data_9CKC
# 
_entry.id   9CKC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   9CKC         pdb_00009ckc 10.2210/pdb9ckc/pdb 
WWPDB D_1000285686 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_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                        9CKC 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          6N3G 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              zyang@med.wayne.edu 
_pdbx_contact_author.name_first         Zhe 
_pdbx_contact_author.name_last          Yang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9406-9516 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhang, Y.'      1 0000-0001-8099-4225 
'Alshammari, E.' 2 0000-0002-8676-9480 
'Spellmon, N.'   3 ?                   
'Brunzelle, J.'  4 ?                   
'Yang, Z.'       5 0000-0001-9406-9516 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structure of the SMYD2-PARP1 Complex Reveals Both Productive and Allosteric Modes of Peptide Binding.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2024.12.03.626679 
_citation.pdbx_database_id_PubMed   39677743 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhang, Y.'            1  ? 
primary 'Alshammari, E.'       2  ? 
primary 'Sobota, J.'           3  ? 
primary 'Spellmon, N.'         4  ? 
primary 'Perry, E.'            5  ? 
primary 'Cao, T.'              6  ? 
primary 'Mugunamalwaththa, T.' 7  ? 
primary 'Smith, S.'            8  ? 
primary 'Brunzelle, J.'        9  ? 
primary 'Wu, G.'               10 ? 
primary 'Stemmler, T.'         11 ? 
primary 'Jin, J.'              12 ? 
primary 'Li, C.'               13 ? 
primary 'Yang, Z.'             14 ? 
# 
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 'N-lysine methyltransferase SMYD2'                     49832.164 2   2.1.1.-,2.1.1.43 ? ? ? 
2 polymer     syn 'Poly [ADP-ribose] polymerase 1, processed C-terminus' 1362.662  4   ?                ? ? ? 
3 non-polymer syn S-ADENOSYL-L-HOMOCYSTEINE                              384.411   2   ?                ? ? ? 
4 non-polymer syn 'ZINC ION'                                             65.409    6   ?                ? ? ? 
5 water       nat water                                                  18.015    420 ?                ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'HSKM-B,Histone methyltransferase SMYD2,Lysine N-methyltransferase 3C,SET and MYND domain-containing protein 2' 
2 'Poly [ADP-ribose] polymerase 1,89-kDa form'                                                                    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQK
EDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFY
SKHLEFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSY
IDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEI
CELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAA
GEKALKKAIAIMEVAHGKDHPYISEIKQEIESH
;
;MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQK
EDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFY
SKHLEFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSY
IDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEI
CELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAA
GEKALKKAIAIMEVAHGKDHPYISEIKQEIESH
;
A,B     ? 
2 'polypeptide(L)' no no RMKLTLKGGAAVD RMKLTLKGGAAVD C,D,E,F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 S-ADENOSYL-L-HOMOCYSTEINE SAH 
4 'ZINC ION'                ZN  
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   ARG n 
1 3   ALA n 
1 4   GLU n 
1 5   GLY n 
1 6   LEU n 
1 7   GLY n 
1 8   GLY n 
1 9   LEU n 
1 10  GLU n 
1 11  ARG n 
1 12  PHE n 
1 13  CYS n 
1 14  SER n 
1 15  PRO n 
1 16  GLY n 
1 17  LYS n 
1 18  GLY n 
1 19  ARG n 
1 20  GLY n 
1 21  LEU n 
1 22  ARG n 
1 23  ALA n 
1 24  LEU n 
1 25  GLN n 
1 26  PRO n 
1 27  PHE n 
1 28  GLN n 
1 29  VAL n 
1 30  GLY n 
1 31  ASP n 
1 32  LEU n 
1 33  LEU n 
1 34  PHE n 
1 35  SER n 
1 36  CYS n 
1 37  PRO n 
1 38  ALA n 
1 39  TYR n 
1 40  ALA n 
1 41  TYR n 
1 42  VAL n 
1 43  LEU n 
1 44  THR n 
1 45  VAL n 
1 46  ASN n 
1 47  GLU n 
1 48  ARG n 
1 49  GLY n 
1 50  ASN n 
1 51  HIS n 
1 52  CYS n 
1 53  GLU n 
1 54  TYR n 
1 55  CYS n 
1 56  PHE n 
1 57  THR n 
1 58  ARG n 
1 59  LYS n 
1 60  GLU n 
1 61  GLY n 
1 62  LEU n 
1 63  SER n 
1 64  LYS n 
1 65  CYS n 
1 66  GLY n 
1 67  ARG n 
1 68  CYS n 
1 69  LYS n 
1 70  GLN n 
1 71  ALA n 
1 72  PHE n 
1 73  TYR n 
1 74  CYS n 
1 75  ASN n 
1 76  VAL n 
1 77  GLU n 
1 78  CYS n 
1 79  GLN n 
1 80  LYS n 
1 81  GLU n 
1 82  ASP n 
1 83  TRP n 
1 84  PRO n 
1 85  MET n 
1 86  HIS n 
1 87  LYS n 
1 88  LEU n 
1 89  GLU n 
1 90  CYS n 
1 91  SER n 
1 92  PRO n 
1 93  MET n 
1 94  VAL n 
1 95  VAL n 
1 96  PHE n 
1 97  GLY n 
1 98  GLU n 
1 99  ASN n 
1 100 TRP n 
1 101 ASN n 
1 102 PRO n 
1 103 SER n 
1 104 GLU n 
1 105 THR n 
1 106 VAL n 
1 107 ARG n 
1 108 LEU n 
1 109 THR n 
1 110 ALA n 
1 111 ARG n 
1 112 ILE n 
1 113 LEU n 
1 114 ALA n 
1 115 LYS n 
1 116 GLN n 
1 117 LYS n 
1 118 ILE n 
1 119 HIS n 
1 120 PRO n 
1 121 GLU n 
1 122 ARG n 
1 123 THR n 
1 124 PRO n 
1 125 SER n 
1 126 GLU n 
1 127 LYS n 
1 128 LEU n 
1 129 LEU n 
1 130 ALA n 
1 131 VAL n 
1 132 LYS n 
1 133 GLU n 
1 134 PHE n 
1 135 GLU n 
1 136 SER n 
1 137 HIS n 
1 138 LEU n 
1 139 ASP n 
1 140 LYS n 
1 141 LEU n 
1 142 ASP n 
1 143 ASN n 
1 144 GLU n 
1 145 LYS n 
1 146 LYS n 
1 147 ASP n 
1 148 LEU n 
1 149 ILE n 
1 150 GLN n 
1 151 SER n 
1 152 ASP n 
1 153 ILE n 
1 154 ALA n 
1 155 ALA n 
1 156 LEU n 
1 157 HIS n 
1 158 HIS n 
1 159 PHE n 
1 160 TYR n 
1 161 SER n 
1 162 LYS n 
1 163 HIS n 
1 164 LEU n 
1 165 GLU n 
1 166 PHE n 
1 167 PRO n 
1 168 ASP n 
1 169 ASN n 
1 170 ASP n 
1 171 SER n 
1 172 LEU n 
1 173 VAL n 
1 174 VAL n 
1 175 LEU n 
1 176 PHE n 
1 177 ALA n 
1 178 GLN n 
1 179 VAL n 
1 180 ASN n 
1 181 CYS n 
1 182 ASN n 
1 183 GLY n 
1 184 PHE n 
1 185 THR n 
1 186 ILE n 
1 187 GLU n 
1 188 ASP n 
1 189 GLU n 
1 190 GLU n 
1 191 LEU n 
1 192 SER n 
1 193 HIS n 
1 194 LEU n 
1 195 GLY n 
1 196 SER n 
1 197 ALA n 
1 198 ILE n 
1 199 PHE n 
1 200 PRO n 
1 201 ASP n 
1 202 VAL n 
1 203 ALA n 
1 204 LEU n 
1 205 MET n 
1 206 ASN n 
1 207 HIS n 
1 208 SER n 
1 209 CYS n 
1 210 CYS n 
1 211 PRO n 
1 212 ASN n 
1 213 VAL n 
1 214 ILE n 
1 215 VAL n 
1 216 THR n 
1 217 TYR n 
1 218 LYS n 
1 219 GLY n 
1 220 THR n 
1 221 LEU n 
1 222 ALA n 
1 223 GLU n 
1 224 VAL n 
1 225 ARG n 
1 226 ALA n 
1 227 VAL n 
1 228 GLN n 
1 229 GLU n 
1 230 ILE n 
1 231 LYS n 
1 232 PRO n 
1 233 GLY n 
1 234 GLU n 
1 235 GLU n 
1 236 VAL n 
1 237 PHE n 
1 238 THR n 
1 239 SER n 
1 240 TYR n 
1 241 ILE n 
1 242 ASP n 
1 243 LEU n 
1 244 LEU n 
1 245 TYR n 
1 246 PRO n 
1 247 THR n 
1 248 GLU n 
1 249 ASP n 
1 250 ARG n 
1 251 ASN n 
1 252 ASP n 
1 253 ARG n 
1 254 LEU n 
1 255 ARG n 
1 256 ASP n 
1 257 SER n 
1 258 TYR n 
1 259 PHE n 
1 260 PHE n 
1 261 THR n 
1 262 CYS n 
1 263 GLU n 
1 264 CYS n 
1 265 GLN n 
1 266 GLU n 
1 267 CYS n 
1 268 THR n 
1 269 THR n 
1 270 LYS n 
1 271 ASP n 
1 272 LYS n 
1 273 ASP n 
1 274 LYS n 
1 275 ALA n 
1 276 LYS n 
1 277 VAL n 
1 278 GLU n 
1 279 ILE n 
1 280 ARG n 
1 281 LYS n 
1 282 LEU n 
1 283 SER n 
1 284 ASP n 
1 285 PRO n 
1 286 PRO n 
1 287 LYS n 
1 288 ALA n 
1 289 GLU n 
1 290 ALA n 
1 291 ILE n 
1 292 ARG n 
1 293 ASP n 
1 294 MET n 
1 295 VAL n 
1 296 ARG n 
1 297 TYR n 
1 298 ALA n 
1 299 ARG n 
1 300 ASN n 
1 301 VAL n 
1 302 ILE n 
1 303 GLU n 
1 304 GLU n 
1 305 PHE n 
1 306 ARG n 
1 307 ARG n 
1 308 ALA n 
1 309 LYS n 
1 310 HIS n 
1 311 TYR n 
1 312 LYS n 
1 313 SER n 
1 314 PRO n 
1 315 SER n 
1 316 GLU n 
1 317 LEU n 
1 318 LEU n 
1 319 GLU n 
1 320 ILE n 
1 321 CYS n 
1 322 GLU n 
1 323 LEU n 
1 324 SER n 
1 325 GLN n 
1 326 GLU n 
1 327 LYS n 
1 328 MET n 
1 329 SER n 
1 330 SER n 
1 331 VAL n 
1 332 PHE n 
1 333 GLU n 
1 334 ASP n 
1 335 SER n 
1 336 ASN n 
1 337 VAL n 
1 338 TYR n 
1 339 MET n 
1 340 LEU n 
1 341 HIS n 
1 342 MET n 
1 343 MET n 
1 344 TYR n 
1 345 GLN n 
1 346 ALA n 
1 347 MET n 
1 348 GLY n 
1 349 VAL n 
1 350 CYS n 
1 351 LEU n 
1 352 TYR n 
1 353 MET n 
1 354 GLN n 
1 355 ASP n 
1 356 TRP n 
1 357 GLU n 
1 358 GLY n 
1 359 ALA n 
1 360 LEU n 
1 361 GLN n 
1 362 TYR n 
1 363 GLY n 
1 364 GLN n 
1 365 LYS n 
1 366 ILE n 
1 367 ILE n 
1 368 LYS n 
1 369 PRO n 
1 370 TYR n 
1 371 SER n 
1 372 LYS n 
1 373 HIS n 
1 374 TYR n 
1 375 PRO n 
1 376 LEU n 
1 377 TYR n 
1 378 SER n 
1 379 LEU n 
1 380 ASN n 
1 381 VAL n 
1 382 ALA n 
1 383 SER n 
1 384 MET n 
1 385 TRP n 
1 386 LEU n 
1 387 LYS n 
1 388 LEU n 
1 389 GLY n 
1 390 ARG n 
1 391 LEU n 
1 392 TYR n 
1 393 MET n 
1 394 GLY n 
1 395 LEU n 
1 396 GLU n 
1 397 HIS n 
1 398 LYS n 
1 399 ALA n 
1 400 ALA n 
1 401 GLY n 
1 402 GLU n 
1 403 LYS n 
1 404 ALA n 
1 405 LEU n 
1 406 LYS n 
1 407 LYS n 
1 408 ALA n 
1 409 ILE n 
1 410 ALA n 
1 411 ILE n 
1 412 MET n 
1 413 GLU n 
1 414 VAL n 
1 415 ALA n 
1 416 HIS n 
1 417 GLY n 
1 418 LYS n 
1 419 ASP n 
1 420 HIS n 
1 421 PRO n 
1 422 TYR n 
1 423 ILE n 
1 424 SER n 
1 425 GLU n 
1 426 ILE n 
1 427 LYS n 
1 428 GLN n 
1 429 GLU n 
1 430 ILE n 
1 431 GLU n 
1 432 SER n 
1 433 HIS n 
2 1   ARG n 
2 2   MET n 
2 3   LYS n 
2 4   LEU n 
2 5   THR n 
2 6   LEU n 
2 7   LYS n 
2 8   GLY n 
2 9   GLY n 
2 10  ALA n 
2 11  ALA n 
2 12  VAL n 
2 13  ASP 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                   433 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SMYD2, KMT3C' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pCDF-SUMO 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       13 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                   ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                  ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'           ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                  ? 'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE                 ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'           ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                   ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                 ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                     ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                   ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                    ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                ? 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE             ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                   ? 'C5 H9 N O2'      115.130 
SAH non-polymer         . S-ADENOSYL-L-HOMOCYSTEINE ? 'C14 H20 N6 O5 S' 384.411 
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 
ZN  non-polymer         . 'ZINC ION'                ? 'Zn 2'            65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ARG 2   2   ?   ?   ?   A . n 
A 1 3   ALA 3   3   ?   ?   ?   A . n 
A 1 4   GLU 4   4   ?   ?   ?   A . n 
A 1 5   GLY 5   5   5   GLY GLY A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   GLY 7   7   7   GLY GLY A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  GLU 10  10  10  GLU GLU A . n 
A 1 11  ARG 11  11  11  ARG ARG A . n 
A 1 12  PHE 12  12  12  PHE PHE A . n 
A 1 13  CYS 13  13  13  CYS CYS A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  ARG 19  19  19  ARG ARG A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  PRO 26  26  26  PRO PRO A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  PHE 34  34  34  PHE PHE A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  CYS 36  36  36  CYS CYS A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  TYR 41  41  41  TYR TYR A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ARG 48  48  48  ARG ARG A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  HIS 51  51  51  HIS HIS A . n 
A 1 52  CYS 52  52  52  CYS CYS A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  CYS 55  55  55  CYS CYS A . n 
A 1 56  PHE 56  56  56  PHE PHE A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  LYS 64  64  64  LYS LYS A . n 
A 1 65  CYS 65  65  65  CYS CYS A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  CYS 68  68  68  CYS CYS A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  GLN 70  70  70  GLN GLN A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  PHE 72  72  72  PHE PHE A . n 
A 1 73  TYR 73  73  73  TYR TYR A . n 
A 1 74  CYS 74  74  74  CYS CYS A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  CYS 78  78  78  CYS CYS A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  TRP 83  83  83  TRP TRP A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  MET 85  85  85  MET MET A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  CYS 90  90  90  CYS CYS A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  MET 93  93  93  MET MET A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  PHE 96  96  96  PHE PHE A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 TRP 100 100 100 TRP TRP A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 LYS 115 115 115 LYS LYS A . n 
A 1 116 GLN 116 116 116 GLN GLN A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 HIS 137 137 137 HIS HIS A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASP 142 142 142 ASP ASP A . n 
A 1 143 ASN 143 143 143 ASN ASN A . n 
A 1 144 GLU 144 144 144 GLU GLU A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 LYS 146 146 146 LYS LYS A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 ASP 152 152 152 ASP ASP A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 HIS 157 157 157 HIS HIS A . n 
A 1 158 HIS 158 158 158 HIS HIS A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 TYR 160 160 160 TYR TYR A . n 
A 1 161 SER 161 161 161 SER SER A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 GLU 165 165 165 GLU GLU A . n 
A 1 166 PHE 166 166 166 PHE PHE A . n 
A 1 167 PRO 167 167 167 PRO PRO A . n 
A 1 168 ASP 168 168 168 ASP ASP A . n 
A 1 169 ASN 169 169 169 ASN ASN A . n 
A 1 170 ASP 170 170 170 ASP ASP A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 VAL 173 173 173 VAL VAL A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 PHE 176 176 176 PHE PHE A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 GLN 178 178 178 GLN GLN A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 CYS 181 181 181 CYS CYS A . n 
A 1 182 ASN 182 182 182 ASN ASN A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PHE 184 184 184 PHE PHE A . n 
A 1 185 THR 185 185 185 THR THR A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 GLU 190 190 190 GLU GLU A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 HIS 193 193 193 HIS HIS A . n 
A 1 194 LEU 194 194 194 LEU LEU A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 PHE 199 199 199 PHE PHE A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 MET 205 205 205 MET MET A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 HIS 207 207 207 HIS HIS A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 CYS 209 209 209 CYS CYS A . n 
A 1 210 CYS 210 210 210 CYS CYS A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 ILE 214 214 214 ILE ILE A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 THR 216 216 216 THR THR A . n 
A 1 217 TYR 217 217 217 TYR TYR A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 GLY 219 219 219 GLY GLY A . n 
A 1 220 THR 220 220 220 THR THR A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 ARG 225 225 225 ARG ARG A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 VAL 227 227 227 VAL VAL A . n 
A 1 228 GLN 228 228 228 GLN GLN A . n 
A 1 229 GLU 229 229 229 GLU GLU A . n 
A 1 230 ILE 230 230 230 ILE ILE A . n 
A 1 231 LYS 231 231 231 LYS LYS A . n 
A 1 232 PRO 232 232 232 PRO PRO A . n 
A 1 233 GLY 233 233 233 GLY GLY A . n 
A 1 234 GLU 234 234 234 GLU GLU A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 PHE 237 237 237 PHE PHE A . n 
A 1 238 THR 238 238 238 THR THR A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 TYR 245 245 245 TYR TYR A . n 
A 1 246 PRO 246 246 246 PRO PRO A . n 
A 1 247 THR 247 247 247 THR THR A . n 
A 1 248 GLU 248 248 248 GLU GLU A . n 
A 1 249 ASP 249 249 249 ASP ASP A . n 
A 1 250 ARG 250 250 250 ARG ARG A . n 
A 1 251 ASN 251 251 251 ASN ASN A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ASP 256 256 256 ASP ASP A . n 
A 1 257 SER 257 257 257 SER SER A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 PHE 260 260 260 PHE PHE A . n 
A 1 261 THR 261 261 261 THR THR A . n 
A 1 262 CYS 262 262 262 CYS CYS A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 CYS 264 264 264 CYS CYS A . n 
A 1 265 GLN 265 265 265 GLN GLN A . n 
A 1 266 GLU 266 266 266 GLU GLU A . n 
A 1 267 CYS 267 267 267 CYS CYS A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 THR 269 269 269 THR THR A . n 
A 1 270 LYS 270 270 270 LYS LYS A . n 
A 1 271 ASP 271 271 271 ASP ASP A . n 
A 1 272 LYS 272 272 272 LYS LYS A . n 
A 1 273 ASP 273 273 273 ASP ASP A . n 
A 1 274 LYS 274 274 274 LYS LYS A . n 
A 1 275 ALA 275 275 275 ALA ALA A . n 
A 1 276 LYS 276 276 276 LYS LYS A . n 
A 1 277 VAL 277 277 277 VAL VAL A . n 
A 1 278 GLU 278 278 278 GLU GLU A . n 
A 1 279 ILE 279 279 279 ILE ILE A . n 
A 1 280 ARG 280 280 280 ARG ARG A . n 
A 1 281 LYS 281 281 281 LYS LYS A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 SER 283 283 283 SER SER A . n 
A 1 284 ASP 284 284 284 ASP ASP A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 PRO 286 286 286 PRO PRO A . n 
A 1 287 LYS 287 287 287 LYS LYS A . n 
A 1 288 ALA 288 288 288 ALA ALA A . n 
A 1 289 GLU 289 289 289 GLU GLU A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 ILE 291 291 291 ILE ILE A . n 
A 1 292 ARG 292 292 292 ARG ARG A . n 
A 1 293 ASP 293 293 293 ASP ASP A . n 
A 1 294 MET 294 294 294 MET MET A . n 
A 1 295 VAL 295 295 295 VAL VAL A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 TYR 297 297 297 TYR TYR A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 ARG 299 299 299 ARG ARG A . n 
A 1 300 ASN 300 300 300 ASN ASN A . n 
A 1 301 VAL 301 301 301 VAL VAL A . n 
A 1 302 ILE 302 302 302 ILE ILE A . n 
A 1 303 GLU 303 303 303 GLU GLU A . n 
A 1 304 GLU 304 304 304 GLU GLU A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 ARG 306 306 306 ARG ARG A . n 
A 1 307 ARG 307 307 307 ARG ARG A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 LYS 309 309 309 LYS LYS A . n 
A 1 310 HIS 310 310 310 HIS HIS A . n 
A 1 311 TYR 311 311 311 TYR TYR A . n 
A 1 312 LYS 312 312 312 LYS LYS A . n 
A 1 313 SER 313 313 313 SER SER A . n 
A 1 314 PRO 314 314 314 PRO PRO A . n 
A 1 315 SER 315 315 315 SER SER A . n 
A 1 316 GLU 316 316 316 GLU GLU A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 GLU 319 319 319 GLU GLU A . n 
A 1 320 ILE 320 320 320 ILE ILE A . n 
A 1 321 CYS 321 321 321 CYS CYS A . n 
A 1 322 GLU 322 322 322 GLU GLU A . n 
A 1 323 LEU 323 323 323 LEU LEU A . n 
A 1 324 SER 324 324 324 SER SER A . n 
A 1 325 GLN 325 325 325 GLN GLN A . n 
A 1 326 GLU 326 326 326 GLU GLU A . n 
A 1 327 LYS 327 327 327 LYS LYS A . n 
A 1 328 MET 328 328 328 MET MET A . n 
A 1 329 SER 329 329 329 SER SER A . n 
A 1 330 SER 330 330 330 SER SER A . n 
A 1 331 VAL 331 331 331 VAL VAL A . n 
A 1 332 PHE 332 332 332 PHE PHE A . n 
A 1 333 GLU 333 333 333 GLU GLU A . n 
A 1 334 ASP 334 334 334 ASP ASP A . n 
A 1 335 SER 335 335 335 SER SER A . n 
A 1 336 ASN 336 336 336 ASN ASN A . n 
A 1 337 VAL 337 337 337 VAL VAL A . n 
A 1 338 TYR 338 338 338 TYR TYR A . n 
A 1 339 MET 339 339 339 MET MET A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 HIS 341 341 341 HIS HIS A . n 
A 1 342 MET 342 342 342 MET MET A . n 
A 1 343 MET 343 343 343 MET MET A . n 
A 1 344 TYR 344 344 344 TYR TYR A . n 
A 1 345 GLN 345 345 345 GLN GLN A . n 
A 1 346 ALA 346 346 346 ALA ALA A . n 
A 1 347 MET 347 347 347 MET MET A . n 
A 1 348 GLY 348 348 348 GLY GLY A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 CYS 350 350 350 CYS CYS A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 TYR 352 352 352 TYR TYR A . n 
A 1 353 MET 353 353 353 MET MET A . n 
A 1 354 GLN 354 354 354 GLN GLN A . n 
A 1 355 ASP 355 355 355 ASP ASP A . n 
A 1 356 TRP 356 356 356 TRP TRP A . n 
A 1 357 GLU 357 357 357 GLU GLU A . n 
A 1 358 GLY 358 358 358 GLY GLY A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 GLN 361 361 361 GLN GLN A . n 
A 1 362 TYR 362 362 362 TYR TYR A . n 
A 1 363 GLY 363 363 363 GLY GLY A . n 
A 1 364 GLN 364 364 364 GLN GLN A . n 
A 1 365 LYS 365 365 365 LYS LYS A . n 
A 1 366 ILE 366 366 366 ILE ILE A . n 
A 1 367 ILE 367 367 367 ILE ILE A . n 
A 1 368 LYS 368 368 368 LYS LYS A . n 
A 1 369 PRO 369 369 369 PRO PRO A . n 
A 1 370 TYR 370 370 370 TYR TYR A . n 
A 1 371 SER 371 371 371 SER SER A . n 
A 1 372 LYS 372 372 372 LYS LYS A . n 
A 1 373 HIS 373 373 373 HIS HIS A . n 
A 1 374 TYR 374 374 374 TYR TYR A . n 
A 1 375 PRO 375 375 375 PRO PRO A . n 
A 1 376 LEU 376 376 376 LEU LEU A . n 
A 1 377 TYR 377 377 377 TYR TYR A . n 
A 1 378 SER 378 378 378 SER SER A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 VAL 381 381 381 VAL VAL A . n 
A 1 382 ALA 382 382 382 ALA ALA A . n 
A 1 383 SER 383 383 383 SER SER A . n 
A 1 384 MET 384 384 384 MET MET A . n 
A 1 385 TRP 385 385 385 TRP TRP A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 LYS 387 387 387 LYS LYS A . n 
A 1 388 LEU 388 388 388 LEU LEU A . n 
A 1 389 GLY 389 389 389 GLY GLY A . n 
A 1 390 ARG 390 390 390 ARG ARG A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 TYR 392 392 392 TYR TYR A . n 
A 1 393 MET 393 393 393 MET MET A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 LEU 395 395 395 LEU LEU A . n 
A 1 396 GLU 396 396 396 GLU GLU A . n 
A 1 397 HIS 397 397 397 HIS HIS A . n 
A 1 398 LYS 398 398 398 LYS LYS A . n 
A 1 399 ALA 399 399 399 ALA ALA A . n 
A 1 400 ALA 400 400 400 ALA ALA A . n 
A 1 401 GLY 401 401 401 GLY GLY A . n 
A 1 402 GLU 402 402 402 GLU GLU A . n 
A 1 403 LYS 403 403 403 LYS LYS A . n 
A 1 404 ALA 404 404 404 ALA ALA A . n 
A 1 405 LEU 405 405 405 LEU LEU A . n 
A 1 406 LYS 406 406 406 LYS LYS A . n 
A 1 407 LYS 407 407 407 LYS LYS A . n 
A 1 408 ALA 408 408 408 ALA ALA A . n 
A 1 409 ILE 409 409 409 ILE ILE A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 ILE 411 411 411 ILE ILE A . n 
A 1 412 MET 412 412 412 MET MET A . n 
A 1 413 GLU 413 413 413 GLU GLU A . n 
A 1 414 VAL 414 414 414 VAL VAL A . n 
A 1 415 ALA 415 415 415 ALA ALA A . n 
A 1 416 HIS 416 416 416 HIS HIS A . n 
A 1 417 GLY 417 417 417 GLY GLY A . n 
A 1 418 LYS 418 418 418 LYS LYS A . n 
A 1 419 ASP 419 419 419 ASP ASP A . n 
A 1 420 HIS 420 420 420 HIS HIS A . n 
A 1 421 PRO 421 421 421 PRO PRO A . n 
A 1 422 TYR 422 422 422 TYR TYR A . n 
A 1 423 ILE 423 423 423 ILE ILE A . n 
A 1 424 SER 424 424 424 SER SER A . n 
A 1 425 GLU 425 425 425 GLU GLU A . n 
A 1 426 ILE 426 426 426 ILE ILE A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 GLN 428 428 428 GLN GLN A . n 
A 1 429 GLU 429 429 429 GLU GLU A . n 
A 1 430 ILE 430 430 430 ILE ILE A . n 
A 1 431 GLU 431 431 431 GLU GLU A . n 
A 1 432 SER 432 432 432 SER SER A . n 
A 1 433 HIS 433 433 433 HIS HIS A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ARG 2   2   ?   ?   ?   B . n 
B 1 3   ALA 3   3   ?   ?   ?   B . n 
B 1 4   GLU 4   4   4   GLU GLU B . n 
B 1 5   GLY 5   5   5   GLY GLY B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   GLY 7   7   7   GLY GLY B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  GLU 10  10  10  GLU GLU B . n 
B 1 11  ARG 11  11  11  ARG ARG B . n 
B 1 12  PHE 12  12  12  PHE PHE B . n 
B 1 13  CYS 13  13  13  CYS CYS B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  PRO 15  15  15  PRO PRO B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  GLY 18  18  18  GLY GLY B . n 
B 1 19  ARG 19  19  19  ARG ARG B . n 
B 1 20  GLY 20  20  20  GLY GLY B . n 
B 1 21  LEU 21  21  21  LEU LEU B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  LEU 24  24  24  LEU LEU B . n 
B 1 25  GLN 25  25  25  GLN GLN B . n 
B 1 26  PRO 26  26  26  PRO PRO B . n 
B 1 27  PHE 27  27  27  PHE PHE B . n 
B 1 28  GLN 28  28  28  GLN GLN B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  GLY 30  30  30  GLY GLY B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  LEU 33  33  33  LEU LEU B . n 
B 1 34  PHE 34  34  34  PHE PHE B . n 
B 1 35  SER 35  35  35  SER SER B . n 
B 1 36  CYS 36  36  36  CYS CYS B . n 
B 1 37  PRO 37  37  37  PRO PRO B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ALA 40  40  40  ALA ALA B . n 
B 1 41  TYR 41  41  41  TYR TYR B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  VAL 45  45  45  VAL VAL B . n 
B 1 46  ASN 46  46  46  ASN ASN B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ARG 48  48  48  ARG ARG B . n 
B 1 49  GLY 49  49  49  GLY GLY B . n 
B 1 50  ASN 50  50  50  ASN ASN B . n 
B 1 51  HIS 51  51  51  HIS HIS B . n 
B 1 52  CYS 52  52  52  CYS CYS B . n 
B 1 53  GLU 53  53  53  GLU GLU B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  CYS 55  55  55  CYS CYS B . n 
B 1 56  PHE 56  56  56  PHE PHE B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  LYS 59  59  59  LYS LYS B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  LEU 62  62  62  LEU LEU B . n 
B 1 63  SER 63  63  63  SER SER B . n 
B 1 64  LYS 64  64  64  LYS LYS B . n 
B 1 65  CYS 65  65  65  CYS CYS B . n 
B 1 66  GLY 66  66  66  GLY GLY B . n 
B 1 67  ARG 67  67  67  ARG ARG B . n 
B 1 68  CYS 68  68  68  CYS CYS B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  GLN 70  70  70  GLN GLN B . n 
B 1 71  ALA 71  71  71  ALA ALA B . n 
B 1 72  PHE 72  72  72  PHE PHE B . n 
B 1 73  TYR 73  73  73  TYR TYR B . n 
B 1 74  CYS 74  74  74  CYS CYS B . n 
B 1 75  ASN 75  75  75  ASN ASN B . n 
B 1 76  VAL 76  76  76  VAL VAL B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  CYS 78  78  78  CYS CYS B . n 
B 1 79  GLN 79  79  79  GLN GLN B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  GLU 81  81  81  GLU GLU B . n 
B 1 82  ASP 82  82  82  ASP ASP B . n 
B 1 83  TRP 83  83  83  TRP TRP B . n 
B 1 84  PRO 84  84  84  PRO PRO B . n 
B 1 85  MET 85  85  85  MET MET B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  GLU 89  89  89  GLU GLU B . n 
B 1 90  CYS 90  90  90  CYS CYS B . n 
B 1 91  SER 91  91  91  SER SER B . n 
B 1 92  PRO 92  92  92  PRO PRO B . n 
B 1 93  MET 93  93  93  MET MET B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  PHE 96  96  96  PHE PHE B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  GLU 98  98  98  GLU GLU B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 TRP 100 100 100 TRP TRP B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 PRO 102 102 102 PRO PRO B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 THR 105 105 105 THR THR B . n 
B 1 106 VAL 106 106 106 VAL VAL B . n 
B 1 107 ARG 107 107 107 ARG ARG B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 THR 109 109 109 THR THR B . n 
B 1 110 ALA 110 110 110 ALA ALA B . n 
B 1 111 ARG 111 111 111 ARG ARG B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 LYS 115 115 115 LYS LYS B . n 
B 1 116 GLN 116 116 116 GLN GLN B . n 
B 1 117 LYS 117 117 117 LYS LYS B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 PRO 120 120 120 PRO PRO B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 ARG 122 122 122 ARG ARG B . n 
B 1 123 THR 123 123 123 THR THR B . n 
B 1 124 PRO 124 124 124 PRO PRO B . n 
B 1 125 SER 125 125 125 SER SER B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 LYS 127 127 127 LYS LYS B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 VAL 131 131 131 VAL VAL B . n 
B 1 132 LYS 132 132 132 LYS LYS B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 GLU 135 135 135 GLU GLU B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 HIS 137 137 137 HIS HIS B . n 
B 1 138 LEU 138 138 138 LEU LEU B . n 
B 1 139 ASP 139 139 139 ASP ASP B . n 
B 1 140 LYS 140 140 140 LYS LYS B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASP 142 142 142 ASP ASP B . n 
B 1 143 ASN 143 143 143 ASN ASN B . n 
B 1 144 GLU 144 144 144 GLU GLU B . n 
B 1 145 LYS 145 145 145 LYS LYS B . n 
B 1 146 LYS 146 146 146 LYS LYS B . n 
B 1 147 ASP 147 147 147 ASP ASP B . n 
B 1 148 LEU 148 148 148 LEU LEU B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 GLN 150 150 150 GLN GLN B . n 
B 1 151 SER 151 151 151 SER SER B . n 
B 1 152 ASP 152 152 152 ASP ASP B . n 
B 1 153 ILE 153 153 153 ILE ILE B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 ALA 155 155 155 ALA ALA B . n 
B 1 156 LEU 156 156 156 LEU LEU B . n 
B 1 157 HIS 157 157 157 HIS HIS B . n 
B 1 158 HIS 158 158 158 HIS HIS B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 TYR 160 160 160 TYR TYR B . n 
B 1 161 SER 161 161 161 SER SER B . n 
B 1 162 LYS 162 162 162 LYS LYS B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 GLU 165 165 165 GLU GLU B . n 
B 1 166 PHE 166 166 166 PHE PHE B . n 
B 1 167 PRO 167 167 167 PRO PRO B . n 
B 1 168 ASP 168 168 168 ASP ASP B . n 
B 1 169 ASN 169 169 169 ASN ASN B . n 
B 1 170 ASP 170 170 170 ASP ASP B . n 
B 1 171 SER 171 171 171 SER SER B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 VAL 173 173 173 VAL VAL B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 LEU 175 175 175 LEU LEU B . n 
B 1 176 PHE 176 176 176 PHE PHE B . n 
B 1 177 ALA 177 177 177 ALA ALA B . n 
B 1 178 GLN 178 178 178 GLN GLN B . n 
B 1 179 VAL 179 179 179 VAL VAL B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 CYS 181 181 181 CYS CYS B . n 
B 1 182 ASN 182 182 182 ASN ASN B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 PHE 184 184 184 PHE PHE B . n 
B 1 185 THR 185 185 185 THR THR B . n 
B 1 186 ILE 186 186 186 ILE ILE B . n 
B 1 187 GLU 187 187 187 GLU GLU B . n 
B 1 188 ASP 188 188 188 ASP ASP B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 GLU 190 190 190 GLU GLU B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 SER 192 192 192 SER SER B . n 
B 1 193 HIS 193 193 193 HIS HIS B . n 
B 1 194 LEU 194 194 194 LEU LEU B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 ALA 197 197 197 ALA ALA B . n 
B 1 198 ILE 198 198 198 ILE ILE B . n 
B 1 199 PHE 199 199 199 PHE PHE B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 ASP 201 201 201 ASP ASP B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 ALA 203 203 203 ALA ALA B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 MET 205 205 205 MET MET B . n 
B 1 206 ASN 206 206 206 ASN ASN B . n 
B 1 207 HIS 207 207 207 HIS HIS B . n 
B 1 208 SER 208 208 208 SER SER B . n 
B 1 209 CYS 209 209 209 CYS CYS B . n 
B 1 210 CYS 210 210 210 CYS CYS B . n 
B 1 211 PRO 211 211 211 PRO PRO B . n 
B 1 212 ASN 212 212 212 ASN ASN B . n 
B 1 213 VAL 213 213 213 VAL VAL B . n 
B 1 214 ILE 214 214 214 ILE ILE B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 THR 216 216 216 THR THR B . n 
B 1 217 TYR 217 217 217 TYR TYR B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 GLY 219 219 219 GLY GLY B . n 
B 1 220 THR 220 220 220 THR THR B . n 
B 1 221 LEU 221 221 221 LEU LEU B . n 
B 1 222 ALA 222 222 222 ALA ALA B . n 
B 1 223 GLU 223 223 223 GLU GLU B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 ARG 225 225 225 ARG ARG B . n 
B 1 226 ALA 226 226 226 ALA ALA B . n 
B 1 227 VAL 227 227 227 VAL VAL B . n 
B 1 228 GLN 228 228 228 GLN GLN B . n 
B 1 229 GLU 229 229 229 GLU GLU B . n 
B 1 230 ILE 230 230 230 ILE ILE B . n 
B 1 231 LYS 231 231 231 LYS LYS B . n 
B 1 232 PRO 232 232 232 PRO PRO B . n 
B 1 233 GLY 233 233 233 GLY GLY B . n 
B 1 234 GLU 234 234 234 GLU GLU B . n 
B 1 235 GLU 235 235 235 GLU GLU B . n 
B 1 236 VAL 236 236 236 VAL VAL B . n 
B 1 237 PHE 237 237 237 PHE PHE B . n 
B 1 238 THR 238 238 238 THR THR B . n 
B 1 239 SER 239 239 239 SER SER B . n 
B 1 240 TYR 240 240 240 TYR TYR B . n 
B 1 241 ILE 241 241 241 ILE ILE B . n 
B 1 242 ASP 242 242 242 ASP ASP B . n 
B 1 243 LEU 243 243 243 LEU LEU B . n 
B 1 244 LEU 244 244 244 LEU LEU B . n 
B 1 245 TYR 245 245 245 TYR TYR B . n 
B 1 246 PRO 246 246 246 PRO PRO B . n 
B 1 247 THR 247 247 247 THR THR B . n 
B 1 248 GLU 248 248 248 GLU GLU B . n 
B 1 249 ASP 249 249 249 ASP ASP B . n 
B 1 250 ARG 250 250 250 ARG ARG B . n 
B 1 251 ASN 251 251 251 ASN ASN B . n 
B 1 252 ASP 252 252 252 ASP ASP B . n 
B 1 253 ARG 253 253 253 ARG ARG B . n 
B 1 254 LEU 254 254 254 LEU LEU B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 ASP 256 256 256 ASP ASP B . n 
B 1 257 SER 257 257 257 SER SER B . n 
B 1 258 TYR 258 258 258 TYR TYR B . n 
B 1 259 PHE 259 259 259 PHE PHE B . n 
B 1 260 PHE 260 260 260 PHE PHE B . n 
B 1 261 THR 261 261 261 THR THR B . n 
B 1 262 CYS 262 262 262 CYS CYS B . n 
B 1 263 GLU 263 263 263 GLU GLU B . n 
B 1 264 CYS 264 264 264 CYS CYS B . n 
B 1 265 GLN 265 265 265 GLN GLN B . n 
B 1 266 GLU 266 266 266 GLU GLU B . n 
B 1 267 CYS 267 267 267 CYS CYS B . n 
B 1 268 THR 268 268 268 THR THR B . n 
B 1 269 THR 269 269 269 THR THR B . n 
B 1 270 LYS 270 270 270 LYS LYS B . n 
B 1 271 ASP 271 271 271 ASP ASP B . n 
B 1 272 LYS 272 272 272 LYS LYS B . n 
B 1 273 ASP 273 273 273 ASP ASP B . n 
B 1 274 LYS 274 274 274 LYS LYS B . n 
B 1 275 ALA 275 275 275 ALA ALA B . n 
B 1 276 LYS 276 276 276 LYS LYS B . n 
B 1 277 VAL 277 277 277 VAL VAL B . n 
B 1 278 GLU 278 278 278 GLU GLU B . n 
B 1 279 ILE 279 279 279 ILE ILE B . n 
B 1 280 ARG 280 280 280 ARG ARG B . n 
B 1 281 LYS 281 281 281 LYS LYS B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 SER 283 283 283 SER SER B . n 
B 1 284 ASP 284 284 284 ASP ASP B . n 
B 1 285 PRO 285 285 285 PRO PRO B . n 
B 1 286 PRO 286 286 286 PRO PRO B . n 
B 1 287 LYS 287 287 287 LYS LYS B . n 
B 1 288 ALA 288 288 288 ALA ALA B . n 
B 1 289 GLU 289 289 289 GLU GLU B . n 
B 1 290 ALA 290 290 290 ALA ALA B . n 
B 1 291 ILE 291 291 291 ILE ILE B . n 
B 1 292 ARG 292 292 292 ARG ARG B . n 
B 1 293 ASP 293 293 293 ASP ASP B . n 
B 1 294 MET 294 294 294 MET MET B . n 
B 1 295 VAL 295 295 295 VAL VAL B . n 
B 1 296 ARG 296 296 296 ARG ARG B . n 
B 1 297 TYR 297 297 297 TYR TYR B . n 
B 1 298 ALA 298 298 298 ALA ALA B . n 
B 1 299 ARG 299 299 299 ARG ARG B . n 
B 1 300 ASN 300 300 300 ASN ASN B . n 
B 1 301 VAL 301 301 301 VAL VAL B . n 
B 1 302 ILE 302 302 302 ILE ILE B . n 
B 1 303 GLU 303 303 303 GLU GLU B . n 
B 1 304 GLU 304 304 304 GLU GLU B . n 
B 1 305 PHE 305 305 305 PHE PHE B . n 
B 1 306 ARG 306 306 306 ARG ARG B . n 
B 1 307 ARG 307 307 307 ARG ARG B . n 
B 1 308 ALA 308 308 308 ALA ALA B . n 
B 1 309 LYS 309 309 309 LYS LYS B . n 
B 1 310 HIS 310 310 310 HIS HIS B . n 
B 1 311 TYR 311 311 311 TYR TYR B . n 
B 1 312 LYS 312 312 312 LYS LYS B . n 
B 1 313 SER 313 313 313 SER SER B . n 
B 1 314 PRO 314 314 314 PRO PRO B . n 
B 1 315 SER 315 315 315 SER SER B . n 
B 1 316 GLU 316 316 316 GLU GLU B . n 
B 1 317 LEU 317 317 317 LEU LEU B . n 
B 1 318 LEU 318 318 318 LEU LEU B . n 
B 1 319 GLU 319 319 319 GLU GLU B . n 
B 1 320 ILE 320 320 320 ILE ILE B . n 
B 1 321 CYS 321 321 321 CYS CYS B . n 
B 1 322 GLU 322 322 322 GLU GLU B . n 
B 1 323 LEU 323 323 323 LEU LEU B . n 
B 1 324 SER 324 324 324 SER SER B . n 
B 1 325 GLN 325 325 325 GLN GLN B . n 
B 1 326 GLU 326 326 326 GLU GLU B . n 
B 1 327 LYS 327 327 327 LYS LYS B . n 
B 1 328 MET 328 328 328 MET MET B . n 
B 1 329 SER 329 329 329 SER SER B . n 
B 1 330 SER 330 330 330 SER SER B . n 
B 1 331 VAL 331 331 331 VAL VAL B . n 
B 1 332 PHE 332 332 332 PHE PHE B . n 
B 1 333 GLU 333 333 333 GLU GLU B . n 
B 1 334 ASP 334 334 334 ASP ASP B . n 
B 1 335 SER 335 335 335 SER SER B . n 
B 1 336 ASN 336 336 336 ASN ASN B . n 
B 1 337 VAL 337 337 337 VAL VAL B . n 
B 1 338 TYR 338 338 338 TYR TYR B . n 
B 1 339 MET 339 339 339 MET MET B . n 
B 1 340 LEU 340 340 340 LEU LEU B . n 
B 1 341 HIS 341 341 341 HIS HIS B . n 
B 1 342 MET 342 342 342 MET MET B . n 
B 1 343 MET 343 343 343 MET MET B . n 
B 1 344 TYR 344 344 344 TYR TYR B . n 
B 1 345 GLN 345 345 345 GLN GLN B . n 
B 1 346 ALA 346 346 346 ALA ALA B . n 
B 1 347 MET 347 347 347 MET MET B . n 
B 1 348 GLY 348 348 348 GLY GLY B . n 
B 1 349 VAL 349 349 349 VAL VAL B . n 
B 1 350 CYS 350 350 350 CYS CYS B . n 
B 1 351 LEU 351 351 351 LEU LEU B . n 
B 1 352 TYR 352 352 352 TYR TYR B . n 
B 1 353 MET 353 353 353 MET MET B . n 
B 1 354 GLN 354 354 354 GLN GLN B . n 
B 1 355 ASP 355 355 355 ASP ASP B . n 
B 1 356 TRP 356 356 356 TRP TRP B . n 
B 1 357 GLU 357 357 357 GLU GLU B . n 
B 1 358 GLY 358 358 358 GLY GLY B . n 
B 1 359 ALA 359 359 359 ALA ALA B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 GLN 361 361 361 GLN GLN B . n 
B 1 362 TYR 362 362 362 TYR TYR B . n 
B 1 363 GLY 363 363 363 GLY GLY B . n 
B 1 364 GLN 364 364 364 GLN GLN B . n 
B 1 365 LYS 365 365 365 LYS LYS B . n 
B 1 366 ILE 366 366 366 ILE ILE B . n 
B 1 367 ILE 367 367 367 ILE ILE B . n 
B 1 368 LYS 368 368 368 LYS LYS B . n 
B 1 369 PRO 369 369 369 PRO PRO B . n 
B 1 370 TYR 370 370 370 TYR TYR B . n 
B 1 371 SER 371 371 371 SER SER B . n 
B 1 372 LYS 372 372 372 LYS LYS B . n 
B 1 373 HIS 373 373 373 HIS HIS B . n 
B 1 374 TYR 374 374 374 TYR TYR B . n 
B 1 375 PRO 375 375 375 PRO PRO B . n 
B 1 376 LEU 376 376 376 LEU LEU B . n 
B 1 377 TYR 377 377 377 TYR TYR B . n 
B 1 378 SER 378 378 378 SER SER B . n 
B 1 379 LEU 379 379 379 LEU LEU B . n 
B 1 380 ASN 380 380 380 ASN ASN B . n 
B 1 381 VAL 381 381 381 VAL VAL B . n 
B 1 382 ALA 382 382 382 ALA ALA B . n 
B 1 383 SER 383 383 383 SER SER B . n 
B 1 384 MET 384 384 384 MET MET B . n 
B 1 385 TRP 385 385 385 TRP TRP B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 LYS 387 387 387 LYS LYS B . n 
B 1 388 LEU 388 388 388 LEU LEU B . n 
B 1 389 GLY 389 389 389 GLY GLY B . n 
B 1 390 ARG 390 390 390 ARG ARG B . n 
B 1 391 LEU 391 391 391 LEU LEU B . n 
B 1 392 TYR 392 392 392 TYR TYR B . n 
B 1 393 MET 393 393 393 MET MET B . n 
B 1 394 GLY 394 394 394 GLY GLY B . n 
B 1 395 LEU 395 395 395 LEU LEU B . n 
B 1 396 GLU 396 396 396 GLU GLU B . n 
B 1 397 HIS 397 397 397 HIS HIS B . n 
B 1 398 LYS 398 398 398 LYS LYS B . n 
B 1 399 ALA 399 399 399 ALA ALA B . n 
B 1 400 ALA 400 400 400 ALA ALA B . n 
B 1 401 GLY 401 401 401 GLY GLY B . n 
B 1 402 GLU 402 402 402 GLU GLU B . n 
B 1 403 LYS 403 403 403 LYS LYS B . n 
B 1 404 ALA 404 404 404 ALA ALA B . n 
B 1 405 LEU 405 405 405 LEU LEU B . n 
B 1 406 LYS 406 406 406 LYS LYS B . n 
B 1 407 LYS 407 407 407 LYS LYS B . n 
B 1 408 ALA 408 408 408 ALA ALA B . n 
B 1 409 ILE 409 409 409 ILE ILE B . n 
B 1 410 ALA 410 410 410 ALA ALA B . n 
B 1 411 ILE 411 411 411 ILE ILE B . n 
B 1 412 MET 412 412 412 MET MET B . n 
B 1 413 GLU 413 413 413 GLU GLU B . n 
B 1 414 VAL 414 414 414 VAL VAL B . n 
B 1 415 ALA 415 415 415 ALA ALA B . n 
B 1 416 HIS 416 416 416 HIS HIS B . n 
B 1 417 GLY 417 417 417 GLY GLY B . n 
B 1 418 LYS 418 418 418 LYS LYS B . n 
B 1 419 ASP 419 419 419 ASP ASP B . n 
B 1 420 HIS 420 420 420 HIS HIS B . n 
B 1 421 PRO 421 421 421 PRO PRO B . n 
B 1 422 TYR 422 422 422 TYR TYR B . n 
B 1 423 ILE 423 423 423 ILE ILE B . n 
B 1 424 SER 424 424 424 SER SER B . n 
B 1 425 GLU 425 425 425 GLU GLU B . n 
B 1 426 ILE 426 426 426 ILE ILE B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 GLN 428 428 428 GLN GLN B . n 
B 1 429 GLU 429 429 429 GLU GLU B . n 
B 1 430 ILE 430 430 430 ILE ILE B . n 
B 1 431 GLU 431 431 431 GLU GLU B . n 
B 1 432 SER 432 432 432 SER SER B . n 
B 1 433 HIS 433 433 433 HIS HIS B . n 
C 2 1   ARG 1   522 ?   ?   ?   C . n 
C 2 2   MET 2   523 ?   ?   ?   C . n 
C 2 3   LYS 3   524 ?   ?   ?   C . n 
C 2 4   LEU 4   525 ?   ?   ?   C . n 
C 2 5   THR 5   526 526 THR THR C . n 
C 2 6   LEU 6   527 527 LEU LEU C . n 
C 2 7   LYS 7   528 528 LYS LYS C . n 
C 2 8   GLY 8   529 529 GLY GLY C . n 
C 2 9   GLY 9   530 530 GLY GLY C . n 
C 2 10  ALA 10  531 531 ALA ALA C . n 
C 2 11  ALA 11  532 ?   ?   ?   C . n 
C 2 12  VAL 12  533 ?   ?   ?   C . n 
C 2 13  ASP 13  534 ?   ?   ?   C . n 
D 2 1   ARG 1   522 ?   ?   ?   D . n 
D 2 2   MET 2   523 ?   ?   ?   D . n 
D 2 3   LYS 3   524 ?   ?   ?   D . n 
D 2 4   LEU 4   525 ?   ?   ?   D . n 
D 2 5   THR 5   526 526 THR THR D . n 
D 2 6   LEU 6   527 527 LEU LEU D . n 
D 2 7   LYS 7   528 528 LYS LYS D . n 
D 2 8   GLY 8   529 529 GLY GLY D . n 
D 2 9   GLY 9   530 ?   ?   ?   D . n 
D 2 10  ALA 10  531 ?   ?   ?   D . n 
D 2 11  ALA 11  532 ?   ?   ?   D . n 
D 2 12  VAL 12  533 ?   ?   ?   D . n 
D 2 13  ASP 13  534 ?   ?   ?   D . n 
E 2 1   ARG 1   522 522 ARG ARG E . n 
E 2 2   MET 2   523 523 MET MET E . n 
E 2 3   LYS 3   524 524 LYS LYS E . n 
E 2 4   LEU 4   525 525 LEU LEU E . n 
E 2 5   THR 5   526 ?   ?   ?   E . n 
E 2 6   LEU 6   527 ?   ?   ?   E . n 
E 2 7   LYS 7   528 ?   ?   ?   E . n 
E 2 8   GLY 8   529 ?   ?   ?   E . n 
E 2 9   GLY 9   530 ?   ?   ?   E . n 
E 2 10  ALA 10  531 ?   ?   ?   E . n 
E 2 11  ALA 11  532 ?   ?   ?   E . n 
E 2 12  VAL 12  533 ?   ?   ?   E . n 
E 2 13  ASP 13  534 ?   ?   ?   E . n 
F 2 1   ARG 1   522 522 ARG ARG F . n 
F 2 2   MET 2   523 523 MET MET F . n 
F 2 3   LYS 3   524 524 LYS LYS F . n 
F 2 4   LEU 4   525 525 LEU LEU F . n 
F 2 5   THR 5   526 526 THR THR F . n 
F 2 6   LEU 6   527 527 LEU LEU F . n 
F 2 7   LYS 7   528 ?   ?   ?   F . n 
F 2 8   GLY 8   529 ?   ?   ?   F . n 
F 2 9   GLY 9   530 ?   ?   ?   F . n 
F 2 10  ALA 10  531 ?   ?   ?   F . n 
F 2 11  ALA 11  532 ?   ?   ?   F . n 
F 2 12  VAL 12  533 ?   ?   ?   F . n 
F 2 13  ASP 13  534 ?   ?   ?   F . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G 3 SAH 1   501 1   SAH SAH A . 
H 4 ZN  1   502 1   ZN  ZN  A . 
I 4 ZN  1   503 2   ZN  ZN  A . 
J 4 ZN  1   504 3   ZN  ZN  A . 
K 3 SAH 1   501 2   SAH SAH B . 
L 4 ZN  1   502 101 ZN  ZN  B . 
M 4 ZN  1   503 102 ZN  ZN  B . 
N 4 ZN  1   504 103 ZN  ZN  B . 
O 5 HOH 1   601 128 HOH HOH A . 
O 5 HOH 2   602 126 HOH HOH A . 
O 5 HOH 3   603 169 HOH HOH A . 
O 5 HOH 4   604 375 HOH HOH A . 
O 5 HOH 5   605 320 HOH HOH A . 
O 5 HOH 6   606 62  HOH HOH A . 
O 5 HOH 7   607 228 HOH HOH A . 
O 5 HOH 8   608 117 HOH HOH A . 
O 5 HOH 9   609 127 HOH HOH A . 
O 5 HOH 10  610 14  HOH HOH A . 
O 5 HOH 11  611 131 HOH HOH A . 
O 5 HOH 12  612 322 HOH HOH A . 
O 5 HOH 13  613 129 HOH HOH A . 
O 5 HOH 14  614 54  HOH HOH A . 
O 5 HOH 15  615 311 HOH HOH A . 
O 5 HOH 16  616 24  HOH HOH A . 
O 5 HOH 17  617 140 HOH HOH A . 
O 5 HOH 18  618 83  HOH HOH A . 
O 5 HOH 19  619 303 HOH HOH A . 
O 5 HOH 20  620 146 HOH HOH A . 
O 5 HOH 21  621 100 HOH HOH A . 
O 5 HOH 22  622 121 HOH HOH A . 
O 5 HOH 23  623 381 HOH HOH A . 
O 5 HOH 24  624 160 HOH HOH A . 
O 5 HOH 25  625 35  HOH HOH A . 
O 5 HOH 26  626 49  HOH HOH A . 
O 5 HOH 27  627 43  HOH HOH A . 
O 5 HOH 28  628 376 HOH HOH A . 
O 5 HOH 29  629 15  HOH HOH A . 
O 5 HOH 30  630 97  HOH HOH A . 
O 5 HOH 31  631 79  HOH HOH A . 
O 5 HOH 32  632 89  HOH HOH A . 
O 5 HOH 33  633 373 HOH HOH A . 
O 5 HOH 34  634 125 HOH HOH A . 
O 5 HOH 35  635 84  HOH HOH A . 
O 5 HOH 36  636 326 HOH HOH A . 
O 5 HOH 37  637 70  HOH HOH A . 
O 5 HOH 38  638 1   HOH HOH A . 
O 5 HOH 39  639 192 HOH HOH A . 
O 5 HOH 40  640 166 HOH HOH A . 
O 5 HOH 41  641 235 HOH HOH A . 
O 5 HOH 42  642 92  HOH HOH A . 
O 5 HOH 43  643 188 HOH HOH A . 
O 5 HOH 44  644 37  HOH HOH A . 
O 5 HOH 45  645 197 HOH HOH A . 
O 5 HOH 46  646 142 HOH HOH A . 
O 5 HOH 47  647 323 HOH HOH A . 
O 5 HOH 48  648 363 HOH HOH A . 
O 5 HOH 49  649 132 HOH HOH A . 
O 5 HOH 50  650 10  HOH HOH A . 
O 5 HOH 51  651 257 HOH HOH A . 
O 5 HOH 52  652 118 HOH HOH A . 
O 5 HOH 53  653 220 HOH HOH A . 
O 5 HOH 54  654 234 HOH HOH A . 
O 5 HOH 55  655 133 HOH HOH A . 
O 5 HOH 56  656 279 HOH HOH A . 
O 5 HOH 57  657 22  HOH HOH A . 
O 5 HOH 58  658 44  HOH HOH A . 
O 5 HOH 59  659 208 HOH HOH A . 
O 5 HOH 60  660 78  HOH HOH A . 
O 5 HOH 61  661 105 HOH HOH A . 
O 5 HOH 62  662 31  HOH HOH A . 
O 5 HOH 63  663 177 HOH HOH A . 
O 5 HOH 64  664 11  HOH HOH A . 
O 5 HOH 65  665 170 HOH HOH A . 
O 5 HOH 66  666 5   HOH HOH A . 
O 5 HOH 67  667 21  HOH HOH A . 
O 5 HOH 68  668 387 HOH HOH A . 
O 5 HOH 69  669 111 HOH HOH A . 
O 5 HOH 70  670 186 HOH HOH A . 
O 5 HOH 71  671 51  HOH HOH A . 
O 5 HOH 72  672 3   HOH HOH A . 
O 5 HOH 73  673 365 HOH HOH A . 
O 5 HOH 74  674 66  HOH HOH A . 
O 5 HOH 75  675 130 HOH HOH A . 
O 5 HOH 76  676 65  HOH HOH A . 
O 5 HOH 77  677 68  HOH HOH A . 
O 5 HOH 78  678 343 HOH HOH A . 
O 5 HOH 79  679 226 HOH HOH A . 
O 5 HOH 80  680 139 HOH HOH A . 
O 5 HOH 81  681 210 HOH HOH A . 
O 5 HOH 82  682 309 HOH HOH A . 
O 5 HOH 83  683 61  HOH HOH A . 
O 5 HOH 84  684 124 HOH HOH A . 
O 5 HOH 85  685 75  HOH HOH A . 
O 5 HOH 86  686 74  HOH HOH A . 
O 5 HOH 87  687 101 HOH HOH A . 
O 5 HOH 88  688 2   HOH HOH A . 
O 5 HOH 89  689 356 HOH HOH A . 
O 5 HOH 90  690 165 HOH HOH A . 
O 5 HOH 91  691 182 HOH HOH A . 
O 5 HOH 92  692 353 HOH HOH A . 
O 5 HOH 93  693 219 HOH HOH A . 
O 5 HOH 94  694 52  HOH HOH A . 
O 5 HOH 95  695 336 HOH HOH A . 
O 5 HOH 96  696 364 HOH HOH A . 
O 5 HOH 97  697 67  HOH HOH A . 
O 5 HOH 98  698 385 HOH HOH A . 
O 5 HOH 99  699 212 HOH HOH A . 
O 5 HOH 100 700 36  HOH HOH A . 
O 5 HOH 101 701 266 HOH HOH A . 
O 5 HOH 102 702 173 HOH HOH A . 
O 5 HOH 103 703 40  HOH HOH A . 
O 5 HOH 104 704 193 HOH HOH A . 
O 5 HOH 105 705 48  HOH HOH A . 
O 5 HOH 106 706 271 HOH HOH A . 
O 5 HOH 107 707 41  HOH HOH A . 
O 5 HOH 108 708 216 HOH HOH A . 
O 5 HOH 109 709 222 HOH HOH A . 
O 5 HOH 110 710 138 HOH HOH A . 
O 5 HOH 111 711 262 HOH HOH A . 
O 5 HOH 112 712 291 HOH HOH A . 
O 5 HOH 113 713 230 HOH HOH A . 
O 5 HOH 114 714 167 HOH HOH A . 
O 5 HOH 115 715 8   HOH HOH A . 
O 5 HOH 116 716 60  HOH HOH A . 
O 5 HOH 117 717 28  HOH HOH A . 
O 5 HOH 118 718 201 HOH HOH A . 
O 5 HOH 119 719 328 HOH HOH A . 
O 5 HOH 120 720 263 HOH HOH A . 
O 5 HOH 121 721 259 HOH HOH A . 
O 5 HOH 122 722 64  HOH HOH A . 
O 5 HOH 123 723 252 HOH HOH A . 
O 5 HOH 124 724 96  HOH HOH A . 
O 5 HOH 125 725 106 HOH HOH A . 
O 5 HOH 126 726 19  HOH HOH A . 
O 5 HOH 127 727 25  HOH HOH A . 
O 5 HOH 128 728 207 HOH HOH A . 
O 5 HOH 129 729 33  HOH HOH A . 
O 5 HOH 130 730 93  HOH HOH A . 
O 5 HOH 131 731 299 HOH HOH A . 
O 5 HOH 132 732 396 HOH HOH A . 
O 5 HOH 133 733 211 HOH HOH A . 
O 5 HOH 134 734 42  HOH HOH A . 
O 5 HOH 135 735 151 HOH HOH A . 
O 5 HOH 136 736 17  HOH HOH A . 
O 5 HOH 137 737 191 HOH HOH A . 
O 5 HOH 138 738 174 HOH HOH A . 
O 5 HOH 139 739 391 HOH HOH A . 
O 5 HOH 140 740 164 HOH HOH A . 
O 5 HOH 141 741 274 HOH HOH A . 
O 5 HOH 142 742 242 HOH HOH A . 
O 5 HOH 143 743 265 HOH HOH A . 
O 5 HOH 144 744 59  HOH HOH A . 
O 5 HOH 145 745 195 HOH HOH A . 
O 5 HOH 146 746 55  HOH HOH A . 
O 5 HOH 147 747 390 HOH HOH A . 
O 5 HOH 148 748 280 HOH HOH A . 
O 5 HOH 149 749 368 HOH HOH A . 
O 5 HOH 150 750 77  HOH HOH A . 
O 5 HOH 151 751 236 HOH HOH A . 
O 5 HOH 152 752 256 HOH HOH A . 
O 5 HOH 153 753 94  HOH HOH A . 
O 5 HOH 154 754 282 HOH HOH A . 
O 5 HOH 155 755 321 HOH HOH A . 
O 5 HOH 156 756 388 HOH HOH A . 
O 5 HOH 157 757 254 HOH HOH A . 
O 5 HOH 158 758 34  HOH HOH A . 
O 5 HOH 159 759 38  HOH HOH A . 
O 5 HOH 160 760 253 HOH HOH A . 
O 5 HOH 161 761 80  HOH HOH A . 
O 5 HOH 162 762 204 HOH HOH A . 
O 5 HOH 163 763 57  HOH HOH A . 
O 5 HOH 164 764 162 HOH HOH A . 
O 5 HOH 165 765 156 HOH HOH A . 
O 5 HOH 166 766 46  HOH HOH A . 
O 5 HOH 167 767 294 HOH HOH A . 
O 5 HOH 168 768 398 HOH HOH A . 
O 5 HOH 169 769 98  HOH HOH A . 
O 5 HOH 170 770 20  HOH HOH A . 
O 5 HOH 171 771 213 HOH HOH A . 
O 5 HOH 172 772 72  HOH HOH A . 
O 5 HOH 173 773 250 HOH HOH A . 
O 5 HOH 174 774 386 HOH HOH A . 
O 5 HOH 175 775 4   HOH HOH A . 
O 5 HOH 176 776 227 HOH HOH A . 
O 5 HOH 177 777 276 HOH HOH A . 
O 5 HOH 178 778 141 HOH HOH A . 
O 5 HOH 179 779 338 HOH HOH A . 
O 5 HOH 180 780 82  HOH HOH A . 
O 5 HOH 181 781 184 HOH HOH A . 
O 5 HOH 182 782 369 HOH HOH A . 
O 5 HOH 183 783 203 HOH HOH A . 
O 5 HOH 184 784 194 HOH HOH A . 
O 5 HOH 185 785 301 HOH HOH A . 
O 5 HOH 186 786 150 HOH HOH A . 
O 5 HOH 187 787 312 HOH HOH A . 
O 5 HOH 188 788 175 HOH HOH A . 
O 5 HOH 189 789 198 HOH HOH A . 
O 5 HOH 190 790 155 HOH HOH A . 
O 5 HOH 191 791 306 HOH HOH A . 
O 5 HOH 192 792 335 HOH HOH A . 
O 5 HOH 193 793 337 HOH HOH A . 
O 5 HOH 194 794 297 HOH HOH A . 
O 5 HOH 195 795 161 HOH HOH A . 
O 5 HOH 196 796 378 HOH HOH A . 
O 5 HOH 197 797 300 HOH HOH A . 
O 5 HOH 198 798 39  HOH HOH A . 
O 5 HOH 199 799 383 HOH HOH A . 
O 5 HOH 200 800 229 HOH HOH A . 
O 5 HOH 201 801 393 HOH HOH A . 
O 5 HOH 202 802 123 HOH HOH A . 
O 5 HOH 203 803 357 HOH HOH A . 
O 5 HOH 204 804 333 HOH HOH A . 
O 5 HOH 205 805 389 HOH HOH A . 
O 5 HOH 206 806 29  HOH HOH A . 
O 5 HOH 207 807 403 HOH HOH A . 
O 5 HOH 208 808 395 HOH HOH A . 
O 5 HOH 209 809 267 HOH HOH A . 
O 5 HOH 210 810 221 HOH HOH A . 
O 5 HOH 211 811 217 HOH HOH A . 
O 5 HOH 212 812 329 HOH HOH A . 
O 5 HOH 213 813 418 HOH HOH A . 
O 5 HOH 214 814 270 HOH HOH A . 
O 5 HOH 215 815 350 HOH HOH A . 
O 5 HOH 216 816 205 HOH HOH A . 
O 5 HOH 217 817 295 HOH HOH A . 
O 5 HOH 218 818 233 HOH HOH A . 
O 5 HOH 219 819 47  HOH HOH A . 
O 5 HOH 220 820 277 HOH HOH A . 
O 5 HOH 221 821 232 HOH HOH A . 
O 5 HOH 222 822 318 HOH HOH A . 
O 5 HOH 223 823 412 HOH HOH A . 
O 5 HOH 224 824 171 HOH HOH A . 
O 5 HOH 225 825 137 HOH HOH A . 
O 5 HOH 226 826 349 HOH HOH A . 
O 5 HOH 227 827 414 HOH HOH A . 
O 5 HOH 228 828 347 HOH HOH A . 
O 5 HOH 229 829 367 HOH HOH A . 
O 5 HOH 230 830 293 HOH HOH A . 
O 5 HOH 231 831 290 HOH HOH A . 
O 5 HOH 232 832 88  HOH HOH A . 
O 5 HOH 233 833 224 HOH HOH A . 
O 5 HOH 234 834 341 HOH HOH A . 
O 5 HOH 235 835 352 HOH HOH A . 
O 5 HOH 236 836 302 HOH HOH A . 
O 5 HOH 237 837 23  HOH HOH A . 
O 5 HOH 238 838 374 HOH HOH A . 
O 5 HOH 239 839 346 HOH HOH A . 
O 5 HOH 240 840 183 HOH HOH A . 
O 5 HOH 241 841 281 HOH HOH A . 
O 5 HOH 242 842 380 HOH HOH A . 
O 5 HOH 243 843 325 HOH HOH A . 
O 5 HOH 244 844 225 HOH HOH A . 
O 5 HOH 245 845 372 HOH HOH A . 
O 5 HOH 246 846 147 HOH HOH A . 
O 5 HOH 247 847 355 HOH HOH A . 
O 5 HOH 248 848 202 HOH HOH A . 
O 5 HOH 249 849 296 HOH HOH A . 
O 5 HOH 250 850 362 HOH HOH A . 
O 5 HOH 251 851 319 HOH HOH A . 
O 5 HOH 252 852 415 HOH HOH A . 
O 5 HOH 253 853 419 HOH HOH A . 
O 5 HOH 254 854 223 HOH HOH A . 
O 5 HOH 255 855 410 HOH HOH A . 
O 5 HOH 256 856 402 HOH HOH A . 
O 5 HOH 257 857 344 HOH HOH A . 
O 5 HOH 258 858 411 HOH HOH A . 
O 5 HOH 259 859 420 HOH HOH A . 
O 5 HOH 260 860 115 HOH HOH A . 
O 5 HOH 261 861 209 HOH HOH A . 
O 5 HOH 262 862 231 HOH HOH A . 
O 5 HOH 263 863 283 HOH HOH A . 
O 5 HOH 264 864 258 HOH HOH A . 
O 5 HOH 265 865 401 HOH HOH A . 
O 5 HOH 266 866 218 HOH HOH A . 
O 5 HOH 267 867 292 HOH HOH A . 
O 5 HOH 268 868 314 HOH HOH A . 
P 5 HOH 1   601 134 HOH HOH B . 
P 5 HOH 2   602 316 HOH HOH B . 
P 5 HOH 3   603 345 HOH HOH B . 
P 5 HOH 4   604 246 HOH HOH B . 
P 5 HOH 5   605 143 HOH HOH B . 
P 5 HOH 6   606 152 HOH HOH B . 
P 5 HOH 7   607 104 HOH HOH B . 
P 5 HOH 8   608 58  HOH HOH B . 
P 5 HOH 9   609 181 HOH HOH B . 
P 5 HOH 10  610 119 HOH HOH B . 
P 5 HOH 11  611 85  HOH HOH B . 
P 5 HOH 12  612 379 HOH HOH B . 
P 5 HOH 13  613 288 HOH HOH B . 
P 5 HOH 14  614 27  HOH HOH B . 
P 5 HOH 15  615 239 HOH HOH B . 
P 5 HOH 16  616 340 HOH HOH B . 
P 5 HOH 17  617 120 HOH HOH B . 
P 5 HOH 18  618 26  HOH HOH B . 
P 5 HOH 19  619 248 HOH HOH B . 
P 5 HOH 20  620 50  HOH HOH B . 
P 5 HOH 21  621 157 HOH HOH B . 
P 5 HOH 22  622 63  HOH HOH B . 
P 5 HOH 23  623 249 HOH HOH B . 
P 5 HOH 24  624 154 HOH HOH B . 
P 5 HOH 25  625 238 HOH HOH B . 
P 5 HOH 26  626 190 HOH HOH B . 
P 5 HOH 27  627 109 HOH HOH B . 
P 5 HOH 28  628 244 HOH HOH B . 
P 5 HOH 29  629 144 HOH HOH B . 
P 5 HOH 30  630 99  HOH HOH B . 
P 5 HOH 31  631 215 HOH HOH B . 
P 5 HOH 32  632 102 HOH HOH B . 
P 5 HOH 33  633 30  HOH HOH B . 
P 5 HOH 34  634 172 HOH HOH B . 
P 5 HOH 35  635 81  HOH HOH B . 
P 5 HOH 36  636 90  HOH HOH B . 
P 5 HOH 37  637 237 HOH HOH B . 
P 5 HOH 38  638 16  HOH HOH B . 
P 5 HOH 39  639 255 HOH HOH B . 
P 5 HOH 40  640 91  HOH HOH B . 
P 5 HOH 41  641 289 HOH HOH B . 
P 5 HOH 42  642 148 HOH HOH B . 
P 5 HOH 43  643 56  HOH HOH B . 
P 5 HOH 44  644 247 HOH HOH B . 
P 5 HOH 45  645 110 HOH HOH B . 
P 5 HOH 46  646 163 HOH HOH B . 
P 5 HOH 47  647 73  HOH HOH B . 
P 5 HOH 48  648 159 HOH HOH B . 
P 5 HOH 49  649 53  HOH HOH B . 
P 5 HOH 50  650 153 HOH HOH B . 
P 5 HOH 51  651 136 HOH HOH B . 
P 5 HOH 52  652 200 HOH HOH B . 
P 5 HOH 53  653 360 HOH HOH B . 
P 5 HOH 54  654 107 HOH HOH B . 
P 5 HOH 55  655 114 HOH HOH B . 
P 5 HOH 56  656 9   HOH HOH B . 
P 5 HOH 57  657 377 HOH HOH B . 
P 5 HOH 58  658 354 HOH HOH B . 
P 5 HOH 59  659 358 HOH HOH B . 
P 5 HOH 60  660 187 HOH HOH B . 
P 5 HOH 61  661 241 HOH HOH B . 
P 5 HOH 62  662 32  HOH HOH B . 
P 5 HOH 63  663 45  HOH HOH B . 
P 5 HOH 64  664 285 HOH HOH B . 
P 5 HOH 65  665 7   HOH HOH B . 
P 5 HOH 66  666 122 HOH HOH B . 
P 5 HOH 67  667 76  HOH HOH B . 
P 5 HOH 68  668 176 HOH HOH B . 
P 5 HOH 69  669 284 HOH HOH B . 
P 5 HOH 70  670 214 HOH HOH B . 
P 5 HOH 71  671 298 HOH HOH B . 
P 5 HOH 72  672 359 HOH HOH B . 
P 5 HOH 73  673 407 HOH HOH B . 
P 5 HOH 74  674 6   HOH HOH B . 
P 5 HOH 75  675 71  HOH HOH B . 
P 5 HOH 76  676 310 HOH HOH B . 
P 5 HOH 77  677 18  HOH HOH B . 
P 5 HOH 78  678 189 HOH HOH B . 
P 5 HOH 79  679 397 HOH HOH B . 
P 5 HOH 80  680 185 HOH HOH B . 
P 5 HOH 81  681 149 HOH HOH B . 
P 5 HOH 82  682 12  HOH HOH B . 
P 5 HOH 83  683 334 HOH HOH B . 
P 5 HOH 84  684 116 HOH HOH B . 
P 5 HOH 85  685 86  HOH HOH B . 
P 5 HOH 86  686 371 HOH HOH B . 
P 5 HOH 87  687 361 HOH HOH B . 
P 5 HOH 88  688 251 HOH HOH B . 
P 5 HOH 89  689 331 HOH HOH B . 
P 5 HOH 90  690 307 HOH HOH B . 
P 5 HOH 91  691 95  HOH HOH B . 
P 5 HOH 92  692 69  HOH HOH B . 
P 5 HOH 93  693 168 HOH HOH B . 
P 5 HOH 94  694 330 HOH HOH B . 
P 5 HOH 95  695 324 HOH HOH B . 
P 5 HOH 96  696 269 HOH HOH B . 
P 5 HOH 97  697 278 HOH HOH B . 
P 5 HOH 98  698 179 HOH HOH B . 
P 5 HOH 99  699 103 HOH HOH B . 
P 5 HOH 100 700 400 HOH HOH B . 
P 5 HOH 101 701 108 HOH HOH B . 
P 5 HOH 102 702 87  HOH HOH B . 
P 5 HOH 103 703 261 HOH HOH B . 
P 5 HOH 104 704 178 HOH HOH B . 
P 5 HOH 105 705 180 HOH HOH B . 
P 5 HOH 106 706 327 HOH HOH B . 
P 5 HOH 107 707 13  HOH HOH B . 
P 5 HOH 108 708 404 HOH HOH B . 
P 5 HOH 109 709 245 HOH HOH B . 
P 5 HOH 110 710 370 HOH HOH B . 
P 5 HOH 111 711 392 HOH HOH B . 
P 5 HOH 112 712 416 HOH HOH B . 
P 5 HOH 113 713 240 HOH HOH B . 
P 5 HOH 114 714 413 HOH HOH B . 
P 5 HOH 115 715 199 HOH HOH B . 
P 5 HOH 116 716 366 HOH HOH B . 
P 5 HOH 117 717 112 HOH HOH B . 
P 5 HOH 118 718 275 HOH HOH B . 
P 5 HOH 119 719 409 HOH HOH B . 
P 5 HOH 120 720 305 HOH HOH B . 
P 5 HOH 121 721 264 HOH HOH B . 
P 5 HOH 122 722 405 HOH HOH B . 
P 5 HOH 123 723 113 HOH HOH B . 
P 5 HOH 124 724 304 HOH HOH B . 
P 5 HOH 125 725 408 HOH HOH B . 
P 5 HOH 126 726 196 HOH HOH B . 
P 5 HOH 127 727 260 HOH HOH B . 
P 5 HOH 128 728 268 HOH HOH B . 
P 5 HOH 129 729 351 HOH HOH B . 
P 5 HOH 130 730 135 HOH HOH B . 
P 5 HOH 131 731 317 HOH HOH B . 
P 5 HOH 132 732 286 HOH HOH B . 
P 5 HOH 133 733 406 HOH HOH B . 
P 5 HOH 134 734 158 HOH HOH B . 
P 5 HOH 135 735 272 HOH HOH B . 
P 5 HOH 136 736 342 HOH HOH B . 
P 5 HOH 137 737 339 HOH HOH B . 
P 5 HOH 138 738 384 HOH HOH B . 
P 5 HOH 139 739 315 HOH HOH B . 
P 5 HOH 140 740 287 HOH HOH B . 
P 5 HOH 141 741 145 HOH HOH B . 
P 5 HOH 142 742 308 HOH HOH B . 
P 5 HOH 143 743 206 HOH HOH B . 
P 5 HOH 144 744 417 HOH HOH B . 
Q 5 HOH 1   601 332 HOH HOH C . 
Q 5 HOH 2   602 394 HOH HOH C . 
R 5 HOH 1   601 313 HOH HOH D . 
R 5 HOH 2   602 382 HOH HOH D . 
S 5 HOH 1   601 348 HOH HOH E . 
T 5 HOH 1   601 243 HOH HOH F . 
T 5 HOH 2   602 399 HOH HOH F . 
T 5 HOH 3   603 273 HOH HOH F . 
# 
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  ? ? ? 1.16_3549 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   113.242 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CKC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     142.792 
_cell.length_a_esd                 ? 
_cell.length_b                     52.185 
_cell.length_b_esd                 ? 
_cell.length_c                     144.916 
_cell.length_c_esd                 ? 
_cell.volume                       992221.839 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CKC 
_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                   9CKC 
_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             2.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.21 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_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    '20% PEG3350, 100 mM Tris pH 7.5, 5% ethanol, 1 mM PARP1 peptide, 0.6 mM AdoHcy' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 225 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-07-22 
_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   0.97856 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 21-ID-F' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97856 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-F 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          32.26 
_reflns.entry_id                                       9CKC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               133.16 
_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                                     57685 
_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                           88.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.114 
_reflns.pdbx_Rpim_I_all                                0.042 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.105 
_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                                    2.1 
_reflns_shell.d_res_low                                     2.137 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             51097 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.505 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.772 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.7 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.862 
_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                               47.37 
_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                                 9CKC 
_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                            2.10 
_refine.ls_d_res_low                             66.58 
_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                     51079 
_refine.ls_number_reflns_R_free                  2578 
_refine.ls_number_reflns_R_work                  48501 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    88.57 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1851 
_refine.ls_R_factor_R_free                       0.2079 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1839 
_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                          0.31 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_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                 22.7534 
_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                            0.2174 
_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                       2.10 
_refine_hist.d_res_low                        66.58 
_refine_hist.number_atoms_solvent             420 
_refine_hist.number_atoms_total               7545 
_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        7067 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         58 
_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' ? 0.0042  ? 7303 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7180  ? 9842 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0463  ? 1052 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0045  ? 1263 ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.1482 ? 2794 ? 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' 2.10 2.14  . . 140 2968 99.97  . . . . 0.2649 . . . . . . . . . . . 0.2696 
'X-RAY DIFFRACTION' 2.14 2.19  . . 161 3041 99.81  . . . . 0.2520 . . . . . . . . . . . 0.3100 
'X-RAY DIFFRACTION' 2.19 2.23  . . 79  1642 91.98  . . . . 0.2594 . . . . . . . . . . . 0.2629 
'X-RAY DIFFRACTION' 2.28 2.34  . . 140 2719 92.82  . . . . 0.2315 . . . . . . . . . . . 0.2866 
'X-RAY DIFFRACTION' 2.34 2.41  . . 176 2987 99.97  . . . . 0.2179 . . . . . . . . . . . 0.2368 
'X-RAY DIFFRACTION' 2.41 2.48  . . 155 3047 100.00 . . . . 0.2188 . . . . . . . . . . . 0.2244 
'X-RAY DIFFRACTION' 2.48 2.56  . . 179 2992 99.97  . . . . 0.2170 . . . . . . . . . . . 0.2530 
'X-RAY DIFFRACTION' 2.56 2.65  . . 164 3039 100.00 . . . . 0.2196 . . . . . . . . . . . 0.2552 
'X-RAY DIFFRACTION' 2.65 2.75  . . 102 2120 69.76  . . . . 0.2262 . . . . . . . . . . . 0.2435 
'X-RAY DIFFRACTION' 2.75 2.88  . . 162 3046 100.00 . . . . 0.2139 . . . . . . . . . . . 0.2464 
'X-RAY DIFFRACTION' 2.88 3.03  . . 171 3030 99.84  . . . . 0.2153 . . . . . . . . . . . 0.2686 
'X-RAY DIFFRACTION' 3.03 3.22  . . 155 3034 99.97  . . . . 0.2103 . . . . . . . . . . . 0.2197 
'X-RAY DIFFRACTION' 3.22 3.47  . . 141 2693 87.82  . . . . 0.1817 . . . . . . . . . . . 0.2105 
'X-RAY DIFFRACTION' 3.47 3.82  . . 149 2863 94.30  . . . . 0.1595 . . . . . . . . . . . 0.1767 
'X-RAY DIFFRACTION' 3.82 4.37  . . 159 3025 98.18  . . . . 0.1411 . . . . . . . . . . . 0.1550 
'X-RAY DIFFRACTION' 4.37 5.51  . . 175 3083 99.94  . . . . 0.1356 . . . . . . . . . . . 0.1625 
'X-RAY DIFFRACTION' 5.51 66.58 . . 170 3172 99.58  . . . . 0.1649 . . . . . . . . . . . 0.1782 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1 1 ? 
2 1 ? 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
1 1 1 A GLY 5   . A PHE 34  . A GLY 5   A PHE 34  ? 
;(chain 'A' and (resid 5 through 34 or resid 36 through 250 or resid 252 through 306 or resid 308 through 323 or resid 325 through 433))
;
1 1 2 A CYS 36  . A ARG 250 . A CYS 36  A ARG 250 ? 
;(chain 'A' and (resid 5 through 34 or resid 36 through 250 or resid 252 through 306 or resid 308 through 323 or resid 325 through 433))
;
1 1 3 A ASP 252 . A ARG 306 . A ASP 252 A ARG 306 ? 
;(chain 'A' and (resid 5 through 34 or resid 36 through 250 or resid 252 through 306 or resid 308 through 323 or resid 325 through 433))
;
1 1 4 A ALA 308 . A LEU 323 . A ALA 308 A LEU 323 ? 
;(chain 'A' and (resid 5 through 34 or resid 36 through 250 or resid 252 through 306 or resid 308 through 323 or resid 325 through 433))
;
1 1 5 A GLN 325 . A HIS 433 . A GLN 325 A HIS 433 ? 
;(chain 'A' and (resid 5 through 34 or resid 36 through 250 or resid 252 through 306 or resid 308 through 323 or resid 325 through 433))
;
1 2 1 B GLY 5   . B PHE 34  . B GLY 5   B PHE 34  ? 
;(chain 'B' and (resid 5 through 34 or resid 36 through 250 or resid 252 through 306 or resid 308 through 323 or resid 325 through 433))
;
1 2 2 B CYS 36  . B ARG 250 . B CYS 36  B ARG 250 ? 
;(chain 'B' and (resid 5 through 34 or resid 36 through 250 or resid 252 through 306 or resid 308 through 323 or resid 325 through 433))
;
1 2 3 B ASP 252 . B ARG 306 . B ASP 252 B ARG 306 ? 
;(chain 'B' and (resid 5 through 34 or resid 36 through 250 or resid 252 through 306 or resid 308 through 323 or resid 325 through 433))
;
1 2 4 B ALA 308 . B LEU 323 . B ALA 308 B LEU 323 ? 
;(chain 'B' and (resid 5 through 34 or resid 36 through 250 or resid 252 through 306 or resid 308 through 323 or resid 325 through 433))
;
1 2 5 B GLN 325 . B HIS 433 . B GLN 325 B HIS 433 ? 
;(chain 'B' and (resid 5 through 34 or resid 36 through 250 or resid 252 through 306 or resid 308 through 323 or resid 325 through 433))
;
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                     9CKC 
_struct.title                        'Crystal structure of SMYD2 in complex with two PARP1 peptides' 
_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        9CKC 
_struct_keywords.text            'SMYD2, PARP1, Methyltransferase, SET and MYND-containing protein, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 3 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
O N N 5 ? 
P N N 5 ? 
Q N N 5 ? 
R N N 5 ? 
S N N 5 ? 
T N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SMYD2_HUMAN Q9NRG4 ? 1 
;MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQK
EDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFY
SKHLGFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSY
IDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEI
CELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAA
GEKALKKAIAIMEVAHGKDHPYISEIKQEIESH
;
1   
2 UNP PARP1_HUMAN P09874 ? 2 RMKLTLKGGAAVD 522 
# 
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 9CKC A 1 ? 433 ? Q9NRG4 1   ? 433 ? 1   433 
2 1 9CKC B 1 ? 433 ? Q9NRG4 1   ? 433 ? 1   433 
3 2 9CKC C 1 ? 13  ? P09874 522 ? 534 ? 522 534 
4 2 9CKC D 1 ? 13  ? P09874 522 ? 534 ? 522 534 
5 2 9CKC E 1 ? 13  ? P09874 522 ? 534 ? 522 534 
6 2 9CKC F 1 ? 13  ? P09874 522 ? 534 ? 522 534 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CKC GLU A 165 ? UNP Q9NRG4 GLY 165 conflict 165 1 
2 9CKC GLU B 165 ? UNP Q9NRG4 GLY 165 conflict 165 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA trimeric 3 
2 author_and_software_defined_assembly PISA trimeric 3 
# 
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)' 1950  ? 
1 MORE         -7    ? 
1 'SSA (A^2)'  20610 ? 
2 'ABSA (A^2)' 1780  ? 
2 MORE         -9    ? 
2 'SSA (A^2)'  20680 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E,G,H,I,J,O,Q,S 
2 1 B,D,F,K,L,M,N,P,R,T 
# 
_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 VAL A 45  ? ARG A 48  ? VAL A 45  ARG A 48  5 ? 4  
HELX_P HELX_P2  AA2 ASN A 75  ? LYS A 87  ? ASN A 75  LYS A 87  1 ? 13 
HELX_P HELX_P3  AA3 GLU A 89  ? GLY A 97  ? GLU A 89  GLY A 97  1 ? 9  
HELX_P HELX_P4  AA4 GLU A 98  ? TRP A 100 ? GLU A 98  TRP A 100 5 ? 3  
HELX_P HELX_P5  AA5 SER A 103 ? HIS A 119 ? SER A 103 HIS A 119 1 ? 17 
HELX_P HELX_P6  AA6 ALA A 130 ? PHE A 134 ? ALA A 130 PHE A 134 5 ? 5  
HELX_P HELX_P7  AA7 HIS A 137 ? LEU A 141 ? HIS A 137 LEU A 141 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 142 ? SER A 161 ? ASP A 142 SER A 161 1 ? 20 
HELX_P HELX_P9  AA9 ASP A 168 ? GLY A 183 ? ASP A 168 GLY A 183 1 ? 16 
HELX_P HELX_P10 AB1 PHE A 199 ? LEU A 204 ? PHE A 199 LEU A 204 1 ? 6  
HELX_P HELX_P11 AB2 PRO A 246 ? PHE A 259 ? PRO A 246 PHE A 259 1 ? 14 
HELX_P HELX_P12 AB3 CYS A 264 ? LYS A 270 ? CYS A 264 LYS A 270 1 ? 7  
HELX_P HELX_P13 AB4 LYS A 272 ? VAL A 277 ? LYS A 272 VAL A 277 1 ? 6  
HELX_P HELX_P14 AB5 LYS A 287 ? LYS A 309 ? LYS A 287 LYS A 309 1 ? 23 
HELX_P HELX_P15 AB6 SER A 313 ? SER A 330 ? SER A 313 SER A 330 1 ? 18 
HELX_P HELX_P16 AB7 ASN A 336 ? MET A 353 ? ASN A 336 MET A 353 1 ? 18 
HELX_P HELX_P17 AB8 ASP A 355 ? TYR A 374 ? ASP A 355 TYR A 374 1 ? 20 
HELX_P HELX_P18 AB9 SER A 378 ? LEU A 395 ? SER A 378 LEU A 395 1 ? 18 
HELX_P HELX_P19 AC1 HIS A 397 ? GLY A 417 ? HIS A 397 GLY A 417 1 ? 21 
HELX_P HELX_P20 AC2 HIS A 420 ? GLU A 431 ? HIS A 420 GLU A 431 1 ? 12 
HELX_P HELX_P21 AC3 VAL B 45  ? ARG B 48  ? VAL B 45  ARG B 48  5 ? 4  
HELX_P HELX_P22 AC4 ASN B 75  ? LYS B 87  ? ASN B 75  LYS B 87  1 ? 13 
HELX_P HELX_P23 AC5 GLU B 89  ? GLY B 97  ? GLU B 89  GLY B 97  1 ? 9  
HELX_P HELX_P24 AC6 GLU B 98  ? TRP B 100 ? GLU B 98  TRP B 100 5 ? 3  
HELX_P HELX_P25 AC7 SER B 103 ? HIS B 119 ? SER B 103 HIS B 119 1 ? 17 
HELX_P HELX_P26 AC8 THR B 123 ? LYS B 127 ? THR B 123 LYS B 127 5 ? 5  
HELX_P HELX_P27 AC9 ALA B 130 ? PHE B 134 ? ALA B 130 PHE B 134 5 ? 5  
HELX_P HELX_P28 AD1 HIS B 137 ? LEU B 141 ? HIS B 137 LEU B 141 5 ? 5  
HELX_P HELX_P29 AD2 ASN B 143 ? SER B 161 ? ASN B 143 SER B 161 1 ? 19 
HELX_P HELX_P30 AD3 ASP B 168 ? GLY B 183 ? ASP B 168 GLY B 183 1 ? 16 
HELX_P HELX_P31 AD4 PHE B 199 ? LEU B 204 ? PHE B 199 LEU B 204 1 ? 6  
HELX_P HELX_P32 AD5 PRO B 246 ? PHE B 259 ? PRO B 246 PHE B 259 1 ? 14 
HELX_P HELX_P33 AD6 CYS B 264 ? LYS B 270 ? CYS B 264 LYS B 270 1 ? 7  
HELX_P HELX_P34 AD7 LYS B 272 ? VAL B 277 ? LYS B 272 VAL B 277 1 ? 6  
HELX_P HELX_P35 AD8 LYS B 287 ? LYS B 309 ? LYS B 287 LYS B 309 1 ? 23 
HELX_P HELX_P36 AD9 SER B 313 ? SER B 329 ? SER B 313 SER B 329 1 ? 17 
HELX_P HELX_P37 AE1 ASN B 336 ? MET B 353 ? ASN B 336 MET B 353 1 ? 18 
HELX_P HELX_P38 AE2 ASP B 355 ? TYR B 374 ? ASP B 355 TYR B 374 1 ? 20 
HELX_P HELX_P39 AE3 SER B 378 ? LEU B 395 ? SER B 378 LEU B 395 1 ? 18 
HELX_P HELX_P40 AE4 HIS B 397 ? GLY B 417 ? HIS B 397 GLY B 417 1 ? 21 
HELX_P HELX_P41 AE5 HIS B 420 ? GLU B 431 ? HIS B 420 GLU B 431 1 ? 12 
# 
_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 CYS 52  SG  ? ? ? 1_555 J ZN . ZN ? ? A CYS 52  A ZN 504 1_555 ? ? ? ? ? ? ? 2.458 ? ? 
metalc2  metalc ? ? A CYS 55  SG  ? ? ? 1_555 J ZN . ZN ? ? A CYS 55  A ZN 504 1_555 ? ? ? ? ? ? ? 2.352 ? ? 
metalc3  metalc ? ? A CYS 65  SG  ? ? ? 1_555 H ZN . ZN ? ? A CYS 65  A ZN 502 1_555 ? ? ? ? ? ? ? 2.428 ? ? 
metalc4  metalc ? ? A CYS 68  SG  ? ? ? 1_555 H ZN . ZN ? ? A CYS 68  A ZN 502 1_555 ? ? ? ? ? ? ? 2.286 ? ? 
metalc5  metalc ? ? A CYS 74  SG  ? ? ? 1_555 J ZN . ZN ? ? A CYS 74  A ZN 504 1_555 ? ? ? ? ? ? ? 2.373 ? ? 
metalc6  metalc ? ? A CYS 78  SG  ? ? ? 1_555 J ZN . ZN ? ? A CYS 78  A ZN 504 1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc7  metalc ? ? A HIS 86  NE2 ? ? ? 1_555 H ZN . ZN ? ? A HIS 86  A ZN 502 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc8  metalc ? ? A CYS 90  SG  ? ? ? 1_555 H ZN . ZN ? ? A CYS 90  A ZN 502 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc9  metalc ? ? A CYS 209 SG  ? ? ? 1_555 I ZN . ZN ? ? A CYS 209 A ZN 503 1_555 ? ? ? ? ? ? ? 2.313 ? ? 
metalc10 metalc ? ? A CYS 262 SG  ? ? ? 1_555 I ZN . ZN ? ? A CYS 262 A ZN 503 1_555 ? ? ? ? ? ? ? 2.338 ? ? 
metalc11 metalc ? ? A CYS 264 SG  ? ? ? 1_555 I ZN . ZN ? ? A CYS 264 A ZN 503 1_555 ? ? ? ? ? ? ? 2.388 ? ? 
metalc12 metalc ? ? A CYS 267 SG  ? ? ? 1_555 I ZN . ZN ? ? A CYS 267 A ZN 503 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc13 metalc ? ? B CYS 52  SG  ? ? ? 1_555 N ZN . ZN ? ? B CYS 52  B ZN 504 1_555 ? ? ? ? ? ? ? 2.427 ? ? 
metalc14 metalc ? ? B CYS 55  SG  ? ? ? 1_555 N ZN . ZN ? ? B CYS 55  B ZN 504 1_555 ? ? ? ? ? ? ? 2.555 ? ? 
metalc15 metalc ? ? B CYS 65  SG  ? ? ? 1_555 L ZN . ZN ? ? B CYS 65  B ZN 502 1_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc16 metalc ? ? B CYS 68  SG  ? ? ? 1_555 L ZN . ZN ? ? B CYS 68  B ZN 502 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc17 metalc ? ? B CYS 74  SG  ? ? ? 1_555 N ZN . ZN ? ? B CYS 74  B ZN 504 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc18 metalc ? ? B CYS 78  SG  ? ? ? 1_555 N ZN . ZN ? ? B CYS 78  B ZN 504 1_555 ? ? ? ? ? ? ? 2.345 ? ? 
metalc19 metalc ? ? B HIS 86  NE2 ? ? ? 1_555 L ZN . ZN ? ? B HIS 86  B ZN 502 1_555 ? ? ? ? ? ? ? 2.292 ? ? 
metalc20 metalc ? ? B CYS 90  SG  ? ? ? 1_555 L ZN . ZN ? ? B CYS 90  B ZN 502 1_555 ? ? ? ? ? ? ? 2.660 ? ? 
metalc21 metalc ? ? B CYS 209 SG  ? ? ? 1_555 M ZN . ZN ? ? B CYS 209 B ZN 503 1_555 ? ? ? ? ? ? ? 2.381 ? ? 
metalc22 metalc ? ? B CYS 262 SG  ? ? ? 1_555 M ZN . ZN ? ? B CYS 262 B ZN 503 1_555 ? ? ? ? ? ? ? 2.339 ? ? 
metalc23 metalc ? ? B CYS 264 SG  ? ? ? 1_555 M ZN . ZN ? ? B CYS 264 B ZN 503 1_555 ? ? ? ? ? ? ? 2.418 ? ? 
metalc24 metalc ? ? B CYS 267 SG  ? ? ? 1_555 M ZN . ZN ? ? B CYS 267 B ZN 503 1_555 ? ? ? ? ? ? ? 2.312 ? ? 
# 
_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  SG  ? A CYS 52  ? A CYS 52  ? 1_555 ZN ? J ZN . ? A ZN 504 ? 1_555 SG  ? A CYS 55  ? A CYS 55  ? 1_555 107.2 ? 
2  SG  ? A CYS 52  ? A CYS 52  ? 1_555 ZN ? J ZN . ? A ZN 504 ? 1_555 SG  ? A CYS 74  ? A CYS 74  ? 1_555 99.8  ? 
3  SG  ? A CYS 55  ? A CYS 55  ? 1_555 ZN ? J ZN . ? A ZN 504 ? 1_555 SG  ? A CYS 74  ? A CYS 74  ? 1_555 100.5 ? 
4  SG  ? A CYS 52  ? A CYS 52  ? 1_555 ZN ? J ZN . ? A ZN 504 ? 1_555 SG  ? A CYS 78  ? A CYS 78  ? 1_555 106.4 ? 
5  SG  ? A CYS 55  ? A CYS 55  ? 1_555 ZN ? J ZN . ? A ZN 504 ? 1_555 SG  ? A CYS 78  ? A CYS 78  ? 1_555 119.7 ? 
6  SG  ? A CYS 74  ? A CYS 74  ? 1_555 ZN ? J ZN . ? A ZN 504 ? 1_555 SG  ? A CYS 78  ? A CYS 78  ? 1_555 120.9 ? 
7  SG  ? A CYS 65  ? A CYS 65  ? 1_555 ZN ? H ZN . ? A ZN 502 ? 1_555 SG  ? A CYS 68  ? A CYS 68  ? 1_555 108.7 ? 
8  SG  ? A CYS 65  ? A CYS 65  ? 1_555 ZN ? H ZN . ? A ZN 502 ? 1_555 NE2 ? A HIS 86  ? A HIS 86  ? 1_555 112.4 ? 
9  SG  ? A CYS 68  ? A CYS 68  ? 1_555 ZN ? H ZN . ? A ZN 502 ? 1_555 NE2 ? A HIS 86  ? A HIS 86  ? 1_555 103.4 ? 
10 SG  ? A CYS 65  ? A CYS 65  ? 1_555 ZN ? H ZN . ? A ZN 502 ? 1_555 SG  ? A CYS 90  ? A CYS 90  ? 1_555 116.5 ? 
11 SG  ? A CYS 68  ? A CYS 68  ? 1_555 ZN ? H ZN . ? A ZN 502 ? 1_555 SG  ? A CYS 90  ? A CYS 90  ? 1_555 109.4 ? 
12 NE2 ? A HIS 86  ? A HIS 86  ? 1_555 ZN ? H ZN . ? A ZN 502 ? 1_555 SG  ? A CYS 90  ? A CYS 90  ? 1_555 105.7 ? 
13 SG  ? A CYS 209 ? A CYS 209 ? 1_555 ZN ? I ZN . ? A ZN 503 ? 1_555 SG  ? A CYS 262 ? A CYS 262 ? 1_555 113.1 ? 
14 SG  ? A CYS 209 ? A CYS 209 ? 1_555 ZN ? I ZN . ? A ZN 503 ? 1_555 SG  ? A CYS 264 ? A CYS 264 ? 1_555 110.1 ? 
15 SG  ? A CYS 262 ? A CYS 262 ? 1_555 ZN ? I ZN . ? A ZN 503 ? 1_555 SG  ? A CYS 264 ? A CYS 264 ? 1_555 106.4 ? 
16 SG  ? A CYS 209 ? A CYS 209 ? 1_555 ZN ? I ZN . ? A ZN 503 ? 1_555 SG  ? A CYS 267 ? A CYS 267 ? 1_555 99.2  ? 
17 SG  ? A CYS 262 ? A CYS 262 ? 1_555 ZN ? I ZN . ? A ZN 503 ? 1_555 SG  ? A CYS 267 ? A CYS 267 ? 1_555 114.1 ? 
18 SG  ? A CYS 264 ? A CYS 264 ? 1_555 ZN ? I ZN . ? A ZN 503 ? 1_555 SG  ? A CYS 267 ? A CYS 267 ? 1_555 113.9 ? 
19 SG  ? B CYS 52  ? B CYS 52  ? 1_555 ZN ? N ZN . ? B ZN 504 ? 1_555 SG  ? B CYS 55  ? B CYS 55  ? 1_555 105.9 ? 
20 SG  ? B CYS 52  ? B CYS 52  ? 1_555 ZN ? N ZN . ? B ZN 504 ? 1_555 SG  ? B CYS 74  ? B CYS 74  ? 1_555 106.2 ? 
21 SG  ? B CYS 55  ? B CYS 55  ? 1_555 ZN ? N ZN . ? B ZN 504 ? 1_555 SG  ? B CYS 74  ? B CYS 74  ? 1_555 94.9  ? 
22 SG  ? B CYS 52  ? B CYS 52  ? 1_555 ZN ? N ZN . ? B ZN 504 ? 1_555 SG  ? B CYS 78  ? B CYS 78  ? 1_555 111.8 ? 
23 SG  ? B CYS 55  ? B CYS 55  ? 1_555 ZN ? N ZN . ? B ZN 504 ? 1_555 SG  ? B CYS 78  ? B CYS 78  ? 1_555 118.4 ? 
24 SG  ? B CYS 74  ? B CYS 74  ? 1_555 ZN ? N ZN . ? B ZN 504 ? 1_555 SG  ? B CYS 78  ? B CYS 78  ? 1_555 117.7 ? 
25 SG  ? B CYS 65  ? B CYS 65  ? 1_555 ZN ? L ZN . ? B ZN 502 ? 1_555 SG  ? B CYS 68  ? B CYS 68  ? 1_555 113.4 ? 
26 SG  ? B CYS 65  ? B CYS 65  ? 1_555 ZN ? L ZN . ? B ZN 502 ? 1_555 NE2 ? B HIS 86  ? B HIS 86  ? 1_555 99.4  ? 
27 SG  ? B CYS 68  ? B CYS 68  ? 1_555 ZN ? L ZN . ? B ZN 502 ? 1_555 NE2 ? B HIS 86  ? B HIS 86  ? 1_555 106.9 ? 
28 SG  ? B CYS 65  ? B CYS 65  ? 1_555 ZN ? L ZN . ? B ZN 502 ? 1_555 SG  ? B CYS 90  ? B CYS 90  ? 1_555 111.0 ? 
29 SG  ? B CYS 68  ? B CYS 68  ? 1_555 ZN ? L ZN . ? B ZN 502 ? 1_555 SG  ? B CYS 90  ? B CYS 90  ? 1_555 126.1 ? 
30 NE2 ? B HIS 86  ? B HIS 86  ? 1_555 ZN ? L ZN . ? B ZN 502 ? 1_555 SG  ? B CYS 90  ? B CYS 90  ? 1_555 94.1  ? 
31 SG  ? B CYS 209 ? B CYS 209 ? 1_555 ZN ? M ZN . ? B ZN 503 ? 1_555 SG  ? B CYS 262 ? B CYS 262 ? 1_555 115.8 ? 
32 SG  ? B CYS 209 ? B CYS 209 ? 1_555 ZN ? M ZN . ? B ZN 503 ? 1_555 SG  ? B CYS 264 ? B CYS 264 ? 1_555 111.9 ? 
33 SG  ? B CYS 262 ? B CYS 262 ? 1_555 ZN ? M ZN . ? B ZN 503 ? 1_555 SG  ? B CYS 264 ? B CYS 264 ? 1_555 101.4 ? 
34 SG  ? B CYS 209 ? B CYS 209 ? 1_555 ZN ? M ZN . ? B ZN 503 ? 1_555 SG  ? B CYS 267 ? B CYS 267 ? 1_555 97.1  ? 
35 SG  ? B CYS 262 ? B CYS 262 ? 1_555 ZN ? M ZN . ? B ZN 503 ? 1_555 SG  ? B CYS 267 ? B CYS 267 ? 1_555 115.8 ? 
36 SG  ? B CYS 264 ? B CYS 264 ? 1_555 ZN ? M ZN . ? B ZN 503 ? 1_555 SG  ? B CYS 267 ? B CYS 267 ? 1_555 115.7 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 3 ? 
AA8 ? 3 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 9   ? SER A 14  ? LEU A 9   SER A 14  
AA1 2 GLY A 18  ? ALA A 23  ? GLY A 18  ALA A 23  
AA2 1 LEU A 32  ? PRO A 37  ? LEU A 32  PRO A 37  
AA2 2 LEU A 221 ? ALA A 226 ? LEU A 221 ALA A 226 
AA2 3 VAL A 213 ? LYS A 218 ? VAL A 213 LYS A 218 
AA3 1 ALA A 40  ? LEU A 43  ? ALA A 40  LEU A 43  
AA3 2 HIS A 193 ? ILE A 198 ? HIS A 193 ILE A 198 
AA3 3 PHE A 184 ? GLU A 187 ? PHE A 184 GLU A 187 
AA4 1 SER A 63  ? LYS A 64  ? SER A 63  LYS A 64  
AA4 2 PHE A 72  ? TYR A 73  ? PHE A 72  TYR A 73  
AA5 1 ASN A 206 ? HIS A 207 ? ASN A 206 HIS A 207 
AA5 2 PHE A 237 ? THR A 238 ? PHE A 237 THR A 238 
AA6 1 LEU B 9   ? SER B 14  ? LEU B 9   SER B 14  
AA6 2 GLY B 18  ? ALA B 23  ? GLY B 18  ALA B 23  
AA7 1 LEU B 32  ? PRO B 37  ? LEU B 32  PRO B 37  
AA7 2 LEU B 221 ? ALA B 226 ? LEU B 221 ALA B 226 
AA7 3 VAL B 213 ? LYS B 218 ? VAL B 213 LYS B 218 
AA8 1 ALA B 40  ? LEU B 43  ? ALA B 40  LEU B 43  
AA8 2 HIS B 193 ? ILE B 198 ? HIS B 193 ILE B 198 
AA8 3 PHE B 184 ? GLU B 187 ? PHE B 184 GLU B 187 
AA9 1 SER B 63  ? LYS B 64  ? SER B 63  LYS B 64  
AA9 2 PHE B 72  ? TYR B 73  ? PHE B 72  TYR B 73  
AB1 1 ASN B 206 ? HIS B 207 ? ASN B 206 HIS B 207 
AB1 2 PHE B 237 ? THR B 238 ? PHE B 237 THR B 238 
# 
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 GLU A 10  ? N GLU A 10  O ARG A 22  ? O ARG A 22  
AA2 1 2 N LEU A 33  ? N LEU A 33  O VAL A 224 ? O VAL A 224 
AA2 2 3 O GLU A 223 ? O GLU A 223 N THR A 216 ? N THR A 216 
AA3 1 2 N ALA A 40  ? N ALA A 40  O ILE A 198 ? O ILE A 198 
AA3 2 3 O LEU A 194 ? O LEU A 194 N ILE A 186 ? N ILE A 186 
AA4 1 2 N SER A 63  ? N SER A 63  O TYR A 73  ? O TYR A 73  
AA5 1 2 N ASN A 206 ? N ASN A 206 O THR A 238 ? O THR A 238 
AA6 1 2 N GLU B 10  ? N GLU B 10  O ARG B 22  ? O ARG B 22  
AA7 1 2 N LEU B 33  ? N LEU B 33  O VAL B 224 ? O VAL B 224 
AA7 2 3 O LEU B 221 ? O LEU B 221 N LYS B 218 ? N LYS B 218 
AA8 1 2 N ALA B 40  ? N ALA B 40  O ILE B 198 ? O ILE B 198 
AA8 2 3 O ALA B 197 ? O ALA B 197 N PHE B 184 ? N PHE B 184 
AA9 1 2 N SER B 63  ? N SER B 63  O TYR B 73  ? O TYR B 73  
AB1 1 2 N ASN B 206 ? N ASN B 206 O THR B 238 ? O THR B 238 
# 
_pdbx_entry_details.entry_id                   9CKC 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 101 ? ? -149.13 51.85   
2  1 HIS A 119 ? ? -119.83 74.68   
3  1 PRO A 167 ? ? -67.70  -178.13 
4  1 VAL A 277 ? ? -112.61 52.34   
5  1 TYR A 377 ? ? -112.37 56.97   
6  1 GLU A 431 ? ? -102.87 44.84   
7  1 SER A 432 ? ? -127.57 -53.65  
8  1 ASN B 101 ? ? -149.16 51.81   
9  1 ASP B 142 ? ? -99.19  44.63   
10 1 ASN B 143 ? ? 61.89   -48.17  
11 1 HIS B 163 ? ? 85.62   -30.46  
12 1 PRO B 167 ? ? -67.39  -177.09 
13 1 VAL B 277 ? ? -111.29 53.71   
14 1 TYR B 377 ? ? -111.58 54.29   
15 1 GLU B 431 ? ? -106.09 51.93   
16 1 SER B 432 ? ? -127.74 -54.82  
# 
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_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         4.65027952193 
_pdbx_refine_tls.origin_y         -11.6364638611 
_pdbx_refine_tls.origin_z         31.917114236 
_pdbx_refine_tls.T[1][1]          0.17311467657 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0321676923398 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0118999345867 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.164345520486 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0133895276072 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.176799568313 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.211141084172 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.155274841532 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.207836579634 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.185131052415 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.22474558159 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.27322751455 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.00886560022923 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0186360025156 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0288223473517 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.00971421518219 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.017102871163 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0259958072511 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.00540884667804 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0226124797701 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -2.26395582269e-05 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1  
2  1 Y 1 A ARG 2   ? A ARG 2  
3  1 Y 1 A ALA 3   ? A ALA 3  
4  1 Y 1 A GLU 4   ? A GLU 4  
5  1 Y 1 B MET 1   ? B MET 1  
6  1 Y 1 B ARG 2   ? B ARG 2  
7  1 Y 1 B ALA 3   ? B ALA 3  
8  1 Y 1 C ARG 522 ? C ARG 1  
9  1 Y 1 C MET 523 ? C MET 2  
10 1 Y 1 C LYS 524 ? C LYS 3  
11 1 Y 1 C LEU 525 ? C LEU 4  
12 1 Y 1 C ALA 532 ? C ALA 11 
13 1 Y 1 C VAL 533 ? C VAL 12 
14 1 Y 1 C ASP 534 ? C ASP 13 
15 1 Y 1 D ARG 522 ? D ARG 1  
16 1 Y 1 D MET 523 ? D MET 2  
17 1 Y 1 D LYS 524 ? D LYS 3  
18 1 Y 1 D LEU 525 ? D LEU 4  
19 1 Y 1 D GLY 530 ? D GLY 9  
20 1 Y 1 D ALA 531 ? D ALA 10 
21 1 Y 1 D ALA 532 ? D ALA 11 
22 1 Y 1 D VAL 533 ? D VAL 12 
23 1 Y 1 D ASP 534 ? D ASP 13 
24 1 Y 1 E THR 526 ? E THR 5  
25 1 Y 1 E LEU 527 ? E LEU 6  
26 1 Y 1 E LYS 528 ? E LYS 7  
27 1 Y 1 E GLY 529 ? E GLY 8  
28 1 Y 1 E GLY 530 ? E GLY 9  
29 1 Y 1 E ALA 531 ? E ALA 10 
30 1 Y 1 E ALA 532 ? E ALA 11 
31 1 Y 1 E VAL 533 ? E VAL 12 
32 1 Y 1 E ASP 534 ? E ASP 13 
33 1 Y 1 F LYS 528 ? F LYS 7  
34 1 Y 1 F GLY 529 ? F GLY 8  
35 1 Y 1 F GLY 530 ? F GLY 9  
36 1 Y 1 F ALA 531 ? F ALA 10 
37 1 Y 1 F ALA 532 ? F ALA 11 
38 1 Y 1 F VAL 533 ? F VAL 12 
39 1 Y 1 F ASP 534 ? F ASP 13 
# 
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 
HIS N      N  N N 137 
HIS CA     C  N S 138 
HIS C      C  N N 139 
HIS O      O  N N 140 
HIS CB     C  N N 141 
HIS CG     C  Y N 142 
HIS ND1    N  Y N 143 
HIS CD2    C  Y N 144 
HIS CE1    C  Y N 145 
HIS NE2    N  Y N 146 
HIS OXT    O  N N 147 
HIS H      H  N N 148 
HIS H2     H  N N 149 
HIS HA     H  N N 150 
HIS HB2    H  N N 151 
HIS HB3    H  N N 152 
HIS HD1    H  N N 153 
HIS HD2    H  N N 154 
HIS HE1    H  N N 155 
HIS HE2    H  N N 156 
HIS HXT    H  N N 157 
HOH O      O  N N 158 
HOH H1     H  N N 159 
HOH H2     H  N N 160 
ILE N      N  N N 161 
ILE CA     C  N S 162 
ILE C      C  N N 163 
ILE O      O  N N 164 
ILE CB     C  N S 165 
ILE CG1    C  N N 166 
ILE CG2    C  N N 167 
ILE CD1    C  N N 168 
ILE OXT    O  N N 169 
ILE H      H  N N 170 
ILE H2     H  N N 171 
ILE HA     H  N N 172 
ILE HB     H  N N 173 
ILE HG12   H  N N 174 
ILE HG13   H  N N 175 
ILE HG21   H  N N 176 
ILE HG22   H  N N 177 
ILE HG23   H  N N 178 
ILE HD11   H  N N 179 
ILE HD12   H  N N 180 
ILE HD13   H  N N 181 
ILE HXT    H  N N 182 
LEU N      N  N N 183 
LEU CA     C  N S 184 
LEU C      C  N N 185 
LEU O      O  N N 186 
LEU CB     C  N N 187 
LEU CG     C  N N 188 
LEU CD1    C  N N 189 
LEU CD2    C  N N 190 
LEU OXT    O  N N 191 
LEU H      H  N N 192 
LEU H2     H  N N 193 
LEU HA     H  N N 194 
LEU HB2    H  N N 195 
LEU HB3    H  N N 196 
LEU HG     H  N N 197 
LEU HD11   H  N N 198 
LEU HD12   H  N N 199 
LEU HD13   H  N N 200 
LEU HD21   H  N N 201 
LEU HD22   H  N N 202 
LEU HD23   H  N N 203 
LEU HXT    H  N N 204 
LYS N      N  N N 205 
LYS CA     C  N S 206 
LYS C      C  N N 207 
LYS O      O  N N 208 
LYS CB     C  N N 209 
LYS CG     C  N N 210 
LYS CD     C  N N 211 
LYS CE     C  N N 212 
LYS NZ     N  N N 213 
LYS OXT    O  N N 214 
LYS H      H  N N 215 
LYS H2     H  N N 216 
LYS HA     H  N N 217 
LYS HB2    H  N N 218 
LYS HB3    H  N N 219 
LYS HG2    H  N N 220 
LYS HG3    H  N N 221 
LYS HD2    H  N N 222 
LYS HD3    H  N N 223 
LYS HE2    H  N N 224 
LYS HE3    H  N N 225 
LYS HZ1    H  N N 226 
LYS HZ2    H  N N 227 
LYS HZ3    H  N N 228 
LYS HXT    H  N N 229 
MET N      N  N N 230 
MET CA     C  N S 231 
MET C      C  N N 232 
MET O      O  N N 233 
MET CB     C  N N 234 
MET CG     C  N N 235 
MET SD     S  N N 236 
MET CE     C  N N 237 
MET OXT    O  N N 238 
MET H      H  N N 239 
MET H2     H  N N 240 
MET HA     H  N N 241 
MET HB2    H  N N 242 
MET HB3    H  N N 243 
MET HG2    H  N N 244 
MET HG3    H  N N 245 
MET HE1    H  N N 246 
MET HE2    H  N N 247 
MET HE3    H  N N 248 
MET HXT    H  N N 249 
PHE N      N  N N 250 
PHE CA     C  N S 251 
PHE C      C  N N 252 
PHE O      O  N N 253 
PHE CB     C  N N 254 
PHE CG     C  Y N 255 
PHE CD1    C  Y N 256 
PHE CD2    C  Y N 257 
PHE CE1    C  Y N 258 
PHE CE2    C  Y N 259 
PHE CZ     C  Y N 260 
PHE OXT    O  N N 261 
PHE H      H  N N 262 
PHE H2     H  N N 263 
PHE HA     H  N N 264 
PHE HB2    H  N N 265 
PHE HB3    H  N N 266 
PHE HD1    H  N N 267 
PHE HD2    H  N N 268 
PHE HE1    H  N N 269 
PHE HE2    H  N N 270 
PHE HZ     H  N N 271 
PHE HXT    H  N N 272 
PRO N      N  N N 273 
PRO CA     C  N S 274 
PRO C      C  N N 275 
PRO O      O  N N 276 
PRO CB     C  N N 277 
PRO CG     C  N N 278 
PRO CD     C  N N 279 
PRO OXT    O  N N 280 
PRO H      H  N N 281 
PRO HA     H  N N 282 
PRO HB2    H  N N 283 
PRO HB3    H  N N 284 
PRO HG2    H  N N 285 
PRO HG3    H  N N 286 
PRO HD2    H  N N 287 
PRO HD3    H  N N 288 
PRO HXT    H  N N 289 
SAH N      N  N N 290 
SAH CA     C  N S 291 
SAH CB     C  N N 292 
SAH CG     C  N N 293 
SAH SD     S  N N 294 
SAH C      C  N N 295 
SAH O      O  N N 296 
SAH OXT    O  N N 297 
SAH "C5'"  C  N N 298 
SAH "C4'"  C  N S 299 
SAH "O4'"  O  N N 300 
SAH "C3'"  C  N S 301 
SAH "O3'"  O  N N 302 
SAH "C2'"  C  N R 303 
SAH "O2'"  O  N N 304 
SAH "C1'"  C  N R 305 
SAH N9     N  Y N 306 
SAH C8     C  Y N 307 
SAH N7     N  Y N 308 
SAH C5     C  Y N 309 
SAH C6     C  Y N 310 
SAH N6     N  N N 311 
SAH N1     N  Y N 312 
SAH C2     C  Y N 313 
SAH N3     N  Y N 314 
SAH C4     C  Y N 315 
SAH HN1    H  N N 316 
SAH HN2    H  N N 317 
SAH HA     H  N N 318 
SAH HB1    H  N N 319 
SAH HB2    H  N N 320 
SAH HG1    H  N N 321 
SAH HG2    H  N N 322 
SAH HXT    H  N N 323 
SAH "H5'1" H  N N 324 
SAH "H5'2" H  N N 325 
SAH "H4'"  H  N N 326 
SAH "H3'"  H  N N 327 
SAH "HO3'" H  N N 328 
SAH "H2'"  H  N N 329 
SAH "HO2'" H  N N 330 
SAH "H1'"  H  N N 331 
SAH H8     H  N N 332 
SAH HN61   H  N N 333 
SAH HN62   H  N N 334 
SAH H2     H  N N 335 
SER N      N  N N 336 
SER CA     C  N S 337 
SER C      C  N N 338 
SER O      O  N N 339 
SER CB     C  N N 340 
SER OG     O  N N 341 
SER OXT    O  N N 342 
SER H      H  N N 343 
SER H2     H  N N 344 
SER HA     H  N N 345 
SER HB2    H  N N 346 
SER HB3    H  N N 347 
SER HG     H  N N 348 
SER HXT    H  N N 349 
THR N      N  N N 350 
THR CA     C  N S 351 
THR C      C  N N 352 
THR O      O  N N 353 
THR CB     C  N R 354 
THR OG1    O  N N 355 
THR CG2    C  N N 356 
THR OXT    O  N N 357 
THR H      H  N N 358 
THR H2     H  N N 359 
THR HA     H  N N 360 
THR HB     H  N N 361 
THR HG1    H  N N 362 
THR HG21   H  N N 363 
THR HG22   H  N N 364 
THR HG23   H  N N 365 
THR HXT    H  N N 366 
TRP N      N  N N 367 
TRP CA     C  N S 368 
TRP C      C  N N 369 
TRP O      O  N N 370 
TRP CB     C  N N 371 
TRP CG     C  Y N 372 
TRP CD1    C  Y N 373 
TRP CD2    C  Y N 374 
TRP NE1    N  Y N 375 
TRP CE2    C  Y N 376 
TRP CE3    C  Y N 377 
TRP CZ2    C  Y N 378 
TRP CZ3    C  Y N 379 
TRP CH2    C  Y N 380 
TRP OXT    O  N N 381 
TRP H      H  N N 382 
TRP H2     H  N N 383 
TRP HA     H  N N 384 
TRP HB2    H  N N 385 
TRP HB3    H  N N 386 
TRP HD1    H  N N 387 
TRP HE1    H  N N 388 
TRP HE3    H  N N 389 
TRP HZ2    H  N N 390 
TRP HZ3    H  N N 391 
TRP HH2    H  N N 392 
TRP HXT    H  N N 393 
TYR N      N  N N 394 
TYR CA     C  N S 395 
TYR C      C  N N 396 
TYR O      O  N N 397 
TYR CB     C  N N 398 
TYR CG     C  Y N 399 
TYR CD1    C  Y N 400 
TYR CD2    C  Y N 401 
TYR CE1    C  Y N 402 
TYR CE2    C  Y N 403 
TYR CZ     C  Y N 404 
TYR OH     O  N N 405 
TYR OXT    O  N N 406 
TYR H      H  N N 407 
TYR H2     H  N N 408 
TYR HA     H  N N 409 
TYR HB2    H  N N 410 
TYR HB3    H  N N 411 
TYR HD1    H  N N 412 
TYR HD2    H  N N 413 
TYR HE1    H  N N 414 
TYR HE2    H  N N 415 
TYR HH     H  N N 416 
TYR HXT    H  N N 417 
VAL N      N  N N 418 
VAL CA     C  N S 419 
VAL C      C  N N 420 
VAL O      O  N N 421 
VAL CB     C  N N 422 
VAL CG1    C  N N 423 
VAL CG2    C  N N 424 
VAL OXT    O  N N 425 
VAL H      H  N N 426 
VAL H2     H  N N 427 
VAL HA     H  N N 428 
VAL HB     H  N N 429 
VAL HG11   H  N N 430 
VAL HG12   H  N N 431 
VAL HG13   H  N N 432 
VAL HG21   H  N N 433 
VAL HG22   H  N N 434 
VAL HG23   H  N N 435 
VAL HXT    H  N N 436 
ZN  ZN     ZN N N 437 
# 
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 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
LEU N     CA     sing N N 173 
LEU N     H      sing N N 174 
LEU N     H2     sing N N 175 
LEU CA    C      sing N N 176 
LEU CA    CB     sing N N 177 
LEU CA    HA     sing N N 178 
LEU C     O      doub N N 179 
LEU C     OXT    sing N N 180 
LEU CB    CG     sing N N 181 
LEU CB    HB2    sing N N 182 
LEU CB    HB3    sing N N 183 
LEU CG    CD1    sing N N 184 
LEU CG    CD2    sing N N 185 
LEU CG    HG     sing N N 186 
LEU CD1   HD11   sing N N 187 
LEU CD1   HD12   sing N N 188 
LEU CD1   HD13   sing N N 189 
LEU CD2   HD21   sing N N 190 
LEU CD2   HD22   sing N N 191 
LEU CD2   HD23   sing N N 192 
LEU OXT   HXT    sing N N 193 
LYS N     CA     sing N N 194 
LYS N     H      sing N N 195 
LYS N     H2     sing N N 196 
LYS CA    C      sing N N 197 
LYS CA    CB     sing N N 198 
LYS CA    HA     sing N N 199 
LYS C     O      doub N N 200 
LYS C     OXT    sing N N 201 
LYS CB    CG     sing N N 202 
LYS CB    HB2    sing N N 203 
LYS CB    HB3    sing N N 204 
LYS CG    CD     sing N N 205 
LYS CG    HG2    sing N N 206 
LYS CG    HG3    sing N N 207 
LYS CD    CE     sing N N 208 
LYS CD    HD2    sing N N 209 
LYS CD    HD3    sing N N 210 
LYS CE    NZ     sing N N 211 
LYS CE    HE2    sing N N 212 
LYS CE    HE3    sing N N 213 
LYS NZ    HZ1    sing N N 214 
LYS NZ    HZ2    sing N N 215 
LYS NZ    HZ3    sing N N 216 
LYS OXT   HXT    sing N N 217 
MET N     CA     sing N N 218 
MET N     H      sing N N 219 
MET N     H2     sing N N 220 
MET CA    C      sing N N 221 
MET CA    CB     sing N N 222 
MET CA    HA     sing N N 223 
MET C     O      doub N N 224 
MET C     OXT    sing N N 225 
MET CB    CG     sing N N 226 
MET CB    HB2    sing N N 227 
MET CB    HB3    sing N N 228 
MET CG    SD     sing N N 229 
MET CG    HG2    sing N N 230 
MET CG    HG3    sing N N 231 
MET SD    CE     sing N N 232 
MET CE    HE1    sing N N 233 
MET CE    HE2    sing N N 234 
MET CE    HE3    sing N N 235 
MET OXT   HXT    sing N N 236 
PHE N     CA     sing N N 237 
PHE N     H      sing N N 238 
PHE N     H2     sing N N 239 
PHE CA    C      sing N N 240 
PHE CA    CB     sing N N 241 
PHE CA    HA     sing N N 242 
PHE C     O      doub N N 243 
PHE C     OXT    sing N N 244 
PHE CB    CG     sing N N 245 
PHE CB    HB2    sing N N 246 
PHE CB    HB3    sing N N 247 
PHE CG    CD1    doub Y N 248 
PHE CG    CD2    sing Y N 249 
PHE CD1   CE1    sing Y N 250 
PHE CD1   HD1    sing N N 251 
PHE CD2   CE2    doub Y N 252 
PHE CD2   HD2    sing N N 253 
PHE CE1   CZ     doub Y N 254 
PHE CE1   HE1    sing N N 255 
PHE CE2   CZ     sing Y N 256 
PHE CE2   HE2    sing N N 257 
PHE CZ    HZ     sing N N 258 
PHE OXT   HXT    sing N N 259 
PRO N     CA     sing N N 260 
PRO N     CD     sing N N 261 
PRO N     H      sing N N 262 
PRO CA    C      sing N N 263 
PRO CA    CB     sing N N 264 
PRO CA    HA     sing N N 265 
PRO C     O      doub N N 266 
PRO C     OXT    sing N N 267 
PRO CB    CG     sing N N 268 
PRO CB    HB2    sing N N 269 
PRO CB    HB3    sing N N 270 
PRO CG    CD     sing N N 271 
PRO CG    HG2    sing N N 272 
PRO CG    HG3    sing N N 273 
PRO CD    HD2    sing N N 274 
PRO CD    HD3    sing N N 275 
PRO OXT   HXT    sing N N 276 
SAH N     CA     sing N N 277 
SAH N     HN1    sing N N 278 
SAH N     HN2    sing N N 279 
SAH CA    CB     sing N N 280 
SAH CA    C      sing N N 281 
SAH CA    HA     sing N N 282 
SAH CB    CG     sing N N 283 
SAH CB    HB1    sing N N 284 
SAH CB    HB2    sing N N 285 
SAH CG    SD     sing N N 286 
SAH CG    HG1    sing N N 287 
SAH CG    HG2    sing N N 288 
SAH SD    "C5'"  sing N N 289 
SAH C     O      doub N N 290 
SAH C     OXT    sing N N 291 
SAH OXT   HXT    sing N N 292 
SAH "C5'" "C4'"  sing N N 293 
SAH "C5'" "H5'1" sing N N 294 
SAH "C5'" "H5'2" sing N N 295 
SAH "C4'" "O4'"  sing N N 296 
SAH "C4'" "C3'"  sing N N 297 
SAH "C4'" "H4'"  sing N N 298 
SAH "O4'" "C1'"  sing N N 299 
SAH "C3'" "O3'"  sing N N 300 
SAH "C3'" "C2'"  sing N N 301 
SAH "C3'" "H3'"  sing N N 302 
SAH "O3'" "HO3'" sing N N 303 
SAH "C2'" "O2'"  sing N N 304 
SAH "C2'" "C1'"  sing N N 305 
SAH "C2'" "H2'"  sing N N 306 
SAH "O2'" "HO2'" sing N N 307 
SAH "C1'" N9     sing N N 308 
SAH "C1'" "H1'"  sing N N 309 
SAH N9    C8     sing Y N 310 
SAH N9    C4     sing Y N 311 
SAH C8    N7     doub Y N 312 
SAH C8    H8     sing N N 313 
SAH N7    C5     sing Y N 314 
SAH C5    C6     sing Y N 315 
SAH C5    C4     doub Y N 316 
SAH C6    N6     sing N N 317 
SAH C6    N1     doub Y N 318 
SAH N6    HN61   sing N N 319 
SAH N6    HN62   sing N N 320 
SAH N1    C2     sing Y N 321 
SAH C2    N3     doub Y N 322 
SAH C2    H2     sing N N 323 
SAH N3    C4     sing Y N 324 
SER N     CA     sing N N 325 
SER N     H      sing N N 326 
SER N     H2     sing N N 327 
SER CA    C      sing N N 328 
SER CA    CB     sing N N 329 
SER CA    HA     sing N N 330 
SER C     O      doub N N 331 
SER C     OXT    sing N N 332 
SER CB    OG     sing N N 333 
SER CB    HB2    sing N N 334 
SER CB    HB3    sing N N 335 
SER OG    HG     sing N N 336 
SER OXT   HXT    sing N N 337 
THR N     CA     sing N N 338 
THR N     H      sing N N 339 
THR N     H2     sing N N 340 
THR CA    C      sing N N 341 
THR CA    CB     sing N N 342 
THR CA    HA     sing N N 343 
THR C     O      doub N N 344 
THR C     OXT    sing N N 345 
THR CB    OG1    sing N N 346 
THR CB    CG2    sing N N 347 
THR CB    HB     sing N N 348 
THR OG1   HG1    sing N N 349 
THR CG2   HG21   sing N N 350 
THR CG2   HG22   sing N N 351 
THR CG2   HG23   sing N N 352 
THR OXT   HXT    sing N N 353 
TRP N     CA     sing N N 354 
TRP N     H      sing N N 355 
TRP N     H2     sing N N 356 
TRP CA    C      sing N N 357 
TRP CA    CB     sing N N 358 
TRP CA    HA     sing N N 359 
TRP C     O      doub N N 360 
TRP C     OXT    sing N N 361 
TRP CB    CG     sing N N 362 
TRP CB    HB2    sing N N 363 
TRP CB    HB3    sing N N 364 
TRP CG    CD1    doub Y N 365 
TRP CG    CD2    sing Y N 366 
TRP CD1   NE1    sing Y N 367 
TRP CD1   HD1    sing N N 368 
TRP CD2   CE2    doub Y N 369 
TRP CD2   CE3    sing Y N 370 
TRP NE1   CE2    sing Y N 371 
TRP NE1   HE1    sing N N 372 
TRP CE2   CZ2    sing Y N 373 
TRP CE3   CZ3    doub Y N 374 
TRP CE3   HE3    sing N N 375 
TRP CZ2   CH2    doub Y N 376 
TRP CZ2   HZ2    sing N N 377 
TRP CZ3   CH2    sing Y N 378 
TRP CZ3   HZ3    sing N N 379 
TRP CH2   HH2    sing N N 380 
TRP OXT   HXT    sing N N 381 
TYR N     CA     sing N N 382 
TYR N     H      sing N N 383 
TYR N     H2     sing N N 384 
TYR CA    C      sing N N 385 
TYR CA    CB     sing N N 386 
TYR CA    HA     sing N N 387 
TYR C     O      doub N N 388 
TYR C     OXT    sing N N 389 
TYR CB    CG     sing N N 390 
TYR CB    HB2    sing N N 391 
TYR CB    HB3    sing N N 392 
TYR CG    CD1    doub Y N 393 
TYR CG    CD2    sing Y N 394 
TYR CD1   CE1    sing Y N 395 
TYR CD1   HD1    sing N N 396 
TYR CD2   CE2    doub Y N 397 
TYR CD2   HD2    sing N N 398 
TYR CE1   CZ     doub Y N 399 
TYR CE1   HE1    sing N N 400 
TYR CE2   CZ     sing Y N 401 
TYR CE2   HE2    sing N N 402 
TYR CZ    OH     sing N N 403 
TYR OH    HH     sing N N 404 
TYR OXT   HXT    sing N N 405 
VAL N     CA     sing N N 406 
VAL N     H      sing N N 407 
VAL N     H2     sing N N 408 
VAL CA    C      sing N N 409 
VAL CA    CB     sing N N 410 
VAL CA    HA     sing N N 411 
VAL C     O      doub N N 412 
VAL C     OXT    sing N N 413 
VAL CB    CG1    sing N N 414 
VAL CB    CG2    sing N N 415 
VAL CB    HB     sing N N 416 
VAL CG1   HG11   sing N N 417 
VAL CG1   HG12   sing N N 418 
VAL CG1   HG13   sing N N 419 
VAL CG2   HG21   sing N N 420 
VAL CG2   HG22   sing N N 421 
VAL CG2   HG23   sing N N 422 
VAL OXT   HXT    sing N N 423 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)' 
_pdbx_audit_support.country                'United States' 
_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             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4WUY 
_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                    9CKC 
_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]   0.007003 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003008 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.019163 
_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]   0.007510 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C    ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
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.
;
? 
ZN   ? ? ?        ?       ? ? ?        ?        ? ? ?   ? ? 
ZN2+ ? ? 27.87530 ?       ? ? 3.31736  ?        ? ? 0.0 
;1-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     . GLY A 1 5   ? 14.87200  0.47600   28.55900  1.000 59.92034  ? 5   GLY A N     1 
ATOM   2    C  CA    . GLY A 1 5   ? 15.08300  -0.48800  27.49300  1.000 45.08962  ? 5   GLY A CA    1 
ATOM   3    C  C     . GLY A 1 5   ? 16.51200  -1.00100  27.37500  1.000 46.18975  ? 5   GLY A C     1 
ATOM   4    O  O     . GLY A 1 5   ? 17.13400  -1.38900  28.36800  1.000 87.28152  ? 5   GLY A O     1 
ATOM   5    N  N     . LEU A 1 6   ? 17.02100  -1.01200  26.14200  1.000 71.07168  ? 6   LEU A N     1 
ATOM   6    C  CA    . LEU A 1 6   ? 18.35800  -1.50000  25.80800  1.000 52.70632  ? 6   LEU A CA    1 
ATOM   7    C  C     . LEU A 1 6   ? 19.22100  -0.32700  25.36400  1.000 42.49720  ? 6   LEU A C     1 
ATOM   8    O  O     . LEU A 1 6   ? 18.89300  0.34900   24.38500  1.000 41.29969  ? 6   LEU A O     1 
ATOM   9    C  CB    . LEU A 1 6   ? 18.28400  -2.55800  24.70600  1.000 54.39863  ? 6   LEU A CB    1 
ATOM   10   C  CG    . LEU A 1 6   ? 17.49000  -3.81600  25.05700  1.000 47.20303  ? 6   LEU A CG    1 
ATOM   11   C  CD1   . LEU A 1 6   ? 17.21800  -4.63800  23.81900  1.000 59.95456  ? 6   LEU A CD1   1 
ATOM   12   C  CD2   . LEU A 1 6   ? 18.25900  -4.64000  26.07900  1.000 64.17875  ? 6   LEU A CD2   1 
ATOM   13   N  N     . GLY A 1 7   ? 20.31500  -0.08500  26.08400  1.000 46.59769  ? 7   GLY A N     1 
ATOM   14   C  CA    . GLY A 1 7   ? 21.15500  1.06100   25.77600  1.000 42.45509  ? 7   GLY A CA    1 
ATOM   15   C  C     . GLY A 1 7   ? 21.73200  0.99100   24.37200  1.000 47.08196  ? 7   GLY A C     1 
ATOM   16   O  O     . GLY A 1 7   ? 22.13600  -0.07300  23.89400  1.000 40.53118  ? 7   GLY A O     1 
ATOM   17   N  N     . GLY A 1 8   ? 21.77600  2.14700   23.70900  1.000 35.68059  ? 8   GLY A N     1 
ATOM   18   C  CA    . GLY A 1 8   ? 22.30900  2.24600   22.36400  1.000 39.83636  ? 8   GLY A CA    1 
ATOM   19   C  C     . GLY A 1 8   ? 21.37400  1.78500   21.27100  1.000 31.53273  ? 8   GLY A C     1 
ATOM   20   O  O     . GLY A 1 8   ? 21.78700  1.72700   20.10700  1.000 32.75393  ? 8   GLY A O     1 
ATOM   21   N  N     . LEU A 1 9   ? 20.12900  1.46300   21.60800  1.000 29.32194  ? 9   LEU A N     1 
ATOM   22   C  CA    . LEU A 1 9   ? 19.16900  0.89600   20.67300  1.000 33.91722  ? 9   LEU A CA    1 
ATOM   23   C  C     . LEU A 1 9   ? 17.80700  1.50400   20.96800  1.000 33.74089  ? 9   LEU A C     1 
ATOM   24   O  O     . LEU A 1 9   ? 17.56800  2.02200   22.06100  1.000 30.06413  ? 9   LEU A O     1 
ATOM   25   C  CB    . LEU A 1 9   ? 19.10500  -0.63300  20.78700  1.000 33.91722  ? 9   LEU A CB    1 
ATOM   26   C  CG    . LEU A 1 9   ? 20.42200  -1.39400  20.60100  1.000 38.39671  ? 9   LEU A CG    1 
ATOM   27   C  CD1   . LEU A 1 9   ? 20.29800  -2.80500  21.14300  1.000 38.46514  ? 9   LEU A CD1   1 
ATOM   28   C  CD2   . LEU A 1 9   ? 20.85800  -1.40700  19.13200  1.000 35.20159  ? 9   LEU A CD2   1 
ATOM   29   N  N     . GLU A 1 10  ? 16.92100  1.47300   19.97400  1.000 32.98553  ? 10  GLU A N     1 
ATOM   30   C  CA    . GLU A 1 10  ? 15.55800  1.93100   20.20000  1.000 34.97261  ? 10  GLU A CA    1 
ATOM   31   C  C     . GLU A 1 10  ? 14.59900  1.19600   19.27400  1.000 31.63274  ? 10  GLU A C     1 
ATOM   32   O  O     . GLU A 1 10  ? 14.94100  0.85500   18.13800  1.000 30.02728  ? 10  GLU A O     1 
ATOM   33   C  CB    . GLU A 1 10  ? 15.42200  3.45500   20.01900  1.000 34.56730  ? 10  GLU A CB    1 
ATOM   34   C  CG    . GLU A 1 10  ? 15.46100  3.94700   18.57800  1.000 45.01066  ? 10  GLU A CG    1 
ATOM   35   C  CD    . GLU A 1 10  ? 15.21800  5.44900   18.45700  1.000 64.22875  ? 10  GLU A CD    1 
ATOM   36   O  OE1   . GLU A 1 10  ? 14.82000  6.08200   19.46200  1.000 49.63753  ? 10  GLU A OE1   1 
ATOM   37   O  OE2   . GLU A 1 10  ? 15.42600  5.99600   17.35100  1.000 57.32003  ? 10  GLU A OE2   1 
ATOM   38   N  N     . ARG A 1 11  ? 13.40200  0.93700   19.79500  1.000 32.84604  ? 11  ARG A N     1 
ATOM   39   C  CA    . ARG A 1 11  ? 12.28200  0.47600   18.98600  1.000 30.30890  ? 11  ARG A CA    1 
ATOM   40   C  C     . ARG A 1 11  ? 11.71600  1.63800   18.18000  1.000 30.37469  ? 11  ARG A C     1 
ATOM   41   O  O     . ARG A 1 11  ? 11.65200  2.76900   18.66600  1.000 36.57281  ? 11  ARG A O     1 
ATOM   42   C  CB    . ARG A 1 11  ? 11.20700  -0.11900  19.89400  1.000 29.97991  ? 11  ARG A CB    1 
ATOM   43   C  CG    . ARG A 1 11  ? 9.88600   -0.45400  19.22900  1.000 33.51981  ? 11  ARG A CG    1 
ATOM   44   C  CD    . ARG A 1 11  ? 9.02800   -1.26500  20.18700  1.000 43.17360  ? 11  ARG A CD    1 
ATOM   45   N  NE    . ARG A 1 11  ? 7.60200   -1.05200  19.98500  1.000 52.58262  ? 11  ARG A NE    1 
ATOM   46   C  CZ    . ARG A 1 11  ? 6.65400   -1.64000  20.71000  1.000 49.77965  ? 11  ARG A CZ    1 
ATOM   47   N  NH1   . ARG A 1 11  ? 6.98600   -2.47600  21.68600  1.000 44.57113  ? 11  ARG A NH1   1 
ATOM   48   N  NH2   . ARG A 1 11  ? 5.37300   -1.39200  20.46000  1.000 59.68874  ? 11  ARG A NH2   1 
ATOM   49   N  N     . PHE A 1 12  ? 11.32800  1.36900   16.93300  1.000 27.09272  ? 12  PHE A N     1 
ATOM   50   C  CA    . PHE A 1 12  ? 10.80300  2.42500   16.07400  1.000 26.63214  ? 12  PHE A CA    1 
ATOM   51   C  C     . PHE A 1 12  ? 9.85900   1.81800   15.04600  1.000 27.71385  ? 12  PHE A C     1 
ATOM   52   O  O     . PHE A 1 12  ? 9.69600   0.59800   14.96200  1.000 27.21116  ? 12  PHE A O     1 
ATOM   53   C  CB    . PHE A 1 12  ? 11.93600  3.21500   15.39700  1.000 30.52998  ? 12  PHE A CB    1 
ATOM   54   C  CG    . PHE A 1 12  ? 12.51000  2.54800   14.17200  1.000 27.03482  ? 12  PHE A CG    1 
ATOM   55   C  CD1   . PHE A 1 12  ? 13.18300  1.34100   14.27000  1.000 25.36357  ? 12  PHE A CD1   1 
ATOM   56   C  CD2   . PHE A 1 12  ? 12.41000  3.15600   12.92700  1.000 28.48763  ? 12  PHE A CD2   1 
ATOM   57   C  CE1   . PHE A 1 12  ? 13.71900  0.73300   13.14400  1.000 27.77175  ? 12  PHE A CE1   1 
ATOM   58   C  CE2   . PHE A 1 12  ? 12.94800  2.55600   11.79600  1.000 26.79269  ? 12  PHE A CE2   1 
ATOM   59   C  CZ    . PHE A 1 12  ? 13.60000  1.34300   11.90500  1.000 27.57173  ? 12  PHE A CZ    1 
ATOM   60   N  N     . CYS A 1 13  ? 9.20200   2.69300   14.28800  1.000 33.96723  ? 13  CYS A N     1 
ATOM   61   C  CA    . CYS A 1 13  ? 8.29700   2.28300   13.21800  1.000 34.59362  ? 13  CYS A CA    1 
ATOM   62   C  C     . CYS A 1 13  ? 9.06900   2.24100   11.90300  1.000 30.78527  ? 13  CYS A C     1 
ATOM   63   O  O     . CYS A 1 13  ? 9.39100   3.28700   11.33000  1.000 37.70189  ? 13  CYS A O     1 
ATOM   64   C  CB    . CYS A 1 13  ? 7.10200   3.22700   13.13300  1.000 37.53871  ? 13  CYS A CB    1 
ATOM   65   S  SG    . CYS A 1 13  ? 5.96900   3.06400   14.53700  1.000 48.18472  ? 13  CYS A SG    1 
ATOM   66   N  N     . SER A 1 14  ? 9.37000   1.03200   11.42900  1.000 32.78025  ? 14  SER A N     1 
ATOM   67   C  CA    . SER A 1 14  ? 10.07900  0.85800   10.16800  1.000 36.49122  ? 14  SER A CA    1 
ATOM   68   C  C     . SER A 1 14  ? 9.07000   0.83500   9.02700   1.000 37.42028  ? 14  SER A C     1 
ATOM   69   O  O     . SER A 1 14  ? 8.25000   -0.08700  8.96400   1.000 27.64279  ? 14  SER A O     1 
ATOM   70   C  CB    . SER A 1 14  ? 10.88300  -0.43200  10.18800  1.000 28.86925  ? 14  SER A CB    1 
ATOM   71   O  OG    . SER A 1 14  ? 11.59700  -0.61800  8.97600   1.000 33.25136  ? 14  SER A OG    1 
ATOM   72   N  N     . PRO A 1 15  ? 9.09600   1.80800   8.11300   1.000 33.61456  ? 15  PRO A N     1 
ATOM   73   C  CA    . PRO A 1 15  ? 8.06800   1.87200   7.05800   1.000 35.45688  ? 15  PRO A CA    1 
ATOM   74   C  C     . PRO A 1 15  ? 7.97500   0.57700   6.26300   1.000 33.47507  ? 15  PRO A C     1 
ATOM   75   O  O     . PRO A 1 15  ? 8.97000   0.07400   5.73900   1.000 36.35436  ? 15  PRO A O     1 
ATOM   76   C  CB    . PRO A 1 15  ? 8.53700   3.03900   6.17800   1.000 37.85717  ? 15  PRO A CB    1 
ATOM   77   C  CG    . PRO A 1 15  ? 9.38600   3.87400   7.07100   1.000 44.94749  ? 15  PRO A CG    1 
ATOM   78   C  CD    . PRO A 1 15  ? 10.05300  2.92200   8.03200   1.000 37.56503  ? 15  PRO A CD    1 
ATOM   79   N  N     . GLY A 1 16  ? 6.76300   0.02900   6.18800   1.000 31.42482  ? 16  GLY A N     1 
ATOM   80   C  CA    . GLY A 1 16  ? 6.53500   -1.20500  5.46900   1.000 37.60188  ? 16  GLY A CA    1 
ATOM   81   C  C     . GLY A 1 16  ? 6.91900   -2.47200  6.20300   1.000 35.48847  ? 16  GLY A C     1 
ATOM   82   O  O     . GLY A 1 16  ? 6.66400   -3.56400  5.68400   1.000 33.38821  ? 16  GLY A O     1 
ATOM   83   N  N     . LYS A 1 17  ? 7.51400   -2.37100  7.39400   1.000 28.01389  ? 17  LYS A N     1 
ATOM   84   C  CA    . LYS A 1 17  ? 7.99000   -3.53500  8.13300   1.000 25.37936  ? 17  LYS A CA    1 
ATOM   85   C  C     . LYS A 1 17  ? 7.39700   -3.62100  9.53500   1.000 26.75321  ? 17  LYS A C     1 
ATOM   86   O  O     . LYS A 1 17  ? 7.82200   -4.47400  10.32500  1.000 37.52555  ? 17  LYS A O     1 
ATOM   87   C  CB    . LYS A 1 17  ? 9.52300   -3.53400  8.21800   1.000 24.48978  ? 17  LYS A CB    1 
ATOM   88   C  CG    . LYS A 1 17  ? 10.24200  -3.45900  6.87400   1.000 27.74806  ? 17  LYS A CG    1 
ATOM   89   C  CD    . LYS A 1 17  ? 11.75500  -3.61800  7.03200   1.000 31.87751  ? 17  LYS A CD    1 
ATOM   90   C  CE    . LYS A 1 17  ? 12.48400  -3.58500  5.68100   1.000 28.35603  ? 17  LYS A CE    1 
ATOM   91   N  NZ    . LYS A 1 17  ? 12.30600  -2.32200  4.91100   1.000 33.00659  ? 17  LYS A NZ    1 
ATOM   92   N  N     . GLY A 1 18  ? 6.42500   -2.77500  9.86100   1.000 29.02190  ? 18  GLY A N     1 
ATOM   93   C  CA    . GLY A 1 18  ? 5.90300   -2.75700  11.21600  1.000 32.36704  ? 18  GLY A CA    1 
ATOM   94   C  C     . GLY A 1 18  ? 6.90300   -2.11400  12.15400  1.000 30.88002  ? 18  GLY A C     1 
ATOM   95   O  O     . GLY A 1 18  ? 7.46200   -1.05000  11.86700  1.000 32.68287  ? 18  GLY A O     1 
ATOM   96   N  N     . ARG A 1 19  ? 7.13600   -2.76100  13.28800  1.000 25.69255  ? 19  ARG A N     1 
ATOM   97   C  CA    . ARG A 1 19  ? 8.09400   -2.28400  14.27400  1.000 25.33725  ? 19  ARG A CA    1 
ATOM   98   C  C     . ARG A 1 19  ? 9.46600   -2.89300  14.00700  1.000 24.59769  ? 19  ARG A C     1 
ATOM   99   O  O     . ARG A 1 19  ? 9.58300   -3.99200  13.45600  1.000 24.90825  ? 19  ARG A O     1 
ATOM   100  C  CB    . ARG A 1 19  ? 7.61400   -2.61900  15.68700  1.000 27.37433  ? 19  ARG A CB    1 
ATOM   101  C  CG    . ARG A 1 19  ? 6.25900   -1.98000  16.01400  1.000 31.21427  ? 19  ARG A CG    1 
ATOM   102  C  CD    . ARG A 1 19  ? 5.53400   -2.68100  17.16100  1.000 28.45341  ? 19  ARG A CD    1 
ATOM   103  N  NE    . ARG A 1 19  ? 5.25400   -4.07900  16.83700  1.000 27.60068  ? 19  ARG A NE    1 
ATOM   104  C  CZ    . ARG A 1 19  ? 4.52200   -4.89300  17.59300  1.000 33.56718  ? 19  ARG A CZ    1 
ATOM   105  N  NH1   . ARG A 1 19  ? 3.98300   -4.44700  18.71800  1.000 32.84868  ? 19  ARG A NH1   1 
ATOM   106  N  NH2   . ARG A 1 19  ? 4.32800   -6.15300  17.22400  1.000 30.30363  ? 19  ARG A NH2   1 
ATOM   107  N  N     . GLY A 1 20  ? 10.51000  -2.14300  14.35200  1.000 24.50031  ? 20  GLY A N     1 
ATOM   108  C  CA    . GLY A 1 20  ? 11.86200  -2.61400  14.15400  1.000 27.13220  ? 20  GLY A CA    1 
ATOM   109  C  C     . GLY A 1 20  ? 12.77100  -2.12000  15.25800  1.000 28.49552  ? 20  GLY A C     1 
ATOM   110  O  O     . GLY A 1 20  ? 12.33000  -1.48700  16.22000  1.000 22.09739  ? 20  GLY A O     1 
ATOM   111  N  N     . LEU A 1 21  ? 14.05600  -2.44100  15.11500  1.000 20.19979  ? 21  LEU A N     1 
ATOM   112  C  CA    . LEU A 1 21  ? 15.10000  -2.03800  16.04900  1.000 21.47626  ? 21  LEU A CA    1 
ATOM   113  C  C     . LEU A 1 21  ? 16.12900  -1.20500  15.29800  1.000 26.26368  ? 21  LEU A C     1 
ATOM   114  O  O     . LEU A 1 21  ? 16.61600  -1.61900  14.23700  1.000 24.02920  ? 21  LEU A O     1 
ATOM   115  C  CB    . LEU A 1 21  ? 15.75600  -3.25900  16.69100  1.000 21.60785  ? 21  LEU A CB    1 
ATOM   116  C  CG    . LEU A 1 21  ? 16.77100  -3.03600  17.81400  1.000 24.96352  ? 21  LEU A CG    1 
ATOM   117  C  CD1   . LEU A 1 21  ? 16.14000  -2.36500  19.03000  1.000 27.29538  ? 21  LEU A CD1   1 
ATOM   118  C  CD2   . LEU A 1 21  ? 17.38400  -4.36800  18.20200  1.000 29.50880  ? 21  LEU A CD2   1 
ATOM   119  N  N     . ARG A 1 22  ? 16.46900  -0.05300  15.86000  1.000 27.40592  ? 22  ARG A N     1 
ATOM   120  C  CA    . ARG A 1 22  ? 17.34500  0.92900   15.24100  1.000 32.70918  ? 22  ARG A CA    1 
ATOM   121  C  C     . ARG A 1 22  ? 18.51200  1.22400   16.17600  1.000 28.16127  ? 22  ARG A C     1 
ATOM   122  O  O     . ARG A 1 22  ? 18.34100  1.25500   17.40000  1.000 28.16654  ? 22  ARG A O     1 
ATOM   123  C  CB    . ARG A 1 22  ? 16.55300  2.21200   14.93100  1.000 34.99104  ? 22  ARG A CB    1 
ATOM   124  C  CG    . ARG A 1 22  ? 17.35500  3.36400   14.37700  1.000 51.09560  ? 22  ARG A CG    1 
ATOM   125  C  CD    . ARG A 1 22  ? 16.44800  4.38000   13.69900  1.000 48.35843  ? 22  ARG A CD    1 
ATOM   126  N  NE    . ARG A 1 22  ? 15.45200  4.95400   14.60300  1.000 38.17037  ? 22  ARG A NE    1 
ATOM   127  C  CZ    . ARG A 1 22  ? 14.48600  5.77900   14.20500  1.000 37.78085  ? 22  ARG A CZ    1 
ATOM   128  N  NH1   . ARG A 1 22  ? 14.39800  6.11100   12.92800  1.000 32.79077  ? 22  ARG A NH1   1 
ATOM   129  N  NH2   . ARG A 1 22  ? 13.61000  6.27400   15.07300  1.000 38.32565  ? 22  ARG A NH2   1 
ATOM   130  N  N     . ALA A 1 23  ? 19.69800  1.41900   15.60300  1.000 25.75046  ? 23  ALA A N     1 
ATOM   131  C  CA    . ALA A 1 23  ? 20.87900  1.75000   16.38900  1.000 25.42147  ? 23  ALA A CA    1 
ATOM   132  C  C     . ALA A 1 23  ? 20.93800  3.24500   16.68300  1.000 29.07454  ? 23  ALA A C     1 
ATOM   133  O  O     . ALA A 1 23  ? 20.64300  4.07600   15.81900  1.000 28.20075  ? 23  ALA A O     1 
ATOM   134  C  CB    . ALA A 1 23  ? 22.15000  1.31100   15.65700  1.000 28.13758  ? 23  ALA A CB    1 
ATOM   135  N  N     . LEU A 1 24  ? 21.32300  3.58500   17.91700  1.000 28.51395  ? 24  LEU A N     1 
ATOM   136  C  CA    . LEU A 1 24  ? 21.55000  4.96800   18.31000  1.000 32.91447  ? 24  LEU A CA    1 
ATOM   137  C  C     . LEU A 1 24  ? 23.02700  5.31400   18.44200  1.000 32.98027  ? 24  LEU A C     1 
ATOM   138  O  O     . LEU A 1 24  ? 23.36300  6.49800   18.54400  1.000 33.21714  ? 24  LEU A O     1 
ATOM   139  C  CB    . LEU A 1 24  ? 20.83600  5.26700   19.63600  1.000 37.87033  ? 24  LEU A CB    1 
ATOM   140  C  CG    . LEU A 1 24  ? 19.31700  5.18800   19.51400  1.000 40.79700  ? 24  LEU A CG    1 
ATOM   141  C  CD1   . LEU A 1 24  ? 18.64700  5.38200   20.86600  1.000 40.87595  ? 24  LEU A CD1   1 
ATOM   142  C  CD2   . LEU A 1 24  ? 18.82600  6.21600   18.50600  1.000 40.10481  ? 24  LEU A CD2   1 
ATOM   143  N  N     . GLN A 1 25  ? 23.90500  4.32300   18.42600  1.000 35.22528  ? 25  GLN A N     1 
ATOM   144  C  CA    . GLN A 1 25  ? 25.34900  4.48800   18.47300  1.000 39.78109  ? 25  GLN A CA    1 
ATOM   145  C  C     . GLN A 1 25  ? 25.96000  3.52500   17.49100  1.000 33.08291  ? 25  GLN A C     1 
ATOM   146  O  O     . GLN A 1 25  ? 25.29500  2.57300   17.03900  1.000 32.52495  ? 25  GLN A O     1 
ATOM   147  C  CB    . GLN A 1 25  ? 25.87200  4.23600   19.89600  1.000 36.42805  ? 25  GLN A CB    1 
ATOM   148  C  CG    . GLN A 1 25  ? 25.64800  2.81300   20.36600  1.000 46.00815  ? 25  GLN A CG    1 
ATOM   149  C  CD    . GLN A 1 25  ? 25.99100  2.63000   21.82900  1.000 47.48201  ? 25  GLN A CD    1 
ATOM   150  O  OE1   . GLN A 1 25  ? 25.83200  3.54900   22.63700  1.000 64.45773  ? 25  GLN A OE1   1 
ATOM   151  N  NE2   . GLN A 1 25  ? 26.45900  1.44000   22.18100  1.000 48.20841  ? 25  GLN A NE2   1 
ATOM   152  N  N     . PRO A 1 26  ? 27.22100  3.71200   17.09500  1.000 35.24896  ? 26  PRO A N     1 
ATOM   153  C  CA    . PRO A 1 26  ? 27.85200  2.78200   16.16300  1.000 29.58249  ? 26  PRO A CA    1 
ATOM   154  C  C     . PRO A 1 26  ? 28.25900  1.47900   16.84000  1.000 32.84868  ? 26  PRO A C     1 
ATOM   155  O  O     . PRO A 1 26  ? 28.64100  1.44800   18.01300  1.000 33.50402  ? 26  PRO A O     1 
ATOM   156  C  CB    . PRO A 1 26  ? 29.08100  3.54800   15.66700  1.000 28.75345  ? 26  PRO A CB    1 
ATOM   157  C  CG    . PRO A 1 26  ? 29.41700  4.45500   16.79700  1.000 34.05145  ? 26  PRO A CG    1 
ATOM   158  C  CD    . PRO A 1 26  ? 28.11600  4.84200   17.43600  1.000 29.56670  ? 26  PRO A CD    1 
ATOM   159  N  N     . PHE A 1 27  ? 28.18000  0.39300   16.07100  1.000 30.12993  ? 27  PHE A N     1 
ATOM   160  C  CA    . PHE A 1 27  ? 28.66500  -0.91500  16.49500  1.000 34.63836  ? 27  PHE A CA    1 
ATOM   161  C  C     . PHE A 1 27  ? 29.62100  -1.45300  15.44100  1.000 33.59613  ? 27  PHE A C     1 
ATOM   162  O  O     . PHE A 1 27  ? 29.29000  -1.44800  14.25000  1.000 31.89067  ? 27  PHE A O     1 
ATOM   163  C  CB    . PHE A 1 27  ? 27.51500  -1.90800  16.68600  1.000 30.25889  ? 27  PHE A CB    1 
ATOM   164  C  CG    . PHE A 1 27  ? 26.55500  -1.54600  17.79200  1.000 30.17204  ? 27  PHE A CG    1 
ATOM   165  C  CD1   . PHE A 1 27  ? 26.82400  -1.89000  19.11000  1.000 28.60606  ? 27  PHE A CD1   1 
ATOM   166  C  CD2   . PHE A 1 27  ? 25.36600  -0.89400  17.50700  1.000 29.50091  ? 27  PHE A CD2   1 
ATOM   167  C  CE1   . PHE A 1 27  ? 25.93200  -1.57300  20.12000  1.000 32.70655  ? 27  PHE A CE1   1 
ATOM   168  C  CE2   . PHE A 1 27  ? 24.47400  -0.57500  18.51400  1.000 29.99307  ? 27  PHE A CE2   1 
ATOM   169  C  CZ    . PHE A 1 27  ? 24.75900  -0.91300  19.82200  1.000 34.54362  ? 27  PHE A CZ    1 
ATOM   170  N  N     . GLN A 1 28  ? 30.78500  -1.93800  15.87800  1.000 29.44564  ? 28  GLN A N     1 
ATOM   171  C  CA    . GLN A 1 28  ? 31.75000  -2.55100  14.97900  1.000 32.70129  ? 28  GLN A CA    1 
ATOM   172  C  C     . GLN A 1 28  ? 31.49100  -4.04600  14.85700  1.000 33.27767  ? 28  GLN A C     1 
ATOM   173  O  O     . GLN A 1 28  ? 30.82900  -4.66100  15.69800  1.000 28.09284  ? 28  GLN A O     1 
ATOM   174  C  CB    . GLN A 1 28  ? 33.19000  -2.33800  15.45000  1.000 41.51024  ? 28  GLN A CB    1 
ATOM   175  C  CG    . GLN A 1 28  ? 33.57000  -0.92500  15.66100  1.000 48.32422  ? 28  GLN A CG    1 
ATOM   176  C  CD    . GLN A 1 28  ? 33.56800  -0.13700  14.37300  1.000 82.83362  ? 28  GLN A CD    1 
ATOM   177  O  OE1   . GLN A 1 28  ? 32.70000  0.70400   14.19300  1.000 83.98639  ? 28  GLN A OE1   1 
ATOM   178  N  NE2   . GLN A 1 28  ? 34.51400  -0.41600  13.45800  1.000 85.36550  ? 28  GLN A NE2   1 
ATOM   179  N  N     . VAL A 1 29  ? 32.04100  -4.62600  13.78900  1.000 31.20374  ? 29  VAL A N     1 
ATOM   180  C  CA    . VAL A 1 29  ? 31.97600  -6.06400  13.59000  1.000 32.33546  ? 29  VAL A CA    1 
ATOM   181  C  C     . VAL A 1 29  ? 32.45700  -6.75600  14.85200  1.000 28.00862  ? 29  VAL A C     1 
ATOM   182  O  O     . VAL A 1 29  ? 33.52400  -6.42800  15.38300  1.000 26.26368  ? 29  VAL A O     1 
ATOM   183  C  CB    . VAL A 1 29  ? 32.83200  -6.45800  12.37200  1.000 28.62448  ? 29  VAL A CB    1 
ATOM   184  C  CG1   . VAL A 1 29  ? 33.05400  -7.95900  12.33400  1.000 33.01185  ? 29  VAL A CG1   1 
ATOM   185  C  CG2   . VAL A 1 29  ? 32.19300  -5.95800  11.08800  1.000 29.25088  ? 29  VAL A CG2   1 
ATOM   186  N  N     . GLY A 1 30  ? 31.65200  -7.69100  15.35700  1.000 24.56084  ? 30  GLY A N     1 
ATOM   187  C  CA    . GLY A 1 30  ? 31.98700  -8.43900  16.54800  1.000 28.03757  ? 30  GLY A CA    1 
ATOM   188  C  C     . GLY A 1 30  ? 31.44700  -7.87600  17.84800  1.000 28.74555  ? 30  GLY A C     1 
ATOM   189  O  O     . GLY A 1 30  ? 31.47200  -8.58600  18.86200  1.000 33.11186  ? 30  GLY A O     1 
ATOM   190  N  N     . ASP A 1 31  ? 30.96000  -6.63500  17.85400  1.000 29.11139  ? 31  ASP A N     1 
ATOM   191  C  CA    . ASP A 1 31  ? 30.40900  -6.03500  19.06600  1.000 32.49600  ? 31  ASP A CA    1 
ATOM   192  C  C     . ASP A 1 31  ? 29.09400  -6.68900  19.46900  1.000 29.49827  ? 31  ASP A C     1 
ATOM   193  O  O     . ASP A 1 31  ? 28.26600  -7.03900  18.62300  1.000 23.54493  ? 31  ASP A O     1 
ATOM   194  C  CB    . ASP A 1 31  ? 30.18100  -4.53600  18.87800  1.000 31.49588  ? 31  ASP A CB    1 
ATOM   195  C  CG    . ASP A 1 31  ? 31.46700  -3.73500  18.92100  1.000 39.69950  ? 31  ASP A CG    1 
ATOM   196  O  OD1   . ASP A 1 31  ? 32.55300  -4.33700  19.09000  1.000 46.23712  ? 31  ASP A OD1   1 
ATOM   197  O  OD2   . ASP A 1 31  ? 31.38400  -2.48900  18.81800  1.000 49.82176  ? 31  ASP A OD2   1 
ATOM   198  N  N     . LEU A 1 32  ? 28.90200  -6.83200  20.77800  1.000 24.68717  ? 32  LEU A N     1 
ATOM   199  C  CA    . LEU A 1 32  ? 27.64100  -7.30000  21.34600  1.000 29.53512  ? 32  LEU A CA    1 
ATOM   200  C  C     . LEU A 1 32  ? 26.63800  -6.15000  21.41700  1.000 31.41956  ? 32  LEU A C     1 
ATOM   201  O  O     . LEU A 1 32  ? 26.84600  -5.18500  22.16200  1.000 33.41190  ? 32  LEU A O     1 
ATOM   202  C  CB    . LEU A 1 32  ? 27.88400  -7.87600  22.74200  1.000 29.28509  ? 32  LEU A CB    1 
ATOM   203  C  CG    . LEU A 1 32  ? 26.69000  -8.45300  23.51400  1.000 26.02944  ? 32  LEU A CG    1 
ATOM   204  C  CD1   . LEU A 1 32  ? 26.09000  -9.63300  22.77700  1.000 23.38438  ? 32  LEU A CD1   1 
ATOM   205  C  CD2   . LEU A 1 32  ? 27.12400  -8.86500  24.90700  1.000 27.41908  ? 32  LEU A CD2   1 
ATOM   206  N  N     . LEU A 1 33  ? 25.54300  -6.25000  20.65900  1.000 32.70918  ? 33  LEU A N     1 
ATOM   207  C  CA    . LEU A 1 33  ? 24.49100  -5.24000  20.76100  1.000 26.47159  ? 33  LEU A CA    1 
ATOM   208  C  C     . LEU A 1 33  ? 23.69700  -5.40500  22.05000  1.000 26.60845  ? 33  LEU A C     1 
ATOM   209  O  O     . LEU A 1 33  ? 23.53400  -4.44800  22.81500  1.000 29.33246  ? 33  LEU A O     1 
ATOM   210  C  CB    . LEU A 1 33  ? 23.55600  -5.30000  19.55200  1.000 24.00551  ? 33  LEU A CB    1 
ATOM   211  C  CG    . LEU A 1 33  ? 23.98400  -4.56000  18.28900  1.000 29.65882  ? 33  LEU A CG    1 
ATOM   212  C  CD1   . LEU A 1 33  ? 25.17800  -5.23500  17.63300  1.000 30.55366  ? 33  LEU A CD1   1 
ATOM   213  C  CD2   . LEU A 1 33  ? 22.80600  -4.45800  17.32600  1.000 25.98469  ? 33  LEU A CD2   1 
ATOM   214  N  N     . PHE A 1 34  ? 23.17700  -6.60700  22.29300  1.000 24.55821  ? 34  PHE A N     1 
ATOM   215  C  CA    . PHE A 1 34  ? 22.44600  -6.89600  23.51900  1.000 24.43714  ? 34  PHE A CA    1 
ATOM   216  C  C     . PHE A 1 34  ? 22.31600  -8.40700  23.66800  1.000 27.00587  ? 34  PHE A C     1 
ATOM   217  O  O     . PHE A 1 34  ? 22.59200  -9.17600  22.74100  1.000 23.12119  ? 34  PHE A O     1 
ATOM   218  C  CB    . PHE A 1 34  ? 21.06900  -6.21700  23.53700  1.000 24.98721  ? 34  PHE A CB    1 
ATOM   219  C  CG    . PHE A 1 34  ? 20.10400  -6.73400  22.49000  1.000 24.50820  ? 34  PHE A CG    1 
ATOM   220  C  CD1   . PHE A 1 34  ? 20.22500  -6.34700  21.15900  1.000 26.40053  ? 34  PHE A CD1   1 
ATOM   221  C  CD2   . PHE A 1 34  ? 19.05100  -7.57100  22.84700  1.000 23.08171  ? 34  PHE A CD2   1 
ATOM   222  C  CE1   . PHE A 1 34  ? 19.33400  -6.80400  20.19800  1.000 23.18173  ? 34  PHE A CE1   1 
ATOM   223  C  CE2   . PHE A 1 34  ? 18.15100  -8.03500  21.88900  1.000 28.82188  ? 34  PHE A CE2   1 
ATOM   224  C  CZ    . PHE A 1 34  ? 18.29300  -7.65100  20.56100  1.000 22.75273  ? 34  PHE A CZ    1 
ATOM   225  N  N     . SER A 1 35  ? 21.91200  -8.82000  24.86600  1.000 30.96687  ? 35  SER A N     1 
ATOM   226  C  CA    . SER A 1 35  ? 21.60500  -10.20600 25.17100  1.000 34.14620  ? 35  SER A CA    1 
ATOM   227  C  C     . SER A 1 35  ? 20.17900  -10.29000 25.69900  1.000 35.67007  ? 35  SER A C     1 
ATOM   228  O  O     . SER A 1 35  ? 19.61200  -9.30300  26.17600  1.000 38.18089  ? 35  SER A O     1 
ATOM   229  C  CB    . SER A 1 35  ? 22.59300  -10.79300 26.18900  1.000 34.01987  ? 35  SER A CB    1 
ATOM   230  O  OG    . SER A 1 35  ? 22.54800  -10.08400 27.41000  1.000 53.03004  ? 35  SER A OG    1 
ATOM   231  N  N     . CYS A 1 36  ? 19.59200  -11.47500 25.59200  1.000 29.47459  ? 36  CYS A N     1 
ATOM   232  C  CA    . CYS A 1 36  ? 18.18600  -11.61500 25.95300  1.000 29.16929  ? 36  CYS A CA    1 
ATOM   233  C  C     . CYS A 1 36  ? 17.91500  -12.98700 26.55700  1.000 25.50832  ? 36  CYS A C     1 
ATOM   234  O  O     . CYS A 1 36  ? 17.97900  -13.99900 25.84700  1.000 25.73466  ? 36  CYS A O     1 
ATOM   235  C  CB    . CYS A 1 36  ? 17.29200  -11.38400 24.72900  1.000 34.30411  ? 36  CYS A CB    1 
ATOM   236  S  SG    . CYS A 1 36  ? 15.50700  -11.42800 25.09100  1.000 31.79065  ? 36  CYS A SG    1 
ATOM   237  N  N     . PRO A 1 37  ? 17.60500  -13.06100 27.85300  1.000 21.81841  ? 37  PRO A N     1 
ATOM   238  C  CA    . PRO A 1 37  ? 17.23900  -14.34900 28.45400  1.000 24.94246  ? 37  PRO A CA    1 
ATOM   239  C  C     . PRO A 1 37  ? 15.97400  -14.89400 27.81000  1.000 24.21606  ? 37  PRO A C     1 
ATOM   240  O  O     . PRO A 1 37  ? 15.08100  -14.13900 27.42300  1.000 29.37721  ? 37  PRO A O     1 
ATOM   241  C  CB    . PRO A 1 37  ? 17.00100  -14.00300 29.93100  1.000 23.57914  ? 37  PRO A CB    1 
ATOM   242  C  CG    . PRO A 1 37  ? 17.66400  -12.68100 30.13900  1.000 30.00097  ? 37  PRO A CG    1 
ATOM   243  C  CD    . PRO A 1 37  ? 17.56500  -11.96100 28.83300  1.000 29.51933  ? 37  PRO A CD    1 
ATOM   244  N  N     . ALA A 1 38  ? 15.90900  -16.21800 27.68900  1.000 29.22719  ? 38  ALA A N     1 
ATOM   245  C  CA    . ALA A 1 38  ? 14.73800  -16.85600 27.10200  1.000 28.67712  ? 38  ALA A CA    1 
ATOM   246  C  C     . ALA A 1 38  ? 13.50700  -16.60600 27.96100  1.000 28.40077  ? 38  ALA A C     1 
ATOM   247  O  O     . ALA A 1 38  ? 13.52300  -16.83900 29.17400  1.000 27.00587  ? 38  ALA A O     1 
ATOM   248  C  CB    . ALA A 1 38  ? 14.98200  -18.35700 26.93800  1.000 27.21642  ? 38  ALA A CB    1 
ATOM   249  N  N     . TYR A 1 39  ? 12.43500  -16.12500 27.33100  1.000 25.31356  ? 39  TYR A N     1 
ATOM   250  C  CA    . TYR A 1 39  ? 11.16100  -16.03300 28.04000  1.000 26.63214  ? 39  TYR A CA    1 
ATOM   251  C  C     . TYR A 1 39  ? 10.60600  -17.42300 28.32800  1.000 26.74794  ? 39  TYR A C     1 
ATOM   252  O  O     . TYR A 1 39  ? 10.07800  -17.67800 29.41900  1.000 26.97692  ? 39  TYR A O     1 
ATOM   253  C  CB    . TYR A 1 39  ? 10.15200  -15.20500 27.23000  1.000 25.03984  ? 39  TYR A CB    1 
ATOM   254  C  CG    . TYR A 1 39  ? 8.77100   -15.12100 27.86900  1.000 26.33210  ? 39  TYR A CG    1 
ATOM   255  C  CD1   . TYR A 1 39  ? 8.45900   -14.10700 28.77400  1.000 27.05588  ? 39  TYR A CD1   1 
ATOM   256  C  CD2   . TYR A 1 39  ? 7.78300   -16.05300 27.56400  1.000 24.73981  ? 39  TYR A CD2   1 
ATOM   257  C  CE1   . TYR A 1 39  ? 7.19900   -14.03000 29.36000  1.000 28.81398  ? 39  TYR A CE1   1 
ATOM   258  C  CE2   . TYR A 1 39  ? 6.52700   -15.98800 28.14900  1.000 27.64279  ? 39  TYR A CE2   1 
ATOM   259  C  CZ    . TYR A 1 39  ? 6.24000   -14.97300 29.03800  1.000 27.67174  ? 39  TYR A CZ    1 
ATOM   260  O  OH    . TYR A 1 39  ? 4.98700   -14.91200 29.61300  1.000 34.48571  ? 39  TYR A OH    1 
ATOM   261  N  N     . ALA A 1 40  ? 10.67300  -18.31400 27.33600  1.000 30.61946  ? 40  ALA A N     1 
ATOM   262  C  CA    . ALA A 1 40  ? 10.31900  -19.71600 27.48100  1.000 24.90035  ? 40  ALA A CA    1 
ATOM   263  C  C     . ALA A 1 40  ? 11.16000  -20.51300 26.49800  1.000 27.14010  ? 40  ALA A C     1 
ATOM   264  O  O     . ALA A 1 40  ? 11.56300  -20.00300 25.44700  1.000 26.26631  ? 40  ALA A O     1 
ATOM   265  C  CB    . ALA A 1 40  ? 8.82600   -19.96900 27.23500  1.000 25.47674  ? 40  ALA A CB    1 
ATOM   266  N  N     . TYR A 1 41  ? 11.42500  -21.76800 26.84700  1.000 22.02369  ? 41  TYR A N     1 
ATOM   267  C  CA    . TYR A 1 41  ? 12.29700  -22.60400 26.03400  1.000 24.77929  ? 41  TYR A CA    1 
ATOM   268  C  C     . TYR A 1 41  ? 12.01100  -24.06600 26.33500  1.000 25.71361  ? 41  TYR A C     1 
ATOM   269  O  O     . TYR A 1 41  ? 11.45600  -24.40500 27.38700  1.000 26.72426  ? 41  TYR A O     1 
ATOM   270  C  CB    . TYR A 1 41  ? 13.77600  -22.28400 26.28700  1.000 22.28425  ? 41  TYR A CB    1 
ATOM   271  C  CG    . TYR A 1 41  ? 14.18900  -22.46100 27.72900  1.000 27.17957  ? 41  TYR A CG    1 
ATOM   272  C  CD1   . TYR A 1 41  ? 14.01900  -21.43100 28.64600  1.000 30.00623  ? 41  TYR A CD1   1 
ATOM   273  C  CD2   . TYR A 1 41  ? 14.73700  -23.65500 28.17800  1.000 27.03482  ? 41  TYR A CD2   1 
ATOM   274  C  CE1   . TYR A 1 41  ? 14.38500  -21.58200 29.97000  1.000 31.83803  ? 41  TYR A CE1   1 
ATOM   275  C  CE2   . TYR A 1 41  ? 15.11000  -23.81100 29.50600  1.000 29.76409  ? 41  TYR A CE2   1 
ATOM   276  C  CZ    . TYR A 1 41  ? 14.92800  -22.77200 30.39400  1.000 27.34538  ? 41  TYR A CZ    1 
ATOM   277  O  OH    . TYR A 1 41  ? 15.29200  -22.92100 31.71400  1.000 35.24896  ? 41  TYR A OH    1 
ATOM   278  N  N     . VAL A 1 42  ? 12.42400  -24.93200 25.41200  1.000 23.85023  ? 42  VAL A N     1 
ATOM   279  C  CA    . VAL A 1 42  ? 12.28100  -26.37200 25.60900  1.000 27.37697  ? 42  VAL A CA    1 
ATOM   280  C  C     . VAL A 1 42  ? 13.41900  -27.08500 24.88600  1.000 22.46322  ? 42  VAL A C     1 
ATOM   281  O  O     . VAL A 1 42  ? 13.77400  -26.73800 23.75300  1.000 23.97656  ? 42  VAL A O     1 
ATOM   282  C  CB    . VAL A 1 42  ? 10.88900  -26.86200 25.14500  1.000 31.48272  ? 42  VAL A CB    1 
ATOM   283  C  CG1   . VAL A 1 42  ? 10.66800  -26.61100 23.64900  1.000 31.44588  ? 42  VAL A CG1   1 
ATOM   284  C  CG2   . VAL A 1 42  ? 10.69800  -28.31000 25.49300  1.000 46.17659  ? 42  VAL A CG2   1 
ATOM   285  N  N     . LEU A 1 43  ? 14.00700  -28.07600 25.56100  1.000 24.74507  ? 43  LEU A N     1 
ATOM   286  C  CA    . LEU A 1 43  ? 15.03400  -28.92500 24.96500  1.000 29.65882  ? 43  LEU A CA    1 
ATOM   287  C  C     . LEU A 1 43  ? 14.38300  -29.97800 24.07800  1.000 26.34263  ? 43  LEU A C     1 
ATOM   288  O  O     . LEU A 1 43  ? 13.43200  -30.64800 24.49400  1.000 28.16127  ? 43  LEU A O     1 
ATOM   289  C  CB    . LEU A 1 43  ? 15.86900  -29.60200 26.05400  1.000 29.18245  ? 43  LEU A CB    1 
ATOM   290  C  CG    . LEU A 1 43  ? 17.04800  -30.44500 25.55800  1.000 29.29299  ? 43  LEU A CG    1 
ATOM   291  C  CD1   . LEU A 1 43  ? 18.17700  -29.54600 25.08700  1.000 27.85334  ? 43  LEU A CD1   1 
ATOM   292  C  CD2   . LEU A 1 43  ? 17.53900  -31.42400 26.62400  1.000 32.08016  ? 43  LEU A CD2   1 
ATOM   293  N  N     . THR A 1 44  ? 14.89200  -30.12900 22.85900  1.000 25.45568  ? 44  THR A N     1 
ATOM   294  C  CA    . THR A 1 44  ? 14.28600  -31.06900 21.92600  1.000 29.99044  ? 44  THR A CA    1 
ATOM   295  C  C     . THR A 1 44  ? 14.49600  -32.50700 22.40100  1.000 31.33270  ? 44  THR A C     1 
ATOM   296  O  O     . THR A 1 44  ? 15.49200  -32.83100 23.05500  1.000 30.15098  ? 44  THR A O     1 
ATOM   297  C  CB    . THR A 1 44  ? 14.83700  -30.85500 20.50700  1.000 24.51347  ? 44  THR A CB    1 
ATOM   298  O  OG1   . THR A 1 44  ? 13.99100  -31.53000 19.57100  1.000 29.07717  ? 44  THR A OG1   1 
ATOM   299  C  CG2   . THR A 1 44  ? 16.25400  -31.39100 20.36800  1.000 26.72952  ? 44  THR A CG2   1 
ATOM   300  N  N     . VAL A 1 45  ? 13.52200  -33.36600 22.09000  1.000 33.13292  ? 45  VAL A N     1 
ATOM   301  C  CA    . VAL A 1 45  ? 13.48700  -34.71300 22.66400  1.000 34.91734  ? 45  VAL A CA    1 
ATOM   302  C  C     . VAL A 1 45  ? 14.76600  -35.48100 22.34700  1.000 38.57568  ? 45  VAL A C     1 
ATOM   303  O  O     . VAL A 1 45  ? 15.31500  -36.18200 23.20900  1.000 39.74687  ? 45  VAL A O     1 
ATOM   304  C  CB    . VAL A 1 45  ? 12.22400  -35.46300 22.18900  1.000 40.08375  ? 45  VAL A CB    1 
ATOM   305  C  CG1   . VAL A 1 45  ? 12.35100  -36.95900 22.42400  1.000 41.67342  ? 45  VAL A CG1   1 
ATOM   306  C  CG2   . VAL A 1 45  ? 11.00200  -34.93900 22.93000  1.000 36.74914  ? 45  VAL A CG2   1 
ATOM   307  N  N     . ASN A 1 46  ? 15.27500  -35.35300 21.12000  1.000 43.27098  ? 46  ASN A N     1 
ATOM   308  C  CA    . ASN A 1 46  ? 16.44400  -36.12800 20.71300  1.000 50.88768  ? 46  ASN A CA    1 
ATOM   309  C  C     . ASN A 1 46  ? 17.72600  -35.73500 21.43900  1.000 45.82655  ? 46  ASN A C     1 
ATOM   310  O  O     . ASN A 1 46  ? 18.70900  -36.47700 21.34700  1.000 41.82344  ? 46  ASN A O     1 
ATOM   311  C  CB    . ASN A 1 46  ? 16.66200  -36.01000 19.20400  1.000 58.67546  ? 46  ASN A CB    1 
ATOM   312  C  CG    . ASN A 1 46  ? 15.66800  -36.83000 18.41100  1.000 54.15123  ? 46  ASN A CG    1 
ATOM   313  O  OD1   . ASN A 1 46  ? 15.12200  -37.81500 18.91000  1.000 61.18892  ? 46  ASN A OD1   1 
ATOM   314  N  ND2   . ASN A 1 46  ? 15.42200  -36.42700 17.17000  1.000 77.65668  ? 46  ASN A ND2   1 
ATOM   315  N  N     . GLU A 1 47  ? 17.76100  -34.59700 22.13300  1.000 41.61025  ? 47  GLU A N     1 
ATOM   316  C  CA    . GLU A 1 47  ? 18.96300  -34.17300 22.84100  1.000 37.91244  ? 47  GLU A CA    1 
ATOM   317  C  C     . GLU A 1 47  ? 18.89500  -34.42600 24.34100  1.000 37.37027  ? 47  GLU A C     1 
ATOM   318  O  O     . GLU A 1 47  ? 19.80600  -34.01600 25.06800  1.000 42.41824  ? 47  GLU A O     1 
ATOM   319  C  CB    . GLU A 1 47  ? 19.24800  -32.69500 22.57000  1.000 36.67282  ? 47  GLU A CB    1 
ATOM   320  C  CG    . GLU A 1 47  ? 19.59000  -32.39100 21.11100  1.000 42.89462  ? 47  GLU A CG    1 
ATOM   321  C  CD    . GLU A 1 47  ? 20.87400  -33.05400 20.62800  1.000 47.17145  ? 47  GLU A CD    1 
ATOM   322  O  OE1   . GLU A 1 47  ? 21.72400  -33.41500 21.47300  1.000 43.74998  ? 47  GLU A OE1   1 
ATOM   323  O  OE2   . GLU A 1 47  ? 21.02500  -33.21800 19.39500  1.000 48.96640  ? 47  GLU A OE2   1 
ATOM   324  N  N     . ARG A 1 48  ? 17.84800  -35.09500 24.81900  1.000 35.55426  ? 48  ARG A N     1 
ATOM   325  C  CA    . ARG A 1 48  ? 17.77500  -35.47100 26.22500  1.000 43.47890  ? 48  ARG A CA    1 
ATOM   326  C  C     . ARG A 1 48  ? 18.88000  -36.46300 26.57400  1.000 38.94151  ? 48  ARG A C     1 
ATOM   327  O  O     . ARG A 1 48  ? 19.16300  -37.39700 25.81900  1.000 42.75776  ? 48  ARG A O     1 
ATOM   328  C  CB    . ARG A 1 48  ? 16.41000  -36.08500 26.52800  1.000 46.13974  ? 48  ARG A CB    1 
ATOM   329  C  CG    . ARG A 1 48  ? 15.25700  -35.11600 26.41100  1.000 48.23210  ? 48  ARG A CG    1 
ATOM   330  C  CD    . ARG A 1 48  ? 13.93800  -35.85500 26.44200  1.000 45.97130  ? 48  ARG A CD    1 
ATOM   331  N  NE    . ARG A 1 48  ? 12.81700  -34.96900 26.73200  1.000 49.54541  ? 48  ARG A NE    1 
ATOM   332  C  CZ    . ARG A 1 48  ? 11.55000  -35.36700 26.77500  1.000 58.72809  ? 48  ARG A CZ    1 
ATOM   333  N  NH1   . ARG A 1 48  ? 11.24600  -36.64000 26.54200  1.000 43.79999  ? 48  ARG A NH1   1 
ATOM   334  N  NH2   . ARG A 1 48  ? 10.58900  -34.49400 27.04800  1.000 49.88493  ? 48  ARG A NH2   1 
ATOM   335  N  N     . GLY A 1 49  ? 19.49900  -36.26500 27.73400  1.000 49.68490  ? 49  GLY A N     1 
ATOM   336  C  CA    . GLY A 1 49  ? 20.61000  -37.08700 28.15300  1.000 52.98004  ? 49  GLY A CA    1 
ATOM   337  C  C     . GLY A 1 49  ? 21.96700  -36.53200 27.78400  1.000 47.96101  ? 49  GLY A C     1 
ATOM   338  O  O     . GLY A 1 49  ? 22.95900  -36.87600 28.43100  1.000 46.75034  ? 49  GLY A O     1 
ATOM   339  N  N     . ASN A 1 50  ? 22.03500  -35.69400 26.75300  1.000 46.20291  ? 50  ASN A N     1 
ATOM   340  C  CA    . ASN A 1 50  ? 23.26000  -35.00700 26.37400  1.000 46.03447  ? 50  ASN A CA    1 
ATOM   341  C  C     . ASN A 1 50  ? 23.33300  -33.59600 26.93100  1.000 45.27122  ? 50  ASN A C     1 
ATOM   342  O  O     . ASN A 1 50  ? 24.43500  -33.08700 27.15900  1.000 44.76853  ? 50  ASN A O     1 
ATOM   343  C  CB    . ASN A 1 50  ? 23.38200  -34.94200 24.84700  1.000 45.59494  ? 50  ASN A CB    1 
ATOM   344  C  CG    . ASN A 1 50  ? 23.31100  -36.30900 24.19800  1.000 66.62641  ? 50  ASN A CG    1 
ATOM   345  O  OD1   . ASN A 1 50  ? 23.80500  -37.29800 24.74300  1.000 87.32889  ? 50  ASN A OD1   1 
ATOM   346  N  ND2   . ASN A 1 50  ? 22.68300  -36.37600 23.02800  1.000 61.35736  ? 50  ASN A ND2   1 
ATOM   347  N  N     . HIS A 1 51  ? 22.18400  -32.96600 27.16700  1.000 47.23724  ? 51  HIS A N     1 
ATOM   348  C  CA    . HIS A 1 51  ? 22.11200  -31.58600 27.61700  1.000 41.19441  ? 51  HIS A CA    1 
ATOM   349  C  C     . HIS A 1 51  ? 21.24700  -31.48200 28.86400  1.000 41.25495  ? 51  HIS A C     1 
ATOM   350  O  O     . HIS A 1 51  ? 20.28100  -32.23200 29.03700  1.000 51.94044  ? 51  HIS A O     1 
ATOM   351  C  CB    . HIS A 1 51  ? 21.53000  -30.67700 26.51900  1.000 43.16307  ? 51  HIS A CB    1 
ATOM   352  C  CG    . HIS A 1 51  ? 22.39300  -30.56400 25.30000  1.000 35.59111  ? 51  HIS A CG    1 
ATOM   353  N  ND1   . HIS A 1 51  ? 23.16800  -29.45600 25.03900  1.000 38.11510  ? 51  HIS A ND1   1 
ATOM   354  C  CD2   . HIS A 1 51  ? 22.59600  -31.41700 24.26700  1.000 43.16570  ? 51  HIS A CD2   1 
ATOM   355  C  CE1   . HIS A 1 51  ? 23.81600  -29.63100 23.90000  1.000 41.97082  ? 51  HIS A CE1   1 
ATOM   356  N  NE2   . HIS A 1 51  ? 23.48600  -30.81200 23.41100  1.000 35.59374  ? 51  HIS A NE2   1 
ATOM   357  N  N     . CYS A 1 52  ? 21.58900  -30.52300 29.72000  1.000 36.08064  ? 52  CYS A N     1 
ATOM   358  C  CA    . CYS A 1 52  ? 20.76300  -30.22200 30.88100  1.000 34.40939  ? 52  CYS A CA    1 
ATOM   359  C  C     . CYS A 1 52  ? 19.48700  -29.51300 30.44300  1.000 37.00707  ? 52  CYS A C     1 
ATOM   360  O  O     . CYS A 1 52  ? 19.53600  -28.54100 29.68400  1.000 32.82499  ? 52  CYS A O     1 
ATOM   361  C  CB    . CYS A 1 52  ? 21.54200  -29.35100 31.86300  1.000 30.79843  ? 52  CYS A CB    1 
ATOM   362  S  SG    . CYS A 1 52  ? 20.56600  -28.67900 33.22600  1.000 38.12562  ? 52  CYS A SG    1 
ATOM   363  N  N     . GLU A 1 53  ? 18.34300  -29.97500 30.95900  1.000 34.43308  ? 53  GLU A N     1 
ATOM   364  C  CA    . GLU A 1 53  ? 17.06400  -29.40200 30.54900  1.000 42.49983  ? 53  GLU A CA    1 
ATOM   365  C  C     . GLU A 1 53  ? 16.98400  -27.92100 30.89700  1.000 40.76278  ? 53  GLU A C     1 
ATOM   366  O  O     . GLU A 1 53  ? 16.39600  -27.13300 30.14700  1.000 33.41190  ? 53  GLU A O     1 
ATOM   367  C  CB    . GLU A 1 53  ? 15.90900  -30.15900 31.20800  1.000 46.72139  ? 53  GLU A CB    1 
ATOM   368  C  CG    . GLU A 1 53  ? 15.79600  -31.62700 30.82900  1.000 47.76889  ? 53  GLU A CG    1 
ATOM   369  C  CD    . GLU A 1 53  ? 14.90400  -31.86800 29.62500  1.000 42.84198  ? 53  GLU A CD    1 
ATOM   370  O  OE1   . GLU A 1 53  ? 14.05700  -31.00300 29.31300  1.000 46.92142  ? 53  GLU A OE1   1 
ATOM   371  O  OE2   . GLU A 1 53  ? 15.04000  -32.93700 28.99700  1.000 53.00109  ? 53  GLU A OE2   1 
ATOM   372  N  N     . TYR A 1 54  ? 17.56700  -27.52300 32.03100  1.000 32.94342  ? 54  TYR A N     1 
ATOM   373  C  CA    . TYR A 1 54  ? 17.41400  -26.14900 32.50300  1.000 30.41417  ? 54  TYR A CA    1 
ATOM   374  C  C     . TYR A 1 54  ? 18.31300  -25.17300 31.75000  1.000 38.36513  ? 54  TYR A C     1 
ATOM   375  O  O     . TYR A 1 54  ? 17.83700  -24.16700 31.21000  1.000 38.54936  ? 54  TYR A O     1 
ATOM   376  C  CB    . TYR A 1 54  ? 17.69300  -26.06200 34.00600  1.000 33.19082  ? 54  TYR A CB    1 
ATOM   377  C  CG    . TYR A 1 54  ? 17.48800  -24.66400 34.52800  1.000 37.46765  ? 54  TYR A CG    1 
ATOM   378  C  CD1   . TYR A 1 54  ? 16.23000  -24.07200 34.49400  1.000 35.46478  ? 54  TYR A CD1   1 
ATOM   379  C  CD2   . TYR A 1 54  ? 18.54900  -23.92600 35.04000  1.000 39.25471  ? 54  TYR A CD2   1 
ATOM   380  C  CE1   . TYR A 1 54  ? 16.03100  -22.78800 34.95900  1.000 45.54757  ? 54  TYR A CE1   1 
ATOM   381  C  CE2   . TYR A 1 54  ? 18.36100  -22.64000 35.51000  1.000 46.28450  ? 54  TYR A CE2   1 
ATOM   382  C  CZ    . TYR A 1 54  ? 17.09900  -22.07600 35.46800  1.000 47.78994  ? 54  TYR A CZ    1 
ATOM   383  O  OH    . TYR A 1 54  ? 16.90200  -20.79600 35.93500  1.000 52.36944  ? 54  TYR A OH    1 
ATOM   384  N  N     . CYS A 1 55  ? 19.61900  -25.44000 31.72200  1.000 34.43571  ? 55  CYS A N     1 
ATOM   385  C  CA    . CYS A 1 55  ? 20.59100  -24.47200 31.22800  1.000 40.38905  ? 55  CYS A CA    1 
ATOM   386  C  C     . CYS A 1 55  ? 21.23500  -24.86100 29.90300  1.000 31.68011  ? 55  CYS A C     1 
ATOM   387  O  O     . CYS A 1 55  ? 22.04800  -24.09000 29.38100  1.000 40.14955  ? 55  CYS A O     1 
ATOM   388  C  CB    . CYS A 1 55  ? 21.68100  -24.24800 32.28100  1.000 48.21104  ? 55  CYS A CB    1 
ATOM   389  S  SG    . CYS A 1 55  ? 22.81400  -25.63200 32.41900  1.000 49.25854  ? 55  CYS A SG    1 
ATOM   390  N  N     . PHE A 1 56  ? 20.90300  -26.03400 29.35600  1.000 31.67485  ? 56  PHE A N     1 
ATOM   391  C  CA    . PHE A 1 56  ? 21.30700  -26.51800 28.03400  1.000 30.33785  ? 56  PHE A CA    1 
ATOM   392  C  C     . PHE A 1 56  ? 22.78100  -26.89600 27.94800  1.000 44.64219  ? 56  PHE A C     1 
ATOM   393  O  O     . PHE A 1 56  ? 23.27400  -27.18400 26.84700  1.000 31.97225  ? 56  PHE A O     1 
ATOM   394  C  CB    . PHE A 1 56  ? 20.98100  -25.50700 26.92600  1.000 32.29071  ? 56  PHE A CB    1 
ATOM   395  C  CG    . PHE A 1 56  ? 19.55900  -25.58100 26.43100  1.000 31.25112  ? 56  PHE A CG    1 
ATOM   396  C  CD1   . PHE A 1 56  ? 18.52900  -25.95600 27.28200  1.000 31.48535  ? 56  PHE A CD1   1 
ATOM   397  C  CD2   . PHE A 1 56  ? 19.25500  -25.27500 25.11200  1.000 29.64303  ? 56  PHE A CD2   1 
ATOM   398  C  CE1   . PHE A 1 56  ? 17.22400  -26.02000 26.82500  1.000 27.52172  ? 56  PHE A CE1   1 
ATOM   399  C  CE2   . PHE A 1 56  ? 17.95800  -25.33900 24.64700  1.000 30.30890  ? 56  PHE A CE2   1 
ATOM   400  C  CZ    . PHE A 1 56  ? 16.93700  -25.70800 25.50800  1.000 28.96926  ? 56  PHE A CZ    1 
ATOM   401  N  N     . THR A 1 57  ? 23.49200  -26.92800 29.07300  1.000 42.23138  ? 57  THR A N     1 
ATOM   402  C  CA    . THR A 1 57  ? 24.89900  -27.31000 29.07200  1.000 45.58968  ? 57  THR A CA    1 
ATOM   403  C  C     . THR A 1 57  ? 25.06800  -28.77000 28.66800  1.000 44.32900  ? 57  THR A C     1 
ATOM   404  O  O     . THR A 1 57  ? 24.43500  -29.66300 29.24000  1.000 39.85741  ? 57  THR A O     1 
ATOM   405  C  CB    . THR A 1 57  ? 25.50600  -27.08200 30.45600  1.000 54.85131  ? 57  THR A CB    1 
ATOM   406  O  OG1   . THR A 1 57  ? 25.33000  -25.71100 30.83400  1.000 53.27218  ? 57  THR A OG1   1 
ATOM   407  C  CG2   . THR A 1 57  ? 26.99000  -27.41900 30.45100  1.000 56.20674  ? 57  THR A CG2   1 
ATOM   408  N  N     . ARG A 1 58  ? 25.94500  -29.01000 27.69700  1.000 43.26571  ? 58  ARG A N     1 
ATOM   409  C  CA    . ARG A 1 58  ? 26.28800  -30.35600 27.25900  1.000 45.05277  ? 58  ARG A CA    1 
ATOM   410  C  C     . ARG A 1 58  ? 27.41900  -30.88800 28.13300  1.000 58.21751  ? 58  ARG A C     1 
ATOM   411  O  O     . ARG A 1 58  ? 28.47000  -30.24900 28.24900  1.000 51.83516  ? 58  ARG A O     1 
ATOM   412  C  CB    . ARG A 1 58  ? 26.70300  -30.35100 25.79000  1.000 44.59219  ? 58  ARG A CB    1 
ATOM   413  C  CG    . ARG A 1 58  ? 26.93600  -31.72800 25.20000  1.000 53.22217  ? 58  ARG A CG    1 
ATOM   414  C  CD    . ARG A 1 58  ? 27.47700  -31.64000 23.78000  1.000 49.99020  ? 58  ARG A CD    1 
ATOM   415  N  NE    . ARG A 1 58  ? 28.59900  -30.71000 23.66700  1.000 77.97251  ? 58  ARG A NE    1 
ATOM   416  C  CZ    . ARG A 1 58  ? 28.59200  -29.60100 22.93100  1.000 104.22039 ? 58  ARG A CZ    1 
ATOM   417  N  NH1   . ARG A 1 58  ? 27.52000  -29.27400 22.21900  1.000 71.70333  ? 58  ARG A NH1   1 
ATOM   418  N  NH2   . ARG A 1 58  ? 29.66600  -28.82200 22.89600  1.000 84.08377  ? 58  ARG A NH2   1 
ATOM   419  N  N     . LYS A 1 59  ? 27.20200  -32.04800 28.74900  1.000 60.19669  ? 59  LYS A N     1 
ATOM   420  C  CA    . LYS A 1 59  ? 28.23900  -32.70700 29.53300  1.000 66.13161  ? 59  LYS A CA    1 
ATOM   421  C  C     . LYS A 1 59  ? 27.83000  -34.15200 29.76900  1.000 63.15757  ? 59  LYS A C     1 
ATOM   422  O  O     . LYS A 1 59  ? 26.67000  -34.52600 29.58100  1.000 65.90001  ? 59  LYS A O     1 
ATOM   423  C  CB    . LYS A 1 59  ? 28.48000  -31.99300 30.86900  1.000 65.59997  ? 59  LYS A CB    1 
ATOM   424  C  CG    . LYS A 1 59  ? 27.25100  -31.92200 31.75100  1.000 70.27158  ? 59  LYS A CG    1 
ATOM   425  C  CD    . LYS A 1 59  ? 27.58300  -31.44000 33.15100  1.000 67.70022  ? 59  LYS A CD    1 
ATOM   426  C  CE    . LYS A 1 59  ? 28.00300  -29.98700 33.13700  1.000 71.17696  ? 59  LYS A CE    1 
ATOM   427  N  NZ    . LYS A 1 59  ? 28.22400  -29.46800 34.51500  1.000 97.33799  ? 59  LYS A NZ    1 
ATOM   428  N  N     . GLU A 1 60  ? 28.80300  -34.96000 30.18300  1.000 74.64053  ? 60  GLU A N     1 
ATOM   429  C  CA    . GLU A 1 60  ? 28.55900  -36.35100 30.53300  1.000 84.22852  ? 60  GLU A CA    1 
ATOM   430  C  C     . GLU A 1 60  ? 28.20400  -36.46800 32.01000  1.000 88.00002  ? 60  GLU A C     1 
ATOM   431  O  O     . GLU A 1 60  ? 28.63600  -35.66100 32.83700  1.000 64.28666  ? 60  GLU A O     1 
ATOM   432  C  CB    . GLU A 1 60  ? 29.77900  -37.22200 30.22000  1.000 84.13904  ? 60  GLU A CB    1 
ATOM   433  C  CG    . GLU A 1 60  ? 30.12400  -37.32900 28.73700  1.000 90.24503  ? 60  GLU A CG    1 
ATOM   434  C  CD    . GLU A 1 60  ? 29.07300  -38.08300 27.93000  1.000 102.18067 ? 60  GLU A CD    1 
ATOM   435  O  OE1   . GLU A 1 60  ? 28.26400  -38.82200 28.53400  1.000 110.88435 ? 60  GLU A OE1   1 
ATOM   436  O  OE2   . GLU A 1 60  ? 29.05700  -37.93800 26.68800  1.000 90.14765  ? 60  GLU A OE2   1 
ATOM   437  N  N     . GLY A 1 61  ? 27.41400  -37.49000 32.33300  1.000 77.33296  ? 61  GLY A N     1 
ATOM   438  C  CA    . GLY A 1 61  ? 27.03900  -37.76000 33.70800  1.000 69.28462  ? 61  GLY A CA    1 
ATOM   439  C  C     . GLY A 1 61  ? 26.04800  -36.77300 34.29400  1.000 72.62187  ? 61  GLY A C     1 
ATOM   440  O  O     . GLY A 1 61  ? 26.24300  -36.27200 35.40700  1.000 60.23880  ? 61  GLY A O     1 
ATOM   441  N  N     . LEU A 1 62  ? 24.98500  -36.48100 33.54600  1.000 51.02717  ? 62  LEU A N     1 
ATOM   442  C  CA    . LEU A 1 62  ? 23.91900  -35.61800 34.03300  1.000 47.41621  ? 62  LEU A CA    1 
ATOM   443  C  C     . LEU A 1 62  ? 23.00300  -36.39100 34.97700  1.000 54.43021  ? 62  LEU A C     1 
ATOM   444  O  O     . LEU A 1 62  ? 22.74000  -37.58100 34.77700  1.000 62.03639  ? 62  LEU A O     1 
ATOM   445  C  CB    . LEU A 1 62  ? 23.11400  -35.05700 32.85800  1.000 48.26631  ? 62  LEU A CB    1 
ATOM   446  C  CG    . LEU A 1 62  ? 23.83100  -34.06200 31.94200  1.000 43.71840  ? 62  LEU A CG    1 
ATOM   447  C  CD1   . LEU A 1 62  ? 23.09100  -33.88100 30.62900  1.000 40.32062  ? 62  LEU A CD1   1 
ATOM   448  C  CD2   . LEU A 1 62  ? 23.96800  -32.72500 32.64700  1.000 50.08232  ? 62  LEU A CD2   1 
ATOM   449  N  N     . SER A 1 63  ? 22.51100  -35.70700 36.00700  1.000 68.93195  ? 63  SER A N     1 
ATOM   450  C  CA    . SER A 1 63  ? 21.59100  -36.32900 36.95100  1.000 57.45426  ? 63  SER A CA    1 
ATOM   451  C  C     . SER A 1 63  ? 20.23800  -36.55500 36.28700  1.000 60.38619  ? 63  SER A C     1 
ATOM   452  O  O     . SER A 1 63  ? 19.67900  -35.64600 35.66700  1.000 53.80119  ? 63  SER A O     1 
ATOM   453  C  CB    . SER A 1 63  ? 21.43500  -35.45900 38.19900  1.000 58.95970  ? 63  SER A CB    1 
ATOM   454  O  OG    . SER A 1 63  ? 22.69000  -35.20300 38.80800  1.000 80.42543  ? 63  SER A OG    1 
ATOM   455  N  N     . LYS A 1 64  ? 19.72000  -37.77400 36.40400  1.000 47.77415  ? 64  LYS A N     1 
ATOM   456  C  CA    . LYS A 1 64  ? 18.46400  -38.15800 35.77500  1.000 48.79269  ? 64  LYS A CA    1 
ATOM   457  C  C     . LYS A 1 64  ? 17.29900  -37.98700 36.74700  1.000 47.92680  ? 64  LYS A C     1 
ATOM   458  O  O     . LYS A 1 64  ? 17.40800  -38.32700 37.92900  1.000 49.42435  ? 64  LYS A O     1 
ATOM   459  C  CB    . LYS A 1 64  ? 18.55100  -39.60600 35.28800  1.000 58.62019  ? 64  LYS A CB    1 
ATOM   460  C  CG    . LYS A 1 64  ? 17.29300  -40.14300 34.64000  1.000 71.17959  ? 64  LYS A CG    1 
ATOM   461  C  CD    . LYS A 1 64  ? 17.58300  -41.43700 33.89600  1.000 83.86005  ? 64  LYS A CD    1 
ATOM   462  C  CE    . LYS A 1 64  ? 18.03200  -42.53400 34.84900  1.000 78.00935  ? 64  LYS A CE    1 
ATOM   463  N  NZ    . LYS A 1 64  ? 18.36900  -43.79500 34.13100  1.000 88.26321  ? 64  LYS A NZ    1 
ATOM   464  N  N     . CYS A 1 65  ? 16.19000  -37.43700 36.24900  1.000 58.19908  ? 65  CYS A N     1 
ATOM   465  C  CA    . CYS A 1 65  ? 14.99800  -37.26200 37.07500  1.000 56.22516  ? 65  CYS A CA    1 
ATOM   466  C  C     . CYS A 1 65  ? 14.45300  -38.61800 37.50600  1.000 57.57796  ? 65  CYS A C     1 
ATOM   467  O  O     . CYS A 1 65  ? 14.08100  -39.44100 36.66700  1.000 60.72833  ? 65  CYS A O     1 
ATOM   468  C  CB    . CYS A 1 65  ? 13.93200  -36.47500 36.31100  1.000 54.32493  ? 65  CYS A CB    1 
ATOM   469  S  SG    . CYS A 1 65  ? 12.39000  -36.21900 37.23700  1.000 53.80645  ? 65  CYS A SG    1 
ATOM   470  N  N     . GLY A 1 66  ? 14.41300  -38.85000 38.82000  1.000 71.86125  ? 66  GLY A N     1 
ATOM   471  C  CA    . GLY A 1 66  ? 14.02100  -40.14900 39.34600  1.000 69.78731  ? 66  GLY A CA    1 
ATOM   472  C  C     . GLY A 1 66  ? 12.59000  -40.55300 39.05000  1.000 74.65106  ? 66  GLY A C     1 
ATOM   473  O  O     . GLY A 1 66  ? 12.26600  -41.74400 39.12000  1.000 80.20699  ? 66  GLY A O     1 
ATOM   474  N  N     . ARG A 1 67  ? 11.72000  -39.59400 38.73500  1.000 59.33080  ? 67  ARG A N     1 
ATOM   475  C  CA    . ARG A 1 67  ? 10.30900  -39.90500 38.52700  1.000 55.80669  ? 67  ARG A CA    1 
ATOM   476  C  C     . ARG A 1 67  ? 10.05600  -40.41600 37.11300  1.000 57.04631  ? 67  ARG A C     1 
ATOM   477  O  O     . ARG A 1 67  ? 9.51100   -41.50800 36.91900  1.000 57.90431  ? 67  ARG A O     1 
ATOM   478  C  CB    . ARG A 1 67  ? 9.45600   -38.66800 38.81200  1.000 61.65476  ? 67  ARG A CB    1 
ATOM   479  C  CG    . ARG A 1 67  ? 9.69500   -38.10500 40.19200  1.000 73.32458  ? 67  ARG A CG    1 
ATOM   480  C  CD    . ARG A 1 67  ? 8.92400   -36.82400 40.44300  1.000 78.77787  ? 67  ARG A CD    1 
ATOM   481  N  NE    . ARG A 1 67  ? 9.49300   -36.07700 41.56100  1.000 91.88470  ? 67  ARG A NE    1 
ATOM   482  C  CZ    . ARG A 1 67  ? 8.97100   -34.96400 42.06200  1.000 96.22733  ? 67  ARG A CZ    1 
ATOM   483  N  NH1   . ARG A 1 67  ? 7.84800   -34.48000 41.56200  1.000 120.40391 ? 67  ARG A NH1   1 
ATOM   484  N  NH2   . ARG A 1 67  ? 9.56100   -34.34300 43.07400  1.000 101.36742 ? 67  ARG A NH2   1 
ATOM   485  N  N     . CYS A 1 68  ? 10.43600  -39.62000 36.11500  1.000 53.39324  ? 68  CYS A N     1 
ATOM   486  C  CA    . CYS A 1 68  ? 10.18100  -39.92500 34.71700  1.000 45.20542  ? 68  CYS A CA    1 
ATOM   487  C  C     . CYS A 1 68  ? 11.38600  -40.50500 33.98900  1.000 49.21380  ? 68  CYS A C     1 
ATOM   488  O  O     . CYS A 1 68  ? 11.20900  -41.11300 32.92500  1.000 44.76853  ? 68  CYS A O     1 
ATOM   489  C  CB    . CYS A 1 68  ? 9.69700   -38.65700 34.00000  1.000 51.12192  ? 68  CYS A CB    1 
ATOM   490  S  SG    . CYS A 1 68  ? 10.94800  -37.34600 33.87200  1.000 42.19716  ? 68  CYS A SG    1 
ATOM   491  N  N     . LYS A 1 69  ? 12.59500  -40.34000 34.53800  1.000 46.55558  ? 69  LYS A N     1 
ATOM   492  C  CA    . LYS A 1 69  ? 13.82700  -40.86800 33.93800  1.000 53.30376  ? 69  LYS A CA    1 
ATOM   493  C  C     . LYS A 1 69  ? 14.01900  -40.39000 32.50200  1.000 44.14213  ? 69  LYS A C     1 
ATOM   494  O  O     . LYS A 1 69  ? 14.64700  -41.06900 31.68600  1.000 61.03100  ? 69  LYS A O     1 
ATOM   495  C  CB    . LYS A 1 69  ? 13.86100  -42.39800 33.99600  1.000 61.48369  ? 69  LYS A CB    1 
ATOM   496  C  CG    . LYS A 1 69  ? 14.16400  -42.98000 35.36900  1.000 63.31549  ? 69  LYS A CG    1 
ATOM   497  C  CD    . LYS A 1 69  ? 12.90200  -43.32700 36.13000  1.000 79.23582  ? 69  LYS A CD    1 
ATOM   498  C  CE    . LYS A 1 69  ? 13.21900  -44.19600 37.34000  1.000 87.10781  ? 69  LYS A CE    1 
ATOM   499  N  NZ    . LYS A 1 69  ? 12.00700  -44.47100 38.16500  1.000 91.73731  ? 69  LYS A NZ    1 
ATOM   500  N  N     . GLN A 1 70  ? 13.49100  -39.21000 32.17800  1.000 51.05612  ? 70  GLN A N     1 
ATOM   501  C  CA    . GLN A 1 70  ? 13.58400  -38.72600 30.80700  1.000 48.70321  ? 70  GLN A CA    1 
ATOM   502  C  C     . GLN A 1 70  ? 13.94400  -37.24300 30.74300  1.000 53.21691  ? 70  GLN A C     1 
ATOM   503  O  O     . GLN A 1 70  ? 13.72500  -36.60200 29.70800  1.000 90.27925  ? 70  GLN A O     1 
ATOM   504  C  CB    . GLN A 1 70  ? 12.27500  -39.00900 30.06700  1.000 45.25806  ? 70  GLN A CB    1 
ATOM   505  C  CG    . GLN A 1 70  ? 12.11800  -40.46800 29.67800  1.000 45.11067  ? 70  GLN A CG    1 
ATOM   506  C  CD    . GLN A 1 70  ? 10.83000  -40.74300 28.94000  1.000 47.08459  ? 70  GLN A CD    1 
ATOM   507  O  OE1   . GLN A 1 70  ? 10.80100  -40.77100 27.70700  1.000 61.89690  ? 70  GLN A OE1   1 
ATOM   508  N  NE2   . GLN A 1 70  ? 9.75300   -40.95700 29.68800  1.000 51.69567  ? 70  GLN A NE2   1 
ATOM   509  N  N     . ALA A 1 71  ? 14.48200  -36.68900 31.82500  1.000 44.37901  ? 71  ALA A N     1 
ATOM   510  C  CA    . ALA A 1 71  ? 14.97800  -35.32200 31.87000  1.000 43.88158  ? 71  ALA A CA    1 
ATOM   511  C  C     . ALA A 1 71  ? 16.25200  -35.32500 32.69700  1.000 55.64615  ? 71  ALA A C     1 
ATOM   512  O  O     . ALA A 1 71  ? 16.26700  -35.86600 33.80700  1.000 49.03746  ? 71  ALA A O     1 
ATOM   513  C  CB    . ALA A 1 71  ? 13.94500  -34.36200 32.47100  1.000 41.10756  ? 71  ALA A CB    1 
ATOM   514  N  N     . PHE A 1 72  ? 17.31900  -34.75400 32.15300  1.000 41.83396  ? 72  PHE A N     1 
ATOM   515  C  CA    . PHE A 1 72  ? 18.62900  -34.80400 32.78200  1.000 39.85741  ? 72  PHE A CA    1 
ATOM   516  C  C     . PHE A 1 72  ? 19.08000  -33.40000 33.16300  1.000 42.93673  ? 72  PHE A C     1 
ATOM   517  O  O     . PHE A 1 72  ? 18.70200  -32.41500 32.52000  1.000 46.79772  ? 72  PHE A O     1 
ATOM   518  C  CB    . PHE A 1 72  ? 19.64900  -35.47700 31.85400  1.000 38.77833  ? 72  PHE A CB    1 
ATOM   519  C  CG    . PHE A 1 72  ? 19.33600  -36.92400 31.56100  1.000 41.34969  ? 72  PHE A CG    1 
ATOM   520  C  CD1   . PHE A 1 72  ? 18.33000  -37.26600 30.66800  1.000 37.75453  ? 72  PHE A CD1   1 
ATOM   521  C  CD2   . PHE A 1 72  ? 20.04900  -37.94000 32.17600  1.000 46.51610  ? 72  PHE A CD2   1 
ATOM   522  C  CE1   . PHE A 1 72  ? 18.04100  -38.59100 30.39700  1.000 41.93924  ? 72  PHE A CE1   1 
ATOM   523  C  CE2   . PHE A 1 72  ? 19.76500  -39.26900 31.90700  1.000 56.57784  ? 72  PHE A CE2   1 
ATOM   524  C  CZ    . PHE A 1 72  ? 18.75800  -39.59400 31.01700  1.000 49.33749  ? 72  PHE A CZ    1 
ATOM   525  N  N     . TYR A 1 73  ? 19.88400  -33.31400 34.22400  1.000 44.11055  ? 73  TYR A N     1 
ATOM   526  C  CA    . TYR A 1 73  ? 20.23600  -32.03400 34.82400  1.000 42.41035  ? 73  TYR A CA    1 
ATOM   527  C  C     . TYR A 1 73  ? 21.69200  -32.03400 35.26900  1.000 51.47459  ? 73  TYR A C     1 
ATOM   528  O  O     . TYR A 1 73  ? 22.27300  -33.08400 35.55500  1.000 54.07227  ? 73  TYR A O     1 
ATOM   529  C  CB    . TYR A 1 73  ? 19.33800  -31.72100 36.02600  1.000 41.75764  ? 73  TYR A CB    1 
ATOM   530  C  CG    . TYR A 1 73  ? 17.88500  -31.57200 35.66100  1.000 52.38786  ? 73  TYR A CG    1 
ATOM   531  C  CD1   . TYR A 1 73  ? 17.42600  -30.41900 35.03900  1.000 45.94498  ? 73  TYR A CD1   1 
ATOM   532  C  CD2   . TYR A 1 73  ? 16.97200  -32.58400 35.93100  1.000 52.31943  ? 73  TYR A CD2   1 
ATOM   533  C  CE1   . TYR A 1 73  ? 16.10700  -30.27400 34.70100  1.000 45.52125  ? 73  TYR A CE1   1 
ATOM   534  C  CE2   . TYR A 1 73  ? 15.64100  -32.44700 35.59200  1.000 60.74149  ? 73  TYR A CE2   1 
ATOM   535  C  CZ    . TYR A 1 73  ? 15.21400  -31.28800 34.97600  1.000 49.04009  ? 73  TYR A CZ    1 
ATOM   536  O  OH    . TYR A 1 73  ? 13.89200  -31.13800 34.62900  1.000 41.93134  ? 73  TYR A OH    1 
ATOM   537  N  N     . CYS A 1 74  ? 22.27300  -30.83200 35.32700  1.000 45.43966  ? 74  CYS A N     1 
ATOM   538  C  CA    . CYS A 1 74  ? 23.61500  -30.67900 35.88000  1.000 46.75824  ? 74  CYS A CA    1 
ATOM   539  C  C     . CYS A 1 74  ? 23.66900  -31.13200 37.33600  1.000 64.06031  ? 74  CYS A C     1 
ATOM   540  O  O     . CYS A 1 74  ? 24.61100  -31.82200 37.74200  1.000 69.04775  ? 74  CYS A O     1 
ATOM   541  C  CB    . CYS A 1 74  ? 24.07300  -29.22400 35.75900  1.000 48.01892  ? 74  CYS A CB    1 
ATOM   542  S  SG    . CYS A 1 74  ? 24.16200  -28.57300 34.07300  1.000 52.79054  ? 74  CYS A SG    1 
ATOM   543  N  N     . ASN A 1 75  ? 22.67100  -30.75600 38.13300  1.000 50.85610  ? 75  ASN A N     1 
ATOM   544  C  CA    . ASN A 1 75  ? 22.65900  -30.97000 39.58000  1.000 53.62485  ? 75  ASN A CA    1 
ATOM   545  C  C     . ASN A 1 75  ? 21.23600  -30.71700 40.07900  1.000 55.01975  ? 75  ASN A C     1 
ATOM   546  O  O     . ASN A 1 75  ? 20.32700  -30.45100 39.28500  1.000 56.39360  ? 75  ASN A O     1 
ATOM   547  C  CB    . ASN A 1 75  ? 23.68300  -30.06000 40.25400  1.000 56.72785  ? 75  ASN A CB    1 
ATOM   548  C  CG    . ASN A 1 75  ? 23.55900  -28.61900 39.79900  1.000 61.27840  ? 75  ASN A CG    1 
ATOM   549  O  OD1   . ASN A 1 75  ? 22.51100  -27.99700 39.96600  1.000 59.84139  ? 75  ASN A OD1   1 
ATOM   550  N  ND2   . ASN A 1 75  ? 24.61800  -28.09100 39.19100  1.000 59.68874  ? 75  ASN A ND2   1 
ATOM   551  N  N     . VAL A 1 76  ? 21.04200  -30.79200 41.40400  1.000 43.38941  ? 76  VAL A N     1 
ATOM   552  C  CA    . VAL A 1 76  ? 19.69800  -30.60300 41.95900  1.000 54.06964  ? 76  VAL A CA    1 
ATOM   553  C  C     . VAL A 1 76  ? 19.24600  -29.15100 41.82400  1.000 50.35341  ? 76  VAL A C     1 
ATOM   554  O  O     . VAL A 1 76  ? 18.03900  -28.87500 41.79200  1.000 52.85897  ? 76  VAL A O     1 
ATOM   555  C  CB    . VAL A 1 76  ? 19.59800  -31.08300 43.42400  1.000 56.60152  ? 76  VAL A CB    1 
ATOM   556  C  CG1   . VAL A 1 76  ? 20.03200  -32.51300 43.55000  1.000 56.34360  ? 76  VAL A CG1   1 
ATOM   557  C  CG2   . VAL A 1 76  ? 20.43900  -30.24700 44.33200  1.000 46.36609  ? 76  VAL A CG2   1 
ATOM   558  N  N     . GLU A 1 77  ? 20.18400  -28.19800 41.77600  1.000 49.33223  ? 77  GLU A N     1 
ATOM   559  C  CA    . GLU A 1 77  ? 19.78700  -26.80200 41.59600  1.000 69.22672  ? 77  GLU A CA    1 
ATOM   560  C  C     . GLU A 1 77  ? 19.14000  -26.59300 40.23100  1.000 52.80370  ? 77  GLU A C     1 
ATOM   561  O  O     . GLU A 1 77  ? 18.05000  -26.01700 40.12800  1.000 41.05229  ? 77  GLU A O     1 
ATOM   562  C  CB    . GLU A 1 77  ? 20.98700  -25.87200 41.77300  1.000 79.26477  ? 77  GLU A CB    1 
ATOM   563  C  CG    . GLU A 1 77  ? 20.59500  -24.41000 41.92400  1.000 85.53657  ? 77  GLU A CG    1 
ATOM   564  C  CD    . GLU A 1 77  ? 21.79200  -23.48500 41.94700  1.000 106.71279 ? 77  GLU A CD    1 
ATOM   565  O  OE1   . GLU A 1 77  ? 22.87000  -23.92000 42.40300  1.000 101.11476 ? 77  GLU A OE1   1 
ATOM   566  O  OE2   . GLU A 1 77  ? 21.66100  -22.32900 41.49200  1.000 132.20269 ? 77  GLU A OE2   1 
ATOM   567  N  N     . CYS A 1 78  ? 19.81500  -27.02900 39.16300  1.000 44.55008  ? 78  CYS A N     1 
ATOM   568  C  CA    . CYS A 1 78  ? 19.20500  -26.98100 37.83800  1.000 53.19585  ? 78  CYS A CA    1 
ATOM   569  C  C     . CYS A 1 78  ? 17.88900  -27.75000 37.81600  1.000 51.75357  ? 78  CYS A C     1 
ATOM   570  O  O     . CYS A 1 78  ? 16.90100  -27.29100 37.23100  1.000 47.96101  ? 78  CYS A O     1 
ATOM   571  C  CB    . CYS A 1 78  ? 20.17300  -27.53000 36.78900  1.000 47.33462  ? 78  CYS A CB    1 
ATOM   572  S  SG    . CYS A 1 78  ? 21.40700  -26.33700 36.19300  1.000 50.67713  ? 78  CYS A SG    1 
ATOM   573  N  N     . GLN A 1 79  ? 17.85000  -28.90900 38.47800  1.000 54.39336  ? 79  GLN A N     1 
ATOM   574  C  CA    . GLN A 1 79  ? 16.62600  -29.70300 38.54000  1.000 53.99068  ? 79  GLN A CA    1 
ATOM   575  C  C     . GLN A 1 79  ? 15.50400  -28.94300 39.23800  1.000 50.07706  ? 79  GLN A C     1 
ATOM   576  O  O     . GLN A 1 79  ? 14.35900  -28.93600 38.77100  1.000 44.34742  ? 79  GLN A O     1 
ATOM   577  C  CB    . GLN A 1 79  ? 16.90500  -31.02700 39.24700  1.000 55.30137  ? 79  GLN A CB    1 
ATOM   578  C  CG    . GLN A 1 79  ? 15.70100  -31.93500 39.37300  1.000 52.12467  ? 79  GLN A CG    1 
ATOM   579  C  CD    . GLN A 1 79  ? 16.07600  -33.29300 39.91100  1.000 55.60930  ? 79  GLN A CD    1 
ATOM   580  O  OE1   . GLN A 1 79  ? 17.22800  -33.52700 40.27700  1.000 58.09381  ? 79  GLN A OE1   1 
ATOM   581  N  NE2   . GLN A 1 79  ? 15.10300  -34.19300 39.98600  1.000 53.36956  ? 79  GLN A NE2   1 
ATOM   582  N  N     . LYS A 1 80  ? 15.81100  -28.30400 40.37000  1.000 49.39540  ? 80  LYS A N     1 
ATOM   583  C  CA    . LYS A 1 80  ? 14.78100  -27.58000 41.10800  1.000 55.96197  ? 80  LYS A CA    1 
ATOM   584  C  C     . LYS A 1 80  ? 14.30700  -26.34900 40.34200  1.000 43.72893  ? 80  LYS A C     1 
ATOM   585  O  O     . LYS A 1 80  ? 13.10800  -26.04500 40.32700  1.000 48.04523  ? 80  LYS A O     1 
ATOM   586  C  CB    . LYS A 1 80  ? 15.30600  -27.18100 42.48900  1.000 57.78324  ? 80  LYS A CB    1 
ATOM   587  C  CG    . LYS A 1 80  ? 14.34500  -26.31500 43.29400  1.000 75.02215  ? 80  LYS A CG    1 
ATOM   588  C  CD    . LYS A 1 80  ? 14.97900  -25.81100 44.58700  1.000 84.20220  ? 80  LYS A CD    1 
ATOM   589  C  CE    . LYS A 1 80  ? 15.28700  -26.95200 45.54800  1.000 87.36837  ? 80  LYS A CE    1 
ATOM   590  N  NZ    . LYS A 1 80  ? 15.92500  -26.47400 46.81100  1.000 100.57522 ? 80  LYS A NZ    1 
ATOM   591  N  N     . GLU A 1 81  ? 15.22800  -25.63500 39.69000  1.000 40.90754  ? 81  GLU A N     1 
ATOM   592  C  CA    . GLU A 1 81  ? 14.83900  -24.44900 38.93200  1.000 46.56348  ? 81  GLU A CA    1 
ATOM   593  C  C     . GLU A 1 81  ? 13.97700  -24.80300 37.72600  1.000 38.10194  ? 81  GLU A C     1 
ATOM   594  O  O     . GLU A 1 81  ? 13.14400  -23.99100 37.30500  1.000 39.23892  ? 81  GLU A O     1 
ATOM   595  C  CB    . GLU A 1 81  ? 16.08100  -23.66700 38.49600  1.000 54.84342  ? 81  GLU A CB    1 
ATOM   596  C  CG    . GLU A 1 81  ? 16.86500  -23.05500 39.65200  1.000 65.65261  ? 81  GLU A CG    1 
ATOM   597  C  CD    . GLU A 1 81  ? 16.06700  -22.01800 40.43100  1.000 53.19848  ? 81  GLU A CD    1 
ATOM   598  O  OE1   . GLU A 1 81  ? 15.43900  -21.14100 39.80000  1.000 61.34157  ? 81  GLU A OE1   1 
ATOM   599  O  OE2   . GLU A 1 81  ? 16.06200  -22.08400 41.67800  1.000 87.71315  ? 81  GLU A OE2   1 
ATOM   600  N  N     . ASP A 1 82  ? 14.16800  -25.99400 37.15200  1.000 39.68634  ? 82  ASP A N     1 
ATOM   601  C  CA    . ASP A 1 82  ? 13.38800  -26.42300 35.99700  1.000 36.67282  ? 82  ASP A CA    1 
ATOM   602  C  C     . ASP A 1 82  ? 12.03200  -27.01300 36.37000  1.000 43.52364  ? 82  ASP A C     1 
ATOM   603  O  O     . ASP A 1 82  ? 11.19400  -27.20300 35.47900  1.000 33.21451  ? 82  ASP A O     1 
ATOM   604  C  CB    . ASP A 1 82  ? 14.17500  -27.44700 35.18400  1.000 38.79676  ? 82  ASP A CB    1 
ATOM   605  C  CG    . ASP A 1 82  ? 13.58300  -27.67100 33.80700  1.000 49.09799  ? 82  ASP A CG    1 
ATOM   606  O  OD1   . ASP A 1 82  ? 13.28100  -26.66800 33.11900  1.000 33.36189  ? 82  ASP A OD1   1 
ATOM   607  O  OD2   . ASP A 1 82  ? 13.42300  -28.84600 33.41200  1.000 34.46992  ? 82  ASP A OD2   1 
ATOM   608  N  N     . TRP A 1 83  ? 11.81100  -27.32600 37.64900  1.000 35.66480  ? 83  TRP A N     1 
ATOM   609  C  CA    . TRP A 1 83  ? 10.57500  -27.97800 38.08100  1.000 39.51263  ? 83  TRP A CA    1 
ATOM   610  C  C     . TRP A 1 83  ? 9.29400   -27.26900 37.65600  1.000 37.54398  ? 83  TRP A C     1 
ATOM   611  O  O     . TRP A 1 83  ? 8.36900   -27.95800 37.19900  1.000 37.85454  ? 83  TRP A O     1 
ATOM   612  C  CB    . TRP A 1 83  ? 10.60200  -28.18800 39.60100  1.000 36.60965  ? 83  TRP A CB    1 
ATOM   613  C  CG    . TRP A 1 83  ? 9.39600   -28.92600 40.08800  1.000 38.35197  ? 83  TRP A CG    1 
ATOM   614  C  CD1   . TRP A 1 83  ? 8.46600   -28.46900 40.97700  1.000 37.11761  ? 83  TRP A CD1   1 
ATOM   615  C  CD2   . TRP A 1 83  ? 8.93100   -30.21300 39.64900  1.000 39.74424  ? 83  TRP A CD2   1 
ATOM   616  N  NE1   . TRP A 1 83  ? 7.48300   -29.41300 41.16200  1.000 44.95802  ? 83  TRP A NE1   1 
ATOM   617  C  CE2   . TRP A 1 83  ? 7.74000   -30.48900 40.35300  1.000 42.22612  ? 83  TRP A CE2   1 
ATOM   618  C  CE3   . TRP A 1 83  ? 9.41800   -31.16800 38.74800  1.000 38.42829  ? 83  TRP A CE3   1 
ATOM   619  C  CZ2   . TRP A 1 83  ? 7.03100   -31.67500 40.18200  1.000 38.10194  ? 83  TRP A CZ2   1 
ATOM   620  C  CZ3   . TRP A 1 83  ? 8.71200   -32.34600 38.58100  1.000 34.98314  ? 83  TRP A CZ3   1 
ATOM   621  C  CH2   . TRP A 1 83  ? 7.52900   -32.58500 39.28600  1.000 39.83372  ? 83  TRP A CH2   1 
ATOM   622  N  N     . PRO A 1 84  ? 9.14300   -25.94600 37.80000  1.000 41.19704  ? 84  PRO A N     1 
ATOM   623  C  CA    . PRO A 1 84  ? 7.86700   -25.33100 37.39700  1.000 41.54972  ? 84  PRO A CA    1 
ATOM   624  C  C     . PRO A 1 84  ? 7.49400   -25.60600 35.95200  1.000 33.03554  ? 84  PRO A C     1 
ATOM   625  O  O     . PRO A 1 84  ? 6.30000   -25.67100 35.64000  1.000 35.84377  ? 84  PRO A O     1 
ATOM   626  C  CB    . PRO A 1 84  ? 8.09900   -23.83500 37.65000  1.000 42.54721  ? 84  PRO A CB    1 
ATOM   627  C  CG    . PRO A 1 84  ? 9.15200   -23.79500 38.70000  1.000 40.39432  ? 84  PRO A CG    1 
ATOM   628  C  CD    . PRO A 1 84  ? 10.06000  -24.94500 38.38000  1.000 41.82870  ? 84  PRO A CD    1 
ATOM   629  N  N     . MET A 1 85  ? 8.47500   -25.78200 35.06400  1.000 32.89605  ? 85  MET A N     1 
ATOM   630  C  CA    . MET A 1 85  ? 8.20100   -26.12700 33.67100  1.000 34.92787  ? 85  MET A CA    1 
ATOM   631  C  C     . MET A 1 85  ? 8.15700   -27.63700 33.44600  1.000 33.91196  ? 85  MET A C     1 
ATOM   632  O  O     . MET A 1 85  ? 7.27400   -28.13700 32.73800  1.000 30.99319  ? 85  MET A O     1 
ATOM   633  C  CB    . MET A 1 85  ? 9.25700   -25.49100 32.76300  1.000 34.47782  ? 85  MET A CB    1 
ATOM   634  C  CG    . MET A 1 85  ? 9.26400   -23.96400 32.80600  1.000 37.99403  ? 85  MET A CG    1 
ATOM   635  S  SD    . MET A 1 85  ? 7.71900   -23.24500 32.20700  1.000 36.96759  ? 85  MET A SD    1 
ATOM   636  C  CE    . MET A 1 85  ? 7.26500   -22.16900 33.56800  1.000 55.42243  ? 85  MET A CE    1 
ATOM   637  N  N     . HIS A 1 86  ? 9.07800   -28.37500 34.07100  1.000 32.34335  ? 86  HIS A N     1 
ATOM   638  C  CA    . HIS A 1 86  ? 9.15800   -29.81500 33.85400  1.000 35.41477  ? 86  HIS A CA    1 
ATOM   639  C  C     . HIS A 1 86  ? 7.90300   -30.54800 34.32100  1.000 38.69411  ? 86  HIS A C     1 
ATOM   640  O  O     . HIS A 1 86  ? 7.53500   -31.57200 33.73400  1.000 35.49636  ? 86  HIS A O     1 
ATOM   641  C  CB    . HIS A 1 86  ? 10.39300  -30.37100 34.56100  1.000 35.80166  ? 86  HIS A CB    1 
ATOM   642  C  CG    . HIS A 1 86  ? 10.55800  -31.84900 34.41000  1.000 37.25183  ? 86  HIS A CG    1 
ATOM   643  N  ND1   . HIS A 1 86  ? 10.53800  -32.47900 33.18300  1.000 31.53273  ? 86  HIS A ND1   1 
ATOM   644  C  CD2   . HIS A 1 86  ? 10.73100  -32.82400 35.33300  1.000 38.95993  ? 86  HIS A CD2   1 
ATOM   645  C  CE1   . HIS A 1 86  ? 10.69400  -33.77800 33.35800  1.000 32.98817  ? 86  HIS A CE1   1 
ATOM   646  N  NE2   . HIS A 1 86  ? 10.81600  -34.01400 34.65200  1.000 43.72630  ? 86  HIS A NE2   1 
ATOM   647  N  N     . LYS A 1 87  ? 7.23800   -30.05700 35.37300  1.000 31.87751  ? 87  LYS A N     1 
ATOM   648  C  CA    . LYS A 1 87  ? 6.05500   -30.74600 35.88600  1.000 34.04882  ? 87  LYS A CA    1 
ATOM   649  C  C     . LYS A 1 87  ? 4.89900   -30.77100 34.88700  1.000 32.08016  ? 87  LYS A C     1 
ATOM   650  O  O     . LYS A 1 87  ? 3.93000   -31.51400 35.09300  1.000 32.10911  ? 87  LYS A O     1 
ATOM   651  C  CB    . LYS A 1 87  ? 5.60500   -30.12900 37.21000  1.000 36.24382  ? 87  LYS A CB    1 
ATOM   652  C  CG    . LYS A 1 87  ? 5.06400   -28.71700 37.15100  1.000 39.56001  ? 87  LYS A CG    1 
ATOM   653  C  CD    . LYS A 1 87  ? 4.61700   -28.30400 38.55200  1.000 53.15637  ? 87  LYS A CD    1 
ATOM   654  C  CE    . LYS A 1 87  ? 4.09000   -26.88300 38.60100  1.000 62.54960  ? 87  LYS A CE    1 
ATOM   655  N  NZ    . LYS A 1 87  ? 3.72300   -26.49100 39.99100  1.000 63.20758  ? 87  LYS A NZ    1 
ATOM   656  N  N     . LEU A 1 88  ? 4.95000   -29.94900 33.83900  1.000 37.06497  ? 88  LEU A N     1 
ATOM   657  C  CA    . LEU A 1 88  ? 3.95100   -30.04200 32.78300  1.000 34.47519  ? 88  LEU A CA    1 
ATOM   658  C  C     . LEU A 1 88  ? 4.04100   -31.36300 32.02900  1.000 34.05145  ? 88  LEU A C     1 
ATOM   659  O  O     . LEU A 1 88  ? 3.04600   -31.80500 31.44600  1.000 41.91818  ? 88  LEU A O     1 
ATOM   660  C  CB    . LEU A 1 88  ? 4.11800   -28.88300 31.79600  1.000 35.73850  ? 88  LEU A CB    1 
ATOM   661  C  CG    . LEU A 1 88  ? 4.11900   -27.45300 32.33700  1.000 39.07837  ? 88  LEU A CG    1 
ATOM   662  C  CD1   . LEU A 1 88  ? 4.38900   -26.45900 31.21300  1.000 41.89186  ? 88  LEU A CD1   1 
ATOM   663  C  CD2   . LEU A 1 88  ? 2.81900   -27.13000 33.03800  1.000 41.32601  ? 88  LEU A CD2   1 
ATOM   664  N  N     . GLU A 1 89  ? 5.21000   -32.00500 32.04000  1.000 30.39575  ? 89  GLU A N     1 
ATOM   665  C  CA    . GLU A 1 89  ? 5.46100   -33.19500 31.24300  1.000 33.80668  ? 89  GLU A CA    1 
ATOM   666  C  C     . GLU A 1 89  ? 5.91900   -34.40000 32.04600  1.000 41.01544  ? 89  GLU A C     1 
ATOM   667  O  O     . GLU A 1 89  ? 5.76800   -35.52700 31.56300  1.000 40.89438  ? 89  GLU A O     1 
ATOM   668  C  CB    . GLU A 1 89  ? 6.52100   -32.89700 30.17200  1.000 30.41680  ? 89  GLU A CB    1 
ATOM   669  C  CG    . GLU A 1 89  ? 6.11600   -31.77800 29.23000  1.000 34.20147  ? 89  GLU A CG    1 
ATOM   670  C  CD    . GLU A 1 89  ? 7.17300   -31.45400 28.19000  1.000 32.50653  ? 89  GLU A CD    1 
ATOM   671  O  OE1   . GLU A 1 89  ? 8.37200   -31.67500 28.45700  1.000 29.29299  ? 89  GLU A OE1   1 
ATOM   672  O  OE2   . GLU A 1 89  ? 6.79400   -30.97100 27.10200  1.000 29.04822  ? 89  GLU A OE2   1 
ATOM   673  N  N     . CYS A 1 90  ? 6.48100   -34.19700 33.24300  1.000 39.42578  ? 90  CYS A N     1 
ATOM   674  C  CA    . CYS A 1 90  ? 7.08900   -35.28400 34.00200  1.000 36.87811  ? 90  CYS A CA    1 
ATOM   675  C  C     . CYS A 1 90  ? 6.14100   -36.47000 34.14200  1.000 38.15721  ? 90  CYS A C     1 
ATOM   676  O  O     . CYS A 1 90  ? 6.39100   -37.55500 33.60500  1.000 40.18640  ? 90  CYS A O     1 
ATOM   677  C  CB    . CYS A 1 90  ? 7.53200   -34.77300 35.37700  1.000 44.34216  ? 90  CYS A CB    1 
ATOM   678  S  SG    . CYS A 1 90  ? 8.47100   -35.98500 36.33700  1.000 41.51550  ? 90  CYS A SG    1 
ATOM   679  N  N     . SER A 1 91  ? 5.03600   -36.27900 34.86700  1.000 38.42303  ? 91  SER A N     1 
ATOM   680  C  CA    . SER A 1 91  ? 4.09000   -37.37300 35.05000  1.000 37.89928  ? 91  SER A CA    1 
ATOM   681  C  C     . SER A 1 91  ? 3.37800   -37.76700 33.75200  1.000 40.95491  ? 91  SER A C     1 
ATOM   682  O  O     . SER A 1 91  ? 3.28800   -38.97000 33.47100  1.000 37.01496  ? 91  SER A O     1 
ATOM   683  C  CB    . SER A 1 91  ? 3.09200   -37.02200 36.15400  1.000 38.25722  ? 91  SER A CB    1 
ATOM   684  O  OG    . SER A 1 91  ? 2.21700   -38.10600 36.40300  1.000 44.00264  ? 91  SER A OG    1 
ATOM   685  N  N     . PRO A 1 92  ? 2.84700   -36.83100 32.94400  1.000 33.89880  ? 92  PRO A N     1 
ATOM   686  C  CA    . PRO A 1 92  ? 2.23100   -37.25200 31.66500  1.000 37.40975  ? 92  PRO A CA    1 
ATOM   687  C  C     . PRO A 1 92  ? 3.11200   -38.13900 30.79800  1.000 38.65463  ? 92  PRO A C     1 
ATOM   688  O  O     . PRO A 1 92  ? 2.59300   -39.04800 30.13800  1.000 33.23556  ? 92  PRO A O     1 
ATOM   689  C  CB    . PRO A 1 92  ? 1.92300   -35.91300 30.97700  1.000 35.94642  ? 92  PRO A CB    1 
ATOM   690  C  CG    . PRO A 1 92  ? 1.67600   -34.97700 32.11300  1.000 39.13101  ? 92  PRO A CG    1 
ATOM   691  C  CD    . PRO A 1 92  ? 2.64100   -35.39200 33.19500  1.000 36.09380  ? 92  PRO A CD    1 
ATOM   692  N  N     . MET A 1 93  ? 4.42800   -37.90500 30.78300  1.000 39.63633  ? 93  MET A N     1 
ATOM   693  C  CA    . MET A 1 93  ? 5.31600   -38.72500 29.96200  1.000 43.41573  ? 93  MET A CA    1 
ATOM   694  C  C     . MET A 1 93  ? 5.27100   -40.19000 30.37800  1.000 38.95730  ? 93  MET A C     1 
ATOM   695  O  O     . MET A 1 93  ? 5.27100   -41.08300 29.52400  1.000 52.65631  ? 93  MET A O     1 
ATOM   696  C  CB    . MET A 1 93  ? 6.75100   -38.19900 30.03500  1.000 39.00731  ? 93  MET A CB    1 
ATOM   697  C  CG    . MET A 1 93  ? 7.02600   -37.03400 29.11500  1.000 41.48392  ? 93  MET A CG    1 
ATOM   698  S  SD    . MET A 1 93  ? 8.78800   -36.76600 28.84900  1.000 42.14453  ? 93  MET A SD    1 
ATOM   699  C  CE    . MET A 1 93  ? 9.31500   -36.22700 30.47400  1.000 49.18221  ? 93  MET A CE    1 
ATOM   700  N  N     . VAL A 1 94  ? 5.24300   -40.46400 31.68300  1.000 42.42088  ? 94  VAL A N     1 
ATOM   701  C  CA    . VAL A 1 94  ? 5.17900   -41.85200 32.12900  1.000 54.69866  ? 94  VAL A CA    1 
ATOM   702  C  C     . VAL A 1 94  ? 3.77500   -42.41700 31.95800  1.000 48.10840  ? 94  VAL A C     1 
ATOM   703  O  O     . VAL A 1 94  ? 3.60400   -43.57400 31.55700  1.000 59.30974  ? 94  VAL A O     1 
ATOM   704  C  CB    . VAL A 1 94  ? 5.64500   -41.96800 33.59100  1.000 57.86483  ? 94  VAL A CB    1 
ATOM   705  C  CG1   . VAL A 1 94  ? 5.99700   -43.41000 33.91000  1.000 65.12623  ? 94  VAL A CG1   1 
ATOM   706  C  CG2   . VAL A 1 94  ? 6.81900   -41.04700 33.85800  1.000 54.33546  ? 94  VAL A CG2   1 
ATOM   707  N  N     . VAL A 1 95  ? 2.75300   -41.60900 32.24300  1.000 49.14010  ? 95  VAL A N     1 
ATOM   708  C  CA    . VAL A 1 95  ? 1.37400   -42.08700 32.20000  1.000 47.40305  ? 95  VAL A CA    1 
ATOM   709  C  C     . VAL A 1 95  ? 0.92600   -42.32900 30.76100  1.000 41.55235  ? 95  VAL A C     1 
ATOM   710  O  O     . VAL A 1 95  ? 0.30400   -43.35200 30.45700  1.000 47.39252  ? 95  VAL A O     1 
ATOM   711  C  CB    . VAL A 1 95  ? 0.45700   -41.09700 32.94000  1.000 45.37913  ? 95  VAL A CB    1 
ATOM   712  C  CG1   . VAL A 1 95  ? -0.99300  -41.50400 32.79300  1.000 50.90610  ? 95  VAL A CG1   1 
ATOM   713  C  CG2   . VAL A 1 95  ? 0.84200   -41.04500 34.41400  1.000 50.37972  ? 95  VAL A CG2   1 
ATOM   714  N  N     . PHE A 1 96  ? 1.23300   -41.39900 29.85100  1.000 35.83588  ? 96  PHE A N     1 
ATOM   715  C  CA    . PHE A 1 96  ? 0.90300   -41.62200 28.44500  1.000 34.81470  ? 96  PHE A CA    1 
ATOM   716  C  C     . PHE A 1 96  ? 1.85000   -42.62600 27.79600  1.000 36.55701  ? 96  PHE A C     1 
ATOM   717  O  O     . PHE A 1 96  ? 1.46700   -43.30000 26.83300  1.000 50.46658  ? 96  PHE A O     1 
ATOM   718  C  CB    . PHE A 1 96  ? 0.91700   -40.30200 27.67100  1.000 34.81207  ? 96  PHE A CB    1 
ATOM   719  C  CG    . PHE A 1 96  ? -0.34500  -39.49200 27.81900  1.000 39.55737  ? 96  PHE A CG    1 
ATOM   720  C  CD1   . PHE A 1 96  ? -1.49800  -39.85700 27.13600  1.000 39.95742  ? 96  PHE A CD1   1 
ATOM   721  C  CD2   . PHE A 1 96  ? -0.37900  -38.36700 28.63100  1.000 37.62293  ? 96  PHE A CD2   1 
ATOM   722  C  CE1   . PHE A 1 96  ? -2.66000  -39.11600 27.26000  1.000 38.77570  ? 96  PHE A CE1   1 
ATOM   723  C  CE2   . PHE A 1 96  ? -1.54000  -37.62100 28.76300  1.000 37.84927  ? 96  PHE A CE2   1 
ATOM   724  C  CZ    . PHE A 1 96  ? -2.68300  -37.99500 28.07500  1.000 39.32050  ? 96  PHE A CZ    1 
ATOM   725  N  N     . GLY A 1 97  ? 3.07900   -42.73200 28.29700  1.000 44.63430  ? 97  GLY A N     1 
ATOM   726  C  CA    . GLY A 1 97  ? 4.02400   -43.71400 27.80500  1.000 49.25854  ? 97  GLY A CA    1 
ATOM   727  C  C     . GLY A 1 97  ? 4.44600   -43.49700 26.36900  1.000 44.15266  ? 97  GLY A C     1 
ATOM   728  O  O     . GLY A 1 97  ? 4.93300   -42.42100 26.01000  1.000 43.03937  ? 97  GLY A O     1 
ATOM   729  N  N     . GLU A 1 98  ? 4.26000   -44.52200 25.53500  1.000 60.87046  ? 98  GLU A N     1 
ATOM   730  C  CA    . GLU A 1 98  ? 4.63200   -44.42000 24.12800  1.000 65.06833  ? 98  GLU A CA    1 
ATOM   731  C  C     . GLU A 1 98  ? 3.73800   -43.44300 23.37600  1.000 50.59291  ? 98  GLU A C     1 
ATOM   732  O  O     . GLU A 1 98  ? 4.15900   -42.87400 22.36300  1.000 59.89929  ? 98  GLU A O     1 
ATOM   733  C  CB    . GLU A 1 98  ? 4.56600   -45.79900 23.47700  1.000 73.89833  ? 98  GLU A CB    1 
ATOM   734  C  CG    . GLU A 1 98  ? 5.53200   -46.80600 24.06700  1.000 84.48645  ? 98  GLU A CG    1 
ATOM   735  C  CD    . GLU A 1 98  ? 5.57000   -48.09300 23.27400  1.000 110.47904 ? 98  GLU A CD    1 
ATOM   736  O  OE1   . GLU A 1 98  ? 4.61800   -48.33400 22.50000  1.000 113.12409 ? 98  GLU A OE1   1 
ATOM   737  O  OE2   . GLU A 1 98  ? 6.54100   -48.86400 23.42800  1.000 104.05985 ? 98  GLU A OE2   1 
ATOM   738  N  N     . ASN A 1 99  ? 2.51100   -43.23600 23.85000  1.000 51.13245  ? 99  ASN A N     1 
ATOM   739  C  CA    . ASN A 1 99  ? 1.55500   -42.35500 23.19400  1.000 40.36537  ? 99  ASN A CA    1 
ATOM   740  C  C     . ASN A 1 99  ? 1.79400   -40.87400 23.47200  1.000 37.49397  ? 99  ASN A C     1 
ATOM   741  O  O     . ASN A 1 99  ? 1.03100   -40.04200 22.97000  1.000 40.60224  ? 99  ASN A O     1 
ATOM   742  C  CB    . ASN A 1 99  ? 0.13400   -42.73700 23.60800  1.000 46.50558  ? 99  ASN A CB    1 
ATOM   743  C  CG    . ASN A 1 99  ? -0.23900  -44.14000 23.16800  1.000 59.02550  ? 99  ASN A CG    1 
ATOM   744  O  OD1   . ASN A 1 99  ? -0.50200  -45.01500 23.99500  1.000 66.43428  ? 99  ASN A OD1   1 
ATOM   745  N  ND2   . ASN A 1 99  ? -0.25200  -44.36500 21.85700  1.000 48.06629  ? 99  ASN A ND2   1 
ATOM   746  N  N     . TRP A 1 100 ? 2.81100   -40.52000 24.25800  1.000 41.32601  ? 100 TRP A N     1 
ATOM   747  C  CA    . TRP A 1 100 ? 3.14600   -39.11900 24.50400  1.000 38.62568  ? 100 TRP A CA    1 
ATOM   748  C  C     . TRP A 1 100 ? 3.95300   -38.59100 23.32700  1.000 37.81769  ? 100 TRP A C     1 
ATOM   749  O  O     . TRP A 1 100 ? 5.13700   -38.91900 23.18400  1.000 45.15278  ? 100 TRP A O     1 
ATOM   750  C  CB    . TRP A 1 100 ? 3.92900   -38.96900 25.80700  1.000 38.66779  ? 100 TRP A CB    1 
ATOM   751  C  CG    . TRP A 1 100 ? 4.07100   -37.53800 26.26800  1.000 41.73395  ? 100 TRP A CG    1 
ATOM   752  C  CD1   . TRP A 1 100 ? 3.18200   -36.82900 27.02800  1.000 37.05971  ? 100 TRP A CD1   1 
ATOM   753  C  CD2   . TRP A 1 100 ? 5.16700   -36.64900 26.00300  1.000 40.36537  ? 100 TRP A CD2   1 
ATOM   754  N  NE1   . TRP A 1 100 ? 3.65500   -35.55700 27.25000  1.000 43.23676  ? 100 TRP A NE1   1 
ATOM   755  C  CE2   . TRP A 1 100 ? 4.86900   -35.41900 26.63100  1.000 40.81016  ? 100 TRP A CE2   1 
ATOM   756  C  CE3   . TRP A 1 100 ? 6.37000   -36.77200 25.29700  1.000 37.52818  ? 100 TRP A CE3   1 
ATOM   757  C  CZ2   . TRP A 1 100 ? 5.73000   -34.32000 26.57200  1.000 52.62736  ? 100 TRP A CZ2   1 
ATOM   758  C  CZ3   . TRP A 1 100 ? 7.22400   -35.67600 25.23800  1.000 40.02585  ? 100 TRP A CZ3   1 
ATOM   759  C  CH2   . TRP A 1 100 ? 6.89900   -34.46900 25.87300  1.000 47.18460  ? 100 TRP A CH2   1 
ATOM   760  N  N     . ASN A 1 101 ? 3.32800   -37.75500 22.49200  1.000 40.16271  ? 101 ASN A N     1 
ATOM   761  C  CA    . ASN A 1 101 ? 4.02100   -37.21300 21.32400  1.000 42.77881  ? 101 ASN A CA    1 
ATOM   762  C  C     . ASN A 1 101 ? 3.54100   -35.81700 20.92700  1.000 34.91471  ? 101 ASN A C     1 
ATOM   763  O  O     . ASN A 1 101 ? 3.21700   -35.59100 19.75300  1.000 44.10792  ? 101 ASN A O     1 
ATOM   764  C  CB    . ASN A 1 101 ? 3.86700   -38.16900 20.13500  1.000 41.83396  ? 101 ASN A CB    1 
ATOM   765  C  CG    . ASN A 1 101 ? 2.42000   -38.33600 19.69300  1.000 47.45306  ? 101 ASN A CG    1 
ATOM   766  O  OD1   . ASN A 1 101 ? 1.48800   -38.03700 20.44100  1.000 48.81112  ? 101 ASN A OD1   1 
ATOM   767  N  ND2   . ASN A 1 101 ? 2.22900   -38.80300 18.46400  1.000 61.25471  ? 101 ASN A ND2   1 
ATOM   768  N  N     . PRO A 1 102 ? 3.49500   -34.84700 21.84400  1.000 33.49349  ? 102 PRO A N     1 
ATOM   769  C  CA    . PRO A 1 102 ? 3.17700   -33.47700 21.42100  1.000 30.58525  ? 102 PRO A CA    1 
ATOM   770  C  C     . PRO A 1 102 ? 4.32500   -32.90600 20.60100  1.000 26.94007  ? 102 PRO A C     1 
ATOM   771  O  O     . PRO A 1 102 ? 5.49800   -33.14100 20.90500  1.000 28.47973  ? 102 PRO A O     1 
ATOM   772  C  CB    . PRO A 1 102 ? 3.00800   -32.72500 22.74700  1.000 30.75632  ? 102 PRO A CB    1 
ATOM   773  C  CG    . PRO A 1 102 ? 3.92100   -33.45100 23.68400  1.000 29.09823  ? 102 PRO A CG    1 
ATOM   774  C  CD    . PRO A 1 102 ? 3.83300   -34.90400 23.28200  1.000 30.57209  ? 102 PRO A CD    1 
ATOM   775  N  N     . SER A 1 103 ? 3.98200   -32.17100 19.54200  1.000 28.98505  ? 103 SER A N     1 
ATOM   776  C  CA    . SER A 1 103 ? 5.00500   -31.50900 18.74200  1.000 27.94546  ? 103 SER A CA    1 
ATOM   777  C  C     . SER A 1 103 ? 5.76400   -30.48300 19.58000  1.000 31.63537  ? 103 SER A C     1 
ATOM   778  O  O     . SER A 1 103 ? 5.29300   -30.01600 20.62600  1.000 28.90873  ? 103 SER A O     1 
ATOM   779  C  CB    . SER A 1 103 ? 4.39200   -30.81300 17.53000  1.000 32.86447  ? 103 SER A CB    1 
ATOM   780  O  OG    . SER A 1 103 ? 3.73400   -29.62000 17.91100  1.000 37.45975  ? 103 SER A OG    1 
ATOM   781  N  N     . GLU A 1 104 ? 6.95400   -30.11700 19.09700  1.000 31.01424  ? 104 GLU A N     1 
ATOM   782  C  CA    . GLU A 1 104 ? 7.79000   -29.17700 19.83600  1.000 32.82762  ? 104 GLU A CA    1 
ATOM   783  C  C     . GLU A 1 104 ? 7.10500   -27.82200 19.99000  1.000 31.66432  ? 104 GLU A C     1 
ATOM   784  O  O     . GLU A 1 104 ? 7.26400   -27.15500 21.01800  1.000 25.29514  ? 104 GLU A O     1 
ATOM   785  C  CB    . GLU A 1 104 ? 9.14400   -29.02700 19.14700  1.000 30.75895  ? 104 GLU A CB    1 
ATOM   786  C  CG    . GLU A 1 104 ? 10.17500  -28.30800 19.99300  1.000 33.63298  ? 104 GLU A CG    1 
ATOM   787  C  CD    . GLU A 1 104 ? 11.59700  -28.72400 19.65100  1.000 36.79125  ? 104 GLU A CD    1 
ATOM   788  O  OE1   . GLU A 1 104 ? 11.88100  -29.94000 19.64900  1.000 32.05384  ? 104 GLU A OE1   1 
ATOM   789  O  OE2   . GLU A 1 104 ? 12.42700  -27.83300 19.37800  1.000 29.38247  ? 104 GLU A OE2   1 
ATOM   790  N  N     . THR A 1 105 ? 6.35000   -27.39300 18.97100  1.000 23.82128  ? 105 THR A N     1 
ATOM   791  C  CA    . THR A 1 105 ? 5.57800   -26.15600 19.07400  1.000 32.03805  ? 105 THR A CA    1 
ATOM   792  C  C     . THR A 1 105 ? 4.57700   -26.21600 20.22200  1.000 27.43224  ? 105 THR A C     1 
ATOM   793  O  O     . THR A 1 105 ? 4.42600   -25.24800 20.98100  1.000 24.20817  ? 105 THR A O     1 
ATOM   794  C  CB    . THR A 1 105 ? 4.85500   -25.87700 17.75200  1.000 36.48069  ? 105 THR A CB    1 
ATOM   795  O  OG1   . THR A 1 105 ? 5.82100   -25.71000 16.70500  1.000 41.07071  ? 105 THR A OG1   1 
ATOM   796  C  CG2   . THR A 1 105 ? 3.99000   -24.62700 17.86000  1.000 39.84162  ? 105 THR A CG2   1 
ATOM   797  N  N     . VAL A 1 106 ? 3.88600   -27.34700 20.36400  1.000 24.56084  ? 106 VAL A N     1 
ATOM   798  C  CA    . VAL A 1 106 ? 2.94200   -27.52600 21.46500  1.000 25.76888  ? 106 VAL A CA    1 
ATOM   799  C  C     . VAL A 1 106 ? 3.67700   -27.47300 22.80200  1.000 24.34766  ? 106 VAL A C     1 
ATOM   800  O  O     . VAL A 1 106 ? 3.24700   -26.79300 23.74000  1.000 28.74292  ? 106 VAL A O     1 
ATOM   801  C  CB    . VAL A 1 106 ? 2.17300   -28.84800 21.28400  1.000 25.47148  ? 106 VAL A CB    1 
ATOM   802  C  CG1   . VAL A 1 106 ? 1.28600   -29.14300 22.49000  1.000 27.45329  ? 106 VAL A CG1   1 
ATOM   803  C  CG2   . VAL A 1 106 ? 1.36000   -28.81300 19.99700  1.000 31.10373  ? 106 VAL A CG2   1 
ATOM   804  N  N     . ARG A 1 107 ? 4.80400   -28.18900 22.90100  1.000 28.16127  ? 107 ARG A N     1 
ATOM   805  C  CA    . ARG A 1 107 ? 5.60100   -28.18600 24.12800  1.000 28.12969  ? 107 ARG A CA    1 
ATOM   806  C  C     . ARG A 1 107 ? 6.00600   -26.77000 24.52900  1.000 23.63968  ? 107 ARG A C     1 
ATOM   807  O  O     . ARG A 1 107 ? 5.93600   -26.40700 25.70800  1.000 25.06090  ? 107 ARG A O     1 
ATOM   808  C  CB    . ARG A 1 107 ? 6.84500   -29.05400 23.94400  1.000 31.33534  ? 107 ARG A CB    1 
ATOM   809  C  CG    . ARG A 1 107 ? 6.56800   -30.52600 23.67300  1.000 33.19609  ? 107 ARG A CG    1 
ATOM   810  C  CD    . ARG A 1 107 ? 7.88200   -31.29700 23.59900  1.000 30.86949  ? 107 ARG A CD    1 
ATOM   811  N  NE    . ARG A 1 107 ? 8.52400   -31.34600 24.90600  1.000 31.38797  ? 107 ARG A NE    1 
ATOM   812  C  CZ    . ARG A 1 107 ? 9.83400   -31.43800 25.10300  1.000 34.98841  ? 107 ARG A CZ    1 
ATOM   813  N  NH1   . ARG A 1 107 ? 10.66900  -31.47100 24.06900  1.000 32.04332  ? 107 ARG A NH1   1 
ATOM   814  N  NH2   . ARG A 1 107 ? 10.31200  -31.46500 26.34300  1.000 35.24896  ? 107 ARG A NH2   1 
ATOM   815  N  N     . LEU A 1 108 ? 6.43100   -25.95800 23.56000  1.000 23.71863  ? 108 LEU A N     1 
ATOM   816  C  CA    . LEU A 1 108 ? 6.84800   -24.58600 23.84700  1.000 24.48451  ? 108 LEU A CA    1 
ATOM   817  C  C     . LEU A 1 108 ? 5.66400   -23.72000 24.26900  1.000 24.75297  ? 108 LEU A C     1 
ATOM   818  O  O     . LEU A 1 108 ? 5.77200   -22.91300 25.20100  1.000 21.54732  ? 108 LEU A O     1 
ATOM   819  C  CB    . LEU A 1 108 ? 7.55600   -23.98600 22.62300  1.000 21.10253  ? 108 LEU A CB    1 
ATOM   820  C  CG    . LEU A 1 108 ? 8.10600   -22.55600 22.74700  1.000 24.71612  ? 108 LEU A CG    1 
ATOM   821  C  CD1   . LEU A 1 108 ? 9.07500   -22.42500 23.91500  1.000 23.70547  ? 108 LEU A CD1   1 
ATOM   822  C  CD2   . LEU A 1 108 ? 8.76000   -22.07500 21.44000  1.000 24.41345  ? 108 LEU A CD2   1 
ATOM   823  N  N     . THR A 1 109 ? 4.54000   -23.84000 23.55600  1.000 26.95586  ? 109 THR A N     1 
ATOM   824  C  CA    . THR A 1 109 ? 3.36200   -23.03500 23.87100  1.000 25.37673  ? 109 THR A CA    1 
ATOM   825  C  C     . THR A 1 109 ? 2.82300   -23.35800 25.26100  1.000 23.84760  ? 109 THR A C     1 
ATOM   826  O  O     . THR A 1 109 ? 2.36700   -22.46400 25.98400  1.000 25.64255  ? 109 THR A O     1 
ATOM   827  C  CB    . THR A 1 109 ? 2.28600   -23.25500 22.80500  1.000 24.27133  ? 109 THR A CB    1 
ATOM   828  O  OG1   . THR A 1 109 ? 2.80600   -22.88000 21.52200  1.000 26.77689  ? 109 THR A OG1   1 
ATOM   829  C  CG2   . THR A 1 109 ? 1.05000   -22.42900 23.10900  1.000 30.74842  ? 109 THR A CG2   1 
ATOM   830  N  N     . ALA A 1 110 ? 2.86400   -24.63500 25.64900  1.000 21.23412  ? 110 ALA A N     1 
ATOM   831  C  CA    . ALA A 1 110 ? 2.48100   -25.01400 27.00500  1.000 26.10576  ? 110 ALA A CA    1 
ATOM   832  C  C     . ALA A 1 110 ? 3.32600   -24.28000 28.03800  1.000 24.48188  ? 110 ALA A C     1 
ATOM   833  O  O     . ALA A 1 110 ? 2.80000   -23.77500 29.03500  1.000 28.13495  ? 110 ALA A O     1 
ATOM   834  C  CB    . ALA A 1 110 ? 2.61000   -26.52600 27.18000  1.000 24.42924  ? 110 ALA A CB    1 
ATOM   835  N  N     . ARG A 1 111 ? 4.63800   -24.18900 27.80100  1.000 27.47961  ? 111 ARG A N     1 
ATOM   836  C  CA    . ARG A 1 111 ? 5.51700   -23.49100 28.73600  1.000 29.56670  ? 111 ARG A CA    1 
ATOM   837  C  C     . ARG A 1 111 ? 5.28100   -21.98700 28.71900  1.000 29.85358  ? 111 ARG A C     1 
ATOM   838  O  O     . ARG A 1 111 ? 5.45400   -21.32600 29.75100  1.000 26.41633  ? 111 ARG A O     1 
ATOM   839  C  CB    . ARG A 1 111 ? 6.98100   -23.81000 28.42300  1.000 30.45365  ? 111 ARG A CB    1 
ATOM   840  C  CG    . ARG A 1 111 ? 7.37500   -25.19700 28.88300  1.000 33.55665  ? 111 ARG A CG    1 
ATOM   841  C  CD    . ARG A 1 111 ? 8.77300   -25.59800 28.47400  1.000 32.76709  ? 111 ARG A CD    1 
ATOM   842  N  NE    . ARG A 1 111 ? 8.94900   -27.04000 28.64300  1.000 38.32565  ? 111 ARG A NE    1 
ATOM   843  C  CZ    . ARG A 1 111 ? 9.86800   -27.60500 29.42100  1.000 46.96879  ? 111 ARG A CZ    1 
ATOM   844  N  NH1   . ARG A 1 111 ? 10.72400  -26.85200 30.10200  1.000 46.72666  ? 111 ARG A NH1   1 
ATOM   845  N  NH2   . ARG A 1 111 ? 9.94000   -28.92900 29.50900  1.000 41.20231  ? 111 ARG A NH2   1 
ATOM   846  N  N     . ILE A 1 112 ? 4.86800   -21.43100 27.57400  1.000 25.47411  ? 112 ILE A N     1 
ATOM   847  C  CA    . ILE A 1 112 ? 4.48900   -20.02100 27.53700  1.000 24.60295  ? 112 ILE A CA    1 
ATOM   848  C  C     . ILE A 1 112 ? 3.29300   -19.77300 28.44800  1.000 27.37170  ? 112 ILE A C     1 
ATOM   849  O  O     . ILE A 1 112 ? 3.29600   -18.85300 29.27600  1.000 28.63501  ? 112 ILE A O     1 
ATOM   850  C  CB    . ILE A 1 112 ? 4.19100   -19.57300 26.09600  1.000 23.16857  ? 112 ILE A CB    1 
ATOM   851  C  CG1   . ILE A 1 112 ? 5.46100   -19.61600 25.24800  1.000 26.77163  ? 112 ILE A CG1   1 
ATOM   852  C  CG2   . ILE A 1 112 ? 3.61800   -18.17500 26.09400  1.000 23.80549  ? 112 ILE A CG2   1 
ATOM   853  C  CD1   . ILE A 1 112 ? 5.18000   -19.44700 23.75300  1.000 26.06365  ? 112 ILE A CD1   1 
ATOM   854  N  N     . LEU A 1 113 ? 2.24800   -20.59200 28.30200  1.000 21.83946  ? 113 LEU A N     1 
ATOM   855  C  CA    . LEU A 1 113 ? 1.05700   -20.43400 29.13000  1.000 21.78682  ? 113 LEU A CA    1 
ATOM   856  C  C     . LEU A 1 113 ? 1.38600   -20.57100 30.61200  1.000 23.23173  ? 113 LEU A C     1 
ATOM   857  O  O     . LEU A 1 113 ? 0.86400   -19.81900 31.44500  1.000 25.12143  ? 113 LEU A O     1 
ATOM   858  C  CB    . LEU A 1 113 ? -0.00200  -21.45300 28.70800  1.000 22.88169  ? 113 LEU A CB    1 
ATOM   859  C  CG    . LEU A 1 113 ? -0.60800  -21.17800 27.32700  1.000 23.09751  ? 113 LEU A CG    1 
ATOM   860  C  CD1   . LEU A 1 113 ? -1.38100  -22.38100 26.80700  1.000 25.26619  ? 113 LEU A CD1   1 
ATOM   861  C  CD2   . LEU A 1 113 ? -1.51800  -19.95300 27.41100  1.000 24.51347  ? 113 LEU A CD2   1 
ATOM   862  N  N     . ALA A 1 114 ? 2.27300   -21.50700 30.95900  1.000 26.94797  ? 114 ALA A N     1 
ATOM   863  C  CA    . ALA A 1 114 ? 2.67200   -21.66200 32.35400  1.000 27.91124  ? 114 ALA A CA    1 
ATOM   864  C  C     . ALA A 1 114 ? 3.43100   -20.43600 32.85200  1.000 30.72210  ? 114 ALA A C     1 
ATOM   865  O  O     . ALA A 1 114 ? 3.19400   -19.96900 33.97000  1.000 30.67999  ? 114 ALA A O     1 
ATOM   866  C  CB    . ALA A 1 114 ? 3.50900   -22.92900 32.52200  1.000 26.74005  ? 114 ALA A CB    1 
ATOM   867  N  N     . LYS A 1 115 ? 4.35100   -19.90600 32.03900  1.000 31.86435  ? 115 LYS A N     1 
ATOM   868  C  CA    . LYS A 1 115 ? 5.07600   -18.69700 32.42100  1.000 33.19082  ? 115 LYS A CA    1 
ATOM   869  C  C     . LYS A 1 115 ? 4.12900   -17.52100 32.63700  1.000 34.62257  ? 115 LYS A C     1 
ATOM   870  O  O     . LYS A 1 115 ? 4.30500   -16.74200 33.58100  1.000 30.25626  ? 115 LYS A O     1 
ATOM   871  C  CB    . LYS A 1 115 ? 6.12600   -18.35600 31.36100  1.000 32.80130  ? 115 LYS A CB    1 
ATOM   872  C  CG    . LYS A 1 115 ? 7.04800   -17.19700 31.72300  1.000 47.30041  ? 115 LYS A CG    1 
ATOM   873  C  CD    . LYS A 1 115 ? 8.02900   -17.56800 32.83000  1.000 58.83600  ? 115 LYS A CD    1 
ATOM   874  C  CE    . LYS A 1 115 ? 8.94900   -16.40100 33.17800  1.000 66.86854  ? 115 LYS A CE    1 
ATOM   875  N  NZ    . LYS A 1 115 ? 9.87200   -16.06100 32.05900  1.000 69.55834  ? 115 LYS A NZ    1 
ATOM   876  N  N     . GLN A 1 116 ? 3.12800   -17.36600 31.76400  1.000 27.69016  ? 116 GLN A N     1 
ATOM   877  C  CA    . GLN A 1 116 ? 2.17600   -16.26500 31.89900  1.000 37.65451  ? 116 GLN A CA    1 
ATOM   878  C  C     . GLN A 1 116 ? 1.37800   -16.37600 33.19400  1.000 37.64399  ? 116 GLN A C     1 
ATOM   879  O  O     . GLN A 1 116 ? 1.02200   -15.36100 33.80500  1.000 37.19130  ? 116 GLN A O     1 
ATOM   880  C  CB    . GLN A 1 116 ? 1.23900   -16.23100 30.68500  1.000 40.67067  ? 116 GLN A CB    1 
ATOM   881  C  CG    . GLN A 1 116 ? 1.89900   -15.72400 29.39600  1.000 44.14477  ? 116 GLN A CG    1 
ATOM   882  C  CD    . GLN A 1 116 ? 0.95600   -15.70200 28.19300  1.000 43.88158  ? 116 GLN A CD    1 
ATOM   883  O  OE1   . GLN A 1 116 ? 0.04500   -16.52400 28.08300  1.000 38.84413  ? 116 GLN A OE1   1 
ATOM   884  N  NE2   . GLN A 1 116 ? 1.18400   -14.76400 27.28100  1.000 43.52364  ? 116 GLN A NE2   1 
ATOM   885  N  N     . LYS A 1 117 ? 1.06700   -17.60300 33.61700  1.000 37.27552  ? 117 LYS A N     1 
ATOM   886  C  CA    . LYS A 1 117 ? 0.32300   -17.79400 34.85800  1.000 36.73862  ? 117 LYS A CA    1 
ATOM   887  C  C     . LYS A 1 117 ? 1.16700   -17.41800 36.06900  1.000 34.44360  ? 117 LYS A C     1 
ATOM   888  O  O     . LYS A 1 117 ? 0.66200   -16.81700 37.02400  1.000 36.35173  ? 117 LYS A O     1 
ATOM   889  C  CB    . LYS A 1 117 ? -0.15300  -19.24200 34.96400  1.000 40.66540  ? 117 LYS A CB    1 
ATOM   890  C  CG    . LYS A 1 117 ? -0.95300  -19.55000 36.21600  1.000 54.44863  ? 117 LYS A CG    1 
ATOM   891  C  CD    . LYS A 1 117 ? -1.43100  -20.99000 36.20900  1.000 77.97251  ? 117 LYS A CD    1 
ATOM   892  C  CE    . LYS A 1 117 ? -2.25300  -21.31300 37.44500  1.000 77.10398  ? 117 LYS A CE    1 
ATOM   893  N  NZ    . LYS A 1 117 ? -3.46500  -20.45100 37.56400  1.000 95.69042  ? 117 LYS A NZ    1 
ATOM   894  N  N     . ILE A 1 118 ? 2.45200   -17.77500 36.05200  1.000 33.32242  ? 118 ILE A N     1 
ATOM   895  C  CA    . ILE A 1 118 ? 3.33100   -17.49400 37.18200  1.000 41.26284  ? 118 ILE A CA    1 
ATOM   896  C  C     . ILE A 1 118 ? 3.75500   -16.03100 37.19000  1.000 57.18580  ? 118 ILE A C     1 
ATOM   897  O  O     . ILE A 1 118 ? 3.66000   -15.34500 38.21400  1.000 40.08112  ? 118 ILE A O     1 
ATOM   898  C  CB    . ILE A 1 118 ? 4.56000   -18.42100 37.14400  1.000 51.70883  ? 118 ILE A CB    1 
ATOM   899  C  CG1   . ILE A 1 118 ? 4.14000   -19.88500 37.24300  1.000 57.47005  ? 118 ILE A CG1   1 
ATOM   900  C  CG2   . ILE A 1 118 ? 5.52400   -18.06600 38.26600  1.000 54.24071  ? 118 ILE A CG2   1 
ATOM   901  C  CD1   . ILE A 1 118 ? 5.24900   -20.85700 36.88600  1.000 55.14609  ? 118 ILE A CD1   1 
ATOM   902  N  N     . HIS A 1 119 ? 4.24100   -15.54100 36.04900  1.000 51.99571  ? 119 HIS A N     1 
ATOM   903  C  CA    . HIS A 1 119 ? 4.88700   -14.23600 35.93500  1.000 45.42124  ? 119 HIS A CA    1 
ATOM   904  C  C     . HIS A 1 119 ? 4.10200   -13.37700 34.95000  1.000 42.10768  ? 119 HIS A C     1 
ATOM   905  O  O     . HIS A 1 119 ? 4.55000   -13.14800 33.81800  1.000 38.12036  ? 119 HIS A O     1 
ATOM   906  C  CB    . HIS A 1 119 ? 6.33500   -14.40900 35.47800  1.000 50.74556  ? 119 HIS A CB    1 
ATOM   907  C  CG    . HIS A 1 119 ? 7.20400   -13.21600 35.72600  1.000 78.18832  ? 119 HIS A CG    1 
ATOM   908  N  ND1   . HIS A 1 119 ? 6.94900   -11.98300 35.16600  1.000 100.84630 ? 119 HIS A ND1   1 
ATOM   909  C  CD2   . HIS A 1 119 ? 8.31800   -13.06400 36.48000  1.000 80.37806  ? 119 HIS A CD2   1 
ATOM   910  C  CE1   . HIS A 1 119 ? 7.87100   -11.12200 35.56200  1.000 82.91257  ? 119 HIS A CE1   1 
ATOM   911  N  NE2   . HIS A 1 119 ? 8.71400   -11.75300 36.35800  1.000 93.34277  ? 119 HIS A NE2   1 
ATOM   912  N  N     . PRO A 1 120 ? 2.93500   -12.86600 35.35800  1.000 37.06497  ? 120 PRO A N     1 
ATOM   913  C  CA    . PRO A 1 120 ? 2.09400   -12.12400 34.40500  1.000 47.96628  ? 120 PRO A CA    1 
ATOM   914  C  C     . PRO A 1 120 ? 2.67200   -10.77900 33.99000  1.000 61.31525  ? 120 PRO A C     1 
ATOM   915  O  O     . PRO A 1 120 ? 2.45700   -10.32000 32.86800  1.000 51.97202  ? 120 PRO A O     1 
ATOM   916  C  CB    . PRO A 1 120 ? 0.77300   -11.95600 35.16700  1.000 46.25028  ? 120 PRO A CB    1 
ATOM   917  C  CG    . PRO A 1 120 ? 1.18500   -11.94600 36.59900  1.000 56.74891  ? 120 PRO A CG    1 
ATOM   918  C  CD    . PRO A 1 120 ? 2.33400   -12.91400 36.70200  1.000 59.35712  ? 120 PRO A CD    1 
ATOM   919  N  N     . GLU A 1 121 ? 3.46500   -10.18900 34.89500  1.000 61.77320  ? 121 GLU A N     1 
ATOM   920  C  CA    . GLU A 1 121 ? 4.10500   -8.85700  34.70200  1.000 54.58549  ? 121 GLU A CA    1 
ATOM   921  C  C     . GLU A 1 121 ? 5.25500   -8.93100  33.68500  1.000 52.62210  ? 121 GLU A C     1 
ATOM   922  O  O     . GLU A 1 121 ? 5.74400   -10.04500 33.40700  1.000 52.50366  ? 121 GLU A O     1 
ATOM   923  C  CB    . GLU A 1 121 ? 4.60000   -8.30700  36.04100  1.000 55.45928  ? 121 GLU A CB    1 
ATOM   924  C  CG    . GLU A 1 121 ? 3.50600   -7.65700  36.86900  1.000 64.54984  ? 121 GLU A CG    1 
ATOM   925  C  CD    . GLU A 1 121 ? 2.78600   -6.51100  36.17900  1.000 71.01115  ? 121 GLU A CD    1 
ATOM   926  O  OE1   . GLU A 1 121 ? 3.41800   -5.45600  35.97400  1.000 59.75190  ? 121 GLU A OE1   1 
ATOM   927  O  OE2   . GLU A 1 121 ? 1.59500   -6.67600  35.85000  1.000 73.70357  ? 121 GLU A OE2   1 
ATOM   928  N  N     . ARG A 1 122 ? 5.68800   -7.76600  33.19000  1.000 43.67103  ? 122 ARG A N     1 
ATOM   929  C  CA    . ARG A 1 122 ? 6.76800   -7.67200  32.16900  1.000 36.08591  ? 122 ARG A CA    1 
ATOM   930  C  C     . ARG A 1 122 ? 8.07100   -8.25700  32.72800  1.000 38.80992  ? 122 ARG A C     1 
ATOM   931  O  O     . ARG A 1 122 ? 8.47700   -7.87600  33.81600  1.000 36.00168  ? 122 ARG A O     1 
ATOM   932  C  CB    . ARG A 1 122 ? 6.96500   -6.21700  31.73200  1.000 44.79221  ? 122 ARG A CB    1 
ATOM   933  C  CG    . ARG A 1 122 ? 7.98500   -6.03600  30.61700  1.000 52.44313  ? 122 ARG A CG    1 
ATOM   934  C  CD    . ARG A 1 122 ? 8.09600   -4.59300  30.16300  1.000 60.38619  ? 122 ARG A CD    1 
ATOM   935  N  NE    . ARG A 1 122 ? 6.89000   -4.12800  29.49200  1.000 64.25770  ? 122 ARG A NE    1 
ATOM   936  C  CZ    . ARG A 1 122 ? 6.72400   -4.10500  28.17400  1.000 58.53333  ? 122 ARG A CZ    1 
ATOM   937  N  NH1   . ARG A 1 122 ? 7.69200   -4.52300  27.37700  1.000 50.38236  ? 122 ARG A NH1   1 
ATOM   938  N  NH2   . ARG A 1 122 ? 5.59100   -3.66300  27.65800  1.000 71.39277  ? 122 ARG A NH2   1 
ATOM   939  N  N     . THR A 1 123 ? 8.71600   -9.13000  31.96200  1.000 40.74699  ? 123 THR A N     1 
ATOM   940  C  CA    . THR A 1 123 ? 9.94800   -9.80100  32.34500  1.000 35.28055  ? 123 THR A CA    1 
ATOM   941  C  C     . THR A 1 123 ? 11.15500  -9.05300  31.79800  1.000 37.21762  ? 123 THR A C     1 
ATOM   942  O  O     . THR A 1 123 ? 11.02900  -8.18600  30.92500  1.000 35.55689  ? 123 THR A O     1 
ATOM   943  C  CB    . THR A 1 123 ? 9.95000   -11.23500 31.80900  1.000 45.58178  ? 123 THR A CB    1 
ATOM   944  O  OG1   . THR A 1 123 ? 9.93100   -11.19600 30.37800  1.000 35.83061  ? 123 THR A OG1   1 
ATOM   945  C  CG2   . THR A 1 123 ? 8.73800   -12.00000 32.29000  1.000 40.33378  ? 123 THR A CG2   1 
ATOM   946  N  N     . PRO A 1 124 ? 12.36000  -9.36300  32.29000  1.000 45.41597  ? 124 PRO A N     1 
ATOM   947  C  CA    . PRO A 1 124 ? 13.57800  -8.81300  31.66900  1.000 38.95467  ? 124 PRO A CA    1 
ATOM   948  C  C     . PRO A 1 124 ? 13.79000  -9.23600  30.22000  1.000 41.30232  ? 124 PRO A C     1 
ATOM   949  O  O     . PRO A 1 124 ? 14.65900  -8.65600  29.55600  1.000 41.26284  ? 124 PRO A O     1 
ATOM   950  C  CB    . PRO A 1 124 ? 14.70400  -9.34000  32.56900  1.000 40.65751  ? 124 PRO A CB    1 
ATOM   951  C  CG    . PRO A 1 124 ? 14.04400  -9.61200  33.87700  1.000 53.51694  ? 124 PRO A CG    1 
ATOM   952  C  CD    . PRO A 1 124 ? 12.66200  -10.08200 33.54300  1.000 54.41442  ? 124 PRO A CD    1 
ATOM   953  N  N     . SER A 1 125 ? 13.06800  -10.24600 29.72500  1.000 43.12096  ? 125 SER A N     1 
ATOM   954  C  CA    . SER A 1 125 ? 13.12300  -10.62000 28.31500  1.000 34.33306  ? 125 SER A CA    1 
ATOM   955  C  C     . SER A 1 125 ? 12.36800  -9.64800  27.42000  1.000 38.48619  ? 125 SER A C     1 
ATOM   956  O  O     . SER A 1 125 ? 12.50300  -9.72700  26.19300  1.000 33.82774  ? 125 SER A O     1 
ATOM   957  C  CB    . SER A 1 125 ? 12.53400  -12.02000 28.10500  1.000 32.80130  ? 125 SER A CB    1 
ATOM   958  O  OG    . SER A 1 125 ? 13.24400  -13.00500 28.82200  1.000 44.09739  ? 125 SER A OG    1 
ATOM   959  N  N     . GLU A 1 126 ? 11.55800  -8.76500  28.00200  1.000 43.61312  ? 126 GLU A N     1 
ATOM   960  C  CA    . GLU A 1 126 ? 10.62600  -7.93900  27.24700  1.000 33.83037  ? 126 GLU A CA    1 
ATOM   961  C  C     . GLU A 1 126 ? 10.88600  -6.45500  27.47400  1.000 35.72797  ? 126 GLU A C     1 
ATOM   962  O  O     . GLU A 1 126 ? 9.95700   -5.69700  27.76200  1.000 37.89402  ? 126 GLU A O     1 
ATOM   963  C  CB    . GLU A 1 126 ? 9.18900   -8.28500  27.63900  1.000 35.97537  ? 126 GLU A CB    1 
ATOM   964  C  CG    . GLU A 1 126 ? 8.81900   -9.75200  27.46200  1.000 42.99463  ? 126 GLU A CG    1 
ATOM   965  C  CD    . GLU A 1 126 ? 7.55900   -10.13400 28.23200  1.000 43.78683  ? 126 GLU A CD    1 
ATOM   966  O  OE1   . GLU A 1 126 ? 7.61500   -10.19700 29.47700  1.000 42.77092  ? 126 GLU A OE1   1 
ATOM   967  O  OE2   . GLU A 1 126 ? 6.50700   -10.35400 27.59300  1.000 34.22779  ? 126 GLU A OE2   1 
ATOM   968  N  N     . LYS A 1 127 ? 12.14700  -6.03500  27.37400  1.000 33.87511  ? 127 LYS A N     1 
ATOM   969  C  CA    . LYS A 1 127 ? 12.47500  -4.62700  27.58800  1.000 42.19453  ? 127 LYS A CA    1 
ATOM   970  C  C     . LYS A 1 127 ? 11.87900  -3.73600  26.50000  1.000 37.66767  ? 127 LYS A C     1 
ATOM   971  O  O     . LYS A 1 127 ? 11.47500  -2.60200  26.77900  1.000 44.91065  ? 127 LYS A O     1 
ATOM   972  C  CB    . LYS A 1 127 ? 13.98800  -4.44600  27.67400  1.000 44.60008  ? 127 LYS A CB    1 
ATOM   973  C  CG    . LYS A 1 127 ? 14.61000  -5.12600  28.88200  1.000 47.37410  ? 127 LYS A CG    1 
ATOM   974  C  CD    . LYS A 1 127 ? 16.11200  -4.93800  28.89500  1.000 55.31979  ? 127 LYS A CD    1 
ATOM   975  C  CE    . LYS A 1 127 ? 16.79100  -5.87900  29.87400  1.000 48.87954  ? 127 LYS A CE    1 
ATOM   976  N  NZ    . LYS A 1 127 ? 16.29600  -5.68400  31.25400  1.000 51.20088  ? 127 LYS A NZ    1 
ATOM   977  N  N     . LEU A 1 128 ? 11.85400  -4.21000  25.24800  1.000 36.86495  ? 128 LEU A N     1 
ATOM   978  C  CA    . LEU A 1 128 ? 11.33300  -3.42000  24.13700  1.000 35.38056  ? 128 LEU A CA    1 
ATOM   979  C  C     . LEU A 1 128 ? 10.07800  -3.99300  23.49100  1.000 36.78862  ? 128 LEU A C     1 
ATOM   980  O  O     . LEU A 1 128 ? 9.31800   -3.23200  22.88100  1.000 35.53321  ? 128 LEU A O     1 
ATOM   981  C  CB    . LEU A 1 128 ? 12.40800  -3.25100  23.05400  1.000 37.78874  ? 128 LEU A CB    1 
ATOM   982  C  CG    . LEU A 1 128 ? 13.58300  -2.36000  23.45900  1.000 42.48667  ? 128 LEU A CG    1 
ATOM   983  C  CD1   . LEU A 1 128 ? 14.59900  -2.25000  22.33600  1.000 42.68670  ? 128 LEU A CD1   1 
ATOM   984  C  CD2   . LEU A 1 128 ? 13.07900  -0.98300  23.86600  1.000 48.68742  ? 128 LEU A CD2   1 
ATOM   985  N  N     . LEU A 1 129 ? 9.83500   -5.29900  23.61400  1.000 35.07526  ? 129 LEU A N     1 
ATOM   986  C  CA    . LEU A 1 129 ? 8.68600   -5.93500  22.97600  1.000 29.55881  ? 129 LEU A CA    1 
ATOM   987  C  C     . LEU A 1 129 ? 8.17600   -7.04700  23.87700  1.000 29.57986  ? 129 LEU A C     1 
ATOM   988  O  O     . LEU A 1 129 ? 8.93800   -7.95200  24.22500  1.000 29.62987  ? 129 LEU A O     1 
ATOM   989  C  CB    . LEU A 1 129 ? 9.07100   -6.49500  21.60600  1.000 29.68514  ? 129 LEU A CB    1 
ATOM   990  C  CG    . LEU A 1 129 ? 7.94200   -7.17400  20.84000  1.000 34.48571  ? 129 LEU A CG    1 
ATOM   991  C  CD1   . LEU A 1 129 ? 6.84600   -6.17300  20.51400  1.000 41.76817  ? 129 LEU A CD1   1 
ATOM   992  C  CD2   . LEU A 1 129 ? 8.46900   -7.83400  19.57300  1.000 35.15158  ? 129 LEU A CD2   1 
ATOM   993  N  N     . ALA A 1 130 ? 6.89700   -6.99900  24.23100  1.000 31.27217  ? 130 ALA A N     1 
ATOM   994  C  CA    . ALA A 1 130 ? 6.30600   -8.02100  25.08400  1.000 34.98314  ? 130 ALA A CA    1 
ATOM   995  C  C     . ALA A 1 130 ? 5.67300   -9.13300  24.25200  1.000 37.45975  ? 130 ALA A C     1 
ATOM   996  O  O     . ALA A 1 130 ? 5.27700   -8.93300  23.10100  1.000 31.62484  ? 130 ALA A O     1 
ATOM   997  C  CB    . ALA A 1 130 ? 5.26600   -7.40800  26.02100  1.000 33.21977  ? 130 ALA A CB    1 
ATOM   998  N  N     . VAL A 1 131 ? 5.56300   -10.31500 24.86900  1.000 30.92476  ? 131 VAL A N     1 
ATOM   999  C  CA    . VAL A 1 131 ? 4.94900   -11.46500 24.20200  1.000 34.67258  ? 131 VAL A CA    1 
ATOM   1000 C  C     . VAL A 1 131 ? 3.53200   -11.13500 23.74500  1.000 31.84592  ? 131 VAL A C     1 
ATOM   1001 O  O     . VAL A 1 131 ? 3.14100   -11.45400 22.61400  1.000 28.00073  ? 131 VAL A O     1 
ATOM   1002 C  CB    . VAL A 1 131 ? 4.97000   -12.69300 25.13800  1.000 33.29873  ? 131 VAL A CB    1 
ATOM   1003 C  CG1   . VAL A 1 131 ? 4.17200   -13.85100 24.54600  1.000 31.09583  ? 131 VAL A CG1   1 
ATOM   1004 C  CG2   . VAL A 1 131 ? 6.40700   -13.11900 25.41800  1.000 33.34610  ? 131 VAL A CG2   1 
ATOM   1005 N  N     . LYS A 1 132 ? 2.75300   -10.46600 24.60400  1.000 37.67031  ? 132 LYS A N     1 
ATOM   1006 C  CA    . LYS A 1 132 ? 1.38900   -10.07800 24.25100  1.000 42.04715  ? 132 LYS A CA    1 
ATOM   1007 C  C     . LYS A 1 132 ? 1.33900   -9.18600  23.01900  1.000 33.94881  ? 132 LYS A C     1 
ATOM   1008 O  O     . LYS A 1 132 ? 0.33100   -9.18100  22.30500  1.000 41.14177  ? 132 LYS A O     1 
ATOM   1009 C  CB    . LYS A 1 132 ? 0.71400   -9.36600  25.42700  1.000 47.85311  ? 132 LYS A CB    1 
ATOM   1010 C  CG    . LYS A 1 132 ? 0.59100   -10.18600 26.69600  1.000 70.55056  ? 132 LYS A CG    1 
ATOM   1011 C  CD    . LYS A 1 132 ? -0.42200  -11.30400 26.51100  1.000 80.75179  ? 132 LYS A CD    1 
ATOM   1012 C  CE    . LYS A 1 132 ? -0.83800  -11.91000 27.84000  1.000 86.85515  ? 132 LYS A CE    1 
ATOM   1013 N  NZ    . LYS A 1 132 ? -1.93700  -12.89700 27.65900  1.000 93.29276  ? 132 LYS A NZ    1 
ATOM   1014 N  N     . GLU A 1 133 ? 2.39500   -8.41400  22.76100  1.000 32.45389  ? 133 GLU A N     1 
ATOM   1015 C  CA    . GLU A 1 133 ? 2.44300   -7.49800  21.62300  1.000 32.51706  ? 133 GLU A CA    1 
ATOM   1016 C  C     . GLU A 1 133 ? 2.94300   -8.15800  20.33700  1.000 36.66492  ? 133 GLU A C     1 
ATOM   1017 O  O     . GLU A 1 133 ? 3.06200   -7.47300  19.31400  1.000 27.07167  ? 133 GLU A O     1 
ATOM   1018 C  CB    . GLU A 1 133 ? 3.32900   -6.28700  21.96700  1.000 37.34395  ? 133 GLU A CB    1 
ATOM   1019 C  CG    . GLU A 1 133 ? 2.84500   -5.48900  23.18000  1.000 35.39109  ? 133 GLU A CG    1 
ATOM   1020 C  CD    . GLU A 1 133 ? 3.85400   -4.45400  23.68900  1.000 50.62975  ? 133 GLU A CD    1 
ATOM   1021 O  OE1   . GLU A 1 133 ? 5.02600   -4.45700  23.24800  1.000 30.73790  ? 133 GLU A OE1   1 
ATOM   1022 O  OE2   . GLU A 1 133 ? 3.47000   -3.63700  24.55400  1.000 64.32877  ? 133 GLU A OE2   1 
ATOM   1023 N  N     . PHE A 1 134 ? 3.24700   -9.45700  20.37200  1.000 32.43547  ? 134 PHE A N     1 
ATOM   1024 C  CA    . PHE A 1 134 ? 3.75200   -10.16500 19.19900  1.000 21.64470  ? 134 PHE A CA    1 
ATOM   1025 C  C     . PHE A 1 134 ? 2.80200   -10.05900 18.01100  1.000 22.00790  ? 134 PHE A C     1 
ATOM   1026 O  O     . PHE A 1 134 ? 1.58100   -10.14100 18.15600  1.000 20.45508  ? 134 PHE A O     1 
ATOM   1027 C  CB    . PHE A 1 134 ? 3.97500   -11.64300 19.52900  1.000 29.04559  ? 134 PHE A CB    1 
ATOM   1028 C  CG    . PHE A 1 134 ? 5.31000   -11.94900 20.16800  1.000 26.94007  ? 134 PHE A CG    1 
ATOM   1029 C  CD1   . PHE A 1 134 ? 6.28300   -10.97500 20.30100  1.000 28.85872  ? 134 PHE A CD1   1 
ATOM   1030 C  CD2   . PHE A 1 134 ? 5.59200   -13.23500 20.61400  1.000 25.81625  ? 134 PHE A CD2   1 
ATOM   1031 C  CE1   . PHE A 1 134 ? 7.51200   -11.27500 20.87800  1.000 28.73239  ? 134 PHE A CE1   1 
ATOM   1032 C  CE2   . PHE A 1 134 ? 6.81600   -13.54000 21.19200  1.000 23.43439  ? 134 PHE A CE2   1 
ATOM   1033 C  CZ    . PHE A 1 134 ? 7.77300   -12.55700 21.32400  1.000 23.14225  ? 134 PHE A CZ    1 
ATOM   1034 N  N     . GLU A 1 135 ? 3.38200   -9.95000  16.81800  1.000 26.40317  ? 135 GLU A N     1 
ATOM   1035 C  CA    . GLU A 1 135 ? 2.61400   -10.03100 15.58400  1.000 31.34586  ? 135 GLU A CA    1 
ATOM   1036 C  C     . GLU A 1 135 ? 2.08400   -11.44600 15.39100  1.000 34.84628  ? 135 GLU A C     1 
ATOM   1037 O  O     . GLU A 1 135 ? 2.79000   -12.42700 15.63600  1.000 27.78754  ? 135 GLU A O     1 
ATOM   1038 C  CB    . GLU A 1 135 ? 3.49600   -9.63800  14.39500  1.000 32.05648  ? 135 GLU A CB    1 
ATOM   1039 C  CG    . GLU A 1 135 ? 2.79400   -9.62400  13.04800  1.000 41.27600  ? 135 GLU A CG    1 
ATOM   1040 C  CD    . GLU A 1 135 ? 1.75100   -8.54300  12.94000  1.000 50.37446  ? 135 GLU A CD    1 
ATOM   1041 O  OE1   . GLU A 1 135 ? 2.10700   -7.35600  13.10500  1.000 64.03926  ? 135 GLU A OE1   1 
ATOM   1042 O  OE2   . GLU A 1 135 ? 0.57300   -8.88300  12.69800  1.000 51.53776  ? 135 GLU A OE2   1 
ATOM   1043 N  N     . SER A 1 136 ? 0.82100   -11.55300 14.97200  1.000 24.56347  ? 136 SER A N     1 
ATOM   1044 C  CA    . SER A 1 136 ? 0.20500   -12.84900 14.71400  1.000 27.14010  ? 136 SER A CA    1 
ATOM   1045 C  C     . SER A 1 136 ? -0.06800  -13.11700 13.24200  1.000 26.60582  ? 136 SER A C     1 
ATOM   1046 O  O     . SER A 1 136 ? -0.07900  -14.28200 12.83900  1.000 26.26368  ? 136 SER A O     1 
ATOM   1047 C  CB    . SER A 1 136 ? -1.12300  -12.97700 15.46800  1.000 28.22444  ? 136 SER A CB    1 
ATOM   1048 O  OG    . SER A 1 136 ? -2.10000  -12.13800 14.87900  1.000 28.77450  ? 136 SER A OG    1 
ATOM   1049 N  N     . HIS A 1 137 ? -0.31500  -12.07000 12.44400  1.000 29.25877  ? 137 HIS A N     1 
ATOM   1050 C  CA    . HIS A 1 137 ? -0.75500  -12.19900 11.04800  1.000 27.53751  ? 137 HIS A CA    1 
ATOM   1051 C  C     . HIS A 1 137 ? -1.99600  -13.08000 10.93300  1.000 25.19513  ? 137 HIS A C     1 
ATOM   1052 O  O     . HIS A 1 137 ? -2.18900  -13.77700 9.93300   1.000 32.00910  ? 137 HIS A O     1 
ATOM   1053 C  CB    . HIS A 1 137 ? 0.36300   -12.72700 10.14000  1.000 31.08794  ? 137 HIS A CB    1 
ATOM   1054 C  CG    . HIS A 1 137 ? 1.51200   -11.78200 9.98200   1.000 28.32182  ? 137 HIS A CG    1 
ATOM   1055 N  ND1   . HIS A 1 137 ? 1.37100   -10.52600 9.43300   1.000 34.89629  ? 137 HIS A ND1   1 
ATOM   1056 C  CD2   . HIS A 1 137 ? 2.82300   -11.90900 10.29900  1.000 37.04918  ? 137 HIS A CD2   1 
ATOM   1057 C  CE1   . HIS A 1 137 ? 2.54400   -9.91800  9.42300   1.000 35.76745  ? 137 HIS A CE1   1 
ATOM   1058 N  NE2   . HIS A 1 137 ? 3.44300   -10.73600 9.94200   1.000 34.88839  ? 137 HIS A NE2   1 
ATOM   1059 N  N     . LEU A 1 138 ? -2.86600  -13.01400 11.94700  1.000 28.32708  ? 138 LEU A N     1 
ATOM   1060 C  CA    . LEU A 1 138 ? -4.04800  -13.86900 11.99000  1.000 36.59386  ? 138 LEU A CA    1 
ATOM   1061 C  C     . LEU A 1 138 ? -4.90600  -13.69800 10.74300  1.000 28.58237  ? 138 LEU A C     1 
ATOM   1062 O  O     . LEU A 1 138 ? -5.38200  -14.68500 10.17000  1.000 35.50426  ? 138 LEU A O     1 
ATOM   1063 C  CB    . LEU A 1 138 ? -4.86000  -13.55900 13.24900  1.000 29.57986  ? 138 LEU A CB    1 
ATOM   1064 C  CG    . LEU A 1 138 ? -6.11900  -14.38700 13.49800  1.000 39.01257  ? 138 LEU A CG    1 
ATOM   1065 C  CD1   . LEU A 1 138 ? -5.77900  -15.86700 13.51700  1.000 35.29371  ? 138 LEU A CD1   1 
ATOM   1066 C  CD2   . LEU A 1 138 ? -6.79700  -13.96100 14.79300  1.000 46.98984  ? 138 LEU A CD2   1 
ATOM   1067 N  N     . ASP A 1 139 ? -5.10200  -12.45200 10.29900  1.000 34.72522  ? 139 ASP A N     1 
ATOM   1068 C  CA    . ASP A 1 139 ? -5.91700  -12.16500 9.12300   1.000 36.52280  ? 139 ASP A CA    1 
ATOM   1069 C  C     . ASP A 1 139 ? -5.30900  -12.68300 7.82400   1.000 35.52268  ? 139 ASP A C     1 
ATOM   1070 O  O     . ASP A 1 139 ? -6.01600  -12.71700 6.81100   1.000 38.28354  ? 139 ASP A O     1 
ATOM   1071 C  CB    . ASP A 1 139 ? -6.14900  -10.65700 8.99400   1.000 39.61264  ? 139 ASP A CB    1 
ATOM   1072 C  CG    . ASP A 1 139 ? -4.84700  -9.87900  8.83600   1.000 55.75932  ? 139 ASP A CG    1 
ATOM   1073 O  OD1   . ASP A 1 139 ? -3.88400  -10.17200 9.57900   1.000 60.77571  ? 139 ASP A OD1   1 
ATOM   1074 O  OD2   . ASP A 1 139 ? -4.78300  -8.98200  7.96800   1.000 82.21512  ? 139 ASP A OD2   1 
ATOM   1075 N  N     . LYS A 1 140 ? -4.03500  -13.08100 7.81400   1.000 30.95371  ? 140 LYS A N     1 
ATOM   1076 C  CA    . LYS A 1 140 ? -3.41200  -13.58700 6.59500   1.000 34.28043  ? 140 LYS A CA    1 
ATOM   1077 C  C     . LYS A 1 140 ? -3.35700  -15.10600 6.54700   1.000 31.80118  ? 140 LYS A C     1 
ATOM   1078 O  O     . LYS A 1 140 ? -3.07500  -15.66500 5.48300   1.000 32.77498  ? 140 LYS A O     1 
ATOM   1079 C  CB    . LYS A 1 140 ? -1.98000  -13.05100 6.44100   1.000 40.21535  ? 140 LYS A CB    1 
ATOM   1080 C  CG    . LYS A 1 140 ? -1.81900  -11.55100 6.59400   1.000 57.45426  ? 140 LYS A CG    1 
ATOM   1081 C  CD    . LYS A 1 140 ? -2.16700  -10.82200 5.31300   1.000 56.34360  ? 140 LYS A CD    1 
ATOM   1082 C  CE    . LYS A 1 140 ? -1.75100  -9.36200  5.39000   1.000 67.65548  ? 140 LYS A CE    1 
ATOM   1083 N  NZ    . LYS A 1 140 ? -0.28200  -9.22800  5.59200   1.000 66.86854  ? 140 LYS A NZ    1 
ATOM   1084 N  N     . LEU A 1 141 ? -3.64200  -15.77800 7.65900   1.000 24.50557  ? 141 LEU A N     1 
ATOM   1085 C  CA    . LEU A 1 141 ? -3.58300  -17.23200 7.71400   1.000 23.92392  ? 141 LEU A CA    1 
ATOM   1086 C  C     . LEU A 1 141 ? -4.66200  -17.85300 6.83800   1.000 25.99785  ? 141 LEU A C     1 
ATOM   1087 O  O     . LEU A 1 141 ? -5.83400  -17.47600 6.91000   1.000 23.67126  ? 141 LEU A O     1 
ATOM   1088 C  CB    . LEU A 1 141 ? -3.76200  -17.69900 9.16300   1.000 32.55390  ? 141 LEU A CB    1 
ATOM   1089 C  CG    . LEU A 1 141 ? -2.72500  -17.26500 10.20600  1.000 34.99367  ? 141 LEU A CG    1 
ATOM   1090 C  CD1   . LEU A 1 141 ? -2.96200  -17.97300 11.53700  1.000 36.29909  ? 141 LEU A CD1   1 
ATOM   1091 C  CD2   . LEU A 1 141 ? -1.31800  -17.53900 9.70600   1.000 37.36501  ? 141 LEU A CD2   1 
ATOM   1092 N  N     . ASP A 1 142 ? -4.28700  -18.86900 6.07400   1.000 31.46693  ? 142 ASP A N     1 
ATOM   1093 C  CA    . ASP A 1 142 ? -5.27900  -19.55300 5.26300   1.000 34.01197  ? 142 ASP A CA    1 
ATOM   1094 C  C     . ASP A 1 142 ? -5.85200  -20.72800 6.05900   1.000 35.96747  ? 142 ASP A C     1 
ATOM   1095 O  O     . ASP A 1 142 ? -5.40900  -21.03200 7.17000   1.000 35.82535  ? 142 ASP A O     1 
ATOM   1096 C  CB    . ASP A 1 142 ? -4.66800  -20.00000 3.93400   1.000 38.80992  ? 142 ASP A CB    1 
ATOM   1097 C  CG    . ASP A 1 142 ? -3.50900  -20.96500 4.11100   1.000 48.05576  ? 142 ASP A CG    1 
ATOM   1098 O  OD1   . ASP A 1 142 ? -3.15800  -21.27200 5.26700   1.000 61.68371  ? 142 ASP A OD1   1 
ATOM   1099 O  OD2   . ASP A 1 142 ? -2.93200  -21.40300 3.09000   1.000 71.86651  ? 142 ASP A OD2   1 
ATOM   1100 N  N     . ASN A 1 143 ? -6.87700  -21.36900 5.49300   1.000 26.70320  ? 143 ASN A N     1 
ATOM   1101 C  CA    . ASN A 1 143 ? -7.57400  -22.42900 6.22100   1.000 34.74101  ? 143 ASN A CA    1 
ATOM   1102 C  C     . ASN A 1 143 ? -6.63700  -23.56600 6.59700   1.000 32.27755  ? 143 ASN A C     1 
ATOM   1103 O  O     . ASN A 1 143 ? -6.78000  -24.16200 7.67000   1.000 31.79592  ? 143 ASN A O     1 
ATOM   1104 C  CB    . ASN A 1 143 ? -8.77700  -22.93500 5.43200   1.000 29.46932  ? 143 ASN A CB    1 
ATOM   1105 C  CG    . ASN A 1 143 ? -9.82300  -21.86200 5.25100   1.000 33.64614  ? 143 ASN A CG    1 
ATOM   1106 O  OD1   . ASN A 1 143 ? -9.89000  -20.91700 6.03700   1.000 34.38044  ? 143 ASN A OD1   1 
ATOM   1107 N  ND2   . ASN A 1 143 ? -10.68100 -22.02700 4.25800   1.000 34.31990  ? 143 ASN A ND2   1 
ATOM   1108 N  N     . GLU A 1 144 ? -5.69500  -23.90600 5.72000   1.000 30.79580  ? 144 GLU A N     1 
ATOM   1109 C  CA    . GLU A 1 144 ? -4.79300  -25.00600 6.04100   1.000 38.53357  ? 144 GLU A CA    1 
ATOM   1110 C  C     . GLU A 1 144 ? -3.90500  -24.65900 7.23400   1.000 32.01700  ? 144 GLU A C     1 
ATOM   1111 O  O     . GLU A 1 144 ? -3.66300  -25.50800 8.10100   1.000 30.07466  ? 144 GLU A O     1 
ATOM   1112 C  CB    . GLU A 1 144 ? -3.94400  -25.35400 4.81800   1.000 37.21236  ? 144 GLU A CB    1 
ATOM   1113 C  CG    . GLU A 1 144 ? -2.69000  -26.16000 5.12100   1.000 56.28833  ? 144 GLU A CG    1 
ATOM   1114 C  CD    . GLU A 1 144 ? -2.04300  -26.72500 3.86400   1.000 70.47687  ? 144 GLU A CD    1 
ATOM   1115 O  OE1   . GLU A 1 144 ? -2.76600  -27.33600 3.04700   1.000 71.79019  ? 144 GLU A OE1   1 
ATOM   1116 O  OE2   . GLU A 1 144 ? -0.81600  -26.55400 3.68900   1.000 61.35209  ? 144 GLU A OE2   1 
ATOM   1117 N  N     . LYS A 1 145 ? -3.46300  -23.40200 7.33400   1.000 29.14034  ? 145 LYS A N     1 
ATOM   1118 C  CA    . LYS A 1 145 ? -2.67400  -23.00700 8.49500   1.000 30.86686  ? 145 LYS A CA    1 
ATOM   1119 C  C     . LYS A 1 145 ? -3.53100  -22.89000 9.74900   1.000 30.22731  ? 145 LYS A C     1 
ATOM   1120 O  O     . LYS A 1 145 ? -3.07900  -23.26400 10.83600  1.000 27.66121  ? 145 LYS A O     1 
ATOM   1121 C  CB    . LYS A 1 145 ? -1.97300  -21.67200 8.24000   1.000 31.03004  ? 145 LYS A CB    1 
ATOM   1122 C  CG    . LYS A 1 145 ? -0.77700  -21.75000 7.31500   1.000 44.45270  ? 145 LYS A CG    1 
ATOM   1123 C  CD    . LYS A 1 145 ? -0.41100  -20.36600 6.79400   1.000 58.98339  ? 145 LYS A CD    1 
ATOM   1124 C  CE    . LYS A 1 145 ? 0.40700   -20.42500 5.50900   1.000 61.53896  ? 145 LYS A CE    1 
ATOM   1125 N  NZ    . LYS A 1 145 ? 1.57000   -21.34000 5.60200   1.000 66.06055  ? 145 LYS A NZ    1 
ATOM   1126 N  N     . LYS A 1 146 ? -4.79000  -22.46100 9.61100   1.000 27.38486  ? 146 LYS A N     1 
ATOM   1127 C  CA    . LYS A 1 146 ? -5.67400  -22.39000 10.77500  1.000 28.10863  ? 146 LYS A CA    1 
ATOM   1128 C  C     . LYS A 1 146 ? -6.03400  -23.77700 11.28200  1.000 25.57938  ? 146 LYS A C     1 
ATOM   1129 O  O     . LYS A 1 146 ? -6.01300  -24.02700 12.49300  1.000 24.84772  ? 146 LYS A O     1 
ATOM   1130 C  CB    . LYS A 1 146 ? -6.95200  -21.62700 10.42100  1.000 35.14106  ? 146 LYS A CB    1 
ATOM   1131 C  CG    . LYS A 1 146 ? -6.78000  -20.13500 10.21100  1.000 46.46347  ? 146 LYS A CG    1 
ATOM   1132 C  CD    . LYS A 1 146 ? -6.98800  -19.38000 11.51600  1.000 67.60811  ? 146 LYS A CD    1 
ATOM   1133 C  CE    . LYS A 1 146 ? -8.09800  -18.34300 11.39200  1.000 72.01390  ? 146 LYS A CE    1 
ATOM   1134 N  NZ    . LYS A 1 146 ? -7.70500  -17.20400 10.51800  1.000 81.15447  ? 146 LYS A NZ    1 
ATOM   1135 N  N     . ASP A 1 147 ? -6.33900  -24.69400 10.36800  1.000 27.92177  ? 147 ASP A N     1 
ATOM   1136 C  CA    . ASP A 1 147 ? -6.64900  -26.06500 10.74800  1.000 29.90885  ? 147 ASP A CA    1 
ATOM   1137 C  C     . ASP A 1 147 ? -5.45700  -26.75200 11.41900  1.000 25.87942  ? 147 ASP A C     1 
ATOM   1138 O  O     . ASP A 1 147 ? -5.64800  -27.57900 12.31700  1.000 28.74555  ? 147 ASP A O     1 
ATOM   1139 C  CB    . ASP A 1 147 ? -7.15100  -26.82400 9.51200   1.000 31.64590  ? 147 ASP A CB    1 
ATOM   1140 C  CG    . ASP A 1 147 ? -8.57600  -26.39100 9.09400   1.000 55.32769  ? 147 ASP A CG    1 
ATOM   1141 O  OD1   . ASP A 1 147 ? -9.18700  -25.55600 9.80500   1.000 38.49672  ? 147 ASP A OD1   1 
ATOM   1142 O  OD2   . ASP A 1 147 ? -9.08300  -26.87200 8.04700   1.000 44.76589  ? 147 ASP A OD2   1 
ATOM   1143 N  N     . LEU A 1 148 ? -4.22500  -26.40900 11.02400  1.000 21.85262  ? 148 LEU A N     1 
ATOM   1144 C  CA    . LEU A 1 148 ? -3.05800  -26.97900 11.69600  1.000 27.58489  ? 148 LEU A CA    1 
ATOM   1145 C  C     . LEU A 1 148 ? -2.91100  -26.43100 13.11400  1.000 26.45317  ? 148 LEU A C     1 
ATOM   1146 O  O     . LEU A 1 148 ? -2.55600  -27.17400 14.03600  1.000 25.66624  ? 148 LEU A O     1 
ATOM   1147 C  CB    . LEU A 1 148 ? -1.78500  -26.70900 10.89400  1.000 32.21965  ? 148 LEU A CB    1 
ATOM   1148 C  CG    . LEU A 1 148 ? -1.59800  -27.51100 9.60600   1.000 52.43260  ? 148 LEU A CG    1 
ATOM   1149 C  CD1   . LEU A 1 148 ? -0.45600  -26.93100 8.79100   1.000 56.04093  ? 148 LEU A CD1   1 
ATOM   1150 C  CD2   . LEU A 1 148 ? -1.35100  -28.98000 9.91100   1.000 51.54302  ? 148 LEU A CD2   1 
ATOM   1151 N  N     . ILE A 1 149 ? -3.15700  -25.13400 13.30700  1.000 21.78156  ? 149 ILE A N     1 
ATOM   1152 C  CA    . ILE A 1 149 ? -3.14600  -24.57400 14.65800  1.000 23.50545  ? 149 ILE A CA    1 
ATOM   1153 C  C     . ILE A 1 149 ? -4.22200  -25.22900 15.51500  1.000 21.95526  ? 149 ILE A C     1 
ATOM   1154 O  O     . ILE A 1 149 ? -3.99400  -25.55800 16.68600  1.000 25.09511  ? 149 ILE A O     1 
ATOM   1155 C  CB    . ILE A 1 149 ? -3.32100  -23.04700 14.60600  1.000 21.81051  ? 149 ILE A CB    1 
ATOM   1156 C  CG1   . ILE A 1 149 ? -2.06700  -22.39400 14.01700  1.000 19.01281  ? 149 ILE A CG1   1 
ATOM   1157 C  CG2   . ILE A 1 149 ? -3.66700  -22.50000 15.99700  1.000 29.71935  ? 149 ILE A CG2   1 
ATOM   1158 C  CD1   . ILE A 1 149 ? -2.17900  -20.90000 13.85400  1.000 19.69973  ? 149 ILE A CD1   1 
ATOM   1159 N  N     . GLN A 1 150 ? -5.41900  -25.41300 14.95300  1.000 21.63944  ? 150 GLN A N     1 
ATOM   1160 C  CA    . GLN A 1 150 ? -6.48400  -26.06100 15.70800  1.000 24.37924  ? 150 GLN A CA    1 
ATOM   1161 C  C     . GLN A 1 150 ? -6.11400  -27.49000 16.07100  1.000 24.86351  ? 150 GLN A C     1 
ATOM   1162 O  O     . GLN A 1 150 ? -6.54900  -28.00300 17.10800  1.000 25.84520  ? 150 GLN A O     1 
ATOM   1163 C  CB    . GLN A 1 150 ? -7.78800  -26.04300 14.91600  1.000 26.18472  ? 150 GLN A CB    1 
ATOM   1164 C  CG    . GLN A 1 150 ? -9.00400  -26.28700 15.79100  1.000 25.75835  ? 150 GLN A CG    1 
ATOM   1165 C  CD    . GLN A 1 150 ? -9.18700  -25.17800 16.79800  1.000 29.17192  ? 150 GLN A CD    1 
ATOM   1166 O  OE1   . GLN A 1 150 ? -9.11600  -23.99800 16.44700  1.000 28.68502  ? 150 GLN A OE1   1 
ATOM   1167 N  NE2   . GLN A 1 150 ? -9.40100  -25.54100 18.05900  1.000 30.20362  ? 150 GLN A NE2   1 
ATOM   1168 N  N     . SER A 1 151 ? -5.33400  -28.15800 15.22100  1.000 30.47207  ? 151 SER A N     1 
ATOM   1169 C  CA    . SER A 1 151 ? -4.82400  -29.47700 15.57600  1.000 30.49839  ? 151 SER A CA    1 
ATOM   1170 C  C     . SER A 1 151 ? -3.85800  -29.39200 16.75300  1.000 28.25339  ? 151 SER A C     1 
ATOM   1171 O  O     . SER A 1 151 ? -3.89500  -30.23900 17.65300  1.000 33.94354  ? 151 SER A O     1 
ATOM   1172 C  CB    . SER A 1 151 ? -4.14700  -30.11300 14.36300  1.000 32.04068  ? 151 SER A CB    1 
ATOM   1173 O  OG    . SER A 1 151 ? -4.05200  -31.51200 14.51800  1.000 42.86830  ? 151 SER A OG    1 
ATOM   1174 N  N     . ASP A 1 152 ? -3.02500  -28.36200 16.76000  1.000 29.38247  ? 152 ASP A N     1 
ATOM   1175 C  CA    . ASP A 1 152 ? -2.06400  -28.11500 17.86400  1.000 28.87451  ? 152 ASP A CA    1 
ATOM   1176 C  C     . ASP A 1 152 ? -2.85200  -27.82500 19.15000  1.000 28.80872  ? 152 ASP A C     1 
ATOM   1177 O  O     . ASP A 1 152 ? -2.47300  -28.31200 20.18200  1.000 30.96687  ? 152 ASP A O     1 
ATOM   1178 C  CB    . ASP A 1 152 ? -1.10500  -26.98100 17.52000  1.000 27.62173  ? 152 ASP A CB    1 
ATOM   1179 C  CG    . ASP A 1 152 ? 0.03500   -27.37900 16.59500  1.000 47.42674  ? 152 ASP A CG    1 
ATOM   1180 O  OD1   . ASP A 1 152 ? 0.22100   -28.57500 16.38800  1.000 44.46849  ? 152 ASP A OD1   1 
ATOM   1181 O  OD2   . ASP A 1 152 ? 0.73500   -26.48100 16.10500  1.000 43.32362  ? 152 ASP A OD2   1 
ATOM   1182 N  N     . ILE A 1 153 ? -3.92400  -27.05600 19.05800  1.000 24.09236  ? 153 ILE A N     1 
ATOM   1183 C  CA    . ILE A 1 153 ? -4.74800  -26.76500 20.22700  1.000 27.60331  ? 153 ILE A CA    1 
ATOM   1184 C  C     . ILE A 1 153 ? -5.31700  -28.05600 20.80300  1.000 30.59841  ? 153 ILE A C     1 
ATOM   1185 O  O     . ILE A 1 153 ? -5.28900  -28.27500 22.02100  1.000 27.86387  ? 153 ILE A O     1 
ATOM   1186 C  CB    . ILE A 1 153 ? -5.85200  -25.75700 19.85500  1.000 25.68203  ? 153 ILE A CB    1 
ATOM   1187 C  CG1   . ILE A 1 153 ? -5.22300  -24.39900 19.54500  1.000 28.02968  ? 153 ILE A CG1   1 
ATOM   1188 C  CG2   . ILE A 1 153 ? -6.88800  -25.62800 20.97600  1.000 27.76122  ? 153 ILE A CG2   1 
ATOM   1189 C  CD1   . ILE A 1 153 ? -6.18900  -23.38400 18.96400  1.000 30.03781  ? 153 ILE A CD1   1 
ATOM   1190 N  N     . ALA A 1 154 ? -5.80300  -28.95000 19.93700  1.000 30.27995  ? 154 ALA A N     1 
ATOM   1191 C  CA    . ALA A 1 154 ? -6.28900  -30.24300 20.41000  1.000 27.89808  ? 154 ALA A CA    1 
ATOM   1192 C  C     . ALA A 1 154 ? -5.18600  -31.02300 21.11800  1.000 26.39527  ? 154 ALA A C     1 
ATOM   1193 O  O     . ALA A 1 154 ? -5.42500  -31.63600 22.16400  1.000 27.71385  ? 154 ALA A O     1 
ATOM   1194 C  CB    . ALA A 1 154 ? -6.86000  -31.05700 19.24800  1.000 25.68729  ? 154 ALA A CB    1 
ATOM   1195 N  N     . ALA A 1 155 ? -3.96800  -31.00500 20.57100  1.000 24.48978  ? 155 ALA A N     1 
ATOM   1196 C  CA    . ALA A 1 155 ? -2.86000  -31.68600 21.23600  1.000 32.41441  ? 155 ALA A CA    1 
ATOM   1197 C  C     . ALA A 1 155 ? -2.54500  -31.04600 22.58200  1.000 30.95898  ? 155 ALA A C     1 
ATOM   1198 O  O     . ALA A 1 155 ? -2.27800  -31.74900 23.56500  1.000 28.72186  ? 155 ALA A O     1 
ATOM   1199 C  CB    . ALA A 1 155 ? -1.62200  -31.68900 20.33700  1.000 26.67425  ? 155 ALA A CB    1 
ATOM   1200 N  N     . LEU A 1 156 ? -2.57400  -29.71100 22.64700  1.000 27.94546  ? 156 LEU A N     1 
ATOM   1201 C  CA    . LEU A 1 156 ? -2.32900  -29.01200 23.90800  1.000 32.81446  ? 156 LEU A CA    1 
ATOM   1202 C  C     . LEU A 1 156 ? -3.33000  -29.44300 24.97800  1.000 31.84066  ? 156 LEU A C     1 
ATOM   1203 O  O     . LEU A 1 156 ? -2.95300  -29.73300 26.12200  1.000 24.18974  ? 156 LEU A O     1 
ATOM   1204 C  CB    . LEU A 1 156 ? -2.39000  -27.50100 23.67900  1.000 27.84281  ? 156 LEU A CB    1 
ATOM   1205 C  CG    . LEU A 1 156 ? -2.02700  -26.56600 24.83300  1.000 28.19022  ? 156 LEU A CG    1 
ATOM   1206 C  CD1   . LEU A 1 156 ? -0.57100  -26.74500 25.24900  1.000 26.46633  ? 156 LEU A CD1   1 
ATOM   1207 C  CD2   . LEU A 1 156 ? -2.29300  -25.12500 24.42800  1.000 29.48248  ? 156 LEU A CD2   1 
ATOM   1208 N  N     . HIS A 1 157 ? -4.61300  -29.50500 24.61300  1.000 32.33546  ? 157 HIS A N     1 
ATOM   1209 C  CA    . HIS A 1 157 ? -5.64900  -29.97800 25.53100  1.000 31.09847  ? 157 HIS A CA    1 
ATOM   1210 C  C     . HIS A 1 157 ? -5.41300  -31.42800 25.93600  1.000 36.20434  ? 157 HIS A C     1 
ATOM   1211 O  O     . HIS A 1 157 ? -5.53600  -31.79000 27.11300  1.000 34.67521  ? 157 HIS A O     1 
ATOM   1212 C  CB    . HIS A 1 157 ? -7.02100  -29.82400 24.87100  1.000 35.69112  ? 157 HIS A CB    1 
ATOM   1213 C  CG    . HIS A 1 157 ? -7.54400  -28.42100 24.86700  1.000 39.94689  ? 157 HIS A CG    1 
ATOM   1214 N  ND1   . HIS A 1 157 ? -7.84900  -27.74200 26.02500  1.000 44.65272  ? 157 HIS A ND1   1 
ATOM   1215 C  CD2   . HIS A 1 157 ? -7.75400  -27.54800 23.85400  1.000 53.94068  ? 157 HIS A CD2   1 
ATOM   1216 C  CE1   . HIS A 1 157 ? -8.28000  -26.53000 25.72300  1.000 39.99690  ? 157 HIS A CE1   1 
ATOM   1217 N  NE2   . HIS A 1 157 ? -8.22000  -26.38300 24.41300  1.000 46.35556  ? 157 HIS A NE2   1 
ATOM   1218 N  N     . HIS A 1 158 ? -5.10700  -32.28000 24.95600  1.000 33.94091  ? 158 HIS A N     1 
ATOM   1219 C  CA    . HIS A 1 158 ? -4.94800  -33.71100 25.20000  1.000 36.85442  ? 158 HIS A CA    1 
ATOM   1220 C  C     . HIS A 1 158 ? -3.86400  -33.99500 26.24100  1.000 30.81422  ? 158 HIS A C     1 
ATOM   1221 O  O     . HIS A 1 158 ? -4.05300  -34.82900 27.13200  1.000 32.71445  ? 158 HIS A O     1 
ATOM   1222 C  CB    . HIS A 1 158 ? -4.64300  -34.41800 23.87700  1.000 40.23904  ? 158 HIS A CB    1 
ATOM   1223 C  CG    . HIS A 1 158 ? -4.58400  -35.91100 23.98000  1.000 44.92907  ? 158 HIS A CG    1 
ATOM   1224 N  ND1   . HIS A 1 158 ? -3.43600  -36.63200 23.72900  1.000 50.60344  ? 158 HIS A ND1   1 
ATOM   1225 C  CD2   . HIS A 1 158 ? -5.53800  -36.82000 24.29000  1.000 43.52890  ? 158 HIS A CD2   1 
ATOM   1226 C  CE1   . HIS A 1 158 ? -3.68300  -37.92000 23.88700  1.000 45.75812  ? 158 HIS A CE1   1 
ATOM   1227 N  NE2   . HIS A 1 158 ? -4.95200  -38.06100 24.22700  1.000 40.85753  ? 158 HIS A NE2   1 
ATOM   1228 N  N     . PHE A 1 159 ? -2.69800  -33.34800 26.11000  1.000 27.88492  ? 159 PHE A N     1 
ATOM   1229 C  CA    . PHE A 1 159 ? -1.50300  -33.69900 26.87500  1.000 32.23808  ? 159 PHE A CA    1 
ATOM   1230 C  C     . PHE A 1 159 ? -1.22600  -32.82000 28.09900  1.000 36.12802  ? 159 PHE A C     1 
ATOM   1231 O  O     . PHE A 1 159 ? -0.39500  -33.20700 28.93000  1.000 31.16689  ? 159 PHE A O     1 
ATOM   1232 C  CB    . PHE A 1 159 ? -0.27200  -33.67200 25.95700  1.000 29.74041  ? 159 PHE A CB    1 
ATOM   1233 C  CG    . PHE A 1 159 ? -0.24900  -34.78500 24.94500  1.000 29.81936  ? 159 PHE A CG    1 
ATOM   1234 C  CD1   . PHE A 1 159 ? -0.16300  -36.10600 25.35300  1.000 36.80704  ? 159 PHE A CD1   1 
ATOM   1235 C  CD2   . PHE A 1 159 ? -0.32500  -34.51100 23.58900  1.000 34.62520  ? 159 PHE A CD2   1 
ATOM   1236 C  CE1   . PHE A 1 159 ? -0.15000  -37.13600 24.42500  1.000 42.19190  ? 159 PHE A CE1   1 
ATOM   1237 C  CE2   . PHE A 1 159 ? -0.31300  -35.53500 22.65700  1.000 36.72809  ? 159 PHE A CE2   1 
ATOM   1238 C  CZ    . PHE A 1 159 ? -0.22400  -36.85000 23.07600  1.000 39.70476  ? 159 PHE A CZ    1 
ATOM   1239 N  N     . TYR A 1 160 ? -1.86800  -31.65100 28.23400  1.000 30.10098  ? 160 TYR A N     1 
ATOM   1240 C  CA    . TYR A 1 160 ? -1.51100  -30.70400 29.28900  1.000 32.49863  ? 160 TYR A CA    1 
ATOM   1241 C  C     . TYR A 1 160 ? -2.71600  -30.23000 30.10400  1.000 36.27540  ? 160 TYR A C     1 
ATOM   1242 O  O     . TYR A 1 160 ? -2.62200  -29.21600 30.80500  1.000 32.58549  ? 160 TYR A O     1 
ATOM   1243 C  CB    . TYR A 1 160 ? -0.77400  -29.49800 28.69100  1.000 28.15601  ? 160 TYR A CB    1 
ATOM   1244 C  CG    . TYR A 1 160 ? 0.54600   -29.84100 28.02000  1.000 26.29526  ? 160 TYR A CG    1 
ATOM   1245 C  CD1   . TYR A 1 160 ? 0.59500   -30.24400 26.68500  1.000 27.43487  ? 160 TYR A CD1   1 
ATOM   1246 C  CD2   . TYR A 1 160 ? 1.74500   -29.76000 28.72200  1.000 27.22168  ? 160 TYR A CD2   1 
ATOM   1247 C  CE1   . TYR A 1 160 ? 1.80600   -30.55500 26.07100  1.000 25.83731  ? 160 TYR A CE1   1 
ATOM   1248 C  CE2   . TYR A 1 160 ? 2.96300   -30.07000 28.11700  1.000 27.01640  ? 160 TYR A CE2   1 
ATOM   1249 C  CZ    . TYR A 1 160 ? 2.98600   -30.46500 26.79600  1.000 28.01915  ? 160 TYR A CZ    1 
ATOM   1250 O  OH    . TYR A 1 160 ? 4.19200   -30.76400 26.20000  1.000 27.95072  ? 160 TYR A OH    1 
ATOM   1251 N  N     . SER A 1 161 ? -3.83200  -30.96200 30.05200  1.000 28.39551  ? 161 SER A N     1 
ATOM   1252 C  CA    . SER A 1 161 ? -5.06200  -30.54500 30.72700  1.000 37.16235  ? 161 SER A CA    1 
ATOM   1253 C  C     . SER A 1 161 ? -4.90700  -30.41600 32.24400  1.000 43.73682  ? 161 SER A C     1 
ATOM   1254 O  O     . SER A 1 161 ? -5.50700  -29.52400 32.85400  1.000 39.45999  ? 161 SER A O     1 
ATOM   1255 C  CB    . SER A 1 161 ? -6.19400  -31.51800 30.39400  1.000 36.28067  ? 161 SER A CB    1 
ATOM   1256 O  OG    . SER A 1 161 ? -6.77600  -31.18900 29.14500  1.000 59.85981  ? 161 SER A OG    1 
ATOM   1257 N  N     . LYS A 1 162 ? -4.12600  -31.29300 32.88100  1.000 41.32338  ? 162 LYS A N     1 
ATOM   1258 C  CA    . LYS A 1 162 ? -4.07300  -31.25900 34.34200  1.000 47.60044  ? 162 LYS A CA    1 
ATOM   1259 C  C     . LYS A 1 162 ? -3.23300  -30.13500 34.93200  1.000 39.32840  ? 162 LYS A C     1 
ATOM   1260 O  O     . LYS A 1 162 ? -3.44100  -29.79000 36.09800  1.000 34.19884  ? 162 LYS A O     1 
ATOM   1261 C  CB    . LYS A 1 162 ? -3.54300  -32.57700 34.91200  1.000 64.59985  ? 162 LYS A CB    1 
ATOM   1262 C  CG    . LYS A 1 162 ? -4.47600  -33.76600 34.82400  1.000 58.24646  ? 162 LYS A CG    1 
ATOM   1263 C  CD    . LYS A 1 162 ? -4.00000  -34.81100 35.82000  1.000 65.38152  ? 162 LYS A CD    1 
ATOM   1264 C  CE    . LYS A 1 162 ? -5.01200  -35.91400 36.04100  1.000 74.91688  ? 162 LYS A CE    1 
ATOM   1265 N  NZ    . LYS A 1 162 ? -4.61200  -36.75100 37.21100  1.000 66.32637  ? 162 LYS A NZ    1 
ATOM   1266 N  N     . HIS A 1 163 ? -2.30600  -29.54600 34.18400  1.000 36.93864  ? 163 HIS A N     1 
ATOM   1267 C  CA    . HIS A 1 163 ? -1.43900  -28.51600 34.74000  1.000 42.71565  ? 163 HIS A CA    1 
ATOM   1268 C  C     . HIS A 1 163 ? -1.73200  -27.10000 34.26700  1.000 45.31596  ? 163 HIS A C     1 
ATOM   1269 O  O     . HIS A 1 163 ? -1.25300  -26.15300 34.89500  1.000 51.27194  ? 163 HIS A O     1 
ATOM   1270 C  CB    . HIS A 1 163 ? 0.03500   -28.85000 34.46900  1.000 45.05803  ? 163 HIS A CB    1 
ATOM   1271 C  CG    . HIS A 1 163 ? 0.50200   -30.09100 35.16400  1.000 50.69555  ? 163 HIS A CG    1 
ATOM   1272 N  ND1   . HIS A 1 163 ? 1.02400   -30.07300 36.44100  1.000 53.83803  ? 163 HIS A ND1   1 
ATOM   1273 C  CD2   . HIS A 1 163 ? 0.49100   -31.38900 34.78000  1.000 52.22468  ? 163 HIS A CD2   1 
ATOM   1274 C  CE1   . HIS A 1 163 ? 1.33400   -31.30500 36.80400  1.000 52.27206  ? 163 HIS A CE1   1 
ATOM   1275 N  NE2   . HIS A 1 163 ? 1.01900   -32.12300 35.81400  1.000 53.51694  ? 163 HIS A NE2   1 
ATOM   1276 N  N     . LEU A 1 164 ? -2.49200  -26.92100 33.19200  1.000 44.76589  ? 164 LEU A N     1 
ATOM   1277 C  CA    . LEU A 1 164 ? -2.68900  -25.60800 32.60100  1.000 34.78049  ? 164 LEU A CA    1 
ATOM   1278 C  C     . LEU A 1 164 ? -4.16100  -25.23700 32.58400  1.000 34.04356  ? 164 LEU A C     1 
ATOM   1279 O  O     . LEU A 1 164 ? -5.03100  -26.09900 32.42800  1.000 37.23604  ? 164 LEU A O     1 
ATOM   1280 C  CB    . LEU A 1 164 ? -2.16200  -25.56600 31.16100  1.000 42.63669  ? 164 LEU A CB    1 
ATOM   1281 C  CG    . LEU A 1 164 ? -0.65500  -25.59900 30.93100  1.000 36.38331  ? 164 LEU A CG    1 
ATOM   1282 C  CD1   . LEU A 1 164 ? -0.36600  -25.82200 29.45500  1.000 43.01832  ? 164 LEU A CD1   1 
ATOM   1283 C  CD2   . LEU A 1 164 ? -0.03200  -24.30500 31.41100  1.000 38.01508  ? 164 LEU A CD2   1 
ATOM   1284 N  N     . GLU A 1 165 ? -4.43200  -23.95500 32.80000  1.000 46.90562  ? 165 GLU A N     1 
ATOM   1285 C  CA    . GLU A 1 165 ? -5.76200  -23.39700 32.60100  1.000 66.59746  ? 165 GLU A CA    1 
ATOM   1286 C  C     . GLU A 1 165 ? -5.72400  -22.61500 31.29100  1.000 43.10517  ? 165 GLU A C     1 
ATOM   1287 O  O     . GLU A 1 165 ? -4.88900  -21.72000 31.11900  1.000 50.70345  ? 165 GLU A O     1 
ATOM   1288 C  CB    . GLU A 1 165 ? -6.18900  -22.51500 33.77600  1.000 69.22409  ? 165 GLU A CB    1 
ATOM   1289 C  CG    . GLU A 1 165 ? -5.18000  -21.45800 34.18400  1.000 87.78684  ? 165 GLU A CG    1 
ATOM   1290 C  CD    . GLU A 1 165 ? -5.79400  -20.39300 35.06700  1.000 92.97431  ? 165 GLU A CD    1 
ATOM   1291 O  OE1   . GLU A 1 165 ? -6.67800  -20.73100 35.88400  1.000 87.87369  ? 165 GLU A OE1   1 
ATOM   1292 O  OE2   . GLU A 1 165 ? -5.40200  -19.21400 34.93200  1.000 76.76447  ? 165 GLU A OE2   1 
ATOM   1293 N  N     . PHE A 1 166 ? -6.58300  -22.99100 30.35200  1.000 40.06796  ? 166 PHE A N     1 
ATOM   1294 C  CA    . PHE A 1 166 ? -6.54600  -22.45100 28.99500  1.000 43.13938  ? 166 PHE A CA    1 
ATOM   1295 C  C     . PHE A 1 166 ? -7.42100  -21.20900 28.84700  1.000 38.55989  ? 166 PHE A C     1 
ATOM   1296 O  O     . PHE A 1 166 ? -8.52600  -21.15900 29.39200  1.000 43.81841  ? 166 PHE A O     1 
ATOM   1297 C  CB    . PHE A 1 166 ? -6.98800  -23.50700 27.99100  1.000 38.18879  ? 166 PHE A CB    1 
ATOM   1298 C  CG    . PHE A 1 166 ? -6.20700  -24.78500 28.07300  1.000 38.33618  ? 166 PHE A CG    1 
ATOM   1299 C  CD1   . PHE A 1 166 ? -4.86700  -24.80600 27.72400  1.000 36.09643  ? 166 PHE A CD1   1 
ATOM   1300 C  CD2   . PHE A 1 166 ? -6.79200  -25.94900 28.53500  1.000 43.52101  ? 166 PHE A CD2   1 
ATOM   1301 C  CE1   . PHE A 1 166 ? -4.13700  -25.97300 27.79500  1.000 43.47100  ? 166 PHE A CE1   1 
ATOM   1302 C  CE2   . PHE A 1 166 ? -6.06300  -27.12300 28.61500  1.000 48.37948  ? 166 PHE A CE2   1 
ATOM   1303 C  CZ    . PHE A 1 166 ? -4.73400  -27.13300 28.24300  1.000 40.71541  ? 166 PHE A CZ    1 
ATOM   1304 N  N     . PRO A 1 167 ? -6.95300  -20.20700 28.08500  1.000 39.29945  ? 167 PRO A N     1 
ATOM   1305 C  CA    . PRO A 1 167 ? -7.86500  -19.15500 27.61000  1.000 39.43104  ? 167 PRO A CA    1 
ATOM   1306 C  C     . PRO A 1 167 ? -8.86900  -19.69900 26.60500  1.000 39.48631  ? 167 PRO A C     1 
ATOM   1307 O  O     . PRO A 1 167 ? -8.85700  -20.89600 26.30500  1.000 35.90167  ? 167 PRO A O     1 
ATOM   1308 C  CB    . PRO A 1 167 ? -6.91800  -18.13300 26.96800  1.000 38.12036  ? 167 PRO A CB    1 
ATOM   1309 C  CG    . PRO A 1 167 ? -5.72600  -18.93300 26.55900  1.000 38.15721  ? 167 PRO A CG    1 
ATOM   1310 C  CD    . PRO A 1 167 ? -5.57400  -20.00600 27.60600  1.000 43.66050  ? 167 PRO A CD    1 
ATOM   1311 N  N     . ASP A 1 168 ? -9.73100  -18.84000 26.06600  1.000 38.12036  ? 168 ASP A N     1 
ATOM   1312 C  CA    . ASP A 1 168 ? -10.68100 -19.28900 25.05800  1.000 41.31811  ? 168 ASP A CA    1 
ATOM   1313 C  C     . ASP A 1 168 ? -9.94400  -19.68700 23.77900  1.000 36.19908  ? 168 ASP A C     1 
ATOM   1314 O  O     . ASP A 1 168 ? -8.73800  -19.47800 23.63000  1.000 31.47746  ? 168 ASP A O     1 
ATOM   1315 C  CB    . ASP A 1 168 ? -11.72700 -18.20900 24.76400  1.000 39.22576  ? 168 ASP A CB    1 
ATOM   1316 C  CG    . ASP A 1 168 ? -11.10900 -16.86600 24.42800  1.000 51.41669  ? 168 ASP A CG    1 
ATOM   1317 O  OD1   . ASP A 1 168 ? -9.88600  -16.70200 24.62000  1.000 96.39577  ? 168 ASP A OD1   1 
ATOM   1318 O  OD2   . ASP A 1 168 ? -11.84900 -15.97100 23.96600  1.000 67.26333  ? 168 ASP A OD2   1 
ATOM   1319 N  N     . ASN A 1 169 ? -10.67900 -20.32100 22.86300  1.000 35.07789  ? 169 ASN A N     1 
ATOM   1320 C  CA    . ASN A 1 169 ? -10.04700 -20.85200 21.66100  1.000 33.19872  ? 169 ASN A CA    1 
ATOM   1321 C  C     . ASN A 1 169 ? -9.41200  -19.74200 20.82600  1.000 32.76182  ? 169 ASN A C     1 
ATOM   1322 O  O     . ASN A 1 169 ? -8.32300  -19.92400 20.26500  1.000 29.24561  ? 169 ASN A O     1 
ATOM   1323 C  CB    . ASN A 1 169 ? -11.06200 -21.64500 20.84100  1.000 34.59099  ? 169 ASN A CB    1 
ATOM   1324 C  CG    . ASN A 1 169 ? -10.40300 -22.48200 19.76900  1.000 32.52758  ? 169 ASN A CG    1 
ATOM   1325 O  OD1   . ASN A 1 169 ? -9.86200  -23.55200 20.05900  1.000 32.33282  ? 169 ASN A OD1   1 
ATOM   1326 N  ND2   . ASN A 1 169 ? -10.43100 -22.00100 18.52300  1.000 34.39886  ? 169 ASN A ND2   1 
ATOM   1327 N  N     . ASP A 1 170 ? -10.08300 -18.58700 20.72700  1.000 29.46143  ? 170 ASP A N     1 
ATOM   1328 C  CA    . ASP A 1 170 ? -9.54700  -17.45900 19.96400  1.000 36.34383  ? 170 ASP A CA    1 
ATOM   1329 C  C     . ASP A 1 170 ? -8.17400  -17.03700 20.46100  1.000 36.02800  ? 170 ASP A C     1 
ATOM   1330 O  O     . ASP A 1 170 ? -7.28000  -16.74200 19.65800  1.000 32.40125  ? 170 ASP A O     1 
ATOM   1331 C  CB    . ASP A 1 170 ? -10.50500 -16.27000 20.02800  1.000 41.77080  ? 170 ASP A CB    1 
ATOM   1332 C  CG    . ASP A 1 170 ? -11.63500 -16.37700 19.03400  1.000 54.40652  ? 170 ASP A CG    1 
ATOM   1333 O  OD1   . ASP A 1 170 ? -11.69600 -17.39500 18.31100  1.000 55.73037  ? 170 ASP A OD1   1 
ATOM   1334 O  OD2   . ASP A 1 170 ? -12.46100 -15.44200 18.97100  1.000 59.85718  ? 170 ASP A OD2   1 
ATOM   1335 N  N     . SER A 1 171 ? -7.98900  -16.99600 21.78000  1.000 31.68538  ? 171 SER A N     1 
ATOM   1336 C  CA    . SER A 1 171 ? -6.70200  -16.57800 22.32400  1.000 34.01460  ? 171 SER A CA    1 
ATOM   1337 C  C     . SER A 1 171 ? -5.62300  -17.60500 22.02100  1.000 29.02190  ? 171 SER A C     1 
ATOM   1338 O  O     . SER A 1 171 ? -4.46600  -17.24400 21.76100  1.000 26.47423  ? 171 SER A O     1 
ATOM   1339 C  CB    . SER A 1 171 ? -6.80800  -16.34600 23.83100  1.000 33.76984  ? 171 SER A CB    1 
ATOM   1340 O  OG    . SER A 1 171 ? -7.60500  -15.21100 24.12000  1.000 45.03698  ? 171 SER A OG    1 
ATOM   1341 N  N     . LEU A 1 172 ? -5.97800  -18.89200 22.06600  1.000 25.04511  ? 172 LEU A N     1 
ATOM   1342 C  CA    . LEU A 1 172 ? -5.00800  -19.93900 21.75800  1.000 28.84556  ? 172 LEU A CA    1 
ATOM   1343 C  C     . LEU A 1 172 ? -4.59100  -19.89200 20.29000  1.000 25.89784  ? 172 LEU A C     1 
ATOM   1344 O  O     . LEU A 1 172 ? -3.42000  -20.12600 19.96400  1.000 29.16665  ? 172 LEU A O     1 
ATOM   1345 C  CB    . LEU A 1 172 ? -5.59200  -21.30500 22.11200  1.000 29.46406  ? 172 LEU A CB    1 
ATOM   1346 C  CG    . LEU A 1 172 ? -5.54300  -21.65100 23.60500  1.000 31.92225  ? 172 LEU A CG    1 
ATOM   1347 C  CD1   . LEU A 1 172 ? -6.16500  -23.01300 23.85400  1.000 41.22336  ? 172 LEU A CD1   1 
ATOM   1348 C  CD2   . LEU A 1 172 ? -4.11600  -21.58200 24.16600  1.000 36.63597  ? 172 LEU A CD2   1 
ATOM   1349 N  N     . VAL A 1 173 ? -5.53800  -19.61200 19.38900  1.000 24.49241  ? 173 VAL A N     1 
ATOM   1350 C  CA    . VAL A 1 173 ? -5.19100  -19.47000 17.97800  1.000 24.21869  ? 173 VAL A CA    1 
ATOM   1351 C  C     . VAL A 1 173 ? -4.17600  -18.34700 17.80500  1.000 25.08985  ? 173 VAL A C     1 
ATOM   1352 O  O     . VAL A 1 173 ? -3.14500  -18.51400 17.14100  1.000 26.45054  ? 173 VAL A O     1 
ATOM   1353 C  CB    . VAL A 1 173 ? -6.45300  -19.23000 17.12900  1.000 27.17694  ? 173 VAL A CB    1 
ATOM   1354 C  CG1   . VAL A 1 173 ? -6.07300  -18.88200 15.69400  1.000 27.47171  ? 173 VAL A CG1   1 
ATOM   1355 C  CG2   . VAL A 1 173 ? -7.35100  -20.45800 17.15100  1.000 26.96902  ? 173 VAL A CG2   1 
ATOM   1356 N  N     . VAL A 1 174 ? -4.43600  -17.19700 18.43300  1.000 24.52662  ? 174 VAL A N     1 
ATOM   1357 C  CA    . VAL A 1 174 ? -3.52400  -16.06100 18.31900  1.000 25.91890  ? 174 VAL A CA    1 
ATOM   1358 C  C     . VAL A 1 174 ? -2.14300  -16.42700 18.85400  1.000 23.42386  ? 174 VAL A C     1 
ATOM   1359 O  O     . VAL A 1 174 ? -1.11900  -16.14300 18.22100  1.000 21.67892  ? 174 VAL A O     1 
ATOM   1360 C  CB    . VAL A 1 174 ? -4.10600  -14.83100 19.04100  1.000 31.28533  ? 174 VAL A CB    1 
ATOM   1361 C  CG1   . VAL A 1 174 ? -3.05900  -13.72900 19.15000  1.000 32.58022  ? 174 VAL A CG1   1 
ATOM   1362 C  CG2   . VAL A 1 174 ? -5.34900  -14.32200 18.30700  1.000 32.74866  ? 174 VAL A CG2   1 
ATOM   1363 N  N     . LEU A 1 175 ? -2.09500  -17.07300 20.02400  1.000 25.22934  ? 175 LEU A N     1 
ATOM   1364 C  CA    . LEU A 1 175 ? -0.81500  -17.41700 20.64500  1.000 26.42159  ? 175 LEU A CA    1 
ATOM   1365 C  C     . LEU A 1 175 ? 0.01700   -18.33500 19.75600  1.000 24.21606  ? 175 LEU A C     1 
ATOM   1366 O  O     . LEU A 1 175 ? 1.21600   -18.10500 19.56400  1.000 23.26332  ? 175 LEU A O     1 
ATOM   1367 C  CB    . LEU A 1 175 ? -1.04400  -18.06800 22.01000  1.000 27.71911  ? 175 LEU A CB    1 
ATOM   1368 C  CG    . LEU A 1 175 ? 0.23700   -18.42000 22.77000  1.000 25.97943  ? 175 LEU A CG    1 
ATOM   1369 C  CD1   . LEU A 1 175 ? 1.09100   -17.18000 22.96600  1.000 30.57209  ? 175 LEU A CD1   1 
ATOM   1370 C  CD2   . LEU A 1 175 ? -0.08100  -19.05500 24.12300  1.000 28.23760  ? 175 LEU A CD2   1 
ATOM   1371 N  N     . PHE A 1 176 ? -0.59500  -19.40900 19.24000  1.000 25.71887  ? 176 PHE A N     1 
ATOM   1372 C  CA    . PHE A 1 176 ? 0.11600   -20.30600 18.33300  1.000 25.01879  ? 176 PHE A CA    1 
ATOM   1373 C  C     . PHE A 1 176 ? 0.61100   -19.56800 17.09400  1.000 24.65559  ? 176 PHE A C     1 
ATOM   1374 O  O     . PHE A 1 176 ? 1.73900   -19.79100 16.63800  1.000 27.97967  ? 176 PHE A O     1 
ATOM   1375 C  CB    . PHE A 1 176 ? -0.78800  -21.47800 17.93900  1.000 25.34514  ? 176 PHE A CB    1 
ATOM   1376 C  CG    . PHE A 1 176 ? -0.71500  -22.64900 18.88300  1.000 24.95036  ? 176 PHE A CG    1 
ATOM   1377 C  CD1   . PHE A 1 176 ? 0.41600   -23.44700 18.93200  1.000 26.89533  ? 176 PHE A CD1   1 
ATOM   1378 C  CD2   . PHE A 1 176 ? -1.78700  -22.96300 19.71500  1.000 26.87954  ? 176 PHE A CD2   1 
ATOM   1379 C  CE1   . PHE A 1 176 ? 0.48700   -24.53400 19.79900  1.000 29.42721  ? 176 PHE A CE1   1 
ATOM   1380 C  CE2   . PHE A 1 176 ? -1.72200  -24.04900 20.58400  1.000 29.52722  ? 176 PHE A CE2   1 
ATOM   1381 C  CZ    . PHE A 1 176 ? -0.58300  -24.83300 20.62700  1.000 26.56898  ? 176 PHE A CZ    1 
ATOM   1382 N  N     . ALA A 1 177 ? -0.21800  -18.68000 16.53500  1.000 26.40053  ? 177 ALA A N     1 
ATOM   1383 C  CA    . ALA A 1 177 ? 0.21300   -17.88200 15.38800  1.000 23.46597  ? 177 ALA A CA    1 
ATOM   1384 C  C     . ALA A 1 177 ? 1.37600   -16.96500 15.75600  1.000 29.32983  ? 177 ALA A C     1 
ATOM   1385 O  O     . ALA A 1 177 ? 2.31500   -16.78700 14.96900  1.000 23.51861  ? 177 ALA A O     1 
ATOM   1386 C  CB    . ALA A 1 177 ? -0.96200  -17.07300 14.84300  1.000 25.29514  ? 177 ALA A CB    1 
ATOM   1387 N  N     . GLN A 1 178 ? 1.33200   -16.37100 16.95200  1.000 19.97608  ? 178 GLN A N     1 
ATOM   1388 C  CA    . GLN A 1 178 ? 2.44600   -15.53800 17.39900  1.000 20.77354  ? 178 GLN A CA    1 
ATOM   1389 C  C     . GLN A 1 178 ? 3.72100   -16.35600 17.53800  1.000 22.30004  ? 178 GLN A C     1 
ATOM   1390 O  O     . GLN A 1 178 ? 4.81400   -15.87900 17.19900  1.000 23.50282  ? 178 GLN A O     1 
ATOM   1391 C  CB    . GLN A 1 178 ? 2.09600   -14.85900 18.72300  1.000 27.18221  ? 178 GLN A CB    1 
ATOM   1392 C  CG    . GLN A 1 178 ? 1.08600   -13.73700 18.60200  1.000 21.07884  ? 178 GLN A CG    1 
ATOM   1393 C  CD    . GLN A 1 178 ? 0.57000   -13.30600 19.96000  1.000 26.82427  ? 178 GLN A CD    1 
ATOM   1394 O  OE1   . GLN A 1 178 ? 0.35200   -14.14000 20.83600  1.000 26.03470  ? 178 GLN A OE1   1 
ATOM   1395 N  NE2   . GLN A 1 178 ? 0.39300   -12.00500 20.15000  1.000 27.01903  ? 178 GLN A NE2   1 
ATOM   1396 N  N     . VAL A 1 179 ? 3.60300   -17.58600 18.04700  1.000 21.04200  ? 179 VAL A N     1 
ATOM   1397 C  CA    . VAL A 1 179 ? 4.76600   -18.46000 18.19300  1.000 22.31057  ? 179 VAL A CA    1 
ATOM   1398 C  C     . VAL A 1 179 ? 5.35600   -18.80800 16.83000  1.000 22.06054  ? 179 VAL A C     1 
ATOM   1399 O  O     . VAL A 1 179 ? 6.57700   -18.76200 16.63700  1.000 23.67126  ? 179 VAL A O     1 
ATOM   1400 C  CB    . VAL A 1 179 ? 4.38800   -19.73100 18.97400  1.000 21.93684  ? 179 VAL A CB    1 
ATOM   1401 C  CG1   . VAL A 1 179 ? 5.53100   -20.73600 18.92800  1.000 24.92667  ? 179 VAL A CG1   1 
ATOM   1402 C  CG2   . VAL A 1 179 ? 4.04500   -19.38600 20.41800  1.000 20.59984  ? 179 VAL A CG2   1 
ATOM   1403 N  N     . ASN A 1 180 ? 4.50000   -19.18100 15.86900  1.000 30.34574  ? 180 ASN A N     1 
ATOM   1404 C  CA    . ASN A 1 180 ? 4.98700   -19.49800 14.52900  1.000 32.65918  ? 180 ASN A CA    1 
ATOM   1405 C  C     . ASN A 1 180 ? 5.72200   -18.32000 13.91200  1.000 27.99546  ? 180 ASN A C     1 
ATOM   1406 O  O     . ASN A 1 180 ? 6.65600   -18.50900 13.12300  1.000 29.25351  ? 180 ASN A O     1 
ATOM   1407 C  CB    . ASN A 1 180 ? 3.83000   -19.91700 13.62300  1.000 26.45844  ? 180 ASN A CB    1 
ATOM   1408 C  CG    . ASN A 1 180 ? 3.24000   -21.25000 14.01400  1.000 31.76433  ? 180 ASN A CG    1 
ATOM   1409 O  OD1   . ASN A 1 180 ? 3.81500   -21.98800 14.81200  1.000 41.12598  ? 180 ASN A OD1   1 
ATOM   1410 N  ND2   . ASN A 1 180 ? 2.08300   -21.56800 13.45500  1.000 42.73144  ? 180 ASN A ND2   1 
ATOM   1411 N  N     . CYS A 1 181 ? 5.29100   -17.10200 14.23700  1.000 26.57161  ? 181 CYS A N     1 
ATOM   1412 C  CA    . CYS A 1 181 ? 5.85300   -15.89400 13.65200  1.000 29.06138  ? 181 CYS A CA    1 
ATOM   1413 C  C     . CYS A 1 181 ? 7.12000   -15.43200 14.36400  1.000 31.69327  ? 181 CYS A C     1 
ATOM   1414 O  O     . CYS A 1 181 ? 8.00600   -14.86000 13.72500  1.000 32.69076  ? 181 CYS A O     1 
ATOM   1415 C  CB    . CYS A 1 181 ? 4.80400   -14.78500 13.68300  1.000 30.89844  ? 181 CYS A CB    1 
ATOM   1416 S  SG    . CYS A 1 181 ? 5.31500   -13.23200 12.94400  1.000 46.20291  ? 181 CYS A SG    1 
ATOM   1417 N  N     . ASN A 1 182 ? 7.21600   -15.63900 15.67800  1.000 22.41585  ? 182 ASN A N     1 
ATOM   1418 C  CA    . ASN A 1 182 ? 8.26700   -15.03100 16.48100  1.000 24.55031  ? 182 ASN A CA    1 
ATOM   1419 C  C     . ASN A 1 182 ? 9.17600   -16.01500 17.20600  1.000 24.96352  ? 182 ASN A C     1 
ATOM   1420 O  O     . ASN A 1 182 ? 10.18300  -15.58100 17.77500  1.000 28.15338  ? 182 ASN A O     1 
ATOM   1421 C  CB    . ASN A 1 182 ? 7.65000   -14.08500 17.52600  1.000 32.12754  ? 182 ASN A CB    1 
ATOM   1422 C  CG    . ASN A 1 182 ? 6.89100   -12.93600 16.89600  1.000 33.14345  ? 182 ASN A CG    1 
ATOM   1423 O  OD1   . ASN A 1 182 ? 7.49100   -11.96400 16.44600  1.000 38.69938  ? 182 ASN A OD1   1 
ATOM   1424 N  ND2   . ASN A 1 182 ? 5.56300   -13.04700 16.84800  1.000 35.49899  ? 182 ASN A ND2   1 
ATOM   1425 N  N     . GLY A 1 183 ? 8.86700   -17.31000 17.20200  1.000 27.43750  ? 183 GLY A N     1 
ATOM   1426 C  CA    . GLY A 1 183 ? 9.70500   -18.27100 17.90300  1.000 35.32266  ? 183 GLY A CA    1 
ATOM   1427 C  C     . GLY A 1 183 ? 11.04900  -18.48900 17.22900  1.000 25.88731  ? 183 GLY A C     1 
ATOM   1428 O  O     . GLY A 1 183 ? 11.21600  -18.27400 16.03000  1.000 29.31141  ? 183 GLY A O     1 
ATOM   1429 N  N     . PHE A 1 184 ? 12.02500  -18.92100 18.02900  1.000 24.80297  ? 184 PHE A N     1 
ATOM   1430 C  CA    . PHE A 1 184 ? 13.38100  -19.18800 17.57100  1.000 24.36608  ? 184 PHE A CA    1 
ATOM   1431 C  C     . PHE A 1 184 ? 13.74400  -20.64700 17.80100  1.000 26.31631  ? 184 PHE A C     1 
ATOM   1432 O  O     . PHE A 1 184 ? 13.29300  -21.27600 18.76500  1.000 25.32672  ? 184 PHE A O     1 
ATOM   1433 C  CB    . PHE A 1 184 ? 14.40900  -18.30900 18.30200  1.000 30.99845  ? 184 PHE A CB    1 
ATOM   1434 C  CG    . PHE A 1 184 ? 14.38700  -16.87500 17.87900  1.000 26.44264  ? 184 PHE A CG    1 
ATOM   1435 C  CD1   . PHE A 1 184 ? 13.43400  -16.01000 18.38100  1.000 31.03267  ? 184 PHE A CD1   1 
ATOM   1436 C  CD2   . PHE A 1 184 ? 15.32000  -16.38900 16.98700  1.000 30.99845  ? 184 PHE A CD2   1 
ATOM   1437 C  CE1   . PHE A 1 184 ? 13.40900  -14.69100 17.99200  1.000 35.45425  ? 184 PHE A CE1   1 
ATOM   1438 C  CE2   . PHE A 1 184 ? 15.29400  -15.07200 16.59100  1.000 31.47746  ? 184 PHE A CE2   1 
ATOM   1439 C  CZ    . PHE A 1 184 ? 14.34000  -14.22300 17.09300  1.000 43.30519  ? 184 PHE A CZ    1 
ATOM   1440 N  N     . THR A 1 185 ? 14.58300  -21.17400 16.91700  1.000 26.80585  ? 185 THR A N     1 
ATOM   1441 C  CA    . THR A 1 185 ? 15.22300  -22.46400 17.12600  1.000 32.99869  ? 185 THR A CA    1 
ATOM   1442 C  C     . THR A 1 185 ? 16.61900  -22.23100 17.68100  1.000 25.55570  ? 185 THR A C     1 
ATOM   1443 O  O     . THR A 1 185 ? 17.33400  -21.33200 17.23000  1.000 31.01951  ? 185 THR A O     1 
ATOM   1444 C  CB    . THR A 1 185 ? 15.31800  -23.27400 15.83200  1.000 28.64554  ? 185 THR A CB    1 
ATOM   1445 O  OG1   . THR A 1 185 ? 15.99200  -22.49700 14.83700  1.000 48.95587  ? 185 THR A OG1   1 
ATOM   1446 C  CG2   . THR A 1 185 ? 13.93100  -23.63400 15.32600  1.000 37.59924  ? 185 THR A CG2   1 
ATOM   1447 N  N     . ILE A 1 186 ? 16.99200  -23.02400 18.67900  1.000 29.61408  ? 186 ILE A N     1 
ATOM   1448 C  CA    . ILE A 1 186 ? 18.33000  -22.99100 19.25200  1.000 26.79005  ? 186 ILE A CA    1 
ATOM   1449 C  C     . ILE A 1 186 ? 19.12700  -24.15000 18.66200  1.000 32.94342  ? 186 ILE A C     1 
ATOM   1450 O  O     . ILE A 1 186 ? 18.64000  -25.28700 18.62700  1.000 24.77665  ? 186 ILE A O     1 
ATOM   1451 C  CB    . ILE A 1 186 ? 18.27300  -23.06600 20.79000  1.000 31.34060  ? 186 ILE A CB    1 
ATOM   1452 C  CG1   . ILE A 1 186 ? 17.54200  -21.84400 21.35400  1.000 31.79592  ? 186 ILE A CG1   1 
ATOM   1453 C  CG2   . ILE A 1 186 ? 19.67900  -23.16800 21.38300  1.000 37.62293  ? 186 ILE A CG2   1 
ATOM   1454 C  CD1   . ILE A 1 186 ? 17.25600  -21.91300 22.85100  1.000 29.87727  ? 186 ILE A CD1   1 
ATOM   1455 N  N     . GLU A 1 187 ? 20.33200  -23.85700 18.16000  1.000 33.06712  ? 187 GLU A N     1 
ATOM   1456 C  CA    . GLU A 1 187 ? 21.23200  -24.85200 17.59100  1.000 29.56407  ? 187 GLU A CA    1 
ATOM   1457 C  C     . GLU A 1 187 ? 22.56100  -24.84100 18.33600  1.000 27.43224  ? 187 GLU A C     1 
ATOM   1458 O  O     . GLU A 1 187 ? 22.96200  -23.81900 18.90200  1.000 26.10576  ? 187 GLU A O     1 
ATOM   1459 C  CB    . GLU A 1 187 ? 21.50600  -24.60800 16.09300  1.000 32.52495  ? 187 GLU A CB    1 
ATOM   1460 C  CG    . GLU A 1 187 ? 20.29800  -24.74700 15.18400  1.000 40.77068  ? 187 GLU A CG    1 
ATOM   1461 C  CD    . GLU A 1 187 ? 19.52300  -23.45300 15.03500  1.000 62.62856  ? 187 GLU A CD    1 
ATOM   1462 O  OE1   . GLU A 1 187 ? 20.09700  -22.37600 15.31000  1.000 62.25483  ? 187 GLU A OE1   1 
ATOM   1463 O  OE2   . GLU A 1 187 ? 18.33100  -23.51500 14.66600  1.000 68.16870  ? 187 GLU A OE2   1 
ATOM   1464 N  N     . ASP A 1 188 ? 23.25100  -25.98400 18.32000  1.000 30.02728  ? 188 ASP A N     1 
ATOM   1465 C  CA    . ASP A 1 188 ? 24.57900  -26.08100 18.91600  1.000 30.55893  ? 188 ASP A CA    1 
ATOM   1466 C  C     . ASP A 1 188 ? 25.63900  -25.60700 17.91600  1.000 32.99343  ? 188 ASP A C     1 
ATOM   1467 O  O     . ASP A 1 188 ? 25.32800  -25.09200 16.84000  1.000 30.28784  ? 188 ASP A O     1 
ATOM   1468 C  CB    . ASP A 1 188 ? 24.84400  -27.49900 19.43100  1.000 27.59541  ? 188 ASP A CB    1 
ATOM   1469 C  CG    . ASP A 1 188 ? 24.94200  -28.54700 18.31600  1.000 36.47806  ? 188 ASP A CG    1 
ATOM   1470 O  OD1   . ASP A 1 188 ? 24.93100  -28.19900 17.10900  1.000 34.10409  ? 188 ASP A OD1   1 
ATOM   1471 O  OD2   . ASP A 1 188 ? 25.05900  -29.74100 18.66200  1.000 38.88098  ? 188 ASP A OD2   1 
ATOM   1472 N  N     . GLU A 1 189 ? 26.91600  -25.76600 18.27800  1.000 27.95072  ? 189 GLU A N     1 
ATOM   1473 C  CA    . GLU A 1 189 ? 28.00700  -25.25400 17.45400  1.000 31.99857  ? 189 GLU A CA    1 
ATOM   1474 C  C     . GLU A 1 189 ? 28.09000  -25.92800 16.08500  1.000 26.06628  ? 189 GLU A C     1 
ATOM   1475 O  O     . GLU A 1 189 ? 28.71300  -25.37400 15.17500  1.000 32.37757  ? 189 GLU A O     1 
ATOM   1476 C  CB    . GLU A 1 189 ? 29.33000  -25.39800 18.21000  1.000 28.46920  ? 189 GLU A CB    1 
ATOM   1477 C  CG    . GLU A 1 189 ? 29.86800  -26.82100 18.29700  1.000 40.26799  ? 189 GLU A CG    1 
ATOM   1478 C  CD    . GLU A 1 189 ? 29.20100  -27.66400 19.36600  1.000 40.61013  ? 189 GLU A CD    1 
ATOM   1479 O  OE1   . GLU A 1 189 ? 28.08800  -27.31100 19.81400  1.000 41.69710  ? 189 GLU A OE1   1 
ATOM   1480 O  OE2   . GLU A 1 189 ? 29.79800  -28.69100 19.75500  1.000 40.91280  ? 189 GLU A OE2   1 
ATOM   1481 N  N     . GLU A 1 190 ? 27.49100  -27.10800 15.91100  1.000 32.03279  ? 190 GLU A N     1 
ATOM   1482 C  CA    . GLU A 1 190 ? 27.44100  -27.77200 14.61400  1.000 31.08267  ? 190 GLU A CA    1 
ATOM   1483 C  C     . GLU A 1 190 ? 26.11900  -27.52400 13.89300  1.000 30.71158  ? 190 GLU A C     1 
ATOM   1484 O  O     . GLU A 1 190 ? 25.80700  -28.22700 12.92500  1.000 33.92512  ? 190 GLU A O     1 
ATOM   1485 C  CB    . GLU A 1 190 ? 27.67900  -29.27700 14.77100  1.000 36.57017  ? 190 GLU A CB    1 
ATOM   1486 C  CG    . GLU A 1 190 ? 29.12100  -29.66000 15.10700  1.000 42.56300  ? 190 GLU A CG    1 
ATOM   1487 C  CD    . GLU A 1 190 ? 29.33300  -31.16800 15.21600  1.000 42.53142  ? 190 GLU A CD    1 
ATOM   1488 O  OE1   . GLU A 1 190 ? 28.48000  -31.93300 14.71500  1.000 46.15027  ? 190 GLU A OE1   1 
ATOM   1489 O  OE2   . GLU A 1 190 ? 30.35300  -31.58500 15.80800  1.000 43.70261  ? 190 GLU A OE2   1 
ATOM   1490 N  N     . LEU A 1 191 ? 25.34700  -26.53300 14.34500  1.000 34.07514  ? 191 LEU A N     1 
ATOM   1491 C  CA    . LEU A 1 191 ? 24.01000  -26.23200 13.82000  1.000 34.71732  ? 191 LEU A CA    1 
ATOM   1492 C  C     . LEU A 1 191 ? 23.06300  -27.42600 13.92000  1.000 32.74866  ? 191 LEU A C     1 
ATOM   1493 O  O     . LEU A 1 191 ? 22.16900  -27.58700 13.08700  1.000 36.70440  ? 191 LEU A O     1 
ATOM   1494 C  CB    . LEU A 1 191 ? 24.05400  -25.72000 12.37400  1.000 30.05097  ? 191 LEU A CB    1 
ATOM   1495 C  CG    . LEU A 1 191 ? 24.59300  -24.30300 12.18100  1.000 41.40233  ? 191 LEU A CG    1 
ATOM   1496 C  CD1   . LEU A 1 191 ? 24.13100  -23.72900 10.84100  1.000 43.94474  ? 191 LEU A CD1   1 
ATOM   1497 C  CD2   . LEU A 1 191 ? 24.18700  -23.40700 13.33900  1.000 39.68634  ? 191 LEU A CD2   1 
ATOM   1498 N  N     . SER A 1 192 ? 23.24500  -28.28000 14.92700  1.000 34.07251  ? 192 SER A N     1 
ATOM   1499 C  CA    . SER A 1 192 ? 22.26300  -29.32300 15.20600  1.000 41.63394  ? 192 SER A CA    1 
ATOM   1500 C  C     . SER A 1 192 ? 21.14900  -28.76700 16.08500  1.000 33.84880  ? 192 SER A C     1 
ATOM   1501 O  O     . SER A 1 192 ? 21.39800  -27.96400 16.98900  1.000 28.99032  ? 192 SER A O     1 
ATOM   1502 C  CB    . SER A 1 192 ? 22.91800  -30.52000 15.89400  1.000 38.70201  ? 192 SER A CB    1 
ATOM   1503 O  OG    . SER A 1 192 ? 23.83800  -31.16500 15.03600  1.000 58.82284  ? 192 SER A OG    1 
ATOM   1504 N  N     . HIS A 1 193 ? 19.92000  -29.22000 15.83400  1.000 36.27277  ? 193 HIS A N     1 
ATOM   1505 C  CA    . HIS A 1 193 ? 18.75800  -28.68600 16.53900  1.000 34.46729  ? 193 HIS A CA    1 
ATOM   1506 C  C     . HIS A 1 193 ? 18.81200  -29.06800 18.01700  1.000 29.12718  ? 193 HIS A C     1 
ATOM   1507 O  O     . HIS A 1 193 ? 18.83300  -30.25500 18.35900  1.000 33.93302  ? 193 HIS A O     1 
ATOM   1508 C  CB    . HIS A 1 193 ? 17.47400  -29.20700 15.89600  1.000 31.91435  ? 193 HIS A CB    1 
ATOM   1509 C  CG    . HIS A 1 193 ? 16.22400  -28.65200 16.50400  1.000 39.63896  ? 193 HIS A CG    1 
ATOM   1510 N  ND1   . HIS A 1 193 ? 15.79400  -27.36200 16.27400  1.000 32.71182  ? 193 HIS A ND1   1 
ATOM   1511 C  CD2   . HIS A 1 193 ? 15.30500  -29.21500 17.32500  1.000 36.09380  ? 193 HIS A CD2   1 
ATOM   1512 C  CE1   . HIS A 1 193 ? 14.66800  -27.15300 16.93400  1.000 40.06533  ? 193 HIS A CE1   1 
ATOM   1513 N  NE2   . HIS A 1 193 ? 14.35000  -28.26100 17.57900  1.000 30.94055  ? 193 HIS A NE2   1 
ATOM   1514 N  N     . LEU A 1 194 ? 18.79500  -28.06100 18.87000  1.000 34.44624  ? 194 LEU A N     1 
ATOM   1515 C  CA    . LEU A 1 194 ? 18.85800  -28.22100 20.33700  1.000 30.67210  ? 194 LEU A CA    1 
ATOM   1516 C  C     . LEU A 1 194 ? 17.46600  -28.04000 20.95800  1.000 30.16414  ? 194 LEU A C     1 
ATOM   1517 O  O     . LEU A 1 194 ? 17.18400  -28.76700 21.89100  1.000 32.89079  ? 194 LEU A O     1 
ATOM   1518 C  CB    . LEU A 1 194 ? 19.82700  -27.16800 20.86300  1.000 34.91471  ? 194 LEU A CB    1 
ATOM   1519 C  CG    . LEU A 1 194 ? 20.81100  -27.62600 21.92500  1.000 55.53824  ? 194 LEU A CG    1 
ATOM   1520 C  CD1   . LEU A 1 194 ? 21.31200  -29.02200 21.61400  1.000 42.38929  ? 194 LEU A CD1   1 
ATOM   1521 C  CD2   . LEU A 1 194 ? 21.96600  -26.65500 22.04500  1.000 47.05038  ? 194 LEU A CD2   1 
ATOM   1522 N  N     . GLY A 1 195 ? 16.65900  -27.09100 20.47200  1.000 33.26715  ? 195 GLY A N     1 
ATOM   1523 C  CA    . GLY A 1 195 ? 15.35500  -26.83200 21.04500  1.000 35.89115  ? 195 GLY A CA    1 
ATOM   1524 C  C     . GLY A 1 195 ? 14.73500  -25.58300 20.44800  1.000 24.46872  ? 195 GLY A C     1 
ATOM   1525 O  O     . GLY A 1 195 ? 15.19700  -25.05600 19.43600  1.000 22.06317  ? 195 GLY A O     1 
ATOM   1526 N  N     . SER A 1 196 ? 13.66100  -25.13600 21.08700  1.000 25.58728  ? 196 SER A N     1 
ATOM   1527 C  CA    . SER A 1 196 ? 12.90900  -23.97600 20.64000  1.000 27.55067  ? 196 SER A CA    1 
ATOM   1528 C  C     . SER A 1 196 ? 12.74200  -23.01000 21.80400  1.000 25.41357  ? 196 SER A C     1 
ATOM   1529 O  O     . SER A 1 196 ? 12.73500  -23.41800 22.97100  1.000 31.71433  ? 196 SER A O     1 
ATOM   1530 C  CB    . SER A 1 196 ? 11.55200  -24.39400 20.07700  1.000 32.40652  ? 196 SER A CB    1 
ATOM   1531 O  OG    . SER A 1 196 ? 11.73300  -25.18900 18.91800  1.000 35.58848  ? 196 SER A OG    1 
ATOM   1532 N  N     . ALA A 1 197 ? 12.62400  -21.72200 21.48800  1.000 23.58177  ? 197 ALA A N     1 
ATOM   1533 C  CA    . ALA A 1 197 ? 12.55800  -20.73600 22.55600  1.000 22.39742  ? 197 ALA A CA    1 
ATOM   1534 C  C     . ALA A 1 197 ? 11.84600  -19.47900 22.08400  1.000 24.85035  ? 197 ALA A C     1 
ATOM   1535 O  O     . ALA A 1 197 ? 11.70100  -19.22500 20.88300  1.000 26.39790  ? 197 ALA A O     1 
ATOM   1536 C  CB    . ALA A 1 197 ? 13.95200  -20.38300 23.08200  1.000 22.97907  ? 197 ALA A CB    1 
ATOM   1537 N  N     . ILE A 1 198 ? 11.40300  -18.69600 23.06300  1.000 25.27671  ? 198 ILE A N     1 
ATOM   1538 C  CA    . ILE A 1 198 ? 10.84600  -17.37000 22.83900  1.000 25.71361  ? 198 ILE A CA    1 
ATOM   1539 C  C     . ILE A 1 198 ? 11.84900  -16.35700 23.38400  1.000 26.87427  ? 198 ILE A C     1 
ATOM   1540 O  O     . ILE A 1 198 ? 12.18100  -16.38700 24.57800  1.000 24.54505  ? 198 ILE A O     1 
ATOM   1541 C  CB    . ILE A 1 198 ? 9.48400   -17.20700 23.53300  1.000 29.25088  ? 198 ILE A CB    1 
ATOM   1542 C  CG1   . ILE A 1 198 ? 8.42400   -18.10400 22.88400  1.000 27.80597  ? 198 ILE A CG1   1 
ATOM   1543 C  CG2   . ILE A 1 198 ? 9.04500   -15.75100 23.48400  1.000 31.39061  ? 198 ILE A CG2   1 
ATOM   1544 C  CD1   . ILE A 1 198 ? 8.27000   -17.92000 21.38700  1.000 29.42195  ? 198 ILE A CD1   1 
ATOM   1545 N  N     . PHE A 1 199 ? 12.32100  -15.45500 22.51900  1.000 23.47387  ? 199 PHE A N     1 
ATOM   1546 C  CA    . PHE A 1 199 ? 13.19700  -14.34000 22.88800  1.000 24.14500  ? 199 PHE A CA    1 
ATOM   1547 C  C     . PHE A 1 199 ? 12.50500  -13.05400 22.45200  1.000 22.35531  ? 199 PHE A C     1 
ATOM   1548 O  O     . PHE A 1 199 ? 12.69200  -12.60100 21.31200  1.000 28.70344  ? 199 PHE A O     1 
ATOM   1549 C  CB    . PHE A 1 199 ? 14.57100  -14.45600 22.22900  1.000 24.69243  ? 199 PHE A CB    1 
ATOM   1550 C  CG    . PHE A 1 199 ? 15.37000  -15.64400 22.67500  1.000 24.16606  ? 199 PHE A CG    1 
ATOM   1551 C  CD1   . PHE A 1 199 ? 15.98900  -15.66000 23.91700  1.000 28.32708  ? 199 PHE A CD1   1 
ATOM   1552 C  CD2   . PHE A 1 199 ? 15.52000  -16.74300 21.84200  1.000 30.69842  ? 199 PHE A CD2   1 
ATOM   1553 C  CE1   . PHE A 1 199 ? 16.74000  -16.75100 24.32000  1.000 26.10839  ? 199 PHE A CE1   1 
ATOM   1554 C  CE2   . PHE A 1 199 ? 16.27000  -17.83700 22.24300  1.000 26.42159  ? 199 PHE A CE2   1 
ATOM   1555 C  CZ    . PHE A 1 199 ? 16.87400  -17.84100 23.48900  1.000 25.02142  ? 199 PHE A CZ    1 
ATOM   1556 N  N     . PRO A 1 200 ? 11.67700  -12.45200 23.31300  1.000 26.02680  ? 200 PRO A N     1 
ATOM   1557 C  CA    . PRO A 1 200 ? 10.83900  -11.32100 22.86000  1.000 28.06915  ? 200 PRO A CA    1 
ATOM   1558 C  C     . PRO A 1 200 ? 11.61500  -10.15400 22.27700  1.000 25.98996  ? 200 PRO A C     1 
ATOM   1559 O  O     . PRO A 1 200 ? 11.25700  -9.65900  21.20000  1.000 30.71684  ? 200 PRO A O     1 
ATOM   1560 C  CB    . PRO A 1 200 ? 10.08200  -10.92200 24.13300  1.000 28.71397  ? 200 PRO A CB    1 
ATOM   1561 C  CG    . PRO A 1 200 ? 10.06700  -12.16500 24.97100  1.000 30.32732  ? 200 PRO A CG    1 
ATOM   1562 C  CD    . PRO A 1 200 ? 11.38900  -12.83300 24.70500  1.000 28.88767  ? 200 PRO A CD    1 
ATOM   1563 N  N     . ASP A 1 201 ? 12.65900  -9.67800  22.96000  1.000 24.46346  ? 201 ASP A N     1 
ATOM   1564 C  CA    . ASP A 1 201 ? 13.38800  -8.52600  22.44100  1.000 25.56359  ? 201 ASP A CA    1 
ATOM   1565 C  C     . ASP A 1 201 ? 14.14300  -8.86600  21.16000  1.000 26.03207  ? 201 ASP A C     1 
ATOM   1566 O  O     . ASP A 1 201 ? 14.30200  -7.99900  20.29000  1.000 27.33486  ? 201 ASP A O     1 
ATOM   1567 C  CB    . ASP A 1 201 ? 14.34000  -7.97900  23.50100  1.000 29.94833  ? 201 ASP A CB    1 
ATOM   1568 C  CG    . ASP A 1 201 ? 13.60800  -7.23900  24.61000  1.000 56.93577  ? 201 ASP A CG    1 
ATOM   1569 O  OD1   . ASP A 1 201 ? 12.48200  -6.74700  24.35900  1.000 42.37877  ? 201 ASP A OD1   1 
ATOM   1570 O  OD2   . ASP A 1 201 ? 14.15600  -7.14700  25.73200  1.000 49.81650  ? 201 ASP A OD2   1 
ATOM   1571 N  N     . VAL A 1 202 ? 14.59900  -10.11500 21.01300  1.000 21.37362  ? 202 VAL A N     1 
ATOM   1572 C  CA    . VAL A 1 202 ? 15.25600  -10.50800 19.76700  1.000 24.71875  ? 202 VAL A CA    1 
ATOM   1573 C  C     . VAL A 1 202 ? 14.24300  -10.57900 18.63100  1.000 26.68215  ? 202 VAL A C     1 
ATOM   1574 O  O     . VAL A 1 202 ? 14.57800  -10.30400 17.47000  1.000 28.58501  ? 202 VAL A O     1 
ATOM   1575 C  CB    . VAL A 1 202 ? 16.00000  -11.84700 19.94000  1.000 26.30052  ? 202 VAL A CB    1 
ATOM   1576 C  CG1   . VAL A 1 202 ? 16.74500  -12.21900 18.66100  1.000 28.66659  ? 202 VAL A CG1   1 
ATOM   1577 C  CG2   . VAL A 1 202 ? 16.98000  -11.76600 21.09800  1.000 26.03207  ? 202 VAL A CG2   1 
ATOM   1578 N  N     . ALA A 1 203 ? 12.99100  -10.93400 18.94100  1.000 25.65044  ? 203 ALA A N     1 
ATOM   1579 C  CA    . ALA A 1 203 ? 11.96200  -11.03500 17.91100  1.000 22.81063  ? 203 ALA A CA    1 
ATOM   1580 C  C     . ALA A 1 203 ? 11.65300  -9.69200  17.25900  1.000 23.61862  ? 203 ALA A C     1 
ATOM   1581 O  O     . ALA A 1 203 ? 11.08300  -9.67100  16.16300  1.000 18.97070  ? 203 ALA A O     1 
ATOM   1582 C  CB    . ALA A 1 203 ? 10.68000  -11.63300 18.50200  1.000 25.96101  ? 203 ALA A CB    1 
ATOM   1583 N  N     . LEU A 1 204 ? 12.02100  -8.57800  17.90100  1.000 24.07394  ? 204 LEU A N     1 
ATOM   1584 C  CA    . LEU A 1 204 ? 11.73100  -7.24900  17.36200  1.000 24.02920  ? 204 LEU A CA    1 
ATOM   1585 C  C     . LEU A 1 204 ? 12.47700  -6.95700  16.06100  1.000 24.73454  ? 204 LEU A C     1 
ATOM   1586 O  O     . LEU A 1 204 ? 12.02100  -6.12800  15.26200  1.000 23.87392  ? 204 LEU A O     1 
ATOM   1587 C  CB    . LEU A 1 204 ? 12.05600  -6.18300  18.41500  1.000 26.48739  ? 204 LEU A CB    1 
ATOM   1588 C  CG    . LEU A 1 204 ? 11.82800  -4.71500  18.04500  1.000 25.20565  ? 204 LEU A CG    1 
ATOM   1589 C  CD1   . LEU A 1 204 ? 10.40600  -4.49400  17.54800  1.000 33.89354  ? 204 LEU A CD1   1 
ATOM   1590 C  CD2   . LEU A 1 204 ? 12.11900  -3.81000  19.23900  1.000 29.50091  ? 204 LEU A CD2   1 
ATOM   1591 N  N     . MET A 1 205 ? 13.62700  -7.59500  15.83600  1.000 20.74196  ? 205 MET A N     1 
ATOM   1592 C  CA    . MET A 1 205 ? 14.44200  -7.29100  14.66200  1.000 21.01831  ? 205 MET A CA    1 
ATOM   1593 C  C     . MET A 1 205 ? 13.81400  -7.83400  13.38200  1.000 18.26272  ? 205 MET A C     1 
ATOM   1594 O  O     . MET A 1 205 ? 13.41300  -8.99800  13.31900  1.000 23.67652  ? 205 MET A O     1 
ATOM   1595 C  CB    . MET A 1 205 ? 15.84600  -7.86900  14.83500  1.000 27.94019  ? 205 MET A CB    1 
ATOM   1596 C  CG    . MET A 1 205 ? 16.64700  -7.22100  15.94500  1.000 26.23736  ? 205 MET A CG    1 
ATOM   1597 S  SD    . MET A 1 205 ? 18.30900  -7.91300  16.04900  1.000 27.93493  ? 205 MET A SD    1 
ATOM   1598 C  CE    . MET A 1 205 ? 17.92100  -9.57500  16.59000  1.000 26.39527  ? 205 MET A CE    1 
ATOM   1599 N  N     . ASN A 1 206 ? 13.76400  -7.00300  12.34700  1.000 23.00539  ? 206 ASN A N     1 
ATOM   1600 C  CA    . ASN A 1 206 ? 13.25000  -7.45000  11.06400  1.000 23.39228  ? 206 ASN A CA    1 
ATOM   1601 C  C     . ASN A 1 206 ? 14.31200  -8.25400  10.30500  1.000 19.57603  ? 206 ASN A C     1 
ATOM   1602 O  O     . ASN A 1 206 ? 15.46400  -8.37900  10.73600  1.000 21.93947  ? 206 ASN A O     1 
ATOM   1603 C  CB    . ASN A 1 206 ? 12.74900  -6.25100  10.26200  1.000 21.08937  ? 206 ASN A CB    1 
ATOM   1604 C  CG    . ASN A 1 206 ? 11.45000  -5.70000  10.82100  1.000 24.03446  ? 206 ASN A CG    1 
ATOM   1605 O  OD1   . ASN A 1 206 ? 10.52900  -6.46100  11.10800  1.000 22.83695  ? 206 ASN A OD1   1 
ATOM   1606 N  ND2   . ASN A 1 206 ? 11.37600  -4.38400  11.00000  1.000 25.63728  ? 206 ASN A ND2   1 
ATOM   1607 N  N     . HIS A 1 207 ? 13.89800  -8.83000  9.17800   1.000 23.53966  ? 207 HIS A N     1 
ATOM   1608 C  CA    . HIS A 1 207 ? 14.73000  -9.73300  8.39200   1.000 22.64219  ? 207 HIS A CA    1 
ATOM   1609 C  C     . HIS A 1 207 ? 15.44200  -9.00400  7.25600   1.000 21.66312  ? 207 HIS A C     1 
ATOM   1610 O  O     . HIS A 1 207 ? 14.89700  -8.08500  6.63700   1.000 23.60020  ? 207 HIS A O     1 
ATOM   1611 C  CB    . HIS A 1 207 ? 13.89400  -10.87800 7.80100   1.000 23.17909  ? 207 HIS A CB    1 
ATOM   1612 C  CG    . HIS A 1 207 ? 14.60000  -11.65400 6.72500   1.000 22.64219  ? 207 HIS A CG    1 
ATOM   1613 N  ND1   . HIS A 1 207 ? 15.39100  -12.75200 6.98800   1.000 19.53918  ? 207 HIS A ND1   1 
ATOM   1614 C  CD2   . HIS A 1 207 ? 14.65500  -11.46800 5.38200   1.000 22.64219  ? 207 HIS A CD2   1 
ATOM   1615 C  CE1   . HIS A 1 207 ? 15.88800  -13.21800 5.85500   1.000 24.35029  ? 207 HIS A CE1   1 
ATOM   1616 N  NE2   . HIS A 1 207 ? 15.46300  -12.45200 4.86700   1.000 21.57101  ? 207 HIS A NE2   1 
ATOM   1617 N  N     . SER A 1 208 ? 16.65900  -9.45800  6.97100   1.000 23.28174  ? 208 SER A N     1 
ATOM   1618 C  CA    . SER A 1 208 ? 17.37600  -9.12900  5.74700   1.000 28.24812  ? 208 SER A CA    1 
ATOM   1619 C  C     . SER A 1 208 ? 18.15000  -10.36300 5.30800   1.000 32.31703  ? 208 SER A C     1 
ATOM   1620 O  O     . SER A 1 208 ? 18.60400  -11.14600 6.14500   1.000 21.69734  ? 208 SER A O     1 
ATOM   1621 C  CB    . SER A 1 208 ? 18.33900  -7.94600  5.94100   1.000 28.51395  ? 208 SER A CB    1 
ATOM   1622 O  OG    . SER A 1 208 ? 19.10600  -7.70900  4.77000   1.000 23.66600  ? 208 SER A OG    1 
ATOM   1623 N  N     . CYS A 1 209 ? 18.27200  -10.55300 3.98700   1.000 24.66875  ? 209 CYS A N     1 
ATOM   1624 C  CA    . CYS A 1 209 ? 19.13100  -11.61900 3.48200   1.000 24.13184  ? 209 CYS A CA    1 
ATOM   1625 C  C     . CYS A 1 209 ? 20.60700  -11.22000 3.44300   1.000 22.22635  ? 209 CYS A C     1 
ATOM   1626 O  O     . CYS A 1 209 ? 21.46200  -12.07500 3.18800   1.000 23.89234  ? 209 CYS A O     1 
ATOM   1627 C  CB    . CYS A 1 209 ? 18.66700  -12.06700 2.08900   1.000 31.03267  ? 209 CYS A CB    1 
ATOM   1628 S  SG    . CYS A 1 209 ? 16.87100  -12.41800 1.96700   1.000 24.30291  ? 209 CYS A SG    1 
ATOM   1629 N  N     . CYS A 1 210 ? 20.93300  -9.95600  3.71600   1.000 21.63944  ? 210 CYS A N     1 
ATOM   1630 C  CA    . CYS A 1 210 ? 22.30000  -9.53300  4.01200   1.000 23.74495  ? 210 CYS A CA    1 
ATOM   1631 C  C     . CYS A 1 210 ? 22.28100  -8.87000  5.38600   1.000 23.41333  ? 210 CYS A C     1 
ATOM   1632 O  O     . CYS A 1 210 ? 22.40800  -7.64500  5.50700   1.000 24.36608  ? 210 CYS A O     1 
ATOM   1633 C  CB    . CYS A 1 210 ? 22.86800  -8.60300  2.94000   1.000 31.64853  ? 210 CYS A CB    1 
ATOM   1634 S  SG    . CYS A 1 210 ? 21.69800  -7.46000  2.18600   1.000 39.95479  ? 210 CYS A SG    1 
ATOM   1635 N  N     . PRO A 1 211 ? 22.12200  -9.66400  6.44500   1.000 21.46310  ? 211 PRO A N     1 
ATOM   1636 C  CA    . PRO A 1 211 ? 21.90200  -9.09500  7.77900   1.000 25.19249  ? 211 PRO A CA    1 
ATOM   1637 C  C     . PRO A 1 211 ? 23.15600  -8.43400  8.32900   1.000 25.83468  ? 211 PRO A C     1 
ATOM   1638 O  O     . PRO A 1 211 ? 24.28000  -8.74100  7.92700   1.000 23.97393  ? 211 PRO A O     1 
ATOM   1639 C  CB    . PRO A 1 211 ? 21.50500  -10.32000 8.61300   1.000 23.03960  ? 211 PRO A CB    1 
ATOM   1640 C  CG    . PRO A 1 211 ? 22.21200  -11.46300 7.94400   1.000 21.41046  ? 211 PRO A CG    1 
ATOM   1641 C  CD    . PRO A 1 211 ? 22.16600  -11.13700 6.46800   1.000 22.83958  ? 211 PRO A CD    1 
ATOM   1642 N  N     . ASN A 1 212 ? 22.95400  -7.50200  9.26600   1.000 19.03386  ? 212 ASN A N     1 
ATOM   1643 C  CA    . ASN A 1 212 ? 24.09400  -6.87500  9.92100   1.000 23.47913  ? 212 ASN A CA    1 
ATOM   1644 C  C     . ASN A 1 212 ? 24.34200  -7.40400  11.33600  1.000 22.93696  ? 212 ASN A C     1 
ATOM   1645 O  O     . ASN A 1 212 ? 25.33300  -7.00900  11.95800  1.000 22.50533  ? 212 ASN A O     1 
ATOM   1646 C  CB    . ASN A 1 212 ? 23.96900  -5.33400  9.91500   1.000 20.12347  ? 212 ASN A CB    1 
ATOM   1647 C  CG    . ASN A 1 212 ? 22.63100  -4.82700  10.44000  1.000 20.53141  ? 212 ASN A CG    1 
ATOM   1648 O  OD1   . ASN A 1 212 ? 21.87600  -5.55800  11.08100  1.000 25.89521  ? 212 ASN A OD1   1 
ATOM   1649 N  ND2   . ASN A 1 212 ? 22.34800  -3.55100  10.18700  1.000 22.61587  ? 212 ASN A ND2   1 
ATOM   1650 N  N     . VAL A 1 213 ? 23.50100  -8.31600  11.84200  1.000 18.59433  ? 213 VAL A N     1 
ATOM   1651 C  CA    . VAL A 1 213 ? 23.77300  -9.01300  13.09500  1.000 20.31296  ? 213 VAL A CA    1 
ATOM   1652 C  C     . VAL A 1 213 ? 23.49200  -10.50100 12.91500  1.000 22.68693  ? 213 VAL A C     1 
ATOM   1653 O  O     . VAL A 1 213 ? 22.76300  -10.91800 12.01300  1.000 25.49779  ? 213 VAL A O     1 
ATOM   1654 C  CB    . VAL A 1 213 ? 22.94600  -8.46900  14.29000  1.000 19.85764  ? 213 VAL A CB    1 
ATOM   1655 C  CG1   . VAL A 1 213 ? 23.20000  -6.98500  14.49200  1.000 21.78156  ? 213 VAL A CG1   1 
ATOM   1656 C  CG2   . VAL A 1 213 ? 21.45500  -8.76500  14.09700  1.000 22.06844  ? 213 VAL A CG2   1 
ATOM   1657 N  N     . ILE A 1 214 ? 24.07500  -11.30400 13.80800  1.000 22.02633  ? 214 ILE A N     1 
ATOM   1658 C  CA    . ILE A 1 214 ? 23.79400  -12.73100 13.90600  1.000 22.23688  ? 214 ILE A CA    1 
ATOM   1659 C  C     . ILE A 1 214 ? 23.43700  -13.05400 15.35200  1.000 23.93445  ? 214 ILE A C     1 
ATOM   1660 O  O     . ILE A 1 214 ? 24.06400  -12.54100 16.28800  1.000 20.35507  ? 214 ILE A O     1 
ATOM   1661 C  CB    . ILE A 1 214 ? 24.98900  -13.59400 13.44500  1.000 28.63764  ? 214 ILE A CB    1 
ATOM   1662 C  CG1   . ILE A 1 214 ? 25.15600  -13.52000 11.93600  1.000 43.44205  ? 214 ILE A CG1   1 
ATOM   1663 C  CG2   . ILE A 1 214 ? 24.81000  -15.04800 13.84900  1.000 28.06652  ? 214 ILE A CG2   1 
ATOM   1664 C  CD1   . ILE A 1 214 ? 26.32400  -14.31800 11.45700  1.000 40.91280  ? 214 ILE A CD1   1 
ATOM   1665 N  N     . VAL A 1 215 ? 22.44100  -13.91600 15.53000  1.000 21.24465  ? 215 VAL A N     1 
ATOM   1666 C  CA    . VAL A 1 215 ? 22.01700  -14.36700 16.84800  1.000 23.49755  ? 215 VAL A CA    1 
ATOM   1667 C  C     . VAL A 1 215 ? 22.71100  -15.68300 17.16700  1.000 28.80609  ? 215 VAL A C     1 
ATOM   1668 O  O     . VAL A 1 215 ? 22.66900  -16.62700 16.36700  1.000 26.17156  ? 215 VAL A O     1 
ATOM   1669 C  CB    . VAL A 1 215 ? 20.49000  -14.53000 16.90800  1.000 26.41369  ? 215 VAL A CB    1 
ATOM   1670 C  CG1   . VAL A 1 215 ? 20.06200  -14.94000 18.31600  1.000 33.50402  ? 215 VAL A CG1   1 
ATOM   1671 C  CG2   . VAL A 1 215 ? 19.80400  -13.24300 16.48000  1.000 28.25339  ? 215 VAL A CG2   1 
ATOM   1672 N  N     . THR A 1 216 ? 23.36700  -15.73800 18.32500  1.000 23.90813  ? 216 THR A N     1 
ATOM   1673 C  CA    . THR A 1 216 ? 23.95000  -16.95800 18.85600  1.000 21.89999  ? 216 THR A CA    1 
ATOM   1674 C  C     . THR A 1 216 ? 23.42200  -17.17000 20.26700  1.000 30.74842  ? 216 THR A C     1 
ATOM   1675 O  O     . THR A 1 216 ? 22.73200  -16.31400 20.83100  1.000 28.16654  ? 216 THR A O     1 
ATOM   1676 C  CB    . THR A 1 216 ? 25.48300  -16.90600 18.89400  1.000 26.54792  ? 216 THR A CB    1 
ATOM   1677 O  OG1   . THR A 1 216 ? 25.89200  -15.82400 19.73700  1.000 30.18520  ? 216 THR A OG1   1 
ATOM   1678 C  CG2   . THR A 1 216 ? 26.06000  -16.70700 17.49400  1.000 24.87667  ? 216 THR A CG2   1 
ATOM   1679 N  N     . TYR A 1 217 ? 23.77200  -18.31500 20.85000  1.000 30.45102  ? 217 TYR A N     1 
ATOM   1680 C  CA    . TYR A 1 217 ? 23.21000  -18.72400 22.13000  1.000 27.35591  ? 217 TYR A CA    1 
ATOM   1681 C  C     . TYR A 1 217 ? 24.32300  -19.16600 23.06400  1.000 28.81924  ? 217 TYR A C     1 
ATOM   1682 O  O     . TYR A 1 217 ? 25.22600  -19.91100 22.66200  1.000 28.75082  ? 217 TYR A O     1 
ATOM   1683 C  CB    . TYR A 1 217 ? 22.17400  -19.84400 21.94200  1.000 23.73706  ? 217 TYR A CB    1 
ATOM   1684 C  CG    . TYR A 1 217 ? 21.11400  -19.46300 20.93300  1.000 27.65595  ? 217 TYR A CG    1 
ATOM   1685 C  CD1   . TYR A 1 217 ? 20.07800  -18.60200 21.27600  1.000 27.69279  ? 217 TYR A CD1   1 
ATOM   1686 C  CD2   . TYR A 1 217 ? 21.17200  -19.93300 19.63000  1.000 26.48475  ? 217 TYR A CD2   1 
ATOM   1687 C  CE1   . TYR A 1 217 ? 19.11800  -18.23100 20.34600  1.000 24.10026  ? 217 TYR A CE1   1 
ATOM   1688 C  CE2   . TYR A 1 217 ? 20.22000  -19.57000 18.69400  1.000 26.46633  ? 217 TYR A CE2   1 
ATOM   1689 C  CZ    . TYR A 1 217 ? 19.19600  -18.71800 19.05900  1.000 31.01161  ? 217 TYR A CZ    1 
ATOM   1690 O  OH    . TYR A 1 217 ? 18.24700  -18.35700 18.13000  1.000 32.34335  ? 217 TYR A OH    1 
ATOM   1691 N  N     . LYS A 1 218 ? 24.26100  -18.67800 24.29800  1.000 27.25590  ? 218 LYS A N     1 
ATOM   1692 C  CA    . LYS A 1 218 ? 25.11900  -19.08700 25.40700  1.000 31.33007  ? 218 LYS A CA    1 
ATOM   1693 C  C     . LYS A 1 218 ? 24.19500  -19.81300 26.38000  1.000 30.88791  ? 218 LYS A C     1 
ATOM   1694 O  O     . LYS A 1 218 ? 23.58800  -19.19700 27.25700  1.000 32.33546  ? 218 LYS A O     1 
ATOM   1695 C  CB    . LYS A 1 218 ? 25.79700  -17.88100 26.05300  1.000 27.60594  ? 218 LYS A CB    1 
ATOM   1696 C  CG    . LYS A 1 218 ? 27.00500  -18.20700 26.91300  1.000 35.08315  ? 218 LYS A CG    1 
ATOM   1697 C  CD    . LYS A 1 218 ? 27.74500  -16.93400 27.31300  1.000 38.69938  ? 218 LYS A CD    1 
ATOM   1698 C  CE    . LYS A 1 218 ? 28.50100  -16.36100 26.12500  1.000 44.77379  ? 218 LYS A CE    1 
ATOM   1699 N  NZ    . LYS A 1 218 ? 29.02300  -14.98500 26.35900  1.000 39.55737  ? 218 LYS A NZ    1 
ATOM   1700 N  N     . GLY A 1 219 ? 24.04900  -21.12000 26.18800  1.000 30.41944  ? 219 GLY A N     1 
ATOM   1701 C  CA    . GLY A 1 219 ? 23.01400  -21.85000 26.89300  1.000 39.25734  ? 219 GLY A CA    1 
ATOM   1702 C  C     . GLY A 1 219 ? 21.63000  -21.45000 26.41800  1.000 38.37829  ? 219 GLY A C     1 
ATOM   1703 O  O     . GLY A 1 219 ? 21.29600  -21.63600 25.24400  1.000 34.46466  ? 219 GLY A O     1 
ATOM   1704 N  N     . THR A 1 220 ? 20.82300  -20.87200 27.30700  1.000 25.79783  ? 220 THR A N     1 
ATOM   1705 C  CA    . THR A 1 220 ? 19.49000  -20.40000 26.95800  1.000 29.60092  ? 220 THR A CA    1 
ATOM   1706 C  C     . THR A 1 220 ? 19.43500  -18.88700 26.78900  1.000 27.55067  ? 220 THR A C     1 
ATOM   1707 O  O     . THR A 1 220 ? 18.34200  -18.32900 26.64700  1.000 25.45832  ? 220 THR A O     1 
ATOM   1708 C  CB    . THR A 1 220 ? 18.47500  -20.83300 28.01700  1.000 32.29071  ? 220 THR A CB    1 
ATOM   1709 O  OG1   . THR A 1 220 ? 18.75400  -20.15400 29.24900  1.000 26.94270  ? 220 THR A OG1   1 
ATOM   1710 C  CG2   . THR A 1 220 ? 18.55800  -22.33400 28.24300  1.000 43.03411  ? 220 THR A CG2   1 
ATOM   1711 N  N     . LEU A 1 221 ? 20.58300  -18.21600 26.82400  1.000 30.89318  ? 221 LEU A N     1 
ATOM   1712 C  CA    . LEU A 1 221 ? 20.67700  -16.76900 26.66200  1.000 28.18233  ? 221 LEU A CA    1 
ATOM   1713 C  C     . LEU A 1 221 ? 21.00700  -16.45100 25.20900  1.000 30.10361  ? 221 LEU A C     1 
ATOM   1714 O  O     . LEU A 1 221 ? 22.04100  -16.89400 24.70000  1.000 28.70344  ? 221 LEU A O     1 
ATOM   1715 C  CB    . LEU A 1 221 ? 21.75500  -16.20300 27.58600  1.000 32.76182  ? 221 LEU A CB    1 
ATOM   1716 C  CG    . LEU A 1 221 ? 22.07500  -14.71100 27.53200  1.000 36.50701  ? 221 LEU A CG    1 
ATOM   1717 C  CD1   . LEU A 1 221 ? 21.01900  -13.89800 28.27100  1.000 31.00898  ? 221 LEU A CD1   1 
ATOM   1718 C  CD2   . LEU A 1 221 ? 23.47400  -14.44400 28.09800  1.000 32.95132  ? 221 LEU A CD2   1 
ATOM   1719 N  N     . ALA A 1 222 ? 20.15400  -15.66400 24.55400  1.000 24.44504  ? 222 ALA A N     1 
ATOM   1720 C  CA    . ALA A 1 222 ? 20.43700  -15.22500 23.19100  1.000 23.12909  ? 222 ALA A CA    1 
ATOM   1721 C  C     . ALA A 1 222 ? 21.36000  -14.01300 23.21200  1.000 22.32899  ? 222 ALA A C     1 
ATOM   1722 O  O     . ALA A 1 222 ? 21.20800  -13.11500 24.04400  1.000 25.65834  ? 222 ALA A O     1 
ATOM   1723 C  CB    . ALA A 1 222 ? 19.14200  -14.88700 22.44600  1.000 21.69734  ? 222 ALA A CB    1 
ATOM   1724 N  N     . GLU A 1 223 ? 22.33200  -13.99900 22.30100  1.000 25.32409  ? 223 GLU A N     1 
ATOM   1725 C  CA    . GLU A 1 223 ? 23.25700  -12.88200 22.15600  1.000 22.07107  ? 223 GLU A CA    1 
ATOM   1726 C  C     . GLU A 1 223 ? 23.23500  -12.40300 20.71100  1.000 22.90011  ? 223 GLU A C     1 
ATOM   1727 O  O     . GLU A 1 223 ? 23.09400  -13.20800 19.78400  1.000 26.83480  ? 223 GLU A O     1 
ATOM   1728 C  CB    . GLU A 1 223 ? 24.68300  -13.28300 22.56900  1.000 23.94234  ? 223 GLU A CB    1 
ATOM   1729 C  CG    . GLU A 1 223 ? 24.79900  -13.67900 24.03300  1.000 32.75393  ? 223 GLU A CG    1 
ATOM   1730 C  CD    . GLU A 1 223 ? 26.24000  -13.82900 24.50600  1.000 43.34467  ? 223 GLU A CD    1 
ATOM   1731 O  OE1   . GLU A 1 223 ? 27.08500  -14.35800 23.74500  1.000 38.79149  ? 223 GLU A OE1   1 
ATOM   1732 O  OE2   . GLU A 1 223 ? 26.53000  -13.39500 25.64200  1.000 42.79197  ? 223 GLU A OE2   1 
ATOM   1733 N  N     . VAL A 1 224 ? 23.36000  -11.09200 20.51900  1.000 21.28413  ? 224 VAL A N     1 
ATOM   1734 C  CA    . VAL A 1 224 ? 23.23900  -10.47700 19.19800  1.000 23.19225  ? 224 VAL A CA    1 
ATOM   1735 C  C     . VAL A 1 224 ? 24.49700  -9.66100  18.92800  1.000 22.77115  ? 224 VAL A C     1 
ATOM   1736 O  O     . VAL A 1 224 ? 24.77800  -8.69000  19.64200  1.000 29.42195  ? 224 VAL A O     1 
ATOM   1737 C  CB    . VAL A 1 224 ? 21.98700  -9.59500  19.07900  1.000 21.49995  ? 224 VAL A CB    1 
ATOM   1738 C  CG1   . VAL A 1 224 ? 21.93100  -8.96100  17.70200  1.000 25.04774  ? 224 VAL A CG1   1 
ATOM   1739 C  CG2   . VAL A 1 224 ? 20.72800  -10.41600 19.33600  1.000 27.14010  ? 224 VAL A CG2   1 
ATOM   1740 N  N     . ARG A 1 225 ? 25.24900  -10.05200 17.90000  1.000 20.26559  ? 225 ARG A N     1 
ATOM   1741 C  CA    . ARG A 1 225 ? 26.52800  -9.43600  17.58200  1.000 25.05300  ? 225 ARG A CA    1 
ATOM   1742 C  C     . ARG A 1 225 ? 26.54700  -8.95200  16.13700  1.000 27.06377  ? 225 ARG A C     1 
ATOM   1743 O  O     . ARG A 1 225 ? 25.95000  -9.57500  15.25400  1.000 23.87655  ? 225 ARG A O     1 
ATOM   1744 C  CB    . ARG A 1 225 ? 27.68000  -10.41200 17.83700  1.000 20.94988  ? 225 ARG A CB    1 
ATOM   1745 C  CG    . ARG A 1 225 ? 28.05600  -10.50300 19.31700  1.000 22.56323  ? 225 ARG A CG    1 
ATOM   1746 C  CD    . ARG A 1 225 ? 29.29100  -11.36600 19.58100  1.000 24.72139  ? 225 ARG A CD    1 
ATOM   1747 N  NE    . ARG A 1 225 ? 29.55400  -11.49000 21.01800  1.000 29.10875  ? 225 ARG A NE    1 
ATOM   1748 C  CZ    . ARG A 1 225 ? 28.92400  -12.33400 21.83000  1.000 25.25829  ? 225 ARG A CZ    1 
ATOM   1749 N  NH1   . ARG A 1 225 ? 27.99500  -13.15500 21.35600  1.000 31.93278  ? 225 ARG A NH1   1 
ATOM   1750 N  NH2   . ARG A 1 225 ? 29.22500  -12.35900 23.11900  1.000 31.71170  ? 225 ARG A NH2   1 
ATOM   1751 N  N     . ALA A 1 226 ? 27.22200  -7.82600  15.91000  1.000 28.11653  ? 226 ALA A N     1 
ATOM   1752 C  CA    . ALA A 1 226 ? 27.32100  -7.24800  14.57500  1.000 23.02381  ? 226 ALA A CA    1 
ATOM   1753 C  C     . ALA A 1 226 ? 28.25300  -8.06600  13.69000  1.000 26.07681  ? 226 ALA A C     1 
ATOM   1754 O  O     . ALA A 1 226 ? 29.35100  -8.45000  14.11000  1.000 24.17921  ? 226 ALA A O     1 
ATOM   1755 C  CB    . ALA A 1 226 ? 27.82100  -5.80700  14.66400  1.000 26.08207  ? 226 ALA A CB    1 
ATOM   1756 N  N     . VAL A 1 227 ? 27.81700  -8.32700  12.45600  1.000 23.06592  ? 227 VAL A N     1 
ATOM   1757 C  CA    . VAL A 1 227 ? 28.67100  -8.91100  11.42800  1.000 28.36393  ? 227 VAL A CA    1 
ATOM   1758 C  C     . VAL A 1 227 ? 28.91200  -7.94800  10.27800  1.000 30.96424  ? 227 VAL A C     1 
ATOM   1759 O  O     . VAL A 1 227 ? 29.63400  -8.29200  9.33100   1.000 27.70595  ? 227 VAL A O     1 
ATOM   1760 C  CB    . VAL A 1 227 ? 28.10300  -10.24500 10.90300  1.000 26.58213  ? 227 VAL A CB    1 
ATOM   1761 C  CG1   . VAL A 1 227 ? 28.04100  -11.27300 12.02200  1.000 28.64291  ? 227 VAL A CG1   1 
ATOM   1762 C  CG2   . VAL A 1 227 ? 26.72700  -10.03100 10.26500  1.000 28.92189  ? 227 VAL A CG2   1 
ATOM   1763 N  N     . GLN A 1 228 ? 28.31800  -6.75700  10.33100  1.000 31.34586  ? 228 GLN A N     1 
ATOM   1764 C  CA    . GLN A 1 228 ? 28.66100  -5.61200  9.49900   1.000 30.75895  ? 228 GLN A CA    1 
ATOM   1765 C  C     . GLN A 1 228 ? 28.72400  -4.40500  10.42300  1.000 28.95347  ? 228 GLN A C     1 
ATOM   1766 O  O     . GLN A 1 228 ? 28.16400  -4.42100  11.52200  1.000 29.22192  ? 228 GLN A O     1 
ATOM   1767 C  CB    . GLN A 1 228 ? 27.62800  -5.35500  8.38400   1.000 28.48763  ? 228 GLN A CB    1 
ATOM   1768 C  CG    . GLN A 1 228 ? 27.48900  -6.46000  7.33800   1.000 32.68023  ? 228 GLN A CG    1 
ATOM   1769 C  CD    . GLN A 1 228 ? 26.49300  -6.09100  6.24000   1.000 37.71242  ? 228 GLN A CD    1 
ATOM   1770 O  OE1   . GLN A 1 228 ? 26.65000  -5.08000  5.56200   1.000 45.01856  ? 228 GLN A OE1   1 
ATOM   1771 N  NE2   . GLN A 1 228 ? 25.45600  -6.90100  6.08000   1.000 40.70488  ? 228 GLN A NE2   1 
ATOM   1772 N  N     . GLU A 1 229 ? 29.41300  -3.35800  9.98100   1.000 28.47710  ? 229 GLU A N     1 
ATOM   1773 C  CA    . GLU A 1 229 ? 29.43500  -2.12100  10.74900  1.000 31.35376  ? 229 GLU A CA    1 
ATOM   1774 C  C     . GLU A 1 229 ? 28.03500  -1.51600  10.74900  1.000 29.31141  ? 229 GLU A C     1 
ATOM   1775 O  O     . GLU A 1 229 ? 27.34800  -1.51500  9.72400   1.000 31.62221  ? 229 GLU A O     1 
ATOM   1776 C  CB    . GLU A 1 229 ? 30.45000  -1.15100  10.14900  1.000 41.99714  ? 229 GLU A CB    1 
ATOM   1777 C  CG    . GLU A 1 229 ? 30.74600  0.08200   10.96400  1.000 79.41478  ? 229 GLU A CG    1 
ATOM   1778 C  CD    . GLU A 1 229 ? 32.01600  0.75800   10.45900  1.000 104.90732 ? 229 GLU A CD    1 
ATOM   1779 O  OE1   . GLU A 1 229 ? 32.27700  0.70700   9.24700   1.000 72.71925  ? 229 GLU A OE1   1 
ATOM   1780 O  OE2   . GLU A 1 229 ? 32.78000  1.34100   11.25300  1.000 81.60715  ? 229 GLU A OE2   1 
ATOM   1781 N  N     . ILE A 1 230 ? 27.57700  -1.06400  11.91600  1.000 30.87739  ? 230 ILE A N     1 
ATOM   1782 C  CA    . ILE A 1 230 ? 26.24300  -0.48300  12.05700  1.000 30.27731  ? 230 ILE A CA    1 
ATOM   1783 C  C     . ILE A 1 230 ? 26.40400  0.94600   12.54600  1.000 30.86159  ? 230 ILE A C     1 
ATOM   1784 O  O     . ILE A 1 230 ? 27.10300  1.19400   13.53400  1.000 27.93230  ? 230 ILE A O     1 
ATOM   1785 C  CB    . ILE A 1 230 ? 25.34600  -1.28700  13.01700  1.000 27.97177  ? 230 ILE A CB    1 
ATOM   1786 C  CG1   . ILE A 1 230 ? 25.26900  -2.75000  12.58100  1.000 24.08973  ? 230 ILE A CG1   1 
ATOM   1787 C  CG2   . ILE A 1 230 ? 23.93200  -0.69700  13.04000  1.000 27.46908  ? 230 ILE A CG2   1 
ATOM   1788 C  CD1   . ILE A 1 230 ? 24.58800  -3.64200  13.58800  1.000 29.90622  ? 230 ILE A CD1   1 
ATOM   1789 N  N     . LYS A 1 231 ? 25.76200  1.87700   11.85700  1.000 22.85011  ? 231 LYS A N     1 
ATOM   1790 C  CA    . LYS A 1 231 ? 25.87400  3.28900   12.16800  1.000 24.65559  ? 231 LYS A CA    1 
ATOM   1791 C  C     . LYS A 1 231 ? 24.59300  3.79100   12.81800  1.000 23.10014  ? 231 LYS A C     1 
ATOM   1792 O  O     . LYS A 1 231 ? 23.53000  3.18200   12.66400  1.000 22.12897  ? 231 LYS A O     1 
ATOM   1793 C  CB    . LYS A 1 231 ? 26.17700  4.09700   10.89900  1.000 27.14010  ? 231 LYS A CB    1 
ATOM   1794 C  CG    . LYS A 1 231 ? 27.47700  3.68700   10.22000  1.000 29.90622  ? 231 LYS A CG    1 
ATOM   1795 C  CD    . LYS A 1 231 ? 28.64800  3.79800   11.18600  1.000 45.76865  ? 231 LYS A CD    1 
ATOM   1796 C  CE    . LYS A 1 231 ? 29.97300  3.87800   10.44500  1.000 60.44672  ? 231 LYS A CE    1 
ATOM   1797 N  NZ    . LYS A 1 231 ? 30.09500  5.14900   9.67000   1.000 84.01270  ? 231 LYS A NZ    1 
ATOM   1798 N  N     . PRO A 1 232 ? 24.66800  4.88100   13.58400  1.000 30.32469  ? 232 PRO A N     1 
ATOM   1799 C  CA    . PRO A 1 232 ? 23.45300  5.46600   14.16900  1.000 32.76445  ? 232 PRO A CA    1 
ATOM   1800 C  C     . PRO A 1 232 ? 22.39200  5.75100   13.11400  1.000 31.31428  ? 232 PRO A C     1 
ATOM   1801 O  O     . PRO A 1 232 ? 22.68300  6.26300   12.02900  1.000 34.77522  ? 232 PRO A O     1 
ATOM   1802 C  CB    . PRO A 1 232 ? 23.96400  6.75900   14.81200  1.000 30.99845  ? 232 PRO A CB    1 
ATOM   1803 C  CG    . PRO A 1 232 ? 25.40000  6.47000   15.12400  1.000 36.83600  ? 232 PRO A CG    1 
ATOM   1804 C  CD    . PRO A 1 232 ? 25.88700  5.58800   14.00900  1.000 33.03291  ? 232 PRO A CD    1 
ATOM   1805 N  N     . GLY A 1 233 ? 21.14500  5.42200   13.44500  1.000 29.72198  ? 233 GLY A N     1 
ATOM   1806 C  CA    . GLY A 1 233 ? 20.03800  5.59000   12.54000  1.000 31.23796  ? 233 GLY A CA    1 
ATOM   1807 C  C     . GLY A 1 233 ? 19.73000  4.38200   11.68300  1.000 28.25865  ? 233 GLY A C     1 
ATOM   1808 O  O     . GLY A 1 233 ? 18.63300  4.30200   11.11900  1.000 30.26679  ? 233 GLY A O     1 
ATOM   1809 N  N     . GLU A 1 234 ? 20.65900  3.43700   11.57200  1.000 27.01640  ? 234 GLU A N     1 
ATOM   1810 C  CA    . GLU A 1 234 ? 20.45400  2.27900   10.71600  1.000 29.77989  ? 234 GLU A CA    1 
ATOM   1811 C  C     . GLU A 1 234 ? 19.66400  1.19600   11.43800  1.000 29.37721  ? 234 GLU A C     1 
ATOM   1812 O  O     . GLU A 1 234 ? 19.83400  0.97600   12.64100  1.000 25.21355  ? 234 GLU A O     1 
ATOM   1813 C  CB    . GLU A 1 234 ? 21.79800  1.72600   10.24600  1.000 27.60594  ? 234 GLU A CB    1 
ATOM   1814 C  CG    . GLU A 1 234 ? 22.59300  2.71800   9.41300   1.000 30.98003  ? 234 GLU A CG    1 
ATOM   1815 C  CD    . GLU A 1 234 ? 23.77600  2.07200   8.72300   1.000 39.76793  ? 234 GLU A CD    1 
ATOM   1816 O  OE1   . GLU A 1 234 ? 24.39000  1.16400   9.32700   1.000 35.49899  ? 234 GLU A OE1   1 
ATOM   1817 O  OE2   . GLU A 1 234 ? 24.09000  2.46800   7.57700   1.000 51.30352  ? 234 GLU A OE2   1 
ATOM   1818 N  N     . GLU A 1 235 ? 18.80500  0.50900   10.69100  1.000 26.97165  ? 235 GLU A N     1 
ATOM   1819 C  CA    . GLU A 1 235 ? 17.99600  -0.55900  11.25500  1.000 26.79005  ? 235 GLU A CA    1 
ATOM   1820 C  C     . GLU A 1 235 ? 18.83500  -1.82100  11.44300  1.000 23.97919  ? 235 GLU A C     1 
ATOM   1821 O  O     . GLU A 1 235 ? 19.73300  -2.12300  10.64400  1.000 18.31009  ? 235 GLU A O     1 
ATOM   1822 C  CB    . GLU A 1 235 ? 16.78600  -0.84200  10.35900  1.000 26.57950  ? 235 GLU A CB    1 
ATOM   1823 C  CG    . GLU A 1 235 ? 15.93100  -2.00600  10.84400  1.000 31.29849  ? 235 GLU A CG    1 
ATOM   1824 C  CD    . GLU A 1 235 ? 14.50400  -1.97600  10.33500  1.000 30.49576  ? 235 GLU A CD    1 
ATOM   1825 O  OE1   . GLU A 1 235 ? 14.20000  -1.16000  9.43500   1.000 29.83516  ? 235 GLU A OE1   1 
ATOM   1826 O  OE2   . GLU A 1 235 ? 13.68400  -2.77200  10.84800  1.000 26.71110  ? 235 GLU A OE2   1 
ATOM   1827 N  N     . VAL A 1 236 ? 18.54700  -2.54500  12.52100  1.000 18.98912  ? 236 VAL A N     1 
ATOM   1828 C  CA    . VAL A 1 236 ? 19.23500  -3.78900  12.85500  1.000 22.08423  ? 236 VAL A CA    1 
ATOM   1829 C  C     . VAL A 1 236 ? 18.45400  -4.95000  12.24900  1.000 19.62077  ? 236 VAL A C     1 
ATOM   1830 O  O     . VAL A 1 236 ? 17.26700  -5.13300  12.54800  1.000 24.25028  ? 236 VAL A O     1 
ATOM   1831 C  CB    . VAL A 1 236 ? 19.36700  -3.94600  14.37800  1.000 26.10313  ? 236 VAL A CB    1 
ATOM   1832 C  CG1   . VAL A 1 236 ? 20.18900  -5.16700  14.71800  1.000 29.35352  ? 236 VAL A CG1   1 
ATOM   1833 C  CG2   . VAL A 1 236 ? 19.95900  -2.67800  14.99400  1.000 21.49205  ? 236 VAL A CG2   1 
ATOM   1834 N  N     . PHE A 1 237 ? 19.11900  -5.74600  11.41300  1.000 20.73143  ? 237 PHE A N     1 
ATOM   1835 C  CA    . PHE A 1 237 ? 18.48300  -6.82900  10.66500  1.000 23.20805  ? 237 PHE A CA    1 
ATOM   1836 C  C     . PHE A 1 237 ? 19.17100  -8.15600  10.95600  1.000 21.46047  ? 237 PHE A C     1 
ATOM   1837 O  O     . PHE A 1 237 ? 20.39500  -8.26900  10.82400  1.000 21.59469  ? 237 PHE A O     1 
ATOM   1838 C  CB    . PHE A 1 237 ? 18.55000  -6.58400  9.15400   1.000 27.16378  ? 237 PHE A CB    1 
ATOM   1839 C  CG    . PHE A 1 237 ? 17.70100  -5.44300  8.66100   1.000 20.92619  ? 237 PHE A CG    1 
ATOM   1840 C  CD1   . PHE A 1 237 ? 16.32500  -5.57800  8.56300   1.000 24.66085  ? 237 PHE A CD1   1 
ATOM   1841 C  CD2   . PHE A 1 237 ? 18.28800  -4.25400  8.24400   1.000 23.91603  ? 237 PHE A CD2   1 
ATOM   1842 C  CE1   . PHE A 1 237 ? 15.54900  -4.53800  8.09700   1.000 21.85262  ? 237 PHE A CE1   1 
ATOM   1843 C  CE2   . PHE A 1 237 ? 17.51800  -3.21200  7.76900   1.000 24.67927  ? 237 PHE A CE2   1 
ATOM   1844 C  CZ    . PHE A 1 237 ? 16.14400  -3.35800  7.68900   1.000 19.93397  ? 237 PHE A CZ    1 
ATOM   1845 N  N     . THR A 1 238 ? 18.38500  -9.17100  11.29100  1.000 20.75775  ? 238 THR A N     1 
ATOM   1846 C  CA    . THR A 1 238 ? 18.87800  -10.53900 11.36700  1.000 24.71086  ? 238 THR A CA    1 
ATOM   1847 C  C     . THR A 1 238 ? 18.33000  -11.32100 10.17800  1.000 24.52662  ? 238 THR A C     1 
ATOM   1848 O  O     . THR A 1 238 ? 17.50000  -10.82200 9.41600   1.000 26.31631  ? 238 THR A O     1 
ATOM   1849 C  CB    . THR A 1 238 ? 18.46200  -11.19000 12.69100  1.000 27.28222  ? 238 THR A CB    1 
ATOM   1850 O  OG1   . THR A 1 238 ? 19.23400  -12.37600 12.90900  1.000 40.16797  ? 238 THR A OG1   1 
ATOM   1851 C  CG2   . THR A 1 238 ? 16.98800  -11.55600 12.65700  1.000 26.95323  ? 238 THR A CG2   1 
ATOM   1852 N  N     . SER A 1 239 ? 18.80700  -12.54800 10.00300  1.000 23.28174  ? 239 SER A N     1 
ATOM   1853 C  CA    . SER A 1 239 ? 18.23800  -13.44600 9.00300   1.000 26.10839  ? 239 SER A CA    1 
ATOM   1854 C  C     . SER A 1 239 ? 17.33300  -14.47100 9.67200   1.000 22.40795  ? 239 SER A C     1 
ATOM   1855 O  O     . SER A 1 239 ? 17.71300  -15.09000 10.67400  1.000 24.77402  ? 239 SER A O     1 
ATOM   1856 C  CB    . SER A 1 239 ? 19.31600  -14.17200 8.19900   1.000 27.95598  ? 239 SER A CB    1 
ATOM   1857 O  OG    . SER A 1 239 ? 18.69600  -15.08800 7.30400   1.000 24.74244  ? 239 SER A OG    1 
ATOM   1858 N  N     . TYR A 1 240 ? 16.15000  -14.66400 9.09500   1.000 28.23760  ? 240 TYR A N     1 
ATOM   1859 C  CA    . TYR A 1 240 ? 15.18300  -15.63300 9.59600   1.000 21.72103  ? 240 TYR A CA    1 
ATOM   1860 C  C     . TYR A 1 240 ? 15.37800  -17.02500 9.00800   1.000 18.88911  ? 240 TYR A C     1 
ATOM   1861 O  O     . TYR A 1 240 ? 14.79500  -17.98500 9.52200   1.000 21.42362  ? 240 TYR A O     1 
ATOM   1862 C  CB    . TYR A 1 240 ? 13.75400  -15.19200 9.26100   1.000 20.79460  ? 240 TYR A CB    1 
ATOM   1863 C  CG    . TYR A 1 240 ? 13.24900  -13.91900 9.91500   1.000 23.85812  ? 240 TYR A CG    1 
ATOM   1864 C  CD1   . TYR A 1 240 ? 14.04500  -13.16500 10.76200  1.000 27.27959  ? 240 TYR A CD1   1 
ATOM   1865 C  CD2   . TYR A 1 240 ? 11.96700  -13.46400 9.65100   1.000 20.26822  ? 240 TYR A CD2   1 
ATOM   1866 C  CE1   . TYR A 1 240 ? 13.56200  -11.99800 11.33900  1.000 22.07107  ? 240 TYR A CE1   1 
ATOM   1867 C  CE2   . TYR A 1 240 ? 11.48300  -12.30600 10.21200  1.000 24.56874  ? 240 TYR A CE2   1 
ATOM   1868 C  CZ    . TYR A 1 240 ? 12.27800  -11.57600 11.05600  1.000 24.07920  ? 240 TYR A CZ    1 
ATOM   1869 O  OH    . TYR A 1 240 ? 11.78600  -10.42400 11.61900  1.000 19.15493  ? 240 TYR A OH    1 
ATOM   1870 N  N     . ILE A 1 241 ? 16.15100  -17.15600 7.92500   1.000 25.69782  ? 241 ILE A N     1 
ATOM   1871 C  CA    . ILE A 1 241 ? 16.14700  -18.35800 7.09900   1.000 26.09523  ? 241 ILE A CA    1 
ATOM   1872 C  C     . ILE A 1 241 ? 17.57300  -18.72000 6.70000   1.000 25.56622  ? 241 ILE A C     1 
ATOM   1873 O  O     . ILE A 1 241 ? 18.51300  -17.93700 6.86600   1.000 23.07119  ? 241 ILE A O     1 
ATOM   1874 C  CB    . ILE A 1 241 ? 15.28100  -18.17300 5.83300   1.000 23.04750  ? 241 ILE A CB    1 
ATOM   1875 C  CG1   . ILE A 1 241 ? 15.77800  -16.96300 5.04100   1.000 25.43989  ? 241 ILE A CG1   1 
ATOM   1876 C  CG2   . ILE A 1 241 ? 13.81000  -18.00700 6.20700   1.000 26.21104  ? 241 ILE A CG2   1 
ATOM   1877 C  CD1   . ILE A 1 241 ? 15.23100  -16.86400 3.62700   1.000 27.76912  ? 241 ILE A CD1   1 
ATOM   1878 N  N     . ASP A 1 242 ? 17.70500  -19.91300 6.11500   1.000 34.86207  ? 242 ASP A N     1 
ATOM   1879 C  CA    . ASP A 1 242 ? 18.94400  -20.37600 5.49300   1.000 32.36704  ? 242 ASP A CA    1 
ATOM   1880 C  C     . ASP A 1 242 ? 19.21400  -19.55700 4.23100   1.000 30.90897  ? 242 ASP A C     1 
ATOM   1881 O  O     . ASP A 1 242 ? 18.39100  -19.53700 3.31000   1.000 31.68801  ? 242 ASP A O     1 
ATOM   1882 C  CB    . ASP A 1 242 ? 18.80400  -21.86400 5.15700   1.000 34.25674  ? 242 ASP A CB    1 
ATOM   1883 C  CG    . ASP A 1 242 ? 20.11900  -22.53400 4.77600   1.000 26.11892  ? 242 ASP A CG    1 
ATOM   1884 O  OD1   . ASP A 1 242 ? 21.05900  -21.84200 4.33900   1.000 29.65619  ? 242 ASP A OD1   1 
ATOM   1885 O  OD2   . ASP A 1 242 ? 20.18900  -23.78000 4.88600   1.000 30.17467  ? 242 ASP A OD2   1 
ATOM   1886 N  N     . LEU A 1 243 ? 20.35800  -18.87500 4.18700   1.000 21.49731  ? 243 LEU A N     1 
ATOM   1887 C  CA    . LEU A 1 243 ? 20.66000  -17.95200 3.09600   1.000 26.24525  ? 243 LEU A CA    1 
ATOM   1888 C  C     . LEU A 1 243 ? 21.34100  -18.62100 1.90000   1.000 22.38163  ? 243 LEU A C     1 
ATOM   1889 O  O     . LEU A 1 243 ? 21.77200  -17.91900 0.97700   1.000 28.07442  ? 243 LEU A O     1 
ATOM   1890 C  CB    . LEU A 1 243 ? 21.51100  -16.78600 3.61700   1.000 25.85836  ? 243 LEU A CB    1 
ATOM   1891 C  CG    . LEU A 1 243 ? 20.80000  -15.92800 4.66800   1.000 21.95790  ? 243 LEU A CG    1 
ATOM   1892 C  CD1   . LEU A 1 243 ? 21.72800  -14.88000 5.24600   1.000 20.85250  ? 243 LEU A CD1   1 
ATOM   1893 C  CD2   . LEU A 1 243 ? 19.56400  -15.27400 4.06300   1.000 32.03805  ? 243 LEU A CD2   1 
ATOM   1894 N  N     . LEU A 1 244 ? 21.44100  -19.95400 1.89600   1.000 21.65523  ? 244 LEU A N     1 
ATOM   1895 C  CA    . LEU A 1 244 ? 22.12700  -20.65900 0.81200   1.000 24.35292  ? 244 LEU A CA    1 
ATOM   1896 C  C     . LEU A 1 244 ? 21.40400  -20.50600 -0.52600  1.000 23.97393  ? 244 LEU A C     1 
ATOM   1897 O  O     . LEU A 1 244 ? 22.04500  -20.44500 -1.58500  1.000 28.50868  ? 244 LEU A O     1 
ATOM   1898 C  CB    . LEU A 1 244 ? 22.26900  -22.14100 1.17200   1.000 19.34969  ? 244 LEU A CB    1 
ATOM   1899 C  CG    . LEU A 1 244 ? 22.89700  -23.08800 0.14200   1.000 25.27145  ? 244 LEU A CG    1 
ATOM   1900 C  CD1   . LEU A 1 244 ? 24.30800  -22.65100 -0.22500  1.000 19.59709  ? 244 LEU A CD1   1 
ATOM   1901 C  CD2   . LEU A 1 244 ? 22.87800  -24.54000 0.63100   1.000 23.49229  ? 244 LEU A CD2   1 
ATOM   1902 N  N     . TYR A 1 245 ? 20.07300  -20.47400 -0.50100  1.000 23.35280  ? 245 TYR A N     1 
ATOM   1903 C  CA    . TYR A 1 245 ? 19.23100  -20.68300 -1.67200  1.000 21.44468  ? 245 TYR A CA    1 
ATOM   1904 C  C     . TYR A 1 245 ? 18.99600  -19.39300 -2.45300  1.000 24.06868  ? 245 TYR A C     1 
ATOM   1905 O  O     . TYR A 1 245 ? 19.18800  -18.28600 -1.93500  1.000 19.37074  ? 245 TYR A O     1 
ATOM   1906 C  CB    . TYR A 1 245 ? 17.90800  -21.31400 -1.23500  1.000 26.23999  ? 245 TYR A CB    1 
ATOM   1907 C  CG    . TYR A 1 245 ? 18.13400  -22.63400 -0.52600  1.000 28.46657  ? 245 TYR A CG    1 
ATOM   1908 C  CD1   . TYR A 1 245 ? 18.39200  -23.79200 -1.25100  1.000 29.23508  ? 245 TYR A CD1   1 
ATOM   1909 C  CD2   . TYR A 1 245 ? 18.14700  -22.71100 0.86000   1.000 31.46430  ? 245 TYR A CD2   1 
ATOM   1910 C  CE1   . TYR A 1 245 ? 18.61800  -24.99800 -0.61700  1.000 34.14620  ? 245 TYR A CE1   1 
ATOM   1911 C  CE2   . TYR A 1 245 ? 18.37600  -23.91600 1.50400   1.000 35.38582  ? 245 TYR A CE2   1 
ATOM   1912 C  CZ    . TYR A 1 245 ? 18.61300  -25.05400 0.76000   1.000 34.82260  ? 245 TYR A CZ    1 
ATOM   1913 O  OH    . TYR A 1 245 ? 18.83900  -26.25500 1.39400   1.000 40.37589  ? 245 TYR A OH    1 
ATOM   1914 N  N     . PRO A 1 246 ? 18.59600  -19.50400 -3.73900  1.000 20.10767  ? 246 PRO A N     1 
ATOM   1915 C  CA    . PRO A 1 246 ? 18.38600  -18.29500 -4.54500  1.000 21.87894  ? 246 PRO A CA    1 
ATOM   1916 C  C     . PRO A 1 246 ? 17.16700  -17.49800 -4.11100  1.000 24.37661  ? 246 PRO A C     1 
ATOM   1917 O  O     . PRO A 1 246 ? 16.39100  -17.93500 -3.25300  1.000 23.48966  ? 246 PRO A O     1 
ATOM   1918 C  CB    . PRO A 1 246 ? 18.22600  -18.83800 -5.97200  1.000 26.52950  ? 246 PRO A CB    1 
ATOM   1919 C  CG    . PRO A 1 246 ? 17.81900  -20.25700 -5.81300  1.000 26.62161  ? 246 PRO A CG    1 
ATOM   1920 C  CD    . PRO A 1 246 ? 18.43900  -20.73900 -4.53100  1.000 22.40532  ? 246 PRO A CD    1 
ATOM   1921 N  N     . THR A 1 247 ? 16.98300  -16.33900 -4.74900  1.000 22.32373  ? 247 THR A N     1 
ATOM   1922 C  CA    . THR A 1 247 ? 16.03200  -15.34600 -4.26700  1.000 26.17682  ? 247 THR A CA    1 
ATOM   1923 C  C     . THR A 1 247 ? 14.60100  -15.87700 -4.27300  1.000 26.69267  ? 247 THR A C     1 
ATOM   1924 O  O     . THR A 1 247 ? 13.83700  -15.61400 -3.33800  1.000 29.59829  ? 247 THR A O     1 
ATOM   1925 C  CB    . THR A 1 247 ? 16.15700  -14.07500 -5.10500  1.000 25.70571  ? 247 THR A CB    1 
ATOM   1926 O  OG1   . THR A 1 247 ? 17.49200  -13.56400 -4.98100  1.000 27.18221  ? 247 THR A OG1   1 
ATOM   1927 C  CG2   . THR A 1 247 ? 15.16900  -13.01500 -4.63000  1.000 27.36907  ? 247 THR A CG2   1 
ATOM   1928 N  N     . GLU A 1 248 ? 14.20300  -16.60100 -5.32300  1.000 23.82128  ? 248 GLU A N     1 
ATOM   1929 C  CA    . GLU A 1 248 ? 12.83000  -17.09900 -5.35600  1.000 30.21152  ? 248 GLU A CA    1 
ATOM   1930 C  C     . GLU A 1 248 ? 12.57200  -18.13000 -4.25700  1.000 27.67700  ? 248 GLU A C     1 
ATOM   1931 O  O     . GLU A 1 248 ? 11.47900  -18.15400 -3.68200  1.000 29.65092  ? 248 GLU A O     1 
ATOM   1932 C  CB    . GLU A 1 248 ? 12.49500  -17.64900 -6.75000  1.000 32.50653  ? 248 GLU A CB    1 
ATOM   1933 C  CG    . GLU A 1 248 ? 13.20800  -18.92900 -7.16800  1.000 40.25219  ? 248 GLU A CG    1 
ATOM   1934 C  CD    . GLU A 1 248 ? 12.68500  -19.47900 -8.49400  1.000 41.89713  ? 248 GLU A CD    1 
ATOM   1935 O  OE1   . GLU A 1 248 ? 11.92200  -18.76900 -9.18600  1.000 42.12347  ? 248 GLU A OE1   1 
ATOM   1936 O  OE2   . GLU A 1 248 ? 13.04900  -20.61900 -8.85300  1.000 31.34850  ? 248 GLU A OE2   1 
ATOM   1937 N  N     . ASP A 1 249 ? 13.56800  -18.95400 -3.91800  1.000 25.69255  ? 249 ASP A N     1 
ATOM   1938 C  CA    . ASP A 1 249 ? 13.41900  -19.89700 -2.80800  1.000 24.21869  ? 249 ASP A CA    1 
ATOM   1939 C  C     . ASP A 1 249 ? 13.33000  -19.18100 -1.46100  1.000 24.61348  ? 249 ASP A C     1 
ATOM   1940 O  O     . ASP A 1 249 ? 12.50700  -19.54600 -0.61200  1.000 32.90131  ? 249 ASP A O     1 
ATOM   1941 C  CB    . ASP A 1 249 ? 14.57600  -20.89800 -2.82800  1.000 25.19776  ? 249 ASP A CB    1 
ATOM   1942 C  CG    . ASP A 1 249 ? 14.50100  -21.85500 -4.01000  1.000 29.32720  ? 249 ASP A CG    1 
ATOM   1943 O  OD1   . ASP A 1 249 ? 13.59000  -21.70000 -4.84800  1.000 35.63848  ? 249 ASP A OD1   1 
ATOM   1944 O  OD2   . ASP A 1 249 ? 15.38100  -22.73300 -4.13100  1.000 36.89390  ? 249 ASP A OD2   1 
ATOM   1945 N  N     . ARG A 1 250 ? 14.18700  -18.18000 -1.23700  1.000 23.76864  ? 250 ARG A N     1 
ATOM   1946 C  CA    . ARG A 1 250 ? 14.14500  -17.41700 0.00900   1.000 22.88432  ? 250 ARG A CA    1 
ATOM   1947 C  C     . ARG A 1 250 ? 12.80500  -16.71600 0.16300   1.000 24.55031  ? 250 ARG A C     1 
ATOM   1948 O  O     . ARG A 1 250 ? 12.17400  -16.76600 1.22500   1.000 24.12131  ? 250 ARG A O     1 
ATOM   1949 C  CB    . ARG A 1 250 ? 15.27300  -16.38400 0.03000   1.000 22.27636  ? 250 ARG A CB    1 
ATOM   1950 C  CG    . ARG A 1 250 ? 16.68100  -16.95600 0.00600   1.000 22.06844  ? 250 ARG A CG    1 
ATOM   1951 C  CD    . ARG A 1 250 ? 17.70000  -15.94600 0.51200   1.000 17.91267  ? 250 ARG A CD    1 
ATOM   1952 N  NE    . ARG A 1 250 ? 17.63100  -14.67100 -0.20600  1.000 20.37350  ? 250 ARG A NE    1 
ATOM   1953 C  CZ    . ARG A 1 250 ? 18.17300  -14.45600 -1.40300  1.000 20.51299  ? 250 ARG A CZ    1 
ATOM   1954 N  NH1   . ARG A 1 250 ? 18.82000  -15.43300 -2.02800  1.000 20.38929  ? 250 ARG A NH1   1 
ATOM   1955 N  NH2   . ARG A 1 250 ? 18.07100  -13.26600 -1.97900  1.000 23.45808  ? 250 ARG A NH2   1 
ATOM   1956 N  N     . ASN A 1 251 ? 12.35500  -16.05800 -0.90300  1.000 22.88695  ? 251 ASN A N     1 
ATOM   1957 C  CA    A ASN A 1 251 ? 11.10800  -15.32000 -0.79300  0.500 25.60833  ? 251 ASN A CA    1 
ATOM   1958 C  CA    B ASN A 1 251 ? 11.09800  -15.31500 -0.92200  0.500 25.60833  ? 251 ASN A CA    1 
ATOM   1959 C  C     . ASN A 1 251 ? 9.89100   -16.23400 -0.75400  1.000 24.78192  ? 251 ASN A C     1 
ATOM   1960 O  O     . ASN A 1 251 ? 8.88200   -15.84500 -0.15700  1.000 29.26140  ? 251 ASN A O     1 
ATOM   1961 C  CB    A ASN A 1 251 ? 11.00200  -14.29400 -1.92000  0.500 29.43511  ? 251 ASN A CB    1 
ATOM   1962 C  CB    B ASN A 1 251 ? 11.03100  -14.54700 -2.24400  0.500 29.43511  ? 251 ASN A CB    1 
ATOM   1963 C  CG    A ASN A 1 251 ? 11.51000  -12.92700 -1.49400  0.500 54.45127  ? 251 ASN A CG    1 
ATOM   1964 C  CG    B ASN A 1 251 ? 9.81100   -13.67600 -2.37100  0.500 54.45127  ? 251 ASN A CG    1 
ATOM   1965 O  OD1   A ASN A 1 251 ? 11.14800  -12.43300 -0.42600  0.500 58.81495  ? 251 ASN A OD1   1 
ATOM   1966 O  OD1   B ASN A 1 251 ? 9.38600   -13.32300 -3.46700  0.500 58.81495  ? 251 ASN A OD1   1 
ATOM   1967 N  ND2   A ASN A 1 251 ? 12.36800  -12.32500 -2.30500  0.500 46.75561  ? 251 ASN A ND2   1 
ATOM   1968 N  ND2   B ASN A 1 251 ? 9.22000   -13.34100 -1.23000  0.500 46.75561  ? 251 ASN A ND2   1 
ATOM   1969 N  N     . ASP A 1 252 ? 9.96900   -17.44400 -1.31700  1.000 24.48978  ? 252 ASP A N     1 
ATOM   1970 C  CA    . ASP A 1 252 ? 8.91400   -18.43600 -1.12300  1.000 27.24537  ? 252 ASP A CA    1 
ATOM   1971 C  C     . ASP A 1 252 ? 8.76100   -18.78800 0.35500   1.000 25.39252  ? 252 ASP A C     1 
ATOM   1972 O  O     . ASP A 1 252 ? 7.64100   -18.84500 0.87900   1.000 23.75022  ? 252 ASP A O     1 
ATOM   1973 C  CB    . ASP A 1 252 ? 9.23000   -19.67900 -1.96500  1.000 35.69375  ? 252 ASP A CB    1 
ATOM   1974 C  CG    . ASP A 1 252 ? 8.26300   -20.83000 -1.73200  1.000 46.55558  ? 252 ASP A CG    1 
ATOM   1975 O  OD1   . ASP A 1 252 ? 8.46700   -21.60500 -0.76700  1.000 44.33426  ? 252 ASP A OD1   1 
ATOM   1976 O  OD2   . ASP A 1 252 ? 7.30900   -20.97200 -2.52900  1.000 41.42865  ? 252 ASP A OD2   1 
ATOM   1977 N  N     . ARG A 1 253 ? 9.88000   -19.00600 1.05000   1.000 22.02633  ? 253 ARG A N     1 
ATOM   1978 C  CA    . ARG A 1 253 ? 9.83000   -19.33500 2.47400   1.000 26.06892  ? 253 ARG A CA    1 
ATOM   1979 C  C     . ARG A 1 253 ? 9.36500   -18.14800 3.31400   1.000 21.26044  ? 253 ARG A C     1 
ATOM   1980 O  O     . ARG A 1 253 ? 8.54300   -18.30900 4.22300   1.000 24.93983  ? 253 ARG A O     1 
ATOM   1981 C  CB    . ARG A 1 253 ? 11.20800  -19.82000 2.93900   1.000 25.02142  ? 253 ARG A CB    1 
ATOM   1982 C  CG    . ARG A 1 253 ? 11.28200  -20.23300 4.40700   1.000 44.09476  ? 253 ARG A CG    1 
ATOM   1983 C  CD    . ARG A 1 253 ? 10.39100  -21.41800 4.73300   1.000 60.15195  ? 253 ARG A CD    1 
ATOM   1984 N  NE    . ARG A 1 253 ? 11.09800  -22.68600 4.58700   1.000 97.49853  ? 253 ARG A NE    1 
ATOM   1985 C  CZ    . ARG A 1 253 ? 11.95900  -23.16900 5.47900   1.000 89.33440  ? 253 ARG A CZ    1 
ATOM   1986 N  NH1   . ARG A 1 253 ? 12.22900  -22.48800 6.58600   1.000 103.46240 ? 253 ARG A NH1   1 
ATOM   1987 N  NH2   . ARG A 1 253 ? 12.55600  -24.33400 5.26100   1.000 89.87393  ? 253 ARG A NH2   1 
ATOM   1988 N  N     . LEU A 1 254 ? 9.89600   -16.95200 3.04000   1.000 21.87894  ? 254 LEU A N     1 
ATOM   1989 C  CA    . LEU A 1 254 ? 9.53400   -15.77100 3.82500   1.000 19.54708  ? 254 LEU A CA    1 
ATOM   1990 C  C     . LEU A 1 254 ? 8.05500   -15.42800 3.67600   1.000 26.28473  ? 254 LEU A C     1 
ATOM   1991 O  O     . LEU A 1 254 ? 7.38800   -15.08900 4.66200   1.000 20.91040  ? 254 LEU A O     1 
ATOM   1992 C  CB    . LEU A 1 254 ? 10.39500  -14.57700 3.40800   1.000 20.53141  ? 254 LEU A CB    1 
ATOM   1993 C  CG    . LEU A 1 254 ? 11.89000  -14.68800 3.68800   1.000 22.32899  ? 254 LEU A CG    1 
ATOM   1994 C  CD1   . LEU A 1 254 ? 12.61700  -13.48900 3.10600   1.000 21.46047  ? 254 LEU A CD1   1 
ATOM   1995 C  CD2   . LEU A 1 254 ? 12.15400  -14.82900 5.18400   1.000 23.14488  ? 254 LEU A CD2   1 
ATOM   1996 N  N     . ARG A 1 255 ? 7.53400   -15.47400 2.44400   1.000 21.52890  ? 255 ARG A N     1 
ATOM   1997 C  CA    . ARG A 1 255 ? 6.10900   -15.23600 2.23100   1.000 27.51383  ? 255 ARG A CA    1 
ATOM   1998 C  C     . ARG A 1 255 ? 5.25900   -16.25900 2.97100   1.000 27.36381  ? 255 ARG A C     1 
ATOM   1999 O  O     . ARG A 1 255 ? 4.26900   -15.90700 3.62600   1.000 35.36213  ? 255 ARG A O     1 
ATOM   2000 C  CB    . ARG A 1 255 ? 5.76900   -15.27700 0.74200   1.000 27.25327  ? 255 ARG A CB    1 
ATOM   2001 C  CG    . ARG A 1 255 ? 5.99600   -14.00600 -0.03800  1.000 41.04966  ? 255 ARG A CG    1 
ATOM   2002 C  CD    . ARG A 1 255 ? 5.57600   -14.25900 -1.48000  1.000 40.51275  ? 255 ARG A CD    1 
ATOM   2003 N  NE    . ARG A 1 255 ? 6.11200   -13.28600 -2.42400  1.000 54.51180  ? 255 ARG A NE    1 
ATOM   2004 C  CZ    . ARG A 1 255 ? 6.43700   -13.57300 -3.68000  1.000 71.51121  ? 255 ARG A CZ    1 
ATOM   2005 N  NH1   . ARG A 1 255 ? 6.29900   -14.81200 -4.13600  1.000 70.44002  ? 255 ARG A NH1   1 
ATOM   2006 N  NH2   . ARG A 1 255 ? 6.90100   -12.62200 -4.47900  1.000 87.20519  ? 255 ARG A NH2   1 
ATOM   2007 N  N     . ASP A 1 256 ? 5.61900   -17.54000 2.85700   1.000 31.54589  ? 256 ASP A N     1 
ATOM   2008 C  CA    . ASP A 1 256 ? 4.80500   -18.59300 3.45600   1.000 31.89330  ? 256 ASP A CA    1 
ATOM   2009 C  C     . ASP A 1 256 ? 4.79400   -18.50400 4.97700   1.000 30.36680  ? 256 ASP A C     1 
ATOM   2010 O  O     . ASP A 1 256 ? 3.74400   -18.68200 5.60100   1.000 31.75118  ? 256 ASP A O     1 
ATOM   2011 C  CB    . ASP A 1 256 ? 5.30500   -19.96600 3.01000   1.000 42.24980  ? 256 ASP A CB    1 
ATOM   2012 C  CG    . ASP A 1 256 ? 4.36300   -21.08700 3.41700   1.000 34.69100  ? 256 ASP A CG    1 
ATOM   2013 O  OD1   . ASP A 1 256 ? 3.14600   -20.98000 3.14600   1.000 57.06474  ? 256 ASP A OD1   1 
ATOM   2014 O  OD2   . ASP A 1 256 ? 4.83900   -22.07400 4.02100   1.000 61.71003  ? 256 ASP A OD2   1 
ATOM   2015 N  N     . SER A 1 257 ? 5.94400   -18.22800 5.59400   1.000 26.30842  ? 257 SER A N     1 
ATOM   2016 C  CA    . SER A 1 257 ? 6.05300   -18.29200 7.04900   1.000 34.41202  ? 257 SER A CA    1 
ATOM   2017 C  C     . SER A 1 257 ? 5.83700   -16.95000 7.73800   1.000 29.11665  ? 257 SER A C     1 
ATOM   2018 O  O     . SER A 1 257 ? 5.31200   -16.91700 8.85800   1.000 28.23496  ? 257 SER A O     1 
ATOM   2019 C  CB    . SER A 1 257 ? 7.42200   -18.84400 7.45400   1.000 35.90430  ? 257 SER A CB    1 
ATOM   2020 O  OG    . SER A 1 257 ? 7.58600   -20.17100 6.99300   1.000 32.70655  ? 257 SER A OG    1 
ATOM   2021 N  N     . TYR A 1 258 ? 6.23900   -15.84600 7.10900   1.000 32.34335  ? 258 TYR A N     1 
ATOM   2022 C  CA    . TYR A 1 258 ? 6.21800   -14.54000 7.75000   1.000 27.15852  ? 258 TYR A CA    1 
ATOM   2023 C  C     . TYR A 1 258 ? 5.41100   -13.50000 6.98400   1.000 23.61336  ? 258 TYR A C     1 
ATOM   2024 O  O     . TYR A 1 258 ? 5.34300   -12.34400 7.41900   1.000 26.01891  ? 258 TYR A O     1 
ATOM   2025 C  CB    . TYR A 1 258 ? 7.65900   -14.06200 7.97600   1.000 26.51107  ? 258 TYR A CB    1 
ATOM   2026 C  CG    . TYR A 1 258 ? 8.46800   -15.08100 8.75600   1.000 29.28772  ? 258 TYR A CG    1 
ATOM   2027 C  CD1   . TYR A 1 258 ? 8.27300   -15.25200 10.12800  1.000 30.37733  ? 258 TYR A CD1   1 
ATOM   2028 C  CD2   . TYR A 1 258 ? 9.38100   -15.91400 8.11600   1.000 30.11677  ? 258 TYR A CD2   1 
ATOM   2029 C  CE1   . TYR A 1 258 ? 8.99900   -16.20200 10.84800  1.000 33.36189  ? 258 TYR A CE1   1 
ATOM   2030 C  CE2   . TYR A 1 258 ? 10.10400  -16.86700 8.82400   1.000 30.06413  ? 258 TYR A CE2   1 
ATOM   2031 C  CZ    . TYR A 1 258 ? 9.90900   -17.00700 10.18600  1.000 29.17718  ? 258 TYR A CZ    1 
ATOM   2032 O  OH    . TYR A 1 258 ? 10.63100  -17.95200 10.88300  1.000 39.47842  ? 258 TYR A OH    1 
ATOM   2033 N  N     . PHE A 1 259 ? 4.82200   -13.86700 5.84400   1.000 25.43200  ? 259 PHE A N     1 
ATOM   2034 C  CA    . PHE A 1 259 ? 3.83600   -13.03600 5.15000   1.000 27.03482  ? 259 PHE A CA    1 
ATOM   2035 C  C     . PHE A 1 259 ? 4.41300   -11.68800 4.73000   1.000 27.53225  ? 259 PHE A C     1 
ATOM   2036 O  O     . PHE A 1 259 ? 3.79100   -10.63800 4.89700   1.000 25.47148  ? 259 PHE A O     1 
ATOM   2037 C  CB    . PHE A 1 259 ? 2.59000   -12.85900 6.02100   1.000 35.29371  ? 259 PHE A CB    1 
ATOM   2038 C  CG    . PHE A 1 259 ? 1.96400   -14.15800 6.41500   1.000 31.47746  ? 259 PHE A CG    1 
ATOM   2039 C  CD1   . PHE A 1 259 ? 1.09200   -14.80500 5.55000   1.000 36.15433  ? 259 PHE A CD1   1 
ATOM   2040 C  CD2   . PHE A 1 259 ? 2.28900   -14.76200 7.61700   1.000 31.08531  ? 259 PHE A CD2   1 
ATOM   2041 C  CE1   . PHE A 1 259 ? 0.53000   -16.01700 5.88900   1.000 38.16773  ? 259 PHE A CE1   1 
ATOM   2042 C  CE2   . PHE A 1 259 ? 1.72800   -15.97600 7.96700   1.000 40.62856  ? 259 PHE A CE2   1 
ATOM   2043 C  CZ    . PHE A 1 259 ? 0.84700   -16.60500 7.09800   1.000 39.25207  ? 259 PHE A CZ    1 
ATOM   2044 N  N     . PHE A 1 260 ? 5.61000   -11.72400 4.15300   1.000 26.81901  ? 260 PHE A N     1 
ATOM   2045 C  CA    . PHE A 1 260 ? 6.17800   -10.52800 3.55600   1.000 28.02968  ? 260 PHE A CA    1 
ATOM   2046 C  C     . PHE A 1 260 ? 7.11700   -10.94700 2.43800   1.000 23.10014  ? 260 PHE A C     1 
ATOM   2047 O  O     . PHE A 1 260 ? 7.62300   -12.07000 2.41400   1.000 26.43212  ? 260 PHE A O     1 
ATOM   2048 C  CB    . PHE A 1 260 ? 6.92100   -9.66600  4.58800   1.000 28.53500  ? 260 PHE A CB    1 
ATOM   2049 C  CG    . PHE A 1 260 ? 8.27200   -10.20900 4.99000   1.000 24.05552  ? 260 PHE A CG    1 
ATOM   2050 C  CD1   . PHE A 1 260 ? 8.38800   -11.12000 6.02800   1.000 30.66947  ? 260 PHE A CD1   1 
ATOM   2051 C  CD2   . PHE A 1 260 ? 9.42900   -9.79000  4.33600   1.000 23.21857  ? 260 PHE A CD2   1 
ATOM   2052 C  CE1   . PHE A 1 260 ? 9.62800   -11.61600 6.40500   1.000 27.69806  ? 260 PHE A CE1   1 
ATOM   2053 C  CE2   . PHE A 1 260 ? 10.66700  -10.28000 4.70800   1.000 23.41597  ? 260 PHE A CE2   1 
ATOM   2054 C  CZ    . PHE A 1 260 ? 10.76600  -11.19500 5.74600   1.000 24.40029  ? 260 PHE A CZ    1 
ATOM   2055 N  N     . THR A 1 261 ? 7.35700   -10.01200 1.52400   1.000 20.76038  ? 261 THR A N     1 
ATOM   2056 C  CA    . THR A 1 261 ? 8.30700   -10.17000 0.43200   1.000 26.49265  ? 261 THR A CA    1 
ATOM   2057 C  C     . THR A 1 261 ? 9.51000   -9.28700  0.72400   1.000 23.31332  ? 261 THR A C     1 
ATOM   2058 O  O     . THR A 1 261 ? 9.37000   -8.06500  0.83100   1.000 25.95048  ? 261 THR A O     1 
ATOM   2059 C  CB    . THR A 1 261 ? 7.67400   -9.77000  -0.90000  1.000 32.13017  ? 261 THR A CB    1 
ATOM   2060 O  OG1   . THR A 1 261 ? 6.52100   -10.58200 -1.14500  1.000 31.09583  ? 261 THR A OG1   1 
ATOM   2061 C  CG2   . THR A 1 261 ? 8.66900   -9.93500  -2.02900  1.000 34.64100  ? 261 THR A CG2   1 
ATOM   2062 N  N     . CYS A 1 262 ? 10.68700  -9.90200  0.81800   1.000 27.17431  ? 262 CYS A N     1 
ATOM   2063 C  CA    . CYS A 1 262 ? 11.89100  -9.17100  1.18100   1.000 29.01401  ? 262 CYS A CA    1 
ATOM   2064 C  C     . CYS A 1 262 ? 12.35900  -8.28100  0.03400   1.000 28.10600  ? 262 CYS A C     1 
ATOM   2065 O  O     . CYS A 1 262 ? 12.27300  -8.65600  -1.13800  1.000 37.31500  ? 262 CYS A O     1 
ATOM   2066 C  CB    . CYS A 1 262 ? 12.99300  -10.15700 1.56600   1.000 26.06365  ? 262 CYS A CB    1 
ATOM   2067 S  SG    . CYS A 1 262 ? 14.46000  -9.38700  2.22600   1.000 25.22934  ? 262 CYS A SG    1 
ATOM   2068 N  N     . GLU A 1 263 ? 12.88000  -7.10100  0.38400   1.000 35.06210  ? 263 GLU A N     1 
ATOM   2069 C  CA    . GLU A 1 263 ? 13.38400  -6.13900  -0.59000  1.000 30.86686  ? 263 GLU A CA    1 
ATOM   2070 C  C     . GLU A 1 263 ? 14.81100  -5.71000  -0.26400  1.000 28.31655  ? 263 GLU A C     1 
ATOM   2071 O  O     . GLU A 1 263 ? 15.24200  -4.62200  -0.65800  1.000 28.69555  ? 263 GLU A O     1 
ATOM   2072 C  CB    . GLU A 1 263 ? 12.47000  -4.91600  -0.68400  1.000 33.39348  ? 263 GLU A CB    1 
ATOM   2073 C  CG    . GLU A 1 263 ? 11.06800  -5.22600  -1.17700  1.000 46.02920  ? 263 GLU A CG    1 
ATOM   2074 C  CD    . GLU A 1 263 ? 10.16000  -4.00900  -1.17600  1.000 59.95192  ? 263 GLU A CD    1 
ATOM   2075 O  OE1   . GLU A 1 263 ? 10.65000  -2.88900  -0.90900  1.000 61.02574  ? 263 GLU A OE1   1 
ATOM   2076 O  OE2   . GLU A 1 263 ? 8.94800   -4.17500  -1.43100  1.000 64.02873  ? 263 GLU A OE2   1 
ATOM   2077 N  N     . CYS A 1 264 ? 15.56400  -6.55500  0.43400   1.000 27.98230  ? 264 CYS A N     1 
ATOM   2078 C  CA    . CYS A 1 264 ? 16.96300  -6.25400  0.70200   1.000 31.16163  ? 264 CYS A CA    1 
ATOM   2079 C  C     . CYS A 1 264 ? 17.75600  -6.23700  -0.60600  1.000 30.39312  ? 264 CYS A C     1 
ATOM   2080 O  O     . CYS A 1 264 ? 17.24400  -6.56800  -1.68100  1.000 30.05887  ? 264 CYS A O     1 
ATOM   2081 C  CB    . CYS A 1 264 ? 17.55200  -7.27000  1.68100   1.000 31.25901  ? 264 CYS A CB    1 
ATOM   2082 S  SG    . CYS A 1 264 ? 17.98400  -8.87300  0.94100   1.000 28.83767  ? 264 CYS A SG    1 
ATOM   2083 N  N     . GLN A 1 265 ? 19.02300  -5.81800  -0.50700  1.000 27.84018  ? 265 GLN A N     1 
ATOM   2084 C  CA    . GLN A 1 265 ? 19.86200  -5.69400  -1.69900  1.000 33.83300  ? 265 GLN A CA    1 
ATOM   2085 C  C     . GLN A 1 265 ? 20.02000  -7.02800  -2.42300  1.000 33.24609  ? 265 GLN A C     1 
ATOM   2086 O  O     . GLN A 1 265 ? 20.00000  -7.07000  -3.65900  1.000 27.09272  ? 265 GLN A O     1 
ATOM   2087 C  CB    . GLN A 1 265 ? 21.23400  -5.13000  -1.33200  1.000 35.73586  ? 265 GLN A CB    1 
ATOM   2088 C  CG    . GLN A 1 265 ? 22.05200  -4.71700  -2.54100  1.000 62.01533  ? 265 GLN A CG    1 
ATOM   2089 C  CD    . GLN A 1 265 ? 23.35800  -4.05300  -2.16300  1.000 64.75250  ? 265 GLN A CD    1 
ATOM   2090 O  OE1   . GLN A 1 265 ? 24.02700  -4.47000  -1.21600  1.000 71.33750  ? 265 GLN A OE1   1 
ATOM   2091 N  NE2   . GLN A 1 265 ? 23.73100  -3.01400  -2.90400  1.000 86.11822  ? 265 GLN A NE2   1 
ATOM   2092 N  N     . GLU A 1 266 ? 20.20800  -8.12600  -1.67600  1.000 24.72665  ? 266 GLU A N     1 
ATOM   2093 C  CA    . GLU A 1 266 ? 20.34600  -9.43500  -2.31300  1.000 23.78969  ? 266 GLU A CA    1 
ATOM   2094 C  C     . GLU A 1 266 ? 19.09300  -9.81400  -3.09200  1.000 25.91100  ? 266 GLU A C     1 
ATOM   2095 O  O     . GLU A 1 266 ? 19.18600  -10.32900 -4.21100  1.000 23.44492  ? 266 GLU A O     1 
ATOM   2096 C  CB    . GLU A 1 266 ? 20.66700  -10.51300 -1.27700  1.000 30.52208  ? 266 GLU A CB    1 
ATOM   2097 C  CG    . GLU A 1 266 ? 22.09400  -10.47000 -0.76300  1.000 53.41167  ? 266 GLU A CG    1 
ATOM   2098 C  CD    . GLU A 1 266 ? 23.11200  -10.78700 -1.85400  1.000 50.40868  ? 266 GLU A CD    1 
ATOM   2099 O  OE1   . GLU A 1 266 ? 22.73100  -11.41800 -2.86900  1.000 65.51838  ? 266 GLU A OE1   1 
ATOM   2100 O  OE2   . GLU A 1 266 ? 24.29000  -10.39700 -1.69600  1.000 61.92058  ? 266 GLU A OE2   1 
ATOM   2101 N  N     . CYS A 1 267 ? 17.91000  -9.57300  -2.51700  1.000 29.78252  ? 267 CYS A N     1 
ATOM   2102 C  CA    . CYS A 1 267 ? 16.67100  -9.89200  -3.21900  1.000 33.12766  ? 267 CYS A CA    1 
ATOM   2103 C  C     . CYS A 1 267 ? 16.43300  -8.94200  -4.38800  1.000 31.21427  ? 267 CYS A C     1 
ATOM   2104 O  O     . CYS A 1 267 ? 15.93100  -9.36000  -5.43900  1.000 29.95096  ? 267 CYS A O     1 
ATOM   2105 C  CB    . CYS A 1 267 ? 15.49400  -9.85900  -2.24500  1.000 25.65834  ? 267 CYS A CB    1 
ATOM   2106 S  SG    . CYS A 1 267 ? 15.52100  -11.21200 -1.05200  1.000 26.75058  ? 267 CYS A SG    1 
ATOM   2107 N  N     . THR A 1 268 ? 16.77900  -7.66100  -4.22100  1.000 23.93445  ? 268 THR A N     1 
ATOM   2108 C  CA    . THR A 1 268 ? 16.56000  -6.67200  -5.27200  1.000 27.92966  ? 268 THR A CA    1 
ATOM   2109 C  C     . THR A 1 268 ? 17.46200  -6.92400  -6.47600  1.000 27.02166  ? 268 THR A C     1 
ATOM   2110 O  O     . THR A 1 268 ? 17.00200  -6.91100  -7.62300  1.000 29.17718  ? 268 THR A O     1 
ATOM   2111 C  CB    . THR A 1 268 ? 16.79100  -5.26600  -4.71300  1.000 30.92739  ? 268 THR A CB    1 
ATOM   2112 O  OG1   . THR A 1 268 ? 15.87600  -5.02400  -3.63800  1.000 36.60439  ? 268 THR A OG1   1 
ATOM   2113 C  CG2   . THR A 1 268 ? 16.59200  -4.21400  -5.79200  1.000 41.52866  ? 268 THR A CG2   1 
ATOM   2114 N  N     . THR A 1 269 ? 18.75700  -7.14400  -6.23500  1.000 25.15565  ? 269 THR A N     1 
ATOM   2115 C  CA    . THR A 1 269 ? 19.70700  -7.32700  -7.32400  1.000 25.28987  ? 269 THR A CA    1 
ATOM   2116 C  C     . THR A 1 269 ? 19.72500  -8.76100  -7.83200  1.000 22.91854  ? 269 THR A C     1 
ATOM   2117 O  O     . THR A 1 269 ? 19.99400  -8.98500  -9.01700  1.000 29.00348  ? 269 THR A O     1 
ATOM   2118 C  CB    . THR A 1 269 ? 21.11700  -6.94600  -6.87300  1.000 24.26344  ? 269 THR A CB    1 
ATOM   2119 O  OG1   . THR A 1 269 ? 21.58500  -7.89700  -5.90700  1.000 21.98421  ? 269 THR A OG1   1 
ATOM   2120 C  CG2   . THR A 1 269 ? 21.11900  -5.56000  -6.24700  1.000 27.35328  ? 269 THR A CG2   1 
ATOM   2121 N  N     . LYS A 1 270 ? 19.47200  -9.73700  -6.95200  1.000 23.68179  ? 270 LYS A N     1 
ATOM   2122 C  CA    . LYS A 1 270 ? 19.60600  -11.15800 -7.28600  1.000 29.13244  ? 270 LYS A CA    1 
ATOM   2123 C  C     . LYS A 1 270 ? 21.02100  -11.48600 -7.75700  1.000 29.44300  ? 270 LYS A C     1 
ATOM   2124 O  O     . LYS A 1 270 ? 21.21700  -12.37800 -8.58700  1.000 35.47531  ? 270 LYS A O     1 
ATOM   2125 C  CB    . LYS A 1 270 ? 18.57700  -11.58400 -8.34400  1.000 28.04810  ? 270 LYS A CB    1 
ATOM   2126 C  CG    . LYS A 1 270 ? 17.12900  -11.30400 -7.95200  1.000 39.14680  ? 270 LYS A CG    1 
ATOM   2127 C  CD    . LYS A 1 270 ? 16.15600  -11.76400 -9.02100  1.000 43.38152  ? 270 LYS A CD    1 
ATOM   2128 C  CE    . LYS A 1 270 ? 14.71300  -11.57200 -8.56800  1.000 58.95181  ? 270 LYS A CE    1 
ATOM   2129 N  NZ    . LYS A 1 270 ? 13.73000  -11.86600 -9.65500  1.000 63.99715  ? 270 LYS A NZ    1 
ATOM   2130 N  N     . ASP A 1 271 ? 22.01500  -10.75700 -7.23700  1.000 29.01401  ? 271 ASP A N     1 
ATOM   2131 C  CA    . ASP A 1 271 ? 23.37000  -10.84700 -7.78000  1.000 33.04607  ? 271 ASP A CA    1 
ATOM   2132 C  C     . ASP A 1 271 ? 23.98600  -12.23200 -7.62100  1.000 32.24334  ? 271 ASP A C     1 
ATOM   2133 O  O     . ASP A 1 271 ? 24.82600  -12.62400 -8.43900  1.000 29.02716  ? 271 ASP A O     1 
ATOM   2134 C  CB    . ASP A 1 271 ? 24.26200  -9.78300  -7.14200  1.000 36.35436  ? 271 ASP A CB    1 
ATOM   2135 C  CG    . ASP A 1 271 ? 24.37200  -8.53800  -8.00000  1.000 38.54936  ? 271 ASP A CG    1 
ATOM   2136 O  OD1   . ASP A 1 271 ? 23.76900  -8.52500  -9.09600  1.000 33.77510  ? 271 ASP A OD1   1 
ATOM   2137 O  OD2   . ASP A 1 271 ? 25.06400  -7.58100  -7.59400  1.000 33.31715  ? 271 ASP A OD2   1 
ATOM   2138 N  N     . LYS A 1 272 ? 23.59400  -12.98400 -6.59100  1.000 22.73167  ? 272 LYS A N     1 
ATOM   2139 C  CA    . LYS A 1 272 ? 24.14700  -14.31200 -6.34200  1.000 27.45856  ? 272 LYS A CA    1 
ATOM   2140 C  C     . LYS A 1 272 ? 23.32100  -15.44000 -6.94800  1.000 28.06389  ? 272 LYS A C     1 
ATOM   2141 O  O     . LYS A 1 272 ? 23.72400  -16.60500 -6.84300  1.000 27.42960  ? 272 LYS A O     1 
ATOM   2142 C  CB    . LYS A 1 272 ? 24.29400  -14.54800 -4.83900  1.000 27.99020  ? 272 LYS A CB    1 
ATOM   2143 C  CG    . LYS A 1 272 ? 25.42200  -13.76500 -4.19400  1.000 24.62664  ? 272 LYS A CG    1 
ATOM   2144 C  CD    . LYS A 1 272 ? 25.68900  -14.28800 -2.80000  1.000 35.09368  ? 272 LYS A CD    1 
ATOM   2145 C  CE    . LYS A 1 272 ? 26.92900  -13.66600 -2.19800  1.000 36.06748  ? 272 LYS A CE    1 
ATOM   2146 N  NZ    . LYS A 1 272 ? 27.34200  -14.38600 -0.96300  1.000 32.43547  ? 272 LYS A NZ    1 
ATOM   2147 N  N     . ASP A 1 273 ? 22.17900  -15.13000 -7.56500  1.000 24.89509  ? 273 ASP A N     1 
ATOM   2148 C  CA    . ASP A 1 273 ? 21.29200  -16.17100 -8.07700  1.000 31.69064  ? 273 ASP A CA    1 
ATOM   2149 C  C     . ASP A 1 273 ? 21.99300  -17.06400 -9.09600  1.000 30.37469  ? 273 ASP A C     1 
ATOM   2150 O  O     . ASP A 1 273 ? 21.84900  -18.29000 -9.05800  1.000 25.80836  ? 273 ASP A O     1 
ATOM   2151 C  CB    . ASP A 1 273 ? 20.03900  -15.54400 -8.69100  1.000 27.11378  ? 273 ASP A CB    1 
ATOM   2152 C  CG    . ASP A 1 273 ? 18.95700  -15.26000 -7.65900  1.000 34.16462  ? 273 ASP A CG    1 
ATOM   2153 O  OD1   . ASP A 1 273 ? 19.24900  -15.29100 -6.43900  1.000 30.21941  ? 273 ASP A OD1   1 
ATOM   2154 O  OD2   . ASP A 1 273 ? 17.80400  -15.01800 -8.07600  1.000 38.68095  ? 273 ASP A OD2   1 
ATOM   2155 N  N     . LYS A 1 274 ? 22.74000  -16.46500 -10.02900 1.000 22.53428  ? 274 LYS A N     1 
ATOM   2156 C  CA    . LYS A 1 274 ? 23.32000  -17.24700 -11.11900 1.000 26.47949  ? 274 LYS A CA    1 
ATOM   2157 C  C     . LYS A 1 274 ? 24.38700  -18.21700 -10.62400 1.000 20.83671  ? 274 LYS A C     1 
ATOM   2158 O  O     . LYS A 1 274 ? 24.44900  -19.36400 -11.08100 1.000 19.34969  ? 274 LYS A O     1 
ATOM   2159 C  CB    . LYS A 1 274 ? 23.90300  -16.31100 -12.17700 1.000 37.68083  ? 274 LYS A CB    1 
ATOM   2160 C  CG    . LYS A 1 274 ? 22.85400  -15.50500 -12.93500 1.000 45.93709  ? 274 LYS A CG    1 
ATOM   2161 C  CD    . LYS A 1 274 ? 22.04400  -16.38100 -13.88000 1.000 71.04010  ? 274 LYS A CD    1 
ATOM   2162 C  CE    . LYS A 1 274 ? 20.90100  -15.60300 -14.52000 1.000 64.07084  ? 274 LYS A CE    1 
ATOM   2163 N  NZ    . LYS A 1 274 ? 21.37800  -14.41000 -15.27300 1.000 85.92609  ? 274 LYS A NZ    1 
ATOM   2164 N  N     . ALA A 1 275 ? 25.23800  -17.78300 -9.69400  1.000 25.36357  ? 275 ALA A N     1 
ATOM   2165 C  CA    . ALA A 1 275 ? 26.23100  -18.69300 -9.13200  1.000 24.47399  ? 275 ALA A CA    1 
ATOM   2166 C  C     . ALA A 1 275 ? 25.57800  -19.80600 -8.32100  1.000 27.61647  ? 275 ALA A C     1 
ATOM   2167 O  O     . ALA A 1 275 ? 26.07100  -20.94000 -8.31300  1.000 25.50043  ? 275 ALA A O     1 
ATOM   2168 C  CB    . ALA A 1 275 ? 27.22200  -17.91500 -8.26300  1.000 26.44791  ? 275 ALA A CB    1 
ATOM   2169 N  N     . LYS A 1 276 ? 24.46400  -19.50900 -7.64800  1.000 31.53010  ? 276 LYS A N     1 
ATOM   2170 C  CA    . LYS A 1 276 ? 23.80800  -20.52300 -6.83200  1.000 25.81362  ? 276 LYS A CA    1 
ATOM   2171 C  C     . LYS A 1 276 ? 23.19700  -21.62600 -7.68800  1.000 27.76649  ? 276 LYS A C     1 
ATOM   2172 O  O     . LYS A 1 276 ? 23.12800  -22.77900 -7.25200  1.000 27.35328  ? 276 LYS A O     1 
ATOM   2173 C  CB    . LYS A 1 276 ? 22.74000  -19.88100 -5.94400  1.000 25.23987  ? 276 LYS A CB    1 
ATOM   2174 C  CG    . LYS A 1 276 ? 23.30900  -19.07800 -4.79400  1.000 22.59218  ? 276 LYS A CG    1 
ATOM   2175 C  CD    . LYS A 1 276 ? 22.24200  -18.31300 -4.02800  1.000 22.76589  ? 276 LYS A CD    1 
ATOM   2176 C  CE    . LYS A 1 276 ? 22.88000  -17.59900 -2.82600  1.000 25.83204  ? 276 LYS A CE    1 
ATOM   2177 N  NZ    . LYS A 1 276 ? 21.88700  -16.89100 -1.97100  1.000 32.69866  ? 276 LYS A NZ    1 
ATOM   2178 N  N     . VAL A 1 277 ? 22.73400  -21.30000 -8.89000  1.000 23.72127  ? 277 VAL A N     1 
ATOM   2179 C  CA    . VAL A 1 277 ? 22.13700  -22.30300 -9.76700  1.000 26.94534  ? 277 VAL A CA    1 
ATOM   2180 C  C     . VAL A 1 277 ? 23.04600  -22.50000 -10.97600 1.000 29.02716  ? 277 VAL A C     1 
ATOM   2181 O  O     . VAL A 1 277 ? 22.59900  -22.43400 -12.12700 1.000 37.75979  ? 277 VAL A O     1 
ATOM   2182 C  CB    . VAL A 1 277 ? 20.70700  -21.89500 -10.17200 1.000 28.46394  ? 277 VAL A CB    1 
ATOM   2183 C  CG1   . VAL A 1 277 ? 19.95900  -23.06700 -10.80700 1.000 29.52722  ? 277 VAL A CG1   1 
ATOM   2184 C  CG2   . VAL A 1 277 ? 19.94600  -21.41000 -8.94100  1.000 25.97943  ? 277 VAL A CG2   1 
ATOM   2185 N  N     . GLU A 1 278 ? 24.32700  -22.76000 -10.72200 1.000 34.16462  ? 278 GLU A N     1 
ATOM   2186 C  CA    . GLU A 1 278 ? 25.29900  -22.84000 -11.80300 1.000 38.38881  ? 278 GLU A CA    1 
ATOM   2187 C  C     . GLU A 1 278 ? 25.02400  -24.05100 -12.68500 1.000 45.46335  ? 278 GLU A C     1 
ATOM   2188 O  O     . GLU A 1 278 ? 24.71800  -25.14100 -12.19300 1.000 32.84341  ? 278 GLU A O     1 
ATOM   2189 C  CB    . GLU A 1 278 ? 26.72000  -22.90700 -11.24600 1.000 39.39683  ? 278 GLU A CB    1 
ATOM   2190 C  CG    . GLU A 1 278 ? 27.79100  -22.74800 -12.31700 1.000 51.47722  ? 278 GLU A CG    1 
ATOM   2191 C  CD    . GLU A 1 278 ? 29.20100  -22.68600 -11.74900 1.000 75.48537  ? 278 GLU A CD    1 
ATOM   2192 O  OE1   . GLU A 1 278 ? 29.44800  -23.29500 -10.68500 1.000 103.10973 ? 278 GLU A OE1   1 
ATOM   2193 O  OE2   . GLU A 1 278 ? 30.06700  -22.03900 -12.37700 1.000 81.00708  ? 278 GLU A OE2   1 
ATOM   2194 N  N     . ILE A 1 279 ? 25.12500  -23.83900 -13.99800 1.000 34.82786  ? 279 ILE A N     1 
ATOM   2195 C  CA    . ILE A 1 279 ? 24.85200  -24.84100 -15.02200 1.000 35.94642  ? 279 ILE A CA    1 
ATOM   2196 C  C     . ILE A 1 279 ? 26.17100  -25.27000 -15.65700 1.000 30.01149  ? 279 ILE A C     1 
ATOM   2197 O  O     . ILE A 1 279 ? 27.07600  -24.44900 -15.84700 1.000 31.11162  ? 279 ILE A O     1 
ATOM   2198 C  CB    . ILE A 1 279 ? 23.88300  -24.28100 -16.08500 1.000 34.65679  ? 279 ILE A CB    1 
ATOM   2199 C  CG1   . ILE A 1 279 ? 22.63400  -23.70100 -15.41600 1.000 38.73622  ? 279 ILE A CG1   1 
ATOM   2200 C  CG2   . ILE A 1 279 ? 23.51000  -25.34200 -17.11100 1.000 42.46035  ? 279 ILE A CG2   1 
ATOM   2201 C  CD1   . ILE A 1 279 ? 21.93700  -24.66300 -14.47500 1.000 39.65212  ? 279 ILE A CD1   1 
ATOM   2202 N  N     . ARG A 1 280 ? 26.28000  -26.55300 -15.99200 1.000 41.24968  ? 280 ARG A N     1 
ATOM   2203 C  CA    . ARG A 1 280 ? 27.48500  -27.04900 -16.64800 1.000 46.96616  ? 280 ARG A CA    1 
ATOM   2204 C  C     . ARG A 1 280 ? 27.64900  -26.42700 -18.03100 1.000 50.12706  ? 280 ARG A C     1 
ATOM   2205 O  O     . ARG A 1 280 ? 26.66800  -26.18900 -18.74500 1.000 45.09751  ? 280 ARG A O     1 
ATOM   2206 C  CB    . ARG A 1 280 ? 27.44100  -28.57300 -16.76200 1.000 46.46083  ? 280 ARG A CB    1 
ATOM   2207 C  CG    . ARG A 1 280 ? 27.74800  -29.29200 -15.46100 1.000 60.60990  ? 280 ARG A CG    1 
ATOM   2208 C  CD    . ARG A 1 280 ? 27.62300  -30.79200 -15.61700 1.000 55.49876  ? 280 ARG A CD    1 
ATOM   2209 N  NE    . ARG A 1 280 ? 28.59200  -31.33300 -16.56300 1.000 65.22887  ? 280 ARG A NE    1 
ATOM   2210 C  CZ    . ARG A 1 280 ? 28.58600  -32.58900 -16.99700 1.000 72.00074  ? 280 ARG A CZ    1 
ATOM   2211 N  NH1   . ARG A 1 280 ? 27.65500  -33.43400 -16.57300 1.000 63.86555  ? 280 ARG A NH1   1 
ATOM   2212 N  NH2   . ARG A 1 280 ? 29.50600  -33.00100 -17.86000 1.000 67.21595  ? 280 ARG A NH2   1 
ATOM   2213 N  N     . LYS A 1 281 ? 28.90300  -26.15100 -18.40300 1.000 63.80239  ? 281 LYS A N     1 
ATOM   2214 C  CA    . LYS A 1 281 ? 29.23000  -25.63200 -19.73300 1.000 52.71422  ? 281 LYS A CA    1 
ATOM   2215 C  C     . LYS A 1 281 ? 29.42000  -26.81200 -20.68500 1.000 53.89330  ? 281 LYS A C     1 
ATOM   2216 O  O     . LYS A 1 281 ? 30.53300  -27.26100 -20.96900 1.000 76.48022  ? 281 LYS A O     1 
ATOM   2217 C  CB    . LYS A 1 281 ? 30.46600  -24.73700 -19.68700 1.000 55.53824  ? 281 LYS A CB    1 
ATOM   2218 C  CG    . LYS A 1 281 ? 30.21900  -23.28400 -19.27100 1.000 74.37734  ? 281 LYS A CG    1 
ATOM   2219 C  CD    . LYS A 1 281 ? 29.68600  -23.13100 -17.85700 1.000 92.99010  ? 281 LYS A CD    1 
ATOM   2220 C  CE    . LYS A 1 281 ? 29.43000  -21.66500 -17.52900 1.000 93.85599  ? 281 LYS A CE    1 
ATOM   2221 N  NZ    . LYS A 1 281 ? 28.82800  -21.47800 -16.17800 1.000 80.34121  ? 281 LYS A NZ    1 
ATOM   2222 N  N     . LEU A 1 282 ? 28.29500  -27.32200 -21.17800 1.000 56.47519  ? 282 LEU A N     1 
ATOM   2223 C  CA    . LEU A 1 282 ? 28.29400  -28.43000 -22.11700 1.000 65.90001  ? 282 LEU A CA    1 
ATOM   2224 C  C     . LEU A 1 282 ? 28.47500  -27.92300 -23.54600 1.000 63.07072  ? 282 LEU A C     1 
ATOM   2225 O  O     . LEU A 1 282 ? 28.25600  -26.74400 -23.84600 1.000 55.56719  ? 282 LEU A O     1 
ATOM   2226 C  CB    . LEU A 1 282 ? 26.99000  -29.21900 -22.00600 1.000 67.92657  ? 282 LEU A CB    1 
ATOM   2227 C  CG    . LEU A 1 282 ? 26.65800  -29.81300 -20.63700 1.000 69.75310  ? 282 LEU A CG    1 
ATOM   2228 C  CD1   . LEU A 1 282 ? 25.28000  -30.45300 -20.66200 1.000 60.48094  ? 282 LEU A CD1   1 
ATOM   2229 C  CD2   . LEU A 1 282 ? 27.71800  -30.82300 -20.21900 1.000 55.92776  ? 282 LEU A CD2   1 
ATOM   2230 N  N     . SER A 1 283 ? 28.87100  -28.84300 -24.43400 1.000 65.00516  ? 283 SER A N     1 
ATOM   2231 C  CA    . SER A 1 283 ? 28.99500  -28.52400 -25.85500 1.000 73.62199  ? 283 SER A CA    1 
ATOM   2232 C  C     . SER A 1 283 ? 27.71900  -27.88500 -26.38400 1.000 81.40713  ? 283 SER A C     1 
ATOM   2233 O  O     . SER A 1 283 ? 27.75400  -26.82900 -27.02600 1.000 67.92920  ? 283 SER A O     1 
ATOM   2234 C  CB    . SER A 1 283 ? 29.33800  -29.78500 -26.64700 1.000 65.79736  ? 283 SER A CB    1 
ATOM   2235 O  OG    . SER A 1 283 ? 30.51400  -30.39200 -26.14500 1.000 72.40605  ? 283 SER A OG    1 
ATOM   2236 N  N     . ASP A 1 284 ? 26.58000  -28.52200 -26.12800 1.000 84.73911  ? 284 ASP A N     1 
ATOM   2237 C  CA    . ASP A 1 284 ? 25.28700  -27.92500 -26.41800 1.000 86.63934  ? 284 ASP A CA    1 
ATOM   2238 C  C     . ASP A 1 284 ? 24.71700  -27.35900 -25.12700 1.000 89.26333  ? 284 ASP A C     1 
ATOM   2239 O  O     . ASP A 1 284 ? 24.35600  -28.13800 -24.22900 1.000 55.38296  ? 284 ASP A O     1 
ATOM   2240 C  CB    . ASP A 1 284 ? 24.33700  -28.95700 -27.01900 1.000 91.50834  ? 284 ASP A CB    1 
ATOM   2241 C  CG    . ASP A 1 284 ? 23.08900  -28.32700 -27.59600 1.000 99.28559  ? 284 ASP A CG    1 
ATOM   2242 O  OD1   . ASP A 1 284 ? 23.08100  -27.09100 -27.78400 1.000 82.57832  ? 284 ASP A OD1   1 
ATOM   2243 O  OD2   . ASP A 1 284 ? 22.11900  -29.06700 -27.86900 1.000 96.00362  ? 284 ASP A OD2   1 
ATOM   2244 N  N     . PRO A 1 285 ? 24.63700  -26.03900 -24.97100 1.000 88.06845  ? 285 PRO A N     1 
ATOM   2245 C  CA    . PRO A 1 285 ? 24.16000  -25.45500 -23.70600 1.000 77.18031  ? 285 PRO A CA    1 
ATOM   2246 C  C     . PRO A 1 285 ? 22.74800  -25.91100 -23.38400 1.000 71.26118  ? 285 PRO A C     1 
ATOM   2247 O  O     . PRO A 1 285 ? 21.86300  -25.89300 -24.25300 1.000 68.87405  ? 285 PRO A O     1 
ATOM   2248 C  CB    . PRO A 1 285 ? 24.20700  -23.94100 -23.97100 1.000 73.65357  ? 285 PRO A CB    1 
ATOM   2249 C  CG    . PRO A 1 285 ? 25.17400  -23.77500 -25.10400 1.000 73.85359  ? 285 PRO A CG    1 
ATOM   2250 C  CD    . PRO A 1 285 ? 25.02400  -25.00700 -25.95000 1.000 79.57796  ? 285 PRO A CD    1 
ATOM   2251 N  N     . PRO A 1 286 ? 22.50400  -26.34300 -22.14800 1.000 42.98673  ? 286 PRO A N     1 
ATOM   2252 C  CA    . PRO A 1 286 ? 21.14000  -26.71600 -21.74700 1.000 55.07766  ? 286 PRO A CA    1 
ATOM   2253 C  C     . PRO A 1 286 ? 20.16500  -25.55600 -21.90900 1.000 47.27935  ? 286 PRO A C     1 
ATOM   2254 O  O     . PRO A 1 286 ? 20.46000  -24.41400 -21.54500 1.000 44.21320  ? 286 PRO A O     1 
ATOM   2255 C  CB    . PRO A 1 286 ? 21.30200  -27.11200 -20.27500 1.000 58.55439  ? 286 PRO A CB    1 
ATOM   2256 C  CG    . PRO A 1 286 ? 22.75800  -27.48600 -20.13900 1.000 45.61336  ? 286 PRO A CG    1 
ATOM   2257 C  CD    . PRO A 1 286 ? 23.48900  -26.57900 -21.07800 1.000 48.25315  ? 286 PRO A CD    1 
ATOM   2258 N  N     . LYS A 1 287 ? 18.99200  -25.86400 -22.45900 1.000 40.92070  ? 287 LYS A N     1 
ATOM   2259 C  CA    . LYS A 1 287 ? 17.95200  -24.87500 -22.70200 1.000 51.82990  ? 287 LYS A CA    1 
ATOM   2260 C  C     . LYS A 1 287 ? 17.22400  -24.51200 -21.40700 1.000 47.06354  ? 287 LYS A C     1 
ATOM   2261 O  O     . LYS A 1 287 ? 17.21900  -25.26900 -20.43200 1.000 37.81506  ? 287 LYS A O     1 
ATOM   2262 C  CB    . LYS A 1 287 ? 16.95300  -25.39200 -23.73900 1.000 70.54267  ? 287 LYS A CB    1 
ATOM   2263 C  CG    . LYS A 1 287 ? 17.58600  -25.85400 -25.04400 1.000 68.93721  ? 287 LYS A CG    1 
ATOM   2264 C  CD    . LYS A 1 287 ? 16.54900  -25.98000 -26.15100 1.000 94.10339  ? 287 LYS A CD    1 
ATOM   2265 C  CE    . LYS A 1 287 ? 15.40100  -26.89500 -25.75100 1.000 104.67834 ? 287 LYS A CE    1 
ATOM   2266 N  NZ    . LYS A 1 287 ? 15.82200  -28.31600 -25.62400 1.000 108.79199 ? 287 LYS A NZ    1 
ATOM   2267 N  N     . ALA A 1 288 ? 16.60400  -23.32400 -21.41400 1.000 53.55642  ? 288 ALA A N     1 
ATOM   2268 C  CA    . ALA A 1 288 ? 15.89600  -22.82100 -20.23500 1.000 50.05337  ? 288 ALA A CA    1 
ATOM   2269 C  C     . ALA A 1 288 ? 14.85900  -23.81600 -19.72400 1.000 44.10529  ? 288 ALA A C     1 
ATOM   2270 O  O     . ALA A 1 288 ? 14.71000  -24.00600 -18.50900 1.000 36.78336  ? 288 ALA A O     1 
ATOM   2271 C  CB    . ALA A 1 288 ? 15.22800  -21.48300 -20.55700 1.000 52.18257  ? 288 ALA A CB    1 
ATOM   2272 N  N     . GLU A 1 289 ? 14.10700  -24.43200 -20.63800 1.000 37.19920  ? 289 GLU A N     1 
ATOM   2273 C  CA    . GLU A 1 289 ? 13.14000  -25.44800 -20.23600 1.000 41.59446  ? 289 GLU A CA    1 
ATOM   2274 C  C     . GLU A 1 289 ? 13.81200  -26.58200 -19.47200 1.000 52.31680  ? 289 GLU A C     1 
ATOM   2275 O  O     . GLU A 1 289 ? 13.29200  -27.04800 -18.45200 1.000 37.79927  ? 289 GLU A O     1 
ATOM   2276 C  CB    . GLU A 1 289 ? 12.41800  -26.01100 -21.45600 1.000 39.16522  ? 289 GLU A CB    1 
ATOM   2277 C  CG    . GLU A 1 289 ? 11.24700  -26.87900 -21.06800 1.000 64.13664  ? 289 GLU A CG    1 
ATOM   2278 C  CD    . GLU A 1 289 ? 10.65800  -27.62900 -22.23500 1.000 79.17791  ? 289 GLU A CD    1 
ATOM   2279 O  OE1   . GLU A 1 289 ? 10.98000  -27.28200 -23.39400 1.000 54.97238  ? 289 GLU A OE1   1 
ATOM   2280 O  OE2   . GLU A 1 289 ? 9.86900   -28.56700 -21.98300 1.000 71.09537  ? 289 GLU A OE2   1 
ATOM   2281 N  N     . ALA A 1 290 ? 14.96200  -27.05500 -19.96400 1.000 45.67916  ? 290 ALA A N     1 
ATOM   2282 C  CA    . ALA A 1 290 ? 15.66400  -28.14100 -19.28900 1.000 45.10804  ? 290 ALA A CA    1 
ATOM   2283 C  C     . ALA A 1 290 ? 16.13000  -27.72000 -17.89900 1.000 48.13735  ? 290 ALA A C     1 
ATOM   2284 O  O     . ALA A 1 290 ? 16.08300  -28.51700 -16.95300 1.000 41.15493  ? 290 ALA A O     1 
ATOM   2285 C  CB    . ALA A 1 290 ? 16.84400  -28.61100 -20.14000 1.000 48.86375  ? 290 ALA A CB    1 
ATOM   2286 N  N     . ILE A 1 291 ? 16.58600  -26.47200 -17.75400 1.000 38.61779  ? 291 ILE A N     1 
ATOM   2287 C  CA    . ILE A 1 291 ? 17.00600  -25.98100 -16.44200 1.000 36.90969  ? 291 ILE A CA    1 
ATOM   2288 C  C     . ILE A 1 291 ? 15.82100  -25.96100 -15.48500 1.000 40.95491  ? 291 ILE A C     1 
ATOM   2289 O  O     . ILE A 1 291 ? 15.88800  -26.48500 -14.36500 1.000 34.81470  ? 291 ILE A O     1 
ATOM   2290 C  CB    . ILE A 1 291 ? 17.63000  -24.57900 -16.56300 1.000 40.80489  ? 291 ILE A CB    1 
ATOM   2291 C  CG1   . ILE A 1 291 ? 18.76700  -24.56100 -17.58400 1.000 41.37338  ? 291 ILE A CG1   1 
ATOM   2292 C  CG2   . ILE A 1 291 ? 18.11500  -24.10000 -15.19400 1.000 42.69722  ? 291 ILE A CG2   1 
ATOM   2293 C  CD1   . ILE A 1 291 ? 19.84800  -25.52200 -17.28500 1.000 48.89534  ? 291 ILE A CD1   1 
ATOM   2294 N  N     . ARG A 1 292 ? 14.71800  -25.34400 -15.91400 1.000 38.75201  ? 292 ARG A N     1 
ATOM   2295 C  CA    . ARG A 1 292 ? 13.53300  -25.27900 -15.06900 1.000 44.52639  ? 292 ARG A CA    1 
ATOM   2296 C  C     . ARG A 1 292 ? 12.99300  -26.67000 -14.77500 1.000 38.37565  ? 292 ARG A C     1 
ATOM   2297 O  O     . ARG A 1 292 ? 12.39700  -26.89200 -13.71600 1.000 37.69399  ? 292 ARG A O     1 
ATOM   2298 C  CB    . ARG A 1 292 ? 12.46500  -24.40500 -15.72800 1.000 44.89486  ? 292 ARG A CB    1 
ATOM   2299 C  CG    . ARG A 1 292 ? 12.92200  -22.97600 -16.00400 1.000 42.90514  ? 292 ARG A CG    1 
ATOM   2300 C  CD    . ARG A 1 292 ? 13.71100  -22.40900 -14.83300 1.000 42.19980  ? 292 ARG A CD    1 
ATOM   2301 N  NE    . ARG A 1 292 ? 12.91000  -22.33800 -13.61400 1.000 41.38654  ? 292 ARG A NE    1 
ATOM   2302 C  CZ    . ARG A 1 292 ? 13.38200  -21.96700 -12.42700 1.000 42.31034  ? 292 ARG A CZ    1 
ATOM   2303 N  NH1   . ARG A 1 292 ? 14.66000  -21.63200 -12.29100 1.000 46.86878  ? 292 ARG A NH1   1 
ATOM   2304 N  NH2   . ARG A 1 292 ? 12.57300  -21.92900 -11.37600 1.000 38.38618  ? 292 ARG A NH2   1 
ATOM   2305 N  N     . ASP A 1 293 ? 13.18300  -27.61300 -15.70100 1.000 39.07574  ? 293 ASP A N     1 
ATOM   2306 C  CA    . ASP A 1 293 ? 12.80200  -28.99700 -15.43500 1.000 38.56778  ? 293 ASP A CA    1 
ATOM   2307 C  C     . ASP A 1 293 ? 13.64100  -29.60500 -14.32200 1.000 34.63573  ? 293 ASP A C     1 
ATOM   2308 O  O     . ASP A 1 293 ? 13.10700  -30.29600 -13.44900 1.000 33.61192  ? 293 ASP A O     1 
ATOM   2309 C  CB    . ASP A 1 293 ? 12.92000  -29.84000 -16.70600 1.000 41.43655  ? 293 ASP A CB    1 
ATOM   2310 C  CG    . ASP A 1 293 ? 11.65100  -29.83400 -17.52500 1.000 50.18496  ? 293 ASP A CG    1 
ATOM   2311 O  OD1   . ASP A 1 293 ? 10.57700  -29.58900 -16.93500 1.000 47.65045  ? 293 ASP A OD1   1 
ATOM   2312 O  OD2   . ASP A 1 293 ? 11.72500  -30.07400 -18.75200 1.000 79.64113  ? 293 ASP A OD2   1 
ATOM   2313 N  N     . MET A 1 294 ? 14.95700  -29.37700 -14.34300 1.000 36.64387  ? 294 MET A N     1 
ATOM   2314 C  CA    . MET A 1 294 ? 15.80500  -29.95200 -13.30700 1.000 36.53859  ? 294 MET A CA    1 
ATOM   2315 C  C     . MET A 1 294 ? 15.59200  -29.26500 -11.96300 1.000 33.03028  ? 294 MET A C     1 
ATOM   2316 O  O     . MET A 1 294 ? 15.66700  -29.92100 -10.91900 1.000 35.23844  ? 294 MET A O     1 
ATOM   2317 C  CB    . MET A 1 294 ? 17.27300  -29.88000 -13.72500 1.000 35.34108  ? 294 MET A CB    1 
ATOM   2318 C  CG    . MET A 1 294 ? 18.17900  -30.80000 -12.93200 1.000 43.25519  ? 294 MET A CG    1 
ATOM   2319 S  SD    . MET A 1 294 ? 17.75600  -32.54100 -13.14300 1.000 34.55151  ? 294 MET A SD    1 
ATOM   2320 C  CE    . MET A 1 294 ? 18.47400  -32.87800 -14.75600 1.000 37.84138  ? 294 MET A CE    1 
ATOM   2321 N  N     . VAL A 1 295 ? 15.30600  -27.96000 -11.96500 1.000 30.80106  ? 295 VAL A N     1 
ATOM   2322 C  CA    . VAL A 1 295 ? 15.02100  -27.25800 -10.71300 1.000 31.13005  ? 295 VAL A CA    1 
ATOM   2323 C  C     . VAL A 1 295 ? 13.75700  -27.81800 -10.07700 1.000 35.53584  ? 295 VAL A C     1 
ATOM   2324 O  O     . VAL A 1 295 ? 13.71100  -28.07600 -8.86700  1.000 28.19022  ? 295 VAL A O     1 
ATOM   2325 C  CB    . VAL A 1 295 ? 14.90900  -25.74200 -10.95600 1.000 29.03506  ? 295 VAL A CB    1 
ATOM   2326 C  CG1   . VAL A 1 295 ? 14.35200  -25.04300 -9.72100  1.000 30.71947  ? 295 VAL A CG1   1 
ATOM   2327 C  CG2   . VAL A 1 295 ? 16.27300  -25.17100 -11.33300 1.000 29.78778  ? 295 VAL A CG2   1 
ATOM   2328 N  N     . ARG A 1 296 ? 12.71300  -28.01100 -10.88900 1.000 32.46968  ? 296 ARG A N     1 
ATOM   2329 C  CA    . ARG A 1 296 ? 11.48600  -28.64700 -10.41700 1.000 44.00001  ? 296 ARG A CA    1 
ATOM   2330 C  C     . ARG A 1 296 ? 11.76200  -30.03300 -9.85000  1.000 44.53955  ? 296 ARG A C     1 
ATOM   2331 O  O     . ARG A 1 296 ? 11.26300  -30.38400 -8.77300  1.000 34.50940  ? 296 ARG A O     1 
ATOM   2332 C  CB    . ARG A 1 296 ? 10.46900  -28.73700 -11.55600 1.000 40.24956  ? 296 ARG A CB    1 
ATOM   2333 C  CG    . ARG A 1 296 ? 9.25100   -29.57400 -11.20900 1.000 41.64973  ? 296 ARG A CG    1 
ATOM   2334 C  CD    . ARG A 1 296 ? 8.17300   -29.45400 -12.26700 1.000 51.12981  ? 296 ARG A CD    1 
ATOM   2335 N  NE    . ARG A 1 296 ? 8.65400   -29.79200 -13.60100 1.000 67.52915  ? 296 ARG A NE    1 
ATOM   2336 C  CZ    . ARG A 1 296 ? 8.41700   -30.95000 -14.20600 1.000 68.42136  ? 296 ARG A CZ    1 
ATOM   2337 N  NH1   . ARG A 1 296 ? 7.70400   -31.88400 -13.58900 1.000 70.16104  ? 296 ARG A NH1   1 
ATOM   2338 N  NH2   . ARG A 1 296 ? 8.88800   -31.16900 -15.42700 1.000 56.88577  ? 296 ARG A NH2   1 
ATOM   2339 N  N     . TYR A 1 297 ? 12.52100  -30.85100 -10.58900 1.000 34.30411  ? 297 TYR A N     1 
ATOM   2340 C  CA    . TYR A 1 297 ? 12.91900  -32.16100 -10.08300 1.000 40.37326  ? 297 TYR A CA    1 
ATOM   2341 C  C     . TYR A 1 297 ? 13.65100  -32.03300 -8.75200  1.000 33.11976  ? 297 TYR A C     1 
ATOM   2342 O  O     . TYR A 1 297 ? 13.33200  -32.73400 -7.78400  1.000 37.90191  ? 297 TYR A O     1 
ATOM   2343 C  CB    . TYR A 1 297 ? 13.79200  -32.87900 -11.11300 1.000 37.87559  ? 297 TYR A CB    1 
ATOM   2344 C  CG    . TYR A 1 297 ? 14.51100  -34.09000 -10.56300 1.000 43.17360  ? 297 TYR A CG    1 
ATOM   2345 C  CD1   . TYR A 1 297 ? 13.87500  -35.32400 -10.48900 1.000 44.05528  ? 297 TYR A CD1   1 
ATOM   2346 C  CD2   . TYR A 1 297 ? 15.83100  -34.00600 -10.13000 1.000 44.85538  ? 297 TYR A CD2   1 
ATOM   2347 C  CE1   . TYR A 1 297 ? 14.52200  -36.43500 -9.98600  1.000 40.08902  ? 297 TYR A CE1   1 
ATOM   2348 C  CE2   . TYR A 1 297 ? 16.49100  -35.11500 -9.62900  1.000 40.53907  ? 297 TYR A CE2   1 
ATOM   2349 C  CZ    . TYR A 1 297 ? 15.83000  -36.32700 -9.55600  1.000 47.28988  ? 297 TYR A CZ    1 
ATOM   2350 O  OH    . TYR A 1 297 ? 16.47800  -37.43500 -9.05700  1.000 42.61300  ? 297 TYR A OH    1 
ATOM   2351 N  N     . ALA A 1 298 ? 14.64100  -31.13900 -8.69000  1.000 30.13519  ? 298 ALA A N     1 
ATOM   2352 C  CA    . ALA A 1 298 ? 15.42200  -30.97500 -7.46900  1.000 28.75871  ? 298 ALA A CA    1 
ATOM   2353 C  C     . ALA A 1 298 ? 14.52500  -30.64600 -6.28300  1.000 30.83528  ? 298 ALA A C     1 
ATOM   2354 O  O     . ALA A 1 298 ? 14.64300  -31.25300 -5.21400  1.000 35.23054  ? 298 ALA A O     1 
ATOM   2355 C  CB    . ALA A 1 298 ? 16.47400  -29.88500 -7.66400  1.000 27.89019  ? 298 ALA A CB    1 
ATOM   2356 N  N     . ARG A 1 299 ? 13.59500  -29.70500 -6.46400  1.000 31.20901  ? 299 ARG A N     1 
ATOM   2357 C  CA    . ARG A 1 299 ? 12.70200  -29.33500 -5.37100  1.000 37.74663  ? 299 ARG A CA    1 
ATOM   2358 C  C     . ARG A 1 299 ? 11.81100  -30.49400 -4.95800  1.000 34.58836  ? 299 ARG A C     1 
ATOM   2359 O  O     . ARG A 1 299 ? 11.41100  -30.58300 -3.79000  1.000 34.48045  ? 299 ARG A O     1 
ATOM   2360 C  CB    . ARG A 1 299 ? 11.84100  -28.14400 -5.77200  1.000 51.38774  ? 299 ARG A CB    1 
ATOM   2361 C  CG    . ARG A 1 299 ? 12.58700  -26.84700 -5.85800  1.000 49.72701  ? 299 ARG A CG    1 
ATOM   2362 C  CD    . ARG A 1 299 ? 11.63200  -25.71900 -6.16100  1.000 57.11737  ? 299 ARG A CD    1 
ATOM   2363 N  NE    . ARG A 1 299 ? 12.35700  -24.47700 -6.36400  1.000 62.68646  ? 299 ARG A NE    1 
ATOM   2364 C  CZ    . ARG A 1 299 ? 12.05400  -23.58400 -7.29500  1.000 36.52806  ? 299 ARG A CZ    1 
ATOM   2365 N  NH1   . ARG A 1 299 ? 11.03800  -23.80000 -8.12400  1.000 35.63848  ? 299 ARG A NH1   1 
ATOM   2366 N  NH2   . ARG A 1 299 ? 12.78000  -22.48000 -7.40200  1.000 38.34670  ? 299 ARG A NH2   1 
ATOM   2367 N  N     . ASN A 1 300 ? 11.49500  -31.39200 -5.89300  1.000 33.68299  ? 300 ASN A N     1 
ATOM   2368 C  CA    . ASN A 1 300 ? 10.63500  -32.52300 -5.56300  1.000 43.16044  ? 300 ASN A CA    1 
ATOM   2369 C  C     . ASN A 1 300 ? 11.38600  -33.57400 -4.75500  1.000 42.32876  ? 300 ASN A C     1 
ATOM   2370 O  O     . ASN A 1 300 ? 10.85900  -34.08700 -3.76100  1.000 37.88612  ? 300 ASN A O     1 
ATOM   2371 C  CB    . ASN A 1 300 ? 10.05800  -33.13400 -6.84000  1.000 53.78540  ? 300 ASN A CB    1 
ATOM   2372 C  CG    . ASN A 1 300 ? 9.28400   -34.41500 -6.57400  1.000 64.08137  ? 300 ASN A CG    1 
ATOM   2373 O  OD1   . ASN A 1 300 ? 8.17400   -34.38500 -6.04200  1.000 74.27733  ? 300 ASN A OD1   1 
ATOM   2374 N  ND2   . ASN A 1 300 ? 9.86900   -35.54900 -6.94500  1.000 88.42113  ? 300 ASN A ND2   1 
ATOM   2375 N  N     . VAL A 1 301 ? 12.61900  -33.90300 -5.15400  1.000 29.69567  ? 301 VAL A N     1 
ATOM   2376 C  CA    . VAL A 1 301 ? 13.38100  -34.88200 -4.38400  1.000 31.80118  ? 301 VAL A CA    1 
ATOM   2377 C  C     . VAL A 1 301 ? 13.73300  -34.32200 -3.01100  1.000 27.68227  ? 301 VAL A C     1 
ATOM   2378 O  O     . VAL A 1 301 ? 13.80200  -35.07300 -2.03000  1.000 39.02047  ? 301 VAL A O     1 
ATOM   2379 C  CB    . VAL A 1 301 ? 14.64100  -35.34300 -5.14800  1.000 33.03817  ? 301 VAL A CB    1 
ATOM   2380 C  CG1   . VAL A 1 301 ? 14.26200  -36.04100 -6.43900  1.000 45.33701  ? 301 VAL A CG1   1 
ATOM   2381 C  CG2   . VAL A 1 301 ? 15.57000  -34.18000 -5.42600  1.000 48.37159  ? 301 VAL A CG2   1 
ATOM   2382 N  N     . ILE A 1 302 ? 13.95200  -33.00600 -2.90800  1.000 26.43212  ? 302 ILE A N     1 
ATOM   2383 C  CA    . ILE A 1 302 ? 14.18200  -32.39900 -1.59900  1.000 28.04810  ? 302 ILE A CA    1 
ATOM   2384 C  C     . ILE A 1 302 ? 12.98500  -32.64200 -0.69600  1.000 30.40365  ? 302 ILE A C     1 
ATOM   2385 O  O     . ILE A 1 302 ? 13.13500  -33.02000 0.47100   1.000 25.42936  ? 302 ILE A O     1 
ATOM   2386 C  CB    . ILE A 1 302 ? 14.49400  -30.89600 -1.73800  1.000 29.16402  ? 302 ILE A CB    1 
ATOM   2387 C  CG1   . ILE A 1 302 ? 15.89300  -30.68000 -2.31200  1.000 35.93852  ? 302 ILE A CG1   1 
ATOM   2388 C  CG2   . ILE A 1 302 ? 14.38500  -30.18900 -0.38900  1.000 32.05121  ? 302 ILE A CG2   1 
ATOM   2389 C  CD1   . ILE A 1 302 ? 16.17100  -29.24900 -2.69000  1.000 35.07789  ? 302 ILE A CD1   1 
ATOM   2390 N  N     . GLU A 1 303 ? 11.77400  -32.46600 -1.23200  1.000 40.33905  ? 303 GLU A N     1 
ATOM   2391 C  CA    . GLU A 1 303 ? 10.57200  -32.72100 -0.44400  1.000 47.98996  ? 303 GLU A CA    1 
ATOM   2392 C  C     . GLU A 1 303 ? 10.40000  -34.20800 -0.15600  1.000 45.75549  ? 303 GLU A C     1 
ATOM   2393 O  O     . GLU A 1 303 ? 10.06800  -34.58700 0.97200   1.000 37.94402  ? 303 GLU A O     1 
ATOM   2394 C  CB    . GLU A 1 303 ? 9.34300   -32.15700 -1.15400  1.000 45.95814  ? 303 GLU A CB    1 
ATOM   2395 C  CG    . GLU A 1 303 ? 8.09000   -32.15900 -0.29200  1.000 58.48070  ? 303 GLU A CG    1 
ATOM   2396 C  CD    . GLU A 1 303 ? 8.28200   -31.42100 1.02500   1.000 69.50570  ? 303 GLU A CD    1 
ATOM   2397 O  OE1   . GLU A 1 303 ? 8.96700   -30.37100 1.03400   1.000 78.48836  ? 303 GLU A OE1   1 
ATOM   2398 O  OE2   . GLU A 1 303 ? 7.75100   -31.89600 2.05300   1.000 75.31166  ? 303 GLU A OE2   1 
ATOM   2399 N  N     . GLU A 1 304 ? 10.61200  -35.06400 -1.16300  1.000 42.62616  ? 304 GLU A N     1 
ATOM   2400 C  CA    . GLU A 1 304 ? 10.52700  -36.50800 -0.94800  1.000 45.21858  ? 304 GLU A CA    1 
ATOM   2401 C  C     . GLU A 1 304 ? 11.51200  -36.97400 0.11800   1.000 50.50869  ? 304 GLU A C     1 
ATOM   2402 O  O     . GLU A 1 304 ? 11.18100  -37.82800 0.95000   1.000 46.24765  ? 304 GLU A O     1 
ATOM   2403 C  CB    . GLU A 1 304 ? 10.77800  -37.25100 -2.26100  1.000 47.38200  ? 304 GLU A CB    1 
ATOM   2404 C  CG    . GLU A 1 304 ? 9.58900   -37.26100 -3.21100  1.000 82.67570  ? 304 GLU A CG    1 
ATOM   2405 C  CD    . GLU A 1 304 ? 9.82500   -38.11100 -4.45200  1.000 110.51588 ? 304 GLU A CD    1 
ATOM   2406 O  OE1   . GLU A 1 304 ? 10.95000  -38.63100 -4.62000  1.000 95.24826  ? 304 GLU A OE1   1 
ATOM   2407 O  OE2   . GLU A 1 304 ? 8.88500   -38.25000 -5.26500  1.000 104.80993 ? 304 GLU A OE2   1 
ATOM   2408 N  N     . PHE A 1 305 ? 12.73400  -36.43500 0.10200   1.000 34.62520  ? 305 PHE A N     1 
ATOM   2409 C  CA    . PHE A 1 305 ? 13.72500  -36.82900 1.09800   1.000 30.99319  ? 305 PHE A CA    1 
ATOM   2410 C  C     . PHE A 1 305 ? 13.32900  -36.35900 2.49000   1.000 34.87523  ? 305 PHE A C     1 
ATOM   2411 O  O     . PHE A 1 305 ? 13.53800  -37.07600 3.47600   1.000 30.77211  ? 305 PHE A O     1 
ATOM   2412 C  CB    . PHE A 1 305 ? 15.10200  -36.27600 0.73500   1.000 29.94043  ? 305 PHE A CB    1 
ATOM   2413 C  CG    . PHE A 1 305 ? 16.20600  -36.81200 1.59800   1.000 25.88468  ? 305 PHE A CG    1 
ATOM   2414 C  CD1   . PHE A 1 305 ? 16.82400  -38.00800 1.28600   1.000 34.98577  ? 305 PHE A CD1   1 
ATOM   2415 C  CD2   . PHE A 1 305 ? 16.61100  -36.13300 2.73100   1.000 28.52447  ? 305 PHE A CD2   1 
ATOM   2416 C  CE1   . PHE A 1 305 ? 17.83600  -38.50900 2.08000   1.000 34.75943  ? 305 PHE A CE1   1 
ATOM   2417 C  CE2   . PHE A 1 305 ? 17.62200  -36.63100 3.53000   1.000 30.49050  ? 305 PHE A CE2   1 
ATOM   2418 C  CZ    . PHE A 1 305 ? 18.23500  -37.82000 3.20400   1.000 29.17981  ? 305 PHE A CZ    1 
ATOM   2419 N  N     . ARG A 1 306 ? 12.79000  -35.14300 2.59600   1.000 31.05636  ? 306 ARG A N     1 
ATOM   2420 C  CA    . ARG A 1 306 ? 12.34000  -34.64700 3.89000   1.000 42.61037  ? 306 ARG A CA    1 
ATOM   2421 C  C     . ARG A 1 306 ? 11.30000  -35.57700 4.50800   1.000 42.61037  ? 306 ARG A C     1 
ATOM   2422 O  O     . ARG A 1 306 ? 11.31400  -35.81100 5.72200   1.000 45.47651  ? 306 ARG A O     1 
ATOM   2423 C  CB    . ARG A 1 306 ? 11.80800  -33.22200 3.74100   1.000 47.71888  ? 306 ARG A CB    1 
ATOM   2424 C  CG    . ARG A 1 306 ? 11.44700  -32.55200 5.05200   1.000 50.08232  ? 306 ARG A CG    1 
ATOM   2425 C  CD    . ARG A 1 306 ? 11.13600  -31.07900 4.84400   1.000 70.17420  ? 306 ARG A CD    1 
ATOM   2426 N  NE    . ARG A 1 306 ? 12.31400  -30.34200 4.38600   1.000 112.95565 ? 306 ARG A NE    1 
ATOM   2427 C  CZ    . ARG A 1 306 ? 12.37800  -29.63400 3.26100   1.000 75.79067  ? 306 ARG A CZ    1 
ATOM   2428 N  NH1   . ARG A 1 306 ? 11.32300  -29.55500 2.45900   1.000 87.39732  ? 306 ARG A NH1   1 
ATOM   2429 N  NH2   . ARG A 1 306 ? 13.50100  -29.00000 2.94200   1.000 53.26428  ? 306 ARG A NH2   1 
ATOM   2430 N  N     . ARG A 1 307 ? 10.39600  -36.12500 3.68800   1.000 40.54433  ? 307 ARG A N     1 
ATOM   2431 C  CA    . ARG A 1 307 ? 9.43000   -37.10300 4.18600   1.000 45.93709  ? 307 ARG A CA    1 
ATOM   2432 C  C     . ARG A 1 307 ? 10.09600  -38.44400 4.48100   1.000 43.72630  ? 307 ARG A C     1 
ATOM   2433 O  O     . ARG A 1 307 ? 9.89800   -39.02200 5.55700   1.000 48.41107  ? 307 ARG A O     1 
ATOM   2434 C  CB    . ARG A 1 307 ? 8.28900   -37.28400 3.18200   1.000 47.77152  ? 307 ARG A CB    1 
ATOM   2435 C  CG    . ARG A 1 307 ? 7.36700   -36.07900 3.05200   1.000 62.69436  ? 307 ARG A CG    1 
ATOM   2436 C  CD    . ARG A 1 307 ? 6.08300   -36.44500 2.31900   1.000 76.68288  ? 307 ARG A CD    1 
ATOM   2437 N  NE    . ARG A 1 307 ? 6.35000   -36.95700 0.97800   1.000 109.83159 ? 307 ARG A NE    1 
ATOM   2438 C  CZ    . ARG A 1 307 ? 6.36500   -36.20600 -0.11800  1.000 105.13629 ? 307 ARG A CZ    1 
ATOM   2439 N  NH1   . ARG A 1 307 ? 6.12400   -34.90400 -0.03500  1.000 73.98255  ? 307 ARG A NH1   1 
ATOM   2440 N  NH2   . ARG A 1 307 ? 6.62200   -36.75700 -1.29800  1.000 89.19490  ? 307 ARG A NH2   1 
ATOM   2441 N  N     . ALA A 1 308 ? 10.89100  -38.95400 3.53200   1.000 29.51933  ? 308 ALA A N     1 
ATOM   2442 C  CA    . ALA A 1 308 ? 11.53000  -40.26000 3.69100   1.000 32.21965  ? 308 ALA A CA    1 
ATOM   2443 C  C     . ALA A 1 308 ? 12.39300  -40.32600 4.94200   1.000 35.30160  ? 308 ALA A C     1 
ATOM   2444 O  O     . ALA A 1 308 ? 12.58000  -41.40500 5.51500   1.000 40.59960  ? 308 ALA A O     1 
ATOM   2445 C  CB    . ALA A 1 308 ? 12.38100  -40.58500 2.46300   1.000 32.54074  ? 308 ALA A CB    1 
ATOM   2446 N  N     . LYS A 1 309 ? 12.91700  -39.18300 5.38200   1.000 40.19956  ? 309 LYS A N     1 
ATOM   2447 C  CA    . LYS A 1 309 ? 13.82700  -39.13600 6.51800   1.000 42.65511  ? 309 LYS A CA    1 
ATOM   2448 C  C     . LYS A 1 309 ? 13.18700  -39.65100 7.80100   1.000 56.26201  ? 309 LYS A C     1 
ATOM   2449 O  O     . LYS A 1 309 ? 13.90700  -40.03500 8.73000   1.000 45.26859  ? 309 LYS A O     1 
ATOM   2450 C  CB    . LYS A 1 309 ? 14.27400  -37.68500 6.70600   1.000 37.87296  ? 309 LYS A CB    1 
ATOM   2451 C  CG    . LYS A 1 309 ? 15.64300  -37.46100 7.28000   1.000 46.48452  ? 309 LYS A CG    1 
ATOM   2452 C  CD    . LYS A 1 309 ? 15.82200  -35.96900 7.48700   1.000 52.87213  ? 309 LYS A CD    1 
ATOM   2453 C  CE    . LYS A 1 309 ? 17.27500  -35.56800 7.63200   1.000 59.91771  ? 309 LYS A CE    1 
ATOM   2454 N  NZ    . LYS A 1 309 ? 17.40500  -34.08100 7.63200   1.000 61.99164  ? 309 LYS A NZ    1 
ATOM   2455 N  N     . HIS A 1 310 ? 11.85600  -39.71700 7.85300   1.000 71.94810  ? 310 HIS A N     1 
ATOM   2456 C  CA    . HIS A 1 310 ? 11.16400  -40.14400 9.06400   1.000 81.38344  ? 310 HIS A CA    1 
ATOM   2457 C  C     . HIS A 1 310 ? 11.13300  -41.65900 9.22800   1.000 77.70142  ? 310 HIS A C     1 
ATOM   2458 O  O     . HIS A 1 310 ? 11.08100  -42.14800 10.36200  1.000 66.52377  ? 310 HIS A O     1 
ATOM   2459 C  CB    . HIS A 1 310 ? 9.73900   -39.58500 9.07000   1.000 76.70920  ? 310 HIS A CB    1 
ATOM   2460 C  CG    . HIS A 1 310 ? 9.68200   -38.09500 9.20500   1.000 103.15447 ? 310 HIS A CG    1 
ATOM   2461 N  ND1   . HIS A 1 310 ? 10.10700  -37.43500 10.33800  1.000 97.26429  ? 310 HIS A ND1   1 
ATOM   2462 C  CD2   . HIS A 1 310 ? 9.26200   -37.13600 8.34500   1.000 106.57857 ? 310 HIS A CD2   1 
ATOM   2463 C  CE1   . HIS A 1 310 ? 9.95000   -36.13400 10.17100  1.000 89.04225  ? 310 HIS A CE1   1 
ATOM   2464 N  NE2   . HIS A 1 310 ? 9.43800   -35.92600 8.97100   1.000 103.27554 ? 310 HIS A NE2   1 
ATOM   2465 N  N     . TYR A 1 311 ? 11.14500  -42.42100 8.13400   1.000 58.98602  ? 311 TYR A N     1 
ATOM   2466 C  CA    . TYR A 1 311 ? 10.91600  -43.85700 8.22600   1.000 70.38212  ? 311 TYR A CA    1 
ATOM   2467 C  C     . TYR A 1 311 ? 11.92500  -44.73400 7.49100   1.000 68.63981  ? 311 TYR A C     1 
ATOM   2468 O  O     . TYR A 1 311 ? 12.07800  -45.89900 7.87400   1.000 71.43751  ? 311 TYR A O     1 
ATOM   2469 C  CB    . TYR A 1 311 ? 9.50300   -44.20900 7.73100   1.000 58.25435  ? 311 TYR A CB    1 
ATOM   2470 C  CG    . TYR A 1 311 ? 9.18200   -43.82800 6.29700   1.000 69.81100  ? 311 TYR A CG    1 
ATOM   2471 C  CD1   . TYR A 1 311 ? 8.66000   -42.57700 5.98600   1.000 63.23653  ? 311 TYR A CD1   1 
ATOM   2472 C  CD2   . TYR A 1 311 ? 9.36800   -44.73500 5.26100   1.000 61.89953  ? 311 TYR A CD2   1 
ATOM   2473 C  CE1   . TYR A 1 311 ? 8.35200   -42.23500 4.67400   1.000 56.38571  ? 311 TYR A CE1   1 
ATOM   2474 C  CE2   . TYR A 1 311 ? 9.06300   -44.40300 3.95200   1.000 61.88110  ? 311 TYR A CE2   1 
ATOM   2475 C  CZ    . TYR A 1 311 ? 8.55600   -43.15000 3.66400   1.000 60.76255  ? 311 TYR A CZ    1 
ATOM   2476 O  OH    . TYR A 1 311 ? 8.25300   -42.80900 2.36800   1.000 61.38104  ? 311 TYR A OH    1 
ATOM   2477 N  N     . LYS A 1 312 ? 12.60900  -44.23700 6.46600   1.000 43.27624  ? 312 LYS A N     1 
ATOM   2478 C  CA    . LYS A 1 312 ? 13.48600  -45.09800 5.68300   1.000 42.60774  ? 312 LYS A CA    1 
ATOM   2479 C  C     . LYS A 1 312 ? 14.82600  -45.31900 6.38300   1.000 33.18819  ? 312 LYS A C     1 
ATOM   2480 O  O     . LYS A 1 312 ? 15.26500  -44.51600 7.21200   1.000 34.49098  ? 312 LYS A O     1 
ATOM   2481 C  CB    . LYS A 1 312 ? 13.70300  -44.51000 4.28900   1.000 39.72845  ? 312 LYS A CB    1 
ATOM   2482 C  CG    . LYS A 1 312 ? 12.52300  -44.72800 3.34800   1.000 53.76171  ? 312 LYS A CG    1 
ATOM   2483 C  CD    . LYS A 1 312 ? 12.78600  -44.12600 1.97600   1.000 53.69328  ? 312 LYS A CD    1 
ATOM   2484 C  CE    . LYS A 1 312 ? 11.59900  -44.31300 1.04600   1.000 58.93865  ? 312 LYS A CE    1 
ATOM   2485 N  NZ    . LYS A 1 312 ? 11.45800  -45.71700 0.59000   1.000 66.72642  ? 312 LYS A NZ    1 
ATOM   2486 N  N     . SER A 1 313 ? 15.47300  -46.43400 6.03900   1.000 36.97022  ? 313 SER A N     1 
ATOM   2487 C  CA    . SER A 1 313 ? 16.74200  -46.79700 6.64800   1.000 45.53704  ? 313 SER A CA    1 
ATOM   2488 C  C     . SER A 1 313 ? 17.85700  -45.87700 6.15400   1.000 41.96819  ? 313 SER A C     1 
ATOM   2489 O  O     . SER A 1 313 ? 17.72700  -45.23300 5.11000   1.000 36.48332  ? 313 SER A O     1 
ATOM   2490 C  CB    . SER A 1 313 ? 17.09400  -48.24600 6.32300   1.000 44.63430  ? 313 SER A CB    1 
ATOM   2491 O  OG    . SER A 1 313 ? 17.60300  -48.35200 5.00400   1.000 45.93445  ? 313 SER A OG    1 
ATOM   2492 N  N     . PRO A 1 314 ? 18.96500  -45.78800 6.90000   1.000 45.87919  ? 314 PRO A N     1 
ATOM   2493 C  CA    . PRO A 1 314 ? 20.08200  -44.93400 6.44300   1.000 45.48177  ? 314 PRO A CA    1 
ATOM   2494 C  C     . PRO A 1 314 ? 20.60000  -45.27800 5.05200   1.000 37.94666  ? 314 PRO A C     1 
ATOM   2495 O  O     . PRO A 1 314 ? 20.79100  -44.37300 4.23100   1.000 34.87787  ? 314 PRO A O     1 
ATOM   2496 C  CB    . PRO A 1 314 ? 21.14100  -45.15300 7.53100   1.000 44.39216  ? 314 PRO A CB    1 
ATOM   2497 C  CG    . PRO A 1 314 ? 20.35500  -45.48700 8.74800   1.000 40.68119  ? 314 PRO A CG    1 
ATOM   2498 C  CD    . PRO A 1 314 ? 19.20100  -46.31600 8.25500   1.000 44.06055  ? 314 PRO A CD    1 
ATOM   2499 N  N     . SER A 1 315 ? 20.81900  -46.56100 4.75400   1.000 39.56790  ? 315 SER A N     1 
ATOM   2500 C  CA    . SER A 1 315 ? 21.30800  -46.93500 3.42900   1.000 45.98972  ? 315 SER A CA    1 
ATOM   2501 C  C     . SER A 1 315 ? 20.31600  -46.54400 2.33700   1.000 43.25519  ? 315 SER A C     1 
ATOM   2502 O  O     . SER A 1 315 ? 20.71800  -46.15700 1.23300   1.000 35.63848  ? 315 SER A O     1 
ATOM   2503 C  CB    . SER A 1 315 ? 21.60500  -48.43500 3.37800   1.000 45.27122  ? 315 SER A CB    1 
ATOM   2504 O  OG    . SER A 1 315 ? 20.42000  -49.19900 3.50900   1.000 60.88625  ? 315 SER A OG    1 
ATOM   2505 N  N     . GLU A 1 316 ? 19.01300  -46.64600 2.62500   1.000 43.25782  ? 316 GLU A N     1 
ATOM   2506 C  CA    . GLU A 1 316 ? 18.00200  -46.22500 1.65900   1.000 52.15099  ? 316 GLU A CA    1 
ATOM   2507 C  C     . GLU A 1 316 ? 18.03600  -44.71700 1.44800   1.000 42.89725  ? 316 GLU A C     1 
ATOM   2508 O  O     . GLU A 1 316 ? 17.81800  -44.23700 0.32800   1.000 41.91029  ? 316 GLU A O     1 
ATOM   2509 C  CB    . GLU A 1 316 ? 16.61400  -46.66800 2.11900   1.000 57.33056  ? 316 GLU A CB    1 
ATOM   2510 C  CG    . GLU A 1 316 ? 16.37300  -48.16300 2.01500   1.000 64.36298  ? 316 GLU A CG    1 
ATOM   2511 C  CD    . GLU A 1 316 ? 15.08100  -48.59500 2.68500   1.000 89.22912  ? 316 GLU A CD    1 
ATOM   2512 O  OE1   . GLU A 1 316 ? 14.75500  -48.05100 3.76300   1.000 72.53238  ? 316 GLU A OE1   1 
ATOM   2513 O  OE2   . GLU A 1 316 ? 14.39200  -49.47800 2.13100   1.000 104.60991 ? 316 GLU A OE2   1 
ATOM   2514 N  N     . LEU A 1 317 ? 18.28700  -43.95400 2.51800   1.000 33.31978  ? 317 LEU A N     1 
ATOM   2515 C  CA    . LEU A 1 317 ? 18.39800  -42.50300 2.39400   1.000 34.60152  ? 317 LEU A CA    1 
ATOM   2516 C  C     . LEU A 1 317 ? 19.61300  -42.10200 1.56000   1.000 28.29813  ? 317 LEU A C     1 
ATOM   2517 O  O     . LEU A 1 317 ? 19.53700  -41.16600 0.75500   1.000 32.26439  ? 317 LEU A O     1 
ATOM   2518 C  CB    . LEU A 1 317 ? 18.44900  -41.86000 3.78100   1.000 33.62508  ? 317 LEU A CB    1 
ATOM   2519 C  CG    . LEU A 1 317 ? 17.15900  -41.96200 4.60700   1.000 32.46968  ? 317 LEU A CG    1 
ATOM   2520 C  CD1   . LEU A 1 317 ? 17.33800  -41.33700 5.97900   1.000 29.79305  ? 317 LEU A CD1   1 
ATOM   2521 C  CD2   . LEU A 1 317 ? 15.97600  -41.33100 3.87300   1.000 36.21224  ? 317 LEU A CD2   1 
ATOM   2522 N  N     . LEU A 1 318 ? 20.74500  -42.78900 1.74600   1.000 34.89892  ? 318 LEU A N     1 
ATOM   2523 C  CA    . LEU A 1 318 ? 21.91900  -42.52500 0.91700   1.000 36.90969  ? 318 LEU A CA    1 
ATOM   2524 C  C     . LEU A 1 318 ? 21.62700  -42.80300 -0.55100  1.000 37.16235  ? 318 LEU A C     1 
ATOM   2525 O  O     . LEU A 1 318 ? 22.06900  -42.05600 -1.43200  1.000 42.73407  ? 318 LEU A O     1 
ATOM   2526 C  CB    . LEU A 1 318 ? 23.10100  -43.36600 1.39600   1.000 35.93852  ? 318 LEU A CB    1 
ATOM   2527 C  CG    . LEU A 1 318 ? 23.80200  -42.83700 2.64600   1.000 38.53620  ? 318 LEU A CG    1 
ATOM   2528 C  CD1   . LEU A 1 318 ? 24.94500  -43.75300 3.06100   1.000 41.06545  ? 318 LEU A CD1   1 
ATOM   2529 C  CD2   . LEU A 1 318 ? 24.30600  -41.42400 2.40000   1.000 40.87595  ? 318 LEU A CD2   1 
ATOM   2530 N  N     . GLU A 1 319 ? 20.87600  -43.87200 -0.83100  1.000 37.37817  ? 319 GLU A N     1 
ATOM   2531 C  CA    . GLU A 1 319 ? 20.51100  -44.18700 -2.20600  1.000 47.30830  ? 319 GLU A CA    1 
ATOM   2532 C  C     . GLU A 1 319 ? 19.77600  -43.02500 -2.85900  1.000 45.26595  ? 319 GLU A C     1 
ATOM   2533 O  O     . GLU A 1 319 ? 20.08700  -42.64400 -3.99300  1.000 36.98865  ? 319 GLU A O     1 
ATOM   2534 C  CB    . GLU A 1 319 ? 19.63500  -45.43800 -2.23300  1.000 54.73288  ? 319 GLU A CB    1 
ATOM   2535 C  CG    . GLU A 1 319 ? 19.28400  -45.94100 -3.61900  1.000 75.53274  ? 319 GLU A CG    1 
ATOM   2536 C  CD    . GLU A 1 319 ? 18.50000  -47.24000 -3.57800  1.000 107.42604 ? 319 GLU A CD    1 
ATOM   2537 O  OE1   . GLU A 1 319 ? 17.94100  -47.56500 -2.50700  1.000 123.03844 ? 319 GLU A OE1   1 
ATOM   2538 O  OE2   . GLU A 1 319 ? 18.43300  -47.93100 -4.61500  1.000 113.48203 ? 319 GLU A OE2   1 
ATOM   2539 N  N     . ILE A 1 320 ? 18.82900  -42.41700 -2.13900  1.000 37.12550  ? 320 ILE A N     1 
ATOM   2540 C  CA    . ILE A 1 320 ? 18.09500  -41.28000 -2.68800  1.000 36.89127  ? 320 ILE A CA    1 
ATOM   2541 C  C     . ILE A 1 320 ? 19.04400  -40.13200 -3.00700  1.000 41.18389  ? 320 ILE A C     1 
ATOM   2542 O  O     . ILE A 1 320 ? 18.93300  -39.49200 -4.06100  1.000 29.90095  ? 320 ILE A O     1 
ATOM   2543 C  CB    . ILE A 1 320 ? 16.98800  -40.84000 -1.71600  1.000 40.28904  ? 320 ILE A CB    1 
ATOM   2544 C  CG1   . ILE A 1 320 ? 15.92600  -41.93200 -1.58300  1.000 35.78850  ? 320 ILE A CG1   1 
ATOM   2545 C  CG2   . ILE A 1 320 ? 16.35600  -39.54200 -2.18900  1.000 41.07335  ? 320 ILE A CG2   1 
ATOM   2546 C  CD1   . ILE A 1 320 ? 14.97500  -41.69700 -0.42500  1.000 42.49457  ? 320 ILE A CD1   1 
ATOM   2547 N  N     . CYS A 1 321 ? 19.98600  -39.84900 -2.10100  1.000 32.82499  ? 321 CYS A N     1 
ATOM   2548 C  CA    . CYS A 1 321 ? 20.95500  -38.78000 -2.33300  1.000 29.76146  ? 321 CYS A CA    1 
ATOM   2549 C  C     . CYS A 1 321 ? 21.83400  -39.08200 -3.54000  1.000 28.54290  ? 321 CYS A C     1 
ATOM   2550 O  O     . CYS A 1 321 ? 22.09300  -38.20100 -4.36600  1.000 30.84844  ? 321 CYS A O     1 
ATOM   2551 C  CB    . CYS A 1 321 ? 21.81500  -38.56700 -1.08800  1.000 32.24334  ? 321 CYS A CB    1 
ATOM   2552 S  SG    . CYS A 1 321 ? 20.90500  -37.87900 0.31700   1.000 31.89856  ? 321 CYS A SG    1 
ATOM   2553 N  N     . GLU A 1 322 ? 22.32800  -40.32000 -3.63500  1.000 31.48799  ? 322 GLU A N     1 
ATOM   2554 C  CA    . GLU A 1 322 ? 23.20000  -40.71000 -4.74300  1.000 44.21583  ? 322 GLU A CA    1 
ATOM   2555 C  C     . GLU A 1 322 ? 22.48000  -40.60500 -6.08300  1.000 37.85191  ? 322 GLU A C     1 
ATOM   2556 O  O     . GLU A 1 322 ? 22.98200  -39.97800 -7.02300  1.000 43.94211  ? 322 GLU A O     1 
ATOM   2557 C  CB    . GLU A 1 322 ? 23.71200  -42.13300 -4.52400  1.000 53.23270  ? 322 GLU A CB    1 
ATOM   2558 C  CG    . GLU A 1 322 ? 24.74800  -42.27100 -3.42200  1.000 64.33140  ? 322 GLU A CG    1 
ATOM   2559 C  CD    . GLU A 1 322 ? 25.01800  -43.72000 -3.06200  1.000 94.17182  ? 322 GLU A CD    1 
ATOM   2560 O  OE1   . GLU A 1 322 ? 24.85800  -44.59100 -3.94200  1.000 94.19814  ? 322 GLU A OE1   1 
ATOM   2561 O  OE2   . GLU A 1 322 ? 25.39000  -43.98700 -1.89900  1.000 89.32913  ? 322 GLU A OE2   1 
ATOM   2562 N  N     . LEU A 1 323 ? 21.29800  -41.21800 -6.18700  1.000 37.38606  ? 323 LEU A N     1 
ATOM   2563 C  CA    . LEU A 1 323 ? 20.55200  -41.19900 -7.44200  1.000 38.66253  ? 323 LEU A CA    1 
ATOM   2564 C  C     . LEU A 1 323 ? 20.17700  -39.77900 -7.85100  1.000 35.08052  ? 323 LEU A C     1 
ATOM   2565 O  O     . LEU A 1 323 ? 20.25200  -39.42700 -9.03400  1.000 34.85418  ? 323 LEU A O     1 
ATOM   2566 C  CB    . LEU A 1 323 ? 19.29800  -42.06100 -7.31800  1.000 40.84700  ? 323 LEU A CB    1 
ATOM   2567 C  CG    . LEU A 1 323 ? 19.51600  -43.57100 -7.25700  1.000 61.54948  ? 323 LEU A CG    1 
ATOM   2568 C  CD1   . LEU A 1 323 ? 18.19700  -44.28600 -7.01200  1.000 55.68826  ? 323 LEU A CD1   1 
ATOM   2569 C  CD2   . LEU A 1 323 ? 20.16700  -44.05300 -8.53900  1.000 58.70704  ? 323 LEU A CD2   1 
ATOM   2570 N  N     . SER A 1 324 ? 19.76700  -38.94800 -6.88800  1.000 36.48595  ? 324 SER A N     1 
ATOM   2571 C  CA    . SER A 1 324 ? 19.36200  -37.58800 -7.22700  1.000 32.25387  ? 324 SER A CA    1 
ATOM   2572 C  C     . SER A 1 324 ? 20.55000  -36.76500 -7.70600  1.000 40.40221  ? 324 SER A C     1 
ATOM   2573 O  O     . SER A 1 324 ? 20.41600  -35.96400 -8.63900  1.000 31.46430  ? 324 SER A O     1 
ATOM   2574 C  CB    . SER A 1 324 ? 18.68600  -36.91600 -6.03200  1.000 31.01951  ? 324 SER A CB    1 
ATOM   2575 O  OG    . SER A 1 324 ? 19.62500  -36.61100 -5.02200  1.000 41.84449  ? 324 SER A OG    1 
ATOM   2576 N  N     . GLN A 1 325 ? 21.72200  -36.96000 -7.09000  1.000 39.32840  ? 325 GLN A N     1 
ATOM   2577 C  CA    . GLN A 1 325 ? 22.92100  -36.26100 -7.54600  1.000 45.43439  ? 325 GLN A CA    1 
ATOM   2578 C  C     . GLN A 1 325 ? 23.30800  -36.68500 -8.95200  1.000 42.92094  ? 325 GLN A C     1 
ATOM   2579 O  O     . GLN A 1 325 ? 23.70200  -35.84500 -9.77000  1.000 42.26559  ? 325 GLN A O     1 
ATOM   2580 C  CB    . GLN A 1 325 ? 24.08500  -36.49900 -6.58800  1.000 37.39659  ? 325 GLN A CB    1 
ATOM   2581 C  CG    . GLN A 1 325 ? 24.01300  -35.67800 -5.33400  1.000 42.72618  ? 325 GLN A CG    1 
ATOM   2582 C  CD    . GLN A 1 325 ? 25.11800  -36.01900 -4.37300  1.000 48.76901  ? 325 GLN A CD    1 
ATOM   2583 O  OE1   . GLN A 1 325 ? 26.29100  -35.73700 -4.62400  1.000 58.84916  ? 325 GLN A OE1   1 
ATOM   2584 N  NE2   . GLN A 1 325 ? 24.75500  -36.65300 -3.26600  1.000 42.17085  ? 325 GLN A NE2   1 
ATOM   2585 N  N     . GLU A 1 326 ? 23.23600  -37.98500 -9.24400  1.000 41.87344  ? 326 GLU A N     1 
ATOM   2586 C  CA    . GLU A 1 326 ? 23.56300  -38.45900 -10.58500 1.000 42.18401  ? 326 GLU A CA    1 
ATOM   2587 C  C     . GLU A 1 326 ? 22.68300  -37.79200 -11.63300 1.000 41.63920  ? 326 GLU A C     1 
ATOM   2588 O  O     . GLU A 1 326 ? 23.18100  -37.28300 -12.64300 1.000 37.77821  ? 326 GLU A O     1 
ATOM   2589 C  CB    . GLU A 1 326 ? 23.43200  -39.97800 -10.65800 1.000 53.41956  ? 326 GLU A CB    1 
ATOM   2590 C  CG    . GLU A 1 326 ? 24.66900  -40.71700 -10.19500 1.000 80.35700  ? 326 GLU A CG    1 
ATOM   2591 C  CD    . GLU A 1 326 ? 24.70700  -42.14100 -10.70400 1.000 101.80958 ? 326 GLU A CD    1 
ATOM   2592 O  OE1   . GLU A 1 326 ? 23.62600  -42.75500 -10.83200 1.000 82.40988  ? 326 GLU A OE1   1 
ATOM   2593 O  OE2   . GLU A 1 326 ? 25.81600  -42.63900 -10.99300 1.000 79.73588  ? 326 GLU A OE2   1 
ATOM   2594 N  N     . LYS A 1 327 ? 21.37700  -37.77500 -11.39200 1.000 31.51694  ? 327 LYS A N     1 
ATOM   2595 C  CA    . LYS A 1 327 ? 20.47100  -37.16400 -12.38800 1.000 39.92058  ? 327 LYS A CA    1 
ATOM   2596 C  C     . LYS A 1 327 ? 20.74600  -35.66600 -12.51500 1.000 36.88074  ? 327 LYS A C     1 
ATOM   2597 O  O     . LYS A 1 327 ? 20.81600  -35.19400 -13.62200 1.000 37.02812  ? 327 LYS A O     1 
ATOM   2598 C  CB    . LYS A 1 327 ? 18.99600  -37.44900 -12.09500 1.000 43.97106  ? 327 LYS A CB    1 
ATOM   2599 C  CG    . LYS A 1 327 ? 18.05100  -37.13200 -13.24500 1.000 56.95157  ? 327 LYS A CG    1 
ATOM   2600 C  CD    . LYS A 1 327 ? 16.61100  -36.92400 -12.84000 1.000 86.62091  ? 327 LYS A CD    1 
ATOM   2601 C  CE    . LYS A 1 327 ? 15.62900  -36.97600 -13.99500 1.000 87.76842  ? 327 LYS A CE    1 
ATOM   2602 N  NZ    . LYS A 1 327 ? 15.73200  -35.79600 -14.88500 1.000 87.35521  ? 327 LYS A NZ    1 
ATOM   2603 N  N     . MET A 1 328 ? 20.88100  -34.95700 -11.40600 1.000 33.29873  ? 328 MET A N     1 
ATOM   2604 C  CA    . MET A 1 328 ? 21.10000  -33.51600 -11.47700 1.000 35.26739  ? 328 MET A CA    1 
ATOM   2605 C  C     . MET A 1 328 ? 22.43100  -33.16900 -12.14100 1.000 44.19214  ? 328 MET A C     1 
ATOM   2606 O  O     . MET A 1 328 ? 22.52100  -32.15600 -12.84600 1.000 36.79915  ? 328 MET A O     1 
ATOM   2607 C  CB    . MET A 1 328 ? 21.03000  -32.90400 -10.07400 1.000 34.68837  ? 328 MET A CB    1 
ATOM   2608 C  CG    . MET A 1 328 ? 19.62000  -32.84300 -9.49400  1.000 36.25961  ? 328 MET A CG    1 
ATOM   2609 S  SD    . MET A 1 328 ? 19.50700  -31.93600 -7.93500  1.000 36.85179  ? 328 MET A SD    1 
ATOM   2610 C  CE    . MET A 1 328 ? 20.56200  -32.91800 -6.87100  1.000 40.01269  ? 328 MET A CE    1 
ATOM   2611 N  N     . SER A 1 329 ? 23.46500  -33.99600 -11.94500 1.000 34.51993  ? 329 SER A N     1 
ATOM   2612 C  CA    . SER A 1 329 ? 24.80100  -33.67400 -12.44500 1.000 37.61767  ? 329 SER A CA    1 
ATOM   2613 C  C     . SER A 1 329 ? 24.86300  -33.59700 -13.96800 1.000 36.92548  ? 329 SER A C     1 
ATOM   2614 O  O     . SER A 1 329 ? 25.83800  -33.06500 -14.51000 1.000 33.73036  ? 329 SER A O     1 
ATOM   2615 C  CB    . SER A 1 329 ? 25.81400  -34.70700 -11.94900 1.000 37.17025  ? 329 SER A CB    1 
ATOM   2616 O  OG    . SER A 1 329 ? 25.57000  -35.96800 -12.55700 1.000 38.12826  ? 329 SER A OG    1 
ATOM   2617 N  N     . SER A 1 330 ? 23.86300  -34.12900 -14.67400 1.000 38.58884  ? 330 SER A N     1 
ATOM   2618 C  CA    . SER A 1 330 ? 23.82700  -33.95800 -16.12100 1.000 41.88660  ? 330 SER A CA    1 
ATOM   2619 C  C     . SER A 1 330 ? 23.61400  -32.50300 -16.52000 1.000 45.80286  ? 330 SER A C     1 
ATOM   2620 O  O     . SER A 1 330 ? 23.91400  -32.13600 -17.66000 1.000 42.42088  ? 330 SER A O     1 
ATOM   2621 C  CB    . SER A 1 330 ? 22.73400  -34.83400 -16.73400 1.000 40.99176  ? 330 SER A CB    1 
ATOM   2622 O  OG    . SER A 1 330 ? 21.46100  -34.51100 -16.20700 1.000 47.72941  ? 330 SER A OG    1 
ATOM   2623 N  N     . VAL A 1 331 ? 23.09400  -31.67300 -15.61300 1.000 33.44085  ? 331 VAL A N     1 
ATOM   2624 C  CA    . VAL A 1 331 ? 22.83500  -30.26800 -15.88500 1.000 34.09883  ? 331 VAL A CA    1 
ATOM   2625 C  C     . VAL A 1 331 ? 23.52100  -29.35000 -14.87400 1.000 35.31476  ? 331 VAL A C     1 
ATOM   2626 O  O     . VAL A 1 331 ? 24.03500  -28.28900 -15.24600 1.000 27.48224  ? 331 VAL A O     1 
ATOM   2627 C  CB    . VAL A 1 331 ? 21.31700  -29.99100 -15.93200 1.000 39.91531  ? 331 VAL A CB    1 
ATOM   2628 C  CG1   . VAL A 1 331 ? 21.05300  -28.52800 -16.15200 1.000 40.64435  ? 331 VAL A CG1   1 
ATOM   2629 C  CG2   . VAL A 1 331 ? 20.66800  -30.81900 -17.03500 1.000 45.20542  ? 331 VAL A CG2   1 
ATOM   2630 N  N     . PHE A 1 332 ? 23.53100  -29.72900 -13.59500 1.000 32.44600  ? 332 PHE A N     1 
ATOM   2631 C  CA    . PHE A 1 332 ? 24.03800  -28.87600 -12.52200 1.000 31.53273  ? 332 PHE A CA    1 
ATOM   2632 C  C     . PHE A 1 332 ? 25.51600  -29.13000 -12.23100 1.000 27.91914  ? 332 PHE A C     1 
ATOM   2633 O  O     . PHE A 1 332 ? 25.97500  -30.27600 -12.23300 1.000 39.53369  ? 332 PHE A O     1 
ATOM   2634 C  CB    . PHE A 1 332 ? 23.22900  -29.09500 -11.23900 1.000 26.16630  ? 332 PHE A CB    1 
ATOM   2635 C  CG    . PHE A 1 332 ? 21.79500  -28.64500 -11.33100 1.000 29.03243  ? 332 PHE A CG    1 
ATOM   2636 C  CD1   . PHE A 1 332 ? 21.37100  -27.82500 -12.36800 1.000 33.24083  ? 332 PHE A CD1   1 
ATOM   2637 C  CD2   . PHE A 1 332 ? 20.87800  -29.00800 -10.35300 1.000 25.76888  ? 332 PHE A CD2   1 
ATOM   2638 C  CE1   . PHE A 1 332 ? 20.05300  -27.39400 -12.44300 1.000 35.02788  ? 332 PHE A CE1   1 
ATOM   2639 C  CE2   . PHE A 1 332 ? 19.55700  -28.57500 -10.41800 1.000 34.19621  ? 332 PHE A CE2   1 
ATOM   2640 C  CZ    . PHE A 1 332 ? 19.14600  -27.76500 -11.46500 1.000 36.89653  ? 332 PHE A CZ    1 
ATOM   2641 N  N     . GLU A 1 333 ? 26.25600  -28.05000 -11.97400 1.000 33.79879  ? 333 GLU A N     1 
ATOM   2642 C  CA    . GLU A 1 333 ? 27.60800  -28.15500 -11.43800 1.000 30.11414  ? 333 GLU A CA    1 
ATOM   2643 C  C     . GLU A 1 333 ? 27.56800  -28.54000 -9.95700  1.000 32.54864  ? 333 GLU A C     1 
ATOM   2644 O  O     . GLU A 1 333 ? 26.53500  -28.43300 -9.29100  1.000 36.63860  ? 333 GLU A O     1 
ATOM   2645 C  CB    . GLU A 1 333 ? 28.36600  -26.83700 -11.61500 1.000 36.10959  ? 333 GLU A CB    1 
ATOM   2646 C  CG    . GLU A 1 333 ? 28.85500  -26.56800 -13.02900 1.000 53.14321  ? 333 GLU A CG    1 
ATOM   2647 C  CD    . GLU A 1 333 ? 30.06400  -27.41500 -13.40700 1.000 65.80526  ? 333 GLU A CD    1 
ATOM   2648 O  OE1   . GLU A 1 333 ? 30.55500  -28.18000 -12.54600 1.000 68.47926  ? 333 GLU A OE1   1 
ATOM   2649 O  OE2   . GLU A 1 333 ? 30.52700  -27.31000 -14.56400 1.000 74.51157  ? 333 GLU A OE2   1 
ATOM   2650 N  N     . ASP A 1 334 ? 28.72100  -28.97900 -9.43600  1.000 30.98003  ? 334 ASP A N     1 
ATOM   2651 C  CA    . ASP A 1 334 ? 28.78300  -29.41800 -8.04100  1.000 34.73574  ? 334 ASP A CA    1 
ATOM   2652 C  C     . ASP A 1 334 ? 28.50300  -28.28500 -7.06600  1.000 31.74065  ? 334 ASP A C     1 
ATOM   2653 O  O     . ASP A 1 334 ? 27.98500  -28.52800 -5.97000  1.000 34.04882  ? 334 ASP A O     1 
ATOM   2654 C  CB    . ASP A 1 334 ? 30.14500  -30.04000 -7.73500  1.000 45.52125  ? 334 ASP A CB    1 
ATOM   2655 C  CG    . ASP A 1 334 ? 30.27600  -31.44900 -8.27600  1.000 54.49864  ? 334 ASP A CG    1 
ATOM   2656 O  OD1   . ASP A 1 334 ? 29.32700  -31.92100 -8.93900  1.000 49.75597  ? 334 ASP A OD1   1 
ATOM   2657 O  OD2   . ASP A 1 334 ? 31.33000  -32.08000 -8.03500  1.000 62.62593  ? 334 ASP A OD2   1 
ATOM   2658 N  N     . SER A 1 335 ? 28.83000  -27.05100 -7.44300  1.000 26.07944  ? 335 SER A N     1 
ATOM   2659 C  CA    . SER A 1 335 ? 28.60300  -25.89400 -6.58900  1.000 28.48763  ? 335 SER A CA    1 
ATOM   2660 C  C     . SER A 1 335 ? 27.15900  -25.41000 -6.61700  1.000 27.98230  ? 335 SER A C     1 
ATOM   2661 O  O     . SER A 1 335 ? 26.83000  -24.47700 -5.87900  1.000 23.31332  ? 335 SER A O     1 
ATOM   2662 C  CB    . SER A 1 335 ? 29.52600  -24.75100 -7.01000  1.000 28.90873  ? 335 SER A CB    1 
ATOM   2663 O  OG    . SER A 1 335 ? 29.14300  -24.27000 -8.29100  1.000 37.05707  ? 335 SER A OG    1 
ATOM   2664 N  N     . ASN A 1 336 ? 26.31300  -26.00900 -7.45900  1.000 23.97656  ? 336 ASN A N     1 
ATOM   2665 C  CA    . ASN A 1 336 ? 24.88600  -25.69700 -7.50000  1.000 27.22168  ? 336 ASN A CA    1 
ATOM   2666 C  C     . ASN A 1 336 ? 24.23100  -26.05000 -6.16800  1.000 26.05576  ? 336 ASN A C     1 
ATOM   2667 O  O     . ASN A 1 336 ? 24.45300  -27.13500 -5.62600  1.000 22.75799  ? 336 ASN A O     1 
ATOM   2668 C  CB    . ASN A 1 336 ? 24.22800  -26.47000 -8.65300  1.000 26.26894  ? 336 ASN A CB    1 
ATOM   2669 C  CG    . ASN A 1 336 ? 22.76000  -26.10900 -8.86300  1.000 28.43762  ? 336 ASN A CG    1 
ATOM   2670 O  OD1   . ASN A 1 336 ? 21.92600  -26.26300 -7.96000  1.000 25.31619  ? 336 ASN A OD1   1 
ATOM   2671 N  ND2   . ASN A 1 336 ? 22.42400  -25.68600 -10.08500 1.000 27.56383  ? 336 ASN A ND2   1 
ATOM   2672 N  N     . VAL A 1 337 ? 23.41100  -25.13300 -5.64500  1.000 22.76062  ? 337 VAL A N     1 
ATOM   2673 C  CA    . VAL A 1 337 ? 22.87400  -25.29100 -4.29300  1.000 27.68490  ? 337 VAL A CA    1 
ATOM   2674 C  C     . VAL A 1 337 ? 21.92900  -26.47800 -4.17300  1.000 27.65332  ? 337 VAL A C     1 
ATOM   2675 O  O     . VAL A 1 337 ? 21.72300  -26.98300 -3.06500  1.000 21.81841  ? 337 VAL A O     1 
ATOM   2676 C  CB    . VAL A 1 337 ? 22.17400  -24.00400 -3.81600  1.000 25.57675  ? 337 VAL A CB    1 
ATOM   2677 C  CG1   . VAL A 1 337 ? 23.16800  -22.84700 -3.76300  1.000 23.52124  ? 337 VAL A CG1   1 
ATOM   2678 C  CG2   . VAL A 1 337 ? 20.96800  -23.67300 -4.69400  1.000 29.14034  ? 337 VAL A CG2   1 
ATOM   2679 N  N     . TYR A 1 338 ? 21.32200  -26.93100 -5.27400  1.000 23.01592  ? 338 TYR A N     1 
ATOM   2680 C  CA    . TYR A 1 338 ? 20.47600  -28.11400 -5.18500  1.000 25.73466  ? 338 TYR A CA    1 
ATOM   2681 C  C     . TYR A 1 338 ? 21.32600  -29.37600 -5.06900  1.000 27.49277  ? 338 TYR A C     1 
ATOM   2682 O  O     . TYR A 1 338 ? 20.94800  -30.32100 -4.36700  1.000 23.41597  ? 338 TYR A O     1 
ATOM   2683 C  CB    . TYR A 1 338 ? 19.52000  -28.16000 -6.38200  1.000 30.13782  ? 338 TYR A CB    1 
ATOM   2684 C  CG    . TYR A 1 338 ? 18.62500  -26.93200 -6.42000  1.000 30.35890  ? 338 TYR A CG    1 
ATOM   2685 C  CD1   . TYR A 1 338 ? 17.75100  -26.64800 -5.37000  1.000 30.88002  ? 338 TYR A CD1   1 
ATOM   2686 C  CD2   . TYR A 1 338 ? 18.69600  -26.02400 -7.47100  1.000 36.74388  ? 338 TYR A CD2   1 
ATOM   2687 C  CE1   . TYR A 1 338 ? 16.94900  -25.50700 -5.38300  1.000 26.44528  ? 338 TYR A CE1   1 
ATOM   2688 C  CE2   . TYR A 1 338 ? 17.90300  -24.88200 -7.49300  1.000 33.35663  ? 338 TYR A CE2   1 
ATOM   2689 C  CZ    . TYR A 1 338 ? 17.03300  -24.62900 -6.45200  1.000 33.47507  ? 338 TYR A CZ    1 
ATOM   2690 O  OH    . TYR A 1 338 ? 16.25100  -23.49400 -6.48700  1.000 32.95921  ? 338 TYR A OH    1 
ATOM   2691 N  N     . MET A 1 339 ? 22.48200  -29.40200 -5.74200  1.000 25.56886  ? 339 MET A N     1 
ATOM   2692 C  CA    . MET A 1 339 ? 23.47300  -30.45000 -5.50300  1.000 28.64028  ? 339 MET A CA    1 
ATOM   2693 C  C     . MET A 1 339 ? 23.98800  -30.40300 -4.06800  1.000 28.55342  ? 339 MET A C     1 
ATOM   2694 O  O     . MET A 1 339 ? 24.06700  -31.43300 -3.38700  1.000 24.63190  ? 339 MET A O     1 
ATOM   2695 C  CB    . MET A 1 339 ? 24.64300  -30.29400 -6.47500  1.000 25.12143  ? 339 MET A CB    1 
ATOM   2696 C  CG    . MET A 1 339 ? 24.32900  -30.62100 -7.91900  1.000 29.78252  ? 339 MET A CG    1 
ATOM   2697 S  SD    . MET A 1 339 ? 24.21400  -32.39700 -8.20600  1.000 40.94438  ? 339 MET A SD    1 
ATOM   2698 C  CE    . MET A 1 339 ? 25.92500  -32.88200 -7.98500  1.000 40.44432  ? 339 MET A CE    1 
ATOM   2699 N  N     . LEU A 1 340 ? 24.35800  -29.20600 -3.59700  1.000 24.14500  ? 340 LEU A N     1 
ATOM   2700 C  CA    . LEU A 1 340 ? 24.86400  -29.04500 -2.23500  1.000 24.90825  ? 340 LEU A CA    1 
ATOM   2701 C  C     . LEU A 1 340 ? 23.83500  -29.47100 -1.19500  1.000 24.64243  ? 340 LEU A C     1 
ATOM   2702 O  O     . LEU A 1 340 ? 24.20300  -29.94600 -0.11400  1.000 26.48739  ? 340 LEU A O     1 
ATOM   2703 C  CB    . LEU A 1 340 ? 25.27400  -27.59300 -1.99400  1.000 25.70308  ? 340 LEU A CB    1 
ATOM   2704 C  CG    . LEU A 1 340 ? 26.40200  -27.01000 -2.84500  1.000 26.92428  ? 340 LEU A CG    1 
ATOM   2705 C  CD1   . LEU A 1 340 ? 26.59300  -25.53800 -2.50300  1.000 25.59517  ? 340 LEU A CD1   1 
ATOM   2706 C  CD2   . LEU A 1 340 ? 27.70000  -27.79000 -2.65200  1.000 29.34036  ? 340 LEU A CD2   1 
ATOM   2707 N  N     . HIS A 1 341 ? 22.54800  -29.25400 -1.47800  1.000 26.51107  ? 341 HIS A N     1 
ATOM   2708 C  CA    . HIS A 1 341 ? 21.50500  -29.68700 -0.55500  1.000 25.85047  ? 341 HIS A CA    1 
ATOM   2709 C  C     . HIS A 1 341 ? 21.56400  -31.19300 -0.32200  1.000 23.56598  ? 341 HIS A C     1 
ATOM   2710 O  O     . HIS A 1 341 ? 21.62900  -31.65800 0.82200   1.000 27.51119  ? 341 HIS A O     1 
ATOM   2711 C  CB    . HIS A 1 341 ? 20.12900  -29.28800 -1.08600  1.000 26.74268  ? 341 HIS A CB    1 
ATOM   2712 C  CG    . HIS A 1 341 ? 19.01300  -29.64900 -0.16000  1.000 29.67198  ? 341 HIS A CG    1 
ATOM   2713 N  ND1   . HIS A 1 341 ? 18.44800  -28.74300 0.71300   1.000 29.53512  ? 341 HIS A ND1   1 
ATOM   2714 C  CD2   . HIS A 1 341 ? 18.38800  -30.82800 0.06500   1.000 25.10564  ? 341 HIS A CD2   1 
ATOM   2715 C  CE1   . HIS A 1 341 ? 17.50900  -29.34400 1.42100   1.000 32.91184  ? 341 HIS A CE1   1 
ATOM   2716 N  NE2   . HIS A 1 341 ? 17.45500  -30.61100 1.05000   1.000 27.67963  ? 341 HIS A NE2   1 
ATOM   2717 N  N     . MET A 1 342 ? 21.53100  -31.97600 -1.40300  1.000 22.29478  ? 342 MET A N     1 
ATOM   2718 C  CA    . MET A 1 342 ? 21.56800  -33.42700 -1.26100  1.000 25.31093  ? 342 MET A CA    1 
ATOM   2719 C  C     . MET A 1 342 ? 22.90700  -33.91500 -0.70700  1.000 23.93708  ? 342 MET A C     1 
ATOM   2720 O  O     . MET A 1 342 ? 22.94900  -34.92800 0.00200   1.000 24.75823  ? 342 MET A O     1 
ATOM   2721 C  CB    . MET A 1 342 ? 21.25800  -34.09100 -2.60200  1.000 26.77163  ? 342 MET A CB    1 
ATOM   2722 C  CG    . MET A 1 342 ? 19.88200  -33.71400 -3.17100  1.000 32.86973  ? 342 MET A CG    1 
ATOM   2723 S  SD    . MET A 1 342 ? 18.52100  -33.93700 -1.99200  1.000 35.09895  ? 342 MET A SD    1 
ATOM   2724 C  CE    . MET A 1 342 ? 18.64500  -35.69200 -1.63800  1.000 28.71923  ? 342 MET A CE    1 
ATOM   2725 N  N     . MET A 1 343 ? 24.00800  -33.22600 -1.02200  1.000 23.83444  ? 343 MET A N     1 
ATOM   2726 C  CA    . MET A 1 343 ? 25.29200  -33.57700 -0.42100  1.000 23.87392  ? 343 MET A CA    1 
ATOM   2727 C  C     . MET A 1 343 ? 25.26600  -33.37800 1.09100   1.000 23.93708  ? 343 MET A C     1 
ATOM   2728 O  O     . MET A 1 343 ? 25.79300  -34.20300 1.84500   1.000 23.58441  ? 343 MET A O     1 
ATOM   2729 C  CB    . MET A 1 343 ? 26.41300  -32.74600 -1.04100  1.000 30.63262  ? 343 MET A CB    1 
ATOM   2730 C  CG    . MET A 1 343 ? 26.80800  -33.14500 -2.45200  1.000 32.08806  ? 343 MET A CG    1 
ATOM   2731 S  SD    . MET A 1 343 ? 28.08100  -32.04000 -3.11200  1.000 42.08663  ? 343 MET A SD    1 
ATOM   2732 C  CE    . MET A 1 343 ? 27.88600  -32.31100 -4.87300  1.000 48.92166  ? 343 MET A CE    1 
ATOM   2733 N  N     . TYR A 1 344 ? 24.67800  -32.27000 1.54800   1.000 25.32146  ? 344 TYR A N     1 
ATOM   2734 C  CA    . TYR A 1 344 ? 24.58300  -32.01600 2.98100   1.000 24.84508  ? 344 TYR A CA    1 
ATOM   2735 C  C     . TYR A 1 344 ? 23.70700  -33.05800 3.66800   1.000 26.77953  ? 344 TYR A C     1 
ATOM   2736 O  O     . TYR A 1 344 ? 24.04000  -33.53900 4.75800   1.000 25.85310  ? 344 TYR A O     1 
ATOM   2737 C  CB    . TYR A 1 344 ? 24.04800  -30.60100 3.21800   1.000 26.58213  ? 344 TYR A CB    1 
ATOM   2738 C  CG    . TYR A 1 344 ? 23.98400  -30.19400 4.67400   1.000 26.91112  ? 344 TYR A CG    1 
ATOM   2739 C  CD1   . TYR A 1 344 ? 25.11000  -29.72100 5.33100   1.000 27.30327  ? 344 TYR A CD1   1 
ATOM   2740 C  CD2   . TYR A 1 344 ? 22.79200  -30.26800 5.38400   1.000 32.31440  ? 344 TYR A CD2   1 
ATOM   2741 C  CE1   . TYR A 1 344 ? 25.05500  -29.34400 6.66500   1.000 35.89115  ? 344 TYR A CE1   1 
ATOM   2742 C  CE2   . TYR A 1 344 ? 22.72600  -29.89400 6.71300   1.000 34.83839  ? 344 TYR A CE2   1 
ATOM   2743 C  CZ    . TYR A 1 344 ? 23.85800  -29.43400 7.35000   1.000 44.54218  ? 344 TYR A CZ    1 
ATOM   2744 O  OH    . TYR A 1 344 ? 23.79000  -29.06300 8.67600   1.000 43.99738  ? 344 TYR A OH    1 
ATOM   2745 N  N     . GLN A 1 345 ? 22.58100  -33.41800 3.04900   1.000 23.01329  ? 345 GLN A N     1 
ATOM   2746 C  CA    . GLN A 1 345 ? 21.72700  -34.45400 3.61800   1.000 24.65559  ? 345 GLN A CA    1 
ATOM   2747 C  C     . GLN A 1 345 ? 22.47300  -35.77900 3.70700   1.000 27.35328  ? 345 GLN A C     1 
ATOM   2748 O  O     . GLN A 1 345 ? 22.41100  -36.47600 4.72600   1.000 25.59517  ? 345 GLN A O     1 
ATOM   2749 C  CB    . GLN A 1 345 ? 20.45700  -34.60700 2.77800   1.000 26.54529  ? 345 GLN A CB    1 
ATOM   2750 C  CG    . GLN A 1 345 ? 19.49700  -33.43100 2.86700   1.000 30.69052  ? 345 GLN A CG    1 
ATOM   2751 C  CD    . GLN A 1 345 ? 19.08300  -33.13100 4.29000   1.000 30.41417  ? 345 GLN A CD    1 
ATOM   2752 O  OE1   . GLN A 1 345 ? 18.77100  -34.04000 5.06500   1.000 32.17491  ? 345 GLN A OE1   1 
ATOM   2753 N  NE2   . GLN A 1 345 ? 19.09500  -31.85300 4.65200   1.000 32.38809  ? 345 GLN A NE2   1 
ATOM   2754 N  N     . ALA A 1 346 ? 23.18400  -36.14300 2.63800   1.000 27.69806  ? 346 ALA A N     1 
ATOM   2755 C  CA    . ALA A 1 346 ? 23.98400  -37.36300 2.65500   1.000 28.87715  ? 346 ALA A CA    1 
ATOM   2756 C  C     . ALA A 1 346 ? 25.04700  -37.31600 3.74900   1.000 27.20589  ? 346 ALA A C     1 
ATOM   2757 O  O     . ALA A 1 346 ? 25.29800  -38.31900 4.42600   1.000 33.14345  ? 346 ALA A O     1 
ATOM   2758 C  CB    . ALA A 1 346 ? 24.61900  -37.58500 1.28300   1.000 29.38773  ? 346 ALA A CB    1 
ATOM   2759 N  N     . MET A 1 347 ? 25.70100  -36.16400 3.92100   1.000 22.61061  ? 347 MET A N     1 
ATOM   2760 C  CA    . MET A 1 347 ? 26.66800  -36.02100 5.00900   1.000 23.10540  ? 347 MET A CA    1 
ATOM   2761 C  C     . MET A 1 347 ? 26.01200  -36.26600 6.36500   1.000 22.39479  ? 347 MET A C     1 
ATOM   2762 O  O     . MET A 1 347 ? 26.58900  -36.93600 7.23000   1.000 25.95574  ? 347 MET A O     1 
ATOM   2763 C  CB    . MET A 1 347 ? 27.30100  -34.63100 4.96800   1.000 21.05252  ? 347 MET A CB    1 
ATOM   2764 C  CG    . MET A 1 347 ? 28.48500  -34.45200 5.90800   1.000 21.48152  ? 347 MET A CG    1 
ATOM   2765 S  SD    . MET A 1 347 ? 29.07100  -32.76000 5.88500   1.000 25.62412  ? 347 MET A SD    1 
ATOM   2766 C  CE    . MET A 1 347 ? 30.51800  -32.86600 6.94100   1.000 28.36656  ? 347 MET A CE    1 
ATOM   2767 N  N     . GLY A 1 348 ? 24.81300  -35.70900 6.57100   1.000 27.31643  ? 348 GLY A N     1 
ATOM   2768 C  CA    . GLY A 1 348 ? 24.08600  -35.93700 7.81400   1.000 26.11366  ? 348 GLY A CA    1 
ATOM   2769 C  C     . GLY A 1 348 ? 23.83900  -37.40700 8.09200   1.000 27.42697  ? 348 GLY A C     1 
ATOM   2770 O  O     . GLY A 1 348 ? 24.01300  -37.87700 9.22100   1.000 33.81984  ? 348 GLY A O     1 
ATOM   2771 N  N     . VAL A 1 349 ? 23.41100  -38.15100 7.06800   1.000 26.22946  ? 349 VAL A N     1 
ATOM   2772 C  CA    . VAL A 1 349 ? 23.18700  -39.58600 7.22600   1.000 26.25052  ? 349 VAL A CA    1 
ATOM   2773 C  C     . VAL A 1 349 ? 24.48500  -40.29600 7.59900   1.000 27.32170  ? 349 VAL A C     1 
ATOM   2774 O  O     . VAL A 1 349 ? 24.49900  -41.17200 8.47300   1.000 25.75046  ? 349 VAL A O     1 
ATOM   2775 C  CB    . VAL A 1 349 ? 22.56400  -40.17700 5.94200   1.000 24.77665  ? 349 VAL A CB    1 
ATOM   2776 C  CG1   . VAL A 1 349 ? 22.41300  -41.68100 6.06100   1.000 28.85872  ? 349 VAL A CG1   1 
ATOM   2777 C  CG2   . VAL A 1 349 ? 21.20500  -39.54000 5.67100   1.000 24.21869  ? 349 VAL A CG2   1 
ATOM   2778 N  N     . CYS A 1 350 ? 25.59100  -39.94200 6.92700   1.000 28.08495  ? 350 CYS A N     1 
ATOM   2779 C  CA    . CYS A 1 350 ? 26.89100  -40.53900 7.23200   1.000 29.95359  ? 350 CYS A CA    1 
ATOM   2780 C  C     . CYS A 1 350 ? 27.31200  -40.25600 8.66900   1.000 30.06939  ? 350 CYS A C     1 
ATOM   2781 O  O     . CYS A 1 350 ? 27.82000  -41.14700 9.36100   1.000 28.87451  ? 350 CYS A O     1 
ATOM   2782 C  CB    . CYS A 1 350 ? 27.95600  -40.01800 6.26100   1.000 31.13268  ? 350 CYS A CB    1 
ATOM   2783 S  SG    . CYS A 1 350 ? 27.83000  -40.63700 4.56100   1.000 33.95407  ? 350 CYS A SG    1 
ATOM   2784 N  N     . LEU A 1 351 ? 27.11900  -39.01800 9.13200   1.000 25.50832  ? 351 LEU A N     1 
ATOM   2785 C  CA    . LEU A 1 351 ? 27.47600  -38.67300 10.50600  1.000 29.64829  ? 351 LEU A CA    1 
ATOM   2786 C  C     . LEU A 1 351 ? 26.67300  -39.48900 11.51200  1.000 31.07478  ? 351 LEU A C     1 
ATOM   2787 O  O     . LEU A 1 351 ? 27.21300  -39.93200 12.53300  1.000 27.08746  ? 351 LEU A O     1 
ATOM   2788 C  CB    . LEU A 1 351 ? 27.27700  -37.17600 10.74300  1.000 30.33258  ? 351 LEU A CB    1 
ATOM   2789 C  CG    . LEU A 1 351 ? 28.29500  -36.23700 10.09100  1.000 26.40843  ? 351 LEU A CG    1 
ATOM   2790 C  CD1   . LEU A 1 351 ? 27.91300  -34.77800 10.33300  1.000 28.35603  ? 351 LEU A CD1   1 
ATOM   2791 C  CD2   . LEU A 1 351 ? 29.69700  -36.52300 10.60700  1.000 28.88767  ? 351 LEU A CD2   1 
ATOM   2792 N  N     . TYR A 1 352 ? 25.37300  -39.68100 11.25600  1.000 30.62472  ? 352 TYR A N     1 
ATOM   2793 C  CA    . TYR A 1 352 ? 24.57300  -40.51100 12.15100  1.000 32.40125  ? 352 TYR A CA    1 
ATOM   2794 C  C     . TYR A 1 352 ? 25.04800  -41.95700 12.13600  1.000 29.09033  ? 352 TYR A C     1 
ATOM   2795 O  O     . TYR A 1 352 ? 25.11200  -42.60800 13.18600  1.000 31.01951  ? 352 TYR A O     1 
ATOM   2796 C  CB    . TYR A 1 352 ? 23.09200  -40.44300 11.78200  1.000 32.72234  ? 352 TYR A CB    1 
ATOM   2797 C  CG    . TYR A 1 352 ? 22.24400  -41.22200 12.75900  1.000 42.24980  ? 352 TYR A CG    1 
ATOM   2798 C  CD1   . TYR A 1 352 ? 22.10700  -40.79400 14.07300  1.000 50.53237  ? 352 TYR A CD1   1 
ATOM   2799 C  CD2   . TYR A 1 352 ? 21.61100  -42.40000 12.38500  1.000 42.51826  ? 352 TYR A CD2   1 
ATOM   2800 C  CE1   . TYR A 1 352 ? 21.34600  -41.50300 14.98200  1.000 52.63789  ? 352 TYR A CE1   1 
ATOM   2801 C  CE2   . TYR A 1 352 ? 20.84700  -43.11600 13.28900  1.000 53.66433  ? 352 TYR A CE2   1 
ATOM   2802 C  CZ    . TYR A 1 352 ? 20.71800  -42.66200 14.58800  1.000 50.76398  ? 352 TYR A CZ    1 
ATOM   2803 O  OH    . TYR A 1 352 ? 19.96100  -43.36400 15.50200  1.000 57.72008  ? 352 TYR A OH    1 
ATOM   2804 N  N     . MET A 1 353 ? 25.37600  -42.48300 10.95200  1.000 29.57197  ? 353 MET A N     1 
ATOM   2805 C  CA    . MET A 1 353 ? 25.91800  -43.83400 10.84600  1.000 33.96460  ? 353 MET A CA    1 
ATOM   2806 C  C     . MET A 1 353 ? 27.33100  -43.94700 11.39800  1.000 29.52722  ? 353 MET A C     1 
ATOM   2807 O  O     . MET A 1 353 ? 27.87600  -45.05500 11.42300  1.000 30.12730  ? 353 MET A O     1 
ATOM   2808 C  CB    . MET A 1 353 ? 25.92300  -44.29100 9.38900   1.000 34.35412  ? 353 MET A CB    1 
ATOM   2809 C  CG    . MET A 1 353 ? 24.55000  -44.44000 8.78800   1.000 40.07586  ? 353 MET A CG    1 
ATOM   2810 S  SD    . MET A 1 353 ? 24.65800  -44.78500 7.02400   1.000 42.46035  ? 353 MET A SD    1 
ATOM   2811 C  CE    . MET A 1 353 ? 24.99000  -46.54300 7.04900   1.000 43.74209  ? 353 MET A CE    1 
ATOM   2812 N  N     . GLN A 1 354 ? 27.94000  -42.83500 11.81100  1.000 30.14835  ? 354 GLN A N     1 
ATOM   2813 C  CA    . GLN A 1 354 ? 29.33400  -42.81500 12.24000  1.000 33.16977  ? 354 GLN A CA    1 
ATOM   2814 C  C     . GLN A 1 354 ? 30.24800  -43.33000 11.13500  1.000 33.53823  ? 354 GLN A C     1 
ATOM   2815 O  O     . GLN A 1 354 ? 31.24600  -44.00200 11.39600  1.000 34.06198  ? 354 GLN A O     1 
ATOM   2816 C  CB    . GLN A 1 354 ? 29.53000  -43.60600 13.53500  1.000 31.11426  ? 354 GLN A CB    1 
ATOM   2817 C  CG    . GLN A 1 354 ? 28.60000  -43.14100 14.63900  1.000 32.10122  ? 354 GLN A CG    1 
ATOM   2818 C  CD    . GLN A 1 354 ? 28.95800  -43.72400 15.98400  1.000 33.17766  ? 354 GLN A CD    1 
ATOM   2819 O  OE1   . GLN A 1 354 ? 29.92400  -44.47300 16.11000  1.000 45.08962  ? 354 GLN A OE1   1 
ATOM   2820 N  NE2   . GLN A 1 354 ? 28.18600  -43.37300 17.00100  1.000 34.06461  ? 354 GLN A NE2   1 
ATOM   2821 N  N     . ASP A 1 355 ? 29.88000  -43.03500 9.89100   1.000 36.65176  ? 355 ASP A N     1 
ATOM   2822 C  CA    . ASP A 1 355 ? 30.70900  -43.29900 8.72000   1.000 33.59877  ? 355 ASP A CA    1 
ATOM   2823 C  C     . ASP A 1 355 ? 31.52600  -42.03700 8.48400   1.000 31.79065  ? 355 ASP A C     1 
ATOM   2824 O  O     . ASP A 1 355 ? 31.12700  -41.14100 7.73900   1.000 28.52974  ? 355 ASP A O     1 
ATOM   2825 C  CB    . ASP A 1 355 ? 29.84000  -43.66500 7.52200   1.000 37.72821  ? 355 ASP A CB    1 
ATOM   2826 C  CG    . ASP A 1 355 ? 30.64100  -43.85700 6.24600   1.000 38.63884  ? 355 ASP A CG    1 
ATOM   2827 O  OD1   . ASP A 1 355 ? 31.89300  -43.82900 6.28600   1.000 39.02836  ? 355 ASP A OD1   1 
ATOM   2828 O  OD2   . ASP A 1 355 ? 30.00600  -44.03400 5.18800   1.000 44.72378  ? 355 ASP A OD2   1 
ATOM   2829 N  N     . TRP A 1 356 ? 32.67900  -41.95800 9.15300   1.000 25.39778  ? 356 TRP A N     1 
ATOM   2830 C  CA    . TRP A 1 356 ? 33.43900  -40.71400 9.14700   1.000 25.98469  ? 356 TRP A CA    1 
ATOM   2831 C  C     . TRP A 1 356 ? 34.08300  -40.45700 7.79200   1.000 24.21080  ? 356 TRP A C     1 
ATOM   2832 O  O     . TRP A 1 356 ? 34.14600  -39.30800 7.34300   1.000 25.40568  ? 356 TRP A O     1 
ATOM   2833 C  CB    . TRP A 1 356 ? 34.49200  -40.73500 10.25700  1.000 29.80884  ? 356 TRP A CB    1 
ATOM   2834 C  CG    . TRP A 1 356 ? 33.96200  -41.17200 11.59400  1.000 28.79556  ? 356 TRP A CG    1 
ATOM   2835 C  CD1   . TRP A 1 356 ? 34.43000  -42.19600 12.36400  1.000 29.05085  ? 356 TRP A CD1   1 
ATOM   2836 C  CD2   . TRP A 1 356 ? 32.85400  -40.60400 12.31300  1.000 27.59541  ? 356 TRP A CD2   1 
ATOM   2837 N  NE1   . TRP A 1 356 ? 33.69000  -42.29800 13.51900  1.000 29.60618  ? 356 TRP A NE1   1 
ATOM   2838 C  CE2   . TRP A 1 356 ? 32.71500  -41.33500 13.50900  1.000 30.27468  ? 356 TRP A CE2   1 
ATOM   2839 C  CE3   . TRP A 1 356 ? 31.96600  -39.55500 12.05800  1.000 27.89282  ? 356 TRP A CE3   1 
ATOM   2840 C  CZ2   . TRP A 1 356 ? 31.72700  -41.04800 14.45300  1.000 29.65092  ? 356 TRP A CZ2   1 
ATOM   2841 C  CZ3   . TRP A 1 356 ? 30.98100  -39.27100 12.99300  1.000 31.93541  ? 356 TRP A CZ3   1 
ATOM   2842 C  CH2   . TRP A 1 356 ? 30.87600  -40.01200 14.18100  1.000 29.91674  ? 356 TRP A CH2   1 
ATOM   2843 N  N     . GLU A 1 357 ? 34.57500  -41.50800 7.13300   1.000 28.09284  ? 357 GLU A N     1 
ATOM   2844 C  CA    . GLU A 1 357 ? 35.15200  -41.35100 5.80000   1.000 34.61204  ? 357 GLU A CA    1 
ATOM   2845 C  C     . GLU A 1 357 ? 34.12000  -40.80000 4.82400   1.000 30.78790  ? 357 GLU A C     1 
ATOM   2846 O  O     . GLU A 1 357 ? 34.39500  -39.84900 4.08400   1.000 30.02465  ? 357 GLU A O     1 
ATOM   2847 C  CB    . GLU A 1 357 ? 35.70100  -42.69000 5.29900   1.000 38.64148  ? 357 GLU A CB    1 
ATOM   2848 C  CG    . GLU A 1 357 ? 36.89700  -43.23000 6.08100   1.000 53.69328  ? 357 GLU A CG    1 
ATOM   2849 C  CD    . GLU A 1 357 ? 38.18300  -42.45500 5.82900   1.000 65.08675  ? 357 GLU A CD    1 
ATOM   2850 O  OE1   . GLU A 1 357 ? 38.21300  -41.62000 4.90000   1.000 106.11272 ? 357 GLU A OE1   1 
ATOM   2851 O  OE2   . GLU A 1 357 ? 39.17100  -42.68400 6.56200   1.000 100.25939 ? 357 GLU A OE2   1 
ATOM   2852 N  N     . GLY A 1 358 ? 32.92000  -41.38700 4.81600   1.000 29.35878  ? 358 GLY A N     1 
ATOM   2853 C  CA    . GLY A 1 358 ? 31.86800  -40.89700 3.93600   1.000 28.08495  ? 358 GLY A CA    1 
ATOM   2854 C  C     . GLY A 1 358 ? 31.52800  -39.44000 4.18200   1.000 29.74304  ? 358 GLY A C     1 
ATOM   2855 O  O     . GLY A 1 358 ? 31.44000  -38.64500 3.24400   1.000 29.46669  ? 358 GLY A O     1 
ATOM   2856 N  N     . ALA A 1 359 ? 31.33000  -39.07400 5.45300   1.000 26.53739  ? 359 ALA A N     1 
ATOM   2857 C  CA    . ALA A 1 359 ? 31.00000  -37.69300 5.79800   1.000 26.29263  ? 359 ALA A CA    1 
ATOM   2858 C  C     . ALA A 1 359 ? 32.11500  -36.73000 5.40200   1.000 26.12682  ? 359 ALA A C     1 
ATOM   2859 O  O     . ALA A 1 359 ? 31.84600  -35.60100 4.97400   1.000 22.44216  ? 359 ALA A O     1 
ATOM   2860 C  CB    . ALA A 1 359 ? 30.70100  -37.58000 7.29500   1.000 26.72426  ? 359 ALA A CB    1 
ATOM   2861 N  N     . LEU A 1 360 ? 33.37500  -37.14100 5.57200   1.000 23.29490  ? 360 LEU A N     1 
ATOM   2862 C  CA    . LEU A 1 360 ? 34.48900  -36.27100 5.20400   1.000 28.02441  ? 360 LEU A CA    1 
ATOM   2863 C  C     . LEU A 1 360 ? 34.47300  -35.96200 3.70700   1.000 26.85322  ? 360 LEU A C     1 
ATOM   2864 O  O     . LEU A 1 360 ? 34.64300  -34.80700 3.29900   1.000 29.40616  ? 360 LEU A O     1 
ATOM   2865 C  CB    . LEU A 1 360 ? 35.81500  -36.91400 5.61000   1.000 28.32971  ? 360 LEU A CB    1 
ATOM   2866 C  CG    . LEU A 1 360 ? 37.05300  -36.07400 5.28800   1.000 32.45389  ? 360 LEU A CG    1 
ATOM   2867 C  CD1   . LEU A 1 360 ? 37.02200  -34.74900 6.05200   1.000 30.24310  ? 360 LEU A CD1   1 
ATOM   2868 C  CD2   . LEU A 1 360 ? 38.32500  -36.84900 5.58000   1.000 31.86171  ? 360 LEU A CD2   1 
ATOM   2869 N  N     . GLN A 1 361 ? 34.26100  -36.98400 2.87300   1.000 28.75345  ? 361 GLN A N     1 
ATOM   2870 C  CA    . GLN A 1 361 ? 34.20100  -36.75900 1.42900   1.000 33.58297  ? 361 GLN A CA    1 
ATOM   2871 C  C     . GLN A 1 361 ? 33.13900  -35.73100 1.05900   1.000 27.04535  ? 361 GLN A C     1 
ATOM   2872 O  O     . GLN A 1 361 ? 33.38200  -34.86400 0.21500   1.000 31.75381  ? 361 GLN A O     1 
ATOM   2873 C  CB    . GLN A 1 361 ? 33.95500  -38.06700 0.68300   1.000 33.80405  ? 361 GLN A CB    1 
ATOM   2874 C  CG    . GLN A 1 361 ? 35.19000  -38.92400 0.52200   1.000 53.35377  ? 361 GLN A CG    1 
ATOM   2875 C  CD    . GLN A 1 361 ? 34.94000  -40.15200 -0.33900  1.000 72.15076  ? 361 GLN A CD    1 
ATOM   2876 O  OE1   . GLN A 1 361 ? 35.65000  -40.38900 -1.31900  1.000 73.92202  ? 361 GLN A OE1   1 
ATOM   2877 N  NE2   . GLN A 1 361 ? 33.92800  -40.93800 0.02200   1.000 67.67917  ? 361 GLN A NE2   1 
ATOM   2878 N  N     . TYR A 1 362 ? 31.94800  -35.81800 1.66300   1.000 28.15074  ? 362 TYR A N     1 
ATOM   2879 C  CA    . TYR A 1 362 ? 30.90700  -34.83300 1.37300   1.000 28.05600  ? 362 TYR A CA    1 
ATOM   2880 C  C     . TYR A 1 362 ? 31.28600  -33.44600 1.88000   1.000 24.32660  ? 362 TYR A C     1 
ATOM   2881 O  O     . TYR A 1 362 ? 31.05300  -32.44300 1.19600   1.000 25.61623  ? 362 TYR A O     1 
ATOM   2882 C  CB    . TYR A 1 362 ? 29.57100  -35.28200 1.96400   1.000 29.66671  ? 362 TYR A CB    1 
ATOM   2883 C  CG    . TYR A 1 362 ? 28.90200  -36.36900 1.15300   1.000 26.65583  ? 362 TYR A CG    1 
ATOM   2884 C  CD1   . TYR A 1 362 ? 28.49700  -36.13600 -0.15900  1.000 24.28712  ? 362 TYR A CD1   1 
ATOM   2885 C  CD2   . TYR A 1 362 ? 28.67000  -37.62400 1.69600   1.000 28.65344  ? 362 TYR A CD2   1 
ATOM   2886 C  CE1   . TYR A 1 362 ? 27.87800  -37.12700 -0.90600  1.000 23.82128  ? 362 TYR A CE1   1 
ATOM   2887 C  CE2   . TYR A 1 362 ? 28.05600  -38.62100 0.95700   1.000 32.96448  ? 362 TYR A CE2   1 
ATOM   2888 C  CZ    . TYR A 1 362 ? 27.66100  -38.36700 -0.34300  1.000 28.99558  ? 362 TYR A CZ    1 
ATOM   2889 O  OH    . TYR A 1 362 ? 27.04700  -39.35900 -1.07500  1.000 41.48392  ? 362 TYR A OH    1 
ATOM   2890 N  N     . GLY A 1 363 ? 31.83700  -33.36000 3.09000   1.000 25.72414  ? 363 GLY A N     1 
ATOM   2891 C  CA    . GLY A 1 363 ? 32.24900  -32.06500 3.61200   1.000 21.56048  ? 363 GLY A CA    1 
ATOM   2892 C  C     . GLY A 1 363 ? 33.26300  -31.35600 2.73400   1.000 21.05516  ? 363 GLY A C     1 
ATOM   2893 O  O     . GLY A 1 363 ? 33.18600  -30.14000 2.53400   1.000 24.26607  ? 363 GLY A O     1 
ATOM   2894 N  N     . GLN A 1 364 ? 34.24500  -32.10100 2.21900   1.000 25.21881  ? 364 GLN A N     1 
ATOM   2895 C  CA    . GLN A 1 364 ? 35.26900  -31.50200 1.36600   1.000 24.18711  ? 364 GLN A CA    1 
ATOM   2896 C  C     . GLN A 1 364 ? 34.68600  -30.93100 0.07500   1.000 24.22396  ? 364 GLN A C     1 
ATOM   2897 O  O     . GLN A 1 364 ? 35.20100  -29.94000 -0.45200  1.000 29.99570  ? 364 GLN A O     1 
ATOM   2898 C  CB    . GLN A 1 364 ? 36.35200  -32.54000 1.06800   1.000 25.36883  ? 364 GLN A CB    1 
ATOM   2899 C  CG    . GLN A 1 364 ? 37.20900  -32.86500 2.29100   1.000 27.72964  ? 364 GLN A CG    1 
ATOM   2900 C  CD    . GLN A 1 364 ? 38.10100  -34.06400 2.07900   1.000 30.61683  ? 364 GLN A CD    1 
ATOM   2901 O  OE1   . GLN A 1 364 ? 37.77100  -34.96500 1.30800   1.000 35.00946  ? 364 GLN A OE1   1 
ATOM   2902 N  NE2   . GLN A 1 364 ? 39.23400  -34.09300 2.77500   1.000 34.23568  ? 364 GLN A NE2   1 
ATOM   2903 N  N     . LYS A 1 365 ? 33.61700  -31.53200 -0.45100  1.000 23.60546  ? 365 LYS A N     1 
ATOM   2904 C  CA    . LYS A 1 365 ? 32.96400  -30.98700 -1.63900  1.000 29.04559  ? 365 LYS A CA    1 
ATOM   2905 C  C     . LYS A 1 365 ? 32.06500  -29.79300 -1.32600  1.000 28.04284  ? 365 LYS A C     1 
ATOM   2906 O  O     . LYS A 1 365 ? 31.78300  -28.98900 -2.22200  1.000 32.05121  ? 365 LYS A O     1 
ATOM   2907 C  CB    . LYS A 1 365 ? 32.13500  -32.07800 -2.32700  1.000 30.57998  ? 365 LYS A CB    1 
ATOM   2908 C  CG    . LYS A 1 365 ? 32.96000  -33.13400 -3.03000  1.000 39.06784  ? 365 LYS A CG    1 
ATOM   2909 C  CD    . LYS A 1 365 ? 32.11600  -34.34500 -3.38200  1.000 42.05767  ? 365 LYS A CD    1 
ATOM   2910 C  CE    . LYS A 1 365 ? 31.09300  -34.01900 -4.45700  1.000 68.53453  ? 365 LYS A CE    1 
ATOM   2911 N  NZ    . LYS A 1 365 ? 31.69000  -33.95400 -5.81900  1.000 83.77583  ? 365 LYS A NZ    1 
ATOM   2912 N  N     . ILE A 1 366 ? 31.62500  -29.64400 -0.07900  1.000 33.84090  ? 366 ILE A N     1 
ATOM   2913 C  CA    . ILE A 1 366 ? 30.64100  -28.62000 0.25600   1.000 25.59517  ? 366 ILE A CA    1 
ATOM   2914 C  C     . ILE A 1 366 ? 31.28200  -27.28900 0.65000   1.000 26.70057  ? 366 ILE A C     1 
ATOM   2915 O  O     . ILE A 1 366 ? 30.71800  -26.22600 0.35800   1.000 24.14763  ? 366 ILE A O     1 
ATOM   2916 C  CB    . ILE A 1 366 ? 29.71400  -29.13600 1.37500   1.000 24.11868  ? 366 ILE A CB    1 
ATOM   2917 C  CG1   . ILE A 1 366 ? 28.81500  -30.26600 0.87200   1.000 26.45844  ? 366 ILE A CG1   1 
ATOM   2918 C  CG2   . ILE A 1 366 ? 28.87000  -28.01300 1.94200   1.000 23.40017  ? 366 ILE A CG2   1 
ATOM   2919 C  CD1   . ILE A 1 366 ? 28.12100  -31.04500 1.99300   1.000 28.79293  ? 366 ILE A CD1   1 
ATOM   2920 N  N     . ILE A 1 367 ? 32.45200  -27.32300 1.30400   1.000 19.97345  ? 367 ILE A N     1 
ATOM   2921 C  CA    . ILE A 1 367 ? 32.92900  -26.16700 2.06400   1.000 26.54529  ? 367 ILE A CA    1 
ATOM   2922 C  C     . ILE A 1 367 ? 33.25800  -24.98100 1.15400   1.000 24.32660  ? 367 ILE A C     1 
ATOM   2923 O  O     . ILE A 1 367 ? 32.92300  -23.83600 1.47200   1.000 25.85310  ? 367 ILE A O     1 
ATOM   2924 C  CB    . ILE A 1 367 ? 34.12700  -26.56200 2.94900   1.000 24.91351  ? 367 ILE A CB    1 
ATOM   2925 C  CG1   . ILE A 1 367 ? 34.60100  -25.36200 3.76900   1.000 24.28712  ? 367 ILE A CG1   1 
ATOM   2926 C  CG2   . ILE A 1 367 ? 35.26200  -27.15600 2.11700   1.000 29.39037  ? 367 ILE A CG2   1 
ATOM   2927 C  CD1   . ILE A 1 367 ? 33.53700  -24.76200 4.67300   1.000 21.01831  ? 367 ILE A CD1   1 
ATOM   2928 N  N     . LYS A 1 368 ? 33.93800  -25.22400 0.03100   1.000 22.09212  ? 368 LYS A N     1 
ATOM   2929 C  CA    . LYS A 1 368 ? 34.30600  -24.08800 -0.83500  1.000 33.05923  ? 368 LYS A CA    1 
ATOM   2930 C  C     . LYS A 1 368 ? 33.09000  -23.43800 -1.46000  1.000 23.42649  ? 368 LYS A C     1 
ATOM   2931 O  O     . LYS A 1 368 ? 33.00700  -22.18400 -1.43800  1.000 27.30854  ? 368 LYS A O     1 
ATOM   2932 C  CB    . LYS A 1 368 ? 35.32500  -24.54700 -1.88400  1.000 41.53656  ? 368 LYS A CB    1 
ATOM   2933 C  CG    . LYS A 1 368 ? 36.09000  -23.40500 -2.53100  1.000 64.81830  ? 368 LYS A CG    1 
ATOM   2934 C  CD    . LYS A 1 368 ? 37.02600  -23.91700 -3.61000  1.000 68.22134  ? 368 LYS A CD    1 
ATOM   2935 C  CE    . LYS A 1 368 ? 37.73700  -22.77600 -4.31600  1.000 67.71601  ? 368 LYS A CE    1 
ATOM   2936 N  NZ    . LYS A 1 368 ? 38.53900  -23.27000 -5.46800  1.000 69.33463  ? 368 LYS A NZ    1 
ATOM   2937 N  N     . PRO A 1 369 ? 32.11900  -24.14900 -2.04800  1.000 28.92715  ? 369 PRO A N     1 
ATOM   2938 C  CA    . PRO A 1 369 ? 30.87100  -23.48800 -2.46400  1.000 25.72677  ? 369 PRO A CA    1 
ATOM   2939 C  C     . PRO A 1 369 ? 30.14200  -22.77800 -1.32900  1.000 23.99761  ? 369 PRO A C     1 
ATOM   2940 O  O     . PRO A 1 369 ? 29.57800  -21.70000 -1.54700  1.000 23.88707  ? 369 PRO A O     1 
ATOM   2941 C  CB    . PRO A 1 369 ? 30.04000  -24.63600 -3.04800  1.000 30.85107  ? 369 PRO A CB    1 
ATOM   2942 C  CG    . PRO A 1 369 ? 31.05000  -25.61800 -3.52200  1.000 31.48272  ? 369 PRO A CG    1 
ATOM   2943 C  CD    . PRO A 1 369 ? 32.16000  -25.55900 -2.50600  1.000 34.99367  ? 369 PRO A CD    1 
ATOM   2944 N  N     . TYR A 1 370 ? 30.12400  -23.35500 -0.12300  1.000 24.99773  ? 370 TYR A N     1 
ATOM   2945 C  CA    . TYR A 1 370 ? 29.51700  -22.67100 1.02100   1.000 24.31081  ? 370 TYR A CA    1 
ATOM   2946 C  C     . TYR A 1 370 ? 30.14000  -21.30100 1.25700   1.000 26.09787  ? 370 TYR A C     1 
ATOM   2947 O  O     . TYR A 1 370 ? 29.43400  -20.32700 1.54900   1.000 27.65068  ? 370 TYR A O     1 
ATOM   2948 C  CB    . TYR A 1 370 ? 29.66500  -23.52500 2.27900   1.000 26.32947  ? 370 TYR A CB    1 
ATOM   2949 C  CG    . TYR A 1 370 ? 28.46000  -24.35000 2.62300   1.000 22.40532  ? 370 TYR A CG    1 
ATOM   2950 C  CD1   . TYR A 1 370 ? 27.55600  -24.74200 1.64400   1.000 22.82379  ? 370 TYR A CD1   1 
ATOM   2951 C  CD2   . TYR A 1 370 ? 28.24000  -24.76700 3.92700   1.000 26.36369  ? 370 TYR A CD2   1 
ATOM   2952 C  CE1   . TYR A 1 370 ? 26.45000  -25.50900 1.96400   1.000 27.13746  ? 370 TYR A CE1   1 
ATOM   2953 C  CE2   . TYR A 1 370 ? 27.14100  -25.53200 4.25900   1.000 27.48487  ? 370 TYR A CE2   1 
ATOM   2954 C  CZ    . TYR A 1 370 ? 26.25200  -25.90500 3.27600   1.000 36.55965  ? 370 TYR A CZ    1 
ATOM   2955 O  OH    . TYR A 1 370 ? 25.16500  -26.67500 3.61300   1.000 25.75309  ? 370 TYR A OH    1 
ATOM   2956 N  N     . SER A 1 371 ? 31.46900  -21.22000 1.17800   1.000 29.67987  ? 371 SER A N     1 
ATOM   2957 C  CA    . SER A 1 371 ? 32.17400  -19.97800 1.48100   1.000 30.65104  ? 371 SER A CA    1 
ATOM   2958 C  C     . SER A 1 371 ? 31.74000  -18.83700 0.56800   1.000 31.39324  ? 371 SER A C     1 
ATOM   2959 O  O     . SER A 1 371 ? 31.68900  -17.68000 1.00000   1.000 31.37481  ? 371 SER A O     1 
ATOM   2960 C  CB    . SER A 1 371 ? 33.68100  -20.20800 1.38900   1.000 31.84066  ? 371 SER A CB    1 
ATOM   2961 O  OG    . SER A 1 371 ? 34.06600  -21.18300 2.34200   1.000 45.57125  ? 371 SER A OG    1 
ATOM   2962 N  N     . LYS A 1 372 ? 31.45300  -19.12700 -0.70200  1.000 25.46095  ? 372 LYS A N     1 
ATOM   2963 C  CA    . LYS A 1 372 ? 31.05400  -18.05600 -1.60900  1.000 30.10098  ? 372 LYS A CA    1 
ATOM   2964 C  C     . LYS A 1 372 ? 29.54300  -17.80200 -1.62100  1.000 25.38462  ? 372 LYS A C     1 
ATOM   2965 O  O     . LYS A 1 372 ? 29.11700  -16.66600 -1.85800  1.000 30.32995  ? 372 LYS A O     1 
ATOM   2966 C  CB    . LYS A 1 372 ? 31.55300  -18.34500 -3.03000  1.000 34.85418  ? 372 LYS A CB    1 
ATOM   2967 C  CG    . LYS A 1 372 ? 30.88800  -19.50900 -3.72400  1.000 48.12156  ? 372 LYS A CG    1 
ATOM   2968 C  CD    . LYS A 1 372 ? 31.24200  -19.52100 -5.20100  1.000 51.02717  ? 372 LYS A CD    1 
ATOM   2969 C  CE    . LYS A 1 372 ? 30.75900  -20.79600 -5.86900  1.000 59.57820  ? 372 LYS A CE    1 
ATOM   2970 N  NZ    . LYS A 1 372 ? 31.23100  -20.90400 -7.27600  1.000 66.25268  ? 372 LYS A NZ    1 
ATOM   2971 N  N     . HIS A 1 373 ? 28.71300  -18.81400 -1.37000  1.000 21.83420  ? 373 HIS A N     1 
ATOM   2972 C  CA    . HIS A 1 373 ? 27.27100  -18.57800 -1.41900  1.000 24.84772  ? 373 HIS A CA    1 
ATOM   2973 C  C     . HIS A 1 373 ? 26.76700  -17.85500 -0.17300  1.000 26.99008  ? 373 HIS A C     1 
ATOM   2974 O  O     . HIS A 1 373 ? 25.87400  -17.00500 -0.26700  1.000 29.79041  ? 373 HIS A O     1 
ATOM   2975 C  CB    . HIS A 1 373 ? 26.52700  -19.89900 -1.60400  1.000 26.77426  ? 373 HIS A CB    1 
ATOM   2976 C  CG    . HIS A 1 373 ? 26.73000  -20.52400 -2.95000  1.000 24.57663  ? 373 HIS A CG    1 
ATOM   2977 N  ND1   . HIS A 1 373 ? 26.94200  -19.77900 -4.09200  1.000 26.56371  ? 373 HIS A ND1   1 
ATOM   2978 C  CD2   . HIS A 1 373 ? 26.76100  -21.82200 -3.33600  1.000 28.73502  ? 373 HIS A CD2   1 
ATOM   2979 C  CE1   . HIS A 1 373 ? 27.08800  -20.59200 -5.12400  1.000 33.80932  ? 373 HIS A CE1   1 
ATOM   2980 N  NE2   . HIS A 1 373 ? 26.98200  -21.83700 -4.69200  1.000 24.88719  ? 373 HIS A NE2   1 
ATOM   2981 N  N     . TYR A 1 374 ? 27.31400  -18.18200 0.99800   1.000 24.86614  ? 374 TYR A N     1 
ATOM   2982 C  CA    . TYR A 1 374 ? 26.90700  -17.58000 2.26000   1.000 25.47674  ? 374 TYR A CA    1 
ATOM   2983 C  C     . TYR A 1 374 ? 27.62200  -16.25000 2.50100   1.000 26.09260  ? 374 TYR A C     1 
ATOM   2984 O  O     . TYR A 1 374 ? 28.64600  -15.96000 1.87700   1.000 26.24525  ? 374 TYR A O     1 
ATOM   2985 C  CB    . TYR A 1 374 ? 27.20200  -18.53400 3.41700   1.000 26.26104  ? 374 TYR A CB    1 
ATOM   2986 C  CG    . TYR A 1 374 ? 26.20300  -19.65900 3.60200   1.000 22.07896  ? 374 TYR A CG    1 
ATOM   2987 C  CD1   . TYR A 1 374 ? 24.91600  -19.40800 4.08200   1.000 30.33522  ? 374 TYR A CD1   1 
ATOM   2988 C  CD2   . TYR A 1 374 ? 26.55600  -20.97700 3.32700   1.000 18.01269  ? 374 TYR A CD2   1 
ATOM   2989 C  CE1   . TYR A 1 374 ? 24.00900  -20.44300 4.26400   1.000 22.74220  ? 374 TYR A CE1   1 
ATOM   2990 C  CE2   . TYR A 1 374 ? 25.65900  -22.01100 3.50300   1.000 18.50222  ? 374 TYR A CE2   1 
ATOM   2991 C  CZ    . TYR A 1 374 ? 24.38800  -21.74300 3.97000   1.000 21.12622  ? 374 TYR A CZ    1 
ATOM   2992 O  OH    . TYR A 1 374 ? 23.50000  -22.78600 4.15100   1.000 19.05492  ? 374 TYR A OH    1 
ATOM   2993 N  N     . PRO A 1 375 ? 27.08600  -15.40900 3.39000   1.000 26.16103  ? 375 PRO A N     1 
ATOM   2994 C  CA    . PRO A 1 375 ? 27.78200  -14.17000 3.76200   1.000 26.55845  ? 375 PRO A CA    1 
ATOM   2995 C  C     . PRO A 1 375 ? 29.10500  -14.42700 4.47400   1.000 40.19692  ? 375 PRO A C     1 
ATOM   2996 O  O     . PRO A 1 375 ? 29.43300  -15.54200 4.88800   1.000 28.26918  ? 375 PRO A O     1 
ATOM   2997 C  CB    . PRO A 1 375 ? 26.79000  -13.46500 4.69500   1.000 30.23257  ? 375 PRO A CB    1 
ATOM   2998 C  CG    . PRO A 1 375 ? 25.45900  -14.06800 4.38500   1.000 33.28294  ? 375 PRO A CG    1 
ATOM   2999 C  CD    . PRO A 1 375 ? 25.74800  -15.49000 4.00600   1.000 33.58824  ? 375 PRO A CD    1 
ATOM   3000 N  N     . LEU A 1 376 ? 29.84800  -13.32900 4.65500   1.000 31.10110  ? 376 LEU A N     1 
ATOM   3001 C  CA    . LEU A 1 376 ? 31.21900  -13.37400 5.16300   1.000 46.90036  ? 376 LEU A CA    1 
ATOM   3002 C  C     . LEU A 1 376 ? 31.32900  -14.11100 6.49700   1.000 36.84389  ? 376 LEU A C     1 
ATOM   3003 O  O     . LEU A 1 376 ? 32.23200  -14.93600 6.69000   1.000 40.02585  ? 376 LEU A O     1 
ATOM   3004 C  CB    . LEU A 1 376 ? 31.75000  -11.94600 5.30400   1.000 50.70871  ? 376 LEU A CB    1 
ATOM   3005 C  CG    . LEU A 1 376 ? 33.26300  -11.73200 5.30900   1.000 64.65775  ? 376 LEU A CG    1 
ATOM   3006 C  CD1   . LEU A 1 376 ? 33.88800  -12.28700 4.04500   1.000 47.03459  ? 376 LEU A CD1   1 
ATOM   3007 C  CD2   . LEU A 1 376 ? 33.58500  -10.24800 5.46700   1.000 44.97645  ? 376 LEU A CD2   1 
ATOM   3008 N  N     . TYR A 1 377 ? 30.43800  -13.81100 7.44300   1.000 26.52423  ? 377 TYR A N     1 
ATOM   3009 C  CA    . TYR A 1 377 ? 30.54800  -14.43100 8.76300   1.000 39.35735  ? 377 TYR A CA    1 
ATOM   3010 C  C     . TYR A 1 377 ? 29.40200  -15.39300 9.05100   1.000 39.02047  ? 377 TYR A C     1 
ATOM   3011 O  O     . TYR A 1 377 ? 28.72300  -15.26200 10.07000  1.000 97.04848  ? 377 TYR A O     1 
ATOM   3012 C  CB    . TYR A 1 377 ? 30.61700  -13.36800 9.86400   1.000 36.48069  ? 377 TYR A CB    1 
ATOM   3013 C  CG    . TYR A 1 377 ? 31.83800  -12.48800 9.78300   1.000 33.29873  ? 377 TYR A CG    1 
ATOM   3014 C  CD1   . TYR A 1 377 ? 33.10100  -12.98400 10.10800  1.000 30.99056  ? 377 TYR A CD1   1 
ATOM   3015 C  CD2   . TYR A 1 377 ? 31.73300  -11.16100 9.39300   1.000 31.17479  ? 377 TYR A CD2   1 
ATOM   3016 C  CE1   . TYR A 1 377 ? 34.21700  -12.18500 10.03500  1.000 32.59865  ? 377 TYR A CE1   1 
ATOM   3017 C  CE2   . TYR A 1 377 ? 32.85000  -10.35000 9.32000   1.000 29.34562  ? 377 TYR A CE2   1 
ATOM   3018 C  CZ    . TYR A 1 377 ? 34.09000  -10.87000 9.64000   1.000 27.92703  ? 377 TYR A CZ    1 
ATOM   3019 O  OH    . TYR A 1 377 ? 35.21300  -10.07700 9.57000   1.000 42.42088  ? 377 TYR A OH    1 
ATOM   3020 N  N     . SER A 1 378 ? 29.21700  -16.39200 8.19500   1.000 36.27277  ? 378 SER A N     1 
ATOM   3021 C  CA    . SER A 1 378 ? 28.07000  -17.28200 8.29300   1.000 27.05061  ? 378 SER A CA    1 
ATOM   3022 C  C     . SER A 1 378 ? 28.31200  -18.40100 9.29900   1.000 24.77402  ? 378 SER A C     1 
ATOM   3023 O  O     . SER A 1 378 ? 29.38200  -19.01500 9.32200   1.000 21.51837  ? 378 SER A O     1 
ATOM   3024 C  CB    . SER A 1 378 ? 27.76800  -17.88700 6.92500   1.000 25.39778  ? 378 SER A CB    1 
ATOM   3025 O  OG    . SER A 1 378 ? 26.76000  -18.86300 7.03700   1.000 29.12454  ? 378 SER A OG    1 
ATOM   3026 N  N     . LEU A 1 379 ? 27.29700  -18.66800 10.13200  1.000 22.16318  ? 379 LEU A N     1 
ATOM   3027 C  CA    . LEU A 1 379 ? 27.34000  -19.81800 11.03600  1.000 25.72414  ? 379 LEU A CA    1 
ATOM   3028 C  C     . LEU A 1 379 ? 27.28000  -21.13500 10.27400  1.000 23.31859  ? 379 LEU A C     1 
ATOM   3029 O  O     . LEU A 1 379 ? 27.75900  -22.16400 10.77300  1.000 20.63932  ? 379 LEU A O     1 
ATOM   3030 C  CB    . LEU A 1 379 ? 26.18500  -19.75500 12.03900  1.000 30.22468  ? 379 LEU A CB    1 
ATOM   3031 C  CG    . LEU A 1 379 ? 26.14500  -18.61200 13.05800  1.000 39.65212  ? 379 LEU A CG    1 
ATOM   3032 C  CD1   . LEU A 1 379 ? 24.94200  -18.78400 13.98300  1.000 37.67294  ? 379 LEU A CD1   1 
ATOM   3033 C  CD2   . LEU A 1 379 ? 27.43500  -18.54500 13.85500  1.000 30.36417  ? 379 LEU A CD2   1 
ATOM   3034 N  N     . ASN A 1 380 ? 26.64700  -21.13500 9.09800   1.000 17.17574  ? 380 ASN A N     1 
ATOM   3035 C  CA    . ASN A 1 380 ? 26.63900  -22.33000 8.26300   1.000 21.19465  ? 380 ASN A CA    1 
ATOM   3036 C  C     . ASN A 1 380 ? 28.05200  -22.67100 7.79700   1.000 17.48631  ? 380 ASN A C     1 
ATOM   3037 O  O     . ASN A 1 380 ? 28.43700  -23.84700 7.74100   1.000 16.75464  ? 380 ASN A O     1 
ATOM   3038 C  CB    . ASN A 1 380 ? 25.71700  -22.10800 7.06400   1.000 24.57926  ? 380 ASN A CB    1 
ATOM   3039 C  CG    . ASN A 1 380 ? 24.28800  -21.79900 7.47400   1.000 27.29011  ? 380 ASN A CG    1 
ATOM   3040 O  OD1   . ASN A 1 380 ? 23.92500  -20.64000 7.67100   1.000 32.39073  ? 380 ASN A OD1   1 
ATOM   3041 N  ND2   . ASN A 1 380 ? 23.46400  -22.83400 7.57200   1.000 18.41273  ? 380 ASN A ND2   1 
ATOM   3042 N  N     . VAL A 1 381 ? 28.84000  -21.65000 7.46400   1.000 25.26619  ? 381 VAL A N     1 
ATOM   3043 C  CA    . VAL A 1 381 ? 30.21500  -21.87600 7.03000   1.000 22.24477  ? 381 VAL A CA    1 
ATOM   3044 C  C     . VAL A 1 381 ? 31.08500  -22.29900 8.21100   1.000 27.36644  ? 381 VAL A C     1 
ATOM   3045 O  O     . VAL A 1 381 ? 31.84200  -23.27100 8.12400   1.000 18.31799  ? 381 VAL A O     1 
ATOM   3046 C  CB    . VAL A 1 381 ? 30.76300  -20.61700 6.33200   1.000 21.20781  ? 381 VAL A CB    1 
ATOM   3047 C  CG1   . VAL A 1 381 ? 32.22700  -20.79900 5.94800   1.000 24.66085  ? 381 VAL A CG1   1 
ATOM   3048 C  CG2   . VAL A 1 381 ? 29.92600  -20.29800 5.09100   1.000 31.42219  ? 381 VAL A CG2   1 
ATOM   3049 N  N     . ALA A 1 382 ? 30.99900  -21.57300 9.33000   1.000 24.25817  ? 382 ALA A N     1 
ATOM   3050 C  CA    . ALA A 1 382 ? 31.79500  -21.93200 10.50400  1.000 26.10839  ? 382 ALA A CA    1 
ATOM   3051 C  C     . ALA A 1 382 ? 31.53300  -23.37100 10.93100  1.000 25.46095  ? 382 ALA A C     1 
ATOM   3052 O  O     . ALA A 1 382 ? 32.47100  -24.14200 11.17700  1.000 21.20517  ? 382 ALA A O     1 
ATOM   3053 C  CB    . ALA A 1 382 ? 31.50100  -20.97300 11.65900  1.000 27.06904  ? 382 ALA A CB    1 
ATOM   3054 N  N     . SER A 1 383 ? 30.25700  -23.75700 11.01700  1.000 21.52363  ? 383 SER A N     1 
ATOM   3055 C  CA    . SER A 1 383 ? 29.93000  -25.10200 11.47800  1.000 26.00049  ? 383 SER A CA    1 
ATOM   3056 C  C     . SER A 1 383 ? 30.40600  -26.16800 10.50000  1.000 23.85023  ? 383 SER A C     1 
ATOM   3057 O  O     . SER A 1 383 ? 30.76500  -27.27000 10.92600  1.000 21.77103  ? 383 SER A O     1 
ATOM   3058 C  CB    . SER A 1 383 ? 28.42600  -25.23200 11.72800  1.000 26.67951  ? 383 SER A CB    1 
ATOM   3059 O  OG    . SER A 1 383 ? 27.69700  -24.95000 10.54800  1.000 36.42805  ? 383 SER A OG    1 
ATOM   3060 N  N     . MET A 1 384 ? 30.41100  -25.87400 9.19300   1.000 22.74220  ? 384 MET A N     1 
ATOM   3061 C  CA    . MET A 1 384 ? 30.97500  -26.83300 8.24300   1.000 24.78718  ? 384 MET A CA    1 
ATOM   3062 C  C     . MET A 1 384 ? 32.48500  -26.97300 8.43100   1.000 23.27121  ? 384 MET A C     1 
ATOM   3063 O  O     . MET A 1 384 ? 33.01700  -28.08700 8.37700   1.000 27.08483  ? 384 MET A O     1 
ATOM   3064 C  CB    . MET A 1 384 ? 30.64000  -26.43300 6.80300   1.000 24.76613  ? 384 MET A CB    1 
ATOM   3065 C  CG    . MET A 1 384 ? 31.01500  -27.48400 5.74800   1.000 27.49277  ? 384 MET A CG    1 
ATOM   3066 S  SD    . MET A 1 384 ? 30.33200  -29.15100 6.01200   1.000 28.53763  ? 384 MET A SD    1 
ATOM   3067 C  CE    . MET A 1 384 ? 28.56900  -28.83800 5.98700   1.000 27.24800  ? 384 MET A CE    1 
ATOM   3068 N  N     . TRP A 1 385 ? 33.20000  -25.85800 8.63900   1.000 21.98421  ? 385 TRP A N     1 
ATOM   3069 C  CA    . TRP A 1 385 ? 34.62100  -25.95800 8.98200   1.000 23.75548  ? 385 TRP A CA    1 
ATOM   3070 C  C     . TRP A 1 385 ? 34.81400  -26.78500 10.24400  1.000 22.35005  ? 385 TRP A C     1 
ATOM   3071 O  O     . TRP A 1 385 ? 35.76500  -27.57000 10.35200  1.000 22.67903  ? 385 TRP A O     1 
ATOM   3072 C  CB    . TRP A 1 385 ? 35.23700  -24.57100 9.18500   1.000 19.49444  ? 385 TRP A CB    1 
ATOM   3073 C  CG    . TRP A 1 385 ? 35.60100  -23.84400 7.91100   1.000 20.88145  ? 385 TRP A CG    1 
ATOM   3074 C  CD1   . TRP A 1 385 ? 35.13400  -22.62600 7.50400   1.000 21.29466  ? 385 TRP A CD1   1 
ATOM   3075 C  CD2   . TRP A 1 385 ? 36.51500  -24.28300 6.89900   1.000 20.09451  ? 385 TRP A CD2   1 
ATOM   3076 N  NE1   . TRP A 1 385 ? 35.69900  -22.28100 6.30000   1.000 20.66037  ? 385 TRP A NE1   1 
ATOM   3077 C  CE2   . TRP A 1 385 ? 36.54700  -23.28100 5.90500   1.000 22.15002  ? 385 TRP A CE2   1 
ATOM   3078 C  CE3   . TRP A 1 385 ? 37.31400  -25.42500 6.73700   1.000 22.03685  ? 385 TRP A CE3   1 
ATOM   3079 C  CZ2   . TRP A 1 385 ? 37.34700  -23.38400 4.76500   1.000 27.34802  ? 385 TRP A CZ2   1 
ATOM   3080 C  CZ3   . TRP A 1 385 ? 38.10600  -25.52700 5.60200   1.000 25.25040  ? 385 TRP A CZ3   1 
ATOM   3081 C  CH2   . TRP A 1 385 ? 38.11600  -24.51100 4.63100   1.000 27.17431  ? 385 TRP A CH2   1 
ATOM   3082 N  N     . LEU A 1 386 ? 33.91100  -26.62200 11.21100  1.000 26.10839  ? 386 LEU A N     1 
ATOM   3083 C  CA    . LEU A 1 386 ? 34.02400  -27.34900 12.46900  1.000 30.11677  ? 386 LEU A CA    1 
ATOM   3084 C  C     . LEU A 1 386 ? 33.79400  -28.84400 12.26500  1.000 25.36357  ? 386 LEU A C     1 
ATOM   3085 O  O     . LEU A 1 386 ? 34.54400  -29.67700 12.79100  1.000 26.11629  ? 386 LEU A O     1 
ATOM   3086 C  CB    . LEU A 1 386 ? 33.04000  -26.76900 13.48600  1.000 26.15050  ? 386 LEU A CB    1 
ATOM   3087 C  CG    . LEU A 1 386 ? 33.05400  -27.38600 14.87900  1.000 30.29311  ? 386 LEU A CG    1 
ATOM   3088 C  CD1   . LEU A 1 386 ? 34.47800  -27.47700 15.40300  1.000 30.32732  ? 386 LEU A CD1   1 
ATOM   3089 C  CD2   . LEU A 1 386 ? 32.21900  -26.50700 15.77600  1.000 34.40939  ? 386 LEU A CD2   1 
ATOM   3090 N  N     . LYS A 1 387 ? 32.74900  -29.21100 11.51500  1.000 24.53452  ? 387 LYS A N     1 
ATOM   3091 C  CA    . LYS A 1 387 ? 32.53700  -30.62400 11.21400  1.000 23.62389  ? 387 LYS A CA    1 
ATOM   3092 C  C     . LYS A 1 387 ? 33.74000  -31.23400 10.50700  1.000 22.36058  ? 387 LYS A C     1 
ATOM   3093 O  O     . LYS A 1 387 ? 34.20300  -32.31800 10.88000  1.000 23.99761  ? 387 LYS A O     1 
ATOM   3094 C  CB    . LYS A 1 387 ? 31.27600  -30.81100 10.38000  1.000 28.99295  ? 387 LYS A CB    1 
ATOM   3095 C  CG    . LYS A 1 387 ? 30.01700  -30.67800 11.18900  1.000 30.36154  ? 387 LYS A CG    1 
ATOM   3096 C  CD    . LYS A 1 387 ? 28.82000  -30.84400 10.30100  1.000 38.40460  ? 387 LYS A CD    1 
ATOM   3097 C  CE    . LYS A 1 387 ? 27.57700  -30.35000 10.98500  1.000 48.42949  ? 387 LYS A CE    1 
ATOM   3098 N  NZ    . LYS A 1 387 ? 26.41700  -30.47900 10.06900  1.000 52.73264  ? 387 LYS A NZ    1 
ATOM   3099 N  N     . LEU A 1 388 ? 34.25800  -30.55700 9.47800   1.000 18.91279  ? 388 LEU A N     1 
ATOM   3100 C  CA    . LEU A 1 388 ? 35.45300  -31.05200 8.79800   1.000 21.65260  ? 388 LEU A CA    1 
ATOM   3101 C  C     . LEU A 1 388 ? 36.59700  -31.26000 9.78300   1.000 21.68944  ? 388 LEU A C     1 
ATOM   3102 O  O     . LEU A 1 388 ? 37.20000  -32.34000 9.84000   1.000 24.28975  ? 388 LEU A O     1 
ATOM   3103 C  CB    . LEU A 1 388 ? 35.87900  -30.07000 7.70300   1.000 23.81338  ? 388 LEU A CB    1 
ATOM   3104 C  CG    . LEU A 1 388 ? 35.17700  -30.09700 6.34100   1.000 27.66121  ? 388 LEU A CG    1 
ATOM   3105 C  CD1   . LEU A 1 388 ? 35.66400  -28.93400 5.47500   1.000 26.90059  ? 388 LEU A CD1   1 
ATOM   3106 C  CD2   . LEU A 1 388 ? 35.40600  -31.41500 5.62700   1.000 27.89808  ? 388 LEU A CD2   1 
ATOM   3107 N  N     . GLY A 1 389 ? 36.89400  -30.23200 10.58500  1.000 22.25530  ? 389 GLY A N     1 
ATOM   3108 C  CA    . GLY A 1 389 ? 38.00200  -30.32800 11.52500  1.000 25.85836  ? 389 GLY A CA    1 
ATOM   3109 C  C     . GLY A 1 389 ? 37.86400  -31.49200 12.48600  1.000 22.18950  ? 389 GLY A C     1 
ATOM   3110 O  O     . GLY A 1 389 ? 38.84200  -32.17900 12.79000  1.000 27.50856  ? 389 GLY A O     1 
ATOM   3111 N  N     . ARG A 1 390 ? 36.65000  -31.72200 12.98800  1.000 21.22360  ? 390 ARG A N     1 
ATOM   3112 C  CA    . ARG A 1 390 ? 36.44000  -32.83200 13.91200  1.000 24.55558  ? 390 ARG A CA    1 
ATOM   3113 C  C     . ARG A 1 390 ? 36.55900  -34.17300 13.20300  1.000 23.69495  ? 390 ARG A C     1 
ATOM   3114 O  O     . ARG A 1 390 ? 37.10200  -35.13200 13.76400  1.000 26.36632  ? 390 ARG A O     1 
ATOM   3115 C  CB    . ARG A 1 390 ? 35.08500  -32.68400 14.60000  1.000 27.41908  ? 390 ARG A CB    1 
ATOM   3116 C  CG    . ARG A 1 390 ? 35.12900  -31.64400 15.70700  1.000 28.72976  ? 390 ARG A CG    1 
ATOM   3117 C  CD    . ARG A 1 390 ? 33.77400  -31.42100 16.34300  1.000 33.26978  ? 390 ARG A CD    1 
ATOM   3118 N  NE    . ARG A 1 390 ? 33.88400  -30.55900 17.51800  1.000 36.64913  ? 390 ARG A NE    1 
ATOM   3119 C  CZ    . ARG A 1 390 ? 32.85400  -29.93500 18.07500  1.000 33.28820  ? 390 ARG A CZ    1 
ATOM   3120 N  NH1   . ARG A 1 390 ? 31.63700  -30.06800 17.55400  1.000 32.69603  ? 390 ARG A NH1   1 
ATOM   3121 N  NH2   . ARG A 1 390 ? 33.04100  -29.17000 19.14000  1.000 48.20052  ? 390 ARG A NH2   1 
ATOM   3122 N  N     . LEU A 1 391 ? 36.06300  -34.26000 11.96900  1.000 23.62125  ? 391 LEU A N     1 
ATOM   3123 C  CA    . LEU A 1 391 ? 36.26400  -35.47300 11.18300  1.000 24.57663  ? 391 LEU A CA    1 
ATOM   3124 C  C     . LEU A 1 391 ? 37.75100  -35.73400 10.95700  1.000 22.87643  ? 391 LEU A C     1 
ATOM   3125 O  O     . LEU A 1 391 ? 38.23400  -36.85200 11.16500  1.000 23.45018  ? 391 LEU A O     1 
ATOM   3126 C  CB    . LEU A 1 391 ? 35.51300  -35.36300 9.85100   1.000 27.27959  ? 391 LEU A CB    1 
ATOM   3127 C  CG    . LEU A 1 391 ? 33.98500  -35.46300 9.95400   1.000 27.86913  ? 391 LEU A CG    1 
ATOM   3128 C  CD1   . LEU A 1 391 ? 33.29500  -34.96900 8.68400   1.000 27.00061  ? 391 LEU A CD1   1 
ATOM   3129 C  CD2   . LEU A 1 391 ? 33.55900  -36.89000 10.26700  1.000 30.21415  ? 391 LEU A CD2   1 
ATOM   3130 N  N     . TYR A 1 392 ? 38.49500  -34.70400 10.53500  1.000 23.86339  ? 392 TYR A N     1 
ATOM   3131 C  CA    . TYR A 1 392 ? 39.93600  -34.84600 10.33100  1.000 25.25566  ? 392 TYR A CA    1 
ATOM   3132 C  C     . TYR A 1 392 ? 40.62800  -35.34500 11.59200  1.000 27.86387  ? 392 TYR A C     1 
ATOM   3133 O  O     . TYR A 1 392 ? 41.41600  -36.29700 11.54600  1.000 28.19022  ? 392 TYR A O     1 
ATOM   3134 C  CB    . TYR A 1 392 ? 40.54800  -33.51000 9.90600   1.000 25.80309  ? 392 TYR A CB    1 
ATOM   3135 C  CG    . TYR A 1 392 ? 40.36500  -33.13500 8.45000   1.000 25.78993  ? 392 TYR A CG    1 
ATOM   3136 C  CD1   . TYR A 1 392 ? 40.65300  -34.03400 7.43100   1.000 26.48739  ? 392 TYR A CD1   1 
ATOM   3137 C  CD2   . TYR A 1 392 ? 39.91700  -31.86700 8.09900   1.000 26.02154  ? 392 TYR A CD2   1 
ATOM   3138 C  CE1   . TYR A 1 392 ? 40.49300  -33.67700 6.09900   1.000 25.31619  ? 392 TYR A CE1   1 
ATOM   3139 C  CE2   . TYR A 1 392 ? 39.75200  -31.50200 6.77400   1.000 27.57699  ? 392 TYR A CE2   1 
ATOM   3140 C  CZ    . TYR A 1 392 ? 40.04000  -32.41000 5.78100   1.000 27.01113  ? 392 TYR A CZ    1 
ATOM   3141 O  OH    . TYR A 1 392 ? 39.87300  -32.03900 4.46500   1.000 32.94606  ? 392 TYR A OH    1 
ATOM   3142 N  N     . MET A 1 393 ? 40.36500  -34.69200 12.72900  1.000 26.51371  ? 393 MET A N     1 
ATOM   3143 C  CA    . MET A 1 393 ? 41.00700  -35.09600 13.97900  1.000 29.43511  ? 393 MET A CA    1 
ATOM   3144 C  C     . MET A 1 393 ? 40.64800  -36.53000 14.33400  1.000 26.45580  ? 393 MET A C     1 
ATOM   3145 O  O     . MET A 1 393 ? 41.52100  -37.33400 14.68100  1.000 27.25853  ? 393 MET A O     1 
ATOM   3146 C  CB    . MET A 1 393 ? 40.59700  -34.15700 15.11800  1.000 29.40879  ? 393 MET A CB    1 
ATOM   3147 C  CG    . MET A 1 393 ? 41.09500  -32.72900 15.00000  1.000 29.45353  ? 393 MET A CG    1 
ATOM   3148 S  SD    . MET A 1 393 ? 42.89100  -32.62900 14.90900  1.000 35.97537  ? 393 MET A SD    1 
ATOM   3149 C  CE    . MET A 1 393 ? 43.12600  -30.88100 15.19700  1.000 48.92692  ? 393 MET A CE    1 
ATOM   3150 N  N     . GLY A 1 394 ? 39.36000  -36.87000 14.23300  1.000 33.50928  ? 394 GLY A N     1 
ATOM   3151 C  CA    . GLY A 1 394 ? 38.92800  -38.23100 14.51000  1.000 38.59410  ? 394 GLY A CA    1 
ATOM   3152 C  C     . GLY A 1 394 ? 39.62600  -39.26300 13.64500  1.000 38.49672  ? 394 GLY A C     1 
ATOM   3153 O  O     . GLY A 1 394 ? 39.88100  -40.38700 14.08800  1.000 35.65164  ? 394 GLY A O     1 
ATOM   3154 N  N     . LEU A 1 395 ? 39.93400  -38.90300 12.40100  1.000 30.97477  ? 395 LEU A N     1 
ATOM   3155 C  CA    . LEU A 1 395 ? 40.61400  -39.80700 11.48500  1.000 32.62496  ? 395 LEU A CA    1 
ATOM   3156 C  C     . LEU A 1 395 ? 42.12800  -39.68000 11.55500  1.000 33.95144  ? 395 LEU A C     1 
ATOM   3157 O  O     . LEU A 1 395 ? 42.82500  -40.31700 10.75700  1.000 32.45126  ? 395 LEU A O     1 
ATOM   3158 C  CB    . LEU A 1 395 ? 40.12700  -39.57300 10.05200  1.000 33.31978  ? 395 LEU A CB    1 
ATOM   3159 C  CG    . LEU A 1 395 ? 38.65200  -39.93400 9.85600   1.000 33.60929  ? 395 LEU A CG    1 
ATOM   3160 C  CD1   . LEU A 1 395 ? 38.09900  -39.39400 8.53900   1.000 38.25195  ? 395 LEU A CD1   1 
ATOM   3161 C  CD2   . LEU A 1 395 ? 38.45100  -41.44100 9.95300   1.000 34.98314  ? 395 LEU A CD2   1 
ATOM   3162 N  N     . GLU A 1 396 ? 42.64300  -38.89100 12.50300  1.000 37.34132  ? 396 GLU A N     1 
ATOM   3163 C  CA    . GLU A 1 396 ? 44.06900  -38.69200 12.75800  1.000 37.79664  ? 396 GLU A CA    1 
ATOM   3164 C  C     . GLU A 1 396 ? 44.75100  -37.85600 11.67900  1.000 36.97549  ? 396 GLU A C     1 
ATOM   3165 O  O     . GLU A 1 396 ? 45.96900  -37.96800 11.49100  1.000 34.41992  ? 396 GLU A O     1 
ATOM   3166 C  CB    . GLU A 1 396 ? 44.81100  -40.02700 12.92000  1.000 45.99499  ? 396 GLU A CB    1 
ATOM   3167 C  CG    . GLU A 1 396 ? 44.16900  -41.01600 13.89500  1.000 58.60966  ? 396 GLU A CG    1 
ATOM   3168 C  CD    . GLU A 1 396 ? 44.55400  -40.76600 15.34100  1.000 78.61995  ? 396 GLU A CD    1 
ATOM   3169 O  OE1   . GLU A 1 396 ? 44.40500  -39.61400 15.80800  1.000 63.14178  ? 396 GLU A OE1   1 
ATOM   3170 O  OE2   . GLU A 1 396 ? 45.01700  -41.72300 16.00300  1.000 64.90252  ? 396 GLU A OE2   1 
ATOM   3171 N  N     . HIS A 1 397 ? 43.98800  -37.03000 10.95700  1.000 27.21905  ? 397 HIS A N     1 
ATOM   3172 C  CA    . HIS A 1 397 ? 44.53700  -36.03600 10.03100  1.000 28.38498  ? 397 HIS A CA    1 
ATOM   3173 C  C     . HIS A 1 397 ? 44.74600  -34.74400 10.81600  1.000 25.44252  ? 397 HIS A C     1 
ATOM   3174 O  O     . HIS A 1 397 ? 43.97700  -33.78900 10.70900  1.000 28.83767  ? 397 HIS A O     1 
ATOM   3175 C  CB    . HIS A 1 397 ? 43.60300  -35.80500 8.84800   1.000 29.25088  ? 397 HIS A CB    1 
ATOM   3176 C  CG    . HIS A 1 397 ? 43.39600  -37.00400 7.97600   1.000 34.85944  ? 397 HIS A CG    1 
ATOM   3177 N  ND1   . HIS A 1 397 ? 43.04000  -36.89900 6.64900   1.000 47.25303  ? 397 HIS A ND1   1 
ATOM   3178 C  CD2   . HIS A 1 397 ? 43.46300  -38.32900 8.24400   1.000 41.88660  ? 397 HIS A CD2   1 
ATOM   3179 C  CE1   . HIS A 1 397 ? 42.91100  -38.10700 6.13300   1.000 35.93589  ? 397 HIS A CE1   1 
ATOM   3180 N  NE2   . HIS A 1 397 ? 43.15700  -38.99300 7.08100   1.000 40.16008  ? 397 HIS A NE2   1 
ATOM   3181 N  N     . LYS A 1 398 ? 45.79900  -34.73600 11.63700  1.000 29.68251  ? 398 LYS A N     1 
ATOM   3182 C  CA    . LYS A 1 398 ? 45.98200  -33.68400 12.63700  1.000 35.51215  ? 398 LYS A CA    1 
ATOM   3183 C  C     . LYS A 1 398 ? 46.18600  -32.31800 11.99200  1.000 29.62724  ? 398 LYS A C     1 
ATOM   3184 O  O     . LYS A 1 398 ? 45.60900  -31.31700 12.43300  1.000 29.02716  ? 398 LYS A O     1 
ATOM   3185 C  CB    . LYS A 1 398 ? 47.18900  -34.01700 13.51700  1.000 36.70703  ? 398 LYS A CB    1 
ATOM   3186 C  CG    . LYS A 1 398 ? 47.20100  -35.42000 14.09000  1.000 60.69149  ? 398 LYS A CG    1 
ATOM   3187 C  CD    . LYS A 1 398 ? 46.22700  -35.59100 15.23000  1.000 66.67115  ? 398 LYS A CD    1 
ATOM   3188 C  CE    . LYS A 1 398 ? 46.54100  -36.86400 16.00100  1.000 74.55894  ? 398 LYS A CE    1 
ATOM   3189 N  NZ    . LYS A 1 398 ? 47.92400  -36.84000 16.55800  1.000 82.83888  ? 398 LYS A NZ    1 
ATOM   3190 N  N     . ALA A 1 399 ? 47.02700  -32.25300 10.95400  1.000 29.00611  ? 399 ALA A N     1 
ATOM   3191 C  CA    . ALA A 1 399 ? 47.33700  -30.97100 10.32400  1.000 29.72725  ? 399 ALA A CA    1 
ATOM   3192 C  C     . ALA A 1 399 ? 46.10800  -30.37500 9.64900   1.000 24.61348  ? 399 ALA A C     1 
ATOM   3193 O  O     . ALA A 1 399 ? 45.83000  -29.17900 9.79200   1.000 23.28437  ? 399 ALA A O     1 
ATOM   3194 C  CB    . ALA A 1 399 ? 48.48400  -31.13500 9.33000   1.000 32.29861  ? 399 ALA A CB    1 
ATOM   3195 N  N     . ALA A 1 400 ? 45.38100  -31.18200 8.87300   1.000 29.01401  ? 400 ALA A N     1 
ATOM   3196 C  CA    . ALA A 1 400 ? 44.15700  -30.68600 8.25000   1.000 26.18209  ? 400 ALA A CA    1 
ATOM   3197 C  C     . ALA A 1 400 ? 43.09000  -30.37900 9.29500   1.000 24.69770  ? 400 ALA A C     1 
ATOM   3198 O  O     . ALA A 1 400 ? 42.29800  -29.44500 9.12600   1.000 23.81601  ? 400 ALA A O     1 
ATOM   3199 C  CB    . ALA A 1 400 ? 43.63300  -31.70000 7.22700   1.000 27.17957  ? 400 ALA A CB    1 
ATOM   3200 N  N     . GLY A 1 401 ? 43.03700  -31.16800 10.37100  1.000 27.57436  ? 401 GLY A N     1 
ATOM   3201 C  CA    . GLY A 1 401 ? 42.09100  -30.88400 11.44100  1.000 30.26679  ? 401 GLY A CA    1 
ATOM   3202 C  C     . GLY A 1 401 ? 42.33200  -29.53500 12.08300  1.000 27.19273  ? 401 GLY A C     1 
ATOM   3203 O  O     . GLY A 1 401 ? 41.40700  -28.73600 12.25000  1.000 29.36931  ? 401 GLY A O     1 
ATOM   3204 N  N     . GLU A 1 402 ? 43.58600  -29.26500 12.44900  1.000 24.08973  ? 402 GLU A N     1 
ATOM   3205 C  CA    . GLU A 1 402 ? 43.94300  -27.98100 13.04600  1.000 27.24274  ? 402 GLU A CA    1 
ATOM   3206 C  C     . GLU A 1 402 ? 43.57600  -26.81900 12.13100  1.000 25.87942  ? 402 GLU A C     1 
ATOM   3207 O  O     . GLU A 1 402 ? 43.01600  -25.81000 12.57900  1.000 25.42147  ? 402 GLU A O     1 
ATOM   3208 C  CB    . GLU A 1 402 ? 45.43600  -27.95800 13.36400  1.000 34.14357  ? 402 GLU A CB    1 
ATOM   3209 C  CG    . GLU A 1 402 ? 45.86700  -26.76000 14.18100  1.000 51.40090  ? 402 GLU A CG    1 
ATOM   3210 C  CD    . GLU A 1 402 ? 47.33400  -26.81800 14.56900  1.000 54.47495  ? 402 GLU A CD    1 
ATOM   3211 O  OE1   . GLU A 1 402 ? 47.89400  -27.93700 14.62300  1.000 53.72223  ? 402 GLU A OE1   1 
ATOM   3212 O  OE2   . GLU A 1 402 ? 47.92100  -25.74100 14.81700  1.000 61.32051  ? 402 GLU A OE2   1 
ATOM   3213 N  N     . LYS A 1 403 ? 43.90500  -26.93600 10.84100  1.000 30.41944  ? 403 LYS A N     1 
ATOM   3214 C  CA    . LYS A 1 403 ? 43.57700  -25.88400 9.88000   1.000 30.52998  ? 403 LYS A CA    1 
ATOM   3215 C  C     . LYS A 1 403 ? 42.07700  -25.61000 9.84800   1.000 23.64231  ? 403 LYS A C     1 
ATOM   3216 O  O     . LYS A 1 403 ? 41.64100  -24.45500 9.90200   1.000 24.66085  ? 403 LYS A O     1 
ATOM   3217 C  CB    . LYS A 1 403 ? 44.08200  -26.28200 8.49200   1.000 36.68335  ? 403 LYS A CB    1 
ATOM   3218 C  CG    . LYS A 1 403 ? 45.56400  -26.00500 8.27400   1.000 60.14669  ? 403 LYS A CG    1 
ATOM   3219 C  CD    . LYS A 1 403 ? 46.06200  -26.61100 6.96700   1.000 94.46133  ? 403 LYS A CD    1 
ATOM   3220 C  CE    . LYS A 1 403 ? 47.57600  -26.80500 6.98500   1.000 82.45199  ? 403 LYS A CE    1 
ATOM   3221 N  NZ    . LYS A 1 403 ? 48.03400  -27.77600 5.94800   1.000 76.28020  ? 403 LYS A NZ    1 
ATOM   3222 N  N     . ALA A 1 404 ? 41.26800  -26.66100 9.74100   1.000 26.65320  ? 404 ALA A N     1 
ATOM   3223 C  CA    . ALA A 1 404 ? 39.82300  -26.46800 9.66700   1.000 25.42147  ? 404 ALA A CA    1 
ATOM   3224 C  C     . ALA A 1 404 ? 39.26500  -25.90700 10.97200  1.000 23.07382  ? 404 ALA A C     1 
ATOM   3225 O  O     . ALA A 1 404 ? 38.38600  -25.03600 10.95400  1.000 22.66851  ? 404 ALA A O     1 
ATOM   3226 C  CB    . ALA A 1 404 ? 39.14000  -27.78400 9.30600   1.000 27.17957  ? 404 ALA A CB    1 
ATOM   3227 N  N     . LEU A 1 405 ? 39.74200  -26.40400 12.11400  1.000 22.42374  ? 405 LEU A N     1 
ATOM   3228 C  CA    . LEU A 1 405 ? 39.24700  -25.90200 13.39200  1.000 25.36883  ? 405 LEU A CA    1 
ATOM   3229 C  C     . LEU A 1 405 ? 39.54700  -24.41700 13.56000  1.000 24.25028  ? 405 LEU A C     1 
ATOM   3230 O  O     . LEU A 1 405 ? 38.70100  -23.65700 14.04700  1.000 26.33474  ? 405 LEU A O     1 
ATOM   3231 C  CB    . LEU A 1 405 ? 39.85200  -26.70600 14.54500  1.000 24.04499  ? 405 LEU A CB    1 
ATOM   3232 C  CG    . LEU A 1 405 ? 39.42400  -28.17800 14.59700  1.000 25.90574  ? 405 LEU A CG    1 
ATOM   3233 C  CD1   . LEU A 1 405 ? 40.10600  -28.91000 15.74200  1.000 30.15625  ? 405 LEU A CD1   1 
ATOM   3234 C  CD2   . LEU A 1 405 ? 37.90600  -28.32400 14.67900  1.000 28.34550  ? 405 LEU A CD2   1 
ATOM   3235 N  N     . LYS A 1 406 ? 40.74100  -23.98000 13.14200  1.000 31.16426  ? 406 LYS A N     1 
ATOM   3236 C  CA    . LYS A 1 406 ? 41.09600  -22.56600 13.24600  1.000 27.57699  ? 406 LYS A CA    1 
ATOM   3237 C  C     . LYS A 1 406 ? 40.22900  -21.70300 12.33600  1.000 30.81948  ? 406 LYS A C     1 
ATOM   3238 O  O     . LYS A 1 406 ? 39.87500  -20.57200 12.69400  1.000 24.14237  ? 406 LYS A O     1 
ATOM   3239 C  CB    . LYS A 1 406 ? 42.57600  -22.37200 12.91900  1.000 32.71445  ? 406 LYS A CB    1 
ATOM   3240 C  CG    . LYS A 1 406 ? 43.51300  -22.83800 14.01700  1.000 34.35675  ? 406 LYS A CG    1 
ATOM   3241 C  CD    . LYS A 1 406 ? 44.96900  -22.66000 13.62200  1.000 45.35281  ? 406 LYS A CD    1 
ATOM   3242 C  CE    . LYS A 1 406 ? 45.90300  -23.16900 14.71100  1.000 63.50761  ? 406 LYS A CE    1 
ATOM   3243 N  NZ    . LYS A 1 406 ? 45.66100  -22.51200 16.02900  1.000 59.05708  ? 406 LYS A NZ    1 
ATOM   3244 N  N     . LYS A 1 407 ? 39.88500  -22.21200 11.14900  1.000 27.42697  ? 407 LYS A N     1 
ATOM   3245 C  CA    . LYS A 1 407 ? 38.97600  -21.48300 10.27200  1.000 29.09823  ? 407 LYS A CA    1 
ATOM   3246 C  C     . LYS A 1 407 ? 37.61700  -21.29100 10.93600  1.000 29.67198  ? 407 LYS A C     1 
ATOM   3247 O  O     . LYS A 1 407 ? 37.00100  -20.22300 10.82100  1.000 28.21391  ? 407 LYS A O     1 
ATOM   3248 C  CB    . LYS A 1 407 ? 38.83600  -22.22200 8.94200   1.000 41.62341  ? 407 LYS A CB    1 
ATOM   3249 C  CG    . LYS A 1 407 ? 40.06700  -22.10900 8.06000   1.000 39.88636  ? 407 LYS A CG    1 
ATOM   3250 C  CD    . LYS A 1 407 ? 40.15500  -20.73400 7.41100   1.000 71.95863  ? 407 LYS A CD    1 
ATOM   3251 C  CE    . LYS A 1 407 ? 41.07900  -20.73500 6.19200   1.000 62.26010  ? 407 LYS A CE    1 
ATOM   3252 N  NZ    . LYS A 1 407 ? 40.91000  -21.92800 5.31400   1.000 78.74628  ? 407 LYS A NZ    1 
ATOM   3253 N  N     . ALA A 1 408 ? 37.13100  -22.32000 11.63200  1.000 29.22719  ? 408 ALA A N     1 
ATOM   3254 C  CA    . ALA A 1 408 ? 35.87600  -22.19600 12.36500  1.000 28.03757  ? 408 ALA A CA    1 
ATOM   3255 C  C     . ALA A 1 408 ? 35.99700  -21.17800 13.49200  1.000 27.90335  ? 408 ALA A C     1 
ATOM   3256 O  O     . ALA A 1 408 ? 35.09400  -20.35900 13.70100  1.000 31.61958  ? 408 ALA A O     1 
ATOM   3257 C  CB    . ALA A 1 408 ? 35.45600  -23.55900 12.91500  1.000 27.60857  ? 408 ALA A CB    1 
ATOM   3258 N  N     . ILE A 1 409 ? 37.10300  -21.22500 14.24100  1.000 28.71660  ? 409 ILE A N     1 
ATOM   3259 C  CA    . ILE A 1 409 ? 37.29100  -20.29800 15.35700  1.000 26.99534  ? 409 ILE A CA    1 
ATOM   3260 C  C     . ILE A 1 409 ? 37.29800  -18.85500 14.86800  1.000 25.41884  ? 409 ILE A C     1 
ATOM   3261 O  O     . ILE A 1 409 ? 36.70200  -17.96800 15.49300  1.000 27.78228  ? 409 ILE A O     1 
ATOM   3262 C  CB    . ILE A 1 409 ? 38.57800  -20.64400 16.12800  1.000 26.40843  ? 409 ILE A CB    1 
ATOM   3263 C  CG1   . ILE A 1 409 ? 38.39100  -21.94100 16.91300  1.000 26.76900  ? 409 ILE A CG1   1 
ATOM   3264 C  CG2   . ILE A 1 409 ? 38.95700  -19.51000 17.07700  1.000 27.70332  ? 409 ILE A CG2   1 
ATOM   3265 C  CD1   . ILE A 1 409 ? 39.67800  -22.46000 17.54900  1.000 35.20159  ? 409 ILE A CD1   1 
ATOM   3266 N  N     . ALA A 1 410 ? 37.97200  -18.59500 13.74400  1.000 33.68562  ? 410 ALA A N     1 
ATOM   3267 C  CA    . ALA A 1 410 ? 38.08200  -17.22600 13.24300  1.000 32.58022  ? 410 ALA A CA    1 
ATOM   3268 C  C     . ALA A 1 410 ? 36.71100  -16.60300 13.00100  1.000 31.07741  ? 410 ALA A C     1 
ATOM   3269 O  O     . ALA A 1 410 ? 36.52400  -15.40000 13.22500  1.000 33.28820  ? 410 ALA A O     1 
ATOM   3270 C  CB    . ALA A 1 410 ? 38.92100  -17.19500 11.96700  1.000 29.16402  ? 410 ALA A CB    1 
ATOM   3271 N  N     . ILE A 1 411 ? 35.74600  -17.39500 12.52300  1.000 26.68215  ? 411 ILE A N     1 
ATOM   3272 C  CA    . ILE A 1 411 ? 34.39200  -16.88200 12.31200  1.000 23.31595  ? 411 ILE A CA    1 
ATOM   3273 C  C     . ILE A 1 411 ? 33.62600  -16.79100 13.62500  1.000 23.66073  ? 411 ILE A C     1 
ATOM   3274 O  O     . ILE A 1 411 ? 32.94000  -15.79700 13.89000  1.000 28.47183  ? 411 ILE A O     1 
ATOM   3275 C  CB    . ILE A 1 411 ? 33.63000  -17.75200 11.29700  1.000 25.50043  ? 411 ILE A CB    1 
ATOM   3276 C  CG1   . ILE A 1 411 ? 34.32600  -17.74500 9.93700   1.000 29.43774  ? 411 ILE A CG1   1 
ATOM   3277 C  CG2   . ILE A 1 411 ? 32.20500  -17.25300 11.15900  1.000 24.96878  ? 411 ILE A CG2   1 
ATOM   3278 C  CD1   . ILE A 1 411 ? 33.77600  -18.78700 8.98000   1.000 32.70918  ? 411 ILE A CD1   1 
ATOM   3279 N  N     . MET A 1 412 ? 33.72000  -17.82300 14.46500  1.000 26.27683  ? 412 MET A N     1 
ATOM   3280 C  CA    . MET A 1 412 ? 32.92300  -17.85700 15.68800  1.000 31.86435  ? 412 MET A CA    1 
ATOM   3281 C  C     . MET A 1 412 ? 33.31900  -16.74700 16.66100  1.000 25.21355  ? 412 MET A C     1 
ATOM   3282 O  O     . MET A 1 412 ? 32.46100  -16.23100 17.38200  1.000 35.80166  ? 412 MET A O     1 
ATOM   3283 C  CB    . MET A 1 412 ? 33.04900  -19.23200 16.34200  1.000 29.91938  ? 412 MET A CB    1 
ATOM   3284 C  CG    . MET A 1 412 ? 32.41600  -20.35700 15.51400  1.000 38.02035  ? 412 MET A CG    1 
ATOM   3285 S  SD    . MET A 1 412 ? 32.71900  -22.01300 16.17600  1.000 37.24657  ? 412 MET A SD    1 
ATOM   3286 C  CE    . MET A 1 412 ? 31.61100  -22.02300 17.58500  1.000 34.52256  ? 412 MET A CE    1 
ATOM   3287 N  N     . GLU A 1 413 ? 34.59700  -16.35700 16.68200  1.000 27.95862  ? 413 GLU A N     1 
ATOM   3288 C  CA    . GLU A 1 413 ? 35.03200  -15.24200 17.52300  1.000 30.57472  ? 413 GLU A CA    1 
ATOM   3289 C  C     . GLU A 1 413 ? 34.23200  -13.97900 17.23100  1.000 34.41728  ? 413 GLU A C     1 
ATOM   3290 O  O     . GLU A 1 413 ? 33.93600  -13.19700 18.14100  1.000 36.76493  ? 413 GLU A O     1 
ATOM   3291 C  CB    . GLU A 1 413 ? 36.52500  -14.98400 17.32000  1.000 30.55366  ? 413 GLU A CB    1 
ATOM   3292 C  CG    . GLU A 1 413 ? 37.41900  -15.95200 18.06800  1.000 35.39372  ? 413 GLU A CG    1 
ATOM   3293 C  CD    . GLU A 1 413 ? 38.90200  -15.70300 17.83600  1.000 51.09823  ? 413 GLU A CD    1 
ATOM   3294 O  OE1   . GLU A 1 413 ? 39.26100  -15.15400 16.77100  1.000 45.31859  ? 413 GLU A OE1   1 
ATOM   3295 O  OE2   . GLU A 1 413 ? 39.71000  -16.05000 18.72800  1.000 50.98769  ? 413 GLU A OE2   1 
ATOM   3296 N  N     . VAL A 1 414 ? 33.87900  -13.76200 15.96300  1.000 24.27396  ? 414 VAL A N     1 
ATOM   3297 C  CA    . VAL A 1 414 ? 33.06200  -12.61400 15.59300  1.000 24.29239  ? 414 VAL A CA    1 
ATOM   3298 C  C     . VAL A 1 414 ? 31.61900  -12.81900 16.04100  1.000 23.18436  ? 414 VAL A C     1 
ATOM   3299 O  O     . VAL A 1 414 ? 31.02800  -11.95000 16.69500  1.000 25.37146  ? 414 VAL A O     1 
ATOM   3300 C  CB    . VAL A 1 414 ? 33.15300  -12.37200 14.07400  1.000 26.22946  ? 414 VAL A CB    1 
ATOM   3301 C  CG1   . VAL A 1 414 ? 32.14500  -11.31900 13.63600  1.000 29.59039  ? 414 VAL A CG1   1 
ATOM   3302 C  CG2   . VAL A 1 414 ? 34.56700  -11.96500 13.69400  1.000 26.26631  ? 414 VAL A CG2   1 
ATOM   3303 N  N     . ALA A 1 415 ? 31.02200  -13.95700 15.66400  1.000 26.60056  ? 415 ALA A N     1 
ATOM   3304 C  CA    . ALA A 1 415 ? 29.60100  -14.21500 15.90400  1.000 25.36094  ? 415 ALA A CA    1 
ATOM   3305 C  C     . ALA A 1 415 ? 29.30200  -14.58700 17.35500  1.000 32.00910  ? 415 ALA A C     1 
ATOM   3306 O  O     . ALA A 1 415 ? 28.26600  -14.18400 17.90000  1.000 34.20410  ? 415 ALA A O     1 
ATOM   3307 C  CB    . ALA A 1 415 ? 29.11000  -15.32300 14.97400  1.000 31.40903  ? 415 ALA A CB    1 
ATOM   3308 N  N     . HIS A 1 416 ? 30.16800  -15.38500 17.98200  1.000 27.04535  ? 416 HIS A N     1 
ATOM   3309 C  CA    . HIS A 1 416 ? 29.92500  -15.88000 19.32900  1.000 25.84257  ? 416 HIS A CA    1 
ATOM   3310 C  C     . HIS A 1 416 ? 30.62200  -15.06300 20.40700  1.000 28.72186  ? 416 HIS A C     1 
ATOM   3311 O  O     . HIS A 1 416 ? 30.30200  -15.23100 21.58900  1.000 32.56443  ? 416 HIS A O     1 
ATOM   3312 C  CB    . HIS A 1 416 ? 30.37100  -17.34300 19.46200  1.000 26.61372  ? 416 HIS A CB    1 
ATOM   3313 C  CG    . HIS A 1 416 ? 29.50600  -18.32200 18.73100  1.000 28.87978  ? 416 HIS A CG    1 
ATOM   3314 N  ND1   . HIS A 1 416 ? 29.69400  -18.63700 17.40100  1.000 29.88253  ? 416 HIS A ND1   1 
ATOM   3315 C  CD2   . HIS A 1 416 ? 28.45200  -19.06500 19.14700  1.000 32.69076  ? 416 HIS A CD2   1 
ATOM   3316 C  CE1   . HIS A 1 416 ? 28.79600  -19.53200 17.02900  1.000 41.89713  ? 416 HIS A CE1   1 
ATOM   3317 N  NE2   . HIS A 1 416 ? 28.03200  -19.81100 18.07100  1.000 29.52722  ? 416 HIS A NE2   1 
ATOM   3318 N  N     . GLY A 1 417 ? 31.56800  -14.20500 20.03900  1.000 27.32959  ? 417 GLY A N     1 
ATOM   3319 C  CA    . GLY A 1 417 ? 32.39100  -13.52300 21.02100  1.000 30.52734  ? 417 GLY A CA    1 
ATOM   3320 C  C     . GLY A 1 417 ? 33.62100  -14.34300 21.35700  1.000 29.81673  ? 417 GLY A C     1 
ATOM   3321 O  O     . GLY A 1 417 ? 33.53500  -15.57100 21.43600  1.000 25.36883  ? 417 GLY A O     1 
ATOM   3322 N  N     . LYS A 1 418 ? 34.76400  -13.67400 21.56400  1.000 30.98003  ? 418 LYS A N     1 
ATOM   3323 C  CA    . LYS A 1 418 ? 36.03600  -14.37200 21.75900  1.000 35.11210  ? 418 LYS A CA    1 
ATOM   3324 C  C     . LYS A 1 418 ? 36.03000  -15.27600 22.98900  1.000 35.98326  ? 418 LYS A C     1 
ATOM   3325 O  O     . LYS A 1 418 ? 36.77500  -16.26300 23.03300  1.000 33.93565  ? 418 LYS A O     1 
ATOM   3326 C  CB    . LYS A 1 418 ? 37.17500  -13.35800 21.86700  1.000 42.01030  ? 418 LYS A CB    1 
ATOM   3327 C  CG    . LYS A 1 418 ? 37.47400  -12.62600 20.57600  1.000 55.35664  ? 418 LYS A CG    1 
ATOM   3328 C  CD    . LYS A 1 418 ? 38.46000  -11.49100 20.79000  1.000 60.30723  ? 418 LYS A CD    1 
ATOM   3329 C  CE    . LYS A 1 418 ? 38.60200  -10.64800 19.53100  1.000 74.20627  ? 418 LYS A CE    1 
ATOM   3330 N  NZ    . LYS A 1 418 ? 39.52400  -9.49400  19.73000  1.000 91.72679  ? 418 LYS A NZ    1 
ATOM   3331 N  N     . ASP A 1 419 ? 35.20600  -14.96000 23.98800  1.000 46.32661  ? 419 ASP A N     1 
ATOM   3332 C  CA    . ASP A 1 419 ? 35.18100  -15.65300 25.27100  1.000 45.95814  ? 419 ASP A CA    1 
ATOM   3333 C  C     . ASP A 1 419 ? 34.10500  -16.73800 25.35200  1.000 37.51502  ? 419 ASP A C     1 
ATOM   3334 O  O     . ASP A 1 419 ? 33.82600  -17.23900 26.44700  1.000 43.14465  ? 419 ASP A O     1 
ATOM   3335 C  CB    . ASP A 1 419 ? 34.97200  -14.63300 26.39500  1.000 54.16965  ? 419 ASP A CB    1 
ATOM   3336 C  CG    . ASP A 1 419 ? 33.72700  -13.76600 26.17900  1.000 71.13748  ? 419 ASP A CG    1 
ATOM   3337 O  OD1   . ASP A 1 419 ? 33.35200  -13.52300 25.00600  1.000 43.11306  ? 419 ASP A OD1   1 
ATOM   3338 O  OD2   . ASP A 1 419 ? 33.11600  -13.33200 27.18100  1.000 56.65153  ? 419 ASP A OD2   1 
ATOM   3339 N  N     . HIS A 1 420 ? 33.50300  -17.11400 24.22700  1.000 34.96998  ? 420 HIS A N     1 
ATOM   3340 C  CA    . HIS A 1 420 ? 32.40000  -18.06700 24.25500  1.000 36.89653  ? 420 HIS A CA    1 
ATOM   3341 C  C     . HIS A 1 420 ? 32.89600  -19.46000 24.64500  1.000 31.30112  ? 420 HIS A C     1 
ATOM   3342 O  O     . HIS A 1 420 ? 33.97700  -19.87800 24.21900  1.000 26.12682  ? 420 HIS A O     1 
ATOM   3343 C  CB    . HIS A 1 420 ? 31.70000  -18.12400 22.89600  1.000 32.70918  ? 420 HIS A CB    1 
ATOM   3344 C  CG    . HIS A 1 420 ? 30.34100  -18.74600 22.94800  1.000 30.87212  ? 420 HIS A CG    1 
ATOM   3345 N  ND1   . HIS A 1 420 ? 30.14800  -20.10800 23.01700  1.000 31.37745  ? 420 HIS A ND1   1 
ATOM   3346 C  CD2   . HIS A 1 420 ? 29.10500  -18.19000 22.95700  1.000 25.73203  ? 420 HIS A CD2   1 
ATOM   3347 C  CE1   . HIS A 1 420 ? 28.85300  -20.36600 23.05900  1.000 31.19848  ? 420 HIS A CE1   1 
ATOM   3348 N  NE2   . HIS A 1 420 ? 28.19900  -19.21900 23.02500  1.000 31.65906  ? 420 HIS A NE2   1 
ATOM   3349 N  N     . PRO A 1 421 ? 32.13700  -20.19300 25.46400  1.000 40.59434  ? 421 PRO A N     1 
ATOM   3350 C  CA    . PRO A 1 421 ? 32.52800  -21.57600 25.79100  1.000 42.73670  ? 421 PRO A CA    1 
ATOM   3351 C  C     . PRO A 1 421 ? 32.81800  -22.44800 24.57500  1.000 38.59936  ? 421 PRO A C     1 
ATOM   3352 O  O     . PRO A 1 421 ? 33.69300  -23.31900 24.65700  1.000 50.42710  ? 421 PRO A O     1 
ATOM   3353 C  CB    . PRO A 1 421 ? 31.31600  -22.09600 26.57600  1.000 43.83683  ? 421 PRO A CB    1 
ATOM   3354 C  CG    . PRO A 1 421 ? 30.72300  -20.88000 27.19500  1.000 40.19956  ? 421 PRO A CG    1 
ATOM   3355 C  CD    . PRO A 1 421 ? 30.93300  -19.76600 26.20100  1.000 35.24896  ? 421 PRO A CD    1 
ATOM   3356 N  N     . TYR A 1 422 ? 32.10900  -22.25300 23.45500  1.000 33.90933  ? 422 TYR A N     1 
ATOM   3357 C  CA    . TYR A 1 422 ? 32.36500  -23.06500 22.26600  1.000 31.73012  ? 422 TYR A CA    1 
ATOM   3358 C  C     . TYR A 1 422 ? 33.80000  -22.90500 21.77900  1.000 31.05109  ? 422 TYR A C     1 
ATOM   3359 O  O     . TYR A 1 422 ? 34.43300  -23.87600 21.34500  1.000 36.89653  ? 422 TYR A O     1 
ATOM   3360 C  CB    . TYR A 1 422 ? 31.38800  -22.70200 21.14500  1.000 31.06951  ? 422 TYR A CB    1 
ATOM   3361 C  CG    . TYR A 1 422 ? 29.98500  -23.22400 21.33900  1.000 30.15362  ? 422 TYR A CG    1 
ATOM   3362 C  CD1   . TYR A 1 422 ? 29.72100  -24.27300 22.21200  1.000 33.72510  ? 422 TYR A CD1   1 
ATOM   3363 C  CD2   . TYR A 1 422 ? 28.92100  -22.68000 20.63000  1.000 30.61946  ? 422 TYR A CD2   1 
ATOM   3364 C  CE1   . TYR A 1 422 ? 28.43000  -24.75400 22.38700  1.000 34.31201  ? 422 TYR A CE1   1 
ATOM   3365 C  CE2   . TYR A 1 422 ? 27.63100  -23.15100 20.79900  1.000 35.69375  ? 422 TYR A CE2   1 
ATOM   3366 C  CZ    . TYR A 1 422 ? 27.38900  -24.18700 21.67200  1.000 33.92249  ? 422 TYR A CZ    1 
ATOM   3367 O  OH    . TYR A 1 422 ? 26.09800  -24.65200 21.82100  1.000 30.47207  ? 422 TYR A OH    1 
ATOM   3368 N  N     . ILE A 1 423 ? 34.32700  -21.68300 21.83700  1.000 26.69267  ? 423 ILE A N     1 
ATOM   3369 C  CA    . ILE A 1 423 ? 35.67300  -21.42600 21.33500  1.000 29.75094  ? 423 ILE A CA    1 
ATOM   3370 C  C     . ILE A 1 423 ? 36.71800  -22.04500 22.25400  1.000 30.18520  ? 423 ILE A C     1 
ATOM   3371 O  O     . ILE A 1 423 ? 37.73600  -22.57900 21.79100  1.000 35.48057  ? 423 ILE A O     1 
ATOM   3372 C  CB    . ILE A 1 423 ? 35.87200  -19.91100 21.16000  1.000 33.09081  ? 423 ILE A CB    1 
ATOM   3373 C  CG1   . ILE A 1 423 ? 35.01600  -19.42300 19.98900  1.000 33.51718  ? 423 ILE A CG1   1 
ATOM   3374 C  CG2   . ILE A 1 423 ? 37.34400  -19.57700 20.96400  1.000 41.03124  ? 423 ILE A CG2   1 
ATOM   3375 C  CD1   . ILE A 1 423 ? 34.95200  -17.93800 19.85200  1.000 38.69674  ? 423 ILE A CD1   1 
ATOM   3376 N  N     . SER A 1 424 ? 36.48700  -21.98300 23.56600  1.000 35.49373  ? 424 SER A N     1 
ATOM   3377 C  CA    . SER A 1 424 ? 37.36300  -22.66900 24.51200  1.000 43.47627  ? 424 SER A CA    1 
ATOM   3378 C  C     . SER A 1 424 ? 37.38100  -24.17200 24.25300  1.000 34.23832  ? 424 SER A C     1 
ATOM   3379 O  O     . SER A 1 424 ? 38.44600  -24.80000 24.24600  1.000 34.31201  ? 424 SER A O     1 
ATOM   3380 C  CB    . SER A 1 424 ? 36.91200  -22.37500 25.94100  1.000 45.56862  ? 424 SER A CB    1 
ATOM   3381 O  OG    . SER A 1 424 ? 36.92700  -20.98300 26.19400  1.000 64.61564  ? 424 SER A OG    1 
ATOM   3382 N  N     . GLU A 1 425 ? 36.20000  -24.76500 24.04000  1.000 35.23317  ? 425 GLU A N     1 
ATOM   3383 C  CA    . GLU A 1 425 ? 36.12100  -26.19500 23.75600  1.000 44.38427  ? 425 GLU A CA    1 
ATOM   3384 C  C     . GLU A 1 425 ? 36.90200  -26.56000 22.49700  1.000 38.12826  ? 425 GLU A C     1 
ATOM   3385 O  O     . GLU A 1 425 ? 37.61000  -27.57400 22.47200  1.000 42.73670  ? 425 GLU A O     1 
ATOM   3386 C  CB    . GLU A 1 425 ? 34.65800  -26.62700 23.62800  1.000 48.99798  ? 425 GLU A CB    1 
ATOM   3387 C  CG    . GLU A 1 425 ? 34.45600  -28.13800 23.54100  1.000 71.75597  ? 425 GLU A CG    1 
ATOM   3388 C  CD    . GLU A 1 425 ? 32.98800  -28.53900 23.47400  1.000 84.21799  ? 425 GLU A CD    1 
ATOM   3389 O  OE1   . GLU A 1 425 ? 32.11800  -27.68200 23.75000  1.000 71.52437  ? 425 GLU A OE1   1 
ATOM   3390 O  OE2   . GLU A 1 425 ? 32.70400  -29.71200 23.14500  1.000 94.30078  ? 425 GLU A OE2   1 
ATOM   3391 N  N     . ILE A 1 426 ? 36.78200  -25.75200 21.43800  1.000 31.96173  ? 426 ILE A N     1 
ATOM   3392 C  CA    . ILE A 1 426 ? 37.41000  -26.10800 20.16800  1.000 31.78013  ? 426 ILE A CA    1 
ATOM   3393 C  C     . ILE A 1 426 ? 38.92700  -26.01500 20.27300  1.000 31.48009  ? 426 ILE A C     1 
ATOM   3394 O  O     . ILE A 1 426 ? 39.65400  -26.82300 19.68100  1.000 35.49899  ? 426 ILE A O     1 
ATOM   3395 C  CB    . ILE A 1 426 ? 36.86200  -25.23200 19.02500  1.000 33.38032  ? 426 ILE A CB    1 
ATOM   3396 C  CG1   . ILE A 1 426 ? 35.37300  -25.50300 18.81000  1.000 33.58034  ? 426 ILE A CG1   1 
ATOM   3397 C  CG2   . ILE A 1 426 ? 37.61200  -25.49700 17.72700  1.000 31.06688  ? 426 ILE A CG2   1 
ATOM   3398 C  CD1   . ILE A 1 426 ? 34.67600  -24.42900 18.02100  1.000 33.87775  ? 426 ILE A CD1   1 
ATOM   3399 N  N     . LYS A 1 427 ? 39.43000  -25.04200 21.03600  1.000 30.92476  ? 427 LYS A N     1 
ATOM   3400 C  CA    . LYS A 1 427 ? 40.87300  -24.94000 21.23600  1.000 36.17802  ? 427 LYS A CA    1 
ATOM   3401 C  C     . LYS A 1 427 ? 41.43800  -26.16100 21.95500  1.000 31.15110  ? 427 LYS A C     1 
ATOM   3402 O  O     . LYS A 1 427 ? 42.58200  -26.55400 21.69700  1.000 35.34108  ? 427 LYS A O     1 
ATOM   3403 C  CB    . LYS A 1 427 ? 41.20400  -23.66100 22.00000  1.000 36.92022  ? 427 LYS A CB    1 
ATOM   3404 C  CG    . LYS A 1 427 ? 41.12100  -22.41000 21.13900  1.000 42.54457  ? 427 LYS A CG    1 
ATOM   3405 C  CD    . LYS A 1 427 ? 41.50100  -21.17600 21.93800  1.000 46.53716  ? 427 LYS A CD    1 
ATOM   3406 C  CE    . LYS A 1 427 ? 41.18600  -19.90200 21.17900  1.000 48.90586  ? 427 LYS A CE    1 
ATOM   3407 N  NZ    . LYS A 1 427 ? 41.38800  -18.70400 22.03600  1.000 71.88230  ? 427 LYS A NZ    1 
ATOM   3408 N  N     . GLN A 1 428 ? 40.65800  -26.78300 22.84600  1.000 30.79843  ? 428 GLN A N     1 
ATOM   3409 C  CA    . GLN A 1 428 ? 41.11200  -28.02800 23.46400  1.000 36.50964  ? 428 GLN A CA    1 
ATOM   3410 C  C     . GLN A 1 428 ? 41.29400  -29.12300 22.42100  1.000 41.07861  ? 428 GLN A C     1 
ATOM   3411 O  O     . GLN A 1 428 ? 42.22900  -29.92600 22.50700  1.000 39.48631  ? 428 GLN A O     1 
ATOM   3412 C  CB    . GLN A 1 428 ? 40.12100  -28.49400 24.53100  1.000 38.36513  ? 428 GLN A CB    1 
ATOM   3413 C  CG    . GLN A 1 428 ? 39.89600  -27.50400 25.64500  1.000 46.02920  ? 428 GLN A CG    1 
ATOM   3414 C  CD    . GLN A 1 428 ? 41.18100  -26.86700 26.11700  1.000 49.82966  ? 428 GLN A CD    1 
ATOM   3415 O  OE1   . GLN A 1 428 ? 42.09000  -27.54900 26.59400  1.000 51.10876  ? 428 GLN A OE1   1 
ATOM   3416 N  NE2   . GLN A 1 428 ? 41.27100  -25.54700 25.97800  1.000 63.20495  ? 428 GLN A NE2   1 
ATOM   3417 N  N     . GLU A 1 429 ? 40.41200  -29.16600 21.42100  1.000 35.33318  ? 429 GLU A N     1 
ATOM   3418 C  CA    . GLU A 1 429 ? 40.48200  -30.21700 20.41700  1.000 36.23856  ? 429 GLU A CA    1 
ATOM   3419 C  C     . GLU A 1 429 ? 41.69000  -30.05300 19.50600  1.000 38.09141  ? 429 GLU A C     1 
ATOM   3420 O  O     . GLU A 1 429 ? 42.09800  -31.02100 18.85400  1.000 48.11103  ? 429 GLU A O     1 
ATOM   3421 C  CB    . GLU A 1 429 ? 39.19400  -30.23500 19.60300  1.000 34.74101  ? 429 GLU A CB    1 
ATOM   3422 C  CG    . GLU A 1 429 ? 37.96600  -30.49900 20.44600  1.000 37.44396  ? 429 GLU A CG    1 
ATOM   3423 C  CD    . GLU A 1 429 ? 36.67800  -30.42000 19.64200  1.000 46.63454  ? 429 GLU A CD    1 
ATOM   3424 O  OE1   . GLU A 1 429 ? 36.61800  -31.02700 18.55200  1.000 48.64004  ? 429 GLU A OE1   1 
ATOM   3425 O  OE2   . GLU A 1 429 ? 35.73100  -29.73900 20.09200  1.000 54.15649  ? 429 GLU A OE2   1 
ATOM   3426 N  N     . ILE A 1 430 ? 42.26500  -28.85000 19.44700  1.000 35.84904  ? 430 ILE A N     1 
ATOM   3427 C  CA    . ILE A 1 430 ? 43.49100  -28.63600 18.68400  1.000 40.88385  ? 430 ILE A CA    1 
ATOM   3428 C  C     . ILE A 1 430 ? 44.68900  -29.22400 19.42000  1.000 45.41071  ? 430 ILE A C     1 
ATOM   3429 O  O     . ILE A 1 430 ? 45.55000  -29.87100 18.81200  1.000 76.02227  ? 430 ILE A O     1 
ATOM   3430 C  CB    . ILE A 1 430 ? 43.67800  -27.13600 18.40200  1.000 37.85980  ? 430 ILE A CB    1 
ATOM   3431 C  CG1   . ILE A 1 430 ? 42.58700  -26.63800 17.45300  1.000 34.46729  ? 430 ILE A CG1   1 
ATOM   3432 C  CG2   . ILE A 1 430 ? 45.05700  -26.86700 17.82800  1.000 39.80740  ? 430 ILE A CG2   1 
ATOM   3433 C  CD1   . ILE A 1 430 ? 42.53500  -25.13100 17.32500  1.000 39.12574  ? 430 ILE A CD1   1 
ATOM   3434 N  N     . GLU A 1 431 ? 44.69200  -29.01000 20.73500  1.000 62.15219  ? 431 GLU A N     1 
ATOM   3435 C  CA    . GLU A 1 431 ? 45.77800  -29.48400 21.62500  1.000 78.29360  ? 431 GLU A CA    1 
ATOM   3436 C  C     . GLU A 1 431 ? 45.35500  -30.73100 22.40600  1.000 97.03005  ? 431 GLU A C     1 
ATOM   3437 O  O     . GLU A 1 431 ? 45.57500  -30.74700 23.60900  1.000 96.81424  ? 431 GLU A O     1 
ATOM   3438 C  CB    . GLU A 1 431 ? 46.25900  -28.40600 22.59800  1.000 80.72547  ? 431 GLU A CB    1 
ATOM   3439 C  CG    . GLU A 1 431 ? 45.39000  -27.18200 22.73500  1.000 58.74915  ? 431 GLU A CG    1 
ATOM   3440 C  CD    . GLU A 1 431 ? 45.98500  -25.93100 22.11700  1.000 82.60201  ? 431 GLU A CD    1 
ATOM   3441 O  OE1   . GLU A 1 431 ? 47.17900  -25.94600 21.81000  1.000 62.29168  ? 431 GLU A OE1   1 
ATOM   3442 O  OE2   . GLU A 1 431 ? 45.23800  -24.95200 21.92700  1.000 78.14884  ? 431 GLU A OE2   1 
ATOM   3443 N  N     . SER A 1 432 ? 44.72400  -31.70800 21.75000  1.000 111.71076 ? 432 SER A N     1 
ATOM   3444 C  CA    . SER A 1 432 ? 44.38100  -32.97200 22.38900  1.000 112.86616 ? 432 SER A CA    1 
ATOM   3445 C  C     . SER A 1 432 ? 44.91700  -34.10100 21.52400  1.000 144.55681 ? 432 SER A C     1 
ATOM   3446 O  O     . SER A 1 432 ? 45.63500  -34.98200 22.00600  1.000 163.32221 ? 432 SER A O     1 
ATOM   3447 C  CB    . SER A 1 432 ? 42.86900  -33.11000 22.58300  1.000 82.99153  ? 432 SER A CB    1 
ATOM   3448 O  OG    . SER A 1 432 ? 42.42800  -32.41600 23.73800  1.000 77.78038  ? 432 SER A OG    1 
ATOM   3449 N  N     . HIS A 1 433 ? 44.55300  -34.08500 20.24700  1.000 134.42401 ? 433 HIS A N     1 
ATOM   3450 C  CA    . HIS A 1 433 ? 45.12600  -35.00000 19.27200  1.000 137.77178 ? 433 HIS A CA    1 
ATOM   3451 C  C     . HIS A 1 433 ? 46.53400  -34.56300 18.86600  1.000 134.06607 ? 433 HIS A C     1 
ATOM   3452 O  O     . HIS A 1 433 ? 46.94300  -33.42700 19.11900  1.000 103.40714 ? 433 HIS A O     1 
ATOM   3453 C  CB    . HIS A 1 433 ? 44.22000  -35.10200 18.04500  1.000 128.63384 ? 433 HIS A CB    1 
ATOM   3454 C  CG    . HIS A 1 433 ? 42.93700  -35.82700 18.30100  1.000 118.38261 ? 433 HIS A CG    1 
ATOM   3455 N  ND1   . HIS A 1 433 ? 42.81200  -37.19100 18.14700  1.000 107.73660 ? 433 HIS A ND1   1 
ATOM   3456 C  CD2   . HIS A 1 433 ? 41.72400  -35.38100 18.70300  1.000 108.01558 ? 433 HIS A CD2   1 
ATOM   3457 C  CE1   . HIS A 1 433 ? 41.57700  -37.55400 18.44300  1.000 130.24983 ? 433 HIS A CE1   1 
ATOM   3458 N  NE2   . HIS A 1 433 ? 40.89600  -36.47400 18.78200  1.000 104.24934 ? 433 HIS A NE2   1 
ATOM   3459 N  N     . GLU B 1 4   ? -23.13000 26.08700  48.57300  1.000 105.68899 ? 4   GLU B N     1 
ATOM   3460 C  CA    . GLU B 1 4   ? -22.51900 24.73100  48.55400  1.000 104.58886 ? 4   GLU B CA    1 
ATOM   3461 C  C     . GLU B 1 4   ? -23.43100 23.75500  49.30700  1.000 123.99908 ? 4   GLU B C     1 
ATOM   3462 O  O     . GLU B 1 4   ? -24.65600 23.98900  49.32800  1.000 150.88125 ? 4   GLU B O     1 
ATOM   3463 C  CB    . GLU B 1 4   ? -21.12000 24.76800  49.17200  1.000 97.32746  ? 4   GLU B CB    1 
ATOM   3464 C  CG    . GLU B 1 4   ? -20.26700 25.91700  48.66700  1.000 89.25807  ? 4   GLU B CG    1 
ATOM   3465 C  CD    . GLU B 1 4   ? -19.56600 25.65300  47.34600  1.000 86.72882  ? 4   GLU B CD    1 
ATOM   3466 O  OE1   . GLU B 1 4   ? -18.53500 24.95200  47.35500  1.000 73.63251  ? 4   GLU B OE1   1 
ATOM   3467 O  OE2   . GLU B 1 4   ? -20.05200 26.15000  46.31100  1.000 89.97921  ? 4   GLU B OE2   1 
ATOM   3468 N  N     . GLY B 1 5   ? -22.84700 22.70800  49.89800  1.000 122.64628 ? 5   GLY B N     1 
ATOM   3469 C  CA    . GLY B 1 5   ? -23.60800 21.71800  50.63800  1.000 122.73840 ? 5   GLY B CA    1 
ATOM   3470 C  C     . GLY B 1 5   ? -22.98100 21.25000  51.93500  1.000 144.75946 ? 5   GLY B C     1 
ATOM   3471 O  O     . GLY B 1 5   ? -23.67800 20.74600  52.82000  1.000 111.15806 ? 5   GLY B O     1 
ATOM   3472 N  N     . LEU B 1 6   ? -21.67100 21.42900  52.07400  1.000 142.44339 ? 6   LEU B N     1 
ATOM   3473 C  CA    . LEU B 1 6   ? -20.93800 20.99200  53.25500  1.000 85.95504  ? 6   LEU B CA    1 
ATOM   3474 C  C     . LEU B 1 6   ? -20.40200 22.21000  53.99700  1.000 64.36561  ? 6   LEU B C     1 
ATOM   3475 O  O     . LEU B 1 6   ? -19.56900 22.95000  53.45900  1.000 51.28510  ? 6   LEU B O     1 
ATOM   3476 C  CB    . LEU B 1 6   ? -19.79700 20.05200  52.86400  1.000 72.89295  ? 6   LEU B CB    1 
ATOM   3477 C  CG    . LEU B 1 6   ? -20.25600 18.79200  52.13400  1.000 75.95121  ? 6   LEU B CG    1 
ATOM   3478 C  CD1   . LEU B 1 6   ? -19.07600 18.03800  51.52600  1.000 85.81029  ? 6   LEU B CD1   1 
ATOM   3479 C  CD2   . LEU B 1 6   ? -21.04200 17.91600  53.08600  1.000 73.17193  ? 6   LEU B CD2   1 
ATOM   3480 N  N     . GLY B 1 7   ? -20.86000 22.39900  55.22700  1.000 62.93649  ? 7   GLY B N     1 
ATOM   3481 C  CA    . GLY B 1 7   ? -20.43100 23.55600  55.99700  1.000 65.57102  ? 7   GLY B CA    1 
ATOM   3482 C  C     . GLY B 1 7   ? -18.93900 23.52800  56.28600  1.000 64.25244  ? 7   GLY B C     1 
ATOM   3483 O  O     . GLY B 1 7   ? -18.36100 22.48100  56.59100  1.000 55.81195  ? 7   GLY B O     1 
ATOM   3484 N  N     . GLY B 1 8   ? -18.31600 24.70200  56.20300  1.000 53.90120  ? 8   GLY B N     1 
ATOM   3485 C  CA    . GLY B 1 8   ? -16.90000 24.84100  56.47200  1.000 44.32900  ? 8   GLY B CA    1 
ATOM   3486 C  C     . GLY B 1 8   ? -15.98500 24.41100  55.34900  1.000 42.42614  ? 8   GLY B C     1 
ATOM   3487 O  O     . GLY B 1 8   ? -14.76600 24.39200  55.54200  1.000 37.33606  ? 8   GLY B O     1 
ATOM   3488 N  N     . LEU B 1 9   ? -16.53000 24.07800  54.18000  1.000 43.44995  ? 9   LEU B N     1 
ATOM   3489 C  CA    . LEU B 1 9   ? -15.75600 23.53600  53.07300  1.000 43.16044  ? 9   LEU B CA    1 
ATOM   3490 C  C     . LEU B 1 9   ? -16.28000 24.11900  51.77000  1.000 42.38666  ? 9   LEU B C     1 
ATOM   3491 O  O     . LEU B 1 9   ? -17.43500 24.53800  51.67500  1.000 46.94773  ? 9   LEU B O     1 
ATOM   3492 C  CB    . LEU B 1 9   ? -15.84500 22.00700  53.02000  1.000 43.96053  ? 9   LEU B CB    1 
ATOM   3493 C  CG    . LEU B 1 9   ? -15.41700 21.25000  54.27500  1.000 42.31297  ? 9   LEU B CG    1 
ATOM   3494 C  CD1   . LEU B 1 9   ? -15.92700 19.82800  54.22300  1.000 46.57927  ? 9   LEU B CD1   1 
ATOM   3495 C  CD2   . LEU B 1 9   ? -13.90200 21.28900  54.42700  1.000 36.95443  ? 9   LEU B CD2   1 
ATOM   3496 N  N     . GLU B 1 10  ? -15.42000 24.12500  50.75300  1.000 44.35269  ? 10  GLU B N     1 
ATOM   3497 C  CA    . GLU B 1 10  ? -15.83100 24.56900  49.43100  1.000 49.65859  ? 10  GLU B CA    1 
ATOM   3498 C  C     . GLU B 1 10  ? -15.02200 23.84300  48.36700  1.000 48.81901  ? 10  GLU B C     1 
ATOM   3499 O  O     . GLU B 1 10  ? -13.84200 23.53500  48.56000  1.000 43.96053  ? 10  GLU B O     1 
ATOM   3500 C  CB    . GLU B 1 10  ? -15.66800 26.08600  49.26300  1.000 60.30460  ? 10  GLU B CB    1 
ATOM   3501 C  CG    . GLU B 1 10  ? -14.22600 26.54200  49.10700  1.000 55.71984  ? 10  GLU B CG    1 
ATOM   3502 C  CD    . GLU B 1 10  ? -14.09800 28.03200  48.84600  1.000 63.18916  ? 10  GLU B CD    1 
ATOM   3503 O  OE1   . GLU B 1 10  ? -15.12900 28.69200  48.59300  1.000 66.18162  ? 10  GLU B OE1   1 
ATOM   3504 O  OE2   . GLU B 1 10  ? -12.95800 28.54300  48.88500  1.000 63.44182  ? 10  GLU B OE2   1 
ATOM   3505 N  N     . ARG B 1 11  ? -15.68600 23.56500  47.24600  1.000 41.53130  ? 11  ARG B N     1 
ATOM   3506 C  CA    . ARG B 1 11  ? -15.02200 23.10100  46.03600  1.000 44.04475  ? 11  ARG B CA    1 
ATOM   3507 C  C     . ARG B 1 11  ? -14.30500 24.26400  45.36000  1.000 48.77427  ? 11  ARG B C     1 
ATOM   3508 O  O     . ARG B 1 11  ? -14.82300 25.38200  45.30800  1.000 49.77176  ? 11  ARG B O     1 
ATOM   3509 C  CB    . ARG B 1 11  ? -16.05500 22.48400  45.09300  1.000 51.26930  ? 11  ARG B CB    1 
ATOM   3510 C  CG    . ARG B 1 11  ? -15.57600 22.15000  43.69500  1.000 55.44612  ? 11  ARG B CG    1 
ATOM   3511 C  CD    . ARG B 1 11  ? -16.64000 21.33000  42.97300  1.000 57.73061  ? 11  ARG B CD    1 
ATOM   3512 N  NE    . ARG B 1 11  ? -16.63400 21.54500  41.53000  1.000 75.84330  ? 11  ARG B NE    1 
ATOM   3513 C  CZ    . ARG B 1 11  ? -17.47200 20.95200  40.68400  1.000 95.92729  ? 11  ARG B CZ    1 
ATOM   3514 N  NH1   . ARG B 1 11  ? -18.38700 20.10400  41.13800  1.000 79.21213  ? 11  ARG B NH1   1 
ATOM   3515 N  NH2   . ARG B 1 11  ? -17.39600 21.20500  39.38300  1.000 114.25580 ? 11  ARG B NH2   1 
ATOM   3516 N  N     . PHE B 1 12  ? -13.11000 24.00000  44.83600  1.000 49.72701  ? 12  PHE B N     1 
ATOM   3517 C  CA    . PHE B 1 12  ? -12.32500 25.04800  44.19700  1.000 50.35604  ? 12  PHE B CA    1 
ATOM   3518 C  C     . PHE B 1 12  ? -11.43000 24.43300  43.13200  1.000 51.87201  ? 12  PHE B C     1 
ATOM   3519 O  O     . PHE B 1 12  ? -11.36000 23.21000  42.97700  1.000 51.95623  ? 12  PHE B O     1 
ATOM   3520 C  CB    . PHE B 1 12  ? -11.50100 25.83900  45.22600  1.000 45.37649  ? 12  PHE B CB    1 
ATOM   3521 C  CG    . PHE B 1 12  ? -10.22200 25.15900  45.64800  1.000 43.09990  ? 12  PHE B CG    1 
ATOM   3522 C  CD1   . PHE B 1 12  ? -10.24800 23.97600  46.36900  1.000 38.58621  ? 12  PHE B CD1   1 
ATOM   3523 C  CD2   . PHE B 1 12  ? -8.99000  25.71700  45.33400  1.000 47.50833  ? 12  PHE B CD2   1 
ATOM   3524 C  CE1   . PHE B 1 12  ? -9.07000  23.35600  46.76700  1.000 38.03088  ? 12  PHE B CE1   1 
ATOM   3525 C  CE2   . PHE B 1 12  ? -7.81000  25.10200  45.72400  1.000 45.92656  ? 12  PHE B CE2   1 
ATOM   3526 C  CZ    . PHE B 1 12  ? -7.85100  23.91900  46.44200  1.000 41.62078  ? 12  PHE B CZ    1 
ATOM   3527 N  N     . CYS B 1 13  ? -10.76400 25.30500  42.37500  1.000 48.60583  ? 13  CYS B N     1 
ATOM   3528 C  CA    . CYS B 1 13  ? -9.82600  24.89300  41.33400  1.000 52.27995  ? 13  CYS B CA    1 
ATOM   3529 C  C     . CYS B 1 13  ? -8.42300  24.83500  41.92700  1.000 46.61085  ? 13  CYS B C     1 
ATOM   3530 O  O     . CYS B 1 13  ? -7.80000  25.87100  42.17300  1.000 47.79257  ? 13  CYS B O     1 
ATOM   3531 C  CB    . CYS B 1 13  ? -9.88300  25.84500  40.14100  1.000 53.22217  ? 13  CYS B CB    1 
ATOM   3532 S  SG    . CYS B 1 13  ? -11.41300 25.71800  39.19000  1.000 72.02969  ? 13  CYS B SG    1 
ATOM   3533 N  N     . SER B 1 14  ? -7.92900  23.62100  42.15500  1.000 55.39612  ? 14  SER B N     1 
ATOM   3534 C  CA    . SER B 1 14  ? -6.59500  23.41900  42.70200  1.000 47.41358  ? 14  SER B CA    1 
ATOM   3535 C  C     . SER B 1 14  ? -5.57900  23.39200  41.56900  1.000 50.19812  ? 14  SER B C     1 
ATOM   3536 O  O     . SER B 1 14  ? -5.66300  22.51200  40.70100  1.000 49.85335  ? 14  SER B O     1 
ATOM   3537 C  CB    . SER B 1 14  ? -6.53200  22.12400  43.49600  1.000 44.02633  ? 14  SER B CB    1 
ATOM   3538 O  OG    . SER B 1 14  ? -5.23700  21.92600  44.03400  1.000 46.57137  ? 14  SER B OG    1 
ATOM   3539 N  N     . PRO B 1 15  ? -4.63300  24.33000  41.52200  1.000 50.37446  ? 15  PRO B N     1 
ATOM   3540 C  CA    . PRO B 1 15  ? -3.67400  24.36800  40.40900  1.000 55.02502  ? 15  PRO B CA    1 
ATOM   3541 C  C     . PRO B 1 15  ? -2.92900  23.05100  40.23900  1.000 48.65583  ? 15  PRO B C     1 
ATOM   3542 O  O     . PRO B 1 15  ? -2.31400  22.53400  41.17400  1.000 45.96867  ? 15  PRO B O     1 
ATOM   3543 C  CB    . PRO B 1 15  ? -2.72500  25.50400  40.80500  1.000 63.11283  ? 15  PRO B CB    1 
ATOM   3544 C  CG    . PRO B 1 15  ? -3.51700  26.35700  41.72900  1.000 58.06749  ? 15  PRO B CG    1 
ATOM   3545 C  CD    . PRO B 1 15  ? -4.43600  25.44000  42.46800  1.000 47.79784  ? 15  PRO B CD    1 
ATOM   3546 N  N     . GLY B 1 16  ? -2.98600  22.50700  39.02500  1.000 46.70823  ? 16  GLY B N     1 
ATOM   3547 C  CA    . GLY B 1 16  ? -2.33200  21.25500  38.71500  1.000 45.93709  ? 16  GLY B CA    1 
ATOM   3548 C  C     . GLY B 1 16  ? -3.07100  20.01000  39.14800  1.000 43.00252  ? 16  GLY B C     1 
ATOM   3549 O  O     . GLY B 1 16  ? -2.61500  18.90300  38.83500  1.000 39.93637  ? 16  GLY B O     1 
ATOM   3550 N  N     . LYS B 1 17  ? -4.20100  20.14400  39.85000  1.000 39.53106  ? 17  LYS B N     1 
ATOM   3551 C  CA    . LYS B 1 17  ? -4.90000  18.98800  40.39300  1.000 37.44660  ? 17  LYS B CA    1 
ATOM   3552 C  C     . LYS B 1 17  ? -6.36400  18.92200  39.96800  1.000 45.00013  ? 17  LYS B C     1 
ATOM   3553 O  O     . LYS B 1 17  ? -7.10100  18.06500  40.47100  1.000 47.97944  ? 17  LYS B O     1 
ATOM   3554 C  CB    . LYS B 1 17  ? -4.80700  18.99100  41.92200  1.000 36.99917  ? 17  LYS B CB    1 
ATOM   3555 C  CG    . LYS B 1 17  ? -3.39500  19.13400  42.44300  1.000 34.12514  ? 17  LYS B CG    1 
ATOM   3556 C  CD    . LYS B 1 17  ? -3.34000  18.97600  43.95200  1.000 36.94127  ? 17  LYS B CD    1 
ATOM   3557 C  CE    . LYS B 1 17  ? -1.92200  19.17100  44.46500  1.000 34.83576  ? 17  LYS B CE    1 
ATOM   3558 N  NZ    . LYS B 1 17  ? -1.42300  20.54700  44.15100  1.000 40.91280  ? 17  LYS B NZ    1 
ATOM   3559 N  N     . GLY B 1 18  ? -6.80300  19.78800  39.05700  1.000 47.92154  ? 18  GLY B N     1 
ATOM   3560 C  CA    . GLY B 1 18  ? -8.21700  19.82400  38.71300  1.000 45.46071  ? 18  GLY B CA    1 
ATOM   3561 C  C     . GLY B 1 18  ? -9.03400  20.45300  39.83100  1.000 45.07383  ? 18  GLY B C     1 
ATOM   3562 O  O     . GLY B 1 18  ? -8.69100  21.51600  40.35900  1.000 47.04248  ? 18  GLY B O     1 
ATOM   3563 N  N     . ARG B 1 19  ? -10.13700 19.80500  40.19100  1.000 39.99953  ? 19  ARG B N     1 
ATOM   3564 C  CA    . ARG B 1 19  ? -11.00200 20.27500  41.26200  1.000 40.73910  ? 19  ARG B CA    1 
ATOM   3565 C  C     . ARG B 1 19  ? -10.58900 19.64700  42.58900  1.000 34.82523  ? 19  ARG B C     1 
ATOM   3566 O  O     . ARG B 1 19  ? -10.18400 18.48300  42.64300  1.000 32.54601  ? 19  ARG B O     1 
ATOM   3567 C  CB    . ARG B 1 19  ? -12.46500 19.93600  40.95600  1.000 44.76326  ? 19  ARG B CB    1 
ATOM   3568 C  CG    . ARG B 1 19  ? -12.98000 20.55200  39.66000  1.000 49.40066  ? 19  ARG B CG    1 
ATOM   3569 C  CD    . ARG B 1 19  ? -14.20200 19.82600  39.11100  1.000 52.60104  ? 19  ARG B CD    1 
ATOM   3570 N  NE    . ARG B 1 19  ? -13.91700 18.42800  38.80200  1.000 54.23282  ? 19  ARG B NE    1 
ATOM   3571 C  CZ    . ARG B 1 19  ? -14.76000 17.60800  38.17900  1.000 60.82045  ? 19  ARG B CZ    1 
ATOM   3572 N  NH1   . ARG B 1 19  ? -15.94900 18.04700  37.78200  1.000 53.90120  ? 19  ARG B NH1   1 
ATOM   3573 N  NH2   . ARG B 1 19  ? -14.41300 16.34800  37.94900  1.000 59.98614  ? 19  ARG B NH2   1 
ATOM   3574 N  N     . GLY B 1 20  ? -10.73100 20.41700  43.66700  1.000 39.28629  ? 20  GLY B N     1 
ATOM   3575 C  CA    . GLY B 1 20  ? -10.36600 19.93600  44.98300  1.000 37.77821  ? 20  GLY B CA    1 
ATOM   3576 C  C     . GLY B 1 20  ? -11.29100 20.47800  46.05200  1.000 39.12838  ? 20  GLY B C     1 
ATOM   3577 O  O     . GLY B 1 20  ? -12.24700 21.20600  45.76800  1.000 39.21786  ? 20  GLY B O     1 
ATOM   3578 N  N     . LEU B 1 21  ? -10.97500 20.12900  47.30100  1.000 34.41465  ? 21  LEU B N     1 
ATOM   3579 C  CA    . LEU B 1 21  ? -11.74400 20.53800  48.46900  1.000 36.25435  ? 21  LEU B CA    1 
ATOM   3580 C  C     . LEU B 1 21  ? -10.86600 21.38800  49.37700  1.000 38.22300  ? 21  LEU B C     1 
ATOM   3581 O  O     . LEU B 1 21  ? -9.74600  20.98700  49.71600  1.000 36.72282  ? 21  LEU B O     1 
ATOM   3582 C  CB    . LEU B 1 21  ? -12.26000 19.31600  49.22900  1.000 41.31548  ? 21  LEU B CB    1 
ATOM   3583 C  CG    . LEU B 1 21  ? -13.24700 19.57100  50.36400  1.000 40.88648  ? 21  LEU B CG    1 
ATOM   3584 C  CD1   . LEU B 1 21  ? -14.52600 20.17700  49.81300  1.000 44.88433  ? 21  LEU B CD1   1 
ATOM   3585 C  CD2   . LEU B 1 21  ? -13.53700 18.28500  51.10900  1.000 43.81315  ? 21  LEU B CD2   1 
ATOM   3586 N  N     . ARG B 1 22  ? -11.39500 22.52700  49.78900  1.000 36.02011  ? 22  ARG B N     1 
ATOM   3587 C  CA    . ARG B 1 22  ? -10.59300 23.45700  50.60300  1.000 37.36764  ? 22  ARG B CA    1 
ATOM   3588 C  C     . ARG B 1 22  ? -11.37700 23.85900  51.84300  1.000 36.74914  ? 22  ARG B C     1 
ATOM   3589 O  O     . ARG B 1 22  ? -12.57500 23.93400  51.77100  1.000 35.04894  ? 22  ARG B O     1 
ATOM   3590 C  CB    . ARG B 1 22  ? -10.10000 24.58300  49.69800  1.000 41.47339  ? 22  ARG B CB    1 
ATOM   3591 C  CG    . ARG B 1 22  ? -10.57100 25.97000  50.07000  1.000 58.44911  ? 22  ARG B CG    1 
ATOM   3592 C  CD    . ARG B 1 22  ? -9.72500  26.97200  49.32100  1.000 54.81184  ? 22  ARG B CD    1 
ATOM   3593 N  NE    . ARG B 1 22  ? -10.55400 27.69400  48.38100  1.000 57.42267  ? 22  ARG B NE    1 
ATOM   3594 C  CZ    . ARG B 1 22  ? -10.09500 28.45400  47.40700  1.000 50.03758  ? 22  ARG B CZ    1 
ATOM   3595 N  NH1   . ARG B 1 22  ? -8.79900  28.58700  47.22000  1.000 45.81865  ? 22  ARG B NH1   1 
ATOM   3596 N  NH2   . ARG B 1 22  ? -10.94200 29.08100  46.62100  1.000 62.14956  ? 22  ARG B NH2   1 
ATOM   3597 N  N     . ALA B 1 23  ? -10.66700 24.04300  52.94400  1.000 36.44384  ? 23  ALA B N     1 
ATOM   3598 C  CA    . ALA B 1 23  ? -11.28000 24.39000  54.22000  1.000 34.44360  ? 23  ALA B CA    1 
ATOM   3599 C  C     . ALA B 1 23  ? -11.54600 25.88900  54.31500  1.000 37.21236  ? 23  ALA B C     1 
ATOM   3600 O  O     . ALA B 1 23  ? -10.73200 26.71100  53.88300  1.000 45.23437  ? 23  ALA B O     1 
ATOM   3601 C  CB    . ALA B 1 23  ? -10.39400 23.94900  55.38400  1.000 34.33570  ? 23  ALA B CB    1 
ATOM   3602 N  N     . LEU B 1 24  ? -12.71000 26.23800  54.86900  1.000 34.81207  ? 24  LEU B N     1 
ATOM   3603 C  CA    . LEU B 1 24  ? -13.06200 27.62100  55.15900  1.000 35.00157  ? 24  LEU B CA    1 
ATOM   3604 C  C     . LEU B 1 24  ? -13.00000 27.94800  56.64300  1.000 38.55199  ? 24  LEU B C     1 
ATOM   3605 O  O     . LEU B 1 24  ? -13.08500 29.12600  57.00800  1.000 48.04787  ? 24  LEU B O     1 
ATOM   3606 C  CB    . LEU B 1 24  ? -14.46800 27.93600  54.63100  1.000 37.12814  ? 24  LEU B CB    1 
ATOM   3607 C  CG    . LEU B 1 24  ? -14.60900 27.88200  53.11100  1.000 45.00803  ? 24  LEU B CG    1 
ATOM   3608 C  CD1   . LEU B 1 24  ? -16.05800 28.10000  52.69300  1.000 44.49481  ? 24  LEU B CD1   1 
ATOM   3609 C  CD2   . LEU B 1 24  ? -13.68800 28.90200  52.45200  1.000 42.91041  ? 24  LEU B CD2   1 
ATOM   3610 N  N     . GLN B 1 25  ? -12.86400 26.94500  57.49900  1.000 42.39719  ? 25  GLN B N     1 
ATOM   3611 C  CA    . GLN B 1 25  ? -12.72500 27.11100  58.93500  1.000 44.45007  ? 25  GLN B CA    1 
ATOM   3612 C  C     . GLN B 1 25  ? -11.64400 26.15600  59.40600  1.000 40.73383  ? 25  GLN B C     1 
ATOM   3613 O  O     . GLN B 1 25  ? -11.27300 25.22600  58.68000  1.000 42.79460  ? 25  GLN B O     1 
ATOM   3614 C  CB    . GLN B 1 25  ? -14.05200 26.82900  59.65500  1.000 41.86028  ? 25  GLN B CB    1 
ATOM   3615 C  CG    . GLN B 1 25  ? -14.52900 25.39600  59.52900  1.000 45.29227  ? 25  GLN B CG    1 
ATOM   3616 C  CD    . GLN B 1 25  ? -15.93900 25.20600  60.06000  1.000 56.55678  ? 25  GLN B CD    1 
ATOM   3617 O  OE1   . GLN B 1 25  ? -16.77200 26.11000  59.97300  1.000 70.78217  ? 25  GLN B OE1   1 
ATOM   3618 N  NE2   . GLN B 1 25  ? -16.21400 24.02700  60.60900  1.000 57.54901  ? 25  GLN B NE2   1 
ATOM   3619 N  N     . PRO B 1 26  ? -11.10400 26.35700  60.60400  1.000 43.14465  ? 26  PRO B N     1 
ATOM   3620 C  CA    . PRO B 1 26  ? -10.08200 25.43300  61.10500  1.000 47.67940  ? 26  PRO B CA    1 
ATOM   3621 C  C     . PRO B 1 26  ? -10.66600 24.10100  61.55700  1.000 43.13149  ? 26  PRO B C     1 
ATOM   3622 O  O     . PRO B 1 26  ? -11.79800 24.01700  62.03800  1.000 37.97034  ? 26  PRO B O     1 
ATOM   3623 C  CB    . PRO B 1 26  ? -9.46500  26.19800  62.28200  1.000 47.87416  ? 26  PRO B CB    1 
ATOM   3624 C  CG    . PRO B 1 26  ? -10.53900 27.10900  62.74300  1.000 53.97226  ? 26  PRO B CG    1 
ATOM   3625 C  CD    . PRO B 1 26  ? -11.30600 27.50300  61.51300  1.000 44.88433  ? 26  PRO B CD    1 
ATOM   3626 N  N     . PHE B 1 27  ? -9.86800  23.04200  61.38400  1.000 32.53811  ? 27  PHE B N     1 
ATOM   3627 C  CA    . PHE B 1 27  ? -10.19900 21.71400  61.89100  1.000 33.01448  ? 27  PHE B CA    1 
ATOM   3628 C  C     . PHE B 1 27  ? -9.06000  21.19500  62.75800  1.000 30.47471  ? 27  PHE B C     1 
ATOM   3629 O  O     . PHE B 1 27  ? -7.88600  21.31600  62.39200  1.000 31.77749  ? 27  PHE B O     1 
ATOM   3630 C  CB    . PHE B 1 27  ? -10.50100 20.73000  60.75700  1.000 31.64327  ? 27  PHE B CB    1 
ATOM   3631 C  CG    . PHE B 1 27  ? -11.74600 21.06200  59.98500  1.000 29.86148  ? 27  PHE B CG    1 
ATOM   3632 C  CD1   . PHE B 1 27  ? -12.98900 20.66300  60.45000  1.000 32.93816  ? 27  PHE B CD1   1 
ATOM   3633 C  CD2   . PHE B 1 27  ? -11.67400 21.75800  58.79100  1.000 31.50904  ? 27  PHE B CD2   1 
ATOM   3634 C  CE1   . PHE B 1 27  ? -14.13800 20.96100  59.74100  1.000 35.04368  ? 27  PHE B CE1   1 
ATOM   3635 C  CE2   . PHE B 1 27  ? -12.81600 22.05500  58.07700  1.000 32.88289  ? 27  PHE B CE2   1 
ATOM   3636 C  CZ    . PHE B 1 27  ? -14.05300 21.65800  58.55600  1.000 40.31799  ? 27  PHE B CZ    1 
ATOM   3637 N  N     . GLN B 1 28  ? -9.41300  20.65700  63.92000  1.000 35.98326  ? 28  GLN B N     1 
ATOM   3638 C  CA    . GLN B 1 28  ? -8.47100  20.07000  64.85900  1.000 30.71421  ? 28  GLN B CA    1 
ATOM   3639 C  C     . GLN B 1 28  ? -8.29700  18.58500  64.54900  1.000 30.26679  ? 28  GLN B C     1 
ATOM   3640 O  O     . GLN B 1 28  ? -9.14700  17.96200  63.90600  1.000 28.35340  ? 28  GLN B O     1 
ATOM   3641 C  CB    . GLN B 1 28  ? -8.99600  20.23200  66.29400  1.000 38.36776  ? 28  GLN B CB    1 
ATOM   3642 C  CG    . GLN B 1 28  ? -9.37200  21.65100  66.71300  1.000 59.12288  ? 28  GLN B CG    1 
ATOM   3643 C  CD    . GLN B 1 28  ? -8.17700  22.52500  66.99400  1.000 69.13724  ? 28  GLN B CD    1 
ATOM   3644 O  OE1   . GLN B 1 28  ? -7.34700  22.75900  66.11600  1.000 83.10207  ? 28  GLN B OE1   1 
ATOM   3645 N  NE2   . GLN B 1 28  ? -8.09500  23.04200  68.21400  1.000 70.89797  ? 28  GLN B NE2   1 
ATOM   3646 N  N     . VAL B 1 29  ? -7.18500  18.01400  65.03100  1.000 25.58991  ? 29  VAL B N     1 
ATOM   3647 C  CA    . VAL B 1 29  ? -6.98100  16.57100  64.91500  1.000 26.42948  ? 29  VAL B CA    1 
ATOM   3648 C  C     . VAL B 1 29  ? -8.17200  15.84400  65.52600  1.000 29.62724  ? 29  VAL B C     1 
ATOM   3649 O  O     . VAL B 1 29  ? -8.59600  16.14700  66.64500  1.000 30.77737  ? 29  VAL B O     1 
ATOM   3650 C  CB    . VAL B 1 29  ? -5.65500  16.14800  65.57900  1.000 27.64542  ? 29  VAL B CB    1 
ATOM   3651 C  CG1   . VAL B 1 29  ? -5.61400  14.64900  65.76200  1.000 29.95622  ? 29  VAL B CG1   1 
ATOM   3652 C  CG2   . VAL B 1 29  ? -4.46600  16.58500  64.72400  1.000 27.43750  ? 29  VAL B CG2   1 
ATOM   3653 N  N     . GLY B 1 30  ? -8.74600  14.91100  64.77100  1.000 29.68514  ? 30  GLY B N     1 
ATOM   3654 C  CA    . GLY B 1 30  ? -9.88500  14.14100  65.23100  1.000 27.45066  ? 30  GLY B CA    1 
ATOM   3655 C  C     . GLY B 1 30  ? -11.24300 14.70600  64.86600  1.000 23.80549  ? 30  GLY B C     1 
ATOM   3656 O  O     . GLY B 1 30  ? -12.23900 13.97900  64.97200  1.000 27.57436  ? 30  GLY B O     1 
ATOM   3657 N  N     . ASP B 1 31  ? -11.31100 15.96100  64.41600  1.000 29.36668  ? 31  ASP B N     1 
ATOM   3658 C  CA    . ASP B 1 31  ? -12.58000 16.58500  64.05400  1.000 32.52495  ? 31  ASP B CA    1 
ATOM   3659 C  C     . ASP B 1 31  ? -13.19000 15.94100  62.81700  1.000 34.88313  ? 31  ASP B C     1 
ATOM   3660 O  O     . ASP B 1 31  ? -12.48500 15.59800  61.86400  1.000 25.91100  ? 31  ASP B O     1 
ATOM   3661 C  CB    . ASP B 1 31  ? -12.38300 18.08100  63.78700  1.000 37.33869  ? 31  ASP B CB    1 
ATOM   3662 C  CG    . ASP B 1 31  ? -12.21100 18.89600  65.05700  1.000 45.66863  ? 31  ASP B CG    1 
ATOM   3663 O  OD1   . ASP B 1 31  ? -12.28200 18.31700  66.16800  1.000 53.51694  ? 31  ASP B OD1   1 
ATOM   3664 O  OD2   . ASP B 1 31  ? -11.98000 20.12300  64.93200  1.000 49.81913  ? 31  ASP B OD2   1 
ATOM   3665 N  N     . LEU B 1 32  ? -14.51700 15.80300  62.83200  1.000 30.88002  ? 32  LEU B N     1 
ATOM   3666 C  CA    . LEU B 1 32  ? -15.27300 15.33200  61.67500  1.000 34.33043  ? 32  LEU B CA    1 
ATOM   3667 C  C     . LEU B 1 32  ? -15.50000 16.48400  60.69800  1.000 31.15374  ? 32  LEU B C     1 
ATOM   3668 O  O     . LEU B 1 32  ? -16.19600 17.45200  61.02500  1.000 34.93050  ? 32  LEU B O     1 
ATOM   3669 C  CB    . LEU B 1 32  ? -16.60900 14.73700  62.12500  1.000 34.25674  ? 32  LEU B CB    1 
ATOM   3670 C  CG    . LEU B 1 32  ? -17.54900 14.15800  61.06100  1.000 32.42231  ? 32  LEU B CG    1 
ATOM   3671 C  CD1   . LEU B 1 32  ? -16.89500 13.00100  60.33600  1.000 31.90646  ? 32  LEU B CD1   1 
ATOM   3672 C  CD2   . LEU B 1 32  ? -18.87400 13.71800  61.67900  1.000 37.85191  ? 32  LEU B CD2   1 
ATOM   3673 N  N     . LEU B 1 33  ? -14.92100 16.38000  59.49700  1.000 33.25925  ? 33  LEU B N     1 
ATOM   3674 C  CA    . LEU B 1 33  ? -15.17300 17.38400  58.46600  1.000 33.34347  ? 33  LEU B CA    1 
ATOM   3675 C  C     . LEU B 1 33  ? -16.57300 17.23400  57.88800  1.000 32.62233  ? 33  LEU B C     1 
ATOM   3676 O  O     . LEU B 1 33  ? -17.34200 18.20300  57.84800  1.000 34.50414  ? 33  LEU B O     1 
ATOM   3677 C  CB    . LEU B 1 33  ? -14.12900 17.29100  57.35000  1.000 31.05372  ? 33  LEU B CB    1 
ATOM   3678 C  CG    . LEU B 1 33  ? -12.78200 17.98000  57.54200  1.000 29.92201  ? 33  LEU B CG    1 
ATOM   3679 C  CD1   . LEU B 1 33  ? -11.95500 17.28100  58.61900  1.000 25.69782  ? 33  LEU B CD1   1 
ATOM   3680 C  CD2   . LEU B 1 33  ? -12.03800 18.01100  56.21700  1.000 31.65116  ? 33  LEU B CD2   1 
ATOM   3681 N  N     . PHE B 1 34  ? -16.91500 16.03000  57.42000  1.000 34.68047  ? 34  PHE B N     1 
ATOM   3682 C  CA    . PHE B 1 34  ? -18.24700 15.75300  56.88800  1.000 32.02752  ? 34  PHE B CA    1 
ATOM   3683 C  C     . PHE B 1 34  ? -18.44400 14.23900  56.78800  1.000 32.48811  ? 34  PHE B C     1 
ATOM   3684 O  O     . PHE B 1 34  ? -17.51800 13.46100  56.99900  1.000 31.75644  ? 34  PHE B O     1 
ATOM   3685 C  CB    . PHE B 1 34  ? -18.47000 16.43700  55.53000  1.000 30.82475  ? 34  PHE B CB    1 
ATOM   3686 C  CG    . PHE B 1 34  ? -17.58500 15.93000  54.41000  1.000 29.87200  ? 34  PHE B CG    1 
ATOM   3687 C  CD1   . PHE B 1 34  ? -16.25300 16.32300  54.31800  1.000 34.16199  ? 34  PHE B CD1   1 
ATOM   3688 C  CD2   . PHE B 1 34  ? -18.10400 15.10400  53.41800  1.000 37.71768  ? 34  PHE B CD2   1 
ATOM   3689 C  CE1   . PHE B 1 34  ? -15.44500 15.87800  53.27500  1.000 32.70655  ? 34  PHE B CE1   1 
ATOM   3690 C  CE2   . PHE B 1 34  ? -17.30500 14.65600  52.37000  1.000 35.14632  ? 34  PHE B CE2   1 
ATOM   3691 C  CZ    . PHE B 1 34  ? -15.97100 15.04300  52.30100  1.000 32.70392  ? 34  PHE B CZ    1 
ATOM   3692 N  N     . SER B 1 35  ? -19.68500 13.84800  56.49700  1.000 38.62042  ? 35  SER B N     1 
ATOM   3693 C  CA    A SER B 1 35  ? -20.06700 12.46600  56.23900  0.500 41.21284  ? 35  SER B CA    1 
ATOM   3694 C  CA    B SER B 1 35  ? -20.04100 12.45800  56.23300  0.500 41.21284  ? 35  SER B CA    1 
ATOM   3695 C  C     . SER B 1 35  ? -20.70200 12.37000  54.85700  1.000 49.27433  ? 35  SER B C     1 
ATOM   3696 O  O     . SER B 1 35  ? -21.18700 13.36100  54.30700  1.000 45.04224  ? 35  SER B O     1 
ATOM   3697 C  CB    A SER B 1 35  ? -21.03200 11.93100  57.29000  0.500 39.79424  ? 35  SER B CB    1 
ATOM   3698 C  CB    B SER B 1 35  ? -20.98300 11.90400  57.32100  0.500 39.79424  ? 35  SER B CB    1 
ATOM   3699 O  OG    A SER B 1 35  ? -20.46500 12.01500  58.58800  0.500 64.19980  ? 35  SER B OG    1 
ATOM   3700 O  OG    B SER B 1 35  ? -22.22500 12.56500  57.31500  0.500 64.19980  ? 35  SER B OG    1 
ATOM   3701 N  N     . CYS B 1 36  ? -20.70600 11.16000  54.29400  1.000 40.97070  ? 36  CYS B N     1 
ATOM   3702 C  CA    . CYS B 1 36  ? -21.24500 10.99800  52.95000  1.000 40.73910  ? 36  CYS B CA    1 
ATOM   3703 C  C     . CYS B 1 36  ? -21.87500 9.62000   52.76500  1.000 40.81805  ? 36  CYS B C     1 
ATOM   3704 O  O     . CYS B 1 36  ? -21.16800 8.60300   52.76000  1.000 43.08411  ? 36  CYS B O     1 
ATOM   3705 C  CB    . CYS B 1 36  ? -20.14900 11.23100  51.90500  1.000 38.42829  ? 36  CYS B CB    1 
ATOM   3706 S  SG    . CYS B 1 36  ? -20.73400 11.18800  50.18100  1.000 46.25291  ? 36  CYS B SG    1 
ATOM   3707 N  N     . PRO B 1 37  ? -23.20000 9.54800   52.61200  1.000 30.00000  ? 37  PRO B N     1 
ATOM   3708 C  CA    . PRO B 1 37  ? -23.84600 8.25900   52.32600  1.000 30.00000  ? 37  PRO B CA    1 
ATOM   3709 C  C     . PRO B 1 37  ? -23.39900 7.70400   50.98500  1.000 30.00000  ? 37  PRO B C     1 
ATOM   3710 O  O     . PRO B 1 37  ? -23.15600 8.44700   50.03300  1.000 30.00000  ? 37  PRO B O     1 
ATOM   3711 C  CB    . PRO B 1 37  ? -25.34500 8.59800   52.31500  1.000 30.00000  ? 37  PRO B CB    1 
ATOM   3712 C  CG    . PRO B 1 37  ? -25.45800 9.91200   53.04900  1.000 30.00000  ? 37  PRO B CG    1 
ATOM   3713 C  CD    . PRO B 1 37  ? -24.17400 10.64400  52.76400  1.000 30.00000  ? 37  PRO B CD    1 
ATOM   3714 N  N     . ALA B 1 38  ? -23.28800 6.37700   50.91600  1.000 45.21858  ? 38  ALA B N     1 
ATOM   3715 C  CA    . ALA B 1 38  ? -22.88000 5.73000   49.67500  1.000 47.27672  ? 38  ALA B CA    1 
ATOM   3716 C  C     . ALA B 1 38  ? -23.90700 5.97600   48.57600  1.000 55.69878  ? 38  ALA B C     1 
ATOM   3717 O  O     . ALA B 1 38  ? -25.10400 5.74500   48.76500  1.000 54.08543  ? 38  ALA B O     1 
ATOM   3718 C  CB    . ALA B 1 38  ? -22.69300 4.22900   49.89900  1.000 45.45808  ? 38  ALA B CB    1 
ATOM   3719 N  N     . TYR B 1 39  ? -23.43200 6.45200   47.42200  1.000 47.43200  ? 39  TYR B N     1 
ATOM   3720 C  CA    . TYR B 1 39  ? -24.29600 6.53400   46.24800  1.000 49.94809  ? 39  TYR B CA    1 
ATOM   3721 C  C     . TYR B 1 39  ? -24.63900 5.14100   45.73400  1.000 55.71457  ? 39  TYR B C     1 
ATOM   3722 O  O     . TYR B 1 39  ? -25.79400 4.86300   45.39100  1.000 51.96149  ? 39  TYR B O     1 
ATOM   3723 C  CB    . TYR B 1 39  ? -23.62300 7.37000   45.15600  1.000 50.91137  ? 39  TYR B CB    1 
ATOM   3724 C  CG    . TYR B 1 39  ? -24.40900 7.46500   43.86400  1.000 58.38858  ? 39  TYR B CG    1 
ATOM   3725 C  CD1   . TYR B 1 39  ? -25.34400 8.47600   43.66500  1.000 57.84115  ? 39  TYR B CD1   1 
ATOM   3726 C  CD2   . TYR B 1 39  ? -24.20600 6.55200   42.83800  1.000 56.98315  ? 39  TYR B CD2   1 
ATOM   3727 C  CE1   . TYR B 1 39  ? -26.06000 8.56300   42.48300  1.000 55.16977  ? 39  TYR B CE1   1 
ATOM   3728 C  CE2   . TYR B 1 39  ? -24.91400 6.63100   41.65700  1.000 55.94092  ? 39  TYR B CE2   1 
ATOM   3729 C  CZ    . TYR B 1 39  ? -25.84000 7.63600   41.48200  1.000 58.54913  ? 39  TYR B CZ    1 
ATOM   3730 O  OH    . TYR B 1 39  ? -26.54900 7.70900   40.30200  1.000 64.67354  ? 39  TYR B OH    1 
ATOM   3731 N  N     . ALA B 1 40  ? -23.64000 4.26000   45.66300  1.000 54.39600  ? 40  ALA B N     1 
ATOM   3732 C  CA    . ALA B 1 40  ? -23.83300 2.85500   45.33600  1.000 50.97716  ? 40  ALA B CA    1 
ATOM   3733 C  C     . ALA B 1 40  ? -22.73700 2.05400   46.02300  1.000 46.95826  ? 40  ALA B C     1 
ATOM   3734 O  O     . ALA B 1 40  ? -21.63300 2.55500   46.24700  1.000 43.89210  ? 40  ALA B O     1 
ATOM   3735 C  CB    . ALA B 1 40  ? -23.81200 2.60800   43.82400  1.000 57.93063  ? 40  ALA B CB    1 
ATOM   3736 N  N     . TYR B 1 41  ? -23.04300 0.80200   46.34700  1.000 50.09285  ? 41  TYR B N     1 
ATOM   3737 C  CA    . TYR B 1 41  ? -22.10500 -0.02000  47.09700  1.000 45.21332  ? 41  TYR B CA    1 
ATOM   3738 C  C     . TYR B 1 41  ? -22.44800 -1.48100  46.86700  1.000 48.97166  ? 41  TYR B C     1 
ATOM   3739 O  O     . TYR B 1 41  ? -23.55500 -1.81800  46.43900  1.000 54.05911  ? 41  TYR B O     1 
ATOM   3740 C  CB    . TYR B 1 41  ? -22.13800 0.31300   48.59100  1.000 43.35520  ? 41  TYR B CB    1 
ATOM   3741 C  CG    . TYR B 1 41  ? -23.49100 0.09800   49.22600  1.000 48.50055  ? 41  TYR B CG    1 
ATOM   3742 C  CD1   . TYR B 1 41  ? -24.47300 1.08100   49.17200  1.000 46.99248  ? 41  TYR B CD1   1 
ATOM   3743 C  CD2   . TYR B 1 41  ? -23.78400 -1.08500  49.89200  1.000 54.15123  ? 41  TYR B CD2   1 
ATOM   3744 C  CE1   . TYR B 1 41  ? -25.71300 0.88600   49.75300  1.000 53.04057  ? 41  TYR B CE1   1 
ATOM   3745 C  CE2   . TYR B 1 41  ? -25.01700 -1.29000  50.47700  1.000 53.93541  ? 41  TYR B CE2   1 
ATOM   3746 C  CZ    . TYR B 1 41  ? -25.97800 -0.30300  50.40500  1.000 56.11199  ? 41  TYR B CZ    1 
ATOM   3747 O  OH    . TYR B 1 41  ? -27.20600 -0.51000  50.98800  1.000 61.23103  ? 41  TYR B OH    1 
ATOM   3748 N  N     . VAL B 1 42  ? -21.48100 -2.34500  47.15700  1.000 40.82332  ? 42  VAL B N     1 
ATOM   3749 C  CA    . VAL B 1 42  ? -21.67700 -3.78500  47.03000  1.000 42.13926  ? 42  VAL B CA    1 
ATOM   3750 C  C     . VAL B 1 42  ? -20.78700 -4.49000  48.04600  1.000 43.04990  ? 42  VAL B C     1 
ATOM   3751 O  O     . VAL B 1 42  ? -19.63400 -4.10200  48.25600  1.000 34.33306  ? 42  VAL B O     1 
ATOM   3752 C  CB    . VAL B 1 42  ? -21.39700 -4.26000  45.58600  1.000 46.33713  ? 42  VAL B CB    1 
ATOM   3753 C  CG1   . VAL B 1 42  ? -19.94900 -3.98000  45.18700  1.000 43.66576  ? 42  VAL B CG1   1 
ATOM   3754 C  CG2   . VAL B 1 42  ? -21.72900 -5.72600  45.44000  1.000 54.11965  ? 42  VAL B CG2   1 
ATOM   3755 N  N     . LEU B 1 43  ? -21.34800 -5.50400  48.70400  1.000 40.27062  ? 43  LEU B N     1 
ATOM   3756 C  CA    . LEU B 1 43  ? -20.59900 -6.35400  49.62300  1.000 39.67055  ? 43  LEU B CA    1 
ATOM   3757 C  C     . LEU B 1 43  ? -19.79500 -7.38900  48.84200  1.000 38.60463  ? 43  LEU B C     1 
ATOM   3758 O  O     . LEU B 1 43  ? -20.33600 -8.05900  47.95700  1.000 41.42865  ? 43  LEU B O     1 
ATOM   3759 C  CB    . LEU B 1 43  ? -21.55300 -7.05900  50.58900  1.000 41.38391  ? 43  LEU B CB    1 
ATOM   3760 C  CG    . LEU B 1 43  ? -20.91800 -7.92400  51.68300  1.000 37.67557  ? 43  LEU B CG    1 
ATOM   3761 C  CD1   . LEU B 1 43  ? -20.30200 -7.06300  52.77500  1.000 37.49923  ? 43  LEU B CD1   1 
ATOM   3762 C  CD2   . LEU B 1 43  ? -21.92900 -8.90800  52.26500  1.000 39.46526  ? 43  LEU B CD2   1 
ATOM   3763 N  N     . THR B 1 44  ? -18.51200 -7.53500  49.18000  1.000 34.65679  ? 44  THR B N     1 
ATOM   3764 C  CA    . THR B 1 44  ? -17.67000 -8.48200  48.46100  1.000 35.85167  ? 44  THR B CA    1 
ATOM   3765 C  C     . THR B 1 44  ? -18.12300 -9.91500  48.73800  1.000 40.62066  ? 44  THR B C     1 
ATOM   3766 O  O     . THR B 1 44  ? -18.62200 -10.23600 49.82000  1.000 38.56515  ? 44  THR B O     1 
ATOM   3767 C  CB    . THR B 1 44  ? -16.19500 -8.29100  48.83000  1.000 34.90155  ? 44  THR B CB    1 
ATOM   3768 O  OG1   . THR B 1 44  ? -15.37600 -9.00200  47.89300  1.000 37.24131  ? 44  THR B OG1   1 
ATOM   3769 C  CG2   . THR B 1 44  ? -15.90000 -8.80100  50.23400  1.000 37.35185  ? 44  THR B CG2   1 
ATOM   3770 N  N     . VAL B 1 45  ? -17.96300 -10.77500 47.72500  1.000 41.03650  ? 45  VAL B N     1 
ATOM   3771 C  CA    . VAL B 1 45  ? -18.54600 -12.11900 47.75400  1.000 41.43128  ? 45  VAL B CA    1 
ATOM   3772 C  C     . VAL B 1 45  ? -18.05100 -12.91400 48.95900  1.000 42.77092  ? 45  VAL B C     1 
ATOM   3773 O  O     . VAL B 1 45  ? -18.82500 -13.63400 49.60400  1.000 43.35520  ? 45  VAL B O     1 
ATOM   3774 C  CB    . VAL B 1 45  ? -18.25500 -12.84900 46.42900  1.000 47.07670  ? 45  VAL B CB    1 
ATOM   3775 C  CG1   . VAL B 1 45  ? -18.50800 -14.33900 46.57000  1.000 54.02227  ? 45  VAL B CG1   1 
ATOM   3776 C  CG2   . VAL B 1 45  ? -19.11600 -12.27800 45.31800  1.000 46.22660  ? 45  VAL B CG2   1 
ATOM   3777 N  N     . ASN B 1 46  ? -16.76000 -12.80400 49.27800  1.000 45.81076  ? 46  ASN B N     1 
ATOM   3778 C  CA    . ASN B 1 46  ? -16.16900 -13.59200 50.35400  1.000 43.17623  ? 46  ASN B CA    1 
ATOM   3779 C  C     . ASN B 1 46  ? -16.69100 -13.22200 51.73700  1.000 41.75501  ? 46  ASN B C     1 
ATOM   3780 O  O     . ASN B 1 46  ? -16.43900 -13.96800 52.68900  1.000 40.79173  ? 46  ASN B O     1 
ATOM   3781 C  CB    . ASN B 1 46  ? -14.64500 -13.45500 50.33400  1.000 43.72630  ? 46  ASN B CB    1 
ATOM   3782 C  CG    . ASN B 1 46  ? -14.00000 -14.24200 49.20600  1.000 54.52233  ? 46  ASN B CG    1 
ATOM   3783 O  OD1   . ASN B 1 46  ? -14.56000 -15.22700 48.71700  1.000 66.52903  ? 46  ASN B OD1   1 
ATOM   3784 N  ND2   . ASN B 1 46  ? -12.81500 -13.80900 48.78500  1.000 60.41514  ? 46  ASN B ND2   1 
ATOM   3785 N  N     . GLU B 1 47  ? -17.38400 -12.09400 51.88800  1.000 41.01018  ? 47  GLU B N     1 
ATOM   3786 C  CA    . GLU B 1 47  ? -17.92700 -11.70300 53.18200  1.000 41.39180  ? 47  GLU B CA    1 
ATOM   3787 C  C     . GLU B 1 47  ? -19.41800 -11.99200 53.30900  1.000 47.20566  ? 47  GLU B C     1 
ATOM   3788 O  O     . GLU B 1 47  ? -20.02200 -11.62900 54.32400  1.000 52.74580  ? 47  GLU B O     1 
ATOM   3789 C  CB    . GLU B 1 47  ? -17.64600 -10.22300 53.45100  1.000 39.58633  ? 47  GLU B CB    1 
ATOM   3790 C  CG    . GLU B 1 47  ? -16.16400 -9.89100  53.63300  1.000 47.66887  ? 47  GLU B CG    1 
ATOM   3791 C  CD    . GLU B 1 47  ? -15.54600 -10.53700 54.86900  1.000 64.08400  ? 47  GLU B CD    1 
ATOM   3792 O  OE1   . GLU B 1 47  ? -16.29300 -10.90600 55.80300  1.000 51.34826  ? 47  GLU B OE1   1 
ATOM   3793 O  OE2   . GLU B 1 47  ? -14.30300 -10.67300 54.90600  1.000 48.10840  ? 47  GLU B OE2   1 
ATOM   3794 N  N     . ARG B 1 48  ? -20.01800 -12.65200 52.31700  1.000 39.90215  ? 48  ARG B N     1 
ATOM   3795 C  CA    . ARG B 1 48  ? -21.41300 -13.05400 52.42700  1.000 48.56109  ? 48  ARG B CA    1 
ATOM   3796 C  C     . ARG B 1 48  ? -21.58800 -14.05800 53.56000  1.000 52.66421  ? 48  ARG B C     1 
ATOM   3797 O  O     . ARG B 1 48  ? -20.76700 -14.96300 53.74500  1.000 55.09608  ? 48  ARG B O     1 
ATOM   3798 C  CB    . ARG B 1 48  ? -21.90000 -13.65600 51.11000  1.000 55.87249  ? 48  ARG B CB    1 
ATOM   3799 C  CG    . ARG B 1 48  ? -21.99000 -12.66800 49.96800  1.000 56.13041  ? 48  ARG B CG    1 
ATOM   3800 C  CD    . ARG B 1 48  ? -22.22400 -13.38900 48.65300  1.000 58.64124  ? 48  ARG B CD    1 
ATOM   3801 N  NE    . ARG B 1 48  ? -22.74100 -12.49300 47.62200  1.000 56.44624  ? 48  ARG B NE    1 
ATOM   3802 C  CZ    . ARG B 1 48  ? -23.01800 -12.87000 46.37900  1.000 62.07586  ? 48  ARG B CZ    1 
ATOM   3803 N  NH1   . ARG B 1 48  ? -22.82500 -14.12900 46.00800  1.000 62.97071  ? 48  ARG B NH1   1 
ATOM   3804 N  NH2   . ARG B 1 48  ? -23.49400 -11.98900 45.50900  1.000 59.20184  ? 48  ARG B NH2   1 
ATOM   3805 N  N     . GLY B 1 49  ? -22.66000 -13.88500 54.33300  1.000 58.66756  ? 49  GLY B N     1 
ATOM   3806 C  CA    . GLY B 1 49  ? -22.91200 -14.70800 55.49100  1.000 58.95707  ? 49  GLY B CA    1 
ATOM   3807 C  C     . GLY B 1 49  ? -22.37300 -14.14500 56.78900  1.000 58.21487  ? 49  GLY B C     1 
ATOM   3808 O  O     . GLY B 1 49  ? -22.87300 -14.50400 57.86200  1.000 55.60404  ? 49  GLY B O     1 
ATOM   3809 N  N     . ASN B 1 50  ? -21.35700 -13.28800 56.72200  1.000 48.50318  ? 50  ASN B N     1 
ATOM   3810 C  CA    . ASN B 1 50  ? -20.81800 -12.60100 57.88700  1.000 51.45354  ? 50  ASN B CA    1 
ATOM   3811 C  C     . ASN B 1 50  ? -21.35100 -11.18700 58.04100  1.000 55.31979  ? 50  ASN B C     1 
ATOM   3812 O  O     . ASN B 1 50  ? -21.37100 -10.66200 59.15900  1.000 56.57520  ? 50  ASN B O     1 
ATOM   3813 C  CB    . ASN B 1 50  ? -19.28900 -12.54700 57.80800  1.000 49.70859  ? 50  ASN B CB    1 
ATOM   3814 C  CG    . ASN B 1 50  ? -18.67000 -13.91600 57.64800  1.000 52.16152  ? 50  ASN B CG    1 
ATOM   3815 O  OD1   . ASN B 1 50  ? -19.16300 -14.90400 58.19400  1.000 61.46000  ? 50  ASN B OD1   1 
ATOM   3816 N  ND2   . ASN B 1 50  ? -17.58200 -13.98400 56.89400  1.000 44.90275  ? 50  ASN B ND2   1 
ATOM   3817 N  N     . HIS B 1 51  ? -21.75100 -10.55400 56.94100  1.000 47.54517  ? 51  HIS B N     1 
ATOM   3818 C  CA    . HIS B 1 51  ? -22.21100 -9.17700  56.93900  1.000 40.07586  ? 51  HIS B CA    1 
ATOM   3819 C  C     . HIS B 1 51  ? -23.56200 -9.07700  56.25000  1.000 41.83660  ? 51  HIS B C     1 
ATOM   3820 O  O     . HIS B 1 51  ? -23.87500 -9.85400  55.34400  1.000 50.12180  ? 51  HIS B O     1 
ATOM   3821 C  CB    . HIS B 1 51  ? -21.20400 -8.26100  56.23900  1.000 41.16283  ? 51  HIS B CB    1 
ATOM   3822 C  CG    . HIS B 1 51  ? -19.90100 -8.14500  56.95900  1.000 37.74400  ? 51  HIS B CG    1 
ATOM   3823 N  ND1   . HIS B 1 51  ? -19.55900 -7.03600  57.70200  1.000 39.61001  ? 51  HIS B ND1   1 
ATOM   3824 C  CD2   . HIS B 1 51  ? -18.86400 -9.00900  57.07200  1.000 37.44133  ? 51  HIS B CD2   1 
ATOM   3825 C  CE1   . HIS B 1 51  ? -18.36200 -7.21600  58.23200  1.000 42.17874  ? 51  HIS B CE1   1 
ATOM   3826 N  NE2   . HIS B 1 51  ? -17.91900 -8.40600  57.86600  1.000 33.75142  ? 51  HIS B NE2   1 
ATOM   3827 N  N     . CYS B 1 52  ? -24.36000 -8.11000  56.69300  1.000 43.15781  ? 52  CYS B N     1 
ATOM   3828 C  CA    . CYS B 1 52  ? -25.62100 -7.81000  56.02700  1.000 48.18999  ? 52  CYS B CA    1 
ATOM   3829 C  C     . CYS B 1 52  ? -25.36700 -7.09800  54.70500  1.000 43.07622  ? 52  CYS B C     1 
ATOM   3830 O  O     . CYS B 1 52  ? -24.54900 -6.17800  54.63200  1.000 39.58896  ? 52  CYS B O     1 
ATOM   3831 C  CB    . CYS B 1 52  ? -26.51000 -6.94900  56.92300  1.000 52.71422  ? 52  CYS B CB    1 
ATOM   3832 S  SG    . CYS B 1 52  ? -27.97900 -6.32200  56.07800  1.000 53.72749  ? 52  CYS B SG    1 
ATOM   3833 N  N     . GLU B 1 53  ? -26.07300 -7.52900  53.65700  1.000 46.88194  ? 53  GLU B N     1 
ATOM   3834 C  CA    . GLU B 1 53  ? -25.87200 -6.94900  52.33300  1.000 51.61672  ? 53  GLU B CA    1 
ATOM   3835 C  C     . GLU B 1 53  ? -26.22700 -5.46600  52.30600  1.000 52.77212  ? 53  GLU B C     1 
ATOM   3836 O  O     . GLU B 1 53  ? -25.58500 -4.68000  51.59900  1.000 55.03818  ? 53  GLU B O     1 
ATOM   3837 C  CB    . GLU B 1 53  ? -26.70000 -7.71300  51.30000  1.000 61.64160  ? 53  GLU B CB    1 
ATOM   3838 C  CG    . GLU B 1 53  ? -26.32200 -9.17200  51.14900  1.000 67.65022  ? 53  GLU B CG    1 
ATOM   3839 C  CD    . GLU B 1 53  ? -25.24700 -9.39200  50.10800  1.000 68.25029  ? 53  GLU B CD    1 
ATOM   3840 O  OE1   . GLU B 1 53  ? -25.07300 -8.52000  49.23100  1.000 66.76064  ? 53  GLU B OE1   1 
ATOM   3841 O  OE2   . GLU B 1 53  ? -24.57200 -10.43800 50.16800  1.000 78.05936  ? 53  GLU B OE2   1 
ATOM   3842 N  N     . TYR B 1 54  ? -27.25900 -5.06600  53.05200  1.000 47.00564  ? 54  TYR B N     1 
ATOM   3843 C  CA    . TYR B 1 54  ? -27.75500 -3.69300  52.97100  1.000 51.81937  ? 54  TYR B CA    1 
ATOM   3844 C  C     . TYR B 1 54  ? -26.88500 -2.71600  53.76200  1.000 46.33187  ? 54  TYR B C     1 
ATOM   3845 O  O     . TYR B 1 54  ? -26.43500 -1.69700  53.22600  1.000 46.64243  ? 54  TYR B O     1 
ATOM   3846 C  CB    . TYR B 1 54  ? -29.21100 -3.62500  53.44400  1.000 57.49637  ? 54  TYR B CB    1 
ATOM   3847 C  CG    . TYR B 1 54  ? -29.80700 -2.24100  53.31800  1.000 57.24897  ? 54  TYR B CG    1 
ATOM   3848 C  CD1   . TYR B 1 54  ? -29.98100 -1.65100  52.07200  1.000 57.04368  ? 54  TYR B CD1   1 
ATOM   3849 C  CD2   . TYR B 1 54  ? -30.18500 -1.51900  54.44400  1.000 61.54159  ? 54  TYR B CD2   1 
ATOM   3850 C  CE1   . TYR B 1 54  ? -30.51500 -0.38300  51.95100  1.000 61.45474  ? 54  TYR B CE1   1 
ATOM   3851 C  CE2   . TYR B 1 54  ? -30.72400 -0.25200  54.33200  1.000 58.15171  ? 54  TYR B CE2   1 
ATOM   3852 C  CZ    . TYR B 1 54  ? -30.88600 0.31100   53.08400  1.000 62.82859  ? 54  TYR B CZ    1 
ATOM   3853 O  OH    . TYR B 1 54  ? -31.42200 1.57100   52.96300  1.000 71.12169  ? 54  TYR B OH    1 
ATOM   3854 N  N     . CYS B 1 55  ? -26.66000 -2.99800  55.04700  1.000 50.03758  ? 55  CYS B N     1 
ATOM   3855 C  CA    . CYS B 1 55  ? -26.03600 -2.04200  55.95400  1.000 49.16905  ? 55  CYS B CA    1 
ATOM   3856 C  C     . CYS B 1 55  ? -24.62700 -2.42800  56.39600  1.000 47.63992  ? 55  CYS B C     1 
ATOM   3857 O  O     . CYS B 1 55  ? -24.01000 -1.67000  57.15300  1.000 48.80059  ? 55  CYS B O     1 
ATOM   3858 C  CB    . CYS B 1 55  ? -26.91500 -1.84900  57.19300  1.000 62.45222  ? 55  CYS B CB    1 
ATOM   3859 S  SG    . CYS B 1 55  ? -26.87400 -3.24500  58.34300  1.000 53.93805  ? 55  CYS B SG    1 
ATOM   3860 N  N     . PHE B 1 56  ? -24.11600 -3.58800  55.97500  1.000 47.90311  ? 56  PHE B N     1 
ATOM   3861 C  CA    . PHE B 1 56  ? -22.74300 -4.04100  56.21500  1.000 43.03937  ? 56  PHE B CA    1 
ATOM   3862 C  C     . PHE B 1 56  ? -22.47900 -4.40900  57.67000  1.000 42.12347  ? 56  PHE B C     1 
ATOM   3863 O  O     . PHE B 1 56  ? -21.31500 -4.59500  58.05000  1.000 44.44743  ? 56  PHE B O     1 
ATOM   3864 C  CB    . PHE B 1 56  ? -21.70200 -3.01100  55.75200  1.000 39.84425  ? 56  PHE B CB    1 
ATOM   3865 C  CG    . PHE B 1 56  ? -21.38300 -3.08600  54.28000  1.000 41.73132  ? 56  PHE B CG    1 
ATOM   3866 C  CD1   . PHE B 1 56  ? -22.34300 -3.50200  53.36700  1.000 40.59697  ? 56  PHE B CD1   1 
ATOM   3867 C  CD2   . PHE B 1 56  ? -20.12700 -2.73200  53.80800  1.000 41.76027  ? 56  PHE B CD2   1 
ATOM   3868 C  CE1   . PHE B 1 56  ? -22.05500 -3.57200  52.01500  1.000 38.88624  ? 56  PHE B CE1   1 
ATOM   3869 C  CE2   . PHE B 1 56  ? -19.83200 -2.79700  52.45400  1.000 38.52304  ? 56  PHE B CE2   1 
ATOM   3870 C  CZ    . PHE B 1 56  ? -20.80100 -3.21700  51.55800  1.000 39.08363  ? 56  PHE B CZ    1 
ATOM   3871 N  N     . THR B 1 57  ? -23.51400 -4.48900  58.50500  1.000 50.00863  ? 57  THR B N     1 
ATOM   3872 C  CA    . THR B 1 57  ? -23.33500 -4.88300  59.89800  1.000 48.38738  ? 57  THR B CA    1 
ATOM   3873 C  C     . THR B 1 57  ? -22.87700 -6.33400  59.99800  1.000 43.80525  ? 57  THR B C     1 
ATOM   3874 O  O     . THR B 1 57  ? -23.47200 -7.22600  59.38700  1.000 48.11103  ? 57  THR B O     1 
ATOM   3875 C  CB    . THR B 1 57  ? -24.63800 -4.69800  60.67700  1.000 54.13017  ? 57  THR B CB    1 
ATOM   3876 O  OG1   . THR B 1 57  ? -25.06600 -3.33400  60.57800  1.000 60.07562  ? 57  THR B OG1   1 
ATOM   3877 C  CG2   . THR B 1 57  ? -24.44300 -5.06000  62.14200  1.000 64.07084  ? 57  THR B CG2   1 
ATOM   3878 N  N     . ARG B 1 58  ? -21.81700 -6.56200  60.77100  1.000 43.95264  ? 58  ARG B N     1 
ATOM   3879 C  CA    . ARG B 1 58  ? -21.31100 -7.90000  61.05100  1.000 47.87416  ? 58  ARG B CA    1 
ATOM   3880 C  C     . ARG B 1 58  ? -22.03600 -8.47200  62.26500  1.000 48.18736  ? 58  ARG B C     1 
ATOM   3881 O  O     . ARG B 1 58  ? -22.01200 -7.86700  63.34100  1.000 49.35592  ? 58  ARG B O     1 
ATOM   3882 C  CB    . ARG B 1 58  ? -19.80400 -7.85800  61.30700  1.000 53.12216  ? 58  ARG B CB    1 
ATOM   3883 C  CG    . ARG B 1 58  ? -19.16200 -9.22800  61.48400  1.000 59.08340  ? 58  ARG B CG    1 
ATOM   3884 C  CD    . ARG B 1 58  ? -17.68600 -9.12700  61.86300  1.000 62.78121  ? 58  ARG B CD    1 
ATOM   3885 N  NE    . ARG B 1 58  ? -17.44100 -8.18100  62.95000  1.000 79.76219  ? 58  ARG B NE    1 
ATOM   3886 C  CZ    . ARG B 1 58  ? -16.70100 -7.08100  62.83400  1.000 91.97682  ? 58  ARG B CZ    1 
ATOM   3887 N  NH1   . ARG B 1 58  ? -16.11500 -6.78800  61.67900  1.000 77.97514  ? 58  ARG B NH1   1 
ATOM   3888 N  NH2   . ARG B 1 58  ? -16.53500 -6.28000  63.87800  1.000 85.82871  ? 58  ARG B NH2   1 
ATOM   3889 N  N     . LYS B 1 59  ? -22.65700 -9.64000  62.10000  1.000 46.66875  ? 59  LYS B N     1 
ATOM   3890 C  CA    . LYS B 1 59  ? -23.30200 -10.32600 63.21500  1.000 66.45270  ? 59  LYS B CA    1 
ATOM   3891 C  C     . LYS B 1 59  ? -23.57700 -11.77200 62.82600  1.000 61.29156  ? 59  LYS B C     1 
ATOM   3892 O  O     . LYS B 1 59  ? -23.54200 -12.14200 61.65000  1.000 61.57580  ? 59  LYS B O     1 
ATOM   3893 C  CB    . LYS B 1 59  ? -24.60300 -9.63600  63.63400  1.000 71.15590  ? 59  LYS B CB    1 
ATOM   3894 C  CG    . LYS B 1 59  ? -25.70300 -9.71600  62.59500  1.000 78.01199  ? 59  LYS B CG    1 
ATOM   3895 C  CD    . LYS B 1 59  ? -27.03900 -9.21700  63.13200  1.000 98.74868  ? 59  LYS B CD    1 
ATOM   3896 C  CE    . LYS B 1 59  ? -27.02900 -7.71200  63.38300  1.000 106.66542 ? 59  LYS B CE    1 
ATOM   3897 N  NZ    . LYS B 1 59  ? -26.46900 -7.33100  64.71300  1.000 129.35762 ? 59  LYS B NZ    1 
ATOM   3898 N  N     . GLU B 1 60  ? -23.87200 -12.58100 63.84000  1.000 87.60524  ? 60  GLU B N     1 
ATOM   3899 C  CA    . GLU B 1 60  ? -24.22000 -13.98100 63.65500  1.000 92.17684  ? 60  GLU B CA    1 
ATOM   3900 C  C     . GLU B 1 60  ? -25.72200 -14.13500 63.44700  1.000 87.47891  ? 60  GLU B C     1 
ATOM   3901 O  O     . GLU B 1 60  ? -26.52200 -13.33200 63.93700  1.000 77.58562  ? 60  GLU B O     1 
ATOM   3902 C  CB    . GLU B 1 60  ? -23.77900 -14.81000 64.86400  1.000 102.77285 ? 60  GLU B CB    1 
ATOM   3903 C  CG    . GLU B 1 60  ? -22.27000 -14.86900 65.08900  1.000 94.75873  ? 60  GLU B CG    1 
ATOM   3904 C  CD    . GLU B 1 60  ? -21.53200 -15.63000 63.99900  1.000 110.53167 ? 60  GLU B CD    1 
ATOM   3905 O  OE1   . GLU B 1 60  ? -22.18000 -16.40700 63.26500  1.000 133.23440 ? 60  GLU B OE1   1 
ATOM   3906 O  OE2   . GLU B 1 60  ? -20.30100 -15.45400 63.88000  1.000 114.68217 ? 60  GLU B OE2   1 
ATOM   3907 N  N     . GLY B 1 61  ? -26.09700 -15.17700 62.70600  1.000 74.35892  ? 61  GLY B N     1 
ATOM   3908 C  CA    . GLY B 1 61  ? -27.49800 -15.49800 62.49100  1.000 74.18784  ? 61  GLY B CA    1 
ATOM   3909 C  C     . GLY B 1 61  ? -28.24600 -14.54200 61.58200  1.000 72.34552  ? 61  GLY B C     1 
ATOM   3910 O  O     . GLY B 1 61  ? -29.35400 -14.10200 61.90500  1.000 74.52999  ? 61  GLY B O     1 
ATOM   3911 N  N     . LEU B 1 62  ? -27.65500 -14.22400 60.43400  1.000 77.21189  ? 62  LEU B N     1 
ATOM   3912 C  CA    . LEU B 1 62  ? -28.29900 -13.35800 59.45800  1.000 70.64531  ? 62  LEU B CA    1 
ATOM   3913 C  C     . LEU B 1 62  ? -29.35700 -14.12200 58.67200  1.000 73.76411  ? 62  LEU B C     1 
ATOM   3914 O  O     . LEU B 1 62  ? -29.19400 -15.30800 58.37100  1.000 66.00791  ? 62  LEU B O     1 
ATOM   3915 C  CB    . LEU B 1 62  ? -27.25500 -12.77300 58.50800  1.000 60.56252  ? 62  LEU B CB    1 
ATOM   3916 C  CG    . LEU B 1 62  ? -26.28800 -11.78500 59.15700  1.000 63.15494  ? 62  LEU B CG    1 
ATOM   3917 C  CD1   . LEU B 1 62  ? -25.07400 -11.56100 58.27700  1.000 53.73276  ? 62  LEU B CD1   1 
ATOM   3918 C  CD2   . LEU B 1 62  ? -26.99800 -10.46900 59.41500  1.000 63.95767  ? 62  LEU B CD2   1 
ATOM   3919 N  N     . SER B 1 63  ? -30.44200 -13.42900 58.33600  1.000 83.78110  ? 63  SER B N     1 
ATOM   3920 C  CA    . SER B 1 63  ? -31.51300 -14.02900 57.55100  1.000 83.83110  ? 63  SER B CA    1 
ATOM   3921 C  C     . SER B 1 63  ? -31.05800 -14.24200 56.11200  1.000 74.32207  ? 63  SER B C     1 
ATOM   3922 O  O     . SER B 1 63  ? -30.55400 -13.31900 55.46500  1.000 98.28020  ? 63  SER B O     1 
ATOM   3923 C  CB    . SER B 1 63  ? -32.75600 -13.13800 57.58000  1.000 84.15746  ? 63  SER B CB    1 
ATOM   3924 O  OG    . SER B 1 63  ? -33.17300 -12.86900 58.90600  1.000 89.34492  ? 63  SER B OG    1 
ATOM   3925 N  N     . LYS B 1 64  ? -31.24200 -15.45900 55.60900  1.000 75.71171  ? 64  LYS B N     1 
ATOM   3926 C  CA    . LYS B 1 64  ? -30.80800 -15.82100 54.26800  1.000 76.16966  ? 64  LYS B CA    1 
ATOM   3927 C  C     . LYS B 1 64  ? -31.95000 -15.68300 53.26200  1.000 70.89797  ? 64  LYS B C     1 
ATOM   3928 O  O     . LYS B 1 64  ? -33.08400 -16.09200 53.52900  1.000 77.88039  ? 64  LYS B O     1 
ATOM   3929 C  CB    . LYS B 1 64  ? -30.26500 -17.25100 54.26700  1.000 79.49901  ? 64  LYS B CB    1 
ATOM   3930 C  CG    . LYS B 1 64  ? -29.79200 -17.75400 52.92000  1.000 86.89463  ? 64  LYS B CG    1 
ATOM   3931 C  CD    . LYS B 1 64  ? -28.98300 -19.03500 53.07300  1.000 85.17600  ? 64  LYS B CD    1 
ATOM   3932 C  CE    . LYS B 1 64  ? -29.83900 -20.16400 53.62200  1.000 81.93877  ? 64  LYS B CE    1 
ATOM   3933 N  NZ    . LYS B 1 64  ? -29.04900 -21.40800 53.81700  1.000 82.06247  ? 64  LYS B NZ    1 
ATOM   3934 N  N     . CYS B 1 65  ? -31.63100 -15.10800 52.10000  1.000 69.29515  ? 65  CYS B N     1 
ATOM   3935 C  CA    . CYS B 1 65  ? -32.59200 -14.94300 51.01200  1.000 73.37196  ? 65  CYS B CA    1 
ATOM   3936 C  C     . CYS B 1 65  ? -33.06000 -16.30700 50.52000  1.000 77.13820  ? 65  CYS B C     1 
ATOM   3937 O  O     . CYS B 1 65  ? -32.25400 -17.11200 50.04400  1.000 72.44290  ? 65  CYS B O     1 
ATOM   3938 C  CB    . CYS B 1 65  ? -31.93200 -14.15000 49.87800  1.000 72.11391  ? 65  CYS B CB    1 
ATOM   3939 S  SG    . CYS B 1 65  ? -32.90300 -13.83400 48.37600  1.000 72.82452  ? 65  CYS B SG    1 
ATOM   3940 N  N     . GLY B 1 66  ? -34.36500 -16.56900 50.63900  1.000 78.69101  ? 66  GLY B N     1 
ATOM   3941 C  CA    . GLY B 1 66  ? -34.90300 -17.88300 50.32000  1.000 82.96784  ? 66  GLY B CA    1 
ATOM   3942 C  C     . GLY B 1 66  ? -34.75300 -18.28700 48.86800  1.000 89.36335  ? 66  GLY B C     1 
ATOM   3943 O  O     . GLY B 1 66  ? -34.82500 -19.48000 48.55400  1.000 106.51014 ? 66  GLY B O     1 
ATOM   3944 N  N     . ARG B 1 67  ? -34.54800 -17.32100 47.97400  1.000 79.94116  ? 67  ARG B N     1 
ATOM   3945 C  CA    . ARG B 1 67  ? -34.47900 -17.60100 46.54400  1.000 76.20914  ? 67  ARG B CA    1 
ATOM   3946 C  C     . ARG B 1 67  ? -33.09300 -18.08600 46.12900  1.000 70.94008  ? 67  ARG B C     1 
ATOM   3947 O  O     . ARG B 1 67  ? -32.94200 -19.19000 45.59600  1.000 76.31441  ? 67  ARG B O     1 
ATOM   3948 C  CB    . ARG B 1 67  ? -34.88600 -16.34600 45.76900  1.000 76.80658  ? 67  ARG B CB    1 
ATOM   3949 C  CG    . ARG B 1 67  ? -36.29800 -15.90600 46.10800  1.000 82.47305  ? 67  ARG B CG    1 
ATOM   3950 C  CD    . ARG B 1 67  ? -36.68100 -14.55100 45.53200  1.000 93.29276  ? 67  ARG B CD    1 
ATOM   3951 N  NE    . ARG B 1 67  ? -37.88700 -14.05700 46.19400  1.000 103.43872 ? 67  ARG B NE    1 
ATOM   3952 C  CZ    . ARG B 1 67  ? -38.46900 -12.88500 45.95700  1.000 110.86329 ? 67  ARG B CZ    1 
ATOM   3953 N  NH1   . ARG B 1 67  ? -37.95900 -12.05200 45.05800  1.000 124.63863 ? 67  ARG B NH1   1 
ATOM   3954 N  NH2   . ARG B 1 67  ? -39.57100 -12.55200 46.62400  1.000 132.47378 ? 67  ARG B NH2   1 
ATOM   3955 N  N     . CYS B 1 68  ? -32.06400 -17.28100 46.39000  1.000 79.21739  ? 68  CYS B N     1 
ATOM   3956 C  CA    . CYS B 1 68  ? -30.71700 -17.60200 45.94500  1.000 74.42998  ? 68  CYS B CA    1 
ATOM   3957 C  C     . CYS B 1 68  ? -29.85100 -18.20700 47.04000  1.000 75.19586  ? 68  CYS B C     1 
ATOM   3958 O  O     . CYS B 1 68  ? -28.83500 -18.83800 46.72500  1.000 68.66350  ? 68  CYS B O     1 
ATOM   3959 C  CB    . CYS B 1 68  ? -30.04400 -16.34200 45.38300  1.000 77.48824  ? 68  CYS B CB    1 
ATOM   3960 S  SG    . CYS B 1 68  ? -29.64800 -15.09000 46.61900  1.000 73.22720  ? 68  CYS B SG    1 
ATOM   3961 N  N     . LYS B 1 69  ? -30.24600 -18.05700 48.30800  1.000 77.13820  ? 69  LYS B N     1 
ATOM   3962 C  CA    . LYS B 1 69  ? -29.49200 -18.58000 49.44800  1.000 73.09297  ? 69  LYS B CA    1 
ATOM   3963 C  C     . LYS B 1 69  ? -28.05300 -18.06800 49.44900  1.000 74.07467  ? 69  LYS B C     1 
ATOM   3964 O  O     . LYS B 1 69  ? -27.14000 -18.73200 49.94600  1.000 77.55667  ? 69  LYS B O     1 
ATOM   3965 C  CB    . LYS B 1 69  ? -29.53400 -20.11100 49.49200  1.000 76.13544  ? 69  LYS B CB    1 
ATOM   3966 C  CG    . LYS B 1 69  ? -30.87000 -20.67700 49.96300  1.000 87.07886  ? 69  LYS B CG    1 
ATOM   3967 C  CD    . LYS B 1 69  ? -31.78700 -21.02400 48.79400  1.000 97.01426  ? 69  LYS B CD    1 
ATOM   3968 C  CE    . LYS B 1 69  ? -31.31600 -22.28300 48.08100  1.000 92.87166  ? 69  LYS B CE    1 
ATOM   3969 N  NZ    . LYS B 1 69  ? -32.33100 -22.81800 47.13400  1.000 92.94535  ? 69  LYS B NZ    1 
ATOM   3970 N  N     . GLN B 1 70  ? -27.84900 -16.86800 48.89400  1.000 70.88481  ? 70  GLN B N     1 
ATOM   3971 C  CA    . GLN B 1 70  ? -26.51400 -16.29300 48.79400  1.000 67.06594  ? 70  GLN B CA    1 
ATOM   3972 C  C     . GLN B 1 70  ? -26.48100 -14.80900 49.15200  1.000 61.97322  ? 70  GLN B C     1 
ATOM   3973 O  O     . GLN B 1 70  ? -25.52100 -14.11800 48.79100  1.000 73.82201  ? 70  GLN B O     1 
ATOM   3974 C  CB    . GLN B 1 70  ? -25.95100 -16.50100 47.38800  1.000 64.50773  ? 70  GLN B CB    1 
ATOM   3975 C  CG    . GLN B 1 70  ? -25.47600 -17.91600 47.13000  1.000 68.64507  ? 70  GLN B CG    1 
ATOM   3976 C  CD    . GLN B 1 70  ? -24.91600 -18.08900 45.73700  1.000 77.38559  ? 70  GLN B CD    1 
ATOM   3977 O  OE1   . GLN B 1 70  ? -25.66400 -18.27500 44.77500  1.000 70.56109  ? 70  GLN B OE1   1 
ATOM   3978 N  NE2   . GLN B 1 70  ? -23.59300 -18.02500 45.61600  1.000 81.87824  ? 70  GLN B NE2   1 
ATOM   3979 N  N     . ALA B 1 71  ? -27.49800 -14.30000 49.84400  1.000 65.01043  ? 71  ALA B N     1 
ATOM   3980 C  CA    . ALA B 1 71  ? -27.50500 -12.92900 50.33900  1.000 66.43165  ? 71  ALA B CA    1 
ATOM   3981 C  C     . ALA B 1 71  ? -28.11500 -12.93400 51.73200  1.000 66.37112  ? 71  ALA B C     1 
ATOM   3982 O  O     . ALA B 1 71  ? -29.21500 -13.45800 51.92400  1.000 67.91077  ? 71  ALA B O     1 
ATOM   3983 C  CB    . ALA B 1 71  ? -28.29200 -11.99700 49.41000  1.000 63.92872  ? 71  ALA B CB    1 
ATOM   3984 N  N     . PHE B 1 72  ? -27.40300 -12.35800 52.69700  1.000 60.92573  ? 72  PHE B N     1 
ATOM   3985 C  CA    . PHE B 1 72  ? -27.79700 -12.41700 54.09600  1.000 61.78899  ? 72  PHE B CA    1 
ATOM   3986 C  C     . PHE B 1 72  ? -28.11000 -11.02100 54.61900  1.000 60.99152  ? 72  PHE B C     1 
ATOM   3987 O  O     . PHE B 1 72  ? -27.51600 -10.02900 54.18500  1.000 56.87524  ? 72  PHE B O     1 
ATOM   3988 C  CB    . PHE B 1 72  ? -26.69700 -13.07600 54.93500  1.000 66.61062  ? 72  PHE B CB    1 
ATOM   3989 C  CG    . PHE B 1 72  ? -26.42700 -14.51200 54.56100  1.000 68.08185  ? 72  PHE B CG    1 
ATOM   3990 C  CD1   . PHE B 1 72  ? -25.70100 -14.82500 53.42100  1.000 67.31070  ? 72  PHE B CD1   1 
ATOM   3991 C  CD2   . PHE B 1 72  ? -26.90200 -15.54900 55.34700  1.000 76.17755  ? 72  PHE B CD2   1 
ATOM   3992 C  CE1   . PHE B 1 72  ? -25.45300 -16.14200 53.07700  1.000 70.98483  ? 72  PHE B CE1   1 
ATOM   3993 C  CE2   . PHE B 1 72  ? -26.65600 -16.86800 55.00600  1.000 74.90635  ? 72  PHE B CE2   1 
ATOM   3994 C  CZ    . PHE B 1 72  ? -25.93100 -17.16300 53.87000  1.000 61.29419  ? 72  PHE B CZ    1 
ATOM   3995 N  N     . TYR B 1 73  ? -29.03600 -10.95400 55.57700  1.000 63.86555  ? 73  TYR B N     1 
ATOM   3996 C  CA    . TYR B 1 73  ? -29.59200 -9.68500  56.02500  1.000 63.61815  ? 73  TYR B CA    1 
ATOM   3997 C  C     . TYR B 1 73  ? -29.81500 -9.70000  57.52900  1.000 58.79652  ? 73  TYR B C     1 
ATOM   3998 O  O     . TYR B 1 73  ? -29.96400 -10.76000 58.14200  1.000 60.39672  ? 73  TYR B O     1 
ATOM   3999 C  CB    . TYR B 1 73  ? -30.91600 -9.37500  55.31700  1.000 60.87835  ? 73  TYR B CB    1 
ATOM   4000 C  CG    . TYR B 1 73  ? -30.77900 -9.19600  53.82600  1.000 59.24658  ? 73  TYR B CG    1 
ATOM   4001 C  CD1   . TYR B 1 73  ? -30.25500 -8.02700  53.29500  1.000 56.64363  ? 73  TYR B CD1   1 
ATOM   4002 C  CD2   . TYR B 1 73  ? -31.16800 -10.19800 52.94700  1.000 62.96808  ? 73  TYR B CD2   1 
ATOM   4003 C  CE1   . TYR B 1 73  ? -30.12700 -7.85800  51.93300  1.000 58.14381  ? 73  TYR B CE1   1 
ATOM   4004 C  CE2   . TYR B 1 73  ? -31.04400 -10.03700 51.58200  1.000 59.64663  ? 73  TYR B CE2   1 
ATOM   4005 C  CZ    . TYR B 1 73  ? -30.52400 -8.86500  51.08000  1.000 59.90455  ? 73  TYR B CZ    1 
ATOM   4006 O  OH    . TYR B 1 73  ? -30.39800 -8.69700  49.72000  1.000 62.34169  ? 73  TYR B OH    1 
ATOM   4007 N  N     . CYS B 1 74  ? -29.81700 -8.50100  58.11900  1.000 74.12731  ? 74  CYS B N     1 
ATOM   4008 C  CA    . CYS B 1 74  ? -30.17800 -8.36900  59.52700  1.000 71.00325  ? 74  CYS B CA    1 
ATOM   4009 C  C     . CYS B 1 74  ? -31.59500 -8.86800  59.77300  1.000 66.83433  ? 74  CYS B C     1 
ATOM   4010 O  O     . CYS B 1 74  ? -31.84200 -9.62500  60.71900  1.000 64.98148  ? 74  CYS B O     1 
ATOM   4011 C  CB    . CYS B 1 74  ? -30.06400 -6.90500  59.97100  1.000 71.84282  ? 74  CYS B CB    1 
ATOM   4012 S  SG    . CYS B 1 74  ? -28.43700 -6.11300  59.83800  1.000 54.32493  ? 74  CYS B SG    1 
ATOM   4013 N  N     . ASN B 1 75  ? -32.52700 -8.47600  58.91400  1.000 60.50989  ? 75  ASN B N     1 
ATOM   4014 C  CA    . ASN B 1 75  ? -33.95500 -8.70400  59.10600  1.000 69.08986  ? 75  ASN B CA    1 
ATOM   4015 C  C     . ASN B 1 75  ? -34.66100 -8.40800  57.78700  1.000 70.76638  ? 75  ASN B C     1 
ATOM   4016 O  O     . ASN B 1 75  ? -34.01900 -8.12400  56.76800  1.000 76.29336  ? 75  ASN B O     1 
ATOM   4017 C  CB    . ASN B 1 75  ? -34.49300 -7.84600  60.25100  1.000 75.37746  ? 75  ASN B CB    1 
ATOM   4018 C  CG    . ASN B 1 75  ? -34.06800 -6.39500  60.13800  1.000 68.87668  ? 75  ASN B CG    1 
ATOM   4019 O  OD1   . ASN B 1 75  ? -34.35500 -5.72300  59.14700  1.000 73.98519  ? 75  ASN B OD1   1 
ATOM   4020 N  ND2   . ASN B 1 75  ? -33.37600 -5.90400  61.15900  1.000 62.33642  ? 75  ASN B ND2   1 
ATOM   4021 N  N     . VAL B 1 76  ? -35.99600 -8.46000  57.81300  1.000 65.18940  ? 76  VAL B N     1 
ATOM   4022 C  CA    . VAL B 1 76  ? -36.78200 -8.25200  56.60100  1.000 69.62677  ? 76  VAL B CA    1 
ATOM   4023 C  C     . VAL B 1 76  ? -36.69800 -6.80500  56.12800  1.000 65.08675  ? 76  VAL B C     1 
ATOM   4024 O  O     . VAL B 1 76  ? -36.79400 -6.53400  54.92400  1.000 62.00743  ? 76  VAL B O     1 
ATOM   4025 C  CB    . VAL B 1 76  ? -38.23900 -8.68700  56.84500  1.000 80.96760  ? 76  VAL B CB    1 
ATOM   4026 C  CG1   . VAL B 1 76  ? -39.06700 -8.53200  55.58000  1.000 84.62330  ? 76  VAL B CG1   1 
ATOM   4027 C  CG2   . VAL B 1 76  ? -38.27900 -10.12300 57.34200  1.000 87.18940  ? 76  VAL B CG2   1 
ATOM   4028 N  N     . GLU B 1 77  ? -36.50500 -5.85300  57.04400  1.000 79.04895  ? 77  GLU B N     1 
ATOM   4029 C  CA    . GLU B 1 77  ? -36.38200 -4.45900  56.62700  1.000 85.12073  ? 77  GLU B CA    1 
ATOM   4030 C  C     . GLU B 1 77  ? -35.14400 -4.26700  55.76400  1.000 71.95073  ? 77  GLU B C     1 
ATOM   4031 O  O     . GLU B 1 77  ? -35.21700 -3.71200  54.66100  1.000 69.37148  ? 77  GLU B O     1 
ATOM   4032 C  CB    . GLU B 1 77  ? -36.32400 -3.53800  57.84500  1.000 94.60608  ? 77  GLU B CB    1 
ATOM   4033 C  CG    . GLU B 1 77  ? -36.53700 -2.07000  57.51600  1.000 99.40929  ? 77  GLU B CG    1 
ATOM   4034 C  CD    . GLU B 1 77  ? -36.31500 -1.16600  58.71200  1.000 98.36706  ? 77  GLU B CD    1 
ATOM   4035 O  OE1   . GLU B 1 77  ? -35.46500 -1.50400  59.56200  1.000 90.79510  ? 77  GLU B OE1   1 
ATOM   4036 O  OE2   . GLU B 1 77  ? -36.99800 -0.12500  58.80800  1.000 112.90827 ? 77  GLU B OE2   1 
ATOM   4037 N  N     . CYS B 1 78  ? -33.99000 -4.71600  56.26400  1.000 77.51719  ? 78  CYS B N     1 
ATOM   4038 C  CA    . CYS B 1 78  ? -32.76300 -4.67700  55.47700  1.000 77.18294  ? 78  CYS B CA    1 
ATOM   4039 C  C     . CYS B 1 78  ? -32.92800 -5.43500  54.16700  1.000 72.54291  ? 78  CYS B C     1 
ATOM   4040 O  O     . CYS B 1 78  ? -32.43600 -4.99700  53.12000  1.000 76.57760  ? 78  CYS B O     1 
ATOM   4041 C  CB    . CYS B 1 78  ? -31.60900 -5.24900  56.29700  1.000 74.13257  ? 78  CYS B CB    1 
ATOM   4042 S  SG    . CYS B 1 78  ? -30.91000 -4.06600  57.47000  1.000 76.60919  ? 78  CYS B SG    1 
ATOM   4043 N  N     . GLN B 1 79  ? -33.61700 -6.57900  54.21000  1.000 64.09453  ? 79  GLN B N     1 
ATOM   4044 C  CA    . GLN B 1 79  ? -33.85700 -7.35700  52.99800  1.000 64.55248  ? 79  GLN B CA    1 
ATOM   4045 C  C     . GLN B 1 79  ? -34.69400 -6.57900  51.98800  1.000 72.13760  ? 79  GLN B C     1 
ATOM   4046 O  O     . GLN B 1 79  ? -34.38600 -6.57100  50.79000  1.000 71.31381  ? 79  GLN B O     1 
ATOM   4047 C  CB    . GLN B 1 79  ? -34.53000 -8.68100  53.35100  1.000 70.94798  ? 79  GLN B CB    1 
ATOM   4048 C  CG    . GLN B 1 79  ? -34.79500 -9.56300  52.14600  1.000 74.61947  ? 79  GLN B CG    1 
ATOM   4049 C  CD    . GLN B 1 79  ? -35.28400 -10.94100 52.53100  1.000 73.04560  ? 79  GLN B CD    1 
ATOM   4050 O  OE1   . GLN B 1 79  ? -35.53500 -11.21900 53.70500  1.000 74.58789  ? 79  GLN B OE1   1 
ATOM   4051 N  NE2   . GLN B 1 79  ? -35.41500 -11.81700 51.54300  1.000 70.50319  ? 79  GLN B NE2   1 
ATOM   4052 N  N     . LYS B 1 80  ? -35.77500 -5.93700  52.44400  1.000 84.62594  ? 80  LYS B N     1 
ATOM   4053 C  CA    . LYS B 1 80  ? -36.62900 -5.20200  51.51200  1.000 90.36083  ? 80  LYS B CA    1 
ATOM   4054 C  C     . LYS B 1 80  ? -35.93500 -3.94500  50.98700  1.000 78.35940  ? 80  LYS B C     1 
ATOM   4055 O  O     . LYS B 1 80  ? -36.10200 -3.58400  49.81700  1.000 74.63263  ? 80  LYS B O     1 
ATOM   4056 C  CB    . LYS B 1 80  ? -37.98500 -4.87300  52.15500  1.000 106.31011 ? 80  LYS B CB    1 
ATOM   4057 C  CG    . LYS B 1 80  ? -38.03200 -3.70000  53.12900  1.000 131.08940 ? 80  LYS B CG    1 
ATOM   4058 C  CD    . LYS B 1 80  ? -39.34100 -2.92400  52.96400  1.000 129.23128 ? 80  LYS B CD    1 
ATOM   4059 C  CE    . LYS B 1 80  ? -39.57200 -1.92400  54.08900  1.000 115.86916 ? 80  LYS B CE    1 
ATOM   4060 N  NZ    . LYS B 1 80  ? -40.19500 -2.56200  55.28200  1.000 109.23678 ? 80  LYS B NZ    1 
ATOM   4061 N  N     . GLU B 1 81  ? -35.15900 -3.26000  51.83400  1.000 75.67486  ? 81  GLU B N     1 
ATOM   4062 C  CA    . GLU B 1 81  ? -34.46400 -2.05600  51.38500  1.000 73.53776  ? 81  GLU B CA    1 
ATOM   4063 C  C     . GLU B 1 81  ? -33.39200 -2.36800  50.34600  1.000 69.09249  ? 81  GLU B C     1 
ATOM   4064 O  O     . GLU B 1 81  ? -33.13000 -1.54400  49.46100  1.000 75.77487  ? 81  GLU B O     1 
ATOM   4065 C  CB    . GLU B 1 81  ? -33.84700 -1.33100  52.58000  1.000 69.06354  ? 81  GLU B CB    1 
ATOM   4066 C  CG    . GLU B 1 81  ? -34.86600 -0.76300  53.55500  1.000 75.49326  ? 81  GLU B CG    1 
ATOM   4067 C  CD    . GLU B 1 81  ? -35.75100 0.29300   52.92300  1.000 76.87501  ? 81  GLU B CD    1 
ATOM   4068 O  OE1   . GLU B 1 81  ? -35.21300 1.17900   52.22500  1.000 88.33164  ? 81  GLU B OE1   1 
ATOM   4069 O  OE2   . GLU B 1 81  ? -36.98200 0.24100   53.12900  1.000 87.96581  ? 81  GLU B OE2   1 
ATOM   4070 N  N     . ASP B 1 82  ? -32.77200 -3.54600  50.42800  1.000 65.38679  ? 82  ASP B N     1 
ATOM   4071 C  CA    . ASP B 1 82  ? -31.74800 -3.95100  49.47300  1.000 64.12874  ? 82  ASP B CA    1 
ATOM   4072 C  C     . ASP B 1 82  ? -32.33500 -4.52300  48.19100  1.000 73.33774  ? 82  ASP B C     1 
ATOM   4073 O  O     . ASP B 1 82  ? -31.59600 -4.70800  47.21600  1.000 64.78935  ? 82  ASP B O     1 
ATOM   4074 C  CB    . ASP B 1 82  ? -30.80800 -4.97800  50.10700  1.000 67.88709  ? 82  ASP B CB    1 
ATOM   4075 C  CG    . ASP B 1 82  ? -29.54800 -5.19600  49.28900  1.000 64.46299  ? 82  ASP B CG    1 
ATOM   4076 O  OD1   . ASP B 1 82  ? -28.92400 -4.19200  48.88300  1.000 54.74341  ? 82  ASP B OD1   1 
ATOM   4077 O  OD2   . ASP B 1 82  ? -29.18400 -6.36900  49.04700  1.000 74.74054  ? 82  ASP B OD2   1 
ATOM   4078 N  N     . TRP B 1 83  ? -33.63700 -4.80600  48.18500  1.000 74.36155  ? 83  TRP B N     1 
ATOM   4079 C  CA    . TRP B 1 83  ? -34.30500 -5.46300  47.06400  1.000 78.89630  ? 83  TRP B CA    1 
ATOM   4080 C  C     . TRP B 1 83  ? -34.04900 -4.79600  45.71400  1.000 78.33571  ? 83  TRP B C     1 
ATOM   4081 O  O     . TRP B 1 83  ? -33.68500 -5.51000  44.76600  1.000 79.17002  ? 83  TRP B O     1 
ATOM   4082 C  CB    . TRP B 1 83  ? -35.79900 -5.52200  47.41700  1.000 106.80491 ? 83  TRP B CB    1 
ATOM   4083 C  CG    . TRP B 1 83  ? -36.67800 -6.36600  46.55300  1.000 114.60848 ? 83  TRP B CG    1 
ATOM   4084 C  CD1   . TRP B 1 83  ? -36.97300 -6.17600  45.23800  1.000 105.61266 ? 83  TRP B CD1   1 
ATOM   4085 C  CD2   . TRP B 1 83  ? -37.43200 -7.51000  46.97400  1.000 138.20341 ? 83  TRP B CD2   1 
ATOM   4086 N  NE1   . TRP B 1 83  ? -37.83600 -7.15200  44.80200  1.000 105.60477 ? 83  TRP B NE1   1 
ATOM   4087 C  CE2   . TRP B 1 83  ? -38.13600 -7.97900  45.85300  1.000 134.50297 ? 83  TRP B CE2   1 
ATOM   4088 C  CE3   . TRP B 1 83  ? -37.56800 -8.19200  48.19000  1.000 141.13797 ? 83  TRP B CE3   1 
ATOM   4089 C  CZ2   . TRP B 1 83  ? -38.96700 -9.09900  45.91000  1.000 139.51673 ? 83  TRP B CZ2   1 
ATOM   4090 C  CZ3   . TRP B 1 83  ? -38.39300 -9.30200  48.24300  1.000 132.20532 ? 83  TRP B CZ3   1 
ATOM   4091 C  CH2   . TRP B 1 83  ? -39.08600 -9.74000  47.10900  1.000 127.64688 ? 83  TRP B CH2   1 
ATOM   4092 N  N     . PRO B 1 84  ? -34.18600 -3.46900  45.55200  1.000 78.11463  ? 84  PRO B N     1 
ATOM   4093 C  CA    . PRO B 1 84  ? -33.96100 -2.87700  44.21900  1.000 79.29109  ? 84  PRO B CA    1 
ATOM   4094 C  C     . PRO B 1 84  ? -32.58300 -3.14700  43.64400  1.000 73.61409  ? 84  PRO B C     1 
ATOM   4095 O  O     . PRO B 1 84  ? -32.43000 -3.18800  42.41800  1.000 82.62570  ? 84  PRO B O     1 
ATOM   4096 C  CB    . PRO B 1 84  ? -34.17600 -1.37600  44.45900  1.000 80.23857  ? 84  PRO B CB    1 
ATOM   4097 C  CG    . PRO B 1 84  ? -35.05000 -1.31000  45.63700  1.000 76.11965  ? 84  PRO B CG    1 
ATOM   4098 C  CD    . PRO B 1 84  ? -34.61600 -2.44100  46.51800  1.000 80.92549  ? 84  PRO B CD    1 
ATOM   4099 N  N     . MET B 1 85  ? -31.57100 -3.30900  44.49300  1.000 68.03974  ? 85  MET B N     1 
ATOM   4100 C  CA    . MET B 1 85  ? -30.22400 -3.63100  44.04100  1.000 69.98207  ? 85  MET B CA    1 
ATOM   4101 C  C     . MET B 1 85  ? -30.00100 -5.13500  43.95500  1.000 66.26058  ? 85  MET B C     1 
ATOM   4102 O  O     . MET B 1 85  ? -29.34500 -5.61400  43.02300  1.000 67.72917  ? 85  MET B O     1 
ATOM   4103 C  CB    . MET B 1 85  ? -29.19000 -2.99700  44.98000  1.000 65.01569  ? 85  MET B CB    1 
ATOM   4104 C  CG    . MET B 1 85  ? -29.23900 -1.47000  45.03800  1.000 60.40724  ? 85  MET B CG    1 
ATOM   4105 S  SD    . MET B 1 85  ? -28.90000 -0.68600  43.45000  1.000 70.59267  ? 85  MET B SD    1 
ATOM   4106 C  CE    . MET B 1 85  ? -29.07100 1.05100   43.86600  1.000 79.71482  ? 85  MET B CE    1 
ATOM   4107 N  N     . HIS B 1 86  ? -30.52200 -5.88300  44.92800  1.000 57.50163  ? 86  HIS B N     1 
ATOM   4108 C  CA    . HIS B 1 86  ? -30.32600 -7.32800  44.95200  1.000 65.61576  ? 86  HIS B CA    1 
ATOM   4109 C  C     . HIS B 1 86  ? -30.96600 -8.02300  43.75200  1.000 69.91101  ? 86  HIS B C     1 
ATOM   4110 O  O     . HIS B 1 86  ? -30.46100 -9.05700  43.29900  1.000 67.74496  ? 86  HIS B O     1 
ATOM   4111 C  CB    . HIS B 1 86  ? -30.87400 -7.90100  46.25500  1.000 65.00779  ? 86  HIS B CB    1 
ATOM   4112 C  CG    . HIS B 1 86  ? -30.71800 -9.38200  46.36700  1.000 69.70573  ? 86  HIS B CG    1 
ATOM   4113 N  ND1   . HIS B 1 86  ? -29.51500 -10.01800 46.15100  1.000 74.64579  ? 86  HIS B ND1   1 
ATOM   4114 C  CD2   . HIS B 1 86  ? -31.60800 -10.35200 46.67800  1.000 72.15339  ? 86  HIS B CD2   1 
ATOM   4115 C  CE1   . HIS B 1 86  ? -29.67200 -11.31800 46.31800  1.000 65.16834  ? 86  HIS B CE1   1 
ATOM   4116 N  NE2   . HIS B 1 86  ? -30.93100 -11.54700 46.64200  1.000 78.79103  ? 86  HIS B NE2   1 
ATOM   4117 N  N     . LYS B 1 87  ? -32.07600 -7.48700  43.23300  1.000 76.70393  ? 87  LYS B N     1 
ATOM   4118 C  CA    . LYS B 1 87  ? -32.75000 -8.13400  42.10800  1.000 81.33080  ? 87  LYS B CA    1 
ATOM   4119 C  C     . LYS B 1 87  ? -31.89200 -8.16900  40.85100  1.000 81.77559  ? 87  LYS B C     1 
ATOM   4120 O  O     . LYS B 1 87  ? -32.18000 -8.95600  39.94200  1.000 80.67020  ? 87  LYS B O     1 
ATOM   4121 C  CB    . LYS B 1 87  ? -34.07300 -7.43200  41.78800  1.000 91.17409  ? 87  LYS B CB    1 
ATOM   4122 C  CG    . LYS B 1 87  ? -35.14100 -7.56000  42.85700  1.000 103.93615 ? 87  LYS B CG    1 
ATOM   4123 C  CD    . LYS B 1 87  ? -35.28800 -8.98900  43.35500  1.000 104.32567 ? 87  LYS B CD    1 
ATOM   4124 C  CE    . LYS B 1 87  ? -34.90300 -9.08800  44.82500  1.000 102.50703 ? 87  LYS B CE    1 
ATOM   4125 N  NZ    . LYS B 1 87  ? -34.93200 -10.48600 45.33300  1.000 116.59029 ? 87  LYS B NZ    1 
ATOM   4126 N  N     . LEU B 1 88  ? -30.84800 -7.34200  40.77600  1.000 80.84127  ? 88  LEU B N     1 
ATOM   4127 C  CA    . LEU B 1 88  ? -29.92200 -7.41500  39.65400  1.000 80.89654  ? 88  LEU B CA    1 
ATOM   4128 C  C     . LEU B 1 88  ? -29.16100 -8.73300  39.63000  1.000 77.13820  ? 88  LEU B C     1 
ATOM   4129 O  O     . LEU B 1 88  ? -28.66000 -9.13100  38.57400  1.000 87.91317  ? 88  LEU B O     1 
ATOM   4130 C  CB    . LEU B 1 88  ? -28.93300 -6.24800  39.70900  1.000 81.34396  ? 88  LEU B CB    1 
ATOM   4131 C  CG    . LEU B 1 88  ? -29.50600 -4.83000  39.76900  1.000 76.42232  ? 88  LEU B CG    1 
ATOM   4132 C  CD1   . LEU B 1 88  ? -28.38500 -3.81600  39.91900  1.000 77.91197  ? 88  LEU B CD1   1 
ATOM   4133 C  CD2   . LEU B 1 88  ? -30.32500 -4.52900  38.52800  1.000 81.14657  ? 88  LEU B CD2   1 
ATOM   4134 N  N     . GLU B 1 89  ? -29.05400 -9.40800  40.77300  1.000 76.66709  ? 89  GLU B N     1 
ATOM   4135 C  CA    . GLU B 1 89  ? -28.24300 -10.60500 40.91100  1.000 71.41383  ? 89  GLU B CA    1 
ATOM   4136 C  C     . GLU B 1 89  ? -29.00200 -11.81700 41.43400  1.000 72.29551  ? 89  GLU B C     1 
ATOM   4137 O  O     . GLU B 1 89  ? -28.54800 -12.94400 41.20900  1.000 71.46120  ? 89  GLU B O     1 
ATOM   4138 C  CB    . GLU B 1 89  ? -27.04500 -10.32000 41.83000  1.000 63.65237  ? 89  GLU B CB    1 
ATOM   4139 C  CG    . GLU B 1 89  ? -26.13700 -9.20700  41.30400  1.000 65.49733  ? 89  GLU B CG    1 
ATOM   4140 C  CD    . GLU B 1 89  ? -24.96900 -8.89900  42.22500  1.000 58.39911  ? 89  GLU B CD    1 
ATOM   4141 O  OE1   . GLU B 1 89  ? -25.10800 -9.10500  43.44900  1.000 56.97788  ? 89  GLU B OE1   1 
ATOM   4142 O  OE2   . GLU B 1 89  ? -23.91200 -8.45500  41.72500  1.000 60.04404  ? 89  GLU B OE2   1 
ATOM   4143 N  N     . CYS B 1 90  ? -30.12500 -11.62000 42.12800  1.000 72.87190  ? 90  CYS B N     1 
ATOM   4144 C  CA    . CYS B 1 90  ? -30.87500 -12.69100 42.78300  1.000 81.08604  ? 90  CYS B CA    1 
ATOM   4145 C  C     . CYS B 1 90  ? -31.17600 -13.86500 41.85300  1.000 85.78397  ? 90  CYS B C     1 
ATOM   4146 O  O     . CYS B 1 90  ? -30.69600 -14.98200 42.07800  1.000 82.09142  ? 90  CYS B O     1 
ATOM   4147 C  CB    . CYS B 1 90  ? -32.17900 -12.13600 43.35600  1.000 91.87681  ? 90  CYS B CB    1 
ATOM   4148 S  SG    . CYS B 1 90  ? -33.11400 -13.31900 44.34000  1.000 96.62474  ? 90  CYS B SG    1 
ATOM   4149 N  N     . SER B 1 91  ? -31.99600 -13.63500 40.81900  1.000 94.12971  ? 91  SER B N     1 
ATOM   4150 C  CA    . SER B 1 91  ? -32.30500 -14.71400 39.88400  1.000 101.95433 ? 91  SER B CA    1 
ATOM   4151 C  C     . SER B 1 91  ? -31.10000 -15.12000 39.03700  1.000 105.75479 ? 91  SER B C     1 
ATOM   4152 O  O     . SER B 1 91  ? -30.87200 -16.32800 38.87700  1.000 114.15053 ? 91  SER B O     1 
ATOM   4153 C  CB    . SER B 1 91  ? -33.50600 -14.33400 39.01300  1.000 102.21752 ? 91  SER B CB    1 
ATOM   4154 O  OG    . SER B 1 91  ? -33.85500 -15.41100 38.15900  1.000 117.78517 ? 91  SER B OG    1 
ATOM   4155 N  N     . PRO B 1 92  ? -30.32500 -14.19200 38.44600  1.000 87.07360  ? 92  PRO B N     1 
ATOM   4156 C  CA    . PRO B 1 92  ? -29.13000 -14.62400 37.69200  1.000 82.89678  ? 92  PRO B CA    1 
ATOM   4157 C  C     . PRO B 1 92  ? -28.20400 -15.55300 38.46100  1.000 83.75741  ? 92  PRO B C     1 
ATOM   4158 O  O     . PRO B 1 92  ? -27.58700 -16.43900 37.85800  1.000 85.24443  ? 92  PRO B O     1 
ATOM   4159 C  CB    . PRO B 1 92  ? -28.43900 -13.29600 37.35900  1.000 78.36466  ? 92  PRO B CB    1 
ATOM   4160 C  CG    . PRO B 1 92  ? -29.54200 -12.31800 37.28700  1.000 77.74616  ? 92  PRO B CG    1 
ATOM   4161 C  CD    . PRO B 1 92  ? -30.52300 -12.73400 38.34700  1.000 79.82799  ? 92  PRO B CD    1 
ATOM   4162 N  N     . MET B 1 93  ? -28.06800 -15.35600 39.77500  1.000 85.09178  ? 93  MET B N     1 
ATOM   4163 C  CA    . MET B 1 93  ? -27.18400 -16.20900 40.56300  1.000 78.55679  ? 93  MET B CA    1 
ATOM   4164 C  C     . MET B 1 93  ? -27.64600 -17.66300 40.54300  1.000 83.93375  ? 93  MET B C     1 
ATOM   4165 O  O     . MET B 1 93  ? -26.82400 -18.58100 40.43100  1.000 92.13999  ? 93  MET B O     1 
ATOM   4166 C  CB    . MET B 1 93  ? -27.09600 -15.68500 41.99500  1.000 76.89606  ? 93  MET B CB    1 
ATOM   4167 C  CG    . MET B 1 93  ? -25.69800 -15.73900 42.58400  1.000 80.68073  ? 93  MET B CG    1 
ATOM   4168 S  SD    . MET B 1 93  ? -25.30900 -14.27900 43.56800  1.000 68.83720  ? 93  MET B SD    1 
ATOM   4169 C  CE    . MET B 1 93  ? -26.74400 -14.19100 44.63500  1.000 66.27374  ? 93  MET B CE    1 
ATOM   4170 N  N     . VAL B 1 94  ? -28.95900 -17.87200 40.60700  1.000 71.29013  ? 94  VAL B N     1 
ATOM   4171 C  CA    . VAL B 1 94  ? -29.49200 -19.26400 40.61900  1.000 79.93590  ? 94  VAL B CA    1 
ATOM   4172 C  C     . VAL B 1 94  ? -29.48400 -19.82500 39.19500  1.000 89.11068  ? 94  VAL B C     1 
ATOM   4173 O  O     . VAL B 1 94  ? -29.15000 -20.99500 39.02100  1.000 89.00014  ? 94  VAL B O     1 
ATOM   4174 C  CB    . VAL B 1 94  ? -30.86000 -19.36300 41.31600  1.000 79.65955  ? 94  VAL B CB    1 
ATOM   4175 C  CG1   . VAL B 1 94  ? -30.76600 -19.00600 42.77500  1.000 78.10147  ? 94  VAL B CG1   1 
ATOM   4176 C  CG2   . VAL B 1 94  ? -31.94700 -18.54700 40.65200  1.000 89.12648  ? 94  VAL B CG2   1 
ATOM   4177 N  N     . VAL B 1 95  ? -29.70900 -18.98100 38.20500  1.000 84.31011  ? 95  VAL B N     1 
ATOM   4178 C  CA    . VAL B 1 95  ? -29.78000 -19.45500 36.82700  1.000 87.62893  ? 95  VAL B CA    1 
ATOM   4179 C  C     . VAL B 1 95  ? -28.38800 -19.79900 36.31000  1.000 82.82572  ? 95  VAL B C     1 
ATOM   4180 O  O     . VAL B 1 95  ? -28.17500 -20.85700 35.70500  1.000 87.18414  ? 95  VAL B O     1 
ATOM   4181 C  CB    . VAL B 1 95  ? -30.47200 -18.40700 35.93700  1.000 93.23223  ? 95  VAL B CB    1 
ATOM   4182 C  CG1   . VAL B 1 95  ? -30.43600 -18.83600 34.48000  1.000 96.53263  ? 95  VAL B CG1   1 
ATOM   4183 C  CG2   . VAL B 1 95  ? -31.90600 -18.17800 36.40000  1.000 95.67200  ? 95  VAL B CG2   1 
ATOM   4184 N  N     . PHE B 1 96  ? -27.41700 -18.91500 36.54300  1.000 81.99931  ? 96  PHE B N     1 
ATOM   4185 C  CA    . PHE B 1 96  ? -26.05100 -19.19100 36.11400  1.000 87.70788  ? 96  PHE B CA    1 
ATOM   4186 C  C     . PHE B 1 96  ? -25.32800 -20.15300 37.05000  1.000 84.88649  ? 96  PHE B C     1 
ATOM   4187 O  O     . PHE B 1 96  ? -24.42300 -20.87000 36.60900  1.000 89.06594  ? 96  PHE B O     1 
ATOM   4188 C  CB    . PHE B 1 96  ? -25.27100 -17.88400 35.98400  1.000 84.66278  ? 96  PHE B CB    1 
ATOM   4189 C  CG    . PHE B 1 96  ? -25.61000 -17.11900 34.74500  1.000 98.22230  ? 96  PHE B CG    1 
ATOM   4190 C  CD1   . PHE B 1 96  ? -25.15800 -17.54600 33.51000  1.000 99.83829  ? 96  PHE B CD1   1 
ATOM   4191 C  CD2   . PHE B 1 96  ? -26.38400 -15.97300 34.81200  1.000 108.16823 ? 96  PHE B CD2   1 
ATOM   4192 C  CE1   . PHE B 1 96  ? -25.47900 -16.85200 32.36500  1.000 103.96246 ? 96  PHE B CE1   1 
ATOM   4193 C  CE2   . PHE B 1 96  ? -26.70200 -15.26900 33.66900  1.000 111.47389 ? 96  PHE B CE2   1 
ATOM   4194 C  CZ    . PHE B 1 96  ? -26.24700 -15.70900 32.44400  1.000 98.69868  ? 96  PHE B CZ    1 
ATOM   4195 N  N     . GLY B 1 97  ? -25.69800 -20.17700 38.32800  1.000 89.35282  ? 97  GLY B N     1 
ATOM   4196 C  CA    . GLY B 1 97  ? -25.11700 -21.11200 39.27200  1.000 81.83613  ? 97  GLY B CA    1 
ATOM   4197 C  C     . GLY B 1 97  ? -23.64000 -20.88100 39.51700  1.000 79.57533  ? 97  GLY B C     1 
ATOM   4198 O  O     . GLY B 1 97  ? -23.22900 -19.77900 39.89400  1.000 81.32554  ? 97  GLY B O     1 
ATOM   4199 N  N     . GLU B 1 98  ? -22.82900 -21.92000 39.30000  1.000 85.44709  ? 98  GLU B N     1 
ATOM   4200 C  CA    . GLU B 1 98  ? -21.39000 -21.79400 39.50100  1.000 81.51240  ? 98  GLU B CA    1 
ATOM   4201 C  C     . GLU B 1 98  ? -20.75600 -20.86200 38.47900  1.000 75.05374  ? 98  GLU B C     1 
ATOM   4202 O  O     . GLU B 1 98  ? -19.68800 -20.29700 38.73900  1.000 76.30915  ? 98  GLU B O     1 
ATOM   4203 C  CB    . GLU B 1 98  ? -20.72100 -23.16700 39.44800  1.000 93.72966  ? 98  GLU B CB    1 
ATOM   4204 C  CG    . GLU B 1 98  ? -21.14500 -24.11700 40.55400  1.000 106.43381 ? 98  GLU B CG    1 
ATOM   4205 C  CD    . GLU B 1 98  ? -20.29700 -25.37300 40.59000  1.000 125.83088 ? 98  GLU B CD    1 
ATOM   4206 O  OE1   . GLU B 1 98  ? -19.64300 -25.67500 39.57000  1.000 128.66279 ? 98  GLU B OE1   1 
ATOM   4207 O  OE2   . GLU B 1 98  ? -20.27600 -26.05400 41.63800  1.000 131.71316 ? 98  GLU B OE2   1 
ATOM   4208 N  N     . ASN B 1 99  ? -21.38100 -20.69700 37.31600  1.000 79.34899  ? 99  ASN B N     1 
ATOM   4209 C  CA    . ASN B 1 99  ? -20.83600 -19.85500 36.25800  1.000 81.40976  ? 99  ASN B CA    1 
ATOM   4210 C  C     . ASN B 1 99  ? -21.06200 -18.36600 36.49300  1.000 80.13856  ? 99  ASN B C     1 
ATOM   4211 O  O     . ASN B 1 99  ? -20.64200 -17.55700 35.65900  1.000 91.51097  ? 99  ASN B O     1 
ATOM   4212 C  CB    . ASN B 1 99  ? -21.43400 -20.26100 34.91000  1.000 86.96043  ? 99  ASN B CB    1 
ATOM   4213 C  CG    . ASN B 1 99  ? -21.06700 -21.67600 34.51900  1.000 88.32901  ? 99  ASN B CG    1 
ATOM   4214 O  OD1   . ASN B 1 99  ? -19.89700 -22.05700 34.55600  1.000 90.86353  ? 99  ASN B OD1   1 
ATOM   4215 N  ND2   . ASN B 1 99  ? -22.06700 -22.46900 34.15300  1.000 85.80502  ? 99  ASN B ND2   1 
ATOM   4216 N  N     . TRP B 1 100 ? -21.71000 -17.98600 37.59100  1.000 73.01928  ? 100 TRP B N     1 
ATOM   4217 C  CA    . TRP B 1 100 ? -21.90800 -16.57900 37.92900  1.000 73.55092  ? 100 TRP B CA    1 
ATOM   4218 C  C     . TRP B 1 100 ? -20.63400 -16.03500 38.56700  1.000 70.53477  ? 100 TRP B C     1 
ATOM   4219 O  O     . TRP B 1 100 ? -20.32400 -16.35300 39.72000  1.000 69.73731  ? 100 TRP B O     1 
ATOM   4220 C  CB    . TRP B 1 100 ? -23.10300 -16.42400 38.86600  1.000 72.35078  ? 100 TRP B CB    1 
ATOM   4221 C  CG    . TRP B 1 100 ? -23.55200 -15.00800 39.04400  1.000 73.66146  ? 100 TRP B CG    1 
ATOM   4222 C  CD1   . TRP B 1 100 ? -24.42300 -14.31800 38.25100  1.000 79.38583  ? 100 TRP B CD1   1 
ATOM   4223 C  CD2   . TRP B 1 100 ? -23.15900 -14.10700 40.08600  1.000 72.15602  ? 100 TRP B CD2   1 
ATOM   4224 N  NE1   . TRP B 1 100 ? -24.59400 -13.04300 38.73000  1.000 76.25388  ? 100 TRP B NE1   1 
ATOM   4225 C  CE2   . TRP B 1 100 ? -23.82900 -12.88700 39.85700  1.000 70.05050  ? 100 TRP B CE2   1 
ATOM   4226 C  CE3   . TRP B 1 100 ? -22.30600 -14.21200 41.19000  1.000 69.01091  ? 100 TRP B CE3   1 
ATOM   4227 C  CZ2   . TRP B 1 100 ? -23.67200 -11.78100 40.69000  1.000 70.51372  ? 100 TRP B CZ2   1 
ATOM   4228 C  CZ3   . TRP B 1 100 ? -22.15000 -13.11100 42.01600  1.000 68.87142  ? 100 TRP B CZ3   1 
ATOM   4229 C  CH2   . TRP B 1 100 ? -22.83000 -11.91200 41.76200  1.000 68.97143  ? 100 TRP B CH2   1 
ATOM   4230 N  N     . ASN B 1 101 ? -19.89200 -15.20900 37.82500  1.000 69.39779  ? 101 ASN B N     1 
ATOM   4231 C  CA    . ASN B 1 101 ? -18.64700 -14.66600 38.36000  1.000 69.06618  ? 101 ASN B CA    1 
ATOM   4232 C  C     . ASN B 1 101 ? -18.30600 -13.27500 37.82300  1.000 63.18126  ? 101 ASN B C     1 
ATOM   4233 O  O     . ASN B 1 101 ? -17.17800 -13.05600 37.36300  1.000 67.88972  ? 101 ASN B O     1 
ATOM   4234 C  CB    . ASN B 1 101 ? -17.49400 -15.63900 38.07600  1.000 70.56636  ? 101 ASN B CB    1 
ATOM   4235 C  CG    . ASN B 1 101 ? -17.25100 -15.85200 36.58600  1.000 82.20722  ? 101 ASN B CG    1 
ATOM   4236 O  OD1   . ASN B 1 101 ? -18.11900 -15.57900 35.75500  1.000 95.07719  ? 101 ASN B OD1   1 
ATOM   4237 N  ND2   . ASN B 1 101 ? -16.06000 -16.33100 36.24400  1.000 89.37651  ? 101 ASN B ND2   1 
ATOM   4238 N  N     . PRO B 1 102 ? -19.21600 -12.29900 37.88200  1.000 57.17791  ? 102 PRO B N     1 
ATOM   4239 C  CA    . PRO B 1 102 ? -18.83400 -10.93600 37.49600  1.000 54.04332  ? 102 PRO B CA    1 
ATOM   4240 C  C     . PRO B 1 102 ? -17.88000 -10.33500 38.51800  1.000 50.86399  ? 102 PRO B C     1 
ATOM   4241 O  O     . PRO B 1 102 ? -18.02600 -10.54200 39.72500  1.000 50.55080  ? 102 PRO B O     1 
ATOM   4242 C  CB    . PRO B 1 102 ? -20.16800 -10.18600 37.46400  1.000 56.56994  ? 102 PRO B CB    1 
ATOM   4243 C  CG    . PRO B 1 102 ? -20.99400 -10.89200 38.47200  1.000 59.88876  ? 102 PRO B CG    1 
ATOM   4244 C  CD    . PRO B 1 102 ? -20.60900 -12.34700 38.36800  1.000 57.67534  ? 102 PRO B CD    1 
ATOM   4245 N  N     . SER B 1 103 ? -16.88800 -9.59800  38.02300  1.000 58.66230  ? 103 SER B N     1 
ATOM   4246 C  CA    . SER B 1 103 ? -15.96100 -8.91100  38.90800  1.000 50.19812  ? 103 SER B CA    1 
ATOM   4247 C  C     . SER B 1 103 ? -16.69900 -7.88900  39.76600  1.000 53.33271  ? 103 SER B C     1 
ATOM   4248 O  O     . SER B 1 103 ? -17.80800 -7.45000  39.44900  1.000 69.84785  ? 103 SER B O     1 
ATOM   4249 C  CB    . SER B 1 103 ? -14.86600 -8.20700  38.11100  1.000 55.53824  ? 103 SER B CB    1 
ATOM   4250 O  OG    . SER B 1 103 ? -15.37000 -7.03500  37.49200  1.000 53.68275  ? 103 SER B OG    1 
ATOM   4251 N  N     . GLU B 1 104 ? -16.05900 -7.51400  40.87600  1.000 54.21439  ? 104 GLU B N     1 
ATOM   4252 C  CA    . GLU B 1 104 ? -16.66200 -6.56200  41.80400  1.000 50.24813  ? 104 GLU B CA    1 
ATOM   4253 C  C     . GLU B 1 104 ? -16.88700 -5.20600  41.14400  1.000 47.20566  ? 104 GLU B C     1 
ATOM   4254 O  O     . GLU B 1 104 ? -17.86500 -4.51400  41.44900  1.000 43.22624  ? 104 GLU B O     1 
ATOM   4255 C  CB    . GLU B 1 104 ? -15.78500 -6.42200  43.04900  1.000 45.00013  ? 104 GLU B CB    1 
ATOM   4256 C  CG    . GLU B 1 104 ? -16.45000 -5.67900  44.18700  1.000 45.81076  ? 104 GLU B CG    1 
ATOM   4257 C  CD    . GLU B 1 104 ? -15.92400 -6.11000  45.53600  1.000 45.92130  ? 104 GLU B CD    1 
ATOM   4258 O  OE1   . GLU B 1 104 ? -15.92700 -7.33000  45.80900  1.000 40.24693  ? 104 GLU B OE1   1 
ATOM   4259 O  OE2   . GLU B 1 104 ? -15.50900 -5.23100  46.32000  1.000 41.40496  ? 104 GLU B OE2   1 
ATOM   4260 N  N     . THR B 1 105 ? -15.97200 -4.79700  40.26100  1.000 46.24502  ? 105 THR B N     1 
ATOM   4261 C  CA    . THR B 1 105 ? -16.16900 -3.56300  39.50600  1.000 53.62222  ? 105 THR B CA    1 
ATOM   4262 C  C     . THR B 1 105 ? -17.44100 -3.62700  38.66500  1.000 58.54649  ? 105 THR B C     1 
ATOM   4263 O  O     . THR B 1 105 ? -18.19900 -2.65200  38.59700  1.000 59.44660  ? 105 THR B O     1 
ATOM   4264 C  CB    . THR B 1 105 ? -14.95300 -3.28800  38.62000  1.000 57.73850  ? 105 THR B CB    1 
ATOM   4265 O  OG1   . THR B 1 105 ? -13.78500 -3.14500  39.43900  1.000 49.00588  ? 105 THR B OG1   1 
ATOM   4266 C  CG2   . THR B 1 105 ? -15.15700 -2.01700  37.80900  1.000 58.90706  ? 105 THR B CG2   1 
ATOM   4267 N  N     . VAL B 1 106 ? -17.68800 -4.76700  38.01400  1.000 57.68850  ? 106 VAL B N     1 
ATOM   4268 C  CA    . VAL B 1 106 ? -18.90900 -4.93300  37.22800  1.000 58.53597  ? 106 VAL B CA    1 
ATOM   4269 C  C     . VAL B 1 106 ? -20.13600 -4.88100  38.13000  1.000 55.80669  ? 106 VAL B C     1 
ATOM   4270 O  O     . VAL B 1 106 ? -21.11600 -4.18500  37.83500  1.000 59.74664  ? 106 VAL B O     1 
ATOM   4271 C  CB    . VAL B 1 106 ? -18.85600 -6.24600  36.42500  1.000 60.09668  ? 106 VAL B CB    1 
ATOM   4272 C  CG1   . VAL B 1 106 ? -20.19000 -6.50600  35.74700  1.000 66.25268  ? 106 VAL B CG1   1 
ATOM   4273 C  CG2   . VAL B 1 106 ? -17.73800 -6.19200  35.39500  1.000 66.36322  ? 106 VAL B CG2   1 
ATOM   4274 N  N     . ARG B 1 107 ? -20.10100 -5.62200  39.24300  1.000 52.08519  ? 107 ARG B N     1 
ATOM   4275 C  CA    . ARG B 1 107 ? -21.21700 -5.62100  40.18700  1.000 53.71960  ? 107 ARG B CA    1 
ATOM   4276 C  C     . ARG B 1 107 ? -21.54000 -4.21000  40.65400  1.000 53.43009  ? 107 ARG B C     1 
ATOM   4277 O  O     . ARG B 1 107 ? -22.71300 -3.83000  40.75800  1.000 55.83564  ? 107 ARG B O     1 
ATOM   4278 C  CB    . ARG B 1 107 ? -20.89000 -6.49800  41.39500  1.000 49.49541  ? 107 ARG B CB    1 
ATOM   4279 C  CG    . ARG B 1 107 ? -20.68900 -7.96900  41.09500  1.000 54.89079  ? 107 ARG B CG    1 
ATOM   4280 C  CD    . ARG B 1 107 ? -20.45200 -8.74500  42.38300  1.000 55.62509  ? 107 ARG B CD    1 
ATOM   4281 N  NE    . ARG B 1 107 ? -21.64000 -8.80300  43.23200  1.000 55.52771  ? 107 ARG B NE    1 
ATOM   4282 C  CZ    . ARG B 1 107 ? -21.60500 -8.91700  44.55600  1.000 50.22181  ? 107 ARG B CZ    1 
ATOM   4283 N  NH1   . ARG B 1 107 ? -20.44200 -8.96200  45.19300  1.000 44.60008  ? 107 ARG B NH1   1 
ATOM   4284 N  NH2   . ARG B 1 107 ? -22.73400 -8.96300  45.24900  1.000 50.44552  ? 107 ARG B NH2   1 
ATOM   4285 N  N     . LEU B 1 108 ? -20.50500 -3.42600  40.95000  1.000 48.27421  ? 108 LEU B N     1 
ATOM   4286 C  CA    . LEU B 1 108 ? -20.69800 -2.05900  41.41300  1.000 50.92453  ? 108 LEU B CA    1 
ATOM   4287 C  C     . LEU B 1 108 ? -21.26900 -1.18200  40.30900  1.000 48.51898  ? 108 LEU B C     1 
ATOM   4288 O  O     . LEU B 1 108 ? -22.21800 -0.42200  40.53300  1.000 49.77702  ? 108 LEU B O     1 
ATOM   4289 C  CB    . LEU B 1 108 ? -19.36600 -1.50900  41.91800  1.000 46.50558  ? 108 LEU B CB    1 
ATOM   4290 C  CG    . LEU B 1 108 ? -19.33700 -0.10000  42.48900  1.000 45.15805  ? 108 LEU B CG    1 
ATOM   4291 C  CD1   . LEU B 1 108 ? -20.34500 0.04300   43.61900  1.000 51.18245  ? 108 LEU B CD1   1 
ATOM   4292 C  CD2   . LEU B 1 108 ? -17.92800 0.19500   42.98800  1.000 42.03925  ? 108 LEU B CD2   1 
ATOM   4293 N  N     . THR B 1 109 ? -20.70800 -1.28500  39.10300  1.000 53.57484  ? 109 THR B N     1 
ATOM   4294 C  CA    . THR B 1 109 ? -21.18000 -0.47200  37.98800  1.000 57.63849  ? 109 THR B CA    1 
ATOM   4295 C  C     . THR B 1 109 ? -22.63600 -0.77800  37.66200  1.000 59.26763  ? 109 THR B C     1 
ATOM   4296 O  O     . THR B 1 109 ? -23.40900 0.12800   37.32500  1.000 67.77128  ? 109 THR B O     1 
ATOM   4297 C  CB    . THR B 1 109 ? -20.29200 -0.70600  36.76500  1.000 53.45115  ? 109 THR B CB    1 
ATOM   4298 O  OG1   . THR B 1 109 ? -18.93900 -0.36000  37.08500  1.000 58.45438  ? 109 THR B OG1   1 
ATOM   4299 C  CG2   . THR B 1 109 ? -20.75700 0.13900   35.59200  1.000 57.78324  ? 109 THR B CG2   1 
ATOM   4300 N  N     . ALA B 1 110 ? -23.03100 -2.04900  37.76900  1.000 61.61265  ? 110 ALA B N     1 
ATOM   4301 C  CA    . ALA B 1 110 ? -24.43000 -2.41000  37.56100  1.000 66.82643  ? 110 ALA B CA    1 
ATOM   4302 C  C     . ALA B 1 110 ? -25.34300 -1.67000  38.53300  1.000 65.45258  ? 110 ALA B C     1 
ATOM   4303 O  O     . ALA B 1 110 ? -26.41900 -1.19800  38.14900  1.000 72.74820  ? 110 ALA B O     1 
ATOM   4304 C  CB    . ALA B 1 110 ? -24.60800 -3.92200  37.68800  1.000 70.92956  ? 110 ALA B CB    1 
ATOM   4305 N  N     . ARG B 1 111 ? -24.91300 -1.55500  39.78600  1.000 63.65763  ? 111 ARG B N     1 
ATOM   4306 C  CA    . ARG B 1 111 ? -25.72100 -0.86700  40.82600  1.000 67.97394  ? 111 ARG B CA    1 
ATOM   4307 C  C     . ARG B 1 111 ? -25.75000 0.64000   40.54500  1.000 67.97657  ? 111 ARG B C     1 
ATOM   4308 O  O     . ARG B 1 111 ? -26.71200 1.27000   40.94000  1.000 64.59722  ? 111 ARG B O     1 
ATOM   4309 C  CB    . ARG B 1 111 ? -25.19000 -1.14600  42.23300  1.000 62.05481  ? 111 ARG B CB    1 
ATOM   4310 C  CG    . ARG B 1 111 ? -25.81400 -2.33900  42.94000  1.000 64.86830  ? 111 ARG B CG    1 
ATOM   4311 C  CD    . ARG B 1 111 ? -24.76800 -3.24800  43.54400  1.000 66.06055  ? 111 ARG B CD    1 
ATOM   4312 N  NE    . ARG B 1 111 ? -25.14200 -4.60900  43.89600  1.000 68.10553  ? 111 ARG B NE    1 
ATOM   4313 C  CZ    . ARG B 1 111 ? -25.66100 -4.95500  45.05600  1.000 59.68874  ? 111 ARG B CZ    1 
ATOM   4314 N  NH1   . ARG B 1 111 ? -25.89700 -4.04400  45.97400  1.000 68.55296  ? 111 ARG B NH1   1 
ATOM   4315 N  NH2   . ARG B 1 111 ? -25.96300 -6.20600  45.29900  1.000 59.93877  ? 111 ARG B NH2   1 
ATOM   4316 N  N     . ILE B 1 112 ? -24.68500 1.19400   39.97100  1.000 55.22241  ? 112 ILE B N     1 
ATOM   4317 C  CA    . ILE B 1 112 ? -24.69200 2.60400   39.58500  1.000 60.36776  ? 112 ILE B CA    1 
ATOM   4318 C  C     . ILE B 1 112 ? -25.76600 2.85900   38.53500  1.000 63.85502  ? 112 ILE B C     1 
ATOM   4319 O  O     . ILE B 1 112 ? -26.57600 3.78700   38.65700  1.000 64.08400  ? 112 ILE B O     1 
ATOM   4320 C  CB    . ILE B 1 112 ? -23.30500 3.02800   39.07500  1.000 55.96724  ? 112 ILE B CB    1 
ATOM   4321 C  CG1   . ILE B 1 112 ? -22.28700 2.98700   40.21100  1.000 53.58800  ? 112 ILE B CG1   1 
ATOM   4322 C  CG2   . ILE B 1 112 ? -23.36700 4.42000   38.46300  1.000 61.90216  ? 112 ILE B CG2   1 
ATOM   4323 C  CD1   . ILE B 1 112 ? -20.87600 3.13600   39.73600  1.000 54.32493  ? 112 ILE B CD1   1 
ATOM   4324 N  N     . LEU B 1 113 ? -25.77700 2.04000   37.48000  1.000 59.76506  ? 113 LEU B N     1 
ATOM   4325 C  CA    . LEU B 1 113 ? -26.77100 2.18600   36.42100  1.000 69.15303  ? 113 LEU B CA    1 
ATOM   4326 C  C     . LEU B 1 113 ? -28.18800 2.05000   36.96900  1.000 66.67115  ? 113 LEU B C     1 
ATOM   4327 O  O     . LEU B 1 113 ? -29.10100 2.76000   36.53300  1.000 71.57963  ? 113 LEU B O     1 
ATOM   4328 C  CB    . LEU B 1 113 ? -26.50600 1.15800   35.32200  1.000 67.59231  ? 113 LEU B CB    1 
ATOM   4329 C  CG    . LEU B 1 113 ? -25.22100 1.40300   34.52800  1.000 71.17432  ? 113 LEU B CG    1 
ATOM   4330 C  CD1   . LEU B 1 113 ? -24.85900 0.19200   33.68400  1.000 77.53824  ? 113 LEU B CD1   1 
ATOM   4331 C  CD2   . LEU B 1 113 ? -25.35200 2.64700   33.66300  1.000 71.63754  ? 113 LEU B CD2   1 
ATOM   4332 N  N     . ALA B 1 114 ? -28.39200 1.14300   37.92700  1.000 67.01593  ? 114 ALA B N     1 
ATOM   4333 C  CA    . ALA B 1 114 ? -29.70700 1.02000   38.54800  1.000 70.00576  ? 114 ALA B CA    1 
ATOM   4334 C  C     . ALA B 1 114 ? -30.06000 2.26900   39.34400  1.000 72.34815  ? 114 ALA B C     1 
ATOM   4335 O  O     . ALA B 1 114 ? -31.19100 2.76400   39.26800  1.000 82.60464  ? 114 ALA B O     1 
ATOM   4336 C  CB    . ALA B 1 114 ? -29.75100 -0.21400  39.44700  1.000 68.68192  ? 114 ALA B CB    1 
ATOM   4337 N  N     . LYS B 1 115 ? -29.10100 2.78900   40.11600  1.000 77.93566  ? 115 LYS B N     1 
ATOM   4338 C  CA    . LYS B 1 115 ? -29.32900 4.01300   40.87900  1.000 71.36119  ? 115 LYS B CA    1 
ATOM   4339 C  C     . LYS B 1 115 ? -29.67400 5.18200   39.96500  1.000 67.44756  ? 115 LYS B C     1 
ATOM   4340 O  O     . LYS B 1 115 ? -30.54500 5.99600   40.29200  1.000 82.01510  ? 115 LYS B O     1 
ATOM   4341 C  CB    . LYS B 1 115 ? -28.09700 4.33900   41.72300  1.000 74.60631  ? 115 LYS B CB    1 
ATOM   4342 C  CG    . LYS B 1 115 ? -28.28100 5.50400   42.68700  1.000 75.09321  ? 115 LYS B CG    1 
ATOM   4343 C  CD    . LYS B 1 115 ? -29.19100 5.13000   43.84300  1.000 82.69939  ? 115 LYS B CD    1 
ATOM   4344 C  CE    . LYS B 1 115 ? -29.36600 6.29400   44.80300  1.000 79.13054  ? 115 LYS B CE    1 
ATOM   4345 N  NZ    . LYS B 1 115 ? -30.16600 5.90700   45.99800  1.000 85.18390  ? 115 LYS B NZ    1 
ATOM   4346 N  N     . GLN B 1 116 ? -28.98100 5.29800   38.82800  1.000 64.73145  ? 116 GLN B N     1 
ATOM   4347 C  CA    . GLN B 1 116 ? -29.26500 6.38600   37.89600  1.000 71.87441  ? 116 GLN B CA    1 
ATOM   4348 C  C     . GLN B 1 116 ? -30.67500 6.27900   37.32200  1.000 75.31429  ? 116 GLN B C     1 
ATOM   4349 O  O     . GLN B 1 116 ? -31.34300 7.29700   37.10800  1.000 81.24658  ? 116 GLN B O     1 
ATOM   4350 C  CB    . GLN B 1 116 ? -28.22800 6.40000   36.77200  1.000 69.56624  ? 116 GLN B CB    1 
ATOM   4351 C  CG    . GLN B 1 116 ? -26.85800 6.90800   37.20100  1.000 62.96281  ? 116 GLN B CG    1 
ATOM   4352 C  CD    . GLN B 1 116 ? -25.85500 6.92300   36.06100  1.000 61.38631  ? 116 GLN B CD    1 
ATOM   4353 O  OE1   . GLN B 1 116 ? -25.92400 6.09700   35.14800  1.000 67.76865  ? 116 GLN B OE1   1 
ATOM   4354 N  NE2   . GLN B 1 116 ? -24.91400 7.85900   36.11300  1.000 68.84773  ? 116 GLN B NE2   1 
ATOM   4355 N  N     . LYS B 1 117 ? -31.14700 5.05400   37.07300  1.000 89.20806  ? 117 LYS B N     1 
ATOM   4356 C  CA    . LYS B 1 117 ? -32.49100 4.87100   36.52600  1.000 97.17481  ? 117 LYS B CA    1 
ATOM   4357 C  C     . LYS B 1 117 ? -33.56500 5.24300   37.54200  1.000 97.10901  ? 117 LYS B C     1 
ATOM   4358 O  O     . LYS B 1 117 ? -34.57900 5.85300   37.18500  1.000 116.07181 ? 117 LYS B O     1 
ATOM   4359 C  CB    . LYS B 1 117 ? -32.67600 3.42700   36.05900  1.000 106.98651 ? 117 LYS B CB    1 
ATOM   4360 C  CG    . LYS B 1 117 ? -31.84600 3.05500   34.84100  1.000 121.48299 ? 117 LYS B CG    1 
ATOM   4361 C  CD    . LYS B 1 117 ? -31.87800 1.55400   34.58100  1.000 137.41648 ? 117 LYS B CD    1 
ATOM   4362 C  CE    . LYS B 1 117 ? -33.28800 1.05900   34.30100  1.000 138.19025 ? 117 LYS B CE    1 
ATOM   4363 N  NZ    . LYS B 1 117 ? -33.32200 -0.41500  34.08600  1.000 141.42485 ? 117 LYS B NZ    1 
ATOM   4364 N  N     . ILE B 1 118 ? -33.36600 4.87800   38.80800  1.000 97.18007  ? 118 ILE B N     1 
ATOM   4365 C  CA    . ILE B 1 118 ? -34.36400 5.15900   39.83600  1.000 93.64544  ? 118 ILE B CA    1 
ATOM   4366 C  C     . ILE B 1 118 ? -34.32500 6.62500   40.24300  1.000 87.80263  ? 118 ILE B C     1 
ATOM   4367 O  O     . ILE B 1 118 ? -35.35700 7.30400   40.28100  1.000 104.14933 ? 118 ILE B O     1 
ATOM   4368 C  CB    . ILE B 1 118 ? -34.15000 4.23500   41.04900  1.000 96.26154  ? 118 ILE B CB    1 
ATOM   4369 C  CG1   . ILE B 1 118 ? -34.31100 2.77100   40.64400  1.000 98.45917  ? 118 ILE B CG1   1 
ATOM   4370 C  CG2   . ILE B 1 118 ? -35.11700 4.58900   42.16600  1.000 94.81663  ? 118 ILE B CG2   1 
ATOM   4371 C  CD1   . ILE B 1 118 ? -33.80800 1.79600   41.68000  1.000 105.07839 ? 118 ILE B CD1   1 
ATOM   4372 N  N     . HIS B 1 119 ? -33.13300 7.13200   40.56100  1.000 83.13628  ? 119 HIS B N     1 
ATOM   4373 C  CA    . HIS B 1 119 ? -32.94400 8.45700   41.14600  1.000 85.27338  ? 119 HIS B CA    1 
ATOM   4374 C  C     . HIS B 1 119 ? -32.05300 9.27600   40.21700  1.000 85.73923  ? 119 HIS B C     1 
ATOM   4375 O  O     . HIS B 1 119 ? -30.85200 9.44300   40.48100  1.000 96.01151  ? 119 HIS B O     1 
ATOM   4376 C  CB    . HIS B 1 119 ? -32.34700 8.34900   42.54700  1.000 84.61804  ? 119 HIS B CB    1 
ATOM   4377 C  CG    . HIS B 1 119 ? -32.51100 9.58600   43.37100  1.000 89.61338  ? 119 HIS B CG    1 
ATOM   4378 N  ND1   . HIS B 1 119 ? -31.70400 10.69200  43.22100  1.000 95.27458  ? 119 HIS B ND1   1 
ATOM   4379 C  CD2   . HIS B 1 119 ? -33.39000 9.89200   44.35500  1.000 96.33260  ? 119 HIS B CD2   1 
ATOM   4380 C  CE1   . HIS B 1 119 ? -32.07500 11.62500  44.07900  1.000 105.45475 ? 119 HIS B CE1   1 
ATOM   4381 N  NE2   . HIS B 1 119 ? -33.09900 11.16700  44.77500  1.000 97.34851  ? 119 HIS B NE2   1 
ATOM   4382 N  N     . PRO B 1 120 ? -32.60000 9.79000   39.11200  1.000 98.00122  ? 120 PRO B N     1 
ATOM   4383 C  CA    . PRO B 1 120 ? -31.75000 10.50100  38.14200  1.000 97.91700  ? 120 PRO B CA    1 
ATOM   4384 C  C     . PRO B 1 120 ? -31.23000 11.84100  38.63900  1.000 94.58239  ? 120 PRO B C     1 
ATOM   4385 O  O     . PRO B 1 120 ? -30.15800 12.27200  38.19700  1.000 82.99679  ? 120 PRO B O     1 
ATOM   4386 C  CB    . PRO B 1 120 ? -32.67800 10.67100  36.93100  1.000 101.08844 ? 120 PRO B CB    1 
ATOM   4387 C  CG    . PRO B 1 120 ? -34.04400 10.71300  37.52600  1.000 100.19096 ? 120 PRO B CG    1 
ATOM   4388 C  CD    . PRO B 1 120 ? -34.01200 9.75900   38.69100  1.000 95.12193  ? 120 PRO B CD    1 
ATOM   4389 N  N     . GLU B 1 121 ? -31.94900 12.51600  39.53400  1.000 105.44159 ? 121 GLU B N     1 
ATOM   4390 C  CA    . GLU B 1 121 ? -31.54000 13.83000  40.00700  1.000 107.13127 ? 121 GLU B CA    1 
ATOM   4391 C  C     . GLU B 1 121 ? -30.39500 13.72400  41.01800  1.000 104.05458 ? 121 GLU B C     1 
ATOM   4392 O  O     . GLU B 1 121 ? -29.95700 12.63400  41.39900  1.000 99.69880  ? 121 GLU B O     1 
ATOM   4393 C  CB    . GLU B 1 121 ? -32.73300 14.57800  40.60800  1.000 116.73505 ? 121 GLU B CB    1 
ATOM   4394 C  CG    . GLU B 1 121 ? -33.17100 14.09800  41.98200  1.000 136.63217 ? 121 GLU B CG    1 
ATOM   4395 C  CD    . GLU B 1 121 ? -34.10400 12.90000  41.92400  1.000 167.39902 ? 121 GLU B CD    1 
ATOM   4396 O  OE1   . GLU B 1 121 ? -33.95200 12.05600  41.01500  1.000 208.65660 ? 121 GLU B OE1   1 
ATOM   4397 O  OE2   . GLU B 1 121 ? -34.99500 12.80300  42.79500  1.000 167.08319 ? 121 GLU B OE2   1 
ATOM   4398 N  N     . ARG B 1 122 ? -29.89600 14.89000  41.43000  1.000 77.96724  ? 122 ARG B N     1 
ATOM   4399 C  CA    . ARG B 1 122 ? -28.76900 14.96500  42.35300  1.000 76.60392  ? 122 ARG B CA    1 
ATOM   4400 C  C     . ARG B 1 122 ? -29.14300 14.39300  43.71500  1.000 72.29814  ? 122 ARG B C     1 
ATOM   4401 O  O     . ARG B 1 122 ? -30.18700 14.73100  44.28100  1.000 88.36849  ? 122 ARG B O     1 
ATOM   4402 C  CB    . ARG B 1 122 ? -28.31300 16.41900  42.48900  1.000 77.19610  ? 122 ARG B CB    1 
ATOM   4403 C  CG    . ARG B 1 122 ? -27.06600 16.63500  43.33400  1.000 78.23043  ? 122 ARG B CG    1 
ATOM   4404 C  CD    . ARG B 1 122 ? -26.68100 18.11200  43.36300  1.000 79.09633  ? 122 ARG B CD    1 
ATOM   4405 N  NE    . ARG B 1 122 ? -26.15200 18.57800  42.08200  1.000 86.27877  ? 122 ARG B NE    1 
ATOM   4406 C  CZ    . ARG B 1 122 ? -24.86500 18.55400  41.74600  1.000 84.83649  ? 122 ARG B CZ    1 
ATOM   4407 N  NH1   . ARG B 1 122 ? -23.96000 18.09700  42.60100  1.000 81.16499  ? 122 ARG B NH1   1 
ATOM   4408 N  NH2   . ARG B 1 122 ? -24.47800 18.99700  40.55600  1.000 77.23031  ? 122 ARG B NH2   1 
ATOM   4409 N  N     . THR B 1 123 ? -28.28900 13.52300  44.23800  1.000 70.09525  ? 123 THR B N     1 
ATOM   4410 C  CA    . THR B 1 123 ? -28.52200 12.85600  45.51100  1.000 67.91867  ? 123 THR B CA    1 
ATOM   4411 C  C     . THR B 1 123 ? -27.84500 13.62300  46.63800  1.000 65.22887  ? 123 THR B C     1 
ATOM   4412 O  O     . THR B 1 123 ? -27.01100 14.50300  46.40300  1.000 60.88362  ? 123 THR B O     1 
ATOM   4413 C  CB    . THR B 1 123 ? -27.99900 11.42100  45.44200  1.000 71.00588  ? 123 THR B CB    1 
ATOM   4414 O  OG1   . THR B 1 123 ? -26.58200 11.43100  45.23300  1.000 60.04667  ? 123 THR B OG1   1 
ATOM   4415 C  CG2   . THR B 1 123 ? -28.65200 10.67000  44.29900  1.000 77.34085  ? 123 THR B CG2   1 
ATOM   4416 N  N     . PRO B 1 124 ? -28.19500 13.32900  47.89500  1.000 75.01689  ? 124 PRO B N     1 
ATOM   4417 C  CA    . PRO B 1 124 ? -27.43500 13.90700  49.01800  1.000 69.65046  ? 124 PRO B CA    1 
ATOM   4418 C  C     . PRO B 1 124 ? -25.97100 13.49100  49.04400  1.000 76.93028  ? 124 PRO B C     1 
ATOM   4419 O  O     . PRO B 1 124 ? -25.17500 14.12600  49.74700  1.000 70.32685  ? 124 PRO B O     1 
ATOM   4420 C  CB    . PRO B 1 124 ? -28.18500 13.39400  50.25500  1.000 69.30305  ? 124 PRO B CB    1 
ATOM   4421 C  CG    . PRO B 1 124 ? -29.56400 13.10400  49.76700  1.000 71.21907  ? 124 PRO B CG    1 
ATOM   4422 C  CD    . PRO B 1 124 ? -29.40000 12.61400  48.35800  1.000 68.32398  ? 124 PRO B CD    1 
ATOM   4423 N  N     . SER B 1 125 ? -25.59200 12.45000  48.30300  1.000 78.11989  ? 125 SER B N     1 
ATOM   4424 C  CA    . SER B 1 125 ? -24.19600 12.05300  48.17100  1.000 64.49457  ? 125 SER B CA    1 
ATOM   4425 C  C     . SER B 1 125 ? -23.40900 12.98300  47.26000  1.000 58.83074  ? 125 SER B C     1 
ATOM   4426 O  O     . SER B 1 125 ? -22.17600 12.89300  47.22300  1.000 53.21428  ? 125 SER B O     1 
ATOM   4427 C  CB    . SER B 1 125 ? -24.10100 10.62000  47.63600  1.000 69.58992  ? 125 SER B CB    1 
ATOM   4428 O  OG    . SER B 1 125 ? -24.73000 9.70300   48.51400  1.000 86.56038  ? 125 SER B OG    1 
ATOM   4429 N  N     . GLU B 1 126 ? -24.09100 13.85500  46.51900  1.000 69.07407  ? 126 GLU B N     1 
ATOM   4430 C  CA    . GLU B 1 126 ? -23.46000 14.65700  45.48000  1.000 62.06534  ? 126 GLU B CA    1 
ATOM   4431 C  C     . GLU B 1 126 ? -23.64500 16.14500  45.74300  1.000 59.54925  ? 126 GLU B C     1 
ATOM   4432 O  O     . GLU B 1 126 ? -23.99600 16.89800  44.82900  1.000 63.68132  ? 126 GLU B O     1 
ATOM   4433 C  CB    . GLU B 1 126 ? -24.04600 14.29100  44.11500  1.000 57.15685  ? 126 GLU B CB    1 
ATOM   4434 C  CG    . GLU B 1 126 ? -23.93300 12.81900  43.77000  1.000 62.24957  ? 126 GLU B CG    1 
ATOM   4435 C  CD    . GLU B 1 126 ? -24.85700 12.40600  42.63400  1.000 61.95216  ? 126 GLU B CD    1 
ATOM   4436 O  OE1   . GLU B 1 126 ? -26.08800 12.36700  42.84300  1.000 61.90479  ? 126 GLU B OE1   1 
ATOM   4437 O  OE2   . GLU B 1 126 ? -24.35000 12.11600  41.53100  1.000 62.59435  ? 126 GLU B OE2   1 
ATOM   4438 N  N     . LYS B 1 127 ? -23.40400 16.58800  46.97800  1.000 57.22002  ? 127 LYS B N     1 
ATOM   4439 C  CA    . LYS B 1 127 ? -23.60000 18.00000  47.28600  1.000 61.73109  ? 127 LYS B CA    1 
ATOM   4440 C  C     . LYS B 1 127 ? -22.62000 18.88100  46.51900  1.000 64.48668  ? 127 LYS B C     1 
ATOM   4441 O  O     . LYS B 1 127 ? -22.99600 19.95300  46.02900  1.000 58.40174  ? 127 LYS B O     1 
ATOM   4442 C  CB    . LYS B 1 127 ? -23.47200 18.23700  48.79000  1.000 74.45630  ? 127 LYS B CB    1 
ATOM   4443 C  CG    . LYS B 1 127 ? -24.55800 17.57900  49.62500  1.000 66.50008  ? 127 LYS B CG    1 
ATOM   4444 C  CD    . LYS B 1 127 ? -24.33500 17.83500  51.10500  1.000 69.03986  ? 127 LYS B CD    1 
ATOM   4445 C  CE    . LYS B 1 127 ? -25.20300 16.93200  51.95800  1.000 64.62880  ? 127 LYS B CE    1 
ATOM   4446 N  NZ    . LYS B 1 127 ? -26.64400 17.13400  51.65700  1.000 86.88147  ? 127 LYS B NZ    1 
ATOM   4447 N  N     . LEU B 1 128 ? -21.36700 18.43700  46.38100  1.000 54.76446  ? 128 LEU B N     1 
ATOM   4448 C  CA    . LEU B 1 128 ? -20.33600 19.22400  45.71700  1.000 52.22731  ? 128 LEU B CA    1 
ATOM   4449 C  C     . LEU B 1 128 ? -19.84500 18.62000  44.41200  1.000 54.45127  ? 128 LEU B C     1 
ATOM   4450 O  O     . LEU B 1 128 ? -19.31800 19.35700  43.57100  1.000 52.52998  ? 128 LEU B O     1 
ATOM   4451 C  CB    . LEU B 1 128 ? -19.12700 19.41900  46.64600  1.000 50.58501  ? 128 LEU B CB    1 
ATOM   4452 C  CG    . LEU B 1 128 ? -19.34900 20.32300  47.85900  1.000 50.74819  ? 128 LEU B CG    1 
ATOM   4453 C  CD1   . LEU B 1 128 ? -18.08300 20.45400  48.70100  1.000 44.03949  ? 128 LEU B CD1   1 
ATOM   4454 C  CD2   . LEU B 1 128 ? -19.84300 21.68600  47.40200  1.000 63.53393  ? 128 LEU B CD2   1 
ATOM   4455 N  N     . LEU B 1 129 ? -19.99900 17.31300  44.22300  1.000 48.24263  ? 129 LEU B N     1 
ATOM   4456 C  CA    . LEU B 1 129 ? -19.50200 16.64500  43.02900  1.000 44.54481  ? 129 LEU B CA    1 
ATOM   4457 C  C     . LEU B 1 129 ? -20.45600 15.52300  42.66000  1.000 46.37925  ? 129 LEU B C     1 
ATOM   4458 O  O     . LEU B 1 129 ? -20.75900 14.66900  43.49700  1.000 47.31620  ? 129 LEU B O     1 
ATOM   4459 C  CB    . LEU B 1 129 ? -18.09100 16.09300  43.25700  1.000 42.10242  ? 129 LEU B CB    1 
ATOM   4460 C  CG    . LEU B 1 129 ? -17.42900 15.37600  42.07900  1.000 41.43128  ? 129 LEU B CG    1 
ATOM   4461 C  CD1   . LEU B 1 129 ? -17.22400 16.32400  40.90600  1.000 43.31309  ? 129 LEU B CD1   1 
ATOM   4462 C  CD2   . LEU B 1 129 ? -16.10100 14.77400  42.52300  1.000 42.69986  ? 129 LEU B CD2   1 
ATOM   4463 N  N     . ALA B 1 130 ? -20.93300 15.53900  41.41800  1.000 53.13532  ? 130 ALA B N     1 
ATOM   4464 C  CA    . ALA B 1 130 ? -21.84400 14.51800  40.92600  1.000 54.71445  ? 130 ALA B CA    1 
ATOM   4465 C  C     . ALA B 1 130 ? -21.08200 13.38900  40.24000  1.000 56.70417  ? 130 ALA B C     1 
ATOM   4466 O  O     . ALA B 1 130 ? -19.97500 13.57900  39.72700  1.000 57.87010  ? 130 ALA B O     1 
ATOM   4467 C  CB    . ALA B 1 130 ? -22.85900 15.12800  39.95600  1.000 57.12527  ? 130 ALA B CB    1 
ATOM   4468 N  N     . VAL B 1 131 ? -21.69900 12.20400  40.23600  1.000 49.59805  ? 131 VAL B N     1 
ATOM   4469 C  CA    . VAL B 1 131 ? -21.11900 11.04200  39.56400  1.000 49.78228  ? 131 VAL B CA    1 
ATOM   4470 C  C     . VAL B 1 131 ? -20.89300 11.33700  38.08800  1.000 59.58609  ? 131 VAL B C     1 
ATOM   4471 O  O     . VAL B 1 131 ? -19.86400 10.96000  37.51300  1.000 57.39109  ? 131 VAL B O     1 
ATOM   4472 C  CB    . VAL B 1 131 ? -22.02000 9.80700   39.76100  1.000 53.04583  ? 131 VAL B CB    1 
ATOM   4473 C  CG1   . VAL B 1 131 ? -21.53100 8.64200   38.91700  1.000 50.90874  ? 131 VAL B CG1   1 
ATOM   4474 C  CG2   . VAL B 1 131 ? -22.05600 9.41100   41.22900  1.000 55.81195  ? 131 VAL B CG2   1 
ATOM   4475 N  N     . LYS B 1 132 ? -21.85600 12.01000  37.45100  1.000 54.46706  ? 132 LYS B N     1 
ATOM   4476 C  CA    . LYS B 1 132 ? -21.71900 12.36100  36.04200  1.000 65.42627  ? 132 LYS B CA    1 
ATOM   4477 C  C     . LYS B 1 132 ? -20.48300 13.22000  35.79600  1.000 62.10481  ? 132 LYS B C     1 
ATOM   4478 O  O     . LYS B 1 132 ? -19.89900 13.17200  34.70800  1.000 59.43081  ? 132 LYS B O     1 
ATOM   4479 C  CB    . LYS B 1 132 ? -22.97900 13.08500  35.57000  1.000 70.49003  ? 132 LYS B CB    1 
ATOM   4480 C  CG    . LYS B 1 132 ? -24.25600 12.29400  35.81500  1.000 75.18007  ? 132 LYS B CG    1 
ATOM   4481 C  CD    . LYS B 1 132 ? -24.34400 11.04600  34.95600  1.000 82.33092  ? 132 LYS B CD    1 
ATOM   4482 C  CE    . LYS B 1 132 ? -24.93600 11.34500  33.58800  1.000 85.96820  ? 132 LYS B CE    1 
ATOM   4483 N  NZ    . LYS B 1 132 ? -25.27900 10.08900  32.86400  1.000 82.95995  ? 132 LYS B NZ    1 
ATOM   4484 N  N     . GLU B 1 133 ? -20.06400 13.99600  36.79100  1.000 67.51862  ? 133 GLU B N     1 
ATOM   4485 C  CA    . GLU B 1 133 ? -18.92000 14.89100  36.67200  1.000 68.97932  ? 133 GLU B CA    1 
ATOM   4486 C  C     . GLU B 1 133 ? -17.59000 14.21800  37.00100  1.000 70.16104  ? 133 GLU B C     1 
ATOM   4487 O  O     . GLU B 1 133 ? -16.55100 14.88600  36.95000  1.000 69.72415  ? 133 GLU B O     1 
ATOM   4488 C  CB    . GLU B 1 133 ? -19.12400 16.10600  37.58400  1.000 71.92441  ? 133 GLU B CB    1 
ATOM   4489 C  CG    . GLU B 1 133 ? -20.39300 16.89000  37.28200  1.000 69.87943  ? 133 GLU B CG    1 
ATOM   4490 C  CD    . GLU B 1 133 ? -20.72800 17.90800  38.35600  1.000 74.85371  ? 133 GLU B CD    1 
ATOM   4491 O  OE1   . GLU B 1 133 ? -20.08700 17.88000  39.42900  1.000 60.77834  ? 133 GLU B OE1   1 
ATOM   4492 O  OE2   . GLU B 1 133 ? -21.64500 18.72800  38.13600  1.000 80.32805  ? 133 GLU B OE2   1 
ATOM   4493 N  N     . PHE B 1 134 ? -17.59900 12.92800  37.34300  1.000 62.99440  ? 134 PHE B N     1 
ATOM   4494 C  CA    . PHE B 1 134 ? -16.36900 12.21800  37.68000  1.000 51.07454  ? 134 PHE B CA    1 
ATOM   4495 C  C     . PHE B 1 134 ? -15.35500 12.30300  36.54800  1.000 55.79880  ? 134 PHE B C     1 
ATOM   4496 O  O     . PHE B 1 134 ? -15.71100 12.26300  35.36600  1.000 55.20399  ? 134 PHE B O     1 
ATOM   4497 C  CB    . PHE B 1 134 ? -16.65800 10.74600  37.97100  1.000 56.31728  ? 134 PHE B CB    1 
ATOM   4498 C  CG    . PHE B 1 134 ? -17.12500 10.47700  39.37000  1.000 51.19298  ? 134 PHE B CG    1 
ATOM   4499 C  CD1   . PHE B 1 134 ? -17.16900 11.48800  40.31200  1.000 55.40138  ? 134 PHE B CD1   1 
ATOM   4500 C  CD2   . PHE B 1 134 ? -17.51200 9.20100   39.74200  1.000 47.79257  ? 134 PHE B CD2   1 
ATOM   4501 C  CE1   . PHE B 1 134 ? -17.60500 11.23300  41.59800  1.000 51.66672  ? 134 PHE B CE1   1 
ATOM   4502 C  CE2   . PHE B 1 134 ? -17.94500 8.94000   41.02700  1.000 47.56886  ? 134 PHE B CE2   1 
ATOM   4503 C  CZ    . PHE B 1 134 ? -17.99200 9.95800   41.95700  1.000 45.98972  ? 134 PHE B CZ    1 
ATOM   4504 N  N     . GLU B 1 135 ? -14.08200 12.40800  36.91800  1.000 49.62700  ? 135 GLU B N     1 
ATOM   4505 C  CA    . GLU B 1 135 ? -13.01200 12.34100  35.93300  1.000 60.84677  ? 135 GLU B CA    1 
ATOM   4506 C  C     . GLU B 1 135 ? -12.85700 10.91600  35.41000  1.000 62.34432  ? 135 GLU B C     1 
ATOM   4507 O  O     . GLU B 1 135 ? -12.92800 9.94800   36.17300  1.000 50.65344  ? 135 GLU B O     1 
ATOM   4508 C  CB    . GLU B 1 135 ? -11.70300 12.84000  36.54000  1.000 52.83791  ? 135 GLU B CB    1 
ATOM   4509 C  CG    . GLU B 1 135 ? -10.57100 12.96200  35.54100  1.000 68.54243  ? 135 GLU B CG    1 
ATOM   4510 C  CD    . GLU B 1 135 ? -9.64000  14.11500  35.86700  1.000 78.37255  ? 135 GLU B CD    1 
ATOM   4511 O  OE1   . GLU B 1 135 ? -9.06400  14.11700  36.97700  1.000 94.65609  ? 135 GLU B OE1   1 
ATOM   4512 O  OE2   . GLU B 1 135 ? -9.49400  15.02600  35.02200  1.000 83.18366  ? 135 GLU B OE2   1 
ATOM   4513 N  N     . SER B 1 136 ? -12.65200 10.79100  34.09600  1.000 51.82200  ? 136 SER B N     1 
ATOM   4514 C  CA    . SER B 1 136 ? -12.49000 9.49400   33.44900  1.000 54.75393  ? 136 SER B CA    1 
ATOM   4515 C  C     . SER B 1 136 ? -11.08200 9.21300   32.94200  1.000 51.40616  ? 136 SER B C     1 
ATOM   4516 O  O     . SER B 1 136 ? -10.67700 8.05000   32.92100  1.000 50.80083  ? 136 SER B O     1 
ATOM   4517 C  CB    . SER B 1 136 ? -13.45700 9.36600   32.26400  1.000 65.92369  ? 136 SER B CB    1 
ATOM   4518 O  OG    . SER B 1 136 ? -13.06900 10.22900  31.21100  1.000 70.19526  ? 136 SER B OG    1 
ATOM   4519 N  N     . HIS B 1 137 ? -10.33200 10.24100  32.53900  1.000 59.97035  ? 137 HIS B N     1 
ATOM   4520 C  CA    . HIS B 1 137 ? -9.02500  10.06800  31.89400  1.000 60.15721  ? 137 HIS B CA    1 
ATOM   4521 C  C     . HIS B 1 137 ? -9.11500  9.17300   30.65900  1.000 66.01844  ? 137 HIS B C     1 
ATOM   4522 O  O     . HIS B 1 137 ? -8.19200  8.41100   30.35600  1.000 63.60236  ? 137 HIS B O     1 
ATOM   4523 C  CB    . HIS B 1 137 ? -7.99100  9.51700   32.87700  1.000 55.40664  ? 137 HIS B CB    1 
ATOM   4524 C  CG    . HIS B 1 137 ? -7.67200  10.45100  34.00300  1.000 55.72510  ? 137 HIS B CG    1 
ATOM   4525 N  ND1   . HIS B 1 137 ? -7.12300  11.69900  33.80300  1.000 51.63251  ? 137 HIS B ND1   1 
ATOM   4526 C  CD2   . HIS B 1 137 ? -7.83100  10.31900  35.34200  1.000 59.70189  ? 137 HIS B CD2   1 
ATOM   4527 C  CE1   . HIS B 1 137 ? -6.95500  12.29500  34.97000  1.000 59.84665  ? 137 HIS B CE1   1 
ATOM   4528 N  NE2   . HIS B 1 137 ? -7.37800  11.48000  35.92000  1.000 45.60284  ? 137 HIS B NE2   1 
ATOM   4529 N  N     . LEU B 1 138 ? -10.23400 9.26700   29.93700  1.000 67.75549  ? 138 LEU B N     1 
ATOM   4530 C  CA    . LEU B 1 138 ? -10.44700 8.42800   28.75900  1.000 76.61708  ? 138 LEU B CA    1 
ATOM   4531 C  C     . LEU B 1 138 ? -9.33400  8.60600   27.73200  1.000 72.36657  ? 138 LEU B C     1 
ATOM   4532 O  O     . LEU B 1 138 ? -8.84300  7.62600   27.16100  1.000 84.67068  ? 138 LEU B O     1 
ATOM   4533 C  CB    . LEU B 1 138 ? -11.80700 8.74500   28.13900  1.000 81.94667  ? 138 LEU B CB    1 
ATOM   4534 C  CG    . LEU B 1 138 ? -12.21600 7.95400   26.89800  1.000 99.29612  ? 138 LEU B CG    1 
ATOM   4535 C  CD1   . LEU B 1 138 ? -12.15000 6.46000   27.16100  1.000 98.60656  ? 138 LEU B CD1   1 
ATOM   4536 C  CD2   . LEU B 1 138 ? -13.61000 8.36400   26.46200  1.000 102.40965 ? 138 LEU B CD2   1 
ATOM   4537 N  N     . ASP B 1 139 ? -8.90900  9.84900   27.50000  1.000 71.75597  ? 139 ASP B N     1 
ATOM   4538 C  CA    . ASP B 1 139 ? -7.87800  10.15000  26.51200  1.000 82.41778  ? 139 ASP B CA    1 
ATOM   4539 C  C     . ASP B 1 139 ? -6.51400  9.56300   26.86200  1.000 73.70621  ? 139 ASP B C     1 
ATOM   4540 O  O     . ASP B 1 139 ? -5.60400  9.62500   26.02800  1.000 81.17815  ? 139 ASP B O     1 
ATOM   4541 C  CB    . ASP B 1 139 ? -7.76000  11.66800  26.33100  1.000 86.97359  ? 139 ASP B CB    1 
ATOM   4542 C  CG    . ASP B 1 139 ? -7.38700  12.38500  27.61500  1.000 95.64305  ? 139 ASP B CG    1 
ATOM   4543 O  OD1   . ASP B 1 139 ? -7.97200  12.05700  28.67200  1.000 85.26022  ? 139 ASP B OD1   1 
ATOM   4544 O  OD2   . ASP B 1 139 ? -6.51500  13.27900  27.56800  1.000 104.17828 ? 139 ASP B OD2   1 
ATOM   4545 N  N     . LYS B 1 140 ? -6.34000  9.02500   28.06900  1.000 74.56157  ? 140 LYS B N     1 
ATOM   4546 C  CA    . LYS B 1 140 ? -5.06400  8.47700   28.51400  1.000 71.55068  ? 140 LYS B CA    1 
ATOM   4547 C  C     . LYS B 1 140 ? -4.99000  6.95200   28.43300  1.000 75.82751  ? 140 LYS B C     1 
ATOM   4548 O  O     . LYS B 1 140 ? -3.92100  6.38700   28.69100  1.000 69.37937  ? 140 LYS B O     1 
ATOM   4549 C  CB    . LYS B 1 140 ? -4.77500  8.95000   29.94200  1.000 67.39755  ? 140 LYS B CB    1 
ATOM   4550 C  CG    . LYS B 1 140 ? -4.98100  10.45400  30.10100  1.000 72.68766  ? 140 LYS B CG    1 
ATOM   4551 C  CD    . LYS B 1 140 ? -3.82300  11.12800  30.80300  1.000 72.00337  ? 140 LYS B CD    1 
ATOM   4552 C  CE    . LYS B 1 140 ? -4.01400  12.63300  30.86000  1.000 68.42136  ? 140 LYS B CE    1 
ATOM   4553 N  NZ    . LYS B 1 140 ? -5.24400  13.02300  31.59700  1.000 78.67522  ? 140 LYS B NZ    1 
ATOM   4554 N  N     . LEU B 1 141 ? -6.09700  6.28000   28.11200  1.000 66.32637  ? 141 LEU B N     1 
ATOM   4555 C  CA    . LEU B 1 141 ? -6.11800  4.82400   27.99900  1.000 79.21213  ? 141 LEU B CA    1 
ATOM   4556 C  C     . LEU B 1 141 ? -5.24000  4.34400   26.84200  1.000 74.57210  ? 141 LEU B C     1 
ATOM   4557 O  O     . LEU B 1 141 ? -5.24800  4.92200   25.75100  1.000 92.47951  ? 141 LEU B O     1 
ATOM   4558 C  CB    . LEU B 1 141 ? -7.55900  4.34800   27.80500  1.000 87.12360  ? 141 LEU B CB    1 
ATOM   4559 C  CG    . LEU B 1 141 ? -8.51600  4.67200   28.95900  1.000 86.30508  ? 141 LEU B CG    1 
ATOM   4560 C  CD1   . LEU B 1 141 ? -9.85100  3.97500   28.77400  1.000 89.59495  ? 141 LEU B CD1   1 
ATOM   4561 C  CD2   . LEU B 1 141 ? -7.90200  4.30700   30.29900  1.000 79.25424  ? 141 LEU B CD2   1 
ATOM   4562 N  N     . ASP B 1 142 ? -4.47300  3.28000   27.09100  1.000 96.22206  ? 142 ASP B N     1 
ATOM   4563 C  CA    . ASP B 1 142 ? -3.53700  2.69700   26.12500  1.000 108.04453 ? 142 ASP B CA    1 
ATOM   4564 C  C     . ASP B 1 142 ? -4.07200  1.46500   25.39300  1.000 128.13115 ? 142 ASP B C     1 
ATOM   4565 O  O     . ASP B 1 142 ? -3.34200  0.47800   25.25700  1.000 126.99681 ? 142 ASP B O     1 
ATOM   4566 C  CB    . ASP B 1 142 ? -2.22500  2.35500   26.82700  1.000 107.57342 ? 142 ASP B CB    1 
ATOM   4567 C  CG    . ASP B 1 142 ? -2.40100  1.32000   27.92700  1.000 122.30677 ? 142 ASP B CG    1 
ATOM   4568 O  OD1   . ASP B 1 142 ? -3.55100  0.89400   28.17600  1.000 140.60633 ? 142 ASP B OD1   1 
ATOM   4569 O  OD2   . ASP B 1 142 ? -1.38800  0.92700   28.54100  1.000 109.63946 ? 142 ASP B OD2   1 
ATOM   4570 N  N     . ASN B 1 143 ? -5.31800  1.47800   24.91300  1.000 143.13032 ? 143 ASN B N     1 
ATOM   4571 C  CA    . ASN B 1 143 ? -5.94200  0.33200   24.24600  1.000 137.72967 ? 143 ASN B CA    1 
ATOM   4572 C  C     . ASN B 1 143 ? -6.07000  -0.89400  25.14500  1.000 112.76089 ? 143 ASN B C     1 
ATOM   4573 O  O     . ASN B 1 143 ? -7.13300  -1.52100  25.21000  1.000 161.99048 ? 143 ASN B O     1 
ATOM   4574 C  CB    . ASN B 1 143 ? -5.13700  -0.10100  23.01000  1.000 125.53874 ? 143 ASN B CB    1 
ATOM   4575 C  CG    . ASN B 1 143 ? -5.01100  0.98400   21.96800  1.000 123.75694 ? 143 ASN B CG    1 
ATOM   4576 O  OD1   . ASN B 1 143 ? -5.85300  1.87100   21.86300  1.000 135.42940 ? 143 ASN B OD1   1 
ATOM   4577 N  ND2   . ASN B 1 143 ? -3.93800  0.91900   21.18900  1.000 120.58551 ? 143 ASN B ND2   1 
ATOM   4578 N  N     . GLU B 1 144 ? -4.98000  -1.25100  25.82500  1.000 105.69162 ? 144 GLU B N     1 
ATOM   4579 C  CA    . GLU B 1 144 ? -4.95300  -2.46000  26.64000  1.000 109.44470 ? 144 GLU B CA    1 
ATOM   4580 C  C     . GLU B 1 144 ? -5.81400  -2.30900  27.88400  1.000 108.22350 ? 144 GLU B C     1 
ATOM   4581 O  O     . GLU B 1 144 ? -6.44200  -3.27500  28.33700  1.000 89.66865  ? 144 GLU B O     1 
ATOM   4582 C  CB    . GLU B 1 144 ? -3.50600  -2.79400  26.97700  1.000 117.26669 ? 144 GLU B CB    1 
ATOM   4583 C  CG    . GLU B 1 144 ? -2.66000  -2.84800  25.71200  1.000 124.95182 ? 144 GLU B CG    1 
ATOM   4584 C  CD    . GLU B 1 144 ? -1.20400  -2.53500  25.95800  1.000 148.46517 ? 144 GLU B CD    1 
ATOM   4585 O  OE1   . GLU B 1 144 ? -0.84600  -2.25000  27.12000  1.000 126.15986 ? 144 GLU B OE1   1 
ATOM   4586 O  OE2   . GLU B 1 144 ? -0.41700  -2.57300  24.98800  1.000 169.58875 ? 144 GLU B OE2   1 
ATOM   4587 N  N     . LYS B 1 145 ? -5.84900  -1.10600  28.45000  1.000 88.88434  ? 145 LYS B N     1 
ATOM   4588 C  CA    . LYS B 1 145 ? -6.78200  -0.84200  29.53200  1.000 96.58790  ? 145 LYS B CA    1 
ATOM   4589 C  C     . LYS B 1 145 ? -8.20700  -0.79500  28.99200  1.000 86.07874  ? 145 LYS B C     1 
ATOM   4590 O  O     . LYS B 1 145 ? -9.15200  -1.18300  29.68700  1.000 67.75023  ? 145 LYS B O     1 
ATOM   4591 C  CB    . LYS B 1 145 ? -6.40000  0.46200   30.23100  1.000 95.43249  ? 145 LYS B CB    1 
ATOM   4592 C  CG    . LYS B 1 145 ? -5.19600  0.34700   31.15800  1.000 102.09382 ? 145 LYS B CG    1 
ATOM   4593 C  CD    . LYS B 1 145 ? -4.61500  1.72000   31.45000  1.000 113.55046 ? 145 LYS B CD    1 
ATOM   4594 C  CE    . LYS B 1 145 ? -3.94900  1.74300   32.81700  1.000 101.27530 ? 145 LYS B CE    1 
ATOM   4595 N  NZ    . LYS B 1 145 ? -3.10200  2.95000   33.00400  1.000 112.84774 ? 145 LYS B NZ    1 
ATOM   4596 N  N     . LYS B 1 146 ? -8.36400  -0.39000  27.72700  1.000 78.32781  ? 146 LYS B N     1 
ATOM   4597 C  CA    . LYS B 1 146 ? -9.66600  -0.46200  27.07100  1.000 84.66278  ? 146 LYS B CA    1 
ATOM   4598 C  C     . LYS B 1 146 ? -10.07700 -1.91100  26.84300  1.000 83.94428  ? 146 LYS B C     1 
ATOM   4599 O  O     . LYS B 1 146 ? -11.26500 -2.24600  26.92300  1.000 89.70549  ? 146 LYS B O     1 
ATOM   4600 C  CB    . LYS B 1 146 ? -9.63500  0.28800   25.74100  1.000 76.64077  ? 146 LYS B CB    1 
ATOM   4601 C  CG    . LYS B 1 146 ? -9.52700  1.79600   25.84600  1.000 86.80778  ? 146 LYS B CG    1 
ATOM   4602 C  CD    . LYS B 1 146 ? -8.90400  2.37400   24.58100  1.000 93.22170  ? 146 LYS B CD    1 
ATOM   4603 C  CE    . LYS B 1 146 ? -9.15400  3.86500   24.45800  1.000 95.16404  ? 146 LYS B CE    1 
ATOM   4604 N  NZ    . LYS B 1 146 ? -10.55500 4.13800   24.04500  1.000 98.51444  ? 146 LYS B NZ    1 
ATOM   4605 N  N     . ASP B 1 147 ? -9.11300  -2.78000  26.52100  1.000 82.82835  ? 147 ASP B N     1 
ATOM   4606 C  CA    . ASP B 1 147 ? -9.42600  -4.19700  26.36400  1.000 96.88530  ? 147 ASP B CA    1 
ATOM   4607 C  C     . ASP B 1 147 ? -10.02100 -4.77000  27.64200  1.000 74.86161  ? 147 ASP B C     1 
ATOM   4608 O  O     . ASP B 1 147 ? -10.90000 -5.63800  27.58500  1.000 76.88817  ? 147 ASP B O     1 
ATOM   4609 C  CB    . ASP B 1 147 ? -8.16300  -4.97900  25.99400  1.000 102.13067 ? 147 ASP B CB    1 
ATOM   4610 C  CG    . ASP B 1 147 ? -7.71100  -4.73700  24.56500  1.000 114.03999 ? 147 ASP B CG    1 
ATOM   4611 O  OD1   . ASP B 1 147 ? -8.40800  -4.01400  23.82300  1.000 106.54962 ? 147 ASP B OD1   1 
ATOM   4612 O  OD2   . ASP B 1 147 ? -6.64200  -5.26200  24.18900  1.000 98.74868  ? 147 ASP B OD2   1 
ATOM   4613 N  N     . LEU B 1 148 ? -9.56100  -4.28700  28.79900  1.000 87.01043  ? 148 LEU B N     1 
ATOM   4614 C  CA    . LEU B 1 148 ? -10.11100 -4.73300  30.07400  1.000 78.43046  ? 148 LEU B CA    1 
ATOM   4615 C  C     . LEU B 1 148 ? -11.49200 -4.13900  30.32500  1.000 79.22002  ? 148 LEU B C     1 
ATOM   4616 O  O     . LEU B 1 148 ? -12.39500 -4.83600  30.80000  1.000 87.75526  ? 148 LEU B O     1 
ATOM   4617 C  CB    . LEU B 1 148 ? -9.13800  -4.37300  31.19300  1.000 74.80107  ? 148 LEU B CB    1 
ATOM   4618 C  CG    . LEU B 1 148 ? -7.87000  -5.23200  31.15900  1.000 83.70214  ? 148 LEU B CG    1 
ATOM   4619 C  CD1   . LEU B 1 148 ? -6.78400  -4.67100  32.06200  1.000 70.81112  ? 148 LEU B CD1   1 
ATOM   4620 C  CD2   . LEU B 1 148 ? -8.19200  -6.67200  31.53600  1.000 80.51755  ? 148 LEU B CD2   1 
ATOM   4621 N  N     . ILE B 1 149 ? -11.67400 -2.85100  30.01900  1.000 75.81962  ? 149 ILE B N     1 
ATOM   4622 C  CA    . ILE B 1 149 ? -12.98800 -2.22500  30.15300  1.000 71.80071  ? 149 ILE B CA    1 
ATOM   4623 C  C     . ILE B 1 149 ? -13.99800 -2.88300  29.22000  1.000 79.32004  ? 149 ILE B C     1 
ATOM   4624 O  O     . ILE B 1 149 ? -15.13900 -3.15900  29.61100  1.000 77.80933  ? 149 ILE B O     1 
ATOM   4625 C  CB    . ILE B 1 149 ? -12.88800 -0.71000  29.89700  1.000 72.20866  ? 149 ILE B CB    1 
ATOM   4626 C  CG1   . ILE B 1 149 ? -12.13000 -0.02100  31.03000  1.000 62.86017  ? 149 ILE B CG1   1 
ATOM   4627 C  CG2   . ILE B 1 149 ? -14.27100 -0.10100  29.76400  1.000 69.73468  ? 149 ILE B CG2   1 
ATOM   4628 C  CD1   . ILE B 1 149 ? -11.92300 1.45800   30.80300  1.000 64.52089  ? 149 ILE B CD1   1 
ATOM   4629 N  N     . GLN B 1 150 ? -13.60400 -3.12900  27.96700  1.000 74.17205  ? 150 GLN B N     1 
ATOM   4630 C  CA    . GLN B 1 150 ? -14.51100 -3.79700  27.04100  1.000 81.11762  ? 150 GLN B CA    1 
ATOM   4631 C  C     . GLN B 1 150 ? -14.84300 -5.20600  27.51100  1.000 80.39911  ? 150 GLN B C     1 
ATOM   4632 O  O     . GLN B 1 150 ? -15.96400 -5.68200  27.30400  1.000 77.60931  ? 150 GLN B O     1 
ATOM   4633 C  CB    . GLN B 1 150 ? -13.90800 -3.82500  25.63700  1.000 87.23678  ? 150 GLN B CB    1 
ATOM   4634 C  CG    . GLN B 1 150 ? -13.95200 -2.48500  24.91900  1.000 88.63694  ? 150 GLN B CG    1 
ATOM   4635 C  CD    . GLN B 1 150 ? -15.36900 -2.02400  24.63800  1.000 95.24300  ? 150 GLN B CD    1 
ATOM   4636 O  OE1   . GLN B 1 150 ? -16.29400 -2.83300  24.55300  1.000 91.23462  ? 150 GLN B OE1   1 
ATOM   4637 N  NE2   . GLN B 1 150 ? -15.54600 -0.71700  24.49100  1.000 94.12708  ? 150 GLN B NE2   1 
ATOM   4638 N  N     . SER B 1 151 ? -13.89200 -5.87900  28.16200  1.000 85.18653  ? 151 SER B N     1 
ATOM   4639 C  CA    . SER B 1 151 ? -14.19100 -7.17100  28.76900  1.000 80.44122  ? 151 SER B CA    1 
ATOM   4640 C  C     . SER B 1 151 ? -15.19500 -7.02100  29.90600  1.000 75.07216  ? 151 SER B C     1 
ATOM   4641 O  O     . SER B 1 151 ? -16.10800 -7.84400  30.04600  1.000 68.38978  ? 151 SER B O     1 
ATOM   4642 C  CB    . SER B 1 151 ? -12.90400 -7.82200  29.27200  1.000 78.53310  ? 151 SER B CB    1 
ATOM   4643 O  OG    . SER B 1 151 ? -13.07900 -9.21400  29.45000  1.000 88.14741  ? 151 SER B OG    1 
ATOM   4644 N  N     . ASP B 1 152 ? -15.04000 -5.97700  30.72700  1.000 74.56420  ? 152 ASP B N     1 
ATOM   4645 C  CA    . ASP B 1 152 ? -16.00700 -5.70600  31.78900  1.000 75.61433  ? 152 ASP B CA    1 
ATOM   4646 C  C     . ASP B 1 152 ? -17.38700 -5.40100  31.22100  1.000 75.79856  ? 152 ASP B C     1 
ATOM   4647 O  O     . ASP B 1 152 ? -18.40400 -5.83400  31.77400  1.000 78.97526  ? 152 ASP B O     1 
ATOM   4648 C  CB    . ASP B 1 152 ? -15.52700 -4.54200  32.65900  1.000 86.16033  ? 152 ASP B CB    1 
ATOM   4649 C  CG    . ASP B 1 152 ? -14.42400 -4.94100  33.62200  1.000 94.02443  ? 152 ASP B CG    1 
ATOM   4650 O  OD1   . ASP B 1 152 ? -14.08400 -6.14300  33.68400  1.000 97.48274  ? 152 ASP B OD1   1 
ATOM   4651 O  OD2   . ASP B 1 152 ? -13.90200 -4.04800  34.32600  1.000 80.64125  ? 152 ASP B OD2   1 
ATOM   4652 N  N     . ILE B 1 153 ? -17.44500 -4.63300  30.13100  1.000 65.82105  ? 153 ILE B N     1 
ATOM   4653 C  CA    . ILE B 1 153 ? -18.72700 -4.34200  29.49100  1.000 69.62677  ? 153 ILE B CA    1 
ATOM   4654 C  C     . ILE B 1 153 ? -19.39100 -5.63100  29.01400  1.000 71.60069  ? 153 ILE B C     1 
ATOM   4655 O  O     . ILE B 1 153 ? -20.60300 -5.82200  29.18000  1.000 67.45546  ? 153 ILE B O     1 
ATOM   4656 C  CB    . ILE B 1 153 ? -18.53400 -3.32800  28.34800  1.000 71.40067  ? 153 ILE B CB    1 
ATOM   4657 C  CG1   . ILE B 1 153 ? -18.14100 -1.96500  28.92300  1.000 67.24227  ? 153 ILE B CG1   1 
ATOM   4658 C  CG2   . ILE B 1 153 ? -19.79900 -3.20300  27.51500  1.000 73.59830  ? 153 ILE B CG2   1 
ATOM   4659 C  CD1   . ILE B 1 153 ? -17.72500 -0.94900  27.88800  1.000 67.29491  ? 153 ILE B CD1   1 
ATOM   4660 N  N     . ALA B 1 154 ? -18.60800 -6.53900  28.42000  1.000 78.92788  ? 154 ALA B N     1 
ATOM   4661 C  CA    . ALA B 1 154 ? -19.15600 -7.82900  28.01200  1.000 86.90779  ? 154 ALA B CA    1 
ATOM   4662 C  C     . ALA B 1 154 ? -19.70600 -8.59700  29.20800  1.000 80.17803  ? 154 ALA B C     1 
ATOM   4663 O  O     . ALA B 1 154 ? -20.78900 -9.18900  29.12900  1.000 84.21273  ? 154 ALA B O     1 
ATOM   4664 C  CB    . ALA B 1 154 ? -18.08800 -8.64900  27.28800  1.000 84.73911  ? 154 ALA B CB    1 
ATOM   4665 N  N     . ALA B 1 155 ? -18.98100 -8.58800  30.33000  1.000 67.41598  ? 155 ALA B N     1 
ATOM   4666 C  CA    . ALA B 1 155 ? -19.48100 -9.24500  31.53200  1.000 65.80789  ? 155 ALA B CA    1 
ATOM   4667 C  C     . ALA B 1 155 ? -20.74500 -8.56600  32.03600  1.000 67.60021  ? 155 ALA B C     1 
ATOM   4668 O  O     . ALA B 1 155 ? -21.68700 -9.23600  32.47800  1.000 66.03423  ? 155 ALA B O     1 
ATOM   4669 C  CB    . ALA B 1 155 ? -18.40600 -9.25400  32.61600  1.000 70.58478  ? 155 ALA B CB    1 
ATOM   4670 N  N     . LEU B 1 156 ? -20.77800 -7.23200  31.98600  1.000 61.71793  ? 156 LEU B N     1 
ATOM   4671 C  CA    . LEU B 1 156 ? -21.97300 -6.50100  32.39400  1.000 64.85251  ? 156 LEU B CA    1 
ATOM   4672 C  C     . LEU B 1 156 ? -23.18300 -6.91900  31.56700  1.000 65.61313  ? 156 LEU B C     1 
ATOM   4673 O  O     . LEU B 1 156 ? -24.27100 -7.13200  32.11300  1.000 66.23426  ? 156 LEU B O     1 
ATOM   4674 C  CB    . LEU B 1 156 ? -21.73500 -4.99200  32.28200  1.000 63.07862  ? 156 LEU B CB    1 
ATOM   4675 C  CG    . LEU B 1 156 ? -22.83200 -4.06300  32.81600  1.000 62.43907  ? 156 LEU B CG    1 
ATOM   4676 C  CD1   . LEU B 1 156 ? -23.00800 -4.23900  34.31600  1.000 64.05768  ? 156 LEU B CD1   1 
ATOM   4677 C  CD2   . LEU B 1 156 ? -22.52200 -2.61500  32.48400  1.000 60.58884  ? 156 LEU B CD2   1 
ATOM   4678 N  N     . HIS B 1 157 ? -23.01700 -7.03400  30.24500  1.000 78.02778  ? 157 HIS B N     1 
ATOM   4679 C  CA    . HIS B 1 157 ? -24.12900 -7.45300  29.39400  1.000 82.88625  ? 157 HIS B CA    1 
ATOM   4680 C  C     . HIS B 1 157 ? -24.56500 -8.87600  29.72400  1.000 87.24467  ? 157 HIS B C     1 
ATOM   4681 O  O     . HIS B 1 157 ? -25.76100 -9.16100  29.85400  1.000 86.02347  ? 157 HIS B O     1 
ATOM   4682 C  CB    . HIS B 1 157 ? -23.75300 -7.36500  27.91400  1.000 88.52114  ? 157 HIS B CB    1 
ATOM   4683 C  CG    . HIS B 1 157 ? -23.57000 -5.97000  27.40500  1.000 88.50798  ? 157 HIS B CG    1 
ATOM   4684 N  ND1   . HIS B 1 157 ? -24.51000 -4.98000  27.59100  1.000 104.41515 ? 157 HIS B ND1   1 
ATOM   4685 C  CD2   . HIS B 1 157 ? -22.61800 -5.43600  26.60300  1.000 89.47125  ? 157 HIS B CD2   1 
ATOM   4686 C  CE1   . HIS B 1 157 ? -24.10100 -3.87100  27.00100  1.000 94.56134  ? 157 HIS B CE1   1 
ATOM   4687 N  NE2   . HIS B 1 157 ? -22.96200 -4.12400  26.38300  1.000 87.33942  ? 157 HIS B NE2   1 
ATOM   4688 N  N     . HIS B 1 158 ? -23.59200 -9.78400  29.85100  1.000 93.45594  ? 158 HIS B N     1 
ATOM   4689 C  CA    . HIS B 1 158 ? -23.88100 -11.20100 30.05700  1.000 88.16583  ? 158 HIS B CA    1 
ATOM   4690 C  C     . HIS B 1 158 ? -24.73400 -11.43800 31.29700  1.000 83.62055  ? 158 HIS B C     1 
ATOM   4691 O  O     . HIS B 1 158 ? -25.75700 -12.13300 31.23700  1.000 83.03364  ? 158 HIS B O     1 
ATOM   4692 C  CB    . HIS B 1 158 ? -22.56800 -11.97600 30.16600  1.000 89.57390  ? 158 HIS B CB    1 
ATOM   4693 C  CG    . HIS B 1 158 ? -22.74900 -13.45400 30.31300  1.000 106.54172 ? 158 HIS B CG    1 
ATOM   4694 N  ND1   . HIS B 1 158 ? -22.57700 -14.33400 29.26600  1.000 105.59950 ? 158 HIS B ND1   1 
ATOM   4695 C  CD2   . HIS B 1 158 ? -23.09000 -14.20800 31.38500  1.000 102.87812 ? 158 HIS B CD2   1 
ATOM   4696 C  CE1   . HIS B 1 158 ? -22.80200 -15.56500 29.68700  1.000 104.07300 ? 158 HIS B CE1   1 
ATOM   4697 N  NE2   . HIS B 1 158 ? -23.11400 -15.51700 30.97000  1.000 116.08234 ? 158 HIS B NE2   1 
ATOM   4698 N  N     . PHE B 1 159 ? -24.34200 -10.85600 32.42700  1.000 76.10649  ? 159 PHE B N     1 
ATOM   4699 C  CA    . PHE B 1 159 ? -24.92900 -11.22200 33.70700  1.000 71.22959  ? 159 PHE B CA    1 
ATOM   4700 C  C     . PHE B 1 159 ? -26.07500 -10.31400 34.12200  1.000 74.48525  ? 159 PHE B C     1 
ATOM   4701 O  O     . PHE B 1 159 ? -26.82700 -10.67400 35.03500  1.000 79.20950  ? 159 PHE B O     1 
ATOM   4702 C  CB    . PHE B 1 159 ? -23.85800 -11.21100 34.80500  1.000 65.73420  ? 159 PHE B CB    1 
ATOM   4703 C  CG    . PHE B 1 159 ? -22.85000 -12.32300 34.68600  1.000 62.67330  ? 159 PHE B CG    1 
ATOM   4704 C  CD1   . PHE B 1 159 ? -23.24300 -13.64900 34.79500  1.000 63.64447  ? 159 PHE B CD1   1 
ATOM   4705 C  CD2   . PHE B 1 159 ? -21.50800 -12.04300 34.48200  1.000 62.56013  ? 159 PHE B CD2   1 
ATOM   4706 C  CE1   . PHE B 1 159 ? -22.31900 -14.67500 34.69000  1.000 60.67043  ? 159 PHE B CE1   1 
ATOM   4707 C  CE2   . PHE B 1 159 ? -20.57700 -13.06400 34.38000  1.000 62.42591  ? 159 PHE B CE2   1 
ATOM   4708 C  CZ    . PHE B 1 159 ? -20.98300 -14.38200 34.48500  1.000 60.28354  ? 159 PHE B CZ    1 
ATOM   4709 N  N     . TYR B 1 160 ? -26.24000 -9.16100  33.47000  1.000 80.99129  ? 160 TYR B N     1 
ATOM   4710 C  CA    . TYR B 1 160 ? -27.21100 -8.16600  33.90700  1.000 83.23366  ? 160 TYR B CA    1 
ATOM   4711 C  C     . TYR B 1 160 ? -28.12500 -7.70500  32.77500  1.000 88.44218  ? 160 TYR B C     1 
ATOM   4712 O  O     . TYR B 1 160 ? -28.72200 -6.62800  32.87900  1.000 88.47113  ? 160 TYR B O     1 
ATOM   4713 C  CB    . TYR B 1 160 ? -26.50100 -6.96200  34.53200  1.000 78.48046  ? 160 TYR B CB    1 
ATOM   4714 C  CG    . TYR B 1 160 ? -25.68200 -7.29400  35.76500  1.000 71.29013  ? 160 TYR B CG    1 
ATOM   4715 C  CD1   . TYR B 1 160 ? -24.34800 -7.66200  35.65600  1.000 63.82081  ? 160 TYR B CD1   1 
ATOM   4716 C  CD2   . TYR B 1 160 ? -26.24300 -7.23300  37.03600  1.000 68.60823  ? 160 TYR B CD2   1 
ATOM   4717 C  CE1   . TYR B 1 160 ? -23.59400 -7.96400  36.77600  1.000 62.16272  ? 160 TYR B CE1   1 
ATOM   4718 C  CE2   . TYR B 1 160 ? -25.49500 -7.53100  38.16400  1.000 65.13149  ? 160 TYR B CE2   1 
ATOM   4719 C  CZ    . TYR B 1 160 ? -24.17300 -7.89800  38.02600  1.000 58.78073  ? 160 TYR B CZ    1 
ATOM   4720 O  OH    . TYR B 1 160 ? -23.42400 -8.19600  39.14000  1.000 65.29993  ? 160 TYR B OH    1 
ATOM   4721 N  N     . SER B 1 161 ? -28.24500 -8.48800  31.69400  1.000 97.41168  ? 161 SER B N     1 
ATOM   4722 C  CA    . SER B 1 161 ? -29.09800 -8.07600  30.57900  1.000 96.32471  ? 161 SER B CA    1 
ATOM   4723 C  C     . SER B 1 161 ? -30.52800 -7.85600  31.04900  1.000 95.04297  ? 161 SER B C     1 
ATOM   4724 O  O     . SER B 1 161 ? -31.20900 -6.93000  30.59500  1.000 97.24061  ? 161 SER B O     1 
ATOM   4725 C  CB    . SER B 1 161 ? -29.05800 -9.11800  29.46300  1.000 97.83015  ? 161 SER B CB    1 
ATOM   4726 O  OG    . SER B 1 161 ? -27.92600 -8.93300  28.63400  1.000 104.53095 ? 161 SER B OG    1 
ATOM   4727 N  N     . LYS B 1 162 ? -31.00600 -8.71900  31.93400  1.000 90.69772  ? 162 LYS B N     1 
ATOM   4728 C  CA    . LYS B 1 162 ? -32.29700 -8.52400  32.56200  1.000 93.83230  ? 162 LYS B CA    1 
ATOM   4729 C  C     . LYS B 1 162 ? -32.12100 -7.54500  33.72000  1.000 113.94787 ? 162 LYS B C     1 
ATOM   4730 O  O     . LYS B 1 162 ? -31.05300 -7.48500  34.33900  1.000 109.23152 ? 162 LYS B O     1 
ATOM   4731 C  CB    . LYS B 1 162 ? -32.85400 -9.85900  33.06200  1.000 98.18019  ? 162 LYS B CB    1 
ATOM   4732 C  CG    . LYS B 1 162 ? -33.17500 -10.85500 31.94700  1.000 111.35019 ? 162 LYS B CG    1 
ATOM   4733 C  CD    . LYS B 1 162 ? -34.08400 -11.98300 32.41700  1.000 107.79977 ? 162 LYS B CD    1 
ATOM   4734 C  CE    . LYS B 1 162 ? -34.57500 -12.82000 31.24400  1.000 121.70143 ? 162 LYS B CE    1 
ATOM   4735 N  NZ    . LYS B 1 162 ? -35.13100 -11.99500 30.13700  1.000 134.62667 ? 162 LYS B NZ    1 
ATOM   4736 N  N     . HIS B 1 163 ? -33.16400 -6.74800  33.97000  1.000 133.58444 ? 163 HIS B N     1 
ATOM   4737 C  CA    . HIS B 1 163 ? -33.28700 -5.76500  35.05100  1.000 136.87431 ? 163 HIS B CA    1 
ATOM   4738 C  C     . HIS B 1 163 ? -32.70400 -4.38300  34.75500  1.000 121.84092 ? 163 HIS B C     1 
ATOM   4739 O  O     . HIS B 1 163 ? -33.18400 -3.39300  35.31600  1.000 149.68637 ? 163 HIS B O     1 
ATOM   4740 C  CB    . HIS B 1 163 ? -32.62000 -6.26600  36.34000  1.000 127.76795 ? 163 HIS B CB    1 
ATOM   4741 C  CG    . HIS B 1 163 ? -33.18400 -7.54700  36.86600  1.000 149.92850 ? 163 HIS B CG    1 
ATOM   4742 N  ND1   . HIS B 1 163 ? -34.26300 -7.59400  37.72100  1.000 163.31432 ? 163 HIS B ND1   1 
ATOM   4743 C  CD2   . HIS B 1 163 ? -32.79600 -8.83100  36.67800  1.000 157.54521 ? 163 HIS B CD2   1 
ATOM   4744 C  CE1   . HIS B 1 163 ? -34.52700 -8.85300  38.02400  1.000 156.22136 ? 163 HIS B CE1   1 
ATOM   4745 N  NE2   . HIS B 1 163 ? -33.65000 -9.62300  37.40500  1.000 169.43874 ? 163 HIS B NE2   1 
ATOM   4746 N  N     . LEU B 1 164 ? -31.65800 -4.31500  33.92800  1.000 99.56457  ? 164 LEU B N     1 
ATOM   4747 C  CA    . LEU B 1 164 ? -31.01600 -2.99600  33.68400  1.000 101.98591 ? 164 LEU B CA    1 
ATOM   4748 C  C     . LEU B 1 164 ? -30.91100 -2.68600  32.18800  1.000 111.75814 ? 164 LEU B C     1 
ATOM   4749 O  O     . LEU B 1 164 ? -30.64700 -3.61300  31.39700  1.000 130.51828 ? 164 LEU B O     1 
ATOM   4750 C  CB    . LEU B 1 164 ? -29.63300 -2.98800  34.34500  1.000 89.32124  ? 164 LEU B CB    1 
ATOM   4751 C  CG    . LEU B 1 164 ? -28.46400 -3.34200  33.42700  1.000 88.97383  ? 164 LEU B CG    1 
ATOM   4752 C  CD1   . LEU B 1 164 ? -28.00400 -2.12300  32.64100  1.000 73.84043  ? 164 LEU B CD1   1 
ATOM   4753 C  CD2   . LEU B 1 164 ? -27.30900 -3.92900  34.22300  1.000 105.64425 ? 164 LEU B CD2   1 
ATOM   4754 N  N     . GLU B 1 165 ? -31.11400 -1.41100  31.84200  1.000 130.51038 ? 165 GLU B N     1 
ATOM   4755 C  CA    . GLU B 1 165 ? -30.99800 -0.91400  30.47500  1.000 117.17194 ? 165 GLU B CA    1 
ATOM   4756 C  C     . GLU B 1 165 ? -29.67500 -0.17300  30.29900  1.000 98.67236  ? 165 GLU B C     1 
ATOM   4757 O  O     . GLU B 1 165 ? -29.38300 0.76900   31.04400  1.000 102.31753 ? 165 GLU B O     1 
ATOM   4758 C  CB    . GLU B 1 165 ? -32.17800 0.00300   30.14900  1.000 125.57295 ? 165 GLU B CB    1 
ATOM   4759 C  CG    . GLU B 1 165 ? -32.39500 0.28200   28.67400  1.000 143.86462 ? 165 GLU B CG    1 
ATOM   4760 C  CD    . GLU B 1 165 ? -33.54500 1.24200   28.43400  1.000 144.71472 ? 165 GLU B CD    1 
ATOM   4761 O  OE1   . GLU B 1 165 ? -33.59800 2.28600   29.12000  1.000 143.73565 ? 165 GLU B OE1   1 
ATOM   4762 O  OE2   . GLU B 1 165 ? -34.40100 0.94800   27.57100  1.000 124.17541 ? 165 GLU B OE2   1 
ATOM   4763 N  N     . PHE B 1 166 ? -28.88400 -0.58700  29.30500  1.000 82.15459  ? 166 PHE B N     1 
ATOM   4764 C  CA    . PHE B 1 166 ? -27.52700 -0.08800  29.11100  1.000 79.63060  ? 166 PHE B CA    1 
ATOM   4765 C  C     . PHE B 1 166 ? -27.54800 1.19800   28.29000  1.000 83.25472  ? 166 PHE B C     1 
ATOM   4766 O  O     . PHE B 1 166 ? -28.29400 1.29700   27.31400  1.000 87.00780  ? 166 PHE B O     1 
ATOM   4767 C  CB    . PHE B 1 166 ? -26.67600 -1.10500  28.35600  1.000 81.11236  ? 166 PHE B CB    1 
ATOM   4768 C  CG    . PHE B 1 166 ? -26.80800 -2.50800  28.85300  1.000 87.48944  ? 166 PHE B CG    1 
ATOM   4769 C  CD1   . PHE B 1 166 ? -26.40100 -2.85200  30.12400  1.000 100.53311 ? 166 PHE B CD1   1 
ATOM   4770 C  CD2   . PHE B 1 166 ? -27.34100 -3.48700  28.03300  1.000 92.43214  ? 166 PHE B CD2   1 
ATOM   4771 C  CE1   . PHE B 1 166 ? -26.52800 -4.14900  30.57300  1.000 109.48418 ? 166 PHE B CE1   1 
ATOM   4772 C  CE2   . PHE B 1 166 ? -27.47100 -4.78400  28.47500  1.000 86.15507  ? 166 PHE B CE2   1 
ATOM   4773 C  CZ    . PHE B 1 166 ? -27.06400 -5.11600  29.74500  1.000 90.79510  ? 166 PHE B CZ    1 
ATOM   4774 N  N     . PRO B 1 167 ? -26.73800 2.19700   28.62200  1.000 103.95457 ? 167 PRO B N     1 
ATOM   4775 C  CA    . PRO B 1 167 ? -26.46800 3.26600   27.64700  1.000 106.89440 ? 167 PRO B CA    1 
ATOM   4776 C  C     . PRO B 1 167 ? -25.66900 2.73800   26.46300  1.000 105.19419 ? 167 PRO B C     1 
ATOM   4777 O  O     . PRO B 1 167 ? -25.37500 1.54100   26.41100  1.000 89.89236  ? 167 PRO B O     1 
ATOM   4778 C  CB    . PRO B 1 167 ? -25.66300 4.28700   28.46000  1.000 106.09167 ? 167 PRO B CB    1 
ATOM   4779 C  CG    . PRO B 1 167 ? -26.03600 4.01900   29.89100  1.000 107.46552 ? 167 PRO B CG    1 
ATOM   4780 C  CD    . PRO B 1 167 ? -26.25400 2.53700   29.97300  1.000 108.34194 ? 167 PRO B CD    1 
ATOM   4781 N  N     . ASP B 1 168 ? -25.29500 3.60400   25.52100  1.000 125.35977 ? 168 ASP B N     1 
ATOM   4782 C  CA    . ASP B 1 168 ? -24.43700 3.18000   24.42600  1.000 130.44722 ? 168 ASP B CA    1 
ATOM   4783 C  C     . ASP B 1 168 ? -23.04500 2.81400   24.94900  1.000 123.34110 ? 168 ASP B C     1 
ATOM   4784 O  O     . ASP B 1 168 ? -22.67300 3.11400   26.09700  1.000 123.69904 ? 168 ASP B O     1 
ATOM   4785 C  CB    . ASP B 1 168 ? -24.33800 4.27100   23.35800  1.000 132.20269 ? 168 ASP B CB    1 
ATOM   4786 C  CG    . ASP B 1 168 ? -24.03000 5.64000   23.93700  1.000 126.49938 ? 168 ASP B CG    1 
ATOM   4787 O  OD1   . ASP B 1 168 ? -24.09200 5.79900   25.17100  1.000 121.33297 ? 168 ASP B OD1   1 
ATOM   4788 O  OD2   . ASP B 1 168 ? -23.78000 6.57300   23.14100  1.000 122.19886 ? 168 ASP B OD2   1 
ATOM   4789 N  N     . ASN B 1 169 ? -22.26900 2.15200   24.07900  1.000 99.08820  ? 169 ASN B N     1 
ATOM   4790 C  CA    . ASN B 1 169 ? -20.97000 1.61700   24.48500  1.000 93.69544  ? 169 ASN B CA    1 
ATOM   4791 C  C     . ASN B 1 169 ? -20.01500 2.72200   24.91600  1.000 96.63001  ? 169 ASN B C     1 
ATOM   4792 O  O     . ASN B 1 169 ? -19.30400 2.57500   25.91400  1.000 84.74700  ? 169 ASN B O     1 
ATOM   4793 C  CB    . ASN B 1 169 ? -20.36700 0.78400   23.35100  1.000 86.44721  ? 169 ASN B CB    1 
ATOM   4794 C  CG    . ASN B 1 169 ? -19.14900 0.01100   23.77800  1.000 83.59950  ? 169 ASN B CG    1 
ATOM   4795 O  OD1   . ASN B 1 169 ? -18.04500 0.55100   23.77000  1.000 80.07539  ? 169 ASN B OD1   1 
ATOM   4796 N  ND2   . ASN B 1 169 ? -19.34500 -1.23000  24.22500  1.000 81.01761  ? 169 ASN B ND2   1 
ATOM   4797 N  N     . ASP B 1 170 ? -20.00400 3.83600   24.18800  1.000 113.87944 ? 170 ASP B N     1 
ATOM   4798 C  CA    . ASP B 1 170 ? -19.16700 4.96500   24.58100  1.000 104.82309 ? 170 ASP B CA    1 
ATOM   4799 C  C     . ASP B 1 170 ? -19.46400 5.40400   26.01300  1.000 93.82441  ? 170 ASP B C     1 
ATOM   4800 O  O     . ASP B 1 170 ? -18.54600 5.76900   26.75400  1.000 87.78421  ? 170 ASP B O     1 
ATOM   4801 C  CB    . ASP B 1 170 ? -19.36600 6.12200   23.60900  1.000 114.71639 ? 170 ASP B CB    1 
ATOM   4802 C  CG    . ASP B 1 170 ? -18.54800 5.96300   22.36300  1.000 121.85935 ? 170 ASP B CG    1 
ATOM   4803 O  OD1   . ASP B 1 170 ? -17.85300 4.92100   22.24200  1.000 132.94489 ? 170 ASP B OD1   1 
ATOM   4804 O  OD2   . ASP B 1 170 ? -18.59100 6.87000   21.51500  1.000 147.54401 ? 170 ASP B OD2   1 
ATOM   4805 N  N     . SER B 1 171 ? -20.73600 5.39300   26.41800  1.000 88.54220  ? 171 SER B N     1 
ATOM   4806 C  CA    . SER B 1 171 ? -21.06300 5.82200   27.77600  1.000 89.77392  ? 171 SER B CA    1 
ATOM   4807 C  C     . SER B 1 171 ? -20.58100 4.81100   28.81000  1.000 83.41526  ? 171 SER B C     1 
ATOM   4808 O  O     . SER B 1 171 ? -20.13900 5.19600   29.90000  1.000 80.19909  ? 171 SER B O     1 
ATOM   4809 C  CB    . SER B 1 171 ? -22.56400 6.06300   27.91700  1.000 91.90839  ? 171 SER B CB    1 
ATOM   4810 O  OG    . SER B 1 171 ? -22.99300 7.19000   27.17000  1.000 108.42879 ? 171 SER B OG    1 
ATOM   4811 N  N     . LEU B 1 172 ? -20.67800 3.51600   28.49300  1.000 81.70980  ? 172 LEU B N     1 
ATOM   4812 C  CA    . LEU B 1 172 ? -20.20100 2.48000   29.40500  1.000 78.94631  ? 172 LEU B CA    1 
ATOM   4813 C  C     . LEU B 1 172 ? -18.68800 2.53800   29.58100  1.000 74.55631  ? 172 LEU B C     1 
ATOM   4814 O  O     . LEU B 1 172 ? -18.18300 2.33400   30.69100  1.000 70.68479  ? 172 LEU B O     1 
ATOM   4815 C  CB    . LEU B 1 172 ? -20.62700 1.09300   28.91700  1.000 77.99883  ? 172 LEU B CB    1 
ATOM   4816 C  CG    . LEU B 1 172 ? -22.03300 0.61800   29.29400  1.000 85.70764  ? 172 LEU B CG    1 
ATOM   4817 C  CD1   . LEU B 1 172 ? -22.18900 0.58300   30.81100  1.000 74.53262  ? 172 LEU B CD1   1 
ATOM   4818 C  CD2   . LEU B 1 172 ? -23.10500 1.47600   28.68300  1.000 100.42520 ? 172 LEU B CD2   1 
ATOM   4819 N  N     . VAL B 1 173 ? -17.94500 2.81600   28.50600  1.000 68.01342  ? 173 VAL B N     1 
ATOM   4820 C  CA    . VAL B 1 173 ? -16.49300 2.93900   28.62200  1.000 63.86029  ? 173 VAL B CA    1 
ATOM   4821 C  C     . VAL B 1 173 ? -16.13000 4.04500   29.60600  1.000 65.01043  ? 173 VAL B C     1 
ATOM   4822 O  O     . VAL B 1 173 ? -15.28200 3.86400   30.48800  1.000 59.59662  ? 173 VAL B O     1 
ATOM   4823 C  CB    . VAL B 1 173 ? -15.85800 3.18100   27.24100  1.000 66.20794  ? 173 VAL B CB    1 
ATOM   4824 C  CG1   . VAL B 1 173 ? -14.37100 3.50700   27.37700  1.000 63.74448  ? 173 VAL B CG1   1 
ATOM   4825 C  CG2   . VAL B 1 173 ? -16.06500 1.96900   26.34500  1.000 70.53740  ? 173 VAL B CG2   1 
ATOM   4826 N  N     . VAL B 1 174 ? -16.76500 5.21000   29.46300  1.000 78.44362  ? 174 VAL B N     1 
ATOM   4827 C  CA    . VAL B 1 174 ? -16.49400 6.33800   30.35300  1.000 69.96102  ? 174 VAL B CA    1 
ATOM   4828 C  C     . VAL B 1 174 ? -16.85700 5.98900   31.79200  1.000 68.03710  ? 174 VAL B C     1 
ATOM   4829 O  O     . VAL B 1 174 ? -16.09400 6.26400   32.72700  1.000 59.07814  ? 174 VAL B O     1 
ATOM   4830 C  CB    . VAL B 1 174 ? -17.24600 7.58800   29.86600  1.000 74.14310  ? 174 VAL B CB    1 
ATOM   4831 C  CG1   . VAL B 1 174 ? -17.16500 8.70000   30.90200  1.000 74.39576  ? 174 VAL B CG1   1 
ATOM   4832 C  CG2   . VAL B 1 174 ? -16.68700 8.04600   28.53100  1.000 77.95145  ? 174 VAL B CG2   1 
ATOM   4833 N  N     . LEU B 1 175 ? -18.03300 5.38600   31.99100  1.000 73.01665  ? 175 LEU B N     1 
ATOM   4834 C  CA    . LEU B 1 175 ? -18.49400 5.06100   33.33900  1.000 70.17157  ? 175 LEU B CA    1 
ATOM   4835 C  C     . LEU B 1 175 ? -17.52700 4.11500   34.04000  1.000 72.63239  ? 175 LEU B C     1 
ATOM   4836 O  O     . LEU B 1 175 ? -17.14300 4.34400   35.19500  1.000 56.24095  ? 175 LEU B O     1 
ATOM   4837 C  CB    . LEU B 1 175 ? -19.89200 4.44700   33.27900  1.000 71.59279  ? 175 LEU B CB    1 
ATOM   4838 C  CG    . LEU B 1 175 ? -20.54400 4.15300   34.63100  1.000 72.78767  ? 175 LEU B CG    1 
ATOM   4839 C  CD1   . LEU B 1 175 ? -20.66800 5.42900   35.45100  1.000 68.74508  ? 175 LEU B CD1   1 
ATOM   4840 C  CD2   . LEU B 1 175 ? -21.89300 3.48700   34.44200  1.000 77.29611  ? 175 LEU B CD2   1 
ATOM   4841 N  N     . PHE B 1 176 ? -17.13700 3.03100   33.36100  1.000 63.47077  ? 176 PHE B N     1 
ATOM   4842 C  CA    . PHE B 1 176 ? -16.15100 2.11500   33.92800  1.000 65.36573  ? 176 PHE B CA    1 
ATOM   4843 C  C     . PHE B 1 176 ? -14.83700 2.83000   34.22600  1.000 54.14333  ? 176 PHE B C     1 
ATOM   4844 O  O     . PHE B 1 176 ? -14.18500 2.54700   35.23700  1.000 57.63323  ? 176 PHE B O     1 
ATOM   4845 C  CB    . PHE B 1 176 ? -15.92100 0.92800   32.99000  1.000 63.17336  ? 176 PHE B CB    1 
ATOM   4846 C  CG    . PHE B 1 176 ? -16.84700 -0.23600  33.23700  1.000 63.79975  ? 176 PHE B CG    1 
ATOM   4847 C  CD1   . PHE B 1 176 ? -16.71100 -1.01700  34.37400  1.000 62.50749  ? 176 PHE B CD1   1 
ATOM   4848 C  CD2   . PHE B 1 176 ? -17.83800 -0.56100  32.32300  1.000 67.30017  ? 176 PHE B CD2   1 
ATOM   4849 C  CE1   . PHE B 1 176 ? -17.55400 -2.08900  34.60300  1.000 65.25519  ? 176 PHE B CE1   1 
ATOM   4850 C  CE2   . PHE B 1 176 ? -18.68500 -1.63400  32.54800  1.000 70.80059  ? 176 PHE B CE2   1 
ATOM   4851 C  CZ    . PHE B 1 176 ? -18.54100 -2.39800  33.69000  1.000 60.17827  ? 176 PHE B CZ    1 
ATOM   4852 N  N     . ALA B 1 177 ? -14.41200 3.73300   33.33800  1.000 56.95157  ? 177 ALA B N     1 
ATOM   4853 C  CA    . ALA B 1 177 ? -13.20900 4.51500   33.60200  1.000 53.41956  ? 177 ALA B CA    1 
ATOM   4854 C  C     . ALA B 1 177 ? -13.39200 5.40800   34.82500  1.000 52.85897  ? 177 ALA B C     1 
ATOM   4855 O  O     . ALA B 1 177 ? -12.46700 5.56900   35.63300  1.000 49.54805  ? 177 ALA B O     1 
ATOM   4856 C  CB    . ALA B 1 177 ? -12.84500 5.34700   32.37100  1.000 56.15147  ? 177 ALA B CB    1 
ATOM   4857 N  N     . GLN B 1 178 ? -14.57800 6.00700   34.97100  1.000 49.41382  ? 178 GLN B N     1 
ATOM   4858 C  CA    . GLN B 1 178 ? -14.87400 6.82800   36.14200  1.000 44.05528  ? 178 GLN B CA    1 
ATOM   4859 C  C     . GLN B 1 178 ? -14.87500 5.99700   37.42100  1.000 46.89246  ? 178 GLN B C     1 
ATOM   4860 O  O     . GLN B 1 178 ? -14.43600 6.46800   38.47700  1.000 41.74711  ? 178 GLN B O     1 
ATOM   4861 C  CB    . GLN B 1 178 ? -16.21800 7.52800   35.95600  1.000 45.18173  ? 178 GLN B CB    1 
ATOM   4862 C  CG    . GLN B 1 178 ? -16.19300 8.65400   34.94300  1.000 48.54266  ? 178 GLN B CG    1 
ATOM   4863 C  CD    . GLN B 1 178 ? -17.58600 9.11500   34.57100  1.000 53.41956  ? 178 GLN B CD    1 
ATOM   4864 O  OE1   . GLN B 1 178 ? -18.50300 8.30200   34.44800  1.000 56.63047  ? 178 GLN B OE1   1 
ATOM   4865 N  NE2   . GLN B 1 178 ? -17.75700 10.42200  34.39600  1.000 52.64315  ? 178 GLN B NE2   1 
ATOM   4866 N  N     . VAL B 1 179 ? -15.41000 4.77600   37.35400  1.000 50.44289  ? 179 VAL B N     1 
ATOM   4867 C  CA    . VAL B 1 179 ? -15.42800 3.89300   38.51800  1.000 49.25064  ? 179 VAL B CA    1 
ATOM   4868 C  C     . VAL B 1 179 ? -14.01200 3.49900   38.92200  1.000 53.61959  ? 179 VAL B C     1 
ATOM   4869 O  O     . VAL B 1 179 ? -13.67400 3.48400   40.11200  1.000 46.10553  ? 179 VAL B O     1 
ATOM   4870 C  CB    . VAL B 1 179 ? -16.30400 2.65800   38.24000  1.000 47.57413  ? 179 VAL B CB    1 
ATOM   4871 C  CG1   . VAL B 1 179 ? -16.16000 1.63300   39.35200  1.000 46.58453  ? 179 VAL B CG1   1 
ATOM   4872 C  CG2   . VAL B 1 179 ? -17.75100 3.07300   38.09500  1.000 57.02263  ? 179 VAL B CG2   1 
ATOM   4873 N  N     . ASN B 1 180 ? -13.17500 3.14100   37.94200  1.000 55.25663  ? 180 ASN B N     1 
ATOM   4874 C  CA    . ASN B 1 180 ? -11.78900 2.77900   38.22900  1.000 52.69842  ? 180 ASN B CA    1 
ATOM   4875 C  C     . ASN B 1 180 ? -11.04500 3.91500   38.91600  1.000 60.40987  ? 180 ASN B C     1 
ATOM   4876 O  O     . ASN B 1 180 ? -10.16400 3.67500   39.75100  1.000 50.75872  ? 180 ASN B O     1 
ATOM   4877 C  CB    . ASN B 1 180 ? -11.06600 2.39800   36.93800  1.000 54.73288  ? 180 ASN B CB    1 
ATOM   4878 C  CG    . ASN B 1 180 ? -11.56900 1.10200   36.34500  1.000 65.69472  ? 180 ASN B CG    1 
ATOM   4879 O  OD1   . ASN B 1 180 ? -12.29800 0.34800   36.99000  1.000 70.62163  ? 180 ASN B OD1   1 
ATOM   4880 N  ND2   . ASN B 1 180 ? -11.18400 0.83600   35.10300  1.000 66.37375  ? 180 ASN B ND2   1 
ATOM   4881 N  N     . CYS B 1 181 ? -11.36500 5.15700   38.55500  1.000 59.06761  ? 181 CYS B N     1 
ATOM   4882 C  CA    . CYS B 1 181 ? -10.64500 6.31200   39.07400  1.000 52.93529  ? 181 CYS B CA    1 
ATOM   4883 C  C     . CYS B 1 181 ? -11.18300 6.79100   40.41800  1.000 45.66337  ? 181 CYS B C     1 
ATOM   4884 O  O     . CYS B 1 181 ? -10.40700 7.26800   41.25400  1.000 54.37757  ? 181 CYS B O     1 
ATOM   4885 C  CB    . CYS B 1 181 ? -10.69600 7.44500   38.04700  1.000 51.02717  ? 181 CYS B CB    1 
ATOM   4886 S  SG    . CYS B 1 181 ? -9.78400  8.92100   38.50300  1.000 73.10877  ? 181 CYS B SG    1 
ATOM   4887 N  N     . ASN B 1 182 ? -12.49300 6.67700   40.64600  1.000 40.52854  ? 182 ASN B N     1 
ATOM   4888 C  CA    . ASN B 1 182 ? -13.14400 7.33000   41.77400  1.000 44.58166  ? 182 ASN B CA    1 
ATOM   4889 C  C     . ASN B 1 182 ? -13.80100 6.38400   42.76700  1.000 38.48356  ? 182 ASN B C     1 
ATOM   4890 O  O     . ASN B 1 182 ? -14.31100 6.85500   43.79200  1.000 37.51766  ? 182 ASN B O     1 
ATOM   4891 C  CB    . ASN B 1 182 ? -14.19400 8.33100   41.27400  1.000 45.90550  ? 182 ASN B CB    1 
ATOM   4892 C  CG    . ASN B 1 182 ? -13.58000 9.43800   40.46000  1.000 50.87715  ? 182 ASN B CG    1 
ATOM   4893 O  OD1   . ASN B 1 182 ? -12.99800 10.37100  41.00900  1.000 50.76661  ? 182 ASN B OD1   1 
ATOM   4894 N  ND2   . ASN B 1 182 ? -13.69400 9.34100   39.14000  1.000 48.06892  ? 182 ASN B ND2   1 
ATOM   4895 N  N     . GLY B 1 183 ? -13.83600 5.08400   42.48800  1.000 42.45509  ? 183 GLY B N     1 
ATOM   4896 C  CA    . GLY B 1 183 ? -14.41700 4.14500   43.42300  1.000 42.21032  ? 183 GLY B CA    1 
ATOM   4897 C  C     . GLY B 1 183 ? -13.57300 3.97700   44.67400  1.000 33.63035  ? 183 GLY B C     1 
ATOM   4898 O  O     . GLY B 1 183 ? -12.36600 4.22100   44.69300  1.000 39.14417  ? 183 GLY B O     1 
ATOM   4899 N  N     . PHE B 1 184 ? -14.23700 3.55700   45.74700  1.000 33.56981  ? 184 PHE B N     1 
ATOM   4900 C  CA    . PHE B 1 184 ? -13.60000 3.33400   47.03800  1.000 32.28808  ? 184 PHE B CA    1 
ATOM   4901 C  C     . PHE B 1 184 ? -13.73900 1.87400   47.44600  1.000 33.89617  ? 184 PHE B C     1 
ATOM   4902 O  O     . PHE B 1 184 ? -14.70500 1.20000   47.08000  1.000 37.93350  ? 184 PHE B O     1 
ATOM   4903 C  CB    . PHE B 1 184 ? -14.21400 4.24100   48.11500  1.000 31.85382  ? 184 PHE B CB    1 
ATOM   4904 C  CG    . PHE B 1 184 ? -13.78900 5.67900   48.00600  1.000 39.61264  ? 184 PHE B CG    1 
ATOM   4905 C  CD1   . PHE B 1 184 ? -14.37500 6.52400   47.07600  1.000 44.57903  ? 184 PHE B CD1   1 
ATOM   4906 C  CD2   . PHE B 1 184 ? -12.80500 6.18400   48.83800  1.000 35.47794  ? 184 PHE B CD2   1 
ATOM   4907 C  CE1   . PHE B 1 184 ? -13.97600 7.84200   46.97500  1.000 40.50749  ? 184 PHE B CE1   1 
ATOM   4908 C  CE2   . PHE B 1 184 ? -12.40500 7.50000   48.74400  1.000 39.69160  ? 184 PHE B CE2   1 
ATOM   4909 C  CZ    . PHE B 1 184 ? -12.98600 8.33200   47.81500  1.000 42.94199  ? 184 PHE B CZ    1 
ATOM   4910 N  N     . THR B 1 185 ? -12.74400 1.37500   48.17000  1.000 33.85669  ? 185 THR B N     1 
ATOM   4911 C  CA    . THR B 1 185 ? -12.84600 0.08600   48.83700  1.000 40.79700  ? 185 THR B CA    1 
ATOM   4912 C  C     . THR B 1 185 ? -13.21100 0.31700   50.29800  1.000 35.72007  ? 185 THR B C     1 
ATOM   4913 O  O     . THR B 1 185 ? -12.67600 1.22100   50.94500  1.000 33.31715  ? 185 THR B O     1 
ATOM   4914 C  CB    . THR B 1 185 ? -11.53900 -0.70800  48.74000  1.000 32.65392  ? 185 THR B CB    1 
ATOM   4915 O  OG1   . THR B 1 185 ? -10.45900 0.08000   49.25300  1.000 43.52890  ? 185 THR B OG1   1 
ATOM   4916 C  CG2   . THR B 1 185 ? -11.24300 -1.07200  47.29000  1.000 42.11821  ? 185 THR B CG2   1 
ATOM   4917 N  N     . ILE B 1 186 ? -14.14500 -0.47600  50.80800  1.000 32.66971  ? 186 ILE B N     1 
ATOM   4918 C  CA    . ILE B 1 186 ? -14.53000 -0.42200  52.21200  1.000 33.00659  ? 186 ILE B CA    1 
ATOM   4919 C  C     . ILE B 1 186 ? -13.85000 -1.57500  52.93600  1.000 30.09308  ? 186 ILE B C     1 
ATOM   4920 O  O     . ILE B 1 186 ? -13.92400 -2.72700  52.48800  1.000 44.63167  ? 186 ILE B O     1 
ATOM   4921 C  CB    . ILE B 1 186 ? -16.05800 -0.48000  52.37400  1.000 36.20171  ? 186 ILE B CB    1 
ATOM   4922 C  CG1   . ILE B 1 186 ? -16.69700 0.74300   51.70900  1.000 38.31249  ? 186 ILE B CG1   1 
ATOM   4923 C  CG2   . ILE B 1 186 ? -16.43700 -0.54500  53.84800  1.000 33.40664  ? 186 ILE B CG2   1 
ATOM   4924 C  CD1   . ILE B 1 186 ? -18.20900 0.69200   51.64200  1.000 35.09368  ? 186 ILE B CD1   1 
ATOM   4925 N  N     . GLU B 1 187 ? -13.18400 -1.26900  54.04900  1.000 33.46454  ? 187 GLU B N     1 
ATOM   4926 C  CA    . GLU B 1 187 ? -12.48700 -2.26400  54.85100  1.000 36.73598  ? 187 GLU B CA    1 
ATOM   4927 C  C     . GLU B 1 187 ? -13.03100 -2.27500  56.27300  1.000 35.56742  ? 187 GLU B C     1 
ATOM   4928 O  O     . GLU B 1 187 ? -13.57300 -1.27500  56.75700  1.000 32.62760  ? 187 GLU B O     1 
ATOM   4929 C  CB    . GLU B 1 187 ? -10.97000 -2.00300  54.89000  1.000 51.44301  ? 187 GLU B CB    1 
ATOM   4930 C  CG    . GLU B 1 187 ? -10.25300 -2.14000  53.55200  1.000 60.05194  ? 187 GLU B CG    1 
ATOM   4931 C  CD    . GLU B 1 187 ? -10.24900 -0.85600  52.74000  1.000 65.98949  ? 187 GLU B CD    1 
ATOM   4932 O  OE1   . GLU B 1 187 ? -10.48400 0.22400   53.32400  1.000 62.76805  ? 187 GLU B OE1   1 
ATOM   4933 O  OE2   . GLU B 1 187 ? -9.99600  -0.92900  51.51900  1.000 64.75513  ? 187 GLU B OE2   1 
ATOM   4934 N  N     . ASP B 1 188 ? -12.88600 -3.42000  56.94000  1.000 30.22204  ? 188 ASP B N     1 
ATOM   4935 C  CA    . ASP B 1 188 ? -13.27900 -3.54400  58.33600  1.000 38.25722  ? 188 ASP B CA    1 
ATOM   4936 C  C     . ASP B 1 188 ? -12.14900 -3.05100  59.24900  1.000 33.58297  ? 188 ASP B C     1 
ATOM   4937 O  O     . ASP B 1 188 ? -11.13200 -2.52200  58.79400  1.000 30.43260  ? 188 ASP B O     1 
ATOM   4938 C  CB    . ASP B 1 188 ? -13.71200 -4.98400  58.63500  1.000 34.81996  ? 188 ASP B CB    1 
ATOM   4939 C  CG    . ASP B 1 188 ? -12.56800 -6.00100  58.55800  1.000 36.18592  ? 188 ASP B CG    1 
ATOM   4940 O  OD1   . ASP B 1 188 ? -11.38100 -5.61900  58.43800  1.000 36.33330  ? 188 ASP B OD1   1 
ATOM   4941 O  OD2   . ASP B 1 188 ? -12.87000 -7.21400  58.60100  1.000 38.17826  ? 188 ASP B OD2   1 
ATOM   4942 N  N     . GLU B 1 189 ? -12.33800 -3.21100  60.56200  1.000 37.06234  ? 189 GLU B N     1 
ATOM   4943 C  CA    . GLU B 1 189 ? -11.38300 -2.68100  61.53400  1.000 30.76421  ? 189 GLU B CA    1 
ATOM   4944 C  C     . GLU B 1 189 ? -10.00300 -3.33200  61.44200  1.000 30.45102  ? 189 GLU B C     1 
ATOM   4945 O  O     . GLU B 1 189 ? -9.03200  -2.76700  61.95700  1.000 29.06664  ? 189 GLU B O     1 
ATOM   4946 C  CB    . GLU B 1 189 ? -11.94100 -2.82300  62.95500  1.000 30.62472  ? 189 GLU B CB    1 
ATOM   4947 C  CG    . GLU B 1 189 ? -11.94800 -4.24300  63.50800  1.000 33.79089  ? 189 GLU B CG    1 
ATOM   4948 C  CD    . GLU B 1 189 ? -13.12400 -5.07600  63.04000  1.000 39.23365  ? 189 GLU B CD    1 
ATOM   4949 O  OE1   . GLU B 1 189 ? -13.76800 -4.71700  62.02900  1.000 44.42901  ? 189 GLU B OE1   1 
ATOM   4950 O  OE2   . GLU B 1 189 ? -13.40200 -6.10200  63.69500  1.000 37.32026  ? 189 GLU B OE2   1 
ATOM   4951 N  N     . GLU B 1 190 ? -9.89300  -4.51200  60.82700  1.000 25.64518  ? 190 GLU B N     1 
ATOM   4952 C  CA    . GLU B 1 190 ? -8.61000  -5.16800  60.59900  1.000 26.18998  ? 190 GLU B CA    1 
ATOM   4953 C  C     . GLU B 1 190 ? -8.08200  -4.93300  59.18600  1.000 29.48775  ? 190 GLU B C     1 
ATOM   4954 O  O     . GLU B 1 190 ? -7.18000  -5.65200  58.74000  1.000 32.88552  ? 190 GLU B O     1 
ATOM   4955 C  CB    . GLU B 1 190 ? -8.71600  -6.66600  60.88600  1.000 32.37230  ? 190 GLU B CB    1 
ATOM   4956 C  CG    . GLU B 1 190 ? -8.81000  -6.99300  62.36500  1.000 33.08555  ? 190 GLU B CG    1 
ATOM   4957 C  CD    . GLU B 1 190 ? -8.87200  -8.48700  62.64900  1.000 39.87583  ? 190 GLU B CD    1 
ATOM   4958 O  OE1   . GLU B 1 190 ? -8.52000  -9.28800  61.75800  1.000 36.21487  ? 190 GLU B OE1   1 
ATOM   4959 O  OE2   . GLU B 1 190 ? -9.27300  -8.85900  63.77000  1.000 42.35508  ? 190 GLU B OE2   1 
ATOM   4960 N  N     . LEU B 1 191 ? -8.63500  -3.94000  58.48000  1.000 31.48272  ? 191 LEU B N     1 
ATOM   4961 C  CA    . LEU B 1 191 ? -8.29700  -3.61400  57.08900  1.000 38.15984  ? 191 LEU B CA    1 
ATOM   4962 C  C     . LEU B 1 191 ? -8.52900  -4.78300  56.13900  1.000 30.22204  ? 191 LEU B C     1 
ATOM   4963 O  O     . LEU B 1 191 ? -7.87700  -4.88300  55.09700  1.000 34.97788  ? 191 LEU B O     1 
ATOM   4964 C  CB    . LEU B 1 191 ? -6.85500  -3.11000  56.96500  1.000 33.17240  ? 191 LEU B CB    1 
ATOM   4965 C  CG    . LEU B 1 191 ? -6.56700  -1.70600  57.49600  1.000 34.45413  ? 191 LEU B CG    1 
ATOM   4966 C  CD1   . LEU B 1 191 ? -5.27600  -1.17600  56.89900  1.000 41.75237  ? 191 LEU B CD1   1 
ATOM   4967 C  CD2   . LEU B 1 191 ? -7.72300  -0.76600  57.19200  1.000 46.84772  ? 191 LEU B CD2   1 
ATOM   4968 N  N     . SER B 1 192 ? -9.48700  -5.64800  56.46000  1.000 32.21965  ? 192 SER B N     1 
ATOM   4969 C  CA    . SER B 1 192 ? -9.92100  -6.70200  55.55200  1.000 36.77809  ? 192 SER B CA    1 
ATOM   4970 C  C     . SER B 1 192 ? -10.96700 -6.15000  54.58500  1.000 36.73335  ? 192 SER B C     1 
ATOM   4971 O  O     . SER B 1 192 ? -11.77400 -5.29300  54.95100  1.000 37.05707  ? 192 SER B O     1 
ATOM   4972 C  CB    . SER B 1 192 ? -10.48400 -7.88500  56.34400  1.000 34.91208  ? 192 SER B CB    1 
ATOM   4973 O  OG    . SER B 1 192 ? -10.31300 -9.10400  55.64200  1.000 52.26416  ? 192 SER B OG    1 
ATOM   4974 N  N     . HIS B 1 193 ? -10.92800 -6.62200  53.33800  1.000 38.84939  ? 193 HIS B N     1 
ATOM   4975 C  CA    . HIS B 1 193 ? -11.80000 -6.09300  52.29100  1.000 36.44384  ? 193 HIS B CA    1 
ATOM   4976 C  C     . HIS B 1 193 ? -13.25900 -6.47900  52.54100  1.000 32.94079  ? 193 HIS B C     1 
ATOM   4977 O  O     . HIS B 1 193 ? -13.58600 -7.66600  52.65500  1.000 33.39611  ? 193 HIS B O     1 
ATOM   4978 C  CB    . HIS B 1 193 ? -11.34300 -6.59600  50.92300  1.000 33.97249  ? 193 HIS B CB    1 
ATOM   4979 C  CG    . HIS B 1 193 ? -12.12600 -6.02800  49.77900  1.000 39.35209  ? 193 HIS B CG    1 
ATOM   4980 N  ND1   . HIS B 1 193 ? -11.96000 -4.73400  49.33500  1.000 40.48380  ? 193 HIS B ND1   1 
ATOM   4981 C  CD2   . HIS B 1 193 ? -13.07700 -6.57800  48.98600  1.000 52.85371  ? 193 HIS B CD2   1 
ATOM   4982 C  CE1   . HIS B 1 193 ? -12.77700 -4.50900  48.32100  1.000 59.81507  ? 193 HIS B CE1   1 
ATOM   4983 N  NE2   . HIS B 1 193 ? -13.46700 -5.61200  48.09000  1.000 42.80513  ? 193 HIS B NE2   1 
ATOM   4984 N  N     . LEU B 1 194 ? -14.13600 -5.47700  52.62800  1.000 30.66947  ? 194 LEU B N     1 
ATOM   4985 C  CA    . LEU B 1 194 ? -15.57000 -5.69800  52.79600  1.000 38.93888  ? 194 LEU B CA    1 
ATOM   4986 C  C     . LEU B 1 194 ? -16.36800 -5.50100  51.51100  1.000 39.17312  ? 194 LEU B C     1 
ATOM   4987 O  O     . LEU B 1 194 ? -17.33900 -6.23000  51.27400  1.000 40.02322  ? 194 LEU B O     1 
ATOM   4988 C  CB    . LEU B 1 194 ? -16.13200 -4.76600  53.87300  1.000 43.08411  ? 194 LEU B CB    1 
ATOM   4989 C  CG    . LEU B 1 194 ? -15.84200 -5.11000  55.33400  1.000 47.99786  ? 194 LEU B CG    1 
ATOM   4990 C  CD1   . LEU B 1 194 ? -16.72000 -4.26700  56.25000  1.000 47.81363  ? 194 LEU B CD1   1 
ATOM   4991 C  CD2   . LEU B 1 194 ? -16.03200 -6.59500  55.60500  1.000 51.68778  ? 194 LEU B CD2   1 
ATOM   4992 N  N     . GLY B 1 195 ? -15.99400 -4.52900  50.68600  1.000 36.23329  ? 195 GLY B N     1 
ATOM   4993 C  CA    . GLY B 1 195 ? -16.72000 -4.26400  49.46100  1.000 39.60212  ? 195 GLY B CA    1 
ATOM   4994 C  C     . GLY B 1 195 ? -16.20100 -3.00800  48.78900  1.000 38.39408  ? 195 GLY B C     1 
ATOM   4995 O  O     . GLY B 1 195 ? -15.14600 -2.47700  49.14800  1.000 33.25925  ? 195 GLY B O     1 
ATOM   4996 N  N     . SER B 1 196 ? -16.96000 -2.55400  47.79200  1.000 39.96005  ? 196 SER B N     1 
ATOM   4997 C  CA    . SER B 1 196 ? -16.61000 -1.39300  46.98900  1.000 36.63860  ? 196 SER B CA    1 
ATOM   4998 C  C     . SER B 1 196 ? -17.78400 -0.42400  46.97000  1.000 36.55175  ? 196 SER B C     1 
ATOM   4999 O  O     . SER B 1 196 ? -18.94000 -0.83800  47.07100  1.000 39.56001  ? 196 SER B O     1 
ATOM   5000 C  CB    . SER B 1 196 ? -16.24200 -1.80400  45.55500  1.000 47.03195  ? 196 SER B CB    1 
ATOM   5001 O  OG    . SER B 1 196 ? -15.07300 -2.61100  45.52400  1.000 46.64770  ? 196 SER B OG    1 
ATOM   5002 N  N     . ALA B 1 197 ? -17.48900 0.86900   46.83200  1.000 34.97525  ? 197 ALA B N     1 
ATOM   5003 C  CA    . ALA B 1 197 ? -18.55000 1.86900   46.89200  1.000 38.80728  ? 197 ALA B CA    1 
ATOM   5004 C  C     . ALA B 1 197 ? -18.14600 3.12800   46.13800  1.000 39.29155  ? 197 ALA B C     1 
ATOM   5005 O  O     . ALA B 1 197 ? -16.96700 3.35700   45.85400  1.000 38.52041  ? 197 ALA B O     1 
ATOM   5006 C  CB    . ALA B 1 197 ? -18.90200 2.22000   48.34100  1.000 35.18317  ? 197 ALA B CB    1 
ATOM   5007 N  N     . ILE B 1 198 ? -19.15800 3.93300   45.80500  1.000 39.75477  ? 198 ILE B N     1 
ATOM   5008 C  CA    . ILE B 1 198 ? -18.99200 5.27900   45.25700  1.000 40.16008  ? 198 ILE B CA    1 
ATOM   5009 C  C     . ILE B 1 198 ? -19.41400 6.28800   46.31700  1.000 36.78336  ? 198 ILE B C     1 
ATOM   5010 O  O     . ILE B 1 198 ? -20.54700 6.24300   46.81500  1.000 41.56551  ? 198 ILE B O     1 
ATOM   5011 C  CB    . ILE B 1 198 ? -19.79500 5.49300   43.95900  1.000 47.06091  ? 198 ILE B CB    1 
ATOM   5012 C  CG1   . ILE B 1 198 ? -19.11900 4.82800   42.75800  1.000 44.62114  ? 198 ILE B CG1   1 
ATOM   5013 C  CG2   . ILE B 1 198 ? -20.02000 6.97900   43.68900  1.000 45.92393  ? 198 ILE B CG2   1 
ATOM   5014 C  CD1   . ILE B 1 198 ? -19.19300 3.37500   42.75100  1.000 55.09871  ? 198 ILE B CD1   1 
ATOM   5015 N  N     . PHE B 1 199 ? -18.50300 7.19700   46.66300  1.000 40.77857  ? 199 PHE B N     1 
ATOM   5016 C  CA    . PHE B 1 199 ? -18.77900 8.30800   47.57100  1.000 37.57819  ? 199 PHE B CA    1 
ATOM   5017 C  C     . PHE B 1 199 ? -18.45300 9.59500   46.82500  1.000 38.97046  ? 199 PHE B C     1 
ATOM   5018 O  O     . PHE B 1 199 ? -17.32600 10.10800  46.92200  1.000 38.46514  ? 199 PHE B O     1 
ATOM   5019 C  CB    . PHE B 1 199 ? -17.96500 8.19200   48.85500  1.000 35.12790  ? 199 PHE B CB    1 
ATOM   5020 C  CG    . PHE B 1 199 ? -18.30100 6.98600   49.67600  1.000 32.44336  ? 199 PHE B CG    1 
ATOM   5021 C  CD1   . PHE B 1 199 ? -19.47200 6.93900   50.41600  1.000 33.82511  ? 199 PHE B CD1   1 
ATOM   5022 C  CD2   . PHE B 1 199 ? -17.43700 5.90100   49.72000  1.000 34.21463  ? 199 PHE B CD2   1 
ATOM   5023 C  CE1   . PHE B 1 199 ? -19.78100 5.82400   51.18400  1.000 34.11725  ? 199 PHE B CE1   1 
ATOM   5024 C  CE2   . PHE B 1 199 ? -17.73500 4.78200   50.48500  1.000 34.72785  ? 199 PHE B CE2   1 
ATOM   5025 C  CZ    . PHE B 1 199 ? -18.91000 4.74300   51.21800  1.000 33.75142  ? 199 PHE B CZ    1 
ATOM   5026 N  N     . PRO B 1 200 ? -19.41700 10.16000  46.08800  1.000 44.09476  ? 200 PRO B N     1 
ATOM   5027 C  CA    . PRO B 1 200 ? -19.09400 11.28600  45.18600  1.000 45.89234  ? 200 PRO B CA    1 
ATOM   5028 C  C     . PRO B 1 200 ? -18.41900 12.47100  45.86500  1.000 43.68155  ? 200 PRO B C     1 
ATOM   5029 O  O     . PRO B 1 200 ? -17.41000 12.97300  45.35200  1.000 43.43152  ? 200 PRO B O     1 
ATOM   5030 C  CB    . PRO B 1 200 ? -20.46500 11.65800  44.60300  1.000 49.65595  ? 200 PRO B CB    1 
ATOM   5031 C  CG    . PRO B 1 200 ? -21.27500 10.39700  44.70600  1.000 51.76936  ? 200 PRO B CG    1 
ATOM   5032 C  CD    . PRO B 1 200 ? -20.82800 9.74600   45.98200  1.000 45.01329  ? 200 PRO B CD    1 
ATOM   5033 N  N     . ASP B 1 201 ? -18.95400 12.95300  46.99200  1.000 46.89246  ? 201 ASP B N     1 
ATOM   5034 C  CA    . ASP B 1 201 ? -18.34700 14.10300  47.66300  1.000 44.41585  ? 201 ASP B CA    1 
ATOM   5035 C  C     . ASP B 1 201 ? -16.97900 13.76500  48.25300  1.000 43.68945  ? 201 ASP B C     1 
ATOM   5036 O  O     . ASP B 1 201 ? -16.11900 14.64600  48.35400  1.000 41.79448  ? 201 ASP B O     1 
ATOM   5037 C  CB    . ASP B 1 201 ? -19.28200 14.64100  48.74900  1.000 45.70548  ? 201 ASP B CB    1 
ATOM   5038 C  CG    . ASP B 1 201 ? -20.44500 15.45200  48.18200  1.000 51.75094  ? 201 ASP B CG    1 
ATOM   5039 O  OD1   . ASP B 1 201 ? -20.29900 16.01900  47.07700  1.000 53.33797  ? 201 ASP B OD1   1 
ATOM   5040 O  OD2   . ASP B 1 201 ? -21.51100 15.51100  48.83800  1.000 51.58776  ? 201 ASP B OD2   1 
ATOM   5041 N  N     . VAL B 1 202 ? -16.76500 12.51200  48.66300  1.000 41.71290  ? 202 VAL B N     1 
ATOM   5042 C  CA    . VAL B 1 202 ? -15.45300 12.10800  49.16400  1.000 34.73574  ? 202 VAL B CA    1 
ATOM   5043 C  C     . VAL B 1 202 ? -14.44800 12.01600  48.02400  1.000 35.45951  ? 202 VAL B C     1 
ATOM   5044 O  O     . VAL B 1 202 ? -13.25100 12.25800  48.21900  1.000 34.33306  ? 202 VAL B O     1 
ATOM   5045 C  CB    . VAL B 1 202 ? -15.56000 10.78000  49.93300  1.000 34.89366  ? 202 VAL B CB    1 
ATOM   5046 C  CG1   . VAL B 1 202 ? -14.21200 10.40000  50.55000  1.000 31.97489  ? 202 VAL B CG1   1 
ATOM   5047 C  CG2   . VAL B 1 202 ? -16.63400 10.87800  51.00300  1.000 34.32517  ? 202 VAL B CG2   1 
ATOM   5048 N  N     . ALA B 1 203 ? -14.90700 11.65400  46.82400  1.000 31.15110  ? 203 ALA B N     1 
ATOM   5049 C  CA    . ALA B 1 203 ? -14.01200 11.54800  45.67700  1.000 33.53823  ? 203 ALA B CA    1 
ATOM   5050 C  C     . ALA B 1 203 ? -13.42500 12.89300  45.26400  1.000 31.35639  ? 203 ALA B C     1 
ATOM   5051 O  O     . ALA B 1 203 ? -12.41900 12.91500  44.54900  1.000 36.29909  ? 203 ALA B O     1 
ATOM   5052 C  CB    . ALA B 1 203 ? -14.74400 10.90700  44.49300  1.000 33.76721  ? 203 ALA B CB    1 
ATOM   5053 N  N     . LEU B 1 204 ? -14.02700 14.00800  45.69400  1.000 33.82511  ? 204 LEU B N     1 
ATOM   5054 C  CA    . LEU B 1 204 ? -13.53600 15.33600  45.32500  1.000 32.69866  ? 204 LEU B CA    1 
ATOM   5055 C  C     . LEU B 1 204 ? -12.15200 15.63200  45.90100  1.000 31.93804  ? 204 LEU B C     1 
ATOM   5056 O  O     . LEU B 1 204 ? -11.41000 16.45600  45.34500  1.000 32.62233  ? 204 LEU B O     1 
ATOM   5057 C  CB    . LEU B 1 204 ? -14.53600 16.40800  45.77100  1.000 34.63047  ? 204 LEU B CB    1 
ATOM   5058 C  CG    . LEU B 1 204 ? -14.17700 17.86900  45.48300  1.000 36.89390  ? 204 LEU B CG    1 
ATOM   5059 C  CD1   . LEU B 1 204 ? -13.87900 18.04700  44.00600  1.000 43.51838  ? 204 LEU B CD1   1 
ATOM   5060 C  CD2   . LEU B 1 204 ? -15.28900 18.80900  45.93000  1.000 42.42351  ? 204 LEU B CD2   1 
ATOM   5061 N  N     . MET B 1 205 ? -11.79400 15.00200  47.01800  1.000 31.18532  ? 205 MET B N     1 
ATOM   5062 C  CA    . MET B 1 205 ? -10.51600 15.29000  47.65800  1.000 28.54553  ? 205 MET B CA    1 
ATOM   5063 C  C     . MET B 1 205 ? -9.36000  14.71400  46.84600  1.000 28.86662  ? 205 MET B C     1 
ATOM   5064 O  O     . MET B 1 205 ? -9.40000  13.56000  46.41100  1.000 34.87787  ? 205 MET B O     1 
ATOM   5065 C  CB    . MET B 1 205 ? -10.50300 14.72600  49.07800  1.000 27.97441  ? 205 MET B CB    1 
ATOM   5066 C  CG    . MET B 1 205 ? -11.49200 15.41700  50.01500  1.000 33.86722  ? 205 MET B CG    1 
ATOM   5067 S  SD    . MET B 1 205 ? -11.42000 14.78500  51.70100  1.000 33.86985  ? 205 MET B SD    1 
ATOM   5068 C  CE    . MET B 1 205 ? -12.04700 13.13100  51.43700  1.000 27.60594  ? 205 MET B CE    1 
ATOM   5069 N  N     . ASN B 1 206 ? -8.33100  15.52000  46.64000  1.000 29.69040  ? 206 ASN B N     1 
ATOM   5070 C  CA    . ASN B 1 206 ? -7.14200  15.07300  45.93500  1.000 33.70141  ? 206 ASN B CA    1 
ATOM   5071 C  C     . ASN B 1 206 ? -6.23000  14.26600  46.86500  1.000 29.15876  ? 206 ASN B C     1 
ATOM   5072 O  O     . ASN B 1 206 ? -6.46900  14.15200  48.07100  1.000 26.29789  ? 206 ASN B O     1 
ATOM   5073 C  CB    . ASN B 1 206 ? -6.42300  16.27800  45.33100  1.000 31.23269  ? 206 ASN B CB    1 
ATOM   5074 C  CG    . ASN B 1 206 ? -7.16200  16.84100  44.13600  1.000 31.64064  ? 206 ASN B CG    1 
ATOM   5075 O  OD1   . ASN B 1 206 ? -7.55900  16.09600  43.23800  1.000 30.20362  ? 206 ASN B OD1   1 
ATOM   5076 N  ND2   . ASN B 1 206 ? -7.38900  18.15000  44.13500  1.000 30.83001  ? 206 ASN B ND2   1 
ATOM   5077 N  N     . HIS B 1 207 ? -5.17800  13.68700  46.28300  1.000 34.57520  ? 207 HIS B N     1 
ATOM   5078 C  CA    . HIS B 1 207 ? -4.27900  12.79600  47.00600  1.000 31.25375  ? 207 HIS B CA    1 
ATOM   5079 C  C     . HIS B 1 207 ? -3.06800  13.54600  47.54900  1.000 34.10409  ? 207 HIS B C     1 
ATOM   5080 O  O     . HIS B 1 207 ? -2.62000  14.54300  46.97900  1.000 36.17013  ? 207 HIS B O     1 
ATOM   5081 C  CB    . HIS B 1 207 ? -3.80000  11.64500  46.11600  1.000 32.03016  ? 207 HIS B CB    1 
ATOM   5082 C  CG    . HIS B 1 207 ? -2.64800  10.87700  46.69200  1.000 30.64315  ? 207 HIS B CG    1 
ATOM   5083 N  ND1   . HIS B 1 207 ? -2.81500  9.80400   47.54400  1.000 27.17957  ? 207 HIS B ND1   1 
ATOM   5084 C  CD2   . HIS B 1 207 ? -1.30900  11.04200  46.55900  1.000 31.29849  ? 207 HIS B CD2   1 
ATOM   5085 C  CE1   . HIS B 1 207 ? -1.63300  9.33600   47.90100  1.000 26.34000  ? 207 HIS B CE1   1 
ATOM   5086 N  NE2   . HIS B 1 207 ? -0.70100  10.07500  47.32300  1.000 29.07980  ? 207 HIS B NE2   1 
ATOM   5087 N  N     . SER B 1 208 ? -2.57800  13.08000  48.69700  1.000 30.55366  ? 208 SER B N     1 
ATOM   5088 C  CA    . SER B 1 208 ? -1.25600  13.42200  49.20700  1.000 29.90095  ? 208 SER B CA    1 
ATOM   5089 C  C     . SER B 1 208 ? -0.69000  12.20900  49.93300  1.000 27.31906  ? 208 SER B C     1 
ATOM   5090 O  O     . SER B 1 208 ? -1.43500  11.43700  50.53600  1.000 26.59266  ? 208 SER B O     1 
ATOM   5091 C  CB    . SER B 1 208 ? -1.30000  14.62600  50.15300  1.000 34.08303  ? 208 SER B CB    1 
ATOM   5092 O  OG    . SER B 1 208 ? -0.02300  14.88400  50.71100  1.000 33.84616  ? 208 SER B OG    1 
ATOM   5093 N  N     . CYS B 1 209 ? 0.63200   12.03000  49.85900  1.000 26.11629  ? 209 CYS B N     1 
ATOM   5094 C  CA    . CYS B 1 209 ? 1.27800   10.98600  50.64900  1.000 28.85083  ? 209 CYS B CA    1 
ATOM   5095 C  C     . CYS B 1 209 ? 1.51900   11.40700  52.09700  1.000 30.73526  ? 209 CYS B C     1 
ATOM   5096 O  O     . CYS B 1 209 ? 2.01000   10.59500  52.88700  1.000 31.55905  ? 209 CYS B O     1 
ATOM   5097 C  CB    . CYS B 1 209 ? 2.59600   10.54500  50.00300  1.000 25.64781  ? 209 CYS B CB    1 
ATOM   5098 S  SG    . CYS B 1 209 ? 2.47600   10.11100  48.23600  1.000 32.03279  ? 209 CYS B SG    1 
ATOM   5099 N  N     . CYS B 1 210 ? 1.23100   12.65900  52.45400  1.000 32.67497  ? 210 CYS B N     1 
ATOM   5100 C  CA    . CYS B 1 210 ? 1.09600   13.08600  53.84700  1.000 39.00468  ? 210 CYS B CA    1 
ATOM   5101 C  C     . CYS B 1 210 ? -0.26500  13.76500  54.01200  1.000 35.05947  ? 210 CYS B C     1 
ATOM   5102 O  O     . CYS B 1 210 ? -0.35900  14.99300  54.12700  1.000 30.57998  ? 210 CYS B O     1 
ATOM   5103 C  CB    . CYS B 1 210 ? 2.24800   13.98700  54.29100  1.000 37.09129  ? 210 CYS B CB    1 
ATOM   5104 S  SG    . CYS B 1 210 ? 2.90700   15.08100  53.04500  1.000 45.88182  ? 210 CYS B SG    1 
ATOM   5105 N  N     . PRO B 1 211 ? -1.33700  12.97700  54.02100  1.000 25.80046  ? 211 PRO B N     1 
ATOM   5106 C  CA    . PRO B 1 211 ? -2.68900  13.55000  54.00400  1.000 28.67712  ? 211 PRO B CA    1 
ATOM   5107 C  C     . PRO B 1 211 ? -3.04400  14.19300  55.33400  1.000 29.45880  ? 211 PRO B C     1 
ATOM   5108 O  O     . PRO B 1 211 ? -2.48100  13.87200  56.38000  1.000 23.45808  ? 211 PRO B O     1 
ATOM   5109 C  CB    . PRO B 1 211 ? -3.57400  12.32700  53.73400  1.000 28.71397  ? 211 PRO B CB    1 
ATOM   5110 C  CG    . PRO B 1 211 ? -2.80400  11.19400  54.36800  1.000 28.41656  ? 211 PRO B CG    1 
ATOM   5111 C  CD    . PRO B 1 211 ? -1.35500  11.50900  54.11800  1.000 27.01377  ? 211 PRO B CD    1 
ATOM   5112 N  N     . ASN B 1 212 ? -4.00500  15.11400  55.29100  1.000 26.74794  ? 212 ASN B N     1 
ATOM   5113 C  CA    . ASN B 1 212 ? -4.50100  15.72000  56.52000  1.000 27.00850  ? 212 ASN B CA    1 
ATOM   5114 C  C     . ASN B 1 212 ? -5.85900  15.18000  56.95900  1.000 29.17718  ? 212 ASN B C     1 
ATOM   5115 O  O     . ASN B 1 212 ? -6.34700  15.56900  58.02800  1.000 23.41860  ? 212 ASN B O     1 
ATOM   5116 C  CB    . ASN B 1 212 ? -4.54000  17.25100  56.40000  1.000 27.85860  ? 212 ASN B CB    1 
ATOM   5117 C  CG    . ASN B 1 212 ? -5.23000  17.73600  55.13600  1.000 28.22707  ? 212 ASN B CG    1 
ATOM   5118 O  OD1   . ASN B 1 212 ? -5.94000  16.98800  54.46600  1.000 24.39766  ? 212 ASN B OD1   1 
ATOM   5119 N  ND2   . ASN B 1 212 ? -5.02000  19.00500  54.80900  1.000 26.06628  ? 212 ASN B ND2   1 
ATOM   5120 N  N     . VAL B 1 213 ? -6.47000  14.27000  56.18900  1.000 20.11031  ? 213 VAL B N     1 
ATOM   5121 C  CA    . VAL B 1 213 ? -7.67800  13.58100  56.62500  1.000 22.85537  ? 213 VAL B CA    1 
ATOM   5122 C  C     . VAL B 1 213 ? -7.54800  12.09400  56.31900  1.000 28.55342  ? 213 VAL B C     1 
ATOM   5123 O  O     . VAL B 1 213 ? -6.70700  11.67000  55.52200  1.000 25.31356  ? 213 VAL B O     1 
ATOM   5124 C  CB    . VAL B 1 213 ? -8.96300  14.15100  55.97700  1.000 22.16845  ? 213 VAL B CB    1 
ATOM   5125 C  CG1   . VAL B 1 213 ? -9.10500  15.62900  56.28800  1.000 25.35567  ? 213 VAL B CG1   1 
ATOM   5126 C  CG2   . VAL B 1 213 ? -8.97800  13.89400  54.46100  1.000 20.81039  ? 213 VAL B CG2   1 
ATOM   5127 N  N     . ILE B 1 214 ? -8.37600  11.29700  56.99900  1.000 29.15613  ? 214 ILE B N     1 
ATOM   5128 C  CA    . ILE B 1 214 ? -8.52700  9.86900   56.73300  1.000 25.78730  ? 214 ILE B CA    1 
ATOM   5129 C  C     . ILE B 1 214 ? -10.01100 9.55600   56.59400  1.000 25.79257  ? 214 ILE B C     1 
ATOM   5130 O  O     . ILE B 1 214 ? -10.84100 10.11200  57.32400  1.000 23.70811  ? 214 ILE B O     1 
ATOM   5131 C  CB    . ILE B 1 214 ? -7.88900  9.00400   57.84600  1.000 27.80597  ? 214 ILE B CB    1 
ATOM   5132 C  CG1   . ILE B 1 214 ? -6.36500  9.07700   57.77800  1.000 46.89510  ? 214 ILE B CG1   1 
ATOM   5133 C  CG2   . ILE B 1 214 ? -8.30600  7.55500   57.73200  1.000 30.71684  ? 214 ILE B CG2   1 
ATOM   5134 C  CD1   . ILE B 1 214 ? -5.67800  8.27900   58.86700  1.000 45.84760  ? 214 ILE B CD1   1 
ATOM   5135 N  N     . VAL B 1 215 ? -10.34400 8.67400   55.64900  1.000 26.61635  ? 215 VAL B N     1 
ATOM   5136 C  CA    . VAL B 1 215 ? -11.70900 8.20600   55.43000  1.000 25.62412  ? 215 VAL B CA    1 
ATOM   5137 C  C     . VAL B 1 215 ? -11.90900 6.88700   56.16200  1.000 26.91902  ? 215 VAL B C     1 
ATOM   5138 O  O     . VAL B 1 215 ? -11.14900 5.93100   55.95500  1.000 24.02393  ? 215 VAL B O     1 
ATOM   5139 C  CB    . VAL B 1 215 ? -12.00600 8.03800   53.92900  1.000 27.82439  ? 215 VAL B CB    1 
ATOM   5140 C  CG1   . VAL B 1 215 ? -13.45100 7.60600   53.72500  1.000 27.38486  ? 215 VAL B CG1   1 
ATOM   5141 C  CG2   . VAL B 1 215 ? -11.71100 9.32700   53.17500  1.000 29.34036  ? 215 VAL B CG2   1 
ATOM   5142 N  N     . THR B 1 216 ? -12.94700 6.82300   56.99500  1.000 25.45042  ? 216 THR B N     1 
ATOM   5143 C  CA    . THR B 1 216 ? -13.36800 5.59500   57.65400  1.000 27.09009  ? 216 THR B CA    1 
ATOM   5144 C  C     . THR B 1 216 ? -14.84400 5.36800   57.34200  1.000 31.38271  ? 216 THR B C     1 
ATOM   5145 O  O     . THR B 1 216 ? -15.49900 6.20100   56.70800  1.000 26.06628  ? 216 THR B O     1 
ATOM   5146 C  CB    . THR B 1 216 ? -13.13200 5.64800   59.17300  1.000 30.54840  ? 216 THR B CB    1 
ATOM   5147 O  OG1   . THR B 1 216 ? -13.88600 6.72300   59.74600  1.000 34.93577  ? 216 THR B OG1   1 
ATOM   5148 C  CG2   . THR B 1 216 ? -11.64700 5.86200   59.47900  1.000 31.05372  ? 216 THR B CG2   1 
ATOM   5149 N  N     . TYR B 1 217 ? -15.37300 4.22800   57.77500  1.000 29.64303  ? 217 TYR B N     1 
ATOM   5150 C  CA    . TYR B 1 217 ? -16.72000 3.82400   57.39800  1.000 30.74053  ? 217 TYR B CA    1 
ATOM   5151 C  C     . TYR B 1 217 ? -17.51800 3.40400   58.62000  1.000 31.11162  ? 217 TYR B C     1 
ATOM   5152 O  O     . TYR B 1 217 ? -17.00500 2.69600   59.49300  1.000 36.43068  ? 217 TYR B O     1 
ATOM   5153 C  CB    . TYR B 1 217 ? -16.68000 2.69400   56.36600  1.000 30.95634  ? 217 TYR B CB    1 
ATOM   5154 C  CG    . TYR B 1 217 ? -15.84500 3.06300   55.16900  1.000 30.31679  ? 217 TYR B CG    1 
ATOM   5155 C  CD1   . TYR B 1 217 ? -16.34900 3.89400   54.17600  1.000 32.31966  ? 217 TYR B CD1   1 
ATOM   5156 C  CD2   . TYR B 1 217 ? -14.53300 2.62500   55.05700  1.000 31.14058  ? 217 TYR B CD2   1 
ATOM   5157 C  CE1   . TYR B 1 217 ? -15.57400 4.25000   53.08400  1.000 32.68550  ? 217 TYR B CE1   1 
ATOM   5158 C  CE2   . TYR B 1 217 ? -13.75400 2.97500   53.97200  1.000 30.97213  ? 217 TYR B CE2   1 
ATOM   5159 C  CZ    . TYR B 1 217 ? -14.27900 3.78400   52.99100  1.000 32.91184  ? 217 TYR B CZ    1 
ATOM   5160 O  OH    . TYR B 1 217 ? -13.49800 4.13100   51.91600  1.000 42.12347  ? 217 TYR B OH    1 
ATOM   5161 N  N     . LYS B 1 218 ? -18.75900 3.87900   58.69100  1.000 34.75680  ? 218 LYS B N     1 
ATOM   5162 C  CA    . LYS B 1 218 ? -19.73800 3.46400   59.69100  1.000 36.66229  ? 218 LYS B CA    1 
ATOM   5163 C  C     . LYS B 1 218 ? -20.83200 2.71500   58.92900  1.000 41.31022  ? 218 LYS B C     1 
ATOM   5164 O  O     . LYS B 1 218 ? -21.81000 3.30500   58.46700  1.000 37.33079  ? 218 LYS B O     1 
ATOM   5165 C  CB    . LYS B 1 218 ? -20.27400 4.67100   60.44800  1.000 41.18915  ? 218 LYS B CB    1 
ATOM   5166 C  CG    . LYS B 1 218 ? -20.91500 4.35500   61.78100  1.000 48.88481  ? 218 LYS B CG    1 
ATOM   5167 C  CD    . LYS B 1 218 ? -21.17300 5.64200   62.54900  1.000 58.44648  ? 218 LYS B CD    1 
ATOM   5168 C  CE    . LYS B 1 218 ? -19.87000 6.23500   63.07400  1.000 55.39875  ? 218 LYS B CE    1 
ATOM   5169 N  NZ    . LYS B 1 218 ? -20.03400 7.62800   63.59200  1.000 52.47734  ? 218 LYS B NZ    1 
ATOM   5170 N  N     . GLY B 1 219 ? -20.64900 1.40800   58.77600  1.000 40.48117  ? 219 GLY B N     1 
ATOM   5171 C  CA    . GLY B 1 219 ? -21.48400 0.66100   57.85900  1.000 39.17838  ? 219 GLY B CA    1 
ATOM   5172 C  C     . GLY B 1 219 ? -21.18000 1.05200   56.42700  1.000 41.97345  ? 219 GLY B C     1 
ATOM   5173 O  O     . GLY B 1 219 ? -20.07000 0.82200   55.93800  1.000 35.14895  ? 219 GLY B O     1 
ATOM   5174 N  N     . THR B 1 220 ? -22.15300 1.64700   55.74400  1.000 39.71002  ? 220 THR B N     1 
ATOM   5175 C  CA    . THR B 1 220 ? -21.96700 2.13400   54.38600  1.000 43.31309  ? 220 THR B CA    1 
ATOM   5176 C  C     . THR B 1 220 ? -21.79800 3.64800   54.33200  1.000 39.51790  ? 220 THR B C     1 
ATOM   5177 O  O     . THR B 1 220 ? -21.77100 4.22200   53.23800  1.000 41.36285  ? 220 THR B O     1 
ATOM   5178 C  CB    . THR B 1 220 ? -23.14200 1.70500   53.50200  1.000 47.50306  ? 220 THR B CB    1 
ATOM   5179 O  OG1   . THR B 1 220 ? -24.33700 2.36300   53.93800  1.000 48.95850  ? 220 THR B OG1   1 
ATOM   5180 C  CG2   . THR B 1 220 ? -23.34100 0.19700   53.58100  1.000 49.86914  ? 220 THR B CG2   1 
ATOM   5181 N  N     . LEU B 1 221 ? -21.68300 4.30300   55.48500  1.000 45.38439  ? 221 LEU B N     1 
ATOM   5182 C  CA    . LEU B 1 221 ? -21.51100 5.74900   55.56300  1.000 44.80011  ? 221 LEU B CA    1 
ATOM   5183 C  C     . LEU B 1 221 ? -20.02700 6.08000   55.67300  1.000 37.56240  ? 221 LEU B C     1 
ATOM   5184 O  O     . LEU B 1 221 ? -19.34700 5.59900   56.58700  1.000 33.24872  ? 221 LEU B O     1 
ATOM   5185 C  CB    . LEU B 1 221 ? -22.27000 6.31800   56.76000  1.000 41.79712  ? 221 LEU B CB    1 
ATOM   5186 C  CG    . LEU B 1 221 ? -22.11500 7.82200   56.99800  1.000 50.06916  ? 221 LEU B CG    1 
ATOM   5187 C  CD1   . LEU B 1 221 ? -22.97200 8.62100   56.03000  1.000 49.19537  ? 221 LEU B CD1   1 
ATOM   5188 C  CD2   . LEU B 1 221 ? -22.44900 8.17300   58.43600  1.000 48.27684  ? 221 LEU B CD2   1 
ATOM   5189 N  N     . ALA B 1 222 ? -19.52700 6.89300   54.74300  1.000 27.56646  ? 222 ALA B N     1 
ATOM   5190 C  CA    . ALA B 1 222 ? -18.15200 7.36500   54.81400  1.000 31.77486  ? 222 ALA B CA    1 
ATOM   5191 C  C     . ALA B 1 222 ? -18.05300 8.58600   55.71900  1.000 33.92512  ? 222 ALA B C     1 
ATOM   5192 O  O     . ALA B 1 222 ? -18.89800 9.48400   55.66900  1.000 40.95491  ? 222 ALA B O     1 
ATOM   5193 C  CB    . ALA B 1 222 ? -17.62800 7.70800   53.41900  1.000 30.92213  ? 222 ALA B CB    1 
ATOM   5194 N  N     . GLU B 1 223 ? -17.01000 8.61500   56.54700  1.000 31.98541  ? 223 GLU B N     1 
ATOM   5195 C  CA    . GLU B 1 223 ? -16.72600 9.73600   57.43100  1.000 31.65906  ? 223 GLU B CA    1 
ATOM   5196 C  C     . GLU B 1 223 ? -15.29500 10.19500  57.18700  1.000 28.78503  ? 223 GLU B C     1 
ATOM   5197 O  O     . GLU B 1 223 ? -14.41500 9.37700   56.91300  1.000 24.15553  ? 223 GLU B O     1 
ATOM   5198 C  CB    . GLU B 1 223 ? -16.91600 9.35600   58.91200  1.000 34.32254  ? 223 GLU B CB    1 
ATOM   5199 C  CG    . GLU B 1 223 ? -18.34500 8.94700   59.27300  1.000 39.61264  ? 223 GLU B CG    1 
ATOM   5200 C  CD    . GLU B 1 223 ? -18.56300 8.82600   60.77200  1.000 49.75333  ? 223 GLU B CD    1 
ATOM   5201 O  OE1   . GLU B 1 223 ? -17.64500 8.35100   61.47400  1.000 51.31142  ? 223 GLU B OE1   1 
ATOM   5202 O  OE2   . GLU B 1 223 ? -19.65700 9.19700   61.25000  1.000 50.67713  ? 223 GLU B OE2   1 
ATOM   5203 N  N     . VAL B 1 224 ? -15.06900 11.50400  57.27800  1.000 26.00575  ? 224 VAL B N     1 
ATOM   5204 C  CA    . VAL B 1 224 ? -13.78400 12.11900  56.95900  1.000 24.33186  ? 224 VAL B CA    1 
ATOM   5205 C  C     . VAL B 1 224 ? -13.33500 12.93000  58.16700  1.000 23.85812  ? 224 VAL B C     1 
ATOM   5206 O  O     . VAL B 1 224 ? -14.00300 13.89900  58.54800  1.000 28.32971  ? 224 VAL B O     1 
ATOM   5207 C  CB    . VAL B 1 224 ? -13.87500 13.00900  55.70700  1.000 28.54026  ? 224 VAL B CB    1 
ATOM   5208 C  CG1   . VAL B 1 224 ? -12.52600 13.65500  55.40600  1.000 28.62712  ? 224 VAL B CG1   1 
ATOM   5209 C  CG2   . VAL B 1 224 ? -14.36700 12.19900  54.51000  1.000 32.72761  ? 224 VAL B CG2   1 
ATOM   5210 N  N     . ARG B 1 225 ? -12.21500 12.53800  58.77200  1.000 21.38677  ? 225 ARG B N     1 
ATOM   5211 C  CA    . ARG B 1 225 ? -11.73200 13.17300  59.99000  1.000 21.72892  ? 225 ARG B CA    1 
ATOM   5212 C  C     . ARG B 1 225 ? -10.29400 13.63600  59.81500  1.000 20.62879  ? 225 ARG B C     1 
ATOM   5213 O  O     . ARG B 1 225 ? -9.50200  12.98200  59.12800  1.000 23.50019  ? 225 ARG B O     1 
ATOM   5214 C  CB    . ARG B 1 225 ? -11.84100 12.22200  61.19500  1.000 24.27133  ? 225 ARG B CB    1 
ATOM   5215 C  CG    . ARG B 1 225 ? -13.25300 12.16300  61.75900  1.000 26.53476  ? 225 ARG B CG    1 
ATOM   5216 C  CD    . ARG B 1 225 ? -13.35000 11.31100  63.00600  1.000 30.25363  ? 225 ARG B CD    1 
ATOM   5217 N  NE    . ARG B 1 225 ? -14.73800 11.20100  63.44900  1.000 30.54314  ? 225 ARG B NE    1 
ATOM   5218 C  CZ    . ARG B 1 225 ? -15.62800 10.37600  62.90300  1.000 29.26140  ? 225 ARG B CZ    1 
ATOM   5219 N  NH1   . ARG B 1 225 ? -15.27400 9.58400   61.89700  1.000 33.14871  ? 225 ARG B NH1   1 
ATOM   5220 N  NH2   . ARG B 1 225 ? -16.87000 10.33600  63.36500  1.000 33.10397  ? 225 ARG B NH2   1 
ATOM   5221 N  N     . ALA B 1 226 ? -9.96700  14.76900  60.44400  1.000 22.23951  ? 226 ALA B N     1 
ATOM   5222 C  CA    . ALA B 1 226 ? -8.62800  15.33900  60.35200  1.000 24.10289  ? 226 ALA B CA    1 
ATOM   5223 C  C     . ALA B 1 226 ? -7.61300  14.52300  61.14700  1.000 24.81613  ? 226 ALA B C     1 
ATOM   5224 O  O     . ALA B 1 226 ? -7.86500  14.12500  62.28900  1.000 27.96125  ? 226 ALA B O     1 
ATOM   5225 C  CB    . ALA B 1 226 ? -8.62800  16.78200  60.85700  1.000 25.23460  ? 226 ALA B CB    1 
ATOM   5226 N  N     . VAL B 1 227 ? -6.45900  14.27200  60.53100  1.000 25.54517  ? 227 VAL B N     1 
ATOM   5227 C  CA    . VAL B 1 227 ? -5.31400  13.68300  61.21000  1.000 24.20817  ? 227 VAL B CA    1 
ATOM   5228 C  C     . VAL B 1 227 ? -4.13800  14.64000  61.27700  1.000 19.95502  ? 227 VAL B C     1 
ATOM   5229 O  O     . VAL B 1 227 ? -3.08400  14.28200  61.81200  1.000 23.54756  ? 227 VAL B O     1 
ATOM   5230 C  CB    . VAL B 1 227 ? -4.89300  12.35300  60.55200  1.000 26.51897  ? 227 VAL B CB    1 
ATOM   5231 C  CG1   . VAL B 1 227 ? -6.02400  11.34000  60.67200  1.000 26.14787  ? 227 VAL B CG1   1 
ATOM   5232 C  CG2   . VAL B 1 227 ? -4.51000  12.57400  59.07800  1.000 21.95526  ? 227 VAL B CG2   1 
ATOM   5233 N  N     . GLN B 1 228 ? -4.28400  15.83300  60.71400  1.000 30.98529  ? 228 GLN B N     1 
ATOM   5234 C  CA    . GLN B 1 228 ? -3.41600  16.97100  60.94800  1.000 31.50641  ? 228 GLN B CA    1 
ATOM   5235 C  C     . GLN B 1 228 ? -4.31900  18.17600  61.16100  1.000 31.13005  ? 228 GLN B C     1 
ATOM   5236 O  O     . GLN B 1 228 ? -5.49100  18.17500  60.76400  1.000 26.74005  ? 228 GLN B O     1 
ATOM   5237 C  CB    . GLN B 1 228 ? -2.47200  17.25000  59.76700  1.000 30.78790  ? 228 GLN B CB    1 
ATOM   5238 C  CG    . GLN B 1 228 ? -1.46800  16.15800  59.47300  1.000 39.46789  ? 228 GLN B CG    1 
ATOM   5239 C  CD    . GLN B 1 228 ? -0.51800  16.54200  58.35400  1.000 34.08040  ? 228 GLN B CD    1 
ATOM   5240 O  OE1   . GLN B 1 228 ? 0.17600   17.55400  58.43400  1.000 52.28785  ? 228 GLN B OE1   1 
ATOM   5241 N  NE2   . GLN B 1 228 ? -0.49200  15.73900  57.30100  1.000 46.72929  ? 228 GLN B NE2   1 
ATOM   5242 N  N     . GLU B 1 229 ? -3.76900  19.21000  61.78200  1.000 31.09847  ? 229 GLU B N     1 
ATOM   5243 C  CA    . GLU B 1 229 ? -4.49900  20.46400  61.88000  1.000 34.43044  ? 229 GLU B CA    1 
ATOM   5244 C  C     . GLU B 1 229 ? -4.68200  21.06500  60.48800  1.000 33.76984  ? 229 GLU B C     1 
ATOM   5245 O  O     . GLU B 1 229 ? -3.75400  21.08200  59.67600  1.000 32.40125  ? 229 GLU B O     1 
ATOM   5246 C  CB    . GLU B 1 229 ? -3.75700  21.43600  62.79400  1.000 37.80980  ? 229 GLU B CB    1 
ATOM   5247 C  CG    . GLU B 1 229 ? -4.51700  22.72600  63.03400  1.000 73.34827  ? 229 GLU B CG    1 
ATOM   5248 C  CD    . GLU B 1 229 ? -4.01300  23.49900  64.23600  1.000 101.05949 ? 229 GLU B CD    1 
ATOM   5249 O  OE1   . GLU B 1 229 ? -2.80300  23.41700  64.55200  1.000 91.71626  ? 229 GLU B OE1   1 
ATOM   5250 O  OE2   . GLU B 1 229 ? -4.83400  24.21400  64.84900  1.000 48.46634  ? 229 GLU B OE2   1 
ATOM   5251 N  N     . ILE B 1 230 ? -5.89400  21.53800  60.20600  1.000 33.01975  ? 230 ILE B N     1 
ATOM   5252 C  CA    . ILE B 1 230 ? -6.24400  22.12700  58.92000  1.000 33.50665  ? 230 ILE B CA    1 
ATOM   5253 C  C     . ILE B 1 230 ? -6.67000  23.57300  59.15200  1.000 36.18065  ? 230 ILE B C     1 
ATOM   5254 O  O     . ILE B 1 230 ? -7.53400  23.83900  59.99400  1.000 42.42351  ? 230 ILE B O     1 
ATOM   5255 C  CB    . ILE B 1 230 ? -7.36300  21.33400  58.21800  1.000 31.63011  ? 230 ILE B CB    1 
ATOM   5256 C  CG1   . ILE B 1 230 ? -6.96500  19.86200  58.04300  1.000 31.29323  ? 230 ILE B CG1   1 
ATOM   5257 C  CG2   . ILE B 1 230 ? -7.71900  21.97300  56.88000  1.000 32.78025  ? 230 ILE B CG2   1 
ATOM   5258 C  CD1   . ILE B 1 230 ? -8.09800  18.97700  57.53700  1.000 35.09368  ? 230 ILE B CD1   1 
ATOM   5259 N  N     . LYS B 1 231 ? -6.07500  24.50500  58.39000  1.000 32.50916  ? 231 LYS B N     1 
ATOM   5260 C  CA    . LYS B 1 231 ? -6.35200  25.93100  58.53000  1.000 31.56431  ? 231 LYS B CA    1 
ATOM   5261 C  C     . LYS B 1 231 ? -7.20500  26.43500  57.36800  1.000 30.36154  ? 231 LYS B C     1 
ATOM   5262 O  O     . LYS B 1 231 ? -7.21200  25.82500  56.29500  1.000 28.72713  ? 231 LYS B O     1 
ATOM   5263 C  CB    . LYS B 1 231 ? -5.05100  26.74300  58.58500  1.000 37.74926  ? 231 LYS B CB    1 
ATOM   5264 C  CG    . LYS B 1 231 ? -4.14600  26.37300  59.74700  1.000 37.41764  ? 231 LYS B CG    1 
ATOM   5265 C  CD    . LYS B 1 231 ? -4.88100  26.51800  61.07400  1.000 50.61660  ? 231 LYS B CD    1 
ATOM   5266 C  CE    . LYS B 1 231 ? -3.91200  26.62500  62.23900  1.000 62.47854  ? 231 LYS B CE    1 
ATOM   5267 N  NZ    . LYS B 1 231 ? -4.62400  26.85700  63.52500  1.000 91.94787  ? 231 LYS B NZ    1 
ATOM   5268 N  N     . PRO B 1 232 ? -7.94600  27.53200  57.55500  1.000 33.96197  ? 232 PRO B N     1 
ATOM   5269 C  CA    . PRO B 1 232 ? -8.70400  28.11000  56.43900  1.000 40.97597  ? 232 PRO B CA    1 
ATOM   5270 C  C     . PRO B 1 232 ? -7.80700  28.38000  55.23900  1.000 38.88887  ? 232 PRO B C     1 
ATOM   5271 O  O     . PRO B 1 232 ? -6.69500  28.89600  55.37300  1.000 36.81231  ? 232 PRO B O     1 
ATOM   5272 C  CB    . PRO B 1 232 ? -9.26200  29.41000  57.03000  1.000 37.27026  ? 232 PRO B CB    1 
ATOM   5273 C  CG    . PRO B 1 232 ? -9.36600  29.13400  58.49100  1.000 36.28593  ? 232 PRO B CG    1 
ATOM   5274 C  CD    . PRO B 1 232 ? -8.19500  28.25000  58.81900  1.000 35.85693  ? 232 PRO B CD    1 
ATOM   5275 N  N     . GLY B 1 233 ? -8.30400  28.02600  54.05300  1.000 35.19633  ? 233 GLY B N     1 
ATOM   5276 C  CA    . GLY B 1 233 ? -7.56300  28.18400  52.82400  1.000 38.87045  ? 233 GLY B CA    1 
ATOM   5277 C  C     . GLY B 1 233 ? -6.75200  26.97600  52.40100  1.000 38.44408  ? 233 GLY B C     1 
ATOM   5278 O  O     . GLY B 1 233 ? -6.33500  26.90400  51.23800  1.000 39.17312  ? 233 GLY B O     1 
ATOM   5279 N  N     . GLU B 1 234 ? -6.50500  26.03200  53.30600  1.000 37.10445  ? 234 GLU B N     1 
ATOM   5280 C  CA    . GLU B 1 234 ? -5.68400  24.87100  52.98600  1.000 36.85968  ? 234 GLU B CA    1 
ATOM   5281 C  C     . GLU B 1 234 ? -6.52200  23.78900  52.31900  1.000 33.51454  ? 234 GLU B C     1 
ATOM   5282 O  O     . GLU B 1 234 ? -7.70000  23.60500  52.63900  1.000 30.91950  ? 234 GLU B O     1 
ATOM   5283 C  CB    . GLU B 1 234 ? -5.01600  24.32300  54.24800  1.000 35.54900  ? 234 GLU B CB    1 
ATOM   5284 C  CG    . GLU B 1 234 ? -4.08500  25.32500  54.92100  1.000 42.29191  ? 234 GLU B CG    1 
ATOM   5285 C  CD    . GLU B 1 234 ? -3.22300  24.69800  56.00500  1.000 53.76697  ? 234 GLU B CD    1 
ATOM   5286 O  OE1   . GLU B 1 234 ? -3.71500  23.77800  56.69800  1.000 44.50534  ? 234 GLU B OE1   1 
ATOM   5287 O  OE2   . GLU B 1 234 ? -2.06100  25.13900  56.17500  1.000 45.24753  ? 234 GLU B OE2   1 
ATOM   5288 N  N     . GLU B 1 235 ? -5.90600  23.07900  51.37900  1.000 29.94306  ? 235 GLU B N     1 
ATOM   5289 C  CA    . GLU B 1 235 ? -6.59200  22.01100  50.67100  1.000 30.19309  ? 235 GLU B CA    1 
ATOM   5290 C  C     . GLU B 1 235 ? -6.67600  20.76200  51.53900  1.000 28.03757  ? 235 GLU B C     1 
ATOM   5291 O  O     . GLU B 1 235 ? -5.76700  20.46400  52.32500  1.000 25.12143  ? 235 GLU B O     1 
ATOM   5292 C  CB    . GLU B 1 235 ? -5.88200  21.70800  49.34800  1.000 30.93792  ? 235 GLU B CB    1 
ATOM   5293 C  CG    . GLU B 1 235 ? -6.47600  20.54300  48.56800  1.000 29.66671  ? 235 GLU B CG    1 
ATOM   5294 C  CD    . GLU B 1 235 ? -6.17700  20.61500  47.07500  1.000 35.48583  ? 235 GLU B CD    1 
ATOM   5295 O  OE1   . GLU B 1 235 ? -5.35700  21.46600  46.66500  1.000 42.34718  ? 235 GLU B OE1   1 
ATOM   5296 O  OE2   . GLU B 1 235 ? -6.76100  19.81500  46.31000  1.000 39.94426  ? 235 GLU B OE2   1 
ATOM   5297 N  N     . VAL B 1 236 ? -7.79100  20.04800  51.40600  1.000 24.47662  ? 236 VAL B N     1 
ATOM   5298 C  CA    . VAL B 1 236 ? -8.02900  18.80300  52.12300  1.000 24.01604  ? 236 VAL B CA    1 
ATOM   5299 C  C     . VAL B 1 236 ? -7.54400  17.64700  51.25600  1.000 24.33976  ? 236 VAL B C     1 
ATOM   5300 O  O     . VAL B 1 236 ? -7.97900  17.49500  50.10700  1.000 26.15840  ? 236 VAL B O     1 
ATOM   5301 C  CB    . VAL B 1 236 ? -9.51500  18.64200  52.47100  1.000 26.54792  ? 236 VAL B CB    1 
ATOM   5302 C  CG1   . VAL B 1 236 ? -9.71500  17.40000  53.31200  1.000 27.20853  ? 236 VAL B CG1   1 
ATOM   5303 C  CG2   . VAL B 1 236 ? -10.00600 19.88000  53.20500  1.000 28.34550  ? 236 VAL B CG2   1 
ATOM   5304 N  N     . PHE B 1 237 ? -6.63500  16.84000  51.80000  1.000 25.43989  ? 237 PHE B N     1 
ATOM   5305 C  CA    . PHE B 1 237 ? -6.00900  15.75100  51.06500  1.000 27.40329  ? 237 PHE B CA    1 
ATOM   5306 C  C     . PHE B 1 237 ? -6.22800  14.43800  51.79700  1.000 27.19273  ? 237 PHE B C     1 
ATOM   5307 O  O     . PHE B 1 237 ? -5.94600  14.33500  52.99800  1.000 25.56622  ? 237 PHE B O     1 
ATOM   5308 C  CB    . PHE B 1 237 ? -4.50300  15.96500  50.90100  1.000 29.08243  ? 237 PHE B CB    1 
ATOM   5309 C  CG    . PHE B 1 237 ? -4.13100  17.11200  50.01300  1.000 27.86650  ? 237 PHE B CG    1 
ATOM   5310 C  CD1   . PHE B 1 237 ? -4.29800  17.02500  48.64200  1.000 29.50091  ? 237 PHE B CD1   1 
ATOM   5311 C  CD2   . PHE B 1 237 ? -3.54900  18.25300  50.54700  1.000 33.41716  ? 237 PHE B CD2   1 
ATOM   5312 C  CE1   . PHE B 1 237 ? -3.93100  18.07200  47.82300  1.000 30.71947  ? 237 PHE B CE1   1 
ATOM   5313 C  CE2   . PHE B 1 237 ? -3.17200  19.30200  49.73600  1.000 33.26451  ? 237 PHE B CE2   1 
ATOM   5314 C  CZ    . PHE B 1 237 ? -3.36200  19.21500  48.36800  1.000 31.86435  ? 237 PHE B CZ    1 
ATOM   5315 N  N     . THR B 1 238 ? -6.68900  13.43200  51.06900  1.000 25.55833  ? 238 THR B N     1 
ATOM   5316 C  CA    . THR B 1 238 ? -6.71100  12.06300  51.55600  1.000 28.65344  ? 238 THR B CA    1 
ATOM   5317 C  C     . THR B 1 238 ? -5.60700  11.29200  50.84100  1.000 30.60630  ? 238 THR B C     1 
ATOM   5318 O  O     . THR B 1 238 ? -4.99400  11.79400  49.90000  1.000 31.80908  ? 238 THR B O     1 
ATOM   5319 C  CB    . THR B 1 238 ? -8.09100  11.43300  51.31500  1.000 29.13244  ? 238 THR B CB    1 
ATOM   5320 O  OG1   . THR B 1 238 ? -8.21400  10.22400  52.07400  1.000 41.81817  ? 238 THR B OG1   1 
ATOM   5321 C  CG2   . THR B 1 238 ? -8.29400  11.13300  49.83500  1.000 29.41668  ? 238 THR B CG2   1 
ATOM   5322 N  N     . SER B 1 239 ? -5.33400  10.07100  51.28900  1.000 31.81960  ? 239 SER B N     1 
ATOM   5323 C  CA    . SER B 1 239 ? -4.39000  9.20800   50.59100  1.000 27.91387  ? 239 SER B CA    1 
ATOM   5324 C  C     . SER B 1 239 ? -5.14600  8.16200   49.78800  1.000 29.30615  ? 239 SER B C     1 
ATOM   5325 O  O     . SER B 1 239 ? -6.08700  7.54000   50.29300  1.000 28.61922  ? 239 SER B O     1 
ATOM   5326 C  CB    . SER B 1 239 ? -3.42300  8.51600   51.54600  1.000 32.60391  ? 239 SER B CB    1 
ATOM   5327 O  OG    . SER B 1 239 ? -2.57200  7.65500   50.80300  1.000 32.85394  ? 239 SER B OG    1 
ATOM   5328 N  N     . TYR B 1 240 ? -4.72500  7.96600   48.54200  1.000 26.86375  ? 240 TYR B N     1 
ATOM   5329 C  CA    . TYR B 1 240 ? -5.35400  6.98700   47.67000  1.000 27.78228  ? 240 TYR B CA    1 
ATOM   5330 C  C     . TYR B 1 240 ? -4.73100  5.60300   47.78300  1.000 25.80573  ? 240 TYR B C     1 
ATOM   5331 O  O     . TYR B 1 240 ? -5.30400  4.64300   47.26200  1.000 26.38474  ? 240 TYR B O     1 
ATOM   5332 C  CB    . TYR B 1 240 ? -5.26000  7.41500   46.20400  1.000 29.71935  ? 240 TYR B CB    1 
ATOM   5333 C  CG    . TYR B 1 240 ? -5.98700  8.68000   45.80900  1.000 28.20865  ? 240 TYR B CG    1 
ATOM   5334 C  CD1   . TYR B 1 240 ? -6.64200  9.47800   46.74200  1.000 26.46370  ? 240 TYR B CD1   1 
ATOM   5335 C  CD2   . TYR B 1 240 ? -6.01200  9.07200   44.48400  1.000 26.42948  ? 240 TYR B CD2   1 
ATOM   5336 C  CE1   . TYR B 1 240 ? -7.29800  10.63400  46.35100  1.000 25.13196  ? 240 TYR B CE1   1 
ATOM   5337 C  CE2   . TYR B 1 240 ? -6.66000  10.20900  44.08700  1.000 29.29825  ? 240 TYR B CE2   1 
ATOM   5338 C  CZ    . TYR B 1 240 ? -7.30500  10.98900  45.01500  1.000 29.71146  ? 240 TYR B CZ    1 
ATOM   5339 O  OH    . TYR B 1 240 ? -7.95200  12.13000  44.58600  1.000 30.52471  ? 240 TYR B OH    1 
ATOM   5340 N  N     . ILE B 1 241 ? -3.55200  5.47900   48.39800  1.000 29.26930  ? 241 ILE B N     1 
ATOM   5341 C  CA    . ILE B 1 241 ? -2.74100  4.27400   48.29200  1.000 32.22228  ? 241 ILE B CA    1 
ATOM   5342 C  C     . ILE B 1 241 ? -2.15200  3.91400   49.65200  1.000 28.52710  ? 241 ILE B C     1 
ATOM   5343 O  O     . ILE B 1 241 ? -2.22200  4.67800   50.61700  1.000 25.66360  ? 241 ILE B O     1 
ATOM   5344 C  CB    . ILE B 1 241 ? -1.60700  4.44300   47.26000  1.000 34.35412  ? 241 ILE B CB    1 
ATOM   5345 C  CG1   . ILE B 1 241 ? -0.74900  5.66000   47.62700  1.000 37.73610  ? 241 ILE B CG1   1 
ATOM   5346 C  CG2   . ILE B 1 241 ? -2.17300  4.56400   45.84900  1.000 40.55486  ? 241 ILE B CG2   1 
ATOM   5347 C  CD1   . ILE B 1 241 ? 0.55700   5.74900   46.87300  1.000 41.56025  ? 241 ILE B CD1   1 
ATOM   5348 N  N     . ASP B 1 242 ? -1.56400  2.72000   49.70500  1.000 28.63501  ? 242 ASP B N     1 
ATOM   5349 C  CA    . ASP B 1 242 ? -0.76600  2.28300   50.84500  1.000 27.16115  ? 242 ASP B CA    1 
ATOM   5350 C  C     . ASP B 1 242 ? 0.53700   3.07700   50.86700  1.000 30.03518  ? 242 ASP B C     1 
ATOM   5351 O  O     . ASP B 1 242 ? 1.31600   3.02500   49.90900  1.000 31.76170  ? 242 ASP B O     1 
ATOM   5352 C  CB    . ASP B 1 242 ? -0.50400  0.78100   50.71900  1.000 30.08255  ? 242 ASP B CB    1 
ATOM   5353 C  CG    . ASP B 1 242 ? 0.05300   0.15100   51.98900  1.000 28.06915  ? 242 ASP B CG    1 
ATOM   5354 O  OD1   . ASP B 1 242 ? 0.68100   0.85700   52.80900  1.000 27.80070  ? 242 ASP B OD1   1 
ATOM   5355 O  OD2   . ASP B 1 242 ? -0.14100  -1.07400  52.15200  1.000 31.54326  ? 242 ASP B OD2   1 
ATOM   5356 N  N     . LEU B 1 243 ? 0.77400   3.81300   51.95100  1.000 23.55809  ? 243 LEU B N     1 
ATOM   5357 C  CA    . LEU B 1 243 ? 1.90900   4.72300   52.05800  1.000 24.20290  ? 243 LEU B CA    1 
ATOM   5358 C  C     . LEU B 1 243 ? 3.17700   4.04900   52.56800  1.000 23.90287  ? 243 LEU B C     1 
ATOM   5359 O  O     . LEU B 1 243 ? 4.15600   4.74500   52.85200  1.000 31.36165  ? 243 LEU B O     1 
ATOM   5360 C  CB    . LEU B 1 243 ? 1.55800   5.90200   52.97200  1.000 28.77713  ? 243 LEU B CB    1 
ATOM   5361 C  CG    . LEU B 1 243 ? 0.39200   6.77300   52.49400  1.000 31.73538  ? 243 LEU B CG    1 
ATOM   5362 C  CD1   . LEU B 1 243 ? 0.03100   7.81300   53.54900  1.000 31.93804  ? 243 LEU B CD1   1 
ATOM   5363 C  CD2   . LEU B 1 243 ? 0.71900   7.42000   51.15500  1.000 34.90418  ? 243 LEU B CD2   1 
ATOM   5364 N  N     . LEU B 1 244 ? 3.17800   2.71900   52.70500  1.000 23.91603  ? 244 LEU B N     1 
ATOM   5365 C  CA    . LEU B 1 244 ? 4.35400   2.02900   53.22800  1.000 28.51395  ? 244 LEU B CA    1 
ATOM   5366 C  C     . LEU B 1 244 ? 5.54800   2.16400   52.28600  1.000 25.39778  ? 244 LEU B C     1 
ATOM   5367 O  O     . LEU B 1 244 ? 6.69400   2.27300   52.73700  1.000 29.09033  ? 244 LEU B O     1 
ATOM   5368 C  CB    . LEU B 1 244 ? 4.03300   0.55200   53.47000  1.000 28.89031  ? 244 LEU B CB    1 
ATOM   5369 C  CG    . LEU B 1 244 ? 5.19900   -0.30300  53.98900  1.000 25.70571  ? 244 LEU B CG    1 
ATOM   5370 C  CD1   . LEU B 1 244 ? 5.72300   0.21200   55.32300  1.000 32.56443  ? 244 LEU B CD1   1 
ATOM   5371 C  CD2   . LEU B 1 244 ? 4.82000   -1.77600  54.08200  1.000 36.21224  ? 244 LEU B CD2   1 
ATOM   5372 N  N     . TYR B 1 245 ? 5.30100   2.16100   50.97900  1.000 29.10612  ? 245 TYR B N     1 
ATOM   5373 C  CA    . TYR B 1 245 ? 6.33500   1.93300   49.98100  1.000 30.32206  ? 245 TYR B CA    1 
ATOM   5374 C  C     . TYR B 1 245 ? 7.07000   3.22000   49.62300  1.000 29.47985  ? 245 TYR B C     1 
ATOM   5375 O  O     . TYR B 1 245 ? 6.58900   4.32700   49.89600  1.000 29.73514  ? 245 TYR B O     1 
ATOM   5376 C  CB    . TYR B 1 245 ? 5.70800   1.28300   48.75000  1.000 33.58297  ? 245 TYR B CB    1 
ATOM   5377 C  CG    . TYR B 1 245 ? 5.02100   0.00700   49.14400  1.000 33.05133  ? 245 TYR B CG    1 
ATOM   5378 C  CD1   . TYR B 1 245 ? 5.74900   -1.15400  49.36300  1.000 35.92010  ? 245 TYR B CD1   1 
ATOM   5379 C  CD2   . TYR B 1 245 ? 3.65200   -0.02100  49.37800  1.000 42.78934  ? 245 TYR B CD2   1 
ATOM   5380 C  CE1   . TYR B 1 245 ? 5.12900   -2.32100  49.76300  1.000 43.10780  ? 245 TYR B CE1   1 
ATOM   5381 C  CE2   . TYR B 1 245 ? 3.02100   -1.18500  49.77700  1.000 39.73634  ? 245 TYR B CE2   1 
ATOM   5382 C  CZ    . TYR B 1 245 ? 3.76500   -2.33000  49.97100  1.000 36.37805  ? 245 TYR B CZ    1 
ATOM   5383 O  OH    . TYR B 1 245 ? 3.13500   -3.48400  50.36600  1.000 34.91471  ? 245 TYR B OH    1 
ATOM   5384 N  N     . PRO B 1 246 ? 8.28400   3.11200   49.03900  1.000 30.80633  ? 246 PRO B N     1 
ATOM   5385 C  CA    . PRO B 1 246 ? 9.04700   4.32300   48.71000  1.000 33.71457  ? 246 PRO B CA    1 
ATOM   5386 C  C     . PRO B 1 246 ? 8.43300   5.12100   47.56700  1.000 35.04894  ? 246 PRO B C     1 
ATOM   5387 O  O     . PRO B 1 246 ? 7.44900   4.69100   46.95300  1.000 31.78276  ? 246 PRO B O     1 
ATOM   5388 C  CB    . PRO B 1 246 ? 10.43700  3.78100   48.35200  1.000 34.46203  ? 246 PRO B CB    1 
ATOM   5389 C  CG    . PRO B 1 246 ? 10.22500  2.37100   47.97700  1.000 33.92249  ? 246 PRO B CG    1 
ATOM   5390 C  CD    . PRO B 1 246 ? 9.04800   1.88000   48.76300  1.000 30.79317  ? 246 PRO B CD    1 
ATOM   5391 N  N     . THR B 1 247 ? 9.02700   6.28500   47.27900  1.000 32.62760  ? 247 THR B N     1 
ATOM   5392 C  CA    . THR B 1 247 ? 8.38600   7.28100   46.42300  1.000 34.96735  ? 247 THR B CA    1 
ATOM   5393 C  C     . THR B 1 247 ? 8.16200   6.77000   45.00200  1.000 40.59960  ? 247 THR B C     1 
ATOM   5394 O  O     . THR B 1 247 ? 7.08100   6.97100   44.43500  1.000 36.54122  ? 247 THR B O     1 
ATOM   5395 C  CB    . THR B 1 247 ? 9.21500   8.56900   46.42100  1.000 36.25961  ? 247 THR B CB    1 
ATOM   5396 O  OG1   . THR B 1 247 ? 9.26200   9.10300   47.75300  1.000 31.30112  ? 247 THR B OG1   1 
ATOM   5397 C  CG2   . THR B 1 247 ? 8.62300   9.61300   45.47100  1.000 39.14154  ? 247 THR B CG2   1 
ATOM   5398 N  N     . GLU B 1 248 ? 9.16000   6.10900   44.40300  1.000 45.28174  ? 248 GLU B N     1 
ATOM   5399 C  CA    . GLU B 1 248 ? 8.96400   5.64400   43.03100  1.000 42.92620  ? 248 GLU B CA    1 
ATOM   5400 C  C     . GLU B 1 248 ? 7.88400   4.57300   42.95800  1.000 40.72330  ? 248 GLU B C     1 
ATOM   5401 O  O     . GLU B 1 248 ? 7.11900   4.53700   41.98700  1.000 40.74699  ? 248 GLU B O     1 
ATOM   5402 C  CB    . GLU B 1 248 ? 10.26900  5.12300   42.42100  1.000 49.33486  ? 248 GLU B CB    1 
ATOM   5403 C  CG    . GLU B 1 248 ? 10.78500  3.81000   42.98600  1.000 75.41431  ? 248 GLU B CG    1 
ATOM   5404 C  CD    . GLU B 1 248 ? 11.94900  3.24300   42.18300  1.000 87.24993  ? 248 GLU B CD    1 
ATOM   5405 O  OE1   . GLU B 1 248 ? 12.48500  3.97200   41.32100  1.000 73.74042  ? 248 GLU B OE1   1 
ATOM   5406 O  OE2   . GLU B 1 248 ? 12.31600  2.06500   42.40600  1.000 71.96916  ? 248 GLU B OE2   1 
ATOM   5407 N  N     . ASP B 1 249 ? 7.77000   3.72900   43.99000  1.000 41.95503  ? 249 ASP B N     1 
ATOM   5408 C  CA    . ASP B 1 249 ? 6.71600   2.71900   43.99900  1.000 41.73658  ? 249 ASP B CA    1 
ATOM   5409 C  C     . ASP B 1 249 ? 5.34300   3.36900   44.08400  1.000 34.26200  ? 249 ASP B C     1 
ATOM   5410 O  O     . ASP B 1 249 ? 4.41800   2.98300   43.36200  1.000 42.36034  ? 249 ASP B O     1 
ATOM   5411 C  CB    . ASP B 1 249 ? 6.91000   1.75600   45.17300  1.000 50.87189  ? 249 ASP B CB    1 
ATOM   5412 C  CG    . ASP B 1 249 ? 8.21300   0.98600   45.08900  1.000 45.26069  ? 249 ASP B CG    1 
ATOM   5413 O  OD1   . ASP B 1 249 ? 9.05200   1.33400   44.23500  1.000 61.32314  ? 249 ASP B OD1   1 
ATOM   5414 O  OD2   . ASP B 1 249 ? 8.39000   0.01600   45.85400  1.000 55.53561  ? 249 ASP B OD2   1 
ATOM   5415 N  N     . ARG B 1 250 ? 5.20300   4.37100   44.95500  1.000 34.11725  ? 250 ARG B N     1 
ATOM   5416 C  CA    . ARG B 1 250 ? 3.93400   5.07400   45.10600  1.000 28.86399  ? 250 ARG B CA    1 
ATOM   5417 C  C     . ARG B 1 250 ? 3.51400   5.73600   43.80000  1.000 32.05648  ? 250 ARG B C     1 
ATOM   5418 O  O     . ARG B 1 250 ? 2.36200   5.61700   43.36700  1.000 31.08267  ? 250 ARG B O     1 
ATOM   5419 C  CB    . ARG B 1 250 ? 4.05600   6.12000   46.21700  1.000 29.28246  ? 250 ARG B CB    1 
ATOM   5420 C  CG    . ARG B 1 250 ? 4.34600   5.53300   47.59900  1.000 24.06868  ? 250 ARG B CG    1 
ATOM   5421 C  CD    . ARG B 1 250 ? 3.98100   6.50500   48.70600  1.000 22.78168  ? 250 ARG B CD    1 
ATOM   5422 N  NE    . ARG B 1 250 ? 4.59900   7.82600   48.55200  1.000 26.21630  ? 250 ARG B NE    1 
ATOM   5423 C  CZ    . ARG B 1 250 ? 5.85100   8.12600   48.89000  1.000 26.02154  ? 250 ARG B CZ    1 
ATOM   5424 N  NH1   . ARG B 1 250 ? 6.64900   7.19800   49.40400  1.000 28.79029  ? 250 ARG B NH1   1 
ATOM   5425 N  NH2   . ARG B 1 250 ? 6.30400   9.36200   48.72400  1.000 26.84269  ? 250 ARG B NH2   1 
ATOM   5426 N  N     . ASN B 1 251 ? 4.43900   6.44100   43.15300  1.000 33.44612  ? 251 ASN B N     1 
ATOM   5427 C  CA    . ASN B 1 251 ? 4.06700   7.18000   41.95400  1.000 36.32278  ? 251 ASN B CA    1 
ATOM   5428 C  C     . ASN B 1 251 ? 3.83700   6.25800   40.76700  1.000 40.78121  ? 251 ASN B C     1 
ATOM   5429 O  O     . ASN B 1 251 ? 3.03400   6.58300   39.88500  1.000 40.61276  ? 251 ASN B O     1 
ATOM   5430 C  CB    . ASN B 1 251 ? 5.12200   8.23800   41.64800  1.000 36.94917  ? 251 ASN B CB    1 
ATOM   5431 C  CG    . ASN B 1 251 ? 4.90800   9.49500   42.45900  1.000 38.81781  ? 251 ASN B CG    1 
ATOM   5432 O  OD1   . ASN B 1 251 ? 3.83600   10.09600  42.40900  1.000 40.37063  ? 251 ASN B OD1   1 
ATOM   5433 N  ND2   . ASN B 1 251 ? 5.90700   9.87600   43.24400  1.000 48.20315  ? 251 ASN B ND2   1 
ATOM   5434 N  N     . ASP B 1 252 ? 4.51300   5.10800   40.72500  1.000 40.78647  ? 252 ASP B N     1 
ATOM   5435 C  CA    . ASP B 1 252 ? 4.16400   4.09500   39.73400  1.000 46.58980  ? 252 ASP B CA    1 
ATOM   5436 C  C     . ASP B 1 252 ? 2.70000   3.69400   39.86900  1.000 45.81865  ? 252 ASP B C     1 
ATOM   5437 O  O     . ASP B 1 252 ? 1.96900   3.61000   38.87500  1.000 42.06031  ? 252 ASP B O     1 
ATOM   5438 C  CB    . ASP B 1 252 ? 5.07600   2.87300   39.87900  1.000 46.60559  ? 252 ASP B CB    1 
ATOM   5439 C  CG    . ASP B 1 252 ? 6.40400   3.03600   39.15100  1.000 49.37960  ? 252 ASP B CG    1 
ATOM   5440 O  OD1   . ASP B 1 252 ? 6.61100   4.08300   38.50000  1.000 57.09632  ? 252 ASP B OD1   1 
ATOM   5441 O  OD2   . ASP B 1 252 ? 7.24200   2.10900   39.22800  1.000 71.05589  ? 252 ASP B OD2   1 
ATOM   5442 N  N     . ARG B 1 253 ? 2.24700   3.47300   41.10700  1.000 39.00731  ? 253 ARG B N     1 
ATOM   5443 C  CA    . ARG B 1 253 ? 0.86300   3.07800   41.34200  1.000 40.96281  ? 253 ARG B CA    1 
ATOM   5444 C  C     . ARG B 1 253 ? -0.09800  4.22500   41.03100  1.000 36.19908  ? 253 ARG B C     1 
ATOM   5445 O  O     . ARG B 1 253 ? -1.12700  4.01700   40.37600  1.000 35.62006  ? 253 ARG B O     1 
ATOM   5446 C  CB    . ARG B 1 253 ? 0.72100   2.58300   42.78800  1.000 42.26823  ? 253 ARG B CB    1 
ATOM   5447 C  CG    . ARG B 1 253 ? -0.62800  2.00200   43.19200  1.000 53.11163  ? 253 ARG B CG    1 
ATOM   5448 C  CD    . ARG B 1 253 ? -0.43500  1.09500   44.41500  1.000 73.82727  ? 253 ARG B CD    1 
ATOM   5449 N  NE    . ARG B 1 253 ? -1.58700  1.06600   45.31700  1.000 91.65573  ? 253 ARG B NE    1 
ATOM   5450 C  CZ    . ARG B 1 253 ? -1.53700  0.63700   46.57900  1.000 67.74760  ? 253 ARG B CZ    1 
ATOM   5451 N  NH1   . ARG B 1 253 ? -0.39600  0.20000   47.09400  1.000 50.25076  ? 253 ARG B NH1   1 
ATOM   5452 N  NH2   . ARG B 1 253 ? -2.62900  0.64500   47.33200  1.000 45.07646  ? 253 ARG B NH2   1 
ATOM   5453 N  N     . LEU B 1 254 ? 0.22700   5.44500   41.47700  1.000 33.75931  ? 254 LEU B N     1 
ATOM   5454 C  CA    . LEU B 1 254 ? -0.64100  6.59300   41.21700  1.000 33.79089  ? 254 LEU B CA    1 
ATOM   5455 C  C     . LEU B 1 254 ? -0.74800  6.88200   39.72100  1.000 39.50210  ? 254 LEU B C     1 
ATOM   5456 O  O     . LEU B 1 254 ? -1.83900  7.16600   39.21000  1.000 44.02107  ? 254 LEU B O     1 
ATOM   5457 C  CB    . LEU B 1 254 ? -0.12400  7.82600   41.96000  1.000 32.10385  ? 254 LEU B CB    1 
ATOM   5458 C  CG    . LEU B 1 254 ? -0.15100  7.80900   43.49600  1.000 30.00886  ? 254 LEU B CG    1 
ATOM   5459 C  CD1   . LEU B 1 254 ? 0.54300   9.04200   44.04800  1.000 34.04619  ? 254 LEU B CD1   1 
ATOM   5460 C  CD2   . LEU B 1 254 ? -1.57200  7.72300   44.03500  1.000 31.73802  ? 254 LEU B CD2   1 
ATOM   5461 N  N     . ARG B 1 255 ? 0.37900   6.82400   39.00700  1.000 33.84616  ? 255 ARG B N     1 
ATOM   5462 C  CA    . ARG B 1 255 ? 0.37300   7.03400   37.56100  1.000 40.74173  ? 255 ARG B CA    1 
ATOM   5463 C  C     . ARG B 1 255 ? -0.48300  5.98800   36.85500  1.000 40.11534  ? 255 ARG B C     1 
ATOM   5464 O  O     . ARG B 1 255 ? -1.30300  6.31700   35.99000  1.000 45.52125  ? 255 ARG B O     1 
ATOM   5465 C  CB    . ARG B 1 255 ? 1.80300   6.98000   37.03400  1.000 54.79341  ? 255 ARG B CB    1 
ATOM   5466 C  CG    . ARG B 1 255 ? 2.61100   8.23900   37.26400  1.000 75.65644  ? 255 ARG B CG    1 
ATOM   5467 C  CD    . ARG B 1 255 ? 4.02300   8.03800   36.75000  1.000 99.99883  ? 255 ARG B CD    1 
ATOM   5468 N  NE    . ARG B 1 255 ? 4.98100   8.95700   37.35900  1.000 106.47329 ? 255 ARG B NE    1 
ATOM   5469 C  CZ    . ARG B 1 255 ? 6.25300   8.65100   37.59900  1.000 85.71554  ? 255 ARG B CZ    1 
ATOM   5470 N  NH1   . ARG B 1 255 ? 6.71400   7.44600   37.29000  1.000 84.79438  ? 255 ARG B NH1   1 
ATOM   5471 N  NH2   . ARG B 1 255 ? 7.06100   9.54300   38.15500  1.000 77.10925  ? 255 ARG B NH2   1 
ATOM   5472 N  N     . ASP B 1 256 ? -0.29300  4.71400   37.21200  1.000 48.75848  ? 256 ASP B N     1 
ATOM   5473 C  CA    . ASP B 1 256 ? -0.97800  3.61900   36.52900  1.000 49.04799  ? 256 ASP B CA    1 
ATOM   5474 C  C     . ASP B 1 256 ? -2.48600  3.65000   36.76500  1.000 44.63956  ? 256 ASP B C     1 
ATOM   5475 O  O     . ASP B 1 256 ? -3.26700  3.38800   35.84200  1.000 45.99499  ? 256 ASP B O     1 
ATOM   5476 C  CB    . ASP B 1 256 ? -0.39300  2.28300   36.98500  1.000 55.76458  ? 256 ASP B CB    1 
ATOM   5477 C  CG    . ASP B 1 256 ? -0.86500  1.11700   36.13700  1.000 80.79653  ? 256 ASP B CG    1 
ATOM   5478 O  OD1   . ASP B 1 256 ? -0.77600  1.21000   34.89400  1.000 105.86796 ? 256 ASP B OD1   1 
ATOM   5479 O  OD2   . ASP B 1 256 ? -1.32300  0.10500   36.71300  1.000 97.51432  ? 256 ASP B OD2   1 
ATOM   5480 N  N     . SER B 1 257 ? -2.91400  3.93600   37.99600  1.000 41.56551  ? 257 SER B N     1 
ATOM   5481 C  CA    . SER B 1 257 ? -4.31900  3.84100   38.38000  1.000 42.64459  ? 257 SER B CA    1 
ATOM   5482 C  C     . SER B 1 257 ? -5.07400  5.16200   38.30300  1.000 42.18137  ? 257 SER B C     1 
ATOM   5483 O  O     . SER B 1 257 ? -6.27600  5.15700   38.01800  1.000 49.48488  ? 257 SER B O     1 
ATOM   5484 C  CB    . SER B 1 257 ? -4.43900  3.28000   39.80300  1.000 43.05779  ? 257 SER B CB    1 
ATOM   5485 O  OG    . SER B 1 257 ? -3.92200  1.96100   39.87500  1.000 48.00312  ? 257 SER B OG    1 
ATOM   5486 N  N     . TYR B 1 258 ? -4.41600  6.29000   38.57700  1.000 40.70751  ? 258 TYR B N     1 
ATOM   5487 C  CA    . TYR B 1 258 ? -5.09000  7.57900   38.65500  1.000 43.96317  ? 258 TYR B CA    1 
ATOM   5488 C  C     . TYR B 1 258 ? -4.49800  8.62300   37.71900  1.000 45.13173  ? 258 TYR B C     1 
ATOM   5489 O  O     . TYR B 1 258 ? -4.98000  9.76300   37.70700  1.000 44.03423  ? 258 TYR B O     1 
ATOM   5490 C  CB    . TYR B 1 258 ? -5.06600  8.09200   40.10100  1.000 38.31512  ? 258 TYR B CB    1 
ATOM   5491 C  CG    . TYR B 1 258 ? -5.60700  7.06700   41.06900  1.000 40.31010  ? 258 TYR B CG    1 
ATOM   5492 C  CD1   . TYR B 1 258 ? -6.96900  6.79400   41.13300  1.000 46.22923  ? 258 TYR B CD1   1 
ATOM   5493 C  CD2   . TYR B 1 258 ? -4.75300  6.34100   41.88900  1.000 39.09679  ? 258 TYR B CD2   1 
ATOM   5494 C  CE1   . TYR B 1 258 ? -7.46600  5.84400   42.00500  1.000 48.88218  ? 258 TYR B CE1   1 
ATOM   5495 C  CE2   . TYR B 1 258 ? -5.24100  5.38800   42.76300  1.000 40.61540  ? 258 TYR B CE2   1 
ATOM   5496 C  CZ    . TYR B 1 258 ? -6.59600  5.14400   42.81500  1.000 53.76960  ? 258 TYR B CZ    1 
ATOM   5497 O  OH    . TYR B 1 258 ? -7.08000  4.19600   43.68400  1.000 46.95826  ? 258 TYR B OH    1 
ATOM   5498 N  N     . PHE B 1 259 ? -3.45100  8.27100   36.96100  1.000 42.19980  ? 259 PHE B N     1 
ATOM   5499 C  CA    . PHE B 1 259 ? -2.91600  9.09100   35.86800  1.000 46.35819  ? 259 PHE B CA    1 
ATOM   5500 C  C     . PHE B 1 259 ? -2.41900  10.45600  36.34500  1.000 42.96041  ? 259 PHE B C     1 
ATOM   5501 O  O     . PHE B 1 259 ? -2.69900  11.49000  35.73500  1.000 46.10553  ? 259 PHE B O     1 
ATOM   5502 C  CB    . PHE B 1 259 ? -3.95100  9.25100   34.75400  1.000 51.69304  ? 259 PHE B CB    1 
ATOM   5503 C  CG    . PHE B 1 259 ? -4.43000  7.95000   34.19700  1.000 58.43332  ? 259 PHE B CG    1 
ATOM   5504 C  CD1   . PHE B 1 259 ? -3.68900  7.28500   33.23600  1.000 60.49410  ? 259 PHE B CD1   1 
ATOM   5505 C  CD2   . PHE B 1 259 ? -5.61200  7.38600   34.63900  1.000 60.58884  ? 259 PHE B CD2   1 
ATOM   5506 C  CE1   . PHE B 1 259 ? -4.11700  6.08200   32.72900  1.000 68.67139  ? 259 PHE B CE1   1 
ATOM   5507 C  CE2   . PHE B 1 259 ? -6.04700  6.18400   34.13300  1.000 63.93925  ? 259 PHE B CE2   1 
ATOM   5508 C  CZ    . PHE B 1 259 ? -5.29900  5.53000   33.17600  1.000 66.56851  ? 259 PHE B CZ    1 
ATOM   5509 N  N     . PHE B 1 260 ? -1.64900  10.45300  37.43200  1.000 45.21858  ? 260 PHE B N     1 
ATOM   5510 C  CA    . PHE B 1 260 ? -0.99100  11.67000  37.88200  1.000 44.83695  ? 260 PHE B CA    1 
ATOM   5511 C  C     . PHE B 1 260 ? 0.26700   11.30100  38.65600  1.000 45.03172  ? 260 PHE B C     1 
ATOM   5512 O  O     . PHE B 1 260 ? 0.44000   10.15900  39.09100  1.000 46.31608  ? 260 PHE B O     1 
ATOM   5513 C  CB    . PHE B 1 260 ? -1.93100  12.54100  38.73300  1.000 44.70273  ? 260 PHE B CB    1 
ATOM   5514 C  CG    . PHE B 1 260 ? -2.14400  12.03200  40.13600  1.000 40.18377  ? 260 PHE B CG    1 
ATOM   5515 C  CD1   . PHE B 1 260 ? -3.13800  11.10800  40.41400  1.000 42.70249  ? 260 PHE B CD1   1 
ATOM   5516 C  CD2   . PHE B 1 260 ? -1.36100  12.49700  41.17900  1.000 37.97561  ? 260 PHE B CD2   1 
ATOM   5517 C  CE1   . PHE B 1 260 ? -3.33400  10.64900  41.70700  1.000 38.80992  ? 260 PHE B CE1   1 
ATOM   5518 C  CE2   . PHE B 1 260 ? -1.55200  12.03600  42.46600  1.000 38.59410  ? 260 PHE B CE2   1 
ATOM   5519 C  CZ    . PHE B 1 260 ? -2.54000  11.11200  42.72900  1.000 33.71194  ? 260 PHE B CZ    1 
ATOM   5520 N  N     . THR B 1 261 ? 1.16700   12.27500  38.77800  1.000 56.46730  ? 261 THR B N     1 
ATOM   5521 C  CA    . THR B 1 261 ? 2.37500   12.17000  39.59300  1.000 45.32386  ? 261 THR B CA    1 
ATOM   5522 C  C     . THR B 1 261 ? 2.25900   13.10500  40.79300  1.000 39.30998  ? 261 THR B C     1 
ATOM   5523 O  O     . THR B 1 261 ? 2.04600   14.31000  40.62100  1.000 41.72869  ? 261 THR B O     1 
ATOM   5524 C  CB    . THR B 1 261 ? 3.63000   12.51200  38.78700  1.000 48.99535  ? 261 THR B CB    1 
ATOM   5525 O  OG1   . THR B 1 261 ? 3.75200   11.62000  37.67400  1.000 59.37817  ? 261 THR B OG1   1 
ATOM   5526 C  CG2   . THR B 1 261 ? 4.87800   12.41100  39.66300  1.000 54.83026  ? 261 THR B CG2   1 
ATOM   5527 N  N     . CYS B 1 262 ? 2.40300   12.55500  41.99700  1.000 40.09954  ? 262 CYS B N     1 
ATOM   5528 C  CA    . CYS B 1 262 ? 2.27500   13.34600  43.21600  1.000 36.56754  ? 262 CYS B CA    1 
ATOM   5529 C  C     . CYS B 1 262 ? 3.47600   14.26900  43.42200  1.000 36.20960  ? 262 CYS B C     1 
ATOM   5530 O  O     . CYS B 1 262 ? 4.62000   13.92700  43.10700  1.000 38.66253  ? 262 CYS B O     1 
ATOM   5531 C  CB    . CYS B 1 262 ? 2.12500   12.43300  44.43500  1.000 39.20207  ? 262 CYS B CB    1 
ATOM   5532 S  SG    . CYS B 1 262 ? 1.79200   13.32600  45.96000  1.000 36.38068  ? 262 CYS B SG    1 
ATOM   5533 N  N     . GLU B 1 263 ? 3.20300   15.45400  43.98100  1.000 30.45365  ? 263 GLU B N     1 
ATOM   5534 C  CA    . GLU B 1 263 ? 4.23300   16.44900  44.26100  1.000 31.95909  ? 263 GLU B CA    1 
ATOM   5535 C  C     . GLU B 1 263 ? 4.18400   16.91600  45.71800  1.000 29.39826  ? 263 GLU B C     1 
ATOM   5536 O  O     . GLU B 1 263 ? 4.61000   18.02900  46.03200  1.000 29.11928  ? 263 GLU B O     1 
ATOM   5537 C  CB    . GLU B 1 263 ? 4.10200   17.63700  43.30800  1.000 35.55426  ? 263 GLU B CB    1 
ATOM   5538 C  CG    . GLU B 1 263 ? 4.28900   17.25700  41.83500  1.000 45.61863  ? 263 GLU B CG    1 
ATOM   5539 C  CD    . GLU B 1 263 ? 4.05400   18.42000  40.88300  1.000 57.63323  ? 263 GLU B CD    1 
ATOM   5540 O  OE1   . GLU B 1 263 ? 3.85400   19.55600  41.36900  1.000 69.14513  ? 263 GLU B OE1   1 
ATOM   5541 O  OE2   . GLU B 1 263 ? 4.07000   18.19800  39.64900  1.000 58.94654  ? 263 GLU B OE2   1 
ATOM   5542 N  N     . CYS B 1 264 ? 3.66700   16.08200  46.61800  1.000 32.63549  ? 264 CYS B N     1 
ATOM   5543 C  CA    . CYS B 1 264 ? 3.64600   16.41000  48.04000  1.000 33.28294  ? 264 CYS B CA    1 
ATOM   5544 C  C     . CYS B 1 264 ? 5.06600   16.44000  48.61700  1.000 33.67509  ? 264 CYS B C     1 
ATOM   5545 O  O     . CYS B 1 264 ? 6.05100   16.10800  47.95100  1.000 33.76721  ? 264 CYS B O     1 
ATOM   5546 C  CB    . CYS B 1 264 ? 2.77100   15.42200  48.80900  1.000 31.78539  ? 264 CYS B CB    1 
ATOM   5547 S  SG    . CYS B 1 264 ? 3.54900   13.82800  49.15600  1.000 33.74089  ? 264 CYS B SG    1 
ATOM   5548 N  N     . GLN B 1 265 ? 5.16200   16.86700  49.87900  1.000 35.23580  ? 265 GLN B N     1 
ATOM   5549 C  CA    . GLN B 1 265 ? 6.46500   17.01300  50.52400  1.000 44.96592  ? 265 GLN B CA    1 
ATOM   5550 C  C     . GLN B 1 265 ? 7.22800   15.69300  50.57400  1.000 33.55139  ? 265 GLN B C     1 
ATOM   5551 O  O     . GLN B 1 265 ? 8.44600   15.66700  50.35800  1.000 39.77845  ? 265 GLN B O     1 
ATOM   5552 C  CB    . GLN B 1 265 ? 6.29800   17.58000  51.93300  1.000 42.99989  ? 265 GLN B CB    1 
ATOM   5553 C  CG    . GLN B 1 265 ? 7.61000   18.02000  52.56100  1.000 61.98901  ? 265 GLN B CG    1 
ATOM   5554 C  CD    . GLN B 1 265 ? 7.42000   18.70700  53.89700  1.000 74.85898  ? 265 GLN B CD    1 
ATOM   5555 O  OE1   . GLN B 1 265 ? 6.58700   18.29600  54.70600  1.000 79.32267  ? 265 GLN B OE1   1 
ATOM   5556 N  NE2   . GLN B 1 265 ? 8.19100   19.76400  54.13400  1.000 90.83458  ? 265 GLN B NE2   1 
ATOM   5557 N  N     . GLU B 1 266 ? 6.53600   14.59000  50.88000  1.000 28.61396  ? 266 GLU B N     1 
ATOM   5558 C  CA    . GLU B 1 266 ? 7.20700   13.29400  50.95000  1.000 30.19836  ? 266 GLU B CA    1 
ATOM   5559 C  C     . GLU B 1 266 ? 7.78500   12.89400  49.59600  1.000 31.74591  ? 266 GLU B C     1 
ATOM   5560 O  O     . GLU B 1 266 ? 8.91700   12.40200  49.51700  1.000 33.06186  ? 266 GLU B O     1 
ATOM   5561 C  CB    . GLU B 1 266 ? 6.24200   12.22100  51.45600  1.000 30.90634  ? 266 GLU B CB    1 
ATOM   5562 C  CG    . GLU B 1 266 ? 5.87100   12.33500  52.93200  1.000 51.18245  ? 266 GLU B CG    1 
ATOM   5563 C  CD    . GLU B 1 266 ? 7.04700   12.11000  53.87600  1.000 58.87811  ? 266 GLU B CD    1 
ATOM   5564 O  OE1   . GLU B 1 266 ? 8.05700   11.49100  53.46500  1.000 60.90467  ? 266 GLU B OE1   1 
ATOM   5565 O  OE2   . GLU B 1 266 ? 6.94900   12.54600  55.04100  1.000 73.39827  ? 266 GLU B OE2   1 
ATOM   5566 N  N     . CYS B 1 267 ? 7.02500   13.10300  48.51600  1.000 35.70428  ? 267 CYS B N     1 
ATOM   5567 C  CA    . CYS B 1 267 ? 7.52000   12.74900  47.18600  1.000 38.63095  ? 267 CYS B CA    1 
ATOM   5568 C  C     . CYS B 1 267 ? 8.63400   13.68400  46.73200  1.000 41.46023  ? 267 CYS B C     1 
ATOM   5569 O  O     . CYS B 1 267 ? 9.59000   13.24800  46.07800  1.000 40.83121  ? 267 CYS B O     1 
ATOM   5570 C  CB    . CYS B 1 267 ? 6.36800   12.75500  46.18100  1.000 40.16271  ? 267 CYS B CB    1 
ATOM   5571 S  SG    . CYS B 1 267 ? 5.20100   11.40600  46.42800  1.000 38.37565  ? 267 CYS B SG    1 
ATOM   5572 N  N     . THR B 1 268 ? 8.52200   14.97300  47.06200  1.000 38.31512  ? 268 THR B N     1 
ATOM   5573 C  CA    . THR B 1 268 ? 9.52300   15.94700  46.63900  1.000 41.52603  ? 268 THR B CA    1 
ATOM   5574 C  C     . THR B 1 268 ? 10.85800  15.71100  47.33800  1.000 40.18903  ? 268 THR B C     1 
ATOM   5575 O  O     . THR B 1 268 ? 11.91500  15.69900  46.69500  1.000 41.68131  ? 268 THR B O     1 
ATOM   5576 C  CB    . THR B 1 268 ? 9.01300   17.36200  46.91500  1.000 46.01604  ? 268 THR B CB    1 
ATOM   5577 O  OG1   . THR B 1 268 ? 7.79200   17.58100  46.19700  1.000 47.43990  ? 268 THR B OG1   1 
ATOM   5578 C  CG2   . THR B 1 268 ? 10.03900  18.39100  46.49100  1.000 44.05002  ? 268 THR B CG2   1 
ATOM   5579 N  N     . THR B 1 269 ? 10.82900  15.53200  48.66300  1.000 34.79628  ? 269 THR B N     1 
ATOM   5580 C  CA    . THR B 1 269 ? 12.06000  15.36800  49.42900  1.000 37.95981  ? 269 THR B CA    1 
ATOM   5581 C  C     . THR B 1 269 ? 12.56400  13.92900  49.43000  1.000 37.75189  ? 269 THR B C     1 
ATOM   5582 O  O     . THR B 1 269 ? 13.77500  13.70800  49.55200  1.000 38.19932  ? 269 THR B O     1 
ATOM   5583 C  CB    . THR B 1 269 ? 11.85900  15.83000  50.87500  1.000 34.84102  ? 269 THR B CB    1 
ATOM   5584 O  OG1   . THR B 1 269 ? 10.96100  14.93500  51.53900  1.000 29.50354  ? 269 THR B OG1   1 
ATOM   5585 C  CG2   . THR B 1 269 ? 11.28500  17.24200  50.91300  1.000 37.61240  ? 269 THR B CG2   1 
ATOM   5586 N  N     . LYS B 1 270 ? 11.66000  12.94700  49.33600  1.000 34.04619  ? 270 LYS B N     1 
ATOM   5587 C  CA    . LYS B 1 270 ? 12.00700  11.52900  49.47800  1.000 35.53847  ? 270 LYS B CA    1 
ATOM   5588 C  C     . LYS B 1 270 ? 12.66400  11.24300  50.83000  1.000 36.50438  ? 270 LYS B C     1 
ATOM   5589 O  O     . LYS B 1 270 ? 13.49400  10.34000  50.94700  1.000 33.36716  ? 270 LYS B O     1 
ATOM   5590 C  CB    . LYS B 1 270 ? 12.91600  11.04700  48.33600  1.000 39.56790  ? 270 LYS B CB    1 
ATOM   5591 C  CG    . LYS B 1 270 ? 12.36700  11.25800  46.92400  1.000 48.36369  ? 270 LYS B CG    1 
ATOM   5592 C  CD    . LYS B 1 270 ? 13.33400  10.70500  45.87900  1.000 52.67737  ? 270 LYS B CD    1 
ATOM   5593 C  CE    . LYS B 1 270 ? 12.77800  10.80800  44.46600  1.000 67.51862  ? 270 LYS B CE    1 
ATOM   5594 N  NZ    . LYS B 1 270 ? 12.87100  12.19300  43.91900  1.000 88.17373  ? 270 LYS B NZ    1 
ATOM   5595 N  N     . ASP B 1 271 ? 12.28700  12.00400  51.86500  1.000 35.38319  ? 271 ASP B N     1 
ATOM   5596 C  CA    . ASP B 1 271 ? 12.99300  11.93700  53.14300  1.000 34.88576  ? 271 ASP B CA    1 
ATOM   5597 C  C     . ASP B 1 271 ? 12.90600  10.55500  53.78900  1.000 38.58884  ? 271 ASP B C     1 
ATOM   5598 O  O     . ASP B 1 271 ? 13.81600  10.17000  54.53300  1.000 46.12132  ? 271 ASP B O     1 
ATOM   5599 C  CB    . ASP B 1 271 ? 12.45400  13.00900  54.09900  1.000 37.93086  ? 271 ASP B CB    1 
ATOM   5600 C  CG    . ASP B 1 271 ? 13.27400  14.30000  54.06400  1.000 35.44372  ? 271 ASP B CG    1 
ATOM   5601 O  OD1   . ASP B 1 271 ? 14.27500  14.37000  53.31300  1.000 41.52866  ? 271 ASP B OD1   1 
ATOM   5602 O  OD2   . ASP B 1 271 ? 12.91600  15.25300  54.79000  1.000 40.62592  ? 271 ASP B OD2   1 
ATOM   5603 N  N     . LYS B 1 272 ? 11.83800  9.79800   53.53100  1.000 30.00623  ? 272 LYS B N     1 
ATOM   5604 C  CA    . LYS B 1 272 ? 11.67900  8.47300   54.12200  1.000 28.29550  ? 272 LYS B CA    1 
ATOM   5605 C  C     . LYS B 1 272 ? 12.16900  7.32900   53.23600  1.000 32.18807  ? 272 LYS B C     1 
ATOM   5606 O  O     . LYS B 1 272 ? 12.12800  6.17600   53.67500  1.000 36.14907  ? 272 LYS B O     1 
ATOM   5607 C  CB    . LYS B 1 272 ? 10.21700  8.22500   54.48600  1.000 27.80597  ? 272 LYS B CB    1 
ATOM   5608 C  CG    . LYS B 1 272 ? 9.73500   9.00700   55.70000  1.000 28.67449  ? 272 LYS B CG    1 
ATOM   5609 C  CD    . LYS B 1 272 ? 8.40800   8.47000   56.19600  1.000 29.85358  ? 272 LYS B CD    1 
ATOM   5610 C  CE    . LYS B 1 272 ? 8.02500   9.09300   57.52200  1.000 38.59147  ? 272 LYS B CE    1 
ATOM   5611 N  NZ    . LYS B 1 272 ? 6.90100   8.37400   58.16100  1.000 44.06844  ? 272 LYS B NZ    1 
ATOM   5612 N  N     . ASP B 1 273 ? 12.61300  7.60300   52.00600  1.000 37.12287  ? 273 ASP B N     1 
ATOM   5613 C  CA    . ASP B 1 273 ? 12.98000  6.52800   51.08000  1.000 35.93589  ? 273 ASP B CA    1 
ATOM   5614 C  C     . ASP B 1 273 ? 14.10800  5.65300   51.62600  1.000 37.44133  ? 273 ASP B C     1 
ATOM   5615 O  O     . ASP B 1 273 ? 14.04800  4.42100   51.54100  1.000 38.09930  ? 273 ASP B O     1 
ATOM   5616 C  CB    . ASP B 1 273 ? 13.36900  7.11000   49.72100  1.000 43.13412  ? 273 ASP B CB    1 
ATOM   5617 C  CG    . ASP B 1 273 ? 12.16700  7.38100   48.83600  1.000 42.07083  ? 273 ASP B CG    1 
ATOM   5618 O  OD1   . ASP B 1 273 ? 11.02800  7.38800   49.35600  1.000 35.48320  ? 273 ASP B OD1   1 
ATOM   5619 O  OD2   . ASP B 1 273 ? 12.36200  7.57700   47.61800  1.000 51.07718  ? 273 ASP B OD2   1 
ATOM   5620 N  N     . LYS B 1 274 ? 15.16400  6.27100   52.16100  1.000 36.59386  ? 274 LYS B N     1 
ATOM   5621 C  CA    . LYS B 1 274 ? 16.33400  5.49800   52.57500  1.000 36.92022  ? 274 LYS B CA    1 
ATOM   5622 C  C     . LYS B 1 274 ? 16.03100  4.60400   53.77500  1.000 38.56252  ? 274 LYS B C     1 
ATOM   5623 O  O     . LYS B 1 274 ? 16.52100  3.46900   53.84900  1.000 35.11210  ? 274 LYS B O     1 
ATOM   5624 C  CB    . LYS B 1 274 ? 17.50500  6.43300   52.84700  1.000 45.77917  ? 274 LYS B CB    1 
ATOM   5625 C  CG    . LYS B 1 274 ? 18.01200  7.07400   51.56400  1.000 49.76649  ? 274 LYS B CG    1 
ATOM   5626 C  CD    . LYS B 1 274 ? 19.21600  7.95900   51.78400  1.000 61.82320  ? 274 LYS B CD    1 
ATOM   5627 C  CE    . LYS B 1 274 ? 19.71200  8.51400   50.45900  1.000 73.96676  ? 274 LYS B CE    1 
ATOM   5628 N  NZ    . LYS B 1 274 ? 20.80700  9.50000   50.64300  1.000 72.01653  ? 274 LYS B NZ    1 
ATOM   5629 N  N     . ALA B 1 275 ? 15.24200  5.09200   54.73100  1.000 34.69890  ? 275 ALA B N     1 
ATOM   5630 C  CA    . ALA B 1 275 ? 14.85400  4.23400   55.84500  1.000 35.17790  ? 275 ALA B CA    1 
ATOM   5631 C  C     . ALA B 1 275 ? 13.95900  3.08500   55.38500  1.000 34.83576  ? 275 ALA B C     1 
ATOM   5632 O  O     . ALA B 1 275 ? 14.00400  1.99500   55.96700  1.000 42.93936  ? 275 ALA B O     1 
ATOM   5633 C  CB    . ALA B 1 275 ? 14.16800  5.06100   56.93200  1.000 33.04607  ? 275 ALA B CB    1 
ATOM   5634 N  N     . LYS B 1 276 ? 13.13000  3.30700   54.36000  1.000 33.40401  ? 276 LYS B N     1 
ATOM   5635 C  CA    . LYS B 1 276 ? 12.24100  2.25000   53.88800  1.000 30.17730  ? 276 LYS B CA    1 
ATOM   5636 C  C     . LYS B 1 276 ? 13.00400  1.12500   53.19400  1.000 31.33534  ? 276 LYS B C     1 
ATOM   5637 O  O     . LYS B 1 276 ? 12.58100  -0.03400  53.26000  1.000 35.55689  ? 276 LYS B O     1 
ATOM   5638 C  CB    . LYS B 1 276 ? 11.17500  2.83500   52.95900  1.000 32.78551  ? 276 LYS B CB    1 
ATOM   5639 C  CG    . LYS B 1 276 ? 10.11100  3.65600   53.69100  1.000 28.92189  ? 276 LYS B CG    1 
ATOM   5640 C  CD    . LYS B 1 276 ? 9.19500   4.38900   52.72000  1.000 34.47782  ? 276 LYS B CD    1 
ATOM   5641 C  CE    . LYS B 1 276 ? 8.09800   5.16000   53.45400  1.000 30.86423  ? 276 LYS B CE    1 
ATOM   5642 N  NZ    . LYS B 1 276 ? 7.17100   5.83500   52.49200  1.000 32.21965  ? 276 LYS B NZ    1 
ATOM   5643 N  N     . VAL B 1 277 ? 14.11400  1.43500   52.52100  1.000 31.63011  ? 277 VAL B N     1 
ATOM   5644 C  CA    . VAL B 1 277 ? 14.90300  0.42200   51.82300  1.000 34.89366  ? 277 VAL B CA    1 
ATOM   5645 C  C     . VAL B 1 277 ? 16.23900  0.24600   52.53900  1.000 38.41776  ? 277 VAL B C     1 
ATOM   5646 O  O     . VAL B 1 277 ? 17.31000  0.34500   51.93000  1.000 52.63263  ? 277 VAL B O     1 
ATOM   5647 C  CB    . VAL B 1 277 ? 15.09100  0.78900   50.33700  1.000 34.54098  ? 277 VAL B CB    1 
ATOM   5648 C  CG1   . VAL B 1 277 ? 15.62500  -0.39800  49.54800  1.000 34.01460  ? 277 VAL B CG1   1 
ATOM   5649 C  CG2   . VAL B 1 277 ? 13.76200  1.24100   49.74200  1.000 32.79341  ? 277 VAL B CG2   1 
ATOM   5650 N  N     . GLU B 1 278 ? 16.18100  -0.01600  53.84300  1.000 42.01293  ? 278 GLU B N     1 
ATOM   5651 C  CA    . GLU B 1 278 ? 17.39100  -0.07500  54.65100  1.000 44.49218  ? 278 GLU B CA    1 
ATOM   5652 C  C     . GLU B 1 278 ? 18.24900  -1.27300  54.27100  1.000 42.48667  ? 278 GLU B C     1 
ATOM   5653 O  O     . GLU B 1 278 ? 17.74700  -2.38400  54.07700  1.000 37.41238  ? 278 GLU B O     1 
ATOM   5654 C  CB    . GLU B 1 278 ? 17.04000  -0.14000  56.13400  1.000 53.94068  ? 278 GLU B CB    1 
ATOM   5655 C  CG    . GLU B 1 278 ? 18.24000  0.03700   57.04700  1.000 62.99703  ? 278 GLU B CG    1 
ATOM   5656 C  CD    . GLU B 1 278 ? 17.85200  0.09800   58.50800  1.000 76.15387  ? 278 GLU B CD    1 
ATOM   5657 O  OE1   . GLU B 1 278 ? 16.83800  -0.53200  58.87800  1.000 91.01881  ? 278 GLU B OE1   1 
ATOM   5658 O  OE2   . GLU B 1 278 ? 18.55600  0.77800   59.28400  1.000 98.35653  ? 278 GLU B OE2   1 
ATOM   5659 N  N     . ILE B 1 279 ? 19.55700  -1.04000  54.19100  1.000 44.66062  ? 279 ILE B N     1 
ATOM   5660 C  CA    . ILE B 1 279 ? 20.53700  -2.04400  53.79500  1.000 50.32972  ? 279 ILE B CA    1 
ATOM   5661 C  C     . ILE B 1 279 ? 21.31600  -2.47400  55.03000  1.000 56.17779  ? 279 ILE B C     1 
ATOM   5662 O  O     . ILE B 1 279 ? 21.57400  -1.66400  55.92800  1.000 56.50941  ? 279 ILE B O     1 
ATOM   5663 C  CB    . ILE B 1 279 ? 21.48300  -1.49700  52.70800  1.000 51.28773  ? 279 ILE B CB    1 
ATOM   5664 C  CG1   . ILE B 1 279 ? 20.67900  -0.91100  51.54900  1.000 56.75944  ? 279 ILE B CG1   1 
ATOM   5665 C  CG2   . ILE B 1 279 ? 22.40200  -2.58700  52.19200  1.000 60.53357  ? 279 ILE B CG2   1 
ATOM   5666 C  CD1   . ILE B 1 279 ? 19.66100  -1.87100  50.97200  1.000 55.85407  ? 279 ILE B CD1   1 
ATOM   5667 N  N     . ARG B 1 280 ? 21.65800  -3.75900  55.08900  1.000 62.90491  ? 280 ARG B N     1 
ATOM   5668 C  CA    . ARG B 1 280 ? 22.47200  -4.27000  56.18300  1.000 67.70812  ? 280 ARG B CA    1 
ATOM   5669 C  C     . ARG B 1 280 ? 23.87400  -3.67400  56.13100  1.000 67.57652  ? 280 ARG B C     1 
ATOM   5670 O  O     . ARG B 1 280 ? 24.44800  -3.48700  55.05400  1.000 63.46287  ? 280 ARG B O     1 
ATOM   5671 C  CB    . ARG B 1 280 ? 22.54700  -5.79500  56.11600  1.000 61.70740  ? 280 ARG B CB    1 
ATOM   5672 C  CG    . ARG B 1 280 ? 21.29400  -6.49200  56.60200  1.000 66.61588  ? 280 ARG B CG    1 
ATOM   5673 C  CD    . ARG B 1 280 ? 21.40300  -7.99400  56.44200  1.000 66.82380  ? 280 ARG B CD    1 
ATOM   5674 N  NE    . ARG B 1 280 ? 22.47600  -8.55800  57.25200  1.000 74.77212  ? 280 ARG B NE    1 
ATOM   5675 C  CZ    . ARG B 1 280 ? 22.87500  -9.82300  57.18400  1.000 90.71877  ? 280 ARG B CZ    1 
ATOM   5676 N  NH1   . ARG B 1 280 ? 22.28800  -10.66000 56.33900  1.000 102.00170 ? 280 ARG B NH1   1 
ATOM   5677 N  NH2   . ARG B 1 280 ? 23.86200  -10.25200 57.95800  1.000 87.61840  ? 280 ARG B NH2   1 
ATOM   5678 N  N     . LYS B 1 281 ? 24.42900  -3.37400  57.30700  1.000 66.87381  ? 281 LYS B N     1 
ATOM   5679 C  CA    . LYS B 1 281 ? 25.79800  -2.86700  57.41000  1.000 96.61948  ? 281 LYS B CA    1 
ATOM   5680 C  C     . LYS B 1 281 ? 26.74600  -4.05900  57.52600  1.000 93.03221  ? 281 LYS B C     1 
ATOM   5681 O  O     . LYS B 1 281 ? 27.17400  -4.45900  58.61100  1.000 86.68671  ? 281 LYS B O     1 
ATOM   5682 C  CB    . LYS B 1 281 ? 25.92900  -1.90700  58.58600  1.000 108.80778 ? 281 LYS B CB    1 
ATOM   5683 C  CG    . LYS B 1 281 ? 25.38500  -0.51600  58.29100  1.000 96.29049  ? 281 LYS B CG    1 
ATOM   5684 C  CD    . LYS B 1 281 ? 26.05200  0.55200   59.14100  1.000 112.80300 ? 281 LYS B CD    1 
ATOM   5685 C  CE    . LYS B 1 281 ? 27.45000  0.86800   58.63100  1.000 106.14957 ? 281 LYS B CE    1 
ATOM   5686 N  NZ    . LYS B 1 281 ? 28.07500  1.98700   59.38700  1.000 101.48848 ? 281 LYS B NZ    1 
ATOM   5687 N  N     . LEU B 1 282 ? 27.06800  -4.63700  56.37300  1.000 80.72020  ? 282 LEU B N     1 
ATOM   5688 C  CA    . LEU B 1 282 ? 27.95600  -5.78600  56.30400  1.000 88.35270  ? 282 LEU B CA    1 
ATOM   5689 C  C     . LEU B 1 282 ? 29.41800  -5.34800  56.29800  1.000 91.99261  ? 282 LEU B C     1 
ATOM   5690 O  O     . LEU B 1 282 ? 29.74100  -4.17300  56.09800  1.000 97.63539  ? 282 LEU B O     1 
ATOM   5691 C  CB    . LEU B 1 282 ? 27.66400  -6.62000  55.05700  1.000 90.13449  ? 282 LEU B CB    1 
ATOM   5692 C  CG    . LEU B 1 282 ? 26.25400  -7.18600  54.90500  1.000 85.02598  ? 282 LEU B CG    1 
ATOM   5693 C  CD1   . LEU B 1 282 ? 26.10200  -7.88900  53.56500  1.000 74.60631  ? 282 LEU B CD1   1 
ATOM   5694 C  CD2   . LEU B 1 282 ? 25.93300  -8.13400  56.05200  1.000 90.82405  ? 282 LEU B CD2   1 
ATOM   5695 N  N     . SER B 1 283 ? 30.30300  -6.31500  56.56700  1.000 101.92538 ? 283 SER B N     1 
ATOM   5696 C  CA    . SER B 1 283 ? 31.74000  -6.07100  56.47000  1.000 114.60585 ? 283 SER B CA    1 
ATOM   5697 C  C     . SER B 1 283 ? 32.09900  -5.48100  55.11400  1.000 117.62463 ? 283 SER B C     1 
ATOM   5698 O  O     . SER B 1 283 ? 32.77600  -4.45100  55.02600  1.000 106.13115 ? 283 SER B O     1 
ATOM   5699 C  CB    . SER B 1 283 ? 32.51100  -7.37000  56.71100  1.000 111.06858 ? 283 SER B CB    1 
ATOM   5700 O  OG    . SER B 1 283 ? 32.16700  -7.94900  57.95600  1.000 104.29408 ? 283 SER B OG    1 
ATOM   5701 N  N     . ASP B 1 284 ? 31.65100  -6.13000  54.04000  1.000 118.72476 ? 284 ASP B N     1 
ATOM   5702 C  CA    . ASP B 1 284 ? 31.77500  -5.58100  52.70100  1.000 119.75646 ? 284 ASP B CA    1 
ATOM   5703 C  C     . ASP B 1 284 ? 30.43900  -4.96800  52.31000  1.000 121.99357 ? 284 ASP B C     1 
ATOM   5704 O  O     . ASP B 1 284 ? 29.46800  -5.71200  52.10000  1.000 123.74905 ? 284 ASP B O     1 
ATOM   5705 C  CB    . ASP B 1 284 ? 32.18200  -6.66700  51.70700  1.000 118.36946 ? 284 ASP B CB    1 
ATOM   5706 C  CG    . ASP B 1 284 ? 32.60100  -6.10300  50.36400  1.000 123.74905 ? 284 ASP B CG    1 
ATOM   5707 O  OD1   . ASP B 1 284 ? 32.84700  -4.88200  50.28000  1.000 133.73446 ? 284 ASP B OD1   1 
ATOM   5708 O  OD2   . ASP B 1 284 ? 32.69100  -6.88400  49.39400  1.000 109.39206 ? 284 ASP B OD2   1 
ATOM   5709 N  N     . PRO B 1 285 ? 30.32800  -3.64400  52.22500  1.000 118.90636 ? 285 PRO B N     1 
ATOM   5710 C  CA    . PRO B 1 285 ? 29.03500  -3.01300  51.91600  1.000 105.25736 ? 285 PRO B CA    1 
ATOM   5711 C  C     . PRO B 1 285 ? 28.50100  -3.47300  50.57200  1.000 97.85647  ? 285 PRO B C     1 
ATOM   5712 O  O     . PRO B 1 285 ? 29.24300  -3.51200  49.57900  1.000 112.75826 ? 285 PRO B O     1 
ATOM   5713 C  CB    . PRO B 1 285 ? 29.36600  -1.51200  51.90300  1.000 106.11799 ? 285 PRO B CB    1 
ATOM   5714 C  CG    . PRO B 1 285 ? 30.61900  -1.38700  52.71200  1.000 110.69485 ? 285 PRO B CG    1 
ATOM   5715 C  CD    . PRO B 1 285 ? 31.38700  -2.65100  52.47300  1.000 110.76591 ? 285 PRO B CD    1 
ATOM   5716 N  N     . PRO B 1 286 ? 27.22300  -3.84600  50.50700  1.000 85.36813  ? 286 PRO B N     1 
ATOM   5717 C  CA    . PRO B 1 286 ? 26.61900  -4.22100  49.22000  1.000 83.77057  ? 286 PRO B CA    1 
ATOM   5718 C  C     . PRO B 1 286 ? 26.70800  -3.09000  48.20200  1.000 75.29850  ? 286 PRO B C     1 
ATOM   5719 O  O     . PRO B 1 286 ? 26.46100  -1.92400  48.51800  1.000 81.15184  ? 286 PRO B O     1 
ATOM   5720 C  CB    . PRO B 1 286 ? 25.16400  -4.53100  49.59100  1.000 81.03866  ? 286 PRO B CB    1 
ATOM   5721 C  CG    . PRO B 1 286 ? 25.20800  -4.86600  51.05400  1.000 73.05613  ? 286 PRO B CG    1 
ATOM   5722 C  CD    . PRO B 1 286 ? 26.28300  -4.00200  51.63100  1.000 70.17420  ? 286 PRO B CD    1 
ATOM   5723 N  N     . LYS B 1 287 ? 27.05000  -3.45000  46.96700  1.000 79.69640  ? 287 LYS B N     1 
ATOM   5724 C  CA    . LYS B 1 287 ? 27.20600  -2.46700  45.90600  1.000 94.72452  ? 287 LYS B CA    1 
ATOM   5725 C  C     . LYS B 1 287 ? 25.84400  -1.98900  45.40300  1.000 92.92430  ? 287 LYS B C     1 
ATOM   5726 O  O     . LYS B 1 287 ? 24.82800  -2.67800  45.52600  1.000 93.34277  ? 287 LYS B O     1 
ATOM   5727 C  CB    . LYS B 1 287 ? 28.02600  -3.05400  44.75400  1.000 102.59388 ? 287 LYS B CB    1 
ATOM   5728 C  CG    . LYS B 1 287 ? 28.81700  -2.02600  43.95200  1.000 112.84511 ? 287 LYS B CG    1 
ATOM   5729 C  CD    . LYS B 1 287 ? 28.05400  -1.55100  42.72500  1.000 111.95816 ? 287 LYS B CD    1 
ATOM   5730 C  CE    . LYS B 1 287 ? 28.51800  -0.17000  42.28800  1.000 123.78589 ? 287 LYS B CE    1 
ATOM   5731 N  NZ    . LYS B 1 287 ? 27.69900  0.36300   41.16300  1.000 123.20425 ? 287 LYS B NZ    1 
ATOM   5732 N  N     . ALA B 1 288 ? 25.84200  -0.77700  44.83500  1.000 89.40546  ? 288 ALA B N     1 
ATOM   5733 C  CA    . ALA B 1 288 ? 24.60900  -0.16000  44.35000  1.000 90.74246  ? 288 ALA B CA    1 
ATOM   5734 C  C     . ALA B 1 288 ? 23.87900  -1.04900  43.34900  1.000 87.78158  ? 288 ALA B C     1 
ATOM   5735 O  O     . ALA B 1 288 ? 22.65100  -1.18000  43.40900  1.000 94.21919  ? 288 ALA B O     1 
ATOM   5736 C  CB    . ALA B 1 288 ? 24.91600  1.20200   43.72900  1.000 84.32853  ? 288 ALA B CB    1 
ATOM   5737 N  N     . GLU B 1 289 ? 24.61300  -1.64900  42.40600  1.000 95.47724  ? 289 GLU B N     1 
ATOM   5738 C  CA    . GLU B 1 289 ? 23.98700  -2.54500  41.43600  1.000 99.51720  ? 289 GLU B CA    1 
ATOM   5739 C  C     . GLU B 1 289 ? 23.27700  -3.70600  42.12600  1.000 85.10231  ? 289 GLU B C     1 
ATOM   5740 O  O     . GLU B 1 289 ? 22.16000  -4.07300  41.74500  1.000 91.80311  ? 289 GLU B O     1 
ATOM   5741 C  CB    . GLU B 1 289 ? 25.02500  -3.06100  40.44000  1.000 94.42711  ? 289 GLU B CB    1 
ATOM   5742 C  CG    . GLU B 1 289 ? 24.41700  -3.79800  39.25600  1.000 102.77022 ? 289 GLU B CG    1 
ATOM   5743 C  CD    . GLU B 1 289 ? 25.46100  -4.45400  38.38100  1.000 119.42748 ? 289 GLU B CD    1 
ATOM   5744 O  OE1   . GLU B 1 289 ? 26.65200  -4.10700  38.51900  1.000 127.33369 ? 289 GLU B OE1   1 
ATOM   5745 O  OE2   . GLU B 1 289 ? 25.09400  -5.32000  37.55900  1.000 140.15101 ? 289 GLU B OE2   1 
ATOM   5746 N  N     . ALA B 1 290 ? 23.91900  -4.30700  43.13300  1.000 67.00277  ? 290 ALA B N     1 
ATOM   5747 C  CA    . ALA B 1 290 ? 23.29300  -5.41600  43.84700  1.000 65.26046  ? 290 ALA B CA    1 
ATOM   5748 C  C     . ALA B 1 290 ? 22.02700  -4.96400  44.56800  1.000 56.40150  ? 290 ALA B C     1 
ATOM   5749 O  O     . ALA B 1 290 ? 21.03700  -5.70300  44.61400  1.000 55.23294  ? 290 ALA B O     1 
ATOM   5750 C  CB    . ALA B 1 290 ? 24.28200  -6.04100  44.83000  1.000 62.94439  ? 290 ALA B CB    1 
ATOM   5751 N  N     . ILE B 1 291 ? 22.04100  -3.75300  45.13700  1.000 62.44170  ? 291 ILE B N     1 
ATOM   5752 C  CA    . ILE B 1 291 ? 20.85100  -3.21700  45.79500  1.000 59.88876  ? 291 ILE B CA    1 
ATOM   5753 C  C     . ILE B 1 291 ? 19.72300  -3.03300  44.78700  1.000 62.82595  ? 291 ILE B C     1 
ATOM   5754 O  O     . ILE B 1 291 ? 18.58500  -3.45600  45.02300  1.000 55.51981  ? 291 ILE B O     1 
ATOM   5755 C  CB    . ILE B 1 291 ? 21.17600  -1.90000  46.52000  1.000 66.75274  ? 291 ILE B CB    1 
ATOM   5756 C  CG1   . ILE B 1 291 ? 22.30400  -2.10400  47.53100  1.000 77.70142  ? 291 ILE B CG1   1 
ATOM   5757 C  CG2   . ILE B 1 291 ? 19.93600  -1.35000  47.20000  1.000 63.31022  ? 291 ILE B CG2   1 
ATOM   5758 C  CD1   . ILE B 1 291 ? 22.71100  -0.83700  48.24500  1.000 83.25209  ? 291 ILE B CD1   1 
ATOM   5759 N  N     . ARG B 1 292 ? 20.01600  -2.38300  43.65700  1.000 59.49134  ? 292 ARG B N     1 
ATOM   5760 C  CA    . ARG B 1 292 ? 18.99300  -2.20300  42.63000  1.000 65.67630  ? 292 ARG B CA    1 
ATOM   5761 C  C     . ARG B 1 292 ? 18.49900  -3.53800  42.09000  1.000 66.92118  ? 292 ARG B C     1 
ATOM   5762 O  O     . ARG B 1 292 ? 17.34000  -3.64400  41.67300  1.000 53.36166  ? 292 ARG B O     1 
ATOM   5763 C  CB    . ARG B 1 292 ? 19.51800  -1.33800  41.48200  1.000 67.55547  ? 292 ARG B CB    1 
ATOM   5764 C  CG    . ARG B 1 292 ? 19.93000  0.06500   41.87900  1.000 73.43249  ? 292 ARG B CG    1 
ATOM   5765 C  CD    . ARG B 1 292 ? 20.14000  0.92400   40.64400  1.000 87.45259  ? 292 ARG B CD    1 
ATOM   5766 N  NE    . ARG B 1 292 ? 21.14600  0.35000   39.75400  1.000 99.63563  ? 292 ARG B NE    1 
ATOM   5767 C  CZ    . ARG B 1 292 ? 22.42600  0.71300   39.74100  1.000 93.84283  ? 292 ARG B CZ    1 
ATOM   5768 N  NH1   . ARG B 1 292 ? 22.85900  1.65300   40.56900  1.000 90.95827  ? 292 ARG B NH1   1 
ATOM   5769 N  NH2   . ARG B 1 292 ? 23.27500  0.13700   38.90000  1.000 90.42400  ? 292 ARG B NH2   1 
ATOM   5770 N  N     . ASP B 1 293 ? 19.36500  -4.55500  42.06900  1.000 64.19191  ? 293 ASP B N     1 
ATOM   5771 C  CA    . ASP B 1 293 ? 18.93500  -5.89000  41.66200  1.000 61.88374  ? 293 ASP B CA    1 
ATOM   5772 C  C     . ASP B 1 293 ? 17.94300  -6.47800  42.65700  1.000 58.33594  ? 293 ASP B C     1 
ATOM   5773 O  O     . ASP B 1 293 ? 16.92800  -7.06300  42.26000  1.000 56.21727  ? 293 ASP B O     1 
ATOM   5774 C  CB    . ASP B 1 293 ? 20.14500  -6.80900  41.51900  1.000 67.14752  ? 293 ASP B CB    1 
ATOM   5775 C  CG    . ASP B 1 293 ? 20.81300  -6.68300  40.16500  1.000 81.53083  ? 293 ASP B CG    1 
ATOM   5776 O  OD1   . ASP B 1 293 ? 20.14300  -6.23400  39.21000  1.000 82.57306  ? 293 ASP B OD1   1 
ATOM   5777 O  OD2   . ASP B 1 293 ? 22.00700  -7.04200  40.05800  1.000 74.07993  ? 293 ASP B OD2   1 
ATOM   5778 N  N     . MET B 1 294 ? 18.22300  -6.33100  43.95600  1.000 58.97549  ? 294 MET B N     1 
ATOM   5779 C  CA    . MET B 1 294 ? 17.34000  -6.87500  44.98100  1.000 54.47232  ? 294 MET B CA    1 
ATOM   5780 C  C     . MET B 1 294 ? 16.02100  -6.11400  45.05100  1.000 49.54805  ? 294 MET B C     1 
ATOM   5781 O  O     . MET B 1 294 ? 14.98100  -6.71200  45.34900  1.000 49.60595  ? 294 MET B O     1 
ATOM   5782 C  CB    . MET B 1 294 ? 18.04700  -6.86300  46.33800  1.000 49.95599  ? 294 MET B CB    1 
ATOM   5783 C  CG    . MET B 1 294 ? 17.39400  -7.74600  47.38900  1.000 55.76195  ? 294 MET B CG    1 
ATOM   5784 S  SD    . MET B 1 294 ? 17.35900  -9.50700  46.99400  1.000 58.58860  ? 294 MET B SD    1 
ATOM   5785 C  CE    . MET B 1 294 ? 19.04000  -9.97500  47.40100  1.000 59.32553  ? 294 MET B CE    1 
ATOM   5786 N  N     . VAL B 1 295 ? 16.04000  -4.80600  44.78100  1.000 46.65823  ? 295 VAL B N     1 
ATOM   5787 C  CA    . VAL B 1 295 ? 14.80300  -4.03000  44.73600  1.000 52.06940  ? 295 VAL B CA    1 
ATOM   5788 C  C     . VAL B 1 295 ? 13.92300  -4.49600  43.58200  1.000 54.24335  ? 295 VAL B C     1 
ATOM   5789 O  O     . VAL B 1 295 ? 12.71200  -4.69100  43.74000  1.000 49.90072  ? 295 VAL B O     1 
ATOM   5790 C  CB    . VAL B 1 295 ? 15.11500  -2.52500  44.63600  1.000 48.65057  ? 295 VAL B CB    1 
ATOM   5791 C  CG1   . VAL B 1 295 ? 13.84700  -1.73600  44.32100  1.000 44.42375  ? 295 VAL B CG1   1 
ATOM   5792 C  CG2   . VAL B 1 295 ? 15.74700  -2.02500  45.92800  1.000 43.49206  ? 295 VAL B CG2   1 
ATOM   5793 N  N     . ARG B 1 296 ? 14.52200  -4.67100  42.40200  1.000 45.73969  ? 296 ARG B N     1 
ATOM   5794 C  CA    . ARG B 1 296 ? 13.79700  -5.19600  41.24800  1.000 57.01473  ? 296 ARG B CA    1 
ATOM   5795 C  C     . ARG B 1 296 ? 13.19100  -6.55900  41.55600  1.000 46.52400  ? 296 ARG B C     1 
ATOM   5796 O  O     . ARG B 1 296 ? 12.02000  -6.81800  41.24800  1.000 47.00037  ? 296 ARG B O     1 
ATOM   5797 C  CB    . ARG B 1 296 ? 14.73400  -5.29000  40.04200  1.000 57.88326  ? 296 ARG B CB    1 
ATOM   5798 C  CG    . ARG B 1 296 ? 14.12700  -5.97900  38.82600  1.000 81.66242  ? 296 ARG B CG    1 
ATOM   5799 C  CD    . ARG B 1 296 ? 15.02500  -5.87000  37.59200  1.000 95.96940  ? 296 ARG B CD    1 
ATOM   5800 N  NE    . ARG B 1 296 ? 15.43200  -4.49500  37.30400  1.000 109.59472 ? 296 ARG B NE    1 
ATOM   5801 C  CZ    . ARG B 1 296 ? 16.63300  -3.99300  37.57900  1.000 96.73528  ? 296 ARG B CZ    1 
ATOM   5802 N  NH1   . ARG B 1 296 ? 17.55700  -4.75200  38.15400  1.000 87.59998  ? 296 ARG B NH1   1 
ATOM   5803 N  NH2   . ARG B 1 296 ? 16.91000  -2.73100  37.28200  1.000 98.50655  ? 296 ARG B NH2   1 
ATOM   5804 N  N     . TYR B 1 297 ? 13.99200  -7.45500  42.13600  1.000 48.32158  ? 297 TYR B N     1 
ATOM   5805 C  CA    . TYR B 1 297 ? 13.48500  -8.75800  42.55200  1.000 53.33271  ? 297 TYR B CA    1 
ATOM   5806 C  C     . TYR B 1 297 ? 12.30600  -8.61200  43.50800  1.000 54.78288  ? 297 TYR B C     1 
ATOM   5807 O  O     . TYR B 1 297 ? 11.24900  -9.22100  43.30400  1.000 47.45832  ? 297 TYR B O     1 
ATOM   5808 C  CB    . TYR B 1 297 ? 14.61100  -9.56900  43.19600  1.000 51.64830  ? 297 TYR B CB    1 
ATOM   5809 C  CG    . TYR B 1 297 ? 14.13800  -10.77700 43.96800  1.000 53.48536  ? 297 TYR B CG    1 
ATOM   5810 C  CD1   . TYR B 1 297 ? 13.88500  -11.98500 43.32900  1.000 61.55738  ? 297 TYR B CD1   1 
ATOM   5811 C  CD2   . TYR B 1 297 ? 13.94800  -10.71200 45.34300  1.000 61.99428  ? 297 TYR B CD2   1 
ATOM   5812 C  CE1   . TYR B 1 297 ? 13.45100  -13.09200 44.04000  1.000 66.08950  ? 297 TYR B CE1   1 
ATOM   5813 C  CE2   . TYR B 1 297 ? 13.51300  -11.80700 46.05800  1.000 57.78324  ? 297 TYR B CE2   1 
ATOM   5814 C  CZ    . TYR B 1 297 ? 13.26700  -12.99400 45.40500  1.000 72.18497  ? 297 TYR B CZ    1 
ATOM   5815 O  OH    . TYR B 1 297 ? 12.83800  -14.08300 46.12800  1.000 66.89223  ? 297 TYR B OH    1 
ATOM   5816 N  N     . ALA B 1 298 ? 12.46900  -7.79400  44.55300  1.000 47.90311  ? 298 ALA B N     1 
ATOM   5817 C  CA    . ALA B 1 298 ? 11.41600  -7.63200  45.55100  1.000 47.57413  ? 298 ALA B CA    1 
ATOM   5818 C  C     . ALA B 1 298 ? 10.11600  -7.16200  44.91400  1.000 50.56922  ? 298 ALA B C     1 
ATOM   5819 O  O     . ALA B 1 298 ? 9.04200   -7.70400  45.19800  1.000 38.58884  ? 298 ALA B O     1 
ATOM   5820 C  CB    . ALA B 1 298 ? 11.86500  -6.65500  46.63800  1.000 47.86890  ? 298 ALA B CB    1 
ATOM   5821 N  N     . ARG B 1 299 ? 10.19200  -6.15700  44.03700  1.000 41.76553  ? 299 ARG B N     1 
ATOM   5822 C  CA    . ARG B 1 299 ? 8.97300   -5.64600  43.42200  1.000 46.60559  ? 299 ARG B CA    1 
ATOM   5823 C  C     . ARG B 1 299 ? 8.31400   -6.69500  42.53800  1.000 57.86746  ? 299 ARG B C     1 
ATOM   5824 O  O     . ARG B 1 299 ? 7.08600   -6.69700  42.39300  1.000 54.87763  ? 299 ARG B O     1 
ATOM   5825 C  CB    . ARG B 1 299 ? 9.26800   -4.38000  42.62200  1.000 48.45055  ? 299 ARG B CB    1 
ATOM   5826 C  CG    . ARG B 1 299 ? 9.62500   -3.19200  43.48800  1.000 54.88553  ? 299 ARG B CG    1 
ATOM   5827 C  CD    . ARG B 1 299 ? 9.75400   -1.93200  42.66400  1.000 60.09931  ? 299 ARG B CD    1 
ATOM   5828 N  NE    . ARG B 1 299 ? 8.44000   -1.35400  42.40700  1.000 57.79904  ? 299 ARG B NE    1 
ATOM   5829 C  CZ    . ARG B 1 299 ? 8.22400   -0.29000  41.64100  1.000 52.07993  ? 299 ARG B CZ    1 
ATOM   5830 N  NH1   . ARG B 1 299 ? 9.24100   0.32500   41.04800  1.000 53.96700  ? 299 ARG B NH1   1 
ATOM   5831 N  NH2   . ARG B 1 299 ? 6.98800   0.16100   41.47300  1.000 60.19932  ? 299 ARG B NH2   1 
ATOM   5832 N  N     . ASN B 1 300 ? 9.10700   -7.60000  41.96000  1.000 50.37183  ? 300 ASN B N     1 
ATOM   5833 C  CA    . ASN B 1 300 ? 8.55600   -8.64800  41.10700  1.000 60.40461  ? 300 ASN B CA    1 
ATOM   5834 C  C     . ASN B 1 300 ? 7.89900   -9.75700  41.91800  1.000 49.95599  ? 300 ASN B C     1 
ATOM   5835 O  O     . ASN B 1 300 ? 6.81800   -10.23200 41.55300  1.000 65.76052  ? 300 ASN B O     1 
ATOM   5836 C  CB    . ASN B 1 300 ? 9.64800   -9.22700  40.20900  1.000 75.01952  ? 300 ASN B CB    1 
ATOM   5837 C  CG    . ASN B 1 300 ? 9.97000   -8.32800  39.03700  1.000 72.84031  ? 300 ASN B CG    1 
ATOM   5838 O  OD1   . ASN B 1 300 ? 9.07400   -7.81300  38.36900  1.000 110.93435 ? 300 ASN B OD1   1 
ATOM   5839 N  ND2   . ASN B 1 300 ? 11.25700  -8.12600  38.78500  1.000 68.50821  ? 300 ASN B ND2   1 
ATOM   5840 N  N     . VAL B 1 301 ? 8.53100   -10.18800 43.01300  1.000 53.63538  ? 301 VAL B N     1 
ATOM   5841 C  CA    . VAL B 1 301 ? 7.93400   -11.25100 43.81800  1.000 56.11989  ? 301 VAL B CA    1 
ATOM   5842 C  C     . VAL B 1 301 ? 6.63300   -10.77100 44.44600  1.000 42.23138  ? 301 VAL B C     1 
ATOM   5843 O  O     . VAL B 1 301 ? 5.70300   -11.56100 44.64500  1.000 45.77128  ? 301 VAL B O     1 
ATOM   5844 C  CB    . VAL B 1 301 ? 8.93500   -11.77400 44.86900  1.000 56.93051  ? 301 VAL B CB    1 
ATOM   5845 C  CG1   . VAL B 1 301 ? 9.31500   -10.69200 45.85900  1.000 69.61887  ? 301 VAL B CG1   1 
ATOM   5846 C  CG2   . VAL B 1 301 ? 8.36600   -12.98900 45.59100  1.000 64.18928  ? 301 VAL B CG2   1 
ATOM   5847 N  N     . ILE B 1 302 ? 6.53100   -9.47400  44.74100  1.000 41.42602  ? 302 ILE B N     1 
ATOM   5848 C  CA    . ILE B 1 302 ? 5.27400   -8.90300  45.21800  1.000 44.40269  ? 302 ILE B CA    1 
ATOM   5849 C  C     . ILE B 1 302 ? 4.16300   -9.13700  44.20000  1.000 46.30029  ? 302 ILE B C     1 
ATOM   5850 O  O     . ILE B 1 302 ? 3.02300   -9.45800  44.56200  1.000 37.24131  ? 302 ILE B O     1 
ATOM   5851 C  CB    . ILE B 1 302 ? 5.46200   -7.40700  45.52800  1.000 49.48488  ? 302 ILE B CB    1 
ATOM   5852 C  CG1   . ILE B 1 302 ? 6.28800   -7.23700  46.80300  1.000 52.86950  ? 302 ILE B CG1   1 
ATOM   5853 C  CG2   . ILE B 1 302 ? 4.12000   -6.70500  45.66100  1.000 45.08698  ? 302 ILE B CG2   1 
ATOM   5854 C  CD1   . ILE B 1 302 ? 6.73000   -5.82300  47.05000  1.000 63.00492  ? 302 ILE B CD1   1 
ATOM   5855 N  N     . GLU B 1 303 ? 4.47000   -8.94400  42.91400  1.000 43.62102  ? 303 GLU B N     1 
ATOM   5856 C  CA    . GLU B 1 303 ? 3.50100   -9.21400  41.85500  1.000 50.00073  ? 303 GLU B CA    1 
ATOM   5857 C  C     . GLU B 1 303 ? 3.24800   -10.70900 41.70000  1.000 40.72594  ? 303 GLU B C     1 
ATOM   5858 O  O     . GLU B 1 303 ? 2.10000   -11.14300 41.55000  1.000 42.28928  ? 303 GLU B O     1 
ATOM   5859 C  CB    . GLU B 1 303 ? 3.99600   -8.62400  40.53300  1.000 71.45067  ? 303 GLU B CB    1 
ATOM   5860 C  CG    . GLU B 1 303 ? 4.05500   -7.11200  40.51300  1.000 80.36227  ? 303 GLU B CG    1 
ATOM   5861 C  CD    . GLU B 1 303 ? 2.67800   -6.48600  40.52100  1.000 107.52342 ? 303 GLU B CD    1 
ATOM   5862 O  OE1   . GLU B 1 303 ? 1.73800   -7.11100  39.98800  1.000 148.54413 ? 303 GLU B OE1   1 
ATOM   5863 O  OE2   . GLU B 1 303 ? 2.53100   -5.37300  41.06900  1.000 130.97623 ? 303 GLU B OE2   1 
ATOM   5864 N  N     . GLU B 1 304 ? 4.31800   -11.51000 41.69100  1.000 47.07933  ? 304 GLU B N     1 
ATOM   5865 C  CA    . GLU B 1 304 ? 4.16000   -12.95800 41.58700  1.000 49.39540  ? 304 GLU B CA    1 
ATOM   5866 C  C     . GLU B 1 304 ? 3.33100   -13.51600 42.73900  1.000 43.94211  ? 304 GLU B C     1 
ATOM   5867 O  O     . GLU B 1 304 ? 2.48100   -14.38800 42.53000  1.000 43.87368  ? 304 GLU B O     1 
ATOM   5868 C  CB    . GLU B 1 304 ? 5.52800   -13.63500 41.54000  1.000 56.73575  ? 304 GLU B CB    1 
ATOM   5869 C  CG    . GLU B 1 304 ? 6.21800   -13.54800 40.19200  1.000 69.41095  ? 304 GLU B CG    1 
ATOM   5870 C  CD    . GLU B 1 304 ? 7.49400   -14.36100 40.14800  1.000 79.26477  ? 304 GLU B CD    1 
ATOM   5871 O  OE1   . GLU B 1 304 ? 7.87100   -14.92300 41.19700  1.000 86.17086  ? 304 GLU B OE1   1 
ATOM   5872 O  OE2   . GLU B 1 304 ? 8.11900   -14.43800 39.07000  1.000 91.61098  ? 304 GLU B OE2   1 
ATOM   5873 N  N     . PHE B 1 305 ? 3.56200   -13.02900 43.96300  1.000 39.30471  ? 305 PHE B N     1 
ATOM   5874 C  CA    . PHE B 1 305 ? 2.80200   -13.54000 45.10000  1.000 37.98087  ? 305 PHE B CA    1 
ATOM   5875 C  C     . PHE B 1 305 ? 1.33500   -13.14800 45.00600  1.000 41.44971  ? 305 PHE B C     1 
ATOM   5876 O  O     . PHE B 1 305 ? 0.45600   -13.94200 45.36200  1.000 37.38606  ? 305 PHE B O     1 
ATOM   5877 C  CB    . PHE B 1 305 ? 3.39700   -13.05900 46.42300  1.000 35.46478  ? 305 PHE B CB    1 
ATOM   5878 C  CG    . PHE B 1 305 ? 2.79100   -13.73900 47.62200  1.000 32.39862  ? 305 PHE B CG    1 
ATOM   5879 C  CD1   . PHE B 1 305 ? 3.27500   -14.96500 48.05500  1.000 34.40676  ? 305 PHE B CD1   1 
ATOM   5880 C  CD2   . PHE B 1 305 ? 1.71200   -13.17800 48.28500  1.000 28.94031  ? 305 PHE B CD2   1 
ATOM   5881 C  CE1   . PHE B 1 305 ? 2.70600   -15.60500 49.14500  1.000 37.06760  ? 305 PHE B CE1   1 
ATOM   5882 C  CE2   . PHE B 1 305 ? 1.13900   -13.81300 49.37000  1.000 30.95371  ? 305 PHE B CE2   1 
ATOM   5883 C  CZ    . PHE B 1 305 ? 1.63800   -15.02700 49.80500  1.000 31.34323  ? 305 PHE B CZ    1 
ATOM   5884 N  N     . ARG B 1 306 ? 1.05100   -11.92200 44.55100  1.000 43.52364  ? 306 ARG B N     1 
ATOM   5885 C  CA    . ARG B 1 306 ? -0.33400  -11.48700 44.37900  1.000 47.95838  ? 306 ARG B CA    1 
ATOM   5886 C  C     . ARG B 1 306 ? -1.10000  -12.43300 43.46200  1.000 44.55271  ? 306 ARG B C     1 
ATOM   5887 O  O     . ARG B 1 306 ? -2.27600  -12.73100 43.70300  1.000 51.49302  ? 306 ARG B O     1 
ATOM   5888 C  CB    . ARG B 1 306 ? -0.37500  -10.07000 43.81000  1.000 49.38487  ? 306 ARG B CB    1 
ATOM   5889 C  CG    . ARG B 1 306 ? -1.77200  -9.47400  43.74600  1.000 57.39109  ? 306 ARG B CG    1 
ATOM   5890 C  CD    . ARG B 1 306 ? -1.75300  -8.02600  43.27800  1.000 75.14059  ? 306 ARG B CD    1 
ATOM   5891 N  NE    . ARG B 1 306 ? -1.02500  -7.13800  44.18000  1.000 91.90312  ? 306 ARG B NE    1 
ATOM   5892 C  CZ    . ARG B 1 306 ? 0.00200   -6.38100  43.80500  1.000 87.97107  ? 306 ARG B CZ    1 
ATOM   5893 N  NH1   . ARG B 1 306 ? 0.41000   -6.40700  42.54500  1.000 101.85169 ? 306 ARG B NH1   1 
ATOM   5894 N  NH2   . ARG B 1 306 ? 0.61600   -5.59600  44.68100  1.000 63.99451  ? 306 ARG B NH2   1 
ATOM   5895 N  N     A ARG B 1 307 ? -0.42400  -12.95400 42.44800  0.500 45.87919  ? 307 ARG B N     1 
ATOM   5896 N  N     B ARG B 1 307 ? -0.40900  -12.97400 42.46100  0.500 45.87919  ? 307 ARG B N     1 
ATOM   5897 C  CA    A ARG B 1 307 ? -1.07000  -13.88600 41.49100  0.500 52.32733  ? 307 ARG B CA    1 
ATOM   5898 C  CA    B ARG B 1 307 ? -1.04900  -13.88600 41.47800  0.500 52.32733  ? 307 ARG B CA    1 
ATOM   5899 C  C     A ARG B 1 307 ? -1.13200  -15.28400 42.10200  0.500 51.89570  ? 307 ARG B C     1 
ATOM   5900 C  C     B ARG B 1 307 ? -1.10600  -15.30800 42.03800  0.500 51.89570  ? 307 ARG B C     1 
ATOM   5901 O  O     A ARG B 1 307 ? -2.18500  -15.90000 42.03500  0.500 42.52878  ? 307 ARG B O     1 
ATOM   5902 O  O     B ARG B 1 307 ? -2.20900  -15.86200 42.08100  0.500 42.52878  ? 307 ARG B O     1 
ATOM   5903 C  CB    A ARG B 1 307 ? -0.27900  -13.90900 40.18300  0.500 56.25148  ? 307 ARG B CB    1 
ATOM   5904 C  CB    B ARG B 1 307 ? -0.26800  -13.87000 40.16200  0.500 56.25148  ? 307 ARG B CB    1 
ATOM   5905 C  CG    A ARG B 1 307 ? -0.80700  -14.88800 39.15200  0.500 73.96150  ? 307 ARG B CG    1 
ATOM   5906 C  CG    B ARG B 1 307 ? -0.78100  -14.85700 39.12900  0.500 73.96150  ? 307 ARG B CG    1 
ATOM   5907 C  CD    A ARG B 1 307 ? -1.78400  -14.25800 38.18800  0.500 74.00098  ? 307 ARG B CD    1 
ATOM   5908 C  CD    B ARG B 1 307 ? -1.91400  -14.28500 38.30600  0.500 74.00098  ? 307 ARG B CD    1 
ATOM   5909 N  NE    A ARG B 1 307 ? -2.21900  -15.24300 37.21400  0.500 87.85790  ? 307 ARG B NE    1 
ATOM   5910 N  NE    B ARG B 1 307 ? -2.02100  -14.96300 37.02500  0.500 87.85790  ? 307 ARG B NE    1 
ATOM   5911 C  CZ    A ARG B 1 307 ? -3.14100  -16.17200 37.45000  0.500 95.48513  ? 307 ARG B CZ    1 
ATOM   5912 C  CZ    B ARG B 1 307 ? -1.47400  -14.52300 35.89900  0.500 95.48513  ? 307 ARG B CZ    1 
ATOM   5913 N  NH1   A ARG B 1 307 ? -3.72500  -16.24500 38.63200  0.500 97.65118  ? 307 ARG B NH1   1 
ATOM   5914 N  NH1   B ARG B 1 307 ? -0.78000  -13.39900 35.89700  0.500 97.65118  ? 307 ARG B NH1   1 
ATOM   5915 N  NH2   A ARG B 1 307 ? -3.49100  -17.02400 36.50900  0.500 83.94164  ? 307 ARG B NH2   1 
ATOM   5916 N  NH2   B ARG B 1 307 ? -1.62600  -15.19800 34.77400  0.500 83.94164  ? 307 ARG B NH2   1 
ATOM   5917 N  N     . ALA B 1 308 ? -0.03800  -15.72500 42.71600  1.000 44.17109  ? 308 ALA B N     1 
ATOM   5918 C  CA    . ALA B 1 308 ? 0.02100   -17.07800 43.26900  1.000 47.11618  ? 308 ALA B CA    1 
ATOM   5919 C  C     . ALA B 1 308 ? -1.02400  -17.32400 44.35300  1.000 48.51634  ? 308 ALA B C     1 
ATOM   5920 O  O     . ALA B 1 308 ? -1.46100  -18.46500 44.53900  1.000 51.16666  ? 308 ALA B O     1 
ATOM   5921 C  CB    . ALA B 1 308 ? 1.42100   -17.35900 43.81800  1.000 49.93230  ? 308 ALA B CB    1 
ATOM   5922 N  N     . LYS B 1 309 ? -1.41500  -16.29000 45.09900  1.000 40.29957  ? 309 LYS B N     1 
ATOM   5923 C  CA    . LYS B 1 309 ? -2.37500  -16.49700 46.18100  1.000 54.74604  ? 309 LYS B CA    1 
ATOM   5924 C  C     . LYS B 1 309 ? -3.74200  -16.94200 45.67200  1.000 56.38571  ? 309 LYS B C     1 
ATOM   5925 O  O     . LYS B 1 309 ? -4.57800  -17.36200 46.48100  1.000 68.37399  ? 309 LYS B O     1 
ATOM   5926 C  CB    . LYS B 1 309 ? -2.48700  -15.23800 47.05100  1.000 44.50270  ? 309 LYS B CB    1 
ATOM   5927 C  CG    . LYS B 1 309 ? -3.25000  -14.09000 46.44000  1.000 63.82081  ? 309 LYS B CG    1 
ATOM   5928 C  CD    . LYS B 1 309 ? -2.98500  -12.80600 47.20900  1.000 74.57999  ? 309 LYS B CD    1 
ATOM   5929 C  CE    . LYS B 1 309 ? -3.15900  -12.99300 48.70800  1.000 53.57221  ? 309 LYS B CE    1 
ATOM   5930 N  NZ    . LYS B 1 309 ? -3.01800  -11.69600 49.42600  1.000 62.93123  ? 309 LYS B NZ    1 
ATOM   5931 N  N     . HIS B 1 310 ? -3.99500  -16.84900 44.36400  1.000 75.81172  ? 310 HIS B N     1 
ATOM   5932 C  CA    . HIS B 1 310 ? -5.28100  -17.26000 43.80900  1.000 80.99129  ? 310 HIS B CA    1 
ATOM   5933 C  C     . HIS B 1 310 ? -5.41000  -18.77500 43.67800  1.000 76.48022  ? 310 HIS B C     1 
ATOM   5934 O  O     . HIS B 1 310 ? -6.53100  -19.29400 43.71000  1.000 81.43345  ? 310 HIS B O     1 
ATOM   5935 C  CB    . HIS B 1 310 ? -5.50900  -16.61300 42.44100  1.000 75.63275  ? 310 HIS B CB    1 
ATOM   5936 C  CG    . HIS B 1 310 ? -5.74000  -15.13500 42.49500  1.000 75.52484  ? 310 HIS B CG    1 
ATOM   5937 N  ND1   . HIS B 1 310 ? -6.84900  -14.57700 43.09300  1.000 94.62187  ? 310 HIS B ND1   1 
ATOM   5938 C  CD2   . HIS B 1 310 ? -5.01300  -14.10000 42.01300  1.000 96.00362  ? 310 HIS B CD2   1 
ATOM   5939 C  CE1   . HIS B 1 310 ? -6.79200  -13.26200 42.98400  1.000 84.42854  ? 310 HIS B CE1   1 
ATOM   5940 N  NE2   . HIS B 1 310 ? -5.68800  -12.94600 42.33200  1.000 81.48082  ? 310 HIS B NE2   1 
ATOM   5941 N  N     . TYR B 1 311 ? -4.30300  -19.50000 43.50400  1.000 57.09632  ? 311 TYR B N     1 
ATOM   5942 C  CA    . TYR B 1 311 ? -4.41000  -20.92400 43.19700  1.000 58.79652  ? 311 TYR B CA    1 
ATOM   5943 C  C     . TYR B 1 311 ? -3.54200  -21.82500 44.07800  1.000 66.05792  ? 311 TYR B C     1 
ATOM   5944 O  O     . TYR B 1 311 ? -3.84100  -23.01600 44.21600  1.000 73.56408  ? 311 TYR B O     1 
ATOM   5945 C  CB    . TYR B 1 311 ? -4.09700  -21.16800 41.71400  1.000 76.05912  ? 311 TYR B CB    1 
ATOM   5946 C  CG    . TYR B 1 311 ? -2.73000  -20.70800 41.25300  1.000 83.26525  ? 311 TYR B CG    1 
ATOM   5947 C  CD1   . TYR B 1 311 ? -2.54200  -19.42700 40.74700  1.000 75.69065  ? 311 TYR B CD1   1 
ATOM   5948 C  CD2   . TYR B 1 311 ? -1.63300  -21.56100 41.30400  1.000 90.91353  ? 311 TYR B CD2   1 
ATOM   5949 C  CE1   . TYR B 1 311 ? -1.29700  -19.00300 40.31900  1.000 79.85694  ? 311 TYR B CE1   1 
ATOM   5950 C  CE2   . TYR B 1 311 ? -0.38400  -21.14700 40.87700  1.000 88.90540  ? 311 TYR B CE2   1 
ATOM   5951 C  CZ    . TYR B 1 311 ? -0.22200  -19.86700 40.38600  1.000 85.60763  ? 311 TYR B CZ    1 
ATOM   5952 O  OH    . TYR B 1 311 ? 1.02000   -19.44900 39.96200  1.000 86.13664  ? 311 TYR B OH    1 
ATOM   5953 N  N     . LYS B 1 312 ? -2.46400  -21.29900 44.65800  1.000 48.81375  ? 312 LYS B N     1 
ATOM   5954 C  CA    . LYS B 1 312 ? -1.56900  -22.14800 45.43600  1.000 51.07981  ? 312 LYS B CA    1 
ATOM   5955 C  C     . LYS B 1 312 ? -2.10000  -22.39400 46.85200  1.000 45.90550  ? 312 LYS B C     1 
ATOM   5956 O  O     . LYS B 1 312 ? -2.86700  -21.60200 47.41000  1.000 36.41752  ? 312 LYS B O     1 
ATOM   5957 C  CB    . LYS B 1 312 ? -0.16300  -21.54700 45.49200  1.000 58.62019  ? 312 LYS B CB    1 
ATOM   5958 C  CG    . LYS B 1 312 ? 0.67000   -21.80500 44.23900  1.000 63.13652  ? 312 LYS B CG    1 
ATOM   5959 C  CD    . LYS B 1 312 ? 2.05600   -21.19300 44.36900  1.000 64.14980  ? 312 LYS B CD    1 
ATOM   5960 C  CE    . LYS B 1 312 ? 2.91800   -21.46400 43.14400  1.000 74.15889  ? 312 LYS B CE    1 
ATOM   5961 N  NZ    . LYS B 1 312 ? 3.37600   -22.88300 43.10300  1.000 77.57509  ? 312 LYS B NZ    1 
ATOM   5962 N  N     . SER B 1 313 ? -1.66400  -23.51500 47.43500  1.000 45.14225  ? 313 SER B N     1 
ATOM   5963 C  CA    . SER B 1 313 ? -2.10500  -23.91200 48.76300  1.000 49.82176  ? 313 SER B CA    1 
ATOM   5964 C  C     . SER B 1 313 ? -1.47300  -23.01700 49.82500  1.000 52.74843  ? 313 SER B C     1 
ATOM   5965 O  O     . SER B 1 313 ? -0.44100  -22.38500 49.58300  1.000 45.23437  ? 313 SER B O     1 
ATOM   5966 C  CB    . SER B 1 313 ? -1.73900  -25.36700 49.04400  1.000 52.66684  ? 313 SER B CB    1 
ATOM   5967 O  OG    . SER B 1 313 ? -0.37200  -25.48900 49.40000  1.000 50.73240  ? 313 SER B OG    1 
ATOM   5968 N  N     . PRO B 1 314 ? -2.07700  -22.95200 51.01700  1.000 43.89210  ? 314 PRO B N     1 
ATOM   5969 C  CA    . PRO B 1 314 ? -1.48900  -22.11500 52.08300  1.000 44.75273  ? 314 PRO B CA    1 
ATOM   5970 C  C     . PRO B 1 314 ? -0.04500  -22.46200 52.41700  1.000 41.84975  ? 314 PRO B C     1 
ATOM   5971 O  O     . PRO B 1 314 ? 0.79200   -21.55600 52.53700  1.000 40.84700  ? 314 PRO B O     1 
ATOM   5972 C  CB    . PRO B 1 314 ? -2.43700  -22.36000 53.26500  1.000 48.84796  ? 314 PRO B CB    1 
ATOM   5973 C  CG    . PRO B 1 314 ? -3.74500  -22.71000 52.62500  1.000 48.55582  ? 314 PRO B CG    1 
ATOM   5974 C  CD    . PRO B 1 314 ? -3.38000  -23.51700 51.41300  1.000 55.29347  ? 314 PRO B CD    1 
ATOM   5975 N  N     . SER B 1 315 ? 0.27500   -23.75100 52.56500  1.000 46.62664  ? 315 SER B N     1 
ATOM   5976 C  CA    . SER B 1 315 ? 1.64300   -24.14700 52.88900  1.000 54.19071  ? 315 SER B CA    1 
ATOM   5977 C  C     . SER B 1 315 ? 2.61900   -23.73400 51.79200  1.000 52.73001  ? 315 SER B C     1 
ATOM   5978 O  O     . SER B 1 315 ? 3.76500   -23.36800 52.08000  1.000 50.55606  ? 315 SER B O     1 
ATOM   5979 C  CB    . SER B 1 315 ? 1.71300   -25.65500 53.12600  1.000 50.10338  ? 315 SER B CB    1 
ATOM   5980 O  OG    . SER B 1 315 ? 1.44700   -26.36700 51.92900  1.000 65.53681  ? 315 SER B OG    1 
ATOM   5981 N  N     . GLU B 1 316 ? 2.18600   -23.79900 50.52800  1.000 48.45055  ? 316 GLU B N     1 
ATOM   5982 C  CA    . GLU B 1 316 ? 3.03500   -23.36000 49.42200  1.000 52.02729  ? 316 GLU B CA    1 
ATOM   5983 C  C     . GLU B 1 316 ? 3.25600   -21.85200 49.45400  1.000 48.45055  ? 316 GLU B C     1 
ATOM   5984 O  O     . GLU B 1 316 ? 4.34700   -21.37100 49.12400  1.000 46.31608  ? 316 GLU B O     1 
ATOM   5985 C  CB    . GLU B 1 316 ? 2.41500   -23.78100 48.08800  1.000 51.81411  ? 316 GLU B CB    1 
ATOM   5986 C  CG    . GLU B 1 316 ? 2.48500   -25.27300 47.81400  1.000 67.57916  ? 316 GLU B CG    1 
ATOM   5987 C  CD    . GLU B 1 316 ? 1.66000   -25.68500 46.60700  1.000 69.15040  ? 316 GLU B CD    1 
ATOM   5988 O  OE1   . GLU B 1 316 ? 0.55100   -25.13400 46.42700  1.000 60.70201  ? 316 GLU B OE1   1 
ATOM   5989 O  OE2   . GLU B 1 316 ? 2.12000   -26.56000 45.84100  1.000 85.69449  ? 316 GLU B OE2   1 
ATOM   5990 N  N     . LEU B 1 317 ? 2.22400   -21.09200 49.83000  1.000 39.60475  ? 317 LEU B N     1 
ATOM   5991 C  CA    . LEU B 1 317 ? 2.35300   -19.64000 49.92800  1.000 38.29670  ? 317 LEU B CA    1 
ATOM   5992 C  C     . LEU B 1 317 ? 3.32900   -19.23100 51.02800  1.000 38.57568  ? 317 LEU B C     1 
ATOM   5993 O  O     . LEU B 1 317 ? 4.11000   -18.28600 50.85500  1.000 44.61851  ? 317 LEU B O     1 
ATOM   5994 C  CB    . LEU B 1 317 ? 0.97800   -19.01500 50.16900  1.000 37.58082  ? 317 LEU B CB    1 
ATOM   5995 C  CG    . LEU B 1 317 ? -0.00500  -19.10500 49.00000  1.000 39.49158  ? 317 LEU B CG    1 
ATOM   5996 C  CD1   . LEU B 1 317 ? -1.36600  -18.53100 49.36900  1.000 36.78599  ? 317 LEU B CD1   1 
ATOM   5997 C  CD2   . LEU B 1 317 ? 0.56600   -18.38200 47.79100  1.000 46.95300  ? 317 LEU B CD2   1 
ATOM   5998 N  N     . LEU B 1 318 ? 3.28000   -19.90900 52.17900  1.000 39.11522  ? 318 LEU B N     1 
ATOM   5999 C  CA    . LEU B 1 318 ? 4.24100   -19.62600 53.24200  1.000 45.15278  ? 318 LEU B CA    1 
ATOM   6000 C  C     . LEU B 1 318 ? 5.66400   -19.92100 52.78800  1.000 46.45820  ? 318 LEU B C     1 
ATOM   6001 O  O     . LEU B 1 318 ? 6.59700   -19.17400 53.10900  1.000 44.35005  ? 318 LEU B O     1 
ATOM   6002 C  CB    . LEU B 1 318 ? 3.90700   -20.44000 54.49400  1.000 38.16247  ? 318 LEU B CB    1 
ATOM   6003 C  CG    . LEU B 1 318 ? 2.75900   -19.95600 55.37400  1.000 39.97321  ? 318 LEU B CG    1 
ATOM   6004 C  CD1   . LEU B 1 318 ? 2.57000   -20.89900 56.55400  1.000 43.35783  ? 318 LEU B CD1   1 
ATOM   6005 C  CD2   . LEU B 1 318 ? 3.01600   -18.54500 55.86500  1.000 40.53118  ? 318 LEU B CD2   1 
ATOM   6006 N  N     . GLU B 1 319 ? 5.85000   -21.01800 52.04900  1.000 52.97214  ? 319 GLU B N     1 
ATOM   6007 C  CA    . GLU B 1 319 ? 7.17500   -21.36300 51.54500  1.000 53.94331  ? 319 GLU B CA    1 
ATOM   6008 C  C     . GLU B 1 319 ? 7.72400   -20.26000 50.64700  1.000 51.08770  ? 319 GLU B C     1 
ATOM   6009 O  O     . GLU B 1 319 ? 8.91700   -19.93700 50.70900  1.000 64.49194  ? 319 GLU B O     1 
ATOM   6010 C  CB    . GLU B 1 319 ? 7.12100   -22.70600 50.81900  1.000 56.59626  ? 319 GLU B CB    1 
ATOM   6011 C  CG    . GLU B 1 319 ? 8.47600   -23.25500 50.41100  1.000 76.69077  ? 319 GLU B CG    1 
ATOM   6012 C  CD    . GLU B 1 319 ? 8.38300   -24.66400 49.85400  1.000 98.13282  ? 319 GLU B CD    1 
ATOM   6013 O  OE1   . GLU B 1 319 ? 7.26900   -25.07600 49.46300  1.000 77.14083  ? 319 GLU B OE1   1 
ATOM   6014 O  OE2   . GLU B 1 319 ? 9.41900   -25.36300 49.82000  1.000 102.69389 ? 319 GLU B OE2   1 
ATOM   6015 N  N     . ILE B 1 320 ? 6.87400   -19.68300 49.79100  1.000 43.68419  ? 320 ILE B N     1 
ATOM   6016 C  CA    . ILE B 1 320 ? 7.30400   -18.56100 48.95700  1.000 43.99738  ? 320 ILE B CA    1 
ATOM   6017 C  C     . ILE B 1 320 ? 7.72200   -17.37800 49.82300  1.000 40.54960  ? 320 ILE B C     1 
ATOM   6018 O  O     . ILE B 1 320 ? 8.75000   -16.73600 49.57300  1.000 37.55977  ? 320 ILE B O     1 
ATOM   6019 C  CB    . ILE B 1 320 ? 6.18800   -18.16300 47.97500  1.000 41.86291  ? 320 ILE B CB    1 
ATOM   6020 C  CG1   . ILE B 1 320 ? 5.95100   -19.27400 46.95500  1.000 45.44229  ? 320 ILE B CG1   1 
ATOM   6021 C  CG2   . ILE B 1 320 ? 6.52000   -16.84700 47.29400  1.000 44.22372  ? 320 ILE B CG2   1 
ATOM   6022 C  CD1   . ILE B 1 320 ? 4.68300   -19.09500 46.15900  1.000 52.44839  ? 320 ILE B CD1   1 
ATOM   6023 N  N     . CYS B 1 321 ? 6.93400   -17.07500 50.85800  1.000 45.66074  ? 321 CYS B N     1 
ATOM   6024 C  CA    . CYS B 1 321 ? 7.26900   -15.97000 51.75000  1.000 40.96807  ? 321 CYS B CA    1 
ATOM   6025 C  C     . CYS B 1 321 ? 8.59500   -16.22200 52.45000  1.000 38.64148  ? 321 CYS B C     1 
ATOM   6026 O  O     . CYS B 1 321 ? 9.45000   -15.33300 52.52500  1.000 40.90490  ? 321 CYS B O     1 
ATOM   6027 C  CB    . CYS B 1 321 ? 6.15700   -15.77300 52.77900  1.000 43.22360  ? 321 CYS B CB    1 
ATOM   6028 S  SG    . CYS B 1 321 ? 4.60000   -15.15200 52.12000  1.000 37.62030  ? 321 CYS B SG    1 
ATOM   6029 N  N     . GLU B 1 322 ? 8.78100   -17.44000 52.96700  1.000 36.28330  ? 322 GLU B N     1 
ATOM   6030 C  CA    . GLU B 1 322 ? 10.01200  -17.78200 53.67100  1.000 39.30471  ? 322 GLU B CA    1 
ATOM   6031 C  C     . GLU B 1 322 ? 11.21800  -17.66900 52.75000  1.000 43.26835  ? 322 GLU B C     1 
ATOM   6032 O  O     . GLU B 1 322 ? 12.22500  -17.04300 53.10100  1.000 43.48153  ? 322 GLU B O     1 
ATOM   6033 C  CB    . GLU B 1 322 ? 9.90300   -19.19100 54.25100  1.000 46.57401  ? 322 GLU B CB    1 
ATOM   6034 C  CG    . GLU B 1 322 ? 8.95000   -19.29700 55.43200  1.000 57.50426  ? 322 GLU B CG    1 
ATOM   6035 C  CD    . GLU B 1 322 ? 8.66500   -20.73300 55.82000  1.000 72.47974  ? 322 GLU B CD    1 
ATOM   6036 O  OE1   . GLU B 1 322 ? 9.55000   -21.59300 55.61700  1.000 94.53765  ? 322 GLU B OE1   1 
ATOM   6037 O  OE2   . GLU B 1 322 ? 7.54900   -21.00400 56.30900  1.000 73.67462  ? 322 GLU B OE2   1 
ATOM   6038 N  N     . LEU B 1 323 ? 11.13600  -18.28600 51.56800  1.000 38.59410  ? 323 LEU B N     1 
ATOM   6039 C  CA    . LEU B 1 323 ? 12.25400  -18.25200 50.62800  1.000 49.66385  ? 323 LEU B CA    1 
ATOM   6040 C  C     . LEU B 1 323 ? 12.56300  -16.83100 50.17600  1.000 45.93182  ? 323 LEU B C     1 
ATOM   6041 O  O     . LEU B 1 323 ? 13.73500  -16.45600 50.04300  1.000 53.11953  ? 323 LEU B O     1 
ATOM   6042 C  CB    . LEU B 1 323 ? 11.95500  -19.14400 49.42500  1.000 46.84246  ? 323 LEU B CB    1 
ATOM   6043 C  CG    . LEU B 1 323 ? 11.97700  -20.64600 49.71100  1.000 62.17588  ? 323 LEU B CG    1 
ATOM   6044 C  CD1   . LEU B 1 323 ? 11.56000  -21.44500 48.48200  1.000 51.44038  ? 323 LEU B CD1   1 
ATOM   6045 C  CD2   . LEU B 1 323 ? 13.35100  -21.07600 50.20800  1.000 56.01198  ? 323 LEU B CD2   1 
ATOM   6046 N  N     . SER B 1 324 ? 11.52900  -16.02500 49.92500  1.000 48.17683  ? 324 SER B N     1 
ATOM   6047 C  CA    A SER B 1 324 ? 11.76600  -14.65600 49.48000  0.500 49.49014  ? 324 SER B CA    1 
ATOM   6048 C  CA    B SER B 1 324 ? 11.75800  -14.65400 49.48400  0.500 49.49014  ? 324 SER B CA    1 
ATOM   6049 C  C     . SER B 1 324 ? 12.46000  -13.83800 50.56300  1.000 50.06390  ? 324 SER B C     1 
ATOM   6050 O  O     . SER B 1 324 ? 13.34600  -13.03000 50.26400  1.000 47.41095  ? 324 SER B O     1 
ATOM   6051 C  CB    A SER B 1 324 ? 10.45000  -13.99500 49.06200  0.500 41.69974  ? 324 SER B CB    1 
ATOM   6052 C  CB    B SER B 1 324 ? 10.43100  -14.00700 49.09000  0.500 41.69974  ? 324 SER B CB    1 
ATOM   6053 O  OG    A SER B 1 324 ? 9.56300   -13.86900 50.15700  0.500 54.51180  ? 324 SER B OG    1 
ATOM   6054 O  OG    B SER B 1 324 ? 10.57900  -13.22300 47.92100  0.500 54.51180  ? 324 SER B OG    1 
ATOM   6055 N  N     . GLN B 1 325 ? 12.07600  -14.04200 51.82700  1.000 45.18700  ? 325 GLN B N     1 
ATOM   6056 C  CA    . GLN B 1 325 ? 12.72900  -13.34700 52.93000  1.000 48.60056  ? 325 GLN B CA    1 
ATOM   6057 C  C     . GLN B 1 325 ? 14.18100  -13.78900 53.07600  1.000 50.58238  ? 325 GLN B C     1 
ATOM   6058 O  O     . GLN B 1 325 ? 15.07500  -12.95500 53.26100  1.000 45.78970  ? 325 GLN B O     1 
ATOM   6059 C  CB    . GLN B 1 325 ? 11.95800  -13.59500 54.22700  1.000 43.57891  ? 325 GLN B CB    1 
ATOM   6060 C  CG    . GLN B 1 325 ? 10.67100  -12.79400 54.34000  1.000 45.71864  ? 325 GLN B CG    1 
ATOM   6061 C  CD    . GLN B 1 325 ? 9.87300   -13.13300 55.58800  1.000 60.99416  ? 325 GLN B CD    1 
ATOM   6062 O  OE1   . GLN B 1 325 ? 10.29100  -12.83800 56.70900  1.000 58.71757  ? 325 GLN B OE1   1 
ATOM   6063 N  NE2   . GLN B 1 325 ? 8.71300   -13.75600 55.39600  1.000 48.80848  ? 325 GLN B NE2   1 
ATOM   6064 N  N     . GLU B 1 326 ? 14.43300  -15.09600 52.98200  1.000 52.10625  ? 326 GLU B N     1 
ATOM   6065 C  CA    . GLU B 1 326 ? 15.79700  -15.60700 53.08200  1.000 54.73814  ? 326 GLU B CA    1 
ATOM   6066 C  C     . GLU B 1 326 ? 16.70100  -14.97600 52.03000  1.000 50.31919  ? 326 GLU B C     1 
ATOM   6067 O  O     . GLU B 1 326 ? 17.81400  -14.53500 52.33700  1.000 67.09225  ? 326 GLU B O     1 
ATOM   6068 C  CB    . GLU B 1 326 ? 15.79000  -17.13100 52.95700  1.000 60.77044  ? 326 GLU B CB    1 
ATOM   6069 C  CG    . GLU B 1 326 ? 17.15400  -17.77900 53.12300  1.000 68.34767  ? 326 GLU B CG    1 
ATOM   6070 C  CD    . GLU B 1 326 ? 17.08900  -19.29200 53.04100  1.000 85.63395  ? 326 GLU B CD    1 
ATOM   6071 O  OE1   . GLU B 1 326 ? 16.05200  -19.86200 53.44100  1.000 104.49674 ? 326 GLU B OE1   1 
ATOM   6072 O  OE2   . GLU B 1 326 ? 18.07100  -19.90700 52.57000  1.000 96.73002  ? 326 GLU B OE2   1 
ATOM   6073 N  N     . LYS B 1 327 ? 16.23600  -14.92100 50.77900  1.000 52.33785  ? 327 LYS B N     1 
ATOM   6074 C  CA    . LYS B 1 327 ? 17.04200  -14.35100 49.70200  1.000 59.84665  ? 327 LYS B CA    1 
ATOM   6075 C  C     . LYS B 1 327 ? 17.29700  -12.86800 49.93600  1.000 55.11187  ? 327 LYS B C     1 
ATOM   6076 O  O     . LYS B 1 327 ? 18.43000  -12.38900 49.80800  1.000 54.17755  ? 327 LYS B O     1 
ATOM   6077 C  CB    . LYS B 1 327 ? 16.33400  -14.56800 48.36300  1.000 64.84198  ? 327 LYS B CB    1 
ATOM   6078 C  CG    . LYS B 1 327 ? 17.12100  -14.14600 47.13200  1.000 79.25950  ? 327 LYS B CG    1 
ATOM   6079 C  CD    . LYS B 1 327 ? 16.46400  -14.67900 45.86700  1.000 89.72655  ? 327 LYS B CD    1 
ATOM   6080 C  CE    . LYS B 1 327 ? 17.21900  -14.24300 44.61400  1.000 87.21572  ? 327 LYS B CE    1 
ATOM   6081 N  NZ    . LYS B 1 327 ? 18.55200  -14.89600 44.47400  1.000 90.19502  ? 327 LYS B NZ    1 
ATOM   6082 N  N     . MET B 1 328 ? 16.24700  -12.12700 50.29500  1.000 47.65308  ? 328 MET B N     1 
ATOM   6083 C  CA    . MET B 1 328 ? 16.37300  -10.69100 50.51400  1.000 50.88242  ? 328 MET B CA    1 
ATOM   6084 C  C     . MET B 1 328 ? 17.23100  -10.37100 51.73200  1.000 55.50402  ? 328 MET B C     1 
ATOM   6085 O  O     . MET B 1 328 ? 17.94000  -9.35600  51.73500  1.000 49.32170  ? 328 MET B O     1 
ATOM   6086 C  CB    . MET B 1 328 ? 14.98500  -10.06300 50.66000  1.000 46.08184  ? 328 MET B CB    1 
ATOM   6087 C  CG    . MET B 1 328 ? 14.19900  -10.01300 49.35700  1.000 46.48189  ? 328 MET B CG    1 
ATOM   6088 S  SD    . MET B 1 328 ? 12.65600  -9.08200  49.46600  1.000 47.84784  ? 328 MET B SD    1 
ATOM   6089 C  CE    . MET B 1 328 ? 11.75600  -10.01400 50.70000  1.000 39.42052  ? 328 MET B CE    1 
ATOM   6090 N  N     . SER B 1 329 ? 17.18600  -11.21800 52.76800  1.000 47.36621  ? 329 SER B N     1 
ATOM   6091 C  CA    . SER B 1 329 ? 17.86900  -10.91300 54.02200  1.000 53.41693  ? 329 SER B CA    1 
ATOM   6092 C  C     . SER B 1 329 ? 19.38000  -10.82200 53.86300  1.000 63.09967  ? 329 SER B C     1 
ATOM   6093 O  O     . SER B 1 329 ? 20.05300  -10.29800 54.75600  1.000 70.37423  ? 329 SER B O     1 
ATOM   6094 C  CB    . SER B 1 329 ? 17.53200  -11.96000 55.08400  1.000 51.36142  ? 329 SER B CB    1 
ATOM   6095 O  OG    . SER B 1 329 ? 18.10700  -13.21500 54.76300  1.000 54.95659  ? 329 SER B OG    1 
ATOM   6096 N  N     . SER B 1 330 ? 19.93400  -11.32700 52.76100  1.000 52.55893  ? 330 SER B N     1 
ATOM   6097 C  CA    . SER B 1 330 ? 21.35800  -11.14600 52.51400  1.000 65.63419  ? 330 SER B CA    1 
ATOM   6098 C  C     . SER B 1 330 ? 21.71800  -9.68500  52.27300  1.000 60.94152  ? 330 SER B C     1 
ATOM   6099 O  O     . SER B 1 330 ? 22.88400  -9.31300  52.44300  1.000 72.51659  ? 330 SER B O     1 
ATOM   6100 C  CB    . SER B 1 330 ? 21.79900  -12.00100 51.32500  1.000 61.35736  ? 330 SER B CB    1 
ATOM   6101 O  OG    . SER B 1 330 ? 21.08600  -11.64900 50.15400  1.000 64.62617  ? 330 SER B OG    1 
ATOM   6102 N  N     . VAL B 1 331 ? 20.74500  -8.84900  51.89900  1.000 66.23689  ? 331 VAL B N     1 
ATOM   6103 C  CA    . VAL B 1 331 ? 20.97600  -7.43800  51.62100  1.000 65.36047  ? 331 VAL B CA    1 
ATOM   6104 C  C     . VAL B 1 331 ? 20.09600  -6.53300  52.47600  1.000 54.16965  ? 331 VAL B C     1 
ATOM   6105 O  O     . VAL B 1 331 ? 20.56300  -5.50500  52.98100  1.000 59.90718  ? 331 VAL B O     1 
ATOM   6106 C  CB    . VAL B 1 331 ? 20.76800  -7.13100  50.12100  1.000 60.92309  ? 331 VAL B CB    1 
ATOM   6107 C  CG1   . VAL B 1 331 ? 20.95700  -5.64900  49.84400  1.000 63.21811  ? 331 VAL B CG1   1 
ATOM   6108 C  CG2   . VAL B 1 331 ? 21.72000  -7.96000  49.27300  1.000 66.05792  ? 331 VAL B CG2   1 
ATOM   6109 N  N     . PHE B 1 332 ? 18.82700  -6.89400  52.65900  1.000 47.03459  ? 332 PHE B N     1 
ATOM   6110 C  CA    . PHE B 1 332 ? 17.85700  -6.04300  53.33900  1.000 44.57903  ? 332 PHE B CA    1 
ATOM   6111 C  C     . PHE B 1 332 ? 17.79000  -6.33200  54.83600  1.000 43.37099  ? 332 PHE B C     1 
ATOM   6112 O  O     . PHE B 1 332 ? 17.84900  -7.48900  55.26300  1.000 52.52998  ? 332 PHE B O     1 
ATOM   6113 C  CB    . PHE B 1 332 ? 16.46300  -6.22900  52.73400  1.000 41.56551  ? 332 PHE B CB    1 
ATOM   6114 C  CG    . PHE B 1 332 ? 16.33300  -5.73500  51.31800  1.000 44.60798  ? 332 PHE B CG    1 
ATOM   6115 C  CD1   . PHE B 1 332 ? 17.28400  -4.88800  50.76800  1.000 45.98972  ? 332 PHE B CD1   1 
ATOM   6116 C  CD2   . PHE B 1 332 ? 15.23800  -6.10100  50.54400  1.000 39.14680  ? 332 PHE B CD2   1 
ATOM   6117 C  CE1   . PHE B 1 332 ? 17.15400  -4.42300  49.47500  1.000 44.25004  ? 332 PHE B CE1   1 
ATOM   6118 C  CE2   . PHE B 1 332 ? 15.10200  -5.64000  49.24900  1.000 38.63095  ? 332 PHE B CE2   1 
ATOM   6119 C  CZ    . PHE B 1 332 ? 16.06400  -4.79700  48.71400  1.000 43.53154  ? 332 PHE B CZ    1 
ATOM   6120 N  N     . GLU B 1 333 ? 17.64800  -5.26700  55.62600  1.000 42.86303  ? 333 GLU B N     1 
ATOM   6121 C  CA    . GLU B 1 333 ? 17.32500  -5.38300  57.04100  1.000 47.52412  ? 333 GLU B CA    1 
ATOM   6122 C  C     . GLU B 1 333 ? 15.86300  -5.79400  57.22400  1.000 41.15230  ? 333 GLU B C     1 
ATOM   6123 O  O     . GLU B 1 333 ? 15.04300  -5.70300  56.30600  1.000 39.86794  ? 333 GLU B O     1 
ATOM   6124 C  CB    . GLU B 1 333 ? 17.58600  -4.05500  57.76100  1.000 56.86471  ? 333 GLU B CB    1 
ATOM   6125 C  CG    . GLU B 1 333 ? 19.05300  -3.74700  58.03400  1.000 73.87202  ? 333 GLU B CG    1 
ATOM   6126 C  CD    . GLU B 1 333 ? 19.62300  -4.53700  59.20000  1.000 78.11989  ? 333 GLU B CD    1 
ATOM   6127 O  OE1   . GLU B 1 333 ? 18.85900  -5.27800  59.85600  1.000 89.14227  ? 333 GLU B OE1   1 
ATOM   6128 O  OE2   . GLU B 1 333 ? 20.84000  -4.42300  59.45500  1.000 97.37746  ? 333 GLU B OE2   1 
ATOM   6129 N  N     . ASP B 1 334 ? 15.53600  -6.24800  58.43800  1.000 44.82906  ? 334 ASP B N     1 
ATOM   6130 C  CA    . ASP B 1 334 ? 14.16900  -6.68600  58.71700  1.000 46.92142  ? 334 ASP B CA    1 
ATOM   6131 C  C     . ASP B 1 334 ? 13.16100  -5.54800  58.60800  1.000 50.88505  ? 334 ASP B C     1 
ATOM   6132 O  O     . ASP B 1 334 ? 11.99300  -5.79100  58.28700  1.000 54.55128  ? 334 ASP B O     1 
ATOM   6133 C  CB    . ASP B 1 334 ? 14.09200  -7.33500  60.09900  1.000 57.78851  ? 334 ASP B CB    1 
ATOM   6134 C  CG    . ASP B 1 334 ? 14.61600  -8.75900  60.10500  1.000 66.40533  ? 334 ASP B CG    1 
ATOM   6135 O  OD1   . ASP B 1 334 ? 15.08500  -9.22700  59.04500  1.000 56.13041  ? 334 ASP B OD1   1 
ATOM   6136 O  OD2   . ASP B 1 334 ? 14.55300  -9.41000  61.17100  1.000 66.08161  ? 334 ASP B OD2   1 
ATOM   6137 N  N     . SER B 1 335 ? 13.57600  -4.31400  58.88500  1.000 39.26787  ? 335 SER B N     1 
ATOM   6138 C  CA    . SER B 1 335 ? 12.68100  -3.16700  58.77900  1.000 37.98087  ? 335 SER B CA    1 
ATOM   6139 C  C     . SER B 1 335 ? 12.52700  -2.65400  57.34700  1.000 33.25662  ? 335 SER B C     1 
ATOM   6140 O  O     . SER B 1 335 ? 11.75500  -1.71300  57.12800  1.000 34.86997  ? 335 SER B O     1 
ATOM   6141 C  CB    . SER B 1 335 ? 13.16200  -2.03800  59.69800  1.000 35.44372  ? 335 SER B CB    1 
ATOM   6142 O  OG    . SER B 1 335 ? 14.39200  -1.49500  59.24700  1.000 45.27122  ? 335 SER B OG    1 
ATOM   6143 N  N     . ASN B 1 336 ? 13.25100  -3.22800  56.38300  1.000 31.95120  ? 336 ASN B N     1 
ATOM   6144 C  CA    . ASN B 1 336 ? 13.07800  -2.88600  54.97300  1.000 32.68813  ? 336 ASN B CA    1 
ATOM   6145 C  C     . ASN B 1 336 ? 11.65800  -3.22400  54.52700  1.000 31.65906  ? 336 ASN B C     1 
ATOM   6146 O  O     . ASN B 1 336 ? 11.16500  -4.32400  54.78800  1.000 33.45401  ? 336 ASN B O     1 
ATOM   6147 C  CB    . ASN B 1 336 ? 14.11200  -3.65300  54.13900  1.000 31.88540  ? 336 ASN B CB    1 
ATOM   6148 C  CG    . ASN B 1 336 ? 14.08600  -3.29200  52.66000  1.000 36.46753  ? 336 ASN B CG    1 
ATOM   6149 O  OD1   . ASN B 1 336 ? 13.08700  -3.49500  51.97000  1.000 37.54924  ? 336 ASN B OD1   1 
ATOM   6150 N  ND2   . ASN B 1 336 ? 15.20600  -2.78000  52.16200  1.000 39.29155  ? 336 ASN B ND2   1 
ATOM   6151 N  N     . VAL B 1 337 ? 11.00800  -2.28500  53.83000  1.000 32.66707  ? 337 VAL B N     1 
ATOM   6152 C  CA    . VAL B 1 337 ? 9.58200   -2.43100  53.53500  1.000 32.68023  ? 337 VAL B CA    1 
ATOM   6153 C  C     . VAL B 1 337 ? 9.28400   -3.62000  52.63500  1.000 29.75094  ? 337 VAL B C     1 
ATOM   6154 O  O     . VAL B 1 337 ? 8.15800   -4.12900  52.64500  1.000 32.38809  ? 337 VAL B O     1 
ATOM   6155 C  CB    . VAL B 1 337 ? 8.99700   -1.13700  52.92600  1.000 35.01209  ? 337 VAL B CB    1 
ATOM   6156 C  CG1   . VAL B 1 337 ? 9.10200   0.01400   53.92200  1.000 36.47279  ? 337 VAL B CG1   1 
ATOM   6157 C  CG2   . VAL B 1 337 ? 9.66600   -0.79500  51.60300  1.000 41.39970  ? 337 VAL B CG2   1 
ATOM   6158 N  N     . TYR B 1 338 ? 10.25800  -4.08500  51.85100  1.000 29.39300  ? 338 TYR B N     1 
ATOM   6159 C  CA    . TYR B 1 338 ? 10.02100  -5.27100  51.03200  1.000 32.34072  ? 338 TYR B CA    1 
ATOM   6160 C  C     . TYR B 1 338 ? 10.03500  -6.53700  51.88300  1.000 31.57221  ? 338 TYR B C     1 
ATOM   6161 O  O     . TYR B 1 338 ? 9.29300   -7.49000  51.60600  1.000 32.00647  ? 338 TYR B O     1 
ATOM   6162 C  CB    . TYR B 1 338 ? 11.05200  -5.34100  49.90700  1.000 33.28294  ? 338 TYR B CB    1 
ATOM   6163 C  CG    . TYR B 1 338 ? 10.98600  -4.14100  48.98500  1.000 34.89629  ? 338 TYR B CG    1 
ATOM   6164 C  CD1   . TYR B 1 338 ? 9.82600   -3.85200  48.27300  1.000 34.05408  ? 338 TYR B CD1   1 
ATOM   6165 C  CD2   . TYR B 1 338 ? 12.07100  -3.28000  48.84700  1.000 42.08926  ? 338 TYR B CD2   1 
ATOM   6166 C  CE1   . TYR B 1 338 ? 9.75100   -2.74800  47.43600  1.000 44.79221  ? 338 TYR B CE1   1 
ATOM   6167 C  CE2   . TYR B 1 338 ? 12.00600  -2.17400  48.01400  1.000 47.21092  ? 338 TYR B CE2   1 
ATOM   6168 C  CZ    . TYR B 1 338 ? 10.84400  -1.91400  47.31200  1.000 43.11833  ? 338 TYR B CZ    1 
ATOM   6169 O  OH    . TYR B 1 338 ? 10.77600  -0.81800  46.47900  1.000 50.76135  ? 338 TYR B OH    1 
ATOM   6170 N  N     . MET B 1 339 ? 10.88700  -6.56900  52.91300  1.000 30.11940  ? 339 MET B N     1 
ATOM   6171 C  CA    . MET B 1 339 ? 10.81800  -7.62800  53.91800  1.000 34.28832  ? 339 MET B CA    1 
ATOM   6172 C  C     . MET B 1 339 ? 9.48500   -7.58700  54.65500  1.000 28.05600  ? 339 MET B C     1 
ATOM   6173 O  O     . MET B 1 339 ? 8.84000   -8.62300  54.85800  1.000 31.26691  ? 339 MET B O     1 
ATOM   6174 C  CB    . MET B 1 339 ? 11.98000  -7.48600  54.91000  1.000 32.19597  ? 339 MET B CB    1 
ATOM   6175 C  CG    . MET B 1 339 ? 13.35700  -7.79700  54.33600  1.000 46.18975  ? 339 MET B CG    1 
ATOM   6176 S  SD    . MET B 1 339 ? 13.65800  -9.56400  54.12200  1.000 48.62951  ? 339 MET B SD    1 
ATOM   6177 C  CE    . MET B 1 339 ? 13.75800  -10.10900 55.82300  1.000 47.92417  ? 339 MET B CE    1 
ATOM   6178 N  N     . LEU B 1 340 ? 9.06600   -6.38700  55.07600  1.000 28.81135  ? 340 LEU B N     1 
ATOM   6179 C  CA    . LEU B 1 340 ? 7.80700   -6.23600  55.80500  1.000 30.86423  ? 340 LEU B CA    1 
ATOM   6180 C  C     . LEU B 1 340 ? 6.61900   -6.68600  54.96700  1.000 25.00563  ? 340 LEU B C     1 
ATOM   6181 O  O     . LEU B 1 340 ? 5.64200   -7.22800  55.50200  1.000 27.86124  ? 340 LEU B O     1 
ATOM   6182 C  CB    . LEU B 1 340 ? 7.62400   -4.78000  56.23400  1.000 28.06915  ? 340 LEU B CB    1 
ATOM   6183 C  CG    . LEU B 1 340 ? 8.66500   -4.19900  57.19000  1.000 30.05097  ? 340 LEU B CG    1 
ATOM   6184 C  CD1   . LEU B 1 340 ? 8.38600   -2.72500  57.41900  1.000 29.45616  ? 340 LEU B CD1   1 
ATOM   6185 C  CD2   . LEU B 1 340 ? 8.66500   -4.96400  58.50600  1.000 32.42494  ? 340 LEU B CD2   1 
ATOM   6186 N  N     . HIS B 1 341 ? 6.67000   -6.44800  53.65300  1.000 29.76936  ? 341 HIS B N     1 
ATOM   6187 C  CA    . HIS B 1 341 ? 5.58400   -6.88200  52.77900  1.000 28.60343  ? 341 HIS B CA    1 
ATOM   6188 C  C     . HIS B 1 341 ? 5.38100   -8.39000  52.85700  1.000 29.54565  ? 341 HIS B C     1 
ATOM   6189 O  O     . HIS B 1 341 ? 4.26800   -8.86500  53.11200  1.000 24.59242  ? 341 HIS B O     1 
ATOM   6190 C  CB    . HIS B 1 341 ? 5.86000   -6.45900  51.33500  1.000 32.24334  ? 341 HIS B CB    1 
ATOM   6191 C  CG    . HIS B 1 341 ? 4.75800   -6.81600  50.39000  1.000 28.01652  ? 341 HIS B CG    1 
ATOM   6192 N  ND1   . HIS B 1 341 ? 3.78700   -5.91500  50.00500  1.000 32.87763  ? 341 HIS B ND1   1 
ATOM   6193 C  CD2   . HIS B 1 341 ? 4.45900   -7.98200  49.77100  1.000 27.82176  ? 341 HIS B CD2   1 
ATOM   6194 C  CE1   . HIS B 1 341 ? 2.94400   -6.50900  49.17800  1.000 35.24370  ? 341 HIS B CE1   1 
ATOM   6195 N  NE2   . HIS B 1 341 ? 3.32700   -7.76400  49.02100  1.000 35.13316  ? 341 HIS B NE2   1 
ATOM   6196 N  N     . MET B 1 342 ? 6.45000   -9.16100  52.63900  1.000 30.99582  ? 342 MET B N     1 
ATOM   6197 C  CA    . MET B 1 342 ? 6.33700   -10.61500 52.67800  1.000 32.19333  ? 342 MET B CA    1 
ATOM   6198 C  C     . MET B 1 342 ? 5.98100   -11.11800 54.07600  1.000 26.15577  ? 342 MET B C     1 
ATOM   6199 O  O     . MET B 1 342 ? 5.30400   -12.14500 54.20800  1.000 26.86901  ? 342 MET B O     1 
ATOM   6200 C  CB    . MET B 1 342 ? 7.64400   -11.25400 52.20200  1.000 32.35125  ? 342 MET B CB    1 
ATOM   6201 C  CG    . MET B 1 342 ? 8.04800   -10.86800 50.78200  1.000 33.73826  ? 342 MET B CG    1 
ATOM   6202 S  SD    . MET B 1 342 ? 6.73600   -11.12400 49.55800  1.000 45.66074  ? 342 MET B SD    1 
ATOM   6203 C  CE    . MET B 1 342 ? 6.44000   -12.88500 49.70900  1.000 49.04535  ? 342 MET B CE    1 
ATOM   6204 N  N     . MET B 1 343 ? 6.43900   -10.42600 55.12500  1.000 30.98003  ? 343 MET B N     1 
ATOM   6205 C  CA    . MET B 1 343 ? 6.02900   -10.77800 56.48500  1.000 28.68502  ? 343 MET B CA    1 
ATOM   6206 C  C     . MET B 1 343 ? 4.53000   -10.58000 56.67400  1.000 27.05061  ? 343 MET B C     1 
ATOM   6207 O  O     . MET B 1 343 ? 3.84900   -11.42400 57.27000  1.000 25.65834  ? 343 MET B O     1 
ATOM   6208 C  CB    . MET B 1 343 ? 6.80200   -9.93800  57.50300  1.000 28.03231  ? 343 MET B CB    1 
ATOM   6209 C  CG    . MET B 1 343 ? 8.26100   -10.33800 57.66900  1.000 40.31273  ? 343 MET B CG    1 
ATOM   6210 S  SD    . MET B 1 343 ? 9.14900   -9.24900  58.80700  1.000 49.26907  ? 343 MET B SD    1 
ATOM   6211 C  CE    . MET B 1 343 ? 10.84900  -9.55000  58.32600  1.000 79.55691  ? 343 MET B CE    1 
ATOM   6212 N  N     . TYR B 1 344 ? 4.00400   -9.45700  56.18100  1.000 22.48691  ? 344 TYR B N     1 
ATOM   6213 C  CA    . TYR B 1 344 ? 2.57400   -9.19400  56.27700  1.000 27.50330  ? 344 TYR B CA    1 
ATOM   6214 C  C     . TYR B 1 344 ? 1.77500   -10.21900 55.48000  1.000 24.94510  ? 344 TYR B C     1 
ATOM   6215 O  O     . TYR B 1 344 ? 0.73200   -10.69800 55.93800  1.000 25.46095  ? 344 TYR B O     1 
ATOM   6216 C  CB    . TYR B 1 344 ? 2.27700   -7.77300  55.79200  1.000 30.78264  ? 344 TYR B CB    1 
ATOM   6217 C  CG    . TYR B 1 344 ? 0.82800   -7.37600  55.91600  1.000 26.73215  ? 344 TYR B CG    1 
ATOM   6218 C  CD1   . TYR B 1 344 ? 0.32200   -6.88000  57.11000  1.000 32.82762  ? 344 TYR B CD1   1 
ATOM   6219 C  CD2   . TYR B 1 344 ? -0.04500  -7.53200  54.84600  1.000 35.11474  ? 344 TYR B CD2   1 
ATOM   6220 C  CE1   . TYR B 1 344 ? -1.00600  -6.52300  57.22700  1.000 32.16438  ? 344 TYR B CE1   1 
ATOM   6221 C  CE2   . TYR B 1 344 ? -1.37700  -7.18900  54.95700  1.000 36.48332  ? 344 TYR B CE2   1 
ATOM   6222 C  CZ    . TYR B 1 344 ? -1.85200  -6.68500  56.15000  1.000 32.36441  ? 344 TYR B CZ    1 
ATOM   6223 O  OH    . TYR B 1 344 ? -3.17800  -6.33800  56.26100  1.000 43.48942  ? 344 TYR B OH    1 
ATOM   6224 N  N     . GLN B 1 345 ? 2.23900   -10.56000 54.27700  1.000 27.80860  ? 345 GLN B N     1 
ATOM   6225 C  CA    . GLN B 1 345 ? 1.55900   -11.59400 53.50600  1.000 33.06449  ? 345 GLN B CA    1 
ATOM   6226 C  C     . GLN B 1 345 ? 1.60300   -12.93100 54.23100  1.000 30.10887  ? 345 GLN B C     1 
ATOM   6227 O  O     . GLN B 1 345 ? 0.58700   -13.63100 54.32200  1.000 27.07167  ? 345 GLN B O     1 
ATOM   6228 C  CB    . GLN B 1 345 ? 2.17900   -11.70800 52.11300  1.000 33.29347  ? 345 GLN B CB    1 
ATOM   6229 C  CG    . GLN B 1 345 ? 1.87100   -10.50800 51.23000  1.000 34.85681  ? 345 GLN B CG    1 
ATOM   6230 C  CD    . GLN B 1 345 ? 0.37600   -10.25600 51.11900  1.000 32.14859  ? 345 GLN B CD    1 
ATOM   6231 O  OE1   . GLN B 1 345 ? -0.41000  -11.18400 50.92800  1.000 36.82810  ? 345 GLN B OE1   1 
ATOM   6232 N  NE2   . GLN B 1 345 ? -0.02500  -9.00000  51.27000  1.000 34.71469  ? 345 GLN B NE2   1 
ATOM   6233 N  N     . ALA B 1 346 ? 2.77100   -13.29500 54.76800  1.000 25.08459  ? 346 ALA B N     1 
ATOM   6234 C  CA    . ALA B 1 346 ? 2.88500   -14.53300 55.53300  1.000 26.44791  ? 346 ALA B CA    1 
ATOM   6235 C  C     . ALA B 1 346 ? 1.94100   -14.53700 56.73000  1.000 25.95048  ? 346 ALA B C     1 
ATOM   6236 O  O     . ALA B 1 346 ? 1.34800   -15.57300 57.05700  1.000 29.00611  ? 346 ALA B O     1 
ATOM   6237 C  CB    . ALA B 1 346 ? 4.32900   -14.74300 55.98100  1.000 28.38235  ? 346 ALA B CB    1 
ATOM   6238 N  N     . MET B 1 347 ? 1.81500   -13.39400 57.41400  1.000 27.82176  ? 347 MET B N     1 
ATOM   6239 C  CA    . MET B 1 347 ? 0.88500   -13.28100 58.53800  1.000 27.23748  ? 347 MET B CA    1 
ATOM   6240 C  C     . MET B 1 347 ? -0.55000  -13.56300 58.10400  1.000 31.21690  ? 347 MET B C     1 
ATOM   6241 O  O     . MET B 1 347 ? -1.29100  -14.28200 58.78600  1.000 26.30579  ? 347 MET B O     1 
ATOM   6242 C  CB    . MET B 1 347 ? 0.99500   -11.88300 59.16500  1.000 25.36357  ? 347 MET B CB    1 
ATOM   6243 C  CG    . MET B 1 347 ? 0.23600   -11.70300 60.48000  1.000 27.30854  ? 347 MET B CG    1 
ATOM   6244 S  SD    . MET B 1 347 ? 0.32900   -10.00400 61.11000  1.000 27.33222  ? 347 MET B SD    1 
ATOM   6245 C  CE    . MET B 1 347 ? -0.51400  -10.13000 62.69600  1.000 28.26128  ? 347 MET B CE    1 
ATOM   6246 N  N     . GLY B 1 348 ? -0.96400  -12.98700 56.97200  1.000 24.96615  ? 348 GLY B N     1 
ATOM   6247 C  CA    . GLY B 1 348 ? -2.30800  -13.23700 56.46600  1.000 26.29263  ? 348 GLY B CA    1 
ATOM   6248 C  C     . GLY B 1 348 ? -2.59200  -14.71100 56.24400  1.000 24.77929  ? 348 GLY B C     1 
ATOM   6249 O  O     . GLY B 1 348 ? -3.66200  -15.21400 56.60200  1.000 26.60319  ? 348 GLY B O     1 
ATOM   6250 N  N     . VAL B 1 349 ? -1.63700  -15.42100 55.63400  1.000 25.78993  ? 349 VAL B N     1 
ATOM   6251 C  CA    . VAL B 1 349 ? -1.80400  -16.85400 55.39600  1.000 26.33474  ? 349 VAL B CA    1 
ATOM   6252 C  C     . VAL B 1 349 ? -1.94900  -17.60300 56.71800  1.000 28.48236  ? 349 VAL B C     1 
ATOM   6253 O  O     . VAL B 1 349 ? -2.79900  -18.49100 56.85400  1.000 27.29538  ? 349 VAL B O     1 
ATOM   6254 C  CB    . VAL B 1 349 ? -0.63300  -17.39700 54.55700  1.000 31.42745  ? 349 VAL B CB    1 
ATOM   6255 C  CG1   . VAL B 1 349 ? -0.76400  -18.90300 54.37200  1.000 33.25662  ? 349 VAL B CG1   1 
ATOM   6256 C  CG2   . VAL B 1 349 ? -0.58400  -16.69500 53.21100  1.000 33.02764  ? 349 VAL B CG2   1 
ATOM   6257 N  N     . CYS B 1 350 ? -1.11900  -17.26200 57.71100  1.000 26.27157  ? 350 CYS B N     1 
ATOM   6258 C  CA    . CYS B 1 350 ? -1.25100  -17.88900 59.02400  1.000 29.06138  ? 350 CYS B CA    1 
ATOM   6259 C  C     . CYS B 1 350 ? -2.62500  -17.61500 59.62600  1.000 29.24824  ? 350 CYS B C     1 
ATOM   6260 O  O     . CYS B 1 350 ? -3.25800  -18.51600 60.19000  1.000 29.92464  ? 350 CYS B O     1 
ATOM   6261 C  CB    . CYS B 1 350 ? -0.14600  -17.39200 59.95600  1.000 33.50139  ? 350 CYS B CB    1 
ATOM   6262 S  SG    . CYS B 1 350 ? 1.49400   -18.00500 59.53200  1.000 35.24896  ? 350 CYS B SG    1 
ATOM   6263 N  N     . LEU B 1 351 ? -3.10500  -16.37400 59.50600  1.000 25.22145  ? 351 LEU B N     1 
ATOM   6264 C  CA    . LEU B 1 351 ? -4.42200  -16.02700 60.03500  1.000 27.53225  ? 351 LEU B CA    1 
ATOM   6265 C  C     . LEU B 1 351 ? -5.52700  -16.84300 59.36900  1.000 28.09021  ? 351 LEU B C     1 
ATOM   6266 O  O     . LEU B 1 351 ? -6.43900  -17.33400 60.04600  1.000 34.25411  ? 351 LEU B O     1 
ATOM   6267 C  CB    . LEU B 1 351 ? -4.66900  -14.52500 59.86300  1.000 22.21582  ? 351 LEU B CB    1 
ATOM   6268 C  CG    . LEU B 1 351 ? -3.88400  -13.61200 60.82200  1.000 27.65595  ? 351 LEU B CG    1 
ATOM   6269 C  CD1   . LEU B 1 351 ? -4.10700  -12.14800 60.49000  1.000 27.63752  ? 351 LEU B CD1   1 
ATOM   6270 C  CD2   . LEU B 1 351 ? -4.27600  -13.88900 62.27200  1.000 25.88205  ? 351 LEU B CD2   1 
ATOM   6271 N  N     . TYR B 1 352 ? -5.46500  -17.01000 58.04500  1.000 27.19800  ? 352 TYR B N     1 
ATOM   6272 C  CA    . TYR B 1 352 ? -6.46200  -17.84900 57.38600  1.000 29.47722  ? 352 TYR B CA    1 
ATOM   6273 C  C     . TYR B 1 352 ? -6.33900  -19.30100 57.83700  1.000 29.09296  ? 352 TYR B C     1 
ATOM   6274 O  O     . TYR B 1 352 ? -7.35100  -19.97000 58.08500  1.000 29.44564  ? 352 TYR B O     1 
ATOM   6275 C  CB    . TYR B 1 352 ? -6.34100  -17.74300 55.86400  1.000 35.34634  ? 352 TYR B CB    1 
ATOM   6276 C  CG    . TYR B 1 352 ? -7.40400  -18.54600 55.15200  1.000 32.39073  ? 352 TYR B CG    1 
ATOM   6277 C  CD1   . TYR B 1 352 ? -8.74300  -18.17900 55.22900  1.000 37.05444  ? 352 TYR B CD1   1 
ATOM   6278 C  CD2   . TYR B 1 352 ? -7.07800  -19.68800 54.43200  1.000 40.48907  ? 352 TYR B CD2   1 
ATOM   6279 C  CE1   . TYR B 1 352 ? -9.72900  -18.92000 54.59400  1.000 41.55498  ? 352 TYR B CE1   1 
ATOM   6280 C  CE2   . TYR B 1 352 ? -8.05800  -20.43400 53.79000  1.000 44.82116  ? 352 TYR B CE2   1 
ATOM   6281 C  CZ    . TYR B 1 352 ? -9.37900  -20.04400 53.87700  1.000 45.94761  ? 352 TYR B CZ    1 
ATOM   6282 O  OH    . TYR B 1 352 ? -10.35500 -20.78200 53.24600  1.000 59.17552  ? 352 TYR B OH    1 
ATOM   6283 N  N     . MET B 1 353 ? -5.10500  -19.80300 57.96600  1.000 27.73490  ? 353 MET B N     1 
ATOM   6284 C  CA    . MET B 1 353 ? -4.88200  -21.15400 58.47100  1.000 34.45413  ? 353 MET B CA    1 
ATOM   6285 C  C     . MET B 1 353 ? -5.21300  -21.30100 59.94900  1.000 30.33522  ? 353 MET B C     1 
ATOM   6286 O  O     . MET B 1 353 ? -5.08300  -22.41100 60.47500  1.000 31.03530  ? 353 MET B O     1 
ATOM   6287 C  CB    . MET B 1 353 ? -3.43000  -21.58100 58.25300  1.000 36.10959  ? 353 MET B CB    1 
ATOM   6288 C  CG    . MET B 1 353 ? -3.03200  -21.73100 56.80900  1.000 39.40472  ? 353 MET B CG    1 
ATOM   6289 S  SD    . MET B 1 353 ? -1.26400  -22.05700 56.66000  1.000 41.75501  ? 353 MET B SD    1 
ATOM   6290 C  CE    . MET B 1 353 ? -1.21600  -23.80900 57.03000  1.000 46.35029  ? 353 MET B CE    1 
ATOM   6291 N  N     . GLN B 1 354 ? -5.57900  -20.21700 60.63600  1.000 29.65882  ? 354 GLN B N     1 
ATOM   6292 C  CA    . GLN B 1 354 ? -5.80700  -20.23800 62.08100  1.000 32.85131  ? 354 GLN B CA    1 
ATOM   6293 C  C     . GLN B 1 354 ? -4.57200  -20.72800 62.83400  1.000 33.91722  ? 354 GLN B C     1 
ATOM   6294 O  O     . GLN B 1 354 ? -4.67500  -21.41000 63.85800  1.000 41.58130  ? 354 GLN B O     1 
ATOM   6295 C  CB    . GLN B 1 354 ? -7.04300  -21.06800 62.43300  1.000 31.94857  ? 354 GLN B CB    1 
ATOM   6296 C  CG    . GLN B 1 354 ? -8.27600  -20.58600 61.69500  1.000 31.63274  ? 354 GLN B CG    1 
ATOM   6297 C  CD    . GLN B 1 354 ? -9.55500  -21.21100 62.19400  1.000 33.46191  ? 354 GLN B CD    1 
ATOM   6298 O  OE1   . GLN B 1 354 ? -9.54700  -22.02200 63.11500  1.000 40.77331  ? 354 GLN B OE1   1 
ATOM   6299 N  NE2   . GLN B 1 354 ? -10.67300 -20.82500 61.59000  1.000 36.44384  ? 354 GLN B NE2   1 
ATOM   6300 N  N     . ASP B 1 355 ? -3.39500  -20.39000 62.31000  1.000 38.63095  ? 355 ASP B N     1 
ATOM   6301 C  CA    . ASP B 1 355 ? -2.12100  -20.62200 62.98400  1.000 39.22839  ? 355 ASP B CA    1 
ATOM   6302 C  C     . ASP B 1 355 ? -1.80700  -19.35000 63.75800  1.000 35.29107  ? 355 ASP B C     1 
ATOM   6303 O  O     . ASP B 1 355 ? -1.09700  -18.46400 63.27900  1.000 32.84868  ? 355 ASP B O     1 
ATOM   6304 C  CB    . ASP B 1 355 ? -1.03400  -20.96300 61.97300  1.000 41.72079  ? 355 ASP B CB    1 
ATOM   6305 C  CG    . ASP B 1 355 ? 0.33500   -21.15400 62.61100  1.000 50.93769  ? 355 ASP B CG    1 
ATOM   6306 O  OD1   . ASP B 1 355 ? 0.43600   -21.16500 63.86000  1.000 43.50258  ? 355 ASP B OD1   1 
ATOM   6307 O  OD2   . ASP B 1 355 ? 1.31800   -21.28900 61.84800  1.000 42.03925  ? 355 ASP B OD2   1 
ATOM   6308 N  N     . TRP B 1 356 ? -2.34200  -19.26000 64.97800  1.000 38.35197  ? 356 TRP B N     1 
ATOM   6309 C  CA    . TRP B 1 356 ? -2.25200  -18.00900 65.72600  1.000 32.77498  ? 356 TRP B CA    1 
ATOM   6310 C  C     . TRP B 1 356 ? -0.82000  -17.73600 66.17300  1.000 30.37733  ? 356 TRP B C     1 
ATOM   6311 O  O     . TRP B 1 356 ? -0.35900  -16.58800 66.13900  1.000 30.52734  ? 356 TRP B O     1 
ATOM   6312 C  CB    . TRP B 1 356 ? -3.19700  -18.06100 66.92700  1.000 34.17778  ? 356 TRP B CB    1 
ATOM   6313 C  CG    . TRP B 1 356 ? -4.56900  -18.56300 66.57400  1.000 36.52017  ? 356 TRP B CG    1 
ATOM   6314 C  CD1   . TRP B 1 356 ? -5.20600  -19.63800 67.11800  1.000 38.91256  ? 356 TRP B CD1   1 
ATOM   6315 C  CD2   . TRP B 1 356 ? -5.47300  -18.01100 65.60200  1.000 38.50988  ? 356 TRP B CD2   1 
ATOM   6316 N  NE1   . TRP B 1 356 ? -6.44400  -19.79500 66.54600  1.000 40.68119  ? 356 TRP B NE1   1 
ATOM   6317 C  CE2   . TRP B 1 356 ? -6.63400  -18.81000 65.61300  1.000 39.08627  ? 356 TRP B CE2   1 
ATOM   6318 C  CE3   . TRP B 1 356 ? -5.41100  -16.92400 64.72500  1.000 35.08052  ? 356 TRP B CE3   1 
ATOM   6319 C  CZ2   . TRP B 1 356 ? -7.72600  -18.55600 64.78100  1.000 37.03602  ? 356 TRP B CZ2   1 
ATOM   6320 C  CZ3   . TRP B 1 356 ? -6.49500  -16.67300 63.90000  1.000 37.68873  ? 356 TRP B CZ3   1 
ATOM   6321 C  CH2   . TRP B 1 356 ? -7.63900  -17.48700 63.93400  1.000 33.99881  ? 356 TRP B CH2   1 
ATOM   6322 N  N     . GLU B 1 357 ? -0.09900  -18.78300 66.57200  1.000 30.22204  ? 357 GLU B N     1 
ATOM   6323 C  CA    . GLU B 1 357 ? 1.29600   -18.63200 66.97000  1.000 36.65176  ? 357 GLU B CA    1 
ATOM   6324 C  C     . GLU B 1 357 ? 2.13900   -18.09100 65.82100  1.000 32.08279  ? 357 GLU B C     1 
ATOM   6325 O  O     . GLU B 1 357 ? 2.90900   -17.14000 65.99200  1.000 33.98039  ? 357 GLU B O     1 
ATOM   6326 C  CB    . GLU B 1 357 ? 1.84100   -19.97600 67.45600  1.000 43.38152  ? 357 GLU B CB    1 
ATOM   6327 C  CG    . GLU B 1 357 ? 1.18700   -20.49200 68.72900  1.000 51.90096  ? 357 GLU B CG    1 
ATOM   6328 C  CD    . GLU B 1 357 ? 1.58400   -19.70200 69.96400  1.000 65.59471  ? 357 GLU B CD    1 
ATOM   6329 O  OE1   . GLU B 1 357 ? 2.51900   -18.87600 69.87600  1.000 70.91377  ? 357 GLU B OE1   1 
ATOM   6330 O  OE2   . GLU B 1 357 ? 0.96200   -19.91200 71.02700  1.000 108.70777 ? 357 GLU B OE2   1 
ATOM   6331 N  N     . GLY B 1 358 ? 2.00600   -18.69200 64.63800  1.000 33.77510  ? 358 GLY B N     1 
ATOM   6332 C  CA    . GLY B 1 358 ? 2.73100   -18.19300 63.48200  1.000 32.43284  ? 358 GLY B CA    1 
ATOM   6333 C  C     . GLY B 1 358 ? 2.40000   -16.74600 63.17900  1.000 29.90622  ? 358 GLY B C     1 
ATOM   6334 O  O     . GLY B 1 358 ? 3.29200   -15.92700 62.94900  1.000 32.49600  ? 358 GLY B O     1 
ATOM   6335 N  N     . ALA B 1 359 ? 1.10600   -16.41400 63.17300  1.000 25.37673  ? 359 ALA B N     1 
ATOM   6336 C  CA    . ALA B 1 359 ? 0.69000   -15.04700 62.88000  1.000 25.52148  ? 359 ALA B CA    1 
ATOM   6337 C  C     . ALA B 1 359 ? 1.25900   -14.05600 63.88700  1.000 22.83958  ? 359 ALA B C     1 
ATOM   6338 O  O     . ALA B 1 359 ? 1.64800   -12.94200 63.51800  1.000 23.39754  ? 359 ALA B O     1 
ATOM   6339 C  CB    . ALA B 1 359 ? -0.83500  -14.95500 62.86200  1.000 31.64590  ? 359 ALA B CB    1 
ATOM   6340 N  N     . LEU B 1 360 ? 1.28500   -14.43100 65.17100  1.000 25.82678  ? 360 LEU B N     1 
ATOM   6341 C  CA    . LEU B 1 360 ? 1.78400   -13.52400 66.20300  1.000 24.74770  ? 360 LEU B CA    1 
ATOM   6342 C  C     . LEU B 1 360 ? 3.25900   -13.20500 65.99200  1.000 24.44504  ? 360 LEU B C     1 
ATOM   6343 O  O     . LEU B 1 360 ? 3.67400   -12.04200 66.08200  1.000 26.57687  ? 360 LEU B O     1 
ATOM   6344 C  CB    . LEU B 1 360 ? 1.55700   -14.12600 67.59200  1.000 24.98984  ? 360 LEU B CB    1 
ATOM   6345 C  CG    . LEU B 1 360 ? 2.01000   -13.25400 68.76900  1.000 26.79795  ? 360 LEU B CG    1 
ATOM   6346 C  CD1   . LEU B 1 360 ? 1.23200   -11.95300 68.79500  1.000 26.66636  ? 360 LEU B CD1   1 
ATOM   6347 C  CD2   . LEU B 1 360 ? 1.88000   -13.99400 70.09200  1.000 32.41704  ? 360 LEU B CD2   1 
ATOM   6348 N  N     . GLN B 1 361 ? 4.06200   -14.22800 65.69900  1.000 31.65643  ? 361 GLN B N     1 
ATOM   6349 C  CA    . GLN B 1 361 ? 5.48800   -14.02900 65.46600  1.000 36.63860  ? 361 GLN B CA    1 
ATOM   6350 C  C     . GLN B 1 361 ? 5.72800   -12.99900 64.36800  1.000 34.02513  ? 361 GLN B C     1 
ATOM   6351 O  O     . GLN B 1 361 ? 6.58500   -12.11900 64.50300  1.000 34.43044  ? 361 GLN B O     1 
ATOM   6352 C  CB    . GLN B 1 361 ? 6.13300   -15.36700 65.10900  1.000 40.97860  ? 361 GLN B CB    1 
ATOM   6353 C  CG    . GLN B 1 361 ? 6.33000   -16.27900 66.30000  1.000 61.89426  ? 361 GLN B CG    1 
ATOM   6354 C  CD    . GLN B 1 361 ? 7.03500   -17.56700 65.93300  1.000 77.21978  ? 361 GLN B CD    1 
ATOM   6355 O  OE1   . GLN B 1 361 ? 8.00300   -17.56400 65.17100  1.000 75.12480  ? 361 GLN B OE1   1 
ATOM   6356 N  NE2   . GLN B 1 361 ? 6.54300   -18.68300 66.46300  1.000 79.00947  ? 361 GLN B NE2   1 
ATOM   6357 N  N     . TYR B 1 362 ? 4.97600   -13.09600 63.26700  1.000 31.02740  ? 362 TYR B N     1 
ATOM   6358 C  CA    . TYR B 1 362 ? 5.12200   -12.12300 62.18700  1.000 32.47495  ? 362 TYR B CA    1 
ATOM   6359 C  C     . TYR B 1 362 ? 4.66700   -10.73500 62.62400  1.000 26.28210  ? 362 TYR B C     1 
ATOM   6360 O  O     . TYR B 1 362 ? 5.33700   -9.73800  62.33800  1.000 22.59218  ? 362 TYR B O     1 
ATOM   6361 C  CB    . TYR B 1 362 ? 4.34200   -12.58800 60.95200  1.000 25.82415  ? 362 TYR B CB    1 
ATOM   6362 C  CG    . TYR B 1 362 ? 5.03600   -13.68300 60.16300  1.000 28.74818  ? 362 TYR B CG    1 
ATOM   6363 C  CD1   . TYR B 1 362 ? 6.26100   -13.45000 59.53600  1.000 29.16139  ? 362 TYR B CD1   1 
ATOM   6364 C  CD2   . TYR B 1 362 ? 4.47600   -14.95400 60.05100  1.000 31.90119  ? 362 TYR B CD2   1 
ATOM   6365 C  CE1   . TYR B 1 362 ? 6.90200   -14.45600 58.80900  1.000 30.11414  ? 362 TYR B CE1   1 
ATOM   6366 C  CE2   . TYR B 1 362 ? 5.11400   -15.96200 59.33500  1.000 36.84126  ? 362 TYR B CE2   1 
ATOM   6367 C  CZ    . TYR B 1 362 ? 6.32300   -15.70400 58.71800  1.000 36.31488  ? 362 TYR B CZ    1 
ATOM   6368 O  OH    . TYR B 1 362 ? 6.94500   -16.70100 58.00600  1.000 49.15326  ? 362 TYR B OH    1 
ATOM   6369 N  N     . GLY B 1 363 ? 3.52600   -10.64700 63.30900  1.000 36.99128  ? 363 GLY B N     1 
ATOM   6370 C  CA    . GLY B 1 363 ? 3.04800   -9.35200  63.76800  1.000 28.63764  ? 363 GLY B CA    1 
ATOM   6371 C  C     . GLY B 1 363 ? 4.04200   -8.63200  64.66100  1.000 27.92703  ? 363 GLY B C     1 
ATOM   6372 O  O     . GLY B 1 363 ? 4.24100   -7.42000  64.53200  1.000 24.91615  ? 363 GLY B O     1 
ATOM   6373 N  N     . GLN B 1 364 ? 4.67500   -9.36800  65.58000  1.000 22.90801  ? 364 GLN B N     1 
ATOM   6374 C  CA    . GLN B 1 364 ? 5.64900   -8.76200  66.48300  1.000 30.21152  ? 364 GLN B CA    1 
ATOM   6375 C  C     . GLN B 1 364 ? 6.84900   -8.19200  65.73500  1.000 30.44576  ? 364 GLN B C     1 
ATOM   6376 O  O     . GLN B 1 364 ? 7.44500   -7.20700  66.18300  1.000 38.95730  ? 364 GLN B O     1 
ATOM   6377 C  CB    . GLN B 1 364 ? 6.10400   -9.79000  67.51500  1.000 30.87475  ? 364 GLN B CB    1 
ATOM   6378 C  CG    . GLN B 1 364 ? 5.02300   -10.14300 68.52900  1.000 29.88253  ? 364 GLN B CG    1 
ATOM   6379 C  CD    . GLN B 1 364 ? 5.40700   -11.31900 69.38800  1.000 30.83001  ? 364 GLN B CD    1 
ATOM   6380 O  OE1   . GLN B 1 364 ? 6.15200   -12.20100 68.95600  1.000 38.70727  ? 364 GLN B OE1   1 
ATOM   6381 N  NE2   . GLN B 1 364 ? 4.92000   -11.33400 70.61900  1.000 28.55342  ? 364 GLN B NE2   1 
ATOM   6382 N  N     . LYS B 1 365 ? 7.22800   -8.79900  64.60900  1.000 41.22863  ? 365 LYS B N     1 
ATOM   6383 C  CA    . LYS B 1 365 ? 8.31600   -8.27000  63.79300  1.000 38.91782  ? 365 LYS B CA    1 
ATOM   6384 C  C     . LYS B 1 365 ? 7.89400   -7.08300  62.93100  1.000 32.84078  ? 365 LYS B C     1 
ATOM   6385 O  O     . LYS B 1 365 ? 8.75900   -6.33000  62.47000  1.000 35.06736  ? 365 LYS B O     1 
ATOM   6386 C  CB    . LYS B 1 365 ? 8.88400   -9.36800  62.89300  1.000 43.39994  ? 365 LYS B CB    1 
ATOM   6387 C  CG    . LYS B 1 365 ? 9.69800   -10.40500 63.62400  1.000 44.20004  ? 365 LYS B CG    1 
ATOM   6388 C  CD    . LYS B 1 365 ? 9.95500   -11.61800 62.75000  1.000 63.00755  ? 365 LYS B CD    1 
ATOM   6389 C  CE    . LYS B 1 365 ? 10.89100  -11.28400 61.59500  1.000 87.05781  ? 365 LYS B CE    1 
ATOM   6390 N  NZ    . LYS B 1 365 ? 12.31800  -11.19200 62.01800  1.000 87.96844  ? 365 LYS B NZ    1 
ATOM   6391 N  N     . ILE B 1 366 ? 6.59900   -6.90900  62.69000  1.000 29.48248  ? 366 ILE B N     1 
ATOM   6392 C  CA    . ILE B 1 366 ? 6.12200   -5.89000  61.75900  1.000 35.55689  ? 366 ILE B CA    1 
ATOM   6393 C  C     . ILE B 1 366 ? 5.83700   -4.56100  62.45200  1.000 29.85621  ? 366 ILE B C     1 
ATOM   6394 O  O     . ILE B 1 366 ? 6.06500   -3.49400  61.87500  1.000 35.21475  ? 366 ILE B O     1 
ATOM   6395 C  CB    . ILE B 1 366 ? 4.87000   -6.41700  61.03300  1.000 34.83049  ? 366 ILE B CB    1 
ATOM   6396 C  CG1   . ILE B 1 366 ? 5.24500   -7.56100  60.09300  1.000 28.67449  ? 366 ILE B CG1   1 
ATOM   6397 C  CG2   . ILE B 1 366 ? 4.16200   -5.29500  60.29400  1.000 33.08555  ? 366 ILE B CG2   1 
ATOM   6398 C  CD1   . ILE B 1 366 ? 4.04500   -8.33900  59.61000  1.000 35.92010  ? 366 ILE B CD1   1 
ATOM   6399 N  N     . ILE B 1 367 ? 5.35000   -4.60100  63.69400  1.000 30.10098  ? 367 ILE B N     1 
ATOM   6400 C  CA    . ILE B 1 367 ? 4.66500   -3.44400  64.25900  1.000 29.46406  ? 367 ILE B CA    1 
ATOM   6401 C  C     . ILE B 1 367 ? 5.61000   -2.25300  64.43500  1.000 26.16893  ? 367 ILE B C     1 
ATOM   6402 O  O     . ILE B 1 367 ? 5.25100   -1.11800  64.10800  1.000 33.59877  ? 367 ILE B O     1 
ATOM   6403 C  CB    . ILE B 1 367 ? 3.95600   -3.83000  65.57400  1.000 32.53548  ? 367 ILE B CB    1 
ATOM   6404 C  CG1   . ILE B 1 367 ? 3.20300   -2.62200  66.13500  1.000 29.14297  ? 367 ILE B CG1   1 
ATOM   6405 C  CG2   . ILE B 1 367 ? 4.93500   -4.40200  66.59800  1.000 29.82989  ? 367 ILE B CG2   1 
ATOM   6406 C  CD1   . ILE B 1 367 ? 2.20400   -2.03700  65.15400  1.000 30.62999  ? 367 ILE B CD1   1 
ATOM   6407 N  N     . LYS B 1 368 ? 6.82400   -2.48300  64.94800  1.000 28.55342  ? 368 LYS B N     1 
ATOM   6408 C  CA    . LYS B 1 368 ? 7.71100   -1.33400  65.18700  1.000 37.80980  ? 368 LYS B CA    1 
ATOM   6409 C  C     . LYS B 1 368 ? 8.14100   -0.67500  63.89200  1.000 27.18221  ? 368 LYS B C     1 
ATOM   6410 O  O     . LYS B 1 368 ? 8.03000   0.56900   63.79300  1.000 25.38725  ? 368 LYS B O     1 
ATOM   6411 C  CB    . LYS B 1 368 ? 8.90900   -1.76600  66.04100  1.000 34.39360  ? 368 LYS B CB    1 
ATOM   6412 C  CG    . LYS B 1 368 ? 9.64800   -0.60200  66.69800  1.000 60.58095  ? 368 LYS B CG    1 
ATOM   6413 C  CD    . LYS B 1 368 ? 10.87900  -1.07300  67.46600  1.000 68.88194  ? 368 LYS B CD    1 
ATOM   6414 C  CE    . LYS B 1 368 ? 10.50800  -1.96900  68.63600  1.000 93.02168  ? 368 LYS B CE    1 
ATOM   6415 N  NZ    . LYS B 1 368 ? 9.74300   -1.23600  69.68100  1.000 105.50476 ? 368 LYS B NZ    1 
ATOM   6416 N  N     . PRO B 1 369 ? 8.61600   -1.38200  62.85600  1.000 32.18544  ? 369 PRO B N     1 
ATOM   6417 C  CA    . PRO B 1 369 ? 8.87300   -0.71400  61.56800  1.000 30.28784  ? 369 PRO B CA    1 
ATOM   6418 C  C     . PRO B 1 369 ? 7.65500   -0.01000  60.98600  1.000 29.86411  ? 369 PRO B C     1 
ATOM   6419 O  O     . PRO B 1 369 ? 7.79200   1.05400   60.36900  1.000 26.66372  ? 369 PRO B O     1 
ATOM   6420 C  CB    . PRO B 1 369 ? 9.34900   -1.86100  60.66900  1.000 36.86495  ? 369 PRO B CB    1 
ATOM   6421 C  CG    . PRO B 1 369 ? 9.93300   -2.85200  61.60500  1.000 33.40401  ? 369 PRO B CG    1 
ATOM   6422 C  CD    . PRO B 1 369 ? 9.05700   -2.79500  62.82600  1.000 34.39886  ? 369 PRO B CD    1 
ATOM   6423 N  N     . TYR B 1 370 ? 6.46500   -0.59700  61.13600  1.000 33.45401  ? 370 TYR B N     1 
ATOM   6424 C  CA    . TYR B 1 370 ? 5.24100   0.06500   60.69300  1.000 33.63824  ? 370 TYR B CA    1 
ATOM   6425 C  C     . TYR B 1 370 ? 5.08800   1.43900   61.32700  1.000 36.19118  ? 370 TYR B C     1 
ATOM   6426 O  O     . TYR B 1 370 ? 4.69800   2.40300   60.65800  1.000 32.21176  ? 370 TYR B O     1 
ATOM   6427 C  CB    . TYR B 1 370 ? 4.02800   -0.79700  61.03600  1.000 33.00922  ? 370 TYR B CB    1 
ATOM   6428 C  CG    . TYR B 1 370 ? 3.48800   -1.63300  59.90500  1.000 27.62436  ? 370 TYR B CG    1 
ATOM   6429 C  CD1   . TYR B 1 370 ? 4.30000   -2.05100  58.86000  1.000 29.05085  ? 370 TYR B CD1   1 
ATOM   6430 C  CD2   . TYR B 1 370 ? 2.15100   -2.00400  59.88900  1.000 27.36644  ? 370 TYR B CD2   1 
ATOM   6431 C  CE1   . TYR B 1 370 ? 3.78600   -2.81400  57.82300  1.000 29.73251  ? 370 TYR B CE1   1 
ATOM   6432 C  CE2   . TYR B 1 370 ? 1.63500   -2.76100  58.87400  1.000 40.01269  ? 370 TYR B CE2   1 
ATOM   6433 C  CZ    . TYR B 1 370 ? 2.44900   -3.16800  57.84400  1.000 31.56168  ? 370 TYR B CZ    1 
ATOM   6434 O  OH    . TYR B 1 370 ? 1.90100   -3.93100  56.83800  1.000 37.30710  ? 370 TYR B OH    1 
ATOM   6435 N  N     . SER B 1 371 ? 5.36500   1.53500   62.62900  1.000 30.30627  ? 371 SER B N     1 
ATOM   6436 C  CA    . SER B 1 371 ? 5.14800   2.77700   63.36300  1.000 38.43882  ? 371 SER B CA    1 
ATOM   6437 C  C     . SER B 1 371 ? 5.94300   3.93700   62.77300  1.000 38.15457  ? 371 SER B C     1 
ATOM   6438 O  O     . SER B 1 371 ? 5.46600   5.07800   62.76300  1.000 43.29203  ? 371 SER B O     1 
ATOM   6439 C  CB    . SER B 1 371 ? 5.51400   2.57800   64.83300  1.000 42.30770  ? 371 SER B CB    1 
ATOM   6440 O  OG    . SER B 1 371 ? 4.68800   1.58900   65.42300  1.000 54.52233  ? 371 SER B OG    1 
ATOM   6441 N  N     . LYS B 1 372 ? 7.16300   3.67900   62.29700  1.000 30.83001  ? 372 LYS B N     1 
ATOM   6442 C  CA    . LYS B 1 372 ? 7.98200   4.76900   61.78100  1.000 28.15864  ? 372 LYS B CA    1 
ATOM   6443 C  C     . LYS B 1 372 ? 7.78800   5.02200   60.28800  1.000 26.53213  ? 372 LYS B C     1 
ATOM   6444 O  O     . LYS B 1 372 ? 7.95800   6.15800   59.83400  1.000 33.54876  ? 372 LYS B O     1 
ATOM   6445 C  CB    . LYS B 1 372 ? 9.46500   4.51000   62.07400  1.000 37.33079  ? 372 LYS B CB    1 
ATOM   6446 C  CG    . LYS B 1 372 ? 10.08600  3.36600   61.30200  1.000 44.78695  ? 372 LYS B CG    1 
ATOM   6447 C  CD    . LYS B 1 372 ? 11.60100  3.38900   61.44100  1.000 39.91794  ? 372 LYS B CD    1 
ATOM   6448 C  CE    . LYS B 1 372 ? 12.22400  2.14100   60.84800  1.000 56.20937  ? 372 LYS B CE    1 
ATOM   6449 N  NZ    . LYS B 1 372 ? 13.68800  2.05500   61.11100  1.000 56.58836  ? 372 LYS B NZ    1 
ATOM   6450 N  N     . HIS B 1 373 ? 7.45700   3.99800   59.50700  1.000 23.91339  ? 373 HIS B N     1 
ATOM   6451 C  CA    . HIS B 1 373 ? 7.29600   4.20000   58.07000  1.000 26.45844  ? 373 HIS B CA    1 
ATOM   6452 C  C     . HIS B 1 373 ? 5.97500   4.89100   57.74500  1.000 27.98757  ? 373 HIS B C     1 
ATOM   6453 O  O     . HIS B 1 373 ? 5.90800   5.69600   56.81000  1.000 36.37541  ? 373 HIS B O     1 
ATOM   6454 C  CB    . HIS B 1 373 ? 7.40500   2.86000   57.33900  1.000 23.18436  ? 373 HIS B CB    1 
ATOM   6455 C  CG    . HIS B 1 373 ? 8.79000   2.28500   57.34300  1.000 27.00850  ? 373 HIS B CG    1 
ATOM   6456 N  ND1   . HIS B 1 373 ? 9.92200   3.07300   57.33900  1.000 29.51407  ? 373 HIS B ND1   1 
ATOM   6457 C  CD2   . HIS B 1 373 ? 9.22700   1.00200   57.36000  1.000 24.93457  ? 373 HIS B CD2   1 
ATOM   6458 C  CE1   . HIS B 1 373 ? 10.99500  2.30300   57.33600  1.000 29.64566  ? 373 HIS B CE1   1 
ATOM   6459 N  NE2   . HIS B 1 373 ? 10.60200  1.04200   57.34700  1.000 31.77749  ? 373 HIS B NE2   1 
ATOM   6460 N  N     . TYR B 1 374 ? 4.91500   4.57000   58.49300  1.000 29.45880  ? 374 TYR B N     1 
ATOM   6461 C  CA    . TYR B 1 374 ? 3.59500   5.14500   58.28900  1.000 27.39539  ? 374 TYR B CA    1 
ATOM   6462 C  C     . TYR B 1 374 ? 3.44600   6.48100   59.01700  1.000 23.13698  ? 374 TYR B C     1 
ATOM   6463 O  O     . TYR B 1 374 ? 4.15700   6.74900   59.98700  1.000 32.66444  ? 374 TYR B O     1 
ATOM   6464 C  CB    . TYR B 1 374 ? 2.52100   4.17800   58.78300  1.000 22.26320  ? 374 TYR B CB    1 
ATOM   6465 C  CG    . TYR B 1 374 ? 2.20100   3.03900   57.84100  1.000 21.82893  ? 374 TYR B CG    1 
ATOM   6466 C  CD1   . TYR B 1 374 ? 1.55000   3.28100   56.63100  1.000 23.66073  ? 374 TYR B CD1   1 
ATOM   6467 C  CD2   . TYR B 1 374 ? 2.49400   1.71800   58.17700  1.000 25.50569  ? 374 TYR B CD2   1 
ATOM   6468 C  CE1   . TYR B 1 374 ? 1.23300   2.24700   55.76700  1.000 22.10002  ? 374 TYR B CE1   1 
ATOM   6469 C  CE2   . TYR B 1 374 ? 2.17700   0.67200   57.31500  1.000 24.15553  ? 374 TYR B CE2   1 
ATOM   6470 C  CZ    . TYR B 1 374 ? 1.54800   0.94600   56.11000  1.000 26.23209  ? 374 TYR B CZ    1 
ATOM   6471 O  OH    . TYR B 1 374 ? 1.21700   -0.07100  55.23900  1.000 21.70523  ? 374 TYR B OH    1 
ATOM   6472 N  N     . PRO B 1 375 ? 2.50200   7.32300   58.58500  1.000 35.11474  ? 375 PRO B N     1 
ATOM   6473 C  CA    . PRO B 1 375 ? 2.20100   8.56100   59.32200  1.000 30.19573  ? 375 PRO B CA    1 
ATOM   6474 C  C     . PRO B 1 375 ? 1.65600   8.28000   60.71800  1.000 37.07813  ? 375 PRO B C     1 
ATOM   6475 O  O     . PRO B 1 375 ? 1.33100   7.15100   61.08900  1.000 30.45102  ? 375 PRO B O     1 
ATOM   6476 C  CB    . PRO B 1 375 ? 1.14900   9.25600   58.45000  1.000 31.53536  ? 375 PRO B CB    1 
ATOM   6477 C  CG    . PRO B 1 375 ? 1.32100   8.65000   57.08500  1.000 39.43894  ? 375 PRO B CG    1 
ATOM   6478 C  CD    . PRO B 1 375 ? 1.75000   7.23900   57.31800  1.000 33.67772  ? 375 PRO B CD    1 
ATOM   6479 N  N     . LEU B 1 376 ? 1.54300   9.36100   61.49300  1.000 28.29550  ? 376 LEU B N     1 
ATOM   6480 C  CA    . LEU B 1 376 ? 1.26100   9.26200   62.92400  1.000 35.59111  ? 376 LEU B CA    1 
ATOM   6481 C  C     . LEU B 1 376 ? -0.04300  8.50800   63.21100  1.000 37.26763  ? 376 LEU B C     1 
ATOM   6482 O  O     . LEU B 1 376 ? -0.08400  7.63800   64.08900  1.000 58.50965  ? 376 LEU B O     1 
ATOM   6483 C  CB    . LEU B 1 376 ? 1.24300   10.66900  63.53100  1.000 37.95192  ? 376 LEU B CB    1 
ATOM   6484 C  CG    . LEU B 1 376 ? 1.61400   10.86600  65.01100  1.000 53.69328  ? 376 LEU B CG    1 
ATOM   6485 C  CD1   . LEU B 1 376 ? 1.50000   12.34100  65.38300  1.000 44.64219  ? 376 LEU B CD1   1 
ATOM   6486 C  CD2   . LEU B 1 376 ? 0.81900   9.99600   65.98100  1.000 54.60392  ? 376 LEU B CD2   1 
ATOM   6487 N  N     . TYR B 1 377 ? -1.12400  8.82800   62.49200  1.000 35.22791  ? 377 TYR B N     1 
ATOM   6488 C  CA    . TYR B 1 377 ? -2.40700  8.19800   62.80900  1.000 32.89868  ? 377 TYR B CA    1 
ATOM   6489 C  C     . TYR B 1 377 ? -2.88100  7.24200   61.72000  1.000 38.39145  ? 377 TYR B C     1 
ATOM   6490 O  O     . TYR B 1 377 ? -4.03000  7.32500   61.27900  1.000 58.86758  ? 377 TYR B O     1 
ATOM   6491 C  CB    . TYR B 1 377 ? -3.48700  9.26100   63.03800  1.000 35.25949  ? 377 TYR B CB    1 
ATOM   6492 C  CG    . TYR B 1 377 ? -3.22400  10.16700  64.21400  1.000 26.10576  ? 377 TYR B CG    1 
ATOM   6493 C  CD1   . TYR B 1 377 ? -3.36100  9.70600   65.51600  1.000 36.73335  ? 377 TYR B CD1   1 
ATOM   6494 C  CD2   . TYR B 1 377 ? -2.83500  11.48400  64.02000  1.000 28.06126  ? 377 TYR B CD2   1 
ATOM   6495 C  CE1   . TYR B 1 377 ? -3.11200  10.53000  66.59200  1.000 31.49851  ? 377 TYR B CE1   1 
ATOM   6496 C  CE2   . TYR B 1 377 ? -2.58100  12.31800  65.09200  1.000 30.74053  ? 377 TYR B CE2   1 
ATOM   6497 C  CZ    . TYR B 1 377 ? -2.72000  11.83600  66.37600  1.000 33.21977  ? 377 TYR B CZ    1 
ATOM   6498 O  OH    . TYR B 1 377 ? -2.47400  12.66000  67.44800  1.000 43.06569  ? 377 TYR B OH    1 
ATOM   6499 N  N     . SER B 1 378 ? -2.04500  6.27900   61.34800  1.000 34.53309  ? 378 SER B N     1 
ATOM   6500 C  CA    . SER B 1 378 ? -2.32800  5.42200   60.20400  1.000 29.50880  ? 378 SER B CA    1 
ATOM   6501 C  C     . SER B 1 378 ? -3.27500  4.29300   60.57600  1.000 27.77175  ? 378 SER B C     1 
ATOM   6502 O  O     . SER B 1 378 ? -3.14500  3.68200   61.63800  1.000 28.99032  ? 378 SER B O     1 
ATOM   6503 C  CB    . SER B 1 378 ? -1.03200  4.83000   59.65400  1.000 31.58800  ? 378 SER B CB    1 
ATOM   6504 O  OG    . SER B 1 378 ? -1.31500  3.85800   58.66600  1.000 27.90861  ? 378 SER B OG    1 
ATOM   6505 N  N     . LEU B 1 379 ? -4.23900  4.02200   59.68900  1.000 20.63405  ? 379 LEU B N     1 
ATOM   6506 C  CA    . LEU B 1 379 ? -5.10600  2.86200   59.87200  1.000 21.84999  ? 379 LEU B CA    1 
ATOM   6507 C  C     . LEU B 1 379 ? -4.34000  1.55200   59.71800  1.000 20.71827  ? 379 LEU B C     1 
ATOM   6508 O  O     . LEU B 1 379 ? -4.72700  0.53900   60.31000  1.000 24.19764  ? 379 LEU B O     1 
ATOM   6509 C  CB    . LEU B 1 379 ? -6.27400  2.90200   58.88400  1.000 28.48236  ? 379 LEU B CB    1 
ATOM   6510 C  CG    . LEU B 1 379 ? -7.29800  4.02900   59.02600  1.000 29.90095  ? 379 LEU B CG    1 
ATOM   6511 C  CD1   . LEU B 1 379 ? -8.41100  3.85600   57.99900  1.000 42.48930  ? 379 LEU B CD1   1 
ATOM   6512 C  CD2   . LEU B 1 379 ? -7.86000  4.05500   60.43000  1.000 33.49612  ? 379 LEU B CD2   1 
ATOM   6513 N  N     . ASN B 1 380 ? -3.27200  1.54500   58.91600  1.000 22.56850  ? 380 ASN B N     1 
ATOM   6514 C  CA    . ASN B 1 380 ? -2.44100  0.35100   58.79300  1.000 19.68920  ? 380 ASN B CA    1 
ATOM   6515 C  C     . ASN B 1 380 ? -1.76000  0.01900   60.11700  1.000 20.56826  ? 380 ASN B C     1 
ATOM   6516 O  O     . ASN B 1 380 ? -1.58300  -1.15500  60.45500  1.000 21.78945  ? 380 ASN B O     1 
ATOM   6517 C  CB    . ASN B 1 380 ? -1.39200  0.56900   57.70000  1.000 25.03195  ? 380 ASN B CB    1 
ATOM   6518 C  CG    . ASN B 1 380 ? -2.01500  0.90000   56.35500  1.000 32.87236  ? 380 ASN B CG    1 
ATOM   6519 O  OD1   . ASN B 1 380 ? -2.23500  2.06900   56.04800  1.000 38.59936  ? 380 ASN B OD1   1 
ATOM   6520 N  ND2   . ASN B 1 380 ? -2.29900  -0.12000  55.54900  1.000 25.04248  ? 380 ASN B ND2   1 
ATOM   6521 N  N     . VAL B 1 381 ? -1.32700  1.04100   60.85500  1.000 23.82391  ? 381 VAL B N     1 
ATOM   6522 C  CA    . VAL B 1 381 ? -0.70000  0.81600   62.15400  1.000 21.41573  ? 381 VAL B CA    1 
ATOM   6523 C  C     . VAL B 1 381 ? -1.74000  0.39500   63.18500  1.000 23.33438  ? 381 VAL B C     1 
ATOM   6524 O  O     . VAL B 1 381 ? -1.53800  -0.57000  63.93500  1.000 23.46860  ? 381 VAL B O     1 
ATOM   6525 C  CB    . VAL B 1 381 ? 0.06300   2.07400   62.60300  1.000 22.79484  ? 381 VAL B CB    1 
ATOM   6526 C  CG1   . VAL B 1 381 ? 0.62600   1.89000   64.01300  1.000 26.93218  ? 381 VAL B CG1   1 
ATOM   6527 C  CG2   . VAL B 1 381 ? 1.18500   2.38300   61.62300  1.000 29.75620  ? 381 VAL B CG2   1 
ATOM   6528 N  N     . ALA B 1 382 ? -2.85900  1.12500   63.25400  1.000 21.76840  ? 382 ALA B N     1 
ATOM   6529 C  CA    . ALA B 1 382 ? -3.91900  0.78300   64.19900  1.000 25.97417  ? 382 ALA B CA    1 
ATOM   6530 C  C     . ALA B 1 382 ? -4.39500  -0.65200  64.00300  1.000 21.84999  ? 382 ALA B C     1 
ATOM   6531 O  O     . ALA B 1 382 ? -4.53000  -1.40700  64.97100  1.000 21.06832  ? 382 ALA B O     1 
ATOM   6532 C  CB    . ALA B 1 382 ? -5.08800  1.76300   64.06500  1.000 25.36883  ? 382 ALA B CB    1 
ATOM   6533 N  N     . SER B 1 383 ? -4.65800  -1.05000  62.75000  1.000 17.87320  ? 383 SER B N     1 
ATOM   6534 C  CA    . SER B 1 383 ? -5.15800  -2.40200  62.51800  1.000 22.04475  ? 383 SER B CA    1 
ATOM   6535 C  C     . SER B 1 383 ? -4.12000  -3.45800  62.88400  1.000 19.36548  ? 383 SER B C     1 
ATOM   6536 O  O     . SER B 1 383 ? -4.48500  -4.55300  63.32600  1.000 22.59481  ? 383 SER B O     1 
ATOM   6537 C  CB    . SER B 1 383 ? -5.60100  -2.57200  61.06400  1.000 26.17945  ? 383 SER B CB    1 
ATOM   6538 O  OG    . SER B 1 383 ? -4.52700  -2.34100  60.17300  1.000 47.23461  ? 383 SER B OG    1 
ATOM   6539 N  N     . MET B 1 384 ? -2.83100  -3.15500  62.71400  1.000 21.84999  ? 384 MET B N     1 
ATOM   6540 C  CA    . MET B 1 384 ? -1.78800  -4.08800  63.13500  1.000 25.05564  ? 384 MET B CA    1 
ATOM   6541 C  C     . MET B 1 384 ? -1.74900  -4.24200  64.65000  1.000 23.81865  ? 384 MET B C     1 
ATOM   6542 O  O     . MET B 1 384 ? -1.60300  -5.36000  65.15800  1.000 24.20553  ? 384 MET B O     1 
ATOM   6543 C  CB    . MET B 1 384 ? -0.42900  -3.63300  62.60700  1.000 25.60307  ? 384 MET B CB    1 
ATOM   6544 C  CG    . MET B 1 384 ? 0.71300   -4.60000  62.89000  1.000 26.68741  ? 384 MET B CG    1 
ATOM   6545 S  SD    . MET B 1 384 ? 0.39600   -6.28900  62.34100  1.000 32.80657  ? 384 MET B SD    1 
ATOM   6546 C  CE    . MET B 1 384 ? 0.14600   -6.02800  60.58600  1.000 34.43571  ? 384 MET B CE    1 
ATOM   6547 N  N     . TRP B 1 385 ? -1.85700  -3.13600  65.39400  1.000 25.15565  ? 385 TRP B N     1 
ATOM   6548 C  CA    . TRP B 1 385 ? -1.98400  -3.24900  66.84700  1.000 23.96866  ? 385 TRP B CA    1 
ATOM   6549 C  C     . TRP B 1 385 ? -3.20500  -4.07600  67.22900  1.000 28.66659  ? 385 TRP B C     1 
ATOM   6550 O  O     . TRP B 1 385 ? -3.17700  -4.83400  68.20800  1.000 23.15278  ? 385 TRP B O     1 
ATOM   6551 C  CB    . TRP B 1 385 ? -2.09100  -1.86900  67.49400  1.000 25.63465  ? 385 TRP B CB    1 
ATOM   6552 C  CG    . TRP B 1 385 ? -0.80700  -1.12900  67.68600  1.000 24.16342  ? 385 TRP B CG    1 
ATOM   6553 C  CD1   . TRP B 1 385 ? -0.50300  0.11200   67.20200  1.000 23.64757  ? 385 TRP B CD1   1 
ATOM   6554 C  CD2   . TRP B 1 385 ? 0.33900   -1.55900  68.43900  1.000 24.42135  ? 385 TRP B CD2   1 
ATOM   6555 N  NE1   . TRP B 1 385 ? 0.76200   0.47700   67.59700  1.000 26.01365  ? 385 TRP B NE1   1 
ATOM   6556 C  CE2   . TRP B 1 385 ? 1.30000   -0.53000  68.35600  1.000 24.55558  ? 385 TRP B CE2   1 
ATOM   6557 C  CE3   . TRP B 1 385 ? 0.64600   -2.71400  69.17000  1.000 28.42972  ? 385 TRP B CE3   1 
ATOM   6558 C  CZ2   . TRP B 1 385 ? 2.54700   -0.62000  68.97400  1.000 28.92452  ? 385 TRP B CZ2   1 
ATOM   6559 C  CZ3   . TRP B 1 385 ? 1.89200   -2.80300  69.78200  1.000 32.12490  ? 385 TRP B CZ3   1 
ATOM   6560 C  CH2   . TRP B 1 385 ? 2.82600   -1.76000  69.67800  1.000 30.47207  ? 385 TRP B CH2   1 
ATOM   6561 N  N     . LEU B 1 386 ? -4.29900  -3.92200  66.48000  1.000 23.84760  ? 386 LEU B N     1 
ATOM   6562 C  CA    . LEU B 1 386 ? -5.53100  -4.63900  66.79600  1.000 24.00025  ? 386 LEU B CA    1 
ATOM   6563 C  C     . LEU B 1 386 ? -5.37000  -6.13800  66.57300  1.000 23.59493  ? 386 LEU B C     1 
ATOM   6564 O  O     . LEU B 1 386 ? -5.77000  -6.94700  67.42100  1.000 22.63956  ? 386 LEU B O     1 
ATOM   6565 C  CB    . LEU B 1 386 ? -6.67900  -4.07800  65.95700  1.000 27.53225  ? 386 LEU B CB    1 
ATOM   6566 C  CG    . LEU B 1 386 ? -8.06900  -4.68900  66.13600  1.000 27.97704  ? 386 LEU B CG    1 
ATOM   6567 C  CD1   . LEU B 1 386 ? -8.45100  -4.80900  67.60400  1.000 29.91148  ? 386 LEU B CD1   1 
ATOM   6568 C  CD2   . LEU B 1 386 ? -9.07300  -3.82100  65.40800  1.000 30.90897  ? 386 LEU B CD2   1 
ATOM   6569 N  N     . LYS B 1 387 ? -4.79200  -6.52800  65.43100  1.000 20.93935  ? 387 LYS B N     1 
ATOM   6570 C  CA    . LYS B 1 387 ? -4.50200  -7.93900  65.17500  1.000 21.78156  ? 387 LYS B CA    1 
ATOM   6571 C  C     . LYS B 1 387 ? -3.60900  -8.52400  66.26200  1.000 20.74986  ? 387 LYS B C     1 
ATOM   6572 O  O     . LYS B 1 387 ? -3.84800  -9.63500  66.75200  1.000 22.89222  ? 387 LYS B O     1 
ATOM   6573 C  CB    . LYS B 1 387 ? -3.84100  -8.09700  63.80700  1.000 22.62903  ? 387 LYS B CB    1 
ATOM   6574 C  CG    . LYS B 1 387 ? -4.78600  -7.92000  62.64200  1.000 26.02680  ? 387 LYS B CG    1 
ATOM   6575 C  CD    . LYS B 1 387 ? -4.02800  -8.04500  61.33900  1.000 28.04020  ? 387 LYS B CD    1 
ATOM   6576 C  CE    . LYS B 1 387 ? -4.82500  -7.47700  60.19400  1.000 38.52830  ? 387 LYS B CE    1 
ATOM   6577 N  NZ    . LYS B 1 387 ? -4.05500  -7.56200  58.92700  1.000 46.76087  ? 387 LYS B NZ    1 
ATOM   6578 N  N     . LEU B 1 388 ? -2.54700  -7.80200  66.62800  1.000 27.62436  ? 388 LEU B N     1 
ATOM   6579 C  CA    . LEU B 1 388 ? -1.68000  -8.24900  67.71600  1.000 29.30088  ? 388 LEU B CA    1 
ATOM   6580 C  C     . LEU B 1 388 ? -2.46700  -8.45800  69.00200  1.000 29.36668  ? 388 LEU B C     1 
ATOM   6581 O  O     . LEU B 1 388 ? -2.33100  -9.49200  69.66700  1.000 35.62006  ? 388 LEU B O     1 
ATOM   6582 C  CB    . LEU B 1 388 ? -0.55800  -7.24300  67.94900  1.000 28.63501  ? 388 LEU B CB    1 
ATOM   6583 C  CG    . LEU B 1 388 ? 0.64300   -7.34400  67.02200  1.000 33.04870  ? 388 LEU B CG    1 
ATOM   6584 C  CD1   . LEU B 1 388 ? 1.59700   -6.20200  67.31700  1.000 43.05516  ? 388 LEU B CD1   1 
ATOM   6585 C  CD2   . LEU B 1 388 ? 1.32300   -8.69000  67.19200  1.000 36.38594  ? 388 LEU B CD2   1 
ATOM   6586 N  N     . GLY B 1 389 ? -3.26400  -7.46000  69.39000  1.000 25.99522  ? 389 GLY B N     1 
ATOM   6587 C  CA    . GLY B 1 389 ? -4.02900  -7.57600  70.62200  1.000 27.36118  ? 389 GLY B CA    1 
ATOM   6588 C  C     . GLY B 1 389 ? -4.96000  -8.77200  70.61600  1.000 28.23760  ? 389 GLY B C     1 
ATOM   6589 O  O     . GLY B 1 389 ? -5.06500  -9.49500  71.61000  1.000 28.27971  ? 389 GLY B O     1 
ATOM   6590 N  N     . ARG B 1 390 ? -5.62800  -9.01200  69.48600  1.000 24.38450  ? 390 ARG B N     1 
ATOM   6591 C  CA    . ARG B 1 390 ? -6.56800  -10.12500 69.41200  1.000 27.87966  ? 390 ARG B CA    1 
ATOM   6592 C  C     . ARG B 1 390 ? -5.84900  -11.46900 69.43700  1.000 26.76637  ? 390 ARG B C     1 
ATOM   6593 O  O     . ARG B 1 390 ? -6.31600  -12.41600 70.08000  1.000 29.31404  ? 390 ARG B O     1 
ATOM   6594 C  CB    . ARG B 1 390 ? -7.43500  -9.97300  68.16500  1.000 29.78252  ? 390 ARG B CB    1 
ATOM   6595 C  CG    . ARG B 1 390 ? -8.49500  -8.90300  68.35700  1.000 26.22156  ? 390 ARG B CG    1 
ATOM   6596 C  CD    . ARG B 1 390 ? -9.33700  -8.67100  67.12100  1.000 26.47686  ? 390 ARG B CD    1 
ATOM   6597 N  NE    . ARG B 1 390 ? -10.46100 -7.79000  67.43200  1.000 29.65882  ? 390 ARG B NE    1 
ATOM   6598 C  CZ    . ARG B 1 390 ? -11.21100 -7.17000  66.52700  1.000 32.99080  ? 390 ARG B CZ    1 
ATOM   6599 N  NH1   . ARG B 1 390 ? -10.96700 -7.32000  65.22700  1.000 34.35149  ? 390 ARG B NH1   1 
ATOM   6600 N  NH2   . ARG B 1 390 ? -12.20600 -6.39200  66.92800  1.000 32.51179  ? 390 ARG B NH2   1 
ATOM   6601 N  N     . LEU B 1 391 ? -4.70700  -11.56800 68.75400  1.000 28.54026  ? 391 LEU B N     1 
ATOM   6602 C  CA    . LEU B 1 391 ? -3.89100  -12.77500 68.83700  1.000 24.66085  ? 391 LEU B CA    1 
ATOM   6603 C  C     . LEU B 1 391 ? -3.42500  -13.01300 70.26700  1.000 30.53787  ? 391 LEU B C     1 
ATOM   6604 O  O     . LEU B 1 391 ? -3.52900  -14.12800 70.79100  1.000 32.23808  ? 391 LEU B O     1 
ATOM   6605 C  CB    . LEU B 1 391 ? -2.70000  -12.65800 67.88000  1.000 25.55306  ? 391 LEU B CB    1 
ATOM   6606 C  CG    . LEU B 1 391 ? -2.99500  -12.76400 66.37100  1.000 23.25542  ? 391 LEU B CG    1 
ATOM   6607 C  CD1   . LEU B 1 391 ? -1.83600  -12.21700 65.57200  1.000 24.23448  ? 391 LEU B CD1   1 
ATOM   6608 C  CD2   . LEU B 1 391 ? -3.25900  -14.21300 65.97300  1.000 24.27659  ? 391 LEU B CD2   1 
ATOM   6609 N  N     . TYR B 1 392 ? -2.90400  -11.96600 70.91500  1.000 29.60355  ? 392 TYR B N     1 
ATOM   6610 C  CA    . TYR B 1 392 ? -2.48800  -12.07100 72.31000  1.000 30.52471  ? 392 TYR B CA    1 
ATOM   6611 C  C     . TYR B 1 392 ? -3.62300  -12.57400 73.19500  1.000 30.95634  ? 392 TYR B C     1 
ATOM   6612 O  O     . TYR B 1 392 ? -3.43500  -13.49100 74.00400  1.000 28.75871  ? 392 TYR B O     1 
ATOM   6613 C  CB    . TYR B 1 392 ? -2.00400  -10.71300 72.81500  1.000 32.74866  ? 392 TYR B CB    1 
ATOM   6614 C  CG    . TYR B 1 392 ? -0.58300  -10.33500 72.46800  1.000 27.04798  ? 392 TYR B CG    1 
ATOM   6615 C  CD1   . TYR B 1 392 ? 0.47500   -11.20400 72.71300  1.000 30.98793  ? 392 TYR B CD1   1 
ATOM   6616 C  CD2   . TYR B 1 392 ? -0.29700  -9.09400  71.92400  1.000 27.74806  ? 392 TYR B CD2   1 
ATOM   6617 C  CE1   . TYR B 1 392 ? 1.77800   -10.84500 72.41400  1.000 30.97477  ? 392 TYR B CE1   1 
ATOM   6618 C  CE2   . TYR B 1 392 ? 0.99800   -8.73000  71.61400  1.000 26.41369  ? 392 TYR B CE2   1 
ATOM   6619 C  CZ    . TYR B 1 392 ? 2.03000   -9.60400  71.86200  1.000 29.44827  ? 392 TYR B CZ    1 
ATOM   6620 O  OH    . TYR B 1 392 ? 3.31600   -9.22900  71.55700  1.000 28.61659  ? 392 TYR B OH    1 
ATOM   6621 N  N     . MET B 1 393 ? -4.80200  -11.95000 73.08200  1.000 29.62460  ? 393 MET B N     1 
ATOM   6622 C  CA    . MET B 1 393 ? -5.95300  -12.36300 73.88600  1.000 35.90167  ? 393 MET B CA    1 
ATOM   6623 C  C     . MET B 1 393 ? -6.35000  -13.80200 73.57800  1.000 31.13794  ? 393 MET B C     1 
ATOM   6624 O  O     . MET B 1 393 ? -6.61900  -14.59300 74.48600  1.000 30.27468  ? 393 MET B O     1 
ATOM   6625 C  CB    . MET B 1 393 ? -7.13700  -11.41900 73.64400  1.000 35.22791  ? 393 MET B CB    1 
ATOM   6626 C  CG    . MET B 1 393 ? -6.94100  -9.98900  74.15000  1.000 33.85143  ? 393 MET B CG    1 
ATOM   6627 S  SD    . MET B 1 393 ? -6.60200  -9.89100  75.92200  1.000 38.92572  ? 393 MET B SD    1 
ATOM   6628 C  CE    . MET B 1 393 ? -6.81600  -8.14000  76.22400  1.000 48.13735  ? 393 MET B CE    1 
ATOM   6629 N  N     . GLY B 1 394 ? -6.40800  -14.15300 72.29300  1.000 39.17049  ? 394 GLY B N     1 
ATOM   6630 C  CA    . GLY B 1 394 ? -6.74300  -15.51900 71.91500  1.000 37.97034  ? 394 GLY B CA    1 
ATOM   6631 C  C     . GLY B 1 394 ? -5.80400  -16.55300 72.50700  1.000 37.39659  ? 394 GLY B C     1 
ATOM   6632 O  O     . GLY B 1 394 ? -6.21100  -17.68000 72.79800  1.000 37.12287  ? 394 GLY B O     1 
ATOM   6633 N  N     . LEU B 1 395 ? -4.52700  -16.20100 72.64700  1.000 30.23784  ? 395 LEU B N     1 
ATOM   6634 C  CA    . LEU B 1 395 ? -3.52000  -17.08700 73.21300  1.000 34.21726  ? 395 LEU B CA    1 
ATOM   6635 C  C     . LEU B 1 395 ? -3.36700  -16.92100 74.72400  1.000 36.77020  ? 395 LEU B C     1 
ATOM   6636 O  O     . LEU B 1 395 ? -2.45900  -17.52300 75.31000  1.000 36.24382  ? 395 LEU B O     1 
ATOM   6637 C  CB    . LEU B 1 395 ? -2.17700  -16.85900 72.51300  1.000 37.33869  ? 395 LEU B CB    1 
ATOM   6638 C  CG    . LEU B 1 395 ? -2.13400  -17.24600 71.02700  1.000 37.73084  ? 395 LEU B CG    1 
ATOM   6639 C  CD1   . LEU B 1 395 ? -0.91700  -16.66500 70.34000  1.000 43.81578  ? 395 LEU B CD1   1 
ATOM   6640 C  CD2   . LEU B 1 395 ? -2.14500  -18.76000 70.87100  1.000 38.10720  ? 395 LEU B CD2   1 
ATOM   6641 N  N     . GLU B 1 396 ? -4.23100  -16.11800 75.35400  1.000 38.59936  ? 396 GLU B N     1 
ATOM   6642 C  CA    . GLU B 1 396 ? -4.27100  -15.88100 76.79700  1.000 41.68658  ? 396 GLU B CA    1 
ATOM   6643 C  C     . GLU B 1 396 ? -3.10100  -15.04000 77.30200  1.000 40.21272  ? 396 GLU B C     1 
ATOM   6644 O  O     . GLU B 1 396 ? -2.75700  -15.10900 78.48900  1.000 41.13125  ? 396 GLU B O     1 
ATOM   6645 C  CB    . GLU B 1 396 ? -4.35300  -17.19300 77.58300  1.000 53.76171  ? 396 GLU B CB    1 
ATOM   6646 C  CG    . GLU B 1 396 ? -5.46200  -18.12400 77.12300  1.000 73.80359  ? 396 GLU B CG    1 
ATOM   6647 C  CD    . GLU B 1 396 ? -6.80300  -17.80100 77.75800  1.000 88.61062  ? 396 GLU B CD    1 
ATOM   6648 O  OE1   . GLU B 1 396 ? -7.22400  -16.62600 77.71200  1.000 93.90336  ? 396 GLU B OE1   1 
ATOM   6649 O  OE2   . GLU B 1 396 ? -7.43500  -18.72700 78.30700  1.000 105.27052 ? 396 GLU B OE2   1 
ATOM   6650 N  N     . HIS B 1 397 ? -2.49500  -14.22900 76.43200  1.000 34.86471  ? 397 HIS B N     1 
ATOM   6651 C  CA    . HIS B 1 397 ? -1.50100  -13.23400 76.83900  1.000 34.54098  ? 397 HIS B CA    1 
ATOM   6652 C  C     . HIS B 1 397 ? -2.23200  -11.93200 77.16400  1.000 33.44875  ? 397 HIS B C     1 
ATOM   6653 O  O     . HIS B 1 397 ? -2.15400  -10.93600 76.44700  1.000 32.20912  ? 397 HIS B O     1 
ATOM   6654 C  CB    . HIS B 1 397 ? -0.47400  -13.00800 75.73400  1.000 34.31990  ? 397 HIS B CB    1 
ATOM   6655 C  CG    . HIS B 1 397 ? 0.36700   -14.20300 75.40300  1.000 42.42614  ? 397 HIS B CG    1 
ATOM   6656 N  ND1   . HIS B 1 397 ? -0.14000  -15.48300 75.31700  1.000 44.25794  ? 397 HIS B ND1   1 
ATOM   6657 C  CD2   . HIS B 1 397 ? 1.68300   -14.30100 75.09900  1.000 40.88648  ? 397 HIS B CD2   1 
ATOM   6658 C  CE1   . HIS B 1 397 ? 0.83000   -16.31900 74.99300  1.000 46.62401  ? 397 HIS B CE1   1 
ATOM   6659 N  NE2   . HIS B 1 397 ? 1.94600   -15.62600 74.85200  1.000 44.19740  ? 397 HIS B NE2   1 
ATOM   6660 N  N     . LYS B 1 398 ? -2.94300  -11.94900 78.29100  1.000 37.75979  ? 398 LYS B N     1 
ATOM   6661 C  CA    . LYS B 1 398 ? -3.90100  -10.88000 78.56800  1.000 38.66253  ? 398 LYS B CA    1 
ATOM   6662 C  C     . LYS B 1 398 ? -3.22100  -9.52200  78.73700  1.000 33.30662  ? 398 LYS B C     1 
ATOM   6663 O  O     . LYS B 1 398 ? -3.73700  -8.50300  78.26200  1.000 32.38546  ? 398 LYS B O     1 
ATOM   6664 C  CB    . LYS B 1 398 ? -4.74600  -11.24700 79.78500  1.000 46.87141  ? 398 LYS B CB    1 
ATOM   6665 C  CG    . LYS B 1 398 ? -5.39900  -12.61500 79.63600  1.000 66.96066  ? 398 LYS B CG    1 
ATOM   6666 C  CD    . LYS B 1 398 ? -6.48900  -12.85400 80.66600  1.000 106.71806 ? 398 LYS B CD    1 
ATOM   6667 C  CE    . LYS B 1 398 ? -7.20900  -14.16900 80.39800  1.000 114.72691 ? 398 LYS B CE    1 
ATOM   6668 N  NZ    . LYS B 1 398 ? -8.29600  -14.42600 81.38300  1.000 119.80121 ? 398 LYS B NZ    1 
ATOM   6669 N  N     . ALA B 1 399 ? -2.07800  -9.47500  79.42500  1.000 33.57508  ? 399 ALA B N     1 
ATOM   6670 C  CA    . ALA B 1 399 ? -1.41800  -8.18900  79.64800  1.000 33.26978  ? 399 ALA B CA    1 
ATOM   6671 C  C     . ALA B 1 399 ? -0.94100  -7.57700  78.33500  1.000 29.39037  ? 399 ALA B C     1 
ATOM   6672 O  O     . ALA B 1 399 ? -1.21200  -6.40500  78.04800  1.000 32.22492  ? 399 ALA B O     1 
ATOM   6673 C  CB    . ALA B 1 399 ? -0.25300  -8.35500  80.62400  1.000 38.39934  ? 399 ALA B CB    1 
ATOM   6674 N  N     . ALA B 1 400 ? -0.23800  -8.35900  77.51300  1.000 30.57735  ? 400 ALA B N     1 
ATOM   6675 C  CA    . ALA B 1 400 ? 0.21600   -7.84400  76.22400  1.000 29.57723  ? 400 ALA B CA    1 
ATOM   6676 C  C     . ALA B 1 400 ? -0.96100  -7.54600  75.30700  1.000 27.41381  ? 400 ALA B C     1 
ATOM   6677 O  O     . ALA B 1 400 ? -0.91600  -6.59600  74.51700  1.000 22.11844  ? 400 ALA B O     1 
ATOM   6678 C  CB    . ALA B 1 400 ? 1.17400   -8.83500  75.56100  1.000 31.14321  ? 400 ALA B CB    1 
ATOM   6679 N  N     . GLY B 1 401 ? -2.02100  -8.35100  75.39300  1.000 37.30184  ? 401 GLY B N     1 
ATOM   6680 C  CA    . GLY B 1 401 ? -3.21600  -8.06500  74.61500  1.000 31.96962  ? 401 GLY B CA    1 
ATOM   6681 C  C     . GLY B 1 401 ? -3.83100  -6.72500  74.96500  1.000 33.19609  ? 401 GLY B C     1 
ATOM   6682 O  O     . GLY B 1 401 ? -4.12800  -5.91300  74.08400  1.000 34.96472  ? 401 GLY B O     1 
ATOM   6683 N  N     . GLU B 1 402 ? -4.02100  -6.47200  76.26200  1.000 29.86411  ? 402 GLU B N     1 
ATOM   6684 C  CA    . GLU B 1 402 ? -4.58800  -5.19900  76.69800  1.000 30.88528  ? 402 GLU B CA    1 
ATOM   6685 C  C     . GLU B 1 402 ? -3.76500  -4.02100  76.18700  1.000 31.15374  ? 402 GLU B C     1 
ATOM   6686 O  O     . GLU B 1 402 ? -4.31500  -3.05800  75.63800  1.000 29.14560  ? 402 GLU B O     1 
ATOM   6687 C  CB    . GLU B 1 402 ? -4.69300  -5.17400  78.22400  1.000 40.13376  ? 402 GLU B CB    1 
ATOM   6688 C  CG    . GLU B 1 402 ? -5.46600  -3.98800  78.76000  1.000 50.89821  ? 402 GLU B CG    1 
ATOM   6689 C  CD    . GLU B 1 402 ? -5.68100  -4.05400  80.25900  1.000 61.05469  ? 402 GLU B CD    1 
ATOM   6690 O  OE1   . GLU B 1 402 ? -5.67500  -5.17500  80.81300  1.000 55.88302  ? 402 GLU B OE1   1 
ATOM   6691 O  OE2   . GLU B 1 402 ? -5.85300  -2.98300  80.88200  1.000 86.89463  ? 402 GLU B OE2   1 
ATOM   6692 N  N     . LYS B 1 403 ? -2.43600  -4.09200  76.33500  1.000 30.67210  ? 403 LYS B N     1 
ATOM   6693 C  CA    . LYS B 1 403 ? -1.57300  -3.01700  75.84600  1.000 32.74603  ? 403 LYS B CA    1 
ATOM   6694 C  C     . LYS B 1 403 ? -1.76900  -2.77100  74.35600  1.000 24.15553  ? 403 LYS B C     1 
ATOM   6695 O  O     . LYS B 1 403 ? -1.92600  -1.62400  73.91900  1.000 23.02908  ? 403 LYS B O     1 
ATOM   6696 C  CB    . LYS B 1 403 ? -0.10200  -3.33000  76.12300  1.000 36.43068  ? 403 LYS B CB    1 
ATOM   6697 C  CG    . LYS B 1 403 ? 0.39400   -2.94800  77.49400  1.000 57.16738  ? 403 LYS B CG    1 
ATOM   6698 C  CD    . LYS B 1 403 ? 1.82100   -3.44100  77.69700  1.000 84.87597  ? 403 LYS B CD    1 
ATOM   6699 C  CE    . LYS B 1 403 ? 2.73600   -2.97800  76.56300  1.000 91.92681  ? 403 LYS B CE    1 
ATOM   6700 N  NZ    . LYS B 1 403 ? 2.69900   -1.50200  76.34900  1.000 79.07790  ? 403 LYS B NZ    1 
ATOM   6701 N  N     . ALA B 1 404 ? -1.73800  -3.83000  73.54900  1.000 25.73993  ? 404 ALA B N     1 
ATOM   6702 C  CA    . ALA B 1 404 ? -1.86300  -3.62600  72.11000  1.000 24.98457  ? 404 ALA B CA    1 
ATOM   6703 C  C     . ALA B 1 404 ? -3.24400  -3.08800  71.74900  1.000 25.14775  ? 404 ALA B C     1 
ATOM   6704 O  O     . ALA B 1 404 ? -3.36300  -2.16400  70.93500  1.000 21.54995  ? 404 ALA B O     1 
ATOM   6705 C  CB    . ALA B 1 404 ? -1.56500  -4.92500  71.36500  1.000 28.93505  ? 404 ALA B CB    1 
ATOM   6706 N  N     . LEU B 1 405 ? -4.30200  -3.62800  72.36400  1.000 25.97943  ? 405 LEU B N     1 
ATOM   6707 C  CA    . LEU B 1 405 ? -5.64400  -3.13700  72.05700  1.000 25.15302  ? 405 LEU B CA    1 
ATOM   6708 C  C     . LEU B 1 405 ? -5.78200  -1.65900  72.40100  1.000 24.92667  ? 405 LEU B C     1 
ATOM   6709 O  O     . LEU B 1 405 ? -6.40400  -0.89400  71.65300  1.000 25.51622  ? 405 LEU B O     1 
ATOM   6710 C  CB    . LEU B 1 405 ? -6.69900  -3.96400  72.79000  1.000 27.31380  ? 405 LEU B CB    1 
ATOM   6711 C  CG    . LEU B 1 405 ? -6.83200  -5.42400  72.35200  1.000 27.50593  ? 405 LEU B CG    1 
ATOM   6712 C  CD1   . LEU B 1 405 ? -7.87300  -6.13800  73.19700  1.000 35.27528  ? 405 LEU B CD1   1 
ATOM   6713 C  CD2   . LEU B 1 405 ? -7.17700  -5.52500  70.87900  1.000 35.10158  ? 405 LEU B CD2   1 
ATOM   6714 N  N     . LYS B 1 406 ? -5.18400  -1.23200  73.51700  1.000 26.68215  ? 406 LYS B N     1 
ATOM   6715 C  CA    . LYS B 1 406 ? -5.22300  0.17900   73.89000  1.000 30.99582  ? 406 LYS B CA    1 
ATOM   6716 C  C     . LYS B 1 406 ? -4.46100  1.03900   72.88800  1.000 26.25841  ? 406 LYS B C     1 
ATOM   6717 O  O     . LYS B 1 406 ? -4.87700  2.16500   72.59000  1.000 32.11964  ? 406 LYS B O     1 
ATOM   6718 C  CB    . LYS B 1 406 ? -4.66700  0.36600   75.30300  1.000 31.41166  ? 406 LYS B CB    1 
ATOM   6719 C  CG    . LYS B 1 406 ? -5.62200  -0.08200  76.39800  1.000 44.79484  ? 406 LYS B CG    1 
ATOM   6720 C  CD    . LYS B 1 406 ? -5.01400  0.05600   77.78500  1.000 44.08686  ? 406 LYS B CD    1 
ATOM   6721 C  CE    . LYS B 1 406 ? -5.99300  -0.43100  78.85200  1.000 60.59674  ? 406 LYS B CE    1 
ATOM   6722 N  NZ    . LYS B 1 406 ? -5.39600  -0.51100  80.22200  1.000 65.04201  ? 406 LYS B NZ    1 
ATOM   6723 N  N     . LYS B 1 407 ? -3.34600  0.52900   72.35300  1.000 34.02513  ? 407 LYS B N     1 
ATOM   6724 C  CA    . LYS B 1 407 ? -2.64400  1.25300   71.29600  1.000 26.67425  ? 407 LYS B CA    1 
ATOM   6725 C  C     . LYS B 1 407 ? -3.53600  1.43900   70.07600  1.000 24.58189  ? 407 LYS B C     1 
ATOM   6726 O  O     . LYS B 1 407 ? -3.54300  2.51100   69.45700  1.000 24.67664  ? 407 LYS B O     1 
ATOM   6727 C  CB    . LYS B 1 407 ? -1.37000  0.51100   70.88800  1.000 35.24107  ? 407 LYS B CB    1 
ATOM   6728 C  CG    . LYS B 1 407 ? -0.19000  0.60300   71.85100  1.000 42.32876  ? 407 LYS B CG    1 
ATOM   6729 C  CD    . LYS B 1 407 ? 0.48600   1.95700   71.75400  1.000 49.77439  ? 407 LYS B CD    1 
ATOM   6730 C  CE    . LYS B 1 407 ? 1.92000   1.89200   72.25400  1.000 64.94726  ? 407 LYS B CE    1 
ATOM   6731 N  NZ    . LYS B 1 407 ? 2.14900   0.73700   73.16500  1.000 64.11558  ? 407 LYS B NZ    1 
ATOM   6732 N  N     . ALA B 1 408 ? -4.29800  0.40200   69.71700  1.000 23.60020  ? 408 ALA B N     1 
ATOM   6733 C  CA    . ALA B 1 408 ? -5.20700  0.50300   68.58300  1.000 25.53464  ? 408 ALA B CA    1 
ATOM   6734 C  C     . ALA B 1 408 ? -6.29800  1.53400   68.84400  1.000 24.45556  ? 408 ALA B C     1 
ATOM   6735 O  O     . ALA B 1 408 ? -6.60600  2.35600   67.97200  1.000 29.03769  ? 408 ALA B O     1 
ATOM   6736 C  CB    . ALA B 1 408 ? -5.81500  -0.86800  68.28700  1.000 24.33450  ? 408 ALA B CB    1 
ATOM   6737 N  N     . ILE B 1 409 ? -6.88200  1.51100   70.04700  1.000 29.24561  ? 409 ILE B N     1 
ATOM   6738 C  CA    . ILE B 1 409 ? -7.96100  2.43500   70.39200  1.000 28.66133  ? 409 ILE B CA    1 
ATOM   6739 C  C     . ILE B 1 409 ? -7.49100  3.88100   70.30100  1.000 28.39814  ? 409 ILE B C     1 
ATOM   6740 O  O     . ILE B 1 409 ? -8.21600  4.75600   69.80600  1.000 28.30076  ? 409 ILE B O     1 
ATOM   6741 C  CB    . ILE B 1 409 ? -8.51600  2.10300   71.79200  1.000 32.13806  ? 409 ILE B CB    1 
ATOM   6742 C  CG1   . ILE B 1 409 ? -9.34100  0.82000   71.74900  1.000 33.49086  ? 409 ILE B CG1   1 
ATOM   6743 C  CG2   . ILE B 1 409 ? -9.34900  3.25700   72.34300  1.000 31.57747  ? 409 ILE B CG2   1 
ATOM   6744 C  CD1   . ILE B 1 409 ? -9.76300  0.32700   73.11100  1.000 50.65871  ? 409 ILE B CD1   1 
ATOM   6745 N  N     . ALA B 1 410 ? -6.28300  4.16200   70.79500  1.000 28.21391  ? 410 ALA B N     1 
ATOM   6746 C  CA    . ALA B 1 410 ? -5.79300  5.53600   70.80200  1.000 32.57496  ? 410 ALA B CA    1 
ATOM   6747 C  C     . ALA B 1 410 ? -5.74500  6.11600   69.39400  1.000 31.77223  ? 410 ALA B C     1 
ATOM   6748 O  O     . ALA B 1 410 ? -6.08600  7.28600   69.18600  1.000 38.53883  ? 410 ALA B O     1 
ATOM   6749 C  CB    . ALA B 1 410 ? -4.41700  5.60100   71.46300  1.000 32.39336  ? 410 ALA B CB    1 
ATOM   6750 N  N     . ILE B 1 411 ? -5.35100  5.30900   68.40900  1.000 27.93756  ? 411 ILE B N     1 
ATOM   6751 C  CA    . ILE B 1 411 ? -5.31500  5.80400   67.03700  1.000 26.52686  ? 411 ILE B CA    1 
ATOM   6752 C  C     . ILE B 1 411 ? -6.72000  5.88800   66.45900  1.000 25.12933  ? 411 ILE B C     1 
ATOM   6753 O  O     . ILE B 1 411 ? -7.06700  6.86600   65.78700  1.000 29.63513  ? 411 ILE B O     1 
ATOM   6754 C  CB    . ILE B 1 411 ? -4.40700  4.91800   66.17000  1.000 29.76936  ? 411 ILE B CB    1 
ATOM   6755 C  CG1   . ILE B 1 411 ? -2.97300  4.96100   66.69400  1.000 29.65619  ? 411 ILE B CG1   1 
ATOM   6756 C  CG2   . ILE B 1 411 ? -4.47500  5.36200   64.70700  1.000 30.51155  ? 411 ILE B CG2   1 
ATOM   6757 C  CD1   . ILE B 1 411 ? -2.06100  3.91500   66.08200  1.000 34.85418  ? 411 ILE B CD1   1 
ATOM   6758 N  N     . MET B 1 412 ? -7.54200  4.86400   66.69900  1.000 27.67437  ? 412 MET B N     1 
ATOM   6759 C  CA    . MET B 1 412 ? -8.87200  4.82000   66.10400  1.000 34.72785  ? 412 MET B CA    1 
ATOM   6760 C  C     . MET B 1 412 ? -9.77400  5.92600   66.64100  1.000 27.86650  ? 412 MET B C     1 
ATOM   6761 O  O     . MET B 1 412 ? -10.65900 6.39800   65.92000  1.000 34.09619  ? 412 MET B O     1 
ATOM   6762 C  CB    . MET B 1 412 ? -9.49900  3.44500   66.33400  1.000 34.59625  ? 412 MET B CB    1 
ATOM   6763 C  CG    . MET B 1 412 ? -8.77600  2.33800   65.59300  1.000 37.47028  ? 412 MET B CG    1 
ATOM   6764 S  SD    . MET B 1 412 ? -9.39900  0.69900   65.98800  1.000 35.00420  ? 412 MET B SD    1 
ATOM   6765 C  CE    . MET B 1 412 ? -10.94500 0.69300   65.08800  1.000 40.94701  ? 412 MET B CE    1 
ATOM   6766 N  N     . GLU B 1 413 ? -9.58600  6.33700   67.90000  1.000 34.61994  ? 413 GLU B N     1 
ATOM   6767 C  CA    . GLU B 1 413 ? -10.37600 7.44100   68.44200  1.000 32.26439  ? 413 GLU B CA    1 
ATOM   6768 C  C     . GLU B 1 413 ? -10.23300 8.69300   67.58700  1.000 30.36417  ? 413 GLU B C     1 
ATOM   6769 O  O     . GLU B 1 413 ? -11.19500 9.44900   67.41100  1.000 36.99654  ? 413 GLU B O     1 
ATOM   6770 C  CB    . GLU B 1 413 ? -9.96800  7.72800   69.88800  1.000 35.57005  ? 413 GLU B CB    1 
ATOM   6771 C  CG    . GLU B 1 413 ? -10.54600 6.74600   70.89800  1.000 47.43990  ? 413 GLU B CG    1 
ATOM   6772 C  CD    . GLU B 1 413 ? -10.11600 7.04000   72.32700  1.000 53.29323  ? 413 GLU B CD    1 
ATOM   6773 O  OE1   . GLU B 1 413 ? -9.05100  7.66600   72.51600  1.000 53.64591  ? 413 GLU B OE1   1 
ATOM   6774 O  OE2   . GLU B 1 413 ? -10.83800 6.62900   73.26200  1.000 58.01222  ? 413 GLU B OE2   1 
ATOM   6775 N  N     . VAL B 1 414 ? -9.03500  8.92900   67.04800  1.000 28.43499  ? 414 VAL B N     1 
ATOM   6776 C  CA    . VAL B 1 414 ? -8.82200  10.06800  66.16100  1.000 28.89031  ? 414 VAL B CA    1 
ATOM   6777 C  C     . VAL B 1 414 ? -9.45900  9.81400   64.79700  1.000 22.96591  ? 414 VAL B C     1 
ATOM   6778 O  O     . VAL B 1 414 ? -10.26200 10.62000  64.31200  1.000 22.32110  ? 414 VAL B O     1 
ATOM   6779 C  CB    . VAL B 1 414 ? -7.31600  10.37300  66.03800  1.000 26.89796  ? 414 VAL B CB    1 
ATOM   6780 C  CG1   . VAL B 1 414 ? -7.07200  11.41700  64.96100  1.000 38.98362  ? 414 VAL B CG1   1 
ATOM   6781 C  CG2   . VAL B 1 414 ? -6.76500  10.84500  67.37700  1.000 29.24298  ? 414 VAL B CG2   1 
ATOM   6782 N  N     . ALA B 1 415 ? -9.12400  8.68000   64.16700  1.000 20.98409  ? 415 ALA B N     1 
ATOM   6783 C  CA    . ALA B 1 415 ? -9.56300  8.42300   62.79300  1.000 25.49779  ? 415 ALA B CA    1 
ATOM   6784 C  C     . ALA B 1 415 ? -11.04200 8.04900   62.71100  1.000 26.12418  ? 415 ALA B C     1 
ATOM   6785 O  O     . ALA B 1 415 ? -11.73500 8.46100   61.77500  1.000 29.59829  ? 415 ALA B O     1 
ATOM   6786 C  CB    . ALA B 1 415 ? -8.70500  7.32300   62.17100  1.000 30.81685  ? 415 ALA B CB    1 
ATOM   6787 N  N     . HIS B 1 416 ? -11.54000 7.24400   63.65300  1.000 27.70859  ? 416 HIS B N     1 
ATOM   6788 C  CA    . HIS B 1 416 ? -12.91700 6.76300   63.62000  1.000 27.06640  ? 416 HIS B CA    1 
ATOM   6789 C  C     . HIS B 1 416 ? -13.86400 7.58300   64.48100  1.000 29.79568  ? 416 HIS B C     1 
ATOM   6790 O  O     . HIS B 1 416 ? -15.08200 7.39700   64.37900  1.000 29.56933  ? 416 HIS B O     1 
ATOM   6791 C  CB    . HIS B 1 416 ? -13.01200 5.30600   64.09700  1.000 29.77199  ? 416 HIS B CB    1 
ATOM   6792 C  CG    . HIS B 1 416 ? -12.43700 4.30500   63.14700  1.000 33.24872  ? 416 HIS B CG    1 
ATOM   6793 N  ND1   . HIS B 1 416 ? -11.09900 3.97300   63.13600  1.000 32.04595  ? 416 HIS B ND1   1 
ATOM   6794 C  CD2   . HIS B 1 416 ? -13.01800 3.55500   62.18100  1.000 40.23114  ? 416 HIS B CD2   1 
ATOM   6795 C  CE1   . HIS B 1 416 ? -10.88100 3.06400   62.20400  1.000 34.66468  ? 416 HIS B CE1   1 
ATOM   6796 N  NE2   . HIS B 1 416 ? -12.03000 2.79000   61.61300  1.000 34.59889  ? 416 HIS B NE2   1 
ATOM   6797 N  N     . GLY B 1 417 ? -13.34700 8.43200   65.36400  1.000 30.60104  ? 417 GLY B N     1 
ATOM   6798 C  CA    . GLY B 1 417 ? -14.20600 9.10700   66.31500  1.000 28.07705  ? 417 GLY B CA    1 
ATOM   6799 C  C     . GLY B 1 417 ? -14.39500 8.29400   67.57900  1.000 32.51706  ? 417 GLY B C     1 
ATOM   6800 O  O     . GLY B 1 417 ? -14.48600 7.06200   67.52800  1.000 33.39611  ? 417 GLY B O     1 
ATOM   6801 N  N     . LYS B 1 418 ? -14.46100 8.98700   68.71900  1.000 31.27217  ? 418 LYS B N     1 
ATOM   6802 C  CA    . LYS B 1 418 ? -14.50200 8.32400   70.02000  1.000 39.13364  ? 418 LYS B CA    1 
ATOM   6803 C  C     . LYS B 1 418 ? -15.72300 7.42800   70.17700  1.000 38.29143  ? 418 LYS B C     1 
ATOM   6804 O  O     . LYS B 1 418 ? -15.69700 6.48400   70.97300  1.000 40.95228  ? 418 LYS B O     1 
ATOM   6805 C  CB    . LYS B 1 418 ? -14.47800 9.36800   71.13400  1.000 45.31070  ? 418 LYS B CB    1 
ATOM   6806 C  CG    . LYS B 1 418 ? -13.16900 10.11600  71.26300  1.000 62.37853  ? 418 LYS B CG    1 
ATOM   6807 C  CD    . LYS B 1 418 ? -13.31000 11.27300  72.23600  1.000 75.30903  ? 418 LYS B CD    1 
ATOM   6808 C  CE    . LYS B 1 418 ? -12.07600 12.15800  72.23900  1.000 69.91101  ? 418 LYS B CE    1 
ATOM   6809 N  NZ    . LYS B 1 418 ? -10.86700 11.42300  72.69700  1.000 84.55751  ? 418 LYS B NZ    1 
ATOM   6810 N  N     . ASP B 1 419 ? -16.80700 7.72500   69.46700  1.000 40.23640  ? 419 ASP B N     1 
ATOM   6811 C  CA    . ASP B 1 419 ? -18.06500 7.01300   69.62700  1.000 45.04224  ? 419 ASP B CA    1 
ATOM   6812 C  C     . ASP B 1 419 ? -18.28300 5.92900   68.57300  1.000 39.69686  ? 419 ASP B C     1 
ATOM   6813 O  O     . ASP B 1 419 ? -19.40000 5.41500   68.45600  1.000 45.25016  ? 419 ASP B O     1 
ATOM   6814 C  CB    . ASP B 1 419 ? -19.23000 8.00700   69.61400  1.000 50.91400  ? 419 ASP B CB    1 
ATOM   6815 C  CG    . ASP B 1 419 ? -19.23300 8.88900   68.37600  1.000 77.17241  ? 419 ASP B CG    1 
ATOM   6816 O  OD1   . ASP B 1 419 ? -18.13800 9.15700   67.82200  1.000 50.02179  ? 419 ASP B OD1   1 
ATOM   6817 O  OD2   . ASP B 1 419 ? -20.33300 9.31800   67.96100  1.000 74.97478  ? 419 ASP B OD2   1 
ATOM   6818 N  N     . HIS B 1 420 ? -17.25200 5.56700   67.81100  1.000 34.05408  ? 420 HIS B N     1 
ATOM   6819 C  CA    . HIS B 1 420 ? -17.43300 4.60000   66.73500  1.000 32.34335  ? 420 HIS B CA    1 
ATOM   6820 C  C     . HIS B 1 420 ? -17.72600 3.21300   67.30800  1.000 37.47028  ? 420 HIS B C     1 
ATOM   6821 O  O     . HIS B 1 420 ? -17.10800 2.80700   68.29700  1.000 43.53680  ? 420 HIS B O     1 
ATOM   6822 C  CB    . HIS B 1 420 ? -16.18700 4.54500   65.84400  1.000 30.19573  ? 420 HIS B CB    1 
ATOM   6823 C  CG    . HIS B 1 420 ? -16.42500 3.90700   64.50900  1.000 28.54026  ? 420 HIS B CG    1 
ATOM   6824 N  ND1   . HIS B 1 420 ? -16.52100 2.54200   64.34100  1.000 32.13543  ? 420 HIS B ND1   1 
ATOM   6825 C  CD2   . HIS B 1 420 ? -16.59100 4.45000   63.27900  1.000 36.20960  ? 420 HIS B CD2   1 
ATOM   6826 C  CE1   . HIS B 1 420 ? -16.74000 2.27100   63.06600  1.000 35.63585  ? 420 HIS B CE1   1 
ATOM   6827 N  NE2   . HIS B 1 420 ? -16.78300 3.41200   62.40000  1.000 37.18604  ? 420 HIS B NE2   1 
ATOM   6828 N  N     . PRO B 1 421 ? -18.66100 2.46800   66.71100  1.000 44.30794  ? 421 PRO B N     1 
ATOM   6829 C  CA    . PRO B 1 421 ? -18.92800 1.09300   67.17200  1.000 45.15541  ? 421 PRO B CA    1 
ATOM   6830 C  C     . PRO B 1 421 ? -17.69200 0.21600   67.27500  1.000 41.87344  ? 421 PRO B C     1 
ATOM   6831 O  O     . PRO B 1 421 ? -17.65200 -0.67300  68.13500  1.000 48.21631  ? 421 PRO B O     1 
ATOM   6832 C  CB    . PRO B 1 421 ? -19.90300 0.56200   66.11400  1.000 49.24801  ? 421 PRO B CB    1 
ATOM   6833 C  CG    . PRO B 1 421 ? -20.60100 1.77900   65.61300  1.000 47.29514  ? 421 PRO B CG    1 
ATOM   6834 C  CD    . PRO B 1 421 ? -19.58400 2.88400   65.64000  1.000 47.09512  ? 421 PRO B CD    1 
ATOM   6835 N  N     . TYR B 1 422 ? -16.69500 0.41200   66.40300  1.000 35.26212  ? 422 TYR B N     1 
ATOM   6836 C  CA    . TYR B 1 422 ? -15.47700 -0.39000  66.48400  1.000 35.18053  ? 422 TYR B CA    1 
ATOM   6837 C  C     . TYR B 1 422 ? -14.79600 -0.23000  67.83600  1.000 33.35663  ? 422 TYR B C     1 
ATOM   6838 O  O     . TYR B 1 422 ? -14.30500 -1.20600  68.41300  1.000 37.64925  ? 422 TYR B O     1 
ATOM   6839 C  CB    . TYR B 1 422 ? -14.50500 -0.00700  65.36300  1.000 32.64339  ? 422 TYR B CB    1 
ATOM   6840 C  CG    . TYR B 1 422 ? -14.87200 -0.54300  63.99500  1.000 34.39097  ? 422 TYR B CG    1 
ATOM   6841 C  CD1   . TYR B 1 422 ? -15.72200 -1.63500  63.86000  1.000 33.34610  ? 422 TYR B CD1   1 
ATOM   6842 C  CD2   . TYR B 1 422 ? -14.35900 0.03800   62.83600  1.000 31.70380  ? 422 TYR B CD2   1 
ATOM   6843 C  CE1   . TYR B 1 422 ? -16.05900 -2.13400  62.61600  1.000 36.49122  ? 422 TYR B CE1   1 
ATOM   6844 C  CE2   . TYR B 1 422 ? -14.69100 -0.45800  61.58200  1.000 42.14453  ? 422 TYR B CE2   1 
ATOM   6845 C  CZ    . TYR B 1 422 ? -15.54300 -1.54400  61.48200  1.000 37.66241  ? 422 TYR B CZ    1 
ATOM   6846 O  OH    . TYR B 1 422 ? -15.88100 -2.04800  60.24800  1.000 48.82427  ? 422 TYR B OH    1 
ATOM   6847 N  N     . ILE B 1 423 ? -14.77500 0.99100   68.36900  1.000 33.95670  ? 423 ILE B N     1 
ATOM   6848 C  CA    . ILE B 1 423 ? -14.07400 1.22900   69.62600  1.000 31.46167  ? 423 ILE B CA    1 
ATOM   6849 C  C     . ILE B 1 423 ? -14.81600 0.57200   70.78300  1.000 35.07526  ? 423 ILE B C     1 
ATOM   6850 O  O     . ILE B 1 423 ? -14.19500 0.02300   71.70200  1.000 38.95993  ? 423 ILE B O     1 
ATOM   6851 C  CB    . ILE B 1 423 ? -13.87300 2.74000   69.83700  1.000 37.29658  ? 423 ILE B CB    1 
ATOM   6852 C  CG1   . ILE B 1 423 ? -12.86300 3.26700   68.81800  1.000 46.07395  ? 423 ILE B CG1   1 
ATOM   6853 C  CG2   . ILE B 1 423 ? -13.38200 3.03700   71.24800  1.000 38.38355  ? 423 ILE B CG2   1 
ATOM   6854 C  CD1   . ILE B 1 423 ? -12.73400 4.75700   68.80100  1.000 51.21930  ? 423 ILE B CD1   1 
ATOM   6855 N  N     . SER B 1 424 ? -16.15200 0.60500   70.75200  1.000 40.34694  ? 424 SER B N     1 
ATOM   6856 C  CA    . SER B 1 424 ? -16.94300 -0.11500  71.74700  1.000 38.23353  ? 424 SER B CA    1 
ATOM   6857 C  C     . SER B 1 424 ? -16.64600 -1.60700  71.71800  1.000 36.62281  ? 424 SER B C     1 
ATOM   6858 O  O     . SER B 1 424 ? -16.52000 -2.23900  72.77200  1.000 36.05432  ? 424 SER B O     1 
ATOM   6859 C  CB    . SER B 1 424 ? -18.43400 0.13300   71.52100  1.000 39.26523  ? 424 SER B CB    1 
ATOM   6860 O  OG    . SER B 1 424 ? -18.73100 1.51500   71.60800  1.000 56.16726  ? 424 SER B OG    1 
ATOM   6861 N  N     . GLU B 1 425 ? -16.55300 -2.19300  70.51900  1.000 34.16725  ? 425 GLU B N     1 
ATOM   6862 C  CA    . GLU B 1 425 ? -16.25000 -3.61800  70.41300  1.000 45.73969  ? 425 GLU B CA    1 
ATOM   6863 C  C     . GLU B 1 425 ? -14.91100 -3.95500  71.05500  1.000 40.13376  ? 425 GLU B C     1 
ATOM   6864 O  O     . GLU B 1 425 ? -14.78400 -4.96500  71.75800  1.000 43.10780  ? 425 GLU B O     1 
ATOM   6865 C  CB    . GLU B 1 425 ? -16.23600 -4.05300  68.94900  1.000 41.09703  ? 425 GLU B CB    1 
ATOM   6866 C  CG    . GLU B 1 425 ? -17.57000 -3.98500  68.24100  1.000 70.35580  ? 425 GLU B CG    1 
ATOM   6867 C  CD    . GLU B 1 425 ? -17.47500 -4.49300  66.81600  1.000 79.54901  ? 425 GLU B CD    1 
ATOM   6868 O  OE1   . GLU B 1 425 ? -16.47700 -5.18000  66.49900  1.000 78.87261  ? 425 GLU B OE1   1 
ATOM   6869 O  OE2   . GLU B 1 425 ? -18.38900 -4.20000  66.01500  1.000 92.57689  ? 425 GLU B OE2   1 
ATOM   6870 N  N     . ILE B 1 426 ? -13.89400 -3.13600  70.79600  1.000 30.49839  ? 426 ILE B N     1 
ATOM   6871 C  CA    . ILE B 1 426 ? -12.54600 -3.43800  71.26800  1.000 33.98302  ? 426 ILE B CA    1 
ATOM   6872 C  C     . ILE B 1 426 ? -12.44900 -3.26300  72.78000  1.000 31.25638  ? 426 ILE B C     1 
ATOM   6873 O  O     . ILE B 1 426 ? -11.76300 -4.03100  73.46400  1.000 38.00456  ? 426 ILE B O     1 
ATOM   6874 C  CB    . ILE B 1 426 ? -11.52500 -2.56400  70.51800  1.000 31.68801  ? 426 ILE B CB    1 
ATOM   6875 C  CG1   . ILE B 1 426 ? -11.55400 -2.89900  69.02400  1.000 32.11174  ? 426 ILE B CG1   1 
ATOM   6876 C  CG2   . ILE B 1 426 ? -10.12100 -2.77600  71.07300  1.000 34.40412  ? 426 ILE B CG2   1 
ATOM   6877 C  CD1   . ILE B 1 426 ? -10.93900 -1.83600  68.13800  1.000 32.17754  ? 426 ILE B CD1   1 
ATOM   6878 N  N     . LYS B 1 427 ? -13.14400 -2.26500  73.33100  1.000 36.71230  ? 427 LYS B N     1 
ATOM   6879 C  CA    . LYS B 1 427 ? -13.15700 -2.10300  74.78100  1.000 42.68143  ? 427 LYS B CA    1 
ATOM   6880 C  C     . LYS B 1 427 ? -13.79300 -3.30100  75.47800  1.000 37.39922  ? 427 LYS B C     1 
ATOM   6881 O  O     . LYS B 1 427 ? -13.39400 -3.63900  76.60200  1.000 48.27684  ? 427 LYS B O     1 
ATOM   6882 C  CB    . LYS B 1 427 ? -13.87500 -0.80700  75.16000  1.000 48.51634  ? 427 LYS B CB    1 
ATOM   6883 C  CG    . LYS B 1 427 ? -13.06400 0.45600   74.94800  1.000 43.51311  ? 427 LYS B CG    1 
ATOM   6884 C  CD    . LYS B 1 427 ? -13.86000 1.66400   75.41400  1.000 49.43487  ? 427 LYS B CD    1 
ATOM   6885 C  CE    . LYS B 1 427 ? -13.19800 2.95700   74.99600  1.000 53.67486  ? 427 LYS B CE    1 
ATOM   6886 N  NZ    . LYS B 1 427 ? -11.87400 3.11900   75.65500  1.000 67.30544  ? 427 LYS B NZ    1 
ATOM   6887 N  N     . GLN B 1 428 ? -14.77000 -3.95800  74.83000  1.000 41.43655  ? 428 GLN B N     1 
ATOM   6888 C  CA    . GLN B 1 428 ? -15.33200 -5.18600  75.38200  1.000 46.45820  ? 428 GLN B CA    1 
ATOM   6889 C  C     . GLN B 1 428 ? -14.26300 -6.26500  75.48500  1.000 53.11953  ? 428 GLN B C     1 
ATOM   6890 O  O     . GLN B 1 428 ? -14.20800 -7.00700  76.47100  1.000 54.88816  ? 428 GLN B O     1 
ATOM   6891 C  CB    . GLN B 1 428 ? -16.49500 -5.68100  74.50800  1.000 52.27995  ? 428 GLN B CB    1 
ATOM   6892 C  CG    . GLN B 1 428 ? -17.66500 -4.72900  74.37100  1.000 66.65536  ? 428 GLN B CG    1 
ATOM   6893 C  CD    . GLN B 1 428 ? -18.68500 -5.21900  73.34700  1.000 72.84294  ? 428 GLN B CD    1 
ATOM   6894 O  OE1   . GLN B 1 428 ? -19.12800 -4.46600  72.47700  1.000 65.07622  ? 428 GLN B OE1   1 
ATOM   6895 N  NE2   . GLN B 1 428 ? -19.06600 -6.48800  73.45400  1.000 77.15136  ? 428 GLN B NE2   1 
ATOM   6896 N  N     . GLU B 1 429 ? -13.39000 -6.34700  74.47600  1.000 43.72630  ? 429 GLU B N     1 
ATOM   6897 C  CA    . GLU B 1 429 ? -12.36600 -7.38200  74.43900  1.000 44.66851  ? 429 GLU B CA    1 
ATOM   6898 C  C     . GLU B 1 429 ? -11.31100 -7.18600  75.52300  1.000 51.32457  ? 429 GLU B C     1 
ATOM   6899 O  O     . GLU B 1 429 ? -10.63300 -8.15000  75.88600  1.000 49.84282  ? 429 GLU B O     1 
ATOM   6900 C  CB    . GLU B 1 429 ? -11.71600 -7.41000  73.05200  1.000 41.81291  ? 429 GLU B CB    1 
ATOM   6901 C  CG    . GLU B 1 429 ? -12.69900 -7.74300  71.93900  1.000 47.76889  ? 429 GLU B CG    1 
ATOM   6902 C  CD    . GLU B 1 429 ? -12.08000 -7.69100  70.55100  1.000 48.12419  ? 429 GLU B CD    1 
ATOM   6903 O  OE1   . GLU B 1 429 ? -10.98100 -8.25200  70.35900  1.000 56.34623  ? 429 GLU B OE1   1 
ATOM   6904 O  OE2   . GLU B 1 429 ? -12.70500 -7.09900  69.64600  1.000 65.91580  ? 429 GLU B OE2   1 
ATOM   6905 N  N     . ILE B 1 430 ? -11.17300 -5.97500  76.06900  1.000 42.57089  ? 430 ILE B N     1 
ATOM   6906 C  CA    . ILE B 1 430 ? -10.24800 -5.76000  77.18100  1.000 45.87392  ? 430 ILE B CA    1 
ATOM   6907 C  C     . ILE B 1 430 ? -10.82100 -6.30700  78.48200  1.000 51.11402  ? 430 ILE B C     1 
ATOM   6908 O  O     . ILE B 1 430 ? -10.11300 -6.95800  79.26000  1.000 74.42998  ? 430 ILE B O     1 
ATOM   6909 C  CB    . ILE B 1 430 ? -9.89700  -4.26600  77.30500  1.000 37.16498  ? 430 ILE B CB    1 
ATOM   6910 C  CG1   . ILE B 1 430 ? -9.06300  -3.81200  76.10400  1.000 37.23078  ? 430 ILE B CG1   1 
ATOM   6911 C  CG2   . ILE B 1 430 ? -9.16800  -3.98000  78.61800  1.000 35.29371  ? 430 ILE B CG2   1 
ATOM   6912 C  CD1   . ILE B 1 430 ? -8.90100  -2.30100  76.02500  1.000 38.63095  ? 430 ILE B CD1   1 
ATOM   6913 N  N     . GLU B 1 431 ? -12.10800 -6.07200  78.73100  1.000 84.40486  ? 431 GLU B N     1 
ATOM   6914 C  CA    . GLU B 1 431 ? -12.74900 -6.55900  79.94400  1.000 122.42257 ? 431 GLU B CA    1 
ATOM   6915 C  C     . GLU B 1 431 ? -13.66500 -7.73700  79.64100  1.000 107.09442 ? 431 GLU B C     1 
ATOM   6916 O  O     . GLU B 1 431 ? -14.84400 -7.72400  80.00400  1.000 101.45953 ? 431 GLU B O     1 
ATOM   6917 C  CB    . GLU B 1 431 ? -13.53000 -5.42700  80.61400  1.000 145.13056 ? 431 GLU B CB    1 
ATOM   6918 C  CG    . GLU B 1 431 ? -12.64900 -4.28800  81.08300  1.000 136.84272 ? 431 GLU B CG    1 
ATOM   6919 C  CD    . GLU B 1 431 ? -11.54200 -4.76900  82.00000  1.000 140.16681 ? 431 GLU B CD    1 
ATOM   6920 O  OE1   . GLU B 1 431 ? -11.80100 -5.66900  82.82800  1.000 137.44279 ? 431 GLU B OE1   1 
ATOM   6921 O  OE2   . GLU B 1 431 ? -10.40700 -4.26000  81.88400  1.000 104.25724 ? 431 GLU B OE2   1 
ATOM   6922 N  N     . SER B 1 432 ? -13.13200 -8.74600  78.95000  1.000 127.69952 ? 432 SER B N     1 
ATOM   6923 C  CA    . SER B 1 432 ? -13.83100 -10.00800 78.73700  1.000 130.58145 ? 432 SER B CA    1 
ATOM   6924 C  C     . SER B 1 432 ? -12.95900 -11.18800 79.15000  1.000 162.59055 ? 432 SER B C     1 
ATOM   6925 O  O     . SER B 1 432 ? -13.36800 -12.03200 79.95500  1.000 144.94633 ? 432 SER B O     1 
ATOM   6926 C  CB    . SER B 1 432 ? -14.24500 -10.14700 77.27300  1.000 116.66136 ? 432 SER B CB    1 
ATOM   6927 O  OG    . SER B 1 432 ? -14.82900 -11.41900 77.02600  1.000 112.48980 ? 432 SER B OG    1 
ATOM   6928 N  N     . HIS B 1 433 ? -11.76100 -11.25400 78.58300  1.000 195.56819 ? 433 HIS B N     1 
ATOM   6929 C  CA    . HIS B 1 433 ? -10.75400 -12.23000 78.97100  1.000 161.72992 ? 433 HIS B CA    1 
ATOM   6930 C  C     . HIS B 1 433 ? -10.12900 -11.82500 80.30100  1.000 142.96451 ? 433 HIS B C     1 
ATOM   6931 O  O     . HIS B 1 433 ? -10.24900 -10.67300 80.73000  1.000 123.85169 ? 433 HIS B O     1 
ATOM   6932 C  CB    . HIS B 1 433 ? -9.67500  -12.35300 77.88800  1.000 138.62715 ? 433 HIS B CB    1 
ATOM   6933 C  CG    . HIS B 1 433 ? -10.15000 -13.00500 76.62600  1.000 148.77836 ? 433 HIS B CG    1 
ATOM   6934 N  ND1   . HIS B 1 433 ? -10.66900 -12.29600 75.56400  1.000 143.19348 ? 433 HIS B ND1   1 
ATOM   6935 C  CD2   . HIS B 1 433 ? -10.17800 -14.30800 76.25600  1.000 133.79499 ? 433 HIS B CD2   1 
ATOM   6936 C  CE1   . HIS B 1 433 ? -10.99800 -13.13300 74.59500  1.000 126.58623 ? 433 HIS B CE1   1 
ATOM   6937 N  NE2   . HIS B 1 433 ? -10.70900 -14.36000 74.99000  1.000 127.27579 ? 433 HIS B NE2   1 
ATOM   6938 N  N     . THR C 2 5   ? 7.83600   -21.63200 15.91800  1.000 82.34145  ? 526 THR C N     1 
ATOM   6939 C  CA    . THR C 2 5   ? 9.29200   -21.43000 16.14600  1.000 72.34025  ? 526 THR C CA    1 
ATOM   6940 C  C     . THR C 2 5   ? 10.07300  -21.91600 14.92000  1.000 74.24574  ? 526 THR C C     1 
ATOM   6941 O  O     . THR C 2 5   ? 10.26900  -23.14100 14.79300  1.000 98.65657  ? 526 THR C O     1 
ATOM   6942 C  CB    . THR C 2 5   ? 9.75400   -22.13700 17.42700  1.000 61.12838  ? 526 THR C CB    1 
ATOM   6943 O  OG1   . THR C 2 5   ? 11.12900  -22.49100 17.27000  1.000 81.88087  ? 526 THR C OG1   1 
ATOM   6944 C  CG2   . THR C 2 5   ? 8.94000   -23.37200 17.74400  1.000 71.71123  ? 526 THR C CG2   1 
ATOM   6945 N  N     . LEU C 2 6   ? 10.49700  -20.98500 14.05900  1.000 89.82656  ? 527 LEU C N     1 
ATOM   6946 C  CA    . LEU C 2 6   ? 11.24700  -21.32400 12.86100  1.000 71.61648  ? 527 LEU C CA    1 
ATOM   6947 C  C     . LEU C 2 6   ? 12.49800  -20.48700 12.63700  1.000 58.81758  ? 527 LEU C C     1 
ATOM   6948 O  O     . LEU C 2 6   ? 13.38700  -20.93900 11.90700  1.000 70.07946  ? 527 LEU C O     1 
ATOM   6949 C  CB    . LEU C 2 6   ? 10.35200  -21.19500 11.61700  1.000 82.76519  ? 527 LEU C CB    1 
ATOM   6950 C  CG    . LEU C 2 6   ? 9.23500   -22.21900 11.42400  1.000 93.77967  ? 527 LEU C CG    1 
ATOM   6951 C  CD1   . LEU C 2 6   ? 7.99900   -21.55500 10.83400  1.000 94.16392  ? 527 LEU C CD1   1 
ATOM   6952 C  CD2   . LEU C 2 6   ? 9.70200   -23.36200 10.53100  1.000 73.61935  ? 527 LEU C CD2   1 
ATOM   6953 N  N     . LYS C 2 7   ? 12.59800  -19.29800 13.23000  1.000 38.79413  ? 528 LYS C N     1 
ATOM   6954 C  CA    . LYS C 2 7   ? 13.67700  -18.37800 12.88400  1.000 37.67031  ? 528 LYS C CA    1 
ATOM   6955 C  C     . LYS C 2 7   ? 15.04600  -18.99000 13.17500  1.000 38.72043  ? 528 LYS C C     1 
ATOM   6956 O  O     . LYS C 2 7   ? 15.37700  -19.28100 14.33000  1.000 36.93601  ? 528 LYS C O     1 
ATOM   6957 C  CB    . LYS C 2 7   ? 13.50800  -17.05900 13.64400  1.000 35.68059  ? 528 LYS C CB    1 
ATOM   6958 C  CG    . LYS C 2 7   ? 12.38600  -16.15800 13.13700  1.000 33.68299  ? 528 LYS C CG    1 
ATOM   6959 C  CD    . LYS C 2 7   ? 12.37800  -14.83800 13.90100  1.000 32.39599  ? 528 LYS C CD    1 
ATOM   6960 C  CE    . LYS C 2 7   ? 11.14900  -13.99700 13.60400  1.000 31.85645  ? 528 LYS C CE    1 
ATOM   6961 N  NZ    . LYS C 2 7   ? 11.16400  -12.73900 14.40000  1.000 31.63537  ? 528 LYS C NZ    1 
ATOM   6962 N  N     . GLY C 2 8   ? 15.83900  -19.18600 12.11900  1.000 65.54470  ? 529 GLY C N     1 
ATOM   6963 C  CA    . GLY C 2 8   ? 17.19700  -19.68400 12.25400  1.000 66.96066  ? 529 GLY C CA    1 
ATOM   6964 C  C     . GLY C 2 8   ? 17.80300  -20.16500 10.94900  1.000 72.89821  ? 529 GLY C C     1 
ATOM   6965 O  O     . GLY C 2 8   ? 17.08300  -20.39200 9.97100   1.000 72.69819  ? 529 GLY C O     1 
ATOM   6966 N  N     . GLY C 2 9   ? 19.12500  -20.32900 10.91900  1.000 59.14657  ? 530 GLY C N     1 
ATOM   6967 C  CA    . GLY C 2 9   ? 19.80700  -20.81000 9.72600   1.000 64.50247  ? 530 GLY C CA    1 
ATOM   6968 C  C     . GLY C 2 9   ? 19.86300  -22.33100 9.69200   1.000 77.05134  ? 530 GLY C C     1 
ATOM   6969 O  O     . GLY C 2 9   ? 20.08600  -22.98200 10.71200  1.000 70.78743  ? 530 GLY C O     1 
ATOM   6970 N  N     . ALA C 2 10  ? 19.66200  -22.88200 8.49700   1.000 88.07372  ? 531 ALA C N     1 
ATOM   6971 C  CA    . ALA C 2 10  ? 19.54600  -24.32600 8.28500   1.000 95.02981  ? 531 ALA C CA    1 
ATOM   6972 C  C     . ALA C 2 10  ? 18.43500  -24.92800 9.14200   1.000 84.78648  ? 531 ALA C C     1 
ATOM   6973 O  O     . ALA C 2 10  ? 17.76800  -25.88000 8.73300   1.000 80.83074  ? 531 ALA C O     1 
ATOM   6974 C  CB    . ALA C 2 10  ? 20.87600  -25.02700 8.56300   1.000 88.16583  ? 531 ALA C CB    1 
ATOM   6975 N  N     . THR D 2 5   ? -8.64400  -1.37900  40.88400  1.000 104.70203 ? 526 THR D N     1 
ATOM   6976 C  CA    . THR D 2 5   ? -7.71600  -0.68100  41.81500  1.000 106.36012 ? 526 THR D CA    1 
ATOM   6977 C  C     . THR D 2 5   ? -8.43800  0.50900   42.45700  1.000 102.14909 ? 526 THR D C     1 
ATOM   6978 O  O     . THR D 2 5   ? -8.03900  1.65800   42.18200  1.000 97.08269  ? 526 THR D O     1 
ATOM   6979 C  CB    . THR D 2 5   ? -6.43600  -0.24000  41.09200  1.000 103.33871 ? 526 THR D CB    1 
ATOM   6980 O  OG1   . THR D 2 5   ? -6.78800  0.77100   40.14700  1.000 99.09609  ? 526 THR D OG1   1 
ATOM   6981 C  CG2   . THR D 2 5   ? -5.73600  -1.38100  40.38600  1.000 104.63886 ? 526 THR D CG2   1 
ATOM   6982 N  N     . LEU D 2 6   ? -9.46100  0.23400   43.27300  1.000 70.56372  ? 527 LEU D N     1 
ATOM   6983 C  CA    . LEU D 2 6   ? -10.24200 1.30300   43.95100  1.000 65.49733  ? 527 LEU D CA    1 
ATOM   6984 C  C     . LEU D 2 6   ? -9.41600  1.88100   45.10600  1.000 58.89654  ? 527 LEU D C     1 
ATOM   6985 O  O     . LEU D 2 6   ? -8.53500  1.16400   45.62000  1.000 69.11355  ? 527 LEU D O     1 
ATOM   6986 C  CB    . LEU D 2 6   ? -11.56000 0.71100   44.46000  1.000 63.00492  ? 527 LEU D CB    1 
ATOM   6987 C  CG    . LEU D 2 6   ? -12.63800 0.49900   43.39700  1.000 52.72211  ? 527 LEU D CG    1 
ATOM   6988 C  CD1   . LEU D 2 6   ? -12.40200 -0.79700  42.63700  1.000 58.42806  ? 527 LEU D CD1   1 
ATOM   6989 C  CD2   . LEU D 2 6   ? -14.02400 0.50600   44.02200  1.000 42.90778  ? 527 LEU D CD2   1 
ATOM   6990 N  N     . LYS D 2 7   ? -9.69900  3.13000   45.49000  1.000 53.08268  ? 528 LYS D N     1 
ATOM   6991 C  CA    . LYS D 2 7   ? -8.96800  3.80200   46.59800  1.000 56.63574  ? 528 LYS D CA    1 
ATOM   6992 C  C     . LYS D 2 7   ? -9.20300  3.02900   47.90100  1.000 63.48919  ? 528 LYS D C     1 
ATOM   6993 O  O     . LYS D 2 7   ? -10.31500 3.13300   48.45700  1.000 51.79305  ? 528 LYS D O     1 
ATOM   6994 C  CB    . LYS D 2 7   ? -9.42400  5.25800   46.73100  1.000 49.76386  ? 528 LYS D CB    1 
ATOM   6995 C  CG    . LYS D 2 7   ? -9.39000  6.07100   45.44300  1.000 43.12622  ? 528 LYS D CG    1 
ATOM   6996 C  CD    . LYS D 2 7   ? -10.19700 7.35000   45.52000  1.000 38.97836  ? 528 LYS D CD    1 
ATOM   6997 C  CE    . LYS D 2 7   ? -9.70900  8.41600   44.56200  1.000 45.38176  ? 528 LYS D CE    1 
ATOM   6998 N  NZ    . LYS D 2 7   ? -10.62700 9.57900   44.52000  1.000 38.22037  ? 528 LYS D NZ    1 
ATOM   6999 N  N     . GLY D 2 8   ? -8.19000  2.28800   48.36000  1.000 95.75885  ? 529 GLY D N     1 
ATOM   7000 C  CA    . GLY D 2 8   ? -8.29500  1.50000   49.60400  1.000 87.76315  ? 529 GLY D CA    1 
ATOM   7001 C  C     . GLY D 2 8   ? -7.25200  1.91900   50.62500  1.000 85.04178  ? 529 GLY D C     1 
ATOM   7002 O  O     . GLY D 2 8   ? -7.61900  2.70700   51.52000  1.000 96.75634  ? 529 GLY D O     1 
ATOM   7003 N  N     . ARG E 2 1   ? 25.66200  -32.23500 16.68200  1.000 54.00911  ? 522 ARG E N     1 
ATOM   7004 C  CA    . ARG E 2 1   ? 26.79300  -32.74700 17.48500  1.000 72.52185  ? 522 ARG E CA    1 
ATOM   7005 C  C     . ARG E 2 1   ? 27.03500  -34.22000 17.14800  1.000 70.97693  ? 522 ARG E C     1 
ATOM   7006 O  O     . ARG E 2 1   ? 26.29000  -35.04900 17.64900  1.000 63.41550  ? 522 ARG E O     1 
ATOM   7007 C  CB    . ARG E 2 1   ? 26.43800  -32.61300 18.96300  1.000 62.89438  ? 522 ARG E CB    1 
ATOM   7008 C  CG    . ARG E 2 1   ? 27.60600  -32.25900 19.86000  1.000 61.28366  ? 522 ARG E CG    1 
ATOM   7009 C  CD    . ARG E 2 1   ? 28.85900  -33.03200 19.57200  1.000 73.95097  ? 522 ARG E CD    1 
ATOM   7010 N  NE    . ARG E 2 1   ? 29.95500  -32.19100 19.99700  1.000 85.87345  ? 522 ARG E NE    1 
ATOM   7011 C  CZ    . ARG E 2 1   ? 30.47400  -32.19300 21.21400  1.000 86.97885  ? 522 ARG E CZ    1 
ATOM   7012 N  NH1   . ARG E 2 1   ? 29.99800  -33.01000 22.13500  1.000 73.11666  ? 522 ARG E NH1   1 
ATOM   7013 N  NH2   . ARG E 2 1   ? 31.47100  -31.37800 21.50500  1.000 81.43345  ? 522 ARG E NH2   1 
ATOM   7014 N  N     . MET E 2 2   ? 28.05700  -34.51300 16.34200  1.000 59.26237  ? 523 MET E N     1 
ATOM   7015 C  CA    . MET E 2 2   ? 28.36200  -35.88600 15.97200  1.000 57.49374  ? 523 MET E CA    1 
ATOM   7016 C  C     . MET E 2 2   ? 28.90100  -36.68800 17.16000  1.000 62.51013  ? 523 MET E C     1 
ATOM   7017 O  O     . MET E 2 2   ? 29.53500  -36.15200 18.07600  1.000 56.11199  ? 523 MET E O     1 
ATOM   7018 C  CB    . MET E 2 2   ? 29.36400  -35.90000 14.81300  1.000 47.63203  ? 523 MET E CB    1 
ATOM   7019 C  CG    . MET E 2 2   ? 30.76300  -35.39300 15.15900  1.000 52.12730  ? 523 MET E CG    1 
ATOM   7020 S  SD    . MET E 2 2   ? 31.85700  -35.26700 13.72400  1.000 44.31584  ? 523 MET E SD    1 
ATOM   7021 C  CE    . MET E 2 2   ? 31.19300  -33.81900 12.90100  1.000 38.33881  ? 523 MET E CE    1 
ATOM   7022 N  N     . LYS E 2 3   ? 28.63900  -37.99800 17.12500  1.000 63.75764  ? 524 LYS E N     1 
ATOM   7023 C  CA    . LYS E 2 3   ? 29.02100  -38.92800 18.19000  1.000 70.10314  ? 524 LYS E CA    1 
ATOM   7024 C  C     . LYS E 2 3   ? 30.39600  -39.52900 17.88600  1.000 67.66338  ? 524 LYS E C     1 
ATOM   7025 O  O     . LYS E 2 3   ? 30.55000  -40.71700 17.59500  1.000 66.98961  ? 524 LYS E O     1 
ATOM   7026 C  CB    . LYS E 2 3   ? 27.96200  -40.01400 18.34600  1.000 74.74317  ? 524 LYS E CB    1 
ATOM   7027 C  CG    . LYS E 2 3   ? 26.59900  -39.51400 18.80300  1.000 73.57461  ? 524 LYS E CG    1 
ATOM   7028 C  CD    . LYS E 2 3   ? 26.58400  -39.21300 20.29200  1.000 71.30592  ? 524 LYS E CD    1 
ATOM   7029 C  CE    . LYS E 2 3   ? 25.22500  -38.69200 20.73500  1.000 80.61493  ? 524 LYS E CE    1 
ATOM   7030 N  NZ    . LYS E 2 3   ? 24.88700  -37.39400 20.08400  1.000 73.44038  ? 524 LYS E NZ    1 
ATOM   7031 N  N     . LEU E 2 4   ? 31.41100  -38.67600 17.97400  1.000 66.91065  ? 525 LEU E N     1 
ATOM   7032 C  CA    . LEU E 2 4   ? 32.77900  -39.08400 17.67200  1.000 67.08436  ? 525 LEU E CA    1 
ATOM   7033 C  C     . LEU E 2 4   ? 33.71200  -38.87300 18.86400  1.000 72.86926  ? 525 LEU E C     1 
ATOM   7034 O  O     . LEU E 2 4   ? 34.04400  -37.74100 19.21600  1.000 79.19371  ? 525 LEU E O     1 
ATOM   7035 C  CB    . LEU E 2 4   ? 33.29400  -38.32000 16.45000  1.000 64.02873  ? 525 LEU E CB    1 
ATOM   7036 C  CG    . LEU E 2 4   ? 34.75000  -38.50900 16.02200  1.000 61.25734  ? 525 LEU E CG    1 
ATOM   7037 C  CD1   . LEU E 2 4   ? 35.11900  -39.98300 15.93900  1.000 59.29658  ? 525 LEU E CD1   1 
ATOM   7038 C  CD2   . LEU E 2 4   ? 34.96600  -37.83100 14.68500  1.000 47.63203  ? 525 LEU E CD2   1 
ATOM   7039 N  N     . ARG F 2 1   ? -11.37700 -9.55900  59.37600  1.000 58.15960  ? 522 ARG F N     1 
ATOM   7040 C  CA    . ARG F 2 1   ? -11.75400 -10.15400 60.65600  1.000 67.16595  ? 522 ARG F CA    1 
ATOM   7041 C  C     . ARG F 2 1   ? -11.26600 -11.60300 60.74200  1.000 72.29025  ? 522 ARG F C     1 
ATOM   7042 O  O     . ARG F 2 1   ? -11.77000 -12.47900 60.03700  1.000 61.79951  ? 522 ARG F O     1 
ATOM   7043 C  CB    . ARG F 2 1   ? -13.27600 -10.08800 60.85300  1.000 68.48190  ? 522 ARG F CB    1 
ATOM   7044 C  CG    . ARG F 2 1   ? -13.76200 -10.47000 62.25000  1.000 72.54817  ? 522 ARG F CG    1 
ATOM   7045 C  CD    . ARG F 2 1   ? -13.38900 -9.40400  63.27300  1.000 88.44745  ? 522 ARG F CD    1 
ATOM   7046 N  NE    . ARG F 2 1   ? -13.69400 -9.78600  64.65400  1.000 92.69796  ? 522 ARG F NE    1 
ATOM   7047 C  CZ    . ARG F 2 1   ? -12.88000 -10.49500 65.43400  1.000 93.75861  ? 522 ARG F CZ    1 
ATOM   7048 N  NH1   . ARG F 2 1   ? -11.71300 -10.92100 64.96600  1.000 80.13856  ? 522 ARG F NH1   1 
ATOM   7049 N  NH2   . ARG F 2 1   ? -13.23000 -10.78600 66.68100  1.000 73.83517  ? 522 ARG F NH2   1 
ATOM   7050 N  N     . MET F 2 2   ? -10.27700 -11.84400 61.60100  1.000 71.73755  ? 523 MET F N     1 
ATOM   7051 C  CA    . MET F 2 2   ? -9.78000  -13.19500 61.82400  1.000 64.34456  ? 523 MET F CA    1 
ATOM   7052 C  C     . MET F 2 2   ? -10.83900 -14.03800 62.52400  1.000 57.86746  ? 523 MET F C     1 
ATOM   7053 O  O     . MET F 2 2   ? -11.65300 -13.53200 63.30100  1.000 61.29419  ? 523 MET F O     1 
ATOM   7054 C  CB    . MET F 2 2   ? -8.49500  -13.16700 62.65800  1.000 63.00755  ? 523 MET F CB    1 
ATOM   7055 C  CG    . MET F 2 2   ? -8.69000  -12.70300 64.10200  1.000 66.88170  ? 523 MET F CG    1 
ATOM   7056 S  SD    . MET F 2 2   ? -7.15500  -12.51600 65.03800  1.000 65.52628  ? 523 MET F SD    1 
ATOM   7057 C  CE    . MET F 2 2   ? -6.33800  -11.21200 64.11300  1.000 58.06222  ? 523 MET F CE    1 
ATOM   7058 N  N     . LYS F 2 3   ? -10.82700 -15.34000 62.24000  1.000 72.15076  ? 524 LYS F N     1 
ATOM   7059 C  CA    . LYS F 2 3   ? -11.80500 -16.26100 62.82400  1.000 74.96688  ? 524 LYS F CA    1 
ATOM   7060 C  C     . LYS F 2 3   ? -11.29600 -16.82800 64.15100  1.000 73.44038  ? 524 LYS F C     1 
ATOM   7061 O  O     . LYS F 2 3   ? -11.10700 -18.03300 64.31900  1.000 76.52233  ? 524 LYS F O     1 
ATOM   7062 C  CB    . LYS F 2 3   ? -12.14300 -17.37600 61.83900  1.000 73.55092  ? 524 LYS F CB    1 
ATOM   7063 C  CG    . LYS F 2 3   ? -12.96000 -16.93900 60.63000  1.000 76.99081  ? 524 LYS F CG    1 
ATOM   7064 C  CD    . LYS F 2 3   ? -13.91000 -18.04900 60.19300  1.000 83.50475  ? 524 LYS F CD    1 
ATOM   7065 C  CE    . LYS F 2 3   ? -14.54700 -17.75700 58.84300  1.000 82.36777  ? 524 LYS F CE    1 
ATOM   7066 N  NZ    . LYS F 2 3   ? -13.58700 -17.95300 57.72100  1.000 83.73636  ? 524 LYS F NZ    1 
ATOM   7067 N  N     . LEU F 2 4   ? -11.07800 -15.92700 65.10700  1.000 59.28342  ? 525 LEU F N     1 
ATOM   7068 C  CA    . LEU F 2 4   ? -10.70100 -16.28700 66.46800  1.000 67.09489  ? 525 LEU F CA    1 
ATOM   7069 C  C     . LEU F 2 4   ? -11.92100 -16.12200 67.36600  1.000 79.98591  ? 525 LEU F C     1 
ATOM   7070 O  O     . LEU F 2 4   ? -12.58600 -15.08000 67.33100  1.000 121.46193 ? 525 LEU F O     1 
ATOM   7071 C  CB    . LEU F 2 4   ? -9.52600  -15.43400 66.95800  1.000 62.84964  ? 525 LEU F CB    1 
ATOM   7072 C  CG    . LEU F 2 4   ? -8.71900  -15.90800 68.17300  1.000 65.78157  ? 525 LEU F CG    1 
ATOM   7073 C  CD1   . LEU F 2 4   ? -8.59800  -17.42400 68.20400  1.000 65.53417  ? 525 LEU F CD1   1 
ATOM   7074 C  CD2   . LEU F 2 4   ? -7.33400  -15.27300 68.16900  1.000 58.02538  ? 525 LEU F CD2   1 
ATOM   7075 N  N     . THR F 2 5   ? -12.20200 -17.15100 68.17500  1.000 105.95481 ? 526 THR F N     1 
ATOM   7076 C  CA    . THR F 2 5   ? -13.52900 -17.31400 68.76800  1.000 115.52964 ? 526 THR F CA    1 
ATOM   7077 C  C     . THR F 2 5   ? -13.91100 -16.15600 69.68000  1.000 122.01200 ? 526 THR F C     1 
ATOM   7078 O  O     . THR F 2 5   ? -15.10500 -15.87000 69.84200  1.000 138.49555 ? 526 THR F O     1 
ATOM   7079 C  CB    . THR F 2 5   ? -13.60000 -18.63000 69.54500  1.000 105.32052 ? 526 THR F CB    1 
ATOM   7080 O  OG1   . THR F 2 5   ? -13.00400 -19.67500 68.76800  1.000 107.40498 ? 526 THR F OG1   1 
ATOM   7081 C  CG2   . THR F 2 5   ? -15.05000 -19.00000 69.84100  1.000 102.19383 ? 526 THR F CG2   1 
ATOM   7082 N  N     . LEU F 2 6   ? -12.92800 -15.49200 70.28200  1.000 83.98112  ? 527 LEU F N     1 
ATOM   7083 C  CA    . LEU F 2 6   ? -13.19100 -14.39600 71.20600  1.000 91.68468  ? 527 LEU F CA    1 
ATOM   7084 C  C     . LEU F 2 6   ? -13.97100 -14.93200 72.40500  1.000 92.87166  ? 527 LEU F C     1 
ATOM   7085 O  O     . LEU F 2 6   ? -13.40500 -15.57400 73.29100  1.000 70.34001  ? 527 LEU F O     1 
ATOM   7086 C  CB    . LEU F 2 6   ? -13.96000 -13.26800 70.50600  1.000 91.99787  ? 527 LEU F CB    1 
ATOM   7087 C  CG    . LEU F 2 6   ? -13.80800 -11.82500 70.99500  1.000 108.68408 ? 527 LEU F CG    1 
ATOM   7088 C  CD1   . LEU F 2 6   ? -14.72300 -10.88400 70.19100  1.000 95.15878  ? 527 LEU F CD1   1 
ATOM   7089 C  CD2   . LEU F 2 6   ? -14.01500 -11.66700 72.51500  1.000 111.26860 ? 527 LEU F CD2   1 
HETATM 7090 N  N     . SAH G 3 .   ? 8.10100   -6.10100  12.36400  1.000 24.38977  ? 501 SAH A N     1 
HETATM 7091 C  CA    . SAH G 3 .   ? 7.70200   -7.03900  13.40800  1.000 24.44767  ? 501 SAH A CA    1 
HETATM 7092 C  CB    . SAH G 3 .   ? 8.92000   -7.56600  14.16300  1.000 27.57436  ? 501 SAH A CB    1 
HETATM 7093 C  CG    . SAH G 3 .   ? 9.53700   -8.81600  13.53200  1.000 24.31344  ? 501 SAH A CG    1 
HETATM 7094 S  SD    . SAH G 3 .   ? 8.49400   -10.28300 13.74400  1.000 25.31093  ? 501 SAH A SD    1 
HETATM 7095 C  C     . SAH G 3 .   ? 6.70100   -6.39500  14.36300  1.000 31.16689  ? 501 SAH A C     1 
HETATM 7096 O  O     . SAH G 3 .   ? 6.22100   -5.28100  14.13600  1.000 29.16929  ? 501 SAH A O     1 
HETATM 7097 O  OXT   . SAH G 3 .   ? 6.31600   -6.99500  15.36500  1.000 30.34048  ? 501 SAH A OXT   1 
HETATM 7098 C  "C5'" . SAH G 3 .   ? 8.41300   -10.73800 11.98600  1.000 22.07633  ? 501 SAH A "C5'" 1 
HETATM 7099 C  "C4'" . SAH G 3 .   ? 7.46700   -9.90100  11.13200  1.000 23.59493  ? 501 SAH A "C4'" 1 
HETATM 7100 O  "O4'" . SAH G 3 .   ? 8.04700   -8.64100  10.81900  1.000 25.61623  ? 501 SAH A "O4'" 1 
HETATM 7101 C  "C3'" . SAH G 3 .   ? 7.20100   -10.55700 9.78700   1.000 24.32397  ? 501 SAH A "C3'" 1 
HETATM 7102 O  "O3'" . SAH G 3 .   ? 6.12100   -11.46100 9.85900   1.000 23.83180  ? 501 SAH A "O3'" 1 
HETATM 7103 C  "C2'" . SAH G 3 .   ? 6.88700   -9.37800  8.90300   1.000 22.87116  ? 501 SAH A "C2'" 1 
HETATM 7104 O  "O2'" . SAH G 3 .   ? 5.55800   -8.99700  9.12600   1.000 28.89557  ? 501 SAH A "O2'" 1 
HETATM 7105 C  "C1'" . SAH G 3 .   ? 7.77100   -8.28900  9.47500   1.000 28.39288  ? 501 SAH A "C1'" 1 
HETATM 7106 N  N9    . SAH G 3 .   ? 9.03400   -8.19800  8.72300   1.000 23.88707  ? 501 SAH A N9    1 
HETATM 7107 C  C8    . SAH G 3 .   ? 10.24800  -8.72000  9.09100   1.000 21.51837  ? 501 SAH A C8    1 
HETATM 7108 N  N7    . SAH G 3 .   ? 11.14600  -8.41700  8.12800   1.000 23.14488  ? 501 SAH A N7    1 
HETATM 7109 C  C5    . SAH G 3 .   ? 10.52600  -7.71100  7.14900   1.000 23.14488  ? 501 SAH A C5    1 
HETATM 7110 C  C6    . SAH G 3 .   ? 10.95600  -7.15800  5.94400   1.000 28.83504  ? 501 SAH A C6    1 
HETATM 7111 N  N6    . SAH G 3 .   ? 12.21900  -7.26500  5.54800   1.000 23.36596  ? 501 SAH A N6    1 
HETATM 7112 N  N1    . SAH G 3 .   ? 10.05900  -6.48600  5.14300   1.000 20.94198  ? 501 SAH A N1    1 
HETATM 7113 C  C2    . SAH G 3 .   ? 8.74700   -6.35900  5.52700   1.000 24.97405  ? 501 SAH A C2    1 
HETATM 7114 N  N3    . SAH G 3 .   ? 8.33400   -6.90700  6.72100   1.000 25.32146  ? 501 SAH A N3    1 
HETATM 7115 C  C4    . SAH G 3 .   ? 9.19700   -7.56900  7.51800   1.000 27.33222  ? 501 SAH A C4    1 
HETATM 7116 ZN ZN    . ZN  H 4 .   ? 10.65000  -35.85900 35.58300  1.000 38.59147  2 502 ZN  A ZN    1 
HETATM 7117 ZN ZN    . ZN  I 4 .   ? 16.17200  -10.42700 1.02000   1.000 26.17945  2 503 ZN  A ZN    1 
HETATM 7118 ZN ZN    . ZN  J 4 .   ? 22.26400  -27.14900 34.13000  1.000 45.23437  2 504 ZN  A ZN    1 
HETATM 7119 N  N     . SAH K 3 .   ? -9.18700  16.48600  41.03700  1.000 37.04392  ? 501 SAH B N     1 
HETATM 7120 C  CA    . SAH K 3 .   ? -10.30000 15.56300  40.81700  1.000 38.85203  ? 501 SAH B CA    1 
HETATM 7121 C  CB    . SAH K 3 .   ? -10.84600 15.10200  42.15600  1.000 39.06521  ? 501 SAH B CB    1 
HETATM 7122 C  CG    . SAH K 3 .   ? -10.13200 13.86500  42.70100  1.000 37.50713  ? 501 SAH B CG    1 
HETATM 7123 S  SD    . SAH K 3 .   ? -10.58300 12.37700  41.77100  1.000 36.70966  ? 501 SAH B SD    1 
HETATM 7124 C  C     . SAH K 3 .   ? -11.40700 16.18300  39.96800  1.000 49.31644  ? 501 SAH B C     1 
HETATM 7125 O  O     . SAH K 3 .   ? -11.28300 17.30400  39.47000  1.000 47.51096  ? 501 SAH B O     1 
HETATM 7126 O  OXT   . SAH K 3 .   ? -12.45000 15.56800  39.75100  1.000 45.30017  ? 501 SAH B OXT   1 
HETATM 7127 C  "C5'" . SAH K 3 .   ? -8.90000  11.81500  41.38700  1.000 39.08627  ? 501 SAH B "C5'" 1 
HETATM 7128 C  "C4'" . SAH K 3 .   ? -8.21300  12.56700  40.24900  1.000 37.00444  ? 501 SAH B "C4'" 1 
HETATM 7129 O  "O4'" . SAH K 3 .   ? -7.74900  13.82500  40.70700  1.000 37.03339  ? 501 SAH B "O4'" 1 
HETATM 7130 C  "C3'" . SAH K 3 .   ? -6.97000  11.86400  39.72900  1.000 39.45210  ? 501 SAH B "C3'" 1 
HETATM 7131 O  "O3'" . SAH K 3 .   ? -7.27300  10.95200  38.69200  1.000 40.30746  ? 501 SAH B "O3'" 1 
HETATM 7132 C  "C2'" . SAH K 3 .   ? -6.11000  13.01000  39.23500  1.000 42.87356  ? 501 SAH B "C2'" 1 
HETATM 7133 O  "O2'" . SAH K 3 .   ? -6.50200  13.40300  37.94400  1.000 43.94737  ? 501 SAH B "O2'" 1 
HETATM 7134 C  "C1'" . SAH K 3 .   ? -6.46700  14.13700  40.18300  1.000 38.35197  ? 501 SAH B "C1'" 1 
HETATM 7135 N  N9    . SAH K 3 .   ? -5.52300  14.26800  41.30600  1.000 37.67294  ? 501 SAH B N9    1 
HETATM 7136 C  C8    . SAH K 3 .   ? -5.73600  13.79300  42.57000  1.000 32.31440  ? 501 SAH B C8    1 
HETATM 7137 N  N7    . SAH K 3 .   ? -4.66900  14.11300  43.33200  1.000 32.57233  ? 501 SAH B N7    1 
HETATM 7138 C  C5    . SAH K 3 .   ? -3.77500  14.78000  42.57700  1.000 33.17766  ? 501 SAH B C5    1 
HETATM 7139 C  C6    . SAH K 3 .   ? -2.52900  15.31700  42.87400  1.000 32.92500  ? 501 SAH B C6    1 
HETATM 7140 N  N6    . SAH K 3 .   ? -2.03300  15.21100  44.10400  1.000 30.47997  ? 501 SAH B N6    1 
HETATM 7141 N  N1    . SAH K 3 .   ? -1.81600  15.96200  41.88400  1.000 34.54625  ? 501 SAH B N1    1 
HETATM 7142 C  C2    . SAH K 3 .   ? -2.35000  16.06100  40.61300  1.000 35.01209  ? 501 SAH B C2    1 
HETATM 7143 N  N3    . SAH K 3 .   ? -3.58700  15.52300  40.32800  1.000 35.05420  ? 501 SAH B N3    1 
HETATM 7144 C  C4    . SAH K 3 .   ? -4.29700  14.89400  41.29500  1.000 35.19896  ? 501 SAH B C4    1 
HETATM 7145 ZN ZN    . ZN  L 4 .   ? -31.61800 -13.72900 46.50100  1.000 64.15243  2 502 ZN  B ZN    1 
HETATM 7146 ZN ZN    . ZN  M 4 .   ? 3.25500   12.19800  47.39400  1.000 30.69315  2 503 ZN  B ZN    1 
HETATM 7147 ZN ZN    . ZN  N 4 .   ? -28.76100 -4.90600  57.88800  1.000 60.81255  2 504 ZN  B ZN    1 
HETATM 7148 O  O     . HOH O 5 .   ? 4.42300   -13.27000 31.08200  1.000 51.34000  ? 601 HOH A O     1 
HETATM 7149 O  O     . HOH O 5 .   ? 18.30800  -17.91900 29.56700  1.000 43.04000  ? 602 HOH A O     1 
HETATM 7150 O  O     . HOH O 5 .   ? 38.02300  -32.61200 17.64500  1.000 52.29000  ? 603 HOH A O     1 
HETATM 7151 O  O     . HOH O 5 .   ? 24.42600  -6.76000  -5.51700  1.000 47.63000  ? 604 HOH A O     1 
HETATM 7152 O  O     . HOH O 5 .   ? 3.30400   -5.26100  12.90500  1.000 30.00000  ? 605 HOH A O     1 
HETATM 7153 O  O     . HOH O 5 .   ? 34.92800  -27.69100 -1.34300  1.000 35.78000  ? 606 HOH A O     1 
HETATM 7154 O  O     . HOH O 5 .   ? 38.72300  -37.08500 17.86700  1.000 47.58000  ? 607 HOH A O     1 
HETATM 7155 O  O     . HOH O 5 .   ? 28.69600  -21.84500 -8.17800  1.000 46.93000  ? 608 HOH A O     1 
HETATM 7156 O  O     . HOH O 5 .   ? 30.24300  -23.51200 14.52900  1.000 43.62000  ? 609 HOH A O     1 
HETATM 7157 O  O     . HOH O 5 .   ? 24.70900  -17.46100 6.76800   1.000 39.01000  ? 610 HOH A O     1 
HETATM 7158 O  O     . HOH O 5 .   ? -8.37700  -29.32700 28.58700  1.000 53.12000  ? 611 HOH A O     1 
HETATM 7159 O  O     . HOH O 5 .   ? -11.74300 -19.87700 17.86300  1.000 30.00000  ? 612 HOH A O     1 
HETATM 7160 O  O     . HOH O 5 .   ? 9.19100   -28.28000 -18.59000 1.000 53.57000  ? 613 HOH A O     1 
HETATM 7161 O  O     . HOH O 5 .   ? 16.46700  -30.97400 -17.38900 1.000 49.64000  ? 614 HOH A O     1 
HETATM 7162 O  O     . HOH O 5 .   ? 16.31700  8.23400   16.57300  1.000 47.58000  ? 615 HOH A O     1 
HETATM 7163 O  O     . HOH O 5 .   ? 14.08900  -33.95000 18.79800  1.000 43.59000  ? 616 HOH A O     1 
HETATM 7164 O  O     . HOH O 5 .   ? 16.01500  -8.50800  26.80700  1.000 58.54000  ? 617 HOH A O     1 
HETATM 7165 O  O     . HOH O 5 .   ? 16.05300  -21.73700 -8.31900  1.000 47.17000  ? 618 HOH A O     1 
HETATM 7166 O  O     . HOH O 5 .   ? 42.02500  -17.12800 18.70000  1.000 47.58000  ? 619 HOH A O     1 
HETATM 7167 O  O     . HOH O 5 .   ? 24.82900  -30.56000 12.06800  1.000 55.00000  ? 620 HOH A O     1 
HETATM 7168 O  O     . HOH O 5 .   ? -10.453   -25.182   11.994    1.000 51.11000  ? 621 HOH A O     1 
HETATM 7169 O  O     . HOH O 5 .   ? 26.57800  -32.02700 8.03700   1.000 54.39000  ? 622 HOH A O     1 
HETATM 7170 O  O     . HOH O 5 .   ? 23.80300  -45.17300 -6.20200  1.000 47.63000  ? 623 HOH A O     1 
HETATM 7171 O  O     . HOH O 5 .   ? 26.30100  -10.02300 -3.24200  1.000 55.15000  ? 624 HOH A O     1 
HETATM 7172 O  O     . HOH O 5 .   ? 33.12000  -10.58400 18.90400  1.000 44.31000  ? 625 HOH A O     1 
HETATM 7173 O  O     . HOH O 5 .   ? 6.25400   -9.68900  16.59700  1.000 40.48000  ? 626 HOH A O     1 
HETATM 7174 O  O     . HOH O 5 .   ? 31.27200  -17.03900 3.48600   1.000 41.68000  ? 627 HOH A O     1 
HETATM 7175 O  O     . HOH O 5 .   ? 25.11500  -30.89800 21.00400  1.000 47.63000  ? 628 HOH A O     1 
HETATM 7176 O  O     . HOH O 5 .   ? 25.81000  -13.50400 18.52900  1.000 35.89000  ? 629 HOH A O     1 
HETATM 7177 O  O     . HOH O 5 .   ? 11.67100  0.04900   6.44300   1.000 44.55000  ? 630 HOH A O     1 
HETATM 7178 O  O     . HOH O 5 .   ? 13.03700  -32.05700 26.67100  1.000 42.72000  ? 631 HOH A O     1 
HETATM 7179 O  O     . HOH O 5 .   ? 5.55500   -18.97100 -0.70700  1.000 43.24000  ? 632 HOH A O     1 
HETATM 7180 O  O     . HOH O 5 .   ? 27.85900  -31.83300 -11.27300 1.000 47.63000  ? 633 HOH A O     1 
HETATM 7181 O  O     . HOH O 5 .   ? 12.31100  -29.78400 31.22300  1.000 50.15000  ? 634 HOH A O     1 
HETATM 7182 O  O     . HOH O 5 .   ? 26.71000  -17.21600 -4.66200  1.000 44.45000  ? 635 HOH A O     1 
HETATM 7183 O  O     . HOH O 5 .   ? 6.67600   -28.39900 27.68200  1.000 47.57000  ? 636 HOH A O     1 
HETATM 7184 O  O     . HOH O 5 .   ? -4.07300  -33.90200 29.60400  1.000 48.55000  ? 637 HOH A O     1 
HETATM 7185 O  O     . HOH O 5 .   ? 14.73500  -4.45600  12.88800  1.000 30.75000  ? 638 HOH A O     1 
HETATM 7186 O  O     . HOH O 5 .   ? 18.16300  -7.74200  27.74900  1.000 61.53000  ? 639 HOH A O     1 
HETATM 7187 O  O     . HOH O 5 .   ? 7.10000   -3.08900  25.23000  1.000 62.99000  ? 640 HOH A O     1 
HETATM 7188 O  O     . HOH O 5 .   ? 17.94900  -25.07800 5.48600   1.000 47.58000  ? 641 HOH A O     1 
HETATM 7189 O  O     . HOH O 5 .   ? 31.08600  -14.80400 24.46700  1.000 47.22000  ? 642 HOH A O     1 
HETATM 7190 O  O     . HOH O 5 .   ? 11.81400  -11.99300 -4.88700  1.000 48.88000  ? 643 HOH A O     1 
HETATM 7191 O  O     . HOH O 5 .   ? 1.53200   -16.33600 12.30900  1.000 41.96000  ? 644 HOH A O     1 
HETATM 7192 O  O     . HOH O 5 .   ? 25.92500  -11.67700 27.59300  1.000 51.51000  ? 645 HOH A O     1 
HETATM 7193 O  O     . HOH O 5 .   ? 11.56300  -23.50400 35.18700  1.000 49.01000  ? 646 HOH A O     1 
HETATM 7194 O  O     . HOH O 5 .   ? 18.16000  -33.87500 29.20200  1.000 30.00000  ? 647 HOH A O     1 
HETATM 7195 O  O     . HOH O 5 .   ? 22.07700  -25.68600 4.62900   1.000 47.63000  ? 648 HOH A O     1 
HETATM 7196 O  O     . HOH O 5 .   ? 27.54100  -45.12000 5.08300   1.000 50.60000  ? 649 HOH A O     1 
HETATM 7197 O  O     . HOH O 5 .   ? -9.41700  -24.40500 23.02200  1.000 41.45000  ? 650 HOH A O     1 
HETATM 7198 O  O     . HOH O 5 .   ? 15.80900  -29.44100 4.27600   1.000 47.58000  ? 651 HOH A O     1 
HETATM 7199 O  O     . HOH O 5 .   ? 23.53700  -27.72800 1.72600   1.000 44.35000  ? 652 HOH A O     1 
HETATM 7200 O  O     . HOH O 5 .   ? 4.08100   -24.40400 36.55400  1.000 30.00000  ? 653 HOH A O     1 
HETATM 7201 O  O     . HOH O 5 .   ? 40.08300  -44.42600 8.43900   1.000 47.58000  ? 654 HOH A O     1 
HETATM 7202 O  O     . HOH O 5 .   ? 23.00200  -13.54200 -10.28100 1.000 46.27000  ? 655 HOH A O     1 
HETATM 7203 O  O     . HOH O 5 .   ? 10.39000  -32.33900 30.16500  1.000 47.58000  ? 656 HOH A O     1 
HETATM 7204 O  O     . HOH O 5 .   ? 24.04600  -22.89100 21.22500  1.000 42.46000  ? 657 HOH A O     1 
HETATM 7205 O  O     . HOH O 5 .   ? 9.97700   -5.75800  2.51600   1.000 49.06000  ? 658 HOH A O     1 
HETATM 7206 O  O     . HOH O 5 .   ? 24.87600  -17.41700 10.01200  1.000 35.40000  ? 659 HOH A O     1 
HETATM 7207 O  O     . HOH O 5 .   ? 10.92400  -14.75500 20.26700  1.000 36.66000  ? 660 HOH A O     1 
HETATM 7208 O  O     . HOH O 5 .   ? 12.73100  -33.18300 39.08400  1.000 47.89000  ? 661 HOH A O     1 
HETATM 7209 O  O     . HOH O 5 .   ? -1.68800  -11.01100 22.49900  1.000 45.43000  ? 662 HOH A O     1 
HETATM 7210 O  O     . HOH O 5 .   ? -4.60100  -9.95600  12.20700  1.000 57.02000  ? 663 HOH A O     1 
HETATM 7211 O  O     . HOH O 5 .   ? 5.94500   -23.32700 -2.77800  1.000 38.62000  ? 664 HOH A O     1 
HETATM 7212 O  O     . HOH O 5 .   ? 39.33600  -16.56100 21.39000  1.000 56.34000  ? 665 HOH A O     1 
HETATM 7213 O  O     . HOH O 5 .   ? 25.93400  -21.43900 -15.03600 1.000 46.77000  ? 666 HOH A O     1 
HETATM 7214 O  O     . HOH O 5 .   ? 37.54700  -18.38500 8.86100   1.000 47.31000  ? 667 HOH A O     1 
HETATM 7215 O  O     . HOH O 5 .   ? -8.40900  -18.42700 6.84300   1.000 47.63000  ? 668 HOH A O     1 
HETATM 7216 O  O     . HOH O 5 .   ? 26.40300  -16.61200 22.31800  1.000 49.65000  ? 669 HOH A O     1 
HETATM 7217 O  O     . HOH O 5 .   ? 15.82700  1.30000   24.06000  1.000 52.75000  ? 670 HOH A O     1 
HETATM 7218 O  O     . HOH O 5 .   ? 15.53500  -16.57000 -7.91000  1.000 37.24000  ? 671 HOH A O     1 
HETATM 7219 O  O     . HOH O 5 .   ? 15.46300  -6.42300  4.51000   1.000 38.07000  ? 672 HOH A O     1 
HETATM 7220 O  O     . HOH O 5 .   ? 18.07800  -15.00800 13.41500  1.000 47.63000  ? 673 HOH A O     1 
HETATM 7221 O  O     . HOH O 5 .   ? 22.64800  -23.34200 23.53000  1.000 43.28000  ? 674 HOH A O     1 
HETATM 7222 O  O     . HOH O 5 .   ? 27.00600  -39.08500 15.16300  1.000 49.11000  ? 675 HOH A O     1 
HETATM 7223 O  O     . HOH O 5 .   ? 36.88200  -35.10600 16.53100  1.000 42.29000  ? 676 HOH A O     1 
HETATM 7224 O  O     . HOH O 5 .   ? 13.81100  -11.22100 14.93400  1.000 42.88000  ? 677 HOH A O     1 
HETATM 7225 O  O     . HOH O 5 .   ? 22.84200  -46.96400 -0.36500  1.000 47.57000  ? 678 HOH A O     1 
HETATM 7226 O  O     . HOH O 5 .   ? 26.97200  -26.48000 8.34500   1.000 47.58000  ? 679 HOH A O     1 
HETATM 7227 O  O     . HOH O 5 .   ? 13.27800  -28.53900 28.21500  1.000 45.63000  ? 680 HOH A O     1 
HETATM 7228 O  O     . HOH O 5 .   ? 21.75200  -13.28500 10.93200  1.000 32.96000  ? 681 HOH A O     1 
HETATM 7229 O  O     . HOH O 5 .   ? 25.06100  -33.85500 -19.53800 1.000 47.58000  ? 682 HOH A O     1 
HETATM 7230 O  O     . HOH O 5 .   ? 20.88000  -14.96000 -4.19600  1.000 41.97000  ? 683 HOH A O     1 
HETATM 7231 O  O     . HOH O 5 .   ? 13.15100  -6.04100  2.95400   1.000 41.74000  ? 684 HOH A O     1 
HETATM 7232 O  O     . HOH O 5 .   ? 12.77500  -30.70900 37.30000  1.000 40.82000  ? 685 HOH A O     1 
HETATM 7233 O  O     . HOH O 5 .   ? 10.75800  -31.94200 21.30800  1.000 39.70000  ? 686 HOH A O     1 
HETATM 7234 O  O     . HOH O 5 .   ? 23.66200  -36.36000 11.55200  1.000 54.80000  ? 687 HOH A O     1 
HETATM 7235 O  O     . HOH O 5 .   ? 15.57600  -32.49100 1.95300   1.000 35.42000  ? 688 HOH A O     1 
HETATM 7236 O  O     . HOH O 5 .   ? 19.12500  -19.98600 37.45100  1.000 47.57000  ? 689 HOH A O     1 
HETATM 7237 O  O     . HOH O 5 .   ? 3.70100   -10.22300 27.47300  1.000 43.91000  ? 690 HOH A O     1 
HETATM 7238 O  O     . HOH O 5 .   ? 20.19200  -36.00700 6.48700   1.000 43.45000  ? 691 HOH A O     1 
HETATM 7239 O  O     . HOH O 5 .   ? 5.78800   -7.68000  1.66900   1.000 47.57000  ? 692 HOH A O     1 
HETATM 7240 O  O     . HOH O 5 .   ? 21.20900  -27.21400 2.57600   1.000 42.84000  ? 693 HOH A O     1 
HETATM 7241 O  O     . HOH O 5 .   ? 17.92500  -21.05400 31.78700  1.000 44.89000  ? 694 HOH A O     1 
HETATM 7242 O  O     . HOH O 5 .   ? 22.29800  -9.63600  -11.22800 1.000 47.57000  ? 695 HOH A O     1 
HETATM 7243 O  O     . HOH O 5 .   ? -1.23900  -13.85900 23.14600  1.000 47.63000  ? 696 HOH A O     1 
HETATM 7244 O  O     . HOH O 5 .   ? 41.22000  -16.68700 15.44000  1.000 48.36000  ? 697 HOH A O     1 
HETATM 7245 O  O     . HOH O 5 .   ? -2.23600  -8.54900  12.65800  1.000 47.63000  ? 698 HOH A O     1 
HETATM 7246 O  O     . HOH O 5 .   ? 22.08400  -18.77900 6.59100   1.000 33.47000  ? 699 HOH A O     1 
HETATM 7247 O  O     . HOH O 5 .   ? 34.34700  -10.89400 21.91600  1.000 50.93000  ? 700 HOH A O     1 
HETATM 7248 O  O     . HOH O 5 .   ? 1.91000   -23.24000 1.95900   1.000 47.58000  ? 701 HOH A O     1 
HETATM 7249 O  O     . HOH O 5 .   ? 17.58500  -15.23400 -10.89700 1.000 48.72000  ? 702 HOH A O     1 
HETATM 7250 O  O     . HOH O 5 .   ? 41.93800  -28.35900 6.52700   1.000 38.42000  ? 703 HOH A O     1 
HETATM 7251 O  O     . HOH O 5 .   ? 33.00400  -44.95000 3.92500   1.000 56.14000  ? 704 HOH A O     1 
HETATM 7252 O  O     . HOH O 5 .   ? 21.91500  -6.75100  26.81300  1.000 45.94000  ? 705 HOH A O     1 
HETATM 7253 O  O     . HOH O 5 .   ? 31.03900  -30.75400 -15.23500 1.000 47.58000  ? 706 HOH A O     1 
HETATM 7254 O  O     . HOH O 5 .   ? 26.071    -14.945   -9.511    1.000 41.13000  ? 707 HOH A O     1 
HETATM 7255 O  O     . HOH O 5 .   ? 14.98200  -21.90000 6.17300   1.000 49.11000  ? 708 HOH A O     1 
HETATM 7256 O  O     . HOH O 5 .   ? 3.26500   -16.64300 40.71500  1.000 30.00000  ? 709 HOH A O     1 
HETATM 7257 O  O     . HOH O 5 .   ? 24.33400  -25.37400 24.91900  1.000 47.87000  ? 710 HOH A O     1 
HETATM 7258 O  O     . HOH O 5 .   ? -4.38200  -33.04900 17.59700  1.000 47.58000  ? 711 HOH A O     1 
HETATM 7259 O  O     . HOH O 5 .   ? 21.77200  8.84100   18.11100  1.000 47.58000  ? 712 HOH A O     1 
HETATM 7260 O  O     . HOH O 5 .   ? 12.31200  -19.72900 9.39100   1.000 47.58000  ? 713 HOH A O     1 
HETATM 7261 O  O     . HOH O 5 .   ? 12.81100  -23.80000 32.84800  1.000 45.83000  ? 714 HOH A O     1 
HETATM 7262 O  O     . HOH O 5 .   ? 25.36000  -41.82800 15.93300  1.000 40.13000  ? 715 HOH A O     1 
HETATM 7263 O  O     . HOH O 5 .   ? 11.83400  -7.83900  -3.85600  1.000 45.52000  ? 716 HOH A O     1 
HETATM 7264 O  O     . HOH O 5 .   ? 2.51300   -33.40800 28.79500  1.000 43.06000  ? 717 HOH A O     1 
HETATM 7265 O  O     . HOH O 5 .   ? 35.47500  -35.29000 -1.72100  1.000 46.10000  ? 718 HOH A O     1 
HETATM 7266 O  O     . HOH O 5 .   ? 43.48200  -22.28400 9.44500   1.000 47.57000  ? 719 HOH A O     1 
HETATM 7267 O  O     . HOH O 5 .   ? 9.80500   -2.02200  3.50200   1.000 47.58000  ? 720 HOH A O     1 
HETATM 7268 O  O     . HOH O 5 .   ? 9.48100   -17.78000 13.77600  1.000 47.58000  ? 721 HOH A O     1 
HETATM 7269 O  O     . HOH O 5 .   ? 18.96200  -4.83200  4.53400   1.000 43.49000  ? 722 HOH A O     1 
HETATM 7270 O  O     . HOH O 5 .   ? 12.63400  -34.42400 7.88800   1.000 47.58000  ? 723 HOH A O     1 
HETATM 7271 O  O     . HOH O 5 .   ? 20.63900  -1.30900  8.01800   1.000 43.02000  ? 724 HOH A O     1 
HETATM 7272 O  O     . HOH O 5 .   ? 6.60900   -28.41300 16.02900  1.000 48.47000  ? 725 HOH A O     1 
HETATM 7273 O  O     . HOH O 5 .   ? 19.76200  -4.54400  1.99000   1.000 34.40000  ? 726 HOH A O     1 
HETATM 7274 O  O     . HOH O 5 .   ? 21.89200  -21.27800 30.08500  1.000 45.36000  ? 727 HOH A O     1 
HETATM 7275 O  O     . HOH O 5 .   ? 24.51700  -25.42100 6.77100   1.000 51.54000  ? 728 HOH A O     1 
HETATM 7276 O  O     . HOH O 5 .   ? 31.63700  -9.66700  21.90800  1.000 51.73000  ? 729 HOH A O     1 
HETATM 7277 O  O     . HOH O 5 .   ? 11.38900  -28.48400 -1.76900  1.000 50.56000  ? 730 HOH A O     1 
HETATM 7278 O  O     . HOH O 5 .   ? 15.33300  -39.06700 23.61800  1.000 47.58000  ? 731 HOH A O     1 
HETATM 7279 O  O     . HOH O 5 .   ? 40.80500  -40.70700 16.83300  1.000 47.63000  ? 732 HOH A O     1 
HETATM 7280 O  O     . HOH O 5 .   ? 20.92900  -14.82700 13.21000  1.000 34.30000  ? 733 HOH A O     1 
HETATM 7281 O  O     . HOH O 5 .   ? -1.95000  -19.05800 31.34800  1.000 54.45000  ? 734 HOH A O     1 
HETATM 7282 O  O     . HOH O 5 .   ? 5.82700   0.95000   10.50800  1.000 50.64000  ? 735 HOH A O     1 
HETATM 7283 O  O     . HOH O 5 .   ? -1.92400  -33.15600 31.41700  1.000 44.88000  ? 736 HOH A O     1 
HETATM 7284 O  O     . HOH O 5 .   ? 24.21700  -32.50900 7.48800   1.000 49.06000  ? 737 HOH A O     1 
HETATM 7285 O  O     . HOH O 5 .   ? 25.71600  -22.43600 24.17600  1.000 43.19000  ? 738 HOH A O     1 
HETATM 7286 O  O     . HOH O 5 .   ? 12.87900  -36.42700 -14.72300 1.000 47.63000  ? 739 HOH A O     1 
HETATM 7287 O  O     . HOH O 5 .   ? 5.01100   -10.79400 30.67300  1.000 46.70000  ? 740 HOH A O     1 
HETATM 7288 O  O     . HOH O 5 .   ? 31.08400  -40.39000 0.45800   1.000 47.58000  ? 741 HOH A O     1 
HETATM 7289 O  O     . HOH O 5 .   ? 23.86400  -19.45000 -13.95600 1.000 47.58000  ? 742 HOH A O     1 
HETATM 7290 O  O     . HOH O 5 .   ? -7.23200  -13.96200 26.75000  1.000 47.58000  ? 743 HOH A O     1 
HETATM 7291 O  O     . HOH O 5 .   ? 20.25600  -29.74300 2.95900   1.000 52.33000  ? 744 HOH A O     1 
HETATM 7292 O  O     . HOH O 5 .   ? -10.09900 -13.80200 23.01400  1.000 57.45000  ? 745 HOH A O     1 
HETATM 7293 O  O     . HOH O 5 .   ? 24.61900  -2.05800  8.71400   1.000 49.39000  ? 746 HOH A O     1 
HETATM 7294 O  O     . HOH O 5 .   ? 11.61700  8.44200   15.38300  1.000 47.63000  ? 747 HOH A O     1 
HETATM 7295 O  O     . HOH O 5 .   ? 22.27600  -2.86000  24.97900  1.000 47.58000  ? 748 HOH A O     1 
HETATM 7296 O  O     . HOH O 5 .   ? 0.15100   -23.55600 35.17800  1.000 47.63000  ? 749 HOH A O     1 
HETATM 7297 O  O     . HOH O 5 .   ? 9.45700   5.57900   14.92400  1.000 43.13000  ? 750 HOH A O     1 
HETATM 7298 O  O     . HOH O 5 .   ? 19.43000  -30.84600 13.39800  1.000 47.58000  ? 751 HOH A O     1 
HETATM 7299 O  O     . HOH O 5 .   ? 14.52600  -24.74700 -2.12300  1.000 47.58000  ? 752 HOH A O     1 
HETATM 7300 O  O     . HOH O 5 .   ? 41.76300  -19.01100 14.38700  1.000 40.28000  ? 753 HOH A O     1 
HETATM 7301 O  O     . HOH O 5 .   ? 5.99900   -22.69600 0.49900   1.000 47.58000  ? 754 HOH A O     1 
HETATM 7302 O  O     . HOH O 5 .   ? 4.36300   -1.21900  8.37200   1.000 30.00000  ? 755 HOH A O     1 
HETATM 7303 O  O     . HOH O 5 .   ? 24.67700  -33.68000 21.80700  1.000 47.63000  ? 756 HOH A O     1 
HETATM 7304 O  O     . HOH O 5 .   ? -7.97000  -33.00500 22.90800  1.000 47.58000  ? 757 HOH A O     1 
HETATM 7305 O  O     . HOH O 5 .   ? 1.15200   -32.26400 18.59900  1.000 39.17000  ? 758 HOH A O     1 
HETATM 7306 O  O     . HOH O 5 .   ? 39.66500  -29.05900 4.38600   1.000 49.60000  ? 759 HOH A O     1 
HETATM 7307 O  O     . HOH O 5 .   ? 12.99900  -39.18300 26.44400  1.000 47.58000  ? 760 HOH A O     1 
HETATM 7308 O  O     . HOH O 5 .   ? 20.847    -49.270   6.470     1.000 52.53000  ? 761 HOH A O     1 
HETATM 7309 O  O     . HOH O 5 .   ? 35.64100  -19.76300 4.68400   1.000 52.44000  ? 762 HOH A O     1 
HETATM 7310 O  O     . HOH O 5 .   ? 12.16400  -33.88300 29.51900  1.000 50.24000  ? 763 HOH A O     1 
HETATM 7311 O  O     . HOH O 5 .   ? -7.62500  -27.09000 5.43600   1.000 57.59000  ? 764 HOH A O     1 
HETATM 7312 O  O     . HOH O 5 .   ? 5.39200   -6.36600  6.93300   1.000 47.69000  ? 765 HOH A O     1 
HETATM 7313 O  O     . HOH O 5 .   ? 8.16300   -32.03500 17.13200  1.000 42.81000  ? 766 HOH A O     1 
HETATM 7314 O  O     . HOH O 5 .   ? 19.91100  -2.48300  28.67400  1.000 47.58000  ? 767 HOH A O     1 
HETATM 7315 O  O     . HOH O 5 .   ? 4.40900   -19.43800 10.22700  1.000 47.63000  ? 768 HOH A O     1 
HETATM 7316 O  O     . HOH O 5 .   ? 48.03100  -27.19800 10.32400  1.000 56.40000  ? 769 HOH A O     1 
HETATM 7317 O  O     . HOH O 5 .   ? 25.74200  -11.16000 6.89400   1.000 39.27000  ? 770 HOH A O     1 
HETATM 7318 O  O     . HOH O 5 .   ? 15.68400  -20.82000 3.01400   1.000 48.09000  ? 771 HOH A O     1 
HETATM 7319 O  O     . HOH O 5 .   ? 5.27500   -6.48700  11.38800  1.000 41.41000  ? 772 HOH A O     1 
HETATM 7320 O  O     . HOH O 5 .   ? 11.26200  -22.45100 0.02200   1.000 47.58000  ? 773 HOH A O     1 
HETATM 7321 O  O     . HOH O 5 .   ? 15.61000  -22.99700 11.87700  1.000 47.63000  ? 774 HOH A O     1 
HETATM 7322 O  O     . HOH O 5 .   ? 25.09500  -20.71300 19.54700  1.000 33.89000  ? 775 HOH A O     1 
HETATM 7323 O  O     . HOH O 5 .   ? 41.97600  -41.68300 5.97700   1.000 47.58000  ? 776 HOH A O     1 
HETATM 7324 O  O     . HOH O 5 .   ? -1.19200  -9.38800  15.79600  1.000 47.58000  ? 777 HOH A O     1 
HETATM 7325 O  O     . HOH O 5 .   ? 31.15900  -6.06700  22.66500  1.000 52.99000  ? 778 HOH A O     1 
HETATM 7326 O  O     . HOH O 5 .   ? 7.79300   -32.81300 4.95400   1.000 47.57000  ? 779 HOH A O     1 
HETATM 7327 O  O     . HOH O 5 .   ? -3.80600  -14.58000 23.07600  1.000 43.80000  ? 780 HOH A O     1 
HETATM 7328 O  O     . HOH O 5 .   ? 1.48100   -24.50800 12.91100  1.000 53.61000  ? 781 HOH A O     1 
HETATM 7329 O  O     . HOH O 5 .   ? 46.54500  -30.42100 5.63200   1.000 47.63000  ? 782 HOH A O     1 
HETATM 7330 O  O     . HOH O 5 .   ? 38.78900  -13.56700 14.14800  1.000 59.93000  ? 783 HOH A O     1 
HETATM 7331 O  O     . HOH O 5 .   ? 15.93000  -17.32400 30.99900  1.000 50.83000  ? 784 HOH A O     1 
HETATM 7332 O  O     . HOH O 5 .   ? 33.99000  -2.97100  11.85700  1.000 47.58000  ? 785 HOH A O     1 
HETATM 7333 O  O     . HOH O 5 .   ? 23.64300  -7.80000  -3.18200  1.000 50.65000  ? 786 HOH A O     1 
HETATM 7334 O  O     . HOH O 5 .   ? 37.41600  -10.93500 11.53700  1.000 47.58000  ? 787 HOH A O     1 
HETATM 7335 O  O     . HOH O 5 .   ? 30.96900  -3.61200  7.33200   1.000 48.84000  ? 788 HOH A O     1 
HETATM 7336 O  O     . HOH O 5 .   ? 28.82900  -10.87300 3.09200   1.000 44.99000  ? 789 HOH A O     1 
HETATM 7337 O  O     . HOH O 5 .   ? 35.07600  -5.74700  17.99700  1.000 54.71000  ? 790 HOH A O     1 
HETATM 7338 O  O     . HOH O 5 .   ? 13.17700  -21.10900 33.06900  1.000 47.58000  ? 791 HOH A O     1 
HETATM 7339 O  O     . HOH O 5 .   ? 3.87500   -10.52100 0.47500   1.000 47.57000  ? 792 HOH A O     1 
HETATM 7340 O  O     . HOH O 5 .   ? 10.55800  6.10800   10.73800  1.000 47.57000  ? 793 HOH A O     1 
HETATM 7341 O  O     . HOH O 5 .   ? 13.96000  -3.46000  2.53400   1.000 47.58000  ? 794 HOH A O     1 
HETATM 7342 O  O     . HOH O 5 .   ? 28.01600  -21.85700 13.86200  1.000 45.94000  ? 795 HOH A O     1 
HETATM 7343 O  O     . HOH O 5 .   ? -9.74400  -22.39300 13.85100  1.000 47.63000  ? 796 HOH A O     1 
HETATM 7344 O  O     . HOH O 5 .   ? 12.29100  -41.27700 -3.66600  1.000 47.58000  ? 797 HOH A O     1 
HETATM 7345 O  O     . HOH O 5 .   ? 18.82500  0.95200   7.60400   1.000 39.78000  ? 798 HOH A O     1 
HETATM 7346 O  O     . HOH O 5 .   ? 27.584    -44.828   -12.343   1.000 47.63000  ? 799 HOH A O     1 
HETATM 7347 O  O     . HOH O 5 .   ? 44.33800  -34.45900 5.17100   1.000 47.58000  ? 800 HOH A O     1 
HETATM 7348 O  O     . HOH O 5 .   ? 12.84900  -17.76800 32.10300  1.000 47.63000  ? 801 HOH A O     1 
HETATM 7349 O  O     . HOH O 5 .   ? 24.41200  -21.81000 16.95700  1.000 48.95000  ? 802 HOH A O     1 
HETATM 7350 O  O     . HOH O 5 .   ? 31.00700  -29.62200 -17.69700 1.000 30.00000  ? 803 HOH A O     1 
HETATM 7351 O  O     . HOH O 5 .   ? 14.90800  -40.08400 -8.28800  1.000 47.57000  ? 804 HOH A O     1 
HETATM 7352 O  O     . HOH O 5 .   ? 1.13500   -42.97300 19.36200  1.000 47.63000  ? 805 HOH A O     1 
HETATM 7353 O  O     . HOH O 5 .   ? -13.19500 -18.40800 21.35200  1.000 46.02000  ? 806 HOH A O     1 
HETATM 7354 O  O     . HOH O 5 .   ? 15.60200  0.70800   7.27500   1.000 30.00000  ? 807 HOH A O     1 
HETATM 7355 O  O     . HOH O 5 .   ? 28.26300  -11.54300 0.13300   1.000 47.63000  ? 808 HOH A O     1 
HETATM 7356 O  O     . HOH O 5 .   ? 22.85800  -22.84000 -20.16200 1.000 47.58000  ? 809 HOH A O     1 
HETATM 7357 O  O     . HOH O 5 .   ? 2.41900   -22.51000 35.72700  1.000 30.00000  ? 810 HOH A O     1 
HETATM 7358 O  O     . HOH O 5 .   ? 34.80100  -44.29400 8.66500   1.000 51.29000  ? 811 HOH A O     1 
HETATM 7359 O  O     . HOH O 5 .   ? 29.21100  -3.11700  22.70600  1.000 47.57000  ? 812 HOH A O     1 
HETATM 7360 O  O     . HOH O 5 .   ? 10.33700  -22.29200 29.82000  1.000 30.00000  ? 813 HOH A O     1 
HETATM 7361 O  O     . HOH O 5 .   ? 33.85900  -17.25500 5.13600   1.000 47.58000  ? 814 HOH A O     1 
HETATM 7362 O  O     . HOH O 5 .   ? 16.15900  -40.11200 -5.59800  1.000 47.57000  ? 815 HOH A O     1 
HETATM 7363 O  O     . HOH O 5 .   ? 29.72800  -4.46800  4.77700   1.000 54.66000  ? 816 HOH A O     1 
HETATM 7364 O  O     . HOH O 5 .   ? 34.873    -34.395   -6.203    1.000 47.58000  ? 817 HOH A O     1 
HETATM 7365 O  O     . HOH O 5 .   ? 21.28700  -18.12400 13.83100  1.000 47.58000  ? 818 HOH A O     1 
HETATM 7366 O  O     . HOH O 5 .   ? 26.95700  -22.29800 16.22500  1.000 47.83000  ? 819 HOH A O     1 
HETATM 7367 O  O     . HOH O 5 .   ? 0.20200   -23.00500 10.71700  1.000 47.58000  ? 820 HOH A O     1 
HETATM 7368 O  O     . HOH O 5 .   ? 21.22400  -17.01200 8.50600   1.000 47.58000  ? 821 HOH A O     1 
HETATM 7369 O  O     . HOH O 5 .   ? 15.68900  -32.76200 4.90500   1.000 47.58000  ? 822 HOH A O     1 
HETATM 7370 O  O     . HOH O 5 .   ? -13.54400 -21.60200 24.05000  1.000 30.00000  ? 823 HOH A O     1 
HETATM 7371 O  O     . HOH O 5 .   ? 8.75600   -33.17500 20.06700  1.000 50.27000  ? 824 HOH A O     1 
HETATM 7372 O  O     . HOH O 5 .   ? 28.58900  -10.48800 6.99600   1.000 45.91000  ? 825 HOH A O     1 
HETATM 7373 O  O     . HOH O 5 .   ? 33.879    -36.438   -6.671    1.000 47.57000  ? 826 HOH A O     1 
HETATM 7374 O  O     . HOH O 5 .   ? 23.47400  -14.62900 0.61400   1.000 30.00000  ? 827 HOH A O     1 
HETATM 7375 O  O     . HOH O 5 .   ? 4.44100   0.11700   13.20300  1.000 47.57000  ? 828 HOH A O     1 
HETATM 7376 O  O     . HOH O 5 .   ? 14.53500  -21.75800 1.23000   1.000 47.63000  ? 829 HOH A O     1 
HETATM 7377 O  O     . HOH O 5 .   ? 20.17500  -20.65800 32.45500  1.000 47.58000  ? 830 HOH A O     1 
HETATM 7378 O  O     . HOH O 5 .   ? 10.82700  -19.12200 33.58400  1.000 47.58000  ? 831 HOH A O     1 
HETATM 7379 O  O     . HOH O 5 .   ? 15.67700  -19.53100 32.71300  1.000 48.28000  ? 832 HOH A O     1 
HETATM 7380 O  O     . HOH O 5 .   ? -4.25300  -34.50500 19.90100  1.000 30.00000  ? 833 HOH A O     1 
HETATM 7381 O  O     . HOH O 5 .   ? 18.03300  -28.38000 4.87000   1.000 47.57000  ? 834 HOH A O     1 
HETATM 7382 O  O     . HOH O 5 .   ? 22.27200  -3.62400  1.86100   1.000 47.57000  ? 835 HOH A O     1 
HETATM 7383 O  O     . HOH O 5 .   ? 23.863    10.000    17.518    1.000 47.58000  ? 836 HOH A O     1 
HETATM 7384 O  O     . HOH O 5 .   ? 25.64300  -9.95100  4.00600   1.000 42.45000  ? 837 HOH A O     1 
HETATM 7385 O  O     . HOH O 5 .   ? 27.50800  -22.46800 26.46500  1.000 47.63000  ? 838 HOH A O     1 
HETATM 7386 O  O     . HOH O 5 .   ? 14.35300  -31.99600 7.02900   1.000 47.57000  ? 839 HOH A O     1 
HETATM 7387 O  O     . HOH O 5 .   ? -5.90000  -12.70500 21.94000  1.000 51.94000  ? 840 HOH A O     1 
HETATM 7388 O  O     . HOH O 5 .   ? 11.88400  -13.93900 -6.70000  1.000 47.58000  ? 841 HOH A O     1 
HETATM 7389 O  O     . HOH O 5 .   ? 26.888    -3.136    -5.017    1.000 47.63000  ? 842 HOH A O     1 
HETATM 7390 O  O     . HOH O 5 .   ? -4.41900  -30.37900 10.05700  1.000 47.57000  ? 843 HOH A O     1 
HETATM 7391 O  O     . HOH O 5 .   ? 0.26200   -6.70700  16.79800  1.000 47.58000  ? 844 HOH A O     1 
HETATM 7392 O  O     . HOH O 5 .   ? 18.32400  -2.17300  0.69700   1.000 47.63000  ? 845 HOH A O     1 
HETATM 7393 O  O     . HOH O 5 .   ? 16.86000  -18.68300 -9.27200  1.000 53.93000  ? 846 HOH A O     1 
HETATM 7394 O  O     . HOH O 5 .   ? -2.46700  -32.48200 10.95600  1.000 47.57000  ? 847 HOH A O     1 
HETATM 7395 O  O     . HOH O 5 .   ? 28.77900  -8.80600  4.68100   1.000 55.87000  ? 848 HOH A O     1 
HETATM 7396 O  O     . HOH O 5 .   ? -5.029    -24.826   0.719     1.000 47.58000  ? 849 HOH A O     1 
HETATM 7397 O  O     . HOH O 5 .   ? 25.76300  -13.42800 7.85700   1.000 47.63000  ? 850 HOH A O     1 
HETATM 7398 O  O     . HOH O 5 .   ? 25.04200  -21.29100 30.56200  1.000 47.58000  ? 851 HOH A O     1 
HETATM 7399 O  O     . HOH O 5 .   ? 1.95200   -5.83900  9.18300   1.000 30.00000  ? 852 HOH A O     1 
HETATM 7400 O  O     . HOH O 5 .   ? 35.241    -20.552   -5.415    1.000 30.00000  ? 853 HOH A O     1 
HETATM 7401 O  O     . HOH O 5 .   ? -6.68400  -35.43900 20.41500  1.000 30.00000  ? 854 HOH A O     1 
HETATM 7402 O  O     . HOH O 5 .   ? -9.04800  -12.97100 17.71300  1.000 30.00000  ? 855 HOH A O     1 
HETATM 7403 O  O     . HOH O 5 .   ? 8.58100   -0.65600  31.78700  1.000 30.00000  ? 856 HOH A O     1 
HETATM 7404 O  O     . HOH O 5 .   ? 24.47700  -22.40000 33.75900  1.000 47.57000  ? 857 HOH A O     1 
HETATM 7405 O  O     . HOH O 5 .   ? -3.30000  -9.71800  18.78300  1.000 30.00000  ? 858 HOH A O     1 
HETATM 7406 O  O     . HOH O 5 .   ? 41.06400  -18.19400 8.80000   1.000 30.00000  ? 859 HOH A O     1 
HETATM 7407 O  O     . HOH O 5 .   ? 9.82300   -21.06200 35.43500  1.000 54.55000  ? 860 HOH A O     1 
HETATM 7408 O  O     . HOH O 5 .   ? 23.19300  -14.91500 9.08100   1.000 43.22000  ? 861 HOH A O     1 
HETATM 7409 O  O     . HOH O 5 .   ? 22.33800  -21.27500 -18.34100 1.000 47.58000  ? 862 HOH A O     1 
HETATM 7410 O  O     . HOH O 5 .   ? 20.56000  -2.70200  5.62900   1.000 47.58000  ? 863 HOH A O     1 
HETATM 7411 O  O     . HOH O 5 .   ? 39.48500  -27.85500 1.78200   1.000 47.58000  ? 864 HOH A O     1 
HETATM 7412 O  O     . HOH O 5 .   ? 1.20300   -7.00900  27.87600  1.000 30.00000  ? 865 HOH A O     1 
HETATM 7413 O  O     . HOH O 5 .   ? 37.24200  -44.69200 10.85100  1.000 59.37000  ? 866 HOH A O     1 
HETATM 7414 O  O     . HOH O 5 .   ? -0.97900  -4.41700  16.46400  1.000 47.58000  ? 867 HOH A O     1 
HETATM 7415 O  O     . HOH O 5 .   ? 22.18500  -21.64200 34.99700  1.000 47.58000  ? 868 HOH A O     1 
HETATM 7416 O  O     . HOH P 5 .   ? 14.95300  8.38100   55.31100  1.000 54.33000  ? 601 HOH B O     1 
HETATM 7417 O  O     . HOH P 5 .   ? -10.35200 5.85600   34.78100  1.000 47.58000  ? 602 HOH B O     1 
HETATM 7418 O  O     . HOH P 5 .   ? -18.21100 27.74400  59.20100  1.000 47.57000  ? 603 HOH B O     1 
HETATM 7419 O  O     . HOH P 5 .   ? -26.38700 -9.70100  45.30800  1.000 47.58000  ? 604 HOH B O     1 
HETATM 7420 O  O     . HOH P 5 .   ? 10.79700  16.24100  54.77300  1.000 52.14000  ? 605 HOH B O     1 
HETATM 7421 O  O     . HOH P 5 .   ? -8.72100  16.11600  38.23300  1.000 55.11000  ? 606 HOH B O     1 
HETATM 7422 O  O     . HOH P 5 .   ? 11.73600  1.07500   45.35300  1.000 47.24000  ? 607 HOH B O     1 
HETATM 7423 O  O     . HOH P 5 .   ? 1.04300   16.57800  44.16800  1.000 45.10000  ? 608 HOH B O     1 
HETATM 7424 O  O     . HOH P 5 .   ? -12.04500 30.60600  49.83600  1.000 55.32000  ? 609 HOH B O     1 
HETATM 7425 O  O     . HOH P 5 .   ? 14.40800  0.84200   58.12400  1.000 59.69000  ? 610 HOH B O     1 
HETATM 7426 O  O     . HOH P 5 .   ? 4.21100   -17.58500 68.60400  1.000 52.01000  ? 611 HOH B O     1 
HETATM 7427 O  O     . HOH P 5 .   ? -15.31200 -8.54800  74.84000  1.000 47.63000  ? 612 HOH B O     1 
HETATM 7428 O  O     . HOH P 5 .   ? -7.35100  -14.03900 76.83900  1.000 47.58000  ? 613 HOH B O     1 
HETATM 7429 O  O     . HOH P 5 .   ? -1.40200  5.27900   56.57000  1.000 38.05000  ? 614 HOH B O     1 
HETATM 7430 O  O     . HOH P 5 .   ? -20.93100 7.59100   30.27600  1.000 47.58000  ? 615 HOH B O     1 
HETATM 7431 O  O     . HOH P 5 .   ? 20.42900  -13.52300 45.52400  1.000 47.57000  ? 616 HOH B O     1 
HETATM 7432 O  O     . HOH P 5 .   ? -24.04800 -11.39500 53.31700  1.000 55.94000  ? 617 HOH B O     1 
HETATM 7433 O  O     . HOH P 5 .   ? 8.34500   -4.85000  65.73800  1.000 44.42000  ? 618 HOH B O     1 
HETATM 7434 O  O     . HOH P 5 .   ? 2.44400   21.00300  39.78400  1.000 47.58000  ? 619 HOH B O     1 
HETATM 7435 O  O     . HOH P 5 .   ? -12.90300 9.07300   59.40200  1.000 38.74000  ? 620 HOH B O     1 
HETATM 7436 O  O     . HOH P 5 .   ? -15.08600 12.96300  65.28800  1.000 53.65000  ? 621 HOH B O     1 
HETATM 7437 O  O     . HOH P 5 .   ? 12.10800  5.95500   45.60700  1.000 45.08000  ? 622 HOH B O     1 
HETATM 7438 O  O     . HOH P 5 .   ? -11.00600 3.29300   51.88200  1.000 47.58000  ? 623 HOH B O     1 
HETATM 7439 O  O     . HOH P 5 .   ? -17.75700 7.85700   65.56800  1.000 49.59000  ? 624 HOH B O     1 
HETATM 7440 O  O     . HOH P 5 .   ? -17.43100 -9.41100  45.17200  1.000 47.58000  ? 625 HOH B O     1 
HETATM 7441 O  O     . HOH P 5 .   ? -16.24700 5.97400   60.72400  1.000 50.56000  ? 626 HOH B O     1 
HETATM 7442 O  O     . HOH P 5 .   ? -14.80200 -11.60300 47.90600  1.000 52.34000  ? 627 HOH B O     1 
HETATM 7443 O  O     . HOH P 5 .   ? -17.91900 11.62200  65.45700  1.000 47.58000  ? 628 HOH B O     1 
HETATM 7444 O  O     . HOH P 5 .   ? -10.78500 11.47900  47.35600  1.000 47.69000  ? 629 HOH B O     1 
HETATM 7445 O  O     . HOH P 5 .   ? 15.53700  9.27300   52.30100  1.000 45.91000  ? 630 HOH B O     1 
HETATM 7446 O  O     . HOH P 5 .   ? -9.95700  -10.08600 72.02600  1.000 43.46000  ? 631 HOH B O     1 
HETATM 7447 O  O     . HOH P 5 .   ? 1.52700   2.09400   47.37100  1.000 47.78000  ? 632 HOH B O     1 
HETATM 7448 O  O     . HOH P 5 .   ? -12.07000 12.02600  66.84800  1.000 39.67000  ? 633 HOH B O     1 
HETATM 7449 O  O     . HOH P 5 .   ? -18.16100 -0.69200  57.15600  1.000 55.69000  ? 634 HOH B O     1 
HETATM 7450 O  O     . HOH P 5 .   ? -13.10500 12.74100  39.67000  1.000 49.02000  ? 635 HOH B O     1 
HETATM 7451 O  O     . HOH P 5 .   ? -15.62500 -0.22200  58.20800  1.000 44.94000  ? 636 HOH B O     1 
HETATM 7452 O  O     . HOH P 5 .   ? -9.25700  -3.34200  50.48200  1.000 47.58000  ? 637 HOH B O     1 
HETATM 7453 O  O     . HOH P 5 .   ? -8.77900  18.31600  47.61500  1.000 37.23000  ? 638 HOH B O     1 
HETATM 7454 O  O     . HOH P 5 .   ? -10.86500 16.62200  68.12700  1.000 47.58000  ? 639 HOH B O     1 
HETATM 7455 O  O     . HOH P 5 .   ? -1.61300  4.44200   69.80400  1.000 49.71000  ? 640 HOH B O     1 
HETATM 7456 O  O     . HOH P 5 .   ? -1.60600  -12.95700 52.66200  1.000 47.58000  ? 641 HOH B O     1 
HETATM 7457 O  O     . HOH P 5 .   ? 2.64300   5.51500   62.88000  1.000 46.46000  ? 642 HOH B O     1 
HETATM 7458 O  O     . HOH P 5 .   ? 8.79600   7.79900   51.03100  1.000 50.87000  ? 643 HOH B O     1 
HETATM 7459 O  O     . HOH P 5 .   ? 8.71800   -12.62000 66.19800  1.000 47.58000  ? 644 HOH B O     1 
HETATM 7460 O  O     . HOH P 5 .   ? -24.17600 4.53300   59.23000  1.000 49.35000  ? 645 HOH B O     1 
HETATM 7461 O  O     . HOH P 5 .   ? -1.44200  -4.57800  80.12300  1.000 50.62000  ? 646 HOH B O     1 
HETATM 7462 O  O     . HOH P 5 .   ? 2.22200   2.80100   67.19200  1.000 44.53000  ? 647 HOH B O     1 
HETATM 7463 O  O     . HOH P 5 .   ? -26.34700 21.25700  52.22200  1.000 67.44000  ? 648 HOH B O     1 
HETATM 7464 O  O     . HOH P 5 .   ? -8.38900  7.75300   53.89400  1.000 41.66000  ? 649 HOH B O     1 
HETATM 7465 O  O     . HOH P 5 .   ? -6.84000  9.00400   71.24400  1.000 56.54000  ? 650 HOH B O     1 
HETATM 7466 O  O     . HOH P 5 .   ? -5.979    21.623    37.117    1.000 47.94000  ? 651 HOH B O     1 
HETATM 7467 O  O     . HOH P 5 .   ? -1.07700  0.47600   75.55800  1.000 50.12000  ? 652 HOH B O     1 
HETATM 7468 O  O     . HOH P 5 .   ? -6.42900  28.27200  48.78900  1.000 47.63000  ? 653 HOH B O     1 
HETATM 7469 O  O     . HOH P 5 .   ? 1.98600   -9.62100  47.16600  1.000 41.91000  ? 654 HOH B O     1 
HETATM 7470 O  O     . HOH P 5 .   ? -6.31900  3.63100   74.50300  1.000 46.28000  ? 655 HOH B O     1 
HETATM 7471 O  O     . HOH P 5 .   ? -19.63100 19.95100  55.87900  1.000 45.37000  ? 656 HOH B O     1 
HETATM 7472 O  O     . HOH P 5 .   ? -0.17600  20.46500  41.62300  1.000 47.63000  ? 657 HOH B O     1 
HETATM 7473 O  O     . HOH P 5 .   ? -11.61700 24.16900  64.85000  1.000 47.57000  ? 658 HOH B O     1 
HETATM 7474 O  O     . HOH P 5 .   ? -17.57700 29.51200  49.75600  1.000 30.00000  ? 659 HOH B O     1 
HETATM 7475 O  O     . HOH P 5 .   ? -4.41100  -25.07700 46.07400  1.000 58.54000  ? 660 HOH B O     1 
HETATM 7476 O  O     . HOH P 5 .   ? 1.82000   -6.92900  51.84900  1.000 47.58000  ? 661 HOH B O     1 
HETATM 7477 O  O     . HOH P 5 .   ? -0.73600  11.88900  57.42700  1.000 40.82000  ? 662 HOH B O     1 
HETATM 7478 O  O     . HOH P 5 .   ? -21.52000 16.01000  56.73300  1.000 46.15000  ? 663 HOH B O     1 
HETATM 7479 O  O     . HOH P 5 .   ? -6.38100  -8.13800  57.38900  1.000 47.58000  ? 664 HOH B O     1 
HETATM 7480 O  O     . HOH P 5 .   ? -14.00500 1.95000   58.82000  1.000 40.54000  ? 665 HOH B O     1 
HETATM 7481 O  O     . HOH P 5 .   ? -1.43500  3.92500   54.02000  1.000 37.92000  ? 666 HOH B O     1 
HETATM 7482 O  O     . HOH P 5 .   ? 1.74900   -5.97300  73.64500  1.000 44.09000  ? 667 HOH B O     1 
HETATM 7483 O  O     . HOH P 5 .   ? -8.69300  -8.33400  52.72000  1.000 52.29000  ? 668 HOH B O     1 
HETATM 7484 O  O     . HOH P 5 .   ? -24.83300 1.09000   57.29900  1.000 47.58000  ? 669 HOH B O     1 
HETATM 7485 O  O     . HOH P 5 .   ? -9.17100  -12.39800 70.52000  1.000 48.03000  ? 670 HOH B O     1 
HETATM 7486 O  O     . HOH P 5 .   ? -7.93700  -0.65000  63.59300  1.000 47.58000  ? 671 HOH B O     1 
HETATM 7487 O  O     . HOH P 5 .   ? -1.37100  -26.30500 52.61900  1.000 30.00000  ? 672 HOH B O     1 
HETATM 7488 O  O     . HOH P 5 .   ? 2.33000   -4.47400  52.97500  1.000 30.00000  ? 673 HOH B O     1 
HETATM 7489 O  O     . HOH P 5 .   ? 0.26400   17.77800  50.88400  1.000 41.27000  ? 674 HOH B O     1 
HETATM 7490 O  O     . HOH P 5 .   ? 6.20800   -1.79300  45.17200  1.000 60.85000  ? 675 HOH B O     1 
HETATM 7491 O  O     . HOH P 5 .   ? -1.27400  15.15000  66.50400  1.000 47.58000  ? 676 HOH B O     1 
HETATM 7492 O  O     . HOH P 5 .   ? -5.76900  9.28300   54.07100  1.000 39.83000  ? 677 HOH B O     1 
HETATM 7493 O  O     . HOH P 5 .   ? -7.71500  23.67000  38.63300  1.000 60.42000  ? 678 HOH B O     1 
HETATM 7494 O  O     . HOH P 5 .   ? -9.75100  17.62300  36.34900  1.000 47.63000  ? 679 HOH B O     1 
HETATM 7495 O  O     . HOH P 5 .   ? -26.69900 4.87300   51.06300  1.000 54.84000  ? 680 HOH B O     1 
HETATM 7496 O  O     . HOH P 5 .   ? -2.13500  -3.69100  59.09200  1.000 50.33000  ? 681 HOH B O     1 
HETATM 7497 O  O     . HOH P 5 .   ? -4.56800  5.20100   57.02500  1.000 36.83000  ? 682 HOH B O     1 
HETATM 7498 O  O     . HOH P 5 .   ? -3.62800  0.20000   52.92700  1.000 47.57000  ? 683 HOH B O     1 
HETATM 7499 O  O     . HOH P 5 .   ? -1.03500  18.86000  62.86600  1.000 46.18000  ? 684 HOH B O     1 
HETATM 7500 O  O     . HOH P 5 .   ? -0.09300  16.09000  47.00800  1.000 50.55000  ? 685 HOH B O     1 
HETATM 7501 O  O     . HOH P 5 .   ? -4.16700  15.74500  32.08300  1.000 47.63000  ? 686 HOH B O     1 
HETATM 7502 O  O     . HOH P 5 .   ? -14.22300 11.94200  68.54900  1.000 47.63000  ? 687 HOH B O     1 
HETATM 7503 O  O     . HOH P 5 .   ? -10.17300 -19.19700 58.66000  1.000 47.58000  ? 688 HOH B O     1 
HETATM 7504 O  O     . HOH P 5 .   ? -2.09400  -9.82200  56.31100  1.000 47.57000  ? 689 HOH B O     1 
HETATM 7505 O  O     . HOH P 5 .   ? 10.21100  2.29700   39.01800  1.000 47.58000  ? 690 HOH B O     1 
HETATM 7506 O  O     . HOH P 5 .   ? -1.34300  -2.82800  56.42200  1.000 49.76000  ? 691 HOH B O     1 
HETATM 7507 O  O     . HOH P 5 .   ? -18.32300 -0.00500  60.06900  1.000 41.94000  ? 692 HOH B O     1 
HETATM 7508 O  O     . HOH P 5 .   ? -2.81400  21.00100  52.60300  1.000 46.65000  ? 693 HOH B O     1 
HETATM 7509 O  O     . HOH P 5 .   ? -3.19100  20.81200  56.55700  1.000 47.57000  ? 694 HOH B O     1 
HETATM 7510 O  O     . HOH P 5 .   ? 5.23900   7.38800   54.40500  1.000 30.00000  ? 695 HOH B O     1 
HETATM 7511 O  O     . HOH P 5 .   ? -13.04500 -5.98400  40.14200  1.000 47.58000  ? 696 HOH B O     1 
HETATM 7512 O  O     . HOH P 5 .   ? 10.92500  18.99200  55.15700  1.000 47.58000  ? 697 HOH B O     1 
HETATM 7513 O  O     . HOH P 5 .   ? 0.45100   17.85100  41.16600  1.000 54.50000  ? 698 HOH B O     1 
HETATM 7514 O  O     . HOH P 5 .   ? 15.31100  7.74600   46.85400  1.000 50.40000  ? 699 HOH B O     1 
HETATM 7515 O  O     . HOH P 5 .   ? -0.73600  21.05700  59.17400  1.000 47.63000  ? 700 HOH B O     1 
HETATM 7516 O  O     . HOH P 5 .   ? -12.34500 -10.83800 52.54400  1.000 51.62000  ? 701 HOH B O     1 
HETATM 7517 O  O     . HOH P 5 .   ? 2.78100   18.18500  51.34800  1.000 51.66000  ? 702 HOH B O     1 
HETATM 7518 O  O     . HOH P 5 .   ? -6.27000  -13.56100 56.33500  1.000 47.58000  ? 703 HOH B O     1 
HETATM 7519 O  O     . HOH P 5 .   ? -11.76400 28.26400  42.52300  1.000 58.75000  ? 704 HOH B O     1 
HETATM 7520 O  O     . HOH P 5 .   ? -16.24700 16.39700  65.37500  1.000 62.13000  ? 705 HOH B O     1 
HETATM 7521 O  O     . HOH P 5 .   ? -4.97700  19.99200  66.12400  1.000 47.57000  ? 706 HOH B O     1 
HETATM 7522 O  O     . HOH P 5 .   ? -2.88300  23.80700  50.76900  1.000 41.59000  ? 707 HOH B O     1 
HETATM 7523 O  O     . HOH P 5 .   ? -1.30100  -21.61200 67.36100  1.000 30.00000  ? 708 HOH B O     1 
HETATM 7524 O  O     . HOH P 5 .   ? -2.90900  5.67500   53.56800  1.000 47.58000  ? 709 HOH B O     1 
HETATM 7525 O  O     . HOH P 5 .   ? -13.75400 -21.64600 61.71500  1.000 47.63000  ? 710 HOH B O     1 
HETATM 7526 O  O     . HOH P 5 .   ? 1.55900   5.36000   65.69200  1.000 47.63000  ? 711 HOH B O     1 
HETATM 7527 O  O     . HOH P 5 .   ? -15.91300 19.72500  63.31000  1.000 30.00000  ? 712 HOH B O     1 
HETATM 7528 O  O     . HOH P 5 .   ? -12.76600 -10.71100 49.77900  1.000 47.58000  ? 713 HOH B O     1 
HETATM 7529 O  O     . HOH P 5 .   ? -27.22100 -23.89800 36.45300  1.000 30.00000  ? 714 HOH B O     1 
HETATM 7530 O  O     . HOH P 5 .   ? -8.58800  3.09200   75.85600  1.000 57.97000  ? 715 HOH B O     1 
HETATM 7531 O  O     . HOH P 5 .   ? -7.92700  0.66900   61.07600  1.000 47.63000  ? 716 HOH B O     1 
HETATM 7532 O  O     . HOH P 5 .   ? -1.11900  11.99600  60.38400  1.000 48.55000  ? 717 HOH B O     1 
HETATM 7533 O  O     . HOH P 5 .   ? -20.41400 -1.46600  60.47300  1.000 47.58000  ? 718 HOH B O     1 
HETATM 7534 O  O     . HOH P 5 .   ? 8.790     9.764     41.491    1.000 30.00000  ? 719 HOH B O     1 
HETATM 7535 O  O     . HOH P 5 .   ? -3.258    -15.020   81.881    1.000 47.58000  ? 720 HOH B O     1 
HETATM 7536 O  O     . HOH P 5 .   ? 2.73000   -2.97300  73.21100  1.000 47.58000  ? 721 HOH B O     1 
HETATM 7537 O  O     . HOH P 5 .   ? -3.14300  -20.95800 74.86000  1.000 30.00000  ? 722 HOH B O     1 
HETATM 7538 O  O     . HOH P 5 .   ? 1.51700   12.83100  57.31100  1.000 47.03000  ? 723 HOH B O     1 
HETATM 7539 O  O     . HOH P 5 .   ? -11.32800 1.23800   58.08500  1.000 47.58000  ? 724 HOH B O     1 
HETATM 7540 O  O     . HOH P 5 .   ? -20.998   -29.368   43.274    1.000 30.00000  ? 725 HOH B O     1 
HETATM 7541 O  O     . HOH P 5 .   ? 3.59400   20.34900  49.85700  1.000 53.99000  ? 726 HOH B O     1 
HETATM 7542 O  O     . HOH P 5 .   ? -20.69900 11.34300  64.73500  1.000 47.58000  ? 727 HOH B O     1 
HETATM 7543 O  O     . HOH P 5 .   ? -14.90800 16.07300  67.92500  1.000 47.58000  ? 728 HOH B O     1 
HETATM 7544 O  O     . HOH P 5 .   ? -29.81800 15.97400  36.99600  1.000 47.57000  ? 729 HOH B O     1 
HETATM 7545 O  O     . HOH P 5 .   ? -2.51100  9.45000   58.15000  1.000 53.60000  ? 730 HOH B O     1 
HETATM 7546 O  O     . HOH P 5 .   ? 10.527    20.129    57.494    1.000 47.58000  ? 731 HOH B O     1 
HETATM 7547 O  O     . HOH P 5 .   ? -20.01900 -0.22300  62.49800  1.000 47.58000  ? 732 HOH B O     1 
HETATM 7548 O  O     . HOH P 5 .   ? 20.739    4.225     59.937    1.000 30.00000  ? 733 HOH B O     1 
HETATM 7549 O  O     . HOH P 5 .   ? 11.18500  -4.68500  65.63000  1.000 61.99000  ? 734 HOH B O     1 
HETATM 7550 O  O     . HOH P 5 .   ? 3.20200   21.78300  47.67000  1.000 47.58000  ? 735 HOH B O     1 
HETATM 7551 O  O     . HOH P 5 .   ? -32.50500 16.60300  38.10600  1.000 47.57000  ? 736 HOH B O     1 
HETATM 7552 O  O     . HOH P 5 .   ? -20.62500 23.50400  60.51600  1.000 47.57000  ? 737 HOH B O     1 
HETATM 7553 O  O     . HOH P 5 .   ? -1.27200  22.09900  48.42100  1.000 47.63000  ? 738 HOH B O     1 
HETATM 7554 O  O     . HOH P 5 .   ? 3.93900   3.18500   69.55800  1.000 47.58000  ? 739 HOH B O     1 
HETATM 7555 O  O     . HOH P 5 .   ? 4.17000   -1.93300  46.19100  1.000 47.58000  ? 740 HOH B O     1 
HETATM 7556 O  O     . HOH P 5 .   ? -0.77700  19.62200  52.97300  1.000 53.23000  ? 741 HOH B O     1 
HETATM 7557 O  O     . HOH P 5 .   ? 11.994    2.376     65.551    1.000 47.58000  ? 742 HOH B O     1 
HETATM 7558 O  O     . HOH P 5 .   ? -3.86900  7.82800   55.43300  1.000 46.13000  ? 743 HOH B O     1 
HETATM 7559 O  O     . HOH P 5 .   ? 5.19500   -3.78100  71.86500  1.000 30.00000  ? 744 HOH B O     1 
HETATM 7560 O  O     . HOH Q 5 .   ? 18.16100  -22.74200 11.91400  1.000 47.57000  ? 601 HOH C O     1 
HETATM 7561 O  O     . HOH Q 5 .   ? 12.92800  -23.36800 11.17900  1.000 47.63000  ? 602 HOH C O     1 
HETATM 7562 O  O     . HOH R 5 .   ? -5.73300  4.66300   51.71300  1.000 47.58000  ? 601 HOH D O     1 
HETATM 7563 O  O     . HOH R 5 .   ? -7.64900  5.01200   54.19500  1.000 47.63000  ? 602 HOH D O     1 
HETATM 7564 O  O     . HOH S 5 .   ? 23.61900  -34.26200 17.62800  1.000 47.57000  ? 601 HOH E O     1 
HETATM 7565 O  O     . HOH T 5 .   ? -9.30400  -16.46200 60.40200  1.000 47.58000  ? 601 HOH F O     1 
HETATM 7566 O  O     . HOH T 5 .   ? -13.53300 -13.94000 58.67900  1.000 47.63000  ? 602 HOH F O     1 
HETATM 7567 O  O     . HOH T 5 .   ? -10.55900 -12.35600 68.25400  1.000 47.58000  ? 603 HOH F O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . GLY A 5   ? 0.74240 0.76790 0.76640 -0.04700 0.04280  -0.11800 5   GLY A N     
2    C  CA    . GLY A 5   ? 0.55550 0.57980 0.57790 -0.04440 0.03830  -0.10410 5   GLY A CA    
3    C  C     . GLY A 5   ? 0.56960 0.59600 0.58940 -0.04700 0.03110  -0.10220 5   GLY A C     
4    O  O     . GLY A 5   ? 1.09080 1.12390 1.10160 -0.05060 0.02690  -0.10850 5   GLY A O     
5    N  N     . LEU A 6   ? 0.88370 0.90500 0.91170 -0.04470 0.02970  -0.09340 6   LEU A N     
6    C  CA    . LEU A 6   ? 0.65040 0.67310 0.67910 -0.04640 0.02370  -0.09050 6   LEU A CA    
7    C  C     . LEU A 6   ? 0.51770 0.53430 0.56270 -0.04790 0.02610  -0.09550 6   LEU A C     
8    O  O     . LEU A 6   ? 0.50140 0.50980 0.55800 -0.04520 0.03100  -0.09130 6   LEU A O     
9    C  CB    . LEU A 6   ? 0.67290 0.69450 0.69950 -0.04310 0.02110  -0.07740 6   LEU A CB    
10   C  CG    . LEU A 6   ? 0.58490 0.61180 0.59680 -0.04210 0.01870  -0.07170 6   LEU A CG    
11   C  CD1   . LEU A 6   ? 0.74690 0.77130 0.75980 -0.03850 0.01800  -0.06020 6   LEU A CD1   
12   C  CD2   . LEU A 6   ? 0.80140 0.83570 0.80140 -0.04500 0.01210  -0.07360 6   LEU A CD2   
13   N  N     . GLY A 7   ? 0.56790 0.58880 0.61380 -0.05230 0.02270  -0.10420 7   GLY A N     
14   C  CA    . GLY A 7   ? 0.51170 0.52770 0.57370 -0.05490 0.02480  -0.11010 7   GLY A CA    
15   C  C     . GLY A 7   ? 0.56890 0.57920 0.64080 -0.05300 0.02520  -0.10010 7   GLY A C     
16   O  O     . GLY A 7   ? 0.48690 0.50100 0.55210 -0.05150 0.02020  -0.09150 7   GLY A O     
17   N  N     . GLY A 8   ? 0.42230 0.42310 0.51030 -0.05290 0.03160  -0.10120 8   GLY A N     
18   C  CA    . GLY A 8   ? 0.47370 0.46820 0.57170 -0.05120 0.03350  -0.09210 8   GLY A CA    
19   C  C     . GLY A 8   ? 0.37110 0.36100 0.46600 -0.04520 0.03580  -0.07910 8   GLY A C     
20   O  O     . GLY A 8   ? 0.38610 0.37190 0.48650 -0.04330 0.03710  -0.07050 8   GLY A O     
21   N  N     . LEU A 9   ? 0.34550 0.33690 0.43170 -0.04240 0.03650  -0.07830 9   LEU A N     
22   C  CA    . LEU A 9   ? 0.40570 0.39560 0.48740 -0.03700 0.03730  -0.06720 9   LEU A CA    
23   C  C     . LEU A 9   ? 0.40380 0.39090 0.48730 -0.03410 0.04240  -0.06950 9   LEU A C     
24   O  O     . LEU A 9   ? 0.35690 0.34550 0.43990 -0.03650 0.04400  -0.07980 9   LEU A O     
25   C  CB    . LEU A 9   ? 0.40790 0.40640 0.47440 -0.03670 0.03080  -0.06240 9   LEU A CB    
26   C  CG    . LEU A 9   ? 0.46410 0.46670 0.52810 -0.03880 0.02520  -0.05980 9   LEU A CG    
27   C  CD1   . LEU A 9   ? 0.46730 0.47790 0.51630 -0.03900 0.01910  -0.05750 9   LEU A CD1   
28   C  CD2   . LEU A 9   ? 0.42310 0.42100 0.49340 -0.03610 0.02670  -0.05030 9   LEU A CD2   
29   N  N     . GLU A 10  ? 0.39470 0.37840 0.48020 -0.02880 0.04480  -0.06020 10  GLU A N     
30   C  CA    . GLU A 10  ? 0.41960 0.40220 0.50700 -0.02510 0.04890  -0.06110 10  GLU A CA    
31   C  C     . GLU A 10  ? 0.37790 0.36330 0.46070 -0.02010 0.04750  -0.05030 10  GLU A C     
32   O  O     . GLU A 10  ? 0.35790 0.34200 0.44100 -0.01800 0.04580  -0.04120 10  GLU A O     
33   C  CB    . GLU A 10  ? 0.41240 0.38510 0.51590 -0.02350 0.05610  -0.06450 10  GLU A CB    
34   C  CG    . GLU A 10  ? 0.54410 0.50890 0.65720 -0.01890 0.05880  -0.05370 10  GLU A CG    
35   C  CD    . GLU A 10  ? 0.78570 0.73950 0.91520 -0.01680 0.06640  -0.05620 10  GLU A CD    
36   O  OE1   . GLU A 10  ? 0.59970 0.55230 0.73400 -0.01820 0.06990  -0.06690 10  GLU A OE1   
37   O  OE2   . GLU A 10  ? 0.69790 0.64420 0.83580 -0.01360 0.06930  -0.04740 10  GLU A OE2   
38   N  N     . ARG A 11  ? 0.39310 0.38310 0.47180 -0.01830 0.04850  -0.05200 11  ARG A N     
39   C  CA    . ARG A 11  ? 0.36030 0.35330 0.43800 -0.01310 0.04840  -0.04370 11  ARG A CA    
40   C  C     . ARG A 11  ? 0.35890 0.34470 0.45050 -0.00760 0.05340  -0.04000 11  ARG A C     
41   O  O     . ARG A 11  ? 0.43620 0.41610 0.53730 -0.00790 0.05850  -0.04690 11  ARG A O     
42   C  CB    . ARG A 11  ? 0.35600 0.35650 0.42660 -0.01380 0.04860  -0.04820 11  ARG A CB    
43   C  CG    . ARG A 11  ? 0.39880 0.40340 0.47140 -0.00880 0.04930  -0.04190 11  ARG A CG    
44   C  CD    . ARG A 11  ? 0.52110 0.53410 0.58520 -0.01070 0.04910  -0.04560 11  ARG A CD    
45   N  NE    . ARG A 11  ? 0.63670 0.65320 0.70800 -0.00630 0.05250  -0.04470 11  ARG A NE    
46   C  CZ    . ARG A 11  ? 0.60020 0.62420 0.66700 -0.00730 0.05370  -0.04750 11  ARG A CZ    
47   N  NH1   . ARG A 11  ? 0.53710 0.56520 0.59120 -0.01260 0.05200  -0.05070 11  ARG A NH1   
48   N  NH2   . ARG A 11  ? 0.72150 0.74920 0.79720 -0.00290 0.05690  -0.04680 11  ARG A NH2   
49   N  N     . PHE A 12  ? 0.31680 0.30300 0.40960 -0.00280 0.05210  -0.02940 12  PHE A N     
50   C  CA    . PHE A 12  ? 0.30900 0.28900 0.41390 0.00340  0.05620  -0.02380 12  PHE A CA    
51   C  C     . PHE A 12  ? 0.32150 0.30760 0.42390 0.00890  0.05330  -0.01410 12  PHE A C     
52   O  O     . PHE A 12  ? 0.31590 0.31020 0.40780 0.00740  0.04850  -0.01200 12  PHE A O     
53   C  CB    . PHE A 12  ? 0.35930 0.32950 0.47120 0.00290  0.05840  -0.02040 12  PHE A CB    
54   C  CG    . PHE A 12  ? 0.31650 0.28820 0.42250 0.00390  0.05470  -0.01020 12  PHE A CG    
55   C  CD1   . PHE A 12  ? 0.29710 0.27510 0.39150 -0.00040 0.04940  -0.01080 12  PHE A CD1   
56   C  CD2   . PHE A 12  ? 0.33460 0.30120 0.44660 0.00930  0.05680  -0.00010 12  PHE A CD2   
57   C  CE1   . PHE A 12  ? 0.32880 0.30820 0.41820 0.00060  0.04650  -0.00240 12  PHE A CE1   
58   C  CE2   . PHE A 12  ? 0.31460 0.28320 0.42020 0.01020  0.05390  0.00870  12  PHE A CE2   
59   C  CZ    . PHE A 12  ? 0.32600 0.30100 0.42060 0.00570  0.04890  0.00700  12  PHE A CZ    
60   N  N     . CYS A 13  ? 0.39850 0.38080 0.51130 0.01550  0.05640  -0.00830 13  CYS A N     
61   C  CA    . CYS A 13  ? 0.40460 0.39310 0.51670 0.02160  0.05360  0.00120  13  CYS A CA    
62   C  C     . CYS A 13  ? 0.35840 0.34360 0.46770 0.02340  0.05180  0.01130  13  CYS A C     
63   O  O     . CYS A 13  ? 0.44630 0.42230 0.56390 0.02650  0.05570  0.01610  13  CYS A O     
64   C  CB    . CYS A 13  ? 0.43810 0.42530 0.56290 0.02860  0.05740  0.00260  13  CYS A CB    
65   S  SG    . CYS A 13  ? 0.56970 0.56450 0.69660 0.02720  0.05930  -0.00830 13  CYS A SG    
66   N  N     . SER A 14  ? 0.38510 0.37750 0.48290 0.02120  0.04640  0.01420  14  SER A N     
67   C  CA    . SER A 14  ? 0.43400 0.42530 0.52720 0.02260  0.04460  0.02310  14  SER A CA    
68   C  C     . SER A 14  ? 0.44360 0.44110 0.53710 0.02990  0.04240  0.03200  14  SER A C     
69   O  O     . SER A 14  ? 0.31790 0.32580 0.40660 0.03060  0.03820  0.03120  14  SER A O     
70   C  CB    . SER A 14  ? 0.33970 0.33620 0.42100 0.01700  0.03990  0.02100  14  SER A CB    
71   O  OG    . SER A 14  ? 0.39680 0.39290 0.47370 0.01810  0.03860  0.02860  14  SER A OG    
72   N  N     . PRO A 15  ? 0.39540 0.38700 0.49480 0.03570  0.04510  0.04080  15  PRO A N     
73   C  CA    . PRO A 15  ? 0.41630 0.41460 0.51630 0.04350  0.04260  0.04960  15  PRO A CA    
74   C  C     . PRO A 15  ? 0.39140 0.40150 0.47900 0.04300  0.03610  0.05250  15  PRO A C     
75   O  O     . PRO A 15  ? 0.43100 0.43970 0.51060 0.03980  0.03520  0.05440  15  PRO A O     
76   C  CB    . PRO A 15  ? 0.44820 0.43650 0.55370 0.04850  0.04680  0.05960  15  PRO A CB    
77   C  CG    . PRO A 15  ? 0.53970 0.51480 0.65330 0.04370  0.05310  0.05360  15  PRO A CG    
78   C  CD    . PRO A 15  ? 0.44750 0.42600 0.55380 0.03510  0.05080  0.04310  15  PRO A CD    
79   N  N     . GLY A 16  ? 0.36160 0.38350 0.44890 0.04580  0.03190  0.05170  16  GLY A N     
80   C  CA    . GLY A 16  ? 0.43930 0.47300 0.51640 0.04520  0.02570  0.05290  16  GLY A CA    
81   C  C     . GLY A 16  ? 0.41390 0.45110 0.48340 0.03730  0.02340  0.04470  16  GLY A C     
82   O  O     . GLY A 16  ? 0.38660 0.43310 0.44890 0.03620  0.01860  0.04460  16  GLY A O     
83   N  N     . LYS A 17  ? 0.32110 0.35100 0.39230 0.03180  0.02660  0.03760  17  LYS A N     
84   C  CA    . LYS A 17  ? 0.28960 0.32140 0.35330 0.02460  0.02460  0.03070  17  LYS A CA    
85   C  C     . LYS A 17  ? 0.30560 0.33850 0.37240 0.02120  0.02620  0.02230  17  LYS A C     
86   O  O     . LYS A 17  ? 0.44380 0.47740 0.50460 0.01540  0.02500  0.01700  17  LYS A O     
87   C  CB    . LYS A 17  ? 0.28240 0.30580 0.34230 0.02030  0.02620  0.03030  17  LYS A CB    
88   C  CG    . LYS A 17  ? 0.32540 0.34710 0.38180 0.02290  0.02580  0.03820  17  LYS A CG    
89   C  CD    . LYS A 17  ? 0.38090 0.39630 0.43400 0.01780  0.02710  0.03640  17  LYS A CD    
90   C  CE    . LYS A 17  ? 0.33790 0.35300 0.38650 0.01960  0.02720  0.04380  17  LYS A CE    
91   N  NZ    . LYS A 17  ? 0.39670 0.40700 0.45040 0.02540  0.03080  0.05200  17  LYS A NZ    
92   N  N     . GLY A 18  ? 0.33100 0.36450 0.40720 0.02520  0.02890  0.02140  18  GLY A N     
93   C  CA    . GLY A 18  ? 0.37200 0.40600 0.45180 0.02240  0.03170  0.01330  18  GLY A CA    
94   C  C     . GLY A 18  ? 0.35640 0.38000 0.43690 0.01850  0.03570  0.00810  18  GLY A C     
95   O  O     . GLY A 18  ? 0.38020 0.39520 0.46640 0.02070  0.03870  0.01070  18  GLY A O     
96   N  N     . ARG A 19  ? 0.29220 0.31700 0.36700 0.01250  0.03570  0.00080  19  ARG A N     
97   C  CA    . ARG A 19  ? 0.29050 0.30780 0.36440 0.00780  0.03840  -0.00570 19  ARG A CA    
98   C  C     . ARG A 19  ? 0.28470 0.29930 0.35060 0.00390  0.03520  -0.00380 19  ARG A C     
99   O  O     . ARG A 19  ? 0.28930 0.30930 0.34780 0.00300  0.03100  -0.00040 19  ARG A O     
100  C  CB    . ARG A 19  ? 0.31610 0.33720 0.38680 0.00390  0.04000  -0.01400 19  ARG A CB    
101  C  CG    . ARG A 19  ? 0.36060 0.38500 0.44040 0.00760  0.04390  -0.01670 19  ARG A CG    
102  C  CD    . ARG A 19  ? 0.32480 0.35640 0.39990 0.00410  0.04500  -0.02300 19  ARG A CD    
103  N  NE    . ARG A 19  ? 0.31420 0.35330 0.38120 0.00210  0.04060  -0.01940 19  ARG A NE    
104  C  CZ    . ARG A 19  ? 0.38890 0.43490 0.45160 -0.00100 0.04130  -0.02270 19  ARG A CZ    
105  N  NH1   . ARG A 19  ? 0.37870 0.42600 0.44340 -0.00230 0.04620  -0.02960 19  ARG A NH1   
106  N  NH2   . ARG A 19  ? 0.34770 0.39920 0.40450 -0.00300 0.03750  -0.01920 19  ARG A NH2   
107  N  N     . GLY A 20  ? 0.28520 0.29200 0.35370 0.00170  0.03730  -0.00650 20  GLY A N     
108  C  CA    . GLY A 20  ? 0.32110 0.32570 0.38410 -0.00210 0.03470  -0.00570 20  GLY A CA    
109  C  C     . GLY A 20  ? 0.33940 0.33940 0.40390 -0.00670 0.03640  -0.01360 20  GLY A C     
110  O  O     . GLY A 20  ? 0.25750 0.25610 0.32600 -0.00740 0.03970  -0.02030 20  GLY A O     
111  N  N     . LEU A 21  ? 0.23580 0.23430 0.29740 -0.01000 0.03420  -0.01340 21  LEU A N     
112  C  CA    . LEU A 21  ? 0.25240 0.24790 0.31570 -0.01470 0.03470  -0.02080 21  LEU A CA    
113  C  C     . LEU A 21  ? 0.31240 0.30100 0.38450 -0.01460 0.03720  -0.01820 21  LEU A C     
114  O  O     . LEU A 21  ? 0.28450 0.27320 0.35530 -0.01320 0.03590  -0.01110 21  LEU A O     
115  C  CB    . LEU A 21  ? 0.25560 0.25680 0.30860 -0.01880 0.02930  -0.02300 21  LEU A CB    
116  C  CG    . LEU A 21  ? 0.29820 0.29950 0.35080 -0.02380 0.02830  -0.03150 21  LEU A CG    
117  C  CD1   . LEU A 21  ? 0.32750 0.32930 0.38030 -0.02510 0.03100  -0.03980 21  LEU A CD1   
118  C  CD2   . LEU A 21  ? 0.35720 0.36430 0.39970 -0.02640 0.02230  -0.03090 21  LEU A CD2   
119  N  N     . ARG A 22  ? 0.32580 0.30840 0.40710 -0.01640 0.04130  -0.02440 22  ARG A N     
120  C  CA    . ARG A 22  ? 0.39200 0.36640 0.48440 -0.01680 0.04540  -0.02280 22  ARG A CA    
121  C  C     . ARG A 22  ? 0.33340 0.30750 0.42910 -0.02310 0.04480  -0.03240 22  ARG A C     
122  O  O     . ARG A 22  ? 0.33330 0.31040 0.42650 -0.02570 0.04390  -0.04160 22  ARG A O     
123  C  CB    . ARG A 22  ? 0.41990 0.38650 0.52310 -0.01270 0.05160  -0.02130 22  ARG A CB    
124  C  CG    . ARG A 22  ? 0.62290 0.57940 0.73910 -0.01320 0.05720  -0.01970 22  ARG A CG    
125  C  CD    . ARG A 22  ? 0.58780 0.53660 0.71300 -0.00710 0.06270  -0.01330 22  ARG A CD    
126  N  NE    . ARG A 22  ? 0.45760 0.40520 0.58750 -0.00570 0.06520  -0.02040 22  ARG A NE    
127  C  CZ    . ARG A 22  ? 0.45170 0.39400 0.58980 0.00030  0.06950  -0.01620 22  ARG A CZ    
128  N  NH1   . ARG A 22  ? 0.38890 0.32670 0.53030 0.00570  0.07130  -0.00410 22  ARG A NH1   
129  N  NH2   . ARG A 22  ? 0.45710 0.39900 0.60010 0.00120  0.07200  -0.02390 22  ARG A NH2   
130  N  N     . ALA A 23  ? 0.30190 0.27340 0.40310 -0.02530 0.04530  -0.03070 23  ALA A N     
131  C  CA    . ALA A 23  ? 0.29570 0.26760 0.40260 -0.03120 0.04480  -0.03980 23  ALA A CA    
132  C  C     . ALA A 23  ? 0.34020 0.30290 0.46160 -0.03250 0.05160  -0.04560 23  ALA A C     
133  O  O     . ALA A 23  ? 0.32920 0.28340 0.45890 -0.02900 0.05730  -0.03910 23  ALA A O     
134  C  CB    . ALA A 23  ? 0.32900 0.30250 0.43760 -0.03310 0.04320  -0.03560 23  ALA A CB    
135  N  N     . LEU A 24  ? 0.33150 0.29620 0.45570 -0.03740 0.05090  -0.05810 24  LEU A N     
136  C  CA    . LEU A 24  ? 0.38500 0.34150 0.52410 -0.04000 0.05710  -0.06630 24  LEU A CA    
137  C  C     . LEU A 24  ? 0.38250 0.33910 0.53150 -0.04620 0.05710  -0.07260 24  LEU A C     
138  O  O     . LEU A 24  ? 0.38320 0.33190 0.54700 -0.04890 0.06280  -0.07850 24  LEU A O     
139  C  CB    . LEU A 24  ? 0.44790 0.40680 0.58420 -0.04120 0.05720  -0.07770 24  LEU A CB    
140  C  CG    . LEU A 24  ? 0.48700 0.44460 0.61850 -0.03540 0.05940  -0.07340 24  LEU A CG    
141  C  CD1   . LEU A 24  ? 0.48790 0.44940 0.61580 -0.03740 0.05960  -0.08570 24  LEU A CD1   
142  C  CD2   . LEU A 24  ? 0.47780 0.42340 0.62260 -0.03060 0.06670  -0.06630 24  LEU A CD2   
143  N  N     . GLN A 25  ? 0.41030 0.37600 0.55210 -0.04840 0.05060  -0.07140 25  GLN A N     
144  C  CA    . GLN A 25  ? 0.46410 0.43210 0.61530 -0.05380 0.04960  -0.07630 25  GLN A CA    
145  C  C     . GLN A 25  ? 0.37950 0.35150 0.52600 -0.05210 0.04670  -0.06580 25  GLN A C     
146  O  O     . GLN A 25  ? 0.37570 0.35020 0.50990 -0.04750 0.04400  -0.05710 25  GLN A O     
147  C  CB    . GLN A 25  ? 0.41950 0.39770 0.56690 -0.05890 0.04340  -0.08960 25  GLN A CB    
148  C  CG    . GLN A 25  ? 0.54310 0.53270 0.67230 -0.05730 0.03480  -0.08730 25  GLN A CG    
149  C  CD    . GLN A 25  ? 0.56040 0.55980 0.68390 -0.06150 0.02900  -0.09980 25  GLN A CD    
150  O  OE1   . GLN A 25  ? 0.77430 0.77200 0.90280 -0.06440 0.03170  -0.11080 25  GLN A OE1   
151  N  NE2   . GLN A 25  ? 0.56970 0.57970 0.68230 -0.06170 0.02090  -0.09820 25  GLN A NE2   
152  N  N     . PRO A 26  ? 0.40310 0.37610 0.56010 -0.05590 0.04750  -0.06660 26  PRO A N     
153  C  CA    . PRO A 26  ? 0.33120 0.30860 0.48420 -0.05440 0.04510  -0.05760 26  PRO A CA    
154  C  C     . PRO A 26  ? 0.37230 0.36240 0.51340 -0.05480 0.03550  -0.06010 26  PRO A C     
155  O  O     . PRO A 26  ? 0.37870 0.37520 0.51910 -0.05830 0.03090  -0.07030 26  PRO A O     
156  C  CB    . PRO A 26  ? 0.31590 0.29040 0.48620 -0.05890 0.05000  -0.05950 26  PRO A CB    
157  C  CG    . PRO A 26  ? 0.37940 0.35410 0.56030 -0.06460 0.05030  -0.07370 26  PRO A CG    
158  C  CD    . PRO A 26  ? 0.32640 0.29640 0.50060 -0.06200 0.05130  -0.07650 26  PRO A CD    
159  N  N     . PHE A 27  ? 0.33990 0.33320 0.47170 -0.05110 0.03290  -0.05070 27  PHE A N     
160  C  CA    . PHE A 27  ? 0.39640 0.40040 0.51930 -0.05110 0.02470  -0.05120 27  PHE A CA    
161  C  C     . PHE A 27  ? 0.38090 0.38710 0.50850 -0.05060 0.02530  -0.04510 27  PHE A C     
162  O  O     . PHE A 27  ? 0.36130 0.36190 0.48850 -0.04760 0.03020  -0.03620 27  PHE A O     
163  C  CB    . PHE A 27  ? 0.34580 0.35180 0.45210 -0.04680 0.02080  -0.04650 27  PHE A CB    
164  C  CG    . PHE A 27  ? 0.34680 0.35220 0.44740 -0.04730 0.02010  -0.05270 27  PHE A CG    
165  C  CD1   . PHE A 27  ? 0.32620 0.33940 0.42130 -0.05000 0.01410  -0.06090 27  PHE A CD1   
166  C  CD2   . PHE A 27  ? 0.34100 0.33860 0.44130 -0.04460 0.02560  -0.05030 27  PHE A CD2   
167  C  CE1   . PHE A 27  ? 0.38020 0.39350 0.46900 -0.05050 0.01410  -0.06690 27  PHE A CE1   
168  C  CE2   . PHE A 27  ? 0.34870 0.34640 0.44450 -0.04500 0.02560  -0.05650 27  PHE A CE2   
169  C  CZ    . PHE A 27  ? 0.40580 0.41130 0.49540 -0.04810 0.02010  -0.06510 27  PHE A CZ    
170  N  N     . GLN A 28  ? 0.32390 0.33890 0.45600 -0.05350 0.02030  -0.05010 28  GLN A N     
171  C  CA    . GLN A 28  ? 0.36210 0.38120 0.49920 -0.05320 0.02020  -0.04570 28  GLN A CA    
172  C  C     . GLN A 28  ? 0.37210 0.39650 0.49580 -0.04910 0.01420  -0.04020 28  GLN A C     
173  O  O     . GLN A 28  ? 0.30940 0.33640 0.42160 -0.04770 0.00880  -0.04150 28  GLN A O     
174  C  CB    . GLN A 28  ? 0.46660 0.49350 0.61710 -0.05810 0.01750  -0.05430 28  GLN A CB    
175  C  CG    . GLN A 28  ? 0.54940 0.57070 0.71600 -0.06290 0.02430  -0.06000 28  GLN A CG    
176  C  CD    . GLN A 28  ? 0.97840 1.00860 1.16030 -0.06830 0.02190  -0.06890 28  GLN A CD    
177  O  OE1   . GLN A 28  ? 0.99030 1.03140 1.16940 -0.06920 0.01330  -0.07530 28  GLN A OE1   
178  N  NE2   . GLN A 28  ? 1.00630 1.03240 1.20480 -0.07180 0.02950  -0.06930 28  GLN A NE2   
179  N  N     . VAL A 29  ? 0.34470 0.37050 0.47040 -0.04730 0.01570  -0.03420 29  VAL A N     
180  C  CA    . VAL A 29  ? 0.36070 0.39130 0.47660 -0.04370 0.01070  -0.02970 29  VAL A CA    
181  C  C     . VAL A 29  ? 0.30380 0.34310 0.41730 -0.04470 0.00180  -0.03550 29  VAL A C     
182  O  O     . VAL A 29  ? 0.27610 0.32150 0.40030 -0.04800 -0.00040 -0.04190 29  VAL A O     
183  C  CB    . VAL A 29  ? 0.31090 0.34340 0.43330 -0.04280 0.01390  -0.02520 29  VAL A CB    
184  C  CG1   . VAL A 29  ? 0.36680 0.40520 0.48230 -0.03960 0.00810  -0.02280 29  VAL A CG1   
185  C  CG2   . VAL A 29  ? 0.32210 0.34660 0.44270 -0.04080 0.02200  -0.01780 29  VAL A CG2   
186  N  N     . GLY A 30  ? 0.26440 0.30470 0.36410 -0.04190 -0.00310 -0.03310 30  GLY A N     
187  C  CA    . GLY A 30  ? 0.30760 0.35550 0.40220 -0.04190 -0.01150 -0.03650 30  GLY A CA    
188  C  C     . GLY A 30  ? 0.31810 0.36710 0.40700 -0.04410 -0.01430 -0.04280 30  GLY A C     
189  O  O     . GLY A 30  ? 0.37410 0.42900 0.45500 -0.04350 -0.02110 -0.04410 30  GLY A O     
190  N  N     . ASP A 31  ? 0.32320 0.36660 0.41630 -0.04650 -0.00870 -0.04640 31  ASP A N     
191  C  CA    . ASP A 31  ? 0.36760 0.41130 0.45580 -0.04870 -0.01000 -0.05330 31  ASP A CA    
192  C  C     . ASP A 31  ? 0.33580 0.37710 0.40790 -0.04590 -0.01110 -0.04930 31  ASP A C     
193  O  O     . ASP A 31  ? 0.26380 0.29920 0.33160 -0.04290 -0.00750 -0.04210 31  ASP A O     
194  C  CB    . ASP A 31  ? 0.35410 0.39050 0.45210 -0.05140 -0.00250 -0.05760 31  ASP A CB    
195  C  CG    . ASP A 31  ? 0.45140 0.49080 0.56620 -0.05580 -0.00130 -0.06450 31  ASP A CG    
196  O  OD1   . ASP A 31  ? 0.52980 0.57780 0.64920 -0.05680 -0.00650 -0.06630 31  ASP A OD1   
197  O  OD2   . ASP A 31  ? 0.57860 0.61140 0.70300 -0.05840 0.00510  -0.06840 31  ASP A OD2   
198  N  N     . LEU A 32  ? 0.27600 0.32250 0.33950 -0.04710 -0.01590 -0.05430 32  LEU A N     
199  C  CA    . LEU A 32  ? 0.34280 0.38760 0.39180 -0.04540 -0.01620 -0.05220 32  LEU A CA    
200  C  C     . LEU A 32  ? 0.36820 0.40680 0.41880 -0.04660 -0.00980 -0.05620 32  LEU A C     
201  O  O     . LEU A 32  ? 0.39140 0.43150 0.44660 -0.04990 -0.00910 -0.06530 32  LEU A O     
202  C  CB    . LEU A 32  ? 0.34010 0.39360 0.37900 -0.04640 -0.02360 -0.05600 32  LEU A CB    
203  C  CG    . LEU A 32  ? 0.30430 0.35770 0.32700 -0.04510 -0.02430 -0.05360 32  LEU A CG    
204  C  CD1   . LEU A 32  ? 0.27410 0.32370 0.29070 -0.04150 -0.02390 -0.04330 32  LEU A CD1   
205  C  CD2   . LEU A 32  ? 0.32190 0.38470 0.33520 -0.04640 -0.03150 -0.05760 32  LEU A CD2   
206  N  N     . LEU A 33  ? 0.38780 0.41970 0.43530 -0.04370 -0.00510 -0.04990 33  LEU A N     
207  C  CA    . LEU A 33  ? 0.31030 0.33640 0.35910 -0.04360 0.00090  -0.05270 33  LEU A CA    
208  C  C     . LEU A 33  ? 0.31470 0.34440 0.35190 -0.04450 -0.00070 -0.05720 33  LEU A C     
209  O  O     . LEU A 33  ? 0.34850 0.37790 0.38810 -0.04680 0.00160  -0.06570 33  LEU A O     
210  C  CB    . LEU A 33  ? 0.28120 0.30080 0.33010 -0.03980 0.00560  -0.04420 33  LEU A CB    
211  C  CG    . LEU A 33  ? 0.35070 0.36460 0.41160 -0.03890 0.01020  -0.04060 33  LEU A CG    
212  C  CD1   . LEU A 33  ? 0.36000 0.37730 0.42360 -0.03910 0.00700  -0.03710 33  LEU A CD1   
213  C  CD2   . LEU A 33  ? 0.30640 0.31490 0.36600 -0.03490 0.01460  -0.03330 33  LEU A CD2   
214  N  N     . PHE A 34  ? 0.29180 0.32460 0.31670 -0.04270 -0.00420 -0.05160 34  PHE A N     
215  C  CA    . PHE A 34  ? 0.29320 0.33000 0.30530 -0.04340 -0.00570 -0.05430 34  PHE A CA    
216  C  C     . PHE A 34  ? 0.32850 0.36870 0.32890 -0.04180 -0.01030 -0.04690 34  PHE A C     
217  O  O     . PHE A 34  ? 0.27920 0.31750 0.28180 -0.03960 -0.01160 -0.03970 34  PHE A O     
218  C  CB    . PHE A 34  ? 0.30180 0.33430 0.31330 -0.04260 0.00070  -0.05600 34  PHE A CB    
219  C  CG    . PHE A 34  ? 0.29720 0.32530 0.30870 -0.03910 0.00370  -0.04730 34  PHE A CG    
220  C  CD1   . PHE A 34  ? 0.31950 0.34220 0.34140 -0.03690 0.00660  -0.04300 34  PHE A CD1   
221  C  CD2   . PHE A 34  ? 0.28200 0.31190 0.28310 -0.03800 0.00380  -0.04360 34  PHE A CD2   
222  C  CE1   . PHE A 34  ? 0.27970 0.30000 0.30110 -0.03360 0.00870  -0.03560 34  PHE A CE1   
223  C  CE2   . PHE A 34  ? 0.35520 0.38250 0.35740 -0.03510 0.00610  -0.03670 34  PHE A CE2   
224  C  CZ    . PHE A 34  ? 0.27660 0.29940 0.28850 -0.03280 0.00820  -0.03290 34  PHE A CZ    
225  N  N     . SER A 35  ? 0.38130 0.42610 0.36920 -0.04290 -0.01260 -0.04890 35  SER A N     
226  C  CA    . SER A 35  ? 0.42490 0.47180 0.40070 -0.04150 -0.01570 -0.04180 35  SER A CA    
227  C  C     . SER A 35  ? 0.44730 0.49300 0.41500 -0.04170 -0.01090 -0.04160 35  SER A C     
228  O  O     . SER A 35  ? 0.47860 0.52410 0.44800 -0.04300 -0.00670 -0.04860 35  SER A O     
229  C  CB    . SER A 35  ? 0.42360 0.47800 0.39100 -0.04260 -0.02280 -0.04320 35  SER A CB    
230  O  OG    . SER A 35  ? 0.66440 0.72360 0.62690 -0.04540 -0.02260 -0.05230 35  SER A OG    
231  N  N     . CYS A 36  ? 0.37160 0.41650 0.33180 -0.04030 -0.01120 -0.03380 36  CYS A N     
232  C  CA    . CYS A 36  ? 0.37020 0.41440 0.32370 -0.04050 -0.00630 -0.03270 36  CYS A CA    
233  C  C     . CYS A 36  ? 0.32740 0.37330 0.26850 -0.04060 -0.00870 -0.02590 36  CYS A C     
234  O  O     . CYS A 36  ? 0.33070 0.37380 0.27330 -0.03910 -0.01050 -0.01860 36  CYS A O     
235  C  CB    . CYS A 36  ? 0.43380 0.47300 0.39660 -0.03860 -0.00160 -0.02970 36  CYS A CB    
236  S  SG    . CYS A 36  ? 0.40320 0.44290 0.36180 -0.03880 0.00490  -0.02980 36  CYS A SG    
237  N  N     . PRO A 37  ? 0.28340 0.33370 0.21190 -0.04250 -0.00850 -0.02790 37  PRO A N     
238  C  CA    . PRO A 37  ? 0.32680 0.37780 0.24310 -0.04260 -0.00930 -0.02050 37  PRO A CA    
239  C  C     . PRO A 37  ? 0.31810 0.36490 0.23710 -0.04230 -0.00390 -0.01550 37  PRO A C     
240  O  O     . PRO A 37  ? 0.38160 0.42780 0.30680 -0.04250 0.00140  -0.01970 37  PRO A O     
241  C  CB    . PRO A 37  ? 0.31210 0.36900 0.21480 -0.04490 -0.00820 -0.02520 37  PRO A CB    
242  C  CG    . PRO A 37  ? 0.39060 0.45080 0.29850 -0.04590 -0.00940 -0.03590 37  PRO A CG    
243  C  CD    . PRO A 37  ? 0.38060 0.43530 0.30570 -0.04460 -0.00690 -0.03770 37  PRO A CD    
244  N  N     . ALA A 38  ? 0.38370 0.42790 0.29890 -0.04170 -0.00530 -0.00690 38  ALA A N     
245  C  CA    . ALA A 38  ? 0.37690 0.41790 0.29480 -0.04200 -0.00050 -0.00250 38  ALA A CA    
246  C  C     . ALA A 38  ? 0.37480 0.41890 0.28540 -0.04430 0.00560  -0.00480 38  ALA A C     
247  O  O     . ALA A 38  ? 0.36040 0.40760 0.25810 -0.04580 0.00540  -0.00440 38  ALA A O     
248  C  CB    . ALA A 38  ? 0.36060 0.39790 0.27560 -0.04150 -0.00320 0.00650  38  ALA A CB    
249  N  N     . TYR A 39  ? 0.33300 0.37690 0.25190 -0.04450 0.01110  -0.00760 39  TYR A N     
250  C  CA    . TYR A 39  ? 0.35000 0.39700 0.26490 -0.04660 0.01810  -0.00960 39  TYR A CA    
251  C  C     . TYR A 39  ? 0.35410 0.39970 0.26250 -0.04840 0.01990  -0.00160 39  TYR A C     
252  O  O     . TYR A 39  ? 0.35980 0.40810 0.25710 -0.05070 0.02360  -0.00080 39  TYR A O     
253  C  CB    . TYR A 39  ? 0.32520 0.37290 0.25330 -0.04540 0.02270  -0.01400 39  TYR A CB    
254  C  CG    . TYR A 39  ? 0.34070 0.39240 0.26740 -0.04730 0.03010  -0.01630 39  TYR A CG    
255  C  CD1   . TYR A 39  ? 0.34950 0.40510 0.27340 -0.04790 0.03410  -0.02400 39  TYR A CD1   
256  C  CD2   . TYR A 39  ? 0.31970 0.37160 0.24870 -0.04860 0.03340  -0.01140 39  TYR A CD2   
257  C  CE1   . TYR A 39  ? 0.37060 0.43050 0.29370 -0.04960 0.04150  -0.02650 39  TYR A CE1   
258  C  CE2   . TYR A 39  ? 0.35500 0.41140 0.28390 -0.05060 0.04060  -0.01370 39  TYR A CE2   
259  C  CZ    . TYR A 39  ? 0.35500 0.41550 0.28090 -0.05090 0.04480  -0.02110 39  TYR A CZ    
260  O  OH    . TYR A 39  ? 0.43940 0.50500 0.36590 -0.05270 0.05250  -0.02370 39  TYR A OH    
261  N  N     . ALA A 40  ? 0.40220 0.44340 0.31780 -0.04750 0.01780  0.00390  40  ALA A N     
262  C  CA    . ALA A 40  ? 0.33200 0.37000 0.24410 -0.04910 0.01900  0.01180  40  ALA A CA    
263  C  C     . ALA A 40  ? 0.36000 0.39280 0.27840 -0.04710 0.01350  0.01620  40  ALA A C     
264  O  O     . ALA A 40  ? 0.34590 0.37830 0.27380 -0.04490 0.01080  0.01300  40  ALA A O     
265  C  CB    . ALA A 40  ? 0.33660 0.37620 0.25520 -0.05120 0.02570  0.01130  40  ALA A CB    
266  N  N     . TYR A 41  ? 0.29850 0.32690 0.21140 -0.04780 0.01230  0.02380  41  TYR A N     
267  C  CA    . TYR A 41  ? 0.33340 0.35640 0.25170 -0.04580 0.00730  0.02830  41  TYR A CA    
268  C  C     . TYR A 41  ? 0.34820 0.36560 0.26320 -0.04750 0.00910  0.03650  41  TYR A C     
269  O  O     . TYR A 41  ? 0.36410 0.38200 0.26930 -0.04990 0.01310  0.04000  41  TYR A O     
270  C  CB    . TYR A 41  ? 0.30290 0.32650 0.21730 -0.04300 0.00050  0.02810  41  TYR A CB    
271  C  CG    . TYR A 41  ? 0.36920 0.39470 0.26880 -0.04340 -0.00120 0.03160  41  TYR A CG    
272  C  CD1   . TYR A 41  ? 0.40570 0.43730 0.29710 -0.04460 0.00030  0.02630  41  TYR A CD1   
273  C  CD2   . TYR A 41  ? 0.37070 0.39200 0.26450 -0.04240 -0.00410 0.04030  41  TYR A CD2   
274  C  CE1   . TYR A 41  ? 0.43290 0.46750 0.30930 -0.04490 -0.00150 0.02910  41  TYR A CE1   
275  C  CE2   . TYR A 41  ? 0.40940 0.43310 0.28840 -0.04230 -0.00610 0.04430  41  TYR A CE2   
276  C  CZ    . TYR A 41  ? 0.37950 0.41040 0.24910 -0.04370 -0.00490 0.03860  41  TYR A CZ    
277  O  OH    . TYR A 41  ? 0.48370 0.51820 0.33740 -0.04350 -0.00710 0.04220  41  TYR A OH    
278  N  N     . VAL A 42  ? 0.32370 0.33560 0.24690 -0.04630 0.00670  0.03950  42  VAL A N     
279  C  CA    . VAL A 42  ? 0.37100 0.37590 0.29330 -0.04750 0.00810  0.04730  42  VAL A CA    
280  C  C     . VAL A 42  ? 0.30850 0.30800 0.23700 -0.04430 0.00270  0.04990  42  VAL A C     
281  O  O     . VAL A 42  ? 0.32410 0.32470 0.26220 -0.04260 0.00040  0.04490  42  VAL A O     
282  C  CB    . VAL A 42  ? 0.42080 0.42460 0.35080 -0.05120 0.01470  0.04650  42  VAL A CB    
283  C  CG1   . VAL A 42  ? 0.41510 0.42070 0.35900 -0.05050 0.01370  0.04020  42  VAL A CG1   
284  C  CG2   . VAL A 42  ? 0.60980 0.60560 0.53910 -0.05320 0.01720  0.05460  42  VAL A CG2   
285  N  N     . LEU A 43  ? 0.34120 0.33510 0.26390 -0.04310 0.00070  0.05810  43  LEU A N     
286  C  CA    . LEU A 43  ? 0.40310 0.39120 0.33260 -0.03990 -0.00380 0.06150  43  LEU A CA    
287  C  C     . LEU A 43  ? 0.35980 0.34110 0.30000 -0.04200 0.00030  0.06210  43  LEU A C     
288  O  O     . LEU A 43  ? 0.38450 0.36240 0.32310 -0.04560 0.00580  0.06560  43  LEU A O     
289  C  CB    . LEU A 43  ? 0.40150 0.38600 0.32130 -0.03750 -0.00720 0.07070  43  LEU A CB    
290  C  CG    . LEU A 43  ? 0.40240 0.38140 0.32920 -0.03320 -0.01240 0.07470  43  LEU A CG    
291  C  CD1   . LEU A 43  ? 0.38080 0.36630 0.31120 -0.02970 -0.01880 0.06890  43  LEU A CD1   
292  C  CD2   . LEU A 43  ? 0.44240 0.41620 0.36030 -0.03110 -0.01420 0.08590  43  LEU A CD2   
293  N  N     . THR A 44  ? 0.34520 0.32520 0.29680 -0.04020 -0.00210 0.05800  44  THR A N     
294  C  CA    . THR A 44  ? 0.40070 0.37540 0.36340 -0.04230 0.00130  0.05650  44  THR A CA    
295  C  C     . THR A 44  ? 0.42110 0.38530 0.38410 -0.04220 0.00250  0.06520  44  THR A C     
296  O  O     . THR A 44  ? 0.40890 0.37000 0.36670 -0.03860 -0.00150 0.07150  44  THR A O     
297  C  CB    . THR A 44  ? 0.32720 0.30370 0.30050 -0.04000 -0.00160 0.04970  44  THR A CB    
298  O  OG1   . THR A 44  ? 0.38260 0.35650 0.36570 -0.04290 0.00210  0.04620  44  THR A OG1   
299  C  CG2   . THR A 44  ? 0.35590 0.32810 0.33160 -0.03550 -0.00650 0.05280  44  THR A CG2   
300  N  N     . VAL A 45  ? 0.44350 0.40240 0.41300 -0.04630 0.00800  0.06560  45  VAL A N     
301  C  CA    . VAL A 45  ? 0.46960 0.41740 0.43970 -0.04730 0.01100  0.07440  45  VAL A CA    
302  C  C     . VAL A 45  ? 0.51670 0.45710 0.49190 -0.04240 0.00650  0.07820  45  VAL A C     
303  O  O     . VAL A 45  ? 0.53570 0.46910 0.50540 -0.04020 0.00570  0.08810  45  VAL A O     
304  C  CB    . VAL A 45  ? 0.53300 0.47690 0.51310 -0.05310 0.01790  0.07180  45  VAL A CB    
305  C  CG1   . VAL A 45  ? 0.55600 0.48630 0.54110 -0.05380 0.02100  0.07960  45  VAL A CG1   
306  C  CG2   . VAL A 45  ? 0.49080 0.44080 0.46470 -0.05770 0.02320  0.07120  45  VAL A CG2   
307  N  N     . ASN A 46  ? 0.57220 0.51440 0.55750 -0.04040 0.00370  0.07070  46  ASN A N     
308  C  CA    . ASN A 46  ? 0.66830 0.60410 0.66110 -0.03580 0.00010  0.07250  46  ASN A CA    
309  C  C     . ASN A 46  ? 0.60580 0.54390 0.59150 -0.03000 -0.00650 0.07770  46  ASN A C     
310  O  O     . ASN A 46  ? 0.55510 0.48730 0.54670 -0.02580 -0.00930 0.08150  46  ASN A O     
311  C  CB    . ASN A 46  ? 0.76210 0.70080 0.76650 -0.03540 -0.00070 0.06210  46  ASN A CB    
312  C  CG    . ASN A 46  ? 0.70290 0.63680 0.71780 -0.04010 0.00480  0.05740  46  ASN A CG    
313  O  OD1   . ASN A 46  ? 0.79430 0.71920 0.81140 -0.04280 0.00900  0.06290  46  ASN A OD1   
314  N  ND2   . ASN A 46  ? 0.99630 0.93640 1.01790 -0.04120 0.00470  0.04730  46  ASN A ND2   
315  N  N     . GLU A 47  ? 0.55310 0.50040 0.52750 -0.02980 -0.00890 0.07730  47  GLU A N     
316  C  CA    . GLU A 47  ? 0.50710 0.45880 0.47460 -0.02500 -0.01560 0.08110  47  GLU A CA    
317  C  C     . GLU A 47  ? 0.50530 0.45560 0.45900 -0.02450 -0.01620 0.09130  47  GLU A C     
318  O  O     . GLU A 47  ? 0.56990 0.52550 0.51630 -0.02070 -0.02210 0.09420  47  GLU A O     
319  C  CB    . GLU A 47  ? 0.48830 0.45160 0.45350 -0.02480 -0.01850 0.07280  47  GLU A CB    
320  C  CG    . GLU A 47  ? 0.56230 0.52780 0.53970 -0.02390 -0.01910 0.06410  47  GLU A CG    
321  C  CD    . GLU A 47  ? 0.61460 0.57700 0.60070 -0.01890 -0.02320 0.06550  47  GLU A CD    
322  O  OE1   . GLU A 47  ? 0.57280 0.53420 0.55530 -0.01520 -0.02750 0.07240  47  GLU A OE1   
323  O  OE2   . GLU A 47  ? 0.63400 0.59570 0.63080 -0.01850 -0.02220 0.05950  47  GLU A OE2   
324  N  N     . ARG A 48  ? 0.48570 0.42940 0.43580 -0.02830 -0.01010 0.09670  48  ARG A N     
325  C  CA    . ARG A 48  ? 0.59160 0.53230 0.52810 -0.02800 -0.00940 0.10800  48  ARG A CA    
326  C  C     . ARG A 48  ? 0.53600 0.46930 0.47430 -0.02210 -0.01400 0.11780  48  ARG A C     
327  O  O     . ARG A 48  ? 0.58260 0.50720 0.53480 -0.02090 -0.01290 0.11780  48  ARG A O     
328  C  CB    . ARG A 48  ? 0.62780 0.56190 0.56340 -0.03380 -0.00050 0.11140  48  ARG A CB    
329  C  CG    . ARG A 48  ? 0.65260 0.59490 0.58510 -0.03920 0.00410  0.10320  48  ARG A CG    
330  C  CD    . ARG A 48  ? 0.62480 0.56080 0.56110 -0.04520 0.01300  0.10510  48  ARG A CD    
331  N  NE    . ARG A 48  ? 0.66940 0.61370 0.59940 -0.04990 0.01770  0.10040  48  ARG A NE    
332  C  CZ    . ARG A 48  ? 0.78530 0.72730 0.71880 -0.05560 0.02580  0.10040  48  ARG A CZ    
333  N  NH1   . ARG A 48  ? 0.59670 0.52780 0.53970 -0.05790 0.03020  0.10480  48  ARG A NH1   
334  N  NH2   . ARG A 48  ? 0.67200 0.62270 0.60070 -0.05920 0.02980  0.09560  48  ARG A NH2   
335  N  N     . GLY A 49  ? 0.67510 0.61240 0.60030 -0.01850 -0.01910 0.12540  49  GLY A N     
336  C  CA    . GLY A 49  ? 0.71810 0.65040 0.64450 -0.01190 -0.02460 0.13520  49  GLY A CA    
337  C  C     . GLY A 49  ? 0.64990 0.59060 0.58180 -0.00640 -0.03350 0.13030  49  GLY A C     
338  O  O     . GLY A 49  ? 0.63520 0.57690 0.56420 -0.00060 -0.03990 0.13800  49  GLY A O     
339  N  N     . ASN A 50  ? 0.62260 0.56980 0.56310 -0.00830 -0.03360 0.11770  50  ASN A N     
340  C  CA    . ASN A 50  ? 0.61540 0.57180 0.56190 -0.00420 -0.04080 0.11140  50  ASN A CA    
341  C  C     . ASN A 50  ? 0.60500 0.57470 0.54040 -0.00580 -0.04420 0.10570  50  ASN A C     
342  O  O     . ASN A 50  ? 0.59580 0.57390 0.53130 -0.00200 -0.05140 0.10410  50  ASN A O     
343  C  CB    . ASN A 50  ? 0.60490 0.55980 0.56770 -0.00520 -0.03850 0.10150  50  ASN A CB    
344  C  CG    . ASN A 50  ? 0.87140 0.81350 0.84660 -0.00390 -0.03510 0.10500  50  ASN A CG    
345  O  OD1   . ASN A 50  ? 1.13550 1.07080 1.11180 0.00050  -0.03720 0.11470  50  ASN A OD1   
346  N  ND2   . ASN A 50  ? 0.80240 0.74150 0.78740 -0.00750 -0.02980 0.09690  50  ASN A ND2   
347  N  N     . HIS A 51  ? 0.63210 0.60370 0.55900 -0.01130 -0.03870 0.10210  51  HIS A N     
348  C  CA    . HIS A 51  ? 0.55490 0.53800 0.47230 -0.01350 -0.04030 0.09540  51  HIS A CA    
349  C  C     . HIS A 51  ? 0.56110 0.54520 0.46120 -0.01650 -0.03710 0.10030  51  HIS A C     
350  O  O     . HIS A 51  ? 0.69990 0.67590 0.59770 -0.01920 -0.03070 0.10580  51  HIS A O     
351  C  CB    . HIS A 51  ? 0.57620 0.56190 0.50190 -0.01730 -0.03620 0.08400  51  HIS A CB    
352  C  CG    . HIS A 51  ? 0.47500 0.46180 0.41550 -0.01470 -0.03900 0.07790  51  HIS A CG    
353  N  ND1   . HIS A 51  ? 0.50300 0.49900 0.44620 -0.01390 -0.04300 0.07050  51  HIS A ND1   
354  C  CD2   . HIS A 51  ? 0.56880 0.54880 0.52250 -0.01310 -0.03790 0.07790  51  HIS A CD2   
355  C  CE1   . HIS A 51  ? 0.54760 0.54260 0.50450 -0.01180 -0.04400 0.06670  51  HIS A CE1   
356  N  NE2   . HIS A 51  ? 0.46790 0.45350 0.43100 -0.01120 -0.04100 0.07080  51  HIS A NE2   
357  N  N     . CYS A 52  ? 0.49590 0.49050 0.38450 -0.01640 -0.04120 0.09760  52  CYS A N     
358  C  CA    . CYS A 52  ? 0.47930 0.47750 0.35060 -0.01950 -0.03790 0.09990  52  CYS A CA    
359  C  C     . CYS A 52  ? 0.51130 0.51000 0.38480 -0.02510 -0.03010 0.09140  52  CYS A C     
360  O  O     . CYS A 52  ? 0.45390 0.45680 0.33650 -0.02600 -0.03040 0.08140  52  CYS A O     
361  C  CB    . CYS A 52  ? 0.43330 0.44370 0.29320 -0.01770 -0.04500 0.09700  52  CYS A CB    
362  S  SG    . CYS A 52  ? 0.53070 0.54830 0.36960 -0.02180 -0.04120 0.09590  52  CYS A SG    
363  N  N     . GLU A 53  ? 0.48270 0.47720 0.34840 -0.02880 -0.02280 0.09600  53  GLU A N     
364  C  CA    . GLU A 53  ? 0.58360 0.57890 0.45230 -0.03390 -0.01500 0.08900  53  GLU A CA    
365  C  C     . GLU A 53  ? 0.55990 0.56600 0.42290 -0.03540 -0.01560 0.07900  53  GLU A C     
366  O  O     . GLU A 53  ? 0.46320 0.47140 0.33490 -0.03770 -0.01220 0.07030  53  GLU A O     
367  C  CB    . GLU A 53  ? 0.64150 0.63140 0.50230 -0.03760 -0.00710 0.09650  53  GLU A CB    
368  C  CG    . GLU A 53  ? 0.65630 0.63390 0.52480 -0.03730 -0.00450 0.10560  53  GLU A CG    
369  C  CD    . GLU A 53  ? 0.59020 0.56300 0.47460 -0.04080 0.00130  0.10000  53  GLU A CD    
370  O  OE1   . GLU A 53  ? 0.63900 0.61770 0.52610 -0.04420 0.00520  0.09130  53  GLU A OE1   
371  O  OE2   . GLU A 53  ? 0.71860 0.68190 0.61330 -0.04010 0.00200  0.10430  53  GLU A OE2   
372  N  N     . TYR A 54  ? 0.46320 0.47650 0.31200 -0.03400 -0.02000 0.08010  54  TYR A N     
373  C  CA    . TYR A 54  ? 0.43010 0.45360 0.27190 -0.03590 -0.02000 0.07030  54  TYR A CA    
374  C  C     . TYR A 54  ? 0.52540 0.55370 0.37860 -0.03410 -0.02560 0.06070  54  TYR A C     
375  O  O     . TYR A 54  ? 0.52470 0.55560 0.38440 -0.03640 -0.02200 0.05130  54  TYR A O     
376  C  CB    . TYR A 54  ? 0.46960 0.49990 0.29160 -0.03530 -0.02290 0.07400  54  TYR A CB    
377  C  CG    . TYR A 54  ? 0.52270 0.56310 0.33780 -0.03770 -0.02200 0.06290  54  TYR A CG    
378  C  CD1   . TYR A 54  ? 0.49720 0.53820 0.31210 -0.04180 -0.01330 0.05730  54  TYR A CD1   
379  C  CD2   . TYR A 54  ? 0.54370 0.59320 0.35460 -0.03580 -0.02970 0.05720  54  TYR A CD2   
380  C  CE1   . TYR A 54  ? 0.62370 0.67310 0.43380 -0.04380 -0.01180 0.04650  54  TYR A CE1   
381  C  CE2   . TYR A 54  ? 0.63150 0.68970 0.43740 -0.03830 -0.02840 0.04590  54  TYR A CE2   
382  C  CZ    . TYR A 54  ? 0.65090 0.70850 0.45640 -0.04220 -0.01930 0.04060  54  TYR A CZ    
383  O  OH    . TYR A 54  ? 0.70760 0.77300 0.50920 -0.04440 -0.01750 0.02910  54  TYR A OH    
384  N  N     . CYS A 55  ? 0.47430 0.50400 0.33010 -0.03000 -0.03380 0.06330  55  CYS A N     
385  C  CA    . CYS A 55  ? 0.54450 0.58050 0.40960 -0.02860 -0.03930 0.05440  55  CYS A CA    
386  C  C     . CYS A 55  ? 0.43000 0.46100 0.31270 -0.02610 -0.04150 0.05420  55  CYS A C     
387  O  O     . CYS A 55  ? 0.53280 0.56840 0.42430 -0.02520 -0.04510 0.04720  55  CYS A O     
388  C  CB    . CYS A 55  ? 0.64400 0.68900 0.49880 -0.02620 -0.04750 0.05480  55  CYS A CB    
389  S  SG    . CYS A 55  ? 0.65780 0.70000 0.51380 -0.02050 -0.05510 0.06670  55  CYS A SG    
390  N  N     . PHE A 56  ? 0.43140 0.45310 0.31900 -0.02530 -0.03870 0.06150  56  PHE A N     
391  C  CA    . PHE A 56  ? 0.41090 0.42710 0.31470 -0.02340 -0.03920 0.06110  56  PHE A CA    
392  C  C     . PHE A 56  ? 0.58940 0.60730 0.49950 -0.01860 -0.04700 0.06360  56  PHE A C     
393  O  O     . PHE A 56  ? 0.42560 0.43990 0.34930 -0.01680 -0.04730 0.06230  56  PHE A O     
394  C  CB    . PHE A 56  ? 0.43170 0.44940 0.34580 -0.02560 -0.03560 0.05120  56  PHE A CB    
395  C  CG    . PHE A 56  ? 0.41950 0.43240 0.33550 -0.02900 -0.02790 0.05040  56  PHE A CG    
396  C  CD1   . PHE A 56  ? 0.42650 0.43760 0.33220 -0.03160 -0.02320 0.05470  56  PHE A CD1   
397  C  CD2   . PHE A 56  ? 0.39560 0.40690 0.32380 -0.02960 -0.02520 0.04510  56  PHE A CD2   
398  C  CE1   . PHE A 56  ? 0.37620 0.38410 0.28540 -0.03490 -0.01620 0.05330  56  PHE A CE1   
399  C  CE2   . PHE A 56  ? 0.40420 0.41260 0.33480 -0.03240 -0.01890 0.04390  56  PHE A CE2   
400  C  CZ    . PHE A 56  ? 0.39060 0.39760 0.31250 -0.03520 -0.01440 0.04770  56  PHE A CZ    
401  N  N     . THR A 57  ? 0.56010 0.58410 0.46040 -0.01630 -0.05320 0.06710  57  THR A N     
402  C  CA    . THR A 57  ? 0.59960 0.62700 0.50560 -0.01130 -0.06130 0.07000  57  THR A CA    
403  C  C     . THR A 57  ? 0.58490 0.60220 0.49720 -0.00780 -0.06100 0.07960  57  THR A C     
404  O  O     . THR A 57  ? 0.53340 0.54390 0.43710 -0.00810 -0.05800 0.08830  57  THR A O     
405  C  CB    . THR A 57  ? 0.71850 0.75510 0.61050 -0.00950 -0.06820 0.07290  57  THR A CB    
406  O  OG1   . THR A 57  ? 0.69740 0.74310 0.58360 -0.01300 -0.06800 0.06300  57  THR A OG1   
407  C  CG2   . THR A 57  ? 0.73130 0.77320 0.63110 -0.00390 -0.07740 0.07520  57  THR A CG2   
408  N  N     . ARG A 58  ? 0.56660 0.58280 0.49450 -0.00470 -0.06360 0.07770  58  ARG A N     
409  C  CA    . ARG A 58  ? 0.58930 0.59630 0.52620 -0.00080 -0.06380 0.08540  58  ARG A CA    
410  C  C     . ARG A 58  ? 0.75560 0.76680 0.68960 0.00510  -0.07240 0.09320  58  ARG A C     
411  O  O     . ARG A 58  ? 0.66990 0.69170 0.60790 0.00720  -0.07890 0.08830  58  ARG A O     
412  C  CB    . ARG A 58  ? 0.57820 0.58320 0.53290 -0.00010 -0.06230 0.07860  58  ARG A CB    
413  C  CG    . ARG A 58  ? 0.68730 0.68210 0.65280 0.00330  -0.06100 0.08450  58  ARG A CG    
414  C  CD    . ARG A 58  ? 0.64090 0.63530 0.62320 0.00430  -0.05970 0.07710  58  ARG A CD    
415  N  NE    . ARG A 58  ? 0.98970 0.99540 0.97750 0.00580  -0.06480 0.07080  58  ARG A NE    
416  C  CZ    . ARG A 58  ? 1.31890 1.33010 1.31090 0.00270  -0.06260 0.06130  58  ARG A CZ    
417  N  NH1   . ARG A 58  ? 0.90870 0.91570 0.90000 -0.00150 -0.05590 0.05700  58  ARG A NH1   
418  N  NH2   . ARG A 58  ? 1.05870 1.07970 1.05640 0.00400  -0.06720 0.05640  58  ARG A NH2   
419  N  N     . LYS A 59  ? 0.78530 0.78860 0.71330 0.00770  -0.07220 0.10500  59  LYS A N     
420  C  CA    . LYS A 59  ? 0.86020 0.86590 0.78660 0.01440  -0.08020 0.11440  59  LYS A CA    
421  C  C     . LYS A 59  ? 0.82760 0.81960 0.75250 0.01690  -0.07710 0.12750  59  LYS A C     
422  O  O     . LYS A 59  ? 0.86660 0.84880 0.78850 0.01260  -0.06890 0.12930  59  LYS A O     
423  C  CB    . LYS A 59  ? 0.85490 0.87310 0.76450 0.01470  -0.08660 0.11550  59  LYS A CB    
424  C  CG    . LYS A 59  ? 0.92150 0.93720 0.81130 0.01060  -0.08160 0.12020  59  LYS A CG    
425  C  CD    . LYS A 59  ? 0.89070 0.91890 0.76270 0.01200  -0.08860 0.12250  59  LYS A CD    
426  C  CE    . LYS A 59  ? 0.93030 0.97210 0.80200 0.00860  -0.09140 0.10840  59  LYS A CE    
427  N  NZ    . LYS A 59  ? 1.26370 1.31800 1.11670 0.00890  -0.09720 0.10900  59  LYS A NZ    
428  N  N     . GLU A 60  ? 0.97200 0.96370 0.90030 0.02410  -0.08380 0.13660  60  GLU A N     
429  C  CA    . GLU A 60  ? 1.09830 1.07680 1.02520 0.02760  -0.08180 0.15070  60  GLU A CA    
430  C  C     . GLU A 60  ? 1.15260 1.13360 1.05740 0.02800  -0.08380 0.16160  60  GLU A C     
431  O  O     . GLU A 60  ? 0.85150 0.84650 0.74460 0.02870  -0.09040 0.15930  60  GLU A O     
432  C  CB    . GLU A 60  ? 1.09260 1.06910 1.03520 0.03580  -0.08780 0.15590  60  GLU A CB    
433  C  CG    . GLU A 60  ? 1.16390 1.13650 1.12850 0.03580  -0.08480 0.14620  60  GLU A CG    
434  C  CD    . GLU A 60  ? 1.31820 1.27500 1.28920 0.03150  -0.07430 0.14570  60  GLU A CD    
435  O  OE1   . GLU A 60  ? 1.43490 1.38110 1.39710 0.03000  -0.06970 0.15530  60  GLU A OE1   
436  O  OE2   . GLU A 60  ? 1.16160 1.11690 1.14670 0.02940  -0.07060 0.13540  60  GLU A OE2   
437  N  N     . GLY A 61  ? 1.02400 0.99130 0.92300 0.02740  -0.07750 0.17310  61  GLY A N     
438  C  CA    . GLY A 61  ? 0.92910 0.89650 0.80690 0.02810  -0.07800 0.18550  61  GLY A CA    
439  C  C     . GLY A 61  ? 0.97490 0.94990 0.83450 0.02100  -0.07400 0.17980  61  GLY A C     
440  O  O     . GLY A 61  ? 0.82040 0.80630 0.66210 0.02210  -0.07920 0.18300  61  GLY A O     
441  N  N     . LEU A 62  ? 0.70140 0.67130 0.56610 0.01380  -0.06480 0.17090  62  LEU A N     
442  C  CA    . LEU A 62  ? 0.65870 0.63390 0.50900 0.00680  -0.05910 0.16550  62  LEU A CA    
443  C  C     . LEU A 62  ? 0.75550 0.72200 0.59060 0.00490  -0.05250 0.17880  62  LEU A C     
444  O  O     . LEU A 62  ? 0.85430 0.80640 0.69640 0.00600  -0.04800 0.18840  62  LEU A O     
445  C  CB    . LEU A 62  ? 0.66620 0.63880 0.52890 0.00050  -0.05180 0.15240  62  LEU A CB    
446  C  CG    . LEU A 62  ? 0.60130 0.58280 0.47700 0.00100  -0.05640 0.13850  62  LEU A CG    
447  C  CD1   . LEU A 62  ? 0.55550 0.53120 0.44530 -0.00390 -0.04900 0.12900  62  LEU A CD1   
448  C  CD2   . LEU A 62  ? 0.68080 0.67760 0.54450 -0.00050 -0.06090 0.13070  62  LEU A CD2   
449  N  N     . SER A 63  ? 0.94300 0.91820 0.75790 0.00190  -0.05140 0.17880  63  SER A N     
450  C  CA    . SER A 63  ? 0.80520 0.77420 0.60360 -0.00070 -0.04410 0.19040  63  SER A CA    
451  C  C     . SER A 63  ? 0.84300 0.80190 0.64950 -0.00810 -0.03180 0.18650  63  SER A C     
452  O  O     . SER A 63  ? 0.75610 0.72070 0.56740 -0.01310 -0.02850 0.17290  63  SER A O     
453  C  CB    . SER A 63  ? 0.82760 0.81050 0.60210 -0.00220 -0.04610 0.18910  63  SER A CB    
454  O  OG    . SER A 63  ? 1.09790 1.09120 0.86670 0.00460  -0.05750 0.18850  63  SER A OG    
455  N  N     . LYS A 64  ? 0.68750 0.63170 0.49600 -0.00860 -0.02500 0.19870  64  LYS A N     
456  C  CA    . LYS A 64  ? 0.70060 0.63460 0.51870 -0.01560 -0.01330 0.19640  64  LYS A CA    
457  C  C     . LYS A 64  ? 0.69510 0.63070 0.49520 -0.02130 -0.00460 0.20070  64  LYS A C     
458  O  O     . LYS A 64  ? 0.72000 0.65470 0.50320 -0.01850 -0.00480 0.21100  64  LYS A O     
459  C  CB    . LYS A 64  ? 0.82620 0.74270 0.65840 -0.01340 -0.01040 0.20670  64  LYS A CB    
460  C  CG    . LYS A 64  ? 0.98520 0.89010 0.82920 -0.02050 0.00140  0.20490  64  LYS A CG    
461  C  CD    . LYS A 64  ? 1.14490 1.03360 1.00780 -0.01810 0.00290  0.21060  64  LYS A CD    
462  C  CE    . LYS A 64  ? 1.07700 0.95500 0.93200 -0.01270 0.00230  0.22820  64  LYS A CE    
463  N  NZ    . LYS A 64  ? 1.20570 1.06730 1.08060 -0.00990 0.00390  0.23180  64  LYS A NZ    
464  N  N     . CYS A 65  ? 0.82280 0.76050 0.62800 -0.02850 0.00330  0.18990  65  CYS A N     
465  C  CA    . CYS A 65  ? 0.80170 0.74130 0.59330 -0.03470 0.01310  0.19190  65  CYS A CA    
466  C  C     . CYS A 65  ? 0.82410 0.74860 0.61500 -0.03600 0.02120  0.20700  65  CYS A C     
467  O  O     . CYS A 65  ? 0.86190 0.77450 0.67100 -0.03820 0.02590  0.20790  65  CYS A O     
468  C  CB    . CYS A 65  ? 0.77240 0.71650 0.57520 -0.04140 0.01970  0.17690  65  CYS A CB    
469  S  SG    . CYS A 65  ? 0.76910 0.71620 0.55910 -0.04910 0.03240  0.17790  65  CYS A SG    
470  N  N     . GLY A 66  ? 1.01180 0.93530 0.78330 -0.03370 0.02300  0.21410  66  GLY A N     
471  C  CA    . GLY A 66  ? 0.99170 0.89930 0.76060 -0.03350 0.02990  0.22600  66  GLY A CA    
472  C  C     . GLY A 66  ? 1.05330 0.95190 0.83120 -0.04200 0.04340  0.22570  66  GLY A C     
473  O  O     . GLY A 66  ? 1.12700 1.00990 0.91060 -0.04290 0.04880  0.23410  66  GLY A O     
474  N  N     . ARG A 67  ? 0.85500 0.76410 0.63520 -0.04850 0.04870  0.21530  67  ARG A N     
475  C  CA    . ARG A 67  ? 0.80890 0.71360 0.59790 -0.05720 0.06180  0.21290  67  ARG A CA    
476  C  C     . ARG A 67  ? 0.81810 0.71580 0.63360 -0.06050 0.06320  0.20900  67  ARG A C     
477  O  O     . ARG A 67  ? 0.83020 0.71360 0.65630 -0.06370 0.07040  0.21390  67  ARG A O     
478  C  CB    . ARG A 67  ? 0.88050 0.80090 0.66120 -0.06200 0.06620  0.20280  67  ARG A CB    
479  C  CG    . ARG A 67  ? 1.03410 0.96270 0.78920 -0.05860 0.06470  0.20450  67  ARG A CG    
480  C  CD    . ARG A 67  ? 1.10000 1.04440 0.84880 -0.06280 0.06860  0.19280  67  ARG A CD    
481  N  NE    . ARG A 67  ? 1.26910 1.22490 0.99720 -0.05800 0.06190  0.19030  67  ARG A NE    
482  C  CZ    . ARG A 67  ? 1.32310 1.29210 1.04100 -0.06020 0.06490  0.18090  67  ARG A CZ    
483  N  NH1   . ARG A 67  ? 1.62510 1.59800 1.35170 -0.06690 0.07470  0.17350  67  ARG A NH1   
484  N  NH2   . ARG A 67  ? 1.39100 1.36950 1.09100 -0.05570 0.05810  0.17840  67  ARG A NH2   
485  N  N     . CYS A 68  ? 0.76530 0.67190 0.59150 -0.05950 0.05610  0.19730  68  CYS A N     
486  C  CA    . CYS A 68  ? 0.65500 0.55640 0.50620 -0.06180 0.05690  0.18740  68  CYS A CA    
487  C  C     . CYS A 68  ? 0.70470 0.59760 0.56760 -0.05550 0.04860  0.18950  68  CYS A C     
488  O  O     . CYS A 68  ? 0.64440 0.52930 0.52730 -0.05730 0.05060  0.18470  68  CYS A O     
489  C  CB    . CYS A 68  ? 0.72320 0.63830 0.58090 -0.06440 0.05560  0.16970  68  CYS A CB    
490  S  SG    . CYS A 68  ? 0.60860 0.53610 0.45860 -0.05740 0.04250  0.16200  68  CYS A SG    
491  N  N     . LYS A 69  ? 0.67420 0.56980 0.52490 -0.04800 0.03930  0.19590  69  LYS A N     
492  C  CA    . LYS A 69  ? 0.75830 0.64790 0.61910 -0.04100 0.03060  0.19800  69  LYS A CA    
493  C  C     . LYS A 69  ? 0.63470 0.52790 0.51460 -0.04100 0.02660  0.18230  69  LYS A C     
494  O  O     . LYS A 69  ? 0.84650 0.73140 0.74100 -0.03750 0.02340  0.18250  69  LYS A O     
495  C  CB    . LYS A 69  ? 0.86550 0.73660 0.73400 -0.03990 0.03510  0.21200  69  LYS A CB    
496  C  CG    . LYS A 69  ? 0.89670 0.76300 0.74600 -0.03590 0.03490  0.22630  69  LYS A CG    
497  C  CD    . LYS A 69  ? 1.10310 0.96410 0.94340 -0.04260 0.04650  0.22990  69  LYS A CD    
498  C  CE    . LYS A 69  ? 1.21110 1.06270 1.03590 -0.03830 0.04620  0.24280  69  LYS A CE    
499  N  NZ    . LYS A 69  ? 1.27480 1.12310 1.08770 -0.04500 0.05690  0.24660  69  LYS A NZ    
500  N  N     . GLN A 70  ? 0.71830 0.62390 0.59770 -0.04460 0.02710  0.16910  70  GLN A N     
501  C  CA    . GLN A 70  ? 0.68150 0.59160 0.57740 -0.04520 0.02430  0.15440  70  GLN A CA    
502  C  C     . GLN A 70  ? 0.73570 0.66130 0.62500 -0.04370 0.01830  0.14360  70  GLN A C     
503  O  O     . GLN A 70  ? 1.19970 1.13070 1.09980 -0.04550 0.01790  0.13120  70  GLN A O     
504  C  CB    . GLN A 70  ? 0.63460 0.54100 0.54400 -0.05250 0.03350  0.14800  70  GLN A CB    
505  C  CG    . GLN A 70  ? 0.63330 0.52380 0.55690 -0.05370 0.03800  0.15390  70  GLN A CG    
506  C  CD    . GLN A 70  ? 0.65410 0.54260 0.59230 -0.06140 0.04650  0.14620  70  GLN A CD    
507  O  OE1   . GLN A 70  ? 0.83630 0.72500 0.79050 -0.06210 0.04510  0.13590  70  GLN A OE1   
508  N  NE2   . GLN A 70  ? 0.71470 0.60220 0.64730 -0.06720 0.05530  0.15100  70  GLN A NE2   
509  N  N     . ALA A 71  ? 0.62740 0.55990 0.49890 -0.04050 0.01370  0.14850  71  ALA A N     
510  C  CA    . ALA A 71  ? 0.61870 0.56520 0.48340 -0.03870 0.00740  0.13920  71  ALA A CA    
511  C  C     . ALA A 71  ? 0.77060 0.72000 0.62370 -0.03220 -0.00150 0.14680  71  ALA A C     
512  O  O     . ALA A 71  ? 0.69260 0.63940 0.53120 -0.03110 -0.00070 0.15880  71  ALA A O     
513  C  CB    . ALA A 71  ? 0.58450 0.53980 0.43760 -0.04360 0.01310  0.13470  71  ALA A CB    
514  N  N     . PHE A 72  ? 0.59160 0.54680 0.45110 -0.02790 -0.01010 0.14010  72  PHE A N     
515  C  CA    . PHE A 72  ? 0.56750 0.52690 0.42000 -0.02130 -0.01970 0.14580  72  PHE A CA    
516  C  C     . PHE A 72  ? 0.60430 0.57890 0.44820 -0.02090 -0.02540 0.13630  72  PHE A C     
517  O  O     . PHE A 72  ? 0.64940 0.62930 0.49940 -0.02420 -0.02330 0.12420  72  PHE A O     
518  C  CB    . PHE A 72  ? 0.55020 0.50330 0.41990 -0.01640 -0.02470 0.14630  72  PHE A CB    
519  C  CG    . PHE A 72  ? 0.58500 0.52250 0.46360 -0.01620 -0.01960 0.15580  72  PHE A CG    
520  C  CD1   . PHE A 72  ? 0.53800 0.46780 0.42870 -0.02160 -0.01120 0.15100  72  PHE A CD1   
521  C  CD2   . PHE A 72  ? 0.65380 0.58420 0.52940 -0.01060 -0.02320 0.16940  72  PHE A CD2   
522  C  CE1   . PHE A 72  ? 0.59270 0.50790 0.49290 -0.02200 -0.00620 0.15870  72  PHE A CE1   
523  C  CE2   . PHE A 72  ? 0.78330 0.69800 0.66840 -0.01040 -0.01790 0.17810  72  PHE A CE2   
524  C  CZ    . PHE A 72  ? 0.69000 0.59690 0.58770 -0.01650 -0.00920 0.17230  72  PHE A CZ    
525  N  N     . TYR A 73  ? 0.62150 0.60300 0.45150 -0.01680 -0.03250 0.14200  73  TYR A N     
526  C  CA    . TYR A 73  ? 0.59890 0.59520 0.41730 -0.01690 -0.03770 0.13390  73  TYR A CA    
527  C  C     . TYR A 73  ? 0.71210 0.71560 0.52810 -0.01020 -0.04930 0.13690  73  TYR A C     
528  O  O     . TYR A 73  ? 0.74710 0.74440 0.56300 -0.00530 -0.05270 0.14920  73  TYR A O     
529  C  CB    . TYR A 73  ? 0.59610 0.59650 0.39400 -0.02060 -0.03230 0.13690  73  TYR A CB    
530  C  CG    . TYR A 73  ? 0.73120 0.72720 0.53210 -0.02720 -0.02100 0.13240  73  TYR A CG    
531  C  CD1   . TYR A 73  ? 0.64520 0.64740 0.45310 -0.03080 -0.01860 0.11820  73  TYR A CD1   
532  C  CD2   . TYR A 73  ? 0.73470 0.72050 0.53270 -0.02990 -0.01260 0.14240  73  TYR A CD2   
533  C  CE1   . TYR A 73  ? 0.63940 0.63890 0.45130 -0.03640 -0.00880 0.11390  73  TYR A CE1   
534  C  CE2   . TYR A 73  ? 0.84080 0.82390 0.64320 -0.03610 -0.00240 0.13770  73  TYR A CE2   
535  C  CZ    . TYR A 73  ? 0.68780 0.67830 0.49720 -0.03910 -0.00080 0.12340  73  TYR A CZ    
536  O  OH    . TYR A 73  ? 0.59640 0.58560 0.41120 -0.04470 0.00870  0.11860  73  TYR A OH    
537  N  N     . CYS A 74  ? 0.63160 0.64810 0.44680 -0.01010 -0.05520 0.12590  74  CYS A N     
538  C  CA    . CYS A 74  ? 0.64600 0.67260 0.45800 -0.00470 -0.06660 0.12680  74  CYS A CA    
539  C  C     . CYS A 74  ? 0.87130 0.90150 0.66120 -0.00220 -0.06950 0.13860  74  CYS A C     
540  O  O     . CYS A 74  ? 0.93460 0.96600 0.72290 0.00400  -0.07740 0.14810  74  CYS A O     
541  C  CB    . CYS A 74  ? 0.65700 0.69730 0.47020 -0.00670 -0.07060 0.11170  74  CYS A CB    
542  S  SG    . CYS A 74  ? 0.71060 0.74800 0.54720 -0.00930 -0.06740 0.09840  74  CYS A SG    
543  N  N     . ASN A 75  ? 0.70890 0.74130 0.48210 -0.00700 -0.06300 0.13810  75  ASN A N     
544  C  CA    . ASN A 75  ? 0.75010 0.78830 0.49910 -0.00570 -0.06480 0.14740  75  ASN A CA    
545  C  C     . ASN A 75  ? 0.77280 0.80940 0.50830 -0.01220 -0.05370 0.14630  75  ASN A C     
546  O  O     . ASN A 75  ? 0.78860 0.81900 0.53510 -0.01720 -0.04510 0.13930  75  ASN A O     
547  C  CB    . ASN A 75  ? 0.78640 0.84100 0.52800 -0.00300 -0.07510 0.13910  75  ASN A CB    
548  C  CG    . ASN A 75  ? 0.83900 0.90310 0.58620 -0.00810 -0.07450 0.12140  75  ASN A CG    
549  O  OD1   . ASN A 75  ? 0.82280 0.88700 0.56390 -0.01380 -0.06600 0.11500  75  ASN A OD1   
550  N  ND2   . ASN A 75  ? 0.81190 0.88320 0.57280 -0.00580 -0.08270 0.11270  75  ASN A ND2   
551  N  N     . VAL A 76  ? 0.63100 0.67040 0.34720 -0.01080 -0.05260 0.14930  76  VAL A N     
552  C  CA    . VAL A 76  ? 0.77120 0.80900 0.47420 -0.01610 -0.04160 0.14830  76  VAL A CA    
553  C  C     . VAL A 76  ? 0.72080 0.76950 0.42290 -0.02220 -0.03850 0.13220  76  VAL A C     
554  O  O     . VAL A 76  ? 0.75420 0.80050 0.45370 -0.02770 -0.02800 0.12970  76  VAL A O     
555  C  CB    . VAL A 76  ? 0.81030 0.84850 0.49180 -0.01280 -0.04170 0.15520  76  VAL A CB    
556  C  CG1   . VAL A 76  ? 0.81140 0.83620 0.49320 -0.00740 -0.04260 0.17190  76  VAL A CG1   
557  C  CG2   . VAL A 76  ? 0.67900 0.73190 0.35080 -0.00950 -0.05210 0.14670  76  VAL A CG2   
558  N  N     . GLU A 77  ? 0.70280 0.76340 0.40820 -0.02100 -0.04740 0.12110  77  GLU A N     
559  C  CA    . GLU A 77  ? 0.95110 1.02130 0.65790 -0.02630 -0.04500 0.10500  77  GLU A CA    
560  C  C     . GLU A 77  ? 0.73890 0.80010 0.46730 -0.02970 -0.03810 0.09880  77  GLU A C     
561  O  O     . GLU A 77  ? 0.59020 0.65060 0.31900 -0.03450 -0.02890 0.09220  77  GLU A O     
562  C  CB    . GLU A 77  ? 1.07320 1.15630 0.78220 -0.02390 -0.05590 0.09400  77  GLU A CB    
563  C  CG    . GLU A 77  ? 1.15000 1.24300 0.85700 -0.02890 -0.05310 0.07700  77  GLU A CG    
564  C  CD    . GLU A 77  ? 1.41250 1.51730 1.12480 -0.02720 -0.06350 0.06550  77  GLU A CD    
565  O  OE1   . GLU A 77  ? 1.34150 1.45030 1.05010 -0.02190 -0.07270 0.06980  77  GLU A OE1   
566  O  OE2   . GLU A 77  ? 1.73060 1.83900 1.45350 -0.03070 -0.06170 0.05120  77  GLU A OE2   
567  N  N     . CYS A 78  ? 0.63030 0.68500 0.37740 -0.02650 -0.04270 0.10050  78  CYS A N     
568  C  CA    . CYS A 78  ? 0.73580 0.78150 0.50390 -0.02870 -0.03690 0.09550  78  CYS A CA    
569  C  C     . CYS A 78  ? 0.72150 0.75720 0.48770 -0.03230 -0.02580 0.10260  78  CYS A C     
570  O  O     . CYS A 78  ? 0.67130 0.70510 0.44590 -0.03650 -0.01820 0.09500  78  CYS A O     
571  C  CB    . CYS A 78  ? 0.65760 0.69750 0.44340 -0.02430 -0.04330 0.09850  78  CYS A CB    
572  S  SG    . CYS A 78  ? 0.69240 0.74190 0.49120 -0.02270 -0.05170 0.08460  78  CYS A SG    
573  N  N     . GLN A 79  ? 0.76050 0.79050 0.51570 -0.03070 -0.02490 0.11720  79  GLN A N     
574  C  CA    . GLN A 79  ? 0.75940 0.77980 0.51220 -0.03430 -0.01420 0.12530  79  GLN A CA    
575  C  C     . GLN A 79  ? 0.71170 0.73820 0.45280 -0.03990 -0.00530 0.11930  79  GLN A C     
576  O  O     . GLN A 79  ? 0.63790 0.65940 0.38770 -0.04430 0.00410  0.11670  79  GLN A O     
577  C  CB    . GLN A 79  ? 0.78200 0.79570 0.52350 -0.03110 -0.01530 0.14290  79  GLN A CB    
578  C  CG    . GLN A 79  ? 0.74590 0.74860 0.48600 -0.03510 -0.00380 0.15240  79  GLN A CG    
579  C  CD    . GLN A 79  ? 0.79560 0.78850 0.52880 -0.03120 -0.00470 0.17010  79  GLN A CD    
580  O  OE1   . GLN A 79  ? 0.82790 0.82230 0.55710 -0.02440 -0.01420 0.17450  79  GLN A OE1   
581  N  NE2   . GLN A 79  ? 0.77040 0.75160 0.50580 -0.03440 0.00560  0.17780  79  GLN A NE2   
582  N  N     . LYS A 80  ? 0.70560 0.74360 0.42760 -0.03950 -0.00830 0.11670  80  LYS A N     
583  C  CA    . LYS A 80  ? 0.79070 0.83580 0.49980 -0.04430 0.00000  0.11040  80  LYS A CA    
584  C  C     . LYS A 80  ? 0.62960 0.67880 0.35310 -0.04750 0.00330  0.09360  80  LYS A C     
585  O  O     . LYS A 80  ? 0.68400 0.73310 0.40840 -0.05200 0.01320  0.08940  80  LYS A O     
586  C  CB    . LYS A 80  ? 0.81750 0.87240 0.50560 -0.04160 -0.00460 0.10940  80  LYS A CB    
587  C  CG    . LYS A 80  ? 1.03720 1.09910 0.71420 -0.04530 0.00370  0.10040  80  LYS A CG    
588  C  CD    . LYS A 80  ? 1.15590 1.22740 0.81600 -0.04190 -0.00250 0.09590  80  LYS A CD    
589  C  CE    . LYS A 80  ? 1.20300 1.26910 0.84750 -0.03740 -0.00370 0.11020  80  LYS A CE    
590  N  NZ    . LYS A 80  ? 1.37290 1.44870 0.99980 -0.03430 -0.01010 0.10550  80  LYS A NZ    
591  N  N     . GLU A 81  ? 0.58880 0.64160 0.32390 -0.04500 -0.00500 0.08450  81  GLU A N     
592  C  CA    . GLU A 81  ? 0.65460 0.71060 0.40400 -0.04720 -0.00270 0.06950  81  GLU A CA    
593  C  C     . GLU A 81  ? 0.54420 0.59080 0.31270 -0.04920 0.00400  0.06930  81  GLU A C     
594  O  O     . GLU A 81  ? 0.55520 0.60390 0.33180 -0.05210 0.00980  0.05960  81  GLU A O     
595  C  CB    . GLU A 81  ? 0.75500 0.81610 0.51270 -0.04410 -0.01300 0.06140  81  GLU A CB    
596  C  CG    . GLU A 81  ? 0.89350 0.96660 0.63440 -0.04300 -0.01960 0.05730  81  GLU A CG    
597  C  CD    . GLU A 81  ? 0.73630 0.81770 0.46730 -0.04700 -0.01330 0.04630  81  GLU A CD    
598  O  OE1   . GLU A 81  ? 0.83530 0.91590 0.57950 -0.04940 -0.00820 0.03550  81  GLU A OE1   
599  O  OE2   . GLU A 81  ? 1.17800 1.26680 0.88790 -0.04750 -0.01340 0.04840  81  GLU A OE2   
600  N  N     . ASP A 82  ? 0.56510 0.60180 0.34100 -0.04750 0.00290  0.07980  82  ASP A N     
601  C  CA    . ASP A 82  ? 0.52390 0.55190 0.31760 -0.04940 0.00850  0.08010  82  ASP A CA    
602  C  C     . ASP A 82  ? 0.61310 0.63740 0.40320 -0.05390 0.01950  0.08520  82  ASP A C     
603  O  O     . ASP A 82  ? 0.47910 0.49900 0.28390 -0.05640 0.02510  0.08270  82  ASP A O     
604  C  CB    . ASP A 82  ? 0.55030 0.56930 0.35450 -0.04590 0.00310  0.08800  82  ASP A CB    
605  C  CG    . ASP A 82  ? 0.67620 0.68840 0.50090 -0.04730 0.00650  0.08450  82  ASP A CG    
606  O  OD1   . ASP A 82  ? 0.47210 0.48870 0.30680 -0.04830 0.00720  0.07350  82  ASP A OD1   
607  O  OD2   . ASP A 82  ? 0.49200 0.49480 0.32290 -0.04730 0.00850  0.09280  82  ASP A OD2   
608  N  N     . TRP A 83  ? 0.51930 0.54600 0.28980 -0.05490 0.02240  0.09230  83  TRP A N     
609  C  CA    . TRP A 83  ? 0.57110 0.59380 0.33640 -0.05920 0.03310  0.09940  83  TRP A CA    
610  C  C     . TRP A 83  ? 0.54160 0.56730 0.31760 -0.06390 0.04230  0.08960  83  TRP A C     
611  O  O     . TRP A 83  ? 0.54410 0.56350 0.33070 -0.06700 0.04930  0.09310  83  TRP A O     
612  C  CB    . TRP A 83  ? 0.54120 0.56850 0.28130 -0.05940 0.03480  0.10710  83  TRP A CB    
613  C  CG    . TRP A 83  ? 0.56640 0.58940 0.30140 -0.06420 0.04680  0.11470  83  TRP A CG    
614  C  CD1   . TRP A 83  ? 0.55240 0.58260 0.27530 -0.06820 0.05560  0.11160  83  TRP A CD1   
615  C  CD2   . TRP A 83  ? 0.58500 0.59570 0.32940 -0.06600 0.05210  0.12560  83  TRP A CD2   
616  N  NE1   . TRP A 83  ? 0.65350 0.67660 0.37810 -0.07180 0.06600  0.12000  83  TRP A NE1   
617  C  CE2   . TRP A 83  ? 0.61880 0.63000 0.35560 -0.07130 0.06420  0.12920  83  TRP A CE2   
618  C  CE3   . TRP A 83  ? 0.56740 0.56660 0.32610 -0.06380 0.04820  0.13220  83  TRP A CE3   
619  C  CZ2   . TRP A 83  ? 0.56770 0.56810 0.31190 -0.07460 0.07240  0.13910  83  TRP A CZ2   
620  C  CZ3   . TRP A 83  ? 0.52510 0.51340 0.29070 -0.06710 0.05620  0.14170  83  TRP A CZ3   
621  C  CH2   . TRP A 83  ? 0.58870 0.57760 0.34720 -0.07270 0.06810  0.14530  83  TRP A CH2   
622  N  N     . PRO A 84  ? 0.58490 0.62040 0.36000 -0.06440 0.04260  0.07690  84  PRO A N     
623  C  CA    . PRO A 84  ? 0.58450 0.62350 0.37070 -0.06810 0.05110  0.06770  84  PRO A CA    
624  C  C     . PRO A 84  ? 0.47070 0.50410 0.28040 -0.06830 0.05140  0.06520  84  PRO A C     
625  O  O     . PRO A 84  ? 0.50300 0.53710 0.32180 -0.07190 0.05950  0.06270  84  PRO A O     
626  C  CB    . PRO A 84  ? 0.59480 0.64370 0.37810 -0.06690 0.04850  0.05460  84  PRO A CB    
627  C  CG    . PRO A 84  ? 0.57290 0.62560 0.33630 -0.06450 0.04170  0.05810  84  PRO A CG    
628  C  CD    . PRO A 84  ? 0.59360 0.63750 0.35820 -0.06160 0.03500  0.07030  84  PRO A CD    
629  N  N     . MET A 85  ? 0.46750 0.49620 0.28620 -0.06470 0.04270  0.06580  85  MET A N     
630  C  CA    . MET A 85  ? 0.48820 0.51150 0.32740 -0.06460 0.04220  0.06390  85  MET A CA    
631  C  C     . MET A 85  ? 0.47750 0.49060 0.32040 -0.06570 0.04380  0.07500  85  MET A C     
632  O  O     . MET A 85  ? 0.43710 0.44700 0.29350 -0.06860 0.04890  0.07440  85  MET A O     
633  C  CB    . MET A 85  ? 0.47940 0.50340 0.32720 -0.06040 0.03310  0.05800  85  MET A CB    
634  C  CG    . MET A 85  ? 0.52090 0.55340 0.36930 -0.05960 0.03210  0.04630  85  MET A CG    
635  S  SD    . MET A 85  ? 0.50190 0.53880 0.36390 -0.06250 0.04070  0.03760  85  MET A SD    
636  C  CE    . MET A 85  ? 0.73760 0.78350 0.58470 -0.06430 0.04600  0.03170  85  MET A CE    
637  N  N     . HIS A 86  ? 0.46310 0.47130 0.29450 -0.06330 0.03940  0.08490  86  HIS A N     
638  C  CA    . HIS A 86  ? 0.50450 0.50160 0.33950 -0.06350 0.04030  0.09610  86  HIS A CA    
639  C  C     . HIS A 86  ? 0.54770 0.54100 0.38150 -0.06890 0.05130  0.10220  86  HIS A C     
640  O  O     . HIS A 86  ? 0.50630 0.49070 0.35170 -0.07080 0.05440  0.10680  86  HIS A O     
641  C  CB    . HIS A 86  ? 0.51490 0.50880 0.33660 -0.05900 0.03320  0.10600  86  HIS A CB    
642  C  CG    . HIS A 86  ? 0.53620 0.51750 0.36170 -0.05840 0.03400  0.11820  86  HIS A CG    
643  N  ND1   . HIS A 86  ? 0.46000 0.43350 0.30460 -0.05840 0.03350  0.11690  86  HIS A ND1   
644  C  CD2   . HIS A 86  ? 0.56410 0.53910 0.37710 -0.05770 0.03550  0.13190  86  HIS A CD2   
645  C  CE1   . HIS A 86  ? 0.48210 0.44450 0.32680 -0.05790 0.03490  0.12880  86  HIS A CE1   
646  N  NE2   . HIS A 86  ? 0.62430 0.58700 0.45010 -0.05730 0.03620  0.13860  86  HIS A NE2   
647  N  N     . LYS A 87  ? 0.46350 0.46380 0.28390 -0.07170 0.05750  0.10150  87  LYS A N     
648  C  CA    . LYS A 87  ? 0.49250 0.49050 0.31070 -0.07720 0.06890  0.10710  87  LYS A CA    
649  C  C     . LYS A 87  ? 0.46050 0.45890 0.29950 -0.08170 0.07560  0.10000  87  LYS A C     
650  O  O     . LYS A 87  ? 0.46100 0.45570 0.30330 -0.08670 0.08470  0.10500  87  LYS A O     
651  C  CB    . LYS A 87  ? 0.52390 0.53070 0.32250 -0.07900 0.07430  0.10690  87  LYS A CB    
652  C  CG    . LYS A 87  ? 0.56100 0.57980 0.36230 -0.07990 0.07630  0.09260  87  LYS A CG    
653  C  CD    . LYS A 87  ? 0.73730 0.76370 0.51870 -0.08220 0.08310  0.09330  87  LYS A CD    
654  C  CE    . LYS A 87  ? 0.85150 0.88950 0.63560 -0.08280 0.08550  0.07860  87  LYS A CE    
655  N  NZ    . LYS A 87  ? 0.86420 0.91010 0.62730 -0.08460 0.09140  0.07830  87  LYS A NZ    
656  N  N     . LEU A 88  ? 0.51740 0.52070 0.37020 -0.08000 0.07090  0.08860  88  LEU A N     
657  C  CA    . LEU A 88  ? 0.47740 0.48170 0.35080 -0.08310 0.07480  0.08170  88  LEU A CA    
658  C  C     . LEU A 88  ? 0.47150 0.46470 0.35760 -0.08420 0.07440  0.08750  88  LEU A C     
659  O  O     . LEU A 88  ? 0.56610 0.55910 0.46750 -0.08850 0.07980  0.08450  88  LEU A O     
660  C  CB    . LEU A 88  ? 0.48760 0.49910 0.37120 -0.07990 0.06880  0.06970  88  LEU A CB    
661  C  CG    . LEU A 88  ? 0.52920 0.55100 0.40460 -0.07820 0.06840  0.06170  88  LEU A CG    
662  C  CD1   . LEU A 88  ? 0.55920 0.58510 0.44740 -0.07480 0.06220  0.05180  88  LEU A CD1   
663  C  CD2   . LEU A 88  ? 0.55580 0.58490 0.42950 -0.08250 0.07870  0.05870  88  LEU A CD2   
664  N  N     . GLU A 89  ? 0.42990 0.41460 0.31040 -0.08040 0.06780  0.09520  89  GLU A N     
665  C  CA    . GLU A 89  ? 0.47270 0.44620 0.36560 -0.08050 0.06640  0.09980  89  GLU A CA    
666  C  C     . GLU A 89  ? 0.57090 0.53270 0.45480 -0.08050 0.06850  0.11440  89  GLU A C     
667  O  O     . GLU A 89  ? 0.56890 0.52070 0.46420 -0.08290 0.07170  0.11870  89  GLU A O     
668  C  CB    . GLU A 89  ? 0.42740 0.40060 0.32770 -0.07520 0.05620  0.09450  89  GLU A CB    
669  C  CG    . GLU A 89  ? 0.46840 0.45140 0.37970 -0.07500 0.05430  0.08130  89  GLU A CG    
670  C  CD    . GLU A 89  ? 0.44490 0.42750 0.36270 -0.06990 0.04500  0.07650  89  GLU A CD    
671  O  OE1   . GLU A 89  ? 0.40810 0.38660 0.31830 -0.06570 0.03890  0.08170  89  GLU A OE1   
672  O  OE2   . GLU A 89  ? 0.39530 0.38240 0.32600 -0.07010 0.04390  0.06770  89  GLU A OE2   
673  N  N     . CYS A 90  ? 0.55710 0.52020 0.42070 -0.07780 0.06670  0.12180  90  CYS A N     
674  C  CA    . CYS A 90  ? 0.53200 0.48450 0.38470 -0.07600 0.06650  0.13680  90  CYS A CA    
675  C  C     . CYS A 90  ? 0.54940 0.49170 0.40870 -0.08160 0.07700  0.14520  90  CYS A C     
676  O  O     . CYS A 90  ? 0.57570 0.50570 0.44550 -0.08110 0.07650  0.15100  90  CYS A O     
677  C  CB    . CYS A 90  ? 0.63260 0.59150 0.46070 -0.07350 0.06500  0.14250  90  CYS A CB    
678  S  SG    . CYS A 90  ? 0.60530 0.55300 0.41910 -0.06940 0.06220  0.16120  90  CYS A SG    
679  N  N     . SER A 91  ? 0.55290 0.50010 0.40690 -0.08720 0.08690  0.14520  91  SER A N     
680  C  CA    . SER A 91  ? 0.54710 0.48570 0.40720 -0.09360 0.09820  0.15270  91  SER A CA    
681  C  C     . SER A 91  ? 0.57810 0.51380 0.46420 -0.09800 0.10110  0.14420  91  SER A C     
682  O  O     . SER A 91  ? 0.52890 0.45190 0.42560 -0.10020 0.10460  0.15070  91  SER A O     
683  C  CB    . SER A 91  ? 0.55340 0.49970 0.40050 -0.09830 0.10830  0.15440  91  SER A CB    
684  O  OG    . SER A 91  ? 0.62710 0.56470 0.48010 -0.10470 0.11980  0.16270  91  SER A OG    
685  N  N     . PRO A 92  ? 0.48110 0.42830 0.37860 -0.09920 0.09970  0.12950  92  PRO A N     
686  C  CA    . PRO A 92  ? 0.51780 0.46410 0.43950 -0.10270 0.10100  0.12060  92  PRO A CA    
687  C  C     . PRO A 92  ? 0.53400 0.46820 0.46650 -0.09990 0.09480  0.12280  92  PRO A C     
688  O  O     . PRO A 92  ? 0.46190 0.38960 0.41130 -0.10440 0.09940  0.12150  92  PRO A O     
689  C  CB    . PRO A 92  ? 0.49270 0.45370 0.41940 -0.10100 0.09610  0.10610  92  PRO A CB    
690  C  CG    . PRO A 92  ? 0.53600 0.50630 0.44450 -0.10040 0.09890  0.10680  92  PRO A CG    
691  C  CD    . PRO A 92  ? 0.50700 0.46890 0.39550 -0.09730 0.09720  0.12050  92  PRO A CD    
692  N  N     . MET A 93  ? 0.55010 0.48220 0.47370 -0.09260 0.08500  0.12530  93  MET A N     
693  C  CA    . MET A 93  ? 0.59830 0.51960 0.53170 -0.08910 0.07900  0.12710  93  MET A CA    
694  C  C     . MET A 93  ? 0.54610 0.45120 0.48290 -0.09140 0.08510  0.13960  93  MET A C     
695  O  O     . MET A 93  ? 0.71680 0.61310 0.67080 -0.09300 0.08590  0.13740  93  MET A O     
696  C  CB    . MET A 93  ? 0.54570 0.46870 0.46770 -0.08080 0.06810  0.12870  93  MET A CB    
697  C  CG    . MET A 93  ? 0.57150 0.50570 0.49900 -0.07800 0.06080  0.11520  93  MET A CG    
698  S  SD    . MET A 93  ? 0.58190 0.51520 0.50420 -0.06920 0.04850  0.11630  93  MET A SD    
699  C  CE    . MET A 93  ? 0.67840 0.61470 0.57560 -0.06610 0.04680  0.12680  93  MET A CE    
700  N  N     . VAL A 94  ? 0.59680 0.49800 0.51700 -0.09180 0.08990  0.15250  94  VAL A N     
701  C  CA    . VAL A 94  ? 0.75720 0.64220 0.67890 -0.09380 0.09650  0.16650  94  VAL A CA    
702  C  C     . VAL A 94  ? 0.66990 0.55180 0.60620 -0.10320 0.10870  0.16430  94  VAL A C     
703  O  O     . VAL A 94  ? 0.81160 0.68010 0.76180 -0.10600 0.11290  0.16820  94  VAL A O     
704  C  CB    . VAL A 94  ? 0.80640 0.68810 0.70410 -0.09070 0.09780  0.18260  94  VAL A CB    
705  C  CG1   . VAL A 94  ? 0.90370 0.76710 0.80370 -0.08950 0.09920  0.19480  94  VAL A CG1   
706  C  CG2   . VAL A 94  ? 0.76420 0.65500 0.64530 -0.08270 0.08630  0.18190  94  VAL A CG2   
707  N  N     . VAL A 95  ? 0.67940 0.57440 0.61330 -0.10790 0.11400  0.15730  95  VAL A N     
708  C  CA    . VAL A 95  ? 0.65280 0.54840 0.59990 -0.11700 0.12550  0.15460  95  VAL A CA    
709  C  C     . VAL A 95  ? 0.56980 0.46600 0.54300 -0.12070 0.12500  0.14140  95  VAL A C     
710  O  O     . VAL A 95  ? 0.64070 0.53050 0.62950 -0.12580 0.12980  0.14110  95  VAL A O     
711  C  CB    . VAL A 95  ? 0.62520 0.53650 0.56250 -0.12010 0.13080  0.15030  95  VAL A CB    
712  C  CG1   . VAL A 95  ? 0.68710 0.60450 0.64260 -0.12790 0.13900  0.14390  95  VAL A CG1   
713  C  CG2   . VAL A 95  ? 0.69650 0.60820 0.60950 -0.11710 0.13150  0.16320  95  VAL A CG2   
714  N  N     . PHE A 96  ? 0.49230 0.39940 0.46990 -0.11690 0.11580  0.12840  96  PHE A N     
715  C  CA    . PHE A 96  ? 0.47120 0.38030 0.47130 -0.11910 0.11320  0.11550  96  PHE A CA    
716  C  C     . PHE A 96  ? 0.49530 0.38970 0.50400 -0.11600 0.10850  0.11820  96  PHE A C     
717  O  O     . PHE A 96  ? 0.66610 0.55690 0.69450 -0.12000 0.11020  0.11100  96  PHE A O     
718  C  CB    . PHE A 96  ? 0.46540 0.39090 0.46640 -0.11570 0.10530  0.10190  96  PHE A CB    
719  C  CG    . PHE A 96  ? 0.51930 0.45980 0.52390 -0.12040 0.11080  0.09410  96  PHE A CG    
720  C  CD1   . PHE A 96  ? 0.51600 0.46110 0.54110 -0.12720 0.11590  0.08530  96  PHE A CD1   
721  C  CD2   . PHE A 96  ? 0.49690 0.44740 0.48520 -0.11800 0.11070  0.09490  96  PHE A CD2   
722  C  CE1   . PHE A 96  ? 0.49450 0.45430 0.52450 -0.13110 0.12070  0.07800  96  PHE A CE1   
723  C  CE2   . PHE A 96  ? 0.49360 0.45800 0.48650 -0.12190 0.11610  0.08740  96  PHE A CE2   
724  C  CZ    . PHE A 96  ? 0.50360 0.47280 0.51760 -0.12830 0.12100  0.07930  96  PHE A CZ    
725  N  N     . GLY A 97  ? 0.60490 0.49180 0.59920 -0.10880 0.10270  0.12820  97  GLY A N     
726  C  CA    . GLY A 97  ? 0.66610 0.53840 0.66710 -0.10500 0.09870  0.13270  97  GLY A CA    
727  C  C     . GLY A 97  ? 0.59540 0.47220 0.61000 -0.10240 0.09080  0.11900  97  GLY A C     
728  O  O     . GLY A 97  ? 0.57970 0.46810 0.58750 -0.09760 0.08290  0.11230  97  GLY A O     
729  N  N     . GLU A 98  ? 0.80380 0.67130 0.83770 -0.10580 0.09340  0.11470  98  GLU A N     
730  C  CA    . GLU A 98  ? 0.85120 0.72220 0.89890 -0.10410 0.08710  0.10130  98  GLU A CA    
731  C  C     . GLU A 98  ? 0.66000 0.54890 0.71340 -0.10740 0.08580  0.08670  98  GLU A C     
732  O  O     . GLU A 98  ? 0.77400 0.67090 0.83100 -0.10400 0.07840  0.07650  98  GLU A O     
733  C  CB    . GLU A 98  ? 0.96120 0.81800 1.02860 -0.10800 0.09150  0.09950  98  GLU A CB    
734  C  CG    . GLU A 98  ? 1.10230 0.94010 1.16770 -0.10370 0.09210  0.11310  98  GLU A CG    
735  C  CD    . GLU A 98  ? 1.43380 1.27120 1.49270 -0.09400 0.08180  0.11360  98  GLU A CD    
736  O  OE1   . GLU A 98  ? 1.46260 1.31150 1.52410 -0.09170 0.07500  0.10130  98  GLU A OE1   
737  O  OE2   . GLU A 98  ? 1.35880 1.18460 1.41040 -0.08870 0.08060  0.12680  98  GLU A OE2   
738  N  N     . ASN A 99  ? 0.66430 0.55980 0.71870 -0.11390 0.09320  0.08620  99  ASN A N     
739  C  CA    . ASN A 99  ? 0.51990 0.43280 0.58100 -0.11720 0.09280  0.07320  99  ASN A CA    
740  C  C     . ASN A 99  ? 0.48380 0.41090 0.52990 -0.11190 0.08690  0.07100  99  ASN A C     
741  O  O     . ASN A 99  ? 0.51660 0.45810 0.56800 -0.11340 0.08590  0.06090  99  ASN A O     
742  C  CB    . ASN A 99  ? 0.59390 0.50890 0.66420 -0.12620 0.10350  0.07310  99  ASN A CB    
743  C  CG    . ASN A 99  ? 0.75010 0.65300 0.83960 -0.13270 0.10960  0.07180  99  ASN A CG    
744  O  OD1   . ASN A 99  ? 0.84810 0.73840 0.93770 -0.13630 0.11760  0.08230  99  ASN A OD1   
745  N  ND2   . ASN A 99  ? 0.60460 0.51150 0.71020 -0.13390 0.10550  0.05870  99  ASN A ND2   
746  N  N     . TRP A 100 ? 0.53960 0.46270 0.56790 -0.10570 0.08290  0.08040  100 TRP A N     
747  C  CA    . TRP A 100 ? 0.50620 0.44100 0.52040 -0.10040 0.07700  0.07830  100 TRP A CA    
748  C  C     . TRP A 100 ? 0.49330 0.43240 0.51120 -0.09490 0.06740  0.06980  100 TRP A C     
749  O  O     . TRP A 100 ? 0.58990 0.52070 0.60500 -0.09010 0.06240  0.07380  100 TRP A O     
750  C  CB    . TRP A 100 ? 0.51520 0.44470 0.50930 -0.09630 0.07630  0.09090  100 TRP A CB    
751  C  CG    . TRP A 100 ? 0.55450 0.49670 0.53450 -0.09280 0.07250  0.08820  100 TRP A CG    
752  C  CD1   . TRP A 100 ? 0.49460 0.44580 0.46770 -0.09590 0.07800  0.08750  100 TRP A CD1   
753  C  CD2   . TRP A 100 ? 0.53820 0.48510 0.51040 -0.08590 0.06310  0.08540  100 TRP A CD2   
754  N  NE1   . TRP A 100 ? 0.57350 0.53420 0.53510 -0.09110 0.07240  0.08410  100 TRP A NE1   
755  C  CE2   . TRP A 100 ? 0.54380 0.50200 0.50480 -0.08520 0.06330  0.08290  100 TRP A CE2   
756  C  CE3   . TRP A 100 ? 0.50300 0.44560 0.47730 -0.08040 0.05510  0.08450  100 TRP A CE3   
757  C  CZ2   . TRP A 100 ? 0.69410 0.65890 0.64660 -0.07950 0.05570  0.07940  100 TRP A CZ2   
758  C  CZ3   . TRP A 100 ? 0.53510 0.48500 0.50070 -0.07480 0.04750  0.08140  100 TRP A CZ3   
759  C  CH2   . TRP A 100 ? 0.62570 0.58630 0.58080 -0.07450 0.04790  0.07880  100 TRP A CH2   
760  N  N     . ASN A 101 ? 0.51630 0.46880 0.54090 -0.09560 0.06530  0.05850  101 ASN A N     
761  C  CA    . ASN A 101 ? 0.54630 0.50420 0.57490 -0.09090 0.05710  0.05000  101 ASN A CA    
762  C  C     . ASN A 101 ? 0.44190 0.41550 0.46920 -0.08930 0.05420  0.04180  101 ASN A C     
763  O  O     . ASN A 101 ? 0.55230 0.53350 0.59010 -0.08950 0.05140  0.03230  101 ASN A O     
764  C  CB    . ASN A 101 ? 0.53000 0.48380 0.57570 -0.09380 0.05720  0.04320  101 ASN A CB    
765  C  CG    . ASN A 101 ? 0.59380 0.55580 0.65340 -0.10070 0.06230  0.03520  101 ASN A CG    
766  O  OD1   . ASN A 101 ? 0.60970 0.57740 0.66750 -0.10420 0.06770  0.03690  101 ASN A OD1   
767  N  ND2   . ASN A 101 ? 0.76330 0.72690 0.83720 -0.10260 0.06060  0.02590  101 ASN A ND2   
768  N  N     . PRO A 102 ? 0.42630 0.40540 0.44090 -0.08750 0.05470  0.04500  102 PRO A N     
769  C  CA    . PRO A 102 ? 0.38530 0.37780 0.39900 -0.08500 0.05160  0.03770  102 PRO A CA    
770  C  C     . PRO A 102 ? 0.33960 0.33300 0.35100 -0.07870 0.04310  0.03450  102 PRO A C     
771  O  O     . PRO A 102 ? 0.36440 0.34980 0.36790 -0.07540 0.03990  0.04030  102 PRO A O     
772  C  CB    . PRO A 102 ? 0.39120 0.38640 0.39100 -0.08460 0.05480  0.04280  102 PRO A CB    
773  C  CG    . PRO A 102 ? 0.37810 0.36070 0.36680 -0.08380 0.05520  0.05360  102 PRO A CG    
774  C  CD    . PRO A 102 ? 0.39610 0.36900 0.39650 -0.08750 0.05810  0.05560  102 PRO A CD    
775  N  N     . SER A 103 ? 0.35980 0.36310 0.37840 -0.07720 0.03980  0.02590  103 SER A N     
776  C  CA    . SER A 103 ? 0.34680 0.35200 0.36300 -0.07150 0.03260  0.02300  103 SER A CA    
777  C  C     . SER A 103 ? 0.39780 0.40350 0.40070 -0.06750 0.03050  0.02690  103 SER A C     
778  O  O     . SER A 103 ? 0.36460 0.37280 0.36100 -0.06890 0.03430  0.02940  103 SER A O     
779  C  CB    . SER A 103 ? 0.40230 0.41920 0.42720 -0.07060 0.03030  0.01420  103 SER A CB    
780  O  OG    . SER A 103 ? 0.45840 0.48440 0.48050 -0.06980 0.03160  0.01260  103 SER A OG    
781  N  N     . GLU A 104 ? 0.39170 0.39570 0.39100 -0.06260 0.02460  0.02680  104 GLU A N     
782  C  CA    . GLU A 104 ? 0.41830 0.42270 0.40630 -0.05890 0.02180  0.02960  104 GLU A CA    
783  C  C     . GLU A 104 ? 0.40100 0.41500 0.38710 -0.05830 0.02300  0.02540  104 GLU A C     
784  O  O     . GLU A 104 ? 0.32320 0.33810 0.29980 -0.05770 0.02390  0.02760  104 GLU A O     
785  C  CB    . GLU A 104 ? 0.39300 0.39490 0.38080 -0.05430 0.01570  0.02900  104 GLU A CB    
786  C  CG    . GLU A 104 ? 0.43320 0.43440 0.41030 -0.05100 0.01260  0.03230  104 GLU A CG    
787  C  CD    . GLU A 104 ? 0.47510 0.47070 0.45210 -0.04750 0.00760  0.03470  104 GLU A CD    
788  O  OE1   . GLU A 104 ? 0.41690 0.40480 0.39620 -0.04820 0.00800  0.03890  104 GLU A OE1   
789  O  OE2   . GLU A 104 ? 0.38060 0.37940 0.35640 -0.04410 0.00370  0.03230  104 GLU A OE2   
790  N  N     . THR A 105 ? 0.29610 0.31760 0.29140 -0.05820 0.02290  0.01910  105 THR A N     
791  C  CA    . THR A 105 ? 0.39670 0.42740 0.39320 -0.05740 0.02440  0.01500  105 THR A CA    
792  C  C     . THR A 105 ? 0.33840 0.37150 0.33240 -0.06120 0.03080  0.01630  105 THR A C     
793  O  O     . THR A 105 ? 0.29820 0.33500 0.28660 -0.06000 0.03240  0.01550  105 THR A O     
794  C  CB    . THR A 105 ? 0.44650 0.48520 0.45440 -0.05660 0.02300  0.00900  105 THR A CB    
795  O  OG1   . THR A 105 ? 0.50490 0.54200 0.51360 -0.05300 0.01770  0.00780  105 THR A OG1   
796  C  CG2   . THR A 105 ? 0.48520 0.53320 0.49540 -0.05490 0.02450  0.00540  105 THR A CG2   
797  N  N     . VAL A 106 ? 0.30130 0.33190 0.30000 -0.06580 0.03490  0.01810  106 VAL A N     
798  C  CA    . VAL A 106 ? 0.31670 0.34890 0.31350 -0.07020 0.04200  0.02010  106 VAL A CA    
799  C  C     . VAL A 106 ? 0.30580 0.33210 0.28720 -0.06980 0.04320  0.02650  106 VAL A C     
800  O  O     . VAL A 106 ? 0.36200 0.39280 0.33730 -0.07050 0.04710  0.02610  106 VAL A O     
801  C  CB    . VAL A 106 ? 0.31090 0.34010 0.31680 -0.07570 0.04630  0.02110  106 VAL A CB    
802  C  CG1   . VAL A 106 ? 0.33700 0.36640 0.33970 -0.08060 0.05450  0.02470  106 VAL A CG1   
803  C  CG2   . VAL A 106 ? 0.37420 0.41210 0.39550 -0.07660 0.04520  0.01350  106 VAL A CG2   
804  N  N     . ARG A 107 ? 0.35920 0.37620 0.33460 -0.06840 0.03960  0.03210  107 ARG A N     
805  C  CA    . ARG A 107 ? 0.36570 0.37730 0.32580 -0.06730 0.03910  0.03890  107 ARG A CA    
806  C  C     . ARG A 107 ? 0.30940 0.32710 0.26170 -0.06380 0.03650  0.03530  107 ARG A C     
807  O  O     . ARG A 107 ? 0.33080 0.34980 0.27160 -0.06470 0.03930  0.03770  107 ARG A O     
808  C  CB    . ARG A 107 ? 0.41010 0.41230 0.36820 -0.06490 0.03400  0.04430  107 ARG A CB    
809  C  CG    . ARG A 107 ? 0.43410 0.42800 0.39920 -0.06810 0.03690  0.04860  107 ARG A CG    
810  C  CD    . ARG A 107 ? 0.40860 0.39300 0.37130 -0.06490 0.03190  0.05430  107 ARG A CD    
811  N  NE    . ARG A 107 ? 0.42120 0.40240 0.36900 -0.06330 0.03120  0.06240  107 ARG A NE    
812  C  CZ    . ARG A 107 ? 0.47010 0.44740 0.41190 -0.05880 0.02500  0.06650  107 ARG A CZ    
813  N  NH1   . ARG A 107 ? 0.43070 0.40630 0.38050 -0.05540 0.01970  0.06330  107 ARG A NH1   
814  N  NH2   . ARG A 107 ? 0.47850 0.45460 0.40620 -0.05750 0.02430  0.07360  107 ARG A NH2   
815  N  N     . LEU A 108 ? 0.30730 0.32840 0.26550 -0.06030 0.03170  0.02980  108 LEU A N     
816  C  CA    . LEU A 108 ? 0.31700 0.34300 0.27030 -0.05710 0.02930  0.02570  108 LEU A CA    
817  C  C     . LEU A 108 ? 0.31740 0.35120 0.27190 -0.05860 0.03490  0.02100  108 LEU A C     
818  O  O     . LEU A 108 ? 0.27900 0.31520 0.22450 -0.05830 0.03640  0.01980  108 LEU A O     
819  C  CB    . LEU A 108 ? 0.27140 0.29830 0.23210 -0.05320 0.02370  0.02180  108 LEU A CB    
820  C  CG    . LEU A 108 ? 0.31700 0.34740 0.27470 -0.05000 0.02130  0.01760  108 LEU A CG    
821  C  CD1   . LEU A 108 ? 0.30920 0.33700 0.25450 -0.04940 0.01900  0.02050  108 LEU A CD1   
822  C  CD2   . LEU A 108 ? 0.31040 0.34110 0.27610 -0.04650 0.01670  0.01490  108 LEU A CD2   
823  N  N     . THR A 109 ? 0.33980 0.37820 0.30620 -0.06020 0.03800  0.01780  109 THR A N     
824  C  CA    . THR A 109 ? 0.31560 0.36230 0.28630 -0.06120 0.04330  0.01290  109 THR A CA    
825  C  C     . THR A 109 ? 0.29900 0.34620 0.26090 -0.06520 0.05020  0.01560  109 THR A C     
826  O  O     . THR A 109 ? 0.32090 0.37360 0.27980 -0.06500 0.05410  0.01180  109 THR A O     
827  C  CB    . THR A 109 ? 0.29450 0.34700 0.28070 -0.06220 0.04450  0.00930  109 THR A CB    
828  O  OG1   . THR A 109 ? 0.32400 0.37690 0.31650 -0.05820 0.03820  0.00690  109 THR A OG1   
829  C  CG2   . THR A 109 ? 0.37130 0.43330 0.36370 -0.06260 0.04980  0.00420  109 THR A CG2   
830  N  N     . ALA A 110 ? 0.26940 0.31030 0.22710 -0.06860 0.05210  0.02220  110 ALA A N     
831  C  CA    . ALA A 110 ? 0.33500 0.37500 0.28190 -0.07230 0.05870  0.02670  110 ALA A CA    
832  C  C     . ALA A 110 ? 0.31970 0.35990 0.25060 -0.07010 0.05710  0.02730  110 ALA A C     
833  O  O     . ALA A 110 ? 0.36670 0.41180 0.29050 -0.07180 0.06280  0.02560  110 ALA A O     
834  C  CB    . ALA A 110 ? 0.31740 0.34850 0.26230 -0.07540 0.05990  0.03510  110 ALA A CB    
835  N  N     . ARG A 111 ? 0.36090 0.39650 0.28670 -0.06640 0.04940  0.02880  111 ARG A N     
836  C  CA    . ARG A 111 ? 0.39200 0.42810 0.30330 -0.06410 0.04620  0.02870  111 ARG A CA    
837  C  C     . ARG A 111 ? 0.39220 0.43560 0.30650 -0.06220 0.04680  0.01930  111 ARG A C     
838  O  O     . ARG A 111 ? 0.35140 0.39810 0.25420 -0.06230 0.04810  0.01720  111 ARG A O     
839  C  CB    . ARG A 111 ? 0.40620 0.43620 0.31470 -0.06090 0.03780  0.03260  111 ARG A CB    
840  C  CG    . ARG A 111 ? 0.45040 0.47290 0.35170 -0.06210 0.03740  0.04270  111 ARG A CG    
841  C  CD    . ARG A 111 ? 0.44250 0.45920 0.34330 -0.05840 0.02930  0.04640  111 ARG A CD    
842  N  NE    . ARG A 111 ? 0.51630 0.52470 0.41520 -0.05950 0.02980  0.05600  111 ARG A NE    
843  C  CZ    . ARG A 111 ? 0.63090 0.63500 0.51870 -0.05760 0.02620  0.06390  111 ARG A CZ    
844  N  NH1   . ARG A 111 ? 0.63000 0.63840 0.50700 -0.05480 0.02120  0.06290  111 ARG A NH1   
845  N  NH2   . ARG A 111 ? 0.56050 0.55600 0.44900 -0.05840 0.02760  0.07270  111 ARG A NH2   
846  N  N     . ILE A 112 ? 0.33090 0.37710 0.25990 -0.06050 0.04600  0.01400  112 ILE A N     
847  C  CA    . ILE A 112 ? 0.31620 0.36850 0.25010 -0.05850 0.04740  0.00580  112 ILE A CA    
848  C  C     . ILE A 112 ? 0.35000 0.40840 0.28160 -0.06140 0.05600  0.00300  112 ILE A C     
849  O  O     . ILE A 112 ? 0.36710 0.42900 0.29190 -0.06090 0.05820  -0.00180 112 ILE A O     
850  C  CB    . ILE A 112 ? 0.29190 0.34620 0.24220 -0.05580 0.04520  0.00220  112 ILE A CB    
851  C  CG1   . ILE A 112 ? 0.33890 0.38790 0.29040 -0.05260 0.03740  0.00390  112 ILE A CG1   
852  C  CG2   . ILE A 112 ? 0.29600 0.35620 0.25230 -0.05350 0.04790  -0.00540 112 ILE A CG2   
853  C  CD1   . ILE A 112 ? 0.32480 0.37520 0.29030 -0.05030 0.03500  0.00220  112 ILE A CD1   
854  N  N     . LEU A 113 ? 0.27730 0.33730 0.21520 -0.06460 0.06120  0.00540  113 LEU A N     
855  C  CA    . LEU A 113 ? 0.27460 0.34100 0.21220 -0.06790 0.07020  0.00310  113 LEU A CA    
856  C  C     . LEU A 113 ? 0.29940 0.36520 0.21810 -0.07020 0.07380  0.00570  113 LEU A C     
857  O  O     . LEU A 113 ? 0.32250 0.39440 0.23760 -0.07100 0.07980  0.00050  113 LEU A O     
858  C  CB    . LEU A 113 ? 0.28460 0.35220 0.23260 -0.07160 0.07470  0.00610  113 LEU A CB    
859  C  CG    . LEU A 113 ? 0.27940 0.35150 0.24670 -0.06960 0.07240  0.00150  113 LEU A CG    
860  C  CD1   . LEU A 113 ? 0.30350 0.37580 0.28070 -0.07380 0.07520  0.00460  113 LEU A CD1   
861  C  CD2   . LEU A 113 ? 0.29130 0.37280 0.26730 -0.06760 0.07640  -0.00640 113 LEU A CD2   
862  N  N     . ALA A 114 ? 0.35270 0.41150 0.25970 -0.07080 0.07010  0.01370  114 ALA A N     
863  C  CA    . ALA A 114 ? 0.37170 0.42990 0.25890 -0.07230 0.07190  0.01770  114 ALA A CA    
864  C  C     . ALA A 114 ? 0.40900 0.47070 0.28760 -0.06950 0.06840  0.01080  114 ALA A C     
865  O  O     . ALA A 114 ? 0.41060 0.47740 0.27770 -0.07090 0.07330  0.00770  114 ALA A O     
866  C  CB    . ALA A 114 ? 0.36260 0.41220 0.24120 -0.07260 0.06740  0.02830  114 ALA A CB    
867  N  N     . LYS A 115 ? 0.42220 0.48150 0.30700 -0.06570 0.06040  0.00790  115 LYS A N     
868  C  CA    . LYS A 115 ? 0.43960 0.50170 0.31980 -0.06310 0.05670  0.00050  115 LYS A CA    
869  C  C     . LYS A 115 ? 0.45350 0.52250 0.33950 -0.06330 0.06320  -0.00950 115 LYS A C     
870  O  O     . LYS A 115 ? 0.40020 0.47310 0.27630 -0.06350 0.06470  -0.01530 115 LYS A O     
871  C  CB    . LYS A 115 ? 0.43300 0.49100 0.32230 -0.05940 0.04820  -0.00060 115 LYS A CB    
872  C  CG    . LYS A 115 ? 0.61730 0.67720 0.50270 -0.05730 0.04390  -0.00760 115 LYS A CG    
873  C  CD    . LYS A 115 ? 0.76930 0.82940 0.63680 -0.05790 0.03970  -0.00420 115 LYS A CD    
874  C  CE    . LYS A 115 ? 0.87100 0.93410 0.73560 -0.05640 0.03530  -0.01240 115 LYS A CE    
875  N  NZ    . LYS A 115 ? 0.90250 0.96170 0.77870 -0.05350 0.02830  -0.01320 115 LYS A NZ    
876  N  N     . GLN A 116 ? 0.35960 0.43040 0.26210 -0.06290 0.06680  -0.01180 116 GLN A N     
877  C  CA    . GLN A 116 ? 0.48080 0.55800 0.39190 -0.06230 0.07320  -0.02090 116 GLN A CA    
878  C  C     . GLN A 116 ? 0.48220 0.56520 0.38290 -0.06590 0.08220  -0.02260 116 GLN A C     
879  O  O     . GLN A 116 ? 0.47490 0.56300 0.37520 -0.06540 0.08670  -0.03130 116 GLN A O     
880  C  CB    . GLN A 116 ? 0.51170 0.59080 0.44280 -0.06090 0.07460  -0.02160 116 GLN A CB    
881  C  CG    . GLN A 116 ? 0.55310 0.62860 0.49560 -0.05650 0.06720  -0.02260 116 GLN A CG    
882  C  CD    . GLN A 116 ? 0.54260 0.62130 0.50340 -0.05480 0.06790  -0.02300 116 GLN A CD    
883  O  OE1   . GLN A 116 ? 0.47630 0.55800 0.44160 -0.05750 0.07170  -0.02020 116 GLN A OE1   
884  N  NE2   . GLN A 116 ? 0.53470 0.61290 0.50610 -0.05030 0.06420  -0.02630 116 GLN A NE2   
885  N  N     . LYS A 117 ? 0.48060 0.56240 0.37330 -0.06960 0.08540  -0.01440 117 LYS A N     
886  C  CA    . LYS A 117 ? 0.47590 0.56280 0.35720 -0.07350 0.09460  -0.01420 117 LYS A CA    
887  C  C     . LYS A 117 ? 0.45340 0.54170 0.31360 -0.07380 0.09360  -0.01610 117 LYS A C     
888  O  O     . LYS A 117 ? 0.47760 0.57250 0.33110 -0.07530 0.10070  -0.02250 117 LYS A O     
889  C  CB    . LYS A 117 ? 0.52760 0.61130 0.40620 -0.07740 0.09790  -0.00350 117 LYS A CB    
890  C  CG    . LYS A 117 ? 0.70430 0.79280 0.57170 -0.08200 0.10860  -0.00190 117 LYS A CG    
891  C  CD    . LYS A 117 ? 1.00340 1.08760 0.87160 -0.08610 0.11250  0.00880  117 LYS A CD    
892  C  CE    . LYS A 117 ? 0.99490 1.08360 0.85110 -0.09090 0.12390  0.01140  117 LYS A CE    
893  N  NZ    . LYS A 117 ? 1.22340 1.32240 1.09000 -0.09200 0.13300  0.00130  117 LYS A NZ    
894  N  N     . ILE A 118 ? 0.44430 0.52720 0.29460 -0.07230 0.08460  -0.01100 118 ILE A N     
895  C  CA    . ILE A 118 ? 0.55100 0.63590 0.38090 -0.07230 0.08180  -0.01220 118 ILE A CA    
896  C  C     . ILE A 118 ? 0.75030 0.83880 0.58370 -0.06980 0.07920  -0.02480 118 ILE A C     
897  O  O     . ILE A 118 ? 0.53530 0.63000 0.35760 -0.07100 0.08320  -0.03210 118 ILE A O     
898  C  CB    . ILE A 118 ? 0.68850 0.76710 0.50910 -0.07100 0.07230  -0.00240 118 ILE A CB    
899  C  CG1   . ILE A 118 ? 0.76450 0.83830 0.58080 -0.07340 0.07530  0.01050  118 ILE A CG1   
900  C  CG2   . ILE A 118 ? 0.72590 0.80840 0.52660 -0.07040 0.06790  -0.00450 118 ILE A CG2   
901  C  CD1   . ILE A 118 ? 0.73860 0.80450 0.55220 -0.07130 0.06620  0.02040  118 ILE A CD1   
902  N  N     . HIS A 119 ? 0.68080 0.76510 0.52970 -0.06660 0.07290  -0.02730 119 HIS A N     
903  C  CA    . HIS A 119 ? 0.59550 0.68100 0.44930 -0.06410 0.06920  -0.03760 119 HIS A CA    
904  C  C     . HIS A 119 ? 0.54650 0.63160 0.42180 -0.06190 0.07250  -0.04380 119 HIS A C     
905  O  O     . HIS A 119 ? 0.49330 0.57370 0.38140 -0.05900 0.06690  -0.04290 119 HIS A O     
906  C  CB    . HIS A 119 ? 0.66520 0.74560 0.51730 -0.06200 0.05840  -0.03390 119 HIS A CB    
907  C  CG    . HIS A 119 ? 1.01220 1.09450 0.86410 -0.06070 0.05420  -0.04380 119 HIS A CG    
908  N  ND1   . HIS A 119 ? 1.30350 1.38810 1.14010 -0.06130 0.04820  -0.04420 119 HIS A ND1   
909  C  CD2   . HIS A 119 ? 1.03540 1.11710 0.90150 -0.05890 0.05480  -0.05330 119 HIS A CD2   
910  C  CE1   . HIS A 119 ? 1.07420 1.16010 0.91600 -0.06040 0.04550  -0.05460 119 HIS A CE1   
911  N  NE2   . HIS A 119 ? 1.20120 1.28460 1.06080 -0.05900 0.04970  -0.06000 119 HIS A NE2   
912  N  N     . PRO A 120 ? 0.47920 0.56980 0.35930 -0.06280 0.08170  -0.05010 120 PRO A N     
913  C  CA    . PRO A 120 ? 0.61000 0.70110 0.51140 -0.06010 0.08490  -0.05480 120 PRO A CA    
914  C  C     . PRO A 120 ? 0.77650 0.86520 0.68800 -0.05650 0.08160  -0.06350 120 PRO A C     
915  O  O     . PRO A 120 ? 0.65310 0.73960 0.58200 -0.05330 0.08070  -0.06360 120 PRO A O     
916  C  CB    . PRO A 120 ? 0.58580 0.68440 0.48710 -0.06220 0.09590  -0.05990 120 PRO A CB    
917  C  CG    . PRO A 120 ? 0.72490 0.82690 0.60440 -0.06520 0.09800  -0.06300 120 PRO A CG    
918  C  CD    . PRO A 120 ? 0.76420 0.86140 0.62970 -0.06620 0.08960  -0.05310 120 PRO A CD    
919  N  N     . GLU A 121 ? 0.78460 0.77390 0.78860 -0.03300 -0.01160 0.01440  121 GLU A N     
920  C  CA    . GLU A 121 ? 0.69410 0.68370 0.69620 -0.03370 -0.01240 0.01480  121 GLU A CA    
921  C  C     . GLU A 121 ? 0.66920 0.66000 0.67020 -0.03370 -0.01240 0.01510  121 GLU A C     
922  O  O     . GLU A 121 ? 0.66720 0.65890 0.66880 -0.03320 -0.01200 0.01500  121 GLU A O     
923  C  CB    . GLU A 121 ? 0.70510 0.69520 0.70690 -0.03420 -0.01210 0.01550  121 GLU A CB    
924  C  CG    . GLU A 121 ? 0.81960 0.81180 0.82120 -0.03390 -0.01160 0.01610  121 GLU A CG    
925  C  CD    . GLU A 121 ? 0.90130 0.89320 0.90360 -0.03270 -0.01070 0.01640  121 GLU A CD    
926  O  OE1   . GLU A 121 ? 0.75890 0.74910 0.76230 -0.03230 -0.01030 0.01600  121 GLU A OE1   
927  O  OE2   . GLU A 121 ? 0.93500 0.92850 0.93690 -0.03190 -0.01040 0.01690  121 GLU A OE2   
928  N  N     . ARG A 122 ? 0.55220 0.62850 0.47860 -0.05040 0.06650  -0.08100 122 ARG A N     
929  C  CA    . ARG A 122 ? 0.45580 0.52560 0.38970 -0.04830 0.05880  -0.07750 122 ARG A CA    
930  C  C     . ARG A 122 ? 0.49520 0.56540 0.41400 -0.05060 0.05160  -0.07510 122 ARG A C     
931  O  O     . ARG A 122 ? 0.46190 0.53640 0.36960 -0.05300 0.05210  -0.08250 122 ARG A O     
932  C  CB    . ARG A 122 ? 0.56240 0.62850 0.51100 -0.04590 0.06040  -0.08630 122 ARG A CB    
933  C  CG    . ARG A 122 ? 0.65840 0.71780 0.61640 -0.04380 0.05410  -0.08280 122 ARG A CG    
934  C  CD    . ARG A 122 ? 0.75540 0.81020 0.72880 -0.04150 0.05700  -0.09090 122 ARG A CD    
935  N  NE    . ARG A 122 ? 0.80000 0.85360 0.78790 -0.03750 0.06230  -0.08950 122 ARG A NE    
936  C  CZ    . ARG A 122 ? 0.72500 0.77460 0.72440 -0.03380 0.06030  -0.08180 122 ARG A CZ    
937  N  NH1   . ARG A 122 ? 0.62340 0.66930 0.62160 -0.03360 0.05370  -0.07490 122 ARG A NH1   
938  N  NH2   . ARG A 122 ? 0.88350 0.93360 0.89550 -0.02990 0.06480  -0.08120 122 ARG A NH2   
939  N  N     . THR A 123 ? 0.52090 0.58760 0.43970 -0.04980 0.04510  -0.06550 123 THR A N     
940  C  CA    . THR A 123 ? 0.45560 0.52270 0.36220 -0.05120 0.03760  -0.06190 123 THR A CA    
941  C  C     . THR A 123 ? 0.47840 0.54230 0.39340 -0.05000 0.03190  -0.06560 123 THR A C     
942  O  O     . THR A 123 ? 0.45370 0.51330 0.38400 -0.04790 0.03370  -0.06840 123 THR A O     
943  C  CB    . THR A 123 ? 0.58800 0.65280 0.49110 -0.05080 0.03400  -0.04930 123 THR A CB    
944  O  OG1   . THR A 123 ? 0.46120 0.52070 0.37950 -0.04810 0.03250  -0.04540 123 THR A OG1   
945  C  CG2   . THR A 123 ? 0.52310 0.59070 0.41870 -0.05260 0.03980  -0.04490 123 THR A CG2   
946  N  N     . PRO A 124 ? 0.58460 0.65060 0.49040 -0.05130 0.02510  -0.06540 124 PRO A N     
947  C  CA    . PRO A 124 ? 0.50070 0.56390 0.41550 -0.05050 0.01930  -0.06770 124 PRO A CA    
948  C  C     . PRO A 124 ? 0.52850 0.58540 0.45540 -0.04770 0.01700  -0.05930 124 PRO A C     
949  O  O     . PRO A 124 ? 0.52560 0.57960 0.46260 -0.04690 0.01420  -0.06150 124 PRO A O     
950  C  CB    . PRO A 124 ? 0.52510 0.59370 0.42600 -0.05210 0.01200  -0.06670 124 PRO A CB    
951  C  CG    . PRO A 124 ? 0.69160 0.76640 0.57540 -0.05420 0.01530  -0.06840 124 PRO A CG    
952  C  CD    . PRO A 124 ? 0.70310 0.77490 0.58950 -0.05340 0.02260  -0.06310 124 PRO A CD    
953  N  N     . SER A 125 ? 0.55250 0.60770 0.47820 -0.04660 0.01830  -0.05040 125 SER A N     
954  C  CA    . SER A 125 ? 0.43930 0.48940 0.37580 -0.04410 0.01680  -0.04320 125 SER A CA    
955  C  C     . SER A 125 ? 0.48810 0.53500 0.43920 -0.04190 0.02170  -0.04600 125 SER A C     
956  O  O     . SER A 125 ? 0.42720 0.47030 0.38780 -0.03960 0.02020  -0.04140 125 SER A O     
957  C  CB    . SER A 125 ? 0.42190 0.47180 0.35260 -0.04410 0.01690  -0.03400 125 SER A CB    
958  O  OG    . SER A 125 ? 0.56860 0.62010 0.48680 -0.04540 0.01220  -0.02950 125 SER A OG    
959  N  N     . GLU A 126 ? 0.55180 0.60070 0.50460 -0.04230 0.02760  -0.05320 126 GLU A N     
960  C  CA    . GLU A 126 ? 0.42420 0.47080 0.39040 -0.03970 0.03290  -0.05510 126 GLU A CA    
961  C  C     . GLU A 126 ? 0.44620 0.49080 0.42050 -0.03940 0.03580  -0.06470 126 GLU A C     
962  O  O     . GLU A 126 ? 0.47160 0.51690 0.45130 -0.03850 0.04190  -0.07010 126 GLU A O     
963  C  CB    . GLU A 126 ? 0.45090 0.50170 0.41430 -0.04000 0.03860  -0.05470 126 GLU A CB    
964  C  CG    . GLU A 126 ? 0.54140 0.59380 0.49840 -0.04090 0.03700  -0.04580 126 GLU A CG    
965  C  CD    . GLU A 126 ? 0.55150 0.60900 0.50320 -0.04270 0.04300  -0.04660 126 GLU A CD    
966  O  OE1   . GLU A 126 ? 0.54170 0.60250 0.48090 -0.04550 0.04470  -0.04990 126 GLU A OE1   
967  O  OE2   . GLU A 126 ? 0.42720 0.48620 0.38710 -0.04140 0.04630  -0.04400 126 GLU A OE2   
968  N  N     . LYS A 127 ? 0.42290 0.46490 0.39930 -0.04020 0.03180  -0.06730 127 LYS A N     
969  C  CA    . LYS A 127 ? 0.52620 0.56540 0.51160 -0.04050 0.03450  -0.07690 127 LYS A CA    
970  C  C     . LYS A 127 ? 0.46540 0.49850 0.46730 -0.03660 0.03910  -0.07590 127 LYS A C     
971  O  O     . LYS A 127 ? 0.55520 0.58640 0.56480 -0.03600 0.04450  -0.08350 127 LYS A O     
972  C  CB    . LYS A 127 ? 0.55700 0.59530 0.54230 -0.04270 0.02900  -0.07950 127 LYS A CB    
973  C  CG    . LYS A 127 ? 0.59500 0.64040 0.56460 -0.04620 0.02420  -0.08210 127 LYS A CG    
974  C  CD    . LYS A 127 ? 0.69470 0.74040 0.66680 -0.04790 0.01830  -0.08470 127 LYS A CD    
975  C  CE    . LYS A 127 ? 0.61580 0.66900 0.57240 -0.05010 0.01160  -0.08370 127 LYS A CE    
976  N  NZ    . LYS A 127 ? 0.64720 0.70690 0.59130 -0.05260 0.01360  -0.09150 127 LYS A NZ    
977  N  N     . LEU A 128 ? 0.45440 0.48470 0.46160 -0.03370 0.03680  -0.06630 128 LEU A N     
978  C  CA    . LEU A 128 ? 0.43260 0.45750 0.45420 -0.02940 0.04010  -0.06330 128 LEU A CA    
979  C  C     . LEU A 128 ? 0.44890 0.47640 0.47250 -0.02590 0.04160  -0.05640 128 LEU A C     
980  O  O     . LEU A 128 ? 0.43000 0.45510 0.46500 -0.02190 0.04520  -0.05550 128 LEU A O     
981  C  CB    . LEU A 128 ? 0.46280 0.48240 0.49060 -0.02850 0.03670  -0.05840 128 LEU A CB    
982  C  CG    . LEU A 128 ? 0.52200 0.53790 0.55440 -0.03120 0.03660  -0.06570 128 LEU A CG    
983  C  CD1   . LEU A 128 ? 0.52390 0.53510 0.56290 -0.03030 0.03400  -0.05980 128 LEU A CD1   
984  C  CD2   . LEU A 128 ? 0.59840 0.61010 0.64140 -0.03040 0.04310  -0.07400 128 LEU A CD2   
985  N  N     . LEU A 129 ? 0.42900 0.46140 0.44230 -0.02740 0.03870  -0.05160 129 LEU A N     
986  C  CA    . LEU A 129 ? 0.35730 0.39340 0.37240 -0.02520 0.03960  -0.04580 129 LEU A CA    
987  C  C     . LEU A 129 ? 0.35960 0.40150 0.36280 -0.02850 0.03960  -0.04550 129 LEU A C     
988  O  O     . LEU A 129 ? 0.36360 0.40580 0.35640 -0.03140 0.03550  -0.04300 129 LEU A O     
989  C  CB    . LEU A 129 ? 0.35870 0.39290 0.37630 -0.02300 0.03510  -0.03720 129 LEU A CB    
990  C  CG    . LEU A 129 ? 0.41700 0.45560 0.43770 -0.02060 0.03510  -0.03160 129 LEU A CG    
991  C  CD1   . LEU A 129 ? 0.50480 0.54470 0.53750 -0.01630 0.03950  -0.03310 129 LEU A CD1   
992  C  CD2   . LEU A 129 ? 0.42580 0.46300 0.44680 -0.01920 0.03020  -0.02440 129 LEU A CD2   
993  N  N     . ALA A 130 ? 0.37870 0.42520 0.38430 -0.02800 0.04460  -0.04760 130 ALA A N     
994  C  CA    . ALA A 130 ? 0.42720 0.47920 0.42280 -0.03130 0.04620  -0.04690 130 ALA A CA    
995  C  C     . ALA A 130 ? 0.45710 0.51160 0.45460 -0.03070 0.04440  -0.03920 130 ALA A C     
996  O  O     . ALA A 130 ? 0.37970 0.43400 0.38790 -0.02700 0.04340  -0.03610 130 ALA A O     
997  C  CB    . ALA A 130 ? 0.40270 0.45910 0.40040 -0.03160 0.05340  -0.05400 130 ALA A CB    
998  N  N     . VAL A 131 ? 0.37690 0.43400 0.36410 -0.03430 0.04390  -0.03610 131 VAL A N     
999  C  CA    . VAL A 131 ? 0.42310 0.48250 0.41180 -0.03490 0.04270  -0.02980 131 VAL A CA    
1000 C  C     . VAL A 131 ? 0.38130 0.44660 0.38210 -0.03280 0.04700  -0.03120 131 VAL A C     
1001 O  O     . VAL A 131 ? 0.32940 0.39640 0.33810 -0.03080 0.04470  -0.02740 131 VAL A O     
1002 C  CB    . VAL A 131 ? 0.40960 0.47000 0.38560 -0.03950 0.04330  -0.02680 131 VAL A CB    
1003 C  CG1   . VAL A 131 ? 0.37970 0.44240 0.35940 -0.04070 0.04350  -0.02160 131 VAL A CG1   
1004 C  CG2   . VAL A 131 ? 0.41550 0.47090 0.38060 -0.04080 0.03780  -0.02420 131 VAL A CG2   
1005 N  N     . LYS A 132 ? 0.45330 0.52230 0.45570 -0.03310 0.05320  -0.03710 132 LYS A N     
1006 C  CA    . LYS A 132 ? 0.50230 0.57780 0.51750 -0.03070 0.05790  -0.03950 132 LYS A CA    
1007 C  C     . LYS A 132 ? 0.39540 0.47000 0.42450 -0.02480 0.05550  -0.03870 132 LYS A C     
1008 O  O     . LYS A 132 ? 0.48080 0.56140 0.52100 -0.02210 0.05640  -0.03770 132 LYS A O     
1009 C  CB    . LYS A 132 ? 0.57500 0.65380 0.58940 -0.03170 0.06520  -0.04710 132 LYS A CB    
1010 C  CG    . LYS A 132 ? 0.86590 0.94770 0.86700 -0.03730 0.06900  -0.04750 132 LYS A CG    
1011 C  CD    . LYS A 132 ? 0.99120 1.07970 0.99730 -0.03920 0.07220  -0.04440 132 LYS A CD    
1012 C  CE    . LYS A 132 ? 1.07170 1.16310 1.06530 -0.04470 0.07770  -0.04470 132 LYS A CE    
1013 N  NZ    . LYS A 132 ? 1.14910 1.24680 1.14880 -0.04730 0.08140  -0.04160 132 LYS A NZ    
1014 N  N     . GLU A 133 ? 0.37900 0.44650 0.40760 -0.02270 0.05270  -0.03910 133 GLU A N     
1015 C  CA    . GLU A 133 ? 0.37670 0.44170 0.41710 -0.01700 0.05090  -0.03740 133 GLU A CA    
1016 C  C     . GLU A 133 ? 0.42970 0.49320 0.47020 -0.01550 0.04450  -0.03000 133 GLU A C     
1017 O  O     . GLU A 133 ? 0.30600 0.36780 0.35480 -0.01070 0.04270  -0.02730 133 GLU A O     
1018 C  CB    . GLU A 133 ? 0.44020 0.49760 0.48110 -0.01590 0.05200  -0.04180 133 GLU A CB    
1019 C  CG    . GLU A 133 ? 0.41470 0.47330 0.45670 -0.01690 0.05850  -0.05050 133 GLU A CG    
1020 C  CD    . GLU A 133 ? 0.61060 0.66170 0.65140 -0.01740 0.05910  -0.05600 133 GLU A CD    
1021 O  OE1   . GLU A 133 ? 0.36170 0.40710 0.39910 -0.01800 0.05440  -0.05300 133 GLU A OE1   
1022 O  OE2   . GLU A 133 ? 0.78300 0.83430 0.82690 -0.01750 0.06470  -0.06420 133 GLU A OE2   
1023 N  N     . PHE A 134 ? 0.37900 0.44310 0.41030 -0.01940 0.04140  -0.02670 134 PHE A N     
1024 C  CA    . PHE A 134 ? 0.24290 0.30600 0.27350 -0.01870 0.03570  -0.02080 134 PHE A CA    
1025 C  C     . PHE A 134 ? 0.24180 0.31120 0.28320 -0.01450 0.03460  -0.01820 134 PHE A C     
1026 O  O     . PHE A 134 ? 0.21750 0.29430 0.26540 -0.01410 0.03740  -0.02010 134 PHE A O     
1027 C  CB    . PHE A 134 ? 0.33960 0.40320 0.36080 -0.02360 0.03380  -0.01840 134 PHE A CB    
1028 C  CG    . PHE A 134 ? 0.31890 0.37590 0.32880 -0.02650 0.03160  -0.01790 134 PHE A CG    
1029 C  CD1   . PHE A 134 ? 0.34540 0.39710 0.35400 -0.02530 0.03080  -0.01990 134 PHE A CD1   
1030 C  CD2   . PHE A 134 ? 0.30770 0.36410 0.30910 -0.03050 0.03010  -0.01510 134 PHE A CD2   
1031 C  CE1   . PHE A 134 ? 0.34840 0.39580 0.34750 -0.02800 0.02800  -0.01960 134 PHE A CE1   
1032 C  CE2   . PHE A 134 ? 0.28250 0.33380 0.27410 -0.03260 0.02740  -0.01390 134 PHE A CE2   
1033 C  CZ    . PHE A 134 ? 0.28040 0.32800 0.27090 -0.03130 0.02610  -0.01640 134 PHE A CZ    
1034 N  N     . GLU A 135 ? 0.29760 0.36490 0.34070 -0.01140 0.03020  -0.01390 135 GLU A N     
1035 C  CA    . GLU A 135 ? 0.35540 0.42930 0.40630 -0.00740 0.02760  -0.01070 135 GLU A CA    
1036 C  C     . GLU A 135 ? 0.39840 0.47850 0.44710 -0.01110 0.02560  -0.01020 135 GLU A C     
1037 O  O     . GLU A 135 ? 0.31320 0.38930 0.35330 -0.01540 0.02410  -0.00940 135 GLU A O     
1038 C  CB    . GLU A 135 ? 0.36620 0.43540 0.41640 -0.00380 0.02390  -0.00600 135 GLU A CB    
1039 C  CG    . GLU A 135 ? 0.47850 0.55470 0.53510 0.00110  0.02070  -0.00210 135 GLU A CG    
1040 C  CD    . GLU A 135 ? 0.58830 0.66950 0.65620 0.00650  0.02290  -0.00250 135 GLU A CD    
1041 O  OE1   . GLU A 135 ? 0.76220 0.83710 0.83390 0.00980  0.02570  -0.00220 135 GLU A OE1   
1042 O  OE2   . GLU A 135 ? 0.59750 0.68910 0.67160 0.00760  0.02190  -0.00320 135 GLU A OE2   
1043 N  N     . SER A 136 ? 0.26190 0.35180 0.31960 -0.00940 0.02580  -0.01090 136 SER A N     
1044 C  CA    . SER A 136 ? 0.29190 0.38880 0.35050 -0.01310 0.02430  -0.01130 136 SER A CA    
1045 C  C     . SER A 136 ? 0.28140 0.38500 0.34450 -0.00990 0.01880  -0.00890 136 SER A C     
1046 O  O     . SER A 136 ? 0.27690 0.38300 0.33800 -0.01340 0.01630  -0.00910 136 SER A O     
1047 C  CB    . SER A 136 ? 0.30030 0.40540 0.36670 -0.01480 0.02890  -0.01520 136 SER A CB    
1048 O  OG    . SER A 136 ? 0.30060 0.41370 0.37900 -0.00890 0.02870  -0.01570 136 SER A OG    
1049 N  N     . HIS A 137 ? 0.31200 0.41850 0.38120 -0.00340 0.01720  -0.00680 137 HIS A N     
1050 C  CA    . HIS A 137 ? 0.28570 0.40100 0.35960 0.00070  0.01210  -0.00450 137 HIS A CA    
1051 C  C     . HIS A 137 ? 0.24910 0.37730 0.33090 -0.00160 0.01120  -0.00810 137 HIS A C     
1052 O  O     . HIS A 137 ? 0.33290 0.46800 0.41530 -0.00160 0.00640  -0.00790 137 HIS A O     
1053 C  CB    . HIS A 137 ? 0.33530 0.44590 0.40000 0.00030  0.00780  -0.00140 137 HIS A CB    
1054 C  CG    . HIS A 137 ? 0.30540 0.40580 0.36490 0.00340  0.00830  0.00250  137 HIS A CG    
1055 N  ND1   . HIS A 137 ? 0.38700 0.48750 0.45140 0.01010  0.00840  0.00610  137 HIS A ND1   
1056 C  CD2   . HIS A 137 ? 0.42240 0.51220 0.47310 0.00080  0.00870  0.00350  137 HIS A CD2   
1057 C  CE1   . HIS A 137 ? 0.40340 0.49320 0.46240 0.01080  0.00950  0.00890  137 HIS A CE1   
1058 N  NE2   . HIS A 137 ? 0.39690 0.48080 0.44790 0.00520  0.00950  0.00710  137 HIS A NE2   
1059 N  N     . LEU A 138 ? 0.28540 0.41720 0.37370 -0.00380 0.01600  -0.01180 138 LEU A N     
1060 C  CA    . LEU A 138 ? 0.38330 0.52680 0.48030 -0.00730 0.01660  -0.01580 138 LEU A CA    
1061 C  C     . LEU A 138 ? 0.27380 0.43140 0.38080 -0.00250 0.01120  -0.01570 138 LEU A C     
1062 O  O     . LEU A 138 ? 0.35770 0.52360 0.46770 -0.00570 0.00810  -0.01820 138 LEU A O     
1063 C  CB    . LEU A 138 ? 0.29160 0.43730 0.39500 -0.00910 0.02350  -0.01940 138 LEU A CB    
1064 C  CG    . LEU A 138 ? 0.40370 0.56130 0.51730 -0.01340 0.02580  -0.02380 138 LEU A CG    
1065 C  CD1   . LEU A 138 ? 0.36000 0.51410 0.46690 -0.02110 0.02550  -0.02440 138 LEU A CD1   
1066 C  CD2   . LEU A 138 ? 0.50250 0.66150 0.62140 -0.01460 0.03360  -0.02720 138 LEU A CD2   
1067 N  N     . ASP A 139 ? 0.34910 0.50900 0.46130 0.00540  0.00990  -0.01280 139 ASP A N     
1068 C  CA    . ASP A 139 ? 0.36420 0.53790 0.48560 0.01170  0.00430  -0.01140 139 ASP A CA    
1069 C  C     . ASP A 139 ? 0.35330 0.52920 0.46720 0.01280  -0.00280 -0.00860 139 ASP A C     
1070 O  O     . ASP A 139 ? 0.38180 0.57110 0.50170 0.01700  -0.00820 -0.00820 139 ASP A O     
1071 C  CB    . ASP A 139 ? 0.40140 0.57450 0.52920 0.02050  0.00520  -0.00750 139 ASP A CB    
1072 C  CG    . ASP A 139 ? 0.61450 0.77250 0.73160 0.02340  0.00560  -0.00190 139 ASP A CG    
1073 O  OD1   . ASP A 139 ? 0.68550 0.83100 0.79270 0.01800  0.00890  -0.00290 139 ASP A OD1   
1074 O  OD2   . ASP A 139 ? 0.94860 1.10750 1.06770 0.03100  0.00270  0.00360  139 ASP A OD2   
1075 N  N     . LYS A 140 ? 0.30400 0.46750 0.40460 0.00940  -0.00260 -0.00690 140 LYS A N     
1076 C  CA    . LYS A 140 ? 0.34870 0.51280 0.44100 0.01010  -0.00820 -0.00470 140 LYS A CA    
1077 C  C     . LYS A 140 ? 0.31750 0.48380 0.40700 0.00260  -0.00970 -0.00970 140 LYS A C     
1078 O  O     . LYS A 140 ? 0.32990 0.50040 0.41500 0.00290  -0.01460 -0.00990 140 LYS A O     
1079 C  CB    . LYS A 140 ? 0.43260 0.58190 0.51350 0.01190  -0.00710 0.00050  140 LYS A CB    
1080 C  CG    . LYS A 140 ? 0.65150 0.79600 0.73550 0.01860  -0.00480 0.00540  140 LYS A CG    
1081 C  CD    . LYS A 140 ? 0.63450 0.78650 0.71980 0.02670  -0.00970 0.01100  140 LYS A CD    
1082 C  CE    . LYS A 140 ? 0.78060 0.92350 0.86650 0.03310  -0.00700 0.01740  140 LYS A CE    
1083 N  NZ    . LYS A 140 ? 0.77930 0.90690 0.85450 0.03060  -0.00440 0.02000  140 LYS A NZ    
1084 N  N     . LEU A 141 ? 0.22520 0.38850 0.31740 -0.00410 -0.00500 -0.01380 141 LEU A N     
1085 C  CA    . LEU A 141 ? 0.21850 0.38140 0.30910 -0.01160 -0.00510 -0.01820 141 LEU A CA    
1086 C  C     . LEU A 141 ? 0.23590 0.41550 0.33640 -0.01230 -0.00960 -0.02300 141 LEU A C     
1087 O  O     . LEU A 141 ? 0.19860 0.38980 0.31100 -0.01070 -0.00920 -0.02520 141 LEU A O     
1088 C  CB    . LEU A 141 ? 0.32950 0.48600 0.42140 -0.01810 0.00150  -0.02030 141 LEU A CB    
1089 C  CG    . LEU A 141 ? 0.36860 0.51000 0.45100 -0.01850 0.00600  -0.01680 141 LEU A CG    
1090 C  CD1   . LEU A 141 ? 0.38600 0.52380 0.46940 -0.02460 0.01240  -0.01890 141 LEU A CD1   
1091 C  CD2   . LEU A 141 ? 0.40630 0.53660 0.47680 -0.01920 0.00380  -0.01410 141 LEU A CD2   
1092 N  N     . ASP A 142 ? 0.30600 0.48740 0.40220 -0.01450 -0.01370 -0.02540 142 ASP A N     
1093 C  CA    . ASP A 142 ? 0.33000 0.52710 0.43520 -0.01660 -0.01810 -0.03160 142 ASP A CA    
1094 C  C     . ASP A 142 ? 0.35220 0.54890 0.46550 -0.02530 -0.01340 -0.03720 142 ASP A C     
1095 O  O     . ASP A 142 ? 0.35610 0.53970 0.46540 -0.02920 -0.00740 -0.03530 142 ASP A O     
1096 C  CB    . ASP A 142 ? 0.39280 0.59180 0.49000 -0.01590 -0.02380 -0.03290 142 ASP A CB    
1097 C  CG    . ASP A 142 ? 0.51840 0.70180 0.60570 -0.02080 -0.02120 -0.03280 142 ASP A CG    
1098 O  OD1   . ASP A 142 ? 0.69470 0.86710 0.78190 -0.02560 -0.01560 -0.03230 142 ASP A OD1   
1099 O  OD2   . ASP A 142 ? 0.82280 1.00560 0.90220 -0.01970 -0.02480 -0.03330 142 ASP A OD2   
1100 N  N     . ASN A 143 ? 0.22610 0.43750 0.35100 -0.02840 -0.01610 -0.04400 143 ASN A N     
1101 C  CA    . ASN A 143 ? 0.32420 0.53660 0.45920 -0.03700 -0.01110 -0.04950 143 ASN A CA    
1102 C  C     . ASN A 143 ? 0.30050 0.49760 0.42830 -0.04410 -0.00770 -0.05010 143 ASN A C     
1103 O  O     . ASN A 143 ? 0.29540 0.48590 0.42680 -0.05040 -0.00120 -0.05070 143 ASN A O     
1104 C  CB    . ASN A 143 ? 0.24570 0.47820 0.39580 -0.03890 -0.01540 -0.05740 143 ASN A CB    
1105 C  CG    . ASN A 143 ? 0.28980 0.53790 0.45070 -0.03280 -0.01730 -0.05690 143 ASN A CG    
1106 O  OD1   . ASN A 143 ? 0.30120 0.54430 0.46080 -0.02860 -0.01360 -0.05160 143 ASN A OD1   
1107 N  ND2   . ASN A 143 ? 0.28780 0.55570 0.46050 -0.03220 -0.02320 -0.06300 143 ASN A ND2   
1108 N  N     . GLU A 144 ? 0.28690 0.47850 0.40470 -0.04280 -0.01170 -0.04970 144 GLU A N     
1109 C  CA    . GLU A 144 ? 0.39190 0.56880 0.50340 -0.04840 -0.00890 -0.05010 144 GLU A CA    
1110 C  C     . GLU A 144 ? 0.31780 0.47800 0.42070 -0.04890 -0.00300 -0.04310 144 GLU A C     
1111 O  O     . GLU A 144 ? 0.29610 0.44690 0.39970 -0.05500 0.00200  -0.04300 144 GLU A O     
1112 C  CB    . GLU A 144 ? 0.37890 0.55390 0.48110 -0.04570 -0.01420 -0.05090 144 GLU A CB    
1113 C  CG    . GLU A 144 ? 0.62850 0.78690 0.72330 -0.04970 -0.01150 -0.05010 144 GLU A CG    
1114 C  CD    . GLU A 144 ? 0.80890 0.96930 0.89960 -0.04920 -0.01610 -0.05460 144 GLU A CD    
1115 O  OE1   . GLU A 144 ? 0.81890 0.99080 0.91800 -0.05230 -0.01890 -0.06280 144 GLU A OE1   
1116 O  OE2   . GLU A 144 ? 0.70010 0.85130 0.77970 -0.04590 -0.01680 -0.05070 144 GLU A OE2   
1117 N  N     . LYS A 145 ? 0.28530 0.44200 0.37990 -0.04230 -0.00390 -0.03720 145 LYS A N     
1118 C  CA    . LYS A 145 ? 0.31470 0.45740 0.40070 -0.04180 0.00070  -0.03120 145 LYS A CA    
1119 C  C     . LYS A 145 ? 0.30410 0.44790 0.39650 -0.04520 0.00680  -0.03130 145 LYS A C     
1120 O  O     . LYS A 145 ? 0.27680 0.40970 0.36450 -0.04930 0.01170  -0.02890 145 LYS A O     
1121 C  CB    . LYS A 145 ? 0.31990 0.46070 0.39840 -0.03420 -0.00160 -0.02620 145 LYS A CB    
1122 C  CG    . LYS A 145 ? 0.49450 0.63060 0.56390 -0.03130 -0.00590 -0.02460 145 LYS A CG    
1123 C  CD    . LYS A 145 ? 0.68140 0.81520 0.74450 -0.02420 -0.00720 -0.01920 145 LYS A CD    
1124 C  CE    . LYS A 145 ? 0.71490 0.85110 0.77220 -0.02030 -0.01220 -0.01840 145 LYS A CE    
1125 N  NZ    . LYS A 145 ? 0.77750 0.90450 0.82800 -0.02370 -0.01220 -0.01940 145 LYS A NZ    
1126 N  N     . LYS A 146 ? 0.25990 0.41760 0.36300 -0.04310 0.00640  -0.03390 146 LYS A N     
1127 C  CA    . LYS A 146 ? 0.26500 0.42660 0.37640 -0.04630 0.01260  -0.03510 146 LYS A CA    
1128 C  C     . LYS A 146 ? 0.23240 0.39100 0.34850 -0.05510 0.01730  -0.03790 146 LYS A C     
1129 O  O     . LYS A 146 ? 0.22620 0.37780 0.34010 -0.05900 0.02400  -0.03560 146 LYS A O     
1130 C  CB    . LYS A 146 ? 0.34360 0.52300 0.46860 -0.04260 0.01050  -0.03860 146 LYS A CB    
1131 C  CG    . LYS A 146 ? 0.48680 0.66840 0.61020 -0.03410 0.00910  -0.03500 146 LYS A CG    
1132 C  CD    . LYS A 146 ? 0.75520 0.93350 0.88010 -0.03440 0.01640  -0.03370 146 LYS A CD    
1133 C  CE    . LYS A 146 ? 0.80330 0.99370 0.93920 -0.02780 0.01600  -0.03450 146 LYS A CE    
1134 N  NZ    . LYS A 146 ? 0.92030 1.11080 1.05240 -0.01910 0.01020  -0.03060 146 LYS A NZ    
1135 N  N     . ASP A 147 ? 0.25820 0.42210 0.38060 -0.05840 0.01380  -0.04280 147 ASP A N     
1136 C  CA    . ASP A 147 ? 0.28230 0.44300 0.41110 -0.06710 0.01810  -0.04590 147 ASP A CA    
1137 C  C     . ASP A 147 ? 0.24160 0.38320 0.35850 -0.07020 0.02140  -0.04090 147 ASP A C     
1138 O  O     . ASP A 147 ? 0.27940 0.41440 0.39840 -0.07660 0.02770  -0.03980 147 ASP A O     
1139 C  CB    . ASP A 147 ? 0.29680 0.46910 0.43650 -0.06960 0.01320  -0.05380 147 ASP A CB    
1140 C  CG    . ASP A 147 ? 0.58460 0.77750 0.74010 -0.06870 0.01140  -0.05950 147 ASP A CG    
1141 O  OD1   . ASP A 147 ? 0.36850 0.56570 0.52850 -0.06750 0.01570  -0.05760 147 ASP A OD1   
1142 O  OD2   . ASP A 147 ? 0.44380 0.64940 0.60770 -0.06920 0.00570  -0.06630 147 ASP A OD2   
1143 N  N     . LEU A 148 ? 0.19750 0.33060 0.30220 -0.06560 0.01720  -0.03750 148 LEU A N     
1144 C  CA    . LEU A 148 ? 0.27970 0.39560 0.37280 -0.06710 0.01950  -0.03200 148 LEU A CA    
1145 C  C     . LEU A 148 ? 0.27020 0.37890 0.35600 -0.06710 0.02510  -0.02610 148 LEU A C     
1146 O  O     . LEU A 148 ? 0.26510 0.36330 0.34680 -0.07140 0.02970  -0.02250 148 LEU A O     
1147 C  CB    . LEU A 148 ? 0.34360 0.45390 0.42670 -0.06180 0.01380  -0.03020 148 LEU A CB    
1148 C  CG    . LEU A 148 ? 0.59740 0.71060 0.68420 -0.06270 0.00930  -0.03550 148 LEU A CG    
1149 C  CD1   . LEU A 148 ? 0.64710 0.75800 0.72420 -0.05650 0.00410  -0.03370 148 LEU A CD1   
1150 C  CD2   . LEU A 148 ? 0.58890 0.69150 0.67800 -0.06910 0.01260  -0.03640 148 LEU A CD2   
1151 N  N     . ILE A 149 ? 0.20950 0.32420 0.29390 -0.06220 0.02480  -0.02520 149 ILE A N     
1152 C  CA    . ILE A 149 ? 0.23470 0.34520 0.31320 -0.06220 0.03020  -0.02140 149 ILE A CA    
1153 C  C     . ILE A 149 ? 0.21150 0.32510 0.29760 -0.06870 0.03750  -0.02270 149 ILE A C     
1154 O  O     . ILE A 149 ? 0.25660 0.36170 0.33520 -0.07180 0.04300  -0.01850 149 ILE A O     
1155 C  CB    . ILE A 149 ? 0.21090 0.32830 0.28950 -0.05570 0.02890  -0.02170 149 ILE A CB    
1156 C  CG1   . ILE A 149 ? 0.18080 0.29190 0.24970 -0.04990 0.02350  -0.01890 149 ILE A CG1   
1157 C  CG2   . ILE A 149 ? 0.31250 0.42850 0.38820 -0.05670 0.03560  -0.02020 149 ILE A CG2   
1158 C  CD1   . ILE A 149 ? 0.18710 0.30390 0.25750 -0.04330 0.02190  -0.01890 149 ILE A CD1   
1159 N  N     . GLN A 150 ? 0.19820 0.32480 0.29920 -0.07080 0.03760  -0.02830 150 GLN A N     
1160 C  CA    . GLN A 150 ? 0.22820 0.35930 0.33880 -0.07740 0.04480  -0.03020 150 GLN A CA    
1161 C  C     . GLN A 150 ? 0.23900 0.35830 0.34740 -0.08440 0.04860  -0.02760 150 GLN A C     
1162 O  O     . GLN A 150 ? 0.25260 0.36830 0.36110 -0.08970 0.05640  -0.02510 150 GLN A O     
1163 C  CB    . GLN A 150 ? 0.23920 0.38770 0.36800 -0.07830 0.04330  -0.03750 150 GLN A CB    
1164 C  CG    . GLN A 150 ? 0.22770 0.38370 0.36730 -0.08350 0.05160  -0.03950 150 GLN A CG    
1165 C  CD    . GLN A 150 ? 0.27280 0.42910 0.40650 -0.07990 0.05610  -0.03670 150 GLN A CD    
1166 O  OE1   . GLN A 150 ? 0.26530 0.42670 0.39790 -0.07270 0.05190  -0.03720 150 GLN A OE1   
1167 N  NE2   . GLN A 150 ? 0.28920 0.43970 0.41870 -0.08490 0.06500  -0.03370 150 GLN A NE2   
1168 N  N     . SER A 151 ? 0.31280 0.42580 0.41920 -0.08430 0.04350  -0.02810 151 SER A N     
1169 C  CA    . SER A 151 ? 0.31840 0.41810 0.42230 -0.08970 0.04640  -0.02500 151 SER A CA    
1170 C  C     . SER A 151 ? 0.30020 0.38550 0.38780 -0.08870 0.04940  -0.01620 151 SER A C     
1171 O  O     . SER A 151 ? 0.37590 0.45240 0.46140 -0.09370 0.05550  -0.01180 151 SER A O     
1172 C  CB    . SER A 151 ? 0.33840 0.43530 0.44370 -0.08870 0.03990  -0.02830 151 SER A CB    
1173 O  OG    . SER A 151 ? 0.47730 0.56460 0.58690 -0.09500 0.04340  -0.02800 151 SER A OG    
1174 N  N     . ASP A 152 ? 0.31890 0.40240 0.39510 -0.08200 0.04510  -0.01370 152 ASP A N     
1175 C  CA    . ASP A 152 ? 0.32130 0.39390 0.38190 -0.08030 0.04680  -0.00650 152 ASP A CA    
1176 C  C     . ASP A 152 ? 0.32070 0.39530 0.37860 -0.08300 0.05450  -0.00420 152 ASP A C     
1177 O  O     . ASP A 152 ? 0.35450 0.41980 0.40230 -0.08530 0.05860  0.00210  152 ASP A O     
1178 C  CB    . ASP A 152 ? 0.30840 0.38090 0.36020 -0.07300 0.04080  -0.00600 152 ASP A CB    
1179 C  CG    . ASP A 152 ? 0.56230 0.62830 0.61140 -0.07040 0.03440  -0.00570 152 ASP A CG    
1180 O  OD1   . ASP A 152 ? 0.52530 0.58590 0.57840 -0.07400 0.03470  -0.00580 152 ASP A OD1   
1181 O  OD2   . ASP A 152 ? 0.51230 0.57830 0.55550 -0.06490 0.02970  -0.00540 152 ASP A OD2   
1182 N  N     . ILE A 153 ? 0.25360 0.34120 0.32060 -0.08260 0.05640  -0.00920 153 ILE A N     
1183 C  CA    . ILE A 153 ? 0.29680 0.38850 0.36350 -0.08530 0.06440  -0.00850 153 ILE A CA    
1184 C  C     . ILE A 153 ? 0.33460 0.42240 0.40560 -0.09330 0.07190  -0.00600 153 ILE A C     
1185 O  O     . ILE A 153 ? 0.30490 0.38720 0.36660 -0.09600 0.07860  -0.00080 153 ILE A O     
1186 C  CB    . ILE A 153 ? 0.26320 0.37060 0.34200 -0.08280 0.06480  -0.01510 153 ILE A CB    
1187 C  CG1   . ILE A 153 ? 0.29470 0.40330 0.36700 -0.07500 0.05940  -0.01570 153 ILE A CG1   
1188 C  CG2   . ILE A 153 ? 0.28660 0.39960 0.36860 -0.08670 0.07420  -0.01560 153 ILE A CG2   
1189 C  CD1   . ILE A 153 ? 0.31120 0.43410 0.39600 -0.07090 0.05810  -0.02150 153 ILE A CD1   
1190 N  N     . ALA A 154 ? 0.32510 0.41550 0.40990 -0.09710 0.07100  -0.00970 154 ALA A N     
1191 C  CA    . ALA A 154 ? 0.29460 0.37980 0.38560 -0.10510 0.07810  -0.00760 154 ALA A CA    
1192 C  C     . ALA A 154 ? 0.28620 0.35390 0.36280 -0.10620 0.07960  0.00160  154 ALA A C     
1193 O  O     . ALA A 154 ? 0.30610 0.36770 0.37920 -0.11110 0.08750  0.00730  154 ALA A O     
1194 C  CB    . ALA A 154 ? 0.25890 0.34960 0.36750 -0.10870 0.07560  -0.01440 154 ALA A CB    
1195 N  N     . ALA A 155 ? 0.26740 0.32730 0.33580 -0.10130 0.07190  0.00340  155 ALA A N     
1196 C  CA    . ALA A 155 ? 0.37740 0.42170 0.43250 -0.10090 0.07190  0.01220  155 ALA A CA    
1197 C  C     . ALA A 155 ? 0.36550 0.40700 0.40380 -0.09910 0.07520  0.01880  155 ALA A C     
1198 O  O     . ALA A 155 ? 0.34350 0.37500 0.37280 -0.10170 0.07980  0.02700  155 ALA A O     
1199 C  CB    . ALA A 155 ? 0.30760 0.34670 0.35920 -0.09550 0.06290  0.01140  155 ALA A CB    
1200 N  N     . LEU A 156 ? 0.32580 0.37610 0.35990 -0.09450 0.07280  0.01510  156 LEU A N     
1201 C  CA    . LEU A 156 ? 0.39270 0.44240 0.41170 -0.09280 0.07580  0.01910  156 LEU A CA    
1202 C  C     . LEU A 156 ? 0.38000 0.43120 0.39860 -0.09890 0.08630  0.02210  156 LEU A C     
1203 O  O     . LEU A 156 ? 0.29030 0.33430 0.29450 -0.10000 0.09010  0.02960  156 LEU A O     
1204 C  CB    . LEU A 156 ? 0.32640 0.38620 0.34530 -0.08760 0.07250  0.01290  156 LEU A CB    
1205 C  CG    . LEU A 156 ? 0.33610 0.39550 0.33950 -0.08500 0.07420  0.01500  156 LEU A CG    
1206 C  CD1   . LEU A 156 ? 0.32290 0.37160 0.31110 -0.08210 0.06890  0.02110  156 LEU A CD1   
1207 C  CD2   . LEU A 156 ? 0.34750 0.41710 0.35560 -0.08040 0.07210  0.00770  156 LEU A CD2   
1208 N  N     . HIS A 157 ? 0.37760 0.43880 0.41220 -0.10270 0.09090  0.01620  157 HIS A N     
1209 C  CA    . HIS A 157 ? 0.36000 0.42390 0.39770 -0.10920 0.10180  0.01810  157 HIS A CA    
1210 C  C     . HIS A 157 ? 0.42970 0.48070 0.46520 -0.11480 0.10650  0.02650  157 HIS A C     
1211 O  O     . HIS A 157 ? 0.41540 0.46170 0.44040 -0.11800 0.11420  0.03360  157 HIS A O     
1212 C  CB    . HIS A 157 ? 0.40640 0.48460 0.46510 -0.11210 0.10470  0.00930  157 HIS A CB    
1213 C  CG    . HIS A 157 ? 0.45520 0.54650 0.51610 -0.10760 0.10390  0.00270  157 HIS A CG    
1214 N  ND1   . HIS A 157 ? 0.51480 0.61140 0.57040 -0.10870 0.11190  0.00280  157 HIS A ND1   
1215 C  CD2   . HIS A 157 ? 0.62710 0.72700 0.69540 -0.10180 0.09650  -0.00400 157 HIS A CD2   
1216 C  CE1   . HIS A 157 ? 0.45050 0.55800 0.51120 -0.10370 0.10940  -0.00400 157 HIS A CE1   
1217 N  NE2   . HIS A 157 ? 0.52790 0.63720 0.59620 -0.09930 0.10000  -0.00770 157 HIS A NE2   
1218 N  N     . HIS A 158 ? 0.39980 0.44480 0.44500 -0.11580 0.10200  0.02560  158 HIS A N     
1219 C  CA    . HIS A 158 ? 0.44070 0.47240 0.48720 -0.12080 0.10620  0.03280  158 HIS A CA    
1220 C  C     . HIS A 158 ? 0.37560 0.39360 0.40160 -0.11870 0.10650  0.04460  158 HIS A C     
1221 O  O     . HIS A 158 ? 0.40370 0.41380 0.42550 -0.12330 0.11440  0.05290  158 HIS A O     
1222 C  CB    . HIS A 158 ? 0.48040 0.50840 0.54010 -0.12080 0.09970  0.02810  158 HIS A CB    
1223 C  CG    . HIS A 158 ? 0.54230 0.55700 0.60780 -0.12650 0.10460  0.03360  158 HIS A CG    
1224 N  ND1   . HIS A 158 ? 0.60960 0.62510 0.68800 -0.13470 0.11420  0.03340  158 HIS A ND1   
1225 C  CD2   . HIS A 158 ? 0.53090 0.53070 0.59230 -0.12500 0.10140  0.03950  158 HIS A CD2   
1226 C  CE1   . HIS A 158 ? 0.55200 0.55280 0.63380 -0.13820 0.11690  0.03910  158 HIS A CE1   
1227 N  NE2   . HIS A 158 ? 0.49650 0.48760 0.56830 -0.13220 0.10920  0.04280  158 HIS A NE2   
1228 N  N     . PHE A 159 ? 0.34340 0.35920 0.35690 -0.11150 0.09780  0.04550  159 PHE A N     
1229 C  CA    . PHE A 159 ? 0.40850 0.41210 0.40430 -0.10840 0.09550  0.05590  159 PHE A CA    
1230 C  C     . PHE A 159 ? 0.46360 0.46980 0.43930 -0.10570 0.09680  0.06040  159 PHE A C     
1231 O  O     . PHE A 159 ? 0.40890 0.40590 0.36940 -0.10400 0.09610  0.07010  159 PHE A O     
1232 C  CB    . PHE A 159 ? 0.37850 0.37710 0.37440 -0.10260 0.08480  0.05430  159 PHE A CB    
1233 C  CG    . PHE A 159 ? 0.37690 0.36830 0.38780 -0.10500 0.08370  0.05280  159 PHE A CG    
1234 C  CD1   . PHE A 159 ? 0.46940 0.44770 0.48140 -0.10870 0.08870  0.06130  159 PHE A CD1   
1235 C  CD2   . PHE A 159 ? 0.43150 0.42900 0.45510 -0.10330 0.07770  0.04300  159 PHE A CD2   
1236 C  CE1   . PHE A 159 ? 0.53510 0.50620 0.56180 -0.11110 0.08800  0.05890  159 PHE A CE1   
1237 C  CE2   . PHE A 159 ? 0.45560 0.44720 0.49270 -0.10570 0.07670  0.04040  159 PHE A CE2   
1238 C  CZ    . PHE A 159 ? 0.49710 0.47520 0.53630 -0.10970 0.08200  0.04790  159 PHE A CZ    
1239 N  N     . TYR A 160 ? 0.38300 0.40190 0.35880 -0.10490 0.09820  0.05310  160 TYR A N     
1240 C  CA    . TYR A 160 ? 0.41790 0.44110 0.37580 -0.10170 0.09830  0.05410  160 TYR A CA    
1241 C  C     . TYR A 160 ? 0.46240 0.49550 0.42040 -0.10570 0.10820  0.05120  160 TYR A C     
1242 O  O     . TYR A 160 ? 0.41770 0.45670 0.36370 -0.10300 0.10850  0.04890  160 TYR A O     
1243 C  CB    . TYR A 160 ? 0.36150 0.38980 0.31850 -0.09510 0.08880  0.04700  160 TYR A CB    
1244 C  CG    . TYR A 160 ? 0.34140 0.36110 0.29660 -0.09080 0.07940  0.04970  160 TYR A CG    
1245 C  CD1   . TYR A 160 ? 0.35130 0.36950 0.32160 -0.09030 0.07500  0.04570  160 TYR A CD1   
1246 C  CD2   . TYR A 160 ? 0.36060 0.37460 0.29910 -0.08710 0.07490  0.05580  160 TYR A CD2   
1247 C  CE1   . TYR A 160 ? 0.33400 0.34470 0.30300 -0.08630 0.06700  0.04770  160 TYR A CE1   
1248 C  CE2   . TYR A 160 ? 0.36050 0.36740 0.29860 -0.08290 0.06650  0.05800  160 TYR A CE2   
1249 C  CZ    . TYR A 160 ? 0.36870 0.37370 0.32220 -0.08260 0.06290  0.05400  160 TYR A CZ    
1250 O  OH    . TYR A 160 ? 0.37000 0.36850 0.32350 -0.07860 0.05530  0.05560  160 TYR A OH    
1251 N  N     . SER A 161 ? 0.35760 0.39250 0.32880 -0.11200 0.11650  0.05090  161 SER A N     
1252 C  CA    . SER A 161 ? 0.46430 0.50950 0.43820 -0.11620 0.12680  0.04760  161 SER A CA    
1253 C  C     . SER A 161 ? 0.55520 0.59920 0.50740 -0.11700 0.13340  0.05450  161 SER A C     
1254 O  O     . SER A 161 ? 0.49860 0.55290 0.44780 -0.11720 0.13850  0.04930  161 SER A O     
1255 C  CB    . SER A 161 ? 0.44680 0.49280 0.43890 -0.12370 0.13500  0.04750  161 SER A CB    
1256 O  OG    . SER A 161 ? 0.73510 0.79080 0.74850 -0.12340 0.13150  0.03690  161 SER A OG    
1257 N  N     . LYS A 162 ? 0.53360 0.56530 0.47120 -0.11740 0.13330  0.06620  162 LYS A N     
1258 C  CA    . LYS A 162 ? 0.62080 0.65090 0.53690 -0.11870 0.13990  0.07440  162 LYS A CA    
1259 C  C     . LYS A 162 ? 0.52090 0.55580 0.41760 -0.11300 0.13450  0.07190  162 LYS A C     
1260 O  O     . LYS A 162 ? 0.45970 0.49900 0.34070 -0.11440 0.14110  0.07410  162 LYS A O     
1261 C  CB    . LYS A 162 ? 0.84410 0.85930 0.75110 -0.12040 0.14120  0.08880  162 LYS A CB    
1262 C  CG    . LYS A 162 ? 0.76080 0.77210 0.68020 -0.12700 0.15150  0.09380  162 LYS A CG    
1263 C  CD    . LYS A 162 ? 0.85960 0.85790 0.76670 -0.12630 0.15310  0.10930  162 LYS A CD    
1264 C  CE    . LYS A 162 ? 0.97730 0.97590 0.89330 -0.13090 0.16340  0.11460  162 LYS A CE    
1265 N  NZ    . LYS A 162 ? 0.87690 0.86480 0.77840 -0.12960 0.16520  0.13080  162 LYS A NZ    
1266 N  N     . HIS A 163 ? 0.49030 0.52470 0.38850 -0.10700 0.12300  0.06720  163 HIS A N     
1267 C  CA    . HIS A 163 ? 0.56790 0.60570 0.44940 -0.10170 0.11680  0.06460  163 HIS A CA    
1268 C  C     . HIS A 163 ? 0.59440 0.64330 0.48410 -0.09880 0.11450  0.05130  163 HIS A C     
1269 O  O     . HIS A 163 ? 0.67250 0.72640 0.54920 -0.09610 0.11290  0.04740  163 HIS A O     
1270 C  CB    . HIS A 163 ? 0.60300 0.63130 0.47770 -0.09700 0.10580  0.07050  163 HIS A CB    
1271 C  CG    . HIS A 163 ? 0.68230 0.70010 0.54380 -0.09830 0.10750  0.08450  163 HIS A CG    
1272 N  ND1   . HIS A 163 ? 0.72990 0.74770 0.56800 -0.09690 0.10760  0.09130  163 HIS A ND1   
1273 C  CD2   . HIS A 163 ? 0.70290 0.70990 0.57150 -0.10090 0.10960  0.09330  163 HIS A CD2   
1274 C  CE1   . HIS A 163 ? 0.71590 0.72330 0.54690 -0.09800 0.10950  0.10460  163 HIS A CE1   
1275 N  NE2   . HIS A 163 ? 0.72790 0.72780 0.57770 -0.10050 0.11090  0.10600  163 HIS A NE2   
1276 N  N     . LEU A 164 ? 0.57890 0.63180 0.49020 -0.09930 0.11410  0.04420  164 LEU A N     
1277 C  CA    . LEU A 164 ? 0.44590 0.50820 0.36740 -0.09580 0.11120  0.03270  164 LEU A CA    
1278 C  C     . LEU A 164 ? 0.42860 0.50180 0.36310 -0.09910 0.12060  0.02590  164 LEU A C     
1279 O  O     . LEU A 164 ? 0.46540 0.53900 0.41040 -0.10410 0.12690  0.02830  164 LEU A O     
1280 C  CB    . LEU A 164 ? 0.54150 0.60110 0.47740 -0.09230 0.10180  0.02970  164 LEU A CB    
1281 C  CG    . LEU A 164 ? 0.46800 0.52010 0.39430 -0.08740 0.09130  0.03250  164 LEU A CG    
1282 C  CD1   . LEU A 164 ? 0.54780 0.59730 0.48940 -0.08510 0.08410  0.03030  164 LEU A CD1   
1283 C  CD2   . LEU A 164 ? 0.49030 0.54710 0.40700 -0.08320 0.08810  0.02670  164 LEU A CD2   
1284 N  N     . GLU A 165 ? 0.58830 0.67040 0.52350 -0.09610 0.12140  0.01700  165 GLU A N     
1285 C  CA    . GLU A 165 ? 0.82830 0.92190 0.78020 -0.09730 0.12800  0.00860  165 GLU A CA    
1286 C  C     . GLU A 165 ? 0.52390 0.62140 0.49250 -0.09200 0.12000  0.00120  165 GLU A C     
1287 O  O     . GLU A 165 ? 0.62230 0.71860 0.58560 -0.08680 0.11360  -0.00220 165 GLU A O     
1288 C  CB    . GLU A 165 ? 0.86230 0.96350 0.80440 -0.09770 0.13610  0.00390  165 GLU A CB    
1289 C  CG    . GLU A 165 ? 1.10280 1.20290 1.02980 -0.09290 0.13090  0.00020  165 GLU A CG    
1290 C  CD    . GLU A 165 ? 1.16570 1.27560 1.09130 -0.09240 0.13860  -0.00890 165 GLU A CD    
1291 O  OE1   . GLU A 165 ? 1.10040 1.21560 1.02280 -0.09700 0.14940  -0.00830 165 GLU A OE1   
1292 O  OE2   . GLU A 165 ? 0.95870 1.07100 0.88700 -0.08750 0.13420  -0.01680 165 GLU A OE2   
1293 N  N     . PHE A 166 ? 0.47710 0.57950 0.46580 -0.09350 0.12060  -0.00110 166 PHE A N     
1294 C  CA    . PHE A 166 ? 0.50990 0.61540 0.51380 -0.08880 0.11240  -0.00620 166 PHE A CA    
1295 C  C     . PHE A 166 ? 0.44380 0.56120 0.46010 -0.08520 0.11470  -0.01530 166 PHE A C     
1296 O  O     . PHE A 166 ? 0.50530 0.63130 0.52830 -0.08820 0.12370  -0.01860 166 PHE A O     
1297 C  CB    . PHE A 166 ? 0.44190 0.54780 0.46130 -0.09210 0.11100  -0.00470 166 PHE A CB    
1298 C  CG    . PHE A 166 ? 0.45100 0.54450 0.46110 -0.09520 0.10870  0.00390  166 PHE A CG    
1299 C  CD1   . PHE A 166 ? 0.42900 0.51320 0.42930 -0.09110 0.09970  0.00710  166 PHE A CD1   
1300 C  CD2   . PHE A 166 ? 0.51680 0.60760 0.52920 -0.10200 0.11600  0.00880  166 PHE A CD2   
1301 C  CE1   . PHE A 166 ? 0.52870 0.60140 0.52160 -0.09320 0.09750  0.01500  166 PHE A CE1   
1302 C  CE2   . PHE A 166 ? 0.58500 0.66330 0.58990 -0.10440 0.11410  0.01710  166 PHE A CE2   
1303 C  CZ    . PHE A 166 ? 0.49410 0.56340 0.48950 -0.09970 0.10460  0.02010  166 PHE A CZ    
1304 N  N     . PRO A 167 ? 0.45160 0.56960 0.47200 -0.07870 0.10720  -0.01940 167 PRO A N     
1305 C  CA    . PRO A 167 ? 0.44400 0.57310 0.48110 -0.07470 0.10820  -0.02720 167 PRO A CA    
1306 C  C     . PRO A 167 ? 0.43510 0.57260 0.49260 -0.07610 0.10750  -0.02860 167 PRO A C     
1307 O  O     . PRO A 167 ? 0.39080 0.52460 0.44870 -0.08060 0.10660  -0.02420 167 PRO A O     
1308 C  CB    . PRO A 167 ? 0.42960 0.55430 0.46450 -0.06770 0.09940  -0.02880 167 PRO A CB    
1309 C  CG    . PRO A 167 ? 0.43770 0.55100 0.46110 -0.06840 0.09220  -0.02210 167 PRO A CG    
1310 C  CD    . PRO A 167 ? 0.51360 0.62190 0.52340 -0.07470 0.09790  -0.01660 167 PRO A CD    
1311 N  N     . ASP A 168 ? 0.40830 0.55730 0.48280 -0.07220 0.10790  -0.03490 168 ASP A N     
1312 C  CA    . ASP A 168 ? 0.43850 0.59790 0.53350 -0.07280 0.10610  -0.03730 168 ASP A CA    
1313 C  C     . ASP A 168 ? 0.37500 0.52950 0.47090 -0.07040 0.09520  -0.03450 168 ASP A C     
1314 O  O     . ASP A 168 ? 0.32300 0.46710 0.40590 -0.06720 0.08940  -0.03130 168 ASP A O     
1315 C  CB    . ASP A 168 ? 0.40150 0.57470 0.51420 -0.06790 0.10810  -0.04430 168 ASP A CB    
1316 C  CG    . ASP A 168 ? 0.55710 0.72790 0.66860 -0.05920 0.10170  -0.04600 168 ASP A CG    
1317 O  OD1   . ASP A 168 ? 1.13600 1.29470 1.23190 -0.05760 0.09720  -0.04260 168 ASP A OD1   
1318 O  OD2   . ASP A 168 ? 0.74900 0.93020 0.87650 -0.05400 0.10140  -0.05060 168 ASP A OD2   
1319 N  N     . ASN A 169 ? 0.35280 0.51550 0.46450 -0.07210 0.09280  -0.03630 169 ASN A N     
1320 C  CA    . ASN A 169 ? 0.33000 0.48900 0.44240 -0.07090 0.08340  -0.03430 169 ASN A CA    
1321 C  C     . ASN A 169 ? 0.32540 0.48330 0.43610 -0.06240 0.07490  -0.03460 169 ASN A C     
1322 O  O     . ASN A 169 ? 0.28730 0.43570 0.38820 -0.06090 0.06840  -0.03100 169 ASN A O     
1323 C  CB    . ASN A 169 ? 0.33780 0.50800 0.46850 -0.07450 0.08260  -0.03780 169 ASN A CB    
1324 C  CG    . ASN A 169 ? 0.31410 0.47870 0.44310 -0.07530 0.07470  -0.03590 169 ASN A CG    
1325 O  OD1   . ASN A 169 ? 0.31770 0.47190 0.43890 -0.08090 0.07640  -0.03210 169 ASN A OD1   
1326 N  ND2   . ASN A 169 ? 0.33320 0.50450 0.46930 -0.06970 0.06620  -0.03840 169 ASN A ND2   
1327 N  N     . ASP A 170 ? 0.27710 0.44450 0.39780 -0.05680 0.07550  -0.03860 170 ASP A N     
1328 C  CA    . ASP A 170 ? 0.36470 0.53110 0.48510 -0.04840 0.06880  -0.03850 170 ASP A CA    
1329 C  C     . ASP A 170 ? 0.37170 0.52340 0.47380 -0.04670 0.06730  -0.03480 170 ASP A C     
1330 O  O     . ASP A 170 ? 0.32910 0.47530 0.42670 -0.04250 0.06020  -0.03240 170 ASP A O     
1331 C  CB    . ASP A 170 ? 0.42520 0.60260 0.55930 -0.04290 0.07170  -0.04300 170 ASP A CB    
1332 C  CG    . ASP A 170 ? 0.57320 0.76670 0.72730 -0.04080 0.06840  -0.04610 170 ASP A CG    
1333 O  OD1   . ASP A 170 ? 0.58770 0.78450 0.74530 -0.04450 0.06440  -0.04570 170 ASP A OD1   
1334 O  OD2   . ASP A 170 ? 0.63470 0.83790 0.80170 -0.03530 0.06970  -0.04930 170 ASP A OD2   
1335 N  N     . SER A 171 ? 0.32210 0.46820 0.41360 -0.05010 0.07420  -0.03480 171 SER A N     
1336 C  CA    . SER A 171 ? 0.36140 0.49520 0.43580 -0.04900 0.07320  -0.03230 171 SER A CA    
1337 C  C     . SER A 171 ? 0.30560 0.42890 0.36820 -0.05170 0.06800  -0.02680 171 SER A C     
1338 O  O     . SER A 171 ? 0.27910 0.39410 0.33270 -0.04860 0.06290  -0.02470 171 SER A O     
1339 C  CB    . SER A 171 ? 0.36180 0.49400 0.42730 -0.05240 0.08190  -0.03410 171 SER A CB    
1340 O  OG    . SER A 171 ? 0.49880 0.63870 0.57370 -0.04870 0.08650  -0.03980 171 SER A OG    
1341 N  N     . LEU A 172 ? 0.25480 0.37840 0.31840 -0.05760 0.06970  -0.02470 172 LEU A N     
1342 C  CA    . LEU A 172 ? 0.30910 0.42300 0.36390 -0.06020 0.06520  -0.01970 172 LEU A CA    
1343 C  C     . LEU A 172 ? 0.26980 0.38410 0.33010 -0.05620 0.05650  -0.01960 172 LEU A C     
1344 O  O     . LEU A 172 ? 0.31740 0.42250 0.36830 -0.05510 0.05160  -0.01620 172 LEU A O     
1345 C  CB    . LEU A 172 ? 0.31630 0.43010 0.37310 -0.06760 0.07000  -0.01770 172 LEU A CB    
1346 C  CG    . LEU A 172 ? 0.35320 0.46200 0.39770 -0.07220 0.07780  -0.01470 172 LEU A CG    
1347 C  CD1   . LEU A 172 ? 0.46930 0.57840 0.51860 -0.07940 0.08340  -0.01250 172 LEU A CD1   
1348 C  CD2   . LEU A 172 ? 0.42320 0.51980 0.44900 -0.07100 0.07490  -0.00970 172 LEU A CD2   
1349 N  N     . VAL A 173 ? 0.24310 0.36890 0.31860 -0.05400 0.05480  -0.02340 173 VAL A N     
1350 C  CA    . VAL A 173 ? 0.23720 0.36540 0.31760 -0.04970 0.04670  -0.02360 173 VAL A CA    
1351 C  C     . VAL A 173 ? 0.25310 0.37480 0.32540 -0.04340 0.04280  -0.02170 173 VAL A C     
1352 O  O     . VAL A 173 ? 0.27450 0.38980 0.34070 -0.04180 0.03730  -0.01900 173 VAL A O     
1353 C  CB    . VAL A 173 ? 0.26370 0.40730 0.36160 -0.04740 0.04540  -0.02800 173 VAL A CB    
1354 C  CG1   . VAL A 173 ? 0.26550 0.41220 0.36610 -0.04180 0.03690  -0.02760 173 VAL A CG1   
1355 C  CG2   . VAL A 173 ? 0.25560 0.40600 0.36310 -0.05420 0.04850  -0.03050 173 VAL A CG2   
1356 N  N     . VAL A 174 ? 0.24520 0.36840 0.31830 -0.04030 0.04640  -0.02340 174 VAL A N     
1357 C  CA    . VAL A 174 ? 0.26680 0.38380 0.33420 -0.03480 0.04400  -0.02240 174 VAL A CA    
1358 C  C     . VAL A 174 ? 0.24470 0.34890 0.29640 -0.03690 0.04260  -0.01910 174 VAL A C     
1359 O  O     . VAL A 174 ? 0.22590 0.32440 0.27340 -0.03380 0.03760  -0.01680 174 VAL A O     
1360 C  CB    . VAL A 174 ? 0.33210 0.45250 0.40410 -0.03190 0.04930  -0.02600 174 VAL A CB    
1361 C  CG1   . VAL A 174 ? 0.35370 0.46540 0.41880 -0.02780 0.04810  -0.02550 174 VAL A CG1   
1362 C  CG2   . VAL A 174 ? 0.34070 0.47380 0.42980 -0.02760 0.04900  -0.02850 174 VAL A CG2   
1363 N  N     . LEU A 175 ? 0.27160 0.37200 0.31500 -0.04220 0.04730  -0.01850 175 LEU A N     
1364 C  CA    . LEU A 175 ? 0.29520 0.38490 0.32380 -0.04420 0.04600  -0.01520 175 LEU A CA    
1365 C  C     . LEU A 175 ? 0.27010 0.35420 0.29580 -0.04470 0.04010  -0.01140 175 LEU A C     
1366 O  O     . LEU A 175 ? 0.26270 0.33990 0.28130 -0.04260 0.03600  -0.00940 175 LEU A O     
1367 C  CB    . LEU A 175 ? 0.31490 0.40300 0.33530 -0.04970 0.05220  -0.01430 175 LEU A CB    
1368 C  CG    . LEU A 175 ? 0.30140 0.37990 0.30580 -0.05130 0.05100  -0.01070 175 LEU A CG    
1369 C  CD1   . LEU A 175 ? 0.36220 0.43780 0.36160 -0.04740 0.04910  -0.01320 175 LEU A CD1   
1370 C  CD2   . LEU A 175 ? 0.33300 0.41100 0.32890 -0.05650 0.05750  -0.00910 175 LEU A CD2   
1371 N  N     . PHE A 176 ? 0.28590 0.37340 0.31790 -0.04780 0.03990  -0.01090 176 PHE A N     
1372 C  CA    . PHE A 176 ? 0.27870 0.36190 0.31000 -0.04840 0.03480  -0.00860 176 PHE A CA    
1373 C  C     . PHE A 176 ? 0.27270 0.35720 0.30690 -0.04280 0.02880  -0.00910 176 PHE A C     
1374 O  O     . PHE A 176 ? 0.31890 0.39680 0.34740 -0.04170 0.02470  -0.00680 176 PHE A O     
1375 C  CB    . PHE A 176 ? 0.27830 0.36630 0.31840 -0.05280 0.03620  -0.00970 176 PHE A CB    
1376 C  CG    . PHE A 176 ? 0.27740 0.35870 0.31190 -0.05880 0.04040  -0.00650 176 PHE A CG    
1377 C  CD1   . PHE A 176 ? 0.30840 0.37910 0.33440 -0.05980 0.03770  -0.00230 176 PHE A CD1   
1378 C  CD2   . PHE A 176 ? 0.29920 0.38470 0.33740 -0.06330 0.04730  -0.00730 176 PHE A CD2   
1379 C  CE1   . PHE A 176 ? 0.34440 0.40830 0.36540 -0.06460 0.04150  0.00180  176 PHE A CE1   
1380 C  CE2   . PHE A 176 ? 0.33690 0.41560 0.36940 -0.06870 0.05170  -0.00320 176 PHE A CE2   
1381 C  CZ    . PHE A 176 ? 0.30610 0.37360 0.32980 -0.06920 0.04860  0.00170  176 PHE A CZ    
1382 N  N     . ALA A 177 ? 0.28880 0.38210 0.33220 -0.03910 0.02860  -0.01190 177 ALA A N     
1383 C  CA    . ALA A 177 ? 0.25010 0.34530 0.29620 -0.03320 0.02370  -0.01150 177 ALA A CA    
1384 C  C     . ALA A 177 ? 0.33010 0.41650 0.36780 -0.03030 0.02300  -0.00950 177 ALA A C     
1385 O  O     . ALA A 177 ? 0.25860 0.34140 0.29360 -0.02760 0.01880  -0.00750 177 ALA A O     
1386 C  CB    . ALA A 177 ? 0.26560 0.37200 0.32350 -0.02940 0.02410  -0.01410 177 ALA A CB    
1387 N  N     . GLN A 178 ? 0.21370 0.29750 0.24780 -0.03120 0.02730  -0.01070 178 GLN A N     
1388 C  CA    . GLN A 178 ? 0.22880 0.30490 0.25560 -0.02940 0.02700  -0.01010 178 GLN A CA    
1389 C  C     . GLN A 178 ? 0.25420 0.32210 0.27100 -0.03170 0.02410  -0.00710 178 GLN A C     
1390 O  O     . GLN A 178 ? 0.27210 0.33500 0.28590 -0.02930 0.02110  -0.00590 178 GLN A O     
1391 C  CB    . GLN A 178 ? 0.31070 0.38690 0.33520 -0.03060 0.03250  -0.01310 178 GLN A CB    
1392 C  CG    . GLN A 178 ? 0.22770 0.31040 0.26280 -0.02670 0.03550  -0.01640 178 GLN A CG    
1393 C  CD    . GLN A 178 ? 0.30060 0.38460 0.33400 -0.02870 0.04190  -0.02050 178 GLN A CD    
1394 O  OE1   . GLN A 178 ? 0.29250 0.37690 0.31980 -0.03360 0.04500  -0.02060 178 GLN A OE1   
1395 N  NE2   . GLN A 178 ? 0.30120 0.38550 0.33990 -0.02490 0.04440  -0.02390 178 GLN A NE2   
1396 N  N     . VAL A 179 ? 0.24010 0.30660 0.25280 -0.03640 0.02520  -0.00580 179 VAL A N     
1397 C  CA    . VAL A 179 ? 0.26140 0.32040 0.26590 -0.03840 0.02240  -0.00240 179 VAL A CA    
1398 C  C     . VAL A 179 ? 0.25770 0.31540 0.26510 -0.03630 0.01750  -0.00110 179 VAL A C     
1399 O  O     . VAL A 179 ? 0.28160 0.33360 0.28420 -0.03510 0.01450  0.00060  179 VAL A O     
1400 C  CB    . VAL A 179 ? 0.25840 0.31580 0.25930 -0.04350 0.02520  -0.00050 179 VAL A CB    
1401 C  CG1   . VAL A 179 ? 0.30090 0.35060 0.29560 -0.04470 0.02200  0.00350  179 VAL A CG1   
1402 C  CG2   . VAL A 179 ? 0.24340 0.30130 0.23800 -0.04560 0.03020  -0.00120 179 VAL A CG2   
1403 N  N     . ASN A 180 ? 0.35790 0.42180 0.37330 -0.03600 0.01670  -0.00240 180 ASN A N     
1404 C  CA    . ASN A 180 ? 0.38620 0.45060 0.40410 -0.03400 0.01240  -0.00200 180 ASN A CA    
1405 C  C     . ASN A 180 ? 0.32780 0.39100 0.34490 -0.02910 0.01000  -0.00120 180 ASN A C     
1406 O  O     . ASN A 180 ? 0.34550 0.40560 0.36040 -0.02780 0.00690  0.00010  180 ASN A O     
1407 C  CB    . ASN A 180 ? 0.30160 0.37520 0.32850 -0.03430 0.01180  -0.00460 180 ASN A CB    
1408 C  CG    . ASN A 180 ? 0.36790 0.44170 0.39730 -0.03980 0.01390  -0.00560 180 ASN A CG    
1409 O  OD1   . ASN A 180 ? 0.49100 0.55700 0.51460 -0.04310 0.01540  -0.00330 180 ASN A OD1   
1410 N  ND2   . ASN A 180 ? 0.50070 0.58370 0.53920 -0.04090 0.01400  -0.00880 180 ASN A ND2   
1411 N  N     . CYS A 181 ? 0.30810 0.37380 0.32770 -0.02650 0.01190  -0.00210 181 CYS A N     
1412 C  CA    . CYS A 181 ? 0.33980 0.40410 0.36030 -0.02180 0.01080  -0.00100 181 CYS A CA    
1413 C  C     . CYS A 181 ? 0.37790 0.43400 0.39230 -0.02210 0.01100  -0.00030 181 CYS A C     
1414 O  O     . CYS A 181 ? 0.39170 0.44470 0.40570 -0.01950 0.00930  0.00120  181 CYS A O     
1415 C  CB    . CYS A 181 ? 0.35880 0.42880 0.38640 -0.01860 0.01310  -0.00240 181 CYS A CB    
1416 S  SG    . CYS A 181 ? 0.55240 0.62000 0.58310 -0.01240 0.01260  -0.00030 181 CYS A SG    
1417 N  N     . ASN A 182 ? 0.26290 0.31630 0.27250 -0.02530 0.01330  -0.00160 182 ASN A N     
1418 C  CA    . ASN A 182 ? 0.29360 0.34130 0.29790 -0.02570 0.01360  -0.00230 182 ASN A CA    
1419 C  C     . ASN A 182 ? 0.30310 0.34620 0.29920 -0.02890 0.01180  -0.00080 182 ASN A C     
1420 O  O     . ASN A 182 ? 0.34600 0.38560 0.33810 -0.02900 0.01090  -0.00150 182 ASN A O     
1421 C  CB    . ASN A 182 ? 0.38870 0.43810 0.39390 -0.02580 0.01780  -0.00580 182 ASN A CB    
1422 C  CG    . ASN A 182 ? 0.39750 0.45010 0.41170 -0.02160 0.01940  -0.00690 182 ASN A CG    
1423 O  OD1   . ASN A 182 ? 0.46810 0.51730 0.48500 -0.01880 0.01900  -0.00670 182 ASN A OD1   
1424 N  ND2   . ASN A 182 ? 0.42320 0.48240 0.44320 -0.02110 0.02150  -0.00780 182 ASN A ND2   
1425 N  N     . GLY A 183 ? 0.33490 0.37830 0.32930 -0.03130 0.01120  0.00110  183 GLY A N     
1426 C  CA    . GLY A 183 ? 0.43870 0.47750 0.42590 -0.03390 0.00960  0.00350  183 GLY A CA    
1427 C  C     . GLY A 183 ? 0.32060 0.35540 0.30760 -0.03230 0.00550  0.00520  183 GLY A C     
1428 O  O     . GLY A 183 ? 0.36190 0.39780 0.35400 -0.03000 0.00410  0.00510  183 GLY A O     
1429 N  N     . PHE A 184 ? 0.31020 0.34120 0.29100 -0.03330 0.00350  0.00700  184 PHE A N     
1430 C  CA    . PHE A 184 ? 0.30570 0.33330 0.28680 -0.03190 -0.00030 0.00840  184 PHE A CA    
1431 C  C     . PHE A 184 ? 0.33250 0.35650 0.31090 -0.03320 -0.00200 0.01210  184 PHE A C     
1432 O  O     . PHE A 184 ? 0.32200 0.34500 0.29530 -0.03550 -0.00060 0.01410  184 PHE A O     
1433 C  CB    . PHE A 184 ? 0.39090 0.41800 0.36890 -0.03140 -0.00190 0.00700  184 PHE A CB    
1434 C  CG    . PHE A 184 ? 0.33110 0.35980 0.31380 -0.02960 -0.00040 0.00360  184 PHE A CG    
1435 C  CD1   . PHE A 184 ? 0.38840 0.41940 0.37130 -0.03000 0.00310  0.00070  184 PHE A CD1   
1436 C  CD2   . PHE A 184 ? 0.38750 0.41510 0.37520 -0.02770 -0.00200 0.00330  184 PHE A CD2   
1437 C  CE1   . PHE A 184 ? 0.44240 0.47380 0.43090 -0.02810 0.00480  -0.00200 184 PHE A CE1   
1438 C  CE2   . PHE A 184 ? 0.39180 0.41980 0.38440 -0.02610 -0.00000 0.00100  184 PHE A CE2   
1439 C  CZ    . PHE A 184 ? 0.54090 0.57040 0.53410 -0.02620 0.00330  -0.00150 184 PHE A CZ    
1440 N  N     . THR A 185 ? 0.33820 0.36000 0.32030 -0.03170 -0.00460 0.01300  185 THR A N     
1441 C  CA    . THR A 185 ? 0.41850 0.43590 0.39940 -0.03210 -0.00660 0.01640  185 THR A CA    
1442 C  C     . THR A 185 ? 0.32540 0.34170 0.30390 -0.03050 -0.01020 0.01740  185 THR A C     
1443 O  O     . THR A 185 ? 0.39290 0.41120 0.37450 -0.02880 -0.01130 0.01490  185 THR A O     
1444 C  CB    . THR A 185 ? 0.36160 0.37770 0.34910 -0.03120 -0.00710 0.01570  185 THR A CB    
1445 O  OG1   . THR A 185 ? 0.61670 0.63540 0.60800 -0.02870 -0.00810 0.01330  185 THR A OG1   
1446 C  CG2   . THR A 185 ? 0.47330 0.49140 0.46390 -0.03320 -0.00430 0.01420  185 THR A CG2   
1447 N  N     . ILE A 186 ? 0.37950 0.39310 0.35260 -0.03110 -0.01190 0.02120  186 ILE A N     
1448 C  CA    . ILE A 186 ? 0.34440 0.35790 0.31560 -0.02930 -0.01620 0.02260  186 ILE A CA    
1449 C  C     . ILE A 186 ? 0.42190 0.43140 0.39840 -0.02740 -0.01850 0.02540  186 ILE A C     
1450 O  O     . ILE A 186 ? 0.31990 0.32490 0.29660 -0.02820 -0.01710 0.02860  186 ILE A O     
1451 C  CB    . ILE A 186 ? 0.40520 0.41930 0.36630 -0.03040 -0.01730 0.02540  186 ILE A CB    
1452 C  CG1   . ILE A 186 ? 0.41090 0.42940 0.36780 -0.03220 -0.01460 0.02110  186 ILE A CG1   
1453 C  CG2   . ILE A 186 ? 0.48480 0.50020 0.44450 -0.02820 -0.02280 0.02700  186 ILE A CG2   
1454 C  CD1   . ILE A 186 ? 0.39000 0.40980 0.33540 -0.03380 -0.01440 0.02310  186 ILE A CD1   
1455 N  N     . GLU A 187 ? 0.42110 0.43220 0.40310 -0.02510 -0.02140 0.02380  187 GLU A N     
1456 C  CA    . GLU A 187 ? 0.37570 0.38380 0.36380 -0.02270 -0.02350 0.02560  187 GLU A CA    
1457 C  C     . GLU A 187 ? 0.34800 0.35810 0.33620 -0.02040 -0.02850 0.02730  187 GLU A C     
1458 O  O     . GLU A 187 ? 0.33030 0.34530 0.31630 -0.02070 -0.03020 0.02500  187 GLU A O     
1459 C  CB    . GLU A 187 ? 0.41010 0.41930 0.40640 -0.02170 -0.02190 0.02160  187 GLU A CB    
1460 C  CG    . GLU A 187 ? 0.51440 0.52300 0.51170 -0.02340 -0.01790 0.01960  187 GLU A CG    
1461 C  CD    . GLU A 187 ? 0.79070 0.80340 0.78550 -0.02460 -0.01560 0.01680  187 GLU A CD    
1462 O  OE1   . GLU A 187 ? 0.78510 0.80080 0.77950 -0.02400 -0.01650 0.01540  187 GLU A OE1   
1463 O  OE2   . GLU A 187 ? 0.86080 0.87410 0.85520 -0.02610 -0.01290 0.01580  187 GLU A OE2   
1464 N  N     . ASP A 188 ? 0.38080 0.38740 0.37270 -0.01810 -0.03090 0.03110  188 ASP A N     
1465 C  CA    . ASP A 188 ? 0.38590 0.39510 0.38010 -0.01510 -0.03630 0.03300  188 ASP A CA    
1466 C  C     . ASP A 188 ? 0.41190 0.42490 0.41680 -0.01330 -0.03690 0.02830  188 ASP A C     
1467 O  O     . ASP A 188 ? 0.37630 0.38960 0.38490 -0.01450 -0.03300 0.02430  188 ASP A O     
1468 C  CB    . ASP A 188 ? 0.35030 0.35380 0.34440 -0.01270 -0.03850 0.03980  188 ASP A CB    
1469 C  CG    . ASP A 188 ? 0.46140 0.45910 0.46550 -0.01110 -0.03630 0.03960  188 ASP A CG    
1470 O  OD1   . ASP A 188 ? 0.42850 0.42790 0.43940 -0.01140 -0.03370 0.03400  188 ASP A OD1   
1471 O  OD2   . ASP A 188 ? 0.49370 0.48500 0.49860 -0.00940 -0.03690 0.04510  188 ASP A OD2   
1472 N  N     . GLU A 189 ? 0.34520 0.36180 0.35500 -0.01050 -0.04170 0.02920  189 GLU A N     
1473 C  CA    . GLU A 189 ? 0.39130 0.41260 0.41190 -0.00900 -0.04210 0.02480  189 GLU A CA    
1474 C  C     . GLU A 189 ? 0.31440 0.33220 0.34380 -0.00770 -0.03840 0.02320  189 GLU A C     
1475 O  O     . GLU A 189 ? 0.39060 0.41210 0.42750 -0.00750 -0.03670 0.01900  189 GLU A O     
1476 C  CB    . GLU A 189 ? 0.34320 0.37020 0.36830 -0.00610 -0.04860 0.02620  189 GLU A CB    
1477 C  CG    . GLU A 189 ? 0.49220 0.51560 0.52220 -0.00180 -0.05150 0.03150  189 GLU A CG    
1478 C  CD    . GLU A 189 ? 0.50170 0.51970 0.52160 -0.00120 -0.05340 0.03870  189 GLU A CD    
1479 O  OE1   . GLU A 189 ? 0.51980 0.53570 0.52880 -0.00460 -0.05100 0.03950  189 GLU A OE1   
1480 O  OE2   . GLU A 189 ? 0.50510 0.52090 0.52850 0.00280  -0.05690 0.04410  189 GLU A OE2   
1481 N  N     . GLU A 190 ? 0.39260 0.40340 0.42110 -0.00720 -0.03690 0.02630  190 GLU A N     
1482 C  CA    . GLU A 190 ? 0.37940 0.38660 0.41500 -0.00640 -0.03310 0.02380  190 GLU A CA    
1483 C  C     . GLU A 190 ? 0.37700 0.38210 0.40780 -0.00970 -0.02820 0.02110  190 GLU A C     
1484 O  O     . GLU A 190 ? 0.41740 0.41950 0.45210 -0.00970 -0.02520 0.01880  190 GLU A O     
1485 C  CB    . GLU A 190 ? 0.44960 0.45020 0.48970 -0.00360 -0.03440 0.02780  190 GLU A CB    
1486 C  CG    . GLU A 190 ? 0.52170 0.52500 0.57050 0.00080  -0.03880 0.02950  190 GLU A CG    
1487 C  CD    . GLU A 190 ? 0.52190 0.51760 0.57650 0.00420  -0.03960 0.03390  190 GLU A CD    
1488 O  OE1   . GLU A 190 ? 0.57040 0.55850 0.62460 0.00280  -0.03570 0.03380  190 GLU A OE1   
1489 O  OE2   . GLU A 190 ? 0.53430 0.53170 0.59450 0.00840  -0.04430 0.03730  190 GLU A OE2   
1490 N  N     . LEU A 191 ? 0.42140 0.42900 0.44430 -0.01240 -0.02760 0.02090  191 LEU A N     
1491 C  CA    . LEU A 191 ? 0.43140 0.43820 0.44950 -0.01520 -0.02370 0.01900  191 LEU A CA    
1492 C  C     . LEU A 191 ? 0.40910 0.40980 0.42540 -0.01660 -0.02210 0.02100  191 LEU A C     
1493 O  O     . LEU A 191 ? 0.45920 0.45970 0.47570 -0.01830 -0.01890 0.01820  191 LEU A O     
1494 C  CB    . LEU A 191 ? 0.36990 0.38000 0.39190 -0.01520 -0.02060 0.01430  191 LEU A CB    
1495 C  CG    . LEU A 191 ? 0.51160 0.52710 0.53440 -0.01510 -0.02030 0.01240  191 LEU A CG    
1496 C  CD1   . LEU A 191 ? 0.54290 0.56060 0.56620 -0.01550 -0.01630 0.00940  191 LEU A CD1   
1497 C  CD2   . LEU A 191 ? 0.49140 0.50840 0.50810 -0.01680 -0.02150 0.01340  191 LEU A CD2   
1498 N  N     . SER A 192 ? 0.42790 0.42400 0.44270 -0.01580 -0.02430 0.02610  192 SER A N     
1499 C  CA    . SER A 192 ? 0.52650 0.51610 0.53930 -0.01760 -0.02230 0.02910  192 SER A CA    
1500 C  C     . SER A 192 ? 0.43060 0.42160 0.43390 -0.02080 -0.02110 0.03080  192 SER A C     
1501 O  O     . SER A 192 ? 0.36970 0.36470 0.36710 -0.02060 -0.02330 0.03210  192 SER A O     
1502 C  CB    . SER A 192 ? 0.49070 0.47400 0.50580 -0.01510 -0.02480 0.03510  192 SER A CB    
1503 O  OG    . SER A 192 ? 0.74280 0.72410 0.76810 -0.01210 -0.02510 0.03300  192 SER A OG    
1504 N  N     . HIS A 193 ? 0.46240 0.45080 0.46500 -0.02390 -0.01730 0.03020  193 HIS A N     
1505 C  CA    . HIS A 193 ? 0.44140 0.43170 0.43650 -0.02710 -0.01520 0.03100  193 HIS A CA    
1506 C  C     . HIS A 193 ? 0.37740 0.36430 0.36500 -0.02730 -0.01630 0.03800  193 HIS A C     
1507 O  O     . HIS A 193 ? 0.44010 0.42010 0.42910 -0.02710 -0.01590 0.04270  193 HIS A O     
1508 C  CB    . HIS A 193 ? 0.40830 0.39750 0.40680 -0.03030 -0.01100 0.02830  193 HIS A CB    
1509 C  CG    . HIS A 193 ? 0.50690 0.49940 0.49980 -0.03350 -0.00820 0.02830  193 HIS A CG    
1510 N  ND1   . HIS A 193 ? 0.41750 0.41700 0.40840 -0.03360 -0.00780 0.02450  193 HIS A ND1   
1511 C  CD2   . HIS A 193 ? 0.46420 0.45360 0.45360 -0.03660 -0.00530 0.03180  193 HIS A CD2   
1512 C  CE1   . HIS A 193 ? 0.51140 0.51260 0.49830 -0.03640 -0.00480 0.02510  193 HIS A CE1   
1513 N  NE2   . HIS A 193 ? 0.39810 0.39360 0.38390 -0.03850 -0.00310 0.02950  193 HIS A NE2   
1514 N  N     . LEU A 194 ? 0.44580 0.43770 0.42530 -0.02760 -0.01750 0.03840  194 LEU A N     
1515 C  CA    . LEU A 194 ? 0.40170 0.39230 0.37140 -0.02790 -0.01860 0.04440  194 LEU A CA    
1516 C  C     . LEU A 194 ? 0.39730 0.38860 0.36020 -0.03180 -0.01400 0.04500  194 LEU A C     
1517 O  O     . LEU A 194 ? 0.43530 0.42280 0.39160 -0.03300 -0.01260 0.05120  194 LEU A O     
1518 C  CB    . LEU A 194 ? 0.45500 0.45180 0.41980 -0.02580 -0.02330 0.04370  194 LEU A CB    
1519 C  CG    . LEU A 194 ? 0.71460 0.71180 0.68380 -0.02170 -0.02880 0.04530  194 LEU A CG    
1520 C  CD1   . LEU A 194 ? 0.54810 0.55220 0.51030 -0.02090 -0.03320 0.04470  194 LEU A CD1   
1521 C  CD2   . LEU A 194 ? 0.60910 0.59900 0.57960 -0.01970 -0.03000 0.05260  194 LEU A CD2   
1522 N  N     . GLY A 195 ? 0.43430 0.43080 0.39890 -0.03360 -0.01140 0.03900  195 GLY A N     
1523 C  CA    . GLY A 195 ? 0.46840 0.46700 0.42830 -0.03700 -0.00670 0.03830  195 GLY A CA    
1524 C  C     . GLY A 195 ? 0.32060 0.32570 0.28340 -0.03760 -0.00500 0.03150  195 GLY A C     
1525 O  O     . GLY A 195 ? 0.28740 0.29470 0.25620 -0.03560 -0.00680 0.02770  195 GLY A O     
1526 N  N     . SER A 196 ? 0.33510 0.34330 0.29380 -0.04020 -0.00100 0.03060  196 SER A N     
1527 C  CA    . SER A 196 ? 0.35690 0.37110 0.31880 -0.04050 0.00130  0.02480  196 SER A CA    
1528 C  C     . SER A 196 ? 0.33130 0.34930 0.28500 -0.04110 0.00260  0.02340  196 SER A C     
1529 O  O     . SER A 196 ? 0.41450 0.43120 0.35930 -0.04260 0.00340  0.02720  196 SER A O     
1530 C  CB    . SER A 196 ? 0.41600 0.43140 0.38390 -0.04310 0.00560  0.02350  196 SER A CB    
1531 O  OG    . SER A 196 ? 0.45450 0.46740 0.43030 -0.04260 0.00420  0.02300  196 SER A OG    
1532 N  N     . ALA A 197 ? 0.30570 0.32810 0.26220 -0.03990 0.00290  0.01810  197 ALA A N     
1533 C  CA    . ALA A 197 ? 0.29160 0.31760 0.24180 -0.04040 0.00420  0.01510  197 ALA A CA    
1534 C  C     . ALA A 197 ? 0.31920 0.34940 0.27560 -0.03960 0.00690  0.00940  197 ALA A C     
1535 O  O     . ALA A 197 ? 0.33580 0.36630 0.30090 -0.03770 0.00630  0.00790  197 ALA A O     
1536 C  CB    . ALA A 197 ? 0.30080 0.32640 0.24590 -0.03890 -0.00060 0.01520  197 ALA A CB    
1537 N  N     . ILE A 198 ? 0.32520 0.35850 0.27670 -0.04070 0.00990  0.00620  198 ILE A N     
1538 C  CA    . ILE A 198 ? 0.32780 0.36450 0.28470 -0.03960 0.01270  0.00040  198 ILE A CA    
1539 C  C     . ILE A 198 ? 0.34360 0.38040 0.29710 -0.03890 0.01050  -0.00350 198 ILE A C     
1540 O  O     . ILE A 198 ? 0.31700 0.35490 0.26070 -0.04050 0.01010  -0.00400 198 ILE A O     
1541 C  CB    . ILE A 198 ? 0.37180 0.41250 0.32710 -0.04160 0.01870  -0.00180 198 ILE A CB    
1542 C  CG1   . ILE A 198 ? 0.35150 0.39320 0.31180 -0.04300 0.02120  0.00120  198 ILE A CG1   
1543 C  CG2   . ILE A 198 ? 0.39590 0.43970 0.35710 -0.03990 0.02160  -0.00810 198 ILE A CG2   
1544 C  CD1   . ILE A 198 ? 0.36820 0.41020 0.33950 -0.04070 0.01930  0.00140  198 ILE A CD1   
1545 N  N     . PHE A 199 ? 0.29810 0.33410 0.25970 -0.03650 0.00910  -0.00620 199 PHE A N     
1546 C  CA    . PHE A 199 ? 0.30650 0.34250 0.26840 -0.03610 0.00790  -0.01100 199 PHE A CA    
1547 C  C     . PHE A 199 ? 0.28070 0.31720 0.25150 -0.03450 0.01190  -0.01560 199 PHE A C     
1548 O  O     . PHE A 199 ? 0.35890 0.39340 0.33830 -0.03210 0.01130  -0.01490 199 PHE A O     
1549 C  CB    . PHE A 199 ? 0.31310 0.34660 0.27850 -0.03470 0.00290  -0.00920 199 PHE A CB    
1550 C  CG    . PHE A 199 ? 0.30900 0.34190 0.26730 -0.03550 -0.00150 -0.00480 199 PHE A CG    
1551 C  CD1   . PHE A 199 ? 0.36390 0.39910 0.31330 -0.03690 -0.00390 -0.00610 199 PHE A CD1   
1552 C  CD2   . PHE A 199 ? 0.39170 0.42210 0.35260 -0.03450 -0.00340 0.00050  199 PHE A CD2   
1553 C  CE1   . PHE A 199 ? 0.33800 0.37270 0.28130 -0.03680 -0.00840 -0.00110 199 PHE A CE1   
1554 C  CE2   . PHE A 199 ? 0.33970 0.36880 0.29540 -0.03460 -0.00730 0.00490  199 PHE A CE2   
1555 C  CZ    . PHE A 199 ? 0.32420 0.35530 0.27120 -0.03550 -0.00990 0.00470  199 PHE A CZ    
1556 N  N     . PRO A 200 ? 0.32690 0.36600 0.29600 -0.03540 0.01650  -0.02000 200 PRO A N     
1557 C  CA    . PRO A 200 ? 0.34940 0.38890 0.32820 -0.03330 0.02080  -0.02370 200 PRO A CA    
1558 C  C     . PRO A 200 ? 0.32140 0.35740 0.30870 -0.03120 0.02020  -0.02640 200 PRO A C     
1559 O  O     . PRO A 200 ? 0.37870 0.41330 0.37510 -0.02820 0.02140  -0.02450 200 PRO A O     
1560 C  CB    . PRO A 200 ? 0.35810 0.40100 0.33190 -0.03530 0.02550  -0.02930 200 PRO A CB    
1561 C  CG    . PRO A 200 ? 0.38190 0.42700 0.34340 -0.03830 0.02440  -0.02580 200 PRO A CG    
1562 C  CD    . PRO A 200 ? 0.36590 0.40800 0.32370 -0.03840 0.01800  -0.02150 200 PRO A CD    
1563 N  N     . ASP A 201 ? 0.30340 0.33830 0.28780 -0.03290 0.01840  -0.03060 201 ASP A N     
1564 C  CA    . ASP A 201 ? 0.31560 0.34670 0.30900 -0.03170 0.01860  -0.03380 201 ASP A CA    
1565 C  C     . ASP A 201 ? 0.32080 0.34890 0.31940 -0.02980 0.01540  -0.02790 201 ASP A C     
1566 O  O     . ASP A 201 ? 0.33530 0.35990 0.34340 -0.02770 0.01720  -0.02770 201 ASP A O     
1567 C  CB    . ASP A 201 ? 0.37210 0.40400 0.36180 -0.03460 0.01710  -0.04080 201 ASP A CB    
1568 C  CG    . ASP A 201 ? 0.71390 0.74800 0.70140 -0.03600 0.02170  -0.04870 201 ASP A CG    
1569 O  OD1   . ASP A 201 ? 0.52780 0.56120 0.52120 -0.03410 0.02670  -0.04960 201 ASP A OD1   
1570 O  OD2   . ASP A 201 ? 0.62530 0.66240 0.60510 -0.03900 0.02010  -0.05440 201 ASP A OD2   
1571 N  N     . VAL A 202 ? 0.26340 0.29280 0.25590 -0.03050 0.01120  -0.02300 202 VAL A N     
1572 C  CA    . VAL A 202 ? 0.30510 0.33240 0.30170 -0.02880 0.00850  -0.01780 202 VAL A CA    
1573 C  C     . VAL A 202 ? 0.32830 0.35560 0.32990 -0.02590 0.01060  -0.01360 202 VAL A C     
1574 O  O     . VAL A 202 ? 0.35110 0.37640 0.35860 -0.02370 0.01050  -0.01080 202 VAL A O     
1575 C  CB    . VAL A 202 ? 0.32700 0.35560 0.31670 -0.03010 0.00380  -0.01410 202 VAL A CB    
1576 C  CG1   . VAL A 202 ? 0.35590 0.38260 0.35070 -0.02840 0.00160  -0.01010 202 VAL A CG1   
1577 C  CG2   . VAL A 202 ? 0.32490 0.35510 0.30910 -0.03250 0.00080  -0.01780 202 VAL A CG2   
1578 N  N     . ALA A 203 ? 0.31510 0.34520 0.31430 -0.02600 0.01270  -0.01350 203 ALA A N     
1579 C  CA    . ALA A 203 ? 0.27680 0.30890 0.28100 -0.02330 0.01420  -0.01030 203 ALA A CA    
1580 C  C     . ALA A 203 ? 0.28450 0.31510 0.29780 -0.01980 0.01720  -0.01090 203 ALA A C     
1581 O  O     . ALA A 203 ? 0.22360 0.25580 0.24140 -0.01680 0.01720  -0.00730 203 ALA A O     
1582 C  CB    . ALA A 203 ? 0.31640 0.35270 0.31730 -0.02470 0.01610  -0.01090 203 ALA A CB    
1583 N  N     . LEU A 204 ? 0.29030 0.31790 0.30650 -0.02020 0.01960  -0.01560 204 LEU A N     
1584 C  CA    . LEU A 204 ? 0.28750 0.31200 0.31350 -0.01690 0.02310  -0.01620 204 LEU A CA    
1585 C  C     . LEU A 204 ? 0.29600 0.31690 0.32690 -0.01440 0.02210  -0.01110 204 LEU A C     
1586 O  O     . LEU A 204 ? 0.28330 0.30240 0.32140 -0.01050 0.02450  -0.00850 204 LEU A O     
1587 C  CB    . LEU A 204 ? 0.31890 0.34020 0.34730 -0.01870 0.02610  -0.02340 204 LEU A CB    
1588 C  CG    . LEU A 204 ? 0.30050 0.31690 0.34030 -0.01550 0.03050  -0.02480 204 LEU A CG    
1589 C  CD1   . LEU A 204 ? 0.40780 0.42670 0.45330 -0.01110 0.03310  -0.02220 204 LEU A CD1   
1590 C  CD2   . LEU A 204 ? 0.35520 0.36900 0.39670 -0.01830 0.03340  -0.03370 204 LEU A CD2   
1591 N  N     . MET A 205 ? 0.24710 0.26710 0.27390 -0.01640 0.01880  -0.00960 205 MET A N     
1592 C  CA    . MET A 205 ? 0.25030 0.26730 0.28100 -0.01460 0.01840  -0.00520 205 MET A CA    
1593 C  C     . MET A 205 ? 0.21460 0.23480 0.24450 -0.01130 0.01720  0.00090  205 MET A C     
1594 O  O     . MET A 205 ? 0.28350 0.30810 0.30800 -0.01210 0.01460  0.00180  205 MET A O     
1595 C  CB    . MET A 205 ? 0.33930 0.35560 0.36670 -0.01770 0.01530  -0.00600 205 MET A CB    
1596 C  CG    . MET A 205 ? 0.31780 0.33190 0.34720 -0.02090 0.01580  -0.01230 205 MET A CG    
1597 S  SD    . MET A 205 ? 0.33960 0.35440 0.36740 -0.02380 0.01160  -0.01280 205 MET A SD    
1598 C  CE    . MET A 205 ? 0.32220 0.34190 0.33880 -0.02490 0.00690  -0.01150 205 MET A CE    
1599 N  N     . ASN A 206 ? 0.27360 0.29150 0.30900 -0.00760 0.01930  0.00510  206 ASN A N     
1600 C  CA    . ASN A 206 ? 0.27760 0.29940 0.31180 -0.00410 0.01790  0.01100  206 ASN A CA    
1601 C  C     . ASN A 206 ? 0.23060 0.25270 0.26050 -0.00520 0.01560  0.01350  206 ASN A C     
1602 O  O     . ASN A 206 ? 0.26170 0.28080 0.29110 -0.00830 0.01520  0.01120  206 ASN A O     
1603 C  CB    . ASN A 206 ? 0.24700 0.26650 0.28780 0.00090  0.02110  0.01530  206 ASN A CB    
1604 C  CG    . ASN A 206 ? 0.28210 0.30350 0.32760 0.00310  0.02290  0.01330  206 ASN A CG    
1605 O  OD1   . ASN A 206 ? 0.26560 0.29350 0.30860 0.00280  0.02090  0.01170  206 ASN A OD1   
1606 N  ND2   . ASN A 206 ? 0.30170 0.31730 0.35510 0.00520  0.02700  0.01310  206 ASN A ND2   
1607 N  N     . HIS A 207 ? 0.28020 0.30700 0.30720 -0.00270 0.01380  0.01750  207 HIS A N     
1608 C  CA    . HIS A 207 ? 0.26980 0.29800 0.29250 -0.00350 0.01180  0.01920  207 HIS A CA    
1609 C  C     . HIS A 207 ? 0.25770 0.28340 0.28200 -0.00100 0.01420  0.02410  207 HIS A C     
1610 O  O     . HIS A 207 ? 0.28150 0.30670 0.30850 0.00290  0.01640  0.02830  207 HIS A O     
1611 C  CB    . HIS A 207 ? 0.27570 0.31110 0.29390 -0.00290 0.00860  0.01950  207 HIS A CB    
1612 C  CG    . HIS A 207 ? 0.26960 0.30690 0.28380 -0.00280 0.00720  0.02110  207 HIS A CG    
1613 N  ND1   . HIS A 207 ? 0.23140 0.26780 0.24320 -0.00600 0.00540  0.01840  207 HIS A ND1   
1614 C  CD2   . HIS A 207 ? 0.26930 0.30950 0.28150 0.00040  0.00760  0.02510  207 HIS A CD2   
1615 C  CE1   . HIS A 207 ? 0.29240 0.33110 0.30170 -0.00500 0.00510  0.01990  207 HIS A CE1   
1616 N  NE2   . HIS A 207 ? 0.25650 0.29780 0.26530 -0.00130 0.00640  0.02390  207 HIS A NE2   
1617 N  N     . SER A 208 ? 0.27910 0.30350 0.30200 -0.00300 0.01410  0.02390  208 SER A N     
1618 C  CA    . SER A 208 ? 0.34230 0.36610 0.36490 -0.00110 0.01640  0.02860  208 SER A CA    
1619 C  C     . SER A 208 ? 0.39420 0.42110 0.41260 -0.00300 0.01420  0.02690  208 SER A C     
1620 O  O     . SER A 208 ? 0.25980 0.28620 0.27840 -0.00620 0.01200  0.02250  208 SER A O     
1621 C  CB    . SER A 208 ? 0.34570 0.36250 0.37520 -0.00210 0.02070  0.02940  208 SER A CB    
1622 O  OG    . SER A 208 ? 0.28460 0.30080 0.31380 -0.00080 0.02370  0.03420  208 SER A OG    
1623 N  N     . CYS A 209 ? 0.29750 0.32780 0.31200 -0.00070 0.01490  0.03040  209 CYS A N     
1624 C  CA    . CYS A 209 ? 0.29080 0.32370 0.30240 -0.00220 0.01400  0.02860  209 CYS A CA    
1625 C  C     . CYS A 209 ? 0.26640 0.29530 0.28280 -0.00390 0.01750  0.02900  209 CYS A C     
1626 O  O     . CYS A 209 ? 0.28700 0.31770 0.30310 -0.00520 0.01720  0.02690  209 CYS A O     
1627 C  CB    . CYS A 209 ? 0.37830 0.41770 0.38310 0.00070  0.01340  0.03090  209 CYS A CB    
1628 S  SG    . CYS A 209 ? 0.29220 0.33760 0.29360 0.00300  0.00970  0.03090  209 CYS A SG    
1629 N  N     . CYS A 210 ? 0.25880 0.28250 0.28090 -0.00390 0.02100  0.03120  210 CYS A N     
1630 C  CA    . CYS A 210 ? 0.28430 0.30420 0.31370 -0.00670 0.02400  0.02990  210 CYS A CA    
1631 C  C     . CYS A 210 ? 0.27950 0.29500 0.31510 -0.00910 0.02330  0.02610  210 CYS A C     
1632 O  O     . CYS A 210 ? 0.29120 0.30180 0.33280 -0.00920 0.02720  0.02760  210 CYS A O     
1633 C  CB    . CYS A 210 ? 0.38450 0.40210 0.41590 -0.00520 0.03000  0.03570  210 CYS A CB    
1634 S  SG    . CYS A 210 ? 0.49140 0.50690 0.51980 -0.00040 0.03290  0.04360  210 CYS A SG    
1635 N  N     . PRO A 211 ? 0.25470 0.27190 0.28890 -0.01110 0.01870  0.02100  211 PRO A N     
1636 C  CA    . PRO A 211 ? 0.30170 0.31610 0.33940 -0.01320 0.01780  0.01700  211 PRO A CA    
1637 C  C     . PRO A 211 ? 0.30790 0.31960 0.35410 -0.01630 0.01950  0.01380  211 PRO A C     
1638 O  O     . PRO A 211 ? 0.28280 0.29610 0.33200 -0.01740 0.02000  0.01380  211 PRO A O     
1639 C  CB    . PRO A 211 ? 0.27510 0.29300 0.30730 -0.01440 0.01250  0.01360  211 PRO A CB    
1640 C  CG    . PRO A 211 ? 0.25410 0.27510 0.28430 -0.01430 0.01090  0.01410  211 PRO A CG    
1641 C  CD    . PRO A 211 ? 0.27230 0.29390 0.30160 -0.01160 0.01460  0.01890  211 PRO A CD    
1642 N  N     . ASN A 212 ? 0.22140 0.22960 0.27220 -0.01780 0.02060  0.01060  212 ASN A N     
1643 C  CA    . ASN A 212 ? 0.27530 0.28190 0.33490 -0.02140 0.02170  0.00590  212 ASN A CA    
1644 C  C     . ASN A 212 ? 0.26780 0.27780 0.32590 -0.02440 0.01640  -0.00080 212 ASN A C     
1645 O  O     . ASN A 212 ? 0.25980 0.27050 0.32480 -0.02750 0.01600  -0.00560 212 ASN A O     
1646 C  CB    . ASN A 212 ? 0.23230 0.23230 0.30000 -0.02160 0.02730  0.00610  212 ASN A CB    
1647 C  CG    . ASN A 212 ? 0.23910 0.23660 0.30440 -0.01990 0.02770  0.00530  212 ASN A CG    
1648 O  OD1   . ASN A 212 ? 0.30820 0.30930 0.36640 -0.01970 0.02360  0.00300  212 ASN A OD1   
1649 N  ND2   . ASN A 212 ? 0.26540 0.25640 0.33750 -0.01870 0.03300  0.00720  212 ASN A ND2   
1650 N  N     . VAL A 213 ? 0.21490 0.22760 0.26400 -0.02330 0.01250  -0.00080 213 VAL A N     
1651 C  CA    . VAL A 213 ? 0.23670 0.25310 0.28200 -0.02550 0.00730  -0.00530 213 VAL A CA    
1652 C  C     . VAL A 213 ? 0.26840 0.28790 0.30570 -0.02400 0.00340  -0.00250 213 VAL A C     
1653 O  O     . VAL A 213 ? 0.30530 0.32440 0.33910 -0.02170 0.00460  0.00160  213 VAL A O     
1654 C  CB    . VAL A 213 ? 0.23210 0.24770 0.27470 -0.02670 0.00710  -0.00970 213 VAL A CB    
1655 C  CG1   . VAL A 213 ? 0.25470 0.26640 0.30650 -0.02840 0.01120  -0.01360 213 VAL A CG1   
1656 C  CG2   . VAL A 213 ? 0.26250 0.27740 0.29860 -0.02430 0.00810  -0.00670 213 VAL A CG2   
1657 N  N     . ILE A 214 ? 0.25970 0.28250 0.29470 -0.02550 -0.00140 -0.00480 214 ILE A N     
1658 C  CA    . ILE A 214 ? 0.26410 0.28870 0.29210 -0.02450 -0.00500 -0.00250 214 ILE A CA    
1659 C  C     . ILE A 214 ? 0.28730 0.31330 0.30880 -0.02610 -0.00850 -0.00500 214 ILE A C     
1660 O  O     . ILE A 214 ? 0.24070 0.26860 0.26410 -0.02800 -0.01020 -0.00910 214 ILE A O     
1661 C  CB    . ILE A 214 ? 0.34320 0.37010 0.37480 -0.02400 -0.00750 -0.00160 214 ILE A CB    
1662 C  CG1   . ILE A 214 ? 0.52970 0.55560 0.56530 -0.02230 -0.00360 0.00120  214 ILE A CG1   
1663 C  CG2   . ILE A 214 ? 0.33770 0.36550 0.36320 -0.02310 -0.01150 0.00030  214 ILE A CG2   
1664 C  CD1   . ILE A 214 ? 0.49500 0.52350 0.53600 -0.02170 -0.00480 0.00120  214 ILE A CD1   
1665 N  N     . VAL A 215 ? 0.25580 0.28160 0.26980 -0.02540 -0.00930 -0.00250 215 VAL A N     
1666 C  CA    . VAL A 215 ? 0.28650 0.31350 0.29280 -0.02680 -0.01190 -0.00340 215 VAL A CA    
1667 C  C     . VAL A 215 ? 0.35420 0.38240 0.35790 -0.02630 -0.01650 -0.00080 215 VAL A C     
1668 O  O     . VAL A 215 ? 0.32100 0.34780 0.32560 -0.02480 -0.01660 0.00240  215 VAL A O     
1669 C  CB    . VAL A 215 ? 0.32570 0.35160 0.32630 -0.02660 -0.00950 -0.00180 215 VAL A CB    
1670 C  CG1   . VAL A 215 ? 0.41790 0.44520 0.40990 -0.02830 -0.01120 -0.00260 215 VAL A CG1   
1671 C  CG2   . VAL A 215 ? 0.34810 0.37280 0.35260 -0.02610 -0.00500 -0.00360 215 VAL A CG2   
1672 N  N     . THR A 216 ? 0.29210 0.32330 0.29300 -0.02730 -0.02050 -0.00260 216 THR A N     
1673 C  CA    . THR A 216 ? 0.26740 0.29980 0.26490 -0.02640 -0.02530 0.00060  216 THR A CA    
1674 C  C     . THR A 216 ? 0.38250 0.41640 0.36940 -0.02770 -0.02720 0.00090  216 THR A C     
1675 O  O     . THR A 216 ? 0.35080 0.38540 0.33400 -0.02950 -0.02480 -0.00260 216 THR A O     
1676 C  CB    . THR A 216 ? 0.32250 0.35870 0.32750 -0.02570 -0.02920 -0.00110 216 THR A CB    
1677 O  OG1   . THR A 216 ? 0.36680 0.40720 0.37290 -0.02780 -0.03040 -0.00660 216 THR A OG1   
1678 C  CG2   . THR A 216 ? 0.29830 0.33330 0.31360 -0.02460 -0.02640 -0.00110 216 THR A CG2   
1679 N  N     . TYR A 217 ? 0.38030 0.41450 0.36220 -0.02650 -0.03130 0.00520  217 TYR A N     
1680 C  CA    . TYR A 217 ? 0.34480 0.37990 0.31470 -0.02750 -0.03280 0.00740  217 TYR A CA    
1681 C  C     . TYR A 217 ? 0.36270 0.40250 0.32980 -0.02620 -0.03950 0.00880  217 TYR A C     
1682 O  O     . TYR A 217 ? 0.35980 0.39940 0.33320 -0.02370 -0.04280 0.01180  217 TYR A O     
1683 C  CB    . TYR A 217 ? 0.30220 0.33190 0.26780 -0.02730 -0.02990 0.01300  217 TYR A CB    
1684 C  CG    . TYR A 217 ? 0.35140 0.37830 0.32110 -0.02810 -0.02430 0.01140  217 TYR A CG    
1685 C  CD1   . TYR A 217 ? 0.35260 0.38060 0.31900 -0.03000 -0.02040 0.00810  217 TYR A CD1   
1686 C  CD2   . TYR A 217 ? 0.33490 0.35900 0.31240 -0.02670 -0.02310 0.01260  217 TYR A CD2   
1687 C  CE1   . TYR A 217 ? 0.30610 0.33250 0.27710 -0.03010 -0.01580 0.00690  217 TYR A CE1   
1688 C  CE2   . TYR A 217 ? 0.33400 0.35690 0.31470 -0.02700 -0.01870 0.01120  217 TYR A CE2   
1689 C  CZ    . TYR A 217 ? 0.39210 0.41630 0.36990 -0.02860 -0.01530 0.00870  217 TYR A CZ    
1690 O  OH    . TYR A 217 ? 0.40780 0.43170 0.38940 -0.02830 -0.01160 0.00770  217 TYR A OH    
1691 N  N     . LYS A 218 ? 0.34430 0.38880 0.30250 -0.02780 -0.04140 0.00610  218 LYS A N     
1692 C  CA    . LYS A 218 ? 0.39600 0.44640 0.34800 -0.02660 -0.04820 0.00780  218 LYS A CA    
1693 C  C     . LYS A 218 ? 0.39600 0.44470 0.33290 -0.02710 -0.04730 0.01320  218 LYS A C     
1694 O  O     . LYS A 218 ? 0.41640 0.46820 0.34400 -0.02950 -0.04570 0.00960  218 LYS A O     
1695 C  CB    . LYS A 218 ? 0.34580 0.40400 0.29910 -0.02850 -0.05090 -0.00070 218 LYS A CB    
1696 C  CG    . LYS A 218 ? 0.43830 0.50480 0.38990 -0.02690 -0.05930 -0.00050 218 LYS A CG    
1697 C  CD    . LYS A 218 ? 0.47970 0.55430 0.43640 -0.02930 -0.06170 -0.01060 218 LYS A CD    
1698 C  CE    . LYS A 218 ? 0.55090 0.62490 0.52540 -0.02950 -0.06040 -0.01460 218 LYS A CE    
1699 N  NZ    . LYS A 218 ? 0.48070 0.56010 0.46220 -0.03290 -0.06010 -0.02510 218 LYS A NZ    
1700 N  N     . GLY A 219 ? 0.39240 0.43570 0.32770 -0.02500 -0.04760 0.02170  219 GLY A N     
1701 C  CA    . GLY A 219 ? 0.50960 0.54900 0.43300 -0.02590 -0.04460 0.02780  219 GLY A CA    
1702 C  C     . GLY A 219 ? 0.49950 0.53490 0.42380 -0.02880 -0.03680 0.02500  219 GLY A C     
1703 O  O     . GLY A 219 ? 0.44830 0.47890 0.38230 -0.02850 -0.03370 0.02500  219 GLY A O     
1704 N  N     . THR A 220 ? 0.34260 0.38080 0.25680 -0.03140 -0.03370 0.02230  220 THR A N     
1705 C  CA    . THR A 220 ? 0.39120 0.42720 0.30630 -0.03400 -0.02630 0.01930  220 THR A CA    
1706 C  C     . THR A 220 ? 0.36240 0.40220 0.28220 -0.03530 -0.02440 0.00960  220 THR A C     
1707 O  O     . THR A 220 ? 0.33580 0.37490 0.25660 -0.03700 -0.01860 0.00650  220 THR A O     
1708 C  CB    . THR A 220 ? 0.42980 0.46580 0.33130 -0.03610 -0.02260 0.02280  220 THR A CB    
1709 O  OG1   . THR A 220 ? 0.36340 0.40640 0.25390 -0.03700 -0.02490 0.01900  220 THR A OG1   
1710 C  CG2   . THR A 220 ? 0.56910 0.60000 0.46600 -0.03490 -0.02360 0.03300  220 THR A CG2   
1711 N  N     . LEU A 221 ? 0.40190 0.44590 0.32600 -0.03460 -0.02910 0.00510  221 LEU A N     
1712 C  CA    . LEU A 221 ? 0.36450 0.41120 0.29510 -0.03590 -0.02750 -0.00410 221 LEU A CA    
1713 C  C     . LEU A 221 ? 0.38520 0.42820 0.33040 -0.03460 -0.02630 -0.00490 221 LEU A C     
1714 O  O     . LEU A 221 ? 0.36560 0.40840 0.31660 -0.03280 -0.03040 -0.00230 221 LEU A O     
1715 C  CB    . LEU A 221 ? 0.42110 0.47490 0.34880 -0.03640 -0.03320 -0.00920 221 LEU A CB    
1716 C  CG    . LEU A 221 ? 0.46500 0.52170 0.40040 -0.03830 -0.03180 -0.01950 221 LEU A CG    
1717 C  CD1   . LEU A 221 ? 0.39740 0.45540 0.32540 -0.04070 -0.02670 -0.02520 221 LEU A CD1   
1718 C  CD2   . LEU A 221 ? 0.41710 0.48100 0.35390 -0.03840 -0.03890 -0.02360 221 LEU A CD2   
1719 N  N     . ALA A 222 ? 0.31250 0.35290 0.26340 -0.03530 -0.02070 -0.00820 222 ALA A N     
1720 C  CA    . ALA A 222 ? 0.29260 0.33000 0.25620 -0.03400 -0.01910 -0.00900 222 ALA A CA    
1721 C  C     . ALA A 222 ? 0.27930 0.31920 0.24990 -0.03480 -0.02020 -0.01570 222 ALA A C     
1722 O  O     . ALA A 222 ? 0.32150 0.36410 0.28930 -0.03670 -0.01920 -0.02180 222 ALA A O     
1723 C  CB    . ALA A 222 ? 0.27450 0.30870 0.24120 -0.03390 -0.01310 -0.00890 222 ALA A CB    
1724 N  N     . GLU A 223 ? 0.31420 0.35340 0.29460 -0.03360 -0.02180 -0.01500 223 GLU A N     
1725 C  CA    . GLU A 223 ? 0.26930 0.31020 0.25910 -0.03470 -0.02210 -0.02090 223 GLU A CA    
1726 C  C     . GLU A 223 ? 0.27780 0.31410 0.27820 -0.03340 -0.01790 -0.01940 223 GLU A C     
1727 O  O     . GLU A 223 ? 0.32820 0.36210 0.32930 -0.03140 -0.01750 -0.01380 223 GLU A O     
1728 C  CB    . GLU A 223 ? 0.29060 0.33680 0.28230 -0.03460 -0.02860 -0.02150 223 GLU A CB    
1729 C  CG    . GLU A 223 ? 0.40410 0.45600 0.38440 -0.03550 -0.03350 -0.02270 223 GLU A CG    
1730 C  CD    . GLU A 223 ? 0.53470 0.59370 0.51850 -0.03530 -0.04050 -0.02450 223 GLU A CD    
1731 O  OE1   . GLU A 223 ? 0.47440 0.53320 0.46630 -0.03330 -0.04260 -0.02100 223 GLU A OE1   
1732 O  OE2   . GLU A 223 ? 0.52720 0.59270 0.50600 -0.03710 -0.04400 -0.03000 223 GLU A OE2   
1733 N  N     . VAL A 224 ? 0.25520 0.29010 0.26340 -0.03470 -0.01440 -0.02440 224 VAL A N     
1734 C  CA    . VAL A 224 ? 0.27790 0.30810 0.29520 -0.03340 -0.00960 -0.02250 224 VAL A CA    
1735 C  C     . VAL A 224 ? 0.26860 0.29950 0.29710 -0.03490 -0.00950 -0.02640 224 VAL A C     
1736 O  O     . VAL A 224 ? 0.35130 0.38330 0.38330 -0.03740 -0.00890 -0.03320 224 VAL A O     
1737 C  CB    . VAL A 224 ? 0.25760 0.28410 0.27520 -0.03300 -0.00410 -0.02380 224 VAL A CB    
1738 C  CG1   . VAL A 224 ? 0.30120 0.32300 0.32750 -0.03110 0.00040  -0.02070 224 VAL A CG1   
1739 C  CG2   . VAL A 224 ? 0.33220 0.35900 0.34000 -0.03200 -0.00400 -0.02070 224 VAL A CG2   
1740 N  N     . ARG A 225 ? 0.23490 0.26560 0.26950 -0.03360 -0.00960 -0.02270 225 ARG A N     
1741 C  CA    . ARG A 225 ? 0.29110 0.32330 0.33750 -0.03530 -0.00930 -0.02570 225 ARG A CA    
1742 C  C     . ARG A 225 ? 0.31580 0.34300 0.36950 -0.03390 -0.00350 -0.02170 225 ARG A C     
1743 O  O     . ARG A 225 ? 0.27760 0.30290 0.32670 -0.03110 -0.00230 -0.01580 225 ARG A O     
1744 C  CB    . ARG A 225 ? 0.23680 0.27520 0.28400 -0.03510 -0.01540 -0.02540 225 ARG A CB    
1745 C  CG    . ARG A 225 ? 0.25650 0.30120 0.29960 -0.03690 -0.02130 -0.03070 225 ARG A CG    
1746 C  CD    . ARG A 225 ? 0.28050 0.33230 0.32650 -0.03630 -0.02780 -0.03040 225 ARG A CD    
1747 N  NE    . ARG A 225 ? 0.33610 0.39450 0.37540 -0.03750 -0.03390 -0.03450 225 ARG A NE    
1748 C  CZ    . ARG A 225 ? 0.29160 0.35070 0.31740 -0.03610 -0.03720 -0.03120 225 ARG A CZ    
1749 N  NH1   . ARG A 225 ? 0.38040 0.43380 0.39910 -0.03380 -0.03500 -0.02430 225 ARG A NH1   
1750 N  NH2   . ARG A 225 ? 0.37330 0.43920 0.39240 -0.03720 -0.04270 -0.03500 225 ARG A NH2   
1751 N  N     . ALA A 226 ? 0.32600 0.35150 0.39080 -0.03600 0.00020  -0.02500 226 ALA A N     
1752 C  CA    . ALA A 226 ? 0.26070 0.28140 0.33270 -0.03490 0.00630  -0.02070 226 ALA A CA    
1753 C  C     . ALA A 226 ? 0.29730 0.32120 0.37230 -0.03390 0.00540  -0.01720 226 ALA A C     
1754 O  O     . ALA A 226 ? 0.26980 0.29950 0.34940 -0.03540 0.00140  -0.02040 226 ALA A O     
1755 C  CB    . ALA A 226 ? 0.29650 0.31400 0.38050 -0.03800 0.01080  -0.02550 226 ALA A CB    
1756 N  N     . VAL A 227 ? 0.26100 0.28200 0.33340 -0.03100 0.00900  -0.01070 227 VAL A N     
1757 C  CA    . VAL A 227 ? 0.32620 0.34960 0.40190 -0.02990 0.01000  -0.00740 227 VAL A CA    
1758 C  C     . VAL A 227 ? 0.35830 0.37750 0.44070 -0.02990 0.01740  -0.00390 227 VAL A C     
1759 O  O     . VAL A 227 ? 0.31550 0.33660 0.40060 -0.02910 0.01970  -0.00120 227 VAL A O     
1760 C  CB    . VAL A 227 ? 0.30650 0.33130 0.37220 -0.02670 0.00740  -0.00330 227 VAL A CB    
1761 C  CG1   . VAL A 227 ? 0.33330 0.36160 0.39340 -0.02690 0.00050  -0.00580 227 VAL A CG1   
1762 C  CG2   . VAL A 227 ? 0.34000 0.36080 0.39810 -0.02430 0.01020  0.00110  227 VAL A CG2   
1763 N  N     . GLN A 228 ? 0.36420 0.37770 0.44910 -0.03050 0.02160  -0.00380 228 GLN A N     
1764 C  CA    . GLN A 228 ? 0.35560 0.36400 0.44910 -0.03110 0.02910  -0.00090 228 GLN A CA    
1765 C  C     . GLN A 228 ? 0.33130 0.33570 0.43310 -0.03440 0.03070  -0.00660 228 GLN A C     
1766 O  O     . GLN A 228 ? 0.33580 0.34100 0.43350 -0.03490 0.02670  -0.01130 228 GLN A O     
1767 C  CB    . GLN A 228 ? 0.33070 0.33440 0.41730 -0.02710 0.03320  0.00700  228 GLN A CB    
1768 C  CG    . GLN A 228 ? 0.38540 0.39290 0.46340 -0.02390 0.03230  0.01220  228 GLN A CG    
1769 C  CD    . GLN A 228 ? 0.45240 0.45650 0.52400 -0.01990 0.03620  0.01990  228 GLN A CD    
1770 O  OE1   . GLN A 228 ? 0.54490 0.54410 0.62150 -0.01950 0.04240  0.02430  228 GLN A OE1   
1771 N  NE2   . GLN A 228 ? 0.49290 0.49970 0.55400 -0.01680 0.03240  0.02170  228 GLN A NE2   
1772 N  N     . GLU A 229 ? 0.32270 0.32290 0.43640 -0.03670 0.03710  -0.00640 229 GLU A N     
1773 C  CA    . GLU A 229 ? 0.35770 0.35270 0.48090 -0.03990 0.03990  -0.01210 229 GLU A CA    
1774 C  C     . GLU A 229 ? 0.33610 0.32410 0.45350 -0.03660 0.04210  -0.00870 229 GLU A C     
1775 O  O     . GLU A 229 ? 0.36830 0.35310 0.48010 -0.03240 0.04520  -0.00010 229 GLU A O     
1776 C  CB    . GLU A 229 ? 0.48890 0.47970 0.62710 -0.04320 0.04730  -0.01170 229 GLU A CB    
1777 C  CG    . GLU A 229 ? 0.95970 0.94690 1.11080 -0.04800 0.04940  -0.02040 229 GLU A CG    
1778 C  CD    . GLU A 229 ? 1.27670 1.26480 1.44450 -0.05320 0.05370  -0.02380 229 GLU A CD    
1779 O  OE1   . GLU A 229 ? 0.86890 0.85270 1.04140 -0.05260 0.06090  -0.01640 229 GLU A OE1   
1780 O  OE2   . GLU A 229 ? 0.97690 0.97070 1.15310 -0.05790 0.05000  -0.03410 229 GLU A OE2   
1781 N  N     . ILE A 230 ? 0.35600 0.34280 0.47440 -0.03830 0.04030  -0.01600 230 ILE A N     
1782 C  CA    . ILE A 230 ? 0.35150 0.33250 0.46640 -0.03530 0.04240  -0.01440 230 ILE A CA    
1783 C  C     . ILE A 230 ? 0.35690 0.33070 0.48500 -0.03840 0.04760  -0.02050 230 ILE A C     
1784 O  O     . ILE A 230 ? 0.31680 0.29360 0.45090 -0.04320 0.04550  -0.03030 230 ILE A O     
1785 C  CB    . ILE A 230 ? 0.32440 0.31080 0.42760 -0.03420 0.03600  -0.01830 230 ILE A CB    
1786 C  CG1   . ILE A 230 ? 0.27680 0.27010 0.36840 -0.03190 0.03070  -0.01350 230 ILE A CG1   
1787 C  CG2   . ILE A 230 ? 0.32060 0.30170 0.42140 -0.03080 0.03880  -0.01640 230 ILE A CG2   
1788 C  CD1   . ILE A 230 ? 0.35210 0.35100 0.43320 -0.03180 0.02450  -0.01740 230 ILE A CD1   
1789 N  N     . LYS A 231 ? 0.25700 0.22130 0.38990 -0.03560 0.05440  -0.01460 231 LYS A N     
1790 C  CA    . LYS A 231 ? 0.27810 0.23340 0.42530 -0.03810 0.06080  -0.01910 231 LYS A CA    
1791 C  C     . LYS A 231 ? 0.26040 0.21170 0.40560 -0.03540 0.06130  -0.02200 231 LYS A C     
1792 O  O     . LYS A 231 ? 0.25100 0.20490 0.38490 -0.03060 0.05850  -0.01700 231 LYS A O     
1793 C  CB    . LYS A 231 ? 0.30980 0.25590 0.46550 -0.03660 0.06900  -0.00950 231 LYS A CB    
1794 C  CG    . LYS A 231 ? 0.34250 0.29250 0.50130 -0.03930 0.07000  -0.00650 231 LYS A CG    
1795 C  CD    . LYS A 231 ? 0.53830 0.49310 0.70760 -0.04650 0.06800  -0.01820 231 LYS A CD    
1796 C  CE    . LYS A 231 ? 0.72080 0.67590 0.90000 -0.04980 0.07260  -0.01540 231 LYS A CE    
1797 N  NZ    . LYS A 231 ? 1.01880 0.96150 1.21180 -0.05090 0.08300  -0.01100 231 LYS A NZ    
1798 N  N     . PRO A 232 ? 0.35000 0.29530 0.50690 -0.03860 0.06510  -0.03080 232 PRO A N     
1799 C  CA    . PRO A 232 ? 0.38240 0.32290 0.53960 -0.03570 0.06710  -0.03370 232 PRO A CA    
1800 C  C     . PRO A 232 ? 0.36680 0.30090 0.52210 -0.02840 0.07090  -0.02120 232 PRO A C     
1801 O  O     . PRO A 232 ? 0.41090 0.33860 0.57180 -0.02680 0.07580  -0.01210 232 PRO A O     
1802 C  CB    . PRO A 232 ? 0.35710 0.28950 0.53120 -0.04050 0.07290  -0.04340 232 PRO A CB    
1803 C  CG    . PRO A 232 ? 0.42750 0.36620 0.60590 -0.04730 0.07000  -0.05040 232 PRO A CG    
1804 C  CD    . PRO A 232 ? 0.38020 0.32350 0.55140 -0.04520 0.06780  -0.03930 232 PRO A CD    
1805 N  N     . GLY A 233 ? 0.34840 0.28520 0.49570 -0.02410 0.06860  -0.02070 233 GLY A N     
1806 C  CA    . GLY A 233 ? 0.36950 0.30280 0.51460 -0.01670 0.07080  -0.00970 233 GLY A CA    
1807 C  C     . GLY A 233 ? 0.33370 0.27540 0.46460 -0.01300 0.06550  -0.00050 233 GLY A C     
1808 O  O     . GLY A 233 ? 0.36030 0.30260 0.48710 -0.00690 0.06530  0.00650  233 GLY A O     
1809 N  N     . GLU A 234 ? 0.31790 0.26630 0.44230 -0.01660 0.06130  -0.00120 234 GLU A N     
1810 C  CA    . GLU A 234 ? 0.35460 0.31050 0.46640 -0.01370 0.05670  0.00650  234 GLU A CA    
1811 C  C     . GLU A 234 ? 0.35020 0.31520 0.45080 -0.01330 0.05020  0.00230  234 GLU A C     
1812 O  O     . GLU A 234 ? 0.29680 0.26470 0.39650 -0.01730 0.04770  -0.00710 234 GLU A O     
1813 C  CB    . GLU A 234 ? 0.32630 0.28510 0.43750 -0.01740 0.05580  0.00750  234 GLU A CB    
1814 C  CG    . GLU A 234 ? 0.36830 0.31880 0.49000 -0.01780 0.06300  0.01310  234 GLU A CG    
1815 C  CD    . GLU A 234 ? 0.47880 0.43340 0.59880 -0.02020 0.06260  0.01600  234 GLU A CD    
1816 O  OE1   . GLU A 234 ? 0.42330 0.38530 0.54020 -0.02390 0.05740  0.00940  234 GLU A OE1   
1817 O  OE2   . GLU A 234 ? 0.62570 0.57620 0.74740 -0.01810 0.06760  0.02510  234 GLU A OE2   
1818 N  N     . GLU A 235 ? 0.32110 0.29070 0.41300 -0.00870 0.04770  0.00950  235 GLU A N     
1819 C  CA    . GLU A 235 ? 0.31940 0.29730 0.40120 -0.00830 0.04220  0.00690  235 GLU A CA    
1820 C  C     . GLU A 235 ? 0.28420 0.26870 0.35820 -0.01200 0.03700  0.00470  235 GLU A C     
1821 O  O     . GLU A 235 ? 0.21250 0.19710 0.28610 -0.01260 0.03710  0.00870  235 GLU A O     
1822 C  CB    . GLU A 235 ? 0.31720 0.29840 0.39430 -0.00230 0.04130  0.01460  235 GLU A CB    
1823 C  CG    . GLU A 235 ? 0.37720 0.36710 0.44490 -0.00240 0.03600  0.01220  235 GLU A CG    
1824 C  CD    . GLU A 235 ? 0.36610 0.35940 0.43320 0.00310  0.03580  0.01660  235 GLU A CD    
1825 O  OE1   . GLU A 235 ? 0.35730 0.34690 0.42940 0.00790  0.03880  0.02320  235 GLU A OE1   
1826 O  OE2   . GLU A 235 ? 0.31780 0.31760 0.37950 0.00260  0.03260  0.01350  235 GLU A OE2   
1827 N  N     . VAL A 236 ? 0.22130 0.21090 0.28930 -0.01440 0.03290  -0.00160 236 VAL A N     
1828 C  CA    . VAL A 236 ? 0.26100 0.25660 0.32150 -0.01740 0.02770  -0.00360 236 VAL A CA    
1829 C  C     . VAL A 236 ? 0.23100 0.23200 0.28250 -0.01460 0.02440  0.00140  236 VAL A C     
1830 O  O     . VAL A 236 ? 0.29000 0.29310 0.33830 -0.01290 0.02400  0.00120  236 VAL A O     
1831 C  CB    . VAL A 236 ? 0.31190 0.31000 0.36990 -0.02130 0.02510  -0.01230 236 VAL A CB    
1832 C  CG1   . VAL A 236 ? 0.35340 0.35720 0.40470 -0.02390 0.01960  -0.01340 236 VAL A CG1   
1833 C  CG2   . VAL A 236 ? 0.25180 0.24510 0.31970 -0.02420 0.02850  -0.01880 236 VAL A CG2   
1834 N  N     . PHE A 237 ? 0.24540 0.24870 0.29360 -0.01440 0.02250  0.00550  237 PHE A N     
1835 C  CA    . PHE A 237 ? 0.27760 0.28580 0.31840 -0.01210 0.01970  0.00970  237 PHE A CA    
1836 C  C     . PHE A 237 ? 0.25590 0.26800 0.29150 -0.01470 0.01540  0.00780  237 PHE A C     
1837 O  O     . PHE A 237 ? 0.25690 0.26830 0.29530 -0.01650 0.01510  0.00710  237 PHE A O     
1838 C  CB    . PHE A 237 ? 0.32770 0.33520 0.36920 -0.00860 0.02200  0.01680  237 PHE A CB    
1839 C  CG    . PHE A 237 ? 0.24830 0.25260 0.29420 -0.00470 0.02590  0.02090  237 PHE A CG    
1840 C  CD1   . PHE A 237 ? 0.29530 0.30300 0.33870 -0.00140 0.02470  0.02230  237 PHE A CD1   
1841 C  CD2   . PHE A 237 ? 0.28590 0.28370 0.33910 -0.00400 0.03080  0.02390  237 PHE A CD2   
1842 C  CE1   . PHE A 237 ? 0.25900 0.26410 0.30720 0.00300  0.02790  0.02670  237 PHE A CE1   
1843 C  CE2   . PHE A 237 ? 0.29540 0.28930 0.35300 0.00030  0.03440  0.02870  237 PHE A CE2   
1844 C  CZ    . PHE A 237 ? 0.23490 0.23260 0.28990 0.00410  0.03270  0.03030  237 PHE A CZ    
1845 N  N     . THR A 238 ? 0.24790 0.26390 0.27690 -0.01480 0.01220  0.00720  238 THR A N     
1846 C  CA    . THR A 238 ? 0.29860 0.31760 0.32270 -0.01630 0.00820  0.00680  238 THR A CA    
1847 C  C     . THR A 238 ? 0.29640 0.31840 0.31710 -0.01390 0.00760  0.01070  238 THR A C     
1848 O  O     . THR A 238 ? 0.31860 0.34140 0.33990 -0.01110 0.00950  0.01350  238 THR A O     
1849 C  CB    . THR A 238 ? 0.33230 0.35280 0.35150 -0.01870 0.00550  0.00330  238 THR A CB    
1850 O  OG1   . THR A 238 ? 0.49600 0.51810 0.51210 -0.02010 0.00190  0.00320  238 THR A OG1   
1851 C  CG2   . THR A 238 ? 0.32850 0.35140 0.34420 -0.01750 0.00580  0.00430  238 THR A CG2   
1852 N  N     . SER A 239 ? 0.28100 0.30500 0.29860 -0.01480 0.00480  0.01060  239 SER A N     
1853 C  CA    . SER A 239 ? 0.31680 0.34430 0.33090 -0.01320 0.00380  0.01260  239 SER A CA    
1854 C  C     . SER A 239 ? 0.27060 0.29990 0.28090 -0.01470 0.00140  0.01090  239 SER A C     
1855 O  O     . SER A 239 ? 0.30150 0.32940 0.31040 -0.01700 -0.00050 0.00910  239 SER A O     
1856 C  CB    . SER A 239 ? 0.33990 0.36810 0.35420 -0.01300 0.00330  0.01320  239 SER A CB    
1857 O  OG    . SER A 239 ? 0.29920 0.33100 0.30990 -0.01190 0.00230  0.01380  239 SER A OG    
1858 N  N     . TYR A 240 ? 0.34370 0.37660 0.35260 -0.01330 0.00140  0.01170  240 TYR A N     
1859 C  CA    . TYR A 240 ? 0.26110 0.29650 0.26770 -0.01490 -0.00010 0.01020  240 TYR A CA    
1860 C  C     . TYR A 240 ? 0.22530 0.26200 0.23040 -0.01580 -0.00210 0.00950  240 TYR A C     
1861 O  O     . TYR A 240 ? 0.25770 0.29470 0.26160 -0.01800 -0.00310 0.00820  240 TYR A O     
1862 C  CB    . TYR A 240 ? 0.24740 0.28740 0.25530 -0.01300 0.00080  0.01070  240 TYR A CB    
1863 C  CG    . TYR A 240 ? 0.28560 0.32460 0.29630 -0.01190 0.00320  0.01060  240 TYR A CG    
1864 C  CD1   . TYR A 240 ? 0.33030 0.36420 0.34200 -0.01290 0.00460  0.00960  240 TYR A CD1   
1865 C  CD2   . TYR A 240 ? 0.23780 0.28120 0.25110 -0.00980 0.00400  0.01100  240 TYR A CD2   
1866 C  CE1   . TYR A 240 ? 0.26370 0.29620 0.27870 -0.01200 0.00720  0.00860  240 TYR A CE1   
1867 C  CE2   . TYR A 240 ? 0.29140 0.33370 0.30840 -0.00840 0.00660  0.01060  240 TYR A CE2   
1868 C  CZ    . TYR A 240 ? 0.28690 0.32330 0.30470 -0.00960 0.00840  0.00920  240 TYR A CZ    
1869 O  OH    . TYR A 240 ? 0.22360 0.25840 0.24580 -0.00830 0.01140  0.00790  240 TYR A OH    
1870 N  N     . ILE A 241 ? 0.31130 0.34850 0.31660 -0.01430 -0.00200 0.01030  241 ILE A N     
1871 C  CA    . ILE A 241 ? 0.31590 0.35530 0.32030 -0.01460 -0.00330 0.00880  241 ILE A CA    
1872 C  C     . ILE A 241 ? 0.30970 0.34670 0.31500 -0.01440 -0.00320 0.00860  241 ILE A C     
1873 O  O     . ILE A 241 ? 0.27830 0.31290 0.28540 -0.01380 -0.00210 0.00990  241 ILE A O     
1874 C  CB    . ILE A 241 ? 0.27560 0.32140 0.27870 -0.01230 -0.00320 0.00900  241 ILE A CB    
1875 C  CG1   . ILE A 241 ? 0.30580 0.35230 0.30850 -0.00910 -0.00120 0.01240  241 ILE A CG1   
1876 C  CG2   . ILE A 241 ? 0.31410 0.36380 0.31800 -0.01250 -0.00370 0.00860  241 ILE A CG2   
1877 C  CD1   . ILE A 241 ? 0.33400 0.38730 0.33380 -0.00630 -0.00140 0.01340  241 ILE A CD1   
1878 N  N     . ASP A 242 ? 0.42710 0.46510 0.43240 -0.01490 -0.00410 0.00630  242 ASP A N     
1879 C  CA    . ASP A 242 ? 0.39530 0.43230 0.40220 -0.01420 -0.00360 0.00530  242 ASP A CA    
1880 C  C     . ASP A 242 ? 0.37610 0.41700 0.38130 -0.01180 -0.00130 0.00660  242 ASP A C     
1881 O  O     . ASP A 242 ? 0.38530 0.43140 0.38730 -0.01060 -0.00120 0.00620  242 ASP A O     
1882 C  CB    . ASP A 242 ? 0.41890 0.45600 0.42670 -0.01540 -0.00470 0.00180  242 ASP A CB    
1883 C  CG    . ASP A 242 ? 0.31540 0.35050 0.32650 -0.01470 -0.00410 0.00020  242 ASP A CG    
1884 O  OD1   . ASP A 242 ? 0.35960 0.39550 0.37170 -0.01320 -0.00240 0.00130  242 ASP A OD1   
1885 O  OD2   . ASP A 242 ? 0.36680 0.39930 0.38040 -0.01580 -0.00500 -0.00220 242 ASP A OD2   
1886 N  N     . LEU A 243 ? 0.25670 0.29580 0.26430 -0.01100 0.00070  0.00840  243 LEU A N     
1887 C  CA    . LEU A 243 ? 0.31650 0.35820 0.32250 -0.00890 0.00390  0.01090  243 LEU A CA    
1888 C  C     . LEU A 243 ? 0.26690 0.31190 0.27160 -0.00790 0.00570  0.00910  243 LEU A C     
1889 O  O     . LEU A 243 ? 0.33890 0.38600 0.34180 -0.00630 0.00890  0.01160  243 LEU A O     
1890 C  CB    . LEU A 243 ? 0.31140 0.34940 0.32170 -0.00910 0.00610  0.01350  243 LEU A CB    
1891 C  CG    . LEU A 243 ? 0.26260 0.29790 0.27380 -0.00970 0.00530  0.01490  243 LEU A CG    
1892 C  CD1   . LEU A 243 ? 0.24800 0.27960 0.26470 -0.01060 0.00730  0.01570  243 LEU A CD1   
1893 C  CD2   . LEU A 243 ? 0.39060 0.42850 0.39820 -0.00740 0.00610  0.01770  243 LEU A CD2   
1894 N  N     . LEU A 244 ? 0.25730 0.30240 0.26310 -0.00900 0.00400  0.00480  244 LEU A N     
1895 C  CA    . LEU A 244 ? 0.29060 0.33870 0.29600 -0.00830 0.00580  0.00150  244 LEU A CA    
1896 C  C     . LEU A 244 ? 0.28600 0.34090 0.28400 -0.00660 0.00690  0.00130  244 LEU A C     
1897 O  O     . LEU A 244 ? 0.34310 0.40140 0.33870 -0.00530 0.01010  0.00100  244 LEU A O     
1898 C  CB    . LEU A 244 ? 0.22680 0.27260 0.23580 -0.00970 0.00370  -0.00340 244 LEU A CB    
1899 C  CG    . LEU A 244 ? 0.30060 0.34900 0.31060 -0.00910 0.00570  -0.00830 244 LEU A CG    
1900 C  CD1   . LEU A 244 ? 0.22740 0.27580 0.24140 -0.00800 0.00910  -0.00730 244 LEU A CD1   
1901 C  CD2   . LEU A 244 ? 0.27770 0.32210 0.29280 -0.01050 0.00360  -0.01270 244 LEU A CD2   
1902 N  N     . TYR A 245 ? 0.27840 0.33610 0.27280 -0.00670 0.00420  0.00120  245 TYR A N     
1903 C  CA    . TYR A 245 ? 0.25370 0.31950 0.24160 -0.00540 0.00330  -0.00080 245 TYR A CA    
1904 C  C     . TYR A 245 ? 0.28750 0.35750 0.26950 -0.00230 0.00520  0.00520  245 TYR A C     
1905 O  O     . TYR A 245 ? 0.22880 0.29440 0.21280 -0.00140 0.00670  0.01070  245 TYR A O     
1906 C  CB    . TYR A 245 ? 0.31350 0.38100 0.30250 -0.00710 -0.00050 -0.00390 245 TYR A CB    
1907 C  CG    . TYR A 245 ? 0.34150 0.40380 0.33630 -0.01020 -0.00160 -0.00880 245 TYR A CG    
1908 C  CD1   . TYR A 245 ? 0.35040 0.41440 0.34600 -0.01110 -0.00110 -0.01510 245 TYR A CD1   
1909 C  CD2   . TYR A 245 ? 0.38020 0.43560 0.37970 -0.01190 -0.00260 -0.00690 245 TYR A CD2   
1910 C  CE1   . TYR A 245 ? 0.41250 0.47050 0.41440 -0.01350 -0.00170 -0.01900 245 TYR A CE1   
1911 C  CE2   . TYR A 245 ? 0.43000 0.48000 0.43450 -0.01430 -0.00340 -0.01010 245 TYR A CE2   
1912 C  CZ    . TYR A 245 ? 0.42200 0.47280 0.42830 -0.01490 -0.00290 -0.01580 245 TYR A CZ    
1913 O  OH    . TYR A 245 ? 0.49250 0.53700 0.50460 -0.01680 -0.00340 -0.01830 245 TYR A OH    
1914 N  N     . PRO A 246 ? 0.23710 0.31540 0.21150 -0.00030 0.00520  0.00430  246 PRO A N     
1915 C  CA    . PRO A 246 ? 0.26040 0.34280 0.22810 0.00330  0.00690  0.01110  246 PRO A CA    
1916 C  C     . PRO A 246 ? 0.29150 0.37510 0.25960 0.00500  0.00390  0.01540  246 PRO A C     
1917 O  O     . PRO A 246 ? 0.27900 0.36160 0.25190 0.00300  0.00070  0.01210  246 PRO A O     
1918 C  CB    . PRO A 246 ? 0.31900 0.41130 0.27770 0.00470  0.00680  0.00780  246 PRO A CB    
1919 C  CG    . PRO A 246 ? 0.31840 0.41300 0.28010 0.00170  0.00340  -0.00170 246 PRO A CG    
1920 C  CD    . PRO A 246 ? 0.26510 0.34940 0.23680 -0.00140 0.00380  -0.00340 246 PRO A CD    
1921 N  N     . THR A 247 ? 0.26630 0.35210 0.22980 0.00880  0.00550  0.02290  247 THR A N     
1922 C  CA    . THR A 247 ? 0.31460 0.39980 0.28020 0.01120  0.00390  0.02820  247 THR A CA    
1923 C  C     . THR A 247 ? 0.31840 0.41190 0.28390 0.01170  -0.00160 0.02460  247 THR A C     
1924 O  O     . THR A 247 ? 0.35400 0.44500 0.32560 0.01120  -0.00320 0.02500  247 THR A O     
1925 C  CB    . THR A 247 ? 0.31010 0.39580 0.27080 0.01580  0.00710  0.03750  247 THR A CB    
1926 O  OG1   . THR A 247 ? 0.33070 0.40800 0.29410 0.01450  0.01280  0.04040  247 THR A OG1   
1927 C  CG2   . THR A 247 ? 0.33040 0.41490 0.29460 0.01890  0.00580  0.04320  247 THR A CG2   
1928 N  N     . GLU A 248 ? 0.28080 0.38450 0.23980 0.01230  -0.00420 0.02060  248 GLU A N     
1929 C  CA    . GLU A 248 ? 0.35830 0.47140 0.31820 0.01230  -0.00960 0.01630  248 GLU A CA    
1930 C  C     . GLU A 248 ? 0.32470 0.43380 0.29310 0.00720  -0.01120 0.00890  248 GLU A C     
1931 O  O     . GLU A 248 ? 0.34700 0.45920 0.32040 0.00670  -0.01400 0.00770  248 GLU A O     
1932 C  CB    . GLU A 248 ? 0.38600 0.51210 0.33700 0.01380  -0.01240 0.01270  248 GLU A CB    
1933 C  CG    . GLU A 248 ? 0.48450 0.61130 0.43360 0.01000  -0.01160 0.00380  248 GLU A CG    
1934 C  CD    . GLU A 248 ? 0.50370 0.64460 0.44360 0.01140  -0.01460 -0.00090 248 GLU A CD    
1935 O  OE1   . GLU A 248 ? 0.50530 0.65610 0.43910 0.01590  -0.01750 0.00380  248 GLU A OE1   
1936 O  OE2   . GLU A 248 ? 0.36990 0.51230 0.30890 0.00830  -0.01400 -0.00970 248 GLU A OE2   
1937 N  N     . ASP A 249 ? 0.30120 0.40330 0.27170 0.00350  -0.00890 0.00470  249 ASP A N     
1938 C  CA    . ASP A 249 ? 0.28190 0.37840 0.25990 -0.00110 -0.00970 -0.00080 249 ASP A CA    
1939 C  C     . ASP A 249 ? 0.28770 0.37600 0.27150 -0.00170 -0.00870 0.00330  249 ASP A C     
1940 O  O     . ASP A 249 ? 0.39110 0.47910 0.37990 -0.00420 -0.01040 0.00080  249 ASP A O     
1941 C  CB    . ASP A 249 ? 0.29590 0.38670 0.27480 -0.00380 -0.00740 -0.00530 249 ASP A CB    
1942 C  CG    . ASP A 249 ? 0.34700 0.44580 0.32150 -0.00420 -0.00840 -0.01210 249 ASP A CG    
1943 O  OD1   . ASP A 249 ? 0.42490 0.53440 0.39480 -0.00250 -0.01120 -0.01330 249 ASP A OD1   
1944 O  OD2   . ASP A 249 ? 0.44360 0.53850 0.41970 -0.00610 -0.00650 -0.01680 249 ASP A OD2   
1945 N  N     . ARG A 250 ? 0.27920 0.36140 0.26250 0.00020  -0.00570 0.00930  250 ARG A N     
1946 C  CA    . ARG A 250 ? 0.26880 0.34350 0.25720 -0.00030 -0.00440 0.01270  250 ARG A CA    
1947 C  C     . ARG A 250 ? 0.28770 0.36730 0.27780 0.00190  -0.00620 0.01490  250 ARG A C     
1948 O  O     . ARG A 250 ? 0.28140 0.35880 0.27630 -0.00030 -0.00680 0.01310  250 ARG A O     
1949 C  CB    . ARG A 250 ? 0.26330 0.33160 0.25150 0.00120  -0.00060 0.01790  250 ARG A CB    
1950 C  CG    . ARG A 250 ? 0.26200 0.32580 0.25070 -0.00090 0.00140  0.01570  250 ARG A CG    
1951 C  CD    . ARG A 250 ? 0.21070 0.26720 0.20270 -0.00090 0.00480  0.01950  250 ARG A CD    
1952 N  NE    . ARG A 250 ? 0.24240 0.29950 0.23220 0.00260  0.00760  0.02580  250 ARG A NE    
1953 C  CZ    . ARG A 250 ? 0.24480 0.30470 0.22990 0.00470  0.01030  0.02890  250 ARG A CZ    
1954 N  NH1   . ARG A 250 ? 0.24320 0.30620 0.22530 0.00370  0.01070  0.02520  250 ARG A NH1   
1955 N  NH2   . ARG A 250 ? 0.28280 0.34220 0.26630 0.00790  0.01300  0.03580  250 ARG A NH2   
1956 N  N     . ASN A 251 ? 0.26560 0.35220 0.25180 0.00630  -0.00690 0.01880  251 ASN A N     
1957 C  CA    A ASN A 251 ? 0.29730 0.38940 0.28630 0.00930  -0.00880 0.02130  251 ASN A CA    
1958 C  CA    B ASN A 251 ? 0.29730 0.38940 0.28630 0.00930  -0.00880 0.02130  251 ASN A CA    
1959 C  C     . ASN A 251 ? 0.28290 0.38390 0.27480 0.00750  -0.01280 0.01540  251 ASN A C     
1960 O  O     . ASN A 251 ? 0.33700 0.44040 0.33440 0.00820  -0.01370 0.01580  251 ASN A O     
1961 C  CB    A ASN A 251 ? 0.34580 0.44250 0.33010 0.01520  -0.00860 0.02840  251 ASN A CB    
1962 C  CB    B ASN A 251 ? 0.34580 0.44250 0.33010 0.01520  -0.00860 0.02840  251 ASN A CB    
1963 C  CG    A ASN A 251 ? 0.66510 0.75200 0.65180 0.01730  -0.00420 0.03530  251 ASN A CG    
1964 C  CG    B ASN A 251 ? 0.66510 0.75200 0.65180 0.01730  -0.00420 0.03530  251 ASN A CG    
1965 O  OD1   A ASN A 251 ? 0.71990 0.80150 0.71330 0.01690  -0.00310 0.03570  251 ASN A OD1   
1966 O  OD1   B ASN A 251 ? 0.71990 0.80150 0.71330 0.01690  -0.00310 0.03570  251 ASN A OD1   
1967 N  ND2   A ASN A 251 ? 0.57020 0.65450 0.55180 0.01920  -0.00120 0.04010  251 ASN A ND2   
1968 N  ND2   B ASN A 251 ? 0.57020 0.65450 0.55180 0.01920  -0.00120 0.04010  251 ASN A ND2   
1969 N  N     . ASP A 252 ? 0.27860 0.38420 0.26770 0.00480  -0.01470 0.00950  252 ASP A N     
1970 C  CA    . ASP A 252 ? 0.30970 0.42220 0.30330 0.00150  -0.01780 0.00260  252 ASP A CA    
1971 C  C     . ASP A 252 ? 0.28650 0.39120 0.28710 -0.00270 -0.01610 0.00080  252 ASP A C     
1972 O  O     . ASP A 252 ? 0.26230 0.37150 0.26860 -0.00360 -0.01720 -0.00100 252 ASP A O     
1973 C  CB    . ASP A 252 ? 0.41670 0.53260 0.40690 -0.00120 -0.01900 -0.00410 252 ASP A CB    
1974 C  CG    . ASP A 252 ? 0.55040 0.67200 0.54650 -0.00550 -0.02150 -0.01210 252 ASP A CG    
1975 O  OD1   . ASP A 252 ? 0.52330 0.63700 0.52420 -0.01020 -0.01980 -0.01530 252 ASP A OD1   
1976 O  OD2   . ASP A 252 ? 0.48120 0.61560 0.47730 -0.00430 -0.02530 -0.01510 252 ASP A OD2   
1977 N  N     . ARG A 253 ? 0.24780 0.34140 0.24770 -0.00500 -0.01320 0.00140  253 ARG A N     
1978 C  CA    . ARG A 253 ? 0.30020 0.38570 0.30460 -0.00890 -0.01150 0.00030  253 ARG A CA    
1979 C  C     . ARG A 253 ? 0.23910 0.32260 0.24610 -0.00700 -0.01000 0.00440  253 ARG A C     
1980 O  O     . ARG A 253 ? 0.28400 0.36810 0.29550 -0.00930 -0.00970 0.00260  253 ARG A O     
1981 C  CB    . ARG A 253 ? 0.29080 0.36660 0.29330 -0.01100 -0.00970 0.00010  253 ARG A CB    
1982 C  CG    . ARG A 253 ? 0.53400 0.60190 0.53950 -0.01470 -0.00850 -0.00040 253 ARG A CG    
1983 C  CD    . ARG A 253 ? 0.73540 0.80530 0.74480 -0.01870 -0.00920 -0.00470 253 ARG A CD    
1984 N  NE    . ARG A 253 ? 1.20970 1.27510 1.21970 -0.02150 -0.00920 -0.00790 253 ARG A NE    
1985 C  CZ    . ARG A 253 ? 1.10940 1.16560 1.11930 -0.02310 -0.00810 -0.00650 253 ARG A CZ    
1986 N  NH1   . ARG A 253 ? 1.29050 1.34170 1.29890 -0.02260 -0.00710 -0.00240 253 ARG A NH1   
1987 N  NH2   . ARG A 253 ? 1.11690 1.16930 1.12860 -0.02510 -0.00810 -0.00930 253 ARG A NH2   
1988 N  N     . LEU A 254 ? 0.24840 0.32960 0.25330 -0.00310 -0.00860 0.00950  254 LEU A N     
1989 C  CA    . LEU A 254 ? 0.21870 0.29700 0.22700 -0.00100 -0.00670 0.01290  254 LEU A CA    
1990 C  C     . LEU A 254 ? 0.29950 0.38680 0.31240 0.00130  -0.00820 0.01280  254 LEU A C     
1991 O  O     . LEU A 254 ? 0.23020 0.31630 0.24800 0.00050  -0.00670 0.01200  254 LEU A O     
1992 C  CB    . LEU A 254 ? 0.23340 0.30700 0.23970 0.00260  -0.00450 0.01840  254 LEU A CB    
1993 C  CG    . LEU A 254 ? 0.25990 0.32440 0.26410 0.00040  -0.00240 0.01860  254 LEU A CG    
1994 C  CD1   . LEU A 254 ? 0.25030 0.31150 0.25360 0.00380  0.00020  0.02410  254 LEU A CD1   
1995 C  CD2   . LEU A 254 ? 0.27150 0.32930 0.27860 -0.00320 -0.00110 0.01630  254 LEU A CD2   
1996 N  N     . ARG A 255 ? 0.23650 0.33360 0.24790 0.00440  -0.01120 0.01330  255 ARG A N     
1997 C  CA    . ARG A 255 ? 0.30680 0.41520 0.32340 0.00710  -0.01380 0.01280  255 ARG A CA    
1998 C  C     . ARG A 255 ? 0.30180 0.41390 0.32400 0.00210  -0.01440 0.00640  255 ARG A C     
1999 O  O     . ARG A 255 ? 0.39970 0.51510 0.42880 0.00270  -0.01360 0.00600  255 ARG A O     
2000 C  CB    . ARG A 255 ? 0.30120 0.42070 0.31360 0.01080  -0.01790 0.01360  255 ARG A CB    
2001 C  CG    . ARG A 255 ? 0.47730 0.59660 0.48580 0.01730  -0.01740 0.02160  255 ARG A CG    
2002 C  CD    . ARG A 255 ? 0.46800 0.60010 0.47120 0.02090  -0.02200 0.02220  255 ARG A CD    
2003 N  NE    . ARG A 255 ? 0.64840 0.77850 0.64430 0.02610  -0.02080 0.03020  255 ARG A NE    
2004 C  CZ    . ARG A 255 ? 0.86480 1.00100 0.85130 0.02780  -0.02260 0.03120  255 ARG A CZ    
2005 N  NH1   . ARG A 255 ? 0.84930 0.99410 0.83300 0.02450  -0.02600 0.02360  255 ARG A NH1   
2006 N  NH2   . ARG A 255 ? 1.06660 1.20010 1.04670 0.03250  -0.02060 0.03950  255 ARG A NH2   
2007 N  N     . ASP A 256 ? 0.35580 0.46700 0.37580 -0.00270 -0.01520 0.00170  256 ASP A N     
2008 C  CA    . ASP A 256 ? 0.35730 0.47150 0.38300 -0.00790 -0.01540 -0.00410 256 ASP A CA    
2009 C  C     . ASP A 256 ? 0.33970 0.44570 0.36840 -0.01110 -0.01150 -0.00380 256 ASP A C     
2010 O  O     . ASP A 256 ? 0.35350 0.46420 0.38870 -0.01330 -0.01060 -0.00640 256 ASP A O     
2011 C  CB    . ASP A 256 ? 0.48980 0.60270 0.51280 -0.01200 -0.01640 -0.00890 256 ASP A CB    
2012 C  CG    . ASP A 256 ? 0.39030 0.50750 0.42030 -0.01740 -0.01670 -0.01510 256 ASP A CG    
2013 O  OD1   . ASP A 256 ? 0.66770 0.79650 0.70400 -0.01680 -0.01870 -0.01750 256 ASP A OD1   
2014 O  OD2   . ASP A 256 ? 0.73510 0.84440 0.76520 -0.02210 -0.01480 -0.01740 256 ASP A OD2   
2015 N  N     . SER A 257 ? 0.29370 0.38830 0.31760 -0.01150 -0.00900 -0.00090 257 SER A N     
2016 C  CA    . SER A 257 ? 0.39880 0.48540 0.42330 -0.01490 -0.00570 -0.00090 257 SER A CA    
2017 C  C     . SER A 257 ? 0.33180 0.41650 0.35800 -0.01220 -0.00320 0.00170  257 SER A C     
2018 O  O     . SER A 257 ? 0.32020 0.40370 0.34890 -0.01460 -0.00050 0.00040  257 SER A O     
2019 C  CB    . SER A 257 ? 0.42300 0.49930 0.44190 -0.01730 -0.00500 -0.00020 257 SER A CB    
2020 O  OG    . SER A 257 ? 0.38240 0.45920 0.40110 -0.02040 -0.00640 -0.00330 257 SER A OG    
2021 N  N     . TYR A 258 ? 0.37330 0.45720 0.39840 -0.00730 -0.00350 0.00540  258 TYR A N     
2022 C  CA    . TYR A 258 ? 0.30840 0.38800 0.33550 -0.00450 -0.00060 0.00780  258 TYR A CA    
2023 C  C     . TYR A 258 ? 0.25960 0.34600 0.29160 0.00140  -0.00140 0.01060  258 TYR A C     
2024 O  O     . TYR A 258 ? 0.29010 0.37300 0.32550 0.00410  0.00130  0.01230  258 TYR A O     
2025 C  CB    . TYR A 258 ? 0.30520 0.37480 0.32730 -0.00470 0.00060  0.01000  258 TYR A CB    
2026 C  CG    . TYR A 258 ? 0.34370 0.40750 0.36160 -0.00970 0.00070  0.00780  258 TYR A CG    
2027 C  CD1   . TYR A 258 ? 0.35860 0.41930 0.37630 -0.01310 0.00270  0.00570  258 TYR A CD1   
2028 C  CD2   . TYR A 258 ? 0.35620 0.41800 0.37010 -0.01080 -0.00120 0.00800  258 TYR A CD2   
2029 C  CE1   . TYR A 258 ? 0.39960 0.45510 0.41290 -0.01710 0.00240  0.00480  258 TYR A CE1   
2030 C  CE2   . TYR A 258 ? 0.35830 0.41470 0.36930 -0.01470 -0.00130 0.00660  258 TYR A CE2   
2031 C  CZ    . TYR A 258 ? 0.34830 0.40150 0.35880 -0.01770 0.00020  0.00550  258 TYR A CZ    
2032 O  OH    . TYR A 258 ? 0.48160 0.52960 0.48880 -0.02090 -0.00030 0.00510  258 TYR A OH    
2033 N  N     . PHE A 259 ? 0.27920 0.37530 0.31180 0.00350  -0.00500 0.01070  259 PHE A N     
2034 C  CA    . PHE A 259 ? 0.29480 0.39980 0.33260 0.00950  -0.00670 0.01350  259 PHE A CA    
2035 C  C     . PHE A 259 ? 0.30320 0.40290 0.34000 0.01520  -0.00530 0.01990  259 PHE A C     
2036 O  O     . PHE A 259 ? 0.27460 0.37550 0.31770 0.01960  -0.00400 0.02240  259 PHE A O     
2037 C  CB    . PHE A 259 ? 0.39440 0.50510 0.44150 0.00930  -0.00520 0.01050  259 PHE A CB    
2038 C  CG    . PHE A 259 ? 0.34350 0.45980 0.39270 0.00350  -0.00600 0.00470  259 PHE A CG    
2039 C  CD1   . PHE A 259 ? 0.39750 0.52630 0.44990 0.00380  -0.01020 0.00220  259 PHE A CD1   
2040 C  CD2   . PHE A 259 ? 0.34140 0.45050 0.38920 -0.00230 -0.00250 0.00170  259 PHE A CD2   
2041 C  CE1   . PHE A 259 ? 0.42040 0.55370 0.47610 -0.00210 -0.01030 -0.00340 259 PHE A CE1   
2042 C  CE2   . PHE A 259 ? 0.46020 0.57330 0.51020 -0.00780 -0.00250 -0.00280 259 PHE A CE2   
2043 C  CZ    . PHE A 259 ? 0.43730 0.56210 0.49200 -0.00790 -0.00620 -0.00550 259 PHE A CZ    
2044 N  N     . PHE A 260 ? 0.29870 0.39220 0.32810 0.01500  -0.00510 0.02260  260 PHE A N     
2045 C  CA    . PHE A 260 ? 0.31610 0.40480 0.34410 0.02000  -0.00360 0.02940  260 PHE A CA    
2046 C  C     . PHE A 260 ? 0.25650 0.34530 0.27590 0.02010  -0.00500 0.03180  260 PHE A C     
2047 O  O     . PHE A 260 ? 0.30010 0.38910 0.31510 0.01560  -0.00620 0.02750  260 PHE A O     
2048 C  CB    . PHE A 260 ? 0.32560 0.40210 0.35650 0.01890  0.00130  0.02990  260 PHE A CB    
2049 C  CG    . PHE A 260 ? 0.27340 0.34160 0.29900 0.01380  0.00270  0.02770  260 PHE A CG    
2050 C  CD1   . PHE A 260 ? 0.35800 0.42440 0.38290 0.00820  0.00270  0.02200  260 PHE A CD1   
2051 C  CD2   . PHE A 260 ? 0.26600 0.32840 0.28780 0.01480  0.00410  0.03170  260 PHE A CD2   
2052 C  CE1   . PHE A 260 ? 0.32410 0.38360 0.34470 0.00410  0.00330  0.02040  260 PHE A CE1   
2053 C  CE2   . PHE A 260 ? 0.27180 0.32770 0.29020 0.01030  0.00520  0.02940  260 PHE A CE2   
2054 C  CZ    . PHE A 260 ? 0.28480 0.33950 0.30280 0.00530  0.00440  0.02380  260 PHE A CZ    
2055 N  N     . THR A 261 ? 0.22770 0.31600 0.24510 0.02550  -0.00430 0.03880  261 THR A N     
2056 C  CA    . THR A 261 ? 0.30330 0.39100 0.31230 0.02630  -0.00430 0.04230  261 THR A CA    
2057 C  C     . THR A 261 ? 0.26710 0.34200 0.27670 0.02620  0.00090  0.04640  261 THR A C     
2058 O  O     . THR A 261 ? 0.30040 0.37060 0.31500 0.03000  0.00360  0.05140  261 THR A O     
2059 C  CB    . THR A 261 ? 0.37270 0.47020 0.37790 0.03280  -0.00720 0.04840  261 THR A CB    
2060 O  OG1   . THR A 261 ? 0.35480 0.46540 0.36130 0.03300  -0.01250 0.04380  261 THR A OG1   
2061 C  CG2   . THR A 261 ? 0.40790 0.50540 0.40290 0.03330  -0.00660 0.05160  261 THR A CG2   
2062 N  N     . CYS A 262 ? 0.31910 0.38870 0.32470 0.02180  0.00240  0.04390  262 CYS A N     
2063 C  CA    . CYS A 262 ? 0.34550 0.40410 0.35280 0.02050  0.00720  0.04620  262 CYS A CA    
2064 C  C     . CYS A 262 ? 0.33550 0.39270 0.33970 0.02490  0.00990  0.05470  262 CYS A C     
2065 O  O     . CYS A 262 ? 0.45210 0.51690 0.44880 0.02740  0.00790  0.05740  262 CYS A O     
2066 C  CB    . CYS A 262 ? 0.31000 0.36560 0.31470 0.01490  0.00730  0.04090  262 CYS A CB    
2067 S  SG    . CYS A 262 ? 0.30190 0.34580 0.31090 0.01230  0.01230  0.04170  262 CYS A SG    
2068 N  N     . GLU A 263 ? 0.42500 0.47240 0.43480 0.02580  0.01480  0.05870  263 GLU A N     
2069 C  CA    . GLU A 263 ? 0.37370 0.41720 0.38190 0.02970  0.01880  0.06760  263 GLU A CA    
2070 C  C     . GLU A 263 ? 0.34370 0.37670 0.35550 0.02590  0.02430  0.06760  263 GLU A C     
2071 O  O     . GLU A 263 ? 0.34980 0.37600 0.36450 0.02820  0.02920  0.07450  263 GLU A O     
2072 C  CB    . GLU A 263 ? 0.40440 0.44610 0.41830 0.03570  0.01990  0.07400  263 GLU A CB    
2073 C  CG    . GLU A 263 ? 0.56130 0.61510 0.57250 0.04040  0.01430  0.07520  263 GLU A CG    
2074 C  CD    . GLU A 263 ? 0.73570 0.78810 0.75410 0.04710  0.01520  0.08190  263 GLU A CD    
2075 O  OE1   . GLU A 263 ? 0.75110 0.79240 0.77520 0.04870  0.02080  0.08720  263 GLU A OE1   
2076 O  OE2   . GLU A 263 ? 0.78370 0.84610 0.80300 0.05090  0.01050  0.08170  263 GLU A OE2   
2077 N  N     . CYS A 264 ? 0.33970 0.37180 0.35170 0.02010  0.02340  0.06000  264 CYS A N     
2078 C  CA    . CYS A 264 ? 0.38120 0.40590 0.39690 0.01610  0.02760  0.05870  264 CYS A CA    
2079 C  C     . CYS A 264 ? 0.37300 0.39890 0.38290 0.01740  0.03080  0.06460  264 CYS A C     
2080 O  O     . CYS A 264 ? 0.36910 0.40240 0.37060 0.02110  0.02900  0.06860  264 CYS A O     
2081 C  CB    . CYS A 264 ? 0.38190 0.40740 0.39840 0.01050  0.02480  0.04980  264 CYS A CB    
2082 S  SG    . CYS A 264 ? 0.35150 0.38480 0.35940 0.00900  0.02170  0.04680  264 CYS A SG    
2083 N  N     . GLN A 265 ? 0.34120 0.36070 0.35590 0.01430  0.03580  0.06490  265 GLN A N     
2084 C  CA    . GLN A 265 ? 0.41840 0.43830 0.42880 0.01520  0.04040  0.07060  265 GLN A CA    
2085 C  C     . GLN A 265 ? 0.41120 0.44050 0.41150 0.01490  0.03730  0.06790  265 GLN A C     
2086 O  O     . GLN A 265 ? 0.33450 0.36850 0.32640 0.01810  0.03880  0.07360  265 GLN A O     
2087 C  CB    . GLN A 265 ? 0.44210 0.45420 0.46150 0.01090  0.04610  0.06960  265 GLN A CB    
2088 C  CG    . GLN A 265 ? 0.77620 0.78720 0.79290 0.01190  0.05270  0.07720  265 GLN A CG    
2089 C  CD    . GLN A 265 ? 0.80960 0.81310 0.83760 0.00740  0.05900  0.07620  265 GLN A CD    
2090 O  OE1   . GLN A 265 ? 0.89080 0.89390 0.92580 0.00270  0.05740  0.06790  265 GLN A OE1   
2091 N  NE2   . GLN A 265 ? 1.08140 1.07930 1.11140 0.00880  0.06640  0.08500  265 GLN A NE2   
2092 N  N     . GLU A 266 ? 0.30200 0.33410 0.30340 0.01120  0.03320  0.05910  266 GLU A N     
2093 C  CA    . GLU A 266 ? 0.29000 0.33020 0.28370 0.01060  0.03030  0.05500  266 GLU A CA    
2094 C  C     . GLU A 266 ? 0.31710 0.36580 0.30160 0.01450  0.02610  0.05660  266 GLU A C     
2095 O  O     . GLU A 266 ? 0.28640 0.34200 0.26240 0.01590  0.02610  0.05720  266 GLU A O     
2096 C  CB    . GLU A 266 ? 0.37390 0.41390 0.37190 0.00630  0.02670  0.04610  266 GLU A CB    
2097 C  CG    . GLU A 266 ? 0.66290 0.69800 0.66850 0.00250  0.02990  0.04350  266 GLU A CG    
2098 C  CD    . GLU A 266 ? 0.62480 0.66270 0.62780 0.00240  0.03410  0.04460  266 GLU A CD    
2099 O  OE1   . GLU A 266 ? 0.81690 0.86150 0.81100 0.00440  0.03330  0.04490  266 GLU A OE1   
2100 O  OE2   . GLU A 266 ? 0.76940 0.80360 0.77970 0.00010  0.03830  0.04460  266 GLU A OE2   
2101 N  N     . CYS A 267 ? 0.36520 0.41450 0.35190 0.01620  0.02250  0.05650  267 CYS A N     
2102 C  CA    . CYS A 267 ? 0.40670 0.46520 0.38680 0.01990  0.01800  0.05770  267 CYS A CA    
2103 C  C     . CYS A 267 ? 0.38370 0.44470 0.35760 0.02550  0.02030  0.06750  267 CYS A C     
2104 O  O     . CYS A 267 ? 0.36760 0.43830 0.33210 0.02830  0.01760  0.06860  267 CYS A O     
2105 C  CB    . CYS A 267 ? 0.31020 0.36880 0.29590 0.02010  0.01420  0.05500  267 CYS A CB    
2106 S  SG    . CYS A 267 ? 0.32290 0.38180 0.31170 0.01440  0.01060  0.04450  267 CYS A SG    
2107 N  N     . THR A 268 ? 0.29270 0.34490 0.27180 0.02710  0.02530  0.07450  268 THR A N     
2108 C  CA    . THR A 268 ? 0.34480 0.39710 0.31930 0.03270  0.02830  0.08540  268 THR A CA    
2109 C  C     . THR A 268 ? 0.33550 0.39120 0.30000 0.03300  0.03190  0.08910  268 THR A C     
2110 O  O     . THR A 268 ? 0.36360 0.42730 0.31770 0.03760  0.03070  0.09490  268 THR A O     
2111 C  CB    . THR A 268 ? 0.38350 0.42340 0.36820 0.03340  0.03390  0.09140  268 THR A CB    
2112 O  OG1   . THR A 268 ? 0.45340 0.49080 0.44660 0.03360  0.03100  0.08770  268 THR A OG1   
2113 C  CG2   . THR A 268 ? 0.51970 0.55820 0.50000 0.03960  0.03760  0.10410  268 THR A CG2   
2114 N  N     . THR A 269 ? 0.31240 0.36290 0.28050 0.02810  0.03650  0.08560  269 THR A N     
2115 C  CA    . THR A 269 ? 0.31580 0.36880 0.27630 0.02760  0.04130  0.08830  269 THR A CA    
2116 C  C     . THR A 269 ? 0.28510 0.34880 0.23690 0.02620  0.03750  0.08040  269 THR A C     
2117 O  O     . THR A 269 ? 0.36360 0.43370 0.30470 0.02790  0.03960  0.08330  269 THR A O     
2118 C  CB    . THR A 269 ? 0.30280 0.34650 0.27260 0.02290  0.04820  0.08730  269 THR A CB    
2119 O  OG1   . THR A 269 ? 0.27170 0.31500 0.24860 0.01780  0.04520  0.07640  269 THR A OG1   
2120 C  CG2   . THR A 269 ? 0.34230 0.37480 0.32220 0.02350  0.05280  0.09400  269 THR A CG2   
2121 N  N     . LYS A 270 ? 0.29270 0.35790 0.24920 0.02290  0.03220  0.07050  270 LYS A N     
2122 C  CA    . LYS A 270 ? 0.36080 0.43380 0.31230 0.02060  0.02910  0.06160  270 LYS A CA    
2123 C  C     . LYS A 270 ? 0.36530 0.43720 0.31620 0.01790  0.03490  0.05970  270 LYS A C     
2124 O  O     . LYS A 270 ? 0.44160 0.52110 0.38520 0.01760  0.03450  0.05510  270 LYS A O     
2125 C  CB    . LYS A 270 ? 0.34710 0.43220 0.28640 0.02440  0.02470  0.06210  270 LYS A CB    
2126 C  CG    . LYS A 270 ? 0.48610 0.57440 0.42690 0.02730  0.01870  0.06330  270 LYS A CG    
2127 C  CD    . LYS A 270 ? 0.53880 0.64090 0.46860 0.03070  0.01350  0.06260  270 LYS A CD    
2128 C  CE    . LYS A 270 ? 0.73330 0.83930 0.66730 0.03330  0.00740  0.06300  270 LYS A CE    
2129 N  NZ    . LYS A 270 ? 0.79570 0.91630 0.71960 0.03750  0.00210  0.06370  270 LYS A NZ    
2130 N  N     . ASP A 271 ? 0.35990 0.42280 0.31970 0.01580  0.04040  0.06250  271 ASP A N     
2131 C  CA    . ASP A 271 ? 0.41090 0.47290 0.37180 0.01360  0.04710  0.06230  271 ASP A CA    
2132 C  C     . ASP A 271 ? 0.39880 0.46440 0.36190 0.01030  0.04550  0.05190  271 ASP A C     
2133 O  O     . ASP A 271 ? 0.35790 0.42730 0.31770 0.00970  0.05010  0.05060  271 ASP A O     
2134 C  CB    . ASP A 271 ? 0.45230 0.50420 0.42480 0.01140  0.05290  0.06650  271 ASP A CB    
2135 C  CG    . ASP A 271 ? 0.48240 0.53140 0.45090 0.01430  0.05970  0.07800  271 ASP A CG    
2136 O  OD1   . ASP A 271 ? 0.42420 0.47940 0.37970 0.01840  0.05970  0.08370  271 ASP A OD1   
2137 O  OD2   . ASP A 271 ? 0.41560 0.45620 0.39410 0.01230  0.06520  0.08160  271 ASP A OD2   
2138 N  N     . LYS A 272 ? 0.27680 0.34110 0.24580 0.00830  0.03950  0.04490  272 LYS A N     
2139 C  CA    . LYS A 272 ? 0.33480 0.40130 0.30720 0.00560  0.03740  0.03550  272 LYS A CA    
2140 C  C     . LYS A 272 ? 0.34260 0.41720 0.30650 0.00660  0.03280  0.02960  272 LYS A C     
2141 O  O     . LYS A 272 ? 0.33310 0.40920 0.29990 0.00460  0.03180  0.02180  272 LYS A O     
2142 C  CB    . LYS A 272 ? 0.33990 0.39990 0.32370 0.00280  0.03380  0.03150  272 LYS A CB    
2143 C  CG    . LYS A 272 ? 0.29600 0.34950 0.29020 0.00060  0.03810  0.03350  272 LYS A CG    
2144 C  CD    . LYS A 272 ? 0.42670 0.47610 0.43060 -0.00220 0.03390  0.02800  272 LYS A CD    
2145 C  CE    . LYS A 272 ? 0.43670 0.48190 0.45180 -0.00460 0.03730  0.02830  272 LYS A CE    
2146 N  NZ    . LYS A 272 ? 0.38860 0.43200 0.41180 -0.00690 0.03270  0.02240  272 LYS A NZ    
2147 N  N     . ASP A 273 ? 0.30370 0.38380 0.25840 0.00960  0.03010  0.03300  273 ASP A N     
2148 C  CA    . ASP A 273 ? 0.38930 0.47800 0.33680 0.01020  0.02520  0.02680  273 ASP A CA    
2149 C  C     . ASP A 273 ? 0.37240 0.46740 0.31430 0.00960  0.02780  0.02070  273 ASP A C     
2150 O  O     . ASP A 273 ? 0.31310 0.41070 0.25680 0.00760  0.02480  0.01160  273 ASP A O     
2151 C  CB    . ASP A 273 ? 0.33210 0.42750 0.27060 0.01410  0.02200  0.03230  273 ASP A CB    
2152 C  CG    . ASP A 273 ? 0.42040 0.51280 0.36490 0.01430  0.01700  0.03340  273 ASP A CG    
2153 O  OD1   . ASP A 273 ? 0.36990 0.45370 0.32460 0.01160  0.01690  0.03200  273 ASP A OD1   
2154 O  OD2   . ASP A 273 ? 0.47710 0.57650 0.41610 0.01730  0.01300  0.03560  273 ASP A OD2   
2155 N  N     . LYS A 274 ? 0.27440 0.37170 0.21010 0.01110  0.03400  0.02560  274 LYS A N     
2156 C  CA    . LYS A 274 ? 0.32430 0.42870 0.25310 0.01090  0.03760  0.02010  274 LYS A CA    
2157 C  C     . LYS A 274 ? 0.25060 0.35100 0.19010 0.00760  0.03980  0.01180  274 LYS A C     
2158 O  O     . LYS A 274 ? 0.23070 0.33610 0.16840 0.00670  0.03920  0.00280  274 LYS A O     
2159 C  CB    . LYS A 274 ? 0.46840 0.57550 0.38780 0.01330  0.04460  0.02860  274 LYS A CB    
2160 C  CG    . LYS A 274 ? 0.57520 0.68830 0.48190 0.01760  0.04240  0.03700  274 LYS A CG    
2161 C  CD    . LYS A 274 ? 0.89320 1.01920 0.78680 0.01920  0.03820  0.03080  274 LYS A CD    
2162 C  CE    . LYS A 274 ? 0.80640 0.93920 0.68880 0.02390  0.03400  0.03900  274 LYS A CE    
2163 N  NZ    . LYS A 274 ? 1.08630 1.21830 0.96020 0.02730  0.04040  0.05190  274 LYS A NZ    
2164 N  N     . ALA A 275 ? 0.30690 0.39850 0.25830 0.00590  0.04210  0.01440  275 ALA A N     
2165 C  CA    . ALA A 275 ? 0.29290 0.38090 0.25610 0.00330  0.04330  0.00740  275 ALA A CA    
2166 C  C     . ALA A 275 ? 0.33160 0.41770 0.30000 0.00190  0.03650  -0.00020 275 ALA A C     
2167 O  O     . ALA A 275 ? 0.30300 0.38940 0.27650 0.00070  0.03680  -0.00810 275 ALA A O     
2168 C  CB    . ALA A 275 ? 0.31660 0.39690 0.29140 0.00190  0.04630  0.01210  275 ALA A CB    
2169 N  N     . LYS A 276 ? 0.38220 0.46620 0.34960 0.00200  0.03100  0.00240  276 LYS A N     
2170 C  CA    . LYS A 276 ? 0.30890 0.39070 0.28120 0.00030  0.02510  -0.00350 276 LYS A CA    
2171 C  C     . LYS A 276 ? 0.33330 0.42220 0.29950 0.00020  0.02300  -0.01160 276 LYS A C     
2172 O  O     . LYS A 276 ? 0.32680 0.41330 0.29920 -0.00170 0.02070  -0.01870 276 LYS A O     
2173 C  CB    . LYS A 276 ? 0.30250 0.38110 0.27540 0.00040  0.02060  0.00140  276 LYS A CB    
2174 C  CG    . LYS A 276 ? 0.26880 0.33910 0.25050 -0.00060 0.02150  0.00600  276 LYS A CG    
2175 C  CD    . LYS A 276 ? 0.27200 0.33970 0.25330 -0.00010 0.01830  0.01090  276 LYS A CD    
2176 C  CE    . LYS A 276 ? 0.31050 0.37040 0.30060 -0.00150 0.01890  0.01380  276 LYS A CE    
2177 N  NZ    . LYS A 276 ? 0.39820 0.45560 0.38860 -0.00120 0.01610  0.01720  276 LYS A NZ    
2178 N  N     . VAL A 277 ? 0.28310 0.38080 0.23740 0.00230  0.02390  -0.01040 277 VAL A N     
2179 C  CA    . VAL A 277 ? 0.32330 0.42970 0.27080 0.00210  0.02180  -0.01870 277 VAL A CA    
2180 C  C     . VAL A 277 ? 0.34990 0.46230 0.29070 0.00300  0.02760  -0.02200 277 VAL A C     
2181 O  O     . VAL A 277 ? 0.46130 0.58370 0.38970 0.00460  0.02770  -0.02300 277 VAL A O     
2182 C  CB    . VAL A 277 ? 0.34300 0.45720 0.28130 0.00380  0.01690  -0.01590 277 VAL A CB    
2183 C  CG1   . VAL A 277 ? 0.35490 0.47810 0.28890 0.00270  0.01340  -0.02630 277 VAL A CG1   
2184 C  CG2   . VAL A 277 ? 0.31130 0.41930 0.25650 0.00330  0.01260  -0.01130 277 VAL A CG2   
2185 N  N     . GLU A 278 ? 0.41390 0.52090 0.36330 0.00200  0.03240  -0.02390 278 GLU A N     
2186 C  CA    . GLU A 278 ? 0.46720 0.57930 0.41210 0.00280  0.03930  -0.02640 278 GLU A CA    
2187 C  C     . GLU A 278 ? 0.55600 0.67560 0.49580 0.00220  0.03900  -0.03810 278 GLU A C     
2188 O  O     . GLU A 278 ? 0.39450 0.51100 0.34240 0.00020  0.03570  -0.04640 278 GLU A O     
2189 C  CB    . GLU A 278 ? 0.47800 0.58320 0.43570 0.00180  0.04420  -0.02640 278 GLU A CB    
2190 C  CG    . GLU A 278 ? 0.63060 0.74140 0.58390 0.00270  0.05260  -0.02690 278 GLU A CG    
2191 C  CD    . GLU A 278 ? 0.93180 1.03710 0.89920 0.00190  0.05760  -0.02640 278 GLU A CD    
2192 O  OE1   . GLU A 278 ? 1.27940 1.37810 1.26020 0.00080  0.05430  -0.02980 278 GLU A OE1   
2193 O  OE2   . GLU A 278 ? 1.00150 1.10980 0.96660 0.00240  0.06480  -0.02240 278 GLU A OE2   
2194 N  N     . ILE A 279 ? 0.42250 0.55210 0.34870 0.00380  0.04280  -0.03850 279 ILE A N     
2195 C  CA    . ILE A 279 ? 0.43600 0.57520 0.35460 0.00340  0.04310  -0.04990 279 ILE A CA    
2196 C  C     . ILE A 279 ? 0.35980 0.50030 0.28020 0.00340  0.05150  -0.05500 279 ILE A C     
2197 O  O     . ILE A 279 ? 0.37440 0.51370 0.29400 0.00450  0.05770  -0.04730 279 ILE A O     
2198 C  CB    . ILE A 279 ? 0.42190 0.57330 0.32160 0.00570  0.04100  -0.04650 279 ILE A CB    
2199 C  CG1   . ILE A 279 ? 0.47410 0.62450 0.37320 0.00640  0.03320  -0.03970 279 ILE A CG1   
2200 C  CG2   . ILE A 279 ? 0.51980 0.68250 0.41100 0.00500  0.04040  -0.05960 279 ILE A CG2   
2201 C  CD1   . ILE A 279 ? 0.48340 0.62930 0.39390 0.00360  0.02680  -0.04740 279 ILE A CD1   
2202 N  N     . ARG A 280 ? 0.50010 0.64300 0.42420 0.00190  0.05220  -0.06840 280 ARG A N     
2203 C  CA    . ARG A 280 ? 0.57080 0.71600 0.49770 0.00190  0.06040  -0.07580 280 ARG A CA    
2204 C  C     . ARG A 280 ? 0.61310 0.77030 0.52120 0.00370  0.06600  -0.07340 280 ARG A C     
2205 O  O     . ARG A 280 ? 0.55150 0.71780 0.44420 0.00450  0.06180  -0.07310 280 ARG A O     
2206 C  CB    . ARG A 280 ? 0.56190 0.70710 0.49630 0.00020  0.05940  -0.09130 280 ARG A CB    
2207 C  CG    . ARG A 280 ? 0.73860 0.87090 0.69340 -0.00110 0.05680  -0.09340 280 ARG A CG    
2208 C  CD    . ARG A 280 ? 0.67160 0.80250 0.63460 -0.00280 0.05630  -0.10820 280 ARG A CD    
2209 N  NE    . ARG A 280 ? 0.79310 0.92960 0.75570 -0.00210 0.06410  -0.11790 280 ARG A NE    
2210 C  CZ    . ARG A 280 ? 0.87670 1.01420 0.84480 -0.00330 0.06560  -0.13250 280 ARG A CZ    
2211 N  NH1   . ARG A 280 ? 0.77310 0.90560 0.74790 -0.00550 0.05980  -0.13890 280 ARG A NH1   
2212 N  NH2   . ARG A 280 ? 0.81450 0.95750 0.78190 -0.00240 0.07350  -0.14090 280 ARG A NH2   
2213 N  N     . LYS A 281 ? 0.78560 0.94330 0.69530 0.00440  0.07500  -0.07160 281 LYS A N     
2214 C  CA    . LYS A 281 ? 0.64720 0.81600 0.53970 0.00580  0.08200  -0.06980 281 LYS A CA    
2215 C  C     . LYS A 281 ? 0.66060 0.83810 0.54900 0.00510  0.08550  -0.08580 281 LYS A C     
2216 O  O     . LYS A 281 ? 0.94430 1.12200 0.83960 0.00490  0.09360  -0.09160 281 LYS A O     
2217 C  CB    . LYS A 281 ? 0.68250 0.84770 0.58000 0.00630  0.09100  -0.06050 281 LYS A CB    
2218 C  CG    . LYS A 281 ? 0.92380 1.08480 0.81740 0.00740  0.08970  -0.04400 281 LYS A CG    
2219 C  CD    . LYS A 281 ? 1.15900 1.30930 1.06490 0.00670  0.08110  -0.03970 281 LYS A CD    
2220 C  CE    . LYS A 281 ? 1.17250 1.31830 1.07530 0.00780  0.08100  -0.02420 281 LYS A CE    
2221 N  NZ    . LYS A 281 ? 1.00090 1.13700 0.91470 0.00710  0.07290  -0.02050 281 LYS A NZ    
2222 N  N     . LEU A 282 ? 0.69430 0.87930 0.57220 0.00480  0.07910  -0.09340 282 LEU A N     
2223 C  CA    . LEU A 282 ? 0.81240 1.00670 0.68480 0.00380  0.08120  -0.10980 282 LEU A CA    
2224 C  C     . LEU A 282 ? 0.77930 0.98810 0.62900 0.00550  0.08730  -0.10860 282 LEU A C     
2225 O  O     . LEU A 282 ? 0.68760 0.89980 0.52390 0.00770  0.08730  -0.09470 282 LEU A O     
2226 C  CB    . LEU A 282 ? 0.83750 1.03440 0.70900 0.00210  0.07150  -0.11880 282 LEU A CB    
2227 C  CG    . LEU A 282 ? 0.85830 1.04150 0.75050 0.00010  0.06530  -0.12030 282 LEU A CG    
2228 C  CD1   . LEU A 282 ? 0.74020 0.92800 0.62980 -0.00180 0.05640  -0.12850 282 LEU A CD1   
2229 C  CD2   . LEU A 282 ? 0.67980 0.85390 0.59130 -0.00100 0.07050  -0.12950 282 LEU A CD2   
2230 N  N     . SER A 283 ? 0.80270 1.01790 0.64930 0.00470  0.09190  -0.12240 283 SER A N     
2231 C  CA    . SER A 283 ? 0.91530 1.13830 0.74370 0.00610  0.09550  -0.12010 283 SER A CA    
2232 C  C     . SER A 283 ? 1.01780 1.24780 0.82750 0.00770  0.08720  -0.11170 283 SER A C     
2233 O  O     . SER A 283 ? 0.85100 1.08380 0.64620 0.01010  0.08980  -0.09850 283 SER A O     
2234 C  CB    . SER A 283 ? 0.81440 1.04040 0.64520 0.00450  0.09780  -0.13710 283 SER A CB    
2235 O  OG    . SER A 283 ? 0.89410 1.11320 0.74380 0.00360  0.10530  -0.14450 283 SER A OG    
2236 N  N     . ASP A 284 ? 1.05850 1.29100 0.87020 0.00630  0.07720  -0.11940 284 ASP A N     
2237 C  CA    . ASP A 284 ? 1.08460 1.32370 0.88360 0.00790  0.06770  -0.11220 284 ASP A CA    
2238 C  C     . ASP A 284 ? 1.11690 1.35000 0.92470 0.00820  0.06240  -0.10390 284 ASP A C     
2239 O  O     . ASP A 284 ? 0.68450 0.91330 0.50650 0.00560  0.05840  -0.11300 284 ASP A O     
2240 C  CB    . ASP A 284 ? 1.14420 1.39100 0.94170 0.00580  0.06030  -0.12660 284 ASP A CB    
2241 C  CG    . ASP A 284 ? 1.24420 1.50070 1.02750 0.00790  0.05100  -0.11980 284 ASP A CG    
2242 O  OD1   . ASP A 284 ? 1.03620 1.29400 0.80740 0.01140  0.05140  -0.10400 284 ASP A OD1   
2243 O  OD2   . ASP A 284 ? 1.19990 1.46260 0.98520 0.00590  0.04350  -0.13050 284 ASP A OD2   
2244 N  N     . PRO A 285 ? 1.10470 1.33640 0.90510 0.01120  0.06270  -0.08640 285 PRO A N     
2245 C  CA    . PRO A 285 ? 0.96600 1.19200 0.77450 0.01160  0.05820  -0.07810 285 PRO A CA    
2246 C  C     . PRO A 285 ? 0.88910 1.11880 0.69970 0.01060  0.04670  -0.08390 285 PRO A C     
2247 O  O     . PRO A 285 ? 0.85950 1.09810 0.65930 0.01180  0.04060  -0.08440 285 PRO A O     
2248 C  CB    . PRO A 285 ? 0.92530 1.15070 0.72250 0.01550  0.06000  -0.05860 285 PRO A CB    
2249 C  CG    . PRO A 285 ? 0.93050 1.15780 0.71780 0.01620  0.06920  -0.05680 285 PRO A CG    
2250 C  CD    . PRO A 285 ? 1.00150 1.23600 0.78610 0.01420  0.06790  -0.07370 285 PRO A CD    
2251 N  N     . PRO A 286 ? 0.52840 0.74620 0.35870 0.00810  0.04220  -0.08630 286 PRO A N     
2252 C  CA    . PRO A 286 ? 0.67940 0.90000 0.51330 0.00690  0.03200  -0.09030 286 PRO A CA    
2253 C  C     . PRO A 286 ? 0.58230 0.81020 0.40390 0.01070  0.02600  -0.07700 286 PRO A C     
2254 O  O     . PRO A 286 ? 0.54600 0.76690 0.36700 0.01340  0.02860  -0.06190 286 PRO A O     
2255 C  CB    . PRO A 286 ? 0.72160 0.92520 0.57800 0.00420  0.03070  -0.08960 286 PRO A CB    
2256 C  CG    . PRO A 286 ? 0.55760 0.75220 0.42330 0.00310  0.03960  -0.09290 286 PRO A CG    
2257 C  CD    . PRO A 286 ? 0.59390 0.79550 0.44400 0.00620  0.04690  -0.08550 286 PRO A CD    
2258 N  N     . LYS A 287 ? 0.50000 0.74080 0.31400 0.01090  0.01800  -0.08290 287 LYS A N     
2259 C  CA    . LYS A 287 ? 0.63890 0.88580 0.44460 0.01490  0.01110  -0.07080 287 LYS A CA    
2260 C  C     . LYS A 287 ? 0.57680 0.81680 0.39460 0.01470  0.00580  -0.06500 287 LYS A C     
2261 O  O     . LYS A 287 ? 0.45720 0.68720 0.29240 0.01050  0.00500  -0.07250 287 LYS A O     
2262 C  CB    . LYS A 287 ? 0.87340 1.13330 0.67360 0.01470  0.00390  -0.07890 287 LYS A CB    
2263 C  CG    . LYS A 287 ? 0.85440 1.12040 0.64450 0.01430  0.00850  -0.08630 287 LYS A CG    
2264 C  CD    . LYS A 287 ? 1.17160 1.45190 0.95200 0.01580  0.00130  -0.08920 287 LYS A CD    
2265 C  CE    . LYS A 287 ? 1.29970 1.58570 1.09190 0.01230  -0.00720 -0.10190 287 LYS A CE    
2266 N  NZ    . LYS A 287 ? 1.34920 1.63210 1.15230 0.00650  -0.00430 -0.11990 287 LYS A NZ    
2267 N  N     . ALA A 288 ? 0.66030 0.90280 0.47180 0.01930  0.00240  -0.05050 288 ALA A N     
2268 C  CA    . ALA A 288 ? 0.61440 0.84850 0.43890 0.01960  -0.00260 -0.04290 288 ALA A CA    
2269 C  C     . ALA A 288 ? 0.53410 0.77110 0.37060 0.01560  -0.01010 -0.05520 288 ALA A C     
2270 O  O     . ALA A 288 ? 0.44000 0.66450 0.29310 0.01280  -0.01060 -0.05510 288 ALA A O     
2271 C  CB    . ALA A 288 ? 0.64280 0.88340 0.45650 0.02580  -0.00610 -0.02780 288 ALA A CB    
2272 N  N     . GLU A 289 ? 0.44370 0.69760 0.27210 0.01520  -0.01570 -0.06580 289 GLU A N     
2273 C  CA    . GLU A 289 ? 0.49400 0.75200 0.33440 0.01070  -0.02220 -0.07890 289 GLU A CA    
2274 C  C     . GLU A 289 ? 0.62900 0.87360 0.48520 0.00460  -0.01790 -0.09010 289 GLU A C     
2275 O  O     . GLU A 289 ? 0.44240 0.67950 0.31430 0.00120  -0.02070 -0.09300 289 GLU A O     
2276 C  CB    . GLU A 289 ? 0.46040 0.73180 0.29590 0.01050  -0.02660 -0.08760 289 GLU A CB    
2277 C  CG    . GLU A 289 ? 0.77040 1.04740 0.61910 0.00640  -0.03380 -0.09870 289 GLU A CG    
2278 C  CD    . GLU A 289 ? 0.95760 1.24690 0.80390 0.00460  -0.03680 -0.11090 289 GLU A CD    
2279 O  OE1   . GLU A 289 ? 0.65360 0.94910 0.48600 0.00740  -0.03450 -0.10940 289 GLU A OE1   
2280 O  OE2   . GLU A 289 ? 0.84990 1.14280 0.70860 0.00030  -0.04130 -0.12200 289 GLU A OE2   
2281 N  N     . ALA A 290 ? 0.54730 0.78860 0.39970 0.00350  -0.01080 -0.09590 290 ALA A N     
2282 C  CA    . ALA A 290 ? 0.53940 0.76760 0.40690 -0.00140 -0.00600 -0.10580 290 ALA A CA    
2283 C  C     . ALA A 290 ? 0.57930 0.78850 0.46120 -0.00180 -0.00330 -0.09560 290 ALA A C     
2284 O  O     . ALA A 290 ? 0.48900 0.68790 0.38680 -0.00580 -0.00370 -0.10140 290 ALA A O     
2285 C  CB    . ALA A 290 ? 0.58900 0.81860 0.44900 -0.00150 0.00150  -0.11270 290 ALA A CB    
2286 N  N     . ILE A 291 ? 0.46210 0.66690 0.33830 0.00230  -0.00060 -0.08040 291 ILE A N     
2287 C  CA    . ILE A 291 ? 0.44180 0.63040 0.33020 0.00220  0.00160  -0.07040 291 ILE A CA    
2288 C  C     . ILE A 291 ? 0.49060 0.67660 0.38890 0.00090  -0.00500 -0.06840 291 ILE A C     
2289 O  O     . ILE A 291 ? 0.41210 0.58600 0.32470 -0.00220 -0.00460 -0.06990 291 ILE A O     
2290 C  CB    . ILE A 291 ? 0.49480 0.68030 0.37530 0.00670  0.00570  -0.05480 291 ILE A CB    
2291 C  CG1   . ILE A 291 ? 0.50440 0.69290 0.37470 0.00800  0.01320  -0.05550 291 ILE A CG1   
2292 C  CG2   . ILE A 291 ? 0.51970 0.68870 0.41390 0.00590  0.00770  -0.04670 291 ILE A CG2   
2293 C  CD1   . ILE A 291 ? 0.59870 0.78030 0.47880 0.00450  0.01830  -0.06640 291 ILE A CD1   
2294 N  N     . ARG A 292 ? 0.46130 0.65940 0.35170 0.00350  -0.01100 -0.06480 292 ARG A N     
2295 C  CA    . ARG A 292 ? 0.53130 0.72960 0.43090 0.00270  -0.01730 -0.06300 292 ARG A CA    
2296 C  C     . ARG A 292 ? 0.44950 0.64790 0.36070 -0.00320 -0.01990 -0.07740 292 ARG A C     
2297 O  O     . ARG A 292 ? 0.43910 0.63020 0.36290 -0.00560 -0.02190 -0.07640 292 ARG A O     
2298 C  CB    . ARG A 292 ? 0.53440 0.74800 0.42340 0.00720  -0.02340 -0.05730 292 ARG A CB    
2299 C  CG    . ARG A 292 ? 0.51310 0.72590 0.39120 0.01320  -0.02080 -0.04180 292 ARG A CG    
2300 C  CD    . ARG A 292 ? 0.50730 0.70230 0.39380 0.01330  -0.01530 -0.03180 292 ARG A CD    
2301 N  NE    . ARG A 292 ? 0.49480 0.68240 0.39530 0.01140  -0.01840 -0.03060 292 ARG A NE    
2302 C  CZ    . ARG A 292 ? 0.50820 0.68060 0.41880 0.01010  -0.01490 -0.02520 292 ARG A CZ    
2303 N  NH1   . ARG A 292 ? 0.56950 0.73210 0.47920 0.01040  -0.00840 -0.02080 292 ARG A NH1   
2304 N  NH2   . ARG A 292 ? 0.45640 0.62400 0.37810 0.00840  -0.01780 -0.02470 292 ARG A NH2   
2305 N  N     . ASP A 293 ? 0.45710 0.66330 0.36430 -0.00540 -0.01940 -0.09040 293 ASP A N     
2306 C  CA    . ASP A 293 ? 0.44700 0.65210 0.36630 -0.01130 -0.02070 -0.10510 293 ASP A CA    
2307 C  C     . ASP A 293 ? 0.39880 0.58470 0.33250 -0.01440 -0.01550 -0.10550 293 ASP A C     
2308 O  O     . ASP A 293 ? 0.38350 0.56300 0.33060 -0.01850 -0.01710 -0.10980 293 ASP A O     
2309 C  CB    . ASP A 293 ? 0.48200 0.69900 0.39340 -0.01280 -0.02030 -0.11950 293 ASP A CB    
2310 C  CG    . ASP A 293 ? 0.58860 0.82600 0.49220 -0.01240 -0.02790 -0.12550 293 ASP A CG    
2311 O  OD1   . ASP A 293 ? 0.55320 0.79440 0.46290 -0.01260 -0.03360 -0.12230 293 ASP A OD1   
2312 O  OD2   . ASP A 293 ? 0.96130 1.21180 0.85290 -0.01180 -0.02810 -0.13400 293 ASP A OD2   
2313 N  N     . MET A 294 ? 0.42800 0.60530 0.35900 -0.01240 -0.00930 -0.10080 294 MET A N     
2314 C  CA    . MET A 294 ? 0.42800 0.58820 0.37210 -0.01450 -0.00470 -0.10040 294 MET A CA    
2315 C  C     . MET A 294 ? 0.38470 0.53400 0.33630 -0.01410 -0.00590 -0.08860 294 MET A C     
2316 O  O     . MET A 294 ? 0.41240 0.54970 0.37680 -0.01690 -0.00490 -0.08970 294 MET A O     
2317 C  CB    . MET A 294 ? 0.41560 0.57180 0.35540 -0.01240 0.00210  -0.09940 294 MET A CB    
2318 C  CG    . MET A 294 ? 0.51590 0.65750 0.47010 -0.01460 0.00650  -0.10320 294 MET A CG    
2319 S  SD    . MET A 294 ? 0.40230 0.54310 0.36740 -0.01970 0.00590  -0.12100 294 MET A SD    
2320 C  CE    . MET A 294 ? 0.44370 0.59620 0.39790 -0.01860 0.01020  -0.13250 294 MET A CE    
2321 N  N     . VAL A 295 ? 0.35770 0.51130 0.30130 -0.01040 -0.00780 -0.07740 295 VAL A N     
2322 C  CA    . VAL A 295 ? 0.36260 0.50770 0.31250 -0.00980 -0.00900 -0.06690 295 VAL A CA    
2323 C  C     . VAL A 295 ? 0.41510 0.56100 0.37410 -0.01330 -0.01370 -0.07130 295 VAL A C     
2324 O  O     . VAL A 295 ? 0.32230 0.45710 0.29170 -0.01560 -0.01310 -0.06880 295 VAL A O     
2325 C  CB    . VAL A 295 ? 0.33780 0.48770 0.27770 -0.00490 -0.00980 -0.05470 295 VAL A CB    
2326 C  CG1   . VAL A 295 ? 0.35920 0.50170 0.30630 -0.00460 -0.01160 -0.04600 295 VAL A CG1   
2327 C  CG2   . VAL A 295 ? 0.35080 0.49700 0.28400 -0.00200 -0.00400 -0.04880 295 VAL A CG2   
2328 N  N     . ARG A 296 ? 0.37280 0.53300 0.32790 -0.01380 -0.01830 -0.07790 296 ARG A N     
2329 C  CA    . ARG A 296 ? 0.51440 0.67850 0.47890 -0.01780 -0.02270 -0.08420 296 ARG A CA    
2330 C  C     . ARG A 296 ? 0.52060 0.67390 0.49780 -0.02330 -0.02000 -0.09310 296 ARG A C     
2331 O  O     . ARG A 296 ? 0.39260 0.53810 0.38050 -0.02620 -0.02040 -0.09150 296 ARG A O     
2332 C  CB    . ARG A 296 ? 0.46270 0.64600 0.42060 -0.01740 -0.02800 -0.09180 296 ARG A CB    
2333 C  CG    . ARG A 296 ? 0.47490 0.66370 0.44390 -0.02240 -0.03210 -0.10110 296 ARG A CG    
2334 C  CD    . ARG A 296 ? 0.59010 0.79990 0.55270 -0.02110 -0.03870 -0.10650 296 ARG A CD    
2335 N  NE    . ARG A 296 ? 0.79820 1.01810 0.74950 -0.02030 -0.03860 -0.11480 296 ARG A NE    
2336 C  CZ    . ARG A 296 ? 0.80620 1.03240 0.76110 -0.02490 -0.03950 -0.13040 296 ARG A CZ    
2337 N  NH1   . ARG A 296 ? 0.82420 1.04680 0.79480 -0.03110 -0.04010 -0.13920 296 ARG A NH1   
2338 N  NH2   . ARG A 296 ? 0.66090 0.89680 0.60370 -0.02360 -0.03910 -0.13740 296 ARG A NH2   
2339 N  N     . TYR A 297 ? 0.39150 0.54430 0.36760 -0.02450 -0.01710 -0.10230 297 TYR A N     
2340 C  CA    . TYR A 297 ? 0.46810 0.60940 0.45650 -0.02900 -0.01380 -0.11080 297 TYR A CA    
2341 C  C     . TYR A 297 ? 0.37950 0.50350 0.37540 -0.02860 -0.01050 -0.10110 297 TYR A C     
2342 O  O     . TYR A 297 ? 0.43930 0.55380 0.44700 -0.03230 -0.01010 -0.10250 297 TYR A O     
2343 C  CB    . TYR A 297 ? 0.43690 0.58060 0.42160 -0.02880 -0.01030 -0.12060 297 TYR A CB    
2344 C  CG    . TYR A 297 ? 0.50450 0.63380 0.50210 -0.03180 -0.00580 -0.12670 297 TYR A CG    
2345 C  CD1   . TYR A 297 ? 0.51250 0.63990 0.52150 -0.03710 -0.00620 -0.13840 297 TYR A CD1   
2346 C  CD2   . TYR A 297 ? 0.52910 0.64640 0.52880 -0.02930 -0.00120 -0.12030 297 TYR A CD2   
2347 C  CE1   . TYR A 297 ? 0.46280 0.57580 0.48460 -0.03930 -0.00190 -0.14290 297 TYR A CE1   
2348 C  CE2   . TYR A 297 ? 0.47460 0.57890 0.48680 -0.03120 0.00260  -0.12510 297 TYR A CE2   
2349 C  CZ    . TYR A 297 ? 0.55740 0.65890 0.58050 -0.03600 0.00230  -0.13600 297 TYR A CZ    
2350 O  OH    . TYR A 297 ? 0.49840 0.58610 0.53460 -0.03750 0.00630  -0.13990 297 TYR A OH    
2351 N  N     . ALA A 298 ? 0.34510 0.46560 0.33430 -0.02430 -0.00810 -0.09170 298 ALA A N     
2352 C  CA    . ALA A 298 ? 0.33050 0.43660 0.32560 -0.02350 -0.00550 -0.08290 298 ALA A CA    
2353 C  C     . ALA A 298 ? 0.35650 0.45790 0.35720 -0.02510 -0.00810 -0.07650 298 ALA A C     
2354 O  O     . ALA A 298 ? 0.41290 0.50290 0.42280 -0.02730 -0.00680 -0.07530 298 ALA A O     
2355 C  CB    . ALA A 298 ? 0.32230 0.42820 0.30920 -0.01890 -0.00300 -0.07410 298 ALA A CB    
2356 N  N     . ARG A 299 ? 0.36000 0.47080 0.35500 -0.02370 -0.01150 -0.07220 299 ARG A N     
2357 C  CA    . ARG A 299 ? 0.44210 0.55040 0.44170 -0.02480 -0.01370 -0.06620 299 ARG A CA    
2358 C  C     . ARG A 299 ? 0.39900 0.50610 0.40910 -0.03020 -0.01470 -0.07390 299 ARG A C     
2359 O  O     . ARG A 299 ? 0.39800 0.49760 0.41450 -0.03220 -0.01440 -0.06940 299 ARG A O     
2360 C  CB    . ARG A 299 ? 0.61340 0.73360 0.60550 -0.02160 -0.01710 -0.06130 299 ARG A CB    
2361 C  CG    . ARG A 299 ? 0.59570 0.71340 0.58030 -0.01670 -0.01550 -0.05060 299 ARG A CG    
2362 C  CD    . ARG A 299 ? 0.68760 0.81660 0.66600 -0.01320 -0.01890 -0.04570 299 ARG A CD    
2363 N  NE    . ARG A 299 ? 0.76130 0.88850 0.73200 -0.00850 -0.01680 -0.03630 299 ARG A NE    
2364 C  CZ    . ARG A 299 ? 0.42980 0.56680 0.39130 -0.00420 -0.01830 -0.03210 299 ARG A CZ    
2365 N  NH1   . ARG A 299 ? 0.41500 0.56590 0.37320 -0.00350 -0.02270 -0.03660 299 ARG A NH1   
2366 N  NH2   . ARG A 299 ? 0.45590 0.58910 0.41200 -0.00050 -0.01530 -0.02310 299 ARG A NH2   
2367 N  N     . ASN A 300 ? 0.38460 0.49890 0.39630 -0.03270 -0.01550 -0.08520 300 ASN A N     
2368 C  CA    . ASN A 300 ? 0.50130 0.61440 0.52420 -0.03840 -0.01590 -0.09380 300 ASN A CA    
2369 C  C     . ASN A 300 ? 0.49300 0.58970 0.52560 -0.04120 -0.01170 -0.09490 300 ASN A C     
2370 O  O     . ASN A 300 ? 0.43600 0.52550 0.47800 -0.04510 -0.01090 -0.09410 300 ASN A O     
2371 C  CB    . ASN A 300 ? 0.63160 0.75860 0.65340 -0.04040 -0.01840 -0.10660 300 ASN A CB    
2372 C  CG    . ASN A 300 ? 0.75810 0.88320 0.79350 -0.04700 -0.01800 -0.11700 300 ASN A CG    
2373 O  OD1   . ASN A 300 ? 0.88400 1.01220 0.92600 -0.05000 -0.01990 -0.11660 300 ASN A OD1   
2374 N  ND2   . ASN A 300 ? 1.06650 1.18630 1.10680 -0.04950 -0.01510 -0.12660 300 ASN A ND2   
2375 N  N     . VAL A 301 ? 0.33560 0.42640 0.36630 -0.03910 -0.00880 -0.09630 301 VAL A N     
2376 C  CA    . VAL A 301 ? 0.36430 0.43950 0.40450 -0.04060 -0.00500 -0.09650 301 VAL A CA    
2377 C  C     . VAL A 301 ? 0.31540 0.37960 0.35680 -0.03910 -0.00430 -0.08390 301 VAL A C     
2378 O  O     . VAL A 301 ? 0.46000 0.51240 0.51020 -0.04150 -0.00250 -0.08210 301 VAL A O     
2379 C  CB    . VAL A 301 ? 0.38120 0.45370 0.42040 -0.03820 -0.00190 -0.10140 301 VAL A CB    
2380 C  CG1   . VAL A 301 ? 0.53380 0.61620 0.57260 -0.04030 -0.00200 -0.11550 301 VAL A CG1   
2381 C  CG2   . VAL A 301 ? 0.57800 0.65320 0.60670 -0.03280 -0.00140 -0.09340 301 VAL A CG2   
2382 N  N     . ILE A 302 ? 0.30130 0.36950 0.33350 -0.03520 -0.00570 -0.07520 302 ILE A N     
2383 C  CA    . ILE A 302 ? 0.32450 0.38470 0.35650 -0.03390 -0.00560 -0.06420 302 ILE A CA    
2384 C  C     . ILE A 302 ? 0.35310 0.41160 0.39050 -0.03780 -0.00640 -0.06270 302 ILE A C     
2385 O  O     . ILE A 302 ? 0.29220 0.34000 0.33400 -0.03900 -0.00500 -0.05740 302 ILE A O     
2386 C  CB    . ILE A 302 ? 0.33990 0.40620 0.36200 -0.02960 -0.00680 -0.05660 302 ILE A CB    
2387 C  CG1   . ILE A 302 ? 0.42750 0.49200 0.44600 -0.02600 -0.00450 -0.05570 302 ILE A CG1   
2388 C  CG2   . ILE A 302 ? 0.37840 0.43910 0.40030 -0.02910 -0.00720 -0.04710 302 ILE A CG2   
2389 C  CD1   . ILE A 302 ? 0.41750 0.48890 0.42640 -0.02210 -0.00490 -0.04990 302 ILE A CD1   
2390 N  N     . GLU A 303 ? 0.47530 0.54510 0.51230 -0.03970 -0.00870 -0.06750 303 GLU A N     
2391 C  CA    . GLU A 303 ? 0.57000 0.64010 0.61330 -0.04380 -0.00920 -0.06720 303 GLU A CA    
2392 C  C     . GLU A 303 ? 0.54080 0.60240 0.59530 -0.04900 -0.00660 -0.07320 303 GLU A C     
2393 O  O     . GLU A 303 ? 0.44280 0.49610 0.50280 -0.05170 -0.00480 -0.06870 303 GLU A O     
2394 C  CB    . GLU A 303 ? 0.53960 0.62570 0.58090 -0.04400 -0.01270 -0.07100 303 GLU A CB    
2395 C  CG    . GLU A 303 ? 0.69540 0.78340 0.74320 -0.04750 -0.01290 -0.06940 303 GLU A CG    
2396 C  CD    . GLU A 303 ? 0.83840 0.91870 0.88380 -0.04590 -0.01140 -0.05850 303 GLU A CD    
2397 O  OE1   . GLU A 303 ? 0.95490 1.03520 0.99210 -0.04110 -0.01210 -0.05200 303 GLU A OE1   
2398 O  OE2   . GLU A 303 ? 0.91180 0.98610 0.96360 -0.04970 -0.00920 -0.05660 303 GLU A OE2   
2399 N  N     . GLU A 304 ? 0.49930 0.56290 0.55740 -0.05040 -0.00620 -0.08340 304 GLU A N     
2400 C  CA    . GLU A 304 ? 0.53130 0.58550 0.60130 -0.05520 -0.00310 -0.08990 304 GLU A CA    
2401 C  C     . GLU A 304 ? 0.60290 0.63980 0.67640 -0.05410 0.00020  -0.08220 304 GLU A C     
2402 O  O     . GLU A 304 ? 0.54930 0.57620 0.63170 -0.05800 0.00270  -0.08100 304 GLU A O     
2403 C  CB    . GLU A 304 ? 0.55630 0.61540 0.62860 -0.05610 -0.00290 -0.10270 304 GLU A CB    
2404 C  CG    . GLU A 304 ? 0.99770 1.07250 1.07110 -0.05950 -0.00590 -0.11310 304 GLU A CG    
2405 C  CD    . GLU A 304 ? 1.34790 1.42810 1.42310 -0.06070 -0.00570 -0.12700 304 GLU A CD    
2406 O  OE1   . GLU A 304 ? 1.15740 1.22980 1.23180 -0.05830 -0.00290 -0.12830 304 GLU A OE1   
2407 O  OE2   . GLU A 304 ? 1.27050 1.36360 1.34820 -0.06420 -0.00830 -0.13730 304 GLU A OE2   
2408 N  N     . PHE A 305 ? 0.40500 0.43890 0.47170 -0.04890 0.00000  -0.07670 305 PHE A N     
2409 C  CA    . PHE A 305 ? 0.36280 0.38230 0.43250 -0.04690 0.00220  -0.06930 305 PHE A CA    
2410 C  C     . PHE A 305 ? 0.41430 0.42820 0.48260 -0.04760 0.00200  -0.05860 305 PHE A C     
2411 O  O     . PHE A 305 ? 0.36450 0.36620 0.43850 -0.04880 0.00420  -0.05420 305 PHE A O     
2412 C  CB    . PHE A 305 ? 0.35140 0.37110 0.41510 -0.04130 0.00180  -0.06640 305 PHE A CB    
2413 C  CG    . PHE A 305 ? 0.30290 0.30910 0.37150 -0.03910 0.00350  -0.06050 305 PHE A CG    
2414 C  CD1   . PHE A 305 ? 0.41760 0.41630 0.49540 -0.03910 0.00610  -0.06640 305 PHE A CD1   
2415 C  CD2   . PHE A 305 ? 0.33920 0.34060 0.40400 -0.03690 0.00240  -0.04950 305 PHE A CD2   
2416 C  CE1   . PHE A 305 ? 0.41680 0.40360 0.50030 -0.03640 0.00730  -0.06060 305 PHE A CE1   
2417 C  CE2   . PHE A 305 ? 0.36620 0.35650 0.43580 -0.03450 0.00320  -0.04390 305 PHE A CE2   
2418 C  CZ    . PHE A 305 ? 0.34890 0.33180 0.42800 -0.03400 0.00560  -0.04910 305 PHE A CZ    
2419 N  N     . ARG A 306 ? 0.36560 0.38850 0.42590 -0.04660 -0.00030 -0.05440 306 ARG A N     
2420 C  CA    . ARG A 306 ? 0.51390 0.53370 0.57140 -0.04710 -0.00030 -0.04520 306 ARG A CA    
2421 C  C     . ARG A 306 ? 0.51270 0.52770 0.57860 -0.05280 0.00220  -0.04630 306 ARG A C     
2422 O  O     . ARG A 306 ? 0.55200 0.55760 0.61830 -0.05350 0.00390  -0.03850 306 ARG A O     
2423 C  CB    . ARG A 306 ? 0.57730 0.60890 0.62690 -0.04530 -0.00280 -0.04300 306 ARG A CB    
2424 C  CG    . ARG A 306 ? 0.60920 0.63840 0.65530 -0.04530 -0.00250 -0.03440 306 ARG A CG    
2425 C  CD    . ARG A 306 ? 0.86270 0.90200 0.90160 -0.04230 -0.00470 -0.03190 306 ARG A CD    
2426 N  NE    . ARG A 306 ? 1.40660 1.44580 1.43940 -0.03750 -0.00580 -0.02940 306 ARG A NE    
2427 C  CZ    . ARG A 306 ? 0.93440 0.98260 0.96270 -0.03460 -0.00740 -0.03170 306 ARG A CZ    
2428 N  NH1   . ARG A 306 ? 1.07780 1.13670 1.10620 -0.03530 -0.00890 -0.03640 306 ARG A NH1   
2429 N  NH2   . ARG A 306 ? 0.65110 0.69790 0.67480 -0.03080 -0.00740 -0.02870 306 ARG A NH2   
2430 N  N     . ARG A 307 ? 0.48220 0.50370 0.55460 -0.05680 0.00240  -0.05580 307 ARG A N     
2431 C  CA    . ARG A 307 ? 0.54840 0.56590 0.63110 -0.06310 0.00540  -0.05870 307 ARG A CA    
2432 C  C     . ARG A 307 ? 0.52270 0.52490 0.61380 -0.06460 0.00890  -0.05890 307 ARG A C     
2433 O  O     . ARG A 307 ? 0.58420 0.57580 0.67940 -0.06720 0.01210  -0.05250 307 ARG A O     
2434 C  CB    . ARG A 307 ? 0.56540 0.59610 0.65360 -0.06680 0.00400  -0.07020 307 ARG A CB    
2435 C  CG    . ARG A 307 ? 0.75110 0.79690 0.83410 -0.06600 0.00080  -0.06950 307 ARG A CG    
2436 C  CD    . ARG A 307 ? 0.92150 0.97920 1.01290 -0.07100 -0.00020 -0.08000 307 ARG A CD    
2437 N  NE    . ARG A 307 ? 1.33880 1.40280 1.43150 -0.07080 -0.00220 -0.09100 307 ARG A NE    
2438 C  CZ    . ARG A 307 ? 1.27750 1.35520 1.36200 -0.06700 -0.00660 -0.09470 307 ARG A CZ    
2439 N  NH1   . ARG A 307 ? 0.88300 0.96920 0.95880 -0.06280 -0.00950 -0.08800 307 ARG A NH1   
2440 N  NH2   . ARG A 307 ? 1.07360 1.15650 1.15890 -0.06740 -0.00780 -0.10520 307 ARG A NH2   
2441 N  N     . ALA A 308 ? 0.34240 0.34330 0.43590 -0.06270 0.00860  -0.06570 308 ALA A N     
2442 C  CA    . ALA A 308 ? 0.37810 0.36480 0.48130 -0.06350 0.01200  -0.06750 308 ALA A CA    
2443 C  C     . ALA A 308 ? 0.42230 0.39490 0.52410 -0.06020 0.01330  -0.05510 308 ALA A C     
2444 O  O     . ALA A 308 ? 0.49090 0.45020 0.60150 -0.06180 0.01670  -0.05320 308 ALA A O     
2445 C  CB    . ALA A 308 ? 0.38080 0.37070 0.48490 -0.06090 0.01130  -0.07690 308 ALA A CB    
2446 N  N     . LYS A 309 ? 0.48700 0.46280 0.57760 -0.05560 0.01050  -0.04680 309 LYS A N     
2447 C  CA    . LYS A 309 ? 0.52260 0.48830 0.60980 -0.05190 0.01040  -0.03520 309 LYS A CA    
2448 C  C     . LYS A 309 ? 0.69730 0.65360 0.78680 -0.05530 0.01320  -0.02720 309 LYS A C     
2449 O  O     . LYS A 309 ? 0.56180 0.50740 0.65080 -0.05280 0.01370  -0.01810 309 LYS A O     
2450 C  CB    . LYS A 309 ? 0.46330 0.43750 0.53820 -0.04780 0.00680  -0.02960 309 LYS A CB    
2451 C  CG    . LYS A 309 ? 0.57520 0.54450 0.64650 -0.04230 0.00510  -0.02260 309 LYS A CG    
2452 C  CD    . LYS A 309 ? 0.65680 0.63500 0.71710 -0.03970 0.00210  -0.01830 309 LYS A CD    
2453 C  CE    . LYS A 309 ? 0.74720 0.72450 0.80490 -0.03430 0.00000  -0.01480 309 LYS A CE    
2454 N  NZ    . LYS A 309 ? 0.77360 0.75970 0.82210 -0.03230 -0.00230 -0.01210 309 LYS A NZ    
2455 N  N     . HIS A 310 ? 0.89360 0.85480 0.98530 -0.06080 0.01490  -0.03030 310 HIS A N     
2456 C  CA    . HIS A 310 ? 1.01480 0.96910 1.10830 -0.06480 0.01840  -0.02310 310 HIS A CA    
2457 C  C     . HIS A 310 ? 0.96880 0.90880 1.07470 -0.06840 0.02320  -0.02330 310 HIS A C     
2458 O  O     . HIS A 310 ? 0.83080 0.76040 0.93640 -0.06940 0.02620  -0.01360 310 HIS A O     
2459 C  CB    . HIS A 310 ? 0.95190 0.91800 1.04470 -0.06950 0.01890  -0.02680 310 HIS A CB    
2460 C  CG    . HIS A 310 ? 1.28710 1.26440 1.36790 -0.06610 0.01530  -0.02350 310 HIS A CG    
2461 N  ND1   . HIS A 310 ? 1.21670 1.19080 1.28810 -0.06340 0.01490  -0.01310 310 HIS A ND1   
2462 C  CD2   . HIS A 310 ? 1.32690 1.31850 1.40410 -0.06490 0.01210  -0.02940 310 HIS A CD2   
2463 C  CE1   . HIS A 310 ? 1.11160 1.09670 1.17490 -0.06090 0.01190  -0.01320 310 HIS A CE1   
2464 N  NE2   . HIS A 310 ? 1.28720 1.28280 1.35400 -0.06160 0.01020  -0.02240 310 HIS A NE2   
2465 N  N     . TYR A 311 ? 0.72850 0.66770 0.84500 -0.07030 0.02430  -0.03430 311 TYR A N     
2466 C  CA    . TYR A 311 ? 0.87220 0.79860 1.00340 -0.07500 0.02960  -0.03730 311 TYR A CA    
2467 C  C     . TYR A 311 ? 0.85020 0.76810 0.98970 -0.07190 0.03010  -0.04280 311 TYR A C     
2468 O  O     . TYR A 311 ? 0.88720 0.78970 1.03740 -0.07340 0.03450  -0.04010 311 TYR A O     
2469 C  CB    . TYR A 311 ? 0.71320 0.64740 0.85280 -0.08280 0.03190  -0.04740 311 TYR A CB    
2470 C  CG    . TYR A 311 ? 0.85410 0.80380 0.99460 -0.08330 0.02840  -0.06160 311 TYR A CG    
2471 C  CD1   . TYR A 311 ? 0.76860 0.73510 0.89900 -0.08200 0.02400  -0.06300 311 TYR A CD1   
2472 C  CD2   . TYR A 311 ? 0.75100 0.69850 0.90240 -0.08520 0.02960  -0.07380 311 TYR A CD2   
2473 C  CE1   . TYR A 311 ? 0.67700 0.65820 0.80720 -0.08210 0.02060  -0.07510 311 TYR A CE1   
2474 C  CE2   . TYR A 311 ? 0.74590 0.70860 0.89670 -0.08580 0.02630  -0.08700 311 TYR A CE2   
2475 C  CZ    . TYR A 311 ? 0.72980 0.70950 0.86940 -0.08410 0.02160  -0.08710 311 TYR A CZ    
2476 O  OH    . TYR A 311 ? 0.73310 0.72810 0.87100 -0.08410 0.01800  -0.09910 311 TYR A OH    
2477 N  N     . LYS A 312 ? 0.52730 0.45420 0.66280 -0.06780 0.02630  -0.05000 312 LYS A N     
2478 C  CA    . LYS A 312 ? 0.51810 0.43840 0.66240 -0.06520 0.02740  -0.05710 312 LYS A CA    
2479 C  C     . LYS A 312 ? 0.40300 0.31140 0.54660 -0.05840 0.02700  -0.04650 312 LYS A C     
2480 O  O     . LYS A 312 ? 0.42260 0.33250 0.55540 -0.05440 0.02410  -0.03550 312 LYS A O     
2481 C  CB    . LYS A 312 ? 0.47810 0.41320 0.61820 -0.06350 0.02430  -0.06900 312 LYS A CB    
2482 C  CG    . LYS A 312 ? 0.65070 0.59550 0.79650 -0.06990 0.02500  -0.08310 312 LYS A CG    
2483 C  CD    . LYS A 312 ? 0.64700 0.60560 0.78750 -0.06750 0.02200  -0.09430 312 LYS A CD    
2484 C  CE    . LYS A 312 ? 0.70810 0.68110 0.85020 -0.07310 0.02090  -0.10690 312 LYS A CE    
2485 N  NZ    . LYS A 312 ? 0.80350 0.77030 0.96150 -0.07910 0.02490  -0.11880 312 LYS A NZ    
2486 N  N     . SER A 313 ? 0.45050 0.34760 0.60660 -0.05700 0.02990  -0.05080 313 SER A N     
2487 C  CA    . SER A 313 ? 0.56200 0.44770 0.72050 -0.05020 0.02960  -0.04180 313 SER A CA    
2488 C  C     . SER A 313 ? 0.51610 0.41200 0.66650 -0.04360 0.02520  -0.04270 313 SER A C     
2489 O  O     . SER A 313 ? 0.44370 0.35280 0.58970 -0.04440 0.02370  -0.05280 313 SER A O     
2490 C  CB    . SER A 313 ? 0.54960 0.42050 0.72580 -0.05040 0.03450  -0.04720 313 SER A CB    
2491 O  OG    . SER A 313 ? 0.56230 0.43960 0.74340 -0.04930 0.03460  -0.06150 313 SER A OG    
2492 N  N     . PRO A 314 ? 0.56810 0.45880 0.71630 -0.03700 0.02290  -0.03200 314 PRO A N     
2493 C  CA    . PRO A 314 ? 0.56190 0.46200 0.70420 -0.03110 0.01920  -0.03270 314 PRO A CA    
2494 C  C     . PRO A 314 ? 0.46260 0.36690 0.61230 -0.03000 0.02100  -0.04660 314 PRO A C     
2495 O  O     . PRO A 314 ? 0.42200 0.33960 0.56360 -0.02910 0.01900  -0.05190 314 PRO A O     
2496 C  CB    . PRO A 314 ? 0.55060 0.44090 0.69520 -0.02480 0.01740  -0.02010 314 PRO A CB    
2497 C  CG    . PRO A 314 ? 0.50740 0.38830 0.65000 -0.02780 0.01860  -0.00930 314 PRO A CG    
2498 C  CD    . PRO A 314 ? 0.54890 0.42530 0.69990 -0.03500 0.02370  -0.01830 314 PRO A CD    
2499 N  N     . SER A 315 ? 0.48200 0.37480 0.64660 -0.03020 0.02520  -0.05220 315 SER A N     
2500 C  CA    . SER A 315 ? 0.55970 0.45560 0.73210 -0.02940 0.02770  -0.06650 315 SER A CA    
2501 C  C     . SER A 315 ? 0.52250 0.43170 0.68930 -0.03520 0.02810  -0.07970 315 SER A C     
2502 O  O     . SER A 315 ? 0.42350 0.34300 0.58760 -0.03370 0.02810  -0.08920 315 SER A O     
2503 C  CB    . SER A 315 ? 0.54990 0.42950 0.74070 -0.02910 0.03270  -0.07030 315 SER A CB    
2504 O  OG    . SER A 315 ? 0.74800 0.62060 0.94480 -0.03620 0.03590  -0.07360 315 SER A OG    
2505 N  N     . GLU A 316 ? 0.52300 0.43240 0.68820 -0.04160 0.02850  -0.07990 316 GLU A N     
2506 C  CA    . GLU A 316 ? 0.63280 0.55600 0.79270 -0.04710 0.02790  -0.09120 316 GLU A CA    
2507 C  C     . GLU A 316 ? 0.51580 0.45530 0.65880 -0.04500 0.02320  -0.08820 316 GLU A C     
2508 O  O     . GLU A 316 ? 0.50070 0.45350 0.63820 -0.04590 0.02230  -0.09820 316 GLU A O     
2509 C  CB    . GLU A 316 ? 0.69830 0.61770 0.86230 -0.05440 0.02950  -0.09100 316 GLU A CB    
2510 C  CG    . GLU A 316 ? 0.78600 0.69160 0.96790 -0.05830 0.03490  -0.09840 316 GLU A CG    
2511 C  CD    . GLU A 316 ? 1.10100 1.00100 1.28830 -0.06550 0.03720  -0.09590 316 GLU A CD    
2512 O  OE1   . GLU A 316 ? 0.89260 0.79060 1.07270 -0.06540 0.03600  -0.08240 316 GLU A OE1   
2513 O  OE2   . GLU A 316 ? 1.29250 1.19040 1.49180 -0.07160 0.04070  -0.10790 316 GLU A OE2   
2514 N  N     . LEU A 317 ? 0.39760 0.33590 0.53250 -0.04210 0.02050  -0.07430 317 LEU A N     
2515 C  CA    . LEU A 317 ? 0.41430 0.36570 0.53470 -0.03970 0.01650  -0.07000 317 LEU A CA    
2516 C  C     . LEU A 317 ? 0.33330 0.29100 0.45090 -0.03440 0.01600  -0.07360 317 LEU A C     
2517 O  O     . LEU A 317 ? 0.38230 0.35330 0.49030 -0.03400 0.01440  -0.07730 317 LEU A O     
2518 C  CB    . LEU A 317 ? 0.40540 0.35290 0.51930 -0.03800 0.01410  -0.05530 317 LEU A CB    
2519 C  CG    . LEU A 317 ? 0.39190 0.33700 0.50480 -0.04330 0.01460  -0.05090 317 LEU A CG    
2520 C  CD1   . LEU A 317 ? 0.36170 0.30310 0.46720 -0.04110 0.01260  -0.03690 317 LEU A CD1   
2521 C  CD2   . LEU A 317 ? 0.43670 0.39580 0.54340 -0.04730 0.01330  -0.05780 317 LEU A CD2   
2522 N  N     . LEU A 318 ? 0.41700 0.36530 0.54370 -0.03020 0.01770  -0.07210 318 LEU A N     
2523 C  CA    . LEU A 318 ? 0.44060 0.39410 0.56770 -0.02540 0.01840  -0.07650 318 LEU A CA    
2524 C  C     . LEU A 318 ? 0.44080 0.40260 0.56860 -0.02760 0.02100  -0.09170 318 LEU A C     
2525 O  O     . LEU A 318 ? 0.51020 0.48320 0.63030 -0.02550 0.02080  -0.09540 318 LEU A O     
2526 C  CB    . LEU A 318 ? 0.42820 0.36960 0.56770 -0.02050 0.01990  -0.07280 318 LEU A CB    
2527 C  CG    . LEU A 318 ? 0.46310 0.40090 0.60020 -0.01610 0.01640  -0.05830 318 LEU A CG    
2528 C  CD1   . LEU A 318 ? 0.49430 0.42070 0.64530 -0.01090 0.01770  -0.05540 318 LEU A CD1   
2529 C  CD2   . LEU A 318 ? 0.49230 0.44280 0.61800 -0.01360 0.01360  -0.05540 318 LEU A CD2   
2530 N  N     . GLU A 319 ? 0.44240 0.39870 0.57910 -0.03200 0.02360  -0.10060 319 GLU A N     
2531 C  CA    . GLU A 319 ? 0.56520 0.52960 0.70270 -0.03500 0.02580  -0.11630 319 GLU A CA    
2532 C  C     . GLU A 319 ? 0.53870 0.52030 0.66090 -0.03710 0.02270  -0.11880 319 GLU A C     
2533 O  O     . GLU A 319 ? 0.43220 0.42510 0.54810 -0.03600 0.02320  -0.12710 319 GLU A O     
2534 C  CB    . GLU A 319 ? 0.65790 0.61320 0.80850 -0.04040 0.02880  -0.12490 319 GLU A CB    
2535 C  CG    . GLU A 319 ? 0.91790 0.87870 1.07330 -0.04270 0.03200  -0.14290 319 GLU A CG    
2536 C  CD    . GLU A 319 ? 1.32080 1.27840 1.48250 -0.03740 0.03550  -0.14770 319 GLU A CD    
2537 O  OE1   . GLU A 319 ? 1.51990 1.46610 1.68890 -0.03260 0.03630  -0.13830 319 GLU A OE1   
2538 O  OE2   . GLU A 319 ? 1.39500 1.36240 1.55440 -0.03780 0.03740  -0.16110 319 GLU A OE2   
2539 N  N     . ILE A 320 ? 0.43690 0.42050 0.55320 -0.03980 0.01950  -0.11120 320 ILE A N     
2540 C  CA    . ILE A 320 ? 0.43330 0.43240 0.53600 -0.04100 0.01610  -0.11150 320 ILE A CA    
2541 C  C     . ILE A 320 ? 0.48880 0.49600 0.58000 -0.03570 0.01470  -0.10580 320 ILE A C     
2542 O  O     . ILE A 320 ? 0.34470 0.36520 0.42620 -0.03530 0.01390  -0.11100 320 ILE A O     
2543 C  CB    . ILE A 320 ? 0.47740 0.47600 0.57740 -0.04420 0.01340  -0.10320 320 ILE A CB    
2544 C  CG1   . ILE A 320 ? 0.41840 0.41200 0.52940 -0.05050 0.01510  -0.11030 320 ILE A CG1   
2545 C  CG2   . ILE A 320 ? 0.48670 0.50090 0.57300 -0.04400 0.00970  -0.10170 320 ILE A CG2   
2546 C  CD1   . ILE A 320 ? 0.50450 0.49410 0.61600 -0.05370 0.01410  -0.10130 320 ILE A CD1   
2547 N  N     . CYS A 321 ? 0.38510 0.38430 0.47780 -0.03170 0.01460  -0.09520 321 CYS A N     
2548 C  CA    . CYS A 321 ? 0.34700 0.35230 0.43150 -0.02700 0.01400  -0.08970 321 CYS A CA    
2549 C  C     . CYS A 321 ? 0.32950 0.33990 0.41510 -0.02470 0.01730  -0.09900 321 CYS A C     
2550 O  O     . CYS A 321 ? 0.35840 0.38000 0.43370 -0.02320 0.01730  -0.10000 321 CYS A O     
2551 C  CB    . CYS A 321 ? 0.38030 0.37630 0.46850 -0.02360 0.01300  -0.07790 321 CYS A CB    
2552 S  SG    . CYS A 321 ? 0.37880 0.37190 0.46130 -0.02550 0.00920  -0.06570 321 CYS A SG    
2553 N  N     . GLU A 322 ? 0.36550 0.36720 0.46370 -0.02430 0.02060  -0.10570 322 GLU A N     
2554 C  CA    . GLU A 322 ? 0.52440 0.52990 0.62570 -0.02220 0.02470  -0.11590 322 GLU A CA    
2555 C  C     . GLU A 322 ? 0.44240 0.46100 0.53480 -0.02500 0.02540  -0.12780 322 GLU A C     
2556 O  O     . GLU A 322 ? 0.51890 0.54790 0.60280 -0.02280 0.02700  -0.13070 322 GLU A O     
2557 C  CB    . GLU A 322 ? 0.63730 0.62970 0.75560 -0.02160 0.02820  -0.12150 322 GLU A CB    
2558 C  CG    . GLU A 322 ? 0.77840 0.76000 0.90590 -0.01680 0.02810  -0.11110 322 GLU A CG    
2559 C  CD    . GLU A 322 ? 1.15540 1.12230 1.30040 -0.01630 0.03100  -0.11460 322 GLU A CD    
2560 O  OE1   . GLU A 322 ? 1.15380 1.11980 1.30550 -0.01850 0.03470  -0.12780 322 GLU A OE1   
2561 O  OE2   . GLU A 322 ? 1.09530 1.05140 1.24740 -0.01360 0.02940  -0.10410 322 GLU A OE2   
2562 N  N     . LEU A 323 ? 0.43580 0.45430 0.53040 -0.03000 0.02430  -0.13450 323 LEU A N     
2563 C  CA    . LEU A 323 ? 0.45000 0.48190 0.53710 -0.03320 0.02390  -0.14660 323 LEU A CA    
2564 C  C     . LEU A 323 ? 0.40560 0.45210 0.47520 -0.03210 0.02040  -0.14100 323 LEU A C     
2565 O  O     . LEU A 323 ? 0.40180 0.46100 0.46150 -0.03140 0.02120  -0.14810 323 LEU A O     
2566 C  CB    . LEU A 323 ? 0.47610 0.50510 0.57080 -0.03920 0.02270  -0.15380 323 LEU A CB    
2567 C  CG    . LEU A 323 ? 0.73680 0.75300 0.84880 -0.04140 0.02700  -0.16350 323 LEU A CG    
2568 C  CD1   . LEU A 323 ? 0.66100 0.67410 0.78080 -0.04790 0.02580  -0.16860 323 LEU A CD1   
2569 C  CD2   . LEU A 323 ? 0.69850 0.72080 0.81130 -0.04060 0.03090  -0.17840 323 LEU A CD2   
2570 N  N     . SER A 324 ? 0.42530 0.46990 0.49110 -0.03170 0.01690  -0.12810 324 SER A N     
2571 C  CA    . SER A 324 ? 0.37270 0.42920 0.42360 -0.03030 0.01370  -0.12150 324 SER A CA    
2572 C  C     . SER A 324 ? 0.47690 0.53820 0.52000 -0.02560 0.01610  -0.11760 324 SER A C     
2573 O  O     . SER A 324 ? 0.36370 0.43760 0.39420 -0.02450 0.01560  -0.11870 324 SER A O     
2574 C  CB    . SER A 324 ? 0.35870 0.41100 0.40890 -0.03090 0.01010  -0.10950 324 SER A CB    
2575 O  OG    . SER A 324 ? 0.49790 0.53970 0.55230 -0.02800 0.01110  -0.09930 324 SER A OG    
2576 N  N     . GLN A 325 ? 0.46400 0.51540 0.51490 -0.02280 0.01880  -0.11300 325 GLN A N     
2577 C  CA    . GLN A 325 ? 0.54150 0.59650 0.58830 -0.01870 0.02190  -0.10990 325 GLN A CA    
2578 C  C     . GLN A 325 ? 0.50800 0.57160 0.55120 -0.01830 0.02610  -0.12190 325 GLN A C     
2579 O  O     . GLN A 325 ? 0.50010 0.57390 0.53190 -0.01630 0.02770  -0.12060 325 GLN A O     
2580 C  CB    . GLN A 325 ? 0.43960 0.48300 0.49830 -0.01590 0.02350  -0.10400 325 GLN A CB    
2581 C  CG    . GLN A 325 ? 0.50900 0.54760 0.56680 -0.01510 0.01990  -0.09050 325 GLN A CG    
2582 C  CD    . GLN A 325 ? 0.58510 0.61340 0.65450 -0.01230 0.02050  -0.08500 325 GLN A CD    
2583 O  OE1   . GLN A 325 ? 0.71130 0.74150 0.78320 -0.00910 0.02320  -0.08440 325 GLN A OE1   
2584 N  NE2   . GLN A 325 ? 0.50260 0.52070 0.57900 -0.01340 0.01790  -0.08070 325 GLN A NE2   
2585 N  N     . GLU A 326 ? 0.49290 0.55220 0.54590 -0.02020 0.02810  -0.13360 326 GLU A N     
2586 C  CA    . GLU A 326 ? 0.49500 0.56220 0.54560 -0.02030 0.03240  -0.14720 326 GLU A CA    
2587 C  C     . GLU A 326 ? 0.48840 0.57170 0.52200 -0.02180 0.03020  -0.15110 326 GLU A C     
2588 O  O     . GLU A 326 ? 0.43960 0.53300 0.46280 -0.01970 0.03330  -0.15380 326 GLU A O     
2589 C  CB    . GLU A 326 ? 0.63520 0.69440 0.70010 -0.02300 0.03440  -0.15980 326 GLU A CB    
2590 C  CG    . GLU A 326 ? 0.97520 1.02190 1.05610 -0.02000 0.03880  -0.16010 326 GLU A CG    
2591 C  CD    . GLU A 326 ? 1.24440 1.28680 1.33710 -0.02180 0.04300  -0.17600 326 GLU A CD    
2592 O  OE1   . GLU A 326 ? 0.99810 1.03970 1.09340 -0.02640 0.04130  -0.18390 326 GLU A OE1   
2593 O  OE2   . GLU A 326 ? 0.96300 1.00320 1.06340 -0.01860 0.04830  -0.18100 326 GLU A OE2   
2594 N  N     . LYS A 327 ? 0.36020 0.44620 0.39110 -0.02510 0.02500  -0.15090 327 LYS A N     
2595 C  CA    . LYS A 327 ? 0.46630 0.56830 0.48220 -0.02620 0.02180  -0.15430 327 LYS A CA    
2596 C  C     . LYS A 327 ? 0.43020 0.53990 0.43120 -0.02240 0.02090  -0.14190 327 LYS A C     
2597 O  O     . LYS A 327 ? 0.43230 0.55500 0.41960 -0.02090 0.02180  -0.14490 327 LYS A O     
2598 C  CB    . LYS A 327 ? 0.51620 0.61940 0.53510 -0.03040 0.01620  -0.15630 327 LYS A CB    
2599 C  CG    . LYS A 327 ? 0.67920 0.80050 0.68420 -0.03140 0.01220  -0.16160 327 LYS A CG    
2600 C  CD    . LYS A 327 ? 1.05170 1.17600 1.06350 -0.03670 0.00790  -0.17010 327 LYS A CD    
2601 C  CE    . LYS A 327 ? 1.06440 1.20840 1.06200 -0.03680 0.00280  -0.17410 327 LYS A CE    
2602 N  NZ    . LYS A 327 ? 1.05480 1.20440 1.05990 -0.04230 -0.00150 -0.18440 327 LYS A NZ    
2603 N  N     . MET A 328 ? 0.38660 0.48810 0.39050 -0.02080 0.01940  -0.12830 328 MET A N     
2604 C  CA    . MET A 328 ? 0.41370 0.52010 0.40620 -0.01750 0.01900  -0.11590 328 MET A CA    
2605 C  C     . MET A 328 ? 0.52740 0.63630 0.51540 -0.01430 0.02500  -0.11500 328 MET A C     
2606 O  O     . MET A 328 ? 0.43520 0.55320 0.40980 -0.01200 0.02580  -0.10970 328 MET A O     
2607 C  CB    . MET A 328 ? 0.40780 0.50400 0.40620 -0.01710 0.01640  -0.10320 328 MET A CB    
2608 C  CG    . MET A 328 ? 0.42730 0.52460 0.42580 -0.01960 0.01070  -0.10100 328 MET A CG    
2609 S  SD    . MET A 328 ? 0.43680 0.52440 0.43900 -0.01880 0.00820  -0.08610 328 MET A SD    
2610 C  CE    . MET A 328 ? 0.47690 0.54860 0.49480 -0.01940 0.01070  -0.08640 328 MET A CE    
2611 N  N     . SER A 329 ? 0.40370 0.50450 0.40340 -0.01390 0.02940  -0.12000 329 SER A N     
2612 C  CA    . SER A 329 ? 0.44260 0.54490 0.44180 -0.01100 0.03580  -0.11940 329 SER A CA    
2613 C  C     . SER A 329 ? 0.43380 0.54970 0.41950 -0.01030 0.03970  -0.12720 329 SER A C     
2614 O  O     . SER A 329 ? 0.39350 0.51290 0.37520 -0.00800 0.04530  -0.12470 329 SER A O     
2615 C  CB    . SER A 329 ? 0.43480 0.52620 0.45130 -0.01050 0.03930  -0.12440 329 SER A CB    
2616 O  OG    . SER A 329 ? 0.44510 0.53700 0.46660 -0.01250 0.04080  -0.13900 329 SER A OG    
2617 N  N     . SER A 330 ? 0.45440 0.57850 0.43330 -0.01260 0.03700  -0.13710 330 SER A N     
2618 C  CA    . SER A 330 ? 0.49640 0.63550 0.45960 -0.01210 0.03950  -0.14420 330 SER A CA    
2619 C  C     . SER A 330 ? 0.54870 0.69710 0.49450 -0.00950 0.03840  -0.13200 330 SER A C     
2620 O  O     . SER A 330 ? 0.50680 0.66620 0.43880 -0.00780 0.04230  -0.13380 330 SER A O     
2621 C  CB    . SER A 330 ? 0.48340 0.63000 0.44410 -0.01540 0.03570  -0.15800 330 SER A CB    
2622 O  OG    . SER A 330 ? 0.56880 0.71650 0.52820 -0.01700 0.02810  -0.15290 330 SER A OG    
2623 N  N     . VAL A 331 ? 0.39340 0.53700 0.34020 -0.00900 0.03350  -0.11960 331 VAL A N     
2624 C  CA    . VAL A 331 ? 0.40430 0.55420 0.33710 -0.00630 0.03230  -0.10680 331 VAL A CA    
2625 C  C     . VAL A 331 ? 0.42100 0.56040 0.36040 -0.00470 0.03390  -0.09280 331 VAL A C     
2626 O  O     . VAL A 331 ? 0.32360 0.46610 0.25450 -0.00220 0.03760  -0.08400 331 VAL A O     
2627 C  CB    . VAL A 331 ? 0.47790 0.63470 0.40400 -0.00710 0.02430  -0.10540 331 VAL A CB    
2628 C  CG1   . VAL A 331 ? 0.48960 0.65160 0.40310 -0.00370 0.02280  -0.09130 331 VAL A CG1   
2629 C  CG2   . VAL A 331 ? 0.54310 0.71280 0.46170 -0.00880 0.02230  -0.11960 331 VAL A CG2   
2630 N  N     . PHE A 332 ? 0.38380 0.51100 0.33800 -0.00610 0.03130  -0.09090 332 PHE A N     
2631 C  CA    . PHE A 332 ? 0.37310 0.49080 0.33420 -0.00500 0.03160  -0.07890 332 PHE A CA    
2632 C  C     . PHE A 332 ? 0.32590 0.43650 0.29840 -0.00430 0.03730  -0.07950 332 PHE A C     
2633 O  O     . PHE A 332 ? 0.47100 0.57790 0.45320 -0.00530 0.03890  -0.08880 332 PHE A O     
2634 C  CB    . PHE A 332 ? 0.30490 0.41420 0.27510 -0.00690 0.02550  -0.07610 332 PHE A CB    
2635 C  CG    . PHE A 332 ? 0.34190 0.45740 0.30380 -0.00740 0.01970  -0.07360 332 PHE A CG    
2636 C  CD1   . PHE A 332 ? 0.39630 0.52340 0.34330 -0.00530 0.01930  -0.07040 332 PHE A CD1   
2637 C  CD2   . PHE A 332 ? 0.29980 0.40980 0.26950 -0.00970 0.01470  -0.07380 332 PHE A CD2   
2638 C  CE1   . PHE A 332 ? 0.41880 0.55230 0.35980 -0.00520 0.01340  -0.06800 332 PHE A CE1   
2639 C  CE2   . PHE A 332 ? 0.40630 0.52270 0.37030 -0.01010 0.00950  -0.07180 332 PHE A CE2   
2640 C  CZ    . PHE A 332 ? 0.44110 0.56950 0.39130 -0.00770 0.00850  -0.06910 332 PHE A CZ    
2641 N  N     . GLU A 333 ? 0.40110 0.50980 0.37330 -0.00260 0.04040  -0.06960 333 GLU A N     
2642 C  CA    . GLU A 333 ? 0.35230 0.45430 0.33760 -0.00200 0.04460  -0.06820 333 GLU A CA    
2643 C  C     . GLU A 333 ? 0.38230 0.47320 0.38120 -0.00290 0.03970  -0.06560 333 GLU A C     
2644 O  O     . GLU A 333 ? 0.43570 0.52390 0.43250 -0.00400 0.03400  -0.06220 333 GLU A O     
2645 C  CB    . GLU A 333 ? 0.42890 0.53270 0.41040 -0.00050 0.04900  -0.05830 333 GLU A CB    
2646 C  CG    . GLU A 333 ? 0.64500 0.75860 0.61560 0.00060  0.05610  -0.06020 333 GLU A CG    
2647 C  CD    . GLU A 333 ? 0.80200 0.91650 0.78180 0.00090  0.06260  -0.06870 333 GLU A CD    
2648 O  OE1   . GLU A 333 ? 0.83310 0.94020 0.82860 0.00060  0.06130  -0.07260 333 GLU A OE1   
2649 O  OE2   . GLU A 333 ? 0.91240 1.03520 0.88350 0.00160  0.06920  -0.07140 333 GLU A OE2   
2650 N  N     . ASP A 334 ? 0.35980 0.44490 0.37240 -0.00220 0.04200  -0.06690 334 ASP A N     
2651 C  CA    . ASP A 334 ? 0.40650 0.48140 0.43190 -0.00260 0.03760  -0.06430 334 ASP A CA    
2652 C  C     . ASP A 334 ? 0.37020 0.44160 0.39420 -0.00290 0.03380  -0.05350 334 ASP A C     
2653 O  O     . ASP A 334 ? 0.40010 0.46470 0.42890 -0.00380 0.02880  -0.05090 334 ASP A O     
2654 C  CB    . ASP A 334 ? 0.53940 0.61060 0.57960 -0.00090 0.04080  -0.06710 334 ASP A CB    
2655 C  CG    . ASP A 334 ? 0.65120 0.72210 0.69740 -0.00060 0.04330  -0.07860 334 ASP A CG    
2656 O  OD1   . ASP A 334 ? 0.59270 0.66700 0.63080 -0.00210 0.04300  -0.08530 334 ASP A OD1   
2657 O  OD2   . ASP A 334 ? 0.75080 0.81810 0.81060 0.00130  0.04560  -0.08130 334 ASP A OD2   
2658 N  N     . SER A 335 ? 0.29910 0.37510 0.31670 -0.00220 0.03680  -0.04720 335 SER A N     
2659 C  CA    . SER A 335 ? 0.33100 0.40410 0.34730 -0.00250 0.03440  -0.03760 335 SER A CA    
2660 C  C     . SER A 335 ? 0.32780 0.40250 0.33290 -0.00320 0.03030  -0.03410 335 SER A C     
2661 O  O     . SER A 335 ? 0.26990 0.34160 0.27430 -0.00340 0.02790  -0.02680 335 SER A O     
2662 C  CB    . SER A 335 ? 0.33540 0.41190 0.35110 -0.00170 0.04000  -0.03250 335 SER A CB    
2663 O  OG    . SER A 335 ? 0.44050 0.52460 0.44290 -0.00110 0.04380  -0.03200 335 SER A OG    
2664 N  N     . ASN A 336 ? 0.27790 0.35800 0.27510 -0.00350 0.02950  -0.03990 336 ASN A N     
2665 C  CA    . ASN A 336 ? 0.32100 0.40410 0.30920 -0.00400 0.02500  -0.03810 336 ASN A CA    
2666 C  C     . ASN A 336 ? 0.30640 0.38190 0.30170 -0.00570 0.01960  -0.03690 336 ASN A C     
2667 O  O     . ASN A 336 ? 0.26350 0.33360 0.26760 -0.00680 0.01860  -0.04190 336 ASN A O     
2668 C  CB    . ASN A 336 ? 0.30880 0.40000 0.28930 -0.00430 0.02490  -0.04670 336 ASN A CB    
2669 C  CG    . ASN A 336 ? 0.33740 0.43420 0.30890 -0.00460 0.02000  -0.04530 336 ASN A CG    
2670 O  OD1   . ASN A 336 ? 0.29770 0.39040 0.27380 -0.00620 0.01540  -0.04460 336 ASN A OD1   
2671 N  ND2   . ASN A 336 ? 0.32710 0.43430 0.28590 -0.00300 0.02100  -0.04530 336 ASN A ND2   
2672 N  N     . VAL A 337 ? 0.26610 0.34110 0.25760 -0.00570 0.01660  -0.03010 337 VAL A N     
2673 C  CA    . VAL A 337 ? 0.32880 0.39670 0.32640 -0.00730 0.01240  -0.02760 337 VAL A CA    
2674 C  C     . VAL A 337 ? 0.32790 0.39480 0.32800 -0.00950 0.00910  -0.03400 337 VAL A C     
2675 O  O     . VAL A 337 ? 0.25410 0.31390 0.26100 -0.01100 0.00690  -0.03310 337 VAL A O     
2676 C  CB    . VAL A 337 ? 0.30350 0.37150 0.29680 -0.00670 0.01050  -0.01970 337 VAL A CB    
2677 C  CG1   . VAL A 337 ? 0.27780 0.34420 0.27170 -0.00520 0.01390  -0.01330 337 VAL A CG1   
2678 C  CG2   . VAL A 337 ? 0.34900 0.42540 0.33280 -0.00590 0.00880  -0.01980 337 VAL A CG2   
2679 N  N     . TYR A 338 ? 0.26850 0.34280 0.26320 -0.00990 0.00910  -0.04050 338 TYR A N     
2680 C  CA    . TYR A 338 ? 0.30180 0.37610 0.29990 -0.01260 0.00650  -0.04830 338 TYR A CA    
2681 C  C     . TYR A 338 ? 0.32310 0.39080 0.33070 -0.01340 0.00880  -0.05470 338 TYR A C     
2682 O  O     . TYR A 338 ? 0.27110 0.33230 0.28630 -0.01570 0.00710  -0.05740 338 TYR A O     
2683 C  CB    . TYR A 338 ? 0.35660 0.44270 0.34580 -0.01270 0.00520  -0.05340 338 TYR A CB    
2684 C  CG    . TYR A 338 ? 0.36000 0.45220 0.34130 -0.01110 0.00250  -0.04630 338 TYR A CG    
2685 C  CD1   . TYR A 338 ? 0.36650 0.45530 0.35150 -0.01230 -0.00070 -0.04200 338 TYR A CD1   
2686 C  CD2   . TYR A 338 ? 0.44150 0.54260 0.41200 -0.00820 0.00360  -0.04330 338 TYR A CD2   
2687 C  CE1   . TYR A 338 ? 0.31050 0.40440 0.28990 -0.01040 -0.00280 -0.03550 338 TYR A CE1   
2688 C  CE2   . TYR A 338 ? 0.39910 0.50480 0.36350 -0.00610 0.00130  -0.03580 338 TYR A CE2   
2689 C  CZ    . TYR A 338 ? 0.40010 0.50230 0.36950 -0.00710 -0.00200 -0.03220 338 TYR A CZ    
2690 O  OH    . TYR A 338 ? 0.39360 0.50030 0.35840 -0.00460 -0.00400 -0.02530 338 TYR A OH    
2691 N  N     . MET A 339 ? 0.29820 0.36730 0.30600 -0.01150 0.01290  -0.05670 339 MET A N     
2692 C  CA    . MET A 339 ? 0.33570 0.39830 0.35420 -0.01130 0.01540  -0.06150 339 MET A CA    
2693 C  C     . MET A 339 ? 0.33500 0.38750 0.36240 -0.01090 0.01380  -0.05460 339 MET A C     
2694 O  O     . MET A 339 ? 0.28480 0.32960 0.32150 -0.01170 0.01300  -0.05690 339 MET A O     
2695 C  CB    . MET A 339 ? 0.29010 0.35740 0.30700 -0.00900 0.02070  -0.06420 339 MET A CB    
2696 C  CG    . MET A 339 ? 0.34860 0.42580 0.35720 -0.00930 0.02280  -0.07290 339 MET A CG    
2697 S  SD    . MET A 339 ? 0.48800 0.56190 0.50580 -0.01140 0.02350  -0.08660 339 MET A SD    
2698 C  CE    . MET A 339 ? 0.47960 0.54810 0.50900 -0.00870 0.02910  -0.08850 339 MET A CE    
2699 N  N     . LEU A 340 ? 0.28000 0.33280 0.30460 -0.00960 0.01340  -0.04610 340 LEU A N     
2700 C  CA    . LEU A 340 ? 0.28990 0.33510 0.32140 -0.00920 0.01140  -0.03950 340 LEU A CA    
2701 C  C     . LEU A 340 ? 0.28800 0.32730 0.32100 -0.01140 0.00730  -0.03750 340 LEU A C     
2702 O  O     . LEU A 340 ? 0.31150 0.34330 0.35160 -0.01120 0.00580  -0.03490 340 LEU A O     
2703 C  CB    . LEU A 340 ? 0.30050 0.34820 0.32790 -0.00810 0.01180  -0.03200 340 LEU A CB    
2704 C  CG    . LEU A 340 ? 0.31440 0.36690 0.34170 -0.00630 0.01650  -0.03210 340 LEU A CG    
2705 C  CD1   . LEU A 340 ? 0.29820 0.35190 0.32240 -0.00590 0.01700  -0.02440 340 LEU A CD1   
2706 C  CD2   . LEU A 340 ? 0.34220 0.39160 0.38100 -0.00490 0.01840  -0.03510 340 LEU A CD2   
2707 N  N     . HIS A 341 ? 0.31260 0.35590 0.33880 -0.01320 0.00570  -0.03830 341 HIS A N     
2708 C  CA    . HIS A 341 ? 0.30520 0.34410 0.33290 -0.01570 0.00270  -0.03700 341 HIS A CA    
2709 C  C     . HIS A 341 ? 0.27570 0.30740 0.31230 -0.01710 0.00310  -0.04200 341 HIS A C     
2710 O  O     . HIS A 341 ? 0.32670 0.35020 0.36840 -0.01770 0.00170  -0.03800 341 HIS A O     
2711 C  CB    . HIS A 341 ? 0.31640 0.36260 0.33710 -0.01730 0.00120  -0.03890 341 HIS A CB    
2712 C  CG    . HIS A 341 ? 0.35390 0.39670 0.37680 -0.02020 -0.00120 -0.03740 341 HIS A CG    
2713 N  ND1   . HIS A 341 ? 0.35150 0.39010 0.38060 -0.02310 -0.00130 -0.04270 341 HIS A ND1   
2714 C  CD2   . HIS A 341 ? 0.29710 0.33950 0.31730 -0.02070 -0.00300 -0.03140 341 HIS A CD2   
2715 C  CE1   . HIS A 341 ? 0.39480 0.43100 0.42470 -0.02540 -0.00290 -0.03940 341 HIS A CE1   
2716 N  NE2   . HIS A 341 ? 0.32950 0.36840 0.35380 -0.02390 -0.00400 -0.03280 341 HIS A NE2   
2717 N  N     . MET A 342 ? 0.25810 0.29280 0.29620 -0.01760 0.00510  -0.05070 342 MET A N     
2718 C  CA    . MET A 342 ? 0.29550 0.32310 0.34310 -0.01900 0.00620  -0.05680 342 MET A CA    
2719 C  C     . MET A 342 ? 0.27770 0.29710 0.33470 -0.01630 0.00750  -0.05460 342 MET A C     
2720 O  O     . MET A 342 ? 0.28840 0.29840 0.35390 -0.01690 0.00730  -0.05440 342 MET A O     
2721 C  CB    . MET A 342 ? 0.31210 0.34620 0.35890 -0.02030 0.00820  -0.06800 342 MET A CB    
2722 C  CG    . MET A 342 ? 0.38890 0.43210 0.42790 -0.02300 0.00600  -0.07100 342 MET A CG    
2723 S  SD    . MET A 342 ? 0.41760 0.45590 0.46010 -0.02700 0.00300  -0.06750 342 MET A SD    
2724 C  CE    . MET A 342 ? 0.33620 0.36240 0.39260 -0.02950 0.00530  -0.07370 342 MET A CE    
2725 N  N     . MET A 343 ? 0.27560 0.29860 0.33140 -0.01310 0.00890  -0.05240 343 MET A N     
2726 C  CA    . MET A 343 ? 0.27490 0.29220 0.34000 -0.01010 0.00950  -0.04950 343 MET A CA    
2727 C  C     . MET A 343 ? 0.27740 0.28780 0.34430 -0.00990 0.00570  -0.04040 343 MET A C     
2728 O  O     . MET A 343 ? 0.27260 0.27510 0.34840 -0.00840 0.00500  -0.03840 343 MET A O     
2729 C  CB    . MET A 343 ? 0.35870 0.38290 0.42230 -0.00740 0.01190  -0.04890 343 MET A CB    
2730 C  CG    . MET A 343 ? 0.37510 0.40470 0.43940 -0.00660 0.01650  -0.05810 343 MET A CG    
2731 S  SD    . MET A 343 ? 0.49970 0.53770 0.56170 -0.00400 0.02030  -0.05610 343 MET A SD    
2732 C  CE    . MET A 343 ? 0.58550 0.63210 0.64120 -0.00450 0.02540  -0.06670 343 MET A CE    
2733 N  N     . TYR A 344 ? 0.29670 0.31040 0.35500 -0.01110 0.00350  -0.03470 344 TYR A N     
2734 C  CA    . TYR A 344 ? 0.29250 0.30140 0.35010 -0.01130 -0.00000 -0.02640 344 TYR A CA    
2735 C  C     . TYR A 344 ? 0.31880 0.31970 0.37900 -0.01360 -0.00100 -0.02590 344 TYR A C     
2736 O  O     . TYR A 344 ? 0.30800 0.30180 0.37250 -0.01260 -0.00280 -0.02050 344 TYR A O     
2737 C  CB    . TYR A 344 ? 0.31580 0.33030 0.36390 -0.01240 -0.00130 -0.02210 344 TYR A CB    
2738 C  CG    . TYR A 344 ? 0.32170 0.33240 0.36840 -0.01260 -0.00440 -0.01480 344 TYR A CG    
2739 C  CD1   . TYR A 344 ? 0.32570 0.33640 0.37530 -0.01040 -0.00590 -0.01080 344 TYR A CD1   
2740 C  CD2   . TYR A 344 ? 0.39240 0.40020 0.43520 -0.01530 -0.00580 -0.01230 344 TYR A CD2   
2741 C  CE1   . TYR A 344 ? 0.43600 0.44430 0.48340 -0.01060 -0.00900 -0.00480 344 TYR A CE1   
2742 C  CE2   . TYR A 344 ? 0.42620 0.43100 0.46650 -0.01550 -0.00830 -0.00600 344 TYR A CE2   
2743 C  CZ    . TYR A 344 ? 0.54840 0.55350 0.59050 -0.01320 -0.01010 -0.00240 344 TYR A CZ    
2744 O  OH    . TYR A 344 ? 0.54320 0.54650 0.58200 -0.01350 -0.01280 0.00310  344 TYR A OH    
2745 N  N     . GLN A 345 ? 0.27130 0.27380 0.32930 -0.01670 0.00020  -0.03120 345 GLN A N     
2746 C  CA    . GLN A 345 ? 0.29320 0.28850 0.35510 -0.01970 0.00020  -0.03140 345 GLN A CA    
2747 C  C     . GLN A 345 ? 0.32670 0.31280 0.39980 -0.01810 0.00170  -0.03330 345 GLN A C     
2748 O  O     . GLN A 345 ? 0.30610 0.28300 0.38340 -0.01820 0.00090  -0.02790 345 GLN A O     
2749 C  CB    . GLN A 345 ? 0.31630 0.31670 0.37560 -0.02340 0.00120  -0.03840 345 GLN A CB    
2750 C  CG    . GLN A 345 ? 0.36930 0.37760 0.41920 -0.02490 -0.00060 -0.03560 345 GLN A CG    
2751 C  CD    . GLN A 345 ? 0.36810 0.37170 0.41580 -0.02590 -0.00220 -0.02720 345 GLN A CD    
2752 O  OE1   . GLN A 345 ? 0.39150 0.38710 0.44390 -0.02780 -0.00180 -0.02520 345 GLN A OE1   
2753 N  NE2   . GLN A 345 ? 0.39380 0.40230 0.43450 -0.02460 -0.00370 -0.02220 345 GLN A NE2   
2754 N  N     . ALA A 346 ? 0.32870 0.31720 0.40650 -0.01620 0.00410  -0.04060 346 ALA A N     
2755 C  CA    . ALA A 346 ? 0.34240 0.32270 0.43210 -0.01400 0.00600  -0.04330 346 ALA A CA    
2756 C  C     . ALA A 346 ? 0.32150 0.29620 0.41600 -0.00990 0.00370  -0.03430 346 ALA A C     
2757 O  O     . ALA A 346 ? 0.39730 0.36180 0.50020 -0.00860 0.00360  -0.03140 346 ALA A O     
2758 C  CB    . ALA A 346 ? 0.34590 0.33210 0.43860 -0.01240 0.00920  -0.05290 346 ALA A CB    
2759 N  N     . MET A 347 ? 0.26280 0.24430 0.35200 -0.00770 0.00160  -0.02990 347 MET A N     
2760 C  CA    . MET A 347 ? 0.26880 0.24770 0.36140 -0.00410 -0.00150 -0.02180 347 MET A CA    
2761 C  C     . MET A 347 ? 0.26320 0.23470 0.35300 -0.00530 -0.00440 -0.01340 347 MET A C     
2762 O  O     . MET A 347 ? 0.30850 0.27300 0.40470 -0.00230 -0.00620 -0.00790 347 MET A O     
2763 C  CB    . MET A 347 ? 0.24160 0.23000 0.32830 -0.00300 -0.00290 -0.01960 347 MET A CB    
2764 C  CG    . MET A 347 ? 0.24520 0.23360 0.33740 0.00090  -0.00610 -0.01360 347 MET A CG    
2765 S  SD    . MET A 347 ? 0.29600 0.29520 0.38240 0.00100  -0.00730 -0.01190 347 MET A SD    
2766 C  CE    . MET A 347 ? 0.32750 0.32670 0.42360 0.00550  -0.01170 -0.00640 347 MET A CE    
2767 N  N     . GLY A 348 ? 0.32810 0.30160 0.40820 -0.00940 -0.00480 -0.01220 348 GLY A N     
2768 C  CA    . GLY A 348 ? 0.31620 0.28370 0.39230 -0.01140 -0.00640 -0.00510 348 GLY A CA    
2769 C  C     . GLY A 348 ? 0.33400 0.28990 0.41820 -0.01190 -0.00470 -0.00400 348 GLY A C     
2770 O  O     . GLY A 348 ? 0.41710 0.36590 0.50200 -0.01030 -0.00660 0.00430  348 GLY A O     
2771 N  N     . VAL A 349 ? 0.31750 0.27140 0.40770 -0.01390 -0.00110 -0.01250 349 VAL A N     
2772 C  CA    . VAL A 349 ? 0.31840 0.26050 0.41850 -0.01480 0.00150  -0.01320 349 VAL A CA    
2773 C  C     . VAL A 349 ? 0.33100 0.26590 0.44120 -0.00900 0.00070  -0.00930 349 VAL A C     
2774 O  O     . VAL A 349 ? 0.31310 0.23720 0.42810 -0.00800 0.00060  -0.00240 349 VAL A O     
2775 C  CB    . VAL A 349 ? 0.29760 0.24070 0.40310 -0.01820 0.00540  -0.02530 349 VAL A CB    
2776 C  CG1   . VAL A 349 ? 0.34960 0.27940 0.46750 -0.01920 0.00870  -0.02690 349 VAL A CG1   
2777 C  CG2   . VAL A 349 ? 0.29090 0.24150 0.38780 -0.02360 0.00560  -0.02860 349 VAL A CG2   
2778 N  N     . CYS A 350 ? 0.33740 0.27870 0.45100 -0.00520 0.00020  -0.01340 350 CYS A N     
2779 C  CA    . CYS A 350 ? 0.35890 0.29580 0.48340 0.00090  -0.00080 -0.01050 350 CYS A CA    
2780 C  C     . CYS A 350 ? 0.36230 0.29700 0.48320 0.00400  -0.00580 0.00210  350 CYS A C     
2781 O  O     . CYS A 350 ? 0.34760 0.27310 0.47640 0.00760  -0.00680 0.00830  350 CYS A O     
2782 C  CB    . CYS A 350 ? 0.36950 0.31600 0.49740 0.00390  0.00000  -0.01730 350 CYS A CB    
2783 S  SG    . CYS A 350 ? 0.40250 0.35030 0.53730 0.00210  0.00610  -0.03220 350 CYS A SG    
2784 N  N     . LEU A 351 ? 0.30570 0.24900 0.41450 0.00250  -0.00890 0.00570  351 LEU A N     
2785 C  CA    . LEU A 351 ? 0.35990 0.30330 0.46330 0.00480  -0.01390 0.01630  351 LEU A CA    
2786 C  C     . LEU A 351 ? 0.38250 0.31490 0.48330 0.00340  -0.01390 0.02460  351 LEU A C     
2787 O  O     . LEU A 351 ? 0.33300 0.26050 0.43570 0.00750  -0.01710 0.03350  351 LEU A O     
2788 C  CB    . LEU A 351 ? 0.36900 0.32330 0.46020 0.00260  -0.01630 0.01690  351 LEU A CB    
2789 C  CG    . LEU A 351 ? 0.31500 0.27990 0.40850 0.00480  -0.01720 0.01210  351 LEU A CG    
2790 C  CD1   . LEU A 351 ? 0.34070 0.31420 0.42250 0.00190  -0.01880 0.01280  351 LEU A CD1   
2791 C  CD2   . LEU A 351 ? 0.34300 0.30880 0.44580 0.01070  -0.02080 0.01590  351 LEU A CD2   
2792 N  N     . TYR A 352 ? 0.37930 0.30820 0.47610 -0.00220 -0.01020 0.02180  352 TYR A N     
2793 C  CA    . TYR A 352 ? 0.40590 0.32390 0.50130 -0.00460 -0.00860 0.02890  352 TYR A CA    
2794 C  C     . TYR A 352 ? 0.36360 0.26880 0.47290 -0.00140 -0.00650 0.03070  352 TYR A C     
2795 O  O     . TYR A 352 ? 0.39110 0.28730 0.50020 0.00060  -0.00760 0.04140  352 TYR A O     
2796 C  CB    . TYR A 352 ? 0.41130 0.32970 0.50230 -0.01170 -0.00460 0.02400  352 TYR A CB    
2797 C  CG    . TYR A 352 ? 0.53600 0.44370 0.62560 -0.01460 -0.00230 0.03170  352 TYR A CG    
2798 C  CD1   . TYR A 352 ? 0.64450 0.55220 0.72330 -0.01410 -0.00490 0.04230  352 TYR A CD1   
2799 C  CD2   . TYR A 352 ? 0.53950 0.43700 0.63900 -0.01770 0.00270  0.02850  352 TYR A CD2   
2800 C  CE1   . TYR A 352 ? 0.67500 0.57310 0.75190 -0.01670 -0.00210 0.05030  352 TYR A CE1   
2801 C  CE2   . TYR A 352 ? 0.68430 0.57140 0.78330 -0.02060 0.00560  0.03630  352 TYR A CE2   
2802 C  CZ    . TYR A 352 ? 0.65140 0.53880 0.73860 -0.02010 0.00330  0.04770  352 TYR A CZ    
2803 O  OH    . TYR A 352 ? 0.74330 0.62060 0.82920 -0.02300 0.00680  0.05600  352 TYR A OH    
2804 N  N     . MET A 353 ? 0.36620 0.27050 0.48690 -0.00070 -0.00350 0.02080  353 MET A N     
2805 C  CA    . MET A 353 ? 0.42080 0.31300 0.55670 0.00280  -0.00110 0.02090  353 MET A CA    
2806 C  C     . MET A 353 ? 0.36270 0.25440 0.50480 0.01090  -0.00540 0.02790  353 MET A C     
2807 O  O     . MET A 353 ? 0.36940 0.25070 0.52460 0.01500  -0.00400 0.02990  353 MET A O     
2808 C  CB    . MET A 353 ? 0.42210 0.31510 0.56810 0.00120  0.00350  0.00670  353 MET A CB    
2809 C  CG    . MET A 353 ? 0.49560 0.38750 0.63960 -0.00640 0.00790  -0.00110 353 MET A CG    
2810 S  SD    . MET A 353 ? 0.52110 0.41780 0.67440 -0.00770 0.01220  -0.01880 353 MET A SD    
2811 C  CE    . MET A 353 ? 0.53670 0.41550 0.70980 -0.00510 0.01650  -0.01990 353 MET A CE    
2812 N  N     . GLN A 354 ? 0.36950 0.27280 0.50320 0.01330  -0.01060 0.03100  354 GLN A N     
2813 C  CA    . GLN A 354 ? 0.40460 0.31130 0.54440 0.02070  -0.01550 0.03610  354 GLN A CA    
2814 C  C     . GLN A 354 ? 0.40380 0.31090 0.55960 0.02460  -0.01290 0.02720  354 GLN A C     
2815 O  O     . GLN A 354 ? 0.40770 0.31130 0.57520 0.03120  -0.01490 0.03130  354 GLN A O     
2816 C  CB    . GLN A 354 ? 0.38160 0.27850 0.52210 0.02490  -0.01860 0.04990  354 GLN A CB    
2817 C  CG    . GLN A 354 ? 0.39970 0.29640 0.52360 0.02090  -0.02040 0.05850  354 GLN A CG    
2818 C  CD    . GLN A 354 ? 0.41630 0.30630 0.53800 0.02580  -0.02450 0.07320  354 GLN A CD    
2819 O  OE1   . GLN A 354 ? 0.56490 0.45010 0.69820 0.03270  -0.02660 0.07760  354 GLN A OE1   
2820 N  NE2   . GLN A 354 ? 0.43250 0.32260 0.53920 0.02260  -0.02570 0.08090  354 GLN A NE2   
2821 N  N     . ASP A 355 ? 0.44150 0.35350 0.59760 0.02050  -0.00840 0.01490  355 ASP A N     
2822 C  CA    . ASP A 355 ? 0.39760 0.31300 0.56600 0.02320  -0.00530 0.00470  355 ASP A CA    
2823 C  C     . ASP A 355 ? 0.37120 0.30200 0.53470 0.02440  -0.00820 0.00270  355 ASP A C     
2824 O  O     . ASP A 355 ? 0.32990 0.26930 0.48480 0.02010  -0.00640 -0.00400 355 ASP A O     
2825 C  CB    . ASP A 355 ? 0.45020 0.36360 0.61970 0.01770  0.00100  -0.00740 355 ASP A CB    
2826 C  CG    . ASP A 355 ? 0.45660 0.37500 0.63650 0.01990  0.00490  -0.01920 355 ASP A CG    
2827 O  OD1   . ASP A 355 ? 0.45730 0.37940 0.64620 0.02600  0.00330  -0.01790 355 ASP A OD1   
2828 O  OD2   . ASP A 355 ? 0.53350 0.45320 0.71260 0.01560  0.00950  -0.03010 355 ASP A OD2   
2829 N  N     . TRP A 356 ? 0.28710 0.22130 0.45660 0.03050  -0.01290 0.00890  356 TRP A N     
2830 C  CA    . TRP A 356 ? 0.29120 0.23940 0.45670 0.03150  -0.01640 0.00880  356 TRP A CA    
2831 C  C     . TRP A 356 ? 0.26350 0.22010 0.43630 0.03170  -0.01180 -0.00250 356 TRP A C     
2832 O  O     . TRP A 356 ? 0.27760 0.24480 0.44290 0.02900  -0.01150 -0.00590 356 TRP A O     
2833 C  CB    . TRP A 356 ? 0.33700 0.28750 0.50810 0.03780  -0.02310 0.01820  356 TRP A CB    
2834 C  CG    . TRP A 356 ? 0.32940 0.27120 0.49350 0.03850  -0.02730 0.03000  356 TRP A CG    
2835 C  CD1   . TRP A 356 ? 0.33250 0.26590 0.50540 0.04450  -0.03010 0.03850  356 TRP A CD1   
2836 C  CD2   . TRP A 356 ? 0.32030 0.26100 0.46720 0.03320  -0.02860 0.03510  356 TRP A CD2   
2837 N  NE1   . TRP A 356 ? 0.34550 0.27270 0.50670 0.04310  -0.03300 0.04890  356 TRP A NE1   
2838 C  CE2   . TRP A 356 ? 0.35770 0.28950 0.50310 0.03600  -0.03200 0.04670  356 TRP A CE2   
2839 C  CE3   . TRP A 356 ? 0.32670 0.27320 0.45990 0.02660  -0.02710 0.03130  356 TRP A CE3   
2840 C  CZ2   . TRP A 356 ? 0.35590 0.28480 0.48590 0.03210  -0.03340 0.05390  356 TRP A CZ2   
2841 C  CZ3   . TRP A 356 ? 0.38350 0.32710 0.50280 0.02300  -0.02870 0.03800  356 TRP A CZ3   
2842 C  CH2   . TRP A 356 ? 0.36130 0.29650 0.47890 0.02560  -0.03160 0.04900  356 TRP A CH2   
2843 N  N     . GLU A 357 ? 0.30960 0.26080 0.49700 0.03500  -0.00780 -0.00820 357 GLU A N     
2844 C  CA    . GLU A 357 ? 0.38740 0.34560 0.58210 0.03540  -0.00240 -0.01960 357 GLU A CA    
2845 C  C     . GLU A 357 ? 0.34190 0.30390 0.52400 0.02860  0.00210  -0.02760 357 GLU A C     
2846 O  O     . GLU A 357 ? 0.33000 0.30300 0.50780 0.02710  0.00400  -0.03250 357 GLU A O     
2847 C  CB    . GLU A 357 ? 0.43530 0.38510 0.64780 0.03980  0.00160  -0.02470 357 GLU A CB    
2848 C  CG    . GLU A 357 ? 0.62140 0.56940 0.84930 0.04790  -0.00250 -0.01770 357 GLU A CG    
2849 C  CD    . GLU A 357 ? 0.75860 0.72080 0.99360 0.05140  -0.00380 -0.01980 357 GLU A CD    
2850 O  OE1   . GLU A 357 ? 1.27660 1.24890 1.50630 0.04790  0.00000  -0.02760 357 GLU A OE1   
2851 O  OE2   . GLU A 357 ? 1.19970 1.16350 1.44620 0.05790  -0.00860 -0.01350 357 GLU A OE2   
2852 N  N     . GLY A 358 ? 0.32860 0.28160 0.50530 0.02450  0.00370  -0.02850 358 GLY A N     
2853 C  CA    . GLY A 358 ? 0.31520 0.27190 0.48000 0.01830  0.00690  -0.03550 358 GLY A CA    
2854 C  C     . GLY A 358 ? 0.33800 0.30440 0.48770 0.01520  0.00400  -0.03140 358 GLY A C     
2855 O  O     . GLY A 358 ? 0.33360 0.30920 0.47680 0.01290  0.00660  -0.03740 358 GLY A O     
2856 N  N     . ALA A 359 ? 0.29990 0.26420 0.44420 0.01540  -0.00130 -0.02110 359 ALA A N     
2857 C  CA    . ALA A 359 ? 0.29850 0.27090 0.42960 0.01270  -0.00420 -0.01690 359 ALA A CA    
2858 C  C     . ALA A 359 ? 0.29210 0.27580 0.42480 0.01470  -0.00420 -0.01880 359 ALA A C     
2859 O  O     . ALA A 359 ? 0.24600 0.23740 0.36930 0.01160  -0.00310 -0.02060 359 ALA A O     
2860 C  CB    . ALA A 359 ? 0.30710 0.27500 0.43330 0.01320  -0.00960 -0.00610 359 ALA A CB    
2861 N  N     . LEU A 360 ? 0.25150 0.23630 0.39730 0.01980  -0.00510 -0.01820 360 LEU A N     
2862 C  CA    . LEU A 360 ? 0.30630 0.30190 0.45660 0.02170  -0.00470 -0.02020 360 LEU A CA    
2863 C  C     . LEU A 360 ? 0.28990 0.29180 0.43860 0.01960  0.00200  -0.02960 360 LEU A C     
2864 O  O     . LEU A 360 ? 0.32130 0.33190 0.46410 0.01760  0.00320  -0.03030 360 LEU A O     
2865 C  CB    . LEU A 360 ? 0.30450 0.30040 0.47150 0.02790  -0.00680 -0.01850 360 LEU A CB    
2866 C  CG    . LEU A 360 ? 0.35020 0.35820 0.52470 0.02980  -0.00620 -0.02090 360 LEU A CG    
2867 C  CD1   . LEU A 360 ? 0.32300 0.33780 0.48830 0.02730  -0.01060 -0.01560 360 LEU A CD1   
2868 C  CD2   . LEU A 360 ? 0.33630 0.34500 0.52930 0.03640  -0.00810 -0.02020 360 LEU A CD2   
2869 N  N     . GLN A 361 ? 0.31380 0.31100 0.46770 0.01990  0.00650  -0.03680 361 GLN A N     
2870 C  CA    . GLN A 361 ? 0.37390 0.37700 0.52510 0.01800  0.01290  -0.04640 361 GLN A CA    
2871 C  C     . GLN A 361 ? 0.29510 0.30320 0.42930 0.01300  0.01350  -0.04640 361 GLN A C     
2872 O  O     . GLN A 361 ? 0.35330 0.37030 0.48290 0.01200  0.01690  -0.04930 361 GLN A O     
2873 C  CB    . GLN A 361 ? 0.37670 0.37300 0.53470 0.01840  0.01700  -0.05460 361 GLN A CB    
2874 C  CG    . GLN A 361 ? 0.61880 0.61320 0.79520 0.02390  0.01910  -0.05790 361 GLN A CG    
2875 C  CD    . GLN A 361 ? 0.85640 0.84560 1.03940 0.02390  0.02470  -0.06860 361 GLN A CD    
2876 O  OE1   . GLN A 361 ? 0.87480 0.86970 1.06420 0.02550  0.03030  -0.07720 361 GLN A OE1   
2877 N  NE2   . GLN A 361 ? 0.80370 0.78220 0.98560 0.02180  0.02380  -0.06860 361 GLN A NE2   
2878 N  N     . TYR A 362 ? 0.31390 0.31640 0.43930 0.00990  0.01040  -0.04260 362 TYR A N     
2879 C  CA    . TYR A 362 ? 0.31640 0.32310 0.42650 0.00560  0.01010  -0.04170 362 TYR A CA    
2880 C  C     . TYR A 362 ? 0.26880 0.28170 0.37380 0.00550  0.00770  -0.03520 362 TYR A C     
2881 O  O     . TYR A 362 ? 0.28550 0.30560 0.38220 0.00370  0.01010  -0.03650 362 TYR A O     
2882 C  CB    . TYR A 362 ? 0.34110 0.34030 0.44580 0.00250  0.00750  -0.03940 362 TYR A CB    
2883 C  CG    . TYR A 362 ? 0.30350 0.29870 0.41060 0.00080  0.01080  -0.04780 362 TYR A CG    
2884 C  CD1   . TYR A 362 ? 0.27310 0.27560 0.37410 -0.00130 0.01440  -0.05610 362 TYR A CD1   
2885 C  CD2   . TYR A 362 ? 0.32960 0.31400 0.44510 0.00110  0.01020  -0.04760 362 TYR A CD2   
2886 C  CE1   . TYR A 362 ? 0.26730 0.26720 0.37060 -0.00320 0.01710  -0.06510 362 TYR A CE1   
2887 C  CE2   . TYR A 362 ? 0.38430 0.36470 0.50350 -0.00110 0.01350  -0.05630 362 TYR A CE2   
2888 C  CZ    . TYR A 362 ? 0.33330 0.32190 0.44650 -0.00340 0.01680  -0.06570 362 TYR A CZ    
2889 O  OH    . TYR A 362 ? 0.49110 0.47690 0.60820 -0.00580 0.01970  -0.07550 362 TYR A OH    
2890 N  N     . GLY A 363 ? 0.28570 0.29610 0.39560 0.00750  0.00320  -0.02840 363 GLY A N     
2891 C  CA    . GLY A 363 ? 0.23210 0.24820 0.33890 0.00730  0.00070  -0.02320 363 GLY A CA    
2892 C  C     . GLY A 363 ? 0.22140 0.24640 0.33220 0.00800  0.00480  -0.02670 363 GLY A C     
2893 O  O     . GLY A 363 ? 0.26260 0.29290 0.36650 0.00590  0.00580  -0.02500 363 GLY A O     
2894 N  N     . GLN A 364 ? 0.26980 0.29600 0.39240 0.01110  0.00770  -0.03140 364 GLN A N     
2895 C  CA    . GLN A 364 ? 0.25200 0.28680 0.38020 0.01200  0.01270  -0.03520 364 GLN A CA    
2896 C  C     . GLN A 364 ? 0.25460 0.29410 0.37170 0.00910  0.01850  -0.03930 364 GLN A C     
2897 O  O     . GLN A 364 ? 0.32570 0.37220 0.44180 0.00840  0.02200  -0.03910 364 GLN A O     
2898 C  CB    . GLN A 364 ? 0.26170 0.29650 0.40570 0.01610  0.01500  -0.04000 364 GLN A CB    
2899 C  CG    . GLN A 364 ? 0.28780 0.32150 0.44430 0.01980  0.00920  -0.03510 364 GLN A CG    
2900 C  CD    . GLN A 364 ? 0.31940 0.35140 0.49250 0.02480  0.01060  -0.03900 364 GLN A CD    
2901 O  OE1   . GLN A 364 ? 0.36960 0.40490 0.55570 0.02850  0.00750  -0.03660 364 GLN A OE1   
2902 N  NE2   . GLN A 364 ? 0.36670 0.39380 0.54030 0.02500  0.01500  -0.04540 364 GLN A NE2   
2903 N  N     . LYS A 365 ? 0.25070 0.28650 0.35970 0.00750  0.01940  -0.04280 365 LYS A N     
2904 C  CA    . LYS A 365 ? 0.32210 0.36280 0.41870 0.00510  0.02360  -0.04620 365 LYS A CA    
2905 C  C     . LYS A 365 ? 0.31320 0.35530 0.39700 0.00230  0.02120  -0.04000 365 LYS A C     
2906 O  O     . LYS A 365 ? 0.36530 0.41290 0.43960 0.00100  0.02450  -0.04040 365 LYS A O     
2907 C  CB    . LYS A 365 ? 0.34350 0.38110 0.43730 0.00430  0.02490  -0.05330 365 LYS A CB    
2908 C  CG    . LYS A 365 ? 0.44720 0.48560 0.55160 0.00670  0.02970  -0.06170 365 LYS A CG    
2909 C  CD    . LYS A 365 ? 0.48680 0.51960 0.59160 0.00580  0.03000  -0.06890 365 LYS A CD    
2910 C  CE    . LYS A 365 ? 0.82510 0.86330 0.91560 0.00260  0.03180  -0.07370 365 LYS A CE    
2911 N  NZ    . LYS A 365 ? 1.01620 1.06300 1.10390 0.00320  0.03840  -0.08150 365 LYS A NZ    
2912 N  N     . ILE A 366 ? 0.38850 0.42540 0.47190 0.00170  0.01560  -0.03410 366 ILE A N     
2913 C  CA    . ILE A 366 ? 0.28770 0.32480 0.36000 -0.00080 0.01320  -0.02890 366 ILE A CA    
2914 C  C     . ILE A 366 ? 0.30030 0.34110 0.37310 -0.00100 0.01320  -0.02390 366 ILE A C     
2915 O  O     . ILE A 366 ? 0.27010 0.31340 0.33400 -0.00270 0.01430  -0.02120 366 ILE A O     
2916 C  CB    . ILE A 366 ? 0.27190 0.30190 0.34260 -0.00180 0.00780  -0.02560 366 ILE A CB    
2917 C  CG1   . ILE A 366 ? 0.30330 0.32980 0.37220 -0.00280 0.00830  -0.03060 366 ILE A CG1   
2918 C  CG2   . ILE A 366 ? 0.26570 0.29640 0.32700 -0.00400 0.00550  -0.02030 366 ILE A CG2   
2919 C  CD1   . ILE A 366 ? 0.33500 0.35330 0.40570 -0.00350 0.00420  -0.02770 366 ILE A CD1   
2920 N  N     . ILE A 367 ? 0.21120 0.25250 0.29520 0.00060  0.01200  -0.02280 367 ILE A N     
2921 C  CA    . ILE A 367 ? 0.29290 0.33660 0.37910 -0.00020 0.01040  -0.01840 367 ILE A CA    
2922 C  C     . ILE A 367 ? 0.26370 0.31320 0.34740 -0.00150 0.01590  -0.01800 367 ILE A C     
2923 O  O     . ILE A 367 ? 0.28460 0.33410 0.36360 -0.00340 0.01530  -0.01410 367 ILE A O     
2924 C  CB    . ILE A 367 ? 0.26740 0.31190 0.36730 0.00200  0.00710  -0.01790 367 ILE A CB    
2925 C  CG1   . ILE A 367 ? 0.25770 0.30530 0.35980 0.00060  0.00470  -0.01430 367 ILE A CG1   
2926 C  CG2   . ILE A 367 ? 0.31880 0.36770 0.43020 0.00440  0.01150  -0.02270 367 ILE A CG2   
2927 C  CD1   . ILE A 367 ? 0.22100 0.26470 0.31290 -0.00160 0.00060  -0.01020 367 ILE A CD1   
2928 N  N     . LYS A 368 ? 0.23290 0.28680 0.31970 -0.00050 0.02180  -0.02190 368 LYS A N     
2929 C  CA    . LYS A 368 ? 0.37090 0.42990 0.45530 -0.00170 0.02800  -0.02080 368 LYS A CA    
2930 C  C     . LYS A 368 ? 0.25410 0.31260 0.32340 -0.00310 0.02940  -0.01800 368 LYS A C     
2931 O  O     . LYS A 368 ? 0.30410 0.36320 0.37030 -0.00460 0.03100  -0.01350 368 LYS A O     
2932 C  CB    . LYS A 368 ? 0.47420 0.53860 0.56540 -0.00030 0.03450  -0.02580 368 LYS A CB    
2933 C  CG    . LYS A 368 ? 0.76640 0.83630 0.86010 -0.00160 0.04110  -0.02390 368 LYS A CG    
2934 C  CD    . LYS A 368 ? 0.80500 0.88080 0.90630 -0.00020 0.04790  -0.02930 368 LYS A CD    
2935 C  CE    . LYS A 368 ? 0.79690 0.87800 0.89800 -0.00190 0.05600  -0.02690 368 LYS A CE    
2936 N  NZ    . LYS A 368 ? 0.81440 0.90170 0.91830 -0.00070 0.06390  -0.03230 368 LYS A NZ    
2937 N  N     . PRO A 369 ? 0.32710 0.38470 0.38730 -0.00270 0.02890  -0.02070 369 PRO A N     
2938 C  CA    . PRO A 369 ? 0.29100 0.34880 0.33770 -0.00370 0.02840  -0.01790 369 PRO A CA    
2939 C  C     . PRO A 369 ? 0.27140 0.32480 0.31560 -0.00500 0.02360  -0.01250 369 PRO A C     
2940 O  O     . PRO A 369 ? 0.27200 0.32640 0.30920 -0.00550 0.02490  -0.00820 369 PRO A O     
2941 C  CB    . PRO A 369 ? 0.35770 0.41520 0.39930 -0.00330 0.02680  -0.02330 369 PRO A CB    
2942 C  CG    . PRO A 369 ? 0.36220 0.42130 0.41270 -0.00190 0.03010  -0.02950 369 PRO A CG    
2943 C  CD    . PRO A 369 ? 0.40290 0.46020 0.46650 -0.00130 0.02900  -0.02730 369 PRO A CD    
2944 N  N     . TYR A 370 ? 0.28370 0.33260 0.33350 -0.00520 0.01840  -0.01260 370 TYR A N     
2945 C  CA    . TYR A 370 ? 0.27680 0.32200 0.32490 -0.00650 0.01390  -0.00820 370 TYR A CA    
2946 C  C     . TYR A 370 ? 0.29790 0.34450 0.34920 -0.00740 0.01610  -0.00470 370 TYR A C     
2947 O  O     . TYR A 370 ? 0.31990 0.36510 0.36560 -0.00840 0.01580  -0.00110 370 TYR A O     
2948 C  CB    . TYR A 370 ? 0.30180 0.34270 0.35590 -0.00630 0.00860  -0.00870 370 TYR A CB    
2949 C  CG    . TYR A 370 ? 0.25530 0.29230 0.30370 -0.00680 0.00530  -0.00920 370 TYR A CG    
2950 C  CD1   . TYR A 370 ? 0.26230 0.30050 0.30440 -0.00700 0.00710  -0.01220 370 TYR A CD1   
2951 C  CD2   . TYR A 370 ? 0.30660 0.33910 0.35600 -0.00740 0.00060  -0.00700 370 TYR A CD2   
2952 C  CE1   . TYR A 370 ? 0.31910 0.35420 0.35780 -0.00810 0.00430  -0.01320 370 TYR A CE1   
2953 C  CE2   . TYR A 370 ? 0.32350 0.35220 0.36860 -0.00830 -0.00160 -0.00710 370 TYR A CE2   
2954 C  CZ    . TYR A 370 ? 0.43960 0.46940 0.48010 -0.00880 0.00030  -0.01040 370 TYR A CZ    
2955 O  OH    . TYR A 370 ? 0.30470 0.33120 0.34260 -0.01030 -0.00150 -0.01120 370 TYR A OH    
2956 N  N     . SER A 371 ? 0.33910 0.38830 0.40030 -0.00710 0.01860  -0.00610 371 SER A N     
2957 C  CA    . SER A 371 ? 0.34900 0.39960 0.41600 -0.00850 0.02090  -0.00370 371 SER A CA    
2958 C  C     . SER A 371 ? 0.36060 0.41170 0.42050 -0.00920 0.02620  0.00000  371 SER A C     
2959 O  O     . SER A 371 ? 0.36050 0.40980 0.42180 -0.01080 0.02670  0.00310  371 SER A O     
2960 C  CB    . SER A 371 ? 0.35830 0.41320 0.43830 -0.00810 0.02330  -0.00650 371 SER A CB    
2961 O  OG    . SER A 371 ? 0.52990 0.58420 0.61740 -0.00690 0.01770  -0.00880 371 SER A OG    
2962 N  N     . LYS A 372 ? 0.28710 0.34080 0.33950 -0.00800 0.03020  -0.00030 372 LYS A N     
2963 C  CA    . LYS A 372 ? 0.34820 0.40290 0.39260 -0.00790 0.03530  0.00420  372 LYS A CA    
2964 C  C     . LYS A 372 ? 0.29300 0.34560 0.32590 -0.00720 0.03230  0.00740  372 LYS A C     
2965 O  O     . LYS A 372 ? 0.35740 0.40870 0.38630 -0.00720 0.03470  0.01260  372 LYS A O     
2966 C  CB    . LYS A 372 ? 0.40770 0.46770 0.44890 -0.00680 0.04160  0.00280  372 LYS A CB    
2967 C  CG    . LYS A 372 ? 0.57760 0.64020 0.61060 -0.00520 0.04000  -0.00150 372 LYS A CG    
2968 C  CD    . LYS A 372 ? 0.61410 0.68270 0.64200 -0.00420 0.04700  -0.00260 372 LYS A CD    
2969 C  CE    . LYS A 372 ? 0.72400 0.79610 0.74360 -0.00290 0.04560  -0.00830 372 LYS A CE    
2970 N  NZ    . LYS A 372 ? 0.80750 0.88610 0.82370 -0.00210 0.05250  -0.01140 372 LYS A NZ    
2971 N  N     . HIS A 373 ? 0.24960 0.30180 0.27820 -0.00670 0.02740  0.00430  373 HIS A N     
2972 C  CA    . HIS A 373 ? 0.29110 0.34280 0.31020 -0.00610 0.02450  0.00640  373 HIS A CA    
2973 C  C     . HIS A 373 ? 0.31920 0.36610 0.34020 -0.00710 0.02100  0.00920  373 HIS A C     
2974 O  O     . HIS A 373 ? 0.35660 0.40300 0.37230 -0.00650 0.02100  0.01310  373 HIS A O     
2975 C  CB    . HIS A 373 ? 0.31630 0.36970 0.33130 -0.00570 0.02110  0.00150  373 HIS A CB    
2976 C  CG    . HIS A 373 ? 0.28820 0.34710 0.29850 -0.00450 0.02450  -0.00190 373 HIS A CG    
2977 N  ND1   . HIS A 373 ? 0.31400 0.37720 0.31810 -0.00330 0.02950  0.00120  373 HIS A ND1   
2978 C  CD2   . HIS A 373 ? 0.34010 0.40090 0.35080 -0.00440 0.02390  -0.00850 373 HIS A CD2   
2979 C  CE1   . HIS A 373 ? 0.40540 0.47390 0.40530 -0.00250 0.03180  -0.00360 373 HIS A CE1   
2980 N  NE2   . HIS A 373 ? 0.29140 0.35840 0.29580 -0.00330 0.02840  -0.01000 373 HIS A NE2   
2981 N  N     . TYR A 374 ? 0.29060 0.33470 0.31950 -0.00860 0.01800  0.00720  374 TYR A N     
2982 C  CA    . TYR A 374 ? 0.29900 0.33910 0.32990 -0.00990 0.01460  0.00860  374 TYR A CA    
2983 C  C     . TYR A 374 ? 0.30530 0.34410 0.34200 -0.01100 0.01790  0.01110  374 TYR A C     
2984 O  O     . TYR A 374 ? 0.30490 0.34570 0.34660 -0.01110 0.02210  0.01110  374 TYR A O     
2985 C  CB    . TYR A 374 ? 0.30790 0.34630 0.34360 -0.01080 0.00980  0.00560  374 TYR A CB    
2986 C  CG    . TYR A 374 ? 0.25700 0.29430 0.28760 -0.01050 0.00630  0.00400  374 TYR A CG    
2987 C  CD1   . TYR A 374 ? 0.36400 0.39980 0.38880 -0.01110 0.00420  0.00540  374 TYR A CD1   
2988 C  CD2   . TYR A 374 ? 0.20460 0.24230 0.23750 -0.00990 0.00550  0.00070  374 TYR A CD2   
2989 C  CE1   . TYR A 374 ? 0.26920 0.30420 0.29070 -0.01150 0.00150  0.00380  374 TYR A CE1   
2990 C  CE2   . TYR A 374 ? 0.21250 0.24840 0.24210 -0.01010 0.00280  -0.00100 374 TYR A CE2   
2991 C  CZ    . TYR A 374 ? 0.24800 0.28280 0.27190 -0.01120 0.00080  0.00070  374 TYR A CZ    
2992 O  OH    . TYR A 374 ? 0.22300 0.25620 0.24480 -0.01200 -0.00130 -0.00110 374 TYR A OH    
2993 N  N     . PRO A 375 ? 0.30720 0.34270 0.34410 -0.01200 0.01660  0.01270  375 PRO A N     
2994 C  CA    . PRO A 375 ? 0.31040 0.34400 0.35470 -0.01360 0.01940  0.01380  375 PRO A CA    
2995 C  C     . PRO A 375 ? 0.47920 0.51430 0.53380 -0.01550 0.01790  0.01010  375 PRO A C     
2996 O  O     . PRO A 375 ? 0.32730 0.36410 0.38270 -0.01510 0.01380  0.00730  375 PRO A O     
2997 C  CB    . PRO A 375 ? 0.35890 0.38880 0.40100 -0.01430 0.01710  0.01440  375 PRO A CB    
2998 C  CG    . PRO A 375 ? 0.40050 0.43110 0.43300 -0.01230 0.01490  0.01560  375 PRO A CG    
2999 C  CD    . PRO A 375 ? 0.40390 0.43760 0.43470 -0.01180 0.01290  0.01310  375 PRO A CD    
3000 N  N     . LEU A 376 ? 0.36140 0.39590 0.42440 -0.01740 0.02120  0.01010  376 LEU A N     
3001 C  CA    . LEU A 376 ? 0.55660 0.59410 0.63130 -0.01940 0.02040  0.00640  376 LEU A CA    
3002 C  C     . LEU A 376 ? 0.42820 0.46720 0.50450 -0.01980 0.01290  0.00270  376 LEU A C     
3003 O  O     . LEU A 376 ? 0.46510 0.50820 0.54750 -0.01930 0.01050  0.00030  376 LEU A O     
3004 C  CB    . LEU A 376 ? 0.60270 0.63820 0.68580 -0.02220 0.02480  0.00670  376 LEU A CB    
3005 C  CG    . LEU A 376 ? 0.77320 0.81290 0.87060 -0.02460 0.02700  0.00350  376 LEU A CG    
3006 C  CD1   . LEU A 376 ? 0.54800 0.59170 0.64740 -0.02320 0.03120  0.00440  376 LEU A CD1   
3007 C  CD2   . LEU A 376 ? 0.52250 0.55870 0.62770 -0.02770 0.03230  0.00400  376 LEU A CD2   
3008 N  N     . TYR A 377 ? 0.30030 0.33640 0.37110 -0.02050 0.00940  0.00250  377 TYR A N     
3009 C  CA    . TYR A 377 ? 0.46260 0.50010 0.53270 -0.02100 0.00240  -0.00010 377 TYR A CA    
3010 C  C     . TYR A 377 ? 0.46290 0.49790 0.52180 -0.01930 -0.00050 0.00170  377 TYR A C     
3011 O  O     . TYR A 377 ? 1.20030 1.23320 1.25390 -0.02020 -0.00250 0.00160  377 TYR A O     
3012 C  CB    . TYR A 377 ? 0.42520 0.46220 0.49870 -0.02370 0.00140  -0.00290 377 TYR A CB    
3013 C  CG    . TYR A 377 ? 0.37980 0.41940 0.46600 -0.02620 0.00410  -0.00560 377 TYR A CG    
3014 C  CD1   . TYR A 377 ? 0.34540 0.39120 0.44090 -0.02660 0.00090  -0.00880 377 TYR A CD1   
3015 C  CD2   . TYR A 377 ? 0.35280 0.38880 0.44290 -0.02800 0.01020  -0.00500 377 TYR A CD2   
3016 C  CE1   . TYR A 377 ? 0.36020 0.40940 0.46900 -0.02930 0.00360  -0.01190 377 TYR A CE1   
3017 C  CE2   . TYR A 377 ? 0.32460 0.36260 0.42780 -0.03080 0.01340  -0.00770 377 TYR A CE2   
3018 C  CZ    . TYR A 377 ? 0.30110 0.34620 0.41380 -0.03170 0.01010  -0.01160 377 TYR A CZ    
3019 O  OH    . TYR A 377 ? 0.47890 0.52700 0.60590 -0.03490 0.01340  -0.01480 377 TYR A OH    
3020 N  N     . SER A 378 ? 0.42900 0.46430 0.48490 -0.01720 -0.00030 0.00290  378 SER A N     
3021 C  CA    . SER A 378 ? 0.31590 0.34900 0.36290 -0.01610 -0.00250 0.00420  378 SER A CA    
3022 C  C     . SER A 378 ? 0.28700 0.32020 0.33410 -0.01570 -0.00800 0.00350  378 SER A C     
3023 O  O     . SER A 378 ? 0.24280 0.27820 0.29660 -0.01460 -0.00940 0.00240  378 SER A O     
3024 C  CB    . SER A 378 ? 0.29580 0.32930 0.33990 -0.01440 0.00060  0.00500  378 SER A CB    
3025 O  OG    . SER A 378 ? 0.34570 0.37760 0.38330 -0.01380 -0.00170 0.00530  378 SER A OG    
3026 N  N     . LEU A 379 ? 0.25720 0.28790 0.29700 -0.01620 -0.01080 0.00450  379 LEU A N     
3027 C  CA    . LEU A 379 ? 0.30320 0.33290 0.34130 -0.01570 -0.01540 0.00530  379 LEU A CA    
3028 C  C     . LEU A 379 ? 0.27300 0.30110 0.31190 -0.01390 -0.01500 0.00580  379 LEU A C     
3029 O  O     . LEU A 379 ? 0.23850 0.26570 0.28000 -0.01250 -0.01820 0.00650  379 LEU A O     
3030 C  CB    . LEU A 379 ? 0.36390 0.39120 0.39330 -0.01700 -0.01700 0.00660  379 LEU A CB    
3031 C  CG    . LEU A 379 ? 0.48340 0.51210 0.51110 -0.01890 -0.01780 0.00530  379 LEU A CG    
3032 C  CD1   . LEU A 379 ? 0.46200 0.48860 0.48080 -0.02010 -0.01870 0.00640  379 LEU A CD1   
3033 C  CD2   . LEU A 379 ? 0.36290 0.39510 0.39570 -0.01900 -0.02180 0.00370  379 LEU A CD2   
3034 N  N     . ASN A 380 ? 0.19610 0.22380 0.23270 -0.01360 -0.01120 0.00520  380 ASN A N     
3035 C  CA    . ASN A 380 ? 0.24690 0.27370 0.28470 -0.01230 -0.01020 0.00410  380 ASN A CA    
3036 C  C     . ASN A 380 ? 0.19620 0.22520 0.24300 -0.01050 -0.00950 0.00240  380 ASN A C     
3037 O  O     . ASN A 380 ? 0.18620 0.21360 0.23680 -0.00900 -0.01060 0.00150  380 ASN A O     
3038 C  CB    . ASN A 380 ? 0.29100 0.31890 0.32400 -0.01250 -0.00660 0.00320  380 ASN A CB    
3039 C  CG    . ASN A 380 ? 0.32820 0.35470 0.35400 -0.01390 -0.00730 0.00450  380 ASN A CG    
3040 O  OD1   . ASN A 380 ? 0.39420 0.41870 0.41780 -0.01450 -0.00840 0.00410  380 ASN A OD1   
3041 N  ND2   . ASN A 380 ? 0.21630 0.24380 0.23950 -0.01450 -0.00620 0.00590  380 ASN A ND2   
3042 N  N     . VAL A 381 ? 0.29200 0.32470 0.34330 -0.01070 -0.00730 0.00180  381 VAL A N     
3043 C  CA    . VAL A 381 ? 0.24930 0.28540 0.31050 -0.00940 -0.00600 -0.00020 381 VAL A CA    
3044 C  C     . VAL A 381 ? 0.31160 0.34860 0.37960 -0.00840 -0.01120 0.00010  381 VAL A C     
3045 O  O     . VAL A 381 ? 0.19440 0.23210 0.26950 -0.00610 -0.01230 -0.00090 381 VAL A O     
3046 C  CB    . VAL A 381 ? 0.23390 0.27350 0.29840 -0.01050 -0.00150 -0.00060 381 VAL A CB    
3047 C  CG1   . VAL A 381 ? 0.27220 0.31630 0.34850 -0.00950 0.00020  -0.00280 381 VAL A CG1   
3048 C  CG2   . VAL A 381 ? 0.36580 0.40510 0.42300 -0.01050 0.00350  0.00010  381 VAL A CG2   
3049 N  N     . ALA A 382 ? 0.27280 0.31020 0.33870 -0.01000 -0.01460 0.00130  382 ALA A N     
3050 C  CA    . ALA A 382 ? 0.29400 0.33360 0.36440 -0.00900 -0.02040 0.00190  382 ALA A CA    
3051 C  C     . ALA A 382 ? 0.28780 0.32340 0.35620 -0.00670 -0.02390 0.00430  382 ALA A C     
3052 O  O     . ALA A 382 ? 0.23060 0.26810 0.30700 -0.00400 -0.02690 0.00460  382 ALA A O     
3053 C  CB    . ALA A 382 ? 0.30750 0.34800 0.37300 -0.01140 -0.02320 0.00230  382 ALA A CB    
3054 N  N     . SER A 383 ? 0.24290 0.27310 0.30180 -0.00760 -0.02320 0.00610  383 SER A N     
3055 C  CA    . SER A 383 ? 0.30200 0.32710 0.35880 -0.00600 -0.02560 0.00890  383 SER A CA    
3056 C  C     . SER A 383 ? 0.27270 0.29610 0.33740 -0.00350 -0.02360 0.00720  383 SER A C     
3057 O  O     . SER A 383 ? 0.24600 0.26640 0.31480 -0.00100 -0.02640 0.00930  383 SER A O     
3058 C  CB    . SER A 383 ? 0.31580 0.33600 0.36190 -0.00830 -0.02450 0.01050  383 SER A CB    
3059 O  OG    . SER A 383 ? 0.43990 0.46010 0.48410 -0.00950 -0.01970 0.00790  383 SER A OG    
3060 N  N     . MET A 384 ? 0.25730 0.28270 0.32410 -0.00390 -0.01860 0.00340  384 MET A N     
3061 C  CA    . MET A 384 ? 0.28070 0.30570 0.35540 -0.00160 -0.01590 0.00040  384 MET A CA    
3062 C  C     . MET A 384 ? 0.25600 0.28520 0.34300 0.00130  -0.01770 -0.00030 384 MET A C     
3063 O  O     . MET A 384 ? 0.30250 0.32950 0.39710 0.00430  -0.01850 -0.00070 384 MET A O     
3064 C  CB    . MET A 384 ? 0.28060 0.30780 0.35260 -0.00290 -0.01010 -0.00350 384 MET A CB    
3065 C  CG    . MET A 384 ? 0.31320 0.34000 0.39140 -0.00090 -0.00680 -0.00770 384 MET A CG    
3066 S  SD    . MET A 384 ? 0.32900 0.34730 0.40800 0.00010  -0.00850 -0.00790 384 MET A SD    
3067 C  CE    . MET A 384 ? 0.31800 0.33360 0.38370 -0.00380 -0.00810 -0.00700 384 MET A CE    
3068 N  N     . TRP A 385 ? 0.23650 0.27200 0.32680 0.00040  -0.01820 -0.00070 385 TRP A N     
3069 C  CA    . TRP A 385 ? 0.25270 0.29400 0.35590 0.00290  -0.02080 -0.00150 385 TRP A CA    
3070 C  C     . TRP A 385 ? 0.23500 0.27440 0.33980 0.00570  -0.02780 0.00240  385 TRP A C     
3071 O  O     . TRP A 385 ? 0.23480 0.27620 0.35070 0.00950  -0.02990 0.00240  385 TRP A O     
3072 C  CB    . TRP A 385 ? 0.19530 0.24360 0.30180 0.00060  -0.02060 -0.00280 385 TRP A CB    
3073 C  CG    . TRP A 385 ? 0.21040 0.26220 0.32080 -0.00090 -0.01350 -0.00620 385 TRP A CG    
3074 C  CD1   . TRP A 385 ? 0.21740 0.26960 0.32210 -0.00420 -0.00950 -0.00630 385 TRP A CD1   
3075 C  CD2   . TRP A 385 ? 0.19580 0.25120 0.31650 0.00100  -0.00910 -0.00950 385 TRP A CD2   
3076 N  NE1   . TRP A 385 ? 0.20650 0.26210 0.31640 -0.00450 -0.00290 -0.00870 385 TRP A NE1   
3077 C  CE2   . TRP A 385 ? 0.22130 0.27940 0.34090 -0.00150 -0.00230 -0.01110 385 TRP A CE2   
3078 C  CE3   . TRP A 385 ? 0.21650 0.27300 0.34780 0.00490  -0.00980 -0.01120 385 TRP A CE3   
3079 C  CZ2   . TRP A 385 ? 0.28320 0.34540 0.41050 -0.00070 0.00400  -0.01430 385 TRP A CZ2   
3080 C  CZ3   . TRP A 385 ? 0.25280 0.31370 0.39290 0.00580  -0.00360 -0.01530 385 TRP A CZ3   
3081 C  CH2   . TRP A 385 ? 0.27700 0.34090 0.41460 0.00280  0.00340  -0.01690 385 TRP A CH2   
3082 N  N     . LEU A 386 ? 0.28750 0.32330 0.38120 0.00400  -0.03110 0.00620  386 LEU A N     
3083 C  CA    . LEU A 386 ? 0.33940 0.37330 0.43160 0.00630  -0.03770 0.01110  386 LEU A CA    
3084 C  C     . LEU A 386 ? 0.28100 0.30720 0.37550 0.00940  -0.03740 0.01360  386 LEU A C     
3085 O  O     . LEU A 386 ? 0.28790 0.31430 0.39010 0.01370  -0.04150 0.01650  386 LEU A O     
3086 C  CB    . LEU A 386 ? 0.29430 0.32650 0.37280 0.00330  -0.04000 0.01410  386 LEU A CB    
3087 C  CG    . LEU A 386 ? 0.34880 0.37950 0.42270 0.00530  -0.04650 0.02000  386 LEU A CG    
3088 C  CD1   . LEU A 386 ? 0.34330 0.38170 0.42730 0.00900  -0.05240 0.02050  386 LEU A CD1   
3089 C  CD2   . LEU A 386 ? 0.40530 0.43620 0.46590 0.00170  -0.04770 0.02120  386 LEU A CD2   
3090 N  N     . LYS A 387 ? 0.27450 0.29420 0.36350 0.00740  -0.03250 0.01230  387 LYS A N     
3091 C  CA    . LYS A 387 ? 0.26440 0.27620 0.35700 0.00960  -0.03100 0.01300  387 LYS A CA    
3092 C  C     . LYS A 387 ? 0.24270 0.25670 0.35020 0.01370  -0.02980 0.00970  387 LYS A C     
3093 O  O     . LYS A 387 ? 0.26240 0.27210 0.37730 0.01770  -0.03210 0.01260  387 LYS A O     
3094 C  CB    . LYS A 387 ? 0.33640 0.34320 0.42200 0.00610  -0.02570 0.01000  387 LYS A CB    
3095 C  CG    . LYS A 387 ? 0.35930 0.36200 0.43230 0.00280  -0.02670 0.01380  387 LYS A CG    
3096 C  CD    . LYS A 387 ? 0.46370 0.46370 0.53180 -0.00040 -0.02180 0.00990  387 LYS A CD    
3097 C  CE    . LYS A 387 ? 0.59480 0.59400 0.65130 -0.00410 -0.02210 0.01240  387 LYS A CE    
3098 N  NZ    . LYS A 387 ? 0.65090 0.64910 0.70360 -0.00700 -0.01790 0.00830  387 LYS A NZ    
3099 N  N     . LEU A 388 ? 0.19530 0.21580 0.30750 0.01280  -0.02580 0.00400  388 LEU A N     
3100 C  CA    . LEU A 388 ? 0.22380 0.24820 0.35070 0.01640  -0.02370 0.00010  388 LEU A CA    
3101 C  C     . LEU A 388 ? 0.21930 0.24800 0.35680 0.02080  -0.02990 0.00350  388 LEU A C     
3102 O  O     . LEU A 388 ? 0.24920 0.27570 0.39800 0.02540  -0.03070 0.00380  388 LEU A O     
3103 C  CB    . LEU A 388 ? 0.24800 0.28010 0.37670 0.01420  -0.01850 -0.00550 388 LEU A CB    
3104 C  CG    . LEU A 388 ? 0.29920 0.32920 0.42260 0.01190  -0.01150 -0.01040 388 LEU A CG    
3105 C  CD1   . LEU A 388 ? 0.28690 0.32480 0.41040 0.00980  -0.00660 -0.01380 388 LEU A CD1   
3106 C  CD2   . LEU A 388 ? 0.30060 0.32670 0.43270 0.01500  -0.00860 -0.01440 388 LEU A CD2   
3107 N  N     . GLY A 389 ? 0.22530 0.26060 0.35970 0.01940  -0.03440 0.00580  389 GLY A N     
3108 C  CA    . GLY A 389 ? 0.26570 0.30750 0.40930 0.02320  -0.04120 0.00850  389 GLY A CA    
3109 C  C     . GLY A 389 ? 0.22140 0.25670 0.36500 0.02760  -0.04660 0.01530  389 GLY A C     
3110 O  O     . GLY A 389 ? 0.28360 0.32170 0.43990 0.03300  -0.05010 0.01680  389 GLY A O     
3111 N  N     . ARG A 390 ? 0.21670 0.24330 0.34640 0.02540  -0.04690 0.01970  390 ARG A N     
3112 C  CA    . ARG A 390 ? 0.26240 0.28110 0.38950 0.02890  -0.05130 0.02760  390 ARG A CA    
3113 C  C     . ARG A 390 ? 0.25080 0.26100 0.38850 0.03260  -0.04760 0.02700  390 ARG A C     
3114 O  O     . ARG A 390 ? 0.28310 0.29030 0.42840 0.03810  -0.05160 0.03250  390 ARG A O     
3115 C  CB    . ARG A 390 ? 0.30660 0.31900 0.41620 0.02460  -0.05120 0.03180  390 ARG A CB    
3116 C  CG    . ARG A 390 ? 0.32380 0.34390 0.42390 0.02270  -0.05650 0.03400  390 ARG A CG    
3117 C  CD    . ARG A 390 ? 0.38880 0.40340 0.47190 0.01850  -0.05580 0.03750  390 ARG A CD    
3118 N  NE    . ARG A 390 ? 0.43170 0.45410 0.50670 0.01740  -0.06130 0.03930  390 ARG A NE    
3119 C  CZ    . ARG A 390 ? 0.39420 0.41570 0.45490 0.01320  -0.06080 0.04040  390 ARG A CZ    
3120 N  NH1   . ARG A 390 ? 0.39180 0.40540 0.44510 0.00980  -0.05530 0.04030  390 ARG A NH1   
3121 N  NH2   . ARG A 390 ? 0.58260 0.61190 0.63690 0.01250  -0.06590 0.04080  390 ARG A NH2   
3122 N  N     . LEU A 391 ? 0.25070 0.25750 0.38930 0.02980  -0.04020 0.02030  391 LEU A N     
3123 C  CA    . LEU A 391 ? 0.26140 0.26120 0.41120 0.03280  -0.03600 0.01730  391 LEU A CA    
3124 C  C     . LEU A 391 ? 0.23170 0.23810 0.39940 0.03860  -0.03740 0.01530  391 LEU A C     
3125 O  O     . LEU A 391 ? 0.23720 0.23820 0.41560 0.04410  -0.03890 0.01830  391 LEU A O     
3126 C  CB    . LEU A 391 ? 0.29750 0.29540 0.44360 0.02830  -0.02820 0.00920  391 LEU A CB    
3127 C  CG    . LEU A 391 ? 0.31230 0.30220 0.44440 0.02330  -0.02640 0.01070  391 LEU A CG    
3128 C  CD1   . LEU A 391 ? 0.30240 0.29480 0.42870 0.01870  -0.02030 0.00290  391 LEU A CD1   
3129 C  CD2   . LEU A 391 ? 0.34490 0.32230 0.48080 0.02520  -0.02570 0.01390  391 LEU A CD2   
3130 N  N     . TYR A 392 ? 0.23890 0.25720 0.41060 0.03750  -0.03680 0.01030  392 TYR A N     
3131 C  CA    . TYR A 392 ? 0.24740 0.27490 0.43730 0.04230  -0.03770 0.00730  392 TYR A CA    
3132 C  C     . TYR A 392 ? 0.27760 0.30680 0.47430 0.04830  -0.04640 0.01510  392 TYR A C     
3133 O  O     . TYR A 392 ? 0.27690 0.30500 0.48920 0.05450  -0.04710 0.01540  392 TYR A O     
3134 C  CB    . TYR A 392 ? 0.24980 0.28980 0.44080 0.03890  -0.03600 0.00220  392 TYR A CB    
3135 C  CG    . TYR A 392 ? 0.24930 0.29050 0.44010 0.03530  -0.02690 -0.00590 392 TYR A CG    
3136 C  CD1   . TYR A 392 ? 0.25520 0.29430 0.45690 0.03810  -0.02110 -0.01140 392 TYR A CD1   
3137 C  CD2   . TYR A 392 ? 0.25460 0.29970 0.43440 0.02950  -0.02400 -0.00800 392 TYR A CD2   
3138 C  CE1   . TYR A 392 ? 0.24020 0.28160 0.44010 0.03490  -0.01280 -0.01880 392 TYR A CE1   
3139 C  CE2   . TYR A 392 ? 0.27430 0.32100 0.45250 0.02670  -0.01580 -0.01440 392 TYR A CE2   
3140 C  CZ    . TYR A 392 ? 0.26440 0.30980 0.45210 0.02930  -0.01030 -0.01980 392 TYR A CZ    
3141 O  OH    . TYR A 392 ? 0.33990 0.38770 0.52420 0.02640  -0.00230 -0.02590 392 TYR A OH    
3142 N  N     . MET A 393 ? 0.26320 0.29550 0.44870 0.04670  -0.05300 0.02090  393 MET A N     
3143 C  CA    . MET A 393 ? 0.29800 0.33340 0.48700 0.05220  -0.06220 0.02890  393 MET A CA    
3144 C  C     . MET A 393 ? 0.26430 0.28650 0.45440 0.05700  -0.06310 0.03620  393 MET A C     
3145 O  O     . MET A 393 ? 0.26980 0.29310 0.47280 0.06420  -0.06760 0.04040  393 MET A O     
3146 C  CB    . MET A 393 ? 0.30110 0.34170 0.47460 0.04870  -0.06830 0.03300  393 MET A CB    
3147 C  CG    . MET A 393 ? 0.29660 0.35080 0.47170 0.04480  -0.06890 0.02650  393 MET A CG    
3148 S  SD    . MET A 393 ? 0.36620 0.43590 0.56480 0.05010  -0.07300 0.02280  393 MET A SD    
3149 C  CE    . MET A 393 ? 0.52700 0.61010 0.72190 0.04350  -0.07440 0.01700  393 MET A CE    
3150 N  N     . GLY A 394 ? 0.36190 0.37170 0.53960 0.05300  -0.05850 0.03760  394 GLY A N     
3151 C  CA    . GLY A 394 ? 0.43080 0.42610 0.60950 0.05610  -0.05760 0.04380  394 GLY A CA    
3152 C  C     . GLY A 394 ? 0.42440 0.41550 0.62280 0.06170  -0.05390 0.04020  394 GLY A C     
3153 O  O     . GLY A 394 ? 0.38840 0.37160 0.59460 0.06770  -0.05630 0.04710  394 GLY A O     
3154 N  N     . LEU A 395 ? 0.32470 0.32110 0.53110 0.05970  -0.04780 0.02940  395 LEU A N     
3155 C  CA    . LEU A 395 ? 0.34030 0.33400 0.56530 0.06420  -0.04300 0.02360  395 LEU A CA    
3156 C  C     . LEU A 395 ? 0.34690 0.35320 0.58990 0.07050  -0.04670 0.02230  395 LEU A C     
3157 O  O     . LEU A 395 ? 0.32220 0.32840 0.58240 0.07460  -0.04250 0.01660  395 LEU A O     
3158 C  CB    . LEU A 395 ? 0.35010 0.34300 0.57290 0.05860  -0.03360 0.01230  395 LEU A CB    
3159 C  CG    . LEU A 395 ? 0.36250 0.34280 0.57170 0.05320  -0.02950 0.01230  395 LEU A CG    
3160 C  CD1   . LEU A 395 ? 0.42240 0.40590 0.62510 0.04700  -0.02210 0.00190  395 LEU A CD1   
3161 C  CD2   . LEU A 395 ? 0.38150 0.34730 0.60040 0.05710  -0.02740 0.01440  395 LEU A CD2   
3162 N  N     . GLU A 396 ? 0.38730 0.40470 0.62680 0.07110  -0.05470 0.02710  396 GLU A N     
3163 C  CA    . GLU A 396 ? 0.38290 0.41430 0.63890 0.07690  -0.06010 0.02680  396 GLU A CA    
3164 C  C     . GLU A 396 ? 0.36510 0.40890 0.63090 0.07400  -0.05460 0.01570  396 GLU A C     
3165 O  O     . GLU A 396 ? 0.32300 0.37690 0.60790 0.07910  -0.05600 0.01290  396 GLU A O     
3166 C  CB    . GLU A 396 ? 0.48230 0.50870 0.75660 0.08640  -0.06240 0.03120  396 GLU A CB    
3167 C  CG    . GLU A 396 ? 0.64910 0.66170 0.91610 0.09000  -0.06670 0.04310  396 GLU A CG    
3168 C  CD    . GLU A 396 ? 0.90150 0.92190 1.16380 0.09400  -0.07830 0.05360  396 GLU A CD    
3169 O  OE1   . GLU A 396 ? 0.70680 0.73670 0.95560 0.08880  -0.08200 0.05330  396 GLU A OE1   
3170 O  OE2   . GLU A 396 ? 0.72560 0.74270 0.99770 0.10250  -0.08360 0.06220  396 GLU A OE2   
3171 N  N     . HIS A 397 ? 0.24610 0.28920 0.49890 0.06610  -0.04830 0.00990  397 HIS A N     
3172 C  CA    . HIS A 397 ? 0.25540 0.30980 0.51330 0.06230  -0.04280 0.00090  397 HIS A CA    
3173 C  C     . HIS A 397 ? 0.21670 0.28220 0.46780 0.05880  -0.04860 0.00280  397 HIS A C     
3174 O  O     . HIS A 397 ? 0.26470 0.32990 0.50110 0.05200  -0.04590 0.00110  397 HIS A O     
3175 C  CB    . HIS A 397 ? 0.27240 0.32030 0.51870 0.05600  -0.03330 -0.00540 397 HIS A CB    
3176 C  CG    . HIS A 397 ? 0.34450 0.38270 0.59730 0.05830  -0.02670 -0.00970 397 HIS A CG    
3177 N  ND1   . HIS A 397 ? 0.50150 0.54010 0.75380 0.05500  -0.01730 -0.01880 397 HIS A ND1   
3178 C  CD2   . HIS A 397 ? 0.43470 0.46220 0.69460 0.06360  -0.02780 -0.00650 397 HIS A CD2   
3179 C  CE1   . HIS A 397 ? 0.35910 0.38840 0.61790 0.05780  -0.01310 -0.02200 397 HIS A CE1   
3180 N  NE2   . HIS A 397 ? 0.41330 0.43510 0.67750 0.06300  -0.01910 -0.01460 397 HIS A NE2   
3181 N  N     . LYS A 398 ? 0.26300 0.33890 0.52590 0.06360  -0.05670 0.00580  398 LYS A N     
3182 C  CA    . LYS A 398 ? 0.33530 0.42170 0.59230 0.06100  -0.06420 0.00810  398 LYS A CA    
3183 C  C     . LYS A 398 ? 0.25770 0.35360 0.51440 0.05400  -0.05920 0.00050  398 LYS A C     
3184 O  O     . LYS A 398 ? 0.25430 0.35150 0.49710 0.04850  -0.06110 0.00120  398 LYS A O     
3185 C  CB    . LYS A 398 ? 0.34120 0.43930 0.61420 0.06800  -0.07380 0.01140  398 LYS A CB    
3186 C  CG    . LYS A 398 ? 0.64570 0.73620 0.92410 0.07660  -0.07890 0.01950  398 LYS A CG    
3187 C  CD    . LYS A 398 ? 0.73140 0.81200 0.98980 0.07630  -0.08450 0.02930  398 LYS A CD    
3188 C  CE    . LYS A 398 ? 0.83040 0.90600 1.09650 0.08570  -0.09090 0.03870  398 LYS A CE    
3189 N  NZ    . LYS A 398 ? 0.92500 1.01690 1.20560 0.09210  -0.10090 0.04090  398 LYS A NZ    
3190 N  N     . ALA A 399 ? 0.24240 0.34470 0.51500 0.05440  -0.05250 -0.00670 399 ALA A N     
3191 C  CA    . ALA A 399 ? 0.24780 0.35910 0.52260 0.04830  -0.04680 -0.01340 399 ALA A CA    
3192 C  C     . ALA A 399 ? 0.19260 0.29460 0.44800 0.04130  -0.03960 -0.01460 399 ALA A C     
3193 O  O     . ALA A 399 ? 0.17760 0.28280 0.42430 0.03570  -0.03960 -0.01530 399 ALA A O     
3194 C  CB    . ALA A 399 ? 0.27060 0.39010 0.56650 0.05060  -0.04040 -0.02030 399 ALA A CB    
3195 N  N     . ALA A 400 ? 0.25420 0.34490 0.50330 0.04200  -0.03370 -0.01510 400 ALA A N     
3196 C  CA    . ALA A 400 ? 0.22720 0.30960 0.45800 0.03610  -0.02750 -0.01610 400 ALA A CA    
3197 C  C     . ALA A 400 ? 0.21650 0.29270 0.42920 0.03340  -0.03340 -0.00990 400 ALA A C     
3198 O  O     . ALA A 400 ? 0.21020 0.28490 0.40980 0.02780  -0.03060 -0.01040 400 ALA A O     
3199 C  CB    . ALA A 400 ? 0.24350 0.31640 0.47280 0.03770  -0.02080 -0.01870 400 ALA A CB    
3200 N  N     . GLY A 401 ? 0.25430 0.32690 0.46650 0.03770  -0.04120 -0.00390 401 GLY A N     
3201 C  CA    . GLY A 401 ? 0.29560 0.36310 0.49130 0.03560  -0.04690 0.00230  401 GLY A CA    
3202 C  C     . GLY A 401 ? 0.25470 0.33170 0.44680 0.03160  -0.05060 0.00150  401 GLY A C     
3203 O  O     . GLY A 401 ? 0.28830 0.36200 0.46560 0.02650  -0.04920 0.00190  401 GLY A O     
3204 N  N     . GLU A 402 ? 0.20630 0.29560 0.41340 0.03400  -0.05500 -0.00030 402 GLU A N     
3205 C  CA    . GLU A 402 ? 0.24280 0.34250 0.44980 0.03010  -0.05860 -0.00250 402 GLU A CA    
3206 C  C     . GLU A 402 ? 0.22720 0.32670 0.42940 0.02320  -0.05030 -0.00760 402 GLU A C     
3207 O  O     . GLU A 402 ? 0.22530 0.32440 0.41620 0.01860  -0.05140 -0.00750 402 GLU A O     
3208 C  CB    . GLU A 402 ? 0.31860 0.43260 0.54610 0.03370  -0.06350 -0.00520 402 GLU A CB    
3209 C  CG    . GLU A 402 ? 0.53290 0.65850 0.76160 0.03000  -0.06900 -0.00770 402 GLU A CG    
3210 C  CD    . GLU A 402 ? 0.55960 0.70080 0.80940 0.03380  -0.07530 -0.01030 402 GLU A CD    
3211 O  OE1   . GLU A 402 ? 0.54590 0.68840 0.80690 0.04090  -0.07820 -0.00770 402 GLU A OE1   
3212 O  OE2   . GLU A 402 ? 0.64050 0.79290 0.89650 0.02970  -0.07710 -0.01540 402 GLU A OE2   
3213 N  N     . LYS A 403 ? 0.28190 0.38140 0.49250 0.02300  -0.04180 -0.01190 403 LYS A N     
3214 C  CA    . LYS A 403 ? 0.28500 0.38390 0.49110 0.01720  -0.03310 -0.01570 403 LYS A CA    
3215 C  C     . LYS A 403 ? 0.20830 0.29630 0.39370 0.01370  -0.03100 -0.01290 403 LYS A C     
3216 O  O     . LYS A 403 ? 0.22350 0.31180 0.40170 0.00880  -0.02910 -0.01360 403 LYS A O     
3217 C  CB    . LYS A 403 ? 0.35950 0.45910 0.57520 0.01830  -0.02420 -0.01990 403 LYS A CB    
3218 C  CG    . LYS A 403 ? 0.64530 0.75770 0.88230 0.01930  -0.02280 -0.02450 403 LYS A CG    
3219 C  CD    . LYS A 403 ? 1.07610 1.18910 1.32390 0.02250  -0.01550 -0.02820 403 LYS A CD    
3220 C  CE    . LYS A 403 ? 0.91160 1.03790 1.18330 0.02530  -0.01600 -0.03220 403 LYS A CE    
3221 N  NZ    . LYS A 403 ? 0.82950 0.95610 1.11270 0.02980  -0.01020 -0.03560 403 LYS A NZ    
3222 N  N     . ALA A 404 ? 0.25240 0.33090 0.42940 0.01610  -0.03110 -0.00980 404 ALA A N     
3223 C  CA    . ALA A 404 ? 0.24600 0.31500 0.40490 0.01310  -0.02910 -0.00740 404 ALA A CA    
3224 C  C     . ALA A 404 ? 0.22000 0.28840 0.36830 0.01100  -0.03560 -0.00380 404 ALA A C     
3225 O  O     . ALA A 404 ? 0.21950 0.28520 0.35660 0.00670  -0.03330 -0.00380 404 ALA A O     
3226 C  CB    . ALA A 404 ? 0.27280 0.33240 0.42750 0.01590  -0.02790 -0.00570 404 ALA A CB    
3227 N  N     . LEU A 405 ? 0.20960 0.28100 0.36140 0.01430  -0.04370 -0.00070 405 LEU A N     
3228 C  CA    . LEU A 405 ? 0.25030 0.32220 0.39140 0.01260  -0.05010 0.00250  405 LEU A CA    
3229 C  C     . LEU A 405 ? 0.23320 0.31270 0.37550 0.00790  -0.04970 -0.00180 405 LEU A C     
3230 O  O     . LEU A 405 ? 0.26450 0.34150 0.39460 0.00430  -0.05010 -0.00120 405 LEU A O     
3231 C  CB    . LEU A 405 ? 0.23120 0.30640 0.37600 0.01760  -0.05910 0.00700  405 LEU A CB    
3232 C  CG    . LEU A 405 ? 0.25930 0.32450 0.40050 0.02190  -0.05980 0.01270  405 LEU A CG    
3233 C  CD1   . LEU A 405 ? 0.31030 0.37920 0.45630 0.02750  -0.06870 0.01800  405 LEU A CD1   
3234 C  CD2   . LEU A 405 ? 0.29970 0.35430 0.42300 0.01880  -0.05750 0.01610  405 LEU A CD2   
3235 N  N     . LYS A 406 ? 0.31250 0.40110 0.47050 0.00790  -0.04820 -0.00640 406 LYS A N     
3236 C  CA    . LYS A 406 ? 0.26330 0.35880 0.42570 0.00310  -0.04680 -0.01110 406 LYS A CA    
3237 C  C     . LYS A 406 ? 0.30930 0.39830 0.46340 -0.00160 -0.03820 -0.01230 406 LYS A C     
3238 O  O     . LYS A 406 ? 0.22600 0.31560 0.37570 -0.00590 -0.03770 -0.01400 406 LYS A O     
3239 C  CB    . LYS A 406 ? 0.31770 0.42460 0.50070 0.00400  -0.04640 -0.01560 406 LYS A CB    
3240 C  CG    . LYS A 406 ? 0.33220 0.44900 0.52420 0.00760  -0.05660 -0.01530 406 LYS A CG    
3241 C  CD    . LYS A 406 ? 0.45990 0.58900 0.67430 0.00870  -0.05610 -0.02030 406 LYS A CD    
3242 C  CE    . LYS A 406 ? 0.68290 0.82330 0.90680 0.01310  -0.06720 -0.01980 406 LYS A CE    
3243 N  NZ    . LYS A 406 ? 0.62790 0.77290 0.84310 0.01030  -0.07490 -0.02030 406 LYS A NZ    
3244 N  N     . LYS A 407 ? 0.26910 0.35200 0.42100 -0.00060 -0.03150 -0.01150 407 LYS A N     
3245 C  CA    . LYS A 407 ? 0.29550 0.37220 0.43790 -0.00410 -0.02390 -0.01150 407 LYS A CA    
3246 C  C     . LYS A 407 ? 0.31070 0.38020 0.43650 -0.00570 -0.02620 -0.00840 407 LYS A C     
3247 O  O     . LYS A 407 ? 0.29500 0.36230 0.41470 -0.00930 -0.02290 -0.00890 407 LYS A O     
3248 C  CB    . LYS A 407 ? 0.45560 0.52830 0.59760 -0.00220 -0.01750 -0.01140 407 LYS A CB    
3249 C  CG    . LYS A 407 ? 0.42650 0.50580 0.58320 -0.00160 -0.01210 -0.01510 407 LYS A CG    
3250 C  CD    . LYS A 407 ? 0.83210 0.91290 0.98910 -0.00600 -0.00490 -0.01650 407 LYS A CD    
3251 C  CE    . LYS A 407 ? 0.70200 0.78980 0.87380 -0.00580 0.00130  -0.01980 407 LYS A CE    
3252 N  NZ    . LYS A 407 ? 0.91130 0.99750 1.08320 -0.00240 0.00530  -0.02070 407 LYS A NZ    
3253 N  N     . ALA A 408 ? 0.30850 0.37430 0.42770 -0.00300 -0.03150 -0.00500 408 ALA A N     
3254 C  CA    . ALA A 408 ? 0.30040 0.36020 0.40470 -0.00440 -0.03380 -0.00190 408 ALA A CA    
3255 C  C     . ALA A 408 ? 0.29800 0.36220 0.40000 -0.00710 -0.03790 -0.00330 408 ALA A C     
3256 O  O     . ALA A 408 ? 0.34920 0.41010 0.44210 -0.01020 -0.03580 -0.00360 408 ALA A O     
3257 C  CB    . ALA A 408 ? 0.29810 0.35330 0.39760 -0.00090 -0.03830 0.00240  408 ALA A CB    
3258 N  N     . ILE A 409 ? 0.30250 0.37490 0.41370 -0.00580 -0.04380 -0.00480 409 ILE A N     
3259 C  CA    . ILE A 409 ? 0.27900 0.35740 0.38930 -0.00850 -0.04850 -0.00750 409 ILE A CA    
3260 C  C     . ILE A 409 ? 0.25750 0.33690 0.37140 -0.01330 -0.04280 -0.01230 409 ILE A C     
3261 O  O     . ILE A 409 ? 0.29030 0.36850 0.39680 -0.01640 -0.04330 -0.01390 409 ILE A O     
3262 C  CB    . ILE A 409 ? 0.26420 0.35330 0.38590 -0.00590 -0.05610 -0.00890 409 ILE A CB    
3263 C  CG1   . ILE A 409 ? 0.27160 0.35900 0.38650 -0.00120 -0.06290 -0.00300 409 ILE A CG1   
3264 C  CG2   . ILE A 409 ? 0.27710 0.37450 0.40100 -0.00950 -0.06000 -0.01410 409 ILE A CG2   
3265 C  CD1   . ILE A 409 ? 0.37090 0.46880 0.49780 0.00280  -0.07070 -0.00310 409 ILE A CD1   
3266 N  N     . ALA A 410 ? 0.35780 0.43890 0.48320 -0.01380 -0.03700 -0.01440 410 ALA A N     
3267 C  CA    . ALA A 410 ? 0.34190 0.42340 0.47260 -0.01820 -0.03080 -0.01800 410 ALA A CA    
3268 C  C     . ALA A 410 ? 0.33030 0.40270 0.44780 -0.02040 -0.02610 -0.01600 410 ALA A C     
3269 O  O     . ALA A 410 ? 0.35840 0.43030 0.47610 -0.02400 -0.02410 -0.01880 410 ALA A O     
3270 C  CB    . ALA A 410 ? 0.29360 0.37750 0.43700 -0.01800 -0.02430 -0.01920 410 ALA A CB    
3271 N  N     . ILE A 411 ? 0.28040 0.34600 0.38740 -0.01800 -0.02440 -0.01170 411 ILE A N     
3272 C  CA    . ILE A 411 ? 0.24430 0.30240 0.33920 -0.01940 -0.02060 -0.00950 411 ILE A CA    
3273 C  C     . ILE A 411 ? 0.25260 0.30920 0.33720 -0.02020 -0.02560 -0.00930 411 ILE A C     
3274 O  O     . ILE A 411 ? 0.31600 0.36980 0.39600 -0.02280 -0.02340 -0.01050 411 ILE A O     
3275 C  CB    . ILE A 411 ? 0.27610 0.32880 0.36400 -0.01690 -0.01740 -0.00590 411 ILE A CB    
3276 C  CG1   . ILE A 411 ? 0.32260 0.37700 0.41890 -0.01630 -0.01150 -0.00650 411 ILE A CG1   
3277 C  CG2   . ILE A 411 ? 0.27540 0.32180 0.35150 -0.01800 -0.01460 -0.00380 411 ILE A CG2   
3278 C  CD1   . ILE A 411 ? 0.36670 0.41790 0.45820 -0.01360 -0.00910 -0.00450 411 ILE A CD1   
3279 N  N     . MET A 412 ? 0.28620 0.34470 0.36750 -0.01800 -0.03210 -0.00770 412 MET A N     
3280 C  CA    . MET A 412 ? 0.36110 0.41850 0.43110 -0.01850 -0.03660 -0.00670 412 MET A CA    
3281 C  C     . MET A 412 ? 0.27450 0.33720 0.34630 -0.02160 -0.03930 -0.01170 412 MET A C     
3282 O  O     . MET A 412 ? 0.41240 0.47310 0.47480 -0.02340 -0.03960 -0.01250 412 MET A O     
3283 C  CB    . MET A 412 ? 0.33750 0.39540 0.40390 -0.01500 -0.04260 -0.00260 412 MET A CB    
3284 C  CG    . MET A 412 ? 0.44390 0.49470 0.50600 -0.01270 -0.03980 0.00180  412 MET A CG    
3285 S  SD    . MET A 412 ? 0.43470 0.48470 0.49580 -0.00830 -0.04590 0.00700  412 MET A SD    
3286 C  CE    . MET A 412 ? 0.40610 0.45420 0.45140 -0.00980 -0.04950 0.00990  412 MET A CE    
3287 N  N     . GLU A 413 ? 0.30250 0.37260 0.38720 -0.02240 -0.04100 -0.01580 413 GLU A N     
3288 C  CA    . GLU A 413 ? 0.33230 0.40820 0.42120 -0.02600 -0.04320 -0.02210 413 GLU A CA    
3289 C  C     . GLU A 413 ? 0.38370 0.45380 0.47020 -0.02960 -0.03670 -0.02470 413 GLU A C     
3290 O  O     . GLU A 413 ? 0.41440 0.48580 0.49670 -0.03220 -0.03830 -0.02890 413 GLU A O     
3291 C  CB    . GLU A 413 ? 0.32330 0.40810 0.42950 -0.02670 -0.04450 -0.02650 413 GLU A CB    
3292 C  CG    . GLU A 413 ? 0.38050 0.47420 0.49010 -0.02340 -0.05340 -0.02580 413 GLU A CG    
3293 C  CD    . GLU A 413 ? 0.56970 0.67360 0.69820 -0.02390 -0.05490 -0.03050 413 GLU A CD    
3294 O  OE1   . GLU A 413 ? 0.49340 0.59580 0.63270 -0.02580 -0.04770 -0.03220 413 GLU A OE1   
3295 O  OE2   . GLU A 413 ? 0.56360 0.67750 0.69620 -0.02230 -0.06320 -0.03220 413 GLU A OE2   
3296 N  N     . VAL A 414 ? 0.25660 0.32040 0.34530 -0.02950 -0.02930 -0.02210 414 VAL A N     
3297 C  CA    . VAL A 414 ? 0.25960 0.31700 0.34640 -0.03190 -0.02270 -0.02290 414 VAL A CA    
3298 C  C     . VAL A 414 ? 0.25240 0.30420 0.32430 -0.03100 -0.02290 -0.02020 414 VAL A C     
3299 O  O     . VAL A 414 ? 0.28170 0.33220 0.35010 -0.03320 -0.02240 -0.02360 414 VAL A O     
3300 C  CB    . VAL A 414 ? 0.28360 0.33680 0.37620 -0.03130 -0.01520 -0.01990 414 VAL A CB    
3301 C  CG1   . VAL A 414 ? 0.32990 0.37560 0.41880 -0.03260 -0.00880 -0.01880 414 VAL A CG1   
3302 C  CG2   . VAL A 414 ? 0.27690 0.33570 0.38540 -0.03310 -0.01360 -0.02330 414 VAL A CG2   
3303 N  N     . ALA A 415 ? 0.29920 0.34810 0.36340 -0.02790 -0.02350 -0.01480 415 ALA A N     
3304 C  CA    . ALA A 415 ? 0.28940 0.33330 0.34090 -0.02720 -0.02280 -0.01180 415 ALA A CA    
3305 C  C     . ALA A 415 ? 0.37590 0.42210 0.41820 -0.02760 -0.02830 -0.01260 415 ALA A C     
3306 O  O     . ALA A 415 ? 0.40720 0.45080 0.44160 -0.02870 -0.02680 -0.01320 415 ALA A O     
3307 C  CB    . ALA A 415 ? 0.36830 0.40890 0.41620 -0.02430 -0.02150 -0.00650 415 ALA A CB    
3308 N  N     . HIS A 416 ? 0.31090 0.36250 0.35420 -0.02640 -0.03450 -0.01230 416 HIS A N     
3309 C  CA    . HIS A 416 ? 0.29810 0.35240 0.33140 -0.02620 -0.04010 -0.01170 416 HIS A CA    
3310 C  C     . HIS A 416 ? 0.33150 0.39320 0.36660 -0.02850 -0.04430 -0.01800 416 HIS A C     
3311 O  O     . HIS A 416 ? 0.38260 0.44710 0.40760 -0.02890 -0.04820 -0.01840 416 HIS A O     
3312 C  CB    . HIS A 416 ? 0.30780 0.36330 0.34010 -0.02260 -0.04490 -0.00630 416 HIS A CB    
3313 C  CG    . HIS A 416 ? 0.34040 0.38870 0.36820 -0.02070 -0.04180 -0.00070 416 HIS A CG    
3314 N  ND1   . HIS A 416 ? 0.35830 0.40280 0.37430 -0.02040 -0.04230 0.00340  416 HIS A ND1   
3315 C  CD2   . HIS A 416 ? 0.38800 0.43260 0.42150 -0.01930 -0.03800 0.00110  416 HIS A CD2   
3316 C  CE1   . HIS A 416 ? 0.51240 0.55120 0.52830 -0.01910 -0.03910 0.00700  416 HIS A CE1   
3317 N  NE2   . HIS A 416 ? 0.35240 0.39130 0.37820 -0.01830 -0.03660 0.00550  416 HIS A NE2   
3318 N  N     . GLY A 417 ? 0.30820 0.37370 0.35650 -0.03030 -0.04340 -0.02310 417 GLY A N     
3319 C  CA    . GLY A 417 ? 0.34430 0.41820 0.39740 -0.03280 -0.04790 -0.03020 417 GLY A CA    
3320 C  C     . GLY A 417 ? 0.33070 0.41330 0.38890 -0.03030 -0.05550 -0.02920 417 GLY A C     
3321 O  O     . GLY A 417 ? 0.27680 0.35860 0.32850 -0.02660 -0.05890 -0.02260 417 GLY A O     
3322 N  N     . LYS A 418 ? 0.33840 0.42950 0.40920 -0.03240 -0.05810 -0.03590 418 LYS A N     
3323 C  CA    . LYS A 418 ? 0.38440 0.48560 0.46410 -0.03010 -0.06530 -0.03600 418 LYS A CA    
3324 C  C     . LYS A 418 ? 0.39730 0.50450 0.46540 -0.02710 -0.07440 -0.03280 418 LYS A C     
3325 O  O     . LYS A 418 ? 0.36830 0.48050 0.44060 -0.02300 -0.07980 -0.02880 418 LYS A O     
3326 C  CB    . LYS A 418 ? 0.46360 0.57380 0.55880 -0.03400 -0.06640 -0.04540 418 LYS A CB    
3327 C  CG    . LYS A 418 ? 0.62910 0.73500 0.73920 -0.03630 -0.05790 -0.04710 418 LYS A CG    
3328 C  CD    . LYS A 418 ? 0.68410 0.79760 0.80970 -0.04120 -0.05770 -0.05680 418 LYS A CD    
3329 C  CE    . LYS A 418 ? 0.85780 0.96510 0.99660 -0.04360 -0.04780 -0.05710 418 LYS A CE    
3330 N  NZ    . LYS A 418 ? 1.07270 1.18530 1.22720 -0.04930 -0.04600 -0.06660 418 LYS A NZ    
3331 N  N     . ASP A 419 ? 0.53340 0.63990 0.58690 -0.02880 -0.07550 -0.03430 419 ASP A N     
3332 C  CA    . ASP A 419 ? 0.53120 0.64380 0.57120 -0.02660 -0.08350 -0.03150 419 ASP A CA    
3333 C  C     . ASP A 419 ? 0.43250 0.53620 0.45670 -0.02340 -0.08220 -0.02160 419 ASP A C     
3334 O  O     . ASP A 419 ? 0.50730 0.61420 0.51780 -0.02200 -0.08740 -0.01830 419 ASP A O     
3335 C  CB    . ASP A 419 ? 0.63550 0.75420 0.66850 -0.03090 -0.08540 -0.04040 419 ASP A CB    
3336 C  CG    . ASP A 419 ? 0.85580 0.96460 0.88250 -0.03450 -0.07660 -0.04300 419 ASP A CG    
3337 O  OD1   . ASP A 419 ? 0.50180 0.60110 0.53520 -0.03480 -0.06890 -0.04100 419 ASP A OD1   
3338 O  OD2   . ASP A 419 ? 0.67550 0.78650 0.69050 -0.03680 -0.07730 -0.04730 419 ASP A OD2   
3339 N  N     . HIS A 420 ? 0.40310 0.49610 0.42950 -0.02250 -0.07530 -0.01680 420 HIS A N     
3340 C  CA    . HIS A 420 ? 0.43470 0.51880 0.44840 -0.02050 -0.07290 -0.00850 420 HIS A CA    
3341 C  C     . HIS A 420 ? 0.36410 0.44980 0.37540 -0.01540 -0.07920 -0.00050 420 HIS A C     
3342 O  O     . HIS A 420 ? 0.29320 0.38240 0.31710 -0.01260 -0.08210 0.00030  420 HIS A O     
3343 C  CB    . HIS A 420 ? 0.38360 0.45740 0.40180 -0.02080 -0.06460 -0.00650 420 HIS A CB    
3344 C  CG    . HIS A 420 ? 0.36740 0.43260 0.37300 -0.02040 -0.06090 -0.00070 420 HIS A CG    
3345 N  ND1   . HIS A 420 ? 0.37680 0.43790 0.37750 -0.01710 -0.06260 0.00730  420 HIS A ND1   
3346 C  CD2   . HIS A 420 ? 0.30650 0.36650 0.30470 -0.02310 -0.05520 -0.00200 420 HIS A CD2   
3347 C  CE1   . HIS A 420 ? 0.38010 0.43420 0.37110 -0.01830 -0.05810 0.01040  420 HIS A CE1   
3348 N  NE2   . HIS A 420 ? 0.38660 0.44040 0.37590 -0.02170 -0.05370 0.00480  420 HIS A NE2   
3349 N  N     . PRO A 421 ? 0.48780 0.57080 0.48380 -0.01400 -0.08110 0.00600  421 PRO A N     
3350 C  CA    . PRO A 421 ? 0.51590 0.59850 0.50940 -0.00890 -0.08640 0.01510  421 PRO A CA    
3351 C  C     . PRO A 421 ? 0.46160 0.53760 0.46740 -0.00560 -0.08390 0.01940  421 PRO A C     
3352 O  O     . PRO A 421 ? 0.60840 0.68760 0.62000 -0.00100 -0.08950 0.02370  421 PRO A O     
3353 C  CB    . PRO A 421 ? 0.53800 0.61420 0.51340 -0.00930 -0.08430 0.02150  421 PRO A CB    
3354 C  CG    . PRO A 421 ? 0.49370 0.57340 0.46030 -0.01420 -0.08210 0.01410  421 PRO A CG    
3355 C  CD    . PRO A 421 ? 0.42610 0.50650 0.40670 -0.01720 -0.07800 0.00520  421 PRO A CD    
3356 N  N     . TYR A 422 ? 0.40380 0.47130 0.41330 -0.00760 -0.07590 0.01800  422 TYR A N     
3357 C  CA    . TYR A 422 ? 0.37460 0.43590 0.39510 -0.00520 -0.07240 0.02050  422 TYR A CA    
3358 C  C     . TYR A 422 ? 0.35790 0.42690 0.39500 -0.00320 -0.07530 0.01650  422 TYR A C     
3359 O  O     . TYR A 422 ? 0.42960 0.49710 0.47520 0.00090  -0.07660 0.02020  422 TYR A O     
3360 C  CB    . TYR A 422 ? 0.36880 0.42230 0.38940 -0.00820 -0.06380 0.01810  422 TYR A CB    
3361 C  CG    . TYR A 422 ? 0.36410 0.40920 0.37240 -0.00940 -0.06000 0.02260  422 TYR A CG    
3362 C  CD1   . TYR A 422 ? 0.41330 0.45500 0.41310 -0.00730 -0.06280 0.03000  422 TYR A CD1   
3363 C  CD2   . TYR A 422 ? 0.37230 0.41280 0.37830 -0.01260 -0.05330 0.01980  422 TYR A CD2   
3364 C  CE1   . TYR A 422 ? 0.42660 0.46070 0.41640 -0.00890 -0.05860 0.03390  422 TYR A CE1   
3365 C  CE2   . TYR A 422 ? 0.44200 0.47590 0.43830 -0.01400 -0.04970 0.02320  422 TYR A CE2   
3366 C  CZ    . TYR A 422 ? 0.42320 0.45390 0.41180 -0.01240 -0.05210 0.03010  422 TYR A CZ    
3367 O  OH    . TYR A 422 ? 0.38430 0.40870 0.36480 -0.01420 -0.04790 0.03340  422 TYR A OH    
3368 N  N     . ILE A 423 ? 0.29820 0.37520 0.34080 -0.00630 -0.07600 0.00900  423 ILE A N     
3369 C  CA    . ILE A 423 ? 0.32860 0.41360 0.38820 -0.00540 -0.07790 0.00440  423 ILE A CA    
3370 C  C     . ILE A 423 ? 0.32960 0.42410 0.39320 -0.00110 -0.08740 0.00680  423 ILE A C     
3371 O  O     . ILE A 423 ? 0.39080 0.48880 0.46850 0.00240  -0.08910 0.00730  423 ILE A O     
3372 C  CB    . ILE A 423 ? 0.36740 0.45730 0.43260 -0.01050 -0.07510 -0.00440 423 ILE A CB    
3373 C  CG1   . ILE A 423 ? 0.37590 0.45650 0.44110 -0.01320 -0.06540 -0.00540 423 ILE A CG1   
3374 C  CG2   . ILE A 423 ? 0.45850 0.55900 0.54150 -0.01000 -0.07810 -0.00950 423 ILE A CG2   
3375 C  CD1   . ILE A 423 ? 0.43980 0.52190 0.50860 -0.01810 -0.06120 -0.01260 423 ILE A CD1   
3376 N  N     . SER A 424 ? 0.39950 0.49850 0.45060 -0.00100 -0.09350 0.00850  424 SER A N     
3377 C  CA    . SER A 424 ? 0.49750 0.60540 0.54900 0.00370  -0.10340 0.01240  424 SER A CA    
3378 C  C     . SER A 424 ? 0.38240 0.48310 0.43540 0.00980  -0.10410 0.02210  424 SER A C     
3379 O  O     . SER A 424 ? 0.37730 0.48410 0.44230 0.01470  -0.10950 0.02410  424 SER A O     
3380 C  CB    . SER A 424 ? 0.52840 0.64090 0.56210 0.00260  -0.10870 0.01350  424 SER A CB    
3381 O  OG    . SER A 424 ? 0.76780 0.88670 0.80060 -0.00300 -0.10790 0.00360  424 SER A OG    
3382 N  N     . GLU A 425 ? 0.40300 0.49070 0.44500 0.00930  -0.09850 0.02780  425 GLU A N     
3383 C  CA    . GLU A 425 ? 0.52150 0.60010 0.56480 0.01420  -0.09780 0.03660  425 GLU A CA    
3384 C  C     . GLU A 425 ? 0.43640 0.51380 0.49850 0.01680  -0.09500 0.03450  425 GLU A C     
3385 O  O     . GLU A 425 ? 0.49220 0.56930 0.56230 0.02260  -0.09860 0.03970  425 GLU A O     
3386 C  CB    . GLU A 425 ? 0.58870 0.65380 0.61920 0.01180  -0.09090 0.04090  425 GLU A CB    
3387 C  CG    . GLU A 425 ? 0.88060 0.93680 0.90900 0.01670  -0.09170 0.05110  425 GLU A CG    
3388 C  CD    . GLU A 425 ? 1.04630 1.08960 1.06400 0.01390  -0.08470 0.05500  425 GLU A CD    
3389 O  OE1   . GLU A 425 ? 0.88930 0.93220 0.89610 0.00890  -0.08120 0.05190  425 GLU A OE1   
3390 O  OE2   . GLU A 425 ? 1.17590 1.20970 1.19740 0.01680  -0.08250 0.06080  425 GLU A OE2   
3391 N  N     . ILE A 426 ? 0.35630 0.43280 0.42530 0.01280  -0.08820 0.02700  426 ILE A N     
3392 C  CA    . ILE A 426 ? 0.34900 0.42430 0.43420 0.01440  -0.08390 0.02430  426 ILE A CA    
3393 C  C     . ILE A 426 ? 0.33550 0.42340 0.43720 0.01760  -0.08950 0.02120  426 ILE A C     
3394 O  O     . ILE A 426 ? 0.38200 0.46970 0.49710 0.02190  -0.08910 0.02220  426 ILE A O     
3395 C  CB    . ILE A 426 ? 0.37030 0.44160 0.45640 0.00930  -0.07490 0.01810  426 ILE A CB    
3396 C  CG1   . ILE A 426 ? 0.38140 0.44080 0.45370 0.00710  -0.06950 0.02140  426 ILE A CG1   
3397 C  CG2   . ILE A 426 ? 0.33550 0.40720 0.43770 0.01090  -0.07040 0.01480  426 ILE A CG2   
3398 C  CD1   . ILE A 426 ? 0.38710 0.44410 0.45600 0.00190  -0.06250 0.01620  426 ILE A CD1   
3399 N  N     . LYS A 427 ? 0.32470 0.42400 0.42630 0.01530  -0.09480 0.01680  427 LYS A N     
3400 C  CA    . LYS A 427 ? 0.38130 0.49460 0.49870 0.01800  -0.10130 0.01340  427 LYS A CA    
3401 C  C     . LYS A 427 ? 0.31570 0.43220 0.43570 0.02560  -0.10980 0.02110  427 LYS A C     
3402 O  O     . LYS A 427 ? 0.36040 0.48470 0.49770 0.02980  -0.11290 0.02000  427 LYS A O     
3403 C  CB    . LYS A 427 ? 0.38720 0.51220 0.50340 0.01340  -0.10540 0.00630  427 LYS A CB    
3404 C  CG    . LYS A 427 ? 0.45620 0.58100 0.57930 0.00710  -0.09740 -0.00230 427 LYS A CG    
3405 C  CD    . LYS A 427 ? 0.50270 0.63870 0.62680 0.00240  -0.10120 -0.01020 427 LYS A CD    
3406 C  CE    . LYS A 427 ? 0.53260 0.66500 0.66060 -0.00420 -0.09230 -0.01730 427 LYS A CE    
3407 N  NZ    . LYS A 427 ? 0.82180 0.96190 0.94750 -0.00930 -0.09520 -0.02480 427 LYS A NZ    
3408 N  N     . GLN A 428 ? 0.31900 0.42900 0.42220 0.02750  -0.11290 0.02930  428 GLN A N     
3409 C  CA    . GLN A 428 ? 0.39110 0.50100 0.49510 0.03520  -0.11990 0.03870  428 GLN A CA    
3410 C  C     . GLN A 428 ? 0.44780 0.54840 0.56460 0.03970  -0.11500 0.04200  428 GLN A C     
3411 O  O     . GLN A 428 ? 0.42240 0.52690 0.55100 0.04660  -0.12030 0.04610  428 GLN A O     
3412 C  CB    . GLN A 428 ? 0.42420 0.52690 0.50660 0.03570  -0.12220 0.04770  428 GLN A CB    
3413 C  CG    . GLN A 428 ? 0.52320 0.63500 0.59070 0.03190  -0.12730 0.04500  428 GLN A CG    
3414 C  CD    . GLN A 428 ? 0.56150 0.69200 0.63980 0.03290  -0.13600 0.03870  428 GLN A CD    
3415 O  OE1   . GLN A 428 ? 0.57260 0.71110 0.65820 0.03950  -0.14440 0.04350  428 GLN A OE1   
3416 N  NE2   . GLN A 428 ? 0.72790 0.86540 0.80820 0.02640  -0.13400 0.02790  428 GLN A NE2   
3417 N  N     . GLU A 429 ? 0.37980 0.46830 0.49440 0.03600  -0.10510 0.03980  429 GLU A N     
3418 C  CA    . GLU A 429 ? 0.39100 0.46980 0.51610 0.03930  -0.09940 0.04140  429 GLU A CA    
3419 C  C     . GLU A 429 ? 0.40440 0.49150 0.55140 0.04130  -0.09790 0.03470  429 GLU A C     
3420 O  O     . GLU A 429 ? 0.52890 0.61130 0.68780 0.04590  -0.09560 0.03620  429 GLU A O     
3421 C  CB    . GLU A 429 ? 0.37970 0.44520 0.49510 0.03430  -0.08990 0.04020  429 GLU A CB    
3422 C  CG    . GLU A 429 ? 0.42340 0.47990 0.51940 0.03280  -0.09030 0.04740  429 GLU A CG    
3423 C  CD    . GLU A 429 ? 0.54630 0.59170 0.63390 0.02760  -0.08130 0.04520  429 GLU A CD    
3424 O  OE1   . GLU A 429 ? 0.57110 0.60970 0.66730 0.02830  -0.07540 0.04320  429 GLU A OE1   
3425 O  OE2   . GLU A 429 ? 0.64700 0.69090 0.71980 0.02290  -0.08010 0.04520  429 GLU A OE2   
3426 N  N     . ILE A 430 ? 0.37010 0.46930 0.52270 0.03750  -0.09880 0.02700  430 ILE A N     
3427 C  CA    . ILE A 430 ? 0.42330 0.53280 0.59730 0.03870  -0.09770 0.02030  430 ILE A CA    
3428 C  C     . ILE A 430 ? 0.47230 0.59330 0.65980 0.04590  -0.10750 0.02320  430 ILE A C     
3429 O  O     . ILE A 430 ? 0.85300 0.97680 1.05870 0.05050  -0.10630 0.02190  430 ILE A O     
3430 C  CB    . ILE A 430 ? 0.38140 0.49950 0.55760 0.03170  -0.09490 0.01140  430 ILE A CB    
3431 C  CG1   . ILE A 430 ? 0.34530 0.45240 0.51190 0.02580  -0.08440 0.00860  430 ILE A CG1   
3432 C  CG2   . ILE A 430 ? 0.39410 0.52500 0.59340 0.03290  -0.09470 0.00490  430 ILE A CG2   
3433 C  CD1   . ILE A 430 ? 0.40310 0.51550 0.56800 0.01880  -0.08150 0.00170  430 ILE A CD1   
3434 N  N     . GLU A 431 ? 0.68500 0.81320 0.86330 0.04700  -0.11710 0.02700  431 GLU A N     
3435 C  CA    . GLU A 431 ? 0.88200 1.02220 1.07060 0.05440  -0.12800 0.03090  431 GLU A CA    
3436 C  C     . GLU A 431 ? 1.12620 1.25820 1.30230 0.06050  -0.13360 0.04330  431 GLU A C     
3437 O  O     . GLU A 431 ? 1.12330 1.26370 1.29150 0.06310  -0.14350 0.04800  431 GLU A O     
3438 C  CB    . GLU A 431 ? 0.90570 1.06440 1.09710 0.05170  -0.13610 0.02490  431 GLU A CB    
3439 C  CG    . GLU A 431 ? 0.63380 0.79250 0.80590 0.04410  -0.13590 0.02160  431 GLU A CG    
3440 C  CD    . GLU A 431 ? 0.93110 1.09590 1.11150 0.03630  -0.13020 0.00990  431 GLU A CD    
3441 O  OE1   . GLU A 431 ? 0.66280 0.84030 0.86370 0.03690  -0.13170 0.00360  431 GLU A OE1   
3442 O  OE2   . GLU A 431 ? 0.88170 1.03870 1.04890 0.02970  -0.12390 0.00710  431 GLU A OE2   
3443 N  N     . SER A 432 ? 1.31830 1.43380 1.49240 0.06250  -0.12690 0.04840  432 SER A N     
3444 C  CA    . SER A 432 ? 1.33880 1.44400 1.50560 0.06890  -0.13020 0.06060  432 SER A CA    
3445 C  C     . SER A 432 ? 1.73620 1.83450 1.92180 0.07530  -0.12660 0.06240  432 SER A C     
3446 O  O     . SER A 432 ? 1.96960 2.07100 2.16490 0.08380  -0.13350 0.06930  432 SER A O     
3447 C  CB    . SER A 432 ? 0.97300 1.06270 1.11760 0.06400  -0.12460 0.06520  432 SER A CB    
3448 O  OG    . SER A 432 ? 0.91140 1.00650 1.03740 0.06180  -0.13090 0.06850  432 SER A OG    
3449 N  N     . HIS A 433 ? 1.60920 1.69850 1.79980 0.07150  -0.11580 0.05590  433 HIS A N     
3450 C  CA    . HIS A 433 ? 1.64700 1.73110 1.85660 0.07630  -0.11070 0.05420  433 HIS A CA    
3451 C  C     . HIS A 433 ? 1.58710 1.68760 1.81920 0.07900  -0.11300 0.04680  433 HIS A C     
3452 O  O     . HIS A 433 ? 1.19390 1.30830 1.42680 0.07490  -0.11590 0.04080  433 HIS A O     
3453 C  CB    . HIS A 433 ? 1.53690 1.60810 1.74250 0.07050  -0.09860 0.04850  433 HIS A CB    
3454 C  CG    . HIS A 433 ? 1.41810 1.47210 1.60780 0.06920  -0.09540 0.05550  433 HIS A CG    
3455 N  ND1   . HIS A 433 ? 1.28550 1.32630 1.48170 0.07410  -0.09250 0.06040  433 HIS A ND1   
3456 C  CD2   . HIS A 433 ? 1.29590 1.34360 1.46460 0.06320  -0.09400 0.05800  433 HIS A CD2   
3457 C  CE1   . HIS A 433 ? 1.58050 1.60780 1.76060 0.07100  -0.08950 0.06570  433 HIS A CE1   
3458 N  NE2   . HIS A 433 ? 1.25540 1.28700 1.41860 0.06440  -0.09040 0.06440  433 HIS A NE2   
3459 N  N     . GLU B 4   ? 1.35280 1.11450 1.54840 -0.05320 -0.34360 0.10050  4   GLU B N     
3460 C  CA    . GLU B 4   ? 1.33160 1.11780 1.52450 -0.05610 -0.31620 0.09650  4   GLU B CA    
3461 C  C     . GLU B 4   ? 1.54470 1.36170 1.80500 -0.04950 -0.30540 0.09050  4   GLU B C     
3462 O  O     . GLU B 4   ? 1.86330 1.69630 2.17320 -0.04000 -0.29990 0.08820  4   GLU B O     
3463 C  CB    . GLU B 4   ? 1.24470 1.03600 1.41730 -0.05400 -0.29710 0.09780  4   GLU B CB    
3464 C  CG    . GLU B 4   ? 1.17190 0.93100 1.28850 -0.05820 -0.30450 0.10460  4   GLU B CG    
3465 C  CD    . GLU B 4   ? 1.16850 0.90400 1.22280 -0.07000 -0.30950 0.10700  4   GLU B CD    
3466 O  OE1   . GLU B 4   ? 1.00210 0.74870 1.04690 -0.07580 -0.29950 0.10310  4   GLU B OE1   
3467 O  OE2   . GLU B 4   ? 1.23400 0.93750 1.24730 -0.07300 -0.32180 0.11300  4   GLU B OE2   
3468 N  N     . GLY B 5   ? 1.52590 1.34830 1.78580 -0.05380 -0.29960 0.08840  5   GLY B N     
3469 C  CA    . GLY B 5   ? 1.49990 1.34600 1.81760 -0.04780 -0.28770 0.08400  5   GLY B CA    
3470 C  C     . GLY B 5   ? 1.76530 1.63930 2.09560 -0.04410 -0.25620 0.08050  5   GLY B C     
3471 O  O     . GLY B 5   ? 1.31500 1.20960 1.69890 -0.03710 -0.24200 0.07650  5   GLY B O     
3472 N  N     . LEU B 6   ? 1.75290 1.62680 2.03250 -0.04800 -0.24420 0.08170  6   LEU B N     
3473 C  CA    . LEU B 6   ? 1.02920 0.92690 1.30980 -0.04370 -0.21590 0.07850  6   LEU B CA    
3474 C  C     . LEU B 6   ? 0.75250 0.65640 1.03670 -0.04110 -0.20980 0.07730  6   LEU B C     
3475 O  O     . LEU B 6   ? 0.60790 0.49530 0.84540 -0.04530 -0.21570 0.08080  6   LEU B O     
3476 C  CB    . LEU B 6   ? 0.88410 0.77710 1.10840 -0.04940 -0.20740 0.08030  6   LEU B CB    
3477 C  CG    . LEU B 6   ? 0.92830 0.81320 1.14430 -0.05100 -0.21400 0.08210  6   LEU B CG    
3478 C  CD1   . LEU B 6   ? 1.07530 0.95290 1.23220 -0.05790 -0.20680 0.08380  6   LEU B CD1   
3479 C  CD2   . LEU B 6   ? 0.86930 0.77560 1.13530 -0.04270 -0.20160 0.07920  6   LEU B CD2   
3480 N  N     . GLY B 7   ? 0.71260 0.63550 1.04320 -0.03040 -0.19110 0.07230  7   GLY B N     
3481 C  CA    . GLY B 7   ? 0.74790 0.66770 1.07580 -0.02150 -0.17690 0.06970  7   GLY B CA    
3482 C  C     . GLY B 7   ? 0.75130 0.66310 1.02690 -0.02510 -0.16200 0.06900  7   GLY B C     
3483 O  O     . GLY B 7   ? 0.64580 0.56780 0.90700 -0.02870 -0.15020 0.06750  7   GLY B O     
3484 N  N     . GLY B 8   ? 0.63630 0.52820 0.88350 -0.02560 -0.16150 0.06920  8   GLY B N     
3485 C  CA    . GLY B 8   ? 0.53440 0.41580 0.73410 -0.03210 -0.14680 0.06660  8   GLY B CA    
3486 C  C     . GLY B 8   ? 0.53050 0.40290 0.67860 -0.04480 -0.15510 0.07230  8   GLY B C     
3487 O  O     . GLY B 8   ? 0.47880 0.34800 0.59180 -0.05160 -0.14080 0.06900  8   GLY B O     
3488 N  N     . LEU B 9   ? 0.54600 0.41400 0.69090 -0.04850 -0.17770 0.07930  9   LEU B N     
3489 C  CA    . LEU B 9   ? 0.56200 0.41970 0.65820 -0.06020 -0.18540 0.08360  9   LEU B CA    
3490 C  C     . LEU B 9   ? 0.56450 0.39910 0.64690 -0.06460 -0.21020 0.08960  9   LEU B C     
3491 O  O     . LEU B 9   ? 0.61070 0.44380 0.72930 -0.05860 -0.22510 0.09060  9   LEU B O     
3492 C  CB    . LEU B 9   ? 0.56470 0.44000 0.66560 -0.06220 -0.18570 0.08270  9   LEU B CB    
3493 C  CG    . LEU B 9   ? 0.53340 0.42970 0.64460 -0.05780 -0.15960 0.07630  9   LEU B CG    
3494 C  CD1   . LEU B 9   ? 0.57650 0.48820 0.70510 -0.05510 -0.16110 0.07720  9   LEU B CD1   
3495 C  CD2   . LEU B 9   ? 0.48180 0.37490 0.54740 -0.06540 -0.14080 0.07210  9   LEU B CD2   
3496 N  N     . GLU B 10  ? 0.61370 0.42850 0.64300 -0.07520 -0.21210 0.09260  10  GLU B N     
3497 C  CA    . GLU B 10  ? 0.69840 0.48500 0.70340 -0.08040 -0.23300 0.09760  10  GLU B CA    
3498 C  C     . GLU B 10  ? 0.71060 0.48160 0.66270 -0.09240 -0.23110 0.09750  10  GLU B C     
3499 O  O     . GLU B 10  ? 0.65550 0.43310 0.58170 -0.09750 -0.21090 0.09500  10  GLU B O     
3500 C  CB    . GLU B 10  ? 0.84400 0.60900 0.83830 -0.07770 -0.23510 0.10270  10  GLU B CB    
3501 C  CG    . GLU B 10  ? 0.80500 0.55710 0.75500 -0.08490 -0.21590 0.10410  10  GLU B CG    
3502 C  CD    . GLU B 10  ? 0.91090 0.63830 0.85170 -0.08320 -0.21830 0.10990  10  GLU B CD    
3503 O  OE1   . GLU B 10  ? 0.94620 0.66220 0.90620 -0.07680 -0.23790 0.11380  10  GLU B OE1   
3504 O  OE2   . GLU B 10  ? 0.92500 0.64410 0.84140 -0.08860 -0.20020 0.11040  10  GLU B OE2   
3505 N  N     . ARG B 11  ? 0.63040 0.37900 0.56860 -0.09590 -0.25080 0.09940  11  ARG B N     
3506 C  CA    . ARG B 11  ? 0.68960 0.41190 0.57200 -0.10560 -0.25070 0.10000  11  ARG B CA    
3507 C  C     . ARG B 11  ? 0.77190 0.46820 0.61310 -0.10820 -0.24660 0.10600  11  ARG B C     
3508 O  O     . ARG B 11  ? 0.78330 0.46950 0.63830 -0.10240 -0.25830 0.11130  11  ARG B O     
3509 C  CB    . ARG B 11  ? 0.78720 0.49020 0.67060 -0.10540 -0.27400 0.10070  11  ARG B CB    
3510 C  CG    . ARG B 11  ? 0.87140 0.54030 0.69500 -0.11250 -0.27710 0.10210  11  ARG B CG    
3511 C  CD    . ARG B 11  ? 0.90390 0.55760 0.73200 -0.11090 -0.29840 0.10150  11  ARG B CD    
3512 N  NE    . ARG B 11  ? 1.16480 0.77720 0.93970 -0.11390 -0.31270 0.10520  11  ARG B NE    
3513 C  CZ    . ARG B 11  ? 1.42930 1.02020 1.19530 -0.11250 -0.33370 0.10500  11  ARG B CZ    
3514 N  NH1   . ARG B 11  ? 1.19710 0.80540 1.00720 -0.10830 -0.34180 0.10170  11  ARG B NH1   
3515 N  NH2   . ARG B 11  ? 1.69300 1.24350 1.40470 -0.11490 -0.34610 0.10860  11  ARG B NH2   
3516 N  N     . PHE B 12  ? 0.80270 0.48830 0.59840 -0.11630 -0.22890 0.10520  12  PHE B N     
3517 C  CA    . PHE B 12  ? 0.83210 0.49190 0.58930 -0.11980 -0.22040 0.11130  12  PHE B CA    
3518 C  C     . PHE B 12  ? 0.87490 0.51530 0.58070 -0.12840 -0.20770 0.11020  12  PHE B C     
3519 O  O     . PHE B 12  ? 0.87430 0.52370 0.57610 -0.13130 -0.20400 0.10370  12  PHE B O     
3520 C  CB    . PHE B 12  ? 0.75710 0.43450 0.53250 -0.11820 -0.19980 0.11130  12  PHE B CB    
3521 C  CG    . PHE B 12  ? 0.72430 0.42140 0.49190 -0.12380 -0.17240 0.10470  12  PHE B CG    
3522 C  CD1   . PHE B 12  ? 0.65050 0.37680 0.43880 -0.12290 -0.16750 0.09670  12  PHE B CD1   
3523 C  CD2   . PHE B 12  ? 0.79160 0.47830 0.53520 -0.12960 -0.15130 0.10650  12  PHE B CD2   
3524 C  CE1   . PHE B 12  ? 0.63900 0.38370 0.42230 -0.12690 -0.14360 0.09010  12  PHE B CE1   
3525 C  CE2   . PHE B 12  ? 0.76500 0.47150 0.50850 -0.13400 -0.12690 0.09950  12  PHE B CE2   
3526 C  CZ    . PHE B 12  ? 0.69430 0.43000 0.45710 -0.13220 -0.12380 0.09090  12  PHE B CZ    
3527 N  N     . CYS B 13  ? 0.85540 0.46790 0.52350 -0.13190 -0.19990 0.11690  13  CYS B N     
3528 C  CA    . CYS B 13  ? 0.92530 0.51680 0.54430 -0.13940 -0.18390 0.11690  13  CYS B CA    
3529 C  C     . CYS B 13  ? 0.84430 0.45750 0.46920 -0.14380 -0.15190 0.11270  13  CYS B C     
3530 O  O     . CYS B 13  ? 0.85910 0.46940 0.48740 -0.14480 -0.13970 0.11760  13  CYS B O     
3531 C  CB    . CYS B 13  ? 0.96680 0.51390 0.54150 -0.14070 -0.19160 0.12740  13  CYS B CB    
3532 S  SG    . CYS B 13  ? 1.22000 0.73630 0.78050 -0.13570 -0.23090 0.13120  13  CYS B SG    
3533 N  N     . SER B 14  ? 0.94660 0.58150 0.57670 -0.14610 -0.13910 0.10350  14  SER B N     
3534 C  CA    . SER B 14  ? 0.83470 0.49250 0.47430 -0.14950 -0.11030 0.09780  14  SER B CA    
3535 C  C     . SER B 14  ? 0.89260 0.52560 0.48910 -0.15600 -0.09220 0.09990  14  SER B C     
3536 O  O     . SER B 14  ? 0.90230 0.52110 0.47080 -0.15770 -0.09410 0.09710  14  SER B O     
3537 C  CB    . SER B 14  ? 0.77190 0.46320 0.43770 -0.14790 -0.10640 0.08710  14  SER B CB    
3538 O  OG    . SER B 14  ? 0.79260 0.50660 0.47030 -0.15000 -0.08070 0.08090  14  SER B OG    
3539 N  N     . PRO B 15  ? 0.89900 0.52470 0.49030 -0.15980 -0.07320 0.10510  15  PRO B N     
3540 C  CA    . PRO B 15  ? 0.97860 0.58050 0.53160 -0.16610 -0.05330 0.10830  15  PRO B CA    
3541 C  C     . PRO B 15  ? 0.89380 0.51110 0.44380 -0.16800 -0.03700 0.09810  15  PRO B C     
3542 O  O     . PRO B 15  ? 0.83570 0.48840 0.42250 -0.16680 -0.02620 0.08990  15  PRO B O     
3543 C  CB    . PRO B 15  ? 1.07370 0.68010 0.64420 -0.16980 -0.03290 0.11320  15  PRO B CB    
3544 C  CG    . PRO B 15  ? 0.99660 0.61130 0.59840 -0.16480 -0.04990 0.11640  15  PRO B CG    
3545 C  CD    . PRO B 15  ? 0.85100 0.48980 0.47530 -0.15840 -0.06880 0.10820  15  PRO B CD    
3546 N  N     . GLY B 16  ? 0.89340 0.48210 0.39920 -0.17020 -0.03660 0.09890  16  GLY B N     
3547 C  CA    . GLY B 16  ? 0.88280 0.48040 0.38220 -0.17150 -0.02130 0.08990  16  GLY B CA    
3548 C  C     . GLY B 16  ? 0.83450 0.44980 0.34960 -0.16720 -0.03680 0.08110  16  GLY B C     
3549 O  O     . GLY B 16  ? 0.79710 0.41590 0.30440 -0.16780 -0.02620 0.07410  16  GLY B O     
3550 N  N     . LYS B 17  ? 0.77890 0.40480 0.31830 -0.16300 -0.06080 0.08180  17  LYS B N     
3551 C  CA    . LYS B 17  ? 0.73700 0.38430 0.30150 -0.15940 -0.07380 0.07440  17  LYS B CA    
3552 C  C     . LYS B 17  ? 0.84190 0.46950 0.39840 -0.15670 -0.10430 0.07830  17  LYS B C     
3553 O  O     . LYS B 17  ? 0.86510 0.51000 0.44790 -0.15380 -0.11590 0.07390  17  LYS B O     
3554 C  CB    . LYS B 17  ? 0.70010 0.38960 0.31610 -0.15630 -0.07030 0.06960  17  LYS B CB    
3555 C  CG    . LYS B 17  ? 0.65090 0.36290 0.28280 -0.15780 -0.04320 0.06490  17  LYS B CG    
3556 C  CD    . LYS B 17  ? 0.65810 0.40920 0.33630 -0.15350 -0.04200 0.05920  17  LYS B CD    
3557 C  CE    . LYS B 17  ? 0.61880 0.38960 0.31520 -0.15430 -0.01800 0.05530  17  LYS B CE    
3558 N  NZ    . LYS B 17  ? 0.70290 0.45850 0.39310 -0.15790 -0.01000 0.06320  17  LYS B NZ    
3559 N  N     . GLY B 18  ? 0.90290 0.49350 0.42440 -0.15730 -0.11720 0.08690  18  GLY B N     
3560 C  CA    . GLY B 18  ? 0.87940 0.45040 0.39750 -0.15380 -0.14890 0.09120  18  GLY B CA    
3561 C  C     . GLY B 18  ? 0.85070 0.44540 0.41650 -0.14930 -0.16370 0.09330  18  GLY B C     
3562 O  O     . GLY B 18  ? 0.86940 0.47160 0.44640 -0.14920 -0.15580 0.09720  18  GLY B O     
3563 N  N     . ARG B 19  ? 0.77300 0.37840 0.36840 -0.14530 -0.18400 0.09110  19  ARG B N     
3564 C  CA    . ARG B 19  ? 0.75780 0.38650 0.40360 -0.14000 -0.19860 0.09250  19  ARG B CA    
3565 C  C     . ARG B 19  ? 0.65540 0.32660 0.34120 -0.13950 -0.18140 0.08550  19  ARG B C     
3566 O  O     . ARG B 19  ? 0.62470 0.30560 0.30630 -0.14190 -0.16840 0.07930  19  ARG B O     
3567 C  CB    . ARG B 19  ? 0.80730 0.42480 0.46870 -0.13530 -0.22830 0.09430  19  ARG B CB    
3568 C  CG    . ARG B 19  ? 0.89460 0.46800 0.51440 -0.13500 -0.24890 0.10060  19  ARG B CG    
3569 C  CD    . ARG B 19  ? 0.93830 0.49690 0.56340 -0.13130 -0.27520 0.10000  19  ARG B CD    
3570 N  NE    . ARG B 19  ? 0.96180 0.52330 0.57550 -0.13340 -0.26600 0.09410  19  ARG B NE    
3571 C  CZ    . ARG B 19  ? 1.05220 0.59770 0.66100 -0.13080 -0.28520 0.09310  19  ARG B CZ    
3572 N  NH1   . ARG B 19  ? 0.96880 0.49440 0.58480 -0.12620 -0.31610 0.09700  19  ARG B NH1   
3573 N  NH2   . ARG B 19  ? 1.04350 0.59350 0.64220 -0.13220 -0.27440 0.08790  19  ARG B NH2   
3574 N  N     . GLY B 20  ? 0.69240 0.38630 0.41400 -0.13570 -0.18140 0.08670  20  GLY B N     
3575 C  CA    . GLY B 20  ? 0.64870 0.38080 0.40590 -0.13390 -0.16730 0.08090  20  GLY B CA    
3576 C  C     . GLY B 20  ? 0.64460 0.39500 0.44710 -0.12650 -0.18020 0.08340  20  GLY B C     
3577 O  O     . GLY B 20  ? 0.64820 0.38280 0.45910 -0.12280 -0.20050 0.08900  20  GLY B O     
3578 N  N     . LEU B 21  ? 0.56410 0.34760 0.39590 -0.12300 -0.16790 0.07920  21  LEU B N     
3579 C  CA    . LEU B 21  ? 0.56580 0.37000 0.44170 -0.11350 -0.17450 0.08130  21  LEU B CA    
3580 C  C     . LEU B 21  ? 0.58550 0.40150 0.46530 -0.10940 -0.15510 0.08100  21  LEU B C     
3581 O  O     . LEU B 21  ? 0.56640 0.39440 0.43450 -0.11210 -0.13470 0.07580  21  LEU B O     
3582 C  CB    . LEU B 21  ? 0.60980 0.44170 0.51830 -0.10450 -0.16700 0.07830  21  LEU B CB    
3583 C  CG    . LEU B 21  ? 0.58150 0.43270 0.53930 -0.09220 -0.17210 0.08060  21  LEU B CG    
3584 C  CD1   . LEU B 21  ? 0.63020 0.46480 0.61040 -0.09060 -0.19560 0.08440  21  LEU B CD1   
3585 C  CD2   . LEU B 21  ? 0.60400 0.47750 0.58320 -0.08340 -0.16050 0.07970  21  LEU B CD2   
3586 N  N     . ARG B 22  ? 0.55240 0.36300 0.45320 -0.10310 -0.16110 0.08510  22  ARG B N     
3587 C  CA    . ARG B 22  ? 0.56650 0.37920 0.47410 -0.10080 -0.14440 0.08370  22  ARG B CA    
3588 C  C     . ARG B 22  ? 0.53850 0.36660 0.49120 -0.08980 -0.14430 0.08130  22  ARG B C     
3589 O  O     . ARG B 22  ? 0.50860 0.33580 0.48730 -0.08350 -0.16220 0.08480  22  ARG B O     
3590 C  CB    . ARG B 22  ? 0.63570 0.41880 0.52130 -0.10460 -0.15000 0.09010  22  ARG B CB    
3591 C  CG    . ARG B 22  ? 0.84840 0.62890 0.74350 -0.10350 -0.13560 0.08880  22  ARG B CG    
3592 C  CD    . ARG B 22  ? 0.82210 0.57360 0.68690 -0.11030 -0.13450 0.09540  22  ARG B CD    
3593 N  NE    . ARG B 22  ? 0.86590 0.59290 0.72300 -0.10770 -0.15720 0.10400  22  ARG B NE    
3594 C  CZ    . ARG B 22  ? 0.79290 0.48940 0.61890 -0.11250 -0.16020 0.11170  22  ARG B CZ    
3595 N  NH1   . ARG B 22  ? 0.75030 0.43780 0.55280 -0.12060 -0.14020 0.11240  22  ARG B NH1   
3596 N  NH2   . ARG B 22  ? 0.95540 0.63000 0.77600 -0.10880 -0.18280 0.11880  22  ARG B NH2   
3597 N  N     . ALA B 23  ? 0.52680 0.36760 0.49030 -0.08780 -0.12460 0.07400  23  ALA B N     
3598 C  CA    . ALA B 23  ? 0.48590 0.33610 0.48670 -0.07850 -0.12050 0.06890  23  ALA B CA    
3599 C  C     . ALA B 23  ? 0.52450 0.35520 0.53420 -0.07560 -0.12600 0.07120  23  ALA B C     
3600 O  O     . ALA B 23  ? 0.63890 0.45410 0.62570 -0.08210 -0.12220 0.07300  23  ALA B O     
3601 C  CB    . ALA B 23  ? 0.47800 0.34530 0.48130 -0.07880 -0.09940 0.05810  23  ALA B CB    
3602 N  N     . LEU B 24  ? 0.48150 0.31340 0.52780 -0.06530 -0.13400 0.07100  24  LEU B N     
3603 C  CA    . LEU B 24  ? 0.48430 0.29970 0.54590 -0.05980 -0.13770 0.07120  24  LEU B CA    
3604 C  C     . LEU B 24  ? 0.51940 0.34080 0.60460 -0.05310 -0.12190 0.05980  24  LEU B C     
3605 O  O     . LEU B 24  ? 0.64160 0.44830 0.73570 -0.04900 -0.12110 0.05730  24  LEU B O     
3606 C  CB    . LEU B 24  ? 0.50380 0.31460 0.59230 -0.05180 -0.15890 0.07790  24  LEU B CB    
3607 C  CG    . LEU B 24  ? 0.61760 0.41360 0.67890 -0.05860 -0.17890 0.08800  24  LEU B CG    
3608 C  CD1   . LEU B 24  ? 0.60000 0.39540 0.69520 -0.05080 -0.20150 0.09180  24  LEU B CD1   
3609 C  CD2   . LEU B 24  ? 0.61230 0.38190 0.63620 -0.06590 -0.17700 0.09270  24  LEU B CD2   
3610 N  N     . GLN B 25  ? 0.55910 0.39960 0.65220 -0.05190 -0.10960 0.05250  25  GLN B N     
3611 C  CA    . GLN B 25  ? 0.57940 0.42260 0.68690 -0.04660 -0.09420 0.04010  25  GLN B CA    
3612 C  C     . GLN B 25  ? 0.53510 0.39200 0.62060 -0.05440 -0.08140 0.03330  25  GLN B C     
3613 O  O     . GLN B 25  ? 0.56350 0.43150 0.63100 -0.06110 -0.08290 0.03830  25  GLN B O     
3614 C  CB    . GLN B 25  ? 0.52920 0.38130 0.68000 -0.03290 -0.09210 0.03770  25  GLN B CB    
3615 C  CG    . GLN B 25  ? 0.56110 0.43470 0.72510 -0.03270 -0.09130 0.04070  25  GLN B CG    
3616 C  CD    . GLN B 25  ? 0.68330 0.56760 0.89800 -0.01890 -0.08760 0.03950  25  GLN B CD    
3617 O  OE1   . GLN B 25  ? 0.85630 0.73510 1.09800 -0.01020 -0.09430 0.04070  25  GLN B OE1   
3618 N  NE2   . GLN B 25  ? 0.68510 0.58740 0.91410 -0.01670 -0.07480 0.03660  25  GLN B NE2   
3619 N  N     . PRO B 26  ? 0.56640 0.42170 0.65120 -0.05330 -0.06950 0.02080  26  PRO B N     
3620 C  CA    . PRO B 26  ? 0.62540 0.49460 0.69160 -0.05990 -0.06010 0.01360  26  PRO B CA    
3621 C  C     . PRO B 26  ? 0.55720 0.44740 0.63420 -0.05380 -0.05290 0.01310  26  PRO B C     
3622 O  O     . PRO B 26  ? 0.48210 0.37590 0.58470 -0.04170 -0.04880 0.01270  26  PRO B O     
3623 C  CB    . PRO B 26  ? 0.63290 0.49120 0.69490 -0.05750 -0.05330 -0.00110 26  PRO B CB    
3624 C  CG    . PRO B 26  ? 0.70670 0.55170 0.79230 -0.04370 -0.05240 -0.00360 26  PRO B CG    
3625 C  CD    . PRO B 26  ? 0.58920 0.42750 0.68870 -0.04470 -0.06570 0.01150  26  PRO B CD    
3626 N  N     . PHE B 27  ? 0.42410 0.32950 0.48270 -0.06120 -0.04950 0.01310  27  PHE B N     
3627 C  CA    . PHE B 27  ? 0.42200 0.34810 0.48430 -0.05520 -0.03940 0.01100  27  PHE B CA    
3628 C  C     . PHE B 27  ? 0.39470 0.32940 0.43380 -0.05680 -0.03010 0.00070  27  PHE B C     
3629 O  O     . PHE B 27  ? 0.41710 0.35080 0.43950 -0.06770 -0.03420 -0.00030 27  PHE B O     
3630 C  CB    . PHE B 27  ? 0.40110 0.33610 0.46510 -0.06160 -0.04740 0.02180  27  PHE B CB    
3631 C  CG    . PHE B 27  ? 0.37280 0.30140 0.46040 -0.05770 -0.05970 0.03120  27  PHE B CG    
3632 C  CD1   . PHE B 27  ? 0.39680 0.33460 0.52010 -0.04740 -0.05620 0.03190  27  PHE B CD1   
3633 C  CD2   . PHE B 27  ? 0.40250 0.31910 0.47560 -0.06120 -0.07270 0.03830  27  PHE B CD2   
3634 C  CE1   . PHE B 27  ? 0.41530 0.34790 0.56830 -0.04420 -0.07110 0.04020  27  PHE B CE1   
3635 C  CE2   . PHE B 27  ? 0.41530 0.32530 0.50880 -0.05680 -0.08810 0.04680  27  PHE B CE2   
3636 C  CZ    . PHE B 27  ? 0.49240 0.41160 0.62790 -0.04810 -0.08880 0.04740  27  PHE B CZ    
3637 N  N     . GLN B 28  ? 0.46220 0.40380 0.50120 -0.04550 -0.01740 -0.00660 28  GLN B N     
3638 C  CA    . GLN B 28  ? 0.40130 0.34890 0.41680 -0.04410 -0.01060 -0.01610 28  GLN B CA    
3639 C  C     . GLN B 28  ? 0.39100 0.35630 0.40270 -0.04620 -0.00710 -0.01080 28  GLN B C     
3640 O  O     . GLN B 28  ? 0.35880 0.33090 0.38760 -0.04570 -0.00640 -0.00200 28  GLN B O     
3641 C  CB    . GLN B 28  ? 0.50310 0.44290 0.51180 -0.02960 0.00190  -0.02610 28  GLN B CB    
3642 C  CG    . GLN B 28  ? 0.76890 0.69010 0.78740 -0.02280 0.00290  -0.03130 28  GLN B CG    
3643 C  CD    . GLN B 28  ? 0.90660 0.81280 0.90750 -0.02670 -0.00520 -0.04250 28  GLN B CD    
3644 O  OE1   . GLN B 28  ? 1.09280 0.98390 1.08080 -0.01720 0.00040  -0.05430 28  GLN B OE1   
3645 N  NE2   . GLN B 28  ? 0.92830 0.83700 0.92850 -0.04100 -0.01760 -0.03940 28  GLN B NE2   
3646 N  N     . VAL B 29  ? 0.33640 0.30820 0.32770 -0.04830 -0.00600 -0.01700 29  VAL B N     
3647 C  CA    . VAL B 29  ? 0.34410 0.33060 0.32950 -0.04890 -0.00200 -0.01350 29  VAL B CA    
3648 C  C     . VAL B 29  ? 0.38100 0.36970 0.37500 -0.03780 0.01060  -0.01010 29  VAL B C     
3649 O  O     . VAL B 29  ? 0.40050 0.38030 0.38860 -0.02700 0.02030  -0.01570 29  VAL B O     
3650 C  CB    . VAL B 29  ? 0.36510 0.35580 0.32950 -0.04850 -0.00290 -0.02260 29  VAL B CB    
3651 C  CG1   . VAL B 29  ? 0.39290 0.39510 0.35020 -0.04500 0.00320  -0.01960 29  VAL B CG1   
3652 C  CG2   . VAL B 29  ? 0.36130 0.35470 0.32650 -0.06160 -0.01280 -0.02470 29  VAL B CG2   
3653 N  N     . GLY B 30  ? 0.37360 0.37230 0.38200 -0.04110 0.01110  -0.00110 30  GLY B N     
3654 C  CA    . GLY B 30  ? 0.33870 0.34160 0.36270 -0.03300 0.02370  0.00330  30  GLY B CA    
3655 C  C     . GLY B 30  ? 0.28140 0.28290 0.34020 -0.03030 0.02400  0.00880  30  GLY B C     
3656 O  O     . GLY B 30  ? 0.31940 0.32750 0.40080 -0.02600 0.03340  0.01350  30  GLY B O     
3657 N  N     . ASP B 31  ? 0.35230 0.34490 0.41860 -0.03260 0.01350  0.00820  31  ASP B N     
3658 C  CA    . ASP B 31  ? 0.38110 0.37130 0.48340 -0.02940 0.00960  0.01330  31  ASP B CA    
3659 C  C     . ASP B 31  ? 0.40130 0.39950 0.52460 -0.03700 -0.00410 0.02310  31  ASP B C     
3660 O  O     . ASP B 31  ? 0.29430 0.29210 0.39810 -0.04750 -0.01650 0.02600  31  ASP B O     
3661 C  CB    . ASP B 31  ? 0.44740 0.42270 0.54860 -0.03070 -0.00110 0.01110  31  ASP B CB    
3662 C  CG    . ASP B 31  ? 0.56040 0.52410 0.65070 -0.02100 0.01120  0.00060  31  ASP B CG    
3663 O  OD1   . ASP B 31  ? 0.66310 0.62850 0.74180 -0.01260 0.02830  -0.00500 31  ASP B OD1   
3664 O  OD2   . ASP B 31  ? 0.61750 0.56720 0.70820 -0.02170 0.00330  -0.00220 31  ASP B OD2   
3665 N  N     . LEU B 32  ? 0.33500 0.33920 0.49910 -0.03130 -0.00180 0.02740  32  LEU B N     
3666 C  CA    . LEU B 32  ? 0.36800 0.37750 0.55890 -0.03700 -0.01910 0.03560  32  LEU B CA    
3667 C  C     . LEU B 32  ? 0.33000 0.32630 0.52740 -0.03920 -0.04070 0.03980  32  LEU B C     
3668 O  O     . LEU B 32  ? 0.37020 0.36180 0.59520 -0.03130 -0.03950 0.03910  32  LEU B O     
3669 C  CB    . LEU B 32  ? 0.34720 0.36920 0.58520 -0.02900 -0.00790 0.03750  32  LEU B CB    
3670 C  CG    . LEU B 32  ? 0.31720 0.34180 0.57290 -0.02820 -0.02510 0.04240  32  LEU B CG    
3671 C  CD1   . LEU B 32  ? 0.32320 0.34790 0.54120 -0.03480 -0.03180 0.04250  32  LEU B CD1   
3672 C  CD2   . LEU B 32  ? 0.36790 0.40050 0.66980 -0.01920 -0.01080 0.04260  32  LEU B CD2   
3673 N  N     . LEU B 33  ? 0.37090 0.35940 0.53340 -0.04580 -0.05720 0.04290  33  LEU B N     
3674 C  CA    . LEU B 33  ? 0.37790 0.35100 0.53800 -0.04710 -0.07810 0.04890  33  LEU B CA    
3675 C  C     . LEU B 33  ? 0.35500 0.33050 0.55400 -0.04150 -0.09360 0.05510  33  LEU B C     
3676 O  O     . LEU B 33  ? 0.37010 0.33930 0.60160 -0.03660 -0.10450 0.05830  33  LEU B O     
3677 C  CB    . LEU B 33  ? 0.36900 0.33120 0.47970 -0.05530 -0.08650 0.05130  33  LEU B CB    
3678 C  CG    . LEU B 33  ? 0.36800 0.32280 0.44610 -0.06050 -0.07740 0.04660  33  LEU B CG    
3679 C  CD1   . LEU B 33  ? 0.31270 0.28090 0.38280 -0.06080 -0.05820 0.03800  33  LEU B CD1   
3680 C  CD2   . LEU B 33  ? 0.40670 0.34930 0.44660 -0.06760 -0.08610 0.05130  33  LEU B CD2   
3681 N  N     . PHE B 34  ? 0.37970 0.36210 0.57590 -0.04200 -0.09520 0.05630  34  PHE B N     
3682 C  CA    . PHE B 34  ? 0.33440 0.31630 0.56620 -0.03710 -0.10890 0.06100  34  PHE B CA    
3683 C  C     . PHE B 34  ? 0.33860 0.32940 0.56640 -0.03820 -0.10220 0.05880  34  PHE B C     
3684 O  O     . PHE B 34  ? 0.33950 0.33480 0.53230 -0.04300 -0.09100 0.05490  34  PHE B O     
3685 C  CB    . PHE B 34  ? 0.33120 0.28920 0.55080 -0.03980 -0.13750 0.06940  34  PHE B CB    
3686 C  CG    . PHE B 34  ? 0.34280 0.28590 0.50630 -0.04880 -0.14540 0.07240  34  PHE B CG    
3687 C  CD1   . PHE B 34  ? 0.41350 0.35130 0.53320 -0.05530 -0.13910 0.07160  34  PHE B CD1   
3688 C  CD2   . PHE B 34  ? 0.44840 0.38020 0.60450 -0.05140 -0.15790 0.07520  34  PHE B CD2   
3689 C  CE1   . PHE B 34  ? 0.41630 0.33880 0.48760 -0.06350 -0.14310 0.07450  34  PHE B CE1   
3690 C  CE2   . PHE B 34  ? 0.43850 0.35320 0.54370 -0.05990 -0.16260 0.07740  34  PHE B CE2   
3691 C  CZ    . PHE B 34  ? 0.42310 0.33280 0.48670 -0.06590 -0.15420 0.07780  34  PHE B CZ    
3692 N  N     . SER B 35  ? 0.40310 0.39480 0.66950 -0.03380 -0.10920 0.06070  35  SER B N     
3693 C  CA    A SER B 35  ? 0.43380 0.43030 0.70180 -0.03520 -0.10820 0.05920  35  SER B CA    
3694 C  CA    B SER B 35  ? 0.43380 0.43030 0.70180 -0.03520 -0.10820 0.05920  35  SER B CA    
3695 C  C     . SER B 35  ? 0.54230 0.52010 0.80980 -0.03760 -0.13530 0.06420  35  SER B C     
3696 O  O     . SER B 35  ? 0.48930 0.45240 0.76970 -0.03650 -0.15220 0.06850  35  SER B O     
3697 C  CB    A SER B 35  ? 0.39490 0.40580 0.71130 -0.02880 -0.09090 0.05640  35  SER B CB    
3698 C  CB    B SER B 35  ? 0.39490 0.40580 0.71130 -0.02880 -0.09090 0.05640  35  SER B CB    
3699 O  OG    A SER B 35  ? 0.70050 0.72310 1.01570 -0.02610 -0.06520 0.05230  35  SER B OG    
3700 O  OG    B SER B 35  ? 0.70050 0.72310 1.01570 -0.02610 -0.06520 0.05230  35  SER B OG    
3701 N  N     . CYS B 36  ? 0.44290 0.41890 0.69490 -0.04150 -0.13970 0.06300  36  CYS B N     
3702 C  CA    . CYS B 36  ? 0.44870 0.40450 0.69470 -0.04470 -0.16520 0.06640  36  CYS B CA    
3703 C  C     . CYS B 36  ? 0.44140 0.40440 0.70510 -0.04500 -0.16530 0.06300  36  CYS B C     
3704 O  O     . CYS B 36  ? 0.47700 0.44620 0.71380 -0.04860 -0.15480 0.05950  36  CYS B O     
3705 C  CB    . CYS B 36  ? 0.44650 0.38150 0.63210 -0.05240 -0.17450 0.06910  36  CYS B CB    
3706 S  SG    . CYS B 36  ? 0.56260 0.46390 0.73090 -0.05730 -0.20660 0.07310  36  CYS B SG    
3714 N  N     . ALA B 38  ? 0.49630 0.44820 0.77360 -0.05210 -0.19530 0.05670  38  ALA B N     
3715 C  CA    . ALA B 38  ? 0.54230 0.47510 0.77890 -0.05810 -0.21130 0.05550  38  ALA B CA    
3716 C  C     . ALA B 38  ? 0.65060 0.56180 0.90390 -0.05780 -0.24260 0.05760  38  ALA B C     
3717 O  O     . ALA B 38  ? 0.60960 0.52820 0.91720 -0.05400 -0.24960 0.05680  38  ALA B O     
3718 C  CB    . ALA B 38  ? 0.51520 0.46010 0.75190 -0.06080 -0.19990 0.04980  38  ALA B CB    
3719 N  N     . TYR B 39  ? 0.57100 0.45340 0.77780 -0.06200 -0.26110 0.06000  39  TYR B N     
3720 C  CA    . TYR B 39  ? 0.61170 0.46630 0.81980 -0.06290 -0.29410 0.06100  39  TYR B CA    
3721 C  C     . TYR B 39  ? 0.68370 0.53730 0.89590 -0.06500 -0.30310 0.05570  39  TYR B C     
3722 O  O     . TYR B 39  ? 0.62460 0.47310 0.87660 -0.06280 -0.32440 0.05450  39  TYR B O     
3723 C  CB    . TYR B 39  ? 0.65520 0.47630 0.80290 -0.06780 -0.30750 0.06460  39  TYR B CB    
3724 C  CG    . TYR B 39  ? 0.76390 0.55190 0.90270 -0.06910 -0.34210 0.06490  39  TYR B CG    
3725 C  CD1   . TYR B 39  ? 0.75270 0.52720 0.91780 -0.06620 -0.36340 0.06820  39  TYR B CD1   
3726 C  CD2   . TYR B 39  ? 0.76410 0.53290 0.86810 -0.07290 -0.35460 0.06120  39  TYR B CD2   
3727 C  CE1   . TYR B 39  ? 0.73260 0.47510 0.88850 -0.06700 -0.39740 0.06790  39  TYR B CE1   
3728 C  CE2   . TYR B 39  ? 0.76560 0.50160 0.85830 -0.07360 -0.38810 0.06090  39  TYR B CE2   
3729 C  CZ    . TYR B 39  ? 0.79470 0.51710 0.91280 -0.07050 -0.41030 0.06440  39  TYR B CZ    
3730 O  OH    . TYR B 39  ? 0.88770 0.57600 0.99360 -0.07080 -0.44550 0.06360  39  TYR B OH    
3731 N  N     . ALA B 40  ? 0.67880 0.53590 0.85210 -0.06940 -0.28790 0.05200  40  ALA B N     
3732 C  CA    . ALA B 40  ? 0.63430 0.49310 0.80950 -0.07200 -0.29140 0.04590  40  ALA B CA    
3733 C  C     . ALA B 40  ? 0.58410 0.46190 0.73820 -0.07470 -0.26190 0.04210  40  ALA B C     
3734 O  O     . ALA B 40  ? 0.55610 0.43530 0.67630 -0.07580 -0.24530 0.04390  40  ALA B O     
3735 C  CB    . ALA B 40  ? 0.74900 0.57230 0.87980 -0.07610 -0.31750 0.04440  40  ALA B CB    
3736 N  N     . TYR B 41  ? 0.61190 0.50310 0.78830 -0.07590 -0.25610 0.03660  41  TYR B N     
3737 C  CA    . TYR B 41  ? 0.54790 0.45740 0.71260 -0.07830 -0.22880 0.03210  41  TYR B CA    
3738 C  C     . TYR B 41  ? 0.59150 0.50110 0.76810 -0.08190 -0.23360 0.02560  41  TYR B C     
3739 O  O     . TYR B 41  ? 0.64690 0.55060 0.85650 -0.08130 -0.25460 0.02500  41  TYR B O     
3740 C  CB    . TYR B 41  ? 0.50320 0.44050 0.70360 -0.07400 -0.20440 0.03420  41  TYR B CB    
3741 C  CG    . TYR B 41  ? 0.54220 0.49320 0.80740 -0.07020 -0.20700 0.03520  41  TYR B CG    
3742 C  CD1   . TYR B 41  ? 0.51280 0.46080 0.81190 -0.06540 -0.22100 0.03970  41  TYR B CD1   
3743 C  CD2   . TYR B 41  ? 0.59930 0.56450 0.89370 -0.07150 -0.19490 0.03150  41  TYR B CD2   
3744 C  CE1   . TYR B 41  ? 0.56410 0.52400 0.92720 -0.06160 -0.22190 0.04010  41  TYR B CE1   
3745 C  CE2   . TYR B 41  ? 0.57220 0.54870 0.92840 -0.06820 -0.19520 0.03270  41  TYR B CE2   
3746 C  CZ    . TYR B 41  ? 0.58850 0.56300 0.98050 -0.06300 -0.20810 0.03670  41  TYR B CZ    
3747 O  OH    . TYR B 41  ? 0.62810 0.61330 1.08510 -0.05950 -0.20660 0.03730  41  TYR B OH    
3748 N  N     . VAL B 42  ? 0.49440 0.40990 0.64680 -0.08550 -0.21500 0.02060  42  VAL B N     
3749 C  CA    . VAL B 42  ? 0.50700 0.42360 0.67050 -0.08940 -0.21540 0.01400  42  VAL B CA    
3750 C  C     . VAL B 42  ? 0.51480 0.44800 0.67290 -0.09090 -0.18610 0.01090  42  VAL B C     
3751 O  O     . VAL B 42  ? 0.41670 0.34950 0.53830 -0.09100 -0.17200 0.01060  42  VAL B O     
3752 C  CB    . VAL B 42  ? 0.58370 0.47190 0.70500 -0.09370 -0.23600 0.00900  42  VAL B CB    
3753 C  CG1   . VAL B 42  ? 0.57440 0.44990 0.63480 -0.09560 -0.22500 0.00780  42  VAL B CG1   
3754 C  CG2   . VAL B 42  ? 0.67690 0.56490 0.81450 -0.09790 -0.23930 0.00160  42  VAL B CG2   
3755 N  N     . LEU B 43  ? 0.46260 0.40860 0.65890 -0.09210 -0.17760 0.00890  43  LEU B N     
3756 C  CA    . LEU B 43  ? 0.45240 0.40940 0.64550 -0.09410 -0.15230 0.00620  43  LEU B CA    
3757 C  C     . LEU B 43  ? 0.45630 0.39730 0.61320 -0.09950 -0.15570 -0.00160 43  LEU B C     
3758 O  O     . LEU B 43  ? 0.49580 0.42310 0.65520 -0.10280 -0.17510 -0.00570 43  LEU B O     
3759 C  CB    . LEU B 43  ? 0.45190 0.42290 0.69760 -0.09370 -0.14310 0.00810  43  LEU B CB    
3760 C  CG    . LEU B 43  ? 0.40260 0.38190 0.64700 -0.09510 -0.11650 0.00760  43  LEU B CG    
3761 C  CD1   . LEU B 43  ? 0.39890 0.39020 0.63570 -0.08990 -0.09590 0.01250  43  LEU B CD1   
3762 C  CD2   . LEU B 43  ? 0.40760 0.39290 0.69900 -0.09640 -0.11170 0.00890  43  LEU B CD2   
3763 N  N     . THR B 44  ? 0.41690 0.35830 0.54160 -0.10000 -0.13750 -0.00420 44  THR B N     
3764 C  CA    . THR B 44  ? 0.44870 0.37440 0.53910 -0.10410 -0.13800 -0.01220 44  THR B CA    
3765 C  C     . THR B 44  ? 0.50110 0.42610 0.61620 -0.10850 -0.13580 -0.01660 44  THR B C     
3766 O  O     . THR B 44  ? 0.45840 0.39770 0.60920 -0.10810 -0.12300 -0.01250 44  THR B O     
3767 C  CB    . THR B 44  ? 0.44700 0.37430 0.50480 -0.10230 -0.11890 -0.01350 44  THR B CB    
3768 O  OG1   . THR B 44  ? 0.49520 0.40350 0.51630 -0.10500 -0.12270 -0.02110 44  THR B OG1   
3769 C  CG2   . THR B 44  ? 0.46600 0.40860 0.54460 -0.10130 -0.09580 -0.01220 44  THR B CG2   
3770 N  N     . VAL B 45  ? 0.51960 0.42540 0.61420 -0.11270 -0.14850 -0.02460 45  VAL B N     
3771 C  CA    . VAL B 45  ? 0.51860 0.41940 0.63620 -0.11780 -0.15150 -0.02950 45  VAL B CA    
3772 C  C     . VAL B 45  ? 0.52790 0.43770 0.65950 -0.11880 -0.12620 -0.02850 45  VAL B C     
3773 O  O     . VAL B 45  ? 0.52090 0.43650 0.68990 -0.12100 -0.12260 -0.02590 45  VAL B O     
3774 C  CB    . VAL B 45  ? 0.61020 0.48520 0.69330 -0.12160 -0.16770 -0.03980 45  VAL B CB    
3775 C  CG1   . VAL B 45  ? 0.69470 0.56270 0.79520 -0.12710 -0.16560 -0.04640 45  VAL B CG1   
3776 C  CG2   . VAL B 45  ? 0.60500 0.46730 0.68410 -0.12130 -0.19680 -0.03940 45  VAL B CG2   
3777 N  N     . ASN B 46  ? 0.57610 0.48590 0.67860 -0.11670 -0.10930 -0.02980 46  ASN B N     
3778 C  CA    . ASN B 46  ? 0.53970 0.45280 0.64800 -0.11690 -0.08670 -0.02830 46  ASN B CA    
3779 C  C     . ASN B 46  ? 0.50570 0.43670 0.64410 -0.11390 -0.07140 -0.01740 46  ASN B C     
3780 O  O     . ASN B 46  ? 0.49150 0.42170 0.63670 -0.11410 -0.05550 -0.01380 46  ASN B O     
3781 C  CB    . ASN B 46  ? 0.56020 0.46820 0.63300 -0.11380 -0.07540 -0.03250 46  ASN B CB    
3782 C  CG    . ASN B 46  ? 0.71360 0.60040 0.75760 -0.11590 -0.08360 -0.04370 46  ASN B CG    
3783 O  OD1   . ASN B 46  ? 0.86730 0.74170 0.91880 -0.12090 -0.09230 -0.04910 46  ASN B OD1   
3784 N  ND2   . ASN B 46  ? 0.80160 0.68280 0.81110 -0.11180 -0.08080 -0.04680 46  ASN B ND2   
3785 N  N     . GLU B 47  ? 0.48660 0.43110 0.64050 -0.11020 -0.07660 -0.01170 47  GLU B N     
3786 C  CA    . GLU B 47  ? 0.47670 0.43720 0.65880 -0.10590 -0.06260 -0.00210 47  GLU B CA    
3787 C  C     . GLU B 47  ? 0.53190 0.49920 0.76250 -0.10610 -0.06940 0.00180  47  GLU B C     
3788 O  O     . GLU B 47  ? 0.58870 0.56880 0.84660 -0.10130 -0.05780 0.00910  47  GLU B O     
3789 C  CB    . GLU B 47  ? 0.45430 0.42540 0.62440 -0.10030 -0.05990 0.00140  47  GLU B CB    
3790 C  CG    . GLU B 47  ? 0.57000 0.53860 0.70260 -0.09860 -0.04830 -0.00100 47  GLU B CG    
3791 C  CD    . GLU B 47  ? 0.77870 0.74790 0.90830 -0.09710 -0.02770 0.00320  47  GLU B CD    
3792 O  OE1   . GLU B 47  ? 0.60720 0.58160 0.76220 -0.09520 -0.01940 0.01020  47  GLU B OE1   
3793 O  OE2   . GLU B 47  ? 0.58690 0.55070 0.69030 -0.09640 -0.02010 0.00010  47  GLU B OE2   
3794 N  N     . ARG B 48  ? 0.43860 0.39650 0.68100 -0.11110 -0.08790 -0.00380 48  ARG B N     
3795 C  CA    . ARG B 48  ? 0.52930 0.49220 0.82360 -0.11220 -0.09620 -0.00170 48  ARG B CA    
3796 C  C     . ARG B 48  ? 0.57210 0.53800 0.89090 -0.11270 -0.07490 0.00310  48  ARG B C     
3797 O  O     . ARG B 48  ? 0.61510 0.56950 0.90880 -0.11590 -0.06600 0.00060  48  ARG B O     
3798 C  CB    . ARG B 48  ? 0.62650 0.57490 0.92150 -0.11800 -0.12190 -0.00990 48  ARG B CB    
3799 C  CG    . ARG B 48  ? 0.63840 0.58070 0.91360 -0.11640 -0.14580 -0.01280 48  ARG B CG    
3800 C  CD    . ARG B 48  ? 0.68150 0.60360 0.94300 -0.12170 -0.17050 -0.02190 48  ARG B CD    
3801 N  NE    . ARG B 48  ? 0.65750 0.57220 0.91500 -0.11940 -0.19750 -0.02210 48  ARG B NE    
3802 C  CZ    . ARG B 48  ? 0.74070 0.63500 0.98290 -0.12250 -0.22380 -0.02910 48  ARG B CZ    
3803 N  NH1   . ARG B 48  ? 0.76090 0.64100 0.99070 -0.12830 -0.22600 -0.03770 48  ARG B NH1   
3804 N  NH2   . ARG B 48  ? 0.70850 0.59410 0.94680 -0.11940 -0.24830 -0.02740 48  ARG B NH2   
3805 N  N     . GLY B 49  ? 0.62800 0.60690 0.99420 -0.10910 -0.06660 0.00970  49  GLY B N     
3806 C  CA    . GLY B 49  ? 0.62290 0.60380 1.01340 -0.10820 -0.04430 0.01550  49  GLY B CA    
3807 C  C     . GLY B 49  ? 0.61610 0.60380 0.99200 -0.10080 -0.01910 0.02320  49  GLY B C     
3808 O  O     . GLY B 49  ? 0.57320 0.56430 0.97520 -0.09750 0.00050  0.02970  49  GLY B O     
3809 N  N     . ASN B 50  ? 0.50720 0.49510 0.84060 -0.09810 -0.01960 0.02230  50  ASN B N     
3810 C  CA    . ASN B 50  ? 0.54870 0.54210 0.86420 -0.09060 0.00010  0.02840  50  ASN B CA    
3811 C  C     . ASN B 50  ? 0.58890 0.59480 0.91820 -0.08490 -0.00140 0.03060  50  ASN B C     
3812 O  O     . ASN B 50  ? 0.60190 0.61300 0.93470 -0.07790 0.01680  0.03620  50  ASN B O     
3813 C  CB    . ASN B 50  ? 0.54690 0.53220 0.80960 -0.09110 0.00110  0.02580  50  ASN B CB    
3814 C  CG    . ASN B 50  ? 0.58790 0.55830 0.83570 -0.09570 0.00320  0.02360  50  ASN B CG    
3815 O  OD1   . ASN B 50  ? 0.69970 0.66610 0.96940 -0.09590 0.01350  0.02750  50  ASN B OD1   
3816 N  ND2   . ASN B 50  ? 0.51140 0.47210 0.72260 -0.09930 -0.00530 0.01720  50  ASN B ND2   
3817 N  N     . HIS B 51  ? 0.48790 0.49590 0.82270 -0.08730 -0.02340 0.02620  51  HIS B N     
3818 C  CA    . HIS B 51  ? 0.38600 0.40310 0.73360 -0.08220 -0.02900 0.02790  51  HIS B CA    
3819 C  C     . HIS B 51  ? 0.39160 0.41190 0.78610 -0.08310 -0.04740 0.02690  51  HIS B C     
3820 O  O     . HIS B 51  ? 0.49670 0.50990 0.89780 -0.08900 -0.06470 0.02240  51  HIS B O     
3821 C  CB    . HIS B 51  ? 0.41580 0.42960 0.71860 -0.08290 -0.04020 0.02440  51  HIS B CB    
3822 C  CG    . HIS B 51  ? 0.38660 0.39900 0.64850 -0.08090 -0.02390 0.02520  51  HIS B CG    
3823 N  ND1   . HIS B 51  ? 0.41150 0.43050 0.66300 -0.07500 -0.01440 0.02830  51  HIS B ND1   
3824 C  CD2   . HIS B 51  ? 0.39590 0.40000 0.62670 -0.08390 -0.01670 0.02320  51  HIS B CD2   
3825 C  CE1   . HIS B 51  ? 0.45720 0.47250 0.67290 -0.07430 -0.00310 0.02810  51  HIS B CE1   
3826 N  NE2   . HIS B 51  ? 0.35740 0.36390 0.56110 -0.07940 -0.00410 0.02540  51  HIS B NE2   
3827 N  N     . CYS B 52  ? 0.39440 0.42360 0.82180 -0.07690 -0.04430 0.03080  52  CYS B N     
3828 C  CA    . CYS B 52  ? 0.44140 0.47340 0.91620 -0.07610 -0.06320 0.03040  52  CYS B CA    
3829 C  C     . CYS B 52  ? 0.38810 0.41280 0.83580 -0.07770 -0.09100 0.02690  52  CYS B C     
3830 O  O     . CYS B 52  ? 0.35680 0.38050 0.76690 -0.07560 -0.08970 0.02760  52  CYS B O     
3831 C  CB    . CYS B 52  ? 0.48200 0.52330 0.99760 -0.06820 -0.04870 0.03540  52  CYS B CB    
3832 S  SG    . CYS B 52  ? 0.47430 0.51820 1.04890 -0.06550 -0.07180 0.03530  52  CYS B SG    
3833 N  N     . GLU B 53  ? 0.43240 0.45010 0.89880 -0.08150 -0.11640 0.02340  53  GLU B N     
3834 C  CA    . GLU B 53  ? 0.50590 0.51120 0.94410 -0.08290 -0.14470 0.02040  53  GLU B CA    
3835 C  C     . GLU B 53  ? 0.51710 0.52440 0.96360 -0.07650 -0.15220 0.02460  53  GLU B C     
3836 O  O     . GLU B 53  ? 0.56300 0.56080 0.96740 -0.07640 -0.16340 0.02450  53  GLU B O     
3837 C  CB    . GLU B 53  ? 0.62830 0.62340 1.09040 -0.08710 -0.17190 0.01590  53  GLU B CB    
3838 C  CG    . GLU B 53  ? 0.71040 0.69930 1.16070 -0.09440 -0.16930 0.01050  53  GLU B CG    
3839 C  CD    . GLU B 53  ? 0.74490 0.71630 1.13200 -0.09930 -0.18060 0.00450  53  GLU B CD    
3840 O  OE1   . GLU B 53  ? 0.73980 0.70010 1.09670 -0.09770 -0.19860 0.00420  53  GLU B OE1   
3841 O  OE2   . GLU B 53  ? 0.87700 0.84370 1.24520 -0.10450 -0.17080 0.00030  53  GLU B OE2   
3842 N  N     . TYR B 54  ? 0.42200 0.44000 0.92400 -0.07110 -0.14490 0.02840  54  TYR B N     
3843 C  CA    . TYR B 54  ? 0.47610 0.49460 0.99820 -0.06470 -0.15360 0.03210  54  TYR B CA    
3844 C  C     . TYR B 54  ? 0.41550 0.43940 0.90550 -0.06090 -0.13300 0.03520  54  TYR B C     
3845 O  O     . TYR B 54  ? 0.43190 0.44790 0.89240 -0.05970 -0.14600 0.03630  54  TYR B O     
3846 C  CB    . TYR B 54  ? 0.52030 0.54710 1.11720 -0.06040 -0.15080 0.03400  54  TYR B CB    
3847 C  CG    . TYR B 54  ? 0.51010 0.53480 1.13030 -0.05430 -0.16140 0.03690  54  TYR B CG    
3848 C  CD1   . TYR B 54  ? 0.51610 0.52570 1.12560 -0.05470 -0.19490 0.03640  54  TYR B CD1   
3849 C  CD2   . TYR B 54  ? 0.55180 0.58630 1.20020 -0.04820 -0.13800 0.04020  54  TYR B CD2   
3850 C  CE1   . TYR B 54  ? 0.56680 0.57180 1.19640 -0.04950 -0.20580 0.03930  54  TYR B CE1   
3851 C  CE2   . TYR B 54  ? 0.50270 0.53390 1.17290 -0.04300 -0.14750 0.04240  54  TYR B CE2   
3852 C  CZ    . TYR B 54  ? 0.56950 0.58630 1.23140 -0.04380 -0.18200 0.04210  54  TYR B CZ    
3853 O  OH    . TYR B 54  ? 0.66910 0.68040 1.35280 -0.03920 -0.19270 0.04430  54  TYR B OH    
3854 N  N     . CYS B 55  ? 0.45710 0.49180 0.95230 -0.05890 -0.10270 0.03670  55  CYS B N     
3855 C  CA    . CYS B 55  ? 0.45110 0.49090 0.92620 -0.05400 -0.08290 0.03940  55  CYS B CA    
3856 C  C     . CYS B 55  ? 0.45030 0.49000 0.86980 -0.05670 -0.06630 0.03810  55  CYS B C     
3857 O  O     . CYS B 55  ? 0.47080 0.51350 0.86990 -0.05300 -0.05160 0.03970  55  CYS B O     
3858 C  CB    . CYS B 55  ? 0.60010 0.64810 1.12470 -0.04790 -0.06050 0.04250  55  CYS B CB    
3859 S  SG    . CYS B 55  ? 0.48880 0.54060 1.02000 -0.04910 -0.03170 0.04310  55  CYS B SG    
3860 N  N     . PHE B 56  ? 0.46250 0.49760 0.86000 -0.06290 -0.06930 0.03490  56  PHE B N     
3861 C  CA    . PHE B 56  ? 0.41900 0.45120 0.76510 -0.06620 -0.05760 0.03270  56  PHE B CA    
3862 C  C     . PHE B 56  ? 0.40640 0.44340 0.75070 -0.06310 -0.02900 0.03530  56  PHE B C     
3863 O  O     . PHE B 56  ? 0.45030 0.48400 0.75450 -0.06480 -0.01950 0.03400  56  PHE B O     
3864 C  CB    . PHE B 56  ? 0.39480 0.42270 0.69640 -0.06630 -0.06500 0.03150  56  PHE B CB    
3865 C  CG    . PHE B 56  ? 0.43130 0.44710 0.70720 -0.07150 -0.08850 0.02780  56  PHE B CG    
3866 C  CD1   . PHE B 56  ? 0.41070 0.42010 0.71170 -0.07350 -0.11010 0.02700  56  PHE B CD1   
3867 C  CD2   . PHE B 56  ? 0.45050 0.45930 0.67690 -0.07390 -0.08910 0.02510  56  PHE B CD2   
3868 C  CE1   . PHE B 56  ? 0.40400 0.39790 0.67560 -0.07760 -0.13190 0.02370  56  PHE B CE1   
3869 C  CE2   . PHE B 56  ? 0.42330 0.41750 0.62290 -0.07790 -0.10840 0.02210  56  PHE B CE2   
3870 C  CZ    . PHE B 56  ? 0.42670 0.41230 0.64600 -0.07970 -0.13010 0.02160  56  PHE B CZ    
3871 N  N     . THR B 57  ? 0.48990 0.53230 0.87790 -0.05830 -0.01550 0.03890  57  THR B N     
3872 C  CA    . THR B 57  ? 0.46950 0.51220 0.85680 -0.05420 0.01230  0.04230  57  THR B CA    
3873 C  C     . THR B 57  ? 0.41780 0.45490 0.79170 -0.05900 0.01820  0.04170  57  THR B C     
3874 O  O     . THR B 57  ? 0.46400 0.50020 0.86380 -0.06360 0.00870  0.04020  57  THR B O     
3875 C  CB    . THR B 57  ? 0.52300 0.56930 0.96440 -0.04870 0.02630  0.04590  57  THR B CB    
3876 O  OG1   . THR B 57  ? 0.59170 0.64160 1.04930 -0.04420 0.02060  0.04630  57  THR B OG1   
3877 C  CG2   . THR B 57  ? 0.65270 0.69460 1.08710 -0.04390 0.05680  0.04970  57  THR B CG2   
3878 N  N     . ARG B 58  ? 0.43430 0.46660 0.76910 -0.05740 0.03290  0.04270  58  ARG B N     
3879 C  CA    . ARG B 58  ? 0.49180 0.51640 0.81080 -0.06040 0.04140  0.04340  58  ARG B CA    
3880 C  C     . ARG B 58  ? 0.48770 0.50950 0.83370 -0.05550 0.06490  0.04890  58  ARG B C     
3881 O  O     . ARG B 58  ? 0.50500 0.52550 0.84480 -0.04820 0.08180  0.05220  58  ARG B O     
3882 C  CB    . ARG B 58  ? 0.57760 0.59680 0.84400 -0.05970 0.04470  0.04240  58  ARG B CB    
3883 C  CG    . ARG B 58  ? 0.66230 0.67170 0.91090 -0.06250 0.05010  0.04290  58  ARG B CG    
3884 C  CD    . ARG B 58  ? 0.72620 0.73040 0.92880 -0.06020 0.05360  0.04250  58  ARG B CD    
3885 N  NE    . ARG B 58  ? 0.94490 0.95120 1.13450 -0.05190 0.06540  0.04540  58  ARG B NE    
3886 C  CZ    . ARG B 58  ? 1.10620 1.11670 1.27180 -0.05050 0.05960  0.04280  58  ARG B CZ    
3887 N  NH1   . ARG B 58  ? 0.93320 0.94600 1.08350 -0.05670 0.04380  0.03770  58  ARG B NH1   
3888 N  NH2   . ARG B 58  ? 1.03170 1.04200 1.18740 -0.04290 0.07080  0.04510  58  ARG B NH2   
3889 N  N     . LYS B 59  ? 0.46020 0.47910 0.83390 -0.05960 0.06660  0.04970  59  LYS B N     
3890 C  CA    . LYS B 59  ? 0.70470 0.71810 1.10210 -0.05600 0.09070  0.05530  59  LYS B CA    
3891 C  C     . LYS B 59  ? 0.63470 0.64320 1.05090 -0.06280 0.08850  0.05520  59  LYS B C     
3892 O  O     . LYS B 59  ? 0.63650 0.64680 1.05630 -0.07010 0.06670  0.05000  59  LYS B O     
3893 C  CB    . LYS B 59  ? 0.74630 0.76570 1.19160 -0.05140 0.10040  0.05760  59  LYS B CB    
3894 C  CG    . LYS B 59  ? 0.81310 0.84200 1.30900 -0.05610 0.08090  0.05420  59  LYS B CG    
3895 C  CD    . LYS B 59  ? 1.05600 1.08860 1.60740 -0.05140 0.09480  0.05710  59  LYS B CD    
3896 C  CE    . LYS B 59  ? 1.15640 1.19250 1.70390 -0.04480 0.09640  0.05710  59  LYS B CE    
3897 N  NZ    . LYS B 59  ? 1.45950 1.48680 1.96870 -0.03800 0.12090  0.06060  59  LYS B NZ    
3898 N  N     . GLU B 60  ? 0.96750 0.96730 1.39380 -0.06020 0.11180  0.06090  60  GLU B N     
3899 C  CA    . GLU B 60  ? 1.01990 1.01370 1.46870 -0.06630 0.11390  0.06190  60  GLU B CA    
3900 C  C     . GLU B 60  ? 0.93600 0.93740 1.45040 -0.06870 0.11460  0.06190  60  GLU B C     
3901 O  O     . GLU B 60  ? 0.79980 0.80680 1.34130 -0.06310 0.12520  0.06400  60  GLU B O     
3902 C  CB    . GLU B 60  ? 1.16660 1.14490 1.59340 -0.06220 0.13960  0.06890  60  GLU B CB    
3903 C  CG    . GLU B 60  ? 1.08830 1.05720 1.45490 -0.05950 0.13790  0.06920  60  GLU B CG    
3904 C  CD    . GLU B 60  ? 1.29420 1.26060 1.64490 -0.06750 0.11710  0.06390  60  GLU B CD    
3905 O  OE1   . GLU B 60  ? 1.57090 1.53800 1.95340 -0.07540 0.10750  0.06110  60  GLU B OE1   
3906 O  OE2   . GLU B 60  ? 1.36270 1.32490 1.66980 -0.06590 0.11050  0.06210  60  GLU B OE2   
3907 N  N     . GLY B 61  ? 0.76130 0.76180 1.30220 -0.07700 0.10260  0.05910  61  GLY B N     
3908 C  CA    . GLY B 61  ? 0.73490 0.74160 1.34230 -0.08010 0.10180  0.05880  61  GLY B CA    
3909 C  C     . GLY B 61  ? 0.69570 0.71580 1.33730 -0.08000 0.07960  0.05390  61  GLY B C     
3910 O  O     . GLY B 61  ? 0.70420 0.73080 1.39680 -0.07650 0.08870  0.05590  61  GLY B O     
3911 N  N     . LEU B 62  ? 0.76630 0.78810 1.37930 -0.08360 0.05110  0.04750  62  LEU B N     
3912 C  CA    . LEU B 62  ? 0.67180 0.70260 1.30980 -0.08360 0.02550  0.04290  62  LEU B CA    
3913 C  C     . LEU B 62  ? 0.69300 0.72500 1.38470 -0.09010 0.00730  0.03890  62  LEU B C     
3914 O  O     . LEU B 62  ? 0.59880 0.62300 1.28620 -0.09720 0.00350  0.03650  62  LEU B O     
3915 C  CB    . LEU B 62  ? 0.56330 0.59140 1.14640 -0.08530 0.00290  0.03790  62  LEU B CB    
3916 C  CG    . LEU B 62  ? 0.61250 0.64090 1.14620 -0.07920 0.01480  0.04060  62  LEU B CG    
3917 C  CD1   . LEU B 62  ? 0.51340 0.53630 0.99190 -0.08290 -0.00410 0.03540  62  LEU B CD1   
3918 C  CD2   . LEU B 62  ? 0.61150 0.64880 1.16980 -0.07190 0.01760  0.04280  62  LEU B CD2   
3919 N  N     . SER B 63  ? 0.79990 0.84040 1.54300 -0.08750 -0.00460 0.03780  63  SER B N     
3920 C  CA    . SER B 63  ? 0.78110 0.82320 1.58090 -0.09270 -0.02580 0.03350  63  SER B CA    
3921 C  C     . SER B 63  ? 0.67380 0.70830 1.44180 -0.09880 -0.06210 0.02570  63  SER B C     
3922 O  O     . SER B 63  ? 0.98910 1.02240 1.72270 -0.09610 -0.07910 0.02380  63  SER B O     
3923 C  CB    . SER B 63  ? 0.76110 0.81280 1.62370 -0.08700 -0.03010 0.03450  63  SER B CB    
3924 O  OG    . SER B 63  ? 0.81660 0.87250 1.70560 -0.08090 0.00520  0.04100  63  SER B OG    
3925 N  N     . LYS B 64  ? 0.69000 0.71730 1.46940 -0.10690 -0.07290 0.02120  64  LYS B N     
3926 C  CA    . LYS B 64  ? 0.71070 0.72590 1.45750 -0.11350 -0.10510 0.01290  64  LYS B CA    
3927 C  C     . LYS B 64  ? 0.62720 0.64260 1.42400 -0.11470 -0.13800 0.00770  64  LYS B C     
3928 O  O     . LYS B 64  ? 0.69060 0.71280 1.55570 -0.11530 -0.13540 0.00860  64  LYS B O     
3929 C  CB    . LYS B 64  ? 0.76240 0.76630 1.49190 -0.12170 -0.09810 0.01020  64  LYS B CB    
3930 C  CG    . LYS B 64  ? 0.87310 0.86060 1.56790 -0.12910 -0.12820 0.00030  64  LYS B CG    
3931 C  CD    . LYS B 64  ? 0.86590 0.83970 1.53070 -0.13610 -0.11600 -0.00190 64  LYS B CD    
3932 C  CE    . LYS B 64  ? 0.80540 0.78060 1.52730 -0.14070 -0.10370 0.00020  64  LYS B CE    
3933 N  NZ    . LYS B 64  ? 0.82280 0.78180 1.51340 -0.14710 -0.09170 -0.00130 64  LYS B NZ    
3934 N  N     . CYS B 65  ? 0.62150 0.62770 1.38370 -0.11460 -0.16900 0.00250  65  CYS B N     
3935 C  CA    . CYS B 65  ? 0.66300 0.66390 1.46090 -0.11520 -0.20580 -0.00280 65  CYS B CA    
3936 C  C     . CYS B 65  ? 0.70450 0.69710 1.52930 -0.12390 -0.21910 -0.00950 65  CYS B C     
3937 O  O     . CYS B 65  ? 0.66570 0.64410 1.44270 -0.13030 -0.22370 -0.01500 65  CYS B O     
3938 C  CB    . CYS B 65  ? 0.67140 0.65800 1.41060 -0.11370 -0.23410 -0.00650 65  CYS B CB    
3939 S  SG    . CYS B 65  ? 0.67430 0.64780 1.44490 -0.11370 -0.28240 -0.01260 65  CYS B SG    
3940 N  N     . GLY B 66  ? 0.69510 0.69580 1.59900 -0.12400 -0.22470 -0.00960 66  GLY B N     
3941 C  CA    . GLY B 66  ? 0.73800 0.73340 1.68100 -0.13220 -0.23400 -0.01530 66  GLY B CA    
3942 C  C     . GLY B 66  ? 0.83520 0.81000 1.75020 -0.13810 -0.27440 -0.02600 66  GLY B C     
3943 O  O     . GLY B 66  ? 1.05290 1.01850 1.97550 -0.14640 -0.27930 -0.03190 66  GLY B O     
3944 N  N     . ARG B 67  ? 0.73070 0.69540 1.61130 -0.13370 -0.30280 -0.02830 67  ARG B N     
3945 C  CA    . ARG B 67  ? 0.70210 0.64260 1.55090 -0.13740 -0.34460 -0.03840 67  ARG B CA    
3946 C  C     . ARG B 67  ? 0.67070 0.59360 1.43110 -0.14200 -0.33940 -0.04300 67  ARG B C     
3947 O  O     . ARG B 67  ? 0.74820 0.65520 1.49620 -0.14980 -0.35060 -0.05160 67  ARG B O     
3948 C  CB    . ARG B 67  ? 0.71200 0.64600 1.56030 -0.12990 -0.37550 -0.03760 67  ARG B CB    
3949 C  CG    . ARG B 67  ? 0.74860 0.69800 1.68700 -0.12470 -0.38170 -0.03390 67  ARG B CG    
3950 C  CD    . ARG B 67  ? 0.88910 0.83060 1.82500 -0.11670 -0.40950 -0.03190 67  ARG B CD    
3951 N  NE    . ARG B 67  ? 1.03090 0.94630 1.95300 -0.11820 -0.45720 -0.04010 67  ARG B NE    
3952 C  CZ    . ARG B 67  ? 1.16100 1.05030 2.00100 -0.11920 -0.47790 -0.04410 67  ARG B CZ    
3953 N  NH1   . ARG B 67  ? 1.36060 1.24820 2.12690 -0.11920 -0.45490 -0.04100 67  ARG B NH1   
3954 N  NH2   . ARG B 67  ? 1.44610 1.30940 2.27790 -0.12010 -0.52160 -0.05160 67  ARG B NH2   
3955 N  N     . CYS B 68  ? 0.79390 0.71860 1.49740 -0.13740 -0.32270 -0.03790 68  CYS B N     
3956 C  CA    . CYS B 68  ? 0.76670 0.67410 1.38720 -0.14070 -0.31810 -0.04250 68  CYS B CA    
3957 C  C     . CYS B 68  ? 0.78020 0.69570 1.38120 -0.14360 -0.27900 -0.03940 68  CYS B C     
3958 O  O     . CYS B 68  ? 0.72160 0.62130 1.26600 -0.14790 -0.27450 -0.04500 68  CYS B O     
3959 C  CB    . CYS B 68  ? 0.82600 0.72600 1.39220 -0.13440 -0.32770 -0.04000 68  CYS B CB    
3960 S  SG    . CYS B 68  ? 0.76140 0.68650 1.33440 -0.12640 -0.29520 -0.02780 68  CYS B SG    
3961 N  N     . LYS B 69  ? 0.78200 0.71970 1.42920 -0.14070 -0.25100 -0.03040 69  LYS B N     
3962 C  CA    . LYS B 69  ? 0.73330 0.67770 1.36620 -0.14190 -0.21360 -0.02530 69  LYS B CA    
3963 C  C     . LYS B 69  ? 0.77290 0.71090 1.33070 -0.13990 -0.20070 -0.02480 69  LYS B C     
3964 O  O     . LYS B 69  ? 0.82800 0.76110 1.35770 -0.14270 -0.17890 -0.02440 69  LYS B O     
3965 C  CB    . LYS B 69  ? 0.77060 0.70480 1.41740 -0.15070 -0.20920 -0.03030 69  LYS B CB    
3966 C  CG    . LYS B 69  ? 0.87810 0.82360 1.60690 -0.15280 -0.20670 -0.02780 69  LYS B CG    
3967 C  CD    . LYS B 69  ? 0.99640 0.93190 1.75780 -0.15730 -0.24440 -0.03710 69  LYS B CD    
3968 C  CE    . LYS B 69  ? 0.96230 0.87450 1.69190 -0.16660 -0.25570 -0.04750 69  LYS B CE    
3969 N  NZ    . LYS B 69  ? 0.95080 0.85440 1.72630 -0.17200 -0.28780 -0.05610 69  LYS B NZ    
3970 N  N     . GLN B 70  ? 0.74270 0.67990 1.27070 -0.13470 -0.21420 -0.02430 70  GLN B N     
3971 C  CA    . GLN B 70  ? 0.71910 0.65010 1.17900 -0.13270 -0.20470 -0.02450 70  GLN B CA    
3972 C  C     . GLN B 70  ? 0.65240 0.59640 1.10590 -0.12460 -0.19910 -0.01700 70  GLN B C     
3973 O  O     . GLN B 70  ? 0.82230 0.76020 1.22240 -0.12280 -0.19750 -0.01760 70  GLN B O     
3974 C  CB    . GLN B 70  ? 0.71200 0.61820 1.12080 -0.13670 -0.22930 -0.03480 70  GLN B CB    
3975 C  CG    . GLN B 70  ? 0.77490 0.66520 1.16810 -0.14440 -0.22550 -0.04310 70  GLN B CG    
3976 C  CD    . GLN B 70  ? 0.91250 0.77590 1.25190 -0.14740 -0.24790 -0.05420 70  GLN B CD    
3977 O  OE1   . GLN B 70  ? 0.84810 0.70100 1.13190 -0.14710 -0.23730 -0.05770 70  GLN B OE1   
3978 N  NE2   . GLN B 70  ? 0.96810 0.81900 1.32390 -0.14960 -0.27910 -0.06020 70  GLN B NE2   
3979 N  N     . ALA B 71  ? 0.66640 0.62740 1.17630 -0.11980 -0.19470 -0.01030 71  ALA B N     
3980 C  CA    . ALA B 71  ? 0.67940 0.65310 1.19160 -0.11180 -0.18630 -0.00310 71  ALA B CA    
3981 C  C     . ALA B 71  ? 0.65530 0.64750 1.21900 -0.10810 -0.15900 0.00420  71  ALA B C     
3982 O  O     . ALA B 71  ? 0.65350 0.65090 1.27590 -0.10920 -0.16150 0.00440  71  ALA B O     
3983 C  CB    . ALA B 71  ? 0.64420 0.61300 1.17180 -0.10820 -0.21700 -0.00350 71  ALA B CB    
3984 N  N     . PHE B 72  ? 0.59130 0.59180 1.13180 -0.10370 -0.13270 0.00980  72  PHE B N     
3985 C  CA    . PHE B 72  ? 0.58610 0.59970 1.16190 -0.09950 -0.10280 0.01680  72  PHE B CA    
3986 C  C     . PHE B 72  ? 0.56850 0.59250 1.15640 -0.09090 -0.09620 0.02200  72  PHE B C     
3987 O  O     . PHE B 72  ? 0.52960 0.55080 1.08060 -0.08860 -0.10690 0.02140  72  PHE B O     
3988 C  CB    . PHE B 72  ? 0.66130 0.67150 1.19810 -0.10110 -0.07680 0.01880  72  PHE B CB    
3989 C  CG    . PHE B 72  ? 0.68640 0.68460 1.21580 -0.10920 -0.08030 0.01410  72  PHE B CG    
3990 C  CD1   . PHE B 72  ? 0.69580 0.67970 1.18200 -0.11480 -0.10020 0.00620  72  PHE B CD1   
3991 C  CD2   . PHE B 72  ? 0.77690 0.77610 1.34140 -0.11130 -0.06220 0.01730  72  PHE B CD2   
3992 C  CE1   . PHE B 72  ? 0.74930 0.71980 1.22800 -0.12220 -0.10290 0.00100  72  PHE B CE1   
3993 C  CE2   . PHE B 72  ? 0.76720 0.75370 1.32520 -0.11900 -0.06550 0.01300  72  PHE B CE2   
3994 C  CZ    . PHE B 72  ? 0.61390 0.58580 1.12920 -0.12450 -0.08630 0.00450  72  PHE B CZ    
3995 N  N     . TYR B 73  ? 0.58390 0.61810 1.22460 -0.08640 -0.07760 0.02690  73  TYR B N     
3996 C  CA    . TYR B 73  ? 0.56890 0.61160 1.23670 -0.07820 -0.07170 0.03100  73  TYR B CA    
3997 C  C     . TYR B 73  ? 0.49910 0.54810 1.18680 -0.07310 -0.03470 0.03700  73  TYR B C     
3998 O  O     . TYR B 73  ? 0.51460 0.56220 1.21800 -0.07600 -0.01770 0.03840  73  TYR B O     
3999 C  CB    . TYR B 73  ? 0.51360 0.55790 1.24160 -0.07740 -0.09580 0.02910  73  TYR B CB    
4000 C  CG    . TYR B 73  ? 0.50410 0.53800 1.20900 -0.08080 -0.13380 0.02380  73  TYR B CG    
4001 C  CD1   . TYR B 73  ? 0.48570 0.51460 1.15190 -0.07750 -0.14740 0.02430  73  TYR B CD1   
4002 C  CD2   . TYR B 73  ? 0.54910 0.57530 1.26810 -0.08740 -0.15600 0.01830  73  TYR B CD2   
4003 C  CE1   . TYR B 73  ? 0.51810 0.53310 1.15800 -0.08020 -0.18110 0.02020  73  TYR B CE1   
4004 C  CE2   . TYR B 73  ? 0.52060 0.53280 1.21290 -0.09000 -0.19100 0.01330  73  TYR B CE2   
4005 C  CZ    . TYR B 73  ? 0.53980 0.54550 1.19080 -0.08620 -0.20300 0.01460  73  TYR B CZ    
4006 O  OH    . TYR B 73  ? 0.58700 0.57480 1.20690 -0.08840 -0.23620 0.01040  73  TYR B OH    
4007 N  N     . CYS B 74  ? 0.69300 0.74590 1.37760 -0.06580 -0.02260 0.04030  74  CYS B N     
4008 C  CA    . CYS B 74  ? 0.64610 0.70150 1.35020 -0.05980 0.01170  0.04560  74  CYS B CA    
4009 C  C     . CYS B 74  ? 0.56700 0.62590 1.34650 -0.05970 0.01930  0.04660  74  CYS B C     
4010 O  O     . CYS B 74  ? 0.53890 0.59570 1.33440 -0.05920 0.04720  0.05020  74  CYS B O     
4011 C  CB    . CYS B 74  ? 0.65900 0.71640 1.35430 -0.05230 0.01780  0.04740  74  CYS B CB    
4012 S  SG    . CYS B 74  ? 0.46440 0.51890 1.08080 -0.05190 0.01020  0.04630  74  CYS B SG    
4013 N  N     . ASN B 75  ? 0.47030 0.53290 1.29590 -0.06020 -0.00640 0.04360  75  ASN B N     
4014 C  CA    . ASN B 75  ? 0.55080 0.61770 1.45660 -0.05950 -0.00310 0.04380  75  ASN B CA    
4015 C  C     . ASN B 75  ? 0.56020 0.62780 1.50080 -0.06130 -0.04280 0.03900  75  ASN B C     
4016 O  O     . ASN B 75  ? 0.64630 0.70910 1.54340 -0.06350 -0.07090 0.03600  75  ASN B O     
4017 C  CB    . ASN B 75  ? 0.62060 0.68910 1.55430 -0.05170 0.02550  0.04800  75  ASN B CB    
4018 C  CG    . ASN B 75  ? 0.54800 0.61610 1.45290 -0.04640 0.01630  0.04790  75  ASN B CG    
4019 O  OD1   . ASN B 75  ? 0.60870 0.67740 1.52500 -0.04640 -0.01490 0.04490  75  ASN B OD1   
4020 N  ND2   . ASN B 75  ? 0.47930 0.54420 1.34500 -0.04170 0.04280  0.05110  75  ASN B ND2   
4021 N  N     . VAL B 76  ? 0.46210 0.53380 1.48100 -0.06030 -0.04470 0.03840  76  VAL B N     
4022 C  CA    . VAL B 76  ? 0.50450 0.57520 1.56580 -0.06150 -0.08330 0.03380  76  VAL B CA    
4023 C  C     . VAL B 76  ? 0.45300 0.52020 1.49980 -0.05600 -0.10370 0.03380  76  VAL B C     
4024 O  O     . VAL B 76  ? 0.41640 0.47680 1.46280 -0.05740 -0.14170 0.03020  76  VAL B O     
4025 C  CB    . VAL B 76  ? 0.61460 0.69100 1.77080 -0.06150 -0.07840 0.03310  76  VAL B CB    
4026 C  CG1   . VAL B 76  ? 0.64700 0.72040 1.84790 -0.06210 -0.12160 0.02800  76  VAL B CG1   
4027 C  CG2   . VAL B 76  ? 0.68720 0.76540 1.86020 -0.06780 -0.06110 0.03320  76  VAL B CG2   
4028 N  N     . GLU B 77  ? 0.63360 0.70290 1.66700 -0.05000 -0.07890 0.03770  77  GLU B N     
4029 C  CA    . GLU B 77  ? 0.71740 0.78270 1.73410 -0.04520 -0.09490 0.03810  77  GLU B CA    
4030 C  C     . GLU B 77  ? 0.57980 0.63760 1.51640 -0.04770 -0.11660 0.03710  77  GLU B C     
4031 O  O     . GLU B 77  ? 0.55260 0.60200 1.48120 -0.04790 -0.15070 0.03520  77  GLU B O     
4032 C  CB    . GLU B 77  ? 0.83670 0.90480 1.85310 -0.03890 -0.06120 0.04200  77  GLU B CB    
4033 C  CG    . GLU B 77  ? 0.89590 0.96030 1.92090 -0.03410 -0.07720 0.04210  77  GLU B CG    
4034 C  CD    . GLU B 77  ? 0.88710 0.95240 1.89800 -0.02880 -0.04530 0.04510  77  GLU B CD    
4035 O  OE1   . GLU B 77  ? 0.80810 0.87380 1.76790 -0.02860 -0.02000 0.04720  77  GLU B OE1   
4036 O  OE2   . GLU B 77  ? 1.05840 1.12260 2.10900 -0.02490 -0.04670 0.04510  77  GLU B OE2   
4037 N  N     . CYS B 78  ? 0.66960 0.72860 1.54710 -0.04980 -0.09620 0.03840  78  CYS B N     
4038 C  CA    . CYS B 78  ? 0.69280 0.74480 1.49500 -0.05320 -0.11210 0.03700  78  CYS B CA    
4039 C  C     . CYS B 78  ? 0.63760 0.68100 1.43770 -0.05920 -0.14710 0.03240  78  CYS B C     
4040 O  O     . CYS B 78  ? 0.70510 0.73750 1.46700 -0.06020 -0.17410 0.03090  78  CYS B O     
4041 C  CB    . CYS B 78  ? 0.67080 0.72530 1.42060 -0.05510 -0.08400 0.03840  78  CYS B CB    
4042 S  SG    . CYS B 78  ? 0.71310 0.77020 1.42750 -0.04850 -0.05760 0.04230  78  CYS B SG    
4043 N  N     . GLN B 79  ? 0.51560 0.56190 1.35780 -0.06320 -0.14640 0.03020  79  GLN B N     
4044 C  CA    . GLN B 79  ? 0.52290 0.56000 1.36980 -0.06920 -0.17900 0.02490  79  GLN B CA    
4045 C  C     . GLN B 79  ? 0.61220 0.64010 1.48860 -0.06660 -0.21620 0.02300  79  GLN B C     
4046 O  O     . GLN B 79  ? 0.61910 0.63180 1.45870 -0.06960 -0.24760 0.01960  79  GLN B O     
4047 C  CB    . GLN B 79  ? 0.58500 0.62810 1.48260 -0.07360 -0.16850 0.02310  79  GLN B CB    
4048 C  CG    . GLN B 79  ? 0.63290 0.66580 1.53650 -0.08040 -0.20180 0.01670  79  GLN B CG    
4049 C  CD    . GLN B 79  ? 0.59700 0.63520 1.54320 -0.08600 -0.18920 0.01490  79  GLN B CD    
4050 O  OE1   . GLN B 79  ? 0.60130 0.65050 1.58220 -0.08430 -0.15590 0.01910  79  GLN B OE1   
4051 N  NE2   . GLN B 79  ? 0.56940 0.59750 1.51190 -0.09290 -0.21540 0.00850  79  GLN B NE2   
4052 N  N     . LYS B 80  ? 0.74630 0.78090 1.68820 -0.06100 -0.21220 0.02510  80  LYS B N     
4053 C  CA    . LYS B 80  ? 0.80990 0.83500 1.78840 -0.05800 -0.24700 0.02350  80  LYS B CA    
4054 C  C     . LYS B 80  ? 0.68040 0.69300 1.60390 -0.05480 -0.26350 0.02570  80  LYS B C     
4055 O  O     . LYS B 80  ? 0.64260 0.63810 1.55500 -0.05520 -0.30070 0.02360  80  LYS B O     
4056 C  CB    . LYS B 80  ? 0.97840 1.01390 2.04700 -0.05340 -0.23570 0.02460  80  LYS B CB    
4057 C  CG    . LYS B 80  ? 1.28720 1.32860 2.36500 -0.04660 -0.21160 0.02910  80  LYS B CG    
4058 C  CD    . LYS B 80  ? 1.23870 1.27870 2.39280 -0.04230 -0.22720 0.02820  80  LYS B CD    
4059 C  CE    . LYS B 80  ? 1.05780 1.10600 2.23870 -0.03660 -0.19430 0.03170  80  LYS B CE    
4060 N  NZ    . LYS B 80  ? 0.94810 1.00890 2.19350 -0.03650 -0.15970 0.03210  80  LYS B NZ    
4061 N  N     . GLU B 81  ? 0.65620 0.67540 1.54370 -0.05180 -0.23580 0.02990  81  GLU B N     
4062 C  CA    . GLU B 81  ? 0.65000 0.65840 1.48570 -0.04910 -0.24680 0.03240  81  GLU B CA    
4063 C  C     . GLU B 81  ? 0.62450 0.61740 1.38330 -0.05420 -0.26650 0.03060  81  GLU B C     
4064 O  O     . GLU B 81  ? 0.72650 0.70240 1.45020 -0.05330 -0.29000 0.03170  81  GLU B O     
4065 C  CB    . GLU B 81  ? 0.59570 0.61550 1.41290 -0.04520 -0.21110 0.03650  81  GLU B CB    
4066 C  CG    . GLU B 81  ? 0.65100 0.68110 1.53630 -0.03960 -0.19130 0.03820  81  GLU B CG    
4067 C  CD    . GLU B 81  ? 0.65870 0.67950 1.58270 -0.03600 -0.21770 0.03830  81  GLU B CD    
4068 O  OE1   . GLU B 81  ? 0.82250 0.83060 1.70310 -0.03520 -0.23680 0.03980  81  GLU B OE1   
4069 O  OE2   . GLU B 81  ? 0.77270 0.79780 1.77180 -0.03410 -0.21900 0.03690  81  GLU B OE2   
4070 N  N     . ASP B 82  ? 0.58480 0.58150 1.31810 -0.05980 -0.25570 0.02780  82  ASP B N     
4071 C  CA    . ASP B 82  ? 0.59740 0.57910 1.26010 -0.06550 -0.27010 0.02490  82  ASP B CA    
4072 C  C     . ASP B 82  ? 0.71860 0.68160 1.38630 -0.06910 -0.30800 0.01990  82  ASP B C     
4073 O  O     . ASP B 82  ? 0.63670 0.58090 1.24410 -0.07280 -0.32490 0.01740  82  ASP B O     
4074 C  CB    . ASP B 82  ? 0.65120 0.64300 1.28520 -0.07030 -0.24200 0.02320  82  ASP B CB    
4075 C  CG    . ASP B 82  ? 0.63880 0.61660 1.19390 -0.07520 -0.24780 0.02060  82  ASP B CG    
4076 O  OD1   . ASP B 82  ? 0.53300 0.50210 1.04490 -0.07320 -0.25250 0.02310  82  ASP B OD1   
4077 O  OD2   . ASP B 82  ? 0.77580 0.75030 1.31370 -0.08130 -0.24660 0.01580  82  ASP B OD2   
4078 N  N     . TRP B 83  ? 0.70620 0.67300 1.44620 -0.06780 -0.32080 0.01820  83  TRP B N     
4079 C  CA    . TRP B 83  ? 0.76370 0.71430 1.51970 -0.07120 -0.35690 0.01250  83  TRP B CA    
4080 C  C     . TRP B 83  ? 0.78380 0.70490 1.48770 -0.07090 -0.39330 0.01170  83  TRP B C     
4081 O  O     . TRP B 83  ? 0.81420 0.71670 1.47720 -0.07580 -0.41310 0.00670  83  TRP B O     
4082 C  CB    . TRP B 83  ? 1.08240 1.04260 1.93310 -0.06830 -0.36490 0.01160  83  TRP B CB    
4083 C  CG    . TRP B 83  ? 1.17250 1.12240 2.05970 -0.07210 -0.39650 0.00500  83  TRP B CG    
4084 C  CD1   . TRP B 83  ? 1.07130 0.99560 1.94590 -0.07230 -0.44070 0.00120  83  TRP B CD1   
4085 C  CD2   . TRP B 83  ? 1.44610 1.41020 2.39480 -0.07580 -0.38720 0.00140  83  TRP B CD2   
4086 N  NE1   . TRP B 83  ? 1.05620 0.97820 1.97810 -0.07590 -0.46050 -0.00520 83  TRP B NE1   
4087 C  CE2   . TRP B 83  ? 1.39780 1.34480 2.36790 -0.07840 -0.42800 -0.00520 83  TRP B CE2   
4088 C  CE3   . TRP B 83  ? 1.46350 1.45050 2.44860 -0.07740 -0.34820 0.00320  83  TRP B CE3   
4089 C  CZ2   . TRP B 83  ? 1.43870 1.39320 2.46910 -0.08300 -0.43120 -0.01030 83  TRP B CZ2   
4090 C  CZ3   . TRP B 83  ? 1.32880 1.32210 2.37230 -0.08200 -0.34990 -0.00110 83  TRP B CZ3   
4091 C  CH2   . TRP B 83  ? 1.26810 1.24630 2.33560 -0.08500 -0.39120 -0.00800 83  TRP B CH2   
4092 N  N     . PRO B 84  ? 0.78480 0.69780 1.48540 -0.06540 -0.40280 0.01650  84  PRO B N     
4093 C  CA    . PRO B 84  ? 0.82760 0.70850 1.47660 -0.06510 -0.43720 0.01660  84  PRO B CA    
4094 C  C     . PRO B 84  ? 0.79180 0.65670 1.34850 -0.07000 -0.43320 0.01560  84  PRO B C     
4095 O  O     . PRO B 84  ? 0.93020 0.76510 1.44410 -0.07190 -0.46300 0.01300  84  PRO B O     
4096 C  CB    . PRO B 84  ? 0.83600 0.71680 1.49590 -0.05910 -0.43520 0.02290  84  PRO B CB    
4097 C  CG    . PRO B 84  ? 0.74640 0.65630 1.48950 -0.05530 -0.41210 0.02400  84  PRO B CG    
4098 C  CD    . PRO B 84  ? 0.79980 0.73100 1.54400 -0.05940 -0.38100 0.02180  84  PRO B CD    
4099 N  N     . MET B 85  ? 0.72440 0.60780 1.25300 -0.07180 -0.39680 0.01720  85  MET B N     
4100 C  CA    . MET B 85  ? 0.77970 0.65110 1.22820 -0.07660 -0.38840 0.01540  85  MET B CA    
4101 C  C     . MET B 85  ? 0.73380 0.60750 1.17630 -0.08290 -0.38410 0.00810  85  MET B C     
4102 O  O     . MET B 85  ? 0.77840 0.62930 1.16570 -0.08720 -0.39740 0.00340  85  MET B O     
4103 C  CB    . MET B 85  ? 0.72020 0.60850 1.14160 -0.07520 -0.35350 0.02030  85  MET B CB    
4104 C  CG    . MET B 85  ? 0.66500 0.54780 1.08240 -0.07000 -0.35720 0.02700  85  MET B CG    
4105 S  SD    . MET B 85  ? 0.83040 0.67070 1.18110 -0.07130 -0.39120 0.02830  85  MET B SD    
4106 C  CE    . MET B 85  ? 0.94410 0.78420 1.30050 -0.06580 -0.38770 0.03650  85  MET B CE    
4107 N  N     . HIS B 86  ? 0.59540 0.49470 1.09470 -0.08350 -0.36490 0.00700  86  HIS B N     
4108 C  CA    . HIS B 86  ? 0.69640 0.59940 1.19730 -0.09000 -0.35800 0.00050  86  HIS B CA    
4109 C  C     . HIS B 86  ? 0.75670 0.63730 1.26230 -0.09350 -0.39420 -0.00670 86  HIS B C     
4110 O  O     . HIS B 86  ? 0.74330 0.61390 1.21680 -0.09960 -0.39540 -0.01340 86  HIS B O     
4111 C  CB    . HIS B 86  ? 0.65760 0.58940 1.22300 -0.08960 -0.33040 0.00210  86  HIS B CB    
4112 C  CG    . HIS B 86  ? 0.71490 0.64980 1.28380 -0.09670 -0.32100 -0.00380 86  HIS B CG    
4113 N  ND1   . HIS B 86  ? 0.80070 0.72760 1.30790 -0.10200 -0.30980 -0.00770 86  HIS B ND1   
4114 C  CD2   . HIS B 86  ? 0.72300 0.66700 1.35150 -0.09950 -0.32060 -0.00650 86  HIS B CD2   
4115 C  CE1   . HIS B 86  ? 0.67320 0.60290 1.20000 -0.10780 -0.30370 -0.01260 86  HIS B CE1   
4116 N  NE2   . HIS B 86  ? 0.81790 0.75810 1.41770 -0.10670 -0.30990 -0.01170 86  HIS B NE2   
4117 N  N     . LYS B 87  ? 0.83270 0.70370 1.37800 -0.08950 -0.42460 -0.00580 87  LYS B N     
4118 C  CA    . LYS B 87  ? 0.89660 0.74390 1.44970 -0.09190 -0.46380 -0.01280 87  LYS B CA    
4119 C  C     . LYS B 87  ? 0.94260 0.75450 1.41000 -0.09490 -0.48460 -0.01710 87  LYS B C     
4120 O  O     . LYS B 87  ? 0.93830 0.72860 1.39820 -0.09820 -0.51260 -0.02470 87  LYS B O     
4121 C  CB    . LYS B 87  ? 1.00390 0.84560 1.61470 -0.08610 -0.49350 -0.01060 87  LYS B CB    
4122 C  CG    . LYS B 87  ? 1.12350 0.99420 1.83140 -0.08350 -0.48130 -0.00900 87  LYS B CG    
4123 C  CD    . LYS B 87  ? 1.10980 0.99680 1.85730 -0.08940 -0.46760 -0.01430 87  LYS B CD    
4124 C  CE    . LYS B 87  ? 1.07850 0.99260 1.82370 -0.09080 -0.41940 -0.01020 87  LYS B CE    
4125 N  NZ    . LYS B 87  ? 1.23160 1.16350 2.03480 -0.09530 -0.40340 -0.01320 87  LYS B NZ    
4126 N  N     . LEU B 88  ? 0.95460 0.75880 1.35820 -0.09360 -0.47070 -0.01250 88  LEU B N     
4127 C  CA    . LEU B 88  ? 0.99470 0.76610 1.31290 -0.09650 -0.48160 -0.01600 88  LEU B CA    
4128 C  C     . LEU B 88  ? 0.95690 0.72900 1.24500 -0.10340 -0.46570 -0.02420 88  LEU B C     
4129 O  O     . LEU B 88  ? 1.12340 0.86540 1.35150 -0.10640 -0.47970 -0.03030 88  LEU B O     
4130 C  CB    . LEU B 88  ? 1.01930 0.78650 1.28490 -0.09390 -0.46500 -0.00870 88  LEU B CB    
4131 C  CG    . LEU B 88  ? 0.95150 0.71550 1.23670 -0.08760 -0.47680 -0.00030 88  LEU B CG    
4132 C  CD1   . LEU B 88  ? 0.98900 0.75100 1.22030 -0.08670 -0.45490 0.00600  88  LEU B CD1   
4133 C  CD2   . LEU B 88  ? 1.02630 0.75380 1.30310 -0.08580 -0.52170 -0.00190 88  LEU B CD2   
4134 N  N     . GLU B 89  ? 0.92690 0.73110 1.25500 -0.10560 -0.43560 -0.02440 89  GLU B N     
4135 C  CA    . GLU B 89  ? 0.86770 0.67460 1.17110 -0.11210 -0.41590 -0.03140 89  GLU B CA    
4136 C  C     . GLU B 89  ? 0.85370 0.67530 1.21790 -0.11650 -0.41460 -0.03660 89  GLU B C     
4137 O  O     . GLU B 89  ? 0.85370 0.66520 1.19630 -0.12260 -0.41330 -0.04500 89  GLU B O     
4138 C  CB    . GLU B 89  ? 0.77080 0.59760 1.05010 -0.11170 -0.37640 -0.02690 89  GLU B CB    
4139 C  CG    . GLU B 89  ? 0.82030 0.63170 1.03660 -0.10860 -0.37490 -0.02260 89  GLU B CG    
4140 C  CD    . GLU B 89  ? 0.73130 0.56170 0.92590 -0.10810 -0.33810 -0.01890 89  GLU B CD    
4141 O  OE1   . GLU B 89  ? 0.68950 0.54840 0.92700 -0.10750 -0.31450 -0.01600 89  GLU B OE1   
4142 O  OE2   . GLU B 89  ? 0.77760 0.59250 0.91130 -0.10820 -0.33270 -0.01880 89  GLU B OE2   
4143 N  N     . CYS B 90  ? 0.82830 0.67190 1.26860 -0.11340 -0.41420 -0.03190 90  CYS B N     
4144 C  CA    . CYS B 90  ? 0.90460 0.76630 1.41000 -0.11740 -0.40550 -0.03470 90  CYS B CA    
4145 C  C     . CYS B 90  ? 0.97230 0.81280 1.47430 -0.12390 -0.43130 -0.04560 90  CYS B C     
4146 O  O     . CYS B 90  ? 0.92890 0.77010 1.42010 -0.13040 -0.41580 -0.05110 90  CYS B O     
4147 C  CB    . CYS B 90  ? 1.00670 0.88850 1.59570 -0.11220 -0.40820 -0.02880 90  CYS B CB    
4148 S  SG    . CYS B 90  ? 1.03330 0.93910 1.69890 -0.11700 -0.38690 -0.03010 90  CYS B SG    
4149 N  N     . SER B 91  ? 1.08240 0.90170 1.59240 -0.12200 -0.47150 -0.04890 91  SER B N     
4150 C  CA    . SER B 91  ? 1.19060 0.98640 1.69680 -0.12750 -0.50120 -0.05990 91  SER B CA    
4151 C  C     . SER B 91  ? 1.27840 1.04510 1.69470 -0.13150 -0.50300 -0.06750 91  SER B C     
4152 O  O     . SER B 91  ? 1.38990 1.14930 1.79800 -0.13840 -0.50050 -0.07650 91  SER B O     
4153 C  CB    . SER B 91  ? 1.18850 0.96750 1.72780 -0.12360 -0.54570 -0.06140 91  SER B CB    
4154 O  OG    . SER B 91  ? 1.39380 1.14980 1.93170 -0.12890 -0.57540 -0.07270 91  SER B OG    
4155 N  N     . PRO B 92  ? 1.07140 0.81890 1.41810 -0.12760 -0.50640 -0.06460 92  PRO B N     
4156 C  CA    . PRO B 92  ? 1.05590 0.77630 1.31750 -0.13080 -0.50270 -0.07160 92  PRO B CA    
4157 C  C     . PRO B 92  ? 1.06560 0.80080 1.31600 -0.13650 -0.46580 -0.07560 92  PRO B C     
4158 O  O     . PRO B 92  ? 1.10580 0.81910 1.31400 -0.14120 -0.46870 -0.08580 92  PRO B O     
4159 C  CB    . PRO B 92  ? 1.01970 0.73050 1.22730 -0.12500 -0.49810 -0.06350 92  PRO B CB    
4160 C  CG    . PRO B 92  ? 0.99540 0.70910 1.24950 -0.11890 -0.52250 -0.05600 92  PRO B CG    
4161 C  CD    . PRO B 92  ? 0.97960 0.72740 1.32610 -0.11990 -0.51440 -0.05470 92  PRO B CD    
4162 N  N     . MET B 93  ? 1.05880 0.82820 1.34610 -0.13550 -0.43260 -0.06770 93  MET B N     
4163 C  CA    . MET B 93  ? 0.97420 0.75690 1.25370 -0.14020 -0.39760 -0.07000 93  MET B CA    
4164 C  C     . MET B 93  ? 1.03290 0.81200 1.34420 -0.14760 -0.40210 -0.07910 93  MET B C     
4165 O  O     . MET B 93  ? 1.15210 0.92010 1.42870 -0.15250 -0.38860 -0.08670 93  MET B O     
4166 C  CB    . MET B 93  ? 0.92950 0.74690 1.24530 -0.13700 -0.36460 -0.05910 93  MET B CB    
4167 C  CG    . MET B 93  ? 0.99120 0.81390 1.26040 -0.13720 -0.33070 -0.05800 93  MET B CG    
4168 S  SD    . MET B 93  ? 0.82960 0.67980 1.10610 -0.13010 -0.30390 -0.04480 93  MET B SD    
4169 C  CE    . MET B 93  ? 0.75740 0.63550 1.12520 -0.12800 -0.30060 -0.03730 93  MET B CE    
4170 N  N     . VAL B 94  ? 0.84750 0.63460 1.22660 -0.14840 -0.42110 -0.07870 94  VAL B N     
4171 C  CA    . VAL B 94  ? 0.94590 0.72920 1.36210 -0.15590 -0.42770 -0.08700 94  VAL B CA    
4172 C  C     . VAL B 94  ? 1.08910 0.83510 1.46160 -0.15940 -0.46110 -0.10020 94  VAL B C     
4173 O  O     . VAL B 94  ? 1.09610 0.82910 1.45640 -0.16630 -0.45770 -0.11010 94  VAL B O     
4174 C  CB    . VAL B 94  ? 0.90380 0.70890 1.41400 -0.15580 -0.43560 -0.08260 94  VAL B CB    
4175 C  CG1   . VAL B 94  ? 0.86030 0.69790 1.40930 -0.14990 -0.40740 -0.06930 94  VAL B CG1   
4176 C  CG2   . VAL B 94  ? 1.02140 0.81080 1.55420 -0.15320 -0.48070 -0.08630 94  VAL B CG2   
4177 N  N     . VAL B 95  ? 1.04370 0.76980 1.38990 -0.15430 -0.49300 -0.10030 95  VAL B N     
4178 C  CA    . VAL B 95  ? 1.11350 0.80030 1.41570 -0.15610 -0.52890 -0.11200 95  VAL B CA    
4179 C  C     . VAL B 95  ? 1.09090 0.75200 1.30410 -0.15790 -0.51560 -0.11960 95  VAL B C     
4180 O  O     . VAL B 95  ? 1.16310 0.79930 1.35020 -0.16310 -0.52620 -0.13240 95  VAL B O     
4181 C  CB    . VAL B 95  ? 1.19190 0.86150 1.48900 -0.14920 -0.56660 -0.10830 95  VAL B CB    
4182 C  CG1   . VAL B 95  ? 1.26970 0.89260 1.50550 -0.15030 -0.60250 -0.11990 95  VAL B CG1   
4183 C  CG2   . VAL B 95  ? 1.18430 0.87540 1.57540 -0.14760 -0.58380 -0.10380 95  VAL B CG2   
4184 N  N     . PHE B 96  ? 1.09330 0.76010 1.26220 -0.15330 -0.49190 -0.11230 96  PHE B N     
4185 C  CA    . PHE B 96  ? 1.19830 0.84500 1.28920 -0.15420 -0.47370 -0.11860 96  PHE B CA    
4186 C  C     . PHE B 96  ? 1.15390 0.81630 1.25510 -0.15940 -0.43860 -0.12270 96  PHE B C     
4187 O  O     . PHE B 96  ? 1.23110 0.87200 1.28100 -0.16180 -0.42950 -0.13290 96  PHE B O     
4188 C  CB    . PHE B 96  ? 1.17600 0.82200 1.21880 -0.14750 -0.46190 -0.10930 96  PHE B CB    
4189 C  CG    . PHE B 96  ? 1.37500 0.98630 1.37070 -0.14330 -0.49520 -0.10910 96  PHE B CG    
4190 C  CD1   . PHE B 96  ? 1.43400 1.00390 1.35550 -0.14420 -0.50660 -0.11940 96  PHE B CD1   
4191 C  CD2   . PHE B 96  ? 1.48970 1.10660 1.51360 -0.13810 -0.51470 -0.09870 96  PHE B CD2   
4192 C  CE1   . PHE B 96  ? 1.51460 1.04780 1.38770 -0.14020 -0.53710 -0.11860 96  PHE B CE1   
4193 C  CE2   . PHE B 96  ? 1.55880 1.13950 1.53720 -0.13420 -0.54630 -0.09810 96  PHE B CE2   
4194 C  CZ    . PHE B 96  ? 1.43700 0.97500 1.33810 -0.13530 -0.55760 -0.10770 96  PHE B CZ    
4195 N  N     . GLY B 97  ? 1.17700 0.87440 1.34360 -0.16060 -0.41850 -0.11450 97  GLY B N     
4196 C  CA    . GLY B 97  ? 1.07170 0.78280 1.25490 -0.16550 -0.38630 -0.11630 97  GLY B CA    
4197 C  C     . GLY B 97  ? 1.06080 0.77220 1.19050 -0.16290 -0.35520 -0.11550 97  GLY B C     
4198 O  O     . GLY B 97  ? 1.08070 0.80800 1.20130 -0.15730 -0.34230 -0.10560 97  GLY B O     
4199 N  N     . GLU B 98  ? 1.15240 0.84530 1.24890 -0.16670 -0.34360 -0.12660 98  GLU B N     
4200 C  CA    . GLU B 98  ? 1.11940 0.80980 1.16790 -0.16400 -0.31500 -0.12820 98  GLU B CA    
4201 C  C     . GLU B 98  ? 1.06540 0.73760 1.04870 -0.15820 -0.32300 -0.12930 98  GLU B C     
4202 O  O     . GLU B 98  ? 1.08890 0.76780 1.04270 -0.15390 -0.30000 -0.12580 98  GLU B O     
4203 C  CB    . GLU B 98  ? 1.28590 0.95710 1.31830 -0.16870 -0.30340 -0.14110 98  GLU B CB    
4204 C  CG    . GLU B 98  ? 1.42260 1.11000 1.51140 -0.17400 -0.28600 -0.13760 98  GLU B CG    
4205 C  CD    . GLU B 98  ? 1.68160 1.34970 1.74970 -0.17720 -0.26810 -0.14840 98  GLU B CD    
4206 O  OE1   . GLU B 98  ? 1.74220 1.38080 1.76560 -0.17760 -0.27930 -0.16260 98  GLU B OE1   
4207 O  OE2   . GLU B 98  ? 1.74310 1.42330 1.83810 -0.17860 -0.24290 -0.14250 98  GLU B OE2   
4208 N  N     . ASN B 99  ? 1.13540 0.78300 1.09650 -0.15790 -0.35580 -0.13370 99  ASN B N     
4209 C  CA    . ASN B 99  ? 1.19180 0.81500 1.08640 -0.15290 -0.36590 -0.13400 99  ASN B CA    
4210 C  C     . ASN B 99  ? 1.16910 0.80770 1.06810 -0.14730 -0.36840 -0.11920 99  ASN B C     
4211 O  O     . ASN B 99  ? 1.33830 0.95570 1.18300 -0.14330 -0.37540 -0.11720 99  ASN B O     
4212 C  CB    . ASN B 99  ? 1.28530 0.87000 1.14880 -0.15460 -0.40130 -0.14430 99  ASN B CB    
4213 C  CG    . ASN B 99  ? 1.31630 0.87890 1.16090 -0.15940 -0.39830 -0.16070 99  ASN B CG    
4214 O  OD1   . ASN B 99  ? 1.36390 0.91880 1.16970 -0.15820 -0.37320 -0.16690 99  ASN B OD1   
4215 N  ND2   . ASN B 99  ? 1.27800 0.82990 1.15230 -0.16450 -0.42410 -0.16820 99  ASN B ND2   
4216 N  N     . TRP B 100 ? 1.04620 0.71930 1.00890 -0.14700 -0.36180 -0.10880 100 TRP B N     
4217 C  CA    . TRP B 100 ? 1.04340 0.73420 1.01700 -0.14160 -0.36010 -0.09520 100 TRP B CA    
4218 C  C     . TRP B 100 ? 1.00830 0.71410 0.95760 -0.13860 -0.32590 -0.09030 100 TRP B C     
4219 O  O     . TRP B 100 ? 0.97900 0.71010 0.96060 -0.13980 -0.30060 -0.08820 100 TRP B O     
4220 C  CB    . TRP B 100 ? 0.99200 0.71290 1.04410 -0.14170 -0.36440 -0.08700 100 TRP B CB    
4221 C  CG    . TRP B 100 ? 1.00030 0.73300 1.06550 -0.13560 -0.37060 -0.07460 100 TRP B CG    
4222 C  CD1   . TRP B 100 ? 1.07760 0.79470 1.14400 -0.13250 -0.40290 -0.07160 100 TRP B CD1   
4223 C  CD2   . TRP B 100 ? 0.96730 0.72780 1.04650 -0.13170 -0.34480 -0.06410 100 TRP B CD2   
4224 N  NE1   . TRP B 100 ? 1.02780 0.76080 1.10870 -0.12700 -0.39790 -0.05990 100 TRP B NE1   
4225 C  CE2   . TRP B 100 ? 0.93770 0.69780 1.02610 -0.12660 -0.36230 -0.05540 100 TRP B CE2   
4226 C  CE3   . TRP B 100 ? 0.91840 0.70160 1.00210 -0.13190 -0.30960 -0.06150 100 TRP B CE3   
4227 C  CZ2   . TRP B 100 ? 0.93150 0.71400 1.03370 -0.12190 -0.34480 -0.04480 100 TRP B CZ2   
4228 C  CZ3   . TRP B 100 ? 0.90530 0.71050 1.00100 -0.12710 -0.29350 -0.05100 100 TRP B CZ3   
4229 C  CH2   . TRP B 100 ? 0.90360 0.70860 1.00840 -0.12230 -0.31060 -0.04300 100 TRP B CH2   
4230 N  N     . ASN B 101 ? 1.01910 0.70700 0.91070 -0.13490 -0.32570 -0.08830 101 ASN B N     
4231 C  CA    . ASN B 101 ? 1.02030 0.71880 0.88510 -0.13190 -0.29550 -0.08440 101 ASN B CA    
4232 C  C     . ASN B 101 ? 0.96300 0.65020 0.78740 -0.12760 -0.29890 -0.07580 101 ASN B C     
4233 O  O     . ASN B 101 ? 1.04550 0.71690 0.81710 -0.12620 -0.28530 -0.07770 101 ASN B O     
4234 C  CB    . ASN B 101 ? 1.05760 0.74030 0.88330 -0.13340 -0.27870 -0.09620 101 ASN B CB    
4235 C  CG    . ASN B 101 ? 1.24000 0.88100 1.00250 -0.13350 -0.29540 -0.10450 101 ASN B CG    
4236 O  OD1   . ASN B 101 ? 1.41320 1.03410 1.16520 -0.13360 -0.32440 -0.10330 101 ASN B OD1   
4237 N  ND2   . ASN B 101 ? 1.35030 0.97610 1.06950 -0.13270 -0.27710 -0.11310 101 ASN B ND2   
4238 N  N     . PRO B 102 ? 0.87650 0.57030 0.72570 -0.12530 -0.31580 -0.06590 102 PRO B N     
4239 C  CA    . PRO B 102 ? 0.85110 0.53540 0.66690 -0.12160 -0.31630 -0.05660 102 PRO B CA    
4240 C  C     . PRO B 102 ? 0.80040 0.51140 0.62080 -0.11960 -0.28350 -0.05050 102 PRO B C     
4241 O  O     . PRO B 102 ? 0.76950 0.51210 0.63910 -0.11940 -0.26960 -0.04870 102 PRO B O     
4242 C  CB    . PRO B 102 ? 0.86810 0.55700 0.72430 -0.11950 -0.34200 -0.04870 102 PRO B CB    
4243 C  CG    . PRO B 102 ? 0.87660 0.59580 0.80310 -0.12120 -0.33970 -0.05060 102 PRO B CG    
4244 C  CD    . PRO B 102 ? 0.85590 0.56630 0.76920 -0.12590 -0.33370 -0.06300 102 PRO B CD    
4245 N  N     . SER B 103 ? 0.92110 0.61720 0.69060 -0.11820 -0.27170 -0.04760 103 SER B N     
4246 C  CA    . SER B 103 ? 0.80540 0.52410 0.57780 -0.11620 -0.24370 -0.04150 103 SER B CA    
4247 C  C     . SER B 103 ? 0.82230 0.56510 0.63900 -0.11360 -0.24690 -0.03080 103 SER B C     
4248 O  O     . SER B 103 ? 1.02880 0.76390 0.86120 -0.11280 -0.27130 -0.02680 103 SER B O     
4249 C  CB    . SER B 103 ? 0.90130 0.59590 0.61300 -0.11600 -0.23360 -0.03940 103 SER B CB    
4250 O  OG    . SER B 103 ? 0.88950 0.56600 0.58420 -0.11530 -0.25080 -0.03090 103 SER B OG    
4251 N  N     . GLU B 104 ? 0.81760 0.58820 0.65410 -0.11170 -0.22270 -0.02650 104 GLU B N     
4252 C  CA    . GLU B 104 ? 0.74540 0.54030 0.62350 -0.10870 -0.22130 -0.01740 104 GLU B CA    
4253 C  C     . GLU B 104 ? 0.71940 0.49710 0.57710 -0.10730 -0.23560 -0.00890 104 GLU B C     
4254 O  O     . GLU B 104 ? 0.65460 0.44060 0.54720 -0.10490 -0.24870 -0.00290 104 GLU B O     
4255 C  CB    . GLU B 104 ? 0.66560 0.48740 0.55680 -0.10690 -0.19240 -0.01550 104 GLU B CB    
4256 C  CG    . GLU B 104 ? 0.65120 0.50010 0.58930 -0.10350 -0.18790 -0.00800 104 GLU B CG    
4257 C  CD    . GLU B 104 ? 0.63560 0.51100 0.59820 -0.10220 -0.16300 -0.00940 104 GLU B CD    
4258 O  OE1   . GLU B 104 ? 0.55780 0.43700 0.53440 -0.10440 -0.15810 -0.01590 104 GLU B OE1   
4259 O  OE2   . GLU B 104 ? 0.57220 0.46200 0.53900 -0.09920 -0.14910 -0.00400 104 GLU B OE2   
4260 N  N     . THR B 105 ? 0.73430 0.48650 0.53630 -0.10880 -0.23180 -0.00850 105 THR B N     
4261 C  CA    . THR B 105 ? 0.84550 0.57330 0.61860 -0.10880 -0.24500 -0.00110 105 THR B CA    
4262 C  C     . THR B 105 ? 0.91430 0.61920 0.69100 -0.10840 -0.27930 -0.00100 105 THR B C     
4263 O  O     . THR B 105 ? 0.92270 0.62280 0.71320 -0.10630 -0.29510 0.00630  105 THR B O     
4264 C  CB    . THR B 105 ? 0.92820 0.62800 0.63760 -0.11180 -0.23310 -0.00250 105 THR B CB    
4265 O  OG1   . THR B 105 ? 0.80970 0.53120 0.52110 -0.11190 -0.20270 -0.00220 105 THR B OG1   
4266 C  CG2   . THR B 105 ? 0.96370 0.63400 0.64050 -0.11260 -0.24650 0.00500  105 THR B CG2   
4267 N  N     . VAL B 106 ? 0.91210 0.60210 0.67770 -0.11020 -0.29160 -0.00970 106 VAL B N     
4268 C  CA    . VAL B 106 ? 0.92850 0.59620 0.69940 -0.10980 -0.32600 -0.01140 106 VAL B CA    
4269 C  C     . VAL B 106 ? 0.86030 0.55630 0.70380 -0.10700 -0.33740 -0.00800 106 VAL B C     
4270 O  O     . VAL B 106 ? 0.90900 0.59350 0.76760 -0.10460 -0.36220 -0.00300 106 VAL B O     
4271 C  CB    . VAL B 106 ? 0.96310 0.61100 0.70930 -0.11270 -0.33460 -0.02290 106 VAL B CB    
4272 C  CG1   . VAL B 106 ? 1.04220 0.67110 0.80400 -0.11220 -0.37190 -0.02540 106 VAL B CG1   
4273 C  CG2   . VAL B 106 ? 1.07880 0.69260 0.75010 -0.11470 -0.32530 -0.02620 106 VAL B CG2   
4274 N  N     . ARG B 107 ? 0.78650 0.51780 0.67470 -0.10720 -0.31820 -0.01070 107 ARG B N     
4275 C  CA    . ARG B 107 ? 0.77290 0.53450 0.73370 -0.10470 -0.32150 -0.00790 107 ARG B CA    
4276 C  C     . ARG B 107 ? 0.75970 0.53040 0.74000 -0.10030 -0.32170 0.00240  107 ARG B C     
4277 O  O     . ARG B 107 ? 0.77390 0.54860 0.79900 -0.09740 -0.34070 0.00560  107 ARG B O     
4278 C  CB    . ARG B 107 ? 0.69780 0.49210 0.69070 -0.10600 -0.29370 -0.01160 107 ARG B CB    
4279 C  CG    . ARG B 107 ? 0.77100 0.55850 0.75610 -0.11060 -0.29340 -0.02220 107 ARG B CG    
4280 C  CD    . ARG B 107 ? 0.75800 0.57570 0.77980 -0.11190 -0.26740 -0.02450 107 ARG B CD    
4281 N  NE    . ARG B 107 ? 0.72720 0.56750 0.81510 -0.11040 -0.27050 -0.02040 107 ARG B NE    
4282 C  CZ    . ARG B 107 ? 0.63790 0.50640 0.76390 -0.10940 -0.24690 -0.01730 107 ARG B CZ    
4283 N  NH1   . ARG B 107 ? 0.57010 0.44860 0.67590 -0.10960 -0.22010 -0.01790 107 ARG B NH1   
4284 N  NH2   . ARG B 107 ? 0.61560 0.50080 0.80030 -0.10760 -0.25020 -0.01330 107 ARG B NH2   
4285 N  N     . LEU B 108 ? 0.70350 0.47700 0.65370 -0.09990 -0.30130 0.00690  108 LEU B N     
4286 C  CA    . LEU B 108 ? 0.73000 0.51070 0.69420 -0.09630 -0.29940 0.01610  108 LEU B CA    
4287 C  C     . LEU B 108 ? 0.71780 0.46490 0.66080 -0.09550 -0.32880 0.02050  108 LEU B C     
4288 O  O     . LEU B 108 ? 0.71970 0.47100 0.70060 -0.09170 -0.34270 0.02570  108 LEU B O     
4289 C  CB    . LEU B 108 ? 0.68140 0.47040 0.61520 -0.09710 -0.27110 0.01870  108 LEU B CB    
4290 C  CG    . LEU B 108 ? 0.65780 0.45510 0.60290 -0.09410 -0.26530 0.02740  108 LEU B CG    
4291 C  CD1   . LEU B 108 ? 0.70200 0.52960 0.71310 -0.08930 -0.26320 0.02960  108 LEU B CD1   
4292 C  CD2   . LEU B 108 ? 0.62600 0.43070 0.54060 -0.09580 -0.23770 0.02840  108 LEU B CD2   
4293 N  N     . THR B 109 ? 0.81410 0.52570 0.69580 -0.09890 -0.33780 0.01800  109 THR B N     
4294 C  CA    . THR B 109 ? 0.88930 0.56180 0.73890 -0.09870 -0.36570 0.02150  109 THR B CA    
4295 C  C     . THR B 109 ? 0.89960 0.56420 0.78810 -0.09590 -0.40000 0.01990  109 THR B C     
4296 O  O     . THR B 109 ? 1.01040 0.65790 0.90670 -0.09330 -0.42310 0.02500  109 THR B O     
4297 C  CB    . THR B 109 ? 0.87460 0.50870 0.64760 -0.10290 -0.36600 0.01770  109 THR B CB    
4298 O  OG1   . THR B 109 ? 0.94530 0.58720 0.68850 -0.10540 -0.33400 0.01940  109 THR B OG1   
4299 C  CG2   . THR B 109 ? 0.95720 0.54680 0.69150 -0.10270 -0.39470 0.02150  109 THR B CG2   
4300 N  N     . ALA B 110 ? 0.91630 0.59300 0.83170 -0.09680 -0.40360 0.01240  110 ALA B N     
4301 C  CA    . ALA B 110 ? 0.96720 0.64180 0.93010 -0.09460 -0.43390 0.00990  110 ALA B CA    
4302 C  C     . ALA B 110 ? 0.91780 0.61880 0.95030 -0.08970 -0.43540 0.01630  110 ALA B C     
4303 O  O     . ALA B 110 ? 1.00660 0.69320 1.06430 -0.08650 -0.46480 0.01830  110 ALA B O     
4304 C  CB    . ALA B 110 ? 1.00690 0.69580 0.99230 -0.09740 -0.43040 0.00070  110 ALA B CB    
4305 N  N     . ARG B 111 ? 0.87280 0.61080 0.93510 -0.08870 -0.40360 0.01890  111 ARG B N     
4306 C  CA    . ARG B 111 ? 0.89610 0.66230 1.02430 -0.08370 -0.39750 0.02440  111 ARG B CA    
4307 C  C     . ARG B 111 ? 0.90690 0.65710 1.01880 -0.08090 -0.40560 0.03210  111 ARG B C     
4308 O  O     . ARG B 111 ? 0.84420 0.60190 1.00830 -0.07630 -0.41720 0.03560  111 ARG B O     
4309 C  CB    . ARG B 111 ? 0.79980 0.60490 0.95310 -0.08360 -0.36040 0.02410  111 ARG B CB    
4310 C  CG    . ARG B 111 ? 0.81630 0.64030 1.00810 -0.08560 -0.35460 0.01750  111 ARG B CG    
4311 C  CD    . ARG B 111 ? 0.81570 0.67210 1.02220 -0.08620 -0.31800 0.01690  111 ARG B CD    
4312 N  NE    . ARG B 111 ? 0.83220 0.69760 1.05790 -0.09010 -0.31310 0.00990  111 ARG B NE    
4313 C  CZ    . ARG B 111 ? 0.69810 0.58890 0.98090 -0.08950 -0.29930 0.00950  111 ARG B CZ    
4314 N  NH1   . ARG B 111 ? 0.78880 0.69980 1.11610 -0.08440 -0.28720 0.01520  111 ARG B NH1   
4315 N  NH2   . ARG B 111 ? 0.69640 0.59030 0.99070 -0.09410 -0.29640 0.00320  111 ARG B NH2   
4316 N  N     . ILE B 112 ? 0.77500 0.50320 0.82000 -0.08390 -0.39910 0.03440  112 ILE B N     
4317 C  CA    . ILE B 112 ? 0.85440 0.56140 0.87790 -0.08280 -0.40890 0.04140  112 ILE B CA    
4318 C  C     . ILE B 112 ? 0.90820 0.58230 0.93570 -0.08100 -0.44970 0.04140  112 ILE B C     
4319 O  O     . ILE B 112 ? 0.89960 0.57260 0.96270 -0.07710 -0.46420 0.04560  112 ILE B O     
4320 C  CB    . ILE B 112 ? 0.83050 0.51660 0.77940 -0.08750 -0.39380 0.04310  112 ILE B CB    
4321 C  CG1   . ILE B 112 ? 0.78800 0.50740 0.74070 -0.08840 -0.35560 0.04380  112 ILE B CG1   
4322 C  CG2   . ILE B 112 ? 0.92410 0.58100 0.84690 -0.08750 -0.40860 0.04970  112 ILE B CG2   
4323 C  CD1   . ILE B 112 ? 0.82460 0.52820 0.71130 -0.09360 -0.33700 0.04360  112 ILE B CD1   
4324 N  N     . LEU B 113 ? 0.87760 0.52420 0.86900 -0.08360 -0.46880 0.03590  113 LEU B N     
4325 C  CA    . LEU B 113 ? 1.00930 0.62050 0.99770 -0.08200 -0.51030 0.03460  113 LEU B CA    
4326 C  C     . LEU B 113 ? 0.94300 0.57390 1.01630 -0.07700 -0.52920 0.03370  113 LEU B C     
4327 O  O     . LEU B 113 ? 1.00600 0.61690 1.09680 -0.07380 -0.55910 0.03580  113 LEU B O     
4328 C  CB    . LEU B 113 ? 1.01670 0.59810 0.95340 -0.08550 -0.52440 0.02750  113 LEU B CB    
4329 C  CG    . LEU B 113 ? 1.10230 0.65210 0.94990 -0.09000 -0.51220 0.02810  113 LEU B CG    
4330 C  CD1   . LEU B 113 ? 1.20530 0.73300 1.00780 -0.09320 -0.51820 0.01950  113 LEU B CD1   
4331 C  CD2   . LEU B 113 ? 1.13520 0.64430 0.94240 -0.08930 -0.53360 0.03390  113 LEU B CD2   
4332 N  N     . ALA B 114 ? 0.91680 0.58610 1.04340 -0.07660 -0.51080 0.03020  114 ALA B N     
4333 C  CA    . ALA B 114 ? 0.91800 0.61060 1.13130 -0.07240 -0.52140 0.02900  114 ALA B CA    
4334 C  C     . ALA B 114 ? 0.92760 0.63680 1.18450 -0.06760 -0.51340 0.03570  114 ALA B C     
4335 O  O     . ALA B 114 ? 1.04230 0.74690 1.34940 -0.06360 -0.53750 0.03620  114 ALA B O     
4336 C  CB    . ALA B 114 ? 0.87620 0.60430 1.12910 -0.07400 -0.49820 0.02410  114 ALA B CB    
4337 N  N     . LYS B 115 ? 0.99850 0.72600 1.23670 -0.06810 -0.48000 0.04000  115 LYS B N     
4338 C  CA    . LYS B 115 ? 0.89960 0.64120 1.17060 -0.06410 -0.46960 0.04590  115 LYS B CA    
4339 C  C     . LYS B 115 ? 0.86830 0.57480 1.11960 -0.06290 -0.49960 0.04960  115 LYS B C     
4340 O  O     . LYS B 115 ? 1.03320 0.74510 1.33790 -0.05850 -0.51010 0.05160  115 LYS B O     
4341 C  CB    . LYS B 115 ? 0.94390 0.70540 1.18540 -0.06560 -0.43150 0.04910  115 LYS B CB    
4342 C  CG    . LYS B 115 ? 0.93200 0.71150 1.20970 -0.06130 -0.41710 0.05410  115 LYS B CG    
4343 C  CD    . LYS B 115 ? 0.98970 0.80380 1.34870 -0.05650 -0.40410 0.05240  115 LYS B CD    
4344 C  CE    . LYS B 115 ? 0.92880 0.75720 1.32060 -0.05210 -0.38980 0.05660  115 LYS B CE    
4345 N  NZ    . LYS B 115 ? 0.97040 0.83270 1.43350 -0.04770 -0.36840 0.05470  115 LYS B NZ    
4346 N  N     . GLN B 116 ? 0.87180 0.54130 1.04640 -0.06700 -0.51220 0.05020  116 GLN B N     
4347 C  CA    . GLN B 116 ? 0.98560 0.61580 1.12950 -0.06680 -0.54140 0.05360  116 GLN B CA    
4348 C  C     . GLN B 116 ? 1.02050 0.63360 1.20750 -0.06300 -0.58280 0.05060  116 GLN B C     
4349 O  O     . GLN B 116 ? 1.09620 0.69280 1.29800 -0.06030 -0.60480 0.05340  116 GLN B O     
4350 C  CB    . GLN B 116 ? 1.00070 0.59220 1.05030 -0.07220 -0.54440 0.05400  116 GLN B CB    
4351 C  CG    . GLN B 116 ? 0.92950 0.52880 0.93400 -0.07620 -0.50950 0.05800  116 GLN B CG    
4352 C  CD    . GLN B 116 ? 0.95280 0.51220 0.86740 -0.08170 -0.51080 0.05810  116 GLN B CD    
4353 O  OE1   . GLN B 116 ? 1.05070 0.59960 0.92460 -0.08480 -0.49630 0.06250  116 GLN B OE1   
4354 N  NE2   . GLN B 116 ? 1.06560 0.60130 0.94900 -0.08310 -0.52770 0.05280  116 GLN B NE2   
4355 N  N     . LYS B 117 ? 1.18820 0.80510 1.39620 -0.06300 -0.59400 0.04440  117 LYS B N     
4356 C  CA    . LYS B 117 ? 1.27860 0.88110 1.53250 -0.05970 -0.63380 0.04040  117 LYS B CA    
4357 C  C     . LYS B 117 ? 1.23470 0.86890 1.58610 -0.05440 -0.63260 0.04090  117 LYS B C     
4358 O  O     . LYS B 117 ? 1.46860 1.08680 1.85480 -0.05090 -0.66450 0.04060  117 LYS B O     
4359 C  CB    . LYS B 117 ? 1.40360 1.00480 1.65660 -0.06180 -0.64300 0.03300  117 LYS B CB    
4360 C  CG    . LYS B 117 ? 1.63210 1.18990 1.79380 -0.06600 -0.65850 0.03050  117 LYS B CG    
4361 C  CD    . LYS B 117 ? 1.83320 1.39510 1.99290 -0.06880 -0.66000 0.02250  117 LYS B CD    
4362 C  CE    . LYS B 117 ? 1.82560 1.38090 2.04410 -0.06590 -0.69860 0.01660  117 LYS B CE    
4363 N  NZ    . LYS B 117 ? 1.86160 1.42500 2.08690 -0.06920 -0.69850 0.00820  117 LYS B NZ    
4364 N  N     . ILE B 118 ? 1.20680 0.88460 1.60100 -0.05390 -0.59510 0.04130  118 ILE B N     
4365 C  CA    . ILE B 118 ? 1.12050 0.83060 1.60700 -0.04910 -0.58600 0.04130  118 ILE B CA    
4366 C  C     . ILE B 118 ? 1.04370 0.75490 1.53750 -0.04650 -0.57900 0.04690  118 ILE B C     
4367 O  O     . ILE B 118 ? 1.23230 0.94200 1.78290 -0.04250 -0.59790 0.04660  118 ILE B O     
4368 C  CB    . ILE B 118 ? 1.12760 0.88060 1.64930 -0.04950 -0.54580 0.03980  118 ILE B CB    
4369 C  CG1   . ILE B 118 ? 1.15400 0.90830 1.67870 -0.05260 -0.55330 0.03350  118 ILE B CG1   
4370 C  CG2   . ILE B 118 ? 1.06890 0.85250 1.68120 -0.04460 -0.53170 0.04010  118 ILE B CG2   
4371 C  CD1   . ILE B 118 ? 1.22270 1.01210 1.75770 -0.05470 -0.51370 0.03210  118 ILE B CD1   
4372 N  N     . HIS B 119 ? 1.00230 0.71630 1.44020 -0.04900 -0.55190 0.05130  119 HIS B N     
4373 C  CA    . HIS B 119 ? 1.02570 0.74570 1.46860 -0.04720 -0.53850 0.05630  119 HIS B CA    
4374 C  C     . HIS B 119 ? 1.07120 0.75520 1.43130 -0.05100 -0.54970 0.06040  119 HIS B C     
4375 O  O     . HIS B 119 ? 1.21640 0.90460 1.52700 -0.05420 -0.52330 0.06350  119 HIS B O     
4376 C  CB    . HIS B 119 ? 0.99940 0.75820 1.45750 -0.04660 -0.49300 0.05760  119 HIS B CB    
4377 C  CG    . HIS B 119 ? 1.04750 0.81980 1.53760 -0.04340 -0.47900 0.06080  119 HIS B CG    
4378 N  ND1   . HIS B 119 ? 1.13990 0.90030 1.57980 -0.04550 -0.47210 0.06530  119 HIS B ND1   
4379 C  CD2   . HIS B 119 ? 1.09920 0.89340 1.66760 -0.03850 -0.47230 0.05950  119 HIS B CD2   
4380 C  CE1   . HIS B 119 ? 1.24860 1.02440 1.73380 -0.04190 -0.46190 0.06650  119 HIS B CE1   
4381 N  NE2   . HIS B 119 ? 1.11330 0.90950 1.67600 -0.03760 -0.46110 0.06290  119 HIS B NE2   
4382 N  N     . PRO B 120 ? 1.24490 0.89100 1.58770 -0.05080 -0.58920 0.06040  120 PRO B N     
4383 C  CA    . PRO B 120 ? 1.28520 0.89180 1.54340 -0.05480 -0.60090 0.06410  120 PRO B CA    
4384 C  C     . PRO B 120 ? 1.24630 0.85590 1.49150 -0.05540 -0.58490 0.06950  120 PRO B C     
4385 O  O     . PRO B 120 ? 1.13060 0.71950 1.30340 -0.06010 -0.57700 0.07280  120 PRO B O     
4386 C  CB    . PRO B 120 ? 1.33820 0.90630 1.59640 -0.05270 -0.64950 0.06220  120 PRO B CB    
4387 C  CG    . PRO B 120 ? 1.28500 0.87820 1.64360 -0.04700 -0.66050 0.05910  120 PRO B CG    
4388 C  CD    . PRO B 120 ? 1.19070 0.82890 1.59460 -0.04660 -0.62480 0.05680  120 PRO B CD    
4389 N  N     . GLU B 121 ? 1.35190 0.98670 1.66770 -0.05090 -0.57980 0.06990  121 GLU B N     
4390 C  CA    . GLU B 121 ? 1.37220 1.01310 1.68520 -0.05100 -0.56540 0.07410  121 GLU B CA    
4391 C  C     . GLU B 121 ? 1.33000 0.99910 1.62450 -0.05350 -0.52140 0.07590  121 GLU B C     
4392 O  O     . GLU B 121 ? 1.26990 0.95730 1.56090 -0.05440 -0.50110 0.07390  121 GLU B O     
4393 C  CB    . GLU B 121 ? 1.45980 1.11810 1.85750 -0.04510 -0.57480 0.07280  121 GLU B CB    
4394 C  CG    . GLU B 121 ? 1.67120 1.37500 2.14520 -0.04120 -0.54520 0.06990  121 GLU B CG    
4395 C  CD    . GLU B 121 ? 2.04080 1.75440 2.56520 -0.03890 -0.55530 0.06490  121 GLU B CD    
4396 O  OE1   . GLU B 121 ? 2.58300 2.27760 3.06740 -0.04150 -0.57010 0.06360  121 GLU B OE1   
4397 O  OE2   . GLU B 121 ? 2.00090 1.74070 2.60680 -0.03450 -0.54810 0.06200  121 GLU B OE2   
4398 N  N     . ARG B 122 ? 1.00240 0.67430 1.28570 -0.05430 -0.50870 0.07950  122 ARG B N     
4399 C  CA    . ARG B 122 ? 0.98390 0.67890 1.24780 -0.05660 -0.47040 0.08130  122 ARG B CA    
4400 C  C     . ARG B 122 ? 0.89290 0.63050 1.22360 -0.05160 -0.44410 0.07840  122 ARG B C     
4401 O  O     . ARG B 122 ? 1.06900 0.82060 1.46800 -0.04640 -0.44980 0.07660  122 ARG B O     
4402 C  CB    . ARG B 122 ? 0.99930 0.68640 1.24740 -0.05790 -0.46920 0.08500  122 ARG B CB    
4403 C  CG    . ARG B 122 ? 1.01400 0.72010 1.23830 -0.06070 -0.43420 0.08670  122 ARG B CG    
4404 C  CD    . ARG B 122 ? 1.03430 0.73010 1.24090 -0.06230 -0.43650 0.09000  122 ARG B CD    
4405 N  NE    . ARG B 122 ? 1.16250 0.81860 1.29710 -0.06810 -0.45400 0.09330  122 ARG B NE    
4406 C  CZ    . ARG B 122 ? 1.17050 0.81430 1.23860 -0.07500 -0.43820 0.09510  122 ARG B CZ    
4407 N  NH1   . ARG B 122 ? 1.11700 0.78570 1.18120 -0.07730 -0.40660 0.09390  122 ARG B NH1   
4408 N  NH2   . ARG B 122 ? 1.10780 0.71330 1.11330 -0.07950 -0.45390 0.09790  122 ARG B NH2   
4409 N  N     . THR B 123 ? 0.86520 0.62180 1.17630 -0.05300 -0.41590 0.07780  123 THR B N     
4410 C  CA    . THR B 123 ? 0.80730 0.60200 1.17130 -0.04830 -0.38860 0.07510  123 THR B CA    
4411 C  C     . THR B 123 ? 0.76560 0.58050 1.13230 -0.04690 -0.35930 0.07680  123 THR B C     
4412 O  O     . THR B 123 ? 0.73050 0.53130 1.05150 -0.05090 -0.35820 0.07990  123 THR B O     
4413 C  CB    . THR B 123 ? 0.85060 0.65560 1.19170 -0.05010 -0.37500 0.07280  123 THR B CB    
4414 O  OG1   . THR B 123 ? 0.73750 0.53480 1.00920 -0.05540 -0.36060 0.07490  123 THR B OG1   
4415 C  CG2   . THR B 123 ? 0.93770 0.72340 1.27750 -0.05130 -0.40380 0.07020  123 THR B CG2   
4416 N  N     . PRO B 124 ? 0.86140 0.70850 1.28040 -0.04160 -0.33440 0.07430  124 PRO B N     
4417 C  CA    . PRO B 124 ? 0.78790 0.65420 1.20430 -0.03980 -0.30470 0.07490  124 PRO B CA    
4418 C  C     . PRO B 124 ? 0.90120 0.76850 1.25330 -0.04390 -0.28740 0.07650  124 PRO B C     
4419 O  O     . PRO B 124 ? 0.81810 0.69500 1.15900 -0.04330 -0.26860 0.07750  124 PRO B O     
4420 C  CB    . PRO B 124 ? 0.75230 0.64910 1.23180 -0.03360 -0.28170 0.07100  124 PRO B CB    
4421 C  CG    . PRO B 124 ? 0.76100 0.65270 1.29230 -0.03200 -0.30400 0.06890  124 PRO B CG    
4422 C  CD    . PRO B 124 ? 0.74900 0.61350 1.23350 -0.03710 -0.33340 0.07040  124 PRO B CD    
4423 N  N     . SER B 125 ? 0.93210 0.78990 1.24620 -0.04810 -0.29390 0.07610  125 SER B N     
4424 C  CA    . SER B 125 ? 0.78070 0.63670 1.03310 -0.05320 -0.27960 0.07680  125 SER B CA    
4425 C  C     . SER B 125 ? 0.73770 0.56400 0.93360 -0.05990 -0.29050 0.08080  125 SER B C     
4426 O  O     . SER B 125 ? 0.68260 0.50760 0.83170 -0.06460 -0.27540 0.08160  125 SER B O     
4427 C  CB    . SER B 125 ? 0.85220 0.70660 1.08530 -0.05600 -0.28290 0.07370  125 SER B CB    
4428 O  OG    . SER B 125 ? 1.04230 0.92360 1.32300 -0.05140 -0.27040 0.06960  125 SER B OG    
4429 N  N     . GLU B 126 ? 0.87360 0.67590 1.07500 -0.06090 -0.31650 0.08270  126 GLU B N     
4430 C  CA    . GLU B 126 ? 0.81450 0.58330 0.96040 -0.06800 -0.33100 0.08570  126 GLU B CA    
4431 C  C     . GLU B 126 ? 0.77910 0.54270 0.94080 -0.06750 -0.33790 0.08790  126 GLU B C     
4432 O  O     . GLU B 126 ? 0.84560 0.58210 0.99190 -0.06970 -0.36250 0.08950  126 GLU B O     
4433 C  CB    . GLU B 126 ? 0.76880 0.50750 0.89540 -0.07010 -0.36080 0.08520  126 GLU B CB    
4434 C  CG    . GLU B 126 ? 0.83850 0.57880 0.94790 -0.07110 -0.35830 0.08210  126 GLU B CG    
4435 C  CD    . GLU B 126 ? 0.84330 0.55790 0.95270 -0.07070 -0.39110 0.08050  126 GLU B CD    
4436 O  OE1   . GLU B 126 ? 0.81990 0.54380 0.98840 -0.06510 -0.40570 0.07900  126 GLU B OE1   
4437 O  OE2   . GLU B 126 ? 0.88110 0.56530 0.93190 -0.07590 -0.40190 0.08040  126 GLU B OE2   
4438 N  N     . LYS B 127 ? 0.73150 0.52050 0.92210 -0.06410 -0.31660 0.08760  127 LYS B N     
4439 C  CA    . LYS B 127 ? 0.78240 0.57090 0.99220 -0.06310 -0.32110 0.08850  127 LYS B CA    
4440 C  C     . LYS B 127 ? 0.84590 0.60920 0.99510 -0.07120 -0.32720 0.09140  127 LYS B C     
4441 O  O     . LYS B 127 ? 0.77330 0.52190 0.92380 -0.07090 -0.34540 0.09310  127 LYS B O     
4442 C  CB    . LYS B 127 ? 0.91930 0.74070 1.16900 -0.05720 -0.29470 0.08640  127 LYS B CB    
4443 C  CG    . LYS B 127 ? 0.78860 0.63400 1.10410 -0.04890 -0.28670 0.08290  127 LYS B CG    
4444 C  CD    . LYS B 127 ? 0.80070 0.67650 1.14600 -0.04280 -0.25710 0.08010  127 LYS B CD    
4445 C  CE    . LYS B 127 ? 0.71930 0.61750 1.11880 -0.03590 -0.24210 0.07640  127 LYS B CE    
4446 N  NZ    . LYS B 127 ? 0.98330 0.87970 1.43810 -0.03320 -0.25890 0.07460  127 LYS B NZ    
4447 N  N     . LEU B 128 ? 0.74130 0.50070 0.83880 -0.07780 -0.31090 0.09200  128 LEU B N     
4448 C  CA    . LEU B 128 ? 0.73570 0.47370 0.77500 -0.08610 -0.31060 0.09390  128 LEU B CA    
4449 C  C     . LEU B 128 ? 0.79430 0.50230 0.77230 -0.09310 -0.31720 0.09450  128 LEU B C     
4450 O  O     . LEU B 128 ? 0.79390 0.47660 0.72540 -0.09840 -0.32320 0.09660  128 LEU B O     
4451 C  CB    . LEU B 128 ? 0.71070 0.47090 0.74040 -0.08810 -0.28280 0.09260  128 LEU B CB    
4452 C  CG    . LEU B 128 ? 0.68920 0.47510 0.76390 -0.08070 -0.27520 0.09170  128 LEU B CG    
4453 C  CD1   . LEU B 128 ? 0.60350 0.40960 0.66020 -0.08150 -0.24910 0.08990  128 LEU B CD1   
4454 C  CD2   . LEU B 128 ? 0.85590 0.62360 0.93450 -0.08050 -0.29640 0.09450  128 LEU B CD2   
4455 N  N     . LEU B 129 ? 0.71480 0.42610 0.69210 -0.09230 -0.31450 0.09260  129 LEU B N     
4456 C  CA    . LEU B 129 ? 0.69500 0.38000 0.61750 -0.09780 -0.31910 0.09180  129 LEU B CA    
4457 C  C     . LEU B 129 ? 0.71160 0.39610 0.65450 -0.09300 -0.33350 0.08990  129 LEU B C     
4458 O  O     . LEU B 129 ? 0.70140 0.41470 0.68170 -0.08820 -0.32160 0.08790  129 LEU B O     
4459 C  CB    . LEU B 129 ? 0.67270 0.36690 0.56010 -0.10400 -0.29040 0.08960  129 LEU B CB    
4460 C  CG    . LEU B 129 ? 0.69200 0.36060 0.52160 -0.10990 -0.28930 0.08760  129 LEU B CG    
4461 C  CD1   . LEU B 129 ? 0.74490 0.37570 0.52510 -0.11460 -0.30230 0.09010  129 LEU B CD1   
4462 C  CD2   . LEU B 129 ? 0.70910 0.39430 0.51900 -0.11460 -0.25900 0.08410  129 LEU B CD2   
4463 N  N     . ALA B 130 ? 0.81700 0.46820 0.73370 -0.09400 -0.35960 0.09040  130 ALA B N     
4464 C  CA    . ALA B 130 ? 0.83390 0.47960 0.76540 -0.09020 -0.37790 0.08800  130 ALA B CA    
4465 C  C     . ALA B 130 ? 0.87970 0.51380 0.76100 -0.09480 -0.36870 0.08500  130 ALA B C     
4466 O  O     . ALA B 130 ? 0.91860 0.53580 0.74440 -0.10140 -0.35580 0.08530  130 ALA B O     
4467 C  CB    . ALA B 130 ? 0.87530 0.48920 0.80600 -0.08810 -0.41410 0.08950  130 ALA B CB    
4468 N  N     . VAL B 131 ? 0.77900 0.42280 0.68270 -0.09120 -0.37470 0.08150  131 VAL B N     
4469 C  CA    . VAL B 131 ? 0.79820 0.43210 0.66120 -0.09450 -0.36930 0.07750  131 VAL B CA    
4470 C  C     . VAL B 131 ? 0.96060 0.54630 0.75710 -0.09920 -0.38700 0.07790  131 VAL B C     
4471 O  O     . VAL B 131 ? 0.95510 0.52700 0.69850 -0.10450 -0.37190 0.07600  131 VAL B O     
4472 C  CB    . VAL B 131 ? 0.82070 0.47010 0.72470 -0.08950 -0.38010 0.07330  131 VAL B CB    
4473 C  CG1   . VAL B 131 ? 0.81360 0.44780 0.67290 -0.09300 -0.37890 0.06840  131 VAL B CG1   
4474 C  CG2   . VAL B 131 ? 0.82050 0.51670 0.78340 -0.08480 -0.35810 0.07240  131 VAL B CG2   
4475 N  N     . LYS B 132 ? 0.90310 0.46280 0.70360 -0.09670 -0.41890 0.08020  132 LYS B N     
4476 C  CA    . LYS B 132 ? 1.07970 0.58960 0.81660 -0.09970 -0.43980 0.08140  132 LYS B CA    
4477 C  C     . LYS B 132 ? 1.06190 0.55490 0.74290 -0.10600 -0.42050 0.08440  132 LYS B C     
4478 O  O     . LYS B 132 ? 1.06250 0.51770 0.67790 -0.10970 -0.42370 0.08430  132 LYS B O     
4479 C  CB    . LYS B 132 ? 1.14350 0.63220 0.90260 -0.09490 -0.47770 0.08380  132 LYS B CB    
4480 C  CG    . LYS B 132 ? 1.17660 0.68080 0.99910 -0.08840 -0.50000 0.08060  132 LYS B CG    
4481 C  CD    . LYS B 132 ? 1.28100 0.76780 1.07940 -0.08860 -0.51320 0.07560  132 LYS B CD    
4482 C  CE    . LYS B 132 ? 1.36100 0.79440 1.11100 -0.08830 -0.55000 0.07590  132 LYS B CE    
4483 N  NZ    . LYS B 132 ? 1.33230 0.75040 1.06940 -0.08740 -0.56760 0.07000  132 LYS B NZ    
4484 N  N     . GLU B 133 ? 1.11250 0.63280 0.82010 -0.10690 -0.40040 0.08690  133 GLU B N     
4485 C  CA    . GLU B 133 ? 1.14860 0.65860 0.81370 -0.11280 -0.38120 0.08960  133 GLU B CA    
4486 C  C     . GLU B 133 ? 1.16550 0.69230 0.80800 -0.11820 -0.34520 0.08610  133 GLU B C     
4487 O  O     . GLU B 133 ? 1.17310 0.69340 0.78270 -0.12330 -0.32660 0.08740  133 GLU B O     
4488 C  CB    . GLU B 133 ? 1.16550 0.69570 0.87160 -0.11090 -0.37970 0.09340  133 GLU B CB    
4489 C  CG    . GLU B 133 ? 1.13720 0.65100 0.86690 -0.10550 -0.41380 0.09680  133 GLU B CG    
4490 C  CD    . GLU B 133 ? 1.17350 0.71420 0.95640 -0.10220 -0.41120 0.09920  133 GLU B CD    
4491 O  OE1   . GLU B 133 ? 0.97580 0.55030 0.78320 -0.10330 -0.38450 0.09800  133 GLU B OE1   
4492 O  OE2   . GLU B 133 ? 1.24110 0.76860 1.04240 -0.09780 -0.43710 0.10210  133 GLU B OE2   
4493 N  N     . PHE B 134 ? 1.06060 0.60960 0.72330 -0.11660 -0.33570 0.08150  134 PHE B N     
4494 C  CA    . PHE B 134 ? 0.90890 0.47570 0.55600 -0.12070 -0.30360 0.07730  134 PHE B CA    
4495 C  C     . PHE B 134 ? 1.00340 0.53610 0.58060 -0.12670 -0.29350 0.07590  134 PHE B C     
4496 O  O     . PHE B 134 ? 1.02270 0.51640 0.55840 -0.12660 -0.31310 0.07640  134 PHE B O     
4497 C  CB    . PHE B 134 ? 0.96070 0.54760 0.63150 -0.11730 -0.30140 0.07260  134 PHE B CB    
4498 C  CG    . PHE B 134 ? 0.85870 0.49040 0.59600 -0.11200 -0.29360 0.07270  134 PHE B CG    
4499 C  CD1   . PHE B 134 ? 0.89330 0.54650 0.66520 -0.11070 -0.28600 0.07640  134 PHE B CD1   
4500 C  CD2   . PHE B 134 ? 0.80050 0.45230 0.56310 -0.10820 -0.29230 0.06860  134 PHE B CD2   
4501 C  CE1   . PHE B 134 ? 0.81430 0.50600 0.64280 -0.10480 -0.27740 0.07630  134 PHE B CE1   
4502 C  CE2   . PHE B 134 ? 0.76540 0.45680 0.58520 -0.10280 -0.28340 0.06840  134 PHE B CE2   
4503 C  CZ    . PHE B 134 ? 0.72830 0.43910 0.58000 -0.10070 -0.27530 0.07250  134 PHE B CZ    
4504 N  N     . GLU B 135 ? 0.92440 0.47160 0.48960 -0.13150 -0.26250 0.07380  135 GLU B N     
4505 C  CA    . GLU B 135 ? 1.09530 0.61590 0.60070 -0.13670 -0.24630 0.07150  135 GLU B CA    
4506 C  C     . GLU B 135 ? 1.12190 0.63690 0.61000 -0.13580 -0.24400 0.06560  135 GLU B C     
4507 O  O     . GLU B 135 ? 0.95020 0.49740 0.47700 -0.13320 -0.23750 0.06200  135 GLU B O     
4508 C  CB    . GLU B 135 ? 0.98550 0.52820 0.49390 -0.14120 -0.21400 0.06990  135 GLU B CB    
4509 C  CG    . GLU B 135 ? 1.21330 0.72760 0.66340 -0.14610 -0.19570 0.06880  135 GLU B CG    
4510 C  CD    . GLU B 135 ? 1.33640 0.85710 0.78430 -0.14980 -0.17760 0.07160  135 GLU B CD    
4511 O  OE1   . GLU B 135 ? 1.51750 1.07610 1.00290 -0.15060 -0.15820 0.06830  135 GLU B OE1   
4512 O  OE2   . GLU B 135 ? 1.42160 0.90880 0.83020 -0.15150 -0.18350 0.07740  135 GLU B OE2   
4513 N  N     . SER B 136 ? 1.02310 0.49500 0.45090 -0.13760 -0.24990 0.06500  136 SER B N     
4514 C  CA    . SER B 136 ? 1.07360 0.53220 0.47460 -0.13700 -0.24910 0.05900  136 SER B CA    
4515 C  C     . SER B 136 ? 1.04870 0.49750 0.40700 -0.14140 -0.21810 0.05460  136 SER B C     
4516 O  O     . SER B 136 ? 1.03960 0.49590 0.39470 -0.14090 -0.20710 0.04810  136 SER B O     
4517 C  CB    . SER B 136 ? 1.24360 0.65590 0.60530 -0.13470 -0.28220 0.06060  136 SER B CB    
4518 O  OG    . SER B 136 ? 1.33310 0.70150 0.63250 -0.13780 -0.28160 0.06420  136 SER B OG    
4519 N  N     . HIS B 137 ? 1.17370 0.60490 0.50000 -0.14540 -0.20440 0.05820  137 HIS B N     
4520 C  CA    . HIS B 137 ? 1.19640 0.61140 0.47790 -0.14940 -0.17550 0.05510  137 HIS B CA    
4521 C  C     . HIS B 137 ? 1.30320 0.67700 0.52820 -0.14870 -0.18230 0.05130  137 HIS B C     
4522 O  O     . HIS B 137 ? 1.28090 0.65210 0.48360 -0.15040 -0.15800 0.04560  137 HIS B O     
4523 C  CB    . HIS B 137 ? 1.10800 0.56820 0.42900 -0.15070 -0.14400 0.04930  137 HIS B CB    
4524 C  CG    . HIS B 137 ? 1.08600 0.58030 0.45100 -0.15200 -0.13380 0.05220  137 HIS B CG    
4525 N  ND1   . HIS B 137 ? 1.04520 0.52630 0.39030 -0.15540 -0.12440 0.05710  137 HIS B ND1   
4526 C  CD2   . HIS B 137 ? 1.10120 0.64060 0.52660 -0.15010 -0.13150 0.05090  137 HIS B CD2   
4527 C  CE1   . HIS B 137 ? 1.12150 0.63870 0.51370 -0.15570 -0.11750 0.05800  137 HIS B CE1   
4528 N  NE2   . HIS B 137 ? 0.91350 0.46560 0.35360 -0.15250 -0.12180 0.05420  137 HIS B NE2   
4529 N  N     . LEU B 138 ? 1.34420 0.68440 0.54580 -0.14590 -0.21630 0.05430  138 LEU B N     
4530 C  CA    . LEU B 138 ? 1.48880 0.78630 0.63600 -0.14450 -0.22970 0.05060  138 LEU B CA    
4531 C  C     . LEU B 138 ? 1.47140 0.72970 0.54850 -0.14830 -0.20580 0.05010  138 LEU B C     
4532 O  O     . LEU B 138 ? 1.64300 0.88600 0.68810 -0.14820 -0.19510 0.04360  138 LEU B O     
4533 C  CB    . LEU B 138 ? 1.57250 0.83640 0.70470 -0.14100 -0.27230 0.05500  138 LEU B CB    
4534 C  CG    . LEU B 138 ? 1.82920 1.04240 0.90120 -0.13900 -0.29360 0.05160  138 LEU B CG    
4535 C  CD1   . LEU B 138 ? 1.81220 1.04080 0.89360 -0.13770 -0.28620 0.04210  138 LEU B CD1   
4536 C  CD2   . LEU B 138 ? 1.87610 1.06500 0.95000 -0.13470 -0.33890 0.05550  138 LEU B CD2   
4537 N  N     . ASP B 139 ? 1.47640 0.71890 0.53110 -0.15130 -0.19640 0.05700  139 ASP B N     
4538 C  CA    . ASP B 139 ? 1.64610 0.85020 0.63520 -0.15510 -0.17150 0.05830  139 ASP B CA    
4539 C  C     . ASP B 139 ? 1.52320 0.75370 0.52360 -0.15800 -0.12940 0.05200  139 ASP B C     
4540 O  O     . ASP B 139 ? 1.64600 0.84490 0.59350 -0.16070 -0.10620 0.05170  139 ASP B O     
4541 C  CB    . ASP B 139 ? 1.71630 0.90180 0.68650 -0.15750 -0.17130 0.06820  139 ASP B CB    
4542 C  CG    . ASP B 139 ? 1.78690 1.02460 0.82250 -0.15930 -0.15600 0.07040  139 ASP B CG    
4543 O  OD1   . ASP B 139 ? 1.62010 0.90040 0.71900 -0.15680 -0.16790 0.06790  139 ASP B OD1   
4544 O  OD2   . ASP B 139 ? 1.90020 1.13500 0.92310 -0.16320 -0.13200 0.07480  139 ASP B OD2   
4545 N  N     . LYS B 140 ? 1.49220 0.77920 0.56160 -0.15720 -0.11960 0.04730  140 LYS B N     
4546 C  CA    . LYS B 140 ? 1.43670 0.75430 0.52760 -0.15910 -0.08270 0.04100  140 LYS B CA    
4547 C  C     . LYS B 140 ? 1.48660 0.81280 0.58170 -0.15630 -0.07920 0.03150  140 LYS B C     
4548 O  O     . LYS B 140 ? 1.39790 0.73930 0.49890 -0.15730 -0.04940 0.02550  140 LYS B O     
4549 C  CB    . LYS B 140 ? 1.34210 0.71500 0.50370 -0.15970 -0.07180 0.04180  140 LYS B CB    
4550 C  CG    . LYS B 140 ? 1.41080 0.77790 0.57310 -0.16190 -0.07790 0.05090  140 LYS B CG    
4551 C  CD    . LYS B 140 ? 1.38190 0.77950 0.57440 -0.16520 -0.04840 0.05150  140 LYS B CD    
4552 C  CE    . LYS B 140 ? 1.34350 0.72810 0.52810 -0.16720 -0.05610 0.06110  140 LYS B CE    
4553 N  NZ    . LYS B 140 ? 1.45080 0.85850 0.68000 -0.16440 -0.08350 0.06410  140 LYS B NZ    
4554 N  N     . LEU B 141 ? 1.37040 0.68630 0.46340 -0.15270 -0.11010 0.03010  141 LEU B N     
4555 C  CA    . LEU B 141 ? 1.52930 0.85280 0.62760 -0.14970 -0.11120 0.02130  141 LEU B CA    
4556 C  C     . LEU B 141 ? 1.50840 0.78730 0.53770 -0.15060 -0.09630 0.01620  141 LEU B C     
4557 O  O     . LEU B 141 ? 1.77360 1.00090 0.73930 -0.15170 -0.10500 0.01990  141 LEU B O     
4558 C  CB    . LEU B 141 ? 1.62500 0.94640 0.73890 -0.14580 -0.15000 0.02170  141 LEU B CB    
4559 C  CG    . LEU B 141 ? 1.57820 0.94080 0.76020 -0.14410 -0.16670 0.02650  141 LEU B CG    
4560 C  CD1   . LEU B 141 ? 1.61920 0.97330 0.81170 -0.14000 -0.20460 0.02650  141 LEU B CD1   
4561 C  CD2   . LEU B 141 ? 1.44910 0.86830 0.69390 -0.14370 -0.14400 0.02290  141 LEU B CD2   
4562 N  N     . ASP B 142 ? 1.77260 1.06990 0.81350 -0.14960 -0.07520 0.00730  142 ASP B N     
4563 C  CA    . ASP B 142 ? 1.95060 1.21660 0.93800 -0.15070 -0.04850 0.00150  142 ASP B CA    
4564 C  C     . ASP B 142 ? 2.22820 1.46460 1.17560 -0.14770 -0.05890 -0.00710 142 ASP B C     
4565 O  O     . ASP B 142 ? 2.21440 1.45490 1.15600 -0.14690 -0.03430 -0.01550 142 ASP B O     
4566 C  CB    . ASP B 142 ? 1.91630 1.22450 0.94650 -0.15180 -0.01080 -0.00300 142 ASP B CB    
4567 C  CG    . ASP B 142 ? 2.06430 1.42320 1.15960 -0.14830 -0.01360 -0.00910 142 ASP B CG    
4568 O  OD1   . ASP B 142 ? 2.29280 1.65260 1.39700 -0.14530 -0.04200 -0.01060 142 ASP B OD1   
4569 O  OD2   . ASP B 142 ? 1.87680 1.27400 1.01500 -0.14830 0.01170  -0.01220 142 ASP B OD2   
4570 N  N     . ASN B 143 ? 2.43680 1.64340 1.35810 -0.14560 -0.09590 -0.00550 143 ASN B N     
4571 C  CA    . ASN B 143 ? 2.39690 1.56600 1.27020 -0.14280 -0.11050 -0.01350 143 ASN B CA    
4572 C  C     . ASN B 143 ? 2.05720 1.25920 0.96800 -0.14000 -0.10470 -0.02430 143 ASN B C     
4573 O  O     . ASN B 143 ? 2.70430 1.87750 1.57310 -0.13830 -0.10390 -0.03300 143 ASN B O     
4574 C  CB    . ASN B 143 ? 2.28980 1.40150 1.07860 -0.14440 -0.09050 -0.01540 143 ASN B CB    
4575 C  CG    . ASN B 143 ? 2.30180 1.36500 1.03540 -0.14630 -0.10450 -0.00560 143 ASN B CG    
4576 O  OD1   . ASN B 143 ? 2.44150 1.50890 1.19530 -0.14580 -0.13420 0.00180  143 ASN B OD1   
4577 N  ND2   . ASN B 143 ? 2.30170 1.31650 0.96350 -0.14820 -0.08250 -0.00560 143 ASN B ND2   
4578 N  N     . GLU B 144 ? 1.92250 1.18310 0.91020 -0.13930 -0.10050 -0.02390 144 GLU B N     
4579 C  CA    . GLU B 144 ? 1.94490 1.23990 0.97360 -0.13640 -0.09540 -0.03320 144 GLU B CA    
4580 C  C     . GLU B 144 ? 1.88430 1.23470 0.99300 -0.13530 -0.10590 -0.02930 144 GLU B C     
4581 O  O     . GLU B 144 ? 1.63170 1.00220 0.77310 -0.13250 -0.12130 -0.03420 144 GLU B O     
4582 C  CB    . GLU B 144 ? 2.04420 1.34600 1.06540 -0.13660 -0.05570 -0.04090 144 GLU B CB    
4583 C  CG    . GLU B 144 ? 2.12700 1.45120 1.16940 -0.13940 -0.02350 -0.03590 144 GLU B CG    
4584 C  CD    . GLU B 144 ? 2.37960 1.76400 1.49740 -0.13790 -0.00900 -0.03790 144 GLU B CD    
4585 O  OE1   . GLU B 144 ? 2.08710 1.48640 1.22000 -0.13490 0.00200  -0.04730 144 GLU B OE1   
4586 O  OE2   . GLU B 144 ? 2.62270 2.03770 1.78320 -0.13940 -0.00900 -0.03040 144 GLU B OE2   
4587 N  N     . LYS B 145 ? 1.62330 0.99410 0.75980 -0.13740 -0.10000 -0.02010 145 LYS B N     
4588 C  CA    . LYS B 145 ? 1.69170 1.09460 0.88360 -0.13650 -0.12110 -0.01330 145 LYS B CA    
4589 C  C     . LYS B 145 ? 1.57610 0.94780 0.74670 -0.13510 -0.16080 -0.01040 145 LYS B C     
4590 O  O     . LYS B 145 ? 1.32310 0.71590 0.53520 -0.13250 -0.18310 -0.01090 145 LYS B O     
4591 C  CB    . LYS B 145 ? 1.66550 1.08410 0.87640 -0.13940 -0.10850 -0.00460 145 LYS B CB    
4592 C  CG    . LYS B 145 ? 1.72320 1.18240 0.97350 -0.14010 -0.07540 -0.00690 145 LYS B CG    
4593 C  CD    . LYS B 145 ? 1.85980 1.33010 1.12450 -0.14330 -0.06520 0.00080  145 LYS B CD    
4594 C  CE    . LYS B 145 ? 1.67430 1.18820 0.98550 -0.14350 -0.03690 -0.00190 145 LYS B CE    
4595 N  NZ    . LYS B 145 ? 1.83190 1.33680 1.11900 -0.14400 -0.00770 -0.00910 145 LYS B NZ    
4596 N  N     . LYS B 146 ? 1.51680 0.83680 0.62250 -0.13670 -0.16910 -0.00760 146 LYS B N     
4597 C  CA    . LYS B 146 ? 1.62090 0.90140 0.69450 -0.13490 -0.20770 -0.00610 146 LYS B CA    
4598 C  C     . LYS B 146 ? 1.61230 0.88950 0.68770 -0.13190 -0.22580 -0.01570 146 LYS B C     
4599 O  O     . LYS B 146 ? 1.67610 0.95580 0.77650 -0.12950 -0.25910 -0.01490 146 LYS B O     
4600 C  CB    . LYS B 146 ? 1.56720 0.78660 0.55820 -0.13670 -0.20800 -0.00350 146 LYS B CB    
4601 C  CG    . LYS B 146 ? 1.70180 0.91070 0.68580 -0.13900 -0.21070 0.00750  146 LYS B CG    
4602 C  CD    . LYS B 146 ? 1.83260 0.97920 0.73020 -0.14080 -0.20620 0.00960  146 LYS B CD    
4603 C  CE    . LYS B 146 ? 1.86720 0.99590 0.75270 -0.14240 -0.21740 0.02050  146 LYS B CE    
4604 N  NZ    . LYS B 146 ? 1.90910 1.02660 0.80740 -0.13900 -0.26290 0.02460  146 LYS B NZ    
4605 N  N     . ASP B 147 ? 1.60840 0.87960 0.65910 -0.13190 -0.20380 -0.02520 147 ASP B N     
4606 C  CA    . ASP B 147 ? 1.78920 1.05500 0.83700 -0.12950 -0.21750 -0.03620 147 ASP B CA    
4607 C  C     . ASP B 147 ? 1.46540 0.78620 0.59280 -0.12770 -0.22300 -0.03870 147 ASP B C     
4608 O  O     . ASP B 147 ? 1.48690 0.80630 0.62820 -0.12590 -0.24900 -0.04430 147 ASP B O     
4609 C  CB    . ASP B 147 ? 1.87730 1.12350 0.87970 -0.12970 -0.18900 -0.04640 147 ASP B CB    
4610 C  CG    . ASP B 147 ? 2.07900 1.26120 0.99280 -0.13080 -0.18720 -0.04620 147 ASP B CG    
4611 O  OD1   . ASP B 147 ? 2.00580 1.15480 0.88780 -0.13140 -0.21000 -0.03840 147 ASP B OD1   
4612 O  OD2   . ASP B 147 ? 1.90510 1.06810 0.77880 -0.13080 -0.16210 -0.05420 147 ASP B OD2   
4613 N  N     . LEU B 148 ? 1.58660 0.95410 0.76530 -0.12830 -0.19860 -0.03480 148 LEU B N     
4614 C  CA    . LEU B 148 ? 1.43650 0.85470 0.68880 -0.12650 -0.20200 -0.03540 148 LEU B CA    
4615 C  C     . LEU B 148 ? 1.43200 0.85820 0.71980 -0.12530 -0.23510 -0.02810 148 LEU B C     
4616 O  O     . LEU B 148 ? 1.52020 0.96540 0.84870 -0.12350 -0.25290 -0.03170 148 LEU B O     
4617 C  CB    . LEU B 148 ? 1.36300 0.82390 0.65520 -0.12700 -0.16910 -0.03250 148 LEU B CB    
4618 C  CG    . LEU B 148 ? 1.47710 0.94430 0.75890 -0.12660 -0.13810 -0.04180 148 LEU B CG    
4619 C  CD1   . LEU B 148 ? 1.29160 0.79340 0.60550 -0.12730 -0.10750 -0.03790 148 LEU B CD1   
4620 C  CD2   . LEU B 148 ? 1.42240 0.90600 0.73090 -0.12400 -0.14440 -0.05200 148 LEU B CD2   
4621 N  N     . ILE B 149 ? 1.39900 0.80940 0.67240 -0.12640 -0.24290 -0.01820 149 ILE B N     
4622 C  CA    . ILE B 149 ? 1.33850 0.74950 0.64010 -0.12470 -0.27570 -0.01120 149 ILE B CA    
4623 C  C     . ILE B 149 ? 1.45290 0.82950 0.73140 -0.12300 -0.31160 -0.01640 149 ILE B C     
4624 O  O     . ILE B 149 ? 1.41270 0.80580 0.73790 -0.12080 -0.33670 -0.01630 149 ILE B O     
4625 C  CB    . ILE B 149 ? 1.35610 0.74940 0.63810 -0.12620 -0.27730 -0.00070 149 ILE B CB    
4626 C  CG1   . ILE B 149 ? 1.21040 0.64550 0.53250 -0.12770 -0.24780 0.00450  149 ILE B CG1   
4627 C  CG2   . ILE B 149 ? 1.32160 0.70480 0.62320 -0.12380 -0.31560 0.00520  149 ILE B CG2   
4628 C  CD1   . ILE B 149 ? 1.24210 0.66260 0.54680 -0.13000 -0.24540 0.01360  149 ILE B CD1   
4629 N  N     . GLN B 150 ? 1.42790 0.75560 0.63470 -0.12390 -0.31390 -0.02120 150 GLN B N     
4630 C  CA    . GLN B 150 ? 1.53880 0.82810 0.71520 -0.12230 -0.34880 -0.02720 150 GLN B CA    
4631 C  C     . GLN B 150 ? 1.50830 0.82260 0.72390 -0.12130 -0.35420 -0.03780 150 GLN B C     
4632 O  O     . GLN B 150 ? 1.47120 0.77610 0.70150 -0.11980 -0.38810 -0.04120 150 GLN B O     
4633 C  CB    . GLN B 150 ? 1.66630 0.89630 0.75200 -0.12330 -0.34600 -0.03120 150 GLN B CB    
4634 C  CG    . GLN B 150 ? 1.71460 0.90240 0.75080 -0.12380 -0.35680 -0.02180 150 GLN B CG    
4635 C  CD    . GLN B 150 ? 1.79750 0.97080 0.85050 -0.12100 -0.40180 -0.01660 150 GLN B CD    
4636 O  OE1   . GLN B 150 ? 1.74060 0.91200 0.81390 -0.11870 -0.43200 -0.02250 150 GLN B OE1   
4637 N  NE2   . GLN B 150 ? 1.78880 0.95170 0.83590 -0.12130 -0.40680 -0.00610 150 GLN B NE2   
4638 N  N     . SER B 151 ? 1.55250 0.89800 0.78620 -0.12230 -0.32130 -0.04330 151 SER B N     
4639 C  CA    . SER B 151 ? 1.46870 0.84260 0.74510 -0.12190 -0.32180 -0.05320 151 SER B CA    
4640 C  C     . SER B 151 ? 1.35930 0.77700 0.71610 -0.12070 -0.33570 -0.04830 151 SER B C     
4641 O  O     . SER B 151 ? 1.26160 0.68640 0.65050 -0.12030 -0.35710 -0.05450 151 SER B O     
4642 C  CB    . SER B 151 ? 1.43640 0.83300 0.71450 -0.12260 -0.28220 -0.05910 151 SER B CB    
4643 O  OG    . SER B 151 ? 1.55010 0.95480 0.84430 -0.12240 -0.28480 -0.07160 151 SER B OG    
4644 N  N     . ASP B 152 ? 1.33270 0.77860 0.72180 -0.12030 -0.32270 -0.03760 152 ASP B N     
4645 C  CA    . ASP B 152 ? 1.30890 0.79340 0.77070 -0.11860 -0.33380 -0.03150 152 ASP B CA    
4646 C  C     . ASP B 152 ? 1.31510 0.77860 0.78630 -0.11690 -0.37510 -0.02870 152 ASP B C     
4647 O  O     . ASP B 152 ? 1.32820 0.81520 0.85730 -0.11550 -0.39170 -0.03000 152 ASP B O     
4648 C  CB    . ASP B 152 ? 1.42650 0.93730 0.90990 -0.11830 -0.31240 -0.02080 152 ASP B CB    
4649 C  CG    . ASP B 152 ? 1.50710 1.05410 1.01130 -0.11890 -0.27580 -0.02320 152 ASP B CG    
4650 O  OD1   . ASP B 152 ? 1.54760 1.10180 1.05450 -0.11930 -0.26680 -0.03300 152 ASP B OD1   
4651 O  OD2   . ASP B 152 ? 1.32600 0.89320 0.84480 -0.11890 -0.25700 -0.01570 152 ASP B OD2   
4652 N  N     . ILE B 153 ? 1.22280 0.64060 0.63750 -0.11680 -0.39130 -0.02500 153 ILE B N     
4653 C  CA    . ILE B 153 ? 1.28030 0.67010 0.69510 -0.11460 -0.43330 -0.02300 153 ILE B CA    
4654 C  C     . ILE B 153 ? 1.30790 0.68550 0.72710 -0.11440 -0.45800 -0.03420 153 ILE B C     
4655 O  O     . ILE B 153 ? 1.23610 0.62260 0.70430 -0.11250 -0.48700 -0.03440 153 ILE B O     
4656 C  CB    . ILE B 153 ? 1.34410 0.68130 0.68750 -0.11460 -0.44440 -0.01760 153 ILE B CB    
4657 C  CG1   . ILE B 153 ? 1.28220 0.63510 0.63760 -0.11500 -0.42700 -0.00600 153 ILE B CG1   
4658 C  CG2   . ILE B 153 ? 1.38700 0.68750 0.72190 -0.11190 -0.49150 -0.01780 153 ILE B CG2   
4659 C  CD1   . ILE B 153 ? 1.32320 0.62700 0.60670 -0.11620 -0.42920 -0.00070 153 ILE B CD1   
4660 N  N     . ALA B 154 ? 1.42330 0.78120 0.79440 -0.11650 -0.44560 -0.04420 154 ALA B N     
4661 C  CA    . ALA B 154 ? 1.52810 0.87390 0.90010 -0.11710 -0.46570 -0.05660 154 ALA B CA    
4662 C  C     . ALA B 154 ? 1.39780 0.79450 0.85410 -0.11770 -0.46320 -0.05990 154 ALA B C     
4663 O  O     . ALA B 154 ? 1.43860 0.83370 0.92740 -0.11760 -0.49260 -0.06510 154 ALA B O     
4664 C  CB    . ALA B 154 ? 1.53100 0.85030 0.83840 -0.11900 -0.44610 -0.06700 154 ALA B CB    
4665 N  N     . ALA B 155 ? 1.20990 0.65030 0.70130 -0.11850 -0.42810 -0.05690 155 ALA B N     
4666 C  CA    . ALA B 155 ? 1.14750 0.63610 0.71680 -0.11910 -0.42100 -0.05870 155 ALA B CA    
4667 C  C     . ALA B 155 ? 1.14330 0.65060 0.77460 -0.11670 -0.44430 -0.05050 155 ALA B C     
4668 O  O     . ALA B 155 ? 1.09850 0.62440 0.78610 -0.11720 -0.45870 -0.05440 155 ALA B O     
4669 C  CB    . ALA B 155 ? 1.19020 0.71580 0.77590 -0.11970 -0.37960 -0.05640 155 ALA B CB    
4670 N  N     . LEU B 156 ? 1.07380 0.57510 0.69610 -0.11410 -0.44700 -0.03930 156 LEU B N     
4671 C  CA    . LEU B 156 ? 1.09060 0.60540 0.76810 -0.11090 -0.46890 -0.03120 156 LEU B CA    
4672 C  C     . LEU B 156 ? 1.10610 0.59410 0.79280 -0.10990 -0.51240 -0.03630 156 LEU B C     
4673 O  O     . LEU B 156 ? 1.08290 0.59470 0.83900 -0.10870 -0.52730 -0.03650 156 LEU B O     
4674 C  CB    . LEU B 156 ? 1.08020 0.58300 0.73350 -0.10880 -0.46650 -0.01980 156 LEU B CB    
4675 C  CG    . LEU B 156 ? 1.04660 0.56660 0.75920 -0.10490 -0.48350 -0.01110 156 LEU B CG    
4676 C  CD1   . LEU B 156 ? 1.02430 0.59920 0.81040 -0.10400 -0.46000 -0.00880 156 LEU B CD1   
4677 C  CD2   . LEU B 156 ? 1.04220 0.54060 0.71930 -0.10360 -0.48410 -0.00140 156 LEU B CD2   
4678 N  N     . HIS B 157 ? 1.30390 0.74090 0.91990 -0.11030 -0.53200 -0.04050 157 HIS B N     
4679 C  CA    . HIS B 157 ? 1.37770 0.78150 0.99010 -0.10930 -0.57570 -0.04680 157 HIS B CA    
4680 C  C     . HIS B 157 ? 1.41340 0.83490 1.06660 -0.11210 -0.58060 -0.05840 157 HIS B C     
4681 O  O     . HIS B 157 ? 1.37810 0.80510 1.08530 -0.11110 -0.61010 -0.06070 157 HIS B O     
4682 C  CB    . HIS B 157 ? 1.50130 0.84390 1.01820 -0.10930 -0.59030 -0.05010 157 HIS B CB    
4683 C  CG    . HIS B 157 ? 1.52420 0.83730 1.00140 -0.10670 -0.59890 -0.03950 157 HIS B CG    
4684 N  ND1   . HIS B 157 ? 1.77030 1.02320 1.17380 -0.10540 -0.62560 -0.04080 157 HIS B ND1   
4685 C  CD2   . HIS B 157 ? 1.52250 0.85580 1.02120 -0.10520 -0.58440 -0.02790 157 HIS B CD2   
4686 C  CE1   . HIS B 157 ? 1.65790 0.89510 1.03990 -0.10360 -0.62690 -0.03020 157 HIS B CE1   
4687 N  NE2   . HIS B 157 ? 1.53080 0.81670 0.97100 -0.10360 -0.60240 -0.02250 157 HIS B NE2   
4688 N  N     . HIS B 158 ? 1.49740 0.92700 1.12650 -0.11580 -0.55120 -0.06590 158 HIS B N     
4689 C  CA    . HIS B 158 ? 1.41660 0.85870 1.07460 -0.11960 -0.55180 -0.07810 158 HIS B CA    
4690 C  C     . HIS B 158 ? 1.31040 0.80140 1.06540 -0.12030 -0.54960 -0.07610 158 HIS B C     
4691 O  O     . HIS B 158 ? 1.28950 0.78100 1.08440 -0.12210 -0.57300 -0.08320 158 HIS B O     
4692 C  CB    . HIS B 158 ? 1.44640 0.89230 1.06470 -0.12270 -0.51480 -0.08510 158 HIS B CB    
4693 C  CG    . HIS B 158 ? 1.65530 1.10380 1.28900 -0.12700 -0.51610 -0.09920 158 HIS B CG    
4694 N  ND1   . HIS B 158 ? 1.67300 1.07810 1.26120 -0.12830 -0.54170 -0.11100 158 HIS B ND1   
4695 C  CD2   . HIS B 158 ? 1.57840 1.06510 1.26540 -0.13040 -0.49430 -0.10370 158 HIS B CD2   
4696 C  CE1   . HIS B 158 ? 1.64030 1.05800 1.25600 -0.13270 -0.53590 -0.12250 158 HIS B CE1   
4697 N  NE2   . HIS B 158 ? 1.75600 1.22270 1.43190 -0.13420 -0.50710 -0.11800 158 HIS B NE2   
4698 N  N     . PHE B 159 ? 1.18980 0.72010 0.98180 -0.11890 -0.52130 -0.06640 159 PHE B N     
4699 C  CA    . PHE B 159 ? 1.08360 0.66180 0.96100 -0.11970 -0.50850 -0.06440 159 PHE B CA    
4700 C  C     . PHE B 159 ? 1.09690 0.69370 1.03950 -0.11540 -0.52530 -0.05490 159 PHE B C     
4701 O  O     . PHE B 159 ? 1.12100 0.75160 1.13700 -0.11600 -0.52010 -0.05440 159 PHE B O     
4702 C  CB    . PHE B 159 ? 1.00230 0.61350 0.88180 -0.12080 -0.46350 -0.06130 159 PHE B CB    
4703 C  CG    . PHE B 159 ? 0.97730 0.58250 0.82150 -0.12520 -0.44350 -0.07220 159 PHE B CG    
4704 C  CD1   . PHE B 159 ? 0.97740 0.58790 0.85290 -0.12960 -0.44830 -0.08240 159 PHE B CD1   
4705 C  CD2   . PHE B 159 ? 1.00010 0.59410 0.78280 -0.12490 -0.41890 -0.07250 159 PHE B CD2   
4706 C  CE1   . PHE B 159 ? 0.95260 0.55580 0.79680 -0.13340 -0.42980 -0.09310 159 PHE B CE1   
4707 C  CE2   . PHE B 159 ? 1.00990 0.59820 0.76380 -0.12800 -0.39990 -0.08310 159 PHE B CE2   
4708 C  CZ    . PHE B 159 ? 0.97150 0.56370 0.75530 -0.13220 -0.40570 -0.09370 159 PHE B CZ    
4709 N  N     . TYR B 160 ? 1.19590 0.76900 1.11240 -0.11110 -0.54430 -0.04750 160 TYR B N     
4710 C  CA    . TYR B 160 ? 1.20020 0.78860 1.17370 -0.10610 -0.55750 -0.03800 160 TYR B CA    
4711 C  C     . TYR B 160 ? 1.28340 0.83190 1.24510 -0.10280 -0.60400 -0.03810 160 TYR B C     
4712 O  O     . TYR B 160 ? 1.27330 0.82430 1.26390 -0.09810 -0.61600 -0.02980 160 TYR B O     
4713 C  CB    . TYR B 160 ? 1.13940 0.74310 1.09940 -0.10350 -0.52970 -0.02730 160 TYR B CB    
4714 C  CG    . TYR B 160 ? 1.02950 0.67280 1.00640 -0.10570 -0.48650 -0.02660 160 TYR B CG    
4715 C  CD1   . TYR B 160 ? 0.95680 0.59380 0.87430 -0.10860 -0.46050 -0.02930 160 TYR B CD1   
4716 C  CD2   . TYR B 160 ? 0.95630 0.64170 1.00880 -0.10440 -0.47160 -0.02340 160 TYR B CD2   
4717 C  CE1   . TYR B 160 ? 0.91910 0.59040 0.85240 -0.11020 -0.42340 -0.02910 160 TYR B CE1   
4718 C  CE2   . TYR B 160 ? 0.89740 0.61550 0.96180 -0.10610 -0.43350 -0.02280 160 TYR B CE2   
4719 C  CZ    . TYR B 160 ? 0.83920 0.55010 0.84410 -0.10900 -0.41060 -0.02580 160 TYR B CZ    
4720 O  OH    . TYR B 160 ? 0.90760 0.64870 0.92480 -0.11030 -0.37550 -0.02570 160 TYR B OH    
4721 N  N     . SER B 161 ? 1.42180 0.93400 1.34540 -0.10500 -0.63060 -0.04770 161 SER B N     
4722 C  CA    . SER B 161 ? 1.42830 0.89720 1.33440 -0.10170 -0.67800 -0.04890 161 SER B CA    
4723 C  C     . SER B 161 ? 1.37660 0.86280 1.37180 -0.09800 -0.70560 -0.04670 161 SER B C     
4724 O  O     . SER B 161 ? 1.41250 0.87470 1.40750 -0.09330 -0.73570 -0.04210 161 SER B O     
4725 C  CB    . SER B 161 ? 1.47760 0.90730 1.33220 -0.10490 -0.70040 -0.06140 161 SER B CB    
4726 O  OG    . SER B 161 ? 1.60760 0.99970 1.36440 -0.10580 -0.69020 -0.06200 161 SER B OG    
4727 N  N     . LYS B 162 ? 1.28240 0.80880 1.35490 -0.10010 -0.69470 -0.05020 162 LYS B N     
4728 C  CA    . LYS B 162 ? 1.28150 0.83350 1.45020 -0.09670 -0.71010 -0.04750 162 LYS B CA    
4729 C  C     . LYS B 162 ? 1.51200 1.10120 1.71630 -0.09360 -0.67700 -0.03640 162 LYS B C     
4730 O  O     . LYS B 162 ? 1.45250 1.06330 1.63450 -0.09610 -0.63720 -0.03390 162 LYS B O     
4731 C  CB    . LYS B 162 ? 1.30620 0.88370 1.54050 -0.10110 -0.70900 -0.05590 162 LYS B CB    
4732 C  CG    . LYS B 162 ? 1.49660 1.03860 1.69560 -0.10490 -0.73940 -0.06840 162 LYS B CG    
4733 C  CD    . LYS B 162 ? 1.41740 0.98090 1.69760 -0.10860 -0.74940 -0.07630 162 LYS B CD    
4734 C  CE    . LYS B 162 ? 1.61760 1.14150 1.86500 -0.11180 -0.78680 -0.08920 162 LYS B CE    
4735 N  NZ    . LYS B 162 ? 1.80480 1.28430 2.02610 -0.10630 -0.83590 -0.08960 162 LYS B NZ    
4736 N  N     . HIS B 163 ? 1.74120 1.33520 1.99920 -0.08800 -0.69490 -0.03050 163 HIS B N     
4737 C  CA    . HIS B 163 ? 1.75830 1.38460 2.05770 -0.08410 -0.66870 -0.02050 163 HIS B CA    
4738 C  C     . HIS B 163 ? 1.59600 1.20000 1.83340 -0.08140 -0.66610 -0.01230 163 HIS B C     
4739 O  O     . HIS B 163 ? 1.93290 1.54870 2.20580 -0.07690 -0.66340 -0.00510 163 HIS B O     
4740 C  CB    . HIS B 163 ? 1.61820 1.29050 1.94590 -0.08690 -0.62060 -0.01900 163 HIS B CB    
4741 C  CG    . HIS B 163 ? 1.87050 1.56630 2.25980 -0.09040 -0.61730 -0.02610 163 HIS B CG    
4742 N  ND1   . HIS B 163 ? 2.05280 1.74280 2.40960 -0.09680 -0.61180 -0.03450 163 HIS B ND1   
4743 C  CD2   . HIS B 163 ? 1.92650 1.65060 2.40890 -0.08890 -0.61710 -0.02620 163 HIS B CD2   
4744 C  CE1   . HIS B 163 ? 1.93190 1.64540 2.35840 -0.09950 -0.60910 -0.03920 163 HIS B CE1   
4745 N  NE2   . HIS B 163 ? 2.06660 1.80100 2.57030 -0.09470 -0.61180 -0.03400 163 HIS B NE2   
4746 N  N     . LEU B 164 ? 1.35540 0.92650 1.50110 -0.08440 -0.66540 -0.01390 164 LEU B N     
4747 C  CA    . LEU B 164 ? 1.41450 0.96580 1.49470 -0.08350 -0.65480 -0.00640 164 LEU B CA    
4748 C  C     . LEU B 164 ? 1.57910 1.07270 1.59450 -0.08240 -0.69380 -0.00750 164 LEU B C     
4749 O  O     . LEU B 164 ? 1.83820 1.30310 1.81780 -0.08460 -0.71460 -0.01560 164 LEU B O     
4750 C  CB    . LEU B 164 ? 1.26810 0.83070 1.29500 -0.08820 -0.61400 -0.00690 164 LEU B CB    
4751 C  CG    . LEU B 164 ? 1.26890 0.84250 1.26920 -0.08770 -0.58250 0.00200  164 LEU B CG    
4752 C  CD1   . LEU B 164 ? 1.07690 0.67470 1.05400 -0.09190 -0.54120 -0.00030 164 LEU B CD1   
4753 C  CD2   . LEU B 164 ? 1.52060 1.04680 1.44660 -0.08730 -0.59900 0.00600  164 LEU B CD2   
4754 N  N     . GLU B 165 ? 1.82770 1.30310 1.82800 -0.07910 -0.70400 0.00030  165 GLU B N     
4755 C  CA    . GLU B 165 ? 1.70190 1.11970 1.63040 -0.07810 -0.73620 0.00090  165 GLU B CA    
4756 C  C     . GLU B 165 ? 1.49790 0.90140 1.34980 -0.08070 -0.70750 0.00730  165 GLU B C     
4757 O  O     . GLU B 165 ? 1.53000 0.95610 1.40150 -0.07980 -0.68550 0.01500  165 GLU B O     
4758 C  CB    . GLU B 165 ? 1.79840 1.20200 1.77080 -0.07250 -0.77400 0.00430  165 GLU B CB    
4759 C  CG    . GLU B 165 ? 2.07250 1.41310 1.98060 -0.07100 -0.81810 0.00230  165 GLU B CG    
4760 C  CD    . GLU B 165 ? 2.07360 1.40000 2.02490 -0.06530 -0.85540 0.00570  165 GLU B CD    
4761 O  OE1   . GLU B 165 ? 2.04470 1.39130 2.02530 -0.06360 -0.83980 0.01330  165 GLU B OE1   
4762 O  OE2   . GLU B 165 ? 1.82280 1.11670 1.77860 -0.06250 -0.90120 0.00020  165 GLU B OE2   
4763 N  N     . PHE B 166 ? 1.33020 0.69550 1.09580 -0.08410 -0.70720 0.00350  166 PHE B N     
4764 C  CA    . PHE B 166 ? 1.32740 0.67890 1.01930 -0.08740 -0.67630 0.00820  166 PHE B CA    
4765 C  C     . PHE B 166 ? 1.40790 0.71110 1.04430 -0.08590 -0.69750 0.01440  166 PHE B C     
4766 O  O     . PHE B 166 ? 1.47780 0.73780 1.09030 -0.08340 -0.73840 0.01170  166 PHE B O     
4767 C  CB    . PHE B 166 ? 1.37490 0.70780 0.99920 -0.09180 -0.66110 0.00070  166 PHE B CB    
4768 C  CG    . PHE B 166 ? 1.43220 0.79390 1.09810 -0.09340 -0.65660 -0.00860 166 PHE B CG    
4769 C  CD1   . PHE B 166 ? 1.55350 0.97290 1.29340 -0.09380 -0.63010 -0.00780 166 PHE B CD1   
4770 C  CD2   . PHE B 166 ? 1.51860 0.84710 1.14630 -0.09460 -0.67880 -0.01850 166 PHE B CD2   
4771 C  CE1   . PHE B 166 ? 1.64640 1.09020 1.42330 -0.09580 -0.62570 -0.01650 166 PHE B CE1   
4772 C  CE2   . PHE B 166 ? 1.41800 0.77170 1.08380 -0.09680 -0.67510 -0.02780 166 PHE B CE2   
4773 C  CZ    . PHE B 166 ? 1.43220 0.84370 1.17390 -0.09760 -0.64860 -0.02660 166 PHE B CZ    
4774 N  N     . PRO B 167 ? 1.67680 0.98360 1.28940 -0.08740 -0.67150 0.02250  167 PRO B N     
4775 C  CA    . PRO B 167 ? 1.75620 1.01120 1.29410 -0.08790 -0.68360 0.02750  167 PRO B CA    
4776 C  C     . PRO B 167 ? 1.78120 0.99100 1.22470 -0.09120 -0.67990 0.02250  167 PRO B C     
4777 O  O     . PRO B 167 ? 1.58360 0.80600 1.02590 -0.09310 -0.66800 0.01500  167 PRO B O     
4778 C  CB    . PRO B 167 ? 1.73630 1.01610 1.27860 -0.09010 -0.64810 0.03580  167 PRO B CB    
4779 C  CG    . PRO B 167 ? 1.70190 1.04520 1.33610 -0.08860 -0.62870 0.03620  167 PRO B CG    
4780 C  CD    . PRO B 167 ? 1.69980 1.05910 1.35760 -0.08870 -0.63120 0.02730  167 PRO B CD    
4781 N  N     . ASP B 168 ? 2.07970 1.23720 1.44620 -0.09180 -0.68910 0.02640  168 ASP B N     
4782 C  CA    . ASP B 168 ? 2.19180 1.30190 1.46270 -0.09460 -0.68230 0.02240  168 ASP B CA    
4783 C  C     . ASP B 168 ? 2.09820 1.23630 1.35190 -0.09990 -0.63020 0.02140  168 ASP B C     
4784 O  O     . ASP B 168 ? 2.06810 1.25660 1.37530 -0.10130 -0.60120 0.02530  168 ASP B O     
4785 C  CB    . ASP B 168 ? 2.26060 1.30860 1.45390 -0.09390 -0.70090 0.02790  168 ASP B CB    
4786 C  CG    . ASP B 168 ? 2.18390 1.24420 1.37830 -0.09600 -0.67660 0.03790  168 ASP B CG    
4787 O  OD1   . ASP B 168 ? 2.07700 1.19360 1.33950 -0.09710 -0.65170 0.04080  168 ASP B OD1   
4788 O  OD2   . ASP B 168 ? 2.16890 1.18020 1.29390 -0.09650 -0.68340 0.04270  168 ASP B OD2   
4789 N  N     . ASN B 169 ? 1.82720 0.93120 1.00650 -0.10240 -0.61900 0.01570  169 ASN B N     
4790 C  CA    . ASN B 169 ? 1.75600 0.88410 0.91990 -0.10690 -0.57190 0.01290  169 ASN B CA    
4791 C  C     . ASN B 169 ? 1.78880 0.93400 0.94870 -0.11010 -0.53620 0.02140  169 ASN B C     
4792 O  O     . ASN B 169 ? 1.60950 0.80250 0.80800 -0.11250 -0.50100 0.02120  169 ASN B O     
4793 C  CB    . ASN B 169 ? 1.70810 0.78890 0.78760 -0.10840 -0.56850 0.00500  169 ASN B CB    
4794 C  CG    . ASN B 169 ? 1.66480 0.77340 0.73820 -0.11230 -0.52250 -0.00010 169 ASN B CG    
4795 O  OD1   . ASN B 169 ? 1.63090 0.73850 0.67310 -0.11550 -0.48850 0.00410  169 ASN B OD1   
4796 N  ND2   . ASN B 169 ? 1.61260 0.74680 0.71890 -0.11210 -0.52140 -0.00940 169 ASN B ND2   
4797 N  N     . ASP B 170 ? 2.03630 1.14110 1.14950 -0.11010 -0.54690 0.02850  170 ASP B N     
4798 C  CA    . ASP B 170 ? 1.92100 1.03580 1.02600 -0.11350 -0.51680 0.03650  170 ASP B CA    
4799 C  C     . ASP B 170 ? 1.73180 0.90780 0.92530 -0.11310 -0.50550 0.04090  170 ASP B C     
4800 O  O     . ASP B 170 ? 1.63980 0.84790 0.84770 -0.11650 -0.46840 0.04320  170 ASP B O     
4801 C  CB    . ASP B 170 ? 2.08410 1.14400 1.13060 -0.11280 -0.53780 0.04340  170 ASP B CB    
4802 C  CG    . ASP B 170 ? 2.22860 1.22810 1.17340 -0.11480 -0.53060 0.04130  170 ASP B CG    
4803 O  OD1   . ASP B 170 ? 2.37680 1.37710 1.29740 -0.11670 -0.50920 0.03400  170 ASP B OD1   
4804 O  OD2   . ASP B 170 ? 2.58960 1.53920 1.47720 -0.11420 -0.54610 0.04700  170 ASP B OD2   
4805 N  N     . SER B 171 ? 1.64010 0.83090 0.89320 -0.10850 -0.53790 0.04180  171 SER B N     
4806 C  CA    . SER B 171 ? 1.60920 0.85450 0.94730 -0.10710 -0.53030 0.04570  171 SER B CA    
4807 C  C     . SER B 171 ? 1.49410 0.79370 0.88160 -0.10820 -0.50000 0.04100  171 SER B C     
4808 O  O     . SER B 171 ? 1.42540 0.76670 0.85510 -0.10930 -0.47390 0.04460  171 SER B O     
4809 C  CB    . SER B 171 ? 1.61870 0.86410 1.00930 -0.10140 -0.57240 0.04680  171 SER B CB    
4810 O  OG    . SER B 171 ? 1.85350 1.05630 1.21000 -0.09990 -0.59830 0.05240  171 SER B OG    
4811 N  N     . LEU B 172 ? 1.47570 0.77260 0.85630 -0.10780 -0.50500 0.03280  172 LEU B N     
4812 C  CA    . LEU B 172 ? 1.41210 0.75520 0.83230 -0.10890 -0.47830 0.02730  172 LEU B CA    
4813 C  C     . LEU B 172 ? 1.36440 0.71730 0.75110 -0.11350 -0.43490 0.02690  172 LEU B C     
4814 O  O     . LEU B 172 ? 1.28510 0.68440 0.71620 -0.11420 -0.40760 0.02680  172 LEU B O     
4815 C  CB    . LEU B 172 ? 1.40500 0.73790 0.82070 -0.10780 -0.49590 0.01760  172 LEU B CB    
4816 C  CG    . LEU B 172 ? 1.47430 0.82470 0.95750 -0.10360 -0.52800 0.01540  172 LEU B CG    
4817 C  CD1   . LEU B 172 ? 1.28450 0.69650 0.85090 -0.10250 -0.50780 0.01740  172 LEU B CD1   
4818 C  CD2   . LEU B 172 ? 1.67150 0.98980 1.15440 -0.10010 -0.56740 0.02030  172 LEU B CD2   
4819 N  N     . VAL B 173 ? 1.32240 0.63040 0.63140 -0.11630 -0.42880 0.02660  173 VAL B N     
4820 C  CA    . VAL B 173 ? 1.27930 0.59200 0.55510 -0.12070 -0.38810 0.02630  173 VAL B CA    
4821 C  C     . VAL B 173 ? 1.27050 0.61590 0.58370 -0.12220 -0.36820 0.03400  173 VAL B C     
4822 O  O     . VAL B 173 ? 1.18020 0.56390 0.52030 -0.12400 -0.33610 0.03270  173 VAL B O     
4823 C  CB    . VAL B 173 ? 1.35890 0.61250 0.54420 -0.12310 -0.38680 0.02580  173 VAL B CB    
4824 C  CG1   . VAL B 173 ? 1.33440 0.59440 0.49320 -0.12770 -0.34390 0.02670  173 VAL B CG1   
4825 C  CG2   . VAL B 173 ? 1.43800 0.65990 0.58220 -0.12190 -0.40160 0.01670  173 VAL B CG2   
4826 N  N     . VAL B 174 ? 1.44520 0.77460 0.76070 -0.12100 -0.38900 0.04130  174 VAL B N     
4827 C  CA    . VAL B 174 ? 1.31810 0.67340 0.66670 -0.12220 -0.37500 0.04840  174 VAL B CA    
4828 C  C     . VAL B 174 ? 1.24710 0.66100 0.67700 -0.11980 -0.36550 0.04810  174 VAL B C     
4829 O  O     . VAL B 174 ? 1.11550 0.56180 0.56740 -0.12190 -0.33610 0.04950  174 VAL B O     
4830 C  CB    . VAL B 174 ? 1.38450 0.70940 0.72320 -0.12040 -0.40500 0.05550  174 VAL B CB    
4831 C  CG1   . VAL B 174 ? 1.36170 0.71840 0.74660 -0.12080 -0.39450 0.06180  174 VAL B CG1   
4832 C  CG2   . VAL B 174 ? 1.48030 0.74780 0.73370 -0.12320 -0.40760 0.05720  174 VAL B CG2   
4833 N  N     . LEU B 175 ? 1.29180 0.71740 0.76510 -0.11520 -0.39050 0.04610  175 LEU B N     
4834 C  CA    . LEU B 175 ? 1.21280 0.69040 0.76300 -0.11200 -0.38370 0.04600  175 LEU B CA    
4835 C  C     . LEU B 175 ? 1.22890 0.74070 0.79010 -0.11380 -0.35000 0.04080  175 LEU B C     
4836 O  O     . LEU B 175 ? 0.99510 0.54550 0.59630 -0.11350 -0.32830 0.04300  175 LEU B O     
4837 C  CB    . LEU B 175 ? 1.21650 0.69610 0.80760 -0.10710 -0.41650 0.04340  175 LEU B CB    
4838 C  CG    . LEU B 175 ? 1.18740 0.71760 0.86060 -0.10320 -0.41160 0.04370  175 LEU B CG    
4839 C  CD1   . LEU B 175 ? 1.11850 0.66750 0.82600 -0.10170 -0.40480 0.05120  175 LEU B CD1   
4840 C  CD2   . LEU B 175 ? 1.23220 0.76050 0.94420 -0.09900 -0.44430 0.04030  175 LEU B CD2   
4841 N  N     . PHE B 176 ? 1.13020 0.62610 0.65530 -0.11530 -0.34700 0.03360  176 PHE B N     
4842 C  CA    . PHE B 176 ? 1.14400 0.66660 0.67300 -0.11700 -0.31620 0.02760  176 PHE B CA    
4843 C  C     . PHE B 176 ? 1.00510 0.53610 0.51600 -0.12080 -0.28310 0.03020  176 PHE B C     
4844 O  O     . PHE B 176 ? 1.02580 0.59460 0.56940 -0.12070 -0.25860 0.02880  176 PHE B O     
4845 C  CB    . PHE B 176 ? 1.13970 0.63570 0.62490 -0.11810 -0.32030 0.01880  176 PHE B CB    
4846 C  CG    . PHE B 176 ? 1.13030 0.64070 0.65310 -0.11530 -0.33850 0.01260  176 PHE B CG    
4847 C  CD1   . PHE B 176 ? 1.08210 0.63720 0.65570 -0.11420 -0.32110 0.00900  176 PHE B CD1   
4848 C  CD2   . PHE B 176 ? 1.19040 0.66860 0.69810 -0.11380 -0.37340 0.00990  176 PHE B CD2   
4849 C  CE1   . PHE B 176 ? 1.10040 0.66870 0.71030 -0.11240 -0.33630 0.00290  176 PHE B CE1   
4850 C  CE2   . PHE B 176 ? 1.21710 0.70940 0.76360 -0.11180 -0.39000 0.00350  176 PHE B CE2   
4851 C  CZ    . PHE B 176 ? 1.05000 0.58800 0.64850 -0.11150 -0.37050 0.00000  176 PHE B CZ    
4852 N  N     . ALA B 177 ? 1.07020 0.56470 0.52900 -0.12390 -0.28330 0.03360  177 ALA B N     
4853 C  CA    . ALA B 177 ? 1.02960 0.52860 0.47150 -0.12810 -0.25410 0.03600  177 ALA B CA    
4854 C  C     . ALA B 177 ? 0.99340 0.52760 0.48740 -0.12740 -0.24760 0.04200  177 ALA B C     
4855 O  O     . ALA B 177 ? 0.93710 0.49850 0.44700 -0.12940 -0.22000 0.04140  177 ALA B O     
4856 C  CB    . ALA B 177 ? 1.10270 0.55210 0.47870 -0.13130 -0.25890 0.03880  177 ALA B CB    
4857 N  N     . GLN B 178 ? 0.94110 0.47390 0.46250 -0.12420 -0.27400 0.04730  178 GLN B N     
4858 C  CA    . GLN B 178 ? 0.84570 0.40990 0.41830 -0.12250 -0.27100 0.05260  178 GLN B CA    
4859 C  C     . GLN B 178 ? 0.84760 0.45950 0.47460 -0.11940 -0.25530 0.04990  178 GLN B C     
4860 O  O     . GLN B 178 ? 0.76430 0.40450 0.41740 -0.11980 -0.23570 0.05180  178 GLN B O     
4861 C  CB    . GLN B 178 ? 0.85720 0.40860 0.45090 -0.11870 -0.30420 0.05770  178 GLN B CB    
4862 C  CG    . GLN B 178 ? 0.92960 0.43820 0.47660 -0.12120 -0.31870 0.06210  178 GLN B CG    
4863 C  CD    . GLN B 178 ? 0.99130 0.48220 0.55620 -0.11670 -0.35610 0.06570  178 GLN B CD    
4864 O  OE1   . GLN B 178 ? 1.02410 0.51610 0.61150 -0.11260 -0.37660 0.06280  178 GLN B OE1   
4865 N  NE2   . GLN B 178 ? 0.98940 0.46410 0.54670 -0.11730 -0.36590 0.07140  178 GLN B NE2   
4866 N  N     . VAL B 179 ? 0.88540 0.50400 0.52720 -0.11630 -0.26480 0.04500  179 VAL B N     
4867 C  CA    . VAL B 179 ? 0.84070 0.50090 0.52970 -0.11300 -0.25140 0.04150  179 VAL B CA    
4868 C  C     . VAL B 179 ? 0.89490 0.57150 0.57090 -0.11600 -0.21880 0.03740  179 VAL B C     
4869 O  O     . VAL B 179 ? 0.77640 0.48740 0.48800 -0.11420 -0.20150 0.03800  179 VAL B O     
4870 C  CB    . VAL B 179 ? 0.81480 0.47440 0.51840 -0.11020 -0.26960 0.03590  179 VAL B CB    
4871 C  CG1   . VAL B 179 ? 0.77620 0.47470 0.51910 -0.10800 -0.25210 0.03080  179 VAL B CG1   
4872 C  CG2   . VAL B 179 ? 0.92590 0.57920 0.66150 -0.10630 -0.30070 0.03980  179 VAL B CG2   
4873 N  N     . ASN B 180 ? 0.94110 0.59190 0.56650 -0.11990 -0.21090 0.03300  180 ASN B N     
4874 C  CA    . ASN B 180 ? 0.90920 0.57170 0.52140 -0.12260 -0.18050 0.02850  180 ASN B CA    
4875 C  C     . ASN B 180 ? 0.99840 0.67610 0.62080 -0.12510 -0.16160 0.03270  180 ASN B C     
4876 O  O     . ASN B 180 ? 0.86110 0.56560 0.50190 -0.12530 -0.13880 0.02980  180 ASN B O     
4877 C  CB    . ASN B 180 ? 0.96670 0.59310 0.51980 -0.12620 -0.17580 0.02370  180 ASN B CB    
4878 C  CG    . ASN B 180 ? 1.11390 0.72780 0.65440 -0.12430 -0.18860 0.01680  180 ASN B CG    
4879 O  OD1   . ASN B 180 ? 1.15580 0.79230 0.73520 -0.12080 -0.19730 0.01450  180 ASN B OD1   
4880 N  ND2   . ASN B 180 ? 1.15350 0.72990 0.63850 -0.12660 -0.18920 0.01300  180 ASN B ND2   
4881 N  N     . CYS B 181 ? 0.99170 0.65060 0.60200 -0.12700 -0.17290 0.03890  181 CYS B N     
4882 C  CA    . CYS B 181 ? 0.90980 0.57700 0.52450 -0.13030 -0.15840 0.04230  181 CYS B CA    
4883 C  C     . CYS B 181 ? 0.78910 0.48950 0.45640 -0.12700 -0.15920 0.04670  181 CYS B C     
4884 O  O     . CYS B 181 ? 0.88760 0.60850 0.57000 -0.12880 -0.14070 0.04650  181 CYS B O     
4885 C  CB    . CYS B 181 ? 0.91180 0.54070 0.48630 -0.13380 -0.17100 0.04670  181 CYS B CB    
4886 S  SG    . CYS B 181 ? 1.19030 0.82410 0.76340 -0.13860 -0.15430 0.04980  181 CYS B SG    
4887 N  N     . ASN B 182 ? 0.71330 0.41790 0.40870 -0.12170 -0.18100 0.04990  182 ASN B N     
4888 C  CA    . ASN B 182 ? 0.74110 0.46990 0.48290 -0.11750 -0.18540 0.05500  182 ASN B CA    
4889 C  C     . ASN B 182 ? 0.63730 0.39880 0.42610 -0.11040 -0.18520 0.05350  182 ASN B C     
4890 O  O     . ASN B 182 ? 0.60460 0.38850 0.43240 -0.10580 -0.18460 0.05690  182 ASN B O     
4891 C  CB    . ASN B 182 ? 0.76590 0.47110 0.50720 -0.11650 -0.21200 0.06070  182 ASN B CB    
4892 C  CG    . ASN B 182 ? 0.85270 0.52840 0.55200 -0.12290 -0.21170 0.06290  182 ASN B CG    
4893 O  OD1   . ASN B 182 ? 0.84590 0.53130 0.55170 -0.12550 -0.19970 0.06480  182 ASN B OD1   
4894 N  ND2   . ASN B 182 ? 0.84460 0.48320 0.49860 -0.12520 -0.22470 0.06200  182 ASN B ND2   
4895 N  N     . GLY B 183 ? 0.68840 0.45170 0.47300 -0.10940 -0.18520 0.04760  183 GLY B N     
4896 C  CA    . GLY B 183 ? 0.66160 0.45480 0.48740 -0.10380 -0.18260 0.04420  183 GLY B CA    
4897 C  C     . GLY B 183 ? 0.53650 0.36110 0.38020 -0.10220 -0.15680 0.04240  183 GLY B C     
4898 O  O     . GLY B 183 ? 0.61520 0.43740 0.43470 -0.10630 -0.13940 0.04150  183 GLY B O     
4899 N  N     . PHE B 184 ? 0.51170 0.36450 0.39930 -0.09610 -0.15460 0.04120  184 PHE B N     
4900 C  CA    . PHE B 184 ? 0.47950 0.36120 0.38610 -0.09310 -0.13270 0.03870  184 PHE B CA    
4901 C  C     . PHE B 184 ? 0.48910 0.38530 0.41350 -0.09100 -0.12810 0.03160  184 PHE B C     
4902 O  O     . PHE B 184 ? 0.53550 0.42870 0.47710 -0.09030 -0.14270 0.02970  184 PHE B O     
4903 C  CB    . PHE B 184 ? 0.45570 0.35620 0.39840 -0.08760 -0.13200 0.04260  184 PHE B CB    
4904 C  CG    . PHE B 184 ? 0.56230 0.45290 0.48990 -0.08970 -0.13170 0.04880  184 PHE B CG    
4905 C  CD1   . PHE B 184 ? 0.63700 0.50280 0.55400 -0.09220 -0.15100 0.05440  184 PHE B CD1   
4906 C  CD2   . PHE B 184 ? 0.50640 0.41080 0.43080 -0.08940 -0.11340 0.04870  184 PHE B CD2   
4907 C  CE1   . PHE B 184 ? 0.59390 0.44810 0.49710 -0.09540 -0.15100 0.05980  184 PHE B CE1   
4908 C  CE2   . PHE B 184 ? 0.56720 0.46180 0.47910 -0.09260 -0.11340 0.05410  184 PHE B CE2   
4909 C  CZ    . PHE B 184 ? 0.62020 0.48950 0.52190 -0.09600 -0.13180 0.05970  184 PHE B CZ    
4910 N  N     . THR B 185 ? 0.48490 0.39530 0.40620 -0.09060 -0.10840 0.02760  185 THR B N     
4911 C  CA    . THR B 185 ? 0.56080 0.48630 0.50300 -0.08840 -0.10120 0.02130  185 THR B CA    
4912 C  C     . THR B 185 ? 0.47600 0.42600 0.45520 -0.08290 -0.09110 0.02190  185 THR B C     
4913 O  O     . THR B 185 ? 0.44400 0.40130 0.42060 -0.08070 -0.08170 0.02460  185 THR B O     
4914 C  CB    . THR B 185 ? 0.46660 0.39020 0.38390 -0.09070 -0.08630 0.01670  185 THR B CB    
4915 O  OG1   . THR B 185 ? 0.60620 0.53580 0.51190 -0.09060 -0.07200 0.01970  185 THR B OG1   
4916 C  CG2   . THR B 185 ? 0.60710 0.50500 0.48820 -0.09600 -0.09370 0.01410  185 THR B CG2   
4917 N  N     . ILE B 186 ? 0.42260 0.38300 0.43570 -0.08130 -0.09240 0.01930  186 ILE B N     
4918 C  CA    . ILE B 186 ? 0.40950 0.38940 0.45520 -0.07700 -0.07920 0.01930  186 ILE B CA    
4919 C  C     . ILE B 186 ? 0.37050 0.35680 0.41610 -0.07700 -0.06360 0.01430  186 ILE B C     
4920 O  O     . ILE B 186 ? 0.55740 0.53740 0.60100 -0.08030 -0.06710 0.01050  186 ILE B O     
4921 C  CB    . ILE B 186 ? 0.43520 0.42030 0.52000 -0.07600 -0.08810 0.02150  186 ILE B CB    
4922 C  CG1   . ILE B 186 ? 0.46390 0.44070 0.55110 -0.07490 -0.10530 0.02730  186 ILE B CG1   
4923 C  CG2   . ILE B 186 ? 0.38440 0.38630 0.49860 -0.07240 -0.07070 0.02220  186 ILE B CG2   
4924 C  CD1   . ILE B 186 ? 0.40900 0.38740 0.53700 -0.07320 -0.11890 0.02990  186 ILE B CD1   
4925 N  N     . GLU B 187 ? 0.40960 0.40590 0.45600 -0.07300 -0.04770 0.01450  187 GLU B N     
4926 C  CA    . GLU B 187 ? 0.44950 0.44970 0.49660 -0.07150 -0.03320 0.01170  187 GLU B CA    
4927 C  C     . GLU B 187 ? 0.42380 0.43390 0.49370 -0.06820 -0.01870 0.01300  187 GLU B C     
4928 O  O     . GLU B 187 ? 0.38190 0.39750 0.46030 -0.06590 -0.01760 0.01560  187 GLU B O     
4929 C  CB    . GLU B 187 ? 0.64620 0.64480 0.66360 -0.06990 -0.02790 0.01200  187 GLU B CB    
4930 C  CG    . GLU B 187 ? 0.77030 0.75620 0.75520 -0.07530 -0.03590 0.01080  187 GLU B CG    
4931 C  CD    . GLU B 187 ? 0.85380 0.83250 0.82100 -0.07730 -0.04380 0.01450  187 GLU B CD    
4932 O  OE1   . GLU B 187 ? 0.80760 0.79340 0.78390 -0.07400 -0.04240 0.01760  187 GLU B OE1   
4933 O  OE2   . GLU B 187 ? 0.85140 0.81470 0.79430 -0.08250 -0.05080 0.01440  187 GLU B OE2   
4934 N  N     . ASP B 188 ? 0.35470 0.36430 0.42930 -0.06870 -0.00730 0.01190  188 ASP B N     
4935 C  CA    . ASP B 188 ? 0.45280 0.46720 0.53360 -0.06700 0.00680  0.01560  188 ASP B CA    
4936 C  C     . ASP B 188 ? 0.39960 0.41380 0.46260 -0.06050 0.01820  0.01470  188 ASP B C     
4937 O  O     . ASP B 188 ? 0.36240 0.37620 0.41770 -0.05580 0.01260  0.01540  188 ASP B O     
4938 C  CB    . ASP B 188 ? 0.40740 0.41860 0.49700 -0.07010 0.01050  0.01880  188 ASP B CB    
4939 C  CG    . ASP B 188 ? 0.43400 0.43720 0.50370 -0.07170 0.01620  0.01590  188 ASP B CG    
4940 O  OD1   . ASP B 188 ? 0.43930 0.44100 0.50020 -0.06310 0.01950  0.01290  188 ASP B OD1   
4941 O  OD2   . ASP B 188 ? 0.45860 0.45700 0.53500 -0.07450 0.01650  0.01910  188 ASP B OD2   
4942 N  N     . GLU B 189 ? 0.44420 0.46260 0.50140 -0.05910 0.02560  0.02090  189 GLU B N     
4943 C  CA    . GLU B 189 ? 0.37050 0.39090 0.40750 -0.05230 0.03000  0.02180  189 GLU B CA    
4944 C  C     . GLU B 189 ? 0.36570 0.38100 0.41030 -0.03590 0.03340  0.02790  189 GLU B C     
4945 O  O     . GLU B 189 ? 0.35320 0.37140 0.37980 -0.03230 0.03420  0.02740  189 GLU B O     
4946 C  CB    . GLU B 189 ? 0.36410 0.38800 0.41150 -0.04610 0.04050  0.03050  189 GLU B CB    
4947 C  CG    . GLU B 189 ? 0.40600 0.42310 0.45480 -0.04250 0.04840  0.03430  189 GLU B CG    
4948 C  CD    . GLU B 189 ? 0.46740 0.48150 0.54180 -0.04660 0.04910  0.03590  189 GLU B CD    
4949 O  OE1   . GLU B 189 ? 0.52740 0.54480 0.61590 -0.05310 0.03960  0.03300  189 GLU B OE1   
4950 O  OE2   . GLU B 189 ? 0.44340 0.45070 0.52390 -0.04290 0.05920  0.03980  189 GLU B OE2   
4951 N  N     . GLU B 190 ? 0.30470 0.31810 0.35160 -0.04090 0.03050  0.02840  190 GLU B N     
4952 C  CA    . GLU B 190 ? 0.31880 0.33090 0.34540 -0.04300 0.03080  0.02590  190 GLU B CA    
4953 C  C     . GLU B 190 ? 0.36640 0.37660 0.37740 -0.05120 0.02030  0.01650  190 GLU B C     
4954 O  O     . GLU B 190 ? 0.41570 0.42310 0.41070 -0.05410 0.02020  0.01200  190 GLU B O     
4955 C  CB    . GLU B 190 ? 0.39680 0.40680 0.42640 -0.04550 0.03310  0.03130  190 GLU B CB    
4956 C  CG    . GLU B 190 ? 0.41020 0.41970 0.42720 -0.04270 0.04140  0.03420  190 GLU B CG    
4957 C  CD    . GLU B 190 ? 0.50030 0.49610 0.51870 -0.04210 0.04920  0.03560  190 GLU B CD    
4958 O  OE1   . GLU B 190 ? 0.45480 0.44510 0.47610 -0.04680 0.04640  0.03360  190 GLU B OE1   
4959 O  OE2   . GLU B 190 ? 0.53470 0.52280 0.55180 -0.03600 0.05900  0.03930  190 GLU B OE2   
4960 N  N     . LEU B 191 ? 0.39030 0.40160 0.40430 -0.05460 0.01220  0.01480  191 LEU B N     
4961 C  CA    . LEU B 191 ? 0.48210 0.48980 0.47800 -0.06180 0.00150  0.01020  191 LEU B CA    
4962 C  C     . LEU B 191 ? 0.38540 0.38340 0.37950 -0.06860 -0.00360 0.00750  191 LEU B C     
4963 O  O     . LEU B 191 ? 0.45620 0.44720 0.42560 -0.07390 -0.00740 0.00330  191 LEU B O     
4964 C  CB    . LEU B 191 ? 0.42700 0.43740 0.39600 -0.06190 0.00280  0.00560  191 LEU B CB    
4965 C  CG    . LEU B 191 ? 0.44190 0.45840 0.40880 -0.05770 0.00210  0.00570  191 LEU B CG    
4966 C  CD1   . LEU B 191 ? 0.54100 0.55780 0.48760 -0.06120 0.00050  -0.00070 191 LEU B CD1   
4967 C  CD2   . LEU B 191 ? 0.59530 0.61070 0.57400 -0.05820 -0.00340 0.01060  191 LEU B CD2   
4968 N  N     . SER B 192 ? 0.40260 0.39830 0.42330 -0.06860 -0.00210 0.00930  192 SER B N     
4969 C  CA    . SER B 192 ? 0.46240 0.44770 0.48730 -0.07470 -0.00930 0.00520  192 SER B CA    
4970 C  C     . SER B 192 ? 0.46030 0.44330 0.49210 -0.07800 -0.02260 0.00280  192 SER B C     
4971 O  O     . SER B 192 ? 0.45640 0.44710 0.50450 -0.07600 -0.02230 0.00520  192 SER B O     
4972 C  CB    . SER B 192 ? 0.43040 0.41370 0.48240 -0.07400 0.00040  0.00720  192 SER B CB    
4973 O  OG    . SER B 192 ? 0.65560 0.62680 0.70340 -0.07940 -0.00430 0.00260  192 SER B OG    
4974 N  N     . HIS B 193 ? 0.49680 0.46740 0.51190 -0.08300 -0.03430 -0.00190 193 HIS B N     
4975 C  CA    . HIS B 193 ? 0.46870 0.43360 0.48240 -0.08580 -0.05000 -0.00280 193 HIS B CA    
4976 C  C     . HIS B 193 ? 0.41110 0.38070 0.45980 -0.08770 -0.05390 -0.00280 193 HIS B C     
4977 O  O     . HIS B 193 ? 0.41410 0.37990 0.47490 -0.09100 -0.05170 -0.00590 193 HIS B O     
4978 C  CB    . HIS B 193 ? 0.45450 0.40070 0.43560 -0.09010 -0.05990 -0.00780 193 HIS B CB    
4979 C  CG    . HIS B 193 ? 0.52920 0.46460 0.50140 -0.09240 -0.07750 -0.00720 193 HIS B CG    
4980 N  ND1   . HIS B 193 ? 0.55110 0.48270 0.50440 -0.09170 -0.08180 -0.00190 193 HIS B ND1   
4981 C  CD2   . HIS B 193 ? 0.70140 0.62660 0.68020 -0.09570 -0.09290 -0.01040 193 HIS B CD2   
4982 C  CE1   . HIS B 193 ? 0.80240 0.72040 0.74990 -0.09400 -0.09960 -0.00130 193 HIS B CE1   
4983 N  NE2   . HIS B 193 ? 0.58310 0.49750 0.54580 -0.09620 -0.10750 -0.00650 193 HIS B NE2   
4984 N  N     . LEU B 194 ? 0.37490 0.35160 0.43880 -0.08610 -0.05930 0.00180  194 LEU B N     
4985 C  CA    . LEU B 194 ? 0.46680 0.44810 0.56460 -0.08750 -0.06520 0.00440  194 LEU B CA    
4986 C  C     . LEU B 194 ? 0.47290 0.44380 0.57170 -0.08990 -0.08890 0.00410  194 LEU B C     
4987 O  O     . LEU B 194 ? 0.47600 0.44510 0.59960 -0.09240 -0.09820 0.00350  194 LEU B O     
4988 C  CB    . LEU B 194 ? 0.50750 0.50250 0.62700 -0.08280 -0.05670 0.01060  194 LEU B CB    
4989 C  CG    . LEU B 194 ? 0.56480 0.56830 0.69060 -0.08000 -0.03490 0.01320  194 LEU B CG    
4990 C  CD1   . LEU B 194 ? 0.55060 0.56430 0.70180 -0.07520 -0.03070 0.01930  194 LEU B CD1   
4991 C  CD2   . LEU B 194 ? 0.60920 0.60910 0.74560 -0.08320 -0.02810 0.01300  194 LEU B CD2   
4992 N  N     . GLY B 195 ? 0.44760 0.40970 0.51940 -0.08890 -0.09930 0.00550  195 GLY B N     
4993 C  CA    . GLY B 195 ? 0.49760 0.44450 0.56260 -0.09060 -0.12290 0.00650  195 GLY B CA    
4994 C  C     . GLY B 195 ? 0.49690 0.43220 0.52970 -0.08950 -0.13000 0.01070  195 GLY B C     
4995 O  O     . GLY B 195 ? 0.43760 0.37630 0.44980 -0.08810 -0.11640 0.01190  195 GLY B O     
4996 N  N     . SER B 196 ? 0.52340 0.44270 0.55220 -0.09030 -0.15240 0.01340  196 SER B N     
4997 C  CA    . SER B 196 ? 0.49830 0.39960 0.49420 -0.09060 -0.16180 0.01840  196 SER B CA    
4998 C  C     . SER B 196 ? 0.48820 0.38870 0.51190 -0.08750 -0.17830 0.02480  196 SER B C     
4999 O  O     . SER B 196 ? 0.51190 0.41760 0.57360 -0.08620 -0.18960 0.02420  196 SER B O     
5000 C  CB    . SER B 196 ? 0.65390 0.52640 0.60670 -0.09500 -0.17470 0.01500  196 SER B CB    
5001 O  OG    . SER B 196 ? 0.65820 0.52990 0.58430 -0.09720 -0.15790 0.00930  196 SER B OG    
5002 N  N     . ALA B 197 ? 0.47630 0.36920 0.48340 -0.08650 -0.17950 0.03090  197 ALA B N     
5003 C  CA    . ALA B 197 ? 0.51650 0.40750 0.55050 -0.08300 -0.19440 0.03710  197 ALA B CA    
5004 C  C     . ALA B 197 ? 0.54180 0.40970 0.54140 -0.08470 -0.20310 0.04320  197 ALA B C     
5005 O  O     . ALA B 197 ? 0.54800 0.40790 0.50770 -0.08820 -0.19090 0.04340  197 ALA B O     
5006 C  CB    . ALA B 197 ? 0.44650 0.36610 0.52420 -0.07790 -0.17860 0.03840  197 ALA B CB    
5007 N  N     . ILE B 198 ? 0.54510 0.40150 0.56390 -0.08240 -0.22420 0.04800  198 ILE B N     
5008 C  CA    . ILE B 198 ? 0.56510 0.39960 0.56120 -0.08360 -0.23420 0.05440  198 ILE B CA    
5009 C  C     . ILE B 198 ? 0.50240 0.35610 0.53910 -0.07830 -0.22850 0.05870  198 ILE B C     
5010 O  O     . ILE B 198 ? 0.54200 0.40840 0.62890 -0.07310 -0.23600 0.05870  198 ILE B O     
5011 C  CB    . ILE B 198 ? 0.66670 0.46880 0.65260 -0.08480 -0.26560 0.05600  198 ILE B CB    
5012 C  CG1   . ILE B 198 ? 0.66260 0.43810 0.59470 -0.09050 -0.27050 0.05220  198 ILE B CG1   
5013 C  CG2   . ILE B 198 ? 0.66430 0.44430 0.63630 -0.08560 -0.27750 0.06260  198 ILE B CG2   
5014 C  CD1   . ILE B 198 ? 0.78840 0.57830 0.72680 -0.09090 -0.26240 0.04480  198 ILE B CD1   
5015 N  N     . PHE B 199 ? 0.55960 0.41430 0.57550 -0.07970 -0.21440 0.06170  199 PHE B N     
5016 C  CA    . PHE B 199 ? 0.50510 0.37250 0.55020 -0.07530 -0.20960 0.06560  199 PHE B CA    
5017 C  C     . PHE B 199 ? 0.54280 0.38210 0.55580 -0.07980 -0.22010 0.07140  199 PHE B C     
5018 O  O     . PHE B 199 ? 0.54770 0.38440 0.52940 -0.08420 -0.20580 0.07240  199 PHE B O     
5019 C  CB    . PHE B 199 ? 0.46320 0.35860 0.51290 -0.07330 -0.18190 0.06270  199 PHE B CB    
5020 C  CG    . PHE B 199 ? 0.41030 0.33150 0.49090 -0.06970 -0.16930 0.05660  199 PHE B CG    
5021 C  CD1   . PHE B 199 ? 0.40490 0.34200 0.53830 -0.06370 -0.17010 0.05640  199 PHE B CD1   
5022 C  CD2   . PHE B 199 ? 0.43800 0.36580 0.49620 -0.07280 -0.15520 0.05110  199 PHE B CD2   
5023 C  CE1   . PHE B 199 ? 0.39280 0.35030 0.55320 -0.06180 -0.15640 0.05140  199 PHE B CE1   
5024 C  CE2   . PHE B 199 ? 0.42870 0.37690 0.51390 -0.07050 -0.14350 0.04560  199 PHE B CE2   
5025 C  CZ    . PHE B 199 ? 0.39510 0.35740 0.52990 -0.06550 -0.14370 0.04610  199 PHE B CZ    
5026 N  N     . PRO B 200 ? 0.61310 0.42910 0.63320 -0.07960 -0.24580 0.07450  200 PRO B N     
5027 C  CA    . PRO B 200 ? 0.65920 0.44270 0.64180 -0.08560 -0.25800 0.07860  200 PRO B CA    
5028 C  C     . PRO B 200 ? 0.63060 0.41910 0.61000 -0.08730 -0.24490 0.08180  200 PRO B C     
5029 O  O     . PRO B 200 ? 0.64820 0.41920 0.58280 -0.09520 -0.23880 0.08240  200 PRO B O     
5030 C  CB    . PRO B 200 ? 0.70370 0.47020 0.71280 -0.08230 -0.28780 0.08030  200 PRO B CB    
5031 C  CG    . PRO B 200 ? 0.71410 0.49550 0.75740 -0.07740 -0.29340 0.07630  200 PRO B CG    
5032 C  CD    . PRO B 200 ? 0.60880 0.42750 0.67400 -0.07420 -0.26470 0.07340  200 PRO B CD    
5033 N  N     . ASP B 201 ? 0.64770 0.45920 0.67480 -0.08010 -0.24010 0.08300  201 ASP B N     
5034 C  CA    . ASP B 201 ? 0.61480 0.43070 0.64210 -0.08100 -0.23000 0.08570  201 ASP B CA    
5035 C  C     . ASP B 201 ? 0.60970 0.44040 0.60990 -0.08410 -0.20410 0.08420  201 ASP B C     
5036 O  O     . ASP B 201 ? 0.59350 0.42290 0.57160 -0.08800 -0.19540 0.08340  201 ASP B O     
5037 C  CB    . ASP B 201 ? 0.60430 0.44100 0.69130 -0.07140 -0.23030 0.08600  201 ASP B CB    
5038 C  CG    . ASP B 201 ? 0.67820 0.49670 0.79140 -0.07030 -0.25640 0.08750  201 ASP B CG    
5039 O  OD1   . ASP B 201 ? 0.72020 0.50840 0.79800 -0.07720 -0.27430 0.08910  201 ASP B OD1   
5040 O  OD2   . ASP B 201 ? 0.65190 0.48670 0.82150 -0.06240 -0.25840 0.08610  201 ASP B OD2   
5041 N  N     . VAL B 202 ? 0.57600 0.42860 0.58030 -0.08100 -0.19000 0.07960  202 VAL B N     
5042 C  CA    . VAL B 202 ? 0.49040 0.35810 0.47130 -0.08350 -0.16640 0.07620  202 VAL B CA    
5043 C  C     . VAL B 202 ? 0.52550 0.36740 0.45440 -0.09490 -0.16420 0.07620  202 VAL B C     
5044 O  O     . VAL B 202 ? 0.51600 0.36450 0.42400 -0.09890 -0.14660 0.07290  202 VAL B O     
5045 C  CB    . VAL B 202 ? 0.47610 0.37220 0.47750 -0.07800 -0.15270 0.06910  202 VAL B CB    
5046 C  CG1   . VAL B 202 ? 0.44110 0.35210 0.42170 -0.08000 -0.12960 0.06430  202 VAL B CG1   
5047 C  CG2   . VAL B 202 ? 0.44340 0.36260 0.49820 -0.06880 -0.15160 0.06720  202 VAL B CG2   
5048 N  N     . ALA B 203 ? 0.48470 0.30250 0.39640 -0.09840 -0.18040 0.07590  203 ALA B N     
5049 C  CA    . ALA B 203 ? 0.54020 0.33160 0.40250 -0.10830 -0.17890 0.07360  203 ALA B CA    
5050 C  C     . ALA B 203 ? 0.52860 0.29860 0.36420 -0.11660 -0.18010 0.07500  203 ALA B C     
5051 O  O     . ALA B 203 ? 0.60880 0.36450 0.40590 -0.12420 -0.17070 0.07110  203 ALA B O     
5052 C  CB    . ALA B 203 ? 0.55500 0.32420 0.40380 -0.10780 -0.19870 0.07260  203 ALA B CB    
5053 N  N     . LEU B 204 ? 0.55140 0.32380 0.41000 -0.11310 -0.19040 0.07860  204 LEU B N     
5054 C  CA    . LEU B 204 ? 0.54920 0.30640 0.38680 -0.11910 -0.19300 0.07890  204 LEU B CA    
5055 C  C     . LEU B 204 ? 0.53690 0.31310 0.36350 -0.12230 -0.16840 0.07390  204 LEU B C     
5056 O  O     . LEU B 204 ? 0.56240 0.31980 0.35730 -0.13060 -0.16770 0.07300  204 LEU B O     
5057 C  CB    . LEU B 204 ? 0.56090 0.32180 0.43310 -0.11270 -0.20930 0.08300  204 LEU B CB    
5058 C  CG    . LEU B 204 ? 0.60080 0.34590 0.45510 -0.11800 -0.21580 0.08440  204 LEU B CG    
5059 C  CD1   . LEU B 204 ? 0.71500 0.42220 0.51630 -0.12460 -0.22500 0.08570  204 LEU B CD1   
5060 C  CD2   . LEU B 204 ? 0.65580 0.40520 0.55090 -0.11050 -0.23350 0.08810  204 LEU B CD2   
5061 N  N     . MET B 205 ? 0.50750 0.31810 0.35930 -0.11560 -0.14950 0.07080  205 MET B N     
5062 C  CA    . MET B 205 ? 0.46870 0.29950 0.31640 -0.11690 -0.12820 0.06470  205 MET B CA    
5063 C  C     . MET B 205 ? 0.48770 0.30790 0.30120 -0.12570 -0.11590 0.05880  205 MET B C     
5064 O  O     . MET B 205 ? 0.56760 0.38350 0.37410 -0.12650 -0.11370 0.05760  205 MET B O     
5065 C  CB    . MET B 205 ? 0.43970 0.30370 0.31950 -0.10620 -0.11370 0.06380  205 MET B CB    
5066 C  CG    . MET B 205 ? 0.50070 0.37500 0.41110 -0.09610 -0.12370 0.07030  205 MET B CG    
5067 S  SD    . MET B 205 ? 0.48000 0.38770 0.41920 -0.08710 -0.11070 0.06730  205 MET B SD    
5068 C  CE    . MET B 205 ? 0.39730 0.30750 0.34410 -0.08540 -0.11170 0.06770  205 MET B CE    
5069 N  N     . ASN B 206 ? 0.50750 0.32130 0.29930 -0.13270 -0.10830 0.05550  206 ASN B N     
5070 C  CA    . ASN B 206 ? 0.57200 0.37480 0.33370 -0.14160 -0.09420 0.04920  206 ASN B CA    
5071 C  C     . ASN B 206 ? 0.49550 0.33290 0.27950 -0.13580 -0.07410 0.04140  206 ASN B C     
5072 O  O     . ASN B 206 ? 0.43870 0.30510 0.25540 -0.12530 -0.07110 0.04100  206 ASN B O     
5073 C  CB    . ASN B 206 ? 0.55510 0.34120 0.29040 -0.14420 -0.08850 0.05180  206 ASN B CB    
5074 C  CG    . ASN B 206 ? 0.58260 0.33180 0.28780 -0.14620 -0.10480 0.05960  206 ASN B CG    
5075 O  OD1   . ASN B 206 ? 0.57760 0.30720 0.26280 -0.14720 -0.11180 0.06000  206 ASN B OD1   
5076 N  ND2   . ASN B 206 ? 0.57770 0.31560 0.27810 -0.14570 -0.11160 0.06600  206 ASN B ND2   
5077 N  N     . HIS B 207 ? 0.57270 0.40380 0.33720 -0.14160 -0.06050 0.03510  207 HIS B N     
5078 C  CA    . HIS B 207 ? 0.51520 0.37360 0.29870 -0.13740 -0.04420 0.02680  207 HIS B CA    
5079 C  C     . HIS B 207 ? 0.54490 0.41730 0.33360 -0.13620 -0.03020 0.02260  207 HIS B C     
5080 O  O     . HIS B 207 ? 0.58220 0.43890 0.35320 -0.13950 -0.02460 0.02620  207 HIS B O     
5081 C  CB    . HIS B 207 ? 0.53470 0.38160 0.30070 -0.14000 -0.03590 0.02340  207 HIS B CB    
5082 C  CG    . HIS B 207 ? 0.50420 0.37400 0.28610 -0.13650 -0.01930 0.01480  207 HIS B CG    
5083 N  ND1   . HIS B 207 ? 0.44350 0.33680 0.25240 -0.12940 -0.01800 0.01170  207 HIS B ND1   
5084 C  CD2   . HIS B 207 ? 0.51240 0.38630 0.29050 -0.13610 -0.00270 0.01040  207 HIS B CD2   
5085 C  CE1   . HIS B 207 ? 0.42590 0.33250 0.24240 -0.12850 -0.00510 0.00380  207 HIS B CE1   
5086 N  NE2   . HIS B 207 ? 0.46880 0.36610 0.27000 -0.13100 0.00500  0.00350  207 HIS B NE2   
5087 N  N     . SER B 208 ? 0.48190 0.38270 0.29630 -0.12990 -0.02390 0.01650  208 SER B N     
5088 C  CA    . SER B 208 ? 0.46500 0.38050 0.29060 -0.12660 -0.00860 0.01220  208 SER B CA    
5089 C  C     . SER B 208 ? 0.41900 0.35590 0.26310 -0.12060 -0.00240 0.00440  208 SER B C     
5090 O  O     . SER B 208 ? 0.40050 0.34930 0.26060 -0.11170 -0.00820 0.00550  208 SER B O     
5091 C  CB    . SER B 208 ? 0.51020 0.43480 0.35000 -0.12260 -0.01070 0.01580  208 SER B CB    
5092 O  OG    . SER B 208 ? 0.49730 0.43520 0.35350 -0.12040 0.00270  0.01180  208 SER B OG    
5093 N  N     . CYS B 209 ? 0.39990 0.34290 0.24950 -0.12030 0.01210  -0.00010 209 CYS B N     
5094 C  CA    . CYS B 209 ? 0.42170 0.38410 0.29040 -0.11380 0.01730  -0.00680 209 CYS B CA    
5095 C  C     . CYS B 209 ? 0.43200 0.41380 0.32200 -0.10620 0.01620  -0.00810 209 CYS B C     
5096 O  O     . CYS B 209 ? 0.43290 0.42920 0.33700 -0.10000 0.01800  -0.01270 209 CYS B O     
5097 C  CB    . CYS B 209 ? 0.38190 0.34260 0.25000 -0.11630 0.03280  -0.01040 209 CYS B CB    
5098 S  SG    . CYS B 209 ? 0.48290 0.41550 0.31870 -0.12430 0.03740  -0.00730 209 CYS B SG    
5099 N  N     . CYS B 210 ? 0.45710 0.43610 0.34830 -0.10680 0.01320  -0.00330 210 CYS B N     
5100 C  CA    . CYS B 210 ? 0.52740 0.51900 0.43560 -0.09960 0.01020  -0.00280 210 CYS B CA    
5101 C  C     . CYS B 210 ? 0.48180 0.46610 0.38420 -0.09800 0.00000  0.00400  210 CYS B C     
5102 O  O     . CYS B 210 ? 0.42590 0.40390 0.33210 -0.10000 -0.00150 0.00790  210 CYS B O     
5103 C  CB    . CYS B 210 ? 0.49560 0.49220 0.42150 -0.10170 0.01750  -0.00440 210 CYS B CB    
5104 S  SG    . CYS B 210 ? 0.61480 0.59510 0.53340 -0.11290 0.02560  -0.00040 210 CYS B SG    
5105 N  N     . PRO B 211 ? 0.36560 0.35050 0.26420 -0.09370 -0.00700 0.00630  211 PRO B N     
5106 C  CA    . PRO B 211 ? 0.40500 0.38210 0.30250 -0.09240 -0.01640 0.01430  211 PRO B CA    
5107 C  C     . PRO B 211 ? 0.40710 0.39050 0.32170 -0.08620 -0.01650 0.01580  211 PRO B C     
5108 O  O     . PRO B 211 ? 0.32340 0.31830 0.24960 -0.08110 -0.01040 0.01060  211 PRO B O     
5109 C  CB    . PRO B 211 ? 0.40260 0.38180 0.30660 -0.08600 -0.01870 0.01570  211 PRO B CB    
5110 C  CG    . PRO B 211 ? 0.39070 0.38330 0.30570 -0.07950 -0.01040 0.00880  211 PRO B CG    
5111 C  CD    . PRO B 211 ? 0.37510 0.36780 0.28350 -0.08630 -0.00430 0.00310  211 PRO B CD    
5112 N  N     . ASN B 212 ? 0.37470 0.34850 0.29310 -0.08690 -0.02410 0.02180  212 ASN B N     
5113 C  CA    . ASN B 212 ? 0.37010 0.34730 0.30880 -0.08150 -0.02440 0.02050  212 ASN B CA    
5114 C  C     . ASN B 212 ? 0.39220 0.37250 0.34390 -0.07580 -0.02870 0.02300  212 ASN B C     
5115 O  O     . ASN B 212 ? 0.31270 0.29610 0.28100 -0.07220 -0.02770 0.02010  212 ASN B O     
5116 C  CB    . ASN B 212 ? 0.38420 0.34890 0.32540 -0.08580 -0.02810 0.02260  212 ASN B CB    
5117 C  CG    . ASN B 212 ? 0.39910 0.34660 0.32680 -0.09140 -0.03880 0.03150  212 ASN B CG    
5118 O  OD1   . ASN B 212 ? 0.35410 0.29870 0.27420 -0.09160 -0.04650 0.03640  212 ASN B OD1   
5119 N  ND2   . ASN B 212 ? 0.37740 0.31120 0.30180 -0.09640 -0.04080 0.03390  212 ASN B ND2   
5120 N  N     . VAL B 213 ? 0.28000 0.25910 0.22500 -0.07620 -0.03320 0.02740  213 VAL B N     
5121 C  CA    . VAL B 213 ? 0.30710 0.29170 0.26960 -0.07110 -0.03570 0.02870  213 VAL B CA    
5122 C  C     . VAL B 213 ? 0.37980 0.37000 0.33510 -0.06990 -0.03260 0.02790  213 VAL B C     
5123 O  O     . VAL B 213 ? 0.34710 0.33370 0.28100 -0.07440 -0.03130 0.02810  213 VAL B O     
5124 C  CB    . VAL B 213 ? 0.29870 0.27270 0.27090 -0.07260 -0.04950 0.03640  213 VAL B CB    
5125 C  CG1   . VAL B 213 ? 0.33880 0.30510 0.31950 -0.07340 -0.05330 0.03740  213 VAL B CG1   
5126 C  CG2   . VAL B 213 ? 0.29410 0.25370 0.24290 -0.07910 -0.06060 0.04400  213 VAL B CG2   
5127 N  N     . ILE B 214 ? 0.37840 0.37680 0.35260 -0.06480 -0.03050 0.02640  214 ILE B N     
5128 C  CA    . ILE B 214 ? 0.33500 0.33690 0.30790 -0.06350 -0.02900 0.02600  214 ILE B CA    
5129 C  C     . ILE B 214 ? 0.32780 0.32920 0.32300 -0.06240 -0.03630 0.02950  214 ILE B C     
5130 O  O     . ILE B 214 ? 0.29220 0.29760 0.31100 -0.05990 -0.03600 0.02970  214 ILE B O     
5131 C  CB    . ILE B 214 ? 0.35610 0.36860 0.33180 -0.05860 -0.01850 0.01990  214 ILE B CB    
5132 C  CG1   . ILE B 214 ? 0.60390 0.61780 0.56010 -0.05990 -0.01390 0.01570  214 ILE B CG1   
5133 C  CG2   . ILE B 214 ? 0.39070 0.40580 0.37060 -0.05720 -0.01750 0.01980  214 ILE B CG2   
5134 C  CD1   . ILE B 214 ? 0.58740 0.61000 0.54460 -0.05580 -0.00760 0.00960  214 ILE B CD1   
5135 N  N     . VAL B 215 ? 0.34190 0.33810 0.33130 -0.06490 -0.04260 0.03200  215 VAL B N     
5136 C  CA    . VAL B 215 ? 0.32160 0.31790 0.33410 -0.06390 -0.05090 0.03430  215 VAL B CA    
5137 C  C     . VAL B 215 ? 0.32960 0.33650 0.35670 -0.06070 -0.04090 0.02940  215 VAL B C     
5138 O  O     . VAL B 215 ? 0.29830 0.30520 0.30930 -0.06130 -0.03590 0.02680  215 VAL B O     
5139 C  CB    . VAL B 215 ? 0.36010 0.34040 0.35670 -0.06930 -0.06560 0.03960  215 VAL B CB    
5140 C  CG1   . VAL B 215 ? 0.34490 0.32540 0.37020 -0.06740 -0.07710 0.04150  215 VAL B CG1   
5141 C  CG2   . VAL B 215 ? 0.39240 0.35590 0.36650 -0.07450 -0.07450 0.04610  215 VAL B CG2   
5142 N  N     . THR B 216 ? 0.29810 0.31300 0.35590 -0.05770 -0.03720 0.02920  216 THR B N     
5143 C  CA    . THR B 216 ? 0.31130 0.33350 0.38450 -0.05610 -0.02750 0.02660  216 THR B CA    
5144 C  C     . THR B 216 ? 0.35510 0.37860 0.45870 -0.05590 -0.03620 0.03040  216 THR B C     
5145 O  O     . THR B 216 ? 0.28570 0.30460 0.40010 -0.05570 -0.04990 0.03470  216 THR B O     
5146 C  CB    . THR B 216 ? 0.35100 0.38010 0.42960 -0.05260 -0.01030 0.02440  216 THR B CB    
5147 O  OG1   . THR B 216 ? 0.39890 0.43120 0.49730 -0.05050 -0.00980 0.02790  216 THR B OG1   
5148 C  CG2   . THR B 216 ? 0.36670 0.39360 0.41960 -0.05110 -0.00470 0.02130  216 THR B CG2   
5149 N  N     . TYR B 217 ? 0.32630 0.35470 0.44530 -0.05550 -0.02930 0.02950  217 TYR B N     
5150 C  CA    . TYR B 217 ? 0.32890 0.35830 0.48080 -0.05490 -0.03810 0.03270  217 TYR B CA    
5151 C  C     . TYR B 217 ? 0.32100 0.35870 0.50240 -0.05030 -0.02210 0.03440  217 TYR B C     
5152 O  O     . TYR B 217 ? 0.39240 0.43180 0.56000 -0.05000 -0.00690 0.03270  217 TYR B O     
5153 C  CB    . TYR B 217 ? 0.33750 0.36040 0.47830 -0.05970 -0.04830 0.03060  217 TYR B CB    
5154 C  CG    . TYR B 217 ? 0.34450 0.35580 0.45160 -0.06310 -0.06060 0.03000  217 TYR B CG    
5155 C  CD1   . TYR B 217 ? 0.37340 0.37440 0.48020 -0.06380 -0.07920 0.03460  217 TYR B CD1   
5156 C  CD2   . TYR B 217 ? 0.36650 0.37460 0.44210 -0.06490 -0.05330 0.02610  217 TYR B CD2   
5157 C  CE1   . TYR B 217 ? 0.39510 0.38100 0.46580 -0.06750 -0.08880 0.03600  217 TYR B CE1   
5158 C  CE2   . TYR B 217 ? 0.37910 0.37490 0.42280 -0.06800 -0.06210 0.02740  217 TYR B CE2   
5159 C  CZ    . TYR B 217 ? 0.40940 0.39300 0.44810 -0.07000 -0.07890 0.03260  217 TYR B CZ    
5160 O  OH    . TYR B 217 ? 0.54370 0.51050 0.54630 -0.07450 -0.08530 0.03520  217 TYR B OH    
5161 N  N     . LYS B 218 ? 0.35300 0.39340 0.57420 -0.04610 -0.02550 0.03810  218 LYS B N     
5162 C  CA    . LYS B 218 ? 0.36340 0.40900 0.62060 -0.04090 -0.01050 0.04010  218 LYS B CA    
5163 C  C     . LYS B 218 ? 0.41150 0.45640 0.70170 -0.04250 -0.02360 0.04130  218 LYS B C     
5164 O  O     . LYS B 218 ? 0.35040 0.39450 0.67350 -0.04010 -0.03590 0.04340  218 LYS B O     
5165 C  CB    . LYS B 218 ? 0.41200 0.45950 0.69350 -0.03420 -0.00270 0.04220  218 LYS B CB    
5166 C  CG    . LYS B 218 ? 0.50080 0.54960 0.80700 -0.02780 0.02140  0.04350  218 LYS B CG    
5167 C  CD    . LYS B 218 ? 0.61790 0.66580 0.93700 -0.02160 0.03200  0.04400  218 LYS B CD    
5168 C  CE    . LYS B 218 ? 0.59420 0.64010 0.87060 -0.02130 0.04030  0.04180  218 LYS B CE    
5169 N  NZ    . LYS B 218 ? 0.55370 0.59790 0.84230 -0.01620 0.04700  0.04150  218 LYS B NZ    
5170 N  N     . GLY B 219 ? 0.40410 0.44800 0.68600 -0.04670 -0.02250 0.03960  219 GLY B N     
5171 C  CA    . GLY B 219 ? 0.38060 0.42210 0.68590 -0.04990 -0.03830 0.03930  219 GLY B CA    
5172 C  C     . GLY B 219 ? 0.42640 0.45920 0.70920 -0.05410 -0.06310 0.03810  219 GLY B C     
5173 O  O     . GLY B 219 ? 0.35610 0.38350 0.59590 -0.05840 -0.06480 0.03520  219 GLY B O     
5174 N  N     . THR B 220 ? 0.38930 0.41820 0.70130 -0.05230 -0.08180 0.04050  220 THR B N     
5175 C  CA    . THR B 220 ? 0.44660 0.46190 0.73720 -0.05520 -0.10720 0.04100  220 THR B CA    
5176 C  C     . THR B 220 ? 0.40250 0.41320 0.68580 -0.05200 -0.11340 0.04460  220 THR B C     
5177 O  O     . THR B 220 ? 0.43630 0.43180 0.70350 -0.05380 -0.13500 0.04670  220 THR B O     
5178 C  CB    . THR B 220 ? 0.49060 0.49890 0.81540 -0.05580 -0.12940 0.04160  220 THR B CB    
5179 O  OG1   . THR B 220 ? 0.48980 0.50330 0.86710 -0.04980 -0.13000 0.04470  220 THR B OG1   
5180 C  CG2   . THR B 220 ? 0.51570 0.52770 0.85140 -0.05950 -0.12490 0.03800  220 THR B CG2   
5181 N  N     . LEU B 221 ? 0.46970 0.49060 0.76410 -0.04750 -0.09470 0.04540  221 LEU B N     
5182 C  CA    . LEU B 221 ? 0.46460 0.48230 0.75530 -0.04440 -0.09780 0.04820  221 LEU B CA    
5183 C  C     . LEU B 221 ? 0.39010 0.40670 0.63040 -0.04760 -0.08890 0.04640  221 LEU B C     
5184 O  O     . LEU B 221 ? 0.33640 0.36200 0.56490 -0.04770 -0.06870 0.04310  221 LEU B O     
5185 C  CB    . LEU B 221 ? 0.40890 0.43680 0.74240 -0.03740 -0.08100 0.04920  221 LEU B CB    
5186 C  CG    . LEU B 221 ? 0.51340 0.53890 0.85010 -0.03360 -0.08140 0.05130  221 LEU B CG    
5187 C  CD1   . LEU B 221 ? 0.49760 0.51120 0.86040 -0.03210 -0.10620 0.05510  221 LEU B CD1   
5188 C  CD2   . LEU B 221 ? 0.47860 0.51400 0.84170 -0.02740 -0.05540 0.05010  221 LEU B CD2   
5189 N  N     . ALA B 222 ? 0.27760 0.28080 0.48900 -0.05030 -0.10420 0.04880  222 ALA B N     
5190 C  CA    . ALA B 222 ? 0.34610 0.34680 0.51440 -0.05340 -0.09640 0.04730  222 ALA B CA    
5191 C  C     . ALA B 222 ? 0.36720 0.37390 0.54790 -0.04930 -0.08740 0.04840  222 ALA B C     
5192 O  O     . ALA B 222 ? 0.44710 0.45090 0.65810 -0.04530 -0.09680 0.05230  222 ALA B O     
5193 C  CB    . ALA B 222 ? 0.35440 0.33480 0.48570 -0.05850 -0.11420 0.05050  222 ALA B CB    
5194 N  N     . GLU B 223 ? 0.34760 0.36110 0.50660 -0.05010 -0.06980 0.04430  223 GLU B N     
5195 C  CA    . GLU B 223 ? 0.34080 0.35790 0.50420 -0.04740 -0.06070 0.04410  223 GLU B CA    
5196 C  C     . GLU B 223 ? 0.32100 0.33160 0.44110 -0.05230 -0.05930 0.04190  223 GLU B C     
5197 O  O     . GLU B 223 ? 0.27190 0.28160 0.36430 -0.05550 -0.05470 0.03850  223 GLU B O     
5198 C  CB    . GLU B 223 ? 0.36400 0.39360 0.54650 -0.04290 -0.03830 0.04110  223 GLU B CB    
5199 C  CG    . GLU B 223 ? 0.41360 0.44870 0.64280 -0.03710 -0.03520 0.04330  223 GLU B CG    
5200 C  CD    . GLU B 223 ? 0.53410 0.57630 0.78000 -0.03120 -0.01000 0.04180  223 GLU B CD    
5201 O  OE1   . GLU B 223 ? 0.56290 0.60640 0.78030 -0.03240 0.00400  0.03900  223 GLU B OE1   
5202 O  OE2   . GLU B 223 ? 0.53180 0.57550 0.81820 -0.02480 -0.00340 0.04340  223 GLU B OE2   
5203 N  N     . VAL B 224 ? 0.28820 0.29340 0.40650 -0.05220 -0.06290 0.04380  224 VAL B N     
5204 C  CA    . VAL B 224 ? 0.28200 0.27900 0.36350 -0.05690 -0.06250 0.04250  224 VAL B CA    
5205 C  C     . VAL B 224 ? 0.27280 0.27430 0.35940 -0.05550 -0.05020 0.03860  224 VAL B C     
5206 O  O     . VAL B 224 ? 0.32160 0.32130 0.43350 -0.05260 -0.05330 0.04090  224 VAL B O     
5207 C  CB    . VAL B 224 ? 0.34570 0.32470 0.41400 -0.06040 -0.08200 0.04980  224 VAL B CB    
5208 C  CG1   . VAL B 224 ? 0.36200 0.33230 0.39340 -0.06580 -0.07850 0.04910  224 VAL B CG1   
5209 C  CG2   . VAL B 224 ? 0.40440 0.37350 0.46560 -0.06250 -0.09610 0.05450  224 VAL B CG2   
5210 N  N     . ARG B 225 ? 0.24720 0.25310 0.31230 -0.05690 -0.03710 0.03270  225 ARG B N     
5211 C  CA    . ARG B 225 ? 0.25030 0.25860 0.31670 -0.05650 -0.02580 0.02870  225 ARG B CA    
5212 C  C     . ARG B 225 ? 0.24850 0.25130 0.28400 -0.06020 -0.02580 0.02470  225 ARG B C     
5213 O  O     . ARG B 225 ? 0.29160 0.29470 0.30660 -0.06090 -0.02640 0.02380  225 ARG B O     
5214 C  CB    . ARG B 225 ? 0.27580 0.29510 0.35130 -0.05340 -0.01000 0.02680  225 ARG B CB    
5215 C  CG    . ARG B 225 ? 0.28970 0.31450 0.40400 -0.04680 -0.00290 0.03040  225 ARG B CG    
5216 C  CD    . ARG B 225 ? 0.33320 0.36460 0.45170 -0.04070 0.01860  0.02940  225 ARG B CD    
5217 N  NE    . ARG B 225 ? 0.32360 0.35850 0.47840 -0.03260 0.02770  0.03160  225 ARG B NE    
5218 C  CZ    . ARG B 225 ? 0.30040 0.33900 0.47240 -0.03190 0.02200  0.03400  225 ARG B CZ    
5219 N  NH1   . ARG B 225 ? 0.35590 0.39420 0.50940 -0.03820 0.00870  0.03380  225 ARG B NH1   
5220 N  NH2   . ARG B 225 ? 0.33630 0.37690 0.54460 -0.02460 0.03130  0.03580  225 ARG B NH2   
5221 N  N     . ALA B 226 ? 0.27070 0.26790 0.30640 -0.06200 -0.02480 0.02230  226 ALA B N     
5222 C  CA    . ALA B 226 ? 0.30330 0.29600 0.31650 -0.06500 -0.02420 0.01760  226 ALA B CA    
5223 C  C     . ALA B 226 ? 0.31340 0.31590 0.31360 -0.06430 -0.01560 0.01140  226 ALA B C     
5224 O  O     . ALA B 226 ? 0.34990 0.35800 0.35450 -0.06380 -0.00810 0.00890  226 ALA B O     
5225 C  CB    . ALA B 226 ? 0.31930 0.30090 0.33860 -0.06730 -0.02680 0.01550  226 ALA B CB    
5226 N  N     . VAL B 227 ? 0.32780 0.33150 0.31130 -0.06460 -0.01540 0.00980  227 VAL B N     
5227 C  CA    . VAL B 227 ? 0.31170 0.32340 0.28470 -0.06370 -0.00980 0.00390  227 VAL B CA    
5228 C  C     . VAL B 227 ? 0.26000 0.26900 0.22920 -0.06620 -0.01030 -0.00070 227 VAL B C     
5229 O  O     . VAL B 227 ? 0.30420 0.32010 0.27040 -0.06520 -0.00740 -0.00590 227 VAL B O     
5230 C  CB    . VAL B 227 ? 0.34210 0.35900 0.30650 -0.06150 -0.00740 0.00570  227 VAL B CB    
5231 C  CG1   . VAL B 227 ? 0.33370 0.35350 0.30630 -0.05840 -0.00710 0.00870  227 VAL B CG1   
5232 C  CG2   . VAL B 227 ? 0.28950 0.30010 0.24460 -0.06460 -0.01010 0.00920  227 VAL B CG2   
5233 N  N     . GLN B 228 ? 0.40180 0.40090 0.37460 -0.06940 -0.01460 0.00140  228 GLN B N     
5234 C  CA    . GLN B 228 ? 0.40910 0.40350 0.38450 -0.07240 -0.01590 -0.00350 228 GLN B CA    
5235 C  C     . GLN B 228 ? 0.40620 0.38780 0.38880 -0.07420 -0.02100 -0.00290 228 GLN B C     
5236 O  O     . GLN B 228 ? 0.35080 0.32750 0.33770 -0.07370 -0.02390 0.00360  228 GLN B O     
5237 C  CB    . GLN B 228 ? 0.40240 0.39440 0.37300 -0.07710 -0.01430 -0.00040 228 GLN B CB    
5238 C  CG    . GLN B 228 ? 0.51060 0.51290 0.47610 -0.07670 -0.00880 -0.00200 228 GLN B CG    
5239 C  CD    . GLN B 228 ? 0.44500 0.44340 0.40650 -0.08370 -0.00570 -0.00070 228 GLN B CD    
5240 O  OE1   . GLN B 228 ? 0.67360 0.66850 0.64460 -0.08810 -0.00560 -0.00320 228 GLN B OE1   
5241 N  NE2   . GLN B 228 ? 0.61000 0.60780 0.55770 -0.08570 -0.00320 0.00240  228 GLN B NE2   
5242 N  N     . GLU B 229 ? 0.40670 0.38170 0.39320 -0.07620 -0.02320 -0.00980 229 GLU B N     
5243 C  CA    . GLU B 229 ? 0.45220 0.41080 0.44520 -0.07810 -0.02790 -0.00990 229 GLU B CA    
5244 C  C     . GLU B 229 ? 0.44700 0.39710 0.43900 -0.08180 -0.03020 0.00040  229 GLU B C     
5245 O  O     . GLU B 229 ? 0.43090 0.38360 0.41660 -0.08550 -0.02740 0.00270  229 GLU B O     
5246 C  CB    . GLU B 229 ? 0.49670 0.44800 0.49190 -0.07910 -0.03030 -0.02130 229 GLU B CB    
5247 C  CG    . GLU B 229 ? 0.94860 0.90360 0.93470 -0.07440 -0.03060 -0.03380 229 GLU B CG    
5248 C  CD    . GLU B 229 ? 1.30580 1.24840 1.28560 -0.06600 -0.02780 -0.03820 229 GLU B CD    
5249 O  OE1   . GLU B 229 ? 1.19080 1.11670 1.17730 -0.06330 -0.02940 -0.03930 229 GLU B OE1   
5250 O  OE2   . GLU B 229 ? 0.63950 0.59090 0.61110 -0.05650 -0.02070 -0.03890 229 GLU B OE2   
5251 N  N     . ILE B 230 ? 0.43970 0.37770 0.43720 -0.08070 -0.03590 0.00670  230 ILE B N     
5252 C  CA    . ILE B 230 ? 0.45180 0.37730 0.44400 -0.08380 -0.04210 0.01700  230 ILE B CA    
5253 C  C     . ILE B 230 ? 0.48890 0.39520 0.49060 -0.08370 -0.04770 0.01720  230 ILE B C     
5254 O  O     . ILE B 230 ? 0.56480 0.46580 0.58130 -0.07820 -0.05020 0.01440  230 ILE B O     
5255 C  CB    . ILE B 230 ? 0.42720 0.35470 0.41990 -0.08090 -0.04880 0.02580  230 ILE B CB    
5256 C  CG1   . ILE B 230 ? 0.42030 0.36470 0.40400 -0.08000 -0.04280 0.02450  230 ILE B CG1   
5257 C  CG2   . ILE B 230 ? 0.45100 0.36190 0.43260 -0.08470 -0.05960 0.03640  230 ILE B CG2   
5258 C  CD1   . ILE B 230 ? 0.46570 0.41350 0.45420 -0.07700 -0.04930 0.03080  230 ILE B CD1   
5259 N  N     . LYS B 231 ? 0.44910 0.34290 0.44320 -0.08930 -0.04880 0.02050  231 LYS B N     
5260 C  CA    . LYS B 231 ? 0.44130 0.31490 0.44310 -0.08920 -0.05340 0.02070  231 LYS B CA    
5261 C  C     . LYS B 231 ? 0.43350 0.29030 0.42980 -0.08920 -0.06450 0.03390  231 LYS B C     
5262 O  O     . LYS B 231 ? 0.41760 0.27600 0.39790 -0.09260 -0.06760 0.04180  231 LYS B O     
5263 C  CB    . LYS B 231 ? 0.52150 0.39110 0.52170 -0.09610 -0.04700 0.01450  231 LYS B CB    
5264 C  CG    . LYS B 231 ? 0.50980 0.39520 0.51670 -0.09580 -0.04040 0.00050  231 LYS B CG    
5265 C  CD    . LYS B 231 ? 0.67590 0.55720 0.69010 -0.08880 -0.04330 -0.00890 231 LYS B CD    
5266 C  CE    . LYS B 231 ? 0.82360 0.71070 0.83960 -0.08930 -0.04100 -0.02440 231 LYS B CE    
5267 N  NZ    . LYS B 231 ? 1.20120 1.07720 1.21520 -0.08130 -0.04390 -0.03490 231 LYS B NZ    
5268 N  N     . PRO B 232 ? 0.48110 0.31970 0.48960 -0.08480 -0.07220 0.03610  232 PRO B N     
5269 C  CA    . PRO B 232 ? 0.57760 0.39810 0.58120 -0.08430 -0.08540 0.04860  232 PRO B CA    
5270 C  C     . PRO B 232 ? 0.56380 0.37360 0.54020 -0.09460 -0.08340 0.05550  232 PRO B C     
5271 O  O     . PRO B 232 ? 0.53890 0.34790 0.51190 -0.10100 -0.07190 0.05020  232 PRO B O     
5272 C  CB    . PRO B 232 ? 0.53030 0.33340 0.55240 -0.07820 -0.08930 0.04620  232 PRO B CB    
5273 C  CG    . PRO B 232 ? 0.50790 0.32200 0.54880 -0.07170 -0.08110 0.03310  232 PRO B CG    
5274 C  CD    . PRO B 232 ? 0.50100 0.33360 0.52780 -0.07890 -0.06970 0.02600  232 PRO B CD    
5275 N  N     . GLY B 233 ? 0.52570 0.32700 0.48460 -0.09630 -0.09460 0.06630  233 GLY B N     
5276 C  CA    . GLY B 233 ? 0.58720 0.37400 0.51570 -0.10580 -0.09220 0.07310  233 GLY B CA    
5277 C  C     . GLY B 233 ? 0.58310 0.38460 0.49300 -0.11160 -0.08280 0.07080  233 GLY B C     
5278 O  O     . GLY B 233 ? 0.60620 0.39420 0.48800 -0.11850 -0.08230 0.07680  233 GLY B O     
5279 N  N     . GLU B 234 ? 0.55270 0.37990 0.47720 -0.10830 -0.07480 0.06170  234 GLU B N     
5280 C  CA    . GLU B 234 ? 0.54860 0.39190 0.46000 -0.11210 -0.06510 0.05800  234 GLU B CA    
5281 C  C     . GLU B 234 ? 0.50990 0.35490 0.40860 -0.11050 -0.07670 0.06250  234 GLU B C     
5282 O  O     . GLU B 234 ? 0.47100 0.31850 0.38530 -0.10380 -0.08940 0.06480  234 GLU B O     
5283 C  CB    . GLU B 234 ? 0.51700 0.38500 0.44870 -0.10850 -0.05290 0.04630  234 GLU B CB    
5284 C  CG    . GLU B 234 ? 0.59830 0.46490 0.54370 -0.11160 -0.04350 0.03980  234 GLU B CG    
5285 C  CD    . GLU B 234 ? 0.73080 0.62040 0.69170 -0.10940 -0.03400 0.02780  234 GLU B CD    
5286 O  OE1   . GLU B 234 ? 0.60670 0.51060 0.57370 -0.10250 -0.03550 0.02350  234 GLU B OE1   
5287 O  OE2   . GLU B 234 ? 0.61940 0.51160 0.58820 -0.11440 -0.02590 0.02280  234 GLU B OE2   
5288 N  N     . GLU B 235 ? 0.47390 0.31690 0.34690 -0.11690 -0.07230 0.06290  235 GLU B N     
5289 C  CA    . GLU B 235 ? 0.48230 0.32460 0.34030 -0.11750 -0.08310 0.06490  235 GLU B CA    
5290 C  C     . GLU B 235 ? 0.44020 0.30970 0.31540 -0.11180 -0.07780 0.05830  235 GLU B C     
5291 O  O     . GLU B 235 ? 0.39400 0.28120 0.27930 -0.11010 -0.06200 0.05070  235 GLU B O     
5292 C  CB    . GLU B 235 ? 0.50900 0.33480 0.33170 -0.12670 -0.07820 0.06560  235 GLU B CB    
5293 C  CG    . GLU B 235 ? 0.49970 0.32150 0.30600 -0.12890 -0.08870 0.06470  235 GLU B CG    
5294 C  CD    . GLU B 235 ? 0.59620 0.38810 0.36400 -0.13660 -0.08930 0.06750  235 GLU B CD    
5295 O  OE1   . GLU B 235 ? 0.69300 0.47080 0.44520 -0.14050 -0.07750 0.07050  235 GLU B OE1   
5296 O  OE2   . GLU B 235 ? 0.66110 0.44170 0.41490 -0.13860 -0.10080 0.06710  235 GLU B OE2   
5297 N  N     . VAL B 236 ? 0.39250 0.26420 0.27330 -0.10850 -0.09220 0.06150  236 VAL B N     
5298 C  CA    . VAL B 236 ? 0.37440 0.26810 0.27000 -0.10260 -0.08780 0.05770  236 VAL B CA    
5299 C  C     . VAL B 236 ? 0.38730 0.28030 0.25720 -0.10920 -0.08660 0.05470  236 VAL B C     
5300 O  O     . VAL B 236 ? 0.42130 0.29610 0.27650 -0.11420 -0.09730 0.05700  236 VAL B O     
5301 C  CB    . VAL B 236 ? 0.39700 0.29280 0.31890 -0.09520 -0.10270 0.06310  236 VAL B CB    
5302 C  CG1   . VAL B 236 ? 0.39160 0.30920 0.33300 -0.08810 -0.09240 0.05860  236 VAL B CG1   
5303 C  CG2   . VAL B 236 ? 0.41240 0.30450 0.36010 -0.08990 -0.10530 0.06400  236 VAL B CG2   
5304 N  N     . PHE B 237 ? 0.39460 0.30570 0.26630 -0.10710 -0.06970 0.04710  237 PHE B N     
5305 C  CA    . PHE B 237 ? 0.42290 0.33570 0.28260 -0.10990 -0.06110 0.04070  237 PHE B CA    
5306 C  C     . PHE B 237 ? 0.40700 0.34040 0.28580 -0.10000 -0.05330 0.03760  237 PHE B C     
5307 O  O     . PHE B 237 ? 0.37640 0.32580 0.26920 -0.09420 -0.04580 0.03490  237 PHE B O     
5308 C  CB    . PHE B 237 ? 0.44850 0.36180 0.29470 -0.11690 -0.04780 0.03370  237 PHE B CB    
5309 C  CG    . PHE B 237 ? 0.44640 0.33690 0.27550 -0.12420 -0.04690 0.03770  237 PHE B CG    
5310 C  CD1   . PHE B 237 ? 0.48480 0.34990 0.28620 -0.13220 -0.05150 0.04000  237 PHE B CD1   
5311 C  CD2   . PHE B 237 ? 0.51240 0.40430 0.35300 -0.12290 -0.03970 0.03930  237 PHE B CD2   
5312 C  CE1   . PHE B 237 ? 0.51450 0.35660 0.29610 -0.13720 -0.04820 0.04540  237 PHE B CE1   
5313 C  CE2   . PHE B 237 ? 0.52290 0.39310 0.34790 -0.12950 -0.03700 0.04430  237 PHE B CE2   
5314 C  CZ    . PHE B 237 ? 0.52380 0.36920 0.31770 -0.13610 -0.04080 0.04800  237 PHE B CZ    
5315 N  N     . THR B 238 ? 0.38860 0.31800 0.26450 -0.09950 -0.05580 0.03760  238 THR B N     
5316 C  CA    . THR B 238 ? 0.41910 0.36300 0.30660 -0.09240 -0.04720 0.03540  238 THR B CA    
5317 C  C     . THR B 238 ? 0.44680 0.38970 0.32640 -0.09800 -0.03910 0.02500  238 THR B C     
5318 O  O     . THR B 238 ? 0.47410 0.40040 0.33410 -0.10820 -0.03870 0.02450  238 THR B O     
5319 C  CB    . THR B 238 ? 0.42530 0.36130 0.32030 -0.09170 -0.05760 0.04330  238 THR B CB    
5320 O  OG1   . THR B 238 ? 0.57620 0.52820 0.48450 -0.08610 -0.05100 0.04020  238 THR B OG1   
5321 C  CG2   . THR B 238 ? 0.44320 0.35470 0.31980 -0.10080 -0.06510 0.04550  238 THR B CG2   
5322 N  N     . SER B 239 ? 0.45400 0.41020 0.34480 -0.09240 -0.03160 0.02010  239 SER B N     
5323 C  CA    . SER B 239 ? 0.40890 0.35970 0.29200 -0.09830 -0.02350 0.01570  239 SER B CA    
5324 C  C     . SER B 239 ? 0.43390 0.37170 0.30790 -0.10180 -0.02770 0.02070  239 SER B C     
5325 O  O     . SER B 239 ? 0.41980 0.36370 0.30390 -0.09580 -0.03090 0.02570  239 SER B O     
5326 C  CB    . SER B 239 ? 0.45700 0.42720 0.35460 -0.09050 -0.01390 0.00810  239 SER B CB    
5327 O  OG    . SER B 239 ? 0.46510 0.42990 0.35330 -0.09630 -0.00750 0.00380  239 SER B OG    
5328 N  N     . TYR B 240 ? 0.41900 0.33530 0.26640 -0.11220 -0.02840 0.01950  240 TYR B N     
5329 C  CA    . TYR B 240 ? 0.44420 0.33940 0.27200 -0.11780 -0.03500 0.02300  240 TYR B CA    
5330 C  C     . TYR B 240 ? 0.41500 0.31910 0.24640 -0.11650 -0.02480 0.01680  240 TYR B C     
5331 O  O     . TYR B 240 ? 0.43090 0.32150 0.25010 -0.11940 -0.03020 0.01940  240 TYR B O     
5332 C  CB    . TYR B 240 ? 0.49390 0.35270 0.28260 -0.13050 -0.04030 0.02400  240 TYR B CB    
5333 C  CG    . TYR B 240 ? 0.48470 0.32500 0.26210 -0.13350 -0.05440 0.03090  240 TYR B CG    
5334 C  CD1   . TYR B 240 ? 0.44770 0.30610 0.25170 -0.12580 -0.06040 0.03540  240 TYR B CD1   
5335 C  CD2   . TYR B 240 ? 0.48520 0.29380 0.22520 -0.13790 -0.06030 0.03220  240 TYR B CD2   
5336 C  CE1   . TYR B 240 ? 0.44020 0.28010 0.23460 -0.12880 -0.07470 0.04150  240 TYR B CE1   
5337 C  CE2   . TYR B 240 ? 0.53200 0.32140 0.25980 -0.14010 -0.07460 0.03840  240 TYR B CE2   
5338 C  CZ    . TYR B 240 ? 0.52380 0.32590 0.27920 -0.13860 -0.08350 0.04310  240 TYR B CZ    
5339 O  OH    . TYR B 240 ? 0.54410 0.32670 0.28900 -0.14000 -0.09910 0.04900  240 TYR B OH    
5340 N  N     . ILE B 241 ? 0.44780 0.37080 0.29350 -0.11270 -0.01270 0.00900  241 ILE B N     
5341 C  CA    . ILE B 241 ? 0.48380 0.41080 0.32970 -0.11330 -0.00330 0.00230  241 ILE B CA    
5342 C  C     . ILE B 241 ? 0.41760 0.37290 0.29340 -0.10200 0.00240  -0.00240 241 ILE B C     
5343 O  O     . ILE B 241 ? 0.37110 0.34030 0.26370 -0.09440 0.00040  -0.00150 241 ILE B O     
5344 C  CB    . ILE B 241 ? 0.52430 0.43510 0.34590 -0.12070 0.00610  -0.00330 241 ILE B CB    
5345 C  CG1   . ILE B 241 ? 0.56270 0.48130 0.38980 -0.12110 0.01110  -0.00600 241 ILE B CG1   
5346 C  CG2   . ILE B 241 ? 0.62500 0.50490 0.41100 -0.12550 0.00060  0.00120  241 ILE B CG2   
5347 C  CD1   . ILE B 241 ? 0.61810 0.53000 0.43100 -0.12210 0.02610  -0.01030 241 ILE B CD1   
5348 N  N     . ASP B 242 ? 0.41710 0.37600 0.29490 -0.10180 0.00880  -0.00750 242 ASP B N     
5349 C  CA    . ASP B 242 ? 0.38470 0.36360 0.28370 -0.09330 0.01340  -0.01260 242 ASP B CA    
5350 C  C     . ASP B 242 ? 0.42020 0.40260 0.31840 -0.09700 0.01990  -0.01850 242 ASP B C     
5351 O  O     . ASP B 242 ? 0.45070 0.42230 0.33380 -0.10280 0.02860  -0.02170 242 ASP B O     
5352 C  CB    . ASP B 242 ? 0.42320 0.40020 0.31960 -0.09520 0.01850  -0.01660 242 ASP B CB    
5353 C  CG    . ASP B 242 ? 0.38520 0.37990 0.30140 -0.08640 0.02060  -0.02020 242 ASP B CG    
5354 O  OD1   . ASP B 242 ? 0.37410 0.38060 0.30160 -0.08180 0.02050  -0.02180 242 ASP B OD1   
5355 O  OD2   . ASP B 242 ? 0.42920 0.42340 0.34590 -0.08610 0.02240  -0.02170 242 ASP B OD2   
5356 N  N     . LEU B 243 ? 0.32830 0.32510 0.24170 -0.08950 0.01760  -0.01820 243 LEU B N     
5357 C  CA    . LEU B 243 ? 0.33560 0.33620 0.24780 -0.09390 0.02300  -0.02330 243 LEU B CA    
5358 C  C     . LEU B 243 ? 0.32350 0.33650 0.24820 -0.09010 0.03170  -0.02920 243 LEU B C     
5359 O  O     . LEU B 243 ? 0.41330 0.43310 0.34520 -0.08970 0.03770  -0.03120 243 LEU B O     
5360 C  CB    . LEU B 243 ? 0.38850 0.39600 0.30890 -0.08720 0.01690  -0.01890 243 LEU B CB    
5361 C  CG    . LEU B 243 ? 0.43240 0.42890 0.34450 -0.08810 0.01020  -0.01190 243 LEU B CG    
5362 C  CD1   . LEU B 243 ? 0.42970 0.43310 0.35070 -0.08090 0.00560  -0.00840 243 LEU B CD1   
5363 C  CD2   . LEU B 243 ? 0.48550 0.46540 0.37530 -0.10170 0.01390  -0.01330 243 LEU B CD2   
5364 N  N     . LEU B 244 ? 0.32090 0.33700 0.25080 -0.08630 0.03310  -0.03050 244 LEU B N     
5365 C  CA    . LEU B 244 ? 0.37030 0.39850 0.31460 -0.08060 0.04080  -0.03470 244 LEU B CA    
5366 C  C     . LEU B 244 ? 0.33160 0.35770 0.27570 -0.08410 0.05500  -0.03820 244 LEU B C     
5367 O  O     . LEU B 244 ? 0.36790 0.40740 0.33000 -0.08200 0.06180  -0.04200 244 LEU B O     
5368 C  CB    . LEU B 244 ? 0.37430 0.40270 0.32070 -0.07590 0.04030  -0.03460 244 LEU B CB    
5369 C  CG    . LEU B 244 ? 0.32480 0.36590 0.28600 -0.07030 0.04790  -0.03950 244 LEU B CG    
5370 C  CD1   . LEU B 244 ? 0.40080 0.45850 0.37800 -0.06580 0.04380  -0.04080 244 LEU B CD1   
5371 C  CD2   . LEU B 244 ? 0.45960 0.49760 0.41870 -0.06620 0.04780  -0.03900 244 LEU B CD2   
5372 N  N     . TYR B 245 ? 0.39100 0.39980 0.31510 -0.09050 0.06030  -0.03730 245 TYR B N     
5373 C  CA    . TYR B 245 ? 0.41050 0.41260 0.32900 -0.09340 0.07670  -0.04050 245 TYR B CA    
5374 C  C     . TYR B 245 ? 0.39940 0.40110 0.31960 -0.09860 0.08500  -0.04000 245 TYR B C     
5375 O  O     . TYR B 245 ? 0.40400 0.40440 0.32140 -0.10100 0.07720  -0.03660 245 TYR B O     
5376 C  CB    . TYR B 245 ? 0.46800 0.44870 0.35930 -0.09730 0.07850  -0.03940 245 TYR B CB    
5377 C  CG    . TYR B 245 ? 0.46000 0.44240 0.35340 -0.09230 0.07090  -0.03930 245 TYR B CG    
5378 C  CD1   . TYR B 245 ? 0.48970 0.48040 0.39470 -0.08690 0.07840  -0.04420 245 TYR B CD1   
5379 C  CD2   . TYR B 245 ? 0.58760 0.56410 0.47410 -0.09360 0.05700  -0.03450 245 TYR B CD2   
5380 C  CE1   . TYR B 245 ? 0.58010 0.57140 0.48640 -0.08270 0.07240  -0.04420 245 TYR B CE1   
5381 C  CE2   . TYR B 245 ? 0.54710 0.52540 0.43730 -0.09000 0.05170  -0.03410 245 TYR B CE2   
5382 C  CZ    . TYR B 245 ? 0.49960 0.48450 0.39810 -0.08460 0.05940  -0.03900 245 TYR B CZ    
5383 O  OH    . TYR B 245 ? 0.48070 0.46530 0.38060 -0.08150 0.05510  -0.03870 245 TYR B OH    
5384 N  N     . PRO B 246 ? 0.41310 0.41660 0.34080 -0.10010 0.10230  -0.04340 246 PRO B N     
5385 C  CA    . PRO B 246 ? 0.44840 0.45160 0.38100 -0.10580 0.11280  -0.04230 246 PRO B CA    
5386 C  C     . PRO B 246 ? 0.48550 0.46280 0.38340 -0.11370 0.11510  -0.03750 246 PRO B C     
5387 O  O     . PRO B 246 ? 0.45860 0.41880 0.33020 -0.11470 0.10860  -0.03570 246 PRO B O     
5388 C  CB    . PRO B 246 ? 0.44830 0.46040 0.40070 -0.10550 0.13200  -0.04790 246 PRO B CB    
5389 C  CG    . PRO B 246 ? 0.44700 0.45310 0.38880 -0.10150 0.13410  -0.05140 246 PRO B CG    
5390 C  CD    . PRO B 246 ? 0.40930 0.41630 0.34440 -0.09680 0.11390  -0.04880 246 PRO B CD    
5391 N  N     . THR B 247 ? 0.45500 0.42970 0.35500 -0.11930 0.12400  -0.03490 247 THR B N     
5392 C  CA    . THR B 247 ? 0.50260 0.45400 0.37200 -0.12620 0.12340  -0.02880 247 THR B CA    
5393 C  C     . THR B 247 ? 0.59630 0.51930 0.42700 -0.13020 0.13180  -0.02780 247 THR B C     
5394 O  O     . THR B 247 ? 0.56190 0.46420 0.36230 -0.13290 0.12110  -0.02300 247 THR B O     
5395 C  CB    . THR B 247 ? 0.51290 0.46840 0.39640 -0.13130 0.13400  -0.02600 247 THR B CB    
5396 O  OG1   . THR B 247 ? 0.43210 0.41030 0.34690 -0.12750 0.12270  -0.02640 247 THR B OG1   
5397 C  CG2   . THR B 247 ? 0.56950 0.49850 0.41920 -0.13830 0.13390  -0.01840 247 THR B CG2   
5398 N  N     . GLU B 248 ? 0.65570 0.57710 0.48770 -0.13050 0.15060  -0.03230 248 GLU B N     
5399 C  CA    . GLU B 248 ? 0.64910 0.54090 0.44100 -0.13390 0.16070  -0.03210 248 GLU B CA    
5400 C  C     . GLU B 248 ? 0.63070 0.51310 0.40350 -0.13040 0.14500  -0.03280 248 GLU B C     
5401 O  O     . GLU B 248 ? 0.65380 0.50760 0.38680 -0.13380 0.14160  -0.02960 248 GLU B O     
5402 C  CB    . GLU B 248 ? 0.72810 0.61980 0.52660 -0.13480 0.18690  -0.03750 248 GLU B CB    
5403 C  CG    . GLU B 248 ? 1.04140 0.95460 0.86940 -0.12760 0.18990  -0.04510 248 GLU B CG    
5404 C  CD    . GLU B 248 ? 1.19400 1.10040 1.02070 -0.12840 0.21610  -0.05070 248 GLU B CD    
5405 O  OE1   . GLU B 248 ? 1.03260 0.92360 0.84560 -0.13500 0.23490  -0.04900 248 GLU B OE1   
5406 O  OE2   . GLU B 248 ? 0.99320 0.90870 0.83260 -0.12250 0.21910  -0.05700 248 GLU B OE2   
5407 N  N     . ASP B 249 ? 0.62920 0.53460 0.43030 -0.12360 0.13500  -0.03630 249 ASP B N     
5408 C  CA    . ASP B 249 ? 0.63160 0.53200 0.42220 -0.12020 0.12020  -0.03650 249 ASP B CA    
5409 C  C     . ASP B 249 ? 0.54470 0.43560 0.32150 -0.12260 0.09980  -0.03000 249 ASP B C     
5410 O  O     . ASP B 249 ? 0.66260 0.53380 0.41310 -0.12400 0.09110  -0.02760 249 ASP B O     
5411 C  CB    . ASP B 249 ? 0.72680 0.65400 0.55210 -0.11230 0.11510  -0.04070 249 ASP B CB    
5412 C  CG    . ASP B 249 ? 0.64690 0.58420 0.48860 -0.10860 0.13320  -0.04730 249 ASP B CG    
5413 O  OD1   . ASP B 249 ? 0.85460 0.78460 0.69080 -0.11240 0.15140  -0.04900 249 ASP B OD1   
5414 O  OD2   . ASP B 249 ? 0.76470 0.71790 0.62750 -0.10210 0.13010  -0.05110 249 ASP B OD2   
5415 N  N     . ARG B 250 ? 0.53170 0.43680 0.32780 -0.12270 0.09200  -0.02730 250 ARG B N     
5416 C  CA    . ARG B 250 ? 0.46940 0.36870 0.25860 -0.12460 0.07370  -0.02120 250 ARG B CA    
5417 C  C     . ARG B 250 ? 0.53360 0.40130 0.28310 -0.13110 0.07420  -0.01600 250 ARG B C     
5418 O  O     . ARG B 250 ? 0.53280 0.38460 0.26360 -0.13220 0.06000  -0.01200 250 ARG B O     
5419 C  CB    . ARG B 250 ? 0.45950 0.37860 0.27450 -0.12310 0.06910  -0.02040 250 ARG B CB    
5420 C  CG    . ARG B 250 ? 0.37290 0.31980 0.22180 -0.11590 0.06510  -0.02470 250 ARG B CG    
5421 C  CD    . ARG B 250 ? 0.34640 0.30710 0.21210 -0.11380 0.05490  -0.02290 250 ARG B CD    
5422 N  NE    . ARG B 250 ? 0.39060 0.34940 0.25610 -0.11750 0.06230  -0.02090 250 ARG B NE    
5423 C  CZ    . ARG B 250 ? 0.37710 0.34910 0.26250 -0.11690 0.07430  -0.02370 250 ARG B CZ    
5424 N  NH1   . ARG B 250 ? 0.40000 0.38800 0.30590 -0.11200 0.07970  -0.02910 250 ARG B NH1   
5425 N  NH2   . ARG B 250 ? 0.38770 0.35700 0.27520 -0.12140 0.08080  -0.02050 250 ARG B NH2   
5426 N  N     . ASN B 251 ? 0.55860 0.41630 0.29590 -0.13510 0.09030  -0.01550 251 ASN B N     
5427 C  CA    . ASN B 251 ? 0.61980 0.44460 0.31570 -0.14110 0.09170  -0.00970 251 ASN B CA    
5428 C  C     . ASN B 251 ? 0.69870 0.49500 0.35580 -0.14230 0.09440  -0.01060 251 ASN B C     
5429 O  O     . ASN B 251 ? 0.71900 0.48550 0.33860 -0.14560 0.08570  -0.00550 251 ASN B O     
5430 C  CB    . ASN B 251 ? 0.62930 0.45080 0.32380 -0.14550 0.10940  -0.00770 251 ASN B CB    
5431 C  CG    . ASN B 251 ? 0.64360 0.47600 0.35530 -0.14620 0.09980  -0.00270 251 ASN B CG    
5432 O  OD1   . ASN B 251 ? 0.67340 0.49200 0.36850 -0.14770 0.08340  0.00270  251 ASN B OD1   
5433 N  ND2   . ASN B 251 ? 0.74340 0.59940 0.48870 -0.14550 0.10940  -0.00480 251 ASN B ND2   
5434 N  N     . ASP B 252 ? 0.69360 0.49760 0.35850 -0.13920 0.10560  -0.01730 252 ASP B N     
5435 C  CA    . ASP B 252 ? 0.78660 0.56610 0.41750 -0.13890 0.10650  -0.01940 252 ASP B CA    
5436 C  C     . ASP B 252 ? 0.78180 0.55440 0.40470 -0.13740 0.08160  -0.01620 252 ASP B C     
5437 O  O     . ASP B 252 ? 0.75840 0.49910 0.34060 -0.13980 0.07370  -0.01350 252 ASP B O     
5438 C  CB    . ASP B 252 ? 0.77570 0.57030 0.42480 -0.13450 0.12150  -0.02760 252 ASP B CB    
5439 C  CG    . ASP B 252 ? 0.81850 0.60250 0.45520 -0.13720 0.14870  -0.03100 252 ASP B CG    
5440 O  OD1   . ASP B 252 ? 0.93040 0.69520 0.54380 -0.14270 0.15710  -0.02660 252 ASP B OD1   
5441 O  OD2   . ASP B 252 ? 1.08480 0.87920 0.73580 -0.13360 0.16280  -0.03790 252 ASP B OD2   
5442 N  N     . ARG B 253 ? 0.67320 0.47420 0.33470 -0.13350 0.06940  -0.01620 253 ARG B N     
5443 C  CA    . ARG B 253 ? 0.69770 0.49730 0.36140 -0.13230 0.04750  -0.01280 253 ARG B CA    
5444 C  C     . ARG B 253 ? 0.64870 0.43100 0.29570 -0.13640 0.03220  -0.00500 253 ARG B C     
5445 O  O     . ARG B 253 ? 0.65770 0.41670 0.27900 -0.13730 0.01720  -0.00150 253 ARG B O     
5446 C  CB    . ARG B 253 ? 0.68730 0.52180 0.39690 -0.12720 0.04330  -0.01470 253 ARG B CB    
5447 C  CG    . ARG B 253 ? 0.82140 0.65780 0.53880 -0.12550 0.02500  -0.01100 253 ARG B CG    
5448 C  CD    . ARG B 253 ? 1.06270 0.92720 0.81520 -0.11990 0.02750  -0.01460 253 ARG B CD    
5449 N  NE    . ARG B 253 ? 1.27690 1.15420 1.05140 -0.11830 0.01370  -0.00950 253 ARG B NE    
5450 C  CZ    . ARG B 253 ? 0.95470 0.85760 0.76180 -0.11380 0.01490  -0.01060 253 ARG B CZ    
5451 N  NH1   . ARG B 253 ? 0.72260 0.64130 0.54540 -0.10990 0.02630  -0.01710 253 ARG B NH1   
5452 N  NH2   . ARG B 253 ? 0.65970 0.57080 0.48220 -0.11260 0.00450  -0.00480 253 ARG B NH2   
5453 N  N     . LEU B 254 ? 0.61020 0.40210 0.27040 -0.13830 0.03490  -0.00250 254 LEU B N     
5454 C  CA    . LEU B 254 ? 0.62070 0.39660 0.26660 -0.14190 0.02090  0.00480  254 LEU B CA    
5455 C  C     . LEU B 254 ? 0.72450 0.45870 0.31770 -0.14610 0.02010  0.00840  254 LEU B C     
5456 O  O     . LEU B 254 ? 0.79560 0.50830 0.36870 -0.14730 0.00100  0.01400  254 LEU B O     
5457 C  CB    . LEU B 254 ? 0.58610 0.37950 0.25420 -0.14290 0.02630  0.00580  254 LEU B CB    
5458 C  CG    . LEU B 254 ? 0.53180 0.36170 0.24670 -0.13860 0.02260  0.00320  254 LEU B CG    
5459 C  CD1   . LEU B 254 ? 0.57320 0.41660 0.30380 -0.13910 0.02930  0.00330  254 LEU B CD1   
5460 C  CD2   . LEU B 254 ? 0.54900 0.38150 0.27540 -0.13770 0.00240  0.00770  254 LEU B CD2   
5461 N  N     . ARG B 255 ? 0.66450 0.38630 0.23520 -0.14790 0.04070  0.00540  255 ARG B N     
5462 C  CA    . ARG B 255 ? 0.78500 0.46360 0.29940 -0.15180 0.04430  0.00820  255 ARG B CA    
5463 C  C     . ARG B 255 ? 0.79400 0.44990 0.28030 -0.15000 0.02990  0.00710  255 ARG B C     
5464 O  O     . ARG B 255 ? 0.88680 0.50850 0.33430 -0.15190 0.01420  0.01230  255 ARG B O     
5465 C  CB    . ARG B 255 ? 0.96940 0.64230 0.47020 -0.15360 0.07320  0.00430  255 ARG B CB    
5466 C  CG    . ARG B 255 ? 1.22880 0.90750 0.73830 -0.15710 0.08800  0.00770  255 ARG B CG    
5467 C  CD    . ARG B 255 ? 1.54110 1.21580 1.04260 -0.15890 0.11820  0.00370  255 ARG B CD    
5468 N  NE    . ARG B 255 ? 1.60340 1.30250 1.13960 -0.16050 0.13330  0.00440  255 ARG B NE    
5469 C  CZ    . ARG B 255 ? 1.32550 1.04360 0.88770 -0.16040 0.15640  -0.00120 255 ARG B CZ    
5470 N  NH1   . ARG B 255 ? 1.31590 1.03230 0.87360 -0.15820 0.16850  -0.00830 255 ARG B NH1   
5471 N  NH2   . ARG B 255 ? 1.19880 0.93770 0.79330 -0.16230 0.16710  0.00010  255 ARG B NH2   
5472 N  N     . ASP B 256 ? 0.89160 0.56470 0.39630 -0.14620 0.03440  0.00060  256 ASP B N     
5473 C  CA    . ASP B 256 ? 0.91040 0.56350 0.38970 -0.14420 0.02290  -0.00170 256 ASP B CA    
5474 C  C     . ASP B 256 ? 0.85350 0.50350 0.33910 -0.14290 -0.00670 0.00340  256 ASP B C     
5475 O  O     . ASP B 256 ? 0.89390 0.51160 0.34210 -0.14310 -0.02240 0.00490  256 ASP B O     
5476 C  CB    . ASP B 256 ? 0.98010 0.65570 0.48300 -0.14010 0.03490  -0.00990 256 ASP B CB    
5477 C  CG    . ASP B 256 ? 1.31640 0.96720 0.78630 -0.13830 0.02750  -0.01400 256 ASP B CG    
5478 O  OD1   . ASP B 256 ? 1.66410 1.27620 1.08220 -0.14080 0.02940  -0.01400 256 ASP B OD1   
5479 O  OD2   . ASP B 256 ? 1.51430 1.18270 1.00810 -0.13440 0.01980  -0.01740 256 ASP B OD2   
5480 N  N     . SER B 257 ? 0.78800 0.47060 0.32070 -0.14120 -0.01430 0.00600  257 SER B N     
5481 C  CA    . SER B 257 ? 0.79490 0.48120 0.34420 -0.13900 -0.03950 0.01070  257 SER B CA    
5482 C  C     . SER B 257 ? 0.79490 0.46840 0.33940 -0.14120 -0.05640 0.01890  257 SER B C     
5483 O  O     . SER B 257 ? 0.89510 0.55290 0.43220 -0.13990 -0.07990 0.02300  257 SER B O     
5484 C  CB    . SER B 257 ? 0.76870 0.49620 0.37110 -0.13510 -0.03730 0.00910  257 SER B CB    
5485 O  OG    . SER B 257 ? 0.82710 0.56350 0.43330 -0.13220 -0.02690 0.00200  257 SER B OG    
5486 N  N     . TYR B 258 ? 0.77230 0.45210 0.32230 -0.14420 -0.04540 0.02080  258 TYR B N     
5487 C  CA    . TYR B 258 ? 0.81490 0.48800 0.36750 -0.14600 -0.05950 0.02820  258 TYR B CA    
5488 C  C     . TYR B 258 ? 0.85370 0.49680 0.36430 -0.15050 -0.05180 0.03090  258 TYR B C     
5489 O  O     . TYR B 258 ? 0.84430 0.47740 0.35140 -0.15200 -0.06370 0.03720  258 TYR B O     
5490 C  CB    . TYR B 258 ? 0.71340 0.42540 0.31700 -0.14480 -0.05550 0.02840  258 TYR B CB    
5491 C  CG    . TYR B 258 ? 0.71700 0.45630 0.35830 -0.14010 -0.06020 0.02680  258 TYR B CG    
5492 C  CD1   . TYR B 258 ? 0.79040 0.52530 0.44080 -0.13700 -0.08210 0.03180  258 TYR B CD1   
5493 C  CD2   . TYR B 258 ? 0.68320 0.45150 0.35080 -0.13790 -0.04300 0.02060  258 TYR B CD2   
5494 C  CE1   . TYR B 258 ? 0.80490 0.56410 0.48830 -0.13190 -0.08470 0.03110  258 TYR B CE1   
5495 C  CE2   . TYR B 258 ? 0.68480 0.47550 0.38290 -0.13330 -0.04630 0.02000  258 TYR B CE2   
5496 C  CZ    . TYR B 258 ? 0.85050 0.63690 0.55560 -0.13030 -0.06610 0.02550  258 TYR B CZ    
5497 O  OH    . TYR B 258 ? 0.74730 0.55560 0.48130 -0.12490 -0.06800 0.02510  258 TYR B OH    
5498 N  N     . PHE B 259 ? 0.83180 0.46000 0.31160 -0.15220 -0.03220 0.02680  259 PHE B N     
5499 C  CA    . PHE B 259 ? 0.91190 0.50540 0.34410 -0.15630 -0.02300 0.03010  259 PHE B CA    
5500 C  C     . PHE B 259 ? 0.86100 0.46470 0.30660 -0.15910 -0.01380 0.03430  259 PHE B C     
5501 O  O     . PHE B 259 ? 0.92050 0.49590 0.33540 -0.16160 -0.02090 0.04120  259 PHE B O     
5502 C  CB    . PHE B 259 ? 1.01000 0.55920 0.39490 -0.15660 -0.04660 0.03540  259 PHE B CB    
5503 C  CG    . PHE B 259 ? 1.10590 0.64140 0.47290 -0.15390 -0.05590 0.03100  259 PHE B CG    
5504 C  CD1   . PHE B 259 ? 1.15450 0.66510 0.47890 -0.15490 -0.03980 0.02650  259 PHE B CD1   
5505 C  CD2   . PHE B 259 ? 1.11960 0.66820 0.51430 -0.15010 -0.07920 0.03110  259 PHE B CD2   
5506 C  CE1   . PHE B 259 ? 1.26840 0.76570 0.57510 -0.15220 -0.04860 0.02160  259 PHE B CE1   
5507 C  CE2   . PHE B 259 ? 1.17120 0.70770 0.55050 -0.14740 -0.08820 0.02670  259 PHE B CE2   
5508 C  CZ    . PHE B 259 ? 1.22800 0.73880 0.56250 -0.14850 -0.07340 0.02160  259 PHE B CZ    
5509 N  N     . PHE B 260 ? 0.86140 0.50450 0.35220 -0.15810 0.00140  0.03000  260 PHE B N     
5510 C  CA    . PHE B 260 ? 0.84780 0.50270 0.35310 -0.16050 0.01350  0.03270  260 PHE B CA    
5511 C  C     . PHE B 260 ? 0.82650 0.51620 0.36830 -0.15920 0.03650  0.02570  260 PHE B C     
5512 O  O     . PHE B 260 ? 0.82840 0.53870 0.39270 -0.15560 0.03840  0.01910  260 PHE B O     
5513 C  CB    . PHE B 260 ? 0.83330 0.50080 0.36440 -0.15950 -0.00630 0.03760  260 PHE B CB    
5514 C  CG    . PHE B 260 ? 0.74480 0.45360 0.32840 -0.15560 -0.01050 0.03260  260 PHE B CG    
5515 C  CD1   . PHE B 260 ? 0.77040 0.48500 0.36710 -0.15250 -0.02700 0.03150  260 PHE B CD1   
5516 C  CD2   . PHE B 260 ? 0.69470 0.43470 0.31350 -0.15460 0.00240  0.02950  260 PHE B CD2   
5517 C  CE1   . PHE B 260 ? 0.69410 0.44420 0.33630 -0.14900 -0.02880 0.02800  260 PHE B CE1   
5518 C  CE2   . PHE B 260 ? 0.67670 0.45130 0.33840 -0.15050 -0.00160 0.02480  260 PHE B CE2   
5519 C  CZ    . PHE B 260 ? 0.60980 0.38890 0.28220 -0.14790 -0.01640 0.02430  260 PHE B CZ    
5520 N  N     . THR B 261 ? 0.96780 0.66230 0.51540 -0.16190 0.05340  0.02780  261 THR B N     
5521 C  CA    . THR B 261 ? 0.80260 0.53020 0.38930 -0.16060 0.07290  0.02220  261 THR B CA    
5522 C  C     . THR B 261 ? 0.70570 0.45870 0.32920 -0.15940 0.06540  0.02430  261 THR B C     
5523 O  O     . THR B 261 ? 0.74490 0.48390 0.35670 -0.16270 0.06240  0.03160  261 THR B O     
5524 C  CB    . THR B 261 ? 0.86030 0.57310 0.42820 -0.16530 0.09970  0.02370  261 THR B CB    
5525 O  OG1   . THR B 261 ? 1.01500 0.69910 0.54200 -0.16650 0.10750  0.02190  261 THR B OG1   
5526 C  CG2   . THR B 261 ? 0.90780 0.65500 0.52050 -0.16410 0.11870  0.01800  261 THR B CG2   
5527 N  N     . CYS B 262 ? 0.68980 0.47800 0.35580 -0.15440 0.06250  0.01790  262 CYS B N     
5528 C  CA    . CYS B 262 ? 0.62540 0.43820 0.32580 -0.15210 0.05520  0.01850  262 CYS B CA    
5529 C  C     . CYS B 262 ? 0.61230 0.43430 0.32920 -0.15470 0.07330  0.01990  262 CYS B C     
5530 O  O     . CYS B 262 ? 0.64050 0.46640 0.36210 -0.15610 0.09270  0.01670  262 CYS B O     
5531 C  CB    . CYS B 262 ? 0.63670 0.48070 0.37210 -0.14560 0.04820  0.01120  262 CYS B CB    
5532 S  SG    . CYS B 262 ? 0.58060 0.45060 0.35110 -0.14160 0.03800  0.01140  262 CYS B SG    
5533 N  N     . GLU B 263 ? 0.53480 0.35960 0.26270 -0.15570 0.06690  0.02510  263 GLU B N     
5534 C  CA    . GLU B 263 ? 0.54430 0.37730 0.29270 -0.15900 0.08160  0.02770  263 GLU B CA    
5535 C  C     . GLU B 263 ? 0.48930 0.35000 0.27770 -0.15470 0.07340  0.02550  263 GLU B C     
5536 O  O     . GLU B 263 ? 0.47990 0.34240 0.28410 -0.15790 0.07830  0.02960  263 GLU B O     
5537 C  CB    . GLU B 263 ? 0.61050 0.41200 0.32840 -0.16580 0.08500  0.03820  263 GLU B CB    
5538 C  CG    . GLU B 263 ? 0.76340 0.53320 0.43670 -0.17010 0.09550  0.04090  263 GLU B CG    
5539 C  CD    . GLU B 263 ? 0.93960 0.67370 0.57650 -0.17600 0.09650  0.05220  263 GLU B CD    
5540 O  OE1   . GLU B 263 ? 1.08130 0.81580 0.73010 -0.17700 0.08880  0.05840  263 GLU B OE1   
5541 O  OE2   . GLU B 263 ? 0.98060 0.68400 0.57510 -0.17940 0.10490  0.05510  263 GLU B OE2   
5542 N  N     . CYS B 264 ? 0.51860 0.39880 0.32260 -0.14760 0.06120  0.01910  264 CYS B N     
5543 C  CA    . CYS B 264 ? 0.50740 0.41220 0.34500 -0.14210 0.05370  0.01610  264 CYS B CA    
5544 C  C     . CYS B 264 ? 0.49480 0.41940 0.36530 -0.14230 0.06780  0.01180  264 CYS B C     
5545 O  O     . CYS B 264 ? 0.49680 0.41950 0.36670 -0.14620 0.08350  0.01060  264 CYS B O     
5546 C  CB    . CYS B 264 ? 0.48210 0.40080 0.32480 -0.13450 0.03970  0.01080  264 CYS B CB    
5547 S  SG    . CYS B 264 ? 0.49500 0.43340 0.35360 -0.12950 0.04740  0.00150  264 CYS B SG    
5548 N  N     . GLN B 265 ? 0.49870 0.44140 0.39870 -0.13850 0.06170  0.00950  265 GLN B N     
5549 C  CA    . GLN B 265 ? 0.60370 0.56530 0.53950 -0.13930 0.07050  0.00520  265 GLN B CA    
5550 C  C     . GLN B 265 ? 0.45050 0.42730 0.39700 -0.13610 0.07820  -0.00190 265 GLN B C     
5551 O  O     . GLN B 265 ? 0.52090 0.50450 0.48600 -0.14060 0.09180  -0.00340 265 GLN B O     
5552 C  CB    . GLN B 265 ? 0.56540 0.54100 0.52740 -0.13460 0.05880  0.00270  265 GLN B CB    
5553 C  CG    . GLN B 265 ? 0.78800 0.77890 0.78840 -0.13800 0.06400  -0.00080 265 GLN B CG    
5554 C  CD    . GLN B 265 ? 0.94120 0.93960 0.96350 -0.13460 0.05070  -0.00350 265 GLN B CD    
5555 O  OE1   . GLN B 265 ? 0.99840 1.00080 1.01470 -0.12620 0.03960  -0.00650 265 GLN B OE1   
5556 N  NE2   . GLN B 265 ? 1.13490 1.13390 1.18250 -0.14150 0.05180  -0.00280 265 GLN B NE2   
5557 N  N     . GLU B 266 ? 0.38970 0.37130 0.32620 -0.12880 0.06960  -0.00590 266 GLU B N     
5558 C  CA    . GLU B 266 ? 0.40300 0.39660 0.34780 -0.12530 0.07540  -0.01250 266 GLU B CA    
5559 C  C     . GLU B 266 ? 0.43220 0.41300 0.36100 -0.13100 0.09120  -0.01210 266 GLU B C     
5560 O  O     . GLU B 266 ? 0.43910 0.43070 0.38640 -0.13150 0.10360  -0.01650 266 GLU B O     
5561 C  CB    . GLU B 266 ? 0.41400 0.41150 0.34880 -0.11740 0.06280  -0.01560 266 GLU B CB    
5562 C  CG    . GLU B 266 ? 0.66000 0.67270 0.61200 -0.11010 0.05100  -0.01750 266 GLU B CG    
5563 C  CD    . GLU B 266 ? 0.74000 0.77250 0.72460 -0.10750 0.05460  -0.02290 266 GLU B CD    
5564 O  OE1   . GLU B 266 ? 0.75990 0.79830 0.75590 -0.10950 0.06540  -0.02620 266 GLU B OE1   
5565 O  OE2   . GLU B 266 ? 0.91590 0.95750 0.91540 -0.10370 0.04610  -0.02410 266 GLU B OE2   
5566 N  N     . CYS B 267 ? 0.50190 0.45850 0.39620 -0.13510 0.09080  -0.00680 267 CYS B N     
5567 C  CA    . CYS B 267 ? 0.55280 0.49110 0.42390 -0.14060 0.10610  -0.00570 267 CYS B CA    
5568 C  C     . CYS B 267 ? 0.58570 0.52170 0.46790 -0.14810 0.12460  -0.00260 267 CYS B C     
5569 O  O     . CYS B 267 ? 0.57730 0.51240 0.46170 -0.15100 0.14260  -0.00540 267 CYS B O     
5570 C  CB    . CYS B 267 ? 0.59560 0.50580 0.42460 -0.14290 0.09780  -0.00030 267 CYS B CB    
5571 S  SG    . CYS B 267 ? 0.57440 0.48770 0.39600 -0.13630 0.08140  -0.00490 267 CYS B SG    
5572 N  N     . THR B 268 ? 0.54320 0.47820 0.43440 -0.15150 0.12070  0.00310  268 THR B N     
5573 C  CA    . THR B 268 ? 0.58080 0.51230 0.48470 -0.16000 0.13690  0.00740  268 THR B CA    
5574 C  C     . THR B 268 ? 0.53940 0.49800 0.48960 -0.16060 0.14670  0.00090  268 THR B C     
5575 O  O     . THR B 268 ? 0.55590 0.51340 0.51440 -0.16670 0.16670  0.00030  268 THR B O     
5576 C  CB    . THR B 268 ? 0.63950 0.56350 0.54540 -0.16330 0.12750  0.01480  268 THR B CB    
5577 O  OG1   . THR B 268 ? 0.68030 0.57810 0.54410 -0.16330 0.11790  0.02090  268 THR B OG1   
5578 C  CG2   . THR B 268 ? 0.61100 0.53060 0.53210 -0.17330 0.14410  0.01990  268 THR B CG2   
5579 N  N     . THR B 269 ? 0.45340 0.43530 0.43340 -0.15420 0.13220  -0.00430 269 THR B N     
5580 C  CA    . THR B 269 ? 0.46930 0.47760 0.49540 -0.15400 0.13590  -0.01070 269 THR B CA    
5581 C  C     . THR B 269 ? 0.45970 0.48070 0.49400 -0.14850 0.14210  -0.01860 269 THR B C     
5582 O  O     . THR B 269 ? 0.44890 0.48600 0.51650 -0.15080 0.15300  -0.02350 269 THR B O     
5583 C  CB    . THR B 269 ? 0.41550 0.44060 0.46770 -0.14920 0.11610  -0.01310 269 THR B CB    
5584 O  OG1   . THR B 269 ? 0.35180 0.37980 0.38940 -0.13900 0.10200  -0.01630 269 THR B OG1   
5585 C  CG2   . THR B 269 ? 0.45600 0.46870 0.50440 -0.15420 0.10920  -0.00610 269 THR B CG2   
5586 N  N     . LYS B 270 ? 0.42450 0.43820 0.43090 -0.14160 0.13440  -0.02000 270 LYS B N     
5587 C  CA    . LYS B 270 ? 0.43730 0.46220 0.45080 -0.13520 0.13650  -0.02700 270 LYS B CA    
5588 C  C     . LYS B 270 ? 0.42610 0.47900 0.48190 -0.12980 0.12810  -0.03340 270 LYS B C     
5589 O  O     . LYS B 270 ? 0.37520 0.44130 0.45130 -0.12690 0.13490  -0.03990 270 LYS B O     
5590 C  CB    . LYS B 270 ? 0.49160 0.50960 0.50220 -0.13990 0.15960  -0.02910 270 LYS B CB    
5591 C  CG    . LYS B 270 ? 0.62880 0.61540 0.59340 -0.14560 0.16930  -0.02350 270 LYS B CG    
5592 C  CD    . LYS B 270 ? 0.68610 0.66600 0.64940 -0.14960 0.19440  -0.02670 270 LYS B CD    
5593 C  CE    . LYS B 270 ? 0.90300 0.84800 0.81440 -0.15420 0.20400  -0.02210 270 LYS B CE    
5594 N  NZ    . LYS B 270 ? 1.17480 1.10240 1.07300 -0.16330 0.21400  -0.01420 270 LYS B NZ    
5595 N  N     . ASP B 271 ? 0.40560 0.46550 0.47330 -0.12840 0.11270  -0.03210 271 ASP B N     
5596 C  CA    . ASP B 271 ? 0.37880 0.46190 0.48480 -0.12470 0.10270  -0.03800 271 ASP B CA    
5597 C  C     . ASP B 271 ? 0.42040 0.51530 0.53050 -0.11500 0.09520  -0.04400 271 ASP B C     
5598 O  O     . ASP B 271 ? 0.49770 0.61230 0.64240 -0.11240 0.09240  -0.05060 271 ASP B O     
5599 C  CB    . ASP B 271 ? 0.41590 0.49890 0.52640 -0.12480 0.08650  -0.03530 271 ASP B CB    
5600 C  CG    . ASP B 271 ? 0.37430 0.46080 0.51160 -0.13430 0.09050  -0.03410 271 ASP B CG    
5601 O  OD1   . ASP B 271 ? 0.44460 0.53480 0.59850 -0.14110 0.10710  -0.03520 271 ASP B OD1   
5602 O  OD2   . ASP B 271 ? 0.43880 0.52370 0.58110 -0.13520 0.07740  -0.03250 271 ASP B OD2   
5603 N  N     . LYS B 272 ? 0.32710 0.40950 0.40350 -0.11020 0.09140  -0.04200 272 LYS B N     
5604 C  CA    . LYS B 272 ? 0.30290 0.39310 0.37910 -0.10170 0.08530  -0.04650 272 LYS B CA    
5605 C  C     . LYS B 272 ? 0.35310 0.44230 0.42760 -0.10110 0.09880  -0.04990 272 LYS B C     
5606 O  O     . LYS B 272 ? 0.39890 0.49600 0.47860 -0.09440 0.09510  -0.05390 272 LYS B O     
5607 C  CB    . LYS B 272 ? 0.31090 0.38960 0.35600 -0.09700 0.07250  -0.04290 272 LYS B CB    
5608 C  CG    . LYS B 272 ? 0.31830 0.40210 0.36910 -0.09400 0.05820  -0.04200 272 LYS B CG    
5609 C  CD    . LYS B 272 ? 0.34460 0.42060 0.36910 -0.08810 0.04780  -0.03960 272 LYS B CD    
5610 C  CE    . LYS B 272 ? 0.45070 0.53320 0.48240 -0.08350 0.03580  -0.03980 272 LYS B CE    
5611 N  NZ    . LYS B 272 ? 0.52830 0.60690 0.53920 -0.07700 0.02880  -0.03770 272 LYS B NZ    
5612 N  N     . ASP B 273 ? 0.42200 0.50020 0.48830 -0.10790 0.11530  -0.04820 273 ASP B N     
5613 C  CA    . ASP B 273 ? 0.41120 0.48380 0.47040 -0.10760 0.12990  -0.05140 273 ASP B CA    
5614 C  C     . ASP B 273 ? 0.41030 0.50460 0.50770 -0.10270 0.13490  -0.05960 273 ASP B C     
5615 O  O     . ASP B 273 ? 0.42050 0.51430 0.51280 -0.09740 0.13650  -0.06290 273 ASP B O     
5616 C  CB    . ASP B 273 ? 0.51210 0.56890 0.55790 -0.11640 0.14900  -0.04880 273 ASP B CB    
5617 C  CG    . ASP B 273 ? 0.52360 0.55280 0.52210 -0.11970 0.14620  -0.04210 273 ASP B CG    
5618 O  OD1   . ASP B 273 ? 0.44750 0.47180 0.42890 -0.11640 0.12850  -0.03900 273 ASP B OD1   
5619 O  OD2   . ASP B 273 ? 0.65010 0.66170 0.62890 -0.12570 0.16210  -0.04040 273 ASP B OD2   
5620 N  N     . LYS B 274 ? 0.37980 0.49290 0.51770 -0.10450 0.13630  -0.06310 274 LYS B N     
5621 C  CA    . LYS B 274 ? 0.36240 0.49720 0.54320 -0.10000 0.14020  -0.07180 274 LYS B CA    
5622 C  C     . LYS B 274 ? 0.37560 0.52340 0.56620 -0.08970 0.12250  -0.07540 274 LYS B C     
5623 O  O     . LYS B 274 ? 0.32390 0.48000 0.53020 -0.08360 0.12640  -0.08110 274 LYS B O     
5624 C  CB    . LYS B 274 ? 0.45500 0.60560 0.67880 -0.10530 0.14430  -0.07510 274 LYS B CB    
5625 C  CG    . LYS B 274 ? 0.51030 0.64960 0.73100 -0.11470 0.16860  -0.07340 274 LYS B CG    
5626 C  CD    . LYS B 274 ? 0.64360 0.79720 0.90820 -0.12150 0.17430  -0.07640 274 LYS B CD    
5627 C  CE    . LYS B 274 ? 0.80420 0.94380 1.06240 -0.13090 0.20170  -0.07430 274 LYS B CE    
5628 N  NZ    . LYS B 274 ? 0.76140 0.91280 1.06210 -0.13900 0.20890  -0.07640 274 LYS B NZ    
5629 N  N     . ALA B 275 ? 0.33030 0.47800 0.51010 -0.08750 0.10390  -0.07200 275 ALA B N     
5630 C  CA    . ALA B 275 ? 0.33270 0.48910 0.51480 -0.07800 0.08770  -0.07460 275 ALA B CA    
5631 C  C     . ALA B 275 ? 0.34330 0.48670 0.49360 -0.07410 0.09070  -0.07260 275 ALA B C     
5632 O  O     . ALA B 275 ? 0.43960 0.59180 0.60010 -0.06610 0.08580  -0.07660 275 ALA B O     
5633 C  CB    . ALA B 275 ? 0.30890 0.46460 0.48210 -0.07720 0.06970  -0.07140 275 ALA B CB    
5634 N  N     . LYS B 276 ? 0.34490 0.46650 0.45780 -0.07960 0.09720  -0.06650 276 LYS B N     
5635 C  CA    . LYS B 276 ? 0.31950 0.42580 0.40130 -0.07720 0.09800  -0.06430 276 LYS B CA    
5636 C  C     . LYS B 276 ? 0.33080 0.43810 0.42170 -0.07500 0.11220  -0.06940 276 LYS B C     
5637 O  O     . LYS B 276 ? 0.38860 0.49250 0.46990 -0.06970 0.10980  -0.07020 276 LYS B O     
5638 C  CB    . LYS B 276 ? 0.37320 0.45590 0.41660 -0.08360 0.09820  -0.05740 276 LYS B CB    
5639 C  CG    . LYS B 276 ? 0.33040 0.40910 0.35940 -0.08320 0.08220  -0.05240 276 LYS B CG    
5640 C  CD    . LYS B 276 ? 0.41810 0.47550 0.41640 -0.08930 0.08180  -0.04640 276 LYS B CD    
5641 C  CE    . LYS B 276 ? 0.37700 0.43150 0.36420 -0.08780 0.06630  -0.04220 276 LYS B CE    
5642 N  NZ    . LYS B 276 ? 0.40930 0.44450 0.37040 -0.09330 0.06430  -0.03700 276 LYS B NZ    
5643 N  N     . VAL B 277 ? 0.32670 0.43820 0.43690 -0.07920 0.12790  -0.07280 277 VAL B N     
5644 C  CA    . VAL B 277 ? 0.36420 0.47620 0.48540 -0.07730 0.14450  -0.07860 277 VAL B CA    
5645 C  C     . VAL B 277 ? 0.38250 0.52050 0.55670 -0.07250 0.14660  -0.08650 277 VAL B C     
5646 O  O     . VAL B 277 ? 0.55330 0.69590 0.75060 -0.07520 0.16360  -0.09110 277 VAL B O     
5647 C  CB    . VAL B 277 ? 0.37360 0.46620 0.47260 -0.08570 0.16370  -0.07690 277 VAL B CB    
5648 C  CG1   . VAL B 277 ? 0.36820 0.45570 0.46850 -0.08320 0.18100  -0.08280 277 VAL B CG1   
5649 C  CG2   . VAL B 277 ? 0.37580 0.44370 0.42650 -0.09030 0.15650  -0.06910 277 VAL B CG2   
5650 N  N     . GLU B 278 ? 0.41580 0.57030 0.61020 -0.06490 0.12870  -0.08840 278 GLU B N     
5651 C  CA    . GLU B 278 ? 0.42160 0.60090 0.66800 -0.05930 0.12380  -0.09590 278 GLU B CA    
5652 C  C     . GLU B 278 ? 0.38560 0.57180 0.65690 -0.05280 0.13540  -0.10310 278 GLU B C     
5653 O  O     . GLU B 278 ? 0.33060 0.50820 0.58270 -0.04720 0.13660  -0.10300 278 GLU B O     
5654 C  CB    . GLU B 278 ? 0.53410 0.72560 0.78980 -0.05150 0.09950  -0.09630 278 GLU B CB    
5655 C  CG    . GLU B 278 ? 0.62350 0.83840 0.93170 -0.04600 0.08840  -0.10380 278 GLU B CG    
5656 C  CD    . GLU B 278 ? 0.78660 1.00930 1.09760 -0.03810 0.06200  -0.10410 278 GLU B CD    
5657 O  OE1   . GLU B 278 ? 0.98660 1.20200 1.26970 -0.03260 0.05440  -0.10080 278 GLU B OE1   
5658 O  OE2   . GLU B 278 ? 1.05400 1.28880 1.39430 -0.03740 0.04860  -0.10790 278 GLU B OE2   
5659 N  N     . ILE B 279 ? 0.39300 0.59450 0.70940 -0.05340 0.14370  -0.10970 279 ILE B N     
5660 C  CA    . ILE B 279 ? 0.45130 0.66100 0.80000 -0.04760 0.15680  -0.11760 279 ILE B CA    
5661 C  C     . ILE B 279 ? 0.50050 0.73430 0.89970 -0.03660 0.13810  -0.12430 279 ILE B C     
5662 O  O     . ILE B 279 ? 0.49310 0.73950 0.91450 -0.03720 0.12180  -0.12500 279 ILE B O     
5663 C  CB    . ILE B 279 ? 0.45760 0.66630 0.82480 -0.05650 0.18140  -0.12060 279 ILE B CB    
5664 C  CG1   . ILE B 279 ? 0.55340 0.73570 0.86750 -0.06730 0.19630  -0.11310 279 ILE B CG1   
5665 C  CG2   . ILE B 279 ? 0.56190 0.77690 0.96120 -0.05060 0.19800  -0.12900 279 ILE B CG2   
5666 C  CD1   . ILE B 279 ? 0.56570 0.72590 0.83060 -0.06490 0.19960  -0.10990 279 ILE B CD1   
5667 N  N     . ARG B 280 ? 0.57860 0.81710 0.99440 -0.02590 0.13890  -0.12920 280 ARG B N     
5668 C  CA    . ARG B 280 ? 0.61640 0.87550 1.08070 -0.01310 0.11960  -0.13580 280 ARG B CA    
5669 C  C     . ARG B 280 ? 0.59000 0.86680 1.11080 -0.01620 0.12440  -0.14310 280 ARG B C     
5670 O  O     . ARG B 280 ? 0.53670 0.80980 1.06480 -0.02410 0.15070  -0.14520 280 ARG B O     
5671 C  CB    . ARG B 280 ? 0.53980 0.79670 1.00810 -0.00120 0.12290  -0.13890 280 ARG B CB    
5672 C  CG    . ARG B 280 ? 0.62030 0.86440 1.04640 0.00550  0.11050  -0.13290 280 ARG B CG    
5673 C  CD    . ARG B 280 ? 0.62300 0.86270 1.05330 0.01720  0.11560  -0.13600 280 ARG B CD    
5674 N  NE    . ARG B 280 ? 0.70090 0.95820 1.18190 0.03090  0.10010  -0.14210 280 ARG B NE    
5675 C  CZ    . ARG B 280 ? 0.89720 1.15420 1.39550 0.04280  0.10290  -0.14610 280 ARG B CZ    
5676 N  NH1   . ARG B 280 ? 1.05580 1.29540 1.52440 0.04250  0.12200  -0.14550 280 ARG B NH1   
5677 N  NH2   . ARG B 280 ? 0.83730 1.10960 1.38220 0.05530  0.08550  -0.15090 280 ARG B NH2   
5678 N  N     . LYS B 281 ? 0.56320 0.85670 1.12100 -0.01010 0.09940  -0.14700 281 LYS B N     
5679 C  CA    . LYS B 281 ? 0.91380 1.22540 1.53190 -0.01180 0.09970  -0.15500 281 LYS B CA    
5680 C  C     . LYS B 281 ? 0.84900 1.17270 1.51310 0.00030  0.09890  -0.16310 281 LYS B C     
5681 O  O     . LYS B 281 ? 0.75520 1.09010 1.44840 0.01190  0.07170  -0.16690 281 LYS B O     
5682 C  CB    . LYS B 281 ? 1.06000 1.38050 1.69370 -0.01160 0.07110  -0.15590 281 LYS B CB    
5683 C  CG    . LYS B 281 ? 0.91460 1.22610 1.51790 -0.02530 0.07570  -0.14980 281 LYS B CG    
5684 C  CD    . LYS B 281 ? 1.10760 1.43110 1.74730 -0.02810 0.05740  -0.15440 281 LYS B CD    
5685 C  CE    . LYS B 281 ? 1.00000 1.33670 1.69650 -0.03470 0.07540  -0.16180 281 LYS B CE    
5686 N  NZ    . LYS B 281 ? 0.92410 1.27220 1.65980 -0.03750 0.05660  -0.16710 281 LYS B NZ    
5687 N  N     . LEU B 282 ? 0.69350 1.01260 1.36090 -0.00180 0.12830  -0.16540 282 LEU B N     
5688 C  CA    . LEU B 282 ? 0.77280 1.10160 1.48260 0.00910  0.13310  -0.17300 282 LEU B CA    
5689 C  C     . LEU B 282 ? 0.78870 1.13730 1.56930 0.00690  0.13850  -0.18230 282 LEU B C     
5690 O  O     . LEU B 282 ? 0.85570 1.20700 1.64700 -0.00520 0.14770  -0.18250 282 LEU B O     
5691 C  CB    . LEU B 282 ? 0.81070 1.12340 1.49060 0.00740  0.16390  -0.17210 282 LEU B CB    
5692 C  CG    . LEU B 282 ? 0.77570 1.06680 1.38810 0.00900  0.16240  -0.16400 282 LEU B CG    
5693 C  CD1   . LEU B 282 ? 0.65910 0.93210 1.24350 0.00550  0.19370  -0.16460 282 LEU B CD1   
5694 C  CD2   . LEU B 282 ? 0.84720 1.14190 1.46180 0.02500  0.13500  -0.16330 282 LEU B CD2   
5695 N  N     . SER B 283 ? 0.89360 1.25530 1.72380 0.01900  0.13290  -0.19000 283 SER B N     
5696 C  CA    . SER B 283 ? 1.02240 1.40410 1.92800 0.01860  0.13840  -0.20020 283 SER B CA    
5697 C  C     . SER B 283 ? 1.06040 1.43790 1.97090 0.00380  0.17800  -0.20150 283 SER B C     
5698 O  O     . SER B 283 ? 0.89970 1.28700 1.84580 -0.00540 0.18190  -0.20470 283 SER B O     
5699 C  CB    . SER B 283 ? 0.95990 1.35140 1.90880 0.03370  0.13510  -0.20730 283 SER B CB    
5700 O  OG    . SER B 283 ? 0.87830 1.26910 1.81530 0.04840  0.09990  -0.20480 283 SER B OG    
5701 N  N     . ASP B 284 ? 1.09290 1.45330 1.96480 0.00190  0.20690  -0.19900 284 ASP B N     
5702 C  CA    . ASP B 284 ? 1.11550 1.46330 1.97140 -0.01180 0.24520  -0.19810 284 ASP B CA    
5703 C  C     . ASP B 284 ? 1.17810 1.50240 1.95470 -0.02110 0.24730  -0.18700 284 ASP B C     
5704 O  O     . ASP B 284 ? 1.22350 1.53110 1.94730 -0.01680 0.24630  -0.18210 284 ASP B O     
5705 C  CB    . ASP B 284 ? 1.09860 1.43920 1.95970 -0.00720 0.27460  -0.20320 284 ASP B CB    
5706 C  CG    . ASP B 284 ? 1.17220 1.50080 2.02890 -0.02010 0.31590  -0.20450 284 ASP B CG    
5707 O  OD1   . ASP B 284 ? 1.29380 1.62510 2.16240 -0.03190 0.32230  -0.20300 284 ASP B OD1   
5708 O  OD2   . ASP B 284 ? 1.00040 1.31520 1.84080 -0.01810 0.34230  -0.20700 284 ASP B OD2   
5709 N  N     . PRO B 285 ? 1.14300 1.46490 1.91000 -0.03360 0.24880  -0.18270 285 PRO B N     
5710 C  CA    . PRO B 285 ? 1.00170 1.30150 1.69610 -0.04210 0.24880  -0.17200 285 PRO B CA    
5711 C  C     . PRO B 285 ? 0.93460 1.20800 1.57550 -0.04650 0.27810  -0.16850 285 PRO B C     
5712 O  O     . PRO B 285 ? 1.11960 1.38830 1.77640 -0.05130 0.30850  -0.17280 285 PRO B O     
5713 C  CB    . PRO B 285 ? 1.00670 1.31000 1.71530 -0.05480 0.25220  -0.17010 285 PRO B CB    
5714 C  CG    . PRO B 285 ? 1.02850 1.35980 1.81760 -0.05040 0.23910  -0.17970 285 PRO B CG    
5715 C  CD    . PRO B 285 ? 1.01390 1.35380 1.84090 -0.04000 0.24940  -0.18800 285 PRO B CD    
5716 N  N     . PRO B 286 ? 0.80440 1.05840 1.38080 -0.04490 0.26990  -0.16120 286 PRO B N     
5717 C  CA    . PRO B 286 ? 0.81260 1.03800 1.33230 -0.04980 0.29380  -0.15770 286 PRO B CA    
5718 C  C     . PRO B 286 ? 0.71740 0.92710 1.21650 -0.06420 0.31760  -0.15400 286 PRO B C     
5719 O  O     . PRO B 286 ? 0.79220 1.00440 1.28680 -0.07130 0.30680  -0.14860 286 PRO B O     
5720 C  CB    . PRO B 286 ? 0.80260 1.01330 1.26320 -0.04720 0.27280  -0.14960 286 PRO B CB    
5721 C  CG    . PRO B 286 ? 0.68300 0.91610 1.17670 -0.03600 0.24210  -0.15140 286 PRO B CG    
5722 C  CD    . PRO B 286 ? 0.61790 0.87510 1.17330 -0.03810 0.23700  -0.15630 286 PRO B CD    
5723 N  N     . LYS B 287 ? 0.78320 0.97570 1.26920 -0.06780 0.34930  -0.15680 287 LYS B N     
5724 C  CA    . LYS B 287 ? 0.98630 1.16070 1.45210 -0.08070 0.37550  -0.15350 287 LYS B CA    
5725 C  C     . LYS B 287 ? 0.99970 1.14430 1.38670 -0.08720 0.37030  -0.14300 287 LYS B C     
5726 O  O     . LYS B 287 ? 1.02240 1.15570 1.36850 -0.08170 0.35570  -0.14020 287 LYS B O     
5727 C  CB    . LYS B 287 ? 1.08550 1.24960 1.56300 -0.08110 0.41210  -0.16070 287 LYS B CB    
5728 C  CG    . LYS B 287 ? 1.21180 1.37000 1.70580 -0.09280 0.44180  -0.16090 287 LYS B CG    
5729 C  CD    . LYS B 287 ? 1.23830 1.35750 1.65810 -0.10220 0.46200  -0.15360 287 LYS B CD    
5730 C  CE    . LYS B 287 ? 1.38870 1.50270 1.81190 -0.11500 0.47510  -0.14830 287 LYS B CE    
5731 N  NZ    . LYS B 287 ? 1.42030 1.49410 1.76680 -0.12340 0.49090  -0.14020 287 LYS B NZ    
5732 N  N     . ALA B 288 ? 0.96540 1.09720 1.33440 -0.09880 0.38190  -0.13730 288 ALA B N     
5733 C  CA    . ALA B 288 ? 1.01430 1.11900 1.31450 -0.10550 0.37480  -0.12680 288 ALA B CA    
5734 C  C     . ALA B 288 ? 1.00800 1.08130 1.24600 -0.10370 0.38310  -0.12550 288 ALA B C     
5735 O  O     . ALA B 288 ? 1.10990 1.16950 1.30050 -0.10250 0.36310  -0.11920 288 ALA B O     
5736 C  CB    . ALA B 288 ? 0.93830 1.03220 1.23360 -0.11770 0.39220  -0.12200 288 ALA B CB    
5737 N  N     . GLU B 289 ? 1.10880 1.17030 1.34860 -0.10350 0.41280  -0.13180 289 GLU B N     
5738 C  CA    . GLU B 289 ? 1.18860 1.21960 1.37300 -0.10120 0.42280  -0.13260 289 GLU B CA    
5739 C  C     . GLU B 289 ? 1.00620 1.04420 1.18310 -0.09050 0.39810  -0.13430 289 GLU B C     
5740 O  O     . GLU B 289 ? 1.11790 1.13210 1.23810 -0.09040 0.38780  -0.13000 289 GLU B O     
5741 C  CB    . GLU B 289 ? 1.12210 1.14430 1.32140 -0.10110 0.45960  -0.14110 289 GLU B CB    
5742 C  CG    . GLU B 289 ? 1.26210 1.24640 1.39630 -0.10050 0.47350  -0.14180 289 GLU B CG    
5743 C  CD    . GLU B 289 ? 1.47230 1.44590 1.61950 -0.10000 0.51200  -0.15060 289 GLU B CD    
5744 O  OE1   . GLU B 289 ? 1.55030 1.53930 1.74850 -0.10360 0.53300  -0.15400 289 GLU B OE1   
5745 O  OE2   . GLU B 289 ? 1.75640 1.70540 1.86330 -0.09600 0.52200  -0.15450 289 GLU B OE2   
5746 N  N     . ALA B 290 ? 0.74700 0.81650 0.98230 -0.08160 0.38860  -0.14060 290 ALA B N     
5747 C  CA    . ALA B 290 ? 0.72220 0.80010 0.95730 -0.07060 0.36620  -0.14230 290 ALA B CA    
5748 C  C     . ALA B 290 ? 0.62080 0.69740 0.82480 -0.07140 0.33500  -0.13320 290 ALA B C     
5749 O  O     . ALA B 290 ? 0.62200 0.68600 0.79060 -0.06700 0.32180  -0.13130 290 ALA B O     
5750 C  CB    . ALA B 290 ? 0.65770 0.76940 0.96450 -0.06080 0.36140  -0.15030 290 ALA B CB    
5751 N  N     . ILE B 291 ? 0.68860 0.77720 0.90670 -0.07730 0.32440  -0.12790 291 ILE B N     
5752 C  CA    . ILE B 291 ? 0.66590 0.75290 0.85670 -0.07890 0.29720  -0.11930 291 ILE B CA    
5753 C  C     . ILE B 291 ? 0.73730 0.79020 0.85960 -0.08520 0.29810  -0.11240 291 ILE B C     
5754 O  O     . ILE B 291 ? 0.65790 0.70220 0.74940 -0.08210 0.27910  -0.10840 291 ILE B O     
5755 C  CB    . ILE B 291 ? 0.73760 0.84210 0.95660 -0.08440 0.28830  -0.11570 291 ILE B CB    
5756 C  CG1   . ILE B 291 ? 0.84180 0.98010 1.13040 -0.07790 0.28260  -0.12300 291 ILE B CG1   
5757 C  CG2   . ILE B 291 ? 0.70600 0.80610 0.89340 -0.08580 0.26210  -0.10690 291 ILE B CG2   
5758 C  CD1   . ILE B 291 ? 0.89490 1.05040 1.21790 -0.08370 0.27640  -0.12160 291 ILE B CD1   
5759 N  N     . ARG B 292 ? 0.70940 0.74190 0.80910 -0.09390 0.32010  -0.11100 292 ARG B N     
5760 C  CA    . ARG B 292 ? 0.82180 0.81850 0.85510 -0.10010 0.32170  -0.10470 292 ARG B CA    
5761 C  C     . ARG B 292 ? 0.85440 0.83280 0.85550 -0.09450 0.32240  -0.10850 292 ARG B C     
5762 O  O     . ARG B 292 ? 0.70640 0.66240 0.65870 -0.09630 0.30870  -0.10320 292 ARG B O     
5763 C  CB    . ARG B 292 ? 0.85760 0.83440 0.87480 -0.10950 0.34880  -0.10350 292 ARG B CB    
5764 C  CG    . ARG B 292 ? 0.91810 0.90900 0.96300 -0.11640 0.34970  -0.09920 292 ARG B CG    
5765 C  CD    . ARG B 292 ? 1.11560 1.07870 1.12850 -0.12650 0.37310  -0.09500 292 ARG B CD    
5766 N  NE    . ARG B 292 ? 1.27510 1.22390 1.28670 -0.12750 0.40630  -0.10170 292 ARG B NE    
5767 C  CZ    . ARG B 292 ? 1.18260 1.14380 1.23920 -0.13030 0.43210  -0.10670 292 ARG B CZ    
5768 N  NH1   . ARG B 292 ? 1.11910 1.10860 1.22830 -0.13280 0.42710  -0.10620 292 ARG B NH1   
5769 N  NH2   . ARG B 292 ? 1.14690 1.09170 1.19710 -0.13070 0.46310  -0.11270 292 ARG B NH2   
5770 N  N     . ASP B 293 ? 0.80730 0.79470 0.83700 -0.08780 0.33740  -0.11770 293 ASP B N     
5771 C  CA    . ASP B 293 ? 0.79120 0.76360 0.79650 -0.08130 0.33860  -0.12260 293 ASP B CA    
5772 C  C     . ASP B 293 ? 0.74410 0.72550 0.74690 -0.07460 0.30920  -0.12010 293 ASP B C     
5773 O  O     . ASP B 293 ? 0.73880 0.69830 0.69890 -0.07390 0.30080  -0.11890 293 ASP B O     
5774 C  CB    . ASP B 293 ? 0.84100 0.82460 0.88570 -0.07440 0.36080  -0.13340 293 ASP B CB    
5775 C  CG    . ASP B 293 ? 1.03830 0.99740 1.06210 -0.07980 0.39440  -0.13750 293 ASP B CG    
5776 O  OD1   . ASP B 293 ? 1.08170 1.00810 1.04760 -0.08700 0.39900  -0.13270 293 ASP B OD1   
5777 O  OD2   . ASP B 293 ? 0.92580 0.89740 0.99150 -0.07640 0.41660  -0.14560 293 ASP B OD2   
5778 N  N     . MET B 294 ? 0.72640 0.73920 0.77520 -0.06980 0.29390  -0.11960 294 MET B N     
5779 C  CA    . MET B 294 ? 0.66560 0.68810 0.71600 -0.06310 0.26790  -0.11690 294 MET B CA    
5780 C  C     . MET B 294 ? 0.62050 0.63000 0.63210 -0.06930 0.24810  -0.10710 294 MET B C     
5781 O  O     . MET B 294 ? 0.63060 0.63290 0.62130 -0.06620 0.23170  -0.10460 294 MET B O     
5782 C  CB    . MET B 294 ? 0.57770 0.63470 0.68570 -0.05600 0.25770  -0.11930 294 MET B CB    
5783 C  CG    . MET B 294 ? 0.64680 0.71210 0.75980 -0.04640 0.23700  -0.11890 294 MET B CG    
5784 S  SD    . MET B 294 ? 0.68950 0.74210 0.79450 -0.03680 0.24580  -0.12680 294 MET B SD    
5785 C  CE    . MET B 294 ? 0.66630 0.74770 0.84010 -0.02740 0.25780  -0.13640 294 MET B CE    
5786 N  N     . VAL B 295 ? 0.58730 0.59380 0.59170 -0.07800 0.25030  -0.10180 295 VAL B N     
5787 C  CA    . VAL B 295 ? 0.67170 0.66510 0.64160 -0.08390 0.23310  -0.09270 295 VAL B CA    
5788 C  C     . VAL B 295 ? 0.72830 0.68830 0.64440 -0.08700 0.23390  -0.09120 295 VAL B C     
5789 O  O     . VAL B 295 ? 0.68370 0.63530 0.57700 -0.08680 0.21450  -0.08650 295 VAL B O     
5790 C  CB    . VAL B 295 ? 0.62630 0.62150 0.60070 -0.09200 0.23810  -0.08800 295 VAL B CB    
5791 C  CG1   . VAL B 295 ? 0.59340 0.56840 0.52610 -0.09830 0.22400  -0.07920 295 VAL B CG1   
5792 C  CG2   . VAL B 295 ? 0.53330 0.56080 0.55840 -0.08920 0.23050  -0.08890 295 VAL B CG2   
5793 N  N     . ARG B 296 ? 0.63340 0.57410 0.53040 -0.08990 0.25690  -0.09550 296 ARG B N     
5794 C  CA    . ARG B 296 ? 0.80600 0.71140 0.64890 -0.09260 0.26070  -0.09580 296 ARG B CA    
5795 C  C     . ARG B 296 ? 0.67530 0.57920 0.51320 -0.08530 0.24870  -0.09960 296 ARG B C     
5796 O  O     . ARG B 296 ? 0.69970 0.58450 0.50160 -0.08720 0.23280  -0.09580 296 ARG B O     
5797 C  CB    . ARG B 296 ? 0.82770 0.71480 0.65680 -0.09530 0.29110  -0.10150 296 ARG B CB    
5798 C  CG    . ARG B 296 ? 1.16090 1.00960 0.93230 -0.09690 0.29570  -0.10330 296 ARG B CG    
5799 C  CD    . ARG B 296 ? 1.35750 1.18240 1.10650 -0.10040 0.32700  -0.10800 296 ARG B CD    
5800 N  NE    . ARG B 296 ? 1.53120 1.35300 1.27990 -0.10840 0.33930  -0.10250 296 ARG B NE    
5801 C  CZ    . ARG B 296 ? 1.34560 1.18990 1.14000 -0.10940 0.35710  -0.10450 296 ARG B CZ    
5802 N  NH1   . ARG B 296 ? 1.20310 1.07590 1.04940 -0.10230 0.36410  -0.11200 296 ARG B NH1   
5803 N  NH2   . ARG B 296 ? 1.37190 1.20960 1.16130 -0.11730 0.36750  -0.09900 296 ARG B NH2   
5804 N  N     . TYR B 297 ? 0.67970 0.60240 0.55390 -0.07710 0.25620  -0.10710 297 TYR B N     
5805 C  CA    . TYR B 297 ? 0.74180 0.66590 0.61870 -0.06880 0.24630  -0.11140 297 TYR B CA    
5806 C  C     . TYR B 297 ? 0.75730 0.68980 0.63440 -0.06830 0.21880  -0.10410 297 TYR B C     
5807 O  O     . TYR B 297 ? 0.67930 0.59510 0.52880 -0.06780 0.20710  -0.10360 297 TYR B O     
5808 C  CB    . TYR B 297 ? 0.69650 0.64430 0.62160 -0.05930 0.25720  -0.11950 297 TYR B CB    
5809 C  CG    . TYR B 297 ? 0.71400 0.66820 0.65000 -0.04990 0.24360  -0.12240 297 TYR B CG    
5810 C  CD1   . TYR B 297 ? 0.83050 0.76440 0.74400 -0.04550 0.24910  -0.12920 297 TYR B CD1   
5811 C  CD2   . TYR B 297 ? 0.80360 0.78180 0.77010 -0.04520 0.22560  -0.11850 297 TYR B CD2   
5812 C  CE1   . TYR B 297 ? 0.88330 0.82090 0.80690 -0.03680 0.23740  -0.13200 297 TYR B CE1   
5813 C  CE2   . TYR B 297 ? 0.74680 0.72780 0.72090 -0.03650 0.21430  -0.12050 297 TYR B CE2   
5814 C  CZ    . TYR B 297 ? 0.94270 0.90350 0.89650 -0.03230 0.22030  -0.12730 297 TYR B CZ    
5815 O  OH    . TYR B 297 ? 0.87250 0.83430 0.83480 -0.02360 0.20980  -0.12940 297 TYR B OH    
5816 N  N     . ALA B 298 ? 0.65190 0.60860 0.55960 -0.06860 0.20940  -0.09910 298 ALA B N     
5817 C  CA    . ALA B 298 ? 0.64330 0.60950 0.55480 -0.06760 0.18580  -0.09250 298 ALA B CA    
5818 C  C     . ALA B 298 ? 0.70270 0.64590 0.57280 -0.07480 0.17280  -0.08580 298 ALA B C     
5819 O  O     . ALA B 298 ? 0.55620 0.49410 0.41590 -0.07320 0.15770  -0.08360 298 ALA B O     
5820 C  CB    . ALA B 298 ? 0.62700 0.61900 0.57280 -0.06750 0.18020  -0.08900 298 ALA B CB    
5821 N  N     . ARG B 299 ? 0.60370 0.53220 0.45100 -0.08250 0.17920  -0.08270 299 ARG B N     
5822 C  CA    . ARG B 299 ? 0.68560 0.59100 0.49420 -0.08930 0.16650  -0.07610 299 ARG B CA    
5823 C  C     . ARG B 299 ? 0.84880 0.72800 0.62190 -0.08900 0.16540  -0.07970 299 ARG B C     
5824 O  O     . ARG B 299 ? 0.82280 0.68860 0.57370 -0.09180 0.14810  -0.07510 299 ARG B O     
5825 C  CB    . ARG B 299 ? 0.71900 0.61200 0.50990 -0.09680 0.17620  -0.07270 299 ARG B CB    
5826 C  CG    . ARG B 299 ? 0.78270 0.69830 0.60440 -0.09820 0.17350  -0.06860 299 ARG B CG    
5827 C  CD    . ARG B 299 ? 0.86110 0.76110 0.66130 -0.10610 0.18040  -0.06400 299 ARG B CD    
5828 N  NE    . ARG B 299 ? 0.84600 0.73070 0.61940 -0.11000 0.16140  -0.05680 299 ARG B NE    
5829 C  CZ    . ARG B 299 ? 0.78930 0.65420 0.53530 -0.11670 0.16220  -0.05160 299 ARG B CZ    
5830 N  NH1   . ARG B 299 ? 0.81770 0.67500 0.55780 -0.12080 0.18250  -0.05240 299 ARG B NH1   
5831 N  NH2   . ARG B 299 ? 0.90280 0.75550 0.62900 -0.11930 0.14300  -0.04540 299 ARG B NH2   
5832 N  N     . ASN B 300 ? 0.75770 0.62940 0.52680 -0.08540 0.18320  -0.08830 300 ASN B N     
5833 C  CA    . ASN B 300 ? 0.90500 0.75040 0.63970 -0.08430 0.18330  -0.09360 300 ASN B CA    
5834 C  C     . ASN B 300 ? 0.76590 0.61870 0.51350 -0.07830 0.16920  -0.09590 300 ASN B C     
5835 O  O     . ASN B 300 ? 0.98220 0.81480 0.70160 -0.07980 0.15680  -0.09620 300 ASN B O     
5836 C  CB    . ASN B 300 ? 1.09740 0.93050 0.82250 -0.08220 0.20910  -0.10260 300 ASN B CB    
5837 C  CG    . ASN B 300 ? 1.08840 0.89890 0.78030 -0.08960 0.22290  -0.10050 300 ASN B CG    
5838 O  OD1   . ASN B 300 ? 1.56560 1.38000 1.26940 -0.08980 0.24600  -0.10390 300 ASN B OD1   
5839 N  ND2   . ASN B 300 ? 1.05550 0.84130 0.70620 -0.09560 0.20930  -0.09460 300 ASN B ND2   
5840 N  N     . VAL B 301 ? 0.78930 0.66940 0.57920 -0.07140 0.17110  -0.09800 301 VAL B N     
5841 C  CA    . VAL B 301 ? 0.81390 0.70060 0.61780 -0.06530 0.15950  -0.09990 301 VAL B CA    
5842 C  C     . VAL B 301 ? 0.63810 0.52730 0.43920 -0.06940 0.13740  -0.09100 301 VAL B C     
5843 O  O     . VAL B 301 ? 0.68840 0.56880 0.48190 -0.06820 0.12620  -0.09190 301 VAL B O     
5844 C  CB    . VAL B 301 ? 0.80050 0.71370 0.64890 -0.05590 0.16640  -0.10390 301 VAL B CB    
5845 C  CG1   . VAL B 301 ? 0.94180 0.88200 0.82140 -0.05640 0.16200  -0.09740 301 VAL B CG1   
5846 C  CG2   . VAL B 301 ? 0.88980 0.80280 0.74630 -0.04910 0.15680  -0.10670 301 VAL B CG2   
5847 N  N     . ILE B 302 ? 0.62210 0.52200 0.42990 -0.07420 0.13190  -0.08300 302 ILE B N     
5848 C  CA    . ILE B 302 ? 0.66010 0.56150 0.46550 -0.07840 0.11270  -0.07440 302 ILE B CA    
5849 C  C     . ILE B 302 ? 0.70610 0.57940 0.47370 -0.08360 0.10270  -0.07370 302 ILE B C     
5850 O  O     . ILE B 302 ? 0.59240 0.46310 0.35950 -0.08410 0.08790  -0.07130 302 ILE B O     
5851 C  CB    . ILE B 302 ? 0.71680 0.63060 0.53280 -0.08250 0.11020  -0.06740 302 ILE B CB    
5852 C  CG1   . ILE B 302 ? 0.73680 0.67970 0.59230 -0.07660 0.11310  -0.06790 302 ILE B CG1   
5853 C  CG2   . ILE B 302 ? 0.66580 0.57470 0.47260 -0.08760 0.09190  -0.05900 302 ILE B CG2   
5854 C  CD1   . ILE B 302 ? 0.85700 0.81200 0.72490 -0.07970 0.11290  -0.06350 302 ILE B CD1   
5855 N  N     . GLU B 303 ? 0.69010 0.54130 0.42600 -0.08710 0.11110  -0.07620 303 GLU B N     
5856 C  CA    . GLU B 303 ? 0.79480 0.61540 0.48960 -0.09130 0.10140  -0.07670 303 GLU B CA    
5857 C  C     . GLU B 303 ? 0.68460 0.49270 0.37010 -0.08710 0.09920  -0.08530 303 GLU B C     
5858 O  O     . GLU B 303 ? 0.71310 0.50840 0.38530 -0.08890 0.08180  -0.08480 303 GLU B O     
5859 C  CB    . GLU B 303 ? 1.08590 0.88330 0.74560 -0.09520 0.11410  -0.07820 303 GLU B CB    
5860 C  CG    . GLU B 303 ? 1.19880 0.99820 0.85640 -0.10080 0.11320  -0.06980 303 GLU B CG    
5861 C  CD    . GLU B 303 ? 1.54790 1.34100 1.19650 -0.10490 0.09000  -0.06150 303 GLU B CD    
5862 O  OE1   . GLU B 303 ? 2.08280 1.85520 1.70600 -0.10560 0.07630  -0.06260 303 GLU B OE1   
5863 O  OE2   . GLU B 303 ? 1.83310 1.64190 1.50150 -0.10700 0.08480  -0.05430 303 GLU B OE2   
5864 N  N     . GLU B 304 ? 0.76120 0.57230 0.45530 -0.08130 0.11670  -0.09400 304 GLU B N     
5865 C  CA    . GLU B 304 ? 0.79620 0.59560 0.48500 -0.07630 0.11670  -0.10370 304 GLU B CA    
5866 C  C     . GLU B 304 ? 0.71490 0.52640 0.42830 -0.07400 0.10150  -0.10190 304 GLU B C     
5867 O  O     . GLU B 304 ? 0.72400 0.51850 0.42450 -0.07400 0.09030  -0.10680 304 GLU B O     
5868 C  CB    . GLU B 304 ? 0.88250 0.68780 0.58540 -0.06920 0.13930  -0.11260 304 GLU B CB    
5869 C  CG    . GLU B 304 ? 1.06130 0.84450 0.73150 -0.07080 0.15650  -0.11830 304 GLU B CG    
5870 C  CD    . GLU B 304 ? 1.18020 0.96650 0.86500 -0.06290 0.17850  -0.12890 304 GLU B CD    
5871 O  OE1   . GLU B 304 ? 1.24870 1.05510 0.97030 -0.05550 0.17910  -0.13160 304 GLU B OE1   
5872 O  OE2   . GLU B 304 ? 1.35140 1.11890 1.01050 -0.06360 0.19560  -0.13450 304 GLU B OE2   
5873 N  N     . PHE B 305 ? 0.63520 0.47460 0.38360 -0.07240 0.10110  -0.09540 305 PHE B N     
5874 C  CA    . PHE B 305 ? 0.60760 0.45730 0.37820 -0.07040 0.08970  -0.09320 305 PHE B CA    
5875 C  C     . PHE B 305 ? 0.65880 0.49910 0.41700 -0.07730 0.06930  -0.08700 305 PHE B C     
5876 O  O     . PHE B 305 ? 0.60880 0.44140 0.37030 -0.07730 0.05840  -0.08930 305 PHE B O     
5877 C  CB    . PHE B 305 ? 0.55360 0.43330 0.36060 -0.06640 0.09400  -0.08810 305 PHE B CB    
5878 C  CG    . PHE B 305 ? 0.50620 0.39240 0.33240 -0.06310 0.08660  -0.08730 305 PHE B CG    
5879 C  CD1   . PHE B 305 ? 0.52810 0.41210 0.36710 -0.05480 0.09380  -0.09500 305 PHE B CD1   
5880 C  CD2   . PHE B 305 ? 0.45910 0.35060 0.28990 -0.06820 0.07310  -0.07900 305 PHE B CD2   
5881 C  CE1   . PHE B 305 ? 0.55630 0.44140 0.41070 -0.05180 0.08820  -0.09390 305 PHE B CE1   
5882 C  CE2   . PHE B 305 ? 0.47870 0.37270 0.32470 -0.06620 0.06840  -0.07830 305 PHE B CE2   
5883 C  CZ    . PHE B 305 ? 0.48160 0.37100 0.33830 -0.05820 0.07620  -0.08560 305 PHE B CZ    
5884 N  N     . ARG B 306 ? 0.68890 0.52910 0.43570 -0.08300 0.06380  -0.07940 306 ARG B N     
5885 C  CA    . ARG B 306 ? 0.75110 0.58310 0.48800 -0.08880 0.04360  -0.07270 306 ARG B CA    
5886 C  C     . ARG B 306 ? 0.72550 0.53030 0.43700 -0.08990 0.03180  -0.08000 306 ARG B C     
5887 O  O     . ARG B 306 ? 0.81130 0.61390 0.53130 -0.09200 0.01400  -0.07840 306 ARG B O     
5888 C  CB    . ARG B 306 ? 0.77360 0.60460 0.49820 -0.09330 0.04210  -0.06500 306 ARG B CB    
5889 C  CG    . ARG B 306 ? 0.87710 0.70420 0.59930 -0.09770 0.02140  -0.05720 306 ARG B CG    
5890 C  CD    . ARG B 306 ? 1.10650 0.93090 0.81760 -0.10170 0.01980  -0.04950 306 ARG B CD    
5891 N  NE    . ARG B 306 ? 1.30240 1.15060 1.03890 -0.10100 0.03140  -0.04530 306 ARG B NE    
5892 C  CZ    . ARG B 306 ? 1.25470 1.10270 0.98510 -0.10220 0.04420  -0.04540 306 ARG B CZ    
5893 N  NH1   . ARG B 306 ? 1.45010 1.27380 1.14600 -0.10460 0.04980  -0.04850 306 ARG B NH1   
5894 N  NH2   . ARG B 306 ? 0.93410 0.80520 0.69220 -0.10100 0.05100  -0.04280 306 ARG B NH2   
5895 N  N     A ARG B 307 ? 0.75820 0.54330 0.44170 -0.08860 0.04140  -0.08830 307 ARG B N     
5896 N  N     B ARG B 307 ? 0.75820 0.54330 0.44170 -0.08860 0.04140  -0.08830 307 ARG B N     
5897 C  CA    A ARG B 307 ? 0.85850 0.61520 0.51450 -0.08910 0.03150  -0.09760 307 ARG B CA    
5898 C  CA    B ARG B 307 ? 0.85850 0.61520 0.51450 -0.08910 0.03150  -0.09760 307 ARG B CA    
5899 C  C     A ARG B 307 ? 0.84600 0.60360 0.52220 -0.08490 0.03070  -0.10590 307 ARG B C     
5900 C  C     B ARG B 307 ? 0.84600 0.60360 0.52220 -0.08490 0.03070  -0.10590 307 ARG B C     
5901 O  O     A ARG B 307 ? 0.73040 0.47710 0.40840 -0.08730 0.01200  -0.10890 307 ARG B O     
5902 O  O     B ARG B 307 ? 0.73040 0.47710 0.40840 -0.08730 0.01200  -0.10890 307 ARG B O     
5903 C  CB    A ARG B 307 ? 0.92790 0.66280 0.54660 -0.08850 0.04580  -0.10420 307 ARG B CB    
5904 C  CB    B ARG B 307 ? 0.92790 0.66280 0.54660 -0.08850 0.04580  -0.10420 307 ARG B CB    
5905 C  CG    A ARG B 307 ? 1.17530 0.87710 0.75780 -0.08960 0.03460  -0.11380 307 ARG B CG    
5906 C  CG    B ARG B 307 ? 1.17530 0.87710 0.75780 -0.08960 0.03460  -0.11380 307 ARG B CG    
5907 C  CD    A ARG B 307 ? 1.18690 0.87410 0.75070 -0.09540 0.00960  -0.10850 307 ARG B CD    
5908 C  CD    B ARG B 307 ? 1.18690 0.87410 0.75070 -0.09540 0.00960  -0.10850 307 ARG B CD    
5909 N  NE    A ARG B 307 ? 1.38540 1.03960 0.91320 -0.09640 -0.00210 -0.11860 307 ARG B NE    
5910 N  NE    B ARG B 307 ? 1.38540 1.03960 0.91320 -0.09640 -0.00210 -0.11860 307 ARG B NE    
5911 C  CZ    A ARG B 307 ? 1.48090 1.12820 1.01890 -0.09640 -0.01870 -0.12670 307 ARG B CZ    
5912 C  CZ    B ARG B 307 ? 1.48090 1.12820 1.01890 -0.09640 -0.01870 -0.12670 307 ARG B CZ    
5913 N  NH1   A ARG B 307 ? 1.48570 1.15580 1.06880 -0.09560 -0.02460 -0.12530 307 ARG B NH1   
5914 N  NH1   B ARG B 307 ? 1.48570 1.15580 1.06880 -0.09560 -0.02460 -0.12530 307 ARG B NH1   
5915 N  NH2   A ARG B 307 ? 1.35720 0.97270 0.85950 -0.09770 -0.02940 -0.13640 307 ARG B NH2   
5916 N  NH2   B ARG B 307 ? 1.35720 0.97270 0.85950 -0.09770 -0.02940 -0.13640 307 ARG B NH2   
5917 N  N     . ALA B 308 ? 0.73820 0.50810 0.43200 -0.07880 0.04970  -0.10960 308 ALA B N     
5918 C  CA    . ALA B 308 ? 0.77010 0.53780 0.48230 -0.07360 0.05190  -0.11750 308 ALA B CA    
5919 C  C     . ALA B 308 ? 0.77610 0.55140 0.51590 -0.07590 0.03650  -0.11290 308 ALA B C     
5920 O  O     . ALA B 308 ? 0.81090 0.57360 0.55960 -0.07460 0.03030  -0.11960 308 ALA B O     
5921 C  CB    . ALA B 308 ? 0.79390 0.57770 0.52560 -0.06570 0.07420  -0.11990 308 ALA B CB    
5922 N  N     . LYS B 309 ? 0.66060 0.45530 0.41530 -0.07950 0.03100  -0.10140 309 LYS B N     
5923 C  CA    . LYS B 309 ? 0.83120 0.63470 0.61420 -0.08200 0.01950  -0.09570 309 LYS B CA    
5924 C  C     . LYS B 309 ? 0.85620 0.64510 0.64110 -0.08750 -0.00280 -0.09730 309 LYS B C     
5925 O  O     . LYS B 309 ? 0.99700 0.78990 0.81100 -0.08960 -0.01130 -0.09420 309 LYS B O     
5926 C  CB    . LYS B 309 ? 0.68780 0.51640 0.48670 -0.08360 0.02160  -0.08390 309 LYS B CB    
5927 C  CG    . LYS B 309 ? 0.93300 0.76510 0.72680 -0.08930 0.00670  -0.07550 309 LYS B CG    
5928 C  CD    . LYS B 309 ? 1.05810 0.91320 0.86240 -0.08940 0.01350  -0.06570 309 LYS B CD    
5929 C  CE    . LYS B 309 ? 0.77670 0.64880 0.61000 -0.08810 0.01690  -0.06160 309 LYS B CE    
5930 N  NZ    . LYS B 309 ? 0.88480 0.77830 0.72800 -0.08870 0.01970  -0.05240 309 LYS B NZ    
5931 N  N     . HIS B 310 ? 1.11760 0.88900 0.87390 -0.08970 -0.01140 -0.10250 310 HIS B N     
5932 C  CA    . HIS B 310 ? 1.18700 0.94480 0.94550 -0.09450 -0.03350 -0.10620 310 HIS B CA    
5933 C  C     . HIS B 310 ? 1.13320 0.87340 0.89930 -0.09390 -0.03690 -0.11800 310 HIS B C     
5934 O  O     . HIS B 310 ? 1.18900 0.92660 0.97850 -0.09870 -0.05320 -0.11940 310 HIS B O     
5935 C  CB    . HIS B 310 ? 1.13690 0.87920 0.85760 -0.09720 -0.04230 -0.10720 310 HIS B CB    
5936 C  CG    . HIS B 310 ? 1.13160 0.88740 0.85060 -0.09930 -0.04570 -0.09480 310 HIS B CG    
5937 N  ND1   . HIS B 310 ? 1.35840 1.12950 1.10730 -0.10220 -0.06060 -0.08640 310 HIS B ND1   
5938 C  CD2   . HIS B 310 ? 1.39960 1.15500 1.09310 -0.09880 -0.03540 -0.08960 310 HIS B CD2   
5939 C  CE1   . HIS B 310 ? 1.22980 1.00850 0.96960 -0.10280 -0.06010 -0.07680 310 HIS B CE1   
5940 N  NE2   . HIS B 310 ? 1.20690 0.97570 0.91330 -0.10130 -0.04510 -0.07830 310 HIS B NE2   
5941 N  N     . TYR B 311 ? 0.89670 0.62570 0.64700 -0.08810 -0.02070 -0.12670 311 TYR B N     
5942 C  CA    . TYR B 311 ? 0.92540 0.63250 0.67610 -0.08650 -0.02300 -0.13990 311 TYR B CA    
5943 C  C     . TYR B 311 ? 1.01080 0.71930 0.77980 -0.07910 -0.00580 -0.14220 311 TYR B C     
5944 O  O     . TYR B 311 ? 1.10510 0.79930 0.89070 -0.07880 -0.01100 -0.14900 311 TYR B O     
5945 C  CB    . TYR B 311 ? 1.16670 0.84990 0.87330 -0.08600 -0.02310 -0.15100 311 TYR B CB    
5946 C  CG    . TYR B 311 ? 1.26770 0.95090 0.94510 -0.08010 -0.00070 -0.15190 311 TYR B CG    
5947 C  CD1   . TYR B 311 ? 1.17660 0.86660 0.83270 -0.08240 0.00270  -0.14340 311 TYR B CD1   
5948 C  CD2   . TYR B 311 ? 1.36810 1.04380 1.04240 -0.07230 0.01790  -0.16120 311 TYR B CD2   
5949 C  CE1   . TYR B 311 ? 1.23600 0.92670 0.87150 -0.07830 0.02480  -0.14390 311 TYR B CE1   
5950 C  CE2   . TYR B 311 ? 1.34830 1.02650 1.00320 -0.06730 0.04000  -0.16220 311 TYR B CE2   
5951 C  CZ    . TYR B 311 ? 1.31010 0.99610 0.94650 -0.07080 0.04390  -0.15350 311 TYR B CZ    
5952 O  OH    . TYR B 311 ? 1.32020 1.00930 0.94330 -0.06700 0.06660  -0.15410 311 TYR B OH    
5953 N  N     . LYS B 312 ? 0.78700 0.51150 0.55620 -0.07330 0.01340  -0.13700 312 LYS B N     
5954 C  CA    . LYS B 312 ? 0.80960 0.53510 0.59610 -0.06460 0.02990  -0.13970 312 LYS B CA    
5955 C  C     . LYS B 312 ? 0.72920 0.46300 0.55200 -0.06520 0.02720  -0.13050 312 LYS B C     
5956 O  O     . LYS B 312 ? 0.60010 0.34760 0.43600 -0.07150 0.01850  -0.12000 312 LYS B O     
5957 C  CB    . LYS B 312 ? 0.90230 0.64360 0.68140 -0.05730 0.05170  -0.13920 312 LYS B CB    
5958 C  CG    . LYS B 312 ? 0.97400 0.70100 0.72390 -0.05360 0.06160  -0.15020 312 LYS B CG    
5959 C  CD    . LYS B 312 ? 0.98060 0.72660 0.73020 -0.04840 0.08250  -0.14800 312 LYS B CD    
5960 C  CE    . LYS B 312 ? 1.11970 0.85050 0.84750 -0.04320 0.09700  -0.15960 312 LYS B CE    
5961 N  NZ    . LYS B 312 ? 1.15920 0.88320 0.90510 -0.03270 0.10620  -0.16890 312 LYS B NZ    
5962 N  N     . SER B 313 ? 0.71750 0.44130 0.55640 -0.05780 0.03570  -0.13380 313 SER B N     
5963 C  CA    . SER B 313 ? 0.76540 0.49110 0.63650 -0.05710 0.03580  -0.12390 313 SER B CA    
5964 C  C     . SER B 313 ? 0.79120 0.54060 0.67240 -0.05230 0.04890  -0.11450 313 SER B C     
5965 O  O     . SER B 313 ? 0.69520 0.45880 0.56470 -0.04680 0.06040  -0.11800 313 SER B O     
5966 C  CB    . SER B 313 ? 0.80400 0.50950 0.68760 -0.04880 0.04130  -0.12910 313 SER B CB    
5967 O  OG    . SER B 313 ? 0.77700 0.48970 0.66090 -0.03540 0.05960  -0.13230 313 SER B OG    
5968 N  N     . PRO B 314 ? 0.66910 0.42400 0.57460 -0.05420 0.04790  -0.10190 314 PRO B N     
5969 C  CA    . PRO B 314 ? 0.67050 0.44510 0.58480 -0.04870 0.05910  -0.09390 314 PRO B CA    
5970 C  C     . PRO B 314 ? 0.63010 0.41180 0.54820 -0.03230 0.07410  -0.09850 314 PRO B C     
5971 O  O     . PRO B 314 ? 0.61010 0.41590 0.52600 -0.02810 0.08030  -0.09810 314 PRO B O     
5972 C  CB    . PRO B 314 ? 0.71250 0.48900 0.65450 -0.04930 0.05510  -0.07680 314 PRO B CB    
5973 C  CG    . PRO B 314 ? 0.71240 0.47340 0.65910 -0.06290 0.04030  -0.07810 314 PRO B CG    
5974 C  CD    . PRO B 314 ? 0.80990 0.55350 0.73750 -0.06140 0.03620  -0.09390 314 PRO B CD    
5975 N  N     . SER B 315 ? 0.69390 0.45640 0.62130 -0.02330 0.07810  -0.10220 315 SER B N     
5976 C  CA    . SER B 315 ? 0.78410 0.55320 0.72170 -0.00620 0.08970  -0.10650 315 SER B CA    
5977 C  C     . SER B 315 ? 0.76540 0.54870 0.68940 -0.00460 0.09650  -0.11840 315 SER B C     
5978 O  O     . SER B 315 ? 0.72640 0.53120 0.66330 0.00600  0.10530  -0.11920 315 SER B O     
5979 C  CB    . SER B 315 ? 0.73640 0.48130 0.68600 0.00240  0.08960  -0.10710 315 SER B CB    
5980 O  OG    . SER B 315 ? 0.94300 0.66950 0.87760 -0.00390 0.08510  -0.11890 315 SER B OG    
5981 N  N     . GLU B 316 ? 0.72340 0.49430 0.62320 -0.01470 0.09150  -0.12630 316 GLU B N     
5982 C  CA    . GLU B 316 ? 0.77200 0.55100 0.65380 -0.01470 0.09890  -0.13500 316 GLU B CA    
5983 C  C     . GLU B 316 ? 0.71930 0.52500 0.59660 -0.01980 0.10130  -0.12880 316 GLU B C     
5984 O  O     . GLU B 316 ? 0.68600 0.50790 0.56590 -0.01500 0.11250  -0.13150 316 GLU B O     
5985 C  CB    . GLU B 316 ? 0.78710 0.54170 0.63990 -0.02320 0.09070  -0.14350 316 GLU B CB    
5986 C  CG    . GLU B 316 ? 0.99480 0.72350 0.84940 -0.01690 0.09070  -0.15320 316 GLU B CG    
5987 C  CD    . GLU B 316 ? 1.03210 0.73560 0.85970 -0.02590 0.07810  -0.16180 316 GLU B CD    
5988 O  OE1   . GLU B 316 ? 0.92820 0.63010 0.74810 -0.03760 0.06240  -0.15690 316 GLU B OE1   
5989 O  OE2   . GLU B 316 ? 1.25140 0.93710 1.06750 -0.02050 0.08280  -0.17390 316 GLU B OE2   
5990 N  N     . LEU B 317 ? 0.60720 0.41690 0.48070 -0.02990 0.09050  -0.12000 317 LEU B N     
5991 C  CA    . LEU B 317 ? 0.58330 0.41730 0.45450 -0.03500 0.09070  -0.11270 317 LEU B CA    
5992 C  C     . LEU B 317 ? 0.56920 0.42950 0.46700 -0.02480 0.09960  -0.10850 317 LEU B C     
5993 O  O     . LEU B 317 ? 0.63750 0.51930 0.53850 -0.02450 0.10470  -0.10690 317 LEU B O     
5994 C  CB    . LEU B 317 ? 0.57720 0.40850 0.44220 -0.04710 0.07590  -0.10460 317 LEU B CB    
5995 C  CG    . LEU B 317 ? 0.61540 0.42790 0.45720 -0.05720 0.06190  -0.10690 317 LEU B CG    
5996 C  CD1   . LEU B 317 ? 0.57790 0.39300 0.42680 -0.06700 0.04610  -0.09740 317 LEU B CD1   
5997 C  CD2   . LEU B 317 ? 0.71740 0.53230 0.53430 -0.05900 0.06560  -0.10960 317 LEU B CD2   
5998 N  N     . LEU B 318 ? 0.57050 0.42720 0.48850 -0.01570 0.10000  -0.10610 318 LEU B N     
5999 C  CA    . LEU B 318 ? 0.63080 0.50990 0.57490 -0.00240 0.10530  -0.10240 318 LEU B CA    
6000 C  C     . LEU B 318 ? 0.63820 0.53010 0.59690 0.00780  0.11460  -0.11000 318 LEU B C     
6001 O  O     . LEU B 318 ? 0.59670 0.51510 0.57330 0.01260  0.11730  -0.10840 318 LEU B O     
6002 C  CB    . LEU B 318 ? 0.53920 0.41030 0.50050 0.00770  0.09850  -0.09190 318 LEU B CB    
6003 C  CG    . LEU B 318 ? 0.56110 0.43610 0.52160 0.00160  0.08700  -0.07490 318 LEU B CG    
6004 C  CD1   . LEU B 318 ? 0.60350 0.46690 0.57700 0.01290  0.08320  -0.06310 318 LEU B CD1   
6005 C  CD2   . LEU B 318 ? 0.55740 0.46180 0.52080 0.00070  0.08460  -0.06870 318 LEU B CD2   
6006 N  N     . GLU B 319 ? 0.72930 0.60140 0.68200 0.01050  0.11890  -0.11860 319 GLU B N     
6007 C  CA    . GLU B 319 ? 0.73460 0.61480 0.70020 0.01940  0.12970  -0.12680 319 GLU B CA    
6008 C  C     . GLU B 319 ? 0.69570 0.59270 0.65270 0.01140  0.13680  -0.12800 319 GLU B C     
6009 O  O     . GLU B 319 ? 0.85060 0.76880 0.83100 0.01800  0.14460  -0.12960 319 GLU B O     
6010 C  CB    . GLU B 319 ? 0.78160 0.63350 0.73530 0.02190  0.13290  -0.13630 319 GLU B CB    
6011 C  CG    . GLU B 319 ? 1.02720 0.88490 1.00180 0.03530  0.14420  -0.14460 319 GLU B CG    
6012 C  CD    . GLU B 319 ? 1.31150 1.13950 1.27760 0.04010  0.14580  -0.15350 319 GLU B CD    
6013 O  OE1   . GLU B 319 ? 1.06370 0.86680 1.00050 0.02990  0.14020  -0.15610 319 GLU B OE1   
6014 O  OE2   . GLU B 319 ? 1.36080 1.19030 1.35080 0.05440  0.15120  -0.15800 319 GLU B OE2   
6015 N  N     . ILE B 320 ? 0.61640 0.50210 0.54130 -0.00270 0.13310  -0.12640 320 ILE B N     
6016 C  CA    . ILE B 320 ? 0.62100 0.51690 0.53380 -0.01090 0.13870  -0.12490 320 ILE B CA    
6017 C  C     . ILE B 320 ? 0.56000 0.48560 0.49510 -0.01100 0.13640  -0.11660 320 ILE B C     
6018 O  O     . ILE B 320 ? 0.51330 0.45410 0.45970 -0.01080 0.14540  -0.11740 320 ILE B O     
6019 C  CB    . ILE B 320 ? 0.61340 0.48950 0.48770 -0.02440 0.13060  -0.12280 320 ILE B CB    
6020 C  CG1   . ILE B 320 ? 0.67680 0.52320 0.52660 -0.02420 0.13280  -0.13290 320 ILE B CG1   
6021 C  CG2   . ILE B 320 ? 0.64400 0.52930 0.50700 -0.03220 0.13480  -0.11840 320 ILE B CG2   
6022 C  CD1   . ILE B 320 ? 0.78450 0.60880 0.59950 -0.03550 0.11910  -0.13160 320 ILE B CD1   
6023 N  N     . CYS B 321 ? 0.62070 0.55250 0.56170 -0.01150 0.12490  -0.10910 321 CYS B N     
6024 C  CA    . CYS B 321 ? 0.54590 0.50420 0.50650 -0.01060 0.12070  -0.10170 321 CYS B CA    
6025 C  C     . CYS B 321 ? 0.49750 0.47610 0.49460 0.00310  0.12620  -0.10540 321 CYS B C     
6026 O  O     . CYS B 321 ? 0.51360 0.51300 0.52760 0.00260  0.12880  -0.10440 321 CYS B O     
6027 C  CB    . CYS B 321 ? 0.57570 0.53330 0.53330 -0.01230 0.10900  -0.09390 321 CYS B CB    
6028 S  SG    . CYS B 321 ? 0.52080 0.46300 0.44560 -0.02920 0.09930  -0.08770 321 CYS B SG    
6029 N  N     . GLU B 322 ? 0.46560 0.43630 0.47670 0.01560  0.12670  -0.10960 322 GLU B N     
6030 C  CA    . GLU B 322 ? 0.48550 0.47340 0.53450 0.03110  0.12850  -0.11300 322 GLU B CA    
6031 C  C     . GLU B 322 ? 0.52760 0.52540 0.59100 0.03130  0.14170  -0.12030 322 GLU B C     
6032 O  O     . GLU B 322 ? 0.51220 0.53420 0.60570 0.03520  0.14250  -0.12050 322 GLU B O     
6033 C  CB    . GLU B 322 ? 0.58060 0.55100 0.63800 0.04470  0.12560  -0.11510 322 GLU B CB    
6034 C  CG    . GLU B 322 ? 0.72250 0.68500 0.77740 0.04950  0.11410  -0.10650 322 GLU B CG    
6035 C  CD    . GLU B 322 ? 0.92080 0.85610 0.97700 0.06040  0.11200  -0.10640 322 GLU B CD    
6036 O  OE1   . GLU B 322 ? 1.19510 1.12840 1.26850 0.07100  0.11540  -0.11270 322 GLU B OE1   
6037 O  OE2   . GLU B 322 ? 0.94780 0.86390 0.98760 0.05740  0.10510  -0.09710 322 GLU B OE2   
6038 N  N     . LEU B 323 ? 0.48230 0.45980 0.52430 0.02700  0.15210  -0.12670 323 LEU B N     
6039 C  CA    . LEU B 323 ? 0.61830 0.59970 0.66900 0.02690  0.16810  -0.13430 323 LEU B CA    
6040 C  C     . LEU B 323 ? 0.56710 0.56260 0.61550 0.01550  0.17360  -0.13090 323 LEU B C     
6041 O  O     . LEU B 323 ? 0.64340 0.65540 0.71950 0.01800  0.18400  -0.13460 323 LEU B O     
6042 C  CB    . LEU B 323 ? 0.60250 0.55470 0.62260 0.02420  0.17740  -0.14180 323 LEU B CB    
6043 C  CG    . LEU B 323 ? 0.79900 0.73580 0.82760 0.03700  0.17640  -0.14810 323 LEU B CG    
6044 C  CD1   . LEU B 323 ? 0.68540 0.59090 0.67820 0.03230  0.18330  -0.15600 323 LEU B CD1   
6045 C  CD2   . LEU B 323 ? 0.70000 0.65490 0.77330 0.05190  0.18310  -0.15300 323 LEU B CD2   
6046 N  N     . SER B 324 ? 0.60860 0.59610 0.62580 0.00310  0.16620  -0.12380 324 SER B N     
6047 C  CA    A SER B 324 ? 0.62440 0.62040 0.63560 -0.00780 0.16960  -0.11940 324 SER B CA    
6048 C  CA    B SER B 324 ? 0.62440 0.62040 0.63560 -0.00780 0.16960  -0.11940 324 SER B CA    
6049 C  C     . SER B 324 ? 0.60910 0.63500 0.65810 -0.00420 0.16410  -0.11590 324 SER B C     
6050 O  O     . SER B 324 ? 0.56580 0.60420 0.63140 -0.00770 0.17310  -0.11720 324 SER B O     
6051 C  CB    A SER B 324 ? 0.54420 0.52410 0.51610 -0.02000 0.15960  -0.11200 324 SER B CB    
6052 C  CB    B SER B 324 ? 0.54420 0.52410 0.51610 -0.02000 0.15960  -0.11200 324 SER B CB    
6053 O  OG    A SER B 324 ? 0.70280 0.69000 0.67840 -0.01930 0.14340  -0.10480 324 SER B OG    
6054 O  OG    B SER B 324 ? 0.70280 0.69000 0.67840 -0.01930 0.14340  -0.10480 324 SER B OG    
6055 N  N     . GLN B 325 ? 0.53980 0.57520 0.60190 0.00280  0.14980  -0.11210 325 GLN B N     
6056 C  CA    . GLN B 325 ? 0.56230 0.62460 0.65970 0.00830  0.14160  -0.10990 325 GLN B CA    
6057 C  C     . GLN B 325 ? 0.56700 0.64650 0.70840 0.01870  0.14870  -0.11750 325 GLN B C     
6058 O  O     . GLN B 325 ? 0.49030 0.58990 0.65960 0.01690  0.14950  -0.11830 325 GLN B O     
6059 C  CB    . GLN B 325 ? 0.49760 0.56210 0.59610 0.01590  0.12560  -0.10490 325 GLN B CB    
6060 C  CG    . GLN B 325 ? 0.53720 0.59480 0.60510 0.00510  0.11670  -0.09630 325 GLN B CG    
6061 C  CD    . GLN B 325 ? 0.73110 0.78830 0.79810 0.01280  0.10450  -0.09180 325 GLN B CD    
6062 O  OE1   . GLN B 325 ? 0.68800 0.76350 0.77950 0.02200  0.09580  -0.09140 325 GLN B OE1   
6063 N  NE2   . GLN B 325 ? 0.59340 0.62860 0.63250 0.00930  0.10320  -0.08890 325 GLN B NE2   
6064 N  N     . GLU B 326 ? 0.58680 0.65730 0.73570 0.02930  0.15330  -0.12330 326 GLU B N     
6065 C  CA    . GLU B 326 ? 0.60090 0.68580 0.79310 0.04040  0.15950  -0.13070 326 GLU B CA    
6066 C  C     . GLU B 326 ? 0.53940 0.63080 0.74170 0.03170  0.17780  -0.13550 326 GLU B C     
6067 O  O     . GLU B 326 ? 0.73030 0.84440 0.97450 0.03440  0.17860  -0.13820 326 GLU B O     
6068 C  CB    . GLU B 326 ? 0.68360 0.75130 0.87410 0.05190  0.16310  -0.13590 326 GLU B CB    
6069 C  CG    . GLU B 326 ? 0.75840 0.84110 0.99740 0.06680  0.16440  -0.14230 326 GLU B CG    
6070 C  CD    . GLU B 326 ? 0.98540 1.04800 1.22030 0.07850  0.16740  -0.14710 326 GLU B CD    
6071 O  OE1   . GLU B 326 ? 1.23910 1.28250 1.44880 0.08180  0.15750  -0.14290 326 GLU B OE1   
6072 O  OE2   . GLU B 326 ? 1.11740 1.18240 1.37550 0.08440  0.18010  -0.15520 326 GLU B OE2   
6073 N  N     . LYS B 327 ? 0.58510 0.65490 0.74860 0.02100  0.19180  -0.13640 327 LYS B N     
6074 C  CA    . LYS B 327 ? 0.67950 0.74930 0.84510 0.01270  0.21170  -0.14040 327 LYS B CA    
6075 C  C     . LYS B 327 ? 0.61080 0.69640 0.78680 0.00300  0.20900  -0.13520 327 LYS B C     
6076 O  O     . LYS B 327 ? 0.58260 0.68350 0.79240 0.00180  0.22000  -0.13920 327 LYS B O     
6077 C  CB    . LYS B 327 ? 0.77000 0.80890 0.88480 0.00430  0.22400  -0.14170 327 LYS B CB    
6078 C  CG    . LYS B 327 ? 0.95490 0.98880 1.06780 -0.00260 0.24760  -0.14640 327 LYS B CG    
6079 C  CD    . LYS B 327 ? 1.11620 1.11650 1.17650 -0.00840 0.25840  -0.14880 327 LYS B CD    
6080 C  CE    . LYS B 327 ? 1.08940 1.08100 1.14340 -0.01480 0.28390  -0.15330 327 LYS B CE    
6081 N  NZ    . LYS B 327 ? 1.10920 1.11250 1.20530 -0.00550 0.30240  -0.16330 327 LYS B NZ    
6082 N  N     . MET B 328 ? 0.52710 0.60810 0.67540 -0.00410 0.19460  -0.12660 328 MET B N     
6083 C  CA    . MET B 328 ? 0.56240 0.65500 0.71590 -0.01320 0.19010  -0.12130 328 MET B CA    
6084 C  C     . MET B 328 ? 0.59360 0.71640 0.79890 -0.00630 0.17980  -0.12290 328 MET B C     
6085 O  O     . MET B 328 ? 0.50390 0.63950 0.73060 -0.01220 0.18340  -0.12320 328 MET B O     
6086 C  CB    . MET B 328 ? 0.51910 0.59930 0.63250 -0.02080 0.17560  -0.11190 328 MET B CB    
6087 C  CG    . MET B 328 ? 0.54980 0.60170 0.61460 -0.03070 0.18310  -0.10940 328 MET B CG    
6088 S  SD    . MET B 328 ? 0.58420 0.62360 0.61020 -0.04010 0.16500  -0.09830 328 MET B SD    
6089 C  CE    . MET B 328 ? 0.47620 0.51790 0.50370 -0.03100 0.14810  -0.09640 328 MET B CE    
6090 N  N     . SER B 329 ? 0.48080 0.61280 0.70610 0.00670  0.16610  -0.12420 329 SER B N     
6091 C  CA    . SER B 329 ? 0.53370 0.69160 0.80430 0.01520  0.15010  -0.12530 329 SER B CA    
6092 C  C     . SER B 329 ? 0.63260 0.80980 0.95510 0.01830  0.15840  -0.13300 329 SER B C     
6093 O  O     . SER B 329 ? 0.70510 0.90330 1.06550 0.02220  0.14430  -0.13420 329 SER B O     
6094 C  CB    . SER B 329 ? 0.50560 0.66390 0.78200 0.03040  0.13350  -0.12450 329 SER B CB    
6095 O  OG    . SER B 329 ? 0.54810 0.70120 0.83880 0.04060  0.14210  -0.13060 329 SER B OG    
6096 N  N     . SER B 330 ? 0.50130 0.67020 0.82550 0.01680  0.18060  -0.13870 330 SER B N     
6097 C  CA    . SER B 330 ? 0.64510 0.83050 1.01820 0.01760  0.19340  -0.14640 330 SER B CA    
6098 C  C     . SER B 330 ? 0.58000 0.77350 0.96200 0.00440  0.19930  -0.14490 330 SER B C     
6099 O  O     . SER B 330 ? 0.70380 0.91630 1.13520 0.00500  0.20300  -0.15040 330 SER B O     
6100 C  CB    . SER B 330 ? 0.59790 0.76890 0.96450 0.01840  0.21860  -0.15280 330 SER B CB    
6101 O  OG    . SER B 330 ? 0.66530 0.81140 0.97880 0.00610  0.23400  -0.14960 330 SER B OG    
6102 N  N     . VAL B 331 ? 0.66780 0.84580 1.00310 -0.00710 0.19940  -0.13740 331 VAL B N     
6103 C  CA    . VAL B 331 ? 0.65560 0.83650 0.99130 -0.01950 0.20420  -0.13450 331 VAL B CA    
6104 C  C     . VAL B 331 ? 0.51900 0.70240 0.83680 -0.02330 0.18230  -0.12680 331 VAL B C     
6105 O  O     . VAL B 331 ? 0.57830 0.77620 0.92170 -0.02720 0.17560  -0.12670 331 VAL B O     
6106 C  CB    . VAL B 331 ? 0.62110 0.77740 0.91630 -0.03070 0.22810  -0.13280 331 VAL B CB    
6107 C  CG1   . VAL B 331 ? 0.65050 0.80730 0.94420 -0.04290 0.23290  -0.12890 331 VAL B CG1   
6108 C  CG2   . VAL B 331 ? 0.68090 0.83430 0.99470 -0.02740 0.25230  -0.14130 331 VAL B CG2   
6109 N  N     . PHE B 332 ? 0.44800 0.61630 0.72280 -0.02220 0.17190  -0.12070 332 PHE B N     
6110 C  CA    . PHE B 332 ? 0.42510 0.59190 0.67680 -0.02620 0.15400  -0.11310 332 PHE B CA    
6111 C  C     . PHE B 332 ? 0.39710 0.58030 0.67050 -0.01530 0.13080  -0.11340 332 PHE B C     
6112 O  O     . PHE B 332 ? 0.50990 0.69450 0.79150 -0.00380 0.12610  -0.11600 332 PHE B O     
6113 C  CB    . PHE B 332 ? 0.41460 0.55530 0.60940 -0.03120 0.15460  -0.10630 332 PHE B CB    
6114 C  CG    . PHE B 332 ? 0.47050 0.59050 0.63390 -0.04210 0.17190  -0.10440 332 PHE B CG    
6115 C  CD1   . PHE B 332 ? 0.48070 0.60510 0.66160 -0.04900 0.18640  -0.10660 332 PHE B CD1   
6116 C  CD2   . PHE B 332 ? 0.42570 0.52040 0.54130 -0.04560 0.17260  -0.10020 332 PHE B CD2   
6117 C  CE1   . PHE B 332 ? 0.47670 0.57950 0.62510 -0.05830 0.20240  -0.10450 332 PHE B CE1   
6118 C  CE2   . PHE B 332 ? 0.43670 0.51030 0.52080 -0.05470 0.18580  -0.09840 332 PHE B CE2   
6119 C  CZ    . PHE B 332 ? 0.49280 0.56970 0.59150 -0.06080 0.20120  -0.10040 332 PHE B CZ    
6120 N  N     . GLU B 333 ? 0.38520 0.57820 0.66520 -0.01830 0.11600  -0.11070 333 GLU B N     
6121 C  CA    . GLU B 333 ? 0.43800 0.64150 0.72620 -0.00910 0.09190  -0.10970 333 GLU B CA    
6122 C  C     . GLU B 333 ? 0.37780 0.56500 0.62080 -0.00880 0.08700  -0.10300 333 GLU B C     
6123 O  O     . GLU B 333 ? 0.38030 0.54870 0.58580 -0.01820 0.09820  -0.09810 333 GLU B O     
6124 C  CB    . GLU B 333 ? 0.54780 0.76260 0.85020 -0.01380 0.07860  -0.10910 333 GLU B CB    
6125 C  CG    . GLU B 333 ? 0.73910 0.97330 1.09440 -0.01110 0.07480  -0.11650 333 GLU B CG    
6126 C  CD    . GLU B 333 ? 0.77800 1.02530 1.16490 0.00470  0.05350  -0.12130 333 GLU B CD    
6127 O  OE1   . GLU B 333 ? 0.92640 1.16770 1.29290 0.01420  0.04150  -0.11840 333 GLU B OE1   
6128 O  OE2   . GLU B 333 ? 1.00170 1.26410 1.43410 0.00800  0.04790  -0.12790 333 GLU B OE2   
6129 N  N     . ASP B 334 ? 0.42110 0.61440 0.66780 0.00260  0.06870  -0.10260 334 ASP B N     
6130 C  CA    . ASP B 334 ? 0.46440 0.64450 0.67390 0.00430  0.06410  -0.09670 334 ASP B CA    
6131 C  C     . ASP B 334 ? 0.52860 0.70000 0.70480 -0.00810 0.06280  -0.09000 334 ASP B C     
6132 O  O     . ASP B 334 ? 0.59270 0.74710 0.73290 -0.01210 0.06610  -0.08400 334 ASP B O     
6133 C  CB    . ASP B 334 ? 0.59500 0.78370 0.81700 0.02110  0.04340  -0.09770 334 ASP B CB    
6134 C  CG    . ASP B 334 ? 0.69840 0.88540 0.93930 0.03530  0.04420  -0.10130 334 ASP B CG    
6135 O  OD1   . ASP B 334 ? 0.56730 0.74990 0.81550 0.03160  0.06180  -0.10460 334 ASP B OD1   
6136 O  OD2   . ASP B 334 ? 0.69280 0.87990 0.93810 0.05130  0.02590  -0.10030 334 ASP B OD2   
6137 N  N     . SER B 335 ? 0.37400 0.55480 0.56320 -0.01370 0.05690  -0.09060 335 SER B N     
6138 C  CA    . SER B 335 ? 0.37000 0.54170 0.53140 -0.02450 0.05490  -0.08440 335 SER B CA    
6139 C  C     . SER B 335 ? 0.32350 0.47740 0.46270 -0.03690 0.07090  -0.08040 335 SER B C     
6140 O  O     . SER B 335 ? 0.35620 0.49840 0.47030 -0.04460 0.06870  -0.07450 335 SER B O     
6141 C  CB    . SER B 335 ? 0.32600 0.51160 0.50910 -0.02420 0.04070  -0.08690 335 SER B CB    
6142 O  OG    . SER B 335 ? 0.43820 0.63110 0.65080 -0.02840 0.04810  -0.09100 335 SER B OG    
6143 N  N     . ASN B 336 ? 0.30480 0.45590 0.45330 -0.03740 0.08560  -0.08390 336 ASN B N     
6144 C  CA    . ASN B 336 ? 0.32860 0.46080 0.45260 -0.04700 0.10020  -0.08090 336 ASN B CA    
6145 C  C     . ASN B 336 ? 0.33740 0.44720 0.41830 -0.04960 0.09710  -0.07410 336 ASN B C     
6146 O  O     . ASN B 336 ? 0.36330 0.47010 0.43770 -0.04340 0.09380  -0.07410 336 ASN B O     
6147 C  CB    . ASN B 336 ? 0.31160 0.44580 0.45410 -0.04490 0.11690  -0.08740 336 ASN B CB    
6148 C  CG    . ASN B 336 ? 0.38460 0.49930 0.50170 -0.05400 0.13310  -0.08570 336 ASN B CG    
6149 O  OD1   . ASN B 336 ? 0.41820 0.51160 0.49690 -0.05760 0.13280  -0.08100 336 ASN B OD1   
6150 N  ND2   . ASN B 336 ? 0.41030 0.53180 0.55080 -0.05740 0.14720  -0.08990 336 ASN B ND2   
6151 N  N     . VAL B 337 ? 0.36430 0.45820 0.41870 -0.05830 0.09710  -0.06850 337 VAL B N     
6152 C  CA    . VAL B 337 ? 0.38230 0.45700 0.40240 -0.06090 0.08910  -0.06180 337 VAL B CA    
6153 C  C     . VAL B 337 ? 0.35620 0.41560 0.35860 -0.06020 0.09520  -0.06270 337 VAL B C     
6154 O  O     . VAL B 337 ? 0.39950 0.44780 0.38330 -0.05990 0.08680  -0.05840 337 VAL B O     
6155 C  CB    . VAL B 337 ? 0.42310 0.48440 0.42280 -0.06930 0.08630  -0.05650 337 VAL B CB    
6156 C  CG1   . VAL B 337 ? 0.43330 0.50670 0.44580 -0.06960 0.07780  -0.05520 337 VAL B CG1   
6157 C  CG2   . VAL B 337 ? 0.50970 0.56100 0.50230 -0.07550 0.10170  -0.05840 337 VAL B CG2   
6158 N  N     . TYR B 338 ? 0.34930 0.40820 0.35930 -0.05980 0.11050  -0.06870 338 TYR B N     
6159 C  CA    . TYR B 338 ? 0.39720 0.44090 0.39070 -0.05850 0.11870  -0.07170 338 TYR B CA    
6160 C  C     . TYR B 338 ? 0.37970 0.43200 0.38790 -0.04860 0.11520  -0.07490 338 TYR B C     
6161 O  O     . TYR B 338 ? 0.39650 0.43420 0.38540 -0.04750 0.11330  -0.07450 338 TYR B O     
6162 C  CB    . TYR B 338 ? 0.40970 0.44900 0.40590 -0.06130 0.13800  -0.07740 338 TYR B CB    
6163 C  CG    . TYR B 338 ? 0.44080 0.46760 0.41750 -0.07090 0.14270  -0.07380 338 TYR B CG    
6164 C  CD1   . TYR B 338 ? 0.44950 0.45440 0.39000 -0.07670 0.13540  -0.06830 338 TYR B CD1   
6165 C  CD2   . TYR B 338 ? 0.52220 0.55860 0.51840 -0.07410 0.15410  -0.07580 338 TYR B CD2   
6166 C  CE1   . TYR B 338 ? 0.59640 0.58800 0.51750 -0.08460 0.13940  -0.06490 338 TYR B CE1   
6167 C  CE2   . TYR B 338 ? 0.59810 0.62090 0.57480 -0.08260 0.15990  -0.07220 338 TYR B CE2   
6168 C  CZ    . TYR B 338 ? 0.56700 0.56670 0.50460 -0.08750 0.15230  -0.06660 338 TYR B CZ    
6169 O  OH    . TYR B 338 ? 0.67570 0.66040 0.59260 -0.09530 0.15750  -0.06280 338 TYR B OH    
6170 N  N     . MET B 339 ? 0.34250 0.41720 0.38470 -0.04150 0.11380  -0.07840 339 MET B N     
6171 C  CA    . MET B 339 ? 0.38730 0.47090 0.44460 -0.03050 0.10810  -0.08070 339 MET B CA    
6172 C  C     . MET B 339 ? 0.31700 0.39450 0.35450 -0.03060 0.09410  -0.07330 339 MET B C     
6173 O  O     . MET B 339 ? 0.36410 0.43230 0.39160 -0.02590 0.09230  -0.07290 339 MET B O     
6174 C  CB    . MET B 339 ? 0.33790 0.44760 0.43780 -0.02250 0.10560  -0.08600 339 MET B CB    
6175 C  CG    . MET B 339 ? 0.50280 0.62070 0.63150 -0.02000 0.11950  -0.09400 339 MET B CG    
6176 S  SD    . MET B 339 ? 0.53340 0.64480 0.66950 -0.00840 0.12740  -0.10050 339 MET B SD    
6177 C  CE    . MET B 339 ? 0.50970 0.63780 0.67340 0.00740  0.10920  -0.10100 339 MET B CE    
6178 N  N     . LEU B 340 ? 0.32680 0.40830 0.35960 -0.03600 0.08520  -0.06770 340 LEU B N     
6179 C  CA    . LEU B 340 ? 0.36020 0.43630 0.37620 -0.03670 0.07280  -0.06000 340 LEU B CA    
6180 C  C     . LEU B 340 ? 0.30270 0.35640 0.29100 -0.04190 0.07110  -0.05520 340 LEU B C     
6181 O  O     . LEU B 340 ? 0.34360 0.39160 0.32340 -0.03970 0.06480  -0.05070 340 LEU B O     
6182 C  CB    . LEU B 340 ? 0.32280 0.40490 0.33880 -0.04190 0.06490  -0.05610 340 LEU B CB    
6183 C  CG    . LEU B 340 ? 0.33070 0.43620 0.37490 -0.03780 0.06250  -0.06150 340 LEU B CG    
6184 C  CD1   . LEU B 340 ? 0.32480 0.43100 0.36340 -0.04430 0.05560  -0.05810 340 LEU B CD1   
6185 C  CD2   . LEU B 340 ? 0.35190 0.47150 0.40860 -0.02620 0.05600  -0.06390 340 LEU B CD2   
6186 N  N     . HIS B 341 ? 0.37160 0.41280 0.34670 -0.04910 0.07710  -0.05650 341 HIS B N     
6187 C  CA    . HIS B 341 ? 0.37170 0.39260 0.32250 -0.05470 0.07500  -0.05420 341 HIS B CA    
6188 C  C     . HIS B 341 ? 0.38710 0.40070 0.33480 -0.04970 0.07820  -0.05800 341 HIS B C     
6189 O  O     . HIS B 341 ? 0.33070 0.33530 0.26840 -0.05120 0.07140  -0.05460 341 HIS B O     
6190 C  CB    . HIS B 341 ? 0.42760 0.43510 0.36240 -0.06180 0.08320  -0.05680 341 HIS B CB    
6191 C  CG    . HIS B 341 ? 0.39020 0.37610 0.29820 -0.06790 0.07930  -0.05490 341 HIS B CG    
6192 N  ND1   . HIS B 341 ? 0.45920 0.43640 0.35360 -0.07510 0.07030  -0.04890 341 HIS B ND1   
6193 C  CD2   . HIS B 341 ? 0.39790 0.36840 0.29080 -0.06780 0.08220  -0.05890 341 HIS B CD2   
6194 C  CE1   . HIS B 341 ? 0.50300 0.46110 0.37500 -0.07930 0.06730  -0.04880 341 HIS B CE1   
6195 N  NE2   . HIS B 341 ? 0.50400 0.45720 0.37370 -0.07530 0.07400  -0.05500 341 HIS B NE2   
6196 N  N     . MET B 342 ? 0.40070 0.41770 0.35930 -0.04380 0.08950  -0.06580 342 MET B N     
6197 C  CA    . MET B 342 ? 0.41930 0.42730 0.37660 -0.03760 0.09400  -0.07120 342 MET B CA    
6198 C  C     . MET B 342 ? 0.33630 0.35180 0.30570 -0.02920 0.08810  -0.06900 342 MET B C     
6199 O  O     . MET B 342 ? 0.35300 0.35420 0.31370 -0.02730 0.08780  -0.07030 342 MET B O     
6200 C  CB    . MET B 342 ? 0.41610 0.42660 0.38650 -0.03190 0.10800  -0.08040 342 MET B CB    
6201 C  CG    . MET B 342 ? 0.44300 0.44190 0.39700 -0.03950 0.11780  -0.08320 342 MET B CG    
6202 S  SD    . MET B 342 ? 0.61810 0.58670 0.53010 -0.04920 0.11330  -0.08160 342 MET B SD    
6203 C  CE    . MET B 342 ? 0.66670 0.62130 0.57550 -0.04220 0.11400  -0.08840 342 MET B CE    
6204 N  N     . MET B 343 ? 0.38470 0.42000 0.37240 -0.02430 0.08370  -0.06620 343 MET B N     
6205 C  CA    . MET B 343 ? 0.35160 0.39270 0.34560 -0.01600 0.07790  -0.06310 343 MET B CA    
6206 C  C     . MET B 343 ? 0.34200 0.37060 0.31520 -0.02300 0.07070  -0.05400 343 MET B C     
6207 O  O     . MET B 343 ? 0.32930 0.34770 0.29790 -0.01870 0.07060  -0.05140 343 MET B O     
6208 C  CB    . MET B 343 ? 0.32850 0.39330 0.34330 -0.01020 0.07300  -0.06320 343 MET B CB    
6209 C  CG    . MET B 343 ? 0.46770 0.54890 0.51510 0.00090  0.07710  -0.07280 343 MET B CG    
6210 S  SD    . MET B 343 ? 0.56160 0.67270 0.63770 0.00640  0.06650  -0.07500 343 MET B SD    
6211 C  CE    . MET B 343 ? 0.92650 1.05220 1.04410 0.01280  0.07210  -0.08490 343 MET B CE    
6212 N  N     . TYR B 344 ? 0.28770 0.31510 0.25160 -0.03290 0.06430  -0.04840 344 TYR B N     
6213 C  CA    . TYR B 344 ? 0.35860 0.37640 0.31000 -0.03980 0.05650  -0.04040 344 TYR B CA    
6214 C  C     . TYR B 344 ? 0.33780 0.33540 0.27460 -0.04590 0.05970  -0.04380 344 TYR B C     
6215 O  O     . TYR B 344 ? 0.34880 0.33790 0.28070 -0.04810 0.05870  -0.03980 344 TYR B O     
6216 C  CB    . TYR B 344 ? 0.40010 0.42020 0.34930 -0.04720 0.04940  -0.03660 344 TYR B CB    
6217 C  CG    . TYR B 344 ? 0.35310 0.36650 0.29610 -0.05290 0.04130  -0.02990 344 TYR B CG    
6218 C  CD1   . TYR B 344 ? 0.42560 0.44600 0.37570 -0.04800 0.03630  -0.02300 344 TYR B CD1   
6219 C  CD2   . TYR B 344 ? 0.46850 0.46770 0.39800 -0.06330 0.03930  -0.03090 344 TYR B CD2   
6220 C  CE1   . TYR B 344 ? 0.41940 0.43490 0.36780 -0.05240 0.03080  -0.01770 344 TYR B CE1   
6221 C  CE2   . TYR B 344 ? 0.48840 0.48320 0.41460 -0.07000 0.03220  -0.02600 344 TYR B CE2   
6222 C  CZ    . TYR B 344 ? 0.42920 0.43350 0.36700 -0.06380 0.02840  -0.01970 344 TYR B CZ    
6223 O  OH    . TYR B 344 ? 0.57110 0.57270 0.50860 -0.06790 0.02250  -0.01470 344 TYR B OH    
6224 N  N     . GLN B 345 ? 0.38000 0.36790 0.30870 -0.04910 0.06460  -0.05120 345 GLN B N     
6225 C  CA    . GLN B 345 ? 0.45980 0.42490 0.37160 -0.05440 0.06630  -0.05650 345 GLN B CA    
6226 C  C     . GLN B 345 ? 0.42370 0.37980 0.34050 -0.04680 0.07240  -0.06100 345 GLN B C     
6227 O  O     . GLN B 345 ? 0.39100 0.33140 0.30620 -0.04980 0.06590  -0.05720 345 GLN B O     
6228 C  CB    . GLN B 345 ? 0.46980 0.42530 0.36990 -0.05670 0.07140  -0.06290 345 GLN B CB    
6229 C  CG    . GLN B 345 ? 0.49440 0.44800 0.38200 -0.06530 0.06600  -0.05820 345 GLN B CG    
6230 C  CD    . GLN B 345 ? 0.46800 0.41050 0.34300 -0.07390 0.05380  -0.05280 345 GLN B CD    
6231 O  OE1   . GLN B 345 ? 0.53600 0.46210 0.40120 -0.07640 0.04950  -0.05580 345 GLN B OE1   
6232 N  NE2   . GLN B 345 ? 0.49690 0.44740 0.37470 -0.07800 0.04710  -0.04520 345 GLN B NE2   
6233 N  N     . ALA B 346 ? 0.35050 0.31830 0.28430 -0.03460 0.07930  -0.06410 346 ALA B N     
6234 C  CA    . ALA B 346 ? 0.36570 0.32610 0.31310 -0.02250 0.07920  -0.06230 346 ALA B CA    
6235 C  C     . ALA B 346 ? 0.35820 0.31730 0.31050 -0.02000 0.07010  -0.04760 346 ALA B C     
6236 O  O     . ALA B 346 ? 0.40240 0.34350 0.35620 -0.01780 0.06870  -0.04320 346 ALA B O     
6237 C  CB    . ALA B 346 ? 0.37810 0.35430 0.34600 -0.00900 0.08480  -0.06740 346 ALA B CB    
6238 N  N     . MET B 347 ? 0.37560 0.35180 0.32970 -0.02070 0.06570  -0.04020 347 MET B N     
6239 C  CA    . MET B 347 ? 0.36860 0.34280 0.32350 -0.01900 0.06050  -0.02670 347 MET B CA    
6240 C  C     . MET B 347 ? 0.42520 0.38400 0.37690 -0.03030 0.05840  -0.02230 347 MET B C     
6241 O  O     . MET B 347 ? 0.36540 0.31170 0.32240 -0.02770 0.05910  -0.01340 347 MET B O     
6242 C  CB    . MET B 347 ? 0.33860 0.33210 0.29300 -0.01960 0.05680  -0.02260 347 MET B CB    
6243 C  CG    . MET B 347 ? 0.36480 0.35570 0.31710 -0.01460 0.05420  -0.00980 347 MET B CG    
6244 S  SD    . MET B 347 ? 0.35970 0.36990 0.30890 -0.01570 0.04960  -0.00780 347 MET B SD    
6245 C  CE    . MET B 347 ? 0.37820 0.37700 0.31860 -0.00700 0.05060  0.00640  347 MET B CE    
6246 N  N     . GLY B 348 ? 0.34900 0.30720 0.29240 -0.04280 0.05560  -0.02840 348 GLY B N     
6247 C  CA    . GLY B 348 ? 0.37060 0.31480 0.31360 -0.05420 0.04930  -0.02660 348 GLY B CA    
6248 C  C     . GLY B 348 ? 0.35730 0.27950 0.30470 -0.05400 0.04990  -0.02910 348 GLY B C     
6249 O  O     . GLY B 348 ? 0.37910 0.29200 0.33970 -0.05800 0.04710  -0.02190 348 GLY B O     
6250 N  N     . VAL B 349 ? 0.37570 0.28930 0.31490 -0.04930 0.05490  -0.03990 349 VAL B N     
6251 C  CA    . VAL B 349 ? 0.38940 0.27970 0.33150 -0.04770 0.05600  -0.04410 349 VAL B CA    
6252 C  C     . VAL B 349 ? 0.41240 0.29870 0.37110 -0.03790 0.05970  -0.03210 349 VAL B C     
6253 O  O     . VAL B 349 ? 0.40020 0.26840 0.36850 -0.04160 0.05840  -0.02800 349 VAL B O     
6254 C  CB    . VAL B 349 ? 0.46030 0.34290 0.39090 -0.04230 0.06320  -0.05870 349 VAL B CB    
6255 C  CG1   . VAL B 349 ? 0.49080 0.34740 0.42540 -0.03930 0.06440  -0.06330 349 VAL B CG1   
6256 C  CG2   . VAL B 349 ? 0.48970 0.36880 0.39640 -0.05260 0.06210  -0.07000 349 VAL B CG2   
6257 N  N     . CYS B 350 ? 0.37880 0.27980 0.33960 -0.02560 0.06370  -0.02630 350 CYS B N     
6258 C  CA    . CYS B 350 ? 0.41430 0.30810 0.38180 -0.01480 0.06670  -0.01360 350 CYS B CA    
6259 C  C     . CYS B 350 ? 0.41580 0.30580 0.38970 -0.02200 0.06730  -0.00030 350 CYS B C     
6260 O  O     . CYS B 350 ? 0.42820 0.29960 0.40920 -0.02060 0.07180  0.00850  350 CYS B O     
6261 C  CB    . CYS B 350 ? 0.46610 0.37610 0.43070 -0.00080 0.06650  -0.01080 350 CYS B CB    
6262 S  SG    . CYS B 350 ? 0.48560 0.39810 0.45560 0.01210  0.06790  -0.02380 350 CYS B SG    
6263 N  N     . LEU B 351 ? 0.35930 0.26620 0.33280 -0.02980 0.06410  0.00120  351 LEU B N     
6264 C  CA    . LEU B 351 ? 0.38490 0.29160 0.36960 -0.03660 0.06600  0.01250  351 LEU B CA    
6265 C  C     . LEU B 351 ? 0.39150 0.28180 0.39400 -0.04830 0.06410  0.01200  351 LEU B C     
6266 O  O     . LEU B 351 ? 0.46770 0.34800 0.48580 -0.04970 0.07110  0.02300  351 LEU B O     
6267 C  CB    . LEU B 351 ? 0.31120 0.23860 0.29430 -0.04260 0.06140  0.01190  351 LEU B CB    
6268 C  CG    . LEU B 351 ? 0.37920 0.32170 0.34990 -0.03210 0.06340  0.01540  351 LEU B CG    
6269 C  CD1   . LEU B 351 ? 0.37320 0.33330 0.34360 -0.03940 0.05840  0.01340  351 LEU B CD1   
6270 C  CD2   . LEU B 351 ? 0.36080 0.29420 0.32840 -0.02240 0.07210  0.02890  351 LEU B CD2   
6271 N  N     . TYR B 352 ? 0.38280 0.26820 0.38240 -0.05680 0.05490  -0.00100 352 TYR B N     
6272 C  CA    . TYR B 352 ? 0.41250 0.27970 0.42780 -0.06830 0.04860  -0.00480 352 TYR B CA    
6273 C  C     . TYR B 352 ? 0.41280 0.25770 0.43490 -0.06260 0.05620  -0.00190 352 TYR B C     
6274 O  O     . TYR B 352 ? 0.41180 0.25220 0.45480 -0.06650 0.05360  0.00450  352 TYR B O     
6275 C  CB    . TYR B 352 ? 0.49390 0.35510 0.49400 -0.07700 0.03590  -0.02070 352 TYR B CB    
6276 C  CG    . TYR B 352 ? 0.45550 0.30360 0.47160 -0.08510 0.02270  -0.02390 352 TYR B CG    
6277 C  CD1   . TYR B 352 ? 0.50250 0.36210 0.54330 -0.09040 0.01130  -0.01500 352 TYR B CD1   
6278 C  CD2   . TYR B 352 ? 0.56840 0.39380 0.57620 -0.08520 0.02000  -0.03460 352 TYR B CD2   
6279 C  CE1   . TYR B 352 ? 0.56060 0.40710 0.61120 -0.09850 -0.00320 -0.01680 352 TYR B CE1   
6280 C  CE2   . TYR B 352 ? 0.62190 0.43610 0.64500 -0.09150 0.00470  -0.03690 352 TYR B CE2   
6281 C  CZ    . TYR B 352 ? 0.62640 0.44990 0.66950 -0.09920 -0.00790 -0.02750 352 TYR B CZ    
6282 O  OH    . TYR B 352 ? 0.80020 0.60830 0.83990 -0.10950 -0.01570 -0.03170 352 TYR B OH    
6283 N  N     . MET B 353 ? 0.40270 0.24280 0.40830 -0.05020 0.06110  -0.00600 353 MET B N     
6284 C  CA    . MET B 353 ? 0.49390 0.31130 0.50390 -0.04230 0.06800  -0.00220 353 MET B CA    
6285 C  C     . MET B 353 ? 0.44130 0.25430 0.45700 -0.03470 0.07890  0.01660  353 MET B C     
6286 O  O     . MET B 353 ? 0.45680 0.24740 0.47500 -0.02840 0.08530  0.02290  353 MET B O     
6287 C  CB    . MET B 353 ? 0.52090 0.33610 0.51500 -0.02920 0.06950  -0.01190 353 MET B CB    
6288 C  CG    . MET B 353 ? 0.56770 0.37750 0.55200 -0.03500 0.06410  -0.03090 353 MET B CG    
6289 S  SD    . MET B 353 ? 0.59990 0.41330 0.57330 -0.01830 0.07030  -0.04170 353 MET B SD    
6290 C  CE    . MET B 353 ? 0.66590 0.44610 0.64910 -0.00980 0.07420  -0.04010 353 MET B CE    
6291 N  N     . GLN B 354 ? 0.42710 0.25850 0.44130 -0.03460 0.08170  0.02560  354 GLN B N     
6292 C  CA    . GLN B 354 ? 0.46950 0.29930 0.47940 -0.02550 0.09170  0.04190  354 GLN B CA    
6293 C  C     . GLN B 354 ? 0.49480 0.31110 0.48280 -0.00800 0.09520  0.04630  354 GLN B C     
6294 O  O     . GLN B 354 ? 0.59930 0.40010 0.58050 0.00020  0.10210  0.05840  354 GLN B O     
6295 C  CB    . GLN B 354 ? 0.45250 0.27940 0.48200 -0.03050 0.09330  0.04810  354 GLN B CB    
6296 C  CG    . GLN B 354 ? 0.43520 0.27850 0.48820 -0.04470 0.08440  0.04290  354 GLN B CG    
6297 C  CD    . GLN B 354 ? 0.45190 0.29400 0.52550 -0.04850 0.08870  0.04990  354 GLN B CD    
6298 O  OE1   . GLN B 354 ? 0.55040 0.37930 0.61950 -0.04170 0.09970  0.05880  354 GLN B OE1   
6299 N  NE2   . GLN B 354 ? 0.47830 0.33260 0.57380 -0.05930 0.08010  0.04590  354 GLN B NE2   
6300 N  N     . ASP B 355 ? 0.55300 0.38330 0.53150 -0.00150 0.08630  0.03380  355 ASP B N     
6301 C  CA    . ASP B 355 ? 0.56620 0.39460 0.52970 0.01640  0.08370  0.03460  355 ASP B CA    
6302 C  C     . ASP B 355 ? 0.51390 0.36290 0.46410 0.02170  0.08080  0.03840  355 ASP B C     
6303 O  O     . ASP B 355 ? 0.47480 0.34750 0.42580 0.02070  0.07400  0.02760  355 ASP B O     
6304 C  CB    . ASP B 355 ? 0.59420 0.42840 0.56260 0.01960  0.07760  0.01750  355 ASP B CB    
6305 C  CG    . ASP B 355 ? 0.71210 0.54900 0.67430 0.03850  0.07290  0.01680  355 ASP B CG    
6306 O  OD1   . ASP B 355 ? 0.62490 0.45400 0.57400 0.04990  0.07180  0.02990  355 ASP B OD1   
6307 O  OD2   . ASP B 355 ? 0.59370 0.43940 0.56420 0.04240  0.07020  0.00260  355 ASP B OD2   
6308 N  N     . TRP B 356 ? 0.56110 0.39850 0.49760 0.02690  0.08730  0.05390  356 TRP B N     
6309 C  CA    . TRP B 356 ? 0.49070 0.34270 0.41190 0.03030  0.08590  0.05810  356 TRP B CA    
6310 C  C     . TRP B 356 ? 0.46210 0.32290 0.36920 0.04580  0.07360  0.05310  356 TRP B C     
6311 O  O     . TRP B 356 ? 0.45720 0.34060 0.36210 0.04550  0.06670  0.04690  356 TRP B O     
6312 C  CB    . TRP B 356 ? 0.51900 0.35300 0.42660 0.03200  0.09810  0.07440  356 TRP B CB    
6313 C  CG    . TRP B 356 ? 0.53900 0.37500 0.47360 0.01770  0.10490  0.07380  356 TRP B CG    
6314 C  CD1   . TRP B 356 ? 0.57310 0.39340 0.51200 0.01790  0.11200  0.08040  356 TRP B CD1   
6315 C  CD2   . TRP B 356 ? 0.54910 0.40370 0.51040 0.00190  0.10290  0.06630  356 TRP B CD2   
6316 N  NE1   . TRP B 356 ? 0.58280 0.41170 0.55120 0.00390  0.11480  0.07760  356 TRP B NE1   
6317 C  CE2   . TRP B 356 ? 0.55110 0.40070 0.53330 -0.00550 0.10760  0.06890  356 TRP B CE2   
6318 C  CE3   . TRP B 356 ? 0.49660 0.37120 0.46510 -0.00640 0.09620  0.05770  356 TRP B CE3   
6319 C  CZ2   . TRP B 356 ? 0.51110 0.37470 0.52140 -0.01930 0.10330  0.06320  356 TRP B CZ2   
6320 C  CZ3   . TRP B 356 ? 0.51700 0.40410 0.51090 -0.02040 0.09170  0.05220  356 TRP B CZ3   
6321 C  CH2   . TRP B 356 ? 0.46530 0.34660 0.47990 -0.02600 0.09410  0.05510  356 TRP B CH2   
6322 N  N     . GLU B 357 ? 0.46820 0.31080 0.36930 0.05930  0.06970  0.05560  357 GLU B N     
6323 C  CA    . GLU B 357 ? 0.54920 0.39900 0.44440 0.07530  0.05530  0.05050  357 GLU B CA    
6324 C  C     . GLU B 357 ? 0.47270 0.35380 0.39250 0.07050  0.04870  0.03220  357 GLU B C     
6325 O  O     . GLU B 357 ? 0.48960 0.39130 0.41020 0.07480  0.03910  0.02630  357 GLU B O     
6326 C  CB    . GLU B 357 ? 0.64530 0.46770 0.53530 0.09010  0.05210  0.05630  357 GLU B CB    
6327 C  CG    . GLU B 357 ? 0.77570 0.56240 0.63390 0.09810  0.05840  0.07620  357 GLU B CG    
6328 C  CD    . GLU B 357 ? 0.96140 0.74440 0.78650 0.11090  0.04840  0.08300  357 GLU B CD    
6329 O  OE1   . GLU B 357 ? 1.01800 0.82670 0.84970 0.11540  0.03330  0.07180  357 GLU B OE1   
6330 O  OE2   . GLU B 357 ? 1.52040 1.28740 1.32260 0.11030  0.05420  0.09260  357 GLU B OE2   
6331 N  N     . GLY B 358 ? 0.48780 0.36950 0.42600 0.06120  0.05460  0.02320  358 GLY B N     
6332 C  CA    . GLY B 358 ? 0.45660 0.36230 0.41340 0.05510  0.05330  0.00630  358 GLY B CA    
6333 C  C     . GLY B 358 ? 0.41720 0.34650 0.37260 0.04330  0.05290  0.00290  358 GLY B C     
6334 O  O     . GLY B 358 ? 0.43960 0.39130 0.40380 0.04500  0.04800  -0.00610 358 GLY B O     
6335 N  N     . ALA B 359 ? 0.36400 0.28810 0.31210 0.03150  0.05820  0.01030  359 ALA B N     
6336 C  CA    . ALA B 359 ? 0.35990 0.30300 0.30680 0.02040  0.05760  0.00830  359 ALA B CA    
6337 C  C     . ALA B 359 ? 0.32460 0.28060 0.26260 0.02880  0.05070  0.01100  359 ALA B C     
6338 O  O     . ALA B 359 ? 0.32310 0.30000 0.26590 0.02370  0.04700  0.00360  359 ALA B O     
6339 C  CB    . ALA B 359 ? 0.44100 0.37450 0.38690 0.00880  0.06380  0.01700  359 ALA B CB    
6340 N  N     . LEU B 360 ? 0.37300 0.31320 0.29510 0.04160  0.04860  0.02160  360 LEU B N     
6341 C  CA    . LEU B 360 ? 0.36240 0.30840 0.26950 0.05100  0.03980  0.02410  360 LEU B CA    
6342 C  C     . LEU B 360 ? 0.34670 0.31310 0.26900 0.05800  0.02730  0.01180  360 LEU B C     
6343 O  O     . LEU B 360 ? 0.36670 0.35160 0.29150 0.05580  0.02070  0.00640  360 LEU B O     
6344 C  CB    . LEU B 360 ? 0.38390 0.30190 0.26370 0.06470  0.03960  0.03810  360 LEU B CB    
6345 C  CG    . LEU B 360 ? 0.41500 0.33240 0.27080 0.07580  0.02820  0.04020  360 LEU B CG    
6346 C  CD1   . LEU B 360 ? 0.41140 0.34030 0.26150 0.06580  0.03310  0.03980  360 LEU B CD1   
6347 C  CD2   . LEU B 360 ? 0.50930 0.39220 0.33020 0.09070  0.02790  0.05430  360 LEU B CD2   
6348 N  N     . GLN B 361 ? 0.43450 0.39750 0.37080 0.06620  0.02460  0.00710  361 GLN B N     
6349 C  CA    . GLN B 361 ? 0.48280 0.46630 0.44300 0.07340  0.01470  -0.00520 361 GLN B CA    
6350 C  C     . GLN B 361 ? 0.43410 0.44490 0.41380 0.05950  0.01950  -0.01720 361 GLN B C     
6351 O  O     . GLN B 361 ? 0.42790 0.45890 0.42140 0.06170  0.01100  -0.02420 361 GLN B O     
6352 C  CB    . GLN B 361 ? 0.53500 0.51000 0.51200 0.08250  0.01580  -0.00920 361 GLN B CB    
6353 C  CG    . GLN B 361 ? 0.81270 0.76380 0.77520 0.10110  0.00490  0.00090  361 GLN B CG    
6354 C  CD    . GLN B 361 ? 1.00450 0.94460 0.98490 0.11020  0.00660  -0.00270 361 GLN B CD    
6355 O  OE1   . GLN B 361 ? 0.96090 0.92010 0.97340 0.11200  0.00680  -0.01640 361 GLN B OE1   
6356 N  NE2   . GLN B 361 ? 1.04460 0.95220 1.00520 0.11620  0.00940  0.00950  361 GLN B NE2   
6357 N  N     . TYR B 362 ? 0.39670 0.40580 0.37640 0.04510  0.03250  -0.01940 362 TYR B N     
6358 C  CA    . TYR B 362 ? 0.40540 0.43340 0.39510 0.03070  0.03880  -0.02900 362 TYR B CA    
6359 C  C     . TYR B 362 ? 0.32710 0.36480 0.30670 0.02420  0.03420  -0.02490 362 TYR B C     
6360 O  O     . TYR B 362 ? 0.26950 0.32700 0.26190 0.02020  0.03220  -0.03250 362 TYR B O     
6361 C  CB    . TYR B 362 ? 0.32690 0.34330 0.31100 0.01830  0.05010  -0.03140 362 TYR B CB    
6362 C  CG    . TYR B 362 ? 0.36180 0.37250 0.35800 0.02240  0.05680  -0.04090 362 TYR B CG    
6363 C  CD1   . TYR B 362 ? 0.35450 0.38240 0.37110 0.02460  0.06130  -0.05310 362 TYR B CD1   
6364 C  CD2   . TYR B 362 ? 0.41170 0.39900 0.40140 0.02400  0.06020  -0.03810 362 TYR B CD2   
6365 C  CE1   . TYR B 362 ? 0.36460 0.38640 0.39320 0.02930  0.07000  -0.06280 362 TYR B CE1   
6366 C  CE2   . TYR B 362 ? 0.47350 0.45300 0.47330 0.02850  0.06670  -0.04780 362 TYR B CE2   
6367 C  CZ    . TYR B 362 ? 0.45490 0.45160 0.47330 0.03170  0.07220  -0.06050 362 TYR B CZ    
6368 O  OH    . TYR B 362 ? 0.61690 0.60490 0.64580 0.03690  0.08110  -0.07100 362 TYR B OH    
6369 N  N     . GLY B 363 ? 0.47420 0.49760 0.43370 0.02330  0.03410  -0.01360 363 GLY B N     
6370 C  CA    . GLY B 363 ? 0.36980 0.39930 0.31900 0.01870  0.03100  -0.00980 363 GLY B CA    
6371 C  C     . GLY B 363 ? 0.35620 0.39740 0.30750 0.02780  0.01880  -0.01350 363 GLY B C     
6372 O  O     . GLY B 363 ? 0.31170 0.36740 0.26760 0.02100  0.01600  -0.01800 363 GLY B O     
6373 N  N     . GLN B 364 ? 0.29640 0.32950 0.24450 0.04330  0.00980  -0.01170 364 GLN B N     
6374 C  CA    . GLN B 364 ? 0.38550 0.42660 0.33580 0.05400  -0.00680 -0.01590 364 GLN B CA    
6375 C  C     . GLN B 364 ? 0.36730 0.43640 0.35310 0.04990  -0.01100 -0.02980 364 GLN B C     
6376 O  O     . GLN B 364 ? 0.46890 0.55010 0.46120 0.05090  -0.02250 -0.03490 364 GLN B O     
6377 C  CB    . GLN B 364 ? 0.40400 0.42670 0.34240 0.07230  -0.01740 -0.01050 364 GLN B CB    
6378 C  CG    . GLN B 364 ? 0.41500 0.40760 0.31280 0.07760  -0.01360 0.00410  364 GLN B CG    
6379 C  CD    . GLN B 364 ? 0.44080 0.40880 0.32180 0.09480  -0.02140 0.01180  364 GLN B CD    
6380 O  OE1   . GLN B 364 ? 0.53270 0.50290 0.43510 0.10020  -0.02350 0.00820  364 GLN B OE1   
6381 N  NE2   . GLN B 364 ? 0.43430 0.37580 0.27480 0.10400  -0.02450 0.02270  364 GLN B NE2   
6382 N  N     . LYS B 365 ? 0.49340 0.57100 0.50210 0.04490  -0.00010 -0.03620 365 LYS B N     
6383 C  CA    . LYS B 365 ? 0.44410 0.54680 0.48780 0.03910  0.00290  -0.04890 365 LYS B CA    
6384 C  C     . LYS B 365 ? 0.36440 0.47680 0.40660 0.02110  0.01310  -0.05130 365 LYS B C     
6385 O  O     . LYS B 365 ? 0.37770 0.50980 0.44490 0.01540  0.01440  -0.06000 365 LYS B O     
6386 C  CB    . LYS B 365 ? 0.49370 0.59750 0.55780 0.04140  0.01380  -0.05510 365 LYS B CB    
6387 C  CG    . LYS B 365 ? 0.49920 0.60060 0.57960 0.06010  0.00190  -0.05640 365 LYS B CG    
6388 C  CD    . LYS B 365 ? 0.73530 0.83010 0.82860 0.06300  0.01480  -0.06090 365 LYS B CD    
6389 C  CE    . LYS B 365 ? 1.02130 1.13760 1.14890 0.05550  0.02970  -0.07470 365 LYS B CE    
6390 N  NZ    . LYS B 365 ? 1.00960 1.14920 1.18360 0.06640  0.02030  -0.08420 365 LYS B NZ    
6391 N  N     . ILE B 366 ? 0.33570 0.43360 0.35090 0.01240  0.02010  -0.04320 366 ILE B N     
6392 C  CA    . ILE B 366 ? 0.41270 0.51510 0.42320 -0.00380 0.02850  -0.04410 366 ILE B CA    
6393 C  C     . ILE B 366 ? 0.34150 0.44830 0.34460 -0.00700 0.02020  -0.04150 366 ILE B C     
6394 O  O     . ILE B 366 ? 0.40340 0.52040 0.41420 -0.01800 0.02360  -0.04550 366 ILE B O     
6395 C  CB    . ILE B 366 ? 0.41630 0.50110 0.40600 -0.01200 0.03740  -0.03770 366 ILE B CB    
6396 C  CG1   . ILE B 366 ? 0.33840 0.41740 0.33370 -0.01210 0.04700  -0.04310 366 ILE B CG1   
6397 C  CG2   . ILE B 366 ? 0.39870 0.47610 0.38230 -0.02480 0.03610  -0.03330 366 ILE B CG2   
6398 C  CD1   . ILE B 366 ? 0.44310 0.50150 0.42020 -0.01660 0.05070  -0.03720 366 ILE B CD1   
6399 N  N     . ILE B 367 ? 0.35400 0.45010 0.33960 0.00250  0.01080  -0.03470 367 ILE B N     
6400 C  CA    . ILE B 367 ? 0.35200 0.44500 0.32250 -0.00050 0.00620  -0.03100 367 ILE B CA    
6401 C  C     . ILE B 367 ? 0.29990 0.40860 0.28580 -0.00290 -0.00300 -0.03930 367 ILE B C     
6402 O  O     . ILE B 367 ? 0.39410 0.50500 0.37750 -0.01290 -0.00080 -0.03930 367 ILE B O     
6403 C  CB    . ILE B 367 ? 0.40640 0.48000 0.34980 0.01110  0.00180  -0.02190 367 ILE B CB    
6404 C  CG1   . ILE B 367 ? 0.37040 0.43640 0.30050 0.00760  0.00080  -0.01810 367 ILE B CG1   
6405 C  CG2   . ILE B 367 ? 0.37400 0.44440 0.31500 0.02710  -0.01200 -0.02410 367 ILE B CG2   
6406 C  CD1   . ILE B 367 ? 0.38800 0.44730 0.32850 -0.00520 0.00970  -0.01330 367 ILE B CD1   
6407 N  N     . LYS B 368 ? 0.32040 0.43950 0.32500 0.00600  -0.01430 -0.04670 368 LYS B N     
6408 C  CA    . LYS B 368 ? 0.42560 0.56010 0.45090 0.00360  -0.02510 -0.05570 368 LYS B CA    
6409 C  C     . LYS B 368 ? 0.27670 0.42770 0.32840 -0.01220 -0.01270 -0.06160 368 LYS B C     
6410 O  O     . LYS B 368 ? 0.25240 0.40600 0.30620 -0.02110 -0.01340 -0.06310 368 LYS B O     
6411 C  CB    . LYS B 368 ? 0.37400 0.51550 0.41730 0.01780  -0.04350 -0.06250 368 LYS B CB    
6412 C  CG    . LYS B 368 ? 0.69960 0.84720 0.75500 0.01810  -0.06000 -0.06980 368 LYS B CG    
6413 C  CD    . LYS B 368 ? 0.79600 0.94700 0.87420 0.03030  -0.07740 -0.07540 368 LYS B CD    
6414 C  CE    . LYS B 368 ? 1.12040 1.24940 1.16460 0.04800  -0.09190 -0.06940 368 LYS B CE    
6415 N  NZ    . LYS B 368 ? 1.30240 1.40410 1.30220 0.04940  -0.09510 -0.06200 368 LYS B NZ    
6416 N  N     . PRO B 369 ? 0.33160 0.49010 0.40120 -0.01580 0.00080  -0.06450 369 PRO B N     
6417 C  CA    . PRO B 369 ? 0.30450 0.46400 0.38230 -0.03020 0.01660  -0.06610 369 PRO B CA    
6418 C  C     . PRO B 369 ? 0.31700 0.45580 0.36190 -0.04020 0.02220  -0.05730 369 PRO B C     
6419 O  O     . PRO B 369 ? 0.27980 0.41040 0.32290 -0.04710 0.02510  -0.05630 369 PRO B O     
6420 C  CB    . PRO B 369 ? 0.38650 0.54310 0.47110 -0.02830 0.02890  -0.06790 369 PRO B CB    
6421 C  CG    . PRO B 369 ? 0.33070 0.50170 0.43680 -0.01250 0.01800  -0.07310 369 PRO B CG    
6422 C  CD    . PRO B 369 ? 0.35760 0.51470 0.43470 -0.00450 0.00140  -0.06530 369 PRO B CD    
6423 N  N     . TYR B 370 ? 0.37350 0.50230 0.39530 -0.03910 0.02230  -0.05030 370 TYR B N     
6424 C  CA    . TYR B 370 ? 0.39080 0.49730 0.39000 -0.04540 0.02020  -0.04090 370 TYR B CA    
6425 C  C     . TYR B 370 ? 0.42280 0.53390 0.41840 -0.04770 0.01530  -0.04150 370 TYR B C     
6426 O  O     . TYR B 370 ? 0.38000 0.47560 0.36830 -0.05210 0.01610  -0.03740 370 TYR B O     
6427 C  CB    . TYR B 370 ? 0.39150 0.48350 0.37920 -0.03960 0.01860  -0.03120 370 TYR B CB    
6428 C  CG    . TYR B 370 ? 0.33060 0.40590 0.31310 -0.04160 0.02240  -0.02790 370 TYR B CG    
6429 C  CD1   . TYR B 370 ? 0.34700 0.42310 0.33370 -0.04420 0.02910  -0.03360 370 TYR B CD1   
6430 C  CD2   . TYR B 370 ? 0.33490 0.39510 0.30980 -0.04040 0.02020  -0.02050 370 TYR B CD2   
6431 C  CE1   . TYR B 370 ? 0.36300 0.42490 0.34180 -0.04640 0.03250  -0.03190 370 TYR B CE1   
6432 C  CE2   . TYR B 370 ? 0.50020 0.54970 0.47040 -0.04330 0.02250  -0.02000 370 TYR B CE2   
6433 C  CZ    . TYR B 370 ? 0.39310 0.44290 0.36320 -0.04650 0.02820  -0.02560 370 TYR B CZ    
6434 O  OH    . TYR B 370 ? 0.47240 0.51070 0.43440 -0.05050 0.03060  -0.02600 370 TYR B OH    
6435 N  N     . SER B 371 ? 0.34250 0.46470 0.34430 -0.03920 0.00800  -0.04330 371 SER B N     
6436 C  CA    . SER B 371 ? 0.44950 0.56290 0.44810 -0.03660 0.00130  -0.04080 371 SER B CA    
6437 C  C     . SER B 371 ? 0.44070 0.55610 0.45290 -0.04340 0.00290  -0.04490 371 SER B C     
6438 O  O     . SER B 371 ? 0.51110 0.61680 0.51700 -0.04620 0.00280  -0.04100 371 SER B O     
6439 C  CB    . SER B 371 ? 0.50150 0.61120 0.49480 -0.02320 -0.01310 -0.04350 371 SER B CB    
6440 O  OG    . SER B 371 ? 0.66780 0.76410 0.63970 -0.01480 -0.01220 -0.03640 371 SER B OG    
6441 N  N     . LYS B 372 ? 0.33730 0.46340 0.37070 -0.04520 0.00480  -0.05190 372 LYS B N     
6442 C  CA    . LYS B 372 ? 0.29800 0.42400 0.34790 -0.05110 0.00700  -0.05440 372 LYS B CA    
6443 C  C     . LYS B 372 ? 0.28480 0.39930 0.32400 -0.05960 0.02000  -0.05050 372 LYS B C     
6444 O  O     . LYS B 372 ? 0.37490 0.48350 0.41630 -0.06490 0.02200  -0.04880 372 LYS B O     
6445 C  CB    . LYS B 372 ? 0.39760 0.53950 0.48130 -0.04800 0.00180  -0.06280 372 LYS B CB    
6446 C  CG    . LYS B 372 ? 0.48450 0.63510 0.58210 -0.04730 0.01130  -0.06640 372 LYS B CG    
6447 C  CD    . LYS B 372 ? 0.40500 0.57000 0.54170 -0.04640 0.00980  -0.07340 372 LYS B CD    
6448 C  CE    . LYS B 372 ? 0.60200 0.77730 0.75640 -0.04080 0.01510  -0.07810 372 LYS B CE    
6449 N  NZ    . LYS B 372 ? 0.58800 0.77800 0.78410 -0.03900 0.01420  -0.08490 372 LYS B NZ    
6450 N  N     . HIS B 373 ? 0.25770 0.36640 0.28450 -0.06030 0.02650  -0.04930 373 HIS B N     
6451 C  CA    . HIS B 373 ? 0.29910 0.39280 0.31340 -0.06660 0.03440  -0.04640 373 HIS B CA    
6452 C  C     . HIS B 373 ? 0.33250 0.40940 0.32150 -0.06900 0.02990  -0.03990 373 HIS B C     
6453 O  O     . HIS B 373 ? 0.44410 0.51130 0.42670 -0.07450 0.03330  -0.03780 373 HIS B O     
6454 C  CB    . HIS B 373 ? 0.25880 0.35010 0.27200 -0.06570 0.04050  -0.04790 373 HIS B CB    
6455 C  CG    . HIS B 373 ? 0.29270 0.39920 0.33430 -0.06410 0.04810  -0.05470 373 HIS B CG    
6456 N  ND1   . HIS B 373 ? 0.31940 0.43210 0.36990 -0.05910 0.05150  -0.05810 373 HIS B ND1   
6457 C  CD2   . HIS B 373 ? 0.25430 0.37150 0.32160 -0.06650 0.05270  -0.05860 373 HIS B CD2   
6458 C  CE1   . HIS B 373 ? 0.30610 0.43320 0.38710 -0.05780 0.05770  -0.06440 373 HIS B CE1   
6459 N  NE2   . HIS B 373 ? 0.32820 0.45840 0.42080 -0.06270 0.05820  -0.06470 373 HIS B NE2   
6460 N  N     . TYR B 374 ? 0.35580 0.43030 0.33320 -0.06490 0.02250  -0.03670 374 TYR B N     
6461 C  CA    . TYR B 374 ? 0.33820 0.39770 0.30500 -0.06260 0.01680  -0.02770 374 TYR B CA    
6462 C  C     . TYR B 374 ? 0.28360 0.34540 0.25010 -0.06250 0.01590  -0.02590 374 TYR B C     
6463 O  O     . TYR B 374 ? 0.39670 0.47210 0.37230 -0.06260 0.01720  -0.03070 374 TYR B O     
6464 C  CB    . TYR B 374 ? 0.27390 0.32860 0.24340 -0.05560 0.01200  -0.02190 374 TYR B CB    
6465 C  CG    . TYR B 374 ? 0.27110 0.32000 0.23830 -0.05750 0.01300  -0.02170 374 TYR B CG    
6466 C  CD1   . TYR B 374 ? 0.30070 0.33850 0.25980 -0.06140 0.01260  -0.01930 374 TYR B CD1   
6467 C  CD2   . TYR B 374 ? 0.31410 0.36970 0.28530 -0.05690 0.01490  -0.02470 374 TYR B CD2   
6468 C  CE1   . TYR B 374 ? 0.28440 0.31660 0.23870 -0.06500 0.01430  -0.01990 374 TYR B CE1   
6469 C  CE2   . TYR B 374 ? 0.30050 0.34970 0.26760 -0.05980 0.01700  -0.02540 374 TYR B CE2   
6470 C  CZ    . TYR B 374 ? 0.33380 0.37090 0.29200 -0.06410 0.01680  -0.02300 374 TYR B CZ    
6471 O  OH    . TYR B 374 ? 0.28110 0.31070 0.23290 -0.06830 0.01930  -0.02410 374 TYR B OH    
6472 N  N     . PRO B 375 ? 0.44140 0.49160 0.40120 -0.06270 0.01310  -0.02000 375 PRO B N     
6473 C  CA    . PRO B 375 ? 0.37890 0.43010 0.33830 -0.06350 0.01220  -0.01810 375 PRO B CA    
6474 C  C     . PRO B 375 ? 0.46240 0.51840 0.42800 -0.05760 0.01060  -0.01610 375 PRO B C     
6475 O  O     . PRO B 375 ? 0.37730 0.43320 0.34650 -0.05220 0.00990  -0.01430 375 PRO B O     
6476 C  CB    . PRO B 375 ? 0.40290 0.44090 0.35440 -0.06470 0.00900  -0.01220 375 PRO B CB    
6477 C  CG    . PRO B 375 ? 0.50690 0.53880 0.45280 -0.06800 0.00950  -0.01300 375 PRO B CG    
6478 C  CD    . PRO B 375 ? 0.42970 0.46750 0.38240 -0.06420 0.01100  -0.01630 375 PRO B CD    
6479 N  N     . LEU B 376 ? 0.34970 0.40780 0.31760 -0.05960 0.00900  -0.01720 376 LEU B N     
6480 C  CA    . LEU B 376 ? 0.43970 0.50000 0.41260 -0.05390 0.00400  -0.01930 376 LEU B CA    
6481 C  C     . LEU B 376 ? 0.46270 0.52080 0.43250 -0.05170 0.00580  -0.01420 376 LEU B C     
6482 O  O     . LEU B 376 ? 0.73260 0.79050 0.70000 -0.04370 0.00300  -0.01620 376 LEU B O     
6483 C  CB    . LEU B 376 ? 0.47150 0.52490 0.44560 -0.05330 -0.00250 -0.02300 376 LEU B CB    
6484 C  CG    . LEU B 376 ? 0.67180 0.72360 0.64470 -0.04530 -0.01230 -0.03110 376 LEU B CG    
6485 C  CD1   . LEU B 376 ? 0.56040 0.60300 0.53280 -0.04610 -0.01890 -0.03560 376 LEU B CD1   
6486 C  CD2   . LEU B 376 ? 0.68980 0.73680 0.64810 -0.03580 -0.01280 -0.03020 376 LEU B CD2   
6487 N  N     . TYR B 377 ? 0.44080 0.48960 0.40810 -0.05310 0.00640  -0.00880 377 TYR B N     
6488 C  CA    . TYR B 377 ? 0.41190 0.45720 0.38090 -0.05110 0.00440  -0.00670 377 TYR B CA    
6489 C  C     . TYR B 377 ? 0.48390 0.52260 0.45220 -0.04790 0.00160  -0.00470 377 TYR B C     
6490 O  O     . TYR B 377 ? 0.74590 0.78040 0.71040 -0.04900 -0.00000 -0.00130 377 TYR B O     
6491 C  CB    . TYR B 377 ? 0.44490 0.48600 0.40880 -0.05460 0.00360  -0.00550 377 TYR B CB    
6492 C  CG    . TYR B 377 ? 0.33160 0.37230 0.28800 -0.05290 0.00430  -0.01070 377 TYR B CG    
6493 C  CD1   . TYR B 377 ? 0.47150 0.50700 0.41720 -0.04040 0.00690  -0.01320 377 TYR B CD1   
6494 C  CD2   . TYR B 377 ? 0.35770 0.39380 0.31470 -0.05610 0.00040  -0.01350 377 TYR B CD2   
6495 C  CE1   . TYR B 377 ? 0.41250 0.43950 0.34480 -0.03350 0.00470  -0.01990 377 TYR B CE1   
6496 C  CE2   . TYR B 377 ? 0.39580 0.42590 0.34630 -0.05100 -0.00370 -0.02160 377 TYR B CE2   
6497 C  CZ    . TYR B 377 ? 0.43380 0.45910 0.36930 -0.03960 -0.00180 -0.02550 377 TYR B CZ    
6498 O  OH    . TYR B 377 ? 0.56640 0.58070 0.48920 -0.03260 -0.00620 -0.03390 377 TYR B OH    
6499 N  N     . SER B 378 ? 0.43340 0.47390 0.40480 -0.04650 0.00230  -0.00620 378 SER B N     
6500 C  CA    . SER B 378 ? 0.37230 0.40760 0.34130 -0.04580 0.00150  -0.00530 378 SER B CA    
6501 C  C     . SER B 378 ? 0.34970 0.38600 0.31950 -0.04520 0.00170  -0.00380 378 SER B C     
6502 O  O     . SER B 378 ? 0.36260 0.40440 0.33450 -0.04380 0.00390  -0.00440 378 SER B O     
6503 C  CB    . SER B 378 ? 0.39730 0.43560 0.36730 -0.04680 0.00340  -0.00850 378 SER B CB    
6504 O  OG    . SER B 378 ? 0.35280 0.38750 0.32010 -0.04850 0.00370  -0.00850 378 SER B OG    
6505 N  N     . LEU B 379 ? 0.26220 0.29380 0.22800 -0.04700 -0.00010 -0.00110 379 LEU B N     
6506 C  CA    . LEU B 379 ? 0.27710 0.30890 0.24420 -0.04740 0.00110  0.00130  379 LEU B CA    
6507 C  C     . LEU B 379 ? 0.26270 0.29510 0.22940 -0.04730 0.00310  -0.00160 379 LEU B C     
6508 O  O     . LEU B 379 ? 0.30570 0.33640 0.27730 -0.04270 0.00820  0.00170  379 LEU B O     
6509 C  CB    . LEU B 379 ? 0.36270 0.38960 0.32990 -0.05030 -0.00180 0.00640  379 LEU B CB    
6510 C  CG    . LEU B 379 ? 0.37760 0.40330 0.35520 -0.05010 -0.00330 0.01130  379 LEU B CG    
6511 C  CD1   . LEU B 379 ? 0.53610 0.55670 0.52160 -0.05390 -0.00940 0.01580  379 LEU B CD1   
6512 C  CD2   . LEU B 379 ? 0.41670 0.44520 0.41080 -0.04480 0.00450  0.01320  379 LEU B CD2   
6513 N  N     . ASN B 380 ? 0.28690 0.31860 0.25200 -0.04870 0.00280  -0.00500 380 ASN B N     
6514 C  CA    . ASN B 380 ? 0.24970 0.28360 0.21480 -0.05010 0.00560  -0.00820 380 ASN B CA    
6515 C  C     . ASN B 380 ? 0.25720 0.29730 0.22700 -0.04380 0.00900  -0.00770 380 ASN B C     
6516 O  O     . ASN B 380 ? 0.27360 0.31170 0.24260 -0.03870 0.01320  -0.00600 380 ASN B O     
6517 C  CB    . ASN B 380 ? 0.31840 0.35100 0.28170 -0.05280 0.00730  -0.01120 380 ASN B CB    
6518 C  CG    . ASN B 380 ? 0.42330 0.44630 0.37940 -0.05650 0.00590  -0.00950 380 ASN B CG    
6519 O  OD1   . ASN B 380 ? 0.49940 0.51740 0.44980 -0.06070 0.00710  -0.01020 380 ASN B OD1   
6520 N  ND2   . ASN B 380 ? 0.32570 0.34590 0.27990 -0.05680 0.00350  -0.00740 380 ASN B ND2   
6521 N  N     . VAL B 381 ? 0.29570 0.34130 0.26820 -0.04240 0.00790  -0.00820 381 VAL B N     
6522 C  CA    . VAL B 381 ? 0.26460 0.31350 0.23560 -0.03420 0.01060  -0.00730 381 VAL B CA    
6523 C  C     . VAL B 381 ? 0.29440 0.33360 0.25860 -0.02580 0.01450  -0.00160 381 VAL B C     
6524 O  O     . VAL B 381 ? 0.30060 0.33460 0.25650 -0.01820 0.01830  0.00060  381 VAL B O     
6525 C  CB    . VAL B 381 ? 0.27820 0.33630 0.25160 -0.03680 0.00840  -0.01060 381 VAL B CB    
6526 C  CG1   . VAL B 381 ? 0.33350 0.39240 0.29740 -0.02700 0.00800  -0.01160 381 VAL B CG1   
6527 C  CG2   . VAL B 381 ? 0.36060 0.42920 0.34080 -0.04560 0.00800  -0.01620 381 VAL B CG2   
6528 N  N     . ALA B 382 ? 0.27510 0.31100 0.24100 -0.02740 0.01490  0.00100  382 ALA B N     
6529 C  CA    . ALA B 382 ? 0.33260 0.35970 0.29460 -0.02010 0.02240  0.00710  382 ALA B CA    
6530 C  C     . ALA B 382 ? 0.28120 0.30370 0.24530 -0.01820 0.02770  0.01140  382 ALA B C     
6531 O  O     . ALA B 382 ? 0.27620 0.29160 0.23270 -0.00940 0.03530  0.01660  382 ALA B O     
6532 C  CB    . ALA B 382 ? 0.32260 0.34940 0.29190 -0.02320 0.02340  0.00930  382 ALA B CB    
6533 N  N     . SER B 383 ? 0.22720 0.25270 0.19920 -0.02590 0.02370  0.00970  383 SER B N     
6534 C  CA    . SER B 383 ? 0.27990 0.30130 0.25640 -0.02570 0.02810  0.01350  383 SER B CA    
6535 C  C     . SER B 383 ? 0.24930 0.26930 0.21720 -0.02060 0.03120  0.01340  383 SER B C     
6536 O  O     . SER B 383 ? 0.29080 0.30820 0.25950 -0.01730 0.03740  0.01970  383 SER B O     
6537 C  CB    . SER B 383 ? 0.33060 0.35270 0.31140 -0.03540 0.02200  0.01050  383 SER B CB    
6538 O  OG    . SER B 383 ? 0.59930 0.62440 0.57100 -0.04010 0.01600  0.00320  383 SER B OG    
6539 N  N     . MET B 384 ? 0.28110 0.30590 0.24320 -0.02090 0.02670  0.00730  384 MET B N     
6540 C  CA    . MET B 384 ? 0.32450 0.34960 0.27790 -0.01580 0.02930  0.00620  384 MET B CA    
6541 C  C     . MET B 384 ? 0.31760 0.33250 0.25490 -0.00550 0.03380  0.01050  384 MET B C     
6542 O  O     . MET B 384 ? 0.32900 0.33460 0.25610 -0.00620 0.03740  0.01120  384 MET B O     
6543 C  CB    . MET B 384 ? 0.32680 0.36330 0.28270 -0.01940 0.02450  -0.00190 384 MET B CB    
6544 C  CG    . MET B 384 ? 0.34030 0.38270 0.29100 -0.01480 0.02710  -0.00570 384 MET B CG    
6545 S  SD    . MET B 384 ? 0.42100 0.45600 0.36950 -0.01510 0.03480  -0.00410 384 MET B SD    
6546 C  CE    . MET B 384 ? 0.43870 0.47310 0.39660 -0.02720 0.03280  -0.00890 384 MET B CE    
6547 N  N     . TRP B 385 ? 0.33790 0.34860 0.26930 -0.00360 0.03170  0.00970  385 TRP B N     
6548 C  CA    . TRP B 385 ? 0.32940 0.33530 0.24600 -0.00700 0.03100  0.00920  385 TRP B CA    
6549 C  C     . TRP B 385 ? 0.38560 0.39630 0.30730 -0.00630 0.03740  0.01780  385 TRP B C     
6550 O  O     . TRP B 385 ? 0.32500 0.32160 0.23310 0.00340  0.04120  0.02290  385 TRP B O     
6551 C  CB    . TRP B 385 ? 0.35340 0.35570 0.26490 -0.00630 0.02840  0.00700  385 TRP B CB    
6552 C  CG    . TRP B 385 ? 0.33690 0.34210 0.23910 -0.00010 0.01990  0.00210  385 TRP B CG    
6553 C  CD1   . TRP B 385 ? 0.32310 0.33870 0.23670 -0.00070 0.01460  -0.00180 385 TRP B CD1   
6554 C  CD2   . TRP B 385 ? 0.34130 0.35310 0.23350 0.00760  0.01120  -0.00040 385 TRP B CD2   
6555 N  NE1   . TRP B 385 ? 0.35070 0.37620 0.26150 0.00130  0.00450  -0.00840 385 TRP B NE1   
6556 C  CE2   . TRP B 385 ? 0.33770 0.36010 0.23520 0.00830  0.00100  -0.00790 385 TRP B CE2   
6557 C  CE3   . TRP B 385 ? 0.39790 0.40480 0.27750 0.01800  0.00990  0.00340  385 TRP B CE3   
6558 C  CZ2   . TRP B 385 ? 0.39200 0.42170 0.28530 0.01690  -0.01210 -0.01380 385 TRP B CZ2   
6559 C  CZ3   . TRP B 385 ? 0.44760 0.45580 0.31720 0.02970  -0.00340 -0.00110 385 TRP B CZ3   
6560 C  CH2   . TRP B 385 ? 0.41920 0.44060 0.29800 0.02840  -0.01530 -0.01050 385 TRP B CH2   
6561 N  N     . LEU B 386 ? 0.31550 0.33420 0.25640 -0.01200 0.03830  0.02000  386 LEU B N     
6562 C  CA    . LEU B 386 ? 0.31880 0.32820 0.26490 -0.01190 0.04700  0.02690  386 LEU B CA    
6563 C  C     . LEU B 386 ? 0.31720 0.31660 0.26270 -0.01010 0.05140  0.03040  386 LEU B C     
6564 O  O     . LEU B 386 ? 0.31240 0.29620 0.25160 -0.00420 0.05970  0.03600  386 LEU B O     
6565 C  CB    . LEU B 386 ? 0.35410 0.37230 0.31970 -0.01910 0.04590  0.02810  386 LEU B CB    
6566 C  CG    . LEU B 386 ? 0.35910 0.36710 0.33680 -0.02030 0.05460  0.03290  386 LEU B CG    
6567 C  CD1   . LEU B 386 ? 0.39170 0.38570 0.35910 -0.01150 0.06570  0.03640  386 LEU B CD1   
6568 C  CD2   . LEU B 386 ? 0.38760 0.40300 0.38380 -0.02700 0.05200  0.03260  386 LEU B CD2   
6569 N  N     . LYS B 387 ? 0.27900 0.28620 0.23040 -0.01420 0.04730  0.02780  387 LYS B N     
6570 C  CA    . LYS B 387 ? 0.29430 0.28990 0.24340 -0.01250 0.05230  0.02990  387 LYS B CA    
6571 C  C     . LYS B 387 ? 0.29290 0.27450 0.22100 -0.00050 0.05540  0.03260  387 LYS B C     
6572 O  O     . LYS B 387 ? 0.32740 0.29180 0.25060 0.00470  0.06280  0.03930  387 LYS B O     
6573 C  CB    . LYS B 387 ? 0.30070 0.30410 0.25500 -0.01720 0.04880  0.02450  387 LYS B CB    
6574 C  CG    . LYS B 387 ? 0.33770 0.34260 0.30860 -0.02650 0.04630  0.02370  387 LYS B CG    
6575 C  CD    . LYS B 387 ? 0.36460 0.36930 0.33150 -0.03310 0.04290  0.01410  387 LYS B CD    
6576 C  CE    . LYS B 387 ? 0.49490 0.50010 0.46890 -0.04300 0.03590  0.01060  387 LYS B CE    
6577 N  NZ    . LYS B 387 ? 0.60330 0.60730 0.56610 -0.05090 0.03270  0.00090  387 LYS B NZ    
6578 N  N     . LEU B 388 ? 0.38210 0.36980 0.29770 0.00480  0.04870  0.02800  388 LEU B N     
6579 C  CA    . LEU B 388 ? 0.41540 0.38990 0.30800 0.01930  0.04700  0.03090  388 LEU B CA    
6580 C  C     . LEU B 388 ? 0.42640 0.38260 0.30680 0.02530  0.05270  0.03840  388 LEU B C     
6581 O  O     . LEU B 388 ? 0.51710 0.45400 0.38230 0.03470  0.05680  0.04490  388 LEU B O     
6582 C  CB    . LEU B 388 ? 0.40590 0.39160 0.29050 0.02370  0.03590  0.02340  388 LEU B CB    
6583 C  CG    . LEU B 388 ? 0.45510 0.45630 0.34430 0.02610  0.03060  0.01560  388 LEU B CG    
6584 C  CD1   . LEU B 388 ? 0.57720 0.59290 0.46580 0.02880  0.01830  0.00700  388 LEU B CD1   
6585 C  CD2   . LEU B 388 ? 0.50150 0.49280 0.38820 0.03740  0.02770  0.01680  388 LEU B CD2   
6586 N  N     . GLY B 389 ? 0.38030 0.34120 0.26620 0.02040  0.05400  0.03720  389 GLY B N     
6587 C  CA    . GLY B 389 ? 0.40710 0.35160 0.28090 0.02590  0.06200  0.04270  389 GLY B CA    
6588 C  C     . GLY B 389 ? 0.42060 0.35160 0.30070 0.02560  0.07430  0.05020  389 GLY B C     
6589 O  O     . GLY B 389 ? 0.43430 0.34470 0.29550 0.03420  0.08140  0.05620  389 GLY B O     
6590 N  N     . ARG B 390 ? 0.35970 0.30120 0.26560 0.01550  0.07630  0.04950  390 ARG B N     
6591 C  CA    . ARG B 390 ? 0.40300 0.33420 0.32210 0.01280  0.08720  0.05540  390 ARG B CA    
6592 C  C     . ARG B 390 ? 0.39800 0.31360 0.30540 0.01880  0.08930  0.05980  390 ARG B C     
6593 O  O     . ARG B 390 ? 0.43750 0.33550 0.34080 0.02240  0.09980  0.06670  390 ARG B O     
6594 C  CB    . ARG B 390 ? 0.41190 0.35850 0.36120 0.00030  0.08480  0.05210  390 ARG B CB    
6595 C  CG    . ARG B 390 ? 0.35970 0.31490 0.32170 -0.00330 0.08650  0.05080  390 ARG B CG    
6596 C  CD    . ARG B 390 ? 0.34940 0.31780 0.33880 -0.01410 0.08180  0.04810  390 ARG B CD    
6597 N  NE    . ARG B 390 ? 0.38390 0.35680 0.38620 -0.01500 0.08580  0.04840  390 ARG B NE    
6598 C  CZ    . ARG B 390 ? 0.41510 0.39960 0.43880 -0.02250 0.08010  0.04590  390 ARG B CZ    
6599 N  NH1   . ARG B 390 ? 0.42720 0.41920 0.45880 -0.03080 0.06900  0.04260  390 ARG B NH1   
6600 N  NH2   . ARG B 390 ? 0.40430 0.39080 0.44020 -0.02120 0.08590  0.04670  390 ARG B NH2   
6601 N  N     . LEU B 391 ? 0.42070 0.34140 0.32230 0.02040  0.08090  0.05630  391 LEU B N     
6602 C  CA    . LEU B 391 ? 0.38200 0.28560 0.26940 0.02900  0.08220  0.06080  391 LEU B CA    
6603 C  C     . LEU B 391 ? 0.47310 0.35700 0.33020 0.04310  0.08230  0.06640  391 LEU B C     
6604 O  O     . LEU B 391 ? 0.50460 0.36760 0.35270 0.04840  0.08920  0.07370  391 LEU B O     
6605 C  CB    . LEU B 391 ? 0.39060 0.30440 0.27590 0.03030  0.07410  0.05520  391 LEU B CB    
6606 C  CG    . LEU B 391 ? 0.34960 0.27470 0.25930 0.01640  0.07630  0.04980  391 LEU B CG    
6607 C  CD1   . LEU B 391 ? 0.35450 0.29890 0.26740 0.01570  0.06640  0.03790  391 LEU B CD1   
6608 C  CD2   . LEU B 391 ? 0.36660 0.27180 0.28400 0.01460  0.08460  0.05500  391 LEU B CD2   
6609 N  N     . TYR B 392 ? 0.46480 0.35410 0.30590 0.04860  0.07370  0.06240  392 TYR B N     
6610 C  CA    . TYR B 392 ? 0.49380 0.36370 0.30230 0.06180  0.07040  0.06570  392 TYR B CA    
6611 C  C     . TYR B 392 ? 0.50770 0.35870 0.30980 0.06170  0.08580  0.07300  392 TYR B C     
6612 O  O     . TYR B 392 ? 0.49550 0.32250 0.27470 0.07090  0.08870  0.07980  392 TYR B O     
6613 C  CB    . TYR B 392 ? 0.52180 0.40200 0.32050 0.06390  0.05950  0.05850  392 TYR B CB    
6614 C  CG    . TYR B 392 ? 0.44710 0.33900 0.24160 0.06990  0.04200  0.05170  392 TYR B CG    
6615 C  CD1   . TYR B 392 ? 0.50670 0.38620 0.28450 0.08340  0.03130  0.05360  392 TYR B CD1   
6616 C  CD2   . TYR B 392 ? 0.44340 0.35880 0.25210 0.06290  0.03460  0.04290  392 TYR B CD2   
6617 C  CE1   . TYR B 392 ? 0.50160 0.39460 0.28070 0.09080  0.01260  0.04600  392 TYR B CE1   
6618 C  CE2   . TYR B 392 ? 0.42230 0.35070 0.23060 0.06870  0.01850  0.03530  392 TYR B CE2   
6619 C  CZ    . TYR B 392 ? 0.46840 0.38710 0.26340 0.08330  0.00670  0.03630  392 TYR B CZ    
6620 O  OH    . TYR B 392 ? 0.44970 0.38550 0.25210 0.09030  -0.01220 0.02700  392 TYR B OH    
6621 N  N     . MET B 393 ? 0.48110 0.34200 0.30250 0.05220  0.09510  0.07180  393 MET B N     
6622 C  CA    . MET B 393 ? 0.56670 0.41170 0.38570 0.05240  0.11180  0.07820  393 MET B CA    
6623 C  C     . MET B 393 ? 0.50670 0.34020 0.33620 0.05030  0.12160  0.08510  393 MET B C     
6624 O  O     . MET B 393 ? 0.50970 0.31980 0.32080 0.05640  0.13240  0.09260  393 MET B O     
6625 C  CB    . MET B 393 ? 0.54490 0.40500 0.38860 0.04330  0.11840  0.07510  393 MET B CB    
6626 C  CG    . MET B 393 ? 0.52940 0.39570 0.36110 0.04560  0.11220  0.06960  393 MET B CG    
6627 S  SD    . MET B 393 ? 0.61960 0.45550 0.40390 0.05990  0.11670  0.07330  393 MET B SD    
6628 C  CE    . MET B 393 ? 0.73280 0.57980 0.51640 0.05820  0.11270  0.06610  393 MET B CE    
6629 N  N     . GLY B 394 ? 0.59410 0.44240 0.45180 0.04140  0.11780  0.08240  394 GLY B N     
6630 C  CA    . GLY B 394 ? 0.57780 0.41610 0.44880 0.03810  0.12490  0.08750  394 GLY B CA    
6631 C  C     . GLY B 394 ? 0.58820 0.40210 0.43060 0.04960  0.12360  0.09400  394 GLY B C     
6632 O  O     . GLY B 394 ? 0.59080 0.38680 0.43290 0.04990  0.13390  0.10130  394 GLY B O     
6633 N  N     . LEU B 395 ? 0.50540 0.31870 0.32480 0.05920  0.10970  0.09140  395 LEU B N     
6634 C  CA    . LEU B 395 ? 0.57250 0.36350 0.36410 0.07230  0.10300  0.09660  395 LEU B CA    
6635 C  C     . LEU B 395 ? 0.62450 0.39470 0.37790 0.08350  0.10280  0.10090  395 LEU B C     
6636 O  O     . LEU B 395 ? 0.63320 0.38380 0.36010 0.09540  0.09380  0.10500  395 LEU B O     
6637 C  CB    . LEU B 395 ? 0.60890 0.41030 0.39950 0.07830  0.08570  0.09090  395 LEU B CB    
6638 C  CG    . LEU B 395 ? 0.59990 0.41250 0.42120 0.06940  0.08740  0.08800  395 LEU B CG    
6639 C  CD1   . LEU B 395 ? 0.67200 0.49870 0.49410 0.07480  0.07350  0.08130  395 LEU B CD1   
6640 C  CD2   . LEU B 395 ? 0.61000 0.40130 0.43660 0.07100  0.09240  0.09430  395 LEU B CD2   
6641 N  N     . GLU B 396 ? 0.64770 0.42040 0.39850 0.07990  0.11220  0.09970  396 GLU B N     
6642 C  CA    . GLU B 396 ? 0.70680 0.45690 0.42020 0.08920  0.11570  0.10330  396 GLU B CA    
6643 C  C     . GLU B 396 ? 0.69770 0.44700 0.38320 0.09940  0.09620  0.09740  396 GLU B C     
6644 O  O     . GLU B 396 ? 0.73050 0.45470 0.37760 0.11000  0.09360  0.10060  396 GLU B O     
6645 C  CB    . GLU B 396 ? 0.87810 0.59620 0.56840 0.09580  0.12510  0.11440  396 GLU B CB    
6646 C  CG    . GLU B 396 ? 1.12260 0.83970 0.84190 0.08570  0.14400  0.12030  396 GLU B CG    
6647 C  CD    . GLU B 396 ? 1.31100 1.02230 1.03350 0.08140  0.16500  0.12320  396 GLU B CD    
6648 O  OE1   . GLU B 396 ? 1.37020 1.09690 1.10080 0.07840  0.16560  0.11680  396 GLU B OE1   
6649 O  OE2   . GLU B 396 ? 1.53070 1.22080 1.24830 0.08150  0.18140  0.13230  396 GLU B OE2   
6650 N  N     . HIS B 397 ? 0.61460 0.39050 0.31960 0.09580  0.08250  0.08850  397 HIS B N     
6651 C  CA    . HIS B 397 ? 0.61420 0.39570 0.30250 0.10270  0.06380  0.08080  397 HIS B CA    
6652 C  C     . HIS B 397 ? 0.59580 0.38690 0.28820 0.09640  0.07010  0.07600  397 HIS B C     
6653 O  O     . HIS B 397 ? 0.56340 0.38050 0.27990 0.08850  0.06480  0.06870  397 HIS B O     
6654 C  CB    . HIS B 397 ? 0.59590 0.40200 0.30610 0.10160  0.04760  0.07360  397 HIS B CB    
6655 C  CG    . HIS B 397 ? 0.70200 0.49950 0.41050 0.11000  0.03860  0.07710  397 HIS B CG    
6656 N  ND1   . HIS B 397 ? 0.73010 0.51100 0.44050 0.10940  0.05090  0.08620  397 HIS B ND1   
6657 C  CD2   . HIS B 397 ? 0.67950 0.48410 0.38990 0.11930  0.01780  0.07210  397 HIS B CD2   
6658 C  CE1   . HIS B 397 ? 0.76130 0.53740 0.47280 0.11830  0.03810  0.08720  397 HIS B CE1   
6659 N  NE2   . HIS B 397 ? 0.72510 0.51620 0.43800 0.12510  0.01760  0.07860  397 HIS B NE2   
6660 N  N     . LYS B 398 ? 0.66640 0.43450 0.33380 0.10030  0.08220  0.08070  398 LYS B N     
6661 C  CA    . LYS B 398 ? 0.67420 0.44730 0.34750 0.09470  0.09320  0.07810  398 LYS B CA    
6662 C  C     . LYS B 398 ? 0.60420 0.38920 0.27210 0.09560  0.07820  0.06870  398 LYS B C     
6663 O  O     . LYS B 398 ? 0.57800 0.38280 0.26970 0.08670  0.08150  0.06410  398 LYS B O     
6664 C  CB    . LYS B 398 ? 0.79810 0.53980 0.44300 0.10030  0.11190  0.08590  398 LYS B CB    
6665 C  CG    . LYS B 398 ? 1.05060 0.78420 0.70940 0.09660  0.12920  0.09490  398 LYS B CG    
6666 C  CD    . LYS B 398 ? 1.57180 1.27560 1.20740 0.10070  0.15170  0.10290  398 LYS B CD    
6667 C  CE    . LYS B 398 ? 1.66880 1.36680 1.32350 0.09580  0.16830  0.11150  398 LYS B CE    
6668 N  NZ    . LYS B 398 ? 1.74820 1.41840 1.38530 0.09870  0.19340  0.11960  398 LYS B NZ    
6669 N  N     . ALA B 399 ? 0.62170 0.39430 0.25970 0.10630  0.06050  0.06570  399 ALA B N     
6670 C  CA    . ALA B 399 ? 0.61650 0.39850 0.24910 0.10760  0.04430  0.05610  399 ALA B CA    
6671 C  C     . ALA B 399 ? 0.54220 0.36050 0.21400 0.09800  0.03400  0.04850  399 ALA B C     
6672 O  O     . ALA B 399 ? 0.56780 0.40240 0.25420 0.09080  0.03370  0.04270  399 ALA B O     
6673 C  CB    . ALA B 399 ? 0.70130 0.46140 0.29630 0.12140  0.02490  0.05400  399 ALA B CB    
6674 N  N     . ALA B 400 ? 0.54860 0.37760 0.23560 0.09820  0.02630  0.04880  400 ALA B N     
6675 C  CA    . ALA B 400 ? 0.51410 0.37460 0.23510 0.08970  0.01850  0.04220  400 ALA B CA    
6676 C  C     . ALA B 400 ? 0.47070 0.34870 0.22220 0.07530  0.03460  0.04350  400 ALA B C     
6677 O  O     . ALA B 400 ? 0.38860 0.28960 0.16220 0.06630  0.03080  0.03710  400 ALA B O     
6678 C  CB    . ALA B 400 ? 0.53080 0.39460 0.25790 0.09530  0.00880  0.04290  400 ALA B CB    
6679 N  N     . GLY B 401 ? 0.59930 0.46540 0.35260 0.07320  0.05150  0.05150  401 GLY B N     
6680 C  CA    . GLY B 401 ? 0.51720 0.39720 0.30030 0.06070  0.06470  0.05260  401 GLY B CA    
6681 C  C     . GLY B 401 ? 0.52910 0.41620 0.31600 0.05630  0.06710  0.04840  401 GLY B C     
6682 O  O     . GLY B 401 ? 0.53550 0.44470 0.34830 0.04620  0.06490  0.04370  401 GLY B O     
6683 N  N     . GLU B 402 ? 0.50370 0.36930 0.26170 0.06460  0.07150  0.05030  402 GLU B N     
6684 C  CA    . GLU B 402 ? 0.51710 0.38380 0.27260 0.06290  0.07510  0.04670  402 GLU B CA    
6685 C  C     . GLU B 402 ? 0.51020 0.39790 0.27560 0.05850  0.05930  0.03740  402 GLU B C     
6686 O  O     . GLU B 402 ? 0.47270 0.37610 0.25860 0.05030  0.06180  0.03400  402 GLU B O     
6687 C  CB    . GLU B 402 ? 0.65840 0.49370 0.37280 0.07460  0.08070  0.04960  402 GLU B CB    
6688 C  CG    . GLU B 402 ? 0.79770 0.62890 0.50730 0.07400  0.08930  0.04730  402 GLU B CG    
6689 C  CD    . GLU B 402 ? 0.95290 0.74850 0.61840 0.08560  0.09840  0.05080  402 GLU B CD    
6690 O  OE1   . GLU B 402 ? 0.90170 0.67500 0.54660 0.09210  0.10590  0.05790  402 GLU B OE1   
6691 O  OE2   . GLU B 402 ? 1.28790 1.07600 0.93770 0.08830  0.09900  0.04660  402 GLU B OE2   
6692 N  N     . LYS B 403 ? 0.50890 0.39600 0.26050 0.06430  0.04300  0.03330  403 LYS B N     
6693 C  CA    . LYS B 403 ? 0.52530 0.43140 0.28750 0.06030  0.02770  0.02410  403 LYS B CA    
6694 C  C     . LYS B 403 ? 0.39510 0.32890 0.19380 0.04710  0.02850  0.02140  403 LYS B C     
6695 O  O     . LYS B 403 ? 0.37170 0.31950 0.18380 0.03960  0.02630  0.01600  403 LYS B O     
6696 C  CB    . LYS B 403 ? 0.57790 0.48020 0.32610 0.06920  0.00950  0.02030  403 LYS B CB    
6697 C  CG    . LYS B 403 ? 0.85900 0.73980 0.57330 0.08030  -0.00080 0.01720  403 LYS B CG    
6698 C  CD    . LYS B 403 ? 1.21280 1.09240 0.91970 0.08920  -0.02250 0.01240  403 LYS B CD    
6699 C  CE    . LYS B 403 ? 1.28120 1.19060 1.02100 0.08230  -0.03520 0.00390  403 LYS B CE    
6700 N  NZ    . LYS B 403 ? 1.10860 1.03290 0.86310 0.07240  -0.03500 -0.00280 403 LYS B NZ    
6701 N  N     . ALA B 404 ? 0.40890 0.34800 0.22110 0.04450  0.03150  0.02520  404 ALA B N     
6702 C  CA    . ALA B 404 ? 0.38210 0.34330 0.22390 0.03250  0.03190  0.02250  404 ALA B CA    
6703 C  C     . ALA B 404 ? 0.37590 0.34370 0.23590 0.02330  0.04200  0.02400  404 ALA B C     
6704 O  O     . ALA B 404 ? 0.31920 0.30320 0.19640 0.01400  0.03890  0.01930  404 ALA B O     
6705 C  CB    . ALA B 404 ? 0.43010 0.39130 0.27800 0.03330  0.03350  0.02610  404 ALA B CB    
6706 N  N     . LEU B 405 ? 0.39280 0.34630 0.24800 0.02680  0.05410  0.03060  405 LEU B N     
6707 C  CA    . LEU B 405 ? 0.37470 0.33290 0.24810 0.02060  0.06350  0.03220  405 LEU B CA    
6708 C  C     . LEU B 405 ? 0.37160 0.33330 0.24220 0.02040  0.06210  0.02750  405 LEU B C     
6709 O  O     . LEU B 405 ? 0.36840 0.34230 0.25880 0.01360  0.06300  0.02590  405 LEU B O     
6710 C  CB    . LEU B 405 ? 0.40960 0.34960 0.27860 0.02540  0.07870  0.03990  405 LEU B CB    
6711 C  CG    . LEU B 405 ? 0.41040 0.34670 0.28800 0.02420  0.08260  0.04490  405 LEU B CG    
6712 C  CD1   . LEU B 405 ? 0.51760 0.43360 0.38910 0.02930  0.09930  0.05250  405 LEU B CD1   
6713 C  CD2   . LEU B 405 ? 0.49010 0.44530 0.39830 0.01310  0.07880  0.04290  405 LEU B CD2   
6714 N  N     . LYS B 406 ? 0.40660 0.35610 0.25110 0.02830  0.05890  0.02530  406 LYS B N     
6715 C  CA    . LYS B 406 ? 0.46330 0.41330 0.30110 0.02900  0.05670  0.02000  406 LYS B CA    
6716 C  C     . LYS B 406 ? 0.39100 0.36210 0.24460 0.02040  0.04460  0.01270  406 LYS B C     
6717 O  O     . LYS B 406 ? 0.46030 0.43790 0.32220 0.01670  0.04570  0.00950  406 LYS B O     
6718 C  CB    . LYS B 406 ? 0.48740 0.41610 0.29000 0.03990  0.05410  0.01870  406 LYS B CB    
6719 C  CG    . LYS B 406 ? 0.67170 0.57570 0.45460 0.04790  0.07010  0.02530  406 LYS B CG    
6720 C  CD    . LYS B 406 ? 0.68500 0.56340 0.42670 0.05950  0.06680  0.02420  406 LYS B CD    
6721 C  CE    . LYS B 406 ? 0.91050 0.76150 0.63040 0.06690  0.08590  0.03130  406 LYS B CE    
6722 N  NZ    . LYS B 406 ? 0.99260 0.81290 0.66580 0.07930  0.08280  0.03150  406 LYS B NZ    
6723 N  N     . LYS B 407 ? 0.48580 0.46480 0.34220 0.01810  0.03440  0.01020  407 LYS B N     
6724 C  CA    . LYS B 407 ? 0.38250 0.37770 0.25330 0.00900  0.02550  0.00380  407 LYS B CA    
6725 C  C     . LYS B 407 ? 0.34370 0.35180 0.23850 -0.00160 0.03030  0.00500  407 LYS B C     
6726 O  O     . LYS B 407 ? 0.34030 0.35160 0.24570 -0.00730 0.02680  0.00100  407 LYS B O     
6727 C  CB    . LYS B 407 ? 0.49090 0.48790 0.36020 0.00990  0.01670  0.00170  407 LYS B CB    
6728 C  CG    . LYS B 407 ? 0.58990 0.57890 0.43950 0.02050  0.00520  -0.00190 407 LYS B CG    
6729 C  CD    . LYS B 407 ? 0.68190 0.67600 0.53330 0.01750  -0.00480 -0.01010 407 LYS B CD    
6730 C  CE    . LYS B 407 ? 0.87240 0.87120 0.72410 0.02300  -0.02130 -0.01650 407 LYS B CE    
6731 N  NZ    . LYS B 407 ? 0.87270 0.85880 0.70460 0.03660  -0.02790 -0.01460 407 LYS B NZ    
6732 N  N     . ALA B 408 ? 0.32790 0.33650 0.23230 -0.00180 0.03660  0.01100  408 ALA B N     
6733 C  CA    . ALA B 408 ? 0.34130 0.36020 0.26870 -0.00800 0.03830  0.01340  408 ALA B CA    
6734 C  C     . ALA B 408 ? 0.32580 0.34530 0.25810 -0.00760 0.04440  0.01530  408 ALA B C     
6735 O  O     . ALA B 408 ? 0.37520 0.40450 0.32360 -0.00980 0.03990  0.01560  408 ALA B O     
6736 C  CB    . ALA B 408 ? 0.32540 0.34060 0.25860 -0.00840 0.04420  0.01930  408 ALA B CB    
6737 N  N     . ILE B 409 ? 0.39550 0.39940 0.31630 -0.00020 0.05380  0.01760  409 ILE B N     
6738 C  CA    . ILE B 409 ? 0.38830 0.38720 0.31350 0.00210  0.06260  0.01870  409 ILE B CA    
6739 C  C     . ILE B 409 ? 0.38490 0.38860 0.30550 0.00150  0.05730  0.01290  409 ILE B C     
6740 O  O     . ILE B 409 ? 0.37780 0.38510 0.31240 -0.00090 0.06060  0.01370  409 ILE B O     
6741 C  CB    . ILE B 409 ? 0.44470 0.42330 0.35310 0.01150  0.07530  0.02200  409 ILE B CB    
6742 C  CG1   . ILE B 409 ? 0.46020 0.43260 0.37970 0.01160  0.08490  0.02890  409 ILE B CG1   
6743 C  CG2   . ILE B 409 ? 0.44040 0.41110 0.34830 0.01540  0.08550  0.02130  409 ILE B CG2   
6744 C  CD1   . ILE B 409 ? 0.69170 0.64140 0.59170 0.02090  0.09910  0.03350  409 ILE B CD1   
6745 N  N     . ALA B 410 ? 0.38930 0.39140 0.29130 0.00380  0.04900  0.00730  410 ALA B N     
6746 C  CA    . ALA B 410 ? 0.44620 0.45010 0.34140 0.00390  0.04340  0.00050  410 ALA B CA    
6747 C  C     . ALA B 410 ? 0.42440 0.44350 0.33930 -0.00050 0.03760  0.00140  410 ALA B C     
6748 O  O     . ALA B 410 ? 0.51220 0.52670 0.42540 -0.00000 0.03980  -0.00050 410 ALA B O     
6749 C  CB    . ALA B 410 ? 0.45180 0.45100 0.32800 0.00590  0.03300  -0.00580 410 ALA B CB    
6750 N  N     . ILE B 411 ? 0.37390 0.38920 0.29840 0.00210  0.03470  0.00650  411 ILE B N     
6751 C  CA    . ILE B 411 ? 0.35040 0.36870 0.28880 -0.01120 0.03040  0.00450  411 ILE B CA    
6752 C  C     . ILE B 411 ? 0.32510 0.34740 0.28230 -0.01610 0.03670  0.01060  411 ILE B C     
6753 O  O     . ILE B 411 ? 0.37770 0.40440 0.34390 -0.02490 0.03340  0.00930  411 ILE B O     
6754 C  CB    . ILE B 411 ? 0.38710 0.41100 0.33300 -0.01610 0.02300  0.00290  411 ILE B CB    
6755 C  CG1   . ILE B 411 ? 0.38930 0.41320 0.32430 -0.01290 0.01640  -0.00290 411 ILE B CG1   
6756 C  CG2   . ILE B 411 ? 0.38820 0.42170 0.34940 -0.02880 0.01630  0.00140  411 ILE B CG2   
6757 C  CD1   . ILE B 411 ? 0.45090 0.48110 0.39230 -0.01510 0.01300  -0.00380 411 ILE B CD1   
6758 N  N     . MET B 412 ? 0.35320 0.37850 0.31980 -0.01130 0.04330  0.01810  412 MET B N     
6759 C  CA    . MET B 412 ? 0.43190 0.46560 0.42200 -0.01880 0.04470  0.02310  412 MET B CA    
6760 C  C     . MET B 412 ? 0.34420 0.37430 0.34030 -0.02040 0.05360  0.02110  412 MET B C     
6761 O  O     . MET B 412 ? 0.41450 0.44740 0.43360 -0.02610 0.05210  0.02320  412 MET B O     
6762 C  CB    . MET B 412 ? 0.42940 0.46310 0.42200 -0.02200 0.04850  0.02380  412 MET B CB    
6763 C  CG    . MET B 412 ? 0.46410 0.50070 0.45890 -0.02070 0.03950  0.02620  412 MET B CG    
6764 S  SD    . MET B 412 ? 0.43520 0.46550 0.42930 -0.02480 0.04790  0.02660  412 MET B SD    
6765 C  CE    . MET B 412 ? 0.50110 0.53160 0.52310 -0.03150 0.04850  0.02860  412 MET B CE    
6766 N  N     . GLU B 413 ? 0.43940 0.45910 0.41690 -0.01190 0.06190  0.01740  413 GLU B N     
6767 C  CA    . GLU B 413 ? 0.41080 0.42180 0.39330 -0.00720 0.07310  0.01610  413 GLU B CA    
6768 C  C     . GLU B 413 ? 0.38170 0.39670 0.37530 -0.01400 0.06910  0.01460  413 GLU B C     
6769 O  O     . GLU B 413 ? 0.45700 0.47200 0.47670 -0.01410 0.07540  0.01660  413 GLU B O     
6770 C  CB    . GLU B 413 ? 0.46790 0.46400 0.41960 0.00290  0.07890  0.01110  413 GLU B CB    
6771 C  CG    . GLU B 413 ? 0.62360 0.60910 0.56980 0.00930  0.08920  0.01470  413 GLU B CG    
6772 C  CD    . GLU B 413 ? 0.71470 0.68290 0.62730 0.01840  0.09260  0.01060  413 GLU B CD    
6773 O  OE1   . GLU B 413 ? 0.72620 0.69380 0.61830 0.01910  0.08150  0.00380  413 GLU B OE1   
6774 O  OE2   . GLU B 413 ? 0.78130 0.73510 0.68780 0.02450  0.10620  0.01400  413 GLU B OE2   
6775 N  N     . VAL B 414 ? 0.36180 0.37980 0.33880 -0.02080 0.05730  0.01040  414 VAL B N     
6776 C  CA    . VAL B 414 ? 0.36360 0.38430 0.34980 -0.02880 0.04270  0.00760  414 VAL B CA    
6777 C  C     . VAL B 414 ? 0.27690 0.30560 0.29010 -0.03860 0.03390  0.01460  414 VAL B C     
6778 O  O     . VAL B 414 ? 0.26220 0.28920 0.29670 -0.04020 0.02930  0.01700  414 VAL B O     
6779 C  CB    . VAL B 414 ? 0.34550 0.36730 0.30920 -0.03300 0.03100  0.00040  414 VAL B CB    
6780 C  CG1   . VAL B 414 ? 0.49490 0.51810 0.46820 -0.04360 0.01820  -0.00030 414 VAL B CG1   
6781 C  CG2   . VAL B 414 ? 0.38730 0.39830 0.32550 -0.02320 0.03420  -0.00800 414 VAL B CG2   
6782 N  N     . ALA B 415 ? 0.25100 0.28400 0.26230 -0.04130 0.02920  0.01680  415 ALA B N     
6783 C  CA    . ALA B 415 ? 0.30380 0.33570 0.32930 -0.04510 0.01750  0.01910  415 ALA B CA    
6784 C  C     . ALA B 415 ? 0.30240 0.33510 0.35510 -0.04530 0.02140  0.02170  415 ALA B C     
6785 O  O     . ALA B 415 ? 0.34270 0.37450 0.40740 -0.04840 0.00970  0.02310  415 ALA B O     
6786 C  CB    . ALA B 415 ? 0.37660 0.40800 0.38630 -0.04420 0.01240  0.01620  415 ALA B CB    
6787 N  N     . HIS B 416 ? 0.32060 0.35740 0.37480 -0.04160 0.03270  0.02370  416 HIS B N     
6788 C  CA    . HIS B 416 ? 0.30280 0.34140 0.38420 -0.03820 0.03490  0.02750  416 HIS B CA    
6789 C  C     . HIS B 416 ? 0.32940 0.36700 0.43570 -0.03020 0.04680  0.02990  416 HIS B C     
6790 O  O     . HIS B 416 ? 0.31570 0.35480 0.45300 -0.02760 0.04770  0.03250  416 HIS B O     
6791 C  CB    . HIS B 416 ? 0.33990 0.37760 0.41370 -0.03530 0.04240  0.02810  416 HIS B CB    
6792 C  CG    . HIS B 416 ? 0.38860 0.42560 0.44910 -0.04230 0.03320  0.02490  416 HIS B CG    
6793 N  ND1   . HIS B 416 ? 0.38440 0.41270 0.42050 -0.04090 0.03390  0.01810  416 HIS B ND1   
6794 C  CD2   . HIS B 416 ? 0.47310 0.50940 0.54610 -0.04570 0.02710  0.02490  416 HIS B CD2   
6795 C  CE1   . HIS B 416 ? 0.41670 0.44130 0.45910 -0.04020 0.02980  0.01850  416 HIS B CE1   
6796 N  NE2   . HIS B 416 ? 0.40980 0.43970 0.46510 -0.04810 0.02560  0.01900  416 HIS B NE2   
6797 N  N     . GLY B 417 ? 0.34560 0.37890 0.43820 -0.02540 0.05740  0.02780  417 GLY B N     
6798 C  CA    . GLY B 417 ? 0.31070 0.33810 0.41800 -0.01610 0.07430  0.02750  417 GLY B CA    
6799 C  C     . GLY B 417 ? 0.37600 0.39370 0.46580 -0.00740 0.09080  0.02700  417 GLY B C     
6800 O  O     . GLY B 417 ? 0.38710 0.40600 0.47580 -0.00890 0.08900  0.02940  417 GLY B O     
6801 N  N     . LYS B 418 ? 0.36960 0.37490 0.44370 0.00150  0.10590  0.02380  418 LYS B N     
6802 C  CA    . LYS B 418 ? 0.48280 0.47320 0.53090 0.00940  0.11910  0.02370  418 LYS B CA    
6803 C  C     . LYS B 418 ? 0.46430 0.45260 0.53800 0.01050  0.12930  0.02920  418 LYS B C     
6804 O  O     . LYS B 418 ? 0.50760 0.48600 0.56240 0.01350  0.13640  0.03120  418 LYS B O     
6805 C  CB    . LYS B 418 ? 0.57310 0.54790 0.60060 0.01820  0.13140  0.01870  418 LYS B CB    
6806 C  CG    . LYS B 418 ? 0.80290 0.77340 0.79380 0.01930  0.12200  0.01120  418 LYS B CG    
6807 C  CD    . LYS B 418 ? 0.97690 0.93170 0.95280 0.02770  0.13150  0.00430  418 LYS B CD    
6808 C  CE    . LYS B 418 ? 0.91990 0.87010 0.86630 0.02770  0.11920  -0.00530 418 LYS B CE    
6809 N  NZ    . LYS B 418 ? 1.11880 1.06580 1.02820 0.02770  0.10630  -0.00770 418 LYS B NZ    
6810 N  N     . ASP B 419 ? 0.47100 0.46790 0.58990 0.00810  0.12920  0.03170  419 ASP B N     
6811 C  CA    . ASP B 419 ? 0.52150 0.51670 0.67320 0.00910  0.13940  0.03610  419 ASP B CA    
6812 C  C     . ASP B 419 ? 0.44250 0.44940 0.61640 0.00210  0.12570  0.03900  419 ASP B C     
6813 O  O     . ASP B 419 ? 0.50130 0.50870 0.70930 0.00210  0.13110  0.04200  419 ASP B O     
6814 C  CB    . ASP B 419 ? 0.58210 0.57810 0.77430 0.01180  0.14680  0.03610  419 ASP B CB    
6815 C  CG    . ASP B 419 ? 0.90060 0.91130 1.12030 0.00690  0.12690  0.03500  419 ASP B CG    
6816 O  OD1   . ASP B 419 ? 0.56240 0.57910 0.75910 0.00250  0.11230  0.03300  419 ASP B OD1   
6817 O  OD2   . ASP B 419 ? 0.85630 0.87120 1.12120 0.00730  0.12520  0.03650  419 ASP B OD2   
6818 N  N     . HIS B 420 ? 0.37510 0.39000 0.52880 -0.00410 0.10840  0.03750  420 HIS B N     
6819 C  CA    . HIS B 420 ? 0.34570 0.36960 0.51360 -0.01110 0.09410  0.03900  420 HIS B CA    
6820 C  C     . HIS B 420 ? 0.41400 0.43110 0.57860 -0.00960 0.10440  0.04160  420 HIS B C     
6821 O  O     . HIS B 420 ? 0.50490 0.51180 0.63750 -0.00560 0.11400  0.04160  420 HIS B O     
6822 C  CB    . HIS B 420 ? 0.32520 0.35550 0.46660 -0.01830 0.07590  0.03630  420 HIS B CB    
6823 C  CG    . HIS B 420 ? 0.29740 0.33460 0.45240 -0.02620 0.05890  0.03660  420 HIS B CG    
6824 N  ND1   . HIS B 420 ? 0.34360 0.37980 0.49760 -0.02860 0.05870  0.03740  420 HIS B ND1   
6825 C  CD2   . HIS B 420 ? 0.38900 0.43100 0.55580 -0.03170 0.04120  0.03600  420 HIS B CD2   
6826 C  CE1   . HIS B 420 ? 0.38320 0.42340 0.54740 -0.03530 0.04240  0.03660  420 HIS B CE1   
6827 N  NE2   . HIS B 420 ? 0.39990 0.44280 0.57020 -0.03690 0.03110  0.03580  420 HIS B NE2   
6828 N  N     . PRO B 421 ? 0.48800 0.50940 0.68610 -0.01250 0.10180  0.04390  421 PRO B N     
6829 C  CA    . PRO B 421 ? 0.50060 0.51560 0.69950 -0.01200 0.11170  0.04670  421 PRO B CA    
6830 C  C     . PRO B 421 ? 0.47370 0.48480 0.63250 -0.01370 0.10800  0.04590  421 PRO B C     
6831 O  O     . PRO B 421 ? 0.56140 0.56150 0.70910 -0.00990 0.12130  0.04870  421 PRO B O     
6832 C  CB    . PRO B 421 ? 0.53590 0.56010 0.77520 -0.01750 0.10030  0.04750  421 PRO B CB    
6833 C  CG    . PRO B 421 ? 0.49860 0.52920 0.76920 -0.01680 0.09320  0.04680  421 PRO B CG    
6834 C  CD    . PRO B 421 ? 0.50650 0.53760 0.74530 -0.01600 0.08850  0.04410  421 PRO B CD    
6835 N  N     . TYR B 422 ? 0.39400 0.41250 0.53330 -0.01920 0.09060  0.04250  422 TYR B N     
6836 C  CA    . TYR B 422 ? 0.40530 0.42110 0.51030 -0.02090 0.08540  0.04110  422 TYR B CA    
6837 C  C     . TYR B 422 ? 0.39620 0.40120 0.47000 -0.01310 0.09620  0.04120  422 TYR B C     
6838 O  O     . TYR B 422 ? 0.45960 0.45660 0.51430 -0.01080 0.09950  0.04260  422 TYR B O     
6839 C  CB    . TYR B 422 ? 0.37480 0.39920 0.46630 -0.02830 0.06710  0.03690  422 TYR B CB    
6840 C  CG    . TYR B 422 ? 0.38980 0.41920 0.49770 -0.03660 0.05410  0.03590  422 TYR B CG    
6841 C  CD1   . TYR B 422 ? 0.36990 0.39750 0.49960 -0.03780 0.05680  0.03830  422 TYR B CD1   
6842 C  CD2   . TYR B 422 ? 0.35740 0.39060 0.45660 -0.04330 0.03940  0.03190  422 TYR B CD2   
6843 C  CE1   . TYR B 422 ? 0.40460 0.43470 0.54720 -0.04520 0.04340  0.03650  422 TYR B CE1   
6844 C  CE2   . TYR B 422 ? 0.48660 0.51970 0.59500 -0.04990 0.02760  0.02980  422 TYR B CE2   
6845 C  CZ    . TYR B 422 ? 0.42300 0.45500 0.55300 -0.05090 0.02850  0.03210  422 TYR B CZ    
6846 O  OH    . TYR B 422 ? 0.56200 0.59260 0.70050 -0.05700 0.01540  0.02960  422 TYR B OH    
6847 N  N     . ILE B 423 ? 0.40620 0.40920 0.47480 -0.00880 0.10090  0.03980  423 ILE B N     
6848 C  CA    . ILE B 423 ? 0.38960 0.38030 0.42550 -0.00120 0.10880  0.03890  423 ILE B CA    
6849 C  C     . ILE B 423 ? 0.44190 0.41570 0.47510 0.00560  0.12790  0.04350  423 ILE B C     
6850 O  O     . ILE B 423 ? 0.50540 0.46640 0.50850 0.01070  0.13170  0.04450  423 ILE B O     
6851 C  CB    . ILE B 423 ? 0.46520 0.45700 0.49490 0.00100  0.10820  0.03530  423 ILE B CB    
6852 C  CG1   . ILE B 423 ? 0.57440 0.57930 0.59690 -0.00550 0.09030  0.03110  423 ILE B CG1   
6853 C  CG2   . ILE B 423 ? 0.49550 0.47070 0.49220 0.00980  0.11780  0.03410  423 ILE B CG2   
6854 C  CD1   . ILE B 423 ? 0.63900 0.64630 0.66080 -0.00500 0.08890  0.02790  423 ILE B CD1   
6855 N  N     . SER B 424 ? 0.49800 0.47100 0.56400 0.00580  0.13970  0.04660  424 SER B N     
6856 C  CA    . SER B 424 ? 0.47530 0.43220 0.54520 0.01100  0.16030  0.05170  424 SER B CA    
6857 C  C     . SER B 424 ? 0.45880 0.41130 0.52140 0.00960  0.16000  0.05490  424 SER B C     
6858 O  O     . SER B 424 ? 0.46580 0.40010 0.50400 0.01560  0.17240  0.05840  424 SER B O     
6859 C  CB    . SER B 424 ? 0.47140 0.43230 0.58820 0.00980  0.17080  0.05400  424 SER B CB    
6860 O  OG    . SER B 424 ? 0.68150 0.64500 0.80760 0.01170  0.17250  0.05140  424 SER B OG    
6861 N  N     . GLU B 425 ? 0.41630 0.38350 0.49840 0.00200  0.14580  0.05390  425 GLU B N     
6862 C  CA    . GLU B 425 ? 0.56520 0.52890 0.64380 -0.00010 0.14470  0.05640  425 GLU B CA    
6863 C  C     . GLU B 425 ? 0.51180 0.46510 0.54800 0.00430  0.14160  0.05630  425 GLU B C     
6864 O  O     . GLU B 425 ? 0.55870 0.49720 0.58200 0.00820  0.15140  0.06070  425 GLU B O     
6865 C  CB    . GLU B 425 ? 0.49390 0.47390 0.59370 -0.00940 0.12730  0.05390  425 GLU B CB    
6866 C  CG    . GLU B 425 ? 0.84660 0.83470 0.99190 -0.01410 0.12810  0.05500  425 GLU B CG    
6867 C  CD    . GLU B 425 ? 0.95490 0.95500 1.11260 -0.02320 0.10880  0.05200  425 GLU B CD    
6868 O  OE1   . GLU B 425 ? 0.95460 0.95270 1.08950 -0.02580 0.10150  0.05090  425 GLU B OE1   
6869 O  OE2   . GLU B 425 ? 1.10600 1.11550 1.29600 -0.02740 0.10070  0.05070  425 GLU B OE2   
6870 N  N     . ILE B 426 ? 0.39390 0.35460 0.41030 0.00380  0.12750  0.05130  426 ILE B N     
6871 C  CA    . ILE B 426 ? 0.45160 0.40600 0.43360 0.00750  0.12060  0.05000  426 ILE B CA    
6872 C  C     . ILE B 426 ? 0.43420 0.36730 0.38610 0.01760  0.13310  0.05250  426 ILE B C     
6873 O  O     . ILE B 426 ? 0.53250 0.45250 0.45900 0.02280  0.13360  0.05480  426 ILE B O     
6874 C  CB    . ILE B 426 ? 0.42000 0.38940 0.39460 0.00350  0.10280  0.04350  426 ILE B CB    
6875 C  CG1   . ILE B 426 ? 0.41280 0.39810 0.40920 -0.00620 0.09100  0.04160  426 ILE B CG1   
6876 C  CG2   . ILE B 426 ? 0.46670 0.43020 0.41030 0.00830  0.09590  0.04170  426 ILE B CG2   
6877 C  CD1   . ILE B 426 ? 0.40890 0.40870 0.40500 -0.01160 0.07710  0.03620  426 ILE B CD1   
6878 N  N     . LYS B 427 ? 0.50440 0.43240 0.45810 0.02080  0.14330  0.05240  427 LYS B N     
6879 C  CA    . LYS B 427 ? 0.59800 0.50230 0.52140 0.03040  0.15740  0.05490  427 LYS B CA    
6880 C  C     . LYS B 427 ? 0.53890 0.42340 0.45870 0.03450  0.17560  0.06240  427 LYS B C     
6881 O  O     . LYS B 427 ? 0.69620 0.55800 0.58010 0.04270  0.18250  0.06520  427 LYS B O     
6882 C  CB    . LYS B 427 ? 0.67080 0.57330 0.59930 0.03230  0.16630  0.05290  427 LYS B CB    
6883 C  CG    . LYS B 427 ? 0.60870 0.52080 0.52380 0.03180  0.15140  0.04570  427 LYS B CG    
6884 C  CD    . LYS B 427 ? 0.68500 0.59060 0.60270 0.03530  0.16330  0.04410  427 LYS B CD    
6885 C  CE    . LYS B 427 ? 0.73650 0.65370 0.64920 0.03360  0.14930  0.03670  427 LYS B CE    
6886 N  NZ    . LYS B 427 ? 0.92490 0.83420 0.79820 0.03800  0.13770  0.03230  427 LYS B NZ    
6887 N  N     . GLN B 428 ? 0.57530 0.46740 0.53170 0.02900  0.18260  0.06550  428 GLN B N     
6888 C  CA    . GLN B 428 ? 0.64370 0.51920 0.60230 0.03140  0.19970  0.07260  428 GLN B CA    
6889 C  C     . GLN B 428 ? 0.73880 0.60720 0.67230 0.03320  0.19160  0.07450  428 GLN B C     
6890 O  O     . GLN B 428 ? 0.77620 0.62180 0.68750 0.03940  0.20500  0.08040  428 GLN B O     
6891 C  CB    . GLN B 428 ? 0.69650 0.58520 0.70470 0.02400  0.20500  0.07440  428 GLN B CB    
6892 C  CG    . GLN B 428 ? 0.86560 0.76060 0.90640 0.02270  0.21490  0.07350  428 GLN B CG    
6893 C  CD    . GLN B 428 ? 0.92050 0.83340 1.01380 0.01450  0.21200  0.07340  428 GLN B CD    
6894 O  OE1   . GLN B 428 ? 0.81750 0.72600 0.92910 0.01270  0.22120  0.07770  428 GLN B OE1   
6895 N  NE2   . GLN B 428 ? 0.96030 0.89270 1.07840 0.00980  0.19860  0.06860  428 GLN B NE2   
6896 N  N     . GLU B 429 ? 0.61260 0.49940 0.54940 0.02790  0.17030  0.06980  429 GLU B N     
6897 C  CA    . GLU B 429 ? 0.63190 0.51470 0.55060 0.02900  0.16130  0.07100  429 GLU B CA    
6898 C  C     . GLU B 429 ? 0.73730 0.60240 0.61040 0.03870  0.15790  0.07110  429 GLU B C     
6899 O  O     . GLU B 429 ? 0.72960 0.58190 0.58230 0.04320  0.15630  0.07450  429 GLU B O     
6900 C  CB    . GLU B 429 ? 0.58200 0.48830 0.51840 0.02040  0.14160  0.06560  429 GLU B CB    
6901 C  CG    . GLU B 429 ? 0.63920 0.55960 0.61620 0.01110  0.14210  0.06550  429 GLU B CG    
6902 C  CD    . GLU B 429 ? 0.63300 0.57340 0.62210 0.00270  0.12300  0.05980  429 GLU B CD    
6903 O  OE1   . GLU B 429 ? 0.74300 0.68260 0.71530 0.00360  0.11420  0.05860  429 GLU B OE1   
6904 O  OE2   . GLU B 429 ? 0.84490 0.79970 0.85990 -0.00400 0.11800  0.05690  429 GLU B OE2   
6905 N  N     . ILE B 430 ? 0.63260 0.49510 0.48980 0.04270  0.15660  0.06750  430 ILE B N     
6906 C  CA    . ILE B 430 ? 0.69530 0.53900 0.50870 0.05240  0.15280  0.06680  430 ILE B CA    
6907 C  C     . ILE B 430 ? 0.78200 0.59300 0.56710 0.06140  0.17310  0.07400  430 ILE B C     
6908 O  O     . ILE B 430 ? 1.09630 0.88660 0.84510 0.06950  0.17080  0.07670  430 ILE B O     
6909 C  CB    . ILE B 430 ? 0.58480 0.43610 0.39120 0.05290  0.14440  0.05970  430 ILE B CB    
6910 C  CG1   . ILE B 430 ? 0.56970 0.44930 0.39560 0.04510  0.12350  0.05280  430 ILE B CG1   
6911 C  CG2   . ILE B 430 ? 0.58460 0.41200 0.34440 0.06370  0.14220  0.05890  430 ILE B CG2   
6912 C  CD1   . ILE B 430 ? 0.58290 0.47390 0.41100 0.04300  0.11630  0.04590  430 ILE B CD1   
6913 N  N     . GLU B 431 ? 1.20020 1.00510 1.00170 0.06040  0.19350  0.07730  431 GLU B N     
6914 C  CA    . GLU B 431 ? 1.70010 1.47300 1.47840 0.06790  0.21750  0.08470  431 GLU B CA    
6915 C  C     . GLU B 431 ? 1.49610 1.26830 1.30470 0.06340  0.23400  0.09150  431 GLU B C     
6916 O  O     . GLU B 431 ? 1.42280 1.18560 1.24660 0.06340  0.25650  0.09540  431 GLU B O     
6917 C  CB    . GLU B 431 ? 1.99400 1.75570 1.76460 0.07160  0.23180  0.08350  431 GLU B CB    
6918 C  CG    . GLU B 431 ? 1.90030 1.65990 1.63920 0.07630  0.21660  0.07660  431 GLU B CG    
6919 C  CD    . GLU B 431 ? 1.96850 1.70270 1.65450 0.08620  0.20840  0.07760  431 GLU B CD    
6920 O  OE1   . GLU B 431 ? 1.95270 1.65750 1.61200 0.09280  0.22430  0.08490  431 GLU B OE1   
6921 O  OE2   . GLU B 431 ? 1.51550 1.25860 1.18720 0.08730  0.18590  0.07110  431 GLU B OE2   
6922 N  N     . SER B 432 ? 1.75030 1.53260 1.56910 0.05930  0.22280  0.09260  432 SER B N     
6923 C  CA    . SER B 432 ? 1.78040 1.55910 1.62200 0.05550  0.23600  0.09910  432 SER B CA    
6924 C  C     . SER B 432 ? 2.20390 1.96250 2.01130 0.06150  0.23330  0.10430  432 SER B C     
6925 O  O     . SER B 432 ? 1.99510 1.72710 1.78510 0.06640  0.25220  0.11230  432 SER B O     
6926 C  CB    . SER B 432 ? 1.57670 1.38700 1.46890 0.04370  0.22500  0.09520  432 SER B CB    
6927 O  OG    . SER B 432 ? 1.51750 1.32450 1.43210 0.03960  0.23530  0.10080  432 SER B OG    
6928 N  N     . HIS B 433 ? 2.62070 2.39100 2.41900 0.06140  0.21020  0.09980  433 HIS B N     
6929 C  CA    . HIS B 433 ? 2.20980 1.96150 1.97370 0.06860  0.20350  0.10380  433 HIS B CA    
6930 C  C     . HIS B 433 ? 1.99900 1.72330 1.70970 0.08090  0.20300  0.10460  433 HIS B C     
6931 O  O     . HIS B 433 ? 1.75960 1.48490 1.46130 0.08280  0.20230  0.10000  433 HIS B O     
6932 C  CB    . HIS B 433 ? 1.90630 1.67980 1.68110 0.06490  0.17980  0.09830  433 HIS B CB    
6933 C  CG    . HIS B 433 ? 2.01230 1.80810 1.83250 0.05350  0.17850  0.09730  433 HIS B CG    
6934 N  ND1   . HIS B 433 ? 1.92030 1.74400 1.77640 0.04390  0.17170  0.09060  433 HIS B ND1   
6935 C  CD2   . HIS B 433 ? 1.81930 1.61130 1.65300 0.05010  0.18240  0.10210  433 HIS B CD2   
6936 C  CE1   . HIS B 433 ? 1.69520 1.53100 1.58350 0.03530  0.17070  0.09090  433 HIS B CE1   
6937 N  NE2   . HIS B 433 ? 1.71400 1.53120 1.59070 0.03860  0.17740  0.09760  433 HIS B NE2   
6938 N  N     . THR C 5   ? 1.04050 1.01990 1.06820 0.09110  -0.01750 -0.02980 526 THR C N     
6939 C  CA    . THR C 5   ? 0.91170 0.89430 0.94260 0.09330  -0.01780 -0.03810 526 THR C CA    
6940 C  C     . THR C 5   ? 0.93320 0.92090 0.96690 0.09480  -0.01940 -0.04610 526 THR C C     
6941 O  O     . THR C 5   ? 1.24270 1.22860 1.27720 0.09730  -0.02600 -0.05090 526 THR C O     
6942 C  CB    . THR C 5   ? 0.77190 0.74860 0.80210 0.09570  -0.02390 -0.03900 526 THR C CB    
6943 O  OG1   . THR C 5   ? 1.03260 1.01250 1.06600 0.09810  -0.02550 -0.04790 526 THR C OG1   
6944 C  CG2   . THR C 5   ? 0.90870 0.87930 0.93670 0.09670  -0.03160 -0.03660 526 THR C CG2   
6945 N  N     . LEU C 6   ? 1.12790 1.12210 1.16300 0.09320  -0.01320 -0.04730 527 LEU C N     
6946 C  CA    . LEU C 6   ? 0.89470 0.89410 0.93230 0.09410  -0.01380 -0.05390 527 LEU C CA    
6947 C  C     . LEU C 6   ? 0.72910 0.73540 0.77030 0.09480  -0.00930 -0.06120 527 LEU C C     
6948 O  O     . LEU C 6   ? 0.86980 0.87950 0.91340 0.09660  -0.01170 -0.06860 527 LEU C O     
6949 C  CB    . LEU C 6   ? 1.03570 1.03700 1.07200 0.09170  -0.01090 -0.04940 527 LEU C CB    
6950 C  CG    . LEU C 6   ? 1.17810 1.17360 1.21150 0.09150  -0.01630 -0.04410 527 LEU C CG    
6951 C  CD1   . LEU C 6   ? 1.18380 1.17920 1.21480 0.08840  -0.01160 -0.03600 527 LEU C CD1   
6952 C  CD2   . LEU C 6   ? 0.92200 0.91850 0.95670 0.09340  -0.02200 -0.04980 527 LEU C CD2   
6953 N  N     . LYS C 7   ? 0.47470 0.48310 0.51620 0.09340  -0.00300 -0.05930 528 LYS C N     
6954 C  CA    . LYS C 7   ? 0.45700 0.47250 0.50180 0.09350  0.00240  -0.06530 528 LYS C CA    
6955 C  C     . LYS C 7   ? 0.46890 0.48580 0.51650 0.09660  -0.00180 -0.07450 528 LYS C C     
6956 O  O     . LYS C 7   ? 0.44750 0.46090 0.49500 0.09810  -0.00460 -0.07560 528 LYS C O     
6957 C  CB    . LYS C 7   ? 0.43170 0.44800 0.47600 0.09170  0.00910  -0.06140 528 LYS C CB    
6958 C  CG    . LYS C 7   ? 0.40670 0.42400 0.44910 0.08830  0.01520  -0.05370 528 LYS C CG    
6959 C  CD    . LYS C 7   ? 0.38950 0.40910 0.43230 0.08670  0.02240  -0.05160 528 LYS C CD    
6960 C  CE    . LYS C 7   ? 0.38400 0.40240 0.42400 0.08350  0.02740  -0.04250 528 LYS C CE    
6961 N  NZ    . LYS C 7   ? 0.38050 0.40070 0.42080 0.08200  0.03410  -0.04010 528 LYS C NZ    
6962 N  N     . GLY C 8   ? 0.80610 0.82810 0.85620 0.09760  -0.00210 -0.08120 529 GLY C N     
6963 C  CA    . GLY C 8   ? 0.82230 0.84650 0.87540 0.10050  -0.00560 -0.09030 529 GLY C CA    
6964 C  C     . GLY C 8   ? 0.89530 0.92400 0.95050 0.10140  -0.00700 -0.09640 529 GLY C C     
6965 O  O     . GLY C 8   ? 0.89310 0.92200 0.94710 0.10010  -0.00710 -0.09330 529 GLY C O     
6966 N  N     . GLY C 9   ? 0.71890 0.75120 0.77720 0.10360  -0.00820 -0.10500 530 GLY C N     
6967 C  CA    . GLY C 9   ? 0.78450 0.82120 0.84510 0.10480  -0.01000 -0.11180 530 GLY C CA    
6968 C  C     . GLY C 9   ? 0.94510 0.97740 1.00510 0.10710  -0.01880 -0.11390 530 GLY C C     
6969 O  O     . GLY C 9   ? 0.86750 0.89510 0.92700 0.10890  -0.02380 -0.11480 530 GLY C O     
6970 N  N     . ALA C 10  ? 1.08420 1.11800 1.14420 0.10700  -0.02060 -0.11490 531 ALA C N     
6971 C  CA    . ALA C 10  ? 1.17400 1.20360 1.23310 0.10870  -0.02860 -0.11590 531 ALA C CA    
6972 C  C     . ALA C 10  ? 1.04810 1.06980 1.10360 0.10820  -0.03230 -0.10810 531 ALA C C     
6973 O  O     . ALA C 10  ? 0.99980 1.01780 1.05360 0.10860  -0.03750 -0.10610 531 ALA C O     
6974 C  CB    . ALA C 10  ? 1.08610 1.11610 1.14770 0.11200  -0.03380 -0.12460 531 ALA C CB    
6975 N  N     . THR D 5   ? 1.32940 1.30930 1.33950 -0.03520 -0.01670 0.00710  526 THR D N     
6976 C  CA    . THR D 5   ? 1.35140 1.33040 1.35940 -0.03600 -0.01640 0.00930  526 THR D CA    
6977 C  C     . THR D 5   ? 1.29850 1.27650 1.30620 -0.03630 -0.01680 0.00920  526 THR D C     
6978 O  O     . THR D 5   ? 1.23540 1.21240 1.24090 -0.03650 -0.01690 0.01040  526 THR D O     
6979 C  CB    . THR D 5   ? 1.31430 1.29280 1.31930 -0.03550 -0.01680 0.01050  526 THR D CB    
6980 O  OG1   . THR D 5   ? 1.26120 1.23920 1.26480 -0.03400 -0.01800 0.00960  526 THR D OG1   
6981 C  CG2   . THR D 5   ? 1.33040 1.30990 1.33550 -0.03540 -0.01640 0.01080  526 THR D CG2   
6982 N  N     . LEU D 6   ? 0.89760 0.87580 0.90770 -0.03640 -0.01660 0.00780  527 LEU D N     
6983 C  CA    . LEU D 6   ? 0.83360 0.81110 0.84390 -0.03670 -0.01700 0.00750  527 LEU D CA    
6984 C  C     . LEU D 6   ? 0.75050 0.72740 0.75990 -0.03790 -0.01610 0.00930  527 LEU D C     
6985 O  O     . LEU D 6   ? 0.87970 0.85700 0.88930 -0.03850 -0.01510 0.01010  527 LEU D O     
6986 C  CB    . LEU D 6   ? 0.80080 0.77890 0.81420 -0.03670 -0.01670 0.00530  527 LEU D CB    
6987 C  CG    . LEU D 6   ? 0.66950 0.64910 0.68460 -0.03550 -0.01760 0.00280  527 LEU D CG    
6988 C  CD1   . LEU D 6   ? 0.74090 0.72140 0.75770 -0.03570 -0.01660 0.00200  527 LEU D CD1   
6989 C  CD2   . LEU D 6   ? 0.54410 0.52440 0.56180 -0.03540 -0.01790 0.00030  527 LEU D CD2   
6990 N  N     . LYS D 7   ? 0.67760 0.65350 0.68580 -0.03820 -0.01650 0.00960  528 LYS D N     
6991 C  CA    . LYS D 7   ? 0.72290 0.69870 0.73030 -0.03930 -0.01590 0.01090  528 LYS D CA    
6992 C  C     . LYS D 7   ? 0.80890 0.78540 0.81800 -0.04000 -0.01500 0.01090  528 LYS D C     
6993 O  O     . LYS D 7   ? 0.66040 0.63650 0.67100 -0.04010 -0.01490 0.01000  528 LYS D O     
6994 C  CB    . LYS D 7   ? 0.63680 0.61110 0.64290 -0.03950 -0.01630 0.01100  528 LYS D CB    
6995 C  CG    . LYS D 7   ? 0.55410 0.52680 0.55770 -0.03840 -0.01680 0.01130  528 LYS D CG    
6996 C  CD    . LYS D 7   ? 0.50270 0.47340 0.50490 -0.03840 -0.01690 0.01130  528 LYS D CD    
6997 C  CE    . LYS D 7   ? 0.58560 0.55400 0.58470 -0.03670 -0.01720 0.01160  528 LYS D CE    
6998 N  NZ    . LYS D 7   ? 0.49610 0.46230 0.49380 -0.03640 -0.01720 0.01160  528 LYS D NZ    
6999 N  N     . GLY D 8   ? 1.21740 1.19500 1.22600 -0.04030 -0.01420 0.01190  529 GLY D N     
7000 C  CA    . GLY D 8   ? 1.11570 1.09380 1.12510 -0.04040 -0.01320 0.01220  529 GLY D CA    
7001 C  C     . GLY D 8   ? 1.08110 1.06050 1.08960 -0.04090 -0.01300 0.01300  529 GLY D C     
7002 O  O     . GLY D 8   ? 1.22930 1.20870 1.23830 -0.04120 -0.01280 0.01280  529 GLY D O     
7003 N  N     . ARG E 1   ? 0.67350 0.69570 0.68290 -0.01830 -0.00240 0.00730  522 ARG E N     
7004 C  CA    . ARG E 1   ? 0.90750 0.93180 0.91620 -0.01610 -0.00220 0.00750  522 ARG E CA    
7005 C  C     . ARG E 1   ? 0.88820 0.91100 0.89760 -0.01470 -0.00070 0.00740  522 ARG E C     
7006 O  O     . ARG E 1   ? 0.79360 0.81260 0.80330 -0.01370 0.00100  0.00790  522 ARG E O     
7007 C  CB    . ARG E 1   ? 0.78630 0.81000 0.79340 -0.01410 -0.00210 0.00870  522 ARG E CB    
7008 C  CG    . ARG E 1   ? 0.76530 0.79190 0.77130 -0.01140 -0.00220 0.00870  522 ARG E CG    
7009 C  CD    . ARG E 1   ? 0.92380 0.95580 0.93020 -0.01250 -0.00380 0.00730  522 ARG E CD    
7010 N  NE    . ARG E 1   ? 1.07390 1.10940 1.07950 -0.00980 -0.00410 0.00680  522 ARG E NE    
7011 C  CZ    . ARG E 1   ? 1.08720 1.12430 1.09330 -0.00870 -0.00380 0.00610  522 ARG E CZ    
7012 N  NH1   . ARG E 1   ? 0.91180 0.94720 0.91910 -0.01030 -0.00310 0.00590  522 ARG E NH1   
7013 N  NH2   . ARG E 1   ? 1.01600 1.05680 1.02130 -0.00590 -0.00420 0.00550  522 ARG E NH2   
7014 N  N     . MET E 2   ? 0.73870 0.76450 0.74850 -0.01460 -0.00110 0.00650  523 MET E N     
7015 C  CA    . MET E 2   ? 0.71650 0.74110 0.72690 -0.01310 0.00040  0.00620  523 MET E CA    
7016 C  C     . MET E 2   ? 0.78090 0.80460 0.78960 -0.00960 0.00140  0.00740  523 MET E C     
7017 O  O     . MET E 2   ? 0.69980 0.72530 0.70690 -0.00820 0.00050  0.00790  523 MET E O     
7018 C  CB    . MET E 2   ? 0.59010 0.61830 0.60140 -0.01410 -0.00040 0.00490  523 MET E CB    
7019 C  CG    . MET E 2   ? 0.64580 0.67850 0.65630 -0.01310 -0.00150 0.00460  523 MET E CG    
7020 S  SD    . MET E 2   ? 0.54520 0.58180 0.55680 -0.01460 -0.00220 0.00280  523 MET E SD    
7021 C  CE    . MET E 2   ? 0.46940 0.50610 0.48120 -0.01820 -0.00310 0.00230  523 MET E CE    
7022 N  N     . LYS E 3   ? 0.79760 0.81830 0.80660 -0.00800 0.00350  0.00770  524 LYS E N     
7023 C  CA    . LYS E 3   ? 0.87950 0.89790 0.88620 -0.00420 0.00500  0.00900  524 LYS E CA    
7024 C  C     . LYS E 3   ? 0.84770 0.86960 0.85360 -0.00190 0.00460  0.00860  524 LYS E C     
7025 O  O     . LYS E 3   ? 0.84010 0.85970 0.84550 0.00030  0.00650  0.00900  524 LYS E O     
7026 C  CB    . LYS E 3   ? 0.94020 0.95250 0.94720 -0.00360 0.00810  0.00960  524 LYS E CB    
7027 C  CG    . LYS E 3   ? 0.92620 0.93520 0.93410 -0.00550 0.00880  0.00980  524 LYS E CG    
7028 C  CD    . LYS E 3   ? 0.89870 0.90670 0.90390 -0.00360 0.00860  0.01150  524 LYS E CD    
7029 C  CE    . LYS E 3   ? 1.01890 1.02280 1.02130 0.00050  0.01120  0.01310  524 LYS E CE    
7030 N  NZ    . LYS E 3   ? 0.92980 0.92740 0.93320 0.00020  0.01480  0.01310  524 LYS E NZ    
7031 N  N     . LEU E 4   ? 0.83630 0.86370 0.84230 -0.00260 0.00220  0.00760  525 LEU E N     
7032 C  CA    . LEU E 4   ? 0.83710 0.86890 0.84290 -0.00080 0.00150  0.00670  525 LEU E CA    
7033 C  C     . LEU E 4   ? 0.91000 0.94510 0.91360 0.00240  0.00040  0.00680  525 LEU E C     
7034 O  O     . LEU E 4   ? 0.98920 1.02700 0.99280 0.00130  -0.00110 0.00640  525 LEU E O     
7035 C  CB    . LEU E 4   ? 0.79620 0.83230 0.80430 -0.00410 0.00000  0.00480  525 LEU E CB    
7036 C  CG    . LEU E 4   ? 0.75930 0.80040 0.76780 -0.00310 -0.00080 0.00330  525 LEU E CG    
7037 C  CD1   . LEU E 4   ? 0.73540 0.77470 0.74290 0.00050  0.00070  0.00400  525 LEU E CD1   
7038 C  CD2   . LEU E 4   ? 0.58540 0.62840 0.59600 -0.00670 -0.00150 0.00180  525 LEU E CD2   
7039 N  N     . ARG F 1   ? 0.77410 0.66580 0.76990 0.00370  0.05790  0.04210  522 ARG F N     
7040 C  CA    . ARG F 1   ? 0.89020 0.77840 0.88340 0.00420  0.05860  0.04120  522 ARG F CA    
7041 C  C     . ARG F 1   ? 0.95570 0.84440 0.94660 0.00520  0.05800  0.04050  522 ARG F C     
7042 O  O     . ARG F 1   ? 0.82240 0.71190 0.81380 0.00570  0.05800  0.04090  522 ARG F O     
7043 C  CB    . ARG F 1   ? 0.90740 0.79310 0.90150 0.00420  0.05990  0.04150  522 ARG F CB    
7044 C  CG    . ARG F 1   ? 0.96100 0.84280 0.95270 0.00460  0.06080  0.04070  522 ARG F CG    
7045 C  CD    . ARG F 1   ? 1.16310 1.04300 1.15450 0.00400  0.06110  0.04040  522 ARG F CD    
7046 N  NE    . ARG F 1   ? 1.21900 1.09540 1.20770 0.00440  0.06180  0.03950  522 ARG F NE    
7047 C  CZ    . ARG F 1   ? 1.23350 1.10940 1.21950 0.00500  0.06120  0.03860  522 ARG F CZ    
7048 N  NH1   . ARG F 1   ? 1.06030 0.93890 1.04570 0.00530  0.06000  0.03840  522 ARG F NH1   
7049 N  NH2   . ARG F 1   ? 0.98300 0.85560 0.96680 0.00530  0.06190  0.03780  522 ARG F NH2   
7050 N  N     . MET F 2   ? 0.94970 0.83780 0.93820 0.00550  0.05740  0.03970  523 MET F N     
7051 C  CA    . MET F 2   ? 0.85690 0.74500 0.84290 0.00650  0.05690  0.03900  523 MET F CA    
7052 C  C     . MET F 2   ? 0.77630 0.66140 0.76100 0.00710  0.05790  0.03860  523 MET F C     
7053 O  O     . MET F 2   ? 0.82070 0.70290 0.80530 0.00680  0.05890  0.03850  523 MET F O     
7054 C  CB    . MET F 2   ? 0.84080 0.72870 0.82450 0.00660  0.05620  0.03810  523 MET F CB    
7055 C  CG    . MET F 2   ? 0.89160 0.77590 0.87370 0.00650  0.05700  0.03750  523 MET F CG    
7056 S  SD    . MET F 2   ? 0.87530 0.75950 0.85490 0.00650  0.05610  0.03650  523 MET F SD    
7057 C  CE    . MET F 2   ? 0.77880 0.66620 0.76110 0.00550  0.05540  0.03730  523 MET F CE    
7058 N  N     . LYS F 3   ? 0.95750 0.84300 0.94090 0.00790  0.05760  0.03830  524 LYS F N     
7059 C  CA    . LYS F 3   ? 0.99450 0.87730 0.97660 0.00860  0.05850  0.03790  524 LYS F CA    
7060 C  C     . LYS F 3   ? 0.97710 0.85740 0.95590 0.00910  0.05850  0.03680  524 LYS F C     
7061 O  O     . LYS F 3   ? 1.01680 0.89700 0.99370 0.01000  0.05820  0.03630  524 LYS F O     
7062 C  CB    . LYS F 3   ? 0.97590 0.86030 0.95840 0.00920  0.05830  0.03820  524 LYS F CB    
7063 C  CG    . LYS F 3   ? 1.01780 0.90400 1.00350 0.00870  0.05850  0.03930  524 LYS F CG    
7064 C  CD    . LYS F 3   ? 1.10040 0.98630 1.08610 0.00940  0.05900  0.03940  524 LYS F CD    
7065 C  CE    . LYS F 3   ? 1.08420 0.97240 1.07300 0.00900  0.05900  0.04050  524 LYS F CE    
7066 N  NZ    . LYS F 3   ? 1.10000 0.99200 1.08960 0.00910  0.05780  0.04080  524 LYS F NZ    
7067 N  N     . LEU F 4   ? 0.79860 0.67710 0.77680 0.00870  0.05880  0.03640  525 LEU F N     
7068 C  CA    . LEU F 4   ? 0.89940 0.77530 0.87460 0.00910  0.05900  0.03540  525 LEU F CA    
7069 C  C     . LEU F 4   ? 1.06400 0.93620 1.03890 0.00900  0.06030  0.03530  525 LEU F C     
7070 O  O     . LEU F 4   ? 1.58900 1.46040 1.56560 0.00830  0.06100  0.03570  525 LEU F O     
7071 C  CB    . LEU F 4   ? 0.84560 0.72220 0.82020 0.00870  0.05830  0.03510  525 LEU F CB    
7072 C  CG    . LEU F 4   ? 0.88440 0.75920 0.85580 0.00910  0.05800  0.03400  525 LEU F CG    
7073 C  CD1   . LEU F 4   ? 0.88220 0.75650 0.85130 0.01020  0.05780  0.03340  525 LEU F CD1   
7074 C  CD2   . LEU F 4   ? 0.78550 0.66250 0.75670 0.00880  0.05690  0.03380  525 LEU F CD2   
7075 N  N     . THR F 5   ? 1.39450 1.26430 1.36700 0.00980  0.06070  0.03460  526 THR F N     
7076 C  CA    . THR F 5   ? 1.51690 1.38350 1.48920 0.00990  0.06200  0.03450  526 THR F CA    
7077 C  C     . THR F 5   ? 1.59980 1.46380 1.57230 0.00920  0.06290  0.03440  526 THR F C     
7078 O  O     . THR F 5   ? 1.80880 1.67100 1.78240 0.00900  0.06400  0.03480  526 THR F O     
7079 C  CB    . THR F 5   ? 1.38930 1.25380 1.35860 0.01090  0.06220  0.03360  526 THR F CB    
7080 O  OG1   . THR F 5   ? 1.41510 1.28200 1.38380 0.01150  0.06130  0.03350  526 THR F OG1   
7081 C  CG2   . THR F 5   ? 1.35050 1.21240 1.32000 0.01110  0.06350  0.03370  526 THR F CG2   
7082 N  N     . LEU F 6   ? 1.11850 0.98240 1.09000 0.00890  0.06240  0.03400  527 LEU F N     
7083 C  CA    . LEU F 6   ? 1.21680 1.07840 1.18840 0.00830  0.06310  0.03380  527 LEU F CA    
7084 C  C     . LEU F 6   ? 1.23380 1.09160 1.20330 0.00870  0.06410  0.03310  527 LEU F C     
7085 O  O     . LEU F 6   ? 0.94970 0.80640 0.91650 0.00930  0.06380  0.03230  527 LEU F O     
7086 C  CB    . LEU F 6   ? 1.21950 1.08170 1.19430 0.00740  0.06370  0.03480  527 LEU F CB    
7087 C  CG    . LEU F 6   ? 1.43090 1.29210 1.40650 0.00650  0.06410  0.03490  527 LEU F CG    
7088 C  CD1   . LEU F 6   ? 1.25830 1.12020 1.23710 0.00570  0.06460  0.03590  527 LEU F CD1   
7089 C  CD2   . LEU F 6   ? 1.46560 1.32290 1.43920 0.00660  0.06500  0.03420  527 LEU F CD2   
7090 N  N     . SAH G .   ? 0.28010 0.31590 0.33070 0.00450  0.02410  0.00530  501 SAH A N     
7091 C  CA    . SAH G .   ? 0.28110 0.32120 0.32660 0.00000  0.02350  0.00030  501 SAH A CA    
7092 C  CB    . SAH G .   ? 0.32480 0.36030 0.36260 -0.00530 0.02250  -0.00250 501 SAH A CB    
7093 C  CG    . SAH G .   ? 0.28530 0.32220 0.31630 -0.00720 0.01820  0.00060  501 SAH A CG    
7094 S  SD    . SAH G .   ? 0.29650 0.34150 0.32370 -0.00940 0.01610  0.00030  501 SAH A SD    
7095 C  C     . SAH G .   ? 0.36370 0.40540 0.41510 0.00060  0.02760  -0.00450 501 SAH A C     
7096 O  O     . SAH G .   ? 0.33610 0.37590 0.39630 0.00500  0.03050  -0.00390 501 SAH A O     
7097 O  OXT   . SAH G .   ? 0.35340 0.39830 0.40110 -0.00310 0.02860  -0.00880 501 SAH A OXT   
7098 C  "C5'" . SAH G .   ? 0.25370 0.30310 0.28200 -0.00600 0.01260  0.00550  501 SAH A "C5'" 
7099 C  "C4'" . SAH G .   ? 0.26920 0.32290 0.30440 -0.00060 0.01320  0.00810  501 SAH A "C4'" 
7100 O  "O4'" . SAH G .   ? 0.29580 0.34320 0.33430 0.00260  0.01520  0.01060  501 SAH A "O4'" 
7101 C  "C3'" . SAH G .   ? 0.27650 0.33680 0.31090 0.00170  0.00950  0.01150  501 SAH A "C3'" 
7102 O  "O3'" . SAH G .   ? 0.26710 0.33560 0.30280 -0.00000 0.00820  0.00890  501 SAH A "O3'" 
7103 C  "C2'" . SAH G .   ? 0.25590 0.31710 0.29600 0.00800  0.01040  0.01580  501 SAH A "C2'" 
7104 O  "O2'" . SAH G .   ? 0.32770 0.39500 0.37520 0.01080  0.01140  0.01470  501 SAH A "O2'" 
7105 C  "C1'" . SAH G .   ? 0.32900 0.37970 0.37010 0.00780  0.01390  0.01600  501 SAH A "C1'" 
7106 N  N9    . SAH G .   ? 0.27490 0.32060 0.31210 0.00810  0.01340  0.01970  501 SAH A N9    
7107 C  C8    . SAH G .   ? 0.24830 0.28880 0.28050 0.00380  0.01310  0.01800  501 SAH A C8    
7108 N  N7    . SAH G .   ? 0.27040 0.30790 0.30110 0.00520  0.01320  0.02200  501 SAH A N7    
7109 C  C5    . SAH G .   ? 0.26850 0.30880 0.30210 0.01070  0.01360  0.02720  501 SAH A C5    
7110 C  C6    . SAH G .   ? 0.34120 0.38050 0.37390 0.01450  0.01430  0.03380  501 SAH A C6    
7111 N  N6    . SAH G .   ? 0.27450 0.30940 0.30390 0.01290  0.01530  0.03560  501 SAH A N6    
7112 N  N1    . SAH G .   ? 0.23900 0.28230 0.27440 0.02030  0.01410  0.03890  501 SAH A N1    
7113 C  C2    . SAH G .   ? 0.28670 0.33530 0.32690 0.02210  0.01320  0.03670  501 SAH A C2    
7114 N  N3    . SAH G .   ? 0.28990 0.34010 0.33210 0.01850  0.01300  0.03020  501 SAH A N3    
7115 C  C4    . SAH G .   ? 0.31830 0.36390 0.35630 0.01280  0.01330  0.02590  501 SAH A C4    
7116 ZN ZN    . ZN  H .   ? 0.51350 0.45000 0.50280 -0.00570 0.03520  0.02680  502 ZN  A ZN    
7117 ZN ZN    . ZN  I .   ? 0.36550 0.33990 0.28930 -0.00630 -0.00010 0.02080  503 ZN  A ZN    
7118 ZN ZN    . ZN  J .   ? 0.57430 0.58280 0.56160 -0.00040 -0.00430 0.02190  504 ZN  A ZN    
7119 N  N     . SAH K .   ? 0.70760 0.36600 0.33390 -0.14720 -0.15070 0.07140  501 SAH B N     
7120 C  CA    . SAH K .   ? 0.72850 0.38180 0.36590 -0.14350 -0.17010 0.07180  501 SAH B CA    
7121 C  CB    . SAH K .   ? 0.70080 0.38990 0.39360 -0.13920 -0.17160 0.07070  501 SAH B CB    
7122 C  CG    . SAH K .   ? 0.66810 0.38310 0.37390 -0.13950 -0.15060 0.06430  501 SAH B CG    
7123 S  SD    . SAH K .   ? 0.66940 0.36960 0.35580 -0.13740 -0.15620 0.06230  501 SAH B SD    
7124 C  C     . SAH K .   ? 0.87770 0.49790 0.49820 -0.14130 -0.19850 0.07850  501 SAH B C     
7125 O  O     . SAH K .   ? 0.87010 0.46930 0.46580 -0.14290 -0.20210 0.08330  501 SAH B O     
7126 O  OXT   . SAH K .   ? 0.82480 0.43880 0.45760 -0.13730 -0.21870 0.07950  501 SAH B OXT   
7127 C  "C5'" . SAH K .   ? 0.70950 0.41060 0.36500 -0.14230 -0.12730 0.05440  501 SAH B "C5'" 
7128 C  "C4'" . SAH K .   ? 0.70940 0.37930 0.31730 -0.14690 -0.12270 0.05520  501 SAH B "C4'" 
7129 O  "O4'" . SAH K .   ? 0.70470 0.38220 0.32020 -0.14900 -0.11640 0.05730  501 SAH B "O4'" 
7130 C  "C3'" . SAH K .   ? 0.75040 0.41660 0.33200 -0.14950 -0.09940 0.04900  501 SAH B "C3'" 
7131 O  "O3'" . SAH K .   ? 0.77970 0.42120 0.33060 -0.14860 -0.10690 0.04800  501 SAH B "O3'" 
7132 C  "C2'" . SAH K .   ? 0.80970 0.45750 0.36180 -0.15350 -0.08940 0.05180  501 SAH B "C2'" 
7133 O  "O2'" . SAH K .   ? 0.85340 0.45810 0.35830 -0.15470 -0.10320 0.05730  501 SAH B "O2'" 
7134 C  "C1'" . SAH K .   ? 0.73420 0.40250 0.32050 -0.15280 -0.09540 0.05520  501 SAH B "C1'" 
7135 N  N9    . SAH K .   ? 0.70300 0.40680 0.32160 -0.15280 -0.07550 0.05000  501 SAH B N9    
7136 C  C8    . SAH K .   ? 0.60880 0.34760 0.27140 -0.14970 -0.07500 0.04600  501 SAH B C8    
7137 N  N7    . SAH K .   ? 0.59720 0.36120 0.27920 -0.14950 -0.05760 0.04130  501 SAH B N7    
7138 C  C5    . SAH K .   ? 0.62060 0.36650 0.27350 -0.15280 -0.04450 0.04300  501 SAH B C5    
7139 C  C6    . SAH K .   ? 0.61130 0.36930 0.27040 -0.15380 -0.02360 0.04080  501 SAH B C6    
7140 N  N6    . SAH K .   ? 0.55700 0.34860 0.25250 -0.15060 -0.01470 0.03530  501 SAH B N6    
7141 N  N1    . SAH K .   ? 0.65140 0.38360 0.27760 -0.15790 -0.01240 0.04530  501 SAH B N1    
7142 C  C2    . SAH K .   ? 0.68330 0.37870 0.26830 -0.16010 -0.02270 0.05080  501 SAH B C2    
7143 N  N3    . SAH K .   ? 0.69270 0.37280 0.26640 -0.15870 -0.04460 0.05250  501 SAH B N3    
7144 C  C4    . SAH K .   ? 0.67250 0.38050 0.28440 -0.15510 -0.05450 0.04860  501 SAH B C4    
7145 ZN ZN    . ZN  L .   ? 0.77120 0.77640 0.88990 -0.06710 0.03030  -0.08230 502 ZN  B ZN    
7146 ZN ZN    . ZN  M .   ? 0.39110 0.37530 0.39980 -0.05490 -0.00440 0.00910  503 ZN  B ZN    
7147 ZN ZN    . ZN  N .   ? 0.75770 0.72850 0.82440 -0.06120 0.02210  -0.03350 504 ZN  B ZN    
# 
