   1371 N  N   . ILE A 1 179 ? 23.72800  14.20300  11.07900 1.000 11.39000 ? 179 ILE A N   1 
ATOM   1372 C  CA  . ILE A 1 179 ? 23.32700  12.87400  11.52200 1.000 11.98000 ? 179 ILE A CA  1 
ATOM   1373 C  C   . ILE A 1 179 ? 23.20000  12.92700  13.02900 1.000 15.71000 ? 179 ILE A C   1 
ATOM   1374 O  O   . ILE A 1 179 ? 24.04100  13.53200  13.70300 1.000 14.11000 ? 179 ILE A O   1 
ATOM   1375 C  CB  . ILE A 1 179 ? 24.29500  11.74300  11.09800 1.000 12.54000 ? 179 ILE A CB  1 
ATOM   1376 C  CG1 . ILE A 1 179 ? 25.73100  12.02900  11.54200 1.000 11.25000 ? 179 ILE A CG1 1 
ATOM   1377 C  CG2 . ILE A 1 179 ? 24.18600  11.48700  9.57600  1.000 11.84000 ? 179 ILE A CG2 1 
ATOM   1378 C  CD1 . ILE A 1 179 ? 26.65900  10.79000  11.43100 1.000 14.19000 ? 179 ILE A CD1 1 
ATOM   1379 N  N   . SER A 1 180 ? 22.13200  12.32000  13.54400 1.000 10.73000 ? 180 SER A N   1 
ATOM   1380 C  CA  . SER A 1 180 ? 21.92900  12.18900  14.97800 1.000 12.93000 ? 180 SER A CA  1 
ATOM   1381 C  C   . SER A 1 180 ? 22.58400  10.89300  15.43700 1.000 13.34000 ? 180 SER A C   1 
ATOM   1382 O  O   . SER A 1 180 ? 22.20700  9.81400   14.97100 1.000 13.74000 ? 180 SER A O   1 
ATOM   1383 C  CB  . SER A 1 180 ? 20.43100  12.19400  15.30000 1.000 11.07000 ? 180 SER A CB  1 
ATOM   1384 O  OG  . SER A 1 180 ? 20.20300  11.84600  16.65600 1.000 10.89000 ? 180 SER A OG  1 
ATOM   1385 N  N   . ILE A 1 181 ? 23.56900  10.99300  16.32300 1.000 12.32000 ? 181 ILE A N   1 
ATOM   1386 C  CA  . ILE A 1 181 ? 24.28500  9.81600   16.80800 1.000 11.13000 ? 181 ILE A CA  1 
ATOM   1387 C  C   . ILE A 1 181 ? 24.11500  9.75600   18.31300 1.000 13.02000 ? 181 ILE A C   1 
ATOM   1388 O  O   . ILE A 1 181 ? 23.81400  10.77700  18.96100 1.000 14.09000 ? 181 ILE A O   1 
ATOM   1389 C  CB  . ILE A 1 181 ? 25.77700  9.83200   16.38600 1.000 12.41000 ? 181 ILE A CB  1 
ATOM   1390 C  CG1 . ILE A 1 181 ? 26.53800  11.00400  17.00700 1.000 11.48000 ? 181 ILE A CG1 1 
ATOM   1391 C  CG2 . ILE A 1 181 ? 25.91800  9.78200   14.85700 1.000 12.61000 ? 181 ILE A CG2 1 
ATOM   1392 C  CD1 . ILE A 1 181 ? 28.09100  10.83100  16.95300 1.000 13.90000 ? 181 ILE A CD1 1 
ATOM   1393 N  N   . PRO A 1 182 ? 24.29100  8.57700   18.91400 1.000 13.63000 ? 182 PRO A N   1 
ATOM   1394 C  CA  . PRO A 1 182 ? 24.09800  8.44200   20.36400 1.000 14.47000 ? 182 PRO A CA  1 
ATOM   1395 C  C   . PRO A 1 182 ? 25.08400  9.30500   21.12700 1.000 15.07000 ? 182 PRO A C   1 
ATOM   1396 O  O   . PRO A 1 182 ? 26.29100  9.26200   20.87800 1.000 16.70000 ? 182 PRO A O   1 
ATOM   1397 C  CB  . PRO A 1 182 ? 24.35400  6.95200   20.62400 1.000 15.50000 ? 182 PRO A CB  1 
ATOM   1398 C  CG  . PRO A 1 182 ? 24.34400  6.29800   19.31000 1.000 19.59000 ? 182 PRO A CG  1 
ATOM   1399 C  CD  . PRO A 1 182 ? 24.64600  7.29400   18.27500 1.000 15.69000 ? 182 PRO A CD  1 
ATOM   1400 N  N   . GLU A 1 183 ? 24.57100  10.09000  22.07700 1.000 13.93000 ? 183 GLU A N   1 
ATOM   1401 C  CA  . GLU A 1 183 ? 25.44800  11.05500  22.73400 1.000 13.90000 ? 183 GLU A CA  1 
ATOM   1402 C  C   . GLU A 1 183 ? 26.45300  10.37400  23.66100 1.000 14.20000 ? 183 GLU A C   1 
ATOM   1403 O  O   . GLU A 1 183 ? 27.54500  10.90500  23.87600 1.000 13.88000 ? 183 GLU A O   1 
ATOM   1404 C  CB  . GLU A 1 183 ? 24.63500  12.09200  23.50400 1.000 15.47000 ? 183 GLU A CB  1 
ATOM   1405 C  CG  . GLU A 1 183 ? 23.75800  11.52800  24.59000 1.000 12.89000 ? 183 GLU A CG  1 
ATOM   1406 C  CD  . GLU A 1 183 ? 23.36200  12.60500  25.59200 1.000 18.54000 ? 183 GLU A CD  1 
ATOM   1407 O  OE1 . GLU A 1 183 ? 24.06400  13.63500  25.66800 1.000 18.01000 ? 183 GLU A OE1 1 
ATOM   1408 O  OE2 . GLU A 1 183 ? 22.34900  12.43000  26.29800 1.000 17.51000 ? 183 GLU A OE2 1 
ATOM   1409 N  N   . THR A 1 184 ? 26.12000  9.21100   24.21200 1.000 13.92000 ? 184 THR A N   1 
ATOM   1410 C  CA  . THR A 1 184 ? 27.01500  8.48700   25.11700 1.000 13.73000 ? 184 THR A CA  1 
ATOM   1411 C  C   . THR A 1 184 ? 26.94200  7.01500   24.74900 1.000 17.08000 ? 184 THR A C   1 
ATOM   1412 O  O   . THR A 1 184 ? 26.23800  6.23300   25.40300 1.000 17.67000 ? 184 THR A O   1 
ATOM   1413 C  CB  . THR A 1 184 ? 26.63800  8.71700   26.58900 1.000 16.28000 ? 184 THR A CB  1 
ATOM   1414 O  OG1 . THR A 1 184 ? 25.25900  8.38100   26.80900 1.000 15.27000 ? 184 THR A OG1 1 
ATOM   1415 C  CG2 . THR A 1 184 ? 26.88200  10.15900  26.99800 1.000 15.98000 ? 184 THR A CG2 1 
ATOM   1416 N  N   . PRO A 1 185 ? 27.66000  6.60100   23.69000 1.000 14.03000 ? 185 PRO A N   1 
ATOM   1417 C  CA  . PRO A 1 185 ? 27.43800  5.26100   23.11900 1.000 15.21000 ? 185 PRO A CA  1 
ATOM   1418 C  C   . PRO A 1 185 ? 27.75100  4.13300   24.07300 1.000 14.58000 ? 185 PRO A C   1 
ATOM   1419 O  O   . PRO A 1 185 ? 27.19300  3.03900   23.93100 1.000 16.21000 ? 185 PRO A O   1 
ATOM   1420 C  CB  . PRO A 1 185 ? 28.38600  5.22800   21.90600 1.000 16.14000 ? 185 PRO A CB  1 
ATOM   1421 C  CG  . PRO A 1 185 ? 28.71400  6.62100   21.61900 1.000 19.68000 ? 185 PRO A CG  1 
ATOM   1422 C  CD  . PRO A 1 185 ? 28.64700  7.36800   22.91800 1.000 16.61000 ? 185 PRO A CD  1 
ATOM   1423 N  N   . TYR A 1 186 ? 28.65200  4.35100   25.02500 1.000 15.81000 ? 186 TYR A N   1 
ATOM   1424 C  CA  . TYR A 1 186 ? 28.95100  3.31700   25.99600 1.000 16.40000 ? 186 TYR A CA  1 
ATOM   1425 C  C   . TYR A 1 186 ? 27.76500  3.03700   26.91800 1.000 21.75000 ? 186 TYR A C   1 
ATOM   1426 O  O   . TYR A 1 186 ? 27.76700  2.01900   27.61900 1.000 18.41000 ? 186 TYR A O   1 
ATOM   1427 C  CB  . TYR A 1 186 ? 30.19100  3.72000   26.79500 1.000 14.99000 ? 186 TYR A CB  1 
ATOM   1428 C  CG  . TYR A 1 186 ? 30.08900  5.11900   27.35600 1.000 18.32000 ? 186 TYR A CG  1 
ATOM   1429 C  CD1 . TYR A 1 186 ? 29.52000  5.34400   28.59900 1.000 16.32000 ? 186 TYR A CD1 1 
ATOM   1430 C  CD2 . TYR A 1 186 ? 30.56200  6.21700   26.64100 1.000 16.46000 ? 186 TYR A CD2 1 
ATOM   1431 C  CE1 . TYR A 1 186 ? 29.42600  6.62000   29.11700 1.000 18.81000 ? 186 TYR A CE1 1 
ATOM   1432 C  CE2 . TYR A 1 186 ? 30.45900  7.50000   27.14200 1.000 16.43000 ? 186 TYR A CE2 1 
ATOM   1433 C  CZ  . TYR A 1 186 ? 29.88800  7.69800   28.38400 1.000 16.61000 ? 186 TYR A CZ  1 
ATOM   1434 O  OH  . TYR A 1 186 ? 29.79100  8.97100   28.91100 1.000 16.53000 ? 186 TYR A OH  1 
ATOM   1435 N  N   . GLY A 1 187 ? 26.75200  3.90200   26.92100 1.000 16.54000 ? 187 GLY A N   1 
ATOM   1436 C  CA  . GLY A 1 187 ? 25.55000  3.70200   27.70400 1.000 18.06000 ? 187 GLY A CA  1 
ATOM   1437 C  C   . GLY A 1 187 ? 24.41700  3.00000   26.98300 1.000 21.67000 ? 187 GLY A C   1 
ATOM   1438 O  O   . GLY A 1 187 ? 23.36900  2.74600   27.59300 1.000 21.35000 ? 187 GLY A O   1 
ATOM   1439 N  N   . VAL A 1 188 ? 24.61000  2.66100   25.70900 1.000 17.21000 ? 188 VAL A N   1 
ATOM   1440 C  CA  . VAL A 1 188 ? 23.55000  2.16100   24.84100 1.000 18.23000 ? 188 VAL A CA  1 
ATOM   1441 C  C   . VAL A 1 188 ? 23.56600  0.64200   24.89000 1.000 22.20000 ? 188 VAL A C   1 
ATOM   1442 O  O   . VAL A 1 188 ? 24.58100  0.01900   24.55500 1.000 20.00000 ? 188 VAL A O   1 
ATOM   1443 C  CB  . VAL A 1 188 ? 23.74700  2.65600   23.39800 1.000 18.56000 ? 188 VAL A CB  1 
ATOM   1444 C  CG1 . VAL A 1 188 ? 22.73300  2.00100   22.44300 1.000 19.73000 ? 188 VAL A CG1 1 
ATOM   1445 C  CG2 . VAL A 1 188 ? 23.67700  4.16600   23.33700 1.000 18.93000 ? 188 VAL A CG2 1 
ATOM   1446 N  N   . GLY A 1 189 ? 22.44500  0.04300   25.28700 1.000 21.00000 ? 189 GLY A N   1 
ATOM   1447 C  CA  . GLY A 1 189 ? 22.38400  -1.40800  25.35400 1.000 26.74000 ? 189 GLY A CA  1 
ATOM   1448 C  C   . GLY A 1 189 ? 23.48500  -1.95000  26.23800 1.000 29.09000 ? 189 GLY A C   1 
ATOM   1449 O  O   . GLY A 1 189 ? 23.73300  -1.44400  27.33800 1.000 28.46000 ? 189 GLY A O   1 
ATOM   1450 N  N   . GLU A 1 190 ? 24.12400  -2.96400  25.71900 1.000 31.91000 ? 190 GLU A N   1 
ATOM   1451 C  CA  A GLU A 1 190 ? 25.33600  -3.50600  26.45400 0.450 34.32000 ? 190 GLU A CA  1 
ATOM   1452 C  CA  B GLU A 1 190 ? 25.31100  -3.53300  26.33300 0.550 34.33000 ? 190 GLU A CA  1 
ATOM   1453 C  C   . GLU A 1 190 ? 26.67400  -2.64200  26.24400 1.000 32.73000 ? 190 GLU A C   1 
ATOM   1454 O  O   . GLU A 1 190 ? 27.82200  -2.89000  26.70300 1.000 35.91000 ? 190 GLU A O   1 
ATOM   1455 C  CB  A GLU A 1 190 ? 25.64200  -4.92400  25.96400 0.450 40.62000 ? 190 GLU A CB  1 
ATOM   1456 C  CB  B GLU A 1 190 ? 25.64000  -4.85300  25.65800 0.550 40.62000 ? 190 GLU A CB  1 
ATOM   1457 C  CG  A GLU A 1 190 ? 24.88700  -6.01900  26.70800 0.450 44.64000 ? 190 GLU A CG  1 
ATOM   1458 C  CG  B GLU A 1 190 ? 24.64700  -5.95100  25.91300 0.550 46.00000 ? 190 GLU A CG  1 
ATOM   1459 C  CD  A GLU A 1 190 ? 24.92300  -7.32500  25.94400 0.450 45.71000 ? 190 GLU A CD  1 
ATOM   1460 C  CD  B GLU A 1 190 ? 24.76300  -6.40600  27.31800 0.550 44.52000 ? 190 GLU A CD  1 
ATOM   1461 O  OE1 A GLU A 1 190 ? 23.86800  -7.71500  25.39600 0.450 46.22000 ? 190 GLU A OE1 1 
ATOM   1462 O  OE1 B GLU A 1 190 ? 25.85700  -6.89100  27.66200 0.550 43.05000 ? 190 GLU A OE1 1 
ATOM   1463 O  OE2 A GLU A 1 190 ? 26.00600  -7.94700  25.86800 0.450 45.47000 ? 190 GLU A OE2 1 
ATOM   1464 O  OE2 B GLU A 1 190 ? 23.79200  -6.21600  28.06800 0.550 45.47000 ? 190 GLU A OE2 1 
ATOM   1465 N  N   . GLY A 1 191 ? 26.45800  -1.56600  25.48300 1.000 25.06000 ? 191 GLY A N   1 
ATOM   1466 C  CA  . GLY A 1 191 ? 27.58300  -0.68000  25.29300 1.000 22.53000 ? 191 GLY A CA  1 
ATOM   1467 C  C   . GLY A 1 191 ? 28.14600  -0.75400  23.89200 1.000 25.79000 ? 191 GLY A C   1 
ATOM   1468 O  O   . GLY A 1 191 ? 28.41700  -1.84200  23.36600 1.000 24.19000 ? 191 GLY A O   1 
ATOM   1469 N  N   . PHE A 1 192 ? 28.29200  0.40300   23.26700 1.000 19.96000 ? 192 PHE A N   1 
ATOM   1470 C  CA  . PHE A 1 192 ? 29.02000  0.53400   22.02300 1.000 18.14000 ? 192 PHE A CA  1 
ATOM   1471 C  C   . PHE A 1 192 ? 30.32400  1.27500   22.28200 1.000 18.24000 ? 192 PHE A C   1 
ATOM   1472 O  O   . PHE A 1 192 ? 30.48900  1.88500   23.34200 1.000 16.88000 ? 192 PHE A O   1 
ATOM   1473 C  CB  . PHE A 1 192 ? 28.14800  1.25700   20.99100 1.000 16.21000 ? 192 PHE A CB  1 
ATOM   1474 C  CG  . PHE A 1 192 ? 27.06000  0.38000   20.42800 1.000 18.79000 ? 192 PHE A CG  1 
ATOM   1475 C  CD1 . PHE A 1 192 ? 25.84400  0.24800   21.09200 1.000 18.85000 ? 192 PHE A CD1 1 
ATOM   1476 C  CD2 . PHE A 1 192 ? 27.27100  -0.35800  19.28300 1.000 21.02000 ? 192 PHE A CD2 1 
ATOM   1477 C  CE1 . PHE A 1 192 ? 24.84400  -0.57400  20.60100 1.000 21.56000 ? 192 PHE A CE1 1 
ATOM   1478 C  CE2 . PHE A 1 192 ? 26.27000  -1.18500  18.78100 1.000 21.39000 ? 192 PHE A CE2 1 
ATOM   1479 C  CZ  . PHE A 1 192 ? 25.05500  -1.29000  19.44100 1.000 18.37000 ? 192 PHE A CZ  1 
ATOM   1480 N  N   . PRO A 1 193 ? 31.29300  1.21300   21.36500 1.000 16.16000 ? 193 PRO A N   1 
ATOM   1481 C  CA  . PRO A 1 193 ? 32.56900  1.89400   21.61000 1.000 17.20000 ? 193 PRO A CA  1 
ATOM   1482 C  C   . PRO A 1 193 ? 32.36900  3.38800   21.83400 1.000 17.73000 ? 193 PRO A C   1 
ATOM   1483 O  O   . PRO A 1 193 ? 31.44200  4.00000   21.29500 1.000 15.63000 ? 193 PRO A O   1 
ATOM   1484 C  CB  . PRO A 1 193 ? 33.37300  1.61800   20.32900 1.000 16.22000 ? 193 PRO A CB  1 
ATOM   1485 C  CG  . PRO A 1 193 ? 32.77000  0.35500   19.78700 1.000 21.29000 ? 193 PRO A CG  1 
ATOM   1486 C  CD  . PRO A 1 193 ? 31.30400  0.46100   20.09800 1.000 20.79000 ? 193 PRO A CD  1 
ATOM   1487 N  N   . ASP A 1 194 ? 33.25300  3.97600   22.64500 1.000 16.31000 ? 194 ASP A N   1 
ATOM   1488 C  CA  . ASP A 1 194 ? 33.12700  5.38700   22.98900 1.000 14.99000 ? 194 ASP A CA  1 
ATOM   1489 C  C   . ASP A 1 194 ? 33.90400  6.24800   21.98700 1.000 16.30000 ? 194 ASP A C   1 
ATOM   1490 O  O   . ASP A 1 194 ? 34.60100  5.74800   21.10300 1.000 16.25000 ? 194 ASP A O   1 
ATOM   1491 C  CB  . ASP A 1 194 ? 33.58500  5.65100   24.43100 1.000 17.89000 ? 194 ASP A CB  1 
ATOM   1492 C  CG  . ASP A 1 194 ? 35.10300  5.57400   24.61300 1.000 23.70000 ? 194 ASP A CG  1 
ATOM   1493 O  OD1 . ASP A 1 194 ? 35.80600  4.96700   23.78800 1.000 21.36000 ? 194 ASP A OD1 1 
ATOM   1494 O  OD2 . ASP A 1 194 ? 35.60200  6.14000   25.60700 1.000 32.36000 ? 194 ASP A OD2 1 
ATOM   1495 N  N   . PHE A 1 195 ? 33.75100  7.56800   22.11300 1.000 13.38000 ? 195 PHE A N   1 
ATOM   1496 C  CA  . PHE A 1 195 ? 34.32000  8.45800   21.10400 1.000 14.17000 ? 195 PHE A CA  1 
ATOM   1497 C  C   . PHE A 1 195 ? 35.84000  8.46000   21.14900 1.000 16.55000 ? 195 PHE A C   1 
ATOM   1498 O  O   . PHE A 1 195 ? 36.48900  8.75800   20.13700 1.000 14.34000 ? 195 PHE A O   1 
ATOM   1499 C  CB  . PHE A 1 195 ? 33.78800  9.88500   21.28400 1.000 12.22000 ? 195 PHE A CB  1 
ATOM   1500 C  CG  . PHE A 1 195 ? 32.30100  10.01600  21.03100 1.000 16.24000 ? 195 PHE A CG  1 
ATOM   1501 C  CD1 . PHE A 1 195 ? 31.70500  9.34400   19.97500 1.000 17.04000 ? 195 PHE A CD1 1 
ATOM   1502 C  CD2 . PHE A 1 195 ? 31.50600  10.81900  21.84300 1.000 15.57000 ? 195 PHE A CD2 1 
ATOM   1503 C  CE1 . PHE A 1 195 ? 30.33800  9.44900   19.74300 1.000 16.72000 ? 195 PHE A CE1 1 
ATOM   1504 C  CE2 . PHE A 1 195 ? 30.14500  10.93500  21.61100 1.000 13.67000 ? 195 PHE A CE2 1 
ATOM   1505 C  CZ  . PHE A 1 195 ? 29.56400  10.24200  20.55500 1.000 15.03000 ? 195 PHE A CZ  1 
ATOM   1506 N  N   . LYS A 1 196 ? 36.41700  8.15700   22.30600 1.000 14.41000 ? 196 LYS A N   1 
ATOM   1507 C  CA  . LYS A 1 196 ? 37.86300  8.16400   22.46000 1.000 19.49000 ? 196 LYS A CA  1 
ATOM   1508 C  C   . LYS A 1 196 ? 38.51300  6.92400   21.87300 1.000 14.12000 ? 196 LYS A C   1 
ATOM   1509 O  O   . LYS A 1 196 ? 39.73200  6.91800   21.68500 1.000 19.54000 ? 196 LYS A O   1 
ATOM   1510 C  CB  . LYS A 1 196 ? 38.23200  8.27300   23.94200 1.000 23.95000 ? 196 LYS A CB  1 
ATOM   1511 C  CG  . LYS A 1 196 ? 39.66000  8.73400   24.17700 1.000 23.10000 ? 196 LYS A CG  1 
ATOM   1512 C  CD  . LYS A 1 196 ? 39.96700  8.90600   25.65800 1.000 29.13000 ? 196 LYS A CD  1 
ATOM   1513 C  CE  . LYS A 1 196 ? 41.40500  9.39200   25.84100 1.000 40.65000 ? 196 LYS A CE  1 
ATOM   1514 N  NZ  . LYS A 1 196 ? 41.79200  9.53800   27.27400 1.000 42.26000 ? 196 LYS A NZ  1 
ATOM   1515 N  N   . SER A 1 197 ? 37.72900  5.88500   21.57400 1.000 15.85000 ? 197 SER A N   1 
ATOM   1516 C  CA  . SER A 1 197 ? 38.29000  4.61000   21.14200 1.000 16.30000 ? 197 SER A CA  1 
ATOM   1517 C  C   . SER A 1 197 ? 38.83300  4.65300   19.72500 1.000 20.09000 ? 197 SER A C   1 
ATOM   1518 O  O   . SER A 1 197 ? 39.61600  3.77400   19.35600 1.000 19.49000 ? 197 SER A O   1 
ATOM   1519 C  CB  . SER A 1 197 ? 37.23400  3.50800   21.23000 1.000 17.09000 ? 197 SER A CB  1 
ATOM   1520 O  OG  . SER A 1 197 ? 36.21700  3.68100   20.24200 1.000 18.47000 ? 197 SER A OG  1 
ATOM   1521 N  N   . GLY A 1 198 ? 38.44400  5.64500   18.92400 1.000 17.36000 ? 198 GLY A N   1 
ATOM   1522 C  CA  . GLY A 1 198 ? 38.77300  5.65400   17.51900 1.000 19.48000 ? 198 GLY A CA  1 
ATOM   1523 C  C   . GLY A 1 198 ? 37.75100  4.97400   16.63700 1.000 15.82000 ? 198 GLY A C   1 
ATOM   1524 O  O   . GLY A 1 198 ? 37.82400  5.11200   15.41000 1.000 14.00000 ? 198 GLY A O   1 
ATOM   1525 N  N   . TYR A 1 199 ? 36.80000  4.24600   17.22900 1.000 15.93000 ? 199 TYR A N   1 
ATOM   1526 C  CA  . TYR A 1 199 ? 35.79700  3.53300   16.44800 1.000 17.10000 ? 199 TYR A CA  1 
ATOM   1527 C  C   . TYR A 1 199 ? 35.02700  4.47400   15.53000 1.000 20.22000 ? 199 TYR A C   1 
ATOM   1528 O  O   . TYR A 1 199 ? 34.67900  4.10800   14.39600 1.000 16.70000 ? 199 TYR A O   1 
ATOM   1529 C  CB  . TYR A 1 199 ? 34.85200  2.81000   17.39900 1.000 14.46000 ? 199 TYR A CB  1 
ATOM   1530 C  CG  . TYR A 1 199 ? 33.66300  2.15200   16.75500 1.000 17.35000 ? 199 TYR A CG  1 
ATOM   1531 C  CD1 . TYR A 1 199 ? 33.74500  0.85600   16.25800 1.000 18.59000 ? 199 TYR A CD1 1 
ATOM   1532 C  CD2 . TYR A 1 199 ? 32.43800  2.81400   16.66900 1.000 15.29000 ? 199 TYR A CD2 1 
ATOM   1533 C  CE1 . TYR A 1 199 ? 32.63800  0.23700   15.67600 1.000 19.85000 ? 199 TYR A CE1 1 
ATOM   1534 C  CE2 . TYR A 1 199 ? 31.33400  2.20800   16.08500 1.000 15.65000 ? 199 TYR A CE2 1 
ATOM   1535 C  CZ  . TYR A 1 199 ? 31.43900  0.92400   15.59000 1.000 18.50000 ? 199 TYR A CZ  1 
ATOM   1536 O  OH  . TYR A 1 199 ? 30.34900  0.32000   15.01600 1.000 16.81000 ? 199 TYR A OH  1 
ATOM   1537 N  N   . TRP A 1 200 ? 34.76300  5.68900   15.99600 1.000 13.46000 ? 200 TRP A N   1 
ATOM   1538 C  CA  . TRP A 1 200 ? 33.92900  6.62400   15.25800 1.000 17.48000 ? 200 TRP A CA  1 
ATOM   1539 C  C   . TRP A 1 200 ? 34.72100  7.45300   14.26100 1.000 15.15000 ? 200 TRP A C   1 
ATOM   1540 O  O   . TRP A 1 200 ? 34.11700  8.19600   13.47100 1.000 14.27000 ? 200 TRP A O   1 
ATOM   1541 C  CB  . TRP A 1 200 ? 33.19300  7.54500   16.23900 1.000 13.78000 ? 200 TRP A CB  1 
ATOM   1542 C  CG  . TRP A 1 200 ? 32.28700  6.79100   17.16100 1.000 17.31000 ? 200 TRP A CG  1 
ATOM   1543 C  CD1 . TRP A 1 200 ? 32.64100  6.14400   18.30700 1.000 15.47000 ? 200 TRP A CD1 1 
ATOM   1544 C  CD2 . TRP A 1 200 ? 30.86900  6.62300   17.02400 1.000 16.53000 ? 200 TRP A CD2 1 
ATOM   1545 N  NE1 . TRP A 1 200 ? 31.53800  5.56700   18.88400 1.000 16.08000 ? 200 TRP A NE1 1 
ATOM   1546 C  CE2 . TRP A 1 200 ? 30.43600  5.84300   18.11800 1.000 14.06000 ? 200 TRP A CE2 1 
ATOM   1547 C  CE3 . TRP A 1 200 ? 29.93000  7.04600   16.08000 1.000 16.93000 ? 200 TRP A CE3 1 
ATOM   1548 C  CZ2 . TRP A 1 200 ? 29.10500  5.46900   18.29300 1.000 15.23000 ? 200 TRP A CZ2 1 
ATOM   1549 C  CZ3 . TRP A 1 200 ? 28.58800  6.67700   16.26000 1.000 15.90000 ? 200 TRP A CZ3 1 
ATOM   1550 C  CH2 . TRP A 1 200 ? 28.19300  5.90300   17.36100 1.000 13.45000 ? 200 TRP A CH2 1 
ATOM   1551 N  N   . ASP A 1 201 ? 36.05100  7.33600   14.27300 1.000 13.90000 ? 201 ASP A N   1 
ATOM   1552 C  CA  . ASP A 1 201 ? 36.87200  8.22800   13.45900 1.000 15.02000 ? 201 ASP A CA  1 
ATOM   1553 C  C   . ASP A 1 201 ? 36.51800  8.19300   11.97400 1.000 13.28000 ? 201 ASP A C   1 
ATOM   1554 O  O   . ASP A 1 201 ? 36.49900  9.26800   11.35200 1.000 16.14000 ? 201 ASP A O   1 
ATOM   1555 C  CB  . ASP A 1 201 ? 38.35400  7.90200   13.68400 1.000 15.43000 ? 201 ASP A CB  1 
ATOM   1556 C  CG  . ASP A 1 201 ? 38.85200  8.37300   15.04000 1.000 18.63000 ? 201 ASP A CG  1 
ATOM   1557 O  OD1 . ASP A 1 201 ? 38.03400  8.89400   15.82300 1.000 18.70000 ? 201 ASP A OD1 1 
ATOM   1558 O  OD2 . ASP A 1 201 ? 40.06100  8.23400   15.31600 1.000 21.25000 ? 201 ASP A OD2 1 
ATOM   1559 N  N   . PRO A 1 202 ? 36.25600  7.04500   11.34600 1.000 13.55000 ? 202 PRO A N   1 
ATOM   1560 C  CA  . PRO A 1 202 ? 35.87800  7.09400   9.92300  1.000 15.28000 ? 202 PRO A CA  1 
ATOM   1561 C  C   . PRO A 1 202 ? 34.53200  7.74900   9.69800  1.000 16.95000 ? 202 PRO A C   1 
ATOM   1562 O  O   . PRO A 1 202 ? 34.30100  8.30000   8.61500  1.000 12.59000 ? 202 PRO A O   1 
ATOM   1563 C  CB  . PRO A 1 202 ? 35.86900  5.62200   9.48600  1.000 13.59000 ? 202 PRO A CB  1 
ATOM   1564 C  CG  . PRO A 1 202 ? 35.97200  4.82400   10.68600 1.000 23.16000 ? 202 PRO A CG  1 
ATOM   1565 C  CD  . PRO A 1 202 ? 36.50700  5.67100   11.80800 1.000 17.08000 ? 202 PRO A CD  1 
ATOM   1566 N  N   . ILE A 1 203 ? 33.63100  7.67100   10.67800 1.000 12.62000 ? 203 ILE A N   1 
ATOM   1567 C  CA  . ILE A 1 203 ? 32.37500  8.41300   10.59500 1.000 13.09000 ? 203 ILE A CA  1 
ATOM   1568 C  C   . ILE A 1 203 ? 32.62900  9.90800   10.74100 1.000 14.52000 ? 203 ILE A C   1 
ATOM   1569 O  O   . ILE A 1 203 ? 32.09600  10.71800  9.97300  1.000 14.23000 ? 203 ILE A O   1 
ATOM   1570 C  CB  . ILE A 1 203 ? 31.38500  7.89700   11.65000 1.000 12.80000 ? 203 ILE A CB  1 
ATOM   1571 C  CG1 . ILE A 1 203 ? 31.03600  6.43200   11.34100 1.000 12.98000 ? 203 ILE A CG1 1 
ATOM   1572 C  CG2 . ILE A 1 203 ? 30.12700  8.81000   11.69400 1.000 14.49000 ? 203 ILE A CG2 1 
ATOM   1573 C  CD1 . ILE A 1 203 ? 30.50900  5.63400   12.55300 1.000 13.75000 ? 203 ILE A CD1 1 
ATOM   1574 N  N   . PHE A 1 204 ? 33.43600  10.29500  11.73700 1.000 16.12000 ? 204 PHE A N   1 
ATOM   1575 C  CA  . PHE A 1 204 ? 33.81000  11.69400  11.89800 1.000 9.81000  ? 204 PHE A CA  1 
ATOM   1576 C  C   . PHE A 1 204 ? 34.44200  12.22700  10.62100 1.000 16.72000 ? 204 PHE A C   1 
ATOM   1577 O  O   . PHE A 1 204 ? 34.15400  13.34800  10.18400 1.000 14.90000 ? 204 PHE A O   1 
ATOM   1578 C  CB  . PHE A 1 204 ? 34.80500  11.85300  13.04900 1.000 14.67000 ? 204 PHE A CB  1 
ATOM   1579 C  CG  . PHE A 1 204 ? 34.24900  11.56100  14.41600 1.000 17.26000 ? 204 PHE A CG  1 
ATOM   1580 C  CD1 . PHE A 1 204 ? 32.89000  11.37000  14.62600 1.000 17.40000 ? 204 PHE A CD1 1 
ATOM   1581 C  CD2 . PHE A 1 204 ? 35.10900  11.48100  15.50400 1.000 18.05000 ? 204 PHE A CD2 1 
ATOM   1582 C  CE1 . PHE A 1 204 ? 32.40100  11.10300  15.90700 1.000 16.77000 ? 204 PHE A CE1 1 
ATOM   1583 C  CE2 . PHE A 1 204 ? 34.62400  11.21600  16.78400 1.000 17.87000 ? 204 PHE A CE2 1 
ATOM   1584 C  CZ  . PHE A 1 204 ? 33.27700  11.03200  16.98300 1.000 14.36000 ? 204 PHE A CZ  1 
ATOM   1585 N  N   . LYS A 1 205 ? 35.31800  11.42400  10.01900 1.000 12.03000 ? 205 LYS A N   1 
ATOM   1586 C  CA  . LYS A 1 205 ? 36.03900  11.84600  8.82600  1.000 15.26000 ? 205 LYS A CA  1 
ATOM   1587 C  C   . LYS A 1 205 ? 35.07800  12.11300  7.68100  1.000 15.45000 ? 205 LYS A C   1 
ATOM   1588 O  O   . LYS A 1 205 ? 35.17800  13.14100  6.99800  1.000 13.61000 ? 205 LYS A O   1 
ATOM   1589 C  CB  . LYS A 1 205 ? 37.05400  10.77100  8.43700  1.000 14.55000 ? 205 LYS A CB  1 
ATOM   1590 C  CG  . LYS A 1 205 ? 37.91700  11.14400  7.23000  1.000 18.32000 ? 205 LYS A CG  1 
ATOM   1591 C  CD  . LYS A 1 205 ? 39.03700  10.12900  7.05600  1.000 19.73000 ? 205 LYS A CD  1 
ATOM   1592 C  CE  . LYS A 1 205 ? 40.22300  10.72500  6.31100  1.000 30.14000 ? 205 LYS A CE  1 
ATOM   1593 N  NZ  . LYS A 1 205 ? 41.42800  9.87500   6.49700  1.000 30.73000 ? 205 LYS A NZ  1 
ATOM   1594 N  N   . ALA A 1 206 ? 34.12700  11.19300  7.46500  1.000 12.78000 ? 206 ALA A N   1 
ATOM   1595 C  CA  . ALA A 1 206 ? 33.17700  11.34600  6.36800  1.000 14.43000 ? 206 ALA A CA  1 
ATOM   1596 C  C   . ALA A 1 206 ? 32.24700  12.53300  6.59800  1.000 14.25000 ? 206 ALA A C   1 
ATOM   1597 O  O   . ALA A 1 206 ? 31.87600  13.22500  5.64400  1.000 13.98000 ? 206 ALA A O   1 
ATOM   1598 C  CB  . ALA A 1 206 ? 32.37700  10.06100  6.18800  1.000 11.82000 ? 206 ALA A CB  1 
ATOM   1599 N  N   . CYS A 1 207 ? 31.85200  12.78200  7.85300  1.000 14.17000 ? 207 CYS A N   1 
ATOM   1600 C  CA  . CYS A 1 207 ? 31.01100  13.94200  8.15100  1.000 13.04000 ? 207 CYS A CA  1 
ATOM   1601 C  C   . CYS A 1 207 ? 31.72400  15.25100  7.83500  1.000 14.03000 ? 207 CYS A C   1 
ATOM   1602 O  O   . CYS A 1 207 ? 31.11900  16.17300  7.27500  1.000 13.58000 ? 207 CYS A O   1 
ATOM   1603 C  CB  . CYS A 1 207 ? 30.57100  13.92100  9.61300  1.000 13.06000 ? 207 CYS A CB  1 
ATOM   1604 S  SG  . CYS A 1 207 ? 29.28500  12.66900  9.93000  1.000 15.89000 ? 207 CYS A SG  1 
ATOM   1605 N  N   . VAL A 1 208 ? 32.99400  15.37500  8.23300  1.000 13.36000 ? 208 VAL A N   1 
ATOM   1606 C  CA  . VAL A 1 208 ? 33.75100  16.58200  7.89000  1.000 13.52000 ? 208 VAL A CA  1 
ATOM   1607 C  C   . VAL A 1 208 ? 33.81800  16.74600  6.38100  1.000 13.82000 ? 208 VAL A C   1 
ATOM   1608 O  O   . VAL A 1 208 ? 33.64900  17.84800  5.85400  1.000 16.03000 ? 208 VAL A O   1 
ATOM   1609 C  CB  . VAL A 1 208 ? 35.16300  16.55200  8.50700  1.000 16.16000 ? 208 VAL A CB  1 
ATOM   1610 C  CG1 . VAL A 1 208 ? 36.02300  17.68800  7.92500  1.000 16.45000 ? 208 VAL A CG1 1 
ATOM   1611 C  CG2 . VAL A 1 208 ? 35.08800  16.66100  10.02100 1.000 14.48000 ? 208 VAL A CG2 1 
ATOM   1612 N  N   . GLU A 1 209 ? 34.02700  15.64900  5.66100  1.000 14.04000 ? 209 GLU A N   1 
ATOM   1613 C  CA  . GLU A 1 209 ? 34.14300  15.74100  4.20700  1.000 17.15000 ? 209 GLU A CA  1 
ATOM   1614 C  C   . GLU A 1 209 ? 32.87900  16.30700  3.57800  1.000 18.20000 ? 209 GLU A C   1 
ATOM   1615 O  O   . GLU A 1 209 ? 32.94400  16.98000  2.54400  1.000 18.29000 ? 209 GLU A O   1 
ATOM   1616 C  CB  . GLU A 1 209 ? 34.45500  14.36700  3.63000  1.000 17.49000 ? 209 GLU A CB  1 
ATOM   1617 C  CG  . GLU A 1 209 ? 35.87400  13.92900  3.88400  1.000 17.39000 ? 209 GLU A CG  1 
ATOM   1618 C  CD  . GLU A 1 209 ? 36.87000  14.86700  3.26800  1.000 21.63000 ? 209 GLU A CD  1 
ATOM   1619 O  OE1 . GLU A 1 209 ? 36.87100  14.98200  2.02700  1.000 23.29000 ? 209 GLU A OE1 1 
ATOM   1620 O  OE2 . GLU A 1 209 ? 37.64800  15.48800  4.01900  1.000 21.45000 ? 209 GLU A OE2 1 
ATOM   1621 N  N   . HIS A 1 210 ? 31.72200  16.07200  4.19800  1.000 15.19000 ? 210 HIS A N   1 
ATOM   1622 C  CA  . HIS A 1 210 ? 30.45400  16.55800  3.67900  1.000 13.98000 ? 210 HIS A CA  1 
ATOM   1623 C  C   . HIS A 1 210 ? 29.90000  17.73400  4.47300  1.000 14.66000 ? 210 HIS A C   1 
ATOM   1624 O  O   . HIS A 1 210 ? 28.75400  18.14800  4.23300  1.000 14.96000 ? 210 HIS A O   1 
ATOM   1625 C  CB  . HIS A 1 210 ? 29.44200  15.40900  3.64900  1.000 14.70000 ? 210 HIS A CB  1 
ATOM   1626 C  CG  . HIS A 1 210 ? 29.78900  14.34200  2.66000  1.000 15.56000 ? 210 HIS A CG  1 
ATOM   1627 N  ND1 . HIS A 1 210 ? 29.77100  14.55700  1.29900  1.000 17.38000 ? 210 HIS A ND1 1 
ATOM   1628 C  CD2 . HIS A 1 210 ? 30.17400  13.05700  2.83200  1.000 11.99000 ? 210 HIS A CD2 1 
ATOM   1629 C  CE1 . HIS A 1 210 ? 30.12800  13.44900  0.67400  1.000 16.86000 ? 210 HIS A CE1 1 
ATOM   1630 N  NE2 . HIS A 1 210 ? 30.37600  12.52200  1.58100  1.000 16.87000 ? 210 HIS A NE2 1 
ATOM   1631 N  N   . ASN A 1 211 ? 30.67100  18.26300  5.42400  1.000 14.25000 ? 211 ASN A N   1 
ATOM   1632 C  CA  . ASN A 1 211 ? 30.23500  19.37100  6.27600  1.000 13.50000 ? 211 ASN A CA  1 
ATOM   1633 C  C   . ASN A 1 211 ? 28.96400  19.00800  7.04800  1.000 17.62000 ? 211 ASN A C   1 
ATOM   1634 O  O   . ASN A 1 211 ? 28.07200  19.83500  7.24800  1.000 19.12000 ? 211 ASN A O   1 
ATOM   1635 C  CB  . ASN A 1 211 ? 30.03600  20.64800  5.44600  1.000 23.27000 ? 211 ASN A CB  1 
ATOM   1636 C  CG  . ASN A 1 211 ? 30.14000  21.91700  6.27600  1.000 29.41000 ? 211 ASN A CG  1 
ATOM   1637 O  OD1 . ASN A 1 211 ? 30.76100  21.93000  7.33900  1.000 31.59000 ? 211 ASN A OD1 1 
ATOM   1638 N  ND2 . ASN A 1 211 ? 29.53700  22.99600  5.78400  1.000 31.73000 ? 211 ASN A ND2 1 
ATOM   1639 N  N   . ILE A 1 212 ? 28.87300  17.76000  7.47600  1.000 14.97000 ? 212 ILE A N   1 
ATOM   1640 C  CA  . ILE A 1 212 ? 27.68200  17.25700  8.15100  1.000 13.61000 ? 212 ILE A CA  1 
ATOM   1641 C  C   . ILE A 1 212 ? 27.87300  17.37300  9.66000  1.000 14.29000 ? 212 ILE A C   1 
ATOM   1642 O  O   . ILE A 1 212 ? 28.91700  16.98300  10.19400 1.000 15.07000 ? 212 ILE A O   1 
ATOM   1643 C  CB  . ILE A 1 212 ? 27.39200  15.81500  7.70800  1.000 12.94000 ? 212 ILE A CB  1 
ATOM   1644 C  CG1 . ILE A 1 212 ? 26.85800  15.85600  6.27100  1.000 14.26000 ? 212 ILE A CG1 1 
ATOM   1645 C  CG2 . ILE A 1 212 ? 26.40800  15.09800  8.66300  1.000 9.74000  ? 212 ILE A CG2 1 
ATOM   1646 C  CD1 . ILE A 1 212 ? 26.38500  14.54300  5.73200  1.000 13.47000 ? 212 ILE A CD1 1 
ATOM   1647 N  N   . VAL A 1 213 ? 26.86800  17.95100  10.34300 1.000 12.88000 ? 213 VAL A N   1 
ATOM   1648 C  CA  . VAL A 1 213 ? 26.89700  18.19100  11.78800 1.000 13.01000 ? 213 VAL A CA  1 
ATOM   1649 C  C   . VAL A 1 213 ? 26.54500  16.91500  12.54700 1.000 12.05000 ? 213 VAL A C   1 
ATOM   1650 O  O   . VAL A 1 213 ? 25.59700  16.20600  12.19700 1.000 13.10000 ? 213 VAL A O   1 
ATOM   1651 C  CB  . VAL A 1 213 ? 25.90400  19.31100  12.16600 1.000 13.99000 ? 213 VAL A CB  1 
ATOM   1652 C  CG1 . VAL A 1 213 ? 25.82600  19.46800  13.70000 1.000 13.87000 ? 213 VAL A CG1 1 
ATOM   1653 C  CG2 . VAL A 1 213 ? 26.23200  20.62500  11.47900 1.000 12.45000 ? 213 VAL A CG2 1 
ATOM   1654 N  N   . LEU A 1 214 ? 27.28300  16.62700  13.61500 1.000 12.73000 ? 214 LEU A N   1 
ATOM   1655 C  CA  . LEU A 1 214 ? 26.86600  15.58800  14.54900 1.000 11.43000 ? 214 LEU A CA  1 
ATOM   1656 C  C   . LEU A 1 214 ? 25.88300  16.18100  15.54300 1.000 13.81000 ? 214 LEU A C   1 
ATOM   1657 O  O   . LEU A 1 214 ? 26.25500  17.06400  16.31800 1.000 10.80000 ? 214 LEU A O   1 
ATOM   1658 C  CB  . LEU A 1 214 ? 28.05900  15.02500  15.31000 1.000 9.95000  ? 214 LEU A CB  1 
ATOM   1659 C  CG  . LEU A 1 214 ? 29.22500  14.56100  14.45200 1.000 11.68000 ? 214 LEU A CG  1 
ATOM   1660 C  CD1 . LEU A 1 214 ? 30.37600  14.21700  15.37500 1.000 11.19000 ? 214 LEU A CD1 1 
ATOM   1661 C  CD2 . LEU A 1 214 ? 28.78600  13.33900  13.67600 1.000 12.57000 ? 214 LEU A CD2 1 
ATOM   1662 N  N   . SER A 1 215 ? 24.64400  15.68400  15.55200 1.000 13.02000 ? 215 SER A N   1 
ATOM   1663 C  CA  . SER A 1 215 ? 23.66500  16.10800  16.54200 1.000 10.23000 ? 215 SER A CA  1 
ATOM   1664 C  C   . SER A 1 215 ? 23.68800  15.09500  17.67700 1.000 11.45000 ? 215 SER A C   1 
ATOM   1665 O  O   . SER A 1 215 ? 23.44600  13.90300  17.45200 1.000 13.68000 ? 215 SER A O   1 
ATOM   1666 C  CB  . SER A 1 215 ? 22.26700  16.21900  15.93500 1.000 11.18000 ? 215 SER A CB  1 
ATOM   1667 O  OG  . SER A 1 215 ? 22.13800  17.35800  15.09700 1.000 11.75000 ? 215 SER A OG  1 
ATOM   1668 N  N   . LEU A 1 216 ? 24.02300  15.55700  18.87800 1.000 10.25000 ? 216 LEU A N   1 
ATOM   1669 C  CA  . LEU A 1 216 ? 24.05200  14.71000  20.07100 1.000 12.55000 ? 216 LEU A CA  1 
ATOM   1670 C  C   . LEU A 1 216 ? 22.86900  15.12300  20.94200 1.000 14.35000 ? 216 LEU A C   1 
ATOM   1671 O  O   . LEU A 1 216 ? 22.98700  16.01100  21.78500 1.000 13.03000 ? 216 LEU A O   1 
ATOM   1672 C  CB  . LEU A 1 216 ? 25.38700  14.84200  20.82400 1.000 10.52000 ? 216 LEU A CB  1 
ATOM   1673 C  CG  . LEU A 1 216 ? 26.58900  14.00900  20.36300 1.000 16.71000 ? 216 LEU A CG  1 
ATOM   1674 C  CD1 . LEU A 1 216 ? 26.86600  14.11400  18.86600 1.000 16.37000 ? 216 LEU A CD1 1 
ATOM   1675 C  CD2 . LEU A 1 216 ? 27.82800  14.43500  21.12800 1.000 15.98000 ? 216 LEU A CD2 1 
ATOM   1676 N  N   . HIS A 1 217 ? 21.72800  14.46600  20.72400 1.000 13.77000 ? 217 HIS A N   1 
ATOM   1677 C  CA  . HIS A 1 217 ? 20.48300  14.79100  21.40400 1.000 12.51000 ? 217 HIS A CA  1 
ATOM   1678 C  C   . HIS A 1 217 ? 20.44500  14.17500  22.80300 1.000 14.73000 ? 217 HIS A C   1 
ATOM   1679 O  O   . HIS A 1 217 ? 20.93700  13.06500  23.01800 1.000 16.90000 ? 217 HIS A O   1 
ATOM   1680 C  CB  . HIS A 1 217 ? 19.30600  14.27500  20.57800 1.000 12.17000 ? 217 HIS A CB  1 
ATOM   1681 C  CG  . HIS A 1 217 ? 17.97700  14.83200  20.99100 1.000 16.41000 ? 217 HIS A CG  1 
ATOM   1682 N  ND1 . HIS A 1 217 ? 17.31100  14.40900  22.12000 1.000 15.75000 ? 217 HIS A ND1 1 
ATOM   1683 C  CD2 . HIS A 1 217 ? 17.16500  15.74100  20.39800 1.000 16.80000 ? 217 HIS A CD2 1 
ATOM   1684 C  CE1 . HIS A 1 217 ? 16.16000  15.05100  22.21900 1.000 14.04000 ? 217 HIS A CE1 1 
ATOM   1685 N  NE2 . HIS A 1 217 ? 16.05000  15.87000  21.19100 1.000 10.88000 ? 217 HIS A NE2 1 
ATOM   1686 N  N   . ILE A 1 218 ? 19.86400  14.90900  23.76000 1.000 13.62000 ? 218 ILE A N   1 
ATOM   1687 C  CA  . ILE A 1 218 ? 19.71600  14.38700  25.12900 1.000 16.01000 ? 218 ILE A CA  1 
ATOM   1688 C  C   . ILE A 1 218 ? 18.91600  13.08100  25.13100 1.000 16.90000 ? 218 ILE A C   1 
ATOM   1689 O  O   . ILE A 1 218 ? 18.14200  12.78100  24.21400 1.000 15.52000 ? 218 ILE A O   1 
ATOM   1690 C  CB  . ILE A 1 218 ? 19.03600  15.41400  26.05000 1.000 17.22000 ? 218 ILE A CB  1 
ATOM   1691 C  CG1 . ILE A 1 218 ? 17.56800  15.56500  25.65400 1.000 16.51000 ? 218 ILE A CG1 1 
ATOM   1692 C  CG2 . ILE A 1 218 ? 19.76100  16.74700  25.99700 1.000 19.33000 ? 218 ILE A CG2 1 
ATOM   1693 C  CD1 . ILE A 1 218 ? 16.77000  16.47300  26.57800 1.000 14.59000 ? 218 ILE A CD1 1 
ATOM   1694 N  N   . GLY A 1 219 ? 19.07100  12.32400  26.21400 1.000 20.13000 ? 219 GLY A N   1 
ATOM   1695 C  CA  . GLY A 1 219 ? 18.40600  11.04400  26.38700 1.000 18.86000 ? 219 GLY A CA  1 
ATOM   1696 C  C   . GLY A 1 219 ? 19.35300  9.88300   26.60000 1.000 18.08000 ? 219 GLY A C   1 
ATOM   1697 O  O   . GLY A 1 219 ? 18.91300  8.81300   27.04200 1.000 21.70000 ? 219 GLY A O   1 
ATOM   1698 N  N   . GLY A 1 220 ? 20.63900  10.04400  26.29000 1.000 18.48000 ? 220 GLY A N   1 
ATOM   1699 C  CA  . GLY A 1 220 ? 21.59700  8.97000   26.50300 1.000 17.92000 ? 220 GLY A CA  1 
ATOM   1700 C  C   . GLY A 1 220 ? 22.27100  9.10100   27.85300 1.000 18.18000 ? 220 GLY A C   1 
ATOM   1701 O  O   . GLY A 1 220 ? 22.43200  8.12200   28.58900 1.000 19.83000 ? 220 GLY A O   1 
ATOM   1702 N  N   . GLY A 1 221 ? 22.64500  10.33100  28.19500 1.000 16.82000 ? 221 GLY A N   1 
ATOM   1703 C  CA  . GLY A 1 221 ? 23.31100  10.57200  29.47000 1.000 20.40000 ? 221 GLY A CA  1 
ATOM   1704 C  C   . GLY A 1 221 ? 22.47100  10.16900  30.66900 1.000 18.67000 ? 221 GLY A C   1 
ATOM   1705 O  O   . GLY A 1 221 ? 23.00000  9.64700   31.65400 1.000 18.80000 ? 221 GLY A O   1 
ATOM   1706 N  N   . ILE A 1 222 ? 21.15300  10.40700  30.60600 1.000 17.45000 ? 222 ILE A N   1 
ATOM   1707 C  CA  . ILE A 1 222 ? 20.29000  10.01500  31.72300 1.000 17.37000 ? 222 ILE A CA  1 
ATOM   1708 C  C   . ILE A 1 222 ? 20.36800  8.50900   31.96500 1.000 22.04000 ? 222 ILE A C   1 
ATOM   1709 O  O   . ILE A 1 222 ? 20.33700  8.05400   33.11600 1.000 19.23000 ? 222 ILE A O   1 
ATOM   1710 C  CB  . ILE A 1 222 ? 18.83800  10.49900  31.48900 1.000 18.45000 ? 222 ILE A CB  1 
ATOM   1711 C  CG1 . ILE A 1 222 ? 18.01400  10.40100  32.78000 1.000 19.48000 ? 222 ILE A CG1 1 
ATOM   1712 C  CG2 . ILE A 1 222 ? 18.14300  9.70400   30.38600 1.000 18.52000 ? 222 ILE A CG2 1 
ATOM   1713 C  CD1 . ILE A 1 222 ? 18.60700  11.12700  33.96900 1.000 23.92000 ? 222 ILE A CD1 1 
ATOM   1714 N  N   . ASN A 1 223 ? 20.52800  7.71000   30.90500 1.000 21.79000 ? 223 ASN A N   1 
ATOM   1715 C  CA  . ASN A 1 223 ? 20.60500  6.26500   31.09500 1.000 22.38000 ? 223 ASN A CA  1 
ATOM   1716 C  C   . ASN A 1 223 ? 21.91000  5.81900   31.74800 1.000 18.85000 ? 223 ASN A C   1 
ATOM   1717 O  O   . ASN A 1 223 ? 22.04000  4.64000   32.09800 1.000 23.16000 ? 223 ASN A O   1 
ATOM   1718 C  CB  . ASN A 1 223 ? 20.40000  5.56000   29.75700 1.000 22.96000 ? 223 ASN A CB  1 
ATOM   1719 C  CG  . ASN A 1 223 ? 18.95000  5.63600   29.27900 1.000 32.02000 ? 223 ASN A CG  1 
ATOM   1720 O  OD1 . ASN A 1 223 ? 18.03300  5.86400   30.07100 1.000 26.03000 ? 223 ASN A OD1 1 
ATOM   1721 N  ND2 . ASN A 1 223 ? 18.74300  5.45400   27.97700 1.000 27.22000 ? 223 ASN A ND2 1 
ATOM   1722 N  N   . LEU A 1 224 ? 22.87100  6.72300   31.92400 1.000 15.61000 ? 224 LEU A N   1 
ATOM   1723 C  CA  . LEU A 1 224 ? 24.09800  6.40700   32.64900 1.000 15.03000 ? 224 LEU A CA  1 
ATOM   1724 C  C   . LEU A 1 224 ? 23.95600  6.53800   34.16000 1.000 19.19000 ? 224 LEU A C   1 
ATOM   1725 O  O   . LEU A 1 224 ? 24.81900  6.03700   34.89300 1.000 17.18000 ? 224 LEU A O   1 
ATOM   1726 C  CB  . LEU A 1 224 ? 25.23000  7.34100   32.21700 1.000 16.22000 ? 224 LEU A CB  1 
ATOM   1727 C  CG  . LEU A 1 224 ? 25.56500  7.40100   30.73900 1.000 16.27000 ? 224 LEU A CG  1 
ATOM   1728 C  CD1 . LEU A 1 224 ? 26.57300  8.50000   30.54500 1.000 18.06000 ? 224 LEU A CD1 1 
ATOM   1729 C  CD2 . LEU A 1 224 ? 26.13000  6.06700   30.30300 1.000 17.43000 ? 224 LEU A CD2 1 
ATOM   1730 N  N   . VAL A 1 225 ? 22.90900  7.20100   34.64100 1.000 16.89000 ? 225 VAL A N   1 
ATOM   1731 C  CA  . VAL A 1 225 ? 22.84600  7.67400   36.02100 1.000 15.72000 ? 225 VAL A CA  1 
ATOM   1732 C  C   . VAL A 1 225 ? 22.01800  6.71000   36.85400 1.000 15.65000 ? 225 VAL A C   1 
ATOM   1733 O  O   . VAL A 1 225 ? 20.81300  6.55800   36.62900 1.000 16.61000 ? 225 VAL A O   1 
ATOM   1734 C  CB  . VAL A 1 225 ? 22.27000  9.09500   36.09800 1.000 15.94000 ? 225 VAL A CB  1 
ATOM   1735 C  CG1 . VAL A 1 225 ? 22.35000  9.61700   37.53600 1.000 15.28000 ? 225 VAL A CG1 1 
ATOM   1736 C  CG2 . VAL A 1 225 ? 23.03900  10.01800  35.16500 1.000 15.59000 ? 225 VAL A CG2 1 
ATOM   1737 N  N   . LYS A 1 226 ? 22.65700  6.07400   37.83300 1.000 14.82000 ? 226 LYS A N   1 
ATOM   1738 C  CA  . LYS A 1 226 ? 21.92000  5.26000   38.78700 1.000 14.24000 ? 226 LYS A CA  1 
ATOM   1739 C  C   . LYS A 1 226 ? 20.92300  6.13700   39.53300 1.000 18.55000 ? 226 LYS A C   1 
ATOM   1740 O  O   . LYS A 1 226 ? 21.24400  7.26000   39.93100 1.000 15.01000 ? 226 LYS A O   1 
ATOM   1741 C  CB  . LYS A 1 226 ? 22.87800  4.59700   39.77500 1.000 13.59000 ? 226 LYS A CB  1 
ATOM   1742 C  CG  . LYS A 1 226 ? 22.15600  3.81800   40.89400 1.000 20.34000 ? 226 LYS A CG  1 
ATOM   1743 C  CD  . LYS A 1 226 ? 23.13600  3.34100   41.96800 1.000 21.33000 ? 226 LYS A CD  1 
ATOM   1744 C  CE  . LYS A 1 226 ? 24.21800  2.43500   41.38500 1.000 28.09000 ? 226 LYS A CE  1 
ATOM   1745 N  NZ  . LYS A 1 226 ? 25.22200  1.95900   42.40200 1.000 23.50000 ? 226 LYS A NZ  1 
ATOM   1746 N  N   . ARG A 1 227 ? 19.70300  5.63400   39.69800 1.000 14.32000 ? 227 ARG A N   1 
ATOM   1747 C  CA  . ARG A 1 227 ? 18.67400  6.30100   40.47600 1.000 16.12000 ? 227 ARG A CA  1 
ATOM   1748 C  C   . ARG A 1 227 ? 18.17500  5.37100   41.57500 1.000 20.25000 ? 227 ARG A C   1 
ATOM   1749 O  O   . ARG A 1 227 ? 18.34800  4.14900   41.49000 1.000 17.31000 ? 227 ARG A O   1 
ATOM   1750 C  CB  . ARG A 1 227 ? 17.49300  6.72700   39.58700 1.000 17.24000 ? 227 ARG A CB  1 
ATOM   1751 C  CG  . ARG A 1 227 ? 17.87900  7.27200   38.20500 1.000 19.53000 ? 227 ARG A CG  1 
ATOM   1752 C  CD  . ARG A 1 227 ? 18.68700  8.57400   38.25600 1.000 21.71000 ? 227 ARG A CD  1 
ATOM   1753 N  NE  . ARG A 1 227 ? 18.07800  9.63900   39.06300 1.000 20.38000 ? 227 ARG A NE  1 
ATOM   1754 C  CZ  . ARG A 1 227 ? 18.64600  10.17400  40.14400 1.000 20.14000 ? 227 ARG A CZ  1 
ATOM   1755 N  NH1 . ARG A 1 227 ? 19.82900  9.74700   40.56700 1.000 14.08000 ? 227 ARG A NH1 1 
ATOM   1756 N  NH2 . ARG A 1 227 ? 18.03300  11.13900  40.81300 1.000 19.67000 ? 227 ARG A NH2 1 
ATOM   1757 N  N   . PRO A 1 228 ? 17.54500  5.90900   42.61900 1.000 19.30000 ? 228 PRO A N   1 
ATOM   1758 C  CA  . PRO A 1 228 ? 16.92400  5.04100   43.62600 1.000 22.56000 ? 228 PRO A CA  1 
ATOM   1759 C  C   . PRO A 1 228 ? 15.77100  4.24700   43.02600 1.000 22.18000 ? 228 PRO A C   1 
ATOM   1760 O  O   . PRO A 1 228 ? 15.25000  4.53700   41.94200 1.000 22.98000 ? 228 PRO A O   1 
ATOM   1761 C  CB  . PRO A 1 228 ? 16.44400  6.01700   44.70800 1.000 21.29000 ? 228 PRO A CB  1 
ATOM   1762 C  CG  . PRO A 1 228 ? 16.26900  7.31400   43.99100 1.000 22.13000 ? 228 PRO A CG  1 
ATOM   1763 C  CD  . PRO A 1 228 ? 17.32600  7.33400   42.91200 1.000 16.29000 ? 228 PRO A CD  1 
ATOM   1764 N  N   . GLU A 1 229 ? 15.35100  3.24100   43.79200 1.000 29.36000 ? 229 GLU A N   1 
ATOM   1765 C  CA  . GLU A 1 229 ? 14.42100  2.22800   43.30200 1.000 31.36000 ? 229 GLU A CA  1 
ATOM   1766 C  C   . GLU A 1 229 ? 13.14900  2.82400   42.69500 1.000 27.37000 ? 229 GLU A C   1 
ATOM   1767 O  O   . GLU A 1 229 ? 12.77100  2.48500   41.56500 1.000 41.95000 ? 229 GLU A O   1 
ATOM   1768 C  CB  . GLU A 1 229 ? 14.06500  1.28700   44.44800 1.000 36.65000 ? 229 GLU A CB  1 
ATOM   1769 C  CG  . GLU A 1 229 ? 13.22000  0.11000   44.04600 1.000 35.40000 ? 229 GLU A CG  1 
ATOM   1770 C  CD  . GLU A 1 229 ? 13.17400  -0.92100  45.14800 1.000 34.73000 ? 229 GLU A CD  1 
ATOM   1771 O  OE1 . GLU A 1 229 ? 14.25400  -1.37200  45.58800 1.000 44.33000 ? 229 GLU A OE1 1 
ATOM   1772 O  OE2 . GLU A 1 229 ? 12.06900  -1.26400  45.58300 1.000 30.19000 ? 229 GLU A OE2 1 
ATOM   1773 N  N   . GLY A 1 230 ? 12.46900  3.69500   43.42400 1.000 26.83000 ? 230 GLY A N   1 
ATOM   1774 C  CA  . GLY A 1 230 ? 11.17000  4.15900   42.95500 1.000 38.77000 ? 230 GLY A CA  1 
ATOM   1775 C  C   . GLY A 1 230 ? 11.20400  5.16700   41.81600 1.000 43.30000 ? 230 GLY A C   1 
ATOM   1776 O  O   . GLY A 1 230 ? 11.58900  6.32100   42.03700 1.000 44.85000 ? 230 GLY A O   1 
ATOM   1777 N  N   . PHE A 1 231 ? 10.79400  4.75400   40.60300 1.000 44.24000 ? 231 PHE A N   1 
ATOM   1778 C  CA  . PHE A 1 231 ? 10.80600  5.61800   39.41900 1.000 49.28000 ? 231 PHE A CA  1 
ATOM   1779 C  C   . PHE A 1 231 ? 10.09700  6.93800   39.67700 1.000 49.07000 ? 231 PHE A C   1 
ATOM   1780 O  O   . PHE A 1 231 ? 8.86900   6.96800   39.82800 1.000 50.52000 ? 231 PHE A O   1 
ATOM   1781 C  CB  . PHE A 1 231 ? 10.15100  4.92700   38.21600 1.000 49.46000 ? 231 PHE A CB  1 
ATOM   1782 C  CG  . PHE A 1 231 ? 10.02100  5.81500   36.98700 1.000 54.24000 ? 231 PHE A CG  1 
ATOM   1783 C  CD1 . PHE A 1 231 ? 11.04200  5.87800   36.04300 1.000 54.15000 ? 231 PHE A CD1 1 
ATOM   1784 C  CD2 . PHE A 1 231 ? 8.87600   6.57200   36.76900 1.000 51.64000 ? 231 PHE A CD2 1 
ATOM   1785 C  CE1 . PHE A 1 231 ? 10.92700  6.68500   34.91600 1.000 47.67000 ? 231 PHE A CE1 1 
ATOM   1786 C  CE2 . PHE A 1 231 ? 8.76000   7.38100   35.64500 1.000 49.88000 ? 231 PHE A CE2 1 
ATOM   1787 C  CZ  . PHE A 1 231 ? 9.78500   7.43400   34.71900 1.000 47.68000 ? 231 PHE A CZ  1 
ATOM   1788 N  N   . ASP A 1 232 ? 10.85600  8.02900   39.69200 1.000 41.77000 ? 232 ASP A N   1 
ATOM   1789 C  CA  . ASP A 1 232 ? 10.28800  9.35500   39.90800 1.000 36.21000 ? 232 ASP A CA  1 
ATOM   1790 C  C   . ASP A 1 232 ? 10.27400  10.14700  38.60200 1.000 37.89000 ? 232 ASP A C   1 
ATOM   1791 O  O   . ASP A 1 232 ? 11.29400  10.70600  38.19700 1.000 30.26000 ? 232 ASP A O   1 
ATOM   1792 C  CB  . ASP A 1 232 ? 11.07800  10.11100  40.97700 1.000 36.66000 ? 232 ASP A CB  1 
ATOM   1793 C  CG  . ASP A 1 232 ? 10.33700  11.32600  41.49900 1.000 36.91000 ? 232 ASP A CG  1 
ATOM   1794 O  OD1 . ASP A 1 232 ? 9.72400   11.23000  42.58300 1.000 56.14000 ? 232 ASP A OD1 1 
ATOM   1795 O  OD2 . ASP A 1 232 ? 10.36700  12.37800  40.82500 1.000 41.17000 ? 232 ASP A OD2 1 
ATOM   1796 N  N   . ILE A 1 233 ? 9.11700   10.19300  37.94800 1.000 35.22000 ? 233 ILE A N   1 
ATOM   1797 C  CA  . ILE A 1 233 ? 8.98000   10.90900  36.68500 1.000 29.14000 ? 233 ILE A CA  1 
ATOM   1798 C  C   . ILE A 1 233 ? 9.50700   12.33600  36.81900 1.000 26.64000 ? 233 ILE A C   1 
ATOM   1799 O  O   . ILE A 1 233 ? 10.26400  12.82000  35.96700 1.000 25.14000 ? 233 ILE A O   1 
ATOM   1800 C  CB  . ILE A 1 233 ? 7.50700   10.87900  36.22900 1.000 32.30000 ? 233 ILE A CB  1 
ATOM   1801 C  CG1 . ILE A 1 233 ? 7.32200   11.64800  34.92500 1.000 31.99000 ? 233 ILE A CG1 1 
ATOM   1802 C  CG2 . ILE A 1 233 ? 6.59100   11.41000  37.31300 1.000 32.74000 ? 233 ILE A CG2 1 
ATOM   1803 C  CD1 . ILE A 1 233 ? 8.08700   11.04000  33.78600 1.000 42.52000 ? 233 ILE A CD1 1 
ATOM   1804 N  N   . ASP A 1 234 ? 9.13000   13.02600  37.90100 1.000 21.42000 ? 234 ASP A N   1 
ATOM   1805 C  CA  . ASP A 1 234 ? 9.48900   14.43400  38.03900 1.000 25.53000 ? 234 ASP A CA  1 
ATOM   1806 C  C   . ASP A 1 234 ? 10.99800  14.60200  38.16000 1.000 27.25000 ? 234 ASP A C   1 
ATOM   1807 O  O   . ASP A 1 234 ? 11.57800  15.53800  37.59300 1.000 23.53000 ? 234 ASP A O   1 
ATOM   1808 C  CB  . ASP A 1 234 ? 8.79300   15.04200  39.25800 1.000 31.33000 ? 234 ASP A CB  1 
ATOM   1809 C  CG  . ASP A 1 234 ? 7.31900   15.34800  39.01400 1.000 35.73000 ? 234 ASP A CG  1 
ATOM   1810 O  OD1 . ASP A 1 234 ? 6.88500   15.40100  37.84100 1.000 30.16000 ? 234 ASP A OD1 1 
ATOM   1811 O  OD2 . ASP A 1 234 ? 6.59600   15.53600  40.01200 1.000 39.37000 ? 234 ASP A OD2 1 
ATOM   1812 N  N   . ASN A 1 235 ? 11.64700  13.70200  38.89900 1.000 21.53000 ? 235 ASN A N   1 
ATOM   1813 C  CA  . ASN A 1 235 ? 13.09900  13.75700  39.02900 1.000 23.52000 ? 235 ASN A CA  1 
ATOM   1814 C  C   . ASN A 1 235 ? 13.77300  13.53200  37.67900 1.000 25.67000 ? 235 ASN A C   1 
ATOM   1815 O  O   . ASN A 1 235 ? 14.67200  14.28300  37.29100 1.000 21.91000 ? 235 ASN A O   1 
ATOM   1816 C  CB  . ASN A 1 235 ? 13.55900  12.72800  40.06300 1.000 26.70000 ? 235 ASN A CB  1 
ATOM   1817 C  CG  . ASN A 1 235 ? 15.01100  12.90500  40.46500 1.000 25.39000 ? 235 ASN A CG  1 
ATOM   1818 O  OD1 . ASN A 1 235 ? 15.91700  12.68900  39.66100 1.000 20.39000 ? 235 ASN A OD1 1 
ATOM   1819 N  ND2 . ASN A 1 235 ? 15.24100  13.28800  41.71500 1.000 18.94000 ? 235 ASN A ND2 1 
ATOM   1820 N  N   . MET A 1 236 ? 13.32400  12.52100  36.93100 1.000 24.39000 ? 236 MET A N   1 
ATOM   1821 C  CA  . MET A 1 236 ? 13.89900  12.26600  35.61300 1.000 27.20000 ? 236 MET A CA  1 
ATOM   1822 C  C   . MET A 1 236 ? 13.72100  13.46700  34.68800 1.000 24.33000 ? 236 MET A C   1 
ATOM   1823 O  O   . MET A 1 236 ? 14.68200  13.92400  34.05900 1.000 29.06000 ? 236 MET A O   1 
ATOM   1824 C  CB  . MET A 1 236 ? 13.27300  11.01700  34.99400 1.000 27.65000 ? 236 MET A CB  1 
ATOM   1825 C  CG  . MET A 1 236 ? 13.84300  9.70800   35.53800 1.000 49.54000 ? 236 MET A CG  1 
ATOM   1826 S  SD  . MET A 1 236 ? 15.51400  9.38400   34.91800 1.000 50.05000 ? 236 MET A SD  1 
ATOM   1827 C  CE  . MET A 1 236 ? 15.59100  7.59400   34.95300 1.000 38.18000 ? 236 MET A CE  1 
ATOM   1828 N  N   . LEU A 1 237 ? 12.49200  13.98900  34.58900 1.000 26.79000 ? 237 LEU A N   1 
ATOM   1829 C  CA  . LEU A 1 237 ? 12.24000  15.16200  33.75000 1.000 26.10000 ? 237 LEU A CA  1 
ATOM   1830 C  C   . LEU A 1 237 ? 13.12700  16.33800  34.13500 1.000 27.14000 ? 237 LEU A C   1 
ATOM   1831 O  O   . LEU A 1 237 ? 13.50400  17.13900  33.27000 1.000 28.07000 ? 237 LEU A O   1 
ATOM   1832 C  CB  . LEU A 1 237 ? 10.77100  15.58300  33.84400 1.000 27.59000 ? 237 LEU A CB  1 
ATOM   1833 C  CG  . LEU A 1 237 ? 9.72100   14.57600  33.38500 1.000 29.06000 ? 237 LEU A CG  1 
ATOM   1834 C  CD1 . LEU A 1 237 ? 8.33800   15.20300  33.45400 1.000 33.43000 ? 237 LEU A CD1 1 
ATOM   1835 C  CD2 . LEU A 1 237 ? 10.05300  14.08100  31.98400 1.000 35.75000 ? 237 LEU A CD2 1 
ATOM   1836 N  N   . MET A 1 238 ? 13.46000  16.47000  35.42400 1.000 24.69000 ? 238 MET A N   1 
ATOM   1837 C  CA  . MET A 1 238 ? 14.35100  17.54500  35.84300 1.000 20.09000 ? 238 MET A CA  1 
ATOM   1838 C  C   . MET A 1 238 ? 15.79500  17.27400  35.42600 1.000 25.14000 ? 238 MET A C   1 
ATOM   1839 O  O   . MET A 1 238 ? 16.49900  18.19400  35.00200 1.000 30.30000 ? 238 MET A O   1 
ATOM   1840 C  CB  . MET A 1 238 ? 14.25600  17.76600  37.35400 1.000 17.30000 ? 238 MET A CB  1 
ATOM   1841 C  CG  . MET A 1 238 ? 12.93700  18.41600  37.81400 1.000 23.57000 ? 238 MET A CG  1 
ATOM   1842 S  SD  . MET A 1 238 ? 12.69800  20.06600  37.10700 1.000 24.95000 ? 238 MET A SD  1 
ATOM   1843 C  CE  . MET A 1 238 ? 14.37100  20.68300  37.30300 1.000 25.71000 ? 238 MET A CE  1 
ATOM   1844 N  N   . LEU A 1 239 ? 16.26600  16.02800  35.53900 1.000 23.56000 ? 239 LEU A N   1 
ATOM   1845 C  CA  . LEU A 1 239 ? 17.68400  15.79200  35.27000 1.000 23.39000 ? 239 LEU A CA  1 
ATOM   1846 C  C   . LEU A 1 239 ? 17.97200  15.62900  33.78600 1.000 25.91000 ? 239 LEU A C   1 
ATOM   1847 O  O   . LEU A 1 239 ? 19.00100  16.11200  33.30100 1.000 28.96000 ? 239 LEU A O   1 
ATOM   1848 C  CB  . LEU A 1 239 ? 18.17900  14.54800  35.99600 1.000 26.53000 ? 239 LEU A CB  1 
ATOM   1849 C  CG  . LEU A 1 239 ? 18.24300  14.57500  37.51400 1.000 23.92000 ? 239 LEU A CG  1 
ATOM   1850 C  CD1 . LEU A 1 239 ? 18.87900  13.26000  37.91900 1.000 25.86000 ? 239 LEU A CD1 1 
ATOM   1851 C  CD2 . LEU A 1 239 ? 19.06000  15.77600  37.98800 1.000 20.18000 ? 239 LEU A CD2 1 
ATOM   1852 N  N   . THR A 1 240 ? 17.09100  14.93200  33.06100 1.000 22.45000 ? 240 THR A N   1 
ATOM   1853 C  CA  . THR A 1 240 ? 17.40100  14.50100  31.69700 1.000 25.32000 ? 240 THR A CA  1 
ATOM   1854 C  C   . THR A 1 240 ? 17.99800  15.59600  30.81500 1.000 24.35000 ? 240 THR A C   1 
ATOM   1855 O  O   . THR A 1 240 ? 19.00100  15.32200  30.13300 1.000 28.22000 ? 240 THR A O   1 
ATOM   1856 C  CB  . THR A 1 240 ? 16.14700  13.89100  31.04800 1.000 26.17000 ? 240 THR A CB  1 
ATOM   1857 O  OG1 . THR A 1 240 ? 15.78500  12.68800  31.73800 1.000 29.47000 ? 240 THR A OG1 1 
ATOM   1858 C  CG2 . THR A 1 240 ? 16.41400  13.54600  29.55900 1.000 23.73000 ? 240 THR A CG2 1 
ATOM   1859 N  N   . PRO A 1 241 ? 17.47900  16.82700  30.77700 1.000 23.76000 ? 241 PRO A N   1 
ATOM   1860 C  CA  . PRO A 1 241 ? 18.06300  17.83500  29.88400 1.000 23.51000 ? 241 PRO A CA  1 
ATOM   1861 C  C   . PRO A 1 241 ? 19.15000  18.70400  30.49700 1.000 21.03000 ? 241 PRO A C   1 
ATOM   1862 O  O   . PRO A 1 241 ? 19.60400  19.63900  29.83000 1.000 23.18000 ? 241 PRO A O   1 
ATOM   1863 C  CB  . PRO A 1 241 ? 16.84600  18.68900  29.52200 1.000 24.67000 ? 241 PRO A CB  1 
ATOM   1864 C  CG  . PRO A 1 241 ? 16.03400  18.68200  30.77800 1.000 24.90000 ? 241 PRO A CG  1 
ATOM   1865 C  CD  . PRO A 1 241 ? 16.21900  17.31500  31.37600 1.000 22.89000 ? 241 PRO A CD  1 
ATOM   1866 N  N   . LEU A 1 242 ? 19.58200  18.44000  31.72500 1.000 22.43000 ? 242 LEU A N   1 
ATOM   1867 C  CA  . LEU A 1 242 ? 20.54900  19.29500  32.40400 1.000 21.29000 ? 242 LEU A CA  1 
ATOM   1868 C  C   . LEU A 1 242 ? 21.93400  18.66200  32.50900 1.000 26.54000 ? 242 LEU A C   1 
ATOM   1869 O  O   . LEU A 1 242 ? 22.80300  19.21000  33.19900 1.000 23.82000 ? 242 LEU A O   1 
ATOM   1870 C  CB  . LEU A 1 242 ? 20.02100  19.65400  33.79300 1.000 23.02000 ? 242 LEU A CB  1 
ATOM   1871 C  CG  . LEU A 1 242 ? 18.69700  20.43000  33.82600 1.000 21.00000 ? 242 LEU A CG  1 
ATOM   1872 C  CD1 . LEU A 1 242 ? 18.28300  20.67100  35.26300 1.000 24.58000 ? 242 LEU A CD1 1 
ATOM   1873 C  CD2 . LEU A 1 242 ? 18.80500  21.76000  33.05800 1.000 27.01000 ? 242 LEU A CD2 1 
ATOM   1874 N  N   . ILE A 1 243 ? 22.16500  17.52800  31.84700 1.000 18.95000 ? 243 ILE A N   1 
ATOM   1875 C  CA  . ILE A 1 243 ? 23.41100  16.79100  32.03400 1.000 21.41000 ? 243 ILE A CA  1 
ATOM   1876 C  C   . ILE A 1 243 ? 24.09800  16.52500  30.69800 1.000 20.32000 ? 243 ILE A C   1 
ATOM   1877 O  O   . ILE A 1 243 ? 24.79800  15.52100  30.53600 1.000 20.44000 ? 243 ILE A O   1 
ATOM   1878 C  CB  . ILE A 1 243 ? 23.16300  15.48000  32.80200 1.000 22.37000 ? 243 ILE A CB  1 
ATOM   1879 C  CG1 . ILE A 1 243 ? 22.12000  14.62200  32.09200 1.000 22.25000 ? 243 ILE A CG1 1 
ATOM   1880 C  CG2 . ILE A 1 243 ? 22.72300  15.77500  34.25800 1.000 22.19000 ? 243 ILE A CG2 1 
ATOM   1881 C  CD1 . ILE A 1 243 ? 22.06900  13.20400  32.62800 1.000 21.70000 ? 243 ILE A CD1 1 
ATOM   1882 N  N   . SER A 1 244 ? 23.92200  17.43300  29.73700 1.000 18.09000 ? 244 SER A N   1 
ATOM   1883 C  CA  . SER A 1 244 ? 24.70300  17.37900  28.50400 1.000 16.68000 ? 244 SER A CA  1 
ATOM   1884 C  C   . SER A 1 244 ? 26.19100  17.54700  28.75600 1.000 15.44000 ? 244 SER A C   1 
ATOM   1885 O  O   . SER A 1 244 ? 26.99000  17.31800  27.84000 1.000 14.75000 ? 244 SER A O   1 
ATOM   1886 C  CB  . SER A 1 244 ? 24.23300  18.46800  27.54200 1.000 16.27000 ? 244 SER A CB  1 
ATOM   1887 O  OG  . SER A 1 244 ? 22.89300  18.24900  27.14300 1.000 19.99000 ? 244 SER A OG  1 
ATOM   1888 N  N   . THR A 1 245 ? 26.56300  17.98800  29.95700 1.000 17.25000 ? 245 THR A N   1 
ATOM   1889 C  CA  . THR A 1 245 ? 27.96200  18.06400  30.35900 1.000 15.49000 ? 245 THR A CA  1 
ATOM   1890 C  C   . THR A 1 245 ? 28.69500  16.74700  30.12600 1.000 15.38000 ? 245 THR A C   1 
ATOM   1891 O  O   . THR A 1 245 ? 29.88900  16.75100  29.80700 1.000 15.75000 ? 245 THR A O   1 
ATOM   1892 C  CB  . THR A 1 245 ? 28.04200  18.45300  31.84000 1.000 19.64000 ? 245 THR A CB  1 
ATOM   1893 O  OG1 . THR A 1 245 ? 27.25000  19.62800  32.06500 1.000 16.75000 ? 245 THR A OG1 1 
ATOM   1894 C  CG2 . THR A 1 245 ? 29.47900  18.74200  32.24900 1.000 17.40000 ? 245 THR A CG2 1 
ATOM   1895 N  N   . ILE A 1 246 ? 28.01900  15.61200  30.32900 1.000 12.04000 ? 246 ILE A N   1 
ATOM   1896 C  CA  . ILE A 1 246 ? 28.70600  14.32800  30.21900 1.000 16.35000 ? 246 ILE A CA  1 
ATOM   1897 C  C   . ILE A 1 246 ? 29.17300  14.09800  28.78700 1.000 15.64000 ? 246 ILE A C   1 
ATOM   1898 O  O   . ILE A 1 246 ? 30.36600  13.89500  28.52600 1.000 14.94000 ? 246 ILE A O   1 
ATOM   1899 C  CB  . ILE A 1 246 ? 27.80900  13.17100  30.68900 1.000 18.33000 ? 246 ILE A CB  1 
ATOM   1900 C  CG1 . ILE A 1 246 ? 27.33200  13.36500  32.13100 1.000 14.93000 ? 246 ILE A CG1 1 
ATOM   1901 C  CG2 . ILE A 1 246 ? 28.57500  11.85800  30.55600 1.000 15.32000 ? 246 ILE A CG2 1 
ATOM   1902 C  CD1 . ILE A 1 246 ? 26.20400  12.39300  32.51700 1.000 13.22000 ? 246 ILE A CD1 1 
ATOM   1903 N  N   . ALA A 1 247 ? 28.23300  14.11300  27.83800 1.000 14.55000 ? 247 ALA A N   1 
ATOM   1904 C  CA  . ALA A 1 247 ? 28.58400  13.85900  26.44100 1.000 13.23000 ? 247 ALA A CA  1 
ATOM   1905 C  C   . ALA A 1 247 ? 29.53100  14.92300  25.88600 1.000 13.91000 ? 247 ALA A C   1 
ATOM   1906 O  O   . ALA A 1 247 ? 30.44300  14.60900  25.11500 1.000 12.48000 ? 247 ALA A O   1 
ATOM   1907 C  CB  . ALA A 1 247 ? 27.31900  13.78100  25.58700 1.000 13.08000 ? 247 ALA A CB  1 
ATOM   1908 N  N   . ALA A 1 248 ? 29.30900  16.19400  26.22600 1.000 12.80000 ? 248 ALA A N   1 
ATOM   1909 C  CA  . ALA A 1 248 ? 30.21200  17.23600  25.73700 1.000 12.62000 ? 248 ALA A CA  1 
ATOM   1910 C  C   . ALA A 1 248 ? 31.63200  17.03100  26.25900 1.000 17.19000 ? 248 ALA A C   1 
ATOM   1911 O  O   . ALA A 1 248 ? 32.60700  17.19300  25.51000 1.000 15.88000 ? 248 ALA A O   1 
ATOM   1912 C  CB  . ALA A 1 248 ? 29.68800  18.61500  26.13400 1.000 13.62000 ? 248 ALA A CB  1 
ATOM   1913 N  N   . THR A 1 249 ? 31.76600  16.67800  27.54000 1.000 15.33000 ? 249 THR A N   1 
ATOM   1914 C  CA  . THR A 1 249 ? 33.07400  16.32000  28.08900 1.000 14.29000 ? 249 THR A CA  1 
ATOM   1915 C  C   . THR A 1 249 ? 33.68500  15.13400  27.34600 1.000 15.64000 ? 249 THR A C   1 
ATOM   1916 O  O   . THR A 1 249 ? 34.86200  15.17300  26.95800 1.000 15.13000 ? 249 THR A O   1 
ATOM   1917 C  CB  . THR A 1 249 ? 32.93900  16.01300  29.58500 1.000 12.03000 ? 249 THR A CB  1 
ATOM   1918 O  OG1 . THR A 1 249 ? 32.50600  17.19400  30.26600 1.000 15.39000 ? 249 THR A OG1 1 
ATOM   1919 C  CG2 . THR A 1 249 ? 34.27500  15.58000  30.17400 1.000 15.57000 ? 249 THR A CG2 1 
ATOM   1920 N  N   . ASP A 1 250 ? 32.90500  14.06100  27.14200 1.000 14.09000 ? 250 ASP A N   1 
ATOM   1921 C  CA  . ASP A 1 250 ? 33.42400  12.92100  26.37800 1.000 15.45000 ? 250 ASP A CA  1 
ATOM   1922 C  C   . ASP A 1 250 ? 33.95600  13.35500  25.01200 1.000 15.00000 ? 250 ASP A C   1 
ATOM   1923 O  O   . ASP A 1 250 ? 35.04800  12.95000  24.60200 1.000 14.65000 ? 250 ASP A O   1 
ATOM   1924 C  CB  . ASP A 1 250 ? 32.35000  11.85000  26.17000 1.000 13.84000 ? 250 ASP A CB  1 
ATOM   1925 C  CG  . ASP A 1 250 ? 31.84300  11.24000  27.47200 1.000 15.74000 ? 250 ASP A CG  1 
ATOM   1926 O  OD1 . ASP A 1 250 ? 32.56600  11.28900  28.49500 1.000 14.09000 ? 250 ASP A OD1 1 
ATOM   1927 O  OD2 . ASP A 1 250 ? 30.71300  10.69800  27.45600 1.000 13.83000 ? 250 ASP A OD2 1 
ATOM   1928 N  N   . MET A 1 251 ? 33.17000  14.14000  24.26800 1.000 14.71000 ? 251 MET A N   1 
ATOM   1929 C  CA  . MET A 1 251 ? 33.58700  14.54100  22.91900 1.000 13.74000 ? 251 MET A CA  1 
ATOM   1930 C  C   . MET A 1 251 ? 34.83800  15.41300  22.96200 1.000 15.48000 ? 251 MET A C   1 
ATOM   1931 O  O   . MET A 1 251 ? 35.77300  15.22300  22.17200 1.000 14.91000 ? 251 MET A O   1 
ATOM   1932 C  CB  . MET A 1 251 ? 32.44800  15.27700  22.21300 1.000 11.54000 ? 251 MET A CB  1 
ATOM   1933 C  CG  . MET A 1 251 ? 32.73600  15.61000  20.75000 1.000 18.15000 ? 251 MET A CG  1 
ATOM   1934 S  SD  . MET A 1 251 ? 33.02200  14.12700  19.73200 1.000 22.53000 ? 251 MET A SD  1 
ATOM   1935 C  CE  . MET A 1 251 ? 31.35800  13.52500  19.46200 1.000 17.11000 ? 251 MET A CE  1 
ATOM   1936 N  N   . MET A 1 252 ? 34.85900  16.39200  23.87000 1.000 13.56000 ? 252 MET A N   1 
ATOM   1937 C  CA  . MET A 1 252 ? 36.01200  17.27700  24.02500 1.000 16.08000 ? 252 MET A CA  1 
ATOM   1938 C  C   . MET A 1 252 ? 37.28300  16.49400  24.35900 1.000 17.98000 ? 252 MET A C   1 
ATOM   1939 O  O   . MET A 1 252 ? 38.33300  16.69300  23.73300 1.000 18.08000 ? 252 MET A O   1 
ATOM   1940 C  CB  . MET A 1 252 ? 35.69500  18.30700  25.11800 1.000 19.81000 ? 252 MET A CB  1 
ATOM   1941 C  CG  . MET A 1 252 ? 36.58400  19.53800  25.18500 1.000 30.91000 ? 252 MET A CG  1 
ATOM   1942 S  SD  . MET A 1 252 ? 36.46100  20.58700  23.72400 1.000 25.05000 ? 252 MET A SD  1 
ATOM   1943 C  CE  . MET A 1 252 ? 35.55300  22.01800  24.29500 1.000 16.78000 ? 252 MET A CE  1 
ATOM   1944 N  N   . LEU A 1 253 ? 37.20700  15.59600  25.34000 1.000 15.92000 ? 253 LEU A N   1 
ATOM   1945 C  CA  . LEU A 1 253 ? 38.38700  14.88700  25.82300 1.000 17.15000 ? 253 LEU A CA  1 
ATOM   1946 C  C   . LEU A 1 253 ? 38.78000  13.70500  24.94700 1.000 17.81000 ? 253 LEU A C   1 
ATOM   1947 O  O   . LEU A 1 253 ? 39.82600  13.09600  25.19200 1.000 18.31000 ? 253 LEU A O   1 
ATOM   1948 C  CB  . LEU A 1 253 ? 38.16900  14.36200  27.24100 1.000 17.32000 ? 253 LEU A CB  1 
ATOM   1949 C  CG  . LEU A 1 253 ? 37.95400  15.35700  28.39800 1.000 24.23000 ? 253 LEU A CG  1 
ATOM   1950 C  CD1 . LEU A 1 253 ? 38.47300  14.81400  29.72000 1.000 24.45000 ? 253 LEU A CD1 1 
ATOM   1951 C  CD2 . LEU A 1 253 ? 38.41600  16.78400  28.13400 1.000 21.22000 ? 253 LEU A CD2 1 
ATOM   1952 N  N   . SER A 1 254 ? 37.96200  13.35200  23.95800 1.000 15.87000 ? 254 SER A N   1 
ATOM   1953 C  CA  . SER A 1 254 ? 38.26300  12.21600  23.09500 1.000 16.43000 ? 254 SER A CA  1 
ATOM   1954 C  C   . SER A 1 254 ? 39.43400  12.49300  22.17500 1.000 18.96000 ? 254 SER A C   1 
ATOM   1955 O  O   . SER A 1 254 ? 40.00600  11.54600  21.61400 1.000 19.21000 ? 254 SER A O   1 
ATOM   1956 C  CB  . SER A 1 254 ? 37.04400  11.86800  22.23800 1.000 18.09000 ? 254 SER A CB  1 
ATOM   1957 O  OG  . SER A 1 254 ? 36.82300  12.89500  21.28000 1.000 15.55000 ? 254 SER A OG  1 
ATOM   1958 N  N   . GLY A 1 255 ? 39.78600  13.76800  21.99400 1.000 14.46000 ? 255 GLY A N   1 
ATOM   1959 C  CA  . GLY A 1 255 ? 40.74900  14.16600  20.99400 1.000 17.46000 ? 255 GLY A CA  1 
ATOM   1960 C  C   . GLY A 1 255 ? 40.16500  14.28200  19.60600 1.000 16.80000 ? 255 GLY A C   1 
ATOM   1961 O  O   . GLY A 1 255 ? 40.92000  14.47600  18.65100 1.000 15.21000 ? 255 GLY A O   1 
ATOM   1962 N  N   . ALA A 1 256 ? 38.83900  14.14600  19.46800 1.000 17.70000 ? 256 ALA A N   1 
ATOM   1963 C  CA  . ALA A 1 256 ? 38.20000  14.21300  18.15000 1.000 18.16000 ? 256 ALA A CA  1 
ATOM   1964 C  C   . ALA A 1 256 ? 38.52300  15.51200  17.42800 1.000 14.84000 ? 256 ALA A C   1 
ATOM   1965 O  O   . ALA A 1 256 ? 38.70500  15.51800  16.20400 1.000 19.87000 ? 256 ALA A O   1 
ATOM   1966 C  CB  . ALA A 1 256 ? 36.68700  14.07000  18.28100 1.000 18.25000 ? 256 ALA A CB  1 
ATOM   1967 N  N   . PHE A 1 257 ? 38.57200  16.62900  18.14900 1.000 14.16000 ? 257 PHE A N   1 
ATOM   1968 C  CA  . PHE A 1 257 ? 38.81700  17.89200  17.46500 1.000 15.58000 ? 257 PHE A CA  1 
ATOM   1969 C  C   . PHE A 1 257 ? 40.28500  18.09500  17.11900 1.000 19.28000 ? 257 PHE A C   1 
ATOM   1970 O  O   . PHE A 1 257 ? 40.57900  18.82200  16.17100 1.000 17.51000 ? 257 PHE A O   1 
ATOM   1971 C  CB  . PHE A 1 257 ? 38.28000  19.06100  18.29500 1.000 17.55000 ? 257 PHE A CB  1 
ATOM   1972 C  CG  . PHE A 1 257 ? 36.82100  18.93200  18.59700 1.000 13.45000 ? 257 PHE A CG  1 
ATOM   1973 C  CD1 . PHE A 1 257 ? 35.88500  19.08600  17.59000 1.000 13.39000 ? 257 PHE A CD1 1 
ATOM   1974 C  CD2 . PHE A 1 257 ? 36.38900  18.57900  19.86700 1.000 17.16000 ? 257 PHE A CD2 1 
ATOM   1975 C  CE1 . PHE A 1 257 ? 34.52700  18.92600  17.84000 1.000 14.26000 ? 257 PHE A CE1 1 
ATOM   1976 C  CE2 . PHE A 1 257 ? 35.02900  18.42700  20.13500 1.000 16.01000 ? 257 PHE A CE2 1 
ATOM   1977 C  CZ  . PHE A 1 257 ? 34.09700  18.60200  19.11500 1.000 13.25000 ? 257 PHE A CZ  1 
ATOM   1978 N  N   . LYS A 1 258 ? 41.21500  17.46800  17.84500 1.000 18.28000 ? 258 LYS A N   1 
ATOM   1979 C  CA  . LYS A 1 258 ? 42.60000  17.50100  17.38500 1.000 19.36000 ? 258 LYS A CA  1 
ATOM   1980 C  C   . LYS A 1 258 ? 42.76200  16.70600  16.09100 1.000 17.53000 ? 258 LYS A C   1 
ATOM   1981 O  O   . LYS A 1 258 ? 43.46200  17.14600  15.16800 1.000 16.60000 ? 258 LYS A O   1 
ATOM   1982 C  CB  . LYS A 1 258 ? 43.54800  16.97700  18.46700 1.000 16.19000 ? 258 LYS A CB  1 
ATOM   1983 C  CG  . LYS A 1 258 ? 45.02100  17.24300  18.12900 1.000 20.78000 ? 258 LYS A CG  1 
ATOM   1984 C  CD  . LYS A 1 258 ? 45.95100  17.19100  19.34600 1.000 25.43000 ? 258 LYS A CD  1 
ATOM   1985 C  CE  . LYS A 1 258 ? 46.08900  15.77000  19.85900 1.000 23.68000 ? 258 LYS A CE  1 
ATOM   1986 N  NZ  . LYS A 1 258 ? 47.14100  15.64100  20.92400 1.000 26.54000 ? 258 LYS A NZ  1 
ATOM   1987 N  N   . LYS A 1 259 ? 42.09800  15.55000  15.99100 1.000 16.34000 ? 259 LYS A N   1 
ATOM   1988 C  CA  . LYS A 1 259 ? 42.17300  14.75400  14.77000 1.000 17.66000 ? 259 LYS A CA  1 
ATOM   1989 C  C   . LYS A 1 259 ? 41.33500  15.35300  13.64600 1.000 18.49000 ? 259 LYS A C   1 
ATOM   1990 O  O   . LYS A 1 259 ? 41.72700  15.26400  12.48100 1.000 17.15000 ? 259 LYS A O   1 
ATOM   1991 C  CB  . LYS A 1 259 ? 41.71300  13.31000  15.01700 1.000 19.81000 ? 259 LYS A CB  1 
ATOM   1992 C  CG  . LYS A 1 259 ? 42.39600  12.54600  16.16400 1.000 28.88000 ? 259 LYS A CG  1 
ATOM   1993 C  CD  . LYS A 1 259 ? 41.90100  11.07500  16.25300 1.000 32.30000 ? 259 LYS A CD  1 
ATOM   1994 C  CE  . LYS A 1 259 ? 41.45200  10.69300  17.68300 1.000 29.39000 ? 259 LYS A CE  1 
ATOM   1995 N  NZ  . LYS A 1 259 ? 40.80000  9.32700   17.81800 1.000 26.13000 ? 259 LYS A NZ  1 
ATOM   1996 N  N   . PHE A 1 260 ? 40.18200  15.95600  13.97100 1.000 17.00000 ? 260 PHE A N   1 
ATOM   1997 C  CA  . PHE A 1 260 ? 39.23500  16.47900  12.98700 1.000 17.33000 ? 260 PHE A CA  1 
ATOM   1998 C  C   . PHE A 1 260 ? 38.86800  17.91100  13.36400 1.000 17.75000 ? 260 PHE A C   1 
ATOM   1999 O  O   . PHE A 1 260 ? 37.77100  18.17300  13.87400 1.000 15.38000 ? 260 PHE A O   1 
ATOM   2000 C  CB  . PHE A 1 260 ? 37.98800  15.59400  12.91200 1.000 15.72000 ? 260 PHE A CB  1 
ATOM   2001 C  CG  . PHE A 1 260 ? 38.29100  14.16000  12.62000 1.000 16.04000 ? 260 PHE A CG  1 
ATOM   2002 C  CD1 . PHE A 1 260 ? 38.63700  13.75500  11.33000 1.000 16.51000 ? 260 PHE A CD1 1 
ATOM   2003 C  CD2 . PHE A 1 260 ? 38.26400  13.21600  13.63700 1.000 19.18000 ? 260 PHE A CD2 1 
ATOM   2004 C  CE1 . PHE A 1 260 ? 38.92400  12.43100  11.04900 1.000 17.27000 ? 260 PHE A CE1 1 
ATOM   2005 C  CE2 . PHE A 1 260 ? 38.55600  11.88000  13.36800 1.000 18.49000 ? 260 PHE A CE2 1 
ATOM   2006 C  CZ  . PHE A 1 260 ? 38.90000  11.49100  12.07500 1.000 18.02000 ? 260 PHE A CZ  1 
ATOM   2007 N  N   . PRO A 1 261 ? 39.75200  18.86800  13.09300 1.000 14.39000 ? 261 PRO A N   1 
ATOM   2008 C  CA  . PRO A 1 261 ? 39.53900  20.23700  13.59600 1.000 15.57000 ? 261 PRO A CA  1 
ATOM   2009 C  C   . PRO A 1 261 ? 38.30400  20.93100  13.05100 1.000 14.78000 ? 261 PRO A C   1 
ATOM   2010 O  O   . PRO A 1 261 ? 37.90000  21.95300  13.61400 1.000 15.45000 ? 261 PRO A O   1 
ATOM   2011 C  CB  . PRO A 1 261 ? 40.81700  20.97500  13.15900 1.000 17.35000 ? 261 PRO A CB  1 
ATOM   2012 C  CG  . PRO A 1 261 ? 41.79400  19.91000  12.81300 1.000 23.42000 ? 261 PRO A CG  1 
ATOM   2013 C  CD  . PRO A 1 261 ? 41.02300  18.72600  12.36300 1.000 14.57000 ? 261 PRO A CD  1 
ATOM   2014 N  N   . ASP A 1 262 ? 37.70200  20.44500  11.96800 1.000 15.99000 ? 262 ASP A N   1 
ATOM   2015 C  CA  . ASP A 1 262 ? 36.50200  21.07500  11.43000 1.000 17.66000 ? 262 ASP A CA  1 
ATOM   2016 C  C   . ASP A 1 262 ? 35.21800  20.34900  11.83500 1.000 13.66000 ? 262 ASP A C   1 
ATOM   2017 O  O   . ASP A 1 262 ? 34.13600  20.71200  11.36300 1.000 12.07000 ? 262 ASP A O   1 
ATOM   2018 C  CB  . ASP A 1 262 ? 36.59700  21.16800  9.90000  1.000 16.43000 ? 262 ASP A CB  1 
ATOM   2019 C  CG  . ASP A 1 262 ? 37.67400  22.14600  9.44300  1.000 24.50000 ? 262 ASP A CG  1 
ATOM   2020 O  OD1 . ASP A 1 262 ? 38.00300  23.07200  10.21000 1.000 22.83000 ? 262 ASP A OD1 1 
ATOM   2021 O  OD2 . ASP A 1 262 ? 38.17900  21.99800  8.31300  1.000 29.28000 ? 262 ASP A OD2 1 
ATOM   2022 N  N   . LEU A 1 263 ? 35.31400  19.33700  12.69200 1.000 13.23000 ? 263 LEU A N   1 
ATOM   2023 C  CA  . LEU A 1 263 ? 34.13800  18.56500  13.09000 1.000 14.85000 ? 263 LEU A CA  1 
ATOM   2024 C  C   . LEU A 1 263 ? 33.14000  19.45500  13.83100 1.000 15.46000 ? 263 LEU A C   1 
ATOM   2025 O  O   . LEU A 1 263 ? 33.52700  20.26900  14.67300 1.000 13.47000 ? 263 LEU A O   1 
ATOM   2026 C  CB  . LEU A 1 263 ? 34.57500  17.39900  13.97900 1.000 14.40000 ? 263 LEU A CB  1 
ATOM   2027 C  CG  . LEU A 1 263 ? 33.47800  16.46000  14.46200 1.000 12.92000 ? 263 LEU A CG  1 
ATOM   2028 C  CD1 . LEU A 1 263 ? 32.92700  15.67400  13.27000 1.000 11.38000 ? 263 LEU A CD1 1 
ATOM   2029 C  CD2 . LEU A 1 263 ? 34.00400  15.53600  15.55200 1.000 16.03000 ? 263 LEU A CD2 1 
ATOM   2030 N  N   . LYS A 1 264 ? 31.85000  19.31100  13.51100 1.000 13.26000 ? 264 LYS A N   1 
ATOM   2031 C  CA  . LYS A 1 264 ? 30.79800  20.14300  14.09600 1.000 15.02000 ? 264 LYS A CA  1 
ATOM   2032 C  C   . LYS A 1 264 ? 29.88500  19.29200  14.97500 1.000 14.67000 ? 264 LYS A C   1 
ATOM   2033 O  O   . LYS A 1 264 ? 29.43900  18.21400  14.56000 1.000 13.64000 ? 264 LYS A O   1 
ATOM   2034 C  CB  . LYS A 1 264 ? 29.95100  20.84600  13.01500 1.000 14.66000 ? 264 LYS A CB  1 
ATOM   2035 C  CG  . LYS A 1 264 ? 30.61500  22.04400  12.31200 1.000 11.60000 ? 264 LYS A CG  1 
ATOM   2036 C  CD  . LYS A 1 264 ? 29.69300  22.65000  11.23000 1.000 14.43000 ? 264 LYS A CD  1 
ATOM   2037 C  CE  . LYS A 1 264 ? 29.31800  21.63100  10.13700 1.000 20.84000 ? 264 LYS A CE  1 
ATOM   2038 N  NZ  . LYS A 1 264 ? 28.37400  22.16000  9.05000  1.000 19.54000 ? 264 LYS A NZ  1 
ATOM   2039 N  N   . VAL A 1 265 ? 29.57700  19.79400  16.17400 1.000 12.83000 ? 265 VAL A N   1 
ATOM   2040 C  CA  . VAL A 1 265 ? 28.75200  19.07500  17.15100 1.000 10.88000 ? 265 VAL A CA  1 
ATOM   2041 C  C   . VAL A 1 265 ? 27.66800  20.02200  17.65900 1.000 14.51000 ? 265 VAL A C   1 
ATOM   2042 O  O   . VAL A 1 265 ? 27.97800  21.08600  18.21300 1.000 14.60000 ? 265 VAL A O   1 
ATOM   2043 C  CB  . VAL A 1 265 ? 29.59000  18.53300  18.32600 1.000 14.16000 ? 265 VAL A CB  1 
ATOM   2044 C  CG1 . VAL A 1 265 ? 28.68700  17.97400  19.44700 1.000 12.27000 ? 265 VAL A CG1 1 
ATOM   2045 C  CG2 . VAL A 1 265 ? 30.58200  17.46900  17.82900 1.000 14.55000 ? 265 VAL A CG2 1 
ATOM   2046 N  N   . ALA A 1 266 ? 26.41200  19.63200  17.48400 1.000 14.52000 ? 266 ALA A N   1 
ATOM   2047 C  CA  . ALA A 1 266 ? 25.27400  20.33600  18.06700 1.000 12.45000 ? 266 ALA A CA  1 
ATOM   2048 C  C   . ALA A 1 266 ? 24.75200  19.54800  19.26200 1.000 16.57000 ? 266 ALA A C   1 
ATOM   2049 O  O   . ALA A 1 266 ? 24.41500  18.36800  19.11800 1.000 14.19000 ? 266 ALA A O   1 
ATOM   2050 C  CB  . ALA A 1 266 ? 24.15200  20.50100  17.03800 1.000 14.13000 ? 266 ALA A CB  1 
ATOM   2051 N  N   . MET A 1 267 ? 24.65000  20.20400  20.42900 1.000 12.23000 ? 267 MET A N   1 
ATOM   2052 C  CA  . MET A 1 267 ? 24.20200  19.52700  21.65100 1.000 14.05000 ? 267 MET A CA  1 
ATOM   2053 C  C   . MET A 1 267 ? 22.68700  19.68200  21.77300 1.000 14.05000 ? 267 MET A C   1 
ATOM   2054 O  O   . MET A 1 267 ? 22.16500  20.43400  22.59000 1.000 12.34000 ? 267 MET A O   1 
ATOM   2055 C  CB  . MET A 1 267 ? 24.92200  20.07700  22.87900 1.000 14.48000 ? 267 MET A CB  1 
ATOM   2056 C  CG  . MET A 1 267 ? 26.44900  19.86800  22.91100 1.000 13.93000 ? 267 MET A CG  1 
ATOM   2057 S  SD  . MET A 1 267 ? 26.99900  18.18000  22.67600 1.000 15.86000 ? 267 MET A SD  1 
ATOM   2058 C  CE  . MET A 1 267 ? 26.36900  17.38400  24.15100 1.000 17.69000 ? 267 MET A CE  1 
ATOM   2059 N  N   . SER A 1 268 ? 21.98700  18.93600  20.92100 1.000 15.19000 ? 268 SER A N   1 
ATOM   2060 C  CA  . SER A 1 268 ? 20.55800  19.13400  20.71200 1.000 14.23000 ? 268 SER A CA  1 
ATOM   2061 C  C   . SER A 1 268 ? 19.76500  18.95300  22.00500 1.000 12.17000 ? 268 SER A C   1 
ATOM   2062 O  O   . SER A 1 268 ? 19.93100  17.96300  22.72300 1.000 11.59000 ? 268 SER A O   1 
ATOM   2063 C  CB  . SER A 1 268 ? 20.07700  18.16200  19.64200 1.000 11.78000 ? 268 SER A CB  1 
ATOM   2064 O  OG  . SER A 1 268 ? 21.00200  18.16200  18.54600 1.000 12.78000 ? 268 SER A OG  1 
ATOM   2065 N  N   . GLU A 1 269 ? 18.88600  19.91400  22.28500 1.000 12.98000 ? 269 GLU A N   1 
ATOM   2066 C  CA  . GLU A 1 269 ? 18.03100  19.93900  23.48000 1.000 12.64000 ? 269 GLU A CA  1 
ATOM   2067 C  C   . GLU A 1 269 ? 18.83200  20.00200  24.77500 1.000 12.80000 ? 269 GLU A C   1 
ATOM   2068 O  O   . GLU A 1 269 ? 18.30400  19.72000  25.85900 1.000 12.33000 ? 269 GLU A O   1 
ATOM   2069 C  CB  . GLU A 1 269 ? 17.04600  18.75400  23.52500 1.000 14.17000 ? 269 GLU A CB  1 
ATOM   2070 C  CG  . GLU A 1 269 ? 15.69300  19.16100  24.20300 1.000 13.60000 ? 269 GLU A CG  1 
ATOM   2071 C  CD  . GLU A 1 269 ? 14.58600  18.09500  24.17400 1.000 15.44000 ? 269 GLU A CD  1 
ATOM   2072 O  OE1 . GLU A 1 269 ? 14.43500  17.35700  23.17000 1.000 14.35000 ? 269 GLU A OE1 1 
ATOM   2073 O  OE2 . GLU A 1 269 ? 13.83100  18.01700  25.17000 1.000 17.22000 ? 269 GLU A OE2 1 
ATOM   2074 N  N   . GLY A 1 270 ? 20.09100  20.41200  24.70600 1.000 14.46000 ? 270 GLY A N   1 
ATOM   2075 C  CA  . GLY A 1 270 ? 20.88900  20.44600  25.91000 1.000 13.99000 ? 270 GLY A CA  1 
ATOM   2076 C  C   . GLY A 1 270 ? 20.75900  21.68400  26.75500 1.000 14.90000 ? 270 GLY A C   1 
ATOM   2077 O  O   . GLY A 1 270 ? 21.21700  21.68100  27.90500 1.000 16.54000 ? 270 GLY A O   1 
ATOM   2078 N  N   . GLY A 1 271 ? 20.13300  22.73700  26.23700 1.000 15.10000 ? 271 GLY A N   1 
ATOM   2079 C  CA  . GLY A 1 271 ? 20.09100  23.99700  26.95000 1.000 13.85000 ? 271 GLY A CA  1 
ATOM   2080 C  C   . GLY A 1 271 ? 21.40400  24.75500  26.82400 1.000 14.72000 ? 271 GLY A C   1 
ATOM   2081 O  O   . GLY A 1 271 ? 22.31600  24.36500  26.09100 1.000 15.96000 ? 271 GLY A O   1 
ATOM   2082 N  N   . VAL A 1 272 ? 21.49700  25.86000  27.56500 1.000 14.43000 ? 272 VAL A N   1 
ATOM   2083 C  CA  . VAL A 1 272 ? 22.59900  26.80500  27.42900 1.000 15.25000 ? 272 VAL A CA  1 
ATOM   2084 C  C   . VAL A 1 272 ? 23.47600  26.84800  28.67400 1.000 15.25000 ? 272 VAL A C   1 
ATOM   2085 O  O   . VAL A 1 272 ? 24.70600  26.88800  28.57100 1.000 13.25000 ? 272 VAL A O   1 
ATOM   2086 C  CB  . VAL A 1 272 ? 22.05600  28.21200  27.09900 1.000 16.27000 ? 272 VAL A CB  1 
ATOM   2087 C  CG1 . VAL A 1 272 ? 23.19000  29.25700  27.14500 1.000 20.94000 ? 272 VAL A CG1 1 
ATOM   2088 C  CG2 . VAL A 1 272 ? 21.39900  28.19800  25.73500 1.000 19.46000 ? 272 VAL A CG2 1 
ATOM   2089 N  N   . GLY A 1 273 ? 22.85900  26.86500  29.85800 1.000 15.60000 ? 273 GLY A N   1 
ATOM   2090 C  CA  . GLY A 1 273 ? 23.55600  27.22000  31.08100 1.000 16.59000 ? 273 GLY A CA  1 
ATOM   2091 C  C   . GLY A 1 273 ? 24.65700  26.26600  31.48500 1.000 15.44000 ? 273 GLY A C   1 
ATOM   2092 O  O   . GLY A 1 273 ? 25.59400  26.68800  32.17000 1.000 16.72000 ? 273 GLY A O   1 
ATOM   2093 N  N   . TRP A 1 274 ? 24.58000  24.99900  31.06600 1.000 12.69000 ? 274 TRP A N   1 
ATOM   2094 C  CA  . TRP A 1 274 ? 25.62400  24.04900  31.44400 1.000 14.44000 ? 274 TRP A CA  1 
ATOM   2095 C  C   . TRP A 1 274 ? 26.98600  24.43000  30.88200 1.000 14.10000 ? 274 TRP A C   1 
ATOM   2096 O  O   . TRP A 1 274 ? 28.02300  24.03000  31.44200 1.000 13.02000 ? 274 TRP A O   1 
ATOM   2097 C  CB  . TRP A 1 274 ? 25.24800  22.64300  30.97300 1.000 15.24000 ? 274 TRP A CB  1 
ATOM   2098 C  CG  . TRP A 1 274 ? 25.18600  22.47900  29.48100 1.000 14.46000 ? 274 TRP A CG  1 
ATOM   2099 C  CD1 . TRP A 1 274 ? 24.09700  22.68100  28.67600 1.000 15.31000 ? 274 TRP A CD1 1 
ATOM   2100 C  CD2 . TRP A 1 274 ? 26.24900  22.07000  28.61600 1.000 12.72000 ? 274 TRP A CD2 1 
ATOM   2101 N  NE1 . TRP A 1 274 ? 24.42000  22.42500  27.36300 1.000 13.77000 ? 274 TRP A NE1 1 
ATOM   2102 C  CE2 . TRP A 1 274 ? 25.73700  22.04800  27.30100 1.000 12.72000 ? 274 TRP A CE2 1 
ATOM   2103 C  CE3 . TRP A 1 274 ? 27.58900  21.72500  28.82400 1.000 14.62000 ? 274 TRP A CE3 1 
ATOM   2104 C  CZ2 . TRP A 1 274 ? 26.51200  21.70000  26.20600 1.000 12.41000 ? 274 TRP A CZ2 1 
ATOM   2105 C  CZ3 . TRP A 1 274 ? 28.36200  21.38900  27.73400 1.000 13.83000 ? 274 TRP A CZ3 1 
ATOM   2106 C  CH2 . TRP A 1 274 ? 27.82200  21.37400  26.43600 1.000 13.77000 ? 274 TRP A CH2 1 
ATOM   2107 N  N   . VAL A 1 275 ? 27.00800  25.20000  29.79400 1.000 12.49000 ? 275 VAL A N   1 
ATOM   2108 C  CA  . VAL A 1 275 ? 28.25000  25.40900  29.05300 1.000 12.46000 ? 275 VAL A CA  1 
ATOM   2109 C  C   . VAL A 1 275 ? 29.23700  26.25800  29.84800 1.000 13.46000 ? 275 VAL A C   1 
ATOM   2110 O  O   . VAL A 1 275 ? 30.42400  25.91800  29.94600 1.000 12.94000 ? 275 VAL A O   1 
ATOM   2111 C  CB  . VAL A 1 275 ? 27.95000  26.03600  27.68400 1.000 12.70000 ? 275 VAL A CB  1 
ATOM   2112 C  CG1 . VAL A 1 275 ? 29.27500  26.26400  26.90500 1.000 12.25000 ? 275 VAL A CG1 1 
ATOM   2113 C  CG2 . VAL A 1 275 ? 26.99300  25.13000  26.90700 1.000 13.87000 ? 275 VAL A CG2 1 
ATOM   2114 N  N   . ALA A 1 276 ? 28.77100  27.38200  30.40400 1.000 12.58000 ? 276 ALA A N   1 
ATOM   2115 C  CA  . ALA A 1 276 ? 29.67700  28.34100  31.03900 1.000 12.94000 ? 276 ALA A CA  1 
ATOM   2116 C  C   . ALA A 1 276 ? 30.53900  27.73800  32.14500 1.000 12.78000 ? 276 ALA A C   1 
ATOM   2117 O  O   . ALA A 1 276 ? 31.77400  27.89700  32.08100 1.000 12.27000 ? 276 ALA A O   1 
ATOM   2118 C  CB  . ALA A 1 276 ? 28.87200  29.54700  31.54900 1.000 15.72000 ? 276 ALA A CB  1 
ATOM   2119 N  N   . PRO A 1 277 ? 29.99400  27.06700  33.17200 1.000 13.20000 ? 277 PRO A N   1 
ATOM   2120 C  CA  . PRO A 1 277 ? 30.88400  26.46900  34.19200 1.000 11.63000 ? 277 PRO A CA  1 
ATOM   2121 C  C   . PRO A 1 277 ? 31.79100  25.40000  33.61900 1.000 15.19000 ? 277 PRO A C   1 
ATOM   2122 O  O   . PRO A 1 277 ? 32.92200  25.20300  34.08800 1.000 13.66000 ? 277 PRO A O   1 
ATOM   2123 C  CB  . PRO A 1 277 ? 29.90200  25.87900  35.21900 1.000 12.67000 ? 277 PRO A CB  1 
ATOM   2124 C  CG  . PRO A 1 277 ? 28.59700  25.69900  34.46800 1.000 14.89000 ? 277 PRO A CG  1 
ATOM   2125 C  CD  . PRO A 1 277 ? 28.56300  26.84600  33.49700 1.000 11.93000 ? 277 PRO A CD  1 
ATOM   2126 N  N   . TRP A 1 278 ? 31.31000  24.69600  32.60400 1.000 13.21000 ? 278 TRP A N   1 
ATOM   2127 C  CA  . TRP A 1 278 ? 32.09100  23.62800  32.00000 1.000 15.80000 ? 278 TRP A CA  1 
ATOM   2128 C  C   . TRP A 1 278 ? 33.29500  24.20000  31.26800 1.000 13.93000 ? 278 TRP A C   1 
ATOM   2129 O  O   . TRP A 1 278 ? 34.42600  23.71200  31.42100 1.000 13.10000 ? 278 TRP A O   1 
ATOM   2130 C  CB  . TRP A 1 278 ? 31.17400  22.83700  31.07400 1.000 9.92000  ? 278 TRP A CB  1 
ATOM   2131 C  CG  . TRP A 1 278 ? 31.79300  21.79200  30.20100 1.000 12.80000 ? 278 TRP A CG  1 
ATOM   2132 C  CD1 . TRP A 1 278 ? 32.29000  20.56900  30.58200 1.000 15.98000 ? 278 TRP A CD1 1 
ATOM   2133 C  CD2 . TRP A 1 278 ? 31.89500  21.84100  28.77600 1.000 14.38000 ? 278 TRP A CD2 1 
ATOM   2134 N  NE1 . TRP A 1 278 ? 32.72600  19.87000  29.47100 1.000 14.52000 ? 278 TRP A NE1 1 
ATOM   2135 C  CE2 . TRP A 1 278 ? 32.47800  20.62500  28.35200 1.000 15.96000 ? 278 TRP A CE2 1 
ATOM   2136 C  CE3 . TRP A 1 278 ? 31.53800  22.78900  27.81700 1.000 15.03000 ? 278 TRP A CE3 1 
ATOM   2137 C  CZ2 . TRP A 1 278 ? 32.73300  20.35000  27.00200 1.000 16.63000 ? 278 TRP A CZ2 1 
ATOM   2138 C  CZ3 . TRP A 1 278 ? 31.80500  22.51500  26.47400 1.000 16.54000 ? 278 TRP A CZ3 1 
ATOM   2139 C  CH2 . TRP A 1 278 ? 32.39400  21.30600  26.08600 1.000 16.33000 ? 278 TRP A CH2 1 
ATOM   2140 N  N   . LEU A 1 279 ? 33.08100  25.26800  30.49900 1.000 12.38000 ? 279 LEU A N   1 
ATOM   2141 C  CA  . LEU A 1 279 ? 34.20800  25.90600  29.82100 1.000 14.99000 ? 279 LEU A CA  1 
ATOM   2142 C  C   . LEU A 1 279 ? 35.17900  26.51900  30.82500 1.000 14.16000 ? 279 LEU A C   1 
ATOM   2143 O  O   . LEU A 1 279 ? 36.39600  26.48500  30.61300 1.000 15.68000 ? 279 LEU A O   1 
ATOM   2144 C  CB  . LEU A 1 279 ? 33.70300  26.96200  28.83900 1.000 15.91000 ? 279 LEU A CB  1 
ATOM   2145 C  CG  . LEU A 1 279 ? 32.98200  26.45500  27.57700 1.000 15.09000 ? 279 LEU A CG  1 
ATOM   2146 C  CD1 . LEU A 1 279 ? 32.57700  27.62600  26.71600 1.000 15.29000 ? 279 LEU A CD1 1 
ATOM   2147 C  CD2 . LEU A 1 279 ? 33.86200  25.50100  26.78700 1.000 13.76000 ? 279 LEU A CD2 1 
ATOM   2148 N  N   . ASP A 1 280 ? 34.66900  27.09100  31.92200 1.000 15.50000 ? 280 ASP A N   1 
ATOM   2149 C  CA  . ASP A 1 280 ? 35.56100  27.63500  32.94200 1.000 13.68000 ? 280 ASP A CA  1 
ATOM   2150 C  C   . ASP A 1 280 ? 36.48500  26.54900  33.47000 1.000 16.37000 ? 280 ASP A C   1 
ATOM   2151 O  O   . ASP A 1 280 ? 37.69400  26.75100  33.59200 1.000 14.35000 ? 280 ASP A O   1 
ATOM   2152 C  CB  . ASP A 1 280 ? 34.76500  28.24600  34.10400 1.000 14.18000 ? 280 ASP A CB  1 
ATOM   2153 C  CG  . ASP A 1 280 ? 34.20200  29.63600  33.78700 1.000 18.80000 ? 280 ASP A CG  1 
ATOM   2154 O  OD1 . ASP A 1 280 ? 34.42700  30.15500  32.66900 1.000 18.18000 ? 280 ASP A OD1 1 
ATOM   2155 O  OD2 . ASP A 1 280 ? 33.51800  30.20400  34.66400 1.000 14.21000 ? 280 ASP A OD2 1 
ATOM   2156 N  N   . ARG A 1 281 ? 35.92800  25.37700  33.77100 1.000 14.06000 ? 281 ARG A N   1 
ATOM   2157 C  CA  . ARG A 1 281 ? 36.75100  24.30000  34.29800 1.000 14.45000 ? 281 ARG A CA  1 
ATOM   2158 C  C   . ARG A 1 281 ? 37.69900  23.75600  33.23900 1.000 15.03000 ? 281 ARG A C   1 
ATOM   2159 O  O   . ARG A 1 281 ? 38.86800  23.48800  33.53100 1.000 15.58000 ? 281 ARG A O   1 
ATOM   2160 C  CB  . ARG A 1 281 ? 35.87500  23.18200  34.85500 1.000 17.59000 ? 281 ARG A CB  1 
ATOM   2161 C  CG  . ARG A 1 281 ? 36.70200  22.12200  35.53400 1.000 21.47000 ? 281 ARG A CG  1 
ATOM   2162 C  CD  . ARG A 1 281 ? 35.88900  21.13000  36.35700 1.000 21.23000 ? 281 ARG A CD  1 
ATOM   2163 N  NE  . ARG A 1 281 ? 36.81200  20.24200  37.06100 1.000 21.41000 ? 281 ARG A NE  1 
ATOM   2164 C  CZ  . ARG A 1 281 ? 37.46700  20.57900  38.17200 1.000 29.25000 ? 281 ARG A CZ  1 
ATOM   2165 N  NH1 . ARG A 1 281 ? 37.27800  21.77800  38.72000 1.000 25.27000 ? 281 ARG A NH1 1 
ATOM   2166 N  NH2 . ARG A 1 281 ? 38.30400  19.71900  38.74300 1.000 28.46000 ? 281 ARG A NH2 1 
ATOM   2167 N  N   . LEU A 1 282 ? 37.22000  23.57400  32.00700 1.000 14.29000 ? 282 LEU A N   1 
ATOM   2168 C  CA  . LEU A 1 282 ? 38.10700  23.07800  30.95600 1.000 16.45000 ? 282 LEU A CA  1 
ATOM   2169 C  C   . LEU A 1 282 ? 39.21800  24.07900  30.66100 1.000 17.30000 ? 282 LEU A C   1 
ATOM   2170 O  O   . LEU A 1 282 ? 40.39500  23.70500  30.56400 1.000 16.94000 ? 282 LEU A O   1 
ATOM   2171 C  CB  . LEU A 1 282 ? 37.31300  22.78000  29.68800 1.000 16.60000 ? 282 LEU A CB  1 
ATOM   2172 C  CG  . LEU A 1 282 ? 36.58000  21.46300  29.50000 1.000 20.56000 ? 282 LEU A CG  1 
ATOM   2173 C  CD1 . LEU A 1 282 ? 35.67600  21.58800  28.30400 1.000 21.74000 ? 282 LEU A CD1 1 
ATOM   2174 C  CD2 . LEU A 1 282 ? 37.54500  20.33200  29.29000 1.000 22.41000 ? 282 LEU A CD2 1 
ATOM   2175 N  N   . ASP A 1 283 ? 38.85500  25.35400  30.47200 1.000 12.44000 ? 283 ASP A N   1 
ATOM   2176 C  CA  . ASP A 1 283 ? 39.85000  26.38800  30.20000 1.000 14.53000 ? 283 ASP A CA  1 
ATOM   2177 C  C   . ASP A 1 283 ? 40.95100  26.35600  31.24800 1.000 15.84000 ? 283 ASP A C   1 
ATOM   2178 O  O   . ASP A 1 283 ? 42.14000  26.36200  30.91300 1.000 15.32000 ? 283 ASP A O   1 
ATOM   2179 C  CB  . ASP A 1 283 ? 39.20200  27.78000  30.16500 1.000 17.22000 ? 283 ASP A CB  1 
ATOM   2180 C  CG  . ASP A 1 283 ? 38.55800  28.12300  28.81900 1.000 15.83000 ? 283 ASP A CG  1 
ATOM   2181 O  OD1 . ASP A 1 283 ? 38.74500  27.39500  27.82600 1.000 18.11000 ? 283 ASP A OD1 1 
ATOM   2182 O  OD2 . ASP A 1 283 ? 37.85200  29.15700  28.75400 1.000 18.12000 ? 283 ASP A OD2 1 
ATOM   2183 N  N   . ARG A 1 284 ? 40.56700  26.30800  32.53000 1.000 19.50000 ? 284 ARG A N   1 
ATOM   2184 C  CA  A ARG A 1 284 ? 41.55500  26.30300  33.60700 0.459 17.97000 ? 284 ARG A CA  1 
ATOM   2185 C  CA  B ARG A 1 284 ? 41.55800  26.30700  33.60100 0.541 17.96000 ? 284 ARG A CA  1 
ATOM   2186 C  C   . ARG A 1 284 ? 42.39000  25.02900  33.58400 1.000 18.67000 ? 284 ARG A C   1 
ATOM   2187 O  O   . ARG A 1 284 ? 43.59700  25.06600  33.85500 1.000 21.36000 ? 284 ARG A O   1 
ATOM   2188 C  CB  A ARG A 1 284 ? 40.86300  26.46500  34.96700 0.459 19.40000 ? 284 ARG A CB  1 
ATOM   2189 C  CB  B ARG A 1 284 ? 40.85900  26.48400  34.94800 0.541 19.39000 ? 284 ARG A CB  1 
ATOM   2190 C  CG  A ARG A 1 284 ? 41.82400  26.61300  36.16400 0.459 21.09000 ? 284 ARG A CG  1 
ATOM   2191 C  CG  B ARG A 1 284 ? 41.75000  26.28600  36.16400 0.541 21.09000 ? 284 ARG A CG  1 
ATOM   2192 C  CD  A ARG A 1 284 ? 41.13400  26.34300  37.52400 0.459 23.18000 ? 284 ARG A CD  1 
ATOM   2193 C  CD  B ARG A 1 284 ? 40.99200  26.64000  37.44600 0.541 23.18000 ? 284 ARG A CD  1 
ATOM   2194 N  NE  A ARG A 1 284 ? 42.06500  26.46200  38.65500 0.459 20.89000 ? 284 ARG A NE  1 
ATOM   2195 N  NE  B ARG A 1 284 ? 39.56400  26.36800  37.31700 0.541 19.08000 ? 284 ARG A NE  1 
ATOM   2196 C  CZ  A ARG A 1 284 ? 41.86400  25.93500  39.86300 0.459 19.63000 ? 284 ARG A CZ  1 
ATOM   2197 C  CZ  B ARG A 1 284 ? 38.89900  25.44400  38.00500 0.541 23.65000 ? 284 ARG A CZ  1 
ATOM   2198 N  NH1 A ARG A 1 284 ? 40.76000  25.24300  40.12300 0.459 21.51000 ? 284 ARG A NH1 1 
ATOM   2199 N  NH1 B ARG A 1 284 ? 39.51700  24.68800  38.90500 0.541 26.72000 ? 284 ARG A NH1 1 
ATOM   2200 N  NH2 A ARG A 1 284 ? 42.77200  26.09900  40.81800 0.459 20.21000 ? 284 ARG A NH2 1 
ATOM   2201 N  NH2 B ARG A 1 284 ? 37.60300  25.28400  37.79800 0.541 21.04000 ? 284 ARG A NH2 1 
ATOM   2202 N  N   . HIS A 1 285 ? 41.76600  23.89000  33.26800 1.000 17.90000 ? 285 HIS A N   1 
ATOM   2203 C  CA  . HIS A 1 285 ? 42.52300  22.64400  33.16900 1.000 19.57000 ? 285 HIS A CA  1 
ATOM   2204 C  C   . HIS A 1 285 ? 43.61600  22.72900  32.10200 1.000 21.17000 ? 285 HIS A C   1 
ATOM   2205 O  O   . HIS A 1 285 ? 44.74900  22.28400  32.32300 1.000 17.43000 ? 285 HIS A O   1 
ATOM   2206 C  CB  . HIS A 1 285 ? 41.58900  21.48100  32.86300 1.000 19.11000 ? 285 HIS A CB  1 
ATOM   2207 C  CG  . HIS A 1 285 ? 42.27200  20.15300  32.89800 1.000 27.13000 ? 285 HIS A CG  1 
ATOM   2208 N  ND1 . HIS A 1 285 ? 42.48700  19.39200  31.76800 1.000 33.02000 ? 285 HIS A ND1 1 
ATOM   2209 C  CD2 . HIS A 1 285 ? 42.83900  19.47500  33.92300 1.000 26.67000 ? 285 HIS A CD2 1 
ATOM   2210 C  CE1 . HIS A 1 285 ? 43.13200  18.28900  32.10100 1.000 27.85000 ? 285 HIS A CE1 1 
ATOM   2211 N  NE2 . HIS A 1 285 ? 43.35400  18.31400  33.40300 1.000 32.99000 ? 285 HIS A NE2 1 
ATOM   2212 N  N   . ILE A 1 286 ? 43.29300  23.28100  30.93300 1.000 19.99000 ? 286 ILE A N   1 
ATOM   2213 C  CA  . ILE A 1 286 ? 44.28600  23.35600  29.86500 1.000 19.64000 ? 286 ILE A CA  1 
ATOM   2214 C  C   . ILE A 1 286 ? 45.44000  24.27200  30.25800 1.000 22.45000 ? 286 ILE A C   1 
ATOM   2215 O  O   . ILE A 1 286 ? 46.60700  23.98200  29.96400 1.000 20.26000 ? 286 ILE A O   1 
ATOM   2216 C  CB  . ILE A 1 286 ? 43.62000  23.79700  28.55100 1.000 16.51000 ? 286 ILE A CB  1 
ATOM   2217 C  CG1 . ILE A 1 286 ? 42.84800  22.63000  27.94600 1.000 16.39000 ? 286 ILE A CG1 1 
ATOM   2218 C  CG2 . ILE A 1 286 ? 44.66000  24.30600  27.55600 1.000 24.19000 ? 286 ILE A CG2 1 
ATOM   2219 C  CD1 . ILE A 1 286 ? 43.73500  21.46900  27.51400 1.000 20.87000 ? 286 ILE A CD1 1 
ATOM   2220 N  N   . VAL A 1 287 ? 45.14300  25.38800  30.92700 1.000 20.52000 ? 287 VAL A N   1 
ATOM   2221 C  CA  . VAL A 1 287 ? 46.20800  26.26000  31.41600 1.000 19.17000 ? 287 VAL A CA  1 
ATOM   2222 C  C   . VAL A 1 287 ? 47.08000  25.51900  32.42100 1.000 21.86000 ? 287 VAL A C   1 
ATOM   2223 O  O   . VAL A 1 287 ? 48.31100  25.49700  32.30900 1.000 20.25000 ? 287 VAL A O   1 
ATOM   2224 C  CB  . VAL A 1 287 ? 45.61000  27.53900  32.02800 1.000 20.79000 ? 287 VAL A CB  1 
ATOM   2225 C  CG1 . VAL A 1 287 ? 46.65400  28.26500  32.86400 1.000 25.58000 ? 287 VAL A CG1 1 
ATOM   2226 C  CG2 . VAL A 1 287 ? 45.06600  28.44600  30.93400 1.000 17.88000 ? 287 VAL A CG2 1 
ATOM   2227 N  N   . ASN A 1 288 ? 46.45100  24.87500  33.40400 1.000 19.31000 ? 288 ASN A N   1 
ATOM   2228 C  CA  . ASN A 1 288 ? 47.19400  24.22600  34.48000 1.000 21.72000 ? 288 ASN A CA  1 
ATOM   2229 C  C   . ASN A 1 288 ? 47.95300  22.98700  34.02300 1.000 19.10000 ? 288 ASN A C   1 
ATOM   2230 O  O   . ASN A 1 288 ? 48.89100  22.56300  34.70700 1.000 23.92000 ? 288 ASN A O   1 
ATOM   2231 C  CB  . ASN A 1 288 ? 46.23900  23.83800  35.60900 1.000 16.81000 ? 288 ASN A CB  1 
ATOM   2232 C  CG  . ASN A 1 288 ? 45.71700  25.03500  36.36100 1.000 24.19000 ? 288 ASN A CG  1 
ATOM   2233 O  OD1 . ASN A 1 288 ? 46.35000  26.08900  36.38800 1.000 24.44000 ? 288 ASN A OD1 1 
ATOM   2234 N  ND2 . ASN A 1 288 ? 44.55800  24.87900  36.98800 1.000 27.19000 ? 288 ASN A ND2 1 
ATOM   2235 N  N   . GLN A 1 289 ? 47.55400  22.37400  32.91500 1.000 17.78000 ? 289 GLN A N   1 
ATOM   2236 C  CA  . GLN A 1 289 ? 48.22200  21.17900  32.42400 1.000 17.34000 ? 289 GLN A CA  1 
ATOM   2237 C  C   . GLN A 1 289 ? 49.09300  21.45800  31.20500 1.000 19.10000 ? 289 GLN A C   1 
ATOM   2238 O  O   . GLN A 1 289 ? 49.60300  20.51500  30.60200 1.000 19.27000 ? 289 GLN A O   1 
ATOM   2239 C  CB  . GLN A 1 289 ? 47.19500  20.09500  32.10700 1.000 21.16000 ? 289 GLN A CB  1 
ATOM   2240 C  CG  . GLN A 1 289 ? 46.49900  19.53500  33.35000 1.000 27.09000 ? 289 GLN A CG  1 
ATOM   2241 C  CD  . GLN A 1 289 ? 47.43300  18.71400  34.22300 1.000 30.29000 ? 289 GLN A CD  1 
ATOM   2242 O  OE1 . GLN A 1 289 ? 47.93200  19.19000  35.24600 1.000 29.80000 ? 289 GLN A OE1 1 
ATOM   2243 N  NE2 . GLN A 1 289 ? 47.67000  17.46900  33.82200 1.000 33.42000 ? 289 GLN A NE2 1 
ATOM   2244 N  N   . SER A 1 290 ? 49.27700  22.72500  30.83200 1.000 17.99000 ? 290 SER A N   1 
ATOM   2245 C  CA  . SER A 1 290 ? 50.08000  23.03700  29.65300 1.000 20.59000 ? 290 SER A CA  1 
ATOM   2246 C  C   . SER A 1 290 ? 51.51100  22.53000  29.78000 1.000 19.47000 ? 290 SER A C   1 
ATOM   2247 O  O   . SER A 1 290 ? 52.15900  22.28800  28.75700 1.000 21.33000 ? 290 SER A O   1 
ATOM   2248 C  CB  . SER A 1 290 ? 50.06900  24.54600  29.38300 1.000 25.22000 ? 290 SER A CB  1 
ATOM   2249 O  OG  . SER A 1 290 ? 50.71200  25.26300  30.42600 1.000 30.07000 ? 290 SER A OG  1 
ATOM   2250 N  N   . TRP A 1 291 ? 52.00300  22.32800  31.00800 1.000 21.87000 ? 291 TRP A N   1 
ATOM   2251 C  CA  . TRP A 1 291 ? 53.34600  21.78800  31.20900 1.000 22.45000 ? 291 TRP A CA  1 
ATOM   2252 C  C   . TRP A 1 291 ? 53.51600  20.39000  30.61900 1.000 19.84000 ? 291 TRP A C   1 
ATOM   2253 O  O   . TRP A 1 291 ? 54.65700  19.97600  30.39100 1.000 18.01000 ? 291 TRP A O   1 
ATOM   2254 C  CB  . TRP A 1 291 ? 53.68700  21.75100  32.70800 1.000 23.00000 ? 291 TRP A CB  1 
ATOM   2255 C  CG  . TRP A 1 291 ? 52.76900  20.85600  33.49500 1.000 20.14000 ? 291 TRP A CG  1 
ATOM   2256 C  CD1 . TRP A 1 291 ? 51.57000  21.20400  34.08300 1.000 22.87000 ? 291 TRP A CD1 1 
ATOM   2257 C  CD2 . TRP A 1 291 ? 52.96000  19.46600  33.77900 1.000 21.68000 ? 291 TRP A CD2 1 
ATOM   2258 N  NE1 . TRP A 1 291 ? 51.01200  20.10800  34.71000 1.000 17.16000 ? 291 TRP A NE1 1 
ATOM   2259 C  CE2 . TRP A 1 291 ? 51.84100  19.03000  34.53300 1.000 22.87000 ? 291 TRP A CE2 1 
ATOM   2260 C  CE3 . TRP A 1 291 ? 53.96900  18.54300  33.47000 1.000 18.60000 ? 291 TRP A CE3 1 
ATOM   2261 C  CZ2 . TRP A 1 291 ? 51.70800  17.71800  34.98000 1.000 22.84000 ? 291 TRP A CZ2 1 
ATOM   2262 C  CZ3 . TRP A 1 291 ? 53.83000  17.23900  33.91500 1.000 18.48000 ? 291 TRP A CZ3 1 
ATOM   2263 C  CH2 . TRP A 1 291 ? 52.70700  16.84000  34.65900 1.000 22.23000 ? 291 TRP A CH2 1 
ATOM   2264 N  N   . THR A 1 292 ? 52.42800  19.63700  30.39600 1.000 18.01000 ? 292 THR A N   1 
ATOM   2265 C  CA  . THR A 1 292 ? 52.58400  18.28000  29.86400 1.000 19.13000 ? 292 THR A CA  1 
ATOM   2266 C  C   . THR A 1 292 ? 53.02300  18.26500  28.40400 1.000 17.91000 ? 292 THR A C   1 
ATOM   2267 O  O   . THR A 1 292 ? 53.49000  17.22400  27.92100 1.000 20.62000 ? 292 THR A O   1 
ATOM   2268 C  CB  . THR A 1 292 ? 51.28500  17.47400  29.97600 1.000 19.60000 ? 292 THR A CB  1 
ATOM   2269 O  OG1 . THR A 1 292 ? 50.31000  17.99900  29.05600 1.000 18.15000 ? 292 THR A OG1 1 
ATOM   2270 C  CG2 . THR A 1 292 ? 50.75900  17.47600  31.41300 1.000 18.05000 ? 292 THR A CG2 1 
ATOM   2271 N  N   . GLY A 1 293 ? 52.84400  19.36500  27.68400 1.000 14.93000 ? 293 GLY A N   1 
ATOM   2272 C  CA  . GLY A 1 293 ? 53.23200  19.42100  26.28700 1.000 20.65000 ? 293 GLY A CA  1 
ATOM   2273 C  C   . GLY A 1 293 ? 52.25200  18.80200  25.31800 1.000 25.02000 ? 293 GLY A C   1 
ATOM   2274 O  O   . GLY A 1 293 ? 52.60400  18.59700  24.14900 1.000 18.65000 ? 293 GLY A O   1 
ATOM   2275 N  N   . THR A 1 294 ? 51.02900  18.51000  25.75300 1.000 19.44000 ? 294 THR A N   1 
ATOM   2276 C  CA  . THR A 1 294 ? 50.03400  17.96300  24.84200 1.000 22.46000 ? 294 THR A CA  1 
ATOM   2277 C  C   . THR A 1 294 ? 48.65800  18.20900  25.42800 1.000 20.90000 ? 294 THR A C   1 
ATOM   2278 O  O   . THR A 1 294 ? 48.51400  18.48100  26.62200 1.000 23.37000 ? 294 THR A O   1 
ATOM   2279 C  CB  . THR A 1 294 ? 50.25800  16.46800  24.59500 1.000 28.58000 ? 294 THR A CB  1 
ATOM   2280 O  OG1 . THR A 1 294 ? 49.24100  15.96100  23.71700 1.000 36.27000 ? 294 THR A OG1 1 
ATOM   2281 C  CG2 . THR A 1 294 ? 50.24900  15.70400  25.90600 1.000 25.61000 ? 294 THR A CG2 1 
ATOM   2282 N  N   . SER A 1 295 ? 47.64700  18.12200  24.56900 1.000 20.11000 ? 295 SER A N   1 
ATOM   2283 C  CA  . SER A 1 295 ? 46.27200  18.24800  25.02700 1.000 21.97000 ? 295 SER A CA  1 
ATOM   2284 C  C   . SER A 1 295 ? 45.36400  17.57700  24.01100 1.000 21.57000 ? 295 SER A C   1 
ATOM   2285 O  O   . SER A 1 295 ? 45.80300  17.11800  22.95000 1.000 19.49000 ? 295 SER A O   1 
ATOM   2286 C  CB  . SER A 1 295 ? 45.86600  19.71100  25.23500 1.000 24.99000 ? 295 SER A CB  1 
ATOM   2287 O  OG  . SER A 1 295 ? 45.45500  20.31700  24.01900 1.000 25.33000 ? 295 SER A OG  1 
ATOM   2288 N  N   . PHE A 1 296 ? 44.08700  17.50700  24.37000 1.000 20.95000 ? 296 PHE A N   1 
ATOM   2289 C  CA  . PHE A 1 296 ? 43.07600  16.88100  23.53600 1.000 17.25000 ? 296 PHE A CA  1 
ATOM   2290 C  C   . PHE A 1 296 ? 42.58200  17.80500  22.44100 1.000 18.17000 ? 296 PHE A C   1 
ATOM   2291 O  O   . PHE A 1 296 ? 41.73700  17.39500  21.63800 1.000 16.54000 ? 296 PHE A O   1 
ATOM   2292 C  CB  . PHE A 1 296 ? 41.90500  16.41600  24.41300 1.000 18.01000 ? 296 PHE A CB  1 
ATOM   2293 C  CG  . PHE A 1 296 ? 41.51700  17.39800  25.49100 1.000 17.75000 ? 296 PHE A CG  1 
ATOM   2294 C  CD1 . PHE A 1 296 ? 40.60900  18.40600  25.23000 1.000 20.96000 ? 296 PHE A CD1 1 
ATOM   2295 C  CD2 . PHE A 1 296 ? 42.04400  17.29800  26.77300 1.000 24.43000 ? 296 PHE A CD2 1 
ATOM   2296 C  CE1 . PHE A 1 296 ? 40.23500  19.32400  26.21900 1.000 20.37000 ? 296 PHE A CE1 1 
ATOM   2297 C  CE2 . PHE A 1 296 ? 41.67600  18.20300  27.77100 1.000 23.86000 ? 296 PHE A CE2 1 
ATOM   2298 C  CZ  . PHE A 1 296 ? 40.76200  19.21900  27.49100 1.000 17.85000 ? 296 PHE A CZ  1 
ATOM   2299 N  N   . LEU A 1 297 ? 43.11700  19.01600  22.37500 1.000 15.66000 ? 297 LEU A N   1 
ATOM   2300 C  CA  . LEU A 1 297 ? 42.69100  20.05700  21.46900 1.000 19.04000 ? 297 LEU A CA  1 
ATOM   2301 C  C   . LEU A 1 297 ? 43.75400  20.32900  20.41800 1.000 19.23000 ? 297 LEU A C   1 
ATOM   2302 O  O   . LEU A 1 297 ? 44.93100  20.01100  20.61600 1.000 17.21000 ? 297 LEU A O   1 
ATOM   2303 C  CB  . LEU A 1 297 ? 42.39500  21.34200  22.24900 1.000 18.90000 ? 297 LEU A CB  1 
ATOM   2304 C  CG  . LEU A 1 297 ? 41.24100  21.19800  23.24900 1.000 21.90000 ? 297 LEU A CG  1 
ATOM   2305 C  CD1 . LEU A 1 297 ? 40.91000  22.52700  23.83700 1.000 20.03000 ? 297 LEU A CD1 1 
ATOM   2306 C  CD2 . LEU A 1 297 ? 39.99600  20.57000  22.61800 1.000 23.14000 ? 297 LEU A CD2 1 
ATOM   2307 N  N   . PRO A 1 298 ? 43.37300  20.92400  19.28500 1.000 19.22000 ? 298 PRO A N   1 
ATOM   2308 C  CA  . PRO A 1 298 ? 44.37700  21.35400  18.31000 1.000 21.95000 ? 298 PRO A CA  1 
ATOM   2309 C  C   . PRO A 1 298 ? 45.29900  22.39300  18.92100 1.000 23.17000 ? 298 PRO A C   1 
ATOM   2310 O  O   . PRO A 1 298 ? 44.88400  23.21300  19.74100 1.000 20.89000 ? 298 PRO A O   1 
ATOM   2311 C  CB  . PRO A 1 298 ? 43.53600  21.95400  17.17400 1.000 20.22000 ? 298 PRO A CB  1 
ATOM   2312 C  CG  . PRO A 1 298 ? 42.11700  21.48200  17.42800 1.000 20.67000 ? 298 PRO A CG  1 
ATOM   2313 C  CD  . PRO A 1 298 ? 42.01400  21.35700  18.90300 1.000 20.89000 ? 298 PRO A CD  1 
ATOM   2314 N  N   . LYS A 1 299 ? 46.56200  22.37400  18.49400 1.000 24.04000 ? 299 LYS A N   1 
ATOM   2315 C  CA  . LYS A 1 299 ? 47.55300  23.23000  19.13300 1.000 21.84000 ? 299 LYS A CA  1 
ATOM   2316 C  C   . LYS A 1 299 ? 47.15500  24.68900  19.00700 1.000 17.43000 ? 299 LYS A C   1 
ATOM   2317 O  O   . LYS A 1 299 ? 46.58000  25.11200  18.00300 1.000 21.70000 ? 299 LYS A O   1 
ATOM   2318 C  CB  . LYS A 1 299 ? 48.94000  23.01400  18.52300 1.000 30.79000 ? 299 LYS A CB  1 
ATOM   2319 C  CG  . LYS A 1 299 ? 50.05900  23.02300  19.56600 1.000 34.31000 ? 299 LYS A CG  1 
ATOM   2320 C  CD  . LYS A 1 299 ? 51.41300  22.80400  18.92800 1.000 30.08000 ? 299 LYS A CD  1 
ATOM   2321 C  CE  . LYS A 1 299 ? 52.22000  21.74400  19.66600 1.000 36.62000 ? 299 LYS A CE  1 
ATOM   2322 N  NZ  . LYS A 1 299 ? 53.01900  22.31200  20.79300 1.000 26.88000 ? 299 LYS A NZ  1 
ATOM   2323 N  N   . GLY A 1 300 ? 47.44900  25.45600  20.04700 1.000 20.17000 ? 300 GLY A N   1 
ATOM   2324 C  CA  . GLY A 1 300 ? 47.13500  26.86500  20.05200 1.000 21.27000 ? 300 GLY A CA  1 
ATOM   2325 C  C   . GLY A 1 300 ? 45.68000  27.21300  20.29100 1.000 26.27000 ? 300 GLY A C   1 
ATOM   2326 O  O   . GLY A 1 300 ? 45.30600  28.37300  20.09900 1.000 25.74000 ? 300 GLY A O   1 
ATOM   2327 N  N   . MET A 1 301 ? 44.84500  26.26400  20.70900 1.000 22.93000 ? 301 MET A N   1 
ATOM   2328 C  CA  A MET A 1 301 ? 43.43600  26.53700  20.95800 0.620 20.41000 ? 301 MET A CA  1 
ATOM   2329 C  CA  B MET A 1 301 ? 43.43000  26.52300  20.95100 0.380 20.42000 ? 301 MET A CA  1 
ATOM   2330 C  C   . MET A 1 301 ? 43.07800  26.25100  22.40800 1.000 19.32000 ? 301 MET A C   1 
ATOM   2331 O  O   . MET A 1 301 ? 43.55700  25.28100  23.00300 1.000 20.99000 ? 301 MET A O   1 
ATOM   2332 C  CB  A MET A 1 301 ? 42.55000  25.71500  20.03200 0.620 19.95000 ? 301 MET A CB  1 
ATOM   2333 C  CB  B MET A 1 301 ? 42.54100  25.66600  20.03500 0.380 19.93000 ? 301 MET A CB  1 
ATOM   2334 C  CG  A MET A 1 301 ? 42.61600  26.19200  18.60200 0.620 18.29000 ? 301 MET A CG  1 
ATOM   2335 C  CG  B MET A 1 301 ? 42.77700  25.90500  18.54800 0.380 18.64000 ? 301 MET A CG  1 
ATOM   2336 S  SD  A MET A 1 301 ? 41.50200  25.25100  17.57100 0.620 18.99000 ? 301 MET A SD  1 
ATOM   2337 S  SD  B MET A 1 301 ? 41.74800  27.20200  17.83300 0.380 19.57000 ? 301 MET A SD  1 
ATOM   2338 C  CE  A MET A 1 301 ? 39.97600  26.17000  17.79100 0.620 17.38000 ? 301 MET A CE  1 
ATOM   2339 C  CE  B MET A 1 301 ? 40.20400  26.32700  17.58800 0.380 17.55000 ? 301 MET A CE  1 
ATOM   2340 N  N   . THR A 1 302 ? 42.24900  27.11200  22.97100 1.000 17.55000 ? 302 THR A N   1 
ATOM   2341 C  CA  . THR A 1 302 ? 41.65200  26.89000  24.27600 1.000 17.46000 ? 302 THR A CA  1 
ATOM   2342 C  C   . THR A 1 302 ? 40.34900  26.12400  24.11100 1.000 17.73000 ? 302 THR A C   1 
ATOM   2343 O  O   . THR A 1 302 ? 39.79300  26.05700  23.00500 1.000 14.28000 ? 302 THR A O   1 
ATOM   2344 C  CB  . THR A 1 302 ? 41.37600  28.22700  24.97200 1.000 20.71000 ? 302 THR A CB  1 
ATOM   2345 O  OG1 . THR A 1 302 ? 40.30500  28.90800  24.30100 1.000 15.43000 ? 302 THR A OG1 1 
ATOM   2346 C  CG2 . THR A 1 302 ? 42.62200  29.11100  24.96200 1.000 21.38000 ? 302 THR A CG2 1 
ATOM   2347 N  N   . PRO A 1 303 ? 39.84100  25.50700  25.18300 1.000 14.09000 ? 303 PRO A N   1 
ATOM   2348 C  CA  . PRO A 1 303 ? 38.48600  24.94100  25.10800 1.000 13.10000 ? 303 PRO A CA  1 
ATOM   2349 C  C   . PRO A 1 303 ? 37.46100  25.94600  24.61500 1.000 13.99000 ? 303 PRO A C   1 
ATOM   2350 O  O   . PRO A 1 303 ? 36.61900  25.59600  23.77800 1.000 14.94000 ? 303 PRO A O   1 
ATOM   2351 C  CB  . PRO A 1 303 ? 38.22500  24.48600  26.55400 1.000 12.83000 ? 303 PRO A CB  1 
ATOM   2352 C  CG  . PRO A 1 303 ? 39.60000  24.06400  27.03900 1.000 13.63000 ? 303 PRO A CG  1 
ATOM   2353 C  CD  . PRO A 1 303 ? 40.56000  25.07600  26.39800 1.000 14.08000 ? 303 PRO A CD  1 
ATOM   2354 N  N   . THR A 1 304 ? 37.53200  27.20400  25.06600 1.000 13.30000 ? 304 THR A N   1 
ATOM   2355 C  CA  . THR A 1 304 ? 36.57100  28.18600  24.57900 1.000 13.85000 ? 304 THR A CA  1 
ATOM   2356 C  C   . THR A 1 304 ? 36.72700  28.41900  23.07600 1.000 15.59000 ? 304 THR A C   1 
ATOM   2357 O  O   . THR A 1 304 ? 35.72700  28.55500  22.36200 1.000 13.12000 ? 304 THR A O   1 
ATOM   2358 C  CB  . THR A 1 304 ? 36.69500  29.49300  25.36900 1.000 16.24000 ? 304 THR A CB  1 
ATOM   2359 O  OG1 . THR A 1 304 ? 36.23200  29.27000  26.70400 1.000 15.44000 ? 304 THR A OG1 1 
ATOM   2360 C  CG2 . THR A 1 304 ? 35.82100  30.58100  24.75200 1.000 14.71000 ? 304 THR A CG2 1 
ATOM   2361 N  N   . ASP A 1 305 ? 37.96800  28.44300  22.56900 1.000 15.57000 ? 305 ASP A N   1 
ATOM   2362 C  CA  . ASP A 1 305 ? 38.17000  28.53500  21.12300 1.000 14.54000 ? 305 ASP A CA  1 
ATOM   2363 C  C   . ASP A 1 305 ? 37.48600  27.38600  20.39800 1.000 15.28000 ? 305 ASP A C   1 
ATOM   2364 O  O   . ASP A 1 305 ? 36.86100  27.58200  19.34700 1.000 13.17000 ? 305 ASP A O   1 
ATOM   2365 C  CB  . ASP A 1 305 ? 39.66800  28.51900  20.77200 1.000 14.27000 ? 305 ASP A CB  1 
ATOM   2366 C  CG  . ASP A 1 305 ? 40.39400  29.78900  21.18200 1.000 19.94000 ? 305 ASP A CG  1 
ATOM   2367 O  OD1 . ASP A 1 305 ? 39.76200  30.84800  21.35700 1.000 17.37000 ? 305 ASP A OD1 1 
ATOM   2368 O  OD2 . ASP A 1 305 ? 41.62300  29.71100  21.35100 1.000 21.37000 ? 305 ASP A OD2 1 
ATOM   2369 N  N   . VAL A 1 306 ? 37.62200  26.16900  20.92400 1.000 12.23000 ? 306 VAL A N   1 
ATOM   2370 C  CA  . VAL A 1 306 ? 37.01500  25.02300  20.26000 1.000 13.11000 ? 306 VAL A CA  1 
ATOM   2371 C  C   . VAL A 1 306 ? 35.50000  25.06100  20.42400 1.000 15.45000 ? 306 VAL A C   1 
ATOM   2372 O  O   . VAL A 1 306 ? 34.75700  24.71200  19.49600 1.000 14.06000 ? 306 VAL A O   1 
ATOM   2373 C  CB  . VAL A 1 306 ? 37.62400  23.71000  20.78000 1.000 13.99000 ? 306 VAL A CB  1 
ATOM   2374 C  CG1 . VAL A 1 306 ? 36.78800  22.51400  20.34900 1.000 14.45000 ? 306 VAL A CG1 1 
ATOM   2375 C  CG2 . VAL A 1 306 ? 39.04700  23.55900  20.25100 1.000 13.69000 ? 306 VAL A CG2 1 
ATOM   2376 N  N   . TRP A 1 307 ? 35.01000  25.50500  21.58500 1.000 12.83000 ? 307 TRP A N   1 
ATOM   2377 C  CA  . TRP A 1 307 ? 33.57100  25.73400  21.69300 1.000 13.26000 ? 307 TRP A CA  1 
ATOM   2378 C  C   . TRP A 1 307 ? 33.09700  26.63400  20.55400 1.000 13.94000 ? 307 TRP A C   1 
ATOM   2379 O  O   . TRP A 1 307 ? 32.15100  26.31300  19.83000 1.000 12.28000 ? 307 TRP A O   1 
ATOM   2380 C  CB  . TRP A 1 307 ? 33.21000  26.35200  23.05000 1.000 11.87000 ? 307 TRP A CB  1 
ATOM   2381 C  CG  . TRP A 1 307 ? 31.73300  26.64100  23.11300 1.000 12.89000 ? 307 TRP A CG  1 
ATOM   2382 C  CD1 . TRP A 1 307 ? 31.13100  27.86100  22.94300 1.000 12.43000 ? 307 TRP A CD1 1 
ATOM   2383 C  CD2 . TRP A 1 307 ? 30.67200  25.69000  23.28600 1.000 13.22000 ? 307 TRP A CD2 1 
ATOM   2384 N  NE1 . TRP A 1 307 ? 29.76100  27.72300  23.02100 1.000 12.64000 ? 307 TRP A NE1 1 
ATOM   2385 C  CE2 . TRP A 1 307 ? 29.45600  26.40400  23.23400 1.000 11.82000 ? 307 TRP A CE2 1 
ATOM   2386 C  CE3 . TRP A 1 307 ? 30.63100  24.31100  23.51300 1.000 14.88000 ? 307 TRP A CE3 1 
ATOM   2387 C  CZ2 . TRP A 1 307 ? 28.21300  25.78000  23.38000 1.000 13.67000 ? 307 TRP A CZ2 1 
ATOM   2388 C  CZ3 . TRP A 1 307 ? 29.38600  23.69100  23.64500 1.000 10.82000 ? 307 TRP A CZ3 1 
ATOM   2389 C  CH2 . TRP A 1 307 ? 28.20100  24.42900  23.58700 1.000 14.70000 ? 307 TRP A CH2 1 
ATOM   2390 N  N   . ARG A 1 308 ? 33.80400  27.73200  20.32700 1.000 15.30000 ? 308 ARG A N   1 
ATOM   2391 C  CA  . ARG A 1 308 ? 33.30700  28.71200  19.37900 1.000 16.02000 ? 308 ARG A CA  1 
ATOM   2392 C  C   . ARG A 1 308 ? 33.42600  28.23500  17.93900 1.000 16.42000 ? 308 ARG A C   1 
ATOM   2393 O  O   . ARG A 1 308 ? 32.59100  28.60100  17.10200 1.000 17.57000 ? 308 ARG A O   1 
ATOM   2394 C  CB  . ARG A 1 308 ? 34.02700  30.03400  19.60700 1.000 13.77000 ? 308 ARG A CB  1 
ATOM   2395 C  CG  . ARG A 1 308 ? 33.52400  30.67000  20.90200 1.000 14.85000 ? 308 ARG A CG  1 
ATOM   2396 C  CD  . ARG A 1 308 ? 34.27700  31.93200  21.26700 1.000 14.31000 ? 308 ARG A CD  1 
ATOM   2397 N  NE  . ARG A 1 308 ? 33.77900  32.51600  22.51000 1.000 13.99000 ? 308 ARG A NE  1 
ATOM   2398 C  CZ  . ARG A 1 308 ? 34.32900  33.57400  23.09800 1.000 23.11000 ? 308 ARG A CZ  1 
ATOM   2399 N  NH1 . ARG A 1 308 ? 35.39000  34.16000  22.55800 1.000 21.83000 ? 308 ARG A NH1 1 
ATOM   2400 N  NH2 . ARG A 1 308 ? 33.82600  34.04500  24.22000 1.000 17.75000 ? 308 ARG A NH2 1 
ATOM   2401 N  N   . LYS A 1 309 ? 34.41200  27.39900  17.63200 1.000 14.12000 ? 309 LYS A N   1 
ATOM   2402 C  CA  . LYS A 1 309 ? 34.54000  26.93000  16.25600 1.000 16.86000 ? 309 LYS A CA  1 
ATOM   2403 C  C   . LYS A 1 309 ? 33.68000  25.70000  15.97000 1.000 18.88000 ? 309 LYS A C   1 
ATOM   2404 O  O   . LYS A 1 309 ? 33.11300  25.58800  14.87700 1.000 17.40000 ? 309 LYS A O   1 
ATOM   2405 C  CB  . LYS A 1 309 ? 36.00300  26.61700  15.93100 1.000 18.19000 ? 309 LYS A CB  1 
ATOM   2406 C  CG  . LYS A 1 309 ? 36.21100  26.12500  14.49600 1.000 14.64000 ? 309 LYS A CG  1 
ATOM   2407 C  CD  . LYS A 1 309 ? 37.66600  25.89200  14.20200 1.000 21.84000 ? 309 LYS A CD  1 
ATOM   2408 C  CE  . LYS A 1 309 ? 37.85100  25.24100  12.82600 1.000 23.15000 ? 309 LYS A CE  1 
ATOM   2409 N  NZ  . LYS A 1 309 ? 39.28900  25.00700  12.59700 1.000 23.75000 ? 309 LYS A NZ  1 
ATOM   2410 N  N   . ASN A 1 310 ? 33.54100  24.78700  16.93800 1.000 14.13000 ? 310 ASN A N   1 
ATOM   2411 C  CA  . ASN A 1 310 ? 33.05400  23.44500  16.65300 1.000 13.21000 ? 310 ASN A CA  1 
ATOM   2412 C  C   . ASN A 1 310 ? 31.70900  23.07600  17.27600 1.000 14.46000 ? 310 ASN A C   1 
ATOM   2413 O  O   . ASN A 1 310 ? 31.15900  22.02500  16.91300 1.000 12.49000 ? 310 ASN A O   1 
ATOM   2414 C  CB  . ASN A 1 310 ? 34.09800  22.41700  17.10400 1.000 12.79000 ? 310 ASN A CB  1 
ATOM   2415 C  CG  . ASN A 1 310 ? 35.43000  22.61400  16.41900 1.000 14.54000 ? 310 ASN A CG  1 
ATOM   2416 O  OD1 . ASN A 1 310 ? 36.33200  23.26200  16.95600 1.000 13.06000 ? 310 ASN A OD1 1 
ATOM   2417 N  ND2 . ASN A 1 310 ? 35.56000  22.05800  15.21300 1.000 14.22000 ? 310 ASN A ND2 1 
ATOM   2418 N  N   . PHE A 1 311 ? 31.16300  23.88700  18.18400 1.000 13.61000 ? 311 PHE A N   1 
ATOM   2419 C  CA  . PHE A 1 311 ? 29.99800  23.49800  18.96300 1.000 15.64000 ? 311 PHE A CA  1 
ATOM   2420 C  C   . PHE A 1 311 ? 28.83100  24.46300  18.77500 1.000 13.58000 ? 311 PHE A C   1 
ATOM   2421 O  O   . PHE A 1 311 ? 29.00200  25.64700  18.46800 1.000 12.21000 ? 311 PHE A O   1 
ATOM   2422 C  CB  . PHE A 1 311 ? 30.32300  23.44800  20.45100 1.000 12.43000 ? 311 PHE A CB  1 
ATOM   2423 C  CG  . PHE A 1 311 ? 30.94600  22.16600  20.91600 1.000 13.57000 ? 311 PHE A CG  1 
ATOM   2424 C  CD1 . PHE A 1 311 ? 32.32500  21.99800  20.88400 1.000 13.54000 ? 311 PHE A CD1 1 
ATOM   2425 C  CD2 . PHE A 1 311 ? 30.16200  21.15100  21.45000 1.000 11.41000 ? 311 PHE A CD2 1 
ATOM   2426 C  CE1 . PHE A 1 311 ? 32.91300  20.82100  21.33300 1.000 11.93000 ? 311 PHE A CE1 1 
ATOM   2427 C  CE2 . PHE A 1 311 ? 30.74100  19.97000  21.90000 1.000 14.85000 ? 311 PHE A CE2 1 
ATOM   2428 C  CZ  . PHE A 1 311 ? 32.12200  19.80500  21.84900 1.000 14.18000 ? 311 PHE A CZ  1 
ATOM   2429 N  N   . LEU A 1 312 ? 27.63000  23.94100  19.01300 1.000 11.44000 ? 312 LEU A N   1 
ATOM   2430 C  CA  . LEU A 1 312 ? 26.41800  24.74800  19.03300 1.000 12.46000 ? 312 LEU A CA  1 
ATOM   2431 C  C   . LEU A 1 312 ? 25.58900  24.30800  20.23000 1.000 12.29000 ? 312 LEU A C   1 
ATOM   2432 O  O   . LEU A 1 312 ? 25.30300  23.11800  20.37800 1.000 14.30000 ? 312 LEU A O   1 
ATOM   2433 C  CB  . LEU A 1 312 ? 25.62900  24.58500  17.73000 1.000 11.69000 ? 312 LEU A CB  1 
ATOM   2434 C  CG  . LEU A 1 312 ? 24.46600  25.55200  17.50000 1.000 17.98000 ? 312 LEU A CG  1 
ATOM   2435 C  CD1 . LEU A 1 312 ? 25.01200  26.97700  17.28600 1.000 14.96000 ? 312 LEU A CD1 1 
ATOM   2436 C  CD2 . LEU A 1 312 ? 23.59800  25.08900  16.31800 1.000 12.83000 ? 312 LEU A CD2 1 
ATOM   2437 N  N   . ALA A 1 313 ? 25.25600  25.25000  21.11000 1.000 11.07000 ? 313 ALA A N   1 
ATOM   2438 C  CA  . ALA A 1 313 ? 24.32200  24.98600  22.19900 1.000 13.19000 ? 313 ALA A CA  1 
ATOM   2439 C  C   . ALA A 1 313 ? 22.90700  25.24500  21.69900 1.000 12.64000 ? 313 ALA A C   1 
ATOM   2440 O  O   . ALA A 1 313 ? 22.67400  26.18900  20.94500 1.000 14.67000 ? 313 ALA A O   1 
ATOM   2441 C  CB  . ALA A 1 313 ? 24.62400  25.87000  23.41100 1.000 13.97000 ? 313 ALA A CB  1 
ATOM   2442 N  N   . CYS A 1 314 ? 21.96300  24.39800  22.12100 1.000 12.86000 ? 314 CYS A N   1 
ATOM   2443 C  CA  . CYS A 1 314 ? 20.61500  24.37600  21.56700 1.000 14.92000 ? 314 CYS A CA  1 
ATOM   2444 C  C   . CYS A 1 314 ? 19.60200  24.41400  22.70000 1.000 13.20000 ? 314 CYS A C   1 
ATOM   2445 O  O   . CYS A 1 314 ? 19.67900  23.58300  23.60600 1.000 14.19000 ? 314 CYS A O   1 
ATOM   2446 C  CB  . CYS A 1 314 ? 20.41200  23.10400  20.71700 1.000 12.33000 ? 314 CYS A CB  1 
ATOM   2447 S  SG  . CYS A 1 314 ? 21.71200  22.85000  19.46600 1.000 15.38000 ? 314 CYS A SG  1 
ATOM   2448 N  N   . TYR A 1 315 ? 18.64300  25.35100  22.65100 1.000 12.90000 ? 315 TYR A N   1 
ATOM   2449 C  CA  . TYR A 1 315 ? 17.68700  25.44900  23.74600 1.000 15.72000 ? 315 TYR A CA  1 
ATOM   2450 C  C   . TYR A 1 315 ? 16.32700  25.95000  23.28700 1.000 12.60000 ? 315 TYR A C   1 
ATOM   2451 O  O   . TYR A 1 315 ? 16.19500  26.64100  22.27700 1.000 14.79000 ? 315 TYR A O   1 
ATOM   2452 C  CB  . TYR A 1 315 ? 18.19300  26.36300  24.86000 1.000 13.70000 ? 315 TYR A CB  1 
ATOM   2453 C  CG  . TYR A 1 315 ? 18.00100  27.84100  24.63400 1.000 16.21000 ? 315 TYR A CG  1 
ATOM   2454 C  CD1 . TYR A 1 315 ? 18.70300  28.51700  23.64100 1.000 15.63000 ? 315 TYR A CD1 1 
ATOM   2455 C  CD2 . TYR A 1 315 ? 17.14700  28.57600  25.44800 1.000 18.56000 ? 315 TYR A CD2 1 
ATOM   2456 C  CE1 . TYR A 1 315 ? 18.54300  29.88900  23.46000 1.000 15.45000 ? 315 TYR A CE1 1 
ATOM   2457 C  CE2 . TYR A 1 315 ? 16.98100  29.94200  25.27100 1.000 20.19000 ? 315 TYR A CE2 1 
ATOM   2458 C  CZ  . TYR A 1 315 ? 17.67900  30.58900  24.28400 1.000 20.26000 ? 315 TYR A CZ  1 
ATOM   2459 O  OH  . TYR A 1 315 ? 17.52400  31.94500  24.11800 1.000 17.59000 ? 315 TYR A OH  1 
ATOM   2460 N  N   . ILE A 1 316 ? 15.31400  25.60600  24.08000 1.000 13.29000 ? 316 ILE A N   1 
ATOM   2461 C  CA  . ILE A 1 316 ? 13.92400  25.97200  23.82700 1.000 11.72000 ? 316 ILE A CA  1 
ATOM   2462 C  C   . ILE A 1 316 ? 13.58500  27.24500  24.58500 1.000 14.99000 ? 316 ILE A C   1 
ATOM   2463 O  O   . ILE A 1 316 ? 13.13800  28.25000  24.00900 1.000 14.59000 ? 316 ILE A O   1 
ATOM   2464 C  CB  . ILE A 1 316 ? 12.98300  24.83800  24.27600 1.000 12.13000 ? 316 ILE A CB  1 
ATOM   2465 C  CG1 . ILE A 1 316 ? 13.41900  23.49400  23.69700 1.000 14.22000 ? 316 ILE A CG1 1 
ATOM   2466 C  CG2 . ILE A 1 316 ? 11.53800  25.16000  23.90100 1.000 15.88000 ? 316 ILE A CG2 1 
ATOM   2467 C  CD1 . ILE A 1 316 ? 12.80500  22.30900  24.45400 1.000 16.23000 ? 316 ILE A CD1 1 
ATOM   2468 N  N   . THR A 1 317 ? 13.74100  27.17100  25.90300 1.000 14.36000 ? 317 THR A N   1 
ATOM   2469 C  CA  . THR A 1 317 ? 13.42500  28.26100  26.80700 1.000 12.99000 ? 317 THR A CA  1 
ATOM   2470 C  C   . THR A 1 317 ? 14.39100  28.16000  27.97700 1.000 14.88000 ? 317 THR A C   1 
ATOM   2471 O  O   . THR A 1 317 ? 14.56400  27.08600  28.56100 1.000 15.00000 ? 317 THR A O   1 
ATOM   2472 C  CB  . THR A 1 317 ? 11.95800  28.20400  27.27800 1.000 18.16000 ? 317 THR A CB  1 
ATOM   2473 O  OG1 . THR A 1 317 ? 11.74700  29.17500  28.30500 1.000 16.29000 ? 317 THR A OG1 1 
ATOM   2474 C  CG2 . THR A 1 317 ? 11.60600  26.83400  27.83500 1.000 17.45000 ? 317 THR A CG2 1 
ATOM   2475 N  N   . GLU A 1 318 ? 15.02600  29.26700  28.29600 1.000 12.68000 ? 318 GLU A N   1 
ATOM   2476 C  CA  . GLU A 1 318 ? 15.95900  29.32800  29.41100 1.000 13.72000 ? 318 GLU A CA  1 
ATOM   2477 C  C   . GLU A 1 318 ? 16.24800  30.79200  29.70000 1.000 15.66000 ? 318 GLU A C   1 
ATOM   2478 O  O   . GLU A 1 318 ? 17.26700  31.32400  29.23900 1.000 17.28000 ? 318 GLU A O   1 
ATOM   2479 C  CB  . GLU A 1 318 ? 17.25600  28.56600  29.09600 1.000 15.51000 ? 318 GLU A CB  1 
ATOM   2480 C  CG  . GLU A 1 318 ? 18.10300  28.25000  30.33500 1.000 15.67000 ? 318 GLU A CG  1 
ATOM   2481 C  CD  . GLU A 1 318 ? 19.38900  27.48000  30.01300 1.000 15.07000 ? 318 GLU A CD  1 
ATOM   2482 O  OE1 . GLU A 1 318 ? 19.33000  26.49900  29.24500 1.000 14.74000 ? 318 GLU A OE1 1 
ATOM   2483 O  OE2 . GLU A 1 318 ? 20.45000  27.86300  30.54200 1.000 17.75000 ? 318 GLU A OE2 1 
ATOM   2484 N  N   . PRO A 1 319 ? 15.36500  31.46900  30.44100 1.000 16.38000 ? 319 PRO A N   1 
ATOM   2485 C  CA  . PRO A 1 319 ? 15.48200  32.93100  30.58400 1.000 16.92000 ? 319 PRO A CA  1 
ATOM   2486 C  C   . PRO A 1 319 ? 16.84100  33.39500  31.07200 1.000 19.93000 ? 319 PRO A C   1 
ATOM   2487 O  O   . PRO A 1 319 ? 17.34000  34.41600  30.58100 1.000 23.85000 ? 319 PRO A O   1 
ATOM   2488 C  CB  . PRO A 1 319 ? 14.37000  33.26900  31.58300 1.000 19.84000 ? 319 PRO A CB  1 
ATOM   2489 C  CG  . PRO A 1 319 ? 13.36700  32.17000  31.42000 1.000 19.27000 ? 319 PRO A CG  1 
ATOM   2490 C  CD  . PRO A 1 319 ? 14.17400  30.93000  31.12200 1.000 14.43000 ? 319 PRO A CD  1 
ATOM   2491 N  N   . SER A 1 320 ? 17.48000  32.66900  31.99800 1.000 16.06000 ? 320 SER A N   1 
ATOM   2492 C  CA  . SER A 1 320 ? 18.77900  33.11400  32.50100 1.000 15.35000 ? 320 SER A CA  1 
ATOM   2493 C  C   . SER A 1 320 ? 19.94700  32.68600  31.62400 1.000 17.96000 ? 320 SER A C   1 
ATOM   2494 O  O   . SER A 1 320 ? 21.07300  33.14000  31.86100 1.000 16.67000 ? 320 SER A O   1 
ATOM   2495 C  CB  . SER A 1 320 ? 19.01600  32.58300  33.91600 1.000 19.16000 ? 320 SER A CB  1 
ATOM   2496 O  OG  . SER A 1 320 ? 19.20100  31.17500  33.88200 1.000 15.64000 ? 320 SER A OG  1 
ATOM   2497 N  N   . GLY A 1 321 ? 19.71600  31.82700  30.62800 1.000 15.02000 ? 321 GLY A N   1 
ATOM   2498 C  CA  . GLY A 1 321 ? 20.81800  31.30000  29.84800 1.000 15.45000 ? 321 GLY A CA  1 
ATOM   2499 C  C   . GLY A 1 321 ? 21.57500  32.36900  29.08900 1.000 18.77000 ? 321 GLY A C   1 
ATOM   2500 O  O   . GLY A 1 321 ? 22.79400  32.28100  28.93500 1.000 17.61000 ? 321 GLY A O   1 
ATOM   2501 N  N   . LEU A 1 322 ? 20.87900  33.40500  28.63000 1.000 15.05000 ? 322 LEU A N   1 
ATOM   2502 C  CA  . LEU A 1 322 ? 21.54300  34.38700  27.78600 1.000 18.79000 ? 322 LEU A CA  1 
ATOM   2503 C  C   . LEU A 1 322 ? 22.42000  35.34300  28.57900 1.000 15.52000 ? 322 LEU A C   1 
ATOM   2504 O  O   . LEU A 1 322 ? 23.10300  36.17600  27.97600 1.000 16.49000 ? 322 LEU A O   1 
ATOM   2505 C  CB  . LEU A 1 322 ? 20.50100  35.15500  26.95800 1.000 17.66000 ? 322 LEU A CB  1 
ATOM   2506 C  CG  . LEU A 1 322 ? 19.83700  34.24700  25.90800 1.000 17.04000 ? 322 LEU A CG  1 
ATOM   2507 C  CD1 . LEU A 1 322 ? 18.88000  35.01200  25.02500 1.000 21.02000 ? 322 LEU A CD1 1 
ATOM   2508 C  CD2 . LEU A 1 322 ? 20.85000  33.48600  25.05200 1.000 18.02000 ? 322 LEU A CD2 1 
ATOM   2509 N  N   . ASN A 1 323 ? 22.45000  35.22100  29.90900 1.000 19.10000 ? 323 ASN A N   1 
ATOM   2510 C  CA  . ASN A 1 323 ? 23.31500  36.05800  30.72700 1.000 17.67000 ? 323 ASN A CA  1 
ATOM   2511 C  C   . ASN A 1 323 ? 24.77400  35.64800  30.64300 1.000 18.15000 ? 323 ASN A C   1 
ATOM   2512 O  O   . ASN A 1 323 ? 25.63100  36.36600  31.16300 1.000 20.30000 ? 323 ASN A O   1 
ATOM   2513 C  CB  . ASN A 1 323 ? 22.84500  36.03300  32.18200 1.000 20.04000 ? 323 ASN A CB  1 
ATOM   2514 C  CG  . ASN A 1 323 ? 21.51400  36.71400  32.36200 1.000 21.72000 ? 323 ASN A CG  1 
ATOM   2515 O  OD1 . ASN A 1 323 ? 21.16100  37.60300  31.59500 1.000 21.57000 ? 323 ASN A OD1 1 
ATOM   2516 N  ND2 . ASN A 1 323 ? 20.76200  36.29700  33.36900 1.000 22.98000 ? 323 ASN A ND2 1 
ATOM   2517 N  N   . ASN A 1 324 ? 25.08300  34.51800  30.01100 1.000 16.94000 ? 324 ASN A N   1 
ATOM   2518 C  CA  . ASN A 1 324 ? 26.46700  34.16200  29.73000 1.000 18.27000 ? 324 ASN A CA  1 
ATOM   2519 C  C   . ASN A 1 324 ? 26.73400  34.03700  28.23600 1.000 16.81000 ? 324 ASN A C   1 
ATOM   2520 O  O   . ASN A 1 324 ? 27.74000  33.44300  27.84200 1.000 15.40000 ? 324 ASN A O   1 
ATOM   2521 C  CB  . ASN A 1 324 ? 26.85000  32.86900  30.45100 1.000 23.83000 ? 324 ASN A CB  1 
ATOM   2522 C  CG  . ASN A 1 324 ? 27.69600  33.13100  31.68800 1.000 18.46000 ? 324 ASN A CG  1 
ATOM   2523 O  OD1 . ASN A 1 324 ? 28.54900  34.02400  31.69800 1.000 26.13000 ? 324 ASN A OD1 1 
ATOM   2524 N  ND2 . ASN A 1 324 ? 27.44000  32.38100  32.74000 1.000 24.22000 ? 324 ASN A ND2 1 
ATOM   2525 N  N   . ARG A 1 325 ? 25.86100  34.59700  27.39700 1.000 17.89000 ? 325 ARG A N   1 
ATOM   2526 C  CA  . ARG A 1 325 ? 26.05900  34.48700  25.95600 1.000 15.16000 ? 325 ARG A CA  1 
ATOM   2527 C  C   . ARG A 1 325 ? 27.38700  35.10100  25.51200 1.000 18.32000 ? 325 ARG A C   1 
ATOM   2528 O  O   . ARG A 1 325 ? 27.99300  34.62200  24.55000 1.000 16.77000 ? 325 ARG A O   1 
ATOM   2529 C  CB  . ARG A 1 325 ? 24.89300  35.12500  25.20900 1.000 14.95000 ? 325 ARG A CB  1 
ATOM   2530 C  CG  . ARG A 1 325 ? 24.76900  36.63900  25.35000 1.000 16.07000 ? 325 ARG A CG  1 
ATOM   2531 C  CD  . ARG A 1 325 ? 23.51200  37.05800  24.65600 1.000 18.40000 ? 325 ARG A CD  1 
ATOM   2532 N  NE  . ARG A 1 325 ? 23.31900  38.50200  24.53500 1.000 18.43000 ? 325 ARG A NE  1 
ATOM   2533 C  CZ  . ARG A 1 325 ? 22.75900  39.26700  25.46400 1.000 21.13000 ? 325 ARG A CZ  1 
ATOM   2534 N  NH1 . ARG A 1 325 ? 22.37200  38.74400  26.62300 1.000 16.48000 ? 325 ARG A NH1 1 
ATOM   2535 N  NH2 . ARG A 1 325 ? 22.60000  40.56500  25.23300 1.000 17.16000 ? 325 ARG A NH2 1 
ATOM   2536 N  N   . HIS A 1 326 ? 27.87900  36.12600  26.20900 1.000 17.88000 ? 326 HIS A N   1 
ATOM   2537 C  CA  . HIS A 1 326 ? 29.15200  36.71100  25.79200 1.000 19.29000 ? 326 HIS A CA  1 
ATOM   2538 C  C   . HIS A 1 326 ? 30.33100  35.83500  26.19000 1.000 21.58000 ? 326 HIS A C   1 
ATOM   2539 O  O   . HIS A 1 326 ? 31.34200  35.79500  25.48400 1.000 18.63000 ? 326 HIS A O   1 
ATOM   2540 C  CB  . HIS A 1 326 ? 29.27400  38.11900  26.36100 1.000 23.38000 ? 326 HIS A CB  1 
ATOM   2541 C  CG  . HIS A 1 326 ? 28.09100  38.97600  26.02900 1.000 26.20000 ? 326 HIS A CG  1 
ATOM   2542 N  ND1 . HIS A 1 326 ? 27.20200  39.42900  26.98200 1.000 30.16000 ? 326 HIS A ND1 1 
ATOM   2543 C  CD2 . HIS A 1 326 ? 27.61500  39.41000  24.83500 1.000 26.07000 ? 326 HIS A CD2 1 
ATOM   2544 C  CE1 . HIS A 1 326 ? 26.24900  40.13400  26.39500 1.000 23.29000 ? 326 HIS A CE1 1 
ATOM   2545 N  NE2 . HIS A 1 326 ? 26.47700  40.14000  25.09300 1.000 28.32000 ? 326 HIS A NE2 1 
ATOM   2546 N  N   . ARG A 1 327 ? 30.32800  35.14300  27.26300 1.000 19.10000 ? 327 ARG A N   1 
ATOM   2547 C  CA  . ARG A 1 327 ? 31.20700  34.04700  27.65300 1.000 21.38000 ? 327 ARG A CA  1 
ATOM   2548 C  C   . ARG A 1 327 ? 31.24200  32.96100  26.57800 1.000 20.34000 ? 327 ARG A C   1 
ATOM   2549 O  O   . ARG A 1 327 ? 32.29500  32.36100  26.32300 1.000 20.76000 ? 327 ARG A O   1 
ATOM   2550 C  CB  . ARG A 1 327 ? 30.75100  33.49500  28.99800 1.000 25.18000 ? 327 ARG A CB  1 
ATOM   2551 C  CG  . ARG A 1 327 ? 31.55000  32.30100  29.47100 1.000 26.14000 ? 327 ARG A CG  1 
ATOM   2552 C  CD  . ARG A 1 327 ? 32.99300  32.69300  29.72000 1.000 30.10000 ? 327 ARG A CD  1 
ATOM   2553 N  NE  . ARG A 1 327 ? 33.74900  31.53000  30.17600 1.000 29.99000 ? 327 ARG A NE  1 
ATOM   2554 C  CZ  . ARG A 1 327 ? 34.31600  30.65000  29.37000 1.000 20.63000 ? 327 ARG A CZ  1 
ATOM   2555 N  NH1 . ARG A 1 327 ? 34.20800  30.78900  28.05300 1.000 17.14000 ? 327 ARG A NH1 1 
ATOM   2556 N  NH2 . ARG A 1 327 ? 34.98900  29.62800  29.88600 1.000 18.37000 ? 327 ARG A NH2 1 
ATOM   2557 N  N   . LEU A 1 328 ? 30.17200  32.48600  26.28700 1.000 17.37000 ? 328 LEU A N   1 
ATOM   2558 C  CA  . LEU A 1 328 ? 30.14600  31.41600  25.28600 1.000 15.57000 ? 328 LEU A CA  1 
ATOM   2559 C  C   . LEU A 1 328 ? 30.55300  31.94000  23.91600 1.000 19.88000 ? 328 LEU A C   1 
ATOM   2560 O  O   . LEU A 1 328 ? 31.27900  31.26900  23.17100 1.000 15.29000 ? 328 LEU A O   1 
ATOM   2561 C  CB  . LEU A 1 328 ? 28.74800  30.80000  25.20300 1.000 16.00000 ? 328 LEU A CB  1 
ATOM   2562 C  CG  . LEU A 1 328 ? 28.38000  29.62800  26.11200 1.000 17.30000 ? 328 LEU A CG  1 
ATOM   2563 C  CD1 . LEU A 1 328 ? 28.64600  29.94200  27.59000 1.000 15.79000 ? 328 LEU A CD1 1 
ATOM   2564 C  CD2 . LEU A 1 328 ? 26.93400  29.19900  25.91900 1.000 16.48000 ? 328 LEU A CD2 1 
ATOM   2565 N  N   . GLY A 1 329 ? 30.10600  33.14700  23.58100 1.000 17.02000 ? 329 GLY A N   1 
ATOM   2566 C  CA  . GLY A 1 329 ? 30.10800  33.62100  22.21400 1.000 17.53000 ? 329 GLY A CA  1 
ATOM   2567 C  C   . GLY A 1 329 ? 28.69200  33.51400  21.69400 1.000 15.48000 ? 329 GLY A C   1 
ATOM   2568 O  O   . GLY A 1 329 ? 28.16000  32.40400  21.61200 1.000 14.11000 ? 329 GLY A O   1 
ATOM   2569 N  N   . VAL A 1 330 ? 28.05400  34.64400  21.36700 1.000 14.52000 ? 330 VAL A N   1 
ATOM   2570 C  CA  . VAL A 1 330 ? 26.64500  34.62300  20.98100 1.000 16.84000 ? 330 VAL A CA  1 
ATOM   2571 C  C   . VAL A 1 330 ? 26.41400  33.84100  19.68700 1.000 17.09000 ? 330 VAL A C   1 
ATOM   2572 O  O   . VAL A 1 330 ? 25.29900  33.35100  19.45100 1.000 17.55000 ? 330 VAL A O   1 
ATOM   2573 C  CB  . VAL A 1 330 ? 26.09800  36.06900  20.88600 1.000 18.57000 ? 330 VAL A CB  1 
ATOM   2574 C  CG1 . VAL A 1 330 ? 26.57800  36.73300  19.62100 1.000 20.65000 ? 330 VAL A CG1 1 
ATOM   2575 C  CG2 . VAL A 1 330 ? 24.56200  36.08000  20.96300 1.000 20.15000 ? 330 VAL A CG2 1 
ATOM   2576 N  N   . ASP A 1 331 ? 27.45400  33.67200  18.85900 1.000 15.82000 ? 331 ASP A N   1 
ATOM   2577 C  CA  . ASP A 1 331 ? 27.34400  32.88700  17.63200 1.000 15.64000 ? 331 ASP A CA  1 
ATOM   2578 C  C   . ASP A 1 331 ? 27.07900  31.40800  17.88500 1.000 16.76000 ? 331 ASP A C   1 
ATOM   2579 O  O   . ASP A 1 331 ? 26.76500  30.68900  16.93200 1.000 16.62000 ? 331 ASP A O   1 
ATOM   2580 C  CB  . ASP A 1 331 ? 28.62900  32.98100  16.79200 1.000 16.83000 ? 331 ASP A CB  1 
ATOM   2581 C  CG  . ASP A 1 331 ? 28.83800  34.34300  16.15400 1.000 24.36000 ? 331 ASP A CG  1 
ATOM   2582 O  OD1 . ASP A 1 331 ? 28.01600  35.25100  16.32400 1.000 20.87000 ? 331 ASP A OD1 1 
ATOM   2583 O  OD2 . ASP A 1 331 ? 29.84000  34.49000  15.44200 1.000 32.15000 ? 331 ASP A OD2 1 
ATOM   2584 N  N   . THR A 1 332 ? 27.21500  30.93000  19.12100 1.000 14.67000 ? 332 THR A N   1 
ATOM   2585 C  CA  . THR A 1 332 ? 27.16000  29.50200  19.40100 1.000 14.62000 ? 332 THR A CA  1 
ATOM   2586 C  C   . THR A 1 332 ? 25.86000  29.05700  20.04700 1.000 12.78000 ? 332 THR A C   1 
ATOM   2587 O  O   . THR A 1 332 ? 25.79800  27.93300  20.55000 1.000 14.32000 ? 332 THR A O   1 
ATOM   2588 C  CB  . THR A 1 332 ? 28.31800  29.10000  20.29800 1.000 13.87000 ? 332 THR A CB  1 
ATOM   2589 O  OG1 . THR A 1 332 ? 28.11800  29.67000  21.59700 1.000 12.70000 ? 332 THR A OG1 1 
ATOM   2590 C  CG2 . THR A 1 332 ? 29.63500  29.60300  19.69900 1.000 13.69000 ? 332 THR A CG2 1 
ATOM   2591 N  N   . ILE A 1 333 ? 24.82700  29.89500  20.04800 1.000 10.77000 ? 333 ILE A N   1 
ATOM   2592 C  CA  . ILE A 1 333 ? 23.55700  29.57500  20.70200 1.000 12.43000 ? 333 ILE A CA  1 
ATOM   2593 C  C   . ILE A 1 333 ? 22.44300  29.59600  19.65800 1.000 12.85000 ? 333 ILE A C   1 
ATOM   2594 O  O   . ILE A 1 333 ? 22.26200  30.59800  18.95300 1.000 13.36000 ? 333 ILE A O   1 
ATOM   2595 C  CB  . ILE A 1 333 ? 23.25900  30.54600  21.85600 1.000 12.04000 ? 333 ILE A CB  1 
ATOM   2596 C  CG1 . ILE A 1 333 ? 24.36900  30.46800  22.90200 1.000 14.02000 ? 333 ILE A CG1 1 
ATOM   2597 C  CG2 . ILE A 1 333 ? 21.88500  30.23900  22.48600 1.000 14.00000 ? 333 ILE A CG2 1 
ATOM   2598 C  CD1 . ILE A 1 333 ? 24.39200  31.63200  23.86800 1.000 14.38000 ? 333 ILE A CD1 1 
ATOM   2599 N  N   . ALA A 1 334 ? 21.70400  28.48900  19.54900 1.000 14.59000 ? 334 ALA A N   1 
ATOM   2600 C  CA  . ALA A 1 334 ? 20.63200  28.36600  18.56500 1.000 12.11000 ? 334 ALA A CA  1 
ATOM   2601 C  C   . ALA A 1 334 ? 19.34100  27.93200  19.24000 1.000 12.70000 ? 334 ALA A C   1 
ATOM   2602 O  O   . ALA A 1 334 ? 19.35600  27.14300  20.19300 1.000 13.15000 ? 334 ALA A O   1 
ATOM   2603 C  CB  . ALA A 1 334 ? 20.97900  27.37000  17.46900 1.000 10.75000 ? 334 ALA A CB  1 
ATOM   2604 N  N   . TRP A 1 335 ? 18.22300  28.43700  18.73300 1.000 12.48000 ? 335 TRP A N   1 
ATOM   2605 C  CA  . TRP A 1 335 ? 16.92400  28.12800  19.31300 1.000 12.65000 ? 335 TRP A CA  1 
ATOM   2606 C  C   . TRP A 1 335 ? 16.36300  26.84200  18.70600 1.000 15.55000 ? 335 TRP A C   1 
ATOM   2607 O  O   . TRP A 1 335 ? 16.76900  26.40900  17.62300 1.000 13.10000 ? 335 TRP A O   1 
ATOM   2608 C  CB  . TRP A 1 335 ? 15.95700  29.29400  19.10600 1.000 12.64000 ? 335 TRP A CB  1 
ATOM   2609 C  CG  . TRP A 1 335 ? 14.59300  29.01300  19.63500 1.000 13.94000 ? 335 TRP A CG  1 
ATOM   2610 C  CD1 . TRP A 1 335 ? 14.20800  29.01700  20.93800 1.000 14.86000 ? 335 TRP A CD1 1 
ATOM   2611 C  CD2 . TRP A 1 335 ? 13.44400  28.64600  18.87000 1.000 11.43000 ? 335 TRP A CD2 1 
ATOM   2612 N  NE1 . TRP A 1 335 ? 12.87700  28.67700  21.03500 1.000 14.70000 ? 335 TRP A NE1 1 
ATOM   2613 C  CE2 . TRP A 1 335 ? 12.38800  28.44300  19.77600 1.000 12.83000 ? 335 TRP A CE2 1 
ATOM   2614 C  CE3 . TRP A 1 335 ? 13.20800  28.45500  17.50000 1.000 12.30000 ? 335 TRP A CE3 1 
ATOM   2615 C  CZ2 . TRP A 1 335 ? 11.11000  28.07200  19.36100 1.000 16.38000 ? 335 TRP A CZ2 1 
ATOM   2616 C  CZ3 . TRP A 1 335 ? 11.93300  28.08500  17.08900 1.000 12.61000 ? 335 TRP A CZ3 1 
ATOM   2617 C  CH2 . TRP A 1 335 ? 10.90800  27.89700  18.00600 1.000 12.26000 ? 335 TRP A CH2 1 
ATOM   2618 N  N   . GLU A 1 336 ? 15.45200  26.20100  19.44800 1.000 11.93000 ? 336 GLU A N   1 
ATOM   2619 C  CA  . GLU A 1 336 ? 14.73000  25.04100  18.93700 1.000 13.05000 ? 336 GLU A CA  1 
ATOM   2620 C  C   . GLU A 1 336 ? 13.33000  25.03500  19.51700 1.000 12.94000 ? 336 GLU A C   1 
ATOM   2621 O  O   . GLU A 1 336 ? 13.09700  25.56400  20.60800 1.000 11.47000 ? 336 GLU A O   1 
ATOM   2622 C  CB  . GLU A 1 336 ? 15.43000  23.72600  19.28700 1.000 11.28000 ? 336 GLU A CB  1 
ATOM   2623 C  CG  . GLU A 1 336 ? 15.82500  23.66600  20.72900 1.000 11.54000 ? 336 GLU A CG  1 
ATOM   2624 C  CD  . GLU A 1 336 ? 16.24600  22.28400  21.11700 1.000 16.39000 ? 336 GLU A CD  1 
ATOM   2625 O  OE1 . GLU A 1 336 ? 15.36800  21.47800  21.48400 1.000 13.28000 ? 336 GLU A OE1 1 
ATOM   2626 O  OE2 . GLU A 1 336 ? 17.45500  21.99400  21.01100 1.000 16.46000 ? 336 GLU A OE2 1 
ATOM   2627 N  N   . CYS A 1 337 ? 12.40300  24.40300  18.78900 1.000 11.58000 ? 337 CYS A N   1 
ATOM   2628 C  CA  . CYS A 1 337 ? 11.01000  24.33600  19.21600 1.000 12.79000 ? 337 CYS A CA  1 
ATOM   2629 C  C   . CYS A 1 337 ? 10.68100  23.06100  19.98600 1.000 14.90000 ? 337 CYS A C   1 
ATOM   2630 O  O   . CYS A 1 337 ? 9.86500   23.09700  20.91200 1.000 13.07000 ? 337 CYS A O   1 
ATOM   2631 C  CB  . CYS A 1 337 ? 10.08900  24.43400  17.99700 1.000 14.79000 ? 337 CYS A CB  1 
ATOM   2632 S  SG  . CYS A 1 337 ? 8.32900   24.61500  18.41600 1.000 15.29000 ? 337 CYS A SG  1 
ATOM   2633 N  N   . ASP A 1 338 ? 11.29300  21.93800  19.59400 1.000 13.14000 ? 338 ASP A N   1 
ATOM   2634 C  CA  . ASP A 1 338 ? 11.07900  20.61200  20.17800 1.000 12.98000 ? 338 ASP A CA  1 
ATOM   2635 C  C   . ASP A 1 338 ? 9.64100   20.13000  20.01400 1.000 14.08000 ? 338 ASP A C   1 
ATOM   2636 O  O   . ASP A 1 338 ? 9.14200   19.34700  20.82000 1.000 14.94000 ? 338 ASP A O   1 
ATOM   2637 C  CB  . ASP A 1 338 ? 11.49800  20.55700  21.64300 1.000 10.37000 ? 338 ASP A CB  1 
ATOM   2638 C  CG  . ASP A 1 338 ? 11.96600  19.16500  22.06100 1.000 15.45000 ? 338 ASP A CG  1 
ATOM   2639 O  OD1 . ASP A 1 338 ? 12.59800  18.47200  21.22300 1.000 11.95000 ? 338 ASP A OD1 1 
ATOM   2640 O  OD2 . ASP A 1 338 ? 11.68200  18.76700  23.21600 1.000 15.05000 ? 338 ASP A OD2 1 
ATOM   2641 N  N   . TYR A 1 339 ? 8.98200   20.59200  18.96700 1.000 13.38000 ? 339 TYR A N   1 
ATOM   2642 C  CA  . TYR A 1 339 ? 7.66100   20.09100  18.62000 1.000 13.55000 ? 339 TYR A CA  1 
ATOM   2643 C  C   . TYR A 1 339 ? 7.74900   18.59700  18.30400 1.000 12.75000 ? 339 TYR A C   1 
ATOM   2644 O  O   . TYR A 1 339 ? 8.67500   18.16600  17.61100 1.000 13.81000 ? 339 TYR A O   1 
ATOM   2645 C  CB  . TYR A 1 339 ? 7.15100   20.88000  17.41100 1.000 14.65000 ? 339 TYR A CB  1 
ATOM   2646 C  CG  . TYR A 1 339 ? 5.75600   20.55100  16.93600 1.000 16.71000 ? 339 TYR A CG  1 
ATOM   2647 C  CD1 . TYR A 1 339 ? 5.48000   19.33500  16.32500 1.000 15.60000 ? 339 TYR A CD1 1 
ATOM   2648 C  CD2 . TYR A 1 339 ? 4.72300   21.47600  17.06600 1.000 15.62000 ? 339 TYR A CD2 1 
ATOM   2649 C  CE1 . TYR A 1 339 ? 4.20600   19.02700  15.87200 1.000 15.64000 ? 339 TYR A CE1 1 
ATOM   2650 C  CE2 . TYR A 1 339 ? 3.43700   21.17400  16.61800 1.000 14.43000 ? 339 TYR A CE2 1 
ATOM   2651 C  CZ  . TYR A 1 339 ? 3.19700   19.95300  16.02300 1.000 12.48000 ? 339 TYR A CZ  1 
ATOM   2652 O  OH  . TYR A 1 339 ? 1.94500   19.63400  15.55400 1.000 14.10000 ? 339 TYR A OH  1 
ATOM   2653 N  N   . PRO A 1 340 ? 6.81300   17.76800  18.79300 1.000 13.73000 ? 340 PRO A N   1 
ATOM   2654 C  CA  . PRO A 1 340 ? 5.63900   18.01500  19.63700 1.000 15.95000 ? 340 PRO A CA  1 
ATOM   2655 C  C   . PRO A 1 340 ? 5.84000   17.54900  21.08200 1.000 14.96000 ? 340 PRO A C   1 
ATOM   2656 O  O   . PRO A 1 340 ? 4.88700   17.09400  21.71100 1.000 14.94000 ? 340 PRO A O   1 
ATOM   2657 C  CB  . PRO A 1 340 ? 4.54600   17.17800  18.95400 1.000 11.64000 ? 340 PRO A CB  1 
ATOM   2658 C  CG  . PRO A 1 340 ? 5.31700   16.03200  18.24300 1.000 13.81000 ? 340 PRO A CG  1 
ATOM   2659 C  CD  . PRO A 1 340 ? 6.82000   16.37800  18.30400 1.000 14.14000 ? 340 PRO A CD  1 
ATOM   2660 N  N   . HIS A 1 341 ? 7.06300   17.66800  21.58800 1.000 13.33000 ? 341 HIS A N   1 
ATOM   2661 C  CA  . HIS A 1 341 ? 7.39000   17.19700  22.92400 1.000 14.50000 ? 341 HIS A CA  1 
ATOM   2662 C  C   . HIS A 1 341 ? 6.74700   18.06800  23.99400 1.000 13.46000 ? 341 HIS A C   1 
ATOM   2663 O  O   . HIS A 1 341 ? 6.41900   19.23600  23.77400 1.000 14.82000 ? 341 HIS A O   1 
ATOM   2664 C  CB  . HIS A 1 341 ? 8.90400   17.20600  23.14900 1.000 13.15000 ? 341 HIS A CB  1 
ATOM   2665 C  CG  . HIS A 1 341 ? 9.60400   16.00300  22.60300 1.000 14.29000 ? 341 HIS A CG  1 
ATOM   2666 N  ND1 . HIS A 1 341 ? 10.89400  15.67100  22.96000 1.000 14.76000 ? 341 HIS A ND1 1 
ATOM   2667 C  CD2 . HIS A 1 341 ? 9.20300   15.06200  21.71500 1.000 15.34000 ? 341 HIS A CD2 1 
ATOM   2668 C  CE1 . HIS A 1 341 ? 11.25300  14.56800  22.32500 1.000 14.01000 ? 341 HIS A CE1 1 
ATOM   2669 N  NE2 . HIS A 1 341 ? 10.24900  14.18400  21.55600 1.000 17.48000 ? 341 HIS A NE2 1 
ATOM   2670 N  N   . SER A 1 342 ? 6.63400   17.48200  25.18800 1.000 12.93000 ? 342 SER A N   1 
ATOM   2671 C  CA  . SER A 1 342 ? 6.15100   18.18900  26.36600 1.000 15.80000 ? 342 SER A CA  1 
ATOM   2672 C  C   . SER A 1 342 ? 6.89600   19.49800  26.61900 1.000 17.68000 ? 342 SER A C   1 
ATOM   2673 O  O   . SER A 1 342 ? 6.31400   20.45000  27.15300 1.000 17.41000 ? 342 SER A O   1 
ATOM   2674 C  CB  . SER A 1 342 ? 6.26800   17.26900  27.58000 1.000 16.16000 ? 342 SER A CB  1 
ATOM   2675 O  OG  . SER A 1 342 ? 7.55800   16.68500  27.65500 1.000 18.91000 ? 342 SER A OG  1 
ATOM   2676 N  N   . ASP A 1 343 ? 8.17400   19.56900  26.26000 1.000 16.96000 ? 343 ASP A N   1 
ATOM   2677 C  CA  . ASP A 1 343 ? 8.95300   20.77600  26.50300 1.000 16.09000 ? 343 ASP A CA  1 
ATOM   2678 C  C   . ASP A 1 343 ? 8.75500   21.86400  25.44700 1.000 15.01000 ? 343 ASP A C   1 
ATOM   2679 O  O   . ASP A 1 343 ? 9.22000   22.99000  25.65500 1.000 17.28000 ? 343 ASP A O   1 
ATOM   2680 C  CB  . ASP A 1 343 ? 10.44500  20.41500  26.60700 1.000 20.23000 ? 343 ASP A CB  1 
ATOM   2681 C  CG  . ASP A 1 343 ? 10.78100  19.72100  27.91800 1.000 22.51000 ? 343 ASP A CG  1 
ATOM   2682 O  OD1 . ASP A 1 343 ? 10.70100  20.38500  28.97300 1.000 24.87000 ? 343 ASP A OD1 1 
ATOM   2683 O  OD2 . ASP A 1 343 ? 11.09700  18.50900  27.89900 1.000 20.29000 ? 343 ASP A OD2 1 
ATOM   2684 N  N   . SER A 1 344 ? 8.07000   21.57900  24.34300 1.000 16.36000 ? 344 SER A N   1 
ATOM   2685 C  CA  . SER A 1 344 ? 7.89200   22.58500  23.29800 1.000 16.75000 ? 344 SER A CA  1 
ATOM   2686 C  C   . SER A 1 344 ? 7.13400   23.81700  23.80000 1.000 16.41000 ? 344 SER A C   1 
ATOM   2687 O  O   . SER A 1 344 ? 6.25100   23.72600  24.65500 1.000 15.93000 ? 344 SER A O   1 
ATOM   2688 C  CB  . SER A 1 344 ? 7.13600   21.99200  22.11800 1.000 14.64000 ? 344 SER A CB  1 
ATOM   2689 O  OG  . SER A 1 344 ? 6.99600   22.95200  21.09300 1.000 15.33000 ? 344 SER A OG  1 
ATOM   2690 N  N   . THR A 1 345 ? 7.46700   24.98100  23.22800 1.000 13.52000 ? 345 THR A N   1 
ATOM   2691 C  CA  . THR A 1 345 ? 6.71300   26.20500  23.47800 1.000 15.37000 ? 345 THR A CA  1 
ATOM   2692 C  C   . THR A 1 345 ? 5.62700   26.44700  22.44500 1.000 12.13000 ? 345 THR A C   1 
ATOM   2693 O  O   . THR A 1 345 ? 4.97500   27.49300  22.49500 1.000 15.23000 ? 345 THR A O   1 
ATOM   2694 C  CB  . THR A 1 345 ? 7.62900   27.42700  23.50800 1.000 13.75000 ? 345 THR A CB  1 
ATOM   2695 O  OG1 . THR A 1 345 ? 8.49800   27.38600  22.37300 1.000 15.02000 ? 345 THR A OG1 1 
ATOM   2696 C  CG2 . THR A 1 345 ? 8.44100   27.44700  24.79200 1.000 15.26000 ? 345 THR A CG2 1 
ATOM   2697 N  N   . TRP A 1 346 ? 5.45000   25.53700  21.49400 1.000 13.48000 ? 346 TRP A N   1 
ATOM   2698 C  CA  . TRP A 1 346 ? 4.32600   25.62300  20.57500 1.000 15.62000 ? 346 TRP A CA  1 
ATOM   2699 C  C   . TRP A 1 346 ? 3.02800   25.76100  21.37400 1.000 14.20000 ? 346 TRP A C   1 
ATOM   2700 O  O   . TRP A 1 346 ? 2.87600   25.10900  22.41200 1.000 15.72000 ? 346 TRP A O   1 
ATOM   2701 C  CB  . TRP A 1 346 ? 4.28400   24.37000  19.69500 1.000 14.81000 ? 346 TRP A CB  1 
ATOM   2702 C  CG  . TRP A 1 346 ? 3.28700   24.41800  18.57800 1.000 14.16000 ? 346 TRP A CG  1 
ATOM   2703 C  CD1 . TRP A 1 346 ? 3.53400   24.72700  17.26900 1.000 13.11000 ? 346 TRP A CD1 1 
ATOM   2704 C  CD2 . TRP A 1 346 ? 1.88700   24.12100  18.66100 1.000 16.45000 ? 346 TRP A CD2 1 
ATOM   2705 N  NE1 . TRP A 1 346 ? 2.37100   24.65300  16.53900 1.000 15.83000 ? 346 TRP A NE1 1 
ATOM   2706 C  CE2 . TRP A 1 346 ? 1.35000   24.27300  17.36900 1.000 14.72000 ? 346 TRP A CE2 1 
ATOM   2707 C  CE3 . TRP A 1 346 ? 1.03500   23.74900  19.70500 1.000 17.91000 ? 346 TRP A CE3 1 
ATOM   2708 C  CZ2 . TRP A 1 346 ? -0.00500  24.07300  17.09700 1.000 16.59000 ? 346 TRP A CZ2 1 
ATOM   2709 C  CZ3 . TRP A 1 346 ? -0.30500  23.53300  19.43000 1.000 17.32000 ? 346 TRP A CZ3 1 
ATOM   2710 C  CH2 . TRP A 1 346 ? -0.80700  23.69700  18.14000 1.000 13.29000 ? 346 TRP A CH2 1 
ATOM   2711 N  N   . PRO A 1 347 ? 2.08400   26.60000  20.94300 1.000 16.87000 ? 347 PRO A N   1 
ATOM   2712 C  CA  . PRO A 1 347 ? 2.06600   27.42300  19.73300 1.000 16.00000 ? 347 PRO A CA  1 
ATOM   2713 C  C   . PRO A 1 347 ? 2.41400   28.88000  19.99400 1.000 16.75000 ? 347 PRO A C   1 
ATOM   2714 O  O   . PRO A 1 347 ? 1.98800   29.75200  19.23200 1.000 18.78000 ? 347 PRO A O   1 
ATOM   2715 C  CB  . PRO A 1 347 ? 0.61400   27.31000  19.28400 1.000 17.91000 ? 347 PRO A CB  1 
ATOM   2716 C  CG  . PRO A 1 347 ? -0.14600  27.30600  20.59900 1.000 20.40000 ? 347 PRO A CG  1 
ATOM   2717 C  CD  . PRO A 1 347 ? 0.78000   26.65000  21.63700 1.000 19.02000 ? 347 PRO A CD  1 
ATOM   2718 N  N   . ARG A 1 348 ? 3.16300   29.15200  21.05100 1.000 14.51000 ? 348 ARG A N   1 
ATOM   2719 C  CA  . ARG A 1 348 ? 3.55500   30.51600  21.38600 1.000 15.13000 ? 348 ARG A CA  1 
ATOM   2720 C  C   . ARG A 1 348 ? 5.06900   30.67100  21.44000 1.000 13.86000 ? 348 ARG A C   1 
ATOM   2721 O  O   . ARG A 1 348 ? 5.60600   31.41700  22.26200 1.000 17.20000 ? 348 ARG A O   1 
ATOM   2722 C  CB  . ARG A 1 348 ? 2.92500   30.94500  22.70600 1.000 17.59000 ? 348 ARG A CB  1 
ATOM   2723 C  CG  . ARG A 1 348 ? 1.39200   30.97200  22.65100 1.000 23.40000 ? 348 ARG A CG  1 
ATOM   2724 C  CD  . ARG A 1 348 ? 0.78700   31.44900  23.97000 1.000 24.40000 ? 348 ARG A CD  1 
ATOM   2725 N  NE  . ARG A 1 348 ? 1.28100   32.77500  24.34700 1.000 35.23000 ? 348 ARG A NE  1 
ATOM   2726 C  CZ  . ARG A 1 348 ? 0.89100   33.92000  23.78700 1.000 29.70000 ? 348 ARG A CZ  1 
ATOM   2727 N  NH1 . ARG A 1 348 ? -0.00900  33.92400  22.80900 1.000 36.32000 ? 348 ARG A NH1 1 
ATOM   2728 N  NH2 . ARG A 1 348 ? 1.40100   35.06900  24.21400 1.000 30.23000 ? 348 ARG A NH2 1 
ATOM   2729 N  N   . SER A 1 349 ? 5.78600   29.97900  20.55600 1.000 16.73000 ? 349 SER A N   1 
ATOM   2730 C  CA  . SER A 1 349 ? 7.24200   30.09300  20.57100 1.000 14.79000 ? 349 SER A CA  1 
ATOM   2731 C  C   . SER A 1 349 ? 7.73800   31.51100  20.32200 1.000 16.27000 ? 349 SER A C   1 
ATOM   2732 O  O   . SER A 1 349 ? 8.66900   31.94100  21.02900 1.000 15.63000 ? 349 SER A O   1 
ATOM   2733 C  CB  . SER A 1 349 ? 7.85500   29.11100  19.56300 1.000 13.92000 ? 349 SER A CB  1 
ATOM   2734 O  OG  . SER A 1 349 ? 7.54900   27.77500  19.93200 1.000 14.77000 ? 349 SER A OG  1 
ATOM   2735 N  N   . PRO A 1 350 ? 7.20200   32.27700  19.36600 1.000 14.26000 ? 350 PRO A N   1 
ATOM   2736 C  CA  . PRO A 1 350 ? 7.72600   33.63900  19.18400 1.000 13.87000 ? 350 PRO A CA  1 
ATOM   2737 C  C   . PRO A 1 350 ? 7.57900   34.49300  20.42800 1.000 14.24000 ? 350 PRO A C   1 
ATOM   2738 O  O   . PRO A 1 350 ? 8.55200   35.11900  20.85500 1.000 14.95000 ? 350 PRO A O   1 
ATOM   2739 C  CB  . PRO A 1 350 ? 6.90400   34.17700  18.00400 1.000 12.43000 ? 350 PRO A CB  1 
ATOM   2740 C  CG  . PRO A 1 350 ? 6.49400   32.94300  17.24300 1.000 15.85000 ? 350 PRO A CG  1 
ATOM   2741 C  CD  . PRO A 1 350 ? 6.21400   31.93100  18.32900 1.000 13.83000 ? 350 PRO A CD  1 
ATOM   2742 N  N   . GLU A 1 351 ? 6.38400   34.52800  21.02300 1.000 16.15000 ? 351 GLU A N   1 
ATOM   2743 C  CA  . GLU A 1 351 ? 6.14600   35.37900  22.18300 1.000 16.02000 ? 351 GLU A CA  1 
ATOM   2744 C  C   . GLU A 1 351 ? 7.00400   34.95200  23.36800 1.000 18.85000 ? 351 GLU A C   1 
ATOM   2745 O  O   . GLU A 1 351 ? 7.58900   35.79500  24.06600 1.000 18.47000 ? 351 GLU A O   1 
ATOM   2746 C  CB  . GLU A 1 351 ? 4.65800   35.33300  22.56400 1.000 17.32000 ? 351 GLU A CB  1 
ATOM   2747 C  CG  . GLU A 1 351 ? 3.72300   36.02400  21.57200 1.000 19.37000 ? 351 GLU A CG  1 
ATOM   2748 C  CD  . GLU A 1 351 ? 3.34100   35.14100  20.39300 1.000 25.25000 ? 351 GLU A CD  1 
ATOM   2749 O  OE1 . GLU A 1 351 ? 3.69800   33.94400  20.38900 1.000 22.98000 ? 351 GLU A OE1 1 
ATOM   2750 O  OE2 . GLU A 1 351 ? 2.67500   35.64200  19.46400 1.000 25.54000 ? 351 GLU A OE2 1 
ATOM   2751 N  N   . THR A 1 352 ? 7.07100   33.64300  23.61900 1.000 18.86000 ? 352 THR A N   1 
ATOM   2752 C  CA  . THR A 1 352 ? 7.82500   33.13500  24.75700 1.000 15.93000 ? 352 THR A CA  1 
ATOM   2753 C  C   . THR A 1 352 ? 9.31000   33.44300  24.61300 1.000 15.76000 ? 352 THR A C   1 
ATOM   2754 O  O   . THR A 1 352 ? 9.94200   33.93700  25.55300 1.000 17.68000 ? 352 THR A O   1 
ATOM   2755 C  CB  . THR A 1 352 ? 7.58600   31.63500  24.90900 1.000 16.19000 ? 352 THR A CB  1 
ATOM   2756 O  OG1 . THR A 1 352 ? 6.21100   31.42200  25.24700 1.000 17.33000 ? 352 THR A OG1 1 
ATOM   2757 C  CG2 . THR A 1 352 ? 8.46200   31.06800  26.01400 1.000 17.98000 ? 352 THR A CG2 1 
ATOM   2758 N  N   . LEU A 1 353 ? 9.87900   33.19900  23.42900 1.000 13.29000 ? 353 LEU A N   1 
ATOM   2759 C  CA  . LEU A 1 353 ? 11.30100  33.48400  23.24800 1.000 15.32000 ? 353 LEU A CA  1 
ATOM   2760 C  C   . LEU A 1 353 ? 11.56600  34.98800  23.25800 1.000 20.74000 ? 353 LEU A C   1 
ATOM   2761 O  O   . LEU A 1 353 ? 12.52300  35.44700  23.89300 1.000 15.48000 ? 353 LEU A O   1 
ATOM   2762 C  CB  . LEU A 1 353 ? 11.81700  32.86200  21.94800 1.000 15.23000 ? 353 LEU A CB  1 
ATOM   2763 C  CG  . LEU A 1 353 ? 13.32900  32.99300  21.72400 1.000 17.43000 ? 353 LEU A CG  1 
ATOM   2764 C  CD1 . LEU A 1 353 ? 14.10800  32.33400  22.85900 1.000 14.59000 ? 353 LEU A CD1 1 
ATOM   2765 C  CD2 . LEU A 1 353 ? 13.77200  32.44700  20.36900 1.000 13.02000 ? 353 LEU A CD2 1 
ATOM   2766 N  N   . LYS A 1 354 ? 10.72500  35.77300  22.56800 1.000 16.54000 ? 354 LYS A N   1 
ATOM   2767 C  CA  . LYS A 1 354 ? 10.96100  37.21400  22.49300 1.000 14.81000 ? 354 LYS A CA  1 
ATOM   2768 C  C   . LYS A 1 354 ? 11.00300  37.83300  23.87900 1.000 16.04000 ? 354 LYS A C   1 
ATOM   2769 O  O   . LYS A 1 354 ? 11.81700  38.72500  24.15000 1.000 18.34000 ? 354 LYS A O   1 
ATOM   2770 C  CB  . LYS A 1 354 ? 9.88900   37.89000  21.63900 1.000 19.20000 ? 354 LYS A CB  1 
ATOM   2771 C  CG  . LYS A 1 354 ? 10.22400  39.34600  21.23500 1.000 19.37000 ? 354 LYS A CG  1 
ATOM   2772 C  CD  . LYS A 1 354 ? 11.59400  39.45400  20.56300 1.000 20.98000 ? 354 LYS A CD  1 
ATOM   2773 C  CE  . LYS A 1 354 ? 11.77900  40.78200  19.83000 1.000 28.75000 ? 354 LYS A CE  1 
ATOM   2774 N  NZ  . LYS A 1 354 ? 11.43700  41.97000  20.67300 1.000 25.44000 ? 354 LYS A NZ  1 
ATOM   2775 N  N   . SER A 1 355 ? 10.15000  37.36000  24.78200 1.000 18.44000 ? 355 SER A N   1 
ATOM   2776 C  CA  . SER A 1 355 ? 10.15800  37.90100  26.13300 1.000 17.23000 ? 355 SER A CA  1 
ATOM   2777 C  C   . SER A 1 355 ? 11.49600  37.65100  26.81800 1.000 20.13000 ? 355 SER A C   1 
ATOM   2778 O  O   . SER A 1 355 ? 12.00800  38.52900  27.52100 1.000 17.57000 ? 355 SER A O   1 
ATOM   2779 C  CB  . SER A 1 355 ? 9.00800   37.30600  26.93900 1.000 20.98000 ? 355 SER A CB  1 
ATOM   2780 O  OG  . SER A 1 355 ? 9.16600   37.56900  28.31500 1.000 27.45000 ? 355 SER A OG  1 
ATOM   2781 N  N   . GLU A 1 356 ? 12.08600  36.46500  26.61300 1.000 15.01000 ? 356 GLU A N   1 
ATOM   2782 C  CA  . GLU A 1 356 ? 13.38800  36.15900  27.20800 1.000 16.40000 ? 356 GLU A CA  1 
ATOM   2783 C  C   . GLU A 1 356 ? 14.49500  36.96700  26.55100 1.000 17.73000 ? 356 GLU A C   1 
ATOM   2784 O  O   . GLU A 1 356 ? 15.39700  37.47000  27.23500 1.000 17.78000 ? 356 GLU A O   1 
ATOM   2785 C  CB  . GLU A 1 356 ? 13.69800  34.66300  27.08300 1.000 19.38000 ? 356 GLU A CB  1 
ATOM   2786 C  CG  . GLU A 1 356 ? 12.60800  33.75900  27.62900 1.000 22.49000 ? 356 GLU A CG  1 
ATOM   2787 C  CD  . GLU A 1 356 ? 12.89400  32.27900  27.40700 1.000 19.29000 ? 356 GLU A CD  1 
ATOM   2788 O  OE1 . GLU A 1 356 ? 14.08400  31.89400  27.28400 1.000 18.60000 ? 356 GLU A OE1 1 
ATOM   2789 O  OE2 . GLU A 1 356 ? 11.92200  31.49600  27.36600 1.000 19.17000 ? 356 GLU A OE2 1 
ATOM   2790 N  N   . LEU A 1 357 ? 14.44900  37.08600  25.22400 1.000 15.80000 ? 357 LEU A N   1 
ATOM   2791 C  CA  . LEU A 1 357 ? 15.44000  37.88100  24.50500 1.000 16.26000 ? 357 LEU A CA  1 
ATOM   2792 C  C   . LEU A 1 357 ? 15.40300  39.34000  24.95400 1.000 17.92000 ? 357 LEU A C   1 
ATOM   2793 O  O   . LEU A 1 357 ? 16.44900  39.94900  25.20700 1.000 19.76000 ? 357 LEU A O   1 
ATOM   2794 C  CB  . LEU A 1 357 ? 15.19200  37.77600  22.99900 1.000 16.13000 ? 357 LEU A CB  1 
ATOM   2795 C  CG  . LEU A 1 357 ? 15.32900  36.38700  22.37600 1.000 15.24000 ? 357 LEU A CG  1 
ATOM   2796 C  CD1 . LEU A 1 357 ? 14.70200  36.33600  21.00300 1.000 18.36000 ? 357 LEU A CD1 1 
ATOM   2797 C  CD2 . LEU A 1 357 ? 16.79900  36.02300  22.29700 1.000 18.88000 ? 357 LEU A CD2 1 
ATOM   2798 N  N   . ASP A 1 358 ? 14.19900  39.91000  25.07000 1.000 18.38000 ? 358 ASP A N   1 
ATOM   2799 C  CA  . ASP A 1 358 ? 14.06400  41.29800  25.50300 1.000 20.48000 ? 358 ASP A CA  1 
ATOM   2800 C  C   . ASP A 1 358 ? 14.58600  41.49400  26.92100 1.000 20.62000 ? 358 ASP A C   1 
ATOM   2801 O  O   . ASP A 1 358 ? 15.28500  42.47400  27.19800 1.000 19.71000 ? 358 ASP A O   1 
ATOM   2802 C  CB  . ASP A 1 358 ? 12.60100  41.74600  25.40600 1.000 20.03000 ? 358 ASP A CB  1 
ATOM   2803 C  CG  . ASP A 1 358 ? 12.14900  41.96100  23.96500 1.000 21.97000 ? 358 ASP A CG  1 
ATOM   2804 O  OD1 . ASP A 1 358 ? 13.00800  42.06300  23.07000 1.000 28.18000 ? 358 ASP A OD1 1 
ATOM   2805 O  OD2 . ASP A 1 358 ? 10.93200  42.02600  23.73000 1.000 30.08000 ? 358 ASP A OD2 1 
ATOM   2806 N  N   . ALA A 1 359 ? 14.26500  40.57100  27.83200 1.000 17.32000 ? 359 ALA A N   1 
ATOM   2807 C  CA  . ALA A 1 359 ? 14.74300  40.69500  29.20700 1.000 17.82000 ? 359 ALA A CA  1 
ATOM   2808 C  C   . ALA A 1 359 ? 16.25800  40.57800  29.29400 1.000 21.28000 ? 359 ALA A C   1 
ATOM   2809 O  O   . ALA A 1 359 ? 16.87700  41.17900  30.18000 1.000 20.59000 ? 359 ALA A O   1 
ATOM   2810 C  CB  . ALA A 1 359 ? 14.07200  39.64100  30.08700 1.000 19.58000 ? 359 ALA A CB  1 
ATOM   2811 N  N   . ALA A 1 360 ? 16.87400  39.81400  28.39500 1.000 19.60000 ? 360 ALA A N   1 
ATOM   2812 C  CA  . ALA A 1 360 ? 18.32900  39.73700  28.32800 1.000 18.85000 ? 360 ALA A CA  1 
ATOM   2813 C  C   . ALA A 1 360 ? 18.96000  40.89000  27.54800 1.000 19.47000 ? 360 ALA A C   1 
ATOM   2814 O  O   . ALA A 1 360 ? 20.18000  40.89000  27.35900 1.000 20.94000 ? 360 ALA A O   1 
ATOM   2815 C  CB  . ALA A 1 360 ? 18.74500  38.40300  27.70300 1.000 21.37000 ? 360 ALA A CB  1 
ATOM   2816 N  N   . ARG A 1 361 ? 18.16600  41.85800  27.08600 1.000 18.61000 ? 361 ARG A N   1 
ATOM   2817 C  CA  . ARG A 1 361 ? 18.66700  43.02300  26.34800 1.000 19.57000 ? 361 ARG A CA  1 
ATOM   2818 C  C   . ARG A 1 361 ? 19.39600  42.61500  25.06500 1.000 21.61000 ? 361 ARG A C   1 
ATOM   2819 O  O   . ARG A 1 361 ? 20.44300  43.16800  24.72000 1.000 16.34000 ? 361 ARG A O   1 
ATOM   2820 C  CB  . ARG A 1 361 ? 19.56800  43.89800  27.22700 1.000 20.37000 ? 361 ARG A CB  1 
ATOM   2821 N  N   . CYS A 1 362 ? 18.83000  41.65900  24.33200 1.000 19.90000 ? 362 CYS A N   1 
ATOM   2822 C  CA  . CYS A 1 362 ? 19.43700  41.25400  23.06800 1.000 19.87000 ? 362 CYS A CA  1 
ATOM   2823 C  C   . CYS A 1 362 ? 19.21900  42.32800  22.01600 1.000 19.86000 ? 362 CYS A C   1 
ATOM   2824 O  O   . CYS A 1 362 ? 18.10400  42.83900  21.86300 1.000 17.62000 ? 362 CYS A O   1 
ATOM   2825 C  CB  . CYS A 1 362 ? 18.84800  39.93300  22.58600 1.000 20.22000 ? 362 CYS A CB  1 
ATOM   2826 S  SG  . CYS A 1 362 ? 19.36300  38.50300  23.58200 1.000 18.57000 ? 362 CYS A SG  1 
ATOM   2827 N  N   . THR A 1 363 ? 20.28400  42.66700  21.29300 1.000 15.38000 ? 363 THR A N   1 
ATOM   2828 C  CA  . THR A 1 363 ? 20.15500  43.51200  20.11800 1.000 17.30000 ? 363 THR A CA  1 
ATOM   2829 C  C   . THR A 1 363 ? 19.42100  42.75900  19.01100 1.000 20.56000 ? 363 THR A C   1 
ATOM   2830 O  O   . THR A 1 363 ? 19.24700  41.54000  19.06500 1.000 16.09000 ? 363 THR A O   1 
ATOM   2831 C  CB  . THR A 1 363 ? 21.52900  43.95200  19.62300 1.000 19.98000 ? 363 THR A CB  1 
ATOM   2832 O  OG1 . THR A 1 363 ? 22.25200  42.80900  19.13700 1.000 19.45000 ? 363 THR A OG1 1 
ATOM   2833 C  CG2 . THR A 1 363 ? 22.33000  44.61300  20.75700 1.000 15.38000 ? 363 THR A CG2 1 
ATOM   2834 N  N   . ASP A 1 364 ? 18.98800  43.50000  17.98700 1.000 20.65000 ? 364 ASP A N   1 
ATOM   2835 C  CA  . ASP A 1 364 ? 18.37600  42.84700  16.83500 1.000 21.08000 ? 364 ASP A CA  1 
ATOM   2836 C  C   . ASP A 1 364 ? 19.34400  41.85300  16.20100 1.000 18.86000 ? 364 ASP A C   1 
ATOM   2837 O  O   . ASP A 1 364 ? 18.94700  40.74800  15.82200 1.000 18.98000 ? 364 ASP A O   1 
ATOM   2838 C  CB  . ASP A 1 364 ? 17.92000  43.88900  15.80800 1.000 22.13000 ? 364 ASP A CB  1 
ATOM   2839 C  CG  . ASP A 1 364 ? 16.70400  44.68100  16.27200 1.000 25.27000 ? 364 ASP A CG  1 
ATOM   2840 O  OD1 . ASP A 1 364 ? 16.20900  44.42000  17.38100 1.000 25.60000 ? 364 ASP A OD1 1 
ATOM   2841 O  OD2 . ASP A 1 364 ? 16.23800  45.56500  15.52600 1.000 25.85000 ? 364 ASP A OD2 1 
ATOM   2842 N  N   . GLU A 1 365 ? 20.61800  42.22600  16.07800 1.000 18.90000 ? 365 GLU A N   1 
ATOM   2843 C  CA  . GLU A 1 365 ? 21.60400  41.30400  15.52700 1.000 17.29000 ? 365 GLU A CA  1 
ATOM   2844 C  C   . GLU A 1 365 ? 21.64500  40.01000  16.33400 1.000 16.22000 ? 365 GLU A C   1 
ATOM   2845 O  O   . GLU A 1 365 ? 21.65800  38.91100  15.76900 1.000 15.06000 ? 365 GLU A O   1 
ATOM   2846 C  CB  . GLU A 1 365 ? 22.98400  41.97000  15.49200 1.000 17.99000 ? 365 GLU A CB  1 
ATOM   2847 C  CG  . GLU A 1 365 ? 24.11500  41.00600  15.12400 1.000 25.33000 ? 365 GLU A CG  1 
ATOM   2848 C  CD  . GLU A 1 365 ? 25.49700  41.65300  15.13600 1.000 33.61000 ? 365 GLU A CD  1 
ATOM   2849 O  OE1 . GLU A 1 365 ? 25.84000  42.33000  16.13100 1.000 32.56000 ? 365 GLU A OE1 1 
ATOM   2850 O  OE2 . GLU A 1 365 ? 26.24500  41.47500  14.15400 1.000 34.16000 ? 365 GLU A OE2 1 
ATOM   2851 N  N   . GLU A 1 366 ? 21.65100  40.12600  17.66500 1.000 15.74000 ? 366 GLU A N   1 
ATOM   2852 C  CA  . GLU A 1 366 ? 21.66900  38.94300  18.52000 1.000 18.27000 ? 366 GLU A CA  1 
ATOM   2853 C  C   . GLU A 1 366 ? 20.39000  38.12600  18.38600 1.000 17.08000 ? 366 GLU A C   1 
ATOM   2854 O  O   . GLU A 1 366 ? 20.44600  36.88900  18.38800 1.000 14.09000 ? 366 GLU A O   1 
ATOM   2855 C  CB  . GLU A 1 366 ? 21.89100  39.34600  19.97300 1.000 15.87000 ? 366 GLU A CB  1 
ATOM   2856 C  CG  . GLU A 1 366 ? 23.31200  39.84600  20.25900 1.000 14.99000 ? 366 GLU A CG  1 
ATOM   2857 C  CD  . GLU A 1 366 ? 23.49700  40.24600  21.70500 1.000 19.53000 ? 366 GLU A CD  1 
ATOM   2858 O  OE1 . GLU A 1 366 ? 22.60900  40.94100  22.23900 1.000 18.20000 ? 366 GLU A OE1 1 
ATOM   2859 O  OE2 . GLU A 1 366 ? 24.51000  39.85200  22.31400 1.000 17.91000 ? 366 GLU A OE2 1 
ATOM   2860 N  N   . VAL A 1 367 ? 19.23000  38.79300  18.29500 1.000 15.73000 ? 367 VAL A N   1 
ATOM   2861 C  CA  . VAL A 1 367 ? 17.96700  38.08100  18.08500 1.000 15.09000 ? 367 VAL A CA  1 
ATOM   2862 C  C   . VAL A 1 367 ? 18.06500  37.20000  16.84800 1.000 17.10000 ? 367 VAL A C   1 
ATOM   2863 O  O   . VAL A 1 367 ? 17.80200  35.99300  16.90200 1.000 15.36000 ? 367 VAL A O   1 
ATOM   2864 C  CB  . VAL A 1 367 ? 16.79200  39.07100  17.98200 1.000 18.01000 ? 367 VAL A CB  1 
ATOM   2865 C  CG1 . VAL A 1 367 ? 15.51900  38.34400  17.53700 1.000 19.41000 ? 367 VAL A CG1 1 
ATOM   2866 C  CG2 . VAL A 1 367 ? 16.56600  39.77600  19.32500 1.000 16.70000 ? 367 VAL A CG2 1 
ATOM   2867 N  N   . ASP A 1 368 ? 18.50900  37.78100  15.72700 1.000 17.30000 ? 368 ASP A N   1 
ATOM   2868 C  CA  . ASP A 1 368 ? 18.61400  37.02100  14.48200 1.000 15.74000 ? 368 ASP A CA  1 
ATOM   2869 C  C   . ASP A 1 368 ? 19.59900  35.86000  14.61800 1.000 15.58000 ? 368 ASP A C   1 
ATOM   2870 O  O   . ASP A 1 368 ? 19.34000  34.75800  14.11700 1.000 14.41000 ? 368 ASP A O   1 
ATOM   2871 C  CB  . ASP A 1 368 ? 19.03700  37.93800  13.32300 1.000 15.93000 ? 368 ASP A CB  1 
ATOM   2872 C  CG  . ASP A 1 368 ? 17.89000  38.79400  12.78200 1.000 19.62000 ? 368 ASP A CG  1 
ATOM   2873 O  OD1 . ASP A 1 368 ? 16.71600  38.55800  13.13000 1.000 18.48000 ? 368 ASP A OD1 1 
ATOM   2874 O  OD2 . ASP A 1 368 ? 18.17100  39.71600  11.99700 1.000 21.52000 ? 368 ASP A OD2 1 
ATOM   2875 N  N   . LYS A 1 369 ? 20.74100  36.08800  15.27300 1.000 15.25000 ? 369 LYS A N   1 
ATOM   2876 C  CA  . LYS A 1 369 ? 21.70600  35.00400  15.43900 1.000 14.28000 ? 369 LYS A CA  1 
ATOM   2877 C  C   . LYS A 1 369 ? 21.07800  33.83000  16.17700 1.000 15.21000 ? 369 LYS A C   1 
ATOM   2878 O  O   . LYS A 1 369 ? 21.15000  32.68100  15.72200 1.000 14.92000 ? 369 LYS A O   1 
ATOM   2879 C  CB  . LYS A 1 369 ? 22.94600  35.50600  16.18200 1.000 13.75000 ? 369 LYS A CB  1 
ATOM   2880 C  CG  . LYS A 1 369 ? 23.88000  36.40300  15.34800 1.000 18.91000 ? 369 LYS A CG  1 
ATOM   2881 C  CD  . LYS A 1 369 ? 25.08000  36.85500  16.18800 1.000 19.24000 ? 369 LYS A CD  1 
ATOM   2882 C  CE  . LYS A 1 369 ? 26.04600  37.74500  15.40300 1.000 20.21000 ? 369 LYS A CE  1 
ATOM   2883 N  NZ  . LYS A 1 369 ? 26.58700  36.99800  14.26400 1.000 28.65000 ? 369 LYS A NZ  1 
ATOM   2884 N  N   . ILE A 1 370 ? 20.41800  34.11400  17.30100 1.000 12.83000 ? 370 ILE A N   1 
ATOM   2885 C  CA  . ILE A 1 370 ? 19.87800  33.05500  18.14600 1.000 14.40000 ? 370 ILE A CA  1 
ATOM   2886 C  C   . ILE A 1 370 ? 18.69100  32.36800  17.47800 1.000 13.21000 ? 370 ILE A C   1 
ATOM   2887 O  O   . ILE A 1 370 ? 18.54600  31.14300  17.56600 1.000 15.58000 ? 370 ILE A O   1 
ATOM   2888 C  CB  . ILE A 1 370 ? 19.50200  33.62700  19.52300 1.000 13.94000 ? 370 ILE A CB  1 
ATOM   2889 C  CG1 . ILE A 1 370 ? 20.77500  33.96200  20.31500 1.000 14.15000 ? 370 ILE A CG1 1 
ATOM   2890 C  CG2 . ILE A 1 370 ? 18.58800  32.66200  20.26100 1.000 13.58000 ? 370 ILE A CG2 1 
ATOM   2891 C  CD1 . ILE A 1 370 ? 20.55900  34.98500  21.41000 1.000 14.12000 ? 370 ILE A CD1 1 
ATOM   2892 N  N   . THR A 1 371 ? 17.82500  33.12800  16.79700 1.000 12.20000 ? 371 THR A N   1 
ATOM   2893 C  CA  . THR A 1 371 ? 16.60200  32.52100  16.29000 1.000 14.81000 ? 371 THR A CA  1 
ATOM   2894 C  C   . THR A 1 371 ? 16.79700  31.81400  14.95200 1.000 15.46000 ? 371 THR A C   1 
ATOM   2895 O  O   . THR A 1 371 ? 16.04600  30.87800  14.65900 1.000 14.34000 ? 371 THR A O   1 
ATOM   2896 C  CB  . THR A 1 371 ? 15.47600  33.55400  16.16700 1.000 17.67000 ? 371 THR A CB  1 
ATOM   2897 O  OG1 . THR A 1 371 ? 15.81400  34.53100  15.17600 1.000 17.53000 ? 371 THR A OG1 1 
ATOM   2898 C  CG2 . THR A 1 371 ? 15.21200  34.23500  17.48400 1.000 18.64000 ? 371 THR A CG2 1 
ATOM   2899 N  N   . PHE A 1 372 ? 17.79200  32.20300  14.13500 1.000 13.90000 ? 372 PHE A N   1 
ATOM   2900 C  CA  . PHE A 1 372 ? 18.01800  31.44800  12.90100 1.000 15.11000 ? 372 PHE A CA  1 
ATOM   2901 C  C   . PHE A 1 372 ? 19.42500  31.49700  12.31000 1.000 14.96000 ? 372 PHE A C   1 
ATOM   2902 O  O   . PHE A 1 372 ? 19.83200  30.53800  11.65300 1.000 15.98000 ? 372 PHE A O   1 
ATOM   2903 C  CB  . PHE A 1 372 ? 17.02700  31.89200  11.81500 1.000 14.46000 ? 372 PHE A CB  1 
ATOM   2904 C  CG  . PHE A 1 372 ? 17.44600  33.12800  11.05900 1.000 15.19000 ? 372 PHE A CG  1 
ATOM   2905 C  CD1 . PHE A 1 372 ? 17.10700  34.38200  11.53300 1.000 16.85000 ? 372 PHE A CD1 1 
ATOM   2906 C  CD2 . PHE A 1 372 ? 18.13800  33.03400  9.86400  1.000 15.11000 ? 372 PHE A CD2 1 
ATOM   2907 C  CE1 . PHE A 1 372 ? 17.47800  35.53600  10.84200 1.000 16.10000 ? 372 PHE A CE1 1 
ATOM   2908 C  CE2 . PHE A 1 372 ? 18.51100  34.17800  9.15700  1.000 16.44000 ? 372 PHE A CE2 1 
ATOM   2909 C  CZ  . PHE A 1 372 ? 18.17300  35.43300  9.65500  1.000 19.25000 ? 372 PHE A CZ  1 
ATOM   2910 N  N   . ALA A 1 373 ? 20.16200  32.60200  12.47200 1.000 15.00000 ? 373 ALA A N   1 
ATOM   2911 C  CA  . ALA A 1 373 ? 21.39600  32.75200  11.69700 1.000 15.70000 ? 373 ALA A CA  1 
ATOM   2912 C  C   . ALA A 1 373 ? 22.50300  31.83100  12.20300 1.000 15.06000 ? 373 ALA A C   1 
ATOM   2913 O  O   . ALA A 1 373 ? 23.31000  31.33200  11.41000 1.000 16.02000 ? 373 ALA A O   1 
ATOM   2914 C  CB  . ALA A 1 373 ? 21.85500  34.21300  11.70300 1.000 14.43000 ? 373 ALA A CB  1 
ATOM   2915 N  N   . ASN A 1 374 ? 22.58500  31.60000  13.51400 1.000 15.58000 ? 374 ASN A N   1 
ATOM   2916 C  CA  . ASN A 1 374 ? 23.61900  30.68300  14.00300 1.000 15.99000 ? 374 ASN A CA  1 
ATOM   2917 C  C   . ASN A 1 374 ? 23.38000  29.27900  13.47000 1.000 15.86000 ? 374 ASN A C   1 
ATOM   2918 O  O   . ASN A 1 374 ? 24.30600  28.60800  12.99500 1.000 14.46000 ? 374 ASN A O   1 
ATOM   2919 C  CB  . ASN A 1 374 ? 23.65100  30.66200  15.53400 1.000 14.40000 ? 374 ASN A CB  1 
ATOM   2920 C  CG  . ASN A 1 374 ? 24.13500  31.96900  16.11700 1.000 16.06000 ? 374 ASN A CG  1 
ATOM   2921 O  OD1 . ASN A 1 374 ? 24.72800  32.78500  15.41500 1.000 13.72000 ? 374 ASN A OD1 1 
ATOM   2922 N  ND2 . ASN A 1 374 ? 23.89200  32.16900  17.41000 1.000 12.16000 ? 374 ASN A ND2 1 
ATOM   2923 N  N   . ALA A 1 375 ? 22.13600  28.81600  13.57000 1.000 13.15000 ? 375 ALA A N   1 
ATOM   2924 C  CA  . ALA A 1 375 ? 21.77600  27.49800  13.06900 1.000 17.59000 ? 375 ALA A CA  1 
ATOM   2925 C  C   . ALA A 1 375 ? 22.00700  27.40800  11.57500 1.000 13.47000 ? 375 ALA A C   1 
ATOM   2926 O  O   . ALA A 1 375 ? 22.54000  26.40800  11.07600 1.000 14.37000 ? 375 ALA A O   1 
ATOM   2927 C  CB  . ALA A 1 375 ? 20.30800  27.20900  13.39500 1.000 16.56000 ? 375 ALA A CB  1 
ATOM   2928 N  N   . ALA A 1 376 ? 21.61700  28.44800  10.83900 1.000 14.69000 ? 376 ALA A N   1 
ATOM   2929 C  CA  . ALA A 1 376 ? 21.74200  28.39100  9.38900  1.000 15.23000 ? 376 ALA A CA  1 
ATOM   2930 C  C   . ALA A 1 376 ? 23.20000  28.26600  8.97100  1.000 17.19000 ? 376 ALA A C   1 
ATOM   2931 O  O   . ALA A 1 376 ? 23.52400  27.49700  8.06300  1.000 17.65000 ? 376 ALA A O   1 
ATOM   2932 C  CB  . ALA A 1 376 ? 21.08400  29.61400  8.75000  1.000 17.13000 ? 376 ALA A CB  1 
ATOM   2933 N  N   . LYS A 1 377 ? 24.09400  29.00500  9.62500  1.000 14.67000 ? 377 LYS A N   1 
ATOM   2934 C  CA  . LYS A 1 377 ? 25.51200  28.86600  9.32200  1.000 16.81000 ? 377 LYS A CA  1 
ATOM   2935 C  C   . LYS A 1 377 ? 26.03300  27.49300  9.73600  1.000 16.72000 ? 377 LYS A C   1 
ATOM   2936 O  O   . LYS A 1 377 ? 26.74500  26.83700  8.96700  1.000 14.05000 ? 377 LYS A O   1 
ATOM   2937 C  CB  . LYS A 1 377 ? 26.29900  29.97400  10.02300 1.000 18.92000 ? 377 LYS A CB  1 
ATOM   2938 C  CG  . LYS A 1 377 ? 27.78500  29.95200  9.74600  1.000 20.37000 ? 377 LYS A CG  1 
ATOM   2939 C  CD  . LYS A 1 377 ? 28.35300  31.35800  9.67700  1.000 28.70000 ? 377 LYS A CD  1 
ATOM   2940 C  CE  . LYS A 1 377 ? 29.88200  31.36100  9.68800  1.000 37.97000 ? 377 LYS A CE  1 
ATOM   2941 N  NZ  . LYS A 1 377 ? 30.44000  31.57900  11.06500 1.000 46.78000 ? 377 LYS A NZ  1 
ATOM   2942 N  N   . PHE A 1 378 ? 25.66900  27.03400  10.93800 1.000 15.09000 ? 378 PHE A N   1 
ATOM   2943 C  CA  . PHE A 1 378 ? 26.23600  25.79500  11.47400 1.000 15.42000 ? 378 PHE A CA  1 
ATOM   2944 C  C   . PHE A 1 378 ? 25.83000  24.58500  10.64400 1.000 16.53000 ? 378 PHE A C   1 
ATOM   2945 O  O   . PHE A 1 378 ? 26.64600  23.68300  10.40700 1.000 15.27000 ? 378 PHE A O   1 
ATOM   2946 C  CB  . PHE A 1 378 ? 25.80000  25.62100  12.92700 1.000 16.51000 ? 378 PHE A CB  1 
ATOM   2947 C  CG  . PHE A 1 378 ? 26.71300  24.75100  13.74700 1.000 13.26000 ? 378 PHE A CG  1 
ATOM   2948 C  CD1 . PHE A 1 378 ? 27.90500  25.25100  14.25000 1.000 15.68000 ? 378 PHE A CD1 1 
ATOM   2949 C  CD2 . PHE A 1 378 ? 26.35400  23.45000  14.05600 1.000 13.98000 ? 378 PHE A CD2 1 
ATOM   2950 C  CE1 . PHE A 1 378 ? 28.74100  24.45900  15.02400 1.000 14.67000 ? 378 PHE A CE1 1 
ATOM   2951 C  CE2 . PHE A 1 378 ? 27.18600  22.64800  14.83400 1.000 13.75000 ? 378 PHE A CE2 1 
ATOM   2952 C  CZ  . PHE A 1 378 ? 28.38200  23.15900  15.31300 1.000 14.24000 ? 378 PHE A CZ  1 
ATOM   2953 N  N   . PHE A 1 379 ? 24.58200  24.55000  10.18300 1.000 15.50000 ? 379 PHE A N   1 
ATOM   2954 C  CA  . PHE A 1 379 ? 24.07800  23.45000  9.37300  1.000 14.79000 ? 379 PHE A CA  1 
ATOM   2955 C  C   . PHE A 1 379 ? 24.16900  23.72100  7.87200  1.000 18.39000 ? 379 PHE A C   1 
ATOM   2956 O  O   . PHE A 1 379 ? 23.57400  22.97200  7.08500  1.000 17.87000 ? 379 PHE A O   1 
ATOM   2957 C  CB  . PHE A 1 379 ? 22.62900  23.14100  9.76300  1.000 11.81000 ? 379 PHE A CB  1 
ATOM   2958 C  CG  . PHE A 1 379 ? 22.49000  22.51100  11.11300 1.000 15.88000 ? 379 PHE A CG  1 
ATOM   2959 C  CD1 . PHE A 1 379 ? 22.58000  23.27500  12.26700 1.000 15.45000 ? 379 PHE A CD1 1 
ATOM   2960 C  CD2 . PHE A 1 379 ? 22.24800  21.15300  11.22700 1.000 13.80000 ? 379 PHE A CD2 1 
ATOM   2961 C  CE1 . PHE A 1 379 ? 22.44500  22.69100  13.51400 1.000 15.04000 ? 379 PHE A CE1 1 
ATOM   2962 C  CE2 . PHE A 1 379 ? 22.11000  20.56100  12.46300 1.000 15.67000 ? 379 PHE A CE2 1 
ATOM   2963 C  CZ  . PHE A 1 379 ? 22.20800  21.32700  13.61300 1.000 16.15000 ? 379 PHE A CZ  1 
ATOM   2964 N  N   . ASP A 1 380 ? 24.88500  24.77200  7.46600  1.000 13.46000 ? 380 ASP A N   1 
ATOM   2965 C  CA  . ASP A 1 380 ? 25.10700  25.09400  6.05400  1.000 19.47000 ? 380 ASP A CA  1 
ATOM   2966 C  C   . ASP A 1 380 ? 23.78600  25.07900  5.28800  1.000 19.91000 ? 380 ASP A C   1 
ATOM   2967 O  O   . ASP A 1 380 ? 23.61500  24.38500  4.28300  1.000 17.47000 ? 380 ASP A O   1 
ATOM   2968 C  CB  . ASP A 1 380 ? 26.12700  24.13900  5.42500  1.000 19.75000 ? 380 ASP A CB  1 
ATOM   2969 C  CG  . ASP A 1 380 ? 26.66100  24.64900  4.08900  1.000 29.57000 ? 380 ASP A CG  1 
ATOM   2970 O  OD1 . ASP A 1 380 ? 26.52700  25.86500  3.81800  1.000 24.80000 ? 380 ASP A OD1 1 
ATOM   2971 O  OD2 . ASP A 1 380 ? 27.19700  23.82900  3.31100  1.000 35.21000 ? 380 ASP A OD2 1 
ATOM   2972 N  N   . TRP A 1 381 ? 22.82800  25.79600  5.83600  1.000 15.79000 ? 381 TRP A N   1 
ATOM   2973 C  CA  . TRP A 1 381 ? 21.48900  25.86800  5.27100  1.000 18.42000 ? 381 TRP A CA  1 
ATOM   2974 C  C   . TRP A 1 381 ? 21.05900  27.28100  4.95400  1.000 22.54000 ? 381 TRP A C   1 
ATOM   2975 O  O   . TRP A 1 381 ? 21.18800  28.13500  5.77100  1.000 21.63000 ? 381 TRP A O   1 
ATOM   2976 C  CB  . TRP A 1 381 ? 20.45600  25.18600  6.19500  1.000 20.45000 ? 381 TRP A CB  1 
ATOM   2977 C  CG  . TRP A 1 381 ? 19.18800  24.57000  5.55100  1.000 23.41000 ? 381 TRP A CG  1 
ATOM   2978 C  CD1 . TRP A 1 381 ? 19.07000  23.40000  4.84200  1.000 23.08000 ? 381 TRP A CD1 1 
ATOM   2979 C  CD2 . TRP A 1 381 ? 17.91700  25.08900  5.65000  1.000 21.40000 ? 381 TRP A CD2 1 
ATOM   2980 N  NE1 . TRP A 1 381 ? 17.78400  23.19400  4.47100  1.000 26.30000 ? 381 TRP A NE1 1 
ATOM   2981 C  CE2 . TRP A 1 381 ? 17.05200  24.23900  4.96600  1.000 25.26000 ? 381 TRP A CE2 1 
ATOM   2982 C  CE3 . TRP A 1 381 ? 17.41100  26.21900  6.23000  1.000 21.79000 ? 381 TRP A CE3 1 
ATOM   2983 C  CZ2 . TRP A 1 381 ? 15.76300  24.49300  4.88100  1.000 20.61000 ? 381 TRP A CZ2 1 
ATOM   2984 C  CZ3 . TRP A 1 381 ? 16.17800  26.45100  6.14100  1.000 21.88000 ? 381 TRP A CZ3 1 
ATOM   2985 C  CH2 . TRP A 1 381 ? 15.32400  25.59000  5.49700  1.000 28.83000 ? 381 TRP A CH2 1 
ATOM   2986 N  N   . ASP A 1 382 ? 20.57000  27.46900  3.74700  1.000 16.76000 ? 382 ASP A N   1 
ATOM   2987 C  CA  . ASP A 1 382 ? 20.13700  28.78200  3.29900  1.000 23.36000 ? 382 ASP A CA  1 
ATOM   2988 C  C   . ASP A 1 382 ? 18.65200  28.93100  3.61800  1.000 19.62000 ? 382 ASP A C   1 
ATOM   2989 O  O   . ASP A 1 382 ? 17.82100  28.32400  2.92800  1.000 20.98000 ? 382 ASP A O   1 
ATOM   2990 C  CB  . ASP A 1 382 ? 20.39500  28.92500  1.80700  1.000 20.63000 ? 382 ASP A CB  1 
ATOM   2991 C  CG  . ASP A 1 382 ? 19.98500  30.27600  1.25200  1.000 27.16000 ? 382 ASP A CG  1 
ATOM   2992 O  OD1 . ASP A 1 382 ? 19.46300  31.13800  2.00400  1.000 23.60000 ? 382 ASP A OD1 1 
ATOM   2993 O  OD2 . ASP A 1 382 ? 20.19000  30.46600  0.03200  1.000 26.17000 ? 382 ASP A OD2 1 
ATOM   2994 N  N   . PRO A 1 383 ? 18.26900  29.70800  4.63600  1.000 20.26000 ? 383 PRO A N   1 
ATOM   2995 C  CA  . PRO A 1 383 ? 16.84800  29.74100  5.03000  1.000 23.03000 ? 383 PRO A CA  1 
ATOM   2996 C  C   . PRO A 1 383 ? 15.95100  30.37000  3.99100  1.000 19.71000 ? 383 PRO A C   1 
ATOM   2997 O  O   . PRO A 1 383 ? 14.74200  30.13600  4.02000  1.000 16.38000 ? 383 PRO A O   1 
ATOM   2998 C  CB  . PRO A 1 383 ? 16.84700  30.56400  6.32700  1.000 17.77000 ? 383 PRO A CB  1 
ATOM   2999 C  CG  . PRO A 1 383 ? 18.11900  31.33000  6.29800  1.000 20.84000 ? 383 PRO A CG  1 
ATOM   3000 C  CD  . PRO A 1 383 ? 19.10900  30.59200  5.46400  1.000 17.66000 ? 383 PRO A CD  1 
ATOM   3001 N  N   . PHE A 1 384 ? 16.49600  31.17500  3.08800  1.000 16.87000 ? 384 PHE A N   1 
ATOM   3002 C  CA  . PHE A 1 384 ? 15.67000  31.91800  2.15100  1.000 24.16000 ? 384 PHE A CA  1 
ATOM   3003 C  C   . PHE A 1 384 ? 15.85200  31.44600  0.71400  1.000 22.40000 ? 384 PHE A C   1 
ATOM   3004 O  O   . PHE A 1 384 ? 15.44700  32.15100  -0.21800 1.000 25.60000 ? 384 PHE A O   1 
ATOM   3005 C  CB  . PHE A 1 384 ? 15.94900  33.41700  2.28800  1.000 17.54000 ? 384 PHE A CB  1 
ATOM   3006 C  CG  . PHE A 1 384 ? 16.03700  33.87900  3.71900  1.000 17.54000 ? 384 PHE A CG  1 
ATOM   3007 C  CD1 . PHE A 1 384 ? 14.94500  33.75500  4.56900  1.000 17.30000 ? 384 PHE A CD1 1 
ATOM   3008 C  CD2 . PHE A 1 384 ? 17.21800  34.40500  4.22500  1.000 20.71000 ? 384 PHE A CD2 1 
ATOM   3009 C  CE1 . PHE A 1 384 ? 15.01600  34.16700  5.89400  1.000 17.12000 ? 384 PHE A CE1 1 
ATOM   3010 C  CE2 . PHE A 1 384 ? 17.29700  34.81400  5.55600  1.000 21.99000 ? 384 PHE A CE2 1 
ATOM   3011 C  CZ  . PHE A 1 384 ? 16.18800  34.69400  6.38700  1.000 15.08000 ? 384 PHE A CZ  1 
ATOM   3012 N  N   . GLU A 1 385 ? 16.44500  30.26100  0.50900  1.000 20.90000 ? 385 GLU A N   1 
ATOM   3013 C  CA  . GLU A 1 385 ? 16.55700  29.73300  -0.85000 1.000 19.85000 ? 385 GLU A CA  1 
ATOM   3014 C  C   . GLU A 1 385 ? 15.18500  29.56600  -1.48800 1.000 25.15000 ? 385 GLU A C   1 
ATOM   3015 O  O   . GLU A 1 385 ? 14.96800  29.95800  -2.63900 1.000 23.06000 ? 385 GLU A O   1 
ATOM   3016 C  CB  . GLU A 1 385 ? 17.30200  28.39700  -0.84900 1.000 24.98000 ? 385 GLU A CB  1 
ATOM   3017 C  CG  . GLU A 1 385 ? 17.39100  27.76400  -2.24100 1.000 26.93000 ? 385 GLU A CG  1 
ATOM   3018 C  CD  . GLU A 1 385 ? 18.16800  26.45900  -2.25800 1.000 33.90000 ? 385 GLU A CD  1 
ATOM   3019 O  OE1 . GLU A 1 385 ? 18.72400  26.07400  -1.20700 1.000 36.08000 ? 385 GLU A OE1 1 
ATOM   3020 O  OE2 . GLU A 1 385 ? 18.21400  25.81100  -3.32600 1.000 40.32000 ? 385 GLU A OE2 1 
ATOM   3021 N  N   . HIS A 1 386 ? 14.23800  28.98300  -0.75100 1.000 19.23000 ? 386 HIS A N   1 
ATOM   3022 C  CA  . HIS A 1 386 ? 12.92900  28.65300  -1.28900 1.000 22.31000 ? 386 HIS A CA  1 
ATOM   3023 C  C   . HIS A 1 386 ? 11.82100  29.57800  -0.82400 1.000 24.96000 ? 386 HIS A C   1 
ATOM   3024 O  O   . HIS A 1 386 ? 10.74900  29.59000  -1.44200 1.000 26.58000 ? 386 HIS A O   1 
ATOM   3025 C  CB  . HIS A 1 386 ? 12.55100  27.21400  -0.91200 1.000 22.32000 ? 386 HIS A CB  1 
ATOM   3026 C  CG  . HIS A 1 386 ? 13.48900  26.19500  -1.46600 1.000 22.22000 ? 386 HIS A CG  1 
ATOM   3027 N  ND1 . HIS A 1 386 ? 14.41000  25.53100  -0.68900 1.000 28.97000 ? 386 HIS A ND1 1 
ATOM   3028 C  CD2 . HIS A 1 386 ? 13.66900  25.74800  -2.73100 1.000 22.63000 ? 386 HIS A CD2 1 
ATOM   3029 C  CE1 . HIS A 1 386 ? 15.10900  24.70500  -1.44700 1.000 25.91000 ? 386 HIS A CE1 1 
ATOM   3030 N  NE2 . HIS A 1 386 ? 14.67900  24.81800  -2.69000 1.000 26.35000 ? 386 HIS A NE2 1 
ATOM   3031 N  N   . ILE A 1 387 ? 12.04900  30.35100  0.23500  1.000 19.54000 ? 387 ILE A N   1 
ATOM   3032 C  CA  . ILE A 1 387 ? 11.03700  31.23400  0.79500  1.000 21.24000 ? 387 ILE A CA  1 
ATOM   3033 C  C   . ILE A 1 387 ? 11.72700  32.56700  1.04800  1.000 21.86000 ? 387 ILE A C   1 
ATOM   3034 O  O   . ILE A 1 387 ? 12.66200  32.63200  1.85000  1.000 18.96000 ? 387 ILE A O   1 
ATOM   3035 C  CB  . ILE A 1 387 ? 10.43600  30.66300  2.09000  1.000 19.72000 ? 387 ILE A CB  1 
ATOM   3036 C  CG1 . ILE A 1 387 ? 9.83000   29.27800  1.81400  1.000 21.96000 ? 387 ILE A CG1 1 
ATOM   3037 C  CG2 . ILE A 1 387 ? 9.42000   31.62400  2.70200  1.000 21.28000 ? 387 ILE A CG2 1 
ATOM   3038 C  CD1 . ILE A 1 387 ? 9.32800   28.54700  3.04300  1.000 19.48000 ? 387 ILE A CD1 1 
ATOM   3039 N  N   . PRO A 1 388 ? 11.34000  33.65200  0.36800  1.000 22.08000 ? 388 PRO A N   1 
ATOM   3040 C  CA  . PRO A 1 388 ? 12.02200  34.93800  0.57600  1.000 23.01000 ? 388 PRO A CA  1 
ATOM   3041 C  C   . PRO A 1 388 ? 11.91700  35.37900  2.02300  1.000 21.15000 ? 388 PRO A C   1 
ATOM   3042 O  O   . PRO A 1 388 ? 10.98100  35.01000  2.73700  1.000 18.93000 ? 388 PRO A O   1 
ATOM   3043 C  CB  . PRO A 1 388 ? 11.26700  35.90300  -0.34900 1.000 29.47000 ? 388 PRO A CB  1 
ATOM   3044 C  CG  . PRO A 1 388 ? 10.46500  35.04700  -1.26700 1.000 29.91000 ? 388 PRO A CG  1 
ATOM   3045 C  CD  . PRO A 1 388 ? 10.18800  33.77300  -0.53800 1.000 23.10000 ? 388 PRO A CD  1 
ATOM   3046 N  N   . ARG A 1 389 ? 12.88000  36.20300  2.44900  1.000 23.71000 ? 389 ARG A N   1 
ATOM   3047 C  CA  . ARG A 1 389 ? 12.94600  36.56000  3.86300  1.000 22.69000 ? 389 ARG A CA  1 
ATOM   3048 C  C   . ARG A 1 389 ? 11.69000  37.29400  4.31900  1.000 23.07000 ? 389 ARG A C   1 
ATOM   3049 O  O   . ARG A 1 389 ? 11.20800  37.06800  5.43400  1.000 22.45000 ? 389 ARG A O   1 
ATOM   3050 C  CB  . ARG A 1 389 ? 14.18700  37.40200  4.17000  1.000 20.94000 ? 389 ARG A CB  1 
ATOM   3051 C  CG  . ARG A 1 389 ? 14.24000  37.79600  5.64800  1.000 22.25000 ? 389 ARG A CG  1 
ATOM   3052 C  CD  . ARG A 1 389 ? 15.54700  38.43500  6.09700  1.000 21.10000 ? 389 ARG A CD  1 
ATOM   3053 N  NE  . ARG A 1 389 ? 15.46300  38.78300  7.52300  1.000 22.39000 ? 389 ARG A NE  1 
ATOM   3054 C  CZ  . ARG A 1 389 ? 16.51800  38.92100  8.31700  1.000 28.83000 ? 389 ARG A CZ  1 
ATOM   3055 N  NH1 . ARG A 1 389 ? 17.74100  38.74700  7.82700  1.000 31.88000 ? 389 ARG A NH1 1 
ATOM   3056 N  NH2 . ARG A 1 389 ? 16.35200  39.22800  9.59200  1.000 26.85000 ? 389 ARG A NH2 1 
ATOM   3057 N  N   . GLU A 1 390 ? 11.14200  38.17900  3.47700  1.000 22.25000 ? 390 GLU A N   1 
ATOM   3058 C  CA  . GLU A 1 390 ? 9.94000   38.90700  3.87100  1.000 24.33000 ? 390 GLU A CA  1 
ATOM   3059 C  C   . GLU A 1 390 ? 8.73500   37.98700  3.99200  1.000 23.61000 ? 390 GLU A C   1 
ATOM   3060 O  O   . GLU A 1 390 ? 7.75200   38.34300  4.65700  1.000 22.26000 ? 390 GLU A O   1 
ATOM   3061 C  CB  . GLU A 1 390 ? 9.65000   40.04000  2.87700  1.000 24.34000 ? 390 GLU A CB  1 
ATOM   3062 C  CG  . GLU A 1 390 ? 9.11800   39.58600  1.52700  1.000 27.39000 ? 390 GLU A CG  1 
ATOM   3063 C  CD  . GLU A 1 390 ? 10.21200  39.30700  0.50900  1.000 44.76000 ? 390 GLU A CD  1 
ATOM   3064 O  OE1 . GLU A 1 390 ? 11.41200  39.35600  0.87700  1.000 38.85000 ? 390 GLU A OE1 1 
ATOM   3065 O  OE2 . GLU A 1 390 ? 9.86500   39.04800  -0.67000 1.000 49.34000 ? 390 GLU A OE2 1 
ATOM   3066 N  N   . GLU A 1 391 ? 8.79600   36.81300  3.38000  1.000 21.32000 ? 391 GLU A N   1 
ATOM   3067 C  CA  . GLU A 1 391 ? 7.74700   35.81500  3.49500  1.000 19.97000 ? 391 GLU A CA  1 
ATOM   3068 C  C   . GLU A 1 391 ? 8.06100   34.74300  4.52600  1.000 19.17000 ? 391 GLU A C   1 
ATOM   3069 O  O   . GLU A 1 391 ? 7.24600   33.84800  4.72200  1.000 20.36000 ? 391 GLU A O   1 
ATOM   3070 C  CB  . GLU A 1 391 ? 7.49400   35.16100  2.13500  1.000 23.61000 ? 391 GLU A CB  1 
ATOM   3071 C  CG  . GLU A 1 391 ? 6.90500   36.10900  1.10100  1.000 29.34000 ? 391 GLU A CG  1 
ATOM   3072 C  CD  . GLU A 1 391 ? 6.79700   35.48500  -0.28000 1.000 38.02000 ? 391 GLU A CD  1 
ATOM   3073 O  OE1 . GLU A 1 391 ? 6.71700   34.23900  -0.37300 1.000 40.55000 ? 391 GLU A OE1 1 
ATOM   3074 O  OE2 . GLU A 1 391 ? 6.78800   36.24500  -1.27500 1.000 45.63000 ? 391 GLU A OE2 1 
ATOM   3075 N  N   . ALA A 1 392 ? 9.21400   34.81400  5.19100  1.000 20.98000 ? 392 ALA A N   1 
ATOM   3076 C  CA  . ALA A 1 392 ? 9.66100   33.77300  6.11100  1.000 19.21000 ? 392 ALA A CA  1 
ATOM   3077 C  C   . ALA A 1 392 ? 9.54400   34.17000  7.57400  1.000 21.32000 ? 392 ALA A C   1 
ATOM   3078 O  O   . ALA A 1 392 ? 9.87100   33.35700  8.45600  1.000 16.65000 ? 392 ALA A O   1 
ATOM   3079 C  CB  . ALA A 1 392 ? 11.11400  33.39800  5.80100  1.000 16.37000 ? 392 ALA A CB  1 
ATOM   3080 N  N   . THR A 1 393 ? 9.09000   35.39000  7.85800  1.000 17.43000 ? 393 THR A N   1 
ATOM   3081 C  CA  . THR A 1 393 ? 9.01400   35.87500  9.22500  1.000 17.85000 ? 393 THR A CA  1 
ATOM   3082 C  C   . THR A 1 393 ? 7.86300   35.20300  9.97700  1.000 18.44000 ? 393 THR A C   1 
ATOM   3083 O  O   . THR A 1 393 ? 6.98100   34.57100  9.38900  1.000 18.01000 ? 393 THR A O   1 
ATOM   3084 C  CB  . THR A 1 393 ? 8.80600   37.38900  9.25500  1.000 19.33000 ? 393 THR A CB  1 
ATOM   3085 O  OG1 . THR A 1 393 ? 7.52200   37.69000  8.69300  1.000 19.53000 ? 393 THR A OG1 1 
ATOM   3086 C  CG2 . THR A 1 393 ? 9.90700   38.11100  8.48200  1.000 18.13000 ? 393 THR A CG2 1 
ATOM   3087 N  N   . VAL A 1 394 ? 7.90200   35.35200  11.30400 1.000 15.89000 ? 394 VAL A N   1 
ATOM   3088 C  CA  . VAL A 1 394 ? 6.81800   34.88400  12.16400 1.000 19.12000 ? 394 VAL A CA  1 
ATOM   3089 C  C   . VAL A 1 394 ? 5.48500   35.42100  11.66400 1.000 19.62000 ? 394 VAL A C   1 
ATOM   3090 O  O   . VAL A 1 394 ? 4.52200   34.67100  11.47100 1.000 18.75000 ? 394 VAL A O   1 
ATOM   3091 C  CB  . VAL A 1 394 ? 7.08400   35.30700  13.62000 1.000 18.27000 ? 394 VAL A CB  1 
ATOM   3092 C  CG1 . VAL A 1 394 ? 5.81700   35.20200  14.47100 1.000 17.06000 ? 394 VAL A CG1 1 
ATOM   3093 C  CG2 . VAL A 1 394 ? 8.24600   34.49000  14.20900 1.000 15.76000 ? 394 VAL A CG2 1 
ATOM   3094 N  N   . GLY A 1 395 ? 5.42000   36.73600  11.43300 1.000 20.19000 ? 395 GLY A N   1 
ATOM   3095 C  CA  . GLY A 1 395 ? 4.16200   37.34700  11.03500 1.000 20.64000 ? 395 GLY A CA  1 
ATOM   3096 C  C   . GLY A 1 395 ? 3.67100   36.84300  9.69300  1.000 19.93000 ? 395 GLY A C   1 
ATOM   3097 O  O   . GLY A 1 395 ? 2.48100   36.55900  9.52400  1.000 20.99000 ? 395 GLY A O   1 
ATOM   3098 N  N   . ALA A 1 396 ? 4.58200   36.71000  8.72400  1.000 20.31000 ? 396 ALA A N   1 
ATOM   3099 C  CA  . ALA A 1 396 ? 4.17100   36.26900  7.39300  1.000 18.59000 ? 396 ALA A CA  1 
ATOM   3100 C  C   . ALA A 1 396 ? 3.68900   34.82100  7.40600  1.000 21.41000 ? 396 ALA A C   1 
ATOM   3101 O  O   . ALA A 1 396 ? 2.69200   34.48700  6.75400  1.000 19.27000 ? 396 ALA A O   1 
ATOM   3102 C  CB  . ALA A 1 396 ? 5.32000   36.44400  6.40600  1.000 20.63000 ? 396 ALA A CB  1 
ATOM   3103 N  N   . LEU A 1 397 ? 4.37600   33.94300  8.14300  1.000 19.62000 ? 397 LEU A N   1 
ATOM   3104 C  CA  . LEU A 1 397 ? 3.94000   32.54900  8.18400  1.000 20.26000 ? 397 LEU A CA  1 
ATOM   3105 C  C   . LEU A 1 397 ? 2.62400   32.41200  8.94200  1.000 18.49000 ? 397 LEU A C   1 
ATOM   3106 O  O   . LEU A 1 397 ? 1.75100   31.63300  8.54300  1.000 17.79000 ? 397 LEU A O   1 
ATOM   3107 C  CB  . LEU A 1 397 ? 5.02700   31.66300  8.79900  1.000 14.89000 ? 397 LEU A CB  1 
ATOM   3108 C  CG  . LEU A 1 397 ? 6.36900   31.54100  8.05000  1.000 16.77000 ? 397 LEU A CG  1 
ATOM   3109 C  CD1 . LEU A 1 397 ? 7.41300   30.94900  8.97400  1.000 14.65000 ? 397 LEU A CD1 1 
ATOM   3110 C  CD2 . LEU A 1 397 ? 6.26300   30.72800  6.76300  1.000 17.76000 ? 397 LEU A CD2 1 
ATOM   3111 N  N   . ARG A 1 398 ? 2.45300   33.17900  10.02200 1.000 19.25000 ? 398 ARG A N   1 
ATOM   3112 C  CA  . ARG A 1 398 ? 1.20900   33.11100  10.77900 1.000 21.11000 ? 398 ARG A CA  1 
ATOM   3113 C  C   . ARG A 1 398 ? 0.02900   33.59700  9.95600  1.000 22.76000 ? 398 ARG A C   1 
ATOM   3114 O  O   . ARG A 1 398 ? -1.09400  33.12200  10.15200 1.000 23.75000 ? 398 ARG A O   1 
ATOM   3115 C  CB  . ARG A 1 398 ? 1.32900   33.91100  12.07800 1.000 23.13000 ? 398 ARG A CB  1 
ATOM   3116 C  CG  . ARG A 1 398 ? 1.99200   33.10700  13.18600 1.000 20.04000 ? 398 ARG A CG  1 
ATOM   3117 C  CD  . ARG A 1 398 ? 2.23300   33.89900  14.45400 1.000 20.49000 ? 398 ARG A CD  1 
ATOM   3118 N  NE  . ARG A 1 398 ? 2.31500   33.01600  15.61400 1.000 20.31000 ? 398 ARG A NE  1 
ATOM   3119 C  CZ  . ARG A 1 398 ? 2.62100   33.42300  16.84200 1.000 17.35000 ? 398 ARG A CZ  1 
ATOM   3120 N  NH1 . ARG A 1 398 ? 2.87000   34.70400  17.06000 1.000 20.61000 ? 398 ARG A NH1 1 
ATOM   3121 N  NH2 . ARG A 1 398 ? 2.66800   32.55300  17.84900 1.000 19.37000 ? 398 ARG A NH2 1 
ATOM   3122 N  N   . ALA A 1 399 ? 0.26800   34.50500  9.00200  1.000 21.73000 ? 399 ALA A N   1 
ATOM   3123 C  CA  . ALA A 1 399 ? -0.80100  34.96400  8.12500  1.000 23.75000 ? 399 ALA A CA  1 
ATOM   3124 C  C   . ALA A 1 399 ? -1.33100  33.85700  7.21900  1.000 28.46000 ? 399 ALA A C   1 
ATOM   3125 O  O   . ALA A 1 399 ? -2.45300  33.98100  6.71500  1.000 26.79000 ? 399 ALA A O   1 
ATOM   3126 C  CB  . ALA A 1 399 ? -0.32300  36.14900  7.28200  1.000 22.25000 ? 399 ALA A CB  1 
ATOM   3127 N  N   . ARG A 1 400 ? -0.55900  32.78800  6.98700  1.000 18.77000 ? 400 ARG A N   1 
ATOM   3128 C  CA  . ARG A 1 400 ? -1.09000  31.65500  6.23500  1.000 20.59000 ? 400 ARG A CA  1 
ATOM   3129 C  C   . ARG A 1 400 ? -1.91200  30.69400  7.08600  1.000 19.20000 ? 400 ARG A C   1 
ATOM   3130 O  O   . ARG A 1 400 ? -2.48000  29.74700  6.53500  1.000 21.23000 ? 400 ARG A O   1 
ATOM   3131 C  CB  . ARG A 1 400 ? 0.03100   30.85300  5.58200  1.000 24.73000 ? 400 ARG A CB  1 
ATOM   3132 C  CG  . ARG A 1 400 ? 0.95900   31.66800  4.72100  1.000 26.87000 ? 400 ARG A CG  1 
ATOM   3133 C  CD  . ARG A 1 400 ? 2.38500   31.35500  5.07100  1.000 33.67000 ? 400 ARG A CD  1 
ATOM   3134 N  NE  . ARG A 1 400 ? 2.88000   30.10300  4.50100  1.000 34.46000 ? 400 ARG A NE  1 
ATOM   3135 C  CZ  . ARG A 1 400 ? 3.90400   30.03400  3.65200  1.000 35.67000 ? 400 ARG A CZ  1 
ATOM   3136 N  NH1 . ARG A 1 400 ? 4.51800   31.14500  3.26500  1.000 38.10000 ? 400 ARG A NH1 1 
ATOM   3137 N  NH2 . ARG A 1 400 ? 4.32000   28.85800  3.19000  1.000 32.29000 ? 400 ARG A NH2 1 
ATOM   3138 N  N   . ALA A 1 401 ? -1.98300  30.89400  8.39900  1.000 21.71000 ? 401 ALA A N   1 
ATOM   3139 C  CA  . ALA A 1 401 ? -2.57000  29.89000  9.28300  1.000 21.15000 ? 401 ALA A CA  1 
ATOM   3140 C  C   . ALA A 1 401 ? -3.62400  30.48300  10.21000 1.000 23.61000 ? 401 ALA A C   1 
ATOM   3141 O  O   . ALA A 1 401 ? -3.85500  29.96100  11.30700 1.000 22.22000 ? 401 ALA A O   1 
ATOM   3142 C  CB  . ALA A 1 401 ? -1.48800  29.19000  10.10500 1.000 18.42000 ? 401 ALA A CB  1 
ATOM   3143 N  N   . THR A 1 402 ? -4.27700  31.56900  9.79500  1.000 21.31000 ? 402 THR A N   1 
ATOM   3144 C  CA  . THR A 1 402 ? -5.30300  32.15400  10.65200 1.000 21.48000 ? 402 THR A CA  1 
ATOM   3145 C  C   . THR A 1 402 ? -6.47800  31.20400  10.85000 1.000 20.99000 ? 402 THR A C   1 
ATOM   3146 O  O   . THR A 1 402 ? -7.25400  31.37900  11.79700 1.000 27.15000 ? 402 THR A O   1 
ATOM   3147 C  CB  . THR A 1 402 ? -5.79800  33.48500  10.06800 1.000 23.78000 ? 402 THR A CB  1 
ATOM   3148 O  OG1 . THR A 1 402 ? -6.35000  33.25600  8.77000  1.000 25.28000 ? 402 THR A OG1 1 
ATOM   3149 C  CG2 . THR A 1 402 ? -4.64800  34.48600  9.92500  1.000 22.67000 ? 402 THR A CG2 1 
ATOM   3150 N  N   . ASP A 1 403 ? -6.62100  30.21000  9.98200  1.000 22.60000 ? 403 ASP A N   1 
ATOM   3151 C  CA  . ASP A 1 403 ? -7.68000  29.21000  10.06100 1.000 22.44000 ? 403 ASP A CA  1 
ATOM   3152 C  C   . ASP A 1 403 ? -7.26900  27.95400  10.81700 1.000 25.21000 ? 403 ASP A C   1 
ATOM   3153 O  O   . ASP A 1 403 ? -8.10100  27.06200  10.99200 1.000 25.48000 ? 403 ASP A O   1 
ATOM   3154 C  CB  . ASP A 1 403 ? -8.13900  28.82000  8.64800  1.000 26.71000 ? 403 ASP A CB  1 
ATOM   3155 C  CG  . ASP A 1 403 ? -7.00700  28.22400  7.79500  1.000 30.17000 ? 403 ASP A CG  1 
ATOM   3156 O  OD1 . ASP A 1 403 ? -5.91800  28.84700  7.67300  1.000 31.55000 ? 403 ASP A OD1 1 
ATOM   3157 O  OD2 . ASP A 1 403 ? -7.20400  27.11800  7.24300  1.000 34.38000 ? 403 ASP A OD2 1 
ATOM   3158 N  N   . VAL A 1 404 ? -6.01900  27.84700  11.26200 1.000 23.94000 ? 404 VAL A N   1 
ATOM   3159 C  CA  . VAL A 1 404 ? -5.57500  26.65300  11.97800 1.000 22.71000 ? 404 VAL A CA  1 
ATOM   3160 C  C   . VAL A 1 404 ? -6.05200  26.73200  13.42500 1.000 20.93000 ? 404 VAL A C   1 
ATOM   3161 O  O   . VAL A 1 404 ? -5.75600  27.69700  14.13600 1.000 22.14000 ? 404 VAL A O   1 
ATOM   3162 C  CB  . VAL A 1 404 ? -4.04900  26.49700  11.90500 1.000 22.07000 ? 404 VAL A CB  1 
ATOM   3163 C  CG1 . VAL A 1 404 ? -3.59500  25.36500  12.83400 1.000 22.08000 ? 404 VAL A CG1 1 
ATOM   3164 C  CG2 . VAL A 1 404 ? -3.61500  26.21000  10.48100 1.000 22.55000 ? 404 VAL A CG2 1 
ATOM   3165 N  N   . ASP A 1 405 ? -6.79100  25.71700  13.86600 1.000 20.98000 ? 405 ASP A N   1 
ATOM   3166 C  CA  . ASP A 1 405 ? -7.26900  25.65800  15.24400 1.000 24.24000 ? 405 ASP A CA  1 
ATOM   3167 C  C   . ASP A 1 405 ? -6.13900  25.15900  16.13800 1.000 21.68000 ? 405 ASP A C   1 
ATOM   3168 O  O   . ASP A 1 405 ? -5.62500  24.05800  15.93000 1.000 23.24000 ? 405 ASP A O   1 
ATOM   3169 C  CB  . ASP A 1 405 ? -8.49500  24.74700  15.32900 1.000 23.77000 ? 405 ASP A CB  1 
ATOM   3170 C  CG  . ASP A 1 405 ? -9.00200  24.53500  16.75600 1.000 25.09000 ? 405 ASP A CG  1 
ATOM   3171 O  OD1 . ASP A 1 405 ? -8.50100  25.16300  17.70500 1.000 29.21000 ? 405 ASP A OD1 1 
ATOM   3172 O  OD2 . ASP A 1 405 ? -9.92800  23.71700  16.92000 1.000 37.65000 ? 405 ASP A OD2 1 
ATOM   3173 N  N   . ILE A 1 406 ? -5.75400  25.96200  17.12800 1.000 20.84000 ? 406 ILE A N   1 
ATOM   3174 C  CA  . ILE A 1 406 ? -4.68300  25.60700  18.05100 1.000 21.40000 ? 406 ILE A CA  1 
ATOM   3175 C  C   . ILE A 1 406 ? -5.19600  25.48800  19.48400 1.000 23.53000 ? 406 ILE A C   1 
ATOM   3176 O  O   . ILE A 1 406 ? -4.40700  25.49100  20.42400 1.000 22.03000 ? 406 ILE A O   1 
ATOM   3177 C  CB  . ILE A 1 406 ? -3.51500  26.61000  17.97100 1.000 22.18000 ? 406 ILE A CB  1 
ATOM   3178 C  CG1 . ILE A 1 406 ? -3.98200  28.01700  18.36700 1.000 23.39000 ? 406 ILE A CG1 1 
ATOM   3179 C  CG2 . ILE A 1 406 ? -2.86700  26.59600  16.58200 1.000 21.01000 ? 406 ILE A CG2 1 
ATOM   3180 C  CD1 . ILE A 1 406 ? -2.88200  29.05400  18.30800 1.000 23.62000 ? 406 ILE A CD1 1 
ATOM   3181 N  N   . SER A 1 407 ? -6.51200  25.39700  19.66400 1.000 23.24000 ? 407 SER A N   1 
ATOM   3182 C  CA  . SER A 1 407 ? -7.06600  25.28800  21.00500 1.000 25.80000 ? 407 SER A CA  1 
ATOM   3183 C  C   . SER A 1 407 ? -6.77000  23.91100  21.59100 1.000 19.89000 ? 407 SER A C   1 
ATOM   3184 O  O   . SER A 1 407 ? -6.45600  22.95800  20.87300 1.000 20.67000 ? 407 SER A O   1 
ATOM   3185 C  CB  . SER A 1 407 ? -8.58100  25.53300  20.98800 1.000 22.92000 ? 407 SER A CB  1 
ATOM   3186 O  OG  . SER A 1 407 ? -9.25300  24.54500  20.22400 1.000 25.32000 ? 407 SER A OG  1 
ATOM   3187 N  N   . GLU A 1 408 ? -6.88500  23.81200  22.91500 1.000 16.84000 ? 408 GLU A N   1 
ATOM   3188 C  CA  . GLU A 1 408 ? -6.69000  22.53100  23.58400 1.000 18.67000 ? 408 GLU A CA  1 
ATOM   3189 C  C   . GLU A 1 408 ? -7.70700  21.51800  23.08200 1.000 22.42000 ? 408 GLU A C   1 
ATOM   3190 O  O   . GLU A 1 408 ? -8.90200  21.81000  22.98700 1.000 20.01000 ? 408 GLU A O   1 
ATOM   3191 C  CB  . GLU A 1 408 ? -6.81400  22.68300  25.10200 1.000 20.38000 ? 408 GLU A CB  1 
ATOM   3192 C  CG  . GLU A 1 408 ? -5.50800  23.01000  25.79500 1.000 24.72000 ? 408 GLU A CG  1 
ATOM   3193 C  CD  . GLU A 1 408 ? -5.57500  22.77300  27.28200 1.000 25.17000 ? 408 GLU A CD  1 
ATOM   3194 O  OE1 . GLU A 1 408 ? -6.66600  22.43100  27.79000 1.000 29.92000 ? 408 GLU A OE1 1 
ATOM   3195 O  OE2 . GLU A 1 408 ? -4.52800  22.90600  27.94300 1.000 29.69000 ? 408 GLU A OE2 1 
ATOM   3196 N  N   . THR A 1 409 ? -7.23000  20.31700  22.77500 1.000 17.21000 ? 409 THR A N   1 
ATOM   3197 C  CA  . THR A 1 409 ? -8.07000  19.26700  22.21400 1.000 16.95000 ? 409 THR A CA  1 
ATOM   3198 C  C   . THR A 1 409 ? -7.69100  17.95200  22.87400 1.000 17.71000 ? 409 THR A C   1 
ATOM   3199 O  O   . THR A 1 409 ? -6.51800  17.55900  22.84400 1.000 16.78000 ? 409 THR A O   1 
ATOM   3200 C  CB  . THR A 1 409 ? -7.90100  19.20000  20.68800 1.000 22.38000 ? 409 THR A CB  1 
ATOM   3201 O  OG1 . THR A 1 409 ? -8.23100  20.46800  20.10800 1.000 19.77000 ? 409 THR A OG1 1 
ATOM   3202 C  CG2 . THR A 1 409 ? -8.79500  18.13800  20.08900 1.000 16.97000 ? 409 THR A CG2 1 
ATOM   3203 N  N   . SER A 1 410 ? -8.67300  17.28700  23.48200 1.000 18.62000 ? 410 SER A N   1 
ATOM   3204 C  CA  . SER A 1 410 ? -8.41700  16.03200  24.17500 1.000 16.76000 ? 410 SER A CA  1 
ATOM   3205 C  C   . SER A 1 410 ? -7.96800  14.96100  23.19100 1.000 17.59000 ? 410 SER A C   1 
ATOM   3206 O  O   . SER A 1 410 ? -8.40800  14.92000  22.03900 1.000 18.21000 ? 410 SER A O   1 
ATOM   3207 C  CB  . SER A 1 410 ? -9.68200  15.55500  24.90700 1.000 15.28000 ? 410 SER A CB  1 
ATOM   3208 O  OG  . SER A 1 410 ? -9.53800  14.20700  25.32400 1.000 18.21000 ? 410 SER A OG  1 
ATOM   3209 N  N   . LYS A 1 411 ? -7.09300  14.06800  23.66100 1.000 16.92000 ? 411 LYS A N   1 
ATOM   3210 C  CA  . LYS A 1 411 ? -6.73100  12.92000  22.83800 1.000 20.69000 ? 411 LYS A CA  1 
ATOM   3211 C  C   . LYS A 1 411 ? -7.95100  12.07000  22.51000 1.000 20.31000 ? 411 LYS A C   1 
ATOM   3212 O  O   . LYS A 1 411 ? -7.96500  11.38300  21.48100 1.000 19.26000 ? 411 LYS A O   1 
ATOM   3213 C  CB  . LYS A 1 411 ? -5.66300  12.08000  23.53700 1.000 21.79000 ? 411 LYS A CB  1 
ATOM   3214 C  CG  . LYS A 1 411 ? -6.17200  11.34600  24.74600 1.000 20.36000 ? 411 LYS A CG  1 
ATOM   3215 C  CD  . LYS A 1 411 ? -5.10700  10.43300  25.31500 1.000 29.75000 ? 411 LYS A CD  1 
ATOM   3216 C  CE  . LYS A 1 411 ? -4.06600  11.19600  26.09100 1.000 24.94000 ? 411 LYS A CE  1 
ATOM   3217 N  NZ  . LYS A 1 411 ? -3.20000  10.26800  26.87600 1.000 29.73000 ? 411 LYS A NZ  1 
ATOM   3218 N  N   . GLU A 1 412 ? -8.99400  12.11700  23.35500 1.000 18.89000 ? 412 GLU A N   1 
ATOM   3219 C  CA  . GLU A 1 412 ? -10.23100 11.41400  23.03200 1.000 20.57000 ? 412 GLU A CA  1 
ATOM   3220 C  C   . GLU A 1 412 ? -10.94600 12.05200  21.85300 1.000 19.30000 ? 412 GLU A C   1 
ATOM   3221 O  O   . GLU A 1 412 ? -11.61800 11.35300  21.08700 1.000 19.20000 ? 412 GLU A O   1 
ATOM   3222 C  CB  . GLU A 1 412 ? -11.16200 11.38000  24.23700 1.000 20.79000 ? 412 GLU A CB  1 
ATOM   3223 C  CG  . GLU A 1 412 ? -10.64300 10.53800  25.38600 1.000 26.77000 ? 412 GLU A CG  1 
ATOM   3224 C  CD  . GLU A 1 412 ? -10.29000 9.11900   24.97000 1.000 35.15000 ? 412 GLU A CD  1 
ATOM   3225 O  OE1 . GLU A 1 412 ? -9.17400  8.67300   25.30300 1.000 36.27000 ? 412 GLU A OE1 1 
ATOM   3226 O  OE2 . GLU A 1 412 ? -11.12900 8.44300   24.32200 1.000 41.77000 ? 412 GLU A OE2 1 
ATOM   3227 N  N   . GLU A 1 413 ? -10.83100 13.37100  21.69100 1.000 17.00000 ? 413 GLU A N   1 
ATOM   3228 C  CA  . GLU A 1 413 ? -11.49000 13.99300  20.55400 1.000 21.21000 ? 413 GLU A CA  1 
ATOM   3229 C  C   . GLU A 1 413 ? -10.71100 13.74300  19.26700 1.000 19.41000 ? 413 GLU A C   1 
ATOM   3230 O  O   . GLU A 1 413 ? -11.31300 13.53200  18.20900 1.000 19.43000 ? 413 GLU A O   1 
ATOM   3231 C  CB  . GLU A 1 413 ? -11.69500 15.48700  20.80900 1.000 17.01000 ? 413 GLU A CB  1 
ATOM   3232 C  CG  . GLU A 1 413 ? -12.09100 16.30200  19.57900 1.000 18.25000 ? 413 GLU A CG  1 
ATOM   3233 C  CD  . GLU A 1 413 ? -13.41400 15.87700  18.94300 1.000 25.21000 ? 413 GLU A CD  1 
ATOM   3234 O  OE1 . GLU A 1 413 ? -14.14500 15.02100  19.51300 1.000 20.69000 ? 413 GLU A OE1 1 
ATOM   3235 O  OE2 . GLU A 1 413 ? -13.71900 16.41300  17.85200 1.000 21.92000 ? 413 GLU A OE2 1 
ATOM   3236 N  N   . TYR A 1 414 ? -9.37700  13.75100  19.33500 1.000 20.63000 ? 414 TYR A N   1 
ATOM   3237 C  CA  . TYR A 1 414 ? -8.59700  13.32400  18.17800 1.000 18.91000 ? 414 TYR A CA  1 
ATOM   3238 C  C   . TYR A 1 414 ? -8.94700  11.89500  17.79100 1.000 17.22000 ? 414 TYR A C   1 
ATOM   3239 O  O   . TYR A 1 414 ? -9.08000  11.58400  16.60500 1.000 17.49000 ? 414 TYR A O   1 
ATOM   3240 C  CB  . TYR A 1 414 ? -7.10100  13.46200  18.45600 1.000 17.01000 ? 414 TYR A CB  1 
ATOM   3241 C  CG  . TYR A 1 414 ? -6.60800  14.89600  18.41300 1.000 13.96000 ? 414 TYR A CG  1 
ATOM   3242 C  CD1 . TYR A 1 414 ? -6.82000  15.69600  17.29300 1.000 16.55000 ? 414 TYR A CD1 1 
ATOM   3243 C  CD2 . TYR A 1 414 ? -5.94900  15.45100  19.49700 1.000 14.40000 ? 414 TYR A CD2 1 
ATOM   3244 C  CE1 . TYR A 1 414 ? -6.37700  17.02600  17.25800 1.000 16.09000 ? 414 TYR A CE1 1 
ATOM   3245 C  CE2 . TYR A 1 414 ? -5.49500  16.76100  19.46700 1.000 15.78000 ? 414 TYR A CE2 1 
ATOM   3246 C  CZ  . TYR A 1 414 ? -5.70800  17.54300  18.35000 1.000 16.67000 ? 414 TYR A CZ  1 
ATOM   3247 O  OH  . TYR A 1 414 ? -5.25400  18.84300  18.35200 1.000 17.98000 ? 414 TYR A OH  1 
ATOM   3248 N  N   . ARG A 1 415 ? -9.13200  11.01900  18.78100 1.000 19.22000 ? 415 ARG A N   1 
ATOM   3249 C  CA  . ARG A 1 415 ? -9.49100  9.63500   18.48300 1.000 20.07000 ? 415 ARG A CA  1 
ATOM   3250 C  C   . ARG A 1 415 ? -10.84300 9.55000   17.78300 1.000 24.48000 ? 415 ARG A C   1 
ATOM   3251 O  O   . ARG A 1 415 ? -11.00300 8.80400   16.81000 1.000 22.13000 ? 415 ARG A O   1 
ATOM   3252 C  CB  . ARG A 1 415 ? -9.49900  8.80500   19.76500 1.000 23.15000 ? 415 ARG A CB  1 
ATOM   3253 C  CG  . ARG A 1 415 ? -10.00600 7.39000   19.55000 1.000 22.00000 ? 415 ARG A CG  1 
ATOM   3254 C  CD  . ARG A 1 415 ? -9.94000  6.56200   20.81700 1.000 23.73000 ? 415 ARG A CD  1 
ATOM   3255 N  NE  . ARG A 1 415 ? -8.58800  6.40200   21.34600 1.000 23.91000 ? 415 ARG A NE  1 
ATOM   3256 C  CZ  . ARG A 1 415 ? -7.73800  5.46400   20.93900 1.000 30.02000 ? 415 ARG A CZ  1 
ATOM   3257 N  NH1 . ARG A 1 415 ? -8.10000  4.61600   19.98400 1.000 27.37000 ? 415 ARG A NH1 1 
ATOM   3258 N  NH2 . ARG A 1 415 ? -6.52800  5.37100   21.47900 1.000 23.78000 ? 415 ARG A NH2 1 
ATOM   3259 N  N   . ARG A 1 416 ? -11.82900 10.31000  18.25700 1.000 21.56000 ? 416 ARG A N   1 
ATOM   3260 C  CA  . ARG A 1 416 ? -13.13300 10.31600  17.60100 1.000 20.93000 ? 416 ARG A CA  1 
ATOM   3261 C  C   . ARG A 1 416 ? -13.01300 10.77400  16.15400 1.000 21.38000 ? 416 ARG A C   1 
ATOM   3262 O  O   . ARG A 1 416 ? -13.58700 10.16100  15.24600 1.000 24.67000 ? 416 ARG A O   1 
ATOM   3263 C  CB  . ARG A 1 416 ? -14.10500 11.21200  18.37000 1.000 18.49000 ? 416 ARG A CB  1 
ATOM   3264 C  CG  . ARG A 1 416 ? -15.51500 11.24200  17.78600 1.000 21.30000 ? 416 ARG A CG  1 
ATOM   3265 C  CD  . ARG A 1 416 ? -16.35300 12.36200  18.40100 1.000 20.07000 ? 416 ARG A CD  1 
ATOM   3266 N  NE  . ARG A 1 416 ? -15.99200 13.67800  17.86800 1.000 21.04000 ? 416 ARG A NE  1 
ATOM   3267 C  CZ  . ARG A 1 416 ? -16.37500 14.14500  16.68800 1.000 21.23000 ? 416 ARG A CZ  1 
ATOM   3268 N  NH1 . ARG A 1 416 ? -17.14600 13.40800  15.89100 1.000 23.39000 ? 416 ARG A NH1 1 
ATOM   3269 N  NH2 . ARG A 1 416 ? -15.97900 15.34500  16.29200 1.000 16.69000 ? 416 ARG A NH2 1 
ATOM   3270 N  N   . ARG A 1 417 ? -12.26400 11.85300  15.91600 1.000 19.85000 ? 417 ARG A N   1 
ATOM   3271 C  CA  . ARG A 1 417 ? -12.05800 12.31600  14.54700 1.000 19.01000 ? 417 ARG A CA  1 
ATOM   3272 C  C   . ARG A 1 417 ? -11.32200 11.26700  13.72900 1.000 24.47000 ? 417 ARG A C   1 
ATOM   3273 O  O   . ARG A 1 417 ? -11.63300 11.05000  12.55200 1.000 24.81000 ? 417 ARG A O   1 
ATOM   3274 C  CB  . ARG A 1 417 ? -11.27200 13.62600  14.53900 1.000 18.72000 ? 417 ARG A CB  1 
ATOM   3275 C  CG  . ARG A 1 417 ? -11.95600 14.78600  15.23600 1.000 19.54000 ? 417 ARG A CG  1 
ATOM   3276 C  CD  . ARG A 1 417 ? -11.01300 15.96300  15.32400 1.000 17.02000 ? 417 ARG A CD  1 
ATOM   3277 N  NE  . ARG A 1 417 ? -11.55600 17.05200  16.13600 1.000 17.72000 ? 417 ARG A NE  1 
ATOM   3278 C  CZ  . ARG A 1 417 ? -10.92000 18.19500  16.34900 1.000 22.37000 ? 417 ARG A CZ  1 
ATOM   3279 N  NH1 . ARG A 1 417 ? -9.72100  18.39800  15.79700 1.000 19.45000 ? 417 ARG A NH1 1 
ATOM   3280 N  NH2 . ARG A 1 417 ? -11.48000 19.13500  17.10100 1.000 23.72000 ? 417 ARG A NH2 1 
ATOM   3281 N  N   . TYR A 1 418 ? -10.33800 10.61200  14.34500 1.000 23.80000 ? 418 TYR A N   1 
ATOM   3282 C  CA  . TYR A 1 418 ? -9.56000  9.58900   13.65700 1.000 20.95000 ? 418 TYR A CA  1 
ATOM   3283 C  C   . TYR A 1 418 ? -10.43800 8.41100   13.26000 1.000 28.20000 ? 418 TYR A C   1 
ATOM   3284 O  O   . TYR A 1 418 ? -10.32200 7.88600   12.14700 1.000 26.61000 ? 418 TYR A O   1 
ATOM   3285 C  CB  . TYR A 1 418 ? -8.42400  9.13200   14.56700 1.000 19.55000 ? 418 TYR A CB  1 
ATOM   3286 C  CG  . TYR A 1 418 ? -7.36300  8.25800   13.93100 1.000 19.81000 ? 418 TYR A CG  1 
ATOM   3287 C  CD1 . TYR A 1 418 ? -6.29200  8.81600   13.25600 1.000 21.27000 ? 418 TYR A CD1 1 
ATOM   3288 C  CD2 . TYR A 1 418 ? -7.41800  6.87600   14.05000 1.000 23.34000 ? 418 TYR A CD2 1 
ATOM   3289 C  CE1 . TYR A 1 418 ? -5.30300  8.01800   12.69400 1.000 21.32000 ? 418 TYR A CE1 1 
ATOM   3290 C  CE2 . TYR A 1 418 ? -6.44900  6.06900   13.50000 1.000 22.67000 ? 418 TYR A CE2 1 
ATOM   3291 C  CZ  . TYR A 1 418 ? -5.38500  6.64200   12.82200 1.000 25.88000 ? 418 TYR A CZ  1 
ATOM   3292 O  OH  . TYR A 1 418 ? -4.40500  5.83600   12.26900 1.000 28.72000 ? 418 TYR A OH  1 
ATOM   3293 N  N   . GLU A 1 419 ? -11.31200 7.97100   14.16900 1.000 25.61000 ? 419 GLU A N   1 
ATOM   3294 C  CA  . GLU A 1 419 ? -12.20500 6.86200   13.85500 1.000 31.68000 ? 419 GLU A CA  1 
ATOM   3295 C  C   . GLU A 1 419 ? -13.20700 7.24700   12.77600 1.000 31.29000 ? 419 GLU A C   1 
ATOM   3296 O  O   . GLU A 1 419 ? -13.59300 6.40400   11.95900 1.000 41.30000 ? 419 GLU A O   1 
ATOM   3297 C  CB  . GLU A 1 419 ? -12.91000 6.38200   15.12800 1.000 28.18000 ? 419 GLU A CB  1 
ATOM   3298 C  CG  . GLU A 1 419 ? -12.08900 5.31700   15.88000 1.000 29.80000 ? 419 GLU A CG  1 
ATOM   3299 C  CD  . GLU A 1 419 ? -12.26400 5.33500   17.39700 1.000 37.43000 ? 419 GLU A CD  1 
ATOM   3300 O  OE1 . GLU A 1 419 ? -13.28700 5.86000   17.89100 1.000 39.47000 ? 419 GLU A OE1 1 
ATOM   3301 O  OE2 . GLU A 1 419 ? -11.36000 4.81700   18.09700 1.000 45.67000 ? 419 GLU A OE2 1 
ATOM   3302 N  N   . LEU A 1 420 ? -13.61300 8.51500   12.73000 1.000 33.76000 ? 420 LEU A N   1 
ATOM   3303 C  CA  . LEU A 1 420 ? -14.48600 8.96400   11.65300 1.000 33.95000 ? 420 LEU A CA  1 
ATOM   3304 C  C   . LEU A 1 420 ? -13.75200 8.95500   10.31800 1.000 41.50000 ? 420 LEU A C   1 
ATOM   3305 O  O   . LEU A 1 420 ? -14.32400 8.57600   9.29000  1.000 43.51000 ? 420 LEU A O   1 
ATOM   3306 C  CB  . LEU A 1 420 ? -15.01500 10.36100  11.96800 1.000 38.56000 ? 420 LEU A CB  1 
ATOM   3307 C  CG  . LEU A 1 420 ? -16.18000 10.87800  11.12800 1.000 47.88000 ? 420 LEU A CG  1 
ATOM   3308 C  CD1 . LEU A 1 420 ? -17.50000 10.60900  11.84100 1.000 43.09000 ? 420 LEU A CD1 1 
ATOM   3309 C  CD2 . LEU A 1 420 ? -16.00000 12.36000  10.82400 1.000 40.01000 ? 420 LEU A CD2 1 
ATOM   3310 N  N   . THR A 1 421 ? -12.47800 9.35500   10.32600 1.000 37.73000 ? 421 THR A N   1 
ATOM   3311 C  CA  . THR A 1 421 ? -11.67700 9.42400   9.10700  1.000 44.93000 ? 421 THR A CA  1 
ATOM   3312 C  C   . THR A 1 421 ? -11.47600 8.04900   8.47000  1.000 45.42000 ? 421 THR A C   1 
ATOM   3313 O  O   . THR A 1 421 ? -11.36600 7.94200   7.24200  1.000 42.13000 ? 421 THR A O   1 
ATOM   3314 C  CB  . THR A 1 421 ? -10.32800 10.07500  9.44000  1.000 39.76000 ? 421 THR A CB  1 
ATOM   3315 O  OG1 . THR A 1 421 ? -10.52100 11.47900  9.65600  1.000 41.29000 ? 421 THR A OG1 1 
ATOM   3316 C  CG2 . THR A 1 421 ? -9.30400  9.86400   8.33800  1.000 39.48000 ? 421 THR A CG2 1 
ATOM   3317 N  N   . HIS A 1 422 ? -11.45900 6.98700   9.27400  1.000 44.12000 ? 422 HIS A N   1 
ATOM   3318 C  CA  . HIS A 1 422 ? -11.00100 5.68100   8.82300  1.000 45.84000 ? 422 HIS A CA  1 
ATOM   3319 C  C   . HIS A 1 422 ? -12.11400 4.64200   8.77100  1.000 46.53000 ? 422 HIS A C   1 
ATOM   3320 O  O   . HIS A 1 422 ? -11.86300 3.44800   8.94700  1.000 48.99000 ? 422 HIS A O   1 
ATOM   3321 C  CB  . HIS A 1 422 ? -9.85900  5.21200   9.71300  1.000 42.47000 ? 422 HIS A CB  1 
ATOM   3322 C  CG  . HIS A 1 422 ? -8.58900  5.95000   9.46100  1.000 43.21000 ? 422 HIS A CG  1 
ATOM   3323 N  ND1 . HIS A 1 422 ? -7.71000  6.29600   10.46200 1.000 44.34000 ? 422 HIS A ND1 1 
ATOM   3324 C  CD2 . HIS A 1 422 ? -8.06000  6.43200   8.31200  1.000 47.60000 ? 422 HIS A CD2 1 
ATOM   3325 C  CE1 . HIS A 1 422 ? -6.68800  6.95100   9.94200  1.000 42.27000 ? 422 HIS A CE1 1 
ATOM   3326 N  NE2 . HIS A 1 422 ? -6.87400  7.04400   8.63800  1.000 43.08000 ? 422 HIS A NE2 1 
ATOM   3327 N  N   . SER A 1 423 ? -13.33900 5.07900   8.51300  1.000 51.88000 ? 423 SER A N   1 
ATOM   3328 C  CA  . SER A 1 423 ? -14.46200 4.16200   8.36800  1.000 59.98000 ? 423 SER A CA  1 
ATOM   3329 C  C   . SER A 1 423 ? -15.24500 4.48600   7.09900  1.000 62.29000 ? 423 SER A C   1 
ATOM   3330 O  O   . SER A 1 423 ? -16.39700 4.07500   6.94900  1.000 63.79000 ? 423 SER A O   1 
ATOM   3331 C  CB  . SER A 1 423 ? -15.37600 4.22600   9.59400  1.000 56.81000 ? 423 SER A CB  1 
ATOM   3332 O  OG  . SER A 1 423 ? -15.95700 5.51300   9.73700  1.000 48.68000 ? 423 SER A OG  1 
ATOM   3333 O  OXT . SER A 1 423 ? -14.73900 5.16800   6.20100  1.000 58.66000 ? 423 SER A OXT 1 
ATOM   3334 N  N   . MET B 1 1   ? 37.76300  48.41200  46.75600 1.000 35.04000 ? 1   MET B N   1 
ATOM   3335 C  CA  . MET B 1 1   ? 38.41000  47.61600  47.79000 1.000 25.14000 ? 1   MET B CA  1 
ATOM   3336 C  C   . MET B 1 1   ? 39.72700  47.04700  47.27700 1.000 23.63000 ? 1   MET B C   1 
ATOM   3337 O  O   . MET B 1 1   ? 39.81300  46.60600  46.14400 1.000 23.74000 ? 1   MET B O   1 
ATOM   3338 C  CB  . MET B 1 1   ? 37.48800  46.48100  48.25600 1.000 30.89000 ? 1   MET B CB  1 
ATOM   3339 C  CG  . MET B 1 1   ? 38.08700  45.63500  49.36200 1.000 33.16000 ? 1   MET B CG  1 
ATOM   3340 S  SD  . MET B 1 1   ? 37.01900  44.31300  49.97600 1.000 32.26000 ? 1   MET B SD  1 
ATOM   3341 C  CE  . MET B 1 1   ? 35.40900  45.07300  49.77900 1.000 22.03000 ? 1   MET B CE  1 
ATOM   3342 N  N   . LYS B 1 2   ? 40.75900  47.07200  48.10700 1.000 22.94000 ? 2   LYS B N   1 
ATOM   3343 C  CA  . LYS B 1 2   ? 42.00700  46.42000  47.74800 1.000 28.13000 ? 2   LYS B CA  1 
ATOM   3344 C  C   . LYS B 1 2   ? 41.98800  44.95700  48.18600 1.000 25.16000 ? 2   LYS B C   1 
ATOM   3345 O  O   . LYS B 1 2   ? 41.26100  44.56400  49.09900 1.000 23.33000 ? 2   LYS B O   1 
ATOM   3346 C  CB  . LYS B 1 2   ? 43.20000  47.13500  48.38200 1.000 27.19000 ? 2   LYS B CB  1 
ATOM   3347 N  N   . THR B 1 3   ? 42.82100  44.15900  47.52200 1.000 21.78000 ? 3   THR B N   1 
ATOM   3348 C  CA  . THR B 1 3   ? 42.94800  42.74400  47.85400 1.000 22.49000 ? 3   THR B CA  1 
ATOM   3349 C  C   . THR B 1 3   ? 43.22200  42.52900  49.34000 1.000 22.66000 ? 3   THR B C   1 
ATOM   3350 O  O   . THR B 1 3   ? 42.61800  41.65500  49.97300 1.000 23.92000 ? 3   THR B O   1 
ATOM   3351 C  CB  . THR B 1 3   ? 44.06400  42.13500  47.00400 1.000 18.22000 ? 3   THR B CB  1 
ATOM   3352 O  OG1 . THR B 1 3   ? 43.71100  42.23300  45.62300 1.000 21.73000 ? 3   THR B OG1 1 
ATOM   3353 C  CG2 . THR B 1 3   ? 44.30000  40.65600  47.35800 1.000 21.95000 ? 3   THR B CG2 1 
ATOM   3354 N  N   . GLU B 1 4   ? 44.16000  43.25500  49.80100 1.000 22.75000 ? 4   GLU B N   1 
ATOM   3355 C  CA  A GLU B 1 4   ? 44.51000  43.13200  51.31300 0.494 23.29000 ? 4   GLU B CA  1 
ATOM   3356 C  CA  B GLU B 1 4   ? 44.48400  43.16500  51.20300 0.506 23.31000 ? 4   GLU B CA  1 
ATOM   3357 C  C   . GLU B 1 4   ? 43.34400  43.36500  52.33000 1.000 20.48000 ? 4   GLU B C   1 
ATOM   3358 O  O   . GLU B 1 4   ? 43.38700  43.02100  53.54300 1.000 22.88000 ? 4   GLU B O   1 
ATOM   3359 C  CB  A GLU B 1 4   ? 45.62700  44.09000  51.73000 0.494 23.65000 ? 4   GLU B CB  1 
ATOM   3360 C  CB  B GLU B 1 4   ? 45.62200  44.10300  51.58500 0.506 23.67000 ? 4   GLU B CB  1 
ATOM   3361 C  CG  A GLU B 1 4   ? 46.75500  44.21600  50.75600 0.494 30.35000 ? 4   GLU B CG  1 
ATOM   3362 C  CG  B GLU B 1 4   ? 46.37000  44.71300  50.42900 0.506 30.83000 ? 4   GLU B CG  1 
ATOM   3363 C  CD  A GLU B 1 4   ? 46.49800  45.31900  49.76300 0.494 29.89000 ? 4   GLU B CD  1 
ATOM   3364 C  CD  B GLU B 1 4   ? 46.76500  46.13800  50.71000 0.506 29.72000 ? 4   GLU B CD  1 
ATOM   3365 O  OE1 A GLU B 1 4   ? 45.93700  45.01100  48.67400 0.494 22.30000 ? 4   GLU B OE1 1 
ATOM   3366 O  OE1 B GLU B 1 4   ? 46.96600  46.86400  49.74600 0.506 31.10000 ? 4   GLU B OE1 1 
ATOM   3367 O  OE2 A GLU B 1 4   ? 46.83200  46.48600  50.09400 0.494 30.72000 ? 4   GLU B OE2 1 
ATOM   3368 O  OE2 B GLU B 1 4   ? 46.83800  46.51700  51.89600 0.506 25.23000 ? 4   GLU B OE2 1 
ATOM   3369 N  N   . ASP B 1 5   ? 42.30500  44.03900  51.84400 1.000 20.69000 ? 5   ASP B N   1 
ATOM   3370 C  CA  . ASP B 1 5   ? 41.23400  44.37200  52.77200 1.000 21.46000 ? 5   ASP B CA  1 
ATOM   3371 C  C   . ASP B 1 5   ? 40.07100  43.38900  52.73300 1.000 24.49000 ? 5   ASP B C   1 
ATOM   3372 O  O   . ASP B 1 5   ? 39.13500  43.53100  53.52500 1.000 21.46000 ? 5   ASP B O   1 
ATOM   3373 C  CB  . ASP B 1 5   ? 40.72400  45.78400  52.50400 1.000 22.32000 ? 5   ASP B CB  1 
ATOM   3374 C  CG  . ASP B 1 5   ? 41.74500  46.84300  52.87100 1.000 27.62000 ? 5   ASP B CG  1 
ATOM   3375 O  OD1 . ASP B 1 5   ? 42.39700  46.72900  53.94200 1.000 31.01000 ? 5   ASP B OD1 1 
ATOM   3376 O  OD2 . ASP B 1 5   ? 41.89400  47.78500  52.08100 1.000 34.45000 ? 5   ASP B OD2 1 
ATOM   3377 N  N   . MET B 1 6   ? 40.10200  42.39900  51.84600 1.000 19.87000 ? 6   MET B N   1 
ATOM   3378 C  CA  . MET B 1 6   ? 39.07300  41.36600  51.88300 1.000 19.19000 ? 6   MET B CA  1 
ATOM   3379 C  C   . MET B 1 6   ? 39.17200  40.57500  53.18100 1.000 18.13000 ? 6   MET B C   1 
ATOM   3380 O  O   . MET B 1 6   ? 40.21700  40.52600  53.83000 1.000 18.70000 ? 6   MET B O   1 
ATOM   3381 C  CB  . MET B 1 6   ? 39.19700  40.43200  50.67100 1.000 17.30000 ? 6   MET B CB  1 
ATOM   3382 C  CG  . MET B 1 6   ? 38.91400  41.11700  49.34000 1.000 21.56000 ? 6   MET B CG  1 
ATOM   3383 S  SD  . MET B 1 6   ? 38.86800  39.95300  47.97100 1.000 30.22000 ? 6   MET B SD  1 
ATOM   3384 C  CE  . MET B 1 6   ? 40.55600  39.41200  47.95500 1.000 19.33000 ? 6   MET B CE  1 
ATOM   3385 N  N   . VAL B 1 7   ? 38.05200  39.99800  53.58900 1.000 18.87000 ? 7   VAL B N   1 
ATOM   3386 C  CA  . VAL B 1 7   ? 38.01400  38.99700  54.64500 1.000 18.87000 ? 7   VAL B CA  1 
ATOM   3387 C  C   . VAL B 1 7   ? 37.51400  37.71500  53.99600 1.000 19.94000 ? 7   VAL B C   1 
ATOM   3388 O  O   . VAL B 1 7   ? 36.46700  37.72400  53.33800 1.000 18.75000 ? 7   VAL B O   1 
ATOM   3389 C  CB  . VAL B 1 7   ? 37.09800  39.42100  55.80900 1.000 22.17000 ? 7   VAL B CB  1 
ATOM   3390 C  CG1 . VAL B 1 7   ? 37.06500  38.34200  56.88400 1.000 18.01000 ? 7   VAL B CG1 1 
ATOM   3391 C  CG2 . VAL B 1 7   ? 37.55900  40.76200  56.39900 1.000 22.79000 ? 7   VAL B CG2 1 
ATOM   3392 N  N   . MET B 1 8   ? 38.26900  36.63200  54.14000 1.000 16.27000 ? 8   MET B N   1 
ATOM   3393 C  CA  . MET B 1 8   ? 37.97700  35.40800  53.40700 1.000 15.77000 ? 8   MET B CA  1 
ATOM   3394 C  C   . MET B 1 8   ? 37.75500  34.25200  54.37100 1.000 17.52000 ? 8   MET B C   1 
ATOM   3395 O  O   . MET B 1 8   ? 38.66700  33.85500  55.10800 1.000 17.76000 ? 8   MET B O   1 
ATOM   3396 C  CB  . MET B 1 8   ? 39.09000  35.09200  52.41200 1.000 16.80000 ? 8   MET B CB  1 
ATOM   3397 C  CG  . MET B 1 8   ? 39.33200  36.20400  51.38600 1.000 16.69000 ? 8   MET B CG  1 
ATOM   3398 S  SD  . MET B 1 8   ? 40.58100  35.73100  50.19300 1.000 17.86000 ? 8   MET B SD  1 
ATOM   3399 C  CE  . MET B 1 8   ? 39.59500  34.84300  48.98800 1.000 19.34000 ? 8   MET B CE  1 
ATOM   3400 N  N   . ILE B 1 9   ? 36.53700  33.71700  54.34800 1.000 15.07000 ? 9   ILE B N   1 
ATOM   3401 C  CA  . ILE B 1 9   ? 36.16600  32.47100  55.01400 1.000 14.25000 ? 9   ILE B CA  1 
ATOM   3402 C  C   . ILE B 1 9   ? 35.97200  31.40500  53.94400 1.000 13.90000 ? 9   ILE B C   1 
ATOM   3403 O  O   . ILE B 1 9   ? 35.28500  31.64500  52.94700 1.000 15.57000 ? 9   ILE B O   1 
ATOM   3404 C  CB  . ILE B 1 9   ? 34.86700  32.65300  55.82000 1.000 20.13000 ? 9   ILE B CB  1 
ATOM   3405 C  CG1 . ILE B 1 9   ? 35.09400  33.49200  57.07800 1.000 20.97000 ? 9   ILE B CG1 1 
ATOM   3406 C  CG2 . ILE B 1 9   ? 34.20600  31.29900  56.13100 1.000 19.57000 ? 9   ILE B CG2 1 
ATOM   3407 C  CD1 . ILE B 1 9   ? 33.77300  33.88300  57.74600 1.000 22.69000 ? 9   ILE B CD1 1 
ATOM   3408 N  N   . SER B 1 10  ? 36.55500  30.22700  54.14600 1.000 16.08000 ? 10  SER B N   1 
ATOM   3409 C  CA  . SER B 1 10  ? 36.33100  29.09000  53.25800 1.000 14.39000 ? 10  SER B CA  1 
ATOM   3410 C  C   . SER B 1 10  ? 35.37000  28.11200  53.92700 1.000 14.97000 ? 10  SER B C   1 
ATOM   3411 O  O   . SER B 1 10  ? 35.62600  27.66300  55.04900 1.000 13.77000 ? 10  SER B O   1 
ATOM   3412 C  CB  . SER B 1 10  ? 37.65100  28.38700  52.92900 1.000 15.36000 ? 10  SER B CB  1 
ATOM   3413 O  OG  . SER B 1 10  ? 37.41800  27.13700  52.30500 1.000 12.50000 ? 10  SER B OG  1 
ATOM   3414 N  N   . ILE B 1 11  ? 34.27700  27.76600  53.25100 1.000 15.67000 ? 11  ILE B N   1 
ATOM   3415 C  CA  . ILE B 1 11  ? 33.35100  26.77100  53.80600 1.000 14.27000 ? 11  ILE B CA  1 
ATOM   3416 C  C   . ILE B 1 11  ? 33.58800  25.37700  53.21200 1.000 14.01000 ? 11  ILE B C   1 
ATOM   3417 O  O   . ILE B 1 11  ? 32.74400  24.49900  53.34200 1.000 14.08000 ? 11  ILE B O   1 
ATOM   3418 C  CB  . ILE B 1 11  ? 31.87800  27.20100  53.67900 1.000 20.85000 ? 11  ILE B CB  1 
ATOM   3419 C  CG1 . ILE B 1 11  ? 31.55100  27.69000  52.27700 1.000 18.08000 ? 11  ILE B CG1 1 
ATOM   3420 C  CG2 . ILE B 1 11  ? 31.51800  28.25800  54.75000 1.000 22.22000 ? 11  ILE B CG2 1 
ATOM   3421 C  CD1 . ILE B 1 11  ? 31.29700  26.57700  51.33100 1.000 20.85000 ? 11  ILE B CD1 1 
ATOM   3422 N  N   . ASP B 1 12  ? 34.75500  25.14200  52.61700 1.000 16.46000 ? 12  ASP B N   1 
ATOM   3423 C  CA  . ASP B 1 12  ? 35.10600  23.79700  52.16500 1.000 10.74000 ? 12  ASP B CA  1 
ATOM   3424 C  C   . ASP B 1 12  ? 36.62000  23.69300  52.08400 1.000 14.37000 ? 12  ASP B C   1 
ATOM   3425 O  O   . ASP B 1 12  ? 37.23300  24.29200  51.19600 1.000 13.20000 ? 12  ASP B O   1 
ATOM   3426 C  CB  . ASP B 1 12  ? 34.47000  23.48100  50.81900 1.000 12.66000 ? 12  ASP B CB  1 
ATOM   3427 C  CG  . ASP B 1 12  ? 35.01400  22.19500  50.20600 1.000 11.90000 ? 12  ASP B CG  1 
ATOM   3428 O  OD1 . ASP B 1 12  ? 35.52100  21.33700  50.95000 1.000 12.50000 ? 12  ASP B OD1 1 
ATOM   3429 O  OD2 . ASP B 1 12  ? 34.92100  22.02300  48.97600 1.000 13.93000 ? 12  ASP B OD2 1 
ATOM   3430 N  N   . ASP B 1 13  ? 37.20200  22.91800  52.99800 1.000 12.77000 ? 13  ASP B N   1 
ATOM   3431 C  CA  . ASP B 1 13  ? 38.59200  22.48600  52.95700 1.000 13.56000 ? 13  ASP B CA  1 
ATOM   3432 C  C   . ASP B 1 13  ? 38.63900  21.04000  53.42800 1.000 12.81000 ? 13  ASP B C   1 
ATOM   3433 O  O   . ASP B 1 13  ? 37.61600  20.45400  53.77500 1.000 13.95000 ? 13  ASP B O   1 
ATOM   3434 C  CB  . ASP B 1 13  ? 39.47200  23.37900  53.83200 1.000 15.91000 ? 13  ASP B CB  1 
ATOM   3435 C  CG  . ASP B 1 13  ? 39.36900  24.83500  53.45300 1.000 15.81000 ? 13  ASP B CG  1 
ATOM   3436 O  OD1 . ASP B 1 13  ? 38.44900  25.50800  53.97200 1.000 17.38000 ? 13  ASP B OD1 1 
ATOM   3437 O  OD2 . ASP B 1 13  ? 40.20200  25.28600  52.62300 1.000 16.30000 ? 13  ASP B OD2 1 
ATOM   3438 N  N   . HIS B 1 14  ? 39.83100  20.45500  53.46600 1.000 11.03000 ? 14  HIS B N   1 
ATOM   3439 C  CA  . HIS B 1 14  ? 39.96500  19.05800  53.84300 1.000 11.68000 ? 14  HIS B CA  1 
ATOM   3440 C  C   . HIS B 1 14  ? 41.08700  18.91600  54.84700 1.000 13.65000 ? 14  HIS B C   1 
ATOM   3441 O  O   . HIS B 1 14  ? 42.05000  19.67800  54.81700 1.000 15.73000 ? 14  HIS B O   1 
ATOM   3442 C  CB  . HIS B 1 14  ? 40.20900  18.20300  52.61600 1.000 12.54000 ? 14  HIS B CB  1 
ATOM   3443 C  CG  . HIS B 1 14  ? 39.06200  18.24800  51.66000 1.000 15.84000 ? 14  HIS B CG  1 
ATOM   3444 N  ND1 . HIS B 1 14  ? 38.08700  17.27600  51.62300 1.000 12.59000 ? 14  HIS B ND1 1 
ATOM   3445 C  CD2 . HIS B 1 14  ? 38.69300  19.19000  50.76400 1.000 14.64000 ? 14  HIS B CD2 1 
ATOM   3446 C  CE1 . HIS B 1 14  ? 37.18300  17.60100  50.71800 1.000 15.27000 ? 14  HIS B CE1 1 
ATOM   3447 N  NE2 . HIS B 1 14  ? 37.52000  18.76700  50.19200 1.000 15.76000 ? 14  HIS B NE2 1 
ATOM   3448 N  N   . VAL B 1 15  ? 40.94600  17.94800  55.75000 1.000 13.10000 ? 15  VAL B N   1 
ATOM   3449 C  CA  . VAL B 1 15  ? 41.97900  17.68000  56.73800 1.000 15.83000 ? 15  VAL B CA  1 
ATOM   3450 C  C   . VAL B 1 15  ? 42.46700  16.24200  56.59900 1.000 18.45000 ? 15  VAL B C   1 
ATOM   3451 O  O   . VAL B 1 15  ? 41.68700  15.32000  56.33400 1.000 18.32000 ? 15  VAL B O   1 
ATOM   3452 C  CB  . VAL B 1 15  ? 41.49200  17.97900  58.17400 1.000 17.82000 ? 15  VAL B CB  1 
ATOM   3453 C  CG1 . VAL B 1 15  ? 40.32400  17.08500  58.57500 1.000 17.55000 ? 15  VAL B CG1 1 
ATOM   3454 C  CG2 . VAL B 1 15  ? 42.66200  17.86200  59.15800 1.000 18.34000 ? 15  VAL B CG2 1 
ATOM   3455 N  N   . VAL B 1 16  ? 43.77000  16.06100  56.75800 1.000 15.36000 ? 16  VAL B N   1 
ATOM   3456 C  CA  . VAL B 1 16  ? 44.36700  14.74000  56.88500 1.000 12.95000 ? 16  VAL B CA  1 
ATOM   3457 C  C   . VAL B 1 16  ? 44.57100  14.51100  58.37900 1.000 15.56000 ? 16  VAL B C   1 
ATOM   3458 O  O   . VAL B 1 16  ? 45.37500  15.20100  59.01600 1.000 14.47000 ? 16  VAL B O   1 
ATOM   3459 C  CB  . VAL B 1 16  ? 45.68400  14.64200  56.10000 1.000 15.39000 ? 16  VAL B CB  1 
ATOM   3460 C  CG1 . VAL B 1 16  ? 46.41100  13.34600  56.42900 1.000 20.35000 ? 16  VAL B CG1 1 
ATOM   3461 C  CG2 . VAL B 1 16  ? 45.41600  14.72900  54.60700 1.000 15.27000 ? 16  VAL B CG2 1 
ATOM   3462 N  N   . GLU B 1 17  ? 43.83100  13.56800  58.95700 1.000 14.98000 ? 17  GLU B N   1 
ATOM   3463 C  CA  . GLU B 1 17  ? 43.87200  13.39800  60.40100 1.000 15.65000 ? 17  GLU B CA  1 
ATOM   3464 C  C   . GLU B 1 17  ? 45.26700  12.94600  60.82600 1.000 14.97000 ? 17  GLU B C   1 
ATOM   3465 O  O   . GLU B 1 17  ? 45.85900  12.08500  60.17400 1.000 17.37000 ? 17  GLU B O   1 
ATOM   3466 C  CB  . GLU B 1 17  ? 42.82100  12.38400  60.86100 1.000 12.36000 ? 17  GLU B CB  1 
ATOM   3467 C  CG  . GLU B 1 17  ? 41.36200  12.80200  60.54800 1.000 13.57000 ? 17  GLU B CG  1 
ATOM   3468 C  CD  . GLU B 1 17  ? 40.93100  12.43700  59.12200 1.000 16.92000 ? 17  GLU B CD  1 
ATOM   3469 O  OE1 . GLU B 1 17  ? 41.68000  11.71300  58.42000 1.000 18.04000 ? 17  GLU B OE1 1 
ATOM   3470 O  OE2 . GLU B 1 17  ? 39.84300  12.87500  58.70400 1.000 17.12000 ? 17  GLU B OE2 1 
ATOM   3471 N  N   . PRO B 1 18  ? 45.81100  13.49700  61.90600 1.000 16.75000 ? 18  PRO B N   1 
ATOM   3472 C  CA  . PRO B 1 18  ? 47.17600  13.15300  62.32100 1.000 19.25000 ? 18  PRO B CA  1 
ATOM   3473 C  C   . PRO B 1 18  ? 47.23200  11.78400  62.98800 1.000 19.54000 ? 18  PRO B C   1 
ATOM   3474 O  O   . PRO B 1 18  ? 46.21500  11.16300  63.30400 1.000 15.82000 ? 18  PRO B O   1 
ATOM   3475 C  CB  . PRO B 1 18  ? 47.54100  14.26600  63.31000 1.000 19.75000 ? 18  PRO B CB  1 
ATOM   3476 C  CG  . PRO B 1 18  ? 46.22400  14.70200  63.86900 1.000 20.35000 ? 18  PRO B CG  1 
ATOM   3477 C  CD  . PRO B 1 18  ? 45.21800  14.53700  62.75400 1.000 18.72000 ? 18  PRO B CD  1 
ATOM   3478 N  N   . ALA B 1 19  ? 48.46700  11.32900  63.20900 1.000 19.32000 ? 19  ALA B N   1 
ATOM   3479 C  CA  . ALA B 1 19  ? 48.70300  9.95000   63.61800 1.000 17.78000 ? 19  ALA B CA  1 
ATOM   3480 C  C   . ALA B 1 19  ? 48.12400  9.63100   64.99200 1.000 18.67000 ? 19  ALA B C   1 
ATOM   3481 O  O   . ALA B 1 19  ? 47.84800  8.46300   65.28400 1.000 18.55000 ? 19  ALA B O   1 
ATOM   3482 C  CB  . ALA B 1 19  ? 50.20400  9.66100   63.60700 1.000 20.05000 ? 19  ALA B CB  1 
ATOM   3483 N  N   . ASP B 1 20  ? 47.95500  10.63000  65.85700 1.000 20.51000 ? 20  ASP B N   1 
ATOM   3484 C  CA  . ASP B 1 20  ? 47.55200  10.38700  67.23900 1.000 19.56000 ? 20  ASP B CA  1 
ATOM   3485 C  C   . ASP B 1 20  ? 46.05800  10.59200  67.47500 1.000 22.22000 ? 20  ASP B C   1 
ATOM   3486 O  O   . ASP B 1 20  ? 45.62000  10.60200  68.63000 1.000 20.17000 ? 20  ASP B O   1 
ATOM   3487 C  CB  . ASP B 1 20  ? 48.35500  11.27900  68.19400 1.000 16.57000 ? 20  ASP B CB  1 
ATOM   3488 C  CG  . ASP B 1 20  ? 48.21100  12.76600  67.88900 1.000 25.50000 ? 20  ASP B CG  1 
ATOM   3489 O  OD1 . ASP B 1 20  ? 47.50200  13.12900  66.93100 1.000 24.05000 ? 20  ASP B OD1 1 
ATOM   3490 O  OD2 . ASP B 1 20  ? 48.83200  13.58000  68.60100 1.000 24.91000 ? 20  ASP B OD2 1 
ATOM   3491 N  N   . ILE B 1 21  ? 45.26200  10.74100  66.41600 1.000 20.68000 ? 21  ILE B N   1 
ATOM   3492 C  CA  . ILE B 1 21  ? 43.86900  11.13100  66.61600 1.000 18.63000 ? 21  ILE B CA  1 
ATOM   3493 C  C   . ILE B 1 21  ? 43.12000  10.06600  67.41000 1.000 18.65000 ? 21  ILE B C   1 
ATOM   3494 O  O   . ILE B 1 21  ? 42.36700  10.38100  68.33800 1.000 17.37000 ? 21  ILE B O   1 
ATOM   3495 C  CB  . ILE B 1 21  ? 43.18500  11.44200  65.26800 1.000 15.92000 ? 21  ILE B CB  1 
ATOM   3496 C  CG1 . ILE B 1 21  ? 41.74300  11.89900  65.49800 1.000 16.75000 ? 21  ILE B CG1 1 
ATOM   3497 C  CG2 . ILE B 1 21  ? 43.25500  10.25200  64.29800 1.000 17.93000 ? 21  ILE B CG2 1 
ATOM   3498 C  CD1 . ILE B 1 21  ? 40.97200  12.11800  64.22200 1.000 20.02000 ? 21  ILE B CD1 1 
ATOM   3499 N  N   . PHE B 1 22  ? 43.34600  8.79200   67.09800 1.000 19.10000 ? 22  PHE B N   1 
ATOM   3500 C  CA  . PHE B 1 22  ? 42.59100  7.75200   67.77800 1.000 19.37000 ? 22  PHE B CA  1 
ATOM   3501 C  C   . PHE B 1 22  ? 43.22800  7.35300   69.10100 1.000 24.01000 ? 22  PHE B C   1 
ATOM   3502 O  O   . PHE B 1 22  ? 42.50700  6.99200   70.04300 1.000 19.74000 ? 22  PHE B O   1 
ATOM   3503 C  CB  . PHE B 1 22  ? 42.41000  6.56400   66.83800 1.000 19.19000 ? 22  PHE B CB  1 
ATOM   3504 C  CG  . PHE B 1 22  ? 41.60300  6.90800   65.61600 1.000 20.32000 ? 22  PHE B CG  1 
ATOM   3505 C  CD1 . PHE B 1 22  ? 40.26900  7.28300   65.74200 1.000 19.56000 ? 22  PHE B CD1 1 
ATOM   3506 C  CD2 . PHE B 1 22  ? 42.18000  6.91500   64.35600 1.000 20.11000 ? 22  PHE B CD2 1 
ATOM   3507 C  CE1 . PHE B 1 22  ? 39.51200  7.62500   64.62200 1.000 19.34000 ? 22  PHE B CE1 1 
ATOM   3508 C  CE2 . PHE B 1 22  ? 41.43100  7.26600   63.23100 1.000 17.55000 ? 22  PHE B CE2 1 
ATOM   3509 C  CZ  . PHE B 1 22  ? 40.10200  7.62300   63.36500 1.000 19.00000 ? 22  PHE B CZ  1 
ATOM   3510 N  N   . GLU B 1 23  ? 44.55600  7.45800   69.20600 1.000 22.85000 ? 23  GLU B N   1 
ATOM   3511 C  CA  . GLU B 1 23  ? 45.20700  7.34900   70.50600 1.000 22.89000 ? 23  GLU B CA  1 
ATOM   3512 C  C   . GLU B 1 23  ? 44.59900  8.32700   71.50400 1.000 23.61000 ? 23  GLU B C   1 
ATOM   3513 O  O   . GLU B 1 23  ? 44.40500  7.99100   72.67800 1.000 23.73000 ? 23  GLU B O   1 
ATOM   3514 C  CB  . GLU B 1 23  ? 46.71700  7.58100   70.35300 1.000 22.98000 ? 23  GLU B CB  1 
ATOM   3515 C  CG  . GLU B 1 23  ? 47.40900  6.49300   69.54200 1.000 26.18000 ? 23  GLU B CG  1 
ATOM   3516 C  CD  . GLU B 1 23  ? 48.81100  6.87200   69.05300 1.000 28.02000 ? 23  GLU B CD  1 
ATOM   3517 O  OE1 . GLU B 1 23  ? 49.24500  8.03200   69.23700 1.000 27.82000 ? 23  GLU B OE1 1 
ATOM   3518 O  OE2 . GLU B 1 23  ? 49.47900  5.99100   68.47300 1.000 28.21000 ? 23  GLU B OE2 1 
ATOM   3519 N  N   . LYS B 1 24  ? 44.25700  9.53400   71.04800 1.000 21.17000 ? 24  LYS B N   1 
ATOM   3520 C  CA  . LYS B 1 24  ? 43.70800  10.53900  71.95100 1.000 16.64000 ? 24  LYS B CA  1 
ATOM   3521 C  C   . LYS B 1 24  ? 42.20000  10.40100  72.14300 1.000 20.27000 ? 24  LYS B C   1 
ATOM   3522 O  O   . LYS B 1 24  ? 41.69700  10.73200  73.22000 1.000 23.03000 ? 24  LYS B O   1 
ATOM   3523 C  CB  . LYS B 1 24  ? 44.03700  11.94900  71.44000 1.000 22.50000 ? 24  LYS B CB  1 
ATOM   3524 C  CG  . LYS B 1 24  ? 45.53200  12.26300  71.44300 1.000 20.91000 ? 24  LYS B CG  1 
ATOM   3525 C  CD  . LYS B 1 24  ? 45.91900  13.33400  70.43100 1.000 26.05000 ? 24  LYS B CD  1 
ATOM   3526 C  CE  . LYS B 1 24  ? 45.32900  14.68400  70.77300 1.000 27.54000 ? 24  LYS B CE  1 
ATOM   3527 N  NZ  . LYS B 1 24  ? 45.95800  15.75900  69.95000 1.000 28.49000 ? 24  LYS B NZ  1 
ATOM   3528 N  N   . HIS B 1 25  ? 41.45500  9.92100   71.14000 1.000 20.88000 ? 25  HIS B N   1 
ATOM   3529 C  CA  . HIS B 1 25  ? 39.99900  10.04600  71.18900 1.000 21.63000 ? 25  HIS B CA  1 
ATOM   3530 C  C   . HIS B 1 25  ? 39.20100  8.75000   71.07400 1.000 21.29000 ? 25  HIS B C   1 
ATOM   3531 O  O   . HIS B 1 25  ? 38.00500  8.76800   71.37800 1.000 21.02000 ? 25  HIS B O   1 
ATOM   3532 C  CB  . HIS B 1 25  ? 39.51600  11.02000  70.10100 1.000 18.37000 ? 25  HIS B CB  1 
ATOM   3533 C  CG  . HIS B 1 25  ? 39.95400  12.43000  70.34500 1.000 18.80000 ? 25  HIS B CG  1 
ATOM   3534 N  ND1 . HIS B 1 25  ? 39.36500  13.23600  71.29600 1.000 21.39000 ? 25  HIS B ND1 1 
ATOM   3535 C  CD2 . HIS B 1 25  ? 40.95400  13.16200  69.79800 1.000 20.18000 ? 25  HIS B CD2 1 
ATOM   3536 C  CE1 . HIS B 1 25  ? 39.96800  14.41200  71.30800 1.000 19.78000 ? 25  HIS B CE1 1 
ATOM   3537 N  NE2 . HIS B 1 25  ? 40.93500  14.39300  70.40600 1.000 18.66000 ? 25  HIS B NE2 1 
ATOM   3538 N  N   . PHE B 1 26  ? 39.79600  7.65600   70.63100 1.000 21.29000 ? 26  PHE B N   1 
ATOM   3539 C  CA  . PHE B 1 26  ? 39.09100  6.38900   70.61200 1.000 21.67000 ? 26  PHE B CA  1 
ATOM   3540 C  C   . PHE B 1 26  ? 38.90400  5.87500   72.04200 1.000 22.62000 ? 26  PHE B C   1 
ATOM   3541 O  O   . PHE B 1 26  ? 39.75100  6.11400   72.90600 1.000 23.83000 ? 26  PHE B O   1 
ATOM   3542 C  CB  . PHE B 1 26  ? 39.87500  5.37500   69.79600 1.000 21.88000 ? 26  PHE B CB  1 
ATOM   3543 C  CG  . PHE B 1 26  ? 39.02500  4.36100   69.09800 1.000 21.86000 ? 26  PHE B CG  1 
ATOM   3544 C  CD1 . PHE B 1 26  ? 38.22000  4.72900   68.02900 1.000 21.42000 ? 26  PHE B CD1 1 
ATOM   3545 C  CD2 . PHE B 1 26  ? 39.03500  3.03900   69.50600 1.000 18.64000 ? 26  PHE B CD2 1 
ATOM   3546 C  CE1 . PHE B 1 26  ? 37.44600  3.79500   67.37700 1.000 17.41000 ? 26  PHE B CE1 1 
ATOM   3547 C  CE2 . PHE B 1 26  ? 38.26200  2.09400   68.85700 1.000 22.24000 ? 26  PHE B CE2 1 
ATOM   3548 C  CZ  . PHE B 1 26  ? 37.47100  2.47100   67.79100 1.000 21.76000 ? 26  PHE B CZ  1 
ATOM   3549 N  N   . PRO B 1 27  ? 37.80600  5.17100   72.32000 1.000 22.57000 ? 27  PRO B N   1 
ATOM   3550 C  CA  . PRO B 1 27  ? 37.58800  4.66200   73.68200 1.000 24.10000 ? 27  PRO B CA  1 
ATOM   3551 C  C   . PRO B 1 27  ? 38.72300  3.74200   74.11700 1.000 24.26000 ? 27  PRO B C   1 
ATOM   3552 O  O   . PRO B 1 27  ? 39.19500  2.90700   73.34600 1.000 25.23000 ? 27  PRO B O   1 
ATOM   3553 C  CB  . PRO B 1 27  ? 36.25800  3.90500   73.56800 1.000 22.72000 ? 27  PRO B CB  1 
ATOM   3554 C  CG  . PRO B 1 27  ? 35.56100  4.55400   72.42900 1.000 22.39000 ? 27  PRO B CG  1 
ATOM   3555 C  CD  . PRO B 1 27  ? 36.64600  4.90900   71.44900 1.000 21.31000 ? 27  PRO B CD  1 
ATOM   3556 N  N   . LYS B 1 28  ? 39.17600  3.91600   75.36400 1.000 27.11000 ? 28  LYS B N   1 
ATOM   3557 C  CA  . LYS B 1 28  ? 40.34200  3.16400   75.82500 1.000 31.10000 ? 28  LYS B CA  1 
ATOM   3558 C  C   . LYS B 1 28  ? 40.08700  1.66200   75.79500 1.000 27.82000 ? 28  LYS B C   1 
ATOM   3559 O  O   . LYS B 1 28  ? 40.96100  0.88400   75.38900 1.000 28.60000 ? 28  LYS B O   1 
ATOM   3560 C  CB  . LYS B 1 28  ? 40.73500  3.62100   77.22800 1.000 35.89000 ? 28  LYS B CB  1 
ATOM   3561 C  CG  . LYS B 1 28  ? 41.75300  4.74900   77.22100 1.000 37.97000 ? 28  LYS B CG  1 
ATOM   3562 C  CD  . LYS B 1 28  ? 41.31600  5.90200   78.11000 1.000 38.37000 ? 28  LYS B CD  1 
ATOM   3563 C  CE  . LYS B 1 28  ? 42.28300  7.06500   77.99100 1.000 41.04000 ? 28  LYS B CE  1 
ATOM   3564 N  NZ  . LYS B 1 28  ? 42.56600  7.36800   76.56900 1.000 42.32000 ? 28  LYS B NZ  1 
ATOM   3565 N  N   . SER B 1 29  ? 38.88500  1.23900   76.18700 1.000 30.50000 ? 29  SER B N   1 
ATOM   3566 C  CA  . SER B 1 29  ? 38.52900  -0.17500  76.22000 1.000 29.31000 ? 29  SER B CA  1 
ATOM   3567 C  C   . SER B 1 29  ? 38.48600  -0.82100  74.84300 1.000 34.04000 ? 29  SER B C   1 
ATOM   3568 O  O   . SER B 1 29  ? 38.44800  -2.05400  74.75500 1.000 32.16000 ? 29  SER B O   1 
ATOM   3569 C  CB  . SER B 1 29  ? 37.17200  -0.34600  76.89700 1.000 32.41000 ? 29  SER B CB  1 
ATOM   3570 O  OG  . SER B 1 29  ? 36.20500  0.50000   76.29400 1.000 32.20000 ? 29  SER B OG  1 
ATOM   3571 N  N   . LEU B 1 30  ? 38.47300  -0.03200  73.77100 1.000 28.41000 ? 30  LEU B N   1 
ATOM   3572 C  CA  . LEU B 1 30  ? 38.44500  -0.57200  72.41800 1.000 24.07000 ? 30  LEU B CA  1 
ATOM   3573 C  C   . LEU B 1 30  ? 39.72700  -0.27000  71.65000 1.000 26.51000 ? 30  LEU B C   1 
ATOM   3574 O  O   . LEU B 1 30  ? 39.76800  -0.47200  70.43000 1.000 26.82000 ? 30  LEU B O   1 
ATOM   3575 C  CB  . LEU B 1 30  ? 37.23400  -0.01300  71.66700 1.000 24.99000 ? 30  LEU B CB  1 
ATOM   3576 C  CG  . LEU B 1 30  ? 35.87200  -0.24600  72.32900 1.000 29.06000 ? 30  LEU B CG  1 
ATOM   3577 C  CD1 . LEU B 1 30  ? 34.78200  0.54300   71.60600 1.000 26.99000 ? 30  LEU B CD1 1 
ATOM   3578 C  CD2 . LEU B 1 30  ? 35.54200  -1.72600  72.30600 1.000 27.31000 ? 30  LEU B CD2 1 
ATOM   3579 N  N   . MET B 1 31  ? 40.77800  0.19500   72.33300 1.000 30.76000 ? 31  MET B N   1 
ATOM   3580 C  CA  . MET B 1 31  ? 41.94300  0.72600   71.62700 1.000 25.63000 ? 31  MET B CA  1 
ATOM   3581 C  C   . MET B 1 31  ? 42.61100  -0.33600  70.77000 1.000 29.42000 ? 31  MET B C   1 
ATOM   3582 O  O   . MET B 1 31  ? 43.11400  -0.03500  69.68300 1.000 26.76000 ? 31  MET B O   1 
ATOM   3583 C  CB  . MET B 1 31  ? 42.94600  1.32100   72.61500 1.000 26.37000 ? 31  MET B CB  1 
ATOM   3584 C  CG  . MET B 1 31  ? 44.03400  2.16200   71.95100 1.000 26.70000 ? 31  MET B CG  1 
ATOM   3585 S  SD  . MET B 1 31  ? 43.36600  3.60000   71.06900 1.000 26.35000 ? 31  MET B SD  1 
ATOM   3586 C  CE  . MET B 1 31  ? 42.93700  4.64500   72.44200 1.000 22.35000 ? 31  MET B CE  1 
ATOM   3587 N  N   . ASP B 1 32  ? 42.61400  -1.58900  71.22700 1.000 30.27000 ? 32  ASP B N   1 
ATOM   3588 C  CA  . ASP B 1 32  ? 43.23200  -2.62900  70.42100 1.000 32.79000 ? 32  ASP B CA  1 
ATOM   3589 C  C   . ASP B 1 32  ? 42.49100  -2.85200  69.11400 1.000 31.21000 ? 32  ASP B C   1 
ATOM   3590 O  O   . ASP B 1 32  ? 43.02400  -3.53300  68.23500 1.000 27.78000 ? 32  ASP B O   1 
ATOM   3591 C  CB  . ASP B 1 32  ? 43.32000  -3.93800  71.20600 1.000 34.33000 ? 32  ASP B CB  1 
ATOM   3592 C  CG  . ASP B 1 32  ? 41.98400  -4.36000  71.77300 1.000 44.65000 ? 32  ASP B CG  1 
ATOM   3593 O  OD1 . ASP B 1 32  ? 41.61400  -3.86400  72.86100 1.000 51.96000 ? 32  ASP B OD1 1 
ATOM   3594 O  OD2 . ASP B 1 32  ? 41.29400  -5.17800  71.12400 1.000 49.67000 ? 32  ASP B OD2 1 
ATOM   3595 N  N   . GLN B 1 33  ? 41.28700  -2.29500  68.96300 1.000 26.63000 ? 33  GLN B N   1 
ATOM   3596 C  CA  . GLN B 1 33  ? 40.53700  -2.37900  67.71600 1.000 25.77000 ? 33  GLN B CA  1 
ATOM   3597 C  C   . GLN B 1 33  ? 40.47100  -1.05100  66.97100 1.000 23.81000 ? 33  GLN B C   1 
ATOM   3598 O  O   . GLN B 1 33  ? 39.77000  -0.95600  65.95700 1.000 21.49000 ? 33  GLN B O   1 
ATOM   3599 C  CB  . GLN B 1 33  ? 39.11700  -2.88800  67.99500 1.000 30.65000 ? 33  GLN B CB  1 
ATOM   3600 C  CG  . GLN B 1 33  ? 39.08400  -4.23200  68.71900 1.000 31.25000 ? 33  GLN B CG  1 
ATOM   3601 C  CD  . GLN B 1 33  ? 37.67700  -4.70700  68.98200 1.000 34.56000 ? 33  GLN B CD  1 
ATOM   3602 O  OE1 . GLN B 1 33  ? 37.12700  -4.48300  70.06100 1.000 37.30000 ? 33  GLN B OE1 1 
ATOM   3603 N  NE2 . GLN B 1 33  ? 37.07800  -5.36100  67.99100 1.000 30.95000 ? 33  GLN B NE2 1 
ATOM   3604 N  N   . ALA B 1 34  ? 41.17800  -0.03000  67.44500 1.000 25.30000 ? 34  ALA B N   1 
ATOM   3605 C  CA  . ALA B 1 34  ? 41.16300  1.27800   66.82100 1.000 21.92000 ? 34  ALA B CA  1 
ATOM   3606 C  C   . ALA B 1 34  ? 41.80600  1.20900   65.44100 1.000 24.04000 ? 34  ALA B C   1 
ATOM   3607 O  O   . ALA B 1 34  ? 42.53700  0.26300   65.13900 1.000 23.10000 ? 34  ALA B O   1 
ATOM   3608 C  CB  . ALA B 1 34  ? 41.91000  2.27800   67.70300 1.000 19.87000 ? 34  ALA B CB  1 
ATOM   3609 N  N   . PRO B 1 35  ? 41.55000  2.20000   64.57900 1.000 21.88000 ? 35  PRO B N   1 
ATOM   3610 C  CA  . PRO B 1 35  ? 42.36100  2.31600   63.35900 1.000 18.88000 ? 35  PRO B CA  1 
ATOM   3611 C  C   . PRO B 1 35  ? 43.83000  2.46200   63.72800 1.000 18.36000 ? 35  PRO B C   1 
ATOM   3612 O  O   . PRO B 1 35  ? 44.18000  3.17000   64.67300 1.000 24.32000 ? 35  PRO B O   1 
ATOM   3613 C  CB  . PRO B 1 35  ? 41.82300  3.57900   62.67500 1.000 18.25000 ? 35  PRO B CB  1 
ATOM   3614 C  CG  . PRO B 1 35  ? 40.49000  3.85100   63.31400 1.000 18.88000 ? 35  PRO B CG  1 
ATOM   3615 C  CD  . PRO B 1 35  ? 40.58600  3.30800   64.71400 1.000 20.27000 ? 35  PRO B CD  1 
ATOM   3616 N  N   . LYS B 1 36  ? 44.68800  1.76600   62.98200 1.000 23.54000 ? 36  LYS B N   1 
ATOM   3617 C  CA  . LYS B 1 36  ? 46.12300  1.75600   63.22100 1.000 28.03000 ? 36  LYS B CA  1 
ATOM   3618 C  C   . LYS B 1 36  ? 46.84600  1.98600   61.90700 1.000 22.92000 ? 36  LYS B C   1 
ATOM   3619 O  O   . LYS B 1 36  ? 46.39400  1.53400   60.85200 1.000 21.21000 ? 36  LYS B O   1 
ATOM   3620 C  CB  . LYS B 1 36  ? 46.59900  0.42400   63.83600 1.000 29.22000 ? 36  LYS B CB  1 
ATOM   3621 C  CG  . LYS B 1 36  ? 45.88600  0.06200   65.13400 1.000 35.52000 ? 36  LYS B CG  1 
ATOM   3622 C  CD  . LYS B 1 36  ? 46.85400  -0.04600  66.31400 1.000 44.06000 ? 36  LYS B CD  1 
ATOM   3623 C  CE  . LYS B 1 36  ? 46.08100  -0.22600  67.61300 1.000 34.09000 ? 36  LYS B CE  1 
ATOM   3624 N  NZ  . LYS B 1 36  ? 44.87200  -1.04900  67.31400 1.000 38.42000 ? 36  LYS B NZ  1 
ATOM   3625 N  N   . LEU B 1 37  ? 47.97800  2.68500   61.97200 1.000 23.44000 ? 37  LEU B N   1 
ATOM   3626 C  CA  . LEU B 1 37  ? 48.74300  2.96300   60.76200 1.000 20.82000 ? 37  LEU B CA  1 
ATOM   3627 C  C   . LEU B 1 37  ? 49.51400  1.72300   60.34300 1.000 22.17000 ? 37  LEU B C   1 
ATOM   3628 O  O   . LEU B 1 37  ? 49.98800  0.95700   61.18700 1.000 23.34000 ? 37  LEU B O   1 
ATOM   3629 C  CB  . LEU B 1 37  ? 49.70300  4.13600   60.97300 1.000 21.33000 ? 37  LEU B CB  1 
ATOM   3630 C  CG  . LEU B 1 37  ? 49.00300  5.48700   61.13800 1.000 23.52000 ? 37  LEU B CG  1 
ATOM   3631 C  CD1 . LEU B 1 37  ? 49.99000  6.52800   61.64200 1.000 25.25000 ? 37  LEU B CD1 1 
ATOM   3632 C  CD2 . LEU B 1 37  ? 48.34400  5.93700   59.82800 1.000 19.17000 ? 37  LEU B CD2 1 
ATOM   3633 N  N   . THR B 1 38  ? 49.61400  1.52700   59.02900 1.000 21.85000 ? 38  THR B N   1 
ATOM   3634 C  CA  . THR B 1 38  ? 50.33800  0.41600   58.42700 1.000 25.13000 ? 38  THR B CA  1 
ATOM   3635 C  C   . THR B 1 38  ? 50.79000  0.85400   57.03700 1.000 24.00000 ? 38  THR B C   1 
ATOM   3636 O  O   . THR B 1 38  ? 50.31900  1.85900   56.50800 1.000 24.39000 ? 38  THR B O   1 
ATOM   3637 C  CB  . THR B 1 38  ? 49.46000  -0.83300  58.34900 1.000 24.67000 ? 38  THR B CB  1 
ATOM   3638 O  OG1 . THR B 1 38  ? 50.24600  -1.94700  57.90600 1.000 27.98000 ? 38  THR B OG1 1 
ATOM   3639 C  CG2 . THR B 1 38  ? 48.32000  -0.60800  57.38200 1.000 25.95000 ? 38  THR B CG2 1 
ATOM   3640 N  N   . ALA B 1 39  ? 51.71000  0.09500   56.44000 1.000 22.80000 ? 39  ALA B N   1 
ATOM   3641 C  CA  . ALA B 1 39  ? 52.11100  0.39500   55.07000 1.000 20.94000 ? 39  ALA B CA  1 
ATOM   3642 C  C   . ALA B 1 39  ? 50.91800  0.25100   54.13700 1.000 25.98000 ? 39  ALA B C   1 
ATOM   3643 O  O   . ALA B 1 39  ? 50.12800  -0.68800  54.26000 1.000 23.31000 ? 39  ALA B O   1 
ATOM   3644 C  CB  . ALA B 1 39  ? 53.23700  -0.54100  54.61400 1.000 26.06000 ? 39  ALA B CB  1 
ATOM   3645 N  N   . HIS B 1 40  ? 50.78000  1.18600   53.20200 1.000 24.95000 ? 40  HIS B N   1 
ATOM   3646 C  CA  . HIS B 1 40  ? 49.69800  1.08300   52.23100 1.000 24.78000 ? 40  HIS B CA  1 
ATOM   3647 C  C   . HIS B 1 40  ? 49.97900  -0.07400  51.27800 1.000 31.94000 ? 40  HIS B C   1 
ATOM   3648 O  O   . HIS B 1 40  ? 51.05500  -0.12100  50.66900 1.000 29.28000 ? 40  HIS B O   1 
ATOM   3649 C  CB  . HIS B 1 40  ? 49.53800  2.38100   51.44900 1.000 25.41000 ? 40  HIS B CB  1 
ATOM   3650 C  CG  . HIS B 1 40  ? 48.23100  2.48000   50.72400 1.000 28.99000 ? 40  HIS B CG  1 
ATOM   3651 N  ND1 . HIS B 1 40  ? 47.84500  1.57200   49.76300 1.000 30.61000 ? 40  HIS B ND1 1 
ATOM   3652 C  CD2 . HIS B 1 40  ? 47.21100  3.36300   50.83700 1.000 28.45000 ? 40  HIS B CD2 1 
ATOM   3653 C  CE1 . HIS B 1 40  ? 46.64900  1.89800   49.30600 1.000 34.26000 ? 40  HIS B CE1 1 
ATOM   3654 N  NE2 . HIS B 1 40  ? 46.24100  2.97900   49.94400 1.000 25.96000 ? 40  HIS B NE2 1 
ATOM   3655 N  N   . PRO B 1 41  ? 49.05600  -1.02800  51.13100 1.000 26.57000 ? 41  PRO B N   1 
ATOM   3656 C  CA  . PRO B 1 41  ? 49.33400  -2.17900  50.26100 1.000 30.93000 ? 41  PRO B CA  1 
ATOM   3657 C  C   . PRO B 1 41  ? 49.64600  -1.79600  48.82400 1.000 31.59000 ? 41  PRO B C   1 
ATOM   3658 O  O   . PRO B 1 41  ? 50.32700  -2.55800  48.13500 1.000 32.94000 ? 41  PRO B O   1 
ATOM   3659 C  CB  . PRO B 1 41  ? 48.05100  -3.02100  50.35900 1.000 29.08000 ? 41  PRO B CB  1 
ATOM   3660 C  CG  . PRO B 1 41  ? 47.04700  -2.16800  51.06100 1.000 31.80000 ? 41  PRO B CG  1 
ATOM   3661 C  CD  . PRO B 1 41  ? 47.80800  -1.19400  51.88700 1.000 28.61000 ? 41  PRO B CD  1 
ATOM   3662 N  N   . ARG B 1 42  ? 49.19900  -0.63600  48.35700 1.000 29.76000 ? 42  ARG B N   1 
ATOM   3663 C  CA  . ARG B 1 42  ? 49.45800  -0.20500  46.99200 1.000 31.35000 ? 42  ARG B CA  1 
ATOM   3664 C  C   . ARG B 1 42  ? 50.61500  0.77800   46.88900 1.000 31.52000 ? 42  ARG B C   1 
ATOM   3665 O  O   . ARG B 1 42  ? 50.97500  1.16500   45.77600 1.000 37.21000 ? 42  ARG B O   1 
ATOM   3666 C  CB  . ARG B 1 42  ? 48.19500  0.41900   46.38200 1.000 36.64000 ? 42  ARG B CB  1 
ATOM   3667 C  CG  . ARG B 1 42  ? 47.26000  -0.59400  45.73300 1.000 40.65000 ? 42  ARG B CG  1 
ATOM   3668 C  CD  . ARG B 1 42  ? 45.94900  0.03200   45.25000 1.000 46.18000 ? 42  ARG B CD  1 
ATOM   3669 N  NE  . ARG B 1 42  ? 45.62500  1.31000   45.89100 1.000 51.85000 ? 42  ARG B NE  1 
ATOM   3670 C  CZ  . ARG B 1 42  ? 45.65800  2.49700   45.28200 1.000 52.58000 ? 42  ARG B CZ  1 
ATOM   3671 N  NH1 . ARG B 1 42  ? 46.01900  2.59400   44.00500 1.000 47.94000 ? 42  ARG B NH1 1 
ATOM   3672 N  NH2 . ARG B 1 42  ? 45.33200  3.59300   45.95600 1.000 48.89000 ? 42  ARG B NH2 1 
ATOM   3673 N  N   . ASN B 1 43  ? 51.20200  1.19700   48.01500 1.000 30.18000 ? 43  ASN B N   1 
ATOM   3674 C  CA  . ASN B 1 43  ? 52.38400  2.05000   47.99800 1.000 31.56000 ? 43  ASN B CA  1 
ATOM   3675 C  C   . ASN B 1 43  ? 53.15000  1.90400   49.30900 1.000 29.63000 ? 43  ASN B C   1 
ATOM   3676 O  O   . ASN B 1 43  ? 52.92200  2.67200   50.25700 1.000 28.86000 ? 43  ASN B O   1 
ATOM   3677 C  CB  . ASN B 1 43  ? 52.00800  3.51500   47.75300 1.000 26.06000 ? 43  ASN B CB  1 
ATOM   3678 C  CG  . ASN B 1 43  ? 53.23100  4.41400   47.62800 1.000 32.96000 ? 43  ASN B CG  1 
ATOM   3679 O  OD1 . ASN B 1 43  ? 54.36900  3.93000   47.62600 1.000 27.16000 ? 43  ASN B OD1 1 
ATOM   3680 N  ND2 . ASN B 1 43  ? 53.00600  5.72800   47.52800 1.000 29.06000 ? 43  ASN B ND2 1 
ATOM   3681 N  N   . PRO B 1 44  ? 54.08800  0.95400   49.39100 1.000 29.94000 ? 44  PRO B N   1 
ATOM   3682 C  CA  . PRO B 1 44  ? 54.73300  0.65300   50.68700 1.000 26.63000 ? 44  PRO B CA  1 
ATOM   3683 C  C   . PRO B 1 44  ? 55.54200  1.80400   51.26500 1.000 27.96000 ? 44  PRO B C   1 
ATOM   3684 O  O   . PRO B 1 44  ? 55.96200  1.72400   52.42900 1.000 25.87000 ? 44  PRO B O   1 
ATOM   3685 C  CB  . PRO B 1 44  ? 55.63800  -0.54600  50.36400 1.000 35.21000 ? 44  PRO B CB  1 
ATOM   3686 C  CG  . PRO B 1 44  ? 55.12600  -1.09500  49.04800 1.000 36.69000 ? 44  PRO B CG  1 
ATOM   3687 C  CD  . PRO B 1 44  ? 54.56700  0.07800   48.30700 1.000 33.20000 ? 44  PRO B CD  1 
ATOM   3688 N  N   . ARG B 1 45  ? 55.77500  2.86600   50.50000 1.000 26.08000 ? 45  ARG B N   1 
ATOM   3689 C  CA  . ARG B 1 45  ? 56.53700  3.99800   50.99500 1.000 24.61000 ? 45  ARG B CA  1 
ATOM   3690 C  C   . ARG B 1 45  ? 55.72100  4.93900   51.86600 1.000 23.48000 ? 45  ARG B C   1 
ATOM   3691 O  O   . ARG B 1 45  ? 56.29600  5.86900   52.44100 1.000 23.10000 ? 45  ARG B O   1 
ATOM   3692 C  CB  . ARG B 1 45  ? 57.13200  4.77300   49.82000 1.000 29.83000 ? 45  ARG B CB  1 
ATOM   3693 C  CG  . ARG B 1 45  ? 58.37600  4.13900   49.26600 1.000 33.47000 ? 45  ARG B CG  1 
ATOM   3694 C  CD  . ARG B 1 45  ? 59.43200  5.18900   48.94600 1.000 37.95000 ? 45  ARG B CD  1 
ATOM   3695 N  NE  . ARG B 1 45  ? 58.94400  6.12800   47.94800 1.000 34.36000 ? 45  ARG B NE  1 
ATOM   3696 C  CZ  . ARG B 1 45  ? 59.54500  7.27000   47.63100 1.000 36.63000 ? 45  ARG B CZ  1 
ATOM   3697 N  NH1 . ARG B 1 45  ? 60.67200  7.63200   48.23700 1.000 32.19000 ? 45  ARG B NH1 1 
ATOM   3698 N  NH2 . ARG B 1 45  ? 59.00800  8.05600   46.71000 1.000 38.46000 ? 45  ARG B NH2 1 
ATOM   3699 N  N   . VAL B 1 46  ? 54.40900  4.73200   51.99800 1.000 23.96000 ? 46  VAL B N   1 
ATOM   3700 C  CA  . VAL B 1 46  ? 53.58700  5.62900   52.80300 1.000 21.75000 ? 46  VAL B CA  1 
ATOM   3701 C  C   . VAL B 1 46  ? 52.69500  4.81100   53.72600 1.000 22.20000 ? 46  VAL B C   1 
ATOM   3702 O  O   . VAL B 1 46  ? 52.36500  3.65500   53.44900 1.000 25.48000 ? 46  VAL B O   1 
ATOM   3703 C  CB  . VAL B 1 46  ? 52.72700  6.58200   51.93500 1.000 21.81000 ? 46  VAL B CB  1 
ATOM   3704 C  CG1 . VAL B 1 46  ? 53.60900  7.59000   51.19500 1.000 25.32000 ? 46  VAL B CG1 1 
ATOM   3705 C  CG2 . VAL B 1 46  ? 51.85000  5.79100   50.96400 1.000 21.97000 ? 46  VAL B CG2 1 
ATOM   3706 N  N   . GLN B 1 47  ? 52.30400  5.42300   54.83400 1.000 24.30000 ? 47  GLN B N   1 
ATOM   3707 C  CA  . GLN B 1 47  ? 51.41800  4.75300   55.76900 1.000 20.76000 ? 47  GLN B CA  1 
ATOM   3708 C  C   . GLN B 1 47  ? 49.96200  4.99800   55.39600 1.000 23.83000 ? 47  GLN B C   1 
ATOM   3709 O  O   . GLN B 1 47  ? 49.62900  5.92200   54.65400 1.000 20.42000 ? 47  GLN B O   1 
ATOM   3710 C  CB  . GLN B 1 47  ? 51.66100  5.22100   57.19800 1.000 20.32000 ? 47  GLN B CB  1 
ATOM   3711 C  CG  . GLN B 1 47  ? 53.07300  5.02200   57.71000 1.000 26.27000 ? 47  GLN B CG  1 
ATOM   3712 C  CD  . GLN B 1 47  ? 53.16600  5.33000   59.20100 1.000 39.69000 ? 47  GLN B CD  1 
ATOM   3713 O  OE1 . GLN B 1 47  ? 53.07300  6.49200   59.62800 1.000 31.56000 ? 47  GLN B OE1 1 
ATOM   3714 N  NE2 . GLN B 1 47  ? 53.31300  4.27500   60.00900 1.000 43.27000 ? 47  GLN B NE2 1 
ATOM   3715 N  N   . ALA B 1 48  ? 49.09400  4.14900   55.93700 1.000 18.26000 ? 48  ALA B N   1 
ATOM   3716 C  CA  . ALA B 1 48  ? 47.66800  4.21000   55.67700 1.000 20.44000 ? 48  ALA B CA  1 
ATOM   3717 C  C   . ALA B 1 48  ? 46.95400  3.63500   56.88900 1.000 19.36000 ? 48  ALA B C   1 
ATOM   3718 O  O   . ALA B 1 48  ? 47.56900  3.00700   57.75500 1.000 18.50000 ? 48  ALA B O   1 
ATOM   3719 C  CB  . ALA B 1 48  ? 47.29600  3.45200   54.40000 1.000 19.15000 ? 48  ALA B CB  1 
ATOM   3720 N  N   . TRP B 1 49  ? 45.64200  3.86000   56.95500 1.000 21.79000 ? 49  TRP B N   1 
ATOM   3721 C  CA  . TRP B 1 49  ? 44.87200  3.48600   58.13300 1.000 19.94000 ? 49  TRP B CA  1 
ATOM   3722 C  C   . TRP B 1 49  ? 44.27400  2.10300   57.93200 1.000 21.51000 ? 49  TRP B C   1 
ATOM   3723 O  O   . TRP B 1 49  ? 43.49300  1.89800   57.00200 1.000 20.30000 ? 49  TRP B O   1 
ATOM   3724 C  CB  . TRP B 1 49  ? 43.75100  4.49100   58.40100 1.000 19.75000 ? 49  TRP B CB  1 
ATOM   3725 C  CG  . TRP B 1 49  ? 44.18800  5.80700   58.94700 1.000 19.02000 ? 49  TRP B CG  1 
ATOM   3726 C  CD1 . TRP B 1 49  ? 44.19300  7.00300   58.29400 1.000 20.17000 ? 49  TRP B CD1 1 
ATOM   3727 C  CD2 . TRP B 1 49  ? 44.67400  6.06600   60.26700 1.000 15.93000 ? 49  TRP B CD2 1 
ATOM   3728 N  NE1 . TRP B 1 49  ? 44.65500  7.99700   59.12800 1.000 17.32000 ? 49  TRP B NE1 1 
ATOM   3729 C  CE2 . TRP B 1 49  ? 44.95200  7.44500   60.34700 1.000 17.90000 ? 49  TRP B CE2 1 
ATOM   3730 C  CE3 . TRP B 1 49  ? 44.89600  5.26400   61.39400 1.000 17.53000 ? 49  TRP B CE3 1 
ATOM   3731 C  CZ2 . TRP B 1 49  ? 45.44400  8.04200   61.50600 1.000 18.65000 ? 49  TRP B CZ2 1 
ATOM   3732 C  CZ3 . TRP B 1 49  ? 45.39100  5.85500   62.54200 1.000 18.26000 ? 49  TRP B CZ3 1 
ATOM   3733 C  CH2 . TRP B 1 49  ? 45.65300  7.23400   62.59100 1.000 21.87000 ? 49  TRP B CH2 1 
ATOM   3734 N  N   . GLN B 1 50  ? 44.58800  1.17600   58.83600 1.000 24.23000 ? 50  GLN B N   1 
ATOM   3735 C  CA  . GLN B 1 50  ? 43.96100  -0.13900  58.86600 1.000 23.06000 ? 50  GLN B CA  1 
ATOM   3736 C  C   . GLN B 1 50  ? 42.83000  -0.14900  59.88600 1.000 20.58000 ? 50  GLN B C   1 
ATOM   3737 O  O   . GLN B 1 50  ? 43.04100  0.20200   61.05300 1.000 24.52000 ? 50  GLN B O   1 
ATOM   3738 C  CB  . GLN B 1 50  ? 44.97500  -1.22300  59.21800 1.000 24.82000 ? 50  GLN B CB  1 
ATOM   3739 C  CG  . GLN B 1 50  ? 44.43400  -2.63300  59.07500 1.000 24.21000 ? 50  GLN B CG  1 
ATOM   3740 C  CD  . GLN B 1 50  ? 45.54900  -3.65100  59.06000 1.000 35.55000 ? 50  GLN B CD  1 
ATOM   3741 O  OE1 . GLN B 1 50  ? 46.24100  -3.83900  60.05600 1.000 39.72000 ? 50  GLN B OE1 1 
ATOM   3742 N  NE2 . GLN B 1 50  ? 45.74900  -4.29600  57.91700 1.000 41.17000 ? 50  GLN B NE2 1 
ATOM   3743 N  N   . PHE B 1 51  ? 41.64000  -0.55600  59.45000 1.000 20.36000 ? 51  PHE B N   1 
ATOM   3744 C  CA  . PHE B 1 51  ? 40.47300  -0.58900  60.33100 1.000 19.52000 ? 51  PHE B CA  1 
ATOM   3745 C  C   . PHE B 1 51  ? 39.52100  -1.65600  59.82500 1.000 21.57000 ? 51  PHE B C   1 
ATOM   3746 O  O   . PHE B 1 51  ? 39.10200  -1.61300  58.66300 1.000 19.50000 ? 51  PHE B O   1 
ATOM   3747 C  CB  . PHE B 1 51  ? 39.78700  0.78800   60.38000 1.000 18.49000 ? 51  PHE B CB  1 
ATOM   3748 C  CG  . PHE B 1 51  ? 38.76600  0.94200   61.48100 1.000 20.52000 ? 51  PHE B CG  1 
ATOM   3749 C  CD1 . PHE B 1 51  ? 39.03100  0.50700   62.77100 1.000 20.43000 ? 51  PHE B CD1 1 
ATOM   3750 C  CD2 . PHE B 1 51  ? 37.55200  1.57200   61.22700 1.000 15.77000 ? 51  PHE B CD2 1 
ATOM   3751 C  CE1 . PHE B 1 51  ? 38.09100  0.67100   63.79100 1.000 22.45000 ? 51  PHE B CE1 1 
ATOM   3752 C  CE2 . PHE B 1 51  ? 36.61400  1.73800   62.23100 1.000 22.06000 ? 51  PHE B CE2 1 
ATOM   3753 C  CZ  . PHE B 1 51  ? 36.88200  1.28900   63.52100 1.000 19.39000 ? 51  PHE B CZ  1 
ATOM   3754 N  N   . GLN B 1 52  ? 39.18500  -2.60800  60.69900 1.000 21.67000 ? 52  GLN B N   1 
ATOM   3755 C  CA  . GLN B 1 52  ? 38.20400  -3.64900  60.39000 1.000 19.44000 ? 52  GLN B CA  1 
ATOM   3756 C  C   . GLN B 1 52  ? 38.54700  -4.36900  59.08600 1.000 25.86000 ? 52  GLN B C   1 
ATOM   3757 O  O   . GLN B 1 52  ? 37.68700  -4.60100  58.23200 1.000 25.63000 ? 52  GLN B O   1 
ATOM   3758 C  CB  . GLN B 1 52  ? 36.79600  -3.06700  60.33000 1.000 19.42000 ? 52  GLN B CB  1 
ATOM   3759 C  CG  . GLN B 1 52  ? 36.34300  -2.39400  61.60600 1.000 19.64000 ? 52  GLN B CG  1 
ATOM   3760 C  CD  . GLN B 1 52  ? 34.84600  -2.22300  61.64400 1.000 20.60000 ? 52  GLN B CD  1 
ATOM   3761 O  OE1 . GLN B 1 52  ? 34.11100  -3.16200  61.37300 1.000 19.93000 ? 52  GLN B OE1 1 
ATOM   3762 N  NE2 . GLN B 1 52  ? 34.38300  -1.00500  61.96000 1.000 22.07000 ? 52  GLN B NE2 1 
ATOM   3763 N  N   . GLY B 1 53  ? 39.82300  -4.71100  58.92300 1.000 26.96000 ? 53  GLY B N   1 
ATOM   3764 C  CA  . GLY B 1 53  ? 40.23800  -5.49500  57.77300 1.000 29.40000 ? 53  GLY B CA  1 
ATOM   3765 C  C   . GLY B 1 53  ? 40.28700  -4.74400  56.46300 1.000 31.42000 ? 53  GLY B C   1 
ATOM   3766 O  O   . GLY B 1 53  ? 40.32800  -5.36600  55.39600 1.000 26.87000 ? 53  GLY B O   1 
ATOM   3767 N  N   . THR B 1 54  ? 40.25700  -3.42000  56.50700 1.000 23.95000 ? 54  THR B N   1 
ATOM   3768 C  CA  . THR B 1 54  ? 40.44600  -2.60200  55.32500 1.000 23.16000 ? 54  THR B CA  1 
ATOM   3769 C  C   . THR B 1 54  ? 41.58400  -1.63700  55.60100 1.000 22.92000 ? 54  THR B C   1 
ATOM   3770 O  O   . THR B 1 54  ? 41.92700  -1.37300  56.75600 1.000 28.15000 ? 54  THR B O   1 
ATOM   3771 C  CB  . THR B 1 54  ? 39.16400  -1.84100  54.95000 1.000 26.47000 ? 54  THR B CB  1 
ATOM   3772 O  OG1 . THR B 1 54  ? 38.92900  -0.78800  55.89400 1.000 28.16000 ? 54  THR B OG1 1 
ATOM   3773 C  CG2 . THR B 1 54  ? 37.96100  -2.78700  54.92800 1.000 24.32000 ? 54  THR B CG2 1 
ATOM   3774 N  N   . VAL B 1 55  ? 42.19300  -1.13700  54.52900 1.000 25.50000 ? 55  VAL B N   1 
ATOM   3775 C  CA  . VAL B 1 55  ? 43.30500  -0.20100  54.62500 1.000 24.61000 ? 55  VAL B CA  1 
ATOM   3776 C  C   . VAL B 1 55  ? 43.04100  0.92700   53.63800 1.000 27.07000 ? 55  VAL B C   1 
ATOM   3777 O  O   . VAL B 1 55  ? 42.91200  0.67500   52.43500 1.000 26.50000 ? 55  VAL B O   1 
ATOM   3778 C  CB  . VAL B 1 55  ? 44.65600  -0.88100  54.32600 1.000 23.83000 ? 55  VAL B CB  1 
ATOM   3779 C  CG1 . VAL B 1 55  ? 45.77000  0.15200   54.30500 1.000 22.38000 ? 55  VAL B CG1 1 
ATOM   3780 C  CG2 . VAL B 1 55  ? 44.95900  -1.98700  55.34500 1.000 27.28000 ? 55  VAL B CG2 1 
ATOM   3781 N  N   . VAL B 1 56  ? 42.95200  2.16500   54.13500 1.000 25.38000 ? 56  VAL B N   1 
ATOM   3782 C  CA  . VAL B 1 56  ? 42.69300  3.31800   53.27700 1.000 26.48000 ? 56  VAL B CA  1 
ATOM   3783 C  C   . VAL B 1 56  ? 43.70500  4.41300   53.58400 1.000 23.85000 ? 56  VAL B C   1 
ATOM   3784 O  O   . VAL B 1 56  ? 44.04700  4.65300   54.74800 1.000 24.43000 ? 56  VAL B O   1 
ATOM   3785 C  CB  . VAL B 1 56  ? 41.24900  3.85400   53.42400 1.000 26.72000 ? 56  VAL B CB  1 
ATOM   3786 C  CG1 . VAL B 1 56  ? 40.23900  2.80900   52.97400 1.000 22.32000 ? 56  VAL B CG1 1 
ATOM   3787 C  CG2 . VAL B 1 56  ? 40.96800  4.30700   54.85900 1.000 21.72000 ? 56  VAL B CG2 1 
ATOM   3788 N  N   . GLY B 1 57  ? 44.19600  5.06700   52.52800 1.000 26.66000 ? 57  GLY B N   1 
ATOM   3789 C  CA  . GLY B 1 57  ? 45.13800  6.15700   52.66500 1.000 25.95000 ? 57  GLY B CA  1 
ATOM   3790 C  C   . GLY B 1 57  ? 44.69600  7.36000   51.85200 1.000 28.10000 ? 57  GLY B C   1 
ATOM   3791 O  O   . GLY B 1 57  ? 43.69900  7.31100   51.13100 1.000 32.83000 ? 57  GLY B O   1 
ATOM   3792 N  N   . SER B 1 58  ? 45.47000  8.43700   51.97900 1.000 25.49000 ? 58  SER B N   1 
ATOM   3793 C  CA  . SER B 1 58  ? 45.17300  9.64800   51.23000 1.000 20.92000 ? 58  SER B CA  1 
ATOM   3794 C  C   . SER B 1 58  ? 45.52100  9.48400   49.75400 1.000 19.63000 ? 58  SER B C   1 
ATOM   3795 O  O   . SER B 1 58  ? 46.44400  8.76100   49.38200 1.000 25.40000 ? 58  SER B O   1 
ATOM   3796 C  CB  . SER B 1 58  ? 45.93100  10.84000  51.80900 1.000 23.44000 ? 58  SER B CB  1 
ATOM   3797 O  OG  . SER B 1 58  ? 45.37700  11.26100  53.04800 1.000 23.35000 ? 58  SER B OG  1 
ATOM   3798 N  N   . SER B 1 59  ? 44.74800  10.15100  48.91000 1.000 23.76000 ? 59  SER B N   1 
ATOM   3799 C  CA  . SER B 1 59  ? 45.01300  10.21000  47.48400 1.000 19.13000 ? 59  SER B CA  1 
ATOM   3800 C  C   . SER B 1 59  ? 45.97300  11.35200  47.18300 1.000 23.07000 ? 59  SER B C   1 
ATOM   3801 O  O   . SER B 1 59  ? 45.90800  12.41000  47.81300 1.000 22.35000 ? 59  SER B O   1 
ATOM   3802 C  CB  . SER B 1 59  ? 43.72000  10.41700  46.70800 1.000 21.51000 ? 59  SER B CB  1 
ATOM   3803 O  OG  . SER B 1 59  ? 43.99500  10.98100  45.43600 1.000 32.07000 ? 59  SER B OG  1 
ATOM   3804 N  N   . GLY B 1 60  ? 46.85600  11.13700  46.20700 1.000 23.04000 ? 60  GLY B N   1 
ATOM   3805 C  CA  . GLY B 1 60  ? 47.81300  12.15800  45.82400 1.000 21.88000 ? 60  GLY B CA  1 
ATOM   3806 C  C   . GLY B 1 60  ? 47.24000  13.33100  45.05500 1.000 23.50000 ? 60  GLY B C   1 
ATOM   3807 O  O   . GLY B 1 60  ? 48.01500  14.17200  44.58500 1.000 23.02000 ? 60  GLY B O   1 
ATOM   3808 N  N   . LEU B 1 61  ? 45.91600  13.39500  44.87900 1.000 20.30000 ? 61  LEU B N   1 
ATOM   3809 C  CA  . LEU B 1 61  ? 45.26800  14.59500  44.36200 1.000 21.11000 ? 61  LEU B CA  1 
ATOM   3810 C  C   . LEU B 1 61  ? 44.66400  15.44900  45.46100 1.000 19.79000 ? 61  LEU B C   1 
ATOM   3811 O  O   . LEU B 1 61  ? 44.17000  16.54100  45.16700 1.000 19.78000 ? 61  LEU B O   1 
ATOM   3812 C  CB  . LEU B 1 61  ? 44.16800  14.24100  43.35300 1.000 19.60000 ? 61  LEU B CB  1 
ATOM   3813 C  CG  . LEU B 1 61  ? 44.63200  13.63600  42.02700 1.000 23.01000 ? 61  LEU B CG  1 
ATOM   3814 C  CD1 . LEU B 1 61  ? 43.44400  13.28800  41.16700 1.000 26.54000 ? 61  LEU B CD1 1 
ATOM   3815 C  CD2 . LEU B 1 61  ? 45.55800  14.60600  41.30400 1.000 21.99000 ? 61  LEU B CD2 1 
ATOM   3816 N  N   . ASN B 1 62  ? 44.69300  14.98300  46.71300 1.000 17.37000 ? 62  ASN B N   1 
ATOM   3817 C  CA  . ASN B 1 62  ? 44.02000  15.66600  47.80900 1.000 18.37000 ? 62  ASN B CA  1 
ATOM   3818 C  C   . ASN B 1 62  ? 44.96200  16.28700  48.83500 1.000 20.03000 ? 62  ASN B C   1 
ATOM   3819 O  O   . ASN B 1 62  ? 44.48900  16.85200  49.82600 1.000 17.94000 ? 62  ASN B O   1 
ATOM   3820 C  CB  . ASN B 1 62  ? 43.05800  14.68800  48.49500 1.000 18.81000 ? 62  ASN B CB  1 
ATOM   3821 C  CG  . ASN B 1 62  ? 41.88300  14.32000  47.59800 1.000 22.42000 ? 62  ASN B CG  1 
ATOM   3822 O  OD1 . ASN B 1 62  ? 41.68100  14.93400  46.54500 1.000 17.42000 ? 62  ASN B OD1 1 
ATOM   3823 N  ND2 . ASN B 1 62  ? 41.11000  13.31300  48.00500 1.000 22.10000 ? 62  ASN B ND2 1 
ATOM   3824 N  N   . ALA B 1 63  ? 46.27300  16.21700  48.63700 1.000 18.25000 ? 63  ALA B N   1 
ATOM   3825 C  CA  . ALA B 1 63  ? 47.18900  16.86800  49.56600 1.000 16.87000 ? 63  ALA B CA  1 
ATOM   3826 C  C   . ALA B 1 63  ? 48.39300  17.39000  48.79000 1.000 19.87000 ? 63  ALA B C   1 
ATOM   3827 O  O   . ALA B 1 63  ? 49.54700  17.17200  49.16400 1.000 19.88000 ? 63  ALA B O   1 
ATOM   3828 C  CB  . ALA B 1 63  ? 47.59500  15.91100  50.68500 1.000 22.33000 ? 63  ALA B CB  1 
ATOM   3829 N  N   . VAL B 1 64  ? 48.11400  18.09700  47.68900 1.000 15.82000 ? 64  VAL B N   1 
ATOM   3830 C  CA  . VAL B 1 64  ? 49.12600  18.46300  46.69800 1.000 17.51000 ? 64  VAL B CA  1 
ATOM   3831 C  C   . VAL B 1 64  ? 49.85100  19.74500  47.04100 1.000 21.18000 ? 64  VAL B C   1 
ATOM   3832 O  O   . VAL B 1 64  ? 50.74900  20.16400  46.29900 1.000 17.83000 ? 64  VAL B O   1 
ATOM   3833 C  CB  . VAL B 1 64  ? 48.49100  18.67500  45.30900 1.000 18.14000 ? 64  VAL B CB  1 
ATOM   3834 C  CG1 . VAL B 1 64  ? 47.61200  17.50800  44.94000 1.000 19.93000 ? 64  VAL B CG1 1 
ATOM   3835 C  CG2 . VAL B 1 64  ? 47.69900  19.98700  45.29800 1.000 17.31000 ? 64  VAL B CG2 1 
ATOM   3836 N  N   . VAL B 1 65  ? 49.47100  20.38800  48.13300 1.000 17.07000 ? 65  VAL B N   1 
ATOM   3837 C  CA  . VAL B 1 65  ? 49.85000  21.76600  48.37300 1.000 20.57000 ? 65  VAL B CA  1 
ATOM   3838 C  C   . VAL B 1 65  ? 51.38200  21.89100  48.37400 1.000 17.91000 ? 65  VAL B C   1 
ATOM   3839 O  O   . VAL B 1 65  ? 52.08600  21.14600  49.06400 1.000 17.64000 ? 65  VAL B O   1 
ATOM   3840 C  CB  . VAL B 1 65  ? 49.14300  22.23600  49.65600 1.000 21.53000 ? 65  VAL B CB  1 
ATOM   3841 C  CG1 . VAL B 1 65  ? 49.86400  21.82400  50.94500 1.000 18.64000 ? 65  VAL B CG1 1 
ATOM   3842 C  CG2 . VAL B 1 65  ? 48.79000  23.66700  49.59600 1.000 24.69000 ? 65  VAL B CG2 1 
ATOM   3843 N  N   . SER B 1 66  ? 51.90300  22.78100  47.51600 1.000 20.55000 ? 66  SER B N   1 
ATOM   3844 C  CA  . SER B 1 66  ? 53.30200  23.11400  47.23200 1.000 17.63000 ? 66  SER B CA  1 
ATOM   3845 C  C   . SER B 1 66  ? 54.02000  22.07600  46.35800 1.000 20.26000 ? 66  SER B C   1 
ATOM   3846 O  O   . SER B 1 66  ? 55.15500  22.34300  45.92800 1.000 18.79000 ? 66  SER B O   1 
ATOM   3847 C  CB  . SER B 1 66  ? 54.15700  23.35100  48.49500 1.000 15.80000 ? 66  SER B CB  1 
ATOM   3848 O  OG  . SER B 1 66  ? 54.46800  22.12700  49.14100 1.000 16.52000 ? 66  SER B OG  1 
ATOM   3849 N  N   . TRP B 1 67  ? 53.42900  20.91300  46.07400 1.000 17.60000 ? 67  TRP B N   1 
ATOM   3850 C  CA  . TRP B 1 67  ? 54.10900  19.95400  45.20300 1.000 18.75000 ? 67  TRP B CA  1 
ATOM   3851 C  C   . TRP B 1 67  ? 54.19600  20.49000  43.77800 1.000 20.57000 ? 67  TRP B C   1 
ATOM   3852 O  O   . TRP B 1 67  ? 53.23700  21.09800  43.28600 1.000 18.14000 ? 67  TRP B O   1 
ATOM   3853 C  CB  . TRP B 1 67  ? 53.37600  18.62400  45.13000 1.000 17.24000 ? 67  TRP B CB  1 
ATOM   3854 C  CG  . TRP B 1 67  ? 53.36300  17.78400  46.34100 1.000 15.75000 ? 67  TRP B CG  1 
ATOM   3855 C  CD1 . TRP B 1 67  ? 53.96900  18.02300  47.53800 1.000 17.29000 ? 67  TRP B CD1 1 
ATOM   3856 C  CD2 . TRP B 1 67  ? 52.68800  16.53500  46.46700 1.000 16.82000 ? 67  TRP B CD2 1 
ATOM   3857 N  NE1 . TRP B 1 67  ? 53.69700  16.98900  48.41400 1.000 17.98000 ? 67  TRP B NE1 1 
ATOM   3858 C  CE2 . TRP B 1 67  ? 52.90800  16.06800  47.77700 1.000 15.60000 ? 67  TRP B CE2 1 
ATOM   3859 C  CE3 . TRP B 1 67  ? 51.90100  15.77100  45.59800 1.000 19.23000 ? 67  TRP B CE3 1 
ATOM   3860 C  CZ2 . TRP B 1 67  ? 52.37900  14.86900  48.23600 1.000 20.78000 ? 67  TRP B CZ2 1 
ATOM   3861 C  CZ3 . TRP B 1 67  ? 51.37600  14.57700  46.05800 1.000 20.35000 ? 67  TRP B CZ3 1 
ATOM   3862 C  CH2 . TRP B 1 67  ? 51.62000  14.13600  47.36100 1.000 21.52000 ? 67  TRP B CH2 1 
ATOM   3863 N  N   . PRO B 1 68  ? 55.29500  20.21400  43.06500 1.000 17.36000 ? 68  PRO B N   1 
ATOM   3864 C  CA  . PRO B 1 68  ? 55.29100  20.38500  41.61000 1.000 20.00000 ? 68  PRO B CA  1 
ATOM   3865 C  C   . PRO B 1 68  ? 54.14000  19.61300  40.98200 1.000 21.12000 ? 68  PRO B C   1 
ATOM   3866 O  O   . PRO B 1 68  ? 53.81400  18.49500  41.39000 1.000 17.50000 ? 68  PRO B O   1 
ATOM   3867 C  CB  . PRO B 1 68  ? 56.64700  19.81100  41.17400 1.000 21.84000 ? 68  PRO B CB  1 
ATOM   3868 C  CG  . PRO B 1 68  ? 57.47400  19.79000  42.37900 1.000 21.79000 ? 68  PRO B CG  1 
ATOM   3869 C  CD  . PRO B 1 68  ? 56.54800  19.61200  43.54500 1.000 19.68000 ? 68  PRO B CD  1 
ATOM   3870 N  N   . LYS B 1 69  ? 53.54300  20.21100  39.95400 1.000 23.44000 ? 69  LYS B N   1 
ATOM   3871 C  CA  . LYS B 1 69  ? 52.36500  19.61500  39.32900 1.000 21.33000 ? 69  LYS B CA  1 
ATOM   3872 C  C   . LYS B 1 69  ? 52.63200  18.20100  38.82800 1.000 22.14000 ? 69  LYS B C   1 
ATOM   3873 O  O   . LYS B 1 69  ? 51.74900  17.33500  38.90200 1.000 22.36000 ? 69  LYS B O   1 
ATOM   3874 C  CB  . LYS B 1 69  ? 51.88300  20.50700  38.19100 1.000 21.68000 ? 69  LYS B CB  1 
ATOM   3875 C  CG  . LYS B 1 69  ? 51.15900  21.74000  38.67800 1.000 25.71000 ? 69  LYS B CG  1 
ATOM   3876 C  CD  . LYS B 1 69  ? 50.62500  22.53200  37.50500 1.000 27.47000 ? 69  LYS B CD  1 
ATOM   3877 C  CE  . LYS B 1 69  ? 49.31300  23.19100  37.86500 1.000 34.49000 ? 69  LYS B CE  1 
ATOM   3878 N  NZ  . LYS B 1 69  ? 49.51500  24.17600  38.96800 1.000 38.46000 ? 69  LYS B NZ  1 
ATOM   3879 N  N   . HIS B 1 70  ? 53.84000  17.93500  38.31800 1.000 18.44000 ? 70  HIS B N   1 
ATOM   3880 C  CA  . HIS B 1 70  ? 54.11400  16.60100  37.79400 1.000 18.68000 ? 70  HIS B CA  1 
ATOM   3881 C  C   . HIS B 1 70  ? 54.09200  15.53000  38.87200 1.000 18.71000 ? 70  HIS B C   1 
ATOM   3882 O  O   . HIS B 1 70  ? 54.06500  14.34100  38.53800 1.000 19.67000 ? 70  HIS B O   1 
ATOM   3883 C  CB  . HIS B 1 70  ? 55.46000  16.58300  37.05800 1.000 19.46000 ? 70  HIS B CB  1 
ATOM   3884 C  CG  . HIS B 1 70  ? 56.65400  16.65300  37.96100 1.000 18.80000 ? 70  HIS B CG  1 
ATOM   3885 N  ND1 . HIS B 1 70  ? 57.18000  17.84200  38.41400 1.000 19.23000 ? 70  HIS B ND1 1 
ATOM   3886 C  CD2 . HIS B 1 70  ? 57.43500  15.67700  38.48000 1.000 17.82000 ? 70  HIS B CD2 1 
ATOM   3887 C  CE1 . HIS B 1 70  ? 58.22600  17.59600  39.18300 1.000 17.03000 ? 70  HIS B CE1 1 
ATOM   3888 N  NE2 . HIS B 1 70  ? 58.40700  16.29000  39.23300 1.000 15.83000 ? 70  HIS B NE2 1 
ATOM   3889 N  N   . GLU B 1 71  ? 54.09100  15.91700  40.14700 1.000 16.89000 ? 71  GLU B N   1 
ATOM   3890 C  CA  . GLU B 1 71  ? 54.00400  14.96900  41.25400 1.000 20.17000 ? 71  GLU B CA  1 
ATOM   3891 C  C   . GLU B 1 71  ? 52.56700  14.67700  41.67600 1.000 21.63000 ? 71  GLU B C   1 
ATOM   3892 O  O   . GLU B 1 71  ? 52.34100  13.72400  42.43100 1.000 18.87000 ? 71  GLU B O   1 
ATOM   3893 C  CB  . GLU B 1 71  ? 54.80600  15.49000  42.45600 1.000 19.40000 ? 71  GLU B CB  1 
ATOM   3894 C  CG  . GLU B 1 71  ? 56.33400  15.39700  42.26000 1.000 20.98000 ? 71  GLU B CG  1 
ATOM   3895 C  CD  . GLU B 1 71  ? 57.13400  15.76200  43.50700 1.000 21.96000 ? 71  GLU B CD  1 
ATOM   3896 O  OE1 . GLU B 1 71  ? 56.56000  16.34200  44.45800 1.000 17.77000 ? 71  GLU B OE1 1 
ATOM   3897 O  OE2 . GLU B 1 71  ? 58.35100  15.47700  43.52700 1.000 19.56000 ? 71  GLU B OE2 1 
ATOM   3898 N  N   . TRP B 1 72  ? 51.59700  15.45500  41.19800 1.000 21.33000 ? 72  TRP B N   1 
ATOM   3899 C  CA  . TRP B 1 72  ? 50.19600  15.19400  41.51400 1.000 19.69000 ? 72  TRP B CA  1 
ATOM   3900 C  C   . TRP B 1 72  ? 49.72400  13.93200  40.80700 1.000 21.21000 ? 72  TRP B C   1 
ATOM   3901 O  O   . TRP B 1 72  ? 49.98800  13.73700  39.62200 1.000 23.14000 ? 72  TRP B O   1 
ATOM   3902 C  CB  . TRP B 1 72  ? 49.31300  16.36600  41.07400 1.000 19.70000 ? 72  TRP B CB  1 
ATOM   3903 C  CG  . TRP B 1 72  ? 49.67000  17.72300  41.60800 1.000 19.61000 ? 72  TRP B CG  1 
ATOM   3904 C  CD1 . TRP B 1 72  ? 50.79600  18.08600  42.29700 1.000 17.28000 ? 72  TRP B CD1 1 
ATOM   3905 C  CD2 . TRP B 1 72  ? 48.87100  18.90000  41.50000 1.000 18.87000 ? 72  TRP B CD2 1 
ATOM   3906 N  NE1 . TRP B 1 72  ? 50.74700  19.42300  42.61300 1.000 17.41000 ? 72  TRP B NE1 1 
ATOM   3907 C  CE2 . TRP B 1 72  ? 49.57200  19.94400  42.13700 1.000 21.49000 ? 72  TRP B CE2 1 
ATOM   3908 C  CE3 . TRP B 1 72  ? 47.63100  19.17600  40.91500 1.000 16.25000 ? 72  TRP B CE3 1 
ATOM   3909 C  CZ2 . TRP B 1 72  ? 49.06900  21.24400  42.21200 1.000 20.32000 ? 72  TRP B CZ2 1 
ATOM   3910 C  CZ3 . TRP B 1 72  ? 47.13800  20.46600  40.99100 1.000 19.32000 ? 72  TRP B CZ3 1 
ATOM   3911 C  CH2 . TRP B 1 72  ? 47.85100  21.48000  41.63700 1.000 22.98000 ? 72  TRP B CH2 1 
ATOM   3912 N  N   . GLY B 1 73  ? 48.97900  13.09000  41.51600 1.000 22.76000 ? 73  GLY B N   1 
ATOM   3913 C  CA  . GLY B 1 73  ? 48.54900  11.85100  40.89100 1.000 22.12000 ? 73  GLY B CA  1 
ATOM   3914 C  C   . GLY B 1 73  ? 47.59500  11.10300  41.79100 1.000 25.21000 ? 73  GLY B C   1 
ATOM   3915 O  O   . GLY B 1 73  ? 47.32300  11.50800  42.92200 1.000 21.37000 ? 73  GLY B O   1 
ATOM   3916 N  N   . MET B 1 74  ? 47.08600  9.98900   41.28200 1.000 26.13000 ? 74  MET B N   1 
ATOM   3917 C  CA  . MET B 1 74  ? 46.13900  9.20300   42.05900 1.000 26.38000 ? 74  MET B CA  1 
ATOM   3918 C  C   . MET B 1 74  ? 46.80800  8.14100   42.92000 1.000 28.99000 ? 74  MET B C   1 
ATOM   3919 O  O   . MET B 1 74  ? 46.11100  7.40600   43.62100 1.000 30.50000 ? 74  MET B O   1 
ATOM   3920 C  CB  . MET B 1 74  ? 45.10600  8.55200   41.13500 1.000 33.48000 ? 74  MET B CB  1 
ATOM   3921 C  CG  . MET B 1 74  ? 44.11700  9.54200   40.54700 1.000 32.86000 ? 74  MET B CG  1 
ATOM   3922 S  SD  . MET B 1 74  ? 43.16100  8.82700   39.20400 1.000 57.67000 ? 74  MET B SD  1 
ATOM   3923 C  CE  . MET B 1 74  ? 42.89700  7.16700   39.81500 1.000 56.98000 ? 74  MET B CE  1 
ATOM   3924 N  N   . ASP B 1 75  ? 48.13100  8.04400   42.90100 1.000 26.30000 ? 75  ASP B N   1 
ATOM   3925 C  CA  . ASP B 1 75  ? 48.79400  7.10200   43.78600 1.000 30.25000 ? 75  ASP B CA  1 
ATOM   3926 C  C   . ASP B 1 75  ? 48.57900  7.50800   45.24300 1.000 26.79000 ? 75  ASP B C   1 
ATOM   3927 O  O   . ASP B 1 75  ? 48.46300  8.69900   45.55500 1.000 22.70000 ? 75  ASP B O   1 
ATOM   3928 C  CB  . ASP B 1 75  ? 50.28800  7.03900   43.47900 1.000 27.79000 ? 75  ASP B CB  1 
ATOM   3929 C  CG  . ASP B 1 75  ? 50.58100  6.29700   42.20500 1.000 38.61000 ? 75  ASP B CG  1 
ATOM   3930 O  OD1 . ASP B 1 75  ? 49.65000  5.67100   41.64800 1.000 40.74000 ? 75  ASP B OD1 1 
ATOM   3931 O  OD2 . ASP B 1 75  ? 51.74000  6.35400   41.75300 1.000 41.04000 ? 75  ASP B OD2 1 
ATOM   3932 N  N   . PRO B 1 76  ? 48.51200  6.53600   46.15300 1.000 27.91000 ? 76  PRO B N   1 
ATOM   3933 C  CA  . PRO B 1 76  ? 48.41800  6.86900   47.57900 1.000 27.48000 ? 76  PRO B CA  1 
ATOM   3934 C  C   . PRO B 1 76  ? 49.58400  7.74500   48.01000 1.000 25.61000 ? 76  PRO B C   1 
ATOM   3935 O  O   . PRO B 1 76  ? 50.70600  7.61100   47.52000 1.000 23.70000 ? 76  PRO B O   1 
ATOM   3936 C  CB  . PRO B 1 76  ? 48.46100  5.50300   48.27500 1.000 28.58000 ? 76  PRO B CB  1 
ATOM   3937 C  CG  . PRO B 1 76  ? 48.13000  4.49900   47.21800 1.000 33.68000 ? 76  PRO B CG  1 
ATOM   3938 C  CD  . PRO B 1 76  ? 48.60700  5.08400   45.91900 1.000 30.99000 ? 76  PRO B CD  1 
ATOM   3939 N  N   . THR B 1 77  ? 49.31000  8.65400   48.93500 1.000 20.80000 ? 77  THR B N   1 
ATOM   3940 C  CA  . THR B 1 77  ? 50.35900  9.45500   49.53200 1.000 20.19000 ? 77  THR B CA  1 
ATOM   3941 C  C   . THR B 1 77  ? 50.18600  9.40800   51.04500 1.000 21.81000 ? 77  THR B C   1 
ATOM   3942 O  O   . THR B 1 77  ? 49.20700  8.86200   51.56200 1.000 24.68000 ? 77  THR B O   1 
ATOM   3943 C  CB  . THR B 1 77  ? 50.32900  10.88900  48.98300 1.000 19.72000 ? 77  THR B CB  1 
ATOM   3944 O  OG1 . THR B 1 77  ? 51.41700  11.63900  49.53900 1.000 20.81000 ? 77  THR B OG1 1 
ATOM   3945 C  CG2 . THR B 1 77  ? 48.99500  11.56600  49.33900 1.000 23.51000 ? 77  THR B CG2 1 
ATOM   3946 N  N   . GLY B 1 78  ? 51.13900  9.97900   51.77000 1.000 21.91000 ? 78  GLY B N   1 
ATOM   3947 C  CA  . GLY B 1 78  ? 51.08100  9.83800   53.21000 1.000 17.74000 ? 78  GLY B CA  1 
ATOM   3948 C  C   . GLY B 1 78  ? 51.83100  10.94400  53.90400 1.000 18.98000 ? 78  GLY B C   1 
ATOM   3949 O  O   . GLY B 1 78  ? 52.41200  11.82300  53.26500 1.000 18.20000 ? 78  GLY B O   1 
ATOM   3950 N  N   . TYR B 1 79  ? 51.80700  10.88000  55.24300 1.000 18.45000 ? 79  TYR B N   1 
ATOM   3951 C  CA  . TYR B 1 79  ? 52.39300  11.93900  56.06000 1.000 18.56000 ? 79  TYR B CA  1 
ATOM   3952 C  C   . TYR B 1 79  ? 53.76900  12.34800  55.54700 1.000 17.38000 ? 79  TYR B C   1 
ATOM   3953 O  O   . TYR B 1 79  ? 54.07900  13.53900  55.42800 1.000 18.40000 ? 79  TYR B O   1 
ATOM   3954 C  CB  . TYR B 1 79  ? 52.51600  11.48500  57.51600 1.000 20.14000 ? 79  TYR B CB  1 
ATOM   3955 C  CG  . TYR B 1 79  ? 51.22000  11.18600  58.23800 1.000 21.46000 ? 79  TYR B CG  1 
ATOM   3956 C  CD1 . TYR B 1 79  ? 50.23000  12.15700  58.38800 1.000 17.77000 ? 79  TYR B CD1 1 
ATOM   3957 C  CD2 . TYR B 1 79  ? 51.01100  9.93900   58.80500 1.000 17.86000 ? 79  TYR B CD2 1 
ATOM   3958 C  CE1 . TYR B 1 79  ? 49.05500  11.87400  59.07000 1.000 20.39000 ? 79  TYR B CE1 1 
ATOM   3959 C  CE2 . TYR B 1 79  ? 49.85600  9.64300   59.48900 1.000 20.78000 ? 79  TYR B CE2 1 
ATOM   3960 C  CZ  . TYR B 1 79  ? 48.87800  10.61000  59.61600 1.000 22.28000 ? 79  TYR B CZ  1 
ATOM   3961 O  OH  . TYR B 1 79  ? 47.72700  10.30200  60.28100 1.000 18.85000 ? 79  TYR B OH  1 
ATOM   3962 N  N   . ALA B 1 80  ? 54.61600  11.36200  55.25200 1.000 16.50000 ? 80  ALA B N   1 
ATOM   3963 C  CA  . ALA B 1 80  ? 56.00300  11.66600  54.92200 1.000 19.99000 ? 80  ALA B CA  1 
ATOM   3964 C  C   . ALA B 1 80  ? 56.11300  12.58400  53.71100 1.000 20.44000 ? 80  ALA B C   1 
ATOM   3965 O  O   . ALA B 1 80  ? 57.02200  13.42000  53.65400 1.000 22.95000 ? 80  ALA B O   1 
ATOM   3966 C  CB  . ALA B 1 80  ? 56.78100  10.36900  54.67300 1.000 19.63000 ? 80  ALA B CB  1 
ATOM   3967 N  N   . GLU B 1 81  ? 55.19300  12.45900  52.75000 1.000 18.94000 ? 81  GLU B N   1 
ATOM   3968 C  CA  . GLU B 1 81  ? 55.24300  13.22100  51.50500 1.000 21.99000 ? 81  GLU B CA  1 
ATOM   3969 C  C   . GLU B 1 81  ? 54.49400  14.54500  51.56300 1.000 20.23000 ? 81  GLU B C   1 
ATOM   3970 O  O   . GLU B 1 81  ? 54.66700  15.38000  50.66800 1.000 16.61000 ? 81  GLU B O   1 
ATOM   3971 C  CB  . GLU B 1 81  ? 54.67400  12.37600  50.36700 1.000 18.14000 ? 81  GLU B CB  1 
ATOM   3972 C  CG  . GLU B 1 81  ? 55.45100  11.12000  50.16100 1.000 20.97000 ? 81  GLU B CG  1 
ATOM   3973 C  CD  . GLU B 1 81  ? 54.89400  10.26300  49.06300 1.000 23.96000 ? 81  GLU B CD  1 
ATOM   3974 O  OE1 . GLU B 1 81  ? 53.72500  10.48400  48.66400 1.000 22.80000 ? 81  GLU B OE1 1 
ATOM   3975 O  OE2 . GLU B 1 81  ? 55.63000  9.36100   48.61000 1.000 25.81000 ? 81  GLU B OE2 1 
ATOM   3976 N  N   . MET B 1 82  ? 53.67700  14.76600  52.58000 1.000 17.39000 ? 82  MET B N   1 
ATOM   3977 C  CA  . MET B 1 82  ? 52.81700  15.93900  52.62400 1.000 17.08000 ? 82  MET B CA  1 
ATOM   3978 C  C   . MET B 1 82  ? 53.50900  17.13800  53.25400 1.000 20.19000 ? 82  MET B C   1 
ATOM   3979 O  O   . MET B 1 82  ? 54.30600  17.00700  54.18600 1.000 18.82000 ? 82  MET B O   1 
ATOM   3980 C  CB  . MET B 1 82  ? 51.55100  15.63200  53.41400 1.000 17.62000 ? 82  MET B CB  1 
ATOM   3981 C  CG  . MET B 1 82  ? 50.71700  14.52200  52.82000 1.000 19.47000 ? 82  MET B CG  1 
ATOM   3982 S  SD  . MET B 1 82  ? 49.51400  13.95800  54.03100 1.000 19.14000 ? 82  MET B SD  1 
ATOM   3983 C  CE  . MET B 1 82  ? 48.49200  12.96100  52.95800 1.000 16.63000 ? 82  MET B CE  1 
ATOM   3984 N  N   . ARG B 1 83  ? 53.17400  18.31500  52.75500 1.000 15.34000 ? 83  ARG B N   1 
ATOM   3985 C  CA  . ARG B 1 83  ? 53.47800  19.52200  53.50000 1.000 17.65000 ? 83  ARG B CA  1 
ATOM   3986 C  C   . ARG B 1 83  ? 52.86600  19.38200  54.89200 1.000 19.36000 ? 83  ARG B C   1 
ATOM   3987 O  O   . ARG B 1 83  ? 51.69900  18.98500  55.00700 1.000 17.02000 ? 83  ARG B O   1 
ATOM   3988 C  CB  . ARG B 1 83  ? 52.91600  20.73700  52.77500 1.000 16.92000 ? 83  ARG B CB  1 
ATOM   3989 C  CG  . ARG B 1 83  ? 53.19200  22.08200  53.43300 1.000 18.49000 ? 83  ARG B CG  1 
ATOM   3990 C  CD  . ARG B 1 83  ? 52.75700  23.18100  52.48700 1.000 17.45000 ? 83  ARG B CD  1 
ATOM   3991 N  NE  . ARG B 1 83  ? 52.92600  24.52600  53.01700 1.000 18.42000 ? 83  ARG B NE  1 
ATOM   3992 C  CZ  . ARG B 1 83  ? 53.99800  25.28900  52.79800 1.000 23.15000 ? 83  ARG B CZ  1 
ATOM   3993 N  NH1 . ARG B 1 83  ? 55.01300  24.83100  52.07800 1.000 20.24000 ? 83  ARG B NH1 1 
ATOM   3994 N  NH2 . ARG B 1 83  ? 54.05800  26.51100  53.30300 1.000 16.24000 ? 83  ARG B NH2 1 
ATOM   3995 N  N   . PRO B 1 84  ? 53.62400  19.64200  55.96500 1.000 18.43000 ? 84  PRO B N   1 
ATOM   3996 C  CA  . PRO B 1 84  ? 53.12200  19.31400  57.30900 1.000 15.09000 ? 84  PRO B CA  1 
ATOM   3997 C  C   . PRO B 1 84  ? 51.80700  19.98900  57.63600 1.000 16.55000 ? 84  PRO B C   1 
ATOM   3998 O  O   . PRO B 1 84  ? 50.97900  19.39900  58.33800 1.000 17.21000 ? 84  PRO B O   1 
ATOM   3999 C  CB  . PRO B 1 84  ? 54.26100  19.78100  58.22300 1.000 18.75000 ? 84  PRO B CB  1 
ATOM   4000 C  CG  . PRO B 1 84  ? 55.50200  19.63200  57.34900 1.000 19.29000 ? 84  PRO B CG  1 
ATOM   4001 C  CD  . PRO B 1 84  ? 55.03700  20.07300  55.98600 1.000 19.41000 ? 84  PRO B CD  1 
ATOM   4002 N  N   . ALA B 1 85  ? 51.56600  21.17700  57.07900 1.000 19.69000 ? 85  ALA B N   1 
ATOM   4003 C  CA  . ALA B 1 85  ? 50.31900  21.89600  57.31100 1.000 17.90000 ? 85  ALA B CA  1 
ATOM   4004 C  C   . ALA B 1 85  ? 49.08300  21.10100  56.90600 1.000 16.98000 ? 85  ALA B C   1 
ATOM   4005 O  O   . ALA B 1 85  ? 47.97900  21.43200  57.36100 1.000 17.41000 ? 85  ALA B O   1 
ATOM   4006 C  CB  . ALA B 1 85  ? 50.33400  23.23400  56.56600 1.000 16.44000 ? 85  ALA B CB  1 
ATOM   4007 N  N   . VAL B 1 86  ? 49.21700  20.07700  56.06000 1.000 19.28000 ? 86  VAL B N   1 
ATOM   4008 C  CA  . VAL B 1 86  ? 47.99400  19.37800  55.67500 1.000 16.22000 ? 86  VAL B CA  1 
ATOM   4009 C  C   . VAL B 1 86  ? 47.48800  18.49700  56.81500 1.000 18.05000 ? 86  VAL B C   1 
ATOM   4010 O  O   . VAL B 1 86  ? 46.28400  18.22100  56.89400 1.000 15.03000 ? 86  VAL B O   1 
ATOM   4011 C  CB  . VAL B 1 86  ? 48.15200  18.55500  54.37400 1.000 20.78000 ? 86  VAL B CB  1 
ATOM   4012 C  CG1 . VAL B 1 86  ? 48.91700  19.30500  53.29500 1.000 16.44000 ? 86  VAL B CG1 1 
ATOM   4013 C  CG2 . VAL B 1 86  ? 48.72200  17.22200  54.64200 1.000 24.79000 ? 86  VAL B CG2 1 
ATOM   4014 N  N   . TYR B 1 87  ? 48.36900  18.02700  57.70800 1.000 14.96000 ? 87  TYR B N   1 
ATOM   4015 C  CA  . TYR B 1 87  ? 47.91900  17.21600  58.83500 1.000 16.90000 ? 87  TYR B CA  1 
ATOM   4016 C  C   . TYR B 1 87  ? 48.19700  17.82500  60.20700 1.000 19.44000 ? 87  TYR B C   1 
ATOM   4017 O  O   . TYR B 1 87  ? 47.66200  17.31800  61.20100 1.000 22.02000 ? 87  TYR B O   1 
ATOM   4018 C  CB  . TYR B 1 87  ? 48.54900  15.81500  58.78300 1.000 17.04000 ? 87  TYR B CB  1 
ATOM   4019 C  CG  . TYR B 1 87  ? 50.05700  15.83500  58.72300 1.000 17.91000 ? 87  TYR B CG  1 
ATOM   4020 C  CD1 . TYR B 1 87  ? 50.81500  15.97600  59.87400 1.000 18.99000 ? 87  TYR B CD1 1 
ATOM   4021 C  CD2 . TYR B 1 87  ? 50.72300  15.71800  57.50700 1.000 17.26000 ? 87  TYR B CD2 1 
ATOM   4022 C  CE1 . TYR B 1 87  ? 52.20300  16.00700  59.81700 1.000 19.91000 ? 87  TYR B CE1 1 
ATOM   4023 C  CE2 . TYR B 1 87  ? 52.10200  15.73500  57.44400 1.000 17.50000 ? 87  TYR B CE2 1 
ATOM   4024 C  CZ  . TYR B 1 87  ? 52.83700  15.88100  58.59800 1.000 17.49000 ? 87  TYR B CZ  1 
ATOM   4025 O  OH  . TYR B 1 87  ? 54.22300  15.90800  58.50600 1.000 19.52000 ? 87  TYR B OH  1 
ATOM   4026 N  N   . ASP B 1 88  ? 49.01600  18.87400  60.29600 1.000 15.98000 ? 88  ASP B N   1 
ATOM   4027 C  CA  . ASP B 1 88  ? 49.38700  19.50800  61.55900 1.000 16.99000 ? 88  ASP B CA  1 
ATOM   4028 C  C   . ASP B 1 88  ? 48.65200  20.83700  61.63200 1.000 16.15000 ? 88  ASP B C   1 
ATOM   4029 O  O   . ASP B 1 88  ? 48.96900  21.76200  60.88400 1.000 16.83000 ? 88  ASP B O   1 
ATOM   4030 C  CB  . ASP B 1 88  ? 50.90500  19.70400  61.63100 1.000 19.71000 ? 88  ASP B CB  1 
ATOM   4031 C  CG  . ASP B 1 88  ? 51.36800  20.33100  62.93300 1.000 25.37000 ? 88  ASP B CG  1 
ATOM   4032 O  OD1 . ASP B 1 88  ? 50.59800  21.09200  63.56700 1.000 26.99000 ? 88  ASP B OD1 1 
ATOM   4033 O  OD2 . ASP B 1 88  ? 52.52700  20.06300  63.32100 1.000 28.35000 ? 88  ASP B OD2 1 
ATOM   4034 N  N   . MET B 1 89  ? 47.67700  20.94300  62.53100 1.000 17.56000 ? 89  MET B N   1 
ATOM   4035 C  CA  . MET B 1 89  ? 46.83700  22.13300  62.50300 1.000 15.34000 ? 89  MET B CA  1 
ATOM   4036 C  C   . MET B 1 89  ? 47.56400  23.38200  62.99600 1.000 17.86000 ? 89  MET B C   1 
ATOM   4037 O  O   . MET B 1 89  ? 47.16100  24.49900  62.63100 1.000 19.35000 ? 89  MET B O   1 
ATOM   4038 C  CB  . MET B 1 89  ? 45.54700  21.86700  63.27700 1.000 15.31000 ? 89  MET B CB  1 
ATOM   4039 C  CG  . MET B 1 89  ? 44.65700  20.80700  62.59700 1.000 19.76000 ? 89  MET B CG  1 
ATOM   4040 S  SD  . MET B 1 89  ? 44.23200  21.15000  60.86000 1.000 20.40000 ? 89  MET B SD  1 
ATOM   4041 C  CE  . MET B 1 89  ? 45.38300  20.08800  59.96900 1.000 18.37000 ? 89  MET B CE  1 
ATOM   4042 N  N   . ASP B 1 90  ? 48.64300  23.23800  63.77800 1.000 20.80000 ? 90  ASP B N   1 
ATOM   4043 C  CA  . ASP B 1 90  ? 49.47500  24.40800  64.08200 1.000 20.62000 ? 90  ASP B CA  1 
ATOM   4044 C  C   . ASP B 1 90  ? 50.12800  24.96300  62.81500 1.000 18.98000 ? 90  ASP B C   1 
ATOM   4045 O  O   . ASP B 1 90  ? 50.25600  26.18200  62.65000 1.000 19.82000 ? 90  ASP B O   1 
ATOM   4046 C  CB  . ASP B 1 90  ? 50.56100  24.06400  65.10200 1.000 18.91000 ? 90  ASP B CB  1 
ATOM   4047 C  CG  . ASP B 1 90  ? 50.00800  23.73800  66.47300 1.000 25.88000 ? 90  ASP B CG  1 
ATOM   4048 O  OD1 . ASP B 1 90  ? 48.89100  24.17000  66.79800 1.000 29.10000 ? 90  ASP B OD1 1 
ATOM   4049 O  OD2 . ASP B 1 90  ? 50.69600  23.02800  67.22800 1.000 28.84000 ? 90  ASP B OD2 1 
ATOM   4050 N  N   . MET B 1 91  ? 50.57000  24.08600  61.92100 1.000 18.33000 ? 91  MET B N   1 
ATOM   4051 C  CA  . MET B 1 91  ? 51.14500  24.55400  60.66500 1.000 18.84000 ? 91  MET B CA  1 
ATOM   4052 C  C   . MET B 1 91  ? 50.05500  24.94300  59.66800 1.000 21.41000 ? 91  MET B C   1 
ATOM   4053 O  O   . MET B 1 91  ? 50.26800  25.82200  58.81900 1.000 17.22000 ? 91  MET B O   1 
ATOM   4054 C  CB  . MET B 1 91  ? 52.05700  23.47200  60.08800 1.000 18.90000 ? 91  MET B CB  1 
ATOM   4055 C  CG  . MET B 1 91  ? 53.29400  23.17300  60.95600 1.000 19.22000 ? 91  MET B CG  1 
ATOM   4056 S  SD  . MET B 1 91  ? 54.30400  24.64800  61.15400 1.000 27.48000 ? 91  MET B SD  1 
ATOM   4057 C  CE  . MET B 1 91  ? 53.97000  25.05600  62.86100 1.000 26.97000 ? 91  MET B CE  1 
ATOM   4058 N  N   . ARG B 1 92  ? 48.87700  24.32100  59.78000 1.000 20.14000 ? 92  ARG B N   1 
ATOM   4059 C  CA  . ARG B 1 92  ? 47.75600  24.67500  58.91300 1.000 14.70000 ? 92  ARG B CA  1 
ATOM   4060 C  C   . ARG B 1 92  ? 47.39000  26.14900  59.06200 1.000 14.76000 ? 92  ARG B C   1 
ATOM   4061 O  O   . ARG B 1 92  ? 47.21300  26.85500  58.06100 1.000 17.25000 ? 92  ARG B O   1 
ATOM   4062 C  CB  . ARG B 1 92  ? 46.56300  23.77400  59.22200 1.000 15.21000 ? 92  ARG B CB  1 
ATOM   4063 C  CG  . ARG B 1 92  ? 45.29900  24.10600  58.45000 1.000 13.88000 ? 92  ARG B CG  1 
ATOM   4064 C  CD  . ARG B 1 92  ? 45.48800  23.75100  56.98300 1.000 16.34000 ? 92  ARG B CD  1 
ATOM   4065 N  NE  . ARG B 1 92  ? 45.44400  22.31000  56.74600 1.000 17.97000 ? 92  ARG B NE  1 
ATOM   4066 C  CZ  . ARG B 1 92  ? 44.39600  21.66700  56.23600 1.000 18.14000 ? 92  ARG B CZ  1 
ATOM   4067 N  NH1 . ARG B 1 92  ? 43.28700  22.33400  55.91500 1.000 14.73000 ? 92  ARG B NH1 1 
ATOM   4068 N  NH2 . ARG B 1 92  ? 44.46100  20.35400  56.03900 1.000 15.80000 ? 92  ARG B NH2 1 
ATOM   4069 N  N   . VAL B 1 93  ? 47.31600  26.64700  60.30100 1.000 15.48000 ? 93  VAL B N   1 
ATOM   4070 C  CA  . VAL B 1 93  ? 46.89700  28.03400  60.47900 1.000 16.73000 ? 93  VAL B CA  1 
ATOM   4071 C  C   . VAL B 1 93  ? 47.93900  28.99800  59.93500 1.000 16.21000 ? 93  VAL B C   1 
ATOM   4072 O  O   . VAL B 1 93  ? 47.58700  30.08900  59.47700 1.000 17.55000 ? 93  VAL B O   1 
ATOM   4073 C  CB  . VAL B 1 93  ? 46.54200  28.35600  61.94800 1.000 17.00000 ? 93  VAL B CB  1 
ATOM   4074 C  CG1 . VAL B 1 93  ? 45.33300  27.50200  62.41400 1.000 17.38000 ? 93  VAL B CG1 1 
ATOM   4075 C  CG2 . VAL B 1 93  ? 47.73000  28.18400  62.88200 1.000 20.93000 ? 93  VAL B CG2 1 
ATOM   4076 N  N   . ARG B 1 94  ? 49.22400  28.62300  59.95000 1.000 16.02000 ? 94  ARG B N   1 
ATOM   4077 C  CA  . ARG B 1 94  ? 50.22400  29.46200  59.29200 1.000 16.20000 ? 94  ARG B CA  1 
ATOM   4078 C  C   . ARG B 1 94  ? 50.04400  29.46400  57.77700 1.000 15.69000 ? 94  ARG B C   1 
ATOM   4079 O  O   . ARG B 1 94  ? 50.21400  30.50500  57.13200 1.000 15.83000 ? 94  ARG B O   1 
ATOM   4080 C  CB  . ARG B 1 94  ? 51.64000  29.00500  59.65600 1.000 18.32000 ? 94  ARG B CB  1 
ATOM   4081 C  CG  . ARG B 1 94  ? 51.89600  28.87500  61.15300 1.000 22.46000 ? 94  ARG B CG  1 
ATOM   4082 C  CD  . ARG B 1 94  ? 53.32000  29.29600  61.49600 1.000 33.06000 ? 94  ARG B CD  1 
ATOM   4083 N  NE  . ARG B 1 94  ? 53.46000  30.74900  61.43600 1.000 30.57000 ? 94  ARG B NE  1 
ATOM   4084 C  CZ  . ARG B 1 94  ? 54.61100  31.38800  61.25200 1.000 30.33000 ? 94  ARG B CZ  1 
ATOM   4085 N  NH1 . ARG B 1 94  ? 55.73800  30.70900  61.10700 1.000 26.61000 ? 94  ARG B NH1 1 
ATOM   4086 N  NH2 . ARG B 1 94  ? 54.62800  32.70900  61.21200 1.000 32.03000 ? 94  ARG B NH2 1 
ATOM   4087 N  N   . ASP B 1 95  ? 49.72400  28.31300  57.18200 1.000 16.88000 ? 95  ASP B N   1 
ATOM   4088 C  CA  . ASP B 1 95  ? 49.41600  28.30700  55.75000 1.000 12.28000 ? 95  ASP B CA  1 
ATOM   4089 C  C   . ASP B 1 95  ? 48.14900  29.10100  55.45100 1.000 16.32000 ? 95  ASP B C   1 
ATOM   4090 O  O   . ASP B 1 95  ? 48.03400  29.70400  54.37500 1.000 17.05000 ? 95  ASP B O   1 
ATOM   4091 C  CB  . ASP B 1 95  ? 49.26400  26.88100  55.23800 1.000 14.19000 ? 95  ASP B CB  1 
ATOM   4092 C  CG  . ASP B 1 95  ? 50.56200  26.31400  54.72700 1.000 18.41000 ? 95  ASP B CG  1 
ATOM   4093 O  OD1 . ASP B 1 95  ? 51.60700  26.93100  55.02100 1.000 17.87000 ? 95  ASP B OD1 1 
ATOM   4094 O  OD2 . ASP B 1 95  ? 50.53100  25.27200  54.02600 1.000 17.27000 ? 95  ASP B OD2 1 
ATOM   4095 N  N   . MET B 1 96  ? 47.18300  29.10700  56.37500 1.000 15.23000 ? 96  MET B N   1 
ATOM   4096 C  CA  . MET B 1 96  ? 46.00500  29.94300  56.15800 1.000 15.18000 ? 96  MET B CA  1 
ATOM   4097 C  C   . MET B 1 96  ? 46.37000  31.42300  56.24000 1.000 19.83000 ? 96  MET B C   1 
ATOM   4098 O  O   . MET B 1 96  ? 45.95400  32.21500  55.38200 1.000 17.56000 ? 96  MET B O   1 
ATOM   4099 C  CB  . MET B 1 96  ? 44.90300  29.57900  57.15200 1.000 14.49000 ? 96  MET B CB  1 
ATOM   4100 C  CG  . MET B 1 96  ? 44.33200  28.17600  56.91300 1.000 16.61000 ? 96  MET B CG  1 
ATOM   4101 S  SD  . MET B 1 96  ? 43.36400  27.53400  58.29600 1.000 17.34000 ? 96  MET B SD  1 
ATOM   4102 C  CE  . MET B 1 96  ? 42.05700  28.75900  58.38300 1.000 17.38000 ? 96  MET B CE  1 
ATOM   4103 N  N   . ASP B 1 97  ? 47.18200  31.80700  57.23800 1.000 16.40000 ? 97  ASP B N   1 
ATOM   4104 C  CA  . ASP B 1 97  ? 47.69600  33.17600  57.29700 1.000 17.34000 ? 97  ASP B CA  1 
ATOM   4105 C  C   . ASP B 1 97  ? 48.37400  33.56900  55.99000 1.000 15.71000 ? 97  ASP B C   1 
ATOM   4106 O  O   . ASP B 1 97  ? 48.12900  34.65500  55.45700 1.000 18.86000 ? 97  ASP B O   1 
ATOM   4107 C  CB  . ASP B 1 97  ? 48.68900  33.34100  58.45300 1.000 17.20000 ? 97  ASP B CB  1 
ATOM   4108 C  CG  . ASP B 1 97  ? 48.05200  33.18800  59.82300 1.000 22.95000 ? 97  ASP B CG  1 
ATOM   4109 O  OD1 . ASP B 1 97  ? 46.80400  33.28700  59.94700 1.000 17.12000 ? 97  ASP B OD1 1 
ATOM   4110 O  OD2 . ASP B 1 97  ? 48.82400  32.98600  60.79400 1.000 22.29000 ? 97  ASP B OD2 1 
ATOM   4111 N  N   . ALA B 1 98  ? 49.24700  32.70300  55.46400 1.000 15.72000 ? 98  ALA B N   1 
ATOM   4112 C  CA  . ALA B 1 98  ? 49.97400  33.05100  54.24500 1.000 20.94000 ? 98  ALA B CA  1 
ATOM   4113 C  C   . ALA B 1 98  ? 49.02500  33.25600  53.07200 1.000 19.64000 ? 98  ALA B C   1 
ATOM   4114 O  O   . ALA B 1 98  ? 49.30900  34.05900  52.17500 1.000 16.85000 ? 98  ALA B O   1 
ATOM   4115 C  CB  . ALA B 1 98  ? 51.01200  31.97400  53.90900 1.000 18.52000 ? 98  ALA B CB  1 
ATOM   4116 N  N   . ASN B 1 99  ? 47.88700  32.57300  53.07700 1.000 17.13000 ? 99  ASN B N   1 
ATOM   4117 C  CA  . ASN B 1 99  ? 46.89800  32.68600  52.00900 1.000 19.28000 ? 99  ASN B CA  1 
ATOM   4118 C  C   . ASN B 1 99  ? 45.82900  33.74600  52.27700 1.000 17.79000 ? 99  ASN B C   1 
ATOM   4119 O  O   . ASN B 1 99  ? 44.90300  33.89400  51.47000 1.000 14.42000 ? 99  ASN B O   1 
ATOM   4120 C  CB  . ASN B 1 99  ? 46.22700  31.32700  51.79000 1.000 17.38000 ? 99  ASN B CB  1 
ATOM   4121 C  CG  . ASN B 1 99  ? 45.52600  31.22700  50.44100 1.000 18.35000 ? 99  ASN B CG  1 
ATOM   4122 O  OD1 . ASN B 1 99  ? 45.96500  31.81600  49.45000 1.000 17.05000 ? 99  ASN B OD1 1 
ATOM   4123 N  ND2 . ASN B 1 99  ? 44.42000  30.48600  50.40500 1.000 18.64000 ? 99  ASN B ND2 1 
ATOM   4124 N  N   . GLY B 1 100 ? 45.92100  34.47700  53.38400 1.000 19.56000 ? 100 GLY B N   1 
ATOM   4125 C  CA  . GLY B 1 100 ? 44.88500  35.43800  53.72000 1.000 21.11000 ? 100 GLY B CA  1 
ATOM   4126 C  C   . GLY B 1 100 ? 43.55500  34.84100  54.13200 1.000 16.75000 ? 100 GLY B C   1 
ATOM   4127 O  O   . GLY B 1 100 ? 42.53400  35.53100  54.04200 1.000 19.44000 ? 100 GLY B O   1 
ATOM   4128 N  N   . THR B 1 101 ? 43.53300  33.58700  54.60000 1.000 14.92000 ? 101 THR B N   1 
ATOM   4129 C  CA  . THR B 1 101 ? 42.29600  32.85800  54.88500 1.000 14.70000 ? 101 THR B CA  1 
ATOM   4130 C  C   . THR B 1 101 ? 42.00200  32.93600  56.37500 1.000 17.78000 ? 101 THR B C   1 
ATOM   4131 O  O   . THR B 1 101 ? 42.78200  32.43200  57.18800 1.000 18.81000 ? 101 THR B O   1 
ATOM   4132 C  CB  . THR B 1 101 ? 42.39800  31.38500  54.47900 1.000 16.90000 ? 101 THR B CB  1 
ATOM   4133 O  OG1 . THR B 1 101 ? 42.87900  31.26500  53.13300 1.000 18.11000 ? 101 THR B OG1 1 
ATOM   4134 C  CG2 . THR B 1 101 ? 41.02000  30.70500  54.58600 1.000 18.87000 ? 101 THR B CG2 1 
ATOM   4135 N  N   . LEU B 1 102 ? 40.86600  33.53800  56.72900 1.000 19.02000 ? 102 LEU B N   1 
ATOM   4136 C  CA  . LEU B 1 102 ? 40.52600  33.69200  58.13800 1.000 17.48000 ? 102 LEU B CA  1 
ATOM   4137 C  C   . LEU B 1 102 ? 40.08300  32.36600  58.74300 1.000 15.91000 ? 102 LEU B C   1 
ATOM   4138 O  O   . LEU B 1 102 ? 40.53200  31.98400  59.83200 1.000 18.37000 ? 102 LEU B O   1 
ATOM   4139 C  CB  . LEU B 1 102 ? 39.43700  34.75300  58.29600 1.000 16.52000 ? 102 LEU B CB  1 
ATOM   4140 C  CG  . LEU B 1 102 ? 38.83400  34.85300  59.69500 1.000 19.51000 ? 102 LEU B CG  1 
ATOM   4141 C  CD1 . LEU B 1 102 ? 39.87300  35.33900  60.67900 1.000 19.64000 ? 102 LEU B CD1 1 
ATOM   4142 C  CD2 . LEU B 1 102 ? 37.62200  35.77400  59.68100 1.000 20.45000 ? 102 LEU B CD2 1 
ATOM   4143 N  N   . ALA B 1 103 ? 39.21000  31.64400  58.05100 1.000 14.42000 ? 103 ALA B N   1 
ATOM   4144 C  CA  . ALA B 1 103 ? 38.62600  30.44100  58.61300 1.000 16.51000 ? 103 ALA B CA  1 
ATOM   4145 C  C   . ALA B 1 103 ? 38.45300  29.39100  57.53100 1.000 13.84000 ? 103 ALA B C   1 
ATOM   4146 O  O   . ALA B 1 103 ? 38.27300  29.71200  56.35400 1.000 15.83000 ? 103 ALA B O   1 
ATOM   4147 C  CB  . ALA B 1 103 ? 37.27800  30.73500  59.28100 1.000 16.70000 ? 103 ALA B CB  1 
ATOM   4148 N  N   . ALA B 1 104 ? 38.52000  28.13100  57.94600 1.000 14.93000 ? 104 ALA B N   1 
ATOM   4149 C  CA  . ALA B 1 104 ? 38.36900  26.99300  57.05200 1.000 15.83000 ? 104 ALA B CA  1 
ATOM   4150 C  C   . ALA B 1 104 ? 37.36900  26.02400  57.66000 1.000 15.89000 ? 104 ALA B C   1 
ATOM   4151 O  O   . ALA B 1 104 ? 37.03300  26.11000  58.84300 1.000 16.37000 ? 104 ALA B O   1 
ATOM   4152 C  CB  . ALA B 1 104 ? 39.70900  26.28800  56.78800 1.000 15.47000 ? 104 ALA B CB  1 
ATOM   4153 N  N   . THR B 1 105 ? 36.87800  25.10200  56.83200 1.000 15.37000 ? 105 THR B N   1 
ATOM   4154 C  CA  . THR B 1 105 ? 35.82700  24.17300  57.23200 1.000 13.90000 ? 105 THR B CA  1 
ATOM   4155 C  C   . THR B 1 105 ? 36.29300  22.77500  56.84600 1.000 17.18000 ? 105 THR B C   1 
ATOM   4156 O  O   . THR B 1 105 ? 36.32700  22.45300  55.65700 1.000 14.87000 ? 105 THR B O   1 
ATOM   4157 C  CB  . THR B 1 105 ? 34.51300  24.53800  56.54600 1.000 13.24000 ? 105 THR B CB  1 
ATOM   4158 O  OG1 . THR B 1 105 ? 34.20700  25.91200  56.82500 1.000 16.16000 ? 105 THR B OG1 1 
ATOM   4159 C  CG2 . THR B 1 105 ? 33.38300  23.67000  57.05800 1.000 16.07000 ? 105 THR B CG2 1 
ATOM   4160 N  N   . LEU B 1 106 ? 36.66000  21.95100  57.83700 1.000 11.83000 ? 106 LEU B N   1 
ATOM   4161 C  CA  . LEU B 1 106 ? 37.51800  20.78400  57.58600 1.000 14.90000 ? 106 LEU B CA  1 
ATOM   4162 C  C   . LEU B 1 106 ? 36.70400  19.50900  57.34300 1.000 18.04000 ? 106 LEU B C   1 
ATOM   4163 O  O   . LEU B 1 106 ? 36.23100  18.87400  58.28900 1.000 15.92000 ? 106 LEU B O   1 
ATOM   4164 C  CB  . LEU B 1 106 ? 38.48500  20.58100  58.74700 1.000 16.18000 ? 106 LEU B CB  1 
ATOM   4165 C  CG  . LEU B 1 106 ? 39.47800  21.71600  59.04300 1.000 14.18000 ? 106 LEU B CG  1 
ATOM   4166 C  CD1 . LEU B 1 106 ? 40.33700  21.34300  60.23900 1.000 20.01000 ? 106 LEU B CD1 1 
ATOM   4167 C  CD2 . LEU B 1 106 ? 40.35500  22.00500  57.83700 1.000 10.51000 ? 106 LEU B CD2 1 
ATOM   4168 N  N   . PHE B 1 107 ? 36.58800  19.10800  56.06900 1.000 14.97000 ? 107 PHE B N   1 
ATOM   4169 C  CA  . PHE B 1 107 ? 36.03500  17.80800  55.69900 1.000 16.60000 ? 107 PHE B CA  1 
ATOM   4170 C  C   . PHE B 1 107 ? 37.05900  16.69500  55.91400 1.000 15.02000 ? 107 PHE B C   1 
ATOM   4171 O  O   . PHE B 1 107 ? 38.25100  16.86400  55.64100 1.000 17.13000 ? 107 PHE B O   1 
ATOM   4172 C  CB  . PHE B 1 107 ? 35.59200  17.81300  54.23000 1.000 14.10000 ? 107 PHE B CB  1 
ATOM   4173 C  CG  . PHE B 1 107 ? 34.32600  18.59200  53.97400 1.000 14.15000 ? 107 PHE B CG  1 
ATOM   4174 C  CD1 . PHE B 1 107 ? 34.37900  19.95500  53.72400 1.000 12.00000 ? 107 PHE B CD1 1 
ATOM   4175 C  CD2 . PHE B 1 107 ? 33.08200  17.95400  53.96000 1.000 12.91000 ? 107 PHE B CD2 1 
ATOM   4176 C  CE1 . PHE B 1 107 ? 33.20600  20.67600  53.48300 1.000 14.28000 ? 107 PHE B CE1 1 
ATOM   4177 C  CE2 . PHE B 1 107 ? 31.90700  18.66700  53.72100 1.000 11.79000 ? 107 PHE B CE2 1 
ATOM   4178 C  CZ  . PHE B 1 107 ? 31.96000  20.01900  53.49100 1.000 15.09000 ? 107 PHE B CZ  1 
ATOM   4179 N  N   . ALA B 1 108 ? 36.57800  15.53300  56.35300 1.000 17.05000 ? 108 ALA B N   1 
ATOM   4180 C  CA  . ALA B 1 108 ? 37.43000  14.43600  56.80500 1.000 15.46000 ? 108 ALA B CA  1 
ATOM   4181 C  C   . ALA B 1 108 ? 38.08600  13.68700  55.65300 1.000 17.19000 ? 108 ALA B C   1 
ATOM   4182 O  O   . ALA B 1 108 ? 37.58200  13.64900  54.53300 1.000 16.10000 ? 108 ALA B O   1 
ATOM   4183 C  CB  . ALA B 1 108 ? 36.61600  13.42200  57.60200 1.000 13.40000 ? 108 ALA B CB  1 
ATOM   4184 N  N   . THR B 1 109 ? 39.20500  13.02700  55.96700 1.000 15.98000 ? 109 THR B N   1 
ATOM   4185 C  CA  . THR B 1 109 ? 39.81900  12.08900  55.03000 1.000 15.45000 ? 109 THR B CA  1 
ATOM   4186 C  C   . THR B 1 109 ? 39.49600  10.64000  55.39800 1.000 14.84000 ? 109 THR B C   1 
ATOM   4187 O  O   . THR B 1 109 ? 38.76300  9.96500   54.66700 1.000 14.85000 ? 109 THR B O   1 
ATOM   4188 C  CB  . THR B 1 109 ? 41.33100  12.30500  54.97100 1.000 19.89000 ? 109 THR B CB  1 
ATOM   4189 O  OG1 . THR B 1 109 ? 41.59700  13.60600  54.43100 1.000 23.52000 ? 109 THR B OG1 1 
ATOM   4190 C  CG2 . THR B 1 109 ? 41.99200  11.25300  54.08800 1.000 25.31000 ? 109 THR B CG2 1 
ATOM   4191 N  N   . PHE B 1 110 ? 40.02000  10.15400  56.53100 1.000 13.39000 ? 110 PHE B N   1 
ATOM   4192 C  CA  . PHE B 1 110 ? 39.92700  8.72500   56.83100 1.000 15.54000 ? 110 PHE B CA  1 
ATOM   4193 C  C   . PHE B 1 110 ? 38.49700  8.19900   56.91000 1.000 15.31000 ? 110 PHE B C   1 
ATOM   4194 O  O   . PHE B 1 110 ? 38.21400  7.16100   56.28900 1.000 15.66000 ? 110 PHE B O   1 
ATOM   4195 C  CB  . PHE B 1 110 ? 40.68200  8.39900   58.12400 1.000 17.31000 ? 110 PHE B CB  1 
ATOM   4196 C  CG  . PHE B 1 110 ? 40.28000  7.07900   58.73000 1.000 18.19000 ? 110 PHE B CG  1 
ATOM   4197 C  CD1 . PHE B 1 110 ? 40.65000  5.88300   58.12500 1.000 20.14000 ? 110 PHE B CD1 1 
ATOM   4198 C  CD2 . PHE B 1 110 ? 39.51000  7.03800   59.88000 1.000 16.78000 ? 110 PHE B CD2 1 
ATOM   4199 C  CE1 . PHE B 1 110 ? 40.26400  4.66600   58.66600 1.000 17.68000 ? 110 PHE B CE1 1 
ATOM   4200 C  CE2 . PHE B 1 110 ? 39.11400  5.81900   60.43400 1.000 22.28000 ? 110 PHE B CE2 1 
ATOM   4201 C  CZ  . PHE B 1 110 ? 39.49300  4.63100   59.82500 1.000 19.99000 ? 110 PHE B CZ  1 
ATOM   4202 N  N   . PRO B 1 111 ? 37.56500  8.80300   57.65500 1.000 15.96000 ? 111 PRO B N   1 
ATOM   4203 C  CA  . PRO B 1 111 ? 36.21100  8.22500   57.69500 1.000 15.77000 ? 111 PRO B CA  1 
ATOM   4204 C  C   . PRO B 1 111 ? 35.44200  8.39600   56.39800 1.000 16.61000 ? 111 PRO B C   1 
ATOM   4205 O  O   . PRO B 1 111 ? 34.34200  7.84300   56.27200 1.000 16.83000 ? 111 PRO B O   1 
ATOM   4206 C  CB  . PRO B 1 111 ? 35.53300  8.97900   58.84900 1.000 18.98000 ? 111 PRO B CB  1 
ATOM   4207 C  CG  . PRO B 1 111 ? 36.27300  10.25400  58.97200 1.000 15.10000 ? 111 PRO B CG  1 
ATOM   4208 C  CD  . PRO B 1 111 ? 37.69200  9.98300   58.52700 1.000 15.97000 ? 111 PRO B CD  1 
ATOM   4209 N  N   . GLY B 1 112 ? 36.00600  9.10100   55.41900 1.000 17.89000 ? 112 GLY B N   1 
ATOM   4210 C  CA  . GLY B 1 112 ? 35.23300  9.60900   54.30500 1.000 16.14000 ? 112 GLY B CA  1 
ATOM   4211 C  C   . GLY B 1 112 ? 34.77100  11.01500  54.62600 1.000 14.92000 ? 112 GLY B C   1 
ATOM   4212 O  O   . GLY B 1 112 ? 34.39500  11.29300  55.76900 1.000 14.99000 ? 112 GLY B O   1 
ATOM   4213 N  N   . PHE B 1 113 ? 34.79400  11.92700  53.65600 1.000 17.99000 ? 113 PHE B N   1 
ATOM   4214 C  CA  . PHE B 1 113 ? 34.37600  13.28200  53.98600 1.000 18.08000 ? 113 PHE B CA  1 
ATOM   4215 C  C   . PHE B 1 113 ? 32.90200  13.34100  54.37000 1.000 16.65000 ? 113 PHE B C   1 
ATOM   4216 O  O   . PHE B 1 113 ? 32.46800  14.33100  54.96200 1.000 15.58000 ? 113 PHE B O   1 
ATOM   4217 C  CB  . PHE B 1 113 ? 34.67900  14.22800  52.82500 1.000 18.27000 ? 113 PHE B CB  1 
ATOM   4218 C  CG  . PHE B 1 113 ? 34.08900  13.79300  51.53300 1.000 21.29000 ? 113 PHE B CG  1 
ATOM   4219 C  CD1 . PHE B 1 113 ? 32.74800  14.00000  51.26800 1.000 20.66000 ? 113 PHE B CD1 1 
ATOM   4220 C  CD2 . PHE B 1 113 ? 34.86700  13.16200  50.58300 1.000 23.80000 ? 113 PHE B CD2 1 
ATOM   4221 C  CE1 . PHE B 1 113 ? 32.18700  13.58100  50.06800 1.000 23.69000 ? 113 PHE B CE1 1 
ATOM   4222 C  CE2 . PHE B 1 113 ? 34.31500  12.73600  49.38900 1.000 28.73000 ? 113 PHE B CE2 1 
ATOM   4223 C  CZ  . PHE B 1 113 ? 32.97100  12.94700  49.13300 1.000 26.95000 ? 113 PHE B CZ  1 
ATOM   4224 N  N   . ALA B 1 114 ? 32.12800  12.30600  54.04500 1.000 15.55000 ? 114 ALA B N   1 
ATOM   4225 C  CA  . ALA B 1 114 ? 30.75500  12.16900  54.51800 1.000 17.12000 ? 114 ALA B CA  1 
ATOM   4226 C  C   . ALA B 1 114 ? 30.58700  10.93100  55.39800 1.000 15.47000 ? 114 ALA B C   1 
ATOM   4227 O  O   . ALA B 1 114 ? 29.45600  10.49200  55.64300 1.000 17.69000 ? 114 ALA B O   1 
ATOM   4228 C  CB  . ALA B 1 114 ? 29.78000  12.13700  53.33800 1.000 18.21000 ? 114 ALA B CB  1 
ATOM   4229 N  N   . GLY B 1 115 ? 31.69300  10.35200  55.87100 1.000 13.33000 ? 115 GLY B N   1 
ATOM   4230 C  CA  . GLY B 1 115 ? 31.61500  9.22500   56.77800 1.000 12.81000 ? 115 GLY B CA  1 
ATOM   4231 C  C   . GLY B 1 115 ? 31.27300  7.89800   56.13800 1.000 18.82000 ? 115 GLY B C   1 
ATOM   4232 O  O   . GLY B 1 115 ? 31.02100  6.92100   56.86500 1.000 15.50000 ? 115 GLY B O   1 
ATOM   4233 N  N   . THR B 1 116 ? 31.26400  7.81800   54.80500 1.000 14.06000 ? 116 THR B N   1 
ATOM   4234 C  CA  . THR B 1 116 ? 30.83800  6.57600   54.16400 1.000 17.45000 ? 116 THR B CA  1 
ATOM   4235 C  C   . THR B 1 116 ? 31.84200  5.45200   54.35400 1.000 16.86000 ? 116 THR B C   1 
ATOM   4236 O  O   . THR B 1 116 ? 31.45800  4.28400   54.23700 1.000 20.29000 ? 116 THR B O   1 
ATOM   4237 C  CB  . THR B 1 116 ? 30.58000  6.76500   52.66000 1.000 17.98000 ? 116 THR B CB  1 
ATOM   4238 O  OG1 . THR B 1 116 ? 31.81500  6.95500   51.97300 1.000 21.55000 ? 116 THR B OG1 1 
ATOM   4239 C  CG2 . THR B 1 116 ? 29.69300  7.95800   52.40500 1.000 15.59000 ? 116 THR B CG2 1 
ATOM   4240 N  N   . HIS B 1 117 ? 33.11300  5.75400   54.64700 1.000 14.74000 ? 117 HIS B N   1 
ATOM   4241 C  CA  . HIS B 1 117 ? 34.03300  4.65300   54.91600 1.000 19.04000 ? 117 HIS B CA  1 
ATOM   4242 C  C   . HIS B 1 117 ? 33.63800  3.93400   56.19400 1.000 18.48000 ? 117 HIS B C   1 
ATOM   4243 O  O   . HIS B 1 117 ? 33.59200  2.69700   56.22900 1.000 20.95000 ? 117 HIS B O   1 
ATOM   4244 C  CB  . HIS B 1 117 ? 35.47800  5.13800   54.99200 1.000 16.60000 ? 117 HIS B CB  1 
ATOM   4245 C  CG  . HIS B 1 117 ? 36.45600  4.05000   55.30700 1.000 24.52000 ? 117 HIS B CG  1 
ATOM   4246 N  ND1 . HIS B 1 117 ? 36.46400  2.84000   54.64200 1.000 22.69000 ? 117 HIS B ND1 1 
ATOM   4247 C  CD2 . HIS B 1 117 ? 37.45900  3.98800   56.21600 1.000 20.79000 ? 117 HIS B CD2 1 
ATOM   4248 C  CE1 . HIS B 1 117 ? 37.42700  2.07900   55.13200 1.000 23.66000 ? 117 HIS B CE1 1 
ATOM   4249 N  NE2 . HIS B 1 117 ? 38.04600  2.75100   56.08800 1.000 23.40000 ? 117 HIS B NE2 1 
ATOM   4250 N  N   . LEU B 1 118 ? 33.28800  4.69100   57.23700 1.000 16.39000 ? 118 LEU B N   1 
ATOM   4251 C  CA  . LEU B 1 118 ? 32.85500  4.05300   58.47800 1.000 17.26000 ? 118 LEU B CA  1 
ATOM   4252 C  C   . LEU B 1 118 ? 31.55600  3.29500   58.26100 1.000 23.39000 ? 118 LEU B C   1 
ATOM   4253 O  O   . LEU B 1 118 ? 31.35300  2.20400   58.81300 1.000 21.59000 ? 118 LEU B O   1 
ATOM   4254 C  CB  . LEU B 1 118 ? 32.69700  5.10100   59.58100 1.000 15.54000 ? 118 LEU B CB  1 
ATOM   4255 C  CG  . LEU B 1 118 ? 33.95300  5.91400   59.93200 1.000 20.71000 ? 118 LEU B CG  1 
ATOM   4256 C  CD1 . LEU B 1 118 ? 33.64600  6.83200   61.11100 1.000 19.89000 ? 118 LEU B CD1 1 
ATOM   4257 C  CD2 . LEU B 1 118 ? 35.14000  5.01600   60.25700 1.000 18.84000 ? 118 LEU B CD2 1 
ATOM   4258 N  N   . ALA B 1 119 ? 30.67000  3.84600   57.43200 1.000 21.03000 ? 119 ALA B N   1 
ATOM   4259 C  CA  . ALA B 1 119 ? 29.40500  3.17900   57.17300 1.000 22.25000 ? 119 ALA B CA  1 
ATOM   4260 C  C   . ALA B 1 119 ? 29.58200  1.89100   56.37400 1.000 23.84000 ? 119 ALA B C   1 
ATOM   4261 O  O   . ALA B 1 119 ? 28.68100  1.05000   56.37700 1.000 24.63000 ? 119 ALA B O   1 
ATOM   4262 C  CB  . ALA B 1 119 ? 28.45900  4.13800   56.44900 1.000 18.52000 ? 119 ALA B CB  1 
ATOM   4263 N  N   . SER B 1 120 ? 30.71100  1.71400   55.69200 1.000 24.42000 ? 120 SER B N   1 
ATOM   4264 C  CA  . SER B 1 120 ? 30.91100  0.51500   54.88700 1.000 24.34000 ? 120 SER B CA  1 
ATOM   4265 C  C   . SER B 1 120 ? 31.36800  -0.68000  55.71100 1.000 29.57000 ? 120 SER B C   1 
ATOM   4266 O  O   . SER B 1 120 ? 31.36800  -1.80500  55.19700 1.000 28.14000 ? 120 SER B O   1 
ATOM   4267 C  CB  . SER B 1 120 ? 31.93300  0.78100   53.77300 1.000 27.31000 ? 120 SER B CB  1 
ATOM   4268 O  OG  . SER B 1 120 ? 33.26200  0.84300   54.28200 1.000 30.06000 ? 120 SER B OG  1 
ATOM   4269 N  N   . LEU B 1 121 ? 31.73900  -0.46700  56.97700 1.000 24.26000 ? 121 LEU B N   1 
ATOM   4270 C  CA  . LEU B 1 121 ? 32.39500  -1.55900  57.67400 1.000 24.88000 ? 121 LEU B CA  1 
ATOM   4271 C  C   . LEU B 1 121 ? 31.38300  -2.39200  58.45700 1.000 20.81000 ? 121 LEU B C   1 
ATOM   4272 O  O   . LEU B 1 121 ? 30.31600  -1.89700  58.82700 1.000 22.61000 ? 121 LEU B O   1 
ATOM   4273 C  CB  . LEU B 1 121 ? 33.46200  -1.00800  58.61000 1.000 22.07000 ? 121 LEU B CB  1 
ATOM   4274 C  CG  . LEU B 1 121 ? 34.46600  -0.13200  57.83600 1.000 24.72000 ? 121 LEU B CG  1 
ATOM   4275 C  CD1 . LEU B 1 121 ? 35.39000  0.61100   58.78100 1.000 21.68000 ? 121 LEU B CD1 1 
ATOM   4276 C  CD2 . LEU B 1 121 ? 35.26700  -0.96700  56.85200 1.000 21.69000 ? 121 LEU B CD2 1 
ATOM   4277 N  N   . PRO B 1 122 ? 31.69800  -3.67000  58.70600 1.000 23.07000 ? 122 PRO B N   1 
ATOM   4278 C  CA  . PRO B 1 122 ? 30.70000  -4.57600  59.29800 1.000 24.29000 ? 122 PRO B CA  1 
ATOM   4279 C  C   . PRO B 1 122 ? 30.39700  -4.35500  60.77400 1.000 22.03000 ? 122 PRO B C   1 
ATOM   4280 O  O   . PRO B 1 122 ? 29.24800  -4.54900  61.18900 1.000 23.58000 ? 122 PRO B O   1 
ATOM   4281 C  CB  . PRO B 1 122 ? 31.31600  -5.96400  59.07300 1.000 22.56000 ? 122 PRO B CB  1 
ATOM   4282 C  CG  . PRO B 1 122 ? 32.77800  -5.71700  58.94200 1.000 23.18000 ? 122 PRO B CG  1 
ATOM   4283 C  CD  . PRO B 1 122 ? 32.88500  -4.39900  58.22400 1.000 21.77000 ? 122 PRO B CD  1 
ATOM   4284 N  N   . ASP B 1 123 ? 31.38800  -3.99100  61.58600 1.000 22.39000 ? 123 ASP B N   1 
ATOM   4285 C  CA  . ASP B 1 123 ? 31.17000  -3.82400  63.02600 1.000 20.47000 ? 123 ASP B CA  1 
ATOM   4286 C  C   . ASP B 1 123 ? 30.74700  -2.38300  63.28000 1.000 20.85000 ? 123 ASP B C   1 
ATOM   4287 O  O   . ASP B 1 123 ? 31.58300  -1.47900  63.32400 1.000 21.29000 ? 123 ASP B O   1 
ATOM   4288 C  CB  . ASP B 1 123 ? 32.42600  -4.18800  63.81400 1.000 21.25000 ? 123 ASP B CB  1 
ATOM   4289 C  CG  . ASP B 1 123 ? 32.19400  -4.21200  65.32400 1.000 23.59000 ? 123 ASP B CG  1 
ATOM   4290 O  OD1 . ASP B 1 123 ? 31.35800  -3.42700  65.83700 1.000 24.07000 ? 123 ASP B OD1 1 
ATOM   4291 O  OD2 . ASP B 1 123 ? 32.86800  -5.00900  66.01000 1.000 23.44000 ? 123 ASP B OD2 1 
ATOM   4292 N  N   . LYS B 1 124 ? 29.44600  -2.17000  63.48500 1.000 21.26000 ? 124 LYS B N   1 
ATOM   4293 C  CA  . LYS B 1 124 ? 28.93000  -0.81400  63.62400 1.000 21.09000 ? 124 LYS B CA  1 
ATOM   4294 C  C   . LYS B 1 124 ? 29.19000  -0.20900  64.99800 1.000 22.69000 ? 124 LYS B C   1 
ATOM   4295 O  O   . LYS B 1 124 ? 29.13600  1.01500   65.13300 1.000 18.55000 ? 124 LYS B O   1 
ATOM   4296 C  CB  . LYS B 1 124 ? 27.43200  -0.78800  63.32000 1.000 25.29000 ? 124 LYS B CB  1 
ATOM   4297 C  CG  . LYS B 1 124 ? 27.12100  -1.11300  61.87500 1.000 23.35000 ? 124 LYS B CG  1 
ATOM   4298 C  CD  . LYS B 1 124 ? 27.99200  -0.29700  60.92500 1.000 21.44000 ? 124 LYS B CD  1 
ATOM   4299 C  CE  . LYS B 1 124 ? 27.46300  -0.38500  59.49700 1.000 25.59000 ? 124 LYS B CE  1 
ATOM   4300 N  NZ  . LYS B 1 124 ? 27.64800  -1.75000  58.92700 1.000 22.57000 ? 124 LYS B NZ  1 
ATOM   4301 N  N   . LYS B 1 125 ? 29.46300  -1.02100  66.02200 1.000 19.04000 ? 125 LYS B N   1 
ATOM   4302 C  CA  . LYS B 1 125 ? 29.90800  -0.43900  67.28300 1.000 22.08000 ? 125 LYS B CA  1 
ATOM   4303 C  C   . LYS B 1 125 ? 31.26300  0.22700   67.10900 1.000 21.94000 ? 125 LYS B C   1 
ATOM   4304 O  O   . LYS B 1 125 ? 31.48100  1.34400   67.59100 1.000 20.49000 ? 125 LYS B O   1 
ATOM   4305 C  CB  . LYS B 1 125 ? 29.97900  -1.50000  68.38300 1.000 27.14000 ? 125 LYS B CB  1 
ATOM   4306 C  CG  . LYS B 1 125 ? 30.60200  -0.98800  69.68800 1.000 29.05000 ? 125 LYS B CG  1 
ATOM   4307 C  CD  . LYS B 1 125 ? 30.60500  -2.05800  70.78700 1.000 44.36000 ? 125 LYS B CD  1 
ATOM   4308 C  CE  . LYS B 1 125 ? 31.87400  -1.97800  71.64500 1.000 45.31000 ? 125 LYS B CE  1 
ATOM   4309 N  NZ  . LYS B 1 125 ? 31.60700  -1.96200  73.12400 1.000 39.64000 ? 125 LYS B NZ  1 
ATOM   4310 N  N   . LEU B 1 126 ? 32.18400  -0.44000  66.41400 1.000 19.13000 ? 126 LEU B N   1 
ATOM   4311 C  CA  . LEU B 1 126 ? 33.47800  0.17200   66.14400 1.000 19.03000 ? 126 LEU B CA  1 
ATOM   4312 C  C   . LEU B 1 126 ? 33.33900  1.36400   65.20200 1.000 18.53000 ? 126 LEU B C   1 
ATOM   4313 O  O   . LEU B 1 126 ? 34.05300  2.36100   65.34300 1.000 20.13000 ? 126 LEU B O   1 
ATOM   4314 C  CB  . LEU B 1 126 ? 34.43100  -0.86100  65.55900 1.000 20.85000 ? 126 LEU B CB  1 
ATOM   4315 C  CG  . LEU B 1 126 ? 34.85500  -1.94800  66.53600 1.000 19.55000 ? 126 LEU B CG  1 
ATOM   4316 C  CD1 . LEU B 1 126 ? 35.77300  -2.93000  65.82700 1.000 19.29000 ? 126 LEU B CD1 1 
ATOM   4317 C  CD2 . LEU B 1 126 ? 35.53200  -1.32700  67.74400 1.000 22.23000 ? 126 LEU B CD2 1 
ATOM   4318 N  N   . SER B 1 127 ? 32.42400  1.29000   64.23700 1.000 20.28000 ? 127 SER B N   1 
ATOM   4319 C  CA  . SER B 1 127 ? 32.24600  2.42600   63.33800 1.000 20.74000 ? 127 SER B CA  1 
ATOM   4320 C  C   . SER B 1 127 ? 31.67200  3.62800   64.07400 1.000 18.29000 ? 127 SER B C   1 
ATOM   4321 O  O   . SER B 1 127 ? 32.11000  4.76400   63.86100 1.000 18.06000 ? 127 SER B O   1 
ATOM   4322 C  CB  . SER B 1 127 ? 31.36900  2.01600   62.15900 1.000 19.26000 ? 127 SER B CB  1 
ATOM   4323 O  OG  . SER B 1 127 ? 32.14700  1.25700   61.25100 1.000 19.81000 ? 127 SER B OG  1 
ATOM   4324 N  N   . LEU B 1 128 ? 30.70300  3.40000   64.96200 1.000 17.31000 ? 128 LEU B N   1 
ATOM   4325 C  CA  . LEU B 1 128 ? 30.18000  4.49100   65.77700 1.000 17.88000 ? 128 LEU B CA  1 
ATOM   4326 C  C   . LEU B 1 128 ? 31.28600  5.11200   66.62300 1.000 17.68000 ? 128 LEU B C   1 
ATOM   4327 O  O   . LEU B 1 128 ? 31.41800  6.34400   66.69600 1.000 17.99000 ? 128 LEU B O   1 
ATOM   4328 C  CB  . LEU B 1 128 ? 29.04300  3.96900   66.65500 1.000 16.85000 ? 128 LEU B CB  1 
ATOM   4329 C  CG  . LEU B 1 128 ? 28.36500  4.99900   67.55300 1.000 21.93000 ? 128 LEU B CG  1 
ATOM   4330 C  CD1 . LEU B 1 128 ? 27.81300  6.14600   66.71400 1.000 20.66000 ? 128 LEU B CD1 1 
ATOM   4331 C  CD2 . LEU B 1 128 ? 27.26100  4.33500   68.36300 1.000 22.11000 ? 128 LEU B CD2 1 
ATOM   4332 N  N   . ALA B 1 129 ? 32.10000  4.26800   67.26400 1.000 16.60000 ? 129 ALA B N   1 
ATOM   4333 C  CA  . ALA B 1 129 ? 33.19300  4.76700   68.09400 1.000 18.52000 ? 129 ALA B CA  1 
ATOM   4334 C  C   . ALA B 1 129 ? 34.16800  5.61200   67.28200 1.000 16.25000 ? 129 ALA B C   1 
ATOM   4335 O  O   . ALA B 1 129 ? 34.61600  6.66600   67.74400 1.000 17.28000 ? 129 ALA B O   1 
ATOM   4336 C  CB  . ALA B 1 129 ? 33.92400  3.60200   68.76600 1.000 21.14000 ? 129 ALA B CB  1 
ATOM   4337 N  N   . ALA B 1 130 ? 34.49500  5.17100   66.06300 1.000 17.82000 ? 130 ALA B N   1 
ATOM   4338 C  CA  . ALA B 1 130 ? 35.39300  5.94500   65.21200 1.000 16.43000 ? 130 ALA B CA  1 
ATOM   4339 C  C   . ALA B 1 130 ? 34.75700  7.26800   64.79800 1.000 19.07000 ? 130 ALA B C   1 
ATOM   4340 O  O   . ALA B 1 130 ? 35.43800  8.30100   64.73000 1.000 16.15000 ? 130 ALA B O   1 
ATOM   4341 C  CB  . ALA B 1 130 ? 35.78600  5.12200   63.98400 1.000 16.06000 ? 130 ALA B CB  1 
ATOM   4342 N  N   . CYS B 1 131 ? 33.45400  7.26000   64.52100 1.000 16.01000 ? 131 CYS B N   1 
ATOM   4343 C  CA  . CYS B 1 131 ? 32.76800  8.49900   64.18400 1.000 13.64000 ? 131 CYS B CA  1 
ATOM   4344 C  C   . CYS B 1 131 ? 32.83400  9.48500   65.34400 1.000 18.39000 ? 131 CYS B C   1 
ATOM   4345 O  O   . CYS B 1 131 ? 33.16300  10.66600  65.16500 1.000 15.05000 ? 131 CYS B O   1 
ATOM   4346 C  CB  . CYS B 1 131 ? 31.31300  8.19200   63.80900 1.000 13.85000 ? 131 CYS B CB  1 
ATOM   4347 S  SG  . CYS B 1 131 ? 30.40300  9.63900   63.22100 1.000 17.26000 ? 131 CYS B SG  1 
ATOM   4348 N  N   . ARG B 1 132 ? 32.54100  9.01200   66.55600 1.000 16.17000 ? 132 ARG B N   1 
ATOM   4349 C  CA  . ARG B 1 132 ? 32.54000  9.91500   67.69900 1.000 14.10000 ? 132 ARG B CA  1 
ATOM   4350 C  C   . ARG B 1 132 ? 33.94500  10.40400  68.01900 1.000 18.68000 ? 132 ARG B C   1 
ATOM   4351 O  O   . ARG B 1 132 ? 34.13200  11.56900  68.39000 1.000 16.98000 ? 132 ARG B O   1 
ATOM   4352 C  CB  . ARG B 1 132 ? 31.89500  9.21700   68.88700 1.000 15.12000 ? 132 ARG B CB  1 
ATOM   4353 C  CG  . ARG B 1 132 ? 30.42300  8.96100   68.60700 1.000 16.57000 ? 132 ARG B CG  1 
ATOM   4354 C  CD  . ARG B 1 132 ? 29.65100  8.88100   69.88100 1.000 24.62000 ? 132 ARG B CD  1 
ATOM   4355 N  NE  . ARG B 1 132 ? 29.78800  7.55500   70.44800 1.000 29.82000 ? 132 ARG B NE  1 
ATOM   4356 C  CZ  . ARG B 1 132 ? 28.78300  6.85400   70.94500 1.000 32.24000 ? 132 ARG B CZ  1 
ATOM   4357 N  NH1 . ARG B 1 132 ? 27.55600  7.36200   70.95500 1.000 30.04000 ? 132 ARG B NH1 1 
ATOM   4358 N  NH2 . ARG B 1 132 ? 29.01400  5.64600   71.43900 1.000 31.57000 ? 132 ARG B NH2 1 
ATOM   4359 N  N   . ALA B 1 133 ? 34.95200  9.54600   67.84100 1.000 16.69000 ? 133 ALA B N   1 
ATOM   4360 C  CA  . ALA B 1 133 ? 36.31700  9.97700   68.11400 1.000 16.19000 ? 133 ALA B CA  1 
ATOM   4361 C  C   . ALA B 1 133 ? 36.76300  11.03900  67.11600 1.000 14.88000 ? 133 ALA B C   1 
ATOM   4362 O  O   . ALA B 1 133 ? 37.44200  12.00700  67.48800 1.000 15.34000 ? 133 ALA B O   1 
ATOM   4363 C  CB  . ALA B 1 133 ? 37.26700  8.77900   68.07800 1.000 17.11000 ? 133 ALA B CB  1 
ATOM   4364 N  N   . PHE B 1 134 ? 36.39900  10.87000  65.84300 1.000 16.73000 ? 134 PHE B N   1 
ATOM   4365 C  CA  . PHE B 1 134 ? 36.74600  11.87100  64.84100 1.000 11.99000 ? 134 PHE B CA  1 
ATOM   4366 C  C   . PHE B 1 134 ? 36.06200  13.20400  65.13500 1.000 13.94000 ? 134 PHE B C   1 
ATOM   4367 O  O   . PHE B 1 134 ? 36.69800  14.26700  65.08800 1.000 12.84000 ? 134 PHE B O   1 
ATOM   4368 C  CB  . PHE B 1 134 ? 36.37300  11.38700  63.44000 1.000 14.18000 ? 134 PHE B CB  1 
ATOM   4369 C  CG  . PHE B 1 134 ? 36.42700  12.48800  62.41700 1.000 15.21000 ? 134 PHE B CG  1 
ATOM   4370 C  CD1 . PHE B 1 134 ? 37.64400  12.89900  61.89000 1.000 14.97000 ? 134 PHE B CD1 1 
ATOM   4371 C  CD2 . PHE B 1 134 ? 35.27000  13.14600  62.02300 1.000 13.60000 ? 134 PHE B CD2 1 
ATOM   4372 C  CE1 . PHE B 1 134 ? 37.70000  13.94100  60.97000 1.000 18.86000 ? 134 PHE B CE1 1 
ATOM   4373 C  CE2 . PHE B 1 134 ? 35.31400  14.17900  61.11200 1.000 17.16000 ? 134 PHE B CE2 1 
ATOM   4374 C  CZ  . PHE B 1 134 ? 36.54000  14.58800  60.58800 1.000 16.69000 ? 134 PHE B CZ  1 
ATOM   4375 N  N   . ASN B 1 135 ? 34.75500  13.16900  65.41100 1.000 15.69000 ? 135 ASN B N   1 
ATOM   4376 C  CA  . ASN B 1 135 ? 34.04900  14.39200  65.78600 1.000 15.50000 ? 135 ASN B CA  1 
ATOM   4377 C  C   . ASN B 1 135 ? 34.66400  15.03000  67.02800 1.000 16.19000 ? 135 ASN B C   1 
ATOM   4378 O  O   . ASN B 1 135 ? 34.81000  16.25300  67.09200 1.000 14.12000 ? 135 ASN B O   1 
ATOM   4379 C  CB  . ASN B 1 135 ? 32.57000  14.11000  66.02700 1.000 12.26000 ? 135 ASN B CB  1 
ATOM   4380 C  CG  . ASN B 1 135 ? 31.78900  13.93400  64.74000 1.000 14.15000 ? 135 ASN B CG  1 
ATOM   4381 O  OD1 . ASN B 1 135 ? 32.21800  14.37600  63.67800 1.000 13.28000 ? 135 ASN B OD1 1 
ATOM   4382 N  ND2 . ASN B 1 135 ? 30.61800  13.30000  64.83500 1.000 12.13000 ? 135 ASN B ND2 1 
ATOM   4383 N  N   . ASP B 1 136 ? 35.02200  14.22500  68.03100 1.000 15.40000 ? 136 ASP B N   1 
ATOM   4384 C  CA  . ASP B 1 136 ? 35.67700  14.80100  69.20200 1.000 16.96000 ? 136 ASP B CA  1 
ATOM   4385 C  C   . ASP B 1 136 ? 36.91300  15.59400  68.79900 1.000 16.82000 ? 136 ASP B C   1 
ATOM   4386 O  O   . ASP B 1 136 ? 37.16700  16.68800  69.32400 1.000 16.28000 ? 136 ASP B O   1 
ATOM   4387 C  CB  . ASP B 1 136 ? 36.04100  13.69500  70.18800 1.000 17.84000 ? 136 ASP B CB  1 
ATOM   4388 C  CG  . ASP B 1 136 ? 34.85800  13.25800  71.01800 1.000 18.42000 ? 136 ASP B CG  1 
ATOM   4389 O  OD1 . ASP B 1 136 ? 33.77300  13.86100  70.87700 1.000 19.74000 ? 136 ASP B OD1 1 
ATOM   4390 O  OD2 . ASP B 1 136 ? 35.01000  12.31300  71.81300 1.000 17.40000 ? 136 ASP B OD2 1 
ATOM   4391 N  N   . TRP B 1 137 ? 37.68100  15.07100  67.84400 1.000 19.37000 ? 137 TRP B N   1 
ATOM   4392 C  CA  . TRP B 1 137 ? 38.88400  15.76800  67.40000 1.000 17.14000 ? 137 TRP B CA  1 
ATOM   4393 C  C   . TRP B 1 137 ? 38.54200  16.99000  66.54800 1.000 18.68000 ? 137 TRP B C   1 
ATOM   4394 O  O   . TRP B 1 137 ? 39.01500  18.10200  66.82000 1.000 18.24000 ? 137 TRP B O   1 
ATOM   4395 C  CB  . TRP B 1 137 ? 39.79200  14.81000  66.62300 1.000 16.45000 ? 137 TRP B CB  1 
ATOM   4396 C  CG  . TRP B 1 137 ? 41.07800  15.46000  66.21700 1.000 18.75000 ? 137 TRP B CG  1 
ATOM   4397 C  CD1 . TRP B 1 137 ? 42.13400  15.77200  67.02800 1.000 18.87000 ? 137 TRP B CD1 1 
ATOM   4398 C  CD2 . TRP B 1 137 ? 41.43400  15.91200  64.90300 1.000 16.83000 ? 137 TRP B CD2 1 
ATOM   4399 N  NE1 . TRP B 1 137 ? 43.13300  16.36900  66.29200 1.000 17.80000 ? 137 TRP B NE1 1 
ATOM   4400 C  CE2 . TRP B 1 137 ? 42.71900  16.47900  64.99000 1.000 14.85000 ? 137 TRP B CE2 1 
ATOM   4401 C  CE3 . TRP B 1 137 ? 40.78900  15.88700  63.66300 1.000 17.28000 ? 137 TRP B CE3 1 
ATOM   4402 C  CZ2 . TRP B 1 137 ? 43.37300  17.02600  63.88200 1.000 15.44000 ? 137 TRP B CZ2 1 
ATOM   4403 C  CZ3 . TRP B 1 137 ? 41.44500  16.42400  62.56100 1.000 16.74000 ? 137 TRP B CZ3 1 
ATOM   4404 C  CH2 . TRP B 1 137 ? 42.72500  16.97700  62.68100 1.000 14.71000 ? 137 TRP B CH2 1 
ATOM   4405 N  N   . VAL B 1 138 ? 37.73500  16.81100  65.50500 1.000 15.45000 ? 138 VAL B N   1 
ATOM   4406 C  CA  . VAL B 1 138 ? 37.62500  17.87100  64.50700 1.000 13.04000 ? 138 VAL B CA  1 
ATOM   4407 C  C   . VAL B 1 138 ? 36.60300  18.94100  64.90300 1.000 16.72000 ? 138 VAL B C   1 
ATOM   4408 O  O   . VAL B 1 138 ? 36.73000  20.09100  64.47500 1.000 16.59000 ? 138 VAL B O   1 
ATOM   4409 C  CB  . VAL B 1 138 ? 37.31300  17.26700  63.11800 1.000 14.07000 ? 138 VAL B CB  1 
ATOM   4410 C  CG1 . VAL B 1 138 ? 35.82300  16.99800  62.96400 1.000 16.09000 ? 138 VAL B CG1 1 
ATOM   4411 C  CG2 . VAL B 1 138 ? 37.82700  18.18600  62.00400 1.000 15.74000 ? 138 VAL B CG2 1 
ATOM   4412 N  N   . VAL B 1 139 ? 35.59500  18.59400  65.70900 1.000 14.11000 ? 139 VAL B N   1 
ATOM   4413 C  CA  . VAL B 1 139 ? 34.62400  19.57600  66.19700 1.000 16.99000 ? 139 VAL B CA  1 
ATOM   4414 C  C   . VAL B 1 139 ? 35.06200  20.16400  67.52900 1.000 18.57000 ? 139 VAL B C   1 
ATOM   4415 O  O   . VAL B 1 139 ? 34.89000  21.36100  67.77800 1.000 21.96000 ? 139 VAL B O   1 
ATOM   4416 C  CB  . VAL B 1 139 ? 33.22300  18.93000  66.31800 1.000 15.84000 ? 139 VAL B CB  1 
ATOM   4417 C  CG1 . VAL B 1 139 ? 32.21900  19.92700  66.87500 1.000 15.08000 ? 139 VAL B CG1 1 
ATOM   4418 C  CG2 . VAL B 1 139 ? 32.74500  18.38500  64.96800 1.000 16.44000 ? 139 VAL B CG2 1 
ATOM   4419 N  N   . GLY B 1 140 ? 35.61100  19.33100  68.40600 1.000 16.02000 ? 140 GLY B N   1 
ATOM   4420 C  CA  . GLY B 1 140 ? 35.98800  19.77800  69.73000 1.000 19.05000 ? 140 GLY B CA  1 
ATOM   4421 C  C   . GLY B 1 140 ? 37.41100  20.29000  69.84300 1.000 21.19000 ? 140 GLY B C   1 
ATOM   4422 O  O   . GLY B 1 140 ? 37.62400  21.47300  70.11000 1.000 23.02000 ? 140 GLY B O   1 
ATOM   4423 N  N   . GLU B 1 141 ? 38.40000  19.42200  69.64300 1.000 20.14000 ? 141 GLU B N   1 
ATOM   4424 C  CA  . GLU B 1 141 ? 39.77200  19.81400  69.94800 1.000 18.44000 ? 141 GLU B CA  1 
ATOM   4425 C  C   . GLU B 1 141 ? 40.28900  20.88300  68.98900 1.000 21.11000 ? 141 GLU B C   1 
ATOM   4426 O  O   . GLU B 1 141 ? 40.85600  21.89200  69.42400 1.000 19.49000 ? 141 GLU B O   1 
ATOM   4427 C  CB  . GLU B 1 141 ? 40.69500  18.59600  69.93400 1.000 17.56000 ? 141 GLU B CB  1 
ATOM   4428 C  CG  . GLU B 1 141 ? 42.16800  18.97400  70.17400 1.000 22.15000 ? 141 GLU B CG  1 
ATOM   4429 C  CD  . GLU B 1 141 ? 43.09000  17.77200  70.25900 1.000 27.35000 ? 141 GLU B CD  1 
ATOM   4430 O  OE1 . GLU B 1 141 ? 42.59500  16.63000  70.30600 1.000 22.62000 ? 141 GLU B OE1 1 
ATOM   4431 O  OE2 . GLU B 1 141 ? 44.32000  17.96800  70.27500 1.000 29.31000 ? 141 GLU B OE2 1 
ATOM   4432 N  N   . VAL B 1 142 ? 40.12200  20.68500  67.68300 1.000 17.28000 ? 142 VAL B N   1 
ATOM   4433 C  CA  . VAL B 1 142 ? 40.78800  21.56500  66.71700 1.000 18.83000 ? 142 VAL B CA  1 
ATOM   4434 C  C   . VAL B 1 142 ? 40.22800  22.98600  66.77700 1.000 20.63000 ? 142 VAL B C   1 
ATOM   4435 O  O   . VAL B 1 142 ? 41.02000  23.93600  66.89700 1.000 19.08000 ? 142 VAL B O   1 
ATOM   4436 C  CB  . VAL B 1 142 ? 40.73100  20.98400  65.29200 1.000 15.50000 ? 142 VAL B CB  1 
ATOM   4437 C  CG1 . VAL B 1 142 ? 41.19400  22.01900  64.26200 1.000 17.93000 ? 142 VAL B CG1 1 
ATOM   4438 C  CG2 . VAL B 1 142 ? 41.60300  19.75600  65.20800 1.000 17.47000 ? 142 VAL B CG2 1 
ATOM   4439 N  N   . PRO B 1 143 ? 38.90500  23.20600  66.71900 1.000 21.17000 ? 143 PRO B N   1 
ATOM   4440 C  CA  . PRO B 1 143 ? 38.41500  24.58800  66.83300 1.000 22.04000 ? 143 PRO B CA  1 
ATOM   4441 C  C   . PRO B 1 143 ? 38.73500  25.23200  68.16800 1.000 23.39000 ? 143 PRO B C   1 
ATOM   4442 O  O   . PRO B 1 143 ? 38.96700  26.44600  68.21500 1.000 23.06000 ? 143 PRO B O   1 
ATOM   4443 C  CB  . PRO B 1 143 ? 36.90000  24.44800  66.62500 1.000 21.54000 ? 143 PRO B CB  1 
ATOM   4444 C  CG  . PRO B 1 143 ? 36.73800  23.17100  65.89600 1.000 20.72000 ? 143 PRO B CG  1 
ATOM   4445 C  CD  . PRO B 1 143 ? 37.78600  22.27300  66.48900 1.000 16.76000 ? 143 PRO B CD  1 
ATOM   4446 N  N   . ASP B 1 144 ? 38.75500  24.46700  69.26000 1.000 25.65000 ? 144 ASP B N   1 
ATOM   4447 C  CA  . ASP B 1 144 ? 39.11100  25.05900  70.54400 1.000 26.02000 ? 144 ASP B CA  1 
ATOM   4448 C  C   . ASP B 1 144 ? 40.57300  25.48000  70.56000 1.000 25.53000 ? 144 ASP B C   1 
ATOM   4449 O  O   . ASP B 1 144 ? 40.91300  26.53500  71.10500 1.000 23.08000 ? 144 ASP B O   1 
ATOM   4450 C  CB  . ASP B 1 144 ? 38.81200  24.08600  71.68500 1.000 30.26000 ? 144 ASP B CB  1 
ATOM   4451 C  CG  . ASP B 1 144 ? 37.31600  23.93700  71.94500 1.000 42.40000 ? 144 ASP B CG  1 
ATOM   4452 O  OD1 . ASP B 1 144 ? 36.53900  24.76400  71.41500 1.000 40.11000 ? 144 ASP B OD1 1 
ATOM   4453 O  OD2 . ASP B 1 144 ? 36.91000  22.98900  72.66000 1.000 45.34000 ? 144 ASP B OD2 1 
ATOM   4454 N  N   . ALA B 1 145 ? 41.45200  24.67600  69.95400 1.000 22.86000 ? 145 ALA B N   1 
ATOM   4455 C  CA  . ALA B 1 145 ? 42.87200  24.99000  69.94800 1.000 24.53000 ? 145 ALA B CA  1 
ATOM   4456 C  C   . ALA B 1 145 ? 43.20100  26.20900  69.09700 1.000 21.49000 ? 145 ALA B C   1 
ATOM   4457 O  O   . ALA B 1 145 ? 44.24300  26.83200  69.31600 1.000 22.27000 ? 145 ALA B O   1 
ATOM   4458 C  CB  . ALA B 1 145 ? 43.67900  23.78600  69.44900 1.000 24.51000 ? 145 ALA B CB  1 
ATOM   4459 N  N   . HIS B 1 146 ? 42.36900  26.54100  68.11400 1.000 23.44000 ? 146 HIS B N   1 
ATOM   4460 C  CA  . HIS B 1 146 ? 42.62800  27.65100  67.19100 1.000 22.20000 ? 146 HIS B CA  1 
ATOM   4461 C  C   . HIS B 1 146 ? 41.35700  28.47200  67.04500 1.000 20.19000 ? 146 HIS B C   1 
ATOM   4462 O  O   . HIS B 1 146 ? 40.71200  28.46500  65.98800 1.000 21.05000 ? 146 HIS B O   1 
ATOM   4463 C  CB  . HIS B 1 146 ? 43.11700  27.13700  65.83600 1.000 22.52000 ? 146 HIS B CB  1 
ATOM   4464 C  CG  . HIS B 1 146 ? 44.31100  26.24100  65.93400 1.000 25.43000 ? 146 HIS B CG  1 
ATOM   4465 N  ND1 . HIS B 1 146 ? 45.59200  26.72400  66.09800 1.000 22.33000 ? 146 HIS B ND1 1 
ATOM   4466 C  CD2 . HIS B 1 146 ? 44.41600  24.89100  65.92100 1.000 23.41000 ? 146 HIS B CD2 1 
ATOM   4467 C  CE1 . HIS B 1 146 ? 46.43800  25.71000  66.16400 1.000 19.43000 ? 146 HIS B CE1 1 
ATOM   4468 N  NE2 . HIS B 1 146 ? 45.74800  24.58600  66.06600 1.000 22.72000 ? 146 HIS B NE2 1 
ATOM   4469 N  N   . PRO B 1 147 ? 40.97500  29.20800  68.09200 1.000 25.75000 ? 147 PRO B N   1 
ATOM   4470 C  CA  . PRO B 1 147 ? 39.66900  29.87700  68.08800 1.000 21.90000 ? 147 PRO B CA  1 
ATOM   4471 C  C   . PRO B 1 147 ? 39.53000  30.81700  66.90500 1.000 22.24000 ? 147 PRO B C   1 
ATOM   4472 O  O   . PRO B 1 147 ? 40.43900  31.58700  66.59000 1.000 21.93000 ? 147 PRO B O   1 
ATOM   4473 C  CB  . PRO B 1 147 ? 39.66000  30.65000  69.41400 1.000 20.86000 ? 147 PRO B CB  1 
ATOM   4474 C  CG  . PRO B 1 147 ? 40.67000  29.95900  70.26100 1.000 24.87000 ? 147 PRO B CG  1 
ATOM   4475 C  CD  . PRO B 1 147 ? 41.74100  29.52200  69.30800 1.000 25.29000 ? 147 PRO B CD  1 
ATOM   4476 N  N   . GLY B 1 148 ? 38.37300  30.75500  66.25300 1.000 21.69000 ? 148 GLY B N   1 
ATOM   4477 C  CA  . GLY B 1 148 ? 38.09300  31.66900  65.17800 1.000 21.36000 ? 148 GLY B CA  1 
ATOM   4478 C  C   . GLY B 1 148 ? 38.67600  31.28600  63.83800 1.000 21.45000 ? 148 GLY B C   1 
ATOM   4479 O  O   . GLY B 1 148 ? 38.42500  31.99900  62.86100 1.000 17.58000 ? 148 GLY B O   1 
ATOM   4480 N  N   . ARG B 1 149 ? 39.40800  30.16800  63.74500 1.000 16.35000 ? 149 ARG B N   1 
ATOM   4481 C  CA  . ARG B 1 149 ? 40.00700  29.75500  62.47800 1.000 19.94000 ? 149 ARG B CA  1 
ATOM   4482 C  C   . ARG B 1 149 ? 39.29500  28.57900  61.81100 1.000 18.96000 ? 149 ARG B C   1 
ATOM   4483 O  O   . ARG B 1 149 ? 39.55700  28.32000  60.63000 1.000 15.29000 ? 149 ARG B O   1 
ATOM   4484 C  CB  . ARG B 1 149 ? 41.48900  29.37200  62.65200 1.000 19.18000 ? 149 ARG B CB  1 
ATOM   4485 C  CG  . ARG B 1 149 ? 42.38000  30.38100  63.38700 1.000 16.22000 ? 149 ARG B CG  1 
ATOM   4486 C  CD  . ARG B 1 149 ? 42.28800  31.77400  62.80000 1.000 18.03000 ? 149 ARG B CD  1 
ATOM   4487 N  NE  . ARG B 1 149 ? 42.63500  31.87000  61.37700 1.000 16.22000 ? 149 ARG B NE  1 
ATOM   4488 C  CZ  . ARG B 1 149 ? 43.84100  32.20000  60.92600 1.000 19.23000 ? 149 ARG B CZ  1 
ATOM   4489 N  NH1 . ARG B 1 149 ? 44.82000  32.43400  61.78200 1.000 20.52000 ? 149 ARG B NH1 1 
ATOM   4490 N  NH2 . ARG B 1 149 ? 44.07200  32.29800  59.62000 1.000 15.46000 ? 149 ARG B NH2 1 
ATOM   4491 N  N   . PHE B 1 150 ? 38.43000  27.84900  62.52100 1.000 17.06000 ? 150 PHE B N   1 
ATOM   4492 C  CA  . PHE B 1 150 ? 37.76700  26.68500  61.94900 1.000 16.15000 ? 150 PHE B CA  1 
ATOM   4493 C  C   . PHE B 1 150 ? 36.28000  26.70700  62.27000 1.000 17.74000 ? 150 PHE B C   1 
ATOM   4494 O  O   . PHE B 1 150 ? 35.88700  26.80800  63.44000 1.000 18.27000 ? 150 PHE B O   1 
ATOM   4495 C  CB  . PHE B 1 150 ? 38.40300  25.37900  62.45700 1.000 17.64000 ? 150 PHE B CB  1 
ATOM   4496 C  CG  . PHE B 1 150 ? 39.83700  25.23400  62.06100 1.000 17.86000 ? 150 PHE B CG  1 
ATOM   4497 C  CD1 . PHE B 1 150 ? 40.17300  24.95300  60.74600 1.000 18.38000 ? 150 PHE B CD1 1 
ATOM   4498 C  CD2 . PHE B 1 150 ? 40.85000  25.43900  62.98500 1.000 17.99000 ? 150 PHE B CD2 1 
ATOM   4499 C  CE1 . PHE B 1 150 ? 41.49700  24.85400  60.36100 1.000 14.68000 ? 150 PHE B CE1 1 
ATOM   4500 C  CE2 . PHE B 1 150 ? 42.18300  25.33300  62.61300 1.000 20.39000 ? 150 PHE B CE2 1 
ATOM   4501 C  CZ  . PHE B 1 150 ? 42.51100  25.04600  61.30400 1.000 18.21000 ? 150 PHE B CZ  1 
ATOM   4502 N  N   . ILE B 1 151 ? 35.46200  26.60400  61.23200 1.000 14.86000 ? 151 ILE B N   1 
ATOM   4503 C  CA  . ILE B 1 151 ? 34.01900  26.47800  61.38700 1.000 15.27000 ? 151 ILE B CA  1 
ATOM   4504 C  C   . ILE B 1 151 ? 33.74400  25.00600  61.66100 1.000 16.24000 ? 151 ILE B C   1 
ATOM   4505 O  O   . ILE B 1 151 ? 33.99300  24.16300  60.79000 1.000 15.32000 ? 151 ILE B O   1 
ATOM   4506 C  CB  . ILE B 1 151 ? 33.27900  26.97000  60.13500 1.000 13.57000 ? 151 ILE B CB  1 
ATOM   4507 C  CG1 . ILE B 1 151 ? 33.62900  28.42800  59.85300 1.000 19.97000 ? 151 ILE B CG1 1 
ATOM   4508 C  CG2 . ILE B 1 151 ? 31.76600  26.77800  60.28400 1.000 15.59000 ? 151 ILE B CG2 1 
ATOM   4509 C  CD1 . ILE B 1 151 ? 32.99200  28.95600  58.60100 1.000 18.53000 ? 151 ILE B CD1 1 
ATOM   4510 N  N   . PRO B 1 152 ? 33.25400  24.65000  62.84400 1.000 15.26000 ? 152 PRO B N   1 
ATOM   4511 C  CA  . PRO B 1 152 ? 33.15100  23.22800  63.21000 1.000 17.70000 ? 152 PRO B CA  1 
ATOM   4512 C  C   . PRO B 1 152 ? 32.16200  22.48100  62.32600 1.000 15.37000 ? 152 PRO B C   1 
ATOM   4513 O  O   . PRO B 1 152 ? 30.99800  22.87000  62.19900 1.000 15.97000 ? 152 PRO B O   1 
ATOM   4514 C  CB  . PRO B 1 152 ? 32.68400  23.27300  64.67100 1.000 16.10000 ? 152 PRO B CB  1 
ATOM   4515 C  CG  . PRO B 1 152 ? 33.03200  24.66700  65.14400 1.000 17.61000 ? 152 PRO B CG  1 
ATOM   4516 C  CD  . PRO B 1 152 ? 32.85700  25.54300  63.94800 1.000 18.52000 ? 152 PRO B CD  1 
ATOM   4517 N  N   . ILE B 1 153 ? 32.63300  21.39400  61.72100 1.000 14.53000 ? 153 ILE B N   1 
ATOM   4518 C  CA  . ILE B 1 153 ? 31.81000  20.54900  60.86000 1.000 14.59000 ? 153 ILE B CA  1 
ATOM   4519 C  C   . ILE B 1 153 ? 32.09700  19.08800  61.19100 1.000 16.38000 ? 153 ILE B C   1 
ATOM   4520 O  O   . ILE B 1 153 ? 33.25900  18.69300  61.33900 1.000 15.60000 ? 153 ILE B O   1 
ATOM   4521 C  CB  . ILE B 1 153 ? 32.07600  20.86200  59.36900 1.000 16.26000 ? 153 ILE B CB  1 
ATOM   4522 C  CG1 . ILE B 1 153 ? 31.26400  19.93000  58.46800 1.000 14.21000 ? 153 ILE B CG1 1 
ATOM   4523 C  CG2 . ILE B 1 153 ? 33.57800  20.77800  59.06100 1.000 14.42000 ? 153 ILE B CG2 1 
ATOM   4524 C  CD1 . ILE B 1 153 ? 31.23000  20.34400  56.99700 1.000 17.01000 ? 153 ILE B CD1 1 
ATOM   4525 N  N   . GLY B 1 154 ? 31.04200  18.27000  61.30500 1.000 16.25000 ? 154 GLY B N   1 
ATOM   4526 C  CA  . GLY B 1 154 ? 31.19500  16.88100  61.69400 1.000 16.80000 ? 154 GLY B CA  1 
ATOM   4527 C  C   . GLY B 1 154 ? 30.51800  15.92900  60.72100 1.000 14.50000 ? 154 GLY B C   1 
ATOM   4528 O  O   . GLY B 1 154 ? 29.93300  16.34300  59.71800 1.000 15.11000 ? 154 GLY B O   1 
ATOM   4529 N  N   . ILE B 1 155 ? 30.64500  14.63500  61.03000 1.000 16.00000 ? 155 ILE B N   1 
ATOM   4530 C  CA  . ILE B 1 155 ? 29.98600  13.56300  60.29000 1.000 11.78000 ? 155 ILE B CA  1 
ATOM   4531 C  C   . ILE B 1 155 ? 29.05800  12.81400  61.24700 1.000 13.09000 ? 155 ILE B C   1 
ATOM   4532 O  O   . ILE B 1 155 ? 29.08100  13.02700  62.45800 1.000 13.39000 ? 155 ILE B O   1 
ATOM   4533 C  CB  . ILE B 1 155 ? 30.98700  12.59600  59.63100 1.000 12.50000 ? 155 ILE B CB  1 
ATOM   4534 C  CG1 . ILE B 1 155 ? 31.95100  12.03200  60.68000 1.000 13.19000 ? 155 ILE B CG1 1 
ATOM   4535 C  CG2 . ILE B 1 155 ? 31.75700  13.29500  58.49300 1.000 13.00000 ? 155 ILE B CG2 1 
ATOM   4536 C  CD1 . ILE B 1 155 ? 32.86600  10.92300  60.13700 1.000 13.71000 ? 155 ILE B CD1 1 
ATOM   4537 N  N   . ILE B 1 156 ? 28.23800  11.92700  60.68800 1.000 12.67000 ? 156 ILE B N   1 
ATOM   4538 C  CA  . ILE B 1 156 ? 27.29700  11.16400  61.50700 1.000 12.96000 ? 156 ILE B CA  1 
ATOM   4539 C  C   . ILE B 1 156 ? 27.35900  9.69500   61.12800 1.000 14.89000 ? 156 ILE B C   1 
ATOM   4540 O  O   . ILE B 1 156 ? 27.70700  9.33100   59.98900 1.000 15.04000 ? 156 ILE B O   1 
ATOM   4541 C  CB  . ILE B 1 156 ? 25.85200  11.69800  61.37100 1.000 15.08000 ? 156 ILE B CB  1 
ATOM   4542 C  CG1 . ILE B 1 156 ? 25.46800  11.88900  59.90100 1.000 14.37000 ? 156 ILE B CG1 1 
ATOM   4543 C  CG2 . ILE B 1 156 ? 25.67000  12.96300  62.21600 1.000 13.38000 ? 156 ILE B CG2 1 
ATOM   4544 C  CD1 . ILE B 1 156 ? 23.96500  11.89600  59.67900 1.000 16.01000 ? 156 ILE B CD1 1 
ATOM   4545 N  N   . PRO B 1 157 ? 26.99200  8.80900   62.06000 1.000 10.53000 ? 157 PRO B N   1 
ATOM   4546 C  CA  . PRO B 1 157 ? 26.87800  7.37500   61.75800 1.000 12.52000 ? 157 PRO B CA  1 
ATOM   4547 C  C   . PRO B 1 157 ? 25.56400  7.09300   61.04200 1.000 16.09000 ? 157 PRO B C   1 
ATOM   4548 O  O   . PRO B 1 157 ? 24.62300  6.48400   61.57700 1.000 16.74000 ? 157 PRO B O   1 
ATOM   4549 C  CB  . PRO B 1 157 ? 26.95000  6.75100   63.15200 1.000 13.92000 ? 157 PRO B CB  1 
ATOM   4550 C  CG  . PRO B 1 157 ? 26.19300  7.76900   64.01200 1.000 16.25000 ? 157 PRO B CG  1 
ATOM   4551 C  CD  . PRO B 1 157 ? 26.65000  9.10900   63.46800 1.000 15.66000 ? 157 PRO B CD  1 
ATOM   4552 N  N   . PHE B 1 158 ? 25.48000  7.55300   59.78800 1.000 16.59000 ? 158 PHE B N   1 
ATOM   4553 C  CA  . PHE B 1 158 ? 24.20500  7.62500   59.08600 1.000 16.22000 ? 158 PHE B CA  1 
ATOM   4554 C  C   . PHE B 1 158 ? 23.62500  6.26000   58.74800 1.000 15.14000 ? 158 PHE B C   1 
ATOM   4555 O  O   . PHE B 1 158 ? 22.47400  6.19600   58.29800 1.000 16.11000 ? 158 PHE B O   1 
ATOM   4556 C  CB  . PHE B 1 158 ? 24.34800  8.47000   57.80900 1.000 14.43000 ? 158 PHE B CB  1 
ATOM   4557 C  CG  . PHE B 1 158 ? 25.25000  7.86100   56.77300 1.000 14.70000 ? 158 PHE B CG  1 
ATOM   4558 C  CD1 . PHE B 1 158 ? 24.77300  6.89200   55.90300 1.000 15.11000 ? 158 PHE B CD1 1 
ATOM   4559 C  CD2 . PHE B 1 158 ? 26.57000  8.27600   56.65300 1.000 17.51000 ? 158 PHE B CD2 1 
ATOM   4560 C  CE1 . PHE B 1 158 ? 25.60100  6.32800   54.94400 1.000 16.98000 ? 158 PHE B CE1 1 
ATOM   4561 C  CE2 . PHE B 1 158 ? 27.39500  7.72000   55.69800 1.000 15.55000 ? 158 PHE B CE2 1 
ATOM   4562 C  CZ  . PHE B 1 158 ? 26.90600  6.74600   54.83900 1.000 16.68000 ? 158 PHE B CZ  1 
ATOM   4563 N  N   . PHE B 1 159 ? 24.37100  5.17400   58.96900 1.000 16.72000 ? 159 PHE B N   1 
ATOM   4564 C  CA  . PHE B 1 159 ? 23.81600  3.82600   58.88500 1.000 20.51000 ? 159 PHE B CA  1 
ATOM   4565 C  C   . PHE B 1 159 ? 22.78100  3.53600   59.97100 1.000 15.99000 ? 159 PHE B C   1 
ATOM   4566 O  O   . PHE B 1 159 ? 22.08400  2.51800   59.88100 1.000 19.95000 ? 159 PHE B O   1 
ATOM   4567 C  CB  . PHE B 1 159 ? 24.95100  2.79300   58.96700 1.000 16.05000 ? 159 PHE B CB  1 
ATOM   4568 C  CG  . PHE B 1 159 ? 25.84700  2.98100   60.15400 1.000 17.09000 ? 159 PHE B CG  1 
ATOM   4569 C  CD1 . PHE B 1 159 ? 25.49700  2.46400   61.39000 1.000 17.72000 ? 159 PHE B CD1 1 
ATOM   4570 C  CD2 . PHE B 1 159 ? 27.03000  3.69400   60.04100 1.000 19.32000 ? 159 PHE B CD2 1 
ATOM   4571 C  CE1 . PHE B 1 159 ? 26.31000  2.65300   62.49500 1.000 21.44000 ? 159 PHE B CE1 1 
ATOM   4572 C  CE2 . PHE B 1 159 ? 27.85900  3.87700   61.14500 1.000 20.05000 ? 159 PHE B CE2 1 
ATOM   4573 C  CZ  . PHE B 1 159 ? 27.49700  3.35400   62.37100 1.000 19.10000 ? 159 PHE B CZ  1 
ATOM   4574 N  N   . ASP B 1 160 ? 22.64200  4.40300   60.97100 1.000 17.05000 ? 160 ASP B N   1 
ATOM   4575 C  CA  . ASP B 1 160 ? 21.70500  4.19000   62.07400 1.000 18.42000 ? 160 ASP B CA  1 
ATOM   4576 C  C   . ASP B 1 160 ? 21.07400  5.53400   62.40600 1.000 16.12000 ? 160 ASP B C   1 
ATOM   4577 O  O   . ASP B 1 160 ? 21.76000  6.43800   62.89200 1.000 17.63000 ? 160 ASP B O   1 
ATOM   4578 C  CB  . ASP B 1 160 ? 22.42800  3.59000   63.28500 1.000 18.55000 ? 160 ASP B CB  1 
ATOM   4579 C  CG  . ASP B 1 160 ? 21.48600  3.23000   64.42000 1.000 24.14000 ? 160 ASP B CG  1 
ATOM   4580 O  OD1 . ASP B 1 160 ? 20.75700  4.10700   64.90700 1.000 18.74000 ? 160 ASP B OD1 1 
ATOM   4581 O  OD2 . ASP B 1 160 ? 21.50200  2.06000   64.84300 1.000 36.98000 ? 160 ASP B OD2 1 
ATOM   4582 N  N   . ALA B 1 161 ? 19.77000  5.66600   62.14500 1.000 16.28000 ? 161 ALA B N   1 
ATOM   4583 C  CA  . ALA B 1 161 ? 19.12800  6.97800   62.25800 1.000 19.64000 ? 161 ALA B CA  1 
ATOM   4584 C  C   . ALA B 1 161 ? 19.07200  7.45500   63.70500 1.000 17.50000 ? 161 ALA B C   1 
ATOM   4585 O  O   . ALA B 1 161 ? 19.31100  8.63500   63.98100 1.000 16.82000 ? 161 ALA B O   1 
ATOM   4586 C  CB  . ALA B 1 161 ? 17.72000  6.93800   61.65500 1.000 17.08000 ? 161 ALA B CB  1 
ATOM   4587 N  N   . ASP B 1 162 ? 18.74300  6.55800   64.63800 1.000 22.64000 ? 162 ASP B N   1 
ATOM   4588 C  CA  . ASP B 1 162 ? 18.68700  6.93300   66.05100 1.000 19.60000 ? 162 ASP B CA  1 
ATOM   4589 C  C   . ASP B 1 162 ? 20.06300  7.35900   66.56100 1.000 15.29000 ? 162 ASP B C   1 
ATOM   4590 O  O   . ASP B 1 162 ? 20.19000  8.36200   67.27000 1.000 13.19000 ? 162 ASP B O   1 
ATOM   4591 C  CB  . ASP B 1 162 ? 18.14600  5.76800   66.88900 1.000 20.15000 ? 162 ASP B CB  1 
ATOM   4592 C  CG  . ASP B 1 162 ? 16.67900  5.48700   66.63700 1.000 24.23000 ? 162 ASP B CG  1 
ATOM   4593 O  OD1 . ASP B 1 162 ? 15.98200  6.35500   66.06900 1.000 22.93000 ? 162 ASP B OD1 1 
ATOM   4594 O  OD2 . ASP B 1 162 ? 16.22100  4.39400   67.02700 1.000 27.37000 ? 162 ASP B OD2 1 
ATOM   4595 N  N   . GLU B 1 163 ? 21.10700  6.60000   66.22100 1.000 16.29000 ? 163 GLU B N   1 
ATOM   4596 C  CA  . GLU B 1 163 ? 22.44400  7.01500   66.63600 1.000 17.63000 ? 163 GLU B CA  1 
ATOM   4597 C  C   . GLU B 1 163 ? 22.85500  8.31500   65.96200 1.000 15.59000 ? 163 GLU B C   1 
ATOM   4598 O  O   . GLU B 1 163 ? 23.59300  9.11000   66.55700 1.000 13.79000 ? 163 GLU B O   1 
ATOM   4599 C  CB  . GLU B 1 163 ? 23.47300  5.92100   66.34000 1.000 17.67000 ? 163 GLU B CB  1 
ATOM   4600 C  CG  . GLU B 1 163 ? 23.26000  4.61000   67.10000 1.000 20.78000 ? 163 GLU B CG  1 
ATOM   4601 C  CD  . GLU B 1 163 ? 23.66800  4.68600   68.55700 1.000 24.99000 ? 163 GLU B CD  1 
ATOM   4602 O  OE1 . GLU B 1 163 ? 23.97000  5.78700   69.05600 1.000 21.92000 ? 163 GLU B OE1 1 
ATOM   4603 O  OE2 . GLU B 1 163 ? 23.69600  3.62400   69.20700 1.000 33.89000 ? 163 GLU B OE2 1 
ATOM   4604 N  N   . SER B 1 164 ? 22.38400  8.55700   64.73500 1.000 16.39000 ? 164 SER B N   1 
ATOM   4605 C  CA  . SER B 1 164 ? 22.70200  9.81300   64.06600 1.000 12.00000 ? 164 SER B CA  1 
ATOM   4606 C  C   . SER B 1 164 ? 22.04100  10.99500  64.76300 1.000 14.83000 ? 164 SER B C   1 
ATOM   4607 O  O   . SER B 1 164 ? 22.66200  12.04900  64.92900 1.000 14.14000 ? 164 SER B O   1 
ATOM   4608 C  CB  . SER B 1 164 ? 22.27100  9.76000   62.60100 1.000 15.27000 ? 164 SER B CB  1 
ATOM   4609 O  OG  . SER B 1 164 ? 23.05300  8.83200   61.87500 1.000 15.85000 ? 164 SER B OG  1 
ATOM   4610 N  N   . VAL B 1 165 ? 20.77400  10.85100  65.15500 1.000 15.18000 ? 165 VAL B N   1 
ATOM   4611 C  CA  . VAL B 1 165 ? 20.10800  11.92100  65.89400 1.000 14.43000 ? 165 VAL B CA  1 
ATOM   4612 C  C   . VAL B 1 165 ? 20.83900  12.18900  67.20000 1.000 14.49000 ? 165 VAL B C   1 
ATOM   4613 O  O   . VAL B 1 165 ? 21.11000  13.34200  67.55500 1.000 14.09000 ? 165 VAL B O   1 
ATOM   4614 C  CB  . VAL B 1 165 ? 18.63100  11.57000  66.14700 1.000 12.74000 ? 165 VAL B CB  1 
ATOM   4615 C  CG1 . VAL B 1 165 ? 18.01500  12.58700  67.10200 1.000 12.45000 ? 165 VAL B CG1 1 
ATOM   4616 C  CG2 . VAL B 1 165 ? 17.86700  11.51100  64.83300 1.000 15.59000 ? 165 VAL B CG2 1 
ATOM   4617 N  N   . ALA B 1 166 ? 21.17700  11.12500  67.93100 1.000 14.72000 ? 166 ALA B N   1 
ATOM   4618 C  CA  . ALA B 1 166 ? 21.89500  11.29700  69.19000 1.000 14.23000 ? 166 ALA B CA  1 
ATOM   4619 C  C   . ALA B 1 166 ? 23.21700  12.02500  68.97400 1.000 15.29000 ? 166 ALA B C   1 
ATOM   4620 O  O   . ALA B 1 166 ? 23.60400  12.89000  69.77400 1.000 14.52000 ? 166 ALA B O   1 
ATOM   4621 C  CB  . ALA B 1 166 ? 22.12600  9.93800   69.84000 1.000 17.14000 ? 166 ALA B CB  1 
ATOM   4622 N  N   . GLU B 1 167 ? 23.89300  11.73300  67.86700 1.000 12.49000 ? 167 GLU B N   1 
ATOM   4623 C  CA  . GLU B 1 167 ? 25.18900  12.35400  67.63400 1.000 14.06000 ? 167 GLU B CA  1 
ATOM   4624 C  C   . GLU B 1 167 ? 25.04700  13.81400  67.23000 1.000 14.10000 ? 167 GLU B C   1 
ATOM   4625 O  O   . GLU B 1 167 ? 25.85700  14.65400  67.64000 1.000 16.01000 ? 167 GLU B O   1 
ATOM   4626 C  CB  . GLU B 1 167 ? 25.96700  11.55700  66.58600 1.000 12.02000 ? 167 GLU B CB  1 
ATOM   4627 C  CG  . GLU B 1 167 ? 27.36900  12.14700  66.31000 1.000 13.29000 ? 167 GLU B CG  1 
ATOM   4628 C  CD  . GLU B 1 167 ? 28.35700  11.90400  67.44000 1.000 20.35000 ? 167 GLU B CD  1 
ATOM   4629 O  OE1 . GLU B 1 167 ? 27.94900  11.44200  68.53200 1.000 16.26000 ? 167 GLU B OE1 1 
ATOM   4630 O  OE2 . GLU B 1 167 ? 29.55900  12.17500  67.22100 1.000 15.46000 ? 167 GLU B OE2 1 
ATOM   4631 N  N   . VAL B 1 168 ? 24.01200  14.15000  66.45300 1.000 14.48000 ? 168 VAL B N   1 
ATOM   4632 C  CA  . VAL B 1 168 ? 23.76600  15.55800  66.13200 1.000 14.05000 ? 168 VAL B CA  1 
ATOM   4633 C  C   . VAL B 1 168 ? 23.59000  16.37100  67.41200 1.000 17.39000 ? 168 VAL B C   1 
ATOM   4634 O  O   . VAL B 1 168 ? 24.19100  17.44000  67.58400 1.000 14.26000 ? 168 VAL B O   1 
ATOM   4635 C  CB  . VAL B 1 168 ? 22.54900  15.69700  65.20200 1.000 13.98000 ? 168 VAL B CB  1 
ATOM   4636 C  CG1 . VAL B 1 168 ? 22.19900  17.16000  64.99800 1.000 15.23000 ? 168 VAL B CG1 1 
ATOM   4637 C  CG2 . VAL B 1 168 ? 22.85700  15.07300  63.84400 1.000 13.60000 ? 168 VAL B CG2 1 
ATOM   4638 N  N   . HIS B 1 169 ? 22.78300  15.86500  68.34100 1.000 12.20000 ? 169 HIS B N   1 
ATOM   4639 C  CA  . HIS B 1 169 ? 22.59000  16.58900  69.59100 1.000 15.02000 ? 169 HIS B CA  1 
ATOM   4640 C  C   . HIS B 1 169 ? 23.89300  16.69000  70.37200 1.000 14.93000 ? 169 HIS B C   1 
ATOM   4641 O  O   . HIS B 1 169 ? 24.16900  17.71400  71.01000 1.000 15.34000 ? 169 HIS B O   1 
ATOM   4642 C  CB  . HIS B 1 169 ? 21.51000  15.90300  70.42900 1.000 15.07000 ? 169 HIS B CB  1 
ATOM   4643 C  CG  . HIS B 1 169 ? 20.13500  16.01700  69.84400 1.000 15.22000 ? 169 HIS B CG  1 
ATOM   4644 N  ND1 . HIS B 1 169 ? 19.56700  17.23000  69.51700 1.000 16.17000 ? 169 HIS B ND1 1 
ATOM   4645 C  CD2 . HIS B 1 169 ? 19.21100  15.07200  69.53800 1.000 15.11000 ? 169 HIS B CD2 1 
ATOM   4646 C  CE1 . HIS B 1 169 ? 18.35800  17.02700  69.02000 1.000 14.45000 ? 169 HIS B CE1 1 
ATOM   4647 N  NE2 . HIS B 1 169 ? 18.11600  15.72800  69.02500 1.000 13.46000 ? 169 HIS B NE2 1 
ATOM   4648 N  N   . ARG B 1 170 ? 24.71000  15.63600  70.33700 1.000 15.28000 ? 170 ARG B N   1 
ATOM   4649 C  CA  . ARG B 1 170 ? 25.94400  15.63900  71.11700 1.000 13.19000 ? 170 ARG B CA  1 
ATOM   4650 C  C   . ARG B 1 170 ? 26.94800  16.63400  70.54500 1.000 14.96000 ? 170 ARG B C   1 
ATOM   4651 O  O   . ARG B 1 170 ? 27.56900  17.40100  71.29200 1.000 15.92000 ? 170 ARG B O   1 
ATOM   4652 C  CB  . ARG B 1 170 ? 26.54400  14.23500  71.16400 1.000 14.56000 ? 170 ARG B CB  1 
ATOM   4653 C  CG  . ARG B 1 170 ? 27.80700  14.13200  72.00600 1.000 13.54000 ? 170 ARG B CG  1 
ATOM   4654 C  CD  . ARG B 1 170 ? 28.41700  12.74100  71.93200 1.000 15.63000 ? 170 ARG B CD  1 
ATOM   4655 N  NE  . ARG B 1 170 ? 29.24100  12.57900  70.73300 1.000 18.52000 ? 170 ARG B NE  1 
ATOM   4656 C  CZ  . ARG B 1 170 ? 30.53400  12.89400  70.66600 1.000 17.09000 ? 170 ARG B CZ  1 
ATOM   4657 N  NH1 . ARG B 1 170 ? 31.16000  13.37800  71.73100 1.000 16.65000 ? 170 ARG B NH1 1 
ATOM   4658 N  NH2 . ARG B 1 170 ? 31.20100  12.72400  69.53600 1.000 14.47000 ? 170 ARG B NH2 1 
ATOM   4659 N  N   . ILE B 1 171 ? 27.14200  16.62700  69.22400 1.000 15.68000 ? 171 ILE B N   1 
ATOM   4660 C  CA  . ILE B 1 171 ? 28.13400  17.54100  68.65400 1.000 15.33000 ? 171 ILE B CA  1 
ATOM   4661 C  C   . ILE B 1 171 ? 27.59300  18.95700  68.51600 1.000 14.99000 ? 171 ILE B C   1 
ATOM   4662 O  O   . ILE B 1 171 ? 28.38100  19.90900  68.45600 1.000 15.98000 ? 171 ILE B O   1 
ATOM   4663 C  CB  . ILE B 1 171 ? 28.66400  17.02900  67.30100 1.000 12.33000 ? 171 ILE B CB  1 
ATOM   4664 C  CG1 . ILE B 1 171 ? 27.56600  17.05900  66.24000 1.000 13.40000 ? 171 ILE B CG1 1 
ATOM   4665 C  CG2 . ILE B 1 171 ? 29.24100  15.62200  67.46700 1.000 11.99000 ? 171 ILE B CG2 1 
ATOM   4666 C  CD1 . ILE B 1 171 ? 27.97400  16.38300  64.89000 1.000 13.98000 ? 171 ILE B CD1 1 
ATOM   4667 N  N   . ALA B 1 172 ? 26.27200  19.14100  68.47400 1.000 14.09000 ? 172 ALA B N   1 
ATOM   4668 C  CA  . ALA B 1 172 ? 25.74100  20.50100  68.53200 1.000 14.02000 ? 172 ALA B CA  1 
ATOM   4669 C  C   . ALA B 1 172 ? 26.17400  21.20300  69.81800 1.000 14.17000 ? 172 ALA B C   1 
ATOM   4670 O  O   . ALA B 1 172 ? 26.49500  22.39500  69.81000 1.000 14.05000 ? 172 ALA B O   1 
ATOM   4671 C  CB  . ALA B 1 172 ? 24.21400  20.48300  68.42200 1.000 16.71000 ? 172 ALA B CB  1 
ATOM   4672 N  N   . ALA B 1 173 ? 26.21400  20.47300  70.93100 1.000 14.37000 ? 173 ALA B N   1 
ATOM   4673 C  CA  . ALA B 1 173 ? 26.64500  21.06700  72.19200 1.000 15.14000 ? 173 ALA B CA  1 
ATOM   4674 C  C   . ALA B 1 173 ? 28.12600  21.43000  72.17400 1.000 18.81000 ? 173 ALA B C   1 
ATOM   4675 O  O   . ALA B 1 173 ? 28.56700  22.24000  72.99700 1.000 19.01000 ? 173 ALA B O   1 
ATOM   4676 C  CB  . ALA B 1 173 ? 26.35100  20.11000  73.35800 1.000 15.82000 ? 173 ALA B CB  1 
ATOM   4677 N  N   . MET B 1 174 ? 28.90200  20.84900  71.26300 1.000 16.17000 ? 174 MET B N   1 
ATOM   4678 C  CA  . MET B 1 174 ? 30.30300  21.19400  71.12000 1.000 15.86000 ? 174 MET B CA  1 
ATOM   4679 C  C   . MET B 1 174 ? 30.52700  22.33900  70.14000 1.000 17.96000 ? 174 MET B C   1 
ATOM   4680 O  O   . MET B 1 174 ? 31.67700  22.73700  69.92300 1.000 16.91000 ? 174 MET B O   1 
ATOM   4681 C  CB  . MET B 1 174 ? 31.10100  19.95500  70.69000 1.000 15.06000 ? 174 MET B CB  1 
ATOM   4682 C  CG  . MET B 1 174 ? 30.97600  18.79700  71.67700 1.000 16.59000 ? 174 MET B CG  1 
ATOM   4683 S  SD  . MET B 1 174 ? 31.39000  17.17700  70.97600 1.000 28.02000 ? 174 MET B SD  1 
ATOM   4684 C  CE  . MET B 1 174 ? 32.96900  17.57600  70.26000 1.000 20.59000 ? 174 MET B CE  1 
ATOM   4685 N  N   . GLY B 1 175 ? 29.46800  22.88200  69.55300 1.000 14.67000 ? 175 GLY B N   1 
ATOM   4686 C  CA  . GLY B 1 175 ? 29.59300  23.99300  68.63100 1.000 19.50000 ? 175 GLY B CA  1 
ATOM   4687 C  C   . GLY B 1 175 ? 29.49100  23.63500  67.16400 1.000 19.45000 ? 175 GLY B C   1 
ATOM   4688 O  O   . GLY B 1 175 ? 29.72400  24.50300  66.31700 1.000 17.06000 ? 175 GLY B O   1 
ATOM   4689 N  N   . CYS B 1 176 ? 29.17600  22.38300  66.84100 1.000 15.85000 ? 176 CYS B N   1 
ATOM   4690 C  CA  . CYS B 1 176 ? 29.05200  21.96500  65.45500 1.000 14.95000 ? 176 CYS B CA  1 
ATOM   4691 C  C   . CYS B 1 176 ? 28.09300  22.87600  64.70500 1.000 14.18000 ? 176 CYS B C   1 
ATOM   4692 O  O   . CYS B 1 176 ? 27.01200  23.19600  65.20000 1.000 13.82000 ? 176 CYS B O   1 
ATOM   4693 C  CB  . CYS B 1 176 ? 28.56600  20.52100  65.40600 1.000 18.56000 ? 176 CYS B CB  1 
ATOM   4694 S  SG  . CYS B 1 176 ? 28.42200  19.88900  63.73000 1.000 19.66000 ? 176 CYS B SG  1 
ATOM   4695 N  N   . ARG B 1 177 ? 28.50800  23.32500  63.51200 1.000 13.98000 ? 177 ARG B N   1 
ATOM   4696 C  CA  . ARG B 1 177 ? 27.66900  24.18600  62.68900 1.000 15.12000 ? 177 ARG B CA  1 
ATOM   4697 C  C   . ARG B 1 177 ? 27.16600  23.49100  61.43700 1.000 15.06000 ? 177 ARG B C   1 
ATOM   4698 O  O   . ARG B 1 177 ? 26.24000  24.00100  60.78800 1.000 13.60000 ? 177 ARG B O   1 
ATOM   4699 C  CB  . ARG B 1 177 ? 28.42700  25.46500  62.28100 1.000 16.87000 ? 177 ARG B CB  1 
ATOM   4700 C  CG  . ARG B 1 177 ? 28.95800  26.29500  63.45800 1.000 18.24000 ? 177 ARG B CG  1 
ATOM   4701 C  CD  . ARG B 1 177 ? 27.91000  27.24500  64.06100 1.000 15.34000 ? 177 ARG B CD  1 
ATOM   4702 N  NE  . ARG B 1 177 ? 26.85300  26.54100  64.78500 1.000 23.36000 ? 177 ARG B NE  1 
ATOM   4703 C  CZ  . ARG B 1 177 ? 25.60800  26.36300  64.33300 1.000 23.08000 ? 177 ARG B CZ  1 
ATOM   4704 N  NH1 . ARG B 1 177 ? 25.24800  26.83000  63.14500 1.000 22.68000 ? 177 ARG B NH1 1 
ATOM   4705 N  NH2 . ARG B 1 177 ? 24.71900  25.70000  65.06500 1.000 22.74000 ? 177 ARG B NH2 1 
ATOM   4706 N  N   . SER B 1 178 ? 27.74100  22.34500  61.08300 1.000 13.35000 ? 178 SER B N   1 
ATOM   4707 C  CA  . SER B 1 178 ? 27.32200  21.62900  59.89100 1.000 13.95000 ? 178 SER B CA  1 
ATOM   4708 C  C   . SER B 1 178 ? 27.61600  20.15000  60.07700 1.000 14.18000 ? 178 SER B C   1 
ATOM   4709 O  O   . SER B 1 178 ? 28.54000  19.78000  60.80200 1.000 13.73000 ? 178 SER B O   1 
ATOM   4710 C  CB  . SER B 1 178 ? 28.04900  22.17300  58.65000 1.000 16.21000 ? 178 SER B CB  1 
ATOM   4711 O  OG  . SER B 1 178 ? 27.71100  21.42700  57.49800 1.000 13.03000 ? 178 SER B OG  1 
ATOM   4712 N  N   . ILE B 1 179 ? 26.82400  19.29900  59.43900 1.000 13.64000 ? 179 ILE B N   1 
ATOM   4713 C  CA  . ILE B 1 179 ? 27.21400  17.90500  59.26900 1.000 11.81000 ? 179 ILE B CA  1 
ATOM   4714 C  C   . ILE B 1 179 ? 27.36600  17.62700  57.78400 1.000 15.13000 ? 179 ILE B C   1 
ATOM   4715 O  O   . ILE B 1 179 ? 26.53200  18.04900  56.97000 1.000 14.06000 ? 179 ILE B O   1 
ATOM   4716 C  CB  . ILE B 1 179 ? 26.23800  16.91100  59.93300 1.000 15.44000 ? 179 ILE B CB  1 
ATOM   4717 C  CG1 . ILE B 1 179 ? 24.78800  17.07500  59.45200 1.000 13.49000 ? 179 ILE B CG1 1 
ATOM   4718 C  CG2 . ILE B 1 179 ? 26.33300  17.00700  61.46400 1.000 12.32000 ? 179 ILE B CG2 1 
ATOM   4719 C  CD1 . ILE B 1 179 ? 23.89600  15.91400  59.87800 1.000 12.28000 ? 179 ILE B CD1 1 
ATOM   4720 N  N   . SER B 1 180 ? 28.45000  16.94600  57.43100 1.000 15.15000 ? 180 SER B N   1 
ATOM   4721 C  CA  . SER B 1 180 ? 28.65900  16.48100  56.07000 1.000 12.18000 ? 180 SER B CA  1 
ATOM   4722 C  C   . SER B 1 180 ? 27.99400  15.11400  55.92200 1.000 13.37000 ? 180 SER B C   1 
ATOM   4723 O  O   . SER B 1 180 ? 28.33900  14.17400  56.64100 1.000 15.02000 ? 180 SER B O   1 
ATOM   4724 C  CB  . SER B 1 180 ? 30.16000  16.41700  55.77000 1.000 12.80000 ? 180 SER B CB  1 
ATOM   4725 O  OG  . SER B 1 180 ? 30.41800  15.73600  54.55700 1.000 13.89000 ? 180 SER B OG  1 
ATOM   4726 N  N   . ILE B 1 181 ? 27.02500  15.00900  55.02200 1.000 13.90000 ? 181 ILE B N   1 
ATOM   4727 C  CA  . ILE B 1 181 ? 26.29700  13.75900  54.80300 1.000 13.49000 ? 181 ILE B CA  1 
ATOM   4728 C  C   . ILE B 1 181 ? 26.41900  13.41300  53.32900 1.000 14.81000 ? 181 ILE B C   1 
ATOM   4729 O  O   . ILE B 1 181 ? 26.68400  14.29800  52.49800 1.000 15.49000 ? 181 ILE B O   1 
ATOM   4730 C  CB  . ILE B 1 181 ? 24.81800  13.86900  55.24500 1.000 14.41000 ? 181 ILE B CB  1 
ATOM   4731 C  CG1 . ILE B 1 181 ? 24.03300  14.85100  54.34900 1.000 11.22000 ? 181 ILE B CG1 1 
ATOM   4732 C  CG2 . ILE B 1 181 ? 24.75100  14.26600  56.71200 1.000 15.69000 ? 181 ILE B CG2 1 
ATOM   4733 C  CD1 . ILE B 1 181 ? 22.50500  14.83400  54.57900 1.000 14.10000 ? 181 ILE B CD1 1 
ATOM   4734 N  N   . PRO B 1 182 ? 26.25100  12.13700  52.96200 1.000 16.70000 ? 182 PRO B N   1 
ATOM   4735 C  CA  . PRO B 1 182 ? 26.40500  11.75200  51.54700 1.000 15.98000 ? 182 PRO B CA  1 
ATOM   4736 C  C   . PRO B 1 182 ? 25.38600  12.45300  50.66300 1.000 16.48000 ? 182 PRO B C   1 
ATOM   4737 O  O   . PRO B 1 182 ? 24.18400  12.43500  50.93400 1.000 15.75000 ? 182 PRO B O   1 
ATOM   4738 C  CB  . PRO B 1 182 ? 26.18200  10.23600  51.54600 1.000 12.56000 ? 182 PRO B CB  1 
ATOM   4739 C  CG  . PRO B 1 182 ? 26.24600  9.80100   52.97300 1.000 18.99000 ? 182 PRO B CG  1 
ATOM   4740 C  CD  . PRO B 1 182 ? 25.96000  10.98300  53.83700 1.000 15.47000 ? 182 PRO B CD  1 
ATOM   4741 N  N   . GLU B 1 183 ? 25.87000  13.04300  49.57000 1.000 12.13000 ? 183 GLU B N   1 
ATOM   4742 C  CA  . GLU B 1 183 ? 24.97900  13.83700  48.73000 1.000 15.02000 ? 183 GLU B CA  1 
ATOM   4743 C  C   . GLU B 1 183 ? 23.96200  12.97500  48.00200 1.000 15.84000 ? 183 GLU B C   1 
ATOM   4744 O  O   . GLU B 1 183 ? 22.84700  13.43800  47.75500 1.000 16.37000 ? 183 GLU B O   1 
ATOM   4745 C  CB  . GLU B 1 183 ? 25.76700  14.65700  47.71000 1.000 15.96000 ? 183 GLU B CB  1 
ATOM   4746 C  CG  . GLU B 1 183 ? 26.61700  13.84300  46.73300 1.000 15.47000 ? 183 GLU B CG  1 
ATOM   4747 C  CD  . GLU B 1 183 ? 27.07900  14.69600  45.57800 1.000 21.68000 ? 183 GLU B CD  1 
ATOM   4748 O  OE1 . GLU B 1 183 ? 26.43000  15.73800  45.31500 1.000 22.91000 ? 183 GLU B OE1 1 
ATOM   4749 O  OE2 . GLU B 1 183 ? 28.09100  14.34200  44.93900 1.000 19.81000 ? 183 GLU B OE2 1 
ATOM   4750 N  N   . THR B 1 184 ? 24.32800  11.74100  47.63100 1.000 14.15000 ? 184 THR B N   1 
ATOM   4751 C  CA  . THR B 1 184 ? 23.44000  10.82200  46.91100 1.000 13.14000 ? 184 THR B CA  1 
ATOM   4752 C  C   . THR B 1 184 ? 23.52700  9.48100   47.62000 1.000 14.14000 ? 184 THR B C   1 
ATOM   4753 O  O   . THR B 1 184 ? 24.24800  8.57600   47.17700 1.000 14.37000 ? 184 THR B O   1 
ATOM   4754 C  CB  . THR B 1 184 ? 23.80600  10.70100  45.42600 1.000 17.42000 ? 184 THR B CB  1 
ATOM   4755 O  OG1 . THR B 1 184 ? 25.20000  10.37400  45.27500 1.000 14.86000 ? 184 THR B OG1 1 
ATOM   4756 C  CG2 . THR B 1 184 ? 23.50300  11.99900  44.70000 1.000 15.00000 ? 184 THR B CG2 1 
ATOM   4757 N  N   . PRO B 1 185 ? 22.81700  9.33300   48.74300 1.000 13.87000 ? 185 PRO B N   1 
ATOM   4758 C  CA  . PRO B 1 185 ? 23.00600  8.14400   49.59700 1.000 15.58000 ? 185 PRO B CA  1 
ATOM   4759 C  C   . PRO B 1 185 ? 22.72500  6.83700   48.90200 1.000 16.45000 ? 185 PRO B C   1 
ATOM   4760 O  O   . PRO B 1 185 ? 23.31900  5.81800   49.27200 1.000 17.63000 ? 185 PRO B O   1 
ATOM   4761 C  CB  . PRO B 1 185 ? 22.01600  8.37400   50.74800 1.000 13.38000 ? 185 PRO B CB  1 
ATOM   4762 C  CG  . PRO B 1 185 ? 21.74200  9.82800   50.74500 1.000 19.82000 ? 185 PRO B CG  1 
ATOM   4763 C  CD  . PRO B 1 185 ? 21.91400  10.32500  49.34800 1.000 14.16000 ? 185 PRO B CD  1 
ATOM   4764 N  N   . TYR B 1 186 ? 21.83000  6.82800   47.91300 1.000 14.33000 ? 186 TYR B N   1 
ATOM   4765 C  CA  . TYR B 1 186 ? 21.49200  5.60000   47.20500 1.000 15.59000 ? 186 TYR B CA  1 
ATOM   4766 C  C   . TYR B 1 186 ? 22.64000  5.08500   46.34400 1.000 15.97000 ? 186 TYR B C   1 
ATOM   4767 O  O   . TYR B 1 186 ? 22.57700  3.94000   45.89700 1.000 15.01000 ? 186 TYR B O   1 
ATOM   4768 C  CB  . TYR B 1 186 ? 20.25500  5.81700   46.33600 1.000 16.73000 ? 186 TYR B CB  1 
ATOM   4769 C  CG  . TYR B 1 186 ? 20.32200  7.06300   45.48000 1.000 16.74000 ? 186 TYR B CG  1 
ATOM   4770 C  CD1 . TYR B 1 186 ? 20.81600  7.01100   44.17800 1.000 17.48000 ? 186 TYR B CD1 1 
ATOM   4771 C  CD2 . TYR B 1 186 ? 19.90700  8.29800   45.98200 1.000 15.62000 ? 186 TYR B CD2 1 
ATOM   4772 C  CE1 . TYR B 1 186 ? 20.89600  8.15100   43.39200 1.000 15.09000 ? 186 TYR B CE1 1 
ATOM   4773 C  CE2 . TYR B 1 186 ? 19.97800  9.45200   45.20600 1.000 16.54000 ? 186 TYR B CE2 1 
ATOM   4774 C  CZ  . TYR B 1 186 ? 20.46600  9.37000   43.91100 1.000 16.89000 ? 186 TYR B CZ  1 
ATOM   4775 O  OH  . TYR B 1 186 ? 20.53100  10.51300  43.14400 1.000 15.90000 ? 186 TYR B OH  1 
ATOM   4776 N  N   . GLY B 1 187 ? 23.66600  5.89600   46.09200 1.000 16.39000 ? 187 GLY B N   1 
ATOM   4777 C  CA  . GLY B 1 187 ? 24.85500  5.45900   45.37700 1.000 16.68000 ? 187 GLY B CA  1 
ATOM   4778 C  C   . GLY B 1 187 ? 25.99800  4.99700   46.25500 1.000 19.32000 ? 187 GLY B C   1 
ATOM   4779 O  O   . GLY B 1 187 ? 27.04600  4.58900   45.73900 1.000 22.31000 ? 187 GLY B O   1 
ATOM   4780 N  N   . VAL B 1 188 ? 25.82800  5.03400   47.57400 1.000 17.10000 ? 188 VAL B N   1 
ATOM   4781 C  CA  . VAL B 1 188 ? 26.89000  4.68900   48.51500 1.000 17.80000 ? 188 VAL B CA  1 
ATOM   4782 C  C   . VAL B 1 188 ? 26.86000  3.18300   48.77000 1.000 18.69000 ? 188 VAL B C   1 
ATOM   4783 O  O   . VAL B 1 188 ? 25.87300  2.65200   49.29500 1.000 20.11000 ? 188 VAL B O   1 
ATOM   4784 C  CB  . VAL B 1 188 ? 26.74600  5.48200   49.82800 1.000 16.95000 ? 188 VAL B CB  1 
ATOM   4785 C  CG1 . VAL B 1 188 ? 27.75200  4.99400   50.85300 1.000 22.14000 ? 188 VAL B CG1 1 
ATOM   4786 C  CG2 . VAL B 1 188 ? 26.95800  6.96900   49.58400 1.000 19.84000 ? 188 VAL B CG2 1 
ATOM   4787 N  N   . GLY B 1 189 ? 27.94500  2.49700   48.39600 1.000 25.58000 ? 189 GLY B N   1 
ATOM   4788 C  CA  . GLY B 1 189 ? 28.02500  1.06200   48.62100 1.000 21.84000 ? 189 GLY B CA  1 
ATOM   4789 C  C   . GLY B 1 189 ? 26.89200  0.34800   47.91800 1.000 25.80000 ? 189 GLY B C   1 
ATOM   4790 O  O   . GLY B 1 189 ? 26.58400  0.62400   46.75700 1.000 24.68000 ? 189 GLY B O   1 
ATOM   4791 N  N   . GLU B 1 190 ? 26.22400  -0.55800  48.63200 1.000 30.33000 ? 190 GLU B N   1 
ATOM   4792 C  CA  . GLU B 1 190 ? 25.04100  -1.19200  48.06500 1.000 25.68000 ? 190 GLU B CA  1 
ATOM   4793 C  C   . GLU B 1 190 ? 23.82400  -0.27900  48.09600 1.000 30.38000 ? 190 GLU B C   1 
ATOM   4794 O  O   . GLU B 1 190 ? 22.76300  -0.66400  47.58600 1.000 28.92000 ? 190 GLU B O   1 
ATOM   4795 C  CB  . GLU B 1 190 ? 24.73300  -2.50600  48.79700 1.000 32.66000 ? 190 GLU B CB  1 
ATOM   4796 C  CG  . GLU B 1 190 ? 25.76000  -3.61200  48.54300 1.000 35.19000 ? 190 GLU B CG  1 
ATOM   4797 C  CD  . GLU B 1 190 ? 26.06800  -3.81900  47.05800 1.000 47.21000 ? 190 GLU B CD  1 
ATOM   4798 O  OE1 . GLU B 1 190 ? 25.11700  -3.93200  46.25000 1.000 51.40000 ? 190 GLU B OE1 1 
ATOM   4799 O  OE2 . GLU B 1 190 ? 27.26400  -3.86900  46.69400 1.000 48.59000 ? 190 GLU B OE2 1 
ATOM   4800 N  N   . GLY B 1 191 ? 23.94700  0.91500   48.67300 1.000 24.07000 ? 191 GLY B N   1 
ATOM   4801 C  CA  . GLY B 1 191 ? 22.84200  1.85200   48.68900 1.000 18.67000 ? 191 GLY B CA  1 
ATOM   4802 C  C   . GLY B 1 191 ? 22.27700  2.06100   50.07400 1.000 21.78000 ? 191 GLY B C   1 
ATOM   4803 O  O   . GLY B 1 191 ? 21.93400  1.09800   50.76500 1.000 23.52000 ? 191 GLY B O   1 
ATOM   4804 N  N   . PHE B 1 192 ? 22.19500  3.30900   50.50000 1.000 18.80000 ? 192 PHE B N   1 
ATOM   4805 C  CA  . PHE B 1 192 ? 21.48300  3.70600   51.70100 1.000 18.24000 ? 192 PHE B CA  1 
ATOM   4806 C  C   . PHE B 1 192 ? 20.20500  4.44000   51.30800 1.000 18.92000 ? 192 PHE B C   1 
ATOM   4807 O  O   . PHE B 1 192 ? 20.03200  4.83100   50.14900 1.000 16.40000 ? 192 PHE B O   1 
ATOM   4808 C  CB  . PHE B 1 192 ? 22.38000  4.58600   52.57800 1.000 14.78000 ? 192 PHE B CB  1 
ATOM   4809 C  CG  . PHE B 1 192 ? 23.50900  3.83500   53.23000 1.000 21.72000 ? 192 PHE B CG  1 
ATOM   4810 C  CD1 . PHE B 1 192 ? 24.70200  3.62400   52.55200 1.000 19.58000 ? 192 PHE B CD1 1 
ATOM   4811 C  CD2 . PHE B 1 192 ? 23.37000  3.32800   54.51700 1.000 21.70000 ? 192 PHE B CD2 1 
ATOM   4812 C  CE1 . PHE B 1 192 ? 25.75600  2.92700   53.15100 1.000 22.41000 ? 192 PHE B CE1 1 
ATOM   4813 C  CE2 . PHE B 1 192 ? 24.40500  2.62400   55.11800 1.000 21.51000 ? 192 PHE B CE2 1 
ATOM   4814 C  CZ  . PHE B 1 192 ? 25.61100  2.42800   54.42700 1.000 22.56000 ? 192 PHE B CZ  1 
ATOM   4815 N  N   . PRO B 1 193 ? 19.27300  4.61900   52.24100 1.000 16.06000 ? 193 PRO B N   1 
ATOM   4816 C  CA  . PRO B 1 193 ? 17.97400  5.21600   51.89000 1.000 20.24000 ? 193 PRO B CA  1 
ATOM   4817 C  C   . PRO B 1 193 ? 18.10200  6.62200   51.31400 1.000 15.58000 ? 193 PRO B C   1 
ATOM   4818 O  O   . PRO B 1 193 ? 18.95100  7.41000   51.73400 1.000 18.09000 ? 193 PRO B O   1 
ATOM   4819 C  CB  . PRO B 1 193 ? 17.22500  5.23600   53.22900 1.000 17.24000 ? 193 PRO B CB  1 
ATOM   4820 C  CG  . PRO B 1 193 ? 17.84400  4.14500   54.02600 1.000 16.38000 ? 193 PRO B CG  1 
ATOM   4821 C  CD  . PRO B 1 193 ? 19.28200  4.06600   53.61000 1.000 19.52000 ? 193 PRO B CD  1 
ATOM   4822 N  N   . ASP B 1 194 ? 17.22800  6.94800   50.36200 1.000 16.87000 ? 194 ASP B N   1 
ATOM   4823 C  CA  . ASP B 1 194 ? 17.29900  8.27100   49.75500 1.000 14.62000 ? 194 ASP B CA  1 
ATOM   4824 C  C   . ASP B 1 194 ? 16.53400  9.29800   50.59200 1.000 17.24000 ? 194 ASP B C   1 
ATOM   4825 O  O   . ASP B 1 194 ? 15.83200  8.96000   51.54700 1.000 16.74000 ? 194 ASP B O   1 
ATOM   4826 C  CB  . ASP B 1 194 ? 16.80300  8.23400   48.30400 1.000 17.42000 ? 194 ASP B CB  1 
ATOM   4827 C  CG  . ASP B 1 194 ? 15.29100  8.05000   48.17500 1.000 22.28000 ? 194 ASP B CG  1 
ATOM   4828 O  OD1 . ASP B 1 194 ? 14.62600  7.53100   49.08300 1.000 25.64000 ? 194 ASP B OD1 1 
ATOM   4829 O  OD2 . ASP B 1 194 ? 14.76600  8.42400   47.11700 1.000 32.53000 ? 194 ASP B OD2 1 
ATOM   4830 N  N   . PHE B 1 195 ? 16.70400  10.57700  50.23000 1.000 14.98000 ? 195 PHE B N   1 
ATOM   4831 C  CA  . PHE B 1 195 ? 16.14000  11.66100  51.03200 1.000 16.24000 ? 195 PHE B CA  1 
ATOM   4832 C  C   . PHE B 1 195 ? 14.61500  11.67500  50.97900 1.000 17.87000 ? 195 PHE B C   1 
ATOM   4833 O  O   . PHE B 1 195 ? 13.97300  12.18200  51.89900 1.000 15.35000 ? 195 PHE B O   1 
ATOM   4834 C  CB  . PHE B 1 195 ? 16.68000  13.00800  50.55700 1.000 13.78000 ? 195 PHE B CB  1 
ATOM   4835 C  CG  . PHE B 1 195 ? 18.15900  13.17000  50.75200 1.000 17.83000 ? 195 PHE B CG  1 
ATOM   4836 C  CD1 . PHE B 1 195 ? 18.75800  12.80100  51.94600 1.000 16.57000 ? 195 PHE B CD1 1 
ATOM   4837 C  CD2 . PHE B 1 195 ? 18.95700  13.68800  49.73900 1.000 15.20000 ? 195 PHE B CD2 1 
ATOM   4838 C  CE1 . PHE B 1 195 ? 20.13300  12.95900  52.13500 1.000 18.63000 ? 195 PHE B CE1 1 
ATOM   4839 C  CE2 . PHE B 1 195 ? 20.33200  13.82700  49.92500 1.000 16.70000 ? 195 PHE B CE2 1 
ATOM   4840 C  CZ  . PHE B 1 195 ? 20.91100  13.46300  51.12500 1.000 13.70000 ? 195 PHE B CZ  1 
ATOM   4841 N  N   . LYS B 1 196 ? 14.02900  11.15200  49.90500 1.000 17.23000 ? 196 LYS B N   1 
ATOM   4842 C  CA  . LYS B 1 196 ? 12.57900  11.13400  49.75200 1.000 18.51000 ? 196 LYS B CA  1 
ATOM   4843 C  C   . LYS B 1 196 ? 11.92100  10.07000  50.61400 1.000 18.46000 ? 196 LYS B C   1 
ATOM   4844 O  O   . LYS B 1 196 ? 10.71200  10.15000  50.87200 1.000 19.05000 ? 196 LYS B O   1 
ATOM   4845 C  CB  . LYS B 1 196 ? 12.23700  10.88900  48.28200 1.000 21.30000 ? 196 LYS B CB  1 
ATOM   4846 C  CG  . LYS B 1 196 ? 10.79400  11.15000  47.88900 1.000 23.75000 ? 196 LYS B CG  1 
ATOM   4847 C  CD  . LYS B 1 196 ? 10.64600  10.86300  46.39200 1.000 32.19000 ? 196 LYS B CD  1 
ATOM   4848 C  CE  . LYS B 1 196 ? 9.19800   10.89200  45.93300 1.000 41.68000 ? 196 LYS B CE  1 
ATOM   4849 N  NZ  . LYS B 1 196 ? 8.63700   12.27100  45.92700 1.000 45.58000 ? 196 LYS B NZ  1 
ATOM   4850 N  N   . SER B 1 197 ? 12.68800  9.07600   51.06100 1.000 17.73000 ? 197 SER B N   1 
ATOM   4851 C  CA  . SER B 1 197 ? 12.11000  7.92900   51.75100 1.000 16.41000 ? 197 SER B CA  1 
ATOM   4852 C  C   . SER B 1 197 ? 11.60800  8.27500   53.13800 1.000 19.66000 ? 197 SER B C   1 
ATOM   4853 O  O   . SER B 1 197 ? 10.81700  7.51000   53.69300 1.000 17.19000 ? 197 SER B O   1 
ATOM   4854 C  CB  . SER B 1 197 ? 13.14200  6.81100   51.88700 1.000 20.22000 ? 197 SER B CB  1 
ATOM   4855 O  OG  . SER B 1 197 ? 14.13000  7.16400   52.86100 1.000 17.76000 ? 197 SER B OG  1 
ATOM   4856 N  N   . GLY B 1 198 ? 12.07900  9.37800   53.72400 1.000 19.37000 ? 198 GLY B N   1 
ATOM   4857 C  CA  . GLY B 1 198 ? 11.77900  9.72400   55.09800 1.000 20.47000 ? 198 GLY B CA  1 
ATOM   4858 C  C   . GLY B 1 198 ? 12.79300  9.23800   56.11600 1.000 19.68000 ? 198 GLY B C   1 
ATOM   4859 O  O   . GLY B 1 198 ? 12.74300  9.66600   57.26900 1.000 14.58000 ? 198 GLY B O   1 
ATOM   4860 N  N   . TYR B 1 199 ? 13.71900  8.36900   55.71700 1.000 18.68000 ? 199 TYR B N   1 
ATOM   4861 C  CA  . TYR B 1 199 ? 14.72100  7.84300   56.63800 1.000 18.43000 ? 199 TYR B CA  1 
ATOM   4862 C  C   . TYR B 1 199 ? 15.51500  8.95200   57.31300 1.000 18.45000 ? 199 TYR B C   1 
ATOM   4863 O  O   . TYR B 1 199 ? 15.86600  8.84300   58.49100 1.000 17.09000 ? 199 TYR B O   1 
ATOM   4864 C  CB  . TYR B 1 199 ? 15.66100  6.92100   55.86700 1.000 15.93000 ? 199 TYR B CB  1 
ATOM   4865 C  CG  . TYR B 1 199 ? 16.85100  6.41000   56.64600 1.000 16.73000 ? 199 TYR B CG  1 
ATOM   4866 C  CD1 . TYR B 1 199 ? 16.74000  5.29800   57.46900 1.000 20.33000 ? 199 TYR B CD1 1 
ATOM   4867 C  CD2 . TYR B 1 199 ? 18.10000  7.01200   56.52100 1.000 15.10000 ? 199 TYR B CD2 1 
ATOM   4868 C  CE1 . TYR B 1 199 ? 17.83300  4.81300   58.16300 1.000 18.90000 ? 199 TYR B CE1 1 
ATOM   4869 C  CE2 . TYR B 1 199 ? 19.19400  6.53100   57.20900 1.000 16.07000 ? 199 TYR B CE2 1 
ATOM   4870 C  CZ  . TYR B 1 199 ? 19.06000  5.43200   58.02300 1.000 16.78000 ? 199 TYR B CZ  1 
ATOM   4871 O  OH  . TYR B 1 199 ? 20.14800  4.95000   58.71600 1.000 19.40000 ? 199 TYR B OH  1 
ATOM   4872 N  N   . TRP B 1 200 ? 15.83000  10.01400  56.57200 1.000 15.80000 ? 200 TRP B N   1 
ATOM   4873 C  CA  . TRP B 1 200 ? 16.65900  11.10700  57.05800 1.000 18.02000 ? 200 TRP B CA  1 
ATOM   4874 C  C   . TRP B 1 200 ? 15.87500  12.13200  57.86200 1.000 15.80000 ? 200 TRP B C   1 
ATOM   4875 O  O   . TRP B 1 200 ? 16.48100  13.03400  58.44700 1.000 14.84000 ? 200 TRP B O   1 
ATOM   4876 C  CB  . TRP B 1 200 ? 17.35600  11.78900  55.86800 1.000 16.94000 ? 200 TRP B CB  1 
ATOM   4877 C  CG  . TRP B 1 200 ? 18.29000  10.85900  55.12500 1.000 14.14000 ? 200 TRP B CG  1 
ATOM   4878 C  CD1 . TRP B 1 200 ? 17.95200  9.96100   54.16200 1.000 17.98000 ? 200 TRP B CD1 1 
ATOM   4879 C  CD2 . TRP B 1 200 ? 19.71100  10.72300  55.31900 1.000 16.20000 ? 200 TRP B CD2 1 
ATOM   4880 N  NE1 . TRP B 1 200 ? 19.06900  9.28300   53.73500 1.000 17.32000 ? 200 TRP B NE1 1 
ATOM   4881 C  CE2 . TRP B 1 200 ? 20.15900  9.73300   54.43000 1.000 12.98000 ? 200 TRP B CE2 1 
ATOM   4882 C  CE3 . TRP B 1 200 ? 20.63800  11.35000  56.15600 1.000 18.29000 ? 200 TRP B CE3 1 
ATOM   4883 C  CZ2 . TRP B 1 200 ? 21.49100  9.33800   54.35700 1.000 16.22000 ? 200 TRP B CZ2 1 
ATOM   4884 C  CZ3 . TRP B 1 200 ? 21.96900  10.97100  56.07600 1.000 16.15000 ? 200 TRP B CZ3 1 
ATOM   4885 C  CH2 . TRP B 1 200 ? 22.38400  9.97000   55.18400 1.000 20.25000 ? 200 TRP B CH2 1 
ATOM   4886 N  N   . ASP B 1 201 ? 14.55100  12.00300  57.92200 1.000 16.57000 ? 201 ASP B N   1 
ATOM   4887 C  CA  . ASP B 1 201 ? 13.74500  13.05300  58.53500 1.000 17.65000 ? 201 ASP B CA  1 
ATOM   4888 C  C   . ASP B 1 201 ? 14.13400  13.32600  59.98000 1.000 13.50000 ? 201 ASP B C   1 
ATOM   4889 O  O   . ASP B 1 201 ? 14.27500  14.50700  60.33600 1.000 15.06000 ? 201 ASP B O   1 
ATOM   4890 C  CB  . ASP B 1 201 ? 12.25600  12.70800  58.39000 1.000 17.59000 ? 201 ASP B CB  1 
ATOM   4891 C  CG  . ASP B 1 201 ? 11.75700  12.91200  56.97600 1.000 20.27000 ? 201 ASP B CG  1 
ATOM   4892 O  OD1 . ASP B 1 201 ? 12.57500  13.29900  56.10600 1.000 18.09000 ? 201 ASP B OD1 1 
ATOM   4893 O  OD2 . ASP B 1 201 ? 10.55400  12.68900  56.73200 1.000 19.43000 ? 201 ASP B OD2 1 
ATOM   4894 N  N   . PRO B 1 202 ? 14.33500  12.33000  60.85000 1.000 18.55000 ? 202 PRO B N   1 
ATOM   4895 C  CA  . PRO B 1 202 ? 14.72000  12.67600  62.22700 1.000 16.14000 ? 202 PRO B CA  1 
ATOM   4896 C  C   . PRO B 1 202 ? 16.08000  13.32900  62.30200 1.000 19.10000 ? 202 PRO B C   1 
ATOM   4897 O  O   . PRO B 1 202 ? 16.31900  14.11600  63.22900 1.000 15.29000 ? 202 PRO B O   1 
ATOM   4898 C  CB  . PRO B 1 202 ? 14.68000  11.33400  62.97900 1.000 20.25000 ? 202 PRO B CB  1 
ATOM   4899 C  CG  . PRO B 1 202 ? 14.43100  10.30000  62.00800 1.000 22.65000 ? 202 PRO B CG  1 
ATOM   4900 C  CD  . PRO B 1 202 ? 13.96600  10.90700  60.71900 1.000 18.72000 ? 202 PRO B CD  1 
ATOM   4901 N  N   . ILE B 1 203 ? 16.96700  13.06200  61.33000 1.000 17.61000 ? 203 ILE B N   1 
ATOM   4902 C  CA  . ILE B 1 203 ? 18.25100  13.75900  61.28500 1.000 15.56000 ? 203 ILE B CA  1 
ATOM   4903 C  C   . ILE B 1 203 ? 18.05300  15.20900  60.86000 1.000 14.19000 ? 203 ILE B C   1 
ATOM   4904 O  O   . ILE B 1 203 ? 18.58800  16.12400  61.48800 1.000 14.06000 ? 203 ILE B O   1 
ATOM   4905 C  CB  . ILE B 1 203 ? 19.23800  13.02200  60.36200 1.000 15.04000 ? 203 ILE B CB  1 
ATOM   4906 C  CG1 . ILE B 1 203 ? 19.51700  11.62800  60.92400 1.000 17.55000 ? 203 ILE B CG1 1 
ATOM   4907 C  CG2 . ILE B 1 203 ? 20.54500  13.81900  60.22000 1.000 17.73000 ? 203 ILE B CG2 1 
ATOM   4908 C  CD1 . ILE B 1 203 ? 20.16900  10.69000  59.93700 1.000 14.43000 ? 203 ILE B CD1 1 
ATOM   4909 N  N   . PHE B 1 204 ? 17.30200  15.43300  59.77300 1.000 13.86000 ? 204 PHE B N   1 
ATOM   4910 C  CA  . PHE B 1 204 ? 16.92600  16.79000  59.36600 1.000 13.88000 ? 204 PHE B CA  1 
ATOM   4911 C  C   . PHE B 1 204 ? 16.29900  17.55900  60.52400 1.000 13.80000 ? 204 PHE B C   1 
ATOM   4912 O  O   . PHE B 1 204 ? 16.59500  18.73900  60.74600 1.000 14.69000 ? 204 PHE B O   1 
ATOM   4913 C  CB  . PHE B 1 204 ? 15.92400  16.75500  58.20200 1.000 13.45000 ? 204 PHE B CB  1 
ATOM   4914 C  CG  . PHE B 1 204 ? 16.44900  16.15600  56.91900 1.000 16.75000 ? 204 PHE B CG  1 
ATOM   4915 C  CD1 . PHE B 1 204 ? 17.79000  15.89500  56.72700 1.000 15.31000 ? 204 PHE B CD1 1 
ATOM   4916 C  CD2 . PHE B 1 204 ? 15.56100  15.84600  55.89700 1.000 19.03000 ? 204 PHE B CD2 1 
ATOM   4917 C  CE1 . PHE B 1 204 ? 18.24500  15.32800  55.52300 1.000 16.73000 ? 204 PHE B CE1 1 
ATOM   4918 C  CE2 . PHE B 1 204 ? 15.99700  15.28700  54.71000 1.000 16.83000 ? 204 PHE B CE2 1 
ATOM   4919 C  CZ  . PHE B 1 204 ? 17.34000  15.02700  54.52200 1.000 17.23000 ? 204 PHE B CZ  1 
ATOM   4920 N  N   . LYS B 1 205 ? 15.39700  16.91100  61.25400 1.000 13.04000 ? 205 LYS B N   1 
ATOM   4921 C  CA  . LYS B 1 205 ? 14.70400  17.58200  62.35500 1.000 14.82000 ? 205 LYS B CA  1 
ATOM   4922 C  C   . LYS B 1 205 ? 15.68900  18.05200  63.41200 1.000 15.38000 ? 205 LYS B C   1 
ATOM   4923 O  O   . LYS B 1 205 ? 15.60900  19.18900  63.89000 1.000 14.96000 ? 205 LYS B O   1 
ATOM   4924 C  CB  . LYS B 1 205 ? 13.67400  16.63700  62.97800 1.000 12.68000 ? 205 LYS B CB  1 
ATOM   4925 C  CG  . LYS B 1 205 ? 12.86400  17.22000  64.13800 1.000 15.34000 ? 205 LYS B CG  1 
ATOM   4926 C  CD  . LYS B 1 205 ? 11.80400  16.20800  64.61200 1.000 18.97000 ? 205 LYS B CD  1 
ATOM   4927 C  CE  . LYS B 1 205 ? 11.15200  16.60500  65.95400 1.000 16.36000 ? 205 LYS B CE  1 
ATOM   4928 N  NZ  . LYS B 1 205 ? 12.11500  16.55400  67.11500 1.000 18.79000 ? 205 LYS B NZ  1 
ATOM   4929 N  N   . ALA B 1 206 ? 16.63500  17.18300  63.77900 1.000 14.36000 ? 206 ALA B N   1 
ATOM   4930 C  CA  . ALA B 1 206 ? 17.62700  17.53100  64.79000 1.000 14.61000 ? 206 ALA B CA  1 
ATOM   4931 C  C   . ALA B 1 206 ? 18.52300  18.67300  64.32100 1.000 16.69000 ? 206 ALA B C   1 
ATOM   4932 O  O   . ALA B 1 206 ? 18.87600  19.56100  65.10800 1.000 15.68000 ? 206 ALA B O   1 
ATOM   4933 C  CB  . ALA B 1 206 ? 18.46300  16.29300  65.13600 1.000 16.38000 ? 206 ALA B CB  1 
ATOM   4934 N  N   . CYS B 1 207 ? 18.91000  18.65900  63.03900 1.000 16.89000 ? 207 CYS B N   1 
ATOM   4935 C  CA  . CYS B 1 207 ? 19.74200  19.73300  62.50400 1.000 14.71000 ? 207 CYS B CA  1 
ATOM   4936 C  C   . CYS B 1 207 ? 19.02800  21.07400  62.56900 1.000 13.68000 ? 207 CYS B C   1 
ATOM   4937 O  O   . CYS B 1 207 ? 19.62500  22.07800  62.96300 1.000 15.96000 ? 207 CYS B O   1 
ATOM   4938 C  CB  . CYS B 1 207 ? 20.15500  19.40900  61.06600 1.000 13.57000 ? 207 CYS B CB  1 
ATOM   4939 S  SG  . CYS B 1 207 ? 21.40600  18.11600  61.00100 1.000 15.98000 ? 207 CYS B SG  1 
ATOM   4940 N  N   . VAL B 1 208 ? 17.74600  21.10800  62.20700 1.000 15.83000 ? 208 VAL B N   1 
ATOM   4941 C  CA  . VAL B 1 208 ? 17.01000  22.37000  62.25300 1.000 19.01000 ? 208 VAL B CA  1 
ATOM   4942 C  C   . VAL B 1 208 ? 16.93000  22.88900  63.68300 1.000 19.23000 ? 208 VAL B C   1 
ATOM   4943 O  O   . VAL B 1 208 ? 17.06300  24.09300  63.93100 1.000 18.99000 ? 208 VAL B O   1 
ATOM   4944 C  CB  . VAL B 1 208 ? 15.61300  22.20300  61.62700 1.000 16.96000 ? 208 VAL B CB  1 
ATOM   4945 C  CG1 . VAL B 1 208 ? 14.75500  23.43300  61.88800 1.000 25.66000 ? 208 VAL B CG1 1 
ATOM   4946 C  CG2 . VAL B 1 208 ? 15.73000  21.96700  60.12300 1.000 17.65000 ? 208 VAL B CG2 1 
ATOM   4947 N  N   . GLU B 1 209 ? 16.74000  21.99200  64.64900 1.000 17.24000 ? 209 GLU B N   1 
ATOM   4948 C  CA  . GLU B 1 209 ? 16.65400  22.42600  66.04000 1.000 15.95000 ? 209 GLU B CA  1 
ATOM   4949 C  C   . GLU B 1 209 ? 17.93100  23.11000  66.51700 1.000 20.01000 ? 209 GLU B C   1 
ATOM   4950 O  O   . GLU B 1 209 ? 17.87200  23.94100  67.42500 1.000 18.93000 ? 209 GLU B O   1 
ATOM   4951 C  CB  . GLU B 1 209 ? 16.31800  21.23000  66.93400 1.000 16.54000 ? 209 GLU B CB  1 
ATOM   4952 C  CG  . GLU B 1 209 ? 14.91000  20.70700  66.69500 1.000 18.36000 ? 209 GLU B CG  1 
ATOM   4953 C  CD  . GLU B 1 209 ? 14.70600  19.28300  67.17600 1.000 18.25000 ? 209 GLU B CD  1 
ATOM   4954 O  OE1 . GLU B 1 209 ? 15.58400  18.75100  67.87600 1.000 19.10000 ? 209 GLU B OE1 1 
ATOM   4955 O  OE2 . GLU B 1 209 ? 13.64300  18.69500  66.87300 1.000 20.91000 ? 209 GLU B OE2 1 
ATOM   4956 N  N   . HIS B 1 210 ? 19.07700  22.80600  65.91400 1.000 15.57000 ? 210 HIS B N   1 
ATOM   4957 C  CA  . HIS B 1 210 ? 20.33800  23.42900  66.28100 1.000 17.13000 ? 210 HIS B CA  1 
ATOM   4958 C  C   . HIS B 1 210 ? 20.85400  24.38300  65.20200 1.000 16.23000 ? 210 HIS B C   1 
ATOM   4959 O  O   . HIS B 1 210 ? 21.97100  24.89500  65.32000 1.000 16.93000 ? 210 HIS B O   1 
ATOM   4960 C  CB  . HIS B 1 210 ? 21.37300  22.34400  66.58500 1.000 17.04000 ? 210 HIS B CB  1 
ATOM   4961 C  CG  . HIS B 1 210 ? 21.02500  21.48700  67.76600 1.000 16.55000 ? 210 HIS B CG  1 
ATOM   4962 N  ND1 . HIS B 1 210 ? 20.99800  21.97300  69.05600 1.000 19.05000 ? 210 HIS B ND1 1 
ATOM   4963 C  CD2 . HIS B 1 210 ? 20.71600  20.17000  67.85300 1.000 17.32000 ? 210 HIS B CD2 1 
ATOM   4964 C  CE1 . HIS B 1 210 ? 20.67500  20.99700  69.88600 1.000 16.58000 ? 210 HIS B CE1 1 
ATOM   4965 N  NE2 . HIS B 1 210 ? 20.50900  19.89000  69.18200 1.000 18.66000 ? 210 HIS B NE2 1 
ATOM   4966 N  N   . ASN B 1 211 ? 20.05300  24.65200  64.17300 1.000 18.62000 ? 211 ASN B N   1 
ATOM   4967 C  CA  . ASN B 1 211 ? 20.46900  25.47600  63.03200 1.000 19.09000 ? 211 ASN B CA  1 
ATOM   4968 C  C   . ASN B 1 211 ? 21.75900  24.94900  62.39500 1.000 18.58000 ? 211 ASN B C   1 
ATOM   4969 O  O   . ASN B 1 211 ? 22.64800  25.71800  62.02300 1.000 16.14000 ? 211 ASN B O   1 
ATOM   4970 C  CB  . ASN B 1 211 ? 20.62400  26.94600  63.44100 1.000 22.36000 ? 211 ASN B CB  1 
ATOM   4971 C  CG  . ASN B 1 211 ? 20.47700  27.90200  62.25600 1.000 35.68000 ? 211 ASN B CG  1 
ATOM   4972 O  OD1 . ASN B 1 211 ? 19.91400  27.54700  61.21200 1.000 35.69000 ? 211 ASN B OD1 1 
ATOM   4973 N  ND2 . ASN B 1 211 ? 21.00100  29.11600  62.40900 1.000 39.12000 ? 211 ASN B ND2 1 
ATOM   4974 N  N   . ILE B 1 212 ? 21.85900  23.62700  62.26000 1.000 16.61000 ? 212 ILE B N   1 
ATOM   4975 C  CA  . ILE B 1 212 ? 23.04500  22.98500  61.69100 1.000 15.79000 ? 212 ILE B CA  1 
ATOM   4976 C  C   . ILE B 1 212 ? 22.83400  22.76100  60.19600 1.000 14.37000 ? 212 ILE B C   1 
ATOM   4977 O  O   . ILE B 1 212 ? 21.80300  22.22000  59.78000 1.000 16.20000 ? 212 ILE B O   1 
ATOM   4978 C  CB  . ILE B 1 212 ? 23.33500  21.66400  62.41800 1.000 14.61000 ? 212 ILE B CB  1 
ATOM   4979 C  CG1 . ILE B 1 212 ? 23.94900  21.96600  63.79300 1.000 16.46000 ? 212 ILE B CG1 1 
ATOM   4980 C  CG2 . ILE B 1 212 ? 24.19800  20.71300  61.55300 1.000 13.50000 ? 212 ILE B CG2 1 
ATOM   4981 C  CD1 . ILE B 1 212 ? 24.16900  20.75800  64.66100 1.000 17.38000 ? 212 ILE B CD1 1 
ATOM   4982 N  N   . VAL B 1 213 ? 23.81500  23.18500  59.38700 1.000 13.55000 ? 213 VAL B N   1 
ATOM   4983 C  CA  . VAL B 1 213 ? 23.74400  23.09700  57.92700 1.000 12.36000 ? 213 VAL B CA  1 
ATOM   4984 C  C   . VAL B 1 213 ? 24.07200  21.68000  57.47200 1.000 14.28000 ? 213 VAL B C   1 
ATOM   4985 O  O   . VAL B 1 213 ? 24.98100  21.03900  58.00800 1.000 15.50000 ? 213 VAL B O   1 
ATOM   4986 C  CB  . VAL B 1 213 ? 24.72100  24.10700  57.29100 1.000 10.44000 ? 213 VAL B CB  1 
ATOM   4987 C  CG1 . VAL B 1 213 ? 24.73900  23.97300  55.75500 1.000 13.18000 ? 213 VAL B CG1 1 
ATOM   4988 C  CG2 . VAL B 1 213 ? 24.37800  25.52000  57.71200 1.000 12.73000 ? 213 VAL B CG2 1 
ATOM   4989 N  N   . LEU B 1 214 ? 23.32600  21.17600  56.48400 1.000 13.76000 ? 214 LEU B N   1 
ATOM   4990 C  CA  . LEU B 1 214 ? 23.71100  19.95500  55.78500 1.000 12.95000 ? 214 LEU B CA  1 
ATOM   4991 C  C   . LEU B 1 214 ? 24.70500  20.32700  54.69100 1.000 14.31000 ? 214 LEU B C   1 
ATOM   4992 O  O   . LEU B 1 214 ? 24.36000  21.08000  53.77900 1.000 12.68000 ? 214 LEU B O   1 
ATOM   4993 C  CB  . LEU B 1 214 ? 22.48300  19.27100  55.17200 1.000 11.76000 ? 214 LEU B CB  1 
ATOM   4994 C  CG  . LEU B 1 214 ? 21.32600  18.89000  56.09500 1.000 15.84000 ? 214 LEU B CG  1 
ATOM   4995 C  CD1 . LEU B 1 214 ? 20.20400  18.19800  55.30100 1.000 15.74000 ? 214 LEU B CD1 1 
ATOM   4996 C  CD2 . LEU B 1 214 ? 21.79100  17.98400  57.21200 1.000 15.83000 ? 214 LEU B CD2 1 
ATOM   4997 N  N   . SER B 1 215 ? 25.94500  19.84600  54.79700 1.000 13.62000 ? 215 SER B N   1 
ATOM   4998 C  CA  . SER B 1 215 ? 26.92200  20.01300  53.72500 1.000 12.56000 ? 215 SER B CA  1 
ATOM   4999 C  C   . SER B 1 215 ? 26.86100  18.78800  52.82300 1.000 13.27000 ? 215 SER B C   1 
ATOM   5000 O  O   . SER B 1 215 ? 27.06700  17.66300  53.28200 1.000 13.75000 ? 215 SER B O   1 
ATOM   5001 C  CB  . SER B 1 215 ? 28.33400  20.20100  54.27900 1.000 12.84000 ? 215 SER B CB  1 
ATOM   5002 O  OG  . SER B 1 215 ? 28.50600  21.52700  54.75500 1.000 13.11000 ? 215 SER B OG  1 
ATOM   5003 N  N   . LEU B 1 216 ? 26.53400  19.00500  51.55900 1.000 14.05000 ? 216 LEU B N   1 
ATOM   5004 C  CA  . LEU B 1 216 ? 26.45200  17.94500  50.55900 1.000 13.65000 ? 216 LEU B CA  1 
ATOM   5005 C  C   . LEU B 1 216 ? 27.64000  18.15200  49.62100 1.000 14.06000 ? 216 LEU B C   1 
ATOM   5006 O  O   . LEU B 1 216 ? 27.54200  18.86600  48.62900 1.000 15.78000 ? 216 LEU B O   1 
ATOM   5007 C  CB  . LEU B 1 216 ? 25.10200  17.98500  49.80200 1.000 15.18000 ? 216 LEU B CB  1 
ATOM   5008 C  CG  . LEU B 1 216 ? 23.91700  17.25800  50.44600 1.000 18.37000 ? 216 LEU B CG  1 
ATOM   5009 C  CD1 . LEU B 1 216 ? 23.67200  17.76400  51.84100 1.000 14.69000 ? 216 LEU B CD1 1 
ATOM   5010 C  CD2 . LEU B 1 216 ? 22.63400  17.39800  49.61300 1.000 14.81000 ? 216 LEU B CD2 1 
ATOM   5011 N  N   . HIS B 1 217 ? 28.76400  17.51500  49.94100 1.000 15.69000 ? 217 HIS B N   1 
ATOM   5012 C  CA  . HIS B 1 217 ? 29.99800  17.71600  49.19700 1.000 11.60000 ? 217 HIS B CA  1 
ATOM   5013 C  C   . HIS B 1 217 ? 30.02900  16.83200  47.95000 1.000 15.78000 ? 217 HIS B C   1 
ATOM   5014 O  O   . HIS B 1 217 ? 29.54900  15.69200  47.96000 1.000 16.11000 ? 217 HIS B O   1 
ATOM   5015 C  CB  . HIS B 1 217 ? 31.19800  17.40000  50.09600 1.000 12.91000 ? 217 HIS B CB  1 
ATOM   5016 C  CG  . HIS B 1 217 ? 32.51900  17.81100  49.52900 1.000 13.78000 ? 217 HIS B CG  1 
ATOM   5017 N  ND1 . HIS B 1 217 ? 33.11800  17.15200  48.47400 1.000 14.78000 ? 217 HIS B ND1 1 
ATOM   5018 C  CD2 . HIS B 1 217 ? 33.38200  18.78900  49.90000 1.000 12.05000 ? 217 HIS B CD2 1 
ATOM   5019 C  CE1 . HIS B 1 217 ? 34.28000  17.72100  48.20500 1.000 16.39000 ? 217 HIS B CE1 1 
ATOM   5020 N  NE2 . HIS B 1 217 ? 34.47000  18.70900  49.06200 1.000 12.50000 ? 217 HIS B NE2 1 
ATOM   5021 N  N   . ILE B 1 218 ? 30.60000  17.37100  46.86800 1.000 16.43000 ? 218 ILE B N   1 
ATOM   5022 C  CA  . ILE B 1 218 ? 30.74400  16.58200  45.64400 1.000 18.48000 ? 218 ILE B CA  1 
ATOM   5023 C  C   . ILE B 1 218 ? 31.53600  15.30300  45.91200 1.000 19.35000 ? 218 ILE B C   1 
ATOM   5024 O  O   . ILE B 1 218 ? 32.29800  15.19200  46.87800 1.000 19.08000 ? 218 ILE B O   1 
ATOM   5025 C  CB  . ILE B 1 218 ? 31.41500  17.40100  44.53300 1.000 19.56000 ? 218 ILE B CB  1 
ATOM   5026 C  CG1 . ILE B 1 218 ? 32.89800  17.59800  44.85300 1.000 21.84000 ? 218 ILE B CG1 1 
ATOM   5027 C  CG2 . ILE B 1 218 ? 30.67000  18.73100  44.32000 1.000 19.24000 ? 218 ILE B CG2 1 
ATOM   5028 C  CD1 . ILE B 1 218 ? 33.72400  18.14200  43.69200 1.000 20.43000 ? 218 ILE B CD1 1 
ATOM   5029 N  N   . GLY B 1 219 ? 31.35100  14.32500  45.03100 1.000 17.55000 ? 219 GLY B N   1 
ATOM   5030 C  CA  . GLY B 1 219 ? 32.04800  13.05500  45.10200 1.000 22.29000 ? 219 GLY B CA  1 
ATOM   5031 C  C   . GLY B 1 219 ? 31.13000  11.85200  45.15900 1.000 23.18000 ? 219 GLY B C   1 
ATOM   5032 O  O   . GLY B 1 219 ? 31.58000  10.73200  44.89400 1.000 23.65000 ? 219 GLY B O   1 
ATOM   5033 N  N   . GLY B 1 220 ? 29.85200  12.04100  45.48900 1.000 18.58000 ? 220 GLY B N   1 
ATOM   5034 C  CA  . GLY B 1 220 ? 28.92400  10.92800  45.50200 1.000 21.51000 ? 220 GLY B CA  1 
ATOM   5035 C  C   . GLY B 1 220 ? 28.22000  10.81800  44.16700 1.000 24.23000 ? 220 GLY B C   1 
ATOM   5036 O  O   . GLY B 1 220 ? 28.02100  9.71600   43.64800 1.000 19.44000 ? 220 GLY B O   1 
ATOM   5037 N  N   . GLY B 1 221 ? 27.85700  11.97100  43.59800 1.000 20.35000 ? 221 GLY B N   1 
ATOM   5038 C  CA  . GLY B 1 221 ? 27.18100  11.97600  42.30400 1.000 22.03000 ? 221 GLY B CA  1 
ATOM   5039 C  C   . GLY B 1 221 ? 27.96600  11.26800  41.21100 1.000 23.45000 ? 221 GLY B C   1 
ATOM   5040 O  O   . GLY B 1 221 ? 27.38900  10.53100  40.40000 1.000 21.37000 ? 221 GLY B O   1 
ATOM   5041 N  N   . ILE B 1 222 ? 29.29300  11.46300  41.18300 1.000 17.83000 ? 222 ILE B N   1 
ATOM   5042 C  CA  . ILE B 1 222 ? 30.12300  10.83600  40.15300 1.000 17.19000 ? 222 ILE B CA  1 
ATOM   5043 C  C   . ILE B 1 222 ? 30.01800  9.32000   40.21400 1.000 19.91000 ? 222 ILE B C   1 
ATOM   5044 O  O   . ILE B 1 222 ? 30.04000  8.65200   39.17400 1.000 16.68000 ? 222 ILE B O   1 
ATOM   5045 C  CB  . ILE B 1 222 ? 31.59600  11.31400  40.25100 1.000 21.48000 ? 222 ILE B CB  1 
ATOM   5046 C  CG1 . ILE B 1 222 ? 32.39600  10.86400  39.02200 1.000 19.48000 ? 222 ILE B CG1 1 
ATOM   5047 C  CG2 . ILE B 1 222 ? 32.29400  10.81400  41.53000 1.000 20.82000 ? 222 ILE B CG2 1 
ATOM   5048 C  CD1 . ILE B 1 222 ? 31.92600  11.48800  37.73200 1.000 24.44000 ? 222 ILE B CD1 1 
ATOM   5049 N  N   . ASN B 1 223 ? 29.86500  8.74800   41.41400 1.000 18.33000 ? 223 ASN B N   1 
ATOM   5050 C  CA  . ASN B 1 223 ? 29.75400  7.29500   41.52100 1.000 20.43000 ? 223 ASN B CA  1 
ATOM   5051 C  C   . ASN B 1 223 ? 28.40800  6.75300   41.03900 1.000 18.96000 ? 223 ASN B C   1 
ATOM   5052 O  O   . ASN B 1 223 ? 28.23400  5.53000   41.01600 1.000 19.81000 ? 223 ASN B O   1 
ATOM   5053 C  CB  . ASN B 1 223 ? 30.01700  6.85300   42.96200 1.000 24.08000 ? 223 ASN B CB  1 
ATOM   5054 C  CG  . ASN B 1 223 ? 31.48000  6.98000   43.35100 1.000 30.89000 ? 223 ASN B CG  1 
ATOM   5055 O  OD1 . ASN B 1 223 ? 32.37100  6.97300   42.49100 1.000 31.64000 ? 223 ASN B OD1 1 
ATOM   5056 N  ND2 . ASN B 1 223 ? 31.73900  7.09600   44.64800 1.000 29.24000 ? 223 ASN B ND2 1 
ATOM   5057 N  N   . LEU B 1 224 ? 27.45900  7.61100   40.66600 1.000 16.32000 ? 224 LEU B N   1 
ATOM   5058 C  CA  . LEU B 1 224 ? 26.22700  7.18700   40.01400 1.000 17.39000 ? 224 LEU B CA  1 
ATOM   5059 C  C   . LEU B 1 224 ? 26.35400  7.04000   38.50500 1.000 18.91000 ? 224 LEU B C   1 
ATOM   5060 O  O   . LEU B 1 224 ? 25.45100  6.46500   37.88400 1.000 20.72000 ? 224 LEU B O   1 
ATOM   5061 C  CB  . LEU B 1 224 ? 25.09800  8.18900   40.26200 1.000 18.40000 ? 224 LEU B CB  1 
ATOM   5062 C  CG  . LEU B 1 224 ? 24.79700  8.57700   41.70000 1.000 20.36000 ? 224 LEU B CG  1 
ATOM   5063 C  CD1 . LEU B 1 224 ? 23.76700  9.68200   41.69500 1.000 16.90000 ? 224 LEU B CD1 1 
ATOM   5064 C  CD2 . LEU B 1 224 ? 24.30200  7.34400   42.43900 1.000 20.53000 ? 224 LEU B CD2 1 
ATOM   5065 N  N   . VAL B 1 225 ? 27.41200  7.57000   37.89600 1.000 15.86000 ? 225 VAL B N   1 
ATOM   5066 C  CA  . VAL B 1 225 ? 27.48000  7.73100   36.44800 1.000 15.19000 ? 225 VAL B CA  1 
ATOM   5067 C  C   . VAL B 1 225 ? 28.31600  6.60300   35.85600 1.000 17.33000 ? 225 VAL B C   1 
ATOM   5068 O  O   . VAL B 1 225 ? 29.52300  6.51500   36.10700 1.000 16.74000 ? 225 VAL B O   1 
ATOM   5069 C  CB  . VAL B 1 225 ? 28.06200  9.09900   36.05300 1.000 16.84000 ? 225 VAL B CB  1 
ATOM   5070 C  CG1 . VAL B 1 225 ? 27.94300  9.31400   34.52900 1.000 15.71000 ? 225 VAL B CG1 1 
ATOM   5071 C  CG2 . VAL B 1 225 ? 27.36200  10.22400  36.79000 1.000 12.52000 ? 225 VAL B CG2 1 
ATOM   5072 N  N   . LYS B 1 226 ? 27.68100  5.76100   35.04500 1.000 17.65000 ? 226 LYS B N   1 
ATOM   5073 C  CA  . LYS B 1 226 ? 28.41700  4.76100   34.28500 1.000 18.03000 ? 226 LYS B CA  1 
ATOM   5074 C  C   . LYS B 1 226 ? 29.41900  5.45100   33.37700 1.000 21.44000 ? 226 LYS B C   1 
ATOM   5075 O  O   . LYS B 1 226 ? 29.11900  6.47600   32.75500 1.000 17.68000 ? 226 LYS B O   1 
ATOM   5076 C  CB  . LYS B 1 226 ? 27.46000  3.89700   33.45500 1.000 18.22000 ? 226 LYS B CB  1 
ATOM   5077 C  CG  . LYS B 1 226 ? 28.17100  2.89600   32.53300 1.000 20.33000 ? 226 LYS B CG  1 
ATOM   5078 C  CD  . LYS B 1 226 ? 27.20300  2.20900   31.57800 1.000 25.06000 ? 226 LYS B CD  1 
ATOM   5079 C  CE  . LYS B 1 226 ? 26.11500  1.44000   32.31700 1.000 24.13000 ? 226 LYS B CE  1 
ATOM   5080 N  NZ  . LYS B 1 226 ? 25.16900  0.74500   31.38400 1.000 31.21000 ? 226 LYS B NZ  1 
ATOM   5081 N  N   . ARG B 1 227 ? 30.62900  4.91100   33.34100 1.000 20.24000 ? 227 ARG B N   1 
ATOM   5082 C  CA  . ARG B 1 227 ? 31.67700  5.38800   32.45700 1.000 20.21000 ? 227 ARG B CA  1 
ATOM   5083 C  C   . ARG B 1 227 ? 32.09400  4.24400   31.54100 1.000 19.44000 ? 227 ARG B C   1 
ATOM   5084 O  O   . ARG B 1 227 ? 31.79200  3.07800   31.81700 1.000 22.98000 ? 227 ARG B O   1 
ATOM   5085 C  CB  . ARG B 1 227 ? 32.88500  5.91200   33.25000 1.000 20.66000 ? 227 ARG B CB  1 
ATOM   5086 C  CG  . ARG B 1 227 ? 32.54800  6.74500   34.49200 1.000 23.18000 ? 227 ARG B CG  1 
ATOM   5087 C  CD  . ARG B 1 227 ? 31.65800  7.95100   34.18200 1.000 23.13000 ? 227 ARG B CD  1 
ATOM   5088 N  NE  . ARG B 1 227 ? 32.28900  8.90100   33.26300 1.000 24.01000 ? 227 ARG B NE  1 
ATOM   5089 C  CZ  . ARG B 1 227 ? 31.77100  9.28000   32.09700 1.000 23.46000 ? 227 ARG B CZ  1 
ATOM   5090 N  NH1 . ARG B 1 227 ? 30.60100  8.79200   31.69400 1.000 16.60000 ? 227 ARG B NH1 1 
ATOM   5091 N  NH2 . ARG B 1 227 ? 32.42900  10.15000  31.33000 1.000 21.59000 ? 227 ARG B NH2 1 
ATOM   5092 N  N   . PRO B 1 228 ? 32.75100  4.55800   30.44300 1.000 22.36000 ? 228 PRO B N   1 
ATOM   5093 C  CA  . PRO B 1 228 ? 33.24200  3.50400   29.57500 1.000 25.29000 ? 228 PRO B CA  1 
ATOM   5094 C  C   . PRO B 1 228 ? 34.30300  2.70800   30.30200 1.000 28.37000 ? 228 PRO B C   1 
ATOM   5095 O  O   . PRO B 1 228 ? 34.83300  3.16200   31.26100 1.000 25.63000 ? 228 PRO B O   1 
ATOM   5096 C  CB  . PRO B 1 228 ? 33.86800  4.24800   28.41400 1.000 24.40000 ? 228 PRO B CB  1 
ATOM   5097 C  CG  . PRO B 1 228 ? 34.05700  5.61300   28.84400 1.000 21.80000 ? 228 PRO B CG  1 
ATOM   5098 C  CD  . PRO B 1 228 ? 33.17400  5.87800   30.01200 1.000 24.43000 ? 228 PRO B CD  1 
ATOM   5099 N  N   . GLU B 1 229 ? 34.66000  1.54900   29.76400 1.000 29.08000 ? 229 GLU B N   1 
ATOM   5100 C  CA  . GLU B 1 229 ? 35.64600  0.71000   30.38600 1.000 33.67000 ? 229 GLU B CA  1 
ATOM   5101 C  C   . GLU B 1 229 ? 37.04400  1.32700   30.42000 1.000 36.34000 ? 229 GLU B C   1 
ATOM   5102 O  O   . GLU B 1 229 ? 37.78500  1.05500   31.31700 1.000 35.01000 ? 229 GLU B O   1 
ATOM   5103 C  CB  . GLU B 1 229 ? 35.68700  -0.69300  29.78000 1.000 41.25000 ? 229 GLU B CB  1 
ATOM   5104 C  CG  . GLU B 1 229 ? 35.59100  -1.77900  30.81100 1.000 47.51000 ? 229 GLU B CG  1 
ATOM   5105 C  CD  . GLU B 1 229 ? 35.17400  -3.09300  30.20500 1.000 56.02000 ? 229 GLU B CD  1 
ATOM   5106 O  OE1 . GLU B 1 229 ? 34.35700  -3.78800  30.80200 1.000 52.20000 ? 229 GLU B OE1 1 
ATOM   5107 O  OE2 . GLU B 1 229 ? 35.68300  -3.40100  29.12100 1.000 58.80000 ? 229 GLU B OE2 1 
ATOM   5108 N  N   . GLY B 1 230 ? 37.36100  2.15600   29.43700 1.000 36.65000 ? 230 GLY B N   1 
ATOM   5109 C  CA  . GLY B 1 230 ? 38.61100  2.87900   29.34500 1.000 43.79000 ? 230 GLY B CA  1 
ATOM   5110 C  C   . GLY B 1 230 ? 38.63300  4.18500   30.13100 1.000 53.78000 ? 230 GLY B C   1 
ATOM   5111 O  O   . GLY B 1 230 ? 38.14800  5.19700   29.73300 1.000 51.51000 ? 230 GLY B O   1 
ATOM   5112 N  N   . PHE B 1 231 ? 39.25000  4.11700   31.27500 1.000 56.56000 ? 231 PHE B N   1 
ATOM   5113 C  CA  . PHE B 1 231 ? 39.39700  5.21300   32.22600 1.000 57.13000 ? 231 PHE B CA  1 
ATOM   5114 C  C   . PHE B 1 231 ? 40.20500  6.43700   31.77000 1.000 56.26000 ? 231 PHE B C   1 
ATOM   5115 O  O   . PHE B 1 231 ? 41.27200  6.29600   31.20500 1.000 55.25000 ? 231 PHE B O   1 
ATOM   5116 C  CB  . PHE B 1 231 ? 40.02300  4.52400   33.42700 1.000 54.21000 ? 231 PHE B CB  1 
ATOM   5117 C  CG  . PHE B 1 231 ? 40.50300  5.41700   34.49200 1.000 61.26000 ? 231 PHE B CG  1 
ATOM   5118 C  CD1 . PHE B 1 231 ? 39.79400  5.53100   35.65600 1.000 61.01000 ? 231 PHE B CD1 1 
ATOM   5119 C  CD2 . PHE B 1 231 ? 41.71500  6.04700   34.38100 1.000 62.58000 ? 231 PHE B CD2 1 
ATOM   5120 C  CE1 . PHE B 1 231 ? 40.26100  6.31100   36.68400 1.000 64.12000 ? 231 PHE B CE1 1 
ATOM   5121 C  CE2 . PHE B 1 231 ? 42.19000  6.83100   35.38300 1.000 65.87000 ? 231 PHE B CE2 1 
ATOM   5122 C  CZ  . PHE B 1 231 ? 41.45300  6.97600   36.54400 1.000 67.39000 ? 231 PHE B CZ  1 
ATOM   5123 N  N   . ASP B 1 232 ? 39.66300  7.62900   31.98100 1.000 45.23000 ? 232 ASP B N   1 
ATOM   5124 C  CA  . ASP B 1 232 ? 40.36600  8.84600   31.67000 1.000 48.14000 ? 232 ASP B CA  1 
ATOM   5125 C  C   . ASP B 1 232 ? 40.28300  9.67200   32.92300 1.000 51.92000 ? 232 ASP B C   1 
ATOM   5126 O  O   . ASP B 1 232 ? 39.22300  10.16400  33.24100 1.000 48.22000 ? 232 ASP B O   1 
ATOM   5127 C  CB  . ASP B 1 232 ? 39.73500  9.61200   30.52200 1.000 39.53000 ? 232 ASP B CB  1 
ATOM   5128 C  CG  . ASP B 1 232 ? 40.57500  10.78500  30.04900 1.000 45.97000 ? 232 ASP B CG  1 
ATOM   5129 O  OD1 . ASP B 1 232 ? 40.20200  11.43100  29.05900 1.000 36.14000 ? 232 ASP B OD1 1 
ATOM   5130 O  OD2 . ASP B 1 232 ? 41.60900  11.07700  30.66300 1.000 48.32000 ? 232 ASP B OD2 1 
ATOM   5131 N  N   . ILE B 1 233 ? 41.38800  9.76900   33.63600 1.000 47.54000 ? 233 ILE B N   1 
ATOM   5132 C  CA  . ILE B 1 233 ? 41.50100  10.56600  34.81900 1.000 44.56000 ? 233 ILE B CA  1 
ATOM   5133 C  C   . ILE B 1 233 ? 40.96700  11.96600  34.54000 1.000 38.36000 ? 233 ILE B C   1 
ATOM   5134 O  O   . ILE B 1 233 ? 40.15800  12.46700  35.27100 1.000 33.72000 ? 233 ILE B O   1 
ATOM   5135 C  CB  . ILE B 1 233 ? 42.97400  10.60400  35.28100 1.000 46.62000 ? 233 ILE B CB  1 
ATOM   5136 C  CG1 . ILE B 1 233 ? 43.20500  11.59500  36.39100 1.000 46.31000 ? 233 ILE B CG1 1 
ATOM   5137 C  CG2 . ILE B 1 233 ? 43.89700  11.03500  34.18300 1.000 49.48000 ? 233 ILE B CG2 1 
ATOM   5138 C  CD1 . ILE B 1 233 ? 44.67000  11.68700  36.73200 1.000 50.55000 ? 233 ILE B CD1 1 
ATOM   5139 N  N   . ASP B 1 234 ? 41.41900  12.55500  33.45800 1.000 33.67000 ? 234 ASP B N   1 
ATOM   5140 C  CA  . ASP B 1 234 ? 40.94400  13.84200  33.08200 1.000 38.73000 ? 234 ASP B CA  1 
ATOM   5141 C  C   . ASP B 1 234 ? 39.42900  13.84700  32.96300 1.000 29.47000 ? 234 ASP B C   1 
ATOM   5142 O  O   . ASP B 1 234 ? 38.85100  14.80500  33.29200 1.000 29.57000 ? 234 ASP B O   1 
ATOM   5143 C  CB  . ASP B 1 234 ? 41.55600  14.24700  31.75200 1.000 35.64000 ? 234 ASP B CB  1 
ATOM   5144 C  CG  . ASP B 1 234 ? 42.95700  14.79500  31.88500 1.000 42.64000 ? 234 ASP B CG  1 
ATOM   5145 O  OD1 . ASP B 1 234 ? 43.49800  15.21100  30.88100 1.000 43.67000 ? 234 ASP B OD1 1 
ATOM   5146 O  OD2 . ASP B 1 234 ? 43.48300  14.83400  32.97200 1.000 37.51000 ? 234 ASP B OD2 1 
ATOM   5147 N  N   . ASN B 1 235 ? 38.81000  12.82600  32.39800 1.000 29.73000 ? 235 ASN B N   1 
ATOM   5148 C  CA  . ASN B 1 235 ? 37.35600  12.84000  32.26600 1.000 27.64000 ? 235 ASN B CA  1 
ATOM   5149 C  C   . ASN B 1 235 ? 36.69500  12.85000  33.63800 1.000 31.67000 ? 235 ASN B C   1 
ATOM   5150 O  O   . ASN B 1 235 ? 35.77400  13.63600  33.90100 1.000 26.13000 ? 235 ASN B O   1 
ATOM   5151 C  CB  . ASN B 1 235 ? 36.90200  11.63600  31.43900 1.000 31.14000 ? 235 ASN B CB  1 
ATOM   5152 C  CG  . ASN B 1 235 ? 35.45300  11.73400  30.99100 1.000 26.15000 ? 235 ASN B CG  1 
ATOM   5153 O  OD1 . ASN B 1 235 ? 34.53900  11.84600  31.81300 1.000 22.18000 ? 235 ASN B OD1 1 
ATOM   5154 N  ND2 . ASN B 1 235 ? 35.23600  11.67900  29.67900 1.000 19.67000 ? 235 ASN B ND2 1 
ATOM   5155 N  N   . MET B 1 236 ? 37.17500  11.99000  34.53600 1.000 29.46000 ? 236 MET B N   1 
ATOM   5156 C  CA  . MET B 1 236 ? 36.67700  11.99600  35.90800 1.000 35.66000 ? 236 MET B CA  1 
ATOM   5157 C  C   . MET B 1 236 ? 36.89600  13.35600  36.56100 1.000 33.02000 ? 236 MET B C   1 
ATOM   5158 O  O   . MET B 1 236 ? 35.96000  13.94900  37.11300 1.000 34.08000 ? 236 MET B O   1 
ATOM   5159 C  CB  . MET B 1 236 ? 37.35900  10.88500  36.70900 1.000 35.87000 ? 236 MET B CB  1 
ATOM   5160 C  CG  . MET B 1 236 ? 37.20300  10.98900  38.21800 1.000 53.72000 ? 236 MET B CG  1 
ATOM   5161 S  SD  . MET B 1 236 ? 38.41100  9.95500   39.08600 1.000 88.40000 ? 236 MET B SD  1 
ATOM   5162 C  CE  . MET B 1 236 ? 37.32700  8.93600   40.09400 1.000 69.95000 ? 236 MET B CE  1 
ATOM   5163 N  N   . LEU B 1 237 ? 38.12800  13.87500  36.49000 1.000 32.17000 ? 237 LEU B N   1 
ATOM   5164 C  CA  . LEU B 1 237 ? 38.43300  15.15700  37.12300 1.000 35.42000 ? 237 LEU B CA  1 
ATOM   5165 C  C   . LEU B 1 237 ? 37.60400  16.29100  36.54100 1.000 35.21000 ? 237 LEU B C   1 
ATOM   5166 O  O   . LEU B 1 237 ? 37.38600  17.30800  37.21200 1.000 32.16000 ? 237 LEU B O   1 
ATOM   5167 C  CB  . LEU B 1 237 ? 39.92100  15.49000  36.97900 1.000 35.80000 ? 237 LEU B CB  1 
ATOM   5168 C  CG  . LEU B 1 237 ? 40.92000  14.51000  37.59500 1.000 43.79000 ? 237 LEU B CG  1 
ATOM   5169 C  CD1 . LEU B 1 237 ? 42.29500  15.14800  37.68000 1.000 40.41000 ? 237 LEU B CD1 1 
ATOM   5170 C  CD2 . LEU B 1 237 ? 40.44000  14.02000  38.96700 1.000 41.64000 ? 237 LEU B CD2 1 
ATOM   5171 N  N   . MET B 1 238 ? 37.16200  16.15800  35.28900 1.000 28.64000 ? 238 MET B N   1 
ATOM   5172 C  CA  . MET B 1 238 ? 36.37000  17.22800  34.70100 1.000 25.46000 ? 238 MET B CA  1 
ATOM   5173 C  C   . MET B 1 238 ? 34.91200  17.14900  35.13100 1.000 26.63000 ? 238 MET B C   1 
ATOM   5174 O  O   . MET B 1 238 ? 34.28700  18.18400  35.37900 1.000 25.67000 ? 238 MET B O   1 
ATOM   5175 C  CB  . MET B 1 238 ? 36.47300  17.20200  33.17200 1.000 25.26000 ? 238 MET B CB  1 
ATOM   5176 C  CG  . MET B 1 238 ? 37.79200  17.74900  32.62700 1.000 28.04000 ? 238 MET B CG  1 
ATOM   5177 S  SD  . MET B 1 238 ? 37.94900  19.49900  33.02700 1.000 32.44000 ? 238 MET B SD  1 
ATOM   5178 C  CE  . MET B 1 238 ? 36.24700  20.00700  32.74400 1.000 26.54000 ? 238 MET B CE  1 
ATOM   5179 N  N   . LEU B 1 239 ? 34.35800  15.93700  35.22900 1.000 22.13000 ? 239 LEU B N   1 
ATOM   5180 C  CA  . LEU B 1 239 ? 32.92400  15.78000  35.47600 1.000 21.59000 ? 239 LEU B CA  1 
ATOM   5181 C  C   . LEU B 1 239 ? 32.57500  15.89100  36.95300 1.000 27.59000 ? 239 LEU B C   1 
ATOM   5182 O  O   . LEU B 1 239 ? 31.48500  16.37000  37.29600 1.000 24.07000 ? 239 LEU B O   1 
ATOM   5183 C  CB  . LEU B 1 239 ? 32.44200  14.41900  34.97300 1.000 26.09000 ? 239 LEU B CB  1 
ATOM   5184 C  CG  . LEU B 1 239 ? 31.78400  14.22700  33.61300 1.000 30.87000 ? 239 LEU B CG  1 
ATOM   5185 C  CD1 . LEU B 1 239 ? 31.29900  12.78800  33.53900 1.000 29.72000 ? 239 LEU B CD1 1 
ATOM   5186 C  CD2 . LEU B 1 239 ? 30.62800  15.19100  33.41900 1.000 25.63000 ? 239 LEU B CD2 1 
ATOM   5187 N  N   . THR B 1 240 ? 33.46800  15.41100  37.82700 1.000 23.81000 ? 240 THR B N   1 
ATOM   5188 C  CA  . THR B 1 240 ? 33.14500  15.25900  39.24600 1.000 23.13000 ? 240 THR B CA  1 
ATOM   5189 C  C   . THR B 1 240 ? 32.57000  16.50600  39.91100 1.000 22.69000 ? 240 THR B C   1 
ATOM   5190 O  O   . THR B 1 240 ? 31.59200  16.36400  40.67000 1.000 28.23000 ? 240 THR B O   1 
ATOM   5191 C  CB  . THR B 1 240 ? 34.38200  14.79100  40.02900 1.000 27.74000 ? 240 THR B CB  1 
ATOM   5192 O  OG1 . THR B 1 240 ? 34.78800  13.50300  39.55800 1.000 31.74000 ? 240 THR B OG1 1 
ATOM   5193 C  CG2 . THR B 1 240 ? 34.05000  14.69200  41.52400 1.000 21.94000 ? 240 THR B CG2 1 
ATOM   5194 N  N   . PRO B 1 241 ? 33.10100  17.71600  39.71200 1.000 20.76000 ? 241 PRO B N   1 
ATOM   5195 C  CA  . PRO B 1 241 ? 32.51300  18.89000  40.36900 1.000 17.50000 ? 241 PRO B CA  1 
ATOM   5196 C  C   . PRO B 1 241 ? 31.37600  19.56600  39.62000 1.000 24.17000 ? 241 PRO B C   1 
ATOM   5197 O  O   . PRO B 1 241 ? 30.88300  20.59000  40.10600 1.000 22.19000 ? 241 PRO B O   1 
ATOM   5198 C  CB  . PRO B 1 241 ? 33.71000  19.83700  40.46700 1.000 24.06000 ? 241 PRO B CB  1 
ATOM   5199 C  CG  . PRO B 1 241 ? 34.44900  19.57000  39.23600 1.000 25.77000 ? 241 PRO B CG  1 
ATOM   5200 C  CD  . PRO B 1 241 ? 34.32800  18.08400  38.98000 1.000 22.79000 ? 241 PRO B CD  1 
ATOM   5201 N  N   . LEU B 1 242 ? 30.92800  19.04600  38.47800 1.000 20.94000 ? 242 LEU B N   1 
ATOM   5202 C  CA  . LEU B 1 242 ? 29.98700  19.78300  37.64200 1.000 24.62000 ? 242 LEU B CA  1 
ATOM   5203 C  C   . LEU B 1 242 ? 28.57800  19.18700  37.64200 1.000 27.27000 ? 242 LEU B C   1 
ATOM   5204 O  O   . LEU B 1 242 ? 27.72500  19.65500  36.88100 1.000 23.47000 ? 242 LEU B O   1 
ATOM   5205 C  CB  . LEU B 1 242 ? 30.52400  19.88100  36.20800 1.000 22.20000 ? 242 LEU B CB  1 
ATOM   5206 C  CG  . LEU B 1 242 ? 31.90200  20.51700  35.94500 1.000 24.79000 ? 242 LEU B CG  1 
ATOM   5207 C  CD1 . LEU B 1 242 ? 32.28000  20.37300  34.46800 1.000 24.02000 ? 242 LEU B CD1 1 
ATOM   5208 C  CD2 . LEU B 1 242 ? 31.95100  21.97600  36.35400 1.000 23.60000 ? 242 LEU B CD2 1 
ATOM   5209 N  N   . ILE B 1 243 ? 28.30200  18.19000  38.48900 1.000 23.21000 ? 243 ILE B N   1 
ATOM   5210 C  CA  . ILE B 1 243 ? 27.02800  17.47300  38.44400 1.000 24.40000 ? 243 ILE B CA  1 
ATOM   5211 C  C   . ILE B 1 243 ? 26.33700  17.47500  39.80600 1.000 21.21000 ? 243 ILE B C   1 
ATOM   5212 O  O   . ILE B 1 243 ? 25.69600  16.48900  40.19400 1.000 20.97000 ? 243 ILE B O   1 
ATOM   5213 C  CB  . ILE B 1 243 ? 27.23400  16.03200  37.95000 1.000 28.51000 ? 243 ILE B CB  1 
ATOM   5214 C  CG1 . ILE B 1 243 ? 28.27000  15.31500  38.82200 1.000 24.95000 ? 243 ILE B CG1 1 
ATOM   5215 C  CG2 . ILE B 1 243 ? 27.69000  16.02900  36.48400 1.000 21.53000 ? 243 ILE B CG2 1 
ATOM   5216 C  CD1 . ILE B 1 243 ? 28.43600  13.84000  38.47200 1.000 22.89000 ? 243 ILE B CD1 1 
ATOM   5217 N  N   . SER B 1 244 ? 26.47400  18.57800  40.54600 1.000 18.85000 ? 244 SER B N   1 
ATOM   5218 C  CA  . SER B 1 244 ? 25.72200  18.80000  41.78200 1.000 17.90000 ? 244 SER B CA  1 
ATOM   5219 C  C   . SER B 1 244 ? 24.22700  18.94700  41.53200 1.000 17.43000 ? 244 SER B C   1 
ATOM   5220 O  O   . SER B 1 244 ? 23.43700  18.93700  42.48900 1.000 14.70000 ? 244 SER B O   1 
ATOM   5221 C  CB  . SER B 1 244 ? 26.25400  20.05200  42.48600 1.000 17.49000 ? 244 SER B CB  1 
ATOM   5222 O  OG  . SER B 1 244 ? 27.65700  19.95600  42.68000 1.000 20.50000 ? 244 SER B OG  1 
ATOM   5223 N  N   . THR B 1 245 ? 23.83800  19.10700  40.26900 1.000 13.96000 ? 245 THR B N   1 
ATOM   5224 C  CA  . THR B 1 245 ? 22.43600  19.11800  39.87300 1.000 13.22000 ? 245 THR B CA  1 
ATOM   5225 C  C   . THR B 1 245 ? 21.68800  17.89700  40.39300 1.000 15.63000 ? 245 THR B C   1 
ATOM   5226 O  O   . THR B 1 245 ? 20.50900  17.98800  40.74300 1.000 14.73000 ? 245 THR B O   1 
ATOM   5227 C  CB  . THR B 1 245 ? 22.35900  19.17300  38.34800 1.000 15.63000 ? 245 THR B CB  1 
ATOM   5228 O  OG1 . THR B 1 245 ? 23.03800  20.34700  37.87500 1.000 17.51000 ? 245 THR B OG1 1 
ATOM   5229 C  CG2 . THR B 1 245 ? 20.91700  19.18000  37.87100 1.000 14.70000 ? 245 THR B CG2 1 
ATOM   5230 N  N   . ILE B 1 246 ? 22.34600  16.73800  40.42100 1.000 13.95000 ? 246 ILE B N   1 
ATOM   5231 C  CA  . ILE B 1 246 ? 21.65900  15.51100  40.81600 1.000 15.87000 ? 246 ILE B CA  1 
ATOM   5232 C  C   . ILE B 1 246 ? 21.21900  15.59100  42.27600 1.000 16.53000 ? 246 ILE B C   1 
ATOM   5233 O  O   . ILE B 1 246 ? 20.03000  15.45700  42.59700 1.000 14.75000 ? 246 ILE B O   1 
ATOM   5234 C  CB  . ILE B 1 246 ? 22.55200  14.28400  40.56100 1.000 15.94000 ? 246 ILE B CB  1 
ATOM   5235 C  CG1 . ILE B 1 246 ? 22.92600  14.19700  39.07400 1.000 19.42000 ? 246 ILE B CG1 1 
ATOM   5236 C  CG2 . ILE B 1 246 ? 21.84500  13.01100  41.03100 1.000 13.05000 ? 246 ILE B CG2 1 
ATOM   5237 C  CD1 . ILE B 1 246 ? 23.98500  13.14100  38.75100 1.000 15.51000 ? 246 ILE B CD1 1 
ATOM   5238 N  N   . ALA B 1 247 ? 22.17700  15.78800  43.18700 1.000 13.73000 ? 247 ALA B N   1 
ATOM   5239 C  CA  . ALA B 1 247 ? 21.83100  15.79200  44.61100 1.000 13.19000 ? 247 ALA B CA  1 
ATOM   5240 C  C   . ALA B 1 247 ? 20.91300  16.95000  44.96600 1.000 13.36000 ? 247 ALA B C   1 
ATOM   5241 O  O   . ALA B 1 247 ? 20.05200  16.80400  45.83900 1.000 14.05000 ? 247 ALA B O   1 
ATOM   5242 C  CB  . ALA B 1 247 ? 23.09800  15.84200  45.46500 1.000 13.05000 ? 247 ALA B CB  1 
ATOM   5243 N  N   . ALA B 1 248 ? 21.06600  18.10100  44.29700 1.000 14.04000 ? 248 ALA B N   1 
ATOM   5244 C  CA  . ALA B 1 248 ? 20.18700  19.23400  44.56800 1.000 14.27000 ? 248 ALA B CA  1 
ATOM   5245 C  C   . ALA B 1 248 ? 18.75800  18.94000  44.13500 1.000 13.68000 ? 248 ALA B C   1 
ATOM   5246 O  O   . ALA B 1 248 ? 17.80800  19.28100  44.84800 1.000 16.00000 ? 248 ALA B O   1 
ATOM   5247 C  CB  . ALA B 1 248 ? 20.70200  20.48600  43.85800 1.000 16.44000 ? 248 ALA B CB  1 
ATOM   5248 N  N   . THR B 1 249 ? 18.59000  18.32800  42.95600 1.000 12.47000 ? 249 THR B N   1 
ATOM   5249 C  CA  . THR B 1 249 ? 17.26700  17.88300  42.51700 1.000 12.65000 ? 249 THR B CA  1 
ATOM   5250 C  C   . THR B 1 249 ? 16.67300  16.87700  43.49900 1.000 16.97000 ? 249 THR B C   1 
ATOM   5251 O  O   . THR B 1 249 ? 15.50100  16.98600  43.87600 1.000 14.81000 ? 249 THR B O   1 
ATOM   5252 C  CB  . THR B 1 249 ? 17.35800  17.28200  41.10800 1.000 15.38000 ? 249 THR B CB  1 
ATOM   5253 O  OG1 . THR B 1 249 ? 17.86000  18.27600  40.19600 1.000 15.68000 ? 249 THR B OG1 1 
ATOM   5254 C  CG2 . THR B 1 249 ? 15.98900  16.80300  40.63100 1.000 14.54000 ? 249 THR B CG2 1 
ATOM   5255 N  N   . ASP B 1 250 ? 17.46800  15.88400  43.92200 1.000 17.18000 ? 250 ASP B N   1 
ATOM   5256 C  CA  . ASP B 1 250 ? 16.99300  14.92400  44.92100 1.000 14.55000 ? 250 ASP B CA  1 
ATOM   5257 C  C   . ASP B 1 250 ? 16.48800  15.63000  46.17300 1.000 15.15000 ? 250 ASP B C   1 
ATOM   5258 O  O   . ASP B 1 250 ? 15.40600  15.31400  46.69000 1.000 14.65000 ? 250 ASP B O   1 
ATOM   5259 C  CB  . ASP B 1 250 ? 18.10100  13.93700  45.30200 1.000 15.29000 ? 250 ASP B CB  1 
ATOM   5260 C  CG  . ASP B 1 250 ? 18.54500  13.04900  44.14700 1.000 17.48000 ? 250 ASP B CG  1 
ATOM   5261 O  OD1 . ASP B 1 250 ? 17.79400  12.88200  43.16600 1.000 18.52000 ? 250 ASP B OD1 1 
ATOM   5262 O  OD2 . ASP B 1 250 ? 19.65700  12.49300  44.24800 1.000 15.06000 ? 250 ASP B OD2 1 
ATOM   5263 N  N   . MET B 1 251 ? 17.26400  16.58800  46.69100 1.000 17.18000 ? 251 MET B N   1 
ATOM   5264 C  CA  . MET B 1 251 ? 16.87100  17.25600  47.93000 1.000 13.16000 ? 251 MET B CA  1 
ATOM   5265 C  C   . MET B 1 251 ? 15.64300  18.13400  47.70800 1.000 18.14000 ? 251 MET B C   1 
ATOM   5266 O  O   . MET B 1 251 ? 14.68500  18.10300  48.49300 1.000 17.97000 ? 251 MET B O   1 
ATOM   5267 C  CB  . MET B 1 251 ? 18.05000  18.07200  48.47800 1.000 15.13000 ? 251 MET B CB  1 
ATOM   5268 C  CG  . MET B 1 251 ? 17.80800  18.74600  49.81500 1.000 22.28000 ? 251 MET B CG  1 
ATOM   5269 S  SD  . MET B 1 251 ? 17.47500  17.60200  51.18100 1.000 24.33000 ? 251 MET B SD  1 
ATOM   5270 C  CE  . MET B 1 251 ? 19.07700  16.85400  51.37500 1.000 20.12000 ? 251 MET B CE  1 
ATOM   5271 N  N   . MET B 1 252 ? 15.65300  18.91800  46.63300 1.000 16.33000 ? 252 MET B N   1 
ATOM   5272 C  CA  . MET B 1 252 ? 14.51200  19.76500  46.30700 1.000 16.38000 ? 252 MET B CA  1 
ATOM   5273 C  C   . MET B 1 252 ? 13.23600  18.93500  46.16400 1.000 18.32000 ? 252 MET B C   1 
ATOM   5274 O  O   . MET B 1 252 ? 12.22200  19.21000  46.82000 1.000 18.88000 ? 252 MET B O   1 
ATOM   5275 C  CB  . MET B 1 252 ? 14.83500  20.54900  45.02500 1.000 19.24000 ? 252 MET B CB  1 
ATOM   5276 C  CG  . MET B 1 252 ? 13.87300  21.66000  44.65300 1.000 26.18000 ? 252 MET B CG  1 
ATOM   5277 S  SD  . MET B 1 252 ? 13.90000  23.02700  45.81100 1.000 26.41000 ? 252 MET B SD  1 
ATOM   5278 C  CE  . MET B 1 252 ? 15.06600  24.20500  45.11800 1.000 15.77000 ? 252 MET B CE  1 
ATOM   5279 N  N   . LEU B 1 253 ? 13.27200  17.88900  45.34000 1.000 16.09000 ? 253 LEU B N   1 
ATOM   5280 C  CA  . LEU B 1 253 ? 12.05000  17.13900  45.06800 1.000 17.48000 ? 253 LEU B CA  1 
ATOM   5281 C  C   . LEU B 1 253 ? 11.67800  16.17700  46.18800 1.000 18.31000 ? 253 LEU B C   1 
ATOM   5282 O  O   . LEU B 1 253 ? 10.60900  15.56700  46.12300 1.000 16.72000 ? 253 LEU B O   1 
ATOM   5283 C  CB  . LEU B 1 253 ? 12.16400  16.34600  43.75500 1.000 18.70000 ? 253 LEU B CB  1 
ATOM   5284 C  CG  . LEU B 1 253 ? 12.53000  17.02100  42.43100 1.000 24.42000 ? 253 LEU B CG  1 
ATOM   5285 C  CD1 . LEU B 1 253 ? 11.92200  16.27200  41.24400 1.000 22.64000 ? 253 LEU B CD1 1 
ATOM   5286 C  CD2 . LEU B 1 253 ? 12.18700  18.48600  42.38900 1.000 18.92000 ? 253 LEU B CD2 1 
ATOM   5287 N  N   . SER B 1 254 ? 12.51600  16.03200  47.21500 1.000 16.19000 ? 254 SER B N   1 
ATOM   5288 C  CA  . SER B 1 254 ? 12.24000  15.06100  48.26500 1.000 16.33000 ? 254 SER B CA  1 
ATOM   5289 C  C   . SER B 1 254 ? 11.05400  15.46300  49.12600 1.000 19.97000 ? 254 SER B C   1 
ATOM   5290 O  O   . SER B 1 254 ? 10.48600  14.60600  49.81400 1.000 20.14000 ? 254 SER B O   1 
ATOM   5291 C  CB  . SER B 1 254 ? 13.46100  14.90500  49.16500 1.000 14.98000 ? 254 SER B CB  1 
ATOM   5292 O  OG  . SER B 1 254 ? 13.60400  16.07500  49.95700 1.000 17.57000 ? 254 SER B OG  1 
ATOM   5293 N  N   . GLY B 1 255 ? 10.68500  16.74400  49.12000 1.000 17.44000 ? 255 GLY B N   1 
ATOM   5294 C  CA  . GLY B 1 255 ? 9.70600   17.25900  50.04800 1.000 19.71000 ? 255 GLY B CA  1 
ATOM   5295 C  C   . GLY B 1 255 ? 10.27800  17.70400  51.37200 1.000 20.57000 ? 255 GLY B C   1 
ATOM   5296 O  O   . GLY B 1 255 ? 9.51800   18.16800  52.22500 1.000 21.24000 ? 255 GLY B O   1 
ATOM   5297 N  N   . ALA B 1 256 ? 11.59600  17.59500  51.56200 1.000 17.87000 ? 256 ALA B N   1 
ATOM   5298 C  CA  . ALA B 1 256 ? 12.20300  17.93500  52.84700 1.000 19.24000 ? 256 ALA B CA  1 
ATOM   5299 C  C   . ALA B 1 256 ? 11.92200  19.37800  53.23400 1.000 19.14000 ? 256 ALA B C   1 
ATOM   5300 O  O   . ALA B 1 256 ? 11.74000  19.68800  54.41500 1.000 20.01000 ? 256 ALA B O   1 
ATOM   5301 C  CB  . ALA B 1 256 ? 13.71400  17.69400  52.80200 1.000 17.84000 ? 256 ALA B CB  1 
ATOM   5302 N  N   . PHE B 1 257 ? 11.89800  20.28500  52.25900 1.000 20.82000 ? 257 PHE B N   1 
ATOM   5303 C  CA  . PHE B 1 257 ? 11.65600  21.67600  52.60900 1.000 18.23000 ? 257 PHE B CA  1 
ATOM   5304 C  C   . PHE B 1 257 ? 10.19200  21.93600  52.93000 1.000 21.92000 ? 257 PHE B C   1 
ATOM   5305 O  O   . PHE B 1 257 ? 9.88300   22.87500  53.66900 1.000 21.76000 ? 257 PHE B O   1 
ATOM   5306 C  CB  . PHE B 1 257 ? 12.17500  22.57400  51.48800 1.000 18.26000 ? 257 PHE B CB  1 
ATOM   5307 C  CG  . PHE B 1 257 ? 13.65000  22.39900  51.24600 1.000 14.22000 ? 257 PHE B CG  1 
ATOM   5308 C  CD1 . PHE B 1 257 ? 14.55800  22.71900  52.24000 1.000 15.42000 ? 257 PHE B CD1 1 
ATOM   5309 C  CD2 . PHE B 1 257 ? 14.11800  21.86600  50.06500 1.000 15.63000 ? 257 PHE B CD2 1 
ATOM   5310 C  CE1 . PHE B 1 257 ? 15.91600  22.53800  52.05300 1.000 14.17000 ? 257 PHE B CE1 1 
ATOM   5311 C  CE2 . PHE B 1 257 ? 15.48200  21.67600  49.86100 1.000 17.88000 ? 257 PHE B CE2 1 
ATOM   5312 C  CZ  . PHE B 1 257 ? 16.38000  22.01200  50.85900 1.000 17.45000 ? 257 PHE B CZ  1 
ATOM   5313 N  N   . LYS B 1 258 ? 9.28700   21.11400  52.41800 1.000 21.24000 ? 258 LYS B N   1 
ATOM   5314 C  CA  . LYS B 1 258 ? 7.90800   21.21600  52.86800 1.000 25.98000 ? 258 LYS B CA  1 
ATOM   5315 C  C   . LYS B 1 258 ? 7.78000   20.75700  54.31300 1.000 22.79000 ? 258 LYS B C   1 
ATOM   5316 O  O   . LYS B 1 258 ? 7.08500   21.39000  55.11000 1.000 24.07000 ? 258 LYS B O   1 
ATOM   5317 C  CB  . LYS B 1 258 ? 6.98900   20.41600  51.94000 1.000 26.60000 ? 258 LYS B CB  1 
ATOM   5318 C  CG  . LYS B 1 258 ? 5.53400   20.80900  52.06100 1.000 32.90000 ? 258 LYS B CG  1 
ATOM   5319 C  CD  . LYS B 1 258 ? 4.74000   20.52800  50.78500 1.000 28.48000 ? 258 LYS B CD  1 
ATOM   5320 C  CE  . LYS B 1 258 ? 4.46900   19.05100  50.60900 1.000 29.20000 ? 258 LYS B CE  1 
ATOM   5321 N  NZ  . LYS B 1 258 ? 3.42700   18.82900  49.56500 1.000 25.98000 ? 258 LYS B NZ  1 
ATOM   5322 N  N   . LYS B 1 259 ? 8.45900   19.67200  54.68000 1.000 21.19000 ? 259 LYS B N   1 
ATOM   5323 C  CA  A LYS B 1 259 ? 8.40800   19.20600  56.06300 0.505 20.79000 ? 259 LYS B CA  1 
ATOM   5324 C  CA  B LYS B 1 259 ? 8.41200   19.20500  56.05900 0.495 20.79000 ? 259 LYS B CA  1 
ATOM   5325 C  C   . LYS B 1 259 ? 9.29500   20.03400  56.98300 1.000 23.66000 ? 259 LYS B C   1 
ATOM   5326 O  O   . LYS B 1 259 ? 8.95300   20.21700  58.15800 1.000 20.80000 ? 259 LYS B O   1 
ATOM   5327 C  CB  A LYS B 1 259 ? 8.82400   17.73400  56.16600 0.505 21.16000 ? 259 LYS B CB  1 
ATOM   5328 C  CB  B LYS B 1 259 ? 8.82500   17.73700  56.11900 0.495 21.16000 ? 259 LYS B CB  1 
ATOM   5329 C  CG  A LYS B 1 259 ? 8.46700   16.85500  54.97400 0.505 23.51000 ? 259 LYS B CG  1 
ATOM   5330 C  CG  B LYS B 1 259 ? 8.44300   17.03200  57.39400 0.495 20.80000 ? 259 LYS B CG  1 
ATOM   5331 C  CD  A LYS B 1 259 ? 9.15800   15.49300  55.08000 0.505 20.27000 ? 259 LYS B CD  1 
ATOM   5332 C  CD  B LYS B 1 259 ? 8.61500   15.53800  57.24300 0.495 19.55000 ? 259 LYS B CD  1 
ATOM   5333 C  CE  A LYS B 1 259 ? 9.09900   14.70700  53.77200 0.505 17.89000 ? 259 LYS B CE  1 
ATOM   5334 C  CE  B LYS B 1 259 ? 8.15400   14.78400  58.48000 0.495 22.91000 ? 259 LYS B CE  1 
ATOM   5335 N  NZ  A LYS B 1 259 ? 9.69200   13.34500  53.93200 0.505 20.49000 ? 259 LYS B NZ  1 
ATOM   5336 N  NZ  B LYS B 1 259 ? 8.54100   13.34500  58.40300 0.495 18.84000 ? 259 LYS B NZ  1 
ATOM   5337 N  N   . PHE B 1 260 ? 10.43300  20.53400  56.48400 1.000 20.33000 ? 260 PHE B N   1 
ATOM   5338 C  CA  . PHE B 1 260 ? 11.40200  21.28300  57.29100 1.000 17.98000 ? 260 PHE B CA  1 
ATOM   5339 C  C   . PHE B 1 260 ? 11.73400  22.59800  56.59800 1.000 21.61000 ? 260 PHE B C   1 
ATOM   5340 O  O   . PHE B 1 260 ? 12.79300  22.74000  55.96700 1.000 16.63000 ? 260 PHE B O   1 
ATOM   5341 C  CB  . PHE B 1 260 ? 12.66400  20.45200  57.53500 1.000 17.19000 ? 260 PHE B CB  1 
ATOM   5342 C  CG  . PHE B 1 260 ? 12.38700  19.10900  58.16200 1.000 17.22000 ? 260 PHE B CG  1 
ATOM   5343 C  CD1 . PHE B 1 260 ? 12.10800  19.01300  59.51000 1.000 17.24000 ? 260 PHE B CD1 1 
ATOM   5344 C  CD2 . PHE B 1 260 ? 12.41000  17.95400  57.40400 1.000 16.80000 ? 260 PHE B CD2 1 
ATOM   5345 C  CE1 . PHE B 1 260 ? 11.85300  17.79100  60.08700 1.000 18.66000 ? 260 PHE B CE1 1 
ATOM   5346 C  CE2 . PHE B 1 260 ? 12.15600  16.71700  57.97900 1.000 17.64000 ? 260 PHE B CE2 1 
ATOM   5347 C  CZ  . PHE B 1 260 ? 11.87300  16.64200  59.32300 1.000 18.86000 ? 260 PHE B CZ  1 
ATOM   5348 N  N   . PRO B 1 261 ? 10.85900  23.59900  56.72100 1.000 20.08000 ? 261 PRO B N   1 
ATOM   5349 C  CA  . PRO B 1 261 ? 11.03400  24.83700  55.94200 1.000 17.09000 ? 261 PRO B CA  1 
ATOM   5350 C  C   . PRO B 1 261 ? 12.30900  25.60800  56.25400 1.000 16.48000 ? 261 PRO B C   1 
ATOM   5351 O  O   . PRO B 1 261 ? 12.71100  26.44100  55.44200 1.000 18.98000 ? 261 PRO B O   1 
ATOM   5352 C  CB  . PRO B 1 261 ? 9.79700   25.67400  56.31300 1.000 19.80000 ? 261 PRO B CB  1 
ATOM   5353 C  CG  . PRO B 1 261 ? 8.87100   24.74500  57.01800 1.000 25.64000 ? 261 PRO B CG  1 
ATOM   5354 C  CD  . PRO B 1 261 ? 9.67400   23.63400  57.59200 1.000 18.24000 ? 261 PRO B CD  1 
ATOM   5355 N  N   . ASP B 1 262 ? 12.94900  25.38800  57.40100 1.000 15.57000 ? 262 ASP B N   1 
ATOM   5356 C  CA  . ASP B 1 262 ? 14.15600  26.12400  57.73800 1.000 17.11000 ? 262 ASP B CA  1 
ATOM   5357 C  C   . ASP B 1 262 ? 15.43200  25.33200  57.47800 1.000 16.68000 ? 262 ASP B C   1 
ATOM   5358 O  O   . ASP B 1 262 ? 16.51500  25.81600  57.81200 1.000 15.03000 ? 262 ASP B O   1 
ATOM   5359 C  CB  . ASP B 1 262 ? 14.11800  26.57600  59.19700 1.000 17.74000 ? 262 ASP B CB  1 
ATOM   5360 C  CG  . ASP B 1 262 ? 13.05300  27.63900  59.45500 1.000 20.34000 ? 262 ASP B CG  1 
ATOM   5361 O  OD1 . ASP B 1 262 ? 12.72500  28.41000  58.53600 1.000 25.44000 ? 262 ASP B OD1 1 
ATOM   5362 O  OD2 . ASP B 1 262 ? 12.54500  27.70200  60.58200 1.000 23.33000 ? 262 ASP B OD2 1 
ATOM   5363 N  N   . LEU B 1 263 ? 15.32700  24.13700  56.89800 1.000 15.40000 ? 263 LEU B N   1 
ATOM   5364 C  CA  . LEU B 1 263 ? 16.49900  23.29700  56.67100 1.000 17.18000 ? 263 LEU B CA  1 
ATOM   5365 C  C   . LEU B 1 263 ? 17.46700  23.97900  55.71000 1.000 16.22000 ? 263 LEU B C   1 
ATOM   5366 O  O   . LEU B 1 263 ? 17.04900  24.59300  54.72200 1.000 16.45000 ? 263 LEU B O   1 
ATOM   5367 C  CB  . LEU B 1 263 ? 16.06500  21.94600  56.10800 1.000 17.75000 ? 263 LEU B CB  1 
ATOM   5368 C  CG  . LEU B 1 263 ? 17.13900  20.88900  55.84000 1.000 15.00000 ? 263 LEU B CG  1 
ATOM   5369 C  CD1 . LEU B 1 263 ? 17.71400  20.38800  57.15400 1.000 13.78000 ? 263 LEU B CD1 1 
ATOM   5370 C  CD2 . LEU B 1 263 ? 16.56600  19.73200  55.03100 1.000 18.04000 ? 263 LEU B CD2 1 
ATOM   5371 N  N   . LYS B 1 264 ? 18.76800  23.86300  55.99600 1.000 14.04000 ? 264 LYS B N   1 
ATOM   5372 C  CA  . LYS B 1 264 ? 19.81000  24.54000  55.22900 1.000 16.43000 ? 264 LYS B CA  1 
ATOM   5373 C  C   . LYS B 1 264 ? 20.73100  23.52100  54.56900 1.000 14.53000 ? 264 LYS B C   1 
ATOM   5374 O  O   . LYS B 1 264 ? 21.18300  22.57100  55.21800 1.000 14.94000 ? 264 LYS B O   1 
ATOM   5375 C  CB  . LYS B 1 264 ? 20.63700  25.46100  56.12700 1.000 17.10000 ? 264 LYS B CB  1 
ATOM   5376 C  CG  . LYS B 1 264 ? 19.99600  26.78300  56.43700 1.000 16.53000 ? 264 LYS B CG  1 
ATOM   5377 C  CD  . LYS B 1 264 ? 20.88000  27.56000  57.41100 1.000 21.04000 ? 264 LYS B CD  1 
ATOM   5378 C  CE  . LYS B 1 264 ? 20.64900  29.05600  57.28200 1.000 26.39000 ? 264 LYS B CE  1 
ATOM   5379 N  NZ  . LYS B 1 264 ? 19.24400  29.38000  57.62000 1.000 32.29000 ? 264 LYS B NZ  1 
ATOM   5380 N  N   . VAL B 1 265 ? 21.01900  23.73300  53.28900 1.000 12.17000 ? 265 VAL B N   1 
ATOM   5381 C  CA  . VAL B 1 265 ? 21.80500  22.81100  52.48500 1.000 12.46000 ? 265 VAL B CA  1 
ATOM   5382 C  C   . VAL B 1 265 ? 22.88800  23.61900  51.78600 1.000 12.44000 ? 265 VAL B C   1 
ATOM   5383 O  O   . VAL B 1 265 ? 22.57400  24.56200  51.05000 1.000 11.25000 ? 265 VAL B O   1 
ATOM   5384 C  CB  . VAL B 1 265 ? 20.93800  22.06400  51.45700 1.000 14.50000 ? 265 VAL B CB  1 
ATOM   5385 C  CG1 . VAL B 1 265 ? 21.82600  21.23400  50.53900 1.000 16.40000 ? 265 VAL B CG1 1 
ATOM   5386 C  CG2 . VAL B 1 265 ? 19.88200  21.16800  52.16600 1.000 12.66000 ? 265 VAL B CG2 1 
ATOM   5387 N  N   . ALA B 1 266 ? 24.15500  23.27300  52.03700 1.000 10.54000 ? 266 ALA B N   1 
ATOM   5388 C  CA  . ALA B 1 266 ? 25.28700  23.84300  51.31400 1.000 14.47000 ? 266 ALA B CA  1 
ATOM   5389 C  C   . ALA B 1 266 ? 25.82400  22.81100  50.32800 1.000 14.07000 ? 266 ALA B C   1 
ATOM   5390 O  O   . ALA B 1 266 ? 26.14300  21.68100  50.72100 1.000 13.47000 ? 266 ALA B O   1 
ATOM   5391 C  CB  . ALA B 1 266 ? 26.39100  24.27900  52.28200 1.000 11.65000 ? 266 ALA B CB  1 
ATOM   5392 N  N   . MET B 1 267 ? 25.93400  23.20000  49.05400 1.000 13.03000 ? 267 MET B N   1 
ATOM   5393 C  CA  . MET B 1 267 ? 26.38400  22.27700  48.00500 1.000 13.25000 ? 267 MET B CA  1 
ATOM   5394 C  C   . MET B 1 267 ? 27.89500  22.40100  47.85000 1.000 13.86000 ? 267 MET B C   1 
ATOM   5395 O  O   . MET B 1 267 ? 28.42000  22.94800  46.87600 1.000 13.68000 ? 267 MET B O   1 
ATOM   5396 C  CB  . MET B 1 267 ? 25.65600  22.54300  46.69500 1.000 13.60000 ? 267 MET B CB  1 
ATOM   5397 C  CG  . MET B 1 267 ? 24.14100  22.37300  46.77900 1.000 15.27000 ? 267 MET B CG  1 
ATOM   5398 S  SD  . MET B 1 267 ? 23.57900  20.78500  47.42000 1.000 15.55000 ? 267 MET B SD  1 
ATOM   5399 C  CE  . MET B 1 267 ? 24.27200  19.60300  46.26800 1.000 17.36000 ? 267 MET B CE  1 
ATOM   5400 N  N   . SER B 1 268 ? 28.60100  21.80300  48.80500 1.000 12.83000 ? 268 SER B N   1 
ATOM   5401 C  CA  . SER B 1 268 ? 30.02600  22.05800  48.97400 1.000 13.71000 ? 268 SER B CA  1 
ATOM   5402 C  C   . SER B 1 268 ? 30.81900  21.62100  47.74500 1.000 15.12000 ? 268 SER B C   1 
ATOM   5403 O  O   . SER B 1 268 ? 30.60600  20.53000  47.20500 1.000 13.14000 ? 268 SER B O   1 
ATOM   5404 C  CB  . SER B 1 268 ? 30.52400  21.34100  50.23000 1.000 13.12000 ? 268 SER B CB  1 
ATOM   5405 O  OG  . SER B 1 268 ? 29.59100  21.49200  51.29700 1.000 12.09000 ? 268 SER B OG  1 
ATOM   5406 N  N   . GLU B 1 269 ? 31.72200  22.50000  47.29600 1.000 12.13000 ? 269 GLU B N   1 
ATOM   5407 C  CA  . GLU B 1 269 ? 32.56800  22.30100  46.12000 1.000 15.29000 ? 269 GLU B CA  1 
ATOM   5408 C  C   . GLU B 1 269 ? 31.75500  22.09700  44.84800 1.000 17.48000 ? 269 GLU B C   1 
ATOM   5409 O  O   . GLU B 1 269 ? 32.28300  21.63300  43.84500 1.000 13.45000 ? 269 GLU B O   1 
ATOM   5410 C  CB  . GLU B 1 269 ? 33.56500  21.14000  46.30500 1.000 14.05000 ? 269 GLU B CB  1 
ATOM   5411 C  CG  . GLU B 1 269 ? 34.88600  21.39200  45.55500 1.000 15.50000 ? 269 GLU B CG  1 
ATOM   5412 C  CD  . GLU B 1 269 ? 35.99200  20.34400  45.77400 1.000 13.46000 ? 269 GLU B CD  1 
ATOM   5413 O  OE1 . GLU B 1 269 ? 36.18300  19.86900  46.91000 1.000 13.14000 ? 269 GLU B OE1 1 
ATOM   5414 O  OE2 . GLU B 1 269 ? 36.70300  20.00600  44.78800 1.000 17.43000 ? 269 GLU B OE2 1 
ATOM   5415 N  N   . GLY B 1 270 ? 30.48100  22.49000  44.84400 1.000 15.31000 ? 270 GLY B N   1 
ATOM   5416 C  CA  . GLY B 1 270 ? 29.66000  22.24500  43.67700 1.000 16.54000 ? 270 GLY B CA  1 
ATOM   5417 C  C   . GLY B 1 270 ? 29.73100  23.27100  42.56600 1.000 16.75000 ? 270 GLY B C   1 
ATOM   5418 O  O   . GLY B 1 270 ? 29.18700  23.01600  41.48600 1.000 18.37000 ? 270 GLY B O   1 
ATOM   5419 N  N   . GLY B 1 271 ? 30.39500  24.41300  42.78500 1.000 17.42000 ? 271 GLY B N   1 
ATOM   5420 C  CA  . GLY B 1 271 ? 30.41700  25.48600  41.80500 1.000 13.97000 ? 271 GLY B CA  1 
ATOM   5421 C  C   . GLY B 1 271 ? 29.12700  26.28900  41.81500 1.000 14.79000 ? 271 GLY B C   1 
ATOM   5422 O  O   . GLY B 1 271 ? 28.25000  26.08100  42.65900 1.000 14.87000 ? 271 GLY B O   1 
ATOM   5423 N  N   . VAL B 1 272 ? 28.99800  27.21400  40.85300 1.000 13.76000 ? 272 VAL B N   1 
ATOM   5424 C  CA  . VAL B 1 272 ? 27.85500  28.12400  40.80200 1.000 15.26000 ? 272 VAL B CA  1 
ATOM   5425 C  C   . VAL B 1 272 ? 27.00900  27.93400  39.54700 1.000 16.57000 ? 272 VAL B C   1 
ATOM   5426 O  O   . VAL B 1 272 ? 25.77300  27.99800  39.61300 1.000 14.02000 ? 272 VAL B O   1 
ATOM   5427 C  CB  . VAL B 1 272 ? 28.29800  29.59600  40.92500 1.000 16.07000 ? 272 VAL B CB  1 
ATOM   5428 C  CG1 . VAL B 1 272 ? 27.06800  30.51000  41.01600 1.000 16.97000 ? 272 VAL B CG1 1 
ATOM   5429 C  CG2 . VAL B 1 272 ? 29.19600  29.78700  42.13100 1.000 18.29000 ? 272 VAL B CG2 1 
ATOM   5430 N  N   . GLY B 1 273 ? 27.64300  27.74100  38.38600 1.000 13.86000 ? 273 GLY B N   1 
ATOM   5431 C  CA  . GLY B 1 273 ? 26.93000  27.82400  37.11800 1.000 15.40000 ? 273 GLY B CA  1 
ATOM   5432 C  C   . GLY B 1 273 ? 25.81600  26.80800  36.93300 1.000 14.93000 ? 273 GLY B C   1 
ATOM   5433 O  O   . GLY B 1 273 ? 24.90400  27.03700  36.12600 1.000 17.39000 ? 273 GLY B O   1 
ATOM   5434 N  N   . TRP B 1 274 ? 25.87100  25.68200  37.63900 1.000 13.55000 ? 274 TRP B N   1 
ATOM   5435 C  CA  . TRP B 1 274 ? 24.80800  24.69500  37.50300 1.000 13.10000 ? 274 TRP B CA  1 
ATOM   5436 C  C   . TRP B 1 274 ? 23.46800  25.20800  38.01800 1.000 15.07000 ? 274 TRP B C   1 
ATOM   5437 O  O   . TRP B 1 274 ? 22.42100  24.73000  37.56500 1.000 13.56000 ? 274 TRP B O   1 
ATOM   5438 C  CB  . TRP B 1 274 ? 25.19900  23.40800  38.23600 1.000 14.63000 ? 274 TRP B CB  1 
ATOM   5439 C  CG  . TRP B 1 274 ? 25.30200  23.56800  39.72400 1.000 15.20000 ? 274 TRP B CG  1 
ATOM   5440 C  CD1 . TRP B 1 274 ? 26.41200  23.91700  40.43900 1.000 14.34000 ? 274 TRP B CD1 1 
ATOM   5441 C  CD2 . TRP B 1 274 ? 24.25100  23.37700  40.67800 1.000 14.51000 ? 274 TRP B CD2 1 
ATOM   5442 N  NE1 . TRP B 1 274 ? 26.11200  23.95200  41.78800 1.000 14.87000 ? 274 TRP B NE1 1 
ATOM   5443 C  CE2 . TRP B 1 274 ? 24.79300  23.62600  41.95700 1.000 14.66000 ? 274 TRP B CE2 1 
ATOM   5444 C  CE3 . TRP B 1 274 ? 22.90200  23.01600  40.57500 1.000 13.19000 ? 274 TRP B CE3 1 
ATOM   5445 C  CZ2 . TRP B 1 274 ? 24.03200  23.53100  43.12300 1.000 11.95000 ? 274 TRP B CZ2 1 
ATOM   5446 C  CZ3 . TRP B 1 274 ? 22.14800  22.92700  41.72700 1.000 15.37000 ? 274 TRP B CZ3 1 
ATOM   5447 C  CH2 . TRP B 1 274 ? 22.71300  23.18400  42.98900 1.000 15.30000 ? 274 TRP B CH2 1 
ATOM   5448 N  N   . VAL B 1 275 ? 23.47300  26.19400  38.92000 1.000 12.76000 ? 275 VAL B N   1 
ATOM   5449 C  CA  . VAL B 1 275 ? 22.23800  26.57800  39.60700 1.000 12.69000 ? 275 VAL B CA  1 
ATOM   5450 C  C   . VAL B 1 275 ? 21.25000  27.23900  38.64800 1.000 16.58000 ? 275 VAL B C   1 
ATOM   5451 O  O   . VAL B 1 275 ? 20.07700  26.86000  38.59100 1.000 12.88000 ? 275 VAL B O   1 
ATOM   5452 C  CB  . VAL B 1 275 ? 22.55100  27.49600  40.79600 1.000 13.20000 ? 275 VAL B CB  1 
ATOM   5453 C  CG1 . VAL B 1 275 ? 21.24400  27.89800  41.50200 1.000 14.75000 ? 275 VAL B CG1 1 
ATOM   5454 C  CG2 . VAL B 1 275 ? 23.54000  26.80300  41.76300 1.000 11.96000 ? 275 VAL B CG2 1 
ATOM   5455 N  N   . ALA B 1 276 ? 21.69700  28.24600  37.89300 1.000 17.25000 ? 276 ALA B N   1 
ATOM   5456 C  CA  . ALA B 1 276 ? 20.75800  29.03400  37.09300 1.000 15.64000 ? 276 ALA B CA  1 
ATOM   5457 C  C   . ALA B 1 276 ? 19.93100  28.19900  36.12000 1.000 14.78000 ? 276 ALA B C   1 
ATOM   5458 O  O   . ALA B 1 276 ? 18.69800  28.35900  36.10900 1.000 15.82000 ? 276 ALA B O   1 
ATOM   5459 C  CB  . ALA B 1 276 ? 21.50600  30.15700  36.35900 1.000 16.72000 ? 276 ALA B CB  1 
ATOM   5460 N  N   . PRO B 1 277 ? 20.50400  27.33400  35.27400 1.000 13.98000 ? 277 PRO B N   1 
ATOM   5461 C  CA  . PRO B 1 277 ? 19.64500  26.55400  34.36800 1.000 13.14000 ? 277 PRO B CA  1 
ATOM   5462 C  C   . PRO B 1 277 ? 18.72200  25.61400  35.11100 1.000 19.38000 ? 277 PRO B C   1 
ATOM   5463 O  O   . PRO B 1 277 ? 17.61200  25.33000  34.64300 1.000 14.53000 ? 277 PRO B O   1 
ATOM   5464 C  CB  . PRO B 1 277 ? 20.64800  25.77500  33.50300 1.000 16.63000 ? 277 PRO B CB  1 
ATOM   5465 C  CG  . PRO B 1 277 ? 21.90800  25.72500  34.32300 1.000 17.21000 ? 277 PRO B CG  1 
ATOM   5466 C  CD  . PRO B 1 277 ? 21.93300  27.05600  35.03100 1.000 16.08000 ? 277 PRO B CD  1 
ATOM   5467 N  N   . TRP B 1 278 ? 19.16300  25.12900  36.26900 1.000 15.19000 ? 278 TRP B N   1 
ATOM   5468 C  CA  . TRP B 1 278 ? 18.35800  24.21400  37.06900 1.000 14.99000 ? 278 TRP B CA  1 
ATOM   5469 C  C   . TRP B 1 278 ? 17.16900  24.94200  37.68600 1.000 15.02000 ? 278 TRP B C   1 
ATOM   5470 O  O   . TRP B 1 278 ? 16.03400  24.44100  37.66700 1.000 13.28000 ? 278 TRP B O   1 
ATOM   5471 C  CB  . TRP B 1 278 ? 19.27300  23.59400  38.12200 1.000 12.71000 ? 278 TRP B CB  1 
ATOM   5472 C  CG  . TRP B 1 278 ? 18.67500  22.75900  39.21900 1.000 17.50000 ? 278 TRP B CG  1 
ATOM   5473 C  CD1 . TRP B 1 278 ? 18.19700  21.48800  39.12500 1.000 15.04000 ? 278 TRP B CD1 1 
ATOM   5474 C  CD2 . TRP B 1 278 ? 18.58600  23.12000  40.60100 1.000 16.89000 ? 278 TRP B CD2 1 
ATOM   5475 N  NE1 . TRP B 1 278 ? 17.80400  21.04000  40.35700 1.000 15.15000 ? 278 TRP B NE1 1 
ATOM   5476 C  CE2 . TRP B 1 278 ? 18.03100  22.02400  41.28300 1.000 16.96000 ? 278 TRP B CE2 1 
ATOM   5477 C  CE3 . TRP B 1 278 ? 18.91600  24.26900  41.32400 1.000 18.19000 ? 278 TRP B CE3 1 
ATOM   5478 C  CZ2 . TRP B 1 278 ? 17.78100  22.04600  42.65300 1.000 17.41000 ? 278 TRP B CZ2 1 
ATOM   5479 C  CZ3 . TRP B 1 278 ? 18.68500  24.28300  42.69000 1.000 16.32000 ? 278 TRP B CZ3 1 
ATOM   5480 C  CH2 . TRP B 1 278 ? 18.12100  23.18500  43.33600 1.000 16.30000 ? 278 TRP B CH2 1 
ATOM   5481 N  N   . LEU B 1 279 ? 17.40100  26.14600  38.20600 1.000 13.99000 ? 279 LEU B N   1 
ATOM   5482 C  CA  . LEU B 1 279 ? 16.29000  26.92900  38.74700 1.000 14.12000 ? 279 LEU B CA  1 
ATOM   5483 C  C   . LEU B 1 279 ? 15.29900  27.31200  37.65600 1.000 16.18000 ? 279 LEU B C   1 
ATOM   5484 O  O   . LEU B 1 279 ? 14.08400  27.30400  37.88800 1.000 16.21000 ? 279 LEU B O   1 
ATOM   5485 C  CB  . LEU B 1 279 ? 16.82600  28.17200  39.45500 1.000 15.57000 ? 279 LEU B CB  1 
ATOM   5486 C  CG  . LEU B 1 279 ? 17.42200  27.98300  40.85900 1.000 15.60000 ? 279 LEU B CG  1 
ATOM   5487 C  CD1 . LEU B 1 279 ? 17.76300  29.35000  41.42000 1.000 16.37000 ? 279 LEU B CD1 1 
ATOM   5488 C  CD2 . LEU B 1 279 ? 16.44100  27.25800  41.78300 1.000 13.60000 ? 279 LEU B CD2 1 
ATOM   5489 N  N   . ASP B 1 280 ? 15.79000  27.65600  36.46200 1.000 14.78000 ? 280 ASP B N   1 
ATOM   5490 C  CA  . ASP B 1 280 ? 14.87900  27.95800  35.36000 1.000 16.43000 ? 280 ASP B CA  1 
ATOM   5491 C  C   . ASP B 1 280 ? 13.96100  26.77600  35.07500 1.000 17.84000 ? 280 ASP B C   1 
ATOM   5492 O  O   . ASP B 1 280 ? 12.74100  26.94500  34.93900 1.000 15.75000 ? 280 ASP B O   1 
ATOM   5493 C  CB  . ASP B 1 280 ? 15.65400  28.34000  34.09500 1.000 13.93000 ? 280 ASP B CB  1 
ATOM   5494 C  CG  . ASP B 1 280 ? 16.20400  29.74900  34.14800 1.000 17.93000 ? 280 ASP B CG  1 
ATOM   5495 O  OD1 . ASP B 1 280 ? 15.97300  30.46100  35.15100 1.000 17.12000 ? 280 ASP B OD1 1 
ATOM   5496 O  OD2 . ASP B 1 280 ? 16.88000  30.15300  33.18100 1.000 15.00000 ? 280 ASP B OD2 1 
ATOM   5497 N  N   . ARG B 1 281 ? 14.52100  25.56700  35.03000 1.000 17.04000 ? 281 ARG B N   1 
ATOM   5498 C  CA  . ARG B 1 281 ? 13.70400  24.39400  34.74900 1.000 15.82000 ? 281 ARG B CA  1 
ATOM   5499 C  C   . ARG B 1 281 ? 12.77300  24.06400  35.91100 1.000 16.44000 ? 281 ARG B C   1 
ATOM   5500 O  O   . ARG B 1 281 ? 11.62300  23.67800  35.69200 1.000 14.76000 ? 281 ARG B O   1 
ATOM   5501 C  CB  . ARG B 1 281 ? 14.58900  23.19800  34.41100 1.000 17.22000 ? 281 ARG B CB  1 
ATOM   5502 C  CG  . ARG B 1 281 ? 13.76300  22.02600  33.89700 1.000 19.86000 ? 281 ARG B CG  1 
ATOM   5503 C  CD  . ARG B 1 281 ? 14.60000  20.95300  33.25200 1.000 22.83000 ? 281 ARG B CD  1 
ATOM   5504 N  NE  . ARG B 1 281 ? 13.72600  19.87400  32.80400 1.000 28.07000 ? 281 ARG B NE  1 
ATOM   5505 C  CZ  . ARG B 1 281 ? 12.98700  19.92300  31.69900 1.000 31.34000 ? 281 ARG B CZ  1 
ATOM   5506 N  NH1 . ARG B 1 281 ? 13.03100  20.99500  30.90300 1.000 24.08000 ? 281 ARG B NH1 1 
ATOM   5507 N  NH2 . ARG B 1 281 ? 12.22100  18.89000  31.37900 1.000 29.90000 ? 281 ARG B NH2 1 
ATOM   5508 N  N   . LEU B 1 282 ? 13.24700  24.19500  37.15400 1.000 14.57000 ? 282 LEU B N   1 
ATOM   5509 C  CA  . LEU B 1 282 ? 12.36700  23.94800  38.29400 1.000 16.03000 ? 282 LEU B CA  1 
ATOM   5510 C  C   . LEU B 1 282 ? 11.25600  24.98600  38.36400 1.000 18.29000 ? 282 LEU B C   1 
ATOM   5511 O  O   . LEU B 1 282 ? 10.09500  24.63500  38.61000 1.000 20.70000 ? 282 LEU B O   1 
ATOM   5512 C  CB  . LEU B 1 282 ? 13.15600  23.96200  39.60300 1.000 15.88000 ? 282 LEU B CB  1 
ATOM   5513 C  CG  . LEU B 1 282 ? 13.94800  22.73700  40.04200 1.000 22.27000 ? 282 LEU B CG  1 
ATOM   5514 C  CD1 . LEU B 1 282 ? 14.79700  23.11500  41.23200 1.000 23.42000 ? 282 LEU B CD1 1 
ATOM   5515 C  CD2 . LEU B 1 282 ? 13.00200  21.61200  40.40900 1.000 25.52000 ? 282 LEU B CD2 1 
ATOM   5516 N  N   . ASP B 1 283 ? 11.59400  26.27000  38.16400 1.000 16.13000 ? 283 ASP B N   1 
ATOM   5517 C  CA  . ASP B 1 283 ? 10.57500  27.32000  38.18400 1.000 16.22000 ? 283 ASP B CA  1 
ATOM   5518 C  C   . ASP B 1 283 ? 9.51500   27.05600  37.13300 1.000 21.31000 ? 283 ASP B C   1 
ATOM   5519 O  O   . ASP B 1 283 ? 8.31500   27.19800  37.40000 1.000 20.97000 ? 283 ASP B O   1 
ATOM   5520 C  CB  . ASP B 1 283 ? 11.19600  28.70800  37.95400 1.000 20.67000 ? 283 ASP B CB  1 
ATOM   5521 C  CG  . ASP B 1 283 ? 11.89400  29.26700  39.19500 1.000 20.43000 ? 283 ASP B CG  1 
ATOM   5522 O  OD1 . ASP B 1 283 ? 11.68000  28.72600  40.29200 1.000 24.60000 ? 283 ASP B OD1 1 
ATOM   5523 O  OD2 . ASP B 1 283 ? 12.66600  30.25400  39.07300 1.000 20.29000 ? 283 ASP B OD2 1 
ATOM   5524 N  N   . ARG B 1 284 ? 9.94400   26.65100  35.93500 1.000 20.60000 ? 284 ARG B N   1 
ATOM   5525 C  CA  A ARG B 1 284 ? 8.99800   26.36000  34.86000 0.454 21.51000 ? 284 ARG B CA  1 
ATOM   5526 C  CA  B ARG B 1 284 ? 8.99600   26.36500  34.86500 0.546 21.52000 ? 284 ARG B CA  1 
ATOM   5527 C  C   . ARG B 1 284 ? 8.13900   25.15200  35.19800 1.000 22.88000 ? 284 ARG B C   1 
ATOM   5528 O  O   . ARG B 1 284 ? 6.92100   25.16500  34.98900 1.000 23.44000 ? 284 ARG B O   1 
ATOM   5529 C  CB  A ARG B 1 284 ? 9.74000   26.12900  33.54100 0.454 20.21000 ? 284 ARG B CB  1 
ATOM   5530 C  CB  B ARG B 1 284 ? 9.74900   26.14700  33.55700 0.546 20.20000 ? 284 ARG B CB  1 
ATOM   5531 C  CG  A ARG B 1 284 ? 8.81600   25.83600  32.35100 0.454 23.71000 ? 284 ARG B CG  1 
ATOM   5532 C  CG  B ARG B 1 284 ? 8.89800   26.29800  32.31700 0.546 24.79000 ? 284 ARG B CG  1 
ATOM   5533 C  CD  A ARG B 1 284 ? 9.58300   25.43100  31.07800 0.454 22.87000 ? 284 ARG B CD  1 
ATOM   5534 C  CD  B ARG B 1 284 ? 9.77700   26.52500  31.09400 0.546 20.71000 ? 284 ARG B CD  1 
ATOM   5535 N  NE  A ARG B 1 284 ? 8.69900   25.36100  29.91000 0.454 22.41000 ? 284 ARG B NE  1 
ATOM   5536 N  NE  B ARG B 1 284 ? 10.53900  25.32600  30.75500 0.546 20.23000 ? 284 ARG B NE  1 
ATOM   5537 C  CZ  A ARG B 1 284 ? 8.95700   24.67400  28.79600 0.454 20.95000 ? 284 ARG B CZ  1 
ATOM   5538 C  CZ  B ARG B 1 284 ? 11.84000  25.17000  30.97900 0.546 21.18000 ? 284 ARG B CZ  1 
ATOM   5539 N  NH1 A ARG B 1 284 ? 10.08300  23.97900  28.67400 0.454 21.41000 ? 284 ARG B NH1 1 
ATOM   5540 N  NH1 B ARG B 1 284 ? 12.54500  26.14300  31.54200 0.546 19.92000 ? 284 ARG B NH1 1 
ATOM   5541 N  NH2 A ARG B 1 284 ? 8.08200   24.68200  27.79900 0.454 19.33000 ? 284 ARG B NH2 1 
ATOM   5542 N  NH2 B ARG B 1 284 ? 12.43800  24.04200  30.62900 0.546 16.82000 ? 284 ARG B NH2 1 
ATOM   5543 N  N   . HIS B 1 285 ? 8.76200   24.08700  35.71200 1.000 19.23000 ? 285 HIS B N   1 
ATOM   5544 C  CA  . HIS B 1 285 ? 8.00900   22.89400  36.08100 1.000 21.83000 ? 285 HIS B CA  1 
ATOM   5545 C  C   . HIS B 1 285 ? 6.90300   23.21500  37.08700 1.000 22.44000 ? 285 HIS B C   1 
ATOM   5546 O  O   . HIS B 1 285 ? 5.77100   22.73900  36.94900 1.000 20.21000 ? 285 HIS B O   1 
ATOM   5547 C  CB  . HIS B 1 285 ? 8.95100   21.84800  36.65800 1.000 20.38000 ? 285 HIS B CB  1 
ATOM   5548 C  CG  . HIS B 1 285 ? 8.27400   20.55500  36.97500 1.000 27.59000 ? 285 HIS B CG  1 
ATOM   5549 N  ND1 . HIS B 1 285 ? 7.94500   20.18400  38.26100 1.000 33.47000 ? 285 HIS B ND1 1 
ATOM   5550 C  CD2 . HIS B 1 285 ? 7.82800   19.56500  36.16900 1.000 25.97000 ? 285 HIS B CD2 1 
ATOM   5551 C  CE1 . HIS B 1 285 ? 7.34500   19.00800  38.23700 1.000 30.41000 ? 285 HIS B CE1 1 
ATOM   5552 N  NE2 . HIS B 1 285 ? 7.26600   18.60900  36.98100 1.000 35.73000 ? 285 HIS B NE2 1 
ATOM   5553 N  N   . ILE B 1 286 ? 7.21500   24.02500  38.10000 1.000 20.20000 ? 286 ILE B N   1 
ATOM   5554 C  CA  . ILE B 1 286 ? 6.24000   24.33800  39.14000 1.000 19.68000 ? 286 ILE B CA  1 
ATOM   5555 C  C   . ILE B 1 286 ? 5.11900   25.20500  38.58200 1.000 26.30000 ? 286 ILE B C   1 
ATOM   5556 O  O   . ILE B 1 286 ? 3.95600   25.08700  38.99300 1.000 25.09000 ? 286 ILE B O   1 
ATOM   5557 C  CB  . ILE B 1 286 ? 6.95100   25.00200  40.33100 1.000 22.14000 ? 286 ILE B CB  1 
ATOM   5558 C  CG1 . ILE B 1 286 ? 7.78300   23.95700  41.07500 1.000 21.34000 ? 286 ILE B CG1 1 
ATOM   5559 C  CG2 . ILE B 1 286 ? 5.95900   25.63300  41.28100 1.000 24.73000 ? 286 ILE B CG2 1 
ATOM   5560 C  CD1 . ILE B 1 286 ? 6.92600   22.88700  41.79200 1.000 25.14000 ? 286 ILE B CD1 1 
ATOM   5561 N  N   . VAL B 1 287 ? 5.43900   26.08500  37.63200 1.000 21.58000 ? 287 VAL B N   1 
ATOM   5562 C  CA  . VAL B 1 287 ? 4.38400   26.82900  36.94800 1.000 24.07000 ? 287 VAL B CA  1 
ATOM   5563 C  C   . VAL B 1 287 ? 3.51400   25.87700  36.14400 1.000 24.52000 ? 287 VAL B C   1 
ATOM   5564 O  O   . VAL B 1 287 ? 2.28300   25.87100  36.27500 1.000 26.29000 ? 287 VAL B O   1 
ATOM   5565 C  CB  . VAL B 1 287 ? 4.98500   27.93100  36.05700 1.000 21.79000 ? 287 VAL B CB  1 
ATOM   5566 C  CG1 . VAL B 1 287 ? 3.95800   28.42200  35.04600 1.000 23.94000 ? 287 VAL B CG1 1 
ATOM   5567 C  CG2 . VAL B 1 287 ? 5.49300   29.07200  36.91400 1.000 24.16000 ? 287 VAL B CG2 1 
ATOM   5568 N  N   . ASN B 1 288 ? 4.14200   25.03500  35.31900 1.000 22.05000 ? 288 ASN B N   1 
ATOM   5569 C  CA  . ASN B 1 288 ? 3.37300   24.17600  34.42700 1.000 23.60000 ? 288 ASN B CA  1 
ATOM   5570 C  C   . ASN B 1 288 ? 2.65500   23.04000  35.14900 1.000 22.77000 ? 288 ASN B C   1 
ATOM   5571 O  O   . ASN B 1 288 ? 1.71100   22.48100  34.58700 1.000 27.91000 ? 288 ASN B O   1 
ATOM   5572 C  CB  . ASN B 1 288 ? 4.27100   23.58600  33.34300 1.000 22.58000 ? 288 ASN B CB  1 
ATOM   5573 C  CG  . ASN B 1 288 ? 4.82200   24.64400  32.40600 1.000 26.01000 ? 288 ASN B CG  1 
ATOM   5574 O  OD1 . ASN B 1 288 ? 4.19200   25.67100  32.16700 1.000 27.84000 ? 288 ASN B OD1 1 
ATOM   5575 N  ND2 . ASN B 1 288 ? 6.00400   24.38900  31.86300 1.000 25.67000 ? 288 ASN B ND2 1 
ATOM   5576 N  N   . GLN B 1 289 ? 3.09000   22.65100  36.34700 1.000 23.46000 ? 289 GLN B N   1 
ATOM   5577 C  CA  . GLN B 1 289 ? 2.44900   21.56400  37.08000 1.000 24.23000 ? 289 GLN B CA  1 
ATOM   5578 C  C   . GLN B 1 289 ? 1.52500   22.06500  38.17700 1.000 23.42000 ? 289 GLN B C   1 
ATOM   5579 O  O   . GLN B 1 289 ? 1.08300   21.26600  39.01500 1.000 21.18000 ? 289 GLN B O   1 
ATOM   5580 C  CB  . GLN B 1 289 ? 3.49100   20.62900  37.69800 1.000 24.56000 ? 289 GLN B CB  1 
ATOM   5581 C  CG  . GLN B 1 289 ? 4.17400   19.70200  36.69000 1.000 25.67000 ? 289 GLN B CG  1 
ATOM   5582 C  CD  . GLN B 1 289 ? 3.20400   18.78800  35.97500 1.000 30.51000 ? 289 GLN B CD  1 
ATOM   5583 O  OE1 . GLN B 1 289 ? 2.61800   19.15800  34.95100 1.000 34.83000 ? 289 GLN B OE1 1 
ATOM   5584 N  NE2 . GLN B 1 289 ? 3.03200   17.58200  36.50400 1.000 30.71000 ? 289 GLN B NE2 1 
ATOM   5585 N  N   . SER B 1 290 ? 1.22600   23.36100  38.19300 1.000 20.58000 ? 290 SER B N   1 
ATOM   5586 C  CA  . SER B 1 290 ? 0.46400   23.90800  39.30200 1.000 23.64000 ? 290 SER B CA  1 
ATOM   5587 C  C   . SER B 1 290 ? -0.98400  23.44200  39.28100 1.000 22.95000 ? 290 SER B C   1 
ATOM   5588 O  O   . SER B 1 290 ? -1.66300  23.56200  40.30000 1.000 24.05000 ? 290 SER B O   1 
ATOM   5589 C  CB  . SER B 1 290 ? 0.53800   25.43500  39.29200 1.000 30.05000 ? 290 SER B CB  1 
ATOM   5590 O  OG  . SER B 1 290 ? -0.14500  25.96600  38.17400 1.000 36.48000 ? 290 SER B OG  1 
ATOM   5591 N  N   . TRP B 1 291 ? -1.45100  22.89900  38.15500 1.000 22.30000 ? 291 TRP B N   1 
ATOM   5592 C  CA  . TRP B 1 291 ? -2.78600  22.31100  38.07200 1.000 21.17000 ? 291 TRP B CA  1 
ATOM   5593 C  C   . TRP B 1 291 ? -2.95300  21.09900  38.97400 1.000 20.80000 ? 291 TRP B C   1 
ATOM   5594 O  O   . TRP B 1 291 ? -4.09200  20.74000  39.29900 1.000 22.14000 ? 291 TRP B O   1 
ATOM   5595 C  CB  . TRP B 1 291 ? -3.09500  21.89700  36.63500 1.000 20.54000 ? 291 TRP B CB  1 
ATOM   5596 C  CG  . TRP B 1 291 ? -2.13900  20.85600  36.10700 1.000 20.35000 ? 291 TRP B CG  1 
ATOM   5597 C  CD1 . TRP B 1 291 ? -0.92300  21.07700  35.51800 1.000 24.29000 ? 291 TRP B CD1 1 
ATOM   5598 C  CD2 . TRP B 1 291 ? -2.31900  19.43300  36.12400 1.000 19.28000 ? 291 TRP B CD2 1 
ATOM   5599 N  NE1 . TRP B 1 291 ? -0.33700  19.88000  35.17300 1.000 21.20000 ? 291 TRP B NE1 1 
ATOM   5600 C  CE2 . TRP B 1 291 ? -1.17500  18.85800  35.53100 1.000 19.22000 ? 291 TRP B CE2 1 
ATOM   5601 C  CE3 . TRP B 1 291 ? -3.33700  18.59100  36.58500 1.000 19.84000 ? 291 TRP B CE3 1 
ATOM   5602 C  CZ2 . TRP B 1 291 ? -1.02400  17.48600  35.38300 1.000 22.40000 ? 291 TRP B CZ2 1 
ATOM   5603 C  CZ3 . TRP B 1 291 ? -3.18200  17.22600  36.44200 1.000 19.56000 ? 291 TRP B CZ3 1 
ATOM   5604 C  CH2 . TRP B 1 291 ? -2.03400  16.68600  35.84500 1.000 17.51000 ? 291 TRP B CH2 1 
ATOM   5605 N  N   . THR B 1 292 ? -1.85600  20.45300  39.38100 1.000 18.89000 ? 292 THR B N   1 
ATOM   5606 C  CA  . THR B 1 292 ? -1.96700  19.26200  40.21300 1.000 19.26000 ? 292 THR B CA  1 
ATOM   5607 C  C   . THR B 1 292 ? -2.42100  19.57800  41.63000 1.000 18.92000 ? 292 THR B C   1 
ATOM   5608 O  O   . THR B 1 292 ? -2.87100  18.67100  42.33100 1.000 20.60000 ? 292 THR B O   1 
ATOM   5609 C  CB  . THR B 1 292 ? -0.63300  18.50700  40.29800 1.000 18.80000 ? 292 THR B CB  1 
ATOM   5610 O  OG1 . THR B 1 292 ? 0.32400   19.31500  40.99500 1.000 19.56000 ? 292 THR B OG1 1 
ATOM   5611 C  CG2 . THR B 1 292 ? -0.09500  18.15900  38.91800 1.000 19.64000 ? 292 THR B CG2 1 
ATOM   5612 N  N   . GLY B 1 293 ? -2.29000  20.82000  42.07800 1.000 20.69000 ? 293 GLY B N   1 
ATOM   5613 C  CA  . GLY B 1 293 ? -2.61300  21.13500  43.45600 1.000 20.63000 ? 293 GLY B CA  1 
ATOM   5614 C  C   . GLY B 1 293 ? -1.66800  20.54500  44.47800 1.000 28.45000 ? 293 GLY B C   1 
ATOM   5615 O  O   . GLY B 1 293 ? -2.01200  20.49200  45.66300 1.000 22.07000 ? 293 GLY B O   1 
ATOM   5616 N  N   . THR B 1 294 ? -0.49200  20.08300  44.04800 1.000 22.04000 ? 294 THR B N   1 
ATOM   5617 C  CA  . THR B 1 294 ? 0.53300   19.53800  44.92500 1.000 26.26000 ? 294 THR B CA  1 
ATOM   5618 C  C   . THR B 1 294 ? 1.85500   20.18800  44.57900 1.000 22.08000 ? 294 THR B C   1 
ATOM   5619 O  O   . THR B 1 294 ? 2.05100   20.67700  43.46800 1.000 25.26000 ? 294 THR B O   1 
ATOM   5620 C  CB  . THR B 1 294 ? 0.75100   18.02200  44.76500 1.000 25.99000 ? 294 THR B CB  1 
ATOM   5621 O  OG1 . THR B 1 294 ? 1.18400   17.75000  43.42400 1.000 38.65000 ? 294 THR B OG1 1 
ATOM   5622 C  CG2 . THR B 1 294 ? -0.46200  17.24600  45.04000 1.000 29.01000 ? 294 THR B CG2 1 
ATOM   5623 N  N   . SER B 1 295 ? 2.78500   20.12600  45.52300 1.000 22.69000 ? 295 SER B N   1 
ATOM   5624 C  CA  . SER B 1 295 ? 4.13300   20.61000  45.27500 1.000 24.49000 ? 295 SER B CA  1 
ATOM   5625 C  C   . SER B 1 295 ? 5.07300   19.96200  46.27800 1.000 20.38000 ? 295 SER B C   1 
ATOM   5626 O  O   . SER B 1 295 ? 4.67100   19.61300  47.39200 1.000 20.89000 ? 295 SER B O   1 
ATOM   5627 C  CB  . SER B 1 295 ? 4.19600   22.14000  45.37700 1.000 28.71000 ? 295 SER B CB  1 
ATOM   5628 O  OG  . SER B 1 295 ? 5.52600   22.59200  45.30600 1.000 26.64000 ? 295 SER B OG  1 
ATOM   5629 N  N   . PHE B 1 296 ? 6.32800   19.78400  45.86300 1.000 18.22000 ? 296 PHE B N   1 
ATOM   5630 C  CA  . PHE B 1 296 ? 7.35300   19.39500  46.81200 1.000 17.55000 ? 296 PHE B CA  1 
ATOM   5631 C  C   . PHE B 1 296 ? 7.83600   20.56800  47.64500 1.000 21.10000 ? 296 PHE B C   1 
ATOM   5632 O  O   . PHE B 1 296 ? 8.69100   20.37200  48.50900 1.000 20.53000 ? 296 PHE B O   1 
ATOM   5633 C  CB  . PHE B 1 296 ? 8.54200   18.74900  46.08900 1.000 18.03000 ? 296 PHE B CB  1 
ATOM   5634 C  CG  . PHE B 1 296 ? 8.93400   19.44400  44.81900 1.000 17.65000 ? 296 PHE B CG  1 
ATOM   5635 C  CD1 . PHE B 1 296 ? 9.76700   20.54800  44.84700 1.000 21.94000 ? 296 PHE B CD1 1 
ATOM   5636 C  CD2 . PHE B 1 296 ? 8.48100   18.98300  43.59100 1.000 21.70000 ? 296 PHE B CD2 1 
ATOM   5637 C  CE1 . PHE B 1 296 ? 10.13300  21.20800  43.67100 1.000 22.78000 ? 296 PHE B CE1 1 
ATOM   5638 C  CE2 . PHE B 1 296 ? 8.84300   19.63200  42.41000 1.000 22.79000 ? 296 PHE B CE2 1 
ATOM   5639 C  CZ  . PHE B 1 296 ? 9.67100   20.74600  42.45400 1.000 22.32000 ? 296 PHE B CZ  1 
ATOM   5640 N  N   . LEU B 1 297 ? 7.29200   21.76400  47.42900 1.000 18.97000 ? 297 LEU B N   1 
ATOM   5641 C  CA  . LEU B 1 297 ? 7.72100   22.96400  48.12300 1.000 23.99000 ? 297 LEU B CA  1 
ATOM   5642 C  C   . LEU B 1 297 ? 6.64800   23.49400  49.06900 1.000 23.70000 ? 297 LEU B C   1 
ATOM   5643 O  O   . LEU B 1 297 ? 5.45800   23.20600  48.90700 1.000 21.26000 ? 297 LEU B O   1 
ATOM   5644 C  CB  . LEU B 1 297 ? 8.08000   24.05800  47.11200 1.000 23.44000 ? 297 LEU B CB  1 
ATOM   5645 C  CG  . LEU B 1 297 ? 9.21900   23.71800  46.13900 1.000 25.81000 ? 297 LEU B CG  1 
ATOM   5646 C  CD1 . LEU B 1 297 ? 9.60500   24.93800  45.35000 1.000 21.68000 ? 297 LEU B CD1 1 
ATOM   5647 C  CD2 . LEU B 1 297 ? 10.42800  23.15300  46.87400 1.000 27.69000 ? 297 LEU B CD2 1 
ATOM   5648 N  N   . PRO B 1 298 ? 7.03800   24.30200  50.05500 1.000 25.35000 ? 298 PRO B N   1 
ATOM   5649 C  CA  . PRO B 1 298 ? 6.04400   24.96200  50.91300 1.000 24.71000 ? 298 PRO B CA  1 
ATOM   5650 C  C   . PRO B 1 298 ? 5.07500   25.80000  50.09500 1.000 24.98000 ? 298 PRO B C   1 
ATOM   5651 O  O   . PRO B 1 298 ? 5.39800   26.27100  49.00500 1.000 24.69000 ? 298 PRO B O   1 
ATOM   5652 C  CB  . PRO B 1 298 ? 6.89900   25.84600  51.82800 1.000 18.60000 ? 298 PRO B CB  1 
ATOM   5653 C  CG  . PRO B 1 298 ? 8.23600   25.22600  51.82300 1.000 25.51000 ? 298 PRO B CG  1 
ATOM   5654 C  CD  . PRO B 1 298 ? 8.41900   24.62100  50.46100 1.000 26.11000 ? 298 PRO B CD  1 
ATOM   5655 N  N   . LYS B 1 299 ? 3.87600   25.99600  50.63600 1.000 21.57000 ? 299 LYS B N   1 
ATOM   5656 C  CA  . LYS B 1 299 ? 2.86800   26.78400  49.93200 1.000 27.66000 ? 299 LYS B CA  1 
ATOM   5657 C  C   . LYS B 1 299 ? 3.35900   28.20300  49.69200 1.000 23.24000 ? 299 LYS B C   1 
ATOM   5658 O  O   . LYS B 1 299 ? 3.97400   28.82100  50.56000 1.000 24.09000 ? 299 LYS B O   1 
ATOM   5659 C  CB  . LYS B 1 299 ? 1.55900   26.82500  50.72600 1.000 32.49000 ? 299 LYS B CB  1 
ATOM   5660 C  CG  . LYS B 1 299 ? 0.63800   25.64300  50.44900 1.000 35.37000 ? 299 LYS B CG  1 
ATOM   5661 C  CD  . LYS B 1 299 ? -0.56300  26.03800  49.60700 1.000 27.08000 ? 299 LYS B CD  1 
ATOM   5662 C  CE  . LYS B 1 299 ? -0.99600  24.85500  48.75900 1.000 34.15000 ? 299 LYS B CE  1 
ATOM   5663 N  NZ  . LYS B 1 299 ? -2.42900  24.85700  48.40400 1.000 28.54000 ? 299 LYS B NZ  1 
ATOM   5664 N  N   . GLY B 1 300 ? 3.08900   28.71900  48.49900 1.000 22.79000 ? 300 GLY B N   1 
ATOM   5665 C  CA  . GLY B 1 300 ? 3.43900   30.08600  48.19300 1.000 24.39000 ? 300 GLY B CA  1 
ATOM   5666 C  C   . GLY B 1 300 ? 4.90400   30.32500  47.92700 1.000 26.37000 ? 300 GLY B C   1 
ATOM   5667 O  O   . GLY B 1 300 ? 5.33500   31.48300  47.94100 1.000 28.14000 ? 300 GLY B O   1 
ATOM   5668 N  N   . MET B 1 301 ? 5.68700   29.27400  47.69900 1.000 23.37000 ? 301 MET B N   1 
ATOM   5669 C  CA  A MET B 1 301 ? 7.11300   29.40400  47.45400 0.519 22.45000 ? 301 MET B CA  1 
ATOM   5670 C  CA  B MET B 1 301 ? 7.12300   29.38000  47.47200 0.481 22.44000 ? 301 MET B CA  1 
ATOM   5671 C  C   . MET B 1 301 ? 7.47000   28.82100  46.09900 1.000 20.28000 ? 301 MET B C   1 
ATOM   5672 O  O   . MET B 1 301 ? 7.01900   27.73100  45.74400 1.000 23.22000 ? 301 MET B O   1 
ATOM   5673 C  CB  A MET B 1 301 ? 7.92300   28.70600  48.53500 0.519 20.71000 ? 301 MET B CB  1 
ATOM   5674 C  CB  B MET B 1 301 ? 7.91400   28.62500  48.55100 0.481 20.70000 ? 301 MET B CB  1 
ATOM   5675 C  CG  A MET B 1 301 ? 7.84700   29.39500  49.86900 0.519 21.35000 ? 301 MET B CG  1 
ATOM   5676 C  CG  B MET B 1 301 ? 7.75000   29.18300  49.95700 0.481 21.34000 ? 301 MET B CG  1 
ATOM   5677 S  SD  A MET B 1 301 ? 9.12300   28.74800  50.93200 0.519 18.47000 ? 301 MET B SD  1 
ATOM   5678 S  SD  B MET B 1 301 ? 8.83100   30.58500  50.28500 0.481 19.33000 ? 301 MET B SD  1 
ATOM   5679 C  CE  A MET B 1 301 ? 10.54800  29.71600  50.42800 0.519 19.02000 ? 301 MET B CE  1 
ATOM   5680 C  CE  B MET B 1 301 ? 10.42200  29.78500  50.49800 0.481 19.04000 ? 301 MET B CE  1 
ATOM   5681 N  N   . THR B 1 302 ? 8.28900   29.57500  45.32700 1.000 19.35000 ? 302 THR B N   1 
ATOM   5682 C  CA  . THR B 1 302 ? 8.82800   29.04000  44.08900 1.000 17.72000 ? 302 THR B CA  1 
ATOM   5683 C  C   . THR B 1 302 ? 10.15700  28.35900  44.36900 1.000 20.85000 ? 302 THR B C   1 
ATOM   5684 O  O   . THR B 1 302 ? 10.75000  28.55400  45.44400 1.000 17.36000 ? 302 THR B O   1 
ATOM   5685 C  CB  . THR B 1 302 ? 9.04800   30.16000  43.08100 1.000 20.30000 ? 302 THR B CB  1 
ATOM   5686 O  OG1 . THR B 1 302 ? 10.09000  31.00600  43.57200 1.000 18.39000 ? 302 THR B OG1 1 
ATOM   5687 C  CG2 . THR B 1 302 ? 7.80300   30.97200  42.91200 1.000 21.04000 ? 302 THR B CG2 1 
ATOM   5688 N  N   . PRO B 1 303 ? 10.65900  27.54800  43.42600 1.000 18.00000 ? 303 PRO B N   1 
ATOM   5689 C  CA  . PRO B 1 303 ? 12.00400  26.98600  43.61300 1.000 19.78000 ? 303 PRO B CA  1 
ATOM   5690 C  C   . PRO B 1 303 ? 13.05500  28.05500  43.88200 1.000 15.86000 ? 303 PRO B C   1 
ATOM   5691 O  O   . PRO B 1 303 ? 13.91400  27.86000  44.75300 1.000 17.62000 ? 303 PRO B O   1 
ATOM   5692 C  CB  . PRO B 1 303 ? 12.24000  26.21900  42.29900 1.000 17.70000 ? 303 PRO B CB  1 
ATOM   5693 C  CG  . PRO B 1 303 ? 10.86700  25.81100  41.86400 1.000 20.40000 ? 303 PRO B CG  1 
ATOM   5694 C  CD  . PRO B 1 303 ? 9.97100   26.95100  42.25900 1.000 16.54000 ? 303 PRO B CD  1 
ATOM   5695 N  N   . THR B 1 304 ? 12.98600  29.20000  43.19500 1.000 18.35000 ? 304 THR B N   1 
ATOM   5696 C  CA  . THR B 1 304 ? 13.92300  30.28500  43.47900 1.000 17.57000 ? 304 THR B CA  1 
ATOM   5697 C  C   . THR B 1 304 ? 13.76700  30.79700  44.90900 1.000 15.51000 ? 304 THR B C   1 
ATOM   5698 O  O   . THR B 1 304 ? 14.76400  31.13800  45.55400 1.000 15.77000 ? 304 THR B O   1 
ATOM   5699 C  CB  . THR B 1 304 ? 13.75600  31.42600  42.46900 1.000 18.99000 ? 304 THR B CB  1 
ATOM   5700 O  OG1 . THR B 1 304 ? 14.14600  30.95900  41.17300 1.000 17.62000 ? 304 THR B OG1 1 
ATOM   5701 C  CG2 . THR B 1 304 ? 14.64400  32.61800  42.84700 1.000 14.72000 ? 304 THR B CG2 1 
ATOM   5702 N  N   . ASP B 1 305 ? 12.53100  30.84200  45.43700 1.000 14.01000 ? 305 ASP B N   1 
ATOM   5703 C  CA  . ASP B 1 305 ? 12.35800  31.25700  46.83000 1.000 16.83000 ? 305 ASP B CA  1 
ATOM   5704 C  C   . ASP B 1 305 ? 13.06400  30.29300  47.77200 1.000 15.41000 ? 305 ASP B C   1 
ATOM   5705 O  O   . ASP B 1 305 ? 13.68600  30.70900  48.76000 1.000 14.01000 ? 305 ASP B O   1 
ATOM   5706 C  CB  . ASP B 1 305 ? 10.87200  31.32100  47.21700 1.000 14.21000 ? 305 ASP B CB  1 
ATOM   5707 C  CG  . ASP B 1 305 ? 10.11500  32.46000  46.55400 1.000 22.81000 ? 305 ASP B CG  1 
ATOM   5708 O  OD1 . ASP B 1 305 ? 10.71100  33.52100  46.26400 1.000 22.57000 ? 305 ASP B OD1 1 
ATOM   5709 O  OD2 . ASP B 1 305 ? 8.89200   32.29300  46.35700 1.000 18.83000 ? 305 ASP B OD2 1 
ATOM   5710 N  N   . VAL B 1 306 ? 12.94800  28.99400  47.49900 1.000 14.93000 ? 306 VAL B N   1 
ATOM   5711 C  CA  . VAL B 1 306 ? 13.55400  28.00100  48.38100 1.000 15.98000 ? 306 VAL B CA  1 
ATOM   5712 C  C   . VAL B 1 306 ? 15.07000  28.01400  48.22100 1.000 15.87000 ? 306 VAL B C   1 
ATOM   5713 O  O   . VAL B 1 306 ? 15.81300  27.85400  49.20000 1.000 12.69000 ? 306 VAL B O   1 
ATOM   5714 C  CB  . VAL B 1 306 ? 12.93300  26.61200  48.12000 1.000 16.23000 ? 306 VAL B CB  1 
ATOM   5715 C  CG1 . VAL B 1 306 ? 13.80700  25.48500  48.67200 1.000 13.65000 ? 306 VAL B CG1 1 
ATOM   5716 C  CG2 . VAL B 1 306 ? 11.54900  26.53000  48.75900 1.000 16.20000 ? 306 VAL B CG2 1 
ATOM   5717 N  N   . TRP B 1 307 ? 15.55800  28.22200  46.99100 1.000 16.21000 ? 307 TRP B N   1 
ATOM   5718 C  CA  . TRP B 1 307 ? 16.99000  28.42400  46.80000 1.000 14.78000 ? 307 TRP B CA  1 
ATOM   5719 C  C   . TRP B 1 307 ? 17.50600  29.52300  47.72500 1.000 14.94000 ? 307 TRP B C   1 
ATOM   5720 O  O   . TRP B 1 307 ? 18.49900  29.33900  48.43600 1.000 13.68000 ? 307 TRP B O   1 
ATOM   5721 C  CB  . TRP B 1 307 ? 17.31000  28.77900  45.33800 1.000 14.36000 ? 307 TRP B CB  1 
ATOM   5722 C  CG  . TRP B 1 307 ? 18.76100  29.11900  45.21400 1.000 13.96000 ? 307 TRP B CG  1 
ATOM   5723 C  CD1 . TRP B 1 307 ? 19.31500  30.37000  45.15500 1.000 13.08000 ? 307 TRP B CD1 1 
ATOM   5724 C  CD2 . TRP B 1 307 ? 19.85100  28.19400  45.17900 1.000 12.52000 ? 307 TRP B CD2 1 
ATOM   5725 N  NE1 . TRP B 1 307 ? 20.67700  30.27400  45.08600 1.000 14.52000 ? 307 TRP B NE1 1 
ATOM   5726 C  CE2 . TRP B 1 307 ? 21.03500  28.94800  45.10500 1.000 15.16000 ? 307 TRP B CE2 1 
ATOM   5727 C  CE3 . TRP B 1 307 ? 19.93800  26.79800  45.19600 1.000 12.81000 ? 307 TRP B CE3 1 
ATOM   5728 C  CZ2 . TRP B 1 307 ? 22.29700  28.35500  45.05200 1.000 15.33000 ? 307 TRP B CZ2 1 
ATOM   5729 C  CZ3 . TRP B 1 307 ? 21.20100  26.20700  45.16200 1.000 12.10000 ? 307 TRP B CZ3 1 
ATOM   5730 C  CH2 . TRP B 1 307 ? 22.35800  26.98500  45.08800 1.000 12.29000 ? 307 TRP B CH2 1 
ATOM   5731 N  N   . ARG B 1 308 ? 16.83200  30.67600  47.72400 1.000 13.10000 ? 308 ARG B N   1 
ATOM   5732 C  CA  . ARG B 1 308 ? 17.32400  31.85000  48.43200 1.000 16.71000 ? 308 ARG B CA  1 
ATOM   5733 C  C   . ARG B 1 308 ? 17.26100  31.67800  49.94100 1.000 18.61000 ? 308 ARG B C   1 
ATOM   5734 O  O   . ARG B 1 308 ? 18.14400  32.17100  50.64800 1.000 17.07000 ? 308 ARG B O   1 
ATOM   5735 C  CB  . ARG B 1 308 ? 16.53700  33.09500  47.99200 1.000 18.04000 ? 308 ARG B CB  1 
ATOM   5736 C  CG  . ARG B 1 308 ? 16.98200  33.55700  46.60600 1.000 15.17000 ? 308 ARG B CG  1 
ATOM   5737 C  CD  . ARG B 1 308 ? 16.19500  34.72100  46.00700 1.000 18.90000 ? 308 ARG B CD  1 
ATOM   5738 N  NE  . ARG B 1 308 ? 16.67900  34.98600  44.64800 1.000 19.21000 ? 308 ARG B NE  1 
ATOM   5739 C  CZ  . ARG B 1 308 ? 16.11600  35.83300  43.79300 1.000 23.74000 ? 308 ARG B CZ  1 
ATOM   5740 N  NH1 . ARG B 1 308 ? 15.03800  36.51900  44.14800 1.000 21.29000 ? 308 ARG B NH1 1 
ATOM   5741 N  NH2 . ARG B 1 308 ? 16.63300  35.99600  42.57800 1.000 17.71000 ? 308 ARG B NH2 1 
ATOM   5742 N  N   . LYS B 1 309 ? 16.24700  30.98200  50.45000 1.000 19.15000 ? 309 LYS B N   1 
ATOM   5743 C  CA  . LYS B 1 309 ? 16.13500  30.77100  51.88700 1.000 16.05000 ? 309 LYS B CA  1 
ATOM   5744 C  C   . LYS B 1 309 ? 16.92900  29.56700  52.38200 1.000 16.41000 ? 309 LYS B C   1 
ATOM   5745 O  O   . LYS B 1 309 ? 17.43200  29.59500  53.51100 1.000 15.97000 ? 309 LYS B O   1 
ATOM   5746 C  CB  . LYS B 1 309 ? 14.66200  30.59200  52.27800 1.000 17.36000 ? 309 LYS B CB  1 
ATOM   5747 C  CG  . LYS B 1 309 ? 14.44000  30.37200  53.78300 1.000 18.34000 ? 309 LYS B CG  1 
ATOM   5748 C  CD  . LYS B 1 309 ? 13.01200  29.93500  54.07800 1.000 21.95000 ? 309 LYS B CD  1 
ATOM   5749 C  CE  . LYS B 1 309 ? 12.74400  29.90300  55.59100 1.000 26.04000 ? 309 LYS B CE  1 
ATOM   5750 N  NZ  . LYS B 1 309 ? 11.27800  29.76200  55.86300 1.000 27.05000 ? 309 LYS B NZ  1 
ATOM   5751 N  N   . ASN B 1 310 ? 17.06300  28.50800  51.56900 1.000 14.29000 ? 310 ASN B N   1 
ATOM   5752 C  CA  . ASN B 1 310 ? 17.50600  27.21100  52.07500 1.000 12.81000 ? 310 ASN B CA  1 
ATOM   5753 C  C   . ASN B 1 310 ? 18.82300  26.69100  51.51000 1.000 14.81000 ? 310 ASN B C   1 
ATOM   5754 O  O   . ASN B 1 310 ? 19.32100  25.67800  52.01400 1.000 13.63000 ? 310 ASN B O   1 
ATOM   5755 C  CB  . ASN B 1 310 ? 16.43800  26.14000  51.82100 1.000 12.51000 ? 310 ASN B CB  1 
ATOM   5756 C  CG  . ASN B 1 310 ? 15.11900  26.45300  52.51900 1.000 19.61000 ? 310 ASN B CG  1 
ATOM   5757 O  OD1 . ASN B 1 310 ? 14.20500  26.99300  51.90900 1.000 15.70000 ? 310 ASN B OD1 1 
ATOM   5758 N  ND2 . ASN B 1 310 ? 15.03000  26.12600  53.80500 1.000 15.48000 ? 310 ASN B ND2 1 
ATOM   5759 N  N   . PHE B 1 311 ? 19.41000  27.33500  50.50700 1.000 12.73000 ? 311 PHE B N   1 
ATOM   5760 C  CA  . PHE B 1 311 ? 20.57500  26.76700  49.84000 1.000 12.30000 ? 311 PHE B CA  1 
ATOM   5761 C  C   . PHE B 1 311 ? 21.73800  27.74900  49.83300 1.000 14.32000 ? 311 PHE B C   1 
ATOM   5762 O  O   . PHE B 1 311 ? 21.55400  28.96600  49.90500 1.000 14.29000 ? 311 PHE B O   1 
ATOM   5763 C  CB  . PHE B 1 311 ? 20.26200  26.40300  48.38800 1.000 14.27000 ? 311 PHE B CB  1 
ATOM   5764 C  CG  . PHE B 1 311 ? 19.59000  25.06600  48.20800 1.000 13.66000 ? 311 PHE B CG  1 
ATOM   5765 C  CD1 . PHE B 1 311 ? 18.20800  24.95300  48.29200 1.000 16.72000 ? 311 PHE B CD1 1 
ATOM   5766 C  CD2 . PHE B 1 311 ? 20.34000  23.93800  47.89500 1.000 13.55000 ? 311 PHE B CD2 1 
ATOM   5767 C  CE1 . PHE B 1 311 ? 17.58100  23.72200  48.09600 1.000 15.87000 ? 311 PHE B CE1 1 
ATOM   5768 C  CE2 . PHE B 1 311 ? 19.72400  22.70200  47.69900 1.000 17.32000 ? 311 PHE B CE2 1 
ATOM   5769 C  CZ  . PHE B 1 311 ? 18.33900  22.59900  47.81000 1.000 18.56000 ? 311 PHE B CZ  1 
ATOM   5770 N  N   . LEU B 1 312 ? 22.94000  27.19600  49.66200 1.000 13.08000 ? 312 LEU B N   1 
ATOM   5771 C  CA  . LEU B 1 312 ? 24.15300  27.97900  49.45900 1.000 13.35000 ? 312 LEU B CA  1 
ATOM   5772 C  C   . LEU B 1 312 ? 24.99400  27.30700  48.38700 1.000 16.17000 ? 312 LEU B C   1 
ATOM   5773 O  O   . LEU B 1 312 ? 25.34000  26.12800  48.51300 1.000 12.92000 ? 312 LEU B O   1 
ATOM   5774 C  CB  . LEU B 1 312 ? 24.95300  28.10900  50.75900 1.000 13.24000 ? 312 LEU B CB  1 
ATOM   5775 C  CG  . LEU B 1 312 ? 26.14300  29.06700  50.73800 1.000 16.44000 ? 312 LEU B CG  1 
ATOM   5776 C  CD1 . LEU B 1 312 ? 25.64800  30.51300  50.78100 1.000 15.27000 ? 312 LEU B CD1 1 
ATOM   5777 C  CD2 . LEU B 1 312 ? 27.05500  28.77000  51.91800 1.000 15.62000 ? 312 LEU B CD2 1 
ATOM   5778 N  N   . ALA B 1 313 ? 25.32000  28.04600  47.32900 1.000 12.99000 ? 313 ALA B N   1 
ATOM   5779 C  CA  . ALA B 1 313 ? 26.24200  27.53900  46.32300 1.000 13.20000 ? 313 ALA B CA  1 
ATOM   5780 C  C   . ALA B 1 313 ? 27.66400  27.89100  46.75000 1.000 15.17000 ? 313 ALA B C   1 
ATOM   5781 O  O   . ALA B 1 313 ? 27.90200  28.95800  47.32000 1.000 15.20000 ? 313 ALA B O   1 
ATOM   5782 C  CB  . ALA B 1 313 ? 25.90700  28.12300  44.95100 1.000 12.34000 ? 313 ALA B CB  1 
ATOM   5783 N  N   . CYS B 1 314 ? 28.59600  26.96700  46.51400 1.000 12.28000 ? 314 CYS B N   1 
ATOM   5784 C  CA  . CYS B 1 314 ? 29.94900  27.04100  47.05600 1.000 15.17000 ? 314 CYS B CA  1 
ATOM   5785 C  C   . CYS B 1 314 ? 30.95200  26.83900  45.92800 1.000 14.48000 ? 314 CYS B C   1 
ATOM   5786 O  O   . CYS B 1 314 ? 30.85600  25.85000  45.20300 1.000 15.13000 ? 314 CYS B O   1 
ATOM   5787 C  CB  . CYS B 1 314 ? 30.15200  25.96800  48.14500 1.000 14.05000 ? 314 CYS B CB  1 
ATOM   5788 S  SG  . CYS B 1 314 ? 28.81500  25.93100  49.42200 1.000 16.28000 ? 314 CYS B SG  1 
ATOM   5789 N  N   . TYR B 1 315 ? 31.93200  27.73900  45.79700 1.000 14.32000 ? 315 TYR B N   1 
ATOM   5790 C  CA  . TYR B 1 315 ? 32.86900  27.62600  44.68200 1.000 12.95000 ? 315 TYR B CA  1 
ATOM   5791 C  C   . TYR B 1 315 ? 34.24200  28.17600  45.02600 1.000 14.82000 ? 315 TYR B C   1 
ATOM   5792 O  O   . TYR B 1 315 ? 34.37600  29.08000  45.85500 1.000 15.13000 ? 315 TYR B O   1 
ATOM   5793 C  CB  . TYR B 1 315 ? 32.34800  28.34300  43.43200 1.000 13.59000 ? 315 TYR B CB  1 
ATOM   5794 C  CG  . TYR B 1 315 ? 32.60500  29.84300  43.35400 1.000 17.33000 ? 315 TYR B CG  1 
ATOM   5795 C  CD1 . TYR B 1 315 ? 31.87200  30.73700  44.12500 1.000 13.72000 ? 315 TYR B CD1 1 
ATOM   5796 C  CD2 . TYR B 1 315 ? 33.53900  30.36600  42.46000 1.000 15.38000 ? 315 TYR B CD2 1 
ATOM   5797 C  CE1 . TYR B 1 315 ? 32.07400  32.10300  44.02700 1.000 15.93000 ? 315 TYR B CE1 1 
ATOM   5798 C  CE2 . TYR B 1 315 ? 33.74600  31.73800  42.35500 1.000 14.51000 ? 315 TYR B CE2 1 
ATOM   5799 C  CZ  . TYR B 1 315 ? 33.01500  32.59900  43.14000 1.000 16.68000 ? 315 TYR B CZ  1 
ATOM   5800 O  OH  . TYR B 1 315 ? 33.20000  33.96000  43.04200 1.000 13.02000 ? 315 TYR B OH  1 
ATOM   5801 N  N   . ILE B 1 316 ? 35.26300  27.62400  44.35000 1.000 14.03000 ? 316 ILE B N   1 
ATOM   5802 C  CA  . ILE B 1 316 ? 36.65700  28.02700  44.51300 1.000 12.22000 ? 316 ILE B CA  1 
ATOM   5803 C  C   . ILE B 1 316 ? 36.99100  29.11100  43.49900 1.000 14.66000 ? 316 ILE B C   1 
ATOM   5804 O  O   . ILE B 1 316 ? 37.36800  30.23400  43.85300 1.000 15.55000 ? 316 ILE B O   1 
ATOM   5805 C  CB  . ILE B 1 316 ? 37.62200  26.84600  44.32000 1.000 11.62000 ? 316 ILE B CB  1 
ATOM   5806 C  CG1 . ILE B 1 316 ? 37.23100  25.63500  45.15200 1.000 14.16000 ? 316 ILE B CG1 1 
ATOM   5807 C  CG2 . ILE B 1 316 ? 39.08500  27.27800  44.62600 1.000 12.84000 ? 316 ILE B CG2 1 
ATOM   5808 C  CD1 . ILE B 1 316 ? 37.84300  24.37400  44.58600 1.000 16.41000 ? 316 ILE B CD1 1 
ATOM   5809 N  N   . THR B 1 317 ? 36.88200  28.76100  42.22300 1.000 13.41000 ? 317 THR B N   1 
ATOM   5810 C  CA  . THR B 1 317 ? 37.13000  29.68600  41.13200 1.000 14.00000 ? 317 THR B CA  1 
ATOM   5811 C  C   . THR B 1 317 ? 36.16400  29.34100  40.01200 1.000 15.26000 ? 317 THR B C   1 
ATOM   5812 O  O   . THR B 1 317 ? 35.95700  28.16300  39.70500 1.000 17.82000 ? 317 THR B O   1 
ATOM   5813 C  CB  . THR B 1 317 ? 38.59100  29.62000  40.64400 1.000 15.55000 ? 317 THR B CB  1 
ATOM   5814 O  OG1 . THR B 1 317 ? 38.72800  30.40800  39.45200 1.000 16.78000 ? 317 THR B OG1 1 
ATOM   5815 C  CG2 . THR B 1 317 ? 39.00200  28.19700  40.33100 1.000 17.72000 ? 317 THR B CG2 1 
ATOM   5816 N  N   . GLU B 1 318 ? 35.54600  30.35800  39.44100 1.000 16.66000 ? 318 GLU B N   1 
ATOM   5817 C  CA  . GLU B 1 318 ? 34.59600  30.18100  38.35500 1.000 16.70000 ? 318 GLU B CA  1 
ATOM   5818 C  C   . GLU B 1 318 ? 34.33900  31.55600  37.75200 1.000 17.11000 ? 318 GLU B C   1 
ATOM   5819 O  O   . GLU B 1 318 ? 33.35900  32.22000  38.10800 1.000 18.41000 ? 318 GLU B O   1 
ATOM   5820 C  CB  . GLU B 1 318 ? 33.30000  29.53200  38.86100 1.000 13.84000 ? 318 GLU B CB  1 
ATOM   5821 C  CG  . GLU B 1 318 ? 32.42800  28.97600  37.74200 1.000 16.38000 ? 318 GLU B CG  1 
ATOM   5822 C  CD  . GLU B 1 318 ? 31.15100  28.35200  38.24500 1.000 14.57000 ? 318 GLU B CD  1 
ATOM   5823 O  OE1 . GLU B 1 318 ? 31.21600  27.62800  39.25800 1.000 17.00000 ? 318 GLU B OE1 1 
ATOM   5824 O  OE2 . GLU B 1 318 ? 30.08600  28.58100  37.62100 1.000 16.02000 ? 318 GLU B OE2 1 
ATOM   5825 N  N   . PRO B 1 319 ? 35.23400  32.03400  36.88400 1.000 17.22000 ? 319 PRO B N   1 
ATOM   5826 C  CA  . PRO B 1 319 ? 35.14400  33.42600  36.40900 1.000 19.00000 ? 319 PRO B CA  1 
ATOM   5827 C  C   . PRO B 1 319 ? 33.79100  33.82100  35.85300 1.000 19.31000 ? 319 PRO B C   1 
ATOM   5828 O  O   . PRO B 1 319 ? 33.42200  35.00000  35.93500 1.000 22.79000 ? 319 PRO B O   1 
ATOM   5829 C  CB  . PRO B 1 319 ? 36.22100  33.48200  35.31700 1.000 17.66000 ? 319 PRO B CB  1 
ATOM   5830 C  CG  . PRO B 1 319 ? 37.23100  32.47700  35.73500 1.000 19.22000 ? 319 PRO B CG  1 
ATOM   5831 C  CD  . PRO B 1 319 ? 36.42600  31.34500  36.35500 1.000 18.78000 ? 319 PRO B CD  1 
ATOM   5832 N  N   . SER B 1 320 ? 33.03700  32.89100  35.27700 1.000 16.89000 ? 320 SER B N   1 
ATOM   5833 C  CA  . SER B 1 320 ? 31.75200  33.24900  34.69000 1.000 17.91000 ? 320 SER B CA  1 
ATOM   5834 C  C   . SER B 1 320 ? 30.58900  33.02300  35.63900 1.000 17.60000 ? 320 SER B C   1 
ATOM   5835 O  O   . SER B 1 320 ? 29.45500  33.37400  35.29900 1.000 20.15000 ? 320 SER B O   1 
ATOM   5836 C  CB  . SER B 1 320 ? 31.51600  32.46100  33.39900 1.000 17.32000 ? 320 SER B CB  1 
ATOM   5837 O  OG  . SER B 1 320 ? 31.29900  31.09200  33.66900 1.000 15.73000 ? 320 SER B OG  1 
ATOM   5838 N  N   . GLY B 1 321 ? 30.84600  32.45600  36.82000 1.000 16.12000 ? 321 GLY B N   1 
ATOM   5839 C  CA  . GLY B 1 321 ? 29.75600  32.05100  37.69300 1.000 17.07000 ? 321 GLY B CA  1 
ATOM   5840 C  C   . GLY B 1 321 ? 28.93100  33.21400  38.21000 1.000 20.34000 ? 321 GLY B C   1 
ATOM   5841 O  O   . GLY B 1 321 ? 27.73200  33.06800  38.44600 1.000 23.84000 ? 321 GLY B O   1 
ATOM   5842 N  N   . LEU B 1 322 ? 29.54300  34.38300  38.37300 1.000 19.28000 ? 322 LEU B N   1 
ATOM   5843 C  CA  . LEU B 1 322 ? 28.81200  35.50300  38.96000 1.000 18.47000 ? 322 LEU B CA  1 
ATOM   5844 C  C   . LEU B 1 322 ? 27.96900  36.26800  37.94900 1.000 20.12000 ? 322 LEU B C   1 
ATOM   5845 O  O   . LEU B 1 322 ? 27.32600  37.25500  38.32300 1.000 18.35000 ? 322 LEU B O   1 
ATOM   5846 C  CB  . LEU B 1 322 ? 29.78500  36.45700  39.65900 1.000 16.53000 ? 322 LEU B CB  1 
ATOM   5847 C  CG  . LEU B 1 322 ? 30.59000  35.77000  40.76400 1.000 18.55000 ? 322 LEU B CG  1 
ATOM   5848 C  CD1 . LEU B 1 322 ? 31.52700  36.75100  41.43800 1.000 17.18000 ? 322 LEU B CD1 1 
ATOM   5849 C  CD2 . LEU B 1 322 ? 29.66400  35.10500  41.79200 1.000 17.68000 ? 322 LEU B CD2 1 
ATOM   5850 N  N   . ASN B 1 323 ? 27.94400  35.84200  36.69000 1.000 17.87000 ? 323 ASN B N   1 
ATOM   5851 C  CA  . ASN B 1 323 ? 27.10900  36.48600  35.69100 1.000 22.76000 ? 323 ASN B CA  1 
ATOM   5852 C  C   . ASN B 1 323 ? 25.62900  36.14600  35.84200 1.000 20.78000 ? 323 ASN B C   1 
ATOM   5853 O  O   . ASN B 1 323 ? 24.80300  36.73100  35.14000 1.000 19.35000 ? 323 ASN B O   1 
ATOM   5854 C  CB  . ASN B 1 323 ? 27.61000  36.11600  34.28800 1.000 22.17000 ? 323 ASN B CB  1 
ATOM   5855 C  CG  . ASN B 1 323 ? 28.98500  36.70600  33.98500 1.000 24.06000 ? 323 ASN B CG  1 
ATOM   5856 O  OD1 . ASN B 1 323 ? 29.39300  37.70500  34.57900 1.000 25.13000 ? 323 ASN B OD1 1 
ATOM   5857 N  ND2 . ASN B 1 323 ? 29.70200  36.08900  33.05000 1.000 24.09000 ? 323 ASN B ND2 1 
ATOM   5858 N  N   . ASN B 1 324 ? 25.26500  35.22900  36.73800 1.000 17.73000 ? 324 ASN B N   1 
ATOM   5859 C  CA  . ASN B 1 324 ? 23.86900  35.01600  37.09300 1.000 18.07000 ? 324 ASN B CA  1 
ATOM   5860 C  C   . ASN B 1 324 ? 23.65400  35.19200  38.59200 1.000 18.12000 ? 324 ASN B C   1 
ATOM   5861 O  O   . ASN B 1 324 ? 22.74800  34.59500  39.17500 1.000 20.04000 ? 324 ASN B O   1 
ATOM   5862 C  CB  . ASN B 1 324 ? 23.38400  33.64200  36.62500 1.000 19.76000 ? 324 ASN B CB  1 
ATOM   5863 C  CG  . ASN B 1 324 ? 22.61000  33.71200  35.30300 1.000 18.16000 ? 324 ASN B CG  1 
ATOM   5864 O  OD1 . ASN B 1 324 ? 21.81400  34.63400  35.07000 1.000 22.23000 ? 324 ASN B OD1 1 
ATOM   5865 N  ND2 . ASN B 1 324 ? 22.84900  32.74700  34.43800 1.000 18.56000 ? 324 ASN B ND2 1 
ATOM   5866 N  N   . ARG B 1 325 ? 24.47700  36.02300  39.23400 1.000 17.42000 ? 325 ARG B N   1 
ATOM   5867 C  CA  . ARG B 1 325 ? 24.34900  36.17900  40.68100 1.000 16.44000 ? 325 ARG B CA  1 
ATOM   5868 C  C   . ARG B 1 325 ? 23.03100  36.83600  41.05700 1.000 19.25000 ? 325 ARG B C   1 
ATOM   5869 O  O   . ARG B 1 325 ? 22.46400  36.53600  42.11400 1.000 17.23000 ? 325 ARG B O   1 
ATOM   5870 C  CB  . ARG B 1 325 ? 25.52600  36.97800  41.24100 1.000 16.29000 ? 325 ARG B CB  1 
ATOM   5871 C  CG  . ARG B 1 325 ? 25.63900  38.42500  40.74900 1.000 16.82000 ? 325 ARG B CG  1 
ATOM   5872 C  CD  . ARG B 1 325 ? 26.86000  39.04300  41.39100 1.000 19.60000 ? 325 ARG B CD  1 
ATOM   5873 N  NE  . ARG B 1 325 ? 27.09200  40.45900  41.09500 1.000 19.98000 ? 325 ARG B NE  1 
ATOM   5874 C  CZ  . ARG B 1 325 ? 27.79500  40.90000  40.05900 1.000 17.83000 ? 325 ARG B CZ  1 
ATOM   5875 N  NH1 . ARG B 1 325 ? 28.29600  40.04200  39.17400 1.000 19.20000 ? 325 ARG B NH1 1 
ATOM   5876 N  NH2 . ARG B 1 325 ? 28.00700  42.20000  39.90400 1.000 23.08000 ? 325 ARG B NH2 1 
ATOM   5877 N  N   . HIS B 1 326 ? 22.51000  37.70900  40.20400 1.000 19.45000 ? 326 HIS B N   1 
ATOM   5878 C  CA  . HIS B 1 326 ? 21.24300  38.34100  40.52500 1.000 19.35000 ? 326 HIS B CA  1 
ATOM   5879 C  C   . HIS B 1 326 ? 20.07500  37.38900  40.32300 1.000 19.73000 ? 326 HIS B C   1 
ATOM   5880 O  O   . HIS B 1 326 ? 19.10100  37.44600  41.07600 1.000 21.44000 ? 326 HIS B O   1 
ATOM   5881 C  CB  . HIS B 1 326 ? 21.08400  39.60800  39.69600 1.000 19.49000 ? 326 HIS B CB  1 
ATOM   5882 C  CG  . HIS B 1 326 ? 22.13000  40.63900  39.99400 1.000 30.15000 ? 326 HIS B CG  1 
ATOM   5883 N  ND1 . HIS B 1 326 ? 22.44100  41.02800  41.28100 1.000 33.24000 ? 326 HIS B ND1 1 
ATOM   5884 C  CD2 . HIS B 1 326 ? 22.93800  41.35700  39.18000 1.000 30.60000 ? 326 HIS B CD2 1 
ATOM   5885 C  CE1 . HIS B 1 326 ? 23.39400  41.94200  41.24500 1.000 27.35000 ? 326 HIS B CE1 1 
ATOM   5886 N  NE2 . HIS B 1 326 ? 23.71100  42.16200  39.98300 1.000 27.59000 ? 326 HIS B NE2 1 
ATOM   5887 N  N   . ARG B 1 327 ? 19.99500  36.52600  39.31800 1.000 19.00000 ? 327 ARG B N   1 
ATOM   5888 C  CA  . ARG B 1 327 ? 19.15600  35.34300  39.15600 1.000 18.38000 ? 327 ARG B CA  1 
ATOM   5889 C  C   . ARG B 1 327 ? 19.10700  34.51000  40.43500 1.000 17.16000 ? 327 ARG B C   1 
ATOM   5890 O  O   . ARG B 1 327 ? 18.06600  33.92200  40.75400 1.000 22.09000 ? 327 ARG B O   1 
ATOM   5891 C  CB  . ARG B 1 327 ? 19.65200  34.50900  37.98000 1.000 21.44000 ? 327 ARG B CB  1 
ATOM   5892 C  CG  . ARG B 1 327 ? 18.87300  33.21400  37.78600 1.000 26.89000 ? 327 ARG B CG  1 
ATOM   5893 C  CD  . ARG B 1 327 ? 17.42800  33.50900  37.43300 1.000 30.58000 ? 327 ARG B CD  1 
ATOM   5894 N  NE  . ARG B 1 327 ? 16.66500  32.28200  37.24200 1.000 28.92000 ? 327 ARG B NE  1 
ATOM   5895 C  CZ  . ARG B 1 327 ? 16.07800  31.61500  38.22800 1.000 24.14000 ? 327 ARG B CZ  1 
ATOM   5896 N  NH1 . ARG B 1 327 ? 16.15100  32.07200  39.47200 1.000 17.79000 ? 327 ARG B NH1 1 
ATOM   5897 N  NH2 . ARG B 1 327 ? 15.41000  30.49800  37.96500 1.000 20.51000 ? 327 ARG B NH2 1 
ATOM   5898 N  N   . LEU B 1 328 ? 20.25100  34.15500  40.88800 1.000 17.96000 ? 328 LEU B N   1 
ATOM   5899 C  CA  . LEU B 1 328 ? 20.28900  33.29600  42.07300 1.000 14.35000 ? 328 LEU B CA  1 
ATOM   5900 C  C   . LEU B 1 328 ? 19.88800  34.06900  43.31900 1.000 16.74000 ? 328 LEU B C   1 
ATOM   5901 O  O   . LEU B 1 328 ? 19.16600  33.54900  44.17900 1.000 17.16000 ? 328 LEU B O   1 
ATOM   5902 C  CB  . LEU B 1 328 ? 21.69700  32.71300  42.26500 1.000 14.63000 ? 328 LEU B CB  1 
ATOM   5903 C  CG  . LEU B 1 328 ? 22.02200  31.36300  41.63500 1.000 16.51000 ? 328 LEU B CG  1 
ATOM   5904 C  CD1 . LEU B 1 328 ? 21.81900  31.38400  40.12200 1.000 17.46000 ? 328 LEU B CD1 1 
ATOM   5905 C  CD2 . LEU B 1 328 ? 23.46900  30.94400  41.97500 1.000 16.41000 ? 328 LEU B CD2 1 
ATOM   5906 N  N   . GLY B 1 329 ? 20.32700  35.32700  43.40900 1.000 19.41000 ? 329 GLY B N   1 
ATOM   5907 C  CA  . GLY B 1 329 ? 20.37700  36.06800  44.65400 1.000 17.20000 ? 329 GLY B CA  1 
ATOM   5908 C  C   . GLY B 1 329 ? 21.80500  36.05000  45.16200 1.000 19.96000 ? 329 GLY B C   1 
ATOM   5909 O  O   . GLY B 1 329 ? 22.33300  34.98200  45.50400 1.000 15.06000 ? 329 GLY B O   1 
ATOM   5910 N  N   . VAL B 1 330 ? 22.46100  37.21400  45.20000 1.000 17.90000 ? 330 VAL B N   1 
ATOM   5911 C  CA  . VAL B 1 330 ? 23.88300  37.23400  45.54200 1.000 20.69000 ? 330 VAL B CA  1 
ATOM   5912 C  C   . VAL B 1 330 ? 24.14200  36.81300  46.98200 1.000 21.33000 ? 330 VAL B C   1 
ATOM   5913 O  O   . VAL B 1 330 ? 25.28900  36.48700  47.33200 1.000 19.76000 ? 330 VAL B O   1 
ATOM   5914 C  CB  . VAL B 1 330 ? 24.47900  38.62800  45.24500 1.000 21.08000 ? 330 VAL B CB  1 
ATOM   5915 C  CG1 . VAL B 1 330 ? 24.06000  39.63200  46.30900 1.000 22.73000 ? 330 VAL B CG1 1 
ATOM   5916 C  CG2 . VAL B 1 330 ? 26.00400  38.53500  45.13100 1.000 24.48000 ? 330 VAL B CG2 1 
ATOM   5917 N  N   . ASP B 1 331 ? 23.09700  36.76500  47.81900 1.000 15.03000 ? 331 ASP B N   1 
ATOM   5918 C  CA  . ASP B 1 331 ? 23.24400  36.26200  49.17800 1.000 17.45000 ? 331 ASP B CA  1 
ATOM   5919 C  C   . ASP B 1 331 ? 23.49000  34.75900  49.23400 1.000 17.53000 ? 331 ASP B C   1 
ATOM   5920 O  O   . ASP B 1 331 ? 23.80200  34.24200  50.31200 1.000 15.62000 ? 331 ASP B O   1 
ATOM   5921 C  CB  . ASP B 1 331 ? 21.98900  36.59400  49.99100 1.000 19.23000 ? 331 ASP B CB  1 
ATOM   5922 C  CG  . ASP B 1 331 ? 21.96000  38.03900  50.47400 1.000 25.40000 ? 331 ASP B CG  1 
ATOM   5923 O  OD1 . ASP B 1 331 ? 22.74300  38.87400  49.99300 1.000 23.39000 ? 331 ASP B OD1 1 
ATOM   5924 O  OD2 . ASP B 1 331 ? 21.14400  38.33900  51.35400 1.000 29.31000 ? 331 ASP B OD2 1 
ATOM   5925 N  N   . THR B 1 332 ? 23.36200  34.04300  48.11600 1.000 17.94000 ? 332 THR B N   1 
ATOM   5926 C  CA  . THR B 1 332 ? 23.41400  32.58600  48.11400 1.000 14.58000 ? 332 THR B CA  1 
ATOM   5927 C  C   . THR B 1 332 ? 24.72200  32.01600  47.56600 1.000 12.20000 ? 332 THR B C   1 
ATOM   5928 O  O   . THR B 1 332 ? 24.77900  30.81500  47.28700 1.000 12.95000 ? 332 THR B O   1 
ATOM   5929 C  CB  . THR B 1 332 ? 22.25400  32.01400  47.29700 1.000 15.91000 ? 332 THR B CB  1 
ATOM   5930 O  OG1 . THR B 1 332 ? 22.42800  32.37200  45.91800 1.000 14.65000 ? 332 THR B OG1 1 
ATOM   5931 C  CG2 . THR B 1 332 ? 20.91000  32.55500  47.79000 1.000 15.21000 ? 332 THR B CG2 1 
ATOM   5932 N  N   . ILE B 1 333 ? 25.76300  32.82900  47.38400 1.000 11.52000 ? 333 ILE B N   1 
ATOM   5933 C  CA  . ILE B 1 333 ? 27.01200  32.36900  46.76800 1.000 12.11000 ? 333 ILE B CA  1 
ATOM   5934 C  C   . ILE B 1 333 ? 28.16200  32.56500  47.75400 1.000 14.85000 ? 333 ILE B C   1 
ATOM   5935 O  O   . ILE B 1 333 ? 28.38100  33.68000  48.24600 1.000 16.41000 ? 333 ILE B O   1 
ATOM   5936 C  CB  . ILE B 1 333 ? 27.28900  33.10700  45.44400 1.000 14.47000 ? 333 ILE B CB  1 
ATOM   5937 C  CG1 . ILE B 1 333 ? 26.17600  32.83300  44.41700 1.000 13.80000 ? 333 ILE B CG1 1 
ATOM   5938 C  CG2 . ILE B 1 333 ? 28.64600  32.74300  44.87400 1.000 15.06000 ? 333 ILE B CG2 1 
ATOM   5939 C  CD1 . ILE B 1 333 ? 26.07100  33.91900  43.33500 1.000 13.05000 ? 333 ILE B CD1 1 
ATOM   5940 N  N   . ALA B 1 334 ? 28.91300  31.49200  48.01700 1.000 12.74000 ? 334 ALA B N   1 
ATOM   5941 C  CA  . ALA B 1 334 ? 29.96100  31.49000  49.03600 1.000 14.63000 ? 334 ALA B CA  1 
ATOM   5942 C  C   . ALA B 1 334 ? 31.26400  30.94700  48.47300 1.000 14.04000 ? 334 ALA B C   1 
ATOM   5943 O  O   . ALA B 1 334 ? 31.26000  29.98000  47.70600 1.000 14.86000 ? 334 ALA B O   1 
ATOM   5944 C  CB  . ALA B 1 334 ? 29.55000  30.64100  50.24100 1.000 14.64000 ? 334 ALA B CB  1 
ATOM   5945 N  N   . TRP B 1 335 ? 32.38400  31.55600  48.87300 1.000 14.38000 ? 335 TRP B N   1 
ATOM   5946 C  CA  . TRP B 1 335 ? 33.69900  31.15300  48.39000 1.000 15.61000 ? 335 TRP B CA  1 
ATOM   5947 C  C   . TRP B 1 335 ? 34.26200  30.02700  49.24900 1.000 17.08000 ? 335 TRP B C   1 
ATOM   5948 O  O   . TRP B 1 335 ? 33.90000  29.86800  50.41700 1.000 13.41000 ? 335 TRP B O   1 
ATOM   5949 C  CB  . TRP B 1 335 ? 34.68100  32.32800  48.39900 1.000 13.36000 ? 335 TRP B CB  1 
ATOM   5950 C  CG  . TRP B 1 335 ? 36.05600  31.91500  47.95800 1.000 11.85000 ? 335 TRP B CG  1 
ATOM   5951 C  CD1 . TRP B 1 335 ? 36.44900  31.61000  46.69400 1.000 14.65000 ? 335 TRP B CD1 1 
ATOM   5952 C  CD2 . TRP B 1 335 ? 37.20900  31.74800  48.79500 1.000 14.36000 ? 335 TRP B CD2 1 
ATOM   5953 N  NE1 . TRP B 1 335 ? 37.78800  31.26300  46.68300 1.000 14.81000 ? 335 TRP B NE1 1 
ATOM   5954 C  CE2 . TRP B 1 335 ? 38.27400  31.34100  47.96200 1.000 13.56000 ? 335 TRP B CE2 1 
ATOM   5955 C  CE3 . TRP B 1 335 ? 37.44400  31.90000  50.17200 1.000 15.65000 ? 335 TRP B CE3 1 
ATOM   5956 C  CZ2 . TRP B 1 335 ? 39.55700  31.08900  48.45700 1.000 13.85000 ? 335 TRP B CZ2 1 
ATOM   5957 C  CZ3 . TRP B 1 335 ? 38.72000  31.63800  50.66600 1.000 15.82000 ? 335 TRP B CZ3 1 
ATOM   5958 C  CH2 . TRP B 1 335 ? 39.76200  31.24400  49.80200 1.000 13.68000 ? 335 TRP B CH2 1 
ATOM   5959 N  N   . GLU B 1 336 ? 35.17300  29.25200  48.65600 1.000 13.05000 ? 336 GLU B N   1 
ATOM   5960 C  CA  . GLU B 1 336 ? 35.86500  28.20700  49.39600 1.000 11.34000 ? 336 GLU B CA  1 
ATOM   5961 C  C   . GLU B 1 336 ? 37.25800  28.04000  48.82100 1.000 15.39000 ? 336 GLU B C   1 
ATOM   5962 O  O   . GLU B 1 336 ? 37.48000  28.28200  47.63900 1.000 14.37000 ? 336 GLU B O   1 
ATOM   5963 C  CB  . GLU B 1 336 ? 35.11400  26.88200  49.33500 1.000 12.51000 ? 336 GLU B CB  1 
ATOM   5964 C  CG  . GLU B 1 336 ? 34.70100  26.49100  47.92500 1.000 12.13000 ? 336 GLU B CG  1 
ATOM   5965 C  CD  . GLU B 1 336 ? 34.30200  25.03900  47.84500 1.000 16.41000 ? 336 GLU B CD  1 
ATOM   5966 O  OE1 . GLU B 1 336 ? 33.10100  24.74600  48.05500 1.000 12.40000 ? 336 GLU B OE1 1 
ATOM   5967 O  OE2 . GLU B 1 336 ? 35.19900  24.19200  47.62600 1.000 15.08000 ? 336 GLU B OE2 1 
ATOM   5968 N  N   . CYS B 1 337 ? 38.19300  27.61800  49.67300 1.000 10.10000 ? 337 CYS B N   1 
ATOM   5969 C  CA  . CYS B 1 337 ? 39.58300  27.43300  49.26300 1.000 14.72000 ? 337 CYS B CA  1 
ATOM   5970 C  C   . CYS B 1 337 ? 39.87800  26.00300  48.81500 1.000 13.19000 ? 337 CYS B C   1 
ATOM   5971 O  O   . CYS B 1 337 ? 40.67300  25.79300  47.88900 1.000 13.24000 ? 337 CYS B O   1 
ATOM   5972 C  CB  . CYS B 1 337 ? 40.51000  27.83400  50.41400 1.000 13.47000 ? 337 CYS B CB  1 
ATOM   5973 S  SG  . CYS B 1 337 ? 42.26300  27.74300  50.00500 1.000 16.19000 ? 337 CYS B SG  1 
ATOM   5974 N  N   . ASP B 1 338 ? 39.23900  25.01300  49.44400 1.000 13.66000 ? 338 ASP B N   1 
ATOM   5975 C  CA  . ASP B 1 338 ? 39.44200  23.58900  49.15000 1.000 12.31000 ? 338 ASP B CA  1 
ATOM   5976 C  C   . ASP B 1 338 ? 40.88600  23.14700  49.38000 1.000 15.83000 ? 338 ASP B C   1 
ATOM   5977 O  O   . ASP B 1 338 ? 41.37200  22.21900  48.72300 1.000 13.46000 ? 338 ASP B O   1 
ATOM   5978 C  CB  . ASP B 1 338 ? 38.99300  23.22500  47.73400 1.000 10.96000 ? 338 ASP B CB  1 
ATOM   5979 C  CG  . ASP B 1 338 ? 38.55400  21.77500  47.62300 1.000 16.79000 ? 338 ASP B CG  1 
ATOM   5980 O  OD1 . ASP B 1 338 ? 37.92400  21.28000  48.58800 1.000 12.39000 ? 338 ASP B OD1 1 
ATOM   5981 O  OD2 . ASP B 1 338 ? 38.83600  21.14400  46.57600 1.000 14.86000 ? 338 ASP B OD2 1 
ATOM   5982 N  N   . TYR B 1 339 ? 41.56200  23.79700  50.32100 1.000 14.15000 ? 339 TYR B N   1 
ATOM   5983 C  CA  . TYR B 1 339 ? 42.88400  23.35300  50.76000 1.000 12.11000 ? 339 TYR B CA  1 
ATOM   5984 C  C   . TYR B 1 339 ? 42.78600  21.94300  51.34600 1.000 16.11000 ? 339 TYR B C   1 
ATOM   5985 O  O   . TYR B 1 339 ? 41.87200  21.66400  52.12800 1.000 15.84000 ? 339 TYR B O   1 
ATOM   5986 C  CB  . TYR B 1 339 ? 43.40500  24.33700  51.81000 1.000 14.97000 ? 339 TYR B CB  1 
ATOM   5987 C  CG  . TYR B 1 339 ? 44.80200  24.09700  52.33400 1.000 16.14000 ? 339 TYR B CG  1 
ATOM   5988 C  CD1 . TYR B 1 339 ? 45.05800  23.09300  53.25600 1.000 14.57000 ? 339 TYR B CD1 1 
ATOM   5989 C  CD2 . TYR B 1 339 ? 45.84900  24.91100  51.95100 1.000 15.39000 ? 339 TYR B CD2 1 
ATOM   5990 C  CE1 . TYR B 1 339 ? 46.32300  22.89100  53.76100 1.000 16.53000 ? 339 TYR B CE1 1 
ATOM   5991 C  CE2 . TYR B 1 339 ? 47.12800  24.71800  52.46000 1.000 14.04000 ? 339 TYR B CE2 1 
ATOM   5992 C  CZ  . TYR B 1 339 ? 47.35700  23.70500  53.35800 1.000 17.36000 ? 339 TYR B CZ  1 
ATOM   5993 O  OH  . TYR B 1 339 ? 48.63100  23.49200  53.86300 1.000 17.18000 ? 339 TYR B OH  1 
ATOM   5994 N  N   . PRO B 1 340 ? 43.70400  21.02000  50.99500 1.000 13.83000 ? 340 PRO B N   1 
ATOM   5995 C  CA  . PRO B 1 340 ? 44.88600  21.12400  50.14200 1.000 14.09000 ? 340 PRO B CA  1 
ATOM   5996 C  C   . PRO B 1 340 ? 44.70300  20.34900  48.83500 1.000 17.23000 ? 340 PRO B C   1 
ATOM   5997 O  O   . PRO B 1 340 ? 45.66000  19.77400  48.30600 1.000 16.29000 ? 340 PRO B O   1 
ATOM   5998 C  CB  . PRO B 1 340 ? 45.97200  20.48600  51.00900 1.000 15.30000 ? 340 PRO B CB  1 
ATOM   5999 C  CG  . PRO B 1 340 ? 45.18300  19.46200  51.92300 1.000 15.99000 ? 340 PRO B CG  1 
ATOM   6000 C  CD  . PRO B 1 340 ? 43.69600  19.71200  51.67300 1.000 15.18000 ? 340 PRO B CD  1 
ATOM   6001 N  N   . HIS B 1 341 ? 43.46900  20.32900  48.33200 1.000 15.17000 ? 341 HIS B N   1 
ATOM   6002 C  CA  . HIS B 1 341 ? 43.14800  19.61300  47.10600 1.000 13.96000 ? 341 HIS B CA  1 
ATOM   6003 C  C   . HIS B 1 341 ? 43.79200  20.26500  45.89000 1.000 15.68000 ? 341 HIS B C   1 
ATOM   6004 O  O   . HIS B 1 341 ? 44.07600  21.46300  45.87200 1.000 12.85000 ? 341 HIS B O   1 
ATOM   6005 C  CB  . HIS B 1 341 ? 41.63900  19.59600  46.86800 1.000 14.37000 ? 341 HIS B CB  1 
ATOM   6006 C  CG  . HIS B 1 341 ? 40.91900  18.54400  47.63900 1.000 14.65000 ? 341 HIS B CG  1 
ATOM   6007 N  ND1 . HIS B 1 341 ? 39.62100  18.17300  47.35800 1.000 16.18000 ? 341 HIS B ND1 1 
ATOM   6008 C  CD2 . HIS B 1 341 ? 41.31500  17.77900  48.68200 1.000 16.03000 ? 341 HIS B CD2 1 
ATOM   6009 C  CE1 . HIS B 1 341 ? 39.25300  17.21700  48.19300 1.000 16.14000 ? 341 HIS B CE1 1 
ATOM   6010 N  NE2 . HIS B 1 341 ? 40.26200  16.96300  49.00700 1.000 16.11000 ? 341 HIS B NE2 1 
ATOM   6011 N  N   . SER B 1 342 ? 43.94200  19.45800  44.83300 1.000 13.85000 ? 342 SER B N   1 
ATOM   6012 C  CA  . SER B 1 342 ? 44.44800  19.95600  43.55800 1.000 17.96000 ? 342 SER B CA  1 
ATOM   6013 C  C   . SER B 1 342 ? 43.68000  21.17200  43.04800 1.000 16.52000 ? 342 SER B C   1 
ATOM   6014 O  O   . SER B 1 342 ? 44.26000  22.03000  42.37900 1.000 17.32000 ? 342 SER B O   1 
ATOM   6015 C  CB  . SER B 1 342 ? 44.39800  18.83500  42.52000 1.000 17.21000 ? 342 SER B CB  1 
ATOM   6016 O  OG  . SER B 1 342 ? 43.06700  18.38200  42.36300 1.000 19.01000 ? 342 SER B OG  1 
ATOM   6017 N  N   . ASP B 1 343 ? 42.37700  21.26200  43.33000 1.000 14.81000 ? 343 ASP B N   1 
ATOM   6018 C  CA  . ASP B 1 343 ? 41.59100  22.39700  42.86500 1.000 14.28000 ? 343 ASP B CA  1 
ATOM   6019 C  C   . ASP B 1 343 ? 41.81100  23.66400  43.67800 1.000 14.95000 ? 343 ASP B C   1 
ATOM   6020 O  O   . ASP B 1 343 ? 41.32400  24.72600  43.28100 1.000 15.74000 ? 343 ASP B O   1 
ATOM   6021 C  CB  . ASP B 1 343 ? 40.09400  22.03900  42.87600 1.000 14.96000 ? 343 ASP B CB  1 
ATOM   6022 C  CG  . ASP B 1 343 ? 39.73900  21.07300  41.76600 1.000 20.65000 ? 343 ASP B CG  1 
ATOM   6023 O  OD1 . ASP B 1 343 ? 39.86600  21.46000  40.58200 1.000 21.99000 ? 343 ASP B OD1 1 
ATOM   6024 O  OD2 . ASP B 1 343 ? 39.39300  19.91300  42.07200 1.000 17.84000 ? 343 ASP B OD2 1 
ATOM   6025 N  N   . SER B 1 344 ? 42.51500  23.59500  44.79900 1.000 15.73000 ? 344 SER B N   1 
ATOM   6026 C  CA  . SER B 1 344 ? 42.66200  24.78100  45.63200 1.000 14.01000 ? 344 SER B CA  1 
ATOM   6027 C  C   . SER B 1 344 ? 43.45400  25.86700  44.90500 1.000 17.46000 ? 344 SER B C   1 
ATOM   6028 O  O   . SER B 1 344 ? 44.31400  25.58500  44.06900 1.000 13.32000 ? 344 SER B O   1 
ATOM   6029 C  CB  . SER B 1 344 ? 43.35900  24.42500  46.94700 1.000 13.65000 ? 344 SER B CB  1 
ATOM   6030 O  OG  . SER B 1 344 ? 43.57100  25.58900  47.73200 1.000 14.82000 ? 344 SER B OG  1 
ATOM   6031 N  N   . THR B 1 345 ? 43.13800  27.12400  45.22200 1.000 13.33000 ? 345 THR B N   1 
ATOM   6032 C  CA  . THR B 1 345 ? 43.89300  28.27100  44.73600 1.000 14.00000 ? 345 THR B CA  1 
ATOM   6033 C  C   . THR B 1 345 ? 44.95600  28.75400  45.72300 1.000 14.39000 ? 345 THR B C   1 
ATOM   6034 O  O   . THR B 1 345 ? 45.59300  29.78000  45.46500 1.000 16.33000 ? 345 THR B O   1 
ATOM   6035 C  CB  . THR B 1 345 ? 42.94600  29.42700  44.39000 1.000 15.28000 ? 345 THR B CB  1 
ATOM   6036 O  OG1 . THR B 1 345 ? 42.01500  29.62300  45.46000 1.000 15.42000 ? 345 THR B OG1 1 
ATOM   6037 C  CG2 . THR B 1 345 ? 42.17200  29.10200  43.12500 1.000 15.46000 ? 345 THR B CG2 1 
ATOM   6038 N  N   . TRP B 1 346 ? 45.16300  28.04400  46.83700 1.000 14.58000 ? 346 TRP B N   1 
ATOM   6039 C  CA  . TRP B 1 346 ? 46.27300  28.35800  47.73200 1.000 14.71000 ? 346 TRP B CA  1 
ATOM   6040 C  C   . TRP B 1 346 ? 47.57800  28.33300  46.93900 1.000 14.14000 ? 346 TRP B C   1 
ATOM   6041 O  O   . TRP B 1 346 ? 47.72600  27.50500  46.03700 1.000 19.16000 ? 346 TRP B O   1 
ATOM   6042 C  CB  . TRP B 1 346 ? 46.34300  27.33400  48.87000 1.000 13.07000 ? 346 TRP B CB  1 
ATOM   6043 C  CG  . TRP B 1 346 ? 47.39000  27.58400  49.93800 1.000 13.11000 ? 346 TRP B CG  1 
ATOM   6044 C  CD1 . TRP B 1 346 ? 47.19200  28.16600  51.16100 1.000 14.70000 ? 346 TRP B CD1 1 
ATOM   6045 C  CD2 . TRP B 1 346 ? 48.78900  27.24200  49.88100 1.000 15.65000 ? 346 TRP B CD2 1 
ATOM   6046 N  NE1 . TRP B 1 346 ? 48.38100  28.20100  51.87200 1.000 15.79000 ? 346 TRP B NE1 1 
ATOM   6047 C  CE2 . TRP B 1 346 ? 49.37200  27.65100  51.10300 1.000 16.48000 ? 346 TRP B CE2 1 
ATOM   6048 C  CE3 . TRP B 1 346 ? 49.60400  26.64600  48.91400 1.000 16.05000 ? 346 TRP B CE3 1 
ATOM   6049 C  CZ2 . TRP B 1 346 ? 50.73000  27.48100  51.37500 1.000 18.37000 ? 346 TRP B CZ2 1 
ATOM   6050 C  CZ3 . TRP B 1 346 ? 50.94400  26.46900  49.18900 1.000 16.67000 ? 346 TRP B CZ3 1 
ATOM   6051 C  CH2 . TRP B 1 346 ? 51.49400  26.88500  50.41100 1.000 18.66000 ? 346 TRP B CH2 1 
ATOM   6052 N  N   . PRO B 1 347 ? 48.55100  29.21900  47.23900 1.000 16.37000 ? 347 PRO B N   1 
ATOM   6053 C  CA  . PRO B 1 347 ? 48.61200  30.29100  48.23000 1.000 16.41000 ? 347 PRO B CA  1 
ATOM   6054 C  C   . PRO B 1 347 ? 48.27000  31.65300  47.66500 1.000 16.77000 ? 347 PRO B C   1 
ATOM   6055 O  O   . PRO B 1 347 ? 48.67700  32.64100  48.27800 1.000 15.91000 ? 347 PRO B O   1 
ATOM   6056 C  CB  . PRO B 1 347 ? 50.07900  30.27800  48.64800 1.000 19.09000 ? 347 PRO B CB  1 
ATOM   6057 C  CG  . PRO B 1 347 ? 50.77900  29.99400  47.35900 1.000 17.69000 ? 347 PRO B CG  1 
ATOM   6058 C  CD  . PRO B 1 347 ? 49.84600  29.08800  46.54300 1.000 14.92000 ? 347 PRO B CD  1 
ATOM   6059 N  N   . ARG B 1 348 ? 47.55200  31.72000  46.54400 1.000 15.72000 ? 348 ARG B N   1 
ATOM   6060 C  CA  . ARG B 1 348 ? 47.12800  32.99000  45.96000 1.000 16.89000 ? 348 ARG B CA  1 
ATOM   6061 C  C   . ARG B 1 348 ? 45.60600  33.08400  45.84500 1.000 16.63000 ? 348 ARG B C   1 
ATOM   6062 O  O   . ARG B 1 348 ? 45.06300  33.62000  44.87400 1.000 15.69000 ? 348 ARG B O   1 
ATOM   6063 C  CB  . ARG B 1 348 ? 47.78400  33.20500  44.59800 1.000 17.22000 ? 348 ARG B CB  1 
ATOM   6064 C  CG  . ARG B 1 348 ? 49.31400  33.31500  44.67700 1.000 20.76000 ? 348 ARG B CG  1 
ATOM   6065 C  CD  . ARG B 1 348 ? 49.96600  33.51600  43.30200 1.000 28.12000 ? 348 ARG B CD  1 
ATOM   6066 N  NE  . ARG B 1 348 ? 49.45700  34.68900  42.58600 1.000 33.60000 ? 348 ARG B NE  1 
ATOM   6067 C  CZ  . ARG B 1 348 ? 49.89300  35.93700  42.76500 1.000 35.60000 ? 348 ARG B CZ  1 
ATOM   6068 N  NH1 . ARG B 1 348 ? 50.85600  36.19700  43.64600 1.000 35.01000 ? 348 ARG B NH1 1 
ATOM   6069 N  NH2 . ARG B 1 348 ? 49.36200  36.93100  42.06400 1.000 35.74000 ? 348 ARG B NH2 1 
ATOM   6070 N  N   . SER B 1 349 ? 44.89400  32.56000  46.83300 1.000 14.46000 ? 349 SER B N   1 
ATOM   6071 C  CA  . SER B 1 349 ? 43.43500  32.66200  46.80800 1.000 15.79000 ? 349 SER B CA  1 
ATOM   6072 C  C   . SER B 1 349 ? 42.94000  34.10000  46.72500 1.000 16.04000 ? 349 SER B C   1 
ATOM   6073 O  O   . SER B 1 349 ? 42.04900  34.37100  45.90000 1.000 17.12000 ? 349 SER B O   1 
ATOM   6074 C  CB  . SER B 1 349 ? 42.84200  31.94700  48.02600 1.000 14.53000 ? 349 SER B CB  1 
ATOM   6075 O  OG  . SER B 1 349 ? 43.00100  30.55100  47.91300 1.000 15.39000 ? 349 SER B OG  1 
ATOM   6076 N  N   . PRO B 1 350 ? 43.43900  35.05400  47.52600 1.000 16.41000 ? 350 PRO B N   1 
ATOM   6077 C  CA  . PRO B 1 350 ? 42.92100  36.42600  47.40100 1.000 15.67000 ? 350 PRO B CA  1 
ATOM   6078 C  C   . PRO B 1 350 ? 43.10800  36.98800  46.01000 1.000 16.98000 ? 350 PRO B C   1 
ATOM   6079 O  O   . PRO B 1 350 ? 42.16700  37.54000  45.43400 1.000 16.29000 ? 350 PRO B O   1 
ATOM   6080 C  CB  . PRO B 1 350 ? 43.74000  37.20900  48.44500 1.000 17.85000 ? 350 PRO B CB  1 
ATOM   6081 C  CG  . PRO B 1 350 ? 44.24700  36.18200  49.39100 1.000 15.17000 ? 350 PRO B CG  1 
ATOM   6082 C  CD  . PRO B 1 350 ? 44.49600  34.97100  48.55000 1.000 17.54000 ? 350 PRO B CD  1 
ATOM   6083 N  N   . GLU B 1 351 ? 44.30700  36.84000  45.44000 1.000 15.24000 ? 351 GLU B N   1 
ATOM   6084 C  CA  . GLU B 1 351 ? 44.57100  37.44300  44.13900 1.000 15.29000 ? 351 GLU B CA  1 
ATOM   6085 C  C   . GLU B 1 351 ? 43.70900  36.81200  43.06000 1.000 17.27000 ? 351 GLU B C   1 
ATOM   6086 O  O   . GLU B 1 351 ? 43.13300  37.51500  42.21900 1.000 20.25000 ? 351 GLU B O   1 
ATOM   6087 C  CB  . GLU B 1 351 ? 46.05600  37.30200  43.79200 1.000 21.53000 ? 351 GLU B CB  1 
ATOM   6088 C  CG  . GLU B 1 351 ? 46.96800  38.19100  44.62400 1.000 20.65000 ? 351 GLU B CG  1 
ATOM   6089 C  CD  . GLU B 1 351 ? 47.32000  37.59800  45.96500 1.000 22.57000 ? 351 GLU B CD  1 
ATOM   6090 O  OE1 . GLU B 1 351 ? 46.87500  36.47000  46.27400 1.000 20.14000 ? 351 GLU B OE1 1 
ATOM   6091 O  OE2 . GLU B 1 351 ? 48.06200  38.25900  46.71300 1.000 25.12000 ? 351 GLU B OE2 1 
ATOM   6092 N  N   . THR B 1 352 ? 43.59000  35.48500  43.07900 1.000 15.25000 ? 352 THR B N   1 
ATOM   6093 C  CA  . THR B 1 352 ? 42.82500  34.79900  42.04900 1.000 15.06000 ? 352 THR B CA  1 
ATOM   6094 C  C   . THR B 1 352 ? 41.34100  35.15300  42.12500 1.000 16.90000 ? 352 THR B C   1 
ATOM   6095 O  O   . THR B 1 352 ? 40.70900  35.42400  41.09500 1.000 16.72000 ? 352 THR B O   1 
ATOM   6096 C  CB  . THR B 1 352 ? 43.04600  33.29500  42.18300 1.000 18.02000 ? 352 THR B CB  1 
ATOM   6097 O  OG1 . THR B 1 352 ? 44.44700  33.01900  42.00500 1.000 17.82000 ? 352 THR B OG1 1 
ATOM   6098 C  CG2 . THR B 1 352 ? 42.24400  32.54100  41.14900 1.000 15.57000 ? 352 THR B CG2 1 
ATOM   6099 N  N   . LEU B 1 353 ? 40.77100  35.16800  43.32900 1.000 13.23000 ? 353 LEU B N   1 
ATOM   6100 C  CA  . LEU B 1 353 ? 39.35300  35.49400  43.45800 1.000 15.65000 ? 353 LEU B CA  1 
ATOM   6101 C  C   . LEU B 1 353 ? 39.09100  36.96500  43.13700 1.000 18.61000 ? 353 LEU B C   1 
ATOM   6102 O  O   . LEU B 1 353 ? 38.12900  37.28500  42.42500 1.000 18.31000 ? 353 LEU B O   1 
ATOM   6103 C  CB  . LEU B 1 353 ? 38.85600  35.15000  44.86100 1.000 14.48000 ? 353 LEU B CB  1 
ATOM   6104 C  CG  . LEU B 1 353 ? 37.34900  35.37300  45.02700 1.000 18.60000 ? 353 LEU B CG  1 
ATOM   6105 C  CD1 . LEU B 1 353 ? 36.56700  34.47000  44.08300 1.000 16.98000 ? 353 LEU B CD1 1 
ATOM   6106 C  CD2 . LEU B 1 353 ? 36.87600  35.19300  46.47500 1.000 15.87000 ? 353 LEU B CD2 1 
ATOM   6107 N  N   . LYS B 1 354 ? 39.94600  37.87200  43.63300 1.000 16.65000 ? 354 LYS B N   1 
ATOM   6108 C  CA  . LYS B 1 354 ? 39.72300  39.30400  43.40700 1.000 17.83000 ? 354 LYS B CA  1 
ATOM   6109 C  C   . LYS B 1 354 ? 39.66700  39.62800  41.91900 1.000 20.10000 ? 354 LYS B C   1 
ATOM   6110 O  O   . LYS B 1 354 ? 38.83100  40.43200  41.47900 1.000 21.95000 ? 354 LYS B O   1 
ATOM   6111 C  CB  . LYS B 1 354 ? 40.81500  40.13500  44.09300 1.000 20.09000 ? 354 LYS B CB  1 
ATOM   6112 C  CG  . LYS B 1 354 ? 40.57900  41.66500  44.08300 1.000 19.42000 ? 354 LYS B CG  1 
ATOM   6113 C  CD  . LYS B 1 354 ? 39.23600  42.05900  44.73100 1.000 22.11000 ? 354 LYS B CD  1 
ATOM   6114 C  CE  . LYS B 1 354 ? 39.22300  43.52700  45.20300 1.000 25.16000 ? 354 LYS B CE  1 
ATOM   6115 N  NZ  . LYS B 1 354 ? 39.63900  44.47000  44.11300 1.000 26.06000 ? 354 LYS B NZ  1 
ATOM   6116 N  N   . SER B 1 355 ? 40.54100  39.01000  41.12700 1.000 17.81000 ? 355 SER B N   1 
ATOM   6117 C  CA  . SER B 1 355 ? 40.50800  39.23900  39.68900 1.000 23.02000 ? 355 SER B CA  1 
ATOM   6118 C  C   . SER B 1 355 ? 39.16000  38.84300  39.09600 1.000 22.50000 ? 355 SER B C   1 
ATOM   6119 O  O   . SER B 1 355 ? 38.64000  39.53700  38.21300 1.000 19.08000 ? 355 SER B O   1 
ATOM   6120 C  CB  . SER B 1 355 ? 41.64300  38.47800  39.01000 1.000 24.67000 ? 355 SER B CB  1 
ATOM   6121 O  OG  . SER B 1 355 ? 41.38800  38.31500  37.63000 1.000 37.27000 ? 355 SER B OG  1 
ATOM   6122 N  N   . GLU B 1 356 ? 38.57800  37.72900  39.56700 1.000 17.62000 ? 356 GLU B N   1 
ATOM   6123 C  CA  . GLU B 1 356 ? 37.25500  37.32800  39.09700 1.000 20.29000 ? 356 GLU B CA  1 
ATOM   6124 C  C   . GLU B 1 356 ? 36.18800  38.28800  39.59200 1.000 16.06000 ? 356 GLU B C   1 
ATOM   6125 O  O   . GLU B 1 356 ? 35.25800  38.63600  38.85200 1.000 18.30000 ? 356 GLU B O   1 
ATOM   6126 C  CB  . GLU B 1 356 ? 36.91900  35.91200  39.56700 1.000 19.03000 ? 356 GLU B CB  1 
ATOM   6127 C  CG  . GLU B 1 356 ? 37.86100  34.87000  39.08900 1.000 19.83000 ? 356 GLU B CG  1 
ATOM   6128 C  CD  . GLU B 1 356 ? 37.57800  33.50800  39.68700 1.000 20.75000 ? 356 GLU B CD  1 
ATOM   6129 O  OE1 . GLU B 1 356 ? 36.39300  33.18900  39.95300 1.000 16.13000 ? 356 GLU B OE1 1 
ATOM   6130 O  OE2 . GLU B 1 356 ? 38.55200  32.74900  39.88500 1.000 22.45000 ? 356 GLU B OE2 1 
ATOM   6131 N  N   . LEU B 1 357 ? 36.29600  38.71700  40.84600 1.000 15.61000 ? 357 LEU B N   1 
ATOM   6132 C  CA  . LEU B 1 357 ? 35.29800  39.61800  41.40000 1.000 19.34000 ? 357 LEU B CA  1 
ATOM   6133 C  C   . LEU B 1 357 ? 35.31200  40.95600  40.67000 1.000 22.18000 ? 357 LEU B C   1 
ATOM   6134 O  O   . LEU B 1 357 ? 34.25100  41.51700  40.35700 1.000 19.81000 ? 357 LEU B O   1 
ATOM   6135 C  CB  . LEU B 1 357 ? 35.55000  39.80500  42.89800 1.000 17.35000 ? 357 LEU B CB  1 
ATOM   6136 C  CG  . LEU B 1 357 ? 35.42400  38.52900  43.72900 1.000 16.41000 ? 357 LEU B CG  1 
ATOM   6137 C  CD1 . LEU B 1 357 ? 36.01800  38.74800  45.11600 1.000 17.84000 ? 357 LEU B CD1 1 
ATOM   6138 C  CD2 . LEU B 1 357 ? 33.95600  38.09500  43.82400 1.000 22.38000 ? 357 LEU B CD2 1 
ATOM   6139 N  N   . ASP B 1 358 ? 36.50400  41.47200  40.37200 1.000 17.96000 ? 358 ASP B N   1 
ATOM   6140 C  CA  . ASP B 1 358 ? 36.59400  42.74500  39.66000 1.000 22.00000 ? 358 ASP B CA  1 
ATOM   6141 C  C   . ASP B 1 358 ? 36.02800  42.62300  38.25300 1.000 19.64000 ? 358 ASP B C   1 
ATOM   6142 O  O   . ASP B 1 358 ? 35.32000  43.52000  37.78100 1.000 20.95000 ? 358 ASP B O   1 
ATOM   6143 C  CB  . ASP B 1 358 ? 38.04400  43.23000  39.59600 1.000 19.94000 ? 358 ASP B CB  1 
ATOM   6144 C  CG  . ASP B 1 358 ? 38.55900  43.71900  40.92900 1.000 23.46000 ? 358 ASP B CG  1 
ATOM   6145 O  OD1 . ASP B 1 358 ? 37.73500  44.02800  41.81600 1.000 25.31000 ? 358 ASP B OD1 1 
ATOM   6146 O  OD2 . ASP B 1 358 ? 39.80100  43.79700  41.08100 1.000 31.33000 ? 358 ASP B OD2 1 
ATOM   6147 N  N   . ALA B 1 359 ? 36.34200  41.52600  37.56300 1.000 17.80000 ? 359 ALA B N   1 
ATOM   6148 C  CA  . ALA B 1 359 ? 35.87100  41.35500  36.19300 1.000 19.94000 ? 359 ALA B CA  1 
ATOM   6149 C  C   . ALA B 1 359 ? 34.35600  41.26000  36.14200 1.000 25.81000 ? 359 ALA B C   1 
ATOM   6150 O  O   . ALA B 1 359 ? 33.73800  41.63900  35.14000 1.000 23.44000 ? 359 ALA B O   1 
ATOM   6151 C  CB  . ALA B 1 359 ? 36.49600  40.11000  35.57000 1.000 20.90000 ? 359 ALA B CB  1 
ATOM   6152 N  N   . ALA B 1 360 ? 33.74300  40.75600  37.20700 1.000 20.01000 ? 360 ALA B N   1 
ATOM   6153 C  CA  . ALA B 1 360 ? 32.29800  40.66000  37.29400 1.000 21.26000 ? 360 ALA B CA  1 
ATOM   6154 C  C   . ALA B 1 360 ? 31.66900  41.93100  37.85600 1.000 21.42000 ? 360 ALA B C   1 
ATOM   6155 O  O   . ALA B 1 360 ? 30.47500  41.93000  38.16900 1.000 23.47000 ? 360 ALA B O   1 
ATOM   6156 C  CB  . ALA B 1 360 ? 31.91500  39.44100  38.14600 1.000 21.84000 ? 360 ALA B CB  1 
ATOM   6157 N  N   . ARG B 1 361 ? 32.46100  43.00300  38.01000 1.000 21.27000 ? 361 ARG B N   1 
ATOM   6158 C  CA  . ARG B 1 361 ? 31.99100  44.30400  38.51000 1.000 24.15000 ? 361 ARG B CA  1 
ATOM   6159 C  C   . ARG B 1 361 ? 31.25900  44.18100  39.84800 1.000 24.22000 ? 361 ARG B C   1 
ATOM   6160 O  O   . ARG B 1 361 ? 30.22800  44.81300  40.08000 1.000 20.34000 ? 361 ARG B O   1 
ATOM   6161 C  CB  . ARG B 1 361 ? 31.10800  45.00100  37.47500 1.000 24.28000 ? 361 ARG B CB  1 
ATOM   6162 C  CG  . ARG B 1 361 ? 31.72700  45.04900  36.09600 1.000 32.92000 ? 361 ARG B CG  1 
ATOM   6163 C  CD  . ARG B 1 361 ? 30.78800  45.64800  35.05900 1.000 40.68000 ? 361 ARG B CD  1 
ATOM   6164 N  NE  . ARG B 1 361 ? 31.33600  45.49600  33.71200 1.000 51.29000 ? 361 ARG B NE  1 
ATOM   6165 C  CZ  . ARG B 1 361 ? 32.28700  46.27400  33.19900 1.000 56.77000 ? 361 ARG B CZ  1 
ATOM   6166 N  NH1 . ARG B 1 361 ? 32.79400  47.27400  33.91700 1.000 49.17000 ? 361 ARG B NH1 1 
ATOM   6167 N  NH2 . ARG B 1 361 ? 32.73000  46.05100  31.96500 1.000 53.88000 ? 361 ARG B NH2 1 
ATOM   6168 N  N   . CYS B 1 362 ? 31.80200  43.38100  40.75500 1.000 22.96000 ? 362 CYS B N   1 
ATOM   6169 C  CA  . CYS B 1 362 ? 31.17700  43.27100  42.06400 1.000 17.51000 ? 362 CYS B CA  1 
ATOM   6170 C  C   . CYS B 1 362 ? 31.39400  44.54200  42.87600 1.000 22.29000 ? 362 CYS B C   1 
ATOM   6171 O  O   . CYS B 1 362 ? 32.49700  45.09500  42.91500 1.000 23.62000 ? 362 CYS B O   1 
ATOM   6172 C  CB  . CYS B 1 362 ? 31.72700  42.07200  42.82100 1.000 19.15000 ? 362 CYS B CB  1 
ATOM   6173 S  SG  . CYS B 1 362 ? 31.23000  40.51100  42.11500 1.000 20.64000 ? 362 CYS B SG  1 
ATOM   6174 N  N   . THR B 1 363 ? 30.32100  45.01400  43.51000 1.000 21.08000 ? 363 THR B N   1 
ATOM   6175 C  CA  . THR B 1 363 ? 30.43000  46.06100  44.50800 1.000 21.58000 ? 363 THR B CA  1 
ATOM   6176 C  C   . THR B 1 363 ? 31.19000  45.54600  45.72000 1.000 22.77000 ? 363 THR B C   1 
ATOM   6177 O  O   . THR B 1 363 ? 31.30100  44.33600  45.94800 1.000 19.55000 ? 363 THR B O   1 
ATOM   6178 C  CB  . THR B 1 363 ? 29.05400  46.53300  44.96800 1.000 19.75000 ? 363 THR B CB  1 
ATOM   6179 O  OG1 . THR B 1 363 ? 28.41200  45.47100  45.67400 1.000 20.58000 ? 363 THR B OG1 1 
ATOM   6180 C  CG2 . THR B 1 363 ? 28.18200  46.94000  43.79900 1.000 25.48000 ? 363 THR B CG2 1 
ATOM   6181 N  N   . ASP B 1 364 ? 31.70300  46.48900  46.51300 1.000 21.24000 ? 364 ASP B N   1 
ATOM   6182 C  CA  . ASP B 1 364 ? 32.31300  46.13800  47.79200 1.000 23.44000 ? 364 ASP B CA  1 
ATOM   6183 C  C   . ASP B 1 364 ? 31.38400  45.28100  48.64500 1.000 19.78000 ? 364 ASP B C   1 
ATOM   6184 O  O   . ASP B 1 364 ? 31.83300  44.34400  49.31600 1.000 19.08000 ? 364 ASP B O   1 
ATOM   6185 C  CB  . ASP B 1 364 ? 32.69000  47.40400  48.55800 1.000 25.83000 ? 364 ASP B CB  1 
ATOM   6186 C  CG  . ASP B 1 364 ? 33.91800  48.07200  48.00800 1.000 29.31000 ? 364 ASP B CG  1 
ATOM   6187 O  OD1 . ASP B 1 364 ? 34.50200  47.55300  47.03100 1.000 28.95000 ? 364 ASP B OD1 1 
ATOM   6188 O  OD2 . ASP B 1 364 ? 34.29100  49.12600  48.56000 1.000 36.96000 ? 364 ASP B OD2 1 
ATOM   6189 N  N   . GLU B 1 365 ? 30.09200  45.60800  48.66400 1.000 19.46000 ? 365 GLU B N   1 
ATOM   6190 C  CA  . GLU B 1 365 ? 29.15300  44.81700  49.45400 1.000 20.74000 ? 365 GLU B CA  1 
ATOM   6191 C  C   . GLU B 1 365 ? 29.06100  43.39700  48.91200 1.000 18.26000 ? 365 GLU B C   1 
ATOM   6192 O  O   . GLU B 1 365 ? 29.01400  42.43000  49.68400 1.000 17.71000 ? 365 GLU B O   1 
ATOM   6193 C  CB  . GLU B 1 365 ? 27.77000  45.47700  49.46100 1.000 22.98000 ? 365 GLU B CB  1 
ATOM   6194 C  CG  . GLU B 1 365 ? 27.67900  46.83400  50.18500 1.000 26.95000 ? 365 GLU B CG  1 
ATOM   6195 C  CD  . GLU B 1 365 ? 28.56900  47.92600  49.58500 1.000 30.48000 ? 365 GLU B CD  1 
ATOM   6196 O  OE1 . GLU B 1 365 ? 28.61500  48.08700  48.34800 1.000 25.42000 ? 365 GLU B OE1 1 
ATOM   6197 O  OE2 . GLU B 1 365 ? 29.24100  48.63400  50.36400 1.000 32.68000 ? 365 GLU B OE2 1 
ATOM   6198 N  N   . GLU B 1 366 ? 29.03900  43.25500  47.58200 1.000 18.36000 ? 366 GLU B N   1 
ATOM   6199 C  CA  . GLU B 1 366 ? 28.98600  41.92900  46.96700 1.000 18.50000 ? 366 GLU B CA  1 
ATOM   6200 C  C   . GLU B 1 366 ? 30.27100  41.14800  47.22300 1.000 15.04000 ? 366 GLU B C   1 
ATOM   6201 O  O   . GLU B 1 366 ? 30.22800  39.94000  47.47500 1.000 15.10000 ? 366 GLU B O   1 
ATOM   6202 C  CB  . GLU B 1 366 ? 28.73100  42.05400  45.46100 1.000 17.61000 ? 366 GLU B CB  1 
ATOM   6203 C  CG  . GLU B 1 366 ? 27.31500  42.48100  45.07900 1.000 19.56000 ? 366 GLU B CG  1 
ATOM   6204 C  CD  . GLU B 1 366 ? 27.15900  42.71100  43.59300 1.000 17.30000 ? 366 GLU B CD  1 
ATOM   6205 O  OE1 . GLU B 1 366 ? 28.08200  43.28000  42.96500 1.000 18.97000 ? 366 GLU B OE1 1 
ATOM   6206 O  OE2 . GLU B 1 366 ? 26.10700  42.33000  43.04100 1.000 21.65000 ? 366 GLU B OE2 1 
ATOM   6207 N  N   . VAL B 1 367 ? 31.42400  41.81900  47.15300 1.000 15.92000 ? 367 VAL B N   1 
ATOM   6208 C  CA  . VAL B 1 367 ? 32.68700  41.19100  47.54800 1.000 17.81000 ? 367 VAL B CA  1 
ATOM   6209 C  C   . VAL B 1 367 ? 32.58100  40.59700  48.95100 1.000 19.08000 ? 367 VAL B C   1 
ATOM   6210 O  O   . VAL B 1 367 ? 32.88800  39.41900  49.17000 1.000 17.12000 ? 367 VAL B O   1 
ATOM   6211 C  CB  . VAL B 1 367 ? 33.84400  42.20400  47.46000 1.000 17.84000 ? 367 VAL B CB  1 
ATOM   6212 C  CG1 . VAL B 1 367 ? 35.14000  41.57000  47.94400 1.000 17.29000 ? 367 VAL B CG1 1 
ATOM   6213 C  CG2 . VAL B 1 367 ? 34.01200  42.71000  46.04000 1.000 19.78000 ? 367 VAL B CG2 1 
ATOM   6214 N  N   . ASP B 1 368 ? 32.16200  41.41400  49.92800 1.000 14.76000 ? 368 ASP B N   1 
ATOM   6215 C  CA  . ASP B 1 368 ? 32.07400  40.95000  51.31200 1.000 14.64000 ? 368 ASP B CA  1 
ATOM   6216 C  C   . ASP B 1 368 ? 31.10600  39.78600  51.44900 1.000 15.12000 ? 368 ASP B C   1 
ATOM   6217 O  O   . ASP B 1 368 ? 31.34100  38.86100  52.23400 1.000 15.97000 ? 368 ASP B O   1 
ATOM   6218 C  CB  . ASP B 1 368 ? 31.62900  42.10000  52.22200 1.000 18.35000 ? 368 ASP B CB  1 
ATOM   6219 C  CG  . ASP B 1 368 ? 32.77400  43.03300  52.60600 1.000 20.73000 ? 368 ASP B CG  1 
ATOM   6220 O  OD1 . ASP B 1 368 ? 33.92900  42.76100  52.24600 1.000 17.13000 ? 368 ASP B OD1 1 
ATOM   6221 O  OD2 . ASP B 1 368 ? 32.50400  44.05100  53.26700 1.000 23.70000 ? 368 ASP B OD2 1 
ATOM   6222 N  N   . LYS B 1 369 ? 29.99300  39.83000  50.72200 1.000 13.64000 ? 369 LYS B N   1 
ATOM   6223 C  CA  . LYS B 1 369 ? 29.02800  38.73300  50.78800 1.000 15.45000 ? 369 LYS B CA  1 
ATOM   6224 C  C   . LYS B 1 369 ? 29.64800  37.42100  50.30800 1.000 14.94000 ? 369 LYS B C   1 
ATOM   6225 O  O   . LYS B 1 369 ? 29.55100  36.38700  50.97800 1.000 15.30000 ? 369 LYS B O   1 
ATOM   6226 C  CB  . LYS B 1 369 ? 27.79500  39.08000  49.95900 1.000 14.67000 ? 369 LYS B CB  1 
ATOM   6227 C  CG  . LYS B 1 369 ? 26.85400  40.11100  50.61900 1.000 16.32000 ? 369 LYS B CG  1 
ATOM   6228 C  CD  . LYS B 1 369 ? 25.66600  40.42500  49.69700 1.000 18.88000 ? 369 LYS B CD  1 
ATOM   6229 C  CE  . LYS B 1 369 ? 24.75500  41.50900  50.28500 1.000 22.10000 ? 369 LYS B CE  1 
ATOM   6230 N  NZ  . LYS B 1 369 ? 24.01100  41.01300  51.45600 1.000 24.94000 ? 369 LYS B NZ  1 
ATOM   6231 N  N   . ILE B 1 370 ? 30.32300  37.45700  49.16300 1.000 14.75000 ? 370 ILE B N   1 
ATOM   6232 C  CA  . ILE B 1 370 ? 30.83600  36.22400  48.56300 1.000 16.00000 ? 370 ILE B CA  1 
ATOM   6233 C  C   . ILE B 1 370 ? 32.02900  35.67800  49.35100 1.000 16.25000 ? 370 ILE B C   1 
ATOM   6234 O  O   . ILE B 1 370 ? 32.14700  34.46300  49.55100 1.000 15.86000 ? 370 ILE B O   1 
ATOM   6235 C  CB  . ILE B 1 370 ? 31.17500  36.47400  47.08200 1.000 14.77000 ? 370 ILE B CB  1 
ATOM   6236 C  CG1 . ILE B 1 370 ? 29.88300  36.69500  46.28100 1.000 17.64000 ? 370 ILE B CG1 1 
ATOM   6237 C  CG2 . ILE B 1 370 ? 31.98900  35.31100  46.47800 1.000 13.17000 ? 370 ILE B CG2 1 
ATOM   6238 C  CD1 . ILE B 1 370 ? 30.08500  37.45400  44.95600 1.000 16.01000 ? 370 ILE B CD1 1 
ATOM   6239 N  N   . THR B 1 371 ? 32.91900  36.55400  49.83400 1.000 14.90000 ? 371 THR B N   1 
ATOM   6240 C  CA  . THR B 1 371 ? 34.13900  36.06300  50.47200 1.000 13.00000 ? 371 THR B CA  1 
ATOM   6241 C  C   . THR B 1 371 ? 33.93200  35.61300  51.92100 1.000 17.13000 ? 371 THR B C   1 
ATOM   6242 O  O   . THR B 1 371 ? 34.67600  34.74100  52.39400 1.000 16.97000 ? 371 THR B O   1 
ATOM   6243 C  CB  . THR B 1 371 ? 35.24500  37.12000  50.40400 1.000 16.15000 ? 371 THR B CB  1 
ATOM   6244 O  OG1 . THR B 1 371 ? 34.89300  38.26000  51.20400 1.000 16.58000 ? 371 THR B OG1 1 
ATOM   6245 C  CG2 . THR B 1 371 ? 35.45100  37.56000  48.98900 1.000 15.13000 ? 371 THR B CG2 1 
ATOM   6246 N  N   . PHE B 1 372 ? 32.93700  36.15000  52.64000 1.000 17.02000 ? 372 PHE B N   1 
ATOM   6247 C  CA  . PHE B 1 372 ? 32.76600  35.72500  54.02600 1.000 14.87000 ? 372 PHE B CA  1 
ATOM   6248 C  C   . PHE B 1 372 ? 31.35500  35.88700  54.58900 1.000 17.40000 ? 372 PHE B C   1 
ATOM   6249 O  O   . PHE B 1 372 ? 30.94700  35.08600  55.42800 1.000 16.00000 ? 372 PHE B O   1 
ATOM   6250 C  CB  . PHE B 1 372 ? 33.76400  36.45600  54.93500 1.000 17.34000 ? 372 PHE B CB  1 
ATOM   6251 C  CG  . PHE B 1 372 ? 33.30500  37.82200  55.39400 1.000 17.78000 ? 372 PHE B CG  1 
ATOM   6252 C  CD1 . PHE B 1 372 ? 32.55800  37.97100  56.54700 1.000 22.51000 ? 372 PHE B CD1 1 
ATOM   6253 C  CD2 . PHE B 1 372 ? 33.65900  38.95700  54.67900 1.000 18.00000 ? 372 PHE B CD2 1 
ATOM   6254 C  CE1 . PHE B 1 372 ? 32.13900  39.22300  56.96600 1.000 23.76000 ? 372 PHE B CE1 1 
ATOM   6255 C  CE2 . PHE B 1 372 ? 33.25000  40.20600  55.09400 1.000 19.16000 ? 372 PHE B CE2 1 
ATOM   6256 C  CZ  . PHE B 1 372 ? 32.49700  40.34000  56.24100 1.000 20.58000 ? 372 PHE B CZ  1 
ATOM   6257 N  N   . ALA B 1 373 ? 30.60400  36.91900  54.18900 1.000 16.44000 ? 373 ALA B N   1 
ATOM   6258 C  CA  . ALA B 1 373 ? 29.40500  37.23800  54.96300 1.000 18.43000 ? 373 ALA B CA  1 
ATOM   6259 C  C   . ALA B 1 373 ? 28.23800  36.29700  54.66200 1.000 18.25000 ? 373 ALA B C   1 
ATOM   6260 O  O   . ALA B 1 373 ? 27.42100  36.02900  55.55300 1.000 17.68000 ? 373 ALA B O   1 
ATOM   6261 C  CB  . ALA B 1 373 ? 28.99700  38.69600  54.73300 1.000 16.49000 ? 373 ALA B CB  1 
ATOM   6262 N  N   . ASN B 1 374 ? 28.13200  35.78300  53.43700 1.000 15.30000 ? 374 ASN B N   1 
ATOM   6263 C  CA  . ASN B 1 374 ? 27.06600  34.82100  53.15400 1.000 15.48000 ? 374 ASN B CA  1 
ATOM   6264 C  C   . ASN B 1 374 ? 27.29100  33.53600  53.93600 1.000 17.09000 ? 374 ASN B C   1 
ATOM   6265 O  O   . ASN B 1 374 ? 26.36200  33.00700  54.56600 1.000 16.44000 ? 374 ASN B O   1 
ATOM   6266 C  CB  . ASN B 1 374 ? 26.98100  34.52200  51.65800 1.000 16.93000 ? 374 ASN B CB  1 
ATOM   6267 C  CG  . ASN B 1 374 ? 26.48400  35.69900  50.84600 1.000 17.31000 ? 374 ASN B CG  1 
ATOM   6268 O  OD1 . ASN B 1 374 ? 25.85400  36.61000  51.37500 1.000 18.05000 ? 374 ASN B OD1 1 
ATOM   6269 N  ND2 . ASN B 1 374 ? 26.73800  35.66600  49.54200 1.000 13.73000 ? 374 ASN B ND2 1 
ATOM   6270 N  N   . ALA B 1 375 ? 28.53000  33.03900  53.93300 1.000 15.71000 ? 375 ALA B N   1 
ATOM   6271 C  CA  . ALA B 1 375 ? 28.85200  31.82400  54.67900 1.000 17.35000 ? 375 ALA B CA  1 
ATOM   6272 C  C   . ALA B 1 375 ? 28.63300  32.01800  56.17400 1.000 15.75000 ? 375 ALA B C   1 
ATOM   6273 O  O   . ALA B 1 375 ? 28.03300  31.16500  56.83700 1.000 18.54000 ? 375 ALA B O   1 
ATOM   6274 C  CB  . ALA B 1 375 ? 30.29800  31.40400  54.39800 1.000 14.45000 ? 375 ALA B CB  1 
ATOM   6275 N  N   . ALA B 1 376 ? 29.12100  33.13400  56.72600 1.000 16.30000 ? 376 ALA B N   1 
ATOM   6276 C  CA  . ALA B 1 376 ? 29.00100  33.36300  58.16500 1.000 16.67000 ? 376 ALA B CA  1 
ATOM   6277 C  C   . ALA B 1 376 ? 27.54400  33.36800  58.60500 1.000 17.41000 ? 376 ALA B C   1 
ATOM   6278 O  O   . ALA B 1 376 ? 27.20000  32.80200  59.64700 1.000 20.33000 ? 376 ALA B O   1 
ATOM   6279 C  CB  . ALA B 1 376 ? 29.68300  34.68300  58.55000 1.000 19.57000 ? 376 ALA B CB  1 
ATOM   6280 N  N   . LYS B 1 377 ? 26.67000  33.98900  57.81100 1.000 17.38000 ? 377 LYS B N   1 
ATOM   6281 C  CA  . LYS B 1 377 ? 25.25000  33.99600  58.14100 1.000 17.70000 ? 377 LYS B CA  1 
ATOM   6282 C  C   . LYS B 1 377 ? 24.63400  32.61700  57.93600 1.000 15.32000 ? 377 LYS B C   1 
ATOM   6283 O  O   . LYS B 1 377 ? 23.84200  32.15700  58.76100 1.000 14.47000 ? 377 LYS B O   1 
ATOM   6284 C  CB  . LYS B 1 377 ? 24.51900  35.03000  57.28600 1.000 17.54000 ? 377 LYS B CB  1 
ATOM   6285 C  CG  . LYS B 1 377 ? 23.02800  35.15100  57.60400 1.000 21.20000 ? 377 LYS B CG  1 
ATOM   6286 C  CD  . LYS B 1 377 ? 22.29000  36.00400  56.57900 1.000 30.51000 ? 377 LYS B CD  1 
ATOM   6287 C  CE  . LYS B 1 377 ? 20.83600  36.24900  57.00600 1.000 43.51000 ? 377 LYS B CE  1 
ATOM   6288 N  NZ  . LYS B 1 377 ? 20.08300  37.06200  56.00000 1.000 45.87000 ? 377 LYS B NZ  1 
ATOM   6289 N  N   . PHE B 1 378 ? 24.99200  31.94100  56.84200 1.000 15.48000 ? 378 PHE B N   1 
ATOM   6290 C  CA  . PHE B 1 378 ? 24.38400  30.64600  56.54500 1.000 17.67000 ? 378 PHE B CA  1 
ATOM   6291 C  C   . PHE B 1 378 ? 24.72700  29.62200  57.61700 1.000 15.45000 ? 378 PHE B C   1 
ATOM   6292 O  O   . PHE B 1 378 ? 23.87300  28.82900  58.02900 1.000 20.86000 ? 378 PHE B O   1 
ATOM   6293 C  CB  . PHE B 1 378 ? 24.83600  30.15300  55.16100 1.000 13.90000 ? 378 PHE B CB  1 
ATOM   6294 C  CG  . PHE B 1 378 ? 23.91200  29.12800  54.54600 1.000 15.44000 ? 378 PHE B CG  1 
ATOM   6295 C  CD1 . PHE B 1 378 ? 22.66300  29.50100  54.05500 1.000 19.19000 ? 378 PHE B CD1 1 
ATOM   6296 C  CD2 . PHE B 1 378 ? 24.28800  27.79200  54.46700 1.000 13.55000 ? 378 PHE B CD2 1 
ATOM   6297 C  CE1 . PHE B 1 378 ? 21.80700  28.56200  53.48900 1.000 16.85000 ? 378 PHE B CE1 1 
ATOM   6298 C  CE2 . PHE B 1 378 ? 23.44900  26.84400  53.89300 1.000 13.75000 ? 378 PHE B CE2 1 
ATOM   6299 C  CZ  . PHE B 1 378 ? 22.20500  27.22400  53.40200 1.000 13.25000 ? 378 PHE B CZ  1 
ATOM   6300 N  N   . PHE B 1 379 ? 25.97600  29.60900  58.06500 1.000 16.53000 ? 379 PHE B N   1 
ATOM   6301 C  CA  . PHE B 1 379 ? 26.43100  28.67900  59.08100 1.000 14.64000 ? 379 PHE B CA  1 
ATOM   6302 C  C   . PHE B 1 379 ? 26.29600  29.23600  60.50000 1.000 17.38000 ? 379 PHE B C   1 
ATOM   6303 O  O   . PHE B 1 379 ? 26.74800  28.58500  61.44600 1.000 21.27000 ? 379 PHE B O   1 
ATOM   6304 C  CB  . PHE B 1 379 ? 27.88300  28.28400  58.80000 1.000 16.68000 ? 379 PHE B CB  1 
ATOM   6305 C  CG  . PHE B 1 379 ? 28.04300  27.33100  57.64200 1.000 16.44000 ? 379 PHE B CG  1 
ATOM   6306 C  CD1 . PHE B 1 379 ? 27.99200  27.78400  56.33400 1.000 15.55000 ? 379 PHE B CD1 1 
ATOM   6307 C  CD2 . PHE B 1 379 ? 28.25100  25.98200  57.86500 1.000 16.75000 ? 379 PHE B CD2 1 
ATOM   6308 C  CE1 . PHE B 1 379 ? 28.14500  26.89700  55.26600 1.000 17.67000 ? 379 PHE B CE1 1 
ATOM   6309 C  CE2 . PHE B 1 379 ? 28.41100  25.09600  56.80300 1.000 15.94000 ? 379 PHE B CE2 1 
ATOM   6310 C  CZ  . PHE B 1 379 ? 28.36400  25.55600  55.50200 1.000 13.79000 ? 379 PHE B CZ  1 
ATOM   6311 N  N   . ASP B 1 380 ? 25.69100  30.41600  60.66700 1.000 18.17000 ? 380 ASP B N   1 
ATOM   6312 C  CA  . ASP B 1 380 ? 25.46600  31.02300  61.98900 1.000 21.07000 ? 380 ASP B CA  1 
ATOM   6313 C  C   . ASP B 1 380 ? 26.76400  31.07300  62.78500 1.000 23.37000 ? 380 ASP B C   1 
ATOM   6314 O  O   . ASP B 1 380 ? 26.86300  30.57900  63.91200 1.000 22.58000 ? 380 ASP B O   1 
ATOM   6315 C  CB  . ASP B 1 380 ? 24.37600  30.28500  62.77100 1.000 20.73000 ? 380 ASP B CB  1 
ATOM   6316 C  CG  . ASP B 1 380 ? 23.72000  31.17100  63.83800 1.000 30.67000 ? 380 ASP B CG  1 
ATOM   6317 O  OD1 . ASP B 1 380 ? 23.92400  32.40200  63.79500 1.000 25.10000 ? 380 ASP B OD1 1 
ATOM   6318 O  OD2 . ASP B 1 380 ? 22.99600  30.64000  64.71200 1.000 35.96000 ? 380 ASP B OD2 1 
ATOM   6319 N  N   . TRP B 1 381 ? 27.78500  31.64800  62.16300 1.000 18.71000 ? 381 TRP B N   1 
ATOM   6320 C  CA  . TRP B 1 381 ? 29.12800  31.66100  62.71400 1.000 22.32000 ? 381 TRP B CA  1 
ATOM   6321 C  C   . TRP B 1 381 ? 29.65300  33.08200  62.70000 1.000 21.84000 ? 381 TRP B C   1 
ATOM   6322 O  O   . TRP B 1 381 ? 29.65800  33.73000  61.64900 1.000 22.90000 ? 381 TRP B O   1 
ATOM   6323 C  CB  . TRP B 1 381 ? 30.04500  30.73700  61.91400 1.000 24.50000 ? 381 TRP B CB  1 
ATOM   6324 C  CG  . TRP B 1 381 ? 31.29900  30.36700  62.64400 1.000 22.84000 ? 381 TRP B CG  1 
ATOM   6325 C  CD1 . TRP B 1 381 ? 31.42900  29.46200  63.66700 1.000 21.07000 ? 381 TRP B CD1 1 
ATOM   6326 C  CD2 . TRP B 1 381 ? 32.59200  30.89500  62.40900 1.000 21.28000 ? 381 TRP B CD2 1 
ATOM   6327 N  NE1 . TRP B 1 381 ? 32.73100  29.39800  64.07600 1.000 23.77000 ? 381 TRP B NE1 1 
ATOM   6328 C  CE2 . TRP B 1 381 ? 33.47000  30.26800  63.31700 1.000 25.58000 ? 381 TRP B CE2 1 
ATOM   6329 C  CE3 . TRP B 1 381 ? 33.10100  31.83800  61.51800 1.000 21.86000 ? 381 TRP B CE3 1 
ATOM   6330 C  CZ2 . TRP B 1 381 ? 34.81600  30.55200  63.35500 1.000 22.48000 ? 381 TRP B CZ2 1 
ATOM   6331 C  CZ3 . TRP B 1 381 ? 34.44400  32.11000  61.55300 1.000 24.49000 ? 381 TRP B CZ3 1 
ATOM   6332 C  CH2 . TRP B 1 381 ? 35.28600  31.47600  62.46900 1.000 26.07000 ? 381 TRP B CH2 1 
ATOM   6333 N  N   . ASP B 1 382 ? 30.08500  33.56800  63.86700 1.000 25.25000 ? 382 ASP B N   1 
ATOM   6334 C  CA  . ASP B 1 382 ? 30.53400  34.94500  64.00600 1.000 24.77000 ? 382 ASP B CA  1 
ATOM   6335 C  C   . ASP B 1 382 ? 32.01000  35.01400  63.66300 1.000 22.03000 ? 382 ASP B C   1 
ATOM   6336 O  O   . ASP B 1 382 ? 32.84200  34.53500  64.44800 1.000 24.62000 ? 382 ASP B O   1 
ATOM   6337 C  CB  . ASP B 1 382 ? 30.29000  35.45000  65.42100 1.000 25.89000 ? 382 ASP B CB  1 
ATOM   6338 C  CG  . ASP B 1 382 ? 30.78600  36.86800  65.62600 1.000 26.00000 ? 382 ASP B CG  1 
ATOM   6339 O  OD1 . ASP B 1 382 ? 31.22100  37.51000  64.64100 1.000 27.50000 ? 382 ASP B OD1 1 
ATOM   6340 O  OD2 . ASP B 1 382 ? 30.75100  37.33700  66.78500 1.000 30.07000 ? 382 ASP B OD2 1 
ATOM   6341 N  N   . PRO B 1 383 ? 32.38700  35.58900  62.52200 1.000 25.02000 ? 383 PRO B N   1 
ATOM   6342 C  CA  . PRO B 1 383 ? 33.79700  35.54600  62.11300 1.000 25.41000 ? 383 PRO B CA  1 
ATOM   6343 C  C   . PRO B 1 383 ? 34.69800  36.42800  62.94700 1.000 25.24000 ? 383 PRO B C   1 
ATOM   6344 O  O   . PRO B 1 383 ? 35.92200  36.24900  62.90600 1.000 21.86000 ? 383 PRO B O   1 
ATOM   6345 C  CB  . PRO B 1 383 ? 33.76200  36.01900  60.65600 1.000 28.05000 ? 383 PRO B CB  1 
ATOM   6346 C  CG  . PRO B 1 383 ? 32.49900  36.78400  60.52500 1.000 22.31000 ? 383 PRO B CG  1 
ATOM   6347 C  CD  . PRO B 1 383 ? 31.52200  36.21700  61.50800 1.000 23.00000 ? 383 PRO B CD  1 
ATOM   6348 N  N   . PHE B 1 384 ? 34.14000  37.37000  63.71000 1.000 21.91000 ? 384 PHE B N   1 
ATOM   6349 C  CA  . PHE B 1 384 ? 34.95900  38.31900  64.45000 1.000 22.48000 ? 384 PHE B CA  1 
ATOM   6350 C  C   . PHE B 1 384 ? 34.80100  38.17700  65.95900 1.000 26.32000 ? 384 PHE B C   1 
ATOM   6351 O  O   . PHE B 1 384 ? 35.13100  39.10500  66.69800 1.000 28.49000 ? 384 PHE B O   1 
ATOM   6352 C  CB  . PHE B 1 384 ? 34.64000  39.73800  63.98700 1.000 26.35000 ? 384 PHE B CB  1 
ATOM   6353 C  CG  . PHE B 1 384 ? 34.66800  39.89300  62.49300 1.000 25.53000 ? 384 PHE B CG  1 
ATOM   6354 C  CD1 . PHE B 1 384 ? 35.77300  39.48000  61.76600 1.000 21.41000 ? 384 PHE B CD1 1 
ATOM   6355 C  CD2 . PHE B 1 384 ? 33.57700  40.40600  61.81400 1.000 26.70000 ? 384 PHE B CD2 1 
ATOM   6356 C  CE1 . PHE B 1 384 ? 35.79900  39.60000  60.39300 1.000 23.29000 ? 384 PHE B CE1 1 
ATOM   6357 C  CE2 . PHE B 1 384 ? 33.60100  40.52700  60.43000 1.000 21.34000 ? 384 PHE B CE2 1 
ATOM   6358 C  CZ  . PHE B 1 384 ? 34.72000  40.12500  59.72700 1.000 21.76000 ? 384 PHE B CZ  1 
ATOM   6359 N  N   . GLU B 1 385 ? 34.35000  37.01700  66.44400 1.000 23.34000 ? 385 GLU B N   1 
ATOM   6360 C  CA  . GLU B 1 385 ? 34.25600  36.83400  67.88900 1.000 26.74000 ? 385 GLU B CA  1 
ATOM   6361 C  C   . GLU B 1 385 ? 35.63700  36.73900  68.53300 1.000 26.16000 ? 385 GLU B C   1 
ATOM   6362 O  O   . GLU B 1 385 ? 35.87200  37.32200  69.59600 1.000 26.34000 ? 385 GLU B O   1 
ATOM   6363 C  CB  . GLU B 1 385 ? 33.42900  35.59200  68.21800 1.000 27.88000 ? 385 GLU B CB  1 
ATOM   6364 C  CG  . GLU B 1 385 ? 33.47400  35.23800  69.69800 1.000 30.06000 ? 385 GLU B CG  1 
ATOM   6365 C  CD  . GLU B 1 385 ? 32.76600  33.94400  70.02100 1.000 31.88000 ? 385 GLU B CD  1 
ATOM   6366 O  OE1 . GLU B 1 385 ? 32.31200  33.25400  69.08200 1.000 39.22000 ? 385 GLU B OE1 1 
ATOM   6367 O  OE2 . GLU B 1 385 ? 32.66300  33.62000  71.22300 1.000 35.93000 ? 385 GLU B OE2 1 
ATOM   6368 N  N   . HIS B 1 386 ? 36.56100  36.00100  67.92100 1.000 25.03000 ? 386 HIS B N   1 
ATOM   6369 C  CA  . HIS B 1 386 ? 37.88800  35.85200  68.49800 1.000 24.77000 ? 386 HIS B CA  1 
ATOM   6370 C  C   . HIS B 1 386 ? 38.93900  36.70600  67.81600 1.000 28.23000 ? 386 HIS B C   1 
ATOM   6371 O  O   . HIS B 1 386 ? 40.01400  36.91600  68.38700 1.000 31.21000 ? 386 HIS B O   1 
ATOM   6372 C  CB  . HIS B 1 386 ? 38.32200  34.38500  68.45200 1.000 29.78000 ? 386 HIS B CB  1 
ATOM   6373 C  CG  . HIS B 1 386 ? 37.38700  33.47100  69.17300 1.000 26.55000 ? 386 HIS B CG  1 
ATOM   6374 N  ND1 . HIS B 1 386 ? 36.41600  32.73800  68.52600 1.000 31.55000 ? 386 HIS B ND1 1 
ATOM   6375 C  CD2 . HIS B 1 386 ? 37.25000  33.19900  70.49200 1.000 27.77000 ? 386 HIS B CD2 1 
ATOM   6376 C  CE1 . HIS B 1 386 ? 35.72800  32.04400  69.41500 1.000 27.28000 ? 386 HIS B CE1 1 
ATOM   6377 N  NE2 . HIS B 1 386 ? 36.21500  32.30700  70.61500 1.000 27.61000 ? 386 HIS B NE2 1 
ATOM   6378 N  N   . ILE B 1 387 ? 38.65800  37.19600  66.61900 1.000 26.20000 ? 387 ILE B N   1 
ATOM   6379 C  CA  . ILE B 1 387 ? 39.63300  37.96100  65.85800 1.000 26.49000 ? 387 ILE B CA  1 
ATOM   6380 C  C   . ILE B 1 387 ? 38.91200  39.19500  65.34600 1.000 24.90000 ? 387 ILE B C   1 
ATOM   6381 O  O   . ILE B 1 387 ? 37.99900  39.06500  64.52000 1.000 25.25000 ? 387 ILE B O   1 
ATOM   6382 C  CB  . ILE B 1 387 ? 40.22700  37.13800  64.70500 1.000 27.32000 ? 387 ILE B CB  1 
ATOM   6383 C  CG1 . ILE B 1 387 ? 40.89700  35.86600  65.24500 1.000 26.49000 ? 387 ILE B CG1 1 
ATOM   6384 C  CG2 . ILE B 1 387 ? 41.20500  37.97300  63.91800 1.000 21.57000 ? 387 ILE B CG2 1 
ATOM   6385 C  CD1 . ILE B 1 387 ? 41.52100  35.00600  64.18300 1.000 24.86000 ? 387 ILE B CD1 1 
ATOM   6386 N  N   . PRO B 1 388 ? 39.27400  40.39100  65.81100 1.000 28.03000 ? 388 PRO B N   1 
ATOM   6387 C  CA  . PRO B 1 388 ? 38.62800  41.61000  65.31100 1.000 28.02000 ? 388 PRO B CA  1 
ATOM   6388 C  C   . PRO B 1 388 ? 38.82700  41.74800  63.81100 1.000 26.85000 ? 388 PRO B C   1 
ATOM   6389 O  O   . PRO B 1 388 ? 39.84100  41.31800  63.25800 1.000 27.48000 ? 388 PRO B O   1 
ATOM   6390 C  CB  . PRO B 1 388 ? 39.34600  42.73600  66.07000 1.000 31.20000 ? 388 PRO B CB  1 
ATOM   6391 C  CG  . PRO B 1 388 ? 40.12600  42.06900  67.16000 1.000 35.40000 ? 388 PRO B CG  1 
ATOM   6392 C  CD  . PRO B 1 388 ? 40.41200  40.68300  66.70000 1.000 31.13000 ? 388 PRO B CD  1 
ATOM   6393 N  N   . ARG B 1 389 ? 37.84300  42.36700  63.15500 1.000 24.40000 ? 389 ARG B N   1 
ATOM   6394 C  CA  . ARG B 1 389 ? 37.86800  42.42700  61.69800 1.000 26.53000 ? 389 ARG B CA  1 
ATOM   6395 C  C   . ARG B 1 389 ? 39.14000  43.08800  61.19200 1.000 28.75000 ? 389 ARG B C   1 
ATOM   6396 O  O   . ARG B 1 389 ? 39.72800  42.63700  60.20000 1.000 29.07000 ? 389 ARG B O   1 
ATOM   6397 C  CB  . ARG B 1 389 ? 36.64600  43.16800  61.16600 1.000 27.67000 ? 389 ARG B CB  1 
ATOM   6398 C  CG  . ARG B 1 389 ? 36.71100  43.37400  59.65500 1.000 28.32000 ? 389 ARG B CG  1 
ATOM   6399 C  CD  . ARG B 1 389 ? 35.35800  43.74100  59.08100 1.000 31.57000 ? 389 ARG B CD  1 
ATOM   6400 N  NE  . ARG B 1 389 ? 35.41300  43.94300  57.63700 1.000 30.34000 ? 389 ARG B NE  1 
ATOM   6401 C  CZ  . ARG B 1 389 ? 34.33400  43.93400  56.86000 1.000 29.96000 ? 389 ARG B CZ  1 
ATOM   6402 N  NH1 . ARG B 1 389 ? 33.13700  43.74200  57.40400 1.000 27.53000 ? 389 ARG B NH1 1 
ATOM   6403 N  NH2 . ARG B 1 389 ? 34.44900  44.12600  55.55200 1.000 27.18000 ? 389 ARG B NH2 1 
ATOM   6404 N  N   . GLU B 1 390 ? 39.59400  44.14500  61.87500 1.000 26.37000 ? 390 GLU B N   1 
ATOM   6405 C  CA  . GLU B 1 390 ? 40.81500  44.82800  61.45700 1.000 25.42000 ? 390 GLU B CA  1 
ATOM   6406 C  C   . GLU B 1 390 ? 41.99500  43.86800  61.41900 1.000 24.17000 ? 390 GLU B C   1 
ATOM   6407 O  O   . GLU B 1 390 ? 42.91100  44.04100  60.60700 1.000 27.02000 ? 390 GLU B O   1 
ATOM   6408 C  CB  . GLU B 1 390 ? 41.11500  46.00600  62.39500 1.000 29.38000 ? 390 GLU B CB  1 
ATOM   6409 C  CG  . GLU B 1 390 ? 41.21400  45.61400  63.87100 1.000 34.86000 ? 390 GLU B CG  1 
ATOM   6410 C  CD  . GLU B 1 390 ? 40.07700  46.16400  64.71800 1.000 42.86000 ? 390 GLU B CD  1 
ATOM   6411 O  OE1 . GLU B 1 390 ? 38.89900  45.92000  64.36700 1.000 45.28000 ? 390 GLU B OE1 1 
ATOM   6412 O  OE2 . GLU B 1 390 ? 40.35700  46.81600  65.74800 1.000 49.00000 ? 390 GLU B OE2 1 
ATOM   6413 N  N   . GLU B 1 391 ? 41.98600  42.84200  62.26900 1.000 22.60000 ? 391 GLU B N   1 
ATOM   6414 C  CA  . GLU B 1 391 ? 43.05600  41.85500  62.31500 1.000 24.86000 ? 391 GLU B CA  1 
ATOM   6415 C  C   . GLU B 1 391 ? 42.74300  40.60600  61.50000 1.000 23.72000 ? 391 GLU B C   1 
ATOM   6416 O  O   . GLU B 1 391 ? 43.56300  39.68600  61.46500 1.000 22.01000 ? 391 GLU B O   1 
ATOM   6417 C  CB  . GLU B 1 391 ? 43.34400  41.49000  63.77600 1.000 24.78000 ? 391 GLU B CB  1 
ATOM   6418 C  CG  . GLU B 1 391 ? 43.33300  42.72700  64.65800 1.000 29.73000 ? 391 GLU B CG  1 
ATOM   6419 C  CD  . GLU B 1 391 ? 43.92500  42.51000  66.03400 1.000 38.36000 ? 391 GLU B CD  1 
ATOM   6420 O  OE1 . GLU B 1 391 ? 43.95600  41.35600  66.50900 1.000 41.73000 ? 391 GLU B OE1 1 
ATOM   6421 O  OE2 . GLU B 1 391 ? 44.36400  43.50900  66.64000 1.000 42.92000 ? 391 GLU B OE2 1 
ATOM   6422 N  N   . ALA B 1 392 ? 41.60400  40.58300  60.80400 1.000 24.41000 ? 392 ALA B N   1 
ATOM   6423 C  CA  . ALA B 1 392 ? 41.10400  39.39400  60.13000 1.000 23.99000 ? 392 ALA B CA  1 
ATOM   6424 C  C   . ALA B 1 392 ? 41.20800  39.46800  58.60800 1.000 22.92000 ? 392 ALA B C   1 
ATOM   6425 O  O   . ALA B 1 392 ? 40.83700  38.50500  57.92200 1.000 21.84000 ? 392 ALA B O   1 
ATOM   6426 C  CB  . ALA B 1 392 ? 39.64600  39.15400  60.54500 1.000 19.02000 ? 392 ALA B CB  1 
ATOM   6427 N  N   . THR B 1 393 ? 41.70100  40.57300  58.06200 1.000 20.61000 ? 393 THR B N   1 
ATOM   6428 C  CA  . THR B 1 393 ? 41.76500  40.75500  56.62000 1.000 21.11000 ? 393 THR B CA  1 
ATOM   6429 C  C   . THR B 1 393 ? 42.89600  39.92500  56.01600 1.000 20.66000 ? 393 THR B C   1 
ATOM   6430 O  O   . THR B 1 393 ? 43.79800  39.45500  56.71600 1.000 17.37000 ? 393 THR B O   1 
ATOM   6431 C  CB  . THR B 1 393 ? 41.97100  42.23400  56.27300 1.000 22.69000 ? 393 THR B CB  1 
ATOM   6432 O  OG1 . THR B 1 393 ? 43.28200  42.64200  56.70700 1.000 24.01000 ? 393 THR B OG1 1 
ATOM   6433 C  CG2 . THR B 1 393 ? 40.90200  43.10800  56.95000 1.000 20.07000 ? 393 THR B CG2 1 
ATOM   6434 N  N   . VAL B 1 394 ? 42.82100  39.74300  54.69000 1.000 18.80000 ? 394 VAL B N   1 
ATOM   6435 C  CA  . VAL B 1 394 ? 43.90100  39.11500  53.92800 1.000 18.57000 ? 394 VAL B CA  1 
ATOM   6436 C  C   . VAL B 1 394 ? 45.24400  39.73200  54.29800 1.000 21.36000 ? 394 VAL B C   1 
ATOM   6437 O  O   . VAL B 1 394 ? 46.22200  39.02500  54.56700 1.000 22.73000 ? 394 VAL B O   1 
ATOM   6438 C  CB  . VAL B 1 394 ? 43.62800  39.24100  52.41600 1.000 18.59000 ? 394 VAL B CB  1 
ATOM   6439 C  CG1 . VAL B 1 394 ? 44.88800  39.02300  51.61300 1.000 19.49000 ? 394 VAL B CG1 1 
ATOM   6440 C  CG2 . VAL B 1 394 ? 42.54900  38.25400  51.97800 1.000 20.33000 ? 394 VAL B CG2 1 
ATOM   6441 N  N   . GLY B 1 395 ? 45.31100  41.06300  54.30300 1.000 21.30000 ? 395 GLY B N   1 
ATOM   6442 C  CA  . GLY B 1 395 ? 46.57900  41.72400  54.57200 1.000 19.40000 ? 395 GLY B CA  1 
ATOM   6443 C  C   . GLY B 1 395 ? 47.04800  41.52300  55.99900 1.000 19.27000 ? 395 GLY B C   1 
ATOM   6444 O  O   . GLY B 1 395 ? 48.23600  41.29300  56.24400 1.000 21.56000 ? 395 GLY B O   1 
ATOM   6445 N  N   . ALA B 1 396 ? 46.12400  41.60100  56.96200 1.000 18.15000 ? 396 ALA B N   1 
ATOM   6446 C  CA  . ALA B 1 396 ? 46.50800  41.45700  58.36300 1.000 21.93000 ? 396 ALA B CA  1 
ATOM   6447 C  C   . ALA B 1 396 ? 46.97100  40.03700  58.67300 1.000 23.49000 ? 396 ALA B C   1 
ATOM   6448 O  O   . ALA B 1 396 ? 47.95100  39.84300  59.40300 1.000 23.28000 ? 396 ALA B O   1 
ATOM   6449 C  CB  . ALA B 1 396 ? 45.34500  41.84900  59.27500 1.000 18.99000 ? 396 ALA B CB  1 
ATOM   6450 N  N   . LEU B 1 397 ? 46.27100  39.02900  58.14500 1.000 23.15000 ? 397 LEU B N   1 
ATOM   6451 C  CA  . LEU B 1 397 ? 46.71100  37.65100  58.34700 1.000 18.09000 ? 397 LEU B CA  1 
ATOM   6452 C  C   . LEU B 1 397 ? 48.04200  37.39100  57.66400 1.000 20.05000 ? 397 LEU B C   1 
ATOM   6453 O  O   . LEU B 1 397 ? 48.92500  36.74000  58.23500 1.000 22.27000 ? 397 LEU B O   1 
ATOM   6454 C  CB  . LEU B 1 397 ? 45.65600  36.67300  57.83200 1.000 19.29000 ? 397 LEU B CB  1 
ATOM   6455 C  CG  . LEU B 1 397 ? 44.29200  36.71600  58.52700 1.000 20.13000 ? 397 LEU B CG  1 
ATOM   6456 C  CD1 . LEU B 1 397 ? 43.30200  35.86300  57.75600 1.000 21.73000 ? 397 LEU B CD1 1 
ATOM   6457 C  CD2 . LEU B 1 397 ? 44.37600  36.25700  59.97900 1.000 20.43000 ? 397 LEU B CD2 1 
ATOM   6458 N  N   . ARG B 1 398 ? 48.21000  37.88000  56.43500 1.000 17.27000 ? 398 ARG B N   1 
ATOM   6459 C  CA  . ARG B 1 398 ? 49.46600  37.62200  55.74500 1.000 21.03000 ? 398 ARG B CA  1 
ATOM   6460 C  C   . ARG B 1 398 ? 50.64300  38.26200  56.47500 1.000 23.39000 ? 398 ARG B C   1 
ATOM   6461 O  O   . ARG B 1 398 ? 51.76800  37.75100  56.40600 1.000 26.33000 ? 398 ARG B O   1 
ATOM   6462 C  CB  . ARG B 1 398 ? 49.37600  38.10800  54.29900 1.000 22.53000 ? 398 ARG B CB  1 
ATOM   6463 C  CG  . ARG B 1 398 ? 48.67700  37.10500  53.38200 1.000 21.80000 ? 398 ARG B CG  1 
ATOM   6464 C  CD  . ARG B 1 398 ? 48.51300  37.65000  51.98300 1.000 21.42000 ? 398 ARG B CD  1 
ATOM   6465 N  NE  . ARG B 1 398 ? 48.38200  36.58200  51.00300 1.000 18.68000 ? 398 ARG B NE  1 
ATOM   6466 C  CZ  . ARG B 1 398 ? 48.04500  36.78500  49.73500 1.000 18.81000 ? 398 ARG B CZ  1 
ATOM   6467 N  NH1 . ARG B 1 398 ? 47.80600  38.01400  49.30600 1.000 21.42000 ? 398 ARG B NH1 1 
ATOM   6468 N  NH2 . ARG B 1 398 ? 47.96000  35.76600  48.89700 1.000 20.57000 ? 398 ARG B NH2 1 
ATOM   6469 N  N   . ALA B 1 399 ? 50.40100  39.34900  57.21100 1.000 23.96000 ? 399 ALA B N   1 
ATOM   6470 C  CA  . ALA B 1 399 ? 51.47800  39.94200  57.99200 1.000 27.17000 ? 399 ALA B CA  1 
ATOM   6471 C  C   . ALA B 1 399 ? 51.93800  39.02200  59.11600 1.000 28.12000 ? 399 ALA B C   1 
ATOM   6472 O  O   . ALA B 1 399 ? 53.04600  39.20300  59.62800 1.000 25.07000 ? 399 ALA B O   1 
ATOM   6473 C  CB  . ALA B 1 399 ? 51.04500  41.30400  58.55300 1.000 22.44000 ? 399 ALA B CB  1 
ATOM   6474 N  N   . ARG B 1 400 ? 51.11700  38.04000  59.50900 1.000 24.41000 ? 400 ARG B N   1 
ATOM   6475 C  CA  . ARG B 1 400 ? 51.53600  37.05200  60.49300 1.000 23.61000 ? 400 ARG B CA  1 
ATOM   6476 C  C   . ARG B 1 400 ? 52.50100  36.02100  59.92700 1.000 23.43000 ? 400 ARG B C   1 
ATOM   6477 O  O   . ARG B 1 400 ? 53.09400  35.27000  60.70600 1.000 26.41000 ? 400 ARG B O   1 
ATOM   6478 C  CB  . ARG B 1 400 ? 50.33500  36.28800  61.05700 1.000 23.32000 ? 400 ARG B CB  1 
ATOM   6479 C  CG  . ARG B 1 400 ? 49.24400  37.13000  61.71400 1.000 25.12000 ? 400 ARG B CG  1 
ATOM   6480 C  CD  . ARG B 1 400 ? 48.23800  36.20900  62.40700 1.000 25.21000 ? 400 ARG B CD  1 
ATOM   6481 N  NE  . ARG B 1 400 ? 47.16500  36.96000  63.05300 1.000 33.38000 ? 400 ARG B NE  1 
ATOM   6482 C  CZ  . ARG B 1 400 ? 46.17000  36.40500  63.73700 1.000 37.89000 ? 400 ARG B CZ  1 
ATOM   6483 N  NH1 . ARG B 1 400 ? 46.11200  35.08600  63.87000 1.000 34.89000 ? 400 ARG B NH1 1 
ATOM   6484 N  NH2 . ARG B 1 400 ? 45.23700  37.16800  64.29600 1.000 33.90000 ? 400 ARG B NH2 1 
ATOM   6485 N  N   . ALA B 1 401 ? 52.63700  35.93300  58.60700 1.000 21.11000 ? 401 ALA B N   1 
ATOM   6486 C  CA  . ALA B 1 401 ? 53.23200  34.76200  57.98000 1.000 24.74000 ? 401 ALA B CA  1 
ATOM   6487 C  C   . ALA B 1 401 ? 54.29300  35.13000  56.95300 1.000 25.56000 ? 401 ALA B C   1 
ATOM   6488 O  O   . ALA B 1 401 ? 54.51600  34.37600  55.99500 1.000 22.76000 ? 401 ALA B O   1 
ATOM   6489 C  CB  . ALA B 1 401 ? 52.15500  33.89900  57.32200 1.000 27.82000 ? 401 ALA B CB  1 
ATOM   6490 N  N   . THR B 1 402 ? 54.96100  36.27600  57.12700 1.000 26.86000 ? 402 THR B N   1 
ATOM   6491 C  CA  . THR B 1 402 ? 55.96800  36.67700  56.14700 1.000 24.47000 ? 402 THR B CA  1 
ATOM   6492 C  C   . THR B 1 402 ? 57.15100  35.71900  56.11900 1.000 29.04000 ? 402 THR B C   1 
ATOM   6493 O  O   . THR B 1 402 ? 57.85900  35.65400  55.11000 1.000 28.72000 ? 402 THR B O   1 
ATOM   6494 C  CB  . THR B 1 402 ? 56.46700  38.11000  56.41600 1.000 30.47000 ? 402 THR B CB  1 
ATOM   6495 O  OG1 . THR B 1 402 ? 56.97600  38.21300  57.74900 1.000 30.41000 ? 402 THR B OG1 1 
ATOM   6496 C  CG2 . THR B 1 402 ? 55.34600  39.13400  56.22700 1.000 27.14000 ? 402 THR B CG2 1 
ATOM   6497 N  N   . ASP B 1 403 ? 57.37600  34.98100  57.20000 1.000 22.25000 ? 403 ASP B N   1 
ATOM   6498 C  CA  . ASP B 1 403 ? 58.45000  34.00200  57.30000 1.000 26.94000 ? 403 ASP B CA  1 
ATOM   6499 C  C   . ASP B 1 403 ? 58.04100  32.60900  56.83600 1.000 27.99000 ? 403 ASP B C   1 
ATOM   6500 O  O   . ASP B 1 403 ? 58.85400  31.68400  56.92900 1.000 31.77000 ? 403 ASP B O   1 
ATOM   6501 C  CB  . ASP B 1 403 ? 58.92600  33.91400  58.75100 1.000 32.69000 ? 403 ASP B CB  1 
ATOM   6502 C  CG  . ASP B 1 403 ? 57.81500  33.46500  59.68900 1.000 34.50000 ? 403 ASP B CG  1 
ATOM   6503 O  OD1 . ASP B 1 403 ? 56.69100  34.00700  59.58500 1.000 37.27000 ? 403 ASP B OD1 1 
ATOM   6504 O  OD2 . ASP B 1 403 ? 58.05000  32.56400  60.51400 1.000 36.83000 ? 403 ASP B OD2 1 
ATOM   6505 N  N   . VAL B 1 404 ? 56.81100  32.42600  56.36200 1.000 30.01000 ? 404 VAL B N   1 
ATOM   6506 C  CA  . VAL B 1 404 ? 56.33400  31.10700  55.95500 1.000 23.32000 ? 404 VAL B CA  1 
ATOM   6507 C  C   . VAL B 1 404 ? 56.75500  30.85500  54.51700 1.000 24.80000 ? 404 VAL B C   1 
ATOM   6508 O  O   . VAL B 1 404 ? 56.36700  31.59400  53.60700 1.000 23.65000 ? 404 VAL B O   1 
ATOM   6509 C  CB  . VAL B 1 404 ? 54.81200  30.99000  56.10800 1.000 22.70000 ? 404 VAL B CB  1 
ATOM   6510 C  CG1 . VAL B 1 404 ? 54.32600  29.68300  55.48600 1.000 23.63000 ? 404 VAL B CG1 1 
ATOM   6511 C  CG2 . VAL B 1 404 ? 54.41500  31.06300  57.58500 1.000 23.23000 ? 404 VAL B CG2 1 
ATOM   6512 N  N   . ASP B 1 405 ? 57.55000  29.81100  54.31200 1.000 22.91000 ? 405 ASP B N   1 
ATOM   6513 C  CA  . ASP B 1 405 ? 58.00200  29.44200  52.98000 1.000 26.38000 ? 405 ASP B CA  1 
ATOM   6514 C  C   . ASP B 1 405 ? 56.85400  28.80200  52.21600 1.000 21.80000 ? 405 ASP B C   1 
ATOM   6515 O  O   . ASP B 1 405 ? 56.31900  27.77200  52.64100 1.000 25.35000 ? 405 ASP B O   1 
ATOM   6516 C  CB  . ASP B 1 405 ? 59.18000  28.47700  53.08000 1.000 25.44000 ? 405 ASP B CB  1 
ATOM   6517 C  CG  . ASP B 1 405 ? 59.85900  28.24000  51.74600 1.000 30.55000 ? 405 ASP B CG  1 
ATOM   6518 O  OD1 . ASP B 1 405 ? 59.17200  27.95700  50.74300 1.000 22.82000 ? 405 ASP B OD1 1 
ATOM   6519 O  OD2 . ASP B 1 405 ? 61.10100  28.34600  51.69900 1.000 37.00000 ? 405 ASP B OD2 1 
ATOM   6520 N  N   . ILE B 1 406 ? 56.48100  29.39600  51.08700 1.000 21.43000 ? 406 ILE B N   1 
ATOM   6521 C  CA  . ILE B 1 406 ? 55.41200  28.84700  50.26400 1.000 21.51000 ? 406 ILE B CA  1 
ATOM   6522 C  C   . ILE B 1 406 ? 55.91600  28.43900  48.87600 1.000 25.31000 ? 406 ILE B C   1 
ATOM   6523 O  O   . ILE B 1 406 ? 55.12500  28.25900  47.96000 1.000 25.28000 ? 406 ILE B O   1 
ATOM   6524 C  CB  . ILE B 1 406 ? 54.23100  29.83000  50.16500 1.000 20.74000 ? 406 ILE B CB  1 
ATOM   6525 C  CG1 . ILE B 1 406 ? 54.68800  31.17000  49.58900 1.000 23.44000 ? 406 ILE B CG1 1 
ATOM   6526 C  CG2 . ILE B 1 406 ? 53.59600  30.02800  51.52000 1.000 18.27000 ? 406 ILE B CG2 1 
ATOM   6527 C  CD1 . ILE B 1 406 ? 53.63700  31.84000  48.75100 1.000 26.20000 ? 406 ILE B CD1 1 
ATOM   6528 N  N   . SER B 1 407 ? 57.22400  28.26700  48.71300 1.000 23.35000 ? 407 SER B N   1 
ATOM   6529 C  CA  . SER B 1 407 ? 57.75500  27.88600  47.41500 1.000 23.78000 ? 407 SER B CA  1 
ATOM   6530 C  C   . SER B 1 407 ? 57.45100  26.41800  47.11700 1.000 25.86000 ? 407 SER B C   1 
ATOM   6531 O  O   . SER B 1 407 ? 57.19500  25.61300  48.01900 1.000 23.07000 ? 407 SER B O   1 
ATOM   6532 C  CB  . SER B 1 407 ? 59.26300  28.11900  47.36900 1.000 26.42000 ? 407 SER B CB  1 
ATOM   6533 O  OG  . SER B 1 407 ? 59.90100  27.33100  48.35300 1.000 23.78000 ? 407 SER B OG  1 
ATOM   6534 N  N   . GLU B 1 408 ? 57.48800  26.07500  45.82400 1.000 22.84000 ? 408 GLU B N   1 
ATOM   6535 C  CA  . GLU B 1 408 ? 57.33000  24.68800  45.39800 1.000 20.94000 ? 408 GLU B CA  1 
ATOM   6536 C  C   . GLU B 1 408 ? 58.32500  23.79200  46.11800 1.000 22.05000 ? 408 GLU B C   1 
ATOM   6537 O  O   . GLU B 1 408 ? 59.51700  24.10000  46.20000 1.000 18.66000 ? 408 GLU B O   1 
ATOM   6538 C  CB  . GLU B 1 408 ? 57.53300  24.55500  43.88200 1.000 24.09000 ? 408 GLU B CB  1 
ATOM   6539 C  CG  . GLU B 1 408 ? 56.25400  24.66600  43.07900 1.000 30.74000 ? 408 GLU B CG  1 
ATOM   6540 C  CD  . GLU B 1 408 ? 56.34300  24.02500  41.70700 1.000 22.85000 ? 408 GLU B CD  1 
ATOM   6541 O  OE1 . GLU B 1 408 ? 57.40900  23.49000  41.34800 1.000 30.18000 ? 408 GLU B OE1 1 
ATOM   6542 O  OE2 . GLU B 1 408 ? 55.33000  24.05000  40.98700 1.000 30.33000 ? 408 GLU B OE2 1 
ATOM   6543 N  N   . THR B 1 409 ? 57.83700  22.65700  46.61200 1.000 18.41000 ? 409 THR B N   1 
ATOM   6544 C  CA  . THR B 1 409 ? 58.66400  21.73500  47.38300 1.000 19.74000 ? 409 THR B CA  1 
ATOM   6545 C  C   . THR B 1 409 ? 58.27000  20.31500  47.01700 1.000 19.95000 ? 409 THR B C   1 
ATOM   6546 O  O   . THR B 1 409 ? 57.10900  19.92900  47.16800 1.000 18.11000 ? 409 THR B O   1 
ATOM   6547 C  CB  . THR B 1 409 ? 58.50100  21.98500  48.88900 1.000 21.15000 ? 409 THR B CB  1 
ATOM   6548 O  OG1 . THR B 1 409 ? 58.93200  23.31400  49.19800 1.000 18.67000 ? 409 THR B OG1 1 
ATOM   6549 C  CG2 . THR B 1 409 ? 59.32400  20.99900  49.70000 1.000 21.08000 ? 409 THR B CG2 1 
ATOM   6550 N  N   . SER B 1 410 ? 59.22200  19.54200  46.51500 1.000 19.65000 ? 410 SER B N   1 
ATOM   6551 C  CA  . SER B 1 410 ? 58.88500  18.19800  46.08700 1.000 17.06000 ? 410 SER B CA  1 
ATOM   6552 C  C   . SER B 1 410 ? 58.50300  17.33800  47.28100 1.000 18.80000 ? 410 SER B C   1 
ATOM   6553 O  O   . SER B 1 410 ? 58.94200  17.56900  48.41000 1.000 17.33000 ? 410 SER B O   1 
ATOM   6554 C  CB  . SER B 1 410 ? 60.05800  17.55700  45.35600 1.000 20.12000 ? 410 SER B CB  1 
ATOM   6555 O  OG  . SER B 1 410 ? 59.93800  16.14800  45.32900 1.000 17.09000 ? 410 SER B OG  1 
ATOM   6556 N  N   . LYS B 1 411 ? 57.70500  16.30100  47.01300 1.000 18.40000 ? 411 LYS B N   1 
ATOM   6557 C  CA  . LYS B 1 411 ? 57.35100  15.37800  48.08900 1.000 21.04000 ? 411 LYS B CA  1 
ATOM   6558 C  C   . LYS B 1 411 ? 58.57500  14.62300  48.60200 1.000 19.93000 ? 411 LYS B C   1 
ATOM   6559 O  O   . LYS B 1 411 ? 58.56800  14.14300  49.74300 1.000 20.31000 ? 411 LYS B O   1 
ATOM   6560 C  CB  . LYS B 1 411 ? 56.28700  14.38200  47.61700 1.000 22.66000 ? 411 LYS B CB  1 
ATOM   6561 C  CG  . LYS B 1 411 ? 56.79300  13.38900  46.58600 1.000 22.92000 ? 411 LYS B CG  1 
ATOM   6562 C  CD  . LYS B 1 411 ? 55.69200  12.45900  46.07900 1.000 24.33000 ? 411 LYS B CD  1 
ATOM   6563 C  CE  . LYS B 1 411 ? 54.57300  13.23800  45.42800 1.000 20.82000 ? 411 LYS B CE  1 
ATOM   6564 N  NZ  . LYS B 1 411 ? 53.70700  12.30600  44.63200 1.000 26.27000 ? 411 LYS B NZ  1 
ATOM   6565 N  N   . GLU B 1 412 ? 59.62700  14.50100  47.78200 1.000 19.37000 ? 412 GLU B N   1 
ATOM   6566 C  CA  . GLU B 1 412 ? 60.84300  13.84500  48.24900 1.000 20.53000 ? 412 GLU B CA  1 
ATOM   6567 C  C   . GLU B 1 412 ? 61.56600  14.68900  49.28900 1.000 19.23000 ? 412 GLU B C   1 
ATOM   6568 O  O   . GLU B 1 412 ? 62.21900  14.14000  50.18700 1.000 20.34000 ? 412 GLU B O   1 
ATOM   6569 C  CB  . GLU B 1 412 ? 61.76300  13.53800  47.06600 1.000 24.09000 ? 412 GLU B CB  1 
ATOM   6570 C  CG  . GLU B 1 412 ? 61.15800  12.55200  46.08000 1.000 22.60000 ? 412 GLU B CG  1 
ATOM   6571 C  CD  . GLU B 1 412 ? 60.70600  11.26000  46.75500 1.000 31.43000 ? 412 GLU B CD  1 
ATOM   6572 O  OE1 . GLU B 1 412 ? 61.42800  10.76200  47.65200 1.000 34.46000 ? 412 GLU B OE1 1 
ATOM   6573 O  OE2 . GLU B 1 412 ? 59.63400  10.73800  46.38500 1.000 31.13000 ? 412 GLU B OE2 1 
ATOM   6574 N  N   . GLU B 1 413 ? 61.45500  16.01400  49.19700 1.000 20.06000 ? 413 GLU B N   1 
ATOM   6575 C  CA  . GLU B 1 413 ? 62.07500  16.87300  50.20100 1.000 18.15000 ? 413 GLU B CA  1 
ATOM   6576 C  C   . GLU B 1 413 ? 61.27800  16.87200  51.50700 1.000 21.82000 ? 413 GLU B C   1 
ATOM   6577 O  O   . GLU B 1 413 ? 61.86400  16.90200  52.59700 1.000 20.75000 ? 413 GLU B O   1 
ATOM   6578 C  CB  . GLU B 1 413 ? 62.23000  18.29200  49.64600 1.000 20.95000 ? 413 GLU B CB  1 
ATOM   6579 C  CG  . GLU B 1 413 ? 62.68700  19.35200  50.65400 1.000 20.63000 ? 413 GLU B CG  1 
ATOM   6580 C  CD  . GLU B 1 413 ? 64.05900  19.06800  51.28100 1.000 24.48000 ? 413 GLU B CD  1 
ATOM   6581 O  OE1 . GLU B 1 413 ? 64.82400  18.21600  50.76800 1.000 21.38000 ? 413 GLU B OE1 1 
ATOM   6582 O  OE2 . GLU B 1 413 ? 64.37300  19.71700  52.29900 1.000 23.99000 ? 413 GLU B OE2 1 
ATOM   6583 N  N   . TYR B 1 414 ? 59.94100  16.85100  51.43000 1.000 19.14000 ? 414 TYR B N   1 
ATOM   6584 C  CA  . TYR B 1 414 ? 59.16500  16.66400  52.65500 1.000 16.85000 ? 414 TYR B CA  1 
ATOM   6585 C  C   . TYR B 1 414 ? 59.51200  15.33400  53.30600 1.000 18.26000 ? 414 TYR B C   1 
ATOM   6586 O  O   . TYR B 1 414 ? 59.65000  15.24900  54.53200 1.000 16.39000 ? 414 TYR B O   1 
ATOM   6587 C  CB  . TYR B 1 414 ? 57.65400  16.75600  52.36900 1.000 15.66000 ? 414 TYR B CB  1 
ATOM   6588 C  CG  . TYR B 1 414 ? 57.19800  18.17800  52.08400 1.000 14.95000 ? 414 TYR B CG  1 
ATOM   6589 C  CD1 . TYR B 1 414 ? 57.42400  19.19600  53.00600 1.000 17.47000 ? 414 TYR B CD1 1 
ATOM   6590 C  CD2 . TYR B 1 414 ? 56.55400  18.50000  50.88900 1.000 16.18000 ? 414 TYR B CD2 1 
ATOM   6591 C  CE1 . TYR B 1 414 ? 57.03600  20.50000  52.74700 1.000 16.70000 ? 414 TYR B CE1 1 
ATOM   6592 C  CE2 . TYR B 1 414 ? 56.15500  19.80200  50.61600 1.000 15.17000 ? 414 TYR B CE2 1 
ATOM   6593 C  CZ  . TYR B 1 414 ? 56.39300  20.79300  51.55100 1.000 18.52000 ? 414 TYR B CZ  1 
ATOM   6594 O  OH  . TYR B 1 414 ? 56.00300  22.07900  51.28900 1.000 16.70000 ? 414 TYR B OH  1 
ATOM   6595 N  N   . ARG B 1 415 ? 59.68000  14.28700  52.49600 1.000 18.91000 ? 415 ARG B N   1 
ATOM   6596 C  CA  . ARG B 1 415 ? 60.07800  12.99600  53.04400 1.000 20.97000 ? 415 ARG B CA  1 
ATOM   6597 C  C   . ARG B 1 415 ? 61.44300  13.07400  53.72200 1.000 20.27000 ? 415 ARG B C   1 
ATOM   6598 O  O   . ARG B 1 415 ? 61.62400  12.53600  54.82000 1.000 21.14000 ? 415 ARG B O   1 
ATOM   6599 C  CB  . ARG B 1 415 ? 60.07400  11.92700  51.94900 1.000 16.48000 ? 415 ARG B CB  1 
ATOM   6600 C  CG  . ARG B 1 415 ? 60.54500  10.57900  52.42900 1.000 20.79000 ? 415 ARG B CG  1 
ATOM   6601 C  CD  . ARG B 1 415 ? 60.48700  9.52900   51.33300 1.000 25.15000 ? 415 ARG B CD  1 
ATOM   6602 N  NE  . ARG B 1 415 ? 59.12800  9.25600   50.87600 1.000 24.37000 ? 415 ARG B NE  1 
ATOM   6603 C  CZ  . ARG B 1 415 ? 58.27500  8.44800   51.49700 1.000 28.55000 ? 415 ARG B CZ  1 
ATOM   6604 N  NH1 . ARG B 1 415 ? 58.63500  7.83400   52.61900 1.000 26.25000 ? 415 ARG B NH1 1 
ATOM   6605 N  NH2 . ARG B 1 415 ? 57.06000  8.25300   50.99900 1.000 23.08000 ? 415 ARG B NH2 1 
ATOM   6606 N  N   . ARG B 1 416 ? 62.41200  13.74600  53.09300 1.000 20.59000 ? 416 ARG B N   1 
ATOM   6607 C  CA  . ARG B 1 416 ? 63.72800  13.89900  53.71800 1.000 22.04000 ? 416 ARG B CA  1 
ATOM   6608 C  C   . ARG B 1 416 ? 63.60900  14.57700  55.07500 1.000 23.96000 ? 416 ARG B C   1 
ATOM   6609 O  O   . ARG B 1 416 ? 64.18500  14.11700  56.06900 1.000 25.22000 ? 416 ARG B O   1 
ATOM   6610 C  CB  . ARG B 1 416 ? 64.66900  14.69100  52.80100 1.000 21.29000 ? 416 ARG B CB  1 
ATOM   6611 C  CG  . ARG B 1 416 ? 66.10700  14.84800  53.34200 1.000 26.27000 ? 416 ARG B CG  1 
ATOM   6612 C  CD  . ARG B 1 416 ? 66.93400  15.89100  52.54200 1.000 20.75000 ? 416 ARG B CD  1 
ATOM   6613 N  NE  . ARG B 1 416 ? 66.51800  17.27500  52.80900 1.000 21.57000 ? 416 ARG B NE  1 
ATOM   6614 C  CZ  . ARG B 1 416 ? 66.84400  17.97100  53.89700 1.000 21.53000 ? 416 ARG B CZ  1 
ATOM   6615 N  NH1 . ARG B 1 416 ? 67.60200  17.43300  54.84700 1.000 23.77000 ? 416 ARG B NH1 1 
ATOM   6616 N  NH2 . ARG B 1 416 ? 66.40600  19.21300  54.04600 1.000 20.43000 ? 416 ARG B NH2 1 
ATOM   6617 N  N   . ARG B 1 417 ? 62.85100  15.67100  55.13800 1.000 19.62000 ? 417 ARG B N   1 
ATOM   6618 C  CA  . ARG B 1 417 ? 62.67600  16.36400  56.40400 1.000 24.54000 ? 417 ARG B CA  1 
ATOM   6619 C  C   . ARG B 1 417 ? 61.91700  15.49200  57.39600 1.000 24.14000 ? 417 ARG B C   1 
ATOM   6620 O  O   . ARG B 1 417 ? 62.26500  15.43600  58.58200 1.000 24.44000 ? 417 ARG B O   1 
ATOM   6621 C  CB  . ARG B 1 417 ? 61.94800  17.68700  56.18300 1.000 19.23000 ? 417 ARG B CB  1 
ATOM   6622 C  CG  . ARG B 1 417 ? 62.58600  18.62300  55.16300 1.000 20.45000 ? 417 ARG B CG  1 
ATOM   6623 C  CD  . ARG B 1 417 ? 61.71700  19.85800  54.96600 1.000 25.06000 ? 417 ARG B CD  1 
ATOM   6624 N  NE  . ARG B 1 417 ? 62.20800  20.72400  53.89100 1.000 25.69000 ? 417 ARG B NE  1 
ATOM   6625 C  CZ  . ARG B 1 417 ? 61.51200  21.73400  53.37800 1.000 27.85000 ? 417 ARG B CZ  1 
ATOM   6626 N  NH1 . ARG B 1 417 ? 60.29100  22.00300  53.83700 1.000 24.99000 ? 417 ARG B NH1 1 
ATOM   6627 N  NH2 . ARG B 1 417 ? 62.02900  22.47400  52.40700 1.000 23.31000 ? 417 ARG B NH2 1 
ATOM   6628 N  N   . TYR B 1 418 ? 60.89100  14.78600  56.91700 1.000 23.14000 ? 418 TYR B N   1 
ATOM   6629 C  CA  . TYR B 1 418 ? 60.07600  13.94700  57.79000 1.000 22.68000 ? 418 TYR B CA  1 
ATOM   6630 C  C   . TYR B 1 418 ? 60.91200  12.84600  58.42300 1.000 29.06000 ? 418 TYR B C   1 
ATOM   6631 O  O   . TYR B 1 418 ? 60.79800  12.58200  59.62500 1.000 30.06000 ? 418 TYR B O   1 
ATOM   6632 C  CB  . TYR B 1 418 ? 58.92300  13.34100  56.99000 1.000 23.56000 ? 418 TYR B CB  1 
ATOM   6633 C  CG  . TYR B 1 418 ? 57.87900  12.58800  57.79400 1.000 24.99000 ? 418 TYR B CG  1 
ATOM   6634 C  CD1 . TYR B 1 418 ? 56.77100  13.24500  58.31400 1.000 25.55000 ? 418 TYR B CD1 1 
ATOM   6635 C  CD2 . TYR B 1 418 ? 57.97900  11.21400  57.99200 1.000 26.70000 ? 418 TYR B CD2 1 
ATOM   6636 C  CE1 . TYR B 1 418 ? 55.80300  12.55900  59.04100 1.000 25.18000 ? 418 TYR B CE1 1 
ATOM   6637 C  CE2 . TYR B 1 418 ? 57.02200  10.51900  58.71100 1.000 24.39000 ? 418 TYR B CE2 1 
ATOM   6638 C  CZ  . TYR B 1 418 ? 55.93500  11.19900  59.23100 1.000 26.79000 ? 418 TYR B CZ  1 
ATOM   6639 O  OH  . TYR B 1 418 ? 54.97200  10.52100  59.93600 1.000 28.02000 ? 418 TYR B OH  1 
ATOM   6640 N  N   . GLU B 1 419 ? 61.76100  12.19500  57.62500 1.000 26.28000 ? 419 GLU B N   1 
ATOM   6641 C  CA  . GLU B 1 419 ? 62.51100  11.04700  58.11500 1.000 30.68000 ? 419 GLU B CA  1 
ATOM   6642 C  C   . GLU B 1 419 ? 63.64700  11.46500  59.04200 1.000 33.52000 ? 419 GLU B C   1 
ATOM   6643 O  O   . GLU B 1 419 ? 63.95500  10.74300  59.99500 1.000 32.53000 ? 419 GLU B O   1 
ATOM   6644 C  CB  . GLU B 1 419 ? 62.99400  10.21400  56.92100 1.000 26.15000 ? 419 GLU B CB  1 
ATOM   6645 C  CG  . GLU B 1 419 ? 61.81300  9.42000   56.31900 1.000 33.94000 ? 419 GLU B CG  1 
ATOM   6646 C  CD  . GLU B 1 419 ? 62.11200  8.69200   55.01900 1.000 37.84000 ? 419 GLU B CD  1 
ATOM   6647 O  OE1 . GLU B 1 419 ? 63.23100  8.83000   54.47700 1.000 29.14000 ? 419 GLU B OE1 1 
ATOM   6648 O  OE2 . GLU B 1 419 ? 61.20000  7.97400   54.53300 1.000 36.13000 ? 419 GLU B OE2 1 
ATOM   6649 N  N   . LEU B 1 420 ? 64.25300  12.63100  58.80900 1.000 31.58000 ? 420 LEU B N   1 
ATOM   6650 C  CA  . LEU B 1 420 ? 65.17200  13.19200  59.79400 1.000 33.73000 ? 420 LEU B CA  1 
ATOM   6651 C  C   . LEU B 1 420 ? 64.47400  13.38300  61.13200 1.000 42.75000 ? 420 LEU B C   1 
ATOM   6652 O  O   . LEU B 1 420 ? 64.99900  13.00300  62.18500 1.000 40.94000 ? 420 LEU B O   1 
ATOM   6653 C  CB  . LEU B 1 420 ? 65.72800  14.52600  59.29800 1.000 30.72000 ? 420 LEU B CB  1 
ATOM   6654 C  CG  . LEU B 1 420 ? 66.99000  14.43800  58.44600 1.000 42.32000 ? 420 LEU B CG  1 
ATOM   6655 C  CD1 . LEU B 1 420 ? 67.48000  15.83100  58.09300 1.000 39.50000 ? 420 LEU B CD1 1 
ATOM   6656 C  CD2 . LEU B 1 420 ? 68.06800  13.63500  59.16900 1.000 35.57000 ? 420 LEU B CD2 1 
ATOM   6657 N  N   . THR B 1 421 ? 63.27700  13.96800  61.09900 1.000 36.31000 ? 421 THR B N   1 
ATOM   6658 C  CA  . THR B 1 421 ? 62.53600  14.25100  62.32200 1.000 43.87000 ? 421 THR B CA  1 
ATOM   6659 C  C   . THR B 1 421 ? 62.18900  12.96800  63.06900 1.000 43.84000 ? 421 THR B C   1 
ATOM   6660 O  O   . THR B 1 421 ? 62.35300  12.87900  64.29200 1.000 49.47000 ? 421 THR B O   1 
ATOM   6661 C  CB  . THR B 1 421 ? 61.27400  15.03300  61.96900 1.000 41.45000 ? 421 THR B CB  1 
ATOM   6662 O  OG1 . THR B 1 421 ? 61.64600  16.32100  61.46100 1.000 42.83000 ? 421 THR B OG1 1 
ATOM   6663 C  CG2 . THR B 1 421 ? 60.37600  15.19000  63.18400 1.000 43.09000 ? 421 THR B CG2 1 
ATOM   6664 N  N   . HIS B 1 422 ? 61.72400  11.96000  62.34500 1.000 40.48000 ? 422 HIS B N   1 
ATOM   6665 C  CA  . HIS B 1 422 ? 61.34700  10.69500  62.94900 1.000 41.31000 ? 422 HIS B CA  1 
ATOM   6666 C  C   . HIS B 1 422 ? 62.44900  9.65000   62.76400 1.000 46.09000 ? 422 HIS B C   1 
ATOM   6667 O  O   . HIS B 1 422 ? 62.19800  8.54200   62.28600 1.000 42.84000 ? 422 HIS B O   1 
ATOM   6668 C  CB  . HIS B 1 422 ? 60.02800  10.21100  62.34800 1.000 38.46000 ? 422 HIS B CB  1 
ATOM   6669 C  CG  . HIS B 1 422 ? 58.89100  11.16600  62.55200 1.000 38.50000 ? 422 HIS B CG  1 
ATOM   6670 N  ND1 . HIS B 1 422 ? 58.81300  12.38300  61.90800 1.000 38.82000 ? 422 HIS B ND1 1 
ATOM   6671 C  CD2 . HIS B 1 422 ? 57.79500  11.09200  63.34500 1.000 36.95000 ? 422 HIS B CD2 1 
ATOM   6672 C  CE1 . HIS B 1 422 ? 57.71400  13.01200  62.28400 1.000 33.51000 ? 422 HIS B CE1 1 
ATOM   6673 N  NE2 . HIS B 1 422 ? 57.07800  12.25100  63.15800 1.000 38.98000 ? 422 HIS B NE2 1 
HETATM 6674 C  C1  . GOL C 2 .   ? 2.08900   4.63100   16.01700 1.000 21.80000 ? 501 GOL A C1  1 
HETATM 6675 O  O1  . GOL C 2 .   ? 0.86300   4.77400   16.65200 1.000 24.17000 ? 501 GOL A O1  1 
HETATM 6676 C  C2  . GOL C 2 .   ? 3.13800   5.30500   16.92100 1.000 24.88000 ? 501 GOL A C2  1 
HETATM 6677 O  O2  . GOL C 2 .   ? 3.11000   4.81700   18.21400 1.000 33.24000 ? 501 GOL A O2  1 
HETATM 6678 C  C3  . GOL C 2 .   ? 4.48700   5.03100   16.24600 1.000 28.72000 ? 501 GOL A C3  1 
HETATM 6679 O  O3  . GOL C 2 .   ? 5.45000   5.66500   17.04200 1.000 26.02000 ? 501 GOL A O3  1 
HETATM 6680 C  C1  . GOL D 2 .   ? 29.05500  -3.24400  18.12200 1.000 42.86000 ? 502 GOL A C1  1 
HETATM 6681 O  O1  . GOL D 2 .   ? 28.32200  -3.42500  16.93400 1.000 37.12000 ? 502 GOL A O1  1 
HETATM 6682 C  C2  . GOL D 2 .   ? 30.37400  -2.55600  17.70700 1.000 37.54000 ? 502 GOL A C2  1 
HETATM 6683 O  O2  . GOL D 2 .   ? 30.15400  -1.61500  16.71900 1.000 37.61000 ? 502 GOL A O2  1 
HETATM 6684 C  C3  . GOL D 2 .   ? 31.27900  -3.69500  17.20300 1.000 43.54000 ? 502 GOL A C3  1 
HETATM 6685 O  O3  . GOL D 2 .   ? 32.57300  -3.17100  17.15400 1.000 41.80000 ? 502 GOL A O3  1 
HETATM 6686 C  C1  . GOL E 2 .   ? 12.63100  5.54800   -3.08800 1.000 37.69000 ? 503 GOL A C1  1 
HETATM 6687 O  O1  . GOL E 2 .   ? 13.58000  6.49800   -3.49000 1.000 44.09000 ? 503 GOL A O1  1 
HETATM 6688 C  C2  . GOL E 2 .   ? 13.40200  4.41000   -2.35500 1.000 31.92000 ? 503 GOL A C2  1 
HETATM 6689 O  O2  . GOL E 2 .   ? 13.17700  4.40300   -0.94700 1.000 24.36000 ? 503 GOL A O2  1 
HETATM 6690 C  C3  . GOL E 2 .   ? 12.98600  3.11900   -3.08500 1.000 30.18000 ? 503 GOL A C3  1 
HETATM 6691 O  O3  . GOL E 2 .   ? 12.55800  2.20600   -2.11300 1.000 40.95000 ? 503 GOL A O3  1 
HETATM 6692 MN MN  . MN  F 3 .   ? 14.39300  17.27000  21.00500 1.000 14.27000 ? 504 MN  A MN  1 
HETATM 6693 MN MN  . MN  G 3 .   ? 12.22900  16.92700  24.13300 0.859 14.44000 ? 505 MN  A MN  1 
HETATM 6694 MG MG  . MG  H 4 .   ? 35.84600  18.24200  0.03500  1.000 19.38000 ? 506 MG  A MG  1 
HETATM 6695 C  C1  . GOL I 2 .   ? 48.54600  8.87900   56.41600 1.000 23.89000 ? 501 GOL B C1  1 
HETATM 6696 O  O1  . GOL I 2 .   ? 49.68300  8.50100   55.70600 1.000 22.02000 ? 501 GOL B O1  1 
HETATM 6697 C  C2  . GOL I 2 .   ? 47.30000  8.49300   55.60900 1.000 26.49000 ? 501 GOL B C2  1 
HETATM 6698 O  O2  . GOL I 2 .   ? 47.47000  8.70500   54.26100 1.000 25.43000 ? 501 GOL B O2  1 
HETATM 6699 C  C3  . GOL I 2 .   ? 46.19100  9.39000   56.20500 1.000 29.80000 ? 501 GOL B C3  1 
HETATM 6700 O  O3  . GOL I 2 .   ? 45.11100  9.42600   55.32500 1.000 26.48000 ? 501 GOL B O3  1 
HETATM 6701 C  C1  . GOL J 2 .   ? 37.84500  11.72500  75.39100 1.000 22.37000 ? 502 GOL B C1  1 
HETATM 6702 O  O1  . GOL J 2 .   ? 37.57000  10.57100  74.67200 1.000 36.28000 ? 502 GOL B O1  1 
HETATM 6703 C  C2  . GOL J 2 .   ? 37.96000  12.86100  74.37100 1.000 36.95000 ? 502 GOL B C2  1 
HETATM 6704 O  O2  . GOL J 2 .   ? 37.33600  12.54700  73.11900 1.000 24.66000 ? 502 GOL B O2  1 
HETATM 6705 C  C3  . GOL J 2 .   ? 37.33400  14.07800  75.12300 1.000 37.59000 ? 502 GOL B C3  1 
HETATM 6706 O  O3  . GOL J 2 .   ? 37.40600  15.20200  74.27200 1.000 39.28000 ? 502 GOL B O3  1 
HETATM 6707 C  C1  . GOL K 2 .   ? 56.44500  19.87100  36.31600 1.000 33.14000 ? 503 GOL B C1  1 
HETATM 6708 O  O1  . GOL K 2 .   ? 55.80400  20.38700  37.47200 1.000 25.93000 ? 503 GOL B O1  1 
HETATM 6709 C  C2  . GOL K 2 .   ? 56.38300  20.86600  35.15300 1.000 29.41000 ? 503 GOL B C2  1 
HETATM 6710 O  O2  . GOL K 2 .   ? 57.50100  20.67800  34.32200 1.000 32.55000 ? 503 GOL B O2  1 
HETATM 6711 C  C3  . GOL K 2 .   ? 56.35800  22.28200  35.82200 1.000 34.55000 ? 503 GOL B C3  1 
HETATM 6712 O  O3  . GOL K 2 .   ? 55.59400  23.14100  35.00500 1.000 38.87000 ? 503 GOL B O3  1 
HETATM 6713 C  C1  . GOL L 2 .   ? 23.91400  25.69100  69.96200 1.000 38.63000 ? 504 GOL B C1  1 
HETATM 6714 O  O1  . GOL L 2 .   ? 24.20000  24.50800  70.64200 1.000 36.37000 ? 504 GOL B O1  1 
HETATM 6715 C  C2  . GOL L 2 .   ? 22.52300  25.49000  69.29600 1.000 37.43000 ? 504 GOL B C2  1 
HETATM 6716 O  O2  . GOL L 2 .   ? 21.71400  24.51100  69.94000 1.000 34.42000 ? 504 GOL B O2  1 
HETATM 6717 C  C3  . GOL L 2 .   ? 21.87100  26.88800  69.33000 1.000 42.67000 ? 504 GOL B C3  1 
HETATM 6718 O  O3  . GOL L 2 .   ? 21.80600  27.31200  68.00000 1.000 45.60000 ? 504 GOL B O3  1 
HETATM 6719 MN MN  . MN  M 3 .   ? 36.16600  20.18200  49.03000 0.980 13.22000 ? 505 MN  B MN  1 
HETATM 6720 MN MN  . MN  N 3 .   ? 38.24700  19.16400  46.05300 0.922 16.20000 ? 506 MN  B MN  1 
HETATM 6721 O  O   . HOH O 5 .   ? 10.38000  44.56800  13.55800 1.000 34.42000 ? 601 HOH A O   1 
HETATM 6722 O  O   . HOH O 5 .   ? 25.19900  40.28900  12.37200 1.000 40.99000 ? 602 HOH A O   1 
HETATM 6723 O  O   . HOH O 5 .   ? -7.58400  7.86400   23.72200 1.000 26.98000 ? 603 HOH A O   1 
HETATM 6724 O  O   . HOH O 5 .   ? 10.50000  -1.45300  43.78600 1.000 34.80000 ? 604 HOH A O   1 
HETATM 6725 O  O   . HOH O 5 .   ? 14.05000  28.20900  5.26500  1.000 31.62000 ? 605 HOH A O   1 
HETATM 6726 O  O   . HOH O 5 .   ? 4.55500   33.41800  4.03100  1.000 28.18000 ? 606 HOH A O   1 
HETATM 6727 O  O   . HOH O 5 .   ? 8.200     48.172    17.493   1.000 34.61000 ? 607 HOH A O   1 
HETATM 6728 O  O   . HOH O 5 .   ? 19.31900  32.16700  -1.46000 1.000 30.49000 ? 608 HOH A O   1 
HETATM 6729 O  O   . HOH O 5 .   ? 16.07500  43.31200  23.14400 1.000 30.46000 ? 609 HOH A O   1 
HETATM 6730 O  O   . HOH O 5 .   ? 10.63000  17.06900  29.84900 1.000 32.99000 ? 610 HOH A O   1 
HETATM 6731 O  O   . HOH O 5 .   ? 36.16500  -3.24500  7.47500  1.000 28.05000 ? 611 HOH A O   1 
HETATM 6732 O  O   . HOH O 5 .   ? 9.04600   -0.61200  -0.81700 1.000 29.26000 ? 612 HOH A O   1 
HETATM 6733 O  O   . HOH O 5 .   ? 35.27900  32.45000  32.21700 1.000 23.15000 ? 613 HOH A O   1 
HETATM 6734 O  O   . HOH O 5 .   ? 8.35600   29.55100  15.88500 1.000 18.80000 ? 614 HOH A O   1 
HETATM 6735 O  O   . HOH O 5 .   ? 29.31200  22.56300  2.83200  1.000 37.26000 ? 615 HOH A O   1 
HETATM 6736 O  O   . HOH O 5 .   ? 5.04900   -1.77300  7.33000  1.000 21.15000 ? 616 HOH A O   1 
HETATM 6737 O  O   . HOH O 5 .   ? 3.02300   45.24000  13.41900 1.000 21.08000 ? 617 HOH A O   1 
HETATM 6738 O  O   . HOH O 5 .   ? 35.65800  26.79600  37.28100 1.000 25.33000 ? 618 HOH A O   1 
HETATM 6739 O  O   . HOH O 5 .   ? 54.05600  15.08800  29.12900 1.000 20.32000 ? 619 HOH A O   1 
HETATM 6740 O  O   . HOH O 5 .   ? 17.03300  3.90800   -1.54500 1.000 25.95000 ? 620 HOH A O   1 
HETATM 6741 O  O   . HOH O 5 .   ? 0.67600   37.78600  10.80300 1.000 24.15000 ? 621 HOH A O   1 
HETATM 6742 O  O   . HOH O 5 .   ? -2.51600  7.99000   26.00500 1.000 28.30000 ? 622 HOH A O   1 
HETATM 6743 O  O   . HOH O 5 .   ? 43.81600  30.89600  21.80400 1.000 32.94000 ? 623 HOH A O   1 
HETATM 6744 O  O   . HOH O 5 .   ? 10.86100  17.11500  25.79600 1.000 14.79000 ? 624 HOH A O   1 
HETATM 6745 O  O   . HOH O 5 .   ? 12.01600  11.01600  18.90800 1.000 22.07000 ? 625 HOH A O   1 
HETATM 6746 O  O   . HOH O 5 .   ? -4.91500  11.51000  14.98300 1.000 16.97000 ? 626 HOH A O   1 
HETATM 6747 O  O   . HOH O 5 .   ? 17.32000  16.42800  1.79300  1.000 23.02000 ? 627 HOH A O   1 
HETATM 6748 O  O   . HOH O 5 .   ? 20.61400  -0.33800  21.09800 1.000 25.66000 ? 628 HOH A O   1 
HETATM 6749 O  O   . HOH O 5 .   ? 17.99800  25.04300  1.02000  1.000 38.05000 ? 629 HOH A O   1 
HETATM 6750 O  O   . HOH O 5 .   ? 34.77900  2.41000   8.50500  1.000 24.07000 ? 630 HOH A O   1 
HETATM 6751 O  O   . HOH O 5 .   ? 5.52000   39.07600  21.68500 1.000 25.63000 ? 631 HOH A O   1 
HETATM 6752 O  O   . HOH O 5 .   ? 15.58400  10.56500  38.25400 1.000 34.16000 ? 632 HOH A O   1 
HETATM 6753 O  O   . HOH O 5 .   ? 31.93000  37.21900  23.41600 1.000 30.89000 ? 633 HOH A O   1 
HETATM 6754 O  O   . HOH O 5 .   ? 41.15500  32.80800  22.29300 1.000 41.45000 ? 634 HOH A O   1 
HETATM 6755 O  O   . HOH O 5 .   ? 9.17800   14.37400  -1.71700 1.000 29.54000 ? 635 HOH A O   1 
HETATM 6756 O  O   . HOH O 5 .   ? 54.33800  22.69900  27.43000 1.000 23.37000 ? 636 HOH A O   1 
HETATM 6757 O  O   . HOH O 5 .   ? -4.10300  21.82300  30.26100 1.000 27.09000 ? 637 HOH A O   1 
HETATM 6758 O  O   . HOH O 5 .   ? -4.74900  32.30000  6.96700  1.000 27.27000 ? 638 HOH A O   1 
HETATM 6759 O  O   . HOH O 5 .   ? 22.32800  13.88600  28.44900 1.000 19.43000 ? 639 HOH A O   1 
HETATM 6760 O  O   . HOH O 5 .   ? 47.33900  19.25400  28.80700 1.000 26.95000 ? 640 HOH A O   1 
HETATM 6761 O  O   . HOH O 5 .   ? 25.33500  28.56000  33.95800 1.000 16.17000 ? 641 HOH A O   1 
HETATM 6762 O  O   . HOH O 5 .   ? 23.14400  -5.04900  18.90700 1.000 29.19000 ? 642 HOH A O   1 
HETATM 6763 O  O   . HOH O 5 .   ? 14.14000  6.71000   41.02900 1.000 29.74000 ? 643 HOH A O   1 
HETATM 6764 O  O   . HOH O 5 .   ? 9.89800   13.69000  43.45200 1.000 37.82000 ? 644 HOH A O   1 
HETATM 6765 O  O   . HOH O 5 .   ? 7.36600   3.97600   17.61500 1.000 28.96000 ? 645 HOH A O   1 
HETATM 6766 O  O   . HOH O 5 .   ? 16.99200  42.05100  11.88000 1.000 32.47000 ? 646 HOH A O   1 
HETATM 6767 O  O   . HOH O 5 .   ? 37.55100  6.41600   27.33600 1.000 32.80000 ? 647 HOH A O   1 
HETATM 6768 O  O   . HOH O 5 .   ? 28.54600  29.22100  15.67900 1.000 24.82000 ? 648 HOH A O   1 
HETATM 6769 O  O   . HOH O 5 .   ? -8.33900  11.50000  28.52200 1.000 31.54000 ? 649 HOH A O   1 
HETATM 6770 O  O   . HOH O 5 .   ? 22.22400  9.16700   -2.46700 1.000 18.87000 ? 650 HOH A O   1 
HETATM 6771 O  O   . HOH O 5 .   ? 28.49800  16.25500  -0.26100 1.000 20.82000 ? 651 HOH A O   1 
HETATM 6772 O  O   . HOH O 5 .   ? 20.58200  19.58000  16.36500 1.000 13.12000 ? 652 HOH A O   1 
HETATM 6773 O  O   . HOH O 5 .   ? 21.72100  10.97500  21.61200 1.000 18.11000 ? 653 HOH A O   1 
HETATM 6774 O  O   . HOH O 5 .   ? 38.55600  10.24400  18.87700 1.000 32.53000 ? 654 HOH A O   1 
HETATM 6775 O  O   . HOH O 5 .   ? 5.28500   8.20000   3.97400  1.000 34.43000 ? 655 HOH A O   1 
HETATM 6776 O  O   . HOH O 5 .   ? -0.71800  27.07600  6.47300  1.000 23.20000 ? 656 HOH A O   1 
HETATM 6777 O  O   . HOH O 5 .   ? 30.03600  27.28100  16.65300 1.000 15.90000 ? 657 HOH A O   1 
HETATM 6778 O  O   . HOH O 5 .   ? 25.32500  1.41300   4.51100  1.000 21.38000 ? 658 HOH A O   1 
HETATM 6779 O  O   . HOH O 5 .   ? 24.17100  2.82700   2.72700  1.000 21.19000 ? 659 HOH A O   1 
HETATM 6780 O  O   . HOH O 5 .   ? 21.23100  16.54600  29.36900 1.000 23.99000 ? 660 HOH A O   1 
HETATM 6781 O  O   . HOH O 5 .   ? 21.46900  12.02400  18.99300 1.000 12.17000 ? 661 HOH A O   1 
HETATM 6782 O  O   . HOH O 5 .   ? 18.76200  6.72100   34.79200 1.000 26.61000 ? 662 HOH A O   1 
HETATM 6783 O  O   . HOH O 5 .   ? 39.90500  31.42400  25.06200 1.000 24.88000 ? 663 HOH A O   1 
HETATM 6784 O  O   . HOH O 5 .   ? 14.29100  10.89800  30.45200 1.000 36.19000 ? 664 HOH A O   1 
HETATM 6785 O  O   . HOH O 5 .   ? 1.84800   35.39900  4.39900  1.000 30.47000 ? 665 HOH A O   1 
HETATM 6786 O  O   . HOH O 5 .   ? 16.07900  0.10200   2.83600  1.000 19.31000 ? 666 HOH A O   1 
HETATM 6787 O  O   . HOH O 5 .   ? 19.48000  24.24300  30.66100 1.000 22.69000 ? 667 HOH A O   1 
HETATM 6788 O  O   . HOH O 5 .   ? 24.61800  17.17200  2.04200  1.000 17.75000 ? 668 HOH A O   1 
HETATM 6789 O  O   . HOH O 5 .   ? 6.03100   27.42000  1.72900  1.000 34.67000 ? 669 HOH A O   1 
HETATM 6790 O  O   . HOH O 5 .   ? 22.90600  16.19700  25.43300 1.000 25.92000 ? 670 HOH A O   1 
HETATM 6791 O  O   . HOH O 5 .   ? 24.81500  43.23600  18.50500 1.000 27.34000 ? 671 HOH A O   1 
HETATM 6792 O  O   . HOH O 5 .   ? -1.49800  21.77900  25.99500 1.000 32.05000 ? 672 HOH A O   1 
HETATM 6793 O  O   . HOH O 5 .   ? 32.23000  2.26500   3.83500  1.000 19.53000 ? 673 HOH A O   1 
HETATM 6794 O  O   . HOH O 5 .   ? 16.52100  32.82700  26.44000 1.000 18.87000 ? 674 HOH A O   1 
HETATM 6795 O  O   . HOH O 5 .   ? 9.83500   29.70400  22.51400 1.000 15.94000 ? 675 HOH A O   1 
HETATM 6796 O  O   . HOH O 5 .   ? 15.532    34.684    -1.087   1.000 26.98000 ? 676 HOH A O   1 
HETATM 6797 O  O   . HOH O 5 .   ? 18.906    39.066    5.432    1.000 31.42000 ? 677 HOH A O   1 
HETATM 6798 O  O   . HOH O 5 .   ? 10.67100  40.55000  28.67800 1.000 26.32000 ? 678 HOH A O   1 
HETATM 6799 O  O   . HOH O 5 .   ? 2.57400   25.74300  25.00400 1.000 29.48000 ? 679 HOH A O   1 
HETATM 6800 O  O   . HOH O 5 .   ? 9.87700   32.38700  11.00100 1.000 16.68000 ? 680 HOH A O   1 
HETATM 6801 O  O   . HOH O 5 .   ? 12.66800  40.09300  9.42100  1.000 26.07000 ? 681 HOH A O   1 
HETATM 6802 O  O   . HOH O 5 .   ? 25.56400  20.80200  7.16800  1.000 22.95000 ? 682 HOH A O   1 
HETATM 6803 O  O   . HOH O 5 .   ? 20.39400  25.50300  1.91800  1.000 25.72000 ? 683 HOH A O   1 
HETATM 6804 O  O   . HOH O 5 .   ? 15.28100  2.27300   1.25300  1.000 24.08000 ? 684 HOH A O   1 
HETATM 6805 O  O   . HOH O 5 .   ? 15.89600  36.55800  29.81800 1.000 24.46000 ? 685 HOH A O   1 
HETATM 6806 O  O   . HOH O 5 .   ? -0.09700  14.44900  33.50600 1.000 29.75000 ? 686 HOH A O   1 
HETATM 6807 O  O   . HOH O 5 .   ? 20.97000  29.44400  32.66100 1.000 14.22000 ? 687 HOH A O   1 
HETATM 6808 O  O   . HOH O 5 .   ? 14.83600  36.78800  14.07600 1.000 15.48000 ? 688 HOH A O   1 
HETATM 6809 O  O   . HOH O 5 .   ? 26.38100  -4.87300  10.16400 1.000 27.64000 ? 689 HOH A O   1 
HETATM 6810 O  O   . HOH O 5 .   ? 6.71800   38.34500  24.00000 1.000 24.04000 ? 690 HOH A O   1 
HETATM 6811 O  O   . HOH O 5 .   ? -6.84200  22.29300  18.28900 1.000 25.71000 ? 691 HOH A O   1 
HETATM 6812 O  O   . HOH O 5 .   ? 31.26100  18.11100  10.91000 1.000 12.28000 ? 692 HOH A O   1 
HETATM 6813 O  O   . HOH O 5 .   ? 39.12600  16.98100  21.09300 1.000 16.50000 ? 693 HOH A O   1 
HETATM 6814 O  O   . HOH O 5 .   ? 9.14100   14.95800  26.31400 1.000 18.67000 ? 694 HOH A O   1 
HETATM 6815 O  O   . HOH O 5 .   ? -2.23500  21.29000  11.73800 1.000 19.61000 ? 695 HOH A O   1 
HETATM 6816 O  O   . HOH O 5 .   ? 22.27000  20.06100  29.91000 1.000 18.45000 ? 696 HOH A O   1 
HETATM 6817 O  O   . HOH O 5 .   ? 16.84600  11.17500  14.21800 1.000 15.24000 ? 697 HOH A O   1 
HETATM 6818 O  O   . HOH O 5 .   ? -12.57700 8.63800   22.04600 1.000 33.70000 ? 698 HOH A O   1 
HETATM 6819 O  O   . HOH O 5 .   ? 28.33500  21.96200  33.16000 1.000 14.35000 ? 699 HOH A O   1 
HETATM 6820 O  O   . HOH O 5 .   ? 2.52600   26.21000  4.45100  1.000 28.48000 ? 700 HOH A O   1 
HETATM 6821 O  O   . HOH O 5 .   ? 11.59700  12.65100  25.16200 1.000 25.78000 ? 701 HOH A O   1 
HETATM 6822 O  O   . HOH O 5 .   ? 22.51800  7.20400   14.31600 1.000 15.54000 ? 702 HOH A O   1 
HETATM 6823 O  O   . HOH O 5 .   ? 14.16400  17.46600  9.16300  1.000 15.62000 ? 703 HOH A O   1 
HETATM 6824 O  O   . HOH O 5 .   ? 27.19600  17.85300  2.02500  1.000 16.53000 ? 704 HOH A O   1 
HETATM 6825 O  O   . HOH O 5 .   ? 15.20800  15.09700  8.15500  1.000 15.97000 ? 705 HOH A O   1 
HETATM 6826 O  O   . HOH O 5 .   ? -7.67300  26.02200  24.29600 1.000 29.25000 ? 706 HOH A O   1 
HETATM 6827 O  O   . HOH O 5 .   ? -18.31800 10.95100  15.95700 1.000 27.55000 ? 707 HOH A O   1 
HETATM 6828 O  O   . HOH O 5 .   ? 23.22100  6.21200   26.81100 1.000 21.44000 ? 708 HOH A O   1 
HETATM 6829 O  O   . HOH O 5 .   ? -3.76900  36.35900  6.49700  1.000 32.43000 ? 709 HOH A O   1 
HETATM 6830 O  O   . HOH O 5 .   ? 6.73600   40.29900  8.80500  1.000 29.80000 ? 710 HOH A O   1 
HETATM 6831 O  O   . HOH O 5 .   ? 11.90400  6.49100   20.14500 1.000 33.65000 ? 711 HOH A O   1 
HETATM 6832 O  O   . HOH O 5 .   ? -14.34800 19.06700  17.93100 1.000 23.33000 ? 712 HOH A O   1 
HETATM 6833 O  O   . HOH O 5 .   ? -0.21900  21.93700  4.22500  1.000 29.21000 ? 713 HOH A O   1 
HETATM 6834 O  O   . HOH O 5 .   ? 41.23700  15.51500  9.80700  1.000 27.05000 ? 714 HOH A O   1 
HETATM 6835 O  O   . HOH O 5 .   ? 40.78700  24.31800  14.77300 1.000 21.56000 ? 715 HOH A O   1 
HETATM 6836 O  O   . HOH O 5 .   ? -3.11100  24.10700  22.39700 1.000 29.73000 ? 716 HOH A O   1 
HETATM 6837 O  O   . HOH O 5 .   ? 6.27100   6.06500   13.94500 1.000 20.80000 ? 717 HOH A O   1 
HETATM 6838 O  O   . HOH O 5 .   ? 20.61000  40.94800  11.79200 1.000 31.72000 ? 718 HOH A O   1 
HETATM 6839 O  O   . HOH O 5 .   ? 37.70700  14.76100  6.66100  1.000 27.41000 ? 719 HOH A O   1 
HETATM 6840 O  O   . HOH O 5 .   ? 4.14200   15.56100  3.26900  1.000 27.73000 ? 720 HOH A O   1 
HETATM 6841 O  O   . HOH O 5 .   ? 44.87700  19.49800  15.02000 1.000 25.61000 ? 721 HOH A O   1 
HETATM 6842 O  O   . HOH O 5 .   ? 9.93800   32.30200  29.09100 1.000 26.06000 ? 722 HOH A O   1 
HETATM 6843 O  O   . HOH O 5 .   ? -7.54100  12.71300  14.62500 1.000 19.53000 ? 723 HOH A O   1 
HETATM 6844 O  O   . HOH O 5 .   ? 10.95900  -8.19300  11.32400 1.000 23.91000 ? 724 HOH A O   1 
HETATM 6845 O  O   . HOH O 5 .   ? 4.92300   1.02800   6.53600  1.000 19.93000 ? 725 HOH A O   1 
HETATM 6846 O  O   . HOH O 5 .   ? 17.01900  25.12600  28.65300 1.000 22.71000 ? 726 HOH A O   1 
HETATM 6847 O  O   . HOH O 5 .   ? 2.98500   22.42600  23.01900 1.000 19.95000 ? 727 HOH A O   1 
HETATM 6848 O  O   . HOH O 5 .   ? 25.17400  3.81700   36.48300 1.000 26.79000 ? 728 HOH A O   1 
HETATM 6849 O  O   . HOH O 5 .   ? 30.05100  10.15900  24.83400 1.000 13.81000 ? 729 HOH A O   1 
HETATM 6850 O  O   . HOH O 5 .   ? 21.82400  39.22200  29.46300 1.000 33.91000 ? 730 HOH A O   1 
HETATM 6851 O  O   . HOH O 5 .   ? 35.88300  7.75100   6.42000  1.000 19.12000 ? 731 HOH A O   1 
HETATM 6852 O  O   . HOH O 5 .   ? 47.25000  21.88500  28.28600 1.000 24.48000 ? 732 HOH A O   1 
HETATM 6853 O  O   . HOH O 5 .   ? 8.28900   41.99600  20.72300 1.000 33.70000 ? 733 HOH A O   1 
HETATM 6854 O  O   . HOH O 5 .   ? 38.97800  22.85800  16.26900 1.000 16.24000 ? 734 HOH A O   1 
HETATM 6855 O  O   . HOH O 5 .   ? 4.30800   21.81900  25.13400 1.000 27.65000 ? 735 HOH A O   1 
HETATM 6856 O  O   . HOH O 5 .   ? 23.05700  22.59000  24.10400 1.000 16.28000 ? 736 HOH A O   1 
HETATM 6857 O  O   . HOH O 5 .   ? 32.46100  19.99200  9.28300  1.000 16.96000 ? 737 HOH A O   1 
HETATM 6858 O  O   . HOH O 5 .   ? 23.66400  2.83300   30.34200 1.000 26.51000 ? 738 HOH A O   1 
HETATM 6859 O  O   . HOH O 5 .   ? 27.04200  30.75200  34.94200 1.000 20.32000 ? 739 HOH A O   1 
HETATM 6860 O  O   . HOH O 5 .   ? 26.61100  40.34200  20.58000 1.000 22.09000 ? 740 HOH A O   1 
HETATM 6861 O  O   . HOH O 5 .   ? 36.29800  7.59600   17.63200 1.000 17.90000 ? 741 HOH A O   1 
HETATM 6862 O  O   . HOH O 5 .   ? -10.66200 23.64400  24.08700 1.000 30.43000 ? 742 HOH A O   1 
HETATM 6863 O  O   . HOH O 5 .   ? 2.02600   12.51100  23.85900 1.000 28.57000 ? 743 HOH A O   1 
HETATM 6864 O  O   . HOH O 5 .   ? 3.84500   12.47900  7.03700  1.000 20.04000 ? 744 HOH A O   1 
HETATM 6865 O  O   . HOH O 5 .   ? 0.21000   22.26700  23.31200 1.000 21.28000 ? 745 HOH A O   1 
HETATM 6866 O  O   . HOH O 5 .   ? 2.31600   3.05800   20.80500 1.000 28.21000 ? 746 HOH A O   1 
HETATM 6867 O  O   . HOH O 5 .   ? 31.05100  27.24700  14.04800 1.000 27.47000 ? 747 HOH A O   1 
HETATM 6868 O  O   . HOH O 5 .   ? 37.31400  -0.44400  7.34000  1.000 31.91000 ? 748 HOH A O   1 
HETATM 6869 O  O   . HOH O 5 .   ? 27.65100  5.16400   -0.16600 1.000 17.74000 ? 749 HOH A O   1 
HETATM 6870 O  O   . HOH O 5 .   ? 33.90100  23.35000  10.52300 1.000 25.60000 ? 750 HOH A O   1 
HETATM 6871 O  O   . HOH O 5 .   ? 26.43100  33.58500  13.37000 1.000 26.46000 ? 751 HOH A O   1 
HETATM 6872 O  O   . HOH O 5 .   ? 26.20000  -0.04400  28.62600 1.000 28.12000 ? 752 HOH A O   1 
HETATM 6873 O  O   . HOH O 5 .   ? 31.87215  17.31100  0.00000  0.50  19.92000 ? 753 HOH A O   1 
HETATM 6874 O  O   . HOH O 5 .   ? 17.92600  28.45300  15.74300 1.000 15.58000 ? 754 HOH A O   1 
HETATM 6875 O  O   . HOH O 5 .   ? 37.68900  17.33800  0.79500  1.000 24.04000 ? 755 HOH A O   1 
HETATM 6876 O  O   . HOH O 5 .   ? 32.13300  8.52000   24.16600 1.000 15.61000 ? 756 HOH A O   1 
HETATM 6877 O  O   . HOH O 5 .   ? 42.79000  10.97500  4.33000  1.000 23.88000 ? 757 HOH A O   1 
HETATM 6878 O  O   . HOH O 5 .   ? 51.53100  19.34700  21.68900 1.000 27.86000 ? 758 HOH A O   1 
HETATM 6879 O  O   . HOH O 5 .   ? 5.85700   22.66700  28.78300 1.000 35.79000 ? 759 HOH A O   1 
HETATM 6880 O  O   . HOH O 5 .   ? 38.47100  29.41800  33.86300 1.000 20.78000 ? 760 HOH A O   1 
HETATM 6881 O  O   . HOH O 5 .   ? 14.54300  39.57600  11.69100 1.000 18.97000 ? 761 HOH A O   1 
HETATM 6882 O  O   . HOH O 5 .   ? 11.53800  30.45700  24.63000 1.000 16.77000 ? 762 HOH A O   1 
HETATM 6883 O  O   . HOH O 5 .   ? 37.97900  31.94400  19.50300 1.000 31.10000 ? 763 HOH A O   1 
HETATM 6884 O  O   . HOH O 5 .   ? 15.28800  27.44400  2.13200  1.000 28.71000 ? 764 HOH A O   1 
HETATM 6885 O  O   . HOH O 5 .   ? 14.12300  19.90100  27.22000 1.000 23.31000 ? 765 HOH A O   1 
HETATM 6886 O  O   . HOH O 5 .   ? 36.53200  10.83800  25.68800 1.000 18.27000 ? 766 HOH A O   1 
HETATM 6887 O  O   . HOH O 5 .   ? 37.43000  29.80800  17.74400 1.000 15.57000 ? 767 HOH A O   1 
HETATM 6888 O  O   . HOH O 5 .   ? -0.32500  31.33600  19.24700 1.000 23.74000 ? 768 HOH A O   1 
HETATM 6889 O  O   . HOH O 5 .   ? 26.30300  28.87700  29.74300 1.000 17.34000 ? 769 HOH A O   1 
HETATM 6890 O  O   . HOH O 5 .   ? 0.00000   15.07700  0.00000  0.50  39.45000 ? 770 HOH A O   1 
HETATM 6891 O  O   . HOH O 5 .   ? 56.77600  21.78200  30.76900 1.000 22.64000 ? 771 HOH A O   1 
HETATM 6892 O  O   . HOH O 5 .   ? 10.01700  -2.68600  17.03300 1.000 24.92000 ? 772 HOH A O   1 
HETATM 6893 O  O   . HOH O 5 .   ? 35.17200  23.62000  38.45200 1.000 33.48000 ? 773 HOH A O   1 
HETATM 6894 O  O   . HOH O 5 .   ? 34.69500  8.79800   25.46000 1.000 18.94000 ? 774 HOH A O   1 
HETATM 6895 O  O   . HOH O 5 .   ? -2.32600  32.59600  12.62800 1.000 23.30000 ? 775 HOH A O   1 
HETATM 6896 O  O   . HOH O 5 .   ? 25.95800  39.05400  31.93600 1.000 31.00000 ? 776 HOH A O   1 
HETATM 6897 O  O   . HOH O 5 .   ? 8.67300   23.06500  14.75300 1.000 18.54000 ? 777 HOH A O   1 
HETATM 6898 O  O   . HOH O 5 .   ? 23.62600  32.50700  8.86600  1.000 23.21000 ? 778 HOH A O   1 
HETATM 6899 O  O   . HOH O 5 .   ? 16.23200  12.04700  11.60400 1.000 15.55000 ? 779 HOH A O   1 
HETATM 6900 O  O   . HOH O 5 .   ? 21.48000  44.91600  16.17100 1.000 27.93000 ? 780 HOH A O   1 
HETATM 6901 O  O   . HOH O 5 .   ? 32.37100  -1.61700  12.63400 1.000 25.62000 ? 781 HOH A O   1 
HETATM 6902 O  O   . HOH O 5 .   ? -6.71100  23.10600  12.77000 1.000 32.08000 ? 782 HOH A O   1 
HETATM 6903 O  O   . HOH O 5 .   ? 29.88700  0.32700   28.44100 1.000 38.75000 ? 783 HOH A O   1 
HETATM 6904 O  O   . HOH O 5 .   ? 16.86300  -9.56500  -0.22900 1.000 19.26000 ? 784 HOH A O   1 
HETATM 6905 O  O   . HOH O 5 .   ? 42.04800  8.74700   13.35900 1.000 27.44000 ? 785 HOH A O   1 
HETATM 6906 O  O   . HOH O 5 .   ? 35.722    1.781     13.153   1.000 21.23000 ? 786 HOH A O   1 
HETATM 6907 O  O   . HOH O 5 .   ? 20.85100  4.78700   26.20000 1.000 25.54000 ? 787 HOH A O   1 
HETATM 6908 O  O   . HOH O 5 .   ? 19.96600  -4.92600  4.06900  1.000 24.91000 ? 788 HOH A O   1 
HETATM 6909 O  O   . HOH O 5 .   ? -0.90200  15.68000  19.88800 1.000 16.76000 ? 789 HOH A O   1 
HETATM 6910 O  O   . HOH O 5 .   ? -3.13500  15.66100  4.83500  1.000 41.60000 ? 790 HOH A O   1 
HETATM 6911 O  O   . HOH O 5 .   ? 7.60300   25.50800  0.56900  1.000 31.83000 ? 791 HOH A O   1 
HETATM 6912 O  O   . HOH O 5 .   ? 28.17900  11.50500  -1.64600 1.000 31.15000 ? 792 HOH A O   1 
HETATM 6913 O  O   . HOH O 5 .   ? 7.43200   12.31100  18.89200 1.000 27.89000 ? 793 HOH A O   1 
HETATM 6914 O  O   . HOH O 5 .   ? 33.52100  25.52800  36.85600 1.000 21.31000 ? 794 HOH A O   1 
HETATM 6915 O  O   . HOH O 5 .   ? -3.66300  29.83300  14.14900 1.000 27.91000 ? 795 HOH A O   1 
HETATM 6916 O  O   . HOH O 5 .   ? 38.41800  4.40300   24.79500 1.000 29.42000 ? 796 HOH A O   1 
HETATM 6917 O  O   . HOH O 5 .   ? 33.84100  8.73000   28.38800 1.000 26.71000 ? 797 HOH A O   1 
HETATM 6918 O  O   . HOH O 5 .   ? 13.60900  17.27300  28.50900 1.000 31.79000 ? 798 HOH A O   1 
HETATM 6919 O  O   . HOH O 5 .   ? 31.61500  31.29500  17.19600 1.000 22.99000 ? 799 HOH A O   1 
HETATM 6920 O  O   . HOH O 5 .   ? 7.22900   9.97000   19.29500 1.000 28.20000 ? 800 HOH A O   1 
HETATM 6921 O  O   . HOH O 5 .   ? 25.40800  13.85700  28.27700 1.000 17.88000 ? 801 HOH A O   1 
HETATM 6922 O  O   . HOH O 5 .   ? 8.16600   8.68700   21.63900 1.000 23.79000 ? 802 HOH A O   1 
HETATM 6923 O  O   . HOH O 5 .   ? 17.99900  21.94500  29.19100 1.000 23.09000 ? 803 HOH A O   1 
HETATM 6924 O  O   . HOH O 5 .   ? 18.58700  -1.25200  1.90000  1.000 30.08000 ? 804 HOH A O   1 
HETATM 6925 O  O   . HOH O 5 .   ? 20.07100  30.04300  15.17100 1.000 14.00000 ? 805 HOH A O   1 
HETATM 6926 O  O   . HOH O 5 .   ? 9.61100   11.91600  19.88100 1.000 20.47000 ? 806 HOH A O   1 
HETATM 6927 O  O   . HOH O 5 .   ? 24.33800  1.73000   45.15000 1.000 30.14000 ? 807 HOH A O   1 
HETATM 6928 O  O   . HOH O 5 .   ? 14.38800  22.37700  1.18900  1.000 30.27000 ? 808 HOH A O   1 
HETATM 6929 O  O   . HOH O 5 .   ? 35.11800  18.76600  1.83000  1.000 15.68000 ? 809 HOH A O   1 
HETATM 6930 O  O   . HOH O 5 .   ? 11.96700  3.44100   19.40700 1.000 21.16000 ? 810 HOH A O   1 
HETATM 6931 O  O   . HOH O 5 .   ? 13.22200  15.19200  24.84400 1.000 16.68000 ? 811 HOH A O   1 
HETATM 6932 O  O   . HOH O 5 .   ? 4.65100   22.97100  2.14000  1.000 29.42000 ? 812 HOH A O   1 
HETATM 6933 O  O   . HOH O 5 .   ? 5.69300   13.33100  0.77600  1.000 37.84000 ? 813 HOH A O   1 
HETATM 6934 O  O   . HOH O 5 .   ? 19.31000  33.76000  0.73200  1.000 26.88000 ? 814 HOH A O   1 
HETATM 6935 O  O   . HOH O 5 .   ? 20.94100  2.36200   13.62500 1.000 18.10000 ? 815 HOH A O   1 
HETATM 6936 O  O   . HOH O 5 .   ? 17.85800  6.40600   20.01800 1.000 9.34000  ? 816 HOH A O   1 
HETATM 6937 O  O   . HOH O 5 .   ? 19.25400  46.40600  18.21000 1.000 25.39000 ? 817 HOH A O   1 
HETATM 6938 O  O   . HOH O 5 .   ? 31.96900  -3.70400  8.37500  1.000 34.33000 ? 818 HOH A O   1 
HETATM 6939 O  O   . HOH O 5 .   ? 7.59500   40.57700  6.54500  1.000 32.91000 ? 819 HOH A O   1 
HETATM 6940 O  O   . HOH O 5 .   ? 6.66700   24.81400  15.09800 1.000 21.39000 ? 820 HOH A O   1 
HETATM 6941 O  O   . HOH O 5 .   ? 35.220    7.202     2.492    1.000 35.66000 ? 821 HOH A O   1 
HETATM 6942 O  O   . HOH O 5 .   ? 26.66300  -3.86500  22.16500 1.000 38.78000 ? 822 HOH A O   1 
HETATM 6943 O  O   . HOH O 5 .   ? 2.18700   -1.94400  8.89500  1.000 26.37000 ? 823 HOH A O   1 
HETATM 6944 O  O   . HOH O 5 .   ? 18.91800  3.22500   38.21300 1.000 20.96000 ? 824 HOH A O   1 
HETATM 6945 O  O   . HOH O 5 .   ? 32.83100  -1.93700  9.65100  1.000 25.97000 ? 825 HOH A O   1 
HETATM 6946 O  O   . HOH O 5 .   ? 23.76000  7.46400   24.08100 1.000 17.56000 ? 826 HOH A O   1 
HETATM 6947 O  O   . HOH O 5 .   ? 5.09300   25.18900  3.47500  1.000 27.30000 ? 827 HOH A O   1 
HETATM 6948 O  O   . HOH O 5 .   ? 30.31400  -4.37500  6.94000  1.000 39.40000 ? 828 HOH A O   1 
HETATM 6949 O  O   . HOH O 5 .   ? 23.13900  -9.76500  11.38200 1.000 25.39000 ? 829 HOH A O   1 
HETATM 6950 O  O   . HOH O 5 .   ? 4.89100   -8.30800  3.36900  1.000 36.29000 ? 830 HOH A O   1 
HETATM 6951 O  O   . HOH O 5 .   ? 15.68200  24.02900  26.53800 1.000 19.25000 ? 831 HOH A O   1 
HETATM 6952 O  O   . HOH O 5 .   ? 24.22900  -3.68900  22.86800 1.000 33.06000 ? 832 HOH A O   1 
HETATM 6953 O  O   . HOH O 5 .   ? 1.03000   0.06500   7.56500  1.000 30.97000 ? 833 HOH A O   1 
HETATM 6954 O  O   . HOH O 5 .   ? 50.97600  22.03500  26.06900 1.000 23.94000 ? 834 HOH A O   1 
HETATM 6955 O  O   . HOH O 5 .   ? 29.38300  37.24800  21.77700 1.000 25.91000 ? 835 HOH A O   1 
HETATM 6956 O  O   . HOH O 5 .   ? 35.312    -2.426    16.342   1.000 34.65000 ? 836 HOH A O   1 
HETATM 6957 O  O   . HOH O 5 .   ? -7.63500  20.37500  16.49100 1.000 30.91000 ? 837 HOH A O   1 
HETATM 6958 O  O   . HOH O 5 .   ? 49.07000  13.20600  22.65300 1.000 33.43000 ? 838 HOH A O   1 
HETATM 6959 O  O   . HOH O 5 .   ? 27.23200  29.02400  13.13300 1.000 23.01000 ? 839 HOH A O   1 
HETATM 6960 O  O   . HOH O 5 .   ? 33.64000  20.69600  6.65700  1.000 28.46000 ? 840 HOH A O   1 
HETATM 6961 O  O   . HOH O 5 .   ? 19.99500  1.54400   26.01500 1.000 31.67000 ? 841 HOH A O   1 
HETATM 6962 O  O   . HOH O 5 .   ? 20.22200  12.85500  29.02900 1.000 19.22000 ? 842 HOH A O   1 
HETATM 6963 O  O   . HOH O 5 .   ? 7.87500   20.83600  13.12500 1.000 20.30000 ? 843 HOH A O   1 
HETATM 6964 O  O   . HOH O 5 .   ? 12.88900  21.34300  3.24300  1.000 23.72000 ? 844 HOH A O   1 
HETATM 6965 O  O   . HOH O 5 .   ? 42.76400  27.39900  28.19900 1.000 17.48000 ? 845 HOH A O   1 
HETATM 6966 O  O   . HOH O 5 .   ? 22.62900  22.13600  33.71400 1.000 26.07000 ? 846 HOH A O   1 
HETATM 6967 O  O   . HOH O 5 .   ? 14.31800  -5.73500  -3.08400 1.000 16.73000 ? 847 HOH A O   1 
HETATM 6968 O  O   . HOH O 5 .   ? 4.80800   41.77100  16.54500 1.000 22.00000 ? 848 HOH A O   1 
HETATM 6969 O  O   . HOH O 5 .   ? 12.91500  12.73200  43.49800 1.000 24.30000 ? 849 HOH A O   1 
HETATM 6970 O  O   . HOH O 5 .   ? 16.45600  21.63900  27.20300 1.000 19.98000 ? 850 HOH A O   1 
HETATM 6971 O  O   . HOH O 5 .   ? 9.37000   9.82400   27.51600 1.000 42.25000 ? 851 HOH A O   1 
HETATM 6972 O  O   . HOH O 5 .   ? 51.15800  24.25600  33.21100 1.000 27.81000 ? 852 HOH A O   1 
HETATM 6973 O  O   . HOH O 5 .   ? -7.55600  28.27600  17.74100 1.000 22.39000 ? 853 HOH A O   1 
HETATM 6974 O  O   . HOH O 5 .   ? -7.83000  17.24800  13.77400 1.000 25.82000 ? 854 HOH A O   1 
HETATM 6975 O  O   . HOH O 5 .   ? 46.26100  16.49000  31.36200 1.000 37.77000 ? 855 HOH A O   1 
HETATM 6976 O  O   . HOH O 5 .   ? 2.41000   8.91200   33.41300 1.000 37.20000 ? 856 HOH A O   1 
HETATM 6977 O  O   . HOH O 5 .   ? 30.23700  34.79200  19.08900 1.000 27.68000 ? 857 HOH A O   1 
HETATM 6978 O  O   . HOH O 5 .   ? 0.01400   34.26500  19.14800 1.000 23.15000 ? 858 HOH A O   1 
HETATM 6979 O  O   . HOH O 5 .   ? -0.13900  7.52200   9.50100  1.000 25.23000 ? 859 HOH A O   1 
HETATM 6980 O  O   . HOH O 5 .   ? 40.06200  22.61700  36.17400 1.000 26.42000 ? 860 HOH A O   1 
HETATM 6981 O  O   . HOH O 5 .   ? 26.14300  19.56600  4.82600  1.000 25.67000 ? 861 HOH A O   1 
HETATM 6982 O  O   . HOH O 5 .   ? 17.14000  2.76700   46.20200 1.000 32.48000 ? 862 HOH A O   1 
HETATM 6983 O  O   . HOH O 5 .   ? 26.11800  40.01300  18.12900 1.000 28.88000 ? 863 HOH A O   1 
HETATM 6984 O  O   . HOH O 5 .   ? 34.95200  1.87900   24.11500 1.000 22.88000 ? 864 HOH A O   1 
HETATM 6985 O  O   . HOH O 5 .   ? 36.74600  33.97900  19.79100 1.000 27.22000 ? 865 HOH A O   1 
HETATM 6986 O  O   . HOH O 5 .   ? 38.83600  18.35600  9.99600  1.000 14.49000 ? 866 HOH A O   1 
HETATM 6987 O  O   . HOH O 5 .   ? 4.97000   11.44100  4.04900  1.000 31.90000 ? 867 HOH A O   1 
HETATM 6988 O  O   . HOH O 5 .   ? -3.81700  3.66000   14.40000 1.000 35.41000 ? 868 HOH A O   1 
HETATM 6989 O  O   . HOH O 5 .   ? 25.55900  35.43500  11.78900 1.000 27.17000 ? 869 HOH A O   1 
HETATM 6990 O  O   . HOH O 5 .   ? 31.14100  -3.84600  13.69400 1.000 39.92000 ? 870 HOH A O   1 
HETATM 6991 O  O   . HOH O 5 .   ? 6.25900   43.15800  19.16500 1.000 28.64000 ? 871 HOH A O   1 
HETATM 6992 O  O   . HOH O 5 .   ? 18.95400  -3.51500  2.08300  1.000 28.68000 ? 872 HOH A O   1 
HETATM 6993 O  O   . HOH O 5 .   ? 20.40600  6.57100   -2.66500 1.000 24.06000 ? 873 HOH A O   1 
HETATM 6994 O  O   . HOH O 5 .   ? 10.36500  0.07200   -2.76600 1.000 37.05000 ? 874 HOH A O   1 
HETATM 6995 O  O   . HOH O 5 .   ? -3.31800  4.27900   17.07100 1.000 10.22000 ? 875 HOH A O   1 
HETATM 6996 O  O   . HOH O 5 .   ? 47.15000  20.12200  16.37700 1.000 18.02000 ? 876 HOH A O   1 
HETATM 6997 O  O   . HOH O 5 .   ? 8.53800   -9.24300  14.18200 1.000 27.34000 ? 877 HOH A O   1 
HETATM 6998 O  O   . HOH O 5 .   ? -1.74700  31.64700  21.43600 1.000 25.18000 ? 878 HOH A O   1 
HETATM 6999 O  O   . HOH O 5 .   ? 37.11400  23.90600  41.08800 1.000 34.69000 ? 879 HOH A O   1 
HETATM 7000 O  O   . HOH O 5 .   ? -3.25700  18.95000  12.93200 1.000 17.51000 ? 880 HOH A O   1 
HETATM 7001 O  O   . HOH O 5 .   ? 23.457    14.033    -5.795   1.000 33.29000 ? 881 HOH A O   1 
HETATM 7002 O  O   . HOH O 5 .   ? 2.74700   37.22600  15.06100 1.000 22.63000 ? 882 HOH A O   1 
HETATM 7003 O  O   . HOH O 5 .   ? -17.867   15.391    13.425   1.000 34.11000 ? 883 HOH A O   1 
HETATM 7004 O  O   . HOH O 5 .   ? 12.211    38.593    -2.878   1.000 29.59000 ? 884 HOH A O   1 
HETATM 7005 O  O   . HOH O 5 .   ? 30.53200  30.96900  14.26000 1.000 34.40000 ? 885 HOH A O   1 
HETATM 7006 O  O   . HOH O 5 .   ? 28.54900  36.64200  29.56000 1.000 25.86000 ? 886 HOH A O   1 
HETATM 7007 O  O   . HOH O 5 .   ? 21.76600  23.30400  31.20400 1.000 25.74000 ? 887 HOH A O   1 
HETATM 7008 O  O   . HOH O 5 .   ? 10.55300  35.35300  30.33900 1.000 29.75000 ? 888 HOH A O   1 
HETATM 7009 O  O   . HOH O 5 .   ? 13.79300  7.30500   38.28500 1.000 36.19000 ? 889 HOH A O   1 
HETATM 7010 O  O   . HOH O 5 .   ? 17.47300  36.15200  33.96400 1.000 31.92000 ? 890 HOH A O   1 
HETATM 7011 O  O   . HOH O 5 .   ? 23.83900  19.64800  1.49300  1.000 22.32000 ? 891 HOH A O   1 
HETATM 7012 O  O   . HOH O 5 .   ? -10.214   1.769     19.113   1.000 33.75000 ? 892 HOH A O   1 
HETATM 7013 O  O   . HOH O 5 .   ? 49.10500  18.42000  21.19900 1.000 33.42000 ? 893 HOH A O   1 
HETATM 7014 O  O   . HOH O 5 .   ? 29.60500  -5.09300  12.28900 1.000 35.31000 ? 894 HOH A O   1 
HETATM 7015 O  O   . HOH O 5 .   ? 2.82500   16.04100  0.00500  1.000 43.11000 ? 895 HOH A O   1 
HETATM 7016 O  O   . HOH O 5 .   ? 45.82800  26.99200  24.95300 1.000 31.31000 ? 896 HOH A O   1 
HETATM 7017 O  O   . HOH O 5 .   ? 11.84700  9.21800   21.42300 1.000 31.73000 ? 897 HOH A O   1 
HETATM 7018 O  O   . HOH O 5 .   ? -1.84900  36.73000  10.78600 1.000 30.54000 ? 898 HOH A O   1 
HETATM 7019 O  O   . HOH O 5 .   ? 29.80800  18.72200  0.88700  1.000 21.11000 ? 899 HOH A O   1 
HETATM 7020 O  O   . HOH O 5 .   ? 35.29300  30.22700  15.41400 1.000 35.66000 ? 900 HOH A O   1 
HETATM 7021 O  O   . HOH O 5 .   ? 22.33100  3.13100   35.81400 1.000 35.61000 ? 901 HOH A O   1 
HETATM 7022 O  O   . HOH O 5 .   ? 12.10500  43.13700  29.20900 1.000 31.83000 ? 902 HOH A O   1 
HETATM 7023 O  O   . HOH O 5 .   ? 9.67000   6.67200   21.15500 1.000 35.54000 ? 903 HOH A O   1 
HETATM 7024 O  O   . HOH O 5 .   ? 39.72300  7.64500   10.32700 1.000 30.11000 ? 904 HOH A O   1 
HETATM 7025 O  O   . HOH O 5 .   ? 31.90400  4.17200   1.85600  1.000 19.43000 ? 905 HOH A O   1 
HETATM 7026 O  O   . HOH O 5 .   ? 17.03900  37.87000  31.99200 1.000 34.12000 ? 906 HOH A O   1 
HETATM 7027 O  O   . HOH O 5 .   ? 36.04100  3.52400   6.38400  1.000 31.79000 ? 907 HOH A O   1 
HETATM 7028 O  O   . HOH O 5 .   ? 21.90500  32.83100  4.31900  1.000 39.50000 ? 908 HOH A O   1 
HETATM 7029 O  O   . HOH O 5 .   ? 21.35200  8.31300   22.94000 1.000 21.90000 ? 909 HOH A O   1 
HETATM 7030 O  O   . HOH O 5 .   ? 47.75500  27.13700  28.18200 1.000 27.47000 ? 910 HOH A O   1 
HETATM 7031 O  O   . HOH O 5 .   ? 13.57600  14.91400  27.35200 1.000 27.21000 ? 911 HOH A O   1 
HETATM 7032 O  O   . HOH O 5 .   ? 13.76100  10.00500  43.04100 1.000 35.92000 ? 912 HOH A O   1 
HETATM 7033 O  O   . HOH O 5 .   ? 17.60000  7.19200   -2.80500 1.000 35.58000 ? 913 HOH A O   1 
HETATM 7034 O  O   . HOH O 5 .   ? -7.54500  29.01900  20.46600 1.000 35.89000 ? 914 HOH A O   1 
HETATM 7035 O  O   . HOH O 5 .   ? -5.87600  19.37800  14.10600 1.000 25.25000 ? 915 HOH A O   1 
HETATM 7036 O  O   . HOH O 5 .   ? 36.24500  1.07400   10.68100 1.000 25.78000 ? 916 HOH A O   1 
HETATM 7037 O  O   . HOH O 5 .   ? 29.37100  27.91400  11.81800 1.000 27.16000 ? 917 HOH A O   1 
HETATM 7038 O  O   . HOH O 5 .   ? 5.99600   23.54200  0.08700  1.000 35.46000 ? 918 HOH A O   1 
HETATM 7039 O  O   . HOH O 5 .   ? 12.91700  44.80900  12.17300 1.000 36.54000 ? 919 HOH A O   1 
HETATM 7040 O  O   . HOH O 5 .   ? -2.38900  7.39400   9.27700  1.000 34.62000 ? 920 HOH A O   1 
HETATM 7041 O  O   . HOH O 5 .   ? 19.18400  6.92900   23.19500 1.000 25.25000 ? 921 HOH A O   1 
HETATM 7042 O  O   . HOH O 5 .   ? 12.48800  36.35400  30.77800 1.000 28.81000 ? 922 HOH A O   1 
HETATM 7043 O  O   . HOH O 5 .   ? 5.35200   13.64800  2.97000  1.000 39.46000 ? 923 HOH A O   1 
HETATM 7044 O  O   . HOH O 5 .   ? 22.10400  -2.71400  21.84500 1.000 23.71000 ? 924 HOH A O   1 
HETATM 7045 O  O   . HOH O 5 .   ? 11.11100  -9.27400  -4.78200 1.000 29.28000 ? 925 HOH A O   1 
HETATM 7046 O  O   . HOH O 5 .   ? 30.55400  20.94200  1.94800  1.000 30.98000 ? 926 HOH A O   1 
HETATM 7047 O  O   . HOH O 5 .   ? 25.17200  2.73000   0.26500  1.000 29.69000 ? 927 HOH A O   1 
HETATM 7048 O  O   . HOH O 5 .   ? 14.40000  42.50700  11.58800 1.000 33.67000 ? 928 HOH A O   1 
HETATM 7049 O  O   . HOH O 5 .   ? 2.59800   23.45200  26.65900 1.000 35.94000 ? 929 HOH A O   1 
HETATM 7050 O  O   . HOH O 5 .   ? 16.97000  19.35800  0.99200  1.000 29.24000 ? 930 HOH A O   1 
HETATM 7051 O  O   . HOH O 5 .   ? -3.96900  6.24900   27.90000 1.000 40.51000 ? 931 HOH A O   1 
HETATM 7052 O  O   . HOH O 5 .   ? 42.01200  29.96700  28.65300 1.000 19.58000 ? 932 HOH A O   1 
HETATM 7053 O  O   . HOH O 5 .   ? 20.93900  34.90400  3.29000  1.000 34.61000 ? 933 HOH A O   1 
HETATM 7054 O  O   . HOH O 5 .   ? 43.09800  23.70600  13.96400 1.000 23.68000 ? 934 HOH A O   1 
HETATM 7055 O  O   . HOH O 5 .   ? 45.34700  27.75800  27.38900 1.000 21.98000 ? 935 HOH A O   1 
HETATM 7056 O  O   . HOH O 5 .   ? 48.32300  22.84600  26.00400 1.000 30.99000 ? 936 HOH A O   1 
HETATM 7057 O  O   . HOH O 5 .   ? 39.58400  29.23700  16.39500 1.000 40.13000 ? 937 HOH A O   1 
HETATM 7058 O  O   . HOH O 5 .   ? 10.91500  12.55400  -3.23900 1.000 40.07000 ? 938 HOH A O   1 
HETATM 7059 O  O   . HOH O 5 .   ? -11.749   13.557    30.268   1.000 40.71000 ? 939 HOH A O   1 
HETATM 7060 O  O   . HOH O 5 .   ? 29.84500  3.80200   -0.29000 1.000 21.46000 ? 940 HOH A O   1 
HETATM 7061 O  O   . HOH O 5 .   ? 38.74300  6.43400   7.64800  1.000 29.23000 ? 941 HOH A O   1 
HETATM 7062 O  O   . HOH O 5 .   ? 27.36400  20.16300  0.37500  1.000 22.79000 ? 942 HOH A O   1 
HETATM 7063 O  O   . HOH O 5 .   ? 40.58000  5.51800   11.53800 1.000 35.45000 ? 943 HOH A O   1 
HETATM 7064 O  O   . HOH O 5 .   ? 43.44600  29.65200  34.17500 1.000 30.80000 ? 944 HOH A O   1 
HETATM 7065 O  O   . HOH O 5 .   ? 2.45300   22.78100  0.30600  1.000 38.82000 ? 945 HOH A O   1 
HETATM 7066 O  O   . HOH O 5 .   ? 38.92800  15.91300  8.44100  1.000 31.93000 ? 946 HOH A O   1 
HETATM 7067 O  O   . HOH O 5 .   ? -4.82300  22.28100  10.70800 1.000 34.24000 ? 947 HOH A O   1 
HETATM 7068 O  O   . HOH O 5 .   ? 44.59200  21.53400  13.52100 1.000 30.89000 ? 948 HOH A O   1 
HETATM 7069 O  O   . HOH O 5 .   ? -8.26100  14.72000  12.85800 1.000 31.24000 ? 949 HOH A O   1 
HETATM 7070 O  O   . HOH O 5 .   ? 19.34500  -10.07900 4.41200  1.000 30.40000 ? 950 HOH A O   1 
HETATM 7071 O  O   . HOH O 5 .   ? 21.45700  33.37600  7.01600  1.000 31.79000 ? 951 HOH A O   1 
HETATM 7072 O  O   . HOH O 5 .   ? 29.63800  0.94700   0.01400  1.000 33.87000 ? 952 HOH A O   1 
HETATM 7073 O  O   . HOH O 5 .   ? 45.59500  30.39900  26.90900 1.000 33.92000 ? 953 HOH A O   1 
HETATM 7074 O  O   . HOH P 5 .   ? 54.61100  22.86800  39.12800 1.000 31.14000 ? 601 HOH B O   1 
HETATM 7075 O  O   . HOH P 5 .   ? 50.60900  24.47300  41.03000 1.000 38.25000 ? 602 HOH B O   1 
HETATM 7076 O  O   . HOH P 5 .   ? 14.88200  26.06100  31.25100 1.000 24.35000 ? 603 HOH B O   1 
HETATM 7077 O  O   . HOH P 5 .   ? 54.31500  8.25000   58.47800 1.000 34.04000 ? 604 HOH B O   1 
HETATM 7078 O  O   . HOH P 5 .   ? 33.39700  23.52600  68.33000 1.000 24.21000 ? 605 HOH B O   1 
HETATM 7079 O  O   . HOH P 5 .   ? 30.14900  44.80800  53.35000 1.000 30.70000 ? 606 HOH B O   1 
HETATM 7080 O  O   . HOH P 5 .   ? 39.58500  18.93700  44.34400 1.000 14.87000 ? 607 HOH B O   1 
HETATM 7081 O  O   . HOH P 5 .   ? 2.97100   23.16400  48.78100 1.000 31.90000 ? 608 HOH B O   1 
HETATM 7082 O  O   . HOH P 5 .   ? 43.17000  7.88000   55.10400 1.000 24.45000 ? 609 HOH B O   1 
HETATM 7083 O  O   . HOH P 5 .   ? 58.575    19.839    32.229   1.000 24.68000 ? 610 HOH B O   1 
HETATM 7084 O  O   . HOH P 5 .   ? 36.27200  5.06400   32.01900 1.000 34.21000 ? 611 HOH B O   1 
HETATM 7085 O  O   . HOH P 5 .   ? -3.53900  24.24400  41.81700 1.000 27.47000 ? 612 HOH B O   1 
HETATM 7086 O  O   . HOH P 5 .   ? 34.69000  44.91500  41.69500 1.000 32.14000 ? 613 HOH B O   1 
HETATM 7087 O  O   . HOH P 5 .   ? 50.21300  42.04100  54.86000 1.000 28.56000 ? 614 HOH B O   1 
HETATM 7088 O  O   . HOH P 5 .   ? 56.98900  0.10400   54.08000 1.000 33.45000 ? 615 HOH B O   1 
HETATM 7089 O  O   . HOH P 5 .   ? 10.51800  29.65600  58.56900 1.000 39.98000 ? 616 HOH B O   1 
HETATM 7090 O  O   . HOH P 5 .   ? 55.30800  37.66000  59.57600 1.000 33.75000 ? 617 HOH B O   1 
HETATM 7091 O  O   . HOH P 5 .   ? 33.51000  11.96000  73.82600 1.000 24.46000 ? 618 HOH B O   1 
HETATM 7092 O  O   . HOH P 5 .   ? 18.03500  25.60300  59.83400 1.000 21.66000 ? 619 HOH B O   1 
HETATM 7093 O  O   . HOH P 5 .   ? 42.78600  32.29500  67.25600 1.000 31.63000 ? 620 HOH B O   1 
HETATM 7094 O  O   . HOH P 5 .   ? 34.55500  46.48000  44.72900 1.000 27.04000 ? 621 HOH B O   1 
HETATM 7095 O  O   . HOH P 5 .   ? 20.42300  30.84700  51.19900 1.000 13.37000 ? 622 HOH B O   1 
HETATM 7096 O  O   . HOH P 5 .   ? 15.29800  32.92400  35.04200 1.000 26.37000 ? 623 HOH B O   1 
HETATM 7097 O  O   . HOH P 5 .   ? 44.99500  41.32800  43.60400 1.000 30.41000 ? 624 HOH B O   1 
HETATM 7098 O  O   . HOH P 5 .   ? 13.00800  7.99300   45.30500 1.000 29.42000 ? 625 HOH B O   1 
HETATM 7099 O  O   . HOH P 5 .   ? 32.76300  32.14800  66.81100 1.000 32.70000 ? 626 HOH B O   1 
HETATM 7100 O  O   . HOH P 5 .   ? 51.34000  32.95500  61.30500 1.000 28.54000 ? 627 HOH B O   1 
HETATM 7101 O  O   . HOH P 5 .   ? 41.82200  7.42700   74.10800 1.000 29.96000 ? 628 HOH B O   1 
HETATM 7102 O  O   . HOH P 5 .   ? 58.36600  10.28900  48.64700 1.000 27.61000 ? 629 HOH B O   1 
HETATM 7103 O  O   . HOH P 5 .   ? 55.26700  7.77200   46.61800 1.000 35.84000 ? 630 HOH B O   1 
HETATM 7104 O  O   . HOH P 5 .   ? 36.58500  34.98900  65.53900 1.000 32.42000 ? 631 HOH B O   1 
HETATM 7105 O  O   . HOH P 5 .   ? 19.21200  34.51700  50.35200 1.000 28.64000 ? 632 HOH B O   1 
HETATM 7106 O  O   . HOH P 5 .   ? 26.18100  31.50000  37.07200 1.000 25.93000 ? 633 HOH B O   1 
HETATM 7107 O  O   . HOH P 5 .   ? 42.32400  33.07700  51.35100 1.000 19.54000 ? 634 HOH B O   1 
HETATM 7108 O  O   . HOH P 5 .   ? 50.61800  15.15000  37.52700 1.000 31.21000 ? 635 HOH B O   1 
HETATM 7109 O  O   . HOH P 5 .   ? 24.39100  37.81800  53.16100 1.000 25.52000 ? 636 HOH B O   1 
HETATM 7110 O  O   . HOH P 5 .   ? 43.86500  45.13800  56.23700 1.000 27.48000 ? 637 HOH B O   1 
HETATM 7111 O  O   . HOH P 5 .   ? 30.00700  3.78700   47.44900 1.000 37.23000 ? 638 HOH B O   1 
HETATM 7112 O  O   . HOH P 5 .   ? 35.25000  27.52700  65.87000 1.000 27.44000 ? 639 HOH B O   1 
HETATM 7113 O  O   . HOH P 5 .   ? 55.48600  15.71800  56.13200 1.000 21.09000 ? 640 HOH B O   1 
HETATM 7114 O  O   . HOH P 5 .   ? 43.95800  28.88300  53.07000 1.000 18.61000 ? 641 HOH B O   1 
HETATM 7115 O  O   . HOH P 5 .   ? 22.70700  27.83600  60.15400 1.000 24.35000 ? 642 HOH B O   1 
HETATM 7116 O  O   . HOH P 5 .   ? 31.57500  6.75900   37.71700 1.000 28.23000 ? 643 HOH B O   1 
HETATM 7117 O  O   . HOH P 5 .   ? 38.67900  14.67100  52.38200 1.000 21.05000 ? 644 HOH B O   1 
HETATM 7118 O  O   . HOH P 5 .   ? 45.62400  4.56400   66.36500 1.000 23.48000 ? 645 HOH B O   1 
HETATM 7119 O  O   . HOH P 5 .   ? 27.48200  18.14400  45.28500 1.000 26.92000 ? 646 HOH B O   1 
HETATM 7120 O  O   . HOH P 5 .   ? 11.20400  19.98700  49.18300 1.000 23.03000 ? 647 HOH B O   1 
HETATM 7121 O  O   . HOH P 5 .   ? 45.62500  30.79400  42.78800 1.000 27.73000 ? 648 HOH B O   1 
HETATM 7122 O  O   . HOH P 5 .   ? 18.67300  39.26100  42.94300 1.000 25.61000 ? 649 HOH B O   1 
HETATM 7123 O  O   . HOH P 5 .   ? 41.91700  26.83500  53.90100 1.000 16.12000 ? 650 HOH B O   1 
HETATM 7124 O  O   . HOH P 5 .   ? 31.26300  41.80800  34.23100 1.000 38.47000 ? 651 HOH B O   1 
HETATM 7125 O  O   . HOH P 5 .   ? 22.15200  33.00600  51.97600 1.000 24.19000 ? 652 HOH B O   1 
HETATM 7126 O  O   . HOH P 5 .   ? 46.23800  23.77800  43.82400 1.000 22.18000 ? 653 HOH B O   1 
HETATM 7127 O  O   . HOH P 5 .   ? 14.35500  16.83900  69.24400 1.000 24.90000 ? 654 HOH B O   1 
HETATM 7128 O  O   . HOH P 5 .   ? 31.15100  36.22400  36.56100 1.000 27.61000 ? 655 HOH B O   1 
HETATM 7129 O  O   . HOH P 5 .   ? 47.96300  23.71300  69.24300 1.000 28.41000 ? 656 HOH B O   1 
HETATM 7130 O  O   . HOH P 5 .   ? 40.67200  31.86600  44.95000 1.000 15.94000 ? 657 HOH B O   1 
HETATM 7131 O  O   . HOH P 5 .   ? 29.04300  15.47300  52.09100 1.000 11.95000 ? 658 HOH B O   1 
HETATM 7132 O  O   . HOH P 5 .   ? 39.00700  -4.43000  72.89400 1.000 39.62000 ? 659 HOH B O   1 
HETATM 7133 O  O   . HOH P 5 .   ? 13.88700  13.23900  45.97800 1.000 15.75000 ? 660 HOH B O   1 
HETATM 7134 O  O   . HOH P 5 .   ? 35.47200  9.60800   71.37000 1.000 19.63000 ? 661 HOH B O   1 
HETATM 7135 O  O   . HOH P 5 .   ? 16.93700  26.18600  62.27600 1.000 23.40000 ? 662 HOH B O   1 
HETATM 7136 O  O   . HOH P 5 .   ? 14.33300  11.52600  54.46400 1.000 20.31000 ? 663 HOH B O   1 
HETATM 7137 O  O   . HOH P 5 .   ? 35.48000  20.61200  62.16900 1.000 17.07000 ? 664 HOH B O   1 
HETATM 7138 O  O   . HOH P 5 .   ? 34.23100  38.99100  70.89100 1.000 34.60000 ? 665 HOH B O   1 
HETATM 7139 O  O   . HOH P 5 .   ? 45.77500  7.27300   66.48500 1.000 20.42000 ? 666 HOH B O   1 
HETATM 7140 O  O   . HOH P 5 .   ? 28.14700  21.23800  39.77600 1.000 20.19000 ? 667 HOH B O   1 
HETATM 7141 O  O   . HOH P 5 .   ? 43.10900  15.82200  51.87600 1.000 23.51000 ? 668 HOH B O   1 
HETATM 7142 O  O   . HOH P 5 .   ? 22.24800  22.27800  36.19700 1.000 20.61000 ? 669 HOH B O   1 
HETATM 7143 O  O   . HOH P 5 .   ? 34.79200  37.20700  36.63500 1.000 26.67000 ? 670 HOH B O   1 
HETATM 7144 O  O   . HOH P 5 .   ? 38.74700  6.91100   53.67600 1.000 23.30000 ? 671 HOH B O   1 
HETATM 7145 O  O   . HOH P 5 .   ? 35.70000  2.51400   52.09500 1.000 34.91000 ? 672 HOH B O   1 
HETATM 7146 O  O   . HOH P 5 .   ? 32.81500  32.04800  51.98900 1.000 15.39000 ? 673 HOH B O   1 
HETATM 7147 O  O   . HOH P 5 .   ? 53.98000  21.59900  64.97000 1.000 38.16000 ? 674 HOH B O   1 
HETATM 7148 O  O   . HOH P 5 .   ? 27.11700  -1.04500  55.76600 1.000 32.03000 ? 675 HOH B O   1 
HETATM 7149 O  O   . HOH P 5 .   ? 35.80400  40.73300  51.72400 1.000 20.65000 ? 676 HOH B O   1 
HETATM 7150 O  O   . HOH P 5 .   ? 34.05200  34.41800  40.43900 1.000 19.20000 ? 677 HOH B O   1 
HETATM 7151 O  O   . HOH P 5 .   ? 51.46800  18.61600  50.36900 1.000 18.37000 ? 678 HOH B O   1 
HETATM 7152 O  O   . HOH P 5 .   ? 5.08200   25.94100  46.26900 1.000 28.41000 ? 679 HOH B O   1 
HETATM 7153 O  O   . HOH P 5 .   ? 44.16900  39.94600  41.71400 1.000 27.83000 ? 680 HOH B O   1 
HETATM 7154 O  O   . HOH P 5 .   ? 40.73600  36.86000  55.54100 1.000 17.37000 ? 681 HOH B O   1 
HETATM 7155 O  O   . HOH P 5 .   ? 11.67000  26.73300  52.77900 1.000 20.38000 ? 682 HOH B O   1 
HETATM 7156 O  O   . HOH P 5 .   ? 30.02900  23.31900  53.22600 1.000 11.22000 ? 683 HOH B O   1 
HETATM 7157 O  O   . HOH P 5 .   ? 39.82800  41.45900  36.74600 1.000 26.88000 ? 684 HOH B O   1 
HETATM 7158 O  O   . HOH P 5 .   ? 27.98400  15.37300  42.45200 1.000 21.94000 ? 685 HOH B O   1 
HETATM 7159 O  O   . HOH P 5 .   ? 48.25700  27.53800  43.39400 1.000 26.90000 ? 686 HOH B O   1 
HETATM 7160 O  O   . HOH P 5 .   ? 25.17200  8.16500   68.62900 1.000 18.40000 ? 687 HOH B O   1 
HETATM 7161 O  O   . HOH P 5 .   ? 17.10200  24.95300  32.01800 1.000 21.04000 ? 688 HOH B O   1 
HETATM 7162 O  O   . HOH P 5 .   ? 28.03400  11.73700  57.76800 1.000 13.23000 ? 689 HOH B O   1 
HETATM 7163 O  O   . HOH P 5 .   ? 36.87000  16.95000  72.28200 1.000 28.14000 ? 690 HOH B O   1 
HETATM 7164 O  O   . HOH P 5 .   ? 57.553    22.413    38.873   1.000 21.66000 ? 691 HOH B O   1 
HETATM 7165 O  O   . HOH P 5 .   ? 25.96600  24.04200  67.54900 1.000 20.42000 ? 692 HOH B O   1 
HETATM 7166 O  O   . HOH P 5 .   ? 28.77400  13.85600  49.79500 1.000 16.26000 ? 693 HOH B O   1 
HETATM 7167 O  O   . HOH P 5 .   ? 14.71200  7.05200   60.16500 1.000 19.98000 ? 694 HOH B O   1 
HETATM 7168 O  O   . HOH P 5 .   ? 34.26500  17.11000  59.38200 1.000 14.93000 ? 695 HOH B O   1 
HETATM 7169 O  O   . HOH P 5 .   ? 33.66700  15.68400  56.98300 1.000 15.56000 ? 696 HOH B O   1 
HETATM 7170 O  O   . HOH P 5 .   ? 44.73100  23.87900  40.45100 1.000 28.10000 ? 697 HOH B O   1 
HETATM 7171 O  O   . HOH P 5 .   ? 36.23300  43.85000  53.52700 1.000 24.52000 ? 698 HOH B O   1 
HETATM 7172 O  O   . HOH P 5 .   ? 25.14000  5.35600   71.47600 1.000 34.10000 ? 699 HOH B O   1 
HETATM 7173 O  O   . HOH P 5 .   ? 34.10400  22.83900  42.21700 1.000 22.95000 ? 700 HOH B O   1 
HETATM 7174 O  O   . HOH P 5 .   ? 44.27800  10.56800  58.29100 1.000 19.44000 ? 701 HOH B O   1 
HETATM 7175 O  O   . HOH P 5 .   ? 20.38900  12.50500  47.01900 1.000 14.24000 ? 702 HOH B O   1 
HETATM 7176 O  O   . HOH P 5 .   ? 60.17300  16.00000  41.29600 1.000 23.11000 ? 703 HOH B O   1 
HETATM 7177 O  O   . HOH P 5 .   ? 22.45900  42.97000  52.56700 1.000 32.54000 ? 704 HOH B O   1 
HETATM 7178 O  O   . HOH P 5 .   ? 46.90500  18.31600  63.63400 1.000 21.45000 ? 705 HOH B O   1 
HETATM 7179 O  O   . HOH P 5 .   ? 49.41700  9.49000   71.54900 1.000 33.46000 ? 706 HOH B O   1 
HETATM 7180 O  O   . HOH P 5 .   ? 35.79200  -5.56100  56.50100 1.000 34.76000 ? 707 HOH B O   1 
HETATM 7181 O  O   . HOH P 5 .   ? 52.91200  36.80400  54.09700 1.000 31.54000 ? 708 HOH B O   1 
HETATM 7182 O  O   . HOH P 5 .   ? 41.99100  22.02200  71.92300 1.000 28.95000 ? 709 HOH B O   1 
HETATM 7183 O  O   . HOH P 5 .   ? 29.48100  29.61300  35.14500 1.000 18.30000 ? 710 HOH B O   1 
HETATM 7184 O  O   . HOH P 5 .   ? 25.56900  44.25300  41.14900 1.000 26.18000 ? 711 HOH B O   1 
HETATM 7185 O  O   . HOH P 5 .   ? 26.88000  4.12400   42.95500 1.000 25.19000 ? 712 HOH B O   1 
HETATM 7186 O  O   . HOH P 5 .   ? 48.06500  32.27200  63.34100 1.000 25.63000 ? 713 HOH B O   1 
HETATM 7187 O  O   . HOH P 5 .   ? 27.54800  24.70000  44.94100 1.000 14.31000 ? 714 HOH B O   1 
HETATM 7188 O  O   . HOH P 5 .   ? 48.32700  14.95800  47.30300 1.000 27.46000 ? 715 HOH B O   1 
HETATM 7189 O  O   . HOH P 5 .   ? 26.40900  9.88300   70.20300 1.000 20.17000 ? 716 HOH B O   1 
HETATM 7190 O  O   . HOH P 5 .   ? 54.20600  26.31100  46.23900 1.000 36.41000 ? 717 HOH B O   1 
HETATM 7191 O  O   . HOH P 5 .   ? 39.78700  17.73100  40.43300 1.000 35.40000 ? 718 HOH B O   1 
HETATM 7192 O  O   . HOH P 5 .   ? 16.063    19.646    70.440   1.000 15.05000 ? 719 HOH B O   1 
HETATM 7193 O  O   . HOH P 5 .   ? 43.18200  45.85000  58.54200 1.000 35.42000 ? 720 HOH B O   1 
HETATM 7194 O  O   . HOH P 5 .   ? 28.548    17.075    73.852   1.000 17.71000 ? 721 HOH B O   1 
HETATM 7195 O  O   . HOH P 5 .   ? 24.19000  29.81800  38.26600 1.000 16.08000 ? 722 HOH B O   1 
HETATM 7196 O  O   . HOH P 5 .   ? 23.26400  22.35600  72.10000 1.000 22.66000 ? 723 HOH B O   1 
HETATM 7197 O  O   . HOH P 5 .   ? 50.66000  28.04800  64.64900 1.000 30.99000 ? 724 HOH B O   1 
HETATM 7198 O  O   . HOH P 5 .   ? 46.16800  39.54200  62.38000 1.000 34.08000 ? 725 HOH B O   1 
HETATM 7199 O  O   . HOH P 5 .   ? 3.22000   23.32300  40.99100 1.000 26.85000 ? 726 HOH B O   1 
HETATM 7200 O  O   . HOH P 5 .   ? 34.63700  7.37900   70.41600 1.000 20.81000 ? 727 HOH B O   1 
HETATM 7201 O  O   . HOH P 5 .   ? 36.42300  22.85000  60.57700 1.000 18.49000 ? 728 HOH B O   1 
HETATM 7202 O  O   . HOH P 5 .   ? 14.93700  14.21600  65.62800 1.000 19.57000 ? 729 HOH B O   1 
HETATM 7203 O  O   . HOH P 5 .   ? 28.63500  39.89400  36.10700 1.000 25.37000 ? 730 HOH B O   1 
HETATM 7204 O  O   . HOH P 5 .   ? 25.06000  15.53100  42.72100 1.000 18.04000 ? 731 HOH B O   1 
HETATM 7205 O  O   . HOH P 5 .   ? 63.49400  11.68900  49.90500 1.000 28.37000 ? 732 HOH B O   1 
HETATM 7206 O  O   . HOH P 5 .   ? 57.55500  25.69900  50.77800 1.000 23.88000 ? 733 HOH B O   1 
HETATM 7207 O  O   . HOH P 5 .   ? 13.14200  33.14200  49.99200 1.000 18.51000 ? 734 HOH B O   1 
HETATM 7208 O  O   . HOH P 5 .   ? 38.51900  6.36100   76.51600 1.000 38.22000 ? 735 HOH B O   1 
HETATM 7209 O  O   . HOH P 5 .   ? 29.61500  3.00700   52.59000 1.000 28.80000 ? 736 HOH B O   1 
HETATM 7210 O  O   . HOH P 5 .   ? 58.03800  16.87500  56.11300 1.000 17.12000 ? 737 HOH B O   1 
HETATM 7211 O  O   . HOH P 5 .   ? 23.35000  30.47500  32.90800 1.000 23.25000 ? 738 HOH B O   1 
HETATM 7212 O  O   . HOH P 5 .   ? 52.74700  25.97700  57.37700 1.000 19.95000 ? 739 HOH B O   1 
HETATM 7213 O  O   . HOH P 5 .   ? 22.85700  12.72800  72.45500 1.000 15.66000 ? 740 HOH B O   1 
HETATM 7214 O  O   . HOH P 5 .   ? 33.53200  26.29400  40.07100 1.000 21.48000 ? 741 HOH B O   1 
HETATM 7215 O  O   . HOH P 5 .   ? 19.37600  23.36000  58.68000 1.000 15.66000 ? 742 HOH B O   1 
HETATM 7216 O  O   . HOH P 5 .   ? 12.12900  29.45200  33.84800 1.000 21.18000 ? 743 HOH B O   1 
HETATM 7217 O  O   . HOH P 5 .   ? 27.11600  8.14400   45.78400 1.000 18.54000 ? 744 HOH B O   1 
HETATM 7218 O  O   . HOH P 5 .   ? 53.11400  9.57800   46.08300 1.000 29.03000 ? 745 HOH B O   1 
HETATM 7219 O  O   . HOH P 5 .   ? -1.02800  21.83700  47.91800 1.000 29.00000 ? 746 HOH B O   1 
HETATM 7220 O  O   . HOH P 5 .   ? 11.36900  30.14100  61.31400 1.000 43.96000 ? 747 HOH B O   1 
HETATM 7221 O  O   . HOH P 5 .   ? 12.18100  13.75700  67.37000 1.000 30.79000 ? 748 HOH B O   1 
HETATM 7222 O  O   . HOH P 5 .   ? 58.76400  24.03200  52.63500 1.000 36.20000 ? 749 HOH B O   1 
HETATM 7223 O  O   . HOH P 5 .   ? 16.34700  10.52400  43.66200 1.000 27.49000 ? 750 HOH B O   1 
HETATM 7224 O  O   . HOH P 5 .   ? 36.22600  29.27900  67.30800 1.000 30.01000 ? 751 HOH B O   1 
HETATM 7225 O  O   . HOH P 5 .   ? 46.61100  25.83400  70.46400 1.000 36.48000 ? 752 HOH B O   1 
HETATM 7226 O  O   . HOH P 5 .   ? 34.11400  34.78600  73.33900 1.000 38.34000 ? 753 HOH B O   1 
HETATM 7227 O  O   . HOH P 5 .   ? 66.19900  12.14700  55.97800 1.000 29.54000 ? 754 HOH B O   1 
HETATM 7228 O  O   . HOH P 5 .   ? 18.36600  9.11500   69.28300 1.000 19.65000 ? 755 HOH B O   1 
HETATM 7229 O  O   . HOH P 5 .   ? 56.77400  36.42000  61.04000 1.000 37.91000 ? 756 HOH B O   1 
HETATM 7230 O  O   . HOH P 5 .   ? 28.00900  22.31300  35.98100 1.000 25.46000 ? 757 HOH B O   1 
HETATM 7231 O  O   . HOH P 5 .   ? 5.71400   23.80100  54.56400 1.000 27.22000 ? 758 HOH B O   1 
HETATM 7232 O  O   . HOH P 5 .   ? 27.12000  37.60100  57.88300 1.000 25.26000 ? 759 HOH B O   1 
HETATM 7233 O  O   . HOH P 5 .   ? 47.78500  24.68000  45.94600 1.000 18.51000 ? 760 HOH B O   1 
HETATM 7234 O  O   . HOH P 5 .   ? 9.80300   28.36200  53.89600 1.000 26.61000 ? 761 HOH B O   1 
HETATM 7235 O  O   . HOH P 5 .   ? 15.16100  4.80400   49.61600 1.000 24.24000 ? 762 HOH B O   1 
HETATM 7236 O  O   . HOH P 5 .   ? 54.54700  29.33100  45.40400 1.000 35.17000 ? 763 HOH B O   1 
HETATM 7237 O  O   . HOH P 5 .   ? 45.98000  29.52200  66.29200 1.000 27.19000 ? 764 HOH B O   1 
HETATM 7238 O  O   . HOH P 5 .   ? 39.60300  -2.77100  63.78800 1.000 26.94000 ? 765 HOH B O   1 
HETATM 7239 O  O   . HOH P 5 .   ? 30.58000  33.80300  52.13200 1.000 13.51000 ? 766 HOH B O   1 
HETATM 7240 O  O   . HOH P 5 .   ? 37.46100  10.83000  28.13000 1.000 23.85000 ? 767 HOH B O   1 
HETATM 7241 O  O   . HOH P 5 .   ? 29.12100  17.66900  41.19600 1.000 23.98000 ? 768 HOH B O   1 
HETATM 7242 O  O   . HOH P 5 .   ? 49.43200  6.10600   65.44300 1.000 26.12000 ? 769 HOH B O   1 
HETATM 7243 O  O   . HOH P 5 .   ? 39.01700  32.26300  42.73200 1.000 16.56000 ? 770 HOH B O   1 
HETATM 7244 O  O   . HOH P 5 .   ? 27.72300  -4.32900  64.17700 1.000 26.24000 ? 771 HOH B O   1 
HETATM 7245 O  O   . HOH P 5 .   ? 48.70200  41.27300  61.76200 1.000 23.95000 ? 772 HOH B O   1 
HETATM 7246 O  O   . HOH P 5 .   ? 31.52200  40.02800  67.37700 1.000 36.41000 ? 773 HOH B O   1 
HETATM 7247 O  O   . HOH P 5 .   ? 30.32000  32.04500  66.28100 1.000 29.08000 ? 774 HOH B O   1 
HETATM 7248 O  O   . HOH P 5 .   ? 32.13300  6.19600   71.37500 1.000 30.80000 ? 775 HOH B O   1 
HETATM 7249 O  O   . HOH P 5 .   ? 52.49600  23.83800  42.86200 1.000 39.17000 ? 776 HOH B O   1 
HETATM 7250 O  O   . HOH P 5 .   ? 13.17600  22.65900  28.22100 1.000 36.74000 ? 777 HOH B O   1 
HETATM 7251 O  O   . HOH P 5 .   ? 43.53200  4.17600   49.87300 1.000 27.21000 ? 778 HOH B O   1 
HETATM 7252 O  O   . HOH P 5 .   ? 40.43100  1.48900   57.09500 1.000 21.80000 ? 779 HOH B O   1 
HETATM 7253 O  O   . HOH P 5 .   ? 35.14400  -5.80400  61.88000 1.000 27.35000 ? 780 HOH B O   1 
HETATM 7254 O  O   . HOH P 5 .   ? 21.40300  39.60600  43.97600 1.000 27.03000 ? 781 HOH B O   1 
HETATM 7255 O  O   . HOH P 5 .   ? 15.50700  14.80300  68.20100 1.000 26.91000 ? 782 HOH B O   1 
HETATM 7256 O  O   . HOH P 5 .   ? 48.25000  6.17200   52.00000 1.000 24.93000 ? 783 HOH B O   1 
HETATM 7257 O  O   . HOH P 5 .   ? 12.64000  35.04800  47.78300 1.000 32.21000 ? 784 HOH B O   1 
HETATM 7258 O  O   . HOH P 5 .   ? 11.87200  7.03700   48.34900 1.000 25.82000 ? 785 HOH B O   1 
HETATM 7259 O  O   . HOH P 5 .   ? 10.71100  33.46700  42.18200 1.000 28.90000 ? 786 HOH B O   1 
HETATM 7260 O  O   . HOH P 5 .   ? 32.78400  0.78800   27.69600 1.000 34.17000 ? 787 HOH B O   1 
HETATM 7261 O  O   . HOH P 5 .   ? 51.07500  34.22400  47.91500 1.000 25.47000 ? 788 HOH B O   1 
HETATM 7262 O  O   . HOH P 5 .   ? 30.27700  2.65900   69.87500 1.000 29.49000 ? 789 HOH B O   1 
HETATM 7263 O  O   . HOH P 5 .   ? 65.01400  22.48800  51.73400 1.000 26.56000 ? 790 HOH B O   1 
HETATM 7264 O  O   . HOH P 5 .   ? 54.48100  33.83200  53.13900 1.000 36.74000 ? 791 HOH B O   1 
HETATM 7265 O  O   . HOH P 5 .   ? 34.75000  25.76500  42.17400 1.000 17.96000 ? 792 HOH B O   1 
HETATM 7266 O  O   . HOH P 5 .   ? 29.57900  7.17000   59.41700 1.000 20.67000 ? 793 HOH B O   1 
HETATM 7267 O  O   . HOH P 5 .   ? 68.26900  19.42700  56.86800 1.000 34.42000 ? 794 HOH B O   1 
HETATM 7268 O  O   . HOH P 5 .   ? 11.60700  20.43500  65.70800 1.000 20.19000 ? 795 HOH B O   1 
HETATM 7269 O  O   . HOH P 5 .   ? 32.69700  9.72300   52.29100 1.000 11.30000 ? 796 HOH B O   1 
HETATM 7270 O  O   . HOH P 5 .   ? 38.89100  14.98300  45.67100 1.000 25.76000 ? 797 HOH B O   1 
HETATM 7271 O  O   . HOH P 5 .   ? 40.69700  15.00400  51.13500 1.000 17.55000 ? 798 HOH B O   1 
HETATM 7272 O  O   . HOH P 5 .   ? 42.70400  25.20700  55.94300 1.000 22.11000 ? 799 HOH B O   1 
HETATM 7273 O  O   . HOH P 5 .   ? 52.84900  17.14800  63.33600 1.000 35.36000 ? 800 HOH B O   1 
HETATM 7274 O  O   . HOH P 5 .   ? 41.39300  16.83200  44.26700 1.000 17.60000 ? 801 HOH B O   1 
HETATM 7275 O  O   . HOH P 5 .   ? 58.42600  28.14400  43.96600 1.000 26.72000 ? 802 HOH B O   1 
HETATM 7276 O  O   . HOH P 5 .   ? 35.47400  43.26700  64.63700 1.000 24.94000 ? 803 HOH B O   1 
HETATM 7277 O  O   . HOH P 5 .   ? 37.33300  17.20300  45.79500 1.000 16.98000 ? 804 HOH B O   1 
HETATM 7278 O  O   . HOH P 5 .   ? 30.31500  14.05900  42.09700 1.000 21.47000 ? 805 HOH B O   1 
HETATM 7279 O  O   . HOH P 5 .   ? 18.20800  3.28400   61.42700 1.000 24.17000 ? 806 HOH B O   1 
HETATM 7280 O  O   . HOH P 5 .   ? 40.62600  33.39700  37.90800 1.000 26.26000 ? 807 HOH B O   1 
HETATM 7281 O  O   . HOH P 5 .   ? 42.35300  18.71500  39.53000 1.000 38.43000 ? 808 HOH B O   1 
HETATM 7282 O  O   . HOH P 5 .   ? 58.09400  31.57900  49.95100 1.000 24.13000 ? 809 HOH B O   1 
HETATM 7283 O  O   . HOH P 5 .   ? 31.56300  24.80200  38.51500 1.000 24.70000 ? 810 HOH B O   1 
HETATM 7284 O  O   . HOH P 5 .   ? 47.94200  9.22100   38.57100 1.000 35.87000 ? 811 HOH B O   1 
HETATM 7285 O  O   . HOH P 5 .   ? 18.31000  10.97400  47.78400 1.000 14.56000 ? 812 HOH B O   1 
HETATM 7286 O  O   . HOH P 5 .   ? 29.60800  6.89500   46.68900 1.000 28.13000 ? 813 HOH B O   1 
HETATM 7287 O  O   . HOH P 5 .   ? 43.40500  13.23400  52.06300 1.000 26.26000 ? 814 HOH B O   1 
HETATM 7288 O  O   . HOH P 5 .   ? 49.80300  12.36100  71.12600 1.000 34.08000 ? 815 HOH B O   1 
HETATM 7289 O  O   . HOH P 5 .   ? 36.25800  21.41100  42.21000 1.000 19.19000 ? 816 HOH B O   1 
HETATM 7290 O  O   . HOH P 5 .   ? 41.79200  13.33100  27.42000 1.000 29.80000 ? 817 HOH B O   1 
HETATM 7291 O  O   . HOH P 5 .   ? 23.46100  33.59600  54.16200 1.000 23.76000 ? 818 HOH B O   1 
HETATM 7292 O  O   . HOH P 5 .   ? 37.84200  27.59300  65.56200 1.000 26.77000 ? 819 HOH B O   1 
HETATM 7293 O  O   . HOH P 5 .   ? 30.22500  14.75600  74.22800 1.000 21.23000 ? 820 HOH B O   1 
HETATM 7294 O  O   . HOH P 5 .   ? 45.63200  17.92300  66.90700 1.000 29.25000 ? 821 HOH B O   1 
HETATM 7295 O  O   . HOH P 5 .   ? 37.78200  44.85600  56.02100 1.000 32.46000 ? 822 HOH B O   1 
HETATM 7296 O  O   . HOH P 5 .   ? 16.72500  28.36000  56.21600 1.000 30.01000 ? 823 HOH B O   1 
HETATM 7297 O  O   . HOH P 5 .   ? 42.54100  11.73700  50.21400 1.000 22.46000 ? 824 HOH B O   1 
HETATM 7298 O  O   . HOH P 5 .   ? 19.82300  2.45800   67.32600 1.000 34.02000 ? 825 HOH B O   1 
HETATM 7299 O  O   . HOH P 5 .   ? 48.12900  41.22500  46.08600 1.000 30.66000 ? 826 HOH B O   1 
HETATM 7300 O  O   . HOH P 5 .   ? 7.71800   28.75200  39.93600 1.000 19.29000 ? 827 HOH B O   1 
HETATM 7301 O  O   . HOH P 5 .   ? 24.10000  39.41500  33.91000 1.000 34.74000 ? 828 HOH B O   1 
HETATM 7302 O  O   . HOH P 5 .   ? 15.85000  11.18800  46.48700 1.000 22.54000 ? 829 HOH B O   1 
HETATM 7303 O  O   . HOH P 5 .   ? 50.22400  24.42100  45.59100 1.000 23.50000 ? 830 HOH B O   1 
HETATM 7304 O  O   . HOH P 5 .   ? 58.51600  21.29000  56.19400 1.000 29.50000 ? 831 HOH B O   1 
HETATM 7305 O  O   . HOH P 5 .   ? 53.71800  23.27500  56.64800 1.000 18.01000 ? 832 HOH B O   1 
HETATM 7306 O  O   . HOH P 5 .   ? 26.78000  10.04900  48.22600 1.000 18.45000 ? 833 HOH B O   1 
HETATM 7307 O  O   . HOH P 5 .   ? -0.70400  24.59700  35.50800 1.000 27.79000 ? 834 HOH B O   1 
HETATM 7308 O  O   . HOH P 5 .   ? 32.51000  23.15500  39.82800 1.000 26.80000 ? 835 HOH B O   1 
HETATM 7309 O  O   . HOH P 5 .   ? 47.80700  40.80700  50.54100 1.000 25.95000 ? 836 HOH B O   1 
HETATM 7310 O  O   . HOH P 5 .   ? 17.64800  3.77400   64.02400 1.000 23.92000 ? 837 HOH B O   1 
HETATM 7311 O  O   . HOH P 5 .   ? 30.65900  49.76600  46.80400 1.000 36.36000 ? 838 HOH B O   1 
HETATM 7312 O  O   . HOH P 5 .   ? 41.38700  -2.47000  51.88900 1.000 28.66000 ? 839 HOH B O   1 
HETATM 7313 O  O   . HOH P 5 .   ? 48.55100  3.93200   64.71400 1.000 26.98000 ? 840 HOH B O   1 
HETATM 7314 O  O   . HOH P 5 .   ? 23.76700  38.63300  37.32800 1.000 27.50000 ? 841 HOH B O   1 
HETATM 7315 O  O   . HOH P 5 .   ? 36.55000  3.36000   77.39600 1.000 28.55000 ? 842 HOH B O   1 
HETATM 7316 O  O   . HOH P 5 .   ? 58.78500  7.77200   56.44200 1.000 36.46000 ? 843 HOH B O   1 
HETATM 7317 O  O   . HOH P 5 .   ? 53.15100  12.14400  61.83800 1.000 37.81000 ? 844 HOH B O   1 
HETATM 7318 O  O   . HOH P 5 .   ? 20.63700  2.40100   57.02900 1.000 30.75000 ? 845 HOH B O   1 
HETATM 7319 O  O   . HOH P 5 .   ? 50.84600  12.92600  61.96700 1.000 28.52000 ? 846 HOH B O   1 
HETATM 7320 O  O   . HOH P 5 .   ? 45.61700  31.34600  64.60100 1.000 27.74000 ? 847 HOH B O   1 
HETATM 7321 O  O   . HOH P 5 .   ? 21.59400  37.31200  36.66600 1.000 23.62000 ? 848 HOH B O   1 
HETATM 7322 O  O   . HOH P 5 .   ? 26.80900  26.80300  67.90400 1.000 30.39000 ? 849 HOH B O   1 
HETATM 7323 O  O   . HOH P 5 .   ? 1.38200   20.93700  48.45400 1.000 30.51000 ? 850 HOH B O   1 
HETATM 7324 O  O   . HOH P 5 .   ? 42.15700  -4.77500  61.03000 1.000 30.70000 ? 851 HOH B O   1 
HETATM 7325 O  O   . HOH P 5 .   ? 11.96300  23.74100  59.89700 1.000 15.78000 ? 852 HOH B O   1 
HETATM 7326 O  O   . HOH P 5 .   ? 3.92400   17.18800  39.50300 1.000 34.55000 ? 853 HOH B O   1 
HETATM 7327 O  O   . HOH P 5 .   ? 50.92100  10.57800  44.93500 1.000 28.70000 ? 854 HOH B O   1 
HETATM 7328 O  O   . HOH P 5 .   ? 54.97900  19.16600  61.52400 1.000 33.97000 ? 855 HOH B O   1 
HETATM 7329 O  O   . HOH P 5 .   ? 47.77500  42.43700  48.44600 1.000 28.33000 ? 856 HOH B O   1 
HETATM 7330 O  O   . HOH P 5 .   ? 56.66400  24.07500  32.16600 1.000 35.71000 ? 857 HOH B O   1 
HETATM 7331 O  O   . HOH P 5 .   ? 26.23500  -0.73300  51.84600 1.000 32.23000 ? 858 HOH B O   1 
HETATM 7332 O  O   . HOH P 5 .   ? 41.24000  7.79700   53.17100 1.000 27.69000 ? 859 HOH B O   1 
HETATM 7333 O  O   . HOH P 5 .   ? 37.35300  11.07200  51.86300 1.000 30.56000 ? 860 HOH B O   1 
HETATM 7334 O  O   . HOH P 5 .   ? 53.88700  8.17500   55.52600 1.000 9.99000  ? 861 HOH B O   1 
HETATM 7335 O  O   . HOH P 5 .   ? 24.03600  -0.57500  52.59300 1.000 36.28000 ? 862 HOH B O   1 
HETATM 7336 O  O   . HOH P 5 .   ? 56.65000  6.65800   55.59000 1.000 30.23000 ? 863 HOH B O   1 
HETATM 7337 O  O   . HOH P 5 .   ? 44.49500  5.91700   48.10000 1.000 36.11000 ? 864 HOH B O   1 
HETATM 7338 O  O   . HOH P 5 .   ? 9.70600   11.27900  60.65900 1.000 32.10000 ? 865 HOH B O   1 
HETATM 7339 O  O   . HOH P 5 .   ? 45.27600  20.12800  67.99300 1.000 39.04000 ? 866 HOH B O   1 
HETATM 7340 O  O   . HOH P 5 .   ? -0.52300  24.04500  43.36800 1.000 36.87000 ? 867 HOH B O   1 
HETATM 7341 O  O   . HOH P 5 .   ? 13.87400  36.99000  47.26200 1.000 30.67000 ? 868 HOH B O   1 
HETATM 7342 O  O   . HOH P 5 .   ? 25.17500  39.91500  54.42600 1.000 29.39000 ? 869 HOH B O   1 
HETATM 7343 O  O   . HOH P 5 .   ? 3.32000   23.82500  53.17400 1.000 26.24000 ? 870 HOH B O   1 
HETATM 7344 O  O   . HOH P 5 .   ? 30.40900  37.91800  30.27700 1.000 38.58000 ? 871 HOH B O   1 
HETATM 7345 O  O   . HOH P 5 .   ? 28.75600  23.87700  38.02400 1.000 21.82000 ? 872 HOH B O   1 
HETATM 7346 O  O   . HOH P 5 .   ? 53.81400  8.19000   62.62400 1.000 41.20000 ? 873 HOH B O   1 
HETATM 7347 O  O   . HOH P 5 .   ? 38.54400  43.43100  35.56300 1.000 36.19000 ? 874 HOH B O   1 
HETATM 7348 O  O   . HOH P 5 .   ? 20.29800  35.05800  53.05100 1.000 38.59000 ? 875 HOH B O   1 
HETATM 7349 O  O   . HOH P 5 .   ? 50.03100  27.45000  67.70600 1.000 39.27000 ? 876 HOH B O   1 
HETATM 7350 O  O   . HOH P 5 .   ? 20.08100  3.63600   69.28000 1.000 34.45000 ? 877 HOH B O   1 
HETATM 7351 O  O   . HOH P 5 .   ? 47.97900  25.20200  42.10800 1.000 33.12000 ? 878 HOH B O   1 
HETATM 7352 O  O   . HOH P 5 .   ? 25.80000  40.02600  36.50000 1.000 29.98000 ? 879 HOH B O   1 
HETATM 7353 O  O   . HOH P 5 .   ? 46.73900  45.37300  55.36300 1.000 31.97000 ? 880 HOH B O   1 
HETATM 7354 O  O   . HOH P 5 .   ? 31.90800  3.47700   71.96800 1.000 32.25000 ? 881 HOH B O   1 
HETATM 7355 O  O   . HOH P 5 .   ? 35.54100  9.90700   50.69900 1.000 36.47000 ? 882 HOH B O   1 
HETATM 7356 O  O   . HOH P 5 .   ? 14.94400  34.17700  51.70300 1.000 29.98000 ? 883 HOH B O   1 
HETATM 7357 O  O   . HOH P 5 .   ? 65.244    15.566    48.239   1.000 31.61000 ? 884 HOH B O   1 
HETATM 7358 O  O   . HOH P 5 .   ? 45.44800  17.78500  29.03800 1.000 37.48000 ? 885 HOH B O   1 
HETATM 7359 O  O   . HOH P 5 .   ? 10.92600  13.29900  62.02300 1.000 28.77000 ? 886 HOH B O   1 
HETATM 7360 O  O   . HOH P 5 .   ? 29.10900  11.21600  49.12200 1.000 22.41000 ? 887 HOH B O   1 
HETATM 7361 O  O   . HOH P 5 .   ? 14.16500  35.25500  39.50400 1.000 34.90000 ? 888 HOH B O   1 
HETATM 7362 O  O   . HOH P 5 .   ? 18.48500  11.58100  70.50700 1.000 14.84000 ? 889 HOH B O   1 
HETATM 7363 O  O   . HOH P 5 .   ? 45.82400  3.01000   68.09400 1.000 36.74000 ? 890 HOH B O   1 
HETATM 7364 O  O   . HOH P 5 .   ? 14.13300  6.88800   62.79100 1.000 26.27000 ? 891 HOH B O   1 
HETATM 7365 O  O   . HOH P 5 .   ? 56.44900  23.47600  55.34400 1.000 24.62000 ? 892 HOH B O   1 
HETATM 7366 O  O   . HOH P 5 .   ? 40.16100  34.98000  36.17100 1.000 34.66000 ? 893 HOH B O   1 
HETATM 7367 O  O   . HOH P 5 .   ? 28.67100  0.68800   52.53100 1.000 32.20000 ? 894 HOH B O   1 
HETATM 7368 O  O   . HOH P 5 .   ? 43.57600  42.99500  41.30400 1.000 44.37000 ? 895 HOH B O   1 
HETATM 7369 O  O   . HOH P 5 .   ? 31.29900  9.63300   49.12700 1.000 29.13000 ? 896 HOH B O   1 
HETATM 7370 O  O   . HOH P 5 .   ? 36.36700  46.60100  53.13900 1.000 38.99000 ? 897 HOH B O   1 
HETATM 7371 O  O   . HOH P 5 .   ? 29.613    19.132    75.213   1.000 26.62000 ? 898 HOH B O   1 
HETATM 7372 O  O   . HOH P 5 .   ? 48.68800  17.35500  65.03000 1.000 32.72000 ? 899 HOH B O   1 
HETATM 7373 O  O   . HOH P 5 .   ? 21.08100  32.43400  55.85200 1.000 26.33000 ? 900 HOH B O   1 
HETATM 7374 O  O   . HOH P 5 .   ? 2.14000   24.62100  42.86400 1.000 28.88000 ? 901 HOH B O   1 
HETATM 7375 O  O   . HOH P 5 .   ? 50.57200  30.92600  64.21000 1.000 39.31000 ? 902 HOH B O   1 
HETATM 7376 O  O   . HOH P 5 .   ? 25.24400  10.29600  72.44900 1.000 34.24000 ? 903 HOH B O   1 
HETATM 7377 O  O   . HOH P 5 .   ? 50.75700  15.87800  63.34600 1.000 33.17000 ? 904 HOH B O   1 
HETATM 7378 O  O   . HOH P 5 .   ? 8.37500   31.02200  38.85800 1.000 25.43000 ? 905 HOH B O   1 
HETATM 7379 O  O   . HOH P 5 .   ? 37.877    48.546    68.667   1.000 38.26000 ? 906 HOH B O   1 
HETATM 7380 O  O   . HOH P 5 .   ? 25.24600  22.30300  34.73600 1.000 17.98000 ? 907 HOH B O   1 
HETATM 7381 O  O   . HOH P 5 .   ? 27.73900  1.52500   70.87600 1.000 31.31000 ? 908 HOH B O   1 
HETATM 7382 O  O   . HOH P 5 .   ? 10.97200  22.24800  61.56100 1.000 31.76000 ? 909 HOH B O   1 
HETATM 7383 O  O   . HOH P 5 .   ? 33.80300  26.16800  68.04800 1.000 30.45000 ? 910 HOH B O   1 
HETATM 7384 O  O   . HOH P 5 .   ? 5.33500   29.20100  40.82500 1.000 21.19000 ? 911 HOH B O   1 
HETATM 7385 O  O   . HOH P 5 .   ? 44.37600  18.18500  38.00200 1.000 37.32000 ? 912 HOH B O   1 
HETATM 7386 O  O   . HOH P 5 .   ? 18.30200  1.42700   56.27000 1.000 33.14000 ? 913 HOH B O   1 
HETATM 7387 O  O   . HOH P 5 .   ? 55.10900  26.98300  58.14300 1.000 32.66000 ? 914 HOH B O   1 
HETATM 7388 O  O   . HOH P 5 .   ? 40.63000  30.52800  35.12900 1.000 32.18000 ? 915 HOH B O   1 
HETATM 7389 O  O   . HOH P 5 .   ? 11.00700  33.45100  51.52500 1.000 28.41000 ? 916 HOH B O   1 
HETATM 7390 O  O   . HOH P 5 .   ? 15.46500  4.12100   60.51100 1.000 26.93000 ? 917 HOH B O   1 
HETATM 7391 O  O   . HOH P 5 .   ? 29.21200  38.52100  59.35000 1.000 39.02000 ? 918 HOH B O   1 
# 
