data_9CKG
# 
_entry.id   9CKG 
# 
_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   9CKG         pdb_00009ckg 10.2210/pdb9ckg/pdb 
WWPDB D_1000285731 ?            ?                   
# 
_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                        9CKG 
_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 
'Sobota, J.'    1 0000-0002-9198-5495 
'Zhang, Y.'     2 0000-0001-8099-4225 
'Spellmon, N.'  3 ?                   
'Perry, E.'     4 ?                   
'Brunzelle, J.' 5 ?                   
'Yang, Z.'      6 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' 49684.008 1 2.1.1.-,2.1.1.354 F184A ? ? 
2 non-polymer syn S-ADENOSYL-L-HOMOCYSTEINE          384.411   1 ?                 ?     ? ? 
3 non-polymer syn 'ZINC ION'                         65.409    3 ?                 ?     ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'            106.120   2 ?                 ?     ? ? 
5 non-polymer syn 'TETRAETHYLENE GLYCOL'             194.226   1 ?                 ?     ? ? 
6 non-polymer syn ETHANOL                            46.068    1 ?                 ?     ? ? 
7 non-polymer syn GLYCEROL                           92.094    1 ?                 ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'HSKM-B,Histone methyltransferase SMYD2,Lysine N-methyltransferase 3C,SET and MYND domain-containing protein 2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQK
EDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFY
SKHLGFPDNDSLVVLFAQVNCNGATIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSY
IDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEI
CELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAA
GEKALKKAIAIMEVAHGKDHPYISEIKQEIESH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQK
EDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFY
SKHLGFPDNDSLVVLFAQVNCNGATIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSY
IDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEI
CELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAA
GEKALKKAIAIMEVAHGKDHPYISEIKQEIESH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 S-ADENOSYL-L-HOMOCYSTEINE SAH 
3 'ZINC ION'                ZN  
4 'DI(HYDROXYETHYL)ETHER'   PEG 
5 'TETRAETHYLENE GLYCOL'    PG4 
6 ETHANOL                   EOH 
7 GLYCEROL                  GOL 
# 
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 GLY 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 ALA 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 
# 
_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                   ? 
# 
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 
EOH non-polymer         . ETHANOL                   ?                               'C2 H6 O'         46.068  
GLN 'L-peptide linking' y GLUTAMINE                 ?                               'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'           ?                               'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                   ?                               'C2 H5 N O2'      75.067  
GOL non-polymer         . GLYCEROL                  'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'        92.094  
HIS 'L-peptide linking' y HISTIDINE                 ?                               'C6 H10 N3 O2 1'  156.162 
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'   ?                               'C4 H10 O3'       106.120 
PG4 non-polymer         . 'TETRAETHYLENE GLYCOL'    ?                               'C8 H18 O5'       194.226 
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 GLY 165 165 165 GLY GLY 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 ALA 184 184 184 ALA ALA 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 ?   ?   ?   A . 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 
B 2 SAH 1 501 509 SAH SAH A . 
C 3 ZN  1 502 506 ZN  ZN  A . 
D 3 ZN  1 503 507 ZN  ZN  A . 
E 3 ZN  1 504 508 ZN  ZN  A . 
F 4 PEG 1 505 511 PEG PEG A . 
G 4 PEG 1 506 512 PEG PEG A . 
H 5 PG4 1 507 513 PG4 PG4 A . 
I 6 EOH 1 508 510 EOH EOH A . 
J 7 GOL 1 509 514 GOL GOL A . 
# 
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  ? ? ? 1.19.2_4158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CKG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     151.822 
_cell.length_a_esd                 ? 
_cell.length_b                     151.822 
_cell.length_b_esd                 ? 
_cell.length_c                     53.377 
_cell.length_c_esd                 ? 
_cell.volume                       1230335.563 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CKG 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                79 
_symmetry.space_group_name_Hall            'I 4' 
_symmetry.space_group_name_H-M             'I 4' 
_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                   9CKG 
_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             3.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          60.26 
_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, and 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         2018-08-28 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97856 
_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                          87.84 
_reflns.entry_id                                       9CKG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.75 
_reflns.d_resolution_low                               107.35 
_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                                     8636 
_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                           89.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.3 
_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                                0.132 
_reflns.pdbx_Rpim_I_all                                0.053 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.121 
_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                                    2.75 
_reflns_shell.d_res_low                                     3.162 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8635 
_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                               0.455 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.997 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.013 
_reflns_shell.pdbx_Rsym_value                               1.113 
_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                               83.61 
_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                                 9CKG 
_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                            2.75 
_refine.ls_d_res_low                             48.01 
_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                     8626 
_refine.ls_number_reflns_R_free                  870 
_refine.ls_number_reflns_R_work                  7756 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    53.64 
_refine.ls_percent_reflns_R_free                 10.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1965 
_refine.ls_R_factor_R_free                       0.2229 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1935 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.37 
_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                 27.3761 
_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                            0.3375 
_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                       2.75 
_refine_hist.d_res_low                        48.01 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               3497 
_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        3432 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         65 
_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' ? 0.0062  ? 3568 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0751  ? 4797 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0691  ? 509  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0060  ? 614  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.9192 ? 1363 ? 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' 2.75 2.92  . . 5   61   2.51  . . . . 0.3978 . . . . . . . . . . . 0.5213 
'X-RAY DIFFRACTION' 2.92 3.15  . . 30  314  13.08 . . . . 0.3316 . . . . . . . . . . . 0.2494 
'X-RAY DIFFRACTION' 3.15 3.47  . . 79  754  31.42 . . . . 0.3026 . . . . . . . . . . . 0.3559 
'X-RAY DIFFRACTION' 3.47 3.97  . . 207 1758 74.23 . . . . 0.2492 . . . . . . . . . . . 0.2733 
'X-RAY DIFFRACTION' 3.97 5.00  . . 300 2388 99.56 . . . . 0.1839 . . . . . . . . . . . 0.2058 
'X-RAY DIFFRACTION' 5.00 48.01 . . 249 2481 98.84 . . . . 0.1674 . . . . . . . . . . . 0.2045 
# 
_struct.entry_id                     9CKG 
_struct.title                        'Crystal structure of SMYD2 active site mutant' 
_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        9CKG 
_struct_keywords.text            'SMYD2, PARP1, protein lysine-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 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
I N N 6 ? 
J N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SMYD2_HUMAN 
_struct_ref.pdbx_db_accession          Q9NRG4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQK
EDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFY
SKHLGFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSY
IDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEI
CELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAA
GEKALKKAIAIMEVAHGKDHPYISEIKQEIESH
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9CKG 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 433 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9NRG4 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  433 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       433 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9CKG 
_struct_ref_seq_dif.mon_id                       ALA 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      184 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   Q9NRG4 
_struct_ref_seq_dif.db_mon_id                    PHE 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          184 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            184 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_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 THR A 123 ? LYS A 127 ? THR A 123 LYS A 127 5 ? 5  
HELX_P HELX_P7  AA7 ALA A 130 ? PHE A 134 ? ALA A 130 PHE A 134 5 ? 5  
HELX_P HELX_P8  AA8 HIS A 137 ? LEU A 141 ? HIS A 137 LEU A 141 5 ? 5  
HELX_P HELX_P9  AA9 ASP A 142 ? SER A 161 ? ASP A 142 SER A 161 1 ? 20 
HELX_P HELX_P10 AB1 ASP A 168 ? GLY A 183 ? ASP A 168 GLY A 183 1 ? 16 
HELX_P HELX_P11 AB2 PHE A 199 ? LEU A 204 ? PHE A 199 LEU A 204 1 ? 6  
HELX_P HELX_P12 AB3 PRO A 246 ? PHE A 259 ? PRO A 246 PHE A 259 1 ? 14 
HELX_P HELX_P13 AB4 CYS A 264 ? LYS A 270 ? CYS A 264 LYS A 270 1 ? 7  
HELX_P HELX_P14 AB5 LYS A 272 ? VAL A 277 ? LYS A 272 VAL A 277 1 ? 6  
HELX_P HELX_P15 AB6 LYS A 287 ? LYS A 309 ? LYS A 287 LYS A 309 1 ? 23 
HELX_P HELX_P16 AB7 SER A 313 ? SER A 330 ? SER A 313 SER A 330 1 ? 18 
HELX_P HELX_P17 AB8 ASN A 336 ? MET A 353 ? ASN A 336 MET A 353 1 ? 18 
HELX_P HELX_P18 AB9 ASP A 355 ? TYR A 374 ? ASP A 355 TYR A 374 1 ? 20 
HELX_P HELX_P19 AC1 SER A 378 ? LEU A 395 ? SER A 378 LEU A 395 1 ? 18 
HELX_P HELX_P20 AC2 HIS A 397 ? GLY A 417 ? HIS A 397 GLY A 417 1 ? 21 
HELX_P HELX_P21 AC3 HIS A 420 ? SER A 432 ? HIS A 420 SER A 432 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A CYS 52  SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 52  A ZN 504 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc2  metalc ? ? A CYS 55  SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 55  A ZN 504 1_555 ? ? ? ? ? ? ? 2.339 ? ? 
metalc3  metalc ? ? A CYS 65  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 65  A ZN 502 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc4  metalc ? ? A CYS 68  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 68  A ZN 502 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
metalc5  metalc ? ? A CYS 74  SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 74  A ZN 504 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc6  metalc ? ? A CYS 78  SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 78  A ZN 504 1_555 ? ? ? ? ? ? ? 2.354 ? ? 
metalc7  metalc ? ? A HIS 86  NE2 ? ? ? 1_555 C ZN . ZN ? ? A HIS 86  A ZN 502 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc8  metalc ? ? A CYS 90  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 90  A ZN 502 1_555 ? ? ? ? ? ? ? 2.321 ? ? 
metalc9  metalc ? ? A CYS 209 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 209 A ZN 503 1_555 ? ? ? ? ? ? ? 2.313 ? ? 
metalc10 metalc ? ? A CYS 262 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 262 A ZN 503 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc11 metalc ? ? A CYS 264 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 264 A ZN 503 1_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc12 metalc ? ? A CYS 267 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 267 A ZN 503 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
# 
_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 ? E ZN . ? A ZN 504 ? 1_555 SG  ? A CYS 55  ? A CYS 55  ? 1_555 109.2 ? 
2  SG  ? A CYS 52  ? A CYS 52  ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 SG  ? A CYS 74  ? A CYS 74  ? 1_555 99.6  ? 
3  SG  ? A CYS 55  ? A CYS 55  ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 SG  ? A CYS 74  ? A CYS 74  ? 1_555 102.5 ? 
4  SG  ? A CYS 52  ? A CYS 52  ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 SG  ? A CYS 78  ? A CYS 78  ? 1_555 109.0 ? 
5  SG  ? A CYS 55  ? A CYS 55  ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 SG  ? A CYS 78  ? A CYS 78  ? 1_555 117.7 ? 
6  SG  ? A CYS 74  ? A CYS 74  ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 SG  ? A CYS 78  ? A CYS 78  ? 1_555 117.2 ? 
7  SG  ? A CYS 65  ? A CYS 65  ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 SG  ? A CYS 68  ? A CYS 68  ? 1_555 113.5 ? 
8  SG  ? A CYS 65  ? A CYS 65  ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 NE2 ? A HIS 86  ? A HIS 86  ? 1_555 104.3 ? 
9  SG  ? A CYS 68  ? A CYS 68  ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 NE2 ? A HIS 86  ? A HIS 86  ? 1_555 102.2 ? 
10 SG  ? A CYS 65  ? A CYS 65  ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 SG  ? A CYS 90  ? A CYS 90  ? 1_555 115.0 ? 
11 SG  ? A CYS 68  ? A CYS 68  ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 SG  ? A CYS 90  ? A CYS 90  ? 1_555 111.9 ? 
12 NE2 ? A HIS 86  ? A HIS 86  ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 SG  ? A CYS 90  ? A CYS 90  ? 1_555 108.8 ? 
13 SG  ? A CYS 209 ? A CYS 209 ? 1_555 ZN ? D ZN . ? A ZN 503 ? 1_555 SG  ? A CYS 262 ? A CYS 262 ? 1_555 112.0 ? 
14 SG  ? A CYS 209 ? A CYS 209 ? 1_555 ZN ? D ZN . ? A ZN 503 ? 1_555 SG  ? A CYS 264 ? A CYS 264 ? 1_555 105.0 ? 
15 SG  ? A CYS 262 ? A CYS 262 ? 1_555 ZN ? D ZN . ? A ZN 503 ? 1_555 SG  ? A CYS 264 ? A CYS 264 ? 1_555 107.4 ? 
16 SG  ? A CYS 209 ? A CYS 209 ? 1_555 ZN ? D ZN . ? A ZN 503 ? 1_555 SG  ? A CYS 267 ? A CYS 267 ? 1_555 101.5 ? 
17 SG  ? A CYS 262 ? A CYS 262 ? 1_555 ZN ? D ZN . ? A ZN 503 ? 1_555 SG  ? A CYS 267 ? A CYS 267 ? 1_555 113.9 ? 
18 SG  ? A CYS 264 ? A CYS 264 ? 1_555 ZN ? D ZN . ? A ZN 503 ? 1_555 SG  ? A CYS 267 ? A CYS 267 ? 1_555 116.7 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
# 
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      
# 
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 ALA A 184 ? GLU A 187 ? ALA 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 
# 
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 PHE A 12  ? N PHE A 12  O GLY A 20  ? O GLY A 20  
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 GLY A 195 ? O GLY A 195 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 
# 
_pdbx_entry_details.entry_id                   9CKG 
_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 ? ? -149.07 50.82   
2 1 PRO A 167 ? ? -68.82  -179.33 
3 1 VAL A 277 ? ? -110.18 56.13   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y,x,z              
3 y,-x,z              
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 -y+1/2,x+1/2,z+1/2  
7 y+1/2,-x+1/2,z+1/2  
8 -x+1/2,-y+1/2,z+1/2 
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         49.406 
_pdbx_refine_tls.origin_y         -20.400 
_pdbx_refine_tls.origin_z         -24.778 
_pdbx_refine_tls.T[1][1]          0.609218065132 
_pdbx_refine_tls.T[2][2]          0.67954619884 
_pdbx_refine_tls.T[3][3]          0.638260124153 
_pdbx_refine_tls.T[1][2]          -0.0795366725266 
_pdbx_refine_tls.T[1][3]          0.00260842576003 
_pdbx_refine_tls.T[2][3]          0.048573962021 
_pdbx_refine_tls.L[1][1]          2.22098569581 
_pdbx_refine_tls.L[2][2]          2.90572704294 
_pdbx_refine_tls.L[3][3]          3.08259831761 
_pdbx_refine_tls.L[1][2]          0.832682751503 
_pdbx_refine_tls.L[1][3]          -0.13379532039 
_pdbx_refine_tls.L[2][3]          0.0294993895372 
_pdbx_refine_tls.S[1][1]          0.026772247297 
_pdbx_refine_tls.S[2][2]          -0.0738033218246 
_pdbx_refine_tls.S[3][3]          -3.31273267991e-10 
_pdbx_refine_tls.S[1][2]          0.1736254849 
_pdbx_refine_tls.S[1][3]          0.0506793495635 
_pdbx_refine_tls.S[2][3]          -0.095805337621 
_pdbx_refine_tls.S[2][1]          -0.0869957541925 
_pdbx_refine_tls.S[3][1]          0.268152294604 
_pdbx_refine_tls.S[3][2]          -0.183365900257 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     5 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     432 
_pdbx_refine_tls_group.selection_details   '( CHAIN A AND RESID 5:432 )' 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
# 
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 A HIS 433 ? A HIS 433 
# 
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  
EOH C1     C  N N 88  
EOH C2     C  N N 89  
EOH O      O  N N 90  
EOH H11    H  N N 91  
EOH H12    H  N N 92  
EOH H21    H  N N 93  
EOH H22    H  N N 94  
EOH H23    H  N N 95  
EOH HO     H  N N 96  
GLN N      N  N N 97  
GLN CA     C  N S 98  
GLN C      C  N N 99  
GLN O      O  N N 100 
GLN CB     C  N N 101 
GLN CG     C  N N 102 
GLN CD     C  N N 103 
GLN OE1    O  N N 104 
GLN NE2    N  N N 105 
GLN OXT    O  N N 106 
GLN H      H  N N 107 
GLN H2     H  N N 108 
GLN HA     H  N N 109 
GLN HB2    H  N N 110 
GLN HB3    H  N N 111 
GLN HG2    H  N N 112 
GLN HG3    H  N N 113 
GLN HE21   H  N N 114 
GLN HE22   H  N N 115 
GLN HXT    H  N N 116 
GLU N      N  N N 117 
GLU CA     C  N S 118 
GLU C      C  N N 119 
GLU O      O  N N 120 
GLU CB     C  N N 121 
GLU CG     C  N N 122 
GLU CD     C  N N 123 
GLU OE1    O  N N 124 
GLU OE2    O  N N 125 
GLU OXT    O  N N 126 
GLU H      H  N N 127 
GLU H2     H  N N 128 
GLU HA     H  N N 129 
GLU HB2    H  N N 130 
GLU HB3    H  N N 131 
GLU HG2    H  N N 132 
GLU HG3    H  N N 133 
GLU HE2    H  N N 134 
GLU HXT    H  N N 135 
GLY N      N  N N 136 
GLY CA     C  N N 137 
GLY C      C  N N 138 
GLY O      O  N N 139 
GLY OXT    O  N N 140 
GLY H      H  N N 141 
GLY H2     H  N N 142 
GLY HA2    H  N N 143 
GLY HA3    H  N N 144 
GLY HXT    H  N N 145 
GOL C1     C  N N 146 
GOL O1     O  N N 147 
GOL C2     C  N N 148 
GOL O2     O  N N 149 
GOL C3     C  N N 150 
GOL O3     O  N N 151 
GOL H11    H  N N 152 
GOL H12    H  N N 153 
GOL HO1    H  N N 154 
GOL H2     H  N N 155 
GOL HO2    H  N N 156 
GOL H31    H  N N 157 
GOL H32    H  N N 158 
GOL HO3    H  N N 159 
HIS N      N  N N 160 
HIS CA     C  N S 161 
HIS C      C  N N 162 
HIS O      O  N N 163 
HIS CB     C  N N 164 
HIS CG     C  Y N 165 
HIS ND1    N  Y N 166 
HIS CD2    C  Y N 167 
HIS CE1    C  Y N 168 
HIS NE2    N  Y N 169 
HIS OXT    O  N N 170 
HIS H      H  N N 171 
HIS H2     H  N N 172 
HIS HA     H  N N 173 
HIS HB2    H  N N 174 
HIS HB3    H  N N 175 
HIS HD1    H  N N 176 
HIS HD2    H  N N 177 
HIS HE1    H  N N 178 
HIS HE2    H  N N 179 
HIS HXT    H  N N 180 
ILE N      N  N N 181 
ILE CA     C  N S 182 
ILE C      C  N N 183 
ILE O      O  N N 184 
ILE CB     C  N S 185 
ILE CG1    C  N N 186 
ILE CG2    C  N N 187 
ILE CD1    C  N N 188 
ILE OXT    O  N N 189 
ILE H      H  N N 190 
ILE H2     H  N N 191 
ILE HA     H  N N 192 
ILE HB     H  N N 193 
ILE HG12   H  N N 194 
ILE HG13   H  N N 195 
ILE HG21   H  N N 196 
ILE HG22   H  N N 197 
ILE HG23   H  N N 198 
ILE HD11   H  N N 199 
ILE HD12   H  N N 200 
ILE HD13   H  N N 201 
ILE HXT    H  N N 202 
LEU N      N  N N 203 
LEU CA     C  N S 204 
LEU C      C  N N 205 
LEU O      O  N N 206 
LEU CB     C  N N 207 
LEU CG     C  N N 208 
LEU CD1    C  N N 209 
LEU CD2    C  N N 210 
LEU OXT    O  N N 211 
LEU H      H  N N 212 
LEU H2     H  N N 213 
LEU HA     H  N N 214 
LEU HB2    H  N N 215 
LEU HB3    H  N N 216 
LEU HG     H  N N 217 
LEU HD11   H  N N 218 
LEU HD12   H  N N 219 
LEU HD13   H  N N 220 
LEU HD21   H  N N 221 
LEU HD22   H  N N 222 
LEU HD23   H  N N 223 
LEU HXT    H  N N 224 
LYS N      N  N N 225 
LYS CA     C  N S 226 
LYS C      C  N N 227 
LYS O      O  N N 228 
LYS CB     C  N N 229 
LYS CG     C  N N 230 
LYS CD     C  N N 231 
LYS CE     C  N N 232 
LYS NZ     N  N N 233 
LYS OXT    O  N N 234 
LYS H      H  N N 235 
LYS H2     H  N N 236 
LYS HA     H  N N 237 
LYS HB2    H  N N 238 
LYS HB3    H  N N 239 
LYS HG2    H  N N 240 
LYS HG3    H  N N 241 
LYS HD2    H  N N 242 
LYS HD3    H  N N 243 
LYS HE2    H  N N 244 
LYS HE3    H  N N 245 
LYS HZ1    H  N N 246 
LYS HZ2    H  N N 247 
LYS HZ3    H  N N 248 
LYS HXT    H  N N 249 
MET N      N  N N 250 
MET CA     C  N S 251 
MET C      C  N N 252 
MET O      O  N N 253 
MET CB     C  N N 254 
MET CG     C  N N 255 
MET SD     S  N N 256 
MET CE     C  N N 257 
MET OXT    O  N N 258 
MET H      H  N N 259 
MET H2     H  N N 260 
MET HA     H  N N 261 
MET HB2    H  N N 262 
MET HB3    H  N N 263 
MET HG2    H  N N 264 
MET HG3    H  N N 265 
MET HE1    H  N N 266 
MET HE2    H  N N 267 
MET HE3    H  N N 268 
MET HXT    H  N N 269 
PEG C1     C  N N 270 
PEG O1     O  N N 271 
PEG C2     C  N N 272 
PEG O2     O  N N 273 
PEG C3     C  N N 274 
PEG C4     C  N N 275 
PEG O4     O  N N 276 
PEG H11    H  N N 277 
PEG H12    H  N N 278 
PEG HO1    H  N N 279 
PEG H21    H  N N 280 
PEG H22    H  N N 281 
PEG H31    H  N N 282 
PEG H32    H  N N 283 
PEG H41    H  N N 284 
PEG H42    H  N N 285 
PEG HO4    H  N N 286 
PG4 O1     O  N N 287 
PG4 C1     C  N N 288 
PG4 C2     C  N N 289 
PG4 O2     O  N N 290 
PG4 C3     C  N N 291 
PG4 C4     C  N N 292 
PG4 O3     O  N N 293 
PG4 C5     C  N N 294 
PG4 C6     C  N N 295 
PG4 O4     O  N N 296 
PG4 C7     C  N N 297 
PG4 C8     C  N N 298 
PG4 O5     O  N N 299 
PG4 HO1    H  N N 300 
PG4 H11    H  N N 301 
PG4 H12    H  N N 302 
PG4 H21    H  N N 303 
PG4 H22    H  N N 304 
PG4 H31    H  N N 305 
PG4 H32    H  N N 306 
PG4 H41    H  N N 307 
PG4 H42    H  N N 308 
PG4 H51    H  N N 309 
PG4 H52    H  N N 310 
PG4 H61    H  N N 311 
PG4 H62    H  N N 312 
PG4 H71    H  N N 313 
PG4 H72    H  N N 314 
PG4 H81    H  N N 315 
PG4 H82    H  N N 316 
PG4 HO5    H  N N 317 
PHE N      N  N N 318 
PHE CA     C  N S 319 
PHE C      C  N N 320 
PHE O      O  N N 321 
PHE CB     C  N N 322 
PHE CG     C  Y N 323 
PHE CD1    C  Y N 324 
PHE CD2    C  Y N 325 
PHE CE1    C  Y N 326 
PHE CE2    C  Y N 327 
PHE CZ     C  Y N 328 
PHE OXT    O  N N 329 
PHE H      H  N N 330 
PHE H2     H  N N 331 
PHE HA     H  N N 332 
PHE HB2    H  N N 333 
PHE HB3    H  N N 334 
PHE HD1    H  N N 335 
PHE HD2    H  N N 336 
PHE HE1    H  N N 337 
PHE HE2    H  N N 338 
PHE HZ     H  N N 339 
PHE HXT    H  N N 340 
PRO N      N  N N 341 
PRO CA     C  N S 342 
PRO C      C  N N 343 
PRO O      O  N N 344 
PRO CB     C  N N 345 
PRO CG     C  N N 346 
PRO CD     C  N N 347 
PRO OXT    O  N N 348 
PRO H      H  N N 349 
PRO HA     H  N N 350 
PRO HB2    H  N N 351 
PRO HB3    H  N N 352 
PRO HG2    H  N N 353 
PRO HG3    H  N N 354 
PRO HD2    H  N N 355 
PRO HD3    H  N N 356 
PRO HXT    H  N N 357 
SAH N      N  N N 358 
SAH CA     C  N S 359 
SAH CB     C  N N 360 
SAH CG     C  N N 361 
SAH SD     S  N N 362 
SAH C      C  N N 363 
SAH O      O  N N 364 
SAH OXT    O  N N 365 
SAH "C5'"  C  N N 366 
SAH "C4'"  C  N S 367 
SAH "O4'"  O  N N 368 
SAH "C3'"  C  N S 369 
SAH "O3'"  O  N N 370 
SAH "C2'"  C  N R 371 
SAH "O2'"  O  N N 372 
SAH "C1'"  C  N R 373 
SAH N9     N  Y N 374 
SAH C8     C  Y N 375 
SAH N7     N  Y N 376 
SAH C5     C  Y N 377 
SAH C6     C  Y N 378 
SAH N6     N  N N 379 
SAH N1     N  Y N 380 
SAH C2     C  Y N 381 
SAH N3     N  Y N 382 
SAH C4     C  Y N 383 
SAH HN1    H  N N 384 
SAH HN2    H  N N 385 
SAH HA     H  N N 386 
SAH HB1    H  N N 387 
SAH HB2    H  N N 388 
SAH HG1    H  N N 389 
SAH HG2    H  N N 390 
SAH HXT    H  N N 391 
SAH "H5'1" H  N N 392 
SAH "H5'2" H  N N 393 
SAH "H4'"  H  N N 394 
SAH "H3'"  H  N N 395 
SAH "HO3'" H  N N 396 
SAH "H2'"  H  N N 397 
SAH "HO2'" H  N N 398 
SAH "H1'"  H  N N 399 
SAH H8     H  N N 400 
SAH HN61   H  N N 401 
SAH HN62   H  N N 402 
SAH H2     H  N N 403 
SER N      N  N N 404 
SER CA     C  N S 405 
SER C      C  N N 406 
SER O      O  N N 407 
SER CB     C  N N 408 
SER OG     O  N N 409 
SER OXT    O  N N 410 
SER H      H  N N 411 
SER H2     H  N N 412 
SER HA     H  N N 413 
SER HB2    H  N N 414 
SER HB3    H  N N 415 
SER HG     H  N N 416 
SER HXT    H  N N 417 
THR N      N  N N 418 
THR CA     C  N S 419 
THR C      C  N N 420 
THR O      O  N N 421 
THR CB     C  N R 422 
THR OG1    O  N N 423 
THR CG2    C  N N 424 
THR OXT    O  N N 425 
THR H      H  N N 426 
THR H2     H  N N 427 
THR HA     H  N N 428 
THR HB     H  N N 429 
THR HG1    H  N N 430 
THR HG21   H  N N 431 
THR HG22   H  N N 432 
THR HG23   H  N N 433 
THR HXT    H  N N 434 
TRP N      N  N N 435 
TRP CA     C  N S 436 
TRP C      C  N N 437 
TRP O      O  N N 438 
TRP CB     C  N N 439 
TRP CG     C  Y N 440 
TRP CD1    C  Y N 441 
TRP CD2    C  Y N 442 
TRP NE1    N  Y N 443 
TRP CE2    C  Y N 444 
TRP CE3    C  Y N 445 
TRP CZ2    C  Y N 446 
TRP CZ3    C  Y N 447 
TRP CH2    C  Y N 448 
TRP OXT    O  N N 449 
TRP H      H  N N 450 
TRP H2     H  N N 451 
TRP HA     H  N N 452 
TRP HB2    H  N N 453 
TRP HB3    H  N N 454 
TRP HD1    H  N N 455 
TRP HE1    H  N N 456 
TRP HE3    H  N N 457 
TRP HZ2    H  N N 458 
TRP HZ3    H  N N 459 
TRP HH2    H  N N 460 
TRP HXT    H  N N 461 
TYR N      N  N N 462 
TYR CA     C  N S 463 
TYR C      C  N N 464 
TYR O      O  N N 465 
TYR CB     C  N N 466 
TYR CG     C  Y N 467 
TYR CD1    C  Y N 468 
TYR CD2    C  Y N 469 
TYR CE1    C  Y N 470 
TYR CE2    C  Y N 471 
TYR CZ     C  Y N 472 
TYR OH     O  N N 473 
TYR OXT    O  N N 474 
TYR H      H  N N 475 
TYR H2     H  N N 476 
TYR HA     H  N N 477 
TYR HB2    H  N N 478 
TYR HB3    H  N N 479 
TYR HD1    H  N N 480 
TYR HD2    H  N N 481 
TYR HE1    H  N N 482 
TYR HE2    H  N N 483 
TYR HH     H  N N 484 
TYR HXT    H  N N 485 
VAL N      N  N N 486 
VAL CA     C  N S 487 
VAL C      C  N N 488 
VAL O      O  N N 489 
VAL CB     C  N N 490 
VAL CG1    C  N N 491 
VAL CG2    C  N N 492 
VAL OXT    O  N N 493 
VAL H      H  N N 494 
VAL H2     H  N N 495 
VAL HA     H  N N 496 
VAL HB     H  N N 497 
VAL HG11   H  N N 498 
VAL HG12   H  N N 499 
VAL HG13   H  N N 500 
VAL HG21   H  N N 501 
VAL HG22   H  N N 502 
VAL HG23   H  N N 503 
VAL HXT    H  N N 504 
ZN  ZN     ZN N N 505 
# 
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  
EOH C1    C2     sing N N 83  
EOH C1    O      sing N N 84  
EOH C1    H11    sing N N 85  
EOH C1    H12    sing N N 86  
EOH C2    H21    sing N N 87  
EOH C2    H22    sing N N 88  
EOH C2    H23    sing N N 89  
EOH O     HO     sing N N 90  
GLN N     CA     sing N N 91  
GLN N     H      sing N N 92  
GLN N     H2     sing N N 93  
GLN CA    C      sing N N 94  
GLN CA    CB     sing N N 95  
GLN CA    HA     sing N N 96  
GLN C     O      doub N N 97  
GLN C     OXT    sing N N 98  
GLN CB    CG     sing N N 99  
GLN CB    HB2    sing N N 100 
GLN CB    HB3    sing N N 101 
GLN CG    CD     sing N N 102 
GLN CG    HG2    sing N N 103 
GLN CG    HG3    sing N N 104 
GLN CD    OE1    doub N N 105 
GLN CD    NE2    sing N N 106 
GLN NE2   HE21   sing N N 107 
GLN NE2   HE22   sing N N 108 
GLN OXT   HXT    sing N N 109 
GLU N     CA     sing N N 110 
GLU N     H      sing N N 111 
GLU N     H2     sing N N 112 
GLU CA    C      sing N N 113 
GLU CA    CB     sing N N 114 
GLU CA    HA     sing N N 115 
GLU C     O      doub N N 116 
GLU C     OXT    sing N N 117 
GLU CB    CG     sing N N 118 
GLU CB    HB2    sing N N 119 
GLU CB    HB3    sing N N 120 
GLU CG    CD     sing N N 121 
GLU CG    HG2    sing N N 122 
GLU CG    HG3    sing N N 123 
GLU CD    OE1    doub N N 124 
GLU CD    OE2    sing N N 125 
GLU OE2   HE2    sing N N 126 
GLU OXT   HXT    sing N N 127 
GLY N     CA     sing N N 128 
GLY N     H      sing N N 129 
GLY N     H2     sing N N 130 
GLY CA    C      sing N N 131 
GLY CA    HA2    sing N N 132 
GLY CA    HA3    sing N N 133 
GLY C     O      doub N N 134 
GLY C     OXT    sing N N 135 
GLY OXT   HXT    sing N N 136 
GOL C1    O1     sing N N 137 
GOL C1    C2     sing N N 138 
GOL C1    H11    sing N N 139 
GOL C1    H12    sing N N 140 
GOL O1    HO1    sing N N 141 
GOL C2    O2     sing N N 142 
GOL C2    C3     sing N N 143 
GOL C2    H2     sing N N 144 
GOL O2    HO2    sing N N 145 
GOL C3    O3     sing N N 146 
GOL C3    H31    sing N N 147 
GOL C3    H32    sing N N 148 
GOL O3    HO3    sing N N 149 
HIS N     CA     sing N N 150 
HIS N     H      sing N N 151 
HIS N     H2     sing N N 152 
HIS CA    C      sing N N 153 
HIS CA    CB     sing N N 154 
HIS CA    HA     sing N N 155 
HIS C     O      doub N N 156 
HIS C     OXT    sing N N 157 
HIS CB    CG     sing N N 158 
HIS CB    HB2    sing N N 159 
HIS CB    HB3    sing N N 160 
HIS CG    ND1    sing Y N 161 
HIS CG    CD2    doub Y N 162 
HIS ND1   CE1    doub Y N 163 
HIS ND1   HD1    sing N N 164 
HIS CD2   NE2    sing Y N 165 
HIS CD2   HD2    sing N N 166 
HIS CE1   NE2    sing Y N 167 
HIS CE1   HE1    sing N N 168 
HIS NE2   HE2    sing N N 169 
HIS OXT   HXT    sing N N 170 
ILE N     CA     sing N N 171 
ILE N     H      sing N N 172 
ILE N     H2     sing N N 173 
ILE CA    C      sing N N 174 
ILE CA    CB     sing N N 175 
ILE CA    HA     sing N N 176 
ILE C     O      doub N N 177 
ILE C     OXT    sing N N 178 
ILE CB    CG1    sing N N 179 
ILE CB    CG2    sing N N 180 
ILE CB    HB     sing N N 181 
ILE CG1   CD1    sing N N 182 
ILE CG1   HG12   sing N N 183 
ILE CG1   HG13   sing N N 184 
ILE CG2   HG21   sing N N 185 
ILE CG2   HG22   sing N N 186 
ILE CG2   HG23   sing N N 187 
ILE CD1   HD11   sing N N 188 
ILE CD1   HD12   sing N N 189 
ILE CD1   HD13   sing N N 190 
ILE OXT   HXT    sing N N 191 
LEU N     CA     sing N N 192 
LEU N     H      sing N N 193 
LEU N     H2     sing N N 194 
LEU CA    C      sing N N 195 
LEU CA    CB     sing N N 196 
LEU CA    HA     sing N N 197 
LEU C     O      doub N N 198 
LEU C     OXT    sing N N 199 
LEU CB    CG     sing N N 200 
LEU CB    HB2    sing N N 201 
LEU CB    HB3    sing N N 202 
LEU CG    CD1    sing N N 203 
LEU CG    CD2    sing N N 204 
LEU CG    HG     sing N N 205 
LEU CD1   HD11   sing N N 206 
LEU CD1   HD12   sing N N 207 
LEU CD1   HD13   sing N N 208 
LEU CD2   HD21   sing N N 209 
LEU CD2   HD22   sing N N 210 
LEU CD2   HD23   sing N N 211 
LEU OXT   HXT    sing N N 212 
LYS N     CA     sing N N 213 
LYS N     H      sing N N 214 
LYS N     H2     sing N N 215 
LYS CA    C      sing N N 216 
LYS CA    CB     sing N N 217 
LYS CA    HA     sing N N 218 
LYS C     O      doub N N 219 
LYS C     OXT    sing N N 220 
LYS CB    CG     sing N N 221 
LYS CB    HB2    sing N N 222 
LYS CB    HB3    sing N N 223 
LYS CG    CD     sing N N 224 
LYS CG    HG2    sing N N 225 
LYS CG    HG3    sing N N 226 
LYS CD    CE     sing N N 227 
LYS CD    HD2    sing N N 228 
LYS CD    HD3    sing N N 229 
LYS CE    NZ     sing N N 230 
LYS CE    HE2    sing N N 231 
LYS CE    HE3    sing N N 232 
LYS NZ    HZ1    sing N N 233 
LYS NZ    HZ2    sing N N 234 
LYS NZ    HZ3    sing N N 235 
LYS OXT   HXT    sing N N 236 
MET N     CA     sing N N 237 
MET N     H      sing N N 238 
MET N     H2     sing N N 239 
MET CA    C      sing N N 240 
MET CA    CB     sing N N 241 
MET CA    HA     sing N N 242 
MET C     O      doub N N 243 
MET C     OXT    sing N N 244 
MET CB    CG     sing N N 245 
MET CB    HB2    sing N N 246 
MET CB    HB3    sing N N 247 
MET CG    SD     sing N N 248 
MET CG    HG2    sing N N 249 
MET CG    HG3    sing N N 250 
MET SD    CE     sing N N 251 
MET CE    HE1    sing N N 252 
MET CE    HE2    sing N N 253 
MET CE    HE3    sing N N 254 
MET OXT   HXT    sing N N 255 
PEG C1    O1     sing N N 256 
PEG C1    C2     sing N N 257 
PEG C1    H11    sing N N 258 
PEG C1    H12    sing N N 259 
PEG O1    HO1    sing N N 260 
PEG C2    O2     sing N N 261 
PEG C2    H21    sing N N 262 
PEG C2    H22    sing N N 263 
PEG O2    C3     sing N N 264 
PEG C3    C4     sing N N 265 
PEG C3    H31    sing N N 266 
PEG C3    H32    sing N N 267 
PEG C4    O4     sing N N 268 
PEG C4    H41    sing N N 269 
PEG C4    H42    sing N N 270 
PEG O4    HO4    sing N N 271 
PG4 O1    C1     sing N N 272 
PG4 O1    HO1    sing N N 273 
PG4 C1    C2     sing N N 274 
PG4 C1    H11    sing N N 275 
PG4 C1    H12    sing N N 276 
PG4 C2    O2     sing N N 277 
PG4 C2    H21    sing N N 278 
PG4 C2    H22    sing N N 279 
PG4 O2    C3     sing N N 280 
PG4 C3    C4     sing N N 281 
PG4 C3    H31    sing N N 282 
PG4 C3    H32    sing N N 283 
PG4 C4    O3     sing N N 284 
PG4 C4    H41    sing N N 285 
PG4 C4    H42    sing N N 286 
PG4 O3    C5     sing N N 287 
PG4 C5    C6     sing N N 288 
PG4 C5    H51    sing N N 289 
PG4 C5    H52    sing N N 290 
PG4 C6    O4     sing N N 291 
PG4 C6    H61    sing N N 292 
PG4 C6    H62    sing N N 293 
PG4 O4    C7     sing N N 294 
PG4 C7    C8     sing N N 295 
PG4 C7    H71    sing N N 296 
PG4 C7    H72    sing N N 297 
PG4 C8    O5     sing N N 298 
PG4 C8    H81    sing N N 299 
PG4 C8    H82    sing N N 300 
PG4 O5    HO5    sing N N 301 
PHE N     CA     sing N N 302 
PHE N     H      sing N N 303 
PHE N     H2     sing N N 304 
PHE CA    C      sing N N 305 
PHE CA    CB     sing N N 306 
PHE CA    HA     sing N N 307 
PHE C     O      doub N N 308 
PHE C     OXT    sing N N 309 
PHE CB    CG     sing N N 310 
PHE CB    HB2    sing N N 311 
PHE CB    HB3    sing N N 312 
PHE CG    CD1    doub Y N 313 
PHE CG    CD2    sing Y N 314 
PHE CD1   CE1    sing Y N 315 
PHE CD1   HD1    sing N N 316 
PHE CD2   CE2    doub Y N 317 
PHE CD2   HD2    sing N N 318 
PHE CE1   CZ     doub Y N 319 
PHE CE1   HE1    sing N N 320 
PHE CE2   CZ     sing Y N 321 
PHE CE2   HE2    sing N N 322 
PHE CZ    HZ     sing N N 323 
PHE OXT   HXT    sing N N 324 
PRO N     CA     sing N N 325 
PRO N     CD     sing N N 326 
PRO N     H      sing N N 327 
PRO CA    C      sing N N 328 
PRO CA    CB     sing N N 329 
PRO CA    HA     sing N N 330 
PRO C     O      doub N N 331 
PRO C     OXT    sing N N 332 
PRO CB    CG     sing N N 333 
PRO CB    HB2    sing N N 334 
PRO CB    HB3    sing N N 335 
PRO CG    CD     sing N N 336 
PRO CG    HG2    sing N N 337 
PRO CG    HG3    sing N N 338 
PRO CD    HD2    sing N N 339 
PRO CD    HD3    sing N N 340 
PRO OXT   HXT    sing N N 341 
SAH N     CA     sing N N 342 
SAH N     HN1    sing N N 343 
SAH N     HN2    sing N N 344 
SAH CA    CB     sing N N 345 
SAH CA    C      sing N N 346 
SAH CA    HA     sing N N 347 
SAH CB    CG     sing N N 348 
SAH CB    HB1    sing N N 349 
SAH CB    HB2    sing N N 350 
SAH CG    SD     sing N N 351 
SAH CG    HG1    sing N N 352 
SAH CG    HG2    sing N N 353 
SAH SD    "C5'"  sing N N 354 
SAH C     O      doub N N 355 
SAH C     OXT    sing N N 356 
SAH OXT   HXT    sing N N 357 
SAH "C5'" "C4'"  sing N N 358 
SAH "C5'" "H5'1" sing N N 359 
SAH "C5'" "H5'2" sing N N 360 
SAH "C4'" "O4'"  sing N N 361 
SAH "C4'" "C3'"  sing N N 362 
SAH "C4'" "H4'"  sing N N 363 
SAH "O4'" "C1'"  sing N N 364 
SAH "C3'" "O3'"  sing N N 365 
SAH "C3'" "C2'"  sing N N 366 
SAH "C3'" "H3'"  sing N N 367 
SAH "O3'" "HO3'" sing N N 368 
SAH "C2'" "O2'"  sing N N 369 
SAH "C2'" "C1'"  sing N N 370 
SAH "C2'" "H2'"  sing N N 371 
SAH "O2'" "HO2'" sing N N 372 
SAH "C1'" N9     sing N N 373 
SAH "C1'" "H1'"  sing N N 374 
SAH N9    C8     sing Y N 375 
SAH N9    C4     sing Y N 376 
SAH C8    N7     doub Y N 377 
SAH C8    H8     sing N N 378 
SAH N7    C5     sing Y N 379 
SAH C5    C6     sing Y N 380 
SAH C5    C4     doub Y N 381 
SAH C6    N6     sing N N 382 
SAH C6    N1     doub Y N 383 
SAH N6    HN61   sing N N 384 
SAH N6    HN62   sing N N 385 
SAH N1    C2     sing Y N 386 
SAH C2    N3     doub Y N 387 
SAH C2    H2     sing N N 388 
SAH N3    C4     sing Y N 389 
SER N     CA     sing N N 390 
SER N     H      sing N N 391 
SER N     H2     sing N N 392 
SER CA    C      sing N N 393 
SER CA    CB     sing N N 394 
SER CA    HA     sing N N 395 
SER C     O      doub N N 396 
SER C     OXT    sing N N 397 
SER CB    OG     sing N N 398 
SER CB    HB2    sing N N 399 
SER CB    HB3    sing N N 400 
SER OG    HG     sing N N 401 
SER OXT   HXT    sing N N 402 
THR N     CA     sing N N 403 
THR N     H      sing N N 404 
THR N     H2     sing N N 405 
THR CA    C      sing N N 406 
THR CA    CB     sing N N 407 
THR CA    HA     sing N N 408 
THR C     O      doub N N 409 
THR C     OXT    sing N N 410 
THR CB    OG1    sing N N 411 
THR CB    CG2    sing N N 412 
THR CB    HB     sing N N 413 
THR OG1   HG1    sing N N 414 
THR CG2   HG21   sing N N 415 
THR CG2   HG22   sing N N 416 
THR CG2   HG23   sing N N 417 
THR OXT   HXT    sing N N 418 
TRP N     CA     sing N N 419 
TRP N     H      sing N N 420 
TRP N     H2     sing N N 421 
TRP CA    C      sing N N 422 
TRP CA    CB     sing N N 423 
TRP CA    HA     sing N N 424 
TRP C     O      doub N N 425 
TRP C     OXT    sing N N 426 
TRP CB    CG     sing N N 427 
TRP CB    HB2    sing N N 428 
TRP CB    HB3    sing N N 429 
TRP CG    CD1    doub Y N 430 
TRP CG    CD2    sing Y N 431 
TRP CD1   NE1    sing Y N 432 
TRP CD1   HD1    sing N N 433 
TRP CD2   CE2    doub Y N 434 
TRP CD2   CE3    sing Y N 435 
TRP NE1   CE2    sing Y N 436 
TRP NE1   HE1    sing N N 437 
TRP CE2   CZ2    sing Y N 438 
TRP CE3   CZ3    doub Y N 439 
TRP CE3   HE3    sing N N 440 
TRP CZ2   CH2    doub Y N 441 
TRP CZ2   HZ2    sing N N 442 
TRP CZ3   CH2    sing Y N 443 
TRP CZ3   HZ3    sing N N 444 
TRP CH2   HH2    sing N N 445 
TRP OXT   HXT    sing N N 446 
TYR N     CA     sing N N 447 
TYR N     H      sing N N 448 
TYR N     H2     sing N N 449 
TYR CA    C      sing N N 450 
TYR CA    CB     sing N N 451 
TYR CA    HA     sing N N 452 
TYR C     O      doub N N 453 
TYR C     OXT    sing N N 454 
TYR CB    CG     sing N N 455 
TYR CB    HB2    sing N N 456 
TYR CB    HB3    sing N N 457 
TYR CG    CD1    doub Y N 458 
TYR CG    CD2    sing Y N 459 
TYR CD1   CE1    sing Y N 460 
TYR CD1   HD1    sing N N 461 
TYR CD2   CE2    doub Y N 462 
TYR CD2   HD2    sing N N 463 
TYR CE1   CZ     doub Y N 464 
TYR CE1   HE1    sing N N 465 
TYR CE2   CZ     sing Y N 466 
TYR CE2   HE2    sing N N 467 
TYR CZ    OH     sing N N 468 
TYR OH    HH     sing N N 469 
TYR OXT   HXT    sing N N 470 
VAL N     CA     sing N N 471 
VAL N     H      sing N N 472 
VAL N     H2     sing N N 473 
VAL CA    C      sing N N 474 
VAL CA    CB     sing N N 475 
VAL CA    HA     sing N N 476 
VAL C     O      doub N N 477 
VAL C     OXT    sing N N 478 
VAL CB    CG1    sing N N 479 
VAL CB    CG2    sing N N 480 
VAL CB    HB     sing N N 481 
VAL CG1   HG11   sing N N 482 
VAL CG1   HG12   sing N N 483 
VAL CG1   HG13   sing N N 484 
VAL CG2   HG21   sing N N 485 
VAL CG2   HG22   sing N N 486 
VAL CG2   HG23   sing N N 487 
VAL OXT   HXT    sing N N 488 
# 
_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     'I 4' 
_space_group.name_Hall        'I 4' 
_space_group.IT_number        79 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9CKG 
_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]   0.006587 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006587 
_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]   0.018735 
_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    ? ? 7.96527  ?       ? ? 9.05267  ?        ? ? 0.0 
;1-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   ? 44.68000 -6.91000  -0.91800  1.000 113.71363 ? 5   GLY A N     1 
ATOM   2    C  CA    . GLY A 1 5   ? 44.98800 -7.83100  -2.02800  1.000 108.18666 ? 5   GLY A CA    1 
ATOM   3    C  C     . GLY A 1 5   ? 43.78200 -8.64900  -2.45000  1.000 108.87621 ? 5   GLY A C     1 
ATOM   4    O  O     . GLY A 1 5   ? 42.81500 -8.04300  -2.95300  1.000 111.28966 ? 5   GLY A O     1 
ATOM   5    N  N     . LEU A 1 6   ? 43.83300 -9.97400  -2.26500  1.000 101.36215 ? 6   LEU A N     1 
ATOM   6    C  CA    . LEU A 1 6   ? 42.74500 -10.84100 -2.70100  1.000 92.09262  ? 6   LEU A CA    1 
ATOM   7    C  C     . LEU A 1 6   ? 42.25500 -11.72800 -1.56500  1.000 86.48405  ? 6   LEU A C     1 
ATOM   8    O  O     . LEU A 1 6   ? 43.06000 -12.38500 -0.90000  1.000 86.52880  ? 6   LEU A O     1 
ATOM   9    C  CB    . LEU A 1 6   ? 43.18800 -11.71300 -3.88200  1.000 86.28666  ? 6   LEU A CB    1 
ATOM   10   C  CG    . LEU A 1 6   ? 43.61200 -10.97500 -5.15000  1.000 87.57103  ? 6   LEU A CG    1 
ATOM   11   C  CD1   . LEU A 1 6   ? 44.40600 -11.88800 -6.06800  1.000 78.28307  ? 6   LEU A CD1   1 
ATOM   12   C  CD2   . LEU A 1 6   ? 42.38300 -10.43600 -5.86300  1.000 87.32100  ? 6   LEU A CD2   1 
ATOM   13   N  N     . GLY A 1 7   ? 40.94600 -11.72200 -1.32700  1.000 83.23893  ? 7   GLY A N     1 
ATOM   14   C  CA    . GLY A 1 7   ? 40.40500 -12.47200 -0.20400  1.000 85.70238  ? 7   GLY A CA    1 
ATOM   15   C  C     . GLY A 1 7   ? 40.69500 -13.95700 -0.35000  1.000 75.80909  ? 7   GLY A C     1 
ATOM   16   O  O     . GLY A 1 7   ? 40.56100 -14.53200 -1.43200  1.000 77.68826  ? 7   GLY A O     1 
ATOM   17   N  N     . GLY A 1 8   ? 41.08500 -14.58500 0.75800   1.000 74.84582  ? 8   GLY A N     1 
ATOM   18   C  CA    . GLY A 1 8   ? 41.34000 -16.01000 0.78100   1.000 68.45294  ? 8   GLY A CA    1 
ATOM   19   C  C     . GLY A 1 8   ? 42.65100 -16.42500 0.15000   1.000 75.36956  ? 8   GLY A C     1 
ATOM   20   O  O     . GLY A 1 8   ? 42.87400 -17.62600 -0.04900  1.000 78.16200  ? 8   GLY A O     1 
ATOM   21   N  N     . LEU A 1 9   ? 43.53000 -15.47000 -0.15300  1.000 81.50714  ? 9   LEU A N     1 
ATOM   22   C  CA    . LEU A 1 9   ? 44.81000 -15.71400 -0.80500  1.000 70.66900  ? 9   LEU A CA    1 
ATOM   23   C  C     . LEU A 1 9   ? 45.84300 -14.79900 -0.16800  1.000 67.87130  ? 9   LEU A C     1 
ATOM   24   O  O     . LEU A 1 9   ? 45.50300 -13.78000 0.43700   1.000 74.66422  ? 9   LEU A O     1 
ATOM   25   C  CB    . LEU A 1 9   ? 44.75100 -15.49100 -2.32000  1.000 69.66362  ? 9   LEU A CB    1 
ATOM   26   C  CG    . LEU A 1 9   ? 43.70300 -16.29100 -3.09300  1.000 71.70070  ? 9   LEU A CG    1 
ATOM   27   C  CD1   . LEU A 1 9   ? 43.44000 -15.62300 -4.42500  1.000 77.34612  ? 9   LEU A CD1   1 
ATOM   28   C  CD2   . LEU A 1 9   ? 44.17100 -17.72700 -3.29700  1.000 64.88673  ? 9   LEU A CD2   1 
ATOM   29   N  N     . GLU A 1 10  ? 47.12500 -15.13200 -0.35800  1.000 82.05194  ? 10  GLU A N     1 
ATOM   30   C  CA    . GLU A 1 10  ? 48.19400 -14.33600 0.30200   1.000 82.59148  ? 10  GLU A CA    1 
ATOM   31   C  C     . GLU A 1 10  ? 49.53400 -14.49500 -0.41500  1.000 80.77811  ? 10  GLU A C     1 
ATOM   32   O  O     . GLU A 1 10  ? 49.96900 -15.65100 -0.59700  1.000 79.69377  ? 10  GLU A O     1 
ATOM   33   C  CB    . GLU A 1 10  ? 48.36700 -14.81700 1.74200   1.000 84.86017  ? 10  GLU A CB    1 
ATOM   34   C  CG    . GLU A 1 10  ? 49.64200 -14.34900 2.41000   1.000 100.03305 ? 10  GLU A CG    1 
ATOM   35   C  CD    . GLU A 1 10  ? 49.72800 -14.82100 3.84900   1.000 109.16309 ? 10  GLU A CD    1 
ATOM   36   O  OE1   . GLU A 1 10  ? 48.80300 -15.53400 4.27800   1.000 105.18103 ? 10  GLU A OE1   1 
ATOM   37   O  OE2   . GLU A 1 10  ? 50.71500 -14.48300 4.53100   1.000 113.20568 ? 10  GLU A OE2   1 
ATOM   38   N  N     . ARG A 1 11  ? 50.15900 -13.38200 -0.81000  1.000 75.28271  ? 11  ARG A N     1 
ATOM   39   C  CA    . ARG A 1 11  ? 51.50500 -13.45500 -1.36200  1.000 72.25866  ? 11  ARG A CA    1 
ATOM   40   C  C     . ARG A 1 11  ? 52.47900 -13.91900 -0.28600  1.000 73.44302  ? 11  ARG A C     1 
ATOM   41   O  O     . ARG A 1 11  ? 52.39900 -13.47800 0.86400   1.000 79.29109  ? 11  ARG A O     1 
ATOM   42   C  CB    . ARG A 1 11  ? 51.92300 -12.10100 -1.93600  1.000 69.26620  ? 11  ARG A CB    1 
ATOM   43   C  CG    . ARG A 1 11  ? 53.38200 -12.01100 -2.33200  1.000 63.88661  ? 11  ARG A CG    1 
ATOM   44   C  CD    . ARG A 1 11  ? 53.65900 -10.72700 -3.09600  1.000 65.99739  ? 11  ARG A CD    1 
ATOM   45   N  NE    . ARG A 1 11  ? 55.03800 -10.27800 -2.95000  1.000 76.23546  ? 11  ARG A NE    1 
ATOM   46   C  CZ    . ARG A 1 11  ? 55.53500 -9.19000  -3.52300  1.000 84.32064  ? 11  ARG A CZ    1 
ATOM   47   N  NH1   . ARG A 1 11  ? 54.78900 -8.41100  -4.29200  1.000 75.54590  ? 11  ARG A NH1   1 
ATOM   48   N  NH2   . ARG A 1 11  ? 56.81100 -8.87400  -3.32000  1.000 86.31298  ? 11  ARG A NH2   1 
ATOM   49   N  N     . PHE A 1 12  ? 53.39900 -14.81400 -0.64500  1.000 69.00564  ? 12  PHE A N     1 
ATOM   50   C  CA    . PHE A 1 12  ? 54.34400 -15.29900 0.35200   1.000 72.37973  ? 12  PHE A CA    1 
ATOM   51   C  C     . PHE A 1 12  ? 55.64000 -15.69100 -0.33900  1.000 71.71123  ? 12  PHE A C     1 
ATOM   52   O  O     . PHE A 1 12  ? 55.73900 -15.67700 -1.56500  1.000 71.35856  ? 12  PHE A O     1 
ATOM   53   C  CB    . PHE A 1 12  ? 53.77000 -16.47900 1.14100   1.000 76.48812  ? 12  PHE A CB    1 
ATOM   54   C  CG    . PHE A 1 12  ? 53.87800 -17.79100 0.42500   1.000 74.17995  ? 12  PHE A CG    1 
ATOM   55   C  CD1   . PHE A 1 12  ? 53.17900 -18.01700 -0.74800  1.000 71.76387  ? 12  PHE A CD1   1 
ATOM   56   C  CD2   . PHE A 1 12  ? 54.68200 -18.80100 0.92500   1.000 73.14035  ? 12  PHE A CD2   1 
ATOM   57   C  CE1   . PHE A 1 12  ? 53.28200 -19.22300 -1.40700  1.000 66.81064  ? 12  PHE A CE1   1 
ATOM   58   C  CE2   . PHE A 1 12  ? 54.78900 -20.00800 0.27100   1.000 59.27026  ? 12  PHE A CE2   1 
ATOM   59   C  CZ    . PHE A 1 12  ? 54.08800 -20.22000 -0.89500  1.000 61.81531  ? 12  PHE A CZ    1 
ATOM   60   N  N     . CYS A 1 13  ? 56.65800 -15.99300 0.48000   1.000 72.42447  ? 13  CYS A N     1 
ATOM   61   C  CA    . CYS A 1 13  ? 57.97900 -16.41600 -0.05700  1.000 73.34564  ? 13  CYS A CA    1 
ATOM   62   C  C     . CYS A 1 13  ? 58.03100 -17.94300 -0.11500  1.000 73.56408  ? 13  CYS A C     1 
ATOM   63   O  O     . CYS A 1 13  ? 58.14400 -18.56500 0.95900   1.000 80.44912  ? 13  CYS A O     1 
ATOM   64   C  CB    . CYS A 1 13  ? 59.12200 -15.89900 0.80600   1.000 76.40916  ? 13  CYS A CB    1 
ATOM   65   S  SG    . CYS A 1 13  ? 59.25400 -14.09200 0.80300   1.000 111.26597 ? 13  CYS A SG    1 
ATOM   66   N  N     . SER A 1 14  ? 57.95400 -18.51400 -1.31500  1.000 72.19287  ? 14  SER A N     1 
ATOM   67   C  CA    . SER A 1 14  ? 57.96900 -19.95400 -1.51900  1.000 72.06127  ? 14  SER A CA    1 
ATOM   68   C  C     . SER A 1 14  ? 59.40500 -20.43800 -1.68200  1.000 81.14131  ? 14  SER A C     1 
ATOM   69   O  O     . SER A 1 14  ? 60.10000 -20.00300 -2.63000  1.000 86.48932  ? 14  SER A O     1 
ATOM   70   C  CB    . SER A 1 14  ? 57.15800 -20.33700 -2.74300  1.000 70.42423  ? 14  SER A CB    1 
ATOM   71   O  OG    . SER A 1 14  ? 57.15600 -21.74400 -2.92500  1.000 72.17971  ? 14  SER A OG    1 
ATOM   72   N  N     . PRO A 1 15  ? 59.90300 -21.28300 -0.74800  1.000 80.30173  ? 15  PRO A N     1 
ATOM   73   C  CA    . PRO A 1 15  ? 61.30100 -21.73600 -0.75900  1.000 79.33583  ? 15  PRO A CA    1 
ATOM   74   C  C     . PRO A 1 15  ? 61.71100 -22.37200 -2.07600  1.000 75.55380  ? 15  PRO A C     1 
ATOM   75   O  O     . PRO A 1 15  ? 61.08200 -23.32100 -2.55400  1.000 78.03830  ? 15  PRO A O     1 
ATOM   76   C  CB    . PRO A 1 15  ? 61.35600 -22.74600 0.39600   1.000 91.18988  ? 15  PRO A CB    1 
ATOM   77   C  CG    . PRO A 1 15  ? 60.23300 -22.36000 1.30000   1.000 85.68922  ? 15  PRO A CG    1 
ATOM   78   C  CD    . PRO A 1 15  ? 59.15400 -21.81400 0.40700   1.000 80.73600  ? 15  PRO A CD    1 
ATOM   79   N  N     . GLY A 1 16  ? 62.77600 -21.83800 -2.65800  1.000 80.61230  ? 16  GLY A N     1 
ATOM   80   C  CA    . GLY A 1 16  ? 63.32700 -22.26800 -3.92300  1.000 82.76782  ? 16  GLY A CA    1 
ATOM   81   C  C     . GLY A 1 16  ? 62.59900 -21.74000 -5.13600  1.000 79.68850  ? 16  GLY A C     1 
ATOM   82   O  O     . GLY A 1 16  ? 63.02500 -22.01700 -6.26500  1.000 79.01737  ? 16  GLY A O     1 
ATOM   83   N  N     . LYS A 1 17  ? 61.53100 -20.96600 -4.93800  1.000 79.70956  ? 17  LYS A N     1 
ATOM   84   C  CA    . LYS A 1 17  ? 60.74600 -20.41500 -6.02700  1.000 71.06642  ? 17  LYS A CA    1 
ATOM   85   C  C     . LYS A 1 17  ? 60.59300 -18.90700 -5.93200  1.000 68.80299  ? 17  LYS A C     1 
ATOM   86   O  O     . LYS A 1 17  ? 59.88400 -18.32200 -6.75900  1.000 75.14848  ? 17  LYS A O     1 
ATOM   87   C  CB    . LYS A 1 17  ? 59.37600 -21.10100 -6.11700  1.000 71.99811  ? 17  LYS A CB    1 
ATOM   88   C  CG    . LYS A 1 17  ? 59.50800 -22.60900 -6.22700  1.000 70.80849  ? 17  LYS A CG    1 
ATOM   89   C  CD    . LYS A 1 17  ? 58.38500 -23.36400 -5.57000  1.000 72.79294  ? 17  LYS A CD    1 
ATOM   90   C  CE    . LYS A 1 17  ? 58.55600 -24.85000 -5.82800  1.000 77.04082  ? 17  LYS A CE    1 
ATOM   91   N  NZ    . LYS A 1 17  ? 58.10400 -25.67500 -4.67700  1.000 73.76148  ? 17  LYS A NZ    1 
ATOM   92   N  N     . GLY A 1 18  ? 61.24000 -18.25700 -4.96800  1.000 74.24838  ? 18  GLY A N     1 
ATOM   93   C  CA    . GLY A 1 18  ? 61.01500 -16.82200 -4.83200  1.000 80.33858  ? 18  GLY A CA    1 
ATOM   94   C  C     . GLY A 1 18  ? 59.65400 -16.54500 -4.24600  1.000 74.52209  ? 18  GLY A C     1 
ATOM   95   O  O     . GLY A 1 18  ? 59.31400 -17.07000 -3.19300  1.000 75.79067  ? 18  GLY A O     1 
ATOM   96   N  N     . ARG A 1 19  ? 58.90000 -15.64300 -4.86000  1.000 71.94020  ? 19  ARG A N     1 
ATOM   97   C  CA    . ARG A 1 19  ? 57.57800 -15.30600 -4.35400  1.000 67.43966  ? 19  ARG A CA    1 
ATOM   98   C  C     . ARG A 1 19  ? 56.51600 -16.15900 -5.03700  1.000 68.26608  ? 19  ARG A C     1 
ATOM   99   O  O     . ARG A 1 19  ? 56.63700 -16.51400 -6.21200  1.000 68.52664  ? 19  ARG A O     1 
ATOM   100  C  CB    . ARG A 1 19  ? 57.29600 -13.82600 -4.58100  1.000 66.12109  ? 19  ARG A CB    1 
ATOM   101  C  CG    . ARG A 1 19  ? 58.30100 -12.92300 -3.90100  1.000 71.36382  ? 19  ARG A CG    1 
ATOM   102  C  CD    . ARG A 1 19  ? 58.25300 -11.56900 -4.54100  1.000 73.53776  ? 19  ARG A CD    1 
ATOM   103  N  NE    . ARG A 1 19  ? 58.65900 -11.68400 -5.93700  1.000 76.79079  ? 19  ARG A NE    1 
ATOM   104  C  CZ    . ARG A 1 19  ? 58.78300 -10.66200 -6.77200  1.000 76.59603  ? 19  ARG A CZ    1 
ATOM   105  N  NH1   . ARG A 1 19  ? 58.54000 -9.42100  -6.38500  1.000 85.02862  ? 19  ARG A NH1   1 
ATOM   106  N  NH2   . ARG A 1 19  ? 59.16000 -10.89200 -8.02700  1.000 68.66613  ? 19  ARG A NH2   1 
ATOM   107  N  N     . GLY A 1 20  ? 55.47200 -16.49300 -4.28000  1.000 68.63191  ? 20  GLY A N     1 
ATOM   108  C  CA    . GLY A 1 20  ? 54.39200 -17.32800 -4.75600  1.000 60.84940  ? 20  GLY A CA    1 
ATOM   109  C  C     . GLY A 1 20  ? 53.07400 -16.89400 -4.15100  1.000 61.58370  ? 20  GLY A C     1 
ATOM   110  O  O     . GLY A 1 20  ? 53.00800 -15.96600 -3.34100  1.000 70.65847  ? 20  GLY A O     1 
ATOM   111  N  N     . LEU A 1 21  ? 52.02400 -17.62200 -4.51800  1.000 56.15936  ? 21  LEU A N     1 
ATOM   112  C  CA    . LEU A 1 21  ? 50.66700 -17.38800 -4.04200  1.000 59.30185  ? 21  LEU A CA    1 
ATOM   113  C  C     . LEU A 1 21  ? 50.20600 -18.58000 -3.21900  1.000 65.85526  ? 21  LEU A C     1 
ATOM   114  O  O     . LEU A 1 21  ? 50.37700 -19.72900 -3.63800  1.000 73.65094  ? 21  LEU A O     1 
ATOM   115  C  CB    . LEU A 1 21  ? 49.70300 -17.12900 -5.20500  1.000 59.96245  ? 21  LEU A CB    1 
ATOM   116  C  CG    . LEU A 1 21  ? 48.29700 -16.66900 -4.80600  1.000 61.27314  ? 21  LEU A CG    1 
ATOM   117  C  CD1   . LEU A 1 21  ? 48.36900 -15.32900 -4.10900  1.000 72.46395  ? 21  LEU A CD1   1 
ATOM   118  C  CD2   . LEU A 1 21  ? 47.39300 -16.56100 -6.02400  1.000 64.96042  ? 21  LEU A CD2   1 
ATOM   119  N  N     . ARG A 1 22  ? 49.70000 -18.28100 -2.01900  1.000 69.34516  ? 22  ARG A N     1 
ATOM   120  C  CA    . ARG A 1 22  ? 49.25400 -19.34600 -1.09000  1.000 69.06618  ? 22  ARG A CA    1 
ATOM   121  C  C     . ARG A 1 22  ? 47.76800 -19.16500 -0.80300  1.000 69.77942  ? 22  ARG A C     1 
ATOM   122  O  O     . ARG A 1 22  ? 47.31000 -18.01000 -0.79700  1.000 71.61648  ? 22  ARG A O     1 
ATOM   123  C  CB    . ARG A 1 22  ? 49.98800 -19.20500 0.24500   1.000 71.92441  ? 22  ARG A CB    1 
ATOM   124  C  CG    . ARG A 1 22  ? 50.22000 -20.52100 0.96900   1.000 84.78911  ? 22  ARG A CG    1 
ATOM   125  C  CD    . ARG A 1 22  ? 51.33700 -20.43400 1.98800   1.000 87.66314  ? 22  ARG A CD    1 
ATOM   126  N  NE    . ARG A 1 22  ? 51.32100 -19.20200 2.76100   1.000 79.20950  ? 22  ARG A NE    1 
ATOM   127  C  CZ    . ARG A 1 22  ? 52.17000 -18.93200 3.74500   1.000 80.52544  ? 22  ARG A CZ    1 
ATOM   128  N  NH1   . ARG A 1 22  ? 53.10400 -19.81100 4.06800   1.000 85.20232  ? 22  ARG A NH1   1 
ATOM   129  N  NH2   . ARG A 1 22  ? 52.08800 -17.78900 4.40000   1.000 82.07563  ? 22  ARG A NH2   1 
ATOM   130  N  N     . ALA A 1 23  ? 47.05500 -20.26400 -0.57200  1.000 68.47926  ? 23  ALA A N     1 
ATOM   131  C  CA    . ALA A 1 23  ? 45.64600 -20.20500 -0.21600  1.000 67.08436  ? 23  ALA A CA    1 
ATOM   132  C  C     . ALA A 1 23  ? 45.50400 -20.06500 1.29200   1.000 73.30616  ? 23  ALA A C     1 
ATOM   133  O  O     . ALA A 1 23  ? 46.22100 -20.71000 2.06200   1.000 81.43608  ? 23  ALA A O     1 
ATOM   134  C  CB    . ALA A 1 23  ? 44.90900 -21.45100 -0.70400  1.000 68.11080  ? 23  ALA A CB    1 
ATOM   135  N  N     . LEU A 1 24  ? 44.54200 -19.24800 1.71300   1.000 66.47113  ? 24  LEU A N     1 
ATOM   136  C  CA    . LEU A 1 24  ? 44.22000 -19.10400 3.12300   1.000 73.32195  ? 24  LEU A CA    1 
ATOM   137  C  C     . LEU A 1 24  ? 42.90600 -19.76100 3.49900   1.000 79.75430  ? 24  LEU A C     1 
ATOM   138  O  O     . LEU A 1 24  ? 42.61900 -19.89400 4.69300   1.000 82.93889  ? 24  LEU A O     1 
ATOM   139  C  CB    . LEU A 1 24  ? 44.21100 -17.62800 3.54200   1.000 70.31106  ? 24  LEU A CB    1 
ATOM   140  C  CG    . LEU A 1 24  ? 45.60100 -16.99900 3.42900   1.000 76.30915  ? 24  LEU A CG    1 
ATOM   141  C  CD1   . LEU A 1 24  ? 45.56500 -15.50000 3.72300   1.000 83.41000  ? 24  LEU A CD1   1 
ATOM   142  C  CD2   . LEU A 1 24  ? 46.60700 -17.74000 4.33100   1.000 76.66446  ? 24  LEU A CD2   1 
ATOM   143  N  N     . GLN A 1 25  ? 42.10700 -20.16300 2.52200   1.000 77.49087  ? 25  GLN A N     1 
ATOM   144  C  CA    . GLN A 1 25  ? 40.84100 -20.84000 2.74000   1.000 75.74592  ? 25  GLN A CA    1 
ATOM   145  C  C     . GLN A 1 25  ? 40.77800 -21.97500 1.73300   1.000 73.94044  ? 25  GLN A C     1 
ATOM   146  O  O     . GLN A 1 25  ? 41.51500 -21.96400 0.73800   1.000 80.70441  ? 25  GLN A O     1 
ATOM   147  C  CB    . GLN A 1 25  ? 39.67200 -19.85600 2.57400   1.000 76.63287  ? 25  GLN A CB    1 
ATOM   148  C  CG    . GLN A 1 25  ? 39.53600 -19.26300 1.16600   1.000 79.77799  ? 25  GLN A CG    1 
ATOM   149  C  CD    . GLN A 1 25  ? 38.47500 -18.16800 1.07800   1.000 87.05254  ? 25  GLN A CD    1 
ATOM   150  O  OE1   . GLN A 1 25  ? 38.30200 -17.38100 2.01300   1.000 92.21632  ? 25  GLN A OE1   1 
ATOM   151  N  NE2   . GLN A 1 25  ? 37.78000 -18.09800 -0.05700  1.000 75.23534  ? 25  GLN A NE2   1 
ATOM   152  N  N     . PRO A 1 26  ? 39.89700 -22.96000 1.93600   1.000 67.55284  ? 26  PRO A N     1 
ATOM   153  C  CA    . PRO A 1 26  ? 39.81300 -24.05600 0.96400   1.000 67.94236  ? 26  PRO A CA    1 
ATOM   154  C  C     . PRO A 1 26  ? 39.15700 -23.65900 -0.34400  1.000 77.03818  ? 26  PRO A C     1 
ATOM   155  O  O     . PRO A 1 26  ? 38.25700 -22.81700 -0.39700  1.000 81.70716  ? 26  PRO A O     1 
ATOM   156  C  CB    . PRO A 1 26  ? 38.97100 -25.10900 1.68900   1.000 68.12133  ? 26  PRO A CB    1 
ATOM   157  C  CG    . PRO A 1 26  ? 38.15600 -24.33400 2.64600   1.000 76.88290  ? 26  PRO A CG    1 
ATOM   158  C  CD    . PRO A 1 26  ? 39.02700 -23.19500 3.10100   1.000 76.63024  ? 26  PRO A CD    1 
ATOM   159  N  N     . PHE A 1 27  ? 39.62400 -24.29400 -1.41500  1.000 73.72726  ? 27  PHE A N     1 
ATOM   160  C  CA    . PHE A 1 27  ? 38.99900 -24.17000 -2.71900  1.000 74.09573  ? 27  PHE A CA    1 
ATOM   161  C  C     . PHE A 1 27  ? 38.75800 -25.54900 -3.30900  1.000 82.37303  ? 27  PHE A C     1 
ATOM   162  O  O     . PHE A 1 27  ? 39.68300 -26.35800 -3.39600  1.000 84.78122  ? 27  PHE A O     1 
ATOM   163  C  CB    . PHE A 1 27  ? 39.88600 -23.36100 -3.66100  1.000 72.15602  ? 27  PHE A CB    1 
ATOM   164  C  CG    . PHE A 1 27  ? 39.99600 -21.91200 -3.29700  1.000 68.13975  ? 27  PHE A CG    1 
ATOM   165  C  CD1   . PHE A 1 27  ? 39.00800 -21.00900 -3.64800  1.000 74.64579  ? 27  PHE A CD1   1 
ATOM   166  C  CD2   . PHE A 1 27  ? 41.10300 -21.45100 -2.60300  1.000 63.34970  ? 27  PHE A CD2   1 
ATOM   167  C  CE1   . PHE A 1 27  ? 39.12400 -19.67400 -3.31800  1.000 76.21966  ? 27  PHE A CE1   1 
ATOM   168  C  CE2   . PHE A 1 27  ? 41.22300 -20.12000 -2.26800  1.000 68.39241  ? 27  PHE A CE2   1 
ATOM   169  C  CZ    . PHE A 1 27  ? 40.23300 -19.22900 -2.62500  1.000 75.04847  ? 27  PHE A CZ    1 
ATOM   170  N  N     . GLN A 1 28  ? 37.52200 -25.75700 -3.75500  1.000 93.36909  ? 28  GLN A N     1 
ATOM   171  C  CA    . GLN A 1 28  ? 37.16100 -27.04400 -4.38100  1.000 93.00852  ? 28  GLN A CA    1 
ATOM   172  C  C     . GLN A 1 28  ? 37.42700 -26.97100 -5.87500  1.000 92.53478  ? 28  GLN A C     1 
ATOM   173  O  O     . GLN A 1 28  ? 37.55000 -25.85500 -6.39800  1.000 89.82393  ? 28  GLN A O     1 
ATOM   174  C  CB    . GLN A 1 28  ? 35.65800 -27.28100 -4.24600  1.000 94.79558  ? 28  GLN A CB    1 
ATOM   175  C  CG    . GLN A 1 28  ? 35.19700 -27.41900 -2.80900  1.000 96.96426  ? 28  GLN A CG    1 
ATOM   176  C  CD    . GLN A 1 28  ? 36.03900 -28.44900 -2.10300  1.000 106.86808 ? 28  GLN A CD    1 
ATOM   177  O  OE1   . GLN A 1 28  ? 36.80700 -28.13700 -1.19400  1.000 110.19216 ? 28  GLN A OE1   1 
ATOM   178  N  NE2   . GLN A 1 28  ? 35.89300 -29.70100 -2.50800  1.000 103.79402 ? 28  GLN A NE2   1 
ATOM   179  N  N     . VAL A 1 29  ? 37.46300 -28.15400 -6.50600  1.000 76.14860  ? 29  VAL A N     1 
ATOM   180  C  CA    . VAL A 1 29  ? 37.64100 -28.25100 -7.98200  1.000 72.20866  ? 29  VAL A CA    1 
ATOM   181  C  C     . VAL A 1 29  ? 36.53000 -27.43000 -8.62900  1.000 73.83517  ? 29  VAL A C     1 
ATOM   182  O  O     . VAL A 1 29  ? 35.34600 -27.74300 -8.39100  1.000 75.75645  ? 29  VAL A O     1 
ATOM   183  C  CB    . VAL A 1 29  ? 37.58500 -29.72100 -8.43900  1.000 71.53489  ? 29  VAL A CB    1 
ATOM   184  C  CG1   . VAL A 1 29  ? 37.98200 -29.88800 -9.89600  1.000 75.95648  ? 29  VAL A CG1   1 
ATOM   185  C  CG2   . VAL A 1 29  ? 38.42200 -30.62200 -7.54600  1.000 72.74556  ? 29  VAL A CG2   1 
ATOM   186  N  N     . GLY A 1 30  ? 36.90200 -26.42200 -9.40900  1.000 70.40055  ? 30  GLY A N     1 
ATOM   187  C  CA    . GLY A 1 30  ? 35.94800 -25.53200 -10.04500 1.000 65.70788  ? 30  GLY A CA    1 
ATOM   188  C  C     . GLY A 1 30  ? 35.74300 -24.18800 -9.35600  1.000 75.57485  ? 30  GLY A C     1 
ATOM   189  O  O     . GLY A 1 30  ? 35.14400 -23.29100 -9.96500  1.000 74.28522  ? 30  GLY A O     1 
ATOM   190  N  N     . ASP A 1 31  ? 36.19300 -24.01900 -8.10900  1.000 82.41251  ? 31  ASP A N     1 
ATOM   191  C  CA    . ASP A 1 31  ? 36.00600 -22.73800 -7.43200  1.000 83.56791  ? 31  ASP A CA    1 
ATOM   192  C  C     . ASP A 1 31  ? 36.85600 -21.67900 -8.12300  1.000 82.16775  ? 31  ASP A C     1 
ATOM   193  O  O     . ASP A 1 31  ? 37.94600 -21.96100 -8.62600  1.000 80.84127  ? 31  ASP A O     1 
ATOM   194  C  CB    . ASP A 1 31  ? 36.39400 -22.80800 -5.95100  1.000 87.36837  ? 31  ASP A CB    1 
ATOM   195  C  CG    . ASP A 1 31  ? 35.38700 -23.57200 -5.10600  1.000 95.35617  ? 31  ASP A CG    1 
ATOM   196  O  OD1   . ASP A 1 31  ? 34.33800 -23.98700 -5.64200  1.000 97.44853  ? 31  ASP A OD1   1 
ATOM   197  O  OD2   . ASP A 1 31  ? 35.63100 -23.71300 -3.88500  1.000 94.89032  ? 31  ASP A OD2   1 
ATOM   198  N  N     . LEU A 1 32  ? 36.35000 -20.45100 -8.15100  1.000 68.06079  ? 32  LEU A N     1 
ATOM   199  C  CA    . LEU A 1 32  ? 37.11500 -19.34300 -8.70800  1.000 64.89989  ? 32  LEU A CA    1 
ATOM   200  C  C     . LEU A 1 32  ? 38.04200 -18.78300 -7.64100  1.000 66.12109  ? 32  LEU A C     1 
ATOM   201  O  O     . LEU A 1 32  ? 37.58000 -18.25300 -6.62400  1.000 56.74628  ? 32  LEU A O     1 
ATOM   202  C  CB    . LEU A 1 32  ? 36.19000 -18.24400 -9.21800  1.000 62.79700  ? 32  LEU A CB    1 
ATOM   203  C  CG    . LEU A 1 32  ? 36.89900 -17.03500 -9.83500  1.000 59.38870  ? 32  LEU A CG    1 
ATOM   204  C  CD1   . LEU A 1 32  ? 37.70900 -17.43600 -11.05300 1.000 61.32051  ? 32  LEU A CD1   1 
ATOM   205  C  CD2   . LEU A 1 32  ? 35.90300 -15.92700 -10.15900 1.000 66.42112  ? 32  LEU A CD2   1 
ATOM   206  N  N     . LEU A 1 33  ? 39.35600 -18.92100 -7.84900  1.000 66.21320  ? 33  LEU A N     1 
ATOM   207  C  CA    . LEU A 1 33  ? 40.27600 -18.30200 -6.90500  1.000 62.40222  ? 33  LEU A CA    1 
ATOM   208  C  C     . LEU A 1 33  ? 40.26500 -16.79700 -7.10300  1.000 62.78384  ? 33  LEU A C     1 
ATOM   209  O  O     . LEU A 1 33  ? 40.00800 -16.04500 -6.15400  1.000 67.89761  ? 33  LEU A O     1 
ATOM   210  C  CB    . LEU A 1 33  ? 41.69400 -18.86000 -7.04900  1.000 58.13329  ? 33  LEU A CB    1 
ATOM   211  C  CG    . LEU A 1 33  ? 42.02500 -20.19300 -6.37200  1.000 62.06007  ? 33  LEU A CG    1 
ATOM   212  C  CD1   . LEU A 1 33  ? 41.37500 -21.37700 -7.08000  1.000 60.73097  ? 33  LEU A CD1   1 
ATOM   213  C  CD2   . LEU A 1 33  ? 43.53300 -20.36700 -6.25300  1.000 51.27457  ? 33  LEU A CD2   1 
ATOM   214  N  N     . PHE A 1 34  ? 40.51500 -16.33000 -8.32800  1.000 63.65763  ? 34  PHE A N     1 
ATOM   215  C  CA    . PHE A 1 34  ? 40.43900 -14.87700 -8.49700  1.000 64.84198  ? 34  PHE A CA    1 
ATOM   216  C  C     . PHE A 1 34  ? 40.36900 -14.50700 -9.97200  1.000 63.58394  ? 34  PHE A C     1 
ATOM   217  O  O     . PHE A 1 34  ? 40.59700 -15.33100 -10.85700 1.000 63.89187  ? 34  PHE A O     1 
ATOM   218  C  CB    . PHE A 1 34  ? 41.59500 -14.12500 -7.82000  1.000 65.54207  ? 34  PHE A CB    1 
ATOM   219  C  CG    . PHE A 1 34  ? 42.93700 -14.36700 -8.43100  1.000 63.54972  ? 34  PHE A CG    1 
ATOM   220  C  CD1   . PHE A 1 34  ? 43.65600 -15.51400 -8.14900  1.000 62.45749  ? 34  PHE A CD1   1 
ATOM   221  C  CD2   . PHE A 1 34  ? 43.48900 -13.42600 -9.28300  1.000 68.52664  ? 34  PHE A CD2   1 
ATOM   222  C  CE1   . PHE A 1 34  ? 44.90100 -15.72000 -8.70900  1.000 62.51539  ? 34  PHE A CE1   1 
ATOM   223  C  CE2   . PHE A 1 34  ? 44.72900 -13.62700 -9.85000  1.000 72.02706  ? 34  PHE A CE2   1 
ATOM   224  C  CZ    . PHE A 1 34  ? 45.43700 -14.77700 -9.56100  1.000 70.63478  ? 34  PHE A CZ    1 
ATOM   225  N  N     A SER A 1 35  ? 40.07600 -13.23100 -10.22600 1.000 62.71805  ? 35  SER A N     1 
ATOM   226  C  CA    A SER A 1 35  ? 40.11500 -12.67900 -11.57300 1.000 61.37052  ? 35  SER A CA    1 
ATOM   227  C  C     A SER A 1 35  ? 40.96500 -11.41200 -11.58700 1.000 59.40712  ? 35  SER A C     1 
ATOM   228  O  O     A SER A 1 35  ? 41.03400 -10.67400 -10.59900 1.000 63.25758  ? 35  SER A O     1 
ATOM   229  C  CB    A SER A 1 35  ? 38.70500 -12.38300 -12.10600 1.000 60.87835  ? 35  SER A CB    1 
ATOM   230  O  OG    A SER A 1 35  ? 38.11200 -11.31700 -11.39300 1.000 74.16679  ? 35  SER A OG    1 
ATOM   231  N  N     . CYS A 1 36  ? 41.61700 -11.17800 -12.73100 1.000 56.53836  ? 36  CYS A N     1 
ATOM   232  C  CA    . CYS A 1 36  ? 42.63800 -10.15600 -12.94100 1.000 56.97262  ? 36  CYS A CA    1 
ATOM   233  C  C     . CYS A 1 36  ? 42.49500 -9.47200  -14.29600 1.000 57.07526  ? 36  CYS A C     1 
ATOM   234  O  O     . CYS A 1 36  ? 42.68900 -10.10900 -15.34100 1.000 60.22564  ? 36  CYS A O     1 
ATOM   235  C  CB    . CYS A 1 36  ? 44.03500 -10.75800 -12.83700 1.000 59.76243  ? 36  CYS A CB    1 
ATOM   236  S  SG    . CYS A 1 36  ? 45.33900 -9.52400  -12.90600 1.000 70.14788  ? 36  CYS A SG    1 
ATOM   237  N  N     A PRO A 1 37  ? 42.09600 -8.20400  -14.32300 1.000 54.75130  ? 37  PRO A N     1 
ATOM   238  C  CA    A PRO A 1 37  ? 42.06500 -7.45900  -15.58800 1.000 51.63251  ? 37  PRO A CA    1 
ATOM   239  C  C     A PRO A 1 37  ? 43.46300 -7.31400  -16.17200 1.000 54.17492  ? 37  PRO A C     1 
ATOM   240  O  O     A PRO A 1 37  ? 44.45400 -7.22400  -15.44600 1.000 61.39684  ? 37  PRO A O     1 
ATOM   241  C  CB    A PRO A 1 37  ? 41.48900 -6.10000  -15.18500 1.000 54.51969  ? 37  PRO A CB    1 
ATOM   242  C  CG    A PRO A 1 37  ? 41.82600 -5.97600  -13.73300 1.000 58.78073  ? 37  PRO A CG    1 
ATOM   243  C  CD    A PRO A 1 37  ? 41.75000 -7.36000  -13.17000 1.000 62.48907  ? 37  PRO A CD    1 
ATOM   244  N  N     . ALA A 1 38  ? 43.54200 -7.33100  -17.50200 1.000 51.47986  ? 38  ALA A N     1 
ATOM   245  C  CA    . ALA A 1 38  ? 44.83200 -7.18500  -18.16500 1.000 53.16427  ? 38  ALA A CA    1 
ATOM   246  C  C     . ALA A 1 38  ? 45.43100 -5.82200  -17.83900 1.000 56.67785  ? 38  ALA A C     1 
ATOM   247  O  O     . ALA A 1 38  ? 44.75800 -4.79300  -17.95100 1.000 65.03938  ? 38  ALA A O     1 
ATOM   248  C  CB    . ALA A 1 38  ? 44.66800 -7.34600  -19.67600 1.000 56.34886  ? 38  ALA A CB    1 
ATOM   249  N  N     . TYR A 1 39  ? 46.70200 -5.81500  -17.43400 1.000 53.76171  ? 39  TYR A N     1 
ATOM   250  C  CA    . TYR A 1 39  ? 47.41900 -4.55200  -17.28200 1.000 56.27254  ? 39  TYR A CA    1 
ATOM   251  C  C     . TYR A 1 39  ? 47.70200 -3.91700  -18.63700 1.000 61.14681  ? 39  TYR A C     1 
ATOM   252  O  O     . TYR A 1 39  ? 47.49700 -2.71200  -18.82800 1.000 66.98435  ? 39  TYR A O     1 
ATOM   253  C  CB    . TYR A 1 39  ? 48.71900 -4.78800  -16.51400 1.000 57.69376  ? 39  TYR A CB    1 
ATOM   254  C  CG    . TYR A 1 39  ? 49.57200 -3.55400  -16.33000 1.000 56.30675  ? 39  TYR A CG    1 
ATOM   255  C  CD1   . TYR A 1 39  ? 49.37700 -2.71200  -15.24600 1.000 65.55523  ? 39  TYR A CD1   1 
ATOM   256  C  CD2   . TYR A 1 39  ? 50.58400 -3.24200  -17.22600 1.000 55.56456  ? 39  TYR A CD2   1 
ATOM   257  C  CE1   . TYR A 1 39  ? 50.15400 -1.58900  -15.06500 1.000 64.27086  ? 39  TYR A CE1   1 
ATOM   258  C  CE2   . TYR A 1 39  ? 51.36800 -2.12000  -17.05300 1.000 58.54649  ? 39  TYR A CE2   1 
ATOM   259  C  CZ    . TYR A 1 39  ? 51.14800 -1.29700  -15.96900 1.000 64.31824  ? 39  TYR A CZ    1 
ATOM   260  O  OH    . TYR A 1 39  ? 51.91700 -0.17300  -15.77800 1.000 76.33810  ? 39  TYR A OH    1 
ATOM   261  N  N     . ALA A 1 40  ? 48.17100 -4.72100  -19.58800 1.000 58.87285  ? 40  ALA A N     1 
ATOM   262  C  CA    . ALA A 1 40  ? 48.38000 -4.30600  -20.96600 1.000 58.99918  ? 40  ALA A CA    1 
ATOM   263  C  C     . ALA A 1 40  ? 48.15200 -5.52000  -21.85000 1.000 57.66481  ? 40  ALA A C     1 
ATOM   264  O  O     . ALA A 1 40  ? 48.38800 -6.65200  -21.43100 1.000 57.73587  ? 40  ALA A O     1 
ATOM   265  C  CB    . ALA A 1 40  ? 49.78100 -3.72500  -21.18700 1.000 58.20961  ? 40  ALA A CB    1 
ATOM   266  N  N     . TYR A 1 41  ? 47.66900 -5.28700  -23.06600 1.000 60.24670  ? 41  TYR A N     1 
ATOM   267  C  CA    . TYR A 1 41  ? 47.33000 -6.40600  -23.93100 1.000 52.38260  ? 41  TYR A CA    1 
ATOM   268  C  C     . TYR A 1 41  ? 47.34100 -5.94700  -25.37700 1.000 54.32757  ? 41  TYR A C     1 
ATOM   269  O  O     . TYR A 1 41  ? 47.23800 -4.75400  -25.67100 1.000 57.86483  ? 41  TYR A O     1 
ATOM   270  C  CB    . TYR A 1 41  ? 45.95500 -6.97800  -23.57400 1.000 52.04045  ? 41  TYR A CB    1 
ATOM   271  C  CG    . TYR A 1 41  ? 44.83500 -5.96500  -23.70800 1.000 60.86782  ? 41  TYR A CG    1 
ATOM   272  C  CD1   . TYR A 1 41  ? 44.55000 -5.07600  -22.67900 1.000 64.20507  ? 41  TYR A CD1   1 
ATOM   273  C  CD2   . TYR A 1 41  ? 44.06600 -5.89300  -24.86400 1.000 62.77332  ? 41  TYR A CD2   1 
ATOM   274  C  CE1   . TYR A 1 41  ? 43.53000 -4.14500  -22.79400 1.000 63.11020  ? 41  TYR A CE1   1 
ATOM   275  C  CE2   . TYR A 1 41  ? 43.04400 -4.96200  -24.98900 1.000 68.24766  ? 41  TYR A CE2   1 
ATOM   276  C  CZ    . TYR A 1 41  ? 42.78000 -4.09200  -23.94900 1.000 68.73193  ? 41  TYR A CZ    1 
ATOM   277  O  OH    . TYR A 1 41  ? 41.76700 -3.16400  -24.06100 1.000 76.84606  ? 41  TYR A OH    1 
ATOM   278  N  N     . VAL A 1 42  ? 47.43900 -6.92000  -26.27900 1.000 53.37482  ? 42  VAL A N     1 
ATOM   279  C  CA    . VAL A 1 42  ? 47.43900 -6.63400  -27.70700 1.000 56.59626  ? 42  VAL A CA    1 
ATOM   280  C  C     . VAL A 1 42  ? 46.89300 -7.85000  -28.44200 1.000 56.78576  ? 42  VAL A C     1 
ATOM   281  O  O     . VAL A 1 42  ? 47.23300 -8.99800  -28.12700 1.000 62.77595  ? 42  VAL A O     1 
ATOM   282  C  CB    . VAL A 1 42  ? 48.85600 -6.25300  -28.19300 1.000 53.74855  ? 42  VAL A CB    1 
ATOM   283  C  CG1   . VAL A 1 42  ? 49.85300 -7.38100  -27.93800 1.000 46.33450  ? 42  VAL A CG1   1 
ATOM   284  C  CG2   . VAL A 1 42  ? 48.82700 -5.88700  -29.64400 1.000 65.56312  ? 42  VAL A CG2   1 
ATOM   285  N  N     . LEU A 1 43  ? 46.03300 -7.58000  -29.42500 1.000 57.80167  ? 43  LEU A N     1 
ATOM   286  C  CA    . LEU A 1 43  ? 45.46800 -8.60600  -30.29200 1.000 65.52891  ? 43  LEU A CA    1 
ATOM   287  C  C     . LEU A 1 43  ? 46.44600 -8.98000  -31.39900 1.000 68.11606  ? 43  LEU A C     1 
ATOM   288  O  O     . LEU A 1 43  ? 47.00800 -8.10100  -32.06100 1.000 70.85586  ? 43  LEU A O     1 
ATOM   289  C  CB    . LEU A 1 43  ? 44.14800 -8.11800  -30.88900 1.000 65.73946  ? 43  LEU A CB    1 
ATOM   290  C  CG    . LEU A 1 43  ? 43.36400 -9.12300  -31.73000 1.000 61.35472  ? 43  LEU A CG    1 
ATOM   291  C  CD1   . LEU A 1 43  ? 42.73800 -10.17500 -30.83500 1.000 60.58358  ? 43  LEU A CD1   1 
ATOM   292  C  CD2   . LEU A 1 43  ? 42.29600 -8.41700  -32.53500 1.000 80.69125  ? 43  LEU A CD2   1 
ATOM   293  N  N     . THR A 1 44  ? 46.63300 -10.28000 -31.61500 1.000 64.04978  ? 44  THR A N     1 
ATOM   294  C  CA    . THR A 1 44  ? 47.56500 -10.72600 -32.63900 1.000 62.07586  ? 44  THR A CA    1 
ATOM   295  C  C     . THR A 1 44  ? 47.03700 -10.34900 -34.02200 1.000 73.38775  ? 44  THR A C     1 
ATOM   296  O  O     . THR A 1 44  ? 45.82700 -10.26000 -34.24700 1.000 84.04429  ? 44  THR A O     1 
ATOM   297  C  CB    . THR A 1 44  ? 47.80800 -12.23100 -32.53100 1.000 61.50737  ? 44  THR A CB    1 
ATOM   298  O  OG1   . THR A 1 44  ? 49.00700 -12.56700 -33.23800 1.000 74.09573  ? 44  THR A OG1   1 
ATOM   299  C  CG2   . THR A 1 44  ? 46.64800 -13.01300 -33.11100 1.000 68.00552  ? 44  THR A CG2   1 
ATOM   300  N  N     . VAL A 1 45  ? 47.97000 -10.08600 -34.94200 1.000 74.00624  ? 45  VAL A N     1 
ATOM   301  C  CA    . VAL A 1 45  ? 47.62500 -9.50600  -36.24100 1.000 81.22816  ? 45  VAL A CA    1 
ATOM   302  C  C     . VAL A 1 45  ? 46.63200 -10.37300 -37.00400 1.000 89.29492  ? 45  VAL A C     1 
ATOM   303  O  O     . VAL A 1 45  ? 45.67700 -9.86500  -37.60700 1.000 98.05649  ? 45  VAL A O     1 
ATOM   304  C  CB    . VAL A 1 45  ? 48.90500 -9.26600  -37.06200 1.000 76.23019  ? 45  VAL A CB    1 
ATOM   305  C  CG1   . VAL A 1 45  ? 48.56800 -8.96400  -38.51600 1.000 76.32757  ? 45  VAL A CG1   1 
ATOM   306  C  CG2   . VAL A 1 45  ? 49.69700 -8.12400  -36.45400 1.000 79.80957  ? 45  VAL A CG2   1 
ATOM   307  N  N     . ASN A 1 46  ? 46.83200 -11.68900 -36.98600 1.000 87.18677  ? 46  ASN A N     1 
ATOM   308  C  CA    . ASN A 1 46  ? 46.01600 -12.59600 -37.78400 1.000 91.05565  ? 46  ASN A CA    1 
ATOM   309  C  C     . ASN A 1 46  ? 44.55600 -12.66800 -37.34300 1.000 90.27925  ? 46  ASN A C     1 
ATOM   310  O  O     . ASN A 1 46  ? 43.73800 -13.23500 -38.07700 1.000 93.94284  ? 46  ASN A O     1 
ATOM   311  C  CB    . ASN A 1 46  ? 46.65700 -13.97700 -37.79100 1.000 94.42185  ? 46  ASN A CB    1 
ATOM   312  C  CG    . ASN A 1 46  ? 47.89300 -14.02700 -38.67200 1.000 102.82285 ? 46  ASN A CG    1 
ATOM   313  O  OD1   . ASN A 1 46  ? 48.07700 -13.18600 -39.55500 1.000 95.90360  ? 46  ASN A OD1   1 
ATOM   314  N  ND2   . ASN A 1 46  ? 48.72600 -15.03500 -38.46000 1.000 102.56230 ? 46  ASN A ND2   1 
ATOM   315  N  N     . GLU A 1 47  ? 44.21000 -12.15300 -36.16400 1.000 101.88064 ? 47  GLU A N     1 
ATOM   316  C  CA    . GLU A 1 47  ? 42.84300 -12.19800 -35.65700 1.000 102.47018 ? 47  GLU A CA    1 
ATOM   317  C  C     . GLU A 1 47  ? 42.12000 -10.86200 -35.78300 1.000 104.02563 ? 47  GLU A C     1 
ATOM   318  O  O     . GLU A 1 47  ? 41.01000 -10.71600 -35.25800 1.000 104.59938 ? 47  GLU A O     1 
ATOM   319  C  CB    . GLU A 1 47  ? 42.82300 -12.68000 -34.20500 1.000 100.89894 ? 47  GLU A CB    1 
ATOM   320  C  CG    . GLU A 1 47  ? 43.32500 -14.10300 -34.04300 1.000 99.71985  ? 47  GLU A CG    1 
ATOM   321  C  CD    . GLU A 1 47  ? 42.40900 -15.11900 -34.71200 1.000 106.31538 ? 47  GLU A CD    1 
ATOM   322  O  OE1   . GLU A 1 47  ? 41.21400 -14.81400 -34.91300 1.000 109.81843 ? 47  GLU A OE1   1 
ATOM   323  O  OE2   . GLU A 1 47  ? 42.89000 -16.22500 -35.04600 1.000 107.99190 ? 47  GLU A OE2   1 
ATOM   324  N  N     . ARG A 1 48  ? 42.72800 -9.88500  -36.45300 1.000 92.38476  ? 48  ARG A N     1 
ATOM   325  C  CA    . ARG A 1 48  ? 42.04500 -8.63000  -36.72400 1.000 88.11846  ? 48  ARG A CA    1 
ATOM   326  C  C     . ARG A 1 48  ? 40.86500 -8.90500  -37.64400 1.000 92.70059  ? 48  ARG A C     1 
ATOM   327  O  O     . ARG A 1 48  ? 40.95900 -9.71600  -38.57000 1.000 97.37220  ? 48  ARG A O     1 
ATOM   328  C  CB    . ARG A 1 48  ? 43.01000 -7.65800  -37.40300 1.000 92.07157  ? 48  ARG A CB    1 
ATOM   329  C  CG    . ARG A 1 48  ? 44.16300 -7.19300  -36.53500 1.000 93.01642  ? 48  ARG A CG    1 
ATOM   330  C  CD    . ARG A 1 48  ? 45.21300 -6.51400  -37.39600 1.000 89.62654  ? 48  ARG A CD    1 
ATOM   331  N  NE    . ARG A 1 48  ? 46.21100 -5.78900  -36.62100 1.000 80.17803  ? 48  ARG A NE    1 
ATOM   332  C  CZ    . ARG A 1 48  ? 47.25100 -5.16500  -37.15500 1.000 86.07085  ? 48  ARG A CZ    1 
ATOM   333  N  NH1   . ARG A 1 48  ? 47.46100 -5.16800  -38.46100 1.000 94.79558  ? 48  ARG A NH1   1 
ATOM   334  N  NH2   . ARG A 1 48  ? 48.10800 -4.53300  -36.35800 1.000 82.09669  ? 48  ARG A NH2   1 
ATOM   335  N  N     . GLY A 1 49  ? 39.74400 -8.23500  -37.39200 1.000 95.68779  ? 49  GLY A N     1 
ATOM   336  C  CA    . GLY A 1 49  ? 38.54100 -8.48600  -38.15100 1.000 93.16380  ? 49  GLY A CA    1 
ATOM   337  C  C     . GLY A 1 49  ? 37.62700 -9.53900  -37.55300 1.000 89.60548  ? 49  GLY A C     1 
ATOM   338  O  O     . GLY A 1 49  ? 36.41100 -9.48200  -37.76300 1.000 85.53920  ? 49  GLY A O     1 
ATOM   339  N  N     . ASN A 1 50  ? 38.18600 -10.50100 -36.81400 1.000 92.92430  ? 50  ASN A N     1 
ATOM   340  C  CA    . ASN A 1 50  ? 37.38100 -11.50200 -36.12300 1.000 92.09262  ? 50  ASN A CA    1 
ATOM   341  C  C     . ASN A 1 50  ? 37.00900 -11.08800 -34.70500 1.000 89.45546  ? 50  ASN A C     1 
ATOM   342  O  O     . ASN A 1 50  ? 35.92000 -11.43400 -34.23300 1.000 94.14813  ? 50  ASN A O     1 
ATOM   343  C  CB    . ASN A 1 50  ? 38.14200 -12.83600 -36.05100 1.000 94.68240  ? 50  ASN A CB    1 
ATOM   344  C  CG    . ASN A 1 50  ? 38.55700 -13.36400 -37.41700 1.000 98.88291  ? 50  ASN A CG    1 
ATOM   345  O  OD1   . ASN A 1 50  ? 37.85600 -13.17600 -38.41300 1.000 104.44410 ? 50  ASN A OD1   1 
ATOM   346  N  ND2   . ASN A 1 50  ? 39.71400 -14.02200 -37.46900 1.000 93.67439  ? 50  ASN A ND2   1 
ATOM   347  N  N     . HIS A 1 51  ? 37.88000 -10.34500 -34.02900 1.000 81.73348  ? 51  HIS A N     1 
ATOM   348  C  CA    . HIS A 1 51  ? 37.71400 -9.95700  -32.63500 1.000 84.22326  ? 51  HIS A CA    1 
ATOM   349  C  C     . HIS A 1 51  ? 37.78500 -8.44400  -32.48300 1.000 84.05481  ? 51  HIS A C     1 
ATOM   350  O  O     . HIS A 1 51  ? 38.46300 -7.75600  -33.25300 1.000 86.67618  ? 51  HIS A O     1 
ATOM   351  C  CB    . HIS A 1 51  ? 38.74800 -10.62600 -31.71300 1.000 77.42770  ? 51  HIS A CB    1 
ATOM   352  C  CG    . HIS A 1 51  ? 38.63400 -12.11900 -31.65600 1.000 84.53119  ? 51  HIS A CG    1 
ATOM   353  N  ND1   . HIS A 1 51  ? 39.01500 -12.93800 -32.69700 1.000 92.61637  ? 51  HIS A ND1   1 
ATOM   354  C  CD2   . HIS A 1 51  ? 38.17000 -12.94000 -30.68300 1.000 80.56229  ? 51  HIS A CD2   1 
ATOM   355  C  CE1   . HIS A 1 51  ? 38.79300 -14.19900 -32.36800 1.000 88.16847  ? 51  HIS A CE1   1 
ATOM   356  N  NE2   . HIS A 1 51  ? 38.28300 -14.22800 -31.14900 1.000 82.22302  ? 51  HIS A NE2   1 
ATOM   357  N  N     . CYS A 1 52  ? 37.06300 -7.92900  -31.49100 1.000 81.70716  ? 52  CYS A N     1 
ATOM   358  C  CA    . CYS A 1 52  ? 37.16200 -6.51300  -31.17700 1.000 81.13604  ? 52  CYS A CA    1 
ATOM   359  C  C     . CYS A 1 52  ? 38.51400 -6.23400  -30.53900 1.000 79.87273  ? 52  CYS A C     1 
ATOM   360  O  O     . CYS A 1 52  ? 38.96800 -6.97200  -29.66100 1.000 83.50212  ? 52  CYS A O     1 
ATOM   361  C  CB    . CYS A 1 52  ? 36.04000 -6.09600  -30.23100 1.000 83.64161  ? 52  CYS A CB    1 
ATOM   362  S  SG    . CYS A 1 52  ? 36.24900 -4.43500  -29.55300 1.000 84.56540  ? 52  CYS A SG    1 
ATOM   363  N  N     . GLU A 1 53  ? 39.16700 -5.17100  -31.00600 1.000 84.66541  ? 53  GLU A N     1 
ATOM   364  C  CA    . GLU A 1 53  ? 40.50400 -4.84300  -30.52700 1.000 77.54351  ? 53  GLU A CA    1 
ATOM   365  C  C     . GLU A 1 53  ? 40.51700 -4.55200  -29.02800 1.000 78.82787  ? 53  GLU A C     1 
ATOM   366  O  O     . GLU A 1 53  ? 41.46400 -4.92400  -28.32600 1.000 78.34887  ? 53  GLU A O     1 
ATOM   367  C  CB    . GLU A 1 53  ? 41.02900 -3.65600  -31.32700 1.000 83.10996  ? 53  GLU A CB    1 
ATOM   368  C  CG    . GLU A 1 53  ? 41.17500 -3.99900  -32.80700 1.000 90.05817  ? 53  GLU A CG    1 
ATOM   369  C  CD    . GLU A 1 53  ? 42.49400 -4.63200  -33.20700 1.000 95.31143  ? 53  GLU A CD    1 
ATOM   370  O  OE1   . GLU A 1 53  ? 43.49500 -4.50700  -32.46500 1.000 96.35892  ? 53  GLU A OE1   1 
ATOM   371  O  OE2   . GLU A 1 53  ? 42.51900 -5.27600  -34.27600 1.000 101.83063 ? 53  GLU A OE2   1 
ATOM   372  N  N     . TYR A 1 54  ? 39.47800 -3.88300  -28.51800 1.000 83.68898  ? 54  TYR A N     1 
ATOM   373  C  CA    . TYR A 1 54  ? 39.47100 -3.43900  -27.12400 1.000 84.37591  ? 54  TYR A CA    1 
ATOM   374  C  C     . TYR A 1 54  ? 39.14500 -4.56600  -26.15200 1.000 75.99595  ? 54  TYR A C     1 
ATOM   375  O  O     . TYR A 1 54  ? 39.91500 -4.85100  -25.22900 1.000 73.21404  ? 54  TYR A O     1 
ATOM   376  C  CB    . TYR A 1 54  ? 38.47500 -2.29100  -26.93200 1.000 85.98136  ? 54  TYR A CB    1 
ATOM   377  C  CG    . TYR A 1 54  ? 38.45600 -1.77700  -25.50700 1.000 88.68958  ? 54  TYR A CG    1 
ATOM   378  C  CD1   . TYR A 1 54  ? 39.56700 -1.16300  -24.94100 1.000 91.35306  ? 54  TYR A CD1   1 
ATOM   379  C  CD2   . TYR A 1 54  ? 37.32700 -1.94700  -24.71500 1.000 91.25041  ? 54  TYR A CD2   1 
ATOM   380  C  CE1   . TYR A 1 54  ? 39.54400 -0.71500  -23.62500 1.000 89.35808  ? 54  TYR A CE1   1 
ATOM   381  C  CE2   . TYR A 1 54  ? 37.29300 -1.50100  -23.40700 1.000 92.88219  ? 54  TYR A CE2   1 
ATOM   382  C  CZ    . TYR A 1 54  ? 38.40100 -0.88600  -22.86600 1.000 93.23486  ? 54  TYR A CZ    1 
ATOM   383  O  OH    . TYR A 1 54  ? 38.36300 -0.44400  -21.56300 1.000 97.78541  ? 54  TYR A OH    1 
ATOM   384  N  N     . CYS A 1 55  ? 37.99900 -5.21100  -26.34900 1.000 78.94894  ? 55  CYS A N     1 
ATOM   385  C  CA    . CYS A 1 55  ? 37.43500 -6.14600  -25.38900 1.000 77.99619  ? 55  CYS A CA    1 
ATOM   386  C  C     . CYS A 1 55  ? 37.53200 -7.60200  -25.82400 1.000 76.16966  ? 55  CYS A C     1 
ATOM   387  O  O     . CYS A 1 55  ? 37.10300 -8.48500  -25.07300 1.000 73.45354  ? 55  CYS A O     1 
ATOM   388  C  CB    . CYS A 1 55  ? 35.97700 -5.76000  -25.10800 1.000 80.81495  ? 55  CYS A CB    1 
ATOM   389  S  SG    . CYS A 1 55  ? 34.84200 -6.14000  -26.45700 1.000 74.60895  ? 55  CYS A SG    1 
ATOM   390  N  N     . PHE A 1 56  ? 38.05600 -7.87200  -27.02000 1.000 72.63766  ? 56  PHE A N     1 
ATOM   391  C  CA    . PHE A 1 56  ? 38.32900 -9.20900  -27.54900 1.000 71.85335  ? 56  PHE A CA    1 
ATOM   392  C  C     . PHE A 1 56  ? 37.06800 -9.99800  -27.87500 1.000 80.44912  ? 56  PHE A C     1 
ATOM   393  O  O     . PHE A 1 56  ? 37.15400 -11.20800 -28.12800 1.000 80.76495  ? 56  PHE A O     1 
ATOM   394  C  CB    . PHE A 1 56  ? 39.22900 -10.02900 -26.61400 1.000 69.53202  ? 56  PHE A CB    1 
ATOM   395  C  CG    . PHE A 1 56  ? 40.69900 -9.75400  -26.79500 1.000 68.15291  ? 56  PHE A CG    1 
ATOM   396  C  CD1   . PHE A 1 56  ? 41.14900 -8.47900  -27.09900 1.000 73.53776  ? 56  PHE A CD1   1 
ATOM   397  C  CD2   . PHE A 1 56  ? 41.63000 -10.77400 -26.67300 1.000 62.62067  ? 56  PHE A CD2   1 
ATOM   398  C  CE1   . PHE A 1 56  ? 42.49600 -8.22400  -27.26700 1.000 69.81363  ? 56  PHE A CE1   1 
ATOM   399  C  CE2   . PHE A 1 56  ? 42.97900 -10.52400 -26.84200 1.000 60.26775  ? 56  PHE A CE2   1 
ATOM   400  C  CZ    . PHE A 1 56  ? 43.41100 -9.24900  -27.13900 1.000 62.38906  ? 56  PHE A CZ    1 
ATOM   401  N  N     . THR A 1 57  ? 35.90000 -9.35700  -27.87900 1.000 86.05242  ? 57  THR A N     1 
ATOM   402  C  CA    . THR A 1 57  ? 34.67400 -10.06800 -28.21000 1.000 83.04943  ? 57  THR A CA    1 
ATOM   403  C  C     . THR A 1 57  ? 34.72800 -10.46200 -29.67800 1.000 80.39911  ? 57  THR A C     1 
ATOM   404  O  O     . THR A 1 57  ? 35.04300 -9.63300  -30.53700 1.000 81.79928  ? 57  THR A O     1 
ATOM   405  C  CB    . THR A 1 57  ? 33.45400 -9.18600  -27.95200 1.000 80.20962  ? 57  THR A CB    1 
ATOM   406  O  OG1   . THR A 1 57  ? 33.49100 -8.68100  -26.61500 1.000 85.56552  ? 57  THR A OG1   1 
ATOM   407  C  CG2   . THR A 1 57  ? 32.17000 -9.97300  -28.15900 1.000 83.53370  ? 57  THR A CG2   1 
ATOM   408  N  N     . ARG A 1 58  ? 34.39500 -11.71300 -29.98000 1.000 82.73097  ? 58  ARG A N     1 
ATOM   409  C  CA    . ARG A 1 58  ? 34.34700 -12.15300 -31.36400 1.000 84.47329  ? 58  ARG A CA    1 
ATOM   410  C  C     . ARG A 1 58  ? 32.93500 -11.95700 -31.89800 1.000 89.95289  ? 58  ARG A C     1 
ATOM   411  O  O     . ARG A 1 58  ? 31.97500 -12.51100 -31.35000 1.000 89.83446  ? 58  ARG A O     1 
ATOM   412  C  CB    . ARG A 1 58  ? 34.81300 -13.61300 -31.44600 1.000 83.44948  ? 58  ARG A CB    1 
ATOM   413  C  CG    . ARG A 1 58  ? 34.92500 -14.20800 -32.84400 1.000 89.81603  ? 58  ARG A CG    1 
ATOM   414  C  CD    . ARG A 1 58  ? 35.34400 -15.70100 -32.85800 1.000 94.64819  ? 58  ARG A CD    1 
ATOM   415  N  NE    . ARG A 1 58  ? 34.53100 -16.64300 -32.09300 1.000 105.30736 ? 58  ARG A NE    1 
ATOM   416  C  CZ    . ARG A 1 58  ? 34.99300 -17.35700 -31.07200 1.000 104.67308 ? 58  ARG A CZ    1 
ATOM   417  N  NH1   . ARG A 1 58  ? 36.25500 -17.26600 -30.68000 1.000 90.23450  ? 58  ARG A NH1   1 
ATOM   418  N  NH2   . ARG A 1 58  ? 34.17900 -18.20700 -30.45100 1.000 107.78398 ? 58  ARG A NH2   1 
ATOM   419  N  N     . LYS A 1 59  ? 32.81700 -11.17200 -32.97100 1.000 97.56170  ? 59  LYS A N     1 
ATOM   420  C  CA    . LYS A 1 59  ? 31.56300 -10.99700 -33.69300 1.000 102.98603 ? 59  LYS A CA    1 
ATOM   421  C  C     . LYS A 1 59  ? 31.85300 -10.36900 -35.05100 1.000 106.88387 ? 59  LYS A C     1 
ATOM   422  O  O     . LYS A 1 59  ? 32.89400 -9.74100  -35.25900 1.000 106.12062 ? 59  LYS A O     1 
ATOM   423  C  CB    . LYS A 1 59  ? 30.57800 -10.12300 -32.90900 1.000 102.08592 ? 59  LYS A CB    1 
ATOM   424  C  CG    . LYS A 1 59  ? 31.07100 -8.70200  -32.68300 1.000 103.23080 ? 59  LYS A CG    1 
ATOM   425  C  CD    . LYS A 1 59  ? 30.05400 -7.88200  -31.91300 1.000 100.36993 ? 59  LYS A CD    1 
ATOM   426  C  CE    . LYS A 1 59  ? 29.98600 -8.32900  -30.46600 1.000 103.73086 ? 59  LYS A CE    1 
ATOM   427  N  NZ    . LYS A 1 59  ? 29.14200 -7.43000  -29.63300 1.000 106.44171 ? 59  LYS A NZ    1 
ATOM   428  N  N     . GLU A 1 60  ? 30.92500 -10.58300 -35.97600 1.000 113.66889 ? 60  GLU A N     1 
ATOM   429  C  CA    . GLU A 1 60  ? 30.94200 -10.02800 -37.32700 1.000 112.57402 ? 60  GLU A CA    1 
ATOM   430  C  C     . GLU A 1 60  ? 30.35900 -8.61700  -37.40100 1.000 112.92143 ? 60  GLU A C     1 
ATOM   431  O  O     . GLU A 1 60  ? 29.49300 -8.23100  -36.60900 1.000 108.32615 ? 60  GLU A O     1 
ATOM   432  C  CB    . GLU A 1 60  ? 30.27500 -10.98600 -38.29900 1.000 106.72332 ? 60  GLU A CB    1 
ATOM   433  C  CG    . GLU A 1 60  ? 31.03600 -12.30600 -38.27700 1.000 111.78182 ? 60  GLU A CG    1 
ATOM   434  C  CD    . GLU A 1 60  ? 30.78800 -13.17700 -39.47500 1.000 115.36120 ? 60  GLU A CD    1 
ATOM   435  O  OE1   . GLU A 1 60  ? 29.87200 -12.86100 -40.25800 1.000 113.36622 ? 60  GLU A OE1   1 
ATOM   436  O  OE2   . GLU A 1 60  ? 31.48700 -14.20500 -39.60700 1.000 127.69952 ? 60  GLU A OE2   1 
ATOM   437  N  N     . GLY A 1 61  ? 30.86800 -7.83900  -38.35300 1.000 120.65657 ? 61  GLY A N     1 
ATOM   438  C  CA    . GLY A 1 61  ? 30.38300 -6.49000  -38.58800 1.000 121.80408 ? 61  GLY A CA    1 
ATOM   439  C  C     . GLY A 1 61  ? 30.92200 -5.52900  -37.55700 1.000 119.30378 ? 61  GLY A C     1 
ATOM   440  O  O     . GLY A 1 61  ? 30.19500 -4.73200  -36.95500 1.000 120.21705 ? 61  GLY A O     1 
ATOM   441  N  N     . LEU A 1 62  ? 32.22200 -5.66300  -37.32900 1.000 108.60513 ? 62  LEU A N     1 
ATOM   442  C  CA    . LEU A 1 62  ? 32.95300 -4.77800  -36.44700 1.000 117.34302 ? 62  LEU A CA    1 
ATOM   443  C  C     . LEU A 1 62  ? 33.24200 -3.46200  -37.16100 1.000 130.41300 ? 62  LEU A C     1 
ATOM   444  O  O     . LEU A 1 62  ? 33.51300 -3.44300  -38.37000 1.000 117.22195 ? 62  LEU A O     1 
ATOM   445  C  CB    . LEU A 1 62  ? 34.26200 -5.44800  -36.04300 1.000 107.66291 ? 62  LEU A CB    1 
ATOM   446  C  CG    . LEU A 1 62  ? 34.08900 -6.70100  -35.18800 1.000 95.62462  ? 62  LEU A CG    1 
ATOM   447  C  CD1   . LEU A 1 62  ? 35.39100 -7.48400  -35.12100 1.000 95.94835  ? 62  LEU A CD1   1 
ATOM   448  C  CD2   . LEU A 1 62  ? 33.59000 -6.34100  -33.80400 1.000 96.14047  ? 62  LEU A CD2   1 
ATOM   449  N  N     . SER A 1 63  ? 33.17700 -2.35700  -36.41700 1.000 151.21287 ? 63  SER A N     1 
ATOM   450  C  CA    . SER A 1 63  ? 33.50600 -1.06600  -37.00000 1.000 149.87586 ? 63  SER A CA    1 
ATOM   451  C  C     . SER A 1 63  ? 34.99800 -1.00100  -37.29900 1.000 146.48335 ? 63  SER A C     1 
ATOM   452  O  O     . SER A 1 63  ? 35.83100 -1.44000  -36.50000 1.000 141.31168 ? 63  SER A O     1 
ATOM   453  C  CB    . SER A 1 63  ? 33.07600 0.07600   -36.08000 1.000 151.48395 ? 63  SER A CB    1 
ATOM   454  O  OG    . SER A 1 63  ? 31.67200 0.13500   -35.92700 1.000 154.31061 ? 63  SER A OG    1 
ATOM   455  N  N     . LYS A 1 64  ? 35.33500 -0.41900  -38.44500 1.000 124.09909 ? 64  LYS A N     1 
ATOM   456  C  CA    . LYS A 1 64  ? 36.70900 -0.37700  -38.91800 1.000 112.66877 ? 64  LYS A CA    1 
ATOM   457  C  C     . LYS A 1 64  ? 37.28600 1.00100   -38.63300 1.000 108.36562 ? 64  LYS A C     1 
ATOM   458  O  O     . LYS A 1 64  ? 36.57500 2.00200   -38.85100 1.000 115.69545 ? 64  LYS A O     1 
ATOM   459  C  CB    . LYS A 1 64  ? 36.74700 -0.68600  -40.41700 1.000 106.47592 ? 64  LYS A CB    1 
ATOM   460  C  CG    . LYS A 1 64  ? 38.10300 -1.09900  -40.97000 1.000 104.77309 ? 64  LYS A CG    1 
ATOM   461  C  CD    . LYS A 1 64  ? 38.16600 -1.00600  -42.47800 1.000 104.80204 ? 64  LYS A CD    1 
ATOM   462  C  CE    . LYS A 1 64  ? 38.13500 -2.35600  -43.16100 1.000 102.66231 ? 64  LYS A CE    1 
ATOM   463  N  NZ    . LYS A 1 64  ? 39.49700 -2.90700  -43.34900 1.000 94.84821  ? 64  LYS A NZ    1 
ATOM   464  N  N     . CYS A 1 65  ? 38.52700 1.02900   -38.15700 1.000 101.21740 ? 65  CYS A N     1 
ATOM   465  C  CA    . CYS A 1 65  ? 39.16100 2.30700   -37.89200 1.000 105.55476 ? 65  CYS A CA    1 
ATOM   466  C  C     . CYS A 1 65  ? 39.39100 3.00300   -39.22300 1.000 107.78398 ? 65  CYS A C     1 
ATOM   467  O  O     . CYS A 1 65  ? 40.18400 2.54000   -40.04900 1.000 108.34720 ? 65  CYS A O     1 
ATOM   468  C  CB    . CYS A 1 65  ? 40.46400 2.11800   -37.11900 1.000 101.77273 ? 65  CYS A CB    1 
ATOM   469  S  SG    . CYS A 1 65  ? 41.31500 3.66900   -36.73700 1.000 98.63814  ? 65  CYS A SG    1 
ATOM   470  N  N     . GLY A 1 66  ? 38.69900 4.12100   -39.41400 1.000 101.88590 ? 66  GLY A N     1 
ATOM   471  C  CA    . GLY A 1 66  ? 38.75100 4.84000   -40.67100 1.000 103.12815 ? 66  GLY A CA    1 
ATOM   472  C  C     . GLY A 1 66  ? 40.14600 5.31300   -40.99400 1.000 107.31550 ? 66  GLY A C     1 
ATOM   473  O  O     . GLY A 1 66  ? 40.51200 5.46000   -42.16500 1.000 112.76352 ? 66  GLY A O     1 
ATOM   474  N  N     . ARG A 1 67  ? 40.93700 5.56000   -39.95400 1.000 110.53431 ? 67  ARG A N     1 
ATOM   475  C  CA    . ARG A 1 67  ? 42.27300 6.11300   -40.10800 1.000 107.48657 ? 67  ARG A CA    1 
ATOM   476  C  C     . ARG A 1 67  ? 43.20900 5.10700   -40.77400 1.000 103.63611 ? 67  ARG A C     1 
ATOM   477  O  O     . ARG A 1 67  ? 43.71300 5.34800   -41.87700 1.000 104.63097 ? 67  ARG A O     1 
ATOM   478  C  CB    . ARG A 1 67  ? 42.76100 6.48700   -38.70200 1.000 111.88447 ? 67  ARG A CB    1 
ATOM   479  C  CG    . ARG A 1 67  ? 41.82400 7.50700   -38.03900 1.000 119.48011 ? 67  ARG A CG    1 
ATOM   480  C  CD    . ARG A 1 67  ? 42.23400 8.01700   -36.65500 1.000 115.55596 ? 67  ARG A CD    1 
ATOM   481  N  NE    . ARG A 1 67  ? 41.32200 9.08300   -36.24000 1.000 123.60166 ? 67  ARG A NE    1 
ATOM   482  C  CZ    . ARG A 1 67  ? 41.57900 10.02100  -35.33900 1.000 116.67715 ? 67  ARG A CZ    1 
ATOM   483  N  NH1   . ARG A 1 67  ? 42.73900 10.07600  -34.70700 1.000 113.43202 ? 67  ARG A NH1   1 
ATOM   484  N  NH2   . ARG A 1 67  ? 40.63400 10.91000  -35.04200 1.000 112.41348 ? 67  ARG A NH2   1 
ATOM   485  N  N     . CYS A 1 68  ? 43.45700 3.97300   -40.11000 1.000 108.52617 ? 68  CYS A N     1 
ATOM   486  C  CA    . CYS A 1 68  ? 44.40300 2.95100   -40.55300 1.000 103.63348 ? 68  CYS A CA    1 
ATOM   487  C  C     . CYS A 1 68  ? 43.75500 1.77700   -41.29300 1.000 101.40953 ? 68  CYS A C     1 
ATOM   488  O  O     . CYS A 1 68  ? 44.45600 1.06400   -42.02200 1.000 97.51959  ? 68  CYS A O     1 
ATOM   489  C  CB    . CYS A 1 68  ? 45.21300 2.41500   -39.36700 1.000 96.56421  ? 68  CYS A CB    1 
ATOM   490  S  SG    . CYS A 1 68  ? 44.24700 1.55000   -38.11800 1.000 82.63359  ? 68  CYS A SG    1 
ATOM   491  N  N     . LYS A 1 69  ? 42.44300 1.56700   -41.11700 1.000 108.91569 ? 69  LYS A N     1 
ATOM   492  C  CA    . LYS A 1 69  ? 41.66200 0.47400   -41.73000 1.000 107.01283 ? 69  LYS A CA    1 
ATOM   493  C  C     . LYS A 1 69  ? 42.16300 -0.92700  -41.35000 1.000 96.45367  ? 69  LYS A C     1 
ATOM   494  O  O     . LYS A 1 69  ? 41.99400 -1.88800  -42.10500 1.000 91.53992  ? 69  LYS A O     1 
ATOM   495  C  CB    . LYS A 1 69  ? 41.58500 0.62100   -43.25700 1.000 98.71447  ? 69  LYS A CB    1 
ATOM   496  C  CG    . LYS A 1 69  ? 41.06400 1.98000   -43.72900 1.000 96.35892  ? 69  LYS A CG    1 
ATOM   497  C  CD    . LYS A 1 69  ? 40.92900 2.04600   -45.25000 1.000 99.07767  ? 69  LYS A CD    1 
ATOM   498  C  CE    . LYS A 1 69  ? 40.52800 3.44000   -45.73300 1.000 99.51983  ? 69  LYS A CE    1 
ATOM   499  N  NZ    . LYS A 1 69  ? 40.21500 3.46000   -47.19700 1.000 101.58850 ? 69  LYS A NZ    1 
ATOM   500  N  N     . GLN A 1 70  ? 42.78400 -1.05900  -40.17300 1.000 97.76699  ? 70  GLN A N     1 
ATOM   501  C  CA    . GLN A 1 70  ? 43.33400 -2.32800  -39.69600 1.000 96.28260  ? 70  GLN A CA    1 
ATOM   502  C  C     . GLN A 1 70  ? 43.07600 -2.55900  -38.20800 1.000 96.54842  ? 70  GLN A C     1 
ATOM   503  O  O     . GLN A 1 70  ? 43.89000 -3.19800  -37.52900 1.000 95.58514  ? 70  GLN A O     1 
ATOM   504  C  CB    . GLN A 1 70  ? 44.81600 -2.51000  -40.01300 1.000 96.72476  ? 70  GLN A CB    1 
ATOM   505  C  CG    . GLN A 1 70  ? 45.08200 -2.89200  -41.45800 1.000 99.87250  ? 70  GLN A CG    1 
ATOM   506  C  CD    . GLN A 1 70  ? 46.55800 -2.96500  -41.77200 1.000 102.85444 ? 70  GLN A CD    1 
ATOM   507  O  OE1   . GLN A 1 70  ? 47.21100 -3.97500  -41.48700 1.000 104.06248 ? 70  GLN A OE1   1 
ATOM   508  N  NE2   . GLN A 1 70  ? 47.08400 -1.92600  -42.40900 1.000 94.95086  ? 70  GLN A NE2   1 
ATOM   509  N  N     . ALA A 1 71  ? 41.94800 -2.07400  -37.69100 1.000 92.63742  ? 71  ALA A N     1 
ATOM   510  C  CA    . ALA A 1 71  ? 41.59300 -2.27600  -36.28900 1.000 91.02144  ? 71  ALA A CA    1 
ATOM   511  C  C     . ALA A 1 71  ? 40.07900 -2.21000  -36.19400 1.000 96.42472  ? 71  ALA A C     1 
ATOM   512  O  O     . ALA A 1 71  ? 39.46300 -1.22800  -36.62000 1.000 101.25425 ? 71  ALA A O     1 
ATOM   513  C  CB    . ALA A 1 71  ? 42.24000 -1.21900  -35.39200 1.000 92.92430  ? 71  ALA A CB    1 
ATOM   514  N  N     . PHE A 1 72  ? 39.48400 -3.26500  -35.64000 1.000 96.51684  ? 72  PHE A N     1 
ATOM   515  C  CA    . PHE A 1 72  ? 38.04400 -3.42900  -35.68800 1.000 99.06714  ? 72  PHE A CA    1 
ATOM   516  C  C     . PHE A 1 72  ? 37.46600 -3.37200  -34.27900 1.000 98.80395  ? 72  PHE A C     1 
ATOM   517  O  O     . PHE A 1 72  ? 38.10300 -3.80100  -33.31300 1.000 96.41946  ? 72  PHE A O     1 
ATOM   518  C  CB    . PHE A 1 72  ? 37.71700 -4.77600  -36.34800 1.000 101.16476 ? 72  PHE A CB    1 
ATOM   519  C  CG    . PHE A 1 72  ? 38.20600 -4.88700  -37.77400 1.000 93.76387  ? 72  PHE A CG    1 
ATOM   520  C  CD1   . PHE A 1 72  ? 39.55700 -5.09600  -38.02700 1.000 87.78158  ? 72  PHE A CD1   1 
ATOM   521  C  CD2   . PHE A 1 72  ? 37.34600 -4.75200  -38.84900 1.000 99.28032  ? 72  PHE A CD2   1 
ATOM   522  C  CE1   . PHE A 1 72  ? 40.03600 -5.19700  -39.31700 1.000 93.20065  ? 72  PHE A CE1   1 
ATOM   523  C  CE2   . PHE A 1 72  ? 37.82200 -4.84700  -40.14900 1.000 95.42460  ? 72  PHE A CE2   1 
ATOM   524  C  CZ    . PHE A 1 72  ? 39.16800 -5.06900  -40.38200 1.000 96.67212  ? 72  PHE A CZ    1 
ATOM   525  N  N     . TYR A 1 73  ? 36.23100 -2.88400  -34.17200 1.000 107.08652 ? 73  TYR A N     1 
ATOM   526  C  CA    . TYR A 1 73  ? 35.63000 -2.60100  -32.87400 1.000 105.72320 ? 73  TYR A CA    1 
ATOM   527  C  C     . TYR A 1 73  ? 34.15100 -2.95000  -32.84500 1.000 105.73636 ? 73  TYR A C     1 
ATOM   528  O  O     . TYR A 1 73  ? 33.46900 -2.96300  -33.87200 1.000 111.90815 ? 73  TYR A O     1 
ATOM   529  C  CB    . TYR A 1 73  ? 35.81000 -1.13700  -32.44100 1.000 109.47365 ? 73  TYR A CB    1 
ATOM   530  C  CG    . TYR A 1 73  ? 37.24800 -0.73100  -32.23600 1.000 101.99118 ? 73  TYR A CG    1 
ATOM   531  C  CD1   . TYR A 1 73  ? 37.90800 -1.07500  -31.06500 1.000 98.85922  ? 73  TYR A CD1   1 
ATOM   532  C  CD2   . TYR A 1 73  ? 37.94200 0.00300   -33.18900 1.000 100.88052 ? 73  TYR A CD2   1 
ATOM   533  C  CE1   . TYR A 1 73  ? 39.21800 -0.71600  -30.85000 1.000 100.11464 ? 73  TYR A CE1   1 
ATOM   534  C  CE2   . TYR A 1 73  ? 39.26400 0.37200   -32.98100 1.000 98.91449  ? 73  TYR A CE2   1 
ATOM   535  C  CZ    . TYR A 1 73  ? 39.89500 0.00700   -31.80500 1.000 101.03317 ? 73  TYR A CZ    1 
ATOM   536  O  OH    . TYR A 1 73  ? 41.20700 0.35500   -31.56800 1.000 101.25161 ? 73  TYR A OH    1 
ATOM   537  N  N     . CYS A 1 74  ? 33.67400 -3.24400  -31.63300 1.000 103.89404 ? 74  CYS A N     1 
ATOM   538  C  CA    . CYS A 1 74  ? 32.24900 -3.44300  -31.39800 1.000 106.20484 ? 74  CYS A CA    1 
ATOM   539  C  C     . CYS A 1 74  ? 31.46000 -2.19500  -31.77400 1.000 112.38453 ? 74  CYS A C     1 
ATOM   540  O  O     . CYS A 1 74  ? 30.42300 -2.27600  -32.44400 1.000 109.78685 ? 74  CYS A O     1 
ATOM   541  C  CB    . CYS A 1 74  ? 32.00900 -3.79500  -29.92900 1.000 106.51540 ? 74  CYS A CB    1 
ATOM   542  S  SG    . CYS A 1 74  ? 32.80100 -5.30700  -29.35700 1.000 97.09848  ? 74  CYS A SG    1 
ATOM   543  N  N     . ASN A 1 75  ? 31.93600 -1.03100  -31.34400 1.000 111.69497 ? 75  ASN A N     1 
ATOM   544  C  CA    . ASN A 1 75  ? 31.21000 0.22000   -31.51800 1.000 113.26621 ? 75  ASN A CA    1 
ATOM   545  C  C     . ASN A 1 75  ? 32.19000 1.38000   -31.35200 1.000 115.82441 ? 75  ASN A C     1 
ATOM   546  O  O     . ASN A 1 75  ? 33.40400 1.17700   -31.24700 1.000 118.39841 ? 75  ASN A O     1 
ATOM   547  C  CB    . ASN A 1 75  ? 30.07100 0.29300   -30.49500 1.000 114.50320 ? 75  ASN A CB    1 
ATOM   548  C  CG    . ASN A 1 75  ? 30.54600 -0.02000  -29.07500 1.000 112.75562 ? 75  ASN A CG    1 
ATOM   549  O  OD1   . ASN A 1 75  ? 31.51400 0.56400   -28.58700 1.000 114.13737 ? 75  ASN A OD1   1 
ATOM   550  N  ND2   . ASN A 1 75  ? 29.88200 -0.96700  -28.42300 1.000 112.74773 ? 75  ASN A ND2   1 
ATOM   551  N  N     . VAL A 1 76  ? 31.65800 2.60700   -31.32300 1.000 115.16118 ? 76  VAL A N     1 
ATOM   552  C  CA    . VAL A 1 76  ? 32.52600 3.77700   -31.20700 1.000 108.54196 ? 76  VAL A CA    1 
ATOM   553  C  C     . VAL A 1 76  ? 33.08700 3.88900   -29.79500 1.000 109.02623 ? 76  VAL A C     1 
ATOM   554  O  O     . VAL A 1 76  ? 34.14500 4.49100   -29.58300 1.000 107.69186 ? 76  VAL A O     1 
ATOM   555  C  CB    . VAL A 1 76  ? 31.76700 5.05800   -31.60700 1.000 103.50188 ? 76  VAL A CB    1 
ATOM   556  C  CG1   . VAL A 1 76  ? 31.27500 4.96800   -33.04500 1.000 109.30258 ? 76  VAL A CG1   1 
ATOM   557  C  CG2   . VAL A 1 76  ? 30.61200 5.32200   -30.65100 1.000 104.11775 ? 76  VAL A CG2   1 
ATOM   558  N  N     . GLU A 1 77  ? 32.37300 3.34000   -28.81000 1.000 117.02982 ? 77  GLU A N     1 
ATOM   559  C  CA    . GLU A 1 77  ? 32.82400 3.35800   -27.42100 1.000 115.76914 ? 77  GLU A CA    1 
ATOM   560  C  C     . GLU A 1 77  ? 34.07300 2.50100   -27.21300 1.000 112.00290 ? 77  GLU A C     1 
ATOM   561  O  O     . GLU A 1 77  ? 35.04400 2.94900   -26.58900 1.000 111.11595 ? 77  GLU A O     1 
ATOM   562  C  CB    . GLU A 1 77  ? 31.67500 2.94600   -26.50100 1.000 116.81137 ? 77  GLU A CB    1 
ATOM   563  C  CG    . GLU A 1 77  ? 30.61900 4.05600   -26.37400 1.000 129.96821 ? 77  GLU A CG    1 
ATOM   564  C  CD    . GLU A 1 77  ? 29.19900 3.57200   -26.61800 1.000 145.87012 ? 77  GLU A CD    1 
ATOM   565  O  OE1   . GLU A 1 77  ? 28.97200 2.34500   -26.55800 1.000 153.88161 ? 77  GLU A OE1   1 
ATOM   566  O  OE2   . GLU A 1 77  ? 28.31200 4.41600   -26.88200 1.000 137.69809 ? 77  GLU A OE2   1 
ATOM   567  N  N     . CYS A 1 78  ? 34.04600 1.24200   -27.67500 1.000 111.15543 ? 78  CYS A N     1 
ATOM   568  C  CA    . CYS A 1 78  ? 35.25300 0.41200   -27.63600 1.000 109.75263 ? 78  CYS A CA    1 
ATOM   569  C  C     . CYS A 1 78  ? 36.41200 1.09100   -28.36000 1.000 110.19216 ? 78  CYS A C     1 
ATOM   570  O  O     . CYS A 1 78  ? 37.55800 1.04800   -27.89100 1.000 107.42077 ? 78  CYS A O     1 
ATOM   571  C  CB    . CYS A 1 78  ? 34.98400 -0.96800  -28.25400 1.000 106.82070 ? 78  CYS A CB    1 
ATOM   572  S  SG    . CYS A 1 78  ? 34.20100 -2.24500  -27.19900 1.000 98.81711  ? 78  CYS A SG    1 
ATOM   573  N  N     . GLN A 1 79  ? 36.13400 1.70500   -29.51500 1.000 112.06080 ? 79  GLN A N     1 
ATOM   574  C  CA    . GLN A 1 79  ? 37.16900 2.41000   -30.27100 1.000 107.31287 ? 79  GLN A CA    1 
ATOM   575  C  C     . GLN A 1 79  ? 37.76600 3.53800   -29.43000 1.000 105.54423 ? 79  GLN A C     1 
ATOM   576  O  O     . GLN A 1 79  ? 38.99600 3.70000   -29.35900 1.000 101.24109 ? 79  GLN A O     1 
ATOM   577  C  CB    . GLN A 1 79  ? 36.60000 2.88300   -31.61300 1.000 102.31753 ? 79  GLN A CB    1 
ATOM   578  C  CG    . GLN A 1 79  ? 37.60100 3.53500   -32.56400 1.000 104.89152 ? 79  GLN A CG    1 
ATOM   579  C  CD    . GLN A 1 79  ? 37.00300 3.80500   -33.93700 1.000 103.47293 ? 79  GLN A CD    1 
ATOM   580  O  OE1   . GLN A 1 79  ? 35.89000 3.36800   -34.23400 1.000 98.36179  ? 79  GLN A OE1   1 
ATOM   581  N  NE2   . GLN A 1 79  ? 37.74900 4.49700   -34.78900 1.000 100.07779 ? 79  GLN A NE2   1 
ATOM   582  N  N     . LYS A 1 80  ? 36.90800 4.31000   -28.75300 1.000 108.58670 ? 80  LYS A N     1 
ATOM   583  C  CA    . LYS A 1 80  ? 37.41500 5.40700   -27.93800 1.000 103.97826 ? 80  LYS A CA    1 
ATOM   584  C  C     . LYS A 1 80  ? 38.27000 4.84500   -26.80600 1.000 104.13880 ? 80  LYS A C     1 
ATOM   585  O  O     . LYS A 1 80  ? 39.35400 5.36600   -26.51900 1.000 104.73098 ? 80  LYS A O     1 
ATOM   586  C  CB    . LYS A 1 80  ? 36.26800 6.26700   -27.39300 1.000 96.73791  ? 80  LYS A CB    1 
ATOM   587  C  CG    . LYS A 1 80  ? 35.77400 7.37600   -28.33800 1.000 91.71100  ? 80  LYS A CG    1 
ATOM   588  C  CD    . LYS A 1 80  ? 34.41900 7.94100   -27.89500 1.000 97.78014  ? 80  LYS A CD    1 
ATOM   589  C  CE    . LYS A 1 80  ? 33.90500 9.04100   -28.83200 1.000 105.48107 ? 80  LYS A CE    1 
ATOM   590  N  NZ    . LYS A 1 80  ? 34.59300 10.35600  -28.66100 1.000 96.90372  ? 80  LYS A NZ    1 
ATOM   591  N  N     . GLU A 1 81  ? 37.79200 3.78300   -26.14000 1.000 105.95218 ? 81  GLU A N     1 
ATOM   592  C  CA    . GLU A 1 81  ? 38.57200 3.20800   -25.04300 1.000 104.88363 ? 81  GLU A CA    1 
ATOM   593  C  C     . GLU A 1 81  ? 39.89900 2.63400   -25.51100 1.000 103.95457 ? 81  GLU A C     1 
ATOM   594  O  O     . GLU A 1 81  ? 40.85300 2.56700   -24.72700 1.000 101.99907 ? 81  GLU A O     1 
ATOM   595  C  CB    . GLU A 1 81  ? 37.81500 2.07500   -24.35000 1.000 106.91545 ? 81  GLU A CB    1 
ATOM   596  C  CG    . GLU A 1 81  ? 36.55600 2.39000   -23.61000 1.000 112.00817 ? 81  GLU A CG    1 
ATOM   597  C  CD    . GLU A 1 81  ? 36.83700 3.33100   -22.46000 1.000 119.57486 ? 81  GLU A CD    1 
ATOM   598  O  OE1   . GLU A 1 81  ? 37.89800 3.15200   -21.81000 1.000 117.77202 ? 81  GLU A OE1   1 
ATOM   599  O  OE2   . GLU A 1 81  ? 35.98100 4.18900   -22.15900 1.000 123.43059 ? 81  GLU A OE2   1 
ATOM   600  N  N     . ASP A 1 82  ? 39.98700 2.20800   -26.76600 1.000 103.83087 ? 82  ASP A N     1 
ATOM   601  C  CA    . ASP A 1 82  ? 41.23700 1.61300   -27.21200 1.000 101.47006 ? 82  ASP A CA    1 
ATOM   602  C  C     . ASP A 1 82  ? 42.17600 2.63800   -27.82800 1.000 102.17804 ? 82  ASP A C     1 
ATOM   603  O  O     . ASP A 1 82  ? 43.33100 2.30500   -28.11700 1.000 100.46468 ? 82  ASP A O     1 
ATOM   604  C  CB    . ASP A 1 82  ? 40.99000 0.46000   -28.18600 1.000 102.95445 ? 82  ASP A CB    1 
ATOM   605  C  CG    . ASP A 1 82  ? 42.22600 -0.41200  -28.36500 1.000 98.87238  ? 82  ASP A CG    1 
ATOM   606  O  OD1   . ASP A 1 82  ? 42.89600 -0.68400  -27.34300 1.000 96.25628  ? 82  ASP A OD1   1 
ATOM   607  O  OD2   . ASP A 1 82  ? 42.52900 -0.82900  -29.50200 1.000 96.94057  ? 82  ASP A OD2   1 
ATOM   608  N  N     . TRP A 1 83  ? 41.71300 3.87500   -28.00900 1.000 91.78732  ? 83  TRP A N     1 
ATOM   609  C  CA    . TRP A 1 83  ? 42.54300 4.86800   -28.68400 1.000 83.06785  ? 83  TRP A CA    1 
ATOM   610  C  C     . TRP A 1 83  ? 43.84900 5.19600   -27.96600 1.000 78.63838  ? 83  TRP A C     1 
ATOM   611  O  O     . TRP A 1 83  ? 44.86500 5.36100   -28.66300 1.000 78.41466  ? 83  TRP A O     1 
ATOM   612  C  CB    . TRP A 1 83  ? 41.76600 6.17300   -28.86500 1.000 87.25520  ? 83  TRP A CB    1 
ATOM   613  C  CG    . TRP A 1 83  ? 42.61500 7.22100   -29.49200 1.000 92.50320  ? 83  TRP A CG    1 
ATOM   614  C  CD1   . TRP A 1 83  ? 43.08400 8.36400   -28.90700 1.000 96.70896  ? 83  TRP A CD1   1 
ATOM   615  C  CD2   . TRP A 1 83  ? 43.06500 7.24700   -30.84700 1.000 93.65333  ? 83  TRP A CD2   1 
ATOM   616  N  NE1   . TRP A 1 83  ? 43.82900 9.08400   -29.81300 1.000 101.62534 ? 83  TRP A NE1   1 
ATOM   617  C  CE2   . TRP A 1 83  ? 43.82500 8.42200   -31.01300 1.000 96.35629  ? 83  TRP A CE2   1 
ATOM   618  C  CE3   . TRP A 1 83  ? 42.90400 6.38500   -31.93500 1.000 88.75275  ? 83  TRP A CE3   1 
ATOM   619  C  CZ2   . TRP A 1 83  ? 44.42300 8.75600   -32.22500 1.000 94.56397  ? 83  TRP A CZ2   1 
ATOM   620  C  CZ3   . TRP A 1 83  ? 43.49600 6.71800   -33.13600 1.000 93.70597  ? 83  TRP A CZ3   1 
ATOM   621  C  CH2   . TRP A 1 83  ? 44.25000 7.89000   -33.27100 1.000 96.09836  ? 83  TRP A CH2   1 
ATOM   622  N  N     . PRO A 1 84  ? 43.92000 5.29200   -26.63000 1.000 81.20184  ? 84  PRO A N     1 
ATOM   623  C  CA    . PRO A 1 84  ? 45.23000 5.55800   -26.00400 1.000 81.28869  ? 84  PRO A CA    1 
ATOM   624  C  C     . PRO A 1 84  ? 46.29600 4.54500   -26.37500 1.000 78.56995  ? 84  PRO A C     1 
ATOM   625  O  O     . PRO A 1 84  ? 47.47800 4.89900   -26.43200 1.000 80.57545  ? 84  PRO A O     1 
ATOM   626  C  CB    . PRO A 1 84  ? 44.91900 5.53200   -24.50300 1.000 84.77332  ? 84  PRO A CB    1 
ATOM   627  C  CG    . PRO A 1 84  ? 43.50100 5.91400   -24.41700 1.000 94.97455  ? 84  PRO A CG    1 
ATOM   628  C  CD    . PRO A 1 84  ? 42.84000 5.30900   -25.62500 1.000 93.26908  ? 84  PRO A CD    1 
ATOM   629  N  N     . MET A 1 85  ? 45.92400 3.29600   -26.61800 1.000 78.74628  ? 85  MET A N     1 
ATOM   630  C  CA    . MET A 1 85  ? 46.89600 2.31000   -27.06100 1.000 70.76112  ? 85  MET A CA    1 
ATOM   631  C  C     . MET A 1 85  ? 46.97100 2.24100   -28.57800 1.000 71.55068  ? 85  MET A C     1 
ATOM   632  O  O     . MET A 1 85  ? 48.06400 2.11000   -29.14100 1.000 73.44828  ? 85  MET A O     1 
ATOM   633  C  CB    . MET A 1 85  ? 46.56300 0.94000   -26.47900 1.000 72.93769  ? 85  MET A CB    1 
ATOM   634  C  CG    . MET A 1 85  ? 46.63000 0.90000   -24.97100 1.000 77.63299  ? 85  MET A CG    1 
ATOM   635  S  SD    . MET A 1 85  ? 48.32000 1.18500   -24.39000 1.000 77.60141  ? 85  MET A SD    1 
ATOM   636  C  CE    . MET A 1 85  ? 48.24100 0.51200   -22.72700 1.000 74.24048  ? 85  MET A CE    1 
ATOM   637  N  N     . HIS A 1 86  ? 45.81900 2.31400   -29.24600 1.000 73.06929  ? 86  HIS A N     1 
ATOM   638  C  CA    . HIS A 1 86  ? 45.79500 2.17200   -30.69500 1.000 76.49865  ? 86  HIS A CA    1 
ATOM   639  C  C     . HIS A 1 86  ? 46.58000 3.27200   -31.39600 1.000 74.19047  ? 86  HIS A C     1 
ATOM   640  O  O     . HIS A 1 86  ? 47.17600 3.02100   -32.44900 1.000 79.24108  ? 86  HIS A O     1 
ATOM   641  C  CB    . HIS A 1 86  ? 44.35200 2.15900   -31.20000 1.000 87.61840  ? 86  HIS A CB    1 
ATOM   642  C  CG    . HIS A 1 86  ? 44.24100 2.04800   -32.68900 1.000 85.83661  ? 86  HIS A CG    1 
ATOM   643  N  ND1   . HIS A 1 86  ? 44.87500 1.05900   -33.41000 1.000 84.98387  ? 86  HIS A ND1   1 
ATOM   644  C  CD2   . HIS A 1 86  ? 43.56700 2.79900   -33.59200 1.000 85.34708  ? 86  HIS A CD2   1 
ATOM   645  C  CE1   . HIS A 1 86  ? 44.60300 1.21000   -34.69400 1.000 77.92513  ? 86  HIS A CE1   1 
ATOM   646  N  NE2   . HIS A 1 86  ? 43.80800 2.25600   -34.83000 1.000 77.91724  ? 86  HIS A NE2   1 
ATOM   647  N  N     . LYS A 1 87  ? 46.61200 4.48400   -30.83300 1.000 72.84031  ? 87  LYS A N     1 
ATOM   648  C  CA    . LYS A 1 87  ? 47.34000 5.57000   -31.48800 1.000 74.42734  ? 87  LYS A CA    1 
ATOM   649  C  C     . LYS A 1 87  ? 48.83500 5.29000   -31.59200 1.000 76.75920  ? 87  LYS A C     1 
ATOM   650  O  O     . LYS A 1 87  ? 49.52000 5.93300   -32.39600 1.000 81.98351  ? 87  LYS A O     1 
ATOM   651  C  CB    . LYS A 1 87  ? 47.12600 6.88900   -30.74700 1.000 74.13784  ? 87  LYS A CB    1 
ATOM   652  C  CG    . LYS A 1 87  ? 47.80700 6.94400   -29.39600 1.000 73.91676  ? 87  LYS A CG    1 
ATOM   653  C  CD    . LYS A 1 87  ? 47.53100 8.25000   -28.67700 1.000 75.38799  ? 87  LYS A CD    1 
ATOM   654  C  CE    . LYS A 1 87  ? 48.30800 8.32300   -27.36800 1.000 86.51300  ? 87  LYS A CE    1 
ATOM   655  N  NZ    . LYS A 1 87  ? 47.94300 9.51900   -26.55400 1.000 89.61074  ? 87  LYS A NZ    1 
ATOM   656  N  N     . LEU A 1 88  ? 49.35600 4.35000   -30.79900 1.000 70.95061  ? 88  LEU A N     1 
ATOM   657  C  CA    . LEU A 1 88  ? 50.74400 3.92300   -30.93400 1.000 71.65333  ? 88  LEU A CA    1 
ATOM   658  C  C     . LEU A 1 88  ? 51.01700 3.28700   -32.28700 1.000 76.57497  ? 88  LEU A C     1 
ATOM   659  O  O     . LEU A 1 88  ? 52.16500 3.28900   -32.74500 1.000 74.32207  ? 88  LEU A O     1 
ATOM   660  C  CB    . LEU A 1 88  ? 51.10900 2.94700   -29.81800 1.000 66.41849  ? 88  LEU A CB    1 
ATOM   661  C  CG    . LEU A 1 88  ? 50.93300 3.48700   -28.39900 1.000 69.79521  ? 88  LEU A CG    1 
ATOM   662  C  CD1   . LEU A 1 88  ? 51.30000 2.43300   -27.36600 1.000 65.85263  ? 88  LEU A CD1   1 
ATOM   663  C  CD2   . LEU A 1 88  ? 51.75800 4.74000   -28.20500 1.000 85.60763  ? 88  LEU A CD2   1 
ATOM   664  N  N     . GLU A 1 89  ? 49.98800 2.75000   -32.94000 1.000 76.64340  ? 89  GLU A N     1 
ATOM   665  C  CA    . GLU A 1 89  ? 50.16200 1.97900   -34.15700 1.000 74.97478  ? 89  GLU A CA    1 
ATOM   666  C  C     . GLU A 1 89  ? 49.35300 2.50200   -35.33200 1.000 79.80431  ? 89  GLU A C     1 
ATOM   667  O  O     . GLU A 1 89  ? 49.74600 2.25900   -36.47400 1.000 84.52592  ? 89  GLU A O     1 
ATOM   668  C  CB    . GLU A 1 89  ? 49.77000 0.51400   -33.90400 1.000 74.90898  ? 89  GLU A CB    1 
ATOM   669  C  CG    . GLU A 1 89  ? 50.59000 -0.16800  -32.80600 1.000 80.29910  ? 89  GLU A CG    1 
ATOM   670  C  CD    . GLU A 1 89  ? 50.11700 -1.58600  -32.48700 1.000 78.33834  ? 89  GLU A CD    1 
ATOM   671  O  OE1   . GLU A 1 89  ? 48.91600 -1.87900  -32.68100 1.000 80.52808  ? 89  GLU A OE1   1 
ATOM   672  O  OE2   . GLU A 1 89  ? 50.94500 -2.40100  -32.01900 1.000 64.89725  ? 89  GLU A OE2   1 
ATOM   673  N  N     . CYS A 1 90  ? 48.25500 3.22200   -35.08400 1.000 87.80790  ? 90  CYS A N     1 
ATOM   674  C  CA    . CYS A 1 90  ? 47.34700 3.65600   -36.14600 1.000 90.20292  ? 90  CYS A CA    1 
ATOM   675  C  C     . CYS A 1 90  ? 48.10100 4.31300   -37.30100 1.000 91.91102  ? 90  CYS A C     1 
ATOM   676  O  O     . CYS A 1 90  ? 48.09600 3.82000   -38.43300 1.000 92.33739  ? 90  CYS A O     1 
ATOM   677  C  CB    . CYS A 1 90  ? 46.31000 4.61600   -35.56800 1.000 92.22948  ? 90  CYS A CB    1 
ATOM   678  S  SG    . CYS A 1 90  ? 44.97500 5.04200   -36.69300 1.000 95.36670  ? 90  CYS A SG    1 
ATOM   679  N  N     A SER A 1 91  ? 48.77300 5.43300   -37.01400 1.000 87.19993  ? 91  SER A N     1 
ATOM   680  C  CA    A SER A 1 91  ? 49.51400 6.14900   -38.05400 1.000 92.29791  ? 91  SER A CA    1 
ATOM   681  C  C     A SER A 1 91  ? 50.77300 5.40900   -38.49100 1.000 90.39505  ? 91  SER A C     1 
ATOM   682  O  O     A SER A 1 91  ? 51.03900 5.36400   -39.70700 1.000 91.31358  ? 91  SER A O     1 
ATOM   683  C  CB    A SER A 1 91  ? 49.82700 7.57900   -37.59600 1.000 91.26621  ? 91  SER A CB    1 
ATOM   684  O  OG    A SER A 1 91  ? 50.53500 8.28700   -38.59600 1.000 93.46384  ? 91  SER A OG    1 
ATOM   685  N  N     . PRO A 1 92  ? 51.62100 4.88700   -37.59200 1.000 85.18390  ? 92  PRO A N     1 
ATOM   686  C  CA    . PRO A 1 92  ? 52.78000 4.10900   -38.05800 1.000 79.28845  ? 92  PRO A CA    1 
ATOM   687  C  C     . PRO A 1 92  ? 52.41600 2.98200   -38.99900 1.000 80.71757  ? 92  PRO A C     1 
ATOM   688  O  O     . PRO A 1 92  ? 53.16400 2.71200   -39.94100 1.000 84.65752  ? 92  PRO A O     1 
ATOM   689  C  CB    . PRO A 1 92  ? 53.37900 3.56300   -36.75500 1.000 77.04871  ? 92  PRO A CB    1 
ATOM   690  C  CG    . PRO A 1 92  ? 53.02000 4.57100   -35.73600 1.000 88.05003  ? 92  PRO A CG    1 
ATOM   691  C  CD    . PRO A 1 92  ? 51.64900 5.06600   -36.12500 1.000 89.41862  ? 92  PRO A CD    1 
ATOM   692  N  N     . MET A 1 93  ? 51.26500 2.34100   -38.80200 1.000 82.16775  ? 93  MET A N     1 
ATOM   693  C  CA    . MET A 1 93  ? 50.88200 1.23200   -39.66500 1.000 77.63036  ? 93  MET A CA    1 
ATOM   694  C  C     . MET A 1 93  ? 50.71000 1.68900   -41.11300 1.000 77.53298  ? 93  MET A C     1 
ATOM   695  O  O     . MET A 1 93  ? 51.28100 1.08800   -42.03100 1.000 78.89893  ? 93  MET A O     1 
ATOM   696  C  CB    . MET A 1 93  ? 49.59600 0.63600   -39.10300 1.000 71.95336  ? 93  MET A CB    1 
ATOM   697  C  CG    . MET A 1 93  ? 49.85800 -0.31800  -37.94600 1.000 72.60081  ? 93  MET A CG    1 
ATOM   698  S  SD    . MET A 1 93  ? 48.48900 -1.40300  -37.56600 1.000 91.68731  ? 93  MET A SD    1 
ATOM   699  C  CE    . MET A 1 93  ? 48.15400 -2.00600  -39.19700 1.000 85.53394  ? 93  MET A CE    1 
ATOM   700  N  N     . VAL A 1 94  ? 50.06600 2.84000   -41.32000 1.000 74.78002  ? 94  VAL A N     1 
ATOM   701  C  CA    . VAL A 1 94  ? 49.84600 3.32900   -42.68100 1.000 83.96796  ? 94  VAL A CA    1 
ATOM   702  C  C     . VAL A 1 94  ? 51.11300 3.96800   -43.23800 1.000 81.32291  ? 94  VAL A C     1 
ATOM   703  O  O     . VAL A 1 94  ? 51.35700 3.91500   -44.45000 1.000 82.63622  ? 94  VAL A O     1 
ATOM   704  C  CB    . VAL A 1 94  ? 48.64600 4.29200   -42.75800 1.000 85.85766  ? 94  VAL A CB    1 
ATOM   705  C  CG1   . VAL A 1 94  ? 47.33800 3.52500   -42.61500 1.000 85.32076  ? 94  VAL A CG1   1 
ATOM   706  C  CG2   . VAL A 1 94  ? 48.74600 5.37300   -41.70900 1.000 91.63993  ? 94  VAL A CG2   1 
ATOM   707  N  N     . VAL A 1 95  ? 51.93100 4.58400   -42.38400 1.000 78.73576  ? 95  VAL A N     1 
ATOM   708  C  CA    . VAL A 1 95  ? 53.15100 5.21900   -42.87100 1.000 82.88625  ? 95  VAL A CA    1 
ATOM   709  C  C     . VAL A 1 95  ? 54.16900 4.16500   -43.28500 1.000 83.29683  ? 95  VAL A C     1 
ATOM   710  O  O     . VAL A 1 95  ? 54.76800 4.24900   -44.36200 1.000 85.13652  ? 95  VAL A O     1 
ATOM   711  C  CB    . VAL A 1 95  ? 53.73500 6.16300   -41.80400 1.000 82.64149  ? 95  VAL A CB    1 
ATOM   712  C  CG1   . VAL A 1 95  ? 55.09500 6.68600   -42.24900 1.000 82.93626  ? 95  VAL A CG1   1 
ATOM   713  C  CG2   . VAL A 1 95  ? 52.79200 7.32200   -41.55300 1.000 84.72068  ? 95  VAL A CG2   1 
ATOM   714  N  N     . PHE A 1 96  ? 54.38300 3.16100   -42.43600 1.000 81.48082  ? 96  PHE A N     1 
ATOM   715  C  CA    . PHE A 1 96  ? 55.32500 2.10300   -42.76400 1.000 83.44422  ? 96  PHE A CA    1 
ATOM   716  C  C     . PHE A 1 96  ? 54.80600 1.19400   -43.87300 1.000 91.37675  ? 96  PHE A C     1 
ATOM   717  O  O     . PHE A 1 96  ? 55.61600 0.62000   -44.61400 1.000 92.55320  ? 96  PHE A O     1 
ATOM   718  C  CB    . PHE A 1 96  ? 55.62000 1.28300   -41.50700 1.000 79.94643  ? 96  PHE A CB    1 
ATOM   719  C  CG    . PHE A 1 96  ? 56.66700 1.89800   -40.62000 1.000 82.11248  ? 96  PHE A CG    1 
ATOM   720  C  CD1   . PHE A 1 96  ? 58.01000 1.83100   -40.94200 1.000 86.91832  ? 96  PHE A CD1   1 
ATOM   721  C  CD2   . PHE A 1 96  ? 56.29400 2.55000   -39.45000 1.000 80.55176  ? 96  PHE A CD2   1 
ATOM   722  C  CE1   . PHE A 1 96  ? 58.96500 2.41100   -40.11500 1.000 88.23953  ? 96  PHE A CE1   1 
ATOM   723  C  CE2   . PHE A 1 96  ? 57.24100 3.12700   -38.62400 1.000 78.02514  ? 96  PHE A CE2   1 
ATOM   724  C  CZ    . PHE A 1 96  ? 58.57500 3.05900   -38.95400 1.000 78.26465  ? 96  PHE A CZ    1 
ATOM   725  N  N     . GLY A 1 97  ? 53.48000 1.07100   -44.02900 1.000 91.10566  ? 97  GLY A N     1 
ATOM   726  C  CA    . GLY A 1 97  ? 52.96400 0.27300   -45.13300 1.000 90.74246  ? 97  GLY A CA    1 
ATOM   727  C  C     . GLY A 1 97  ? 53.29600 -1.18000  -44.87200 1.000 90.87405  ? 97  GLY A C     1 
ATOM   728  O  O     . GLY A 1 97  ? 53.04000 -1.72000  -43.79000 1.000 86.94727  ? 97  GLY A O     1 
ATOM   729  N  N     . GLU A 1 98  ? 53.86400 -1.82600  -45.88500 1.000 102.44649 ? 98  GLU A N     1 
ATOM   730  C  CA    . GLU A 1 98  ? 54.24700 -3.22100  -45.75700 1.000 100.56469 ? 98  GLU A CA    1 
ATOM   731  C  C     . GLU A 1 98  ? 55.43400 -3.39600  -44.82000 1.000 98.70131  ? 98  GLU A C     1 
ATOM   732  O  O     . GLU A 1 98  ? 55.61500 -4.49200  -44.28500 1.000 97.07743  ? 98  GLU A O     1 
ATOM   733  C  CB    . GLU A 1 98  ? 54.55200 -3.82700  -47.12500 1.000 102.42281 ? 98  GLU A CB    1 
ATOM   734  C  CG    . GLU A 1 98  ? 53.80600 -5.11400  -47.40600 1.000 120.99345 ? 98  GLU A CG    1 
ATOM   735  C  CD    . GLU A 1 98  ? 54.07000 -5.65900  -48.79300 1.000 128.51804 ? 98  GLU A CD    1 
ATOM   736  O  OE1   . GLU A 1 98  ? 54.51100 -4.90200  -49.68900 1.000 125.53084 ? 98  GLU A OE1   1 
ATOM   737  O  OE2   . GLU A 1 98  ? 53.85200 -6.86100  -48.97000 1.000 131.36049 ? 98  GLU A OE2   1 
ATOM   738  N  N     . ASN A 1 99  ? 56.23100 -2.34500  -44.58600 1.000 87.21046  ? 99  ASN A N     1 
ATOM   739  C  CA    . ASN A 1 99  ? 57.39000 -2.47100  -43.71100 1.000 90.43716  ? 99  ASN A CA    1 
ATOM   740  C  C     . ASN A 1 99  ? 57.02300 -2.55200  -42.23200 1.000 89.50284  ? 99  ASN A C     1 
ATOM   741  O  O     . ASN A 1 99  ? 57.90200 -2.83500  -41.40700 1.000 86.56827  ? 99  ASN A O     1 
ATOM   742  C  CB    . ASN A 1 99  ? 58.29700 -1.24500  -43.88800 1.000 86.96569  ? 99  ASN A CB    1 
ATOM   743  C  CG    . ASN A 1 99  ? 58.80400 -1.09100  -45.30400 1.000 95.61936  ? 99  ASN A CG    1 
ATOM   744  O  OD1   . ASN A 1 99  ? 59.11400 -2.07400  -45.97100 1.000 103.58347 ? 99  ASN A OD1   1 
ATOM   745  N  ND2   . ASN A 1 99  ? 58.86000 0.15200   -45.78400 1.000 98.46181  ? 99  ASN A ND2   1 
ATOM   746  N  N     . TRP A 1 100 ? 55.76300 -2.33200  -41.86800 1.000 87.67104  ? 100 TRP A N     1 
ATOM   747  C  CA    . TRP A 1 100 ? 55.35600 -2.46900  -40.47400 1.000 79.81746  ? 100 TRP A CA    1 
ATOM   748  C  C     . TRP A 1 100 ? 55.25500 -3.94200  -40.08000 1.000 77.72248  ? 100 TRP A C     1 
ATOM   749  O  O     . TRP A 1 100 ? 54.30700 -4.62700  -40.47700 1.000 78.66469  ? 100 TRP A O     1 
ATOM   750  C  CB    . TRP A 1 100 ? 54.02200 -1.75900  -40.26800 1.000 76.55918  ? 100 TRP A CB    1 
ATOM   751  C  CG    . TRP A 1 100 ? 53.65500 -1.60200  -38.83500 1.000 80.11224  ? 100 TRP A CG    1 
ATOM   752  C  CD1   . TRP A 1 100 ? 54.05000 -0.59800  -37.99800 1.000 79.32267  ? 100 TRP A CD1   1 
ATOM   753  C  CD2   . TRP A 1 100 ? 52.86000 -2.49000  -38.04800 1.000 74.21153  ? 100 TRP A CD2   1 
ATOM   754  N  NE1   . TRP A 1 100 ? 53.53000 -0.79400  -36.74400 1.000 66.19215  ? 100 TRP A NE1   1 
ATOM   755  C  CE2   . TRP A 1 100 ? 52.79700 -1.95100  -36.74700 1.000 70.58478  ? 100 TRP A CE2   1 
ATOM   756  C  CE3   . TRP A 1 100 ? 52.18800 -3.68600  -38.31700 1.000 72.66661  ? 100 TRP A CE3   1 
ATOM   757  C  CZ2   . TRP A 1 100 ? 52.09000 -2.56600  -35.72000 1.000 75.12480  ? 100 TRP A CZ2   1 
ATOM   758  C  CZ3   . TRP A 1 100 ? 51.48700 -4.29400  -37.29600 1.000 72.60344  ? 100 TRP A CZ3   1 
ATOM   759  C  CH2   . TRP A 1 100 ? 51.44300 -3.73400  -36.01300 1.000 71.96126  ? 100 TRP A CH2   1 
ATOM   760  N  N     . ASN A 1 101 ? 56.22600 -4.44300  -39.29600 1.000 76.71446  ? 101 ASN A N     1 
ATOM   761  C  CA    . ASN A 1 101 ? 56.20300 -5.84700  -38.87400 1.000 77.09345  ? 101 ASN A CA    1 
ATOM   762  C  C     . ASN A 1 101 ? 56.84500 -6.05700  -37.49700 1.000 75.16164  ? 101 ASN A C     1 
ATOM   763  O  O     . ASN A 1 101 ? 57.70400 -6.93800  -37.35400 1.000 79.50690  ? 101 ASN A O     1 
ATOM   764  C  CB    . ASN A 1 101 ? 56.85500 -6.74400  -39.93400 1.000 80.17014  ? 101 ASN A CB    1 
ATOM   765  C  CG    . ASN A 1 101 ? 58.32300 -6.44600  -40.14100 1.000 85.33392  ? 101 ASN A CG    1 
ATOM   766  O  OD1   . ASN A 1 101 ? 58.80400 -5.36400  -39.80800 1.000 84.93124  ? 101 ASN A OD1   1 
ATOM   767  N  ND2   . ASN A 1 101 ? 59.04200 -7.40500  -40.71800 1.000 92.26896  ? 101 ASN A ND2   1 
ATOM   768  N  N     . PRO A 1 102 ? 56.46800 -5.30200  -36.46100 1.000 69.85311  ? 102 PRO A N     1 
ATOM   769  C  CA    . PRO A 1 102 ? 57.01900 -5.56700  -35.12400 1.000 59.47029  ? 102 PRO A CA    1 
ATOM   770  C  C     . PRO A 1 102 ? 56.51500 -6.87100  -34.52800 1.000 63.01019  ? 102 PRO A C     1 
ATOM   771  O  O     . PRO A 1 102 ? 55.35500 -7.24900  -34.71000 1.000 62.46012  ? 102 PRO A O     1 
ATOM   772  C  CB    . PRO A 1 102 ? 56.53100 -4.37300  -34.30000 1.000 64.15769  ? 102 PRO A CB    1 
ATOM   773  C  CG    . PRO A 1 102 ? 55.24300 -4.01900  -34.93100 1.000 70.66374  ? 102 PRO A CG    1 
ATOM   774  C  CD    . PRO A 1 102 ? 55.42100 -4.26600  -36.40900 1.000 74.90898  ? 102 PRO A CD    1 
ATOM   775  N  N     . SER A 1 103 ? 57.40600 -7.57000  -33.82600 1.000 67.37387  ? 103 SER A N     1 
ATOM   776  C  CA    . SER A 1 103 ? 56.98800 -8.79000  -33.15700 1.000 56.36202  ? 103 SER A CA    1 
ATOM   777  C  C     . SER A 1 103 ? 55.98100 -8.44400  -32.06500 1.000 55.29610  ? 103 SER A C     1 
ATOM   778  O  O     . SER A 1 103 ? 55.89700 -7.30700  -31.59400 1.000 57.50426  ? 103 SER A O     1 
ATOM   779  C  CB    . SER A 1 103 ? 58.18500 -9.51800  -32.54600 1.000 57.25950  ? 103 SER A CB    1 
ATOM   780  O  OG    . SER A 1 103 ? 58.66600 -8.82300  -31.40800 1.000 66.03950  ? 103 SER A OG    1 
ATOM   781  N  N     . GLU A 1 104 ? 55.21000 -9.45000  -31.65900 1.000 57.09369  ? 104 GLU A N     1 
ATOM   782  C  CA    . GLU A 1 104 ? 54.17000 -9.22700  -30.66200 1.000 56.68838  ? 104 GLU A CA    1 
ATOM   783  C  C     . GLU A 1 104 ? 54.75700 -8.78100  -29.33000 1.000 58.33068  ? 104 GLU A C     1 
ATOM   784  O  O     . GLU A 1 104 ? 54.14400 -7.97600  -28.61500 1.000 59.75190  ? 104 GLU A O     1 
ATOM   785  C  CB    . GLU A 1 104 ? 53.32100 -10.48300 -30.49600 1.000 56.65416  ? 104 GLU A CB    1 
ATOM   786  C  CG    . GLU A 1 104 ? 52.03700 -10.24500 -29.72700 1.000 66.30532  ? 104 GLU A CG    1 
ATOM   787  C  CD    . GLU A 1 104 ? 50.96900 -11.26400 -30.06300 1.000 66.23952  ? 104 GLU A CD    1 
ATOM   788  O  OE1   . GLU A 1 104 ? 50.64800 -11.41000 -31.26400 1.000 59.76506  ? 104 GLU A OE1   1 
ATOM   789  O  OE2   . GLU A 1 104 ? 50.43900 -11.90600 -29.13000 1.000 68.28450  ? 104 GLU A OE2   1 
ATOM   790  N  N     . THR A 1 105 ? 55.94600 -9.28500  -28.98900 1.000 55.74616  ? 105 THR A N     1 
ATOM   791  C  CA    . THR A 1 105 ? 56.61800 -8.84000  -27.77500 1.000 52.08256  ? 105 THR A CA    1 
ATOM   792  C  C     . THR A 1 105 ? 56.88900 -7.34200  -27.80700 1.000 56.37518  ? 105 THR A C     1 
ATOM   793  O  O     . THR A 1 105 ? 56.67900 -6.64600  -26.80500 1.000 56.15936  ? 105 THR A O     1 
ATOM   794  C  CB    . THR A 1 105 ? 57.93300 -9.60700  -27.60800 1.000 49.58489  ? 105 THR A CB    1 
ATOM   795  O  OG1   . THR A 1 105 ? 57.66000 -10.99900 -27.40900 1.000 65.03411  ? 105 THR A OG1   1 
ATOM   796  C  CG2   . THR A 1 105 ? 58.71800 -9.08500  -26.41200 1.000 57.83325  ? 105 THR A CG2   1 
ATOM   797  N  N     . VAL A 1 106 ? 57.30800 -6.81800  -28.95900 1.000 56.66206  ? 106 VAL A N     1 
ATOM   798  C  CA    . VAL A 1 106 ? 57.54900 -5.38300  -29.07800 1.000 55.82511  ? 106 VAL A CA    1 
ATOM   799  C  C     . VAL A 1 106 ? 56.25200 -4.59100  -28.91500 1.000 58.92285  ? 106 VAL A C     1 
ATOM   800  O  O     . VAL A 1 106 ? 56.21500 -3.57800  -28.20300 1.000 58.19382  ? 106 VAL A O     1 
ATOM   801  C  CB    . VAL A 1 106 ? 58.23600 -5.07900  -30.42100 1.000 52.69579  ? 106 VAL A CB    1 
ATOM   802  C  CG1   . VAL A 1 106 ? 58.33700 -3.58100  -30.63700 1.000 60.52041  ? 106 VAL A CG1   1 
ATOM   803  C  CG2   . VAL A 1 106 ? 59.61100 -5.74600  -30.48100 1.000 65.91053  ? 106 VAL A CG2   1 
ATOM   804  N  N     . ARG A 1 107 ? 55.17500 -5.03300  -29.57700 1.000 55.93565  ? 107 ARG A N     1 
ATOM   805  C  CA    . ARG A 1 107 ? 53.88500 -4.35400  -29.46000 1.000 52.23784  ? 107 ARG A CA    1 
ATOM   806  C  C     . ARG A 1 107 ? 53.43200 -4.28900  -28.01000 1.000 56.34360  ? 107 ARG A C     1 
ATOM   807  O  O     . ARG A 1 107 ? 53.06200 -3.22000  -27.49100 1.000 64.45510  ? 107 ARG A O     1 
ATOM   808  C  CB    . ARG A 1 107 ? 52.84400 -5.09700  -30.30100 1.000 53.81698  ? 107 ARG A CB    1 
ATOM   809  C  CG    . ARG A 1 107 ? 53.16500 -5.13800  -31.77900 1.000 60.34408  ? 107 ARG A CG    1 
ATOM   810  C  CD    . ARG A 1 107 ? 52.08700 -5.82900  -32.59000 1.000 62.12850  ? 107 ARG A CD    1 
ATOM   811  N  NE    . ARG A 1 107 ? 50.83400 -5.08700  -32.59300 1.000 64.99200  ? 107 ARG A NE    1 
ATOM   812  C  CZ    . ARG A 1 107 ? 49.64200 -5.63700  -32.77700 1.000 61.93637  ? 107 ARG A CZ    1 
ATOM   813  N  NH1   . ARG A 1 107 ? 49.50200 -6.94000  -32.96500 1.000 54.74077  ? 107 ARG A NH1   1 
ATOM   814  N  NH2   . ARG A 1 107 ? 48.56100 -4.86200  -32.76300 1.000 66.71589  ? 107 ARG A NH2   1 
ATOM   815  N  N     . LEU A 1 108 ? 53.56200 -5.41400  -27.31100 1.000 52.18520  ? 108 LEU A N     1 
ATOM   816  C  CA    . LEU A 1 108 ? 53.13500 -5.47200  -25.92400 1.000 50.48237  ? 108 LEU A CA    1 
ATOM   817  C  C     . LEU A 1 108 ? 53.99600 -4.57300  -25.04900 1.000 54.91185  ? 108 LEU A C     1 
ATOM   818  O  O     . LEU A 1 108 ? 53.47100 -3.87100  -24.17800 1.000 62.79700  ? 108 LEU A O     1 
ATOM   819  C  CB    . LEU A 1 108 ? 53.15700 -6.91800  -25.43300 1.000 47.93996  ? 108 LEU A CB    1 
ATOM   820  C  CG    . LEU A 1 108 ? 52.64100 -7.12700  -24.00900 1.000 49.41645  ? 108 LEU A CG    1 
ATOM   821  C  CD1   . LEU A 1 108 ? 51.24600 -6.55800  -23.86800 1.000 55.34874  ? 108 LEU A CD1   1 
ATOM   822  C  CD2   . LEU A 1 108 ? 52.63100 -8.59300  -23.64000 1.000 53.14848  ? 108 LEU A CD2   1 
ATOM   823  N  N     . THR A 1 109 ? 55.32000 -4.61100  -25.23100 1.000 53.04320  ? 109 THR A N     1 
ATOM   824  C  CA    . THR A 1 109 ? 56.19100 -3.77400  -24.41200 1.000 53.59853  ? 109 THR A CA    1 
ATOM   825  C  C     . THR A 1 109 ? 55.91000 -2.29300  -24.63200 1.000 54.49601  ? 109 THR A C     1 
ATOM   826  O  O     . THR A 1 109 ? 55.95500 -1.49100  -23.68600 1.000 54.38020  ? 109 THR A O     1 
ATOM   827  C  CB    . THR A 1 109 ? 57.64700 -4.09100  -24.74000 1.000 56.88577  ? 109 THR A CB    1 
ATOM   828  O  OG1   . THR A 1 109 ? 57.89400 -5.47700  -24.47500 1.000 59.63347  ? 109 THR A OG1   1 
ATOM   829  C  CG2   . THR A 1 109 ? 58.57300 -3.25400  -23.89200 1.000 61.25734  ? 109 THR A CG2   1 
ATOM   830  N  N     . ALA A 1 110 ? 55.62200 -1.90800  -25.87800 1.000 50.89558  ? 110 ALA A N     1 
ATOM   831  C  CA    . ALA A 1 110 ? 55.25600 -0.52100  -26.14400 1.000 51.16140  ? 110 ALA A CA    1 
ATOM   832  C  C     . ALA A 1 110 ? 53.99900 -0.13500  -25.37700 1.000 57.46215  ? 110 ALA A C     1 
ATOM   833  O  O     . ALA A 1 110 ? 53.92600 0.94400   -24.76900 1.000 63.23916  ? 110 ALA A O     1 
ATOM   834  C  CB    . ALA A 1 110 ? 55.05900 -0.30300  -27.63700 1.000 59.19657  ? 110 ALA A CB    1 
ATOM   835  N  N     . ARG A 1 111 ? 53.04100 -1.05500  -25.29400 1.000 56.96209  ? 111 ARG A N     1 
ATOM   836  C  CA    . ARG A 1 111 ? 51.82500 -0.71900  -24.55700 1.000 56.91735  ? 111 ARG A CA    1 
ATOM   837  C  C     . ARG A 1 111 ? 52.05700 -0.71300  -23.05000 1.000 60.27302  ? 111 ARG A C     1 
ATOM   838  O  O     . ARG A 1 111 ? 51.42100 0.07000   -22.33200 1.000 63.81818  ? 111 ARG A O     1 
ATOM   839  C  CB    . ARG A 1 111 ? 50.70300 -1.69500  -24.92000 1.000 56.60152  ? 111 ARG A CB    1 
ATOM   840  C  CG    . ARG A 1 111 ? 50.13100 -1.48300  -26.32200 1.000 59.19131  ? 111 ARG A CG    1 
ATOM   841  C  CD    . ARG A 1 111 ? 49.16000 -2.56500  -26.72600 1.000 65.25519  ? 111 ARG A CD    1 
ATOM   842  N  NE    . ARG A 1 111 ? 48.84600 -2.54100  -28.14900 1.000 62.55224  ? 111 ARG A NE    1 
ATOM   843  C  CZ    . ARG A 1 111 ? 47.62300 -2.30700  -28.60500 1.000 72.23234  ? 111 ARG A CZ    1 
ATOM   844  N  NH1   . ARG A 1 111 ? 46.61000 -2.07600  -27.77900 1.000 75.21955  ? 111 ARG A NH1   1 
ATOM   845  N  NH2   . ARG A 1 111 ? 47.39800 -2.33800  -29.91600 1.000 77.28821  ? 111 ARG A NH2   1 
ATOM   846  N  N     . ILE A 1 112 ? 53.00100 -1.52400  -22.56700 1.000 58.98076  ? 112 ILE A N     1 
ATOM   847  C  CA    . ILE A 1 112 ? 53.38200 -1.48300  -21.15700 1.000 57.27002  ? 112 ILE A CA    1 
ATOM   848  C  C     . ILE A 1 112 ? 53.96100 -0.12400  -20.79200 1.000 60.06510  ? 112 ILE A C     1 
ATOM   849  O  O     . ILE A 1 112 ? 53.60000 0.47100   -19.76800 1.000 65.28941  ? 112 ILE A O     1 
ATOM   850  C  CB    . ILE A 1 112 ? 54.35700 -2.62300  -20.82400 1.000 54.04069  ? 112 ILE A CB    1 
ATOM   851  C  CG1   . ILE A 1 112 ? 53.65700 -3.97700  -20.93400 1.000 55.91197  ? 112 ILE A CG1   1 
ATOM   852  C  CG2   . ILE A 1 112 ? 54.93400 -2.43600  -19.43500 1.000 61.10469  ? 112 ILE A CG2   1 
ATOM   853  C  CD1   . ILE A 1 112 ? 54.60100 -5.14900  -20.84700 1.000 52.80633  ? 112 ILE A CD1   1 
ATOM   854  N  N     . LEU A 1 113 ? 54.91400 0.35700   -21.59300 1.000 57.38320  ? 113 LEU A N     1 
ATOM   855  C  CA    . LEU A 1 113 ? 55.50200 1.66600   -21.32300 1.000 55.41717  ? 113 LEU A CA    1 
ATOM   856  C  C     . LEU A 1 113 ? 54.45600 2.77400   -21.35300 1.000 64.48405  ? 113 LEU A C     1 
ATOM   857  O  O     . LEU A 1 113 ? 54.48200 3.68600   -20.51300 1.000 74.44577  ? 113 LEU A O     1 
ATOM   858  C  CB    . LEU A 1 113 ? 56.61700 1.96400   -22.32000 1.000 51.77989  ? 113 LEU A CB    1 
ATOM   859  C  CG    . LEU A 1 113 ? 57.86600 1.10200   -22.20300 1.000 50.75872  ? 113 LEU A CG    1 
ATOM   860  C  CD1   . LEU A 1 113 ? 58.72900 1.23200   -23.44200 1.000 56.63047  ? 113 LEU A CD1   1 
ATOM   861  C  CD2   . LEU A 1 113 ? 58.63800 1.55400   -20.97000 1.000 51.94833  ? 113 LEU A CD2   1 
ATOM   862  N  N     . ALA A 1 114 ? 53.52100 2.71400   -22.30900 1.000 60.82045  ? 114 ALA A N     1 
ATOM   863  C  CA    . ALA A 1 114 ? 52.45800 3.72000   -22.34300 1.000 65.95001  ? 114 ALA A CA    1 
ATOM   864  C  C     . ALA A 1 114 ? 51.58800 3.66300   -21.09300 1.000 71.54542  ? 114 ALA A C     1 
ATOM   865  O  O     . ALA A 1 114 ? 51.26200 4.70300   -20.49400 1.000 72.95085  ? 114 ALA A O     1 
ATOM   866  C  CB    . ALA A 1 114 ? 51.59400 3.52800   -23.58900 1.000 68.82667  ? 114 ALA A CB    1 
ATOM   867  N  N     . LYS A 1 115 ? 51.23000 2.45000   -20.66400 1.000 72.89821  ? 115 LYS A N     1 
ATOM   868  C  CA    . LYS A 1 115 ? 50.38600 2.31000   -19.48800 1.000 74.68001  ? 115 LYS A CA    1 
ATOM   869  C  C     . LYS A 1 115 ? 51.10900 2.82400   -18.24700 1.000 79.48321  ? 115 LYS A C     1 
ATOM   870  O  O     . LYS A 1 115 ? 50.48400 3.39800   -17.35400 1.000 85.18653  ? 115 LYS A O     1 
ATOM   871  C  CB    . LYS A 1 115 ? 50.01700 0.83200   -19.32600 1.000 69.63466  ? 115 LYS A CB    1 
ATOM   872  C  CG    . LYS A 1 115 ? 49.08000 0.42300   -18.19400 1.000 72.18760  ? 115 LYS A CG    1 
ATOM   873  C  CD    . LYS A 1 115 ? 47.68800 1.01400   -18.38100 1.000 76.88027  ? 115 LYS A CD    1 
ATOM   874  C  CE    . LYS A 1 115 ? 46.75000 0.62900   -17.24400 1.000 73.22457  ? 115 LYS A CE    1 
ATOM   875  N  NZ    . LYS A 1 115 ? 45.39100 0.24100   -17.73900 1.000 71.06642  ? 115 LYS A NZ    1 
ATOM   876  N  N     . GLN A 1 116 ? 52.42400 2.61400   -18.15500 1.000 81.30975  ? 116 GLN A N     1 
ATOM   877  C  CA    . GLN A 1 116 ? 53.14600 3.17500   -17.01500 1.000 81.34396  ? 116 GLN A CA    1 
ATOM   878  C  C     . GLN A 1 116 ? 53.20200 4.69600   -17.09300 1.000 83.34157  ? 116 GLN A C     1 
ATOM   879  O  O     . GLN A 1 116 ? 53.18000 5.37200   -16.05800 1.000 84.99177  ? 116 GLN A O     1 
ATOM   880  C  CB    . GLN A 1 116 ? 54.56900 2.62900   -16.92000 1.000 79.24371  ? 116 GLN A CB    1 
ATOM   881  C  CG    . GLN A 1 116 ? 54.68700 1.21600   -16.42100 1.000 80.39385  ? 116 GLN A CG    1 
ATOM   882  C  CD    . GLN A 1 116 ? 56.12700 0.72500   -16.40400 1.000 88.08425  ? 116 GLN A CD    1 
ATOM   883  O  OE1   . GLN A 1 116 ? 56.98900 1.27400   -17.11200 1.000 89.42914  ? 116 GLN A OE1   1 
ATOM   884  N  NE2   . GLN A 1 116 ? 56.36700 -0.39400  -15.72900 1.000 87.26309  ? 116 GLN A NE2   1 
ATOM   885  N  N     . LYS A 1 117 ? 53.30300 5.25400   -18.31200 1.000 78.24096  ? 117 LYS A N     1 
ATOM   886  C  CA    . LYS A 1 117 ? 53.38900 6.71100   -18.44400 1.000 80.10171  ? 117 LYS A CA    1 
ATOM   887  C  C     . LYS A 1 117 ? 52.10600 7.38600   -18.00200 1.000 77.77775  ? 117 LYS A C     1 
ATOM   888  O  O     . LYS A 1 117 ? 52.14500 8.39900   -17.29400 1.000 76.11965  ? 117 LYS A O     1 
ATOM   889  C  CB    . LYS A 1 117 ? 53.75400 7.16800   -19.86000 1.000 85.37603  ? 117 LYS A CB    1 
ATOM   890  C  CG    . LYS A 1 117 ? 53.75400 8.72300   -19.94500 1.000 90.05027  ? 117 LYS A CG    1 
ATOM   891  C  CD    . LYS A 1 117 ? 54.77800 9.36600   -19.00000 1.000 92.77165  ? 117 LYS A CD    1 
ATOM   892  C  CE    . LYS A 1 117 ? 54.84600 10.88300  -19.16300 1.000 90.05027  ? 117 LYS A CE    1 
ATOM   893  N  NZ    . LYS A 1 117 ? 55.36000 11.31800  -20.48200 1.000 85.92609  ? 117 LYS A NZ    1 
ATOM   894  N  N     . ILE A 1 118 ? 50.96300 6.80000   -18.34500 1.000 81.39397  ? 118 ILE A N     1 
ATOM   895  C  CA    . ILE A 1 118 ? 49.69800 7.44000   -18.00100 1.000 83.43632  ? 118 ILE A CA    1 
ATOM   896  C  C     . ILE A 1 118 ? 49.18700 7.01200   -16.62500 1.000 84.48381  ? 118 ILE A C     1 
ATOM   897  O  O     . ILE A 1 118 ? 48.52000 7.80100   -15.94800 1.000 86.29456  ? 118 ILE A O     1 
ATOM   898  C  CB    . ILE A 1 118 ? 48.66400 7.15500   -19.10500 1.000 80.62282  ? 118 ILE A CB    1 
ATOM   899  C  CG1   . ILE A 1 118 ? 48.28300 5.67500   -19.11600 1.000 79.82799  ? 118 ILE A CG1   1 
ATOM   900  C  CG2   . ILE A 1 118 ? 49.21200 7.55800   -20.47400 1.000 79.10685  ? 118 ILE A CG2   1 
ATOM   901  C  CD1   . ILE A 1 118 ? 47.35400 5.29900   -20.24100 1.000 72.45342  ? 118 ILE A CD1   1 
ATOM   902  N  N     . HIS A 1 119 ? 49.48000 5.79500   -16.17900 1.000 89.83446  ? 119 HIS A N     1 
ATOM   903  C  CA    . HIS A 1 119 ? 48.93100 5.27300   -14.92900 1.000 89.98974  ? 119 HIS A CA    1 
ATOM   904  C  C     . HIS A 1 119 ? 50.08400 4.77400   -14.07000 1.000 88.57115  ? 119 HIS A C     1 
ATOM   905  O  O     . HIS A 1 119 ? 50.24600 3.56700   -13.85400 1.000 86.59986  ? 119 HIS A O     1 
ATOM   906  C  CB    . HIS A 1 119 ? 47.87700 4.18700   -15.12700 1.000 89.18438  ? 119 HIS A CB    1 
ATOM   907  C  CG    . HIS A 1 119 ? 46.94300 4.07200   -13.96000 1.000 94.55081  ? 119 HIS A CG    1 
ATOM   908  N  ND1   . HIS A 1 119 ? 47.39600 3.95900   -12.66200 1.000 92.41898  ? 119 HIS A ND1   1 
ATOM   909  C  CD2   . HIS A 1 119 ? 45.59100 4.09400   -13.88400 1.000 98.21441  ? 119 HIS A CD2   1 
ATOM   910  C  CE1   . HIS A 1 119 ? 46.36500 3.89500   -11.84000 1.000 95.45618  ? 119 HIS A CE1   1 
ATOM   911  N  NE2   . HIS A 1 119 ? 45.25700 3.97500   -12.55500 1.000 101.00422 ? 119 HIS A NE2   1 
ATOM   912  N  N     . PRO A 1 120 ? 50.91800 5.69000   -13.57200 1.000 80.44912  ? 120 PRO A N     1 
ATOM   913  C  CA    . PRO A 1 120 ? 52.11600 5.26900   -12.83500 1.000 75.85910  ? 120 PRO A CA    1 
ATOM   914  C  C     . PRO A 1 120 ? 51.79000 4.63900   -11.49700 1.000 79.28582  ? 120 PRO A C     1 
ATOM   915  O  O     . PRO A 1 120 ? 52.61500 3.88600   -10.96700 1.000 82.09142  ? 120 PRO A O     1 
ATOM   916  C  CB    . PRO A 1 120 ? 52.90000 6.57500   -12.66900 1.000 72.18760  ? 120 PRO A CB    1 
ATOM   917  C  CG    . PRO A 1 120 ? 51.84400 7.61200   -12.62600 1.000 90.41347  ? 120 PRO A CG    1 
ATOM   918  C  CD    . PRO A 1 120 ? 50.76900 7.15400   -13.57700 1.000 87.89738  ? 120 PRO A CD    1 
ATOM   919  N  N     . GLU A 1 121 ? 50.62400 4.92500   -10.92700 1.000 78.97789  ? 121 GLU A N     1 
ATOM   920  C  CA    . GLU A 1 121 ? 50.28300 4.34900   -9.64000  1.000 81.16236  ? 121 GLU A CA    1 
ATOM   921  C  C     . GLU A 1 121 ? 49.76900 2.92000   -9.80500  1.000 82.03878  ? 121 GLU A C     1 
ATOM   922  O  O     . GLU A 1 121 ? 49.56600 2.41900   -10.91500 1.000 80.09381  ? 121 GLU A O     1 
ATOM   923  C  CB    . GLU A 1 121 ? 49.22600 5.19800   -8.93900  1.000 85.29181  ? 121 GLU A CB    1 
ATOM   924  C  CG    . GLU A 1 121 ? 49.59400 6.66400   -8.80900  1.000 97.20902  ? 121 GLU A CG    1 
ATOM   925  C  CD    . GLU A 1 121 ? 49.14600 7.25400   -7.48600  1.000 113.83207 ? 121 GLU A CD    1 
ATOM   926  O  OE1   . GLU A 1 121 ? 48.05700 6.87400   -7.00800  1.000 119.46432 ? 121 GLU A OE1   1 
ATOM   927  O  OE2   . GLU A 1 121 ? 49.88900 8.08200   -6.91400  1.000 115.97706 ? 121 GLU A OE2   1 
ATOM   928  N  N     . ARG A 1 122 ? 49.54800 2.26600   -8.66600  1.000 88.66326  ? 122 ARG A N     1 
ATOM   929  C  CA    . ARG A 1 122 ? 49.14000 0.86700   -8.65500  1.000 86.97095  ? 122 ARG A CA    1 
ATOM   930  C  C     . ARG A 1 122 ? 47.78100 0.71200   -9.32400  1.000 87.72104  ? 122 ARG A C     1 
ATOM   931  O  O     . ARG A 1 122 ? 46.83900 1.44900   -9.01800  1.000 90.06606  ? 122 ARG A O     1 
ATOM   932  C  CB    . ARG A 1 122 ? 49.08300 0.34200   -7.21900  1.000 87.39732  ? 122 ARG A CB    1 
ATOM   933  C  CG    . ARG A 1 122 ? 48.80300 -1.15600  -7.10700  1.000 88.62115  ? 122 ARG A CG    1 
ATOM   934  C  CD    . ARG A 1 122 ? 48.85300 -1.63600  -5.65800  1.000 91.49255  ? 122 ARG A CD    1 
ATOM   935  N  NE    . ARG A 1 122 ? 50.18700 -1.55700  -5.07400  1.000 97.87752  ? 122 ARG A NE    1 
ATOM   936  C  CZ    . ARG A 1 122 ? 51.10400 -2.51200  -5.16200  1.000 90.64771  ? 122 ARG A CZ    1 
ATOM   937  N  NH1   . ARG A 1 122 ? 50.86000 -3.64800  -5.79400  1.000 83.33104  ? 122 ARG A NH1   1 
ATOM   938  N  NH2   . ARG A 1 122 ? 52.29400 -2.32200  -4.59900  1.000 89.33176  ? 122 ARG A NH2   1 
ATOM   939  N  N     . THR A 1 123 ? 47.68500 -0.23100  -10.25400 1.000 84.19957  ? 123 THR A N     1 
ATOM   940  C  CA    . THR A 1 123 ? 46.43700 -0.49200  -10.95800 1.000 76.56971  ? 123 THR A CA    1 
ATOM   941  C  C     . THR A 1 123 ? 45.67000 -1.60200  -10.25600 1.000 74.40892  ? 123 THR A C     1 
ATOM   942  O  O     . THR A 1 123 ? 46.20800 -2.30100  -9.39300  1.000 80.51755  ? 123 THR A O     1 
ATOM   943  C  CB    . THR A 1 123 ? 46.73600 -0.88200  -12.40600 1.000 70.26632  ? 123 THR A CB    1 
ATOM   944  O  OG1   . THR A 1 123 ? 47.55000 -2.06300  -12.42900 1.000 63.50498  ? 123 THR A OG1   1 
ATOM   945  C  CG2   . THR A 1 123 ? 47.48400 0.24200   -13.11200 1.000 79.71745  ? 123 THR A CG2   1 
ATOM   946  N  N     . PRO A 1 124 ? 44.38700 -1.79100  -10.58500 1.000 69.54781  ? 124 PRO A N     1 
ATOM   947  C  CA    . PRO A 1 124 ? 43.66600 -2.95300  -10.04200 1.000 66.43691  ? 124 PRO A CA    1 
ATOM   948  C  C     . PRO A 1 124 ? 44.24000 -4.28500  -10.49800 1.000 76.25651  ? 124 PRO A C     1 
ATOM   949  O  O     . PRO A 1 124 ? 43.94900 -5.31500  -9.87900  1.000 77.03029  ? 124 PRO A O     1 
ATOM   950  C  CB    . PRO A 1 124 ? 42.23400 -2.75300  -10.55600 1.000 66.92645  ? 124 PRO A CB    1 
ATOM   951  C  CG    . PRO A 1 124 ? 42.37100 -1.82300  -11.71600 1.000 71.09010  ? 124 PRO A CG    1 
ATOM   952  C  CD    . PRO A 1 124 ? 43.49300 -0.90700  -11.34900 1.000 70.17420  ? 124 PRO A CD    1 
ATOM   953  N  N     . SER A 1 125 ? 45.03900 -4.29700  -11.56600 1.000 74.83266  ? 125 SER A N     1 
ATOM   954  C  CA    . SER A 1 125 ? 45.72400 -5.50400  -12.00900 1.000 64.26560  ? 125 SER A CA    1 
ATOM   955  C  C     . SER A 1 125 ? 46.89500 -5.87500  -11.11000 1.000 65.52101  ? 125 SER A C     1 
ATOM   956  O  O     . SER A 1 125 ? 47.43500 -6.97700  -11.24600 1.000 72.00074  ? 125 SER A O     1 
ATOM   957  C  CB    . SER A 1 125 ? 46.20600 -5.32000  -13.44800 1.000 63.57078  ? 125 SER A CB    1 
ATOM   958  O  OG    . SER A 1 125 ? 45.13300 -4.93400  -14.29000 1.000 66.58956  ? 125 SER A OG    1 
ATOM   959  N  N     . GLU A 1 126 ? 47.29800 -4.98500  -10.20700 1.000 64.06821  ? 126 GLU A N     1 
ATOM   960  C  CA    . GLU A 1 126 ? 48.50800 -5.14600  -9.41300  1.000 64.58406  ? 126 GLU A CA    1 
ATOM   961  C  C     . GLU A 1 126 ? 48.13700 -5.17300  -7.93900  1.000 74.87740  ? 126 GLU A C     1 
ATOM   962  O  O     . GLU A 1 126 ? 48.76600 -4.49500  -7.12000  1.000 80.60703  ? 126 GLU A O     1 
ATOM   963  C  CB    . GLU A 1 126 ? 49.49200 -4.01200  -9.68400  1.000 67.25017  ? 126 GLU A CB    1 
ATOM   964  C  CG    . GLU A 1 126 ? 49.88900 -3.85200  -11.13300 1.000 70.66900  ? 126 GLU A CG    1 
ATOM   965  C  CD    . GLU A 1 126 ? 50.57500 -2.52400  -11.38800 1.000 73.71147  ? 126 GLU A CD    1 
ATOM   966  O  OE1   . GLU A 1 126 ? 49.90100 -1.47600  -11.27800 1.000 77.38823  ? 126 GLU A OE1   1 
ATOM   967  O  OE2   . GLU A 1 126 ? 51.78700 -2.52500  -11.69000 1.000 75.00373  ? 126 GLU A OE2   1 
ATOM   968  N  N     . LYS A 1 127 ? 47.11300 -5.95400  -7.59300  1.000 72.85610  ? 127 LYS A N     1 
ATOM   969  C  CA    . LYS A 1 127 ? 46.66300 -6.00800  -6.20700  1.000 72.59555  ? 127 LYS A CA    1 
ATOM   970  C  C     . LYS A 1 127 ? 47.70600 -6.64800  -5.30000  1.000 71.48489  ? 127 LYS A C     1 
ATOM   971  O  O     . LYS A 1 127 ? 47.88900 -6.21900  -4.15500  1.000 80.09908  ? 127 LYS A O     1 
ATOM   972  C  CB    . LYS A 1 127 ? 45.35000 -6.79300  -6.14900  1.000 78.88577  ? 127 LYS A CB    1 
ATOM   973  C  CG    . LYS A 1 127 ? 44.16200 -6.04200  -6.74000  1.000 79.97275  ? 127 LYS A CG    1 
ATOM   974  C  CD    . LYS A 1 127 ? 42.88400 -6.87900  -6.76500  1.000 85.55236  ? 127 LYS A CD    1 
ATOM   975  C  CE    . LYS A 1 127 ? 42.74000 -7.63900  -8.09000  1.000 88.58957  ? 127 LYS A CE    1 
ATOM   976  N  NZ    . LYS A 1 127 ? 41.33100 -7.67000  -8.58800  1.000 80.75705  ? 127 LYS A NZ    1 
ATOM   977  N  N     . LEU A 1 128 ? 48.41100 -7.65900  -5.79900  1.000 73.23510  ? 128 LEU A N     1 
ATOM   978  C  CA    . LEU A 1 128 ? 49.42000 -8.36900  -5.02900  1.000 70.13472  ? 128 LEU A CA    1 
ATOM   979  C  C     . LEU A 1 128 ? 50.83200 -8.22000  -5.56800  1.000 65.60523  ? 128 LEU A C     1 
ATOM   980  O  O     . LEU A 1 128 ? 51.78700 -8.38400  -4.80000  1.000 70.65058  ? 128 LEU A O     1 
ATOM   981  C  CB    . LEU A 1 128 ? 49.07600 -9.86300  -4.96000  1.000 69.59519  ? 128 LEU A CB    1 
ATOM   982  C  CG    . LEU A 1 128 ? 47.84900 -10.18100 -4.10700  1.000 80.20435  ? 128 LEU A CG    1 
ATOM   983  C  CD1   . LEU A 1 128 ? 47.59300 -11.67300 -4.10200  1.000 84.48645  ? 128 LEU A CD1   1 
ATOM   984  C  CD2   . LEU A 1 128 ? 48.04600 -9.66700  -2.69000  1.000 79.39373  ? 128 LEU A CD2   1 
ATOM   985  N  N     . LEU A 1 129 ? 50.99000 -7.91700  -6.85200  1.000 61.10996  ? 129 LEU A N     1 
ATOM   986  C  CA    . LEU A 1 129 ? 52.29900 -7.80600  -7.47600  1.000 63.88398  ? 129 LEU A CA    1 
ATOM   987  C  C     . LEU A 1 129 ? 52.27400 -6.72900  -8.54500  1.000 71.15064  ? 129 LEU A C     1 
ATOM   988  O  O     . LEU A 1 129 ? 51.41300 -6.75000  -9.42700  1.000 72.26919  ? 129 LEU A O     1 
ATOM   989  C  CB    . LEU A 1 129 ? 52.72100 -9.14400  -8.08900  1.000 62.75226  ? 129 LEU A CB    1 
ATOM   990  C  CG    . LEU A 1 129 ? 54.08800 -9.17000  -8.77200  1.000 64.93410  ? 129 LEU A CG    1 
ATOM   991  C  CD1   . LEU A 1 129 ? 55.18900 -8.87000  -7.76800  1.000 71.49541  ? 129 LEU A CD1   1 
ATOM   992  C  CD2   . LEU A 1 129 ? 54.32500 -10.50600 -9.46900  1.000 64.38140  ? 129 LEU A CD2   1 
ATOM   993  N  N     . ALA A 1 130 ? 53.20900 -5.79100  -8.45900  1.000 72.94032  ? 130 ALA A N     1 
ATOM   994  C  CA    . ALA A 1 130 ? 53.27000 -4.72000  -9.43700  1.000 75.48800  ? 130 ALA A CA    1 
ATOM   995  C  C     . ALA A 1 130 ? 54.23700 -5.08400  -10.56100 1.000 75.56696  ? 130 ALA A C     1 
ATOM   996  O  O     . ALA A 1 130 ? 55.15200 -5.89400  -10.39300 1.000 74.82213  ? 130 ALA A O     1 
ATOM   997  C  CB    . ALA A 1 130 ? 53.70700 -3.40900  -8.77900  1.000 78.30939  ? 130 ALA A CB    1 
ATOM   998  N  N     . VAL A 1 131 ? 54.00800 -4.46400  -11.72200 1.000 71.47962  ? 131 VAL A N     1 
ATOM   999  C  CA    . VAL A 1 131 ? 54.83400 -4.70600  -12.90400 1.000 68.66350  ? 131 VAL A CA    1 
ATOM   1000 C  C     . VAL A 1 131 ? 56.29800 -4.40800  -12.61000 1.000 71.44804  ? 131 VAL A C     1 
ATOM   1001 O  O     . VAL A 1 131 ? 57.19600 -5.16400  -13.00500 1.000 72.14549  ? 131 VAL A O     1 
ATOM   1002 C  CB    . VAL A 1 131 ? 54.31100 -3.87800  -14.09500 1.000 67.26596  ? 131 VAL A CB    1 
ATOM   1003 C  CG1   . VAL A 1 131 ? 55.27500 -3.95600  -15.26700 1.000 58.44122  ? 131 VAL A CG1   1 
ATOM   1004 C  CG2   . VAL A 1 131 ? 52.93300 -4.36800  -14.51000 1.000 65.51049  ? 131 VAL A CG2   1 
ATOM   1005 N  N     . LYS A 1 132 ? 56.56000 -3.30700  -11.90400 1.000 69.97418  ? 132 LYS A N     1 
ATOM   1006 C  CA    . LYS A 1 132 ? 57.92500 -2.92100  -11.57200 1.000 70.46898  ? 132 LYS A CA    1 
ATOM   1007 C  C     . LYS A 1 132 ? 58.62300 -3.94000  -10.68100 1.000 74.47209  ? 132 LYS A C     1 
ATOM   1008 O  O     . LYS A 1 132 ? 59.85800 -3.99400  -10.67100 1.000 73.95624  ? 132 LYS A O     1 
ATOM   1009 C  CB    . LYS A 1 132 ? 57.90800 -1.54900  -10.89400 1.000 75.91700  ? 132 LYS A CB    1 
ATOM   1010 C  CG    . LYS A 1 132 ? 59.27500 -0.92500  -10.68400 1.000 90.34241  ? 132 LYS A CG    1 
ATOM   1011 C  CD    . LYS A 1 132 ? 59.18300 0.32400   -9.82000  1.000 93.26381  ? 132 LYS A CD    1 
ATOM   1012 C  CE    . LYS A 1 132 ? 60.55500 0.94300   -9.58400  1.000 94.22182  ? 132 LYS A CE    1 
ATOM   1013 N  NZ    . LYS A 1 132 ? 60.46000 2.21600   -8.81000  1.000 95.90624  ? 132 LYS A NZ    1 
ATOM   1014 N  N     . GLU A 1 133 ? 57.85900 -4.77700  -9.94900  1.000 78.53573  ? 133 GLU A N     1 
ATOM   1015 C  CA    . GLU A 1 133 ? 58.43800 -5.81400  -9.10700  1.000 76.50917  ? 133 GLU A CA    1 
ATOM   1016 C  C     . GLU A 1 133 ? 58.68900 -7.12200  -9.84900  1.000 72.01390  ? 133 GLU A C     1 
ATOM   1017 O  O     . GLU A 1 133 ? 59.15000 -8.08100  -9.22800  1.000 71.93494  ? 133 GLU A O     1 
ATOM   1018 C  CB    . GLU A 1 133 ? 57.53300 -6.11100  -7.90600  1.000 79.40689  ? 133 GLU A CB    1 
ATOM   1019 C  CG    . GLU A 1 133 ? 57.54900 -5.08200  -6.79100  1.000 89.54495  ? 133 GLU A CG    1 
ATOM   1020 C  CD    . GLU A 1 133 ? 56.44600 -5.31700  -5.76600  1.000 89.99763  ? 133 GLU A CD    1 
ATOM   1021 O  OE1   . GLU A 1 133 ? 55.25400 -5.20200  -6.12500  1.000 86.94464  ? 133 GLU A OE1   1 
ATOM   1022 O  OE2   . GLU A 1 133 ? 56.77300 -5.63000  -4.59900  1.000 83.74162  ? 133 GLU A OE2   1 
ATOM   1023 N  N     . PHE A 1 134 ? 58.41300 -7.17900  -11.15900 1.000 66.16056  ? 134 PHE A N     1 
ATOM   1024 C  CA    . PHE A 1 134 ? 58.61200 -8.41300  -11.91700 1.000 68.85299  ? 134 PHE A CA    1 
ATOM   1025 C  C     . PHE A 1 134 ? 60.05200 -8.92800  -11.86400 1.000 72.55607  ? 134 PHE A C     1 
ATOM   1026 O  O     . PHE A 1 134 ? 61.01200 -8.15900  -11.80000 1.000 76.59603  ? 134 PHE A O     1 
ATOM   1027 C  CB    . PHE A 1 134 ? 58.22600 -8.19300  -13.38300 1.000 66.26058  ? 134 PHE A CB    1 
ATOM   1028 C  CG    . PHE A 1 134 ? 56.76600 -8.35300  -13.66300 1.000 61.96796  ? 134 PHE A CG    1 
ATOM   1029 C  CD1   . PHE A 1 134 ? 55.90800 -8.84400  -12.69600 1.000 68.25818  ? 134 PHE A CD1   1 
ATOM   1030 C  CD2   . PHE A 1 134 ? 56.25600 -8.03800  -14.91400 1.000 67.97657  ? 134 PHE A CD2   1 
ATOM   1031 C  CE1   . PHE A 1 134 ? 54.56100 -9.01200  -12.96200 1.000 68.12922  ? 134 PHE A CE1   1 
ATOM   1032 C  CE2   . PHE A 1 134 ? 54.90900 -8.20000  -15.19000 1.000 74.24574  ? 134 PHE A CE2   1 
ATOM   1033 C  CZ    . PHE A 1 134 ? 54.05800 -8.68800  -14.21000 1.000 66.87381  ? 134 PHE A CZ    1 
ATOM   1034 N  N     . GLU A 1 135 ? 60.15100 -10.26100 -11.95600 1.000 84.71805  ? 135 GLU A N     1 
ATOM   1035 C  CA    . GLU A 1 135 ? 61.48100 -10.91200 -12.01200 1.000 85.24180  ? 135 GLU A CA    1 
ATOM   1036 C  C     . GLU A 1 135 ? 61.97300 -10.81500 -13.45400 1.000 84.64173  ? 135 GLU A C     1 
ATOM   1037 O  O     . GLU A 1 135 ? 61.16600 -11.07400 -14.36900 1.000 83.39158  ? 135 GLU A O     1 
ATOM   1038 C  CB    . GLU A 1 135 ? 61.38000 -12.37500 -11.57700 1.000 90.15818  ? 135 GLU A CB    1 
ATOM   1039 C  CG    . GLU A 1 135 ? 62.71700 -13.09600 -11.53700 1.000 95.18773  ? 135 GLU A CG    1 
ATOM   1040 C  CD    . GLU A 1 135 ? 63.71400 -12.58500 -10.50900 1.000 113.41623 ? 135 GLU A CD    1 
ATOM   1041 O  OE1   . GLU A 1 135 ? 63.40900 -12.66700 -9.30200  1.000 107.74187 ? 135 GLU A OE1   1 
ATOM   1042 O  OE2   . GLU A 1 135 ? 64.79900 -12.11900 -10.91500 1.000 116.42975 ? 135 GLU A OE2   1 
ATOM   1043 N  N     . SER A 1 136 ? 63.24100 -10.46800 -13.64400 1.000 75.61959  ? 136 SER A N     1 
ATOM   1044 C  CA    . SER A 1 136 ? 63.82400 -10.28000 -14.96500 1.000 78.26202  ? 136 SER A CA    1 
ATOM   1045 C  C     . SER A 1 136 ? 64.78600 -11.37100 -15.40800 1.000 74.44840  ? 136 SER A C     1 
ATOM   1046 O  O     . SER A 1 136 ? 64.85400 -11.65500 -16.60500 1.000 71.58227  ? 136 SER A O     1 
ATOM   1047 C  CB    . SER A 1 136 ? 64.55900 -8.93800  -15.02900 1.000 75.05900  ? 136 SER A CB    1 
ATOM   1048 O  OG    . SER A 1 136 ? 65.76100 -8.98400  -14.28200 1.000 77.61720  ? 136 SER A OG    1 
ATOM   1049 N  N     . HIS A 1 137 ? 65.52300 -11.98800 -14.48100 1.000 76.63550  ? 137 HIS A N     1 
ATOM   1050 C  CA    . HIS A 1 137 ? 66.60100 -12.93100 -14.80500 1.000 81.93614  ? 137 HIS A CA    1 
ATOM   1051 C  C     . HIS A 1 137 ? 67.64000 -12.31800 -15.74800 1.000 82.83888  ? 137 HIS A C     1 
ATOM   1052 O  O     . HIS A 1 137 ? 68.17500 -12.98500 -16.63600 1.000 86.01558  ? 137 HIS A O     1 
ATOM   1053 C  CB    . HIS A 1 137 ? 66.02300 -14.21500 -15.39800 1.000 83.83374  ? 137 HIS A CB    1 
ATOM   1054 C  CG    . HIS A 1 137 ? 65.23800 -15.01700 -14.41400 1.000 85.96031  ? 137 HIS A CG    1 
ATOM   1055 N  ND1   . HIS A 1 137 ? 64.46600 -16.09700 -14.78000 1.000 85.44972  ? 137 HIS A ND1   1 
ATOM   1056 C  CD2   . HIS A 1 137 ? 65.09300 -14.88500 -13.07400 1.000 85.69975  ? 137 HIS A CD2   1 
ATOM   1057 C  CE1   . HIS A 1 137 ? 63.88700 -16.60300 -13.70700 1.000 88.03950  ? 137 HIS A CE1   1 
ATOM   1058 N  NE2   . HIS A 1 137 ? 64.25000 -15.88600 -12.65900 1.000 91.43728  ? 137 HIS A NE2   1 
ATOM   1059 N  N     . LEU A 1 138 ? 67.91200 -11.02500 -15.55000 1.000 83.36263  ? 138 LEU A N     1 
ATOM   1060 C  CA    . LEU A 1 138 ? 68.88400 -10.29500 -16.36300 1.000 89.76339  ? 138 LEU A CA    1 
ATOM   1061 C  C     . LEU A 1 138 ? 70.26000 -10.95800 -16.37600 1.000 93.88494  ? 138 LEU A C     1 
ATOM   1062 O  O     . LEU A 1 138 ? 70.85500 -11.18000 -17.43800 1.000 92.83745  ? 138 LEU A O     1 
ATOM   1063 C  CB    . LEU A 1 138 ? 69.00800 -8.87200  -15.81600 1.000 82.90468  ? 138 LEU A CB    1 
ATOM   1064 C  CG    . LEU A 1 138 ? 69.76400 -7.82400  -16.62200 1.000 88.77380  ? 138 LEU A CG    1 
ATOM   1065 C  CD1   . LEU A 1 138 ? 69.18300 -7.74000  -18.01500 1.000 80.97550  ? 138 LEU A CD1   1 
ATOM   1066 C  CD2   . LEU A 1 138 ? 69.72200 -6.47700  -15.91300 1.000 91.46360  ? 138 LEU A CD2   1 
ATOM   1067 N  N     . ASP A 1 139 ? 70.77000 -11.28800 -15.18600 1.000 99.01977  ? 139 ASP A N     1 
ATOM   1068 C  CA    . ASP A 1 139 ? 72.09200 -11.88600 -14.99400 1.000 101.38847 ? 139 ASP A CA    1 
ATOM   1069 C  C     . ASP A 1 139 ? 72.25700 -13.26000 -15.63100 1.000 101.62534 ? 139 ASP A C     1 
ATOM   1070 O  O     . ASP A 1 139 ? 73.39400 -13.70200 -15.83200 1.000 103.77034 ? 139 ASP A O     1 
ATOM   1071 C  CB    . ASP A 1 139 ? 72.41000 -11.96700 -13.50100 1.000 102.73863 ? 139 ASP A CB    1 
ATOM   1072 C  CG    . ASP A 1 139 ? 71.35400 -12.72100 -12.71600 1.000 106.50751 ? 139 ASP A CG    1 
ATOM   1073 O  OD1   . ASP A 1 139 ? 70.18700 -12.75600 -13.16700 1.000 107.73134 ? 139 ASP A OD1   1 
ATOM   1074 O  OD2   . ASP A 1 139 ? 71.69300 -13.27500 -11.64700 1.000 102.89918 ? 139 ASP A OD2   1 
ATOM   1075 N  N     . LYS A 1 140 ? 71.16800 -13.93600 -15.97000 1.000 96.65633  ? 140 LYS A N     1 
ATOM   1076 C  CA    . LYS A 1 140 ? 71.25500 -15.27200 -16.53800 1.000 95.24563  ? 140 LYS A CA    1 
ATOM   1077 C  C     . LYS A 1 140 ? 71.39000 -15.25300 -18.05000 1.000 97.58802  ? 140 LYS A C     1 
ATOM   1078 O  O     . LYS A 1 140 ? 71.84000 -16.24500 -18.63600 1.000 98.99871  ? 140 LYS A O     1 
ATOM   1079 C  CB    . LYS A 1 140 ? 70.02600 -16.08900 -16.12600 1.000 88.98699  ? 140 LYS A CB    1 
ATOM   1080 C  CG    . LYS A 1 140 ? 69.80100 -16.11500 -14.60800 1.000 88.20005  ? 140 LYS A CG    1 
ATOM   1081 C  CD    . LYS A 1 140 ? 68.67000 -17.04900 -14.18400 1.000 81.06498  ? 140 LYS A CD    1 
ATOM   1082 C  CE    . LYS A 1 140 ? 68.27200 -16.83200 -12.72400 1.000 77.76985  ? 140 LYS A CE    1 
ATOM   1083 N  NZ    . LYS A 1 140 ? 69.36300 -17.18700 -11.76900 1.000 87.27889  ? 140 LYS A NZ    1 
ATOM   1084 N  N     . LEU A 1 141 ? 70.98700 -14.16400 -18.68900 1.000 97.16428  ? 141 LEU A N     1 
ATOM   1085 C  CA    . LEU A 1 141 ? 70.99300 -14.09900 -20.14000 1.000 100.24360 ? 141 LEU A CA    1 
ATOM   1086 C  C     . LEU A 1 141 ? 72.41000 -14.24300 -20.69300 1.000 109.52892 ? 141 LEU A C     1 
ATOM   1087 O  O     . LEU A 1 141 ? 73.33600 -13.54800 -20.25900 1.000 105.53371 ? 141 LEU A O     1 
ATOM   1088 C  CB    . LEU A 1 141 ? 70.41700 -12.75000 -20.55700 1.000 96.42735  ? 141 LEU A CB    1 
ATOM   1089 C  CG    . LEU A 1 141 ? 69.00600 -12.42000 -20.07600 1.000 89.61864  ? 141 LEU A CG    1 
ATOM   1090 C  CD1   . LEU A 1 141 ? 68.65300 -11.03200 -20.53100 1.000 88.59220  ? 141 LEU A CD1   1 
ATOM   1091 C  CD2   . LEU A 1 141 ? 68.00500 -13.42600 -20.59900 1.000 89.31860  ? 141 LEU A CD2   1 
ATOM   1092 N  N     . ASP A 1 142 ? 72.58100 -15.16200 -21.64100 1.000 131.28416 ? 142 ASP A N     1 
ATOM   1093 C  CA    . ASP A 1 142 ? 73.82300 -15.28400 -22.38800 1.000 133.79762 ? 142 ASP A CA    1 
ATOM   1094 C  C     . ASP A 1 142 ? 73.85200 -14.23800 -23.50100 1.000 133.68182 ? 142 ASP A C     1 
ATOM   1095 O  O     . ASP A 1 142 ? 72.89700 -13.48200 -23.70000 1.000 131.66579 ? 142 ASP A O     1 
ATOM   1096 C  CB    . ASP A 1 142 ? 74.01600 -16.70600 -22.92100 1.000 135.01092 ? 142 ASP A CB    1 
ATOM   1097 C  CG    . ASP A 1 142 ? 72.92900 -17.13700 -23.89800 1.000 133.26071 ? 142 ASP A CG    1 
ATOM   1098 O  OD1   . ASP A 1 142 ? 72.14000 -16.29400 -24.37500 1.000 131.25258 ? 142 ASP A OD1   1 
ATOM   1099 O  OD2   . ASP A 1 142 ? 72.91000 -18.33400 -24.24300 1.000 134.58193 ? 142 ASP A OD2   1 
ATOM   1100 N  N     . ASN A 1 143 ? 74.96400 -14.18000 -24.23700 1.000 106.13641 ? 143 ASN A N     1 
ATOM   1101 C  CA    . ASN A 1 143 ? 75.10000 -13.14200 -25.25300 1.000 104.19670 ? 143 ASN A CA    1 
ATOM   1102 C  C     . ASN A 1 143 ? 74.06000 -13.30000 -26.36000 1.000 99.63563  ? 143 ASN A C     1 
ATOM   1103 O  O     . ASN A 1 143 ? 73.56700 -12.30200 -26.89100 1.000 103.08341 ? 143 ASN A O     1 
ATOM   1104 C  CB    . ASN A 1 143 ? 76.51400 -13.13600 -25.82900 1.000 104.68097 ? 143 ASN A CB    1 
ATOM   1105 C  CG    . ASN A 1 143 ? 77.53400 -12.58700 -24.84900 1.000 102.32543 ? 143 ASN A CG    1 
ATOM   1106 O  OD1   . ASN A 1 143 ? 77.18600 -11.89700 -23.88900 1.000 99.60668  ? 143 ASN A OD1   1 
ATOM   1107 N  ND2   . ASN A 1 143 ? 78.80700 -12.87000 -25.10500 1.000 98.40127  ? 143 ASN A ND2   1 
ATOM   1108 N  N     . GLU A 1 144 ? 73.74300 -14.53900 -26.75300 1.000 95.53777  ? 144 GLU A N     1 
ATOM   1109 C  CA    . GLU A 1 144 ? 72.71900 -14.76100 -27.77700 1.000 97.00637  ? 144 GLU A CA    1 
ATOM   1110 C  C     . GLU A 1 144 ? 71.37200 -14.18000 -27.35100 1.000 95.55883  ? 144 GLU A C     1 
ATOM   1111 O  O     . GLU A 1 144 ? 70.70400 -13.47000 -28.11800 1.000 93.33487  ? 144 GLU A O     1 
ATOM   1112 C  CB    . GLU A 1 144 ? 72.56600 -16.26100 -28.03700 1.000 100.53574 ? 144 GLU A CB    1 
ATOM   1113 C  CG    . GLU A 1 144 ? 73.85500 -17.02900 -28.28000 1.000 109.37890 ? 144 GLU A CG    1 
ATOM   1114 C  CD    . GLU A 1 144 ? 73.62000 -18.53200 -28.32900 1.000 111.37125 ? 144 GLU A CD    1 
ATOM   1115 O  OE1   . GLU A 1 144 ? 72.56700 -18.98100 -27.82500 1.000 115.13223 ? 144 GLU A OE1   1 
ATOM   1116 O  OE2   . GLU A 1 144 ? 74.47900 -19.26300 -28.86800 1.000 106.15220 ? 144 GLU A OE2   1 
ATOM   1117 N  N     . LYS A 1 145 ? 70.97800 -14.45300 -26.10400 1.000 99.06714  ? 145 LYS A N     1 
ATOM   1118 C  CA    . LYS A 1 145 ? 69.72900 -13.93200 -25.55600 1.000 93.14275  ? 145 LYS A CA    1 
ATOM   1119 C  C     . LYS A 1 145 ? 69.77000 -12.41600 -25.46800 1.000 90.82931  ? 145 LYS A C     1 
ATOM   1120 O  O     . LYS A 1 145 ? 68.80100 -11.73200 -25.82600 1.000 84.83912  ? 145 LYS A O     1 
ATOM   1121 C  CB    . LYS A 1 145 ? 69.45300 -14.55700 -24.18900 1.000 104.47568 ? 145 LYS A CB    1 
ATOM   1122 C  CG    . LYS A 1 145 ? 69.01100 -16.01200 -24.28800 1.000 108.46037 ? 145 LYS A CG    1 
ATOM   1123 C  CD    . LYS A 1 145 ? 68.89000 -16.67600 -22.93000 1.000 104.74151 ? 145 LYS A CD    1 
ATOM   1124 C  CE    . LYS A 1 145 ? 68.25800 -18.05900 -23.05800 1.000 85.55236  ? 145 LYS A CE    1 
ATOM   1125 N  NZ    . LYS A 1 145 ? 67.11200 -18.09700 -24.01000 1.000 75.29324  ? 145 LYS A NZ    1 
ATOM   1126 N  N     . LYS A 1 146 ? 70.89000 -11.88100 -24.97700 1.000 98.11703  ? 146 LYS A N     1 
ATOM   1127 C  CA    . LYS A 1 146 ? 71.06200 -10.43900 -24.88100 1.000 85.19969  ? 146 LYS A CA    1 
ATOM   1128 C  C     . LYS A 1 146 ? 70.91100 -9.79500  -26.24900 1.000 81.82034  ? 146 LYS A C     1 
ATOM   1129 O  O     . LYS A 1 146 ? 70.32000 -8.71900  -26.37300 1.000 83.58107  ? 146 LYS A O     1 
ATOM   1130 C  CB    . LYS A 1 146 ? 72.45700 -10.13700 -24.33500 1.000 85.95767  ? 146 LYS A CB    1 
ATOM   1131 C  CG    . LYS A 1 146 ? 72.69900 -10.46900 -22.87800 1.000 91.94260  ? 146 LYS A CG    1 
ATOM   1132 C  CD    . LYS A 1 146 ? 74.06800 -9.95400  -22.44600 1.000 96.23785  ? 146 LYS A CD    1 
ATOM   1133 C  CE    . LYS A 1 146 ? 74.40500 -10.37900 -21.02600 1.000 90.57402  ? 146 LYS A CE    1 
ATOM   1134 N  NZ    . LYS A 1 146 ? 73.51700 -9.72600  -20.01800 1.000 85.06283  ? 146 LYS A NZ    1 
ATOM   1135 N  N     . ASP A 1 147 ? 71.47300 -10.42300 -27.28400 1.000 82.70992  ? 147 ASP A N     1 
ATOM   1136 C  CA    . ASP A 1 147 ? 71.40900 -9.84600  -28.62000 1.000 83.03890  ? 147 ASP A CA    1 
ATOM   1137 C  C     . ASP A 1 147 ? 70.01000 -9.93700  -29.21600 1.000 81.77033  ? 147 ASP A C     1 
ATOM   1138 O  O     . ASP A 1 147 ? 69.60000 -9.04700  -29.97200 1.000 83.30736  ? 147 ASP A O     1 
ATOM   1139 C  CB    . ASP A 1 147 ? 72.40500 -10.56600 -29.53200 1.000 91.53992  ? 147 ASP A CB    1 
ATOM   1140 C  CG    . ASP A 1 147 ? 73.84800 -10.24400 -29.19000 1.000 103.74665 ? 147 ASP A CG    1 
ATOM   1141 O  OD1   . ASP A 1 147 ? 74.09600 -9.16700  -28.60600 1.000 101.80168 ? 147 ASP A OD1   1 
ATOM   1142 O  OD2   . ASP A 1 147 ? 74.73800 -11.05700 -29.52600 1.000 110.46851 ? 147 ASP A OD2   1 
ATOM   1143 N  N     . LEU A 1 148 ? 69.24600 -10.96700 -28.85100 1.000 82.54148  ? 148 LEU A N     1 
ATOM   1144 C  CA    . LEU A 1 148 ? 67.84300 -11.01600 -29.26100 1.000 78.14358  ? 148 LEU A CA    1 
ATOM   1145 C  C     . LEU A 1 148 ? 67.02900 -9.90900  -28.59300 1.000 72.78241  ? 148 LEU A C     1 
ATOM   1146 O  O     . LEU A 1 148 ? 66.18300 -9.25800  -29.23200 1.000 77.49087  ? 148 LEU A O     1 
ATOM   1147 C  CB    . LEU A 1 148 ? 67.26900 -12.38700 -28.92900 1.000 79.20160  ? 148 LEU A CB    1 
ATOM   1148 C  CG    . LEU A 1 148 ? 67.74700 -13.51900 -29.83500 1.000 77.98567  ? 148 LEU A CG    1 
ATOM   1149 C  CD1   . LEU A 1 148 ? 67.25500 -14.86000 -29.30900 1.000 74.44050  ? 148 LEU A CD1   1 
ATOM   1150 C  CD2   . LEU A 1 148 ? 67.28300 -13.28700 -31.26800 1.000 77.55140  ? 148 LEU A CD2   1 
ATOM   1151 N  N     . ILE A 1 149 ? 67.26400 -9.69500  -27.29700 1.000 70.13999  ? 149 ILE A N     1 
ATOM   1152 C  CA    . ILE A 1 149 ? 66.60800 -8.60400  -26.58400 1.000 68.77667  ? 149 ILE A CA    1 
ATOM   1153 C  C     . ILE A 1 149 ? 66.99700 -7.26300  -27.19500 1.000 71.90336  ? 149 ILE A C     1 
ATOM   1154 O  O     . ILE A 1 149 ? 66.17400 -6.34500  -27.30000 1.000 77.63299  ? 149 ILE A O     1 
ATOM   1155 C  CB    . ILE A 1 149 ? 66.92200 -8.69400  -25.08700 1.000 68.05816  ? 149 ILE A CB    1 
ATOM   1156 C  CG1   . ILE A 1 149 ? 66.20400 -9.91300  -24.49800 1.000 79.25161  ? 149 ILE A CG1   1 
ATOM   1157 C  CG2   . ILE A 1 149 ? 66.48800 -7.40800  -24.38200 1.000 67.56073  ? 149 ILE A CG2   1 
ATOM   1158 C  CD1   . ILE A 1 149 ? 66.47600 -10.12100 -23.04700 1.000 73.36406  ? 149 ILE A CD1   1 
ATOM   1159 N  N     . GLN A 1 150 ? 68.28400 -7.09000  -27.50700 1.000 73.78253  ? 150 GLN A N     1 
ATOM   1160 C  CA    . GLN A 1 150 ? 68.73300 -5.85100  -28.13400 1.000 72.36920  ? 150 GLN A CA    1 
ATOM   1161 C  C     . GLN A 1 150 ? 68.07600 -5.63900  -29.48900 1.000 76.75920  ? 150 GLN A C     1 
ATOM   1162 O  O     . GLN A 1 150 ? 67.75100 -4.50200  -29.84900 1.000 78.27781  ? 150 GLN A O     1 
ATOM   1163 C  CB    . GLN A 1 150 ? 70.25300 -5.84600  -28.29400 1.000 66.13161  ? 150 GLN A CB    1 
ATOM   1164 C  CG    . GLN A 1 150 ? 70.96800 -5.22800  -27.11900 1.000 76.66446  ? 150 GLN A CG    1 
ATOM   1165 C  CD    . GLN A 1 150 ? 70.33400 -3.91700  -26.69500 1.000 78.76997  ? 150 GLN A CD    1 
ATOM   1166 O  OE1   . GLN A 1 150 ? 69.93100 -3.75500  -25.54400 1.000 77.21715  ? 150 GLN A OE1   1 
ATOM   1167 N  NE2   . GLN A 1 150 ? 70.23800 -2.97300  -27.62900 1.000 78.83840  ? 150 GLN A NE2   1 
ATOM   1168 N  N     . SER A 1 151 ? 67.82700 -6.72200  -30.23100 1.000 80.97287  ? 151 SER A N     1 
ATOM   1169 C  CA    . SER A 1 151 ? 67.07700 -6.60100  -31.47800 1.000 81.05446  ? 151 SER A CA    1 
ATOM   1170 C  C     . SER A 1 151 ? 65.64100 -6.14900  -31.23600 1.000 84.82333  ? 151 SER A C     1 
ATOM   1171 O  O     . SER A 1 151 ? 65.11600 -5.30900  -31.98100 1.000 84.41538  ? 151 SER A O     1 
ATOM   1172 C  CB    . SER A 1 151 ? 67.09200 -7.94400  -32.21200 1.000 77.00397  ? 151 SER A CB    1 
ATOM   1173 O  OG    . SER A 1 151 ? 66.65000 -7.81400  -33.54900 1.000 79.17002  ? 151 SER A OG    1 
ATOM   1174 N  N     . ASP A 1 152 ? 64.99600 -6.66900  -30.18800 1.000 91.63730  ? 152 ASP A N     1 
ATOM   1175 C  CA    . ASP A 1 152 ? 63.65800 -6.17500  -29.86000 1.000 88.14215  ? 152 ASP A CA    1 
ATOM   1176 C  C     . ASP A 1 152 ? 63.67800 -4.69700  -29.46600 1.000 86.00768  ? 152 ASP A C     1 
ATOM   1177 O  O     . ASP A 1 152 ? 62.76200 -3.94700  -29.81400 1.000 90.16607  ? 152 ASP A O     1 
ATOM   1178 C  CB    . ASP A 1 152 ? 63.03000 -7.03200  -28.76400 1.000 85.52868  ? 152 ASP A CB    1 
ATOM   1179 C  CG    . ASP A 1 152 ? 62.51200 -8.36200  -29.29300 1.000 87.93686  ? 152 ASP A CG    1 
ATOM   1180 O  OD1   . ASP A 1 152 ? 62.62400 -8.61300  -30.51600 1.000 87.39206  ? 152 ASP A OD1   1 
ATOM   1181 O  OD2   . ASP A 1 152 ? 61.98900 -9.15500  -28.48200 1.000 90.36610  ? 152 ASP A OD2   1 
ATOM   1182 N  N     . ILE A 1 153 ? 64.69100 -4.26800  -28.70900 1.000 73.24036  ? 153 ILE A N     1 
ATOM   1183 C  CA    . ILE A 1 153 ? 64.80500 -2.85000  -28.35400 1.000 70.62689  ? 153 ILE A CA    1 
ATOM   1184 C  C     . ILE A 1 153 ? 64.99000 -1.99400  -29.60400 1.000 76.34600  ? 153 ILE A C     1 
ATOM   1185 O  O     . ILE A 1 153 ? 64.42000 -0.89700  -29.72400 1.000 74.42208  ? 153 ILE A O     1 
ATOM   1186 C  CB    . ILE A 1 153 ? 65.92800 -2.62700  -27.32500 1.000 65.01569  ? 153 ILE A CB    1 
ATOM   1187 C  CG1   . ILE A 1 153 ? 65.48900 -3.17200  -25.97100 1.000 67.88972  ? 153 ILE A CG1   1 
ATOM   1188 C  CG2   . ILE A 1 153 ? 66.28900 -1.15300  -27.21300 1.000 71.96916  ? 153 ILE A CG2   1 
ATOM   1189 C  CD1   . ILE A 1 153 ? 66.58000 -3.24300  -24.97100 1.000 72.92190  ? 153 ILE A CD1   1 
ATOM   1190 N  N     . ALA A 1 154 ? 65.82000 -2.46700  -30.53700 1.000 73.18509  ? 154 ALA A N     1 
ATOM   1191 C  CA    . ALA A 1 154 ? 66.00200 -1.76200  -31.79900 1.000 70.49793  ? 154 ALA A CA    1 
ATOM   1192 C  C     . ALA A 1 154 ? 64.67900 -1.61900  -32.53400 1.000 78.91209  ? 154 ALA A C     1 
ATOM   1193 O  O     . ALA A 1 154 ? 64.36700 -0.54600  -33.06200 1.000 83.95743  ? 154 ALA A O     1 
ATOM   1194 C  CB    . ALA A 1 154 ? 67.02200 -2.49800  -32.66800 1.000 71.63227  ? 154 ALA A CB    1 
ATOM   1195 N  N     . ALA A 1 155 ? 63.88800 -2.69400  -32.58000 1.000 77.92250  ? 155 ALA A N     1 
ATOM   1196 C  CA    . ALA A 1 155 ? 62.57700 -2.61400  -33.22000 1.000 78.11463  ? 155 ALA A CA    1 
ATOM   1197 C  C     . ALA A 1 155 ? 61.64600 -1.65600  -32.47700 1.000 77.13556  ? 155 ALA A C     1 
ATOM   1198 O  O     . ALA A 1 155 ? 60.87700 -0.91400  -33.10300 1.000 77.79880  ? 155 ALA A O     1 
ATOM   1199 C  CB    . ALA A 1 155 ? 61.95400 -4.00700  -33.31100 1.000 78.58311  ? 155 ALA A CB    1 
ATOM   1200 N  N     . LEU A 1 156 ? 61.72400 -1.64100  -31.14200 1.000 73.86938  ? 156 LEU A N     1 
ATOM   1201 C  CA    . LEU A 1 156 ? 60.90800 -0.72900  -30.34100 1.000 71.21907  ? 156 LEU A CA    1 
ATOM   1202 C  C     . LEU A 1 156 ? 61.18700 0.72000   -30.70600 1.000 76.05912  ? 156 LEU A C     1 
ATOM   1203 O  O     . LEU A 1 156 ? 60.25800 1.51000   -30.91400 1.000 75.83278  ? 156 LEU A O     1 
ATOM   1204 C  CB    . LEU A 1 156 ? 61.14600 -0.96600  -28.85000 1.000 69.58729  ? 156 LEU A CB    1 
ATOM   1205 C  CG    . LEU A 1 156 ? 60.23800 -0.13900  -27.93700 1.000 61.23629  ? 156 LEU A CG    1 
ATOM   1206 C  CD1   . LEU A 1 156 ? 58.78400 -0.46700  -28.18700 1.000 61.58107  ? 156 LEU A CD1   1 
ATOM   1207 C  CD2   . LEU A 1 156 ? 60.58400 -0.37700  -26.47900 1.000 56.17779  ? 156 LEU A CD2   1 
ATOM   1208 N  N     . HIS A 1 157 ? 62.46500 1.09100   -30.77000 1.000 74.02466  ? 157 HIS A N     1 
ATOM   1209 C  CA    . HIS A 1 157 ? 62.80800 2.43500   -31.22500 1.000 73.66673  ? 157 HIS A CA    1 
ATOM   1210 C  C     . HIS A 1 157 ? 62.32500 2.65100   -32.65400 1.000 76.86974  ? 157 HIS A C     1 
ATOM   1211 O  O     . HIS A 1 157 ? 61.78700 3.71600   -32.98400 1.000 88.66853  ? 157 HIS A O     1 
ATOM   1212 C  CB    . HIS A 1 157 ? 64.30700 2.69300   -31.08900 1.000 75.13796  ? 157 HIS A CB    1 
ATOM   1213 C  CG    . HIS A 1 157 ? 64.75900 2.82800   -29.66900 1.000 82.17564  ? 157 HIS A CG    1 
ATOM   1214 N  ND1   . HIS A 1 157 ? 64.47300 3.94000   -28.90600 1.000 89.28965  ? 157 HIS A ND1   1 
ATOM   1215 C  CD2   . HIS A 1 157 ? 65.46000 1.99200   -28.86700 1.000 81.11499  ? 157 HIS A CD2   1 
ATOM   1216 C  CE1   . HIS A 1 157 ? 64.98600 3.78700   -27.69800 1.000 91.65309  ? 157 HIS A CE1   1 
ATOM   1217 N  NE2   . HIS A 1 157 ? 65.59000 2.61400   -27.64800 1.000 84.97335  ? 157 HIS A NE2   1 
ATOM   1218 N  N     . HIS A 1 158 ? 62.46200 1.63300   -33.50600 1.000 72.63502  ? 158 HIS A N     1 
ATOM   1219 C  CA    . HIS A 1 158 ? 62.12300 1.80300   -34.94800 1.000 76.53812  ? 158 HIS A CA    1 
ATOM   1220 C  C     . HIS A 1 158 ? 60.63600 2.09700   -35.18400 1.000 77.55930  ? 158 HIS A C     1 
ATOM   1221 O  O     . HIS A 1 158 ? 60.34700 2.92400   -36.06900 1.000 77.13556  ? 158 HIS A O     1 
ATOM   1222 C  CB    . HIS A 1 158 ? 62.59100 0.58000   -35.75000 1.000 80.83864  ? 158 HIS A CB    1 
ATOM   1223 C  CG    . HIS A 1 158 ? 62.38800 0.70800   -37.22100 1.000 82.77045  ? 158 HIS A CG    1 
ATOM   1224 N  ND1   . HIS A 1 158 ? 61.68700 -0.22800  -37.95100 1.000 83.66266  ? 158 HIS A ND1   1 
ATOM   1225 C  CD2   . HIS A 1 158 ? 62.78500 1.65500   -38.09900 1.000 84.19694  ? 158 HIS A CD2   1 
ATOM   1226 C  CE1   . HIS A 1 158 ? 61.66000 0.13300   -39.21800 1.000 90.72140  ? 158 HIS A CE1   1 
ATOM   1227 N  NE2   . HIS A 1 158 ? 62.32600 1.28600   -39.33400 1.000 96.76160  ? 158 HIS A NE2   1 
ATOM   1228 N  N     . PHE A 1 159 ? 59.72400 1.48500   -34.42400 1.000 77.71721  ? 159 PHE A N     1 
ATOM   1229 C  CA    . PHE A 1 159 ? 58.28000 1.64400   -34.75500 1.000 76.60919  ? 159 PHE A CA    1 
ATOM   1230 C  C     . PHE A 1 159 ? 57.50500 2.51400   -33.76000 1.000 74.66948  ? 159 PHE A C     1 
ATOM   1231 O  O     . PHE A 1 159 ? 56.39200 2.94100   -34.12700 1.000 75.71434  ? 159 PHE A O     1 
ATOM   1232 C  CB    . PHE A 1 159 ? 57.59800 0.27500   -34.83300 1.000 74.75107  ? 159 PHE A CB    1 
ATOM   1233 C  CG    . PHE A 1 159 ? 58.09200 -0.62800  -35.93300 1.000 77.52508  ? 159 PHE A CG    1 
ATOM   1234 C  CD1   . PHE A 1 159 ? 57.75100 -0.39100  -37.25400 1.000 81.95983  ? 159 PHE A CD1   1 
ATOM   1235 C  CD2   . PHE A 1 159 ? 58.89100 -1.72300  -35.64600 1.000 73.54829  ? 159 PHE A CD2   1 
ATOM   1236 C  CE1   . PHE A 1 159 ? 58.20300 -1.22400  -38.26300 1.000 80.70705  ? 159 PHE A CE1   1 
ATOM   1237 C  CE2   . PHE A 1 159 ? 59.34300 -2.55700  -36.65600 1.000 72.27709  ? 159 PHE A CE2   1 
ATOM   1238 C  CZ    . PHE A 1 159 ? 59.00000 -2.30400  -37.96200 1.000 74.65369  ? 159 PHE A CZ    1 
ATOM   1239 N  N     . TYR A 1 160 ? 58.03500 2.77300   -32.56100 1.000 73.88254  ? 160 TYR A N     1 
ATOM   1240 C  CA    . TYR A 1 160 ? 57.21100 3.49200   -31.54900 1.000 75.44062  ? 160 TYR A CA    1 
ATOM   1241 C  C     . TYR A 1 160 ? 57.92900 4.71800   -30.97200 1.000 79.84642  ? 160 TYR A C     1 
ATOM   1242 O  O     . TYR A 1 160 ? 57.64700 5.06100   -29.80700 1.000 84.16799  ? 160 TYR A O     1 
ATOM   1243 C  CB    . TYR A 1 160 ? 56.78500 2.52100   -30.44500 1.000 71.93494  ? 160 TYR A CB    1 
ATOM   1244 C  CG    . TYR A 1 160 ? 56.00500 1.33400   -30.95000 1.000 71.28223  ? 160 TYR A CG    1 
ATOM   1245 C  CD1   . TYR A 1 160 ? 54.67300 1.46200   -31.30400 1.000 81.15710  ? 160 TYR A CD1   1 
ATOM   1246 C  CD2   . TYR A 1 160 ? 56.60000 0.09300   -31.10700 1.000 66.43954  ? 160 TYR A CD2   1 
ATOM   1247 C  CE1   . TYR A 1 160 ? 53.94900 0.38500   -31.78500 1.000 77.46718  ? 160 TYR A CE1   1 
ATOM   1248 C  CE2   . TYR A 1 160 ? 55.88900 -0.99400  -31.58600 1.000 62.38906  ? 160 TYR A CE2   1 
ATOM   1249 C  CZ    . TYR A 1 160 ? 54.55800 -0.84700  -31.92600 1.000 68.35030  ? 160 TYR A CZ    1 
ATOM   1250 O  OH    . TYR A 1 160 ? 53.84500 -1.90900  -32.40000 1.000 69.67678  ? 160 TYR A OH    1 
ATOM   1251 N  N     . SER A 1 161 ? 58.76700 5.37900   -31.76700 1.000 75.98016  ? 161 SER A N     1 
ATOM   1252 C  CA    . SER A 1 161 ? 59.57300 6.52100   -31.25600 1.000 83.16787  ? 161 SER A CA    1 
ATOM   1253 C  C     . SER A 1 161 ? 58.74900 7.80400   -31.12200 1.000 85.26285  ? 161 SER A C     1 
ATOM   1254 O  O     . SER A 1 161 ? 59.07600 8.60400   -30.22200 1.000 85.02335  ? 161 SER A O     1 
ATOM   1255 C  CB    . SER A 1 161 ? 60.77500 6.75300   -32.13000 1.000 86.29193  ? 161 SER A CB    1 
ATOM   1256 O  OG    . SER A 1 161 ? 60.43400 6.59800   -33.50000 1.000 98.24862  ? 161 SER A OG    1 
ATOM   1257 N  N     . LYS A 1 162 ? 57.71000 8.00900   -31.96400 1.000 87.54208  ? 162 LYS A N     1 
ATOM   1258 C  CA    . LYS A 1 162 ? 57.00500 9.29100   -31.94900 1.000 90.95301  ? 162 LYS A CA    1 
ATOM   1259 C  C     . LYS A 1 162 ? 56.10600 9.48300   -30.72800 1.000 89.67128  ? 162 LYS A C     1 
ATOM   1260 O  O     . LYS A 1 162 ? 55.84000 10.62900  -30.35600 1.000 91.50044  ? 162 LYS A O     1 
ATOM   1261 C  CB    . LYS A 1 162 ? 56.17900 9.39000   -33.23700 1.000 99.89356  ? 162 LYS A CB    1 
ATOM   1262 C  CG    . LYS A 1 162 ? 57.07400 9.36500   -34.48200 1.000 106.61541 ? 162 LYS A CG    1 
ATOM   1263 C  CD    . LYS A 1 162 ? 56.40000 9.72300   -35.80000 1.000 104.14670 ? 162 LYS A CD    1 
ATOM   1264 C  CE    . LYS A 1 162 ? 56.16100 11.20800  -35.93800 1.000 98.55919  ? 162 LYS A CE    1 
ATOM   1265 N  NZ    . LYS A 1 162 ? 56.48500 11.63700  -37.33000 1.000 101.89380 ? 162 LYS A NZ    1 
ATOM   1266 N  N     . HIS A 1 163 ? 55.67400 8.40600   -30.07300 1.000 86.91832  ? 163 HIS A N     1 
ATOM   1267 C  CA    . HIS A 1 163 ? 54.70600 8.47000   -28.98000 1.000 85.74186  ? 163 HIS A CA    1 
ATOM   1268 C  C     . HIS A 1 163 ? 55.24900 8.11500   -27.60400 1.000 86.55775  ? 163 HIS A C     1 
ATOM   1269 O  O     . HIS A 1 163 ? 54.58500 8.41900   -26.60900 1.000 90.04764  ? 163 HIS A O     1 
ATOM   1270 C  CB    . HIS A 1 163 ? 53.46100 7.61200   -29.25100 1.000 82.20459  ? 163 HIS A CB    1 
ATOM   1271 C  CG    . HIS A 1 163 ? 52.54000 8.18700   -30.28000 1.000 87.81053  ? 163 HIS A CG    1 
ATOM   1272 N  ND1   . HIS A 1 163 ? 51.51600 9.04800   -29.94500 1.000 92.73480  ? 163 HIS A ND1   1 
ATOM   1273 C  CD2   . HIS A 1 163 ? 52.47400 8.02700   -31.62200 1.000 90.13449  ? 163 HIS A CD2   1 
ATOM   1274 C  CE1   . HIS A 1 163 ? 50.86100 9.39900   -31.03700 1.000 92.83218  ? 163 HIS A CE1   1 
ATOM   1275 N  NE2   . HIS A 1 163 ? 51.42200 8.79300   -32.06900 1.000 94.71136  ? 163 HIS A NE2   1 
ATOM   1276 N  N     . LEU A 1 164 ? 56.41900 7.49700   -27.49900 1.000 87.06307  ? 164 LEU A N     1 
ATOM   1277 C  CA    . LEU A 1 164 ? 56.90900 7.04600   -26.20600 1.000 80.31226  ? 164 LEU A CA    1 
ATOM   1278 C  C     . LEU A 1 164 ? 58.21400 7.72700   -25.83200 1.000 85.17863  ? 164 LEU A C     1 
ATOM   1279 O  O     . LEU A 1 164 ? 59.15600 7.76900   -26.63000 1.000 89.05015  ? 164 LEU A O     1 
ATOM   1280 C  CB    . LEU A 1 164 ? 57.13400 5.53300   -26.23500 1.000 70.30580  ? 164 LEU A CB    1 
ATOM   1281 C  CG    . LEU A 1 164 ? 55.90900 4.63200   -26.34200 1.000 73.89833  ? 164 LEU A CG    1 
ATOM   1282 C  CD1   . LEU A 1 164 ? 56.34500 3.21000   -26.65400 1.000 72.54028  ? 164 LEU A CD1   1 
ATOM   1283 C  CD2   . LEU A 1 164 ? 55.09600 4.68700   -25.06600 1.000 72.63502  ? 164 LEU A CD2   1 
ATOM   1284 N  N     . GLY A 1 165 ? 58.25100 8.27200   -24.61700 1.000 84.99177  ? 165 GLY A N     1 
ATOM   1285 C  CA    . GLY A 1 165 ? 59.49600 8.67600   -23.99700 1.000 83.54423  ? 165 GLY A CA    1 
ATOM   1286 C  C     . GLY A 1 165 ? 60.17600 7.46500   -23.39400 1.000 85.29707  ? 165 GLY A C     1 
ATOM   1287 O  O     . GLY A 1 165 ? 59.68600 6.89500   -22.41600 1.000 82.73360  ? 165 GLY A O     1 
ATOM   1288 N  N     . PHE A 1 166 ? 61.28800 7.03800   -23.99400 1.000 95.73253  ? 166 PHE A N     1 
ATOM   1289 C  CA    . PHE A 1 166 ? 62.00500 5.80800   -23.66200 1.000 97.85121  ? 166 PHE A CA    1 
ATOM   1290 C  C     . PHE A 1 166 ? 62.98100 6.01200   -22.50700 1.000 99.76196  ? 166 PHE A C     1 
ATOM   1291 O  O     . PHE A 1 166 ? 63.68900 7.02500   -22.46000 1.000 101.48322 ? 166 PHE A O     1 
ATOM   1292 C  CB    . PHE A 1 166 ? 62.79900 5.29900   -24.85900 1.000 93.85073  ? 166 PHE A CB    1 
ATOM   1293 C  CG    . PHE A 1 166 ? 61.97200 5.01800   -26.07100 1.000 91.16356  ? 166 PHE A CG    1 
ATOM   1294 C  CD1   . PHE A 1 166 ? 61.14500 3.90900   -26.12000 1.000 89.95552  ? 166 PHE A CD1   1 
ATOM   1295 C  CD2   . PHE A 1 166 ? 62.03600 5.85300   -27.17300 1.000 92.97957  ? 166 PHE A CD2   1 
ATOM   1296 C  CE1   . PHE A 1 166 ? 60.38900 3.64500   -27.24400 1.000 90.86089  ? 166 PHE A CE1   1 
ATOM   1297 C  CE2   . PHE A 1 166 ? 61.28500 5.59600   -28.29800 1.000 92.66901  ? 166 PHE A CE2   1 
ATOM   1298 C  CZ    . PHE A 1 166 ? 60.46000 4.49100   -28.33600 1.000 91.43991  ? 166 PHE A CZ    1 
ATOM   1299 N  N     . PRO A 1 167 ? 63.02200 5.07300   -21.55300 1.000 96.98268  ? 167 PRO A N     1 
ATOM   1300 C  CA    . PRO A 1 167 ? 64.12600 5.06300   -20.58400 1.000 94.31657  ? 167 PRO A CA    1 
ATOM   1301 C  C     . PRO A 1 167 ? 65.43400 4.68500   -21.26200 1.000 95.68779  ? 167 PRO A C     1 
ATOM   1302 O  O     . PRO A 1 167 ? 65.46600 4.45000   -22.47500 1.000 85.98926  ? 167 PRO A O     1 
ATOM   1303 C  CB    . PRO A 1 167 ? 63.69400 4.00100   -19.56600 1.000 83.89690  ? 167 PRO A CB    1 
ATOM   1304 C  CG    . PRO A 1 167 ? 62.82600 3.08300   -20.34700 1.000 75.69855  ? 167 PRO A CG    1 
ATOM   1305 C  CD    . PRO A 1 167 ? 62.08600 3.95500   -21.32800 1.000 88.55272  ? 167 PRO A CD    1 
ATOM   1306 N  N     . ASP A 1 168 ? 66.51800 4.62400   -20.49400 1.000 110.87119 ? 168 ASP A N     1 
ATOM   1307 C  CA    . ASP A 1 168 ? 67.81100 4.22700   -21.02700 1.000 111.41599 ? 168 ASP A CA    1 
ATOM   1308 C  C     . ASP A 1 168 ? 67.78100 2.76100   -21.47100 1.000 109.24205 ? 168 ASP A C     1 
ATOM   1309 O  O     . ASP A 1 168 ? 66.83600 2.01600   -21.19100 1.000 107.23654 ? 168 ASP A O     1 
ATOM   1310 C  CB    . ASP A 1 168 ? 68.91300 4.45200   -19.99200 1.000 113.05566 ? 168 ASP A CB    1 
ATOM   1311 C  CG    . ASP A 1 168 ? 68.70700 3.62900   -18.72800 1.000 113.32411 ? 168 ASP A CG    1 
ATOM   1312 O  OD1   . ASP A 1 168 ? 67.69700 2.89600   -18.63200 1.000 110.54483 ? 168 ASP A OD1   1 
ATOM   1313 O  OD2   . ASP A 1 168 ? 69.59600 3.66300   -17.85500 1.000 121.54615 ? 168 ASP A OD2   1 
ATOM   1314 N  N     . ASN A 1 169 ? 68.82900 2.36100   -22.19700 1.000 92.33475  ? 169 ASN A N     1 
ATOM   1315 C  CA    . ASN A 1 169 ? 68.87600 1.02000   -22.77700 1.000 89.38967  ? 169 ASN A CA    1 
ATOM   1316 C  C     . ASN A 1 169 ? 68.77100 -0.06200  -21.70400 1.000 92.91640  ? 169 ASN A C     1 
ATOM   1317 O  O     . ASN A 1 169 ? 67.98900 -1.00900  -21.83600 1.000 91.63204  ? 169 ASN A O     1 
ATOM   1318 C  CB    . ASN A 1 169 ? 70.16900 0.84700   -23.58100 1.000 85.58131  ? 169 ASN A CB    1 
ATOM   1319 C  CG    . ASN A 1 169 ? 70.14400 -0.38300  -24.48400 1.000 78.48046  ? 169 ASN A CG    1 
ATOM   1320 O  OD1   . ASN A 1 169 ? 69.40200 -0.44000  -25.46500 1.000 76.82763  ? 169 ASN A OD1   1 
ATOM   1321 N  ND2   . ASN A 1 169 ? 70.95200 -1.38400  -24.13900 1.000 76.86974  ? 169 ASN A ND2   1 
ATOM   1322 N  N     . ASP A 1 170 ? 69.58500 0.05200   -20.65000 1.000 106.71016 ? 170 ASP A N     1 
ATOM   1323 C  CA    . ASP A 1 170 ? 69.57800 -0.90200  -19.54000 1.000 105.68109 ? 170 ASP A CA    1 
ATOM   1324 C  C     . ASP A 1 170 ? 68.17400 -1.18700  -18.99800 1.000 103.72559 ? 170 ASP A C     1 
ATOM   1325 O  O     . ASP A 1 170 ? 67.78000 -2.35300  -18.82400 1.000 102.03855 ? 170 ASP A O     1 
ATOM   1326 C  CB    . ASP A 1 170 ? 70.49200 -0.35200  -18.43900 1.000 113.44518 ? 170 ASP A CB    1 
ATOM   1327 C  CG    . ASP A 1 170 ? 70.25700 -0.99900  -17.09500 1.000 120.71974 ? 170 ASP A CG    1 
ATOM   1328 O  OD1   . ASP A 1 170 ? 70.67500 -2.16000  -16.91000 1.000 125.18606 ? 170 ASP A OD1   1 
ATOM   1329 O  OD2   . ASP A 1 170 ? 69.67300 -0.33000  -16.21500 1.000 121.18032 ? 170 ASP A OD2   1 
ATOM   1330 N  N     A SER A 1 171 ? 67.38800 -0.13100  -18.76100 1.000 88.88434  ? 171 SER A N     1 
ATOM   1331 C  CA    A SER A 1 171 ? 66.03100 -0.32100  -18.25100 1.000 87.54208  ? 171 SER A CA    1 
ATOM   1332 C  C     A SER A 1 171 ? 65.17200 -1.07600  -19.25200 1.000 79.00684  ? 171 SER A C     1 
ATOM   1333 O  O     A SER A 1 171 ? 64.32800 -1.89700  -18.86600 1.000 75.11427  ? 171 SER A O     1 
ATOM   1334 C  CB    A SER A 1 171 ? 65.38600 1.02400   -17.89700 1.000 92.77691  ? 171 SER A CB    1 
ATOM   1335 O  OG    A SER A 1 171 ? 66.02300 1.61900   -16.78100 1.000 99.44877  ? 171 SER A OG    1 
ATOM   1336 N  N     . LEU A 1 172 ? 65.34400 -0.77600  -20.54200 1.000 77.03292  ? 172 LEU A N     1 
ATOM   1337 C  CA    . LEU A 1 172 ? 64.57200 -1.45100  -21.57600 1.000 66.50797  ? 172 LEU A CA    1 
ATOM   1338 C  C     . LEU A 1 172 ? 64.93700 -2.92900  -21.65500 1.000 69.57150  ? 172 LEU A C     1 
ATOM   1339 O  O     . LEU A 1 172 ? 64.07000 -3.77900  -21.91100 1.000 75.51169  ? 172 LEU A O     1 
ATOM   1340 C  CB    . LEU A 1 172 ? 64.80200 -0.75600  -22.91800 1.000 60.70201  ? 172 LEU A CB    1 
ATOM   1341 C  CG    . LEU A 1 172 ? 63.96200 0.50800   -23.08000 1.000 63.74712  ? 172 LEU A CG    1 
ATOM   1342 C  CD1   . LEU A 1 172 ? 64.26800 1.19600   -24.39900 1.000 69.09776  ? 172 LEU A CD1   1 
ATOM   1343 C  CD2   . LEU A 1 172 ? 62.47800 0.19600   -22.94700 1.000 61.34420  ? 172 LEU A CD2   1 
ATOM   1344 N  N     . VAL A 1 173 ? 66.21500 -3.25600  -21.44400 1.000 70.25579  ? 173 VAL A N     1 
ATOM   1345 C  CA    . VAL A 1 173 ? 66.62000 -4.65900  -21.41400 1.000 69.39516  ? 173 VAL A CA    1 
ATOM   1346 C  C     . VAL A 1 173 ? 65.92000 -5.36700  -20.26000 1.000 67.92393  ? 173 VAL A C     1 
ATOM   1347 O  O     . VAL A 1 173 ? 65.38800 -6.47900  -20.41200 1.000 64.64722  ? 173 VAL A O     1 
ATOM   1348 C  CB    . VAL A 1 173 ? 68.15200 -4.78400  -21.31500 1.000 68.27661  ? 173 VAL A CB    1 
ATOM   1349 C  CG1   . VAL A 1 173 ? 68.55200 -6.23800  -21.10300 1.000 63.41023  ? 173 VAL A CG1   1 
ATOM   1350 C  CG2   . VAL A 1 173 ? 68.82900 -4.20500  -22.54000 1.000 69.70836  ? 173 VAL A CG2   1 
ATOM   1351 N  N     . VAL A 1 174 ? 65.87900 -4.71100  -19.09400 1.000 66.82907  ? 174 VAL A N     1 
ATOM   1352 C  CA    . VAL A 1 174 ? 65.20000 -5.29400  -17.93800 1.000 61.70213  ? 174 VAL A CA    1 
ATOM   1353 C  C     . VAL A 1 174 ? 63.73100 -5.52300  -18.26000 1.000 59.61767  ? 174 VAL A C     1 
ATOM   1354 O  O     . VAL A 1 174 ? 63.16400 -6.57700  -17.94400 1.000 60.36776  ? 174 VAL A O     1 
ATOM   1355 C  CB    . VAL A 1 174 ? 65.36600 -4.38400  -16.70700 1.000 63.23916  ? 174 VAL A CB    1 
ATOM   1356 C  CG1   . VAL A 1 174 ? 64.49200 -4.87000  -15.56300 1.000 62.09692  ? 174 VAL A CG1   1 
ATOM   1357 C  CG2   . VAL A 1 174 ? 66.82000 -4.32500  -16.28500 1.000 78.16990  ? 174 VAL A CG2   1 
ATOM   1358 N  N     . LEU A 1 175 ? 63.09100 -4.53200  -18.87900 1.000 59.36764  ? 175 LEU A N     1 
ATOM   1359 C  CA    . LEU A 1 175 ? 61.66700 -4.62300  -19.17500 1.000 57.23055  ? 175 LEU A CA    1 
ATOM   1360 C  C     . LEU A 1 175 ? 61.37300 -5.79000  -20.10600 1.000 58.15960  ? 175 LEU A C     1 
ATOM   1361 O  O     . LEU A 1 175 ? 60.45600 -6.58200  -19.85800 1.000 61.42052  ? 175 LEU A O     1 
ATOM   1362 C  CB    . LEU A 1 175 ? 61.19500 -3.32000  -19.81700 1.000 52.88529  ? 175 LEU A CB    1 
ATOM   1363 C  CG    . LEU A 1 175 ? 59.70400 -3.15300  -20.10200 1.000 52.08782  ? 175 LEU A CG    1 
ATOM   1364 C  CD1   . LEU A 1 175 ? 58.86800 -3.31700  -18.84500 1.000 51.62987  ? 175 LEU A CD1   1 
ATOM   1365 C  CD2   . LEU A 1 175 ? 59.46900 -1.81400  -20.74900 1.000 58.41753  ? 175 LEU A CD2   1 
ATOM   1366 N  N     . PHE A 1 176 ? 62.13500 -5.89900  -21.19600 1.000 57.85167  ? 176 PHE A N     1 
ATOM   1367 C  CA    . PHE A 1 176 ? 61.95000 -7.00600  -22.13000 1.000 60.66780  ? 176 PHE A CA    1 
ATOM   1368 C  C     . PHE A 1 176 ? 62.16500 -8.36500  -21.47000 1.000 62.87333  ? 176 PHE A C     1 
ATOM   1369 O  O     . PHE A 1 176 ? 61.40100 -9.30800  -21.71700 1.000 70.76375  ? 176 PHE A O     1 
ATOM   1370 C  CB    . PHE A 1 176 ? 62.86700 -6.82700  -23.33700 1.000 56.70154  ? 176 PHE A CB    1 
ATOM   1371 C  CG    . PHE A 1 176 ? 62.24200 -6.03100  -24.44100 1.000 58.33594  ? 176 PHE A CG    1 
ATOM   1372 C  CD1   . PHE A 1 176 ? 61.23100 -6.57500  -25.21400 1.000 65.45785  ? 176 PHE A CD1   1 
ATOM   1373 C  CD2   . PHE A 1 176 ? 62.63100 -4.72500  -24.68000 1.000 61.54685  ? 176 PHE A CD2   1 
ATOM   1374 C  CE1   . PHE A 1 176 ? 60.63800 -5.84200  -26.22500 1.000 65.95791  ? 176 PHE A CE1   1 
ATOM   1375 C  CE2   . PHE A 1 176 ? 62.04100 -3.98500  -25.68900 1.000 66.71326  ? 176 PHE A CE2   1 
ATOM   1376 C  CZ    . PHE A 1 176 ? 61.04400 -4.54400  -26.46300 1.000 66.51324  ? 176 PHE A CZ    1 
ATOM   1377 N  N     . ALA A 1 177 ? 63.20200 -8.49600  -20.64000 1.000 56.39360  ? 177 ALA A N     1 
ATOM   1378 C  CA    . ALA A 1 177 ? 63.39700 -9.75900  -19.93400 1.000 57.41478  ? 177 ALA A CA    1 
ATOM   1379 C  C     . ALA A 1 177 ? 62.22100 -10.07400 -19.01500 1.000 63.01019  ? 177 ALA A C     1 
ATOM   1380 O  O     . ALA A 1 177 ? 61.76100 -11.22700 -18.94300 1.000 69.88733  ? 177 ALA A O     1 
ATOM   1381 C  CB    . ALA A 1 177 ? 64.70200 -9.71400  -19.14300 1.000 70.75585  ? 177 ALA A CB    1 
ATOM   1382 N  N     . GLN A 1 178 ? 61.69900 -9.05100  -18.33300 1.000 63.90503  ? 178 GLN A N     1 
ATOM   1383 C  CA    . GLN A 1 178 ? 60.53200 -9.24300  -17.48100 1.000 61.32051  ? 178 GLN A CA    1 
ATOM   1384 C  C     . GLN A 1 178 ? 59.33200 -9.70800  -18.28800 1.000 62.33116  ? 178 GLN A C     1 
ATOM   1385 O  O     . GLN A 1 178 ? 58.56500 -10.56600 -17.83800 1.000 68.19239  ? 178 GLN A O     1 
ATOM   1386 C  CB    . GLN A 1 178 ? 60.21100 -7.94000  -16.75300 1.000 58.24383  ? 178 GLN A CB    1 
ATOM   1387 C  CG    . GLN A 1 178 ? 61.15700 -7.62300  -15.61800 1.000 62.11271  ? 178 GLN A CG    1 
ATOM   1388 C  CD    . GLN A 1 178 ? 60.96000 -6.22700  -15.08400 1.000 54.16702  ? 178 GLN A CD    1 
ATOM   1389 O  OE1   . GLN A 1 178 ? 60.67400 -5.29600  -15.83500 1.000 58.01222  ? 178 GLN A OE1   1 
ATOM   1390 N  NE2   . GLN A 1 178 ? 61.08200 -6.07700  -13.77400 1.000 55.86459  ? 178 GLN A NE2   1 
ATOM   1391 N  N     . VAL A 1 179 ? 59.15600 -9.15200  -19.48600 1.000 60.50989  ? 179 VAL A N     1 
ATOM   1392 C  CA    . VAL A 1 179 ? 58.03800 -9.55900  -20.33100 1.000 60.22564  ? 179 VAL A CA    1 
ATOM   1393 C  C     . VAL A 1 179 ? 58.19200 -11.01200 -20.74900 1.000 61.59949  ? 179 VAL A C     1 
ATOM   1394 O  O     . VAL A 1 179 ? 57.24400 -11.80200 -20.67200 1.000 69.85048  ? 179 VAL A O     1 
ATOM   1395 C  CB    . VAL A 1 179 ? 57.93200 -8.64100  -21.55800 1.000 61.17839  ? 179 VAL A CB    1 
ATOM   1396 C  CG1   . VAL A 1 179 ? 56.95700 -9.23000  -22.56300 1.000 59.85981  ? 179 VAL A CG1   1 
ATOM   1397 C  CG2   . VAL A 1 179 ? 57.48500 -7.26000  -21.13200 1.000 65.61576  ? 179 VAL A CG2   1 
ATOM   1398 N  N     . ASN A 1 180 ? 59.39400 -11.38100 -21.20300 1.000 65.21045  ? 180 ASN A N     1 
ATOM   1399 C  CA    . ASN A 1 180 ? 59.64500 -12.75700 -21.61900 1.000 67.98447  ? 180 ASN A CA    1 
ATOM   1400 C  C     . ASN A 1 180 ? 59.38500 -13.75500 -20.49900 1.000 74.16416  ? 180 ASN A C     1 
ATOM   1401 O  O     . ASN A 1 180 ? 58.96900 -14.88900 -20.76700 1.000 77.49877  ? 180 ASN A O     1 
ATOM   1402 C  CB    . ASN A 1 180 ? 61.07300 -12.91000 -22.14800 1.000 67.92130  ? 180 ASN A CB    1 
ATOM   1403 C  CG    . ASN A 1 180 ? 61.27500 -12.23300 -23.49300 1.000 72.45869  ? 180 ASN A CG    1 
ATOM   1404 O  OD1   . ASN A 1 180 ? 60.31800 -12.01600 -24.23700 1.000 78.51205  ? 180 ASN A OD1   1 
ATOM   1405 N  ND2   . ASN A 1 180 ? 62.51800 -11.88200 -23.80500 1.000 68.52664  ? 180 ASN A ND2   1 
ATOM   1406 N  N     A CYS A 1 181 ? 59.63800 -13.37000 -19.24600 1.000 75.44589  ? 181 CYS A N     1 
ATOM   1407 C  CA    A CYS A 1 181 ? 59.42900 -14.30400 -18.14300 1.000 73.57198  ? 181 CYS A CA    1 
ATOM   1408 C  C     A CYS A 1 181 ? 58.05200 -14.21100 -17.48900 1.000 69.05828  ? 181 CYS A C     1 
ATOM   1409 O  O     A CYS A 1 181 ? 57.68700 -15.12400 -16.74100 1.000 72.34552  ? 181 CYS A O     1 
ATOM   1410 C  CB    A CYS A 1 181 ? 60.50800 -14.11200 -17.07200 1.000 74.19047  ? 181 CYS A CB    1 
ATOM   1411 S  SG    A CYS A 1 181 ? 60.37300 -15.29000 -15.70800 1.000 102.80443 ? 181 CYS A SG    1 
ATOM   1412 N  N     . ASN A 1 182 ? 57.28100 -13.15400 -17.74800 1.000 61.73898  ? 182 ASN A N     1 
ATOM   1413 C  CA    . ASN A 1 182 ? 55.99700 -12.93600 -17.08700 1.000 62.27062  ? 182 ASN A CA    1 
ATOM   1414 C  C     . ASN A 1 182 ? 54.82800 -12.73800 -18.04300 1.000 62.11797  ? 182 ASN A C     1 
ATOM   1415 O  O     . ASN A 1 182 ? 53.68500 -12.63100 -17.58100 1.000 59.40449  ? 182 ASN A O     1 
ATOM   1416 C  CB    . ASN A 1 182 ? 56.06400 -11.73200 -16.13400 1.000 57.97800  ? 182 ASN A CB    1 
ATOM   1417 C  CG    . ASN A 1 182 ? 57.09800 -11.90200 -15.03900 1.000 69.86101  ? 182 ASN A CG    1 
ATOM   1418 O  OD1   . ASN A 1 182 ? 57.96400 -11.04800 -14.84800 1.000 78.06725  ? 182 ASN A OD1   1 
ATOM   1419 N  ND2   . ASN A 1 182 ? 57.00200 -12.99900 -14.29900 1.000 77.94619  ? 182 ASN A ND2   1 
ATOM   1420 N  N     . GLY A 1 183 ? 55.06700 -12.68000 -19.34800 1.000 62.78911  ? 183 GLY A N     1 
ATOM   1421 C  CA    . GLY A 1 183 ? 53.98900 -12.47800 -20.29500 1.000 54.45390  ? 183 GLY A CA    1 
ATOM   1422 C  C     . GLY A 1 183 ? 53.06200 -13.67200 -20.39100 1.000 54.40126  ? 183 GLY A C     1 
ATOM   1423 O  O     . GLY A 1 183 ? 53.35300 -14.77400 -19.92600 1.000 62.64962  ? 183 GLY A O     1 
ATOM   1424 N  N     . ALA A 1 184 ? 51.89400 -13.42800 -20.98700 1.000 54.24335  ? 184 ALA A N     1 
ATOM   1425 C  CA    . ALA A 1 184 ? 50.81800 -14.42000 -20.99600 1.000 54.54338  ? 184 ALA A CA    1 
ATOM   1426 C  C     . ALA A 1 184 ? 50.09400 -14.37200 -22.33700 1.000 52.31943  ? 184 ALA A C     1 
ATOM   1427 O  O     . ALA A 1 184 ? 49.45700 -13.36600 -22.66700 1.000 57.02263  ? 184 ALA A O     1 
ATOM   1428 C  CB    . ALA A 1 184 ? 49.84900 -14.17900 -19.84000 1.000 52.87739  ? 184 ALA A CB    1 
ATOM   1429 N  N     . THR A 1 185 ? 50.22100 -15.44700 -23.11400 1.000 56.52783  ? 185 THR A N     1 
ATOM   1430 C  CA    . THR A 1 185 ? 49.43300 -15.62400 -24.32900 1.000 52.55104  ? 185 THR A CA    1 
ATOM   1431 C  C     . THR A 1 185 ? 47.96100 -15.85900 -24.00800 1.000 46.82404  ? 185 THR A C     1 
ATOM   1432 O  O     . THR A 1 185 ? 47.62400 -16.61800 -23.09400 1.000 49.87440  ? 185 THR A O     1 
ATOM   1433 C  CB    . THR A 1 185 ? 49.97200 -16.79800 -25.14600 1.000 57.06474  ? 185 THR A CB    1 
ATOM   1434 O  OG1   . THR A 1 185 ? 50.01800 -17.97700 -24.32700 1.000 61.13101  ? 185 THR A OG1   1 
ATOM   1435 C  CG2   . THR A 1 185 ? 51.36800 -16.49100 -25.64900 1.000 58.32805  ? 185 THR A CG2   1 
ATOM   1436 N  N     . ILE A 1 186 ? 47.09300 -15.22600 -24.78700 1.000 44.74484  ? 186 ILE A N     1 
ATOM   1437 C  CA    . ILE A 1 186 ? 45.65600 -15.38300 -24.63200 1.000 48.96113  ? 186 ILE A CA    1 
ATOM   1438 C  C     . ILE A 1 186 ? 45.20000 -16.32100 -25.74200 1.000 55.49350  ? 186 ILE A C     1 
ATOM   1439 O  O     . ILE A 1 186 ? 45.48300 -16.07400 -26.90800 1.000 63.81028  ? 186 ILE A O     1 
ATOM   1440 C  CB    . ILE A 1 186 ? 44.92600 -14.03900 -24.77800 1.000 49.29802  ? 186 ILE A CB    1 
ATOM   1441 C  CG1   . ILE A 1 186 ? 45.43000 -13.04100 -23.73300 1.000 48.89270  ? 186 ILE A CG1   1 
ATOM   1442 C  CG2   . ILE A 1 186 ? 43.42200 -14.23200 -24.66200 1.000 51.54565  ? 186 ILE A CG2   1 
ATOM   1443 C  CD1   . ILE A 1 186 ? 44.88500 -11.64100 -23.91100 1.000 52.80896  ? 186 ILE A CD1   1 
ATOM   1444 N  N     . GLU A 1 187 ? 44.50700 -17.39600 -25.39000 1.000 58.97812  ? 187 GLU A N     1 
ATOM   1445 C  CA    . GLU A 1 187 ? 44.04400 -18.35300 -26.39300 1.000 59.78348  ? 187 GLU A CA    1 
ATOM   1446 C  C     . GLU A 1 187 ? 42.52400 -18.47900 -26.37600 1.000 61.42842  ? 187 GLU A C     1 
ATOM   1447 O  O     . GLU A 1 187 ? 41.89300 -18.22000 -25.37100 1.000 60.94678  ? 187 GLU A O     1 
ATOM   1448 C  CB    . GLU A 1 187 ? 44.69700 -19.71800 -26.16600 1.000 59.16499  ? 187 GLU A CB    1 
ATOM   1449 C  CG    . GLU A 1 187 ? 46.14100 -19.79900 -26.63800 1.000 72.07969  ? 187 GLU A CG    1 
ATOM   1450 C  CD    . GLU A 1 187 ? 47.14000 -19.52200 -25.53100 1.000 79.05685  ? 187 GLU A CD    1 
ATOM   1451 O  OE1   . GLU A 1 187 ? 46.71200 -19.18500 -24.40600 1.000 75.88805  ? 187 GLU A OE1   1 
ATOM   1452 O  OE2   . GLU A 1 187 ? 48.35800 -19.64100 -25.78700 1.000 74.60631  ? 187 GLU A OE2   1 
ATOM   1453 N  N     . ASP A 1 188 ? 41.92500 -18.87800 -27.48800 1.000 61.85215  ? 188 ASP A N     1 
ATOM   1454 C  CA    . ASP A 1 188 ? 40.44100 -19.02000 -27.53000 1.000 60.59411  ? 188 ASP A CA    1 
ATOM   1455 C  C     . ASP A 1 188 ? 39.99700 -20.37700 -26.98300 1.000 66.45007  ? 188 ASP A C     1 
ATOM   1456 O  O     . ASP A 1 188 ? 40.74500 -21.02800 -26.25500 1.000 62.68646  ? 188 ASP A O     1 
ATOM   1457 C  CB    . ASP A 1 188 ? 39.86700 -18.70900 -28.93200 1.000 63.55499  ? 188 ASP A CB    1 
ATOM   1458 C  CG    . ASP A 1 188 ? 40.38800 -19.65600 -29.99400 1.000 67.68969  ? 188 ASP A CG    1 
ATOM   1459 O  OD1   . ASP A 1 188 ? 41.11000 -20.61100 -29.63500 1.000 68.30819  ? 188 ASP A OD1   1 
ATOM   1460 O  OD2   . ASP A 1 188 ? 40.07800 -19.44900 -31.18500 1.000 67.10278  ? 188 ASP A OD2   1 
ATOM   1461 N  N     . GLU A 1 189 ? 38.78400 -20.79900 -27.32000 1.000 71.98758  ? 189 GLU A N     1 
ATOM   1462 C  CA    . GLU A 1 189 ? 38.25600 -22.09800 -26.82200 1.000 72.49817  ? 189 GLU A CA    1 
ATOM   1463 C  C     . GLU A 1 189 ? 38.97400 -23.25700 -27.52800 1.000 71.82703  ? 189 GLU A C     1 
ATOM   1464 O  O     . GLU A 1 189 ? 39.04700 -24.34800 -26.93100 1.000 76.21703  ? 189 GLU A O     1 
ATOM   1465 C  CB    . GLU A 1 189 ? 36.73000 -22.14100 -26.95300 1.000 74.01677  ? 189 GLU A CB    1 
ATOM   1466 C  CG    . GLU A 1 189 ? 36.21200 -22.18400 -28.38100 1.000 77.56983  ? 189 GLU A CG    1 
ATOM   1467 C  CD    . GLU A 1 189 ? 36.38400 -20.92500 -29.20600 1.000 83.78899  ? 189 GLU A CD    1 
ATOM   1468 O  OE1   . GLU A 1 189 ? 35.93200 -19.86000 -28.75500 1.000 87.19730  ? 189 GLU A OE1   1 
ATOM   1469 O  OE2   . GLU A 1 189 ? 36.97800 -21.01300 -30.29800 1.000 86.42878  ? 189 GLU A OE2   1 
ATOM   1470 N  N     . GLU A 1 190 ? 39.49500 -23.02700 -28.73800 1.000 61.95743  ? 190 GLU A N     1 
ATOM   1471 C  CA    . GLU A 1 190 ? 40.25100 -24.07900 -29.47100 1.000 60.65990  ? 190 GLU A CA    1 
ATOM   1472 C  C     . GLU A 1 190 ? 41.75300 -23.81600 -29.31600 1.000 62.33116  ? 190 GLU A C     1 
ATOM   1473 O  O     . GLU A 1 190 ? 42.49800 -24.18700 -30.24700 1.000 60.60727  ? 190 GLU A O     1 
ATOM   1474 C  CB    . GLU A 1 190 ? 39.84900 -24.09100 -30.94700 1.000 70.55056  ? 190 GLU A CB    1 
ATOM   1475 C  CG    . GLU A 1 190 ? 38.34900 -24.13900 -31.18300 1.000 79.37531  ? 190 GLU A CG    1 
ATOM   1476 C  CD    . GLU A 1 190 ? 37.99100 -24.25300 -32.65500 1.000 99.65669  ? 190 GLU A CD    1 
ATOM   1477 O  OE1   . GLU A 1 190 ? 38.76900 -23.71700 -33.46800 1.000 102.62546 ? 190 GLU A OE1   1 
ATOM   1478 O  OE2   . GLU A 1 190 ? 37.06600 -25.00700 -32.99400 1.000 101.95433 ? 190 GLU A OE2   1 
ATOM   1479 N  N     . LEU A 1 191 ? 42.17100 -23.19900 -28.20200 1.000 63.93661  ? 191 LEU A N     1 
ATOM   1480 C  CA    . LEU A 1 191 ? 43.57300 -22.89300 -27.94200 1.000 56.19621  ? 191 LEU A CA    1 
ATOM   1481 C  C     . LEU A 1 191 ? 44.23700 -22.24700 -29.15100 1.000 62.07323  ? 191 LEU A C     1 
ATOM   1482 O  O     . LEU A 1 191 ? 45.43700 -22.40700 -29.35200 1.000 62.88649  ? 191 LEU A O     1 
ATOM   1483 C  CB    . LEU A 1 191 ? 44.37000 -24.13100 -27.50800 1.000 49.73228  ? 191 LEU A CB    1 
ATOM   1484 C  CG    . LEU A 1 191 ? 44.14400 -24.69500 -26.10500 1.000 54.56444  ? 191 LEU A CG    1 
ATOM   1485 C  CD1   . LEU A 1 191 ? 45.27000 -25.65400 -25.74600 1.000 62.63646  ? 191 LEU A CD1   1 
ATOM   1486 C  CD2   . LEU A 1 191 ? 44.03800 -23.57800 -25.08500 1.000 67.15279  ? 191 LEU A CD2   1 
ATOM   1487 N  N     A SER A 1 192 ? 43.48000 -21.47000 -29.93600 1.000 64.58143  ? 192 SER A N     1 
ATOM   1488 C  CA    A SER A 1 192 ? 44.08800 -20.69300 -31.00800 1.000 55.31979  ? 192 SER A CA    1 
ATOM   1489 C  C     A SER A 1 192 ? 44.52200 -19.34400 -30.44500 1.000 56.84366  ? 192 SER A C     1 
ATOM   1490 O  O     A SER A 1 192 ? 43.80100 -18.72800 -29.65700 1.000 64.32613  ? 192 SER A O     1 
ATOM   1491 C  CB    A SER A 1 192 ? 43.11500 -20.49100 -32.17600 1.000 61.35209  ? 192 SER A CB    1 
ATOM   1492 O  OG    A SER A 1 192 ? 42.85300 -21.70200 -32.87400 1.000 77.67510  ? 192 SER A OG    1 
ATOM   1493 N  N     . HIS A 1 193 ? 45.68900 -18.87800 -30.88100 1.000 57.47005  ? 193 HIS A N     1 
ATOM   1494 C  CA    . HIS A 1 193 ? 46.30000 -17.67800 -30.31500 1.000 57.44110  ? 193 HIS A CA    1 
ATOM   1495 C  C     . HIS A 1 193 ? 45.49800 -16.42500 -30.66100 1.000 54.12491  ? 193 HIS A C     1 
ATOM   1496 O  O     . HIS A 1 193 ? 45.25800 -16.14500 -31.84000 1.000 63.14968  ? 193 HIS A O     1 
ATOM   1497 C  CB    . HIS A 1 193 ? 47.74500 -17.53000 -30.76500 1.000 55.40401  ? 193 HIS A CB    1 
ATOM   1498 C  CG    . HIS A 1 193 ? 48.45800 -16.40100 -30.09200 1.000 50.28498  ? 193 HIS A CG    1 
ATOM   1499 N  ND1   . HIS A 1 193 ? 48.83100 -16.45600 -28.76600 1.000 48.44002  ? 193 HIS A ND1   1 
ATOM   1500 C  CD2   . HIS A 1 193 ? 48.84100 -15.18300 -30.54200 1.000 57.61217  ? 193 HIS A CD2   1 
ATOM   1501 C  CE1   . HIS A 1 193 ? 49.43700 -15.33100 -28.43400 1.000 56.72259  ? 193 HIS A CE1   1 
ATOM   1502 N  NE2   . HIS A 1 193 ? 49.45200 -14.54000 -29.49200 1.000 68.16080  ? 193 HIS A NE2   1 
ATOM   1503 N  N     . LEU A 1 194 ? 45.07900 -15.67400 -29.64500 1.000 52.89582  ? 194 LEU A N     1 
ATOM   1504 C  CA    . LEU A 1 194 ? 44.35800 -14.41800 -29.81200 1.000 55.44349  ? 194 LEU A CA    1 
ATOM   1505 C  C     . LEU A 1 194 ? 45.25500 -13.20300 -29.60800 1.000 57.47531  ? 194 LEU A C     1 
ATOM   1506 O  O     . LEU A 1 194 ? 45.08700 -12.19300 -30.29500 1.000 63.99188  ? 194 LEU A O     1 
ATOM   1507 C  CB    . LEU A 1 194 ? 43.17900 -14.34700 -28.83800 1.000 52.13520  ? 194 LEU A CB    1 
ATOM   1508 C  CG    . LEU A 1 194 ? 41.94300 -15.17300 -29.19600 1.000 57.51479  ? 194 LEU A CG    1 
ATOM   1509 C  CD1   . LEU A 1 194 ? 40.76800 -14.82500 -28.28900 1.000 63.75238  ? 194 LEU A CD1   1 
ATOM   1510 C  CD2   . LEU A 1 194 ? 41.56900 -14.99100 -30.65400 1.000 72.85610  ? 194 LEU A CD2   1 
ATOM   1511 N  N     . GLY A 1 195 ? 46.20300 -13.27300 -28.68300 1.000 51.87464  ? 195 GLY A N     1 
ATOM   1512 C  CA    . GLY A 1 195 ? 47.07200 -12.14400 -28.43200 1.000 55.63825  ? 195 GLY A CA    1 
ATOM   1513 C  C     . GLY A 1 195 ? 47.90100 -12.36600 -27.18400 1.000 52.16152  ? 195 GLY A C     1 
ATOM   1514 O  O     . GLY A 1 195 ? 47.97400 -13.47600 -26.65300 1.000 56.33044  ? 195 GLY A O     1 
ATOM   1515 N  N     . SER A 1 196 ? 48.51400 -11.27900 -26.71900 1.000 47.90048  ? 196 SER A N     1 
ATOM   1516 C  CA    . SER A 1 196 ? 49.41300 -11.33700 -25.57400 1.000 46.05026  ? 196 SER A CA    1 
ATOM   1517 C  C     . SER A 1 196 ? 49.02500 -10.27800 -24.55400 1.000 50.47447  ? 196 SER A C     1 
ATOM   1518 O  O     . SER A 1 196 ? 48.50000 -9.21800  -24.90200 1.000 54.10649  ? 196 SER A O     1 
ATOM   1519 C  CB    . SER A 1 196 ? 50.87300 -11.14000 -26.00200 1.000 54.58023  ? 196 SER A CB    1 
ATOM   1520 O  OG    . SER A 1 196 ? 51.27100 -12.14900 -26.91500 1.000 59.83875  ? 196 SER A OG    1 
ATOM   1521 N  N     . ALA A 1 197 ? 49.29400 -10.57200 -23.28500 1.000 46.25818  ? 197 ALA A N     1 
ATOM   1522 C  CA    . ALA A 1 197 ? 48.87800 -9.67300  -22.22400 1.000 50.05074  ? 197 ALA A CA    1 
ATOM   1523 C  C     . ALA A 1 197 ? 49.77200 -9.82600  -21.00500 1.000 46.81088  ? 197 ALA A C     1 
ATOM   1524 O  O     . ALA A 1 197 ? 50.52600 -10.79100 -20.86700 1.000 47.69519  ? 197 ALA A O     1 
ATOM   1525 C  CB    . ALA A 1 197 ? 47.41400 -9.90800  -21.83800 1.000 56.03040  ? 197 ALA A CB    1 
ATOM   1526 N  N     . ILE A 1 198 ? 49.70000 -8.81900  -20.14600 1.000 46.06342  ? 198 ILE A N     1 
ATOM   1527 C  CA    . ILE A 1 198 ? 50.36000 -8.79200  -18.85000 1.000 43.70524  ? 198 ILE A CA    1 
ATOM   1528 C  C     . ILE A 1 198 ? 49.27100 -8.88700  -17.78900 1.000 55.72247  ? 198 ILE A C     1 
ATOM   1529 O  O     . ILE A 1 198 ? 48.36900 -8.04200  -17.73400 1.000 57.41478  ? 198 ILE A O     1 
ATOM   1530 C  CB    . ILE A 1 198 ? 51.21100 -7.52800  -18.67800 1.000 38.92046  ? 198 ILE A CB    1 
ATOM   1531 C  CG1   . ILE A 1 198 ? 52.44500 -7.61600  -19.57000 1.000 48.29263  ? 198 ILE A CG1   1 
ATOM   1532 C  CG2   . ILE A 1 198 ? 51.61400 -7.34700  -17.23200 1.000 48.85849  ? 198 ILE A CG2   1 
ATOM   1533 C  CD1   . ILE A 1 198 ? 53.26600 -8.86100  -19.34900 1.000 55.44086  ? 198 ILE A CD1   1 
ATOM   1534 N  N     . PHE A 1 199 ? 49.36000 -9.91300  -16.94500 1.000 52.13257  ? 199 PHE A N     1 
ATOM   1535 C  CA    . PHE A 1 199 ? 48.43300 -10.13100 -15.83700 1.000 48.69268  ? 199 PHE A CA    1 
ATOM   1536 C  C     . PHE A 1 199 ? 49.26600 -10.18800 -14.56700 1.000 54.72761  ? 199 PHE A C     1 
ATOM   1537 O  O     . PHE A 1 199 ? 49.71300 -11.26800 -14.15100 1.000 63.24969  ? 199 PHE A O     1 
ATOM   1538 C  CB    . PHE A 1 199 ? 47.62400 -11.41100 -16.01800 1.000 52.75633  ? 199 PHE A CB    1 
ATOM   1539 C  CG    . PHE A 1 199 ? 46.65400 -11.37100 -17.16000 1.000 50.63239  ? 199 PHE A CG    1 
ATOM   1540 C  CD1   . PHE A 1 199 ? 45.48700 -10.63500 -17.05900 1.000 54.88553  ? 199 PHE A CD1   1 
ATOM   1541 C  CD2   . PHE A 1 199 ? 46.89000 -12.09000 -18.32000 1.000 46.90562  ? 199 PHE A CD2   1 
ATOM   1542 C  CE1   . PHE A 1 199 ? 44.57700 -10.60500 -18.09800 1.000 52.92740  ? 199 PHE A CE1   1 
ATOM   1543 C  CE2   . PHE A 1 199 ? 45.98400 -12.06200 -19.36400 1.000 48.71374  ? 199 PHE A CE2   1 
ATOM   1544 C  CZ    . PHE A 1 199 ? 44.82500 -11.31700 -19.25200 1.000 51.93517  ? 199 PHE A CZ    1 
ATOM   1545 N  N     . PRO A 1 200 ? 49.52500 -9.04000  -13.94100 1.000 55.11187  ? 200 PRO A N     1 
ATOM   1546 C  CA    . PRO A 1 200 ? 50.48900 -9.01200  -12.82900 1.000 58.00959  ? 200 PRO A CA    1 
ATOM   1547 C  C     . PRO A 1 200 ? 50.12800 -9.96200  -11.70600 1.000 63.06019  ? 200 PRO A C     1 
ATOM   1548 O  O     . PRO A 1 200 ? 50.98300 -10.72200 -11.23400 1.000 68.67929  ? 200 PRO A O     1 
ATOM   1549 C  CB    . PRO A 1 200 ? 50.45100 -7.54500  -12.37700 1.000 64.92884  ? 200 PRO A CB    1 
ATOM   1550 C  CG    . PRO A 1 200 ? 49.95900 -6.79000  -13.56100 1.000 64.94989  ? 200 PRO A CG    1 
ATOM   1551 C  CD    . PRO A 1 200 ? 48.97800 -7.70600  -14.23400 1.000 62.47591  ? 200 PRO A CD    1 
ATOM   1552 N  N     . ASP A 1 201 ? 48.86300 -9.93200  -11.29200 1.000 68.50295  ? 201 ASP A N     1 
ATOM   1553 C  CA    . ASP A 1 201 ? 48.40300 -10.78100 -10.16400 1.000 69.01617  ? 201 ASP A CA    1 
ATOM   1554 C  C     . ASP A 1 201 ? 48.52000 -12.26100 -10.54300 1.000 67.13700  ? 201 ASP A C     1 
ATOM   1555 O  O     . ASP A 1 201 ? 48.83300 -13.07100 -9.64900  1.000 67.21332  ? 201 ASP A O     1 
ATOM   1556 C  CB    . ASP A 1 201 ? 46.99200 -10.34400 -9.78400  1.000 76.55128  ? 201 ASP A CB    1 
ATOM   1557 C  CG    . ASP A 1 201 ? 46.97800 -9.01200  -9.06700  1.000 80.98339  ? 201 ASP A CG    1 
ATOM   1558 O  OD1   . ASP A 1 201 ? 48.04300 -8.61900  -8.55200  1.000 81.78612  ? 201 ASP A OD1   1 
ATOM   1559 O  OD2   . ASP A 1 201 ? 45.90800 -8.38300  -9.03500  1.000 79.08053  ? 201 ASP A OD2   1 
ATOM   1560 N  N     . VAL A 1 202 ? 48.28100 -12.59800 -11.81300 1.000 60.20459  ? 202 VAL A N     1 
ATOM   1561 C  CA    . VAL A 1 202 ? 48.37400 -13.97300 -12.29600 1.000 58.29383  ? 202 VAL A CA    1 
ATOM   1562 C  C     . VAL A 1 202 ? 49.82000 -14.43800 -12.41300 1.000 57.90694  ? 202 VAL A C     1 
ATOM   1563 O  O     . VAL A 1 202 ? 50.12300 -15.61800 -12.18600 1.000 56.37255  ? 202 VAL A O     1 
ATOM   1564 C  CB    . VAL A 1 202 ? 47.63100 -14.09600 -13.63900 1.000 58.59913  ? 202 VAL A CB    1 
ATOM   1565 C  CG1   . VAL A 1 202 ? 47.64800 -15.52700 -14.13800 1.000 53.32745  ? 202 VAL A CG1   1 
ATOM   1566 C  CG2   . VAL A 1 202 ? 46.19800 -13.61700 -13.48200 1.000 67.11857  ? 202 VAL A CG2   1 
ATOM   1567 N  N     . ALA A 1 203 ? 50.73600 -13.52600 -12.73700 1.000 54.62497  ? 203 ALA A N     1 
ATOM   1568 C  CA    . ALA A 1 203 ? 52.13900 -13.88700 -12.89300 1.000 51.74041  ? 203 ALA A CA    1 
ATOM   1569 C  C     . ALA A 1 203 ? 52.77200 -14.35000 -11.59100 1.000 55.59088  ? 203 ALA A C     1 
ATOM   1570 O  O     . ALA A 1 203 ? 53.81800 -15.00400 -11.62700 1.000 62.56803  ? 203 ALA A O     1 
ATOM   1571 C  CB    . ALA A 1 203 ? 52.92300 -12.70500 -13.45800 1.000 61.07838  ? 203 ALA A CB    1 
ATOM   1572 N  N     . LEU A 1 204 ? 52.17300 -14.01100 -10.45000 1.000 53.17216  ? 204 LEU A N     1 
ATOM   1573 C  CA    . LEU A 1 204 ? 52.73600 -14.40300 -9.16300  1.000 55.55666  ? 204 LEU A CA    1 
ATOM   1574 C  C     . LEU A 1 204 ? 52.75500 -15.91800 -8.97500  1.000 59.28079  ? 204 LEU A C     1 
ATOM   1575 O  O     . LEU A 1 204 ? 53.59300 -16.43700 -8.22900  1.000 68.46084  ? 204 LEU A O     1 
ATOM   1576 C  CB    . LEU A 1 204 ? 51.94800 -13.72700 -8.04000  1.000 53.05636  ? 204 LEU A CB    1 
ATOM   1577 C  CG    . LEU A 1 204 ? 52.31400 -14.01400 -6.58300  1.000 58.08854  ? 204 LEU A CG    1 
ATOM   1578 C  CD1   . LEU A 1 204 ? 53.77800 -13.71000 -6.31500  1.000 63.86555  ? 204 LEU A CD1   1 
ATOM   1579 C  CD2   . LEU A 1 204 ? 51.42500 -13.19600 -5.66100  1.000 63.86818  ? 204 LEU A CD2   1 
ATOM   1580 N  N     . MET A 1 205 ? 51.86500 -16.64400 -9.64700  1.000 59.86244  ? 205 MET A N     1 
ATOM   1581 C  CA    . MET A 1 205 ? 51.76700 -18.08300 -9.42900  1.000 58.15434  ? 205 MET A CA    1 
ATOM   1582 C  C     . MET A 1 205 ? 52.96200 -18.80900 -10.04000 1.000 56.29359  ? 205 MET A C     1 
ATOM   1583 O  O     . MET A 1 205 ? 53.32400 -18.57200 -11.19600 1.000 54.16965  ? 205 MET A O     1 
ATOM   1584 C  CB    . MET A 1 205 ? 50.46700 -18.60800 -10.03600 1.000 62.84701  ? 205 MET A CB    1 
ATOM   1585 C  CG    . MET A 1 205 ? 49.21300 -18.12700 -9.32800  1.000 67.17648  ? 205 MET A CG    1 
ATOM   1586 S  SD    . MET A 1 205 ? 47.71900 -18.85600 -10.02900 1.000 70.82691  ? 205 MET A SD    1 
ATOM   1587 C  CE    . MET A 1 205 ? 47.72600 -18.11900 -11.66100 1.000 61.19418  ? 205 MET A CE    1 
ATOM   1588 N  N     . ASN A 1 206 ? 53.57400 -19.69200 -9.25700  1.000 53.71697  ? 206 ASN A N     1 
ATOM   1589 C  CA    . ASN A 1 206 ? 54.69200 -20.50500 -9.71000  1.000 57.87799  ? 206 ASN A CA    1 
ATOM   1590 C  C     . ASN A 1 206 ? 54.20500 -21.69600 -10.53600 1.000 57.92537  ? 206 ASN A C     1 
ATOM   1591 O  O     . ASN A 1 206 ? 53.00800 -21.97800 -10.62500 1.000 60.19669  ? 206 ASN A O     1 
ATOM   1592 C  CB    . ASN A 1 206 ? 55.50300 -20.97500 -8.50800  1.000 65.95528  ? 206 ASN A CB    1 
ATOM   1593 C  CG    . ASN A 1 206 ? 56.30800 -19.85800 -7.88800  1.000 61.53369  ? 206 ASN A CG    1 
ATOM   1594 O  OD1   . ASN A 1 206 ? 56.98000 -19.10500 -8.58800  1.000 66.31848  ? 206 ASN A OD1   1 
ATOM   1595 N  ND2   . ASN A 1 206 ? 56.20900 -19.71600 -6.57300  1.000 62.91544  ? 206 ASN A ND2   1 
ATOM   1596 N  N     . HIS A 1 207 ? 55.15500 -22.40900 -11.14100 1.000 60.67570  ? 207 HIS A N     1 
ATOM   1597 C  CA    . HIS A 1 207 ? 54.85300 -23.49400 -12.06600 1.000 58.78600  ? 207 HIS A CA    1 
ATOM   1598 C  C     . HIS A 1 207 ? 54.86200 -24.84900 -11.36600 1.000 65.50785  ? 207 HIS A C     1 
ATOM   1599 O  O     . HIS A 1 207 ? 55.63400 -25.08500 -10.43200 1.000 69.25830  ? 207 HIS A O     1 
ATOM   1600 C  CB    . HIS A 1 207 ? 55.84300 -23.54500 -13.23000 1.000 52.54577  ? 207 HIS A CB    1 
ATOM   1601 C  CG    . HIS A 1 207 ? 55.74100 -24.80400 -14.03300 1.000 52.49840  ? 207 HIS A CG    1 
ATOM   1602 N  ND1   . HIS A 1 207 ? 54.88700 -24.93700 -15.10600 1.000 56.78049  ? 207 HIS A ND1   1 
ATOM   1603 C  CD2   . HIS A 1 207 ? 56.36300 -25.99900 -13.89900 1.000 57.48847  ? 207 HIS A CD2   1 
ATOM   1604 C  CE1   . HIS A 1 207 ? 54.99800 -26.15400 -15.60800 1.000 59.32290  ? 207 HIS A CE1   1 
ATOM   1605 N  NE2   . HIS A 1 207 ? 55.88800 -26.81900 -14.89300 1.000 60.73360  ? 207 HIS A NE2   1 
ATOM   1606 N  N     . SER A 1 208 ? 53.99700 -25.74500 -11.84200 1.000 69.02407  ? 208 SER A N     1 
ATOM   1607 C  CA    . SER A 1 208 ? 54.07400 -27.16300 -11.51900 1.000 70.25053  ? 208 SER A CA    1 
ATOM   1608 C  C     . SER A 1 208 ? 53.55700 -27.96900 -12.70300 1.000 71.85598  ? 208 SER A C     1 
ATOM   1609 O  O     . SER A 1 208 ? 52.63900 -27.54200 -13.40700 1.000 72.79820  ? 208 SER A O     1 
ATOM   1610 C  CB    . SER A 1 208 ? 53.28700 -27.53000 -10.26000 1.000 73.22983  ? 208 SER A CB    1 
ATOM   1611 O  OG    . SER A 1 208 ? 53.34200 -28.93000 -10.04200 1.000 76.28546  ? 208 SER A OG    1 
ATOM   1612 N  N     . CYS A 1 209 ? 54.15100 -29.14200 -12.91500 1.000 65.77368  ? 209 CYS A N     1 
ATOM   1613 C  CA    . CYS A 1 209 ? 53.66600 -30.05100 -13.94500 1.000 71.79282  ? 209 CYS A CA    1 
ATOM   1614 C  C     . CYS A 1 209 ? 52.45900 -30.85000 -13.47800 1.000 68.71087  ? 209 CYS A C     1 
ATOM   1615 O  O     . CYS A 1 209 ? 51.87200 -31.59100 -14.27200 1.000 73.75884  ? 209 CYS A O     1 
ATOM   1616 C  CB    . CYS A 1 209 ? 54.77800 -30.99300 -14.41900 1.000 78.43046  ? 209 CYS A CB    1 
ATOM   1617 S  SG    . CYS A 1 209 ? 56.32200 -30.15500 -14.88100 1.000 68.18449  ? 209 CYS A SG    1 
ATOM   1618 N  N     A CYS A 1 210 ? 52.08200 -30.73300 -12.20900 1.000 71.12958  ? 210 CYS A N     1 
ATOM   1619 C  CA    A CYS A 1 210 ? 50.78000 -31.19100 -11.73900 1.000 70.97430  ? 210 CYS A CA    1 
ATOM   1620 C  C     A CYS A 1 210 ? 50.06900 -30.00700 -11.09300 1.000 69.85574  ? 210 CYS A C     1 
ATOM   1621 O  O     A CYS A 1 210 ? 49.92700 -29.94600 -9.86500  1.000 70.67426  ? 210 CYS A O     1 
ATOM   1622 C  CB    A CYS A 1 210 ? 50.92300 -32.34300 -10.74600 1.000 79.05948  ? 210 CYS A CB    1 
ATOM   1623 S  SG    A CYS A 1 210 ? 51.98500 -31.98800 -9.33200  1.000 125.36240 ? 210 CYS A SG    1 
ATOM   1624 N  N     . PRO A 1 211 ? 49.62500 -29.03800 -11.89600 1.000 59.85454  ? 211 PRO A N     1 
ATOM   1625 C  CA    . PRO A 1 211 ? 49.08000 -27.80200 -11.32500 1.000 64.25770  ? 211 PRO A CA    1 
ATOM   1626 C  C     . PRO A 1 211 ? 47.74200 -28.04600 -10.65100 1.000 61.29682  ? 211 PRO A C     1 
ATOM   1627 O  O     . PRO A 1 211 ? 47.01300 -28.98500 -10.97600 1.000 64.25770  ? 211 PRO A O     1 
ATOM   1628 C  CB    . PRO A 1 211 ? 48.91800 -26.89300 -12.54600 1.000 62.43907  ? 211 PRO A CB    1 
ATOM   1629 C  CG    . PRO A 1 211 ? 48.68300 -27.84500 -13.67000 1.000 57.69902  ? 211 PRO A CG    1 
ATOM   1630 C  CD    . PRO A 1 211 ? 49.52800 -29.05300 -13.36600 1.000 58.73862  ? 211 PRO A CD    1 
ATOM   1631 N  N     . ASN A 1 212 ? 47.41400 -27.17500 -9.69900  1.000 58.96760  ? 212 ASN A N     1 
ATOM   1632 C  CA    . ASN A 1 212 ? 46.11700 -27.22100 -9.03700  1.000 58.25698  ? 212 ASN A CA    1 
ATOM   1633 C  C     . ASN A 1 212 ? 45.13900 -26.14800 -9.51000  1.000 58.32015  ? 212 ASN A C     1 
ATOM   1634 O  O     . ASN A 1 212 ? 43.98900 -26.15100 -9.06100  1.000 64.60511  ? 212 ASN A O     1 
ATOM   1635 C  CB    . ASN A 1 212 ? 46.29800 -27.11200 -7.51600  1.000 59.80717  ? 212 ASN A CB    1 
ATOM   1636 C  CG    . ASN A 1 212 ? 47.13700 -25.91500 -7.10900  1.000 61.14417  ? 212 ASN A CG    1 
ATOM   1637 O  OD1   . ASN A 1 212 ? 47.40300 -25.02600 -7.91700  1.000 72.49553  ? 212 ASN A OD1   1 
ATOM   1638 N  ND2   . ASN A 1 212 ? 47.56100 -25.88800 -5.85000  1.000 59.56504  ? 212 ASN A ND2   1 
ATOM   1639 N  N     . VAL A 1 213 ? 45.54300 -25.24300 -10.40800 1.000 50.36130  ? 213 VAL A N     1 
ATOM   1640 C  CA    . VAL A 1 213 ? 44.62200 -24.29500 -11.02600 1.000 51.16929  ? 213 VAL A CA    1 
ATOM   1641 C  C     . VAL A 1 213 ? 44.84400 -24.17300 -12.52700 1.000 59.63610  ? 213 VAL A C     1 
ATOM   1642 O  O     . VAL A 1 213 ? 45.88600 -24.55300 -13.06600 1.000 60.21248  ? 213 VAL A O     1 
ATOM   1643 C  CB    . VAL A 1 213 ? 44.71800 -22.89000 -10.39500 1.000 44.79221  ? 213 VAL A CB    1 
ATOM   1644 C  CG1   . VAL A 1 213 ? 44.41300 -22.95100 -8.91400  1.000 54.74867  ? 213 VAL A CG1   1 
ATOM   1645 C  CG2   . VAL A 1 213 ? 46.08800 -22.28500 -10.65100 1.000 55.86196  ? 213 VAL A CG2   1 
ATOM   1646 N  N     . ILE A 1 214 ? 43.82300 -23.63800 -13.19900 1.000 55.55140  ? 214 ILE A N     1 
ATOM   1647 C  CA    . ILE A 1 214 ? 43.89000 -23.28900 -14.61100 1.000 52.09835  ? 214 ILE A CA    1 
ATOM   1648 C  C     . ILE A 1 214 ? 43.42800 -21.85000 -14.79300 1.000 52.80370  ? 214 ILE A C     1 
ATOM   1649 O  O     . ILE A 1 214 ? 42.49700 -21.38300 -14.11600 1.000 55.66457  ? 214 ILE A O     1 
ATOM   1650 C  CB    . ILE A 1 214 ? 43.02200 -24.21900 -15.49300 1.000 49.42172  ? 214 ILE A CB    1 
ATOM   1651 C  CG1   . ILE A 1 214 ? 43.65000 -25.59900 -15.64100 1.000 59.25974  ? 214 ILE A CG1   1 
ATOM   1652 C  CG2   . ILE A 1 214 ? 42.76300 -23.60700 -16.86500 1.000 52.78001  ? 214 ILE A CG2   1 
ATOM   1653 C  CD1   . ILE A 1 214 ? 42.79900 -26.54300 -16.46200 1.000 57.34898  ? 214 ILE A CD1   1 
ATOM   1654 N  N     . VAL A 1 215 ? 44.15600 -21.13300 -15.64900 1.000 49.29538  ? 215 VAL A N     1 
ATOM   1655 C  CA    . VAL A 1 215 ? 43.85900 -19.75900 -16.02800 1.000 49.22959  ? 215 VAL A CA    1 
ATOM   1656 C  C     . VAL A 1 215 ? 43.07100 -19.81200 -17.33300 1.000 53.84067  ? 215 VAL A C     1 
ATOM   1657 O  O     . VAL A 1 215 ? 43.54300 -20.37300 -18.33000 1.000 51.29036  ? 215 VAL A O     1 
ATOM   1658 C  CB    . VAL A 1 215 ? 45.14100 -18.92500 -16.16900 1.000 48.56898  ? 215 VAL A CB    1 
ATOM   1659 C  CG1   . VAL A 1 215 ? 44.80200 -17.47900 -16.50800 1.000 51.04296  ? 215 VAL A CG1   1 
ATOM   1660 C  CG2   . VAL A 1 215 ? 45.97600 -19.01000 -14.89300 1.000 53.63801  ? 215 VAL A CG2   1 
ATOM   1661 N  N     . THR A 1 216 ? 41.89100 -19.21000 -17.34200 1.000 55.70668  ? 216 THR A N     1 
ATOM   1662 C  CA    . THR A 1 216 ? 41.08100 -19.04100 -18.54000 1.000 49.20327  ? 216 THR A CA    1 
ATOM   1663 C  C     . THR A 1 216 ? 40.81800 -17.55700 -18.73900 1.000 51.43775  ? 216 THR A C     1 
ATOM   1664 O  O     . THR A 1 216 ? 41.20100 -16.72800 -17.91400 1.000 57.24897  ? 216 THR A O     1 
ATOM   1665 C  CB    . THR A 1 216 ? 39.76000 -19.81900 -18.44000 1.000 56.19621  ? 216 THR A CB    1 
ATOM   1666 O  OG1   . THR A 1 216 ? 38.98700 -19.32300 -17.34000 1.000 64.12085  ? 216 THR A OG1   1 
ATOM   1667 C  CG2   . THR A 1 216 ? 40.01800 -21.31100 -18.27200 1.000 64.17085  ? 216 THR A CG2   1 
ATOM   1668 N  N     . TYR A 1 217 ? 40.21500 -17.20000 -19.86600 1.000 52.62473  ? 217 TYR A N     1 
ATOM   1669 C  CA    . TYR A 1 217 ? 40.08100 -15.79200 -20.20300 1.000 52.37207  ? 217 TYR A CA    1 
ATOM   1670 C  C     . TYR A 1 217 ? 38.64500 -15.48700 -20.58800 1.000 58.67282  ? 217 TYR A C     1 
ATOM   1671 O  O     . TYR A 1 217 ? 38.03700 -16.21400 -21.38000 1.000 65.47890  ? 217 TYR A O     1 
ATOM   1672 C  CB    . TYR A 1 217 ? 41.04100 -15.42200 -21.32700 1.000 55.90670  ? 217 TYR A CB    1 
ATOM   1673 C  CG    . TYR A 1 217 ? 42.46600 -15.78400 -20.98900 1.000 52.62999  ? 217 TYR A CG    1 
ATOM   1674 C  CD1   . TYR A 1 217 ? 43.20300 -15.02600 -20.08700 1.000 53.56169  ? 217 TYR A CD1   1 
ATOM   1675 C  CD2   . TYR A 1 217 ? 43.06100 -16.91000 -21.53800 1.000 56.88314  ? 217 TYR A CD2   1 
ATOM   1676 C  CE1   . TYR A 1 217 ? 44.50800 -15.36600 -19.76000 1.000 49.79808  ? 217 TYR A CE1   1 
ATOM   1677 C  CE2   . TYR A 1 217 ? 44.36600 -17.25900 -21.21900 1.000 57.84378  ? 217 TYR A CE2   1 
ATOM   1678 C  CZ    . TYR A 1 217 ? 45.08400 -16.48300 -20.32800 1.000 50.73240  ? 217 TYR A CZ    1 
ATOM   1679 O  OH    . TYR A 1 217 ? 46.38200 -16.82000 -20.00500 1.000 44.57113  ? 217 TYR A OH    1 
ATOM   1680 N  N     . LYS A 1 218 ? 38.12000 -14.40600 -20.02300 1.000 58.10434  ? 218 LYS A N     1 
ATOM   1681 C  CA    . LYS A 1 218 ? 36.81700 -13.82200 -20.32200 1.000 62.97597  ? 218 LYS A CA    1 
ATOM   1682 C  C     . LYS A 1 218 ? 37.05100 -12.43800 -20.92500 1.000 60.92046  ? 218 LYS A C     1 
ATOM   1683 O  O     . LYS A 1 218 ? 37.23500 -11.45000 -20.20500 1.000 64.94463  ? 218 LYS A O     1 
ATOM   1684 C  CB    . LYS A 1 218 ? 35.91700 -13.78000 -19.07800 1.000 69.04249  ? 218 LYS A CB    1 
ATOM   1685 C  CG    . LYS A 1 218 ? 34.42300 -13.60500 -19.40400 1.000 63.12862  ? 218 LYS A CG    1 
ATOM   1686 C  CD    . LYS A 1 218 ? 33.54500 -13.76000 -18.16200 1.000 71.86388  ? 218 LYS A CD    1 
ATOM   1687 C  CE    . LYS A 1 218 ? 33.47400 -15.21800 -17.70900 1.000 77.45929  ? 218 LYS A CE    1 
ATOM   1688 N  NZ    . LYS A 1 218 ? 32.76000 -15.40200 -16.40800 1.000 70.77428  ? 218 LYS A NZ    1 
ATOM   1689 N  N     . GLY A 1 219 ? 37.17200 -12.39200 -22.24700 1.000 60.79940  ? 219 GLY A N     1 
ATOM   1690 C  CA    . GLY A 1 219 ? 37.63500 -11.18700 -22.89600 1.000 61.29419  ? 219 GLY A CA    1 
ATOM   1691 C  C     . GLY A 1 219 ? 39.08600 -10.92300 -22.57700 1.000 63.92345  ? 219 GLY A C     1 
ATOM   1692 O  O     . GLY A 1 219 ? 39.95800 -11.73800 -22.89500 1.000 64.85251  ? 219 GLY A O     1 
ATOM   1693 N  N     . THR A 1 220 ? 39.35300 -9.79100  -21.93500 1.000 64.64196  ? 220 THR A N     1 
ATOM   1694 C  CA    . THR A 1 220 ? 40.69400 -9.44100  -21.49500 1.000 62.22588  ? 220 THR A CA    1 
ATOM   1695 C  C     . THR A 1 220 ? 40.89200 -9.72900  -20.01500 1.000 61.74425  ? 220 THR A C     1 
ATOM   1696 O  O     . THR A 1 220 ? 41.93700 -9.37600  -19.45700 1.000 54.30914  ? 220 THR A O     1 
ATOM   1697 C  CB    . THR A 1 220 ? 40.97400 -7.96400  -21.78000 1.000 59.12025  ? 220 THR A CB    1 
ATOM   1698 O  OG1   . THR A 1 220 ? 40.13400 -7.15200  -20.94800 1.000 62.92860  ? 220 THR A OG1   1 
ATOM   1699 C  CG2   . THR A 1 220 ? 40.67900 -7.63800  -23.23600 1.000 60.63359  ? 220 THR A CG2   1 
ATOM   1700 N  N     . LEU A 1 221 ? 39.90200 -10.34500 -19.36600 1.000 63.78133  ? 221 LEU A N     1 
ATOM   1701 C  CA    . LEU A 1 221 ? 39.98800 -10.69400 -17.95400 1.000 63.59184  ? 221 LEU A CA    1 
ATOM   1702 C  C     . LEU A 1 221 ? 40.51100 -12.11300 -17.75900 1.000 61.10469  ? 221 LEU A C     1 
ATOM   1703 O  O     . LEU A 1 221 ? 39.95200 -13.06400 -18.30900 1.000 60.35197  ? 221 LEU A O     1 
ATOM   1704 C  CB    . LEU A 1 221 ? 38.61700 -10.55600 -17.29300 1.000 65.56312  ? 221 LEU A CB    1 
ATOM   1705 C  CG    . LEU A 1 221 ? 38.51600 -10.98100 -15.82500 1.000 66.97382  ? 221 LEU A CG    1 
ATOM   1706 C  CD1   . LEU A 1 221 ? 39.24300 -9.99400  -14.92500 1.000 68.27924  ? 221 LEU A CD1   1 
ATOM   1707 C  CD2   . LEU A 1 221 ? 37.06200 -11.13900 -15.39300 1.000 67.55547  ? 221 LEU A CD2   1 
ATOM   1708 N  N     . ALA A 1 222 ? 41.57900 -12.25800 -16.98100 1.000 54.18018  ? 222 ALA A N     1 
ATOM   1709 C  CA    . ALA A 1 222 ? 42.08500 -13.57600 -16.64100 1.000 50.77451  ? 222 ALA A CA    1 
ATOM   1710 C  C     . ALA A 1 222 ? 41.32200 -14.08700 -15.42900 1.000 56.90682  ? 222 ALA A C     1 
ATOM   1711 O  O     . ALA A 1 222 ? 41.04000 -13.32800 -14.50100 1.000 66.26321  ? 222 ALA A O     1 
ATOM   1712 C  CB    . ALA A 1 222 ? 43.58100 -13.53300 -16.33900 1.000 55.90407  ? 222 ALA A CB    1 
ATOM   1713 N  N     . GLU A 1 223 ? 40.95100 -15.36000 -15.45300 1.000 58.00695  ? 223 GLU A N     1 
ATOM   1714 C  CA    . GLU A 1 223 ? 40.27200 -15.98300 -14.33100 1.000 60.12563  ? 223 GLU A CA    1 
ATOM   1715 C  C     . GLU A 1 223 ? 41.05400 -17.22400 -13.92900 1.000 60.37829  ? 223 GLU A C     1 
ATOM   1716 O  O     . GLU A 1 223 ? 41.55600 -17.95300 -14.78900 1.000 60.00193  ? 223 GLU A O     1 
ATOM   1717 C  CB    . GLU A 1 223 ? 38.82700 -16.35300 -14.69900 1.000 60.48620  ? 223 GLU A CB    1 
ATOM   1718 C  CG    . GLU A 1 223 ? 37.94500 -15.15800 -15.03500 1.000 63.81028  ? 223 GLU A CG    1 
ATOM   1719 C  CD    . GLU A 1 223 ? 36.47100 -15.52100 -15.11700 1.000 78.07252  ? 223 GLU A CD    1 
ATOM   1720 O  OE1   . GLU A 1 223 ? 36.15400 -16.63000 -15.60500 1.000 79.38583  ? 223 GLU A OE1   1 
ATOM   1721 O  OE2   . GLU A 1 223 ? 35.63100 -14.69900 -14.68600 1.000 78.93841  ? 223 GLU A OE2   1 
ATOM   1722 N  N     . VAL A 1 224 ? 41.11600 -17.48800 -12.62700 1.000 55.05660  ? 224 VAL A N     1 
ATOM   1723 C  CA    . VAL A 1 224 ? 41.92000 -18.56900 -12.07900 1.000 52.05887  ? 224 VAL A CA    1 
ATOM   1724 C  C     . VAL A 1 224 ? 40.98800 -19.41900 -11.24400 1.000 57.93853  ? 224 VAL A C     1 
ATOM   1725 O  O     . VAL A 1 224 ? 40.47100 -18.94200 -10.21300 1.000 64.86304  ? 224 VAL A O     1 
ATOM   1726 C  CB    . VAL A 1 224 ? 43.09300 -18.06000 -11.22400 1.000 51.80358  ? 224 VAL A CB    1 
ATOM   1727 C  CG1   . VAL A 1 224 ? 43.90200 -19.23200 -10.69300 1.000 50.19812  ? 224 VAL A CG1   1 
ATOM   1728 C  CG2   . VAL A 1 224 ? 43.97200 -17.13300 -12.03300 1.000 53.22480  ? 224 VAL A CG2   1 
ATOM   1729 N  N     . ARG A 1 225 ? 40.81000 -20.68300 -11.67500 1.000 49.68490  ? 225 ARG A N     1 
ATOM   1730 C  CA    . ARG A 1 225 ? 39.90800 -21.65300 -11.06500 1.000 54.38810  ? 225 ARG A CA    1 
ATOM   1731 C  C     . ARG A 1 225 ? 40.65400 -22.93900 -10.72900 1.000 53.87225  ? 225 ARG A C     1 
ATOM   1732 O  O     . ARG A 1 225 ? 41.52800 -23.37500 -11.48100 1.000 56.26464  ? 225 ARG A O     1 
ATOM   1733 C  CB    . ARG A 1 225 ? 38.72800 -21.97700 -11.99700 1.000 61.74425  ? 225 ARG A CB    1 
ATOM   1734 C  CG    . ARG A 1 225 ? 37.65000 -20.90300 -12.05300 1.000 70.85586  ? 225 ARG A CG    1 
ATOM   1735 C  CD    . ARG A 1 225 ? 36.43700 -21.35800 -12.86200 1.000 68.53716  ? 225 ARG A CD    1 
ATOM   1736 N  NE    . ARG A 1 225 ? 35.43700 -20.30400 -12.99600 1.000 70.57688  ? 225 ARG A NE    1 
ATOM   1737 C  CZ    . ARG A 1 225 ? 35.51300 -19.30000 -13.86000 1.000 74.72475  ? 225 ARG A CZ    1 
ATOM   1738 N  NH1   . ARG A 1 225 ? 36.53100 -19.18600 -14.70000 1.000 74.37207  ? 225 ARG A NH1   1 
ATOM   1739 N  NH2   . ARG A 1 225 ? 34.54400 -18.38800 -13.88300 1.000 72.63502  ? 225 ARG A NH2   1 
ATOM   1740 N  N     . ALA A 1 226 ? 40.28200 -23.55600 -9.61000  1.000 58.27804  ? 226 ALA A N     1 
ATOM   1741 C  CA    . ALA A 1 226 ? 40.93500 -24.77500 -9.14500  1.000 55.44612  ? 226 ALA A CA    1 
ATOM   1742 C  C     . ALA A 1 226 ? 40.55600 -26.00200 -9.96800  1.000 62.36537  ? 226 ALA A C     1 
ATOM   1743 O  O     . ALA A 1 226 ? 39.38800 -26.20800 -10.30700 1.000 70.66900  ? 226 ALA A O     1 
ATOM   1744 C  CB    . ALA A 1 226 ? 40.59300 -25.02800 -7.68200  1.000 59.75716  ? 226 ALA A CB    1 
ATOM   1745 N  N     . VAL A 1 227 ? 41.55900 -26.82500 -10.28400 1.000 63.95767  ? 227 VAL A N     1 
ATOM   1746 C  CA    . VAL A 1 227 ? 41.33400 -28.13200 -10.89100 1.000 62.13113  ? 227 VAL A CA    1 
ATOM   1747 C  C     . VAL A 1 227 ? 41.70700 -29.26500 -9.95300  1.000 70.26106  ? 227 VAL A C     1 
ATOM   1748 O  O     . VAL A 1 227 ? 41.54900 -30.44000 -10.31600 1.000 74.51683  ? 227 VAL A O     1 
ATOM   1749 C  CB    . VAL A 1 227 ? 42.10800 -28.27400 -12.21100 1.000 52.36944  ? 227 VAL A CB    1 
ATOM   1750 C  CG1   . VAL A 1 227 ? 41.64200 -27.22000 -13.18500 1.000 55.69615  ? 227 VAL A CG1   1 
ATOM   1751 C  CG2   . VAL A 1 227 ? 43.60500 -28.19000 -11.95100 1.000 58.01748  ? 227 VAL A CG2   1 
ATOM   1752 N  N     . GLN A 1 228 ? 42.20300 -28.95000 -8.75900  1.000 68.03447  ? 228 GLN A N     1 
ATOM   1753 C  CA    . GLN A 1 228 ? 42.32600 -29.89700 -7.66300  1.000 67.75549  ? 228 GLN A CA    1 
ATOM   1754 C  C     . GLN A 1 228 ? 41.83400 -29.20900 -6.39800  1.000 70.16104  ? 228 GLN A C     1 
ATOM   1755 O  O     . GLN A 1 228 ? 41.74600 -27.98000 -6.33700  1.000 76.91712  ? 228 GLN A O     1 
ATOM   1756 C  CB    . GLN A 1 228 ? 43.76700 -30.39300 -7.49500  1.000 71.04010  ? 228 GLN A CB    1 
ATOM   1757 C  CG    . GLN A 1 228 ? 44.32800 -31.09800 -8.72000  1.000 68.51874  ? 228 GLN A CG    1 
ATOM   1758 C  CD    . GLN A 1 228 ? 45.73000 -31.62400 -8.49100  1.000 70.96114  ? 228 GLN A CD    1 
ATOM   1759 O  OE1   . GLN A 1 228 ? 46.00500 -32.28500 -7.48900  1.000 84.96282  ? 228 GLN A OE1   1 
ATOM   1760 N  NE2   . GLN A 1 228 ? 46.62800 -31.33000 -9.42200  1.000 68.41873  ? 228 GLN A NE2   1 
ATOM   1761 N  N     . GLU A 1 229 ? 41.50100 -30.00500 -5.38500  1.000 71.72965  ? 229 GLU A N     1 
ATOM   1762 C  CA    . GLU A 1 229 ? 41.16700 -29.41400 -4.09700  1.000 74.29312  ? 229 GLU A CA    1 
ATOM   1763 C  C     . GLU A 1 229 ? 42.38900 -28.70600 -3.52700  1.000 75.52748  ? 229 GLU A C     1 
ATOM   1764 O  O     . GLU A 1 229 ? 43.49600 -29.25300 -3.52700  1.000 70.68216  ? 229 GLU A O     1 
ATOM   1765 C  CB    . GLU A 1 229 ? 40.66400 -30.46900 -3.11100  1.000 71.59543  ? 229 GLU A CB    1 
ATOM   1766 C  CG    . GLU A 1 229 ? 40.55900 -29.90900 -1.69500  1.000 90.32662  ? 229 GLU A CG    1 
ATOM   1767 C  CD    . GLU A 1 229 ? 39.69500 -30.73600 -0.76600  1.000 97.94332  ? 229 GLU A CD    1 
ATOM   1768 O  OE1   . GLU A 1 229 ? 39.06000 -31.70200 -1.23600  1.000 111.41336 ? 229 GLU A OE1   1 
ATOM   1769 O  OE2   . GLU A 1 229 ? 39.63500 -30.39800 0.43700   1.000 94.37711  ? 229 GLU A OE2   1 
ATOM   1770 N  N     . ILE A 1 230 ? 42.18600 -27.48000 -3.05100  1.000 79.72798  ? 230 ILE A N     1 
ATOM   1771 C  CA    . ILE A 1 230 ? 43.24300 -26.67800 -2.45200  1.000 74.59315  ? 230 ILE A CA    1 
ATOM   1772 C  C     . ILE A 1 230 ? 42.84700 -26.39800 -1.01400  1.000 77.02502  ? 230 ILE A C     1 
ATOM   1773 O  O     . ILE A 1 230 ? 41.73000 -25.94000 -0.74600  1.000 78.09884  ? 230 ILE A O     1 
ATOM   1774 C  CB    . ILE A 1 230 ? 43.48000 -25.35700 -3.20600  1.000 63.57341  ? 230 ILE A CB    1 
ATOM   1775 C  CG1   . ILE A 1 230 ? 43.78000 -25.61200 -4.68000  1.000 60.01772  ? 230 ILE A CG1   1 
ATOM   1776 C  CG2   . ILE A 1 230 ? 44.61400 -24.58100 -2.56200  1.000 72.53501  ? 230 ILE A CG2   1 
ATOM   1777 C  CD1   . ILE A 1 230 ? 43.88600 -24.33300 -5.49900  1.000 62.15745  ? 230 ILE A CD1   1 
ATOM   1778 N  N     . LYS A 1 231 ? 43.75300 -26.68800 -0.09700  1.000 75.03794  ? 231 LYS A N     1 
ATOM   1779 C  CA    . LYS A 1 231 ? 43.52100 -26.53100 1.32300   1.000 73.45091  ? 231 LYS A CA    1 
ATOM   1780 C  C     . LYS A 1 231 ? 44.29200 -25.32300 1.82300   1.000 72.07180  ? 231 LYS A C     1 
ATOM   1781 O  O     . LYS A 1 231 ? 45.27000 -24.90200 1.19800   1.000 78.50941  ? 231 LYS A O     1 
ATOM   1782 C  CB    . LYS A 1 231 ? 43.94600 -27.78900 2.09400   1.000 81.38344  ? 231 LYS A CB    1 
ATOM   1783 C  CG    . LYS A 1 231 ? 43.21500 -29.06100 1.67100   1.000 87.12624  ? 231 LYS A CG    1 
ATOM   1784 C  CD    . LYS A 1 231 ? 43.42200 -30.19000 2.67600   1.000 86.59459  ? 231 LYS A CD    1 
ATOM   1785 C  CE    . LYS A 1 231 ? 43.10900 -31.55400 2.07600   1.000 94.63766  ? 231 LYS A CE    1 
ATOM   1786 N  NZ    . LYS A 1 231 ? 41.67600 -31.91700 2.30600   1.000 99.64879  ? 231 LYS A NZ    1 
ATOM   1787 N  N     . PRO A 1 232 ? 43.88400 -24.73500 2.94500   1.000 74.86687  ? 232 PRO A N     1 
ATOM   1788 C  CA    . PRO A 1 232 ? 44.64900 -23.61500 3.50300   1.000 75.94068  ? 232 PRO A CA    1 
ATOM   1789 C  C     . PRO A 1 232 ? 46.11100 -23.98500 3.71000   1.000 76.77499  ? 232 PRO A C     1 
ATOM   1790 O  O     . PRO A 1 232 ? 46.44000 -25.07800 4.17500   1.000 81.26501  ? 232 PRO A O     1 
ATOM   1791 C  CB    . PRO A 1 232 ? 43.94600 -23.34300 4.83800   1.000 77.92250  ? 232 PRO A CB    1 
ATOM   1792 C  CG    . PRO A 1 232 ? 42.54500 -23.79600 4.61000   1.000 76.60392  ? 232 PRO A CG    1 
ATOM   1793 C  CD    . PRO A 1 232 ? 42.64000 -24.98400 3.69600   1.000 74.42734  ? 232 PRO A CD    1 
ATOM   1794 N  N     . GLY A 1 233 ? 46.99200 -23.06200 3.32600   1.000 77.49350  ? 233 GLY A N     1 
ATOM   1795 C  CA    . GLY A 1 233 ? 48.42100 -23.24700 3.43400   1.000 84.90228  ? 233 GLY A CA    1 
ATOM   1796 C  C     . GLY A 1 233 ? 49.09400 -23.81000 2.20000   1.000 81.94140  ? 233 GLY A C     1 
ATOM   1797 O  O     . GLY A 1 233 ? 50.31900 -23.70000 2.07900   1.000 86.37615  ? 233 GLY A O     1 
ATOM   1798 N  N     . GLU A 1 234 ? 48.34200 -24.39800 1.27500   1.000 86.17086  ? 234 GLU A N     1 
ATOM   1799 C  CA    . GLU A 1 234 ? 48.96500 -24.96800 0.09200   1.000 84.68384  ? 234 GLU A CA    1 
ATOM   1800 C  C     . GLU A 1 234 ? 49.21900 -23.87500 -0.93600  1.000 83.07049  ? 234 GLU A C     1 
ATOM   1801 O  O     . GLU A 1 234 ? 48.44700 -22.92100 -1.06500  1.000 82.74413  ? 234 GLU A O     1 
ATOM   1802 C  CB    . GLU A 1 234 ? 48.08300 -26.04700 -0.54000  1.000 84.43381  ? 234 GLU A CB    1 
ATOM   1803 C  CG    . GLU A 1 234 ? 47.77100 -27.24600 0.33500   1.000 97.59065  ? 234 GLU A CG    1 
ATOM   1804 C  CD    . GLU A 1 234 ? 47.06900 -28.34800 -0.44100  1.000 98.54866  ? 234 GLU A CD    1 
ATOM   1805 O  OE1   . GLU A 1 234 ? 46.26500 -28.02200 -1.34400  1.000 87.68420  ? 234 GLU A OE1   1 
ATOM   1806 O  OE2   . GLU A 1 234 ? 47.32500 -29.53700 -0.15200  1.000 104.66255 ? 234 GLU A OE2   1 
ATOM   1807 N  N     . GLU A 1 235 ? 50.31200 -24.02600 -1.67400  1.000 82.51252  ? 235 GLU A N     1 
ATOM   1808 C  CA    . GLU A 1 235 ? 50.67600 -23.05200 -2.69000  1.000 81.16236  ? 235 GLU A CA    1 
ATOM   1809 C  C     . GLU A 1 235 ? 49.86700 -23.29000 -3.95600  1.000 79.50427  ? 235 GLU A C     1 
ATOM   1810 O  O     . GLU A 1 235 ? 49.55800 -24.43200 -4.30400  1.000 79.17528  ? 235 GLU A O     1 
ATOM   1811 C  CB    . GLU A 1 235 ? 52.16900 -23.11900 -3.00900  1.000 81.14131  ? 235 GLU A CB    1 
ATOM   1812 C  CG    . GLU A 1 235 ? 52.58500 -22.14500 -4.10500  1.000 79.86484  ? 235 GLU A CG    1 
ATOM   1813 C  CD    . GLU A 1 235 ? 54.05800 -21.80600 -4.08100  1.000 80.25962  ? 235 GLU A CD    1 
ATOM   1814 O  OE1   . GLU A 1 235 ? 54.80900 -22.45600 -3.32100  1.000 81.58083  ? 235 GLU A OE1   1 
ATOM   1815 O  OE2   . GLU A 1 235 ? 54.46000 -20.88500 -4.82700  1.000 79.34899  ? 235 GLU A OE2   1 
ATOM   1816 N  N     . VAL A 1 236 ? 49.52000 -22.20600 -4.64100  1.000 72.27446  ? 236 VAL A N     1 
ATOM   1817 C  CA    . VAL A 1 236 ? 48.74900 -22.27600 -5.87600  1.000 57.06474  ? 236 VAL A CA    1 
ATOM   1818 C  C     . VAL A 1 236 ? 49.72300 -22.36200 -7.04500  1.000 61.67582  ? 236 VAL A C     1 
ATOM   1819 O  O     . VAL A 1 236 ? 50.54600 -21.46100 -7.24200  1.000 68.17923  ? 236 VAL A O     1 
ATOM   1820 C  CB    . VAL A 1 236 ? 47.83400 -21.05100 -6.01800  1.000 52.46155  ? 236 VAL A CB    1 
ATOM   1821 C  CG1   . VAL A 1 236 ? 46.96400 -21.18500 -7.23400  1.000 65.18940  ? 236 VAL A CG1   1 
ATOM   1822 C  CG2   . VAL A 1 236 ? 46.97700 -20.88200 -4.77800  1.000 61.88900  ? 236 VAL A CG2   1 
ATOM   1823 N  N     . PHE A 1 237 ? 49.63600 -23.44600 -7.81700  1.000 60.66780  ? 237 PHE A N     1 
ATOM   1824 C  CA    . PHE A 1 237 ? 50.54500 -23.71700 -8.92600  1.000 54.91448  ? 237 PHE A CA    1 
ATOM   1825 C  C     . PHE A 1 237 ? 49.74700 -23.80500 -10.22000 1.000 58.07012  ? 237 PHE A C     1 
ATOM   1826 O  O     . PHE A 1 237 ? 48.74800 -24.52800 -10.28800 1.000 56.71206  ? 237 PHE A O     1 
ATOM   1827 C  CB    . PHE A 1 237 ? 51.32500 -25.02000 -8.71900  1.000 60.30460  ? 237 PHE A CB    1 
ATOM   1828 C  CG    . PHE A 1 237 ? 52.31800 -24.98000 -7.58600  1.000 64.26034  ? 237 PHE A CG    1 
ATOM   1829 C  CD1   . PHE A 1 237 ? 53.51800 -24.29900 -7.71700  1.000 62.80227  ? 237 PHE A CD1   1 
ATOM   1830 C  CD2   . PHE A 1 237 ? 52.06300 -25.65200 -6.39900  1.000 66.04213  ? 237 PHE A CD2   1 
ATOM   1831 C  CE1   . PHE A 1 237 ? 54.43600 -24.27800 -6.67800  1.000 65.96580  ? 237 PHE A CE1   1 
ATOM   1832 C  CE2   . PHE A 1 237 ? 52.97800 -25.63400 -5.35700  1.000 66.70273  ? 237 PHE A CE2   1 
ATOM   1833 C  CZ    . PHE A 1 237 ? 54.16400 -24.94700 -5.49700  1.000 67.94236  ? 237 PHE A CZ    1 
ATOM   1834 N  N     . THR A 1 238 ? 50.18600 -23.07200 -11.23900 1.000 55.65667  ? 238 THR A N     1 
ATOM   1835 C  CA    . THR A 1 238 ? 49.70800 -23.22100 -12.60800 1.000 50.59291  ? 238 THR A CA    1 
ATOM   1836 C  C     . THR A 1 238 ? 50.78400 -23.87800 -13.47200 1.000 54.89342  ? 238 THR A C     1 
ATOM   1837 O  O     . THR A 1 238 ? 51.92400 -24.06600 -13.04200 1.000 58.50701  ? 238 THR A O     1 
ATOM   1838 C  CB    . THR A 1 238 ? 49.29400 -21.86000 -13.18000 1.000 47.87942  ? 238 THR A CB    1 
ATOM   1839 O  OG1   . THR A 1 238 ? 48.50400 -22.05200 -14.35900 1.000 59.84139  ? 238 THR A OG1   1 
ATOM   1840 C  CG2   . THR A 1 238 ? 50.51900 -21.02900 -13.52100 1.000 56.01987  ? 238 THR A CG2   1 
ATOM   1841 N  N     . SER A 1 239 ? 50.41000 -24.25400 -14.69700 1.000 50.07706  ? 239 SER A N     1 
ATOM   1842 C  CA    . SER A 1 239 ? 51.35900 -24.77600 -15.67500 1.000 47.98996  ? 239 SER A CA    1 
ATOM   1843 C  C     . SER A 1 239 ? 51.74600 -23.69600 -16.67900 1.000 52.08256  ? 239 SER A C     1 
ATOM   1844 O  O     . SER A 1 239 ? 50.88100 -22.97400 -17.18600 1.000 54.95659  ? 239 SER A O     1 
ATOM   1845 C  CB    . SER A 1 239 ? 50.77500 -25.98200 -16.41000 1.000 61.21260  ? 239 SER A CB    1 
ATOM   1846 O  OG    . SER A 1 239 ? 51.68400 -26.45300 -17.38900 1.000 59.88086  ? 239 SER A OG    1 
ATOM   1847 N  N     . TYR A 1 240 ? 53.04700 -23.59600 -16.97300 1.000 50.30340  ? 240 TYR A N     1 
ATOM   1848 C  CA    . TYR A 1 240 ? 53.53200 -22.62700 -17.94800 1.000 43.61839  ? 240 TYR A CA    1 
ATOM   1849 C  C     . TYR A 1 240 ? 53.63200 -23.16100 -19.36900 1.000 50.12180  ? 240 TYR A C     1 
ATOM   1850 O  O     . TYR A 1 240 ? 53.74200 -22.36100 -20.30600 1.000 64.56564  ? 240 TYR A O     1 
ATOM   1851 C  CB    . TYR A 1 240 ? 54.93100 -22.14200 -17.55600 1.000 47.02932  ? 240 TYR A CB    1 
ATOM   1852 C  CG    . TYR A 1 240 ? 55.03300 -21.37100 -16.26100 1.000 48.64267  ? 240 TYR A CG    1 
ATOM   1853 C  CD1   . TYR A 1 240 ? 53.91500 -21.11800 -15.48100 1.000 51.95886  ? 240 TYR A CD1   1 
ATOM   1854 C  CD2   . TYR A 1 240 ? 56.26100 -20.90200 -15.81500 1.000 51.48512  ? 240 TYR A CD2   1 
ATOM   1855 C  CE1   . TYR A 1 240 ? 54.01600 -20.41500 -14.29600 1.000 59.49661  ? 240 TYR A CE1   1 
ATOM   1856 C  CE2   . TYR A 1 240 ? 56.37300 -20.19900 -14.63400 1.000 52.73527  ? 240 TYR A CE2   1 
ATOM   1857 C  CZ    . TYR A 1 240 ? 55.24900 -19.95900 -13.87600 1.000 59.80717  ? 240 TYR A CZ    1 
ATOM   1858 O  OH    . TYR A 1 240 ? 55.35600 -19.25800 -12.69600 1.000 65.96054  ? 240 TYR A OH    1 
ATOM   1859 N  N     . ILE A 1 241 ? 53.59000 -24.47700 -19.56300 1.000 50.91137  ? 241 ILE A N     1 
ATOM   1860 C  CA    . ILE A 1 241 ? 53.99500 -25.08900 -20.82500 1.000 57.39372  ? 241 ILE A CA    1 
ATOM   1861 C  C     . ILE A 1 241 ? 53.03700 -26.21600 -21.18300 1.000 59.30448  ? 241 ILE A C     1 
ATOM   1862 O  O     . ILE A 1 241 ? 52.17300 -26.60700 -20.39600 1.000 60.06246  ? 241 ILE A O     1 
ATOM   1863 C  CB    . ILE A 1 241 ? 55.45300 -25.60500 -20.80300 1.000 53.46431  ? 241 ILE A CB    1 
ATOM   1864 C  CG1   . ILE A 1 241 ? 55.68900 -26.56800 -19.63900 1.000 51.50618  ? 241 ILE A CG1   1 
ATOM   1865 C  CG2   . ILE A 1 241 ? 56.43900 -24.44700 -20.75300 1.000 54.00121  ? 241 ILE A CG2   1 
ATOM   1866 C  CD1   . ILE A 1 241 ? 56.96100 -27.38600 -19.78800 1.000 57.01473  ? 241 ILE A CD1   1 
ATOM   1867 N  N     . ASP A 1 242 ? 53.21400 -26.73800 -22.39400 1.000 68.80035  ? 242 ASP A N     1 
ATOM   1868 C  CA    . ASP A 1 242 ? 52.49200 -27.92800 -22.82800 1.000 69.72415  ? 242 ASP A CA    1 
ATOM   1869 C  C     . ASP A 1 242 ? 53.01900 -29.14600 -22.07800 1.000 71.37435  ? 242 ASP A C     1 
ATOM   1870 O  O     . ASP A 1 242 ? 54.20900 -29.47000 -22.15600 1.000 73.16667  ? 242 ASP A O     1 
ATOM   1871 C  CB    . ASP A 1 242 ? 52.65600 -28.11700 -24.33700 1.000 77.33032  ? 242 ASP A CB    1 
ATOM   1872 C  CG    . ASP A 1 242 ? 51.71300 -29.17500 -24.91700 1.000 75.90384  ? 242 ASP A CG    1 
ATOM   1873 O  OD1   . ASP A 1 242 ? 51.21200 -30.03900 -24.16300 1.000 77.58035  ? 242 ASP A OD1   1 
ATOM   1874 O  OD2   . ASP A 1 242 ? 51.48500 -29.15000 -26.14700 1.000 72.80610  ? 242 ASP A OD2   1 
ATOM   1875 N  N     . LEU A 1 243 ? 52.12600 -29.81800 -21.35700 1.000 62.57592  ? 243 LEU A N     1 
ATOM   1876 C  CA    . LEU A 1 243 ? 52.46900 -30.91000 -20.46000 1.000 55.85670  ? 243 LEU A CA    1 
ATOM   1877 C  C     . LEU A 1 243 ? 52.48800 -32.26300 -21.16100 1.000 58.49912  ? 243 LEU A C     1 
ATOM   1878 O  O     . LEU A 1 243 ? 52.62200 -33.29400 -20.49500 1.000 66.82643  ? 243 LEU A O     1 
ATOM   1879 C  CB    . LEU A 1 243 ? 51.46700 -30.94200 -19.30500 1.000 53.45904  ? 243 LEU A CB    1 
ATOM   1880 C  CG    . LEU A 1 243 ? 51.41400 -29.68600 -18.43200 1.000 56.09883  ? 243 LEU A CG    1 
ATOM   1881 C  CD1   . LEU A 1 243 ? 50.29700 -29.78700 -17.41000 1.000 54.11701  ? 243 LEU A CD1   1 
ATOM   1882 C  CD2   . LEU A 1 243 ? 52.74900 -29.47000 -17.73500 1.000 63.48656  ? 243 LEU A CD2   1 
ATOM   1883 N  N     . LEU A 1 244 ? 52.35300 -32.28000 -22.48800 1.000 60.70728  ? 244 LEU A N     1 
ATOM   1884 C  CA    . LEU A 1 244 ? 52.32900 -33.54100 -23.22200 1.000 58.90180  ? 244 LEU A CA    1 
ATOM   1885 C  C     . LEU A 1 244 ? 53.65900 -34.28600 -23.13900 1.000 63.76291  ? 244 LEU A C     1 
ATOM   1886 O  O     . LEU A 1 244 ? 53.68200 -35.52000 -23.07200 1.000 78.08305  ? 244 LEU A O     1 
ATOM   1887 C  CB    . LEU A 1 244 ? 51.95800 -33.26000 -24.67800 1.000 57.79114  ? 244 LEU A CB    1 
ATOM   1888 C  CG    . LEU A 1 244 ? 51.85100 -34.43100 -25.65000 1.000 69.67941  ? 244 LEU A CG    1 
ATOM   1889 C  CD1   . LEU A 1 244 ? 50.80100 -35.42100 -25.18000 1.000 68.20291  ? 244 LEU A CD1   1 
ATOM   1890 C  CD2   . LEU A 1 244 ? 51.52900 -33.92200 -27.05000 1.000 80.24120  ? 244 LEU A CD2   1 
ATOM   1891 N  N     . TYR A 1 245 ? 54.76500 -33.56300 -23.14500 1.000 60.26249  ? 245 TYR A N     1 
ATOM   1892 C  CA    . TYR A 1 245 ? 56.08200 -34.11200 -23.44100 1.000 67.37124  ? 245 TYR A CA    1 
ATOM   1893 C  C     . TYR A 1 245 ? 56.76800 -34.67200 -22.19700 1.000 69.68730  ? 245 TYR A C     1 
ATOM   1894 O  O     . TYR A 1 245 ? 56.39800 -34.34100 -21.06600 1.000 70.25053  ? 245 TYR A O     1 
ATOM   1895 C  CB    . TYR A 1 245 ? 56.92400 -33.04300 -24.13300 1.000 66.83696  ? 245 TYR A CB    1 
ATOM   1896 C  CG    . TYR A 1 245 ? 56.24900 -32.61900 -25.41700 1.000 70.17947  ? 245 TYR A CG    1 
ATOM   1897 C  CD1   . TYR A 1 245 ? 56.37300 -33.38700 -26.56900 1.000 76.49338  ? 245 TYR A CD1   1 
ATOM   1898 C  CD2   . TYR A 1 245 ? 55.43400 -31.49600 -25.46500 1.000 71.51384  ? 245 TYR A CD2   1 
ATOM   1899 C  CE1   . TYR A 1 245 ? 55.73500 -33.02800 -27.74300 1.000 74.94320  ? 245 TYR A CE1   1 
ATOM   1900 C  CE2   . TYR A 1 245 ? 54.79200 -31.12800 -26.63700 1.000 71.74018  ? 245 TYR A CE2   1 
ATOM   1901 C  CZ    . TYR A 1 245 ? 54.94600 -31.89700 -27.77200 1.000 73.07455  ? 245 TYR A CZ    1 
ATOM   1902 O  OH    . TYR A 1 245 ? 54.30900 -31.53600 -28.93900 1.000 75.62486  ? 245 TYR A OH    1 
ATOM   1903 N  N     . PRO A 1 246 ? 57.77700 -35.53300 -22.37600 1.000 67.92393  ? 246 PRO A N     1 
ATOM   1904 C  CA    . PRO A 1 246 ? 58.46100 -36.13500 -21.22100 1.000 70.17947  ? 246 PRO A CA    1 
ATOM   1905 C  C     . PRO A 1 246 ? 59.19400 -35.10400 -20.37400 1.000 73.38248  ? 246 PRO A C     1 
ATOM   1906 O  O     . PRO A 1 246 ? 59.33200 -33.93300 -20.72900 1.000 76.48022  ? 246 PRO A O     1 
ATOM   1907 C  CB    . PRO A 1 246 ? 59.43500 -37.13900 -21.84900 1.000 77.49350  ? 246 PRO A CB    1 
ATOM   1908 C  CG    . PRO A 1 246 ? 58.95300 -37.34900 -23.23700 1.000 72.77452  ? 246 PRO A CG    1 
ATOM   1909 C  CD    . PRO A 1 246 ? 58.24500 -36.10300 -23.65200 1.000 71.69807  ? 246 PRO A CD    1 
ATOM   1910 N  N     . THR A 1 247 ? 59.68900 -35.58600 -19.23000 1.000 76.62761  ? 247 THR A N     1 
ATOM   1911 C  CA    . THR A 1 247 ? 60.28400 -34.70800 -18.22500 1.000 76.25651  ? 247 THR A CA    1 
ATOM   1912 C  C     . THR A 1 247 ? 61.47000 -33.92000 -18.76400 1.000 76.84079  ? 247 THR A C     1 
ATOM   1913 O  O     . THR A 1 247 ? 61.57700 -32.70700 -18.53700 1.000 80.04118  ? 247 THR A O     1 
ATOM   1914 C  CB    . THR A 1 247 ? 60.71600 -35.53700 -17.01700 1.000 76.61182  ? 247 THR A CB    1 
ATOM   1915 O  OG1   . THR A 1 247 ? 59.57400 -36.19700 -16.46200 1.000 78.10410  ? 247 THR A OG1   1 
ATOM   1916 C  CG2   . THR A 1 247 ? 61.36200 -34.65000 -15.95700 1.000 72.84294  ? 247 THR A CG2   1 
ATOM   1917 N  N     . GLU A 1 248 ? 62.38200 -34.58300 -19.47200 1.000 74.83266  ? 248 GLU A N     1 
ATOM   1918 C  CA    . GLU A 1 248 ? 63.55300 -33.85300 -19.93900 1.000 78.27254  ? 248 GLU A CA    1 
ATOM   1919 C  C     . GLU A 1 248 ? 63.18500 -32.76900 -20.94500 1.000 79.50427  ? 248 GLU A C     1 
ATOM   1920 O  O     . GLU A 1 248 ? 63.74000 -31.67000 -20.89600 1.000 83.39947  ? 248 GLU A O     1 
ATOM   1921 C  CB    . GLU A 1 248 ? 64.56800 -34.80500 -20.56600 1.000 85.68396  ? 248 GLU A CB    1 
ATOM   1922 C  CG    . GLU A 1 248 ? 65.83100 -34.08400 -21.02300 1.000 93.45331  ? 248 GLU A CG    1 
ATOM   1923 C  CD    . GLU A 1 248 ? 66.53900 -34.79500 -22.16400 1.000 110.59221 ? 248 GLU A CD    1 
ATOM   1924 O  OE1   . GLU A 1 248 ? 65.90200 -35.63800 -22.82900 1.000 117.06667 ? 248 GLU A OE1   1 
ATOM   1925 O  OE2   . GLU A 1 248 ? 67.72700 -34.49600 -22.40800 1.000 113.15567 ? 248 GLU A OE2   1 
ATOM   1926 N  N     . ASP A 1 249 ? 62.20000 -33.02900 -21.81200 1.000 83.04417  ? 249 ASP A N     1 
ATOM   1927 C  CA    . ASP A 1 249 ? 61.75100 -32.01000 -22.76000 1.000 81.58873  ? 249 ASP A CA    1 
ATOM   1928 C  C     . ASP A 1 249 ? 61.12100 -30.81700 -22.05100 1.000 78.98842  ? 249 ASP A C     1 
ATOM   1929 O  O     . ASP A 1 249 ? 61.41400 -29.65100 -22.37300 1.000 78.05146  ? 249 ASP A O     1 
ATOM   1930 C  CB    . ASP A 1 249 ? 60.74600 -32.63100 -23.73300 1.000 81.80718  ? 249 ASP A CB    1 
ATOM   1931 C  CG    . ASP A 1 249 ? 61.37500 -33.68100 -24.64000 1.000 90.83458  ? 249 ASP A CG    1 
ATOM   1932 O  OD1   . ASP A 1 249 ? 62.58900 -33.93800 -24.50000 1.000 100.49889 ? 249 ASP A OD1   1 
ATOM   1933 O  OD2   . ASP A 1 249 ? 60.65500 -34.25800 -25.48400 1.000 85.15495  ? 249 ASP A OD2   1 
ATOM   1934 N  N     . ARG A 1 250 ? 60.30900 -31.09900 -21.03300 1.000 71.84546  ? 250 ARG A N     1 
ATOM   1935 C  CA    . ARG A 1 250 ? 59.65600 -30.03700 -20.28400 1.000 66.32901  ? 250 ARG A CA    1 
ATOM   1936 C  C     . ARG A 1 250 ? 60.68300 -29.16700 -19.58300 1.000 71.63754  ? 250 ARG A C     1 
ATOM   1937 O  O     . ARG A 1 250 ? 60.62100 -27.93500 -19.65700 1.000 70.71901  ? 250 ARG A O     1 
ATOM   1938 C  CB    . ARG A 1 250 ? 58.68600 -30.65000 -19.27200 1.000 67.57652  ? 250 ARG A CB    1 
ATOM   1939 C  CG    . ARG A 1 250 ? 57.53300 -31.41900 -19.89800 1.000 73.14824  ? 250 ARG A CG    1 
ATOM   1940 C  CD    . ARG A 1 250 ? 56.38900 -31.57800 -18.91300 1.000 65.60787  ? 250 ARG A CD    1 
ATOM   1941 N  NE    . ARG A 1 250 ? 56.86400 -32.14100 -17.65500 1.000 66.42112  ? 250 ARG A NE    1 
ATOM   1942 C  CZ    . ARG A 1 250 ? 57.09900 -33.42900 -17.44000 1.000 71.65596  ? 250 ARG A CZ    1 
ATOM   1943 N  NH1   . ARG A 1 250 ? 56.92300 -34.33400 -18.38800 1.000 71.44278  ? 250 ARG A NH1   1 
ATOM   1944 N  NH2   . ARG A 1 250 ? 57.54700 -33.81500 -16.25100 1.000 82.74150  ? 250 ARG A NH2   1 
ATOM   1945 N  N     . ASN A 1 251 ? 61.63900 -29.79100 -18.89500 1.000 77.06713  ? 251 ASN A N     1 
ATOM   1946 C  CA    . ASN A 1 251 ? 62.62400 -29.00000 -18.17100 1.000 79.31740  ? 251 ASN A CA    1 
ATOM   1947 C  C     . ASN A 1 251 ? 63.61500 -28.30700 -19.10600 1.000 80.37279  ? 251 ASN A C     1 
ATOM   1948 O  O     . ASN A 1 251 ? 64.12300 -27.23700 -18.76700 1.000 80.41754  ? 251 ASN A O     1 
ATOM   1949 C  CB    . ASN A 1 251 ? 63.34800 -29.88200 -17.15600 1.000 79.04895  ? 251 ASN A CB    1 
ATOM   1950 C  CG    . ASN A 1 251 ? 62.63900 -29.91800 -15.81500 1.000 77.82775  ? 251 ASN A CG    1 
ATOM   1951 O  OD1   . ASN A 1 251 ? 62.40700 -28.87800 -15.19600 1.000 77.92513  ? 251 ASN A OD1   1 
ATOM   1952 N  ND2   . ASN A 1 251 ? 62.28900 -31.11500 -15.36000 1.000 84.04429  ? 251 ASN A ND2   1 
ATOM   1953 N  N     . ASP A 1 252 ? 63.89000 -28.87600 -20.28400 1.000 78.25149  ? 252 ASP A N     1 
ATOM   1954 C  CA    . ASP A 1 252 ? 64.65000 -28.15500 -21.30200 1.000 77.43560  ? 252 ASP A CA    1 
ATOM   1955 C  C     . ASP A 1 252 ? 63.96600 -26.84300 -21.65500 1.000 75.14585  ? 252 ASP A C     1 
ATOM   1956 O  O     . ASP A 1 252 ? 64.59400 -25.77400 -21.67000 1.000 74.76160  ? 252 ASP A O     1 
ATOM   1957 C  CB    . ASP A 1 252 ? 64.84000 -29.02400 -22.54500 1.000 79.47269  ? 252 ASP A CB    1 
ATOM   1958 C  CG    . ASP A 1 252 ? 65.82900 -30.15400 -22.32000 1.000 94.39553  ? 252 ASP A CG    1 
ATOM   1959 O  OD1   . ASP A 1 252 ? 66.23500 -30.36700 -21.15700 1.000 101.05159 ? 252 ASP A OD1   1 
ATOM   1960 O  OD2   . ASP A 1 252 ? 66.20300 -30.83000 -23.30200 1.000 98.39074  ? 252 ASP A OD2   1 
ATOM   1961 N  N     . ARG A 1 253 ? 62.65600 -26.90300 -21.89700 1.000 68.81615  ? 253 ARG A N     1 
ATOM   1962 C  CA    . ARG A 1 253 ? 61.93200 -25.68400 -22.23800 1.000 64.96305  ? 253 ARG A CA    1 
ATOM   1963 C  C     . ARG A 1 253 ? 61.88600 -24.72400 -21.05300 1.000 66.03687  ? 253 ARG A C     1 
ATOM   1964 O  O     . ARG A 1 253 ? 62.04700 -23.51000 -21.22700 1.000 72.02969  ? 253 ARG A O     1 
ATOM   1965 C  CB    . ARG A 1 253 ? 60.52600 -26.02300 -22.72700 1.000 67.50809  ? 253 ARG A CB    1 
ATOM   1966 C  CG    . ARG A 1 253 ? 59.78700 -24.83600 -23.32800 1.000 72.48764  ? 253 ARG A CG    1 
ATOM   1967 C  CD    . ARG A 1 253 ? 58.59000 -25.29900 -24.14300 1.000 78.85946  ? 253 ARG A CD    1 
ATOM   1968 N  NE    . ARG A 1 253 ? 58.93600 -26.39200 -25.04500 1.000 90.57402  ? 253 ARG A NE    1 
ATOM   1969 C  CZ    . ARG A 1 253 ? 59.37200 -26.24000 -26.28900 1.000 95.87992  ? 253 ARG A CZ    1 
ATOM   1970 N  NH1   . ARG A 1 253 ? 59.52700 -25.04100 -26.82600 1.000 80.63598  ? 253 ARG A NH1   1 
ATOM   1971 N  NH2   . ARG A 1 253 ? 59.67200 -27.31900 -27.00600 1.000 99.96462  ? 253 ARG A NH2   1 
ATOM   1972 N  N     . LEU A 1 254 ? 61.64500 -25.24300 -19.84600 1.000 65.18676  ? 254 LEU A N     1 
ATOM   1973 C  CA    . LEU A 1 254 ? 61.54400 -24.37900 -18.67100 1.000 64.30771  ? 254 LEU A CA    1 
ATOM   1974 C  C     . LEU A 1 254 ? 62.86600 -23.68500 -18.38000 1.000 65.38679  ? 254 LEU A C     1 
ATOM   1975 O  O     . LEU A 1 254 ? 62.89300 -22.49100 -18.06800 1.000 64.86830  ? 254 LEU A O     1 
ATOM   1976 C  CB    . LEU A 1 254 ? 61.10100 -25.18400 -17.45200 1.000 62.83911  ? 254 LEU A CB    1 
ATOM   1977 C  CG    . LEU A 1 254 ? 59.68800 -25.75200 -17.47700 1.000 64.91831  ? 254 LEU A CG    1 
ATOM   1978 C  CD1   . LEU A 1 254 ? 59.45800 -26.61800 -16.25300 1.000 71.80861  ? 254 LEU A CD1   1 
ATOM   1979 C  CD2   . LEU A 1 254 ? 58.67700 -24.61900 -17.53400 1.000 59.97824  ? 254 LEU A CD2   1 
ATOM   1980 N  N     . ARG A 1 255 ? 63.97200 -24.41500 -18.49100 1.000 65.30520  ? 255 ARG A N     1 
ATOM   1981 C  CA    . ARG A 1 255 ? 65.29000 -23.82100 -18.32700 1.000 68.16870  ? 255 ARG A CA    1 
ATOM   1982 C  C     . ARG A 1 255 ? 65.51100 -22.74400 -19.37700 1.000 67.25543  ? 255 ARG A C     1 
ATOM   1983 O  O     . ARG A 1 255 ? 66.00200 -21.65100 -19.07100 1.000 68.33451  ? 255 ARG A O     1 
ATOM   1984 C  CB    . ARG A 1 255 ? 66.33700 -24.92800 -18.42100 1.000 71.40856  ? 255 ARG A CB    1 
ATOM   1985 C  CG    . ARG A 1 255 ? 66.44600 -25.72600 -17.13400 1.000 76.77236  ? 255 ARG A CG    1 
ATOM   1986 C  CD    . ARG A 1 255 ? 67.67100 -26.61100 -17.09000 1.000 84.69437  ? 255 ARG A CD    1 
ATOM   1987 N  NE    . ARG A 1 255 ? 67.45800 -27.78500 -17.93100 1.000 90.30556  ? 255 ARG A NE    1 
ATOM   1988 C  CZ    . ARG A 1 255 ? 67.12400 -28.98700 -17.47800 1.000 93.62438  ? 255 ARG A CZ    1 
ATOM   1989 N  NH1   . ARG A 1 255 ? 66.97300 -29.22300 -16.18300 1.000 78.20938  ? 255 ARG A NH1   1 
ATOM   1990 N  NH2   . ARG A 1 255 ? 66.93000 -29.97800 -18.34500 1.000 101.22793 ? 255 ARG A NH2   1 
ATOM   1991 N  N     . ASP A 1 256 ? 65.17200 -23.04700 -20.63200 1.000 77.30927  ? 256 ASP A N     1 
ATOM   1992 C  CA    . ASP A 1 256 ? 65.44700 -22.11100 -21.71400 1.000 76.67761  ? 256 ASP A CA    1 
ATOM   1993 C  C     . ASP A 1 256 ? 64.65000 -20.81700 -21.57100 1.000 74.15626  ? 256 ASP A C     1 
ATOM   1994 O  O     . ASP A 1 256 ? 65.19500 -19.72000 -21.73900 1.000 77.09609  ? 256 ASP A O     1 
ATOM   1995 C  CB    . ASP A 1 256 ? 65.10400 -22.78100 -23.04400 1.000 77.67510  ? 256 ASP A CB    1 
ATOM   1996 C  CG    . ASP A 1 256 ? 65.57400 -21.98700 -24.23700 1.000 88.16320  ? 256 ASP A CG    1 
ATOM   1997 O  OD1   . ASP A 1 256 ? 66.65900 -21.37400 -24.16100 1.000 94.01127  ? 256 ASP A OD1   1 
ATOM   1998 O  OD2   . ASP A 1 256 ? 64.82700 -21.94300 -25.24100 1.000 95.78254  ? 256 ASP A OD2   1 
ATOM   1999 N  N     . SER A 1 257 ? 63.36100 -20.92000 -21.24400 1.000 69.77942  ? 257 SER A N     1 
ATOM   2000 C  CA    . SER A 1 257 ? 62.50200 -19.73800 -21.24700 1.000 67.97920  ? 257 SER A CA    1 
ATOM   2001 C  C     . SER A 1 257 ? 62.38800 -19.02600 -19.90200 1.000 67.11594  ? 257 SER A C     1 
ATOM   2002 O  O     . SER A 1 257 ? 62.27600 -17.79400 -19.87200 1.000 68.07922  ? 257 SER A O     1 
ATOM   2003 C  CB    . SER A 1 257 ? 61.10700 -20.11800 -21.74800 1.000 68.77404  ? 257 SER A CB    1 
ATOM   2004 O  OG    . SER A 1 257 ? 61.16200 -20.55200 -23.09800 1.000 65.59997  ? 257 SER A OG    1 
ATOM   2005 N  N     . TYR A 1 258 ? 62.41700 -19.75900 -18.79100 1.000 63.53393  ? 258 TYR A N     1 
ATOM   2006 C  CA    . TYR A 1 258 ? 62.12700 -19.19800 -17.48000 1.000 61.27577  ? 258 TYR A CA    1 
ATOM   2007 C  C     . TYR A 1 258 ? 63.26100 -19.43700 -16.50100 1.000 64.80514  ? 258 TYR A C     1 
ATOM   2008 O  O     . TYR A 1 258 ? 63.16700 -19.01300 -15.34400 1.000 69.18724  ? 258 TYR A O     1 
ATOM   2009 C  CB    . TYR A 1 258 ? 60.82500 -19.78700 -16.92600 1.000 62.99703  ? 258 TYR A CB    1 
ATOM   2010 C  CG    . TYR A 1 258 ? 59.64200 -19.61200 -17.85200 1.000 64.96042  ? 258 TYR A CG    1 
ATOM   2011 C  CD1   . TYR A 1 258 ? 59.02600 -18.37800 -18.01800 1.000 65.41311  ? 258 TYR A CD1   1 
ATOM   2012 C  CD2   . TYR A 1 258 ? 59.14900 -20.69100 -18.57400 1.000 64.15506  ? 258 TYR A CD2   1 
ATOM   2013 C  CE1   . TYR A 1 258 ? 57.94100 -18.22900 -18.87300 1.000 61.26787  ? 258 TYR A CE1   1 
ATOM   2014 C  CE2   . TYR A 1 258 ? 58.07300 -20.55200 -19.42700 1.000 61.99691  ? 258 TYR A CE2   1 
ATOM   2015 C  CZ    . TYR A 1 258 ? 57.47100 -19.32400 -19.57500 1.000 57.94905  ? 258 TYR A CZ    1 
ATOM   2016 O  OH    . TYR A 1 258 ? 56.39900 -19.20800 -20.43100 1.000 52.27469  ? 258 TYR A OH    1 
ATOM   2017 N  N     . PHE A 1 259 ? 64.30800 -20.13700 -16.93000 1.000 67.30807  ? 259 PHE A N     1 
ATOM   2018 C  CA    . PHE A 1 259 ? 65.56400 -20.25600 -16.19900 1.000 66.58167  ? 259 PHE A CA    1 
ATOM   2019 C  C     . PHE A 1 259 ? 65.36000 -20.91400 -14.83100 1.000 61.93374  ? 259 PHE A C     1 
ATOM   2020 O  O     . PHE A 1 259 ? 65.82700 -20.41400 -13.80500 1.000 64.70513  ? 259 PHE A O     1 
ATOM   2021 C  CB    . PHE A 1 259 ? 66.21100 -18.87400 -16.03400 1.000 71.65859  ? 259 PHE A CB    1 
ATOM   2022 C  CG    . PHE A 1 259 ? 66.40600 -18.11700 -17.32900 1.000 72.44553  ? 259 PHE A CG    1 
ATOM   2023 C  CD1   . PHE A 1 259 ? 67.49800 -18.35900 -18.14800 1.000 79.22792  ? 259 PHE A CD1   1 
ATOM   2024 C  CD2   . PHE A 1 259 ? 65.50200 -17.13100 -17.70400 1.000 70.94798  ? 259 PHE A CD2   1 
ATOM   2025 C  CE1   . PHE A 1 259 ? 67.66800 -17.64700 -19.33000 1.000 83.69161  ? 259 PHE A CE1   1 
ATOM   2026 C  CE2   . PHE A 1 259 ? 65.66700 -16.41600 -18.87900 1.000 73.69831  ? 259 PHE A CE2   1 
ATOM   2027 C  CZ    . PHE A 1 259 ? 66.75100 -16.67400 -19.69400 1.000 78.61206  ? 259 PHE A CZ    1 
ATOM   2028 N  N     . PHE A 1 260 ? 64.65000 -22.04600 -14.81400 1.000 61.69424  ? 260 PHE A N     1 
ATOM   2029 C  CA    . PHE A 1 260 ? 64.54600 -22.85000 -13.59900 1.000 63.66816  ? 260 PHE A CA    1 
ATOM   2030 C  C     . PHE A 1 260 ? 64.26600 -24.30500 -13.95700 1.000 60.76518  ? 260 PHE A C     1 
ATOM   2031 O  O     . PHE A 1 260 ? 63.74900 -24.60500 -15.03400 1.000 67.04751  ? 260 PHE A O     1 
ATOM   2032 C  CB    . PHE A 1 260 ? 63.43500 -22.34300 -12.67600 1.000 63.26285  ? 260 PHE A CB    1 
ATOM   2033 C  CG    . PHE A 1 260 ? 62.05100 -22.69600 -13.14900 1.000 62.81806  ? 260 PHE A CG    1 
ATOM   2034 C  CD1   . PHE A 1 260 ? 61.37000 -21.87300 -14.02400 1.000 63.34181  ? 260 PHE A CD1   1 
ATOM   2035 C  CD2   . PHE A 1 260 ? 61.42300 -23.84800 -12.69600 1.000 67.50020  ? 260 PHE A CD2   1 
ATOM   2036 C  CE1   . PHE A 1 260 ? 60.09400 -22.19700 -14.45300 1.000 64.62617  ? 260 PHE A CE1   1 
ATOM   2037 C  CE2   . PHE A 1 260 ? 60.15000 -24.17800 -13.12600 1.000 67.14489  ? 260 PHE A CE2   1 
ATOM   2038 C  CZ    . PHE A 1 260 ? 59.48400 -23.35000 -14.00300 1.000 60.44146  ? 260 PHE A CZ    1 
ATOM   2039 N  N     . THR A 1 261 ? 64.59600 -25.21100 -13.03500 1.000 64.34719  ? 261 THR A N     1 
ATOM   2040 C  CA    . THR A 1 261 ? 64.30600 -26.63800 -13.17500 1.000 64.58932  ? 261 THR A CA    1 
ATOM   2041 C  C     . THR A 1 261 ? 63.21200 -27.10900 -12.21200 1.000 67.32913  ? 261 THR A C     1 
ATOM   2042 O  O     . THR A 1 261 ? 63.34100 -26.93500 -10.99300 1.000 74.13257  ? 261 THR A O     1 
ATOM   2043 C  CB    . THR A 1 261 ? 65.57600 -27.46200 -12.97200 1.000 69.83469  ? 261 THR A CB    1 
ATOM   2044 O  OG1   . THR A 1 261 ? 66.54200 -27.11300 -13.97400 1.000 69.71099  ? 261 THR A OG1   1 
ATOM   2045 C  CG2   . THR A 1 261 ? 65.26900 -28.94300 -13.05700 1.000 76.38284  ? 261 THR A CG2   1 
ATOM   2046 N  N     . CYS A 1 262 ? 62.13800 -27.68800 -12.76700 1.000 63.60499  ? 262 CYS A N     1 
ATOM   2047 C  CA    . CYS A 1 262 ? 60.97700 -28.10900 -11.98900 1.000 66.64220  ? 262 CYS A CA    1 
ATOM   2048 C  C     . CYS A 1 262 ? 61.27300 -29.40200 -11.24000 1.000 72.62187  ? 262 CYS A C     1 
ATOM   2049 O  O     . CYS A 1 262 ? 61.93500 -30.31800 -11.76300 1.000 66.23163  ? 262 CYS A O     1 
ATOM   2050 C  CB    . CYS A 1 262 ? 59.74000 -28.27200 -12.86500 1.000 64.93937  ? 262 CYS A CB    1 
ATOM   2051 S  SG    . CYS A 1 262 ? 58.24200 -28.61200 -11.92400 1.000 68.75035  ? 262 CYS A SG    1 
ATOM   2052 N  N     . GLU A 1 263 ? 60.78700 -29.46200 -9.98500  1.000 72.98507  ? 263 GLU A N     1 
ATOM   2053 C  CA    . GLU A 1 263 ? 60.99100 -30.65800 -9.11600  1.000 75.63012  ? 263 GLU A CA    1 
ATOM   2054 C  C     . GLU A 1 263 ? 59.63900 -31.14500 -8.58100  1.000 73.49039  ? 263 GLU A C     1 
ATOM   2055 O  O     . GLU A 1 263 ? 59.62400 -31.66800 -7.45000  1.000 75.59591  ? 263 GLU A O     1 
ATOM   2056 C  CB    . GLU A 1 263 ? 61.93600 -30.32500 -7.96100  1.000 77.78301  ? 263 GLU A CB    1 
ATOM   2057 C  CG    . GLU A 1 263 ? 63.31100 -29.87800 -8.41900  1.000 89.17648  ? 263 GLU A CG    1 
ATOM   2058 C  CD    . GLU A 1 263 ? 64.24000 -29.47400 -7.28800  1.000 104.67044 ? 263 GLU A CD    1 
ATOM   2059 O  OE1   . GLU A 1 263 ? 63.83500 -29.60900 -6.11700  1.000 101.05685 ? 263 GLU A OE1   1 
ATOM   2060 O  OE2   . GLU A 1 263 ? 65.36400 -29.02500 -7.58000  1.000 114.80324 ? 263 GLU A OE2   1 
ATOM   2061 N  N     . CYS A 1 264 ? 58.53700 -30.95200 -9.32500  1.000 77.88039  ? 264 CYS A N     1 
ATOM   2062 C  CA    . CYS A 1 264 ? 57.21500 -31.46300 -8.99500  1.000 76.18808  ? 264 CYS A CA    1 
ATOM   2063 C  C     . CYS A 1 264 ? 57.21600 -32.99200 -9.05500  1.000 86.17612  ? 264 CYS A C     1 
ATOM   2064 O  O     . CYS A 1 264 ? 58.20600 -33.62800 -9.43300  1.000 85.96557  ? 264 CYS A O     1 
ATOM   2065 C  CB    . CYS A 1 264 ? 56.17200 -30.86900 -9.93400  1.000 74.84845  ? 264 CYS A CB    1 
ATOM   2066 S  SG    . CYS A 1 264 ? 56.10000 -31.66400 -11.53300 1.000 72.15602  ? 264 CYS A SG    1 
ATOM   2067 N  N     . GLN A 1 265 ? 56.10900 -33.59400 -8.63300  1.000 93.26645  ? 265 GLN A N     1 
ATOM   2068 C  CA    . GLN A 1 265 ? 56.03000 -35.07400 -8.58900  1.000 95.24563  ? 265 GLN A CA    1 
ATOM   2069 C  C     . GLN A 1 265 ? 56.35600 -35.66600 -9.96200  1.000 95.44039  ? 265 GLN A C     1 
ATOM   2070 O  O     . GLN A 1 265 ? 57.13600 -36.62400 -10.00200 1.000 97.56959  ? 265 GLN A O     1 
ATOM   2071 C  CB    . GLN A 1 265 ? 54.65900 -35.49500 -8.06800  1.000 100.02515 ? 265 GLN A CB    1 
ATOM   2072 C  CG    . GLN A 1 265 ? 54.42200 -35.10300 -6.61800  1.000 105.87059 ? 265 GLN A CG    1 
ATOM   2073 C  CD    . GLN A 1 265 ? 55.42900 -35.72400 -5.68100  1.000 119.28272 ? 265 GLN A CD    1 
ATOM   2074 O  OE1   . GLN A 1 265 ? 55.80900 -36.88300 -5.82900  1.000 122.31993 ? 265 GLN A OE1   1 
ATOM   2075 N  NE2   . GLN A 1 265 ? 55.87000 -34.95000 -4.70300  1.000 115.57438 ? 265 GLN A NE2   1 
ATOM   2076 N  N     . GLU A 1 266 ? 55.77400 -35.13000 -11.03600 1.000 87.74210  ? 266 GLU A N     1 
ATOM   2077 C  CA    . GLU A 1 266 ? 56.01400 -35.71800 -12.34500 1.000 83.89427  ? 266 GLU A CA    1 
ATOM   2078 C  C     . GLU A 1 266 ? 57.48300 -35.62700 -12.73600 1.000 85.06809  ? 266 GLU A C     1 
ATOM   2079 O  O     . GLU A 1 266 ? 58.02900 -36.56600 -13.32300 1.000 89.22122  ? 266 GLU A O     1 
ATOM   2080 C  CB    . GLU A 1 266 ? 55.13000 -35.05500 -13.40200 1.000 85.93662  ? 266 GLU A CB    1 
ATOM   2081 C  CG    . GLU A 1 266 ? 53.63900 -35.29900 -13.18800 1.000 98.19598  ? 266 GLU A CG    1 
ATOM   2082 C  CD    . GLU A 1 266 ? 53.24900 -36.77200 -13.16400 1.000 106.52593 ? 266 GLU A CD    1 
ATOM   2083 O  OE1   . GLU A 1 266 ? 53.78100 -37.57500 -13.96600 1.000 105.72583 ? 266 GLU A OE1   1 
ATOM   2084 O  OE2   . GLU A 1 266 ? 52.37100 -37.11800 -12.34700 1.000 108.70514 ? 266 GLU A OE2   1 
ATOM   2085 N  N     . CYS A 1 267 ? 58.15100 -34.51900 -12.40100 1.000 83.89164  ? 267 CYS A N     1 
ATOM   2086 C  CA    . CYS A 1 267 ? 59.56500 -34.40200 -12.74200 1.000 83.19419  ? 267 CYS A CA    1 
ATOM   2087 C  C     . CYS A 1 267 ? 60.44200 -35.30400 -11.88100 1.000 90.35294  ? 267 CYS A C     1 
ATOM   2088 O  O     . CYS A 1 267 ? 61.39800 -35.90800 -12.38600 1.000 94.74557  ? 267 CYS A O     1 
ATOM   2089 C  CB    . CYS A 1 267 ? 60.00500 -32.94600 -12.59100 1.000 81.61242  ? 267 CYS A CB    1 
ATOM   2090 S  SG    . CYS A 1 267 ? 59.31600 -31.84300 -13.83500 1.000 76.73288  ? 267 CYS A SG    1 
ATOM   2091 N  N     . THR A 1 268 ? 60.14100 -35.41400 -10.58500 1.000 87.51839  ? 268 THR A N     1 
ATOM   2092 C  CA    . THR A 1 268 ? 60.97100 -36.24900 -9.72200  1.000 96.01151  ? 268 THR A CA    1 
ATOM   2093 C  C     . THR A 1 268 ? 60.83600 -37.72600 -10.08500 1.000 102.28068 ? 268 THR A C     1 
ATOM   2094 O  O     . THR A 1 268 ? 61.83800 -38.42600 -10.27300 1.000 104.24145 ? 268 THR A O     1 
ATOM   2095 C  CB    . THR A 1 268 ? 60.61600 -36.00400 -8.25400  1.000 89.49231  ? 268 THR A CB    1 
ATOM   2096 O  OG1   . THR A 1 268 ? 59.19400 -36.05800 -8.08100  1.000 97.61960  ? 268 THR A OG1   1 
ATOM   2097 C  CG2   . THR A 1 268 ? 61.12700 -34.64100 -7.81200  1.000 82.72308  ? 268 THR A CG2   1 
ATOM   2098 N  N     . THR A 1 269 ? 59.59400 -38.20400 -10.23800 1.000 109.71579 ? 269 THR A N     1 
ATOM   2099 C  CA    . THR A 1 269 ? 59.36500 -39.66100 -10.46600 1.000 113.70837 ? 269 THR A CA    1 
ATOM   2100 C  C     . THR A 1 269 ? 59.44300 -40.05400 -11.94700 1.000 114.16106 ? 269 THR A C     1 
ATOM   2101 O  O     . THR A 1 269 ? 59.88300 -41.19400 -12.20300 1.000 114.34002 ? 269 THR A O     1 
ATOM   2102 C  CB    . THR A 1 269 ? 58.02100 -40.10300 -9.87600  1.000 115.55070 ? 269 THR A CB    1 
ATOM   2103 O  OG1   . THR A 1 269 ? 56.97800 -39.55000 -10.68000 1.000 118.48789 ? 269 THR A OG1   1 
ATOM   2104 C  CG2   . THR A 1 269 ? 57.84100 -39.68300 -8.43400  1.000 111.71866 ? 269 THR A CG2   1 
ATOM   2105 N  N     . LYS A 1 270 ? 59.01900 -39.18100 -12.87000 1.000 106.76543 ? 270 LYS A N     1 
ATOM   2106 C  CA    . LYS A 1 270 ? 58.97800 -39.51300 -14.32700 1.000 102.82549 ? 270 LYS A CA    1 
ATOM   2107 C  C     . LYS A 1 270 ? 58.22900 -40.83400 -14.54300 1.000 108.05243 ? 270 LYS A C     1 
ATOM   2108 O  O     . LYS A 1 270 ? 58.79300 -41.72700 -15.20500 1.000 113.64784 ? 270 LYS A O     1 
ATOM   2109 C  CB    . LYS A 1 270 ? 60.37700 -39.57900 -14.94800 1.000 100.63838 ? 270 LYS A CB    1 
ATOM   2110 C  CG    . LYS A 1 270 ? 61.35400 -38.50300 -14.50100 1.000 93.14011  ? 270 LYS A CG    1 
ATOM   2111 C  CD    . LYS A 1 270 ? 62.77900 -38.80200 -14.90300 1.000 84.17851  ? 270 LYS A CD    1 
ATOM   2112 C  CE    . LYS A 1 270 ? 63.75700 -37.74000 -14.44500 1.000 89.70286  ? 270 LYS A CE    1 
ATOM   2113 N  NZ    . LYS A 1 270 ? 65.13700 -38.00600 -14.91900 1.000 99.76196  ? 270 LYS A NZ    1 
ATOM   2114 N  N     . ASP A 1 271 ? 57.02100 -40.96300 -13.98800 1.000 122.18307 ? 271 ASP A N     1 
ATOM   2115 C  CA    . ASP A 1 271 ? 56.24200 -42.22200 -14.13600 1.000 126.17039 ? 271 ASP A CA    1 
ATOM   2116 C  C     . ASP A 1 271 ? 55.47200 -42.19100 -15.46100 1.000 122.01726 ? 271 ASP A C     1 
ATOM   2117 O  O     . ASP A 1 271 ? 55.47300 -43.22000 -16.16500 1.000 123.72010 ? 271 ASP A O     1 
ATOM   2118 C  CB    . ASP A 1 271 ? 55.34200 -42.50300 -12.92700 1.000 129.13390 ? 271 ASP A CB    1 
ATOM   2119 C  CG    . ASP A 1 271 ? 54.73600 -41.27100 -12.27800 1.000 134.73721 ? 271 ASP A CG    1 
ATOM   2120 O  OD1   . ASP A 1 271 ? 54.30500 -40.36500 -13.01400 1.000 141.51434 ? 271 ASP A OD1   1 
ATOM   2121 O  OD2   . ASP A 1 271 ? 54.68500 -41.23600 -11.03400 1.000 134.02133 ? 271 ASP A OD2   1 
ATOM   2122 N  N     . LYS A 1 272 ? 54.85000 -41.05300 -15.78500 1.000 104.87573 ? 272 LYS A N     1 
ATOM   2123 C  CA    . LYS A 1 272 ? 54.03500 -40.94400 -17.02500 1.000 102.44123 ? 272 LYS A CA    1 
ATOM   2124 C  C     . LYS A 1 272 ? 54.95500 -40.98600 -18.24500 1.000 105.27052 ? 272 LYS A C     1 
ATOM   2125 O  O     . LYS A 1 272 ? 54.46200 -41.32000 -19.33300 1.000 106.17589 ? 272 LYS A O     1 
ATOM   2126 C  CB    . LYS A 1 272 ? 53.23700 -39.63800 -17.02100 1.000 87.85264  ? 272 LYS A CB    1 
ATOM   2127 C  CG    . LYS A 1 272 ? 52.08800 -39.59000 -16.02600 1.000 83.08365  ? 272 LYS A CG    1 
ATOM   2128 C  CD    . LYS A 1 272 ? 51.22000 -38.36400 -16.18800 1.000 76.55655  ? 272 LYS A CD    1 
ATOM   2129 C  CE    . LYS A 1 272 ? 49.89500 -38.69000 -16.83700 1.000 75.24323  ? 272 LYS A CE    1 
ATOM   2130 N  NZ    . LYS A 1 272 ? 48.91600 -37.57200 -16.71100 1.000 76.95923  ? 272 LYS A NZ    1 
ATOM   2131 N  N     . ASP A 1 273 ? 56.23200 -40.64300 -18.06300 1.000 102.77022 ? 273 ASP A N     1 
ATOM   2132 C  CA    . ASP A 1 273 ? 57.20900 -40.65000 -19.18300 1.000 99.32770  ? 273 ASP A CA    1 
ATOM   2133 C  C     . ASP A 1 273 ? 57.19900 -42.01300 -19.87300 1.000 94.51396  ? 273 ASP A C     1 
ATOM   2134 O  O     . ASP A 1 273 ? 57.40800 -42.04600 -21.09400 1.000 93.09537  ? 273 ASP A O     1 
ATOM   2135 C  CB    . ASP A 1 273 ? 58.62000 -40.36100 -18.67700 1.000 102.46492 ? 273 ASP A CB    1 
ATOM   2136 C  CG    . ASP A 1 273 ? 58.89600 -38.88100 -18.51100 1.000 94.50607  ? 273 ASP A CG    1 
ATOM   2137 O  OD1   . ASP A 1 273 ? 57.93300 -38.12600 -18.26700 1.000 88.88171  ? 273 ASP A OD1   1 
ATOM   2138 O  OD2   . ASP A 1 273 ? 60.07500 -38.49700 -18.62100 1.000 89.96342  ? 273 ASP A OD2   1 
ATOM   2139 N  N     . LYS A 1 274 ? 56.97500 -43.09400 -19.12100 1.000 94.34552  ? 274 LYS A N     1 
ATOM   2140 C  CA    . LYS A 1 274 ? 57.04700 -44.41600 -19.71900 1.000 97.65645  ? 274 LYS A CA    1 
ATOM   2141 C  C     . LYS A 1 274 ? 55.88400 -44.60400 -20.68800 1.000 94.84558  ? 274 LYS A C     1 
ATOM   2142 O  O     . LYS A 1 274 ? 56.05100 -45.21000 -21.75500 1.000 92.37687  ? 274 LYS A O     1 
ATOM   2143 C  CB    . LYS A 1 274 ? 56.94500 -45.47400 -18.61200 1.000 103.29133 ? 274 LYS A CB    1 
ATOM   2144 C  CG    . LYS A 1 274 ? 58.06400 -45.50600 -17.57500 1.000 106.58120 ? 274 LYS A CG    1 
ATOM   2145 C  CD    . LYS A 1 274 ? 57.95700 -46.76200 -16.70100 1.000 112.53455 ? 274 LYS A CD    1 
ATOM   2146 C  CE    . LYS A 1 274 ? 59.08800 -46.86600 -15.68000 1.000 115.88495 ? 274 LYS A CE    1 
ATOM   2147 N  NZ    . LYS A 1 274 ? 58.99100 -48.11600 -14.86400 1.000 115.29014 ? 274 LYS A NZ    1 
ATOM   2148 N  N     . ALA A 1 275 ? 54.69300 -44.09400 -20.33800 1.000 98.32231  ? 275 ALA A N     1 
ATOM   2149 C  CA    . ALA A 1 275 ? 53.57300 -44.12000 -21.27900 1.000 94.79821  ? 275 ALA A CA    1 
ATOM   2150 C  C     . ALA A 1 275 ? 53.80200 -43.20800 -22.48400 1.000 92.23211  ? 275 ALA A C     1 
ATOM   2151 O  O     . ALA A 1 275 ? 53.40100 -43.53700 -23.60800 1.000 87.58155  ? 275 ALA A O     1 
ATOM   2152 C  CB    . ALA A 1 275 ? 52.27800 -43.73900 -20.56200 1.000 91.15830  ? 275 ALA A CB    1 
ATOM   2153 N  N     . LYS A 1 276 ? 54.47000 -42.07300 -22.25400 1.000 96.16416  ? 276 LYS A N     1 
ATOM   2154 C  CA    . LYS A 1 276 ? 54.73800 -41.06500 -23.27700 1.000 86.03137  ? 276 LYS A CA    1 
ATOM   2155 C  C     . LYS A 1 276 ? 55.74300 -41.52500 -24.32300 1.000 86.60249  ? 276 LYS A C     1 
ATOM   2156 O  O     . LYS A 1 276 ? 55.64300 -41.13200 -25.49100 1.000 90.80036  ? 276 LYS A O     1 
ATOM   2157 C  CB    . LYS A 1 276 ? 55.22800 -39.78800 -22.59400 1.000 85.50499  ? 276 LYS A CB    1 
ATOM   2158 C  CG    . LYS A 1 276 ? 54.13900 -39.04900 -21.81300 1.000 81.79928  ? 276 LYS A CG    1 
ATOM   2159 C  CD    . LYS A 1 276 ? 54.70400 -37.89900 -20.98300 1.000 77.04871  ? 276 LYS A CD    1 
ATOM   2160 C  CE    . LYS A 1 276 ? 53.59100 -37.12500 -20.28600 1.000 72.77188  ? 276 LYS A CE    1 
ATOM   2161 N  NZ    . LYS A 1 276 ? 54.09300 -35.91400 -19.58600 1.000 64.18664  ? 276 LYS A NZ    1 
ATOM   2162 N  N     . VAL A 1 277 ? 56.70000 -42.35900 -23.93600 1.000 90.94511  ? 277 VAL A N     1 
ATOM   2163 C  CA    . VAL A 1 277 ? 57.71300 -42.86200 -24.85300 1.000 93.58227  ? 277 VAL A CA    1 
ATOM   2164 C  C     . VAL A 1 277 ? 57.45700 -44.34300 -25.08700 1.000 100.07779 ? 277 VAL A C     1 
ATOM   2165 O  O     . VAL A 1 277 ? 58.31200 -45.18700 -24.79200 1.000 95.49829  ? 277 VAL A O     1 
ATOM   2166 C  CB    . VAL A 1 277 ? 59.13500 -42.61000 -24.31500 1.000 86.66302  ? 277 VAL A CB    1 
ATOM   2167 C  CG1   . VAL A 1 277 ? 60.17400 -42.81300 -25.41100 1.000 83.70214  ? 277 VAL A CG1   1 
ATOM   2168 C  CG2   . VAL A 1 277 ? 59.24500 -41.21100 -23.73700 1.000 83.58371  ? 277 VAL A CG2   1 
ATOM   2169 N  N     . GLU A 1 278 ? 56.24800 -44.67400 -25.53900 1.000 109.97898 ? 278 GLU A N     1 
ATOM   2170 C  CA    . GLU A 1 278 ? 55.88200 -46.07200 -25.67800 1.000 112.30031 ? 278 GLU A CA    1 
ATOM   2171 C  C     . GLU A 1 278 ? 56.68500 -46.72000 -26.79400 1.000 115.78230 ? 278 GLU A C     1 
ATOM   2172 O  O     . GLU A 1 278 ? 56.79400 -46.17200 -27.89900 1.000 114.84008 ? 278 GLU A O     1 
ATOM   2173 C  CB    . GLU A 1 278 ? 54.38900 -46.16700 -26.00800 1.000 111.40020 ? 278 GLU A CB    1 
ATOM   2174 C  CG    . GLU A 1 278 ? 53.77000 -47.53800 -25.89900 1.000 113.66889 ? 278 GLU A CG    1 
ATOM   2175 C  CD    . GLU A 1 278 ? 53.37800 -47.90100 -24.49100 1.000 119.07480 ? 278 GLU A CD    1 
ATOM   2176 O  OE1   . GLU A 1 278 ? 52.84200 -47.02600 -23.77600 1.000 111.90815 ? 278 GLU A OE1   1 
ATOM   2177 O  OE2   . GLU A 1 278 ? 53.61100 -49.06500 -24.09800 1.000 125.42293 ? 278 GLU A OE2   1 
ATOM   2178 N  N     . ILE A 1 279 ? 57.25100 -47.89300 -26.49600 1.000 120.47497 ? 279 ILE A N     1 
ATOM   2179 C  CA    . ILE A 1 279 ? 58.04500 -48.64700 -27.45500 1.000 120.15651 ? 279 ILE A CA    1 
ATOM   2180 C  C     . ILE A 1 279 ? 57.15900 -49.80400 -27.89000 1.000 125.33345 ? 279 ILE A C     1 
ATOM   2181 O  O     . ILE A 1 279 ? 56.45400 -50.37300 -27.04600 1.000 121.77250 ? 279 ILE A O     1 
ATOM   2182 C  CB    . ILE A 1 279 ? 59.34100 -49.15100 -26.78800 1.000 118.70107 ? 279 ILE A CB    1 
ATOM   2183 C  CG1   . ILE A 1 279 ? 60.05800 -48.00900 -26.05800 1.000 108.02611 ? 279 ILE A CG1   1 
ATOM   2184 C  CG2   . ILE A 1 279 ? 60.27500 -49.78500 -27.80000 1.000 121.49088 ? 279 ILE A CG2   1 
ATOM   2185 C  CD1   . ILE A 1 279 ? 60.33900 -46.78800 -26.86100 1.000 104.53095 ? 279 ILE A CD1   1 
ATOM   2186 N  N     . ARG A 1 280 ? 57.17900 -50.17200 -29.17400 1.000 142.72501 ? 280 ARG A N     1 
ATOM   2187 C  CA    . ARG A 1 280 ? 56.40400 -51.36400 -29.62200 1.000 144.42784 ? 280 ARG A CA    1 
ATOM   2188 C  C     . ARG A 1 280 ? 56.97200 -52.61700 -28.94400 1.000 147.71508 ? 280 ARG A C     1 
ATOM   2189 O  O     . ARG A 1 280 ? 58.21100 -52.77300 -28.96500 1.000 149.77848 ? 280 ARG A O     1 
ATOM   2190 C  CB    . ARG A 1 280 ? 56.51000 -51.51600 -31.13900 1.000 145.97013 ? 280 ARG A CB    1 
ATOM   2191 C  CG    . ARG A 1 280 ? 55.78200 -50.43700 -31.92200 1.000 143.30666 ? 280 ARG A CG    1 
ATOM   2192 C  CD    . ARG A 1 280 ? 56.02000 -50.65000 -33.39800 1.000 145.19636 ? 280 ARG A CD    1 
ATOM   2193 N  NE    . ARG A 1 280 ? 55.07000 -51.56600 -34.00700 1.000 146.42808 ? 280 ARG A NE    1 
ATOM   2194 C  CZ    . ARG A 1 280 ? 55.13300 -51.97300 -35.26800 1.000 142.76975 ? 280 ARG A CZ    1 
ATOM   2195 N  NH1   . ARG A 1 280 ? 56.10800 -51.54500 -36.05300 1.000 145.58588 ? 280 ARG A NH1   1 
ATOM   2196 N  NH2   . ARG A 1 280 ? 54.22600 -52.80900 -35.74000 1.000 138.47976 ? 280 ARG A NH2   1 
ATOM   2197 N  N     . LYS A 1 281 ? 56.11500 -53.48300 -28.38300 1.000 141.96702 ? 281 LYS A N     1 
ATOM   2198 C  CA    . LYS A 1 281 ? 56.64400 -54.71600 -27.79700 1.000 146.69390 ? 281 LYS A CA    1 
ATOM   2199 C  C     . LYS A 1 281 ? 56.68200 -55.81600 -28.86200 1.000 145.98592 ? 281 LYS A C     1 
ATOM   2200 O  O     . LYS A 1 281 ? 55.92100 -56.78500 -28.82600 1.000 150.67333 ? 281 LYS A O     1 
ATOM   2201 C  CB    . LYS A 1 281 ? 55.85000 -55.10100 -26.56100 1.000 145.81222 ? 281 LYS A CB    1 
ATOM   2202 C  CG    . LYS A 1 281 ? 55.98600 -54.02500 -25.51100 1.000 136.15580 ? 281 LYS A CG    1 
ATOM   2203 C  CD    . LYS A 1 281 ? 55.40800 -54.39800 -24.17200 1.000 135.85313 ? 281 LYS A CD    1 
ATOM   2204 C  CE    . LYS A 1 281 ? 55.21900 -53.15100 -23.31800 1.000 135.93735 ? 281 LYS A CE    1 
ATOM   2205 N  NZ    . LYS A 1 281 ? 54.59000 -53.49700 -22.01600 1.000 139.43514 ? 281 LYS A NZ    1 
ATOM   2206 N  N     . LEU A 1 282 ? 57.60900 -55.61400 -29.80100 1.000 144.51996 ? 282 LEU A N     1 
ATOM   2207 C  CA    . LEU A 1 282 ? 57.74800 -56.56900 -30.92200 1.000 146.02277 ? 282 LEU A CA    1 
ATOM   2208 C  C     . LEU A 1 282 ? 58.64700 -57.72700 -30.51100 1.000 150.13905 ? 282 LEU A C     1 
ATOM   2209 O  O     . LEU A 1 282 ? 59.37600 -57.58900 -29.50600 1.000 145.18056 ? 282 LEU A O     1 
ATOM   2210 C  CB    . LEU A 1 282 ? 58.34700 -55.83200 -32.12400 1.000 137.39542 ? 282 LEU A CB    1 
ATOM   2211 C  CG    . LEU A 1 282 ? 57.45500 -54.76300 -32.74900 1.000 136.02157 ? 282 LEU A CG    1 
ATOM   2212 C  CD1   . LEU A 1 282 ? 58.14400 -54.10800 -33.93600 1.000 120.51182 ? 282 LEU A CD1   1 
ATOM   2213 C  CD2   . LEU A 1 282 ? 56.11400 -55.34800 -33.16500 1.000 130.66830 ? 282 LEU A CD2   1 
ATOM   2214 N  N     . SER A 1 283 ? 58.59100 -58.81200 -31.27100 1.000 154.37377 ? 283 SER A N     1 
ATOM   2215 C  CA    . SER A 1 283 ? 59.39300 -60.00400 -31.03800 1.000 158.28214 ? 283 SER A CA    1 
ATOM   2216 C  C     . SER A 1 283 ? 60.85400 -59.60500 -30.88400 1.000 158.45058 ? 283 SER A C     1 
ATOM   2217 O  O     . SER A 1 283 ? 61.57000 -60.16400 -30.04400 1.000 155.33968 ? 283 SER A O     1 
ATOM   2218 C  CB    . SER A 1 283 ? 59.18400 -61.02800 -32.16200 1.000 154.35535 ? 283 SER A CB    1 
ATOM   2219 O  OG    . SER A 1 283 ? 59.45600 -60.48100 -33.43600 1.000 154.26323 ? 283 SER A OG    1 
ATOM   2220 N  N     . ASP A 1 284 ? 61.33100 -58.65300 -31.69500 1.000 158.94274 ? 284 ASP A N     1 
ATOM   2221 C  CA    . ASP A 1 284 ? 62.67200 -58.15800 -31.41200 1.000 157.40571 ? 284 ASP A CA    1 
ATOM   2222 C  C     . ASP A 1 284 ? 62.69200 -56.84800 -30.63200 1.000 150.79176 ? 284 ASP A C     1 
ATOM   2223 O  O     . ASP A 1 284 ? 62.30100 -55.80100 -31.17000 1.000 146.35965 ? 284 ASP A O     1 
ATOM   2224 C  CB    . ASP A 1 284 ? 63.36200 -57.94600 -32.76100 1.000 156.56877 ? 284 ASP A CB    1 
ATOM   2225 C  CG    . ASP A 1 284 ? 64.86300 -57.86900 -32.66300 1.000 159.29805 ? 284 ASP A CG    1 
ATOM   2226 O  OD1   . ASP A 1 284 ? 65.47300 -58.88700 -32.27200 1.000 162.95901 ? 284 ASP A OD1   1 
ATOM   2227 O  OD2   . ASP A 1 284 ? 65.44800 -56.81500 -33.02200 1.000 161.29829 ? 284 ASP A OD2   1 
ATOM   2228 N  N     . PRO A 1 285 ? 63.05200 -56.88200 -29.34600 1.000 149.42581 ? 285 PRO A N     1 
ATOM   2229 C  CA    . PRO A 1 285 ? 63.09600 -55.65500 -28.53700 1.000 138.55609 ? 285 PRO A CA    1 
ATOM   2230 C  C     . PRO A 1 285 ? 64.11200 -54.67000 -29.09100 1.000 139.89572 ? 285 PRO A C     1 
ATOM   2231 O  O     . PRO A 1 285 ? 65.27500 -55.03700 -29.32100 1.000 139.49567 ? 285 PRO A O     1 
ATOM   2232 C  CB    . PRO A 1 285 ? 63.51900 -56.16400 -27.14700 1.000 135.05303 ? 285 PRO A CB    1 
ATOM   2233 C  CG    . PRO A 1 285 ? 64.18900 -57.48900 -27.41200 1.000 142.19863 ? 285 PRO A CG    1 
ATOM   2234 C  CD    . PRO A 1 285 ? 63.47000 -58.07100 -28.58300 1.000 147.87826 ? 285 PRO A CD    1 
ATOM   2235 N  N     . PRO A 1 286 ? 63.72000 -53.42900 -29.34600 1.000 139.49304 ? 286 PRO A N     1 
ATOM   2236 C  CA    . PRO A 1 286 ? 64.69600 -52.41200 -29.76500 1.000 135.37939 ? 286 PRO A CA    1 
ATOM   2237 C  C     . PRO A 1 286 ? 65.79100 -52.22300 -28.71700 1.000 130.89201 ? 286 PRO A C     1 
ATOM   2238 O  O     . PRO A 1 286 ? 65.51800 -52.27600 -27.51500 1.000 128.67332 ? 286 PRO A O     1 
ATOM   2239 C  CB    . PRO A 1 286 ? 63.84100 -51.15700 -29.94700 1.000 131.65789 ? 286 PRO A CB    1 
ATOM   2240 C  CG    . PRO A 1 286 ? 62.47500 -51.67900 -30.25000 1.000 131.03413 ? 286 PRO A CG    1 
ATOM   2241 C  CD    . PRO A 1 286 ? 62.33600 -52.93100 -29.42700 1.000 136.61375 ? 286 PRO A CD    1 
ATOM   2242 N  N     . LYS A 1 287 ? 67.03500 -52.01200 -29.15500 1.000 127.08892 ? 287 LYS A N     1 
ATOM   2243 C  CA    . LYS A 1 287 ? 68.05200 -51.85200 -28.12400 1.000 126.69151 ? 287 LYS A CA    1 
ATOM   2244 C  C     . LYS A 1 287 ? 67.94300 -50.42900 -27.58300 1.000 129.74714 ? 287 LYS A C     1 
ATOM   2245 O  O     . LYS A 1 287 ? 67.43000 -49.53100 -28.25400 1.000 130.00769 ? 287 LYS A O     1 
ATOM   2246 C  CB    . LYS A 1 287 ? 69.47200 -52.11100 -28.64300 1.000 125.20975 ? 287 LYS A CB    1 
ATOM   2247 C  CG    . LYS A 1 287 ? 69.73100 -53.49000 -29.22100 1.000 129.60764 ? 287 LYS A CG    1 
ATOM   2248 C  CD    . LYS A 1 287 ? 71.16200 -53.58100 -29.73400 1.000 134.38980 ? 287 LYS A CD    1 
ATOM   2249 C  CE    . LYS A 1 287 ? 71.45300 -54.93300 -30.35700 1.000 140.97743 ? 287 LYS A CE    1 
ATOM   2250 N  NZ    . LYS A 1 287 ? 71.49400 -56.01900 -29.33400 1.000 144.69103 ? 287 LYS A NZ    1 
ATOM   2251 N  N     . ALA A 1 288 ? 68.42100 -50.23100 -26.34800 1.000 128.95230 ? 288 ALA A N     1 
ATOM   2252 C  CA    . ALA A 1 288 ? 68.32600 -48.91400 -25.71500 1.000 129.55501 ? 288 ALA A CA    1 
ATOM   2253 C  C     . ALA A 1 288 ? 68.92100 -47.79800 -26.56500 1.000 131.95793 ? 288 ALA A C     1 
ATOM   2254 O  O     . ALA A 1 288 ? 68.33300 -46.71300 -26.67500 1.000 134.54245 ? 288 ALA A O     1 
ATOM   2255 C  CB    . ALA A 1 288 ? 69.00900 -48.95000 -24.34700 1.000 129.13127 ? 288 ALA A CB    1 
ATOM   2256 N  N     . GLU A 1 289 ? 70.05600 -48.07800 -27.20700 1.000 140.00889 ? 289 GLU A N     1 
ATOM   2257 C  CA    . GLU A 1 289 ? 70.70900 -47.04500 -28.05400 1.000 144.14886 ? 289 GLU A CA    1 
ATOM   2258 C  C     . GLU A 1 289 ? 69.84300 -46.75900 -29.28900 1.000 141.65119 ? 289 GLU A C     1 
ATOM   2259 O  O     . GLU A 1 289 ? 69.84900 -45.59900 -29.72900 1.000 143.06189 ? 289 GLU A O     1 
ATOM   2260 C  CB    . GLU A 1 289 ? 72.15300 -47.41900 -28.39400 1.000 142.80923 ? 289 GLU A CB    1 
ATOM   2261 C  CG    . GLU A 1 289 ? 73.18100 -46.68600 -27.54400 1.000 142.96977 ? 289 GLU A CG    1 
ATOM   2262 C  CD    . GLU A 1 289 ? 72.92200 -45.20900 -27.28500 1.000 141.86175 ? 289 GLU A CD    1 
ATOM   2263 O  OE1   . GLU A 1 289 ? 72.98500 -44.42000 -28.25000 1.000 137.39805 ? 289 GLU A OE1   1 
ATOM   2264 O  OE2   . GLU A 1 289 ? 72.66000 -44.85100 -26.11900 1.000 146.32281 ? 289 GLU A OE2   1 
ATOM   2265 N  N     . ALA A 1 290 ? 69.11400 -47.75800 -29.80700 1.000 135.90314 ? 290 ALA A N     1 
ATOM   2266 C  CA    . ALA A 1 290 ? 68.23200 -47.50700 -30.94500 1.000 128.65753 ? 290 ALA A CA    1 
ATOM   2267 C  C     . ALA A 1 290 ? 67.05300 -46.64400 -30.50500 1.000 129.41025 ? 290 ALA A C     1 
ATOM   2268 O  O     . ALA A 1 290 ? 66.60400 -45.76200 -31.25500 1.000 119.44064 ? 290 ALA A O     1 
ATOM   2269 C  CB    . ALA A 1 290 ? 67.75300 -48.82900 -31.54400 1.000 119.62750 ? 290 ALA A CB    1 
ATOM   2270 N  N     . ILE A 1 291 ? 66.59000 -46.84000 -29.26400 1.000 131.88423 ? 291 ILE A N     1 
ATOM   2271 C  CA    . ILE A 1 291 ? 65.50300 -46.02600 -28.72600 1.000 124.53072 ? 291 ILE A CA    1 
ATOM   2272 C  C     . ILE A 1 291 ? 65.96300 -44.58400 -28.62000 1.000 123.20951 ? 291 ILE A C     1 
ATOM   2273 O  O     . ILE A 1 291 ? 65.26600 -43.65500 -29.04500 1.000 122.45152 ? 291 ILE A O     1 
ATOM   2274 C  CB    . ILE A 1 291 ? 65.05900 -46.54100 -27.34300 1.000 121.06188 ? 291 ILE A CB    1 
ATOM   2275 C  CG1   . ILE A 1 291 ? 64.65100 -48.00600 -27.38000 1.000 124.32017 ? 291 ILE A CG1   1 
ATOM   2276 C  CG2   . ILE A 1 291 ? 63.89900 -45.70400 -26.81300 1.000 111.35019 ? 291 ILE A CG2   1 
ATOM   2277 C  CD1   . ILE A 1 291 ? 63.56500 -48.25000 -28.35200 1.000 124.71759 ? 291 ILE A CD1   1 
ATOM   2278 N  N     . ARG A 1 292 ? 67.13500 -44.37500 -28.01500 1.000 129.92084 ? 292 ARG A N     1 
ATOM   2279 C  CA    . ARG A 1 292 ? 67.64100 -43.01800 -27.86200 1.000 130.46301 ? 292 ARG A CA    1 
ATOM   2280 C  C     . ARG A 1 292 ? 67.92900 -42.36500 -29.21200 1.000 131.39997 ? 292 ARG A C     1 
ATOM   2281 O  O     . ARG A 1 292 ? 67.71100 -41.15700 -29.37500 1.000 131.22100 ? 292 ARG A O     1 
ATOM   2282 C  CB    . ARG A 1 292 ? 68.90100 -43.05400 -26.99300 1.000 133.64234 ? 292 ARG A CB    1 
ATOM   2283 C  CG    . ARG A 1 292 ? 69.79700 -41.84500 -27.12100 1.000 138.75085 ? 292 ARG A CG    1 
ATOM   2284 C  CD    . ARG A 1 292 ? 69.43200 -40.78400 -26.10200 1.000 148.62835 ? 292 ARG A CD    1 
ATOM   2285 N  NE    . ARG A 1 292 ? 69.81900 -39.45100 -26.54600 1.000 152.04191 ? 292 ARG A NE    1 
ATOM   2286 C  CZ    . ARG A 1 292 ? 68.98200 -38.56200 -27.06500 1.000 148.13092 ? 292 ARG A CZ    1 
ATOM   2287 N  NH1   . ARG A 1 292 ? 67.69400 -38.82900 -27.21500 1.000 141.20377 ? 292 ARG A NH1   1 
ATOM   2288 N  NH2   . ARG A 1 292 ? 69.44900 -37.37600 -27.44500 1.000 146.88077 ? 292 ARG A NH2   1 
ATOM   2289 N  N     . ASP A 1 293 ? 68.32300 -43.15800 -30.21400 1.000 131.19731 ? 293 ASP A N     1 
ATOM   2290 C  CA    . ASP A 1 293 ? 68.53600 -42.62700 -31.55900 1.000 130.61303 ? 293 ASP A CA    1 
ATOM   2291 C  C     . ASP A 1 293 ? 67.23000 -42.10400 -32.13900 1.000 119.49064 ? 293 ASP A C     1 
ATOM   2292 O  O     . ASP A 1 293 ? 67.16200 -40.97800 -32.65200 1.000 116.76926 ? 293 ASP A O     1 
ATOM   2293 C  CB    . ASP A 1 293 ? 69.12200 -43.72400 -32.45600 1.000 129.48131 ? 293 ASP A CB    1 
ATOM   2294 C  CG    . ASP A 1 293 ? 70.63900 -43.82000 -32.36700 1.000 126.03090 ? 293 ASP A CG    1 
ATOM   2295 O  OD1   . ASP A 1 293 ? 71.27100 -42.90800 -31.79600 1.000 133.62128 ? 293 ASP A OD1   1 
ATOM   2296 O  OD2   . ASP A 1 293 ? 71.19600 -44.83800 -32.83000 1.000 128.93651 ? 293 ASP A OD2   1 
ATOM   2297 N  N     . MET A 1 294 ? 66.16100 -42.89400 -32.00800 1.000 115.79809 ? 294 MET A N     1 
ATOM   2298 C  CA    . MET A 1 294 ? 64.88300 -42.46700 -32.56600 1.000 110.00266 ? 294 MET A CA    1 
ATOM   2299 C  C     . MET A 1 294 ? 64.29400 -41.29400 -31.78800 1.000 105.95481 ? 294 MET A C     1 
ATOM   2300 O  O     . MET A 1 294 ? 63.63500 -40.43600 -32.38000 1.000 102.08329 ? 294 MET A O     1 
ATOM   2301 C  CB    . MET A 1 294 ? 63.90600 -43.64200 -32.61500 1.000 106.56278 ? 294 MET A CB    1 
ATOM   2302 C  CG    . MET A 1 294 ? 62.69600 -43.37800 -33.49700 1.000 104.51779 ? 294 MET A CG    1 
ATOM   2303 S  SD    . MET A 1 294 ? 63.09300 -43.16400 -35.24600 1.000 107.98400 ? 294 MET A SD    1 
ATOM   2304 C  CE    . MET A 1 294 ? 63.52300 -44.83600 -35.72100 1.000 109.87107 ? 294 MET A CE    1 
ATOM   2305 N  N     . VAL A 1 295 ? 64.51100 -41.24800 -30.47200 1.000 110.30270 ? 295 VAL A N     1 
ATOM   2306 C  CA    . VAL A 1 295 ? 64.08100 -40.10600 -29.66000 1.000 108.44458 ? 295 VAL A CA    1 
ATOM   2307 C  C     . VAL A 1 295 ? 64.77700 -38.81800 -30.10100 1.000 113.62941 ? 295 VAL A C     1 
ATOM   2308 O  O     . VAL A 1 295 ? 64.14200 -37.76000 -30.24500 1.000 108.22613 ? 295 VAL A O     1 
ATOM   2309 C  CB    . VAL A 1 295 ? 64.32900 -40.39800 -28.17000 1.000 101.04369 ? 295 VAL A CB    1 
ATOM   2310 C  CG1   . VAL A 1 295 ? 64.13500 -39.14200 -27.34900 1.000 94.94823  ? 295 VAL A CG1   1 
ATOM   2311 C  CG2   . VAL A 1 295 ? 63.39600 -41.49800 -27.69900 1.000 88.65273  ? 295 VAL A CG2   1 
ATOM   2312 N  N     . ARG A 1 296 ? 66.08600 -38.90200 -30.29700 1.000 118.81161 ? 296 ARG A N     1 
ATOM   2313 C  CA    . ARG A 1 296 ? 66.80200 -37.70200 -30.78000 1.000 117.85097 ? 296 ARG A CA    1 
ATOM   2314 C  C     . ARG A 1 296 ? 66.19400 -37.29200 -32.12500 1.000 114.82429 ? 296 ARG A C     1 
ATOM   2315 O  O     . ARG A 1 296 ? 65.83200 -36.11100 -32.25900 1.000 112.52928 ? 296 ARG A O     1 
ATOM   2316 C  CB    . ARG A 1 296 ? 68.29300 -38.00600 -30.85200 1.000 123.07265 ? 296 ARG A CB    1 
ATOM   2317 C  CG    . ARG A 1 296 ? 69.05300 -36.92700 -31.59300 1.000 124.67811 ? 296 ARG A CG    1 
ATOM   2318 C  CD    . ARG A 1 296 ? 70.49600 -37.23200 -31.77300 1.000 130.02612 ? 296 ARG A CD    1 
ATOM   2319 N  NE    . ARG A 1 296 ? 70.68700 -38.56200 -32.34100 1.000 133.01595 ? 296 ARG A NE    1 
ATOM   2320 C  CZ    . ARG A 1 296 ? 70.22800 -38.95600 -33.52500 1.000 130.66303 ? 296 ARG A CZ    1 
ATOM   2321 N  NH1   . ARG A 1 296 ? 69.53500 -38.12100 -34.28000 1.000 127.26263 ? 296 ARG A NH1   1 
ATOM   2322 N  NH2   . ARG A 1 296 ? 70.45300 -40.18900 -33.94400 1.000 126.39937 ? 296 ARG A NH2   1 
ATOM   2323 N  N     . TYR A 1 297 ? 66.05300 -38.23600 -33.06100 1.000 115.09275 ? 297 TYR A N     1 
ATOM   2324 C  CA    . TYR A 1 297 ? 65.45500 -37.96200 -34.36000 1.000 109.63157 ? 297 TYR A CA    1 
ATOM   2325 C  C     . TYR A 1 297 ? 64.11300 -37.26200 -34.21100 1.000 102.55440 ? 297 TYR A C     1 
ATOM   2326 O  O     . TYR A 1 297 ? 63.81200 -36.30900 -34.94200 1.000 99.01450  ? 297 TYR A O     1 
ATOM   2327 C  CB    . TYR A 1 297 ? 65.32700 -39.28400 -35.12100 1.000 109.52629 ? 297 TYR A CB    1 
ATOM   2328 C  CG    . TYR A 1 297 ? 64.47800 -39.24300 -36.36500 1.000 107.72344 ? 297 TYR A CG    1 
ATOM   2329 C  CD1   . TYR A 1 297 ? 65.00300 -38.82000 -37.57900 1.000 112.48717 ? 297 TYR A CD1   1 
ATOM   2330 C  CD2   . TYR A 1 297 ? 63.15800 -39.66600 -36.33300 1.000 106.34696 ? 297 TYR A CD2   1 
ATOM   2331 C  CE1   . TYR A 1 297 ? 64.22600 -38.79300 -38.72000 1.000 108.74462 ? 297 TYR A CE1   1 
ATOM   2332 C  CE2   . TYR A 1 297 ? 62.37600 -39.64200 -37.46600 1.000 105.94428 ? 297 TYR A CE2   1 
ATOM   2333 C  CZ    . TYR A 1 297 ? 62.91200 -39.20600 -38.65700 1.000 104.46779 ? 297 TYR A CZ    1 
ATOM   2334 O  OH    . TYR A 1 297 ? 62.12500 -39.18500 -39.78300 1.000 109.38943 ? 297 TYR A OH    1 
ATOM   2335 N  N     . ALA A 1 298 ? 63.26700 -37.77100 -33.31900 1.000 104.71255 ? 298 ALA A N     1 
ATOM   2336 C  CA    . ALA A 1 298 ? 61.95600 -37.17800 -33.10800 1.000 94.27709  ? 298 ALA A CA    1 
ATOM   2337 C  C     . ALA A 1 298 ? 62.06900 -35.71700 -32.70700 1.000 93.19012  ? 298 ALA A C     1 
ATOM   2338 O  O     . ALA A 1 298 ? 61.42600 -34.83500 -33.30100 1.000 90.79246  ? 298 ALA A O     1 
ATOM   2339 C  CB    . ALA A 1 298 ? 61.24700 -37.94200 -31.99500 1.000 94.89559  ? 298 ALA A CB    1 
ATOM   2340 N  N     . ARG A 1 299 ? 62.91200 -35.44700 -31.70600 1.000 93.98495  ? 299 ARG A N     1 
ATOM   2341 C  CA    . ARG A 1 299 ? 63.08500 -34.08000 -31.23000 1.000 89.42914  ? 299 ARG A CA    1 
ATOM   2342 C  C     . ARG A 1 299 ? 63.64100 -33.17100 -32.31600 1.000 93.15064  ? 299 ARG A C     1 
ATOM   2343 O  O     . ARG A 1 299 ? 63.32400 -31.97700 -32.34800 1.000 89.21333  ? 299 ARG A O     1 
ATOM   2344 C  CB    . ARG A 1 299 ? 63.99500 -34.08700 -30.00600 1.000 93.55332  ? 299 ARG A CB    1 
ATOM   2345 C  CG    . ARG A 1 299 ? 63.30300 -34.64300 -28.77500 1.000 92.17684  ? 299 ARG A CG    1 
ATOM   2346 C  CD    . ARG A 1 299 ? 64.13200 -34.42900 -27.53500 1.000 93.46910  ? 299 ARG A CD    1 
ATOM   2347 N  NE    . ARG A 1 299 ? 64.21400 -33.00900 -27.22000 1.000 99.87250  ? 299 ARG A NE    1 
ATOM   2348 C  CZ    . ARG A 1 299 ? 64.91100 -32.50200 -26.21400 1.000 98.86185  ? 299 ARG A CZ    1 
ATOM   2349 N  NH1   . ARG A 1 299 ? 65.61000 -33.27500 -25.39900 1.000 103.79139 ? 299 ARG A NH1   1 
ATOM   2350 N  NH2   . ARG A 1 299 ? 64.90600 -31.18600 -26.02000 1.000 98.09334  ? 299 ARG A NH2   1 
ATOM   2351 N  N     . ASN A 1 300 ? 64.46200 -33.71900 -33.21100 1.000 107.20496 ? 300 ASN A N     1 
ATOM   2352 C  CA    . ASN A 1 300 ? 65.03200 -32.92800 -34.29900 1.000 107.58132 ? 300 ASN A CA    1 
ATOM   2353 C  C     . ASN A 1 300 ? 63.98000 -32.58000 -35.34600 1.000 106.62331 ? 300 ASN A C     1 
ATOM   2354 O  O     . ASN A 1 300 ? 63.86400 -31.42300 -35.77200 1.000 105.47054 ? 300 ASN A O     1 
ATOM   2355 C  CB    . ASN A 1 300 ? 66.21400 -33.66500 -34.91900 1.000 110.70275 ? 300 ASN A CB    1 
ATOM   2356 C  CG    . ASN A 1 300 ? 67.34400 -33.85700 -33.93100 1.000 118.90636 ? 300 ASN A CG    1 
ATOM   2357 O  OD1   . ASN A 1 300 ? 68.04600 -34.86800 -33.95900 1.000 128.84966 ? 300 ASN A OD1   1 
ATOM   2358 N  ND2   . ASN A 1 300 ? 67.50900 -32.89400 -33.03000 1.000 116.03760 ? 300 ASN A ND2   1 
ATOM   2359 N  N     . VAL A 1 301 ? 63.21900 -33.58300 -35.78700 1.000 94.81400  ? 301 VAL A N     1 
ATOM   2360 C  CA    . VAL A 1 301 ? 62.19500 -33.38000 -36.80700 1.000 89.22649  ? 301 VAL A CA    1 
ATOM   2361 C  C     . VAL A 1 301 ? 61.09800 -32.43900 -36.33200 1.000 89.32650  ? 301 VAL A C     1 
ATOM   2362 O  O     . VAL A 1 301 ? 60.53800 -31.68200 -37.13100 1.000 96.56684  ? 301 VAL A O     1 
ATOM   2363 C  CB    . VAL A 1 301 ? 61.61100 -34.74500 -37.22100 1.000 88.41060  ? 301 VAL A CB    1 
ATOM   2364 C  CG1   . VAL A 1 301 ? 60.41000 -34.57500 -38.14300 1.000 88.04740  ? 301 VAL A CG1   1 
ATOM   2365 C  CG2   . VAL A 1 301 ? 62.67900 -35.61100 -37.87400 1.000 101.54902 ? 301 VAL A CG2   1 
ATOM   2366 N  N     . ILE A 1 302 ? 60.78600 -32.44300 -35.03400 1.000 85.78397  ? 302 ILE A N     1 
ATOM   2367 C  CA    . ILE A 1 302 ? 59.82500 -31.47400 -34.49200 1.000 86.52880  ? 302 ILE A CA    1 
ATOM   2368 C  C     . ILE A 1 302 ? 60.27600 -30.02900 -34.72800 1.000 91.63730  ? 302 ILE A C     1 
ATOM   2369 O  O     . ILE A 1 302 ? 59.52100 -29.19800 -35.26600 1.000 92.90588  ? 302 ILE A O     1 
ATOM   2370 C  CB    . ILE A 1 302 ? 59.63600 -31.72800 -32.98800 1.000 85.61290  ? 302 ILE A CB    1 
ATOM   2371 C  CG1   . ILE A 1 302 ? 58.81900 -32.99000 -32.73800 1.000 81.08077  ? 302 ILE A CG1   1 
ATOM   2372 C  CG2   . ILE A 1 302 ? 59.01800 -30.51300 -32.31600 1.000 91.88733  ? 302 ILE A CG2   1 
ATOM   2373 C  CD1   . ILE A 1 302 ? 58.78800 -33.38900 -31.28000 1.000 82.41514  ? 302 ILE A CD1   1 
ATOM   2374 N  N     . GLU A 1 303 ? 61.55500 -29.74400 -34.44600 1.000 97.53538  ? 303 GLU A N     1 
ATOM   2375 C  CA    . GLU A 1 303 ? 62.09000 -28.39800 -34.64800 1.000 104.27566 ? 303 GLU A CA    1 
ATOM   2376 C  C     . GLU A 1 303 ? 62.17100 -28.06100 -36.12500 1.000 103.68085 ? 303 GLU A C     1 
ATOM   2377 O  O     . GLU A 1 303 ? 61.81800 -26.94400 -36.54500 1.000 104.18618 ? 303 GLU A O     1 
ATOM   2378 C  CB    . GLU A 1 303 ? 63.50800 -28.30200 -34.06500 1.000 105.76531 ? 303 GLU A CB    1 
ATOM   2379 C  CG    . GLU A 1 303 ? 64.06100 -26.85000 -33.98500 1.000 113.02934 ? 303 GLU A CG    1 
ATOM   2380 C  CD    . GLU A 1 303 ? 63.13100 -26.01200 -33.08100 1.000 112.07133 ? 303 GLU A CD    1 
ATOM   2381 O  OE1   . GLU A 1 303 ? 62.71000 -26.49100 -32.01300 1.000 110.47377 ? 303 GLU A OE1   1 
ATOM   2382 O  OE2   . GLU A 1 303 ? 62.71400 -24.92300 -33.53000 1.000 112.98460 ? 303 GLU A OE2   1 
ATOM   2383 N  N     . GLU A 1 304 ? 62.60500 -29.04100 -36.92000 1.000 107.70239 ? 304 GLU A N     1 
ATOM   2384 C  CA    . GLU A 1 304 ? 62.66600 -28.88700 -38.37000 1.000 108.91306 ? 304 GLU A CA    1 
ATOM   2385 C  C     . GLU A 1 304 ? 61.30200 -28.53500 -38.94700 1.000 107.50236 ? 304 GLU A C     1 
ATOM   2386 O  O     . GLU A 1 304 ? 61.20300 -27.69700 -39.84700 1.000 109.57893 ? 304 GLU A O     1 
ATOM   2387 C  CB    . GLU A 1 304 ? 63.22500 -30.15600 -39.02200 1.000 112.02659 ? 304 GLU A CB    1 
ATOM   2388 C  CG    . GLU A 1 304 ? 63.72600 -29.96500 -40.45600 1.000 113.90313 ? 304 GLU A CG    1 
ATOM   2389 C  CD    . GLU A 1 304 ? 62.65400 -30.24000 -41.49500 1.000 120.29337 ? 304 GLU A CD    1 
ATOM   2390 O  OE1   . GLU A 1 304 ? 61.58000 -30.75500 -41.11600 1.000 121.33034 ? 304 GLU A OE1   1 
ATOM   2391 O  OE2   . GLU A 1 304 ? 62.88900 -29.95000 -42.69000 1.000 115.55859 ? 304 GLU A OE2   1 
ATOM   2392 N  N     . PHE A 1 305 ? 60.24200 -29.17200 -38.45100 1.000 94.95349  ? 305 PHE A N     1 
ATOM   2393 C  CA    . PHE A 1 305 ? 58.90700 -28.88800 -38.96100 1.000 90.32136  ? 305 PHE A CA    1 
ATOM   2394 C  C     . PHE A 1 305 ? 58.48500 -27.47400 -38.58700 1.000 94.69030  ? 305 PHE A C     1 
ATOM   2395 O  O     . PHE A 1 305 ? 57.89700 -26.75500 -39.41400 1.000 99.42771  ? 305 PHE A O     1 
ATOM   2396 C  CB    . PHE A 1 305 ? 57.92000 -29.91200 -38.39600 1.000 83.91006  ? 305 PHE A CB    1 
ATOM   2397 C  CG    . PHE A 1 305 ? 56.55600 -29.86700 -39.02600 1.000 77.93303  ? 305 PHE A CG    1 
ATOM   2398 C  CD1   . PHE A 1 305 ? 55.59000 -28.98900 -38.55800 1.000 74.66158  ? 305 PHE A CD1   1 
ATOM   2399 C  CD2   . PHE A 1 305 ? 56.23000 -30.72200 -40.06300 1.000 83.62582  ? 305 PHE A CD2   1 
ATOM   2400 C  CE1   . PHE A 1 305 ? 54.33500 -28.95000 -39.12600 1.000 73.11929  ? 305 PHE A CE1   1 
ATOM   2401 C  CE2   . PHE A 1 305 ? 54.97600 -30.68900 -40.63500 1.000 83.73636  ? 305 PHE A CE2   1 
ATOM   2402 C  CZ    . PHE A 1 305 ? 54.02700 -29.80200 -40.16600 1.000 85.48130  ? 305 PHE A CZ    1 
ATOM   2403 N  N     . ARG A 1 306 ? 58.77300 -27.07300 -37.34700 1.000 90.45295  ? 306 ARG A N     1 
ATOM   2404 C  CA    . ARG A 1 306 ? 58.44300 -25.69400 -36.89500 1.000 83.03101  ? 306 ARG A CA    1 
ATOM   2405 C  C     . ARG A 1 306 ? 59.04500 -24.69800 -37.89000 1.000 91.32411  ? 306 ARG A C     1 
ATOM   2406 O  O     . ARG A 1 306 ? 58.37200 -23.70400 -38.21800 1.000 92.68480  ? 306 ARG A O     1 
ATOM   2407 C  CB    . ARG A 1 306 ? 59.02700 -25.47100 -35.50000 1.000 89.68444  ? 306 ARG A CB    1 
ATOM   2408 C  CG    . ARG A 1 306 ? 58.87200 -24.05400 -34.97200 1.000 105.55213 ? 306 ARG A CG    1 
ATOM   2409 C  CD    . ARG A 1 306 ? 58.57300 -24.11900 -33.49200 1.000 106.70490 ? 306 ARG A CD    1 
ATOM   2410 N  NE    . ARG A 1 306 ? 59.42200 -25.09400 -32.81900 1.000 121.15400 ? 306 ARG A NE    1 
ATOM   2411 C  CZ    . ARG A 1 306 ? 58.98000 -26.04600 -32.00200 1.000 118.72476 ? 306 ARG A CZ    1 
ATOM   2412 N  NH1   . ARG A 1 306 ? 57.68700 -26.15800 -31.75500 1.000 114.54531 ? 306 ARG A NH1   1 
ATOM   2413 N  NH2   . ARG A 1 306 ? 59.83200 -26.88500 -31.44100 1.000 120.77764 ? 306 ARG A NH2   1 
ATOM   2414 N  N     . ARG A 1 307 ? 60.26800 -24.96300 -38.35200 1.000 101.90696 ? 307 ARG A N     1 
ATOM   2415 C  CA    . ARG A 1 307 ? 60.91400 -24.08900 -39.33200 1.000 102.62020 ? 307 ARG A CA    1 
ATOM   2416 C  C     . ARG A 1 307 ? 60.31700 -24.23400 -40.72900 1.000 99.68037  ? 307 ARG A C     1 
ATOM   2417 O  O     . ARG A 1 307 ? 60.04300 -23.23200 -41.40200 1.000 101.00422 ? 307 ARG A O     1 
ATOM   2418 C  CB    . ARG A 1 307 ? 62.41700 -24.38600 -39.34000 1.000 108.31299 ? 307 ARG A CB    1 
ATOM   2419 C  CG    . ARG A 1 307 ? 63.25100 -23.44200 -38.50100 1.000 105.61266 ? 307 ARG A CG    1 
ATOM   2420 C  CD    . ARG A 1 307 ? 64.74600 -23.60100 -38.78000 1.000 101.51480 ? 307 ARG A CD    1 
ATOM   2421 N  NE    . ARG A 1 307 ? 65.20600 -24.95200 -38.45300 1.000 103.40450 ? 307 ARG A NE    1 
ATOM   2422 C  CZ    . ARG A 1 307 ? 65.36200 -25.96600 -39.29500 1.000 108.84200 ? 307 ARG A CZ    1 
ATOM   2423 N  NH1   . ARG A 1 307 ? 65.09800 -25.84600 -40.58700 1.000 106.89440 ? 307 ARG A NH1   1 
ATOM   2424 N  NH2   . ARG A 1 307 ? 65.79500 -27.13300 -38.82600 1.000 107.25496 ? 307 ARG A NH2   1 
ATOM   2425 N  N     . ALA A 1 308 ? 60.10600 -25.47100 -41.18200 1.000 100.41467 ? 308 ALA A N     1 
ATOM   2426 C  CA    . ALA A 1 308 ? 59.66200 -25.71100 -42.55100 1.000 97.00900  ? 308 ALA A CA    1 
ATOM   2427 C  C     . ALA A 1 308 ? 58.30000 -25.09600 -42.84400 1.000 91.33990  ? 308 ALA A C     1 
ATOM   2428 O  O     . ALA A 1 308 ? 58.06100 -24.62700 -43.96300 1.000 93.45594  ? 308 ALA A O     1 
ATOM   2429 C  CB    . ALA A 1 308 ? 59.62100 -27.21400 -42.81700 1.000 96.86161  ? 308 ALA A CB    1 
ATOM   2430 N  N     . LYS A 1 309 ? 57.41300 -25.04400 -41.85000 1.000 88.50798  ? 309 LYS A N     1 
ATOM   2431 C  CA    . LYS A 1 309 ? 56.05800 -24.57100 -42.13100 1.000 93.39014  ? 309 LYS A CA    1 
ATOM   2432 C  C     . LYS A 1 309 ? 55.97600 -23.08300 -42.45700 1.000 99.93567  ? 309 LYS A C     1 
ATOM   2433 O  O     . LYS A 1 309 ? 54.88700 -22.60900 -42.80600 1.000 100.98316 ? 309 LYS A O     1 
ATOM   2434 C  CB    . LYS A 1 309 ? 55.14400 -24.85200 -40.94000 1.000 87.60524  ? 309 LYS A CB    1 
ATOM   2435 C  CG    . LYS A 1 309 ? 55.52900 -24.04200 -39.72600 1.000 87.29205  ? 309 LYS A CG    1 
ATOM   2436 C  CD    . LYS A 1 309 ? 54.65000 -24.32800 -38.52400 1.000 94.97455  ? 309 LYS A CD    1 
ATOM   2437 C  CE    . LYS A 1 309 ? 53.18600 -24.47400 -38.89700 1.000 86.15507  ? 309 LYS A CE    1 
ATOM   2438 N  NZ    . LYS A 1 309 ? 52.39000 -24.86900 -37.69700 1.000 79.90169  ? 309 LYS A NZ    1 
ATOM   2439 N  N     . HIS A 1 310 ? 57.08500 -22.34400 -42.40900 1.000 103.60979 ? 310 HIS A N     1 
ATOM   2440 C  CA    . HIS A 1 310 ? 57.04200 -20.93800 -42.78400 1.000 102.80706 ? 310 HIS A CA    1 
ATOM   2441 C  C     . HIS A 1 310 ? 57.16300 -20.71800 -44.28700 1.000 103.94141 ? 310 HIS A C     1 
ATOM   2442 O  O     . HIS A 1 310 ? 56.67100 -19.70600 -44.79800 1.000 108.62618 ? 310 HIS A O     1 
ATOM   2443 C  CB    . HIS A 1 310 ? 58.15100 -20.18300 -42.05200 1.000 105.20472 ? 310 HIS A CB    1 
ATOM   2444 C  CG    . HIS A 1 310 ? 57.89200 -20.02700 -40.58800 1.000 105.41790 ? 310 HIS A CG    1 
ATOM   2445 N  ND1   . HIS A 1 310 ? 58.67000 -20.64300 -39.63100 1.000 107.67607 ? 310 HIS A ND1   1 
ATOM   2446 C  CD2   . HIS A 1 310 ? 56.87900 -19.42500 -39.91900 1.000 107.08652 ? 310 HIS A CD2   1 
ATOM   2447 C  CE1   . HIS A 1 310 ? 58.18900 -20.36800 -38.43200 1.000 111.08964 ? 310 HIS A CE1   1 
ATOM   2448 N  NE2   . HIS A 1 310 ? 57.09900 -19.63600 -38.57900 1.000 112.32663 ? 310 HIS A NE2   1 
ATOM   2449 N  N     . TYR A 1 311 ? 57.81800 -21.63100 -45.00800 1.000 95.90624  ? 311 TYR A N     1 
ATOM   2450 C  CA    . TYR A 1 311 ? 58.10500 -21.42700 -46.42300 1.000 96.60369  ? 311 TYR A CA    1 
ATOM   2451 C  C     . TYR A 1 311 ? 57.74800 -22.62800 -47.29100 1.000 92.39266  ? 311 TYR A C     1 
ATOM   2452 O  O     . TYR A 1 311 ? 58.11800 -22.65100 -48.47200 1.000 95.31406  ? 311 TYR A O     1 
ATOM   2453 C  CB    . TYR A 1 311 ? 59.58400 -21.07800 -46.62200 1.000 95.75095  ? 311 TYR A CB    1 
ATOM   2454 C  CG    . TYR A 1 311 ? 60.54300 -22.13000 -46.10600 1.000 95.26405  ? 311 TYR A CG    1 
ATOM   2455 C  CD1   . TYR A 1 311 ? 60.98100 -23.16200 -46.92900 1.000 96.10626  ? 311 TYR A CD1   1 
ATOM   2456 C  CD2   . TYR A 1 311 ? 61.01200 -22.08900 -44.79800 1.000 95.83517  ? 311 TYR A CD2   1 
ATOM   2457 C  CE1   . TYR A 1 311 ? 61.85700 -24.12700 -46.46400 1.000 96.46683  ? 311 TYR A CE1   1 
ATOM   2458 C  CE2   . TYR A 1 311 ? 61.88900 -23.05000 -44.32200 1.000 100.67523 ? 311 TYR A CE2   1 
ATOM   2459 C  CZ    . TYR A 1 311 ? 62.30900 -24.06700 -45.16000 1.000 103.97036 ? 311 TYR A CZ    1 
ATOM   2460 O  OH    . TYR A 1 311 ? 63.18200 -25.02700 -44.69700 1.000 102.10435 ? 311 TYR A OH    1 
ATOM   2461 N  N     . LYS A 1 312 ? 57.06400 -23.63000 -46.75000 1.000 87.17624  ? 312 LYS A N     1 
ATOM   2462 C  CA    . LYS A 1 312 ? 56.79200 -24.84200 -47.50100 1.000 85.11284  ? 312 LYS A CA    1 
ATOM   2463 C  C     . LYS A 1 312 ? 55.29000 -25.01300 -47.68300 1.000 88.57904  ? 312 LYS A C     1 
ATOM   2464 O  O     . LYS A 1 312 ? 54.48500 -24.46600 -46.92400 1.000 84.92860  ? 312 LYS A O     1 
ATOM   2465 C  CB    . LYS A 1 312 ? 57.37600 -26.05400 -46.77300 1.000 92.93220  ? 312 LYS A CB    1 
ATOM   2466 C  CG    . LYS A 1 312 ? 58.88100 -26.18600 -46.92400 1.000 101.37268 ? 312 LYS A CG    1 
ATOM   2467 C  CD    . LYS A 1 312 ? 59.38400 -27.47900 -46.31200 1.000 98.89344  ? 312 LYS A CD    1 
ATOM   2468 C  CE    . LYS A 1 312 ? 60.90300 -27.54700 -46.32100 1.000 105.49686 ? 312 LYS A CE    1 
ATOM   2469 N  NZ    . LYS A 1 312 ? 61.46700 -27.71400 -47.68300 1.000 107.32339 ? 312 LYS A NZ    1 
ATOM   2470 N  N     . SER A 1 313 ? 54.91400 -25.77700 -48.70500 1.000 91.00302  ? 313 SER A N     1 
ATOM   2471 C  CA    . SER A 1 313 ? 53.50400 -25.95500 -49.01300 1.000 89.00541  ? 313 SER A CA    1 
ATOM   2472 C  C     . SER A 1 313 ? 52.84600 -26.93300 -48.04300 1.000 91.16356  ? 313 SER A C     1 
ATOM   2473 O  O     . SER A 1 313 ? 53.52400 -27.75100 -47.41500 1.000 93.34014  ? 313 SER A O     1 
ATOM   2474 C  CB    . SER A 1 313 ? 53.33100 -26.46200 -50.43900 1.000 92.03735  ? 313 SER A CB    1 
ATOM   2475 O  OG    . SER A 1 313 ? 53.63300 -27.84000 -50.51700 1.000 101.15160 ? 313 SER A OG    1 
ATOM   2476 N  N     . PRO A 1 314 ? 51.51900 -26.86000 -47.89800 1.000 86.73935  ? 314 PRO A N     1 
ATOM   2477 C  CA    . PRO A 1 314 ? 50.83000 -27.80300 -46.99600 1.000 84.72595  ? 314 PRO A CA    1 
ATOM   2478 C  C     . PRO A 1 314 ? 51.07800 -29.26900 -47.32800 1.000 92.28738  ? 314 PRO A C     1 
ATOM   2479 O  O     . PRO A 1 314 ? 51.33100 -30.07500 -46.42200 1.000 97.31167  ? 314 PRO A O     1 
ATOM   2480 C  CB    . PRO A 1 314 ? 49.35700 -27.40700 -47.15500 1.000 86.93148  ? 314 PRO A CB    1 
ATOM   2481 C  CG    . PRO A 1 314 ? 49.39800 -25.97000 -47.53100 1.000 80.77547  ? 314 PRO A CG    1 
ATOM   2482 C  CD    . PRO A 1 314 ? 50.60800 -25.82200 -48.41000 1.000 88.34743  ? 314 PRO A CD    1 
ATOM   2483 N  N     . SER A 1 315 ? 51.00100 -29.64000 -48.61100 1.000 87.01306  ? 315 SER A N     1 
ATOM   2484 C  CA    . SER A 1 315 ? 51.20600 -31.03300 -49.00700 1.000 93.19012  ? 315 SER A CA    1 
ATOM   2485 C  C     . SER A 1 315 ? 52.61200 -31.51400 -48.67100 1.000 99.78302  ? 315 SER A C     1 
ATOM   2486 O  O     . SER A 1 315 ? 52.79900 -32.67900 -48.29200 1.000 106.30222 ? 315 SER A O     1 
ATOM   2487 C  CB    . SER A 1 315 ? 50.92300 -31.20600 -50.49900 1.000 89.73971  ? 315 SER A CB    1 
ATOM   2488 O  OG    . SER A 1 315 ? 51.85300 -30.47800 -51.27400 1.000 102.60967 ? 315 SER A OG    1 
ATOM   2489 N  N     . GLU A 1 316 ? 53.60100 -30.61600 -48.79500 1.000 101.71746 ? 316 GLU A N     1 
ATOM   2490 C  CA    . GLU A 1 316 ? 55.00900 -30.95700 -48.44000 1.000 102.52019 ? 316 GLU A CA    1 
ATOM   2491 C  C     . GLU A 1 316 ? 55.06500 -31.24900 -46.93800 1.000 100.45678 ? 316 GLU A C     1 
ATOM   2492 O  O     . GLU A 1 316 ? 55.79600 -32.17500 -46.55300 1.000 101.38321 ? 316 GLU A O     1 
ATOM   2493 C  CB    . GLU A 1 316 ? 55.94800 -29.79300 -48.77900 1.000 102.68336 ? 316 GLU A CB    1 
ATOM   2494 C  CG    . GLU A 1 316 ? 56.44100 -29.77700 -50.22000 1.000 119.23272 ? 316 GLU A CG    1 
ATOM   2495 C  CD    . GLU A 1 316 ? 57.05400 -28.46700 -50.70400 1.000 117.54830 ? 316 GLU A CD    1 
ATOM   2496 O  OE1   . GLU A 1 316 ? 57.95800 -27.95200 -50.01900 1.000 113.05829 ? 316 GLU A OE1   1 
ATOM   2497 O  OE2   . GLU A 1 316 ? 56.61500 -27.96400 -51.75700 1.000 107.17864 ? 316 GLU A OE2   1 
ATOM   2498 N  N     . LEU A 1 317 ? 54.32400 -30.48700 -46.12900 1.000 91.05039  ? 317 LEU A N     1 
ATOM   2499 C  CA    . LEU A 1 317 ? 54.28400 -30.67400 -44.68500 1.000 88.53956  ? 317 LEU A CA    1 
ATOM   2500 C  C     . LEU A 1 317 ? 53.61400 -31.99900 -44.33200 1.000 93.00326  ? 317 LEU A C     1 
ATOM   2501 O  O     . LEU A 1 317 ? 54.05300 -32.70900 -43.41300 1.000 96.66159  ? 317 LEU A O     1 
ATOM   2502 C  CB    . LEU A 1 317 ? 53.55500 -29.49000 -44.05900 1.000 87.38416  ? 317 LEU A CB    1 
ATOM   2503 C  CG    . LEU A 1 317 ? 54.31800 -28.16200 -44.18900 1.000 85.96557  ? 317 LEU A CG    1 
ATOM   2504 C  CD1   . LEU A 1 317 ? 53.48100 -26.99600 -43.68300 1.000 87.56050  ? 317 LEU A CD1   1 
ATOM   2505 C  CD2   . LEU A 1 317 ? 55.67300 -28.19600 -43.49500 1.000 88.57904  ? 317 LEU A CD2   1 
ATOM   2506 N  N     . LEU A 1 318 ? 52.54100 -32.34500 -45.05100 1.000 92.08736  ? 318 LEU A N     1 
ATOM   2507 C  CA    . LEU A 1 318 ? 51.90100 -33.63800 -44.83700 1.000 85.67869  ? 318 LEU A CA    1 
ATOM   2508 C  C     . LEU A 1 318 ? 52.85800 -34.76800 -45.15900 1.000 92.67690  ? 318 LEU A C     1 
ATOM   2509 O  O     . LEU A 1 318 ? 52.86700 -35.80200 -44.48000 1.000 99.83565  ? 318 LEU A O     1 
ATOM   2510 C  CB    . LEU A 1 318 ? 50.65100 -33.74700 -45.70400 1.000 83.22314  ? 318 LEU A CB    1 
ATOM   2511 C  CG    . LEU A 1 318 ? 49.37900 -33.05600 -45.23700 1.000 78.20411  ? 318 LEU A CG    1 
ATOM   2512 C  CD1   . LEU A 1 318 ? 48.30700 -33.16800 -46.28200 1.000 84.36275  ? 318 LEU A CD1   1 
ATOM   2513 C  CD2   . LEU A 1 318 ? 48.93100 -33.80100 -44.01900 1.000 77.91987  ? 318 LEU A CD2   1 
ATOM   2514 N  N     . GLU A 1 319 ? 53.64300 -34.60400 -46.22500 1.000 87.43943  ? 319 GLU A N     1 
ATOM   2515 C  CA    . GLU A 1 319 ? 54.63500 -35.61400 -46.56000 1.000 92.03998  ? 319 GLU A CA    1 
ATOM   2516 C  C     . GLU A 1 319 ? 55.61100 -35.79900 -45.41100 1.000 93.46647  ? 319 GLU A C     1 
ATOM   2517 O  O     . GLU A 1 319 ? 55.95100 -36.93000 -45.04600 1.000 99.76986  ? 319 GLU A O     1 
ATOM   2518 C  CB    . GLU A 1 319 ? 55.36300 -35.24700 -47.84900 1.000 92.81639  ? 319 GLU A CB    1 
ATOM   2519 C  CG    . GLU A 1 319 ? 54.55300 -35.58000 -49.08400 1.000 110.25006 ? 319 GLU A CG    1 
ATOM   2520 C  CD    . GLU A 1 319 ? 55.31800 -35.34000 -50.36600 1.000 127.76532 ? 319 GLU A CD    1 
ATOM   2521 O  OE1   . GLU A 1 319 ? 56.54300 -35.11600 -50.29200 1.000 131.48945 ? 319 GLU A OE1   1 
ATOM   2522 O  OE2   . GLU A 1 319 ? 54.69600 -35.38400 -51.45000 1.000 126.19145 ? 319 GLU A OE2   1 
ATOM   2523 N  N     . ILE A 1 320 ? 56.04200 -34.68900 -44.80300 1.000 88.07372  ? 320 ILE A N     1 
ATOM   2524 C  CA    . ILE A 1 320 ? 56.96800 -34.78100 -43.67700 1.000 89.40546  ? 320 ILE A CA    1 
ATOM   2525 C  C     . ILE A 1 320 ? 56.33500 -35.55200 -42.53100 1.000 95.47987  ? 320 ILE A C     1 
ATOM   2526 O  O     . ILE A 1 320 ? 56.94800 -36.46700 -41.96300 1.000 95.40091  ? 320 ILE A O     1 
ATOM   2527 C  CB    . ILE A 1 320 ? 57.37500 -33.37300 -43.19300 1.000 87.99213  ? 320 ILE A CB    1 
ATOM   2528 C  CG1   . ILE A 1 320 ? 58.16700 -32.61100 -44.24800 1.000 91.32937  ? 320 ILE A CG1   1 
ATOM   2529 C  CG2   . ILE A 1 320 ? 58.15300 -33.45300 -41.88500 1.000 80.15435  ? 320 ILE A CG2   1 
ATOM   2530 C  CD1   . ILE A 1 320 ? 58.29300 -31.13500 -43.94000 1.000 88.45271  ? 320 ILE A CD1   1 
ATOM   2531 N  N     . CYS A 1 321 ? 55.07300 -35.24300 -42.22300 1.000 102.27016 ? 321 CYS A N     1 
ATOM   2532 C  CA    . CYS A 1 321 ? 54.38900 -35.93800 -41.13600 1.000 101.41216 ? 321 CYS A CA    1 
ATOM   2533 C  C     . CYS A 1 321 ? 54.24900 -37.43100 -41.40500 1.000 103.73086 ? 321 CYS A C     1 
ATOM   2534 O  O     . CYS A 1 321 ? 54.54100 -38.25700 -40.53400 1.000 106.11535 ? 321 CYS A O     1 
ATOM   2535 C  CB    . CYS A 1 321 ? 53.01500 -35.31200 -40.91800 1.000 99.19347  ? 321 CYS A CB    1 
ATOM   2536 S  SG    . CYS A 1 321 ? 53.09900 -33.64300 -40.27000 1.000 103.04130 ? 321 CYS A SG    1 
ATOM   2537 N  N     . GLU A 1 322 ? 53.81100 -37.77200 -42.62900 1.000 106.89966 ? 322 GLU A N     1 
ATOM   2538 C  CA    . GLU A 1 322 ? 53.58100 -39.19100 -43.03100 1.000 107.59711 ? 322 GLU A CA    1 
ATOM   2539 C  C     . GLU A 1 322 ? 54.90000 -39.97800 -43.00400 1.000 109.97634 ? 322 GLU A C     1 
ATOM   2540 O  O     . GLU A 1 322 ? 54.89000 -41.10100 -42.46500 1.000 111.11859 ? 322 GLU A O     1 
ATOM   2541 C  CB    . GLU A 1 322 ? 52.94600 -39.24300 -44.43300 1.000 109.04465 ? 322 GLU A CB    1 
ATOM   2542 C  CG    . GLU A 1 322 ? 51.46800 -38.84100 -44.50000 1.000 110.95541 ? 322 GLU A CG    1 
ATOM   2543 C  CD    . GLU A 1 322 ? 50.86000 -38.51900 -45.86800 1.000 125.76771 ? 322 GLU A CD    1 
ATOM   2544 O  OE1   . GLU A 1 322 ? 51.49900 -38.84500 -46.88800 1.000 126.21250 ? 322 GLU A OE1   1 
ATOM   2545 O  OE2   . GLU A 1 322 ? 49.76100 -37.93200 -45.90100 1.000 123.74642 ? 322 GLU A OE2   1 
ATOM   2546 N  N     . LEU A 1 323 ? 55.98600 -39.42400 -43.55700 1.000 104.84678 ? 323 LEU A N     1 
ATOM   2547 C  CA    . LEU A 1 323 ? 57.26500 -40.11600 -43.63800 1.000 108.12612 ? 323 LEU A CA    1 
ATOM   2548 C  C     . LEU A 1 323 ? 57.87300 -40.28700 -42.25500 1.000 109.33153 ? 323 LEU A C     1 
ATOM   2549 O  O     . LEU A 1 323 ? 58.36000 -41.37700 -41.90100 1.000 115.37699 ? 323 LEU A O     1 
ATOM   2550 C  CB    . LEU A 1 323 ? 58.19500 -39.29900 -44.54000 1.000 102.06487 ? 323 LEU A CB    1 
ATOM   2551 C  CG    . LEU A 1 323 ? 58.11400 -39.51500 -46.05800 1.000 104.82046 ? 323 LEU A CG    1 
ATOM   2552 C  CD1   . LEU A 1 323 ? 58.89000 -38.42200 -46.80300 1.000 105.71531 ? 323 LEU A CD1   1 
ATOM   2553 C  CD2   . LEU A 1 323 ? 58.55900 -40.90800 -46.48800 1.000 108.62355 ? 323 LEU A CD2   1 
ATOM   2554 N  N     . SER A 1 324 ? 57.81100 -39.22800 -41.44300 1.000 102.99393 ? 324 SER A N     1 
ATOM   2555 C  CA    . SER A 1 324 ? 58.33900 -39.30100 -40.09200 1.000 99.97514  ? 324 SER A CA    1 
ATOM   2556 C  C     . SER A 1 324 ? 57.55400 -40.29700 -39.25600 1.000 108.33404 ? 324 SER A C     1 
ATOM   2557 O  O     . SER A 1 324 ? 58.14400 -41.05900 -38.48900 1.000 115.47964 ? 324 SER A O     1 
ATOM   2558 C  CB    . SER A 1 324 ? 58.31800 -37.91800 -39.44600 1.000 95.00876  ? 324 SER A CB    1 
ATOM   2559 O  OG    . SER A 1 324 ? 56.98500 -37.50600 -39.20600 1.000 103.71770 ? 324 SER A OG    1 
ATOM   2560 N  N     . GLN A 1 325 ? 56.22900 -40.35400 -39.44000 1.000 104.63886 ? 325 GLN A N     1 
ATOM   2561 C  CA    . GLN A 1 325 ? 55.42600 -41.33700 -38.72100 1.000 105.34158 ? 325 GLN A CA    1 
ATOM   2562 C  C     . GLN A 1 325 ? 55.82500 -42.75800 -39.08400 1.000 113.38202 ? 325 GLN A C     1 
ATOM   2563 O  O     . GLN A 1 325 ? 55.90300 -43.62000 -38.21000 1.000 118.72739 ? 325 GLN A O     1 
ATOM   2564 C  CB    . GLN A 1 325 ? 53.94400 -41.11100 -39.01800 1.000 103.73875 ? 325 GLN A CB    1 
ATOM   2565 C  CG    . GLN A 1 325 ? 53.31000 -39.99200 -38.21300 1.000 99.47772  ? 325 GLN A CG    1 
ATOM   2566 C  CD    . GLN A 1 325 ? 51.87700 -39.74000 -38.62100 1.000 94.27709  ? 325 GLN A CD    1 
ATOM   2567 O  OE1   . GLN A 1 325 ? 50.99000 -40.54600 -38.34100 1.000 100.05147 ? 325 GLN A OE1   1 
ATOM   2568 N  NE2   . GLN A 1 325 ? 51.64200 -38.62000 -39.29800 1.000 86.41036  ? 325 GLN A NE2   1 
ATOM   2569 N  N     . GLU A 1 326 ? 56.04400 -43.03400 -40.36900 1.000 114.51110 ? 326 GLU A N     1 
ATOM   2570 C  CA    . GLU A 1 326 ? 56.47400 -44.37300 -40.77700 1.000 116.30868 ? 326 GLU A CA    1 
ATOM   2571 C  C     . GLU A 1 326 ? 57.79700 -44.76700 -40.10800 1.000 118.32208 ? 326 GLU A C     1 
ATOM   2572 O  O     . GLU A 1 326 ? 57.89800 -45.81100 -39.42300 1.000 125.24396 ? 326 GLU A O     1 
ATOM   2573 C  CB    . GLU A 1 326 ? 56.53600 -44.44200 -42.30000 1.000 117.39829 ? 326 GLU A CB    1 
ATOM   2574 C  CG    . GLU A 1 326 ? 55.16800 -44.85000 -42.84500 1.000 119.66698 ? 326 GLU A CG    1 
ATOM   2575 C  CD    . GLU A 1 326 ? 55.19800 -45.36700 -44.25700 1.000 135.02408 ? 326 GLU A CD    1 
ATOM   2576 O  OE1   . GLU A 1 326 ? 55.98800 -44.82700 -45.05800 1.000 135.30570 ? 326 GLU A OE1   1 
ATOM   2577 O  OE2   . GLU A 1 326 ? 54.41600 -46.29400 -44.57100 1.000 138.03760 ? 326 GLU A OE2   1 
ATOM   2578 N  N     . LYS A 1 327 ? 58.81200 -43.90900 -40.27600 1.000 115.57965 ? 327 LYS A N     1 
ATOM   2579 C  CA    . LYS A 1 327 ? 60.15800 -44.17500 -39.69200 1.000 116.62188 ? 327 LYS A CA    1 
ATOM   2580 C  C     . LYS A 1 327 ? 60.04200 -44.35100 -38.17500 1.000 121.01188 ? 327 LYS A C     1 
ATOM   2581 O  O     . LYS A 1 327 ? 60.57200 -45.34900 -37.65600 1.000 126.60729 ? 327 LYS A O     1 
ATOM   2582 C  CB    . LYS A 1 327 ? 61.10800 -43.02000 -40.02500 1.000 108.70777 ? 327 LYS A CB    1 
ATOM   2583 C  CG    . LYS A 1 327 ? 62.52800 -43.15700 -39.49100 1.000 110.13163 ? 327 LYS A CG    1 
ATOM   2584 C  CD    . LYS A 1 327 ? 63.57200 -42.50000 -40.37300 1.000 114.33213 ? 327 LYS A CD    1 
ATOM   2585 C  CE    . LYS A 1 327 ? 64.99000 -42.70200 -39.87800 1.000 113.53203 ? 327 LYS A CE    1 
ATOM   2586 N  NZ    . LYS A 1 327 ? 65.21500 -44.10700 -39.43400 1.000 110.95278 ? 327 LYS A NZ    1 
ATOM   2587 N  N     . MET A 1 328 ? 59.36900 -43.41900 -37.49500 1.000 117.69043 ? 328 MET A N     1 
ATOM   2588 C  CA    . MET A 1 328 ? 59.27600 -43.48400 -36.01300 1.000 113.41623 ? 328 MET A CA    1 
ATOM   2589 C  C     . MET A 1 328 ? 58.47100 -44.71800 -35.60200 1.000 116.79032 ? 328 MET A C     1 
ATOM   2590 O  O     . MET A 1 328 ? 58.85200 -45.33800 -34.60100 1.000 120.35654 ? 328 MET A O     1 
ATOM   2591 C  CB    . MET A 1 328 ? 58.60900 -42.23300 -35.43500 1.000 111.42915 ? 328 MET A CB    1 
ATOM   2592 C  CG    . MET A 1 328 ? 59.56900 -41.09000 -35.19300 1.000 108.42089 ? 328 MET A CG    1 
ATOM   2593 S  SD    . MET A 1 328 ? 58.68000 -39.53800 -34.93800 1.000 105.38369 ? 328 MET A SD    1 
ATOM   2594 C  CE    . MET A 1 328 ? 59.95300 -38.34500 -35.34500 1.000 97.27745  ? 328 MET A CE    1 
ATOM   2595 N  N     . SER A 1 329 ? 57.42100 -45.06700 -36.35600 1.000 117.54041 ? 329 SER A N     1 
ATOM   2596 C  CA    . SER A 1 329 ? 56.54800 -46.21400 -35.98700 1.000 114.64006 ? 329 SER A CA    1 
ATOM   2597 C  C     . SER A 1 329 ? 57.36200 -47.50300 -35.86100 1.000 125.68875 ? 329 SER A C     1 
ATOM   2598 O  O     . SER A 1 329 ? 57.01900 -48.30200 -34.99800 1.000 131.51577 ? 329 SER A O     1 
ATOM   2599 C  CB    . SER A 1 329 ? 55.39900 -46.40500 -36.94300 1.000 110.02109 ? 329 SER A CB    1 
ATOM   2600 O  OG    . SER A 1 329 ? 55.77100 -47.24800 -38.02300 1.000 119.81437 ? 329 SER A OG    1 
ATOM   2601 N  N     . SER A 1 330 ? 58.37500 -47.69500 -36.71100 1.000 128.45751 ? 330 SER A N     1 
ATOM   2602 C  CA    . SER A 1 330 ? 59.22900 -48.90800 -36.63100 1.000 128.49699 ? 330 SER A CA    1 
ATOM   2603 C  C     . SER A 1 330 ? 59.63300 -49.16200 -35.17400 1.000 125.96510 ? 330 SER A C     1 
ATOM   2604 O  O     . SER A 1 330 ? 59.83700 -50.34100 -34.82100 1.000 127.42580 ? 330 SER A O     1 
ATOM   2605 C  CB    . SER A 1 330 ? 60.43100 -48.78900 -37.53000 1.000 127.97061 ? 330 SER A CB    1 
ATOM   2606 O  OG    . SER A 1 330 ? 61.42500 -47.96700 -36.93800 1.000 129.18917 ? 330 SER A OG    1 
ATOM   2607 N  N     . VAL A 1 331 ? 59.73000 -48.10300 -34.36000 1.000 126.81784 ? 331 VAL A N     1 
ATOM   2608 C  CA    . VAL A 1 331 ? 60.12600 -48.24800 -32.96500 1.000 125.24923 ? 331 VAL A CA    1 
ATOM   2609 C  C     . VAL A 1 331 ? 59.01700 -47.84100 -32.00100 1.000 124.25964 ? 331 VAL A C     1 
ATOM   2610 O  O     . VAL A 1 331 ? 58.80000 -48.50200 -30.97700 1.000 124.17278 ? 331 VAL A O     1 
ATOM   2611 C  CB    . VAL A 1 331 ? 61.40400 -47.42200 -32.68600 1.000 124.25437 ? 331 VAL A CB    1 
ATOM   2612 C  CG1   . VAL A 1 331 ? 61.84400 -47.57500 -31.25400 1.000 124.23332 ? 331 VAL A CG1   1 
ATOM   2613 C  CG2   . VAL A 1 331 ? 62.52600 -47.83500 -33.63100 1.000 127.67320 ? 331 VAL A CG2   1 
ATOM   2614 N  N     . PHE A 1 332 ? 58.30500 -46.76100 -32.30800 1.000 120.44602 ? 332 PHE A N     1 
ATOM   2615 C  CA    . PHE A 1 332 ? 57.32900 -46.15400 -31.41200 1.000 112.27925 ? 332 PHE A CA    1 
ATOM   2616 C  C     . PHE A 1 332 ? 55.91200 -46.66100 -31.65900 1.000 118.79582 ? 332 PHE A C     1 
ATOM   2617 O  O     . PHE A 1 332 ? 55.50500 -46.86200 -32.80700 1.000 115.04537 ? 332 PHE A O     1 
ATOM   2618 C  CB    . PHE A 1 332 ? 57.34500 -44.63500 -31.58400 1.000 108.82357 ? 332 PHE A CB    1 
ATOM   2619 C  CG    . PHE A 1 332 ? 58.61600 -43.98300 -31.12500 1.000 104.05195 ? 332 PHE A CG    1 
ATOM   2620 C  CD1   . PHE A 1 332 ? 59.50700 -44.64900 -30.30000 1.000 108.77094 ? 332 PHE A CD1   1 
ATOM   2621 C  CD2   . PHE A 1 332 ? 58.93900 -42.71100 -31.56100 1.000 98.63551  ? 332 PHE A CD2   1 
ATOM   2622 C  CE1   . PHE A 1 332 ? 60.68500 -44.04500 -29.90000 1.000 99.84355  ? 332 PHE A CE1   1 
ATOM   2623 C  CE2   . PHE A 1 332 ? 60.11400 -42.10500 -31.16600 1.000 97.33272  ? 332 PHE A CE2   1 
ATOM   2624 C  CZ    . PHE A 1 332 ? 60.98800 -42.77200 -30.33400 1.000 92.24527  ? 332 PHE A CZ    1 
ATOM   2625 N  N     . GLU A 1 333 ? 55.16700 -46.87400 -30.57400 1.000 115.15854 ? 333 GLU A N     1 
ATOM   2626 C  CA    . GLU A 1 333 ? 53.73600 -47.09100 -30.71800 1.000 109.68420 ? 333 GLU A CA    1 
ATOM   2627 C  C     . GLU A 1 333 ? 53.03900 -45.79100 -31.09900 1.000 103.87824 ? 333 GLU A C     1 
ATOM   2628 O  O     . GLU A 1 333 ? 53.58000 -44.69000 -30.96300 1.000 108.42353 ? 333 GLU A O     1 
ATOM   2629 C  CB    . GLU A 1 333 ? 53.10100 -47.66100 -29.44500 1.000 106.57857 ? 333 GLU A CB    1 
ATOM   2630 C  CG    . GLU A 1 333 ? 53.33800 -49.14200 -29.18600 1.000 125.20712 ? 333 GLU A CG    1 
ATOM   2631 C  CD    . GLU A 1 333 ? 52.50600 -50.02500 -30.12400 1.000 136.08211 ? 333 GLU A CD    1 
ATOM   2632 O  OE1   . GLU A 1 333 ? 51.69400 -49.46800 -30.89900 1.000 134.54245 ? 333 GLU A OE1   1 
ATOM   2633 O  OE2   . GLU A 1 333 ? 52.64900 -51.26800 -30.08100 1.000 130.52618 ? 333 GLU A OE2   1 
ATOM   2634 N  N     . ASP A 1 334 ? 51.80800 -45.94300 -31.58100 1.000 102.87286 ? 334 ASP A N     1 
ATOM   2635 C  CA    . ASP A 1 334 ? 51.00700 -44.80500 -32.01000 1.000 97.48537  ? 334 ASP A CA    1 
ATOM   2636 C  C     . ASP A 1 334 ? 50.64100 -43.88100 -30.85100 1.000 92.00577  ? 334 ASP A C     1 
ATOM   2637 O  O     . ASP A 1 334 ? 50.40700 -42.68700 -31.07100 1.000 91.10566  ? 334 ASP A O     1 
ATOM   2638 C  CB    . ASP A 1 334 ? 49.77800 -45.31300 -32.75400 1.000 95.37196  ? 334 ASP A CB    1 
ATOM   2639 C  CG    . ASP A 1 334 ? 50.10800 -45.73200 -34.17600 1.000 105.43369 ? 334 ASP A CG    1 
ATOM   2640 O  OD1   . ASP A 1 334 ? 51.31000 -45.73500 -34.53000 1.000 111.42652 ? 334 ASP A OD1   1 
ATOM   2641 O  OD2   . ASP A 1 334 ? 49.17600 -46.03100 -34.94800 1.000 106.07061 ? 334 ASP A OD2   1 
ATOM   2642 N  N     . SER A 1 335 ? 50.56900 -44.40500 -29.62300 1.000 93.32961  ? 335 SER A N     1 
ATOM   2643 C  CA    . SER A 1 335 ? 50.26300 -43.59000 -28.45000 1.000 82.20986  ? 335 SER A CA    1 
ATOM   2644 C  C     . SER A 1 335 ? 51.47600 -42.81000 -27.94900 1.000 88.08425  ? 335 SER A C     1 
ATOM   2645 O  O     . SER A 1 335 ? 51.35300 -42.05400 -26.97900 1.000 85.56552  ? 335 SER A O     1 
ATOM   2646 C  CB    . SER A 1 335 ? 49.70600 -44.46300 -27.31800 1.000 83.35999  ? 335 SER A CB    1 
ATOM   2647 O  OG    . SER A 1 335 ? 50.69800 -45.33300 -26.80100 1.000 99.55404  ? 335 SER A OG    1 
ATOM   2648 N  N     . ASN A 1 336 ? 52.64300 -43.01900 -28.55800 1.000 89.96342  ? 336 ASN A N     1 
ATOM   2649 C  CA    . ASN A 1 336 ? 53.84800 -42.26100 -28.23900 1.000 86.93148  ? 336 ASN A CA    1 
ATOM   2650 C  C     . ASN A 1 336 ? 53.64300 -40.78500 -28.56700 1.000 86.18665  ? 336 ASN A C     1 
ATOM   2651 O  O     . ASN A 1 336 ? 53.13200 -40.44600 -29.63600 1.000 88.49482  ? 336 ASN A O     1 
ATOM   2652 C  CB    . ASN A 1 336 ? 55.03100 -42.81700 -29.03200 1.000 91.27673  ? 336 ASN A CB    1 
ATOM   2653 C  CG    . ASN A 1 336 ? 56.34800 -42.18800 -28.64000 1.000 94.35079  ? 336 ASN A CG    1 
ATOM   2654 O  OD1   . ASN A 1 336 ? 56.54600 -40.98400 -28.79500 1.000 90.22924  ? 336 ASN A OD1   1 
ATOM   2655 N  ND2   . ASN A 1 336 ? 57.26800 -43.00800 -28.14500 1.000 101.39637 ? 336 ASN A ND2   1 
ATOM   2656 N  N     . VAL A 1 337 ? 54.04900 -39.90200 -27.64800 1.000 79.44637  ? 337 VAL A N     1 
ATOM   2657 C  CA    . VAL A 1 337 ? 53.73700 -38.48300 -27.79500 1.000 79.60428  ? 337 VAL A CA    1 
ATOM   2658 C  C     . VAL A 1 337 ? 54.40100 -37.84200 -29.00700 1.000 82.45989  ? 337 VAL A C     1 
ATOM   2659 O  O     . VAL A 1 337 ? 53.90900 -36.82800 -29.50900 1.000 82.24670  ? 337 VAL A O     1 
ATOM   2660 C  CB    . VAL A 1 337 ? 54.14500 -37.70900 -26.52300 1.000 76.48549  ? 337 VAL A CB    1 
ATOM   2661 C  CG1   . VAL A 1 337 ? 53.38500 -38.22600 -25.30900 1.000 77.63036  ? 337 VAL A CG1   1 
ATOM   2662 C  CG2   . VAL A 1 337 ? 55.65300 -37.79800 -26.31000 1.000 73.98519  ? 337 VAL A CG2   1 
ATOM   2663 N  N     . TYR A 1 338 ? 55.50000 -38.40500 -29.50600 1.000 80.62019  ? 338 TYR A N     1 
ATOM   2664 C  CA    . TYR A 1 338 ? 56.11400 -37.83500 -30.70100 1.000 74.49051  ? 338 TYR A CA    1 
ATOM   2665 C  C     . TYR A 1 338 ? 55.34600 -38.20600 -31.97500 1.000 79.17791  ? 338 TYR A C     1 
ATOM   2666 O  O     . TYR A 1 338 ? 55.15600 -37.36100 -32.87300 1.000 89.57127  ? 338 TYR A O     1 
ATOM   2667 C  CB    . TYR A 1 338 ? 57.57000 -38.29300 -30.77200 1.000 76.64340  ? 338 TYR A CB    1 
ATOM   2668 C  CG    . TYR A 1 338 ? 58.43100 -37.86400 -29.59600 1.000 81.70716  ? 338 TYR A CG    1 
ATOM   2669 C  CD1   . TYR A 1 338 ? 58.66400 -36.52100 -29.33100 1.000 85.46288  ? 338 TYR A CD1   1 
ATOM   2670 C  CD2   . TYR A 1 338 ? 59.01600 -38.80600 -28.75600 1.000 80.12276  ? 338 TYR A CD2   1 
ATOM   2671 C  CE1   . TYR A 1 338 ? 59.45200 -36.12400 -28.26000 1.000 84.43381  ? 338 TYR A CE1   1 
ATOM   2672 C  CE2   . TYR A 1 338 ? 59.80800 -38.41800 -27.68300 1.000 80.89128  ? 338 TYR A CE2   1 
ATOM   2673 C  CZ    . TYR A 1 338 ? 60.02200 -37.07500 -27.44000 1.000 82.12827  ? 338 TYR A CZ    1 
ATOM   2674 O  OH    . TYR A 1 338 ? 60.80600 -36.67400 -26.37900 1.000 73.64830  ? 338 TYR A OH    1 
ATOM   2675 N  N     . MET A 1 339 ? 54.78800 -39.42200 -32.01100 1.000 80.90181  ? 339 MET A N     1 
ATOM   2676 C  CA    . MET A 1 339 ? 53.84200 -39.78600 -33.06600 1.000 79.54901  ? 339 MET A CA    1 
ATOM   2677 C  C     . MET A 1 339 ? 52.59800 -38.90000 -33.01700 1.000 77.27769  ? 339 MET A C     1 
ATOM   2678 O  O     . MET A 1 339 ? 52.14100 -38.39700 -34.04700 1.000 76.31178  ? 339 MET A O     1 
ATOM   2679 C  CB    . MET A 1 339 ? 53.46600 -41.26000 -32.92300 1.000 84.22852  ? 339 MET A CB    1 
ATOM   2680 C  CG    . MET A 1 339 ? 54.60200 -42.23200 -33.21000 1.000 89.07121  ? 339 MET A CG    1 
ATOM   2681 S  SD    . MET A 1 339 ? 54.97500 -42.44900 -34.95800 1.000 103.60453 ? 339 MET A SD    1 
ATOM   2682 C  CE    . MET A 1 339 ? 53.57400 -43.40900 -35.52300 1.000 103.95194 ? 339 MET A CE    1 
ATOM   2683 N  N     . LEU A 1 340 ? 52.05000 -38.72400 -31.80800 1.000 74.28259  ? 340 LEU A N     1 
ATOM   2684 C  CA    . LEU A 1 340 ? 50.84400 -37.87000 -31.62300 1.000 78.21990  ? 340 LEU A CA    1 
ATOM   2685 C  C     . LEU A 1 340 ? 51.16800 -36.45500 -32.09500 1.000 76.27230  ? 340 LEU A C     1 
ATOM   2686 O  O     . LEU A 1 340 ? 50.28100 -35.82100 -32.68100 1.000 79.24898  ? 340 LEU A O     1 
ATOM   2687 C  CB    . LEU A 1 340 ? 50.50100 -37.82100 -30.13400 1.000 77.45929  ? 340 LEU A CB    1 
ATOM   2688 C  CG    . LEU A 1 340 ? 49.93600 -39.10200 -29.53400 1.000 83.09944  ? 340 LEU A CG    1 
ATOM   2689 C  CD1   . LEU A 1 340 ? 49.82800 -38.95300 -28.02700 1.000 80.12540  ? 340 LEU A CD1   1 
ATOM   2690 C  CD2   . LEU A 1 340 ? 48.58200 -39.42300 -30.14600 1.000 81.88877  ? 340 LEU A CD2   1 
ATOM   2691 N  N     . HIS A 1 341 ? 52.37500 -35.97500 -31.79000 1.000 70.23737  ? 341 HIS A N     1 
ATOM   2692 C  CA    . HIS A 1 341 ? 52.78400 -34.63800 -32.21200 1.000 68.86878  ? 341 HIS A CA    1 
ATOM   2693 C  C     . HIS A 1 341 ? 52.66400 -34.49200 -33.72100 1.000 77.57509  ? 341 HIS A C     1 
ATOM   2694 O  O     . HIS A 1 341 ? 52.06300 -33.53100 -34.22900 1.000 80.53071  ? 341 HIS A O     1 
ATOM   2695 C  CB    . HIS A 1 341 ? 54.20500 -34.32200 -31.75100 1.000 73.94044  ? 341 HIS A CB    1 
ATOM   2696 C  CG    . HIS A 1 341 ? 54.64100 -32.93200 -32.09500 1.000 74.76423  ? 341 HIS A CG    1 
ATOM   2697 N  ND1   . HIS A 1 341 ? 54.60000 -31.89100 -31.19200 1.000 70.59004  ? 341 HIS A ND1   1 
ATOM   2698 C  CD2   . HIS A 1 341 ? 55.11500 -32.40900 -33.25000 1.000 68.83457  ? 341 HIS A CD2   1 
ATOM   2699 C  CE1   . HIS A 1 341 ? 55.03300 -30.78800 -31.77600 1.000 68.05026  ? 341 HIS A CE1   1 
ATOM   2700 N  NE2   . HIS A 1 341 ? 55.35200 -31.07500 -33.02500 1.000 67.48967  ? 341 HIS A NE2   1 
ATOM   2701 N  N     . MET A 1 342 ? 53.28600 -35.41800 -34.45900 1.000 75.54590  ? 342 MET A N     1 
ATOM   2702 C  CA    . MET A 1 342 ? 53.22200 -35.31100 -35.91400 1.000 71.56648  ? 342 MET A CA    1 
ATOM   2703 C  C     . MET A 1 342 ? 51.79500 -35.48900 -36.42400 1.000 78.18569  ? 342 MET A C     1 
ATOM   2704 O  O     . MET A 1 342 ? 51.39900 -34.83800 -37.39900 1.000 81.80191  ? 342 MET A O     1 
ATOM   2705 C  CB    . MET A 1 342 ? 54.14600 -36.34500 -36.55600 1.000 83.63634  ? 342 MET A CB    1 
ATOM   2706 C  CG    . MET A 1 342 ? 55.60700 -36.17800 -36.18400 1.000 81.79402  ? 342 MET A CG    1 
ATOM   2707 S  SD    . MET A 1 342 ? 56.18300 -34.48300 -36.40100 1.000 81.25711  ? 342 MET A SD    1 
ATOM   2708 C  CE    . MET A 1 342 ? 55.98500 -34.28100 -38.16800 1.000 88.38165  ? 342 MET A CE    1 
ATOM   2709 N  N     . MET A 1 343 ? 50.99500 -36.31700 -35.74800 1.000 83.13892  ? 343 MET A N     1 
ATOM   2710 C  CA    . MET A 1 343 ? 49.58200 -36.45500 -36.10100 1.000 82.58622  ? 343 MET A CA    1 
ATOM   2711 C  C     . MET A 1 343 ? 48.82700 -35.14200 -35.91100 1.000 80.30437  ? 343 MET A C     1 
ATOM   2712 O  O     . MET A 1 343 ? 47.98100 -34.77500 -36.73400 1.000 80.15698  ? 343 MET A O     1 
ATOM   2713 C  CB    . MET A 1 343 ? 48.94400 -37.56000 -35.26400 1.000 82.71255  ? 343 MET A CB    1 
ATOM   2714 C  CG    . MET A 1 343 ? 49.36400 -38.96000 -35.67400 1.000 85.33392  ? 343 MET A CG    1 
ATOM   2715 S  SD    . MET A 1 343 ? 48.62100 -40.23900 -34.64800 1.000 107.13916 ? 343 MET A SD    1 
ATOM   2716 C  CE    . MET A 1 343 ? 49.85000 -41.53900 -34.79300 1.000 98.10387  ? 343 MET A CE    1 
ATOM   2717 N  N     . TYR A 1 344 ? 49.09800 -34.44400 -34.80800 1.000 71.12958  ? 344 TYR A N     1 
ATOM   2718 C  CA    . TYR A 1 344 ? 48.46600 -33.15800 -34.52700 1.000 71.33224  ? 344 TYR A CA    1 
ATOM   2719 C  C     . TYR A 1 344 ? 48.83100 -32.12400 -35.58800 1.000 72.75609  ? 344 TYR A C     1 
ATOM   2720 O  O     . TYR A 1 344 ? 47.96700 -31.36700 -36.05800 1.000 71.13484  ? 344 TYR A O     1 
ATOM   2721 C  CB    . TYR A 1 344 ? 48.90900 -32.72400 -33.12600 1.000 79.59375  ? 344 TYR A CB    1 
ATOM   2722 C  CG    . TYR A 1 344 ? 48.33000 -31.46100 -32.53300 1.000 79.65166  ? 344 TYR A CG    1 
ATOM   2723 C  CD1   . TYR A 1 344 ? 47.07300 -31.46100 -31.94000 1.000 82.45199  ? 344 TYR A CD1   1 
ATOM   2724 C  CD2   . TYR A 1 344 ? 49.08000 -30.29300 -32.47500 1.000 81.36765  ? 344 TYR A CD2   1 
ATOM   2725 C  CE1   . TYR A 1 344 ? 46.55400 -30.31500 -31.36100 1.000 87.05517  ? 344 TYR A CE1   1 
ATOM   2726 C  CE2   . TYR A 1 344 ? 48.57000 -29.14100 -31.89700 1.000 84.68384  ? 344 TYR A CE2   1 
ATOM   2727 C  CZ    . TYR A 1 344 ? 47.30500 -29.15900 -31.34100 1.000 89.94763  ? 344 TYR A CZ    1 
ATOM   2728 O  OH    . TYR A 1 344 ? 46.78600 -28.02100 -30.76400 1.000 100.19359 ? 344 TYR A OH    1 
ATOM   2729 N  N     . GLN A 1 345 ? 50.10700 -32.08100 -35.98300 1.000 76.20651  ? 345 GLN A N     1 
ATOM   2730 C  CA    . GLN A 1 345 ? 50.51000 -31.16800 -37.05300 1.000 72.25866  ? 345 GLN A CA    1 
ATOM   2731 C  C     . GLN A 1 345 ? 49.81900 -31.50700 -38.37000 1.000 74.87740  ? 345 GLN A C     1 
ATOM   2732 O  O     . GLN A 1 345 ? 49.36600 -30.60700 -39.09700 1.000 80.39385  ? 345 GLN A O     1 
ATOM   2733 C  CB    . GLN A 1 345 ? 52.02900 -31.15400 -37.22100 1.000 73.14561  ? 345 GLN A CB    1 
ATOM   2734 C  CG    . GLN A 1 345 ? 52.76300 -30.54400 -36.05100 1.000 71.07168  ? 345 GLN A CG    1 
ATOM   2735 C  CD    . GLN A 1 345 ? 52.31200 -29.11200 -35.80400 1.000 73.08771  ? 345 GLN A CD    1 
ATOM   2736 O  OE1   . GLN A 1 345 ? 52.12100 -28.34000 -36.74600 1.000 76.83026  ? 345 GLN A OE1   1 
ATOM   2737 N  NE2   . GLN A 1 345 ? 52.17000 -28.74400 -34.53900 1.000 77.15136  ? 345 GLN A NE2   1 
ATOM   2738 N  N     . ALA A 1 346 ? 49.74500 -32.79900 -38.70400 1.000 72.65871  ? 346 ALA A N     1 
ATOM   2739 C  CA    . ALA A 1 346 ? 49.03400 -33.20600 -39.91100 1.000 71.97179  ? 346 ALA A CA    1 
ATOM   2740 C  C     . ALA A 1 346 ? 47.57300 -32.78700 -39.84800 1.000 72.32446  ? 346 ALA A C     1 
ATOM   2741 O  O     . ALA A 1 346 ? 46.99300 -32.35700 -40.85300 1.000 73.33774  ? 346 ALA A O     1 
ATOM   2742 C  CB    . ALA A 1 346 ? 49.15300 -34.71600 -40.11500 1.000 76.28020  ? 346 ALA A CB    1 
ATOM   2743 N  N     . MET A 1 347 ? 46.94600 -32.94000 -38.68400 1.000 68.46084  ? 347 MET A N     1 
ATOM   2744 C  CA    . MET A 1 347 ? 45.57200 -32.48200 -38.55100 1.000 70.34528  ? 347 MET A CA    1 
ATOM   2745 C  C     . MET A 1 347 ? 45.45700 -30.98900 -38.81900 1.000 69.26357  ? 347 MET A C     1 
ATOM   2746 O  O     . MET A 1 347 ? 44.54400 -30.55100 -39.52500 1.000 70.70848  ? 347 MET A O     1 
ATOM   2747 C  CB    . MET A 1 347 ? 45.05500 -32.79600 -37.15000 1.000 70.54004  ? 347 MET A CB    1 
ATOM   2748 C  CG    . MET A 1 347 ? 43.58400 -32.52200 -36.97700 1.000 68.13712  ? 347 MET A CG    1 
ATOM   2749 S  SD    . MET A 1 347 ? 43.02500 -32.83200 -35.30000 1.000 64.13137  ? 347 MET A SD    1 
ATOM   2750 C  CE    . MET A 1 347 ? 41.26900 -32.51700 -35.47700 1.000 76.98818  ? 347 MET A CE    1 
ATOM   2751 N  N     . GLY A 1 348 ? 46.37500 -30.19100 -38.26700 1.000 70.41371  ? 348 GLY A N     1 
ATOM   2752 C  CA    . GLY A 1 348 ? 46.33200 -28.75700 -38.52400 1.000 68.24766  ? 348 GLY A CA    1 
ATOM   2753 C  C     . GLY A 1 348 ? 46.47000 -28.38600 -39.98900 1.000 67.95288  ? 348 GLY A C     1 
ATOM   2754 O  O     . GLY A 1 348 ? 45.73400 -27.53200 -40.49600 1.000 73.99571  ? 348 GLY A O     1 
ATOM   2755 N  N     . VAL A 1 349 ? 47.40700 -29.02100 -40.69900 1.000 65.70788  ? 349 VAL A N     1 
ATOM   2756 C  CA    . VAL A 1 349 ? 47.60900 -28.60400 -42.12000 1.000 67.99763  ? 349 VAL A CA    1 
ATOM   2757 C  C     . VAL A 1 349 ? 46.42600 -29.11400 -42.95100 1.000 70.07419  ? 349 VAL A C     1 
ATOM   2758 O  O     . VAL A 1 349 ? 46.10400 -28.45600 -43.94500 1.000 69.43201  ? 349 VAL A O     1 
ATOM   2759 C  CB    . VAL A 1 349 ? 48.98400 -28.99000 -42.70200 1.000 70.72953  ? 349 VAL A CB    1 
ATOM   2760 C  CG1   . VAL A 1 349 ? 50.08300 -28.08200 -42.17700 1.000 74.35102  ? 349 VAL A CG1   1 
ATOM   2761 C  CG2   . VAL A 1 349 ? 49.34000 -30.44400 -42.46500 1.000 82.52832  ? 349 VAL A CG2   1 
ATOM   2762 N  N     . CYS A 1 350 ? 45.78400 -30.21300 -42.53600 1.000 72.87716  ? 350 CYS A N     1 
ATOM   2763 C  CA    . CYS A 1 350 ? 44.56600 -30.69500 -43.24600 1.000 68.42136  ? 350 CYS A CA    1 
ATOM   2764 C  C     . CYS A 1 350 ? 43.43200 -29.70500 -42.97400 1.000 64.07610  ? 350 CYS A C     1 
ATOM   2765 O  O     . CYS A 1 350 ? 42.65500 -29.44400 -43.90600 1.000 69.59255  ? 350 CYS A O     1 
ATOM   2766 C  CB    . CYS A 1 350 ? 44.16100 -32.08100 -42.76500 1.000 69.48728  ? 350 CYS A CB    1 
ATOM   2767 S  SG    . CYS A 1 350 ? 45.37500 -33.36900 -43.15200 1.000 92.54794  ? 350 CYS A SG    1 
ATOM   2768 N  N     . LEU A 1 351 ? 43.32400 -29.20400 -41.74000 1.000 68.98196  ? 351 LEU A N     1 
ATOM   2769 C  CA    . LEU A 1 351 ? 42.34200 -28.18000 -41.41200 1.000 68.12922  ? 351 LEU A CA    1 
ATOM   2770 C  C     . LEU A 1 351 ? 42.53400 -26.95000 -42.29500 1.000 71.20064  ? 351 LEU A C     1 
ATOM   2771 O  O     . LEU A 1 351 ? 41.56200 -26.39600 -42.82300 1.000 72.11654  ? 351 LEU A O     1 
ATOM   2772 C  CB    . LEU A 1 351 ? 42.47500 -27.81100 -39.93400 1.000 70.99009  ? 351 LEU A CB    1 
ATOM   2773 C  CG    . LEU A 1 351 ? 41.95100 -28.84200 -38.93900 1.000 72.03758  ? 351 LEU A CG    1 
ATOM   2774 C  CD1   . LEU A 1 351 ? 42.18000 -28.37000 -37.51500 1.000 77.21452  ? 351 LEU A CD1   1 
ATOM   2775 C  CD2   . LEU A 1 351 ? 40.50300 -29.13300 -39.20300 1.000 70.99799  ? 351 LEU A CD2   1 
ATOM   2776 N  N     . TYR A 1 352 ? 43.78800 -26.52900 -42.49500 1.000 71.51910  ? 352 TYR A N     1 
ATOM   2777 C  CA    . TYR A 1 352 ? 44.05000 -25.40400 -43.38900 1.000 63.28390  ? 352 TYR A CA    1 
ATOM   2778 C  C     . TYR A 1 352 ? 43.67000 -25.73600 -44.82600 1.000 64.23139  ? 352 TYR A C     1 
ATOM   2779 O  O     . TYR A 1 352 ? 43.03300 -24.92400 -45.50800 1.000 67.17384  ? 352 TYR A O     1 
ATOM   2780 C  CB    . TYR A 1 352 ? 45.52600 -25.00500 -43.30200 1.000 59.40975  ? 352 TYR A CB    1 
ATOM   2781 C  CG    . TYR A 1 352 ? 45.89800 -23.80500 -44.14400 1.000 66.23952  ? 352 TYR A CG    1 
ATOM   2782 C  CD1   . TYR A 1 352 ? 45.42300 -22.53700 -43.84600 1.000 73.33248  ? 352 TYR A CD1   1 
ATOM   2783 C  CD2   . TYR A 1 352 ? 46.75300 -23.94500 -45.23200 1.000 75.40115  ? 352 TYR A CD2   1 
ATOM   2784 C  CE1   . TYR A 1 352 ? 45.77100 -21.44300 -44.62800 1.000 78.52520  ? 352 TYR A CE1   1 
ATOM   2785 C  CE2   . TYR A 1 352 ? 47.10800 -22.85900 -46.01600 1.000 83.24156  ? 352 TYR A CE2   1 
ATOM   2786 C  CZ    . TYR A 1 352 ? 46.61500 -21.60900 -45.70900 1.000 80.67809  ? 352 TYR A CZ    1 
ATOM   2787 O  OH    . TYR A 1 352 ? 46.96400 -20.52500 -46.48700 1.000 82.33092  ? 352 TYR A OH    1 
ATOM   2788 N  N     . MET A 1 353 ? 43.99900 -26.94700 -45.28200 1.000 65.86842  ? 353 MET A N     1 
ATOM   2789 C  CA    . MET A 1 353 ? 43.62400 -27.40800 -46.61300 1.000 70.58478  ? 353 MET A CA    1 
ATOM   2790 C  C     . MET A 1 353 ? 42.12100 -27.60100 -46.76200 1.000 74.85371  ? 353 MET A C     1 
ATOM   2791 O  O     . MET A 1 353 ? 41.65600 -27.89000 -47.87100 1.000 77.48561  ? 353 MET A O     1 
ATOM   2792 C  CB    . MET A 1 353 ? 44.36600 -28.70000 -46.95800 1.000 72.26919  ? 353 MET A CB    1 
ATOM   2793 C  CG    . MET A 1 353 ? 45.86500 -28.48600 -47.13600 1.000 75.45642  ? 353 MET A CG    1 
ATOM   2794 S  SD    . MET A 1 353 ? 46.83800 -29.98000 -47.41800 1.000 86.29982  ? 353 MET A SD    1 
ATOM   2795 C  CE    . MET A 1 353 ? 46.57800 -30.24700 -49.16900 1.000 83.51528  ? 353 MET A CE    1 
ATOM   2796 N  N     . GLN A 1 354 ? 41.37100 -27.47400 -45.66900 1.000 74.27733  ? 354 GLN A N     1 
ATOM   2797 C  CA    . GLN A 1 354 ? 39.93200 -27.72000 -45.61800 1.000 71.71386  ? 354 GLN A CA    1 
ATOM   2798 C  C     . GLN A 1 354 ? 39.56700 -29.14600 -46.02000 1.000 73.21141  ? 354 GLN A C     1 
ATOM   2799 O  O     . GLN A 1 354 ? 38.51200 -29.38300 -46.61200 1.000 76.04596  ? 354 GLN A O     1 
ATOM   2800 C  CB    . GLN A 1 354 ? 39.18200 -26.71000 -46.49000 1.000 72.90348  ? 354 GLN A CB    1 
ATOM   2801 C  CG    . GLN A 1 354 ? 39.56400 -25.26800 -46.19400 1.000 71.71386  ? 354 GLN A CG    1 
ATOM   2802 C  CD    . GLN A 1 354 ? 38.55200 -24.27400 -46.72200 1.000 82.31776  ? 354 GLN A CD    1 
ATOM   2803 O  OE1   . GLN A 1 354 ? 37.53500 -24.65400 -47.30500 1.000 88.35796  ? 354 GLN A OE1   1 
ATOM   2804 N  NE2   . GLN A 1 354 ? 38.82900 -22.98800 -46.52900 1.000 75.32745  ? 354 GLN A NE2   1 
ATOM   2805 N  N     . ASP A 1 355 ? 40.44000 -30.10300 -45.71100 1.000 88.22900  ? 355 ASP A N     1 
ATOM   2806 C  CA    . ASP A 1 355 ? 40.14300 -31.52400 -45.89300 1.000 89.76339  ? 355 ASP A CA    1 
ATOM   2807 C  C     . ASP A 1 355 ? 39.58100 -31.99100 -44.55300 1.000 88.29480  ? 355 ASP A C     1 
ATOM   2808 O  O     . ASP A 1 355 ? 40.30600 -32.50600 -43.69700 1.000 87.09465  ? 355 ASP A O     1 
ATOM   2809 C  CB    . ASP A 1 355 ? 41.38300 -32.30100 -46.32300 1.000 90.66350  ? 355 ASP A CB    1 
ATOM   2810 C  CG    . ASP A 1 355 ? 41.13700 -33.80600 -46.42100 1.000 100.93315 ? 355 ASP A CG    1 
ATOM   2811 O  OD1   . ASP A 1 355 ? 39.97000 -34.24500 -46.32100 1.000 102.12014 ? 355 ASP A OD1   1 
ATOM   2812 O  OD2   . ASP A 1 355 ? 42.11900 -34.55700 -46.60100 1.000 109.90002 ? 355 ASP A OD2   1 
ATOM   2813 N  N     . TRP A 1 356 ? 38.27100 -31.81600 -44.36300 1.000 83.47053  ? 356 TRP A N     1 
ATOM   2814 C  CA    . TRP A 1 356 ? 37.69900 -32.04100 -43.03900 1.000 79.28319  ? 356 TRP A CA    1 
ATOM   2815 C  C     . TRP A 1 356 ? 37.72500 -33.51700 -42.66100 1.000 77.15925  ? 356 TRP A C     1 
ATOM   2816 O  O     . TRP A 1 356 ? 37.99500 -33.86000 -41.50300 1.000 79.42268  ? 356 TRP A O     1 
ATOM   2817 C  CB    . TRP A 1 356 ? 36.25600 -31.53600 -42.98800 1.000 78.93315  ? 356 TRP A CB    1 
ATOM   2818 C  CG    . TRP A 1 356 ? 36.01400 -30.15900 -43.54900 1.000 78.34887  ? 356 TRP A CG    1 
ATOM   2819 C  CD1   . TRP A 1 356 ? 35.14200 -29.83400 -44.54700 1.000 76.47496  ? 356 TRP A CD1   1 
ATOM   2820 C  CD2   . TRP A 1 356 ? 36.64000 -28.92900 -43.15100 1.000 70.45845  ? 356 TRP A CD2   1 
ATOM   2821 N  NE1   . TRP A 1 356 ? 35.18200 -28.48500 -44.79400 1.000 76.51444  ? 356 TRP A NE1   1 
ATOM   2822 C  CE2   . TRP A 1 356 ? 36.09400 -27.90600 -43.95400 1.000 72.16655  ? 356 TRP A CE2   1 
ATOM   2823 C  CE3   . TRP A 1 356 ? 37.60700 -28.59300 -42.20000 1.000 68.98722  ? 356 TRP A CE3   1 
ATOM   2824 C  CZ2   . TRP A 1 356 ? 36.48200 -26.57300 -43.83400 1.000 70.46108  ? 356 TRP A CZ2   1 
ATOM   2825 C  CZ3   . TRP A 1 356 ? 37.99100 -27.26600 -42.08300 1.000 69.50307  ? 356 TRP A CZ3   1 
ATOM   2826 C  CH2   . TRP A 1 356 ? 37.42900 -26.27400 -42.89500 1.000 66.95803  ? 356 TRP A CH2   1 
ATOM   2827 N  N     . GLU A 1 357 ? 37.49500 -34.40400 -43.63400 1.000 87.66314  ? 357 GLU A N     1 
ATOM   2828 C  CA    . GLU A 1 357 ? 37.53000 -35.83800 -43.35900 1.000 88.55272  ? 357 GLU A CA    1 
ATOM   2829 C  C     . GLU A 1 357 ? 38.91800 -36.30500 -42.92300 1.000 87.65788  ? 357 GLU A C     1 
ATOM   2830 O  O     . GLU A 1 357 ? 39.05200 -37.06200 -41.95300 1.000 90.32662  ? 357 GLU A O     1 
ATOM   2831 C  CB    . GLU A 1 357 ? 37.07000 -36.62300 -44.59300 1.000 91.51097  ? 357 GLU A CB    1 
ATOM   2832 C  CG    . GLU A 1 357 ? 35.60600 -36.43000 -45.02000 1.000 93.07169  ? 357 GLU A CG    1 
ATOM   2833 C  CD    . GLU A 1 357 ? 35.40200 -35.27600 -45.99800 1.000 102.94655 ? 357 GLU A CD    1 
ATOM   2834 O  OE1   . GLU A 1 357 ? 36.36300 -34.51100 -46.23300 1.000 104.26250 ? 357 GLU A OE1   1 
ATOM   2835 O  OE2   . GLU A 1 357 ? 34.28000 -35.15000 -46.54800 1.000 95.17983  ? 357 GLU A OE2   1 
ATOM   2836 N  N     . GLY A 1 358 ? 39.96500 -35.86900 -43.62900 1.000 83.42316  ? 358 GLY A N     1 
ATOM   2837 C  CA    . GLY A 1 358 ? 41.31900 -36.23100 -43.22700 1.000 81.78086  ? 358 GLY A CA    1 
ATOM   2838 C  C     . GLY A 1 358 ? 41.68100 -35.76000 -41.83100 1.000 75.95384  ? 358 GLY A C     1 
ATOM   2839 O  O     . GLY A 1 358 ? 42.23900 -36.51900 -41.02300 1.000 85.34708  ? 358 GLY A O     1 
ATOM   2840 N  N     . ALA A 1 359 ? 41.39400 -34.48800 -41.53300 1.000 74.63263  ? 359 ALA A N     1 
ATOM   2841 C  CA    . ALA A 1 359 ? 41.72000 -33.95600 -40.21300 1.000 77.66194  ? 359 ALA A CA    1 
ATOM   2842 C  C     . ALA A 1 359 ? 40.95000 -34.68800 -39.12500 1.000 77.85407  ? 359 ALA A C     1 
ATOM   2843 O  O     . ALA A 1 359 ? 41.48200 -34.95100 -38.04000 1.000 78.70417  ? 359 ALA A O     1 
ATOM   2844 C  CB    . ALA A 1 359 ? 41.42600 -32.45800 -40.16700 1.000 74.16416  ? 359 ALA A CB    1 
ATOM   2845 N  N     . LEU A 1 360 ? 39.69300 -35.03100 -39.40700 1.000 77.15925  ? 360 LEU A N     1 
ATOM   2846 C  CA    . LEU A 1 360 ? 38.88400 -35.76500 -38.44300 1.000 77.69353  ? 360 LEU A CA    1 
ATOM   2847 C  C     . LEU A 1 360 ? 39.50800 -37.12900 -38.17700 1.000 81.51504  ? 360 LEU A C     1 
ATOM   2848 O  O     . LEU A 1 360 ? 39.57000 -37.59200 -37.02700 1.000 81.42818  ? 360 LEU A O     1 
ATOM   2849 C  CB    . LEU A 1 360 ? 37.44800 -35.87200 -38.95300 1.000 69.71099  ? 360 LEU A CB    1 
ATOM   2850 C  CG    . LEU A 1 360 ? 36.39400 -36.55300 -38.09100 1.000 70.74006  ? 360 LEU A CG    1 
ATOM   2851 C  CD1   . LEU A 1 360 ? 36.26000 -35.81600 -36.78200 1.000 68.70034  ? 360 LEU A CD1   1 
ATOM   2852 C  CD2   . LEU A 1 360 ? 35.07800 -36.49900 -38.82400 1.000 73.70357  ? 360 LEU A CD2   1 
ATOM   2853 N  N     . GLN A 1 361 ? 39.91400 -37.81200 -39.25300 1.000 84.95229  ? 361 GLN A N     1 
ATOM   2854 C  CA    . GLN A 1 361 ? 40.55800 -39.11600 -39.13900 1.000 86.28140  ? 361 GLN A CA    1 
ATOM   2855 C  C     . GLN A 1 361 ? 41.78900 -39.04400 -38.23300 1.000 84.95492  ? 361 GLN A C     1 
ATOM   2856 O  O     . GLN A 1 361 ? 41.99300 -39.92400 -37.38900 1.000 85.12600  ? 361 GLN A O     1 
ATOM   2857 C  CB    . GLN A 1 361 ? 40.91000 -39.60500 -40.54800 1.000 88.66326  ? 361 GLN A CB    1 
ATOM   2858 C  CG    . GLN A 1 361 ? 39.72800 -40.28200 -41.25500 1.000 90.81615  ? 361 GLN A CG    1 
ATOM   2859 C  CD    . GLN A 1 361 ? 40.08200 -40.88600 -42.60500 1.000 96.14574  ? 361 GLN A CD    1 
ATOM   2860 O  OE1   . GLN A 1 361 ? 41.10800 -40.55600 -43.20100 1.000 101.98328 ? 361 GLN A OE1   1 
ATOM   2861 N  NE2   . GLN A 1 361 ? 39.20900 -41.75300 -43.11000 1.000 96.81424  ? 361 GLN A NE2   1 
ATOM   2862 N  N     . TYR A 1 362 ? 42.62600 -38.01000 -38.39300 1.000 73.41143  ? 362 TYR A N     1 
ATOM   2863 C  CA    . TYR A 1 362 ? 43.79300 -37.87700 -37.50900 1.000 71.08221  ? 362 TYR A CA    1 
ATOM   2864 C  C     . TYR A 1 362 ? 43.38700 -37.57200 -36.06300 1.000 76.16176  ? 362 TYR A C     1 
ATOM   2865 O  O     . TYR A 1 362 ? 43.91700 -38.16900 -35.10800 1.000 82.82835  ? 362 TYR A O     1 
ATOM   2866 C  CB    . TYR A 1 362 ? 44.75700 -36.80300 -38.01900 1.000 68.58454  ? 362 TYR A CB    1 
ATOM   2867 C  CG    . TYR A 1 362 ? 45.65800 -37.23100 -39.15700 1.000 75.59854  ? 362 TYR A CG    1 
ATOM   2868 C  CD1   . TYR A 1 362 ? 46.61600 -38.21900 -38.96700 1.000 82.30724  ? 362 TYR A CD1   1 
ATOM   2869 C  CD2   . TYR A 1 362 ? 45.57900 -36.63200 -40.40500 1.000 81.95456  ? 362 TYR A CD2   1 
ATOM   2870 C  CE1   . TYR A 1 362 ? 47.46000 -38.61600 -39.99200 1.000 83.47317  ? 362 TYR A CE1   1 
ATOM   2871 C  CE2   . TYR A 1 362 ? 46.42100 -37.02200 -41.44200 1.000 90.32399  ? 362 TYR A CE2   1 
ATOM   2872 C  CZ    . TYR A 1 362 ? 47.36000 -38.01500 -41.22700 1.000 89.97131  ? 362 TYR A CZ    1 
ATOM   2873 O  OH    . TYR A 1 362 ? 48.20200 -38.41000 -42.24500 1.000 97.22745  ? 362 TYR A OH    1 
ATOM   2874 N  N     . GLY A 1 363 ? 42.43200 -36.65100 -35.89800 1.000 75.04584  ? 363 GLY A N     1 
ATOM   2875 C  CA    . GLY A 1 363 ? 41.98400 -36.25700 -34.54700 1.000 69.27936  ? 363 GLY A CA    1 
ATOM   2876 C  C     . GLY A 1 363 ? 41.43300 -37.42800 -33.75800 1.000 72.13496  ? 363 GLY A C     1 
ATOM   2877 O  O     . GLY A 1 363 ? 41.58300 -37.43100 -32.52300 1.000 81.92824  ? 363 GLY A O     1 
ATOM   2878 N  N     . GLN A 1 364 ? 40.80600 -38.38400 -34.44400 1.000 77.36980  ? 364 GLN A N     1 
ATOM   2879 C  CA    . GLN A 1 364 ? 40.20300 -39.55200 -33.75300 1.000 74.09309  ? 364 GLN A CA    1 
ATOM   2880 C  C     . GLN A 1 364 ? 41.31400 -40.37400 -33.09700 1.000 74.45893  ? 364 GLN A C     1 
ATOM   2881 O  O     . GLN A 1 364 ? 41.12900 -40.80700 -31.94600 1.000 81.85455  ? 364 GLN A O     1 
ATOM   2882 C  CB    . GLN A 1 364 ? 39.44700 -40.42200 -34.75300 1.000 72.36131  ? 364 GLN A CB    1 
ATOM   2883 C  CG    . GLN A 1 364 ? 38.00500 -39.99100 -34.94100 1.000 72.52185  ? 364 GLN A CG    1 
ATOM   2884 C  CD    . GLN A 1 364 ? 37.42300 -40.58900 -36.19500 1.000 85.94188  ? 364 GLN A CD    1 
ATOM   2885 O  OE1   . GLN A 1 364 ? 38.01700 -40.52900 -37.26800 1.000 97.07480  ? 364 GLN A OE1   1 
ATOM   2886 N  NE2   . GLN A 1 364 ? 36.24200 -41.17200 -36.06900 1.000 97.28272  ? 364 GLN A NE2   1 
ATOM   2887 N  N     . LYS A 1 365 ? 42.45000 -40.53800 -33.78700 1.000 70.30053  ? 365 LYS A N     1 
ATOM   2888 C  CA    . LYS A 1 365 ? 43.58000 -41.34600 -33.24500 1.000 79.18581  ? 365 LYS A CA    1 
ATOM   2889 C  C     . LYS A 1 365 ? 44.50100 -40.46100 -32.39300 1.000 80.19119  ? 365 LYS A C     1 
ATOM   2890 O  O     . LYS A 1 365 ? 45.62100 -40.90800 -32.07400 1.000 78.36992  ? 365 LYS A O     1 
ATOM   2891 C  CB    . LYS A 1 365 ? 44.33000 -42.06800 -34.37200 1.000 77.71984  ? 365 LYS A CB    1 
ATOM   2892 C  CG    . LYS A 1 365 ? 44.97100 -41.18100 -35.43200 1.000 86.09717  ? 365 LYS A CG    1 
ATOM   2893 C  CD    . LYS A 1 365 ? 45.35200 -41.91400 -36.70300 1.000 86.07085  ? 365 LYS A CD    1 
ATOM   2894 C  CE    . LYS A 1 365 ? 46.46600 -41.24200 -37.48000 1.000 89.67128  ? 365 LYS A CE    1 
ATOM   2895 N  NZ    . LYS A 1 365 ? 47.23200 -42.21600 -38.30600 1.000 87.39732  ? 365 LYS A NZ    1 
ATOM   2896 N  N     . ILE A 1 366 ? 44.03800 -39.26300 -32.02200 1.000 79.07001  ? 366 ILE A N     1 
ATOM   2897 C  CA    . ILE A 1 366 ? 44.85500 -38.33200 -31.18400 1.000 78.47257  ? 366 ILE A CA    1 
ATOM   2898 C  C     . ILE A 1 366 ? 44.21400 -38.23000 -29.79800 1.000 75.08005  ? 366 ILE A C     1 
ATOM   2899 O  O     . ILE A 1 366 ? 44.96300 -38.28000 -28.80200 1.000 74.66422  ? 366 ILE A O     1 
ATOM   2900 C  CB    . ILE A 1 366 ? 44.95900 -36.94700 -31.85900 1.000 74.59315  ? 366 ILE A CB    1 
ATOM   2901 C  CG1   . ILE A 1 366 ? 46.01600 -36.90700 -32.96200 1.000 79.09369  ? 366 ILE A CG1   1 
ATOM   2902 C  CG2   . ILE A 1 366 ? 45.19200 -35.83400 -30.85100 1.000 80.52808  ? 366 ILE A CG2   1 
ATOM   2903 C  CD1   . ILE A 1 366 ? 45.86600 -35.71000 -33.86400 1.000 84.44434  ? 366 ILE A CD1   1 
ATOM   2904 N  N     . ILE A 1 367 ? 42.88200 -38.15100 -29.73100 1.000 78.36203  ? 367 ILE A N     1 
ATOM   2905 C  CA    . ILE A 1 367 ? 42.19500 -37.92400 -28.42200 1.000 74.78791  ? 367 ILE A CA    1 
ATOM   2906 C  C     . ILE A 1 367 ? 42.37000 -39.12200 -27.47300 1.000 80.92812  ? 367 ILE A C     1 
ATOM   2907 O  O     . ILE A 1 367 ? 42.49400 -38.87700 -26.26000 1.000 74.04572  ? 367 ILE A O     1 
ATOM   2908 C  CB    . ILE A 1 367 ? 40.72700 -37.49000 -28.63500 1.000 67.62390  ? 367 ILE A CB    1 
ATOM   2909 C  CG1   . ILE A 1 367 ? 40.07400 -36.99200 -27.34200 1.000 58.63598  ? 367 ILE A CG1   1 
ATOM   2910 C  CG2   . ILE A 1 367 ? 39.89800 -38.57300 -29.31100 1.000 76.49601  ? 367 ILE A CG2   1 
ATOM   2911 C  CD1   . ILE A 1 367 ? 40.66300 -35.71500 -26.79200 1.000 60.27038  ? 367 ILE A CD1   1 
ATOM   2912 N  N     . LYS A 1 368 ? 42.40000 -40.35900 -27.98300 1.000 93.91652  ? 368 LYS A N     1 
ATOM   2913 C  CA    . LYS A 1 368 ? 42.48000 -41.53300 -27.06700 1.000 94.63766  ? 368 LYS A CA    1 
ATOM   2914 C  C     . LYS A 1 368 ? 43.74500 -41.44300 -26.19600 1.000 94.31920  ? 368 LYS A C     1 
ATOM   2915 O  O     . LYS A 1 368 ? 43.59600 -41.53400 -24.96300 1.000 93.72703  ? 368 LYS A O     1 
ATOM   2916 C  CB    . LYS A 1 368 ? 42.27400 -42.86800 -27.79700 1.000 97.00637  ? 368 LYS A CB    1 
ATOM   2917 C  CG    . LYS A 1 368 ? 42.27400 -44.10200 -26.90000 1.000 98.18809  ? 368 LYS A CG    1 
ATOM   2918 C  CD    . LYS A 1 368 ? 42.02100 -45.40600 -27.63500 1.000 115.15328 ? 368 LYS A CD    1 
ATOM   2919 C  CE    . LYS A 1 368 ? 42.04900 -46.62300 -26.73000 1.000 119.04848 ? 368 LYS A CE    1 
ATOM   2920 N  NZ    . LYS A 1 368 ? 41.79800 -47.88900 -27.47800 1.000 120.57761 ? 368 LYS A NZ    1 
ATOM   2921 N  N     . PRO A 1 369 ? 44.98100 -41.29900 -26.73300 1.000 82.19407  ? 369 PRO A N     1 
ATOM   2922 C  CA    . PRO A 1 369 ? 46.16100 -41.10600 -25.88000 1.000 79.73588  ? 369 PRO A CA    1 
ATOM   2923 C  C     . PRO A 1 369 ? 46.22300 -39.73200 -25.18700 1.000 78.16990  ? 369 PRO A C     1 
ATOM   2924 O  O     . PRO A 1 369 ? 46.65000 -39.69900 -24.04900 1.000 85.38919  ? 369 PRO A O     1 
ATOM   2925 C  CB    . PRO A 1 369 ? 47.35600 -41.28900 -26.82500 1.000 85.31812  ? 369 PRO A CB    1 
ATOM   2926 C  CG    . PRO A 1 369 ? 46.77800 -42.00700 -28.02100 1.000 80.61230  ? 369 PRO A CG    1 
ATOM   2927 C  CD    . PRO A 1 369 ? 45.37800 -41.45200 -28.13900 1.000 81.56504  ? 369 PRO A CD    1 
ATOM   2928 N  N     . TYR A 1 370 ? 45.80500 -38.67100 -25.86900 1.000 80.25173  ? 370 TYR A N     1 
ATOM   2929 C  CA    . TYR A 1 370 ? 45.81600 -37.32600 -25.30800 1.000 82.45199  ? 370 TYR A CA    1 
ATOM   2930 C  C     . TYR A 1 370 ? 45.16000 -37.28600 -23.93300 1.000 80.94918  ? 370 TYR A C     1 
ATOM   2931 O  O     . TYR A 1 370 ? 45.73300 -36.77700 -22.97000 1.000 80.75968  ? 370 TYR A O     1 
ATOM   2932 C  CB    . TYR A 1 370 ? 45.07600 -36.36900 -26.24400 1.000 80.62546  ? 370 TYR A CB    1 
ATOM   2933 C  CG    . TYR A 1 370 ? 45.95100 -35.31700 -26.88700 1.000 81.86508  ? 370 TYR A CG    1 
ATOM   2934 C  CD1   . TYR A 1 370 ? 47.29200 -35.56300 -27.14900 1.000 89.93973  ? 370 TYR A CD1   1 
ATOM   2935 C  CD2   . TYR A 1 370 ? 45.43200 -34.07800 -27.23800 1.000 77.88829  ? 370 TYR A CD2   1 
ATOM   2936 C  CE1   . TYR A 1 370 ? 48.09200 -34.60300 -27.73900 1.000 96.64317  ? 370 TYR A CE1   1 
ATOM   2937 C  CE2   . TYR A 1 370 ? 46.22400 -33.11200 -27.82800 1.000 83.13102  ? 370 TYR A CE2   1 
ATOM   2938 C  CZ    . TYR A 1 370 ? 47.55300 -33.37900 -28.07600 1.000 94.54555  ? 370 TYR A CZ    1 
ATOM   2939 O  OH    . TYR A 1 370 ? 48.34300 -32.41800 -28.66400 1.000 100.27518 ? 370 TYR A OH    1 
ATOM   2940 N  N     . SER A 1 371 ? 43.94800 -37.82500 -23.85700 1.000 77.04608  ? 371 SER A N     1 
ATOM   2941 C  CA    . SER A 1 371 ? 43.17600 -37.84700 -22.62000 1.000 69.89522  ? 371 SER A CA    1 
ATOM   2942 C  C     . SER A 1 371 ? 43.91600 -38.41500 -21.40800 1.000 75.85383  ? 371 SER A C     1 
ATOM   2943 O  O     . SER A 1 371 ? 43.70700 -37.94300 -20.28800 1.000 83.90480  ? 371 SER A O     1 
ATOM   2944 C  CB    . SER A 1 371 ? 41.85900 -38.60100 -22.82800 1.000 83.68109  ? 371 SER A CB    1 
ATOM   2945 O  OG    . SER A 1 371 ? 42.07900 -39.85600 -23.44700 1.000 98.45128  ? 371 SER A OG    1 
ATOM   2946 N  N     . LYS A 1 372 ? 44.76700 -39.41900 -21.63200 1.000 76.30125  ? 372 LYS A N     1 
ATOM   2947 C  CA    . LYS A 1 372 ? 45.51400 -40.05500 -20.55500 1.000 81.82297  ? 372 LYS A CA    1 
ATOM   2948 C  C     . LYS A 1 372 ? 46.84900 -39.38400 -20.27800 1.000 77.49613  ? 372 LYS A C     1 
ATOM   2949 O  O     . LYS A 1 372 ? 47.33100 -39.43600 -19.13900 1.000 79.51480  ? 372 LYS A O     1 
ATOM   2950 C  CB    . LYS A 1 372 ? 45.78000 -41.52700 -20.89000 1.000 78.40151  ? 372 LYS A CB    1 
ATOM   2951 C  CG    . LYS A 1 372 ? 44.57300 -42.34500 -21.33600 1.000 81.46766  ? 372 LYS A CG    1 
ATOM   2952 C  CD    . LYS A 1 372 ? 45.02800 -43.75300 -21.70300 1.000 89.15016  ? 372 LYS A CD    1 
ATOM   2953 C  CE    . LYS A 1 372 ? 43.89400 -44.63400 -22.19000 1.000 95.36933  ? 372 LYS A CE    1 
ATOM   2954 N  NZ    . LYS A 1 372 ? 44.38500 -46.00400 -22.51400 1.000 99.39350  ? 372 LYS A NZ    1 
ATOM   2955 N  N     . HIS A 1 373 ? 47.46200 -38.75400 -21.27800 1.000 69.66888  ? 373 HIS A N     1 
ATOM   2956 C  CA    . HIS A 1 373 ? 48.74800 -38.10700 -21.02500 1.000 72.56923  ? 373 HIS A CA    1 
ATOM   2957 C  C     . HIS A 1 373 ? 48.57600 -36.79100 -20.26300 1.000 70.67953  ? 373 HIS A C     1 
ATOM   2958 O  O     . HIS A 1 373 ? 49.42500 -36.43800 -19.43600 1.000 67.09752  ? 373 HIS A O     1 
ATOM   2959 C  CB    . HIS A 1 373 ? 49.50600 -37.89800 -22.33600 1.000 77.96987  ? 373 HIS A CB    1 
ATOM   2960 C  CG    . HIS A 1 373 ? 49.97500 -39.17600 -22.96200 1.000 76.98291  ? 373 HIS A CG    1 
ATOM   2961 N  ND1   . HIS A 1 373 ? 50.31400 -40.29000 -22.22300 1.000 83.49685  ? 373 HIS A ND1   1 
ATOM   2962 C  CD2   . HIS A 1 373 ? 50.14600 -39.52000 -24.26000 1.000 70.87955  ? 373 HIS A CD2   1 
ATOM   2963 C  CE1   . HIS A 1 373 ? 50.68000 -41.26300 -23.04000 1.000 89.65285  ? 373 HIS A CE1   1 
ATOM   2964 N  NE2   . HIS A 1 373 ? 50.58600 -40.82100 -24.28100 1.000 81.21500  ? 373 HIS A NE2   1 
ATOM   2965 N  N     . TYR A 1 374 ? 47.51100 -36.03400 -20.55800 1.000 70.39528  ? 374 TYR A N     1 
ATOM   2966 C  CA    . TYR A 1 374 ? 47.23600 -34.74400 -19.94000 1.000 67.13963  ? 374 TYR A CA    1 
ATOM   2967 C  C     . TYR A 1 374 ? 46.53500 -34.89200 -18.58600 1.000 72.15076  ? 374 TYR A C     1 
ATOM   2968 O  O     . TYR A 1 374 ? 45.95300 -35.93900 -18.28600 1.000 71.01904  ? 374 TYR A O     1 
ATOM   2969 C  CB    . TYR A 1 374 ? 46.35400 -33.91300 -20.86800 1.000 57.42267  ? 374 TYR A CB    1 
ATOM   2970 C  CG    . TYR A 1 374 ? 47.09700 -33.26200 -22.00900 1.000 64.16559  ? 374 TYR A CG    1 
ATOM   2971 C  CD1   . TYR A 1 374 ? 47.95100 -32.19100 -21.78700 1.000 65.12097  ? 374 TYR A CD1   1 
ATOM   2972 C  CD2   . TYR A 1 374 ? 46.94500 -33.72100 -23.31100 1.000 70.85323  ? 374 TYR A CD2   1 
ATOM   2973 C  CE1   . TYR A 1 374 ? 48.63600 -31.59800 -22.83000 1.000 56.31728  ? 374 TYR A CE1   1 
ATOM   2974 C  CE2   . TYR A 1 374 ? 47.62300 -33.13500 -24.35700 1.000 70.72953  ? 374 TYR A CE2   1 
ATOM   2975 C  CZ    . TYR A 1 374 ? 48.46600 -32.07700 -24.11100 1.000 59.84928  ? 374 TYR A CZ    1 
ATOM   2976 O  OH    . TYR A 1 374 ? 49.13200 -31.50300 -25.16600 1.000 71.21117  ? 374 TYR A OH    1 
ATOM   2977 N  N     . PRO A 1 375 ? 46.58400 -33.85700 -17.74200 1.000 67.34492  ? 375 PRO A N     1 
ATOM   2978 C  CA    . PRO A 1 375 ? 45.86200 -33.91200 -16.46400 1.000 65.32362  ? 375 PRO A CA    1 
ATOM   2979 C  C     . PRO A 1 375 ? 44.36200 -33.97500 -16.70100 1.000 66.12372  ? 375 PRO A C     1 
ATOM   2980 O  O     . PRO A 1 375 ? 43.86600 -33.72700 -17.80200 1.000 66.32637  ? 375 PRO A O     1 
ATOM   2981 C  CB    . PRO A 1 375 ? 46.26400 -32.61000 -15.76400 1.000 61.58633  ? 375 PRO A CB    1 
ATOM   2982 C  CG    . PRO A 1 375 ? 47.52500 -32.19100 -16.43000 1.000 51.98781  ? 375 PRO A CG    1 
ATOM   2983 C  CD    . PRO A 1 375 ? 47.42000 -32.64900 -17.84700 1.000 55.00396  ? 375 PRO A CD    1 
ATOM   2984 N  N     . LEU A 1 376 ? 43.64100 -34.32600 -15.63200 1.000 68.11080  ? 376 LEU A N     1 
ATOM   2985 C  CA    . LEU A 1 376 ? 42.20000 -34.55900 -15.72800 1.000 68.43715  ? 376 LEU A CA    1 
ATOM   2986 C  C     . LEU A 1 376 ? 41.47000 -33.42200 -16.42100 1.000 65.87106  ? 376 LEU A C     1 
ATOM   2987 O  O     . LEU A 1 376 ? 40.73500 -33.63300 -17.39300 1.000 65.55260  ? 376 LEU A O     1 
ATOM   2988 C  CB    . LEU A 1 376 ? 41.59700 -34.74400 -14.34100 1.000 63.59710  ? 376 LEU A CB    1 
ATOM   2989 C  CG    . LEU A 1 376 ? 41.42100 -36.14400 -13.78400 1.000 64.94463  ? 376 LEU A CG    1 
ATOM   2990 C  CD1   . LEU A 1 376 ? 42.75000 -36.87000 -13.68300 1.000 86.92884  ? 376 LEU A CD1   1 
ATOM   2991 C  CD2   . LEU A 1 376 ? 40.73600 -36.02500 -12.44700 1.000 76.36179  ? 376 LEU A CD2   1 
ATOM   2992 N  N     . TYR A 1 377 ? 41.67000 -32.20800 -15.93600 1.000 62.26536  ? 377 TYR A N     1 
ATOM   2993 C  CA    . TYR A 1 377 ? 41.09500 -31.03100 -16.55500 1.000 58.75968  ? 377 TYR A CA    1 
ATOM   2994 C  C     . TYR A 1 377 ? 42.23100 -30.30800 -17.25600 1.000 53.85383  ? 377 TYR A C     1 
ATOM   2995 O  O     . TYR A 1 377 ? 43.09700 -29.71700 -16.60300 1.000 56.55678  ? 377 TYR A O     1 
ATOM   2996 C  CB    . TYR A 1 377 ? 40.43800 -30.16800 -15.48400 1.000 56.01987  ? 377 TYR A CB    1 
ATOM   2997 C  CG    . TYR A 1 377 ? 39.39600 -30.94100 -14.70900 1.000 60.16248  ? 377 TYR A CG    1 
ATOM   2998 C  CD1   . TYR A 1 377 ? 38.08600 -31.04000 -15.14800 1.000 66.33690  ? 377 TYR A CD1   1 
ATOM   2999 C  CD2   . TYR A 1 377 ? 39.74800 -31.60900 -13.54400 1.000 65.16834  ? 377 TYR A CD2   1 
ATOM   3000 C  CE1   . TYR A 1 377 ? 37.15500 -31.76700 -14.43400 1.000 67.89498  ? 377 TYR A CE1   1 
ATOM   3001 C  CE2   . TYR A 1 377 ? 38.82800 -32.33200 -12.82700 1.000 69.16619  ? 377 TYR A CE2   1 
ATOM   3002 C  CZ    . TYR A 1 377 ? 37.53200 -32.40900 -13.27400 1.000 70.54267  ? 377 TYR A CZ    1 
ATOM   3003 O  OH    . TYR A 1 377 ? 36.61300 -33.13300 -12.55400 1.000 81.03340  ? 377 TYR A OH    1 
ATOM   3004 N  N     . SER A 1 378 ? 42.24000 -30.39000 -18.58000 1.000 51.19561  ? 378 SER A N     1 
ATOM   3005 C  CA    . SER A 1 378 ? 43.29600 -29.82200 -19.39900 1.000 56.36202  ? 378 SER A CA    1 
ATOM   3006 C  C     . SER A 1 378 ? 42.61700 -29.12200 -20.56100 1.000 62.59961  ? 378 SER A C     1 
ATOM   3007 O  O     . SER A 1 378 ? 41.75700 -29.71000 -21.22400 1.000 62.69436  ? 378 SER A O     1 
ATOM   3008 C  CB    . SER A 1 378 ? 44.28000 -30.88800 -19.89500 1.000 59.81770  ? 378 SER A CB    1 
ATOM   3009 O  OG    . SER A 1 378 ? 45.12200 -30.36200 -20.90900 1.000 66.51324  ? 378 SER A OG    1 
ATOM   3010 N  N     . LEU A 1 379 ? 43.02100 -27.88200 -20.82200 1.000 59.15446  ? 379 LEU A N     1 
ATOM   3011 C  CA    . LEU A 1 379 ? 42.47600 -27.16500 -21.96600 1.000 58.51754  ? 379 LEU A CA    1 
ATOM   3012 C  C     . LEU A 1 379 ? 42.89400 -27.80000 -23.28300 1.000 60.82571  ? 379 LEU A C     1 
ATOM   3013 O  O     . LEU A 1 379 ? 42.18000 -27.66300 -24.28100 1.000 65.83684  ? 379 LEU A O     1 
ATOM   3014 C  CB    . LEU A 1 379 ? 42.88000 -25.69600 -21.90600 1.000 61.68108  ? 379 LEU A CB    1 
ATOM   3015 C  CG    . LEU A 1 379 ? 42.32600 -25.01300 -20.65900 1.000 53.25639  ? 379 LEU A CG    1 
ATOM   3016 C  CD1   . LEU A 1 379 ? 42.70900 -23.55000 -20.63500 1.000 60.39145  ? 379 LEU A CD1   1 
ATOM   3017 C  CD2   . LEU A 1 379 ? 40.81400 -25.17500 -20.62300 1.000 54.68287  ? 379 LEU A CD2   1 
ATOM   3018 N  N     . ASN A 1 380 ? 44.04200 -28.48200 -23.31300 1.000 56.14357  ? 380 ASN A N     1 
ATOM   3019 C  CA    . ASN A 1 380 ? 44.45100 -29.17400 -24.53100 1.000 55.35927  ? 380 ASN A CA    1 
ATOM   3020 C  C     . ASN A 1 380 ? 43.47200 -30.28800 -24.88900 1.000 59.03866  ? 380 ASN A C     1 
ATOM   3021 O  O     . ASN A 1 380 ? 43.04800 -30.41800 -26.05000 1.000 69.15040  ? 380 ASN A O     1 
ATOM   3022 C  CB    . ASN A 1 380 ? 45.84600 -29.76200 -24.32100 1.000 57.24371  ? 380 ASN A CB    1 
ATOM   3023 C  CG    . ASN A 1 380 ? 46.87800 -28.70800 -23.97800 1.000 60.68359  ? 380 ASN A CG    1 
ATOM   3024 O  OD1   . ASN A 1 380 ? 46.64700 -27.86500 -23.10900 1.000 58.80968  ? 380 ASN A OD1   1 
ATOM   3025 N  ND2   . ASN A 1 380 ? 48.02500 -28.75500 -24.64300 1.000 64.93937  ? 380 ASN A ND2   1 
ATOM   3026 N  N     . VAL A 1 381 ? 42.99500 -31.01300 -23.87700 1.000 55.85143  ? 381 VAL A N     1 
ATOM   3027 C  CA    . VAL A 1 381 ? 42.03900 -32.09100 -24.10800 1.000 56.85419  ? 381 VAL A CA    1 
ATOM   3028 C  C     . VAL A 1 381 ? 40.68200 -31.52000 -24.49500 1.000 59.75716  ? 381 VAL A C     1 
ATOM   3029 O  O     . VAL A 1 381 ? 40.03600 -31.99300 -25.44100 1.000 69.16882  ? 381 VAL A O     1 
ATOM   3030 C  CB    . VAL A 1 381 ? 41.94400 -32.99400 -22.86600 1.000 50.71398  ? 381 VAL A CB    1 
ATOM   3031 C  CG1   . VAL A 1 381 ? 40.87300 -34.05400 -23.05800 1.000 51.01664  ? 381 VAL A CG1   1 
ATOM   3032 C  CG2   . VAL A 1 381 ? 43.28500 -33.62700 -22.57700 1.000 60.24407  ? 381 VAL A CG2   1 
ATOM   3033 N  N     . ALA A 1 382 ? 40.20900 -30.52800 -23.73700 1.000 55.80669  ? 382 ALA A N     1 
ATOM   3034 C  CA    . ALA A 1 382 ? 38.93700 -29.88600 -24.04900 1.000 50.89558  ? 382 ALA A CA    1 
ATOM   3035 C  C     . ALA A 1 382 ? 38.93300 -29.36100 -25.47900 1.000 58.18856  ? 382 ALA A C     1 
ATOM   3036 O  O     . ALA A 1 382 ? 37.96100 -29.55300 -26.21700 1.000 67.48178  ? 382 ALA A O     1 
ATOM   3037 C  CB    . ALA A 1 382 ? 38.65900 -28.76000 -23.05400 1.000 66.12372  ? 382 ALA A CB    1 
ATOM   3038 N  N     A SER A 1 383 ? 39.98900 -28.64500 -25.87100 1.000 61.72319  ? 383 SER A N     1 
ATOM   3039 C  CA    A SER A 1 383 ? 40.04200 -28.09000 -27.21900 1.000 62.28642  ? 383 SER A CA    1 
ATOM   3040 C  C     A SER A 1 383 ? 40.04800 -29.19200 -28.27100 1.000 65.06043  ? 383 SER A C     1 
ATOM   3041 O  O     A SER A 1 383 ? 39.47400 -29.02100 -29.35400 1.000 69.63466  ? 383 SER A O     1 
ATOM   3042 C  CB    A SER A 1 383 ? 41.26800 -27.19100 -27.38800 1.000 67.29491  ? 383 SER A CB    1 
ATOM   3043 O  OG    A SER A 1 383 ? 42.47100 -27.89000 -27.11900 1.000 66.93960  ? 383 SER A OG    1 
ATOM   3044 N  N     . MET A 1 384 ? 40.69300 -30.33200 -27.98500 1.000 68.38715  ? 384 MET A N     1 
ATOM   3045 C  CA    . MET A 1 384 ? 40.64800 -31.41600 -28.96500 1.000 66.79748  ? 384 MET A CA    1 
ATOM   3046 C  C     . MET A 1 384 ? 39.24600 -31.99200 -29.10300 1.000 66.71326  ? 384 MET A C     1 
ATOM   3047 O  O     . MET A 1 384 ? 38.77100 -32.22000 -30.22400 1.000 71.57700  ? 384 MET A O     1 
ATOM   3048 C  CB    . MET A 1 384 ? 41.62800 -32.52400 -28.58200 1.000 65.17624  ? 384 MET A CB    1 
ATOM   3049 C  CG    . MET A 1 384 ? 42.90700 -32.50700 -29.38900 1.000 79.40952  ? 384 MET A CG    1 
ATOM   3050 S  SD    . MET A 1 384 ? 42.58600 -32.54800 -31.16100 1.000 89.06857  ? 384 MET A SD    1 
ATOM   3051 C  CE    . MET A 1 384 ? 41.85800 -34.17500 -31.34000 1.000 79.45163  ? 384 MET A CE    1 
ATOM   3052 N  N     . TRP A 1 385 ? 38.56500 -32.21700 -27.97600 1.000 60.27565  ? 385 TRP A N     1 
ATOM   3053 C  CA    . TRP A 1 385 ? 37.16200 -32.62600 -28.02200 1.000 61.83899  ? 385 TRP A CA    1 
ATOM   3054 C  C     . TRP A 1 385 ? 36.30000 -31.61900 -28.77000 1.000 64.50773  ? 385 TRP A C     1 
ATOM   3055 O  O     . TRP A 1 385 ? 35.38600 -31.99900 -29.50600 1.000 67.92920  ? 385 TRP A O     1 
ATOM   3056 C  CB    . TRP A 1 385 ? 36.62400 -32.83600 -26.60900 1.000 61.50474  ? 385 TRP A CB    1 
ATOM   3057 C  CG    . TRP A 1 385 ? 36.99200 -34.15400 -26.01600 1.000 63.99188  ? 385 TRP A CG    1 
ATOM   3058 C  CD1   . TRP A 1 385 ? 37.70100 -34.37200 -24.87200 1.000 65.04990  ? 385 TRP A CD1   1 
ATOM   3059 C  CD2   . TRP A 1 385 ? 36.64300 -35.44600 -26.52400 1.000 65.08938  ? 385 TRP A CD2   1 
ATOM   3060 N  NE1   . TRP A 1 385 ? 37.82600 -35.72100 -24.64200 1.000 60.42040  ? 385 TRP A NE1   1 
ATOM   3061 C  CE2   . TRP A 1 385 ? 37.18300 -36.40100 -25.64200 1.000 64.94726  ? 385 TRP A CE2   1 
ATOM   3062 C  CE3   . TRP A 1 385 ? 35.93000 -35.88700 -27.64200 1.000 64.27350  ? 385 TRP A CE3   1 
ATOM   3063 C  CZ2   . TRP A 1 385 ? 37.03200 -37.77000 -25.84200 1.000 69.02143  ? 385 TRP A CZ2   1 
ATOM   3064 C  CZ3   . TRP A 1 385 ? 35.78200 -37.24500 -27.83800 1.000 69.37148  ? 385 TRP A CZ3   1 
ATOM   3065 C  CH2   . TRP A 1 385 ? 36.33100 -38.17100 -26.94400 1.000 66.79748  ? 385 TRP A CH2   1 
ATOM   3066 N  N     . LEU A 1 386 ? 36.58800 -30.33200 -28.60200 1.000 64.32877  ? 386 LEU A N     1 
ATOM   3067 C  CA    . LEU A 1 386 ? 35.80600 -29.29400 -29.26000 1.000 65.23414  ? 386 LEU A CA    1 
ATOM   3068 C  C     . LEU A 1 386 ? 36.02000 -29.32200 -30.77200 1.000 72.33236  ? 386 LEU A C     1 
ATOM   3069 O  O     . LEU A 1 386 ? 35.05800 -29.26400 -31.54700 1.000 72.98770  ? 386 LEU A O     1 
ATOM   3070 C  CB    . LEU A 1 386 ? 36.17600 -27.94200 -28.65400 1.000 62.62330  ? 386 LEU A CB    1 
ATOM   3071 C  CG    . LEU A 1 386 ? 35.39700 -26.68400 -29.00200 1.000 68.16080  ? 386 LEU A CG    1 
ATOM   3072 C  CD1   . LEU A 1 386 ? 33.90800 -26.94500 -28.89200 1.000 67.04488  ? 386 LEU A CD1   1 
ATOM   3073 C  CD2   . LEU A 1 386 ? 35.82400 -25.60500 -28.03400 1.000 69.32147  ? 386 LEU A CD2   1 
ATOM   3074 N  N     . LYS A 1 387 ? 37.28200 -29.38700 -31.20600 1.000 78.73576  ? 387 LYS A N     1 
ATOM   3075 C  CA    . LYS A 1 387 ? 37.58500 -29.50400 -32.63000 1.000 80.00696  ? 387 LYS A CA    1 
ATOM   3076 C  C     . LYS A 1 387 ? 36.90900 -30.72500 -33.24300 1.000 81.85981  ? 387 LYS A C     1 
ATOM   3077 O  O     . LYS A 1 387 ? 36.30500 -30.64500 -34.32200 1.000 83.42579  ? 387 LYS A O     1 
ATOM   3078 C  CB    . LYS A 1 387 ? 39.09300 -29.62800 -32.82600 1.000 79.47795  ? 387 LYS A CB    1 
ATOM   3079 C  CG    . LYS A 1 387 ? 39.91400 -28.39100 -32.58000 1.000 88.43429  ? 387 LYS A CG    1 
ATOM   3080 C  CD    . LYS A 1 387 ? 41.37900 -28.76200 -32.74200 1.000 97.66961  ? 387 LYS A CD    1 
ATOM   3081 C  CE    . LYS A 1 387 ? 42.31900 -27.66400 -32.29800 1.000 98.46444  ? 387 LYS A CE    1 
ATOM   3082 N  NZ    . LYS A 1 387 ? 43.73300 -28.11400 -32.44900 1.000 89.80024  ? 387 LYS A NZ    1 
ATOM   3083 N  N     . LEU A 1 388 ? 37.02500 -31.87700 -32.56900 1.000 73.15351  ? 388 LEU A N     1 
ATOM   3084 C  CA    . LEU A 1 388 ? 36.37200 -33.10200 -33.02600 1.000 64.69723  ? 388 LEU A CA    1 
ATOM   3085 C  C     . LEU A 1 388 ? 34.86600 -32.91800 -33.14600 1.000 68.52664  ? 388 LEU A C     1 
ATOM   3086 O  O     . LEU A 1 388 ? 34.26100 -33.28900 -34.16000 1.000 71.50857  ? 388 LEU A O     1 
ATOM   3087 C  CB    . LEU A 1 388 ? 36.70700 -34.25400 -32.08100 1.000 60.94678  ? 388 LEU A CB    1 
ATOM   3088 C  CG    . LEU A 1 388 ? 38.06800 -34.90000 -32.34300 1.000 69.84785  ? 388 LEU A CG    1 
ATOM   3089 C  CD1   . LEU A 1 388 ? 38.37000 -35.97400 -31.30900 1.000 74.12468  ? 388 LEU A CD1   1 
ATOM   3090 C  CD2   . LEU A 1 388 ? 38.14900 -35.46100 -33.75300 1.000 74.58789  ? 388 LEU A CD2   1 
ATOM   3091 N  N     . GLY A 1 389 ? 34.24200 -32.38800 -32.09300 1.000 65.76315  ? 389 GLY A N     1 
ATOM   3092 C  CA    . GLY A 1 389 ? 32.80700 -32.19200 -32.10900 1.000 65.05517  ? 389 GLY A CA    1 
ATOM   3093 C  C     . GLY A 1 389 ? 32.37100 -31.30400 -33.25300 1.000 75.65907  ? 389 GLY A C     1 
ATOM   3094 O  O     . GLY A 1 389 ? 31.37300 -31.58200 -33.92100 1.000 84.64436  ? 389 GLY A O     1 
ATOM   3095 N  N     . ARG A 1 390 ? 33.12400 -30.23200 -33.50600 1.000 71.58753  ? 390 ARG A N     1 
ATOM   3096 C  CA    . ARG A 1 390 ? 32.75100 -29.31400 -34.57500 1.000 68.08185  ? 390 ARG A CA    1 
ATOM   3097 C  C     . ARG A 1 390 ? 32.94900 -29.93100 -35.95500 1.000 72.92716  ? 390 ARG A C     1 
ATOM   3098 O  O     . ARG A 1 390 ? 32.16500 -29.65800 -36.86800 1.000 84.48645  ? 390 ARG A O     1 
ATOM   3099 C  CB    . ARG A 1 390 ? 33.53700 -28.01500 -34.43700 1.000 73.11140  ? 390 ARG A CB    1 
ATOM   3100 C  CG    . ARG A 1 390 ? 32.95200 -27.07900 -33.39500 1.000 69.08197  ? 390 ARG A CG    1 
ATOM   3101 C  CD    . ARG A 1 390 ? 33.86500 -25.90700 -33.09400 1.000 70.99535  ? 390 ARG A CD    1 
ATOM   3102 N  NE    . ARG A 1 390 ? 33.23400 -24.97000 -32.17200 1.000 73.79569  ? 390 ARG A NE    1 
ATOM   3103 C  CZ    . ARG A 1 390 ? 33.85200 -23.94400 -31.60300 1.000 82.85467  ? 390 ARG A CZ    1 
ATOM   3104 N  NH1   . ARG A 1 390 ? 35.13000 -23.69600 -31.82900 1.000 86.45773  ? 390 ARG A NH1   1 
ATOM   3105 N  NH2   . ARG A 1 390 ? 33.16500 -23.13600 -30.80100 1.000 87.87633  ? 390 ARG A NH2   1 
ATOM   3106 N  N     . LEU A 1 391 ? 33.99300 -30.74700 -36.14100 1.000 68.27924  ? 391 LEU A N     1 
ATOM   3107 C  CA    . LEU A 1 391 ? 34.13000 -31.46900 -37.40800 1.000 70.15052  ? 391 LEU A CA    1 
ATOM   3108 C  C     . LEU A 1 391 ? 32.95500 -32.42600 -37.61200 1.000 76.04333  ? 391 LEU A C     1 
ATOM   3109 O  O     . LEU A 1 391 ? 32.33200 -32.44400 -38.68100 1.000 79.53322  ? 391 LEU A O     1 
ATOM   3110 C  CB    . LEU A 1 391 ? 35.47700 -32.18900 -37.47800 1.000 65.23151  ? 391 LEU A CB    1 
ATOM   3111 C  CG    . LEU A 1 391 ? 36.71000 -31.30300 -37.69300 1.000 62.78911  ? 391 LEU A CG    1 
ATOM   3112 C  CD1   . LEU A 1 391 ? 37.94600 -32.09400 -37.38400 1.000 68.61086  ? 391 LEU A CD1   1 
ATOM   3113 C  CD2   . LEU A 1 391 ? 36.75900 -30.81800 -39.13300 1.000 64.52353  ? 391 LEU A CD2   1 
ATOM   3114 N  N     . TYR A 1 392 ? 32.62700 -33.21600 -36.58400 1.000 72.84031  ? 392 TYR A N     1 
ATOM   3115 C  CA    . TYR A 1 392 ? 31.47900 -34.11700 -36.65200 1.000 73.26668  ? 392 TYR A CA    1 
ATOM   3116 C  C     . TYR A 1 392 ? 30.21500 -33.35200 -37.03300 1.000 80.01222  ? 392 TYR A C     1 
ATOM   3117 O  O     . TYR A 1 392 ? 29.48000 -33.75100 -37.94400 1.000 99.70406  ? 392 TYR A O     1 
ATOM   3118 C  CB    . TYR A 1 392 ? 31.29000 -34.81500 -35.30600 1.000 74.66948  ? 392 TYR A CB    1 
ATOM   3119 C  CG    . TYR A 1 392 ? 32.23200 -35.96800 -35.05500 1.000 77.12767  ? 392 TYR A CG    1 
ATOM   3120 C  CD1   . TYR A 1 392 ? 32.40800 -36.96600 -36.00000 1.000 83.53633  ? 392 TYR A CD1   1 
ATOM   3121 C  CD2   . TYR A 1 392 ? 32.94200 -36.06000 -33.86200 1.000 74.04835  ? 392 TYR A CD2   1 
ATOM   3122 C  CE1   . TYR A 1 392 ? 33.27500 -38.02300 -35.77000 1.000 85.27865  ? 392 TYR A CE1   1 
ATOM   3123 C  CE2   . TYR A 1 392 ? 33.80800 -37.11000 -33.62300 1.000 73.68515  ? 392 TYR A CE2   1 
ATOM   3124 C  CZ    . TYR A 1 392 ? 33.97200 -38.09000 -34.57900 1.000 81.95193  ? 392 TYR A CZ    1 
ATOM   3125 O  OH    . TYR A 1 392 ? 34.83500 -39.13700 -34.34400 1.000 81.34660  ? 392 TYR A OH    1 
ATOM   3126 N  N     . MET A 1 393 ? 29.93200 -32.25800 -36.31700 1.000 81.15184  ? 393 MET A N     1 
ATOM   3127 C  CA    . MET A 1 393 ? 28.74900 -31.45300 -36.60900 1.000 89.01857  ? 393 MET A CA    1 
ATOM   3128 C  C     . MET A 1 393 ? 28.78600 -30.93700 -38.04300 1.000 89.85551  ? 393 MET A C     1 
ATOM   3129 O  O     . MET A 1 393 ? 27.78300 -30.99500 -38.76500 1.000 110.06056 ? 393 MET A O     1 
ATOM   3130 C  CB    . MET A 1 393 ? 28.66000 -30.28100 -35.62800 1.000 94.25604  ? 393 MET A CB    1 
ATOM   3131 C  CG    . MET A 1 393 ? 28.35200 -30.67600 -34.18700 1.000 93.99548  ? 393 MET A CG    1 
ATOM   3132 S  SD    . MET A 1 393 ? 26.83600 -31.62800 -33.95500 1.000 125.12026 ? 393 MET A SD    1 
ATOM   3133 C  CE    . MET A 1 393 ? 26.71800 -31.64300 -32.16600 1.000 104.48095 ? 393 MET A CE    1 
ATOM   3134 N  N     . GLY A 1 394 ? 29.94200 -30.41800 -38.46900 1.000 78.91209  ? 394 GLY A N     1 
ATOM   3135 C  CA    . GLY A 1 394 ? 30.08100 -29.93500 -39.83100 1.000 94.87980  ? 394 GLY A CA    1 
ATOM   3136 C  C     . GLY A 1 394 ? 29.82400 -30.99600 -40.88000 1.000 91.27147  ? 394 GLY A C     1 
ATOM   3137 O  O     . GLY A 1 394 ? 29.26600 -30.70200 -41.94000 1.000 91.59782  ? 394 GLY A O     1 
ATOM   3138 N  N     . LEU A 1 395 ? 30.19900 -32.24200 -40.60300 1.000 84.85754  ? 395 LEU A N     1 
ATOM   3139 C  CA    . LEU A 1 395 ? 29.97000 -33.29500 -41.57300 1.000 88.52904  ? 395 LEU A CA    1 
ATOM   3140 C  C     . LEU A 1 395 ? 28.65900 -34.02000 -41.30700 1.000 100.54890 ? 395 LEU A C     1 
ATOM   3141 O  O     . LEU A 1 395 ? 28.40000 -35.05800 -41.92400 1.000 103.44398 ? 395 LEU A O     1 
ATOM   3142 C  CB    . LEU A 1 395 ? 31.14200 -34.27900 -41.54000 1.000 85.83661  ? 395 LEU A CB    1 
ATOM   3143 C  CG    . LEU A 1 395 ? 32.49600 -33.69500 -41.95800 1.000 79.74377  ? 395 LEU A CG    1 
ATOM   3144 C  CD1   . LEU A 1 395 ? 33.63900 -34.63600 -41.61200 1.000 78.25412  ? 395 LEU A CD1   1 
ATOM   3145 C  CD2   . LEU A 1 395 ? 32.51300 -33.37200 -43.43800 1.000 82.29145  ? 395 LEU A CD2   1 
ATOM   3146 N  N     . GLU A 1 396 ? 27.83800 -33.47800 -40.39600 1.000 106.99178 ? 396 GLU A N     1 
ATOM   3147 C  CA    . GLU A 1 396 ? 26.50200 -33.95500 -40.03300 1.000 108.85252 ? 396 GLU A CA    1 
ATOM   3148 C  C     . GLU A 1 396 ? 26.50100 -35.29100 -39.30500 1.000 108.59460 ? 396 GLU A C     1 
ATOM   3149 O  O     . GLU A 1 396 ? 25.51600 -36.03800 -39.38200 1.000 110.95278 ? 396 GLU A O     1 
ATOM   3150 C  CB    . GLU A 1 396 ? 25.55500 -33.94900 -41.22700 1.000 112.23188 ? 396 GLU A CB    1 
ATOM   3151 C  CG    . GLU A 1 396 ? 25.60200 -32.59700 -41.87600 1.000 112.08976 ? 396 GLU A CG    1 
ATOM   3152 C  CD    . GLU A 1 396 ? 24.73600 -31.62500 -41.10500 1.000 120.53024 ? 396 GLU A CD    1 
ATOM   3153 O  OE1   . GLU A 1 396 ? 23.68000 -32.07500 -40.61300 1.000 128.62595 ? 396 GLU A OE1   1 
ATOM   3154 O  OE2   . GLU A 1 396 ? 25.10700 -30.43600 -40.97300 1.000 126.69151 ? 396 GLU A OE2   1 
ATOM   3155 N  N     . HIS A 1 397 ? 27.60100 -35.60400 -38.60900 1.000 103.98089 ? 397 HIS A N     1 
ATOM   3156 C  CA    . HIS A 1 397 ? 27.64200 -36.81400 -37.74100 1.000 105.38369 ? 397 HIS A CA    1 
ATOM   3157 C  C     . HIS A 1 397 ? 27.20500 -36.31200 -36.36900 1.000 105.35737 ? 397 HIS A C     1 
ATOM   3158 O  O     . HIS A 1 397 ? 28.07400 -36.20000 -35.48600 1.000 102.50966 ? 397 HIS A O     1 
ATOM   3159 C  CB    . HIS A 1 397 ? 29.05900 -37.39000 -37.67000 1.000 101.54902 ? 397 HIS A CB    1 
ATOM   3160 C  CG    . HIS A 1 397 ? 29.54100 -37.96700 -38.95600 1.000 103.58347 ? 397 HIS A CG    1 
ATOM   3161 N  ND1   . HIS A 1 397 ? 29.71200 -37.20000 -40.08800 1.000 101.97012 ? 397 HIS A ND1   1 
ATOM   3162 C  CD2   . HIS A 1 397 ? 29.89300 -39.22600 -39.29400 1.000 106.14167 ? 397 HIS A CD2   1 
ATOM   3163 C  CE1   . HIS A 1 397 ? 30.14600 -37.96000 -41.07200 1.000 102.35175 ? 397 HIS A CE1   1 
ATOM   3164 N  NE2   . HIS A 1 397 ? 30.26500 -39.20900 -40.61000 1.000 105.61529 ? 397 HIS A NE2   1 
ATOM   3165 N  N     . LYS A 1 398 ? 25.91500 -35.94700 -36.22600 1.000 103.53873 ? 398 LYS A N     1 
ATOM   3166 C  CA    . LYS A 1 398 ? 25.38000 -35.31000 -34.98000 1.000 100.75682 ? 398 LYS A CA    1 
ATOM   3167 C  C     . LYS A 1 398 ? 25.55100 -36.20000 -33.73000 1.000 99.82249  ? 398 LYS A C     1 
ATOM   3168 O  O     . LYS A 1 398 ? 25.88000 -35.62300 -32.68200 1.000 106.51803 ? 398 LYS A O     1 
ATOM   3169 C  CB    . LYS A 1 398 ? 23.95300 -34.76200 -35.19700 1.000 106.51014 ? 398 LYS A CB    1 
ATOM   3170 C  CG    . LYS A 1 398 ? 23.29000 -34.01300 -34.02600 1.000 121.66196 ? 398 LYS A CG    1 
ATOM   3171 C  CD    . LYS A 1 398 ? 21.86300 -33.41500 -34.26000 1.000 142.59604 ? 398 LYS A CD    1 
ATOM   3172 C  CE    . LYS A 1 398 ? 21.23500 -32.70000 -33.06100 1.000 149.52319 ? 398 LYS A CE    1 
ATOM   3173 N  NZ    . LYS A 1 398 ? 19.86600 -32.11600 -33.25200 1.000 144.15413 ? 398 LYS A NZ    1 
ATOM   3174 N  N     . ALA A 1 399 ? 25.32600 -37.52400 -33.80500 1.000 92.26106  ? 399 ALA A N     1 
ATOM   3175 C  CA    . ALA A 1 399 ? 25.40900 -38.39500 -32.60800 1.000 92.36634  ? 399 ALA A CA    1 
ATOM   3176 C  C     . ALA A 1 399 ? 26.82000 -38.30800 -32.02000 1.000 97.14849  ? 399 ALA A C     1 
ATOM   3177 O  O     . ALA A 1 399 ? 26.94300 -37.96000 -30.82900 1.000 99.81197  ? 399 ALA A O     1 
ATOM   3178 C  CB    . ALA A 1 399 ? 25.05400 -39.81200 -32.97900 1.000 91.65573  ? 399 ALA A CB    1 
ATOM   3179 N  N     . ALA A 1 400 ? 27.83700 -38.61100 -32.83000 1.000 93.63754  ? 400 ALA A N     1 
ATOM   3180 C  CA    . ALA A 1 400 ? 29.22300 -38.54300 -32.37800 1.000 93.52700  ? 400 ALA A CA    1 
ATOM   3181 C  C     . ALA A 1 400 ? 29.63800 -37.11100 -32.03900 1.000 84.80490  ? 400 ALA A C     1 
ATOM   3182 O  O     . ALA A 1 400 ? 30.41900 -36.89000 -31.09800 1.000 82.91520  ? 400 ALA A O     1 
ATOM   3183 C  CB    . ALA A 1 400 ? 30.14400 -39.12700 -33.44500 1.000 81.58347  ? 400 ALA A CB    1 
ATOM   3184 N  N     . GLY A 1 401 ? 29.10200 -36.12700 -32.76900 1.000 80.35437  ? 401 GLY A N     1 
ATOM   3185 C  CA    . GLY A 1 401 ? 29.39500 -34.73600 -32.45500 1.000 89.28176  ? 401 GLY A CA    1 
ATOM   3186 C  C     . GLY A 1 401 ? 28.92000 -34.32600 -31.07500 1.000 91.38201  ? 401 GLY A C     1 
ATOM   3187 O  O     . GLY A 1 401 ? 29.64800 -33.68000 -30.31900 1.000 90.60823  ? 401 GLY A O     1 
ATOM   3188 N  N     . GLU A 1 402 ? 27.66600 -34.64600 -30.75700 1.000 99.00661  ? 402 GLU A N     1 
ATOM   3189 C  CA    . GLU A 1 402 ? 27.11500 -34.33000 -29.44400 1.000 98.65130  ? 402 GLU A CA    1 
ATOM   3190 C  C     . GLU A 1 402 ? 27.93800 -35.00600 -28.35200 1.000 97.07743  ? 402 GLU A C     1 
ATOM   3191 O  O     . GLU A 1 402 ? 28.21100 -34.39900 -27.30800 1.000 95.42197  ? 402 GLU A O     1 
ATOM   3192 C  CB    . GLU A 1 402 ? 25.63000 -34.69900 -29.36800 1.000 101.55691 ? 402 GLU A CB    1 
ATOM   3193 C  CG    . GLU A 1 402 ? 24.94500 -34.20000 -28.09100 1.000 105.23104 ? 402 GLU A CG    1 
ATOM   3194 C  CD    . GLU A 1 402 ? 23.45500 -34.50200 -28.05500 1.000 122.11201 ? 402 GLU A CD    1 
ATOM   3195 O  OE1   . GLU A 1 402 ? 22.82100 -34.55900 -29.13100 1.000 115.87705 ? 402 GLU A OE1   1 
ATOM   3196 O  OE2   . GLU A 1 402 ? 22.91600 -34.67000 -26.93700 1.000 129.00494 ? 402 GLU A OE2   1 
ATOM   3197 N  N     . LYS A 1 403 ? 28.30900 -36.27800 -28.56000 1.000 88.95014  ? 403 LYS A N     1 
ATOM   3198 C  CA    . LYS A 1 403 ? 29.16800 -36.96900 -27.59700 1.000 79.34636  ? 403 LYS A CA    1 
ATOM   3199 C  C     . LYS A 1 403 ? 30.44300 -36.16400 -27.32600 1.000 76.31705  ? 403 LYS A C     1 
ATOM   3200 O  O     . LYS A 1 403 ? 30.77900 -35.85800 -26.16600 1.000 78.62522  ? 403 LYS A O     1 
ATOM   3201 C  CB    . LYS A 1 403 ? 29.52500 -38.35500 -28.14900 1.000 80.39122  ? 403 LYS A CB    1 
ATOM   3202 C  CG    . LYS A 1 403 ? 28.48100 -39.44700 -27.93000 1.000 87.10781  ? 403 LYS A CG    1 
ATOM   3203 C  CD    . LYS A 1 403 ? 29.04200 -40.81400 -28.31400 1.000 95.41407  ? 403 LYS A CD    1 
ATOM   3204 C  CE    . LYS A 1 403 ? 27.98800 -41.91300 -28.26300 1.000 98.09860  ? 403 LYS A CE    1 
ATOM   3205 N  NZ    . LYS A 1 403 ? 27.48100 -42.14900 -26.88100 1.000 98.75921  ? 403 LYS A NZ    1 
ATOM   3206 N  N     . ALA A 1 404 ? 31.13600 -35.76300 -28.39900 1.000 77.06450  ? 404 ALA A N     1 
ATOM   3207 C  CA    . ALA A 1 404 ? 32.39900 -35.04600 -28.23400 1.000 70.09261  ? 404 ALA A CA    1 
ATOM   3208 C  C     . ALA A 1 404 ? 32.19500 -33.68700 -27.56600 1.000 71.83756  ? 404 ALA A C     1 
ATOM   3209 O  O     . ALA A 1 404 ? 32.98100 -33.28700 -26.69000 1.000 73.28247  ? 404 ALA A O     1 
ATOM   3210 C  CB    . ALA A 1 404 ? 33.07200 -34.88000 -29.59500 1.000 67.27649  ? 404 ALA A CB    1 
ATOM   3211 N  N     . LEU A 1 405 ? 31.14100 -32.96500 -27.95900 1.000 71.94020  ? 405 LEU A N     1 
ATOM   3212 C  CA    . LEU A 1 405 ? 30.87900 -31.66200 -27.35500 1.000 69.33463  ? 405 LEU A CA    1 
ATOM   3213 C  C     . LEU A 1 405 ? 30.58800 -31.79500 -25.86800 1.000 76.65919  ? 405 LEU A C     1 
ATOM   3214 O  O     . LEU A 1 405 ? 31.00300 -30.94200 -25.07500 1.000 72.65345  ? 405 LEU A O     1 
ATOM   3215 C  CB    . LEU A 1 405 ? 29.74200 -30.92600 -28.06300 1.000 66.27900  ? 405 LEU A CB    1 
ATOM   3216 C  CG    . LEU A 1 405 ? 30.02000 -30.45500 -29.48800 1.000 64.56827  ? 405 LEU A CG    1 
ATOM   3217 C  CD1   . LEU A 1 405 ? 28.81500 -29.72500 -30.04800 1.000 74.31681  ? 405 LEU A CD1   1 
ATOM   3218 C  CD2   . LEU A 1 405 ? 31.24600 -29.57000 -29.50200 1.000 68.46084  ? 405 LEU A CD2   1 
ATOM   3219 N  N     . LYS A 1 406 ? 29.84100 -32.83000 -25.46700 1.000 75.53274  ? 406 LYS A N     1 
ATOM   3220 C  CA    . LYS A 1 406 ? 29.59000 -32.99500 -24.04000 1.000 73.36932  ? 406 LYS A CA    1 
ATOM   3221 C  C     . LYS A 1 406 ? 30.87400 -33.28900 -23.27600 1.000 74.52472  ? 406 LYS A C     1 
ATOM   3222 O  O     . LYS A 1 406 ? 31.03600 -32.82900 -22.14100 1.000 75.43273  ? 406 LYS A O     1 
ATOM   3223 C  CB    . LYS A 1 406 ? 28.56600 -34.10100 -23.77400 1.000 80.27805  ? 406 LYS A CB    1 
ATOM   3224 C  CG    . LYS A 1 406 ? 27.12200 -33.74900 -24.08100 1.000 89.17648  ? 406 LYS A CG    1 
ATOM   3225 C  CD    . LYS A 1 406 ? 26.22200 -34.93200 -23.74600 1.000 99.93303  ? 406 LYS A CD    1 
ATOM   3226 C  CE    . LYS A 1 406 ? 24.78000 -34.69500 -24.15200 1.000 105.04681 ? 406 LYS A CE    1 
ATOM   3227 N  NZ    . LYS A 1 406 ? 23.87300 -35.69700 -23.51700 1.000 106.20747 ? 406 LYS A NZ    1 
ATOM   3228 N  N     . LYS A 1 407 ? 31.79700 -34.06100 -23.86300 1.000 76.64340  ? 407 LYS A N     1 
ATOM   3229 C  CA    . LYS A 1 407 ? 33.08700 -34.25400 -23.18900 1.000 76.15650  ? 407 LYS A CA    1 
ATOM   3230 C  C     . LYS A 1 407 ? 33.83700 -32.92900 -22.99900 1.000 70.60320  ? 407 LYS A C     1 
ATOM   3231 O  O     . LYS A 1 407 ? 34.35400 -32.62500 -21.89700 1.000 67.10805  ? 407 LYS A O     1 
ATOM   3232 C  CB    . LYS A 1 407 ? 33.95200 -35.24800 -23.96600 1.000 69.80047  ? 407 LYS A CB    1 
ATOM   3233 C  CG    . LYS A 1 407 ? 33.48200 -36.69100 -23.88400 1.000 68.66613  ? 407 LYS A CG    1 
ATOM   3234 C  CD    . LYS A 1 407 ? 33.90200 -37.31000 -22.55400 1.000 75.46431  ? 407 LYS A CD    1 
ATOM   3235 C  CE    . LYS A 1 407 ? 34.53400 -38.68400 -22.73300 1.000 87.92370  ? 407 LYS A CE    1 
ATOM   3236 N  NZ    . LYS A 1 407 ? 33.66900 -39.62700 -23.50500 1.000 84.04429  ? 407 LYS A NZ    1 
ATOM   3237 N  N     . ALA A 1 408 ? 33.80100 -32.07700 -24.03000 1.000 64.89725  ? 408 ALA A N     1 
ATOM   3238 C  CA    . ALA A 1 408 ? 34.44900 -30.77400 -23.91500 1.000 65.67630  ? 408 ALA A CA    1 
ATOM   3239 C  C     . ALA A 1 408 ? 33.79100 -29.93900 -22.82900 1.000 73.49302  ? 408 ALA A C     1 
ATOM   3240 O  O     . ALA A 1 408 ? 34.47700 -29.31800 -22.00800 1.000 77.46455  ? 408 ALA A O     1 
ATOM   3241 C  CB    . ALA A 1 408 ? 34.39900 -30.04400 -25.25800 1.000 67.36860  ? 408 ALA A CB    1 
ATOM   3242 N  N     . ILE A 1 409 ? 32.45800 -29.90800 -22.81500 1.000 70.49793  ? 409 ILE A N     1 
ATOM   3243 C  CA    . ILE A 1 409 ? 31.73400 -29.13400 -21.81200 1.000 64.87094  ? 409 ILE A CA    1 
ATOM   3244 C  C     . ILE A 1 409 ? 32.07400 -29.64200 -20.41900 1.000 72.05074  ? 409 ILE A C     1 
ATOM   3245 O  O     . ILE A 1 409 ? 32.21500 -28.86100 -19.47300 1.000 75.13006  ? 409 ILE A O     1 
ATOM   3246 C  CB    . ILE A 1 409 ? 30.21900 -29.16400 -22.08100 1.000 63.18126  ? 409 ILE A CB    1 
ATOM   3247 C  CG1   . ILE A 1 409 ? 29.88300 -28.30600 -23.29800 1.000 72.10865  ? 409 ILE A CG1   1 
ATOM   3248 C  CG2   . ILE A 1 409 ? 29.43800 -28.69000 -20.86600 1.000 71.31908  ? 409 ILE A CG2   1 
ATOM   3249 C  CD1   . ILE A 1 409 ? 28.45800 -28.47000 -23.76700 1.000 85.07862  ? 409 ILE A CD1   1 
ATOM   3250 N  N     . ALA A 1 410 ? 32.16800 -30.96700 -20.26200 1.000 76.05649  ? 410 ALA A N     1 
ATOM   3251 C  CA    . ALA A 1 410 ? 32.45100 -31.53700 -18.95000 1.000 73.72989  ? 410 ALA A CA    1 
ATOM   3252 C  C     . ALA A 1 410 ? 33.75300 -30.98900 -18.39500 1.000 72.23761  ? 410 ALA A C     1 
ATOM   3253 O  O     . ALA A 1 410 ? 33.85500 -30.71100 -17.19600 1.000 75.68802  ? 410 ALA A O     1 
ATOM   3254 C  CB    . ALA A 1 410 ? 32.50900 -33.06200 -19.04000 1.000 78.42519  ? 410 ALA A CB    1 
ATOM   3255 N  N     . ILE A 1 411 ? 34.76000 -30.81800 -19.25000 1.000 66.15793  ? 411 ILE A N     1 
ATOM   3256 C  CA    . ILE A 1 411 ? 36.00200 -30.24600 -18.71700 1.000 64.13927  ? 411 ILE A CA    1 
ATOM   3257 C  C     . ILE A 1 411 ? 35.88900 -28.72400 -18.55100 1.000 66.79485  ? 411 ILE A C     1 
ATOM   3258 O  O     . ILE A 1 411 ? 36.33600 -28.14800 -17.54200 1.000 70.25579  ? 411 ILE A O     1 
ATOM   3259 C  CB    . ILE A 1 411 ? 37.21300 -30.63700 -19.57900 1.000 63.41550  ? 411 ILE A CB    1 
ATOM   3260 C  CG1   . ILE A 1 411 ? 37.35600 -32.15700 -19.61700 1.000 71.85862  ? 411 ILE A CG1   1 
ATOM   3261 C  CG2   . ILE A 1 411 ? 38.48600 -30.00900 -19.03000 1.000 61.27577  ? 411 ILE A CG2   1 
ATOM   3262 C  CD1   . ILE A 1 411 ? 38.31600 -32.65500 -20.67000 1.000 65.46838  ? 411 ILE A CD1   1 
ATOM   3263 N  N     . MET A 1 412 ? 35.29200 -28.05000 -19.53800 1.000 64.91568  ? 412 MET A N     1 
ATOM   3264 C  CA    . MET A 1 412 ? 35.22300 -26.59200 -19.52900 1.000 64.87357  ? 412 MET A CA    1 
ATOM   3265 C  C     . MET A 1 412 ? 34.37600 -26.03500 -18.39100 1.000 70.31369  ? 412 MET A C     1 
ATOM   3266 O  O     . MET A 1 412 ? 34.65900 -24.93200 -17.90900 1.000 76.45917  ? 412 MET A O     1 
ATOM   3267 C  CB    . MET A 1 412 ? 34.68100 -26.10300 -20.87000 1.000 66.07108  ? 412 MET A CB    1 
ATOM   3268 C  CG    . MET A 1 412 ? 35.62900 -26.34700 -22.03400 1.000 69.12145  ? 412 MET A CG    1 
ATOM   3269 S  SD    . MET A 1 412 ? 34.92900 -25.85200 -23.61700 1.000 65.64208  ? 412 MET A SD    1 
ATOM   3270 C  CE    . MET A 1 412 ? 35.06400 -24.07200 -23.49100 1.000 69.29515  ? 412 MET A CE    1 
ATOM   3271 N  N     . GLU A 1 413 ? 33.33600 -26.75300 -17.95500 1.000 68.95037  ? 413 GLU A N     1 
ATOM   3272 C  CA    . GLU A 1 413 ? 32.55700 -26.28200 -16.81400 1.000 70.22947  ? 413 GLU A CA    1 
ATOM   3273 C  C     . GLU A 1 413 ? 33.45300 -26.07400 -15.60400 1.000 70.57951  ? 413 GLU A C     1 
ATOM   3274 O  O     . GLU A 1 413 ? 33.27000 -25.12200 -14.83700 1.000 72.93769  ? 413 GLU A O     1 
ATOM   3275 C  CB    . GLU A 1 413 ? 31.45300 -27.28200 -16.47400 1.000 71.71913  ? 413 GLU A CB    1 
ATOM   3276 C  CG    . GLU A 1 413 ? 30.21900 -27.20100 -17.34900 1.000 80.74652  ? 413 GLU A CG    1 
ATOM   3277 C  CD    . GLU A 1 413 ? 29.16800 -28.22000 -16.94800 1.000 91.55308  ? 413 GLU A CD    1 
ATOM   3278 O  OE1   . GLU A 1 413 ? 29.55900 -29.29500 -16.44700 1.000 93.37435  ? 413 GLU A OE1   1 
ATOM   3279 O  OE2   . GLU A 1 413 ? 27.96000 -27.96000 -17.15200 1.000 88.69748  ? 413 GLU A OE2   1 
ATOM   3280 N  N     . VAL A 1 414 ? 34.43900 -26.95400 -15.43100 1.000 65.88948  ? 414 VAL A N     1 
ATOM   3281 C  CA    . VAL A 1 414 ? 35.38800 -26.81900 -14.33500 1.000 63.70764  ? 414 VAL A CA    1 
ATOM   3282 C  C     . VAL A 1 414 ? 36.36600 -25.69000 -14.61900 1.000 64.29981  ? 414 VAL A C     1 
ATOM   3283 O  O     . VAL A 1 414 ? 36.55100 -24.78500 -13.79600 1.000 65.19729  ? 414 VAL A O     1 
ATOM   3284 C  CB    . VAL A 1 414 ? 36.11700 -28.15200 -14.08500 1.000 59.71242  ? 414 VAL A CB    1 
ATOM   3285 C  CG1   . VAL A 1 414 ? 37.23200 -27.96400 -13.07200 1.000 59.16236  ? 414 VAL A CG1   1 
ATOM   3286 C  CG2   . VAL A 1 414 ? 35.13700 -29.19200 -13.59200 1.000 67.03698  ? 414 VAL A CG2   1 
ATOM   3287 N  N     . ALA A 1 415 ? 36.99300 -25.71400 -15.80000 1.000 66.95803  ? 415 ALA A N     1 
ATOM   3288 C  CA    . ALA A 1 415 ? 38.06000 -24.74900 -16.06600 1.000 61.92848  ? 415 ALA A CA    1 
ATOM   3289 C  C     . ALA A 1 415 ? 37.54200 -23.33900 -16.34200 1.000 63.47077  ? 415 ALA A C     1 
ATOM   3290 O  O     . ALA A 1 415 ? 38.10900 -22.36100 -15.84000 1.000 58.12802  ? 415 ALA A O     1 
ATOM   3291 C  CB    . ALA A 1 415 ? 38.91100 -25.22800 -17.24200 1.000 59.37817  ? 415 ALA A CB    1 
ATOM   3292 N  N     . HIS A 1 416 ? 36.46600 -23.20700 -17.11300 1.000 65.23414  ? 416 HIS A N     1 
ATOM   3293 C  CA    . HIS A 1 416 ? 35.98300 -21.89200 -17.51700 1.000 64.06031  ? 416 HIS A CA    1 
ATOM   3294 C  C     . HIS A 1 416 ? 34.89300 -21.34400 -16.60700 1.000 67.96078  ? 416 HIS A C     1 
ATOM   3295 O  O     . HIS A 1 416 ? 34.58600 -20.14800 -16.67600 1.000 73.42196  ? 416 HIS A O     1 
ATOM   3296 C  CB    . HIS A 1 416 ? 35.45900 -21.96200 -18.95300 1.000 62.45486  ? 416 HIS A CB    1 
ATOM   3297 C  CG    . HIS A 1 416 ? 36.53800 -22.09600 -19.98400 1.000 66.15793  ? 416 HIS A CG    1 
ATOM   3298 N  ND1   . HIS A 1 416 ? 37.10100 -21.01200 -20.62300 1.000 70.94272  ? 416 HIS A ND1   1 
ATOM   3299 C  CD2   . HIS A 1 416 ? 37.14600 -23.19200 -20.49700 1.000 64.22086  ? 416 HIS A CD2   1 
ATOM   3300 C  CE1   . HIS A 1 416 ? 38.01300 -21.43400 -21.48100 1.000 71.02694  ? 416 HIS A CE1   1 
ATOM   3301 N  NE2   . HIS A 1 416 ? 38.06100 -22.75300 -21.42300 1.000 67.85814  ? 416 HIS A NE2   1 
ATOM   3302 N  N     . GLY A 1 417 ? 34.29300 -22.19000 -15.77900 1.000 68.98722  ? 417 GLY A N     1 
ATOM   3303 C  CA    . GLY A 1 417 ? 33.13600 -21.82200 -14.99300 1.000 76.60392  ? 417 GLY A CA    1 
ATOM   3304 C  C     . GLY A 1 417 ? 31.89600 -22.18200 -15.78000 1.000 78.68575  ? 417 GLY A C     1 
ATOM   3305 O  O     . GLY A 1 417 ? 31.88400 -22.04500 -17.00600 1.000 77.66984  ? 417 GLY A O     1 
ATOM   3306 N  N     . LYS A 1 418 ? 30.85600 -22.65500 -15.09100 1.000 75.13532  ? 418 LYS A N     1 
ATOM   3307 C  CA    . LYS A 1 418 ? 29.66800 -23.14800 -15.78200 1.000 79.94116  ? 418 LYS A CA    1 
ATOM   3308 C  C     . LYS A 1 418 ? 28.95000 -22.07300 -16.59900 1.000 95.87992  ? 418 LYS A C     1 
ATOM   3309 O  O     . LYS A 1 418 ? 28.25300 -22.40500 -17.56500 1.000 99.53035  ? 418 LYS A O     1 
ATOM   3310 C  CB    . LYS A 1 418 ? 28.72000 -23.82900 -14.79700 1.000 80.49649  ? 418 LYS A CB    1 
ATOM   3311 C  CG    . LYS A 1 418 ? 29.35100 -25.08100 -14.21000 1.000 81.49398  ? 418 LYS A CG    1 
ATOM   3312 C  CD    . LYS A 1 418 ? 28.32000 -26.04700 -13.65400 1.000 90.01342  ? 418 LYS A CD    1 
ATOM   3313 C  CE    . LYS A 1 418 ? 28.99400 -27.22700 -12.96900 1.000 94.73767  ? 418 LYS A CE    1 
ATOM   3314 N  NZ    . LYS A 1 418 ? 27.99300 -28.17900 -12.41600 1.000 93.47173  ? 418 LYS A NZ    1 
ATOM   3315 N  N     . ASP A 1 419 ? 29.07000 -20.80000 -16.21400 1.000 102.39649 ? 419 ASP A N     1 
ATOM   3316 C  CA    . ASP A 1 419 ? 28.33000 -19.70800 -16.84300 1.000 102.37280 ? 419 ASP A CA    1 
ATOM   3317 C  C     . ASP A 1 419 ? 29.12500 -18.99700 -17.93500 1.000 101.02264 ? 419 ASP A C     1 
ATOM   3318 O  O     . ASP A 1 419 ? 28.73600 -17.90400 -18.36300 1.000 102.43860 ? 419 ASP A O     1 
ATOM   3319 C  CB    . ASP A 1 419 ? 27.88600 -18.68900 -15.79000 1.000 110.82645 ? 419 ASP A CB    1 
ATOM   3320 C  CG    . ASP A 1 419 ? 29.03500 -18.18800 -14.93800 1.000 117.06930 ? 419 ASP A CG    1 
ATOM   3321 O  OD1   . ASP A 1 419 ? 30.02500 -18.93100 -14.75800 1.000 111.11859 ? 419 ASP A OD1   1 
ATOM   3322 O  OD2   . ASP A 1 419 ? 28.93000 -17.05700 -14.42200 1.000 127.49950 ? 419 ASP A OD2   1 
ATOM   3323 N  N     . HIS A 1 420 ? 30.22800 -19.58300 -18.38400 1.000 87.49996  ? 420 HIS A N     1 
ATOM   3324 C  CA    . HIS A 1 420 ? 31.09700 -18.91400 -19.33800 1.000 83.68372  ? 420 HIS A CA    1 
ATOM   3325 C  C     . HIS A 1 420 ? 30.38800 -18.81400 -20.69100 1.000 84.96019  ? 420 HIS A C     1 
ATOM   3326 O  O     . HIS A 1 420 ? 29.67900 -19.74300 -21.09200 1.000 88.97383  ? 420 HIS A O     1 
ATOM   3327 C  CB    . HIS A 1 420 ? 32.42200 -19.66500 -19.47500 1.000 81.79928  ? 420 HIS A CB    1 
ATOM   3328 C  CG    . HIS A 1 420 ? 33.52300 -18.85100 -20.08500 1.000 77.87776  ? 420 HIS A CG    1 
ATOM   3329 N  ND1   . HIS A 1 420 ? 33.62100 -18.62000 -21.44000 1.000 79.11475  ? 420 HIS A ND1   1 
ATOM   3330 C  CD2   . HIS A 1 420 ? 34.58400 -18.22600 -19.52000 1.000 77.45139  ? 420 HIS A CD2   1 
ATOM   3331 C  CE1   . HIS A 1 420 ? 34.68800 -17.88000 -21.68300 1.000 76.10649  ? 420 HIS A CE1   1 
ATOM   3332 N  NE2   . HIS A 1 420 ? 35.29100 -17.62800 -20.53500 1.000 77.97514  ? 420 HIS A NE2   1 
ATOM   3333 N  N     . PRO A 1 421 ? 30.54900 -17.69800 -21.40700 1.000 80.03065  ? 421 PRO A N     1 
ATOM   3334 C  CA    . PRO A 1 421 ? 29.93800 -17.58000 -22.74500 1.000 79.82273  ? 421 PRO A CA    1 
ATOM   3335 C  C     . PRO A 1 421 ? 30.26400 -18.72000 -23.69800 1.000 84.04955  ? 421 PRO A C     1 
ATOM   3336 O  O     . PRO A 1 421 ? 29.39200 -19.12300 -24.48600 1.000 92.29528  ? 421 PRO A O     1 
ATOM   3337 C  CB    . PRO A 1 421 ? 30.51100 -16.25000 -23.25500 1.000 75.30903  ? 421 PRO A CB    1 
ATOM   3338 C  CG    . PRO A 1 421 ? 30.77000 -15.46300 -22.02400 1.000 69.22146  ? 421 PRO A CG    1 
ATOM   3339 C  CD    . PRO A 1 421 ? 31.20300 -16.45000 -20.98100 1.000 77.23821  ? 421 PRO A CD    1 
ATOM   3340 N  N     . TYR A 1 422 ? 31.49100 -19.24800 -23.65200 1.000 78.90683  ? 422 TYR A N     1 
ATOM   3341 C  CA    . TYR A 1 422 ? 31.85700 -20.35200 -24.53400 1.000 80.69125  ? 422 TYR A CA    1 
ATOM   3342 C  C     . TYR A 1 422 ? 30.90000 -21.52900 -24.36000 1.000 87.83422  ? 422 TYR A C     1 
ATOM   3343 O  O     . TYR A 1 422 ? 30.47500 -22.14900 -25.34600 1.000 96.37998  ? 422 TYR A O     1 
ATOM   3344 C  CB    . TYR A 1 422 ? 33.28100 -20.81800 -24.21700 1.000 77.49877  ? 422 TYR A CB    1 
ATOM   3345 C  CG    . TYR A 1 422 ? 34.43400 -19.93800 -24.67500 1.000 75.49063  ? 422 TYR A CG    1 
ATOM   3346 C  CD1   . TYR A 1 422 ? 34.27500 -18.96700 -25.65800 1.000 79.45953  ? 422 TYR A CD1   1 
ATOM   3347 C  CD2   . TYR A 1 422 ? 35.69700 -20.09100 -24.10900 1.000 73.20351  ? 422 TYR A CD2   1 
ATOM   3348 C  CE1   . TYR A 1 422 ? 35.35400 -18.17000 -26.06300 1.000 83.65214  ? 422 TYR A CE1   1 
ATOM   3349 C  CE2   . TYR A 1 422 ? 36.77200 -19.30600 -24.50500 1.000 80.45175  ? 422 TYR A CE2   1 
ATOM   3350 C  CZ    . TYR A 1 422 ? 36.60000 -18.34700 -25.48100 1.000 81.60452  ? 422 TYR A CZ    1 
ATOM   3351 O  OH    . TYR A 1 422 ? 37.67600 -17.57200 -25.87100 1.000 65.02885  ? 422 TYR A OH    1 
ATOM   3352 N  N     . ILE A 1 423 ? 30.53300 -21.83600 -23.11200 1.000 82.92310  ? 423 ILE A N     1 
ATOM   3353 C  CA    . ILE A 1 423 ? 29.66500 -22.97900 -22.83900 1.000 90.59244  ? 423 ILE A CA    1 
ATOM   3354 C  C     . ILE A 1 423 ? 28.25900 -22.73400 -23.37800 1.000 96.78002  ? 423 ILE A C     1 
ATOM   3355 O  O     . ILE A 1 423 ? 27.60100 -23.65100 -23.89000 1.000 98.59603  ? 423 ILE A O     1 
ATOM   3356 C  CB    . ILE A 1 423 ? 29.65600 -23.28200 -21.33000 1.000 88.90013  ? 423 ILE A CB    1 
ATOM   3357 C  CG1   . ILE A 1 423 ? 30.99900 -23.88100 -20.90400 1.000 78.12779  ? 423 ILE A CG1   1 
ATOM   3358 C  CG2   . ILE A 1 423 ? 28.49800 -24.20800 -20.96600 1.000 91.21357  ? 423 ILE A CG2   1 
ATOM   3359 C  CD1   . ILE A 1 423 ? 31.16700 -24.01600 -19.41100 1.000 78.25149  ? 423 ILE A CD1   1 
ATOM   3360 N  N     . SER A 1 424 ? 27.80000 -21.48200 -23.32200 1.000 92.18211  ? 424 SER A N     1 
ATOM   3361 C  CA    . SER A 1 424 ? 26.51000 -21.13400 -23.90500 1.000 91.11619  ? 424 SER A CA    1 
ATOM   3362 C  C     . SER A 1 424 ? 26.53100 -21.36400 -25.40500 1.000 94.29552  ? 424 SER A C     1 
ATOM   3363 O  O     . SER A 1 424 ? 25.60000 -21.95500 -25.97300 1.000 106.29432 ? 424 SER A O     1 
ATOM   3364 C  CB    . SER A 1 424 ? 26.16900 -19.68100 -23.58900 1.000 94.17971  ? 424 SER A CB    1 
ATOM   3365 O  OG    . SER A 1 424 ? 26.06300 -19.48500 -22.19200 1.000 103.43872 ? 424 SER A OG    1 
ATOM   3366 N  N     . GLU A 1 425 ? 27.61100 -20.92500 -26.05400 1.000 97.22745  ? 425 GLU A N     1 
ATOM   3367 C  CA    . GLU A 1 425 ? 27.74900 -21.12400 -27.49100 1.000 97.66171  ? 425 GLU A CA    1 
ATOM   3368 C  C     . GLU A 1 425 ? 27.71000 -22.60700 -27.83900 1.000 99.43034  ? 425 GLU A C     1 
ATOM   3369 O  O     . GLU A 1 425 ? 27.03200 -23.02000 -28.79100 1.000 103.00972 ? 425 GLU A O     1 
ATOM   3370 C  CB    . GLU A 1 425 ? 29.10000 -20.54500 -27.91400 1.000 103.16500 ? 425 GLU A CB    1 
ATOM   3371 C  CG    . GLU A 1 425 ? 29.21800 -19.03400 -27.88300 1.000 108.68935 ? 425 GLU A CG    1 
ATOM   3372 C  CD    . GLU A 1 425 ? 30.50100 -18.54000 -28.53800 1.000 114.22685 ? 425 GLU A CD    1 
ATOM   3373 O  OE1   . GLU A 1 425 ? 31.25700 -19.37300 -29.08700 1.000 103.13079 ? 425 GLU A OE1   1 
ATOM   3374 O  OE2   . GLU A 1 425 ? 30.76900 -17.32000 -28.48100 1.000 125.09658 ? 425 GLU A OE2   1 
ATOM   3375 N  N     . ILE A 1 426 ? 28.40900 -23.43000 -27.05300 1.000 100.43836 ? 426 ILE A N     1 
ATOM   3376 C  CA    . ILE A 1 426 ? 28.48300 -24.85500 -27.37000 1.000 99.29085  ? 426 ILE A CA    1 
ATOM   3377 C  C     . ILE A 1 426 ? 27.12600 -25.53100 -27.17000 1.000 96.54052  ? 426 ILE A C     1 
ATOM   3378 O  O     . ILE A 1 426 ? 26.72700 -26.41200 -27.95000 1.000 97.24587  ? 426 ILE A O     1 
ATOM   3379 C  CB    . ILE A 1 426 ? 29.58400 -25.52600 -26.52900 1.000 89.90552  ? 426 ILE A CB    1 
ATOM   3380 C  CG1   . ILE A 1 426 ? 30.95300 -24.93700 -26.87200 1.000 85.80239  ? 426 ILE A CG1   1 
ATOM   3381 C  CG2   . ILE A 1 426 ? 29.60900 -27.01600 -26.79200 1.000 79.28582  ? 426 ILE A CG2   1 
ATOM   3382 C  CD1   . ILE A 1 426 ? 31.98900 -25.13100 -25.78400 1.000 79.22529  ? 426 ILE A CD1   1 
ATOM   3383 N  N     . LYS A 1 427 ? 26.39000 -25.13400 -26.12400 1.000 95.79043  ? 427 LYS A N     1 
ATOM   3384 C  CA    . LYS A 1 427 ? 25.06500 -25.71300 -25.92400 1.000 94.66661  ? 427 LYS A CA    1 
ATOM   3385 C  C     . LYS A 1 427 ? 24.13300 -25.33200 -27.06800 1.000 104.57306 ? 427 LYS A C     1 
ATOM   3386 O  O     . LYS A 1 427 ? 23.28600 -26.13600 -27.49900 1.000 112.75826 ? 427 LYS A O     1 
ATOM   3387 C  CB    . LYS A 1 427 ? 24.51200 -25.23600 -24.58300 1.000 89.56863  ? 427 LYS A CB    1 
ATOM   3388 C  CG    . LYS A 1 427 ? 25.09100 -25.97100 -23.38100 1.000 89.09752  ? 427 LYS A CG    1 
ATOM   3389 C  CD    . LYS A 1 427 ? 24.47300 -25.48200 -22.08100 1.000 91.61625  ? 427 LYS A CD    1 
ATOM   3390 C  CE    . LYS A 1 427 ? 25.20900 -26.02800 -20.86500 1.000 86.76303  ? 427 LYS A CE    1 
ATOM   3391 N  NZ    . LYS A 1 427 ? 25.04300 -27.49900 -20.70500 1.000 80.60966  ? 427 LYS A NZ    1 
ATOM   3392 N  N     . GLN A 1 428 ? 24.28900 -24.10800 -27.58900 1.000 103.47820 ? 428 GLN A N     1 
ATOM   3393 C  CA    . GLN A 1 428 ? 23.54500 -23.74000 -28.78800 1.000 110.27901 ? 428 GLN A CA    1 
ATOM   3394 C  C     . GLN A 1 428 ? 23.92400 -24.65100 -29.94200 1.000 114.61111 ? 428 GLN A C     1 
ATOM   3395 O  O     . GLN A 1 428 ? 23.07700 -25.00500 -30.76700 1.000 118.01941 ? 428 GLN A O     1 
ATOM   3396 C  CB    . GLN A 1 428 ? 23.74100 -22.26600 -29.13500 1.000 107.34182 ? 428 GLN A CB    1 
ATOM   3397 C  CG    . GLN A 1 428 ? 23.24600 -21.33400 -28.04200 1.000 110.56062 ? 428 GLN A CG    1 
ATOM   3398 C  CD    . GLN A 1 428 ? 21.90100 -21.77700 -27.47000 1.000 115.44805 ? 428 GLN A CD    1 
ATOM   3399 O  OE1   . GLN A 1 428 ? 21.76600 -21.97700 -26.26200 1.000 117.95888 ? 428 GLN A OE1   1 
ATOM   3400 N  NE2   . GLN A 1 428 ? 20.90100 -21.93100 -28.33900 1.000 110.60800 ? 428 GLN A NE2   1 
ATOM   3401 N  N     . GLU A 1 429 ? 25.20800 -25.00700 -30.03900 1.000 112.57666 ? 429 GLU A N     1 
ATOM   3402 C  CA    . GLU A 1 429 ? 25.61400 -25.84400 -31.16000 1.000 113.77417 ? 429 GLU A CA    1 
ATOM   3403 C  C     . GLU A 1 429 ? 25.08700 -27.26600 -31.02100 1.000 117.45619 ? 429 GLU A C     1 
ATOM   3404 O  O     . GLU A 1 429 ? 24.98600 -27.97700 -32.02600 1.000 118.69844 ? 429 GLU A O     1 
ATOM   3405 C  CB    . GLU A 1 429 ? 27.14100 -25.88900 -31.28400 1.000 110.65800 ? 429 GLU A CB    1 
ATOM   3406 C  CG    . GLU A 1 429 ? 27.80500 -24.55800 -31.58900 1.000 117.83518 ? 429 GLU A CG    1 
ATOM   3407 C  CD    . GLU A 1 429 ? 29.32500 -24.64400 -31.56700 1.000 107.47604 ? 429 GLU A CD    1 
ATOM   3408 O  OE1   . GLU A 1 429 ? 29.86900 -25.73500 -31.84900 1.000 105.48107 ? 429 GLU A OE1   1 
ATOM   3409 O  OE2   . GLU A 1 429 ? 29.97800 -23.61700 -31.27800 1.000 101.80168 ? 429 GLU A OE2   1 
ATOM   3410 N  N     . ILE A 1 430 ? 24.75000 -27.69000 -29.80100 1.000 113.08724 ? 430 ILE A N     1 
ATOM   3411 C  CA    . ILE A 1 430 ? 24.09000 -28.98600 -29.62400 1.000 111.46336 ? 430 ILE A CA    1 
ATOM   3412 C  C     . ILE A 1 430 ? 22.60900 -28.92000 -30.01100 1.000 130.67093 ? 430 ILE A C     1 
ATOM   3413 O  O     . ILE A 1 430 ? 22.09400 -29.82300 -30.68200 1.000 134.31610 ? 430 ILE A O     1 
ATOM   3414 C  CB    . ILE A 1 430 ? 24.28900 -29.50000 -28.18900 1.000 102.73074 ? 430 ILE A CB    1 
ATOM   3415 C  CG1   . ILE A 1 430 ? 25.77900 -29.70900 -27.91500 1.000 89.96868  ? 430 ILE A CG1   1 
ATOM   3416 C  CG2   . ILE A 1 430 ? 23.55200 -30.80600 -27.99000 1.000 109.38154 ? 430 ILE A CG2   1 
ATOM   3417 C  CD1   . ILE A 1 430 ? 26.11000 -29.94700 -26.46100 1.000 81.05446  ? 430 ILE A CD1   1 
ATOM   3418 N  N     . GLU A 1 431 ? 21.90200 -27.85900 -29.59500 1.000 134.52666 ? 431 GLU A N     1 
ATOM   3419 C  CA    . GLU A 1 431 ? 20.46700 -27.71300 -29.89900 1.000 137.30594 ? 431 GLU A CA    1 
ATOM   3420 C  C     . GLU A 1 431 ? 20.15600 -27.29600 -31.33100 1.000 142.48814 ? 431 GLU A C     1 
ATOM   3421 O  O     . GLU A 1 431 ? 19.06900 -27.62000 -31.82600 1.000 148.02301 ? 431 GLU A O     1 
ATOM   3422 C  CB    . GLU A 1 431 ? 19.74300 -26.79300 -28.91400 1.000 134.75563 ? 431 GLU A CB    1 
ATOM   3423 C  CG    . GLU A 1 431 ? 20.11300 -27.03100 -27.49700 1.000 139.74833 ? 431 GLU A CG    1 
ATOM   3424 C  CD    . GLU A 1 431 ? 19.68700 -28.44500 -27.11600 1.000 147.69402 ? 431 GLU A CD    1 
ATOM   3425 O  OE1   . GLU A 1 431 ? 18.54600 -28.83000 -27.48000 1.000 148.61782 ? 431 GLU A OE1   1 
ATOM   3426 O  OE2   . GLU A 1 431 ? 20.47300 -29.17300 -26.48100 1.000 150.12326 ? 431 GLU A OE2   1 
ATOM   3427 N  N     . SER A 1 432 ? 21.05800 -26.58800 -32.01200 1.000 143.73039 ? 432 SER A N     1 
ATOM   3428 C  CA    . SER A 1 432 ? 20.74400 -26.08500 -33.34700 1.000 148.54676 ? 432 SER A CA    1 
ATOM   3429 C  C     . SER A 1 432 ? 20.50000 -27.23400 -34.31400 1.000 162.49843 ? 432 SER A C     1 
ATOM   3430 O  O     . SER A 1 432 ? 19.38400 -27.40800 -34.81900 1.000 161.75097 ? 432 SER A O     1 
ATOM   3431 C  CB    . SER A 1 432 ? 21.89100 -25.20200 -33.85200 1.000 145.58324 ? 432 SER A CB    1 
ATOM   3432 O  OG    . SER A 1 432 ? 23.11300 -25.92600 -33.92300 1.000 147.70192 ? 432 SER A OG    1 
HETATM 3433 N  N     . SAH B 2 .   ? 58.53200 -16.86500 -8.53500  1.000 77.05398  ? 501 SAH A N     1 
HETATM 3434 C  CA    . SAH B 2 .   ? 58.24300 -15.69200 -9.35000  1.000 75.48273  ? 501 SAH A CA    1 
HETATM 3435 C  CB    . SAH B 2 .   ? 56.79900 -15.72600 -9.83600  1.000 61.44684  ? 501 SAH A CB    1 
HETATM 3436 C  CG    . SAH B 2 .   ? 56.55600 -16.51000 -11.12600 1.000 71.77440  ? 501 SAH A CG    1 
HETATM 3437 S  SD    . SAH B 2 .   ? 57.15900 -15.69300 -12.62500 1.000 73.89307  ? 501 SAH A SD    1 
HETATM 3438 C  C     . SAH B 2 .   ? 58.50600 -14.40500 -8.56600  1.000 81.46766  ? 501 SAH A C     1 
HETATM 3439 O  O     . SAH B 2 .   ? 58.99000 -14.44200 -7.43000  1.000 82.90994  ? 501 SAH A O     1 
HETATM 3440 O  OXT   . SAH B 2 .   ? 58.26300 -13.30100 -9.05900  1.000 82.98890  ? 501 SAH A OXT   1 
HETATM 3441 C  "C5'" . SAH B 2 .   ? 58.15300 -17.11100 -13.20300 1.000 79.48321  ? 501 SAH A "C5'" 1 
HETATM 3442 C  "C4'" . SAH B 2 .   ? 59.46100 -17.38900 -12.45400 1.000 71.55595  ? 501 SAH A "C4'" 1 
HETATM 3443 O  "O4'" . SAH B 2 .   ? 59.23100 -18.04500 -11.21800 1.000 66.27110  ? 501 SAH A "O4'" 1 
HETATM 3444 C  "C3'" . SAH B 2 .   ? 60.36800 -18.34700 -13.21300 1.000 73.11929  ? 501 SAH A "C3'" 1 
HETATM 3445 O  "O3'" . SAH B 2 .   ? 61.17800 -17.65200 -14.13100 1.000 71.16380  ? 501 SAH A "O3'" 1 
HETATM 3446 C  "C2'" . SAH B 2 .   ? 61.16500 -19.02300 -12.11700 1.000 71.91389  ? 501 SAH A "C2'" 1 
HETATM 3447 O  "O2'" . SAH B 2 .   ? 62.25600 -18.21000 -11.74300 1.000 68.66613  ? 501 SAH A "O2'" 1 
HETATM 3448 C  "C1'" . SAH B 2 .   ? 60.19200 -19.05400 -10.95800 1.000 63.97083  ? 501 SAH A "C1'" 1 
HETATM 3449 N  N9    . SAH B 2 .   ? 59.52200 -20.37200 -10.85600 1.000 64.59195  ? 501 SAH A N9    1 
HETATM 3450 C  C8    . SAH B 2 .   ? 58.25700 -20.66600 -11.29700 1.000 62.89701  ? 501 SAH A C8    1 
HETATM 3451 N  N7    . SAH B 2 .   ? 57.98800 -21.96600 -11.03500 1.000 63.14441  ? 501 SAH A N7    1 
HETATM 3452 C  C5    . SAH B 2 .   ? 59.05900 -22.51300 -10.42500 1.000 62.53645  ? 501 SAH A C5    1 
HETATM 3453 C  C6    . SAH B 2 .   ? 59.30600 -23.79600 -9.94800  1.000 67.51073  ? 501 SAH A C6    1 
HETATM 3454 N  N6    . SAH B 2 .   ? 58.38400 -24.75000 -10.05700 1.000 73.10350  ? 501 SAH A N6    1 
HETATM 3455 N  N1    . SAH B 2 .   ? 60.51800 -24.07900 -9.35900  1.000 69.64519  ? 501 SAH A N1    1 
HETATM 3456 C  C2    . SAH B 2 .   ? 61.46800 -23.08500 -9.25200  1.000 76.73025  ? 501 SAH A C2    1 
HETATM 3457 N  N3    . SAH B 2 .   ? 61.21700 -21.81300 -9.72800  1.000 66.42112  ? 501 SAH A N3    1 
HETATM 3458 C  C4    . SAH B 2 .   ? 60.03100 -21.52700 -10.30900 1.000 63.10757  ? 501 SAH A C4    1 
HETATM 3459 ZN ZN    . ZN  C 3 .   ? 43.57800 3.19000   -36.62800 1.000 87.72631  2 502 ZN  A ZN    1 
HETATM 3460 ZN ZN    . ZN  D 3 .   ? 57.56200 -30.57700 -12.97500 1.000 74.86161  2 503 ZN  A ZN    1 
HETATM 3461 ZN ZN    . ZN  E 3 .   ? 34.49800 -4.43200  -28.01700 0.850 79.15686  2 504 ZN  A ZN    1 
HETATM 3462 C  C1    . PEG F 4 .   ? 51.91600 -19.45400 -41.39200 1.000 78.50000  ? 505 PEG A C1    1 
HETATM 3463 O  O1    . PEG F 4 .   ? 53.16600 -19.80600 -40.83000 1.000 77.45000  ? 505 PEG A O1    1 
HETATM 3464 C  C2    . PEG F 4 .   ? 51.70700 -20.11300 -42.72000 1.000 80.28000  ? 505 PEG A C2    1 
HETATM 3465 O  O2    . PEG F 4 .   ? 50.45200 -20.76900 -42.69800 1.000 94.13000  ? 505 PEG A O2    1 
HETATM 3466 C  C3    . PEG F 4 .   ? 50.19600 -21.57400 -43.84000 1.000 85.87000  ? 505 PEG A C3    1 
HETATM 3467 C  C4    . PEG F 4 .   ? 49.51600 -22.82800 -43.38400 1.000 76.62000  ? 505 PEG A C4    1 
HETATM 3468 O  O4    . PEG F 4 .   ? 50.18200 -23.38900 -42.26700 1.000 68.77000  ? 505 PEG A O4    1 
HETATM 3469 C  C1    . PEG G 4 .   ? 47.39400 -27.90000 -35.17900 1.000 86.36000  ? 506 PEG A C1    1 
HETATM 3470 O  O1    . PEG G 4 .   ? 47.77300 -26.76600 -35.94400 1.000 79.73000  ? 506 PEG A O1    1 
HETATM 3471 C  C2    . PEG G 4 .   ? 45.90300 -28.00800 -35.06100 1.000 80.90000  ? 506 PEG A C2    1 
HETATM 3472 O  O2    . PEG G 4 .   ? 45.40700 -26.83400 -34.44000 1.000 90.92000  ? 506 PEG A O2    1 
HETATM 3473 C  C3    . PEG G 4 .   ? 44.26500 -26.28900 -35.08700 1.000 87.46000  ? 506 PEG A C3    1 
HETATM 3474 C  C4    . PEG G 4 .   ? 43.77300 -25.11100 -34.30100 1.000 86.40000  ? 506 PEG A C4    1 
HETATM 3475 O  O4    . PEG G 4 .   ? 42.57700 -24.59600 -34.85500 1.000 72.70000  ? 506 PEG A O4    1 
HETATM 3476 O  O1    . PG4 H 5 .   ? 41.10000 -24.84900 -37.77700 1.000 20.00000  ? 507 PG4 A O1    1 
HETATM 3477 C  C1    . PG4 H 5 .   ? 39.71600 -25.11500 -37.89200 1.000 20.00000  ? 507 PG4 A C1    1 
HETATM 3478 C  C2    . PG4 H 5 .   ? 39.24500 -25.04900 -39.31000 1.000 20.00000  ? 507 PG4 A C2    1 
HETATM 3479 O  O2    . PG4 H 5 .   ? 37.83700 -24.84800 -39.34500 1.000 20.00000  ? 507 PG4 A O2    1 
HETATM 3480 C  C3    . PG4 H 5 .   ? 37.11300 -25.90400 -38.72000 1.000 20.00000  ? 507 PG4 A C3    1 
HETATM 3481 C  C4    . PG4 H 5 .   ? 35.66300 -25.80300 -39.07800 1.000 20.00000  ? 507 PG4 A C4    1 
HETATM 3482 O  O3    . PG4 H 5 .   ? 35.11800 -27.10300 -39.27600 1.000 20.00000  ? 507 PG4 A O3    1 
HETATM 3483 C  C5    . PG4 H 5 .   ? 34.03600 -27.10900 -40.20000 1.000 20.00000  ? 507 PG4 A C5    1 
HETATM 3484 C  C6    . PG4 H 5 .   ? 33.76300 -28.50500 -40.66500 1.000 20.00000  ? 507 PG4 A C6    1 
HETATM 3485 O  O4    . PG4 H 5 .   ? 33.12100 -28.46800 -41.93500 1.000 20.00000  ? 507 PG4 A O4    1 
HETATM 3486 C  C7    . PG4 H 5 .   ? 32.54900 -27.19800 -42.23100 1.000 20.00000  ? 507 PG4 A C7    1 
HETATM 3487 C  C8    . PG4 H 5 .   ? 31.77400 -27.26600 -43.51400 1.000 20.00000  ? 507 PG4 A C8    1 
HETATM 3488 O  O5    . PG4 H 5 .   ? 31.16500 -26.02800 -43.85100 1.000 20.00000  ? 507 PG4 A O5    1 
HETATM 3489 C  C1    . EOH I 6 .   ? 51.44400 -21.93200 -23.49800 1.000 61.29000  ? 508 EOH A C1    1 
HETATM 3490 C  C2    . EOH I 6 .   ? 51.37700 -20.89100 -22.38600 1.000 48.98000  ? 508 EOH A C2    1 
HETATM 3491 O  O     . EOH I 6 .   ? 51.02000 -21.40600 -24.73600 1.000 58.04000  ? 508 EOH A O     1 
HETATM 3492 C  C1    . GOL J 7 .   ? 39.14900 8.49000   -32.40400 1.000 20.00000  ? 509 GOL A C1    1 
HETATM 3493 O  O1    . GOL J 7 .   ? 37.79000 8.43100   -32.78300 1.000 20.00000  ? 509 GOL A O1    1 
HETATM 3494 C  C2    . GOL J 7 .   ? 39.31000 9.00000   -30.98900 1.000 20.00000  ? 509 GOL A C2    1 
HETATM 3495 O  O2    . GOL J 7 .   ? 40.06500 10.19500  -30.99200 1.000 20.00000  ? 509 GOL A O2    1 
HETATM 3496 C  C3    . GOL J 7 .   ? 38.02100 9.25600   -30.25100 1.000 20.00000  ? 509 GOL A C3    1 
HETATM 3497 O  O3    . GOL J 7 .   ? 37.97200 8.49600   -29.03500 1.000 20.00000  ? 509 GOL A O3    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   ? 1.56180 1.47080 1.28800 -0.21870 0.15160  -0.20790 5   GLY A N     
2    C  CA    . GLY A 5   ? 1.47360 1.41280 1.22420 -0.21670 0.13520  -0.17990 5   GLY A CA    
3    C  C     . GLY A 5   ? 1.45770 1.43820 1.24090 -0.20760 0.15420  -0.17670 5   GLY A C     
4    O  O     . GLY A 5   ? 1.46910 1.46830 1.29110 -0.18920 0.17640  -0.19060 5   GLY A O     
5    N  N     . LEU A 6   ? 1.36290 1.35740 1.13100 -0.22090 0.14450  -0.15820 6   LEU A N     
6    C  CA    . LEU A 6   ? 1.22450 1.25690 1.01770 -0.21890 0.15880  -0.15270 6   LEU A CA    
7    C  C     . LEU A 6   ? 1.17170 1.20230 0.91200 -0.24520 0.17410  -0.15760 6   LEU A C     
8    O  O     . LEU A 6   ? 1.19890 1.20260 0.88620 -0.26540 0.15750  -0.14700 6   LEU A O     
9    C  CB    . LEU A 6   ? 1.13650 1.18390 0.95810 -0.21250 0.13520  -0.12580 6   LEU A CB    
10   C  CG    . LEU A 6   ? 1.13380 1.18660 1.00690 -0.18830 0.12100  -0.11770 6   LEU A CG    
11   C  CD1   . LEU A 6   ? 1.01190 1.06820 0.89430 -0.18780 0.09590  -0.09230 6   LEU A CD1   
12   C  CD2   . LEU A 6   ? 1.10180 1.18780 1.02820 -0.16790 0.13960  -0.12630 6   LEU A CD2   
13   N  N     . GLY A 7   ? 1.11610 1.17550 0.87110 -0.24530 0.20560  -0.17310 7   GLY A N     
14   C  CA    . GLY A 7   ? 1.16520 1.22310 0.86800 -0.27270 0.22520  -0.17970 7   GLY A CA    
15   C  C     . GLY A 7   ? 1.04870 1.10450 0.72720 -0.29110 0.20730  -0.15380 7   GLY A C     
16   O  O     . GLY A 7   ? 1.05080 1.12950 0.77150 -0.28120 0.19610  -0.13760 7   GLY A O     
17   N  N     . GLY A 8   ? 1.07090 1.09550 0.67740 -0.31840 0.20440  -0.15000 8   GLY A N     
18   C  CA    . GLY A 8   ? 1.00400 1.01790 0.57900 -0.33710 0.18860  -0.12570 8   GLY A CA    
19   C  C     . GLY A 8   ? 1.09790 1.09000 0.67580 -0.32830 0.14880  -0.10130 8   GLY A C     
20   O  O     . GLY A 8   ? 1.14130 1.12460 0.70390 -0.33780 0.13410  -0.08010 8   GLY A O     
21   N  N     . LEU A 9   ? 1.17250 1.15460 0.76980 -0.31100 0.13200  -0.10430 9   LEU A N     
22   C  CA    . LEU A 9   ? 1.03580 1.00410 0.64520 -0.30070 0.09670  -0.08360 9   LEU A CA    
23   C  C     . LEU A 9   ? 1.01770 0.95900 0.60210 -0.30220 0.08140  -0.09050 9   LEU A C     
24   O  O     . LEU A 9   ? 1.10940 1.04510 0.68240 -0.30420 0.09910  -0.11340 9   LEU A O     
25   C  CB    . LEU A 9   ? 0.98980 0.98630 0.67080 -0.27470 0.09190  -0.07740 9   LEU A CB    
26   C  CG    . LEU A 9   ? 0.99510 1.02210 0.70710 -0.27260 0.10510  -0.07200 9   LEU A CG    
27   C  CD1   . LEU A 9   ? 1.03430 1.09060 0.81390 -0.24680 0.10570  -0.07360 9   LEU A CD1   
28   C  CD2   . LEU A 9   ? 0.92090 0.93330 0.61120 -0.28260 0.08620  -0.04890 9   LEU A CD2   
29   N  N     . GLU A 10  ? 1.20560 1.13010 0.78190 -0.30180 0.04840  -0.07170 10  GLU A N     
30   C  CA    . GLU A 10  ? 1.22520 1.12880 0.78410 -0.30460 0.03000  -0.07680 10  GLU A CA    
31   C  C     . GLU A 10  ? 1.18970 1.09660 0.78290 -0.29140 -0.00200 -0.05700 10  GLU A C     
32   O  O     . GLU A 10  ? 1.17280 1.08310 0.77210 -0.28830 -0.01670 -0.03600 10  GLU A O     
33   C  CB    . GLU A 10  ? 1.29040 1.16300 0.77090 -0.33160 0.02220  -0.07650 10  GLU A CB    
34   C  CG    . GLU A 10  ? 1.50110 1.34980 0.94990 -0.34160 0.00320  -0.08410 10  GLU A CG    
35   C  CD    . GLU A 10  ? 1.65500 1.47310 1.01960 -0.37020 -0.00420 -0.08270 10  GLU A CD    
36   O  OE1   . GLU A 10  ? 1.61720 1.43170 0.94750 -0.38260 0.01230  -0.07920 10  GLU A OE1   
37   O  OE2   . GLU A 10  ? 1.72450 1.52170 1.05510 -0.38210 -0.02680 -0.08480 10  GLU A OE2   
38   N  N     . ARG A 11  ? 1.11350 1.01820 0.72870 -0.28450 -0.01140 -0.06440 11  ARG A N     
39   C  CA    . ARG A 11  ? 1.06520 0.97340 0.70690 -0.27710 -0.04200 -0.04730 11  ARG A CA    
40   C  C     . ARG A 11  ? 1.10380 0.99110 0.69560 -0.29540 -0.06980 -0.03770 11  ARG A C     
41   O  O     . ARG A 11  ? 1.20240 1.06790 0.74240 -0.31440 -0.06780 -0.05130 11  ARG A O     
42   C  CB    . ARG A 11  ? 1.01270 0.92520 0.69390 -0.26690 -0.04170 -0.05800 11  ARG A CB    
43   C  CG    . ARG A 11  ? 0.93460 0.85230 0.64050 -0.26440 -0.07170 -0.04350 11  ARG A CG    
44   C  CD    . ARG A 11  ? 0.94550 0.86790 0.69420 -0.25480 -0.06730 -0.05210 11  ARG A CD    
45   N  NE    . ARG A 11  ? 1.07360 0.99390 0.82910 -0.26340 -0.09350 -0.04700 11  ARG A NE    
46   C  CZ    . ARG A 11  ? 1.16480 1.08580 0.95320 -0.26040 -0.09450 -0.05180 11  ARG A CZ    
47   N  NH1   . ARG A 11  ? 1.04490 0.96480 0.86070 -0.24700 -0.07240 -0.06080 11  ARG A NH1   
48   N  NH2   . ARG A 11  ? 1.18720 1.11040 0.98190 -0.27190 -0.11930 -0.04660 11  ARG A NH2   
49   N  N     . PHE A 12  ? 1.04080 0.93430 0.64680 -0.28950 -0.09620 -0.01450 12  PHE A N     
50   C  CA    . PHE A 12  ? 1.10400 0.97980 0.66630 -0.30450 -0.12670 -0.00250 12  PHE A CA    
51   C  C     . PHE A 12  ? 1.07470 0.96810 0.68190 -0.29040 -0.15640 0.01780  12  PHE A C     
52   O  O     . PHE A 12  ? 1.04350 0.95950 0.70830 -0.27090 -0.15030 0.02210  12  PHE A O     
53   C  CB    . PHE A 12  ? 1.18200 1.03700 0.68720 -0.31760 -0.12500 0.00730  12  PHE A CB    
54   C  CG    . PHE A 12  ? 1.14380 1.00410 0.67060 -0.30390 -0.13350 0.03010  12  PHE A CG    
55   C  CD1   . PHE A 12  ? 1.09140 0.97100 0.66430 -0.28740 -0.11230 0.02910  12  PHE A CD1   
56   C  CD2   . PHE A 12  ? 1.14520 0.98900 0.64480 -0.30730 -0.16370 0.05240  12  PHE A CD2   
57   C  CE1   . PHE A 12  ? 1.02330 0.90320 0.61200 -0.27610 -0.11940 0.04770  12  PHE A CE1   
58   C  CE2   . PHE A 12  ? 0.96360 0.80650 0.48190 -0.29330 -0.17060 0.07200  12  PHE A CE2   
59   C  CZ    . PHE A 12  ? 0.97580 0.83560 0.53730 -0.27850 -0.14750 0.06860  12  PHE A CZ    
60   N  N     . CYS A 13  ? 1.09560 0.97990 0.67630 -0.30070 -0.18880 0.02970  13  CYS A N     
61   C  CA    . CYS A 13  ? 1.08590 0.99040 0.71050 -0.28720 -0.21870 0.04920  13  CYS A CA    
62   C  C     . CYS A 13  ? 1.09500 0.99080 0.70930 -0.27780 -0.23010 0.07190  13  CYS A C     
63   O  O     . CYS A 13  ? 1.20910 1.07990 0.76770 -0.29100 -0.24750 0.08230  13  CYS A O     
64   C  CB    . CYS A 13  ? 1.12860 1.03410 0.74050 -0.30170 -0.25090 0.05010  13  CYS A CB    
65   S  SG    . CYS A 13  ? 1.52770 1.47570 1.22420 -0.28480 -0.27230 0.06030  13  CYS A SG    
66   N  N     . SER A 14  ? 1.05530 0.96800 0.71970 -0.25570 -0.22100 0.07980  14  SER A N     
67   C  CA    . SER A 14  ? 1.05940 0.96000 0.71860 -0.24450 -0.22890 0.09940  14  SER A CA    
68   C  C     . SER A 14  ? 1.15790 1.07310 0.85200 -0.22960 -0.26250 0.11810  14  SER A C     
69   O  O     . SER A 14  ? 1.19370 1.14170 0.95080 -0.21410 -0.26290 0.11670  14  SER A O     
70   C  CB    . SER A 14  ? 1.02500 0.93390 0.71690 -0.22950 -0.20130 0.09630  14  SER A CB    
71   O  OG    . SER A 14  ? 1.05630 0.94730 0.73890 -0.22030 -0.20820 0.11370  14  SER A OG    
72   N  N     . PRO A 15  ? 1.16760 1.06070 0.82280 -0.23420 -0.29150 0.13610  15  PRO A N     
73   C  CA    . PRO A 15  ? 1.13830 1.04790 0.82820 -0.21900 -0.32720 0.15470  15  PRO A CA    
74   C  C     . PRO A 15  ? 1.06170 0.99190 0.81710 -0.18920 -0.32110 0.16200  15  PRO A C     
75   O  O     . PRO A 15  ? 1.10300 1.01200 0.85010 -0.17920 -0.30640 0.16710  15  PRO A O     
76   C  CB    . PRO A 15  ? 1.32290 1.19350 0.94840 -0.22780 -0.35300 0.17400  15  PRO A CB    
77   C  CG    . PRO A 15  ? 1.28770 1.12830 0.83980 -0.25680 -0.33490 0.16110  15  PRO A CG    
78   C  CD    . PRO A 15  ? 1.21360 1.06540 0.78860 -0.25520 -0.29200 0.14000  15  PRO A CD    
79   N  N     . GLY A 16  ? 1.09060 1.06220 0.91010 -0.17690 -0.33140 0.16160  16  GLY A N     
80   C  CA    . GLY A 16  ? 1.08690 1.08480 0.97310 -0.14950 -0.32440 0.16590  16  GLY A CA    
81   C  C     . GLY A 16  ? 1.03460 1.04490 0.94830 -0.14530 -0.28710 0.14970  16  GLY A C     
82   O  O     . GLY A 16  ? 1.00130 1.03370 0.96730 -0.12450 -0.27790 0.15120  16  GLY A O     
83   N  N     . LYS A 17  ? 1.05020 1.04790 0.93050 -0.16390 -0.26570 0.13410  17  LYS A N     
84   C  CA    . LYS A 17  ? 0.92980 0.93780 0.83260 -0.16040 -0.23290 0.11990  17  LYS A CA    
85   C  C     . LYS A 17  ? 0.89480 0.91640 0.80300 -0.17530 -0.22330 0.10360  17  LYS A C     
86   O  O     . LYS A 17  ? 0.96800 0.99570 0.89160 -0.17320 -0.19770 0.09230  17  LYS A O     
87   C  CB    . LYS A 17  ? 0.96460 0.94290 0.82810 -0.16360 -0.21120 0.11690  17  LYS A CB    
88   C  CG    . LYS A 17  ? 0.95970 0.91660 0.81410 -0.15030 -0.22010 0.13270  17  LYS A CG    
89   C  CD    . LYS A 17  ? 1.01820 0.93590 0.81170 -0.16430 -0.21230 0.13460  17  LYS A CD    
90   C  CE    . LYS A 17  ? 1.08260 0.97440 0.87020 -0.15020 -0.22030 0.15020  17  LYS A CE    
91   N  NZ    . LYS A 17  ? 1.07760 0.92590 0.79910 -0.16580 -0.23090 0.16140  17  LYS A NZ    
92   N  N     . GLY A 18  ? 0.96720 0.99150 0.86240 -0.19040 -0.24430 0.10230  18  GLY A N     
93   C  CA    . GLY A 18  ? 1.04350 1.07170 0.93730 -0.20590 -0.23370 0.08480  18  GLY A CA    
94   C  C     . GLY A 18  ? 0.99760 0.99580 0.83810 -0.21950 -0.21310 0.07090  18  GLY A C     
95   O  O     . GLY A 18  ? 1.03980 1.01320 0.82670 -0.23140 -0.22120 0.07350  18  GLY A O     
96   N  N     . ARG A 19  ? 0.95950 0.96040 0.81350 -0.21900 -0.18690 0.05590  19  ARG A N     
97   C  CA    . ARG A 19  ? 0.92390 0.90240 0.73610 -0.22940 -0.16470 0.04070  19  ARG A CA    
98   C  C     . ARG A 19  ? 0.93440 0.91130 0.74810 -0.21810 -0.14370 0.04360  19  ARG A C     
99   O  O     . ARG A 19  ? 0.91830 0.91230 0.77310 -0.20130 -0.13850 0.05080  19  ARG A O     
100  C  CB    . ARG A 19  ? 0.90190 0.88190 0.72850 -0.23370 -0.14900 0.02250  19  ARG A CB    
101  C  CG    . ARG A 19  ? 0.97040 0.94850 0.79260 -0.24890 -0.16880 0.01730  19  ARG A CG    
102  C  CD    . ARG A 19  ? 0.98680 0.96800 0.83930 -0.24800 -0.15460 0.00440  19  ARG A CD    
103  N  NE    . ARG A 19  ? 1.00010 1.00780 0.90980 -0.23030 -0.15090 0.01580  19  ARG A NE    
104  C  CZ    . ARG A 19  ? 0.98430 0.99800 0.92800 -0.22700 -0.14060 0.01100  19  ARG A CZ    
105  N  NH1   . ARG A 19  ? 1.10240 1.09570 1.03260 -0.23830 -0.13340 -0.00530 19  ARG A NH1   
106  N  NH2   . ARG A 19  ? 0.86080 0.89810 0.85010 -0.21240 -0.13670 0.02260  19  ARG A NH2   
107  N  N     . GLY A 20  ? 0.96140 0.91810 0.72820 -0.22940 -0.13130 0.03730  20  GLY A N     
108  C  CA    . GLY A 20  ? 0.86480 0.81960 0.62760 -0.22420 -0.11230 0.03920  20  GLY A CA    
109  C  C     . GLY A 20  ? 0.88770 0.83350 0.61870 -0.23690 -0.08760 0.02210  20  GLY A C     
110  O  O     . GLY A 20  ? 1.01310 0.95010 0.72150 -0.24860 -0.08430 0.00790  20  GLY A O     
111  N  N     . LEU A 21  ? 0.81920 0.76710 0.54750 -0.23560 -0.06990 0.02280  21  LEU A N     
112  C  CA    . LEU A 21  ? 0.86690 0.81380 0.57250 -0.24650 -0.04350 0.00740  21  LEU A CA    
113  C  C     . LEU A 21  ? 0.97390 0.90030 0.62800 -0.26350 -0.04260 0.01530  21  LEU A C     
114  O  O     . LEU A 21  ? 1.07450 0.99450 0.72940 -0.26000 -0.05190 0.03160  21  LEU A O     
115  C  CB    . LEU A 21  ? 0.85160 0.82430 0.60240 -0.23280 -0.02220 0.00050  21  LEU A CB    
116  C  CG    . LEU A 21  ? 0.86800 0.84960 0.61050 -0.24010 0.00640  -0.01780 21  LEU A CG    
117  C  CD1   . LEU A 21  ? 1.01480 0.98960 0.74890 -0.24280 0.01300  -0.03590 21  LEU A CD1   
118  C  CD2   . LEU A 21  ? 0.88890 0.89960 0.67970 -0.22560 0.02170  -0.02060 21  LEU A CD2   
119  N  N     . ARG A 22  ? 1.03830 0.95130 0.64520 -0.28280 -0.03020 0.00340  22  ARG A N     
120  C  CA    . ARG A 22  ? 1.06270 0.95130 0.61020 -0.30380 -0.02900 0.01110  22  ARG A CA    
121  C  C     . ARG A 22  ? 1.07290 0.97170 0.60670 -0.31670 0.00600  -0.00640 22  ARG A C     
122  O  O     . ARG A 22  ? 1.08660 1.00000 0.63450 -0.31410 0.02480  -0.02750 22  ARG A O     
123  C  CB    . ARG A 22  ? 1.12730 0.98720 0.61830 -0.31980 -0.04990 0.01480  22  ARG A CB    
124  C  CG    . ARG A 22  ? 1.32500 1.15410 0.74250 -0.34520 -0.04850 0.02260  22  ARG A CG    
125  C  CD    . ARG A 22  ? 1.38710 1.18740 0.75630 -0.35540 -0.08210 0.03540  22  ARG A CD    
126  N  NE    . ARG A 22  ? 1.28380 1.08540 0.64040 -0.36220 -0.08200 0.01620  22  ARG A NE    
127  C  CZ    . ARG A 22  ? 1.31880 1.10200 0.63880 -0.37240 -0.11070 0.02140  22  ARG A CZ    
128  N  NH1   . ARG A 22  ? 1.39280 1.15690 0.68760 -0.37460 -0.14420 0.04700  22  ARG A NH1   
129  N  NH2   . ARG A 22  ? 1.34210 1.12520 0.65120 -0.38020 -0.10700 0.00040  22  ARG A NH2   
130  N  N     . ALA A 23  ? 1.06770 0.95870 0.57550 -0.33070 0.01550  0.00200  23  ALA A N     
131  C  CA    . ALA A 23  ? 1.04860 0.95450 0.54580 -0.34560 0.04990  -0.01370 23  ALA A CA    
132  C  C     . ALA A 23  ? 1.15940 1.04040 0.58550 -0.37120 0.05850  -0.02160 23  ALA A C     
133  O  O     . ALA A 23  ? 1.29280 1.13810 0.66330 -0.38510 0.03700  -0.00570 23  ALA A O     
134  C  CB    . ALA A 23  ? 1.05950 0.96880 0.55960 -0.35350 0.05780  -0.00200 23  ALA A CB    
135  N  N     . LEU A 24  ? 1.06650 0.96610 0.49300 -0.37730 0.09050  -0.04610 24  LEU A N     
136  C  CA    . LEU A 24  ? 1.18350 1.06210 0.54030 -0.40370 0.10620  -0.05760 24  LEU A CA    
137  C  C     . LEU A 24  ? 1.26780 1.15830 0.60420 -0.42550 0.13940  -0.06270 24  LEU A C     
138  O  O     . LEU A 24  ? 1.33770 1.20710 0.60650 -0.45210 0.15350  -0.06840 24  LEU A O     
139  C  CB    . LEU A 24  ? 1.14210 1.02600 0.50340 -0.39730 0.11990  -0.08490 24  LEU A CB    
140  C  CG    . LEU A 24  ? 1.22230 1.08820 0.58890 -0.38460 0.08570  -0.07960 24  LEU A CG    
141  C  CD1   . LEU A 24  ? 1.30900 1.17640 0.68380 -0.37790 0.09960  -0.10760 24  LEU A CD1   
142  C  CD2   . LEU A 24  ? 1.26330 1.08910 0.56050 -0.40390 0.05410  -0.05950 24  LEU A CD2   
143  N  N     . GLN A 25  ? 1.20970 1.13380 0.60080 -0.41690 0.15230  -0.06100 25  GLN A N     
144  C  CA    . GLN A 25  ? 1.18450 1.12690 0.56660 -0.43860 0.18290  -0.06480 25  GLN A CA    
145  C  C     . GLN A 25  ? 1.15080 1.09720 0.56140 -0.43590 0.16890  -0.04350 25  GLN A C     
146  O  O     . GLN A 25  ? 1.22270 1.16960 0.67410 -0.41170 0.14330  -0.03280 25  GLN A O     
147  C  CB    . GLN A 25  ? 1.16210 1.15460 0.59500 -0.42960 0.22030  -0.09360 25  GLN A CB    
148  C  CG    . GLN A 25  ? 1.15910 1.19090 0.68120 -0.39600 0.21500  -0.09740 25  GLN A CG    
149  C  CD    . GLN A 25  ? 1.21930 1.29670 0.79160 -0.38280 0.24840  -0.12550 25  GLN A CD    
150  O  OE1   . GLN A 25  ? 1.29590 1.36680 0.84110 -0.38770 0.26880  -0.14630 25  GLN A OE1   
151  N  NE2   . GLN A 25  ? 1.03020 1.15270 0.67570 -0.36500 0.25310  -0.12640 25  GLN A NE2   
152  N  N     . PRO A 26  ? 1.07520 1.02400 0.46750 -0.46010 0.18530  -0.03820 26  PRO A N     
153  C  CA    . PRO A 26  ? 1.07250 1.02060 0.48840 -0.45950 0.17230  -0.01980 26  PRO A CA    
154  C  C     . PRO A 26  ? 1.14230 1.14380 0.64100 -0.43940 0.18160  -0.02970 26  PRO A C     
155  O  O     . PRO A 26  ? 1.17260 1.22040 0.71150 -0.43410 0.20790  -0.05110 26  PRO A O     
156  C  CB    . PRO A 26  ? 1.08840 1.02310 0.47680 -0.48380 0.18180  -0.01750 26  PRO A CB    
157  C  CG    . PRO A 26  ? 1.19350 1.15120 0.57650 -0.49280 0.21160  -0.04110 26  PRO A CG    
158  C  CD    . PRO A 26  ? 1.20120 1.14680 0.56360 -0.48150 0.20640  -0.04920 26  PRO A CD    
159  N  N     . PHE A 27  ? 1.09430 1.08790 0.61910 -0.42620 0.15800  -0.01390 27  PHE A N     
160  C  CA    . PHE A 27  ? 1.06040 1.09880 0.65610 -0.41070 0.16190  -0.01930 27  PHE A CA    
161  C  C     . PHE A 27  ? 1.17260 1.19640 0.76080 -0.42610 0.15430  -0.00360 27  PHE A C     
162  O  O     . PHE A 27  ? 1.22970 1.20600 0.78560 -0.42520 0.13010  0.01510  27  PHE A O     
163  C  CB    . PHE A 27  ? 1.01870 1.06340 0.65950 -0.37510 0.14020  -0.01890 27  PHE A CB    
164  C  CG    . PHE A 27  ? 0.95600 1.01810 0.61490 -0.35860 0.14880  -0.03640 27  PHE A CG    
165  C  CD1   . PHE A 27  ? 1.00420 1.11600 0.71600 -0.34770 0.17080  -0.05530 27  PHE A CD1   
166  C  CD2   . PHE A 27  ? 0.91870 0.94610 0.54220 -0.35370 0.13340  -0.03400 27  PHE A CD2   
167  C  CE1   . PHE A 27  ? 1.01630 1.13680 0.74290 -0.33130 0.17880  -0.07200 27  PHE A CE1   
168  C  CE2   . PHE A 27  ? 0.97480 1.01250 0.61130 -0.34060 0.14100  -0.05120 27  PHE A CE2   
169  C  CZ    . PHE A 27  ? 1.02780 1.10910 0.71460 -0.32890 0.16450  -0.07060 27  PHE A CZ    
170  N  N     . GLN A 28  ? 1.28760 1.35210 0.90790 -0.43940 0.17420  -0.01150 28  GLN A N     
171  C  CA    . GLN A 28  ? 1.28620 1.33940 0.90830 -0.45040 0.16490  -0.00120 28  GLN A CA    
172  C  C     . GLN A 28  ? 1.25690 1.32920 0.92980 -0.42990 0.15010  0.00200  28  GLN A C     
173  O  O     . GLN A 28  ? 1.19570 1.30070 0.91650 -0.40200 0.14730  -0.00740 28  GLN A O     
174  C  CB    . GLN A 28  ? 1.29540 1.37740 0.92900 -0.46910 0.18410  -0.01230 28  GLN A CB    
175  C  CG    . GLN A 28  ? 1.34680 1.40690 0.93050 -0.48750 0.19680  -0.01590 28  GLN A CG    
176  C  CD    . GLN A 28  ? 1.51930 1.50650 1.03470 -0.49920 0.17550  0.00450  28  GLN A CD    
177  O  OE1   . GLN A 28  ? 1.58890 1.54020 1.05770 -0.50000 0.16880  0.01000  28  GLN A OE1   
178  N  NE2   . GLN A 28  ? 1.48980 1.45360 1.00030 -0.50660 0.16250  0.01600  28  GLN A NE2   
179  N  N     . VAL A 29  ? 1.06360 1.10730 0.72240 -0.44020 0.13720  0.01480  29  VAL A N     
180  C  CA    . VAL A 29  ? 0.99420 1.05270 0.69670 -0.42170 0.12240  0.01570  29  VAL A CA    
181  C  C     . VAL A 29  ? 0.96950 1.10020 0.73570 -0.41660 0.13760  -0.00060 29  VAL A C     
182  O  O     . VAL A 29  ? 0.97980 1.14190 0.75670 -0.43510 0.15500  -0.00960 29  VAL A O     
183  C  CB    . VAL A 29  ? 1.00790 1.02820 0.68190 -0.44240 0.11400  0.02690  29  VAL A CB    
184  C  CG1   . VAL A 29  ? 1.04150 1.08600 0.75850 -0.43290 0.10540  0.02380  29  VAL A CG1   
185  C  CG2   . VAL A 29  ? 1.06460 1.01280 0.68660 -0.43690 0.09380  0.04460  29  VAL A CG2   
186  N  N     . GLY A 30  ? 0.90270 1.05790 0.71430 -0.38470 0.12700  -0.00480 30  GLY A N     
187  C  CA    . GLY A 30  ? 0.80030 1.02120 0.67510 -0.37350 0.13650  -0.01790 30  GLY A CA    
188  C  C     . GLY A 30  ? 0.90770 1.15830 0.80550 -0.35790 0.15180  -0.03130 30  GLY A C     
189  O  O     . GLY A 30  ? 0.85620 1.15610 0.81020 -0.33990 0.15560  -0.04060 30  GLY A O     
190  N  N     . ASP A 31  ? 1.01860 1.23940 0.87330 -0.36450 0.16040  -0.03280 31  ASP A N     
191  C  CA    . ASP A 31  ? 1.01990 1.26360 0.89170 -0.35070 0.17650  -0.04810 31  ASP A CA    
192  C  C     . ASP A 31  ? 0.99370 1.23400 0.89430 -0.31560 0.15900  -0.04770 31  ASP A C     
193  O  O     . ASP A 31  ? 0.99390 1.19870 0.87900 -0.30560 0.13590  -0.03440 31  ASP A O     
194  C  CB    . ASP A 31  ? 1.10100 1.30740 0.91120 -0.36760 0.18720  -0.04980 31  ASP A CB    
195  C  CG    . ASP A 31  ? 1.20770 1.42440 0.99100 -0.40340 0.21240  -0.05390 31  ASP A CG    
196  O  OD1   . ASP A 31  ? 1.20880 1.46560 1.02820 -0.41310 0.22120  -0.05730 31  ASP A OD1   
197  O  OD2   . ASP A 31  ? 1.23160 1.41630 0.95750 -0.42110 0.22210  -0.05420 31  ASP A OD2   
198  N  N     . LEU A 32  ? 0.78840 1.06530 0.73230 -0.29670 0.17120  -0.06230 32  LEU A N     
199  C  CA    . LEU A 32  ? 0.74260 1.01260 0.71070 -0.26560 0.15700  -0.06230 32  LEU A CA    
200  C  C     . LEU A 32  ? 0.78530 1.01520 0.71180 -0.26410 0.15740  -0.06630 32  LEU A C     
201  O  O     . LEU A 32  ? 0.66820 0.90420 0.58370 -0.27010 0.17890  -0.08170 32  LEU A O     
202  C  CB    . LEU A 32  ? 0.67800 0.99850 0.70950 -0.24430 0.16780  -0.07510 32  LEU A CB    
203  C  CG    . LEU A 32  ? 0.62980 0.94040 0.68630 -0.21300 0.15400  -0.07420 32  LEU A CG    
204  C  CD1   . LEU A 32  ? 0.65890 0.95320 0.71780 -0.20480 0.12710  -0.05610 32  LEU A CD1   
205  C  CD2   . LEU A 32  ? 0.68400 1.03980 0.79990 -0.19140 0.16630  -0.08710 32  LEU A CD2   
206  N  N     . LEU A 33  ? 0.80780 0.99770 0.71030 -0.25730 0.13400  -0.05310 33  LEU A N     
207  C  CA    . LEU A 33  ? 0.78250 0.93830 0.65020 -0.25570 0.13050  -0.05680 33  LEU A CA    
208  C  C     . LEU A 33  ? 0.77070 0.93990 0.67490 -0.23210 0.13540  -0.06990 33  LEU A C     
209  O  O     . LEU A 33  ? 0.84060 1.00700 0.73220 -0.23410 0.15220  -0.08640 33  LEU A O     
210  C  CB    . LEU A 33  ? 0.75180 0.86690 0.59010 -0.25480 0.10340  -0.03900 33  LEU A CB    
211  C  CG    . LEU A 33  ? 0.83070 0.91280 0.61450 -0.27790 0.09650  -0.02640 33  LEU A CG    
212  C  CD1   . LEU A 33  ? 0.80820 0.90000 0.59930 -0.28830 0.09750  -0.01770 33  LEU A CD1   
213  C  CD2   . LEU A 33  ? 0.71500 0.75910 0.47410 -0.27160 0.07020  -0.01260 33  LEU A CD2   
214  N  N     . PHE A 34  ? 0.76360 0.94460 0.71050 -0.21020 0.12180  -0.06330 34  PHE A N     
215  C  CA    . PHE A 34  ? 0.76500 0.95390 0.74480 -0.18820 0.12690  -0.07490 34  PHE A CA    
216  C  C     . PHE A 34  ? 0.72590 0.93510 0.75490 -0.16670 0.11450  -0.06580 34  PHE A C     
217  O  O     . PHE A 34  ? 0.72750 0.93990 0.76020 -0.16870 0.10030  -0.05100 34  PHE A O     
218  C  CB    . PHE A 34  ? 0.79680 0.94630 0.74720 -0.18620 0.11870  -0.07810 34  PHE A CB    
219  C  CG    . PHE A 34  ? 0.78180 0.90770 0.72510 -0.18220 0.09240  -0.06050 34  PHE A CG    
220  C  CD1   . PHE A 34  ? 0.78690 0.89250 0.69370 -0.19740 0.07900  -0.04730 34  PHE A CD1   
221  C  CD2   . PHE A 34  ? 0.83540 0.95880 0.80950 -0.16280 0.08190  -0.05700 34  PHE A CD2   
222  C  CE1   . PHE A 34  ? 0.79350 0.88180 0.70000 -0.19140 0.05650  -0.03250 34  PHE A CE1   
223  C  CE2   . PHE A 34  ? 0.88650 0.99280 0.85740 -0.16000 0.06070  -0.04190 34  PHE A CE2   
224  C  CZ    . PHE A 34  ? 0.88430 0.97560 0.82390 -0.17340 0.04850  -0.03040 34  PHE A CZ    
225  N  N     A SER A 35  ? 0.70040 0.91890 0.76370 -0.14580 0.11990  -0.07480 35  SER A N     
226  C  CA    A SER A 35  ? 0.66570 0.89610 0.77000 -0.12440 0.10650  -0.06480 35  SER A CA    
227  C  C     A SER A 35  ? 0.65050 0.85050 0.75620 -0.10920 0.10020  -0.06660 35  SER A C     
228  O  O     A SER A 35  ? 0.71010 0.89190 0.80150 -0.10950 0.11200  -0.08190 35  SER A O     
229  C  CB    A SER A 35  ? 0.62740 0.90430 0.78140 -0.11170 0.11680  -0.07060 35  SER A CB    
230  O  OG    A SER A 35  ? 0.78830 1.07040 0.95930 -0.09950 0.13560  -0.08910 35  SER A OG    
231  N  N     . CYS A 36  ? 0.61150 0.80460 0.73210 -0.09800 0.08230  -0.05140 36  CYS A N     
232  C  CA    . CYS A 36  ? 0.62800 0.78970 0.74700 -0.08830 0.07270  -0.04790 36  CYS A CA    
233  C  C     . CYS A 36  ? 0.61460 0.78460 0.76940 -0.06850 0.06300  -0.03640 36  CYS A C     
234  O  O     . CYS A 36  ? 0.64910 0.83020 0.80900 -0.06900 0.05070  -0.02100 36  CYS A O     
235  C  CB    . CYS A 36  ? 0.68250 0.81900 0.76920 -0.10210 0.05810  -0.03730 36  CYS A CB    
236  S  SG    . CYS A 36  ? 0.82670 0.92780 0.91080 -0.09670 0.04780  -0.03490 36  CYS A SG    
237  N  N     A PRO A 37  ? 0.57980 0.74300 0.75750 -0.05080 0.06860  -0.04360 37  PRO A N     
238  C  CA    A PRO A 37  ? 0.53100 0.69390 0.73690 -0.03220 0.05710  -0.03000 37  PRO A CA    
239  C  C     A PRO A 37  ? 0.57910 0.71240 0.76690 -0.03790 0.04240  -0.01530 37  PRO A C     
240  O  O     A PRO A 37  ? 0.68800 0.79470 0.85010 -0.05010 0.04210  -0.01970 37  PRO A O     
241  C  CB    A PRO A 37  ? 0.56480 0.71500 0.79170 -0.01320 0.06790  -0.04330 37  PRO A CB    
242  C  CG    A PRO A 37  ? 0.63630 0.76380 0.83330 -0.02610 0.08190  -0.06290 37  PRO A CG    
243  C  CD    A PRO A 37  ? 0.68390 0.83260 0.85780 -0.04730 0.08570  -0.06470 37  PRO A CD    
244  N  N     . ALA A 38  ? 0.53800 0.67890 0.73910 -0.03050 0.03000  0.00250  38  ALA A N     
245  C  CA    . ALA A 38  ? 0.57180 0.68930 0.75890 -0.03610 0.01880  0.01670  38  ALA A CA    
246  C  C     . ALA A 38  ? 0.62910 0.70930 0.81510 -0.03160 0.01990  0.01320  38  ALA A C     
247  O  O     . ALA A 38  ? 0.73180 0.80280 0.93660 -0.01500 0.02300  0.01030  38  ALA A O     
248  C  CB    . ALA A 38  ? 0.60380 0.73510 0.80210 -0.02890 0.00770  0.03520  38  ALA A CB    
249  N  N     . TYR A 39  ? 0.60640 0.66470 0.77160 -0.04640 0.01670  0.01360  39  TYR A N     
250  C  CA    . TYR A 39  ? 0.65140 0.67270 0.81400 -0.04670 0.01550  0.01250  39  TYR A CA    
251  C  C     . TYR A 39  ? 0.71280 0.72370 0.88680 -0.03900 0.00740  0.03180  39  TYR A C     
252  O  O     . TYR A 39  ? 0.79300 0.77670 0.97540 -0.02830 0.00780  0.03280  39  TYR A O     
253  C  CB    . TYR A 39  ? 0.68140 0.68890 0.82180 -0.06700 0.01190  0.00860  39  TYR A CB    
254  C  CG    . TYR A 39  ? 0.67770 0.64790 0.81380 -0.07290 0.00950  0.00710  39  TYR A CG    
255  C  CD1   . TYR A 39  ? 0.80760 0.74990 0.93330 -0.07440 0.01650  -0.01180 39  TYR A CD1   
256  C  CD2   . TYR A 39  ? 0.66970 0.63150 0.81000 -0.07930 0.00150  0.02330  39  TYR A CD2   
257  C  CE1   . TYR A 39  ? 0.80620 0.71040 0.92540 -0.08250 0.01380  -0.01440 39  TYR A CE1   
258  C  CE2   . TYR A 39  ? 0.72030 0.64760 0.85660 -0.08830 -0.00050 0.02210  39  TYR A CE2   
259  C  CZ    . TYR A 39  ? 0.80700 0.70430 0.93250 -0.09020 0.00470  0.00320  39  TYR A CZ    
260  O  OH    . TYR A 39  ? 0.97430 0.83300 1.09320 -0.10160 0.00220  0.00060  39  TYR A OH    
261  N  N     . ALA A 40  ? 0.67880 0.70800 0.85010 -0.04450 0.00050  0.04720  40  ALA A N     
262  C  CA    . ALA A 40  ? 0.68070 0.70420 0.85680 -0.03950 -0.00630 0.06680  40  ALA A CA    
263  C  C     . ALA A 40  ? 0.65380 0.70960 0.82760 -0.04050 -0.01020 0.07640  40  ALA A C     
264  O  O     . ALA A 40  ? 0.65140 0.72540 0.81690 -0.04980 -0.00830 0.07040  40  ALA A O     
265  C  CB    . ALA A 40  ? 0.68210 0.68050 0.84910 -0.05310 -0.00840 0.07490  40  ALA A CB    
266  N  N     . TYR A 41  ? 0.68360 0.74340 0.86210 -0.03110 -0.01640 0.09130  41  TYR A N     
267  C  CA    . TYR A 41  ? 0.57630 0.66470 0.74930 -0.03280 -0.02060 0.09850  41  TYR A CA    
268  C  C     . TYR A 41  ? 0.60520 0.68650 0.77250 -0.02850 -0.02860 0.11840  41  TYR A C     
269  O  O     . TYR A 41  ? 0.65630 0.71370 0.82860 -0.01980 -0.03230 0.12710  41  TYR A O     
270  C  CB    . TYR A 41  ? 0.55790 0.67500 0.74440 -0.02480 -0.02060 0.08880  41  TYR A CB    
271  C  CG    . TYR A 41  ? 0.66200 0.77910 0.87160 -0.00560 -0.02440 0.09050  41  TYR A CG    
272  C  CD1   . TYR A 41  ? 0.70500 0.80630 0.92820 0.00330  -0.01690 0.07750  41  TYR A CD1   
273  C  CD2   . TYR A 41  ? 0.67860 0.81060 0.89590 0.00450  -0.03610 0.10460  41  TYR A CD2   
274  C  CE1   . TYR A 41  ? 0.68310 0.78340 0.93140 0.02440  -0.01940 0.07810  41  TYR A CE1   
275  C  CE2   . TYR A 41  ? 0.73880 0.87240 0.98190 0.02510  -0.04170 0.10750  41  TYR A CE2   
276  C  CZ    . TYR A 41  ? 0.74440 0.86210 1.00500 0.03630  -0.03260 0.09390  41  TYR A CZ    
277  O  OH    . TYR A 41  ? 0.83710 0.95560 1.12710 0.06020  -0.03720 0.09580  41  TYR A OH    
278  N  N     . VAL A 42  ? 0.59180 0.69110 0.74510 -0.03500 -0.03140 0.12550  42  VAL A N     
279  C  CA    . VAL A 42  ? 0.63890 0.73290 0.77860 -0.03380 -0.03900 0.14430  42  VAL A CA    
280  C  C     . VAL A 42  ? 0.63600 0.75760 0.76400 -0.03760 -0.04360 0.14500  42  VAL A C     
281  O  O     . VAL A 42  ? 0.71010 0.84450 0.83060 -0.04710 -0.03720 0.13470  42  VAL A O     
282  C  CB    . VAL A 42  ? 0.61570 0.68730 0.73920 -0.04590 -0.03280 0.15410  42  VAL A CB    
283  C  CG1   . VAL A 42  ? 0.52010 0.60460 0.63580 -0.05920 -0.02320 0.14530  42  VAL A CG1   
284  C  CG2   . VAL A 42  ? 0.77500 0.83740 0.87870 -0.04630 -0.03920 0.17430  42  VAL A CG2   
285  N  N     . LEU A 43  ? 0.64760 0.77580 0.77280 -0.03010 -0.05620 0.15760  43  LEU A N     
286  C  CA    . LEU A 43  ? 0.74280 0.89440 0.85260 -0.03570 -0.06350 0.15980  43  LEU A CA    
287  C  C     . LEU A 43  ? 0.79150 0.93060 0.86600 -0.04850 -0.05970 0.16940  43  LEU A C     
288  O  O     . LEU A 43  ? 0.83810 0.95450 0.89960 -0.04890 -0.06020 0.18450  43  LEU A O     
289  C  CB    . LEU A 43  ? 0.73640 0.90280 0.85860 -0.02290 -0.08140 0.17010  43  LEU A CB    
290  C  CG    . LEU A 43  ? 0.67580 0.87040 0.78500 -0.02980 -0.09280 0.17130  43  LEU A CG    
291  C  CD1   . LEU A 43  ? 0.65050 0.87420 0.77720 -0.03480 -0.08760 0.15190  43  LEU A CD1   
292  C  CD2   . LEU A 43  ? 0.91390 1.11950 1.03250 -0.01710 -0.11430 0.18730  43  LEU A CD2   
293  N  N     . THR A 44  ? 0.74140 0.89330 0.79890 -0.05950 -0.05460 0.16040  44  THR A N     
294  C  CA    . THR A 44  ? 0.73100 0.87250 0.75510 -0.07090 -0.04730 0.16590  44  THR A CA    
295  C  C     . THR A 44  ? 0.88390 1.02240 0.88210 -0.07190 -0.06040 0.18300  44  THR A C     
296  O  O     . THR A 44  ? 1.01150 1.16530 1.01650 -0.06560 -0.07750 0.18710  44  THR A O     
297  C  CB    . THR A 44  ? 0.72460 0.87620 0.73620 -0.08020 -0.03890 0.15070  44  THR A CB    
298  O  OG1   . THR A 44  ? 0.89620 1.03550 0.88360 -0.08860 -0.02540 0.15230  44  THR A OG1   
299  C  CG2   . THR A 44  ? 0.80560 0.97430 0.80400 -0.08400 -0.05110 0.14820  44  THR A CG2   
300  N  N     . VAL A 45  ? 0.90770 1.02770 0.87650 -0.08030 -0.05260 0.19380  45  VAL A N     
301  C  CA    . VAL A 45  ? 1.01290 1.12250 0.95090 -0.08250 -0.06490 0.21380  45  VAL A CA    
302  C  C     . VAL A 45  ? 1.11630 1.24420 1.03230 -0.08690 -0.07940 0.21210  45  VAL A C     
303  O  O     . VAL A 45  ? 1.22760 1.35980 1.13830 -0.08170 -0.10070 0.22640  45  VAL A O     
304  C  CB    . VAL A 45  ? 0.96750 1.05570 0.87320 -0.09510 -0.04870 0.22280  45  VAL A CB    
305  C  CG1   . VAL A 45  ? 0.98760 1.06440 0.84810 -0.10190 -0.06010 0.24210  45  VAL A CG1   
306  C  CG2   . VAL A 45  ? 1.01200 1.08090 0.93950 -0.09240 -0.04040 0.22960  45  VAL A CG2   
307  N  N     . ASN A 46  ? 1.09050 1.22850 0.99370 -0.09670 -0.06950 0.19490  46  ASN A N     
308  C  CA    . ASN A 46  ? 1.14450 1.29540 1.01980 -0.10570 -0.08160 0.19130  46  ASN A CA    
309  C  C     . ASN A 46  ? 1.11550 1.29430 1.02040 -0.09880 -0.10290 0.18920  46  ASN A C     
310  O  O     . ASN A 46  ? 1.16410 1.35680 1.04850 -0.10720 -0.11830 0.18940  46  ASN A O     
311  C  CB    . ASN A 46  ? 1.19470 1.34290 1.05000 -0.11730 -0.06370 0.17180  46  ASN A CB    
312  C  CG    . ASN A 46  ? 1.32080 1.44760 1.13840 -0.12610 -0.04480 0.17460  46  ASN A CG    
313  O  OD1   . ASN A 46  ? 1.24540 1.36010 1.03840 -0.12900 -0.04810 0.19220  46  ASN A OD1   
314  N  ND2   . ASN A 46  ? 1.32100 1.44290 1.13300 -0.13040 -0.02440 0.15740  46  ASN A ND2   
315  N  N     . GLU A 47  ? 1.24330 1.43250 1.19520 -0.08520 -0.10330 0.18560  47  GLU A N     
316  C  CA    . GLU A 47  ? 1.22870 1.44940 1.21530 -0.07790 -0.11940 0.18180  47  GLU A CA    
317  C  C     . GLU A 47  ? 1.23850 1.46390 1.25010 -0.06020 -0.13740 0.19950  47  GLU A C     
318  O  O     . GLU A 47  ? 1.22310 1.47760 1.27360 -0.04990 -0.14880 0.19630  47  GLU A O     
319  C  CB    . GLU A 47  ? 1.19390 1.42530 1.21450 -0.07560 -0.10580 0.16270  47  GLU A CB    
320  C  CG    . GLU A 47  ? 1.18770 1.41490 1.18630 -0.09140 -0.09220 0.14600  47  GLU A CG    
321  C  CD    . GLU A 47  ? 1.27100 1.51710 1.25140 -0.10520 -0.10470 0.14080  47  GLU A CD    
322  O  OE1   . GLU A 47  ? 1.29960 1.57380 1.29920 -0.10200 -0.12380 0.14660  47  GLU A OE1   
323  O  OE2   . GLU A 47  ? 1.30750 1.54030 1.25540 -0.11920 -0.09570 0.13050  47  GLU A OE2   
324  N  N     . ARG A 48  ? 1.10750 1.30400 1.09870 -0.05620 -0.13920 0.21800  48  ARG A N     
325  C  CA    . ARG A 48  ? 1.04860 1.24220 1.05730 -0.03870 -0.15870 0.23760  48  ARG A CA    
326  C  C     . ARG A 48  ? 1.09980 1.32120 1.10120 -0.03960 -0.18620 0.24730  48  ARG A C     
327  O  O     . ARG A 48  ? 1.17270 1.39580 1.13120 -0.05760 -0.19040 0.24760  48  ARG A O     
328  C  CB    . ARG A 48  ? 1.12320 1.27470 1.10040 -0.03980 -0.15490 0.25730  48  ARG A CB    
329  C  CG    . ARG A 48  ? 1.14020 1.26550 1.12850 -0.03950 -0.13110 0.25040  48  ARG A CG    
330  C  CD    . ARG A 48  ? 1.12290 1.21060 1.07190 -0.04900 -0.12450 0.26860  48  ARG A CD    
331  N  NE    . ARG A 48  ? 1.00660 1.06890 0.97090 -0.04820 -0.10670 0.26610  48  ARG A NE    
332  C  CZ    . ARG A 48  ? 1.10070 1.13150 1.03810 -0.05890 -0.09640 0.27940  48  ARG A CZ    
333  N  NH1   . ARG A 48  ? 1.23080 1.24950 1.12150 -0.07080 -0.10010 0.29640  48  ARG A NH1   
334  N  NH2   . ARG A 48  ? 1.05060 1.06210 1.00660 -0.06010 -0.08170 0.27520  48  ARG A NH2   
335  N  N     . GLY A 49  ? 1.11580 1.36000 1.15990 -0.02010 -0.20540 0.25430  49  GLY A N     
336  C  CA    . GLY A 49  ? 1.07100 1.35020 1.11860 -0.01980 -0.23440 0.26290  49  GLY A CA    
337  C  C     . GLY A 49  ? 0.99860 1.32690 1.07910 -0.02640 -0.23540 0.24200  49  GLY A C     
338  O  O     . GLY A 49  ? 0.92330 1.29210 1.03470 -0.01890 -0.25920 0.24700  49  GLY A O     
339  N  N     . ASN A 50  ? 1.04300 1.36920 1.11850 -0.04090 -0.21080 0.21960  50  ASN A N     
340  C  CA    . ASN A 50  ? 1.00920 1.37610 1.11380 -0.04950 -0.20840 0.19970  50  ASN A CA    
341  C  C     . ASN A 50  ? 0.95100 1.33490 1.11300 -0.03320 -0.19510 0.18750  50  ASN A C     
342  O  O     . ASN A 50  ? 0.98200 1.41080 1.18440 -0.03230 -0.20070 0.17810  50  ASN A O     
343  C  CB    . ASN A 50  ? 1.06020 1.41160 1.12570 -0.07410 -0.18930 0.18230  50  ASN A CB    
344  C  CG    . ASN A 50  ? 1.14020 1.47250 1.14440 -0.09210 -0.19750 0.18940  50  ASN A CG    
345  O  OD1   . ASN A 50  ? 1.20980 1.55710 1.20150 -0.09430 -0.22300 0.20310  50  ASN A OD1   
346  N  ND2   . ASN A 50  ? 1.09820 1.39750 1.06350 -0.10470 -0.17570 0.17990  50  ASN A ND2   
347  N  N     . HIS A 51  ? 0.86340 1.21320 1.02890 -0.02170 -0.17730 0.18700  51  HIS A N     
348  C  CA    . HIS A 51  ? 0.87810 1.23470 1.08730 -0.00870 -0.16110 0.17310  51  HIS A CA    
349  C  C     . HIS A 51  ? 0.87610 1.21060 1.10700 0.01670  -0.16400 0.18530  51  HIS A C     
350  O  O     . HIS A 51  ? 0.93100 1.22940 1.13290 0.01970  -0.17010 0.20300  51  HIS A O     
351  C  CB    . HIS A 51  ? 0.80570 1.13910 0.99710 -0.02210 -0.13480 0.15600  51  HIS A CB    
352  C  CG    . HIS A 51  ? 0.89610 1.24590 1.06980 -0.04490 -0.12980 0.14220  51  HIS A CG    
353  N  ND1   . HIS A 51  ? 1.01660 1.35620 1.14620 -0.06230 -0.13560 0.14600  51  HIS A ND1   
354  C  CD2   . HIS A 51  ? 0.83250 1.20450 1.02400 -0.05410 -0.11900 0.12450  51  HIS A CD2   
355  C  CE1   . HIS A 51  ? 0.95860 1.31080 1.08060 -0.08020 -0.12920 0.13080  51  HIS A CE1   
356  N  NE2   . HIS A 51  ? 0.86450 1.23640 1.02320 -0.07640 -0.11950 0.11870  51  HIS A NE2   
357  N  N     . CYS A 52  ? 0.82310 1.17760 1.10380 0.03430  -0.15850 0.17530  52  CYS A N     
358  C  CA    . CYS A 52  ? 0.81810 1.14510 1.11960 0.05910  -0.15760 0.18270  52  CYS A CA    
359  C  C     . CYS A 52  ? 0.82710 1.10530 1.10240 0.05210  -0.13590 0.17630  52  CYS A C     
360  O  O     . CYS A 52  ? 0.87450 1.15440 1.14380 0.03800  -0.11710 0.15800  52  CYS A O     
361  C  CB    . CYS A 52  ? 0.81820 1.17990 1.17990 0.07980  -0.15370 0.16980  52  CYS A CB    
362  S  SG    . CYS A 52  ? 0.83620 1.15520 1.22170 0.10960  -0.14530 0.17100  52  CYS A SG    
363  N  N     . GLU A 53  ? 0.90800 1.14230 1.16660 0.06060  -0.14010 0.19280  53  GLU A N     
364  C  CA    . GLU A 53  ? 0.84090 1.03040 1.07500 0.05150  -0.12200 0.18900  53  GLU A CA    
365  C  C     . GLU A 53  ? 0.84940 1.03490 1.11080 0.05820  -0.10330 0.16730  53  GLU A C     
366  O  O     . GLU A 53  ? 0.85400 1.02410 1.09880 0.04330  -0.08670 0.15520  53  GLU A O     
367  C  CB    . GLU A 53  ? 0.93290 1.07730 1.14760 0.05900  -0.13130 0.21200  53  GLU A CB    
368  C  CG    . GLU A 53  ? 1.03390 1.17770 1.21020 0.04760  -0.14710 0.23310  53  GLU A CG    
369  C  CD    . GLU A 53  ? 1.12170 1.24680 1.25290 0.02230  -0.13370 0.23320  53  GLU A CD    
370  O  OE1   . GLU A 53  ? 1.14310 1.24640 1.27170 0.01480  -0.11480 0.22310  53  GLU A OE1   
371  O  OE2   . GLU A 53  ? 1.21200 1.34620 1.31090 0.00980  -0.14220 0.24270  53  GLU A OE2   
372  N  N     . TYR A 54  ? 0.89220 1.09210 1.19550 0.08090  -0.10570 0.16190  54  TYR A N     
373  C  CA    . TYR A 54  ? 0.89700 1.08700 1.22190 0.08850  -0.08670 0.14080  54  TYR A CA    
374  C  C     . TYR A 54  ? 0.77540 1.00280 1.10930 0.07540  -0.07190 0.11810  54  TYR A C     
375  O  O     . TYR A 54  ? 0.75140 0.96200 1.06840 0.06170  -0.05530 0.10380  54  TYR A O     
376  C  CB    . TYR A 54  ? 0.90330 1.09310 1.27050 0.11970  -0.09170 0.14140  54  TYR A CB    
377  C  CG    . TYR A 54  ? 0.93640 1.11180 1.32160 0.12760  -0.06990 0.11740  54  TYR A CG    
378  C  CD1   . TYR A 54  ? 0.99640 1.11890 1.35570 0.11980  -0.05800 0.11220  54  TYR A CD1   
379  C  CD2   . TYR A 54  ? 0.94090 1.15820 1.36800 0.14030  -0.06030 0.09870  54  TYR A CD2   
380  C  CE1   . TYR A 54  ? 0.97260 1.08010 1.34250 0.12470  -0.03860 0.08860  54  TYR A CE1   
381  C  CE2   . TYR A 54  ? 0.96240 1.16590 1.40080 0.14610  -0.03820 0.07500  54  TYR A CE2   
382  C  CZ    . TYR A 54  ? 0.99620 1.14280 1.40350 0.13820  -0.02810 0.06980  54  TYR A CZ    
383  O  OH    . TYR A 54  ? 1.05730 1.18780 1.47030 0.14210  -0.00680 0.04500  54  TYR A OH    
384  N  N     . CYS A 55  ? 0.78710 1.06550 1.14710 0.07810  -0.07890 0.11560  55  CYS A N     
385  C  CA    . CYS A 55  ? 0.75740 1.07360 1.13250 0.06760  -0.06440 0.09460  55  CYS A CA    
386  C  C     . CYS A 55  ? 0.73470 1.07410 1.08530 0.04220  -0.06830 0.09530  55  CYS A C     
387  O  O     . CYS A 55  ? 0.68880 1.05590 1.04620 0.02960  -0.05670 0.07970  55  CYS A O     
388  C  CB    . CYS A 55  ? 0.75990 1.12030 1.19040 0.08880  -0.06550 0.08760  55  CYS A CB    
389  S  SG    . CYS A 55  ? 0.65540 1.06830 1.11110 0.09400  -0.09380 0.10520  55  CYS A SG    
390  N  N     . PHE A 56  ? 0.70430 1.03100 1.02460 0.03390  -0.08320 0.11260  56  PHE A N     
391  C  CA    . PHE A 56  ? 0.70130 1.03840 0.99040 0.01000  -0.08620 0.11310  56  PHE A CA    
392  C  C     . PHE A 56  ? 0.78570 1.17470 1.09630 0.00420  -0.09660 0.11030  56  PHE A C     
393  O  O     . PHE A 56  ? 0.79480 1.19270 1.08120 -0.01750 -0.09680 0.10640  56  PHE A O     
394  C  CB    . PHE A 56  ? 0.68640 1.00520 0.95030 -0.00820 -0.06720 0.09850  56  PHE A CB    
395  C  CG    . PHE A 56  ? 0.69510 0.96870 0.92570 -0.01260 -0.06270 0.10520  56  PHE A CG    
396  C  CD1   . PHE A 56  ? 0.77230 1.01710 1.00470 0.00130  -0.06630 0.11660  56  PHE A CD1   
397  C  CD2   . PHE A 56  ? 0.63990 0.90010 0.83930 -0.03080 -0.05480 0.10040  56  PHE A CD2   
398  C  CE1   . PHE A 56  ? 0.74650 0.95450 0.95160 -0.00560 -0.06130 0.12250  56  PHE A CE1   
399  C  CE2   . PHE A 56  ? 0.62930 0.85540 0.80520 -0.03450 -0.05020 0.10610  56  PHE A CE2   
400  C  CZ    . PHE A 56  ? 0.66300 0.86520 0.84230 -0.02330 -0.05300 0.11690  56  PHE A CZ    
401  N  N     . THR A 57  ? 0.82960 1.25340 1.18660 0.02290  -0.10550 0.11190  57  THR A N     
402  C  CA    . THR A 57  ? 0.76410 1.24400 1.14740 0.01610  -0.11710 0.10980  57  THR A CA    
403  C  C     . THR A 57  ? 0.74030 1.22060 1.09390 0.00620  -0.14120 0.12720  57  THR A C     
404  O  O     . THR A 57  ? 0.77010 1.22660 1.11130 0.01930  -0.15620 0.14570  57  THR A O     
405  C  CB    . THR A 57  ? 0.69380 1.21400 1.13980 0.04210  -0.12250 0.10890  57  THR A CB    
406  O  OG1   . THR A 57  ? 0.75720 1.26910 1.22480 0.05270  -0.09780 0.09180  57  THR A OG1   
407  C  CG2   . THR A 57  ? 0.70220 1.28900 1.18270 0.03230  -0.13260 0.10440  57  THR A CG2   
408  N  N     . ARG A 58  ? 0.76670 1.27120 1.10550 -0.01820 -0.14520 0.12140  58  ARG A N     
409  C  CA    . ARG A 58  ? 0.79850 1.30510 1.10600 -0.03010 -0.16820 0.13510  58  ARG A CA    
410  C  C     . ARG A 58  ? 0.83420 1.39810 1.18550 -0.02250 -0.19280 0.14220  58  ARG A C     
411  O  O     . ARG A 58  ? 0.80400 1.41650 1.19280 -0.03030 -0.18990 0.12940  58  ARG A O     
412  C  CB    . ARG A 58  ? 0.80410 1.29900 1.06760 -0.06110 -0.15960 0.12410  58  ARG A CB    
413  C  CG    . ARG A 58  ? 0.90180 1.38980 1.12100 -0.07760 -0.17870 0.13390  58  ARG A CG    
414  C  CD    . ARG A 58  ? 0.98230 1.45470 1.15920 -0.10710 -0.16810 0.11990  58  ARG A CD    
415  N  NE    . ARG A 58  ? 1.09890 1.60410 1.29820 -0.12410 -0.16150 0.10360  58  ARG A NE    
416  C  CZ    . ARG A 58  ? 1.10010 1.58650 1.29050 -0.13460 -0.13870 0.08910  58  ARG A CZ    
417  N  NH1   . ARG A 58  ? 0.94190 1.38130 1.10530 -0.12900 -0.12190 0.08800  58  ARG A NH1   
418  N  NH2   . ARG A 58  ? 1.12400 1.63960 1.33170 -0.15280 -0.13360 0.07630  58  ARG A NH2   
419  N  N     . LYS A 59  ? 0.93380 1.49280 1.28030 -0.00820 -0.21770 0.16360  59  LYS A N     
420  C  CA    . LYS A 59  ? 0.97290 1.58480 1.35530 -0.00110 -0.24790 0.17460  59  LYS A CA    
421  C  C     . LYS A 59  ? 1.04310 1.62850 1.38950 0.00610  -0.27500 0.20080  59  LYS A C     
422  O  O     . LYS A 59  ? 1.06430 1.59390 1.37390 0.01320  -0.26770 0.21080  59  LYS A O     
423  C  CB    . LYS A 59  ? 0.92190 1.57550 1.38140 0.02810  -0.24680 0.17130  59  LYS A CB    
424  C  CG    . LYS A 59  ? 0.94730 1.55920 1.41580 0.06040  -0.24230 0.18180  59  LYS A CG    
425  C  CD    . LYS A 59  ? 0.87190 1.52420 1.41750 0.09090  -0.23940 0.17570  59  LYS A CD    
426  C  CE    . LYS A 59  ? 0.90170 1.56870 1.47090 0.08360  -0.20480 0.14770  59  LYS A CE    
427  N  NZ    . LYS A 59  ? 0.90230 1.60010 1.54190 0.11500  -0.19540 0.13880  59  LYS A NZ    
428  N  N     . GLU A 60  ? 1.11250 1.73910 1.46730 0.00120  -0.30670 0.21180  60  GLU A N     
429  C  CA    . GLU A 60  ? 1.11470 1.72570 1.43690 0.00660  -0.33850 0.23860  60  GLU A CA    
430  C  C     . GLU A 60  ? 1.09990 1.72010 1.47050 0.04480  -0.35770 0.25840  60  GLU A C     
431  O  O     . GLU A 60  ? 1.00310 1.66670 1.44610 0.06610  -0.35540 0.25060  60  GLU A O     
432  C  CB    . GLU A 60  ? 1.03560 1.68300 1.33640 -0.01980 -0.36530 0.24070  60  GLU A CB    
433  C  CG    . GLU A 60  ? 1.12750 1.74870 1.37100 -0.05530 -0.34380 0.22180  60  GLU A CG    
434  C  CD    . GLU A 60  ? 1.18670 1.81610 1.38040 -0.08440 -0.36780 0.22540  60  GLU A CD    
435  O  OE1   . GLU A 60  ? 1.14640 1.80700 1.35400 -0.07920 -0.40030 0.23890  60  GLU A OE1   
436  O  OE2   . GLU A 60  ? 1.37130 1.97000 1.51070 -0.11160 -0.35100 0.21110  60  GLU A OE2   
437  N  N     . GLY A 61  ? 1.22670 1.80250 1.55520 0.05350  -0.37510 0.28400  61  GLY A N     
438  C  CA    . GLY A 61  ? 1.23030 1.80340 1.59430 0.08950  -0.39720 0.30700  61  GLY A CA    
439  C  C     . GLY A 61  ? 1.20310 1.73750 1.59240 0.11460  -0.36970 0.30090  61  GLY A C     
440  O  O     . GLY A 61  ? 1.18540 1.74190 1.64040 0.14630  -0.37200 0.30030  61  GLY A O     
441  N  N     . LEU A 62  ? 1.10400 1.58170 1.44080 0.09870  -0.34230 0.29410  62  LEU A N     
442  C  CA    . LEU A 62  ? 1.22730 1.65820 1.57300 0.11580  -0.31670 0.28890  62  LEU A CA    
443  C  C     . LEU A 62  ? 1.41580 1.79640 1.74290 0.13660  -0.33440 0.31860  62  LEU A C     
444  O  O     . LEU A 62  ? 1.27330 1.63260 1.54800 0.12530  -0.35530 0.34160  62  LEU A O     
445  C  CB    . LEU A 62  ? 1.13380 1.52670 1.43020 0.08900  -0.28490 0.27300  62  LEU A CB    
446  C  CG    . LEU A 62  ? 0.96360 1.39450 1.27520 0.06940  -0.26450 0.24410  62  LEU A CG    
447  C  CD1   . LEU A 62  ? 0.99920 1.39250 1.25390 0.04210  -0.24110 0.23380  62  LEU A CD1   
448  C  CD2   . LEU A 62  ? 0.94260 1.39460 1.31570 0.08830  -0.24570 0.22490  62  LEU A CD2   
449  N  N     . SER A 63  ? 1.67370 2.03180 2.03990 0.16610  -0.32550 0.31790  63  SER A N     
450  C  CA    . SER A 63  ? 1.68230 1.98300 2.02930 0.18550  -0.33990 0.34570  63  SER A CA    
451  C  C     . SER A 63  ? 1.68510 1.92010 1.96050 0.16120  -0.32200 0.35150  63  SER A C     
452  O  O     . SER A 63  ? 1.62740 1.84970 1.89210 0.14470  -0.29050 0.32920  63  SER A O     
453  C  CB    . SER A 63  ? 1.68720 1.97530 2.09320 0.22280  -0.33260 0.34040  63  SER A CB    
454  O  OG    . SER A 63  ? 1.70850 2.01000 2.14460 0.22020  -0.29820 0.30700  63  SER A OG    
455  N  N     . LYS A 64  ? 1.43130 1.62520 1.65870 0.15930  -0.34250 0.38240  64  LYS A N     
456  C  CA    . LYS A 64  ? 1.32860 1.46590 1.48640 0.13370  -0.32700 0.39070  64  LYS A CA    
457  C  C     . LYS A 64  ? 1.29690 1.36810 1.45240 0.14990  -0.31970 0.40360  64  LYS A C     
458  O  O     . LYS A 64  ? 1.38730 1.44200 1.56660 0.17900  -0.34180 0.42310  64  LYS A O     
459  C  CB    . LYS A 64  ? 1.27310 1.40480 1.36770 0.11430  -0.35090 0.41600  64  LYS A CB    
460  C  CG    . LYS A 64  ? 1.29270 1.37180 1.31640 0.08540  -0.32940 0.42170  64  LYS A CG    
461  C  CD    . LYS A 64  ? 1.31940 1.39230 1.27030 0.05790  -0.34070 0.43780  64  LYS A CD    
462  C  CE    . LYS A 64  ? 1.27240 1.39970 1.22860 0.05510  -0.36720 0.43680  64  LYS A CE    
463  N  NZ    . LYS A 64  ? 1.20380 1.31760 1.08240 0.02860  -0.37920 0.45320  64  LYS A NZ    
464  N  N     . CYS A 65  ? 1.22780 1.26090 1.35710 0.13130  -0.28910 0.39190  65  CYS A N     
465  C  CA    . CYS A 65  ? 1.30680 1.27410 1.42970 0.14110  -0.28090 0.40260  65  CYS A CA    
466  C  C     . CYS A 65  ? 1.36820 1.28940 1.43770 0.13700  -0.30300 0.44080  65  CYS A C     
467  O  O     . CYS A 65  ? 1.39890 1.30820 1.40960 0.10760  -0.29820 0.45030  65  CYS A O     
468  C  CB    . CYS A 65  ? 1.27240 1.21530 1.37920 0.11820  -0.24540 0.38210  65  CYS A CB    
469  S  SG    . CYS A 65  ? 1.26330 1.12380 1.36070 0.12400  -0.23400 0.39250  65  CYS A SG    
470  N  N     . GLY A 66  ? 1.29610 1.18970 1.38540 0.16720  -0.32620 0.46240  66  GLY A N     
471  C  CA    . GLY A 66  ? 1.34360 1.19180 1.38300 0.16680  -0.35220 0.50230  66  GLY A CA    
472  C  C     . GLY A 66  ? 1.43900 1.22090 1.41760 0.13910  -0.33210 0.51400  66  GLY A C     
473  O  O     . GLY A 66  ? 1.53810 1.29270 1.45370 0.12140  -0.33960 0.53560  66  GLY A O     
474  N  N     . ARG A 67  ? 1.48180 1.24100 1.47700 0.13320  -0.30090 0.49170  67  ARG A N     
475  C  CA    . ARG A 67  ? 1.47920 1.17740 1.42740 0.10730  -0.28030 0.50060  67  ARG A CA    
476  C  C     . ARG A 67  ? 1.44120 1.15890 1.33760 0.06830  -0.26420 0.49820  67  ARG A C     
477  O  O     . ARG A 67  ? 1.48480 1.16950 1.32120 0.04890  -0.26950 0.52520  67  ARG A O     
478  C  CB    . ARG A 67  ? 1.52720 1.20930 1.51460 0.11120  -0.25300 0.47210  67  ARG A CB    
479  C  CG    . ARG A 67  ? 1.61440 1.27350 1.65180 0.15130  -0.26590 0.47180  67  ARG A CG    
480  C  CD    . ARG A 67  ? 1.56190 1.19610 1.63260 0.15640  -0.24050 0.44380  67  ARG A CD    
481  N  NE    . ARG A 67  ? 1.66090 1.26410 1.77130 0.19620  -0.25410 0.44740  67  ARG A NE    
482  C  CZ    . ARG A 67  ? 1.58500 1.13630 1.71190 0.20620  -0.23990 0.43470  67  ARG A CZ    
483  N  NH1   . ARG A 67  ? 1.55890 1.08390 1.66710 0.17760  -0.21320 0.41790  67  ARG A NH1   
484  N  NH2   . ARG A 67  ? 1.52620 1.05350 1.69150 0.24640  -0.25300 0.43730  67  ARG A NH2   
485  N  N     . CYS A 68  ? 1.47890 1.24820 1.39640 0.05670  -0.24350 0.46580  68  CYS A N     
486  C  CA    . CYS A 68  ? 1.42360 1.21280 1.30120 0.02280  -0.22340 0.45720  68  CYS A CA    
487  C  C     . CYS A 68  ? 1.38360 1.22450 1.24500 0.01750  -0.23760 0.45540  68  CYS A C     
488  O  O     . CYS A 68  ? 1.34830 1.19480 1.16220 -0.00950 -0.22600 0.45590  68  CYS A O     
489  C  CB    . CYS A 68  ? 1.31830 1.12570 1.22500 0.01190  -0.19150 0.42350  68  CYS A CB    
490  S  SG    . CYS A 68  ? 1.09950 0.96830 1.07190 0.03240  -0.19100 0.38900  68  CYS A SG    
491  N  N     . LYS A 69  ? 1.45290 1.33190 1.35350 0.04190  -0.26150 0.45210  69  LYS A N     
492  C  CA    . LYS A 69  ? 1.41400 1.34550 1.30650 0.03740  -0.27880 0.44880  69  LYS A CA    
493  C  C     . LYS A 69  ? 1.26790 1.23850 1.15840 0.01550  -0.25390 0.41780  69  LYS A C     
494  O  O     . LYS A 69  ? 1.20760 1.20460 1.06590 -0.00060 -0.26040 0.41610  69  LYS A O     
495  C  CB    . LYS A 69  ? 1.33740 1.24880 1.16450 0.02530  -0.30210 0.48110  69  LYS A CB    
496  C  CG    . LYS A 69  ? 1.32310 1.19150 1.14660 0.04730  -0.33090 0.51610  69  LYS A CG    
497  C  CD    . LYS A 69  ? 1.38480 1.23790 1.14180 0.03510  -0.34640 0.53390  69  LYS A CD    
498  C  CE    . LYS A 69  ? 1.40880 1.21400 1.15850 0.05710  -0.36460 0.55770  69  LYS A CE    
499  N  NZ    . LYS A 69  ? 1.45770 1.25500 1.14720 0.04820  -0.38370 0.57520  69  LYS A NZ    
500  N  N     . GLN A 70  ? 1.27330 1.24530 1.19610 0.01450  -0.22620 0.39300  70  GLN A N     
501  C  CA    . GLN A 70  ? 1.24380 1.24690 1.16760 -0.00370 -0.20240 0.36460  70  GLN A CA    
502  C  C     . GLN A 70  ? 1.21930 1.24700 1.20210 0.00920  -0.18960 0.33690  70  GLN A C     
503  O  O     . GLN A 70  ? 1.20400 1.23770 1.19010 -0.00390 -0.16510 0.31600  70  GLN A O     
504  C  CB    . GLN A 70  ? 1.27230 1.24910 1.15370 -0.02950 -0.17580 0.36360  70  GLN A CB    
505  C  CG    . GLN A 70  ? 1.33620 1.30540 1.15310 -0.04970 -0.18090 0.38000  70  GLN A CG    
506  C  CD    . GLN A 70  ? 1.39430 1.33930 1.17440 -0.07380 -0.15170 0.37930  70  GLN A CD    
507  O  OE1   . GLN A 70  ? 1.40230 1.36860 1.18300 -0.08650 -0.12940 0.35670  70  GLN A OE1   
508  N  NE2   . GLN A 70  ? 1.31970 1.22100 1.06700 -0.08080 -0.15160 0.40460  70  GLN A NE2   
509  N  N     . ALA A 71  ? 1.14900 1.19250 1.17830 0.03480  -0.20580 0.33650  71  ALA A N     
510  C  CA    . ALA A 71  ? 1.10260 1.17060 1.18520 0.04670  -0.19300 0.31010  71  ALA A CA    
511  C  C     . ALA A 71  ? 1.14330 1.25040 1.27000 0.07010  -0.21540 0.31070  71  ALA A C     
512  O  O     . ALA A 71  ? 1.20560 1.29810 1.34350 0.09110  -0.23630 0.33110  71  ALA A O     
513  C  CB    . ALA A 71  ? 1.13520 1.16140 1.23410 0.05500  -0.17730 0.30620  71  ALA A CB    
514  N  N     . PHE A 72  ? 1.11900 1.27630 1.27190 0.06630  -0.21110 0.28890  72  PHE A N     
515  C  CA    . PHE A 72  ? 1.12120 1.32750 1.31540 0.08260  -0.23230 0.28870  72  PHE A CA    
516  C  C     . PHE A 72  ? 1.08960 1.32170 1.34280 0.09840  -0.21760 0.26460  72  PHE A C     
517  O  O     . PHE A 72  ? 1.06120 1.28790 1.31440 0.08720  -0.19180 0.24320  72  PHE A O     
518  C  CB    . PHE A 72  ? 1.14170 1.38830 1.31380 0.06050  -0.24100 0.28420  72  PHE A CB    
519  C  CG    . PHE A 72  ? 1.07670 1.29980 1.18610 0.04390  -0.25490 0.30590  72  PHE A CG    
520  C  CD1   . PHE A 72  ? 1.03060 1.21490 1.08980 0.02320  -0.23430 0.30530  72  PHE A CD1   
521  C  CD2   . PHE A 72  ? 1.14380 1.38420 1.24420 0.04850  -0.28790 0.32690  72  PHE A CD2   
522  C  CE1   . PHE A 72  ? 1.12660 1.28900 1.12560 0.00670  -0.24280 0.32350  72  PHE A CE1   
523  C  CE2   . PHE A 72  ? 1.12510 1.34040 1.16020 0.03090  -0.29930 0.34640  72  PHE A CE2   
524  C  CZ    . PHE A 72  ? 1.17140 1.34700 1.15470 0.00970  -0.27500 0.34400  72  PHE A CZ    
525  N  N     . TYR A 73  ? 1.16720 1.43060 1.47100 0.12420  -0.23420 0.26790  73  TYR A N     
526  C  CA    . TYR A 73  ? 1.12380 1.40810 1.48510 0.14320  -0.21890 0.24620  73  TYR A CA    
527  C  C     . TYR A 73  ? 1.08270 1.43570 1.49910 0.15680  -0.23430 0.24160  73  TYR A C     
528  O  O     . TYR A 73  ? 1.15180 1.52910 1.57110 0.16180  -0.26390 0.26100  73  TYR A O     
529  C  CB    . TYR A 73  ? 1.18180 1.41770 1.56000 0.16990  -0.21450 0.25180  73  TYR A CB    
530  C  CG    . TYR A 73  ? 1.12350 1.29530 1.45640 0.15520  -0.19610 0.25220  73  TYR A CG    
531  C  CD1   . TYR A 73  ? 1.08650 1.25110 1.41860 0.14240  -0.16760 0.22670  73  TYR A CD1   
532  C  CD2   . TYR A 73  ? 1.14050 1.26050 1.43200 0.15260  -0.20770 0.27860  73  TYR A CD2   
533  C  CE1   . TYR A 73  ? 1.13180 1.24420 1.42790 0.12790  -0.15250 0.22660  73  TYR A CE1   
534  C  CE2   . TYR A 73  ? 1.14560 1.21220 1.40050 0.13670  -0.18980 0.27820  73  TYR A CE2   
535  C  CZ    . TYR A 73  ? 1.17120 1.23650 1.43110 0.12470  -0.16290 0.25180  73  TYR A CZ    
536  O  OH    . TYR A 73  ? 1.20000 1.21850 1.42860 0.10780  -0.14670 0.25090  73  TYR A OH    
537  N  N     . CYS A 74  ? 1.03410 1.41970 1.49370 0.16090  -0.21340 0.21530  74  CYS A N     
538  C  CA    . CYS A 74  ? 1.01910 1.47360 1.54260 0.17590  -0.22230 0.20750  74  CYS A CA    
539  C  C     . CYS A 74  ? 1.08230 1.53800 1.64980 0.21480  -0.24390 0.22500  74  CYS A C     
540  O  O     . CYS A 74  ? 1.02130 1.52710 1.62300 0.22570  -0.27110 0.23700  74  CYS A O     
541  C  CB    . CYS A 74  ? 1.00370 1.48250 1.56090 0.17410  -0.19040 0.17600  74  CYS A CB    
542  S  SG    . CYS A 74  ? 0.89950 1.37890 1.41090 0.13140  -0.16650 0.15580  74  CYS A SG    
543  N  N     . ASN A 75  ? 1.09210 1.49190 1.65990 0.23610  -0.23340 0.22650  75  ASN A N     
544  C  CA    . ASN A 75  ? 1.09940 1.49190 1.71230 0.27700  -0.24990 0.24010  75  ASN A CA    
545  C  C     . ASN A 75  ? 1.17140 1.47750 1.75190 0.28730  -0.24020 0.24750  75  ASN A C     
546  O  O     . ASN A 75  ? 1.23810 1.49790 1.76260 0.26090  -0.22460 0.24480  75  ASN A O     
547  C  CB    . ASN A 75  ? 1.06990 1.51950 1.76120 0.30070  -0.23570 0.21600  75  ASN A CB    
548  C  CG    . ASN A 75  ? 1.05220 1.49210 1.73990 0.28710  -0.19430 0.18230  75  ASN A CG    
549  O  OD1   . ASN A 75  ? 1.10300 1.47710 1.75660 0.28520  -0.17670 0.17720  75  ASN A OD1   
550  N  ND2   . ASN A 75  ? 1.01970 1.52480 1.73940 0.27460  -0.17980 0.16010  75  ASN A ND2   
551  N  N     . VAL A 76  ? 1.15780 1.44190 1.77590 0.32600  -0.24970 0.25650  76  VAL A N     
552  C  CA    . VAL A 76  ? 1.11330 1.31020 1.70060 0.33560  -0.24240 0.26460  76  VAL A CA    
553  C  C     . VAL A 76  ? 1.12760 1.29940 1.71550 0.32920  -0.20360 0.23150  76  VAL A C     
554  O  O     . VAL A 76  ? 1.14800 1.24950 1.69430 0.31980  -0.19150 0.23240  76  VAL A O     
555  C  CB    . VAL A 76  ? 1.04410 1.21860 1.66990 0.38040  -0.26520 0.28470  76  VAL A CB    
556  C  CG1   . VAL A 76  ? 1.11340 1.30870 1.73090 0.38470  -0.30750 0.32070  76  VAL A CG1   
557  C  CG2   . VAL A 76  ? 1.00890 1.23060 1.71650 0.41520  -0.25300 0.26040  76  VAL A CG2   
558  N  N     . GLU A 77  ? 1.19450 1.42340 1.82870 0.33320  -0.18400 0.20230  77  GLU A N     
559  C  CA    . GLU A 77  ? 1.18560 1.39570 1.81740 0.32520  -0.14760 0.16950  77  GLU A CA    
560  C  C     . GLU A 77  ? 1.16490 1.35560 1.73510 0.28180  -0.13310 0.16290  77  GLU A C     
561  O  O     . GLU A 77  ? 1.18320 1.31730 1.72140 0.27180  -0.11520 0.15310  77  GLU A O     
562  C  CB    . GLU A 77  ? 1.15450 1.43450 1.84930 0.33880  -0.13060 0.14200  77  GLU A CB    
563  C  CG    . GLU A 77  ? 1.29760 1.58300 2.05760 0.38710  -0.13530 0.14120  77  GLU A CG    
564  C  CD    . GLU A 77  ? 1.44490 1.82270 2.27480 0.40460  -0.14810 0.14100  77  GLU A CD    
565  O  OE1   . GLU A 77  ? 1.52590 1.96460 2.35630 0.37680  -0.14470 0.13280  77  GLU A OE1   
566  O  OE2   . GLU A 77  ? 1.31890 1.70830 2.20470 0.44600  -0.16260 0.14960  77  GLU A OE2   
567  N  N     . CYS A 78  ? 1.14310 1.38160 1.69870 0.25600  -0.14030 0.16630  78  CYS A N     
568  C  CA    . CYS A 78  ? 1.15090 1.37000 1.64920 0.21800  -0.12970 0.16330  78  CYS A CA    
569  C  C     . CYS A 78  ? 1.19610 1.34660 1.64410 0.21000  -0.13800 0.18520  78  CYS A C     
570  O  O     . CYS A 78  ? 1.18590 1.29830 1.59730 0.18910  -0.12140 0.17710  78  CYS A O     
571  C  CB    . CYS A 78  ? 1.09860 1.37280 1.58730 0.19490  -0.14030 0.16740  78  CYS A CB    
572  S  SG    . CYS A 78  ? 0.96290 1.30800 1.48370 0.18110  -0.12050 0.13710  78  CYS A SG    
573  N  N     . GLN A 79  ? 1.22550 1.36150 1.67080 0.22490  -0.16450 0.21400  79  GLN A N     
574  C  CA    . GLN A 79  ? 1.20370 1.27360 1.60010 0.21650  -0.17230 0.23730  79  GLN A CA    
575  C  C     . GLN A 79  ? 1.20320 1.20960 1.59740 0.22530  -0.15490 0.22750  79  GLN A C     
576  O  O     . GLN A 79  ? 1.17810 1.13850 1.53010 0.20250  -0.14400 0.22870  79  GLN A O     
577  C  CB    . GLN A 79  ? 1.14220 1.20900 1.53640 0.23270  -0.20540 0.27080  79  GLN A CB    
578  C  CG    . GLN A 79  ? 1.21550 1.21660 1.55330 0.22060  -0.21500 0.29900  79  GLN A CG    
579  C  CD    . GLN A 79  ? 1.20010 1.20360 1.52780 0.23220  -0.24990 0.33320  79  GLN A CD    
580  O  OE1   . GLN A 79  ? 1.10480 1.16550 1.46700 0.24620  -0.26860 0.33550  79  GLN A OE1   
581  N  NE2   . GLN A 79  ? 1.19360 1.13680 1.47210 0.22400  -0.25920 0.36060  79  GLN A NE2   
582  N  N     . LYS A 80  ? 1.22650 1.23150 1.66780 0.25770  -0.15100 0.21570  80  LYS A N     
583  C  CA    . LYS A 80  ? 1.19100 1.13130 1.62840 0.26630  -0.13440 0.20390  80  LYS A CA    
584  C  C     . LYS A 80  ? 1.20050 1.13880 1.61750 0.23820  -0.10630 0.17540  80  LYS A C     
585  O  O     . LYS A 80  ? 1.23840 1.11990 1.62100 0.22210  -0.09640 0.17360  80  LYS A O     
586  C  CB    . LYS A 80  ? 1.07990 1.02190 1.57380 0.30850  -0.13300 0.19300  80  LYS A CB    
587  C  CG    . LYS A 80  ? 1.02450 0.92970 1.53040 0.34060  -0.15950 0.22290  80  LYS A CG    
588  C  CD    . LYS A 80  ? 1.06960 1.00050 1.64510 0.38620  -0.16050 0.21180  80  LYS A CD    
589  C  CE    . LYS A 80  ? 1.17510 1.06790 1.76480 0.42170  -0.19000 0.24350  80  LYS A CE    
590  N  NZ    . LYS A 80  ? 1.10920 0.90170 1.67100 0.43010  -0.18440 0.24860  80  LYS A NZ    
591  N  N     . GLU A 81  ? 1.19610 1.19600 1.63360 0.23080  -0.09420 0.15350  81  GLU A N     
592  C  CA    . GLU A 81  ? 1.19040 1.18840 1.60630 0.20460  -0.07000 0.12820  81  GLU A CA    
593  C  C     . GLU A 81  ? 1.20120 1.18200 1.56660 0.17000  -0.07180 0.13960  81  GLU A C     
594  O  O     . GLU A 81  ? 1.19260 1.14900 1.53390 0.14970  -0.05610 0.12510  81  GLU A O     
595  C  CB    . GLU A 81  ? 1.18480 1.25110 1.62640 0.19990  -0.05830 0.10670  81  GLU A CB    
596  C  CG    . GLU A 81  ? 1.22140 1.31860 1.71580 0.22800  -0.04790 0.08730  81  GLU A CG    
597  C  CD    . GLU A 81  ? 1.33430 1.38230 1.82670 0.23650  -0.02600 0.06440  81  GLU A CD    
598  O  OE1   . GLU A 81  ? 1.33530 1.35230 1.78720 0.21020  -0.01310 0.05330  81  GLU A OE1   
599  O  OE2   . GLU A 81  ? 1.37160 1.41470 1.90350 0.26900  -0.02130 0.05570  81  GLU A OE2   
600  N  N     . ASP A 82  ? 1.20060 1.19500 1.54950 0.16260  -0.09050 0.16460  82  ASP A N     
601  C  CA    . ASP A 82  ? 1.18960 1.17210 1.49370 0.13100  -0.08890 0.17320  82  ASP A CA    
602  C  C     . ASP A 82  ? 1.22980 1.14930 1.50320 0.12550  -0.09400 0.19340  82  ASP A C     
603  O  O     . ASP A 82  ? 1.22400 1.13010 1.46310 0.09900  -0.08910 0.19900  82  ASP A O     
604  C  CB    . ASP A 82  ? 1.19630 1.22530 1.49020 0.11970  -0.10160 0.18550  82  ASP A CB    
605  C  CG    . ASP A 82  ? 1.15840 1.18550 1.41280 0.08800  -0.09320 0.18530  82  ASP A CG    
606  O  OD1   . ASP A 82  ? 1.12850 1.15010 1.37870 0.07480  -0.07580 0.16610  82  ASP A OD1   
607  O  OD2   . ASP A 82  ? 1.14140 1.17280 1.36910 0.07660  -0.10370 0.20370  82  ASP A OD2   
608  N  N     . TRP A 83  ? 1.10690 0.98720 1.39340 0.14970  -0.10260 0.20390  83  TRP A N     
609  C  CA    . TRP A 83  ? 1.02850 0.84490 1.28280 0.14290  -0.10870 0.22620  83  TRP A CA    
610  C  C     . TRP A 83  ? 0.99430 0.76930 1.22430 0.11820  -0.09060 0.21420  83  TRP A C     
611  O  O     . TRP A 83  ? 1.01230 0.75940 1.20770 0.09600  -0.09220 0.23190  83  TRP A O     
612  C  CB    . TRP A 83  ? 1.08870 0.86360 1.36300 0.17600  -0.12080 0.23800  83  TRP A CB    
613  C  CG    . TRP A 83  ? 1.19140 0.89390 1.42940 0.16690  -0.12610 0.26120  83  TRP A CG    
614  C  CD1   . TRP A 83  ? 1.26900 0.90460 1.50090 0.16870  -0.11700 0.25540  83  TRP A CD1   
615  C  CD2   . TRP A 83  ? 1.22380 0.91070 1.42390 0.15290  -0.14140 0.29420  83  TRP A CD2   
616  N  NE1   . TRP A 83  ? 1.36280 0.94230 1.55620 0.15490  -0.12560 0.28380  83  TRP A NE1   
617  C  CE2   . TRP A 83  ? 1.29260 0.90310 1.46540 0.14540  -0.14000 0.30840  83  TRP A CE2   
618  C  CE3   . TRP A 83  ? 1.15370 0.88180 1.33670 0.14410  -0.15530 0.31250  83  TRP A CE3   
619  C  CZ2   . TRP A 83  ? 1.29580 0.87200 1.42520 0.12890  -0.15090 0.34120  83  TRP A CZ2   
620  C  CZ3   . TRP A 83  ? 1.24290 0.93660 1.38090 0.12880  -0.16610 0.34370  83  TRP A CZ3   
621  C  CH2   . TRP A 83  ? 1.30670 0.92610 1.41850 0.12110  -0.16320 0.35840  83  TRP A CH2   
622  N  N     . PRO A 84  ? 1.02340 0.79410 1.26780 0.11820  -0.07360 0.18520  84  PRO A N     
623  C  CA    . PRO A 84  ? 1.04480 0.77960 1.26420 0.09090  -0.06010 0.17510  84  PRO A CA    
624  C  C     . PRO A 84  ? 1.00910 0.77200 1.20420 0.05920  -0.05700 0.18030  84  PRO A C     
625  O  O     . PRO A 84  ? 1.05260 0.78420 1.22470 0.03570  -0.05210 0.18530  84  PRO A O     
626  C  CB    . PRO A 84  ? 1.08060 0.82160 1.31880 0.09660  -0.04420 0.14130  84  PRO A CB    
627  C  CG    . PRO A 84  ? 1.19480 0.94560 1.46820 0.13270  -0.04800 0.13710  84  PRO A CG    
628  C  CD    . PRO A 84  ? 1.15610 0.94920 1.43850 0.14240  -0.06570 0.16050  84  PRO A CD    
629  N  N     . MET A 85  ? 0.99000 0.81090 1.19110 0.05760  -0.05910 0.17850  85  MET A N     
630  C  CA    . MET A 85  ? 0.88800 0.73360 1.06700 0.03120  -0.05580 0.18360  85  MET A CA    
631  C  C     . MET A 85  ? 0.90510 0.75050 1.06300 0.02790  -0.06780 0.21210  85  MET A C     
632  O  O     . MET A 85  ? 0.94060 0.77690 1.07320 0.00530  -0.06350 0.22280  85  MET A O     
633  C  CB    . MET A 85  ? 0.89330 0.79430 1.08370 0.02810  -0.05020 0.16520  85  MET A CB    
634  C  CG    . MET A 85  ? 0.94890 0.84990 1.15090 0.02600  -0.03740 0.13780  85  MET A CG    
635  S  SD    . MET A 85  ? 0.96580 0.83590 1.14680 -0.00290 -0.02820 0.13220  85  MET A SD    
636  C  CE    . MET A 85  ? 0.91370 0.80520 1.10190 -0.00790 -0.01710 0.10100  85  MET A CE    
637  N  N     . HIS A 86  ? 0.91680 0.77460 1.08490 0.04950  -0.08290 0.22430  86  HIS A N     
638  C  CA    . HIS A 86  ? 0.96790 0.82780 1.11090 0.04560  -0.09650 0.25130  86  HIS A CA    
639  C  C     . HIS A 86  ? 0.96770 0.76980 1.08140 0.03620  -0.09870 0.27440  86  HIS A C     
640  O  O     . HIS A 86  ? 1.04330 0.84350 1.12400 0.01870  -0.10040 0.29290  86  HIS A O     
641  C  CB    . HIS A 86  ? 1.09430 0.97790 1.25690 0.07180  -0.11590 0.26040  86  HIS A CB    
642  C  CG    . HIS A 86  ? 1.08170 0.96570 1.21400 0.06780  -0.13330 0.28880  86  HIS A CG    
643  N  ND1   . HIS A 86  ? 1.07430 0.98020 1.17450 0.04390  -0.12940 0.29290  86  HIS A ND1   
644  C  CD2   . HIS A 86  ? 1.08410 0.94790 1.21080 0.08470  -0.15500 0.31450  86  HIS A CD2   
645  C  CE1   . HIS A 86  ? 0.99680 0.89520 1.06880 0.04410  -0.14690 0.31880  86  HIS A CE1   
646  N  NE2   . HIS A 86  ? 1.00000 0.87340 1.08710 0.06840  -0.16420 0.33360  86  HIS A NE2   
647  N  N     . LYS A 87  ? 0.96420 0.71660 1.08680 0.04560  -0.09710 0.27310  87  LYS A N     
648  C  CA    . LYS A 87  ? 1.01430 0.70630 1.10730 0.03450  -0.09920 0.29620  87  LYS A CA    
649  C  C     . LYS A 87  ? 1.05350 0.74190 1.12110 -0.00150 -0.08320 0.29600  87  LYS A C     
650  O  O     . LYS A 87  ? 1.14270 0.79240 1.17990 -0.01760 -0.08340 0.31830  87  LYS A O     
651  C  CB    . LYS A 87  ? 1.02500 0.65980 1.13210 0.05010  -0.09880 0.29100  87  LYS A CB    
652  C  CG    . LYS A 87  ? 1.02050 0.64850 1.13950 0.03690  -0.08030 0.26170  87  LYS A CG    
653  C  CD    . LYS A 87  ? 1.05600 0.62320 1.18520 0.05270  -0.07930 0.25400  87  LYS A CD    
654  C  CE    . LYS A 87  ? 1.19900 0.75620 1.33190 0.03440  -0.06200 0.22500  87  LYS A CE    
655  N  NZ    . LYS A 87  ? 1.25480 0.75330 1.39670 0.05080  -0.05900 0.21160  87  LYS A NZ    
656  N  N     . LEU A 88  ? 0.96230 0.69080 1.04270 -0.01450 -0.06950 0.27200  88  LEU A N     
657  C  CA    . LEU A 88  ? 0.97360 0.71130 1.03760 -0.04600 -0.05520 0.27130  88  LEU A CA    
658  C  C     . LEU A 88  ? 1.03880 0.79660 1.07410 -0.05780 -0.05630 0.29110  88  LEU A C     
659  O  O     . LEU A 88  ? 1.01840 0.77080 1.03470 -0.08320 -0.04470 0.29880  88  LEU A O     
660  C  CB    . LEU A 88  ? 0.88620 0.66580 0.97160 -0.05260 -0.04410 0.24290  88  LEU A CB    
661  C  CG    . LEU A 88  ? 0.92770 0.68910 1.03510 -0.04530 -0.04080 0.22040  88  LEU A CG    
662  C  CD1   . LEU A 88  ? 0.85890 0.66230 0.98090 -0.05350 -0.03200 0.19570  88  LEU A CD1   
663  C  CD2   . LEU A 88  ? 1.14990 0.85540 1.24740 -0.06040 -0.03690 0.22530  88  LEU A CD2   
664  N  N     . GLU A 89  ? 1.03280 0.81480 1.06450 -0.04100 -0.06960 0.29850  89  GLU A N     
665  C  CA    . GLU A 89  ? 1.01420 0.81910 1.01540 -0.05250 -0.07040 0.31250  89  GLU A CA    
666  C  C     . GLU A 89  ? 1.09110 0.87440 1.06670 -0.04130 -0.09020 0.34050  89  GLU A C     
667  O  O     . GLU A 89  ? 1.16400 0.94650 1.10110 -0.05690 -0.08940 0.35790  89  GLU A O     
668  C  CB    . GLU A 89  ? 0.98970 0.85220 1.00430 -0.04880 -0.06850 0.29310  89  GLU A CB    
669  C  CG    . GLU A 89  ? 1.04300 0.92910 1.07890 -0.05990 -0.05110 0.26760  89  GLU A CG    
670  C  CD    . GLU A 89  ? 0.99790 0.93310 1.04550 -0.05510 -0.05030 0.24940  89  GLU A CD    
671  O  OE1   . GLU A 89  ? 1.01810 0.97020 1.07140 -0.03900 -0.06400 0.25010  89  GLU A OE1   
672  O  OE2   . GLU A 89  ? 0.81880 0.77540 0.87160 -0.06750 -0.03690 0.23460  89  GLU A OE2   
673  N  N     . CYS A 90  ? 1.19170 0.95760 1.18700 -0.01460 -0.10770 0.34530  90  CYS A N     
674  C  CA    . CYS A 90  ? 1.23320 0.98430 1.20980 0.00050  -0.13150 0.37240  90  CYS A CA    
675  C  C     . CYS A 90  ? 1.28700 0.99290 1.21230 -0.01950 -0.13190 0.40250  90  CYS A C     
676  O  O     . CYS A 90  ? 1.30090 1.01900 1.18850 -0.03030 -0.13800 0.41860  90  CYS A O     
677  C  CB    . CYS A 90  ? 1.25540 0.98280 1.26610 0.03280  -0.14670 0.37330  90  CYS A CB    
678  S  SG    . CYS A 90  ? 1.29950 1.02150 1.30250 0.05910  -0.18130 0.40410  90  CYS A SG    
679  N  N     A SER A 91  ? 1.24720 0.89850 1.16750 -0.02710 -0.12430 0.40980  91  SER A N     
680  C  CA    A SER A 91  ? 1.34430 0.94760 1.21500 -0.04900 -0.12270 0.43960  91  SER A CA    
681  C  C     A SER A 91  ? 1.32120 0.94800 1.16540 -0.08410 -0.09880 0.43560  91  SER A C     
682  O  O     A SER A 91  ? 1.35220 0.96900 1.14830 -0.10040 -0.09970 0.45870  91  SER A O     
683  C  CB    A SER A 91  ? 1.35330 0.88760 1.22680 -0.04830 -0.12160 0.44810  91  SER A CB    
684  O  OG    A SER A 91  ? 1.41430 0.89930 1.23760 -0.07200 -0.11950 0.47840  91  SER A OG    
685  N  N     . PRO A 92  ? 1.23690 0.89170 1.10800 -0.09760 -0.07690 0.40880  92  PRO A N     
686  C  CA    . PRO A 92  ? 1.15910 0.84270 1.01080 -0.12720 -0.05430 0.40470  92  PRO A CA    
687  C  C     . PRO A 92  ? 1.17250 0.89580 0.99860 -0.12730 -0.05730 0.40710  92  PRO A C     
688  O  O     . PRO A 92  ? 1.23420 0.95990 1.02250 -0.15050 -0.04360 0.41760  92  PRO A O     
689  C  CB    . PRO A 92  ? 1.10460 0.82180 1.00110 -0.13050 -0.03850 0.37250  92  PRO A CB    
690  C  CG    . PRO A 92  ? 1.24710 0.92770 1.17070 -0.11650 -0.04660 0.36670  92  PRO A CG    
691  C  CD    . PRO A 92  ? 1.27410 0.93160 1.19180 -0.08800 -0.07120 0.38240  92  PRO A CD    
692  N  N     . MET A 93  ? 1.17500 0.92830 1.01870 -0.10340 -0.07440 0.39750  93  MET A N     
693  C  CA    . MET A 93  ? 1.11400 0.90360 0.93200 -0.10540 -0.07850 0.39750  93  MET A CA    
694  C  C     . MET A 93  ? 1.14220 0.90160 0.90210 -0.11420 -0.09040 0.42990  93  MET A C     
695  O  O     . MET A 93  ? 1.16970 0.93980 0.88830 -0.13510 -0.07780 0.43390  93  MET A O     
696  C  CB    . MET A 93  ? 1.01950 0.84310 0.87130 -0.07910 -0.09700 0.38270  93  MET A CB    
697  C  CG    . MET A 93  ? 1.00070 0.86490 0.89290 -0.07800 -0.08170 0.34970  93  MET A CG    
698  S  SD    . MET A 93  ? 1.21710 1.13040 1.13620 -0.05760 -0.09750 0.33200  93  MET A SD    
699  C  CE    . MET A 93  ? 1.15450 1.07650 1.01890 -0.06800 -0.10930 0.34990  93  MET A CE    
700  N  N     . VAL A 94  ? 1.12420 0.83970 0.87740 -0.10030 -0.11210 0.45390  94  VAL A N     
701  C  CA    . VAL A 94  ? 1.27130 0.95350 0.96560 -0.10780 -0.12740 0.48810  94  VAL A CA    
702  C  C     . VAL A 94  ? 1.26490 0.90690 0.91810 -0.13900 -0.10560 0.50480  94  VAL A C     
703  O  O     . VAL A 94  ? 1.30290 0.93570 0.90120 -0.15480 -0.10210 0.51860  94  VAL A O     
704  C  CB    . VAL A 94  ? 1.30350 0.95310 1.00560 -0.07910 -0.16160 0.51020  94  VAL A CB    
705  C  CG1   . VAL A 94  ? 1.27070 0.96910 1.00200 -0.05350 -0.18470 0.49900  94  VAL A CG1   
706  C  CG2   . VAL A 94  ? 1.37610 0.98750 1.11830 -0.06570 -0.15900 0.50650  94  VAL A CG2   
707  N  N     . VAL A 95  ? 1.22920 0.85140 0.91100 -0.14710 -0.08780 0.49600  95  VAL A N     
708  C  CA    . VAL A 95  ? 1.30330 0.89280 0.95320 -0.17770 -0.06490 0.50760  95  VAL A CA    
709  C  C     . VAL A 95  ? 1.29870 0.93230 0.93390 -0.20390 -0.03530 0.49300  95  VAL A C     
710  O  O     . VAL A 95  ? 1.33940 0.96510 0.93030 -0.22230 -0.01990 0.50020  95  VAL A O     
711  C  CB    . VAL A 95  ? 1.29930 0.85580 0.98490 -0.18200 -0.05610 0.50240  95  VAL A CB    
712  C  CG1   . VAL A 95  ? 1.31660 0.85510 0.97950 -0.21410 -0.02740 0.50400  95  VAL A CG1   
713  C  CG2   . VAL A 95  ? 1.34080 0.84430 1.03390 -0.15560 -0.08200 0.51650  95  VAL A CG2   
714  N  N     . PHE A 96  ? 1.24440 0.92890 0.92260 -0.19990 -0.02390 0.46380  96  PHE A N     
715  C  CA    . PHE A 96  ? 1.25740 0.98500 0.92810 -0.22000 0.00420  0.44770  96  PHE A CA    
716  C  C     . PHE A 96  ? 1.36680 1.11390 0.99120 -0.22010 -0.00100 0.45170  96  PHE A C     
717  O  O     . PHE A 96  ? 1.38620 1.14990 0.98050 -0.24140 0.02350  0.44820  96  PHE A O     
718  C  CB    . PHE A 96  ? 1.17730 0.95140 0.90890 -0.21030 0.01460  0.41300  96  PHE A CB    
719  C  CG    . PHE A 96  ? 1.19490 0.96210 0.96290 -0.22390 0.03100  0.40510  96  PHE A CG    
720  C  CD1   . PHE A 96  ? 1.25310 1.03300 1.01640 -0.25240 0.05980  0.40420  96  PHE A CD1   
721  C  CD2   . PHE A 96  ? 1.16780 0.91730 0.97550 -0.20870 0.01770  0.39740  96  PHE A CD2   
722  C  CE1   . PHE A 96  ? 1.25870 1.03580 1.05820 -0.26690 0.07230  0.39720  96  PHE A CE1   
723  C  CE2   . PHE A 96  ? 1.12840 0.86990 0.96630 -0.22340 0.03050  0.38940  96  PHE A CE2   
724  C  CZ    . PHE A 96  ? 1.12750 0.88390 0.96230 -0.25310 0.05640  0.38980  96  PHE A CZ    
725  N  N     . GLY A 97  ? 1.36580 1.11180 0.98400 -0.19710 -0.03170 0.45780  97  GLY A N     
726  C  CA    . GLY A 97  ? 1.37270 1.13360 0.94150 -0.20040 -0.03980 0.46290  97  GLY A CA    
727  C  C     . GLY A 97  ? 1.35100 1.16430 0.93750 -0.20240 -0.02060 0.43040  97  GLY A C     
728  O  O     . GLY A 97  ? 1.27340 1.11630 0.91390 -0.18570 -0.02240 0.40620  97  GLY A O     
729  N  N     . GLU A 98  ? 1.51120 1.33280 1.04850 -0.22320 -0.00140 0.42970  98  GLU A N     
730  C  CA    . GLU A 98  ? 1.46930 1.33420 1.01750 -0.22530 0.01900  0.39920  98  GLU A CA    
731  C  C     . GLU A 98  ? 1.42110 1.30770 1.02140 -0.22970 0.04820  0.37860  98  GLU A C     
732  O  O     . GLU A 98  ? 1.37870 1.30110 1.00870 -0.22250 0.05890  0.35140  98  GLU A O     
733  C  CB    . GLU A 98  ? 1.51590 1.38030 0.99540 -0.24540 0.03380  0.40180  98  GLU A CB    
734  C  CG    . GLU A 98  ? 1.74810 1.63830 1.21080 -0.23860 0.02430  0.38380  98  GLU A CG    
735  C  CD    . GLU A 98  ? 1.86700 1.75210 1.26400 -0.25440 0.03860  0.37950  98  GLU A CD    
736  O  OE1   . GLU A 98  ? 1.84970 1.70840 1.21150 -0.26500 0.04690  0.39370  98  GLU A OE1   
737  O  OE2   . GLU A 98  ? 1.90050 1.80720 1.28340 -0.25510 0.04280  0.35910  98  GLU A OE2   
738  N  N     . ASN A 99  ? 1.27870 1.14360 0.89130 -0.24160 0.05950  0.39130  99  ASN A N     
739  C  CA    . ASN A 99  ? 1.29450 1.18350 0.95820 -0.24790 0.08480  0.37280  99  ASN A CA    
740  C  C     . ASN A 99  ? 1.25630 1.16020 0.98420 -0.22610 0.07080  0.35490  99  ASN A C     
741  O  O     . ASN A 99  ? 1.19580 1.12510 0.96830 -0.22880 0.08770  0.33700  99  ASN A O     
742  C  CB    . ASN A 99  ? 1.26250 1.12210 0.91970 -0.27050 0.09860  0.39270  99  ASN A CB    
743  C  CG    . ASN A 99  ? 1.39570 1.24120 0.99620 -0.28890 0.11690  0.40330  99  ASN A CG    
744  O  OD1   . ASN A 99  ? 1.49500 1.36670 1.07400 -0.29350 0.13530  0.38970  99  ASN A OD1   
745  N  ND2   . ASN A 99  ? 1.45410 1.25590 1.03110 -0.29610 0.11170  0.42460  99  ASN A ND2   
746  N  N     . TRP A 100 ? 1.23510 1.12650 0.96950 -0.20500 0.04100  0.35890  100 TRP A N     
747  C  CA    . TRP A 100 ? 1.11180 1.01840 0.90250 -0.18520 0.03000  0.34030  100 TRP A CA    
748  C  C     . TRP A 100 ? 1.06460 1.01430 0.87420 -0.17630 0.03560  0.31340  100 TRP A C     
749  O  O     . TRP A 100 ? 1.07970 1.03870 0.87050 -0.16660 0.02180  0.31080  100 TRP A O     
750  C  CB    . TRP A 100 ? 1.07790 0.96000 0.87100 -0.16500 -0.00090 0.35280  100 TRP A CB    
751  C  CG    . TRP A 100 ? 1.10270 0.99160 0.94960 -0.14730 -0.00920 0.33620  100 TRP A CG    
752  C  CD1   . TRP A 100 ? 1.09190 0.95650 0.96550 -0.14810 -0.00760 0.33710  100 TRP A CD1   
753  C  CD2   . TRP A 100 ? 1.00730 0.92820 0.88420 -0.12890 -0.01850 0.31510  100 TRP A CD2   
754  N  NE1   . TRP A 100 ? 0.90660 0.78570 0.82270 -0.13040 -0.01530 0.31730  100 TRP A NE1   
755  C  CE2   . TRP A 100 ? 0.94930 0.86380 0.86880 -0.11870 -0.02150 0.30430  100 TRP A CE2   
756  C  CE3   . TRP A 100 ? 0.97990 0.93190 0.84920 -0.12230 -0.02420 0.30400  100 TRP A CE3   
757  C  CZ2   . TRP A 100 ? 0.98720 0.92680 0.94040 -0.10210 -0.02850 0.28380  100 TRP A CZ2   
758  C  CZ3   . TRP A 100 ? 0.95890 0.93540 0.86430 -0.10660 -0.03190 0.28440  100 TRP A CZ3   
759  C  CH2   . TRP A 100 ? 0.93890 0.91000 0.88530 -0.09660 -0.03340 0.27490  100 TRP A CH2   
760  N  N     . ASN A 101 ? 1.03100 1.00610 0.87770 -0.18000 0.05440  0.29410  101 ASN A N     
761  C  CA    . ASN A 101 ? 1.01820 1.02860 0.88240 -0.17100 0.05990  0.26960  101 ASN A CA    
762  C  C     . ASN A 101 ? 0.96910 0.99940 0.88730 -0.16610 0.06580  0.25130  101 ASN A C     
763  O  O     . ASN A 101 ? 1.01010 1.06720 0.94360 -0.16930 0.08340  0.23630  101 ASN A O     
764  C  CB    . ASN A 101 ? 1.06310 1.08820 0.89480 -0.18300 0.08190  0.26470  101 ASN A CB    
765  C  CG    . ASN A 101 ? 1.12300 1.15580 0.96350 -0.20090 0.10980  0.26610  101 ASN A CG    
766  O  OD1   . ASN A 101 ? 1.11700 1.13590 0.97410 -0.20980 0.11080  0.27760  101 ASN A OD1   
767  N  ND2   . ASN A 101 ? 1.20690 1.26200 1.03690 -0.20690 0.13360  0.25380  101 ASN A ND2   
768  N  N     . PRO A 102 ? 0.89640 0.91430 0.84340 -0.15800 0.05140  0.25140  102 PRO A N     
769  C  CA    . PRO A 102 ? 0.74370 0.78000 0.73590 -0.15450 0.05450  0.23360  102 PRO A CA    
770  C  C     . PRO A 102 ? 0.77600 0.83730 0.78080 -0.14040 0.04990  0.21410  102 PRO A C     
771  O  O     . PRO A 102 ? 0.77460 0.83410 0.76450 -0.12960 0.03650  0.21350  102 PRO A O     
772  C  CB    . PRO A 102 ? 0.80680 0.81590 0.81500 -0.14940 0.03940  0.23890  102 PRO A CB    
773  C  CG    . PRO A 102 ? 0.90490 0.89340 0.88660 -0.13820 0.02260  0.25190  102 PRO A CG    
774  C  CD    . PRO A 102 ? 0.97330 0.96010 0.91280 -0.14890 0.03030  0.26590  102 PRO A CD    
775  N  N     . SER A 103 ? 0.81390 0.89910 0.84690 -0.14150 0.06030  0.19920  103 SER A N     
776  C  CA    . SER A 103 ? 0.66480 0.76800 0.70870 -0.12920 0.05550  0.18190  103 SER A CA    
777  C  C     . SER A 103 ? 0.64960 0.74360 0.70780 -0.11860 0.03710  0.17750  103 SER A C     
778  O  O     . SER A 103 ? 0.68000 0.75640 0.74850 -0.11990 0.03060  0.18370  103 SER A O     
779  C  CB    . SER A 103 ? 0.65810 0.78590 0.73160 -0.13080 0.06760  0.16910  103 SER A CB    
780  O  OG    . SER A 103 ? 0.75870 0.88660 0.86390 -0.13380 0.06190  0.16710  103 SER A OG    
781  N  N     . GLU A 104 ? 0.66900 0.77360 0.72670 -0.10870 0.03030  0.16580  104 GLU A N     
782  C  CA    . GLU A 104 ? 0.66120 0.76140 0.73130 -0.09910 0.01590  0.16010  104 GLU A CA    
783  C  C     . GLU A 104 ? 0.67330 0.77180 0.77120 -0.10050 0.01530  0.15250  104 GLU A C     
784  O  O     . GLU A 104 ? 0.69280 0.77800 0.79950 -0.09600 0.00680  0.15150  104 GLU A O     
785  C  CB    . GLU A 104 ? 0.65850 0.77220 0.72190 -0.09240 0.01120  0.14890  104 GLU A CB    
786  C  CG    . GLU A 104 ? 0.77770 0.89090 0.85070 -0.08360 -0.00180 0.14460  104 GLU A CG    
787  C  CD    . GLU A 104 ? 0.77710 0.90290 0.83680 -0.08080 -0.00780 0.13930  104 GLU A CD    
788  O  OE1   . GLU A 104 ? 0.70270 0.82870 0.73940 -0.08310 -0.01020 0.14740  104 GLU A OE1   
789  O  OE2   . GLU A 104 ? 0.79660 0.93150 0.86640 -0.07820 -0.01050 0.12740  104 GLU A OE2   
790  N  N     . THR A 105 ? 0.63130 0.74350 0.74330 -0.10650 0.02400  0.14650  105 THR A N     
791  C  CA    . THR A 105 ? 0.57680 0.68900 0.71310 -0.11080 0.02130  0.14030  105 THR A CA    
792  C  C     . THR A 105 ? 0.63680 0.72800 0.77720 -0.11930 0.02050  0.14960  105 THR A C     
793  O  O     . THR A 105 ? 0.63570 0.71280 0.78530 -0.11950 0.01300  0.14430  105 THR A O     
794  C  CB    . THR A 105 ? 0.53170 0.66660 0.68570 -0.11540 0.02940  0.13530  105 THR A CB    
795  O  OG1   . THR A 105 ? 0.72490 0.87160 0.87450 -0.10620 0.02860  0.12590  105 THR A OG1   
796  C  CG2   . THR A 105 ? 0.62700 0.76440 0.80600 -0.12260 0.02370  0.13050  105 THR A CG2   
797  N  N     . VAL A 106 ? 0.64630 0.73110 0.77550 -0.12730 0.02870  0.16330  106 VAL A N     
798  C  CA    . VAL A 106 ? 0.64470 0.70300 0.77340 -0.13710 0.02810  0.17430  106 VAL A CA    
799  C  C     . VAL A 106 ? 0.69720 0.72650 0.81510 -0.12580 0.01590  0.17780  106 VAL A C     
800  O  O     . VAL A 106 ? 0.69330 0.69840 0.81940 -0.12780 0.01090  0.17630  106 VAL A O     
801  C  CB    . VAL A 106 ? 0.61060 0.66730 0.72430 -0.14970 0.04090  0.18990  106 VAL A CB    
802  C  CG1   . VAL A 106 ? 0.72390 0.74530 0.83030 -0.16050 0.03920  0.20400  106 VAL A CG1   
803  C  CG2   . VAL A 106 ? 0.76050 0.84980 0.89400 -0.16030 0.05550  0.18460  106 VAL A CG2   
804  N  N     . ARG A 107 ? 0.66430 0.69590 0.76510 -0.11350 0.01060  0.18180  107 ARG A N     
805  C  CA    . ARG A 107 ? 0.62540 0.63680 0.72260 -0.09950 -0.00170 0.18510  107 ARG A CA    
806  C  C     . ARG A 107 ? 0.67070 0.68180 0.78830 -0.09160 -0.00650 0.16790  107 ARG A C     
807  O  O     . ARG A 107 ? 0.78030 0.76460 0.90410 -0.08690 -0.01110 0.16740  107 ARG A O     
808  C  CB    . ARG A 107 ? 0.64600 0.67180 0.72700 -0.08910 -0.00800 0.18930  107 ARG A CB    
809  C  CG    . ARG A 107 ? 0.73920 0.76190 0.79170 -0.09730 -0.00400 0.20610  107 ARG A CG    
810  C  CD    . ARG A 107 ? 0.76400 0.79930 0.79730 -0.08900 -0.01330 0.20970  107 ARG A CD    
811  N  NE    . ARG A 107 ? 0.80290 0.82620 0.84030 -0.07430 -0.03010 0.21750  107 ARG A NE    
812  C  CZ    . ARG A 107 ? 0.75820 0.79970 0.79540 -0.06360 -0.04230 0.21510  107 ARG A CZ    
813  N  NH1   . ARG A 107 ? 0.66120 0.72890 0.68980 -0.06780 -0.03980 0.20480  107 ARG A NH1   
814  N  NH2   . ARG A 107 ? 0.81780 0.85130 0.86580 -0.04830 -0.05760 0.22290  107 ARG A NH2   
815  N  N     . LEU A 108 ? 0.60670 0.64380 0.73230 -0.09170 -0.00430 0.15330  108 LEU A N     
816  C  CA    . LEU A 108 ? 0.58060 0.61840 0.71910 -0.08660 -0.00780 0.13690  108 LEU A CA    
817  C  C     . LEU A 108 ? 0.64010 0.65840 0.78790 -0.09710 -0.00650 0.13190  108 LEU A C     
818  O  O     . LEU A 108 ? 0.74490 0.74430 0.89680 -0.09220 -0.00950 0.12300  108 LEU A O     
819  C  CB    . LEU A 108 ? 0.53880 0.60440 0.67830 -0.08660 -0.00640 0.12530  108 LEU A CB    
820  C  CG    . LEU A 108 ? 0.55480 0.62190 0.70090 -0.08320 -0.00910 0.10900  108 LEU A CG    
821  C  CD1   . LEU A 108 ? 0.63160 0.69110 0.78030 -0.07030 -0.01240 0.10630  108 LEU A CD1   
822  C  CD2   . LEU A 108 ? 0.59600 0.68540 0.73800 -0.08420 -0.00860 0.10100  108 LEU A CD2   
823  N  N     . THR A 109 ? 0.61290 0.63740 0.76510 -0.11220 -0.00160 0.13590  109 THR A N     
824  C  CA    . THR A 109 ? 0.62190 0.63080 0.78380 -0.12580 -0.00220 0.13100  109 THR A CA    
825  C  C     . THR A 109 ? 0.64890 0.61690 0.80480 -0.12700 -0.00350 0.13850  109 THR A C     
826  O  O     . THR A 109 ? 0.65470 0.59830 0.81320 -0.13140 -0.00640 0.12880  109 THR A O     
827  C  CB    . THR A 109 ? 0.65270 0.68270 0.82600 -0.14200 0.00360  0.13590  109 THR A CB    
828  O  OG1   . THR A 109 ? 0.67400 0.73760 0.85420 -0.13750 0.00380  0.12850  109 THR A OG1   
829  C  CG2   . THR A 109 ? 0.70790 0.72620 0.89340 -0.15910 0.00070  0.13070  109 THR A CG2   
830  N  N     . ALA A 110 ? 0.61110 0.56730 0.75540 -0.12360 -0.00180 0.15580  110 ALA A N     
831  C  CA    . ALA A 110 ? 0.63190 0.54380 0.76820 -0.12190 -0.00470 0.16540  110 ALA A CA    
832  C  C     . ALA A 110 ? 0.71650 0.61070 0.85610 -0.10230 -0.01110 0.15410  110 ALA A C     
833  O  O     . ALA A 110 ? 0.80190 0.65860 0.94230 -0.10260 -0.01230 0.14890  110 ALA A O     
834  C  CB    . ALA A 110 ? 0.74240 0.64570 0.86110 -0.12020 -0.00410 0.18790  110 ALA A CB    
835  N  N     . ARG A 111 ? 0.69970 0.62190 0.84270 -0.08640 -0.01360 0.14760  111 ARG A N     
836  C  CA    . ARG A 111 ? 0.69980 0.61210 0.85070 -0.06780 -0.01690 0.13570  111 ARG A CA    
837  C  C     . ARG A 111 ? 0.74150 0.65060 0.89800 -0.07360 -0.01340 0.11330  111 ARG A C     
838  O  O     . ARG A 111 ? 0.79370 0.67750 0.95360 -0.06390 -0.01260 0.10220  111 ARG A O     
839  C  CB    . ARG A 111 ? 0.68300 0.62970 0.83790 -0.05210 -0.02030 0.13540  111 ARG A CB    
840  C  CG    . ARG A 111 ? 0.71910 0.66330 0.86660 -0.04250 -0.02770 0.15650  111 ARG A CG    
841  C  CD    . ARG A 111 ? 0.78230 0.76470 0.93240 -0.03250 -0.03240 0.15570  111 ARG A CD    
842  N  NE    . ARG A 111 ? 0.75230 0.73600 0.88840 -0.02910 -0.04080 0.17650  111 ARG A NE    
843  C  CZ    . ARG A 111 ? 0.87060 0.85970 1.01420 -0.01130 -0.05240 0.18370  111 ARG A CZ    
844  N  NH1   . ARG A 111 ? 0.89750 0.89400 1.06650 0.00560  -0.05420 0.17110  111 ARG A NH1   
845  N  NH2   . ARG A 111 ? 0.94030 0.93050 1.06580 -0.01070 -0.06230 0.20350  111 ARG A NH2   
846  N  N     . ILE A 112 ? 0.71770 0.64960 0.87370 -0.08940 -0.01150 0.10670  112 ILE A N     
847  C  CA    . ILE A 112 ? 0.69790 0.62450 0.85360 -0.09880 -0.01090 0.08770  112 ILE A CA    
848  C  C     . ILE A 112 ? 0.74870 0.63260 0.90090 -0.11010 -0.01110 0.08530  112 ILE A C     
849  O  O     . ILE A 112 ? 0.82460 0.68400 0.97210 -0.10840 -0.00990 0.06870  112 ILE A O     
850  C  CB    . ILE A 112 ? 0.64540 0.60520 0.80270 -0.11250 -0.01230 0.08500  112 ILE A CB    
851  C  CG1   . ILE A 112 ? 0.65820 0.65150 0.81470 -0.10160 -0.01180 0.08320  112 ILE A CG1   
852  C  CG2   . ILE A 112 ? 0.73910 0.69000 0.89260 -0.12590 -0.01530 0.06880  112 ILE A CG2   
853  C  CD1   . ILE A 112 ? 0.60860 0.63070 0.76710 -0.11110 -0.01340 0.08400  112 ILE A CD1   
854  N  N     . LEU A 113 ? 0.71800 0.59180 0.87050 -0.12430 -0.01130 0.10050  113 LEU A N     
855  C  CA    . LEU A 113 ? 0.70930 0.53920 0.85710 -0.13870 -0.01160 0.09960  113 LEU A CA    
856  C  C     . LEU A 113 ? 0.84170 0.62500 0.98340 -0.12130 -0.01100 0.09840  113 LEU A C     
857  O  O     . LEU A 113 ? 0.98310 0.72710 1.11840 -0.12610 -0.01030 0.08470  113 LEU A O     
858  C  CB    . LEU A 113 ? 0.66280 0.49220 0.81240 -0.15780 -0.00990 0.11860  113 LEU A CB    
859  C  CG    . LEU A 113 ? 0.63130 0.50370 0.79360 -0.17670 -0.00950 0.11810  113 LEU A CG    
860  C  CD1   . LEU A 113 ? 0.70160 0.58250 0.86760 -0.19060 -0.00330 0.13820  113 LEU A CD1   
861  C  CD2   . LEU A 113 ? 0.64900 0.51050 0.81430 -0.19650 -0.01460 0.10240  113 LEU A CD2   
862  N  N     . ALA A 114 ? 0.79380 0.57990 0.93720 -0.10050 -0.01190 0.11230  114 ALA A N     
863  C  CA    . ALA A 114 ? 0.87230 0.61790 1.01560 -0.07920 -0.01300 0.11200  114 ALA A CA    
864  C  C     . ALA A 114 ? 0.94090 0.68720 1.09030 -0.06480 -0.00890 0.08640  114 ALA A C     
865  O  O     . ALA A 114 ? 0.97460 0.67600 1.12120 -0.05820 -0.00590 0.07470  114 ALA A O     
866  C  CB    . ALA A 114 ? 0.90370 0.66130 1.05010 -0.05910 -0.01820 0.13240  114 ALA A CB    
867  N  N     . LYS A 115 ? 0.94010 0.73420 1.09550 -0.06110 -0.00710 0.07650  115 LYS A N     
868  C  CA    . LYS A 115 ? 0.96000 0.75880 1.11870 -0.04990 -0.00070 0.05250  115 LYS A CA    
869  C  C     . LYS A 115 ? 1.03560 0.80520 1.17920 -0.06830 0.00280  0.03260  115 LYS A C     
870  O  O     . LYS A 115 ? 1.11720 0.86220 1.25730 -0.05920 0.01010  0.01270  115 LYS A O     
871  C  CB    . LYS A 115 ? 0.87620 0.73010 1.03950 -0.04830 0.00010  0.04880  115 LYS A CB    
872  C  CG    . LYS A 115 ? 0.90270 0.77200 1.06810 -0.03920 0.00850  0.02620  115 LYS A CG    
873  C  CD    . LYS A 115 ? 0.95750 0.82150 1.14210 -0.01140 0.01300  0.02290  115 LYS A CD    
874  C  CE    . LYS A 115 ? 0.90350 0.78650 1.09220 -0.00380 0.02520  -0.00090 115 LYS A CE    
875  N  NZ    . LYS A 115 ? 0.85490 0.77440 1.07090 0.01890  0.02680  0.00240  115 LYS A NZ    
876  N  N     . GLN A 116 ? 1.06020 0.83410 1.19510 -0.09450 -0.00200 0.03640  116 GLN A N     
877  C  CA    . GLN A 116 ? 1.07530 0.82070 1.19470 -0.11460 -0.00200 0.01830  116 GLN A CA    
878  C  C     . GLN A 116 ? 1.12370 0.80660 1.23630 -0.11570 -0.00020 0.01690  116 GLN A C     
879  O  O     . GLN A 116 ? 1.16160 0.80850 1.25920 -0.12160 0.00350  -0.00450 116 GLN A O     
880  C  CB    . GLN A 116 ? 1.04140 0.81040 1.15910 -0.14240 -0.00990 0.02380  116 GLN A CB    
881  C  CG    . GLN A 116 ? 1.03930 0.85770 1.15760 -0.14490 -0.01280 0.01950  116 GLN A CG    
882  C  CD    . GLN A 116 ? 1.12670 0.96990 1.25020 -0.16860 -0.02200 0.02660  116 GLN A CD    
883  O  OE1   . GLN A 116 ? 1.14330 0.97870 1.27590 -0.18180 -0.02400 0.03950  116 GLN A OE1   
884  N  NE2   . GLN A 116 ? 1.10590 0.98310 1.22660 -0.17270 -0.02710 0.02090  116 GLN A NE2   
885  N  N     . LYS A 117 ? 1.06280 0.72790 1.18210 -0.11170 -0.00290 0.03970  117 LYS A N     
886  C  CA    . LYS A 117 ? 1.11150 0.71030 1.22170 -0.11370 -0.00210 0.04110  117 LYS A CA    
887  C  C     . LYS A 117 ? 1.09300 0.65760 1.20460 -0.08470 0.00480  0.02610  117 LYS A C     
888  O  O     . LYS A 117 ? 1.09470 0.60470 1.19280 -0.08850 0.00900  0.00940  117 LYS A O     
889  C  CB    . LYS A 117 ? 1.18280 0.76610 1.29500 -0.11670 -0.00650 0.07100  117 LYS A CB    
890  C  CG    . LYS A 117 ? 1.27220 0.77750 1.37180 -0.11780 -0.00600 0.07290  117 LYS A CG    
891  C  CD    . LYS A 117 ? 1.32340 0.79400 1.40750 -0.14960 -0.00530 0.05580  117 LYS A CD    
892  C  CE    . LYS A 117 ? 1.32170 0.70950 1.39030 -0.15400 -0.00470 0.05890  117 LYS A CE    
893  N  NZ    . LYS A 117 ? 1.27640 0.64630 1.34210 -0.16470 -0.00840 0.09090  117 LYS A NZ    
894  N  N     . ILE A 118 ? 1.12180 0.72000 1.25080 -0.05620 0.00670  0.02950  118 ILE A N     
895  C  CA    . ILE A 118 ? 1.15290 0.72570 1.29160 -0.02550 0.01400  0.01610  118 ILE A CA    
896  C  C     . ILE A 118 ? 1.16140 0.75150 1.29710 -0.02240 0.02580  -0.01550 118 ILE A C     
897  O  O     . ILE A 118 ? 1.19690 0.75020 1.33170 -0.00680 0.03610  -0.03580 118 ILE A O     
898  C  CB    . ILE A 118 ? 1.10000 0.70050 1.26280 0.00400  0.00890  0.03650  118 ILE A CB    
899  C  CG1   . ILE A 118 ? 1.06160 0.73540 1.23610 0.00570  0.00890  0.03600  118 ILE A CG1   
900  C  CG2   . ILE A 118 ? 1.08910 0.67000 1.24660 -0.00210 -0.00270 0.06880  118 ILE A CG2   
901  C  CD1   . ILE A 118 ? 0.95050 0.65610 1.14630 0.02920  0.00130  0.05630  118 ILE A CD1   
902  N  N     . HIS A 119 ? 1.21330 0.85520 1.34480 -0.03690 0.02550  -0.02050 119 HIS A N     
903  C  CA    . HIS A 119 ? 1.21100 0.87250 1.33570 -0.03520 0.03680  -0.04750 119 HIS A CA    
904  C  C     . HIS A 119 ? 1.19970 0.86770 1.29790 -0.06860 0.03250  -0.05680 119 HIS A C     
905  O  O     . HIS A 119 ? 1.15950 0.87510 1.25580 -0.07740 0.02950  -0.05490 119 HIS A O     
906  C  CB    . HIS A 119 ? 1.17420 0.89440 1.32000 -0.01660 0.04080  -0.04520 119 HIS A CB    
907  C  CG    . HIS A 119 ? 1.24040 0.96800 1.38410 -0.00660 0.05750  -0.07340 119 HIS A CG    
908  N  ND1   . HIS A 119 ? 1.22770 0.94340 1.34040 -0.02740 0.06430  -0.09650 119 HIS A ND1   
909  C  CD2   . HIS A 119 ? 1.27230 1.01850 1.44090 0.02100  0.06950  -0.08280 119 HIS A CD2   
910  C  CE1   . HIS A 119 ? 1.26250 0.98730 1.37710 -0.01400 0.08190  -0.11920 119 HIS A CE1   
911  N  NE2   . HIS A 119 ? 1.31360 1.05910 1.46500 0.01580  0.08620  -0.11190 119 HIS A NE2   
912  N  N     . PRO A 120 ? 1.12010 0.73930 1.19730 -0.08840 0.03030  -0.06630 120 PRO A N     
913  C  CA    . PRO A 120 ? 1.06630 0.69440 1.12160 -0.12170 0.02170  -0.07230 120 PRO A CA    
914  C  C     . PRO A 120 ? 1.11170 0.75570 1.14510 -0.12710 0.02820  -0.09660 120 PRO A C     
915  O  O     . PRO A 120 ? 1.14380 0.81250 1.16280 -0.14990 0.01830  -0.09670 120 PRO A O     
916  C  CB    . PRO A 120 ? 1.04570 0.61210 1.08500 -0.14030 0.01840  -0.07800 120 PRO A CB    
917  C  CG    . PRO A 120 ? 1.29240 0.81000 1.33290 -0.11460 0.03160  -0.09030 120 PRO A CG    
918  C  CD    . PRO A 120 ? 1.23870 0.79050 1.31050 -0.08140 0.03510  -0.07380 120 PRO A CD    
919  N  N     . GLU A 121 ? 1.11340 0.74400 1.14340 -0.10700 0.04480  -0.11680 121 GLU A N     
920  C  CA    . GLU A 121 ? 1.14530 0.78910 1.14940 -0.11430 0.05380  -0.14030 121 GLU A CA    
921  C  C     . GLU A 121 ? 1.13130 0.83760 1.14820 -0.10690 0.05430  -0.13000 121 GLU A C     
922  O  O     . GLU A 121 ? 1.08600 0.82440 1.13280 -0.09370 0.04890  -0.10740 121 GLU A O     
923  C  CB    . GLU A 121 ? 1.21240 0.81980 1.20850 -0.09620 0.07530  -0.16830 121 GLU A CB    
924  C  CG    . GLU A 121 ? 1.39140 0.92810 1.37400 -0.10020 0.07680  -0.18020 121 GLU A CG    
925  C  CD    . GLU A 121 ? 1.62650 1.12350 1.57510 -0.10230 0.09520  -0.21730 121 GLU A CD    
926  O  OE1   . GLU A 121 ? 1.68880 1.20870 1.64160 -0.08400 0.11410  -0.23270 121 GLU A OE1   
927  O  OE2   . GLU A 121 ? 1.68210 1.12600 1.59850 -0.12420 0.09150  -0.23210 121 GLU A OE2   
928  N  N     . ARG A 122 ? 1.21980 0.93970 1.20930 -0.11730 0.06110  -0.14740 122 ARG A N     
929  C  CA    . ARG A 122 ? 1.17930 0.95210 1.17310 -0.11580 0.06130  -0.13890 122 ARG A CA    
930  C  C     . ARG A 122 ? 1.16830 0.96750 1.19720 -0.08630 0.07520  -0.13570 122 ARG A C     
931  O  O     . ARG A 122 ? 1.20130 0.98350 1.23730 -0.06880 0.09300  -0.15370 122 ARG A O     
932  C  CB    . ARG A 122 ? 1.19870 0.97200 1.15000 -0.13380 0.06780  -0.15930 122 ARG A CB    
933  C  CG    . ARG A 122 ? 1.19940 1.02030 1.14750 -0.13750 0.06620  -0.14920 122 ARG A CG    
934  C  CD    . ARG A 122 ? 1.25440 1.06930 1.15260 -0.15860 0.07050  -0.16680 122 ARG A CD    
935  N  NE    . ARG A 122 ? 1.35280 1.14710 1.21900 -0.18490 0.04980  -0.16570 122 ARG A NE    
936  C  CZ    . ARG A 122 ? 1.25510 1.07200 1.11710 -0.19870 0.02820  -0.14660 122 ARG A CZ    
937  N  NH1   . ARG A 122 ? 1.14280 0.99810 1.02530 -0.18990 0.02530  -0.12780 122 ARG A NH1   
938  N  NH2   . ARG A 122 ? 1.25210 1.05240 1.08970 -0.22180 0.00840  -0.14680 122 ARG A NH2   
939  N  N     . THR A 123 ? 1.10180 0.94310 1.15430 -0.08040 0.06670  -0.11330 123 THR A N     
940  C  CA    . THR A 123 ? 0.98300 0.85620 1.07010 -0.05550 0.07570  -0.10790 123 THR A CA    
941  C  C     . THR A 123 ? 0.94600 0.85670 1.02450 -0.05960 0.08710  -0.11740 123 THR A C     
942  O  O     . THR A 123 ? 1.03420 0.94650 1.07860 -0.08160 0.08470  -0.12240 123 THR A O     
943  C  CB    . THR A 123 ? 0.88730 0.78240 1.00010 -0.04940 0.06010  -0.07910 123 THR A CB    
944  O  OG1   . THR A 123 ? 0.79860 0.71770 0.89660 -0.06860 0.04850  -0.06730 123 THR A OG1   
945  C  CG2   . THR A 123 ? 1.01820 0.87430 1.13640 -0.04790 0.05050  -0.06850 123 THR A CG2   
946  N  N     . PRO A 124 ? 0.86370 0.80590 0.97290 -0.03970 0.09920  -0.11940 124 PRO A N     
947  C  CA    . PRO A 124 ? 0.81320 0.79500 0.91610 -0.04710 0.10980  -0.12520 124 PRO A CA    
948  C  C     . PRO A 124 ? 0.93200 0.93950 1.02590 -0.06260 0.09380  -0.10470 124 PRO A C     
949  O  O     . PRO A 124 ? 0.94090 0.96950 1.01640 -0.07600 0.09970  -0.10840 124 PRO A O     
950  C  CB    . PRO A 124 ? 0.79340 0.80740 0.94210 -0.02100 0.12260  -0.12830 124 PRO A CB    
951  C  CG    . PRO A 124 ? 0.84170 0.83900 1.02040 -0.00050 0.11010  -0.11350 124 PRO A CG    
952  C  CD    . PRO A 124 ? 0.85800 0.80000 1.00830 -0.01020 0.10450  -0.11810 124 PRO A CD    
953  N  N     . SER A 125 ? 0.91140 0.91560 1.01630 -0.06130 0.07510  -0.08330 125 SER A N     
954  C  CA    . SER A 125 ? 0.77440 0.79740 0.87000 -0.07460 0.06070  -0.06540 125 SER A CA    
955  C  C     . SER A 125 ? 0.80930 0.81320 0.86700 -0.09730 0.05230  -0.06760 125 SER A C     
956  O  O     . SER A 125 ? 0.89000 0.90830 0.93740 -0.10800 0.04190  -0.05540 125 SER A O     
957  C  CB    . SER A 125 ? 0.75710 0.78240 0.87590 -0.06560 0.04640  -0.04390 125 SER A CB    
958  O  OG    . SER A 125 ? 0.77890 0.82050 0.93070 -0.04440 0.05040  -0.04000 125 SER A OG    
959  N  N     . GLU A 126 ? 0.80890 0.77980 0.84560 -0.10460 0.05560  -0.08290 126 GLU A N     
960  C  CA    . GLU A 126 ? 0.83300 0.78480 0.83610 -0.12650 0.04310  -0.08400 126 GLU A CA    
961  C  C     . GLU A 126 ? 0.98080 0.91920 0.94500 -0.13930 0.05490  -0.10570 126 GLU A C     
962  O  O     . GLU A 126 ? 1.07290 0.98010 1.00970 -0.15230 0.05180  -0.11800 126 GLU A O     
963  C  CB    . GLU A 126 ? 0.87540 0.79670 0.88310 -0.12950 0.03320  -0.08220 126 GLU A CB    
964  C  CG    . GLU A 126 ? 0.90440 0.83480 0.94590 -0.11900 0.02390  -0.06110 126 GLU A CG    
965  C  CD    . GLU A 126 ? 0.95290 0.84830 0.99950 -0.12120 0.01950  -0.06160 126 GLU A CD    
966  O  OE1   . GLU A 126 ? 1.00680 0.87610 1.05750 -0.10970 0.03080  -0.07400 126 GLU A OE1   
967  O  OE2   . GLU A 126 ? 0.96940 0.86310 1.01730 -0.13460 0.00540  -0.05000 126 GLU A OE2   
968  N  N     . LYS A 127 ? 0.94920 0.91070 0.90830 -0.13790 0.06900  -0.11090 127 LYS A N     
969  C  CA    . LYS A 127 ? 0.96300 0.91320 0.88210 -0.15120 0.08410  -0.13190 127 LYS A CA    
970  C  C     . LYS A 127 ? 0.96970 0.90510 0.84130 -0.17640 0.06760  -0.12800 127 LYS A C     
971  O  O     . LYS A 127 ? 1.10140 1.01020 0.93180 -0.19130 0.07180  -0.14540 127 LYS A O     
972  C  CB    . LYS A 127 ? 1.02860 1.01210 0.95660 -0.14640 0.10310  -0.13540 127 LYS A CB    
973  C  CG    . LYS A 127 ? 1.02180 1.02170 0.99510 -0.12150 0.12170  -0.14470 127 LYS A CG    
974  C  CD    . LYS A 127 ? 1.07310 1.11480 1.06270 -0.11870 0.13870  -0.14660 127 LYS A CD    
975  C  CE    . LYS A 127 ? 1.08860 1.16290 1.11450 -0.11000 0.12490  -0.12320 127 LYS A CE    
976  N  NZ    . LYS A 127 ? 0.96120 1.07630 1.03090 -0.09390 0.14030  -0.12730 127 LYS A NZ    
977  N  N     . LEU A 128 ? 0.98520 0.93620 0.86120 -0.18100 0.04800  -0.10580 128 LEU A N     
978  C  CA    . LEU A 128 ? 0.96230 0.90310 0.79940 -0.20150 0.02870  -0.09820 128 LEU A CA    
979  C  C     . LEU A 128 ? 0.90060 0.83830 0.75380 -0.20340 0.00320  -0.08290 128 LEU A C     
980  O  O     . LEU A 128 ? 0.97850 0.90360 0.80230 -0.22030 -0.01480 -0.08090 128 LEU A O     
981  C  CB    . LEU A 128 ? 0.95340 0.91340 0.77750 -0.20660 0.02740  -0.08540 128 LEU A CB    
982  C  CG    . LEU A 128 ? 1.09640 1.05880 0.89220 -0.21410 0.05130  -0.10020 128 LEU A CG    
983  C  CD1   . LEU A 128 ? 1.15060 1.12720 0.93230 -0.22190 0.04810  -0.08520 128 LEU A CD1   
984  C  CD2   . LEU A 128 ? 1.11380 1.04650 0.85630 -0.23280 0.05500  -0.11840 128 LEU A CD2   
985  N  N     . LEU A 129 ? 0.82420 0.77490 0.72280 -0.18760 0.00090  -0.07170 129 LEU A N     
986  C  CA    . LEU A 129 ? 0.85160 0.80510 0.77060 -0.18940 -0.01950 -0.05680 129 LEU A CA    
987  C  C     . LEU A 129 ? 0.93250 0.88240 0.88850 -0.17620 -0.01400 -0.05540 129 LEU A C     
988  O  O     . LEU A 129 ? 0.93390 0.89700 0.91500 -0.15920 -0.00220 -0.05160 129 LEU A O     
989  C  CB    . LEU A 129 ? 0.82470 0.80340 0.75620 -0.18580 -0.03130 -0.03610 129 LEU A CB    
990  C  CG    . LEU A 129 ? 0.84030 0.82910 0.79780 -0.18620 -0.04990 -0.02070 129 LEU A CG    
991  C  CD1   . LEU A 129 ? 0.93440 0.91100 0.87110 -0.20460 -0.06850 -0.02390 129 LEU A CD1   
992  C  CD2   . LEU A 129 ? 0.82100 0.83270 0.79250 -0.17810 -0.05640 -0.00320 129 LEU A CD2   
993  N  N     . ALA A 130 ? 0.96070 0.89200 0.91870 -0.18540 -0.02370 -0.05770 130 ALA A N     
994  C  CA    . ALA A 130 ? 0.98630 0.90750 0.97440 -0.17570 -0.01940 -0.05460 130 ALA A CA    
995  C  C     . ALA A 130 ? 0.96980 0.91290 0.98850 -0.17430 -0.03180 -0.03280 130 ALA A C     
996  O  O     . ALA A 130 ? 0.95470 0.91570 0.97250 -0.18360 -0.04640 -0.02340 130 ALA A O     
997  C  CB    . ALA A 130 ? 1.03980 0.92340 1.01220 -0.18860 -0.02060 -0.07010 130 ALA A CB    
998  N  N     . VAL A 131 ? 0.90960 0.85090 0.95540 -0.16170 -0.02510 -0.02480 131 VAL A N     
999  C  CA    . VAL A 131 ? 0.85830 0.81910 0.93150 -0.16020 -0.03220 -0.00510 131 VAL A CA    
1000 C  C     . VAL A 131 ? 0.89280 0.85260 0.96930 -0.17980 -0.04670 -0.00210 131 VAL A C     
1001 O  O     . VAL A 131 ? 0.88710 0.87450 0.97960 -0.18320 -0.05600 0.01080  131 VAL A O     
1002 C  CB    . VAL A 131 ? 0.83740 0.78780 0.93060 -0.14630 -0.02290 0.00230  131 VAL A CB    
1003 C  CG1   . VAL A 131 ? 0.71310 0.67880 0.82860 -0.14930 -0.02820 0.02120  131 VAL A CG1   
1004 C  CG2   . VAL A 131 ? 0.80960 0.77280 0.90670 -0.12680 -0.01240 0.00230  131 VAL A CG2   
1005 N  N     . LYS A 132 ? 0.88900 0.81780 0.95190 -0.19330 -0.04870 -0.01480 132 LYS A N     
1006 C  CA    . LYS A 132 ? 0.89390 0.82260 0.96100 -0.21540 -0.06380 -0.01340 132 LYS A CA    
1007 C  C     . LYS A 132 ? 0.94010 0.89280 0.99670 -0.22620 -0.08050 -0.01290 132 LYS A C     
1008 O  O     . LYS A 132 ? 0.92190 0.89290 0.99520 -0.24040 -0.09570 -0.00540 132 LYS A O     
1009 C  CB    . LYS A 132 ? 0.98430 0.86840 1.03180 -0.22890 -0.06210 -0.03040 132 LYS A CB    
1010 C  CG    . LYS A 132 ? 1.16590 1.04640 1.22030 -0.25490 -0.07720 -0.02930 132 LYS A CG    
1011 C  CD    . LYS A 132 ? 1.22910 1.05980 1.25470 -0.27060 -0.07610 -0.05000 132 LYS A CD    
1012 C  CE    . LYS A 132 ? 1.23980 1.06800 1.27220 -0.30070 -0.09290 -0.04950 132 LYS A CE    
1013 N  NZ    . LYS A 132 ? 1.29010 1.06270 1.29120 -0.31760 -0.09130 -0.07110 132 LYS A NZ    
1014 N  N     . GLU A 133 ? 0.99950 0.95410 1.03040 -0.22000 -0.07850 -0.01920 133 GLU A N     
1015 C  CA    . GLU A 133 ? 0.97270 0.94540 0.98890 -0.22860 -0.09560 -0.01600 133 GLU A CA    
1016 C  C     . GLU A 133 ? 0.89620 0.90400 0.93600 -0.21500 -0.09910 0.00200  133 GLU A C     
1017 O  O     . GLU A 133 ? 0.89410 0.91540 0.92370 -0.21860 -0.11400 0.00720  133 GLU A O     
1018 C  CB    . GLU A 133 ? 1.03110 0.98460 1.00140 -0.23150 -0.09110 -0.03080 133 GLU A CB    
1019 C  CG    . GLU A 133 ? 1.18280 1.09920 1.12030 -0.24680 -0.08820 -0.05230 133 GLU A CG    
1020 C  CD    . GLU A 133 ? 1.20900 1.10810 1.10240 -0.24670 -0.07590 -0.06810 133 GLU A CD    
1021 O  OE1   . GLU A 133 ? 1.16820 1.06810 1.06720 -0.22950 -0.05500 -0.07150 133 GLU A OE1   
1022 O  OE2   . GLU A 133 ? 1.14730 1.03420 1.00030 -0.26510 -0.08740 -0.07680 133 GLU A OE2   
1023 N  N     . PHE A 134 ? 0.80880 0.82850 0.87650 -0.19970 -0.08660 0.01170  134 PHE A N     
1024 C  CA    . PHE A 134 ? 0.82690 0.87550 0.91370 -0.18680 -0.08760 0.02630  134 PHE A CA    
1025 C  C     . PHE A 134 ? 0.85740 0.93250 0.96690 -0.19310 -0.10550 0.03670  134 PHE A C     
1026 O  O     . PHE A 134 ? 0.90110 0.98140 1.02780 -0.20650 -0.11410 0.03680  134 PHE A O     
1027 C  CB    . PHE A 134 ? 0.78380 0.83890 0.89490 -0.17330 -0.07220 0.03420  134 PHE A CB    
1028 C  CG    . PHE A 134 ? 0.73730 0.78250 0.83470 -0.16000 -0.05750 0.02980  134 PHE A CG    
1029 C  CD1   . PHE A 134 ? 0.82950 0.86580 0.89820 -0.16020 -0.05570 0.02000  134 PHE A CD1   
1030 C  CD2   . PHE A 134 ? 0.80720 0.85470 0.92090 -0.14840 -0.04580 0.03640  134 PHE A CD2   
1031 C  CE1   . PHE A 134 ? 0.83070 0.86490 0.89300 -0.14910 -0.04170 0.01580  134 PHE A CE1   
1032 C  CE2   . PHE A 134 ? 0.89030 0.93450 0.99620 -0.13620 -0.03490 0.03300  134 PHE A CE2   
1033 C  CZ    . PHE A 134 ? 0.80590 0.84580 0.88920 -0.13650 -0.03240 0.02220  134 PHE A CZ    
1034 N  N     . GLU A 135 ? 1.00520 1.09740 1.11630 -0.18290 -0.11120 0.04530  135 GLU A N     
1035 C  CA    . GLU A 135 ? 0.99170 1.11400 1.13310 -0.18150 -0.12590 0.05670  135 GLU A CA    
1036 C  C     . GLU A 135 ? 0.96350 1.10750 1.14500 -0.17370 -0.11340 0.06470  135 GLU A C     
1037 O  O     . GLU A 135 ? 0.94990 1.08870 1.12990 -0.16210 -0.09600 0.06620  135 GLU A O     
1038 C  CB    . GLU A 135 ? 1.05580 1.18320 1.18660 -0.16930 -0.13290 0.06390  135 GLU A CB    
1039 C  CG    . GLU A 135 ? 1.11490 1.25440 1.24740 -0.17430 -0.15880 0.06990  135 GLU A CG    
1040 C  CD    . GLU A 135 ? 1.35980 1.48650 1.46300 -0.16560 -0.16620 0.07530  135 GLU A CD    
1041 O  OE1   . GLU A 135 ? 1.28330 1.41420 1.39620 -0.14880 -0.15820 0.08220  135 GLU A OE1   
1042 O  OE2   . GLU A 135 ? 1.41680 1.52500 1.48200 -0.17760 -0.17960 0.07200  135 GLU A OE2   
1043 N  N     . SER A 136 ? 0.82860 0.99920 1.04540 -0.18110 -0.12250 0.07020  136 SER A N     
1044 C  CA    . SER A 136 ? 0.84160 1.03570 1.09630 -0.17670 -0.10900 0.07780  136 SER A CA    
1045 C  C     . SER A 136 ? 0.76910 1.00040 1.05920 -0.16420 -0.11260 0.08700  136 SER A C     
1046 O  O     . SER A 136 ? 0.72240 0.96670 1.03070 -0.15360 -0.09550 0.09180  136 SER A O     
1047 C  CB    . SER A 136 ? 0.79340 0.99120 1.06730 -0.19710 -0.11030 0.07640  136 SER A CB    
1048 O  OG    . SER A 136 ? 0.80900 1.03350 1.10660 -0.20920 -0.13110 0.07780  136 SER A OG    
1049 N  N     . HIS A 137 ? 0.78840 1.03580 1.08760 -0.16450 -0.13450 0.08940  137 HIS A N     
1050 C  CA    . HIS A 137 ? 0.82850 1.11460 1.17010 -0.15130 -0.14040 0.09790  137 HIS A CA    
1051 C  C     . HIS A 137 ? 0.81050 1.13420 1.20280 -0.15730 -0.12950 0.10130  137 HIS A C     
1052 O  O     . HIS A 137 ? 0.83050 1.18190 1.25580 -0.14230 -0.11770 0.10610  137 HIS A O     
1053 C  CB    . HIS A 137 ? 0.85910 1.13640 1.18980 -0.12770 -0.12900 0.10080  137 HIS A CB    
1054 C  CG    . HIS A 137 ? 0.91060 1.15740 1.19810 -0.12290 -0.14170 0.09990  137 HIS A CG    
1055 N  ND1   . HIS A 137 ? 0.91780 1.14550 1.18340 -0.10690 -0.13220 0.10090  137 HIS A ND1   
1056 C  CD2   . HIS A 137 ? 0.92260 1.15280 1.18080 -0.13470 -0.16230 0.09810  137 HIS A CD2   
1057 C  CE1   . HIS A 137 ? 0.97240 1.17370 1.19900 -0.10940 -0.14590 0.10070  137 HIS A CE1   
1058 N  NE2   . HIS A 137 ? 1.01730 1.21970 1.23720 -0.12570 -0.16390 0.09910  137 HIS A NE2   
1059 N  N     . LEU A 138 ? 0.81620 1.13870 1.21250 -0.18060 -0.13180 0.09800  138 LEU A N     
1060 C  CA    . LEU A 138 ? 0.87140 1.22680 1.31240 -0.19270 -0.12120 0.10150  138 LEU A CA    
1061 C  C     . LEU A 138 ? 0.88520 1.29750 1.38450 -0.18660 -0.13110 0.10760  138 LEU A C     
1062 O  O     . LEU A 138 ? 0.84830 1.29310 1.38600 -0.17920 -0.11230 0.11160  138 LEU A O     
1063 C  CB    . LEU A 138 ? 0.79290 1.13240 1.22470 -0.22170 -0.12910 0.09630  138 LEU A CB    
1064 C  CG    . LEU A 138 ? 0.85010 1.20830 1.31460 -0.24160 -0.11590 0.09940  138 LEU A CG    
1065 C  CD1   . LEU A 138 ? 0.75860 1.10350 1.21460 -0.23170 -0.08630 0.10370  138 LEU A CD1   
1066 C  CD2   . LEU A 138 ? 0.90060 1.22950 1.34510 -0.27020 -0.12610 0.09240  138 LEU A CD2   
1067 N  N     . ASP A 139 ? 0.94360 1.36890 1.44980 -0.18930 -0.16060 0.10830  139 ASP A N     
1068 C  CA    . ASP A 139 ? 0.93510 1.41690 1.50030 -0.18280 -0.17670 0.11480  139 ASP A CA    
1069 C  C     . ASP A 139 ? 0.92400 1.42460 1.51270 -0.15000 -0.16680 0.11990  139 ASP A C     
1070 O  O     . ASP A 139 ? 0.91340 1.46690 1.56250 -0.14070 -0.17100 0.12460  139 ASP A O     
1071 C  CB    . ASP A 139 ? 0.95540 1.43780 1.51040 -0.19220 -0.21450 0.11560  139 ASP A CB    
1072 C  CG    . ASP A 139 ? 1.03940 1.47370 1.53370 -0.17970 -0.22490 0.11470  139 ASP A CG    
1073 O  OD1   . ASP A 139 ? 1.08280 1.47570 1.53480 -0.17310 -0.20350 0.11010  139 ASP A OD1   
1074 O  OD2   . ASP A 139 ? 0.99400 1.43300 1.48270 -0.17760 -0.25510 0.11930  139 ASP A OD2   
1075 N  N     . LYS A 140 ? 0.88920 1.34900 1.43430 -0.13270 -0.15310 0.11810  140 LYS A N     
1076 C  CA    . LYS A 140 ? 0.86360 1.33170 1.42360 -0.10250 -0.14390 0.12110  140 LYS A CA    
1077 C  C     . LYS A 140 ? 0.88030 1.36480 1.46280 -0.09530 -0.10920 0.11890  140 LYS A C     
1078 O  O     . LYS A 140 ? 0.88180 1.38670 1.49300 -0.07180 -0.09890 0.11970  140 LYS A O     
1079 C  CB    . LYS A 140 ? 0.82210 1.23710 1.32190 -0.09010 -0.14730 0.12000  140 LYS A CB    
1080 C  CG    . LYS A 140 ? 0.83020 1.22370 1.29730 -0.09940 -0.17930 0.12210  140 LYS A CG    
1081 C  CD    . LYS A 140 ? 0.77480 1.11960 1.18570 -0.08780 -0.18160 0.12220  140 LYS A CD    
1082 C  CE    . LYS A 140 ? 0.75680 1.07470 1.12340 -0.10350 -0.20760 0.12250  140 LYS A CE    
1083 N  NZ    . LYS A 140 ? 0.86010 1.20410 1.25200 -0.10220 -0.24100 0.13150  140 LYS A NZ    
1084 N  N     . LEU A 141 ? 0.88440 1.35660 1.45080 -0.11450 -0.09080 0.11600  141 LEU A N     
1085 C  CA    . LEU A 141 ? 0.91760 1.39820 1.49300 -0.11060 -0.05780 0.11500  141 LEU A CA    
1086 C  C     . LEU A 141 ? 0.99150 1.53400 1.63610 -0.10710 -0.04780 0.11690  141 LEU A C     
1087 O  O     . LEU A 141 ? 0.91490 1.49460 1.60030 -0.12460 -0.05950 0.11930  141 LEU A O     
1088 C  CB    . LEU A 141 ? 0.88700 1.34280 1.43400 -0.13500 -0.04590 0.11450  141 LEU A CB    
1089 C  CG    . LEU A 141 ? 0.84020 1.23950 1.32540 -0.13900 -0.05260 0.11140  141 LEU A CG    
1090 C  CD1   . LEU A 141 ? 0.83940 1.21900 1.30770 -0.16080 -0.04150 0.11210  141 LEU A CD1   
1091 C  CD2   . LEU A 141 ? 0.85720 1.22890 1.30760 -0.11790 -0.04140 0.10940  141 LEU A CD2   
1092 N  N     . ASP A 142 ? 1.25830 1.81300 1.91690 -0.08490 -0.02570 0.11460  142 ASP A N     
1093 C  CA    . ASP A 142 ? 1.24920 1.86260 1.97190 -0.08030 -0.00720 0.11410  142 ASP A CA    
1094 C  C     . ASP A 142 ? 1.24780 1.86590 1.96560 -0.10310 0.02210  0.11430  142 ASP A C     
1095 O  O     . ASP A 142 ? 1.25460 1.82820 1.91990 -0.11890 0.02590  0.11560  142 ASP A O     
1096 C  CB    . ASP A 142 ? 1.25700 1.87800 1.99480 -0.04630 0.00620  0.10960  142 ASP A CB    
1097 C  CG    . ASP A 142 ? 1.27020 1.84310 1.95000 -0.03780 0.03040  0.10410  142 ASP A CG    
1098 O  OD1   . ASP A 142 ? 1.26920 1.81240 1.90540 -0.05740 0.04100  0.10490  142 ASP A OD1   
1099 O  OD2   . ASP A 142 ? 1.28930 1.85500 1.96920 -0.01120 0.03930  0.09880  142 ASP A OD2   
1100 N  N     . ASN A 143 ? 0.86210 1.53500 1.63560 -0.10490 0.04350  0.11370  143 ASN A N     
1101 C  CA    . ASN A 143 ? 0.83710 1.51590 1.60600 -0.13040 0.07100  0.11590  143 ASN A CA    
1102 C  C     . ASN A 143 ? 0.81590 1.44700 1.52280 -0.12520 0.09620  0.11400  143 ASN A C     
1103 O  O     . ASN A 143 ? 0.88080 1.48450 1.55140 -0.14760 0.10650  0.11900  143 ASN A O     
1104 C  CB    . ASN A 143 ? 0.79450 1.54580 1.63710 -0.13380 0.09190  0.11490  143 ASN A CB    
1105 C  CG    . ASN A 143 ? 0.73580 1.52670 1.62540 -0.14880 0.06640  0.11470  143 ASN A CG    
1106 O  OD1   . ASN A 143 ? 0.71690 1.48260 1.58510 -0.16630 0.03840  0.11830  143 ASN A OD1   
1107 N  ND2   . ASN A 143 ? 0.64820 1.49660 1.59400 -0.14220 0.07670  0.10700  143 ASN A ND2   
1108 N  N     . GLU A 144 ? 0.77210 1.39200 1.46590 -0.09640 0.10570  0.10720  144 GLU A N     
1109 C  CA    . GLU A 144 ? 0.82640 1.40090 1.45850 -0.09240 0.12630  0.10460  144 GLU A CA    
1110 C  C     . GLU A 144 ? 0.84800 1.36460 1.41820 -0.10310 0.10780  0.10920  144 GLU A C     
1111 O  O     . GLU A 144 ? 0.84340 1.33130 1.37160 -0.11770 0.12040  0.11330  144 GLU A O     
1112 C  CB    . GLU A 144 ? 0.87550 1.44200 1.50240 -0.06020 0.13360  0.09500  144 GLU A CB    
1113 C  CG    . GLU A 144 ? 0.94700 1.56890 1.64000 -0.04120 0.14890  0.08830  144 GLU A CG    
1114 C  CD    . GLU A 144 ? 0.98190 1.58400 1.66570 -0.00730 0.15050  0.07870  144 GLU A CD    
1115 O  OE1   . GLU A 144 ? 1.06270 1.61400 1.69780 -0.00060 0.13140  0.07920  144 GLU A OE1   
1116 O  OE2   . GLU A 144 ? 0.89050 1.52680 1.61600 0.01210  0.17200  0.07020  144 GLU A OE2   
1117 N  N     . LYS A 145 ? 0.89970 1.39970 1.46470 -0.09600 0.07760  0.10900  145 LYS A N     
1118 C  CA    . LYS A 145 ? 0.85880 1.30880 1.37140 -0.10460 0.06040  0.11150  145 LYS A CA    
1119 C  C     . LYS A 145 ? 0.83200 1.27720 1.34190 -0.13300 0.05790  0.11800  145 LYS A C     
1120 O  O     . LYS A 145 ? 0.78400 1.19010 1.24940 -0.14230 0.06120  0.12110  145 LYS A O     
1121 C  CB    . LYS A 145 ? 1.00720 1.44520 1.51720 -0.09320 0.03090  0.10940  145 LYS A CB    
1122 C  CG    . LYS A 145 ? 1.06890 1.49020 1.56190 -0.06700 0.03220  0.10410  145 LYS A CG    
1123 C  CD    . LYS A 145 ? 1.02570 1.43650 1.51750 -0.05680 0.00330  0.10440  145 LYS A CD    
1124 C  CE    . LYS A 145 ? 0.80150 1.18350 1.26560 -0.03430 0.00520  0.10000  145 LYS A CE    
1125 N  NZ    . LYS A 145 ? 0.69950 1.04680 1.11450 -0.03660 0.02320  0.09620  145 LYS A NZ    
1126 N  N     . LYS A 146 ? 0.89510 1.37930 1.45360 -0.14680 0.05080  0.12010  146 LYS A N     
1127 C  CA    . LYS A 146 ? 0.73340 1.21200 1.29180 -0.17640 0.04880  0.12560  146 LYS A CA    
1128 C  C     . LYS A 146 ? 0.70120 1.16860 1.23900 -0.18880 0.07720  0.13150  146 LYS A C     
1129 O  O     . LYS A 146 ? 0.74680 1.17730 1.25160 -0.20620 0.07620  0.13710  146 LYS A O     
1130 C  CB    . LYS A 146 ? 0.70400 1.23650 1.32550 -0.19010 0.04030  0.12640  146 LYS A CB    
1131 C  CG    . LYS A 146 ? 0.77040 1.31300 1.41000 -0.18540 0.00680  0.12330  146 LYS A CG    
1132 C  CD    . LYS A 146 ? 0.78560 1.38340 1.48760 -0.20490 -0.00250 0.12520  146 LYS A CD    
1133 C  CE    . LYS A 146 ? 0.70260 1.31520 1.42360 -0.19940 -0.03840 0.12330  146 LYS A CE    
1134 N  NZ    . LYS A 146 ? 0.66790 1.22750 1.33660 -0.21270 -0.06090 0.12090  146 LYS A NZ    
1135 N  N     . ASP A 147 ? 0.69640 1.19390 1.25230 -0.18030 0.10290  0.13030  147 ASP A N     
1136 C  CA    . ASP A 147 ? 0.71140 1.19970 1.24400 -0.19420 0.13110  0.13670  147 ASP A CA    
1137 C  C     . ASP A 147 ? 0.73590 1.16950 1.20150 -0.18580 0.13350  0.13870  147 ASP A C     
1138 O  O     . ASP A 147 ? 0.77590 1.18200 1.20740 -0.20200 0.14370  0.14790  147 ASP A O     
1139 C  CB    . ASP A 147 ? 0.79070 1.32790 1.35950 -0.18680 0.16010  0.13240  147 ASP A CB    
1140 C  CG    . ASP A 147 ? 0.90100 1.49970 1.54120 -0.20070 0.16260  0.13270  147 ASP A CG    
1141 O  OD1   . ASP A 147 ? 0.87290 1.47080 1.52430 -0.22580 0.14850  0.13880  147 ASP A OD1   
1142 O  OD2   . ASP A 147 ? 0.95400 1.60270 1.64060 -0.18680 0.17920  0.12600  147 ASP A OD2   
1143 N  N     . LEU A 148 ? 0.75790 1.17430 1.20400 -0.16180 0.12230  0.13130  148 LEU A N     
1144 C  CA    . LEU A 148 ? 0.73820 1.10600 1.12490 -0.15560 0.11980  0.13290  148 LEU A CA    
1145 C  C     . LEU A 148 ? 0.69050 1.02130 1.05360 -0.16760 0.10020  0.13880  148 LEU A C     
1146 O  O     . LEU A 148 ? 0.77490 1.07150 1.09790 -0.17370 0.10340  0.14630  148 LEU A O     
1147 C  CB    . LEU A 148 ? 0.75800 1.11800 1.13330 -0.13030 0.11190  0.12300  148 LEU A CB    
1148 C  CG    . LEU A 148 ? 0.73380 1.11370 1.11560 -0.11550 0.13450  0.11570  148 LEU A CG    
1149 C  CD1   . LEU A 148 ? 0.69580 1.06330 1.06930 -0.09190 0.12320  0.10610  148 LEU A CD1   
1150 C  CD2   . LEU A 148 ? 0.74890 1.11040 1.08730 -0.12310 0.15670  0.11930  148 LEU A CD2   
1151 N  N     . ILE A 149 ? 0.64750 0.98360 1.03390 -0.17020 0.07910  0.13530  149 ILE A N     
1152 C  CA    . ILE A 149 ? 0.64840 0.94960 1.01520 -0.18210 0.06250  0.13810  149 ILE A CA    
1153 C  C     . ILE A 149 ? 0.69140 0.98350 1.05710 -0.20640 0.07290  0.14840  149 ILE A C     
1154 O  O     . ILE A 149 ? 0.78870 1.03910 1.12190 -0.21290 0.06880  0.15410  149 ILE A O     
1155 C  CB    . ILE A 149 ? 0.62860 0.93920 1.01810 -0.18250 0.03930  0.13080  149 ILE A CB    
1156 C  CG1   . ILE A 149 ? 0.77780 1.08110 1.15230 -0.15970 0.02810  0.12320  149 ILE A CG1   
1157 C  CG2   . ILE A 149 ? 0.63920 0.91560 1.01220 -0.19900 0.02610  0.13170  149 ILE A CG2   
1158 C  CD1   . ILE A 149 ? 0.69610 1.00610 1.08530 -0.15960 0.00480  0.11740  149 ILE A CD1   
1159 N  N     . GLN A 150 ? 0.68930 1.02030 1.09380 -0.22090 0.08530  0.15100  150 GLN A N     
1160 C  CA    . GLN A 150 ? 0.67470 0.99730 1.07770 -0.24760 0.09750  0.16190  150 GLN A CA    
1161 C  C     . GLN A 150 ? 0.75450 1.04870 1.11330 -0.24750 0.11570  0.17220  150 GLN A C     
1162 O  O     . GLN A 150 ? 0.79480 1.05210 1.12730 -0.26380 0.11670  0.18340  150 GLN A O     
1163 C  CB    . GLN A 150 ? 0.55920 0.93740 1.01610 -0.26360 0.11060  0.16210  150 GLN A CB    
1164 C  CG    . GLN A 150 ? 0.67530 1.06900 1.16860 -0.28130 0.09120  0.15870  150 GLN A CG    
1165 C  CD    . GLN A 150 ? 0.73160 1.06990 1.19140 -0.29920 0.07830  0.16310  150 GLN A CD    
1166 O  OE1   . GLN A 150 ? 0.72070 1.03900 1.17420 -0.29660 0.05510  0.15560  150 GLN A OE1   
1167 N  NE2   . GLN A 150 ? 0.75000 1.06010 1.18540 -0.31740 0.09410  0.17520  150 GLN A NE2   
1168 N  N     . SER A 151 ? 0.80810 1.11420 1.15430 -0.22920 0.12830  0.16880  151 SER A N     
1169 C  CA    . SER A 151 ? 0.83540 1.11200 1.13230 -0.22840 0.14150  0.17810  151 SER A CA    
1170 C  C     . SER A 151 ? 0.91410 1.13970 1.16910 -0.22020 0.12230  0.18220  151 SER A C     
1171 O  O     . SER A 151 ? 0.93230 1.12340 1.15170 -0.22930 0.12500  0.19570  151 SER A O     
1172 C  CB    . SER A 151 ? 0.77890 1.07730 1.06960 -0.21050 0.15720  0.17010  151 SER A CB    
1173 O  OG    . SER A 151 ? 0.82870 1.10630 1.07310 -0.21530 0.17350  0.17910  151 SER A OG    
1174 N  N     . ASP A 152 ? 1.00070 1.22110 1.26000 -0.20330 0.10270  0.17150  152 ASP A N     
1175 C  CA    . ASP A 152 ? 0.98130 1.15900 1.20870 -0.19560 0.08580  0.17390  152 ASP A CA    
1176 C  C     . ASP A 152 ? 0.96490 1.11190 1.19110 -0.21240 0.07810  0.18160  152 ASP A C     
1177 O  O     . ASP A 152 ? 1.04100 1.14850 1.23640 -0.21090 0.07280  0.19070  152 ASP A O     
1178 C  CB    . ASP A 152 ? 0.94520 1.12620 1.17830 -0.17710 0.06930  0.16010  152 ASP A CB    
1179 C  CG    . ASP A 152 ? 0.97770 1.16860 1.19490 -0.15950 0.07430  0.15460  152 ASP A CG    
1180 O  OD1   . ASP A 152 ? 0.97520 1.17010 1.17520 -0.16100 0.09030  0.16010  152 ASP A OD1   
1181 O  OD2   . ASP A 152 ? 1.00760 1.19970 1.22620 -0.14590 0.06260  0.14450  152 ASP A OD2   
1182 N  N     . ILE A 153 ? 0.78650 0.94980 1.04650 -0.22800 0.07570  0.17770  153 ILE A N     
1183 C  CA    . ILE A 153 ? 0.76520 0.89570 1.02260 -0.24730 0.06950  0.18370  153 ILE A CA    
1184 C  C     . ILE A 153 ? 0.85190 0.96130 1.08760 -0.26410 0.08490  0.20180  153 ILE A C     
1185 O  O     . ILE A 153 ? 0.85220 0.91310 1.06240 -0.27010 0.07920  0.21150  153 ILE A O     
1186 C  CB    . ILE A 153 ? 0.67210 0.82820 0.97000 -0.26420 0.06290  0.17520  153 ILE A CB    
1187 C  CG1   . ILE A 153 ? 0.70560 0.86380 1.01010 -0.24940 0.04310  0.15980  153 ILE A CG1   
1188 C  CG2   . ILE A 153 ? 0.77190 0.89560 1.06700 -0.29080 0.06160  0.18240  153 ILE A CG2   
1189 C  CD1   . ILE A 153 ? 0.74560 0.93650 1.08860 -0.26250 0.03340  0.15130  153 ILE A CD1   
1190 N  N     . ALA A 154 ? 0.79730 0.94110 1.04230 -0.27220 0.10530  0.20670  154 ALA A N     
1191 C  CA    . ALA A 154 ? 0.77860 0.90340 0.99660 -0.28970 0.12220  0.22480  154 ALA A CA    
1192 C  C     . ALA A 154 ? 0.91670 0.99800 1.08360 -0.27500 0.11650  0.23560  154 ALA A C     
1193 O  O     . ALA A 154 ? 1.00520 1.04260 1.14220 -0.28640 0.11560  0.25220  154 ALA A O     
1194 C  CB    . ALA A 154 ? 0.77110 0.94480 1.00580 -0.29720 0.14790  0.22480  154 ALA A CB    
1195 N  N     . ALA A 155 ? 0.90400 0.99630 1.06040 -0.25020 0.11120  0.22700  155 ALA A N     
1196 C  CA    . ALA A 155 ? 0.93270 0.99010 1.04520 -0.23580 0.10230  0.23630  155 ALA A CA    
1197 C  C     . ALA A 155 ? 0.93710 0.95080 1.04290 -0.22860 0.08140  0.23880  155 ALA A C     
1198 O  O     . ALA A 155 ? 0.96970 0.94350 1.04280 -0.22650 0.07500  0.25440  155 ALA A O     
1199 C  CB    . ALA A 155 ? 0.93260 1.01360 1.03960 -0.21360 0.10030  0.22420  155 ALA A CB    
1200 N  N     . LEU A 156 ? 0.88390 0.90330 1.01950 -0.22470 0.07050  0.22350  156 LEU A N     
1201 C  CA    . LEU A 156 ? 0.86560 0.84380 0.99660 -0.21790 0.05380  0.22200  156 LEU A CA    
1202 C  C     . LEU A 156 ? 0.94650 0.88000 1.06340 -0.23680 0.05550  0.23810  156 LEU A C     
1203 O  O     . LEU A 156 ? 0.96650 0.85480 1.06000 -0.22760 0.04580  0.24800  156 LEU A O     
1204 C  CB    . LEU A 156 ? 0.82990 0.82300 0.99110 -0.21580 0.04470  0.20190  156 LEU A CB    
1205 C  CG    . LEU A 156 ? 0.73990 0.69190 0.89490 -0.20670 0.03000  0.19570  156 LEU A CG    
1206 C  CD1   . LEU A 156 ? 0.75410 0.69530 0.89040 -0.18080 0.02240  0.19650  156 LEU A CD1   
1207 C  CD2   . LEU A 156 ? 0.66330 0.62960 0.84160 -0.20890 0.02230  0.17570  156 LEU A CD2   
1208 N  N     . HIS A 157 ? 0.91140 0.85680 1.04440 -0.26350 0.06730  0.24100  157 HIS A N     
1209 C  CA    . HIS A 157 ? 0.92730 0.82820 1.04350 -0.28600 0.07110  0.25820  157 HIS A CA    
1210 C  C     . HIS A 157 ? 0.98990 0.86640 1.06440 -0.28460 0.07710  0.28110  157 HIS A C     
1211 O  O     . HIS A 157 ? 1.16720 0.98790 1.21390 -0.28600 0.06980  0.29700  157 HIS A O     
1212 C  CB    . HIS A 157 ? 0.92800 0.85460 1.07230 -0.31800 0.08430  0.25700  157 HIS A CB    
1213 C  CG    . HIS A 157 ? 1.00230 0.93920 1.18080 -0.32420 0.07350  0.23810  157 HIS A CG    
1214 N  ND1   . HIS A 157 ? 1.11200 0.99750 1.28310 -0.33090 0.06100  0.23520  157 HIS A ND1   
1215 C  CD2   . HIS A 157 ? 0.95830 0.94820 1.17550 -0.32460 0.07190  0.22120  157 HIS A CD2   
1216 C  CE1   . HIS A 157 ? 1.12480 1.03200 1.32560 -0.33740 0.05250  0.21660  157 HIS A CE1   
1217 N  NE2   . HIS A 157 ? 1.00920 0.98050 1.23890 -0.33350 0.05760  0.20900  157 HIS A NE2   
1218 N  N     . HIS A 158 ? 0.92570 0.84100 0.99310 -0.28310 0.09060  0.28330  158 HIS A N     
1219 C  CA    . HIS A 158 ? 0.99700 0.89190 1.01920 -0.28570 0.09720  0.30480  158 HIS A CA    
1220 C  C     . HIS A 158 ? 1.03450 0.88630 1.02610 -0.26200 0.07610  0.31460  158 HIS A C     
1221 O  O     . HIS A 158 ? 1.05660 0.86210 1.01210 -0.26790 0.07230  0.33750  158 HIS A O     
1222 C  CB    . HIS A 158 ? 1.03520 0.98080 1.05550 -0.28220 0.11330  0.29840  158 HIS A CB    
1223 C  CG    . HIS A 158 ? 1.08140 1.01190 1.05160 -0.28960 0.12340  0.31830  158 HIS A CG    
1224 N  ND1   . HIS A 158 ? 1.10840 1.02730 1.04310 -0.26970 0.11120  0.32360  158 HIS A ND1   
1225 C  CD2   . HIS A 158 ? 1.10800 1.03540 1.05570 -0.31630 0.14480  0.33380  158 HIS A CD2   
1226 C  CE1   . HIS A 158 ? 1.21730 1.12350 1.10620 -0.28360 0.12280  0.34190  158 HIS A CE1   
1227 N  NE2   . HIS A 158 ? 1.29070 1.20080 1.18500 -0.31200 0.14460  0.34840  158 HIS A NE2   
1228 N  N     . PHE A 159 ? 1.02640 0.89330 1.03320 -0.23510 0.06170  0.29830  159 PHE A N     
1229 C  CA    . PHE A 159 ? 1.02850 0.87030 1.01200 -0.21080 0.04320  0.30630  159 PHE A CA    
1230 C  C     . PHE A 159 ? 1.01220 0.81650 1.00840 -0.19480 0.02540  0.30230  159 PHE A C     
1231 O  O     . PHE A 159 ? 1.03990 0.81800 1.01890 -0.17580 0.01010  0.31330  159 PHE A O     
1232 C  CB    . PHE A 159 ? 0.98970 0.87380 0.97670 -0.19130 0.03980  0.29250  159 PHE A CB    
1233 C  CG    . PHE A 159 ? 1.02450 0.93480 0.98630 -0.20030 0.05420  0.29790  159 PHE A CG    
1234 C  CD1   . PHE A 159 ? 1.10430 0.98990 1.01990 -0.20490 0.05220  0.32050  159 PHE A CD1   
1235 C  CD2   . PHE A 159 ? 0.95200 0.90920 0.93330 -0.20240 0.06860  0.27990  159 PHE A CD2   
1236 C  CE1   . PHE A 159 ? 1.09110 0.99800 0.97740 -0.21420 0.06670  0.32360  159 PHE A CE1   
1237 C  CE2   . PHE A 159 ? 0.93740 0.91520 0.89360 -0.20910 0.08380  0.28220  159 PHE A CE2   
1238 C  CZ    . PHE A 159 ? 0.99220 0.94500 0.89930 -0.21600 0.08380  0.30310  159 PHE A CZ    
1239 N  N     . TYR A 160 ? 0.99380 0.79420 1.01920 -0.20160 0.02660  0.28690  160 TYR A N     
1240 C  CA    . TYR A 160 ? 1.02000 0.78910 1.05730 -0.18360 0.01210  0.27740  160 TYR A CA    
1241 C  C     . TYR A 160 ? 1.09020 0.81270 1.13090 -0.20130 0.01330  0.27840  160 TYR A C     
1242 O  O     . TYR A 160 ? 1.14660 0.84910 1.20230 -0.19200 0.00600  0.26260  160 TYR A O     
1243 C  CB    . TYR A 160 ? 0.95240 0.76270 1.01810 -0.16870 0.00910  0.25100  160 TYR A CB    
1244 C  CG    . TYR A 160 ? 0.93350 0.78100 0.99390 -0.15010 0.00560  0.24930  160 TYR A CG    
1245 C  CD1   . TYR A 160 ? 1.06770 0.90080 1.11510 -0.12820 -0.00760 0.25840  160 TYR A CD1   
1246 C  CD2   . TYR A 160 ? 0.85270 0.74920 0.92250 -0.15490 0.01470  0.23860  160 TYR A CD2   
1247 C  CE1   . TYR A 160 ? 1.01090 0.87910 1.05340 -0.11480 -0.01190 0.25600  160 TYR A CE1   
1248 C  CE2   . TYR A 160 ? 0.79430 0.71970 0.85650 -0.14040 0.01170  0.23570  160 TYR A CE2   
1249 C  CZ    . TYR A 160 ? 0.87920 0.79090 0.92690 -0.12210 -0.00170 0.24420  160 TYR A CZ    
1250 O  OH    . TYR A 160 ? 0.88880 0.82990 0.92870 -0.11110 -0.00580 0.24090  160 TYR A OH    
1251 N  N     . SER A 161 ? 1.05280 0.75640 1.07770 -0.22840 0.02340  0.29580  161 SER A N     
1252 C  CA    . SER A 161 ? 1.15610 0.81910 1.18480 -0.25220 0.02630  0.29600  161 SER A CA    
1253 C  C     . SER A 161 ? 1.21320 0.80210 1.22430 -0.24030 0.01370  0.30470  161 SER A C     
1254 O  O     . SER A 161 ? 1.21880 0.77280 1.23890 -0.24990 0.01190  0.29340  161 SER A O     
1255 C  CB    . SER A 161 ? 1.19860 0.86470 1.21540 -0.28700 0.04260  0.31350  161 SER A CB    
1256 O  OG    . SER A 161 ? 1.31930 1.04610 1.36760 -0.30430 0.05510  0.29840  161 SER A OG    
1257 N  N     . LYS A 162 ? 1.25910 0.82180 1.24530 -0.21890 0.00400  0.32400  162 LYS A N     
1258 C  CA    . LYS A 162 ? 1.33260 0.82060 1.30260 -0.20650 -0.00800 0.33580  162 LYS A CA    
1259 C  C     . LYS A 162 ? 1.31270 0.78780 1.30660 -0.17860 -0.01780 0.31190  162 LYS A C     
1260 O  O     . LYS A 162 ? 1.35930 0.77000 1.34730 -0.17390 -0.02320 0.31300  162 LYS A O     
1261 C  CB    . LYS A 162 ? 1.46250 0.93210 1.40090 -0.19000 -0.01840 0.36480  162 LYS A CB    
1262 C  CG    . LYS A 162 ? 1.55810 1.02940 1.46340 -0.22070 -0.00670 0.38970  162 LYS A CG    
1263 C  CD    . LYS A 162 ? 1.55250 0.98970 1.41490 -0.21150 -0.01820 0.42300  162 LYS A CD    
1264 C  CE    . LYS A 162 ? 1.51860 0.86820 1.35800 -0.21110 -0.02870 0.44430  162 LYS A CE    
1265 N  NZ    . LYS A 162 ? 1.58370 0.91280 1.37500 -0.22470 -0.02250 0.46940  162 LYS A NZ    
1266 N  N     . HIS A 163 ? 1.25040 0.78250 1.26960 -0.16160 -0.01840 0.28970  163 HIS A N     
1267 C  CA    . HIS A 163 ? 1.23030 0.75710 1.27040 -0.13390 -0.02530 0.26710  163 HIS A CA    
1268 C  C     . HIS A 163 ? 1.22560 0.77580 1.28740 -0.14510 -0.01840 0.23640  163 HIS A C     
1269 O  O     . HIS A 163 ? 1.27190 0.80460 1.34490 -0.12780 -0.02130 0.21650  163 HIS A O     
1270 C  CB    . HIS A 163 ? 1.16890 0.73580 1.21870 -0.10140 -0.03410 0.26640  163 HIS A CB    
1271 C  CG    . HIS A 163 ? 1.25620 0.79060 1.28960 -0.08040 -0.04740 0.29230  163 HIS A CG    
1272 N  ND1   . HIS A 163 ? 1.32970 0.82180 1.37200 -0.05180 -0.05760 0.29120  163 HIS A ND1   
1273 C  CD2   . HIS A 163 ? 1.29290 0.83070 1.30110 -0.08300 -0.05320 0.31990  163 HIS A CD2   
1274 C  CE1   . HIS A 163 ? 1.34310 0.81490 1.36920 -0.03650 -0.07150 0.31880  163 HIS A CE1   
1275 N  NE2   . HIS A 163 ? 1.36620 0.86410 1.36830 -0.05630 -0.06960 0.33690  163 HIS A NE2   
1276 N  N     . LEU A 164 ? 1.21680 0.80620 1.28500 -0.17260 -0.00970 0.23150  164 LEU A N     
1277 C  CA    . LEU A 164 ? 1.11560 0.73240 1.20350 -0.18200 -0.00690 0.20420  164 LEU A CA    
1278 C  C     . LEU A 164 ? 1.18390 0.78050 1.27200 -0.21780 -0.00210 0.20150  164 LEU A C     
1279 O  O     . LEU A 164 ? 1.23100 0.83710 1.31540 -0.24210 0.00470  0.21810  164 LEU A O     
1280 C  CB    . LEU A 164 ? 0.95940 0.64970 1.06220 -0.18040 -0.00370 0.19780  164 LEU A CB    
1281 C  CG    . LEU A 164 ? 0.99350 0.71410 1.10020 -0.14950 -0.00840 0.19400  164 LEU A CG    
1282 C  CD1   . LEU A 164 ? 0.95270 0.73600 1.06750 -0.15380 -0.00380 0.19280  164 LEU A CD1   
1283 C  CD2   . LEU A 164 ? 0.97640 0.68980 1.09360 -0.13210 -0.01220 0.17010  164 LEU A CD2   
1284 N  N     . GLY A 165 ? 1.18960 0.75860 1.28110 -0.22230 -0.00490 0.17990  165 GLY A N     
1285 C  CA    . GLY A 165 ? 1.17130 0.73520 1.26780 -0.25780 -0.00300 0.17090  165 GLY A CA    
1286 C  C     . GLY A 165 ? 1.16200 0.79740 1.28150 -0.26660 -0.00310 0.15690  165 GLY A C     
1287 O  O     . GLY A 165 ? 1.12150 0.77540 1.24660 -0.25190 -0.00760 0.13650  165 GLY A O     
1288 N  N     . PHE A 166 ? 1.27600 0.95240 1.40900 -0.28960 0.00260  0.16850  166 PHE A N     
1289 C  CA    . PHE A 166 ? 1.27040 1.01840 1.42910 -0.29500 0.00280  0.16000  166 PHE A CA    
1290 C  C     . PHE A 166 ? 1.28640 1.04370 1.46040 -0.32150 -0.00400 0.14280  166 PHE A C     
1291 O  O     . PHE A 166 ? 1.31960 1.04510 1.49120 -0.35000 -0.00370 0.14530  166 PHE A O     
1292 C  CB    . PHE A 166 ? 1.20230 0.99150 1.37210 -0.30680 0.01400  0.17920  166 PHE A CB    
1293 C  CG    . PHE A 166 ? 1.17600 0.96070 1.32710 -0.28540 0.01970  0.19690  166 PHE A CG    
1294 C  CD1   . PHE A 166 ? 1.14980 0.96640 1.30170 -0.25690 0.01740  0.19180  166 PHE A CD1   
1295 C  CD2   . PHE A 166 ? 1.21850 0.96590 1.34840 -0.29600 0.02650  0.21950  166 PHE A CD2   
1296 C  CE1   . PHE A 166 ? 1.16830 0.98230 1.30170 -0.23970 0.02050  0.20770  166 PHE A CE1   
1297 C  CE2   . PHE A 166 ? 1.22300 0.96630 1.33170 -0.27780 0.02920  0.23680  166 PHE A CE2   
1298 C  CZ    . PHE A 166 ? 1.19510 0.97300 1.30620 -0.24970 0.02560  0.23030  166 PHE A CZ    
1299 N  N     . PRO A 167 ? 1.23310 1.03140 1.42040 -0.31400 -0.01170 0.12570  167 PRO A N     
1300 C  CA    . PRO A 167 ? 1.18560 1.00720 1.39080 -0.34090 -0.02070 0.11280  167 PRO A CA    
1301 C  C     . PRO A 167 ? 1.17450 1.04930 1.41190 -0.36260 -0.01520 0.12570  167 PRO A C     
1302 O  O     . PRO A 167 ? 1.04580 0.93490 1.28650 -0.35740 -0.00210 0.14340  167 PRO A O     
1303 C  CB    . PRO A 167 ? 1.04270 0.89540 1.24960 -0.32220 -0.03020 0.09590  167 PRO A CB    
1304 C  CG    . PRO A 167 ? 0.93270 0.80610 1.13740 -0.29130 -0.02260 0.10500  167 PRO A CG    
1305 C  CD    . PRO A 167 ? 1.11780 0.94350 1.30330 -0.28260 -0.01360 0.11870  167 PRO A CD    
1306 N  N     . ASP A 168 ? 1.34830 1.25440 1.60990 -0.38730 -0.02490 0.11660  168 ASP A N     
1307 C  CA    . ASP A 168 ? 1.32220 1.28780 1.62330 -0.40720 -0.01960 0.12660  168 ASP A CA    
1308 C  C     . ASP A 168 ? 1.26790 1.29360 1.58920 -0.38130 -0.01440 0.13080  168 ASP A C     
1309 O  O     . ASP A 168 ? 1.24870 1.27190 1.55390 -0.35210 -0.01830 0.12460  168 ASP A O     
1310 C  CB    . ASP A 168 ? 1.32650 1.31650 1.65260 -0.43750 -0.03530 0.11480  168 ASP A CB    
1311 C  CG    . ASP A 168 ? 1.32270 1.33420 1.64890 -0.42330 -0.05420 0.09750  168 ASP A CG    
1312 O  OD1   . ASP A 168 ? 1.29560 1.30180 1.60280 -0.39120 -0.05340 0.09420  168 ASP A OD1   
1313 O  OD2   . ASP A 168 ? 1.41190 1.44920 1.75710 -0.44420 -0.07000 0.08790  168 ASP A OD2   
1314 N  N     . ASN A 169 ? 1.02410 1.10310 1.38110 -0.39330 -0.00400 0.14090  169 ASN A N     
1315 C  CA    . ASN A 169 ? 0.96310 1.09450 1.33880 -0.36950 0.00460  0.14500  169 ASN A CA    
1316 C  C     . ASN A 169 ? 0.99390 1.15560 1.38090 -0.35070 -0.01270 0.13120  169 ASN A C     
1317 O  O     . ASN A 169 ? 0.98090 1.14630 1.35440 -0.32170 -0.01110 0.12990  169 ASN A O     
1318 C  CB    . ASN A 169 ? 0.88240 1.06910 1.30020 -0.38810 0.01970  0.15480  169 ASN A CB    
1319 C  CG    . ASN A 169 ? 0.77470 1.00340 1.20380 -0.36360 0.03540  0.16000  169 ASN A CG    
1320 O  OD1   . ASN A 169 ? 0.77250 0.97630 1.17030 -0.35050 0.04960  0.16890  169 ASN A OD1   
1321 N  ND2   . ASN A 169 ? 0.71900 1.00990 1.19180 -0.35680 0.03150  0.15390  169 ASN A ND2   
1322 N  N     . ASP A 170 ? 1.15350 1.33690 1.56410 -0.36870 -0.03030 0.12200  170 ASP A N     
1323 C  CA    . ASP A 170 ? 1.12950 1.33840 1.54750 -0.35460 -0.05000 0.11080  170 ASP A CA    
1324 C  C     . ASP A 170 ? 1.13440 1.29980 1.50690 -0.33020 -0.05530 0.10220  170 ASP A C     
1325 O  O     . ASP A 170 ? 1.10700 1.29200 1.47800 -0.30580 -0.05840 0.10030  170 ASP A O     
1326 C  CB    . ASP A 170 ? 1.21780 1.43850 1.65410 -0.38360 -0.07110 0.10220  170 ASP A CB    
1327 C  CG    . ASP A 170 ? 1.31290 1.53680 1.73710 -0.37370 -0.09520 0.08980  170 ASP A CG    
1328 O  OD1   . ASP A 170 ? 1.34420 1.61700 1.79530 -0.35820 -0.10310 0.09170  170 ASP A OD1   
1329 O  OD2   . ASP A 170 ? 1.34760 1.52290 1.73380 -0.38190 -0.10570 0.07800  170 ASP A OD2   
1330 N  N     A SER A 171 ? 0.97860 1.08390 1.31470 -0.33620 -0.05490 0.09710  171 SER A N     
1331 C  CA    A SER A 171 ? 0.98720 1.05450 1.28450 -0.31360 -0.05740 0.08790  171 SER A CA    
1332 C  C     A SER A 171 ? 0.88020 0.95220 1.16950 -0.28540 -0.04290 0.09700  171 SER A C     
1333 O  O     A SER A 171 ? 0.83610 0.90830 1.10960 -0.26380 -0.04600 0.09100  171 SER A O     
1334 C  CB    A SER A 171 ? 1.08610 1.08820 1.35080 -0.32340 -0.05710 0.08020  171 SER A CB    
1335 O  OG    A SER A 171 ? 1.17440 1.16670 1.43750 -0.34880 -0.07250 0.06740  171 SER A OG    
1336 N  N     . LEU A 172 ? 0.85250 0.92570 1.14870 -0.28770 -0.02700 0.11140  172 LEU A N     
1337 C  CA    . LEU A 172 ? 0.72160 0.79860 1.00680 -0.26410 -0.01430 0.12030  172 LEU A CA    
1338 C  C     . LEU A 172 ? 0.73640 0.86470 1.04230 -0.24970 -0.01410 0.11970  172 LEU A C     
1339 O  O     . LEU A 172 ? 0.81660 0.94530 1.10720 -0.22710 -0.01110 0.11920  172 LEU A O     
1340 C  CB    . LEU A 172 ? 0.65250 0.71800 0.93590 -0.27400 0.00180  0.13660  172 LEU A CB    
1341 C  CG    . LEU A 172 ? 0.72220 0.72530 0.97460 -0.27600 0.00250  0.14030  172 LEU A CG    
1342 C  CD1   . LEU A 172 ? 0.79670 0.78560 1.04310 -0.28850 0.01690  0.15930  172 LEU A CD1   
1343 C  CD2   . LEU A 172 ? 0.70820 0.68780 0.93480 -0.24750 -0.00070 0.13550  172 LEU A CD2   
1344 N  N     . VAL A 173 ? 0.71830 0.89020 1.06090 -0.26230 -0.01760 0.11980  173 VAL A N     
1345 C  CA    . VAL A 173 ? 0.68460 0.90240 1.04970 -0.24630 -0.01900 0.11860  173 VAL A CA    
1346 C  C     . VAL A 173 ? 0.67540 0.88340 1.02200 -0.23150 -0.03570 0.10780  173 VAL A C     
1347 O  O     . VAL A 173 ? 0.63420 0.84980 0.97230 -0.21010 -0.03360 0.10720  173 VAL A O     
1348 C  CB    . VAL A 173 ? 0.63680 0.90610 1.05130 -0.26180 -0.02160 0.12050  173 VAL A CB    
1349 C  CG1   . VAL A 173 ? 0.55260 0.86490 0.99180 -0.24170 -0.02660 0.11820  173 VAL A CG1   
1350 C  CG2   . VAL A 173 ? 0.64420 0.92770 1.07670 -0.27710 -0.00060 0.13130  173 VAL A CG2   
1351 N  N     . VAL A 174 ? 0.67230 0.85920 1.00770 -0.24470 -0.05160 0.09890  174 VAL A N     
1352 C  CA    . VAL A 174 ? 0.61960 0.79370 0.93110 -0.23420 -0.06600 0.08850  174 VAL A CA    
1353 C  C     . VAL A 174 ? 0.61490 0.75810 0.89220 -0.21450 -0.05610 0.08670  174 VAL A C     
1354 O  O     . VAL A 174 ? 0.62660 0.77510 0.89200 -0.19830 -0.05920 0.08380  174 VAL A O     
1355 C  CB    . VAL A 174 ? 0.65130 0.80200 0.94950 -0.25470 -0.08200 0.07760  174 VAL A CB    
1356 C  CG1   . VAL A 174 ? 0.65520 0.78530 0.91890 -0.24520 -0.09260 0.06630  174 VAL A CG1   
1357 C  CG2   . VAL A 174 ? 0.81560 1.00440 1.15010 -0.27470 -0.09640 0.07910  174 VAL A CG2   
1358 N  N     . LEU A 175 ? 0.62770 0.73810 0.88990 -0.21640 -0.04520 0.08920  175 LEU A N     
1359 C  CA    . LEU A 175 ? 0.61850 0.70270 0.85330 -0.19810 -0.03780 0.08770  175 LEU A CA    
1360 C  C     . LEU A 175 ? 0.62130 0.72930 0.85920 -0.18040 -0.02910 0.09520  175 LEU A C     
1361 O  O     . LEU A 175 ? 0.66870 0.77460 0.89040 -0.16550 -0.03010 0.09050  175 LEU A O     
1362 C  CB    . LEU A 175 ? 0.57950 0.62670 0.80320 -0.20220 -0.02930 0.09240  175 LEU A CB    
1363 C  CG    . LEU A 175 ? 0.58640 0.60570 0.78700 -0.18340 -0.02380 0.09140  175 LEU A CG    
1364 C  CD1   . LEU A 175 ? 0.59080 0.59660 0.77430 -0.17650 -0.03010 0.07500  175 LEU A CD1   
1365 C  CD2   . LEU A 175 ? 0.68140 0.66330 0.87490 -0.18790 -0.01820 0.09880  175 LEU A CD2   
1366 N  N     . PHE A 176 ? 0.60380 0.73360 0.86070 -0.18350 -0.01920 0.10610  176 PHE A N     
1367 C  CA    . PHE A 176 ? 0.63260 0.78270 0.88980 -0.16830 -0.00960 0.11140  176 PHE A CA    
1368 C  C     . PHE A 176 ? 0.65020 0.82390 0.91480 -0.15790 -0.01740 0.10520  176 PHE A C     
1369 O  O     . PHE A 176 ? 0.75580 0.92810 1.00480 -0.14290 -0.01460 0.10380  176 PHE A O     
1370 C  CB    . PHE A 176 ? 0.56980 0.73950 0.84510 -0.17610 0.00460  0.12220  176 PHE A CB    
1371 C  CG    . PHE A 176 ? 0.60630 0.74990 0.86030 -0.17760 0.01540  0.13230  176 PHE A CG    
1372 C  CD1   . PHE A 176 ? 0.70710 0.84260 0.93740 -0.16220 0.02060  0.13520  176 PHE A CD1   
1373 C  CD2   . PHE A 176 ? 0.65290 0.77740 0.90820 -0.19530 0.01830  0.13940  176 PHE A CD2   
1374 C  CE1   . PHE A 176 ? 0.72850 0.84010 0.93750 -0.16290 0.02710  0.14630  176 PHE A CE1   
1375 C  CE2   . PHE A 176 ? 0.73550 0.83140 0.96790 -0.19590 0.02610  0.15110  176 PHE A CE2   
1376 C  CZ    . PHE A 176 ? 0.74240 0.83300 0.95180 -0.17890 0.02960  0.15510  176 PHE A CZ    
1377 N  N     . ALA A 177 ? 0.55340 0.74800 0.84130 -0.16620 -0.02860 0.10240  177 ALA A N     
1378 C  CA    . ALA A 177 ? 0.55910 0.77080 0.85160 -0.15530 -0.03910 0.09850  177 ALA A CA    
1379 C  C     . ALA A 177 ? 0.65050 0.83510 0.90850 -0.14900 -0.04760 0.09080  177 ALA A C     
1380 O  O     . ALA A 177 ? 0.74120 0.92670 0.98750 -0.13560 -0.04840 0.08980  177 ALA A O     
1381 C  CB    . ALA A 177 ? 0.70840 0.94750 1.03250 -0.16620 -0.05360 0.09820  177 ALA A CB    
1382 N  N     . GLN A 178 ? 0.67650 0.83480 0.91680 -0.15920 -0.05220 0.08470  178 GLN A N     
1383 C  CA    . GLN A 178 ? 0.66250 0.79670 0.87070 -0.15430 -0.05620 0.07580  178 GLN A CA    
1384 C  C     . GLN A 178 ? 0.68310 0.80930 0.87590 -0.13970 -0.04390 0.07730  178 GLN A C     
1385 O  O     . GLN A 178 ? 0.76490 0.88690 0.93920 -0.13220 -0.04560 0.07300  178 GLN A O     
1386 C  CB    . GLN A 178 ? 0.63760 0.74380 0.83160 -0.16680 -0.05920 0.06720  178 GLN A CB    
1387 C  CG    . GLN A 178 ? 0.68440 0.79360 0.88200 -0.18360 -0.07540 0.06190  178 GLN A CG    
1388 C  CD    . GLN A 178 ? 0.59900 0.67640 0.78270 -0.19790 -0.07590 0.05240  178 GLN A CD    
1389 O  OE1   . GLN A 178 ? 0.65250 0.71240 0.83930 -0.19830 -0.06500 0.05480  178 GLN A OE1   
1390 N  NE2   . GLN A 178 ? 0.63080 0.69660 0.79520 -0.20970 -0.08890 0.04150  178 GLN A NE2   
1391 N  N     . VAL A 179 ? 0.65890 0.78270 0.85750 -0.13730 -0.03240 0.08410  179 VAL A N     
1392 C  CA    . VAL A 179 ? 0.66160 0.78060 0.84610 -0.12480 -0.02340 0.08650  179 VAL A CA    
1393 C  C     . VAL A 179 ? 0.67270 0.81010 0.85770 -0.11590 -0.02140 0.08870  179 VAL A C     
1394 O  O     . VAL A 179 ? 0.78440 0.91740 0.95220 -0.10830 -0.02090 0.08520  179 VAL A O     
1395 C  CB    . VAL A 179 ? 0.67530 0.78660 0.86260 -0.12550 -0.01410 0.09580  179 VAL A CB    
1396 C  CG1   . VAL A 179 ? 0.66260 0.77540 0.83640 -0.11370 -0.00760 0.10000  179 VAL A CG1   
1397 C  CG2   . VAL A 179 ? 0.74250 0.82620 0.92440 -0.13060 -0.01610 0.09280  179 VAL A CG2   
1398 N  N     . ASN A 180 ? 0.70450 0.86250 0.91070 -0.11700 -0.01920 0.09380  180 ASN A N     
1399 C  CA    . ASN A 180 ? 0.73430 0.90630 0.94250 -0.10660 -0.01590 0.09460  180 ASN A CA    
1400 C  C     . ASN A 180 ? 0.81820 0.98490 1.01480 -0.10220 -0.02740 0.08900  180 ASN A C     
1401 O  O     . ASN A 180 ? 0.86560 1.02930 1.04970 -0.09320 -0.02470 0.08790  180 ASN A O     
1402 C  CB    . ASN A 180 ? 0.71440 0.91270 0.95360 -0.10730 -0.01070 0.09930  180 ASN A CB    
1403 C  CG    . ASN A 180 ? 0.76900 0.97180 1.01230 -0.11160 0.00510  0.10590  180 ASN A CG    
1404 O  OD1   . ASN A 180 ? 0.84110 1.05540 1.08660 -0.10510 0.01780  0.10770  180 ASN A OD1   
1405 N  ND2   . ASN A 180 ? 0.72440 0.91430 0.96500 -0.12290 0.00510  0.10950  180 ASN A ND2   
1406 N  N     A CYS A 181 ? 0.83570 0.99840 1.03250 -0.11000 -0.04040 0.08560  181 CYS A N     
1407 C  CA    A CYS A 181 ? 0.82010 0.97500 1.00030 -0.10790 -0.05220 0.08220  181 CYS A CA    
1408 C  C     A CYS A 181 ? 0.78100 0.91380 0.92910 -0.11100 -0.05170 0.07520  181 CYS A C     
1409 O  O     A CYS A 181 ? 0.83240 0.95600 0.96040 -0.11010 -0.05780 0.07340  181 CYS A O     
1410 C  CB    A CYS A 181 ? 0.82030 0.98450 1.01410 -0.11560 -0.06890 0.08280  181 CYS A CB    
1411 S  SG    A CYS A 181 ? 1.15600 1.35520 1.39490 -0.10890 -0.07160 0.09070  181 CYS A SG    
1412 N  N     . ASN A 182 ? 0.69280 0.81670 0.83630 -0.11430 -0.04410 0.07170  182 ASN A N     
1413 C  CA    . ASN A 182 ? 0.71260 0.82070 0.83270 -0.11630 -0.04170 0.06340  182 ASN A CA    
1414 C  C     . ASN A 182 ? 0.71170 0.81900 0.82950 -0.10920 -0.03020 0.06350  182 ASN A C     
1415 O  O     . ASN A 182 ? 0.68410 0.78450 0.78850 -0.10920 -0.02670 0.05630  182 ASN A O     
1416 C  CB    . ASN A 182 ? 0.66400 0.75910 0.77980 -0.12620 -0.04570 0.05580  182 ASN A CB    
1417 C  CG    . ASN A 182 ? 0.81530 0.91100 0.92810 -0.13600 -0.06050 0.05480  182 ASN A CG    
1418 O  OD1   . ASN A 182 ? 0.91440 1.01130 1.04050 -0.14470 -0.06660 0.05460  182 ASN A OD1   
1419 N  ND2   . ASN A 182 ? 0.92450 1.01840 1.01870 -0.13600 -0.06770 0.05480  182 ASN A ND2   
1420 N  N     . GLY A 183 ? 0.71310 0.82900 0.84360 -0.10390 -0.02460 0.07130  183 GLY A N     
1421 C  CA    . GLY A 183 ? 0.60870 0.72470 0.73560 -0.09780 -0.01740 0.07320  183 GLY A CA    
1422 C  C     . GLY A 183 ? 0.61170 0.73160 0.72370 -0.09480 -0.01570 0.07030  183 GLY A C     
1423 O  O     . GLY A 183 ? 0.71940 0.83870 0.82230 -0.09650 -0.01870 0.06870  183 GLY A O     
1424 N  N     . ALA A 184 ? 0.60930 0.73250 0.71920 -0.09100 -0.01210 0.07020  184 ALA A N     
1425 C  CA    . ALA A 184 ? 0.61530 0.74430 0.71280 -0.09150 -0.01090 0.06610  184 ALA A CA    
1426 C  C     . ALA A 184 ? 0.58360 0.72200 0.68230 -0.08710 -0.00950 0.07150  184 ALA A C     
1427 O  O     . ALA A 184 ? 0.63870 0.78040 0.74750 -0.08200 -0.01000 0.07380  184 ALA A O     
1428 C  CB    . ALA A 184 ? 0.59540 0.72410 0.68960 -0.09450 -0.00950 0.05640  184 ALA A CB    
1429 N  N     . THR A 185 ? 0.64020 0.78060 0.72700 -0.08860 -0.00860 0.07360  185 THR A N     
1430 C  CA    . THR A 185 ? 0.58910 0.73800 0.66960 -0.08770 -0.00920 0.07730  185 THR A CA    
1431 C  C     . THR A 185 ? 0.51210 0.67360 0.59340 -0.09050 -0.01170 0.07160  185 THR A C     
1432 O  O     . THR A 185 ? 0.55320 0.71370 0.62810 -0.09700 -0.01020 0.06400  185 THR A O     
1433 C  CB    . THR A 185 ? 0.65370 0.79750 0.71700 -0.09040 -0.00620 0.07770  185 THR A CB    
1434 O  OG1   . THR A 185 ? 0.71140 0.84680 0.76450 -0.09490 -0.00600 0.07060  185 THR A OG1   
1435 C  CG2   . THR A 185 ? 0.66980 0.80850 0.73790 -0.08680 -0.00120 0.08330  185 THR A CG2   
1436 N  N     . ILE A 186 ? 0.47850 0.65300 0.56860 -0.08600 -0.01580 0.07610  186 ILE A N     
1437 C  CA    . ILE A 186 ? 0.52230 0.71740 0.62060 -0.08780 -0.01890 0.07150  186 ILE A CA    
1438 C  C     . ILE A 186 ? 0.60800 0.81070 0.68980 -0.09520 -0.02370 0.07350  186 ILE A C     
1439 O  O     . ILE A 186 ? 0.71860 0.91630 0.78960 -0.09310 -0.02700 0.08170  186 ILE A O     
1440 C  CB    . ILE A 186 ? 0.51470 0.72130 0.63710 -0.07600 -0.02290 0.07570  186 ILE A CB    
1441 C  CG1   . ILE A 186 ? 0.51050 0.70280 0.64440 -0.06990 -0.01740 0.07190  186 ILE A CG1   
1442 C  CG2   . ILE A 186 ? 0.52790 0.76380 0.66680 -0.07630 -0.02610 0.07070  186 ILE A CG2   
1443 C  CD1   . ILE A 186 ? 0.55230 0.74620 0.70800 -0.05590 -0.02050 0.07620  186 ILE A CD1   
1444 N  N     . GLU A 187 ? 0.65100 0.86300 0.72690 -0.10620 -0.02330 0.06560  187 GLU A N     
1445 C  CA    . GLU A 187 ? 0.66520 0.88280 0.72350 -0.11640 -0.02870 0.06520  187 GLU A CA    
1446 C  C     . GLU A 187 ? 0.66950 0.91960 0.74490 -0.12260 -0.03490 0.06190  187 GLU A C     
1447 O  O     . GLU A 187 ? 0.65060 0.91690 0.74820 -0.12170 -0.03070 0.05650  187 GLU A O     
1448 C  CB    . GLU A 187 ? 0.67420 0.86870 0.70510 -0.12780 -0.02320 0.05870  187 GLU A CB    
1449 C  CG    . GLU A 187 ? 0.85170 1.01920 0.86780 -0.12140 -0.01760 0.06140  187 GLU A CG    
1450 C  CD    . GLU A 187 ? 0.94070 1.09650 0.96660 -0.11550 -0.01250 0.06070  187 GLU A CD    
1451 O  OE1   . GLU A 187 ? 0.89660 1.05720 0.92960 -0.11970 -0.01170 0.05610  187 GLU A OE1   
1452 O  OE2   . GLU A 187 ? 0.88890 1.03170 0.91410 -0.10820 -0.00910 0.06420  187 GLU A OE2   
1453 N  N     . ASP A 188 ? 0.67430 0.93610 0.73970 -0.12940 -0.04490 0.06480  188 ASP A N     
1454 C  CA    . ASP A 188 ? 0.64040 0.93810 0.72380 -0.13810 -0.05300 0.06160  188 ASP A CA    
1455 C  C     . ASP A 188 ? 0.72250 1.01440 0.78790 -0.15950 -0.04770 0.05090  188 ASP A C     
1456 O  O     . ASP A 188 ? 0.69420 0.95260 0.73500 -0.16430 -0.03840 0.04680  188 ASP A O     
1457 C  CB    . ASP A 188 ? 0.67320 0.98790 0.75370 -0.13750 -0.06970 0.07050  188 ASP A CB    
1458 C  CG    . ASP A 188 ? 0.74830 1.03900 0.78460 -0.15120 -0.07230 0.06940  188 ASP A CG    
1459 O  OD1   . ASP A 188 ? 0.77400 1.03590 0.78550 -0.16020 -0.06130 0.06120  188 ASP A OD1   
1460 O  OD2   . ASP A 188 ? 0.74190 1.04110 0.76660 -0.15240 -0.08600 0.07690  188 ASP A OD2   
1461 N  N     . GLU A 189 ? 0.77730 1.10220 0.85570 -0.17300 -0.05480 0.04710  189 GLU A N     
1462 C  CA    . GLU A 189 ? 0.78990 1.11120 0.85350 -0.19670 -0.04970 0.03730  189 GLU A CA    
1463 C  C     . GLU A 189 ? 0.80990 1.09210 0.82710 -0.21010 -0.05090 0.03450  189 GLU A C     
1464 O  O     . GLU A 189 ? 0.87950 1.14050 0.87590 -0.22750 -0.04410 0.02720  189 GLU A O     
1465 C  CB    . GLU A 189 ? 0.78250 1.15450 0.87530 -0.20960 -0.05860 0.03440  189 GLU A CB    
1466 C  CG    . GLU A 189 ? 0.82610 1.21210 0.90910 -0.21630 -0.07780 0.03890  189 GLU A CG    
1467 C  CD    . GLU A 189 ? 0.89170 1.29620 0.99570 -0.19290 -0.09050 0.05120  189 GLU A CD    
1468 O  OE1   . GLU A 189 ? 0.91440 1.34110 1.05760 -0.17460 -0.08710 0.05410  189 GLU A OE1   
1469 O  OE2   . GLU A 189 ? 0.93740 1.33090 1.01560 -0.19320 -0.10320 0.05780  189 GLU A OE2   
1470 N  N     . GLU A 190 ? 0.69540 0.96480 0.69390 -0.20270 -0.05820 0.03990  190 GLU A N     
1471 C  CA    . GLU A 190 ? 0.70730 0.93650 0.66100 -0.21180 -0.05600 0.03540  190 GLU A CA    
1472 C  C     . GLU A 190 ? 0.74550 0.93750 0.68530 -0.19550 -0.04420 0.03750  190 GLU A C     
1473 O  O     . GLU A 190 ? 0.74500 0.90570 0.65210 -0.19670 -0.04050 0.03430  190 GLU A O     
1474 C  CB    . GLU A 190 ? 0.83470 1.07450 0.77140 -0.21770 -0.07020 0.03810  190 GLU A CB    
1475 C  CG    . GLU A 190 ? 0.93420 1.20560 0.87610 -0.24050 -0.08370 0.03330  190 GLU A CG    
1476 C  CD    . GLU A 190 ? 1.19510 1.47570 1.11570 -0.24660 -0.10070 0.03700  190 GLU A CD    
1477 O  OE1   . GLU A 190 ? 1.25270 1.50470 1.14190 -0.23790 -0.09830 0.04040  190 GLU A OE1   
1478 O  OE2   . GLU A 190 ? 1.20190 1.52650 1.14540 -0.25600 -0.11760 0.03940  190 GLU A OE2   
1479 N  N     . LEU A 191 ? 0.75660 0.95180 0.72090 -0.18170 -0.03740 0.04120  191 LEU A N     
1480 C  CA    . LEU A 191 ? 0.66840 0.83780 0.62900 -0.16570 -0.02860 0.04460  191 LEU A CA    
1481 C  C     . LEU A 191 ? 0.74630 0.91310 0.69910 -0.15530 -0.03040 0.05150  191 LEU A C     
1482 O  O     . LEU A 191 ? 0.76880 0.91160 0.70900 -0.14750 -0.02190 0.05170  191 LEU A O     
1483 C  CB    . LEU A 191 ? 0.60820 0.73840 0.54300 -0.17030 -0.02020 0.03810  191 LEU A CB    
1484 C  CG    . LEU A 191 ? 0.67170 0.79280 0.60870 -0.17790 -0.01630 0.03470  191 LEU A CG    
1485 C  CD1   . LEU A 191 ? 0.79570 0.87400 0.71020 -0.17410 -0.01020 0.03270  191 LEU A CD1   
1486 C  CD2   . LEU A 191 ? 0.81350 0.95700 0.78100 -0.16880 -0.01510 0.03880  191 LEU A CD2   
1487 N  N     A SER A 192 ? 0.76630 0.95930 0.72820 -0.15450 -0.04130 0.05810  192 SER A N     
1488 C  CA    A SER A 192 ? 0.65330 0.84270 0.60590 -0.14530 -0.04300 0.06740  192 SER A CA    
1489 C  C     A SER A 192 ? 0.66030 0.85670 0.64280 -0.12870 -0.04090 0.07660  192 SER A C     
1490 O  O     A SER A 192 ? 0.73840 0.95500 0.75070 -0.12410 -0.04500 0.07760  192 SER A O     
1491 C  CB    A SER A 192 ? 0.72640 0.93570 0.66900 -0.15260 -0.05860 0.07260  192 SER A CB    
1492 O  OG    A SER A 192 ? 0.94880 1.14630 0.85620 -0.17010 -0.06070 0.06330  192 SER A OG    
1493 N  N     . HIS A 193 ? 0.67660 0.85630 0.65070 -0.12070 -0.03360 0.08250  193 HIS A N     
1494 C  CA    . HIS A 193 ? 0.66810 0.84760 0.66680 -0.10800 -0.03010 0.09000  193 HIS A CA    
1495 C  C     . HIS A 193 ? 0.61470 0.81130 0.63050 -0.10080 -0.04190 0.10130  193 HIS A C     
1496 O  O     . HIS A 193 ? 0.73390 0.93250 0.73300 -0.10230 -0.05000 0.11040  193 HIS A O     
1497 C  CB    . HIS A 193 ? 0.65240 0.81310 0.63960 -0.10430 -0.01880 0.09360  193 HIS A CB    
1498 C  CG    . HIS A 193 ? 0.58000 0.73870 0.59190 -0.09520 -0.01510 0.09970  193 HIS A CG    
1499 N  ND1   . HIS A 193 ? 0.55110 0.70740 0.58200 -0.09240 -0.01140 0.09340  193 HIS A ND1   
1500 C  CD2   . HIS A 193 ? 0.67180 0.82780 0.68940 -0.09040 -0.01560 0.11160  193 HIS A CD2   
1501 C  CE1   . HIS A 193 ? 0.65130 0.80460 0.69930 -0.08670 -0.00970 0.09960  193 HIS A CE1   
1502 N  NE2   . HIS A 193 ? 0.79890 0.95090 0.84000 -0.08550 -0.01170 0.11070  193 HIS A NE2   
1503 N  N     . LEU A 194 ? 0.58550 0.79200 0.63230 -0.09260 -0.04320 0.10070  194 LEU A N     
1504 C  CA    . LEU A 194 ? 0.60630 0.82530 0.67500 -0.08150 -0.05330 0.11050  194 LEU A CA    
1505 C  C     . LEU A 194 ? 0.63560 0.83520 0.71300 -0.07150 -0.04830 0.11850  194 LEU A C     
1506 O  O     . LEU A 194 ? 0.71870 0.91460 0.79810 -0.06390 -0.05630 0.13180  194 LEU A O     
1507 C  CB    . LEU A 194 ? 0.54580 0.78960 0.64550 -0.07810 -0.05610 0.10240  194 LEU A CB    
1508 C  CG    . LEU A 194 ? 0.60380 0.87640 0.70510 -0.08760 -0.06560 0.09820  194 LEU A CG    
1509 C  CD1   . LEU A 194 ? 0.65970 0.96280 0.79980 -0.08180 -0.06660 0.09170  194 LEU A CD1   
1510 C  CD2   . LEU A 194 ? 0.80070 1.08030 0.88720 -0.08820 -0.08140 0.11060  194 LEU A CD2   
1511 N  N     . GLY A 195 ? 0.56790 0.75380 0.64930 -0.07260 -0.03670 0.11150  195 GLY A N     
1512 C  CA    . GLY A 195 ? 0.61870 0.78660 0.70870 -0.06670 -0.03250 0.11770  195 GLY A CA    
1513 C  C     . GLY A 195 ? 0.57490 0.73450 0.67250 -0.06960 -0.02310 0.10730  195 GLY A C     
1514 O  O     . GLY A 195 ? 0.62840 0.79220 0.71970 -0.07570 -0.01950 0.09760  195 GLY A O     
1515 N  N     . SER A 196 ? 0.52180 0.66710 0.63110 -0.06590 -0.02070 0.11010  196 SER A N     
1516 C  CA    . SER A 196 ? 0.49920 0.63610 0.61440 -0.07000 -0.01470 0.10170  196 SER A CA    
1517 C  C     . SER A 196 ? 0.55260 0.68130 0.68390 -0.06470 -0.01530 0.09630  196 SER A C     
1518 O  O     . SER A 196 ? 0.59800 0.71980 0.73800 -0.05640 -0.01880 0.10240  196 SER A O     
1519 C  CB    . SER A 196 ? 0.61180 0.73860 0.72340 -0.07540 -0.00950 0.10840  196 SER A CB    
1520 O  OG    . SER A 196 ? 0.68130 0.81470 0.77760 -0.07910 -0.00570 0.11070  196 SER A OG    
1521 N  N     . ALA A 197 ? 0.49940 0.62590 0.63230 -0.06920 -0.01210 0.08470  197 ALA A N     
1522 C  CA    . ALA A 197 ? 0.54720 0.66440 0.69010 -0.06560 -0.01060 0.07590  197 ALA A CA    
1523 C  C     . ALA A 197 ? 0.51150 0.61870 0.64840 -0.07490 -0.00860 0.06700  197 ALA A C     
1524 O  O     . ALA A 197 ? 0.52410 0.63580 0.65230 -0.08220 -0.00970 0.06730  197 ALA A O     
1525 C  CB    . ALA A 197 ? 0.61490 0.74880 0.76520 -0.05960 -0.00910 0.06740  197 ALA A CB    
1526 N  N     . ILE A 198 ? 0.50580 0.59740 0.64700 -0.07400 -0.00680 0.05910  198 ILE A N     
1527 C  CA    . ILE A 198 ? 0.48270 0.56300 0.61490 -0.08390 -0.00670 0.04870  198 ILE A CA    
1528 C  C     . ILE A 198 ? 0.63590 0.71870 0.76260 -0.08240 -0.00050 0.03400  198 ILE A C     
1529 O  O     . ILE A 198 ? 0.65510 0.73400 0.79240 -0.07250 0.00480  0.02830  198 ILE A O     
1530 C  CB    . ILE A 198 ? 0.42860 0.48530 0.56490 -0.08790 -0.00840 0.04930  198 ILE A CB    
1531 C  CG1   . ILE A 198 ? 0.54450 0.60430 0.68610 -0.09400 -0.01230 0.06290  198 ILE A CG1   
1532 C  CG2   . ILE A 198 ? 0.56290 0.60650 0.68700 -0.09840 -0.00930 0.03560  198 ILE A CG2   
1533 C  CD1   . ILE A 198 ? 0.63080 0.70750 0.76820 -0.10100 -0.01590 0.06400  198 ILE A CD1   
1534 N  N     . PHE A 199 ? 0.59400 0.68270 0.70410 -0.09180 -0.00060 0.02810  199 PHE A N     
1535 C  CA    . PHE A 199 ? 0.55330 0.64450 0.65230 -0.09490 0.00740  0.01400  199 PHE A CA    
1536 C  C     . PHE A 199 ? 0.64320 0.71720 0.71900 -0.10830 0.00410  0.00670  199 PHE A C     
1537 O  O     . PHE A 199 ? 0.75620 0.83250 0.81450 -0.11750 -0.00150 0.00990  199 PHE A O     
1538 C  CB    . PHE A 199 ? 0.59920 0.71170 0.69360 -0.09710 0.01010  0.01530  199 PHE A CB    
1539 C  CG    . PHE A 199 ? 0.55830 0.69130 0.67420 -0.08620 0.01160  0.02070  199 PHE A CG    
1540 C  CD1   . PHE A 199 ? 0.60230 0.74630 0.73680 -0.07630 0.01940  0.01280  199 PHE A CD1   
1541 C  CD2   . PHE A 199 ? 0.50750 0.64970 0.62500 -0.08550 0.00500  0.03300  199 PHE A CD2   
1542 C  CE1   . PHE A 199 ? 0.56270 0.72910 0.71920 -0.06600 0.01740  0.01910  199 PHE A CE1   
1543 C  CE2   . PHE A 199 ? 0.51890 0.68000 0.65200 -0.07750 0.00380  0.03820  199 PHE A CE2   
1544 C  CZ    . PHE A 199 ? 0.54830 0.72290 0.70210 -0.06780 0.00840  0.03220  199 PHE A CZ    
1545 N  N     . PRO A 200 ? 0.65580 0.70940 0.72880 -0.11000 0.00570  -0.00250 200 PRO A N     
1546 C  CA    . PRO A 200 ? 0.70590 0.74270 0.75550 -0.12490 -0.00160 -0.00800 200 PRO A CA    
1547 C  C     . PRO A 200 ? 0.77930 0.81770 0.79900 -0.13560 0.00050  -0.01520 200 PRO A C     
1548 O  O     . PRO A 200 ? 0.85710 0.89310 0.85930 -0.14610 -0.01150 -0.00930 200 PRO A O     
1549 C  CB    . PRO A 200 ? 0.80180 0.81390 0.85130 -0.12450 0.00350  -0.02060 200 PRO A CB    
1550 C  CG    . PRO A 200 ? 0.79190 0.80550 0.87040 -0.10820 0.00810  -0.01420 200 PRO A CG    
1551 C  CD    . PRO A 200 ? 0.74720 0.78940 0.83720 -0.09850 0.01280  -0.00810 200 PRO A CD    
1552 N  N     . ASP A 201 ? 0.84850 0.89170 0.86260 -0.13330 0.01570  -0.02720 201 ASP A N     
1553 C  CA    . ASP A 201 ? 0.86620 0.90880 0.84730 -0.14660 0.02010  -0.03390 201 ASP A CA    
1554 C  C     . ASP A 201 ? 0.83970 0.89560 0.81560 -0.15010 0.01310  -0.01990 201 ASP A C     
1555 O  O     . ASP A 201 ? 0.85440 0.90100 0.79840 -0.16330 0.00730  -0.01780 201 ASP A O     
1556 C  CB    . ASP A 201 ? 0.95830 1.00930 0.94100 -0.14290 0.04140  -0.05010 201 ASP A CB    
1557 C  CG    . ASP A 201 ? 1.02390 1.05350 0.99960 -0.14190 0.05090  -0.06840 201 ASP A CG    
1558 O  OD1   . ASP A 201 ? 1.05050 1.05510 1.00190 -0.15320 0.04100  -0.07140 201 ASP A OD1   
1559 O  OD2   . ASP A 201 ? 0.99040 1.02810 0.98620 -0.12950 0.06780  -0.08030 201 ASP A OD2   
1560 N  N     . VAL A 202 ? 0.73650 0.81070 0.74030 -0.13890 0.01290  -0.01000 202 VAL A N     
1561 C  CA    . VAL A 202 ? 0.71140 0.79360 0.70990 -0.14170 0.00690  0.00190  202 VAL A CA    
1562 C  C     . VAL A 202 ? 0.71180 0.78320 0.70520 -0.14320 -0.01000 0.01380  202 VAL A C     
1563 O  O     . VAL A 202 ? 0.70020 0.76620 0.67550 -0.14900 -0.01680 0.02090  202 VAL A O     
1564 C  CB    . VAL A 202 ? 0.69860 0.80240 0.72550 -0.13040 0.01120  0.00700  202 VAL A CB    
1565 C  CG1   . VAL A 202 ? 0.63360 0.74130 0.65130 -0.13490 0.00660  0.01650  202 VAL A CG1   
1566 C  CG2   . VAL A 202 ? 0.79680 0.91740 0.83600 -0.12730 0.02630  -0.00450 202 VAL A CG2   
1567 N  N     . ALA A 203 ? 0.66570 0.73370 0.67610 -0.13840 -0.01680 0.01610  203 ALA A N     
1568 C  CA    . ALA A 203 ? 0.62860 0.69420 0.64310 -0.13910 -0.03170 0.02680  203 ALA A CA    
1569 C  C     . ALA A 203 ? 0.69150 0.74340 0.67730 -0.15110 -0.04360 0.02630  203 ALA A C     
1570 O  O     . ALA A 203 ? 0.77860 0.83150 0.76720 -0.15040 -0.05760 0.03660  203 ALA A O     
1571 C  CB    . ALA A 203 ? 0.73810 0.80490 0.77770 -0.13500 -0.03460 0.02850  203 ALA A CB    
1572 N  N     . LEU A 204 ? 0.67430 0.71380 0.63220 -0.16160 -0.03840 0.01460  204 LEU A N     
1573 C  CA    . LEU A 204 ? 0.72140 0.74510 0.64440 -0.17530 -0.05110 0.01470  204 LEU A CA    
1574 C  C     . LEU A 204 ? 0.77690 0.79600 0.67950 -0.17770 -0.05820 0.02600  204 LEU A C     
1575 O  O     . LEU A 204 ? 0.90370 0.91160 0.78590 -0.18430 -0.07590 0.03350  204 LEU A O     
1576 C  CB    . LEU A 204 ? 0.70460 0.71440 0.59690 -0.18700 -0.03960 -0.00220 204 LEU A CB    
1577 C  CG    . LEU A 204 ? 0.79100 0.78060 0.63550 -0.20490 -0.05020 -0.00480 204 LEU A CG    
1578 C  CD1   . LEU A 204 ? 0.86430 0.85000 0.71230 -0.20910 -0.07450 0.00190  204 LEU A CD1   
1579 C  CD2   . LEU A 204 ? 0.87750 0.85470 0.69450 -0.21480 -0.03260 -0.02520 204 LEU A CD2   
1580 N  N     . MET A 205 ? 0.78040 0.80630 0.68780 -0.17280 -0.04640 0.02810  205 MET A N     
1581 C  CA    . MET A 205 ? 0.77070 0.78500 0.65390 -0.17730 -0.05130 0.03780  205 MET A CA    
1582 C  C     . MET A 205 ? 0.74150 0.75550 0.64190 -0.16620 -0.06800 0.05220  205 MET A C     
1583 O  O     . MET A 205 ? 0.69730 0.72730 0.63360 -0.15320 -0.06590 0.05460  205 MET A O     
1584 C  CB    . MET A 205 ? 0.82640 0.84920 0.71230 -0.17750 -0.03410 0.03450  205 MET A CB    
1585 C  CG    . MET A 205 ? 0.88520 0.91200 0.75520 -0.18870 -0.01600 0.02050  205 MET A CG    
1586 S  SD    . MET A 205 ? 0.92290 0.96680 0.80140 -0.19150 0.00160  0.01800  205 MET A SD    
1587 C  CE    . MET A 205 ? 0.77520 0.84430 0.70560 -0.17100 0.00250  0.01870  205 MET A CE    
1588 N  N     . ASN A 206 ? 0.72380 0.71920 0.59800 -0.17090 -0.08400 0.06190  206 ASN A N     
1589 C  CA    . ASN A 206 ? 0.77140 0.76530 0.66240 -0.15820 -0.09990 0.07540  206 ASN A CA    
1590 C  C     . ASN A 206 ? 0.77520 0.76030 0.66540 -0.15140 -0.09210 0.08040  206 ASN A C     
1591 O  O     . ASN A 206 ? 0.81140 0.79140 0.68440 -0.16000 -0.07730 0.07480  206 ASN A O     
1592 C  CB    . ASN A 206 ? 0.88910 0.86480 0.75210 -0.16430 -0.12280 0.08520  206 ASN A CB    
1593 C  CG    . ASN A 206 ? 0.82660 0.81380 0.69760 -0.16960 -0.13540 0.08140  206 ASN A CG    
1594 O  OD1   . ASN A 206 ? 0.86560 0.87610 0.77810 -0.16110 -0.13590 0.07940  206 ASN A OD1   
1595 N  ND2   . ASN A 206 ? 0.86430 0.83400 0.69220 -0.18630 -0.14440 0.07970  206 ASN A ND2   
1596 N  N     . HIS A 207 ? 0.80370 0.78780 0.71390 -0.13630 -0.10200 0.08990  207 HIS A N     
1597 C  CA    . HIS A 207 ? 0.78290 0.75610 0.69460 -0.12820 -0.09450 0.09270  207 HIS A CA    
1598 C  C     . HIS A 207 ? 0.89250 0.82900 0.76750 -0.13160 -0.10520 0.10300  207 HIS A C     
1599 O  O     . HIS A 207 ? 0.94860 0.87230 0.81060 -0.13110 -0.12430 0.11260  207 HIS A O     
1600 C  CB    . HIS A 207 ? 0.68440 0.67440 0.63770 -0.10840 -0.09490 0.09510  207 HIS A CB    
1601 C  CG    . HIS A 207 ? 0.69170 0.66260 0.64040 -0.09930 -0.08980 0.09760  207 HIS A CG    
1602 N  ND1   . HIS A 207 ? 0.74470 0.71850 0.69420 -0.10070 -0.07280 0.09000  207 HIS A ND1   
1603 C  CD2   . HIS A 207 ? 0.76600 0.71140 0.70690 -0.08880 -0.10020 0.10640  207 HIS A CD2   
1604 C  CE1   . HIS A 207 ? 0.78810 0.73770 0.72820 -0.09330 -0.07190 0.09250  207 HIS A CE1   
1605 N  NE2   . HIS A 207 ? 0.81380 0.74440 0.74940 -0.08480 -0.08760 0.10230  207 HIS A NE2   
1606 N  N     . SER A 208 ? 0.94920 0.86710 0.80630 -0.13610 -0.09400 0.10160  208 SER A N     
1607 C  CA    . SER A 208 ? 0.98860 0.86570 0.81490 -0.13630 -0.10240 0.11200  208 SER A CA    
1608 C  C     . SER A 208 ? 1.01130 0.87780 0.84110 -0.13240 -0.08910 0.10750  208 SER A C     
1609 O  O     . SER A 208 ? 1.01390 0.90010 0.85200 -0.14000 -0.07280 0.09670  208 SER A O     
1610 C  CB    . SER A 208 ? 1.05260 0.90260 0.82720 -0.15930 -0.10410 0.11600  208 SER A CB    
1611 O  OG    . SER A 208 ? 1.11690 0.92180 0.85980 -0.16020 -0.11210 0.12760  208 SER A OG    
1612 N  N     . CYS A 209 ? 0.94760 0.78130 0.77020 -0.12030 -0.09710 0.11540  209 CYS A N     
1613 C  CA    . CYS A 209 ? 1.03250 0.84610 0.84920 -0.11910 -0.08530 0.11020  209 CYS A CA    
1614 C  C     . CYS A 209 ? 1.02000 0.80050 0.79020 -0.14380 -0.07970 0.11090  209 CYS A C     
1615 O  O     . CYS A 209 ? 1.09330 0.85590 0.85330 -0.14900 -0.06980 0.10520  209 CYS A O     
1616 C  CB    . CYS A 209 ? 1.12100 0.90950 0.94950 -0.09470 -0.09340 0.11600  209 CYS A CB    
1617 S  SG    . CYS A 209 ? 0.95720 0.78870 0.84480 -0.06660 -0.09960 0.11640  209 CYS A SG    
1618 N  N     A CYS A 210 ? 1.06400 0.83500 0.80360 -0.16130 -0.08530 0.11730  210 CYS A N     
1619 C  CA    A CYS A 210 ? 1.08100 0.83440 0.78130 -0.18990 -0.07490 0.11560  210 CYS A CA    
1620 C  C     A CYS A 210 ? 1.05320 0.84480 0.75620 -0.20530 -0.06600 0.10810  210 CYS A C     
1621 O  O     A CYS A 210 ? 1.07860 0.85770 0.74900 -0.21990 -0.07020 0.11390  210 CYS A O     
1622 C  CB    A CYS A 210 ? 1.21890 0.91550 0.86950 -0.19940 -0.08730 0.13120  210 CYS A CB    
1623 S  SG    A CYS A 210 ? 1.82400 1.46770 1.47150 -0.17610 -0.09990 0.14100  210 CYS A SG    
1624 N  N     . PRO A 211 ? 0.89940 0.73570 0.63910 -0.20170 -0.05350 0.09510  211 PRO A N     
1625 C  CA    . PRO A 211 ? 0.94040 0.81220 0.68890 -0.21050 -0.04520 0.08680  211 PRO A CA    
1626 C  C     . PRO A 211 ? 0.91350 0.78340 0.63210 -0.23810 -0.03110 0.08240  211 PRO A C     
1627 O  O     . PRO A 211 ? 0.96170 0.81560 0.66420 -0.25200 -0.02430 0.08260  211 PRO A O     
1628 C  CB    . PRO A 211 ? 0.88820 0.80110 0.68310 -0.19760 -0.03650 0.07620  211 PRO A CB    
1629 C  CG    . PRO A 211 ? 0.83190 0.73210 0.62830 -0.19580 -0.03330 0.07560  211 PRO A CG    
1630 C  CD    . PRO A 211 ? 0.86950 0.72240 0.63990 -0.19050 -0.04600 0.08720  211 PRO A CD    
1631 N  N     . ASN A 212 ? 0.88080 0.76770 0.59200 -0.24750 -0.02520 0.07710  212 ASN A N     
1632 C  CA    . ASN A 212 ? 0.87650 0.77130 0.56570 -0.27330 -0.00740 0.07020  212 ASN A CA    
1633 C  C     . ASN A 212 ? 0.84720 0.79300 0.57570 -0.27250 0.01060  0.05390  212 ASN A C     
1634 O  O     . ASN A 212 ? 0.92450 0.88580 0.64440 -0.29230 0.02800  0.04620  212 ASN A O     
1635 C  CB    . ASN A 212 ? 0.91790 0.79190 0.56260 -0.28750 -0.01000 0.07450  212 ASN A CB    
1636 C  CG    . ASN A 212 ? 0.92530 0.81380 0.58410 -0.27300 -0.01870 0.07080  212 ASN A CG    
1637 O  OD1   . ASN A 212 ? 1.04400 0.96230 0.74820 -0.25440 -0.01840 0.06340  212 ASN A OD1   
1638 N  ND2   . ASN A 212 ? 0.92720 0.79230 0.54370 -0.28340 -0.02720 0.07630  212 ASN A ND2   
1639 N  N     . VAL A 213 ? 0.72280 0.69560 0.49510 -0.25040 0.00730  0.04910  213 VAL A N     
1640 C  CA    . VAL A 213 ? 0.70480 0.72260 0.51680 -0.24640 0.02120  0.03620  213 VAL A CA    
1641 C  C     . VAL A 213 ? 0.79470 0.82800 0.64320 -0.22870 0.01550  0.03710  213 VAL A C     
1642 O  O     . VAL A 213 ? 0.80870 0.82200 0.65710 -0.21600 0.00260  0.04520  213 VAL A O     
1643 C  CB    . VAL A 213 ? 0.61340 0.64990 0.43860 -0.23890 0.02630  0.02700  213 VAL A CB    
1644 C  CG1   . VAL A 213 ? 0.75770 0.78010 0.54240 -0.25820 0.03460  0.02370  213 VAL A CG1   
1645 C  CG2   . VAL A 213 ? 0.75230 0.77980 0.59040 -0.21900 0.01010  0.03240  213 VAL A CG2   
1646 N  N     . ILE A 214 ? 0.72000 0.79090 0.59980 -0.22830 0.02570  0.02840  214 ILE A N     
1647 C  CA    . ILE A 214 ? 0.65870 0.74900 0.57180 -0.21270 0.02090  0.02860  214 ILE A CA    
1648 C  C     . ILE A 214 ? 0.64330 0.76990 0.59310 -0.20050 0.02700  0.02080  214 ILE A C     
1649 O  O     . ILE A 214 ? 0.67000 0.81800 0.62700 -0.20780 0.03940  0.01190  214 ILE A O     
1650 C  CB    . ILE A 214 ? 0.62210 0.71990 0.53580 -0.22460 0.02270  0.02790  214 ILE A CB    
1651 C  CG1   . ILE A 214 ? 0.77220 0.82690 0.65250 -0.23120 0.01500  0.03560  214 ILE A CG1   
1652 C  CG2   . ILE A 214 ? 0.64310 0.77070 0.59160 -0.21130 0.01950  0.02610  214 ILE A CG2   
1653 C  CD1   . ILE A 214 ? 0.74910 0.80540 0.62450 -0.24650 0.01680  0.03320  214 ILE A CD1   
1654 N  N     . VAL A 215 ? 0.59050 0.72070 0.56180 -0.18160 0.01900  0.02440  215 VAL A N     
1655 C  CA    . VAL A 215 ? 0.56950 0.72620 0.57480 -0.16730 0.02180  0.02000  215 VAL A CA    
1656 C  C     . VAL A 215 ? 0.61150 0.79420 0.64000 -0.16390 0.02000  0.02110  215 VAL A C     
1657 O  O     . VAL A 215 ? 0.58430 0.75730 0.60720 -0.16150 0.01200  0.02770  215 VAL A O     
1658 C  CB    . VAL A 215 ? 0.56380 0.70620 0.57540 -0.15200 0.01380  0.02470  215 VAL A CB    
1659 C  CG1   . VAL A 215 ? 0.57820 0.74030 0.62090 -0.13830 0.01690  0.02080  215 VAL A CG1   
1660 C  CG2   . VAL A 215 ? 0.64490 0.76210 0.63100 -0.15760 0.01140  0.02450  215 VAL A CG2   
1661 N  N     . THR A 216 ? 0.61510 0.83160 0.66990 -0.16310 0.02710  0.01440  216 THR A N     
1662 C  CA    . THR A 216 ? 0.51370 0.76050 0.59530 -0.15820 0.02230  0.01620  216 THR A CA    
1663 C  C     . THR A 216 ? 0.52400 0.79050 0.63990 -0.13850 0.02270  0.01480  216 THR A C     
1664 O  O     . THR A 216 ? 0.60080 0.85620 0.71820 -0.13100 0.02870  0.01020  216 THR A O     
1665 C  CB    . THR A 216 ? 0.59100 0.86580 0.67840 -0.17620 0.02820  0.01040  216 THR A CB    
1666 O  OG1   . THR A 216 ? 0.67960 0.97530 0.78140 -0.17920 0.04290  0.00010  216 THR A OG1   
1667 C  CG2   . THR A 216 ? 0.71390 0.96100 0.76330 -0.19710 0.02740  0.01250  216 THR A CG2   
1668 N  N     . TYR A 217 ? 0.52230 0.81400 0.66320 -0.12990 0.01470  0.01930  217 TYR A N     
1669 C  CA    . TYR A 217 ? 0.50560 0.80790 0.67640 -0.10870 0.01200  0.02140  217 TYR A CA    
1670 C  C     . TYR A 217 ? 0.55750 0.90540 0.76640 -0.10380 0.01080  0.01880  217 TYR A C     
1671 O  O     . TYR A 217 ? 0.63550 1.00500 0.84740 -0.11320 0.00250  0.02240  217 TYR A O     
1672 C  CB    . TYR A 217 ? 0.55990 0.84180 0.72250 -0.09860 -0.00030 0.03420  217 TYR A CB    
1673 C  CG    . TYR A 217 ? 0.54090 0.78550 0.67330 -0.10310 0.00080  0.03660  217 TYR A CG    
1674 C  CD1   . TYR A 217 ? 0.56010 0.78470 0.69030 -0.09770 0.00590  0.03320  217 TYR A CD1   
1675 C  CD2   . TYR A 217 ? 0.60810 0.83810 0.71510 -0.11290 -0.00360 0.04110  217 TYR A CD2   
1676 C  CE1   . TYR A 217 ? 0.52940 0.72580 0.63690 -0.10200 0.00440  0.03600  217 TYR A CE1   
1677 C  CE2   . TYR A 217 ? 0.63720 0.83750 0.72310 -0.11440 -0.00310 0.04340  217 TYR A CE2   
1678 C  CZ    . TYR A 217 ? 0.55100 0.73740 0.63920 -0.10900 -0.00010 0.04160  217 TYR A CZ    
1679 O  OH    . TYR A 217 ? 0.48620 0.64890 0.55840 -0.11040 -0.00210 0.04460  217 TYR A OH    
1680 N  N     . LYS A 218 ? 0.53560 0.89780 0.77430 -0.08880 0.01880  0.01190  218 LYS A N     
1681 C  CA    . LYS A 218 ? 0.56670 0.97400 0.85210 -0.07650 0.01780  0.00940  218 LYS A CA    
1682 C  C     . LYS A 218 ? 0.53760 0.93410 0.84300 -0.05000 0.00860  0.01760  218 LYS A C     
1683 O  O     . LYS A 218 ? 0.59100 0.97150 0.90510 -0.03630 0.01850  0.01060  218 LYS A O     
1684 C  CB    . LYS A 218 ? 0.62800 1.06170 0.93360 -0.08050 0.03840  -0.00770 218 LYS A CB    
1685 C  CG    . LYS A 218 ? 0.51540 1.00920 0.87400 -0.07360 0.03810  -0.01130 218 LYS A CG    
1686 C  CD    . LYS A 218 ? 0.61010 1.13390 0.98650 -0.08230 0.06260  -0.02970 218 LYS A CD    
1687 C  CE    . LYS A 218 ? 0.69140 1.21630 1.03540 -0.11630 0.07000  -0.03280 218 LYS A CE    
1688 N  NZ    . LYS A 218 ? 0.59730 1.14410 0.94770 -0.12920 0.09680  -0.04990 218 LYS A NZ    
1689 N  N     . GLY A 219 ? 0.53620 0.93330 0.84060 -0.04500 -0.01030 0.03300  219 GLY A N     
1690 C  CA    . GLY A 219 ? 0.54780 0.92280 0.85830 -0.02410 -0.02020 0.04460  219 GLY A CA    
1691 C  C     . GLY A 219 ? 0.60920 0.93420 0.88540 -0.02690 -0.01530 0.04640  219 GLY A C     
1692 O  O     . GLY A 219 ? 0.63820 0.94470 0.88120 -0.04160 -0.01800 0.05120  219 GLY A O     
1693 N  N     . THR A 220 ? 0.62240 0.92570 0.90800 -0.01300 -0.00790 0.04160  220 THR A N     
1694 C  CA    . THR A 220 ? 0.61580 0.87510 0.87340 -0.01720 -0.00330 0.04150  220 THR A CA    
1695 C  C     . THR A 220 ? 0.61660 0.86760 0.86180 -0.02790 0.01300  0.02410  220 THR A C     
1696 O  O     . THR A 220 ? 0.54040 0.75790 0.76520 -0.03200 0.01620  0.02170  220 THR A O     
1697 C  CB    . THR A 220 ? 0.58150 0.81410 0.85070 0.00150  -0.00720 0.04810  220 THR A CB    
1698 O  OG1   . THR A 220 ? 0.61810 0.85740 0.91550 0.01660  0.00320  0.03450  220 THR A OG1   
1699 C  CG2   . THR A 220 ? 0.59530 0.83490 0.87360 0.01220  -0.02460 0.06740  220 THR A CG2   
1700 N  N     . LEU A 221 ? 0.62840 0.91020 0.88480 -0.03410 0.02280  0.01220  221 LEU A N     
1701 C  CA    . LEU A 221 ? 0.63430 0.90880 0.87310 -0.04690 0.03900  -0.00370 221 LEU A CA    
1702 C  C     . LEU A 221 ? 0.61600 0.88510 0.82060 -0.06980 0.03750  -0.00130 221 LEU A C     
1703 O  O     . LEU A 221 ? 0.59770 0.89070 0.80470 -0.07880 0.03340  0.00290  221 LEU A O     
1704 C  CB    . LEU A 221 ? 0.63740 0.94780 0.90590 -0.04230 0.05400  -0.01870 221 LEU A CB    
1705 C  CG    . LEU A 221 ? 0.66360 0.97050 0.91060 -0.05830 0.07340  -0.03580 221 LEU A CG    
1706 C  CD1   . LEU A 221 ? 0.69880 0.96680 0.92870 -0.05290 0.08130  -0.04580 221 LEU A CD1   
1707 C  CD2   . LEU A 221 ? 0.64480 0.99830 0.92370 -0.05820 0.08950  -0.04890 221 LEU A CD2   
1708 N  N     . ALA A 222 ? 0.54970 0.78630 0.72260 -0.07940 0.03970  -0.00360 222 ALA A N     
1709 C  CA    . ALA A 222 ? 0.52050 0.74770 0.66100 -0.09880 0.03820  -0.00130 222 ALA A CA    
1710 C  C     . ALA A 222 ? 0.59820 0.83600 0.72800 -0.11260 0.05330  -0.01450 222 ALA A C     
1711 O  O     . ALA A 222 ? 0.71650 0.95210 0.84910 -0.10940 0.06560  -0.02720 222 ALA A O     
1712 C  CB    . ALA A 222 ? 0.60620 0.79750 0.72040 -0.10220 0.03130  0.00360  222 ALA A CB    
1713 N  N     . GLU A 223 ? 0.61350 0.86110 0.72940 -0.12910 0.05370  -0.01220 223 GLU A N     
1714 C  CA    . GLU A 223 ? 0.64320 0.89830 0.74300 -0.14690 0.06860  -0.02250 223 GLU A CA    
1715 C  C     . GLU A 223 ? 0.67120 0.89600 0.72690 -0.16530 0.06280  -0.01540 223 GLU A C     
1716 O  O     . GLU A 223 ? 0.67200 0.88700 0.72080 -0.16630 0.05000  -0.00430 223 GLU A O     
1717 C  CB    . GLU A 223 ? 0.62300 0.92300 0.75220 -0.15180 0.07610  -0.02680 223 GLU A CB    
1718 C  CG    . GLU A 223 ? 0.63740 0.97150 0.81560 -0.13110 0.08130  -0.03360 223 GLU A CG    
1719 C  CD    . GLU A 223 ? 0.78980 1.17550 1.00110 -0.13780 0.09110  -0.04030 223 GLU A CD    
1720 O  OE1   . GLU A 223 ? 0.80460 1.20260 1.00910 -0.15510 0.08500  -0.03420 223 GLU A OE1   
1721 O  OE2   . GLU A 223 ? 0.77990 1.19410 1.02530 -0.12620 0.10540  -0.05260 223 GLU A OE2   
1722 N  N     . VAL A 224 ? 0.61960 0.82840 0.64390 -0.17970 0.07250  -0.02200 224 VAL A N     
1723 C  CA    . VAL A 224 ? 0.60800 0.78250 0.58750 -0.19540 0.06510  -0.01390 224 VAL A CA    
1724 C  C     . VAL A 224 ? 0.68780 0.86850 0.64510 -0.21870 0.07970  -0.01920 224 VAL A C     
1725 O  O     . VAL A 224 ? 0.77570 0.96340 0.72540 -0.22540 0.09620  -0.03130 224 VAL A O     
1726 C  CB    . VAL A 224 ? 0.62410 0.76630 0.57790 -0.19280 0.05870  -0.01370 224 VAL A CB    
1727 C  CG1   . VAL A 224 ? 0.62940 0.73790 0.54000 -0.20670 0.04790  -0.00290 224 VAL A CG1   
1728 C  CG2   . VAL A 224 ? 0.63490 0.77380 0.61360 -0.17250 0.04670  -0.00920 224 VAL A CG2   
1729 N  N     . ARG A 225 ? 0.58970 0.76460 0.53350 -0.23250 0.07480  -0.01070 225 ARG A N     
1730 C  CA    . ARG A 225 ? 0.65510 0.83410 0.57730 -0.25860 0.08750  -0.01300 225 ARG A CA    
1731 C  C     . ARG A 225 ? 0.68070 0.81280 0.55340 -0.27370 0.07680  -0.00030 225 ARG A C     
1732 O  O     . ARG A 225 ? 0.71950 0.82910 0.58920 -0.26360 0.05980  0.01010  225 ARG A O     
1733 C  CB    . ARG A 225 ? 0.72280 0.94280 0.68040 -0.26390 0.09220  -0.01580 225 ARG A CB    
1734 C  CG    . ARG A 225 ? 0.80460 1.07670 0.81090 -0.25390 0.10670  -0.02910 225 ARG A CG    
1735 C  CD    . ARG A 225 ? 0.74880 1.06570 0.78960 -0.26320 0.10930  -0.03090 225 ARG A CD    
1736 N  NE    . ARG A 225 ? 0.73870 1.10910 0.83380 -0.24910 0.12030  -0.04230 225 ARG A NE    
1737 C  CZ    . ARG A 225 ? 0.77260 1.16010 0.90650 -0.22170 0.10990  -0.04110 225 ARG A CZ    
1738 N  NH1   . ARG A 225 ? 0.78110 1.13930 0.90540 -0.20760 0.09000  -0.02980 225 ARG A NH1   
1739 N  NH2   . ARG A 225 ? 0.71380 1.14840 0.89760 -0.20790 0.12020  -0.05130 225 ARG A NH2   
1740 N  N     . ALA A 226 ? 0.75460 0.87140 0.58830 -0.29760 0.08770  -0.00100 226 ALA A N     
1741 C  CA    . ALA A 226 ? 0.75260 0.81940 0.53470 -0.31250 0.07720  0.01270  226 ALA A CA    
1742 C  C     . ALA A 226 ? 0.84410 0.90220 0.62330 -0.32460 0.07300  0.01960  226 ALA A C     
1743 O  O     . ALA A 226 ? 0.93190 1.02250 0.73070 -0.33890 0.08570  0.01270  226 ALA A O     
1744 C  CB    . ALA A 226 ? 0.82820 0.87860 0.56370 -0.33690 0.09070  0.01090  226 ALA A CB    
1745 N  N     . VAL A 227 ? 0.88690 0.90090 0.64230 -0.31890 0.05490  0.03260  227 VAL A N     
1746 C  CA    . VAL A 227 ? 0.87720 0.86700 0.61650 -0.33250 0.05060  0.03930  227 VAL A CA    
1747 C  C     . VAL A 227 ? 1.01860 0.95170 0.69930 -0.35080 0.04600  0.05180  227 VAL A C     
1748 O  O     . VAL A 227 ? 1.09010 0.99190 0.74930 -0.36440 0.04260  0.05800  227 VAL A O     
1749 C  CB    . VAL A 227 ? 0.74910 0.73090 0.50980 -0.30990 0.03520  0.04280  227 VAL A CB    
1750 C  CG1   . VAL A 227 ? 0.75630 0.79080 0.56910 -0.29500 0.03890  0.03270  227 VAL A CG1   
1751 C  CG2   . VAL A 227 ? 0.83630 0.78410 0.58400 -0.28870 0.01920  0.05250  227 VAL A CG2   
1752 N  N     . GLN A 228 ? 1.00620 0.92150 0.65730 -0.35220 0.04450  0.05620  228 GLN A N     
1753 C  CA    . GLN A 228 ? 1.03950 0.90510 0.62980 -0.37430 0.04230  0.06860  228 GLN A CA    
1754 C  C     . GLN A 228 ? 1.07140 0.95320 0.64120 -0.39010 0.05810  0.06190  228 GLN A C     
1755 O  O     . GLN A 228 ? 1.13310 1.05470 0.73470 -0.37700 0.06560  0.04900  228 GLN A O     
1756 C  CB    . GLN A 228 ? 1.10670 0.92100 0.67150 -0.35670 0.01700  0.08500  228 GLN A CB    
1757 C  CG    . GLN A 228 ? 1.07490 0.87020 0.65830 -0.33910 0.00400  0.08980  228 GLN A CG    
1758 C  CD    . GLN A 228 ? 1.12850 0.87620 0.69150 -0.32020 -0.01970 0.10570  228 GLN A CD    
1759 O  OE1   . GLN A 228 ? 1.33690 1.04030 0.85100 -0.33190 -0.02830 0.11960  228 GLN A OE1   
1760 N  NE2   . GLN A 228 ? 1.08010 0.83820 0.68130 -0.29070 -0.03050 0.10440  228 GLN A NE2   
1761 N  N     . GLU A 229 ? 1.12150 0.96890 0.63500 -0.41910 0.06420  0.07020  229 GLU A N     
1762 C  CA    . GLU A 229 ? 1.16150 1.01660 0.64470 -0.43510 0.07920  0.06440  229 GLU A CA    
1763 C  C     . GLU A 229 ? 1.18730 1.02540 0.65700 -0.41470 0.06040  0.06860  229 GLU A C     
1764 O  O     . GLU A 229 ? 1.14690 0.94270 0.59600 -0.40290 0.03450  0.08530  229 GLU A O     
1765 C  CB    . GLU A 229 ? 1.15740 0.97620 0.58670 -0.46260 0.08360  0.07030  229 GLU A CB    
1766 C  CG    . GLU A 229 ? 1.40700 1.22460 0.80040 -0.47370 0.09320  0.06380  229 GLU A CG    
1767 C  CD    . GLU A 229 ? 1.52120 1.32220 0.87800 -0.50040 0.10480  0.06190  229 GLU A CD    
1768 O  OE1   . GLU A 229 ? 1.69170 1.48730 1.05420 -0.51150 0.10740  0.06390  229 GLU A OE1   
1769 O  OE2   . GLU A 229 ? 1.49050 1.28390 0.81150 -0.51180 0.11200  0.05750  229 GLU A OE2   
1770 N  N     . ILE A 230 ? 1.22440 1.09660 0.70830 -0.41040 0.07340  0.05260  230 ILE A N     
1771 C  CA    . ILE A 230 ? 1.16750 1.02790 0.63880 -0.39540 0.05760  0.05320  230 ILE A CA    
1772 C  C     . ILE A 230 ? 1.21990 1.07050 0.63620 -0.42050 0.07300  0.04720  230 ILE A C     
1773 O  O     . ILE A 230 ? 1.21940 1.10360 0.64440 -0.43420 0.10330  0.02970  230 ILE A O     
1774 C  CB    . ILE A 230 ? 0.99290 0.89570 0.52690 -0.36690 0.05770  0.03820  230 ILE A CB    
1775 C  CG1   . ILE A 230 ? 0.92680 0.84150 0.51210 -0.34460 0.04580  0.04320  230 ILE A CG1   
1776 C  CG2   . ILE A 230 ? 1.11680 1.00420 0.63500 -0.35550 0.04000  0.03910  230 ILE A CG2   
1777 C  CD1   . ILE A 230 ? 0.92040 0.87590 0.56540 -0.31920 0.04780  0.03000  230 ILE A CD1   
1778 N  N     . LYS A 231 ? 1.22850 1.03430 0.58830 -0.42650 0.05250  0.06150  231 LYS A N     
1779 C  CA    . LYS A 231 ? 1.23620 1.02340 0.53120 -0.45220 0.06310  0.05840  231 LYS A CA    
1780 C  C     . LYS A 231 ? 1.21750 1.01020 0.51070 -0.43930 0.05320  0.04810  231 LYS A C     
1781 O  O     . LYS A 231 ? 1.28460 1.08240 0.61600 -0.41250 0.02970  0.05150  231 LYS A O     
1782 C  CB    . LYS A 231 ? 1.37230 1.10420 0.61570 -0.46350 0.04120  0.07900  231 LYS A CB    
1783 C  CG    . LYS A 231 ? 1.44740 1.16730 0.69570 -0.47400 0.04730  0.08620  231 LYS A CG    
1784 C  CD    . LYS A 231 ? 1.47820 1.14360 0.66840 -0.48980 0.03230  0.10230  231 LYS A CD    
1785 C  CE    . LYS A 231 ? 1.58800 1.22790 0.77990 -0.49410 0.02800  0.11440  231 LYS A CE    
1786 N  NZ    . LYS A 231 ? 1.64530 1.30390 0.83700 -0.51940 0.05760  0.10060  231 LYS A NZ    
1787 N  N     . PRO A 232 ? 1.26680 1.05890 0.51890 -0.45790 0.07120  0.03390  232 PRO A N     
1788 C  CA    . PRO A 232 ? 1.28540 1.07530 0.52470 -0.45030 0.06070  0.02360  232 PRO A CA    
1789 C  C     . PRO A 232 ? 1.31660 1.06940 0.53110 -0.44160 0.01710  0.04640  232 PRO A C     
1790 O  O     . PRO A 232 ? 1.39860 1.11370 0.57540 -0.45080 -0.00150 0.06780  232 PRO A O     
1791 C  CB    . PRO A 232 ? 1.32750 1.11060 0.52260 -0.47350 0.08380  0.00780  232 PRO A CB    
1792 C  CG    . PRO A 232 ? 1.29370 1.10340 0.51350 -0.48400 0.11680  -0.00140 232 PRO A CG    
1793 C  CD    . PRO A 232 ? 1.26290 1.06340 0.50160 -0.47970 0.10120  0.02050  232 PRO A CD    
1794 N  N     . GLY A 233 ? 1.30750 1.07510 0.56180 -0.41850 -0.00060 0.04030  233 GLY A N     
1795 C  CA    . GLY A 233 ? 1.41160 1.15650 0.65780 -0.40730 -0.04190 0.05920  233 GLY A CA    
1796 C  C     . GLY A 233 ? 1.35190 1.10470 0.65680 -0.38010 -0.06240 0.07500  233 GLY A C     
1797 O  O     . GLY A 233 ? 1.40430 1.15290 0.72470 -0.36450 -0.09370 0.08590  233 GLY A O     
1798 N  N     . GLU A 234 ? 1.38990 1.15570 0.72850 -0.37470 -0.04530 0.07560  234 GLU A N     
1799 C  CA    . GLU A 234 ? 1.35300 1.12280 0.74180 -0.34990 -0.06250 0.08870  234 GLU A CA    
1800 C  C     . GLU A 234 ? 1.29470 1.10640 0.75520 -0.32540 -0.05870 0.07410  234 GLU A C     
1801 O  O     . GLU A 234 ? 1.27380 1.11440 0.75570 -0.32680 -0.03430 0.05330  234 GLU A O     
1802 C  CB    . GLU A 234 ? 1.35050 1.11420 0.74340 -0.35580 -0.04730 0.09440  234 GLU A CB    
1803 C  CG    . GLU A 234 ? 1.55600 1.27330 0.87870 -0.38150 -0.04960 0.11120  234 GLU A CG    
1804 C  CD    . GLU A 234 ? 1.56810 1.27590 0.90040 -0.38580 -0.03870 0.11780  234 GLU A CD    
1805 O  OE1   . GLU A 234 ? 1.40150 1.14770 0.78240 -0.38130 -0.01680 0.10230  234 GLU A OE1   
1806 O  OE2   . GLU A 234 ? 1.67530 1.33550 0.96590 -0.39410 -0.05340 0.13870  234 GLU A OE2   
1807 N  N     . GLU A 235 ? 1.27430 1.08850 0.77230 -0.30250 -0.08240 0.08540  235 GLU A N     
1808 C  CA    . GLU A 235 ? 1.22360 1.07380 0.78640 -0.28060 -0.08060 0.07470  235 GLU A CA    
1809 C  C     . GLU A 235 ? 1.18120 1.05300 0.78660 -0.27080 -0.06110 0.06950  235 GLU A C     
1810 O  O     . GLU A 235 ? 1.18550 1.04120 0.78160 -0.27330 -0.06040 0.07970  235 GLU A O     
1811 C  CB    . GLU A 235 ? 1.21510 1.06430 0.80360 -0.26140 -0.11120 0.08830  235 GLU A CB    
1812 C  CG    . GLU A 235 ? 1.16540 1.05030 0.81880 -0.24130 -0.10800 0.07880  235 GLU A CG    
1813 C  CD    . GLU A 235 ? 1.16080 1.05210 0.83660 -0.22920 -0.13540 0.08710  235 GLU A CD    
1814 O  OE1   . GLU A 235 ? 1.19430 1.06420 0.84120 -0.23250 -0.16010 0.10210  235 GLU A OE1   
1815 O  OE2   . GLU A 235 ? 1.12430 1.04310 0.84750 -0.21720 -0.13280 0.07930  235 GLU A OE2   
1816 N  N     . VAL A 236 ? 1.06350 0.96920 0.71340 -0.26050 -0.04660 0.05390  236 VAL A N     
1817 C  CA    . VAL A 236 ? 0.84880 0.77900 0.54040 -0.25100 -0.03040 0.04860  236 VAL A CA    
1818 C  C     . VAL A 236 ? 0.89040 0.82830 0.62470 -0.22810 -0.04540 0.05710  236 VAL A C     
1819 O  O     . VAL A 236 ? 0.95990 0.91030 0.72030 -0.21610 -0.05430 0.05480  236 VAL A O     
1820 C  CB    . VAL A 236 ? 0.77150 0.73300 0.48880 -0.25020 -0.00800 0.02880  236 VAL A CB    
1821 C  CG1   . VAL A 236 ? 0.91060 0.89860 0.66770 -0.24220 0.00570  0.02510  236 VAL A CG1   
1822 C  CG2   . VAL A 236 ? 0.90680 0.86230 0.58240 -0.27190 0.00920  0.01780  236 VAL A CG2   
1823 N  N     . PHE A 237 ? 0.87880 0.80790 0.61840 -0.22360 -0.04700 0.06600  237 PHE A N     
1824 C  CA    . PHE A 237 ? 0.79300 0.72600 0.56750 -0.20270 -0.05840 0.07350  237 PHE A CA    
1825 C  C     . PHE A 237 ? 0.81660 0.76940 0.62040 -0.19740 -0.04320 0.06710  237 PHE A C     
1826 O  O     . PHE A 237 ? 0.80720 0.75350 0.59410 -0.21030 -0.03250 0.06560  237 PHE A O     
1827 C  CB    . PHE A 237 ? 0.88040 0.77860 0.63230 -0.19940 -0.07630 0.08980  237 PHE A CB    
1828 C  CG    . PHE A 237 ? 0.94410 0.82500 0.67250 -0.20070 -0.09780 0.09960  237 PHE A CG    
1829 C  CD1   . PHE A 237 ? 0.90940 0.80740 0.66940 -0.18560 -0.11310 0.10170  237 PHE A CD1   
1830 C  CD2   . PHE A 237 ? 0.99610 0.84380 0.66940 -0.21890 -0.10390 0.10770  237 PHE A CD2   
1831 C  CE1   . PHE A 237 ? 0.96030 0.84580 0.70030 -0.18810 -0.13610 0.11110  237 PHE A CE1   
1832 C  CE2   . PHE A 237 ? 1.01840 0.84960 0.66640 -0.22090 -0.12700 0.11810  237 PHE A CE2   
1833 C  CZ    . PHE A 237 ? 1.01570 0.86730 0.69850 -0.20520 -0.14430 0.11960  237 PHE A CZ    
1834 N  N     . THR A 238 ? 0.76430 0.74080 0.60960 -0.18060 -0.04310 0.06400  238 THR A N     
1835 C  CA    . THR A 238 ? 0.68630 0.67850 0.55750 -0.17310 -0.03410 0.06100  238 THR A CA    
1836 C  C     . THR A 238 ? 0.73970 0.72150 0.62450 -0.15720 -0.04400 0.06930  238 THR A C     
1837 O  O     . THR A 238 ? 0.79000 0.75940 0.67360 -0.14930 -0.05800 0.07720  238 THR A O     
1838 C  CB    . THR A 238 ? 0.62980 0.65500 0.53440 -0.16670 -0.02470 0.05160  238 THR A CB    
1839 O  OG1   . THR A 238 ? 0.77050 0.81140 0.69180 -0.16450 -0.01600 0.04860  238 THR A OG1   
1840 C  CG2   . THR A 238 ? 0.72170 0.75460 0.65220 -0.15180 -0.03370 0.05460  238 THR A CG2   
1841 N  N     . SER A 239 ? 0.67240 0.66030 0.57000 -0.15260 -0.03670 0.06690  239 SER A N     
1842 C  CA    . SER A 239 ? 0.64330 0.62450 0.55560 -0.13660 -0.04110 0.07130  239 SER A CA    
1843 C  C     . SER A 239 ? 0.67310 0.68430 0.62150 -0.12440 -0.03680 0.06810  239 SER A C     
1844 O  O     . SER A 239 ? 0.69920 0.73120 0.65770 -0.12830 -0.02810 0.06220  239 SER A O     
1845 C  CB    . SER A 239 ? 0.82300 0.78450 0.71830 -0.14120 -0.03570 0.07000  239 SER A CB    
1846 O  OG    . SER A 239 ? 0.80430 0.75830 0.71260 -0.12470 -0.03690 0.07150  239 SER A OG    
1847 N  N     . TYR A 240 ? 0.64300 0.65690 0.61140 -0.10980 -0.04300 0.07290  240 TYR A N     
1848 C  CA    . TYR A 240 ? 0.53930 0.57880 0.53920 -0.10030 -0.03780 0.07140  240 TYR A CA    
1849 C  C     . TYR A 240 ? 0.61980 0.65940 0.62520 -0.09230 -0.02920 0.06980  240 TYR A C     
1850 O  O     . TYR A 240 ? 0.79000 0.84940 0.81380 -0.08830 -0.02250 0.06860  240 TYR A O     
1851 C  CB    . TYR A 240 ? 0.57170 0.62050 0.59470 -0.09130 -0.04720 0.07670  240 TYR A CB    
1852 C  CG    . TYR A 240 ? 0.59270 0.64390 0.61160 -0.09970 -0.05670 0.07720  240 TYR A CG    
1853 C  CD1   . TYR A 240 ? 0.64490 0.68940 0.63990 -0.11330 -0.05380 0.07210  240 TYR A CD1   
1854 C  CD2   . TYR A 240 ? 0.61860 0.68000 0.65760 -0.09520 -0.06800 0.08160  240 TYR A CD2   
1855 C  CE1   . TYR A 240 ? 0.74370 0.78710 0.72980 -0.12180 -0.06070 0.07040  240 TYR A CE1   
1856 C  CE2   . TYR A 240 ? 0.63740 0.69830 0.66800 -0.10520 -0.07790 0.08080  240 TYR A CE2   
1857 C  CZ    . TYR A 240 ? 0.74050 0.79000 0.74190 -0.11830 -0.07360 0.07460  240 TYR A CZ    
1858 O  OH    . TYR A 240 ? 0.82420 0.87010 0.81190 -0.12900 -0.08160 0.07160  240 TYR A OH    
1859 N  N     . ILE A 241 ? 0.64450 0.65910 0.63080 -0.09090 -0.02890 0.06950  241 ILE A N     
1860 C  CA    . ILE A 241 ? 0.72730 0.73660 0.71680 -0.08110 -0.02080 0.06650  241 ILE A CA    
1861 C  C     . ILE A 241 ? 0.77080 0.75390 0.72860 -0.09060 -0.01680 0.06150  241 ILE A C     
1862 O  O     . ILE A 241 ? 0.79230 0.76160 0.72820 -0.10450 -0.02060 0.06170  241 ILE A O     
1863 C  CB    . ILE A 241 ? 0.67380 0.67680 0.68080 -0.06320 -0.02410 0.07040  241 ILE A CB    
1864 C  CG1   . ILE A 241 ? 0.66430 0.63780 0.65490 -0.06180 -0.03690 0.07620  241 ILE A CG1   
1865 C  CG2   . ILE A 241 ? 0.65780 0.69310 0.70090 -0.05620 -0.02590 0.07410  241 ILE A CG2   
1866 C  CD1   . ILE A 241 ? 0.73250 0.69450 0.73930 -0.04100 -0.04010 0.07930  241 ILE A CD1   
1867 N  N     . ASP A 242 ? 0.89490 0.87060 0.84860 -0.08490 -0.00810 0.05600  242 ASP A N     
1868 C  CA    . ASP A 242 ? 0.92740 0.87250 0.84930 -0.09390 -0.00470 0.04970  242 ASP A CA    
1869 C  C     . ASP A 242 ? 0.96690 0.87160 0.87340 -0.08800 -0.01050 0.05280  242 ASP A C     
1870 O  O     . ASP A 242 ? 0.98730 0.88390 0.90880 -0.06860 -0.01070 0.05470  242 ASP A O     
1871 C  CB    . ASP A 242 ? 1.02500 0.97020 0.94300 -0.08910 0.00660  0.04170  242 ASP A CB    
1872 C  CG    . ASP A 242 ? 1.02850 0.94500 0.91050 -0.10360 0.00960  0.03300  242 ASP A CG    
1873 O  OD1   . ASP A 242 ? 1.06640 0.95420 0.92710 -0.11390 0.00430  0.03360  242 ASP A OD1   
1874 O  OD2   . ASP A 242 ? 0.99100 0.91210 0.86320 -0.10650 0.01700  0.02570  242 ASP A OD2   
1875 N  N     . LEU A 243 ? 0.87330 0.75330 0.75100 -0.10470 -0.01520 0.05400  243 LEU A N     
1876 C  CA    . LEU A 243 ? 0.80950 0.64640 0.66640 -0.10260 -0.02340 0.06030  243 LEU A CA    
1877 C  C     . LEU A 243 ? 0.86680 0.65780 0.69810 -0.10050 -0.01820 0.05380  243 LEU A C     
1878 O  O     . LEU A 243 ? 0.99510 0.74110 0.80290 -0.10060 -0.02490 0.05920  243 LEU A O     
1879 C  CB    . LEU A 243 ? 0.78900 0.61950 0.62270 -0.12520 -0.02900 0.06520  243 LEU A CB    
1880 C  CG    . LEU A 243 ? 0.80390 0.67140 0.65620 -0.12810 -0.03340 0.06990  243 LEU A CG    
1881 C  CD1   . LEU A 243 ? 0.78950 0.65110 0.61560 -0.15230 -0.03380 0.07160  243 LEU A CD1   
1882 C  CD2   . LEU A 243 ? 0.89210 0.75890 0.76120 -0.10970 -0.04490 0.07910  243 LEU A CD2   
1883 N  N     . LEU A 244 ? 0.89250 0.69000 0.72410 -0.09940 -0.00680 0.04240  244 LEU A N     
1884 C  CA    . LEU A 244 ? 0.89470 0.64540 0.69790 -0.09910 -0.00030 0.03310  244 LEU A CA    
1885 C  C     . LEU A 244 ? 0.96380 0.68310 0.77580 -0.07130 -0.00060 0.03490  244 LEU A C     
1886 O  O     . LEU A 244 ? 1.17270 0.83720 0.95690 -0.06990 -0.00100 0.03260  244 LEU A O     
1887 C  CB    . LEU A 244 ? 0.87580 0.64430 0.67570 -0.10430 0.01160  0.02010  244 LEU A CB    
1888 C  CG    . LEU A 244 ? 1.05270 0.77570 0.81910 -0.10710 0.02060  0.00620  244 LEU A CG    
1889 C  CD1   . LEU A 244 ? 1.06070 0.74230 0.78840 -0.13230 0.01500  0.00510  244 LEU A CD1   
1890 C  CD2   . LEU A 244 ? 1.17910 0.92790 0.94180 -0.11330 0.03040  -0.00500 244 LEU A CD2   
1891 N  N     . TYR A 245 ? 0.89500 0.64780 0.74690 -0.04910 -0.00040 0.03900  245 TYR A N     
1892 C  CA    . TYR A 245 ? 0.98300 0.72150 0.85530 -0.01950 0.00390  0.03710  245 TYR A CA    
1893 C  C     . TYR A 245 ? 1.01840 0.73220 0.89720 -0.00510 -0.01300 0.05100  245 TYR A C     
1894 O  O     . TYR A 245 ? 1.02600 0.74480 0.89840 -0.01760 -0.02780 0.06330  245 TYR A O     
1895 C  CB    . TYR A 245 ? 0.94420 0.73620 0.85910 -0.00540 0.01350  0.03440  245 TYR A CB    
1896 C  CG    . TYR A 245 ? 0.98620 0.79390 0.88640 -0.01940 0.02880  0.02210  245 TYR A CG    
1897 C  CD1   . TYR A 245 ? 1.08160 0.86260 0.96220 -0.01400 0.04480  0.00710  245 TYR A CD1   
1898 C  CD2   . TYR A 245 ? 0.99020 0.83500 0.89200 -0.03840 0.02610  0.02540  245 TYR A CD2   
1899 C  CE1   . TYR A 245 ? 1.06450 0.85760 0.92540 -0.02890 0.05630  -0.00320 245 TYR A CE1   
1900 C  CE2   . TYR A 245 ? 0.99380 0.85160 0.88040 -0.05080 0.03650  0.01650  245 TYR A CE2   
1901 C  CZ    . TYR A 245 ? 1.02660 0.85890 0.89100 -0.04710 0.05070  0.00270  245 TYR A CZ    
1902 O  OH    . TYR A 245 ? 1.06170 0.90590 0.90580 -0.06120 0.05870  -0.00530 245 TYR A OH    
1903 N  N     . PRO A 246 ? 1.00140 0.68740 0.89200 0.02200  -0.01130 0.04950  246 PRO A N     
1904 C  CA    . PRO A 246 ? 1.03680 0.69630 0.93340 0.03830  -0.03050 0.06480  246 PRO A CA    
1905 C  C     . PRO A 246 ? 1.04650 0.75760 0.98410 0.04560  -0.04540 0.07830  246 PRO A C     
1906 O  O     . PRO A 246 ? 1.05770 0.82390 1.02430 0.04160  -0.03890 0.07500  246 PRO A O     
1907 C  CB    . PRO A 246 ? 1.13540 0.76320 1.04580 0.07010  -0.02200 0.05710  246 PRO A CB    
1908 C  CG    . PRO A 246 ? 1.08550 0.70340 0.97620 0.06260  0.00220  0.03620  246 PRO A CG    
1909 C  CD    . PRO A 246 ? 1.05330 0.72430 0.94660 0.03840  0.00870  0.03280  246 PRO A CD    
1910 N  N     . THR A 247 ? 1.09530 0.78380 1.03240 0.05590  -0.06710 0.09420  247 THR A N     
1911 C  CA    . THR A 247 ? 1.06730 0.79700 1.03310 0.05790  -0.08610 0.10830  247 THR A CA    
1912 C  C     . THR A 247 ? 1.03410 0.82280 1.06270 0.07910  -0.08070 0.10450  247 THR A C     
1913 O  O     . THR A 247 ? 1.05040 0.88920 1.10160 0.06870  -0.08360 0.10660  247 THR A O     
1914 C  CB    . THR A 247 ? 1.08990 0.77940 1.04160 0.06830  -0.11190 0.12670  247 THR A CB    
1915 O  OG1   . THR A 247 ? 1.14730 0.78280 1.03750 0.04370  -0.11550 0.13140  247 THR A OG1   
1916 C  CG2   . THR A 247 ? 1.01950 0.75090 0.99730 0.06870  -0.13420 0.14090  247 THR A CG2   
1917 N  N     . GLU A 248 ? 1.00060 0.78410 1.05860 0.10830  -0.07170 0.09840  248 GLU A N     
1918 C  CA    . GLU A 248 ? 1.00290 0.84690 1.12420 0.12710  -0.06530 0.09520  248 GLU A CA    
1919 C  C     . GLU A 248 ? 1.00200 0.88820 1.13060 0.11040  -0.04260 0.08240  248 GLU A C     
1920 O  O     . GLU A 248 ? 1.02010 0.96120 1.18750 0.10810  -0.04380 0.08510  248 GLU A O     
1921 C  CB    . GLU A 248 ? 1.09000 0.92210 1.24350 0.16280  -0.05580 0.08880  248 GLU A CB    
1922 C  CG    . GLU A 248 ? 1.14190 1.04240 1.36650 0.18180  -0.04750 0.08550  248 GLU A CG    
1923 C  CD    . GLU A 248 ? 1.35130 1.24820 1.60250 0.21030  -0.02170 0.06950  248 GLU A CD    
1924 O  OE1   . GLU A 248 ? 1.46530 1.30910 1.67360 0.20970  -0.00570 0.05700  248 GLU A OE1   
1925 O  OE2   . GLU A 248 ? 1.34510 1.29380 1.66050 0.23210  -0.01630 0.06820  248 GLU A OE2   
1926 N  N     . ASP A 249 ? 1.06910 0.92860 1.15760 0.09590  -0.02410 0.06960  249 ASP A N     
1927 C  CA    . ASP A 249 ? 1.03870 0.93360 1.12770 0.07900  -0.00560 0.05980  249 ASP A CA    
1928 C  C     . ASP A 249 ? 0.99790 0.92110 1.08220 0.05480  -0.01760 0.06850  249 ASP A C     
1929 O  O     . ASP A 249 ? 0.96130 0.93100 1.07330 0.04970  -0.01180 0.06810  249 ASP A O     
1930 C  CB    . ASP A 249 ? 1.06980 0.92660 1.11190 0.06700  0.01150  0.04580  249 ASP A CB    
1931 C  CG    . ASP A 249 ? 1.19250 1.02180 1.23700 0.09000  0.02900  0.03260  249 ASP A CG    
1932 O  OD1   . ASP A 249 ? 1.29620 1.13870 1.38360 0.11780  0.02860  0.03470  249 ASP A OD1   
1933 O  OD2   . ASP A 249 ? 1.14540 0.94040 1.14970 0.08050  0.04310  0.01920  249 ASP A OD2   
1934 N  N     . ARG A 250 ? 0.92890 0.82250 0.97840 0.04000  -0.03390 0.07650  250 ARG A N     
1935 C  CA    . ARG A 250 ? 0.85410 0.77000 0.89610 0.01790  -0.04360 0.08260  250 ARG A CA    
1936 C  C     . ARG A 250 ? 0.89400 0.85030 0.97760 0.02510  -0.05710 0.09170  250 ARG A C     
1937 O  O     . ARG A 250 ? 0.86480 0.85790 0.96430 0.01390  -0.05430 0.09080  250 ARG A O     
1938 C  CB    . ARG A 250 ? 0.89890 0.77370 0.89500 0.00160  -0.05640 0.08900  250 ARG A CB    
1939 C  CG    . ARG A 250 ? 0.99560 0.83390 0.94980 -0.01210 -0.04430 0.07990  250 ARG A CG    
1940 C  CD    . ARG A 250 ? 0.92110 0.73660 0.83510 -0.03670 -0.05320 0.08540  250 ARG A CD    
1941 N  NE    . ARG A 250 ? 0.94410 0.73250 0.84710 -0.03160 -0.07250 0.09940  250 ARG A NE    
1942 C  CZ    . ARG A 250 ? 1.03450 0.77190 0.91620 -0.02230 -0.07890 0.10460  250 ARG A CZ    
1943 N  NH1   . ARG A 250 ? 1.04700 0.75210 0.91540 -0.01700 -0.06620 0.09480  250 ARG A NH1   
1944 N  NH2   . ARG A 250 ? 1.18580 0.90110 1.05690 -0.01790 -0.09950 0.12000  250 ARG A NH2   
1945 N  N     . ASN A 251 ? 0.95920 0.90790 1.06110 0.04350  -0.07320 0.10080  251 ASN A N     
1946 C  CA    . ASN A 251 ? 0.96100 0.95000 1.10270 0.04810  -0.08950 0.10970  251 ASN A CA    
1947 C  C     . ASN A 251 ? 0.93950 0.97880 1.13550 0.05960  -0.07520 0.10370  251 ASN A C     
1948 O  O     . ASN A 251 ? 0.91680 0.99670 1.14200 0.05250  -0.08230 0.10730  251 ASN A O     
1949 C  CB    . ASN A 251 ? 0.96300 0.93140 1.10910 0.06450  -0.11430 0.12310  251 ASN A CB    
1950 C  CG    . ASN A 251 ? 0.97230 0.91210 1.07270 0.04520  -0.13520 0.13390  251 ASN A CG    
1951 O  OD1   . ASN A 251 ? 0.96710 0.93000 1.06370 0.02640  -0.14220 0.13550  251 ASN A OD1   
1952 N  ND2   . ASN A 251 ? 1.08150 0.96770 1.14410 0.04880  -0.14390 0.14080  251 ASN A ND2   
1953 N  N     . ASP A 252 ? 0.90980 0.94610 1.11730 0.07500  -0.05380 0.09360  252 ASP A N     
1954 C  CA    . ASP A 252 ? 0.86950 0.95250 1.12020 0.08050  -0.03440 0.08640  252 ASP A CA    
1955 C  C     . ASP A 252 ? 0.83740 0.94160 1.07620 0.05540  -0.02570 0.08370  252 ASP A C     
1956 O  O     . ASP A 252 ? 0.80660 0.95360 1.08040 0.04990  -0.02540 0.08630  252 ASP A O     
1957 C  CB    . ASP A 252 ? 0.90030 0.96820 1.15110 0.09760  -0.00950 0.07350  252 ASP A CB    
1958 C  CG    . ASP A 252 ? 1.08310 1.14040 1.36310 0.12870  -0.01520 0.07510  252 ASP A CG    
1959 O  OD1   . ASP A 252 ? 1.16360 1.21930 1.45660 0.13600  -0.04190 0.08840  252 ASP A OD1   
1960 O  OD2   . ASP A 252 ? 1.13340 1.18280 1.42220 0.14670  0.00670  0.06300  252 ASP A OD2   
1961 N  N     . ARG A 253 ? 0.78360 0.85730 0.97380 0.03930  -0.01990 0.07930  253 ARG A N     
1962 C  CA    . ARG A 253 ? 0.73260 0.82360 0.91210 0.01830  -0.01310 0.07760  253 ARG A CA    
1963 C  C     . ARG A 253 ? 0.73910 0.84520 0.92480 0.00520  -0.03210 0.08610  253 ARG A C     
1964 O  O     . ARG A 253 ? 0.79940 0.93450 1.00290 -0.00480 -0.02870 0.08680  253 ARG A O     
1965 C  CB    . ARG A 253 ? 0.79160 0.85080 0.92260 0.00540  -0.00520 0.07120  253 ARG A CB    
1966 C  CG    . ARG A 253 ? 0.85130 0.92860 0.97430 -0.01160 0.00330  0.06940  253 ARG A CG    
1967 C  CD    . ARG A 253 ? 0.95330 1.00650 1.03650 -0.02070 0.01300  0.06200  253 ARG A CD    
1968 N  NE    . ARG A 253 ? 1.11090 1.14510 1.18540 -0.00870 0.02630  0.05350  253 ARG A NE    
1969 C  CZ    . ARG A 253 ? 1.17190 1.21870 1.25240 -0.00420 0.04470  0.04720  253 ARG A CZ    
1970 N  NH1   . ARG A 253 ? 0.96360 1.04170 1.05850 -0.01130 0.05150  0.05030  253 ARG A NH1   
1971 N  NH2   . ARG A 253 ? 1.23490 1.25940 1.30390 0.00720  0.05760  0.03720  253 ARG A NH2   
1972 N  N     . LEU A 254 ? 0.74240 0.82530 0.90910 0.00360  -0.05150 0.09230  254 LEU A N     
1973 C  CA    . LEU A 254 ? 0.72890 0.82130 0.89320 -0.01060 -0.06890 0.09830  254 LEU A CA    
1974 C  C     . LEU A 254 ? 0.71360 0.84530 0.92550 -0.00560 -0.07840 0.10320  254 LEU A C     
1975 O  O     . LEU A 254 ? 0.69740 0.84950 0.91780 -0.01990 -0.08180 0.10350  254 LEU A O     
1976 C  CB    . LEU A 254 ? 0.73350 0.79100 0.86310 -0.01400 -0.08710 0.10470  254 LEU A CB    
1977 C  CG    . LEU A 254 ? 0.78830 0.80910 0.86920 -0.02590 -0.07990 0.10060  254 LEU A CG    
1978 C  CD1   . LEU A 254 ? 0.89840 0.88400 0.94600 -0.02940 -0.09760 0.10900  254 LEU A CD1   
1979 C  CD2   . LEU A 254 ? 0.72560 0.75910 0.79420 -0.04510 -0.07160 0.09480  254 LEU A CD2   
1980 N  N     . ARG A 255 ? 0.69760 0.84080 0.94290 0.01470  -0.08250 0.10660  255 ARG A N     
1981 C  CA    . ARG A 255 ? 0.70090 0.88930 0.99990 0.01990  -0.09060 0.11080  255 ARG A CA    
1982 C  C     . ARG A 255 ? 0.66990 0.89170 0.99380 0.01150  -0.06930 0.10470  255 ARG A C     
1983 O  O     . ARG A 255 ? 0.66570 0.91730 1.01340 -0.00120 -0.07550 0.10710  255 ARG A O     
1984 C  CB    . ARG A 255 ? 0.72800 0.92340 1.06180 0.04720  -0.09530 0.11430  255 ARG A CB    
1985 C  CG    . ARG A 255 ? 0.80940 0.97970 1.12790 0.05410  -0.12480 0.12550  255 ARG A CG    
1986 C  CD    . ARG A 255 ? 0.88900 1.07490 1.25410 0.08320  -0.13490 0.13140  255 ARG A CD    
1987 N  NE    . ARG A 255 ? 0.97460 1.12790 1.32870 0.10350  -0.11670 0.12480  255 ARG A NE    
1988 C  CZ    . ARG A 255 ? 1.04420 1.14710 1.36600 0.11530  -0.12780 0.13020  255 ARG A CZ    
1989 N  NH1   . ARG A 255 ? 0.86540 0.94510 1.16110 0.10950  -0.15730 0.14390  255 ARG A NH1   
1990 N  NH2   . ARG A 255 ? 1.15460 1.22590 1.46570 0.13170  -0.10840 0.12160  255 ARG A NH2   
1991 N  N     . ASP A 256 ? 0.80250 1.01690 1.11800 0.01700  -0.04440 0.09700  256 ASP A N     
1992 C  CA    . ASP A 256 ? 0.77810 1.02160 1.11370 0.00950  -0.02320 0.09300  256 ASP A CA    
1993 C  C     . ASP A 256 ? 0.75470 0.99490 1.06800 -0.01400 -0.02440 0.09390  256 ASP A C     
1994 O  O     . ASP A 256 ? 0.77400 1.04240 1.11290 -0.02490 -0.02120 0.09600  256 ASP A O     
1995 C  CB    . ASP A 256 ? 0.80140 1.03000 1.11990 0.01840  0.00210  0.08430  256 ASP A CB    
1996 C  CG    . ASP A 256 ? 0.91740 1.17620 1.25620 0.01280  0.02550  0.08120  256 ASP A CG    
1997 O  OD1   . ASP A 256 ? 0.96250 1.26170 1.34780 0.01180  0.02590  0.08460  256 ASP A OD1   
1998 O  OD2   . ASP A 256 ? 1.03050 1.27230 1.33650 0.00690  0.04280  0.07600  256 ASP A OD2   
1999 N  N     . SER A 257 ? 0.72610 0.93180 0.99340 -0.02210 -0.02860 0.09240  257 SER A N     
2000 C  CA    . SER A 257 ? 0.71150 0.91240 0.95900 -0.04040 -0.02670 0.09190  257 SER A CA    
2001 C  C     . SER A 257 ? 0.70290 0.90140 0.94580 -0.05270 -0.04630 0.09460  257 SER A C     
2002 O  O     . SER A 257 ? 0.71150 0.91730 0.95790 -0.06610 -0.04520 0.09450  257 SER A O     
2003 C  CB    . SER A 257 ? 0.74550 0.91710 0.95050 -0.04310 -0.01810 0.08730  257 SER A CB    
2004 O  OG    . SER A 257 ? 0.70540 0.87830 0.90880 -0.03600 0.00080  0.08360  257 SER A OG    
2005 N  N     . TYR A 258 ? 0.66570 0.85070 0.89760 -0.04930 -0.06410 0.09700  258 TYR A N     
2006 C  CA    . TYR A 258 ? 0.64590 0.82170 0.86060 -0.06290 -0.08150 0.09800  258 TYR A CA    
2007 C  C     . TYR A 258 ? 0.67840 0.86880 0.91510 -0.05990 -0.10370 0.10440  258 TYR A C     
2008 O  O     . TYR A 258 ? 0.74200 0.92480 0.96200 -0.07220 -0.12050 0.10520  258 TYR A O     
2009 C  CB    . TYR A 258 ? 0.69510 0.83600 0.86250 -0.06710 -0.08310 0.09550  258 TYR A CB    
2010 C  CG    . TYR A 258 ? 0.72980 0.86030 0.87810 -0.07010 -0.06450 0.08960  258 TYR A CG    
2011 C  CD1   . TYR A 258 ? 0.73520 0.86960 0.88060 -0.08090 -0.05760 0.08570  258 TYR A CD1   
2012 C  CD2   . TYR A 258 ? 0.72950 0.84510 0.86300 -0.06180 -0.05500 0.08810  258 TYR A CD2   
2013 C  CE1   . TYR A 258 ? 0.68970 0.81760 0.82060 -0.08200 -0.04380 0.08210  258 TYR A CE1   
2014 C  CE2   . TYR A 258 ? 0.70990 0.81920 0.82650 -0.06590 -0.04110 0.08320  258 TYR A CE2   
2015 C  CZ    . TYR A 258 ? 0.65580 0.77340 0.77260 -0.07530 -0.03640 0.08100  258 TYR A CZ    
2016 O  OH    . TYR A 258 ? 0.58980 0.70390 0.69250 -0.07780 -0.02560 0.07780  258 TYR A OH    
2017 N  N     . PHE A 259 ? 0.69110 0.90220 0.96410 -0.04320 -0.10450 0.10850  259 PHE A N     
2018 C  CA    . PHE A 259 ? 0.66140 0.89850 0.96990 -0.03820 -0.12590 0.11550  259 PHE A CA    
2019 C  C     . PHE A 259 ? 0.62180 0.83280 0.89860 -0.03900 -0.15180 0.12200  259 PHE A C     
2020 O  O     . PHE A 259 ? 0.65280 0.87370 0.93200 -0.05020 -0.17380 0.12590  259 PHE A O     
2021 C  CB    . PHE A 259 ? 0.70560 0.97470 1.04240 -0.05550 -0.13020 0.11460  259 PHE A CB    
2022 C  CG    . PHE A 259 ? 0.69950 0.99080 1.06230 -0.05870 -0.10510 0.11040  259 PHE A CG    
2023 C  CD1   . PHE A 259 ? 0.75600 1.08510 1.16920 -0.04680 -0.09490 0.11190  259 PHE A CD1   
2024 C  CD2   . PHE A 259 ? 0.69510 0.96930 1.03130 -0.07390 -0.09160 0.10530  259 PHE A CD2   
2025 C  CE1   . PHE A 259 ? 0.80060 1.14790 1.23140 -0.05280 -0.07050 0.10890  259 PHE A CE1   
2026 C  CE2   . PHE A 259 ? 0.71880 1.00850 1.07290 -0.07820 -0.07030 0.10390  259 PHE A CE2   
2027 C  CZ    . PHE A 259 ? 0.75430 1.07970 1.15290 -0.06920 -0.05930 0.10590  259 PHE A CZ    
2028 N  N     . PHE A 260 ? 0.64220 0.81700 0.88490 -0.02940 -0.14930 0.12330  260 PHE A N     
2029 C  CA    . PHE A 260 ? 0.68720 0.83360 0.89830 -0.02860 -0.17320 0.13210  260 PHE A CA    
2030 C  C     . PHE A 260 ? 0.66650 0.78070 0.86160 -0.01030 -0.16830 0.13520  260 PHE A C     
2031 O  O     . PHE A 260 ? 0.75000 0.85550 0.94200 -0.00470 -0.14480 0.12760  260 PHE A O     
2032 C  CB    . PHE A 260 ? 0.70940 0.82800 0.86630 -0.05190 -0.17680 0.12890  260 PHE A CB    
2033 C  CG    . PHE A 260 ? 0.72710 0.81460 0.84510 -0.05630 -0.15580 0.12200  260 PHE A CG    
2034 C  CD1   . PHE A 260 ? 0.72940 0.82640 0.85090 -0.06340 -0.13340 0.11170  260 PHE A CD1   
2035 C  CD2   . PHE A 260 ? 0.81300 0.86130 0.89040 -0.05480 -0.16010 0.12680  260 PHE A CD2   
2036 C  CE1   . PHE A 260 ? 0.76390 0.83780 0.85380 -0.06790 -0.11690 0.10590  260 PHE A CE1   
2037 C  CE2   . PHE A 260 ? 0.82740 0.85150 0.87230 -0.06170 -0.14160 0.12020  260 PHE A CE2   
2038 C  CZ    . PHE A 260 ? 0.73460 0.77420 0.78770 -0.06790 -0.12060 0.10940  260 PHE A CZ    
2039 N  N     . THR A 261 ? 0.72370 0.81640 0.90480 -0.00210 -0.19190 0.14690  261 THR A N     
2040 C  CA    . THR A 261 ? 0.74830 0.79940 0.90640 0.01350  -0.19100 0.15150  261 THR A CA    
2041 C  C     . THR A 261 ? 0.82200 0.82350 0.91270 -0.00360 -0.19910 0.15640  261 THR A C     
2042 O  O     . THR A 261 ? 0.91780 0.91270 0.98620 -0.01460 -0.22250 0.16550  261 THR A O     
2043 C  CB    . THR A 261 ? 0.79890 0.85890 0.99560 0.04030  -0.21090 0.16300  261 THR A CB    
2044 O  OG1   . THR A 261 ? 0.75960 0.86790 1.02120 0.05640  -0.19780 0.15670  261 THR A OG1   
2045 C  CG2   . THR A 261 ? 0.90850 0.91640 1.07730 0.05680  -0.21100 0.16820  261 THR A CG2   
2046 N  N     . CYS A 262 ? 0.79710 0.76540 0.85420 -0.00790 -0.17930 0.14980  262 CYS A N     
2047 C  CA    . CYS A 262 ? 0.87080 0.79570 0.86560 -0.02760 -0.18100 0.15250  262 CYS A CA    
2048 C  C     . CYS A 262 ? 0.97010 0.85100 0.93820 -0.01800 -0.20190 0.16810  262 CYS A C     
2049 O  O     . CYS A 262 ? 0.88580 0.75460 0.87610 0.00670  -0.20410 0.17230  262 CYS A O     
2050 C  CB    . CYS A 262 ? 0.86160 0.77130 0.83450 -0.03740 -0.15410 0.14030  262 CYS A CB    
2051 S  SG    . CYS A 262 ? 0.94660 0.81520 0.85040 -0.06610 -0.15210 0.14140  262 CYS A SG    
2052 N  N     . GLU A 263 ? 1.00040 0.85480 0.91790 -0.03800 -0.21620 0.17660  263 GLU A N     
2053 C  CA    . GLU A 263 ? 1.06210 0.86940 0.94210 -0.03470 -0.23890 0.19450  263 GLU A CA    
2054 C  C     . GLU A 263 ? 1.07450 0.83240 0.88540 -0.05980 -0.23020 0.19600  263 GLU A C     
2055 O  O     . GLU A 263 ? 1.13000 0.84860 0.89370 -0.06870 -0.24950 0.21170  263 GLU A O     
2056 C  CB    . GLU A 263 ? 1.08210 0.90660 0.96670 -0.03510 -0.27060 0.20740  263 GLU A CB    
2057 C  CG    . GLU A 263 ? 1.18520 1.05860 1.14450 -0.00870 -0.27820 0.20670  263 GLU A CG    
2058 C  CD    . GLU A 263 ? 1.36710 1.26660 1.34330 -0.00740 -0.31190 0.21900  263 GLU A CD    
2059 O  OE1   . GLU A 263 ? 1.34860 1.21820 1.27290 -0.02240 -0.33460 0.23190  263 GLU A OE1   
2060 O  OE2   . GLU A 263 ? 1.45750 1.40530 1.49920 0.01030  -0.31690 0.21730  263 GLU A OE2   
2061 N  N     . CYS A 264 ? 1.13140 0.89190 0.93580 -0.07230 -0.20180 0.18060  264 CYS A N     
2062 C  CA    . CYS A 264 ? 1.14130 0.86400 0.88950 -0.09740 -0.18920 0.17940  264 CYS A CA    
2063 C  C     . CYS A 264 ? 1.29690 0.96050 1.01690 -0.08960 -0.19510 0.19100  264 CYS A C     
2064 O  O     . CYS A 264 ? 1.28890 0.94160 1.03580 -0.06160 -0.20690 0.19810  264 CYS A O     
2065 C  CB    . CYS A 264 ? 1.11170 0.86040 0.87180 -0.10930 -0.15980 0.16010  264 CYS A CB    
2066 S  SG    . CYS A 264 ? 1.07280 0.81170 0.85710 -0.09230 -0.14240 0.15100  264 CYS A SG    
2067 N  N     . GLN A 265 ? 1.41790 1.04200 1.08380 -0.11480 -0.18560 0.19240  265 GLN A N     
2068 C  CA    . GLN A 265 ? 1.47690 1.03530 1.10670 -0.11200 -0.19220 0.20480  265 GLN A CA    
2069 C  C     . GLN A 265 ? 1.47180 1.02070 1.13380 -0.08910 -0.18090 0.19580  265 GLN A C     
2070 O  O     . GLN A 265 ? 1.51280 1.02020 1.17420 -0.06710 -0.19390 0.20650  265 GLN A O     
2071 C  CB    . GLN A 265 ? 1.56900 1.09290 1.13860 -0.14820 -0.17880 0.20490  265 GLN A CB    
2072 C  CG    . GLN A 265 ? 1.67960 1.15460 1.18840 -0.16380 -0.19800 0.22630  265 GLN A CG    
2073 C  CD    . GLN A 265 ? 1.84240 1.35020 1.33960 -0.17760 -0.20660 0.22850  265 GLN A CD    
2074 O  OE1   . GLN A 265 ? 1.85850 1.41530 1.37380 -0.18990 -0.18890 0.21140  265 GLN A OE1   
2075 N  NE2   . GLN A 265 ? 1.81540 1.29450 1.28140 -0.17490 -0.23520 0.24950  265 GLN A NE2   
2076 N  N     . GLU A 266 ? 1.35250 0.93860 1.04270 -0.09240 -0.15720 0.17600  266 GLU A N     
2077 C  CA    . GLU A 266 ? 1.29870 0.87530 1.01360 -0.07300 -0.14490 0.16550  266 GLU A CA    
2078 C  C     . GLU A 266 ? 1.28900 0.88680 1.05640 -0.03580 -0.15550 0.16800  266 GLU A C     
2079 O  O     . GLU A 266 ? 1.34940 0.91500 1.12560 -0.01300 -0.15530 0.16790  266 GLU A O     
2080 C  CB    . GLU A 266 ? 1.30700 0.92110 1.03710 -0.08640 -0.11960 0.14520  266 GLU A CB    
2081 C  CG    . GLU A 266 ? 1.45810 1.06410 1.20880 -0.06890 -0.10570 0.13250  266 GLU A CG    
2082 C  CD    . GLU A 266 ? 1.60050 1.13820 1.30880 -0.07590 -0.10220 0.13260  266 GLU A CD    
2083 O  OE1   . GLU A 266 ? 1.62050 1.11260 1.28400 -0.09220 -0.11220 0.14560  266 GLU A OE1   
2084 O  OE2   . GLU A 266 ? 1.62890 1.15540 1.34600 -0.06570 -0.08890 0.11950  266 GLU A OE2   
2085 N  N     . CYS A 267 ? 1.24420 0.89550 1.04780 -0.02950 -0.16440 0.16960  267 CYS A N     
2086 C  CA    . CYS A 267 ? 1.20770 0.88650 1.06680 0.00370  -0.17430 0.17210  267 CYS A CA    
2087 C  C     . CYS A 267 ? 1.31300 0.95480 1.16520 0.02300  -0.20240 0.19240  267 CYS A C     
2088 O  O     . CYS A 267 ? 1.35850 0.99510 1.24630 0.05500  -0.20630 0.19390  267 CYS A O     
2089 C  CB    . CYS A 267 ? 1.15260 0.89770 1.05060 0.00080  -0.17680 0.16850  267 CYS A CB    
2090 S  SG    . CYS A 267 ? 1.06740 0.85950 0.98860 -0.01100 -0.14590 0.14650  267 CYS A SG    
2091 N  N     . THR A 268 ? 1.30100 0.91660 1.10770 0.00500  -0.22230 0.20840  268 THR A N     
2092 C  CA    . THR A 268 ? 1.42430 1.00290 1.22080 0.02310  -0.25300 0.23080  268 THR A CA    
2093 C  C     . THR A 268 ? 1.53590 1.04360 1.30670 0.03630  -0.25050 0.23550  268 THR A C     
2094 O  O     . THR A 268 ? 1.55580 1.04810 1.35680 0.07080  -0.26350 0.24320  268 THR A O     
2095 C  CB    . THR A 268 ? 1.36430 0.92770 1.10830 -0.00320 -0.27400 0.24690  268 THR A CB    
2096 O  OG1   . THR A 268 ? 1.49520 1.03170 1.18220 -0.03870 -0.25470 0.24060  268 THR A OG1   
2097 C  CG2   . THR A 268 ? 1.24620 0.87500 1.02190 -0.00830 -0.28380 0.24420  268 THR A CG2   
2098 N  N     . THR A 269 ? 1.66300 1.12640 1.37930 0.00910  -0.23370 0.23050  269 THR A N     
2099 C  CA    . THR A 269 ? 1.75070 1.13730 1.43240 0.01520  -0.23150 0.23510  269 THR A CA    
2100 C  C     . THR A 269 ? 1.74500 1.13220 1.46040 0.03490  -0.20690 0.21400  269 THR A C     
2101 O  O     . THR A 269 ? 1.76570 1.09980 1.47890 0.05850  -0.20970 0.21690  269 THR A O     
2102 C  CB    . THR A 269 ? 1.81430 1.15390 1.42220 -0.02600 -0.22540 0.23990  269 THR A CB    
2103 O  OG1   . THR A 269 ? 1.83900 1.21510 1.44790 -0.05230 -0.19690 0.21840  269 THR A OG1   
2104 C  CG2   . THR A 269 ? 1.77770 1.11740 1.34970 -0.04450 -0.24840 0.25990  269 THR A CG2   
2105 N  N     . LYS A 270 ? 1.62390 1.06630 1.36640 0.02490  -0.18270 0.19260  270 LYS A N     
2106 C  CA    . LYS A 270 ? 1.56470 1.01220 1.33000 0.03550  -0.15640 0.17040  270 LYS A CA    
2107 C  C     . LYS A 270 ? 1.67100 1.04890 1.38560 0.02030  -0.14280 0.16310  270 LYS A C     
2108 O  O     . LYS A 270 ? 1.74630 1.10050 1.47130 0.03860  -0.12910 0.14980  270 LYS A O     
2109 C  CB    . LYS A 270 ? 1.51430 0.97400 1.33550 0.08000  -0.16040 0.16930  270 LYS A CB    
2110 C  CG    . LYS A 270 ? 1.37780 0.90730 1.25380 0.09470  -0.17510 0.17650  270 LYS A CG    
2111 C  CD    . LYS A 270 ? 1.23800 0.78520 1.17520 0.13820  -0.17770 0.17520  270 LYS A CD    
2112 C  CE    . LYS A 270 ? 1.26410 0.88600 1.25820 0.14820  -0.19240 0.18180  270 LYS A CE    
2113 N  NZ    . LYS A 270 ? 1.36110 1.00770 1.42170 0.19060  -0.19580 0.18150  270 LYS A NZ    
2114 N  N     . ASP A 271 ? 1.88100 1.22250 1.53890 -0.01380 -0.14610 0.17150  271 ASP A N     
2115 C  CA    . ASP A 271 ? 1.97330 1.24140 1.57920 -0.03130 -0.13710 0.16800  271 ASP A CA    
2116 C  C     . ASP A 271 ? 1.91790 1.19580 1.52240 -0.04700 -0.11020 0.14290  271 ASP A C     
2117 O  O     . ASP A 271 ? 1.96350 1.18630 1.55100 -0.03950 -0.10170 0.13370  271 ASP A O     
2118 C  CB    . ASP A 271 ? 2.04060 1.27640 1.58950 -0.06670 -0.14680 0.18440  271 ASP A CB    
2119 C  CG    . ASP A 271 ? 2.11090 1.34870 1.65980 -0.05490 -0.17400 0.20820  271 ASP A CG    
2120 O  OD1   . ASP A 271 ? 2.20710 1.40640 1.76340 -0.02330 -0.19270 0.22200  271 ASP A OD1   
2121 O  OD2   . ASP A 271 ? 2.09190 1.36870 1.63160 -0.07800 -0.17710 0.21300  271 ASP A OD2   
2122 N  N     . LYS A 272 ? 1.66740 1.01700 1.30040 -0.05790 -0.09730 0.12970  272 LYS A N     
2123 C  CA    . LYS A 272 ? 1.63890 0.99080 1.26260 -0.07540 -0.07580 0.10860  272 LYS A CA    
2124 C  C     . LYS A 272 ? 1.65820 1.02300 1.31860 -0.04410 -0.06430 0.09320  272 LYS A C     
2125 O  O     . LYS A 272 ? 1.67750 1.03050 1.32620 -0.05200 -0.04750 0.07470  272 LYS A O     
2126 C  CB    . LYS A 272 ? 1.42830 0.84730 1.06240 -0.10260 -0.06690 0.10150  272 LYS A CB    
2127 C  CG    . LYS A 272 ? 1.37760 0.79820 0.98100 -0.13510 -0.07330 0.11350  272 LYS A CG    
2128 C  CD    . LYS A 272 ? 1.26700 0.75460 0.88720 -0.15750 -0.06150 0.10290  272 LYS A CD    
2129 C  CE    . LYS A 272 ? 1.26450 0.73980 0.85460 -0.19240 -0.04920 0.09270  272 LYS A CE    
2130 N  NZ    . LYS A 272 ? 1.25940 0.79900 0.86570 -0.21410 -0.04160 0.08730  272 LYS A NZ    
2131 N  N     . ASP A 273 ? 1.60910 0.98750 1.30820 -0.00870 -0.07470 0.10180  273 ASP A N     
2132 C  CA    . ASP A 273 ? 1.54570 0.94130 1.28700 0.02530  -0.06350 0.08900  273 ASP A CA    
2133 C  C     . ASP A 273 ? 1.52030 0.84120 1.22960 0.03200  -0.05330 0.07750  273 ASP A C     
2134 O  O     . ASP A 273 ? 1.49750 0.82220 1.21750 0.04260  -0.03350 0.05720  273 ASP A O     
2135 C  CB    . ASP A 273 ? 1.55970 0.98350 1.35000 0.06000  -0.07940 0.10260  273 ASP A CB    
2136 C  CG    . ASP A 273 ? 1.41660 0.92490 1.24930 0.05620  -0.08060 0.10410  273 ASP A CG    
2137 O  OD1   . ASP A 273 ? 1.34030 0.87810 1.15870 0.02650  -0.07250 0.09830  273 ASP A OD1   
2138 O  OD2   . ASP A 273 ? 1.33050 0.87560 1.21210 0.08280  -0.08970 0.11080  273 ASP A OD2   
2139 N  N     . LYS A 274 ? 1.55660 0.80430 1.22380 0.02660  -0.06700 0.09090  274 LYS A N     
2140 C  CA    . LYS A 274 ? 1.63470 0.80300 1.27280 0.03740  -0.05860 0.08050  274 LYS A CA    
2141 C  C     . LYS A 274 ? 1.61650 0.77040 1.21680 0.00360  -0.03880 0.05910  274 LYS A C     
2142 O  O     . LYS A 274 ? 1.59840 0.72010 1.19140 0.01450  -0.02210 0.03890  274 LYS A O     
2143 C  CB    . LYS A 274 ? 1.74730 0.83530 1.34200 0.03390  -0.07880 0.10190  274 LYS A CB    
2144 C  CG    . LYS A 274 ? 1.77960 0.86770 1.40230 0.06690  -0.10390 0.12620  274 LYS A CG    
2145 C  CD    . LYS A 274 ? 1.90450 0.89590 1.47540 0.06530  -0.12210 0.14590  274 LYS A CD    
2146 C  CE    . LYS A 274 ? 1.93960 0.92730 1.53620 0.09970  -0.15110 0.17210  274 LYS A CE    
2147 N  NZ    . LYS A 274 ? 1.98390 0.87080 1.52580 0.09910  -0.17020 0.19350  274 LYS A NZ    
2148 N  N     . ALA A 275 ? 1.66030 0.83880 1.23670 -0.03790 -0.04020 0.06240  275 ALA A N     
2149 C  CA    . ALA A 275 ? 1.62420 0.80440 1.17330 -0.07080 -0.02410 0.04270  275 ALA A CA    
2150 C  C     . ALA A 275 ? 1.55760 0.80360 1.14320 -0.06100 -0.00790 0.02410  275 ALA A C     
2151 O  O     . ALA A 275 ? 1.51040 0.74100 1.07630 -0.07100 0.00710  0.00340  275 ALA A O     
2152 C  CB    . ALA A 275 ? 1.57990 0.77980 1.10390 -0.11490 -0.02970 0.05160  275 ALA A CB    
2153 N  N     . LYS A 276 ? 1.56740 0.88350 1.20290 -0.04250 -0.01150 0.03160  276 LYS A N     
2154 C  CA    . LYS A 276 ? 1.40520 0.78710 1.07650 -0.03430 0.00250  0.01820  276 LYS A CA    
2155 C  C     . LYS A 276 ? 1.41290 0.77810 1.09950 -0.00230 0.01830  0.00200  276 LYS A C     
2156 O  O     . LYS A 276 ? 1.45620 0.84810 1.14570 -0.00550 0.03520  -0.01540 276 LYS A O     
2157 C  CB    . LYS A 276 ? 1.35940 0.81210 1.07730 -0.02480 -0.00710 0.03250  276 LYS A CB    
2158 C  CG    . LYS A 276 ? 1.30570 0.79000 1.01230 -0.05770 -0.01620 0.04250  276 LYS A CG    
2159 C  CD    . LYS A 276 ? 1.21320 0.75430 0.96000 -0.04740 -0.02720 0.05650  276 LYS A CD    
2160 C  CE    . LYS A 276 ? 1.15230 0.72480 0.88790 -0.07880 -0.03220 0.06270  276 LYS A CE    
2161 N  NZ    . LYS A 276 ? 1.01340 0.64020 0.78520 -0.07070 -0.04080 0.07270  276 LYS A NZ    
2162 N  N     . VAL A 277 ? 1.47990 0.80050 1.17510 0.02890  0.01350  0.00730  277 VAL A N     
2163 C  CA    . VAL A 277 ? 1.51280 0.81620 1.22670 0.06320  0.03050  -0.00900 277 VAL A CA    
2164 C  C     . VAL A 277 ? 1.64330 0.85130 1.30790 0.06290  0.03500  -0.01930 277 VAL A C     
2165 O  O     . VAL A 277 ? 1.59800 0.75860 1.27190 0.09550  0.03150  -0.01580 277 VAL A O     
2166 C  CB    . VAL A 277 ? 1.39500 0.72900 1.16880 0.10480  0.02270  0.00340  277 VAL A CB    
2167 C  CG1   . VAL A 277 ? 1.34440 0.68590 1.15000 0.13900  0.04600  -0.01620 277 VAL A CG1   
2168 C  CG2   . VAL A 277 ? 1.31540 0.73170 1.12870 0.09770  0.01160  0.01820  277 VAL A CG2   
2169 N  N     . GLU A 278 ? 1.79640 0.97390 1.40840 0.02510  0.04030  -0.03060 278 GLU A N     
2170 C  CA    . GLU A 278 ? 1.87550 0.95710 1.43430 0.01770  0.04280  -0.03970 278 GLU A CA    
2171 C  C     . GLU A 278 ? 1.93090 0.97720 1.49110 0.04790  0.06500  -0.06430 278 GLU A C     
2172 O  O     . GLU A 278 ? 1.90150 0.98980 1.47210 0.04860  0.08420  -0.08350 278 GLU A O     
2173 C  CB    . GLU A 278 ? 1.88560 0.95450 1.39260 -0.03330 0.04410  -0.04820 278 GLU A CB    
2174 C  CG    . GLU A 278 ? 1.96740 0.93770 1.41380 -0.05340 0.04210  -0.05300 278 GLU A CG    
2175 C  CD    . GLU A 278 ? 2.05260 0.99030 1.48140 -0.06830 0.02100  -0.02680 278 GLU A CD    
2176 O  OE1   . GLU A 278 ? 1.93730 0.93420 1.38050 -0.08870 0.01010  -0.01080 278 GLU A OE1   
2177 O  OE2   . GLU A 278 ? 2.17250 1.02240 1.57060 -0.05940 0.01590  -0.02210 278 GLU A OE2   
2178 N  N     . ILE A 279 ? 2.02090 0.98770 1.56890 0.07350  0.06290  -0.06370 279 ILE A N     
2179 C  CA    . ILE A 279 ? 2.03140 0.95400 1.58000 0.10610  0.08520  -0.08810 279 ILE A CA    
2180 C  C     . ILE A 279 ? 2.15340 0.98050 1.62820 0.07820  0.09120  -0.10500 279 ILE A C     
2181 O  O     . ILE A 279 ? 2.13830 0.91280 1.57570 0.05410  0.07300  -0.08930 279 ILE A O     
2182 C  CB    . ILE A 279 ? 2.00620 0.90570 1.59820 0.15830  0.07730  -0.07520 279 ILE A CB    
2183 C  CG1   . ILE A 279 ? 1.81720 0.80970 1.47760 0.17650  0.06290  -0.05260 279 ILE A CG1   
2184 C  CG2   . ILE A 279 ? 2.04730 0.91570 1.65310 0.19780  0.10400  -0.10210 279 ILE A CG2   
2185 C  CD1   . ILE A 279 ? 1.72780 0.81500 1.42890 0.17650  0.08000  -0.06400 279 ILE A CD1   
2186 N  N     . ARG A 280 ? 2.39070 1.19120 1.84100 0.07960  0.11660  -0.13680 280 ARG A N     
2187 C  CA    . ARG A 280 ? 2.46870 1.17240 1.84650 0.05150  0.12060  -0.15330 280 ARG A CA    
2188 C  C     . ARG A 280 ? 2.54660 1.15230 1.91360 0.08190  0.11410  -0.14650 280 ARG A C     
2189 O  O     . ARG A 280 ? 2.55740 1.16330 1.97020 0.13360  0.12040  -0.14640 280 ARG A O     
2190 C  CB    . ARG A 280 ? 2.50250 1.19340 1.85030 0.04590  0.14920  -0.19080 280 ARG A CB    
2191 C  CG    . ARG A 280 ? 2.45200 1.21050 1.78250 0.00220  0.15210  -0.19960 280 ARG A CG    
2192 C  CD    . ARG A 280 ? 2.49560 1.23170 1.78950 -0.00130 0.17950  -0.23650 280 ARG A CD    
2193 N  NE    . ARG A 280 ? 2.48230 1.30240 1.77890 -0.02720 0.18330  -0.24140 280 ARG A NE    
2194 C  CZ    . ARG A 280 ? 2.44360 1.27800 1.70300 -0.07740 0.17050  -0.24080 280 ARG A CZ    
2195 N  NH1   . ARG A 280 ? 2.51320 1.28760 1.73080 -0.10980 0.15510  -0.23660 280 ARG A NH1   
2196 N  NH2   . ARG A 280 ? 2.36110 1.27320 1.62730 -0.09560 0.17250  -0.24320 280 ARG A NH2   
2197 N  N     . LYS A 281 ? 2.52110 1.04320 1.82980 0.05060  0.10110  -0.13990 281 LYS A N     
2198 C  CA    . LYS A 281 ? 2.60350 1.05680 1.91340 0.07710  0.09170  -0.12970 281 LYS A CA    
2199 C  C     . LYS A 281 ? 2.62240 1.02030 1.90410 0.08010  0.11170  -0.16110 281 LYS A C     
2200 O  O     . LYS A 281 ? 2.71530 1.05830 1.95130 0.04940  0.10620  -0.16310 281 LYS A O     
2201 C  CB    . LYS A 281 ? 2.60900 1.03810 1.89310 0.04450  0.06450  -0.09930 281 LYS A CB    
2202 C  CG    . LYS A 281 ? 2.45800 0.94210 1.77320 0.04770  0.04560  -0.06930 281 LYS A CG    
2203 C  CD    . LYS A 281 ? 2.46720 0.93220 1.76240 0.02260  0.01960  -0.03710 281 LYS A CD    
2204 C  CE    . LYS A 281 ? 2.44010 0.97010 1.75480 0.01040  0.00420  -0.01320 281 LYS A CE    
2205 N  NZ    . LYS A 281 ? 2.49690 1.01330 1.78770 -0.01810 -0.01800 0.01640  281 LYS A NZ    
2206 N  N     . LEU A 282 ? 2.58880 1.00450 1.89780 0.11590  0.13640  -0.18620 282 LEU A N     
2207 C  CA    . LEU A 282 ? 2.63040 1.00020 1.91760 0.12420  0.15860  -0.21880 282 LEU A CA    
2208 C  C     . LEU A 282 ? 2.69430 1.00490 2.00540 0.16690  0.15360  -0.21320 282 LEU A C     
2209 O  O     . LEU A 282 ? 2.61460 0.93200 1.96960 0.19850  0.13550  -0.18570 282 LEU A O     
2210 C  CB    . LEU A 282 ? 2.50120 0.91780 1.80140 0.13860  0.18960  -0.25000 282 LEU A CB    
2211 C  CG    . LEU A 282 ? 2.47930 0.94410 1.74480 0.08810  0.19140  -0.25580 282 LEU A CG    
2212 C  CD1   . LEU A 282 ? 2.26240 0.77900 1.53750 0.09880  0.22120  -0.28350 282 LEU A CD1   
2213 C  CD2   . LEU A 282 ? 2.44850 0.86940 1.64690 0.03180  0.18180  -0.26200 282 LEU A CD2   
2214 N  N     . SER A 283 ? 2.77780 1.02980 2.05790 0.16590  0.16860  -0.23960 283 SER A N     
2215 C  CA    . SER A 283 ? 2.84160 1.03100 2.14140 0.20590  0.16740  -0.24040 283 SER A CA    
2216 C  C     . SER A 283 ? 2.80200 1.03580 2.18260 0.26950  0.17340  -0.23680 283 SER A C     
2217 O  O     . SER A 283 ? 2.75770 0.96710 2.17740 0.30550  0.15700  -0.21670 283 SER A O     
2218 C  CB    . SER A 283 ? 2.82660 0.95570 2.08250 0.19650  0.18850  -0.27640 283 SER A CB    
2219 O  OG    . SER A 283 ? 2.81090 0.98210 2.06830 0.20170  0.21800  -0.30920 283 SER A OG    
2220 N  N     . ASP A 284 ? 2.77590 1.07830 2.18490 0.28400  0.19660  -0.25560 284 ASP A N     
2221 C  CA    . ASP A 284 ? 2.71000 1.06820 2.20250 0.34100  0.19960  -0.24750 284 ASP A CA    
2222 C  C     . ASP A 284 ? 2.59070 1.02260 2.11610 0.33880  0.18390  -0.21870 284 ASP A C     
2223 O  O     . ASP A 284 ? 2.52080 1.00600 2.03420 0.31580  0.19750  -0.22760 284 ASP A O     
2224 C  CB    . ASP A 284 ? 2.68080 1.07470 2.19340 0.36400  0.23770  -0.28550 284 ASP A CB    
2225 C  CG    . ASP A 284 ? 2.67050 1.10940 2.27270 0.42760  0.24560  -0.28570 284 ASP A CG    
2226 O  OD1   . ASP A 284 ? 2.72330 1.11560 2.35280 0.46110  0.23600  -0.28240 284 ASP A OD1   
2227 O  OD2   . ASP A 284 ? 2.65290 1.17540 2.30030 0.44390  0.26240  -0.29030 284 ASP A OD2   
2228 N  N     . PRO A 285 ? 2.56120 0.99420 2.12210 0.35790  0.15360  -0.18300 285 PRO A N     
2229 C  CA    . PRO A 285 ? 2.39070 0.89190 1.98190 0.35630  0.13610  -0.15450 285 PRO A CA    
2230 C  C     . PRO A 285 ? 2.35660 0.94370 2.01510 0.39340  0.15780  -0.16580 285 PRO A C     
2231 O  O     . PRO A 285 ? 2.32580 0.92920 2.04520 0.44220  0.16800  -0.17490 285 PRO A O     
2232 C  CB    . PRO A 285 ? 2.34430 0.82290 1.96420 0.37790  0.10040  -0.11740 285 PRO A CB    
2233 C  CG    . PRO A 285 ? 2.44860 0.86910 2.08520 0.41170  0.10670  -0.13070 285 PRO A CG    
2234 C  CD    . PRO A 285 ? 2.55770 0.92870 2.13230 0.38230  0.13340  -0.16690 285 PRO A CD    
2235 N  N     . PRO A 286 ? 2.33340 0.98030 1.98640 0.37100  0.16660  -0.16640 286 PRO A N     
2236 C  CA    . PRO A 286 ? 2.21860 0.97560 1.94960 0.39800  0.18270  -0.17110 286 PRO A CA    
2237 C  C     . PRO A 286 ? 2.12030 0.92090 1.93210 0.44290  0.15920  -0.14200 286 PRO A C     
2238 O  O     . PRO A 286 ? 2.09910 0.88450 1.90540 0.43430  0.12300  -0.10950 286 PRO A O     
2239 C  CB    . PRO A 286 ? 2.14930 0.98680 1.86630 0.34710  0.17960  -0.16580 286 PRO A CB    
2240 C  CG    . PRO A 286 ? 2.19570 0.96070 1.82230 0.29740  0.17890  -0.17660 286 PRO A CG    
2241 C  CD    . PRO A 286 ? 2.31310 0.97100 1.90660 0.30700  0.15930  -0.16420 286 PRO A CD    
2242 N  N     . LYS A 287 ? 2.02880 0.88470 1.91530 0.48970  0.17910  -0.15340 287 LYS A N     
2243 C  CA    . LYS A 287 ? 1.98300 0.88270 1.94800 0.53060  0.15260  -0.12450 287 LYS A CA    
2244 C  C     . LYS A 287 ? 1.97410 0.98220 1.97350 0.50320  0.13380  -0.10120 287 LYS A C     
2245 O  O     . LYS A 287 ? 1.96450 1.02680 1.94840 0.46770  0.15080  -0.11310 287 LYS A O     
2246 C  CB    . LYS A 287 ? 1.92280 0.86350 1.97110 0.58650  0.17360  -0.14170 287 LYS A CB    
2247 C  CG    . LYS A 287 ? 2.00600 0.87670 2.04180 0.60490  0.18570  -0.16760 287 LYS A CG    
2248 C  CD    . LYS A 287 ? 2.01530 0.94940 2.14150 0.65550  0.20380  -0.18570 287 LYS A CD    
2249 C  CE    . LYS A 287 ? 2.12570 0.99030 2.24050 0.67670  0.21770  -0.21430 287 LYS A CE    
2250 N  NZ    . LYS A 287 ? 2.19640 0.98800 2.31320 0.69170  0.18060  -0.19120 287 LYS A NZ    
2251 N  N     . ALA A 288 ? 1.94020 0.97590 1.98350 0.51970  0.09700  -0.06730 288 ALA A N     
2252 C  CA    . ALA A 288 ? 1.90640 1.03700 1.97910 0.49380  0.07640  -0.04460 288 ALA A CA    
2253 C  C     . ALA A 288 ? 1.88220 1.11900 2.01260 0.49590  0.10390  -0.06080 288 ALA A C     
2254 O  O     . ALA A 288 ? 1.90010 1.19410 2.01780 0.45600  0.10450  -0.05790 288 ALA A O     
2255 C  CB    . ALA A 288 ? 1.88050 1.02620 1.99970 0.51970  0.03490  -0.00920 288 ALA A CB    
2256 N  N     . GLU A 289 ? 1.95310 1.21800 2.14860 0.54240  0.12720  -0.07710 289 GLU A N     
2257 C  CA    . GLU A 289 ? 1.95670 1.31770 2.20260 0.54250  0.15830  -0.09440 289 GLU A CA    
2258 C  C     . GLU A 289 ? 1.95120 1.30030 2.13060 0.50180  0.19050  -0.12070 289 GLU A C     
2259 O  O     . GLU A 289 ? 1.93900 1.36490 2.13180 0.47700  0.20250  -0.12320 289 GLU A O     
2260 C  CB    . GLU A 289 ? 1.90040 1.29550 2.23020 0.59940  0.18020  -0.10840 289 GLU A CB    
2261 C  CG    . GLU A 289 ? 1.84330 1.32450 2.26440 0.62210  0.14950  -0.07950 289 GLU A CG    
2262 C  CD    . GLU A 289 ? 1.79050 1.36910 2.23050 0.58280  0.14120  -0.06600 289 GLU A CD    
2263 O  OE1   . GLU A 289 ? 1.74880 1.33520 2.13650 0.53950  0.15860  -0.07710 289 GLU A OE1   
2264 O  OE2   . GLU A 289 ? 1.80320 1.44760 2.30880 0.59460  0.11320  -0.04230 289 GLU A OE2   
2265 N  N     . ALA A 290 ? 1.93330 1.18720 2.04320 0.49660  0.20610  -0.14180 290 ALA A N     
2266 C  CA    . ALA A 290 ? 1.86750 1.10940 1.91150 0.45690  0.23400  -0.16690 290 ALA A CA    
2267 C  C     . ALA A 290 ? 1.88400 1.14820 1.88480 0.40270  0.21000  -0.14770 290 ALA A C     
2268 O  O     . ALA A 290 ? 1.74810 1.05920 1.73090 0.37120  0.22580  -0.15720 290 ALA A O     
2269 C  CB    . ALA A 290 ? 1.81370 0.94330 1.78830 0.45940  0.25090  -0.19240 290 ALA A CB    
2270 N  N     . ILE A 291 ? 1.92960 1.16450 1.91690 0.39300  0.17170  -0.11950 291 ILE A N     
2271 C  CA    . ILE A 291 ? 1.84000 1.09890 1.79270 0.34460  0.14900  -0.10080 291 ILE A CA    
2272 C  C     . ILE A 291 ? 1.76740 1.13550 1.77850 0.33970  0.14670  -0.08910 291 ILE A C     
2273 O  O     . ILE A 291 ? 1.75150 1.16020 1.74090 0.30340  0.15240  -0.09150 291 ILE A O     
2274 C  CB    . ILE A 291 ? 1.82030 1.02840 1.75110 0.33840  0.11040  -0.07240 291 ILE A CB    
2275 C  CG1   . ILE A 291 ? 1.91930 1.01230 1.79200 0.34320  0.11120  -0.08150 291 ILE A CG1   
2276 C  CG2   . ILE A 291 ? 1.70040 0.93480 1.59560 0.28830  0.09130  -0.05610 291 ILE A CG2   
2277 C  CD1   . ILE A 291 ? 1.96250 1.01310 1.76310 0.30520  0.13160  -0.10590 291 ILE A CD1   
2278 N  N     . ARG A 292 ? 1.81130 1.22720 1.89790 0.37570  0.13620  -0.07510 292 ARG A N     
2279 C  CA    . ARG A 292 ? 1.76500 1.28270 1.90930 0.37020  0.13280  -0.06380 292 ARG A CA    
2280 C  C     . ARG A 292 ? 1.75520 1.32450 1.91290 0.36560  0.17180  -0.08790 292 ARG A C     
2281 O  O     . ARG A 292 ? 1.72890 1.36230 1.89460 0.33890  0.17300  -0.08240 292 ARG A O     
2282 C  CB    . ARG A 292 ? 1.76580 1.32200 1.99000 0.41090  0.11340  -0.04590 292 ARG A CB    
2283 C  CG    . ARG A 292 ? 1.77020 1.43270 2.06900 0.41590  0.12000  -0.04220 292 ARG A CG    
2284 C  CD    . ARG A 292 ? 1.87890 1.58660 2.18170 0.38650  0.08750  -0.01590 292 ARG A CD    
2285 N  NE    . ARG A 292 ? 1.87840 1.67570 2.22280 0.37230  0.10110  -0.01810 292 ARG A NE    
2286 C  CZ    . ARG A 292 ? 1.83570 1.65090 2.14170 0.33340  0.11210  -0.02300 292 ARG A CZ    
2287 N  NH1   . ARG A 292 ? 1.79270 1.55040 2.02200 0.30410  0.11090  -0.02690 292 ARG A NH1   
2288 N  NH2   . ARG A 292 ? 1.78030 1.67330 2.12720 0.32340  0.12390  -0.02320 292 ARG A NH2   
2289 N  N     . ASP A 293 ? 1.76620 1.30120 1.91750 0.38830  0.20460  -0.11520 293 ASP A N     
2290 C  CA    . ASP A 293 ? 1.74540 1.32040 1.89690 0.38110  0.24430  -0.13960 293 ASP A CA    
2291 C  C     . ASP A 293 ? 1.63360 1.19630 1.71020 0.33080  0.24730  -0.14480 293 ASP A C     
2292 O  O     . ASP A 293 ? 1.57580 1.20140 1.65950 0.30880  0.25780  -0.14420 293 ASP A O     
2293 C  CB    . ASP A 293 ? 1.74790 1.27520 1.89660 0.41480  0.27890  -0.17000 293 ASP A CB    
2294 C  CG    . ASP A 293 ? 1.65600 1.23430 1.89830 0.46490  0.29140  -0.17190 293 ASP A CG    
2295 O  OD1   . ASP A 293 ? 1.70230 1.36300 2.01170 0.46880  0.27700  -0.15200 293 ASP A OD1   
2296 O  OD2   . ASP A 293 ? 1.70470 1.23930 1.95500 0.50100  0.31440  -0.19350 293 ASP A OD2   
2297 N  N     . MET A 294 ? 1.63720 1.11960 1.64300 0.31120  0.23560  -0.14760 294 MET A N     
2298 C  CA    . MET A 294 ? 1.58990 1.06210 1.52760 0.26400  0.23650  -0.15270 294 MET A CA    
2299 C  C     . MET A 294 ? 1.51710 1.04390 1.46480 0.23470  0.20860  -0.12610 294 MET A C     
2300 O  O     . MET A 294 ? 1.46580 1.02460 1.38830 0.20310  0.21400  -0.12810 294 MET A O     
2301 C  CB    . MET A 294 ? 1.60360 0.97850 1.46680 0.24870  0.23110  -0.16330 294 MET A CB    
2302 C  CG    . MET A 294 ? 1.60530 0.96760 1.39830 0.20370  0.23850  -0.17630 294 MET A CG    
2303 S  SD    . MET A 294 ? 1.64930 1.02980 1.42380 0.20410  0.28310  -0.20940 294 MET A SD    
2304 C  CE    . MET A 294 ? 1.71560 0.99860 1.46040 0.23410  0.30620  -0.23960 294 MET A CE    
2305 N  N     . VAL A 295 ? 1.55800 1.09330 1.53970 0.24490  0.17850  -0.10120 295 VAL A N     
2306 C  CA    . VAL A 295 ? 1.51200 1.10050 1.50790 0.22070  0.15370  -0.07730 295 VAL A CA    
2307 C  C     . VAL A 295 ? 1.53160 1.20740 1.57840 0.22170  0.16670  -0.07590 295 VAL A C     
2308 O  O     . VAL A 295 ? 1.45480 1.16840 1.48890 0.19150  0.16310  -0.06950 295 VAL A O     
2309 C  CB    . VAL A 295 ? 1.41410 0.99070 1.43440 0.23430  0.12040  -0.05270 295 VAL A CB    
2310 C  CG1   . VAL A 295 ? 1.30830 0.94720 1.35210 0.21430  0.09860  -0.03080 295 VAL A CG1   
2311 C  CG2   . VAL A 295 ? 1.30650 0.79670 1.26520 0.22160  0.10600  -0.05060 295 VAL A CG2   
2312 N  N     . ARG A 296 ? 1.56630 1.27490 1.67310 0.25660  0.18240  -0.08150 296 ARG A N     
2313 C  CA    . ARG A 296 ? 1.51070 1.30050 1.66660 0.25680  0.19900  -0.08190 296 ARG A CA    
2314 C  C     . ARG A 296 ? 1.48540 1.28070 1.59670 0.23110  0.22670  -0.09930 296 ARG A C     
2315 O  O     . ARG A 296 ? 1.43910 1.28370 1.55280 0.20680  0.22640  -0.09110 296 ARG A O     
2316 C  CB    . ARG A 296 ? 1.54530 1.36320 1.76770 0.29850  0.21900  -0.09140 296 ARG A CB    
2317 C  CG    . ARG A 296 ? 1.52030 1.42340 1.79350 0.29470  0.23690  -0.09100 296 ARG A CG    
2318 C  CD    . ARG A 296 ? 1.55000 1.49210 1.89830 0.33460  0.25620  -0.09930 296 ARG A CD    
2319 N  NE    . ARG A 296 ? 1.61730 1.50730 1.92940 0.34870  0.28980  -0.12770 296 ARG A NE    
2320 C  CZ    . ARG A 296 ? 1.59310 1.49380 1.87770 0.33510  0.32670  -0.14820 296 ARG A CZ    
2321 N  NH1   . ARG A 296 ? 1.52860 1.48840 1.81840 0.30770  0.33470  -0.14190 296 ARG A NH1   
2322 N  NH2   . ARG A 296 ? 1.57240 1.41590 1.81430 0.34590  0.35480  -0.17520 296 ARG A NH2   
2323 N  N     . TYR A 297 ? 1.52280 1.26200 1.58820 0.23540  0.24920  -0.12290 297 TYR A N     
2324 C  CA    . TYR A 297 ? 1.47390 1.20700 1.48460 0.20960  0.27360  -0.14070 297 TYR A CA    
2325 C  C     . TYR A 297 ? 1.40020 1.13290 1.36350 0.16810  0.25160  -0.12780 297 TYR A C     
2326 O  O     . TYR A 297 ? 1.34850 1.11710 1.29650 0.14510  0.26080  -0.12780 297 TYR A O     
2327 C  CB    . TYR A 297 ? 1.51330 1.17250 1.47570 0.22020  0.29500  -0.16810 297 TYR A CB    
2328 C  CG    . TYR A 297 ? 1.52330 1.15790 1.41180 0.18920  0.31330  -0.18700 297 TYR A CG    
2329 C  CD1   . TYR A 297 ? 1.57450 1.23990 1.45960 0.18870  0.34840  -0.20410 297 TYR A CD1   
2330 C  CD2   . TYR A 297 ? 1.54660 1.12680 1.36730 0.15940  0.29550  -0.18800 297 TYR A CD2   
2331 C  CE1   . TYR A 297 ? 1.55970 1.20050 1.37160 0.15920  0.36270  -0.22050 297 TYR A CE1   
2332 C  CE2   . TYR A 297 ? 1.57080 1.13040 1.32420 0.13010  0.30870  -0.20470 297 TYR A CE2   
2333 C  CZ    . TYR A 297 ? 1.54460 1.13310 1.29160 0.13040  0.34120  -0.22060 297 TYR A CZ    
2334 O  OH    . TYR A 297 ? 1.63850 1.20480 1.31300 0.09980  0.35170  -0.23620 297 TYR A OH    
2335 N  N     . ALA A 298 ? 1.45060 1.14010 1.38790 0.15800  0.22360  -0.11740 298 ALA A N     
2336 C  CA    . ALA A 298 ? 1.33130 1.02200 1.22880 0.12040  0.20300  -0.10600 298 ALA A CA    
2337 C  C     . ALA A 298 ? 1.28050 1.04280 1.21750 0.11010  0.19180  -0.08620 298 ALA A C     
2338 O  O     . ALA A 298 ? 1.24920 1.03680 1.16370 0.08450  0.19380  -0.08450 298 ALA A O     
2339 C  CB    . ALA A 298 ? 1.36250 1.00340 1.23970 0.11500  0.17570  -0.09540 298 ALA A CB    
2340 N  N     . ARG A 299 ? 1.26050 1.05420 1.25630 0.13030  0.17910  -0.07090 299 ARG A N     
2341 C  CA    . ARG A 299 ? 1.16900 1.02610 1.20280 0.12050  0.16740  -0.05280 299 ARG A CA    
2342 C  C     . ARG A 299 ? 1.19450 1.10030 1.24450 0.11710  0.19280  -0.05930 299 ARG A C     
2343 O  O     . ARG A 299 ? 1.13070 1.07480 1.18420 0.09680  0.18690  -0.04800 299 ARG A O     
2344 C  CB    . ARG A 299 ? 1.19460 1.07330 1.28670 0.14340  0.14930  -0.03760 299 ARG A CB    
2345 C  CG    . ARG A 299 ? 1.19770 1.03580 1.26880 0.13820  0.11940  -0.02470 299 ARG A CG    
2346 C  CD    . ARG A 299 ? 1.18740 1.05290 1.31110 0.15550  0.09730  -0.00670 299 ARG A CD    
2347 N  NE    . ARG A 299 ? 1.23910 1.16470 1.39090 0.13980  0.08920  0.00540  299 ARG A NE    
2348 C  CZ    . ARG A 299 ? 1.19920 1.16050 1.39660 0.14760  0.06980  0.02080  299 ARG A CZ    
2349 N  NH1   . ARG A 299 ? 1.25760 1.20520 1.48080 0.17220  0.05420  0.02810  299 ARG A NH1   
2350 N  NH2   . ARG A 299 ? 1.16710 1.17680 1.38320 0.13010  0.06460  0.02930  299 ARG A NH2   
2351 N  N     . ASN A 300 ? 1.37090 1.27330 1.42910 0.13630  0.22220  -0.07740 300 ASN A N     
2352 C  CA    . ASN A 300 ? 1.35750 1.30360 1.42650 0.13170  0.25030  -0.08440 300 ASN A CA    
2353 C  C     . ASN A 300 ? 1.37360 1.30260 1.37500 0.10080  0.25820  -0.09120 300 ASN A C     
2354 O  O     . ASN A 300 ? 1.34650 1.31380 1.34710 0.08180  0.26110  -0.08230 300 ASN A O     
2355 C  CB    . ASN A 300 ? 1.38670 1.33490 1.48460 0.16200  0.28190  -0.10350 300 ASN A CB    
2356 C  CG    . ASN A 300 ? 1.45500 1.43300 1.62990 0.19370  0.27240  -0.09450 300 ASN A CG    
2357 O  OD1   . ASN A 300 ? 1.58010 1.53840 1.77720 0.22490  0.28460  -0.10720 300 ASN A OD1   
2358 N  ND2   . ASN A 300 ? 1.38980 1.41380 1.60530 0.18610  0.24890  -0.07260 300 ASN A ND2   
2359 N  N     . VAL A 301 ? 1.26300 1.13300 1.20650 0.09500  0.26080  -0.10650 301 VAL A N     
2360 C  CA    . VAL A 301 ? 1.22070 1.07230 1.09720 0.06540  0.26560  -0.11400 301 VAL A CA    
2361 C  C     . VAL A 301 ? 1.22030 1.08920 1.08450 0.03820  0.23670  -0.09380 301 VAL A C     
2362 O  O     . VAL A 301 ? 1.31780 1.20110 1.15020 0.01570  0.23910  -0.09140 301 VAL A O     
2363 C  CB    . VAL A 301 ? 1.25270 1.03430 1.07220 0.06400  0.27060  -0.13500 301 VAL A CB    
2364 C  CG1   . VAL A 301 ? 1.27800 1.04050 1.02690 0.03000  0.26780  -0.14090 301 VAL A CG1   
2365 C  CG2   . VAL A 301 ? 1.42300 1.18540 1.25000 0.09140  0.30410  -0.15850 301 VAL A CG2   
2366 N  N     . ILE A 302 ? 1.16750 1.03570 1.05620 0.04050  0.20950  -0.07870 302 ILE A N     
2367 C  CA    . ILE A 302 ? 1.17080 1.06070 1.05620 0.01790  0.18450  -0.06020 302 ILE A CA    
2368 C  C     . ILE A 302 ? 1.20680 1.15250 1.12250 0.01280  0.18880  -0.04750 302 ILE A C     
2369 O  O     . ILE A 302 ? 1.22730 1.18560 1.11710 -0.00870 0.18420  -0.04120 302 ILE A O     
2370 C  CB    . ILE A 302 ? 1.15350 1.03540 1.06400 0.02390  0.15890  -0.04740 302 ILE A CB    
2371 C  CG1   . ILE A 302 ? 1.12960 0.95280 0.99830 0.01840  0.15010  -0.05590 302 ILE A CG1   
2372 C  CG2   . ILE A 302 ? 1.21650 1.13360 1.14120 0.00730  0.13830  -0.02850 302 ILE A CG2   
2373 C  CD1   . ILE A 302 ? 1.14440 0.95340 1.03360 0.02600  0.12810  -0.04340 302 ILE A CD1   
2374 N  N     . GLU A 303 ? 1.25250 1.23100 1.22240 0.03250  0.19930  -0.04430 303 GLU A N     
2375 C  CA    . GLU A 303 ? 1.31060 1.34010 1.31130 0.02620  0.20480  -0.03240 303 GLU A CA    
2376 C  C     . GLU A 303 ? 1.31240 1.34720 1.27980 0.01490  0.23060  -0.04110 303 GLU A C     
2377 O  O     . GLU A 303 ? 1.31580 1.37150 1.27130 -0.00400 0.22810  -0.02970 303 GLU A O     
2378 C  CB    . GLU A 303 ? 1.29500 1.36020 1.36340 0.04880  0.21140  -0.02920 303 GLU A CB    
2379 C  CG    . GLU A 303 ? 1.35650 1.47490 1.46320 0.03920  0.21180  -0.01430 303 GLU A CG    
2380 C  CD    . GLU A 303 ? 1.34580 1.46540 1.44700 0.02240  0.18140  0.00280  303 GLU A CD    
2381 O  OE1   . GLU A 303 ? 1.33090 1.43180 1.43480 0.02720  0.15930  0.00650  303 GLU A OE1   
2382 O  OE2   . GLU A 303 ? 1.35760 1.49120 1.44410 0.00340  0.18110  0.01150  303 GLU A OE2   
2383 N  N     . GLU A 304 ? 1.37750 1.38920 1.32550 0.02610  0.25550  -0.06130 304 GLU A N     
2384 C  CA    . GLU A 304 ? 1.40760 1.41730 1.31330 0.01430  0.28240  -0.07260 304 GLU A CA    
2385 C  C     . GLU A 304 ? 1.41780 1.40680 1.26000 -0.01400 0.26760  -0.06810 304 GLU A C     
2386 O  O     . GLU A 304 ? 1.44740 1.45200 1.26410 -0.03090 0.27650  -0.06280 304 GLU A O     
2387 C  CB    . GLU A 304 ? 1.46280 1.44150 1.35220 0.03180  0.31040  -0.09860 304 GLU A CB    
2388 C  CG    . GLU A 304 ? 1.49390 1.48080 1.35310 0.02490  0.34670  -0.11220 304 GLU A CG    
2389 C  CD    . GLU A 304 ? 1.61700 1.56270 1.39090 0.00060  0.34750  -0.12260 304 GLU A CD    
2390 O  OE1   . GLU A 304 ? 1.65260 1.56210 1.39530 -0.00820 0.32210  -0.12250 304 GLU A OE1   
2391 O  OE2   . GLU A 304 ? 1.56790 1.51810 1.30470 -0.01120 0.37320  -0.13070 304 GLU A OE2   
2392 N  N     . PHE A 305 ? 1.27900 1.23360 1.09520 -0.02010 0.24440  -0.06940 305 PHE A N     
2393 C  CA    . PHE A 305 ? 1.24310 1.18330 1.00540 -0.04640 0.22790  -0.06540 305 PHE A CA    
2394 C  C     . PHE A 305 ? 1.27940 1.25630 1.06210 -0.05840 0.20840  -0.04140 305 PHE A C     
2395 O  O     . PHE A 305 ? 1.34890 1.33210 1.09680 -0.07710 0.20520  -0.03450 305 PHE A O     
2396 C  CB    . PHE A 305 ? 1.18320 1.08310 0.92190 -0.05080 0.20830  -0.07210 305 PHE A CB    
2397 C  CG    . PHE A 305 ? 1.13140 1.01560 0.81410 -0.07790 0.19290  -0.07240 305 PHE A CG    
2398 C  CD1   . PHE A 305 ? 1.07950 0.98700 0.77030 -0.09220 0.16640  -0.05370 305 PHE A CD1   
2399 C  CD2   . PHE A 305 ? 1.23580 1.08250 0.85910 -0.08880 0.20410  -0.09230 305 PHE A CD2   
2400 C  CE1   . PHE A 305 ? 1.07750 0.97680 0.72390 -0.11560 0.15030  -0.05330 305 PHE A CE1   
2401 C  CE2   . PHE A 305 ? 1.25720 1.09340 0.83100 -0.11520 0.18690  -0.09210 305 PHE A CE2   
2402 C  CZ    . PHE A 305 ? 1.26490 1.13000 0.85300 -0.12800 0.15920  -0.07190 305 PHE A CZ    
2403 N  N     . ARG A 306 ? 1.20040 1.19920 1.03720 -0.04780 0.19430  -0.02850 306 ARG A N     
2404 C  CA    . ARG A 306 ? 1.08950 1.11900 0.94630 -0.05790 0.17740  -0.00770 306 ARG A CA    
2405 C  C     . ARG A 306 ? 1.18660 1.24120 1.04210 -0.06450 0.19490  -0.00080 306 ARG A C     
2406 O  O     . ARG A 306 ? 1.20540 1.27010 1.04610 -0.07950 0.18370  0.01360  306 ARG A O     
2407 C  CB    . ARG A 306 ? 1.14840 1.19720 1.06200 -0.04550 0.16390  0.00250  306 ARG A CB    
2408 C  CG    . ARG A 306 ? 1.35680 1.38380 1.26990 -0.04400 0.14230  0.00190  306 ARG A CG    
2409 C  CD    . ARG A 306 ? 1.34780 1.39430 1.31220 -0.03300 0.12990  0.01240  306 ARG A CD    
2410 N  NE    . ARG A 306 ? 1.52800 1.56100 1.51430 -0.01350 0.13320  0.00490  306 ARG A NE    
2411 C  CZ    . ARG A 306 ? 1.48420 1.52290 1.50390 -0.00460 0.11760  0.01270  306 ARG A CZ    
2412 N  NH1   . ARG A 306 ? 1.42060 1.47720 1.45440 -0.01410 0.09980  0.02570  306 ARG A NH1   
2413 N  NH2   . ARG A 306 ? 1.50950 1.53300 1.54650 0.01470  0.11930  0.00710  306 ARG A NH2   
2414 N  N     . ARG A 307 ? 1.31250 1.37650 1.18300 -0.05340 0.22300  -0.01070 307 ARG A N     
2415 C  CA    . ARG A 307 ? 1.31630 1.40250 1.18030 -0.06250 0.24440  -0.00550 307 ARG A CA    
2416 C  C     . ARG A 307 ? 1.31060 1.37340 1.10340 -0.07960 0.25460  -0.01230 307 ARG A C     
2417 O  O     . ARG A 307 ? 1.33290 1.40410 1.10070 -0.09670 0.25290  0.00160  307 ARG A O     
2418 C  CB    . ARG A 307 ? 1.36560 1.47530 1.27450 -0.04510 0.27300  -0.01520 307 ARG A CB    
2419 C  CG    . ARG A 307 ? 1.29580 1.44710 1.26990 -0.04060 0.26870  -0.00010 307 ARG A CG    
2420 C  CD    . ARG A 307 ? 1.21870 1.40210 1.23630 -0.02760 0.30030  -0.00900 307 ARG A CD    
2421 N  NE    . ARG A 307 ? 1.24000 1.41140 1.27750 -0.00230 0.30830  -0.02750 307 ARG A NE    
2422 C  CZ    . ARG A 307 ? 1.32700 1.47480 1.33370 0.00630  0.33290  -0.04860 307 ARG A CZ    
2423 N  NH1   . ARG A 307 ? 1.32610 1.46020 1.27520 -0.01020 0.35350  -0.05560 307 ARG A NH1   
2424 N  NH2   . ARG A 307 ? 1.30300 1.43740 1.33480 0.03200  0.33640  -0.06310 307 ARG A NH2   
2425 N  N     . ALA A 308 ? 1.34290 1.37310 1.09930 -0.07600 0.26400  -0.03330 308 ALA A N     
2426 C  CA    . ALA A 308 ? 1.33170 1.33800 1.01620 -0.09300 0.27600  -0.04320 308 ALA A CA    
2427 C  C     . ALA A 308 ? 1.27650 1.27510 0.91890 -0.11510 0.24670  -0.02830 308 ALA A C     
2428 O  O     . ALA A 308 ? 1.32150 1.31610 0.91330 -0.13270 0.25210  -0.02420 308 ALA A O     
2429 C  CB    . ALA A 308 ? 1.35290 1.32000 1.00740 -0.08510 0.28830  -0.07020 308 ALA A CB    
2430 N  N     . LYS A 309 ? 1.23350 1.23220 0.89720 -0.11440 0.21570  -0.01910 309 LYS A N     
2431 C  CA    . LYS A 309 ? 1.30850 1.30280 0.93710 -0.13320 0.18760  -0.00700 309 LYS A CA    
2432 C  C     . LYS A 309 ? 1.38270 1.40070 1.01370 -0.14250 0.17970  0.01710  309 LYS A C     
2433 O  O     . LYS A 309 ? 1.40610 1.42230 1.00850 -0.15630 0.15630  0.02880  309 LYS A O     
2434 C  CB    . LYS A 309 ? 1.22650 1.21960 0.88250 -0.12990 0.15940  -0.00370 309 LYS A CB    
2435 C  CG    . LYS A 309 ? 1.19220 1.21260 0.91190 -0.11740 0.15110  0.01150  309 LYS A CG    
2436 C  CD    . LYS A 309 ? 1.28220 1.30100 1.02540 -0.11520 0.12640  0.01380  309 LYS A CD    
2437 C  CE    . LYS A 309 ? 1.18580 1.19590 0.89180 -0.13250 0.10470  0.01470  309 LYS A CE    
2438 N  NZ    . LYS A 309 ? 1.09870 1.10830 0.82890 -0.13150 0.08560  0.01470  309 LYS A NZ    
2439 N  N     . HIS A 310 ? 1.41150 1.45070 1.07450 -0.13620 0.19830  0.02500  310 HIS A N     
2440 C  CA    . HIS A 310 ? 1.39750 1.45170 1.05700 -0.14700 0.19220  0.04830  310 HIS A CA    
2441 C  C     . HIS A 310 ? 1.43680 1.47970 1.03280 -0.16410 0.20840  0.04970  310 HIS A C     
2442 O  O     . HIS A 310 ? 1.50430 1.54760 1.07540 -0.17710 0.19450  0.07020  310 HIS A O     
2443 C  CB    . HIS A 310 ? 1.39870 1.47970 1.11890 -0.13720 0.20370  0.05720  310 HIS A CB    
2444 C  CG    . HIS A 310 ? 1.37940 1.47150 1.15450 -0.12510 0.18190  0.06230  310 HIS A CG    
2445 N  ND1   . HIS A 310 ? 1.38850 1.49070 1.21200 -0.10860 0.18950  0.05150  310 HIS A ND1   
2446 C  CD2   . HIS A 310 ? 1.39670 1.48960 1.18250 -0.12680 0.15260  0.07530  310 HIS A CD2   
2447 C  CE1   . HIS A 310 ? 1.41850 1.52630 1.27610 -0.10300 0.16610  0.05870  310 HIS A CE1   
2448 N  NE2   . HIS A 310 ? 1.44290 1.54560 1.27940 -0.11350 0.14520  0.07200  310 HIS A NE2   
2449 N  N     . TYR A 311 ? 1.34870 1.37940 0.91590 -0.16390 0.23780  0.02840  311 TYR A N     
2450 C  CA    . TYR A 311 ? 1.38170 1.40220 0.88660 -0.18100 0.25910  0.02790  311 TYR A CA    
2451 C  C     . TYR A 311 ? 1.36020 1.34940 0.80090 -0.18820 0.26860  0.00370  311 TYR A C     
2452 O  O     . TYR A 311 ? 1.41960 1.39760 0.80430 -0.20170 0.29230  -0.00250 311 TYR A O     
2453 C  CB    . TYR A 311 ? 1.35450 1.39660 0.88700 -0.17680 0.29700  0.02610  311 TYR A CB    
2454 C  CG    . TYR A 311 ? 1.33110 1.38080 0.90770 -0.15540 0.32240  0.00140  311 TYR A CG    
2455 C  CD1   . TYR A 311 ? 1.36030 1.39210 0.89920 -0.15380 0.35320  -0.02470 311 TYR A CD1   
2456 C  CD2   . TYR A 311 ? 1.30450 1.37760 0.95920 -0.13610 0.31510  0.00420  311 TYR A CD2   
2457 C  CE1   . TYR A 311 ? 1.34870 1.38570 0.93090 -0.13070 0.37590  -0.04680 311 TYR A CE1   
2458 C  CE2   . TYR A 311 ? 1.34950 1.42960 1.04610 -0.11450 0.33510  -0.01610 311 TYR A CE2   
2459 C  CZ    . TYR A 311 ? 1.40870 1.47070 1.07100 -0.11050 0.36550  -0.04130 311 TYR A CZ    
2460 O  OH    . TYR A 311 ? 1.36850 1.43570 1.07530 -0.08580 0.38510  -0.06110 311 TYR A OH    
2461 N  N     . LYS A 312 ? 1.29870 1.27110 0.74250 -0.18150 0.25250  -0.01100 312 LYS A N     
2462 C  CA    . LYS A 312 ? 1.30370 1.24170 0.68850 -0.18870 0.26280  -0.03690 312 LYS A CA    
2463 C  C     . LYS A 312 ? 1.36710 1.28870 0.70980 -0.20580 0.22570  -0.03250 312 LYS A C     
2464 O  O     . LYS A 312 ? 1.30430 1.24240 0.68020 -0.20490 0.19350  -0.01420 312 LYS A O     
2465 C  CB    . LYS A 312 ? 1.39440 1.32060 0.81600 -0.16690 0.27930  -0.06130 312 LYS A CB    
2466 C  CG    . LYS A 312 ? 1.48750 1.42640 0.93780 -0.15080 0.32130  -0.07330 312 LYS A CG    
2467 C  CD    . LYS A 312 ? 1.45200 1.37310 0.93240 -0.12760 0.33530  -0.09790 312 LYS A CD    
2468 C  CE    . LYS A 312 ? 1.51300 1.45680 1.03860 -0.10730 0.37440  -0.10790 312 LYS A CE    
2469 N  NZ    . LYS A 312 ? 1.55760 1.49140 1.02880 -0.11660 0.41270  -0.12500 312 LYS A NZ    
2470 N  N     . SER A 313 ? 1.43260 1.32290 0.70220 -0.22230 0.23100  -0.05050 313 SER A N     
2471 C  CA    . SER A 313 ? 1.42590 1.30390 0.65200 -0.24220 0.19540  -0.04710 313 SER A CA    
2472 C  C     . SER A 313 ? 1.44720 1.31410 0.70250 -0.23580 0.17810  -0.06000 313 SER A C     
2473 O  O     . SER A 313 ? 1.46860 1.32280 0.75510 -0.21830 0.19800  -0.07770 313 SER A O     
2474 C  CB    . SER A 313 ? 1.50580 1.35230 0.63890 -0.26510 0.20570  -0.06320 313 SER A CB    
2475 O  OG    . SER A 313 ? 1.64000 1.45120 0.75210 -0.26150 0.22760  -0.09680 313 SER A OG    
2476 N  N     . PRO A 314 ? 1.39210 1.26450 0.63910 -0.25020 0.14050  -0.05050 314 PRO A N     
2477 C  CA    . PRO A 314 ? 1.36220 1.22390 0.63310 -0.24870 0.12480  -0.06230 314 PRO A CA    
2478 C  C     . PRO A 314 ? 1.48720 1.30240 0.71690 -0.25260 0.14480  -0.09500 314 PRO A C     
2479 O  O     . PRO A 314 ? 1.54440 1.34420 0.80880 -0.23840 0.15190  -0.10700 314 PRO A O     
2480 C  CB    . PRO A 314 ? 1.38910 1.26830 0.64560 -0.26900 0.08380  -0.04730 314 PRO A CB    
2481 C  CG    . PRO A 314 ? 1.29910 1.20830 0.56170 -0.26790 0.07460  -0.01940 314 PRO A CG    
2482 C  CD    . PRO A 314 ? 1.41210 1.30590 0.63880 -0.26590 0.10970  -0.02540 314 PRO A CD    
2483 N  N     . SER A 315 ? 1.45510 1.24350 0.60750 -0.27210 0.15360  -0.10970 315 SER A N     
2484 C  CA    . SER A 315 ? 1.56580 1.30330 0.67170 -0.27710 0.17360  -0.14330 315 SER A CA    
2485 C  C     . SER A 315 ? 1.64400 1.36650 0.78080 -0.24870 0.21430  -0.15940 315 SER A C     
2486 O  O     . SER A 315 ? 1.73870 1.42370 0.87660 -0.24010 0.22580  -0.18210 315 SER A O     
2487 C  CB    . SER A 315 ? 1.56150 1.27420 0.57400 -0.30430 0.17690  -0.15590 315 SER A CB    
2488 O  OG    . SER A 315 ? 1.72450 1.44930 0.72490 -0.29780 0.20220  -0.14940 315 SER A OG    
2489 N  N     . GLU A 316 ? 1.64910 1.40090 0.81480 -0.23340 0.23540  -0.14710 316 GLU A N     
2490 C  CA    . GLU A 316 ? 1.64730 1.39500 0.85300 -0.20510 0.27260  -0.16070 316 GLU A CA    
2491 C  C     . GLU A 316 ? 1.59220 1.34950 0.87520 -0.18250 0.26080  -0.15410 316 GLU A C     
2492 O  O     . GLU A 316 ? 1.60450 1.33780 0.90980 -0.16170 0.28030  -0.17240 316 GLU A O     
2493 C  CB    . GLU A 316 ? 1.63060 1.41560 0.85530 -0.19830 0.29390  -0.14530 316 GLU A CB    
2494 C  CG    . GLU A 316 ? 1.86990 1.64330 1.01710 -0.21830 0.31440  -0.15290 316 GLU A CG    
2495 C  CD    . GLU A 316 ? 1.82880 1.64250 0.99500 -0.21820 0.32570  -0.12900 316 GLU A CD    
2496 O  OE1   . GLU A 316 ? 1.74130 1.58970 0.96470 -0.21200 0.30270  -0.10170 316 GLU A OE1   
2497 O  OE2   . GLU A 316 ? 1.71390 1.52280 0.83560 -0.22600 0.35710  -0.13740 316 GLU A OE2   
2498 N  N     . LEU A 317 ? 1.44950 1.23920 0.77080 -0.18630 0.22800  -0.12830 317 LEU A N     
2499 C  CA    . LEU A 317 ? 1.39280 1.19140 0.77990 -0.16910 0.21400  -0.12070 317 LEU A CA    
2500 C  C     . LEU A 317 ? 1.47110 1.22560 0.83700 -0.17500 0.20410  -0.13900 317 LEU A C     
2501 O  O     . LEU A 317 ? 1.51090 1.24870 0.91310 -0.15590 0.20960  -0.14550 317 LEU A O     
2502 C  CB    . LEU A 317 ? 1.35190 1.19290 0.77540 -0.17500 0.18300  -0.09130 317 LEU A CB    
2503 C  CG    . LEU A 317 ? 1.31080 1.19120 0.76430 -0.16690 0.19260  -0.07160 317 LEU A CG    
2504 C  CD1   . LEU A 317 ? 1.31060 1.22490 0.79140 -0.17360 0.16120  -0.04440 317 LEU A CD1   
2505 C  CD2   . LEU A 317 ? 1.32050 1.21310 0.83200 -0.14020 0.21660  -0.07410 317 LEU A CD2   
2506 N  N     . LEU A 318 ? 1.48640 1.22050 0.79200 -0.20300 0.18800  -0.14640 318 LEU A N     
2507 C  CA    . LEU A 318 ? 1.43000 1.11750 0.70790 -0.21360 0.18030  -0.16560 318 LEU A CA    
2508 C  C     . LEU A 318 ? 1.54300 1.17980 0.79850 -0.19840 0.21400  -0.19440 318 LEU A C     
2509 O  O     . LEU A 318 ? 1.64340 1.24190 0.90800 -0.19020 0.21480  -0.20630 318 LEU A O     
2510 C  CB    . LEU A 318 ? 1.42300 1.10150 0.63760 -0.24920 0.15780  -0.16960 318 LEU A CB    
2511 C  CG    . LEU A 318 ? 1.33870 1.05720 0.57550 -0.26640 0.11900  -0.14670 318 LEU A CG    
2512 C  CD1   . LEU A 318 ? 1.44010 1.15270 0.61260 -0.30030 0.09860  -0.15190 318 LEU A CD1   
2513 C  CD2   . LEU A 318 ? 1.32800 1.03290 0.59970 -0.26420 0.10730  -0.14850 318 LEU A CD2   
2514 N  N     . GLU A 319 ? 1.48870 1.12200 0.71160 -0.19510 0.24270  -0.20610 319 GLU A N     
2515 C  CA    . GLU A 319 ? 1.56700 1.15610 0.77400 -0.17660 0.27910  -0.23490 319 GLU A CA    
2516 C  C     . GLU A 319 ? 1.55640 1.15430 0.84060 -0.14000 0.29020  -0.23020 319 GLU A C     
2517 O  O     . GLU A 319 ? 1.65070 1.20260 0.93750 -0.12420 0.30140  -0.24870 319 GLU A O     
2518 C  CB    . GLU A 319 ? 1.58910 1.18300 0.75450 -0.17880 0.31090  -0.24630 319 GLU A CB    
2519 C  CG    . GLU A 319 ? 1.85250 1.41290 0.92360 -0.21300 0.30660  -0.26260 319 GLU A CG    
2520 C  CD    . GLU A 319 ? 2.09190 1.64960 1.11300 -0.21610 0.34210  -0.27680 319 GLU A CD    
2521 O  OE1   . GLU A 319 ? 2.11900 1.69570 1.18130 -0.18940 0.37520  -0.27900 319 GLU A OE1   
2522 O  OE2   . GLU A 319 ? 2.09410 1.64180 1.05880 -0.24130 0.32950  -0.27920 319 GLU A OE2   
2523 N  N     . ILE A 320 ? 1.44820 1.10320 0.79500 -0.12710 0.28460  -0.20440 320 ILE A N     
2524 C  CA    . ILE A 320 ? 1.43530 1.10460 0.85710 -0.09410 0.29110  -0.19770 320 ILE A CA    
2525 C  C     . ILE A 320 ? 1.51630 1.15680 0.95470 -0.09220 0.26630  -0.19470 320 ILE A C     
2526 O  O     . ILE A 320 ? 1.51850 1.12730 0.97900 -0.06870 0.27650  -0.20540 320 ILE A O     
2527 C  CB    . ILE A 320 ? 1.37580 1.11090 0.85660 -0.08720 0.28400  -0.16940 320 ILE A CB    
2528 C  CG1   . ILE A 320 ? 1.41230 1.17560 0.88220 -0.08800 0.31200  -0.17070 320 ILE A CG1   
2529 C  CG2   . ILE A 320 ? 1.24560 0.99700 0.80290 -0.05770 0.28180  -0.16000 320 ILE A CG2   
2530 C  CD1   . ILE A 320 ? 1.34280 1.16360 0.85440 -0.09100 0.30050  -0.14170 320 ILE A CD1   
2531 N  N     . CYS A 321 ? 1.60410 1.25280 1.02890 -0.11780 0.23410  -0.18080 321 CYS A N     
2532 C  CA    . CYS A 321 ? 1.59760 1.22090 1.03470 -0.12080 0.21150  -0.17690 321 CYS A CA    
2533 C  C     . CYS A 321 ? 1.66690 1.21790 1.05650 -0.12420 0.22080  -0.20350 321 CYS A C     
2534 O  O     . CYS A 321 ? 1.70120 1.21850 1.11220 -0.10750 0.22040  -0.20610 321 CYS A O     
2535 C  CB    . CYS A 321 ? 1.56310 1.21330 0.99250 -0.14990 0.17890  -0.15980 321 CYS A CB    
2536 S  SG    . CYS A 321 ? 1.56610 1.29100 1.05800 -0.14260 0.16450  -0.12780 321 CYS A SG    
2537 N  N     . GLU A 322 ? 1.73910 1.26170 1.06090 -0.14610 0.22900  -0.22330 322 GLU A N     
2538 C  CA    . GLU A 322 ? 1.79050 1.23850 1.05920 -0.15330 0.23780  -0.25100 322 GLU A CA    
2539 C  C     . GLU A 322 ? 1.82790 1.23870 1.11200 -0.11700 0.27040  -0.26960 322 GLU A C     
2540 O  O     . GLU A 322 ? 1.86120 1.21640 1.14440 -0.10620 0.27090  -0.27970 322 GLU A O     
2541 C  CB    . GLU A 322 ? 1.84110 1.27080 1.03130 -0.18520 0.24050  -0.26910 322 GLU A CB    
2542 C  CG    . GLU A 322 ? 1.86640 1.31680 1.03260 -0.22370 0.20510  -0.25660 322 GLU A CG    
2543 C  CD    . GLU A 322 ? 2.08010 1.52530 1.17320 -0.25290 0.20600  -0.27000 322 GLU A CD    
2544 O  OE1   . GLU A 322 ? 2.11700 1.51780 1.16070 -0.24960 0.23430  -0.29710 322 GLU A OE1   
2545 O  OE2   . GLU A 322 ? 2.04420 1.52910 1.12850 -0.27860 0.17830  -0.25380 322 GLU A OE2   
2546 N  N     . LEU A 323 ? 1.74740 1.18890 1.04740 -0.09750 0.29800  -0.27360 323 LEU A N     
2547 C  CA    . LEU A 323 ? 1.79140 1.20580 1.11110 -0.06130 0.33190  -0.29290 323 LEU A CA    
2548 C  C     . LEU A 323 ? 1.77880 1.20170 1.17360 -0.02910 0.32310  -0.27660 323 LEU A C     
2549 O  O     . LEU A 323 ? 1.87090 1.24110 1.27180 -0.00550 0.33330  -0.29090 323 LEU A O     
2550 C  CB    . LEU A 323 ? 1.69660 1.15660 1.02480 -0.05130 0.36240  -0.29660 323 LEU A CB    
2551 C  CG    . LEU A 323 ? 1.76720 1.19990 1.01560 -0.07070 0.38760  -0.32360 323 LEU A CG    
2552 C  CD1   . LEU A 323 ? 1.75500 1.24590 1.01580 -0.06720 0.41180  -0.31770 323 LEU A CD1   
2553 C  CD2   . LEU A 323 ? 1.85250 1.21060 1.06410 -0.05560 0.41630  -0.36030 323 LEU A CD2   
2554 N  N     . SER A 324 ? 1.65970 1.14470 1.10890 -0.02840 0.30200  -0.24640 324 SER A N     
2555 C  CA    . SER A 324 ? 1.59520 1.09170 1.11170 -0.00150 0.28980  -0.22900 324 SER A CA    
2556 C  C     . SER A 324 ? 1.72660 1.16570 1.22390 -0.00980 0.26700  -0.22790 324 SER A C     
2557 O  O     . SER A 324 ? 1.81830 1.22560 1.34380 0.01710  0.26770  -0.22810 324 SER A O     
2558 C  CB    . SER A 324 ? 1.49010 1.06110 1.05870 -0.00480 0.27120  -0.19880 324 SER A CB    
2559 O  OG    . SER A 324 ? 1.60620 1.18480 1.14980 -0.03770 0.24200  -0.18510 324 SER A OG    
2560 N  N     . GLN A 325 ? 1.70170 1.12480 1.14930 -0.04760 0.24710  -0.22730 325 GLN A N     
2561 C  CA    . GLN A 325 ? 1.73730 1.10390 1.16130 -0.06100 0.22780  -0.22760 325 GLN A CA    
2562 C  C     . GLN A 325 ? 1.87920 1.16260 1.26620 -0.04790 0.24710  -0.25490 325 GLN A C     
2563 O  O     . GLN A 325 ? 1.96000 1.19550 1.35560 -0.03570 0.23900  -0.25190 325 GLN A O     
2564 C  CB    . GLN A 325 ? 1.73020 1.10210 1.10930 -0.10610 0.20570  -0.22470 325 GLN A CB    
2565 C  CG    . GLN A 325 ? 1.64110 1.07840 1.06020 -0.11840 0.17960  -0.19540 325 GLN A CG    
2566 C  CD    . GLN A 325 ? 1.58400 1.03360 0.96450 -0.16020 0.15930  -0.19380 325 GLN A CD    
2567 O  OE1   . GLN A 325 ? 1.68040 1.09030 1.03080 -0.18360 0.14600  -0.19880 325 GLN A OE1   
2568 N  NE2   . GLN A 325 ? 1.46530 0.97050 0.84740 -0.17040 0.15620  -0.18620 325 GLN A NE2   
2569 N  N     . GLU A 326 ? 1.91630 1.17700 1.25760 -0.05130 0.27250  -0.28190 326 GLU A N     
2570 C  CA    . GLU A 326 ? 1.97900 1.15670 1.28350 -0.03660 0.29460  -0.31140 326 GLU A CA    
2571 C  C     . GLU A 326 ? 1.98730 1.15630 1.35210 0.01390  0.30940  -0.30960 326 GLU A C     
2572 O  O     . GLU A 326 ? 2.09620 1.20140 1.46110 0.02890  0.30400  -0.31200 326 GLU A O     
2573 C  CB    . GLU A 326 ? 2.01750 1.18060 1.26250 -0.04920 0.32160  -0.34110 326 GLU A CB    
2574 C  CG    . GLU A 326 ? 2.08530 1.20890 1.25260 -0.09750 0.30460  -0.35230 326 GLU A CG    
2575 C  CD    . GLU A 326 ? 2.31990 1.39820 1.41220 -0.11070 0.33050  -0.38790 326 GLU A CD    
2576 O  OE1   . GLU A 326 ? 2.31140 1.42250 1.40710 -0.09600 0.35770  -0.39680 326 GLU A OE1   
2577 O  OE2   . GLU A 326 ? 2.40180 1.41280 1.43020 -0.13840 0.32370  -0.40670 326 GLU A OE2   
2578 N  N     . LYS A 327 ? 1.91090 1.14830 1.33230 0.03940  0.32440  -0.30150 327 LYS A N     
2579 C  CA    . LYS A 327 ? 1.90160 1.14220 1.38730 0.08820  0.33860  -0.30020 327 LYS A CA    
2580 C  C     . LYS A 327 ? 1.94430 1.18050 1.47310 0.09940  0.30730  -0.27290 327 LYS A C     
2581 O  O     . LYS A 327 ? 2.02380 1.21340 1.57330 0.13120  0.30920  -0.27560 327 LYS A O     
2582 C  CB    . LYS A 327 ? 1.75430 1.07990 1.29620 0.10640  0.35730  -0.29340 327 LYS A CB    
2583 C  CG    . LYS A 327 ? 1.74100 1.08460 1.35890 0.15700  0.37280  -0.29240 327 LYS A CG    
2584 C  CD    . LYS A 327 ? 1.75740 1.17270 1.41400 0.17060  0.40350  -0.29760 327 LYS A CD    
2585 C  CE    . LYS A 327 ? 1.71480 1.15010 1.44880 0.22140  0.42300  -0.30130 327 LYS A CE    
2586 N  NZ    . LYS A 327 ? 1.70890 1.06590 1.44090 0.25130  0.42250  -0.31380 327 LYS A NZ    
2587 N  N     . MET A 328 ? 1.88190 1.16590 1.42390 0.07460  0.27860  -0.24610 328 MET A N     
2588 C  CA    . MET A 328 ? 1.81690 1.09990 1.39250 0.07960  0.24860  -0.21950 328 MET A CA    
2589 C  C     . MET A 328 ? 1.90610 1.10020 1.43120 0.06600  0.23580  -0.22530 328 MET A C     
2590 O  O     . MET A 328 ? 1.95560 1.11590 1.50150 0.08480  0.22160  -0.21210 328 MET A O     
2591 C  CB    . MET A 328 ? 1.76620 1.11530 1.35230 0.04940  0.22590  -0.19630 328 MET A CB    
2592 C  CG    . MET A 328 ? 1.68130 1.11440 1.32380 0.06320  0.23280  -0.18430 328 MET A CG    
2593 S  SD    . MET A 328 ? 1.61700 1.11380 1.27330 0.03180  0.20300  -0.15590 328 MET A SD    
2594 C  CE    . MET A 328 ? 1.48450 1.00260 1.20900 0.06080  0.18530  -0.13160 328 MET A CE    
2595 N  N     . SER A 329 ? 1.95190 1.10630 1.40780 0.03130  0.23970  -0.24420 329 SER A N     
2596 C  CA    . SER A 329 ? 1.96140 1.03230 1.36210 0.00870  0.22760  -0.25100 329 SER A CA    
2597 C  C     . SER A 329 ? 2.13160 1.11950 1.52450 0.04220  0.24300  -0.26770 329 SER A C     
2598 O  O     . SER A 329 ? 2.24070 1.15410 1.60220 0.03320  0.23010  -0.26620 329 SER A O     
2599 C  CB    . SER A 329 ? 1.93180 0.98560 1.26290 -0.03590 0.22960  -0.27020 329 SER A CB    
2600 O  OG    . SER A 329 ? 2.07390 1.10420 1.37430 -0.02560 0.26050  -0.30110 329 SER A OG    
2601 N  N     . SER A 330 ? 2.15340 1.15210 1.57530 0.08090  0.27130  -0.28350 330 SER A N     
2602 C  CA    . SER A 330 ? 2.17910 1.10050 1.60270 0.11910  0.28570  -0.29830 330 SER A CA    
2603 C  C     . SER A 330 ? 2.13430 1.04520 1.60660 0.14580  0.26150  -0.26960 330 SER A C     
2604 O  O     . SER A 330 ? 2.18380 1.01290 1.64490 0.16870  0.26250  -0.27570 330 SER A O     
2605 C  CB    . SER A 330 ? 2.15480 1.09850 1.60900 0.15830  0.32290  -0.32100 330 SER A CB    
2606 O  OG    . SER A 330 ? 2.11230 1.15290 1.64340 0.18000  0.32260  -0.30120 330 SER A OG    
2607 N  N     . VAL A 331 ? 2.10290 1.09050 1.62510 0.14290  0.23920  -0.23860 331 VAL A N     
2608 C  CA    . VAL A 331 ? 2.06920 1.05450 1.63520 0.16530  0.21390  -0.20950 331 VAL A CA    
2609 C  C     . VAL A 331 ? 2.05760 1.05670 1.60700 0.12600  0.18150  -0.18270 331 VAL A C     
2610 O  O     . VAL A 331 ? 2.07690 1.02490 1.61620 0.12610  0.16040  -0.16560 331 VAL A O     
2611 C  CB    . VAL A 331 ? 2.00080 1.06820 1.65210 0.20540  0.21820  -0.19710 331 VAL A CB    
2612 C  CG1   . VAL A 331 ? 1.98690 1.05240 1.68100 0.22820  0.18950  -0.16680 331 VAL A CG1   
2613 C  CG2   . VAL A 331 ? 2.03940 1.09870 1.71290 0.24530  0.25350  -0.22450 331 VAL A CG2   
2614 N  N     . PHE A 332 ? 1.98810 1.05460 1.53370 0.09260  0.17800  -0.17860 332 PHE A N     
2615 C  CA    . PHE A 332 ? 1.87520 0.97330 1.41760 0.05890  0.15060  -0.15390 332 PHE A CA    
2616 C  C     . PHE A 332 ? 1.99610 1.04750 1.47010 0.01120  0.14380  -0.16210 332 PHE A C     
2617 O  O     . PHE A 332 ? 1.96820 1.00230 1.40070 -0.00680 0.15950  -0.18660 332 PHE A O     
2618 C  CB    . PHE A 332 ? 1.78430 0.98410 1.36640 0.05140  0.14980  -0.14400 332 PHE A CB    
2619 C  CG    . PHE A 332 ? 1.68120 0.93740 1.33490 0.09020  0.15080  -0.13080 332 PHE A CG    
2620 C  CD1   . PHE A 332 ? 1.74110 0.96630 1.42540 0.12590  0.14340  -0.12080 332 PHE A CD1   
2621 C  CD2   . PHE A 332 ? 1.57260 0.91210 1.26300 0.09050  0.15860  -0.12820 332 PHE A CD2   
2622 C  CE1   . PHE A 332 ? 1.58570 0.86840 1.33950 0.16020  0.14260  -0.10900 332 PHE A CE1   
2623 C  CE2   . PHE A 332 ? 1.51580 0.90920 1.27320 0.12270  0.15970  -0.11690 332 PHE A CE2   
2624 C  CZ    . PHE A 332 ? 1.44870 0.81660 1.23960 0.15730  0.15130  -0.10780 332 PHE A CZ    
2625 N  N     . GLU A 333 ? 1.96070 0.99280 1.42200 -0.01080 0.12030  -0.14180 333 GLU A N     
2626 C  CA    . GLU A 333 ? 1.91570 0.92760 1.32420 -0.06120 0.11180  -0.14590 333 GLU A CA    
2627 C  C     . GLU A 333 ? 1.80760 0.90870 1.23060 -0.08710 0.10820  -0.14220 333 GLU A C     
2628 O  O     . GLU A 333 ? 1.82390 0.99870 1.29700 -0.06920 0.10790  -0.13080 333 GLU A O     
2629 C  CB    . GLU A 333 ? 1.89650 0.86600 1.28700 -0.08050 0.09030  -0.12500 333 GLU A CB    
2630 C  CG    . GLU A 333 ? 2.18160 1.04180 1.53390 -0.07070 0.09110  -0.13010 333 GLU A CG    
2631 C  CD    . GLU A 333 ? 2.36350 1.15760 1.64940 -0.10440 0.10110  -0.15660 333 GLU A CD    
2632 O  OE1   . GLU A 333 ? 2.33410 1.17280 1.60510 -0.13690 0.10420  -0.16840 333 GLU A OE1   
2633 O  OE2   . GLU A 333 ? 2.33850 1.03480 1.58610 -0.09910 0.10440  -0.16510 333 GLU A OE2   
2634 N  N     . ASP A 334 ? 1.81270 0.90480 1.19120 -0.13050 0.10420  -0.15190 334 ASP A N     
2635 C  CA    . ASP A 334 ? 1.71520 0.88570 1.10310 -0.15680 0.09850  -0.14890 334 ASP A CA    
2636 C  C     . ASP A 334 ? 1.61150 0.84360 1.04070 -0.16280 0.08040  -0.12150 334 ASP A C     
2637 O  O     . ASP A 334 ? 1.56560 0.87310 1.02290 -0.16760 0.07740  -0.11510 334 ASP A O     
2638 C  CB    . ASP A 334 ? 1.71630 0.85930 1.04810 -0.20160 0.09580  -0.16570 334 ASP A CB    
2639 C  CG    . ASP A 334 ? 1.86720 0.97780 1.16100 -0.19810 0.11510  -0.19490 334 ASP A CG    
2640 O  OD1   . ASP A 334 ? 1.93940 1.04330 1.25100 -0.15950 0.13320  -0.20260 334 ASP A OD1   
2641 O  OD2   . ASP A 334 ? 1.89590 0.99120 1.14310 -0.23470 0.11260  -0.21050 334 ASP A OD2   
2642 N  N     . SER A 335 ? 1.63940 0.83760 1.06910 -0.16350 0.06850  -0.10530 335 SER A N     
2643 C  CA    . SER A 335 ? 1.46990 0.72030 0.93340 -0.16910 0.05310  -0.08070 335 SER A CA    
2644 C  C     . SER A 335 ? 1.51220 0.80480 1.02980 -0.12910 0.05300  -0.06700 335 SER A C     
2645 O  O     . SER A 335 ? 1.45610 0.79270 1.00230 -0.13090 0.04090  -0.04780 335 SER A O     
2646 C  CB    . SER A 335 ? 1.51160 0.70750 0.94820 -0.18880 0.04100  -0.06800 335 SER A CB    
2647 O  OG    . SER A 335 ? 1.73950 0.87070 1.17240 -0.15840 0.04110  -0.06280 335 SER A OG    
2648 N  N     . ASN A 336 ? 1.53600 0.81460 1.06760 -0.09410 0.06660  -0.07740 336 ASN A N     
2649 C  CA    . ASN A 336 ? 1.46350 0.78870 1.05080 -0.05720 0.06800  -0.06680 336 ASN A CA    
2650 C  C     . ASN A 336 ? 1.41480 0.82640 1.03350 -0.06510 0.06830  -0.06260 336 ASN A C     
2651 O  O     . ASN A 336 ? 1.44320 0.87440 1.04480 -0.08160 0.07740  -0.07620 336 ASN A O     
2652 C  CB    . ASN A 336 ? 1.52530 0.82200 1.12080 -0.02160 0.08690  -0.08320 336 ASN A CB    
2653 C  CG    . ASN A 336 ? 1.52840 0.87080 1.18570 0.01700  0.08770  -0.07220 336 ASN A CG    
2654 O  OD1   . ASN A 336 ? 1.44040 0.85500 1.13290 0.01780  0.08910  -0.06670 336 ASN A OD1   
2655 N  ND2   . ASN A 336 ? 1.62710 0.92680 1.29870 0.04920  0.08600  -0.06860 336 ASN A ND2   
2656 N  N     . VAL A 337 ? 1.29880 0.75900 0.96080 -0.05360 0.05740  -0.04340 337 VAL A N     
2657 C  CA    . VAL A 337 ? 1.26660 0.80220 0.95580 -0.06360 0.05540  -0.03730 337 VAL A CA    
2658 C  C     . VAL A 337 ? 1.28480 0.85630 0.99200 -0.04910 0.07280  -0.04890 337 VAL A C     
2659 O  O     . VAL A 337 ? 1.26390 0.88420 0.97690 -0.06360 0.07340  -0.04820 337 VAL A O     
2660 C  CB    . VAL A 337 ? 1.20120 0.77440 0.93050 -0.05330 0.04090  -0.01610 337 VAL A CB    
2661 C  CG1   . VAL A 337 ? 1.23390 0.77580 0.93990 -0.07230 0.02490  -0.00370 337 VAL A CG1   
2662 C  CG2   . VAL A 337 ? 1.15620 0.73110 0.92380 -0.01520 0.04370  -0.01220 337 VAL A CG2   
2663 N  N     . TYR A 338 ? 1.26640 0.81470 0.98210 -0.02090 0.08770  -0.05940 338 TYR A N     
2664 C  CA    . TYR A 338 ? 1.17360 0.75500 0.90170 -0.01010 0.10780  -0.07160 338 TYR A CA    
2665 C  C     . TYR A 338 ? 1.25860 0.81560 0.93420 -0.03260 0.11960  -0.09160 338 TYR A C     
2666 O  O     . TYR A 338 ? 1.37800 0.97500 1.05030 -0.04310 0.12700  -0.09540 338 TYR A O     
2667 C  CB    . TYR A 338 ? 1.19350 0.76450 0.95410 0.02850  0.12200  -0.07700 338 TYR A CB    
2668 C  CG    . TYR A 338 ? 1.22880 0.83100 1.04470 0.05100  0.10840  -0.05720 338 TYR A CG    
2669 C  CD1   . TYR A 338 ? 1.24030 0.91090 1.09600 0.04890  0.10290  -0.04390 338 TYR A CD1   
2670 C  CD2   . TYR A 338 ? 1.21900 0.77970 1.04560 0.07380  0.09960  -0.05150 338 TYR A CD2   
2671 C  CE1   . TYR A 338 ? 1.20190 0.90070 1.10550 0.06670  0.08900  -0.02700 338 TYR A CE1   
2672 C  CE2   . TYR A 338 ? 1.20250 0.79320 1.07780 0.09320  0.08400  -0.03260 338 TYR A CE2   
2673 C  CZ    . TYR A 338 ? 1.18210 0.84300 1.09540 0.08840  0.07880  -0.02120 338 TYR A CZ    
2674 O  OH    . TYR A 338 ? 1.04940 0.74030 1.00860 0.10470  0.06200  -0.00360 338 TYR A OH    
2675 N  N     . MET A 339 ? 1.31750 0.80840 0.94800 -0.04440 0.11830  -0.10270 339 MET A N     
2676 C  CA    . MET A 339 ? 1.32670 0.79350 0.90230 -0.07350 0.12340  -0.12040 339 MET A CA    
2677 C  C     . MET A 339 ? 1.28410 0.79730 0.85480 -0.10680 0.10660  -0.10980 339 MET A C     
2678 O  O     . MET A 339 ? 1.27030 0.80790 0.82130 -0.12300 0.11050  -0.11760 339 MET A O     
2679 C  CB    . MET A 339 ? 1.42860 0.81260 0.95910 -0.08210 0.12240  -0.13230 339 MET A CB    
2680 C  CG    . MET A 339 ? 1.50890 0.83830 1.03710 -0.04890 0.14150  -0.14760 339 MET A CG    
2681 S  SD    . MET A 339 ? 1.71000 1.02430 1.20220 -0.04600 0.17140  -0.17930 339 MET A SD    
2682 C  CE    . MET A 339 ? 1.76260 1.01220 1.17490 -0.09050 0.16500  -0.19730 339 MET A CE    
2683 N  N     . LEU A 340 ? 1.23650 0.76160 0.82430 -0.11660 0.08790  -0.09190 340 LEU A N     
2684 C  CA    . LEU A 340 ? 1.26960 0.84130 0.86110 -0.14450 0.07270  -0.08150 340 LEU A CA    
2685 C  C     . LEU A 340 ? 1.21090 0.85090 0.83620 -0.13610 0.07450  -0.07360 340 LEU A C     
2686 O  O     . LEU A 340 ? 1.23950 0.91440 0.85720 -0.15660 0.06800  -0.07270 340 LEU A O     
2687 C  CB    . LEU A 340 ? 1.25550 0.82400 0.86360 -0.14880 0.05770  -0.06460 340 LEU A CB    
2688 C  CG    . LEU A 340 ? 1.36320 0.86140 0.93280 -0.16300 0.05410  -0.06950 340 LEU A CG    
2689 C  CD1   . LEU A 340 ? 1.31960 0.81890 0.90590 -0.16480 0.04100  -0.05040 340 LEU A CD1   
2690 C  CD2   . LEU A 340 ? 1.35780 0.85970 0.89390 -0.20540 0.04670  -0.07660 340 LEU A CD2   
2691 N  N     . HIS A 341 ? 1.11550 0.77430 0.77890 -0.10620 0.08270  -0.06740 341 HIS A N     
2692 C  CA    . HIS A 341 ? 1.06830 0.78580 0.76260 -0.09820 0.08670  -0.06000 341 HIS A CA    
2693 C  C     . HIS A 341 ? 1.18800 0.90870 0.85080 -0.10710 0.09930  -0.07370 341 HIS A C     
2694 O  O     . HIS A 341 ? 1.21280 0.97270 0.87430 -0.12150 0.09320  -0.06780 341 HIS A O     
2695 C  CB    . HIS A 341 ? 1.11220 0.84550 0.85170 -0.06640 0.09470  -0.05340 341 HIS A CB    
2696 C  CG    . HIS A 341 ? 1.09270 0.88370 0.86430 -0.06120 0.09870  -0.04460 341 HIS A CG    
2697 N  ND1   . HIS A 341 ? 1.01400 0.84570 0.82240 -0.06080 0.08550  -0.02720 341 HIS A ND1   
2698 C  CD2   . HIS A 341 ? 1.01200 0.82310 0.78030 -0.05800 0.11500  -0.05090 341 HIS A CD2   
2699 C  CE1   . HIS A 341 ? 0.96190 0.83400 0.78970 -0.05740 0.09270  -0.02280 341 HIS A CE1   
2700 N  NE2   . HIS A 341 ? 0.96630 0.82780 0.77020 -0.05610 0.11060  -0.03600 341 HIS A NE2   
2701 N  N     . MET A 342 ? 1.18510 0.86360 0.82170 -0.09710 0.11740  -0.09200 342 MET A N     
2702 C  CA    . MET A 342 ? 1.14710 0.82540 0.74670 -0.10680 0.13120  -0.10650 342 MET A CA    
2703 C  C     . MET A 342 ? 1.24920 0.91860 0.80290 -0.14180 0.11670  -0.11140 342 MET A C     
2704 O  O     . MET A 342 ? 1.29350 0.98810 0.82650 -0.15600 0.11610  -0.11220 342 MET A O     
2705 C  CB    . MET A 342 ? 1.32310 0.95350 0.90120 -0.08910 0.15590  -0.12820 342 MET A CB    
2706 C  CG    . MET A 342 ? 1.27760 0.92380 0.90640 -0.05320 0.17150  -0.12480 342 MET A CG    
2707 S  SD    . MET A 342 ? 1.23010 0.95410 0.90320 -0.04760 0.17540  -0.10790 342 MET A SD    
2708 C  CE    . MET A 342 ? 1.33930 1.06190 0.95690 -0.06500 0.19450  -0.12420 342 MET A CE    
2709 N  N     . MET A 343 ? 1.32760 0.96470 0.86660 -0.15710 0.10330  -0.11270 343 MET A N     
2710 C  CA    . MET A 343 ? 1.33200 0.96940 0.83650 -0.19250 0.08690  -0.11570 343 MET A CA    
2711 C  C     . MET A 343 ? 1.27110 0.97490 0.80520 -0.20310 0.06940  -0.09690 343 MET A C     
2712 O  O     . MET A 343 ? 1.26990 0.99450 0.78120 -0.22480 0.05980  -0.09840 343 MET A O     
2713 C  CB    . MET A 343 ? 1.35350 0.94600 0.84320 -0.20740 0.07750  -0.11870 343 MET A CB    
2714 C  CG    . MET A 343 ? 1.42640 0.94310 0.87280 -0.20480 0.09180  -0.14030 343 MET A CG    
2715 S  SD    . MET A 343 ? 1.72910 1.18670 1.15500 -0.22470 0.08020  -0.14090 343 MET A SD    
2716 C  CE    . MET A 343 ? 1.65010 1.02390 1.05350 -0.19590 0.10170  -0.15880 343 MET A CE    
2717 N  N     . TYR A 344 ? 1.12780 0.86320 0.71160 -0.18810 0.06390  -0.07920 344 TYR A N     
2718 C  CA    . TYR A 344 ? 1.09990 0.89460 0.71580 -0.19370 0.04940  -0.06200 344 TYR A CA    
2719 C  C     . TYR A 344 ? 1.10720 0.93420 0.72300 -0.18760 0.05470  -0.05860 344 TYR A C     
2720 O  O     . TYR A 344 ? 1.07610 0.93730 0.68940 -0.20230 0.04120  -0.05150 344 TYR A O     
2721 C  CB    . TYR A 344 ? 1.18320 0.99450 0.84650 -0.17650 0.04640  -0.04720 344 TYR A CB    
2722 C  CG    . TYR A 344 ? 1.15360 1.01870 0.85410 -0.17900 0.03320  -0.03060 344 TYR A CG    
2723 C  CD1   . TYR A 344 ? 1.18260 1.06320 0.88700 -0.19940 0.01870  -0.02660 344 TYR A CD1   
2724 C  CD2   . TYR A 344 ? 1.15300 1.05170 0.88690 -0.16040 0.03690  -0.01960 344 TYR A CD2   
2725 C  CE1   . TYR A 344 ? 1.21300 1.14120 0.95350 -0.19880 0.00900  -0.01330 344 TYR A CE1   
2726 C  CE2   . TYR A 344 ? 1.17000 1.11120 0.93640 -0.16130 0.02580  -0.00580 344 TYR A CE2   
2727 C  CZ    . TYR A 344 ? 1.23080 1.18620 1.00060 -0.17910 0.01230  -0.00330 344 TYR A CZ    
2728 O  OH    . TYR A 344 ? 1.33560 1.33220 1.13910 -0.17770 0.00340  0.00830  344 TYR A OH    
2729 N  N     . GLN A 345 ? 1.15290 0.97040 0.77220 -0.16610 0.07430  -0.06300 345 GLN A N     
2730 C  CA    . GLN A 345 ? 1.09660 0.93970 0.70920 -0.16320 0.08250  -0.06010 345 GLN A CA    
2731 C  C     . GLN A 345 ? 1.15390 0.98200 0.70910 -0.18580 0.08070  -0.07210 345 GLN A C     
2732 O  O     . GLN A 345 ? 1.21710 1.07520 0.76230 -0.19600 0.07190  -0.06310 345 GLN A O     
2733 C  CB    . GLN A 345 ? 1.10440 0.94180 0.73300 -0.13780 0.10690  -0.06430 345 GLN A CB    
2734 C  CG    . GLN A 345 ? 1.05010 0.91310 0.73720 -0.11720 0.10560  -0.04970 345 GLN A CG    
2735 C  CD    . GLN A 345 ? 1.05080 0.96110 0.76510 -0.12240 0.09110  -0.03020 345 GLN A CD    
2736 O  OE1   . GLN A 345 ? 1.09730 1.02630 0.79560 -0.13060 0.09170  -0.02570 345 GLN A OE1   
2737 N  NE2   . GLN A 345 ? 1.08410 1.01050 0.83680 -0.11710 0.07860  -0.01850 345 GLN A NE2   
2738 N  N     . ALA A 346 ? 1.15580 0.93470 0.67020 -0.19410 0.08810  -0.09230 346 ALA A N     
2739 C  CA    . ALA A 346 ? 1.17300 0.93390 0.62770 -0.21930 0.08440  -0.10580 346 ALA A CA    
2740 C  C     . ALA A 346 ? 1.16710 0.95940 0.62150 -0.24500 0.05510  -0.09500 346 ALA A C     
2741 O  O     . ALA A 346 ? 1.18480 0.99340 0.60830 -0.26210 0.04480  -0.09380 346 ALA A O     
2742 C  CB    . ALA A 346 ? 1.26300 0.95980 0.67550 -0.22500 0.09630  -0.13040 346 ALA A CB    
2743 N  N     . MET A 347 ? 1.10400 0.90560 0.59160 -0.24870 0.04130  -0.08740 347 MET A N     
2744 C  CA    . MET A 347 ? 1.11160 0.95160 0.60960 -0.27060 0.01530  -0.07710 347 MET A CA    
2745 C  C     . MET A 347 ? 1.07070 0.96480 0.59620 -0.26250 0.00550  -0.05750 347 MET A C     
2746 O  O     . MET A 347 ? 1.08500 1.00530 0.59630 -0.27980 -0.01290 -0.05250 347 MET A O     
2747 C  CB    . MET A 347 ? 1.10060 0.94490 0.63470 -0.27310 0.00730  -0.07140 347 MET A CB    
2748 C  CG    . MET A 347 ? 1.05290 0.93640 0.59960 -0.29750 -0.01640 -0.06450 347 MET A CG    
2749 S  SD    . MET A 347 ? 0.98620 0.87690 0.57360 -0.30160 -0.02100 -0.05800 347 MET A SD    
2750 C  CE    . MET A 347 ? 1.12720 1.07100 0.72700 -0.33250 -0.04640 -0.05370 347 MET A CE    
2751 N  N     . GLY A 348 ? 1.06690 0.97690 0.63160 -0.23680 0.01620  -0.04570 348 GLY A N     
2752 C  CA    . GLY A 348 ? 1.01710 0.97070 0.60530 -0.22910 0.00810  -0.02700 348 GLY A CA    
2753 C  C     . GLY A 348 ? 1.02820 0.98090 0.57280 -0.23620 0.00980  -0.02730 348 GLY A C     
2754 O  O     . GLY A 348 ? 1.09490 1.07840 0.63820 -0.24430 -0.00900 -0.01400 348 GLY A O     
2755 N  N     . VAL A 349 ? 1.02480 0.94080 0.53100 -0.23340 0.03200  -0.04280 349 VAL A N     
2756 C  CA    . VAL A 349 ? 1.07240 0.98320 0.52800 -0.24270 0.03660  -0.04490 349 VAL A CA    
2757 C  C     . VAL A 349 ? 1.11490 1.02280 0.52480 -0.27180 0.01410  -0.05080 349 VAL A C     
2758 O  O     . VAL A 349 ? 1.10990 1.03550 0.49270 -0.28280 0.00060  -0.04080 349 VAL A O     
2759 C  CB    . VAL A 349 ? 1.12870 1.00310 0.55560 -0.23210 0.06950  -0.06220 349 VAL A CB    
2760 C  CG1   . VAL A 349 ? 1.15200 1.04270 0.63030 -0.20500 0.08770  -0.05230 349 VAL A CG1   
2761 C  CG2   . VAL A 349 ? 1.29990 1.12940 0.70640 -0.23540 0.07900  -0.08550 349 VAL A CG2   
2762 N  N     . CYS A 350 ? 1.16230 1.04620 0.56050 -0.28610 0.00900  -0.06660 350 CYS A N     
2763 C  CA    . CYS A 350 ? 1.11830 1.00330 0.47810 -0.31690 -0.01470 -0.07270 350 CYS A CA    
2764 C  C     . CYS A 350 ? 1.03150 0.97370 0.42940 -0.32200 -0.04520 -0.05020 350 CYS A C     
2765 O  O     . CYS A 350 ? 1.10470 1.06530 0.47420 -0.34040 -0.06710 -0.04500 350 CYS A O     
2766 C  CB    . CYS A 350 ? 1.14740 0.99690 0.49590 -0.33210 -0.01430 -0.09210 350 CYS A CB    
2767 S  SG    . CYS A 350 ? 1.48440 1.25700 0.77500 -0.33050 0.01760  -0.12280 350 CYS A SG    
2768 N  N     . LEU A 351 ? 1.06270 1.03330 0.52500 -0.30540 -0.04750 -0.03700 351 LEU A N     
2769 C  CA    . LEU A 351 ? 1.01930 1.04420 0.52510 -0.30520 -0.07300 -0.01680 351 LEU A CA    
2770 C  C     . LEU A 351 ? 1.05430 1.10000 0.55100 -0.29690 -0.08050 0.00120  351 LEU A C     
2771 O  O     . LEU A 351 ? 1.05560 1.13340 0.55110 -0.30750 -0.10730 0.01310  351 LEU A O     
2772 C  CB    . LEU A 351 ? 1.02780 1.07120 0.59830 -0.28610 -0.06740 -0.00860 351 LEU A CB    
2773 C  CG    . LEU A 351 ? 1.03960 1.07280 0.62470 -0.29780 -0.06710 -0.02030 351 LEU A CG    
2774 C  CD1   . LEU A 351 ? 1.08050 1.13050 0.72280 -0.27860 -0.06050 -0.01100 351 LEU A CD1   
2775 C  CD2   . LEU A 351 ? 1.01860 1.07860 0.60040 -0.32530 -0.09200 -0.02210 351 LEU A CD2   
2776 N  N     . TYR A 352 ? 1.06680 1.09420 0.55640 -0.27890 -0.05740 0.00400  352 TYR A N     
2777 C  CA    . TYR A 352 ? 0.96390 1.00370 0.43690 -0.27390 -0.06180 0.02150  352 TYR A CA    
2778 C  C     . TYR A 352 ? 1.00430 1.02980 0.40640 -0.29720 -0.07220 0.01610  352 TYR A C     
2779 O  O     . TYR A 352 ? 1.03770 1.08650 0.42810 -0.30340 -0.09610 0.03370  352 TYR A O     
2780 C  CB    . TYR A 352 ? 0.91850 0.94120 0.39760 -0.25370 -0.03160 0.02320  352 TYR A CB    
2781 C  CG    . TYR A 352 ? 1.00740 1.03930 0.47010 -0.24970 -0.03260 0.04280  352 TYR A CG    
2782 C  CD1   . TYR A 352 ? 1.07400 1.13770 0.57460 -0.24030 -0.05210 0.06710  352 TYR A CD1   
2783 C  CD2   . TYR A 352 ? 1.15070 1.15620 0.55800 -0.25540 -0.01210 0.03650  352 TYR A CD2   
2784 C  CE1   . TYR A 352 ? 1.14560 1.21100 0.62700 -0.23780 -0.05360 0.08670  352 TYR A CE1   
2785 C  CE2   . TYR A 352 ? 1.25510 1.26560 0.64210 -0.25480 -0.01180 0.05570  352 TYR A CE2   
2786 C  CZ    . TYR A 352 ? 1.20110 1.23980 0.62450 -0.24630 -0.03360 0.08170  352 TYR A CZ    
2787 O  OH    . TYR A 352 ? 1.23010 1.26800 0.63010 -0.24660 -0.03400 0.10260  352 TYR A OH    
2788 N  N     . MET A 353 ? 1.05490 1.04020 0.40760 -0.31070 -0.05630 -0.00840 353 MET A N     
2789 C  CA    . MET A 353 ? 1.14590 1.11210 0.42390 -0.33630 -0.06530 -0.01810 353 MET A CA    
2790 C  C     . MET A 353 ? 1.19190 1.18450 0.46770 -0.35990 -0.10280 -0.01540 353 MET A C     
2791 O  O     . MET A 353 ? 1.24900 1.23170 0.46340 -0.38400 -0.11740 -0.02090 353 MET A O     
2792 C  CB    . MET A 353 ? 1.20170 1.11400 0.43020 -0.34310 -0.03630 -0.04820 353 MET A CB    
2793 C  CG    . MET A 353 ? 1.25130 1.14200 0.47370 -0.32220 0.00090  -0.05160 353 MET A CG    
2794 S  SD    . MET A 353 ? 1.42440 1.25300 0.60160 -0.32210 0.03900  -0.08800 353 MET A SD    
2795 C  CE    . MET A 353 ? 1.43230 1.23400 0.50690 -0.35210 0.03700  -0.10080 353 MET A CE    
2796 N  N     . GLN A 354 ? 1.15160 1.17840 0.49220 -0.35480 -0.11790 -0.00810 354 GLN A N     
2797 C  CA    . GLN A 354 ? 1.10390 1.16360 0.45730 -0.37650 -0.15110 -0.00700 354 GLN A CA    
2798 C  C     . GLN A 354 ? 1.15140 1.17700 0.45330 -0.40710 -0.15140 -0.03350 354 GLN A C     
2799 O  O     . GLN A 354 ? 1.18370 1.22650 0.47920 -0.42670 -0.17570 -0.03320 354 GLN A O     
2800 C  CB    . GLN A 354 ? 1.10920 1.20680 0.45400 -0.38170 -0.18400 0.01530  354 GLN A CB    
2801 C  CG    . GLN A 354 ? 1.07130 1.19380 0.45970 -0.35230 -0.18380 0.04180  354 GLN A CG    
2802 C  CD    . GLN A 354 ? 1.18650 1.35370 0.58750 -0.35380 -0.22210 0.06640  354 GLN A CD    
2803 O  OE1   . GLN A 354 ? 1.26040 1.44310 0.65370 -0.37130 -0.24570 0.06360  354 GLN A OE1   
2804 N  NE2   . GLN A 354 ? 1.08130 1.26470 0.51610 -0.32880 -0.22380 0.09020  354 GLN A NE2   
2805 N  N     . ASP A 355 ? 1.36510 1.33970 0.64750 -0.40350 -0.12050 -0.05470 355 ASP A N     
2806 C  CA    . ASP A 355 ? 1.41270 1.34600 0.65190 -0.43000 -0.11730 -0.08130 355 ASP A CA    
2807 C  C     . ASP A 355 ? 1.37090 1.31760 0.66630 -0.43170 -0.12050 -0.08280 355 ASP A C     
2808 O  O     . ASP A 355 ? 1.36030 1.27570 0.67320 -0.41640 -0.09600 -0.09090 355 ASP A O     
2809 C  CB    . ASP A 355 ? 1.46400 1.33140 0.64940 -0.42380 -0.08220 -0.10360 355 ASP A CB    
2810 C  CG    . ASP A 355 ? 1.62110 1.43830 0.77560 -0.44330 -0.07470 -0.12970 355 ASP A CG    
2811 O  OD1   . ASP A 355 ? 1.62530 1.45960 0.79520 -0.46500 -0.09710 -0.12930 355 ASP A OD1   
2812 O  OD2   . ASP A 355 ? 1.76610 1.52640 0.88320 -0.43590 -0.04510 -0.15020 355 ASP A OD2   
2813 N  N     . TRP A 356 ? 1.28280 1.27800 0.61070 -0.44910 -0.15020 -0.07370 356 TRP A N     
2814 C  CA    . TRP A 356 ? 1.20260 1.22110 0.58870 -0.45060 -0.15280 -0.07170 356 TRP A CA    
2815 C  C     . TRP A 356 ? 1.20280 1.16760 0.56130 -0.47050 -0.13890 -0.09520 356 TRP A C     
2816 O  O     . TRP A 356 ? 1.22500 1.17660 0.61610 -0.46040 -0.12360 -0.09630 356 TRP A O     
2817 C  CB    . TRP A 356 ? 1.15940 1.24600 0.59370 -0.46230 -0.18400 -0.05700 356 TRP A CB    
2818 C  CG    . TRP A 356 ? 1.12850 1.26470 0.58370 -0.44650 -0.20410 -0.03390 356 TRP A CG    
2819 C  CD1   . TRP A 356 ? 1.09610 1.26140 0.54820 -0.45460 -0.22880 -0.02450 356 TRP A CD1   
2820 C  CD2   . TRP A 356 ? 1.01060 1.16750 0.49900 -0.41520 -0.19890 -0.01530 356 TRP A CD2   
2821 N  NE1   . TRP A 356 ? 1.07710 1.27870 0.55140 -0.43340 -0.24260 -0.00150 356 TRP A NE1   
2822 C  CE2   . TRP A 356 ? 1.01730 1.21520 0.50950 -0.41220 -0.22630 0.00410  356 TRP A CE2   
2823 C  CE3   . TRP A 356 ? 0.98630 1.12780 0.50710 -0.38580 -0.17200 -0.01160 356 TRP A CE3   
2824 C  CZ2   . TRP A 356 ? 0.97770 1.19700 0.50250 -0.38190 -0.22640 0.02640  356 TRP A CZ2   
2825 C  CZ3   . TRP A 356 ? 0.97350 1.13960 0.52770 -0.35730 -0.17200 0.00930  356 TRP A CZ3   
2826 C  CH2   . TRP A 356 ? 0.92880 1.13110 0.48420 -0.35560 -0.19820 0.02790  356 TRP A CH2   
2827 N  N     . GLU A 357 ? 1.36370 1.29290 0.67420 -0.48930 -0.13860 -0.10940 357 GLU A N     
2828 C  CA    . GLU A 357 ? 1.40330 1.27430 0.68700 -0.50560 -0.12410 -0.13010 357 GLU A CA    
2829 C  C     . GLU A 357 ? 1.42250 1.22960 0.67850 -0.48730 -0.09350 -0.14450 357 GLU A C     
2830 O  O     . GLU A 357 ? 1.46420 1.23870 0.72910 -0.48950 -0.08260 -0.15220 357 GLU A O     
2831 C  CB    . GLU A 357 ? 1.46620 1.31060 0.70020 -0.52820 -0.12990 -0.14270 357 GLU A CB    
2832 C  CG    . GLU A 357 ? 1.45910 1.36000 0.71720 -0.55020 -0.16050 -0.13180 357 GLU A CG    
2833 C  CD    . GLU A 357 ? 1.56910 1.51530 0.82710 -0.54220 -0.18020 -0.11570 357 GLU A CD    
2834 O  OE1   . GLU A 357 ? 1.59210 1.53220 0.83720 -0.51970 -0.17000 -0.11010 357 GLU A OE1   
2835 O  OE2   . GLU A 357 ? 1.45350 1.43990 0.72300 -0.55880 -0.20600 -0.10830 357 GLU A OE2   
2836 N  N     . GLY A 358 ? 1.38640 1.17430 0.60900 -0.46850 -0.07860 -0.14770 358 GLY A N     
2837 C  CA    . GLY A 358 ? 1.38380 1.12160 0.60190 -0.44010 -0.04580 -0.15650 358 GLY A CA    
2838 C  C     . GLY A 358 ? 1.27830 1.04000 0.56760 -0.41210 -0.03850 -0.13910 358 GLY A C     
2839 O  O     . GLY A 358 ? 1.40870 1.12850 0.70560 -0.40110 -0.02140 -0.14650 358 GLY A O     
2840 N  N     . ALA A 359 ? 1.22310 1.04950 0.56310 -0.39970 -0.05180 -0.11570 359 ALA A N     
2841 C  CA    . ALA A 359 ? 1.23210 1.08210 0.63660 -0.37460 -0.04550 -0.09990 359 ALA A CA    
2842 C  C     . ALA A 359 ? 1.22840 1.07470 0.65500 -0.39120 -0.05200 -0.10210 359 ALA A C     
2843 O  O     . ALA A 359 ? 1.23690 1.06440 0.68910 -0.37520 -0.03860 -0.09950 359 ALA A O     
2844 C  CB    . ALA A 359 ? 1.15050 1.06690 0.60050 -0.36120 -0.05980 -0.07640 359 ALA A CB    
2845 N  N     . LEU A 360 ? 1.21720 1.08180 0.63270 -0.42510 -0.07310 -0.10630 360 LEU A N     
2846 C  CA    . LEU A 360 ? 1.21880 1.08120 0.65200 -0.44680 -0.07830 -0.10890 360 LEU A CA    
2847 C  C     . LEU A 360 ? 1.30770 1.08920 0.70030 -0.45100 -0.05940 -0.12670 360 LEU A C     
2848 O  O     . LEU A 360 ? 1.30600 1.06890 0.71900 -0.44860 -0.05170 -0.12370 360 LEU A O     
2849 C  CB    . LEU A 360 ? 1.10620 1.00750 0.53500 -0.48460 -0.10480 -0.11130 360 LEU A CB    
2850 C  CG    . LEU A 360 ? 1.10830 1.02060 0.55890 -0.51340 -0.11200 -0.11300 360 LEU A CG    
2851 C  CD1   . LEU A 360 ? 1.04530 1.00280 0.56220 -0.49580 -0.10870 -0.09590 360 LEU A CD1   
2852 C  CD2   . LEU A 360 ? 1.12510 1.08640 0.58890 -0.53340 -0.13280 -0.10830 360 LEU A CD2   
2853 N  N     . GLN A 361 ? 1.38870 1.11900 0.72010 -0.45900 -0.05250 -0.14570 361 GLN A N     
2854 C  CA    . GLN A 361 ? 1.44760 1.09410 0.73660 -0.46000 -0.03360 -0.16460 361 GLN A CA    
2855 C  C     . GLN A 361 ? 1.42880 1.05220 0.74690 -0.42010 -0.01210 -0.15710 361 GLN A C     
2856 O  O     . GLN A 361 ? 1.44760 1.02340 0.76340 -0.41950 -0.00380 -0.16050 361 GLN A O     
2857 C  CB    . GLN A 361 ? 1.51520 1.11750 0.73610 -0.46870 -0.02690 -0.18650 361 GLN A CB    
2858 C  CG    . GLN A 361 ? 1.55140 1.15360 0.74560 -0.50600 -0.04360 -0.19390 361 GLN A CG    
2859 C  CD    . GLN A 361 ? 1.65390 1.21070 0.78850 -0.50950 -0.03370 -0.21240 361 GLN A CD    
2860 O  OE1   . GLN A 361 ? 1.74220 1.28070 0.85200 -0.48780 -0.01720 -0.22000 361 GLN A OE1   
2861 N  NE2   . GLN A 361 ? 1.67510 1.21650 0.78690 -0.53760 -0.04300 -0.21970 361 GLN A NE2   
2862 N  N     . TYR A 362 ? 1.26290 0.91860 0.60780 -0.38770 -0.00410 -0.14610 362 TYR A N     
2863 C  CA    . TYR A 362 ? 1.22690 0.86880 0.60510 -0.35090 0.01360  -0.13800 362 TYR A CA    
2864 C  C     . TYR A 362 ? 1.26420 0.93590 0.69370 -0.34870 0.00510  -0.11980 362 TYR A C     
2865 O  O     . TYR A 362 ? 1.35820 0.99280 0.79610 -0.33630 0.01400  -0.11810 362 TYR A O     
2866 C  CB    . TYR A 362 ? 1.17880 0.85190 0.57520 -0.32080 0.02400  -0.13030 362 TYR A CB    
2867 C  CG    . TYR A 362 ? 1.29710 0.92810 0.64720 -0.31150 0.04390  -0.14910 362 TYR A CG    
2868 C  CD1   . TYR A 362 ? 1.40770 0.97680 0.74280 -0.29380 0.06510  -0.16340 362 TYR A CD1   
2869 C  CD2   . TYR A 362 ? 1.37980 1.03250 0.70160 -0.31890 0.04240  -0.15200 362 TYR A CD2   
2870 C  CE1   . TYR A 362 ? 1.44810 0.97990 0.74360 -0.28330 0.08690  -0.18280 362 TYR A CE1   
2871 C  CE2   . TYR A 362 ? 1.51390 1.12790 0.79010 -0.31140 0.06400  -0.17050 362 TYR A CE2   
2872 C  CZ    . TYR A 362 ? 1.53290 1.08780 0.79780 -0.29310 0.08770  -0.18710 362 TYR A CZ    
2873 O  OH    . TYR A 362 ? 1.65140 1.16920 0.87360 -0.28400 0.11250  -0.20770 362 TYR A OH    
2874 N  N     . GLY A 363 ? 1.21760 0.95440 0.67940 -0.36140 -0.01260 -0.10650 363 GLY A N     
2875 C  CA    . GLY A 363 ? 1.11860 0.88700 0.62670 -0.36140 -0.01870 -0.09130 363 GLY A CA    
2876 C  C     . GLY A 363 ? 1.17480 0.90010 0.66590 -0.38440 -0.01850 -0.09710 363 GLY A C     
2877 O  O     . GLY A 363 ? 1.29340 1.01180 0.80770 -0.37550 -0.01410 -0.08730 363 GLY A O     
2878 N  N     . GLN A 364 ? 1.26480 0.96150 0.71340 -0.41730 -0.02450 -0.11230 364 GLN A N     
2879 C  CA    . GLN A 364 ? 1.24410 0.89750 0.67360 -0.44430 -0.02470 -0.11740 364 GLN A CA    
2880 C  C     . GLN A 364 ? 1.28210 0.85750 0.68950 -0.42460 -0.00830 -0.12100 364 GLN A C     
2881 O  O     . GLN A 364 ? 1.38520 0.93210 0.79280 -0.43470 -0.00720 -0.11530 364 GLN A O     
2882 C  CB    . GLN A 364 ? 1.24500 0.87620 0.62820 -0.48400 -0.03410 -0.13520 364 GLN A CB    
2883 C  CG    . GLN A 364 ? 1.21550 0.92010 0.61990 -0.51130 -0.05460 -0.13170 364 GLN A CG    
2884 C  CD    . GLN A 364 ? 1.40710 1.09010 0.76820 -0.53870 -0.06150 -0.14630 364 GLN A CD    
2885 O  OE1   . GLN A 364 ? 1.58550 1.20660 0.89630 -0.53360 -0.05150 -0.16210 364 GLN A OE1   
2886 N  NE2   . GLN A 364 ? 1.52520 1.26040 0.91070 -0.56230 -0.07560 -0.13950 364 GLN A NE2   
2887 N  N     . LYS A 365 ? 1.24680 0.78810 0.63620 -0.39610 0.00460  -0.12950 365 LYS A N     
2888 C  CA    . LYS A 365 ? 1.38540 0.85960 0.76370 -0.37070 0.01930  -0.13130 365 LYS A CA    
2889 C  C     . LYS A 365 ? 1.37010 0.87710 0.79970 -0.33810 0.02170  -0.11100 365 LYS A C     
2890 O  O     . LYS A 365 ? 1.36200 0.82370 0.79200 -0.32130 0.02760  -0.10590 365 LYS A O     
2891 C  CB    . LYS A 365 ? 1.39770 0.81810 0.73720 -0.35370 0.03480  -0.15120 365 LYS A CB    
2892 C  CG    . LYS A 365 ? 1.48930 0.94810 0.83390 -0.33560 0.04130  -0.15550 365 LYS A CG    
2893 C  CD    . LYS A 365 ? 1.52880 0.91860 0.82290 -0.32790 0.05910  -0.18000 365 LYS A CD    
2894 C  CE    . LYS A 365 ? 1.56640 0.98270 0.85800 -0.30810 0.07160  -0.18650 365 LYS A CE    
2895 N  NZ    . LYS A 365 ? 1.57720 0.92270 0.82080 -0.29820 0.09310  -0.21230 365 LYS A NZ    
2896 N  N     . ILE A 366 ? 1.31680 0.89950 0.78800 -0.32980 0.01570  -0.09890 366 ILE A N     
2897 C  CA    . ILE A 366 ? 1.28460 0.89580 0.80120 -0.29870 0.01850  -0.08190 366 ILE A CA    
2898 C  C     . ILE A 366 ? 1.22980 0.85580 0.76710 -0.31240 0.01030  -0.06780 366 ILE A C     
2899 O  O     . ILE A 366 ? 1.22330 0.83630 0.77730 -0.29330 0.01280  -0.05650 366 ILE A O     
2900 C  CB    . ILE A 366 ? 1.20210 0.88070 0.75140 -0.28380 0.01690  -0.07530 366 ILE A CB    
2901 C  CG1   . ILE A 366 ? 1.27180 0.93320 0.80020 -0.26680 0.02920  -0.08750 366 ILE A CG1   
2902 C  CG2   . ILE A 366 ? 1.24860 0.96450 0.84660 -0.26050 0.01630  -0.05740 366 ILE A CG2   
2903 C  CD1   . ILE A 366 ? 1.31440 1.03440 0.85970 -0.26240 0.02580  -0.08220 366 ILE A CD1   
2904 N  N     . ILE A 367 ? 1.26220 0.91700 0.79820 -0.34640 0.00040  -0.06830 367 ILE A N     
2905 C  CA    . ILE A 367 ? 1.19530 0.88570 0.76060 -0.35800 -0.00490 -0.05460 367 ILE A CA    
2906 C  C     . ILE A 367 ? 1.29980 0.93070 0.84440 -0.36280 -0.00100 -0.04950 367 ILE A C     
2907 O  O     . ILE A 367 ? 1.20080 0.84500 0.76760 -0.35310 -0.00070 -0.03560 367 ILE A O     
2908 C  CB    . ILE A 367 ? 1.08480 0.82540 0.65920 -0.39310 -0.01520 -0.05720 367 ILE A CB    
2909 C  CG1   . ILE A 367 ? 0.94550 0.72780 0.55460 -0.40170 -0.01640 -0.04430 367 ILE A CG1   
2910 C  CG2   . ILE A 367 ? 1.22760 0.92240 0.75650 -0.42850 -0.01770 -0.07130 367 ILE A CG2   
2911 C  CD1   . ILE A 367 ? 0.93880 0.76150 0.58970 -0.36880 -0.01400 -0.03170 367 ILE A CD1   
2912 N  N     . LYS A 368 ? 1.50360 1.06340 1.00140 -0.37820 0.00170  -0.06050 368 LYS A N     
2913 C  CA    . LYS A 368 ? 1.54090 1.03980 1.01510 -0.38590 0.00350  -0.05330 368 LYS A CA    
2914 C  C     . LYS A 368 ? 1.54330 1.01300 1.02740 -0.34690 0.00710  -0.04200 368 LYS A C     
2915 O  O     . LYS A 368 ? 1.53310 1.00270 1.02540 -0.34760 0.00440  -0.02660 368 LYS A O     
2916 C  CB    . LYS A 368 ? 1.61470 1.03650 1.03460 -0.40940 0.00550  -0.06820 368 LYS A CB    
2917 C  CG    . LYS A 368 ? 1.66400 1.01520 1.05150 -0.42490 0.00600  -0.06050 368 LYS A CG    
2918 C  CD    . LYS A 368 ? 1.92330 1.19640 1.25560 -0.45120 0.00790  -0.07700 368 LYS A CD    
2919 C  CE    . LYS A 368 ? 2.01000 1.20600 1.30730 -0.46480 0.00820  -0.06700 368 LYS A CE    
2920 N  NZ    . LYS A 368 ? 2.06470 1.19860 1.31810 -0.47740 0.01100  -0.07990 368 LYS A NZ    
2921 N  N     . PRO A 369 ? 1.39700 0.84440 0.88160 -0.31340 0.01300  -0.04840 369 PRO A N     
2922 C  CA    . PRO A 369 ? 1.36140 0.79970 0.86850 -0.27580 0.01380  -0.03540 369 PRO A CA    
2923 C  C     . PRO A 369 ? 1.30170 0.81260 0.85580 -0.26400 0.00930  -0.02080 369 PRO A C     
2924 O  O     . PRO A 369 ? 1.39150 0.89590 0.95700 -0.25050 0.00490  -0.00600 369 PRO A O     
2925 C  CB    . PRO A 369 ? 1.43960 0.85670 0.94540 -0.24540 0.02350  -0.04850 369 PRO A CB    
2926 C  CG    . PRO A 369 ? 1.40900 0.78370 0.87020 -0.26940 0.02810  -0.06820 369 PRO A CG    
2927 C  CD    . PRO A 369 ? 1.40570 0.82700 0.86640 -0.30890 0.02010  -0.06810 369 PRO A CD    
2928 N  N     . TYR A 370 ? 1.29770 0.87490 0.87660 -0.26980 0.00910  -0.02470 370 TYR A N     
2929 C  CA    . TYR A 370 ? 1.28890 0.93290 0.91100 -0.26030 0.00550  -0.01290 370 TYR A CA    
2930 C  C     . TYR A 370 ? 1.26610 0.91910 0.89050 -0.27910 0.00080  -0.00120 370 TYR A C     
2931 O  O     . TYR A 370 ? 1.25020 0.92170 0.89660 -0.26390 -0.00150 0.01080  370 TYR A O     
2932 C  CB    . TYR A 370 ? 1.23910 0.94400 0.88030 -0.26870 0.00450  -0.01910 370 TYR A CB    
2933 C  CG    . TYR A 370 ? 1.23900 0.97000 0.90150 -0.24090 0.00880  -0.02110 370 TYR A CG    
2934 C  CD1   . TYR A 370 ? 1.35570 1.04990 1.01170 -0.21490 0.01660  -0.02490 370 TYR A CD1   
2935 C  CD2   . TYR A 370 ? 1.15880 0.95150 0.84910 -0.24060 0.00560  -0.01860 370 TYR A CD2   
2936 C  CE1   . TYR A 370 ? 1.42510 1.14600 1.10090 -0.19230 0.02300  -0.02670 370 TYR A CE1   
2937 C  CE2   . TYR A 370 ? 1.21300 1.02670 0.91890 -0.21820 0.01010  -0.01880 370 TYR A CE2   
2938 C  CZ    . TYR A 370 ? 1.37170 1.15070 1.06990 -0.19560 0.01980  -0.02320 370 TYR A CZ    
2939 O  OH    . TYR A 370 ? 1.43160 1.23320 1.14520 -0.17600 0.02690  -0.02360 370 TYR A OH    
2940 N  N     . SER A 371 ? 1.22930 0.86890 0.82920 -0.31420 0.00010  -0.00500 371 SER A N     
2941 C  CA    . SER A 371 ? 1.13370 0.78720 0.73480 -0.33650 -0.00100 0.00470  371 SER A CA    
2942 C  C     . SER A 371 ? 1.23190 0.83550 0.81470 -0.32590 -0.00270 0.01810  371 SER A C     
2943 O  O     . SER A 371 ? 1.32300 0.94890 0.91610 -0.32930 -0.00350 0.02900  371 SER A O     
2944 C  CB    . SER A 371 ? 1.31860 0.96470 0.89620 -0.37860 -0.00020 -0.00270 371 SER A CB    
2945 O  OG    . SER A 371 ? 1.54240 1.11990 1.07840 -0.38630 0.00010  -0.01160 371 SER A OG    
2946 N  N     . LYS A 372 ? 1.26970 0.80500 0.82440 -0.31210 -0.00380 0.01730  372 LYS A N     
2947 C  CA    . LYS A 372 ? 1.36460 0.84540 0.89890 -0.30090 -0.00880 0.03170  372 LYS A CA    
2948 C  C     . LYS A 372 ? 1.29460 0.79050 0.85940 -0.26020 -0.01350 0.03990  372 LYS A C     
2949 O  O     . LYS A 372 ? 1.32760 0.80630 0.88730 -0.25240 -0.02100 0.05520  372 LYS A O     
2950 C  CB    . LYS A 372 ? 1.36480 0.75900 0.85510 -0.30380 -0.00870 0.02740  372 LYS A CB    
2951 C  CG    . LYS A 372 ? 1.42360 0.79240 0.87940 -0.34540 -0.00450 0.01670  372 LYS A CG    
2952 C  CD    . LYS A 372 ? 1.56680 0.84190 0.97860 -0.34270 -0.00400 0.01140  372 LYS A CD    
2953 C  CE    . LYS A 372 ? 1.66940 0.91150 1.04270 -0.38620 -0.00060 -0.00070 372 LYS A CE    
2954 N  NZ    . LYS A 372 ? 1.76890 0.91120 1.09640 -0.38210 0.00040  -0.00670 372 LYS A NZ    
2955 N  N     . HIS A 373 ? 1.17460 0.70290 0.76960 -0.23610 -0.00980 0.03070  373 HIS A N     
2956 C  CA    . HIS A 373 ? 1.19430 0.74100 0.82200 -0.20000 -0.01380 0.03830  373 HIS A CA    
2957 C  C     . HIS A 373 ? 1.13920 0.74840 0.79790 -0.20090 -0.01740 0.04690  373 HIS A C     
2958 O  O     . HIS A 373 ? 1.08770 0.70080 0.76090 -0.18240 -0.02510 0.05850  373 HIS A O     
2959 C  CB    . HIS A 373 ? 1.25210 0.81060 0.89980 -0.17570 -0.00600 0.02580  373 HIS A CB    
2960 C  CG    . HIS A 373 ? 1.27130 0.76290 0.89080 -0.16650 -0.00130 0.01670  373 HIS A CG    
2961 N  ND1   . HIS A 373 ? 1.38520 0.80970 0.97760 -0.16240 -0.00760 0.02490  373 HIS A ND1   
2962 C  CD2   . HIS A 373 ? 1.20140 0.67920 0.81250 -0.16060 0.00960  -0.00050 373 HIS A CD2   
2963 C  CE1   . HIS A 373 ? 1.48790 0.85910 1.05940 -0.15260 -0.00020 0.01240  373 HIS A CE1   
2964 N  NE2   . HIS A 373 ? 1.36720 0.77010 0.94850 -0.15200 0.01110  -0.00420 373 HIS A NE2   
2965 N  N     . TYR A 374 ? 1.11520 0.77390 0.78560 -0.22110 -0.01250 0.04070  374 TYR A N     
2966 C  CA    . TYR A 374 ? 1.04470 0.76150 0.74480 -0.22180 -0.01360 0.04570  374 TYR A CA    
2967 C  C     . TYR A 374 ? 1.11700 0.82690 0.79750 -0.24460 -0.01550 0.05450  374 TYR A C     
2968 O  O     . TYR A 374 ? 1.12840 0.79690 0.77310 -0.26720 -0.01460 0.05580  374 TYR A O     
2969 C  CB    . TYR A 374 ? 0.89650 0.66680 0.61850 -0.23160 -0.00800 0.03560  374 TYR A CB    
2970 C  CG    . TYR A 374 ? 0.96580 0.75930 0.71290 -0.20800 -0.00590 0.03020  374 TYR A CG    
2971 C  CD1   . TYR A 374 ? 0.95680 0.78120 0.73630 -0.18540 -0.00760 0.03590  374 TYR A CD1   
2972 C  CD2   . TYR A 374 ? 1.05810 0.84100 0.79300 -0.21090 -0.00170 0.01900  374 TYR A CD2   
2973 C  CE1   . TYR A 374 ? 0.83160 0.67630 0.63190 -0.16670 -0.00400 0.03200  374 TYR A CE1   
2974 C  CE2   . TYR A 374 ? 1.04420 0.84660 0.79660 -0.19160 0.00210  0.01450  374 TYR A CE2   
2975 C  CZ    . TYR A 374 ? 0.88480 0.71850 0.67070 -0.16980 0.00150  0.02160  374 TYR A CZ    
2976 O  OH    . TYR A 374 ? 1.01730 0.86980 0.81860 -0.15360 0.00700  0.01780  374 TYR A OH    
2977 N  N     . PRO A 375 ? 1.03690 0.78450 0.73740 -0.24080 -0.01700 0.06020  375 PRO A N     
2978 C  CA    . PRO A 375 ? 1.01910 0.76420 0.69870 -0.26420 -0.01550 0.06660  375 PRO A CA    
2979 C  C     . PRO A 375 ? 1.02140 0.79200 0.69900 -0.29510 -0.00510 0.05780  375 PRO A C     
2980 O  O     . PRO A 375 ? 1.00740 0.80730 0.70540 -0.29650 -0.00170 0.04750  375 PRO A O     
2981 C  CB    . PRO A 375 ? 0.94920 0.73530 0.65550 -0.25070 -0.01760 0.06990  375 PRO A CB    
2982 C  CG    . PRO A 375 ? 0.81680 0.60840 0.55010 -0.21880 -0.02430 0.07050  375 PRO A CG    
2983 C  CD    . PRO A 375 ? 0.85490 0.64170 0.59330 -0.21520 -0.01970 0.06120  375 PRO A CD    
2984 N  N     . LEU A 376 ? 1.05870 0.81870 0.71050 -0.32120 -0.00050 0.06270  376 LEU A N     
2985 C  CA    . LEU A 376 ? 1.05610 0.83880 0.70540 -0.35460 0.01020  0.05510  376 LEU A CA    
2986 C  C     . LEU A 376 ? 0.98340 0.83880 0.68060 -0.35150 0.01580  0.04390  376 LEU A C     
2987 O  O     . LEU A 376 ? 0.96940 0.84370 0.67760 -0.36340 0.01710  0.03510  376 LEU A O     
2988 C  CB    . LEU A 376 ? 1.00610 0.78170 0.62860 -0.38060 0.01780  0.06180  376 LEU A CB    
2989 C  CG    . LEU A 376 ? 1.06320 0.77290 0.63150 -0.40690 0.01760  0.07070  376 LEU A CG    
2990 C  CD1   . LEU A 376 ? 1.37390 1.01540 0.91360 -0.38430 0.00270  0.08270  376 LEU A CD1   
2991 C  CD2   . LEU A 376 ? 1.21190 0.93030 0.75920 -0.43330 0.02840  0.07600  376 LEU A CD2   
2992 N  N     . TYR A 377 ? 0.91540 0.81010 0.64030 -0.33550 0.01770  0.04410  377 TYR A N     
2993 C  CA    . TYR A 377 ? 0.83400 0.79290 0.60570 -0.32700 0.02140  0.03540  377 TYR A CA    
2994 C  C     . TYR A 377 ? 0.76390 0.72580 0.55650 -0.29350 0.01260  0.03680  377 TYR A C     
2995 O  O     . TYR A 377 ? 0.79890 0.75560 0.59440 -0.27630 0.00970  0.04210  377 TYR A O     
2996 C  CB    . TYR A 377 ? 0.78150 0.77890 0.56810 -0.33430 0.03240  0.03300  377 TYR A CB    
2997 C  CG    . TYR A 377 ? 0.84340 0.83640 0.60610 -0.36950 0.04380  0.03220  377 TYR A CG    
2998 C  CD1   . TYR A 377 ? 0.90040 0.93520 0.68490 -0.39140 0.05190  0.02360  377 TYR A CD1   
2999 C  CD2   . TYR A 377 ? 0.93770 0.88370 0.65470 -0.38240 0.04570  0.04120  377 TYR A CD2   
3000 C  CE1   . TYR A 377 ? 0.92780 0.96030 0.69160 -0.42650 0.06400  0.02300  377 TYR A CE1   
3001 C  CE2   . TYR A 377 ? 0.99970 0.93800 0.69030 -0.41730 0.05760  0.04180  377 TYR A CE2   
3002 C  CZ    . TYR A 377 ? 0.99420 0.97680 0.70930 -0.44010 0.06800  0.03210  377 TYR A CZ    
3003 O  OH    . TYR A 377 ? 1.13590 1.11410 0.82890 -0.46630 0.07840  0.03000  377 TYR A OH    
3004 N  N     . SER A 378 ? 0.72400 0.69300 0.52820 -0.28690 0.00840  0.03220  378 SER A N     
3005 C  CA    . SER A 378 ? 0.78360 0.75370 0.60420 -0.25860 0.00240  0.03330  378 SER A CA    
3006 C  C     . SER A 378 ? 0.83810 0.85310 0.68730 -0.25680 0.00180  0.02700  378 SER A C     
3007 O  O     . SER A 378 ? 0.83990 0.86010 0.68210 -0.27520 0.00120  0.02140  378 SER A O     
3008 C  CB    . SER A 378 ? 0.85420 0.77100 0.64760 -0.25020 -0.00220 0.03530  378 SER A CB    
3009 O  OG    . SER A 378 ? 0.92990 0.85580 0.74150 -0.22670 -0.00450 0.03390  378 SER A OG    
3010 N  N     . LEU A 379 ? 0.77450 0.81940 0.65370 -0.23580 0.00030  0.02860  379 LEU A N     
3011 C  CA    . LEU A 379 ? 0.74550 0.82860 0.64930 -0.23150 -0.00290 0.02560  379 LEU A CA    
3012 C  C     . LEU A 379 ? 0.78800 0.84960 0.67350 -0.22940 -0.00720 0.02340  379 LEU A C     
3013 O  O     . LEU A 379 ? 0.84140 0.92690 0.73320 -0.23600 -0.01170 0.02000  379 LEU A O     
3014 C  CB    . LEU A 379 ? 0.76570 0.87680 0.70110 -0.20990 -0.00340 0.02930  379 LEU A CB    
3015 C  CG    . LEU A 379 ? 0.64600 0.77930 0.59820 -0.21280 0.00270  0.02810  379 LEU A CG    
3016 C  CD1   . LEU A 379 ? 0.71950 0.87430 0.70080 -0.19210 0.00220  0.03040  379 LEU A CD1   
3017 C  CD2   . LEU A 379 ? 0.64850 0.81600 0.61320 -0.23210 0.00610  0.02220  379 LEU A CD2   
3018 N  N     . ASN A 380 ? 0.75070 0.76850 0.61400 -0.21970 -0.00620 0.02480  380 ASN A N     
3019 C  CA    . ASN A 380 ? 0.75600 0.74910 0.59830 -0.21790 -0.00680 0.01990  380 ASN A CA    
3020 C  C     . ASN A 380 ? 0.81680 0.79410 0.63230 -0.24450 -0.00810 0.01230  380 ASN A C     
3021 O  O     . ASN A 380 ? 0.94510 0.93000 0.75230 -0.25210 -0.01140 0.00620  380 ASN A O     
3022 C  CB    . ASN A 380 ? 0.79910 0.74860 0.62730 -0.20090 -0.00370 0.02200  380 ASN A CB    
3023 C  CG    . ASN A 380 ? 0.82770 0.79440 0.68360 -0.17750 -0.00340 0.02920  380 ASN A CG    
3024 O  OD1   . ASN A 380 ? 0.78910 0.78050 0.66490 -0.17690 -0.00510 0.03410  380 ASN A OD1   
3025 N  ND2   . ASN A 380 ? 0.88550 0.83910 0.74280 -0.15940 -0.00010 0.02890  380 ASN A ND2   
3026 N  N     . VAL A 381 ? 0.78720 0.74610 0.58880 -0.26210 -0.00630 0.01290  381 VAL A N     
3027 C  CA    . VAL A 381 ? 0.81400 0.75620 0.59000 -0.29160 -0.00700 0.00590  381 VAL A CA    
3028 C  C     . VAL A 381 ? 0.82340 0.82300 0.62410 -0.30890 -0.01110 0.00250  381 VAL A C     
3029 O  O     . VAL A 381 ? 0.94550 0.94840 0.73420 -0.32630 -0.01630 -0.00480 381 VAL A O     
3030 C  CB    . VAL A 381 ? 0.75670 0.66110 0.50910 -0.30700 -0.00320 0.00970  381 VAL A CB    
3031 C  CG1   . VAL A 381 ? 0.77410 0.66300 0.50130 -0.34210 -0.00320 0.00280  381 VAL A CG1   
3032 C  CG2   . VAL A 381 ? 0.90430 0.75090 0.63380 -0.28770 -0.00270 0.01410  381 VAL A CG2   
3033 N  N     . ALA A 382 ? 0.74660 0.79180 0.58200 -0.30500 -0.00910 0.00700  382 ALA A N     
3034 C  CA    . ALA A 382 ? 0.65340 0.75900 0.52140 -0.31630 -0.01310 0.00440  382 ALA A CA    
3035 C  C     . ALA A 382 ? 0.73570 0.86270 0.61250 -0.30630 -0.02350 0.00330  382 ALA A C     
3036 O  O     . ALA A 382 ? 0.84320 0.99680 0.72400 -0.32430 -0.03190 -0.00120 382 ALA A O     
3037 C  CB    . ALA A 382 ? 0.82030 0.96650 0.72560 -0.30530 -0.00730 0.00840  382 ALA A CB    
3038 N  N     A SER A 383 ? 0.78210 0.90070 0.66240 -0.27890 -0.02390 0.00820  383 SER A N     
3039 C  CA    A SER A 383 ? 0.78250 0.91830 0.66580 -0.26990 -0.03280 0.00910  383 SER A CA    
3040 C  C     A SER A 383 ? 0.84190 0.94550 0.68460 -0.28600 -0.03670 0.00090  383 SER A C     
3041 O  O     A SER A 383 ? 0.89320 1.01910 0.73350 -0.29370 -0.04740 -0.00090 383 SER A O     
3042 C  CB    A SER A 383 ? 0.84610 0.97380 0.73700 -0.24070 -0.02960 0.01600  383 SER A CB    
3043 O  OG    A SER A 383 ? 0.86630 0.94500 0.73210 -0.23260 -0.02120 0.01460  383 SER A OG    
3044 N  N     . MET A 384 ? 0.91390 0.96240 0.72210 -0.29120 -0.02890 -0.00440 384 MET A N     
3045 C  CA    . MET A 384 ? 0.91960 0.93220 0.68620 -0.30760 -0.03100 -0.01480 384 MET A CA    
3046 C  C     . MET A 384 ? 0.91360 0.94520 0.67600 -0.34170 -0.03960 -0.02110 384 MET A C     
3047 O  O     . MET A 384 ? 0.97900 1.01660 0.72400 -0.35600 -0.04910 -0.02760 384 MET A O     
3048 C  CB    . MET A 384 ? 0.93270 0.87820 0.66550 -0.30330 -0.02070 -0.01920 384 MET A CB    
3049 C  CG    . MET A 384 ? 1.12800 1.04440 0.84480 -0.27960 -0.01420 -0.02190 384 MET A CG    
3050 S  SD    . MET A 384 ? 1.25810 1.17940 0.94670 -0.29010 -0.01990 -0.03210 384 MET A SD    
3051 C  CE    . MET A 384 ? 1.16790 1.04080 0.81010 -0.32440 -0.02160 -0.04710 384 MET A CE    
3052 N  N     . TRP A 385 ? 0.82300 0.86650 0.60070 -0.35700 -0.03630 -0.01910 385 TRP A N     
3053 C  CA    . TRP A 385 ? 0.83010 0.90480 0.61470 -0.39070 -0.04340 -0.02420 385 TRP A CA    
3054 C  C     . TRP A 385 ? 0.82850 0.97240 0.65010 -0.38950 -0.05730 -0.02170 385 TRP A C     
3055 O  O     . TRP A 385 ? 0.86650 1.03110 0.68340 -0.41440 -0.06940 -0.02770 385 TRP A O     
3056 C  CB    . TRP A 385 ? 0.81790 0.90120 0.61780 -0.40480 -0.03420 -0.02120 385 TRP A CB    
3057 C  CG    . TRP A 385 ? 0.88680 0.90190 0.64270 -0.42100 -0.02580 -0.02410 385 TRP A CG    
3058 C  CD1   . TRP A 385 ? 0.91620 0.89430 0.66110 -0.41090 -0.01550 -0.01740 385 TRP A CD1   
3059 C  CD2   . TRP A 385 ? 0.92880 0.90100 0.64330 -0.45140 -0.02850 -0.03370 385 TRP A CD2   
3060 N  NE1   . TRP A 385 ? 0.89420 0.80750 0.59400 -0.43110 -0.01210 -0.02070 385 TRP A NE1   
3061 C  CE2   . TRP A 385 ? 0.96030 0.86690 0.64050 -0.45640 -0.01890 -0.03140 385 TRP A CE2   
3062 C  CE3   . TRP A 385 ? 0.92030 0.90080 0.62100 -0.47570 -0.03940 -0.04390 385 TRP A CE3   
3063 C  CZ2   . TRP A 385 ? 1.04780 0.89350 0.68120 -0.48390 -0.01850 -0.03910 385 TRP A CZ2   
3064 C  CZ3   . TRP A 385 ? 1.02020 0.94200 0.67360 -0.50490 -0.03870 -0.05330 385 TRP A CZ3   
3065 C  CH2   . TRP A 385 ? 1.02140 0.87470 0.64190 -0.50830 -0.02750 -0.05100 385 TRP A CH2   
3066 N  N     . LEU A 386 ? 0.80260 0.98120 0.66040 -0.36080 -0.05730 -0.01240 386 LEU A N     
3067 C  CA    . LEU A 386 ? 0.78070 1.02200 0.67590 -0.35510 -0.07160 -0.00760 386 LEU A CA    
3068 C  C     . LEU A 386 ? 0.88340 1.11500 0.74990 -0.35500 -0.08520 -0.00890 386 LEU A C     
3069 O  O     . LEU A 386 ? 0.87640 1.14580 0.75100 -0.37080 -0.10230 -0.00980 386 LEU A O     
3070 C  CB    . LEU A 386 ? 0.72560 0.99330 0.66050 -0.32350 -0.06660 0.00230  386 LEU A CB    
3071 C  CG    . LEU A 386 ? 0.75850 1.08980 0.74150 -0.31060 -0.07890 0.00960  386 LEU A CG    
3072 C  CD1   . LEU A 386 ? 0.71640 1.10100 0.73000 -0.33500 -0.08680 0.00520  386 LEU A CD1   
3073 C  CD2   . LEU A 386 ? 0.75930 1.10030 0.77430 -0.28390 -0.06790 0.01580  386 LEU A CD2   
3074 N  N     . LYS A 387 ? 0.99150 1.17520 0.82490 -0.33740 -0.07800 -0.00880 387 LYS A N     
3075 C  CA    . LYS A 387 ? 1.02530 1.19240 0.82220 -0.33900 -0.08670 -0.01170 387 LYS A CA    
3076 C  C     . LYS A 387 ? 1.06730 1.21620 0.82680 -0.37350 -0.09450 -0.02490 387 LYS A C     
3077 O  O     . LYS A 387 ? 1.08410 1.25430 0.83140 -0.38690 -0.11160 -0.02630 387 LYS A O     
3078 C  CB    . LYS A 387 ? 1.04630 1.16050 0.81300 -0.31780 -0.07160 -0.01300 387 LYS A CB    
3079 C  CG    . LYS A 387 ? 1.14580 1.27390 0.94040 -0.28610 -0.06590 -0.00060 387 LYS A CG    
3080 C  CD    . LYS A 387 ? 1.28930 1.36640 1.05530 -0.27010 -0.04980 -0.00440 387 LYS A CD    
3081 C  CE    . LYS A 387 ? 1.28660 1.37320 1.08140 -0.24160 -0.04210 0.00680  387 LYS A CE    
3082 N  NZ    . LYS A 387 ? 1.19890 1.24170 0.97140 -0.22720 -0.02630 0.00240  387 LYS A NZ    
3083 N  N     . LEU A 388 ? 0.97890 1.08430 0.71630 -0.38930 -0.08300 -0.03410 388 LEU A N     
3084 C  CA    . LEU A 388 ? 0.89220 0.97340 0.59260 -0.42530 -0.08910 -0.04760 388 LEU A CA    
3085 C  C     . LEU A 388 ? 0.90880 1.05440 0.64050 -0.45180 -0.10740 -0.04670 388 LEU A C     
3086 O  O     . LEU A 388 ? 0.95180 1.10470 0.66050 -0.47540 -0.12340 -0.05390 388 LEU A O     
3087 C  CB    . LEU A 388 ? 0.87150 0.89530 0.54890 -0.43610 -0.07360 -0.05430 388 LEU A CB    
3088 C  CG    . LEU A 388 ? 1.02410 0.97320 0.65660 -0.41890 -0.05950 -0.06100 388 LEU A CG    
3089 C  CD1   . LEU A 388 ? 1.10340 0.99590 0.71710 -0.42650 -0.04690 -0.06400 388 LEU A CD1   
3090 C  CD2   . LEU A 388 ? 1.11080 1.02950 0.69370 -0.43160 -0.06490 -0.07480 388 LEU A CD2   
3091 N  N     . GLY A 389 ? 0.84030 1.03390 0.62450 -0.44950 -0.10480 -0.03890 389 GLY A N     
3092 C  CA    . GLY A 389 ? 0.79500 1.05750 0.61930 -0.47250 -0.12000 -0.03820 389 GLY A CA    
3093 C  C     . GLY A 389 ? 0.90730 1.21920 0.74820 -0.46430 -0.14300 -0.03200 389 GLY A C     
3094 O  O     . GLY A 389 ? 1.01140 1.34880 0.85590 -0.47870 -0.15640 -0.03330 389 GLY A O     
3095 N  N     . ARG A 390 ? 0.85180 1.16630 0.70190 -0.42850 -0.14220 -0.02120 390 ARG A N     
3096 C  CA    . ARG A 390 ? 0.78890 1.14590 0.65200 -0.41870 -0.16490 -0.01200 390 ARG A CA    
3097 C  C     . ARG A 390 ? 0.88210 1.20520 0.68360 -0.43610 -0.17770 -0.01920 390 ARG A C     
3098 O  O     . ARG A 390 ? 1.01490 1.37470 0.82050 -0.44450 -0.20090 -0.01500 390 ARG A O     
3099 C  CB    . ARG A 390 ? 0.84370 1.20520 0.72900 -0.37810 -0.15910 0.00210  390 ARG A CB    
3100 C  CG    . ARG A 390 ? 0.75170 1.16740 0.70570 -0.36130 -0.15610 0.01030  390 ARG A CG    
3101 C  CD    . ARG A 390 ? 0.77390 1.18020 0.74340 -0.32360 -0.14640 0.02170  390 ARG A CD    
3102 N  NE    . ARG A 390 ? 0.77130 1.22820 0.80440 -0.30750 -0.14410 0.02760  390 ARG A NE    
3103 C  CZ    . ARG A 390 ? 0.88020 1.33280 0.93510 -0.27760 -0.13370 0.03530  390 ARG A CZ    
3104 N  NH1   . ARG A 390 ? 0.95250 1.35730 0.97520 -0.26100 -0.12510 0.03930  390 ARG A NH1   
3105 N  NH2   . ARG A 390 ? 0.90970 1.40810 1.02110 -0.26460 -0.13120 0.03800  390 ARG A NH2   
3106 N  N     . LEU A 391 ? 0.86650 1.11680 0.61100 -0.43740 -0.16110 -0.02970 391 LEU A N     
3107 C  CA    . LEU A 391 ? 0.92380 1.13710 0.60450 -0.45770 -0.17000 -0.04080 391 LEU A CA    
3108 C  C     . LEU A 391 ? 0.99680 1.21910 0.67340 -0.49070 -0.17960 -0.04960 391 LEU A C     
3109 O  O     . LEU A 391 ? 1.04040 1.27830 0.70320 -0.50030 -0.19700 -0.04880 391 LEU A O     
3110 C  CB    . LEU A 391 ? 0.90610 1.03900 0.53340 -0.44800 -0.14570 -0.05180 391 LEU A CB    
3111 C  CG    . LEU A 391 ? 0.88090 0.99890 0.50590 -0.41070 -0.13300 -0.04220 391 LEU A CG    
3112 C  CD1   . LEU A 391 ? 0.98890 1.03750 0.58050 -0.40000 -0.10690 -0.05310 391 LEU A CD1   
3113 C  CD2   . LEU A 391 ? 0.91230 1.03660 0.50270 -0.41140 -0.14750 -0.03910 391 LEU A CD2   
3114 N  N     . TYR A 392 ? 0.95570 1.16600 0.64590 -0.50440 -0.16610 -0.05570 392 TYR A N     
3115 C  CA    . TYR A 392 ? 0.95750 1.17650 0.64980 -0.53180 -0.17080 -0.06150 392 TYR A CA    
3116 C  C     . TYR A 392 ? 0.99900 1.29810 0.74300 -0.53130 -0.19290 -0.05080 392 TYR A C     
3117 O  O     . TYR A 392 ? 1.25050 1.55850 0.97930 -0.54920 -0.20850 -0.05420 392 TYR A O     
3118 C  CB    . TYR A 392 ? 0.97490 1.17920 0.68300 -0.54230 -0.15220 -0.06480 392 TYR A CB    
3119 C  CG    . TYR A 392 ? 1.05440 1.17110 0.70500 -0.55080 -0.13390 -0.07690 392 TYR A CG    
3120 C  CD1   . TYR A 392 ? 1.17400 1.23480 0.76520 -0.56740 -0.13480 -0.08990 392 TYR A CD1   
3121 C  CD2   . TYR A 392 ? 1.02340 1.11100 0.67910 -0.54110 -0.11580 -0.07540 392 TYR A CD2   
3122 C  CE1   . TYR A 392 ? 1.24080 1.21790 0.78150 -0.57150 -0.11750 -0.10150 392 TYR A CE1   
3123 C  CE2   . TYR A 392 ? 1.06340 1.06790 0.66840 -0.54580 -0.10060 -0.08530 392 TYR A CE2   
3124 C  CZ    . TYR A 392 ? 1.20530 1.15440 0.75410 -0.55980 -0.10110 -0.09860 392 TYR A CZ    
3125 O  OH    . TYR A 392 ? 1.24230 1.10570 0.74280 -0.56090 -0.08560 -0.10880 392 TYR A OH    
3126 N  N     . MET A 393 ? 0.97320 1.33030 0.77990 -0.51020 -0.19450 -0.03850 393 MET A N     
3127 C  CA    . MET A 393 ? 1.02880 1.46220 0.89130 -0.50420 -0.21510 -0.02820 393 MET A CA    
3128 C  C     . MET A 393 ? 1.04520 1.48510 0.88380 -0.49810 -0.23900 -0.02190 393 MET A C     
3129 O  O     . MET A 393 ? 1.28610 1.76020 1.13550 -0.50960 -0.25940 -0.02030 393 MET A O     
3130 C  CB    . MET A 393 ? 1.05600 1.54030 0.98500 -0.47680 -0.20980 -0.01700 393 MET A CB    
3131 C  CG    . MET A 393 ? 1.04040 1.53090 1.00010 -0.48320 -0.18740 -0.02200 393 MET A CG    
3132 S  SD    . MET A 393 ? 1.41700 1.93840 1.39860 -0.51460 -0.18860 -0.02980 393 MET A SD    
3133 C  CE    . MET A 393 ? 1.13970 1.67110 1.15900 -0.51150 -0.15970 -0.03120 393 MET A CE    
3134 N  N     . GLY A 394 ? 0.92870 1.33610 0.73350 -0.48050 -0.23690 -0.01780 394 GLY A N     
3135 C  CA    . GLY A 394 ? 1.14230 1.54780 0.91490 -0.47500 -0.25690 -0.01090 394 GLY A CA    
3136 C  C     . GLY A 394 ? 1.12740 1.49780 0.84270 -0.50300 -0.26400 -0.02310 394 GLY A C     
3137 O  O     . GLY A 394 ? 1.12710 1.51910 0.83410 -0.50630 -0.28700 -0.01700 394 GLY A O     
3138 N  N     . LEU A 395 ? 1.07840 1.39260 0.75320 -0.52350 -0.24510 -0.04030 395 LEU A N     
3139 C  CA    . LEU A 395 ? 1.15630 1.43220 0.77520 -0.55040 -0.24990 -0.05350 395 LEU A CA    
3140 C  C     . LEU A 395 ? 1.28910 1.59530 0.93600 -0.57650 -0.25770 -0.05820 395 LEU A C     
3141 O  O     . LEU A 395 ? 1.35190 1.62370 0.95480 -0.60300 -0.25960 -0.07090 395 LEU A O     
3142 C  CB    . LEU A 395 ? 1.17200 1.36270 0.72670 -0.55650 -0.22500 -0.07050 395 LEU A CB    
3143 C  CG    . LEU A 395 ? 1.11870 1.27430 0.63690 -0.53330 -0.21530 -0.06920 395 LEU A CG    
3144 C  CD1   . LEU A 395 ? 1.14190 1.21900 0.61240 -0.53420 -0.18760 -0.08650 395 LEU A CD1   
3145 C  CD2   . LEU A 395 ? 1.16570 1.31860 0.64240 -0.53440 -0.23090 -0.06670 395 LEU A CD2   
3146 N  N     . GLU A 396 ? 1.32550 1.69510 1.04460 -0.56930 -0.26100 -0.04880 396 GLU A N     
3147 C  CA    . GLU A 396 ? 1.32110 1.73440 1.08040 -0.59060 -0.26810 -0.05120 396 GLU A CA    
3148 C  C     . GLU A 396 ? 1.34110 1.70830 1.07670 -0.61630 -0.24670 -0.06520 396 GLU A C     
3149 O  O     . GLU A 396 ? 1.36440 1.74590 1.10540 -0.64360 -0.25310 -0.07120 396 GLU A O     
3150 C  CB    . GLU A 396 ? 1.35400 1.80010 1.11020 -0.60510 -0.29730 -0.04950 396 GLU A CB    
3151 C  CG    . GLU A 396 ? 1.33150 1.81790 1.10950 -0.57710 -0.31830 -0.03310 396 GLU A CG    
3152 C  CD    . GLU A 396 ? 1.38250 1.94820 1.24890 -0.55770 -0.32600 -0.02060 396 GLU A CD    
3153 O  OE1   . GLU A 396 ? 1.45880 2.06260 1.36580 -0.57450 -0.32710 -0.02530 396 GLU A OE1   
3154 O  OE2   . GLU A 396 ? 1.44330 2.03190 1.33850 -0.52580 -0.32950 -0.00690 396 GLU A OE2   
3155 N  N     . HIS A 397 ? 1.31220 1.62050 1.01810 -0.60910 -0.22270 -0.07040 397 HIS A N     
3156 C  CA    . HIS A 397 ? 1.35000 1.61480 1.03930 -0.62900 -0.20190 -0.08030 397 HIS A CA    
3157 C  C     . HIS A 397 ? 1.31410 1.62340 1.06560 -0.61970 -0.19010 -0.07230 397 HIS A C     
3158 O  O     . HIS A 397 ? 1.28890 1.56810 1.03790 -0.60680 -0.17060 -0.07130 397 HIS A O     
3159 C  CB    . HIS A 397 ? 1.35230 1.52790 0.97820 -0.62490 -0.18280 -0.09000 397 HIS A CB    
3160 C  CG    . HIS A 397 ? 1.41700 1.54140 0.97730 -0.63570 -0.18900 -0.10130 397 HIS A CG    
3161 N  ND1   . HIS A 397 ? 1.39860 1.53280 0.94300 -0.62070 -0.20200 -0.09790 397 HIS A ND1   
3162 C  CD2   . HIS A 397 ? 1.48870 1.55060 0.99360 -0.66010 -0.18320 -0.11620 397 HIS A CD2   
3163 C  CE1   . HIS A 397 ? 1.44230 1.52300 0.92360 -0.63540 -0.20260 -0.11100 397 HIS A CE1   
3164 N  NE2   . HIS A 397 ? 1.50650 1.54250 0.96390 -0.65890 -0.19140 -0.12290 397 HIS A NE2   
3165 N  N     . LYS A 398 ? 1.24790 1.63020 1.05590 -0.62650 -0.20210 -0.06730 398 LYS A N     
3166 C  CA    . LYS A 398 ? 1.17300 1.60870 1.04660 -0.61350 -0.19170 -0.06000 398 LYS A CA    
3167 C  C     . LYS A 398 ? 1.17790 1.57530 1.03960 -0.62680 -0.16570 -0.06500 398 LYS A C     
3168 O  O     . LYS A 398 ? 1.24920 1.65810 1.13990 -0.60900 -0.15030 -0.05970 398 LYS A O     
3169 C  CB    . LYS A 398 ? 1.19500 1.71710 1.13480 -0.61670 -0.20830 -0.05530 398 LYS A CB    
3170 C  CG    . LYS A 398 ? 1.36260 1.93210 1.32790 -0.59690 -0.23470 -0.04630 398 LYS A CG    
3171 C  CD    . LYS A 398 ? 1.57450 2.22870 1.61480 -0.59740 -0.24640 -0.04230 398 LYS A CD    
3172 C  CE    . LYS A 398 ? 1.63890 2.33990 1.70240 -0.58420 -0.27770 -0.03380 398 LYS A CE    
3173 N  NZ    . LYS A 398 ? 1.51570 2.30190 1.65960 -0.58290 -0.28920 -0.03070 398 LYS A NZ    
3174 N  N     . ALA A 399 ? 1.11110 1.46350 0.93090 -0.65810 -0.16060 -0.07440 399 ALA A N     
3175 C  CA    . ALA A 399 ? 1.12710 1.44530 0.93710 -0.67020 -0.13720 -0.07640 399 ALA A CA    
3176 C  C     . ALA A 399 ? 1.22100 1.47420 0.99600 -0.65080 -0.12040 -0.07520 399 ALA A C     
3177 O  O     . ALA A 399 ? 1.24500 1.50460 1.04280 -0.63860 -0.10460 -0.06960 399 ALA A O     
3178 C  CB    . ALA A 399 ? 1.14610 1.42250 0.91390 -0.70770 -0.13590 -0.08600 399 ALA A CB    
3179 N  N     . ALA A 400 ? 1.21460 1.40720 0.93600 -0.64620 -0.12390 -0.08060 400 ALA A N     
3180 C  CA    . ALA A 400 ? 1.24200 1.37660 0.93500 -0.62560 -0.10980 -0.07990 400 ALA A CA    
3181 C  C     . ALA A 400 ? 1.10020 1.28290 0.83910 -0.59370 -0.11080 -0.06970 400 ALA A C     
3182 O  O     . ALA A 400 ? 1.08310 1.24330 0.82400 -0.57840 -0.09620 -0.06570 400 ALA A O     
3183 C  CB    . ALA A 400 ? 1.13520 1.19980 0.76480 -0.62610 -0.11270 -0.08990 400 ALA A CB    
3184 N  N     . GLY A 401 ? 1.00950 1.25770 0.78590 -0.58330 -0.12880 -0.06470 401 GLY A N     
3185 C  CA    . GLY A 401 ? 1.09120 1.38700 0.91410 -0.55290 -0.13070 -0.05440 401 GLY A CA    
3186 C  C     . GLY A 401 ? 1.08780 1.42290 0.96140 -0.54660 -0.11640 -0.04880 401 GLY A C     
3187 O  O     . GLY A 401 ? 1.07450 1.40630 0.96190 -0.52560 -0.10540 -0.04360 401 GLY A O     
3188 N  N     . GLU A 402 ? 1.16070 1.53680 1.06430 -0.56470 -0.11660 -0.05030 402 GLU A N     
3189 C  CA    . GLU A 402 ? 1.12880 1.54210 1.07740 -0.56130 -0.10060 -0.04720 402 GLU A CA    
3190 C  C     . GLU A 402 ? 1.14300 1.49180 1.05370 -0.56550 -0.07830 -0.04830 402 GLU A C     
3191 O  O     . GLU A 402 ? 1.11030 1.47070 1.04460 -0.54940 -0.06430 -0.04360 402 GLU A O     
3192 C  CB    . GLU A 402 ? 1.13730 1.60180 1.11960 -0.58390 -0.10400 -0.05040 402 GLU A CB    
3193 C  CG    . GLU A 402 ? 1.14930 1.66360 1.18540 -0.57820 -0.08720 -0.04830 402 GLU A CG    
3194 C  CD    . GLU A 402 ? 1.33080 1.90230 1.40660 -0.60000 -0.09060 -0.05210 402 GLU A CD    
3195 O  OE1   . GLU A 402 ? 1.23870 1.83900 1.32510 -0.60880 -0.11230 -0.05340 402 GLU A OE1   
3196 O  OE2   . GLU A 402 ? 1.40560 1.99400 1.50200 -0.60890 -0.07150 -0.05380 402 GLU A OE2   
3197 N  N     . LYS A 403 ? 1.08350 1.36180 0.93440 -0.58700 -0.07520 -0.05430 403 LYS A N     
3198 C  CA    . LYS A 403 ? 0.99840 1.20740 0.80900 -0.58900 -0.05710 -0.05370 403 LYS A CA    
3199 C  C     . LYS A 403 ? 0.96670 1.15650 0.77650 -0.55930 -0.05290 -0.04830 403 LYS A C     
3200 O  O     . LYS A 403 ? 0.99340 1.17990 0.81410 -0.54900 -0.03880 -0.04280 403 LYS A O     
3201 C  CB    . LYS A 403 ? 1.05960 1.19020 0.80470 -0.61040 -0.05820 -0.06120 403 LYS A CB    
3202 C  CG    . LYS A 403 ? 1.15060 1.27580 0.88330 -0.64390 -0.05500 -0.06540 403 LYS A CG    
3203 C  CD    . LYS A 403 ? 1.30920 1.34340 0.97270 -0.66080 -0.05300 -0.07230 403 LYS A CD    
3204 C  CE    . LYS A 403 ? 1.35040 1.37800 0.99890 -0.69660 -0.05210 -0.07700 403 LYS A CE    
3205 N  NZ    . LYS A 403 ? 1.35130 1.38830 1.01280 -0.70750 -0.03660 -0.07080 403 LYS A NZ    
3206 N  N     . ALA A 404 ? 0.98340 1.16370 0.78100 -0.54590 -0.06550 -0.04990 404 ALA A N     
3207 C  CA    . ALA A 404 ? 0.90280 1.06280 0.69760 -0.52010 -0.06230 -0.04560 404 ALA A CA    
3208 C  C     . ALA A 404 ? 0.88300 1.10910 0.73740 -0.49830 -0.05960 -0.03700 404 ALA A C     
3209 O  O     . ALA A 404 ? 0.90540 1.11560 0.76340 -0.48330 -0.04820 -0.03190 404 ALA A O     
3210 C  CB    . ALA A 404 ? 0.88220 1.02340 0.65060 -0.51260 -0.07620 -0.05030 404 ALA A CB    
3211 N  N     . LEU A 405 ? 0.84420 1.14310 0.74610 -0.49530 -0.07020 -0.03510 405 LEU A N     
3212 C  CA    . LEU A 405 ? 0.77130 1.13140 0.73170 -0.47230 -0.06710 -0.02820 405 LEU A CA    
3213 C  C     . LEU A 405 ? 0.85880 1.22120 0.83270 -0.47600 -0.04590 -0.02790 405 LEU A C     
3214 O  O     . LEU A 405 ? 0.79580 1.17160 0.79310 -0.45630 -0.03590 -0.02350 405 LEU A O     
3215 C  CB    . LEU A 405 ? 0.69130 1.12570 0.70130 -0.46710 -0.08340 -0.02630 405 LEU A CB    
3216 C  CG    . LEU A 405 ? 0.66990 1.11170 0.67170 -0.45740 -0.10630 -0.02310 405 LEU A CG    
3217 C  CD1   . LEU A 405 ? 0.75120 1.26680 0.80570 -0.45080 -0.12360 -0.01900 405 LEU A CD1   
3218 C  CD2   . LEU A 405 ? 0.72540 1.15200 0.72380 -0.43180 -0.10570 -0.01670 405 LEU A CD2   
3219 N  N     . LYS A 406 ? 0.85370 1.20420 0.81200 -0.50210 -0.03870 -0.03260 406 LYS A N     
3220 C  CA    . LYS A 406 ? 0.82540 1.17380 0.78850 -0.50740 -0.01810 -0.03200 406 LYS A CA    
3221 C  C     . LYS A 406 ? 0.87700 1.15740 0.79720 -0.50130 -0.00690 -0.02790 406 LYS A C     
3222 O  O     . LYS A 406 ? 0.88280 1.16890 0.81440 -0.49200 0.00750  -0.02470 406 LYS A O     
3223 C  CB    . LYS A 406 ? 0.91810 1.26370 0.86840 -0.53890 -0.01290 -0.03690 406 LYS A CB    
3224 C  CG    . LYS A 406 ? 0.98680 1.41020 0.99130 -0.54600 -0.01870 -0.04030 406 LYS A CG    
3225 C  CD    . LYS A 406 ? 1.13200 1.54610 1.11890 -0.58030 -0.01190 -0.04500 406 LYS A CD    
3226 C  CE    . LYS A 406 ? 1.15300 1.64390 1.19440 -0.59030 -0.01960 -0.04880 406 LYS A CE    
3227 N  NZ    . LYS A 406 ? 1.17110 1.66090 1.20340 -0.62320 -0.00770 -0.05290 406 LYS A NZ    
3228 N  N     . LYS A 407 ? 0.94260 1.15680 0.81270 -0.50600 -0.01320 -0.02840 407 LYS A N     
3229 C  CA    . LYS A 407 ? 0.96910 1.12030 0.80420 -0.49620 -0.00500 -0.02330 407 LYS A CA    
3230 C  C     . LYS A 407 ? 0.87970 1.05700 0.74590 -0.46730 -0.00450 -0.01770 407 LYS A C     
3231 O  O     . LYS A 407 ? 0.84110 1.00360 0.70510 -0.45410 0.00720  -0.01210 407 LYS A O     
3232 C  CB    . LYS A 407 ? 0.93130 1.00820 0.71260 -0.50280 -0.01200 -0.02640 407 LYS A CB    
3233 C  CG    . LYS A 407 ? 0.94670 0.97630 0.68600 -0.52980 -0.00910 -0.03050 407 LYS A CG    
3234 C  CD    . LYS A 407 ? 1.06010 1.03790 0.76930 -0.53330 0.00410  -0.02340 407 LYS A CD    
3235 C  CE    . LYS A 407 ? 1.26840 1.15540 0.91690 -0.54360 0.00330  -0.02480 407 LYS A CE    
3236 N  NZ    . LYS A 407 ? 1.22790 1.10750 0.85790 -0.56910 -0.00150 -0.03390 407 LYS A NZ    
3237 N  N     . ALA A 408 ? 0.78520 1.00110 0.67950 -0.44750 -0.01720 -0.01820 408 ALA A N     
3238 C  CA    . ALA A 408 ? 0.77900 1.01510 0.70130 -0.40880 -0.01660 -0.01190 408 ALA A CA    
3239 C  C     . ALA A 408 ? 0.84630 1.13400 0.81210 -0.40540 -0.00500 -0.01090 408 ALA A C     
3240 O  O     . ALA A 408 ? 0.89980 1.17540 0.86810 -0.38380 0.00410  -0.00670 408 ALA A O     
3241 C  CB    . ALA A 408 ? 0.78370 1.05090 0.72510 -0.39250 -0.03300 -0.01120 408 ALA A CB    
3242 N  N     . ILE A 409 ? 0.77670 1.12380 0.77810 -0.42680 -0.00490 -0.01580 409 ILE A N     
3243 C  CA    . ILE A 409 ? 0.67510 1.07090 0.71880 -0.41870 0.00910  -0.01720 409 ILE A CA    
3244 C  C     . ILE A 409 ? 0.79050 1.14510 0.80200 -0.42800 0.02830  -0.01670 409 ILE A C     
3245 O  O     . ILE A 409 ? 0.81900 1.18830 0.84730 -0.41500 0.04130  -0.01650 409 ILE A O     
3246 C  CB    . ILE A 409 ? 0.62100 1.07590 0.70370 -0.42890 0.00620  -0.02270 409 ILE A CB    
3247 C  CG1   . ILE A 409 ? 0.70390 1.20850 0.82740 -0.41210 -0.01390 -0.02050 409 ILE A CG1   
3248 C  CG2   . ILE A 409 ? 0.69990 1.19340 0.81650 -0.42660 0.02600  -0.02690 409 ILE A CG2   
3249 C  CD1   . ILE A 409 ? 0.83860 1.39670 0.99730 -0.42360 -0.02200 -0.02450 409 ILE A CD1   
3250 N  N     . ALA A 410 ? 0.87540 1.17660 0.83780 -0.45130 0.02990  -0.01670 410 ALA A N     
3251 C  CA    . ALA A 410 ? 0.87240 1.13050 0.79850 -0.46150 0.04530  -0.01410 410 ALA A CA    
3252 C  C     . ALA A 410 ? 0.86970 1.09460 0.78040 -0.44250 0.04820  -0.00710 410 ALA A C     
3253 O  O     . ALA A 410 ? 0.91700 1.13760 0.82120 -0.44060 0.06170  -0.00560 410 ALA A O     
3254 C  CB    . ALA A 410 ? 0.97030 1.16700 0.84250 -0.48650 0.04270  -0.01310 410 ALA A CB    
3255 N  N     . ILE A 411 ? 0.80480 1.00250 0.70640 -0.42100 0.03480  -0.00350 411 ILE A N     
3256 C  CA    . ILE A 411 ? 0.79390 0.95960 0.68350 -0.39110 0.03550  0.00290  411 ILE A CA    
3257 C  C     . ILE A 411 ? 0.79430 1.01260 0.73100 -0.36520 0.03850  0.00120  411 ILE A C     
3258 O  O     . ILE A 411 ? 0.84110 1.05270 0.77560 -0.35350 0.04700  0.00290  411 ILE A O     
3259 C  CB    . ILE A 411 ? 0.81100 0.92520 0.67330 -0.37280 0.02270  0.00710  411 ILE A CB    
3260 C  CG1   . ILE A 411 ? 0.95440 1.00820 0.76770 -0.39640 0.02150  0.00790  411 ILE A CG1   
3261 C  CG2   . ILE A 411 ? 0.79380 0.88340 0.65100 -0.34320 0.02250  0.01380  411 ILE A CG2   
3262 C  CD1   . ILE A 411 ? 0.89610 0.90510 0.68630 -0.38140 0.01100  0.00790  411 ILE A CD1   
3263 N  N     . MET A 412 ? 0.74030 1.00830 0.71790 -0.35610 0.03050  -0.00220 412 MET A N     
3264 C  CA    . MET A 412 ? 0.71070 1.02170 0.73250 -0.32860 0.03120  -0.00290 412 MET A CA    
3265 C  C     . MET A 412 ? 0.75680 1.10840 0.80640 -0.33420 0.04880  -0.00930 412 MET A C     
3266 O  O     . MET A 412 ? 0.82440 1.18720 0.89350 -0.31110 0.05440  -0.01040 412 MET A O     
3267 C  CB    . MET A 412 ? 0.70050 1.05330 0.75660 -0.31980 0.01640  -0.00300 412 MET A CB    
3268 C  CG    . MET A 412 ? 0.76050 1.07570 0.79010 -0.30850 0.00130  0.00250  412 MET A CG    
3269 S  SD    . MET A 412 ? 0.69120 1.05220 0.75070 -0.30310 -0.01800 0.00370  412 MET A SD    
3270 C  CE    . MET A 412 ? 0.71100 1.10570 0.81620 -0.26660 -0.01820 0.00870  412 MET A CE    
3271 N  N     . GLU A 413 ? 0.73130 1.10530 0.78320 -0.36520 0.05920  -0.01450 413 GLU A N     
3272 C  CA    . GLU A 413 ? 0.72700 1.13900 0.80240 -0.37210 0.08030  -0.02210 413 GLU A CA    
3273 C  C     . GLU A 413 ? 0.75830 1.12590 0.79750 -0.36460 0.09160  -0.02030 413 GLU A C     
3274 O  O     . GLU A 413 ? 0.77320 1.16470 0.83340 -0.35210 0.10530  -0.02680 413 GLU A O     
3275 C  CB    . GLU A 413 ? 0.74500 1.16710 0.81290 -0.40140 0.08870  -0.02680 413 GLU A CB    
3276 C  CG    . GLU A 413 ? 0.82360 1.30470 0.93970 -0.40310 0.08090  -0.03160 413 GLU A CG    
3277 C  CD    . GLU A 413 ? 0.96210 1.44830 1.06820 -0.43140 0.08950  -0.03610 413 GLU A CD    
3278 O  OE1   . GLU A 413 ? 1.02260 1.45230 1.07290 -0.45210 0.09340  -0.03270 413 GLU A OE1   
3279 O  OE2   . GLU A 413 ? 0.88990 1.43590 1.04430 -0.43280 0.09150  -0.04210 413 GLU A OE2   
3280 N  N     . VAL A 414 ? 0.73920 1.04070 0.72360 -0.37150 0.08500  -0.01190 414 VAL A N     
3281 C  CA    . VAL A 414 ? 0.73880 0.99580 0.68600 -0.36460 0.09040  -0.00790 414 VAL A CA    
3282 C  C     . VAL A 414 ? 0.74300 0.99470 0.70540 -0.32840 0.08080  -0.00600 414 VAL A C     
3283 O  O     . VAL A 414 ? 0.75030 1.00840 0.71850 -0.31650 0.08980  -0.01030 414 VAL A O     
3284 C  CB    . VAL A 414 ? 0.73080 0.91970 0.61830 -0.38170 0.08390  0.00210  414 VAL A CB    
3285 C  CG1   . VAL A 414 ? 0.75090 0.89480 0.60220 -0.37040 0.08330  0.00850  414 VAL A CG1   
3286 C  CG2   . VAL A 414 ? 0.83020 1.01940 0.69750 -0.42100 0.09640  0.00060  414 VAL A CG2   
3287 N  N     . ALA A 415 ? 0.77910 1.01840 0.74660 -0.31230 0.06330  -0.00040 415 ALA A N     
3288 C  CA    . ALA A 415 ? 0.71640 0.94400 0.69260 -0.28160 0.05440  0.00320  415 ALA A CA    
3289 C  C     . ALA A 415 ? 0.70310 0.97940 0.72910 -0.26140 0.05720  -0.00280 415 ALA A C     
3290 O  O     . ALA A 415 ? 0.63540 0.90620 0.66700 -0.24340 0.05970  -0.00400 415 ALA A O     
3291 C  CB    . ALA A 415 ? 0.69770 0.89670 0.66170 -0.27190 0.03810  0.01060  415 ALA A CB    
3292 N  N     . HIS A 416 ? 0.69770 1.02060 0.76030 -0.26420 0.05570  -0.00640 416 HIS A N     
3293 C  CA    . HIS A 416 ? 0.65190 1.01830 0.76380 -0.24150 0.05480  -0.00980 416 HIS A CA    
3294 C  C     . HIS A 416 ? 0.67610 1.08630 0.81980 -0.24500 0.07370  -0.02140 416 HIS A C     
3295 O  O     . HIS A 416 ? 0.72260 1.16150 0.90560 -0.22250 0.07590  -0.02550 416 HIS A O     
3296 C  CB    . HIS A 416 ? 0.61370 1.00880 0.75050 -0.23890 0.03890  -0.00570 416 HIS A CB    
3297 C  CG    . HIS A 416 ? 0.68050 1.03920 0.79400 -0.22780 0.02260  0.00400  416 HIS A CG    
3298 N  ND1   . HIS A 416 ? 0.73600 1.09410 0.86540 -0.20150 0.01380  0.00960  416 HIS A ND1   
3299 C  CD2   . HIS A 416 ? 0.68130 1.00230 0.75650 -0.23980 0.01520  0.00820  416 HIS A CD2   
3300 C  CE1   . HIS A 416 ? 0.75700 1.08240 0.85930 -0.19910 0.00310  0.01690  416 HIS A CE1   
3301 N  NE2   . HIS A 416 ? 0.73520 1.03770 0.80540 -0.22060 0.00400  0.01530  416 HIS A NE2   
3302 N  N     . GLY A 417 ? 0.69310 1.10770 0.82040 -0.27260 0.08830  -0.02670 417 GLY A N     
3303 C  CA    . GLY A 417 ? 0.76270 1.22580 0.92210 -0.28000 0.10940  -0.03910 417 GLY A CA    
3304 C  C     . GLY A 417 ? 0.75600 1.27610 0.95760 -0.29230 0.10570  -0.04110 417 GLY A C     
3305 O  O     . GLY A 417 ? 0.73210 1.26490 0.95410 -0.28070 0.08530  -0.03450 417 GLY A O     
3306 N  N     . LYS A 418 ? 0.69520 1.25090 0.90870 -0.31770 0.12480  -0.04990 418 LYS A N     
3307 C  CA    . LYS A 418 ? 0.72840 1.33200 0.97700 -0.33080 0.11880  -0.05120 418 LYS A CA    
3308 C  C     . LYS A 418 ? 0.88500 1.55290 1.20510 -0.30450 0.10960  -0.05350 418 LYS A C     
3309 O  O     . LYS A 418 ? 0.91350 1.61020 1.25800 -0.30820 0.09270  -0.04980 418 LYS A O     
3310 C  CB    . LYS A 418 ? 0.73600 1.34730 0.97520 -0.35370 0.13910  -0.05900 418 LYS A CB    
3311 C  CG    . LYS A 418 ? 0.79530 1.33990 0.96120 -0.38120 0.14150  -0.05320 418 LYS A CG    
3312 C  CD    . LYS A 418 ? 0.90460 1.45620 1.05930 -0.40910 0.15350  -0.05740 418 LYS A CD    
3313 C  CE    . LYS A 418 ? 1.01330 1.49360 1.09270 -0.43380 0.15550  -0.05070 418 LYS A CE    
3314 N  NZ    . LYS A 418 ? 1.00010 1.48520 1.06620 -0.46270 0.16730  -0.05420 418 LYS A NZ    
3315 N  N     . ASP A 419 ? 0.95150 1.63640 1.30270 -0.27590 0.11900  -0.05940 419 ASP A N     
3316 C  CA    . ASP A 419 ? 0.90860 1.65150 1.32960 -0.24680 0.11160  -0.06150 419 ASP A CA    
3317 C  C     . ASP A 419 ? 0.90140 1.61660 1.32040 -0.21670 0.08480  -0.04870 419 ASP A C     
3318 O  O     . ASP A 419 ? 0.89200 1.63950 1.36070 -0.18670 0.07800  -0.04820 419 ASP A O     
3319 C  CB    . ASP A 419 ? 0.99560 1.76470 1.45060 -0.22840 0.13840  -0.07650 419 ASP A CB    
3320 C  CG    . ASP A 419 ? 1.11270 1.81650 1.51890 -0.21670 0.14880  -0.07890 419 ASP A CG    
3321 O  OD1   . ASP A 419 ? 1.07820 1.72270 1.42110 -0.23310 0.14330  -0.07130 419 ASP A OD1   
3322 O  OD2   . ASP A 419 ? 1.23340 1.94560 1.66540 -0.19120 0.16230  -0.08910 419 ASP A OD2   
3323 N  N     . HIS A 420 ? 0.76860 1.42420 1.13180 -0.22360 0.07050  -0.03800 420 HIS A N     
3324 C  CA    . HIS A 420 ? 0.73310 1.35830 1.08820 -0.19770 0.04920  -0.02620 420 HIS A CA    
3325 C  C     . HIS A 420 ? 0.72280 1.39090 1.11440 -0.19210 0.02530  -0.01810 420 HIS A C     
3326 O  O     . HIS A 420 ? 0.76250 1.45940 1.15870 -0.21740 0.01900  -0.01870 420 HIS A O     
3327 C  CB    . HIS A 420 ? 0.75400 1.31040 1.04360 -0.20810 0.04240  -0.01830 420 HIS A CB    
3328 C  CG    . HIS A 420 ? 0.72100 1.24010 0.99790 -0.18180 0.02920  -0.00860 420 HIS A CG    
3329 N  ND1   . HIS A 420 ? 0.73280 1.25630 1.01690 -0.17090 0.00720  0.00240  420 HIS A ND1   
3330 C  CD2   . HIS A 420 ? 0.73690 1.21360 0.99230 -0.16700 0.03500  -0.00810 420 HIS A CD2   
3331 C  CE1   . HIS A 420 ? 0.71250 1.19820 0.98100 -0.15070 0.00210  0.00960  420 HIS A CE1   
3332 N  NE2   . HIS A 420 ? 0.75050 1.20860 1.00360 -0.14820 0.01820  0.00320  420 HIS A NE2   
3333 N  N     . PRO A 421 ? 0.65100 1.32280 1.06700 -0.16080 0.01050  -0.01000 421 PRO A N     
3334 C  CA    . PRO A 421 ? 0.62680 1.33510 1.07100 -0.15520 -0.01600 0.00040  421 PRO A CA    
3335 C  C     . PRO A 421 ? 0.70210 1.38890 1.10250 -0.18030 -0.03340 0.00770  421 PRO A C     
3336 O  O     . PRO A 421 ? 0.78500 1.51490 1.20690 -0.19270 -0.05010 0.01020  421 PRO A O     
3337 C  CB    . PRO A 421 ? 0.57380 1.26080 1.02680 -0.11910 -0.02740 0.01090  421 PRO A CB    
3338 C  CG    . PRO A 421 ? 0.49880 1.17050 0.96080 -0.10310 -0.00340 0.00030  421 PRO A CG    
3339 C  CD    . PRO A 421 ? 0.62360 1.26760 1.04350 -0.13050 0.01740  -0.01000 421 PRO A CD    
3340 N  N     . TYR A 422 ? 0.67840 1.30050 1.01920 -0.18780 -0.03020 0.01030  422 TYR A N     
3341 C  CA    . TYR A 422 ? 0.72470 1.32020 1.02100 -0.21000 -0.04370 0.01470  422 TYR A CA    
3342 C  C     . TYR A 422 ? 0.80420 1.42940 1.10370 -0.24470 -0.04090 0.00640  422 TYR A C     
3343 O  O     . TYR A 422 ? 0.91000 1.54910 1.20290 -0.26150 -0.05880 0.00890  422 TYR A O     
3344 C  CB    . TYR A 422 ? 0.72710 1.25180 0.96570 -0.21230 -0.03490 0.01580  422 TYR A CB    
3345 C  CG    . TYR A 422 ? 0.71910 1.20680 0.94240 -0.18600 -0.04070 0.02530  422 TYR A CG    
3346 C  CD1   . TYR A 422 ? 0.75600 1.26180 1.00130 -0.16560 -0.05740 0.03550  422 TYR A CD1   
3347 C  CD2   . TYR A 422 ? 0.72000 1.15470 0.90670 -0.18300 -0.02990 0.02520  422 TYR A CD2   
3348 C  CE1   . TYR A 422 ? 0.82680 1.29620 1.05540 -0.14510 -0.06090 0.04490  422 TYR A CE1   
3349 C  CE2   . TYR A 422 ? 0.82580 1.23000 1.00100 -0.16220 -0.03390 0.03350  422 TYR A CE2   
3350 C  CZ    . TYR A 422 ? 0.82830 1.24890 1.02340 -0.14440 -0.04820 0.04310  422 TYR A CZ    
3351 O  OH    . TYR A 422 ? 0.63350 1.02210 0.81520 -0.12710 -0.05050 0.05200  422 TYR A OH    
3352 N  N     . ILE A 423 ? 0.73610 1.37090 1.04370 -0.25790 -0.01830 -0.00380 423 ILE A N     
3353 C  CA    . ILE A 423 ? 0.82530 1.48410 1.13270 -0.29470 -0.01240 -0.01150 423 ILE A CA    
3354 C  C     . ILE A 423 ? 0.86040 1.59130 1.22550 -0.29550 -0.02380 -0.01300 423 ILE A C     
3355 O  O     . ILE A 423 ? 0.88540 1.62070 1.24010 -0.31800 -0.03300 -0.01450 423 ILE A O     
3356 C  CB    . ILE A 423 ? 0.81110 1.45840 1.10830 -0.30780 0.01630  -0.02060 423 ILE A CB    
3357 C  CG1   . ILE A 423 ? 0.72410 1.29050 0.95390 -0.31150 0.02210  -0.01730 423 ILE A CG1   
3358 C  CG2   . ILE A 423 ? 0.83170 1.50000 1.13400 -0.33500 0.02480  -0.02790 423 ILE A CG2   
3359 C  CD1   . ILE A 423 ? 0.73790 1.28510 0.95020 -0.31990 0.04710  -0.02340 423 ILE A CD1   
3360 N  N     . SER A 424 ? 0.76710 1.54550 1.18990 -0.26620 -0.02470 -0.01210 424 SER A N     
3361 C  CA    . SER A 424 ? 0.71480 1.55350 1.19370 -0.25790 -0.03870 -0.01140 424 SER A CA    
3362 C  C     . SER A 424 ? 0.76070 1.59760 1.22450 -0.26130 -0.07140 -0.00050 424 SER A C     
3363 O  O     . SER A 424 ? 0.90070 1.76290 1.37510 -0.27740 -0.08420 -0.00170 424 SER A O     
3364 C  CB    . SER A 424 ? 0.71860 1.59980 1.26000 -0.22100 -0.03440 -0.01140 424 SER A CB    
3365 O  OG    . SER A 424 ? 0.83130 1.71480 1.38410 -0.21970 -0.00210 -0.02420 424 SER A OG    
3366 N  N     . GLU A 425 ? 0.81760 1.62330 1.25330 -0.24800 -0.08480 0.01020  425 GLU A N     
3367 C  CA    . GLU A 425 ? 0.83420 1.63130 1.24520 -0.25190 -0.11470 0.02080  425 GLU A CA    
3368 C  C     . GLU A 425 ? 0.88410 1.64980 1.24400 -0.28910 -0.11660 0.01450  425 GLU A C     
3369 O  O     . GLU A 425 ? 0.92470 1.70660 1.28260 -0.30100 -0.13700 0.01630  425 GLU A O     
3370 C  CB    . GLU A 425 ? 0.93920 1.67370 1.30690 -0.22870 -0.11790 0.03100  425 GLU A CB    
3371 C  CG    . GLU A 425 ? 0.99390 1.73790 1.39790 -0.18840 -0.12070 0.03990  425 GLU A CG    
3372 C  CD    . GLU A 425 ? 1.10120 1.78120 1.45770 -0.17070 -0.12480 0.05080  425 GLU A CD    
3373 O  OE1   . GLU A 425 ? 0.99510 1.62910 1.29430 -0.18810 -0.12600 0.05100  425 GLU A OE1   
3374 O  OE2   . GLU A 425 ? 1.23370 1.90840 1.61100 -0.13990 -0.12510 0.05840  425 GLU A OE2   
3375 N  N     . ILE A 426 ? 0.92660 1.64540 1.24420 -0.30760 -0.09580 0.00710  426 ILE A N     
3376 C  CA    . ILE A 426 ? 0.94310 1.62200 1.20750 -0.34100 -0.09690 0.00150  426 ILE A CA    
3377 C  C     . ILE A 426 ? 0.88920 1.60220 1.17670 -0.36180 -0.09440 -0.00630 426 ILE A C     
3378 O  O     . ILE A 426 ? 0.90910 1.61400 1.17180 -0.38470 -0.10770 -0.00830 426 ILE A O     
3379 C  CB    . ILE A 426 ? 0.86140 1.47800 1.07660 -0.35240 -0.07630 -0.00280 426 ILE A CB    
3380 C  CG1   . ILE A 426 ? 0.83690 1.40240 1.02080 -0.32430 -0.07810 0.00520  426 ILE A CG1   
3381 C  CG2   . ILE A 426 ? 0.75990 1.33110 0.92150 -0.38500 -0.07630 -0.00890 426 ILE A CG2   
3382 C  CD1   . ILE A 426 ? 0.78230 1.29260 0.93530 -0.31820 -0.05590 0.00310  426 ILE A CD1   
3383 N  N     . LYS A 427 ? 0.85110 1.60280 1.18570 -0.35530 -0.07660 -0.01140 427 LYS A N     
3384 C  CA    . LYS A 427 ? 0.81460 1.60500 1.17730 -0.37510 -0.07360 -0.01830 427 LYS A CA    
3385 C  C     . LYS A 427 ? 0.90920 1.75190 1.31220 -0.36870 -0.10140 -0.01360 427 LYS A C     
3386 O  O     . LYS A 427 ? 1.00760 1.86610 1.41060 -0.39320 -0.11050 -0.01730 427 LYS A O     
3387 C  CB    . LYS A 427 ? 0.72460 1.54750 1.13110 -0.36670 -0.04730 -0.02500 427 LYS A CB    
3388 C  CG    . LYS A 427 ? 0.75070 1.52340 1.11120 -0.38440 -0.02020 -0.03080 427 LYS A CG    
3389 C  CD    . LYS A 427 ? 0.75820 1.56450 1.15830 -0.37770 0.00630  -0.03820 427 LYS A CD    
3390 C  CE    . LYS A 427 ? 0.73210 1.48360 1.08090 -0.39100 0.03120  -0.04180 427 LYS A CE    
3391 N  NZ    . LYS A 427 ? 0.68310 1.39700 0.98270 -0.42760 0.03500  -0.04370 427 LYS A NZ    
3392 N  N     . GLN A 428 ? 0.87600 1.74390 1.31180 -0.33610 -0.11660 -0.00460 428 GLN A N     
3393 C  CA    . GLN A 428 ? 0.93910 1.84740 1.40360 -0.32870 -0.14750 0.00260  428 GLN A CA    
3394 C  C     . GLN A 428 ? 1.02800 1.89670 1.43000 -0.35250 -0.16740 0.00510  428 GLN A C     
3395 O  O     . GLN A 428 ? 1.05950 1.95460 1.47010 -0.36580 -0.18810 0.00540  428 GLN A O     
3396 C  CB    . GLN A 428 ? 0.88110 1.81330 1.38410 -0.28830 -0.16100 0.01400  428 GLN A CB    
3397 C  CG    . GLN A 428 ? 0.88600 1.85960 1.45520 -0.26330 -0.14100 0.00950  428 GLN A CG    
3398 C  CD    . GLN A 428 ? 0.91520 1.93880 1.53250 -0.27860 -0.13010 -0.00130 428 GLN A CD    
3399 O  OE1   . GLN A 428 ? 0.94340 1.96850 1.57000 -0.28550 -0.09990 -0.01170 428 GLN A OE1   
3400 N  NE2   . GLN A 428 ? 0.83040 1.89530 1.47690 -0.28480 -0.15480 0.00150  428 GLN A NE2   
3401 N  N     . GLU A 429 ? 1.04440 1.84960 1.38340 -0.35740 -0.16180 0.00630  429 GLU A N     
3402 C  CA    . GLU A 429 ? 1.09390 1.85780 1.37120 -0.37840 -0.17860 0.00690  429 GLU A CA    
3403 C  C     . GLU A 429 ? 1.15550 1.90210 1.40520 -0.41610 -0.17130 -0.00460 429 GLU A C     
3404 O  O     . GLU A 429 ? 1.19040 1.91800 1.40160 -0.43600 -0.18780 -0.00620 429 GLU A O     
3405 C  CB    . GLU A 429 ? 1.09490 1.79510 1.31450 -0.37380 -0.17260 0.00970  429 GLU A CB    
3406 C  CG    . GLU A 429 ? 1.17790 1.88620 1.41310 -0.34000 -0.18200 0.02270  429 GLU A CG    
3407 C  CD    . GLU A 429 ? 1.08410 1.73260 1.26690 -0.33760 -0.17300 0.02420  429 GLU A CD    
3408 O  OE1   . GLU A 429 ? 1.09500 1.69270 1.22010 -0.36130 -0.16920 0.01650  429 GLU A OE1   
3409 O  OE2   . GLU A 429 ? 1.01090 1.65030 1.20680 -0.30590 -0.16640 0.03240  429 GLU A OE2   
3410 N  N     . ILE A 430 ? 1.09370 1.84410 1.35900 -0.42680 -0.14660 -0.01250 430 ILE A N     
3411 C  CA    . ILE A 430 ? 1.08350 1.82300 1.32860 -0.46270 -0.14020 -0.02180 430 ILE A CA    
3412 C  C     . ILE A 430 ? 1.28590 2.09400 1.58500 -0.47070 -0.15530 -0.02290 430 ILE A C     
3413 O  O     . ILE A 430 ? 1.34130 2.14420 1.61790 -0.49830 -0.16750 -0.02700 430 ILE A O     
3414 C  CB    . ILE A 430 ? 0.98490 1.69860 1.21980 -0.47290 -0.10890 -0.02810 430 ILE A CB    
3415 C  CG1   . ILE A 430 ? 0.86650 1.50790 1.04400 -0.46780 -0.09790 -0.02680 430 ILE A CG1   
3416 C  CG2   . ILE A 430 ? 1.07940 1.78230 1.29430 -0.51010 -0.10270 -0.03600 430 ILE A CG2   
3417 C  CD1   . ILE A 430 ? 0.76480 1.38100 0.93390 -0.47060 -0.06950 -0.03000 430 ILE A CD1   
3418 N  N     . GLU A 431 ? 1.28880 2.16160 1.66100 -0.44660 -0.15460 -0.01990 431 GLU A N     
3419 C  CA    . GLU A 431 ? 1.27960 2.22380 1.71360 -0.45100 -0.16890 -0.02100 431 GLU A CA    
3420 C  C     . GLU A 431 ? 1.33440 2.30280 1.77670 -0.44260 -0.20550 -0.01290 431 GLU A C     
3421 O  O     . GLU A 431 ? 1.38070 2.39200 1.85150 -0.45840 -0.22200 -0.01500 431 GLU A O     
3422 C  CB    . GLU A 431 ? 1.20080 2.20580 1.71350 -0.42870 -0.15340 -0.02240 431 GLU A CB    
3423 C  CG    . GLU A 431 ? 1.27610 2.25630 1.77740 -0.43330 -0.11760 -0.02930 431 GLU A CG    
3424 C  CD    . GLU A 431 ? 1.39460 2.35430 1.86280 -0.47520 -0.10520 -0.03770 431 GLU A CD    
3425 O  OE1   . GLU A 431 ? 1.38010 2.38550 1.88120 -0.49340 -0.11610 -0.04060 431 GLU A OE1   
3426 O  OE2   . GLU A 431 ? 1.46520 2.36340 1.87540 -0.49020 -0.08610 -0.04070 431 GLU A OE2   
3427 N  N     . SER A 432 ? 1.36690 2.30980 1.78440 -0.41930 -0.21940 -0.00320 432 SER A N     
3428 C  CA    . SER A 432 ? 1.41820 2.38390 1.84200 -0.40900 -0.25470 0.00650  432 SER A CA    
3429 C  C     . SER A 432 ? 1.61930 2.56250 1.99240 -0.44460 -0.27130 0.00180  432 SER A C     
3430 O  O     . SER A 432 ? 1.58340 2.57340 1.98900 -0.45650 -0.29070 0.00070  432 SER A O     
3431 C  CB    . SER A 432 ? 1.40180 2.33360 1.79610 -0.38080 -0.26310 0.01860  432 SER A CB    
3432 O  OG    . SER A 432 ? 1.47880 2.33750 1.79570 -0.39600 -0.25100 0.01520  432 SER A OG    
3433 N  N     . SAH B .   ? 0.97430 1.01800 0.93540 -0.16750 -0.14950 0.07090  501 SAH A N     
3434 C  CA    . SAH B .   ? 0.94180 0.99700 0.92920 -0.16640 -0.13230 0.06100  501 SAH A CA    
3435 C  CB    . SAH B .   ? 0.77100 0.81750 0.74620 -0.16320 -0.10850 0.05340  501 SAH A CB    
3436 C  CG    . SAH B .   ? 0.89080 0.94770 0.88860 -0.14780 -0.09810 0.06040  501 SAH A CG    
3437 S  SD    . SAH B .   ? 0.89300 0.97390 0.94070 -0.13690 -0.08990 0.06230  501 SAH A SD    
3438 C  C     . SAH B .   ? 1.02240 1.07250 1.00050 -0.18230 -0.13790 0.05040  501 SAH A C     
3439 O  O     . SAH B .   ? 1.05220 1.09340 1.00460 -0.19490 -0.15640 0.05060  501 SAH A O     
3440 O  OXT   . SAH B .   ? 1.03580 1.08760 1.02980 -0.18350 -0.12510 0.04160  501 SAH A OXT   
3441 C  "C5'" . SAH B .   ? 0.95390 1.04540 1.02070 -0.12290 -0.09910 0.07570  501 SAH A "C5'" 
3442 C  "C4'" . SAH B .   ? 0.84750 0.94670 0.92460 -0.12340 -0.12130 0.08320  501 SAH A "C4'" 
3443 O  "O4'" . SAH B .   ? 0.80040 0.87830 0.83930 -0.13050 -0.13490 0.08540  501 SAH A "O4'" 
3444 C  "C3'" . SAH B .   ? 0.85220 0.96630 0.95970 -0.10660 -0.12450 0.09260  501 SAH A "C3'" 
3445 O  "O3'" . SAH B .   ? 0.80380 0.94600 0.95410 -0.10260 -0.11820 0.09300  501 SAH A "O3'" 
3446 C  "C2'" . SAH B .   ? 0.84050 0.95080 0.94110 -0.10620 -0.14950 0.10110  501 SAH A "C2'" 
3447 O  "O2'" . SAH B .   ? 0.78200 0.91660 0.91040 -0.11240 -0.16420 0.10250  501 SAH A "O2'" 
3448 C  "C1'" . SAH B .   ? 0.76750 0.84790 0.81520 -0.12110 -0.15350 0.09740  501 SAH A "C1'" 
3449 N  N9    . SAH B .   ? 0.79450 0.84840 0.81130 -0.11580 -0.15140 0.10240  501 SAH A N9    
3450 C  C8    . SAH B .   ? 0.78540 0.82390 0.78050 -0.11810 -0.13190 0.09640  501 SAH A C8    
3451 N  N7    . SAH B .   ? 0.80590 0.81890 0.77440 -0.11520 -0.13630 0.10370  501 SAH A N7    
3452 C  C5    . SAH B .   ? 0.79810 0.80770 0.77030 -0.10850 -0.15920 0.11520  501 SAH A C5    
3453 C  C6    . SAH B .   ? 0.87730 0.85980 0.82800 -0.10210 -0.17370 0.12750  501 SAH A C6    
3454 N  N6    . SAH B .   ? 0.96950 0.92080 0.88730 -0.10470 -0.16370 0.12840  501 SAH A N6    
3455 N  N1    . SAH B .   ? 0.89790 0.88560 0.86270 -0.09330 -0.19990 0.13950  501 SAH A N1    
3456 C  C2    . SAH B .   ? 0.96380 0.98690 0.96470 -0.09370 -0.21080 0.13810  501 SAH A C2    
3457 N  N3    . SAH B .   ? 0.81910 0.86610 0.83850 -0.10280 -0.19460 0.12510  501 SAH A N3    
3458 C  C4    . SAH B .   ? 0.78480 0.82350 0.78950 -0.10880 -0.16940 0.11440  501 SAH A C4    
3459 ZN ZN    . ZN  C .   ? 1.15500 0.98390 1.19430 0.07200  -0.19360 0.38150  502 ZN  A ZN    
3460 ZN ZN    . ZN  D .   ? 1.05380 0.86170 0.92890 -0.05770 -0.13690 0.14010  503 ZN  A ZN    
3461 ZN ZN    . ZN  E .   ? 0.71500 1.10420 1.18840 0.13200  -0.12960 0.14070  504 ZN  A ZN    
# 
