data_8XZC
# 
_entry.id   8XZC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8XZC         pdb_00008xzc 10.2210/pdb8xzc/pdb 
WWPDB D_1300043832 ?            ?                   
# 
_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       2025-01-22 
# 
_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                        8XZC 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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          7YH4 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ravimakde@rrcat.gov.in 
_pdbx_contact_author.name_first         Ravindra 
_pdbx_contact_author.name_last          Makde 
_pdbx_contact_author.name_mi            D. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7020-0065 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chandravanshi, K.' 1 ? 
'Kumar, A.'         2 ? 
'Makde, R.D.'       3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of human cytosolic beta-alanyl lysine dipeptidase (PM20D2) Tyr314Phe mutant' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chandravanshi, K.' 1 ? 
primary 'Kumar, A.'         2 ? 
primary 'Makde, R.D.'       3 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Xaa-Arg dipeptidase' 49732.809 1  3.4.13.4 Y314F ? 'Human cytosolic beta-alanyl lysine dipeptidase (PM20D2)' 
2 non-polymer syn 'PHOSPHATE ION'       94.971    2  ?        ?     ? ?                                                         
3 non-polymer syn 'ZINC ION'            65.409    2  ?        ?     ? ?                                                         
4 water       nat water                 18.015    84 ?        ?     ? ?                                                         
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Beta-Ala-Lys dipeptidase' 
# 
_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       
;MASWSHPQFEGGSSHHHHHHSSGSGGGGGENLYFQGSLELLKLRSAECIDEAAERLGALSRAIWSQPELAYEEHHAHRVL
THFFEREPPAASWAVQPHYQLPTAFRAEWEPPEARAPSATPRPLHLGFLCEYDALPGIGHACGHNLIAEVGAAAALGVRG
ALEGLPRPPPPVKVVVLGTPAEEDGGGKIDLIEAGAFTNLDVVFMAHPSQENAAYLPDMAEHDVTVKYYGKASHSASYPW
EGLNALDAAVLAYNNLSVFRQQMKPTWRVHGIIKNGGVKPNIIPSYSELIYYFRAPSMKELQVLTKKAEDCFRAAALASG
CTVEIKGGAHDFYNVLPNKSLWKAYMENGRKLGIEFISEDTMLNGPSGSTDFGNVSFVVPGIHPYFHIGSNALNHTEQYT
EAAGSQEAQFYTLRTAKALAMTALDVIFKPELLEGIREDFKLKLQEEQFVNAVE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MASWSHPQFEGGSSHHHHHHSSGSGGGGGENLYFQGSLELLKLRSAECIDEAAERLGALSRAIWSQPELAYEEHHAHRVL
THFFEREPPAASWAVQPHYQLPTAFRAEWEPPEARAPSATPRPLHLGFLCEYDALPGIGHACGHNLIAEVGAAAALGVRG
ALEGLPRPPPPVKVVVLGTPAEEDGGGKIDLIEAGAFTNLDVVFMAHPSQENAAYLPDMAEHDVTVKYYGKASHSASYPW
EGLNALDAAVLAYNNLSVFRQQMKPTWRVHGIIKNGGVKPNIIPSYSELIYYFRAPSMKELQVLTKKAEDCFRAAALASG
CTVEIKGGAHDFYNVLPNKSLWKAYMENGRKLGIEFISEDTMLNGPSGSTDFGNVSFVVPGIHPYFHIGSNALNHTEQYT
EAAGSQEAQFYTLRTAKALAMTALDVIFKPELLEGIREDFKLKLQEEQFVNAVE
;
_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 'PHOSPHATE ION' PO4 
3 'ZINC ION'      ZN  
4 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   SER n 
1 4   TRP n 
1 5   SER n 
1 6   HIS n 
1 7   PRO n 
1 8   GLN n 
1 9   PHE n 
1 10  GLU n 
1 11  GLY n 
1 12  GLY n 
1 13  SER n 
1 14  SER n 
1 15  HIS n 
1 16  HIS n 
1 17  HIS n 
1 18  HIS n 
1 19  HIS n 
1 20  HIS n 
1 21  SER n 
1 22  SER n 
1 23  GLY n 
1 24  SER n 
1 25  GLY n 
1 26  GLY n 
1 27  GLY n 
1 28  GLY n 
1 29  GLY n 
1 30  GLU n 
1 31  ASN n 
1 32  LEU n 
1 33  TYR n 
1 34  PHE n 
1 35  GLN n 
1 36  GLY n 
1 37  SER n 
1 38  LEU n 
1 39  GLU n 
1 40  LEU n 
1 41  LEU n 
1 42  LYS n 
1 43  LEU n 
1 44  ARG n 
1 45  SER n 
1 46  ALA n 
1 47  GLU n 
1 48  CYS n 
1 49  ILE n 
1 50  ASP n 
1 51  GLU n 
1 52  ALA n 
1 53  ALA n 
1 54  GLU n 
1 55  ARG n 
1 56  LEU n 
1 57  GLY n 
1 58  ALA n 
1 59  LEU n 
1 60  SER n 
1 61  ARG n 
1 62  ALA n 
1 63  ILE n 
1 64  TRP n 
1 65  SER n 
1 66  GLN n 
1 67  PRO n 
1 68  GLU n 
1 69  LEU n 
1 70  ALA n 
1 71  TYR n 
1 72  GLU n 
1 73  GLU n 
1 74  HIS n 
1 75  HIS n 
1 76  ALA n 
1 77  HIS n 
1 78  ARG n 
1 79  VAL n 
1 80  LEU n 
1 81  THR n 
1 82  HIS n 
1 83  PHE n 
1 84  PHE n 
1 85  GLU n 
1 86  ARG n 
1 87  GLU n 
1 88  PRO n 
1 89  PRO n 
1 90  ALA n 
1 91  ALA n 
1 92  SER n 
1 93  TRP n 
1 94  ALA n 
1 95  VAL n 
1 96  GLN n 
1 97  PRO n 
1 98  HIS n 
1 99  TYR n 
1 100 GLN n 
1 101 LEU n 
1 102 PRO n 
1 103 THR n 
1 104 ALA n 
1 105 PHE n 
1 106 ARG n 
1 107 ALA n 
1 108 GLU n 
1 109 TRP n 
1 110 GLU n 
1 111 PRO n 
1 112 PRO n 
1 113 GLU n 
1 114 ALA n 
1 115 ARG n 
1 116 ALA n 
1 117 PRO n 
1 118 SER n 
1 119 ALA n 
1 120 THR n 
1 121 PRO n 
1 122 ARG n 
1 123 PRO n 
1 124 LEU n 
1 125 HIS n 
1 126 LEU n 
1 127 GLY n 
1 128 PHE n 
1 129 LEU n 
1 130 CYS n 
1 131 GLU n 
1 132 TYR n 
1 133 ASP n 
1 134 ALA n 
1 135 LEU n 
1 136 PRO n 
1 137 GLY n 
1 138 ILE n 
1 139 GLY n 
1 140 HIS n 
1 141 ALA n 
1 142 CYS n 
1 143 GLY n 
1 144 HIS n 
1 145 ASN n 
1 146 LEU n 
1 147 ILE n 
1 148 ALA n 
1 149 GLU n 
1 150 VAL n 
1 151 GLY n 
1 152 ALA n 
1 153 ALA n 
1 154 ALA n 
1 155 ALA n 
1 156 LEU n 
1 157 GLY n 
1 158 VAL n 
1 159 ARG n 
1 160 GLY n 
1 161 ALA n 
1 162 LEU n 
1 163 GLU n 
1 164 GLY n 
1 165 LEU n 
1 166 PRO n 
1 167 ARG n 
1 168 PRO n 
1 169 PRO n 
1 170 PRO n 
1 171 PRO n 
1 172 VAL n 
1 173 LYS n 
1 174 VAL n 
1 175 VAL n 
1 176 VAL n 
1 177 LEU n 
1 178 GLY n 
1 179 THR n 
1 180 PRO n 
1 181 ALA n 
1 182 GLU n 
1 183 GLU n 
1 184 ASP n 
1 185 GLY n 
1 186 GLY n 
1 187 GLY n 
1 188 LYS n 
1 189 ILE n 
1 190 ASP n 
1 191 LEU n 
1 192 ILE n 
1 193 GLU n 
1 194 ALA n 
1 195 GLY n 
1 196 ALA n 
1 197 PHE n 
1 198 THR n 
1 199 ASN n 
1 200 LEU n 
1 201 ASP n 
1 202 VAL n 
1 203 VAL n 
1 204 PHE n 
1 205 MET n 
1 206 ALA n 
1 207 HIS n 
1 208 PRO n 
1 209 SER n 
1 210 GLN n 
1 211 GLU n 
1 212 ASN n 
1 213 ALA n 
1 214 ALA n 
1 215 TYR n 
1 216 LEU n 
1 217 PRO n 
1 218 ASP n 
1 219 MET n 
1 220 ALA n 
1 221 GLU n 
1 222 HIS n 
1 223 ASP n 
1 224 VAL n 
1 225 THR n 
1 226 VAL n 
1 227 LYS n 
1 228 TYR n 
1 229 TYR n 
1 230 GLY n 
1 231 LYS n 
1 232 ALA n 
1 233 SER n 
1 234 HIS n 
1 235 SER n 
1 236 ALA n 
1 237 SER n 
1 238 TYR n 
1 239 PRO n 
1 240 TRP n 
1 241 GLU n 
1 242 GLY n 
1 243 LEU n 
1 244 ASN n 
1 245 ALA n 
1 246 LEU n 
1 247 ASP n 
1 248 ALA n 
1 249 ALA n 
1 250 VAL n 
1 251 LEU n 
1 252 ALA n 
1 253 TYR n 
1 254 ASN n 
1 255 ASN n 
1 256 LEU n 
1 257 SER n 
1 258 VAL n 
1 259 PHE n 
1 260 ARG n 
1 261 GLN n 
1 262 GLN n 
1 263 MET n 
1 264 LYS n 
1 265 PRO n 
1 266 THR n 
1 267 TRP n 
1 268 ARG n 
1 269 VAL n 
1 270 HIS n 
1 271 GLY n 
1 272 ILE n 
1 273 ILE n 
1 274 LYS n 
1 275 ASN n 
1 276 GLY n 
1 277 GLY n 
1 278 VAL n 
1 279 LYS n 
1 280 PRO n 
1 281 ASN n 
1 282 ILE n 
1 283 ILE n 
1 284 PRO n 
1 285 SER n 
1 286 TYR n 
1 287 SER n 
1 288 GLU n 
1 289 LEU n 
1 290 ILE n 
1 291 TYR n 
1 292 TYR n 
1 293 PHE n 
1 294 ARG n 
1 295 ALA n 
1 296 PRO n 
1 297 SER n 
1 298 MET n 
1 299 LYS n 
1 300 GLU n 
1 301 LEU n 
1 302 GLN n 
1 303 VAL n 
1 304 LEU n 
1 305 THR n 
1 306 LYS n 
1 307 LYS n 
1 308 ALA n 
1 309 GLU n 
1 310 ASP n 
1 311 CYS n 
1 312 PHE n 
1 313 ARG n 
1 314 ALA n 
1 315 ALA n 
1 316 ALA n 
1 317 LEU n 
1 318 ALA n 
1 319 SER n 
1 320 GLY n 
1 321 CYS n 
1 322 THR n 
1 323 VAL n 
1 324 GLU n 
1 325 ILE n 
1 326 LYS n 
1 327 GLY n 
1 328 GLY n 
1 329 ALA n 
1 330 HIS n 
1 331 ASP n 
1 332 PHE n 
1 333 TYR n 
1 334 ASN n 
1 335 VAL n 
1 336 LEU n 
1 337 PRO n 
1 338 ASN n 
1 339 LYS n 
1 340 SER n 
1 341 LEU n 
1 342 TRP n 
1 343 LYS n 
1 344 ALA n 
1 345 TYR n 
1 346 MET n 
1 347 GLU n 
1 348 ASN n 
1 349 GLY n 
1 350 ARG n 
1 351 LYS n 
1 352 LEU n 
1 353 GLY n 
1 354 ILE n 
1 355 GLU n 
1 356 PHE n 
1 357 ILE n 
1 358 SER n 
1 359 GLU n 
1 360 ASP n 
1 361 THR n 
1 362 MET n 
1 363 LEU n 
1 364 ASN n 
1 365 GLY n 
1 366 PRO n 
1 367 SER n 
1 368 GLY n 
1 369 SER n 
1 370 THR n 
1 371 ASP n 
1 372 PHE n 
1 373 GLY n 
1 374 ASN n 
1 375 VAL n 
1 376 SER n 
1 377 PHE n 
1 378 VAL n 
1 379 VAL n 
1 380 PRO n 
1 381 GLY n 
1 382 ILE n 
1 383 HIS n 
1 384 PRO n 
1 385 TYR n 
1 386 PHE n 
1 387 HIS n 
1 388 ILE n 
1 389 GLY n 
1 390 SER n 
1 391 ASN n 
1 392 ALA n 
1 393 LEU n 
1 394 ASN n 
1 395 HIS n 
1 396 THR n 
1 397 GLU n 
1 398 GLN n 
1 399 TYR n 
1 400 THR n 
1 401 GLU n 
1 402 ALA n 
1 403 ALA n 
1 404 GLY n 
1 405 SER n 
1 406 GLN n 
1 407 GLU n 
1 408 ALA n 
1 409 GLN n 
1 410 PHE n 
1 411 TYR n 
1 412 THR n 
1 413 LEU n 
1 414 ARG n 
1 415 THR n 
1 416 ALA n 
1 417 LYS n 
1 418 ALA n 
1 419 LEU n 
1 420 ALA n 
1 421 MET n 
1 422 THR n 
1 423 ALA n 
1 424 LEU n 
1 425 ASP n 
1 426 VAL n 
1 427 ILE n 
1 428 PHE n 
1 429 LYS n 
1 430 PRO n 
1 431 GLU n 
1 432 LEU n 
1 433 LEU n 
1 434 GLU n 
1 435 GLY n 
1 436 ILE n 
1 437 ARG n 
1 438 GLU n 
1 439 ASP n 
1 440 PHE n 
1 441 LYS n 
1 442 LEU n 
1 443 LYS n 
1 444 LEU n 
1 445 GLN n 
1 446 GLU n 
1 447 GLU n 
1 448 GLN n 
1 449 PHE n 
1 450 VAL n 
1 451 ASN n 
1 452 ALA n 
1 453 VAL n 
1 454 GLU 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                   454 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PM20D2, ACY1L2' 
_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                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION' ? 'O4 P -3'        94.971  
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
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   -17 ?   ?   ?   A . n 
A 1 2   ALA 2   -16 ?   ?   ?   A . n 
A 1 3   SER 3   -15 ?   ?   ?   A . n 
A 1 4   TRP 4   -14 ?   ?   ?   A . n 
A 1 5   SER 5   -13 ?   ?   ?   A . n 
A 1 6   HIS 6   -12 ?   ?   ?   A . n 
A 1 7   PRO 7   -11 ?   ?   ?   A . n 
A 1 8   GLN 8   -10 ?   ?   ?   A . n 
A 1 9   PHE 9   -9  ?   ?   ?   A . n 
A 1 10  GLU 10  -8  ?   ?   ?   A . n 
A 1 11  GLY 11  -7  ?   ?   ?   A . n 
A 1 12  GLY 12  -6  ?   ?   ?   A . n 
A 1 13  SER 13  -5  ?   ?   ?   A . n 
A 1 14  SER 14  -4  ?   ?   ?   A . n 
A 1 15  HIS 15  -3  ?   ?   ?   A . n 
A 1 16  HIS 16  -2  ?   ?   ?   A . n 
A 1 17  HIS 17  -1  ?   ?   ?   A . n 
A 1 18  HIS 18  0   ?   ?   ?   A . n 
A 1 19  HIS 19  1   ?   ?   ?   A . n 
A 1 20  HIS 20  2   ?   ?   ?   A . n 
A 1 21  SER 21  3   ?   ?   ?   A . n 
A 1 22  SER 22  4   ?   ?   ?   A . n 
A 1 23  GLY 23  5   ?   ?   ?   A . n 
A 1 24  SER 24  6   ?   ?   ?   A . n 
A 1 25  GLY 25  7   ?   ?   ?   A . n 
A 1 26  GLY 26  8   ?   ?   ?   A . n 
A 1 27  GLY 27  9   ?   ?   ?   A . n 
A 1 28  GLY 28  10  ?   ?   ?   A . n 
A 1 29  GLY 29  11  ?   ?   ?   A . n 
A 1 30  GLU 30  12  ?   ?   ?   A . n 
A 1 31  ASN 31  13  ?   ?   ?   A . n 
A 1 32  LEU 32  14  14  LEU LEU A . n 
A 1 33  TYR 33  15  15  TYR TYR A . n 
A 1 34  PHE 34  16  16  PHE PHE A . n 
A 1 35  GLN 35  17  17  GLN GLN A . n 
A 1 36  GLY 36  18  18  GLY GLY A . n 
A 1 37  SER 37  19  19  SER SER A . n 
A 1 38  LEU 38  20  20  LEU LEU A . n 
A 1 39  GLU 39  21  21  GLU GLU A . n 
A 1 40  LEU 40  22  22  LEU LEU A . n 
A 1 41  LEU 41  23  23  LEU LEU A . n 
A 1 42  LYS 42  24  24  LYS LYS A . n 
A 1 43  LEU 43  25  25  LEU LEU A . n 
A 1 44  ARG 44  26  26  ARG ARG A . n 
A 1 45  SER 45  27  27  SER SER A . n 
A 1 46  ALA 46  28  28  ALA ALA A . n 
A 1 47  GLU 47  29  29  GLU GLU A . n 
A 1 48  CYS 48  30  30  CYS CYS A . n 
A 1 49  ILE 49  31  31  ILE ILE A . n 
A 1 50  ASP 50  32  32  ASP ASP A . n 
A 1 51  GLU 51  33  33  GLU GLU A . n 
A 1 52  ALA 52  34  34  ALA ALA A . n 
A 1 53  ALA 53  35  35  ALA ALA A . n 
A 1 54  GLU 54  36  36  GLU GLU A . n 
A 1 55  ARG 55  37  37  ARG ARG A . n 
A 1 56  LEU 56  38  38  LEU LEU A . n 
A 1 57  GLY 57  39  39  GLY GLY A . n 
A 1 58  ALA 58  40  40  ALA ALA A . n 
A 1 59  LEU 59  41  41  LEU LEU A . n 
A 1 60  SER 60  42  42  SER SER A . n 
A 1 61  ARG 61  43  43  ARG ARG A . n 
A 1 62  ALA 62  44  44  ALA ALA A . n 
A 1 63  ILE 63  45  45  ILE ILE A . n 
A 1 64  TRP 64  46  46  TRP TRP A . n 
A 1 65  SER 65  47  47  SER SER A . n 
A 1 66  GLN 66  48  48  GLN GLN A . n 
A 1 67  PRO 67  49  49  PRO PRO A . n 
A 1 68  GLU 68  50  50  GLU GLU A . n 
A 1 69  LEU 69  51  51  LEU LEU A . n 
A 1 70  ALA 70  52  52  ALA ALA A . n 
A 1 71  TYR 71  53  53  TYR TYR A . n 
A 1 72  GLU 72  54  54  GLU GLU A . n 
A 1 73  GLU 73  55  55  GLU GLU A . n 
A 1 74  HIS 74  56  56  HIS HIS A . n 
A 1 75  HIS 75  57  57  HIS HIS A . n 
A 1 76  ALA 76  58  58  ALA ALA A . n 
A 1 77  HIS 77  59  59  HIS HIS A . n 
A 1 78  ARG 78  60  60  ARG ARG A . n 
A 1 79  VAL 79  61  61  VAL VAL A . n 
A 1 80  LEU 80  62  62  LEU LEU A . n 
A 1 81  THR 81  63  63  THR THR A . n 
A 1 82  HIS 82  64  64  HIS HIS A . n 
A 1 83  PHE 83  65  65  PHE PHE A . n 
A 1 84  PHE 84  66  66  PHE PHE A . n 
A 1 85  GLU 85  67  67  GLU GLU A . n 
A 1 86  ARG 86  68  68  ARG ARG A . n 
A 1 87  GLU 87  69  69  GLU GLU A . n 
A 1 88  PRO 88  70  70  PRO PRO A . n 
A 1 89  PRO 89  71  71  PRO PRO A . n 
A 1 90  ALA 90  72  72  ALA ALA A . n 
A 1 91  ALA 91  73  73  ALA ALA A . n 
A 1 92  SER 92  74  74  SER SER A . n 
A 1 93  TRP 93  75  75  TRP TRP A . n 
A 1 94  ALA 94  76  76  ALA ALA A . n 
A 1 95  VAL 95  77  77  VAL VAL A . n 
A 1 96  GLN 96  78  78  GLN GLN A . n 
A 1 97  PRO 97  79  79  PRO PRO A . n 
A 1 98  HIS 98  80  80  HIS HIS A . n 
A 1 99  TYR 99  81  81  TYR TYR A . n 
A 1 100 GLN 100 82  82  GLN GLN A . n 
A 1 101 LEU 101 83  83  LEU LEU A . n 
A 1 102 PRO 102 84  84  PRO PRO A . n 
A 1 103 THR 103 85  85  THR THR A . n 
A 1 104 ALA 104 86  86  ALA ALA A . n 
A 1 105 PHE 105 87  87  PHE PHE A . n 
A 1 106 ARG 106 88  88  ARG ARG A . n 
A 1 107 ALA 107 89  89  ALA ALA A . n 
A 1 108 GLU 108 90  90  GLU GLU A . n 
A 1 109 TRP 109 91  91  TRP TRP A . n 
A 1 110 GLU 110 92  92  GLU GLU A . n 
A 1 111 PRO 111 93  93  PRO PRO A . n 
A 1 112 PRO 112 94  94  PRO PRO A . n 
A 1 113 GLU 113 95  95  GLU GLU A . n 
A 1 114 ALA 114 96  96  ALA ALA A . n 
A 1 115 ARG 115 97  97  ARG ARG A . n 
A 1 116 ALA 116 98  98  ALA ALA A . n 
A 1 117 PRO 117 99  99  PRO PRO A . n 
A 1 118 SER 118 100 ?   ?   ?   A . n 
A 1 119 ALA 119 101 ?   ?   ?   A . n 
A 1 120 THR 120 102 ?   ?   ?   A . n 
A 1 121 PRO 121 103 103 PRO PRO A . n 
A 1 122 ARG 122 104 104 ARG ARG A . n 
A 1 123 PRO 123 105 105 PRO PRO A . n 
A 1 124 LEU 124 106 106 LEU LEU A . n 
A 1 125 HIS 125 107 107 HIS HIS A . n 
A 1 126 LEU 126 108 108 LEU LEU A . n 
A 1 127 GLY 127 109 109 GLY GLY A . n 
A 1 128 PHE 128 110 110 PHE PHE A . n 
A 1 129 LEU 129 111 111 LEU LEU A . n 
A 1 130 CYS 130 112 112 CYS CYS A . n 
A 1 131 GLU 131 113 113 GLU GLU A . n 
A 1 132 TYR 132 114 114 TYR TYR A . n 
A 1 133 ASP 133 115 115 ASP ASP A . n 
A 1 134 ALA 134 116 116 ALA ALA A . n 
A 1 135 LEU 135 117 117 LEU LEU A . n 
A 1 136 PRO 136 118 118 PRO PRO A . n 
A 1 137 GLY 137 119 119 GLY GLY A . n 
A 1 138 ILE 138 120 120 ILE ILE A . n 
A 1 139 GLY 139 121 121 GLY GLY A . n 
A 1 140 HIS 140 122 122 HIS HIS A . n 
A 1 141 ALA 141 123 123 ALA ALA A . n 
A 1 142 CYS 142 124 124 CYS CYS A . n 
A 1 143 GLY 143 125 125 GLY GLY A . n 
A 1 144 HIS 144 126 126 HIS HIS A . n 
A 1 145 ASN 145 127 127 ASN ASN A . n 
A 1 146 LEU 146 128 128 LEU LEU A . n 
A 1 147 ILE 147 129 129 ILE ILE A . n 
A 1 148 ALA 148 130 130 ALA ALA A . n 
A 1 149 GLU 149 131 131 GLU GLU A . n 
A 1 150 VAL 150 132 132 VAL VAL A . n 
A 1 151 GLY 151 133 133 GLY GLY A . n 
A 1 152 ALA 152 134 134 ALA ALA A . n 
A 1 153 ALA 153 135 135 ALA ALA A . n 
A 1 154 ALA 154 136 136 ALA ALA A . n 
A 1 155 ALA 155 137 137 ALA ALA A . n 
A 1 156 LEU 156 138 138 LEU LEU A . n 
A 1 157 GLY 157 139 139 GLY GLY A . n 
A 1 158 VAL 158 140 140 VAL VAL A . n 
A 1 159 ARG 159 141 141 ARG ARG A . n 
A 1 160 GLY 160 142 142 GLY GLY A . n 
A 1 161 ALA 161 143 143 ALA ALA A . n 
A 1 162 LEU 162 144 144 LEU LEU A . n 
A 1 163 GLU 163 145 145 GLU GLU A . n 
A 1 164 GLY 164 146 146 GLY GLY A . n 
A 1 165 LEU 165 147 147 LEU LEU A . n 
A 1 166 PRO 166 148 148 PRO PRO A . n 
A 1 167 ARG 167 149 149 ARG ARG A . n 
A 1 168 PRO 168 150 150 PRO PRO A . n 
A 1 169 PRO 169 151 151 PRO PRO A . n 
A 1 170 PRO 170 152 152 PRO PRO A . n 
A 1 171 PRO 171 153 153 PRO PRO A . n 
A 1 172 VAL 172 154 154 VAL VAL A . n 
A 1 173 LYS 173 155 155 LYS LYS A . n 
A 1 174 VAL 174 156 156 VAL VAL A . n 
A 1 175 VAL 175 157 157 VAL VAL A . n 
A 1 176 VAL 176 158 158 VAL VAL A . n 
A 1 177 LEU 177 159 159 LEU LEU A . n 
A 1 178 GLY 178 160 160 GLY GLY A . n 
A 1 179 THR 179 161 161 THR THR A . n 
A 1 180 PRO 180 162 162 PRO PRO A . n 
A 1 181 ALA 181 163 163 ALA ALA A . n 
A 1 182 GLU 182 164 164 GLU GLU A . n 
A 1 183 GLU 183 165 165 GLU GLU A . n 
A 1 184 ASP 184 166 166 ASP ASP A . n 
A 1 185 GLY 185 167 167 GLY GLY A . n 
A 1 186 GLY 186 168 168 GLY GLY A . n 
A 1 187 GLY 187 169 169 GLY GLY A . n 
A 1 188 LYS 188 170 170 LYS LYS A . n 
A 1 189 ILE 189 171 171 ILE ILE A . n 
A 1 190 ASP 190 172 172 ASP ASP A . n 
A 1 191 LEU 191 173 173 LEU LEU A . n 
A 1 192 ILE 192 174 174 ILE ILE A . n 
A 1 193 GLU 193 175 175 GLU GLU A . n 
A 1 194 ALA 194 176 176 ALA ALA A . n 
A 1 195 GLY 195 177 177 GLY GLY A . n 
A 1 196 ALA 196 178 178 ALA ALA A . n 
A 1 197 PHE 197 179 179 PHE PHE A . n 
A 1 198 THR 198 180 180 THR THR A . n 
A 1 199 ASN 199 181 181 ASN ASN A . n 
A 1 200 LEU 200 182 182 LEU LEU A . n 
A 1 201 ASP 201 183 183 ASP ASP A . n 
A 1 202 VAL 202 184 184 VAL VAL A . n 
A 1 203 VAL 203 185 185 VAL VAL A . n 
A 1 204 PHE 204 186 186 PHE PHE A . n 
A 1 205 MET 205 187 187 MET MET A . n 
A 1 206 ALA 206 188 188 ALA ALA A . n 
A 1 207 HIS 207 189 189 HIS HIS A . n 
A 1 208 PRO 208 190 190 PRO PRO A . n 
A 1 209 SER 209 191 191 SER SER A . n 
A 1 210 GLN 210 192 192 GLN GLN A . n 
A 1 211 GLU 211 193 193 GLU GLU A . n 
A 1 212 ASN 212 194 194 ASN ASN A . n 
A 1 213 ALA 213 195 195 ALA ALA A . n 
A 1 214 ALA 214 196 196 ALA ALA A . n 
A 1 215 TYR 215 197 197 TYR TYR A . n 
A 1 216 LEU 216 198 198 LEU LEU A . n 
A 1 217 PRO 217 199 199 PRO PRO A . n 
A 1 218 ASP 218 200 200 ASP ASP A . n 
A 1 219 MET 219 201 201 MET MET A . n 
A 1 220 ALA 220 202 202 ALA ALA A . n 
A 1 221 GLU 221 203 203 GLU GLU A . n 
A 1 222 HIS 222 204 204 HIS HIS A . n 
A 1 223 ASP 223 205 205 ASP ASP A . n 
A 1 224 VAL 224 206 206 VAL VAL A . n 
A 1 225 THR 225 207 207 THR THR A . n 
A 1 226 VAL 226 208 208 VAL VAL A . n 
A 1 227 LYS 227 209 209 LYS LYS A . n 
A 1 228 TYR 228 210 210 TYR TYR A . n 
A 1 229 TYR 229 211 211 TYR TYR A . n 
A 1 230 GLY 230 212 212 GLY GLY A . n 
A 1 231 LYS 231 213 213 LYS LYS A . n 
A 1 232 ALA 232 214 214 ALA ALA A . n 
A 1 233 SER 233 215 ?   ?   ?   A . n 
A 1 234 HIS 234 216 ?   ?   ?   A . n 
A 1 235 SER 235 217 ?   ?   ?   A . n 
A 1 236 ALA 236 218 ?   ?   ?   A . n 
A 1 237 SER 237 219 ?   ?   ?   A . n 
A 1 238 TYR 238 220 220 TYR TYR A . n 
A 1 239 PRO 239 221 221 PRO PRO A . n 
A 1 240 TRP 240 222 222 TRP TRP A . n 
A 1 241 GLU 241 223 223 GLU GLU A . n 
A 1 242 GLY 242 224 224 GLY GLY A . n 
A 1 243 LEU 243 225 225 LEU LEU A . n 
A 1 244 ASN 244 226 226 ASN ASN A . n 
A 1 245 ALA 245 227 227 ALA ALA A . n 
A 1 246 LEU 246 228 228 LEU LEU A . n 
A 1 247 ASP 247 229 229 ASP ASP A . n 
A 1 248 ALA 248 230 230 ALA ALA A . n 
A 1 249 ALA 249 231 231 ALA ALA A . n 
A 1 250 VAL 250 232 232 VAL VAL A . n 
A 1 251 LEU 251 233 233 LEU LEU A . n 
A 1 252 ALA 252 234 234 ALA ALA A . n 
A 1 253 TYR 253 235 235 TYR TYR A . n 
A 1 254 ASN 254 236 236 ASN ASN A . n 
A 1 255 ASN 255 237 237 ASN ASN A . n 
A 1 256 LEU 256 238 238 LEU LEU A . n 
A 1 257 SER 257 239 239 SER SER A . n 
A 1 258 VAL 258 240 240 VAL VAL A . n 
A 1 259 PHE 259 241 241 PHE PHE A . n 
A 1 260 ARG 260 242 242 ARG ARG A . n 
A 1 261 GLN 261 243 243 GLN GLN A . n 
A 1 262 GLN 262 244 244 GLN GLN A . n 
A 1 263 MET 263 245 245 MET MET A . n 
A 1 264 LYS 264 246 246 LYS LYS A . n 
A 1 265 PRO 265 247 247 PRO PRO A . n 
A 1 266 THR 266 248 248 THR THR A . n 
A 1 267 TRP 267 249 249 TRP TRP A . n 
A 1 268 ARG 268 250 250 ARG ARG A . n 
A 1 269 VAL 269 251 251 VAL VAL A . n 
A 1 270 HIS 270 252 252 HIS HIS A . n 
A 1 271 GLY 271 253 253 GLY GLY A . n 
A 1 272 ILE 272 254 254 ILE ILE A . n 
A 1 273 ILE 273 255 255 ILE ILE A . n 
A 1 274 LYS 274 256 256 LYS LYS A . n 
A 1 275 ASN 275 257 257 ASN ASN A . n 
A 1 276 GLY 276 258 258 GLY GLY A . n 
A 1 277 GLY 277 259 259 GLY GLY A . n 
A 1 278 VAL 278 260 260 VAL VAL A . n 
A 1 279 LYS 279 261 261 LYS LYS A . n 
A 1 280 PRO 280 262 262 PRO PRO A . n 
A 1 281 ASN 281 263 263 ASN ASN A . n 
A 1 282 ILE 282 264 264 ILE ILE A . n 
A 1 283 ILE 283 265 265 ILE ILE A . n 
A 1 284 PRO 284 266 266 PRO PRO A . n 
A 1 285 SER 285 267 267 SER SER A . n 
A 1 286 TYR 286 268 268 TYR TYR A . n 
A 1 287 SER 287 269 269 SER SER A . n 
A 1 288 GLU 288 270 270 GLU GLU A . n 
A 1 289 LEU 289 271 271 LEU LEU A . n 
A 1 290 ILE 290 272 272 ILE ILE A . n 
A 1 291 TYR 291 273 273 TYR TYR A . n 
A 1 292 TYR 292 274 274 TYR TYR A . n 
A 1 293 PHE 293 275 275 PHE PHE A . n 
A 1 294 ARG 294 276 276 ARG ARG A . n 
A 1 295 ALA 295 277 277 ALA ALA A . n 
A 1 296 PRO 296 278 278 PRO PRO A . n 
A 1 297 SER 297 279 279 SER SER A . n 
A 1 298 MET 298 280 280 MET MET A . n 
A 1 299 LYS 299 281 281 LYS LYS A . n 
A 1 300 GLU 300 282 282 GLU GLU A . n 
A 1 301 LEU 301 283 283 LEU LEU A . n 
A 1 302 GLN 302 284 284 GLN GLN A . n 
A 1 303 VAL 303 285 285 VAL VAL A . n 
A 1 304 LEU 304 286 286 LEU LEU A . n 
A 1 305 THR 305 287 287 THR THR A . n 
A 1 306 LYS 306 288 288 LYS LYS A . n 
A 1 307 LYS 307 289 289 LYS LYS A . n 
A 1 308 ALA 308 290 290 ALA ALA A . n 
A 1 309 GLU 309 291 291 GLU GLU A . n 
A 1 310 ASP 310 292 292 ASP ASP A . n 
A 1 311 CYS 311 293 293 CYS CYS A . n 
A 1 312 PHE 312 294 294 PHE PHE A . n 
A 1 313 ARG 313 295 295 ARG ARG A . n 
A 1 314 ALA 314 296 296 ALA ALA A . n 
A 1 315 ALA 315 297 297 ALA ALA A . n 
A 1 316 ALA 316 298 298 ALA ALA A . n 
A 1 317 LEU 317 299 299 LEU LEU A . n 
A 1 318 ALA 318 300 300 ALA ALA A . n 
A 1 319 SER 319 301 301 SER SER A . n 
A 1 320 GLY 320 302 302 GLY GLY A . n 
A 1 321 CYS 321 303 303 CYS CYS A . n 
A 1 322 THR 322 304 304 THR THR A . n 
A 1 323 VAL 323 305 305 VAL VAL A . n 
A 1 324 GLU 324 306 306 GLU GLU A . n 
A 1 325 ILE 325 307 307 ILE ILE A . n 
A 1 326 LYS 326 308 308 LYS LYS A . n 
A 1 327 GLY 327 309 309 GLY GLY A . n 
A 1 328 GLY 328 310 310 GLY GLY A . n 
A 1 329 ALA 329 311 311 ALA ALA A . n 
A 1 330 HIS 330 312 312 HIS HIS A . n 
A 1 331 ASP 331 313 313 ASP ASP A . n 
A 1 332 PHE 332 314 314 PHE PHE A . n 
A 1 333 TYR 333 315 315 TYR TYR A . n 
A 1 334 ASN 334 316 316 ASN ASN A . n 
A 1 335 VAL 335 317 317 VAL VAL A . n 
A 1 336 LEU 336 318 318 LEU LEU A . n 
A 1 337 PRO 337 319 319 PRO PRO A . n 
A 1 338 ASN 338 320 320 ASN ASN A . n 
A 1 339 LYS 339 321 321 LYS LYS A . n 
A 1 340 SER 340 322 322 SER SER A . n 
A 1 341 LEU 341 323 323 LEU LEU A . n 
A 1 342 TRP 342 324 324 TRP TRP A . n 
A 1 343 LYS 343 325 325 LYS LYS A . n 
A 1 344 ALA 344 326 326 ALA ALA A . n 
A 1 345 TYR 345 327 327 TYR TYR A . n 
A 1 346 MET 346 328 328 MET MET A . n 
A 1 347 GLU 347 329 329 GLU GLU A . n 
A 1 348 ASN 348 330 330 ASN ASN A . n 
A 1 349 GLY 349 331 331 GLY GLY A . n 
A 1 350 ARG 350 332 332 ARG ARG A . n 
A 1 351 LYS 351 333 333 LYS LYS A . n 
A 1 352 LEU 352 334 334 LEU LEU A . n 
A 1 353 GLY 353 335 335 GLY GLY A . n 
A 1 354 ILE 354 336 336 ILE ILE A . n 
A 1 355 GLU 355 337 337 GLU GLU A . n 
A 1 356 PHE 356 338 338 PHE PHE A . n 
A 1 357 ILE 357 339 339 ILE ILE A . n 
A 1 358 SER 358 340 ?   ?   ?   A . n 
A 1 359 GLU 359 341 ?   ?   ?   A . n 
A 1 360 ASP 360 342 ?   ?   ?   A . n 
A 1 361 THR 361 343 ?   ?   ?   A . n 
A 1 362 MET 362 344 ?   ?   ?   A . n 
A 1 363 LEU 363 345 ?   ?   ?   A . n 
A 1 364 ASN 364 346 ?   ?   ?   A . n 
A 1 365 GLY 365 347 ?   ?   ?   A . n 
A 1 366 PRO 366 348 348 PRO PRO A . n 
A 1 367 SER 367 349 349 SER SER A . n 
A 1 368 GLY 368 350 350 GLY GLY A . n 
A 1 369 SER 369 351 351 SER SER A . n 
A 1 370 THR 370 352 352 THR THR A . n 
A 1 371 ASP 371 353 353 ASP ASP A . n 
A 1 372 PHE 372 354 354 PHE PHE A . n 
A 1 373 GLY 373 355 355 GLY GLY A . n 
A 1 374 ASN 374 356 356 ASN ASN A . n 
A 1 375 VAL 375 357 357 VAL VAL A . n 
A 1 376 SER 376 358 358 SER SER A . n 
A 1 377 PHE 377 359 359 PHE PHE A . n 
A 1 378 VAL 378 360 360 VAL VAL A . n 
A 1 379 VAL 379 361 361 VAL VAL A . n 
A 1 380 PRO 380 362 362 PRO PRO A . n 
A 1 381 GLY 381 363 363 GLY GLY A . n 
A 1 382 ILE 382 364 364 ILE ILE A . n 
A 1 383 HIS 383 365 365 HIS HIS A . n 
A 1 384 PRO 384 366 366 PRO PRO A . n 
A 1 385 TYR 385 367 367 TYR TYR A . n 
A 1 386 PHE 386 368 368 PHE PHE A . n 
A 1 387 HIS 387 369 369 HIS HIS A . n 
A 1 388 ILE 388 370 370 ILE ILE A . n 
A 1 389 GLY 389 371 371 GLY GLY A . n 
A 1 390 SER 390 372 372 SER SER A . n 
A 1 391 ASN 391 373 373 ASN ASN A . n 
A 1 392 ALA 392 374 374 ALA ALA A . n 
A 1 393 LEU 393 375 375 LEU LEU A . n 
A 1 394 ASN 394 376 376 ASN ASN A . n 
A 1 395 HIS 395 377 377 HIS HIS A . n 
A 1 396 THR 396 378 378 THR THR A . n 
A 1 397 GLU 397 379 379 GLU GLU A . n 
A 1 398 GLN 398 380 380 GLN GLN A . n 
A 1 399 TYR 399 381 381 TYR TYR A . n 
A 1 400 THR 400 382 382 THR THR A . n 
A 1 401 GLU 401 383 383 GLU GLU A . n 
A 1 402 ALA 402 384 384 ALA ALA A . n 
A 1 403 ALA 403 385 385 ALA ALA A . n 
A 1 404 GLY 404 386 386 GLY GLY A . n 
A 1 405 SER 405 387 387 SER SER A . n 
A 1 406 GLN 406 388 388 GLN GLN A . n 
A 1 407 GLU 407 389 389 GLU GLU A . n 
A 1 408 ALA 408 390 390 ALA ALA A . n 
A 1 409 GLN 409 391 391 GLN GLN A . n 
A 1 410 PHE 410 392 392 PHE PHE A . n 
A 1 411 TYR 411 393 393 TYR TYR A . n 
A 1 412 THR 412 394 394 THR THR A . n 
A 1 413 LEU 413 395 395 LEU LEU A . n 
A 1 414 ARG 414 396 396 ARG ARG A . n 
A 1 415 THR 415 397 397 THR THR A . n 
A 1 416 ALA 416 398 398 ALA ALA A . n 
A 1 417 LYS 417 399 399 LYS LYS A . n 
A 1 418 ALA 418 400 400 ALA ALA A . n 
A 1 419 LEU 419 401 401 LEU LEU A . n 
A 1 420 ALA 420 402 402 ALA ALA A . n 
A 1 421 MET 421 403 403 MET MET A . n 
A 1 422 THR 422 404 404 THR THR A . n 
A 1 423 ALA 423 405 405 ALA ALA A . n 
A 1 424 LEU 424 406 406 LEU LEU A . n 
A 1 425 ASP 425 407 407 ASP ASP A . n 
A 1 426 VAL 426 408 408 VAL VAL A . n 
A 1 427 ILE 427 409 409 ILE ILE A . n 
A 1 428 PHE 428 410 410 PHE PHE A . n 
A 1 429 LYS 429 411 411 LYS LYS A . n 
A 1 430 PRO 430 412 412 PRO PRO A . n 
A 1 431 GLU 431 413 413 GLU GLU A . n 
A 1 432 LEU 432 414 414 LEU LEU A . n 
A 1 433 LEU 433 415 415 LEU LEU A . n 
A 1 434 GLU 434 416 416 GLU GLU A . n 
A 1 435 GLY 435 417 417 GLY GLY A . n 
A 1 436 ILE 436 418 418 ILE ILE A . n 
A 1 437 ARG 437 419 419 ARG ARG A . n 
A 1 438 GLU 438 420 420 GLU GLU A . n 
A 1 439 ASP 439 421 421 ASP ASP A . n 
A 1 440 PHE 440 422 422 PHE PHE A . n 
A 1 441 LYS 441 423 423 LYS LYS A . n 
A 1 442 LEU 442 424 424 LEU LEU A . n 
A 1 443 LYS 443 425 425 LYS LYS A . n 
A 1 444 LEU 444 426 426 LEU LEU A . n 
A 1 445 GLN 445 427 427 GLN GLN A . n 
A 1 446 GLU 446 428 428 GLU GLU A . n 
A 1 447 GLU 447 429 429 GLU GLU A . n 
A 1 448 GLN 448 430 430 GLN GLN A . n 
A 1 449 PHE 449 431 ?   ?   ?   A . n 
A 1 450 VAL 450 432 ?   ?   ?   A . n 
A 1 451 ASN 451 433 ?   ?   ?   A . n 
A 1 452 ALA 452 434 ?   ?   ?   A . n 
A 1 453 VAL 453 435 ?   ?   ?   A . n 
A 1 454 GLU 454 436 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 PO4 ? ? PO4 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ZN  ? ? ZN  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 PO4 1  501 1  PO4 PO4 A . 
C 2 PO4 1  502 2  PO4 PO4 A . 
D 3 ZN  1  503 1  ZN  ZN  A . 
E 3 ZN  1  504 2  ZN  ZN  A . 
F 4 HOH 1  601 47 HOH HOH A . 
F 4 HOH 2  602 84 HOH HOH A . 
F 4 HOH 3  603 76 HOH HOH A . 
F 4 HOH 4  604 4  HOH HOH A . 
F 4 HOH 5  605 50 HOH HOH A . 
F 4 HOH 6  606 6  HOH HOH A . 
F 4 HOH 7  607 53 HOH HOH A . 
F 4 HOH 8  608 2  HOH HOH A . 
F 4 HOH 9  609 9  HOH HOH A . 
F 4 HOH 10 610 29 HOH HOH A . 
F 4 HOH 11 611 34 HOH HOH A . 
F 4 HOH 12 612 11 HOH HOH A . 
F 4 HOH 13 613 20 HOH HOH A . 
F 4 HOH 14 614 51 HOH HOH A . 
F 4 HOH 15 615 32 HOH HOH A . 
F 4 HOH 16 616 62 HOH HOH A . 
F 4 HOH 17 617 68 HOH HOH A . 
F 4 HOH 18 618 1  HOH HOH A . 
F 4 HOH 19 619 12 HOH HOH A . 
F 4 HOH 20 620 8  HOH HOH A . 
F 4 HOH 21 621 65 HOH HOH A . 
F 4 HOH 22 622 43 HOH HOH A . 
F 4 HOH 23 623 13 HOH HOH A . 
F 4 HOH 24 624 48 HOH HOH A . 
F 4 HOH 25 625 18 HOH HOH A . 
F 4 HOH 26 626 75 HOH HOH A . 
F 4 HOH 27 627 5  HOH HOH A . 
F 4 HOH 28 628 37 HOH HOH A . 
F 4 HOH 29 629 56 HOH HOH A . 
F 4 HOH 30 630 52 HOH HOH A . 
F 4 HOH 31 631 33 HOH HOH A . 
F 4 HOH 32 632 45 HOH HOH A . 
F 4 HOH 33 633 31 HOH HOH A . 
F 4 HOH 34 634 15 HOH HOH A . 
F 4 HOH 35 635 7  HOH HOH A . 
F 4 HOH 36 636 17 HOH HOH A . 
F 4 HOH 37 637 14 HOH HOH A . 
F 4 HOH 38 638 77 HOH HOH A . 
F 4 HOH 39 639 80 HOH HOH A . 
F 4 HOH 40 640 49 HOH HOH A . 
F 4 HOH 41 641 10 HOH HOH A . 
F 4 HOH 42 642 66 HOH HOH A . 
F 4 HOH 43 643 26 HOH HOH A . 
F 4 HOH 44 644 3  HOH HOH A . 
F 4 HOH 45 645 27 HOH HOH A . 
F 4 HOH 46 646 22 HOH HOH A . 
F 4 HOH 47 647 35 HOH HOH A . 
F 4 HOH 48 648 64 HOH HOH A . 
F 4 HOH 49 649 21 HOH HOH A . 
F 4 HOH 50 650 70 HOH HOH A . 
F 4 HOH 51 651 63 HOH HOH A . 
F 4 HOH 52 652 41 HOH HOH A . 
F 4 HOH 53 653 24 HOH HOH A . 
F 4 HOH 54 654 42 HOH HOH A . 
F 4 HOH 55 655 39 HOH HOH A . 
F 4 HOH 56 656 72 HOH HOH A . 
F 4 HOH 57 657 16 HOH HOH A . 
F 4 HOH 58 658 82 HOH HOH A . 
F 4 HOH 59 659 58 HOH HOH A . 
F 4 HOH 60 660 59 HOH HOH A . 
F 4 HOH 61 661 30 HOH HOH A . 
F 4 HOH 62 662 60 HOH HOH A . 
F 4 HOH 63 663 73 HOH HOH A . 
F 4 HOH 64 664 19 HOH HOH A . 
F 4 HOH 65 665 25 HOH HOH A . 
F 4 HOH 66 666 71 HOH HOH A . 
F 4 HOH 67 667 78 HOH HOH A . 
F 4 HOH 68 668 36 HOH HOH A . 
F 4 HOH 69 669 67 HOH HOH A . 
F 4 HOH 70 670 28 HOH HOH A . 
F 4 HOH 71 671 44 HOH HOH A . 
F 4 HOH 72 672 23 HOH HOH A . 
F 4 HOH 73 673 54 HOH HOH A . 
F 4 HOH 74 674 69 HOH HOH A . 
F 4 HOH 75 675 40 HOH HOH A . 
F 4 HOH 76 676 55 HOH HOH A . 
F 4 HOH 77 677 79 HOH HOH A . 
F 4 HOH 78 678 61 HOH HOH A . 
F 4 HOH 79 679 74 HOH HOH A . 
F 4 HOH 80 680 46 HOH HOH A . 
F 4 HOH 81 681 57 HOH HOH A . 
F 4 HOH 82 682 38 HOH HOH A . 
F 4 HOH 83 683 81 HOH HOH A . 
F 4 HOH 84 684 83 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LEU 14  ? CD1 ? A LEU 32  CD1 
2   1 Y 1 A LEU 14  ? CD2 ? A LEU 32  CD2 
3   1 Y 1 A GLN 17  ? CG  ? A GLN 35  CG  
4   1 Y 1 A GLN 17  ? CD  ? A GLN 35  CD  
5   1 Y 1 A GLN 17  ? OE1 ? A GLN 35  OE1 
6   1 Y 1 A GLN 17  ? NE2 ? A GLN 35  NE2 
7   1 Y 1 A SER 19  ? OG  ? A SER 37  OG  
8   1 Y 1 A GLU 21  ? CG  ? A GLU 39  CG  
9   1 Y 1 A GLU 21  ? CD  ? A GLU 39  CD  
10  1 Y 1 A GLU 21  ? OE1 ? A GLU 39  OE1 
11  1 Y 1 A GLU 21  ? OE2 ? A GLU 39  OE2 
12  1 Y 1 A LEU 22  ? CD1 ? A LEU 40  CD1 
13  1 Y 1 A LEU 22  ? CD2 ? A LEU 40  CD2 
14  1 Y 1 A ARG 26  ? NE  ? A ARG 44  NE  
15  1 Y 1 A ARG 26  ? CZ  ? A ARG 44  CZ  
16  1 Y 1 A ARG 26  ? NH1 ? A ARG 44  NH1 
17  1 Y 1 A ARG 26  ? NH2 ? A ARG 44  NH2 
18  1 Y 1 A GLU 36  ? CG  ? A GLU 54  CG  
19  1 Y 1 A GLU 36  ? CD  ? A GLU 54  CD  
20  1 Y 1 A GLU 36  ? OE1 ? A GLU 54  OE1 
21  1 Y 1 A GLU 36  ? OE2 ? A GLU 54  OE2 
22  1 Y 1 A ARG 97  ? CG  ? A ARG 115 CG  
23  1 Y 1 A ARG 97  ? CD  ? A ARG 115 CD  
24  1 Y 1 A ARG 97  ? NE  ? A ARG 115 NE  
25  1 Y 1 A ARG 97  ? CZ  ? A ARG 115 CZ  
26  1 Y 1 A ARG 97  ? NH1 ? A ARG 115 NH1 
27  1 Y 1 A ARG 97  ? NH2 ? A ARG 115 NH2 
28  1 Y 1 A ARG 104 ? CG  ? A ARG 122 CG  
29  1 Y 1 A ARG 104 ? CD  ? A ARG 122 CD  
30  1 Y 1 A ARG 104 ? NE  ? A ARG 122 NE  
31  1 Y 1 A ARG 104 ? CZ  ? A ARG 122 CZ  
32  1 Y 1 A ARG 104 ? NH1 ? A ARG 122 NH1 
33  1 Y 1 A ARG 104 ? NH2 ? A ARG 122 NH2 
34  1 Y 1 A LEU 147 ? CD1 ? A LEU 165 CD1 
35  1 Y 1 A LEU 147 ? CD2 ? A LEU 165 CD2 
36  1 Y 1 A ARG 149 ? CG  ? A ARG 167 CG  
37  1 Y 1 A ARG 149 ? CD  ? A ARG 167 CD  
38  1 Y 1 A ARG 149 ? NE  ? A ARG 167 NE  
39  1 Y 1 A ARG 149 ? CZ  ? A ARG 167 CZ  
40  1 Y 1 A ARG 149 ? NH1 ? A ARG 167 NH1 
41  1 Y 1 A ARG 149 ? NH2 ? A ARG 167 NH2 
42  1 Y 1 A GLU 193 ? CG  ? A GLU 211 CG  
43  1 Y 1 A GLU 193 ? CD  ? A GLU 211 CD  
44  1 Y 1 A GLU 193 ? OE1 ? A GLU 211 OE1 
45  1 Y 1 A GLU 193 ? OE2 ? A GLU 211 OE2 
46  1 Y 1 A LYS 213 ? CG  ? A LYS 231 CG  
47  1 Y 1 A LYS 213 ? CD  ? A LYS 231 CD  
48  1 Y 1 A LYS 213 ? CE  ? A LYS 231 CE  
49  1 Y 1 A LYS 213 ? NZ  ? A LYS 231 NZ  
50  1 Y 1 A TYR 220 ? CG  ? A TYR 238 CG  
51  1 Y 1 A TYR 220 ? CD1 ? A TYR 238 CD1 
52  1 Y 1 A TYR 220 ? CD2 ? A TYR 238 CD2 
53  1 Y 1 A TYR 220 ? CE1 ? A TYR 238 CE1 
54  1 Y 1 A TYR 220 ? CE2 ? A TYR 238 CE2 
55  1 Y 1 A TYR 220 ? CZ  ? A TYR 238 CZ  
56  1 Y 1 A TYR 220 ? OH  ? A TYR 238 OH  
57  1 Y 1 A GLU 223 ? CG  ? A GLU 241 CG  
58  1 Y 1 A GLU 223 ? CD  ? A GLU 241 CD  
59  1 Y 1 A GLU 223 ? OE1 ? A GLU 241 OE1 
60  1 Y 1 A GLU 223 ? OE2 ? A GLU 241 OE2 
61  1 Y 1 A LYS 261 ? CG  ? A LYS 279 CG  
62  1 Y 1 A LYS 261 ? CD  ? A LYS 279 CD  
63  1 Y 1 A LYS 261 ? CE  ? A LYS 279 CE  
64  1 Y 1 A LYS 261 ? NZ  ? A LYS 279 NZ  
65  1 Y 1 A ILE 264 ? CG1 ? A ILE 282 CG1 
66  1 Y 1 A ILE 264 ? CG2 ? A ILE 282 CG2 
67  1 Y 1 A ILE 264 ? CD1 ? A ILE 282 CD1 
68  1 Y 1 A ILE 265 ? CD1 ? A ILE 283 CD1 
69  1 Y 1 A LYS 281 ? CG  ? A LYS 299 CG  
70  1 Y 1 A LYS 281 ? CD  ? A LYS 299 CD  
71  1 Y 1 A LYS 281 ? CE  ? A LYS 299 CE  
72  1 Y 1 A LYS 281 ? NZ  ? A LYS 299 NZ  
73  1 Y 1 A GLN 284 ? CG  ? A GLN 302 CG  
74  1 Y 1 A GLN 284 ? CD  ? A GLN 302 CD  
75  1 Y 1 A GLN 284 ? OE1 ? A GLN 302 OE1 
76  1 Y 1 A GLN 284 ? NE2 ? A GLN 302 NE2 
77  1 Y 1 A LYS 308 ? CE  ? A LYS 326 CE  
78  1 Y 1 A LYS 308 ? NZ  ? A LYS 326 NZ  
79  1 Y 1 A LYS 321 ? CG  ? A LYS 339 CG  
80  1 Y 1 A LYS 321 ? CD  ? A LYS 339 CD  
81  1 Y 1 A LYS 321 ? CE  ? A LYS 339 CE  
82  1 Y 1 A LYS 321 ? NZ  ? A LYS 339 NZ  
83  1 Y 1 A TRP 324 ? CG  ? A TRP 342 CG  
84  1 Y 1 A TRP 324 ? CD1 ? A TRP 342 CD1 
85  1 Y 1 A TRP 324 ? CD2 ? A TRP 342 CD2 
86  1 Y 1 A TRP 324 ? NE1 ? A TRP 342 NE1 
87  1 Y 1 A TRP 324 ? CE2 ? A TRP 342 CE2 
88  1 Y 1 A TRP 324 ? CE3 ? A TRP 342 CE3 
89  1 Y 1 A TRP 324 ? CZ2 ? A TRP 342 CZ2 
90  1 Y 1 A TRP 324 ? CZ3 ? A TRP 342 CZ3 
91  1 Y 1 A TRP 324 ? CH2 ? A TRP 342 CH2 
92  1 Y 1 A LYS 325 ? CG  ? A LYS 343 CG  
93  1 Y 1 A LYS 325 ? CD  ? A LYS 343 CD  
94  1 Y 1 A LYS 325 ? CE  ? A LYS 343 CE  
95  1 Y 1 A LYS 325 ? NZ  ? A LYS 343 NZ  
96  1 Y 1 A GLU 329 ? CG  ? A GLU 347 CG  
97  1 Y 1 A GLU 329 ? CD  ? A GLU 347 CD  
98  1 Y 1 A GLU 329 ? OE1 ? A GLU 347 OE1 
99  1 Y 1 A GLU 329 ? OE2 ? A GLU 347 OE2 
100 1 Y 1 A GLU 337 ? CG  ? A GLU 355 CG  
101 1 Y 1 A GLU 337 ? CD  ? A GLU 355 CD  
102 1 Y 1 A GLU 337 ? OE1 ? A GLU 355 OE1 
103 1 Y 1 A GLU 337 ? OE2 ? A GLU 355 OE2 
104 1 Y 1 A ILE 339 ? CD1 ? A ILE 357 CD1 
105 1 Y 1 A SER 349 ? OG  ? A SER 367 OG  
106 1 Y 1 A GLU 413 ? OE1 ? A GLU 431 OE1 
107 1 Y 1 A GLU 413 ? OE2 ? A GLU 431 OE2 
108 1 Y 1 A GLU 416 ? CG  ? A GLU 434 CG  
109 1 Y 1 A GLU 416 ? CD  ? A GLU 434 CD  
110 1 Y 1 A GLU 416 ? OE1 ? A GLU 434 OE1 
111 1 Y 1 A GLU 416 ? OE2 ? A GLU 434 OE2 
112 1 Y 1 A GLU 420 ? CG  ? A GLU 438 CG  
113 1 Y 1 A GLU 420 ? CD  ? A GLU 438 CD  
114 1 Y 1 A GLU 420 ? OE1 ? A GLU 438 OE1 
115 1 Y 1 A GLU 420 ? OE2 ? A GLU 438 OE2 
116 1 Y 1 A LYS 423 ? CG  ? A LYS 441 CG  
117 1 Y 1 A LYS 423 ? CD  ? A LYS 441 CD  
118 1 Y 1 A LYS 423 ? CE  ? A LYS 441 CE  
119 1 Y 1 A LYS 423 ? NZ  ? A LYS 441 NZ  
120 1 Y 1 A LEU 424 ? CG  ? A LEU 442 CG  
121 1 Y 1 A LEU 424 ? CD1 ? A LEU 442 CD1 
122 1 Y 1 A LEU 424 ? CD2 ? A LEU 442 CD2 
123 1 Y 1 A LYS 425 ? CD  ? A LYS 443 CD  
124 1 Y 1 A LYS 425 ? CE  ? A LYS 443 CE  
125 1 Y 1 A LYS 425 ? NZ  ? A LYS 443 NZ  
126 1 Y 1 A GLN 427 ? CD  ? A GLN 445 CD  
127 1 Y 1 A GLN 427 ? OE1 ? A GLN 445 OE1 
128 1 Y 1 A GLN 427 ? NE2 ? A GLN 445 NE2 
129 1 Y 1 A GLN 430 ? CG  ? A GLN 448 CG  
130 1 Y 1 A GLN 430 ? CD  ? A GLN 448 CD  
131 1 Y 1 A GLN 430 ? OE1 ? A GLN 448 OE1 
132 1 Y 1 A GLN 430 ? NE2 ? A GLN 448 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 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                     8XZC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     79.935 
_cell.length_a_esd                 ? 
_cell.length_b                     115.526 
_cell.length_b_esd                 ? 
_cell.length_c                     124.434 
_cell.length_c_esd                 ? 
_cell.volume                       1149094.584 
_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                         8XZC 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_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                   8XZC 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.81 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.3 
_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          MICROBATCH 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.6 
_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    
'70 mM calcium chloride, 35 mM sodium acetate pH4.6, 7% isopropanol, 15% glycerol, 20 mM Tris-Cl, and 200 mM NaCl (mixed in 1:1)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_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         2023-12-05 
_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   0.987 
_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                        'RRCAT INDUS-2 BEAMLINE PX-BL21' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   PX-BL21 
_diffrn_source.pdbx_synchrotron_site       'RRCAT INDUS-2' 
# 
_reflns.B_iso_Wilson_estimate                          50.95 
_reflns.entry_id                                       8XZC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.35 
_reflns.d_resolution_low                               45.19 
_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                                     24352 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.8 
_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                                0.105 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.098 
_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                                    2.35 
_reflns_shell.d_res_low                                     2.43 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2341 
_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                               8.3 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.668 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.382 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               62.84 
_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                                 8XZC 
_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                            2.35 
_refine.ls_d_res_low                             36.82 
_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                     24315 
_refine.ls_number_reflns_R_free                  1185 
_refine.ls_number_reflns_R_work                  23130 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.79 
_refine.ls_percent_reflns_R_free                 4.87 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1979 
_refine.ls_R_factor_R_free                       0.2399 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1956 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.6230 
_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                            0.2870 
_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                       2.35 
_refine_hist.d_res_low                        36.82 
_refine_hist.number_atoms_solvent             84 
_refine_hist.number_atoms_total               3094 
_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        2998 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_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' ? 0.0031 ? 3120 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5295 ? 4264 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0399 ? 465  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0044 ? 561  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 4.4771 ? 434  ? 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' 2.35 2.46  . . 133 2842 99.93  . . . . 0.2650 . . . . . . . . . . . 0.3274 
'X-RAY DIFFRACTION' 2.46 2.59  . . 119 2888 99.90  . . . . 0.2485 . . . . . . . . . . . 0.2917 
'X-RAY DIFFRACTION' 2.59 2.75  . . 158 2858 99.70  . . . . 0.2543 . . . . . . . . . . . 0.3420 
'X-RAY DIFFRACTION' 2.75 2.96  . . 145 2863 99.90  . . . . 0.2343 . . . . . . . . . . . 0.3061 
'X-RAY DIFFRACTION' 2.96 3.26  . . 173 2849 100.00 . . . . 0.2208 . . . . . . . . . . . 0.2392 
'X-RAY DIFFRACTION' 3.26 3.73  . . 131 2903 99.77  . . . . 0.2059 . . . . . . . . . . . 0.2618 
'X-RAY DIFFRACTION' 3.73 4.70  . . 156 2933 100.00 . . . . 0.1605 . . . . . . . . . . . 0.2079 
'X-RAY DIFFRACTION' 4.70 36.82 . . 170 2994 99.18  . . . . 0.1730 . . . . . . . . . . . 0.2095 
# 
_struct.entry_id                     8XZC 
_struct.title                        
'Crystal structure of human cytosolic beta-alanyl lysine dipeptidase (PM20D2) Tyr314Phe 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        8XZC 
_struct_keywords.text            'PM20D2, Carnosine, Proofreading, Cytosolic, Metabolite, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    P20D2_HUMAN 
_struct_ref.pdbx_db_accession          Q8IYS1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LELLKLRSAECIDEAAERLGALSRAIWSQPELAYEEHHAHRVLTHFFEREPPAASWAVQPHYQLPTAFRAEWEPPEARAP
SATPRPLHLGFLCEYDALPGIGHACGHNLIAEVGAAAALGVRGALEGLPRPPPPVKVVVLGTPAEEDGGGKIDLIEAGAF
TNLDVVFMAHPSQENAAYLPDMAEHDVTVKYYGKASHSASYPWEGLNALDAAVLAYNNLSVFRQQMKPTWRVHGIIKNGG
VKPNIIPSYSELIYYFRAPSMKELQVLTKKAEDCFRAAALASGCTVEIKGGAHDYYNVLPNKSLWKAYMENGRKLGIEFI
SEDTMLNGPSGSTDFGNVSFVVPGIHPYFHIGSNALNHTEQYTEAAGSQEAQFYTLRTAKALAMTALDVIFKPELLEGIR
EDFKLKLQEEQFVNAVE
;
_struct_ref.pdbx_align_begin           20 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8XZC 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 38 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 454 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q8IYS1 
_struct_ref_seq.db_align_beg                  20 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  436 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       20 
_struct_ref_seq.pdbx_auth_seq_align_end       436 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8XZC MET A 1   ? UNP Q8IYS1 ?   ?   'initiating methionine' -17 1  
1 8XZC ALA A 2   ? UNP Q8IYS1 ?   ?   'expression tag'        -16 2  
1 8XZC SER A 3   ? UNP Q8IYS1 ?   ?   'expression tag'        -15 3  
1 8XZC TRP A 4   ? UNP Q8IYS1 ?   ?   'expression tag'        -14 4  
1 8XZC SER A 5   ? UNP Q8IYS1 ?   ?   'expression tag'        -13 5  
1 8XZC HIS A 6   ? UNP Q8IYS1 ?   ?   'expression tag'        -12 6  
1 8XZC PRO A 7   ? UNP Q8IYS1 ?   ?   'expression tag'        -11 7  
1 8XZC GLN A 8   ? UNP Q8IYS1 ?   ?   'expression tag'        -10 8  
1 8XZC PHE A 9   ? UNP Q8IYS1 ?   ?   'expression tag'        -9  9  
1 8XZC GLU A 10  ? UNP Q8IYS1 ?   ?   'expression tag'        -8  10 
1 8XZC GLY A 11  ? UNP Q8IYS1 ?   ?   'expression tag'        -7  11 
1 8XZC GLY A 12  ? UNP Q8IYS1 ?   ?   'expression tag'        -6  12 
1 8XZC SER A 13  ? UNP Q8IYS1 ?   ?   'expression tag'        -5  13 
1 8XZC SER A 14  ? UNP Q8IYS1 ?   ?   'expression tag'        -4  14 
1 8XZC HIS A 15  ? UNP Q8IYS1 ?   ?   'expression tag'        -3  15 
1 8XZC HIS A 16  ? UNP Q8IYS1 ?   ?   'expression tag'        -2  16 
1 8XZC HIS A 17  ? UNP Q8IYS1 ?   ?   'expression tag'        -1  17 
1 8XZC HIS A 18  ? UNP Q8IYS1 ?   ?   'expression tag'        0   18 
1 8XZC HIS A 19  ? UNP Q8IYS1 ?   ?   'expression tag'        1   19 
1 8XZC HIS A 20  ? UNP Q8IYS1 ?   ?   'expression tag'        2   20 
1 8XZC SER A 21  ? UNP Q8IYS1 ?   ?   'expression tag'        3   21 
1 8XZC SER A 22  ? UNP Q8IYS1 ?   ?   'expression tag'        4   22 
1 8XZC GLY A 23  ? UNP Q8IYS1 ?   ?   'expression tag'        5   23 
1 8XZC SER A 24  ? UNP Q8IYS1 ?   ?   'expression tag'        6   24 
1 8XZC GLY A 25  ? UNP Q8IYS1 ?   ?   'expression tag'        7   25 
1 8XZC GLY A 26  ? UNP Q8IYS1 ?   ?   'expression tag'        8   26 
1 8XZC GLY A 27  ? UNP Q8IYS1 ?   ?   'expression tag'        9   27 
1 8XZC GLY A 28  ? UNP Q8IYS1 ?   ?   'expression tag'        10  28 
1 8XZC GLY A 29  ? UNP Q8IYS1 ?   ?   'expression tag'        11  29 
1 8XZC GLU A 30  ? UNP Q8IYS1 ?   ?   'expression tag'        12  30 
1 8XZC ASN A 31  ? UNP Q8IYS1 ?   ?   'expression tag'        13  31 
1 8XZC LEU A 32  ? UNP Q8IYS1 ?   ?   'expression tag'        14  32 
1 8XZC TYR A 33  ? UNP Q8IYS1 ?   ?   'expression tag'        15  33 
1 8XZC PHE A 34  ? UNP Q8IYS1 ?   ?   'expression tag'        16  34 
1 8XZC GLN A 35  ? UNP Q8IYS1 ?   ?   'expression tag'        17  35 
1 8XZC GLY A 36  ? UNP Q8IYS1 ?   ?   'expression tag'        18  36 
1 8XZC SER A 37  ? UNP Q8IYS1 ?   ?   'expression tag'        19  37 
1 8XZC PHE A 332 ? UNP Q8IYS1 TYR 314 'engineered mutation'   314 38 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'       1_555 x,y,z 1.0  0.0 0.0 0.0 0.0 1.0  0.0 0.0 0.0 0.0 1.0  0.0 
2 'point symmetry operation' ?     ?     -1.0 0.0 0.0 0.0 0.0 -1.0 0.0 0.0 0.0 0.0 1.0  0.0 
3 'point symmetry operation' ?     ?     1.0  0.0 0.0 0.0 0.0 -1.0 0.0 0.0 0.0 0.0 -1.0 0.0 
4 'point symmetry operation' ?     ?     -1.0 0.0 0.0 0.0 0.0 1.0  0.0 0.0 0.0 0.0 -1.0 0.0 
# 
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 SER A 37  ? ALA A 52  ? SER A 19  ALA A 34  1 ? 16 
HELX_P HELX_P2  AA2 ALA A 52  ? SER A 65  ? ALA A 34  SER A 47  1 ? 14 
HELX_P HELX_P3  AA3 GLU A 73  ? GLU A 87  ? GLU A 55  GLU A 69  1 ? 15 
HELX_P HELX_P4  AA4 GLY A 143 ? GLY A 164 ? GLY A 125 GLY A 146 1 ? 22 
HELX_P HELX_P5  AA5 GLY A 186 ? ALA A 194 ? GLY A 168 ALA A 176 1 ? 9  
HELX_P HELX_P6  AA6 ASN A 244 ? ARG A 260 ? ASN A 226 ARG A 242 1 ? 17 
HELX_P HELX_P7  AA7 GLN A 261 ? MET A 263 ? GLN A 243 MET A 245 5 ? 3  
HELX_P HELX_P8  AA8 SER A 297 ? GLY A 320 ? SER A 279 GLY A 302 1 ? 24 
HELX_P HELX_P9  AA9 ASN A 338 ? GLY A 353 ? ASN A 320 GLY A 335 1 ? 16 
HELX_P HELX_P10 AB1 ASP A 371 ? PHE A 377 ? ASP A 353 PHE A 359 1 ? 7  
HELX_P HELX_P11 AB2 THR A 396 ? GLY A 404 ? THR A 378 GLY A 386 1 ? 9  
HELX_P HELX_P12 AB3 GLN A 406 ? LYS A 429 ? GLN A 388 LYS A 411 1 ? 24 
HELX_P HELX_P13 AB4 LYS A 429 ? GLU A 447 ? LYS A 411 GLU A 429 1 ? 19 
# 
_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 142 SG  ? ? ? 1_555 D ZN  . ZN ? ? A CYS 124 A ZN  503 1_555 ? ? ? ? ? ? ? 2.273 ? ? 
metalc2 metalc ? ? A CYS 142 SG  ? ? ? 1_555 E ZN  . ZN ? ? A CYS 124 A ZN  504 1_555 ? ? ? ? ? ? ? 2.385 ? ? 
metalc3 metalc ? ? A HIS 144 NE2 ? ? ? 1_555 E ZN  . ZN ? ? A HIS 126 A ZN  504 1_555 ? ? ? ? ? ? ? 2.285 ? ? 
metalc4 metalc ? ? A GLU 183 OE2 ? ? ? 1_555 D ZN  . ZN ? ? A GLU 165 A ZN  503 1_555 ? ? ? ? ? ? ? 1.984 ? ? 
metalc5 metalc ? ? A HIS 207 NE2 ? ? ? 1_555 E ZN  . ZN ? ? A HIS 189 A ZN  504 1_555 ? ? ? ? ? ? ? 2.264 ? ? 
metalc6 metalc ? ? A HIS 395 NE2 ? ? ? 1_555 D ZN  . ZN ? ? A HIS 377 A ZN  503 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc7 metalc ? ? D ZN  .   ZN  ? ? ? 1_555 F HOH . O  ? ? A ZN  503 A HOH 626 1_555 ? ? ? ? ? ? ? 2.343 ? ? 
metalc8 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F HOH . O  ? ? A ZN  504 A HOH 617 1_555 ? ? ? ? ? ? ? 2.218 ? ? 
metalc9 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F HOH . O  ? ? A ZN  504 A HOH 626 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
# 
_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 142 ? A CYS 124 ? 1_555 ZN ? D ZN . ? A ZN 503 ? 1_555 OE2 ? A GLU 183 ? A GLU 165 ? 1_555 111.4 ? 
2  SG  ? A CYS 142 ? A CYS 124 ? 1_555 ZN ? D ZN . ? A ZN 503 ? 1_555 NE2 ? A HIS 395 ? A HIS 377 ? 1_555 88.5  ? 
3  OE2 ? A GLU 183 ? A GLU 165 ? 1_555 ZN ? D ZN . ? A ZN 503 ? 1_555 NE2 ? A HIS 395 ? A HIS 377 ? 1_555 95.5  ? 
4  SG  ? A CYS 142 ? A CYS 124 ? 1_555 ZN ? D ZN . ? A ZN 503 ? 1_555 O   ? F HOH .   ? A HOH 626 ? 1_555 105.3 ? 
5  OE2 ? A GLU 183 ? A GLU 165 ? 1_555 ZN ? D ZN . ? A ZN 503 ? 1_555 O   ? F HOH .   ? A HOH 626 ? 1_555 112.9 ? 
6  NE2 ? A HIS 395 ? A HIS 377 ? 1_555 ZN ? D ZN . ? A ZN 503 ? 1_555 O   ? F HOH .   ? A HOH 626 ? 1_555 139.9 ? 
7  SG  ? A CYS 142 ? A CYS 124 ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 NE2 ? A HIS 144 ? A HIS 126 ? 1_555 94.1  ? 
8  SG  ? A CYS 142 ? A CYS 124 ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 NE2 ? A HIS 207 ? A HIS 189 ? 1_555 88.6  ? 
9  NE2 ? A HIS 144 ? A HIS 126 ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 NE2 ? A HIS 207 ? A HIS 189 ? 1_555 114.2 ? 
10 SG  ? A CYS 142 ? A CYS 124 ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 O   ? F HOH .   ? A HOH 617 ? 1_555 163.2 ? 
11 NE2 ? A HIS 144 ? A HIS 126 ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 O   ? F HOH .   ? A HOH 617 ? 1_555 80.8  ? 
12 NE2 ? A HIS 207 ? A HIS 189 ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 O   ? F HOH .   ? A HOH 617 ? 1_555 79.1  ? 
13 SG  ? A CYS 142 ? A CYS 124 ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 O   ? F HOH .   ? A HOH 626 ? 1_555 112.1 ? 
14 NE2 ? A HIS 144 ? A HIS 126 ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 O   ? F HOH .   ? A HOH 626 ? 1_555 125.0 ? 
15 NE2 ? A HIS 207 ? A HIS 189 ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 O   ? F HOH .   ? A HOH 626 ? 1_555 113.9 ? 
16 O   ? F HOH .   ? A HOH 617 ? 1_555 ZN ? E ZN . ? A ZN 504 ? 1_555 O   ? F HOH .   ? A HOH 626 ? 1_555 83.6  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           88 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            70 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    89 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     71 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -3.03 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 94  ? PRO A 97  ? ALA A 76  PRO A 79  
AA1 2 PHE A 105 ? TRP A 109 ? PHE A 87  TRP A 91  
AA1 3 VAL A 172 ? GLY A 178 ? VAL A 154 GLY A 160 
AA1 4 LEU A 124 ? CYS A 130 ? LEU A 106 CYS A 112 
AA1 5 VAL A 202 ? PHE A 204 ? VAL A 184 PHE A 186 
AA1 6 GLY A 381 ? ILE A 382 ? GLY A 363 ILE A 364 
AA2 1 HIS A 207 ? SER A 209 ? HIS A 189 SER A 191 
AA2 2 TYR A 385 ? HIS A 387 ? TYR A 367 HIS A 369 
AA3 1 ARG A 268 ? ASN A 275 ? ARG A 250 ASN A 257 
AA3 2 TYR A 286 ? ALA A 295 ? TYR A 268 ALA A 277 
AA3 3 ALA A 220 ? TYR A 229 ? ALA A 202 TYR A 211 
AA3 4 THR A 322 ? GLY A 327 ? THR A 304 GLY A 309 
# 
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 GLN A 96  ? N GLN A 78  O ARG A 106 ? O ARG A 88  
AA1 2 3 N ALA A 107 ? N ALA A 89  O VAL A 176 ? O VAL A 158 
AA1 3 4 O VAL A 175 ? O VAL A 157 N LEU A 126 ? N LEU A 108 
AA1 4 5 N GLY A 127 ? N GLY A 109 O VAL A 202 ? O VAL A 184 
AA1 5 6 N VAL A 203 ? N VAL A 185 O ILE A 382 ? O ILE A 364 
AA2 1 2 N SER A 209 ? N SER A 191 O PHE A 386 ? O PHE A 368 
AA3 1 2 N ARG A 268 ? N ARG A 250 O ARG A 294 ? O ARG A 276 
AA3 2 3 O LEU A 289 ? O LEU A 271 N VAL A 226 ? N VAL A 208 
AA3 3 4 N THR A 225 ? N THR A 207 O LYS A 326 ? O LYS A 308 
# 
_pdbx_entry_details.entry_id                   8XZC 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
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 GLN A 82  ? ? 66.15   -55.36  
2 1 GLU A 95  ? ? -171.23 147.50  
3 1 ARG A 97  ? ? 65.07   -52.88  
4 1 ALA A 98  ? ? 72.72   91.57   
5 1 TYR A 114 ? ? -159.81 19.39   
6 1 ALA A 116 ? ? -101.77 -168.18 
7 1 SER A 191 ? A -139.85 -135.27 
8 1 SER A 191 ? B -139.52 -134.54 
9 1 GLU A 429 ? ? -92.61  31.11   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A PO4 502 ? C PO4 . 
2 1 A HOH 657 ? F HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         7.67408003436 
_pdbx_refine_tls.origin_y         21.8270640053 
_pdbx_refine_tls.origin_z         30.0242687056 
_pdbx_refine_tls.T[1][1]          0.291699212214 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.00638647593916 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0197777236864 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.391044265209 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0154891540216 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.388718455902 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.603787822335 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.541734631069 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.33082462673 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.68692789389 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          1.74296694683 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          3.1550647366 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0876085431687 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.252619527073 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.110341878981 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.104343677302 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0282931243184 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0933442467944 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0660357447423 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.103256663936 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0599929071513 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     14 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   F 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    C 
_pdbx_refine_tls_group.end_auth_seq_id     2 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -17 ? A MET 1   
2  1 Y 1 A ALA -16 ? A ALA 2   
3  1 Y 1 A SER -15 ? A SER 3   
4  1 Y 1 A TRP -14 ? A TRP 4   
5  1 Y 1 A SER -13 ? A SER 5   
6  1 Y 1 A HIS -12 ? A HIS 6   
7  1 Y 1 A PRO -11 ? A PRO 7   
8  1 Y 1 A GLN -10 ? A GLN 8   
9  1 Y 1 A PHE -9  ? A PHE 9   
10 1 Y 1 A GLU -8  ? A GLU 10  
11 1 Y 1 A GLY -7  ? A GLY 11  
12 1 Y 1 A GLY -6  ? A GLY 12  
13 1 Y 1 A SER -5  ? A SER 13  
14 1 Y 1 A SER -4  ? A SER 14  
15 1 Y 1 A HIS -3  ? A HIS 15  
16 1 Y 1 A HIS -2  ? A HIS 16  
17 1 Y 1 A HIS -1  ? A HIS 17  
18 1 Y 1 A HIS 0   ? A HIS 18  
19 1 Y 1 A HIS 1   ? A HIS 19  
20 1 Y 1 A HIS 2   ? A HIS 20  
21 1 Y 1 A SER 3   ? A SER 21  
22 1 Y 1 A SER 4   ? A SER 22  
23 1 Y 1 A GLY 5   ? A GLY 23  
24 1 Y 1 A SER 6   ? A SER 24  
25 1 Y 1 A GLY 7   ? A GLY 25  
26 1 Y 1 A GLY 8   ? A GLY 26  
27 1 Y 1 A GLY 9   ? A GLY 27  
28 1 Y 1 A GLY 10  ? A GLY 28  
29 1 Y 1 A GLY 11  ? A GLY 29  
30 1 Y 1 A GLU 12  ? A GLU 30  
31 1 Y 1 A ASN 13  ? A ASN 31  
32 1 Y 1 A SER 100 ? A SER 118 
33 1 Y 1 A ALA 101 ? A ALA 119 
34 1 Y 1 A THR 102 ? A THR 120 
35 1 Y 1 A SER 215 ? A SER 233 
36 1 Y 1 A HIS 216 ? A HIS 234 
37 1 Y 1 A SER 217 ? A SER 235 
38 1 Y 1 A ALA 218 ? A ALA 236 
39 1 Y 1 A SER 219 ? A SER 237 
40 1 Y 1 A SER 340 ? A SER 358 
41 1 Y 1 A GLU 341 ? A GLU 359 
42 1 Y 1 A ASP 342 ? A ASP 360 
43 1 Y 1 A THR 343 ? A THR 361 
44 1 Y 1 A MET 344 ? A MET 362 
45 1 Y 1 A LEU 345 ? A LEU 363 
46 1 Y 1 A ASN 346 ? A ASN 364 
47 1 Y 1 A GLY 347 ? A GLY 365 
48 1 Y 1 A PHE 431 ? A PHE 449 
49 1 Y 1 A VAL 432 ? A VAL 450 
50 1 Y 1 A ASN 433 ? A ASN 451 
51 1 Y 1 A ALA 434 ? A ALA 452 
52 1 Y 1 A VAL 435 ? A VAL 453 
53 1 Y 1 A GLU 436 ? A GLU 454 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
PHE N    N  N N 250 
PHE CA   C  N S 251 
PHE C    C  N N 252 
PHE O    O  N N 253 
PHE CB   C  N N 254 
PHE CG   C  Y N 255 
PHE CD1  C  Y N 256 
PHE CD2  C  Y N 257 
PHE CE1  C  Y N 258 
PHE CE2  C  Y N 259 
PHE CZ   C  Y N 260 
PHE OXT  O  N N 261 
PHE H    H  N N 262 
PHE H2   H  N N 263 
PHE HA   H  N N 264 
PHE HB2  H  N N 265 
PHE HB3  H  N N 266 
PHE HD1  H  N N 267 
PHE HD2  H  N N 268 
PHE HE1  H  N N 269 
PHE HE2  H  N N 270 
PHE HZ   H  N N 271 
PHE HXT  H  N N 272 
PO4 P    P  N N 273 
PO4 O1   O  N N 274 
PO4 O2   O  N N 275 
PO4 O3   O  N N 276 
PO4 O4   O  N N 277 
PRO N    N  N N 278 
PRO CA   C  N S 279 
PRO C    C  N N 280 
PRO O    O  N N 281 
PRO CB   C  N N 282 
PRO CG   C  N N 283 
PRO CD   C  N N 284 
PRO OXT  O  N N 285 
PRO H    H  N N 286 
PRO HA   H  N N 287 
PRO HB2  H  N N 288 
PRO HB3  H  N N 289 
PRO HG2  H  N N 290 
PRO HG3  H  N N 291 
PRO HD2  H  N N 292 
PRO HD3  H  N N 293 
PRO HXT  H  N N 294 
SER N    N  N N 295 
SER CA   C  N S 296 
SER C    C  N N 297 
SER O    O  N N 298 
SER CB   C  N N 299 
SER OG   O  N N 300 
SER OXT  O  N N 301 
SER H    H  N N 302 
SER H2   H  N N 303 
SER HA   H  N N 304 
SER HB2  H  N N 305 
SER HB3  H  N N 306 
SER HG   H  N N 307 
SER HXT  H  N N 308 
THR N    N  N N 309 
THR CA   C  N S 310 
THR C    C  N N 311 
THR O    O  N N 312 
THR CB   C  N R 313 
THR OG1  O  N N 314 
THR CG2  C  N N 315 
THR OXT  O  N N 316 
THR H    H  N N 317 
THR H2   H  N N 318 
THR HA   H  N N 319 
THR HB   H  N N 320 
THR HG1  H  N N 321 
THR HG21 H  N N 322 
THR HG22 H  N N 323 
THR HG23 H  N N 324 
THR HXT  H  N N 325 
TRP N    N  N N 326 
TRP CA   C  N S 327 
TRP C    C  N N 328 
TRP O    O  N N 329 
TRP CB   C  N N 330 
TRP CG   C  Y N 331 
TRP CD1  C  Y N 332 
TRP CD2  C  Y N 333 
TRP NE1  N  Y N 334 
TRP CE2  C  Y N 335 
TRP CE3  C  Y N 336 
TRP CZ2  C  Y N 337 
TRP CZ3  C  Y N 338 
TRP CH2  C  Y N 339 
TRP OXT  O  N N 340 
TRP H    H  N N 341 
TRP H2   H  N N 342 
TRP HA   H  N N 343 
TRP HB2  H  N N 344 
TRP HB3  H  N N 345 
TRP HD1  H  N N 346 
TRP HE1  H  N N 347 
TRP HE3  H  N N 348 
TRP HZ2  H  N N 349 
TRP HZ3  H  N N 350 
TRP HH2  H  N N 351 
TRP HXT  H  N N 352 
TYR N    N  N N 353 
TYR CA   C  N S 354 
TYR C    C  N N 355 
TYR O    O  N N 356 
TYR CB   C  N N 357 
TYR CG   C  Y N 358 
TYR CD1  C  Y N 359 
TYR CD2  C  Y N 360 
TYR CE1  C  Y N 361 
TYR CE2  C  Y N 362 
TYR CZ   C  Y N 363 
TYR OH   O  N N 364 
TYR OXT  O  N N 365 
TYR H    H  N N 366 
TYR H2   H  N N 367 
TYR HA   H  N N 368 
TYR HB2  H  N N 369 
TYR HB3  H  N N 370 
TYR HD1  H  N N 371 
TYR HD2  H  N N 372 
TYR HE1  H  N N 373 
TYR HE2  H  N N 374 
TYR HH   H  N N 375 
TYR HXT  H  N N 376 
VAL N    N  N N 377 
VAL CA   C  N S 378 
VAL C    C  N N 379 
VAL O    O  N N 380 
VAL CB   C  N N 381 
VAL CG1  C  N N 382 
VAL CG2  C  N N 383 
VAL OXT  O  N N 384 
VAL H    H  N N 385 
VAL H2   H  N N 386 
VAL HA   H  N N 387 
VAL HB   H  N N 388 
VAL HG11 H  N N 389 
VAL HG12 H  N N 390 
VAL HG13 H  N N 391 
VAL HG21 H  N N 392 
VAL HG22 H  N N 393 
VAL HG23 H  N N 394 
VAL HXT  H  N N 395 
ZN  ZN   ZN N N 396 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PO4 P   O1   doub N N 260 
PO4 P   O2   sing N N 261 
PO4 P   O3   sing N N 262 
PO4 P   O4   sing N N 263 
PRO N   CA   sing N N 264 
PRO N   CD   sing N N 265 
PRO N   H    sing N N 266 
PRO CA  C    sing N N 267 
PRO CA  CB   sing N N 268 
PRO CA  HA   sing N N 269 
PRO C   O    doub N N 270 
PRO C   OXT  sing N N 271 
PRO CB  CG   sing N N 272 
PRO CB  HB2  sing N N 273 
PRO CB  HB3  sing N N 274 
PRO CG  CD   sing N N 275 
PRO CG  HG2  sing N N 276 
PRO CG  HG3  sing N N 277 
PRO CD  HD2  sing N N 278 
PRO CD  HD3  sing N N 279 
PRO OXT HXT  sing N N 280 
SER N   CA   sing N N 281 
SER N   H    sing N N 282 
SER N   H2   sing N N 283 
SER CA  C    sing N N 284 
SER CA  CB   sing N N 285 
SER CA  HA   sing N N 286 
SER C   O    doub N N 287 
SER C   OXT  sing N N 288 
SER CB  OG   sing N N 289 
SER CB  HB2  sing N N 290 
SER CB  HB3  sing N N 291 
SER OG  HG   sing N N 292 
SER OXT HXT  sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TRP N   CA   sing N N 310 
TRP N   H    sing N N 311 
TRP N   H2   sing N N 312 
TRP CA  C    sing N N 313 
TRP CA  CB   sing N N 314 
TRP CA  HA   sing N N 315 
TRP C   O    doub N N 316 
TRP C   OXT  sing N N 317 
TRP CB  CG   sing N N 318 
TRP CB  HB2  sing N N 319 
TRP CB  HB3  sing N N 320 
TRP CG  CD1  doub Y N 321 
TRP CG  CD2  sing Y N 322 
TRP CD1 NE1  sing Y N 323 
TRP CD1 HD1  sing N N 324 
TRP CD2 CE2  doub Y N 325 
TRP CD2 CE3  sing Y N 326 
TRP NE1 CE2  sing Y N 327 
TRP NE1 HE1  sing N N 328 
TRP CE2 CZ2  sing Y N 329 
TRP CE3 CZ3  doub Y N 330 
TRP CE3 HE3  sing N N 331 
TRP CZ2 CH2  doub Y N 332 
TRP CZ2 HZ2  sing N N 333 
TRP CZ3 CH2  sing Y N 334 
TRP CZ3 HZ3  sing N N 335 
TRP CH2 HH2  sing N N 336 
TRP OXT HXT  sing N N 337 
TYR N   CA   sing N N 338 
TYR N   H    sing N N 339 
TYR N   H2   sing N N 340 
TYR CA  C    sing N N 341 
TYR CA  CB   sing N N 342 
TYR CA  HA   sing N N 343 
TYR C   O    doub N N 344 
TYR C   OXT  sing N N 345 
TYR CB  CG   sing N N 346 
TYR CB  HB2  sing N N 347 
TYR CB  HB3  sing N N 348 
TYR CG  CD1  doub Y N 349 
TYR CG  CD2  sing Y N 350 
TYR CD1 CE1  sing Y N 351 
TYR CD1 HD1  sing N N 352 
TYR CD2 CE2  doub Y N 353 
TYR CD2 HD2  sing N N 354 
TYR CE1 CZ   doub Y N 355 
TYR CE1 HE1  sing N N 356 
TYR CE2 CZ   sing Y N 357 
TYR CE2 HE2  sing N N 358 
TYR CZ  OH   sing N N 359 
TYR OH  HH   sing N N 360 
TYR OXT HXT  sing N N 361 
VAL N   CA   sing N N 362 
VAL N   H    sing N N 363 
VAL N   H2   sing N N 364 
VAL CA  C    sing N N 365 
VAL CA  CB   sing N N 366 
VAL CA  HA   sing N N 367 
VAL C   O    doub N N 368 
VAL C   OXT  sing N N 369 
VAL CB  CG1  sing N N 370 
VAL CB  CG2  sing N N 371 
VAL CB  HB   sing N N 372 
VAL CG1 HG11 sing N N 373 
VAL CG1 HG12 sing N N 374 
VAL CG1 HG13 sing N N 375 
VAL CG2 HG21 sing N N 376 
VAL CG2 HG22 sing N N 377 
VAL CG2 HG23 sing N N 378 
VAL OXT HXT  sing N N 379 
# 
_pdbx_audit_support.funding_organization   'Department of Science & Technology (DST, India)' 
_pdbx_audit_support.country                India 
_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   3RAM 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8XZC 
_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]   0.012510 
_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]   0.008656 
_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]   0.008036 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135  5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LEU A 1 32  ? 5.30497   21.78308 64.92107  1.000 71.15883  ? 14  LEU A N   1 
ATOM   2    C  CA  . LEU A 1 32  ? 4.18940   22.03582 65.82885  1.000 110.97238 ? 14  LEU A CA  1 
ATOM   3    C  C   . LEU A 1 32  ? 4.21913   23.46052 66.37140  1.000 110.93509 ? 14  LEU A C   1 
ATOM   4    O  O   . LEU A 1 32  ? 4.66146   24.38926 65.69276  1.000 109.61442 ? 14  LEU A O   1 
ATOM   5    C  CB  . LEU A 1 32  ? 4.19886   21.03976 66.99527  1.000 86.86186  ? 14  LEU A CB  1 
ATOM   6    C  CG  . LEU A 1 32  ? 4.38642   19.56218 66.64702  1.000 100.24927 ? 14  LEU A CG  1 
ATOM   7    N  N   . TYR A 1 33  ? 3.73657   23.62040 67.60483  1.000 99.04186  ? 15  TYR A N   1 
ATOM   8    C  CA  . TYR A 1 33  ? 3.70625   24.91853 68.27876  1.000 111.40667 ? 15  TYR A CA  1 
ATOM   9    C  C   . TYR A 1 33  ? 5.08225   25.24227 68.86520  1.000 119.00826 ? 15  TYR A C   1 
ATOM   10   O  O   . TYR A 1 33  ? 5.24993   25.48683 70.06082  1.000 113.96472 ? 15  TYR A O   1 
ATOM   11   C  CB  . TYR A 1 33  ? 2.63150   24.93071 69.35960  1.000 102.13731 ? 15  TYR A CB  1 
ATOM   12   C  CG  . TYR A 1 33  ? 1.37308   24.17941 68.99136  1.000 88.45764  ? 15  TYR A CG  1 
ATOM   13   C  CD1 . TYR A 1 33  ? 0.41645   24.75296 68.16294  1.000 90.80775  ? 15  TYR A CD1 1 
ATOM   14   C  CD2 . TYR A 1 33  ? 1.13724   22.90023 69.47676  1.000 88.33409  ? 15  TYR A CD2 1 
ATOM   15   C  CE1 . TYR A 1 33  ? -0.73778  24.07038 67.82224  1.000 92.96931  ? 15  TYR A CE1 1 
ATOM   16   C  CE2 . TYR A 1 33  ? -0.01534  22.20959 69.14196  1.000 93.19451  ? 15  TYR A CE2 1 
ATOM   17   C  CZ  . TYR A 1 33  ? -0.94853  22.79975 68.31469  1.000 92.95445  ? 15  TYR A CZ  1 
ATOM   18   O  OH  . TYR A 1 33  ? -2.09581  22.11825 67.97823  1.000 103.20236 ? 15  TYR A OH  1 
ATOM   19   N  N   . PHE A 1 34  ? 6.08021   25.23690 67.98633  1.000 112.13177 ? 16  PHE A N   1 
ATOM   20   C  CA  . PHE A 1 34  ? 7.46632   25.44261 68.37181  1.000 112.27190 ? 16  PHE A CA  1 
ATOM   21   C  C   . PHE A 1 34  ? 8.04042   26.63244 67.61605  1.000 108.24971 ? 16  PHE A C   1 
ATOM   22   O  O   . PHE A 1 34  ? 7.68270   26.88652 66.46148  1.000 106.75917 ? 16  PHE A O   1 
ATOM   23   C  CB  . PHE A 1 34  ? 8.30447   24.18470 68.10353  1.000 111.00931 ? 16  PHE A CB  1 
ATOM   24   C  CG  . PHE A 1 34  ? 8.02656   23.05728 69.06245  1.000 115.94599 ? 16  PHE A CG  1 
ATOM   25   C  CD1 . PHE A 1 34  ? 6.95421   22.20315 68.85631  1.000 108.86137 ? 16  PHE A CD1 1 
ATOM   26   C  CD2 . PHE A 1 34  ? 8.83205   22.85625 70.17268  1.000 112.10671 ? 16  PHE A CD2 1 
ATOM   27   C  CE1 . PHE A 1 34  ? 6.69334   21.16739 69.73588  1.000 99.51956  ? 16  PHE A CE1 1 
ATOM   28   C  CE2 . PHE A 1 34  ? 8.57521   21.82141 71.05594  1.000 101.96607 ? 16  PHE A CE2 1 
ATOM   29   C  CZ  . PHE A 1 34  ? 7.50485   20.97704 70.83597  1.000 98.03715  ? 16  PHE A CZ  1 
ATOM   30   N  N   . GLN A 1 35  ? 8.93389   27.36184 68.28519  1.000 105.16425 ? 17  GLN A N   1 
ATOM   31   C  CA  . GLN A 1 35  ? 9.54168   28.55888 67.71620  1.000 109.74294 ? 17  GLN A CA  1 
ATOM   32   C  C   . GLN A 1 35  ? 10.27571  28.25156 66.41483  1.000 107.20943 ? 17  GLN A C   1 
ATOM   33   O  O   . GLN A 1 35  ? 11.29215  27.54923 66.41706  1.000 110.86475 ? 17  GLN A O   1 
ATOM   34   C  CB  . GLN A 1 35  ? 10.49807  29.19551 68.72725  1.000 90.27582  ? 17  GLN A CB  1 
ATOM   35   N  N   . GLY A 1 36  ? 9.76199   28.76569 65.30181  1.000 104.93574 ? 18  GLY A N   1 
ATOM   36   C  CA  . GLY A 1 36  ? 10.40643  28.58325 64.01069  1.000 103.21955 ? 18  GLY A CA  1 
ATOM   37   C  C   . GLY A 1 36  ? 10.34294  27.17451 63.45941  1.000 92.80377  ? 18  GLY A C   1 
ATOM   38   O  O   . GLY A 1 36  ? 11.33296  26.68886 62.89784  1.000 92.73024  ? 18  GLY A O   1 
ATOM   39   N  N   . SER A 1 37  ? 9.20433   26.50379 63.60509  1.000 94.82222  ? 19  SER A N   1 
ATOM   40   C  CA  . SER A 1 37  ? 9.06102   25.15816 63.07221  1.000 89.48342  ? 19  SER A CA  1 
ATOM   41   C  C   . SER A 1 37  ? 8.93877   25.19493 61.55365  1.000 77.05540  ? 19  SER A C   1 
ATOM   42   O  O   . SER A 1 37  ? 8.52562   26.19764 60.96441  1.000 75.08117  ? 19  SER A O   1 
ATOM   43   C  CB  . SER A 1 37  ? 7.83616   24.46916 63.67595  1.000 84.05399  ? 19  SER A CB  1 
ATOM   44   N  N   . LEU A 1 38  ? 9.31647   24.08322 60.91689  1.000 68.43128  ? 20  LEU A N   1 
ATOM   45   C  CA  . LEU A 1 38  ? 9.11854   23.96455 59.47618  1.000 71.48356  ? 20  LEU A CA  1 
ATOM   46   C  C   . LEU A 1 38  ? 7.63667   24.02669 59.12963  1.000 74.38341  ? 20  LEU A C   1 
ATOM   47   O  O   . LEU A 1 38  ? 7.25440   24.60069 58.10289  1.000 70.40713  ? 20  LEU A O   1 
ATOM   48   C  CB  . LEU A 1 38  ? 9.74468   22.66628 58.95913  1.000 57.87947  ? 20  LEU A CB  1 
ATOM   49   C  CG  . LEU A 1 38  ? 9.51124   22.26423 57.49783  1.000 74.98520  ? 20  LEU A CG  1 
ATOM   50   C  CD1 . LEU A 1 38  ? 10.13779  23.26889 56.53637  1.000 64.33825  ? 20  LEU A CD1 1 
ATOM   51   C  CD2 . LEU A 1 38  ? 10.04946  20.86174 57.22911  1.000 74.42144  ? 20  LEU A CD2 1 
ATOM   52   N  N   . GLU A 1 39  ? 6.78472   23.44831 59.98165  1.000 62.80656  ? 21  GLU A N   1 
ATOM   53   C  CA  . GLU A 1 39  ? 5.34611   23.55469 59.76809  1.000 73.39834  ? 21  GLU A CA  1 
ATOM   54   C  C   . GLU A 1 39  ? 4.88216   25.00406 59.83186  1.000 70.76861  ? 21  GLU A C   1 
ATOM   55   O  O   . GLU A 1 39  ? 3.93389   25.38546 59.13573  1.000 69.65438  ? 21  GLU A O   1 
ATOM   56   C  CB  . GLU A 1 39  ? 4.59463   22.70809 60.79712  1.000 64.13422  ? 21  GLU A CB  1 
ATOM   57   N  N   . LEU A 1 40  ? 5.54057   25.82766 60.64808  1.000 70.85927  ? 22  LEU A N   1 
ATOM   58   C  CA  . LEU A 1 40  ? 5.15774   27.23178 60.73000  1.000 74.42204  ? 22  LEU A CA  1 
ATOM   59   C  C   . LEU A 1 40  ? 5.62331   28.00165 59.49982  1.000 75.35820  ? 22  LEU A C   1 
ATOM   60   O  O   . LEU A 1 40  ? 4.90138   28.87156 58.99760  1.000 74.84846  ? 22  LEU A O   1 
ATOM   61   C  CB  . LEU A 1 40  ? 5.71862   27.85642 62.00703  1.000 67.83013  ? 22  LEU A CB  1 
ATOM   62   C  CG  . LEU A 1 40  ? 4.96377   27.51051 63.29435  1.000 84.36492  ? 22  LEU A CG  1 
ATOM   63   N  N   . LEU A 1 41  ? 6.82622   27.69875 59.00012  1.000 63.66672  ? 23  LEU A N   1 
ATOM   64   C  CA  . LEU A 1 41  ? 7.28967   28.33408 57.77065  1.000 71.97946  ? 23  LEU A CA  1 
ATOM   65   C  C   . LEU A 1 41  ? 6.40945   27.94866 56.59084  1.000 64.02540  ? 23  LEU A C   1 
ATOM   66   O  O   . LEU A 1 41  ? 6.13118   28.77813 55.71638  1.000 57.51684  ? 23  LEU A O   1 
ATOM   67   C  CB  . LEU A 1 41  ? 8.74329   27.95916 57.48994  1.000 63.17608  ? 23  LEU A CB  1 
ATOM   68   C  CG  . LEU A 1 41  ? 9.76971   28.34368 58.55010  1.000 76.83173  ? 23  LEU A CG  1 
ATOM   69   C  CD1 . LEU A 1 41  ? 11.13170  27.80037 58.16129  1.000 77.45729  ? 23  LEU A CD1 1 
ATOM   70   C  CD2 . LEU A 1 41  ? 9.81509   29.85464 58.72214  1.000 77.83704  ? 23  LEU A CD2 1 
ATOM   71   N  N   . LYS A 1 42  ? 5.96836   26.68877 56.54831  1.000 63.33936  ? 24  LYS A N   1 
ATOM   72   C  CA  . LYS A 1 42  ? 5.05521   26.25207 55.49888  1.000 61.81183  ? 24  LYS A CA  1 
ATOM   73   C  C   . LYS A 1 42  ? 3.74873   27.03278 55.54930  1.000 67.02593  ? 24  LYS A C   1 
ATOM   74   O  O   . LYS A 1 42  ? 3.19325   27.39677 54.50542  1.000 65.57983  ? 24  LYS A O   1 
ATOM   75   C  CB  . LYS A 1 42  ? 4.79698   24.75184 55.62836  1.000 58.08524  ? 24  LYS A CB  1 
ATOM   76   C  CG  . LYS A 1 42  ? 5.98100   23.89793 55.20640  1.000 58.63344  ? 24  LYS A CG  1 
ATOM   77   C  CD  . LYS A 1 42  ? 5.67658   22.41441 55.31983  1.000 58.46954  ? 24  LYS A CD  1 
ATOM   78   C  CE  . LYS A 1 42  ? 6.85338   21.57731 54.83833  1.000 58.65927  ? 24  LYS A CE  1 
ATOM   79   N  NZ  . LYS A 1 42  ? 6.51540   20.12866 54.75665  1.000 59.58332  ? 24  LYS A NZ  1 
ATOM   80   N  N   . LEU A 1 43  ? 3.24769   27.30804 56.75617  1.000 63.70619  ? 25  LEU A N   1 
ATOM   81   C  CA  . LEU A 1 43  ? 2.05082   28.13237 56.88610  1.000 66.98890  ? 25  LEU A CA  1 
ATOM   82   C  C   . LEU A 1 43  ? 2.29942   29.54411 56.37241  1.000 63.04689  ? 25  LEU A C   1 
ATOM   83   O  O   . LEU A 1 43  ? 1.44661   30.12009 55.68620  1.000 63.32097  ? 25  LEU A O   1 
ATOM   84   C  CB  . LEU A 1 43  ? 1.58897   28.17085 58.34347  1.000 64.57673  ? 25  LEU A CB  1 
ATOM   85   C  CG  . LEU A 1 43  ? 0.43980   29.13107 58.66245  1.000 67.58496  ? 25  LEU A CG  1 
ATOM   86   C  CD1 . LEU A 1 43  ? -0.88047  28.59331 58.12397  1.000 56.29187  ? 25  LEU A CD1 1 
ATOM   87   C  CD2 . LEU A 1 43  ? 0.34507   29.37604 60.16085  1.000 63.61628  ? 25  LEU A CD2 1 
ATOM   88   N  N   . ARG A 1 44  ? 3.46225   30.11903 56.69839  1.000 50.46612  ? 26  ARG A N   1 
ATOM   89   C  CA  . ARG A 1 44  ? 3.78818   31.45818 56.21564  1.000 72.07527  ? 26  ARG A CA  1 
ATOM   90   C  C   . ARG A 1 44  ? 3.73776   31.52651 54.69450  1.000 63.39959  ? 26  ARG A C   1 
ATOM   91   O  O   . ARG A 1 44  ? 3.16726   32.46749 54.12929  1.000 61.71970  ? 26  ARG A O   1 
ATOM   92   C  CB  . ARG A 1 44  ? 5.16624   31.88479 56.72349  1.000 67.88532  ? 26  ARG A CB  1 
ATOM   93   C  CG  . ARG A 1 44  ? 5.28601   33.37300 57.01761  1.000 74.44654  ? 26  ARG A CG  1 
ATOM   94   C  CD  . ARG A 1 44  ? 6.57318   33.68680 57.77688  1.000 76.25191  ? 26  ARG A CD  1 
ATOM   95   N  N   . SER A 1 45  ? 4.31187   30.52715 54.01630  1.000 57.17854  ? 27  SER A N   1 
ATOM   96   C  CA  . SER A 1 45  ? 4.32198   30.53027 52.55551  1.000 61.46968  ? 27  SER A CA  1 
ATOM   97   C  C   . SER A 1 45  ? 2.91050   30.44959 51.99149  1.000 59.90293  ? 27  SER A C   1 
ATOM   98   O  O   . SER A 1 45  ? 2.61656   31.05797 50.95697  1.000 57.20365  ? 27  SER A O   1 
ATOM   99   C  CB  . SER A 1 45  ? 5.16837   29.37391 52.02762  1.000 48.10099  ? 27  SER A CB  1 
ATOM   100  O  OG  . SER A 1 45  ? 4.49082   28.13968 52.18274  1.000 55.05565  ? 27  SER A OG  1 
ATOM   101  N  N   . ALA A 1 46  ? 2.02294   29.69859 52.65392  1.000 59.60888  ? 28  ALA A N   1 
ATOM   102  C  CA  . ALA A 1 46  ? 0.63409   29.63168 52.20465  1.000 61.98762  ? 28  ALA A CA  1 
ATOM   103  C  C   . ALA A 1 46  ? -0.08494  30.95337 52.44246  1.000 63.06002  ? 28  ALA A C   1 
ATOM   104  O  O   . ALA A 1 46  ? -0.89853  31.38205 51.61621  1.000 65.38150  ? 28  ALA A O   1 
ATOM   105  C  CB  . ALA A 1 46  ? -0.10133  28.48820 52.90678  1.000 48.38724  ? 28  ALA A CB  1 
ATOM   106  N  N   . GLU A 1 47  ? 0.19799   31.61043 53.56872  1.000 56.30701  ? 29  GLU A N   1 
ATOM   107  C  CA  . GLU A 1 47  ? -0.37357  32.92896 53.81694  1.000 59.81190  ? 29  GLU A CA  1 
ATOM   108  C  C   . GLU A 1 47  ? 0.15519   33.94938 52.81913  1.000 60.65694  ? 29  GLU A C   1 
ATOM   109  O  O   . GLU A 1 47  ? -0.59629  34.80828 52.34228  1.000 64.45552  ? 29  GLU A O   1 
ATOM   110  C  CB  . GLU A 1 47  ? -0.06261  33.37318 55.24471  1.000 55.73346  ? 29  GLU A CB  1 
ATOM   111  C  CG  . GLU A 1 47  ? -0.90588  32.68774 56.30145  1.000 68.72436  ? 29  GLU A CG  1 
ATOM   112  C  CD  . GLU A 1 47  ? -0.41306  32.97089 57.70378  1.000 78.21532  ? 29  GLU A CD  1 
ATOM   113  O  OE1 . GLU A 1 47  ? 0.73457   33.44716 57.84842  1.000 81.30546  ? 29  GLU A OE1 1 
ATOM   114  O  OE2 . GLU A 1 47  ? -1.17599  32.72270 58.65831  1.000 75.48002  ? 29  GLU A OE2 1 
ATOM   115  N  N   A CYS A 1 48  ? 1.44711   33.87302 52.48935  0.573 59.70738  ? 30  CYS A N   1 
ATOM   116  N  N   B CYS A 1 48  ? 1.44953   33.87022 52.49742  0.427 59.78975  ? 30  CYS A N   1 
ATOM   117  C  CA  A CYS A 1 48  ? 2.01680   34.81109 51.52910  0.573 58.55948  ? 30  CYS A CA  1 
ATOM   118  C  CA  B CYS A 1 48  ? 2.04258   34.78693 51.53061  0.427 58.79167  ? 30  CYS A CA  1 
ATOM   119  C  C   A CYS A 1 48  ? 1.43082   34.61383 50.13638  0.573 61.55610  ? 30  CYS A C   1 
ATOM   120  C  C   B CYS A 1 48  ? 1.43399   34.61015 50.14477  0.427 61.28234  ? 30  CYS A C   1 
ATOM   121  O  O   A CYS A 1 48  ? 1.31684   35.57853 49.37181  0.573 61.43964  ? 30  CYS A O   1 
ATOM   122  O  O   B CYS A 1 48  ? 1.30188   35.58449 49.39528  0.427 61.07902  ? 30  CYS A O   1 
ATOM   123  C  CB  A CYS A 1 48  ? 3.53640   34.66708 51.49454  0.573 58.19564  ? 30  CYS A CB  1 
ATOM   124  C  CB  B CYS A 1 48  ? 3.55682   34.57587 51.48841  0.427 58.21420  ? 30  CYS A CB  1 
ATOM   125  S  SG  A CYS A 1 48  ? 4.38277   35.44640 52.89291  0.573 62.10750  ? 30  CYS A SG  1 
ATOM   126  S  SG  B CYS A 1 48  ? 4.44351   35.50708 50.22037  0.427 50.04197  ? 30  CYS A SG  1 
ATOM   127  N  N   . ILE A 1 49  ? 1.04926   33.38236 49.79148  1.000 55.12144  ? 31  ILE A N   1 
ATOM   128  C  CA  . ILE A 1 49  ? 0.43466   33.13872 48.49134  1.000 58.18738  ? 31  ILE A CA  1 
ATOM   129  C  C   . ILE A 1 49  ? -1.01230  33.62623 48.48104  1.000 63.57700  ? 31  ILE A C   1 
ATOM   130  O  O   . ILE A 1 49  ? -1.47722  34.21112 47.49483  1.000 57.19246  ? 31  ILE A O   1 
ATOM   131  C  CB  . ILE A 1 49  ? 0.55080   31.64545 48.13003  1.000 54.98382  ? 31  ILE A CB  1 
ATOM   132  C  CG1 . ILE A 1 49  ? 1.97617   31.33546 47.65915  1.000 51.47510  ? 31  ILE A CG1 1 
ATOM   133  C  CG2 . ILE A 1 49  ? -0.47864  31.25237 47.07376  1.000 53.25393  ? 31  ILE A CG2 1 
ATOM   134  C  CD1 . ILE A 1 49  ? 2.31773   29.86833 47.65085  1.000 46.52418  ? 31  ILE A CD1 1 
ATOM   135  N  N   . ASP A 1 50  ? -1.74242  33.41402 49.58005  1.000 65.30947  ? 32  ASP A N   1 
ATOM   136  C  CA  . ASP A 1 50  ? -3.11657  33.90234 49.65225  1.000 68.33835  ? 32  ASP A CA  1 
ATOM   137  C  C   . ASP A 1 50  ? -3.16754  35.42640 49.60200  1.000 69.83096  ? 32  ASP A C   1 
ATOM   138  O  O   . ASP A 1 50  ? -4.05235  36.00004 48.95550  1.000 71.24645  ? 32  ASP A O   1 
ATOM   139  C  CB  . ASP A 1 50  ? -3.79758  33.38119 50.91958  1.000 61.60061  ? 32  ASP A CB  1 
ATOM   140  C  CG  . ASP A 1 50  ? -4.16686  31.91117 50.82302  1.000 72.69525  ? 32  ASP A CG  1 
ATOM   141  O  OD1 . ASP A 1 50  ? -4.40668  31.42099 49.69586  1.000 68.91605  ? 32  ASP A OD1 1 
ATOM   142  O  OD2 . ASP A 1 50  ? -4.22171  31.24596 51.87881  1.000 74.85460  ? 32  ASP A OD2 1 
ATOM   143  N  N   . GLU A 1 51  ? -2.22427  36.09782 50.27243  1.000 63.16141  ? 33  GLU A N   1 
ATOM   144  C  CA  . GLU A 1 51  ? -2.17301  37.55791 50.23623  1.000 68.01848  ? 33  GLU A CA  1 
ATOM   145  C  C   . GLU A 1 51  ? -1.93277  38.08322 48.82214  1.000 61.01314  ? 33  GLU A C   1 
ATOM   146  O  O   . GLU A 1 51  ? -2.42779  39.15857 48.46506  1.000 65.18788  ? 33  GLU A O   1 
ATOM   147  C  CB  . GLU A 1 51  ? -1.08218  38.06139 51.18837  1.000 63.22221  ? 33  GLU A CB  1 
ATOM   148  C  CG  . GLU A 1 51  ? -0.54611  39.45881 50.87787  1.000 72.83879  ? 33  GLU A CG  1 
ATOM   149  C  CD  . GLU A 1 51  ? 0.75975   39.43108 50.09369  1.000 92.03312  ? 33  GLU A CD  1 
ATOM   150  O  OE1 . GLU A 1 51  ? 1.45121   38.38738 50.10450  1.000 89.90064  ? 33  GLU A OE1 1 
ATOM   151  O  OE2 . GLU A 1 51  ? 1.09231   40.45449 49.45813  1.000 92.56677  ? 33  GLU A OE2 1 
ATOM   152  N  N   . ALA A 1 52  ? -1.18706  37.34577 48.00461  1.000 65.48548  ? 34  ALA A N   1 
ATOM   153  C  CA  . ALA A 1 52  ? -0.86519  37.77155 46.64873  1.000 67.04543  ? 34  ALA A CA  1 
ATOM   154  C  C   . ALA A 1 52  ? -1.83289  37.22494 45.60628  1.000 63.21946  ? 34  ALA A C   1 
ATOM   155  O  O   . ALA A 1 52  ? -1.54944  37.32130 44.40718  1.000 64.38533  ? 34  ALA A O   1 
ATOM   156  C  CB  . ALA A 1 52  ? 0.56345   37.35485 46.29317  1.000 54.05464  ? 34  ALA A CB  1 
ATOM   157  N  N   . ALA A 1 53  ? -2.96459  36.66039 46.03452  1.000 62.13933  ? 35  ALA A N   1 
ATOM   158  C  CA  . ALA A 1 53  ? -3.88496  36.02710 45.09475  1.000 66.84428  ? 35  ALA A CA  1 
ATOM   159  C  C   . ALA A 1 53  ? -4.39452  37.01539 44.05312  1.000 66.81034  ? 35  ALA A C   1 
ATOM   160  O  O   . ALA A 1 53  ? -4.48560  36.68036 42.86515  1.000 68.47467  ? 35  ALA A O   1 
ATOM   161  C  CB  . ALA A 1 53  ? -5.05754  35.40164 45.85062  1.000 64.81227  ? 35  ALA A CB  1 
ATOM   162  N  N   . GLU A 1 54  ? -4.72754  38.23890 44.47782  1.000 61.15953  ? 36  GLU A N   1 
ATOM   163  C  CA  . GLU A 1 54  ? -5.31686  39.21332 43.56183  1.000 66.88148  ? 36  GLU A CA  1 
ATOM   164  C  C   . GLU A 1 54  ? -4.36583  39.54890 42.41634  1.000 68.61217  ? 36  GLU A C   1 
ATOM   165  O  O   . GLU A 1 54  ? -4.73615  39.44958 41.23997  1.000 69.38360  ? 36  GLU A O   1 
ATOM   166  C  CB  . GLU A 1 54  ? -5.71618  40.47793 44.32389  1.000 58.46386  ? 36  GLU A CB  1 
ATOM   167  N  N   . ARG A 1 55  ? -3.12681  39.93618 42.73597  1.000 62.10765  ? 37  ARG A N   1 
ATOM   168  C  CA  . ARG A 1 55  ? -2.19205  40.29920 41.67527  1.000 65.00839  ? 37  ARG A CA  1 
ATOM   169  C  C   . ARG A 1 55  ? -1.68160  39.08428 40.90842  1.000 59.80566  ? 37  ARG A C   1 
ATOM   170  O  O   . ARG A 1 55  ? -1.29897  39.22050 39.74111  1.000 58.80871  ? 37  ARG A O   1 
ATOM   171  C  CB  . ARG A 1 55  ? -1.02248  41.10885 42.24483  1.000 54.91126  ? 37  ARG A CB  1 
ATOM   172  C  CG  . ARG A 1 55  ? -0.07444  40.36888 43.17237  1.000 63.49521  ? 37  ARG A CG  1 
ATOM   173  C  CD  . ARG A 1 55  ? 1.00876   41.32992 43.65619  1.000 59.71993  ? 37  ARG A CD  1 
ATOM   174  N  NE  . ARG A 1 55  ? 2.03495   40.68497 44.46662  1.000 64.53351  ? 37  ARG A NE  1 
ATOM   175  C  CZ  . ARG A 1 55  ? 1.96953   40.54448 45.78428  1.000 75.11115  ? 37  ARG A CZ  1 
ATOM   176  N  NH1 . ARG A 1 55  ? 0.91150   40.94799 46.47212  1.000 61.47930  ? 37  ARG A NH1 1 
ATOM   177  N  NH2 . ARG A 1 55  ? 2.98825   39.98006 46.42784  1.000 62.08339  ? 37  ARG A NH2 1 
ATOM   178  N  N   . LEU A 1 56  ? -1.67705  37.89995 41.52434  1.000 55.17453  ? 38  LEU A N   1 
ATOM   179  C  CA  . LEU A 1 56  ? -1.33165  36.69680 40.77448  1.000 52.63914  ? 38  LEU A CA  1 
ATOM   180  C  C   . LEU A 1 56  ? -2.42553  36.35226 39.77081  1.000 61.28352  ? 38  LEU A C   1 
ATOM   181  O  O   . LEU A 1 56  ? -2.13595  35.90835 38.65199  1.000 47.06712  ? 38  LEU A O   1 
ATOM   182  C  CB  . LEU A 1 56  ? -1.08735  35.53059 41.73174  1.000 47.59852  ? 38  LEU A CB  1 
ATOM   183  C  CG  . LEU A 1 56  ? 0.29149   35.46980 42.39338  1.000 52.47162  ? 38  LEU A CG  1 
ATOM   184  C  CD1 . LEU A 1 56  ? 0.22976   34.62486 43.65793  1.000 47.37986  ? 38  LEU A CD1 1 
ATOM   185  C  CD2 . LEU A 1 56  ? 1.34021   34.92392 41.43011  1.000 47.56523  ? 38  LEU A CD2 1 
ATOM   186  N  N   . GLY A 1 57  ? -3.68991  36.54693 40.15486  1.000 58.00202  ? 39  GLY A N   1 
ATOM   187  C  CA  . GLY A 1 57  ? -4.77061  36.37113 39.20086  1.000 54.76772  ? 39  GLY A CA  1 
ATOM   188  C  C   . GLY A 1 57  ? -4.67654  37.34860 38.04599  1.000 58.42660  ? 39  GLY A C   1 
ATOM   189  O  O   . GLY A 1 57  ? -4.90682  36.98483 36.88906  1.000 59.19842  ? 39  GLY A O   1 
ATOM   190  N  N   . ALA A 1 58  ? -4.32364  38.60212 38.34384  1.000 60.74485  ? 40  ALA A N   1 
ATOM   191  C  CA  . ALA A 1 58  ? -4.11799  39.58573 37.28619  1.000 65.16868  ? 40  ALA A CA  1 
ATOM   192  C  C   . ALA A 1 58  ? -3.01832  39.14280 36.32982  1.000 66.04222  ? 40  ALA A C   1 
ATOM   193  O  O   . ALA A 1 58  ? -3.13227  39.32928 35.11154  1.000 66.16578  ? 40  ALA A O   1 
ATOM   194  C  CB  . ALA A 1 58  ? -3.78460  40.94728 37.89425  1.000 50.71398  ? 40  ALA A CB  1 
ATOM   195  N  N   . LEU A 1 59  ? -1.94868  38.54652 36.86471  1.000 60.46040  ? 41  LEU A N   1 
ATOM   196  C  CA  . LEU A 1 59  ? -0.85990  38.06510 36.02000  1.000 57.61885  ? 41  LEU A CA  1 
ATOM   197  C  C   . LEU A 1 59  ? -1.35084  36.99288 35.05412  1.000 55.53013  ? 41  LEU A C   1 
ATOM   198  O  O   . LEU A 1 59  ? -1.04743  37.03386 33.85584  1.000 52.22535  ? 41  LEU A O   1 
ATOM   199  C  CB  . LEU A 1 59  ? 0.27996   37.53443 36.89356  1.000 53.10397  ? 41  LEU A CB  1 
ATOM   200  C  CG  . LEU A 1 59  ? 1.38917   36.72742 36.21337  1.000 57.13845  ? 41  LEU A CG  1 
ATOM   201  C  CD1 . LEU A 1 59  ? 2.01746   37.51330 35.07241  1.000 52.95387  ? 41  LEU A CD1 1 
ATOM   202  C  CD2 . LEU A 1 59  ? 2.44614   36.32555 37.23336  1.000 56.10888  ? 41  LEU A CD2 1 
ATOM   203  N  N   . SER A 1 60  ? -2.11898  36.02345 35.55940  1.000 58.85424  ? 42  SER A N   1 
ATOM   204  C  CA  . SER A 1 60  ? -2.67139  34.99230 34.68595  1.000 55.49856  ? 42  SER A CA  1 
ATOM   205  C  C   . SER A 1 60  ? -3.60153  35.59817 33.64387  1.000 60.95775  ? 42  SER A C   1 
ATOM   206  O  O   . SER A 1 60  ? -3.56819  35.21055 32.46857  1.000 53.45896  ? 42  SER A O   1 
ATOM   207  C  CB  . SER A 1 60  ? -3.41097  33.94163 35.51389  1.000 51.51904  ? 42  SER A CB  1 
ATOM   208  O  OG  . SER A 1 60  ? -4.32022  33.21181 34.71008  1.000 49.34615  ? 42  SER A OG  1 
ATOM   209  N  N   . ARG A 1 61  ? -4.43107  36.56149 34.05690  1.000 49.93328  ? 43  ARG A N   1 
ATOM   210  C  CA  . ARG A 1 61  ? -5.38087  37.17441 33.13450  1.000 57.76299  ? 43  ARG A CA  1 
ATOM   211  C  C   . ARG A 1 61  ? -4.66599  37.93044 32.02096  1.000 58.55932  ? 43  ARG A C   1 
ATOM   212  O  O   . ARG A 1 61  ? -5.12198  37.93317 30.87262  1.000 60.78606  ? 43  ARG A O   1 
ATOM   213  C  CB  . ARG A 1 61  ? -6.31570  38.10841 33.90317  1.000 57.92030  ? 43  ARG A CB  1 
ATOM   214  C  CG  . ARG A 1 61  ? -7.76449  38.04534 33.47527  1.000 60.38300  ? 43  ARG A CG  1 
ATOM   215  C  CD  . ARG A 1 61  ? -8.63039  38.94811 34.34486  1.000 71.16327  ? 43  ARG A CD  1 
ATOM   216  N  NE  . ARG A 1 61  ? -8.43703  38.68512 35.76753  1.000 80.70138  ? 43  ARG A NE  1 
ATOM   217  C  CZ  . ARG A 1 61  ? -7.85398  39.52010 36.61887  1.000 77.82730  ? 43  ARG A CZ  1 
ATOM   218  N  NH1 . ARG A 1 61  ? -7.42078  40.71072 36.23467  1.000 72.44365  ? 43  ARG A NH1 1 
ATOM   219  N  NH2 . ARG A 1 61  ? -7.70712  39.15342 37.88976  1.000 70.17923  ? 43  ARG A NH2 1 
ATOM   220  N  N   . ALA A 1 62  ? -3.54048  38.57756 32.34117  1.000 62.30416  ? 44  ALA A N   1 
ATOM   221  C  CA  . ALA A 1 62  ? -2.82109  39.35562 31.33695  1.000 57.02543  ? 44  ALA A CA  1 
ATOM   222  C  C   . ALA A 1 62  ? -2.25306  38.45993 30.24299  1.000 59.32302  ? 44  ALA A C   1 
ATOM   223  O  O   . ALA A 1 62  ? -2.25570  38.83045 29.06253  1.000 61.66029  ? 44  ALA A O   1 
ATOM   224  C  CB  . ALA A 1 62  ? -1.70764  40.16655 32.00080  1.000 58.12340  ? 44  ALA A CB  1 
ATOM   225  N  N   . ILE A 1 63  ? -1.76810  37.27659 30.61416  1.000 55.98779  ? 45  ILE A N   1 
ATOM   226  C  CA  . ILE A 1 63  ? -1.20486  36.35863 29.63115  1.000 53.28824  ? 45  ILE A CA  1 
ATOM   227  C  C   . ILE A 1 63  ? -2.30948  35.62091 28.88050  1.000 62.86487  ? 45  ILE A C   1 
ATOM   228  O  O   . ILE A 1 63  ? -2.22766  35.43073 27.66029  1.000 57.30006  ? 45  ILE A O   1 
ATOM   229  C  CB  . ILE A 1 63  ? -0.23292  35.38968 30.32789  1.000 44.88894  ? 45  ILE A CB  1 
ATOM   230  C  CG1 . ILE A 1 63  ? 0.92148   36.17111 30.96379  1.000 55.37645  ? 45  ILE A CG1 1 
ATOM   231  C  CG2 . ILE A 1 63  ? 0.29196   34.35302 29.34952  1.000 46.19066  ? 45  ILE A CG2 1 
ATOM   232  C  CD1 . ILE A 1 63  ? 1.76872   35.35615 31.92515  1.000 45.82056  ? 45  ILE A CD1 1 
ATOM   233  N  N   . TRP A 1 64  ? -3.36176  35.20497 29.59066  1.000 59.58658  ? 46  TRP A N   1 
ATOM   234  C  CA  . TRP A 1 64  ? -4.44824  34.46793 28.95072  1.000 56.39658  ? 46  TRP A CA  1 
ATOM   235  C  C   . TRP A 1 64  ? -5.16078  35.32221 27.90769  1.000 59.11534  ? 46  TRP A C   1 
ATOM   236  O  O   . TRP A 1 64  ? -5.48722  34.83885 26.81573  1.000 52.49568  ? 46  TRP A O   1 
ATOM   237  C  CB  . TRP A 1 64  ? -5.43586  33.97688 30.01367  1.000 58.20345  ? 46  TRP A CB  1 
ATOM   238  C  CG  . TRP A 1 64  ? -6.56511  33.13260 29.48482  1.000 63.44445  ? 46  TRP A CG  1 
ATOM   239  C  CD1 . TRP A 1 64  ? -6.56011  31.77941 29.30137  1.000 55.81838  ? 46  TRP A CD1 1 
ATOM   240  C  CD2 . TRP A 1 64  ? -7.87077  33.58539 29.09163  1.000 48.77439  ? 46  TRP A CD2 1 
ATOM   241  N  NE1 . TRP A 1 64  ? -7.77551  31.36388 28.80898  1.000 62.15093  ? 46  TRP A NE1 1 
ATOM   242  C  CE2 . TRP A 1 64  ? -8.59645  32.45223 28.67067  1.000 52.57154  ? 46  TRP A CE2 1 
ATOM   243  C  CE3 . TRP A 1 64  ? -8.49103  34.83698 29.04884  1.000 52.93496  ? 46  TRP A CE3 1 
ATOM   244  C  CZ2 . TRP A 1 64  ? -9.91204  32.53227 28.21511  1.000 57.63400  ? 46  TRP A CZ2 1 
ATOM   245  C  CZ3 . TRP A 1 64  ? -9.80536  34.91559 28.59545  1.000 61.05757  ? 46  TRP A CZ3 1 
ATOM   246  C  CH2 . TRP A 1 64  ? -10.49812 33.76960 28.18605  1.000 62.04462  ? 46  TRP A CH2 1 
ATOM   247  N  N   . SER A 1 65  ? -5.39753  36.60031 28.21936  1.000 54.84542  ? 47  SER A N   1 
ATOM   248  C  CA  . SER A 1 65  ? -6.18022  37.45661 27.33293  1.000 63.34483  ? 47  SER A CA  1 
ATOM   249  C  C   . SER A 1 65  ? -5.42184  37.85919 26.07345  1.000 68.84400  ? 47  SER A C   1 
ATOM   250  O  O   . SER A 1 65  ? -6.04594  38.33746 25.12104  1.000 70.83707  ? 47  SER A O   1 
ATOM   251  C  CB  . SER A 1 65  ? -6.63172  38.71259 28.07854  1.000 61.88074  ? 47  SER A CB  1 
ATOM   252  O  OG  . SER A 1 65  ? -5.51582  39.43826 28.57010  1.000 70.80452  ? 47  SER A OG  1 
ATOM   253  N  N   . GLN A 1 66  ? -4.10100  37.68570 26.04411  1.000 69.97502  ? 48  GLN A N   1 
ATOM   254  C  CA  . GLN A 1 66  ? -3.27224  38.05609 24.89577  1.000 65.10626  ? 48  GLN A CA  1 
ATOM   255  C  C   . GLN A 1 66  ? -2.39890  36.86803 24.50897  1.000 62.08285  ? 48  GLN A C   1 
ATOM   256  O  O   . GLN A 1 66  ? -1.18500  36.86668 24.74656  1.000 70.04839  ? 48  GLN A O   1 
ATOM   257  C  CB  . GLN A 1 66  ? -2.42482  39.29036 25.21272  1.000 68.40191  ? 48  GLN A CB  1 
ATOM   258  C  CG  . GLN A 1 66  ? -1.95637  40.06682 23.98832  1.000 71.46031  ? 48  GLN A CG  1 
ATOM   259  C  CD  . GLN A 1 66  ? -1.49401  41.47557 24.32701  1.000 77.80951  ? 48  GLN A CD  1 
ATOM   260  O  OE1 . GLN A 1 66  ? -1.88764  42.04525 25.34676  1.000 79.06640  ? 48  GLN A OE1 1 
ATOM   261  N  NE2 . GLN A 1 66  ? -0.64507  42.03964 23.47428  1.000 75.26116  ? 48  GLN A NE2 1 
ATOM   262  N  N   . PRO A 1 67  ? -2.98861  35.83684 23.90189  1.000 60.51826  ? 49  PRO A N   1 
ATOM   263  C  CA  . PRO A 1 67  ? -2.21507  34.62640 23.58022  1.000 51.64499  ? 49  PRO A CA  1 
ATOM   264  C  C   . PRO A 1 67  ? -1.13237  34.91208 22.54648  1.000 61.95843  ? 49  PRO A C   1 
ATOM   265  O  O   . PRO A 1 67  ? -1.37862  35.57469 21.53571  1.000 63.64347  ? 49  PRO A O   1 
ATOM   266  C  CB  . PRO A 1 67  ? -3.27495  33.66042 23.03431  1.000 59.14414  ? 49  PRO A CB  1 
ATOM   267  C  CG  . PRO A 1 67  ? -4.38750  34.54823 22.53814  1.000 50.20256  ? 49  PRO A CG  1 
ATOM   268  C  CD  . PRO A 1 67  ? -4.39051  35.74672 23.45115  1.000 55.05681  ? 49  PRO A CD  1 
ATOM   269  N  N   . GLU A 1 68  ? 0.07289   34.40072 22.80929  1.000 64.55051  ? 50  GLU A N   1 
ATOM   270  C  CA  . GLU A 1 68  ? 1.22480   34.58791 21.93689  1.000 57.89434  ? 50  GLU A CA  1 
ATOM   271  C  C   . GLU A 1 68  ? 1.91229   33.24999 21.69749  1.000 56.80157  ? 50  GLU A C   1 
ATOM   272  O  O   . GLU A 1 68  ? 1.95839   32.39177 22.58312  1.000 57.99133  ? 50  GLU A O   1 
ATOM   273  C  CB  . GLU A 1 68  ? 2.22458   35.59254 22.53247  1.000 60.18917  ? 50  GLU A CB  1 
ATOM   274  C  CG  . GLU A 1 68  ? 1.67911   37.00694 22.66070  1.000 59.36972  ? 50  GLU A CG  1 
ATOM   275  C  CD  . GLU A 1 68  ? 2.62418   37.93568 23.39916  1.000 62.37954  ? 50  GLU A CD  1 
ATOM   276  O  OE1 . GLU A 1 68  ? 3.01203   37.60922 24.54197  1.000 67.24808  ? 50  GLU A OE1 1 
ATOM   277  O  OE2 . GLU A 1 68  ? 2.97301   38.99690 22.83979  1.000 64.83972  ? 50  GLU A OE2 1 
ATOM   278  N  N   . LEU A 1 69  ? 2.45946   33.08754 20.49079  1.000 58.53213  ? 51  LEU A N   1 
ATOM   279  C  CA  . LEU A 1 69  ? 3.03699   31.82533 20.05491  1.000 57.56603  ? 51  LEU A CA  1 
ATOM   280  C  C   . LEU A 1 69  ? 4.52394   31.74632 20.40847  1.000 57.19025  ? 51  LEU A C   1 
ATOM   281  O  O   . LEU A 1 69  ? 5.11731   32.68197 20.95129  1.000 57.80050  ? 51  LEU A O   1 
ATOM   282  C  CB  . LEU A 1 69  ? 2.82827   31.63957 18.55333  1.000 61.70836  ? 51  LEU A CB  1 
ATOM   283  C  CG  . LEU A 1 69  ? 1.38844   31.50004 18.05772  1.000 61.62655  ? 51  LEU A CG  1 
ATOM   284  C  CD1 . LEU A 1 69  ? 1.37565   31.23249 16.56036  1.000 60.08539  ? 51  LEU A CD1 1 
ATOM   285  C  CD2 . LEU A 1 69  ? 0.66204   30.39065 18.80742  1.000 59.92310  ? 51  LEU A CD2 1 
ATOM   286  N  N   . ALA A 1 70  ? 5.13176   30.60734 20.07621  1.000 57.19742  ? 52  ALA A N   1 
ATOM   287  C  CA  . ALA A 1 70  ? 6.51704   30.33218 20.43998  1.000 59.45635  ? 52  ALA A CA  1 
ATOM   288  C  C   . ALA A 1 70  ? 7.45600   31.41997 19.92955  1.000 59.85411  ? 52  ALA A C   1 
ATOM   289  O  O   . ALA A 1 70  ? 7.38947   31.81918 18.76269  1.000 67.20481  ? 52  ALA A O   1 
ATOM   290  C  CB  . ALA A 1 70  ? 6.93631   28.97194 19.88479  1.000 51.59743  ? 52  ALA A CB  1 
ATOM   291  N  N   . TYR A 1 71  ? 8.32001   31.90740 20.82553  1.000 49.55223  ? 53  TYR A N   1 
ATOM   292  C  CA  . TYR A 1 71  ? 9.33035   32.92257 20.53522  1.000 60.79607  ? 53  TYR A CA  1 
ATOM   293  C  C   . TYR A 1 71  ? 8.72260   34.27099 20.16976  1.000 60.50611  ? 53  TYR A C   1 
ATOM   294  O  O   . TYR A 1 71  ? 9.45068   35.20975 19.82907  1.000 57.85192  ? 53  TYR A O   1 
ATOM   295  C  CB  . TYR A 1 71  ? 10.27576  32.45401 19.42096  1.000 50.62553  ? 53  TYR A CB  1 
ATOM   296  C  CG  . TYR A 1 71  ? 11.04645  31.19591 19.76305  1.000 54.14525  ? 53  TYR A CG  1 
ATOM   297  C  CD1 . TYR A 1 71  ? 12.03208  31.21281 20.74040  1.000 53.15855  ? 53  TYR A CD1 1 
ATOM   298  C  CD2 . TYR A 1 71  ? 10.79899  29.99841 19.10300  1.000 52.68026  ? 53  TYR A CD2 1 
ATOM   299  C  CE1 . TYR A 1 71  ? 12.74525  30.07341 21.05488  1.000 50.36412  ? 53  TYR A CE1 1 
ATOM   300  C  CE2 . TYR A 1 71  ? 11.50738  28.85084 19.41339  1.000 48.30229  ? 53  TYR A CE2 1 
ATOM   301  C  CZ  . TYR A 1 71  ? 12.47846  28.89613 20.39017  1.000 49.45870  ? 53  TYR A CZ  1 
ATOM   302  O  OH  . TYR A 1 71  ? 13.19008  27.75964 20.70471  1.000 50.28243  ? 53  TYR A OH  1 
ATOM   303  N  N   . GLU A 1 72  ? 7.40068   34.39286 20.25389  1.000 62.78540  ? 54  GLU A N   1 
ATOM   304  C  CA  . GLU A 1 72  ? 6.72317   35.65537 19.99105  1.000 59.98601  ? 54  GLU A CA  1 
ATOM   305  C  C   . GLU A 1 72  ? 6.06170   36.22705 21.23882  1.000 64.83038  ? 54  GLU A C   1 
ATOM   306  O  O   . GLU A 1 72  ? 5.23237   37.13561 21.12904  1.000 62.60823  ? 54  GLU A O   1 
ATOM   307  C  CB  . GLU A 1 72  ? 5.68677   35.47849 18.87767  1.000 66.28698  ? 54  GLU A CB  1 
ATOM   308  C  CG  . GLU A 1 72  ? 6.27185   35.11143 17.52077  1.000 70.26778  ? 54  GLU A CG  1 
ATOM   309  C  CD  . GLU A 1 72  ? 7.35731   36.07438 17.06650  1.000 84.88425  ? 54  GLU A CD  1 
ATOM   310  O  OE1 . GLU A 1 72  ? 7.18386   37.30491 17.22799  1.000 79.80923  ? 54  GLU A OE1 1 
ATOM   311  O  OE2 . GLU A 1 72  ? 8.38601   35.59629 16.54206  1.000 88.58135  ? 54  GLU A OE2 1 
ATOM   312  N  N   . GLU A 1 73  ? 6.41486   35.72452 22.42303  1.000 58.96343  ? 55  GLU A N   1 
ATOM   313  C  CA  . GLU A 1 73  ? 5.75523   36.11463 23.66909  1.000 54.33588  ? 55  GLU A CA  1 
ATOM   314  C  C   . GLU A 1 73  ? 6.34633   37.41350 24.22481  1.000 58.90250  ? 55  GLU A C   1 
ATOM   315  O  O   . GLU A 1 73  ? 6.85035   37.47974 25.34489  1.000 66.16894  ? 55  GLU A O   1 
ATOM   316  C  CB  . GLU A 1 73  ? 5.85179   34.98152 24.68378  1.000 48.20055  ? 55  GLU A CB  1 
ATOM   317  C  CG  . GLU A 1 73  ? 5.70897   33.58719 24.07352  1.000 52.22702  ? 55  GLU A CG  1 
ATOM   318  C  CD  . GLU A 1 73  ? 7.04734   32.95187 23.71463  1.000 52.68709  ? 55  GLU A CD  1 
ATOM   319  O  OE1 . GLU A 1 73  ? 8.04151   33.69092 23.56319  1.000 49.37556  ? 55  GLU A OE1 1 
ATOM   320  O  OE2 . GLU A 1 73  ? 7.10448   31.71002 23.57558  1.000 47.19084  ? 55  GLU A OE2 1 
ATOM   321  N  N   . HIS A 1 74  ? 6.25811   38.47086 23.41565  1.000 58.42424  ? 56  HIS A N   1 
ATOM   322  C  CA  . HIS A 1 74  ? 6.80463   39.75952 23.83139  1.000 66.25289  ? 56  HIS A CA  1 
ATOM   323  C  C   . HIS A 1 74  ? 5.97109   40.38916 24.93951  1.000 72.79048  ? 56  HIS A C   1 
ATOM   324  O  O   . HIS A 1 74  ? 6.52287   40.94274 25.89991  1.000 71.82380  ? 56  HIS A O   1 
ATOM   325  C  CB  . HIS A 1 74  ? 6.90118   40.70199 22.63277  1.000 69.03338  ? 56  HIS A CB  1 
ATOM   326  C  CG  . HIS A 1 74  ? 7.56900   40.09071 21.44224  1.000 71.90588  ? 56  HIS A CG  1 
ATOM   327  N  ND1 . HIS A 1 74  ? 8.93741   39.95669 21.34599  1.000 69.95042  ? 56  HIS A ND1 1 
ATOM   328  C  CD2 . HIS A 1 74  ? 7.05795   39.57089 20.30099  1.000 73.70356  ? 56  HIS A CD2 1 
ATOM   329  C  CE1 . HIS A 1 74  ? 9.24070   39.37951 20.19668  1.000 77.23487  ? 56  HIS A CE1 1 
ATOM   330  N  NE2 . HIS A 1 74  ? 8.11852   39.13617 19.54324  1.000 77.92035  ? 56  HIS A NE2 1 
ATOM   331  N  N   . HIS A 1 75  ? 4.64149   40.31967 24.82553  1.000 66.56781  ? 57  HIS A N   1 
ATOM   332  C  CA  . HIS A 1 75  ? 3.78944   40.91294 25.85184  1.000 71.69979  ? 57  HIS A CA  1 
ATOM   333  C  C   . HIS A 1 75  ? 3.88650   40.14708 27.16602  1.000 62.77880  ? 57  HIS A C   1 
ATOM   334  O  O   . HIS A 1 75  ? 3.97302   40.75568 28.23837  1.000 63.34005  ? 57  HIS A O   1 
ATOM   335  C  CB  . HIS A 1 75  ? 2.33897   40.96808 25.37585  1.000 72.77190  ? 57  HIS A CB  1 
ATOM   336  C  CG  . HIS A 1 75  ? 1.37244   41.35421 26.45127  1.000 71.10959  ? 57  HIS A CG  1 
ATOM   337  N  ND1 . HIS A 1 75  ? 1.24129   42.65010 26.90258  1.000 74.54591  ? 57  HIS A ND1 1 
ATOM   338  C  CD2 . HIS A 1 75  ? 0.50465   40.61218 27.17932  1.000 72.31609  ? 57  HIS A CD2 1 
ATOM   339  C  CE1 . HIS A 1 75  ? 0.32571   42.69179 27.85407  1.000 79.43678  ? 57  HIS A CE1 1 
ATOM   340  N  NE2 . HIS A 1 75  ? -0.13624  41.46842 28.04165  1.000 77.51822  ? 57  HIS A NE2 1 
ATOM   341  N  N   . ALA A 1 76  ? 3.86650   38.81295 27.10511  1.000 56.19726  ? 58  ALA A N   1 
ATOM   342  C  CA  . ALA A 1 76  ? 4.02186   38.01753 28.31949  1.000 57.13297  ? 58  ALA A CA  1 
ATOM   343  C  C   . ALA A 1 76  ? 5.37534   38.26856 28.97386  1.000 57.08959  ? 58  ALA A C   1 
ATOM   344  O  O   . ALA A 1 76  ? 5.48458   38.28951 30.20655  1.000 55.90903  ? 58  ALA A O   1 
ATOM   345  C  CB  . ALA A 1 76  ? 3.84521   36.53274 28.00219  1.000 49.09572  ? 58  ALA A CB  1 
ATOM   346  N  N   . HIS A 1 77  ? 6.41986   38.46362 28.16449  1.000 60.23500  ? 59  HIS A N   1 
ATOM   347  C  CA  . HIS A 1 77  ? 7.73152   38.78712 28.71906  1.000 64.50258  ? 59  HIS A CA  1 
ATOM   348  C  C   . HIS A 1 77  ? 7.70250   40.12292 29.45527  1.000 63.95539  ? 59  HIS A C   1 
ATOM   349  O  O   . HIS A 1 77  ? 8.28895   40.25723 30.53593  1.000 59.82988  ? 59  HIS A O   1 
ATOM   350  C  CB  . HIS A 1 77  ? 8.78420   38.80073 27.60726  1.000 62.66444  ? 59  HIS A CB  1 
ATOM   351  C  CG  . HIS A 1 77  ? 10.11733  39.32332 28.04355  1.000 63.62392  ? 59  HIS A CG  1 
ATOM   352  N  ND1 . HIS A 1 77  ? 10.47195  40.64985 27.92331  1.000 66.55760  ? 59  HIS A ND1 1 
ATOM   353  C  CD2 . HIS A 1 77  ? 11.17856  38.69958 28.60921  1.000 55.12191  ? 59  HIS A CD2 1 
ATOM   354  C  CE1 . HIS A 1 77  ? 11.69578  40.82014 28.39228  1.000 67.34521  ? 59  HIS A CE1 1 
ATOM   355  N  NE2 . HIS A 1 77  ? 12.14629  39.65274 28.81528  1.000 65.16014  ? 59  HIS A NE2 1 
ATOM   356  N  N   . ARG A 1 78  ? 7.01647   41.12113 28.88906  1.000 67.20992  ? 60  ARG A N   1 
ATOM   357  C  CA  . ARG A 1 78  ? 6.88769   42.40946 29.56486  1.000 65.42765  ? 60  ARG A CA  1 
ATOM   358  C  C   . ARG A 1 78  ? 6.11840   42.27050 30.87139  1.000 65.01588  ? 60  ARG A C   1 
ATOM   359  O  O   . ARG A 1 78  ? 6.52928   42.81355 31.90445  1.000 60.52557  ? 60  ARG A O   1 
ATOM   360  C  CB  . ARG A 1 78  ? 6.19569   43.41866 28.64698  1.000 75.47422  ? 60  ARG A CB  1 
ATOM   361  C  CG  . ARG A 1 78  ? 7.13544   44.22627 27.76516  1.000 86.68001  ? 60  ARG A CG  1 
ATOM   362  C  CD  . ARG A 1 78  ? 6.38060   45.28523 26.96478  1.000 84.33869  ? 60  ARG A CD  1 
ATOM   363  N  NE  . ARG A 1 78  ? 5.39719   44.68814 26.06750  1.000 96.15937  ? 60  ARG A NE  1 
ATOM   364  C  CZ  . ARG A 1 78  ? 5.59339   44.47259 24.77291  1.000 87.43258  ? 60  ARG A CZ  1 
ATOM   365  N  NH1 . ARG A 1 78  ? 6.73304   44.79566 24.18241  1.000 90.44590  ? 60  ARG A NH1 1 
ATOM   366  N  NH2 . ARG A 1 78  ? 4.62330   43.91456 24.05319  1.000 78.76436  ? 60  ARG A NH2 1 
ATOM   367  N  N   . VAL A 1 79  ? 5.00283   41.53659 30.84557  1.000 65.28703  ? 61  VAL A N   1 
ATOM   368  C  CA  . VAL A 1 79  ? 4.15874   41.40738 32.03149  1.000 65.56671  ? 61  VAL A CA  1 
ATOM   369  C  C   . VAL A 1 79  ? 4.91357   40.71410 33.15913  1.000 62.38617  ? 61  VAL A C   1 
ATOM   370  O  O   . VAL A 1 79  ? 4.85906   41.14229 34.31905  1.000 61.94232  ? 61  VAL A O   1 
ATOM   371  C  CB  . VAL A 1 79  ? 2.85784   40.66116 31.67883  1.000 64.37876  ? 61  VAL A CB  1 
ATOM   372  C  CG1 . VAL A 1 79  ? 2.03745   40.40458 32.92941  1.000 62.64902  ? 61  VAL A CG1 1 
ATOM   373  C  CG2 . VAL A 1 79  ? 2.04853   41.45793 30.66888  1.000 66.62109  ? 61  VAL A CG2 1 
ATOM   374  N  N   . LEU A 1 80  ? 5.63853   39.64145 32.83840  1.000 59.62762  ? 62  LEU A N   1 
ATOM   375  C  CA  . LEU A 1 80  ? 6.30678   38.87067 33.88140  1.000 58.84259  ? 62  LEU A CA  1 
ATOM   376  C  C   . LEU A 1 80  ? 7.52010   39.60936 34.43691  1.000 58.64732  ? 62  LEU A C   1 
ATOM   377  O  O   . LEU A 1 80  ? 7.77047   39.57115 35.64754  1.000 54.25265  ? 62  LEU A O   1 
ATOM   378  C  CB  . LEU A 1 80  ? 6.70579   37.49872 33.34105  1.000 56.32036  ? 62  LEU A CB  1 
ATOM   379  C  CG  . LEU A 1 80  ? 5.57746   36.46861 33.33451  1.000 54.71336  ? 62  LEU A CG  1 
ATOM   380  C  CD1 . LEU A 1 80  ? 5.88416   35.35345 32.35275  1.000 47.65325  ? 62  LEU A CD1 1 
ATOM   381  C  CD2 . LEU A 1 80  ? 5.36111   35.91210 34.73070  1.000 53.44349  ? 62  LEU A CD2 1 
ATOM   382  N  N   . THR A 1 81  ? 8.29175   40.27871 33.57420  1.000 54.08501  ? 63  THR A N   1 
ATOM   383  C  CA  . THR A 1 81  ? 9.42720   41.05579 34.06571  1.000 55.67789  ? 63  THR A CA  1 
ATOM   384  C  C   . THR A 1 81  ? 8.95858   42.21049 34.93997  1.000 60.63021  ? 63  THR A C   1 
ATOM   385  O  O   . THR A 1 81  ? 9.55553   42.48873 35.98693  1.000 65.20494  ? 63  THR A O   1 
ATOM   386  C  CB  . THR A 1 81  ? 10.27371  41.57850 32.90141  1.000 60.20724  ? 63  THR A CB  1 
ATOM   387  O  OG1 . THR A 1 81  ? 9.42712   42.17506 31.91013  1.000 66.22666  ? 63  THR A OG1 1 
ATOM   388  C  CG2 . THR A 1 81  ? 11.06125  40.44781 32.26667  1.000 49.10441  ? 63  THR A CG2 1 
ATOM   389  N  N   . HIS A 1 82  ? 7.88066   42.88679 34.53387  1.000 68.47730  ? 64  HIS A N   1 
ATOM   390  C  CA  . HIS A 1 82  ? 7.32897   43.95702 35.35772  1.000 74.11365  ? 64  HIS A CA  1 
ATOM   391  C  C   . HIS A 1 82  ? 6.77694   43.42393 36.67359  1.000 70.74537  ? 64  HIS A C   1 
ATOM   392  O  O   . HIS A 1 82  ? 6.82601   44.12411 37.69211  1.000 67.37460  ? 64  HIS A O   1 
ATOM   393  C  CB  . HIS A 1 82  ? 6.23754   44.70532 34.59068  1.000 72.65647  ? 64  HIS A CB  1 
ATOM   394  C  CG  . HIS A 1 82  ? 6.76049   45.57486 33.48899  1.000 87.18145  ? 64  HIS A CG  1 
ATOM   395  N  ND1 . HIS A 1 82  ? 6.00726   45.91006 32.38432  1.000 86.68712  ? 64  HIS A ND1 1 
ATOM   396  C  CD2 . HIS A 1 82  ? 7.96107   46.17918 33.32240  1.000 91.32686  ? 64  HIS A CD2 1 
ATOM   397  C  CE1 . HIS A 1 82  ? 6.72141   46.68114 31.58389  1.000 88.04582  ? 64  HIS A CE1 1 
ATOM   398  N  NE2 . HIS A 1 82  ? 7.91066   46.86003 32.12994  1.000 90.79121  ? 64  HIS A NE2 1 
ATOM   399  N  N   . PHE A 1 83  ? 6.25268   42.19494 36.67317  1.000 62.59732  ? 65  PHE A N   1 
ATOM   400  C  CA  . PHE A 1 83  ? 5.70299   41.61739 37.89751  1.000 58.71675  ? 65  PHE A CA  1 
ATOM   401  C  C   . PHE A 1 83  ? 6.77424   41.49147 38.97438  1.000 60.54470  ? 65  PHE A C   1 
ATOM   402  O  O   . PHE A 1 83  ? 6.57158   41.90725 40.12173  1.000 59.97244  ? 65  PHE A O   1 
ATOM   403  C  CB  . PHE A 1 83  ? 5.07284   40.25428 37.59755  1.000 52.31491  ? 65  PHE A CB  1 
ATOM   404  C  CG  . PHE A 1 83  ? 4.37442   39.63217 38.77585  1.000 55.78537  ? 65  PHE A CG  1 
ATOM   405  C  CD1 . PHE A 1 83  ? 5.06110   38.81251 39.65874  1.000 56.51943  ? 65  PHE A CD1 1 
ATOM   406  C  CD2 . PHE A 1 83  ? 3.02824   39.86880 39.00158  1.000 60.86781  ? 65  PHE A CD2 1 
ATOM   407  C  CE1 . PHE A 1 83  ? 4.41687   38.24127 40.74260  1.000 61.32197  ? 65  PHE A CE1 1 
ATOM   408  C  CE2 . PHE A 1 83  ? 2.37830   39.30250 40.08468  1.000 56.83667  ? 65  PHE A CE2 1 
ATOM   409  C  CZ  . PHE A 1 83  ? 3.07420   38.48774 40.95640  1.000 56.13317  ? 65  PHE A CZ  1 
ATOM   410  N  N   . PHE A 1 84  ? 7.92866   40.92226 38.62192  1.000 58.60817  ? 66  PHE A N   1 
ATOM   411  C  CA  . PHE A 1 84  ? 8.98761   40.73946 39.60549  1.000 66.30408  ? 66  PHE A CA  1 
ATOM   412  C  C   . PHE A 1 84  ? 9.71910   42.03575 39.92437  1.000 62.09953  ? 66  PHE A C   1 
ATOM   413  O  O   . PHE A 1 84  ? 10.28951  42.15544 41.01400  1.000 61.00526  ? 66  PHE A O   1 
ATOM   414  C  CB  . PHE A 1 84  ? 9.97173   39.66785 39.12668  1.000 55.43925  ? 66  PHE A CB  1 
ATOM   415  C  CG  . PHE A 1 84  ? 9.44816   38.26620 39.28109  1.000 57.68092  ? 66  PHE A CG  1 
ATOM   416  C  CD1 . PHE A 1 84  ? 9.47722   37.63494 40.51684  1.000 55.94025  ? 66  PHE A CD1 1 
ATOM   417  C  CD2 . PHE A 1 84  ? 8.90710   37.58808 38.19932  1.000 51.40149  ? 66  PHE A CD2 1 
ATOM   418  C  CE1 . PHE A 1 84  ? 8.98397   36.35075 40.66957  1.000 55.02508  ? 66  PHE A CE1 1 
ATOM   419  C  CE2 . PHE A 1 84  ? 8.41104   36.30088 38.34517  1.000 53.04127  ? 66  PHE A CE2 1 
ATOM   420  C  CZ  . PHE A 1 84  ? 8.45125   35.68194 39.58210  1.000 51.48865  ? 66  PHE A CZ  1 
ATOM   421  N  N   . GLU A 1 85  ? 9.69837   43.01134 39.01268  1.000 65.01554  ? 67  GLU A N   1 
ATOM   422  C  CA  . GLU A 1 85  ? 10.28920  44.31152 39.31068  1.000 67.91422  ? 67  GLU A CA  1 
ATOM   423  C  C   . GLU A 1 85  ? 9.43653   45.10146 40.29676  1.000 74.58938  ? 67  GLU A C   1 
ATOM   424  O  O   . GLU A 1 85  ? 9.96825   45.91937 41.05642  1.000 76.00437  ? 67  GLU A O   1 
ATOM   425  C  CB  . GLU A 1 85  ? 10.48737  45.10823 38.01916  1.000 62.38306  ? 67  GLU A CB  1 
ATOM   426  C  CG  . GLU A 1 85  ? 11.88677  44.98934 37.42524  1.000 73.20759  ? 67  GLU A CG  1 
ATOM   427  C  CD  . GLU A 1 85  ? 11.90153  45.14190 35.91183  1.000 84.56423  ? 67  GLU A CD  1 
ATOM   428  O  OE1 . GLU A 1 85  ? 10.87040  45.56483 35.34329  1.000 83.35454  ? 67  GLU A OE1 1 
ATOM   429  O  OE2 . GLU A 1 85  ? 12.94294  44.83112 35.28990  1.000 75.74616  ? 67  GLU A OE2 1 
ATOM   430  N  N   . ARG A 1 86  ? 8.12413   44.86636 40.31100  1.000 67.13080  ? 68  ARG A N   1 
ATOM   431  C  CA  . ARG A 1 86  ? 7.21641   45.61375 41.17089  1.000 75.29929  ? 68  ARG A CA  1 
ATOM   432  C  C   . ARG A 1 86  ? 7.01175   44.96909 42.53696  1.000 75.02548  ? 68  ARG A C   1 
ATOM   433  O  O   . ARG A 1 86  ? 6.41786   45.60251 43.41786  1.000 68.15864  ? 68  ARG A O   1 
ATOM   434  C  CB  . ARG A 1 86  ? 5.85816   45.78808 40.47939  1.000 73.01718  ? 68  ARG A CB  1 
ATOM   435  C  CG  . ARG A 1 86  ? 5.75408   47.04469 39.62728  1.000 89.06197  ? 68  ARG A CG  1 
ATOM   436  C  CD  . ARG A 1 86  ? 4.74007   46.88001 38.49959  1.000 105.22661 ? 68  ARG A CD  1 
ATOM   437  N  NE  . ARG A 1 86  ? 5.07210   47.69948 37.33819  1.000 107.25365 ? 68  ARG A NE  1 
ATOM   438  C  CZ  . ARG A 1 86  ? 4.46085   47.62157 36.16317  1.000 101.08963 ? 68  ARG A CZ  1 
ATOM   439  N  NH1 . ARG A 1 86  ? 3.46885   46.77100 35.95492  1.000 102.12371 ? 68  ARG A NH1 1 
ATOM   440  N  NH2 . ARG A 1 86  ? 4.85308   48.41905 35.17270  1.000 95.03457  ? 68  ARG A NH2 1 
ATOM   441  N  N   . GLU A 1 87  ? 7.47905   43.73978 42.73347  1.000 69.58509  ? 69  GLU A N   1 
ATOM   442  C  CA  . GLU A 1 87  ? 7.34269   43.09095 44.02950  1.000 67.94377  ? 69  GLU A CA  1 
ATOM   443  C  C   . GLU A 1 87  ? 8.09275   43.89670 45.08714  1.000 71.80987  ? 69  GLU A C   1 
ATOM   444  O  O   . GLU A 1 87  ? 9.27914   44.19959 44.90203  1.000 71.76335  ? 69  GLU A O   1 
ATOM   445  C  CB  . GLU A 1 87  ? 7.87667   41.65990 43.97183  1.000 57.85906  ? 69  GLU A CB  1 
ATOM   446  C  CG  . GLU A 1 87  ? 6.94070   40.67011 43.28671  1.000 63.37110  ? 69  GLU A CG  1 
ATOM   447  C  CD  . GLU A 1 87  ? 5.64121   40.45475 44.05132  1.000 67.78608  ? 69  GLU A CD  1 
ATOM   448  O  OE1 . GLU A 1 87  ? 5.70694   40.10998 45.24962  1.000 61.01054  ? 69  GLU A OE1 1 
ATOM   449  O  OE2 . GLU A 1 87  ? 4.55428   40.62649 43.45550  1.000 62.64620  ? 69  GLU A OE2 1 
ATOM   450  N  N   . PRO A 1 88  ? 7.45020   44.26072 46.19268  1.000 77.30305  ? 70  PRO A N   1 
ATOM   451  C  CA  . PRO A 1 88  ? 8.08351   45.16192 47.16660  1.000 72.18228  ? 70  PRO A CA  1 
ATOM   452  C  C   . PRO A 1 88  ? 9.06899   44.41697 48.04827  1.000 70.98986  ? 70  PRO A C   1 
ATOM   453  O  O   . PRO A 1 88  ? 8.82880   43.25920 48.42340  1.000 71.85529  ? 70  PRO A O   1 
ATOM   454  C  CB  . PRO A 1 88  ? 6.89850   45.69844 47.98695  1.000 62.38758  ? 70  PRO A CB  1 
ATOM   455  C  CG  . PRO A 1 88  ? 5.65971   45.00633 47.45678  1.000 72.61683  ? 70  PRO A CG  1 
ATOM   456  C  CD  . PRO A 1 88  ? 6.09023   43.86999 46.59046  1.000 70.27217  ? 70  PRO A CD  1 
ATOM   457  N  N   . PRO A 1 89  ? 10.20004  45.04707 48.40422  1.000 72.43225  ? 71  PRO A N   1 
ATOM   458  C  CA  . PRO A 1 89  ? 10.65767  46.38590 47.99413  1.000 74.05596  ? 71  PRO A CA  1 
ATOM   459  C  C   . PRO A 1 89  ? 11.09118  46.40358 46.53447  1.000 81.76427  ? 71  PRO A C   1 
ATOM   460  O  O   . PRO A 1 89  ? 11.49312  45.37392 46.00318  1.000 75.88222  ? 71  PRO A O   1 
ATOM   461  C  CB  . PRO A 1 89  ? 11.84230  46.66324 48.93927  1.000 72.63763  ? 71  PRO A CB  1 
ATOM   462  C  CG  . PRO A 1 89  ? 11.73277  45.64620 50.04752  1.000 78.39275  ? 71  PRO A CG  1 
ATOM   463  C  CD  . PRO A 1 89  ? 11.10272  44.45224 49.40129  1.000 76.20608  ? 71  PRO A CD  1 
ATOM   464  N  N   . ALA A 1 90  ? 11.01962  47.55463 45.86920  1.000 87.52950  ? 72  ALA A N   1 
ATOM   465  C  CA  . ALA A 1 90  ? 11.37814  47.62665 44.45972  1.000 89.29189  ? 72  ALA A CA  1 
ATOM   466  C  C   . ALA A 1 90  ? 12.81429  47.16584 44.24439  1.000 88.27435  ? 72  ALA A C   1 
ATOM   467  O  O   . ALA A 1 90  ? 13.71285  47.47887 45.03249  1.000 83.48906  ? 72  ALA A O   1 
ATOM   468  C  CB  . ALA A 1 90  ? 11.19616  49.05163 43.93672  1.000 100.22434 ? 72  ALA A CB  1 
ATOM   469  N  N   . ALA A 1 91  ? 13.01444  46.39475 43.17681  1.000 87.19029  ? 73  ALA A N   1 
ATOM   470  C  CA  . ALA A 1 91  ? 14.29831  45.82537 42.77839  1.000 81.63746  ? 73  ALA A CA  1 
ATOM   471  C  C   . ALA A 1 91  ? 14.85087  44.82075 43.78582  1.000 73.39344  ? 73  ALA A C   1 
ATOM   472  O  O   . ALA A 1 91  ? 16.01127  44.41023 43.66243  1.000 73.94612  ? 73  ALA A O   1 
ATOM   473  C  CB  . ALA A 1 91  ? 15.34276  46.91692 42.50630  1.000 79.62600  ? 73  ALA A CB  1 
ATOM   474  N  N   . SER A 1 92  ? 14.05601  44.39801 44.77669  1.000 71.82547  ? 74  SER A N   1 
ATOM   475  C  CA  . SER A 1 92  ? 14.51217  43.32476 45.65551  1.000 56.84171  ? 74  SER A CA  1 
ATOM   476  C  C   . SER A 1 92  ? 14.63446  42.00849 44.89731  1.000 63.30201  ? 74  SER A C   1 
ATOM   477  O  O   . SER A 1 92  ? 15.47205  41.16968 45.24630  1.000 69.79074  ? 74  SER A O   1 
ATOM   478  C  CB  . SER A 1 92  ? 13.58072  43.17223 46.86100  1.000 64.10034  ? 74  SER A CB  1 
ATOM   479  O  OG  . SER A 1 92  ? 12.24955  42.89630 46.47025  1.000 70.37473  ? 74  SER A OG  1 
ATOM   480  N  N   . TRP A 1 93  ? 13.82106  41.81099 43.86246  1.000 59.07047  ? 75  TRP A N   1 
ATOM   481  C  CA  . TRP A 1 93  ? 14.06494  40.76348 42.87835  1.000 53.77406  ? 75  TRP A CA  1 
ATOM   482  C  C   . TRP A 1 93  ? 15.01103  41.30834 41.81525  1.000 63.03660  ? 75  TRP A C   1 
ATOM   483  O  O   . TRP A 1 93  ? 14.73921  42.35124 41.20920  1.000 64.94111  ? 75  TRP A O   1 
ATOM   484  C  CB  . TRP A 1 93  ? 12.76171  40.29431 42.22592  1.000 54.82618  ? 75  TRP A CB  1 
ATOM   485  C  CG  . TRP A 1 93  ? 11.91094  39.39318 43.08067  1.000 57.11103  ? 75  TRP A CG  1 
ATOM   486  C  CD1 . TRP A 1 93  ? 10.86150  39.76813 43.86038  1.000 51.63428  ? 75  TRP A CD1 1 
ATOM   487  C  CD2 . TRP A 1 93  ? 12.02959  37.96915 43.22651  1.000 56.51006  ? 75  TRP A CD2 1 
ATOM   488  N  NE1 . TRP A 1 93  ? 10.32079  38.67353 44.48967  1.000 56.88410  ? 75  TRP A NE1 1 
ATOM   489  C  CE2 . TRP A 1 93  ? 11.02077  37.55683 44.11843  1.000 54.61430  ? 75  TRP A CE2 1 
ATOM   490  C  CE3 . TRP A 1 93  ? 12.89031  37.00511 42.69079  1.000 55.32314  ? 75  TRP A CE3 1 
ATOM   491  C  CZ2 . TRP A 1 93  ? 10.84755  36.22269 44.48825  1.000 57.01126  ? 75  TRP A CZ2 1 
ATOM   492  C  CZ3 . TRP A 1 93  ? 12.71814  35.68080 43.06112  1.000 53.54854  ? 75  TRP A CZ3 1 
ATOM   493  C  CH2 . TRP A 1 93  ? 11.70557  35.30297 43.95238  1.000 57.29135  ? 75  TRP A CH2 1 
ATOM   494  N  N   . ALA A 1 94  ? 16.12386  40.61278 41.59877  1.000 52.98178  ? 76  ALA A N   1 
ATOM   495  C  CA  . ALA A 1 94  ? 17.07760  41.00305 40.56525  1.000 56.81598  ? 76  ALA A CA  1 
ATOM   496  C  C   . ALA A 1 94  ? 16.60495  40.43040 39.23429  1.000 58.29493  ? 76  ALA A C   1 
ATOM   497  O  O   . ALA A 1 94  ? 16.72963  39.22665 38.98823  1.000 63.33898  ? 76  ALA A O   1 
ATOM   498  C  CB  . ALA A 1 94  ? 18.47874  40.51393 40.91837  1.000 55.22699  ? 76  ALA A CB  1 
ATOM   499  N  N   . VAL A 1 95  ? 16.06375  41.28807 38.37174  1.000 51.93045  ? 77  VAL A N   1 
ATOM   500  C  CA  . VAL A 1 95  ? 15.41974  40.85987 37.13679  1.000 47.62987  ? 77  VAL A CA  1 
ATOM   501  C  C   . VAL A 1 95  ? 16.36214  41.09952 35.96938  1.000 59.56100  ? 77  VAL A C   1 
ATOM   502  O  O   . VAL A 1 95  ? 16.90617  42.19989 35.81440  1.000 65.76848  ? 77  VAL A O   1 
ATOM   503  C  CB  . VAL A 1 95  ? 14.08878  41.59601 36.91920  1.000 54.88965  ? 77  VAL A CB  1 
ATOM   504  C  CG1 . VAL A 1 95  ? 13.36832  41.03273 35.69515  1.000 48.41631  ? 77  VAL A CG1 1 
ATOM   505  C  CG2 . VAL A 1 95  ? 13.22111  41.50477 38.17173  1.000 53.24874  ? 77  VAL A CG2 1 
ATOM   506  N  N   . GLN A 1 96  ? 16.54052  40.07513 35.13923  1.000 61.93685  ? 78  GLN A N   1 
ATOM   507  C  CA  . GLN A 1 96  ? 17.32317  40.17301 33.90756  1.000 57.94142  ? 78  GLN A CA  1 
ATOM   508  C  C   . GLN A 1 96  ? 16.40687  39.90112 32.72458  1.000 57.66635  ? 78  GLN A C   1 
ATOM   509  O  O   . GLN A 1 96  ? 16.12539  38.73078 32.40971  1.000 55.26951  ? 78  GLN A O   1 
ATOM   510  C  CB  . GLN A 1 96  ? 18.49066  39.18626 33.91848  1.000 58.44232  ? 78  GLN A CB  1 
ATOM   511  C  CG  . GLN A 1 96  ? 19.52683  39.46716 34.99308  1.000 67.02140  ? 78  GLN A CG  1 
ATOM   512  C  CD  . GLN A 1 96  ? 20.00066  38.20675 35.69373  1.000 72.48271  ? 78  GLN A CD  1 
ATOM   513  O  OE1 . GLN A 1 96  ? 20.89207  37.51167 35.20731  1.000 63.85898  ? 78  GLN A OE1 1 
ATOM   514  N  NE2 . GLN A 1 96  ? 19.40143  37.90609 36.84557  1.000 73.21053  ? 78  GLN A NE2 1 
ATOM   515  N  N   . PRO A 1 97  ? 15.91545  40.92948 32.04342  1.000 60.31895  ? 79  PRO A N   1 
ATOM   516  C  CA  . PRO A 1 97  ? 15.08789  40.70325 30.85714  1.000 62.13845  ? 79  PRO A CA  1 
ATOM   517  C  C   . PRO A 1 97  ? 15.93061  40.28373 29.66266  1.000 60.42384  ? 79  PRO A C   1 
ATOM   518  O  O   . PRO A 1 97  ? 17.14562  40.48603 29.61810  1.000 66.03065  ? 79  PRO A O   1 
ATOM   519  C  CB  . PRO A 1 97  ? 14.43486  42.06745 30.61629  1.000 66.19101  ? 79  PRO A CB  1 
ATOM   520  C  CG  . PRO A 1 97  ? 15.41342  43.04323 31.17961  1.000 65.45423  ? 79  PRO A CG  1 
ATOM   521  C  CD  . PRO A 1 97  ? 16.08225  42.36214 32.34309  1.000 61.70717  ? 79  PRO A CD  1 
ATOM   522  N  N   . HIS A 1 98  ? 15.24881  39.68368 28.68549  1.000 58.20290  ? 80  HIS A N   1 
ATOM   523  C  CA  . HIS A 1 98  ? 15.87675  39.23244 27.44271  1.000 69.52622  ? 80  HIS A CA  1 
ATOM   524  C  C   . HIS A 1 98  ? 17.04435  38.28727 27.72228  1.000 68.07847  ? 80  HIS A C   1 
ATOM   525  O  O   . HIS A 1 98  ? 18.05321  38.28933 27.01379  1.000 66.42526  ? 80  HIS A O   1 
ATOM   526  C  CB  . HIS A 1 98  ? 16.32436  40.42221 26.58884  1.000 67.46356  ? 80  HIS A CB  1 
ATOM   527  C  CG  . HIS A 1 98  ? 15.27162  41.47461 26.42317  1.000 73.31150  ? 80  HIS A CG  1 
ATOM   528  N  ND1 . HIS A 1 98  ? 14.12130  41.26906 25.69095  1.000 70.19532  ? 80  HIS A ND1 1 
ATOM   529  C  CD2 . HIS A 1 98  ? 15.19203  42.73942 26.90069  1.000 71.36019  ? 80  HIS A CD2 1 
ATOM   530  C  CE1 . HIS A 1 98  ? 13.38002  42.36235 25.72276  1.000 73.19414  ? 80  HIS A CE1 1 
ATOM   531  N  NE2 . HIS A 1 98  ? 14.00692  43.26968 26.45009  1.000 73.36457  ? 80  HIS A NE2 1 
ATOM   532  N  N   . TYR A 1 99  ? 16.90033  37.46960 28.76523  1.000 65.15349  ? 81  TYR A N   1 
ATOM   533  C  CA  . TYR A 1 99  ? 17.94805  36.53939 29.17604  1.000 61.70491  ? 81  TYR A CA  1 
ATOM   534  C  C   . TYR A 1 99  ? 18.12692  35.46241 28.11130  1.000 66.27384  ? 81  TYR A C   1 
ATOM   535  O  O   . TYR A 1 99  ? 17.29332  34.55751 27.98632  1.000 59.27747  ? 81  TYR A O   1 
ATOM   536  C  CB  . TYR A 1 99  ? 17.60016  35.92090 30.52670  1.000 64.76512  ? 81  TYR A CB  1 
ATOM   537  C  CG  . TYR A 1 99  ? 18.67229  35.00498 31.07368  1.000 66.78434  ? 81  TYR A CG  1 
ATOM   538  C  CD1 . TYR A 1 99  ? 18.45978  33.63566 31.16841  1.000 72.28549  ? 81  TYR A CD1 1 
ATOM   539  C  CD2 . TYR A 1 99  ? 19.89700  35.50856 31.49413  1.000 61.72324  ? 81  TYR A CD2 1 
ATOM   540  C  CE1 . TYR A 1 99  ? 19.43663  32.79283 31.66396  1.000 64.64898  ? 81  TYR A CE1 1 
ATOM   541  C  CE2 . TYR A 1 99  ? 20.88003  34.67345 31.99195  1.000 69.09107  ? 81  TYR A CE2 1 
ATOM   542  C  CZ  . TYR A 1 99  ? 20.64322  33.31630 32.07374  1.000 70.80967  ? 81  TYR A CZ  1 
ATOM   543  O  OH  . TYR A 1 99  ? 21.61350  32.47637 32.56921  1.000 88.69660  ? 81  TYR A OH  1 
ATOM   544  N  N   . GLN A 1 100 ? 19.21379  35.56953 27.34048  1.000 58.07057  ? 82  GLN A N   1 
ATOM   545  C  CA  . GLN A 1 100 ? 19.57166  34.62819 26.28095  1.000 60.53675  ? 82  GLN A CA  1 
ATOM   546  C  C   . GLN A 1 100 ? 18.56902  34.65651 25.13129  1.000 61.51138  ? 82  GLN A C   1 
ATOM   547  O  O   . GLN A 1 100 ? 18.95619  34.86125 23.97725  1.000 66.78581  ? 82  GLN A O   1 
ATOM   548  C  CB  . GLN A 1 100 ? 19.71987  33.21001 26.84299  1.000 58.03982  ? 82  GLN A CB  1 
ATOM   549  C  CG  . GLN A 1 100 ? 20.64392  33.12759 28.05892  1.000 72.19024  ? 82  GLN A CG  1 
ATOM   550  C  CD  . GLN A 1 100 ? 22.07258  33.58088 27.76495  1.000 75.75987  ? 82  GLN A CD  1 
ATOM   551  O  OE1 . GLN A 1 100 ? 22.55924  33.47512 26.63534  1.000 82.10883  ? 82  GLN A OE1 1 
ATOM   552  N  NE2 . GLN A 1 100 ? 22.74445  34.09971 28.78496  1.000 70.77710  ? 82  GLN A NE2 1 
ATOM   553  N  N   . LEU A 1 101 ? 17.27866  34.44581 25.42539  1.000 68.82776  ? 83  LEU A N   1 
ATOM   554  C  CA  . LEU A 1 101 ? 16.28049  34.60785 24.38002  1.000 54.56376  ? 83  LEU A CA  1 
ATOM   555  C  C   . LEU A 1 101 ? 15.56963  35.95027 24.52777  1.000 61.09615  ? 83  LEU A C   1 
ATOM   556  O  O   . LEU A 1 101 ? 15.48892  36.49941 25.63209  1.000 59.80504  ? 83  LEU A O   1 
ATOM   557  C  CB  . LEU A 1 101 ? 15.24984  33.47688 24.43124  1.000 53.21911  ? 83  LEU A CB  1 
ATOM   558  C  CG  . LEU A 1 101 ? 15.72491  32.11234 23.93965  1.000 59.82555  ? 83  LEU A CG  1 
ATOM   559  C  CD1 . LEU A 1 101 ? 14.73666  31.02760 24.35140  1.000 53.20506  ? 83  LEU A CD1 1 
ATOM   560  C  CD2 . LEU A 1 101 ? 15.91923  32.12887 22.42867  1.000 50.92698  ? 83  LEU A CD2 1 
ATOM   561  N  N   . PRO A 1 102 ? 15.05502  36.51031 23.42841  1.000 57.97586  ? 84  PRO A N   1 
ATOM   562  C  CA  . PRO A 1 102 ? 14.37041  37.81401 23.52860  1.000 52.18297  ? 84  PRO A CA  1 
ATOM   563  C  C   . PRO A 1 102 ? 13.17884  37.82399 24.47832  1.000 58.54022  ? 84  PRO A C   1 
ATOM   564  O  O   . PRO A 1 102 ? 12.95033  38.83246 25.15896  1.000 57.68100  ? 84  PRO A O   1 
ATOM   565  C  CB  . PRO A 1 102 ? 13.94251  38.08763 22.07953  1.000 59.35975  ? 84  PRO A CB  1 
ATOM   566  C  CG  . PRO A 1 102 ? 14.92373  37.32324 21.24496  1.000 55.53940  ? 84  PRO A CG  1 
ATOM   567  C  CD  . PRO A 1 102 ? 15.24921  36.08497 22.02975  1.000 55.84168  ? 84  PRO A CD  1 
ATOM   568  N  N   . THR A 1 103 ? 12.40473  36.74030 24.54311  1.000 51.43897  ? 85  THR A N   1 
ATOM   569  C  CA  . THR A 1 103 ? 11.23297  36.68316 25.40867  1.000 51.82246  ? 85  THR A CA  1 
ATOM   570  C  C   . THR A 1 103 ? 11.47172  35.89557 26.69110  1.000 58.82168  ? 85  THR A C   1 
ATOM   571  O  O   . THR A 1 103 ? 10.53376  35.72580 27.47744  1.000 52.71619  ? 85  THR A O   1 
ATOM   572  C  CB  . THR A 1 103 ? 10.03805  36.07754 24.66239  1.000 53.83211  ? 85  THR A CB  1 
ATOM   573  O  OG1 . THR A 1 103 ? 10.32566  34.71534 24.32342  1.000 55.44298  ? 85  THR A OG1 1 
ATOM   574  C  CG2 . THR A 1 103 ? 9.73331   36.86535 23.39892  1.000 54.51932  ? 85  THR A CG2 1 
ATOM   575  N  N   . ALA A 1 104 ? 12.68715  35.40555 26.91966  1.000 52.64953  ? 86  ALA A N   1 
ATOM   576  C  CA  . ALA A 1 104 ? 13.01325  34.75102 28.17672  1.000 45.16684  ? 86  ALA A CA  1 
ATOM   577  C  C   . ALA A 1 104 ? 13.47500  35.78249 29.19878  1.000 49.81729  ? 86  ALA A C   1 
ATOM   578  O  O   . ALA A 1 104 ? 13.81485  36.91875 28.86128  1.000 56.60567  ? 86  ALA A O   1 
ATOM   579  C  CB  . ALA A 1 104 ? 14.08920  33.68497 27.97722  1.000 43.90231  ? 86  ALA A CB  1 
ATOM   580  N  N   . PHE A 1 105 ? 13.47411  35.37592 30.46650  1.000 51.73259  ? 87  PHE A N   1 
ATOM   581  C  CA  . PHE A 1 105 ? 13.87989  36.26756 31.54206  1.000 45.58321  ? 87  PHE A CA  1 
ATOM   582  C  C   . PHE A 1 105 ? 14.38208  35.44218 32.71588  1.000 50.26830  ? 87  PHE A C   1 
ATOM   583  O  O   . PHE A 1 105 ? 14.20416  34.22217 32.77009  1.000 48.80391  ? 87  PHE A O   1 
ATOM   584  C  CB  . PHE A 1 105 ? 12.73153  37.19155 31.96623  1.000 49.33549  ? 87  PHE A CB  1 
ATOM   585  C  CG  . PHE A 1 105 ? 11.69073  36.52561 32.82828  1.000 51.37179  ? 87  PHE A CG  1 
ATOM   586  C  CD1 . PHE A 1 105 ? 11.80289  36.53239 34.21514  1.000 50.12423  ? 87  PHE A CD1 1 
ATOM   587  C  CD2 . PHE A 1 105 ? 10.58751  35.91151 32.25481  1.000 48.79228  ? 87  PHE A CD2 1 
ATOM   588  C  CE1 . PHE A 1 105 ? 10.84423  35.92246 35.01022  1.000 49.87199  ? 87  PHE A CE1 1 
ATOM   589  C  CE2 . PHE A 1 105 ? 9.61993   35.30764 33.04456  1.000 50.08409  ? 87  PHE A CE2 1 
ATOM   590  C  CZ  . PHE A 1 105 ? 9.75092   35.30835 34.42314  1.000 47.42310  ? 87  PHE A CZ  1 
ATOM   591  N  N   . ARG A 1 106 ? 15.00522  36.13369 33.66895  1.000 48.57491  ? 88  ARG A N   1 
ATOM   592  C  CA  . ARG A 1 106 ? 15.53966  35.50805 34.87105  1.000 49.98651  ? 88  ARG A CA  1 
ATOM   593  C  C   . ARG A 1 106 ? 15.37690  36.46117 36.04384  1.000 50.40376  ? 88  ARG A C   1 
ATOM   594  O  O   . ARG A 1 106 ? 15.74121  37.63692 35.94586  1.000 51.44376  ? 88  ARG A O   1 
ATOM   595  C  CB  . ARG A 1 106 ? 17.01323  35.13806 34.68670  1.000 55.61277  ? 88  ARG A CB  1 
ATOM   596  C  CG  . ARG A 1 106 ? 17.67634  34.53100 35.90817  1.000 47.37354  ? 88  ARG A CG  1 
ATOM   597  C  CD  . ARG A 1 106 ? 19.08054  34.06053 35.55143  1.000 61.00695  ? 88  ARG A CD  1 
ATOM   598  N  NE  . ARG A 1 106 ? 19.71592  33.27683 36.60432  1.000 68.99647  ? 88  ARG A NE  1 
ATOM   599  C  CZ  . ARG A 1 106 ? 20.74686  32.46594 36.40406  1.000 69.70416  ? 88  ARG A CZ  1 
ATOM   600  N  NH1 . ARG A 1 106 ? 21.27716  32.30771 35.20262  1.000 58.28480  ? 88  ARG A NH1 1 
ATOM   601  N  NH2 . ARG A 1 106 ? 21.25840  31.79737 37.43360  1.000 66.18869  ? 88  ARG A NH2 1 
ATOM   602  N  N   . ALA A 1 107 ? 14.83260  35.95201 37.14691  1.000 45.28120  ? 89  ALA A N   1 
ATOM   603  C  CA  . ALA A 1 107 ? 14.62255  36.72922 38.36024  1.000 47.49223  ? 89  ALA A CA  1 
ATOM   604  C  C   . ALA A 1 107 ? 15.17876  35.95360 39.54314  1.000 51.01661  ? 89  ALA A C   1 
ATOM   605  O  O   . ALA A 1 107 ? 14.93997  34.74767 39.66739  1.000 52.27023  ? 89  ALA A O   1 
ATOM   606  C  CB  . ALA A 1 107 ? 13.12623  37.03810 38.58218  1.000 38.13146  ? 89  ALA A CB  1 
ATOM   607  N  N   . GLU A 1 108 ? 15.91711  36.64639 40.41039  1.000 53.83626  ? 90  GLU A N   1 
ATOM   608  C  CA  . GLU A 1 108 ? 16.60687  36.01688 41.52857  1.000 56.11734  ? 90  GLU A CA  1 
ATOM   609  C  C   . GLU A 1 108 ? 16.38449  36.80697 42.81022  1.000 61.18196  ? 90  GLU A C   1 
ATOM   610  O  O   . GLU A 1 108 ? 16.38687  38.04276 42.80042  1.000 54.65522  ? 90  GLU A O   1 
ATOM   611  C  CB  . GLU A 1 108 ? 18.11285  35.90077 41.26881  1.000 45.54774  ? 90  GLU A CB  1 
ATOM   612  C  CG  . GLU A 1 108 ? 18.49078  35.19763 39.97115  1.000 65.05972  ? 90  GLU A CG  1 
ATOM   613  C  CD  . GLU A 1 108 ? 19.92183  34.68458 39.98859  1.000 72.17102  ? 90  GLU A CD  1 
ATOM   614  O  OE1 . GLU A 1 108 ? 20.72889  35.19593 40.79965  1.000 72.72860  ? 90  GLU A OE1 1 
ATOM   615  O  OE2 . GLU A 1 108 ? 20.23836  33.77156 39.19412  1.000 64.97915  ? 90  GLU A OE2 1 
ATOM   616  N  N   . TRP A 1 109 ? 16.20873  36.08238 43.91469  1.000 52.89965  ? 91  TRP A N   1 
ATOM   617  C  CA  . TRP A 1 109 ? 16.13642  36.68196 45.23675  1.000 55.25191  ? 91  TRP A CA  1 
ATOM   618  C  C   . TRP A 1 109 ? 16.88063  35.81191 46.23762  1.000 56.32598  ? 91  TRP A C   1 
ATOM   619  O  O   . TRP A 1 109 ? 16.86351  34.58114 46.14444  1.000 56.64695  ? 91  TRP A O   1 
ATOM   620  C  CB  . TRP A 1 109 ? 14.69058  36.87190 45.70441  1.000 58.57180  ? 91  TRP A CB  1 
ATOM   621  C  CG  . TRP A 1 109 ? 14.60605  37.42727 47.09366  1.000 58.49256  ? 91  TRP A CG  1 
ATOM   622  C  CD1 . TRP A 1 109 ? 14.54603  38.74423 47.44874  1.000 60.75032  ? 91  TRP A CD1 1 
ATOM   623  C  CD2 . TRP A 1 109 ? 14.59169  36.68090 48.31764  1.000 57.84622  ? 91  TRP A CD2 1 
ATOM   624  N  NE1 . TRP A 1 109 ? 14.48413  38.86250 48.81760  1.000 68.74587  ? 91  TRP A NE1 1 
ATOM   625  C  CE2 . TRP A 1 109 ? 14.51308  37.61045 49.37315  1.000 58.87482  ? 91  TRP A CE2 1 
ATOM   626  C  CE3 . TRP A 1 109 ? 14.63424  35.31709 48.62218  1.000 57.82052  ? 91  TRP A CE3 1 
ATOM   627  C  CZ2 . TRP A 1 109 ? 14.47839  37.22045 50.70668  1.000 60.19323  ? 91  TRP A CZ2 1 
ATOM   628  C  CZ3 . TRP A 1 109 ? 14.59859  34.93288 49.94761  1.000 58.43432  ? 91  TRP A CZ3 1 
ATOM   629  C  CH2 . TRP A 1 109 ? 14.52271  35.87969 50.97264  1.000 58.99700  ? 91  TRP A CH2 1 
ATOM   630  N  N   . GLU A 1 110 ? 17.52104  36.46461 47.19871  1.000 54.17280  ? 92  GLU A N   1 
ATOM   631  C  CA  . GLU A 1 110 ? 18.19805  35.80157 48.30005  1.000 61.79157  ? 92  GLU A CA  1 
ATOM   632  C  C   . GLU A 1 110 ? 18.12568  36.71911 49.50793  1.000 68.12014  ? 92  GLU A C   1 
ATOM   633  O  O   . GLU A 1 110 ? 17.92035  37.93014 49.35833  1.000 69.91903  ? 92  GLU A O   1 
ATOM   634  C  CB  . GLU A 1 110 ? 19.65776  35.48460 47.94996  1.000 59.94480  ? 92  GLU A CB  1 
ATOM   635  C  CG  . GLU A 1 110 ? 20.59913  36.66383 48.12873  1.000 66.28548  ? 92  GLU A CG  1 
ATOM   636  C  CD  . GLU A 1 110 ? 21.79432  36.59649 47.20324  1.000 73.26861  ? 92  GLU A CD  1 
ATOM   637  O  OE1 . GLU A 1 110 ? 22.54506  35.59992 47.27038  1.000 70.51937  ? 92  GLU A OE1 1 
ATOM   638  O  OE2 . GLU A 1 110 ? 21.97665  37.53823 46.40313  1.000 76.46157  ? 92  GLU A OE2 1 
ATOM   639  N  N   . PRO A 1 111 ? 18.25736  36.17751 50.71561  1.000 67.11740  ? 93  PRO A N   1 
ATOM   640  C  CA  . PRO A 1 111 ? 18.37832  37.03537 51.90383  1.000 72.95361  ? 93  PRO A CA  1 
ATOM   641  C  C   . PRO A 1 111 ? 19.61768  37.90757 51.81303  1.000 80.31330  ? 93  PRO A C   1 
ATOM   642  O  O   . PRO A 1 111 ? 20.73526  37.39488 51.64525  1.000 83.64856  ? 93  PRO A O   1 
ATOM   643  C  CB  . PRO A 1 111 ? 18.48861  36.02943 53.05915  1.000 63.74110  ? 93  PRO A CB  1 
ATOM   644  C  CG  . PRO A 1 111 ? 17.85548  34.78235 52.54045  1.000 67.77220  ? 93  PRO A CG  1 
ATOM   645  C  CD  . PRO A 1 111 ? 18.14991  34.75053 51.06693  1.000 62.08772  ? 93  PRO A CD  1 
ATOM   646  N  N   . PRO A 1 112 ? 19.46384  39.23644 51.91118  1.000 99.25142  ? 94  PRO A N   1 
ATOM   647  C  CA  . PRO A 1 112 ? 20.61082  40.17077 51.77510  1.000 104.56751 ? 94  PRO A CA  1 
ATOM   648  C  C   . PRO A 1 112 ? 21.44993  40.34178 53.03994  1.000 98.17286  ? 94  PRO A C   1 
ATOM   649  O  O   . PRO A 1 112 ? 21.40619  41.35975 53.72723  1.000 99.12172  ? 94  PRO A O   1 
ATOM   650  C  CB  . PRO A 1 112 ? 19.92766  41.48584 51.38184  1.000 88.15643  ? 94  PRO A CB  1 
ATOM   651  C  CG  . PRO A 1 112 ? 18.47660  41.12912 51.08209  1.000 86.99449  ? 94  PRO A CG  1 
ATOM   652  C  CD  . PRO A 1 112 ? 18.18725  39.96109 51.95334  1.000 89.96237  ? 94  PRO A CD  1 
ATOM   653  N  N   . GLU A 1 113 ? 22.25662  39.32458 53.33022  1.000 110.33331 ? 95  GLU A N   1 
ATOM   654  C  CA  . GLU A 1 113 ? 23.17945  39.28663 54.46145  1.000 103.69624 ? 95  GLU A CA  1 
ATOM   655  C  C   . GLU A 1 113 ? 24.05844  38.04701 54.29413  1.000 115.72300 ? 95  GLU A C   1 
ATOM   656  O  O   . GLU A 1 113 ? 23.60380  37.03751 53.74948  1.000 124.42646 ? 95  GLU A O   1 
ATOM   657  C  CB  . GLU A 1 113 ? 22.42086  39.28046 55.79899  1.000 103.96968 ? 95  GLU A CB  1 
ATOM   658  C  CG  . GLU A 1 113 ? 22.41249  40.65329 56.48126  1.000 94.75919  ? 95  GLU A CG  1 
ATOM   659  C  CD  . GLU A 1 113 ? 21.60676  40.71398 57.77082  1.000 93.20996  ? 95  GLU A CD  1 
ATOM   660  O  OE1 . GLU A 1 113 ? 21.51422  39.68214 58.46582  1.000 104.09841 ? 95  GLU A OE1 1 
ATOM   661  O  OE2 . GLU A 1 113 ? 21.09961  41.80977 58.11176  1.000 76.42250  ? 95  GLU A OE2 1 
ATOM   662  N  N   . ALA A 1 114 ? 25.32131  38.13346 54.74831  1.000 103.89135 ? 96  ALA A N   1 
ATOM   663  C  CA  . ALA A 1 114 ? 26.38344  37.25893 54.24302  1.000 114.30550 ? 96  ALA A CA  1 
ATOM   664  C  C   . ALA A 1 114 ? 27.05347  36.34038 55.26768  1.000 111.28900 ? 96  ALA A C   1 
ATOM   665  O  O   . ALA A 1 114 ? 27.39625  35.21073 54.91267  1.000 120.87986 ? 96  ALA A O   1 
ATOM   666  C  CB  . ALA A 1 114 ? 27.47588  38.10258 53.56338  1.000 106.82305 ? 96  ALA A CB  1 
ATOM   667  N  N   . ARG A 1 115 ? 27.31393  36.80627 56.49415  1.000 101.76625 ? 97  ARG A N   1 
ATOM   668  C  CA  . ARG A 1 115 ? 27.86343  35.97043 57.56761  1.000 93.09810  ? 97  ARG A CA  1 
ATOM   669  C  C   . ARG A 1 115 ? 29.27930  35.44552 57.31372  1.000 98.72855  ? 97  ARG A C   1 
ATOM   670  O  O   . ARG A 1 115 ? 30.15042  35.58882 58.17929  1.000 100.05515 ? 97  ARG A O   1 
ATOM   671  C  CB  . ARG A 1 115 ? 26.92766  34.79021 57.84764  1.000 105.94301 ? 97  ARG A CB  1 
ATOM   672  N  N   . ALA A 1 116 ? 29.50601  34.79620 56.15955  1.000 118.01128 ? 98  ALA A N   1 
ATOM   673  C  CA  . ALA A 1 116 ? 30.78111  34.22368 55.71255  1.000 126.78104 ? 98  ALA A CA  1 
ATOM   674  C  C   . ALA A 1 116 ? 31.14495  32.96036 56.49007  1.000 131.20811 ? 98  ALA A C   1 
ATOM   675  O  O   . ALA A 1 116 ? 31.80996  33.03939 57.53208  1.000 117.83165 ? 98  ALA A O   1 
ATOM   676  C  CB  . ALA A 1 116 ? 31.91716  35.24736 55.81466  1.000 102.93687 ? 98  ALA A CB  1 
ATOM   677  N  N   . PRO A 1 117 ? 30.75003  31.76998 56.00049  1.000 143.10747 ? 99  PRO A N   1 
ATOM   678  C  CA  . PRO A 1 117 ? 31.02311  30.47817 56.64168  1.000 134.46537 ? 99  PRO A CA  1 
ATOM   679  C  C   . PRO A 1 117 ? 32.42981  29.96139 56.34839  1.000 132.90279 ? 99  PRO A C   1 
ATOM   680  O  O   . PRO A 1 117 ? 32.69307  29.55066 55.21680  1.000 127.44510 ? 99  PRO A O   1 
ATOM   681  C  CB  . PRO A 1 117 ? 29.96400  29.54259 56.02831  1.000 129.60233 ? 99  PRO A CB  1 
ATOM   682  C  CG  . PRO A 1 117 ? 29.17124  30.38565 55.03792  1.000 123.96426 ? 99  PRO A CG  1 
ATOM   683  C  CD  . PRO A 1 117 ? 29.99619  31.59601 54.74991  1.000 137.58027 ? 99  PRO A CD  1 
ATOM   684  N  N   . PRO A 1 121 ? 29.93480  25.64537 52.57539  1.000 107.96111 ? 103 PRO A N   1 
ATOM   685  C  CA  . PRO A 1 121 ? 29.44118  27.02583 52.52375  1.000 109.01823 ? 103 PRO A CA  1 
ATOM   686  C  C   . PRO A 1 121 ? 28.79810  27.38057 51.18305  1.000 115.13908 ? 103 PRO A C   1 
ATOM   687  O  O   . PRO A 1 121 ? 28.77751  28.55495 50.81150  1.000 117.42684 ? 103 PRO A O   1 
ATOM   688  C  CB  . PRO A 1 121 ? 30.70688  27.85638 52.75164  1.000 108.57231 ? 103 PRO A CB  1 
ATOM   689  C  CG  . PRO A 1 121 ? 31.60197  26.96310 53.53624  1.000 110.04776 ? 103 PRO A CG  1 
ATOM   690  C  CD  . PRO A 1 121 ? 31.33296  25.57335 53.03463  1.000 100.82770 ? 103 PRO A CD  1 
ATOM   691  N  N   . ARG A 1 122 ? 28.28235  26.37861 50.46948  1.000 99.35017  ? 104 ARG A N   1 
ATOM   692  C  CA  . ARG A 1 122 ? 27.66249  26.60849 49.16906  1.000 95.52947  ? 104 ARG A CA  1 
ATOM   693  C  C   . ARG A 1 122 ? 26.16595  26.82944 49.34459  1.000 84.38427  ? 104 ARG A C   1 
ATOM   694  O  O   . ARG A 1 122 ? 25.49164  25.97411 49.93480  1.000 81.33450  ? 104 ARG A O   1 
ATOM   695  C  CB  . ARG A 1 122 ? 27.90927  25.43186 48.23891  1.000 82.62279  ? 104 ARG A CB  1 
ATOM   696  N  N   . PRO A 1 123 ? 25.60999  27.93994 48.86704  1.000 73.37376  ? 105 PRO A N   1 
ATOM   697  C  CA  . PRO A 1 123 ? 24.16980  28.16442 49.01785  1.000 70.59998  ? 105 PRO A CA  1 
ATOM   698  C  C   . PRO A 1 123 ? 23.37115  27.21826 48.13558  1.000 66.64984  ? 105 PRO A C   1 
ATOM   699  O  O   . PRO A 1 123 ? 23.85087  26.70601 47.12228  1.000 65.79948  ? 105 PRO A O   1 
ATOM   700  C  CB  . PRO A 1 123 ? 23.97749  29.62282 48.57764  1.000 69.99742  ? 105 PRO A CB  1 
ATOM   701  C  CG  . PRO A 1 123 ? 25.36050  30.20357 48.46906  1.000 76.94544  ? 105 PRO A CG  1 
ATOM   702  C  CD  . PRO A 1 123 ? 26.26982  29.05452 48.17123  1.000 79.18153  ? 105 PRO A CD  1 
ATOM   703  N  N   . LEU A 1 124 ? 22.12967  26.98717 48.54715  1.000 60.39528  ? 106 LEU A N   1 
ATOM   704  C  CA  . LEU A 1 124 ? 21.20384  26.14924 47.80204  1.000 64.25808  ? 106 LEU A CA  1 
ATOM   705  C  C   . LEU A 1 124 ? 20.49918  26.99145 46.74579  1.000 59.00918  ? 106 LEU A C   1 
ATOM   706  O  O   . LEU A 1 124 ? 19.97003  28.06471 47.05524  1.000 60.39944  ? 106 LEU A O   1 
ATOM   707  C  CB  . LEU A 1 124 ? 20.18484  25.51218 48.74875  1.000 61.48635  ? 106 LEU A CB  1 
ATOM   708  C  CG  . LEU A 1 124 ? 19.36698  24.34055 48.20476  1.000 69.94864  ? 106 LEU A CG  1 
ATOM   709  C  CD1 . LEU A 1 124 ? 20.28404  23.22488 47.73851  1.000 62.21304  ? 106 LEU A CD1 1 
ATOM   710  C  CD2 . LEU A 1 124 ? 18.39485  23.83658 49.25935  1.000 69.19234  ? 106 LEU A CD2 1 
ATOM   711  N  N   . HIS A 1 125 ? 20.49983  26.50825 45.50272  1.000 56.97037  ? 107 HIS A N   1 
ATOM   712  C  CA  . HIS A 1 125 ? 19.84524  27.18056 44.38313  1.000 50.73754  ? 107 HIS A CA  1 
ATOM   713  C  C   . HIS A 1 125 ? 18.57104  26.42313 44.02626  1.000 44.08007  ? 107 HIS A C   1 
ATOM   714  O  O   . HIS A 1 125 ? 18.63391  25.25659 43.62268  1.000 54.30164  ? 107 HIS A O   1 
ATOM   715  C  CB  . HIS A 1 125 ? 20.77038  27.25705 43.16779  1.000 53.59434  ? 107 HIS A CB  1 
ATOM   716  C  CG  . HIS A 1 125 ? 21.89746  28.23328 43.31398  1.000 65.80444  ? 107 HIS A CG  1 
ATOM   717  N  ND1 . HIS A 1 125 ? 22.71315  28.27487 44.42571  1.000 66.62554  ? 107 HIS A ND1 1 
ATOM   718  C  CD2 . HIS A 1 125 ? 22.35807  29.19117 42.47436  1.000 57.04770  ? 107 HIS A CD2 1 
ATOM   719  C  CE1 . HIS A 1 125 ? 23.61800  29.22507 44.27001  1.000 65.99256  ? 107 HIS A CE1 1 
ATOM   720  N  NE2 . HIS A 1 125 ? 23.42461  29.79593 43.09456  1.000 57.60503  ? 107 HIS A NE2 1 
ATOM   721  N  N   . LEU A 1 126 ? 17.42422  27.08771 44.15425  1.000 40.63200  ? 108 LEU A N   1 
ATOM   722  C  CA  . LEU A 1 126 ? 16.12220  26.48610 43.88094  1.000 40.87164  ? 108 LEU A CA  1 
ATOM   723  C  C   . LEU A 1 126 ? 15.47673  27.21467 42.71192  1.000 45.33485  ? 108 LEU A C   1 
ATOM   724  O  O   . LEU A 1 126 ? 15.25786  28.43030 42.77942  1.000 47.44746  ? 108 LEU A O   1 
ATOM   725  C  CB  . LEU A 1 126 ? 15.21378  26.54672 45.11338  1.000 47.53034  ? 108 LEU A CB  1 
ATOM   726  C  CG  . LEU A 1 126 ? 15.67361  25.75781 46.34361  1.000 55.91582  ? 108 LEU A CG  1 
ATOM   727  C  CD1 . LEU A 1 126 ? 14.56495  25.69498 47.36447  1.000 53.41962  ? 108 LEU A CD1 1 
ATOM   728  C  CD2 . LEU A 1 126 ? 16.11566  24.35431 45.95633  1.000 58.38985  ? 108 LEU A CD2 1 
ATOM   729  N  N   . GLY A 1 127 ? 15.14861  26.47270 41.66060  1.000 40.09181  ? 109 GLY A N   1 
ATOM   730  C  CA  . GLY A 1 127 ? 14.62769  27.04428 40.42539  1.000 42.45834  ? 109 GLY A CA  1 
ATOM   731  C  C   . GLY A 1 127 ? 13.13568  26.80767 40.27070  1.000 43.33172  ? 109 GLY A C   1 
ATOM   732  O  O   . GLY A 1 127 ? 12.62475  25.74683 40.64095  1.000 40.91746  ? 109 GLY A O   1 
ATOM   733  N  N   . PHE A 1 128 ? 12.44690  27.80879 39.71796  1.000 45.60755  ? 110 PHE A N   1 
ATOM   734  C  CA  . PHE A 1 128 ? 11.03120  27.72897 39.37639  1.000 43.53736  ? 110 PHE A CA  1 
ATOM   735  C  C   . PHE A 1 128 ? 10.85121  28.24634 37.95657  1.000 45.89545  ? 110 PHE A C   1 
ATOM   736  O  O   . PHE A 1 128 ? 11.32845  29.33832 37.63113  1.000 45.62604  ? 110 PHE A O   1 
ATOM   737  C  CB  . PHE A 1 128 ? 10.16549  28.54538 40.34660  1.000 46.73691  ? 110 PHE A CB  1 
ATOM   738  C  CG  . PHE A 1 128 ? 10.30252  28.12899 41.78564  1.000 51.01226  ? 110 PHE A CG  1 
ATOM   739  C  CD1 . PHE A 1 128 ? 11.36832  28.57469 42.55421  1.000 48.91183  ? 110 PHE A CD1 1 
ATOM   740  C  CD2 . PHE A 1 128 ? 9.36201   27.29812 42.37213  1.000 45.18080  ? 110 PHE A CD2 1 
ATOM   741  C  CE1 . PHE A 1 128 ? 11.49647  28.19556 43.88132  1.000 53.58618  ? 110 PHE A CE1 1 
ATOM   742  C  CE2 . PHE A 1 128 ? 9.48504   26.91458 43.69732  1.000 53.46249  ? 110 PHE A CE2 1 
ATOM   743  C  CZ  . PHE A 1 128 ? 10.55229  27.36515 44.45274  1.000 47.63311  ? 110 PHE A CZ  1 
ATOM   744  N  N   . LEU A 1 129 ? 10.15789  27.47410 37.12007  1.000 38.06400  ? 111 LEU A N   1 
ATOM   745  C  CA  . LEU A 1 129 ? 10.01145  27.78633 35.70390  1.000 43.32590  ? 111 LEU A CA  1 
ATOM   746  C  C   . LEU A 1 129 ? 8.63571   28.36421 35.40228  1.000 43.14228  ? 111 LEU A C   1 
ATOM   747  O  O   . LEU A 1 129 ? 7.62224   27.91375 35.94616  1.000 39.48073  ? 111 LEU A O   1 
ATOM   748  C  CB  . LEU A 1 129 ? 10.23143  26.54294 34.84255  1.000 39.06186  ? 111 LEU A CB  1 
ATOM   749  C  CG  . LEU A 1 129 ? 11.50477  25.74918 35.11896  1.000 43.11907  ? 111 LEU A CG  1 
ATOM   750  C  CD1 . LEU A 1 129 ? 11.58026  24.56432 34.17891  1.000 39.30793  ? 111 LEU A CD1 1 
ATOM   751  C  CD2 . LEU A 1 129 ? 12.73319  26.64190 34.98040  1.000 32.79717  ? 111 LEU A CD2 1 
ATOM   752  N  N   . CYS A 1 130 ? 8.60887   29.35377 34.51515  1.000 37.92741  ? 112 CYS A N   1 
ATOM   753  C  CA  . CYS A 1 130 ? 7.37282   29.94065 34.01297  1.000 45.76317  ? 112 CYS A CA  1 
ATOM   754  C  C   . CYS A 1 130 ? 7.28879   29.67792 32.51496  1.000 52.91384  ? 112 CYS A C   1 
ATOM   755  O  O   . CYS A 1 130 ? 8.20893   30.03601 31.77058  1.000 46.56805  ? 112 CYS A O   1 
ATOM   756  C  CB  . CYS A 1 130 ? 7.32884   31.44359 34.29574  1.000 47.76390  ? 112 CYS A CB  1 
ATOM   757  S  SG  . CYS A 1 130 ? 7.25481   31.88856 36.05466  1.000 47.83520  ? 112 CYS A SG  1 
ATOM   758  N  N   . GLU A 1 131 ? 6.20702   29.03316 32.07806  1.000 55.03618  ? 113 GLU A N   1 
ATOM   759  C  CA  . GLU A 1 131 ? 5.89133   28.91015 30.66059  1.000 43.49800  ? 113 GLU A CA  1 
ATOM   760  C  C   . GLU A 1 131 ? 4.76586   29.87614 30.32083  1.000 52.63332  ? 113 GLU A C   1 
ATOM   761  O  O   . GLU A 1 131 ? 3.97907   30.26259 31.18837  1.000 43.36236  ? 113 GLU A O   1 
ATOM   762  C  CB  . GLU A 1 131 ? 5.47730   27.48421 30.28146  1.000 45.79639  ? 113 GLU A CB  1 
ATOM   763  C  CG  . GLU A 1 131 ? 6.53007   26.41526 30.54173  1.000 43.36632  ? 113 GLU A CG  1 
ATOM   764  C  CD  . GLU A 1 131 ? 6.07641   25.02393 30.11324  1.000 53.11452  ? 113 GLU A CD  1 
ATOM   765  O  OE1 . GLU A 1 131 ? 4.93993   24.88934 29.60084  1.000 48.60375  ? 113 GLU A OE1 1 
ATOM   766  O  OE2 . GLU A 1 131 ? 6.85570   24.06180 30.29212  1.000 45.06908  ? 113 GLU A OE2 1 
ATOM   767  N  N   . TYR A 1 132 ? 4.70489   30.28702 29.04548  1.000 51.70628  ? 114 TYR A N   1 
ATOM   768  C  CA  . TYR A 1 132 ? 3.68712   31.28208 28.69015  1.000 45.02247  ? 114 TYR A CA  1 
ATOM   769  C  C   . TYR A 1 132 ? 3.36335   31.32897 27.19941  1.000 51.97601  ? 114 TYR A C   1 
ATOM   770  O  O   . TYR A 1 132 ? 2.80417   32.34075 26.76409  1.000 49.63042  ? 114 TYR A O   1 
ATOM   771  C  CB  . TYR A 1 132 ? 4.11402   32.68711 29.16620  1.000 42.53149  ? 114 TYR A CB  1 
ATOM   772  C  CG  . TYR A 1 132 ? 5.61227   32.94885 29.20611  1.000 49.92393  ? 114 TYR A CG  1 
ATOM   773  C  CD1 . TYR A 1 132 ? 6.25776   33.56523 28.13736  1.000 55.89325  ? 114 TYR A CD1 1 
ATOM   774  C  CD2 . TYR A 1 132 ? 6.37617   32.60533 30.31844  1.000 48.28600  ? 114 TYR A CD2 1 
ATOM   775  C  CE1 . TYR A 1 132 ? 7.62050   33.81602 28.16709  1.000 55.23853  ? 114 TYR A CE1 1 
ATOM   776  C  CE2 . TYR A 1 132 ? 7.74007   32.85197 30.35570  1.000 53.86833  ? 114 TYR A CE2 1 
ATOM   777  C  CZ  . TYR A 1 132 ? 8.35778   33.45714 29.27798  1.000 54.18433  ? 114 TYR A CZ  1 
ATOM   778  O  OH  . TYR A 1 132 ? 9.71495   33.70767 29.31538  1.000 51.95837  ? 114 TYR A OH  1 
ATOM   779  N  N   . ASP A 1 133 ? 3.66469   30.30280 26.40466  1.000 40.65382  ? 115 ASP A N   1 
ATOM   780  C  CA  . ASP A 1 133 ? 3.32654   30.30504 24.98557  1.000 58.07769  ? 115 ASP A CA  1 
ATOM   781  C  C   . ASP A 1 133 ? 2.00676   29.57827 24.75601  1.000 51.67803  ? 115 ASP A C   1 
ATOM   782  O  O   . ASP A 1 133 ? 1.71146   28.57649 25.41503  1.000 47.05226  ? 115 ASP A O   1 
ATOM   783  C  CB  . ASP A 1 133 ? 4.43264   29.65918 24.14473  1.000 48.29332  ? 115 ASP A CB  1 
ATOM   784  C  CG  . ASP A 1 133 ? 4.77065   28.25578 24.59886  1.000 50.27595  ? 115 ASP A CG  1 
ATOM   785  O  OD1 . ASP A 1 133 ? 4.89512   28.03895 25.82377  1.000 51.24242  ? 115 ASP A OD1 1 
ATOM   786  O  OD2 . ASP A 1 133 ? 4.93174   27.37766 23.72457  1.000 50.84397  ? 115 ASP A OD2 1 
ATOM   787  N  N   . ALA A 1 134 ? 1.22258   30.08312 23.80836  1.000 54.22745  ? 116 ALA A N   1 
ATOM   788  C  CA  . ALA A 1 134 ? -0.11089  29.57562 23.52973  1.000 60.94658  ? 116 ALA A CA  1 
ATOM   789  C  C   . ALA A 1 134 ? -0.09877  28.68198 22.28806  1.000 64.52732  ? 116 ALA A C   1 
ATOM   790  O  O   . ALA A 1 134 ? 0.95792   28.28874 21.78232  1.000 52.37353  ? 116 ALA A O   1 
ATOM   791  C  CB  . ALA A 1 134 ? -1.09104  30.74099 23.37200  1.000 60.14561  ? 116 ALA A CB  1 
ATOM   792  N  N   . LEU A 1 135 ? -1.29220  28.35475 21.78806  1.000 53.69612  ? 117 LEU A N   1 
ATOM   793  C  CA  . LEU A 1 135 ? -1.46243  27.48061 20.63959  1.000 58.74136  ? 117 LEU A CA  1 
ATOM   794  C  C   . LEU A 1 135 ? -2.13532  28.22628 19.49122  1.000 63.38194  ? 117 LEU A C   1 
ATOM   795  O  O   . LEU A 1 135 ? -2.98172  29.09938 19.71929  1.000 62.31237  ? 117 LEU A O   1 
ATOM   796  C  CB  . LEU A 1 135 ? -2.29613  26.24453 21.00275  1.000 54.57281  ? 117 LEU A CB  1 
ATOM   797  C  CG  . LEU A 1 135 ? -1.59543  25.21486 21.89352  1.000 61.87853  ? 117 LEU A CG  1 
ATOM   798  C  CD1 . LEU A 1 135 ? -2.58970  24.21692 22.47022  1.000 60.99831  ? 117 LEU A CD1 1 
ATOM   799  C  CD2 . LEU A 1 135 ? -0.50333  24.50061 21.12263  1.000 49.65703  ? 117 LEU A CD2 1 
ATOM   800  N  N   . PRO A 1 136 ? -1.77961  27.90420 18.24782  1.000 63.21274  ? 118 PRO A N   1 
ATOM   801  C  CA  . PRO A 1 136 ? -2.35775  28.62177 17.10121  1.000 59.77777  ? 118 PRO A CA  1 
ATOM   802  C  C   . PRO A 1 136 ? -3.86391  28.42446 17.01757  1.000 56.09333  ? 118 PRO A C   1 
ATOM   803  O  O   . PRO A 1 136 ? -4.36112  27.29676 17.01256  1.000 59.76321  ? 118 PRO A O   1 
ATOM   804  C  CB  . PRO A 1 136 ? -1.64090  28.00221 15.89426  1.000 54.18277  ? 118 PRO A CB  1 
ATOM   805  C  CG  . PRO A 1 136 ? -0.41290  27.34303 16.46056  1.000 72.45906  ? 118 PRO A CG  1 
ATOM   806  C  CD  . PRO A 1 136 ? -0.79349  26.89237 17.83392  1.000 61.41969  ? 118 PRO A CD  1 
ATOM   807  N  N   . GLY A 1 137 ? -4.58325  29.52868 16.96092  1.000 60.12569  ? 119 GLY A N   1 
ATOM   808  C  CA  . GLY A 1 137 ? -6.03061  29.49980 16.76532  1.000 73.26632  ? 119 GLY A CA  1 
ATOM   809  C  C   . GLY A 1 137 ? -6.89418  29.34621 17.99860  1.000 75.28511  ? 119 GLY A C   1 
ATOM   810  O  O   . GLY A 1 137 ? -7.83687  30.11240 18.19352  1.000 78.48167  ? 119 GLY A O   1 
ATOM   811  N  N   . ILE A 1 138 ? -6.58554  28.35586 18.84420  1.000 64.29016  ? 120 ILE A N   1 
ATOM   812  C  CA  . ILE A 1 138 ? -7.42338  28.07004 20.00767  1.000 68.44584  ? 120 ILE A CA  1 
ATOM   813  C  C   . ILE A 1 138 ? -6.97777  28.80531 21.26487  1.000 64.97080  ? 120 ILE A C   1 
ATOM   814  O  O   . ILE A 1 138 ? -7.66704  28.72396 22.29396  1.000 70.10100  ? 120 ILE A O   1 
ATOM   815  C  CB  . ILE A 1 138 ? -7.47575  26.55388 20.28813  1.000 67.34838  ? 120 ILE A CB  1 
ATOM   816  C  CG1 . ILE A 1 138 ? -6.07334  25.94327 20.23706  1.000 69.02950  ? 120 ILE A CG1 1 
ATOM   817  C  CG2 . ILE A 1 138 ? -8.39720  25.86132 19.29350  1.000 71.51166  ? 120 ILE A CG2 1 
ATOM   818  C  CD1 . ILE A 1 138 ? -6.05965  24.43649 20.39818  1.000 54.55977  ? 120 ILE A CD1 1 
ATOM   819  N  N   . GLY A 1 139 ? -5.86008  29.52507 21.21961  1.000 58.33662  ? 121 GLY A N   1 
ATOM   820  C  CA  . GLY A 1 139 ? -5.40636  30.28143 22.36991  1.000 49.38634  ? 121 GLY A CA  1 
ATOM   821  C  C   . GLY A 1 139 ? -4.68570  29.42764 23.39378  1.000 60.57387  ? 121 GLY A C   1 
ATOM   822  O  O   . GLY A 1 139 ? -3.93030  28.51984 23.03041  1.000 52.97703  ? 121 GLY A O   1 
ATOM   823  N  N   . HIS A 1 140 ? -4.92193  29.69688 24.67856  1.000 51.10733  ? 122 HIS A N   1 
ATOM   824  C  CA  . HIS A 1 140 ? -4.20493  29.01376 25.75671  1.000 63.19557  ? 122 HIS A CA  1 
ATOM   825  C  C   . HIS A 1 140 ? -4.93126  27.72943 26.16360  1.000 59.78187  ? 122 HIS A C   1 
ATOM   826  O  O   . HIS A 1 140 ? -5.37401  27.54870 27.29768  1.000 59.53845  ? 122 HIS A O   1 
ATOM   827  C  CB  . HIS A 1 140 ? -4.01352  29.95686 26.93943  1.000 54.61900  ? 122 HIS A CB  1 
ATOM   828  C  CG  . HIS A 1 140 ? -2.70167  30.67650 26.91472  1.000 60.77867  ? 122 HIS A CG  1 
ATOM   829  N  ND1 . HIS A 1 140 ? -1.49473  30.02240 27.04213  1.000 54.64844  ? 122 HIS A ND1 1 
ATOM   830  C  CD2 . HIS A 1 140 ? -2.40414  31.98604 26.73858  1.000 52.10506  ? 122 HIS A CD2 1 
ATOM   831  C  CE1 . HIS A 1 140 ? -0.51067  30.90031 26.96278  1.000 56.02049  ? 122 HIS A CE1 1 
ATOM   832  N  NE2 . HIS A 1 140 ? -1.03551  32.09860 26.77627  1.000 52.80132  ? 122 HIS A NE2 1 
ATOM   833  N  N   . ALA A 1 141 ? -5.02856  26.81693 25.19648  1.000 59.02089  ? 123 ALA A N   1 
ATOM   834  C  CA  . ALA A 1 141 ? -5.72344  25.55263 25.39304  1.000 52.43084  ? 123 ALA A CA  1 
ATOM   835  C  C   . ALA A 1 141 ? -4.91727  24.54544 26.19813  1.000 58.49872  ? 123 ALA A C   1 
ATOM   836  O  O   . ALA A 1 141 ? -5.43806  23.46484 26.49768  1.000 60.70224  ? 123 ALA A O   1 
ATOM   837  C  CB  . ALA A 1 141 ? -6.09993  24.95037 24.03840  1.000 56.08148  ? 123 ALA A CB  1 
ATOM   838  N  N   . CYS A 1 142 ? -3.66665  24.86119 26.53789  1.000 48.84388  ? 124 CYS A N   1 
ATOM   839  C  CA  . CYS A 1 142 ? -2.86864  24.05274 27.44888  1.000 55.04413  ? 124 CYS A CA  1 
ATOM   840  C  C   . CYS A 1 142 ? -2.74421  24.68820 28.82902  1.000 54.05752  ? 124 CYS A C   1 
ATOM   841  O  O   . CYS A 1 142 ? -2.02715  24.15467 29.68175  1.000 46.44782  ? 124 CYS A O   1 
ATOM   842  C  CB  . CYS A 1 142 ? -1.47309  23.80127 26.85464  1.000 47.79588  ? 124 CYS A CB  1 
ATOM   843  S  SG  . CYS A 1 142 ? -0.51924  22.43945 27.59424  1.000 64.80798  ? 124 CYS A SG  1 
ATOM   844  N  N   . GLY A 1 143 ? -3.42740  25.80562 29.07052  1.000 45.92131  ? 125 GLY A N   1 
ATOM   845  C  CA  . GLY A 1 143 ? -3.36620  26.45622 30.36938  1.000 47.78582  ? 125 GLY A CA  1 
ATOM   846  C  C   . GLY A 1 143 ? -1.99333  26.96801 30.74117  1.000 53.25119  ? 125 GLY A C   1 
ATOM   847  O  O   . GLY A 1 143 ? -1.63879  26.97837 31.92695  1.000 50.43336  ? 125 GLY A O   1 
ATOM   848  N  N   . HIS A 1 144 ? -1.20369  27.39914 29.75670  1.000 47.78833  ? 126 HIS A N   1 
ATOM   849  C  CA  . HIS A 1 144 ? 0.14507   27.86525 30.04923  1.000 42.02149  ? 126 HIS A CA  1 
ATOM   850  C  C   . HIS A 1 144 ? 0.15455   29.16672 30.83948  1.000 47.64166  ? 126 HIS A C   1 
ATOM   851  O  O   . HIS A 1 144 ? 1.14352   29.44777 31.52618  1.000 48.51578  ? 126 HIS A O   1 
ATOM   852  C  CB  . HIS A 1 144 ? 0.93614   28.02124 28.75525  1.000 43.17596  ? 126 HIS A CB  1 
ATOM   853  C  CG  . HIS A 1 144 ? 1.52244   26.73758 28.25797  1.000 44.98752  ? 126 HIS A CG  1 
ATOM   854  N  ND1 . HIS A 1 144 ? 2.56895   26.69383 27.36135  1.000 50.13005  ? 126 HIS A ND1 1 
ATOM   855  C  CD2 . HIS A 1 144 ? 1.21235   25.44933 28.53834  1.000 41.66968  ? 126 HIS A CD2 1 
ATOM   856  C  CE1 . HIS A 1 144 ? 2.87759   25.43363 27.10979  1.000 53.05538  ? 126 HIS A CE1 1 
ATOM   857  N  NE2 . HIS A 1 144 ? 2.07089   24.65900 27.81322  1.000 44.77824  ? 126 HIS A NE2 1 
ATOM   858  N  N   . ASN A 1 145 ? -0.91864  29.95913 30.76749  1.000 42.73061  ? 127 ASN A N   1 
ATOM   859  C  CA  . ASN A 1 145 ? -1.03645  31.12057 31.64505  1.000 48.73488  ? 127 ASN A CA  1 
ATOM   860  C  C   . ASN A 1 145 ? -0.97596  30.70755 33.11058  1.000 50.12134  ? 127 ASN A C   1 
ATOM   861  O  O   . ASN A 1 145 ? -0.40194  31.42173 33.94198  1.000 44.63959  ? 127 ASN A O   1 
ATOM   862  C  CB  . ASN A 1 145 ? -2.33619  31.87626 31.35541  1.000 51.24494  ? 127 ASN A CB  1 
ATOM   863  C  CG  . ASN A 1 145 ? -3.56804  30.99512 31.49135  1.000 51.34406  ? 127 ASN A CG  1 
ATOM   864  O  OD1 . ASN A 1 145 ? -3.80866  30.11389 30.66654  1.000 51.90483  ? 127 ASN A OD1 1 
ATOM   865  N  ND2 . ASN A 1 145 ? -4.35332  31.23077 32.53416  1.000 52.22616  ? 127 ASN A ND2 1 
ATOM   866  N  N   . LEU A 1 146 ? -1.55482  29.55040 33.44675  1.000 45.35843  ? 128 LEU A N   1 
ATOM   867  C  CA  . LEU A 1 146 ? -1.51259  29.08214 34.82878  1.000 51.38736  ? 128 LEU A CA  1 
ATOM   868  C  C   . LEU A 1 146 ? -0.13310  28.54527 35.20957  1.000 48.26722  ? 128 LEU A C   1 
ATOM   869  O  O   . LEU A 1 146 ? 0.22929   28.56656 36.39137  1.000 49.11152  ? 128 LEU A O   1 
ATOM   870  C  CB  . LEU A 1 146 ? -2.58843  28.01604 35.05295  1.000 45.00371  ? 128 LEU A CB  1 
ATOM   871  C  CG  . LEU A 1 146 ? -4.02162  28.39064 34.64877  1.000 45.84033  ? 128 LEU A CG  1 
ATOM   872  C  CD1 . LEU A 1 146 ? -4.97427  27.22449 34.85646  1.000 41.47717  ? 128 LEU A CD1 1 
ATOM   873  C  CD2 . LEU A 1 146 ? -4.51306  29.61830 35.40517  1.000 42.37060  ? 128 LEU A CD2 1 
ATOM   874  N  N   . ILE A 1 147 ? 0.65058   28.07239 34.23610  1.000 43.11031  ? 129 ILE A N   1 
ATOM   875  C  CA  . ILE A 1 147 ? 2.00627   27.61942 34.53920  1.000 45.89933  ? 129 ILE A CA  1 
ATOM   876  C  C   . ILE A 1 147 ? 2.87973   28.79674 34.95225  1.000 50.10389  ? 129 ILE A C   1 
ATOM   877  O  O   . ILE A 1 147 ? 3.63348   28.71446 35.92937  1.000 49.90177  ? 129 ILE A O   1 
ATOM   878  C  CB  . ILE A 1 147 ? 2.60357   26.86377 33.33846  1.000 50.02512  ? 129 ILE A CB  1 
ATOM   879  C  CG1 . ILE A 1 147 ? 1.76430   25.62399 33.02576  1.000 41.73148  ? 129 ILE A CG1 1 
ATOM   880  C  CG2 . ILE A 1 147 ? 4.05515   26.47395 33.61525  1.000 43.25646  ? 129 ILE A CG2 1 
ATOM   881  C  CD1 . ILE A 1 147 ? 2.37806   24.71256 31.98409  1.000 42.07896  ? 129 ILE A CD1 1 
ATOM   882  N  N   . ALA A 1 148 ? 2.79529   29.90985 34.21798  1.000 47.23998  ? 130 ALA A N   1 
ATOM   883  C  CA  . ALA A 1 148 ? 3.49629   31.11898 34.63419  1.000 44.74683  ? 130 ALA A CA  1 
ATOM   884  C  C   . ALA A 1 148 ? 3.06457   31.54901 36.02881  1.000 47.88414  ? 130 ALA A C   1 
ATOM   885  O  O   . ALA A 1 148 ? 3.90352   31.91087 36.86160  1.000 48.09344  ? 130 ALA A O   1 
ATOM   886  C  CB  . ALA A 1 148 ? 3.24502   32.24353 33.63249  1.000 46.46104  ? 130 ALA A CB  1 
ATOM   887  N  N   . GLU A 1 149 ? 1.75709   31.50874 36.29976  1.000 44.43461  ? 131 GLU A N   1 
ATOM   888  C  CA  . GLU A 1 149 ? 1.23897   31.93055 37.59837  1.000 46.18024  ? 131 GLU A CA  1 
ATOM   889  C  C   . GLU A 1 149 ? 1.77598   31.05096 38.71991  1.000 41.97729  ? 131 GLU A C   1 
ATOM   890  O  O   . GLU A 1 149 ? 2.25339   31.55065 39.74398  1.000 42.21558  ? 131 GLU A O   1 
ATOM   891  C  CB  . GLU A 1 149 ? -0.29192  31.89806 37.58149  1.000 39.49343  ? 131 GLU A CB  1 
ATOM   892  C  CG  . GLU A 1 149 ? -0.94247  32.81543 38.60788  1.000 48.72016  ? 131 GLU A CG  1 
ATOM   893  C  CD  . GLU A 1 149 ? -2.40458  32.48741 38.85541  1.000 48.19786  ? 131 GLU A CD  1 
ATOM   894  O  OE1 . GLU A 1 149 ? -3.02997  31.82010 38.00030  1.000 44.17527  ? 131 GLU A OE1 1 
ATOM   895  O  OE2 . GLU A 1 149 ? -2.93663  32.91334 39.90242  1.000 44.89804  ? 131 GLU A OE2 1 
ATOM   896  N  N   . VAL A 1 150 ? 1.70459   29.73087 38.53946  1.000 45.76593  ? 132 VAL A N   1 
ATOM   897  C  CA  . VAL A 1 150 ? 2.10895   28.80909 39.59342  1.000 48.63010  ? 132 VAL A CA  1 
ATOM   898  C  C   . VAL A 1 150 ? 3.60901   28.91795 39.87189  1.000 49.15519  ? 132 VAL A C   1 
ATOM   899  O  O   . VAL A 1 150 ? 4.04160   28.81212 41.02784  1.000 46.09646  ? 132 VAL A O   1 
ATOM   900  C  CB  . VAL A 1 150 ? 1.66780   27.37761 39.21394  1.000 52.08484  ? 132 VAL A CB  1 
ATOM   901  C  CG1 . VAL A 1 150 ? 2.69993   26.67814 38.35718  1.000 56.87332  ? 132 VAL A CG1 1 
ATOM   902  C  CG2 . VAL A 1 150 ? 1.35754   26.55630 40.44848  1.000 61.09373  ? 132 VAL A CG2 1 
ATOM   903  N  N   . GLY A 1 151 ? 4.42231   29.16634 38.84189  1.000 48.97945  ? 133 GLY A N   1 
ATOM   904  C  CA  . GLY A 1 151 ? 5.84905   29.33699 39.06870  1.000 40.73135  ? 133 GLY A CA  1 
ATOM   905  C  C   . GLY A 1 151 ? 6.16201   30.62937 39.79753  1.000 50.87612  ? 133 GLY A C   1 
ATOM   906  O  O   . GLY A 1 151 ? 7.01479   30.66129 40.69072  1.000 47.78158  ? 133 GLY A O   1 
ATOM   907  N  N   . ALA A 1 152 ? 5.47297   31.71270 39.43259  1.000 50.00992  ? 134 ALA A N   1 
ATOM   908  C  CA  . ALA A 1 152 ? 5.63550   32.96428 40.16255  1.000 51.98536  ? 134 ALA A CA  1 
ATOM   909  C  C   . ALA A 1 152 ? 5.14519   32.82702 41.59669  1.000 48.58486  ? 134 ALA A C   1 
ATOM   910  O  O   . ALA A 1 152 ? 5.78678   33.32098 42.53128  1.000 51.67144  ? 134 ALA A O   1 
ATOM   911  C  CB  . ALA A 1 152 ? 4.88858   34.08952 39.44924  1.000 45.74597  ? 134 ALA A CB  1 
ATOM   912  N  N   . ALA A 1 153 ? 4.01293   32.14776 41.78979  1.000 45.42951  ? 135 ALA A N   1 
ATOM   913  C  CA  . ALA A 1 153 ? 3.41668   32.05442 43.11725  1.000 45.28888  ? 135 ALA A CA  1 
ATOM   914  C  C   . ALA A 1 153 ? 4.28332   31.22346 44.05478  1.000 51.05011  ? 135 ALA A C   1 
ATOM   915  O  O   . ALA A 1 153 ? 4.53811   31.62399 45.19902  1.000 50.03227  ? 135 ALA A O   1 
ATOM   916  C  CB  . ALA A 1 153 ? 2.00901   31.46492 43.01952  1.000 45.97860  ? 135 ALA A CB  1 
ATOM   917  N  N   . ALA A 1 154 ? 4.74277   30.05895 43.58665  1.000 46.48145  ? 136 ALA A N   1 
ATOM   918  C  CA  . ALA A 1 154 ? 5.61204   29.21605 44.40314  1.000 51.21031  ? 136 ALA A CA  1 
ATOM   919  C  C   . ALA A 1 154 ? 6.82934   29.99006 44.88662  1.000 48.17866  ? 136 ALA A C   1 
ATOM   920  O  O   . ALA A 1 154 ? 7.17381   29.95288 46.07382  1.000 51.73013  ? 136 ALA A O   1 
ATOM   921  C  CB  . ALA A 1 154 ? 6.04460   27.97939 43.61466  1.000 42.99057  ? 136 ALA A CB  1 
ATOM   922  N  N   . ALA A 1 155 ? 7.48479   30.71417 43.97544  1.000 49.62970  ? 137 ALA A N   1 
ATOM   923  C  CA  . ALA A 1 155 ? 8.68425   31.46080 44.34390  1.000 53.22088  ? 137 ALA A CA  1 
ATOM   924  C  C   . ALA A 1 155 ? 8.35714   32.60515 45.29473  1.000 52.56779  ? 137 ALA A C   1 
ATOM   925  O  O   . ALA A 1 155 ? 9.12792   32.88932 46.21950  1.000 57.27936  ? 137 ALA A O   1 
ATOM   926  C  CB  . ALA A 1 155 ? 9.38361   31.98912 43.09291  1.000 40.96984  ? 137 ALA A CB  1 
ATOM   927  N  N   . LEU A 1 156 ? 7.22794   33.28260 45.07859  1.000 50.54894  ? 138 LEU A N   1 
ATOM   928  C  CA  . LEU A 1 156 ? 6.80198   34.30837 46.02427  1.000 52.18573  ? 138 LEU A CA  1 
ATOM   929  C  C   . LEU A 1 156 ? 6.60126   33.71710 47.41288  1.000 55.89848  ? 138 LEU A C   1 
ATOM   930  O  O   . LEU A 1 156 ? 7.05640   34.28777 48.41144  1.000 54.48598  ? 138 LEU A O   1 
ATOM   931  C  CB  . LEU A 1 156 ? 5.51294   34.97071 45.54102  1.000 53.59676  ? 138 LEU A CB  1 
ATOM   932  C  CG  . LEU A 1 156 ? 5.65205   36.38491 44.98227  1.000 60.16361  ? 138 LEU A CG  1 
ATOM   933  C  CD1 . LEU A 1 156 ? 6.53148   36.36986 43.74340  1.000 58.28298  ? 138 LEU A CD1 1 
ATOM   934  C  CD2 . LEU A 1 156 ? 4.28735   36.97429 44.67135  1.000 53.86642  ? 138 LEU A CD2 1 
ATOM   935  N  N   . GLY A 1 157 ? 5.93269   32.56347 47.49057  1.000 52.74482  ? 139 GLY A N   1 
ATOM   936  C  CA  . GLY A 1 157 ? 5.66906   31.95329 48.78200  1.000 51.54620  ? 139 GLY A CA  1 
ATOM   937  C  C   . GLY A 1 157 ? 6.93433   31.53829 49.50732  1.000 59.62297  ? 139 GLY A C   1 
ATOM   938  O  O   . GLY A 1 157 ? 7.03286   31.67780 50.72882  1.000 56.61926  ? 139 GLY A O   1 
ATOM   939  N  N   . VAL A 1 158 ? 7.92188   31.02698 48.76821  1.000 56.52815  ? 140 VAL A N   1 
ATOM   940  C  CA  . VAL A 1 158 ? 9.17951   30.63049 49.39705  1.000 56.98388  ? 140 VAL A CA  1 
ATOM   941  C  C   . VAL A 1 158 ? 9.86820   31.84370 50.01016  1.000 63.12422  ? 140 VAL A C   1 
ATOM   942  O  O   . VAL A 1 158 ? 10.30851  31.81182 51.16722  1.000 58.43151  ? 140 VAL A O   1 
ATOM   943  C  CB  . VAL A 1 158 ? 10.09258  29.91662 48.38512  1.000 51.72695  ? 140 VAL A CB  1 
ATOM   944  C  CG1 . VAL A 1 158 ? 11.47326  29.69336 48.99083  1.000 45.87712  ? 140 VAL A CG1 1 
ATOM   945  C  CG2 . VAL A 1 158 ? 9.47280   28.59500 47.94565  1.000 59.43815  ? 140 VAL A CG2 1 
ATOM   946  N  N   . ARG A 1 159 ? 9.95684   32.93892 49.24735  1.000 52.88502  ? 141 ARG A N   1 
ATOM   947  C  CA  . ARG A 1 159 ? 10.63181  34.13215 49.74917  1.000 61.17015  ? 141 ARG A CA  1 
ATOM   948  C  C   . ARG A 1 159 ? 9.96099   34.66140 51.01039  1.000 58.99398  ? 141 ARG A C   1 
ATOM   949  O  O   . ARG A 1 159 ? 10.64075  35.00965 51.98263  1.000 59.67401  ? 141 ARG A O   1 
ATOM   950  C  CB  . ARG A 1 159 ? 10.66761  35.21917 48.67614  1.000 57.94439  ? 141 ARG A CB  1 
ATOM   951  C  CG  . ARG A 1 159 ? 10.93772  36.60191 49.25745  1.000 62.86338  ? 141 ARG A CG  1 
ATOM   952  C  CD  . ARG A 1 159 ? 11.07342  37.67272 48.19349  1.000 60.40106  ? 141 ARG A CD  1 
ATOM   953  N  NE  . ARG A 1 159 ? 11.10786  38.99675 48.80104  1.000 60.67838  ? 141 ARG A NE  1 
ATOM   954  C  CZ  . ARG A 1 159 ? 11.28753  40.12749 48.13377  1.000 66.46869  ? 141 ARG A CZ  1 
ATOM   955  N  NH1 . ARG A 1 159 ? 11.46641  40.13618 46.82416  1.000 66.63403  ? 141 ARG A NH1 1 
ATOM   956  N  NH2 . ARG A 1 159 ? 11.28976  41.27861 48.79888  1.000 72.42223  ? 141 ARG A NH2 1 
ATOM   957  N  N   . GLY A 1 160 ? 8.62638   34.71920 51.01680  1.000 60.42115  ? 142 GLY A N   1 
ATOM   958  C  CA  . GLY A 1 160 ? 7.91666   35.23728 52.17413  1.000 59.01078  ? 142 GLY A CA  1 
ATOM   959  C  C   . GLY A 1 160 ? 8.07900   34.38637 53.41790  1.000 60.90045  ? 142 GLY A C   1 
ATOM   960  O  O   . GLY A 1 160 ? 8.05245   34.90790 54.53693  1.000 71.37001  ? 142 GLY A O   1 
ATOM   961  N  N   . ALA A 1 161 ? 8.24258   33.07247 53.24746  1.000 56.50944  ? 143 ALA A N   1 
ATOM   962  C  CA  . ALA A 1 161 ? 8.47539   32.20482 54.39705  1.000 63.48637  ? 143 ALA A CA  1 
ATOM   963  C  C   . ALA A 1 161 ? 9.86539   32.42800 54.98002  1.000 68.83144  ? 143 ALA A C   1 
ATOM   964  O  O   . ALA A 1 161 ? 10.04778  32.38393 56.20309  1.000 74.76840  ? 143 ALA A O   1 
ATOM   965  C  CB  . ALA A 1 161 ? 8.28455   30.74078 53.99703  1.000 57.65268  ? 143 ALA A CB  1 
ATOM   966  N  N   . LEU A 1 162 ? 10.85512  32.67372 54.11979  1.000 61.48517  ? 144 LEU A N   1 
ATOM   967  C  CA  . LEU A 1 162 ? 12.22430  32.92116 54.55340  1.000 71.52263  ? 144 LEU A CA  1 
ATOM   968  C  C   . LEU A 1 162 ? 12.47034  34.36930 54.95841  1.000 77.36364  ? 144 LEU A C   1 
ATOM   969  O  O   . LEU A 1 162 ? 13.38644  34.62797 55.74747  1.000 77.01212  ? 144 LEU A O   1 
ATOM   970  C  CB  . LEU A 1 162 ? 13.20642  32.53124 53.44061  1.000 64.73233  ? 144 LEU A CB  1 
ATOM   971  C  CG  . LEU A 1 162 ? 13.16401  31.06070 53.01427  1.000 64.88412  ? 144 LEU A CG  1 
ATOM   972  C  CD1 . LEU A 1 162 ? 13.93465  30.85058 51.72409  1.000 49.23609  ? 144 LEU A CD1 1 
ATOM   973  C  CD2 . LEU A 1 162 ? 13.68735  30.14519 54.12382  1.000 57.09988  ? 144 LEU A CD2 1 
ATOM   974  N  N   . GLU A 1 163 ? 11.68634  35.31558 54.43124  1.000 74.33525  ? 145 GLU A N   1 
ATOM   975  C  CA  . GLU A 1 163 ? 11.83871  36.71193 54.82863  1.000 74.91272  ? 145 GLU A CA  1 
ATOM   976  C  C   . GLU A 1 163 ? 11.39628  36.92580 56.26862  1.000 82.42757  ? 145 GLU A C   1 
ATOM   977  O  O   . GLU A 1 163 ? 12.00243  37.71732 56.99978  1.000 91.89650  ? 145 GLU A O   1 
ATOM   978  C  CB  . GLU A 1 163 ? 11.04029  37.61496 53.88988  1.000 67.48371  ? 145 GLU A CB  1 
ATOM   979  C  CG  . GLU A 1 163 ? 11.88893  38.50768 53.01437  1.000 75.11941  ? 145 GLU A CG  1 
ATOM   980  C  CD  . GLU A 1 163 ? 11.06079  39.28559 52.01876  1.000 82.00926  ? 145 GLU A CD  1 
ATOM   981  O  OE1 . GLU A 1 163 ? 9.82055   39.29234 52.15802  1.000 85.69599  ? 145 GLU A OE1 1 
ATOM   982  O  OE2 . GLU A 1 163 ? 11.64858  39.88544 51.09552  1.000 90.92184  ? 145 GLU A OE2 1 
ATOM   983  N  N   . GLY A 1 164 ? 10.33564  36.24032 56.68782  1.000 86.49379  ? 146 GLY A N   1 
ATOM   984  C  CA  . GLY A 1 164 ? 9.85644   36.34130 58.05027  1.000 91.14569  ? 146 GLY A CA  1 
ATOM   985  C  C   . GLY A 1 164 ? 10.56991  35.38682 58.98390  1.000 107.67232 ? 146 GLY A C   1 
ATOM   986  O  O   . GLY A 1 164 ? 9.93084   34.56793 59.65144  1.000 115.59945 ? 146 GLY A O   1 
ATOM   987  N  N   . LEU A 1 165 ? 11.89895  35.48274 59.03948  1.000 104.49953 ? 147 LEU A N   1 
ATOM   988  C  CA  . LEU A 1 165 ? 12.70916  34.60535 59.86900  1.000 105.21129 ? 147 LEU A CA  1 
ATOM   989  C  C   . LEU A 1 165 ? 13.73161  35.43878 60.63238  1.000 108.47791 ? 147 LEU A C   1 
ATOM   990  O  O   . LEU A 1 165 ? 14.44481  36.25597 60.02373  1.000 103.85175 ? 147 LEU A O   1 
ATOM   991  C  CB  . LEU A 1 165 ? 13.41220  33.53854 59.01771  1.000 96.28722  ? 147 LEU A CB  1 
ATOM   992  C  CG  . LEU A 1 165 ? 12.87798  32.10982 59.14561  1.000 82.18124  ? 147 LEU A CG  1 
ATOM   993  N  N   . PRO A 1 166 ? 13.83699  35.27022 61.95245  1.000 114.65066 ? 148 PRO A N   1 
ATOM   994  C  CA  . PRO A 1 166 ? 14.83420  36.03058 62.71671  1.000 117.61065 ? 148 PRO A CA  1 
ATOM   995  C  C   . PRO A 1 166 ? 16.20364  35.37524 62.67589  1.000 120.30275 ? 148 PRO A C   1 
ATOM   996  O  O   . PRO A 1 166 ? 17.17198  35.97657 62.19780  1.000 120.86166 ? 148 PRO A O   1 
ATOM   997  C  CB  . PRO A 1 166 ? 14.26134  36.04245 64.14082  1.000 115.65514 ? 148 PRO A CB  1 
ATOM   998  C  CG  . PRO A 1 166 ? 13.18304  34.97613 64.17003  1.000 114.55506 ? 148 PRO A CG  1 
ATOM   999  C  CD  . PRO A 1 166 ? 13.05501  34.36178 62.80507  1.000 120.38423 ? 148 PRO A CD  1 
ATOM   1000 N  N   . ARG A 1 167 ? 16.28791  34.14825 63.18762  1.000 121.54832 ? 149 ARG A N   1 
ATOM   1001 C  CA  . ARG A 1 167 ? 17.50662  33.35694 63.13175  1.000 122.46117 ? 149 ARG A CA  1 
ATOM   1002 C  C   . ARG A 1 167 ? 18.06019  33.35307 61.70688  1.000 117.38350 ? 149 ARG A C   1 
ATOM   1003 O  O   . ARG A 1 167 ? 17.32022  33.02353 60.76630  1.000 102.84091 ? 149 ARG A O   1 
ATOM   1004 C  CB  . ARG A 1 167 ? 17.23364  31.92803 63.59675  1.000 104.67003 ? 149 ARG A CB  1 
ATOM   1005 N  N   . PRO A 1 168 ? 19.32152  33.74094 61.50981  1.000 117.14692 ? 150 PRO A N   1 
ATOM   1006 C  CA  . PRO A 1 168 ? 19.90079  33.84810 60.16037  1.000 116.86698 ? 150 PRO A CA  1 
ATOM   1007 C  C   . PRO A 1 168 ? 19.49670  32.68403 59.27600  1.000 109.48314 ? 150 PRO A C   1 
ATOM   1008 O  O   . PRO A 1 168 ? 19.71033  31.51585 59.63227  1.000 104.67460 ? 150 PRO A O   1 
ATOM   1009 C  CB  . PRO A 1 168 ? 21.41582  33.84175 60.43089  1.000 110.43054 ? 150 PRO A CB  1 
ATOM   1010 C  CG  . PRO A 1 168 ? 21.56962  34.07755 61.94955  1.000 112.86867 ? 150 PRO A CG  1 
ATOM   1011 C  CD  . PRO A 1 168 ? 20.20483  34.34710 62.51433  1.000 103.01317 ? 150 PRO A CD  1 
ATOM   1012 N  N   . PRO A 1 169 ? 18.89763  32.96462 58.11514  1.000 115.63978 ? 151 PRO A N   1 
ATOM   1013 C  CA  . PRO A 1 169 ? 18.33227  31.88311 57.31084  1.000 105.06224 ? 151 PRO A CA  1 
ATOM   1014 C  C   . PRO A 1 169 ? 19.42148  31.11758 56.58885  1.000 93.72830  ? 151 PRO A C   1 
ATOM   1015 O  O   . PRO A 1 169 ? 20.51199  31.65600 56.32583  1.000 92.00589  ? 151 PRO A O   1 
ATOM   1016 C  CB  . PRO A 1 169 ? 17.41058  32.62124 56.32231  1.000 98.89375  ? 151 PRO A CB  1 
ATOM   1017 C  CG  . PRO A 1 169 ? 17.99138  33.99439 56.21173  1.000 106.28691 ? 151 PRO A CG  1 
ATOM   1018 C  CD  . PRO A 1 169 ? 18.79806  34.27956 57.45506  1.000 112.35028 ? 151 PRO A CD  1 
ATOM   1019 N  N   . PRO A 1 170 ? 19.19007  29.84278 56.27369  1.000 96.67162  ? 152 PRO A N   1 
ATOM   1020 C  CA  . PRO A 1 170 ? 20.19818  29.07639 55.55131  1.000 94.51070  ? 152 PRO A CA  1 
ATOM   1021 C  C   . PRO A 1 170 ? 20.46822  29.69698 54.19688  1.000 81.76136  ? 152 PRO A C   1 
ATOM   1022 O  O   . PRO A 1 170 ? 19.59779  30.37468 53.61841  1.000 70.10969  ? 152 PRO A O   1 
ATOM   1023 C  CB  . PRO A 1 170 ? 19.55979  27.68486 55.41950  1.000 89.96449  ? 152 PRO A CB  1 
ATOM   1024 C  CG  . PRO A 1 170 ? 18.52889  27.63082 56.50116  1.000 87.22072  ? 152 PRO A CG  1 
ATOM   1025 C  CD  . PRO A 1 170 ? 18.01009  29.02988 56.61320  1.000 93.39331  ? 152 PRO A CD  1 
ATOM   1026 N  N   . PRO A 1 171 ? 21.67079  29.50829 53.65621  1.000 75.11607  ? 153 PRO A N   1 
ATOM   1027 C  CA  . PRO A 1 171 ? 22.00412  30.12624 52.36640  1.000 79.13325  ? 153 PRO A CA  1 
ATOM   1028 C  C   . PRO A 1 171 ? 21.16621  29.55436 51.23674  1.000 69.61755  ? 153 PRO A C   1 
ATOM   1029 O  O   . PRO A 1 171 ? 21.35274  28.39966 50.84048  1.000 72.39743  ? 153 PRO A O   1 
ATOM   1030 C  CB  . PRO A 1 171 ? 23.49334  29.79457 52.18676  1.000 80.63911  ? 153 PRO A CB  1 
ATOM   1031 C  CG  . PRO A 1 171 ? 23.97497  29.35960 53.53752  1.000 79.53839  ? 153 PRO A CG  1 
ATOM   1032 C  CD  . PRO A 1 171 ? 22.79487  28.73495 54.20490  1.000 80.59955  ? 153 PRO A CD  1 
ATOM   1033 N  N   . VAL A 1 172 ? 20.22953  30.34872 50.72502  1.000 65.61632  ? 154 VAL A N   1 
ATOM   1034 C  CA  . VAL A 1 172 ? 19.33183  29.92385 49.65726  1.000 65.95466  ? 154 VAL A CA  1 
ATOM   1035 C  C   . VAL A 1 172 ? 19.22864  31.04929 48.63774  1.000 60.66582  ? 154 VAL A C   1 
ATOM   1036 O  O   . VAL A 1 172 ? 19.20359  32.22978 49.00119  1.000 64.07870  ? 154 VAL A O   1 
ATOM   1037 C  CB  . VAL A 1 172 ? 17.93196  29.55077 50.19832  1.000 65.53596  ? 154 VAL A CB  1 
ATOM   1038 C  CG1 . VAL A 1 172 ? 16.99007  29.18054 49.05893  1.000 54.40237  ? 154 VAL A CG1 1 
ATOM   1039 C  CG2 . VAL A 1 172 ? 18.02102  28.41357 51.20633  1.000 70.25304  ? 154 VAL A CG2 1 
ATOM   1040 N  N   . LYS A 1 173 ? 19.18144  30.68315 47.35868  1.000 57.33376  ? 155 LYS A N   1 
ATOM   1041 C  CA  . LYS A 1 173 ? 18.86596  31.61102 46.28000  1.000 56.16748  ? 155 LYS A CA  1 
ATOM   1042 C  C   . LYS A 1 173 ? 17.65424  31.07861 45.52619  1.000 57.37967  ? 155 LYS A C   1 
ATOM   1043 O  O   . LYS A 1 173 ? 17.68875  29.96010 45.00011  1.000 58.80580  ? 155 LYS A O   1 
ATOM   1044 C  CB  . LYS A 1 173 ? 20.05797  31.79277 45.33663  1.000 53.69952  ? 155 LYS A CB  1 
ATOM   1045 C  CG  . LYS A 1 173 ? 19.83889  32.85130 44.26289  1.000 64.75020  ? 155 LYS A CG  1 
ATOM   1046 C  CD  . LYS A 1 173 ? 21.02304  32.93964 43.31694  1.000 67.31047  ? 155 LYS A CD  1 
ATOM   1047 C  CE  . LYS A 1 173 ? 21.94907  34.08417 43.69813  1.000 79.60208  ? 155 LYS A CE  1 
ATOM   1048 N  NZ  . LYS A 1 173 ? 23.26479  33.97827 43.00661  1.000 75.24381  ? 155 LYS A NZ  1 
ATOM   1049 N  N   . VAL A 1 174 ? 16.58632  31.86939 45.48462  1.000 47.42474  ? 156 VAL A N   1 
ATOM   1050 C  CA  . VAL A 1 174 ? 15.39346  31.52891 44.71519  1.000 49.25361  ? 156 VAL A CA  1 
ATOM   1051 C  C   . VAL A 1 174 ? 15.55137  32.08942 43.30723  1.000 53.01145  ? 156 VAL A C   1 
ATOM   1052 O  O   . VAL A 1 174 ? 15.68655  33.30501 43.13014  1.000 53.15013  ? 156 VAL A O   1 
ATOM   1053 C  CB  . VAL A 1 174 ? 14.12435  32.07592 45.38340  1.000 49.46554  ? 156 VAL A CB  1 
ATOM   1054 C  CG1 . VAL A 1 174 ? 12.89897  31.76790 44.52477  1.000 42.09113  ? 156 VAL A CG1 1 
ATOM   1055 C  CG2 . VAL A 1 174 ? 13.97303  31.50134 46.78697  1.000 42.71519  ? 156 VAL A CG2 1 
ATOM   1056 N  N   . VAL A 1 175 ? 15.51965  31.20791 42.30696  1.000 46.97289  ? 157 VAL A N   1 
ATOM   1057 C  CA  . VAL A 1 175 ? 15.72942  31.57019 40.90813  1.000 44.61578  ? 157 VAL A CA  1 
ATOM   1058 C  C   . VAL A 1 175 ? 14.45934  31.27279 40.12076  1.000 49.99072  ? 157 VAL A C   1 
ATOM   1059 O  O   . VAL A 1 175 ? 13.94736  30.14737 40.15947  1.000 44.25216  ? 157 VAL A O   1 
ATOM   1060 C  CB  . VAL A 1 175 ? 16.92517  30.81111 40.30061  1.000 50.23911  ? 157 VAL A CB  1 
ATOM   1061 C  CG1 . VAL A 1 175 ? 17.08744  31.15474 38.82187  1.000 42.72320  ? 157 VAL A CG1 1 
ATOM   1062 C  CG2 . VAL A 1 175 ? 18.19864  31.12723 41.06644  1.000 51.24151  ? 157 VAL A CG2 1 
ATOM   1063 N  N   . VAL A 1 176 ? 13.96457  32.27299 39.39449  1.000 47.43339  ? 158 VAL A N   1 
ATOM   1064 C  CA  . VAL A 1 176 ? 12.84735  32.10904 38.47080  1.000 44.09344  ? 158 VAL A CA  1 
ATOM   1065 C  C   . VAL A 1 176 ? 13.37904  32.25923 37.05134  1.000 52.71099  ? 158 VAL A C   1 
ATOM   1066 O  O   . VAL A 1 176 ? 14.12271  33.20450 36.75680  1.000 49.43525  ? 158 VAL A O   1 
ATOM   1067 C  CB  . VAL A 1 176 ? 11.72132  33.12085 38.74589  1.000 52.94994  ? 158 VAL A CB  1 
ATOM   1068 C  CG1 . VAL A 1 176 ? 10.58228  32.91762 37.76185  1.000 43.59750  ? 158 VAL A CG1 1 
ATOM   1069 C  CG2 . VAL A 1 176 ? 11.21835  32.99356 40.18121  1.000 50.78236  ? 158 VAL A CG2 1 
ATOM   1070 N  N   . LEU A 1 177 ? 12.99687  31.32878 36.17551  1.000 41.78547  ? 159 LEU A N   1 
ATOM   1071 C  CA  . LEU A 1 177 ? 13.41554  31.31989 34.77753  1.000 40.02505  ? 159 LEU A CA  1 
ATOM   1072 C  C   . LEU A 1 177 ? 12.18136  31.32126 33.88734  1.000 46.26414  ? 159 LEU A C   1 
ATOM   1073 O  O   . LEU A 1 177 ? 11.37976  30.38021 33.93298  1.000 41.46992  ? 159 LEU A O   1 
ATOM   1074 C  CB  . LEU A 1 177 ? 14.27559  30.09310 34.46970  1.000 40.21105  ? 159 LEU A CB  1 
ATOM   1075 C  CG  . LEU A 1 177 ? 15.73755  30.10872 34.91878  1.000 34.99573  ? 159 LEU A CG  1 
ATOM   1076 C  CD1 . LEU A 1 177 ? 16.39823  28.78294 34.56437  1.000 40.37213  ? 159 LEU A CD1 1 
ATOM   1077 C  CD2 . LEU A 1 177 ? 16.48669  31.27932 34.29434  1.000 46.73538  ? 159 LEU A CD2 1 
ATOM   1078 N  N   . GLY A 1 178 ? 12.02719  32.36972 33.08172  1.000 44.26870  ? 160 GLY A N   1 
ATOM   1079 C  CA  . GLY A 1 178 ? 11.00955  32.35308 32.04805  1.000 42.55500  ? 160 GLY A CA  1 
ATOM   1080 C  C   . GLY A 1 178 ? 11.46697  31.54624 30.85018  1.000 48.69353  ? 160 GLY A C   1 
ATOM   1081 O  O   . GLY A 1 178 ? 12.45372  31.90828 30.20245  1.000 49.72652  ? 160 GLY A O   1 
ATOM   1082 N  N   . THR A 1 179 ? 10.77778  30.44279 30.55183  1.000 42.57707  ? 161 THR A N   1 
ATOM   1083 C  CA  . THR A 1 179 ? 11.18184  29.54968 29.46729  1.000 48.07041  ? 161 THR A CA  1 
ATOM   1084 C  C   . THR A 1 179 ? 10.15798  29.59852 28.34320  1.000 52.95796  ? 161 THR A C   1 
ATOM   1085 O  O   . THR A 1 179 ? 9.13912   28.89221 28.40231  1.000 45.13299  ? 161 THR A O   1 
ATOM   1086 C  CB  . THR A 1 179 ? 11.34144  28.11311 29.97306  1.000 47.50746  ? 161 THR A CB  1 
ATOM   1087 O  OG1 . THR A 1 179 ? 10.05085  27.57384 30.30350  1.000 44.62320  ? 161 THR A OG1 1 
ATOM   1088 C  CG2 . THR A 1 179 ? 12.24929  28.07225 31.19632  1.000 41.97145  ? 161 THR A CG2 1 
ATOM   1089 N  N   . PRO A 1 180 ? 10.38118  30.38952 27.29711  1.000 54.19615  ? 162 PRO A N   1 
ATOM   1090 C  CA  . PRO A 1 180 ? 9.40184   30.47091 26.20758  1.000 46.14124  ? 162 PRO A CA  1 
ATOM   1091 C  C   . PRO A 1 180 ? 9.39399   29.20368 25.36727  1.000 47.95122  ? 162 PRO A C   1 
ATOM   1092 O  O   . PRO A 1 180 ? 10.19779  28.28894 25.55003  1.000 42.53293  ? 162 PRO A O   1 
ATOM   1093 C  CB  . PRO A 1 180 ? 9.86718   31.67678 25.38681  1.000 53.73121  ? 162 PRO A CB  1 
ATOM   1094 C  CG  . PRO A 1 180 ? 11.31087  31.83538 25.70648  1.000 56.58788  ? 162 PRO A CG  1 
ATOM   1095 C  CD  . PRO A 1 180 ? 11.54159  31.27291 27.08518  1.000 49.90856  ? 162 PRO A CD  1 
ATOM   1096 N  N   . ALA A 1 181 ? 8.42686   29.15453 24.44980  1.000 48.51519  ? 163 ALA A N   1 
ATOM   1097 C  CA  . ALA A 1 181 ? 8.40141   28.18653 23.35178  1.000 56.79536  ? 163 ALA A CA  1 
ATOM   1098 C  C   . ALA A 1 181 ? 8.46785   26.73986 23.85071  1.000 51.17127  ? 163 ALA A C   1 
ATOM   1099 O  O   . ALA A 1 181 ? 9.38314   25.98436 23.52492  1.000 57.62487  ? 163 ALA A O   1 
ATOM   1100 C  CB  . ALA A 1 181 ? 9.53494   28.47394 22.36056  1.000 50.01913  ? 163 ALA A CB  1 
ATOM   1101 N  N   . GLU A 1 182 ? 7.46294   26.35155 24.63703  1.000 48.63040  ? 164 GLU A N   1 
ATOM   1102 C  CA  . GLU A 1 182 ? 7.37145   24.94899 25.02947  1.000 51.36871  ? 164 GLU A CA  1 
ATOM   1103 C  C   . GLU A 1 182 ? 6.69827   24.10913 23.95000  1.000 49.94531  ? 164 GLU A C   1 
ATOM   1104 O  O   . GLU A 1 182 ? 7.11730   22.97496 23.69491  1.000 56.41700  ? 164 GLU A O   1 
ATOM   1105 C  CB  . GLU A 1 182 ? 6.61525   24.80705 26.35227  1.000 44.13394  ? 164 GLU A CB  1 
ATOM   1106 C  CG  . GLU A 1 182 ? 6.63800   23.39629 26.93443  1.000 39.14315  ? 164 GLU A CG  1 
ATOM   1107 C  CD  . GLU A 1 182 ? 5.57154   22.47959 26.33690  1.000 53.71643  ? 164 GLU A CD  1 
ATOM   1108 O  OE1 . GLU A 1 182 ? 4.51038   22.98852 25.89656  1.000 47.48900  ? 164 GLU A OE1 1 
ATOM   1109 O  OE2 . GLU A 1 182 ? 5.79564   21.24743 26.31140  1.000 43.14448  ? 164 GLU A OE2 1 
ATOM   1110 N  N   . GLU A 1 183 ? 5.64447   24.63805 23.31969  1.000 57.09553  ? 165 GLU A N   1 
ATOM   1111 C  CA  . GLU A 1 183 ? 4.88739   23.85204 22.35050  1.000 66.80204  ? 165 GLU A CA  1 
ATOM   1112 C  C   . GLU A 1 183 ? 5.64879   23.63617 21.04860  1.000 66.87154  ? 165 GLU A C   1 
ATOM   1113 O  O   . GLU A 1 183 ? 5.29897   22.72981 20.28613  1.000 75.10318  ? 165 GLU A O   1 
ATOM   1114 C  CB  . GLU A 1 183 ? 3.54194   24.52159 22.05855  1.000 64.37607  ? 165 GLU A CB  1 
ATOM   1115 C  CG  . GLU A 1 183 ? 2.66293   24.73736 23.28102  1.000 58.62967  ? 165 GLU A CG  1 
ATOM   1116 C  CD  . GLU A 1 183 ? 1.94135   23.47290 23.72119  1.000 64.30374  ? 165 GLU A CD  1 
ATOM   1117 O  OE1 . GLU A 1 183 ? 2.13407   22.41757 23.07820  1.000 67.05962  ? 165 GLU A OE1 1 
ATOM   1118 O  OE2 . GLU A 1 183 ? 1.17543   23.53735 24.70979  1.000 53.39682  ? 165 GLU A OE2 1 
ATOM   1119 N  N   . ASP A 1 184 ? 6.68137   24.43474 20.78446  1.000 63.75925  ? 166 ASP A N   1 
ATOM   1120 C  CA  . ASP A 1 184 ? 7.42548   24.34744 19.53471  1.000 65.50807  ? 166 ASP A CA  1 
ATOM   1121 C  C   . ASP A 1 184 ? 8.80478   24.94501 19.76762  1.000 58.00550  ? 166 ASP A C   1 
ATOM   1122 O  O   . ASP A 1 184 ? 8.91741   26.07277 20.25600  1.000 65.92015  ? 166 ASP A O   1 
ATOM   1123 C  CB  . ASP A 1 184 ? 6.68331   25.09112 18.41148  1.000 72.87885  ? 166 ASP A CB  1 
ATOM   1124 C  CG  . ASP A 1 184 ? 7.51802   25.26471 17.14543  1.000 83.18170  ? 166 ASP A CG  1 
ATOM   1125 O  OD1 . ASP A 1 184 ? 8.62967   24.70133 17.03814  1.000 89.43977  ? 166 ASP A OD1 1 
ATOM   1126 O  OD2 . ASP A 1 184 ? 7.04756   25.98657 16.24189  1.000 93.57873  ? 166 ASP A OD2 1 
ATOM   1127 N  N   . GLY A 1 185 ? 9.84477   24.19829 19.40494  1.000 56.58074  ? 167 GLY A N   1 
ATOM   1128 C  CA  . GLY A 1 185 ? 11.20364  24.67882 19.56452  1.000 55.88516  ? 167 GLY A CA  1 
ATOM   1129 C  C   . GLY A 1 185 ? 11.88432  24.16055 20.81452  1.000 65.27309  ? 167 GLY A C   1 
ATOM   1130 O  O   . GLY A 1 185 ? 12.92912  23.50744 20.73296  1.000 63.37131  ? 167 GLY A O   1 
ATOM   1131 N  N   . GLY A 1 186 ? 11.30046  24.44131 21.97869  1.000 64.12138  ? 168 GLY A N   1 
ATOM   1132 C  CA  . GLY A 1 186 ? 11.88907  24.02813 23.23908  1.000 56.43148  ? 168 GLY A CA  1 
ATOM   1133 C  C   . GLY A 1 186 ? 12.81495  25.07320 23.82773  1.000 57.96296  ? 168 GLY A C   1 
ATOM   1134 O  O   . GLY A 1 186 ? 14.03920  24.96528 23.70481  1.000 51.91302  ? 168 GLY A O   1 
ATOM   1135 N  N   . GLY A 1 187 ? 12.23914  26.08886 24.47809  1.000 50.26423  ? 169 GLY A N   1 
ATOM   1136 C  CA  . GLY A 1 187 ? 13.04507  27.18193 24.99572  1.000 51.50369  ? 169 GLY A CA  1 
ATOM   1137 C  C   . GLY A 1 187 ? 13.94893  26.78361 26.14429  1.000 53.30501  ? 169 GLY A C   1 
ATOM   1138 O  O   . GLY A 1 187 ? 15.01064  27.38599 26.33811  1.000 51.94285  ? 169 GLY A O   1 
ATOM   1139 N  N   . LYS A 1 188 ? 13.54721  25.77660 26.92502  1.000 45.85425  ? 170 LYS A N   1 
ATOM   1140 C  CA  . LYS A 1 188 ? 14.41313  25.29587 27.99763  1.000 45.70125  ? 170 LYS A CA  1 
ATOM   1141 C  C   . LYS A 1 188 ? 15.73325  24.78038 27.43692  1.000 53.79367  ? 170 LYS A C   1 
ATOM   1142 O  O   . LYS A 1 188 ? 16.79319  24.96332 28.04868  1.000 49.68367  ? 170 LYS A O   1 
ATOM   1143 C  CB  . LYS A 1 188 ? 13.70266  24.20553 28.80191  1.000 41.36039  ? 170 LYS A CB  1 
ATOM   1144 C  CG  . LYS A 1 188 ? 12.38180  24.65655 29.44106  1.000 41.79179  ? 170 LYS A CG  1 
ATOM   1145 C  CD  . LYS A 1 188 ? 11.78212  23.56609 30.32158  1.000 44.39782  ? 170 LYS A CD  1 
ATOM   1146 C  CE  . LYS A 1 188 ? 10.34189  23.88784 30.74036  1.000 44.36703  ? 170 LYS A CE  1 
ATOM   1147 N  NZ  . LYS A 1 188 ? 9.52637   24.42438 29.60927  1.000 43.77983  ? 170 LYS A NZ  1 
ATOM   1148 N  N   . ILE A 1 189 ? 15.69007  24.16198 26.25490  1.000 52.44202  ? 171 ILE A N   1 
ATOM   1149 C  CA  . ILE A 1 189 ? 16.89823  23.60969 25.65355  1.000 52.23395  ? 171 ILE A CA  1 
ATOM   1150 C  C   . ILE A 1 189 ? 17.85225  24.72477 25.24233  1.000 55.18792  ? 171 ILE A C   1 
ATOM   1151 O  O   . ILE A 1 189 ? 19.07161  24.62238 25.43682  1.000 50.28734  ? 171 ILE A O   1 
ATOM   1152 C  CB  . ILE A 1 189 ? 16.52725  22.70098 24.46908  1.000 49.74696  ? 171 ILE A CB  1 
ATOM   1153 C  CG1 . ILE A 1 189 ? 15.78248  21.46338 24.97419  1.000 51.18287  ? 171 ILE A CG1 1 
ATOM   1154 C  CG2 . ILE A 1 189 ? 17.77132  22.30431 23.68624  1.000 49.88807  ? 171 ILE A CG2 1 
ATOM   1155 C  CD1 . ILE A 1 189 ? 15.10840  20.66580 23.88134  1.000 51.95262  ? 171 ILE A CD1 1 
ATOM   1156 N  N   . ASP A 1 190 ? 17.31988  25.80846 24.67413  1.000 50.03002  ? 172 ASP A N   1 
ATOM   1157 C  CA  . ASP A 1 190 ? 18.16127  26.96796 24.39331  1.000 52.25640  ? 172 ASP A CA  1 
ATOM   1158 C  C   . ASP A 1 190 ? 18.78160  27.51049 25.67535  1.000 60.04511  ? 172 ASP A C   1 
ATOM   1159 O  O   . ASP A 1 190 ? 19.94709  27.92716 25.68546  1.000 58.90308  ? 172 ASP A O   1 
ATOM   1160 C  CB  . ASP A 1 190 ? 17.34834  28.05367 23.68374  1.000 50.78263  ? 172 ASP A CB  1 
ATOM   1161 C  CG  . ASP A 1 190 ? 16.53904  27.50976 22.51353  1.000 61.95628  ? 172 ASP A CG  1 
ATOM   1162 O  OD1 . ASP A 1 190 ? 16.95344  26.49140 21.91887  1.000 74.00420  ? 172 ASP A OD1 1 
ATOM   1163 O  OD2 . ASP A 1 190 ? 15.49209  28.10360 22.18412  1.000 59.24986  ? 172 ASP A OD2 1 
ATOM   1164 N  N   . LEU A 1 191 ? 18.02157  27.49471 26.77471  1.000 56.28948  ? 173 LEU A N   1 
ATOM   1165 C  CA  . LEU A 1 191 ? 18.56220  27.95873 28.04543  1.000 52.09494  ? 173 LEU A CA  1 
ATOM   1166 C  C   . LEU A 1 191 ? 19.61168  26.99363 28.58313  1.000 49.17920  ? 173 LEU A C   1 
ATOM   1167 O  O   . LEU A 1 191 ? 20.60149  27.42311 29.18587  1.000 47.77965  ? 173 LEU A O   1 
ATOM   1168 C  CB  . LEU A 1 191 ? 17.43425  28.15252 29.05729  1.000 49.97484  ? 173 LEU A CB  1 
ATOM   1169 C  CG  . LEU A 1 191 ? 16.57501  29.39428 28.82847  1.000 53.55970  ? 173 LEU A CG  1 
ATOM   1170 C  CD1 . LEU A 1 191 ? 15.56794  29.57130 29.95626  1.000 52.31408  ? 173 LEU A CD1 1 
ATOM   1171 C  CD2 . LEU A 1 191 ? 17.44977  30.62292 28.67850  1.000 50.01249  ? 173 LEU A CD2 1 
ATOM   1172 N  N   . ILE A 1 192 ? 19.41658  25.68794 28.37341  1.000 44.05927  ? 174 ILE A N   1 
ATOM   1173 C  CA  . ILE A 1 192 ? 20.41726  24.71346 28.80038  1.000 49.68037  ? 174 ILE A CA  1 
ATOM   1174 C  C   . ILE A 1 192 ? 21.73895  24.95271 28.07684  1.000 53.56067  ? 174 ILE A C   1 
ATOM   1175 O  O   . ILE A 1 192 ? 22.81489  24.88822 28.68332  1.000 50.95568  ? 174 ILE A O   1 
ATOM   1176 C  CB  . ILE A 1 192 ? 19.90256  23.27768 28.58239  1.000 50.48809  ? 174 ILE A CB  1 
ATOM   1177 C  CG1 . ILE A 1 192 ? 18.71183  22.98679 29.49546  1.000 50.78151  ? 174 ILE A CG1 1 
ATOM   1178 C  CG2 . ILE A 1 192 ? 21.01038  22.26280 28.84704  1.000 45.63237  ? 174 ILE A CG2 1 
ATOM   1179 C  CD1 . ILE A 1 192 ? 18.03493  21.66225 29.20551  1.000 42.78112  ? 174 ILE A CD1 1 
ATOM   1180 N  N   . GLU A 1 193 ? 21.68003  25.25205 26.77585  1.000 53.47289  ? 175 GLU A N   1 
ATOM   1181 C  CA  . GLU A 1 193 ? 22.89657  25.48372 26.00184  1.000 53.78307  ? 175 GLU A CA  1 
ATOM   1182 C  C   . GLU A 1 193 ? 23.62733  26.74948 26.42691  1.000 55.80561  ? 175 GLU A C   1 
ATOM   1183 O  O   . GLU A 1 193 ? 24.82748  26.87494 26.16016  1.000 61.20254  ? 175 GLU A O   1 
ATOM   1184 C  CB  . GLU A 1 193 ? 22.57063  25.55751 24.51138  1.000 48.32635  ? 175 GLU A CB  1 
ATOM   1185 C  CG  . GLU A 1 193 ? 22.24014  24.21384 23.88524  1.000 59.13869  ? 175 GLU A CG  1 
ATOM   1186 C  CD  . GLU A 1 193 ? 21.74801  24.34338 22.45763  1.000 63.50326  ? 175 GLU A CD  1 
ATOM   1187 O  OE1 . GLU A 1 193 ? 21.66211  25.48495 21.95574  1.000 68.16166  ? 175 GLU A OE1 1 
ATOM   1188 O  OE2 . GLU A 1 193 ? 21.44246  23.30265 21.83915  1.000 70.68075  ? 175 GLU A OE2 1 
ATOM   1189 N  N   . ALA A 1 194 ? 22.93834  27.68928 27.06778  1.000 46.37699  ? 176 ALA A N   1 
ATOM   1190 C  CA  . ALA A 1 194 ? 23.58461  28.87091 27.62018  1.000 51.54428  ? 176 ALA A CA  1 
ATOM   1191 C  C   . ALA A 1 194 ? 24.09855  28.65027 29.03688  1.000 48.39736  ? 176 ALA A C   1 
ATOM   1192 O  O   . ALA A 1 194 ? 24.67368  29.57388 29.62328  1.000 47.69404  ? 176 ALA A O   1 
ATOM   1193 C  CB  . ALA A 1 194 ? 22.62258  30.06289 27.59918  1.000 40.88215  ? 176 ALA A CB  1 
ATOM   1194 N  N   . GLY A 1 195 ? 23.91618  27.45420 29.59401  1.000 50.68015  ? 177 GLY A N   1 
ATOM   1195 C  CA  . GLY A 1 195 ? 24.36233  27.17875 30.94531  1.000 51.54686  ? 177 GLY A CA  1 
ATOM   1196 C  C   . GLY A 1 195 ? 23.43089  27.65845 32.03421  1.000 54.24451  ? 177 GLY A C   1 
ATOM   1197 O  O   . GLY A 1 195 ? 23.85076  27.75924 33.18936  1.000 55.02068  ? 177 GLY A O   1 
ATOM   1198 N  N   . ALA A 1 196 ? 22.16759  27.94345 31.70631  1.000 43.55014  ? 178 ALA A N   1 
ATOM   1199 C  CA  . ALA A 1 196 ? 21.24350  28.50409 32.68748  1.000 58.75996  ? 178 ALA A CA  1 
ATOM   1200 C  C   . ALA A 1 196 ? 20.95398  27.55307 33.84290  1.000 53.21556  ? 178 ALA A C   1 
ATOM   1201 O  O   . ALA A 1 196 ? 20.59605  28.01610 34.93211  1.000 46.88658  ? 178 ALA A O   1 
ATOM   1202 C  CB  . ALA A 1 196 ? 19.93006  28.89943 32.00841  1.000 44.79437  ? 178 ALA A CB  1 
ATOM   1203 N  N   . PHE A 1 197 ? 21.09685  26.24460 33.63553  1.000 46.72266  ? 179 PHE A N   1 
ATOM   1204 C  CA  . PHE A 1 197 ? 20.74188  25.25146 34.63997  1.000 48.09967  ? 179 PHE A CA  1 
ATOM   1205 C  C   . PHE A 1 197 ? 21.95017  24.63747 35.33763  1.000 57.46912  ? 179 PHE A C   1 
ATOM   1206 O  O   . PHE A 1 197 ? 21.77146  23.81839 36.24443  1.000 61.06551  ? 179 PHE A O   1 
ATOM   1207 C  CB  . PHE A 1 197 ? 19.89877  24.14109 33.99994  1.000 42.03092  ? 179 PHE A CB  1 
ATOM   1208 C  CG  . PHE A 1 197 ? 18.54819  24.60430 33.51043  1.000 51.97332  ? 179 PHE A CG  1 
ATOM   1209 C  CD1 . PHE A 1 197 ? 18.40521  25.16987 32.25036  1.000 45.89357  ? 179 PHE A CD1 1 
ATOM   1210 C  CD2 . PHE A 1 197 ? 17.42091  24.46994 34.31030  1.000 42.97123  ? 179 PHE A CD2 1 
ATOM   1211 C  CE1 . PHE A 1 197 ? 17.15993  25.59226 31.79525  1.000 53.89429  ? 179 PHE A CE1 1 
ATOM   1212 C  CE2 . PHE A 1 197 ? 16.17532  24.89081 33.86359  1.000 41.93769  ? 179 PHE A CE2 1 
ATOM   1213 C  CZ  . PHE A 1 197 ? 16.04393  25.45452 32.60785  1.000 47.23754  ? 179 PHE A CZ  1 
ATOM   1214 N  N   . THR A 1 198 ? 23.17110  25.02102 34.95505  1.000 51.17437  ? 180 THR A N   1 
ATOM   1215 C  CA  . THR A 1 198 ? 24.36076  24.35173 35.47151  1.000 58.01928  ? 180 THR A CA  1 
ATOM   1216 C  C   . THR A 1 198 ? 24.56190  24.55073 36.97010  1.000 50.37814  ? 180 THR A C   1 
ATOM   1217 O  O   . THR A 1 198 ? 25.28562  23.76304 37.58816  1.000 59.30256  ? 180 THR A O   1 
ATOM   1218 C  CB  . THR A 1 198 ? 25.60646  24.83532 34.72661  1.000 59.78046  ? 180 THR A CB  1 
ATOM   1219 O  OG1 . THR A 1 198 ? 25.64350  26.26805 34.73485  1.000 57.82143  ? 180 THR A OG1 1 
ATOM   1220 C  CG2 . THR A 1 198 ? 25.59465  24.33856 33.28918  1.000 59.87817  ? 180 THR A CG2 1 
ATOM   1221 N  N   . ASN A 1 199 ? 23.95091  25.57629 37.56950  1.000 58.20698  ? 181 ASN A N   1 
ATOM   1222 C  CA  . ASN A 1 199 ? 24.15127  25.87919 38.98488  1.000 53.27395  ? 181 ASN A CA  1 
ATOM   1223 C  C   . ASN A 1 199 ? 22.86157  25.77594 39.79403  1.000 50.45105  ? 181 ASN A C   1 
ATOM   1224 O  O   . ASN A 1 199 ? 22.77727  26.32961 40.89437  1.000 58.60024  ? 181 ASN A O   1 
ATOM   1225 C  CB  . ASN A 1 199 ? 24.76880  27.26910 39.15457  1.000 60.20879  ? 181 ASN A CB  1 
ATOM   1226 C  CG  . ASN A 1 199 ? 25.66782  27.35934 40.36653  1.000 66.82868  ? 181 ASN A CG  1 
ATOM   1227 O  OD1 . ASN A 1 199 ? 26.26851  26.36837 40.78334  1.000 69.99770  ? 181 ASN A OD1 1 
ATOM   1228 N  ND2 . ASN A 1 199 ? 25.75640  28.54928 40.95007  1.000 75.43535  ? 181 ASN A ND2 1 
ATOM   1229 N  N   . LEU A 1 200 ? 21.85227  25.08639 39.27436  1.000 55.49827  ? 182 LEU A N   1 
ATOM   1230 C  CA  . LEU A 1 200 ? 20.62884  24.84204 40.02088  1.000 45.48168  ? 182 LEU A CA  1 
ATOM   1231 C  C   . LEU A 1 200 ? 20.71415  23.48936 40.71621  1.000 47.50792  ? 182 LEU A C   1 
ATOM   1232 O  O   . LEU A 1 200 ? 21.22334  22.51735 40.15279  1.000 55.41823  ? 182 LEU A O   1 
ATOM   1233 C  CB  . LEU A 1 200 ? 19.40724  24.88220 39.10027  1.000 43.95014  ? 182 LEU A CB  1 
ATOM   1234 C  CG  . LEU A 1 200 ? 18.95929  26.23069 38.52937  1.000 42.05579  ? 182 LEU A CG  1 
ATOM   1235 C  CD1 . LEU A 1 200 ? 17.70582  26.03384 37.67871  1.000 45.28166  ? 182 LEU A CD1 1 
ATOM   1236 C  CD2 . LEU A 1 200 ? 18.69754  27.24702 39.62330  1.000 43.83510  ? 182 LEU A CD2 1 
ATOM   1237 N  N   . ASP A 1 201 ? 20.21122  23.43064 41.94615  1.000 54.12087  ? 183 ASP A N   1 
ATOM   1238 C  CA  . ASP A 1 201 ? 20.20722  22.17273 42.68173  1.000 51.29668  ? 183 ASP A CA  1 
ATOM   1239 C  C   . ASP A 1 201 ? 18.89346  21.41704 42.52888  1.000 53.64781  ? 183 ASP A C   1 
ATOM   1240 O  O   . ASP A 1 201 ? 18.89828  20.18354 42.44100  1.000 55.16656  ? 183 ASP A O   1 
ATOM   1241 C  CB  . ASP A 1 201 ? 20.49861  22.43204 44.16105  1.000 52.94940  ? 183 ASP A CB  1 
ATOM   1242 C  CG  . ASP A 1 201 ? 21.86768  23.05260 44.38340  1.000 57.38340  ? 183 ASP A CG  1 
ATOM   1243 O  OD1 . ASP A 1 201 ? 22.88314  22.34604 44.18894  1.000 53.18579  ? 183 ASP A OD1 1 
ATOM   1244 O  OD2 . ASP A 1 201 ? 21.92676  24.24782 44.74714  1.000 55.27798  ? 183 ASP A OD2 1 
ATOM   1245 N  N   . VAL A 1 202 ? 17.76842  22.13656 42.50894  1.000 48.33881  ? 184 VAL A N   1 
ATOM   1246 C  CA  . VAL A 1 202 ? 16.43781  21.56470 42.32505  1.000 46.94259  ? 184 VAL A CA  1 
ATOM   1247 C  C   . VAL A 1 202 ? 15.63581  22.53990 41.47210  1.000 45.10113  ? 184 VAL A C   1 
ATOM   1248 O  O   . VAL A 1 202 ? 15.83094  23.75740 41.54677  1.000 45.41761  ? 184 VAL A O   1 
ATOM   1249 C  CB  . VAL A 1 202 ? 15.71366  21.29778 43.67553  1.000 50.84203  ? 184 VAL A CB  1 
ATOM   1250 C  CG1 . VAL A 1 202 ? 14.43540  20.52181 43.46056  1.000 55.53180  ? 184 VAL A CG1 1 
ATOM   1251 C  CG2 . VAL A 1 202 ? 16.60905  20.55173 44.65791  1.000 56.68169  ? 184 VAL A CG2 1 
ATOM   1252 N  N   . VAL A 1 203 ? 14.72855  22.00564 40.65178  1.000 41.25782  ? 185 VAL A N   1 
ATOM   1253 C  CA  . VAL A 1 203 ? 13.88554  22.82761 39.78927  1.000 48.37471  ? 185 VAL A CA  1 
ATOM   1254 C  C   . VAL A 1 203 ? 12.43650  22.36607 39.91612  1.000 44.39444  ? 185 VAL A C   1 
ATOM   1255 O  O   . VAL A 1 203 ? 12.15479  21.16215 39.93120  1.000 43.04994  ? 185 VAL A O   1 
ATOM   1256 C  CB  . VAL A 1 203 ? 14.36454  22.78504 38.31966  1.000 45.36601  ? 185 VAL A CB  1 
ATOM   1257 C  CG1 . VAL A 1 203 ? 14.36418  21.36195 37.78872  1.000 43.48172  ? 185 VAL A CG1 1 
ATOM   1258 C  CG2 . VAL A 1 203 ? 13.51101  23.69057 37.44887  1.000 43.23013  ? 185 VAL A CG2 1 
ATOM   1259 N  N   . PHE A 1 204 ? 11.51954  23.32990 40.02580  1.000 41.02407  ? 186 PHE A N   1 
ATOM   1260 C  CA  . PHE A 1 204 ? 10.09853  23.07309 40.22360  1.000 46.51141  ? 186 PHE A CA  1 
ATOM   1261 C  C   . PHE A 1 204 ? 9.27299   23.73611 39.12801  1.000 46.94279  ? 186 PHE A C   1 
ATOM   1262 O  O   . PHE A 1 204 ? 9.61012   24.82386 38.64884  1.000 43.95897  ? 186 PHE A O   1 
ATOM   1263 C  CB  . PHE A 1 204 ? 9.59209   23.61816 41.56988  1.000 48.08261  ? 186 PHE A CB  1 
ATOM   1264 C  CG  . PHE A 1 204 ? 10.28145  23.04974 42.77231  1.000 43.11111  ? 186 PHE A CG  1 
ATOM   1265 C  CD1 . PHE A 1 204 ? 11.38949  23.67669 43.30883  1.000 45.09191  ? 186 PHE A CD1 1 
ATOM   1266 C  CD2 . PHE A 1 204 ? 9.79520   21.90946 43.39241  1.000 53.73376  ? 186 PHE A CD2 1 
ATOM   1267 C  CE1 . PHE A 1 204 ? 12.01702  23.16550 44.43006  1.000 58.98036  ? 186 PHE A CE1 1 
ATOM   1268 C  CE2 . PHE A 1 204 ? 10.41687  21.39333 44.51251  1.000 56.74942  ? 186 PHE A CE2 1 
ATOM   1269 C  CZ  . PHE A 1 204 ? 11.52908  22.02313 45.03339  1.000 52.72044  ? 186 PHE A CZ  1 
ATOM   1270 N  N   . MET A 1 205 ? 8.16762   23.08594 38.76675  1.000 41.86484  ? 187 MET A N   1 
ATOM   1271 C  CA  . MET A 1 205 ? 7.11952   23.68264 37.94160  1.000 44.98818  ? 187 MET A CA  1 
ATOM   1272 C  C   . MET A 1 205 ? 5.90469   22.76462 38.01594  1.000 47.70732  ? 187 MET A C   1 
ATOM   1273 O  O   . MET A 1 205 ? 5.98532   21.64989 38.53691  1.000 41.36899  ? 187 MET A O   1 
ATOM   1274 C  CB  . MET A 1 205 ? 7.58147   23.90073 36.49533  1.000 38.70980  ? 187 MET A CB  1 
ATOM   1275 C  CG  . MET A 1 205 ? 7.53477   22.66798 35.60269  1.000 52.33483  ? 187 MET A CG  1 
ATOM   1276 S  SD  . MET A 1 205 ? 7.79220   23.09064 33.85813  1.000 47.98984  ? 187 MET A SD  1 
ATOM   1277 C  CE  . MET A 1 205 ? 6.09378   23.20535 33.29933  1.000 43.82265  ? 187 MET A CE  1 
ATOM   1278 N  N   . ALA A 1 206 ? 4.77038   23.24765 37.50558  1.000 39.42496  ? 188 ALA A N   1 
ATOM   1279 C  CA  . ALA A 1 206 ? 3.54390   22.45774 37.53097  1.000 47.83628  ? 188 ALA A CA  1 
ATOM   1280 C  C   . ALA A 1 206 ? 2.71509   22.75505 36.28712  1.000 47.92219  ? 188 ALA A C   1 
ATOM   1281 O  O   . ALA A 1 206 ? 2.81730   23.82921 35.68936  1.000 45.58350  ? 188 ALA A O   1 
ATOM   1282 C  CB  . ALA A 1 206 ? 2.72282   22.72694 38.80276  1.000 39.46533  ? 188 ALA A CB  1 
ATOM   1283 N  N   . HIS A 1 207 ? 1.86096   21.79515 35.92063  1.000 45.03087  ? 189 HIS A N   1 
ATOM   1284 C  CA  . HIS A 1 207 ? 1.14071   21.85770 34.65351  1.000 54.92903  ? 189 HIS A CA  1 
ATOM   1285 C  C   . HIS A 1 207 ? -0.33124  21.49450 34.81489  1.000 51.54011  ? 189 HIS A C   1 
ATOM   1286 O  O   . HIS A 1 207 ? -0.65206  20.39459 35.28135  1.000 53.21573  ? 189 HIS A O   1 
ATOM   1287 C  CB  . HIS A 1 207 ? 1.80086   20.92388 33.64387  1.000 41.99050  ? 189 HIS A CB  1 
ATOM   1288 C  CG  . HIS A 1 207 ? 1.46530   21.23107 32.21893  1.000 60.45204  ? 189 HIS A CG  1 
ATOM   1289 N  ND1 . HIS A 1 207 ? 0.17027   21.40526 31.77610  1.000 59.99141  ? 189 HIS A ND1 1 
ATOM   1290 C  CD2 . HIS A 1 207 ? 2.25828   21.37679 31.13089  1.000 50.50032  ? 189 HIS A CD2 1 
ATOM   1291 C  CE1 . HIS A 1 207 ? 0.18047   21.65210 30.47802  1.000 51.55974  ? 189 HIS A CE1 1 
ATOM   1292 N  NE2 . HIS A 1 207 ? 1.43513   21.63997 30.06352  1.000 57.33402  ? 189 HIS A NE2 1 
ATOM   1293 N  N   . PRO A 1 208 ? -1.25332  22.37039 34.42503  1.000 50.05331  ? 190 PRO A N   1 
ATOM   1294 C  CA  . PRO A 1 208 ? -2.67671  22.05322 34.58783  1.000 52.99166  ? 190 PRO A CA  1 
ATOM   1295 C  C   . PRO A 1 208 ? -3.11124  20.97246 33.60954  1.000 55.23821  ? 190 PRO A C   1 
ATOM   1296 O  O   . PRO A 1 208 ? -2.76320  21.00257 32.42685  1.000 50.37693  ? 190 PRO A O   1 
ATOM   1297 C  CB  . PRO A 1 208 ? -3.36421  23.39257 34.29657  1.000 48.19220  ? 190 PRO A CB  1 
ATOM   1298 C  CG  . PRO A 1 208 ? -2.44015  24.04385 33.31210  1.000 51.02897  ? 190 PRO A CG  1 
ATOM   1299 C  CD  . PRO A 1 208 ? -1.06008  23.70670 33.83662  1.000 47.15567  ? 190 PRO A CD  1 
ATOM   1300 N  N   A SER A 1 209 ? -3.87636  20.00918 34.12056  0.605 51.77656  ? 191 SER A N   1 
ATOM   1301 N  N   B SER A 1 209 ? -3.87469  20.00622 34.12074  0.395 54.40094  ? 191 SER A N   1 
ATOM   1302 C  CA  A SER A 1 209 ? -4.35079  18.89158 33.31361  0.605 56.83355  ? 191 SER A CA  1 
ATOM   1303 C  CA  B SER A 1 209 ? -4.35264  18.89211 33.30944  0.395 56.85062  ? 191 SER A CA  1 
ATOM   1304 C  C   A SER A 1 209 ? -5.79514  18.55473 33.66612  0.605 60.87831  ? 191 SER A C   1 
ATOM   1305 C  C   B SER A 1 209 ? -5.79785  18.55516 33.65751  0.395 60.84344  ? 191 SER A C   1 
ATOM   1306 O  O   A SER A 1 209 ? -6.63168  19.45338 33.80021  0.605 60.14389  ? 191 SER A O   1 
ATOM   1307 O  O   B SER A 1 209 ? -6.63680  19.45292 33.78164  0.395 60.08470  ? 191 SER A O   1 
ATOM   1308 C  CB  A SER A 1 209 ? -3.44808  17.67148 33.51156  0.605 57.35367  ? 191 SER A CB  1 
ATOM   1309 C  CB  B SER A 1 209 ? -3.46117  17.66421 33.50486  0.395 56.33244  ? 191 SER A CB  1 
ATOM   1310 O  OG  A SER A 1 209 ? -3.90593  16.56433 32.75723  0.605 57.04427  ? 191 SER A OG  1 
ATOM   1311 O  OG  B SER A 1 209 ? -3.49469  17.22549 34.85255  0.395 59.17369  ? 191 SER A OG  1 
ATOM   1312 N  N   . GLN A 1 210 ? -6.09872  17.26339 33.81923  1.000 64.20254  ? 192 GLN A N   1 
ATOM   1313 C  CA  . GLN A 1 210 ? -7.43408  16.82190 34.19907  1.000 69.42810  ? 192 GLN A CA  1 
ATOM   1314 C  C   . GLN A 1 210 ? -7.49369  16.17489 35.57482  1.000 79.72735  ? 192 GLN A C   1 
ATOM   1315 O  O   . GLN A 1 210 ? -8.57241  16.14214 36.17565  1.000 86.78546  ? 192 GLN A O   1 
ATOM   1316 C  CB  . GLN A 1 210 ? -7.99466  15.83142 33.16614  1.000 63.09559  ? 192 GLN A CB  1 
ATOM   1317 C  CG  . GLN A 1 210 ? -8.40826  16.46287 31.84779  1.000 60.41175  ? 192 GLN A CG  1 
ATOM   1318 C  CD  . GLN A 1 210 ? -7.21769  16.75293 30.95198  1.000 80.76206  ? 192 GLN A CD  1 
ATOM   1319 O  OE1 . GLN A 1 210 ? -6.43844  15.85595 30.62849  1.000 81.96578  ? 192 GLN A OE1 1 
ATOM   1320 N  NE2 . GLN A 1 210 ? -7.06779  18.01126 30.55053  1.000 83.24714  ? 192 GLN A NE2 1 
ATOM   1321 N  N   . GLU A 1 211 ? -6.37482  15.66477 36.08661  1.000 83.31584  ? 193 GLU A N   1 
ATOM   1322 C  CA  . GLU A 1 211 ? -6.32851  15.05712 37.40945  1.000 92.26805  ? 193 GLU A CA  1 
ATOM   1323 C  C   . GLU A 1 211 ? -5.04908  15.50699 38.10882  1.000 87.77963  ? 193 GLU A C   1 
ATOM   1324 O  O   . GLU A 1 211 ? -4.20335  16.19186 37.52270  1.000 75.65260  ? 193 GLU A O   1 
ATOM   1325 C  CB  . GLU A 1 211 ? -6.42304  13.52860 37.31833  1.000 84.04238  ? 193 GLU A CB  1 
ATOM   1326 N  N   . ASN A 1 212 ? -4.91294  15.12607 39.37878  1.000 91.65534  ? 194 ASN A N   1 
ATOM   1327 C  CA  . ASN A 1 212 ? -3.76071  15.49155 40.19609  1.000 85.40810  ? 194 ASN A CA  1 
ATOM   1328 C  C   . ASN A 1 212 ? -2.79766  14.31059 40.26542  1.000 90.06750  ? 194 ASN A C   1 
ATOM   1329 O  O   . ASN A 1 212 ? -3.16811  13.22941 40.73677  1.000 95.66757  ? 194 ASN A O   1 
ATOM   1330 C  CB  . ASN A 1 212 ? -4.19755  15.90870 41.60109  1.000 80.69293  ? 194 ASN A CB  1 
ATOM   1331 C  CG  . ASN A 1 212 ? -5.17761  17.06845 41.59050  1.000 76.82961  ? 194 ASN A CG  1 
ATOM   1332 O  OD1 . ASN A 1 212 ? -4.88568  18.13991 41.05858  1.000 63.54807  ? 194 ASN A OD1 1 
ATOM   1333 N  ND2 . ASN A 1 212 ? -6.34718  16.86048 42.18860  1.000 82.47295  ? 194 ASN A ND2 1 
ATOM   1334 N  N   . ALA A 1 213 ? -1.56603  14.51985 39.80237  1.000 86.10303  ? 195 ALA A N   1 
ATOM   1335 C  CA  . ALA A 1 213 ? -0.55232  13.47207 39.80410  1.000 82.11756  ? 195 ALA A CA  1 
ATOM   1336 C  C   . ALA A 1 213 ? 0.81526   14.10699 39.99422  1.000 78.73217  ? 195 ALA A C   1 
ATOM   1337 O  O   . ALA A 1 213 ? 1.15630   15.06298 39.29117  1.000 77.98714  ? 195 ALA A O   1 
ATOM   1338 C  CB  . ALA A 1 213 ? -0.58483  12.66277 38.50171  1.000 78.22278  ? 195 ALA A CB  1 
ATOM   1339 N  N   . ALA A 1 214 ? 1.59283   13.57347 40.94171  1.000 85.42614  ? 196 ALA A N   1 
ATOM   1340 C  CA  . ALA A 1 214 ? 2.93869   14.08444 41.18146  1.000 77.29525  ? 196 ALA A CA  1 
ATOM   1341 C  C   . ALA A 1 214 ? 3.88070   13.80420 40.02019  1.000 80.16049  ? 196 ALA A C   1 
ATOM   1342 O  O   . ALA A 1 214 ? 4.90295   14.48622 39.89285  1.000 72.99776  ? 196 ALA A O   1 
ATOM   1343 C  CB  . ALA A 1 214 ? 3.51545   13.48479 42.46270  1.000 70.86403  ? 196 ALA A CB  1 
ATOM   1344 N  N   . TYR A 1 215 ? 3.56304   12.81826 39.18121  1.000 87.47801  ? 197 TYR A N   1 
ATOM   1345 C  CA  . TYR A 1 215 ? 4.36657   12.49085 38.01310  1.000 87.75553  ? 197 TYR A CA  1 
ATOM   1346 C  C   . TYR A 1 215 ? 3.47069   11.81562 36.98449  1.000 85.63856  ? 197 TYR A C   1 
ATOM   1347 O  O   . TYR A 1 215 ? 2.54315   11.08085 37.33703  1.000 75.95729  ? 197 TYR A O   1 
ATOM   1348 C  CB  . TYR A 1 215 ? 5.56286   11.59039 38.38075  1.000 73.71693  ? 197 TYR A CB  1 
ATOM   1349 C  CG  . TYR A 1 215 ? 6.15373   10.79895 37.22195  1.000 89.68778  ? 197 TYR A CG  1 
ATOM   1350 C  CD1 . TYR A 1 215 ? 5.65910   9.54303  36.87425  1.000 95.95910  ? 197 TYR A CD1 1 
ATOM   1351 C  CD2 . TYR A 1 215 ? 7.20366   11.31618 36.46924  1.000 88.02039  ? 197 TYR A CD2 1 
ATOM   1352 C  CE1 . TYR A 1 215 ? 6.19902   8.82867  35.81306  1.000 91.87372  ? 197 TYR A CE1 1 
ATOM   1353 C  CE2 . TYR A 1 215 ? 7.74765   10.60871 35.40911  1.000 79.03837  ? 197 TYR A CE2 1 
ATOM   1354 C  CZ  . TYR A 1 215 ? 7.24214   9.36800  35.08671  1.000 84.54036  ? 197 TYR A CZ  1 
ATOM   1355 O  OH  . TYR A 1 215 ? 7.78269   8.66490  34.03533  1.000 92.54425  ? 197 TYR A OH  1 
ATOM   1356 N  N   . LEU A 1 216 ? 3.75523   12.07786 35.70618  1.000 82.09067  ? 198 LEU A N   1 
ATOM   1357 C  CA  . LEU A 1 216 ? 3.08123   11.41872 34.59467  1.000 87.11170  ? 198 LEU A CA  1 
ATOM   1358 C  C   . LEU A 1 216 ? 4.08761   11.20069 33.47213  1.000 85.72297  ? 198 LEU A C   1 
ATOM   1359 O  O   . LEU A 1 216 ? 4.92267   12.07917 33.20777  1.000 83.91376  ? 198 LEU A O   1 
ATOM   1360 C  CB  . LEU A 1 216 ? 1.88574   12.22987 34.07724  1.000 78.94075  ? 198 LEU A CB  1 
ATOM   1361 C  CG  . LEU A 1 216 ? 0.55010   11.96454 34.77744  1.000 75.46754  ? 198 LEU A CG  1 
ATOM   1362 C  CD1 . LEU A 1 216 ? -0.60799  12.56766 33.99019  1.000 71.01119  ? 198 LEU A CD1 1 
ATOM   1363 C  CD2 . LEU A 1 216 ? 0.34035   10.47403 35.00782  1.000 74.76621  ? 198 LEU A CD2 1 
ATOM   1364 N  N   . PRO A 1 217 ? 4.03503   10.04429 32.79681  1.000 94.19324  ? 199 PRO A N   1 
ATOM   1365 C  CA  . PRO A 1 217 ? 5.08375   9.70496  31.82066  1.000 88.07225  ? 199 PRO A CA  1 
ATOM   1366 C  C   . PRO A 1 217 ? 5.03013   10.50978 30.52892  1.000 81.73147  ? 199 PRO A C   1 
ATOM   1367 O  O   . PRO A 1 217 ? 4.19461   10.25078 29.65513  1.000 86.67171  ? 199 PRO A O   1 
ATOM   1368 C  CB  . PRO A 1 217 ? 4.84015   8.21187  31.54681  1.000 77.91800  ? 199 PRO A CB  1 
ATOM   1369 C  CG  . PRO A 1 217 ? 3.92867   7.74086  32.65248  1.000 88.64020  ? 199 PRO A CG  1 
ATOM   1370 C  CD  . PRO A 1 217 ? 3.10013   8.92860  33.01301  1.000 89.77979  ? 199 PRO A CD  1 
ATOM   1371 N  N   . ASP A 1 218 ? 5.93136   11.48068 30.39749  1.000 73.22352  ? 200 ASP A N   1 
ATOM   1372 C  CA  . ASP A 1 218 ? 6.16856   12.17722 29.13941  1.000 67.36153  ? 200 ASP A CA  1 
ATOM   1373 C  C   . ASP A 1 218 ? 7.34434   11.51720 28.43088  1.000 61.81096  ? 200 ASP A C   1 
ATOM   1374 O  O   . ASP A 1 218 ? 8.39848   11.29943 29.03809  1.000 57.10802  ? 200 ASP A O   1 
ATOM   1375 C  CB  . ASP A 1 218 ? 6.45343   13.66159 29.37399  1.000 62.18746  ? 200 ASP A CB  1 
ATOM   1376 C  CG  . ASP A 1 218 ? 5.22420   14.42682 29.83389  1.000 73.99680  ? 200 ASP A CG  1 
ATOM   1377 O  OD1 . ASP A 1 218 ? 4.26402   14.54729 29.04445  1.000 84.15808  ? 200 ASP A OD1 1 
ATOM   1378 O  OD2 . ASP A 1 218 ? 5.21828   14.91019 30.98597  1.000 71.49185  ? 200 ASP A OD2 1 
ATOM   1379 N  N   . MET A 1 219 ? 7.16543   11.20632 27.15327  1.000 58.53958  ? 201 MET A N   1 
ATOM   1380 C  CA  . MET A 1 219 ? 8.13579   10.40870 26.42114  1.000 55.28347  ? 201 MET A CA  1 
ATOM   1381 C  C   . MET A 1 219 ? 9.15144   11.29856 25.70971  1.000 54.07295  ? 201 MET A C   1 
ATOM   1382 O  O   . MET A 1 219 ? 8.96310   12.50749 25.55792  1.000 56.33712  ? 201 MET A O   1 
ATOM   1383 C  CB  . MET A 1 219 ? 7.42250   9.51296  25.40870  1.000 58.80553  ? 201 MET A CB  1 
ATOM   1384 C  CG  . MET A 1 219 ? 6.65800   8.35643  26.02960  1.000 57.98488  ? 201 MET A CG  1 
ATOM   1385 S  SD  . MET A 1 219 ? 6.06523   7.19351  24.78981  1.000 66.32539  ? 201 MET A SD  1 
ATOM   1386 C  CE  . MET A 1 219 ? 4.64158   8.06465  24.14930  1.000 52.06930  ? 201 MET A CE  1 
ATOM   1387 N  N   . ALA A 1 220 ? 10.24482  10.67917 25.26888  1.000 45.49888  ? 202 ALA A N   1 
ATOM   1388 C  CA  . ALA A 1 220 ? 11.17246  11.35896 24.37868  1.000 51.53439  ? 202 ALA A CA  1 
ATOM   1389 C  C   . ALA A 1 220 ? 10.54700  11.51675 22.99480  1.000 55.75686  ? 202 ALA A C   1 
ATOM   1390 O  O   . ALA A 1 220 ? 9.60446   10.81120 22.62980  1.000 51.06141  ? 202 ALA A O   1 
ATOM   1391 C  CB  . ALA A 1 220 ? 12.48970  10.59115 24.27752  1.000 47.30748  ? 202 ALA A CB  1 
ATOM   1392 N  N   . GLU A 1 221 ? 11.07961  12.46206 22.22076  1.000 54.39029  ? 203 GLU A N   1 
ATOM   1393 C  CA  . GLU A 1 221 ? 10.51660  12.77352 20.91536  1.000 56.21180  ? 203 GLU A CA  1 
ATOM   1394 C  C   . GLU A 1 221 ? 11.62733  13.15345 19.94829  1.000 58.97064  ? 203 GLU A C   1 
ATOM   1395 O  O   . GLU A 1 221 ? 12.59752  13.81101 20.33290  1.000 58.36805  ? 203 GLU A O   1 
ATOM   1396 C  CB  . GLU A 1 221 ? 9.49066   13.90909 21.00279  1.000 56.42135  ? 203 GLU A CB  1 
ATOM   1397 C  CG  . GLU A 1 221 ? 8.82490   14.24558 19.67356  1.000 62.21320  ? 203 GLU A CG  1 
ATOM   1398 C  CD  . GLU A 1 221 ? 7.73711   15.29332 19.80167  1.000 59.48865  ? 203 GLU A CD  1 
ATOM   1399 O  OE1 . GLU A 1 221 ? 7.02498   15.29300 20.82617  1.000 73.38021  ? 203 GLU A OE1 1 
ATOM   1400 O  OE2 . GLU A 1 221 ? 7.59821   16.12266 18.87715  1.000 64.37221  ? 203 GLU A OE2 1 
ATOM   1401 N  N   . HIS A 1 222 ? 11.47175  12.73420 18.69209  1.000 58.86892  ? 204 HIS A N   1 
ATOM   1402 C  CA  . HIS A 1 222 ? 12.38663  13.09331 17.61284  1.000 51.84063  ? 204 HIS A CA  1 
ATOM   1403 C  C   . HIS A 1 222 ? 11.55835  13.50731 16.40613  1.000 56.97370  ? 204 HIS A C   1 
ATOM   1404 O  O   . HIS A 1 222 ? 10.69253  12.74950 15.95783  1.000 55.01030  ? 204 HIS A O   1 
ATOM   1405 C  CB  . HIS A 1 222 ? 13.31482  11.92418 17.26247  1.000 56.92233  ? 204 HIS A CB  1 
ATOM   1406 C  CG  . HIS A 1 222 ? 14.24253  12.20284 16.11975  1.000 58.19455  ? 204 HIS A CG  1 
ATOM   1407 N  ND1 . HIS A 1 222 ? 15.21005  13.18279 16.16773  1.000 57.10738  ? 204 HIS A ND1 1 
ATOM   1408 C  CD2 . HIS A 1 222 ? 14.36066  11.61829 14.90342  1.000 59.67118  ? 204 HIS A CD2 1 
ATOM   1409 C  CE1 . HIS A 1 222 ? 15.87902  13.19629 15.02839  1.000 56.18468  ? 204 HIS A CE1 1 
ATOM   1410 N  NE2 . HIS A 1 222 ? 15.38537  12.25466 14.24475  1.000 54.44473  ? 204 HIS A NE2 1 
ATOM   1411 N  N   . ASP A 1 223 ? 11.80859  14.70896 15.89699  1.000 60.73093  ? 205 ASP A N   1 
ATOM   1412 C  CA  . ASP A 1 223 ? 11.13089  15.22623 14.71782  1.000 53.98571  ? 205 ASP A CA  1 
ATOM   1413 C  C   . ASP A 1 223 ? 11.99359  15.01050 13.48422  1.000 54.76412  ? 205 ASP A C   1 
ATOM   1414 O  O   . ASP A 1 223 ? 13.22398  14.98746 13.56439  1.000 54.64533  ? 205 ASP A O   1 
ATOM   1415 C  CB  . ASP A 1 223 ? 10.82408  16.71667 14.86654  1.000 52.25892  ? 205 ASP A CB  1 
ATOM   1416 C  CG  . ASP A 1 223 ? 9.81870   16.99811 15.95688  1.000 55.86521  ? 205 ASP A CG  1 
ATOM   1417 O  OD1 . ASP A 1 223 ? 9.20350   16.03650 16.46447  1.000 55.84226  ? 205 ASP A OD1 1 
ATOM   1418 O  OD2 . ASP A 1 223 ? 9.64610   18.18440 16.30753  1.000 65.18604  ? 205 ASP A OD2 1 
ATOM   1419 N  N   . VAL A 1 224 ? 11.33733  14.86173 12.33331  1.000 55.14815  ? 206 VAL A N   1 
ATOM   1420 C  CA  . VAL A 1 224 ? 12.04831  14.67570 11.07405  1.000 47.75989  ? 206 VAL A CA  1 
ATOM   1421 C  C   . VAL A 1 224 ? 11.21677  15.25041 9.93567   1.000 52.66466  ? 206 VAL A C   1 
ATOM   1422 O  O   . VAL A 1 224 ? 9.98127   15.26280 9.98128   1.000 49.72887  ? 206 VAL A O   1 
ATOM   1423 C  CB  . VAL A 1 224 ? 12.38917  13.18489 10.83458  1.000 48.19980  ? 206 VAL A CB  1 
ATOM   1424 C  CG1 . VAL A 1 224 ? 11.21739  12.44436 10.20080  1.000 58.26027  ? 206 VAL A CG1 1 
ATOM   1425 C  CG2 . VAL A 1 224 ? 13.62918  13.06268 9.98614   1.000 57.50298  ? 206 VAL A CG2 1 
ATOM   1426 N  N   . THR A 1 225 ? 11.91345  15.75798 8.92125   1.000 55.11004  ? 207 THR A N   1 
ATOM   1427 C  CA  . THR A 1 225 ? 11.30990  16.21199 7.67442   1.000 53.61503  ? 207 THR A CA  1 
ATOM   1428 C  C   . THR A 1 225 ? 11.96443  15.45436 6.53104   1.000 55.56720  ? 207 THR A C   1 
ATOM   1429 O  O   . THR A 1 225 ? 13.19360  15.46510 6.40291   1.000 51.40478  ? 207 THR A O   1 
ATOM   1430 C  CB  . THR A 1 225 ? 11.48259  17.72075 7.47363   1.000 54.23980  ? 207 THR A CB  1 
ATOM   1431 O  OG1 . THR A 1 225 ? 10.67066  18.42582 8.42021   1.000 61.55185  ? 207 THR A OG1 1 
ATOM   1432 C  CG2 . THR A 1 225 ? 11.05677  18.12010 6.06125   1.000 48.62275  ? 207 THR A CG2 1 
ATOM   1433 N  N   . VAL A 1 226 ? 11.14779  14.79748 5.70963   1.000 54.39423  ? 208 VAL A N   1 
ATOM   1434 C  CA  . VAL A 1 226 ? 11.62302  13.93248 4.63395   1.000 47.43261  ? 208 VAL A CA  1 
ATOM   1435 C  C   . VAL A 1 226 ? 11.24030  14.55489 3.29842   1.000 52.37793  ? 208 VAL A C   1 
ATOM   1436 O  O   . VAL A 1 226 ? 10.06417  14.85606 3.06080   1.000 52.92176  ? 208 VAL A O   1 
ATOM   1437 C  CB  . VAL A 1 226 ? 11.04408  12.51280 4.76157   1.000 49.11942  ? 208 VAL A CB  1 
ATOM   1438 C  CG1 . VAL A 1 226 ? 11.57455  11.61886 3.64911   1.000 43.79763  ? 208 VAL A CG1 1 
ATOM   1439 C  CG2 . VAL A 1 226 ? 11.35776  11.92899 6.13821   1.000 43.17895  ? 208 VAL A CG2 1 
ATOM   1440 N  N   . LYS A 1 227 ? 12.22808  14.73254 2.42407   1.000 49.66801  ? 209 LYS A N   1 
ATOM   1441 C  CA  . LYS A 1 227 ? 12.02495  15.31797 1.10495   1.000 53.97911  ? 209 LYS A CA  1 
ATOM   1442 C  C   . LYS A 1 227 ? 12.51507  14.35106 0.03463   1.000 47.51199  ? 209 LYS A C   1 
ATOM   1443 O  O   . LYS A 1 227 ? 13.63881  13.84577 0.11711   1.000 49.67250  ? 209 LYS A O   1 
ATOM   1444 C  CB  . LYS A 1 227 ? 12.75255  16.66349 0.98821   1.000 51.89159  ? 209 LYS A CB  1 
ATOM   1445 C  CG  . LYS A 1 227 ? 12.09641  17.78428 1.79008   1.000 60.90901  ? 209 LYS A CG  1 
ATOM   1446 C  CD  . LYS A 1 227 ? 12.90681  19.07667 1.76586   1.000 56.28478  ? 209 LYS A CD  1 
ATOM   1447 C  CE  . LYS A 1 227 ? 12.28624  20.11149 2.69830   1.000 60.32804  ? 209 LYS A CE  1 
ATOM   1448 N  NZ  . LYS A 1 227 ? 13.05279  21.38756 2.75466   1.000 57.58776  ? 209 LYS A NZ  1 
ATOM   1449 N  N   . TYR A 1 228 ? 11.67595  14.09912 -0.96660  1.000 47.82397  ? 210 TYR A N   1 
ATOM   1450 C  CA  . TYR A 1 228 ? 12.00873  13.20990 -2.07120  1.000 52.18734  ? 210 TYR A CA  1 
ATOM   1451 C  C   . TYR A 1 228 ? 12.17108  14.01422 -3.35324  1.000 50.28198  ? 210 TYR A C   1 
ATOM   1452 O  O   . TYR A 1 228 ? 11.39564  14.93773 -3.61855  1.000 55.03463  ? 210 TYR A O   1 
ATOM   1453 C  CB  . TYR A 1 228 ? 10.92779  12.14333 -2.25987  1.000 47.75530  ? 210 TYR A CB  1 
ATOM   1454 C  CG  . TYR A 1 228 ? 10.95199  11.05862 -1.20677  1.000 46.18765  ? 210 TYR A CG  1 
ATOM   1455 C  CD1 . TYR A 1 228 ? 11.97207  10.11641 -1.17482  1.000 42.35973  ? 210 TYR A CD1 1 
ATOM   1456 C  CD2 . TYR A 1 228 ? 9.95431   10.97991 -0.24048  1.000 46.93564  ? 210 TYR A CD2 1 
ATOM   1457 C  CE1 . TYR A 1 228 ? 11.99516  9.12073  -0.21324  1.000 49.47074  ? 210 TYR A CE1 1 
ATOM   1458 C  CE2 . TYR A 1 228 ? 9.96718   9.98975  0.72656   1.000 46.85630  ? 210 TYR A CE2 1 
ATOM   1459 C  CZ  . TYR A 1 228 ? 10.99291  9.06429  0.73707   1.000 49.98321  ? 210 TYR A CZ  1 
ATOM   1460 O  OH  . TYR A 1 228 ? 11.01618  8.07817  1.69544   1.000 43.93383  ? 210 TYR A OH  1 
ATOM   1461 N  N   . TYR A 1 229 ? 13.17627  13.65293 -4.15017  1.000 58.82259  ? 211 TYR A N   1 
ATOM   1462 C  CA  . TYR A 1 229 ? 13.49278  14.34894 -5.39435  1.000 56.13947  ? 211 TYR A CA  1 
ATOM   1463 C  C   . TYR A 1 229 ? 13.60211  13.33661 -6.52032  1.000 57.35480  ? 211 TYR A C   1 
ATOM   1464 O  O   . TYR A 1 229 ? 14.39446  12.39311 -6.43117  1.000 54.44818  ? 211 TYR A O   1 
ATOM   1465 C  CB  . TYR A 1 229 ? 14.80123  15.13009 -5.28051  1.000 55.88864  ? 211 TYR A CB  1 
ATOM   1466 C  CG  . TYR A 1 229 ? 14.88212  16.05020 -4.08887  1.000 65.94604  ? 211 TYR A CG  1 
ATOM   1467 C  CD1 . TYR A 1 229 ? 14.43762  17.36181 -4.17161  1.000 72.04364  ? 211 TYR A CD1 1 
ATOM   1468 C  CD2 . TYR A 1 229 ? 15.42058  15.61431 -2.88588  1.000 66.00842  ? 211 TYR A CD2 1 
ATOM   1469 C  CE1 . TYR A 1 229 ? 14.51618  18.21198 -3.08640  1.000 69.67563  ? 211 TYR A CE1 1 
ATOM   1470 C  CE2 . TYR A 1 229 ? 15.50297  16.45667 -1.79511  1.000 66.87292  ? 211 TYR A CE2 1 
ATOM   1471 C  CZ  . TYR A 1 229 ? 15.04921  17.75470 -1.90168  1.000 67.22618  ? 211 TYR A CZ  1 
ATOM   1472 O  OH  . TYR A 1 229 ? 15.12838  18.59785 -0.81880  1.000 76.27639  ? 211 TYR A OH  1 
ATOM   1473 N  N   . GLY A 1 230 ? 12.82840  13.54361 -7.58293  1.000 52.68736  ? 212 GLY A N   1 
ATOM   1474 C  CA  . GLY A 1 230 ? 12.89969  12.67632 -8.74090  1.000 50.06155  ? 212 GLY A CA  1 
ATOM   1475 C  C   . GLY A 1 230 ? 13.28107  13.41037 -10.00997 1.000 71.51452  ? 212 GLY A C   1 
ATOM   1476 O  O   . GLY A 1 230 ? 14.20495  14.23154 -10.01292 1.000 64.19414  ? 212 GLY A O   1 
ATOM   1477 N  N   . LYS A 1 231 ? 12.57302  13.11546 -11.09881 1.000 80.08202  ? 213 LYS A N   1 
ATOM   1478 C  CA  . LYS A 1 231 ? 12.79055  13.77925 -12.37675 1.000 90.30592  ? 213 LYS A CA  1 
ATOM   1479 C  C   . LYS A 1 231 ? 11.45356  13.86794 -13.09491 1.000 92.58306  ? 213 LYS A C   1 
ATOM   1480 O  O   . LYS A 1 231 ? 10.70504  12.88740 -13.13432 1.000 88.97448  ? 213 LYS A O   1 
ATOM   1481 C  CB  . LYS A 1 231 ? 13.81850  13.02851 -13.23515 1.000 80.67208  ? 213 LYS A CB  1 
ATOM   1482 N  N   . ALA A 1 232 ? 11.15624  15.03915 -13.65142 1.000 101.07730 ? 214 ALA A N   1 
ATOM   1483 C  CA  . ALA A 1 232 ? 9.86191   15.28128 -14.28325 1.000 92.58689  ? 214 ALA A CA  1 
ATOM   1484 C  C   . ALA A 1 232 ? 9.82095   14.75852 -15.71587 1.000 89.09925  ? 214 ALA A C   1 
ATOM   1485 O  O   . ALA A 1 232 ? 10.85463  14.45868 -16.31074 1.000 91.24145  ? 214 ALA A O   1 
ATOM   1486 C  CB  . ALA A 1 232 ? 9.53002   16.76929 -14.25312 1.000 83.24992  ? 214 ALA A CB  1 
ATOM   1487 N  N   . TYR A 1 238 ? 7.74951   11.67010 -21.87007 1.000 81.33504  ? 220 TYR A N   1 
ATOM   1488 C  CA  . TYR A 1 238 ? 6.63632   10.80298 -21.50105 1.000 100.40280 ? 220 TYR A CA  1 
ATOM   1489 C  C   . TYR A 1 238 ? 6.88079   10.20867 -20.11176 1.000 105.47903 ? 220 TYR A C   1 
ATOM   1490 O  O   . TYR A 1 238 ? 8.01895   10.20068 -19.63933 1.000 108.82797 ? 220 TYR A O   1 
ATOM   1491 C  CB  . TYR A 1 238 ? 6.45048   9.70644  -22.55223 1.000 98.36541  ? 220 TYR A CB  1 
ATOM   1492 N  N   . PRO A 1 239 ? 5.82108   9.72586  -19.45090 1.000 102.24242 ? 221 PRO A N   1 
ATOM   1493 C  CA  . PRO A 1 239 ? 5.97260   9.27251  -18.05684 1.000 91.39149  ? 221 PRO A CA  1 
ATOM   1494 C  C   . PRO A 1 239 ? 6.93331   8.10534  -17.86825 1.000 93.83082  ? 221 PRO A C   1 
ATOM   1495 O  O   . PRO A 1 239 ? 7.35414   7.86382  -16.72862 1.000 80.47566  ? 221 PRO A O   1 
ATOM   1496 C  CB  . PRO A 1 239 ? 4.53698   8.89347  -17.65892 1.000 74.20771  ? 221 PRO A CB  1 
ATOM   1497 C  CG  . PRO A 1 239 ? 3.85192   8.62450  -18.95504 1.000 87.45353  ? 221 PRO A CG  1 
ATOM   1498 C  CD  . PRO A 1 239 ? 4.40920   9.67317  -19.86614 1.000 97.83277  ? 221 PRO A CD  1 
ATOM   1499 N  N   . TRP A 1 240 ? 7.29612   7.37447  -18.93060 1.000 100.82254 ? 222 TRP A N   1 
ATOM   1500 C  CA  . TRP A 1 240 ? 8.32657   6.34725  -18.78824 1.000 88.24981  ? 222 TRP A CA  1 
ATOM   1501 C  C   . TRP A 1 240 ? 9.62260   6.97007  -18.28205 1.000 96.02471  ? 222 TRP A C   1 
ATOM   1502 O  O   . TRP A 1 240 ? 10.24250  6.46893  -17.33694 1.000 100.35178 ? 222 TRP A O   1 
ATOM   1503 C  CB  . TRP A 1 240 ? 8.57812   5.61112  -20.11250 1.000 85.14747  ? 222 TRP A CB  1 
ATOM   1504 C  CG  . TRP A 1 240 ? 7.69631   5.98907  -21.27687 1.000 87.00740  ? 222 TRP A CG  1 
ATOM   1505 C  CD1 . TRP A 1 240 ? 8.10984   6.46469  -22.48690 1.000 90.79116  ? 222 TRP A CD1 1 
ATOM   1506 C  CD2 . TRP A 1 240 ? 6.26637   5.88152  -21.35664 1.000 100.84629 ? 222 TRP A CD2 1 
ATOM   1507 N  NE1 . TRP A 1 240 ? 7.02833   6.68194  -23.30681 1.000 103.84047 ? 222 TRP A NE1 1 
ATOM   1508 C  CE2 . TRP A 1 240 ? 5.88505   6.33386  -22.63701 1.000 100.55789 ? 222 TRP A CE2 1 
ATOM   1509 C  CE3 . TRP A 1 240 ? 5.27133   5.46196  -20.46511 1.000 104.10075 ? 222 TRP A CE3 1 
ATOM   1510 C  CZ2 . TRP A 1 240 ? 4.55324   6.37720  -23.04947 1.000 104.42797 ? 222 TRP A CZ2 1 
ATOM   1511 C  CZ3 . TRP A 1 240 ? 3.94735   5.50570  -20.87709 1.000 102.78278 ? 222 TRP A CZ3 1 
ATOM   1512 C  CH2 . TRP A 1 240 ? 3.60162   5.95980  -22.15865 1.000 95.92952  ? 222 TRP A CH2 1 
ATOM   1513 N  N   . GLU A 1 241 ? 10.03897  8.07884  -18.89943 1.000 102.86154 ? 223 GLU A N   1 
ATOM   1514 C  CA  . GLU A 1 241 ? 11.18070  8.85822  -18.43498 1.000 112.42911 ? 223 GLU A CA  1 
ATOM   1515 C  C   . GLU A 1 241 ? 10.72810  9.70964  -17.24853 1.000 105.74712 ? 223 GLU A C   1 
ATOM   1516 O  O   . GLU A 1 241 ? 10.60546  10.93368 -17.32308 1.000 112.40064 ? 223 GLU A O   1 
ATOM   1517 C  CB  . GLU A 1 241 ? 11.74743  9.71366  -19.56461 1.000 94.57428  ? 223 GLU A CB  1 
ATOM   1518 N  N   . GLY A 1 242 ? 10.44717  9.02295  -16.14322 1.000 86.38808  ? 224 GLY A N   1 
ATOM   1519 C  CA  . GLY A 1 242 ? 9.95205   9.68950  -14.95898 1.000 76.04911  ? 224 GLY A CA  1 
ATOM   1520 C  C   . GLY A 1 242 ? 10.30825  9.00922  -13.65629 1.000 67.23482  ? 224 GLY A C   1 
ATOM   1521 O  O   . GLY A 1 242 ? 10.14206  7.79507  -13.49899 1.000 68.31299  ? 224 GLY A O   1 
ATOM   1522 N  N   . LEU A 1 243 ? 10.80834  9.79599  -12.71457 1.000 64.58438  ? 225 LEU A N   1 
ATOM   1523 C  CA  . LEU A 1 243 ? 10.94733  9.37441  -11.32892 1.000 63.70000  ? 225 LEU A CA  1 
ATOM   1524 C  C   . LEU A 1 243 ? 9.84706   10.05485 -10.52633 1.000 57.72918  ? 225 LEU A C   1 
ATOM   1525 O  O   . LEU A 1 243 ? 9.79603   11.28749 -10.45967 1.000 59.89151  ? 225 LEU A O   1 
ATOM   1526 C  CB  . LEU A 1 243 ? 12.32773  9.72718  -10.78186 1.000 61.36250  ? 225 LEU A CB  1 
ATOM   1527 C  CG  . LEU A 1 243 ? 13.49790  9.03839  -11.48766 1.000 69.48412  ? 225 LEU A CG  1 
ATOM   1528 C  CD1 . LEU A 1 243 ? 14.82083  9.37811  -10.81170 1.000 72.38306  ? 225 LEU A CD1 1 
ATOM   1529 C  CD2 . LEU A 1 243 ? 13.28460  7.52887  -11.54820 1.000 59.34191  ? 225 LEU A CD2 1 
ATOM   1530 N  N   . ASN A 1 244 ? 8.97460   9.25266  -9.92237  1.000 53.65135  ? 226 ASN A N   1 
ATOM   1531 C  CA  . ASN A 1 244 ? 7.75690   9.74924  -9.28653  1.000 47.41963  ? 226 ASN A CA  1 
ATOM   1532 C  C   . ASN A 1 244 ? 8.01287   9.94852  -7.79714  1.000 50.72636  ? 226 ASN A C   1 
ATOM   1533 O  O   . ASN A 1 244 ? 7.97800   8.99520  -7.01407  1.000 47.05396  ? 226 ASN A O   1 
ATOM   1534 C  CB  . ASN A 1 244 ? 6.60332   8.78187  -9.52938  1.000 54.90520  ? 226 ASN A CB  1 
ATOM   1535 C  CG  . ASN A 1 244 ? 5.25287   9.40270  -9.23951  1.000 56.54514  ? 226 ASN A CG  1 
ATOM   1536 O  OD1 . ASN A 1 244 ? 5.10876   10.18431 -8.29857  1.000 44.69069  ? 226 ASN A OD1 1 
ATOM   1537 N  ND2 . ASN A 1 244 ? 4.25094   9.05262  -10.04467 1.000 50.98765  ? 226 ASN A ND2 1 
ATOM   1538 N  N   . ALA A 1 245 ? 8.25013   11.20121 -7.39804  1.000 40.59245  ? 227 ALA A N   1 
ATOM   1539 C  CA  . ALA A 1 245 ? 8.44368   11.50655 -5.98490  1.000 50.10191  ? 227 ALA A CA  1 
ATOM   1540 C  C   . ALA A 1 245 ? 7.16631   11.33990 -5.16918  1.000 50.06874  ? 227 ALA A C   1 
ATOM   1541 O  O   . ALA A 1 245 ? 7.24552   11.19449 -3.94340  1.000 43.22791  ? 227 ALA A O   1 
ATOM   1542 C  CB  . ALA A 1 245 ? 8.98310   12.92701 -5.81833  1.000 52.54771  ? 227 ALA A CB  1 
ATOM   1543 N  N   . LEU A 1 246 ? 5.99203   11.36028 -5.80716  1.000 40.96391  ? 228 LEU A N   1 
ATOM   1544 C  CA  . LEU A 1 246 ? 4.77182   11.07831 -5.05828  1.000 44.16043  ? 228 LEU A CA  1 
ATOM   1545 C  C   . LEU A 1 246 ? 4.69343   9.60182  -4.68776  1.000 43.64591  ? 228 LEU A C   1 
ATOM   1546 O  O   . LEU A 1 246 ? 4.28937   9.26065  -3.56847  1.000 46.81183  ? 228 LEU A O   1 
ATOM   1547 C  CB  . LEU A 1 246 ? 3.54018   11.51122 -5.85435  1.000 47.59345  ? 228 LEU A CB  1 
ATOM   1548 C  CG  . LEU A 1 246 ? 2.16489   11.22560 -5.23803  1.000 48.51361  ? 228 LEU A CG  1 
ATOM   1549 C  CD1 . LEU A 1 246 ? 2.07444   11.71832 -3.80231  1.000 37.63199  ? 228 LEU A CD1 1 
ATOM   1550 C  CD2 . LEU A 1 246 ? 1.07475   11.86274 -6.08011  1.000 42.92454  ? 228 LEU A CD2 1 
ATOM   1551 N  N   . ASP A 1 247 ? 5.07981   8.71116  -5.60986  1.000 45.73091  ? 229 ASP A N   1 
ATOM   1552 C  CA  . ASP A 1 247 ? 5.19793   7.29651  -5.26340  1.000 43.06097  ? 229 ASP A CA  1 
ATOM   1553 C  C   . ASP A 1 247 ? 6.08476   7.10809  -4.04350  1.000 40.10977  ? 229 ASP A C   1 
ATOM   1554 O  O   . ASP A 1 247 ? 5.76049   6.32862  -3.13996  1.000 42.41209  ? 229 ASP A O   1 
ATOM   1555 C  CB  . ASP A 1 247 ? 5.76862   6.49660  -6.43443  1.000 43.27074  ? 229 ASP A CB  1 
ATOM   1556 C  CG  . ASP A 1 247 ? 4.79801   6.36873  -7.58423  1.000 54.30399  ? 229 ASP A CG  1 
ATOM   1557 O  OD1 . ASP A 1 247 ? 5.15718   5.70913  -8.58300  1.000 41.83074  ? 229 ASP A OD1 1 
ATOM   1558 O  OD2 . ASP A 1 247 ? 3.68327   6.93383  -7.49315  1.000 45.65906  ? 229 ASP A OD2 1 
ATOM   1559 N  N   . ALA A 1 248 ? 7.21231   7.81884  -4.00246  1.000 36.13113  ? 230 ALA A N   1 
ATOM   1560 C  CA  . ALA A 1 248 ? 8.11856   7.70674  -2.86538  1.000 48.27955  ? 230 ALA A CA  1 
ATOM   1561 C  C   . ALA A 1 248 ? 7.40645   8.02182  -1.55673  1.000 41.94695  ? 230 ALA A C   1 
ATOM   1562 O  O   . ALA A 1 248 ? 7.55875   7.29374  -0.56949  1.000 46.45092  ? 230 ALA A O   1 
ATOM   1563 C  CB  . ALA A 1 248 ? 9.31702   8.63170  -3.06023  1.000 43.76184  ? 230 ALA A CB  1 
ATOM   1564 N  N   . ALA A 1 249 ? 6.61057   9.09308  -1.53259  1.000 36.29319  ? 231 ALA A N   1 
ATOM   1565 C  CA  . ALA A 1 249 ? 5.90128   9.44926  -0.30773  1.000 45.27518  ? 231 ALA A CA  1 
ATOM   1566 C  C   . ALA A 1 249 ? 4.90745   8.36495  0.08888   1.000 45.06201  ? 231 ALA A C   1 
ATOM   1567 O  O   . ALA A 1 249 ? 4.83383   7.97932  1.26200   1.000 42.54814  ? 231 ALA A O   1 
ATOM   1568 C  CB  . ALA A 1 249 ? 5.18984   10.79087 -0.48023  1.000 38.03825  ? 231 ALA A CB  1 
ATOM   1569 N  N   . VAL A 1 250 ? 4.14291   7.85502  -0.88010  1.000 43.63864  ? 232 VAL A N   1 
ATOM   1570 C  CA  . VAL A 1 250 ? 3.12372   6.85127  -0.58676  1.000 41.64131  ? 232 VAL A CA  1 
ATOM   1571 C  C   . VAL A 1 250 ? 3.76369   5.54700  -0.12437  1.000 40.12011  ? 232 VAL A C   1 
ATOM   1572 O  O   . VAL A 1 250 ? 3.27684   4.90058  0.81092   1.000 46.13316  ? 232 VAL A O   1 
ATOM   1573 C  CB  . VAL A 1 250 ? 2.22303   6.63857  -1.81798  1.000 43.24119  ? 232 VAL A CB  1 
ATOM   1574 C  CG1 . VAL A 1 250 ? 1.30945   5.43217  -1.61515  1.000 42.62606  ? 232 VAL A CG1 1 
ATOM   1575 C  CG2 . VAL A 1 250 ? 1.40655   7.89380  -2.09800  1.000 43.29530  ? 232 VAL A CG2 1 
ATOM   1576 N  N   . LEU A 1 251 ? 4.86119   5.13686  -0.76627  1.000 41.17068  ? 233 LEU A N   1 
ATOM   1577 C  CA  . LEU A 1 251 ? 5.52699   3.89931  -0.36854  1.000 42.29193  ? 233 LEU A CA  1 
ATOM   1578 C  C   . LEU A 1 251 ? 6.12546   4.02065  1.02955   1.000 41.69198  ? 233 LEU A C   1 
ATOM   1579 O  O   . LEU A 1 251 ? 6.10753   3.06057  1.80974   1.000 35.78863  ? 233 LEU A O   1 
ATOM   1580 C  CB  . LEU A 1 251 ? 6.60672   3.53775  -1.38650  1.000 37.97413  ? 233 LEU A CB  1 
ATOM   1581 C  CG  . LEU A 1 251 ? 6.12008   3.17711  -2.79218  1.000 46.96624  ? 233 LEU A CG  1 
ATOM   1582 C  CD1 . LEU A 1 251 ? 7.30762   2.92761  -3.71836  1.000 43.17657  ? 233 LEU A CD1 1 
ATOM   1583 C  CD2 . LEU A 1 251 ? 5.18713   1.96650  -2.76132  1.000 35.75823  ? 233 LEU A CD2 1 
ATOM   1584 N  N   . ALA A 1 252 ? 6.66524   5.19335  1.36271   1.000 37.44616  ? 234 ALA A N   1 
ATOM   1585 C  CA  . ALA A 1 252 ? 7.14709   5.42022  2.72196   1.000 49.28253  ? 234 ALA A CA  1 
ATOM   1586 C  C   . ALA A 1 252 ? 6.01157   5.28141  3.72844   1.000 37.83356  ? 234 ALA A C   1 
ATOM   1587 O  O   . ALA A 1 252 ? 6.16825   4.64641  4.77829   1.000 40.81046  ? 234 ALA A O   1 
ATOM   1588 C  CB  . ALA A 1 252 ? 7.79830   6.80165  2.82273   1.000 35.51952  ? 234 ALA A CB  1 
ATOM   1589 N  N   . TYR A 1 253 ? 4.85248   5.85145  3.40830   1.000 39.81946  ? 235 TYR A N   1 
ATOM   1590 C  CA  . TYR A 1 253 ? 3.67710   5.70430  4.25754   1.000 40.77790  ? 235 TYR A CA  1 
ATOM   1591 C  C   . TYR A 1 253 ? 3.30452   4.23436  4.42592   1.000 46.74618  ? 235 TYR A C   1 
ATOM   1592 O  O   . TYR A 1 253 ? 3.02600   3.77628  5.54189   1.000 46.75780  ? 235 TYR A O   1 
ATOM   1593 C  CB  . TYR A 1 253 ? 2.52830   6.50268  3.64607   1.000 41.40402  ? 235 TYR A CB  1 
ATOM   1594 C  CG  . TYR A 1 253 ? 1.44452   6.94631  4.59832   1.000 46.76086  ? 235 TYR A CG  1 
ATOM   1595 C  CD1 . TYR A 1 253 ? 0.34381   6.13408  4.85626   1.000 40.99414  ? 235 TYR A CD1 1 
ATOM   1596 C  CD2 . TYR A 1 253 ? 1.49089   8.19826  5.19662   1.000 44.71749  ? 235 TYR A CD2 1 
ATOM   1597 C  CE1 . TYR A 1 253 ? -0.66618  6.54468  5.70204   1.000 42.66087  ? 235 TYR A CE1 1 
ATOM   1598 C  CE2 . TYR A 1 253 ? 0.47968   8.62159  6.05132   1.000 48.61946  ? 235 TYR A CE2 1 
ATOM   1599 C  CZ  . TYR A 1 253 ? -0.59382  7.78864  6.29902   1.000 46.71852  ? 235 TYR A CZ  1 
ATOM   1600 O  OH  . TYR A 1 253 ? -1.59973  8.19425  7.14392   1.000 48.49121  ? 235 TYR A OH  1 
ATOM   1601 N  N   . ASN A 1 254 ? 3.29765   3.47507  3.32155   1.000 42.96699  ? 236 ASN A N   1 
ATOM   1602 C  CA  . ASN A 1 254 ? 3.00374   2.04491  3.40557   1.000 37.87337  ? 236 ASN A CA  1 
ATOM   1603 C  C   . ASN A 1 254 ? 4.05303   1.31446  4.23758   1.000 43.74232  ? 236 ASN A C   1 
ATOM   1604 O  O   . ASN A 1 254 ? 3.71894   0.43308  5.04053   1.000 40.94218  ? 236 ASN A O   1 
ATOM   1605 C  CB  . ASN A 1 254 ? 2.92386   1.43882  2.00335   1.000 39.81146  ? 236 ASN A CB  1 
ATOM   1606 C  CG  . ASN A 1 254 ? 1.68361   1.87832  1.23896   1.000 47.13722  ? 236 ASN A CG  1 
ATOM   1607 O  OD1 . ASN A 1 254 ? 0.60764   2.02054  1.81220   1.000 40.47141  ? 236 ASN A OD1 1 
ATOM   1608 N  ND2 . ASN A 1 254 ? 1.83264   2.08808  -0.06830  1.000 40.41294  ? 236 ASN A ND2 1 
ATOM   1609 N  N   . ASN A 1 255 ? 5.32859   1.67510  4.06282   1.000 35.94244  ? 237 ASN A N   1 
ATOM   1610 C  CA  . ASN A 1 255 ? 6.40636   1.01667  4.79850   1.000 47.56912  ? 237 ASN A CA  1 
ATOM   1611 C  C   . ASN A 1 255 ? 6.23976   1.19305  6.30271   1.000 43.23266  ? 237 ASN A C   1 
ATOM   1612 O  O   . ASN A 1 255 ? 6.39119   0.23821  7.07433   1.000 41.36196  ? 237 ASN A O   1 
ATOM   1613 C  CB  . ASN A 1 255 ? 7.76243   1.56793  4.35139   1.000 43.43803  ? 237 ASN A CB  1 
ATOM   1614 C  CG  . ASN A 1 255 ? 8.09360   1.22057  2.91217   1.000 44.48128  ? 237 ASN A CG  1 
ATOM   1615 O  OD1 . ASN A 1 255 ? 7.48681   0.32825  2.31122   1.000 41.10101  ? 237 ASN A OD1 1 
ATOM   1616 N  ND2 . ASN A 1 255 ? 9.06240   1.92954  2.34996   1.000 39.67514  ? 237 ASN A ND2 1 
ATOM   1617 N  N   . LEU A 1 256 ? 5.93761   2.41521  6.74151   1.000 44.00003  ? 238 LEU A N   1 
ATOM   1618 C  CA  . LEU A 1 256 ? 5.77341   2.65098  8.17088   1.000 43.62239  ? 238 LEU A CA  1 
ATOM   1619 C  C   . LEU A 1 256 ? 4.49266   2.01297  8.69122   1.000 44.56536  ? 238 LEU A C   1 
ATOM   1620 O  O   . LEU A 1 256 ? 4.45724   1.51306  9.82297   1.000 47.32083  ? 238 LEU A O   1 
ATOM   1621 C  CB  . LEU A 1 256 ? 5.77961   4.14910  8.45665   1.000 45.75612  ? 238 LEU A CB  1 
ATOM   1622 C  CG  . LEU A 1 256 ? 7.05895   4.90644  8.10563   1.000 46.98591  ? 238 LEU A CG  1 
ATOM   1623 C  CD1 . LEU A 1 256 ? 6.75574   6.38335  7.90031   1.000 50.32719  ? 238 LEU A CD1 1 
ATOM   1624 C  CD2 . LEU A 1 256 ? 8.09874   4.72239  9.19743   1.000 40.86629  ? 238 LEU A CD2 1 
ATOM   1625 N  N   . SER A 1 257 ? 3.43459   2.01217  7.87497   1.000 41.38364  ? 239 SER A N   1 
ATOM   1626 C  CA  . SER A 1 257 ? 2.14002   1.51444  8.33032   1.000 36.56384  ? 239 SER A CA  1 
ATOM   1627 C  C   . SER A 1 257 ? 2.21360   0.04016  8.71416   1.000 47.56497  ? 239 SER A C   1 
ATOM   1628 O  O   . SER A 1 257 ? 1.70345   -0.36468 9.76696   1.000 41.80886  ? 239 SER A O   1 
ATOM   1629 C  CB  . SER A 1 257 ? 1.08228   1.73905  7.24859   1.000 44.79972  ? 239 SER A CB  1 
ATOM   1630 O  OG  . SER A 1 257 ? 0.92877   3.12124  6.97240   1.000 47.06097  ? 239 SER A OG  1 
ATOM   1631 N  N   . VAL A 1 258 ? 2.84339   -0.78350 7.87169   1.000 42.91348  ? 240 VAL A N   1 
ATOM   1632 C  CA  . VAL A 1 258 ? 2.92861   -2.20108 8.20366   1.000 48.66876  ? 240 VAL A CA  1 
ATOM   1633 C  C   . VAL A 1 258 ? 3.89972   -2.41041 9.35479   1.000 42.07763  ? 240 VAL A C   1 
ATOM   1634 O  O   . VAL A 1 258 ? 3.77751   -3.38120 10.11362  1.000 39.25694  ? 240 VAL A O   1 
ATOM   1635 C  CB  . VAL A 1 258 ? 3.31388   -3.03786 6.96443   1.000 47.89588  ? 240 VAL A CB  1 
ATOM   1636 C  CG1 . VAL A 1 258 ? 2.36760   -2.72992 5.81334   1.000 40.87274  ? 240 VAL A CG1 1 
ATOM   1637 C  CG2 . VAL A 1 258 ? 4.76928   -2.80425 6.56225   1.000 36.01104  ? 240 VAL A CG2 1 
ATOM   1638 N  N   . PHE A 1 259 ? 4.86333   -1.50335 9.51828   1.000 42.50865  ? 241 PHE A N   1 
ATOM   1639 C  CA  . PHE A 1 259 ? 5.78763   -1.59468 10.64152  1.000 46.17646  ? 241 PHE A CA  1 
ATOM   1640 C  C   . PHE A 1 259 ? 5.07667   -1.42420 11.97883  1.000 49.75014  ? 241 PHE A C   1 
ATOM   1641 O  O   . PHE A 1 259 ? 5.57350   -1.91551 13.00049  1.000 40.77420  ? 241 PHE A O   1 
ATOM   1642 C  CB  . PHE A 1 259 ? 6.90241   -0.55327 10.48453  1.000 43.09882  ? 241 PHE A CB  1 
ATOM   1643 C  CG  . PHE A 1 259 ? 7.78785   -0.41902 11.69536  1.000 51.70306  ? 241 PHE A CG  1 
ATOM   1644 C  CD1 . PHE A 1 259 ? 8.46831   -1.51605 12.20379  1.000 45.54440  ? 241 PHE A CD1 1 
ATOM   1645 C  CD2 . PHE A 1 259 ? 7.93564   0.80507  12.32652  1.000 48.71009  ? 241 PHE A CD2 1 
ATOM   1646 C  CE1 . PHE A 1 259 ? 9.27568   -1.39345 13.31999  1.000 53.58150  ? 241 PHE A CE1 1 
ATOM   1647 C  CE2 . PHE A 1 259 ? 8.73921   0.93516  13.44278  1.000 52.91827  ? 241 PHE A CE2 1 
ATOM   1648 C  CZ  . PHE A 1 259 ? 9.41254   -0.16359 13.94107  1.000 54.90005  ? 241 PHE A CZ  1 
ATOM   1649 N  N   . ARG A 1 260 ? 3.91035   -0.76889 11.99345  1.000 47.61771  ? 242 ARG A N   1 
ATOM   1650 C  CA  . ARG A 1 260 ? 3.21788   -0.53175 13.25848  1.000 45.20375  ? 242 ARG A CA  1 
ATOM   1651 C  C   . ARG A 1 260 ? 2.93737   -1.83499 13.99996  1.000 43.80572  ? 242 ARG A C   1 
ATOM   1652 O  O   . ARG A 1 260 ? 2.97970   -1.86344 15.23357  1.000 43.29305  ? 242 ARG A O   1 
ATOM   1653 C  CB  . ARG A 1 260 ? 1.92171   0.24613  13.01660  1.000 34.09861  ? 242 ARG A CB  1 
ATOM   1654 C  CG  . ARG A 1 260 ? 2.14194   1.69855  12.57774  1.000 40.20906  ? 242 ARG A CG  1 
ATOM   1655 C  CD  . ARG A 1 260 ? 0.82251   2.38328  12.20039  1.000 39.80037  ? 242 ARG A CD  1 
ATOM   1656 N  NE  . ARG A 1 260 ? 1.03678   3.73088  11.68257  1.000 47.51610  ? 242 ARG A NE  1 
ATOM   1657 C  CZ  . ARG A 1 260 ? 1.34575   4.78382  12.43010  1.000 49.55254  ? 242 ARG A CZ  1 
ATOM   1658 N  NH1 . ARG A 1 260 ? 1.46107   4.68900  13.74586  1.000 40.39683  ? 242 ARG A NH1 1 
ATOM   1659 N  NH2 . ARG A 1 260 ? 1.54507   5.96211  11.84298  1.000 36.88129  ? 242 ARG A NH2 1 
ATOM   1660 N  N   . GLN A 1 261 ? 2.69208   -2.92852 13.27073  1.000 44.77524  ? 243 GLN A N   1 
ATOM   1661 C  CA  . GLN A 1 261 ? 2.42549   -4.20785 13.92208  1.000 43.99499  ? 243 GLN A CA  1 
ATOM   1662 C  C   . GLN A 1 261 ? 3.59905   -4.66518 14.78196  1.000 50.30474  ? 243 GLN A C   1 
ATOM   1663 O  O   . GLN A 1 261 ? 3.39583   -5.35699 15.78538  1.000 46.78461  ? 243 GLN A O   1 
ATOM   1664 C  CB  . GLN A 1 261 ? 2.08446   -5.27379 12.87784  1.000 42.95029  ? 243 GLN A CB  1 
ATOM   1665 C  CG  . GLN A 1 261 ? 1.66030   -6.61668 13.47586  1.000 44.55350  ? 243 GLN A CG  1 
ATOM   1666 C  CD  . GLN A 1 261 ? 1.31819   -7.65333 12.41842  1.000 44.42593  ? 243 GLN A CD  1 
ATOM   1667 O  OE1 . GLN A 1 261 ? 1.61548   -7.47969 11.23285  1.000 43.33419  ? 243 GLN A OE1 1 
ATOM   1668 N  NE2 . GLN A 1 261 ? 0.69042   -8.73893 12.84318  1.000 44.43616  ? 243 GLN A NE2 1 
ATOM   1669 N  N   . GLN A 1 262 ? 4.82403   -4.27724 14.42785  1.000 43.71247  ? 244 GLN A N   1 
ATOM   1670 C  CA  . GLN A 1 262 ? 6.00508   -4.67647 15.18253  1.000 51.29940  ? 244 GLN A CA  1 
ATOM   1671 C  C   . GLN A 1 262 ? 6.53515   -3.58197 16.10074  1.000 53.48887  ? 244 GLN A C   1 
ATOM   1672 O  O   . GLN A 1 262 ? 7.56716   -3.78415 16.74886  1.000 51.27160  ? 244 GLN A O   1 
ATOM   1673 C  CB  . GLN A 1 262 ? 7.11328   -5.12799 14.22816  1.000 50.09660  ? 244 GLN A CB  1 
ATOM   1674 C  CG  . GLN A 1 262 ? 6.87516   -6.50257 13.62160  1.000 47.72408  ? 244 GLN A CG  1 
ATOM   1675 C  CD  . GLN A 1 262 ? 5.89355   -6.44832 12.47725  1.000 47.22407  ? 244 GLN A CD  1 
ATOM   1676 O  OE1 . GLN A 1 262 ? 6.02027   -5.61747 11.57344  1.000 41.82957  ? 244 GLN A OE1 1 
ATOM   1677 N  NE2 . GLN A 1 262 ? 4.89699   -7.32216 12.51321  1.000 44.35326  ? 244 GLN A NE2 1 
ATOM   1678 N  N   . MET A 1 263 ? 5.86571   -2.43543 16.16842  1.000 41.30726  ? 245 MET A N   1 
ATOM   1679 C  CA  . MET A 1 263 ? 6.26898   -1.38140 17.08894  1.000 50.00943  ? 245 MET A CA  1 
ATOM   1680 C  C   . MET A 1 263 ? 5.97232   -1.80782 18.51903  1.000 55.04060  ? 245 MET A C   1 
ATOM   1681 O  O   . MET A 1 263 ? 4.98885   -2.50734 18.78020  1.000 53.15489  ? 245 MET A O   1 
ATOM   1682 C  CB  . MET A 1 263 ? 5.51634   -0.08767 16.77462  1.000 47.32026  ? 245 MET A CB  1 
ATOM   1683 C  CG  . MET A 1 263 ? 5.79546   0.49853  15.39875  1.000 54.05102  ? 245 MET A CG  1 
ATOM   1684 S  SD  . MET A 1 263 ? 5.45766   2.26810  15.26996  1.000 58.39139  ? 245 MET A SD  1 
ATOM   1685 C  CE  . MET A 1 263 ? 4.39638   2.55046  16.68313  1.000 54.72030  ? 245 MET A CE  1 
ATOM   1686 N  N   . LYS A 1 264 ? 6.82512   -1.38772 19.44702  1.000 58.02559  ? 246 LYS A N   1 
ATOM   1687 C  CA  . LYS A 1 264 ? 6.52429   -1.59747 20.85397  1.000 58.14442  ? 246 LYS A CA  1 
ATOM   1688 C  C   . LYS A 1 264 ? 5.24799   -0.83977 21.20931  1.000 50.46298  ? 246 LYS A C   1 
ATOM   1689 O  O   . LYS A 1 264 ? 5.02908   0.27218  20.71190  1.000 56.13269  ? 246 LYS A O   1 
ATOM   1690 C  CB  . LYS A 1 264 ? 7.68508   -1.13057 21.73107  1.000 59.11820  ? 246 LYS A CB  1 
ATOM   1691 C  CG  . LYS A 1 264 ? 8.74303   -2.19452 21.96912  1.000 70.58068  ? 246 LYS A CG  1 
ATOM   1692 C  CD  . LYS A 1 264 ? 9.43662   -1.99037 23.30592  1.000 67.84610  ? 246 LYS A CD  1 
ATOM   1693 C  CE  . LYS A 1 264 ? 10.55341  -2.99659 23.50252  1.000 74.92430  ? 246 LYS A CE  1 
ATOM   1694 N  NZ  . LYS A 1 264 ? 11.88685  -2.39473 23.22788  1.000 80.33909  ? 246 LYS A NZ  1 
ATOM   1695 N  N   . PRO A 1 265 ? 4.38215   -1.40911 22.04970  1.000 57.71743  ? 247 PRO A N   1 
ATOM   1696 C  CA  . PRO A 1 265 ? 3.07068   -0.78251 22.28826  1.000 51.59143  ? 247 PRO A CA  1 
ATOM   1697 C  C   . PRO A 1 265 ? 3.15068   0.61291  22.88305  1.000 54.46963  ? 247 PRO A C   1 
ATOM   1698 O  O   . PRO A 1 265 ? 2.17166   1.36335  22.78987  1.000 61.15279  ? 247 PRO A O   1 
ATOM   1699 C  CB  . PRO A 1 265 ? 2.38009   -1.76769 23.24135  1.000 56.68581  ? 247 PRO A CB  1 
ATOM   1700 C  CG  . PRO A 1 265 ? 3.49188   -2.49149 23.91080  1.000 60.45156  ? 247 PRO A CG  1 
ATOM   1701 C  CD  . PRO A 1 265 ? 4.60734   -2.58254 22.90963  1.000 63.91677  ? 247 PRO A CD  1 
ATOM   1702 N  N   . THR A 1 266 ? 4.28122   0.99627  23.46833  1.000 51.88316  ? 248 THR A N   1 
ATOM   1703 C  CA  . THR A 1 266 ? 4.44786   2.33648  24.01068  1.000 55.21162  ? 248 THR A CA  1 
ATOM   1704 C  C   . THR A 1 266 ? 4.96076   3.33544  22.98404  1.000 60.24568  ? 248 THR A C   1 
ATOM   1705 O  O   . THR A 1 266 ? 5.07640   4.52154  23.30678  1.000 63.41119  ? 248 THR A O   1 
ATOM   1706 C  CB  . THR A 1 266 ? 5.40421   2.31009  25.20386  1.000 57.97527  ? 248 THR A CB  1 
ATOM   1707 O  OG1 . THR A 1 266 ? 6.68632   1.83479  24.77326  1.000 59.21596  ? 248 THR A OG1 1 
ATOM   1708 C  CG2 . THR A 1 266 ? 4.86323   1.40082  26.30651  1.000 46.85200  ? 248 THR A CG2 1 
ATOM   1709 N  N   . TRP A 1 267 ? 5.27249   2.89707  21.76683  1.000 49.14824  ? 249 TRP A N   1 
ATOM   1710 C  CA  . TRP A 1 267 ? 5.83586   3.78840  20.76277  1.000 51.26917  ? 249 TRP A CA  1 
ATOM   1711 C  C   . TRP A 1 267 ? 4.72874   4.47984  19.97495  1.000 46.88223  ? 249 TRP A C   1 
ATOM   1712 O  O   . TRP A 1 267 ? 3.61074   3.97119  19.85641  1.000 51.28203  ? 249 TRP A O   1 
ATOM   1713 C  CB  . TRP A 1 267 ? 6.75393   3.02197  19.81267  1.000 56.58097  ? 249 TRP A CB  1 
ATOM   1714 C  CG  . TRP A 1 267 ? 7.96250   2.44308  20.47881  1.000 58.66780  ? 249 TRP A CG  1 
ATOM   1715 C  CD1 . TRP A 1 267 ? 8.29314   2.52807  21.80050  1.000 57.01858  ? 249 TRP A CD1 1 
ATOM   1716 C  CD2 . TRP A 1 267 ? 9.00051   1.67931  19.85340  1.000 60.46129  ? 249 TRP A CD2 1 
ATOM   1717 N  NE1 . TRP A 1 267 ? 9.47494   1.86949  22.03587  1.000 59.75060  ? 249 TRP A NE1 1 
ATOM   1718 C  CE2 . TRP A 1 267 ? 9.93033   1.33852  20.85738  1.000 63.33521  ? 249 TRP A CE2 1 
ATOM   1719 C  CE3 . TRP A 1 267 ? 9.23425   1.25086  18.54145  1.000 52.87302  ? 249 TRP A CE3 1 
ATOM   1720 C  CZ2 . TRP A 1 267 ? 11.07615  0.58766  20.59178  1.000 57.80389  ? 249 TRP A CZ2 1 
ATOM   1721 C  CZ3 . TRP A 1 267 ? 10.37278  0.50921  18.27820  1.000 59.77107  ? 249 TRP A CZ3 1 
ATOM   1722 C  CH2 . TRP A 1 267 ? 11.28038  0.18542  19.29893  1.000 65.37107  ? 249 TRP A CH2 1 
ATOM   1723 N  N   . ARG A 1 268 ? 5.05211   5.65249  19.43321  1.000 44.51428  ? 250 ARG A N   1 
ATOM   1724 C  CA  . ARG A 1 268 ? 4.08149   6.45818  18.70612  1.000 53.42461  ? 250 ARG A CA  1 
ATOM   1725 C  C   . ARG A 1 268 ? 4.73492   7.03877  17.46358  1.000 51.68621  ? 250 ARG A C   1 
ATOM   1726 O  O   . ARG A 1 268 ? 5.87704   7.50673  17.51352  1.000 48.99675  ? 250 ARG A O   1 
ATOM   1727 C  CB  . ARG A 1 268 ? 3.51452   7.59175  19.57834  1.000 51.41716  ? 250 ARG A CB  1 
ATOM   1728 C  CG  . ARG A 1 268 ? 2.69136   7.11763  20.76948  1.000 45.39640  ? 250 ARG A CG  1 
ATOM   1729 C  CD  . ARG A 1 268 ? 1.53035   6.24060  20.32402  1.000 42.37455  ? 250 ARG A CD  1 
ATOM   1730 N  NE  . ARG A 1 268 ? 0.69622   5.82328  21.44682  1.000 55.60959  ? 250 ARG A NE  1 
ATOM   1731 C  CZ  . ARG A 1 268 ? 0.95117   4.78771  22.23673  1.000 54.95597  ? 250 ARG A CZ  1 
ATOM   1732 N  NH1 . ARG A 1 268 ? 2.03412   4.04363  22.07770  1.000 56.43491  ? 250 ARG A NH1 1 
ATOM   1733 N  NH2 . ARG A 1 268 ? 0.09729   4.49077  23.21211  1.000 59.09447  ? 250 ARG A NH2 1 
ATOM   1734 N  N   . VAL A 1 269 ? 4.00371   7.00195  16.34944  1.000 49.13720  ? 251 VAL A N   1 
ATOM   1735 C  CA  . VAL A 1 269 ? 4.48463   7.51173  15.07010  1.000 45.83577  ? 251 VAL A CA  1 
ATOM   1736 C  C   . VAL A 1 269 ? 3.32634   8.22813  14.38998  1.000 49.15084  ? 251 VAL A C   1 
ATOM   1737 O  O   . VAL A 1 269 ? 2.26393   7.63134  14.17480  1.000 50.53192  ? 251 VAL A O   1 
ATOM   1738 C  CB  . VAL A 1 269 ? 5.03541   6.39240  14.16604  1.000 50.18270  ? 251 VAL A CB  1 
ATOM   1739 C  CG1 . VAL A 1 269 ? 5.31433   6.92363  12.76857  1.000 35.25354  ? 251 VAL A CG1 1 
ATOM   1740 C  CG2 . VAL A 1 269 ? 6.30183   5.79069  14.76831  1.000 48.24092  ? 251 VAL A CG2 1 
ATOM   1741 N  N   . HIS A 1 270 ? 3.52310   9.50401  14.06161  1.000 45.87723  ? 252 HIS A N   1 
ATOM   1742 C  CA  . HIS A 1 270 ? 2.49733   10.32182 13.42827  1.000 47.05900  ? 252 HIS A CA  1 
ATOM   1743 C  C   . HIS A 1 270 ? 3.14763   11.19774 12.37014  1.000 51.54185  ? 252 HIS A C   1 
ATOM   1744 O  O   . HIS A 1 270 ? 4.25583   11.70361 12.57471  1.000 47.20838  ? 252 HIS A O   1 
ATOM   1745 C  CB  . HIS A 1 270 ? 1.75881   11.20010 14.45027  1.000 40.23602  ? 252 HIS A CB  1 
ATOM   1746 C  CG  . HIS A 1 270 ? 1.12630   10.43051 15.56673  1.000 49.13391  ? 252 HIS A CG  1 
ATOM   1747 N  ND1 . HIS A 1 270 ? 1.53056   10.55294 16.88021  1.000 52.70226  ? 252 HIS A ND1 1 
ATOM   1748 C  CD2 . HIS A 1 270 ? 0.11221   9.53353  15.56759  1.000 39.50764  ? 252 HIS A CD2 1 
ATOM   1749 C  CE1 . HIS A 1 270 ? 0.79502   9.76081  17.64022  1.000 56.72923  ? 252 HIS A CE1 1 
ATOM   1750 N  NE2 . HIS A 1 270 ? -0.07272  9.13019  16.86827  1.000 49.40341  ? 252 HIS A NE2 1 
ATOM   1751 N  N   . GLY A 1 271 ? 2.46118   11.37837 11.24447  1.000 48.17654  ? 253 GLY A N   1 
ATOM   1752 C  CA  . GLY A 1 271 ? 3.03798   12.14403 10.15720  1.000 53.46341  ? 253 GLY A CA  1 
ATOM   1753 C  C   . GLY A 1 271 ? 2.03295   12.46474 9.07560   1.000 47.89878  ? 253 GLY A C   1 
ATOM   1754 O  O   . GLY A 1 271 ? 0.96354   11.85089 8.98127   1.000 43.41900  ? 253 GLY A O   1 
ATOM   1755 N  N   . ILE A 1 272 ? 2.40710   13.43905 8.24525   1.000 37.58152  ? 254 ILE A N   1 
ATOM   1756 C  CA  . ILE A 1 272 ? 1.56484   13.95437 7.17688   1.000 51.49822  ? 254 ILE A CA  1 
ATOM   1757 C  C   . ILE A 1 272 ? 2.37722   14.03371 5.89153   1.000 48.11306  ? 254 ILE A C   1 
ATOM   1758 O  O   . ILE A 1 272 ? 3.61083   14.06104 5.90480   1.000 48.34125  ? 254 ILE A O   1 
ATOM   1759 C  CB  . ILE A 1 272 ? 0.98966   15.34372 7.51506   1.000 50.76829  ? 254 ILE A CB  1 
ATOM   1760 C  CG1 . ILE A 1 272 ? 2.13430   16.33929 7.71542   1.000 50.21455  ? 254 ILE A CG1 1 
ATOM   1761 C  CG2 . ILE A 1 272 ? 0.11730   15.27287 8.75183   1.000 52.23364  ? 254 ILE A CG2 1 
ATOM   1762 C  CD1 . ILE A 1 272 ? 1.75237   17.77058 7.46900   1.000 54.65082  ? 254 ILE A CD1 1 
ATOM   1763 N  N   . ILE A 1 273 ? 1.66483   14.07807 4.77011   1.000 41.13292  ? 255 ILE A N   1 
ATOM   1764 C  CA  . ILE A 1 273 ? 2.26225   14.36711 3.47069   1.000 40.16100  ? 255 ILE A CA  1 
ATOM   1765 C  C   . ILE A 1 273 ? 2.02168   15.84915 3.20742   1.000 49.01032  ? 255 ILE A C   1 
ATOM   1766 O  O   . ILE A 1 273 ? 0.93938   16.25170 2.77244   1.000 49.97375  ? 255 ILE A O   1 
ATOM   1767 C  CB  . ILE A 1 273 ? 1.68462   13.48635 2.36180   1.000 43.44254  ? 255 ILE A CB  1 
ATOM   1768 C  CG1 . ILE A 1 273 ? 1.99030   12.01576 2.64292   1.000 44.84419  ? 255 ILE A CG1 1 
ATOM   1769 C  CG2 . ILE A 1 273 ? 2.25764   13.89468 1.00331   1.000 39.41662  ? 255 ILE A CG2 1 
ATOM   1770 C  CD1 . ILE A 1 273 ? 1.30060   11.05822 1.68129   1.000 38.61328  ? 255 ILE A CD1 1 
ATOM   1771 N  N   . LYS A 1 274 ? 3.03176   16.67011 3.49675   1.000 53.62480  ? 256 LYS A N   1 
ATOM   1772 C  CA  . LYS A 1 274 ? 2.89104   18.11298 3.33413   1.000 47.16875  ? 256 LYS A CA  1 
ATOM   1773 C  C   . LYS A 1 274 ? 2.73780   18.48960 1.86361   1.000 54.89992  ? 256 LYS A C   1 
ATOM   1774 O  O   . LYS A 1 274 ? 1.84424   19.26371 1.49829   1.000 55.40659  ? 256 LYS A O   1 
ATOM   1775 C  CB  . LYS A 1 274 ? 4.09763   18.81925 3.95804   1.000 58.26657  ? 256 LYS A CB  1 
ATOM   1776 C  CG  . LYS A 1 274 ? 4.00138   20.33603 3.98635   1.000 57.51709  ? 256 LYS A CG  1 
ATOM   1777 C  CD  . LYS A 1 274 ? 2.77907   20.80327 4.76265   1.000 69.95933  ? 256 LYS A CD  1 
ATOM   1778 C  CE  . LYS A 1 274 ? 2.78724   22.31426 4.92897   1.000 71.90753  ? 256 LYS A CE  1 
ATOM   1779 N  NZ  . LYS A 1 274 ? 4.17269   22.85741 4.86768   1.000 77.00532  ? 256 LYS A NZ  1 
ATOM   1780 N  N   . ASN A 1 275 ? 3.59721   17.94538 1.00381   1.000 54.04980  ? 257 ASN A N   1 
ATOM   1781 C  CA  . ASN A 1 275 ? 3.60071   18.25407 -0.42463  1.000 52.26628  ? 257 ASN A CA  1 
ATOM   1782 C  C   . ASN A 1 275 ? 3.50345   16.94543 -1.19442  1.000 51.01494  ? 257 ASN A C   1 
ATOM   1783 O  O   . ASN A 1 275 ? 4.43507   16.13497 -1.16010  1.000 49.46321  ? 257 ASN A O   1 
ATOM   1784 C  CB  . ASN A 1 275 ? 4.86375   19.02185 -0.81680  1.000 41.50348  ? 257 ASN A CB  1 
ATOM   1785 C  CG  . ASN A 1 275 ? 4.71211   19.77671 -2.12387  1.000 59.82274  ? 257 ASN A CG  1 
ATOM   1786 O  OD1 . ASN A 1 275 ? 4.24190   19.23215 -3.12710  1.000 58.14802  ? 257 ASN A OD1 1 
ATOM   1787 N  ND2 . ASN A 1 275 ? 5.12111   21.03806 -2.12099  1.000 58.82223  ? 257 ASN A ND2 1 
ATOM   1788 N  N   . GLY A 1 276 ? 2.38376   16.74031 -1.88598  1.000 52.39106  ? 258 GLY A N   1 
ATOM   1789 C  CA  . GLY A 1 276 ? 2.18354   15.53000 -2.65872  1.000 42.62675  ? 258 GLY A CA  1 
ATOM   1790 C  C   . GLY A 1 276 ? 1.90230   15.78607 -4.12745  1.000 52.72395  ? 258 GLY A C   1 
ATOM   1791 O  O   . GLY A 1 276 ? 1.20980   14.99916 -4.77932  1.000 47.64991  ? 258 GLY A O   1 
ATOM   1792 N  N   . GLY A 1 277 ? 2.43877   16.87199 -4.66451  1.000 51.77410  ? 259 GLY A N   1 
ATOM   1793 C  CA  . GLY A 1 277 ? 2.22562   17.24002 -6.04929  1.000 54.24678  ? 259 GLY A CA  1 
ATOM   1794 C  C   . GLY A 1 277 ? 1.54337   18.59007 -6.17929  1.000 57.18098  ? 259 GLY A C   1 
ATOM   1795 O  O   . GLY A 1 277 ? 1.03358   19.16485 -5.21913  1.000 63.22376  ? 259 GLY A O   1 
ATOM   1796 N  N   . VAL A 1 278 ? 1.54940   19.08997 -7.41252  1.000 63.19688  ? 260 VAL A N   1 
ATOM   1797 C  CA  . VAL A 1 278 ? 0.98885   20.40791 -7.68831  1.000 75.11103  ? 260 VAL A CA  1 
ATOM   1798 C  C   . VAL A 1 278 ? -0.04682  20.31482 -8.80158  1.000 74.26568  ? 260 VAL A C   1 
ATOM   1799 O  O   . VAL A 1 278 ? -1.15821  20.83997 -8.67147  1.000 84.19743  ? 260 VAL A O   1 
ATOM   1800 C  CB  . VAL A 1 278 ? 2.09665   21.42095 -8.03668  1.000 82.57998  ? 260 VAL A CB  1 
ATOM   1801 C  CG1 . VAL A 1 278 ? 2.73032   21.96878 -6.76203  1.000 68.23367  ? 260 VAL A CG1 1 
ATOM   1802 C  CG2 . VAL A 1 278 ? 3.15592   20.77706 -8.91794  1.000 83.29892  ? 260 VAL A CG2 1 
ATOM   1803 N  N   . LYS A 1 279 ? 0.29977   19.63722 -9.89684  1.000 68.45829  ? 261 LYS A N   1 
ATOM   1804 C  CA  . LYS A 1 279 ? -0.59183  19.49714 -11.03974 1.000 64.02922  ? 261 LYS A CA  1 
ATOM   1805 C  C   . LYS A 1 279 ? -0.55567  18.05695 -11.53289 1.000 62.13742  ? 261 LYS A C   1 
ATOM   1806 O  O   . LYS A 1 279 ? 0.52627   17.45663 -11.62128 1.000 63.55851  ? 261 LYS A O   1 
ATOM   1807 C  CB  . LYS A 1 279 ? -0.20569  20.44936 -12.18096 1.000 69.86305  ? 261 LYS A CB  1 
ATOM   1808 N  N   . PRO A 1 280 ? -1.71434  17.48162 -11.86533 1.000 66.11782  ? 262 PRO A N   1 
ATOM   1809 C  CA  . PRO A 1 280 ? -1.74594  16.06261 -12.25900 1.000 67.06118  ? 262 PRO A CA  1 
ATOM   1810 C  C   . PRO A 1 280 ? -1.07626  15.76866 -13.59098 1.000 72.09480  ? 262 PRO A C   1 
ATOM   1811 O  O   . PRO A 1 280 ? -0.67592  14.61960 -13.81508 1.000 79.94005  ? 262 PRO A O   1 
ATOM   1812 C  CB  . PRO A 1 280 ? -3.24758  15.74141 -12.32047 1.000 69.88115  ? 262 PRO A CB  1 
ATOM   1813 C  CG  . PRO A 1 280 ? -3.93977  16.89784 -11.66998 1.000 71.93106  ? 262 PRO A CG  1 
ATOM   1814 C  CD  . PRO A 1 280 ? -3.05536  18.08340 -11.83878 1.000 74.61905  ? 262 PRO A CD  1 
ATOM   1815 N  N   . ASN A 1 281 ? -0.94851  16.74858 -14.48539 1.000 78.56442  ? 263 ASN A N   1 
ATOM   1816 C  CA  . ASN A 1 281 ? -0.36830  16.48191 -15.79685 1.000 77.51674  ? 263 ASN A CA  1 
ATOM   1817 C  C   . ASN A 1 281 ? 1.15537   16.48764 -15.78784 1.000 74.07022  ? 263 ASN A C   1 
ATOM   1818 O  O   . ASN A 1 281 ? 1.76405   16.16740 -16.81339 1.000 76.68575  ? 263 ASN A O   1 
ATOM   1819 C  CB  . ASN A 1 281 ? -0.88626  17.49545 -16.82311 1.000 75.60043  ? 263 ASN A CB  1 
ATOM   1820 C  CG  . ASN A 1 281 ? -1.10261  18.87319 -16.22858 1.000 88.27470  ? 263 ASN A CG  1 
ATOM   1821 O  OD1 . ASN A 1 281 ? -1.94235  19.05883 -15.34652 1.000 98.28188  ? 263 ASN A OD1 1 
ATOM   1822 N  ND2 . ASN A 1 281 ? -0.35470  19.85239 -16.72164 1.000 102.36711 ? 263 ASN A ND2 1 
ATOM   1823 N  N   . ILE A 1 282 ? 1.78267   16.84154 -14.66995 1.000 75.72056  ? 264 ILE A N   1 
ATOM   1824 C  CA  . ILE A 1 282 ? 3.22891   16.75343 -14.50600 1.000 74.26627  ? 264 ILE A CA  1 
ATOM   1825 C  C   . ILE A 1 282 ? 3.51340   15.68588 -13.46177 1.000 69.43642  ? 264 ILE A C   1 
ATOM   1826 O  O   . ILE A 1 282 ? 2.96344   15.73390 -12.35403 1.000 72.10881  ? 264 ILE A O   1 
ATOM   1827 C  CB  . ILE A 1 282 ? 3.84197   18.10344 -14.09168 1.000 60.43436  ? 264 ILE A CB  1 
ATOM   1828 N  N   . ILE A 1 283 ? 4.35000   14.71498 -13.81730 1.000 64.20757  ? 265 ILE A N   1 
ATOM   1829 C  CA  . ILE A 1 283 ? 4.75429   13.68317 -12.86577 1.000 64.20825  ? 265 ILE A CA  1 
ATOM   1830 C  C   . ILE A 1 283 ? 5.49856   14.38356 -11.73639 1.000 64.12232  ? 265 ILE A C   1 
ATOM   1831 O  O   . ILE A 1 283 ? 6.47415   15.10352 -11.99397 1.000 62.91104  ? 265 ILE A O   1 
ATOM   1832 C  CB  . ILE A 1 283 ? 5.61227   12.59437 -13.52993 1.000 62.18670  ? 265 ILE A CB  1 
ATOM   1833 C  CG1 . ILE A 1 283 ? 4.74322   11.70520 -14.42459 1.000 76.58131  ? 265 ILE A CG1 1 
ATOM   1834 C  CG2 . ILE A 1 283 ? 6.30443   11.74523 -12.47722 1.000 60.77847  ? 265 ILE A CG2 1 
ATOM   1835 N  N   . PRO A 1 284 ? 5.06095   14.23180 -10.48723 1.000 62.31924  ? 266 PRO A N   1 
ATOM   1836 C  CA  . PRO A 1 284 ? 5.68218   14.98323 -9.38566  1.000 55.34582  ? 266 PRO A CA  1 
ATOM   1837 C  C   . PRO A 1 284 ? 7.14340   14.60316 -9.21062  1.000 55.33778  ? 266 PRO A C   1 
ATOM   1838 O  O   . PRO A 1 284 ? 7.48579   13.43047 -9.04070  1.000 53.66182  ? 266 PRO A O   1 
ATOM   1839 C  CB  . PRO A 1 284 ? 4.84124   14.58572 -8.16528  1.000 53.96074  ? 266 PRO A CB  1 
ATOM   1840 C  CG  . PRO A 1 284 ? 3.56715   14.03629 -8.72587  1.000 60.63341  ? 266 PRO A CG  1 
ATOM   1841 C  CD  . PRO A 1 284 ? 3.93154   13.40590 -10.03217 1.000 61.23199  ? 266 PRO A CD  1 
ATOM   1842 N  N   . SER A 1 285 ? 8.00950   15.61065 -9.26564  1.000 48.36491  ? 267 SER A N   1 
ATOM   1843 C  CA  . SER A 1 285 ? 9.43599   15.43133 -9.04415  1.000 62.65890  ? 267 SER A CA  1 
ATOM   1844 C  C   . SER A 1 285 ? 9.85953   15.86499 -7.64890  1.000 57.77157  ? 267 SER A C   1 
ATOM   1845 O  O   . SER A 1 285 ? 11.05862  15.91247 -7.36021  1.000 61.15837  ? 267 SER A O   1 
ATOM   1846 C  CB  . SER A 1 285 ? 10.23369  16.19817 -10.09925 1.000 61.11833  ? 267 SER A CB  1 
ATOM   1847 O  OG  . SER A 1 285 ? 10.02932  17.59448 -9.97495  1.000 60.61317  ? 267 SER A OG  1 
ATOM   1848 N  N   . TYR A 1 286 ? 8.90317   16.17882 -6.77926  1.000 59.17952  ? 268 TYR A N   1 
ATOM   1849 C  CA  . TYR A 1 286 ? 9.20562   16.59566 -5.41967  1.000 55.96259  ? 268 TYR A CA  1 
ATOM   1850 C  C   . TYR A 1 286 ? 8.04182   16.21926 -4.51682  1.000 51.67108  ? 268 TYR A C   1 
ATOM   1851 O  O   . TYR A 1 286 ? 6.87882   16.40632 -4.88296  1.000 58.06222  ? 268 TYR A O   1 
ATOM   1852 C  CB  . TYR A 1 286 ? 9.46772   18.10353 -5.34508  1.000 58.69161  ? 268 TYR A CB  1 
ATOM   1853 C  CG  . TYR A 1 286 ? 9.60384   18.63816 -3.93721  1.000 58.50695  ? 268 TYR A CG  1 
ATOM   1854 C  CD1 . TYR A 1 286 ? 10.82081  18.58627 -3.26805  1.000 61.90928  ? 268 TYR A CD1 1 
ATOM   1855 C  CD2 . TYR A 1 286 ? 8.51575   19.20052 -3.27670  1.000 59.00562  ? 268 TYR A CD2 1 
ATOM   1856 C  CE1 . TYR A 1 286 ? 10.95041  19.07765 -1.97540  1.000 61.28959  ? 268 TYR A CE1 1 
ATOM   1857 C  CE2 . TYR A 1 286 ? 8.63525   19.69193 -1.98775  1.000 61.67565  ? 268 TYR A CE2 1 
ATOM   1858 C  CZ  . TYR A 1 286 ? 9.85526   19.62935 -1.34217  1.000 60.86823  ? 268 TYR A CZ  1 
ATOM   1859 O  OH  . TYR A 1 286 ? 9.97631   20.11841 -0.05953  1.000 63.99756  ? 268 TYR A OH  1 
ATOM   1860 N  N   . SER A 1 287 ? 8.36585   15.68326 -3.34305  1.000 48.98720  ? 269 SER A N   1 
ATOM   1861 C  CA  . SER A 1 287 ? 7.38815   15.42131 -2.29759  1.000 48.61628  ? 269 SER A CA  1 
ATOM   1862 C  C   . SER A 1 287 ? 8.05085   15.65861 -0.94779  1.000 49.88398  ? 269 SER A C   1 
ATOM   1863 O  O   . SER A 1 287 ? 9.27825   15.67525 -0.83318  1.000 51.22266  ? 269 SER A O   1 
ATOM   1864 C  CB  . SER A 1 287 ? 6.82390   13.99556 -2.38402  1.000 42.78751  ? 269 SER A CB  1 
ATOM   1865 O  OG  . SER A 1 287 ? 7.74245   13.03815 -1.88210  1.000 49.21641  ? 269 SER A OG  1 
ATOM   1866 N  N   . GLU A 1 288 ? 7.22615   15.84136 0.08066   1.000 47.67882  ? 270 GLU A N   1 
ATOM   1867 C  CA  . GLU A 1 288 ? 7.73865   16.22352 1.39002   1.000 47.36230  ? 270 GLU A CA  1 
ATOM   1868 C  C   . GLU A 1 288 ? 6.82119   15.68328 2.47533   1.000 47.41943  ? 270 GLU A C   1 
ATOM   1869 O  O   . GLU A 1 288 ? 5.60568   15.89577 2.42850   1.000 45.76635  ? 270 GLU A O   1 
ATOM   1870 C  CB  . GLU A 1 288 ? 7.86374   17.74787 1.50430   1.000 49.05815  ? 270 GLU A CB  1 
ATOM   1871 C  CG  . GLU A 1 288 ? 8.12420   18.26419 2.92002   1.000 52.79341  ? 270 GLU A CG  1 
ATOM   1872 C  CD  . GLU A 1 288 ? 8.11909   19.78627 2.99438   1.000 58.36681  ? 270 GLU A CD  1 
ATOM   1873 O  OE1 . GLU A 1 288 ? 8.50711   20.43804 1.99862   1.000 64.31966  ? 270 GLU A OE1 1 
ATOM   1874 O  OE2 . GLU A 1 288 ? 7.71691   20.33146 4.04358   1.000 64.40446  ? 270 GLU A OE2 1 
ATOM   1875 N  N   . LEU A 1 289 ? 7.40653   14.99018 3.44732   1.000 42.06396  ? 271 LEU A N   1 
ATOM   1876 C  CA  . LEU A 1 289 ? 6.67445   14.46289 4.58817   1.000 49.60756  ? 271 LEU A CA  1 
ATOM   1877 C  C   . LEU A 1 289 ? 7.22382   15.07276 5.87058   1.000 48.68563  ? 271 LEU A C   1 
ATOM   1878 O  O   . LEU A 1 289 ? 8.39145   15.46926 5.93860   1.000 55.86230  ? 271 LEU A O   1 
ATOM   1879 C  CB  . LEU A 1 289 ? 6.76913   12.93257 4.65733   1.000 41.86784  ? 271 LEU A CB  1 
ATOM   1880 C  CG  . LEU A 1 289 ? 6.31444   12.16075 3.41429   1.000 51.98233  ? 271 LEU A CG  1 
ATOM   1881 C  CD1 . LEU A 1 289 ? 7.47248   11.94262 2.45546   1.000 48.90144  ? 271 LEU A CD1 1 
ATOM   1882 C  CD2 . LEU A 1 289 ? 5.70947   10.82813 3.80455   1.000 38.62059  ? 271 LEU A CD2 1 
ATOM   1883 N  N   . ILE A 1 290 ? 6.36936   15.15658 6.88605   1.000 48.46216  ? 272 ILE A N   1 
ATOM   1884 C  CA  . ILE A 1 290 ? 6.75768   15.65000 8.20205   1.000 52.78576  ? 272 ILE A CA  1 
ATOM   1885 C  C   . ILE A 1 290 ? 6.26254   14.65452 9.24060   1.000 51.29904  ? 272 ILE A C   1 
ATOM   1886 O  O   . ILE A 1 290 ? 5.05622   14.39590 9.33116   1.000 54.57670  ? 272 ILE A O   1 
ATOM   1887 C  CB  . ILE A 1 290 ? 6.20137   17.05513 8.48699   1.000 53.88052  ? 272 ILE A CB  1 
ATOM   1888 C  CG1 . ILE A 1 290 ? 6.52911   18.00872 7.33856   1.000 49.67113  ? 272 ILE A CG1 1 
ATOM   1889 C  CG2 . ILE A 1 290 ? 6.78673   17.59849 9.77047   1.000 55.12303  ? 272 ILE A CG2 1 
ATOM   1890 C  CD1 . ILE A 1 290 ? 6.04297   19.41763 7.57427   1.000 53.44576  ? 272 ILE A CD1 1 
ATOM   1891 N  N   . TYR A 1 291 ? 7.18814   14.10426 10.02404  1.000 52.37219  ? 273 TYR A N   1 
ATOM   1892 C  CA  . TYR A 1 291 ? 6.88896   13.05872 10.99150  1.000 44.93946  ? 273 TYR A CA  1 
ATOM   1893 C  C   . TYR A 1 291 ? 7.51198   13.39908 12.33706  1.000 44.63585  ? 273 TYR A C   1 
ATOM   1894 O  O   . TYR A 1 291 ? 8.50190   14.13269 12.42428  1.000 54.11190  ? 273 TYR A O   1 
ATOM   1895 C  CB  . TYR A 1 291 ? 7.42293   11.69361 10.53052  1.000 40.72873  ? 273 TYR A CB  1 
ATOM   1896 C  CG  . TYR A 1 291 ? 6.44457   10.87516 9.73251   1.000 49.68758  ? 273 TYR A CG  1 
ATOM   1897 C  CD1 . TYR A 1 291 ? 6.29873   11.07669 8.36467   1.000 53.82848  ? 273 TYR A CD1 1 
ATOM   1898 C  CD2 . TYR A 1 291 ? 5.68104   9.88679  10.33665  1.000 45.11654  ? 273 TYR A CD2 1 
ATOM   1899 C  CE1 . TYR A 1 291 ? 5.40670   10.32624 7.62249   1.000 51.40130  ? 273 TYR A CE1 1 
ATOM   1900 C  CE2 . TYR A 1 291 ? 4.78624   9.12910  9.60322   1.000 49.61806  ? 273 TYR A CE2 1 
ATOM   1901 C  CZ  . TYR A 1 291 ? 4.65410   9.35268  8.24568   1.000 53.98941  ? 273 TYR A CZ  1 
ATOM   1902 O  OH  . TYR A 1 291 ? 3.76331   8.60497  7.50743   1.000 45.48778  ? 273 TYR A OH  1 
ATOM   1903 N  N   . TYR A 1 292 ? 6.92729   12.83390 13.39016  1.000 44.32374  ? 274 TYR A N   1 
ATOM   1904 C  CA  . TYR A 1 292 ? 7.53482   12.84336 14.71122  1.000 51.47685  ? 274 TYR A CA  1 
ATOM   1905 C  C   . TYR A 1 292 ? 7.34709   11.47248 15.34635  1.000 50.24149  ? 274 TYR A C   1 
ATOM   1906 O  O   . TYR A 1 292 ? 6.31590   10.82402 15.14754  1.000 51.93759  ? 274 TYR A O   1 
ATOM   1907 C  CB  . TYR A 1 292 ? 6.95770   13.97349 15.59104  1.000 55.84003  ? 274 TYR A CB  1 
ATOM   1908 C  CG  . TYR A 1 292 ? 5.57884   13.75580 16.17665  1.000 59.98073  ? 274 TYR A CG  1 
ATOM   1909 C  CD1 . TYR A 1 292 ? 4.45703   14.32020 15.58040  1.000 70.73794  ? 274 TYR A CD1 1 
ATOM   1910 C  CD2 . TYR A 1 292 ? 5.40049   13.04115 17.35801  1.000 68.70793  ? 274 TYR A CD2 1 
ATOM   1911 C  CE1 . TYR A 1 292 ? 3.18865   14.14465 16.11962  1.000 74.01560  ? 274 TYR A CE1 1 
ATOM   1912 C  CE2 . TYR A 1 292 ? 4.13565   12.86142 17.90565  1.000 71.09491  ? 274 TYR A CE2 1 
ATOM   1913 C  CZ  . TYR A 1 292 ? 3.03431   13.41649 17.28257  1.000 78.03242  ? 274 TYR A CZ  1 
ATOM   1914 O  OH  . TYR A 1 292 ? 1.77572   13.24364 17.81950  1.000 75.79497  ? 274 TYR A OH  1 
ATOM   1915 N  N   . PHE A 1 293 ? 8.36591   11.02713 16.08044  1.000 45.83014  ? 275 PHE A N   1 
ATOM   1916 C  CA  . PHE A 1 293 ? 8.37784   9.73211  16.74510  1.000 52.05090  ? 275 PHE A CA  1 
ATOM   1917 C  C   . PHE A 1 293 ? 8.53778   9.92230  18.24857  1.000 51.08833  ? 275 PHE A C   1 
ATOM   1918 O  O   . PHE A 1 293 ? 9.19698   10.86048 18.70340  1.000 54.54534  ? 275 PHE A O   1 
ATOM   1919 C  CB  . PHE A 1 293 ? 9.51978   8.84494  16.22220  1.000 49.35687  ? 275 PHE A CB  1 
ATOM   1920 C  CG  . PHE A 1 293 ? 9.73136   8.93376  14.73637  1.000 46.82281  ? 275 PHE A CG  1 
ATOM   1921 C  CD1 . PHE A 1 293 ? 8.72781   8.56503  13.85414  1.000 55.15248  ? 275 PHE A CD1 1 
ATOM   1922 C  CD2 . PHE A 1 293 ? 10.93643  9.37769  14.22164  1.000 56.83842  ? 275 PHE A CD2 1 
ATOM   1923 C  CE1 . PHE A 1 293 ? 8.92409   8.64170  12.48375  1.000 55.73843  ? 275 PHE A CE1 1 
ATOM   1924 C  CE2 . PHE A 1 293 ? 11.13848  9.45800  12.85146  1.000 60.41300  ? 275 PHE A CE2 1 
ATOM   1925 C  CZ  . PHE A 1 293 ? 10.13133  9.08886  11.98274  1.000 48.63682  ? 275 PHE A CZ  1 
ATOM   1926 N  N   . ARG A 1 294 ? 7.94479   9.01437  19.01950  1.000 47.84035  ? 276 ARG A N   1 
ATOM   1927 C  CA  . ARG A 1 294 ? 8.00234   9.08039  20.47265  1.000 46.65806  ? 276 ARG A CA  1 
ATOM   1928 C  C   . ARG A 1 294 ? 8.28494   7.70172  21.04759  1.000 52.33598  ? 276 ARG A C   1 
ATOM   1929 O  O   . ARG A 1 294 ? 7.78529   6.69512  20.53675  1.000 56.75885  ? 276 ARG A O   1 
ATOM   1930 C  CB  . ARG A 1 294 ? 6.69374   9.61732  21.06258  1.000 53.43893  ? 276 ARG A CB  1 
ATOM   1931 C  CG  . ARG A 1 294 ? 6.65694   11.11763 21.23383  1.000 61.11507  ? 276 ARG A CG  1 
ATOM   1932 C  CD  . ARG A 1 294 ? 5.23073   11.60499 21.36832  1.000 59.93569  ? 276 ARG A CD  1 
ATOM   1933 N  NE  . ARG A 1 294 ? 5.09372   12.96743 20.87301  1.000 76.41448  ? 276 ARG A NE  1 
ATOM   1934 C  CZ  . ARG A 1 294 ? 4.21113   13.84515 21.32660  1.000 84.00428  ? 276 ARG A CZ  1 
ATOM   1935 N  NH1 . ARG A 1 294 ? 3.34944   13.52833 22.27853  1.000 88.86352  ? 276 ARG A NH1 1 
ATOM   1936 N  NH2 . ARG A 1 294 ? 4.18512   15.06789 20.80343  1.000 88.69102  ? 276 ARG A NH2 1 
ATOM   1937 N  N   . ALA A 1 295 ? 9.07379   7.66834  22.12120  1.000 52.15098  ? 277 ALA A N   1 
ATOM   1938 C  CA  . ALA A 1 295 ? 9.41365   6.44417  22.83297  1.000 58.32879  ? 277 ALA A CA  1 
ATOM   1939 C  C   . ALA A 1 295 ? 9.75447   6.79600  24.27544  1.000 58.77091  ? 277 ALA A C   1 
ATOM   1940 O  O   . ALA A 1 295 ? 10.20833  7.91441  24.54615  1.000 56.33611  ? 277 ALA A O   1 
ATOM   1941 C  CB  . ALA A 1 295 ? 10.58908  5.71566  22.16404  1.000 53.29040  ? 277 ALA A CB  1 
ATOM   1942 N  N   . PRO A 1 296 ? 9.54982   5.87033  25.22000  1.000 53.61384  ? 278 PRO A N   1 
ATOM   1943 C  CA  . PRO A 1 296 ? 9.76588   6.19991  26.64276  1.000 62.60590  ? 278 PRO A CA  1 
ATOM   1944 C  C   . PRO A 1 296 ? 11.22058  6.43168  27.03454  1.000 57.43329  ? 278 PRO A C   1 
ATOM   1945 O  O   . PRO A 1 296 ? 11.45935  6.96908  28.12362  1.000 60.93945  ? 278 PRO A O   1 
ATOM   1946 C  CB  . PRO A 1 296 ? 9.18859   4.98219  27.38065  1.000 47.98602  ? 278 PRO A CB  1 
ATOM   1947 C  CG  . PRO A 1 296 ? 9.15434   3.88588  26.35995  1.000 62.20874  ? 278 PRO A CG  1 
ATOM   1948 C  CD  . PRO A 1 296 ? 8.91479   4.55312  25.04518  1.000 55.91898  ? 278 PRO A CD  1 
ATOM   1949 N  N   . SER A 1 297 ? 12.19276  6.05353  26.20683  1.000 59.04191  ? 279 SER A N   1 
ATOM   1950 C  CA  . SER A 1 297 ? 13.59743  6.27472  26.52496  1.000 57.71020  ? 279 SER A CA  1 
ATOM   1951 C  C   . SER A 1 297 ? 14.34422  6.68646  25.26515  1.000 55.62582  ? 279 SER A C   1 
ATOM   1952 O  O   . SER A 1 297 ? 13.86218  6.50553  24.14445  1.000 58.70217  ? 279 SER A O   1 
ATOM   1953 C  CB  . SER A 1 297 ? 14.24653  5.02669  27.13613  1.000 58.96773  ? 279 SER A CB  1 
ATOM   1954 O  OG  . SER A 1 297 ? 14.39911  4.00810  26.16338  1.000 58.70491  ? 279 SER A OG  1 
ATOM   1955 N  N   . MET A 1 298 ? 15.53644  7.25144  25.46141  1.000 55.21137  ? 280 MET A N   1 
ATOM   1956 C  CA  . MET A 1 298 ? 16.33708  7.67817  24.31746  1.000 62.32148  ? 280 MET A CA  1 
ATOM   1957 C  C   . MET A 1 298 ? 16.87247  6.48178  23.54039  1.000 61.61910  ? 280 MET A C   1 
ATOM   1958 O  O   . MET A 1 298 ? 16.97937  6.53298  22.30883  1.000 62.22254  ? 280 MET A O   1 
ATOM   1959 C  CB  . MET A 1 298 ? 17.48397  8.57795  24.77943  1.000 60.75635  ? 280 MET A CB  1 
ATOM   1960 C  CG  . MET A 1 298 ? 17.03011  9.91944  25.33235  1.000 73.04580  ? 280 MET A CG  1 
ATOM   1961 S  SD  . MET A 1 298 ? 16.12031  10.90402 24.12146  1.000 83.65449  ? 280 MET A SD  1 
ATOM   1962 C  CE  . MET A 1 298 ? 17.29345  10.95412 22.77215  1.000 59.34948  ? 280 MET A CE  1 
ATOM   1963 N  N   . LYS A 1 299 ? 17.21076  5.39433  24.23896  1.000 54.33362  ? 281 LYS A N   1 
ATOM   1964 C  CA  . LYS A 1 299 ? 17.70659  4.20801  23.54937  1.000 56.71268  ? 281 LYS A CA  1 
ATOM   1965 C  C   . LYS A 1 299 ? 16.62196  3.59030  22.67545  1.000 59.95398  ? 281 LYS A C   1 
ATOM   1966 O  O   . LYS A 1 299 ? 16.88668  3.18860  21.53534  1.000 55.63787  ? 281 LYS A O   1 
ATOM   1967 C  CB  . LYS A 1 299 ? 18.23600  3.19015  24.56110  1.000 51.45154  ? 281 LYS A CB  1 
ATOM   1968 N  N   . GLU A 1 300 ? 15.39323  3.51097  23.18858  1.000 54.27156  ? 282 GLU A N   1 
ATOM   1969 C  CA  . GLU A 1 300 ? 14.28986  3.02995  22.36512  1.000 58.76773  ? 282 GLU A CA  1 
ATOM   1970 C  C   . GLU A 1 300 ? 13.99673  3.99421  21.22290  1.000 56.62858  ? 282 GLU A C   1 
ATOM   1971 O  O   . GLU A 1 300 ? 13.66517  3.56587  20.11111  1.000 52.56851  ? 282 GLU A O   1 
ATOM   1972 C  CB  . GLU A 1 300 ? 13.04406  2.81883  23.22398  1.000 57.95245  ? 282 GLU A CB  1 
ATOM   1973 C  CG  . GLU A 1 300 ? 13.04440  1.51397  24.00623  1.000 60.15130  ? 282 GLU A CG  1 
ATOM   1974 C  CD  . GLU A 1 300 ? 11.78061  1.32881  24.82042  1.000 67.13126  ? 282 GLU A CD  1 
ATOM   1975 O  OE1 . GLU A 1 300 ? 10.79054  0.79528  24.27827  1.000 74.66377  ? 282 GLU A OE1 1 
ATOM   1976 O  OE2 . GLU A 1 300 ? 11.77555  1.72266  26.00408  1.000 72.88812  ? 282 GLU A OE2 1 
ATOM   1977 N  N   . LEU A 1 301 ? 14.11966  5.30017  21.47297  1.000 50.93408  ? 283 LEU A N   1 
ATOM   1978 C  CA  . LEU A 1 301 ? 13.83149  6.26768  20.42175  1.000 51.85833  ? 283 LEU A CA  1 
ATOM   1979 C  C   . LEU A 1 301 ? 14.82396  6.15714  19.27233  1.000 54.66574  ? 283 LEU A C   1 
ATOM   1980 O  O   . LEU A 1 301 ? 14.44480  6.35255  18.11284  1.000 51.76032  ? 283 LEU A O   1 
ATOM   1981 C  CB  . LEU A 1 301 ? 13.82369  7.68659  20.99121  1.000 45.83659  ? 283 LEU A CB  1 
ATOM   1982 C  CG  . LEU A 1 301 ? 13.45928  8.78597  19.98958  1.000 57.24751  ? 283 LEU A CG  1 
ATOM   1983 C  CD1 . LEU A 1 301 ? 12.02718  8.60790  19.50212  1.000 56.82872  ? 283 LEU A CD1 1 
ATOM   1984 C  CD2 . LEU A 1 301 ? 13.65551  10.16920 20.59837  1.000 55.28911  ? 283 LEU A CD2 1 
ATOM   1985 N  N   . GLN A 1 302 ? 16.08759  5.83532  19.56650  1.000 51.54983  ? 284 GLN A N   1 
ATOM   1986 C  CA  . GLN A 1 302 ? 17.06940  5.66491  18.49885  1.000 55.57421  ? 284 GLN A CA  1 
ATOM   1987 C  C   . GLN A 1 302 ? 16.75512  4.43806  17.65100  1.000 55.31550  ? 284 GLN A C   1 
ATOM   1988 O  O   . GLN A 1 302 ? 16.94793  4.45510  16.42926  1.000 50.36770  ? 284 GLN A O   1 
ATOM   1989 C  CB  . GLN A 1 302 ? 18.48030  5.56695  19.08353  1.000 52.31724  ? 284 GLN A CB  1 
ATOM   1990 N  N   . VAL A 1 303 ? 16.27187  3.36507  18.27996  1.000 54.10889  ? 285 VAL A N   1 
ATOM   1991 C  CA  . VAL A 1 303 ? 15.88633  2.17313  17.52970  1.000 50.71008  ? 285 VAL A CA  1 
ATOM   1992 C  C   . VAL A 1 303 ? 14.68878  2.47468  16.63599  1.000 53.00778  ? 285 VAL A C   1 
ATOM   1993 O  O   . VAL A 1 303 ? 14.66868  2.11805  15.45239  1.000 55.00342  ? 285 VAL A O   1 
ATOM   1994 C  CB  . VAL A 1 303 ? 15.59994  1.00863  18.49411  1.000 49.93786  ? 285 VAL A CB  1 
ATOM   1995 C  CG1 . VAL A 1 303 ? 14.99913  -0.17032 17.75051  1.000 49.29469  ? 285 VAL A CG1 1 
ATOM   1996 C  CG2 . VAL A 1 303 ? 16.87784  0.59506  19.20714  1.000 48.52576  ? 285 VAL A CG2 1 
ATOM   1997 N  N   . LEU A 1 304 ? 13.67967  3.15078  17.18800  1.000 55.76386  ? 286 LEU A N   1 
ATOM   1998 C  CA  . LEU A 1 304 ? 12.50529  3.52030  16.40319  1.000 50.31202  ? 286 LEU A CA  1 
ATOM   1999 C  C   . LEU A 1 304 ? 12.87606  4.44941  15.25280  1.000 54.95693  ? 286 LEU A C   1 
ATOM   2000 O  O   . LEU A 1 304 ? 12.34612  4.32011  14.14234  1.000 50.47825  ? 286 LEU A O   1 
ATOM   2001 C  CB  . LEU A 1 304 ? 11.46858  4.17299  17.31673  1.000 52.68208  ? 286 LEU A CB  1 
ATOM   2002 C  CG  . LEU A 1 304 ? 10.26266  4.88707  16.70830  1.000 55.16045  ? 286 LEU A CG  1 
ATOM   2003 C  CD1 . LEU A 1 304 ? 9.45321   3.93355  15.84582  1.000 52.07605  ? 286 LEU A CD1 1 
ATOM   2004 C  CD2 . LEU A 1 304 ? 9.40296   5.47406  17.82400  1.000 49.27087  ? 286 LEU A CD2 1 
ATOM   2005 N  N   . THR A 1 305 ? 13.79385  5.38652  15.49528  1.000 52.54728  ? 287 THR A N   1 
ATOM   2006 C  CA  . THR A 1 305 ? 14.20613  6.30482  14.43928  1.000 53.04727  ? 287 THR A CA  1 
ATOM   2007 C  C   . THR A 1 305 ? 14.96278  5.57503  13.33440  1.000 55.22636  ? 287 THR A C   1 
ATOM   2008 O  O   . THR A 1 305 ? 14.83062  5.91738  12.15297  1.000 50.33554  ? 287 THR A O   1 
ATOM   2009 C  CB  . THR A 1 305 ? 15.05612  7.43020  15.03356  1.000 46.71370  ? 287 THR A CB  1 
ATOM   2010 O  OG1 . THR A 1 305 ? 14.25561  8.20789  15.93452  1.000 52.22139  ? 287 THR A OG1 1 
ATOM   2011 C  CG2 . THR A 1 305 ? 15.60816  8.33535  13.93805  1.000 52.95434  ? 287 THR A CG2 1 
ATOM   2012 N  N   . LYS A 1 306 ? 15.74918  4.55666  13.69404  1.000 48.04331  ? 288 LYS A N   1 
ATOM   2013 C  CA  . LYS A 1 306 ? 16.52076  3.83906  12.68385  1.000 55.90626  ? 288 LYS A CA  1 
ATOM   2014 C  C   . LYS A 1 306 ? 15.61293  3.01481  11.77711  1.000 53.05441  ? 288 LYS A C   1 
ATOM   2015 O  O   . LYS A 1 306 ? 15.83741  2.95075  10.56242  1.000 53.36934  ? 288 LYS A O   1 
ATOM   2016 C  CB  . LYS A 1 306 ? 17.57632  2.95659  13.35541  1.000 53.95692  ? 288 LYS A CB  1 
ATOM   2017 C  CG  . LYS A 1 306 ? 18.14622  1.85237  12.47238  1.000 60.25471  ? 288 LYS A CG  1 
ATOM   2018 C  CD  . LYS A 1 306 ? 19.01211  2.40622  11.34575  1.000 66.93735  ? 288 LYS A CD  1 
ATOM   2019 C  CE  . LYS A 1 306 ? 19.44789  1.29545  10.39597  1.000 69.26729  ? 288 LYS A CE  1 
ATOM   2020 N  NZ  . LYS A 1 306 ? 20.13682  1.82310  9.18545   1.000 70.57410  ? 288 LYS A NZ  1 
ATOM   2021 N  N   . LYS A 1 307 ? 14.57852  2.38344  12.34345  1.000 51.29560  ? 289 LYS A N   1 
ATOM   2022 C  CA  . LYS A 1 307 ? 13.64206  1.62500  11.51782  1.000 48.97741  ? 289 LYS A CA  1 
ATOM   2023 C  C   . LYS A 1 307 ? 12.85969  2.54726  10.59298  1.000 51.17292  ? 289 LYS A C   1 
ATOM   2024 O  O   . LYS A 1 307 ? 12.58325  2.19373  9.43993   1.000 54.31175  ? 289 LYS A O   1 
ATOM   2025 C  CB  . LYS A 1 307 ? 12.68572  0.81608  12.39523  1.000 49.94747  ? 289 LYS A CB  1 
ATOM   2026 C  CG  . LYS A 1 307 ? 13.37038  -0.01064 13.47232  1.000 62.75498  ? 289 LYS A CG  1 
ATOM   2027 C  CD  . LYS A 1 307 ? 13.21031  -1.50353 13.22548  1.000 71.46418  ? 289 LYS A CD  1 
ATOM   2028 C  CE  . LYS A 1 307 ? 13.82876  -2.31735 14.35883  1.000 56.74938  ? 289 LYS A CE  1 
ATOM   2029 N  NZ  . LYS A 1 307 ? 13.42347  -3.74745 14.27735  1.000 71.22402  ? 289 LYS A NZ  1 
ATOM   2030 N  N   . ALA A 1 308 ? 12.49155  3.73323  11.08032  1.000 53.99667  ? 290 ALA A N   1 
ATOM   2031 C  CA  . ALA A 1 308 ? 11.83488  4.70539  10.21438  1.000 53.39691  ? 290 ALA A CA  1 
ATOM   2032 C  C   . ALA A 1 308 ? 12.76593  5.15156  9.09624   1.000 53.21805  ? 290 ALA A C   1 
ATOM   2033 O  O   . ALA A 1 308 ? 12.34116  5.28895  7.94283   1.000 55.21448  ? 290 ALA A O   1 
ATOM   2034 C  CB  . ALA A 1 308 ? 11.35947  5.90652  11.03109  1.000 43.72293  ? 290 ALA A CB  1 
ATOM   2035 N  N   . GLU A 1 309 ? 14.04127  5.38487  9.42201   1.000 46.54167  ? 291 GLU A N   1 
ATOM   2036 C  CA  . GLU A 1 309 ? 15.01874  5.73985  8.39944   1.000 50.53951  ? 291 GLU A CA  1 
ATOM   2037 C  C   . GLU A 1 309 ? 15.07631  4.68152  7.30324   1.000 54.31705  ? 291 GLU A C   1 
ATOM   2038 O  O   . GLU A 1 309 ? 15.13073  5.01208  6.11181   1.000 54.31739  ? 291 GLU A O   1 
ATOM   2039 C  CB  . GLU A 1 309 ? 16.39345  5.93243  9.04178   1.000 52.80765  ? 291 GLU A CB  1 
ATOM   2040 C  CG  . GLU A 1 309 ? 17.56111  5.61289  8.11957   1.000 60.68309  ? 291 GLU A CG  1 
ATOM   2041 C  CD  . GLU A 1 309 ? 18.74375  6.54246  8.31417   1.000 81.44829  ? 291 GLU A CD  1 
ATOM   2042 O  OE1 . GLU A 1 309 ? 19.42685  6.84954  7.31363   1.000 82.03377  ? 291 GLU A OE1 1 
ATOM   2043 O  OE2 . GLU A 1 309 ? 18.99534  6.95948  9.46672   1.000 84.08964  ? 291 GLU A OE2 1 
ATOM   2044 N  N   . ASP A 1 310 ? 15.05870  3.40162  7.68579   1.000 45.30634  ? 292 ASP A N   1 
ATOM   2045 C  CA  . ASP A 1 310 ? 14.99776  2.33932  6.68702   1.000 52.13810  ? 292 ASP A CA  1 
ATOM   2046 C  C   . ASP A 1 310 ? 13.74314  2.45752  5.83117   1.000 50.67493  ? 292 ASP A C   1 
ATOM   2047 O  O   . ASP A 1 310 ? 13.79885  2.28111  4.60762   1.000 49.12825  ? 292 ASP A O   1 
ATOM   2048 C  CB  . ASP A 1 310 ? 15.05454  0.97216  7.36593   1.000 50.23703  ? 292 ASP A CB  1 
ATOM   2049 C  CG  . ASP A 1 310 ? 16.40285  0.69372  7.99278   1.000 57.98006  ? 292 ASP A CG  1 
ATOM   2050 O  OD1 . ASP A 1 310 ? 17.35268  1.46172  7.72284   1.000 56.39992  ? 292 ASP A OD1 1 
ATOM   2051 O  OD2 . ASP A 1 310 ? 16.51379  -0.28977 8.75499   1.000 55.53692  ? 292 ASP A OD2 1 
ATOM   2052 N  N   . CYS A 1 311 ? 12.60079  2.75932  6.45401   1.000 44.72755  ? 293 CYS A N   1 
ATOM   2053 C  CA  . CYS A 1 311 ? 11.36322  2.88600  5.68922   1.000 46.71631  ? 293 CYS A CA  1 
ATOM   2054 C  C   . CYS A 1 311 ? 11.44257  4.04715  4.70287   1.000 50.09302  ? 293 CYS A C   1 
ATOM   2055 O  O   . CYS A 1 311 ? 10.96223  3.94295  3.56781   1.000 43.07707  ? 293 CYS A O   1 
ATOM   2056 C  CB  . CYS A 1 311 ? 10.17516  3.05952  6.63594   1.000 44.07162  ? 293 CYS A CB  1 
ATOM   2057 S  SG  . CYS A 1 311 ? 9.67920   1.55493  7.53568   1.000 45.89906  ? 293 CYS A SG  1 
ATOM   2058 N  N   . PHE A 1 312 ? 12.06300  5.15745  5.10892   1.000 38.66327  ? 294 PHE A N   1 
ATOM   2059 C  CA  . PHE A 1 312 ? 12.18451  6.29266  4.20066   1.000 44.79444  ? 294 PHE A CA  1 
ATOM   2060 C  C   . PHE A 1 312 ? 13.16018  5.99101  3.07117   1.000 51.12453  ? 294 PHE A C   1 
ATOM   2061 O  O   . PHE A 1 312 ? 12.90846  6.34668  1.91191   1.000 47.37204  ? 294 PHE A O   1 
ATOM   2062 C  CB  . PHE A 1 312 ? 12.62228  7.53941  4.96742   1.000 45.43905  ? 294 PHE A CB  1 
ATOM   2063 C  CG  . PHE A 1 312 ? 11.57089  8.08054  5.89867   1.000 52.52898  ? 294 PHE A CG  1 
ATOM   2064 C  CD1 . PHE A 1 312 ? 10.27640  8.30867  5.45087   1.000 48.69411  ? 294 PHE A CD1 1 
ATOM   2065 C  CD2 . PHE A 1 312 ? 11.87666  8.36172  7.22183   1.000 46.59240  ? 294 PHE A CD2 1 
ATOM   2066 C  CE1 . PHE A 1 312 ? 9.30180   8.80977  6.30936   1.000 45.69229  ? 294 PHE A CE1 1 
ATOM   2067 C  CE2 . PHE A 1 312 ? 10.91044  8.86149  8.08276   1.000 53.72792  ? 294 PHE A CE2 1 
ATOM   2068 C  CZ  . PHE A 1 312 ? 9.62051   9.08625  7.62369   1.000 48.35403  ? 294 PHE A CZ  1 
ATOM   2069 N  N   . ARG A 1 313 ? 14.27550  5.32803  3.38612   1.000 45.22480  ? 295 ARG A N   1 
ATOM   2070 C  CA  . ARG A 1 313 ? 15.26034  5.03102  2.35409   1.000 48.30460  ? 295 ARG A CA  1 
ATOM   2071 C  C   . ARG A 1 313 ? 14.75860  3.96222  1.39452   1.000 49.55402  ? 295 ARG A C   1 
ATOM   2072 O  O   . ARG A 1 313 ? 15.07696  4.01176  0.19980   1.000 43.11761  ? 295 ARG A O   1 
ATOM   2073 C  CB  . ARG A 1 313 ? 16.58647  4.61372  2.99130   1.000 47.17615  ? 295 ARG A CB  1 
ATOM   2074 C  CG  . ARG A 1 313 ? 17.23216  5.73439  3.79747   1.000 58.26534  ? 295 ARG A CG  1 
ATOM   2075 C  CD  . ARG A 1 313 ? 18.74473  5.58900  3.91034   1.000 65.61841  ? 295 ARG A CD  1 
ATOM   2076 N  NE  . ARG A 1 313 ? 19.29158  6.60824  4.79958   1.000 66.88458  ? 295 ARG A NE  1 
ATOM   2077 C  CZ  . ARG A 1 313 ? 19.66399  7.82224  4.41496   1.000 63.21618  ? 295 ARG A CZ  1 
ATOM   2078 N  NH1 . ARG A 1 313 ? 19.64081  8.18301  3.14161   1.000 64.50059  ? 295 ARG A NH1 1 
ATOM   2079 N  NH2 . ARG A 1 313 ? 20.06549  8.69846  5.33220   1.000 62.57680  ? 295 ARG A NH2 1 
ATOM   2080 N  N   . ALA A 1 314 ? 13.95880  3.00904  1.88498   1.000 40.07616  ? 296 ALA A N   1 
ATOM   2081 C  CA  . ALA A 1 314 ? 13.41613  1.98237  1.00030   1.000 43.52646  ? 296 ALA A CA  1 
ATOM   2082 C  C   . ALA A 1 314 ? 12.52891  2.59481  -0.07273  1.000 47.39772  ? 296 ALA A C   1 
ATOM   2083 O  O   . ALA A 1 314 ? 12.57456  2.18011  -1.23678  1.000 44.69339  ? 296 ALA A O   1 
ATOM   2084 C  CB  . ALA A 1 314 ? 12.63394  0.94762  1.80096   1.000 37.76901  ? 296 ALA A CB  1 
ATOM   2085 N  N   . ALA A 1 315 ? 11.71848  3.58944  0.29880   1.000 41.94716  ? 297 ALA A N   1 
ATOM   2086 C  CA  . ALA A 1 315 ? 10.86141  4.24585  -0.68235  1.000 45.04519  ? 297 ALA A CA  1 
ATOM   2087 C  C   . ALA A 1 315 ? 11.68944  4.91267  -1.77375  1.000 48.55233  ? 297 ALA A C   1 
ATOM   2088 O  O   . ALA A 1 315 ? 11.31384  4.88686  -2.95196  1.000 42.87404  ? 297 ALA A O   1 
ATOM   2089 C  CB  . ALA A 1 315 ? 9.95635   5.26379  0.00939   1.000 32.67507  ? 297 ALA A CB  1 
ATOM   2090 N  N   . ALA A 1 316 ? 12.82749  5.50456  -1.40146  1.000 49.16750  ? 298 ALA A N   1 
ATOM   2091 C  CA  . ALA A 1 316 ? 13.72858  6.07665  -2.39690  1.000 41.78757  ? 298 ALA A CA  1 
ATOM   2092 C  C   . ALA A 1 316 ? 14.25726  4.99932  -3.33565  1.000 50.92411  ? 298 ALA A C   1 
ATOM   2093 O  O   . ALA A 1 316 ? 14.23229  5.16017  -4.56329  1.000 48.65875  ? 298 ALA A O   1 
ATOM   2094 C  CB  . ALA A 1 316 ? 14.88075  6.80296  -1.70495  1.000 42.91327  ? 298 ALA A CB  1 
ATOM   2095 N  N   . LEU A 1 317 ? 14.73042  3.88304  -2.77223  1.000 41.54105  ? 299 LEU A N   1 
ATOM   2096 C  CA  . LEU A 1 317 ? 15.23064  2.78927  -3.59980  1.000 41.22386  ? 299 LEU A CA  1 
ATOM   2097 C  C   . LEU A 1 317 ? 14.15038  2.25956  -4.53712  1.000 45.55403  ? 299 LEU A C   1 
ATOM   2098 O  O   . LEU A 1 317 ? 14.41091  2.01986  -5.72326  1.000 47.99580  ? 299 LEU A O   1 
ATOM   2099 C  CB  . LEU A 1 317 ? 15.76833  1.66469  -2.71354  1.000 43.04842  ? 299 LEU A CB  1 
ATOM   2100 C  CG  . LEU A 1 317 ? 16.24372  0.39113  -3.42365  1.000 56.17314  ? 299 LEU A CG  1 
ATOM   2101 C  CD1 . LEU A 1 317 ? 17.32263  0.70670  -4.45515  1.000 52.60579  ? 299 LEU A CD1 1 
ATOM   2102 C  CD2 . LEU A 1 317 ? 16.76265  -0.62185 -2.41400  1.000 43.99828  ? 299 LEU A CD2 1 
ATOM   2103 N  N   . ALA A 1 318 ? 12.92737  2.07984  -4.02633  1.000 40.55514  ? 300 ALA A N   1 
ATOM   2104 C  CA  . ALA A 1 318 ? 11.85873  1.50753  -4.84139  1.000 47.24052  ? 300 ALA A CA  1 
ATOM   2105 C  C   . ALA A 1 318 ? 11.43082  2.45851  -5.95364  1.000 43.12566  ? 300 ALA A C   1 
ATOM   2106 O  O   . ALA A 1 318 ? 11.09177  2.01964  -7.05818  1.000 40.92493  ? 300 ALA A O   1 
ATOM   2107 C  CB  . ALA A 1 318 ? 10.66281  1.14657  -3.95951  1.000 43.89263  ? 300 ALA A CB  1 
ATOM   2108 N  N   . SER A 1 319 ? 11.44010  3.76156  -5.68469  1.000 43.46421  ? 301 SER A N   1 
ATOM   2109 C  CA  . SER A 1 319 ? 10.97378  4.73632  -6.66172  1.000 44.86102  ? 301 SER A CA  1 
ATOM   2110 C  C   . SER A 1 319 ? 12.07443  5.21974  -7.59285  1.000 50.46406  ? 301 SER A C   1 
ATOM   2111 O  O   . SER A 1 319 ? 11.77704  5.64890  -8.71374  1.000 45.97023  ? 301 SER A O   1 
ATOM   2112 C  CB  . SER A 1 319 ? 10.35645  5.94300  -5.94895  1.000 48.40670  ? 301 SER A CB  1 
ATOM   2113 O  OG  . SER A 1 319 ? 11.33619  6.64032  -5.18971  1.000 46.06546  ? 301 SER A OG  1 
ATOM   2114 N  N   . GLY A 1 320 ? 13.33316  5.15905  -7.15995  1.000 47.54854  ? 302 GLY A N   1 
ATOM   2115 C  CA  . GLY A 1 320 ? 14.43577  5.70165  -7.92470  1.000 39.64064  ? 302 GLY A CA  1 
ATOM   2116 C  C   . GLY A 1 320 ? 14.80127  7.12464  -7.56588  1.000 56.91719  ? 302 GLY A C   1 
ATOM   2117 O  O   . GLY A 1 320 ? 15.70671  7.69418  -8.19054  1.000 58.92077  ? 302 GLY A O   1 
ATOM   2118 N  N   . CYS A 1 321 ? 14.12994  7.71354  -6.58312  1.000 41.38633  ? 303 CYS A N   1 
ATOM   2119 C  CA  . CYS A 1 321 ? 14.38064  9.08057  -6.15891  1.000 50.76694  ? 303 CYS A CA  1 
ATOM   2120 C  C   . CYS A 1 321 ? 15.52206  9.12739  -5.14895  1.000 51.33401  ? 303 CYS A C   1 
ATOM   2121 O  O   . CYS A 1 321 ? 15.88895  8.11981  -4.54036  1.000 53.93551  ? 303 CYS A O   1 
ATOM   2122 C  CB  . CYS A 1 321 ? 13.11916  9.68954  -5.53528  1.000 45.61380  ? 303 CYS A CB  1 
ATOM   2123 S  SG  . CYS A 1 321 ? 11.70479  9.81503  -6.65194  1.000 52.64423  ? 303 CYS A SG  1 
ATOM   2124 N  N   . THR A 1 322 ? 16.08266  10.31972 -4.97918  1.000 46.11699  ? 304 THR A N   1 
ATOM   2125 C  CA  . THR A 1 322 ? 16.96119  10.60177 -3.85682  1.000 54.38402  ? 304 THR A CA  1 
ATOM   2126 C  C   . THR A 1 322 ? 16.14661  11.22767 -2.72949  1.000 57.62390  ? 304 THR A C   1 
ATOM   2127 O  O   . THR A 1 322 ? 15.02287  11.69569 -2.93198  1.000 55.18260  ? 304 THR A O   1 
ATOM   2128 C  CB  . THR A 1 322 ? 18.10785  11.52544 -4.27310  1.000 50.44530  ? 304 THR A CB  1 
ATOM   2129 O  OG1 . THR A 1 322 ? 17.58268  12.80850 -4.63604  1.000 58.09844  ? 304 THR A OG1 1 
ATOM   2130 C  CG2 . THR A 1 322 ? 18.85170  10.93363 -5.45887  1.000 50.62730  ? 304 THR A CG2 1 
ATOM   2131 N  N   . VAL A 1 323 ? 16.72174  11.22705 -1.52879  1.000 51.43446  ? 305 VAL A N   1 
ATOM   2132 C  CA  . VAL A 1 323 ? 15.97636  11.57225 -0.32406  1.000 49.10211  ? 305 VAL A CA  1 
ATOM   2133 C  C   . VAL A 1 323 ? 16.87200  12.34668 0.63276   1.000 53.46007  ? 305 VAL A C   1 
ATOM   2134 O  O   . VAL A 1 323 ? 18.05500  12.02829 0.79527   1.000 55.05031  ? 305 VAL A O   1 
ATOM   2135 C  CB  . VAL A 1 323 ? 15.40269  10.30811 0.35496   1.000 49.21161  ? 305 VAL A CB  1 
ATOM   2136 C  CG1 . VAL A 1 323 ? 16.51789  9.31702  0.67350   1.000 47.25517  ? 305 VAL A CG1 1 
ATOM   2137 C  CG2 . VAL A 1 323 ? 14.62094  10.66941 1.60895   1.000 47.93945  ? 305 VAL A CG2 1 
ATOM   2138 N  N   . GLU A 1 324 ? 16.30328  13.37750 1.25408   1.000 52.73418  ? 306 GLU A N   1 
ATOM   2139 C  CA  . GLU A 1 324 ? 16.92865  14.08953 2.35949   1.000 56.61807  ? 306 GLU A CA  1 
ATOM   2140 C  C   . GLU A 1 324 ? 16.11133  13.82767 3.61580   1.000 61.12445  ? 306 GLU A C   1 
ATOM   2141 O  O   . GLU A 1 324 ? 14.89837  14.06959 3.63342   1.000 63.79993  ? 306 GLU A O   1 
ATOM   2142 C  CB  . GLU A 1 324 ? 17.01577  15.59170 2.08923   1.000 60.74304  ? 306 GLU A CB  1 
ATOM   2143 C  CG  . GLU A 1 324 ? 17.10333  16.42547 3.36672   1.000 68.13580  ? 306 GLU A CG  1 
ATOM   2144 C  CD  . GLU A 1 324 ? 17.47330  17.87342 3.11020   1.000 84.03067  ? 306 GLU A CD  1 
ATOM   2145 O  OE1 . GLU A 1 324 ? 18.62355  18.12705 2.69067   1.000 94.95019  ? 306 GLU A OE1 1 
ATOM   2146 O  OE2 . GLU A 1 324 ? 16.61801  18.75677 3.33843   1.000 80.91534  ? 306 GLU A OE2 1 
ATOM   2147 N  N   . ILE A 1 325 ? 16.77116  13.32902 4.65490   1.000 58.60394  ? 307 ILE A N   1 
ATOM   2148 C  CA  . ILE A 1 325 ? 16.14827  13.07599 5.94863   1.000 57.98432  ? 307 ILE A CA  1 
ATOM   2149 C  C   . ILE A 1 325 ? 16.77378  14.04723 6.94022   1.000 59.51809  ? 307 ILE A C   1 
ATOM   2150 O  O   . ILE A 1 325 ? 17.94102  13.89290 7.32185   1.000 66.09193  ? 307 ILE A O   1 
ATOM   2151 C  CB  . ILE A 1 325 ? 16.33219  11.61785 6.39090   1.000 59.62413  ? 307 ILE A CB  1 
ATOM   2152 C  CG1 . ILE A 1 325 ? 15.56488  10.67908 5.45843   1.000 52.92019  ? 307 ILE A CG1 1 
ATOM   2153 C  CG2 . ILE A 1 325 ? 15.87517  11.42260 7.82609   1.000 54.08594  ? 307 ILE A CG2 1 
ATOM   2154 C  CD1 . ILE A 1 325 ? 15.76561  9.21535  5.78104   1.000 52.96400  ? 307 ILE A CD1 1 
ATOM   2155 N  N   . LYS A 1 326 ? 16.01019  15.05811 7.34625   1.000 55.06996  ? 308 LYS A N   1 
ATOM   2156 C  CA  . LYS A 1 326 ? 16.50652  16.13369 8.20001   1.000 62.27074  ? 308 LYS A CA  1 
ATOM   2157 C  C   . LYS A 1 326 ? 15.79937  16.06723 9.54691   1.000 57.45289  ? 308 LYS A C   1 
ATOM   2158 O  O   . LYS A 1 326 ? 14.59812  16.34483 9.63974   1.000 58.25310  ? 308 LYS A O   1 
ATOM   2159 C  CB  . LYS A 1 326 ? 16.29686  17.49540 7.53967   1.000 61.39041  ? 308 LYS A CB  1 
ATOM   2160 C  CG  . LYS A 1 326 ? 16.79251  18.66897 8.36979   1.000 63.68911  ? 308 LYS A CG  1 
ATOM   2161 C  CD  . LYS A 1 326 ? 16.86710  19.94023 7.53986   1.000 72.26683  ? 308 LYS A CD  1 
ATOM   2162 N  N   . GLY A 1 327 ? 16.54667  15.70722 10.58766  1.000 64.08585  ? 309 GLY A N   1 
ATOM   2163 C  CA  . GLY A 1 327 ? 15.98374  15.67167 11.91996  1.000 56.26464  ? 309 GLY A CA  1 
ATOM   2164 C  C   . GLY A 1 327 ? 15.77046  17.06046 12.48862  1.000 56.36655  ? 309 GLY A C   1 
ATOM   2165 O  O   . GLY A 1 327 ? 16.33402  18.05255 12.02672  1.000 57.51194  ? 309 GLY A O   1 
ATOM   2166 N  N   . GLY A 1 328 ? 14.92466  17.12933 13.51164  1.000 59.86336  ? 310 GLY A N   1 
ATOM   2167 C  CA  . GLY A 1 328 ? 14.64488  18.40228 14.14363  1.000 63.41074  ? 310 GLY A CA  1 
ATOM   2168 C  C   . GLY A 1 328 ? 15.86562  18.98148 14.83112  1.000 62.89563  ? 310 GLY A C   1 
ATOM   2169 O  O   . GLY A 1 328 ? 16.84138  18.28934 15.12846  1.000 54.41148  ? 310 GLY A O   1 
ATOM   2170 N  N   . ALA A 1 329 ? 15.79963  20.29063 15.08584  1.000 69.80901  ? 311 ALA A N   1 
ATOM   2171 C  CA  . ALA A 1 329 ? 16.92723  20.97893 15.70839  1.000 79.90380  ? 311 ALA A CA  1 
ATOM   2172 C  C   . ALA A 1 329 ? 17.21017  20.43600 17.10439  1.000 72.85402  ? 311 ALA A C   1 
ATOM   2173 O  O   . ALA A 1 329 ? 18.37249  20.31570 17.50933  1.000 63.82438  ? 311 ALA A O   1 
ATOM   2174 C  CB  . ALA A 1 329 ? 16.65890  22.48305 15.75990  1.000 75.23442  ? 311 ALA A CB  1 
ATOM   2175 N  N   . HIS A 1 330 ? 16.16383  20.08931 17.84894  1.000 75.79582  ? 312 HIS A N   1 
ATOM   2176 C  CA  . HIS A 1 330 ? 16.30303  19.61709 19.21868  1.000 67.89355  ? 312 HIS A CA  1 
ATOM   2177 C  C   . HIS A 1 330 ? 15.42364  18.39608 19.43309  1.000 66.60461  ? 312 HIS A C   1 
ATOM   2178 O  O   . HIS A 1 330 ? 14.21882  18.44048 19.16629  1.000 75.30962  ? 312 HIS A O   1 
ATOM   2179 C  CB  . HIS A 1 330 ? 15.92187  20.71334 20.22079  1.000 77.29484  ? 312 HIS A CB  1 
ATOM   2180 C  CG  . HIS A 1 330 ? 16.82410  21.90623 20.18286  1.000 83.47966  ? 312 HIS A CG  1 
ATOM   2181 N  ND1 . HIS A 1 330 ? 18.19865  21.79920 20.17097  1.000 74.34427  ? 312 HIS A ND1 1 
ATOM   2182 C  CD2 . HIS A 1 330 ? 16.54831  23.23178 20.14809  1.000 80.87862  ? 312 HIS A CD2 1 
ATOM   2183 C  CE1 . HIS A 1 330 ? 18.73077  23.00768 20.13357  1.000 85.21253  ? 312 HIS A CE1 1 
ATOM   2184 N  NE2 . HIS A 1 330 ? 17.75124  23.89452 20.11807  1.000 94.33908  ? 312 HIS A NE2 1 
ATOM   2185 N  N   . ASP A 1 331 ? 16.02763  17.31153 19.90841  1.000 62.80729  ? 313 ASP A N   1 
ATOM   2186 C  CA  . ASP A 1 331 ? 15.26581  16.18188 20.41541  1.000 56.69713  ? 313 ASP A CA  1 
ATOM   2187 C  C   . ASP A 1 331 ? 14.79852  16.48253 21.83337  1.000 61.17254  ? 313 ASP A C   1 
ATOM   2188 O  O   . ASP A 1 331 ? 15.54972  17.03289 22.64302  1.000 52.09143  ? 313 ASP A O   1 
ATOM   2189 C  CB  . ASP A 1 331 ? 16.11786  14.91204 20.40545  1.000 62.96563  ? 313 ASP A CB  1 
ATOM   2190 C  CG  . ASP A 1 331 ? 16.08608  14.18971 19.06728  1.000 63.77526  ? 313 ASP A CG  1 
ATOM   2191 O  OD1 . ASP A 1 331 ? 15.38483  14.65602 18.14525  1.000 59.81137  ? 313 ASP A OD1 1 
ATOM   2192 O  OD2 . ASP A 1 331 ? 16.77047  13.15347 18.94037  1.000 64.60290  ? 313 ASP A OD2 1 
ATOM   2193 N  N   . PHE A 1 332 ? 13.54896  16.13401 22.12849  1.000 59.02847  ? 314 PHE A N   1 
ATOM   2194 C  CA  . PHE A 1 332 ? 13.00758  16.28002 23.47390  1.000 51.79758  ? 314 PHE A CA  1 
ATOM   2195 C  C   . PHE A 1 332 ? 13.24899  14.99715 24.26160  1.000 57.87326  ? 314 PHE A C   1 
ATOM   2196 O  O   . PHE A 1 332 ? 13.07546  13.89102 23.74031  1.000 55.29161  ? 314 PHE A O   1 
ATOM   2197 C  CB  . PHE A 1 332 ? 11.50943  16.59565 23.43470  1.000 59.64731  ? 314 PHE A CB  1 
ATOM   2198 C  CG  . PHE A 1 332 ? 11.18184  18.03684 23.10525  1.000 64.64807  ? 314 PHE A CG  1 
ATOM   2199 C  CD1 . PHE A 1 332 ? 12.11932  18.87288 22.51782  1.000 59.01657  ? 314 PHE A CD1 1 
ATOM   2200 C  CD2 . PHE A 1 332 ? 9.91327   18.54424 23.36858  1.000 71.47777  ? 314 PHE A CD2 1 
ATOM   2201 C  CE1 . PHE A 1 332 ? 11.80507  20.19076 22.21129  1.000 59.68929  ? 314 PHE A CE1 1 
ATOM   2202 C  CE2 . PHE A 1 332 ? 9.58981   19.86080 23.06415  1.000 65.91783  ? 314 PHE A CE2 1 
ATOM   2203 C  CZ  . PHE A 1 332 ? 10.53896  20.68436 22.48569  1.000 72.93510  ? 314 PHE A CZ  1 
ATOM   2204 N  N   . TYR A 1 333 ? 13.65390  15.14948 25.51815  1.000 54.23724  ? 315 TYR A N   1 
ATOM   2205 C  CA  . TYR A 1 333 ? 13.96016  14.00772 26.36664  1.000 54.01999  ? 315 TYR A CA  1 
ATOM   2206 C  C   . TYR A 1 333 ? 12.73610  13.60953 27.18067  1.000 54.15468  ? 315 TYR A C   1 
ATOM   2207 O  O   . TYR A 1 333 ? 11.86402  14.43408 27.46821  1.000 48.18603  ? 315 TYR A O   1 
ATOM   2208 C  CB  . TYR A 1 333 ? 15.11828  14.32523 27.31718  1.000 54.57796  ? 315 TYR A CB  1 
ATOM   2209 C  CG  . TYR A 1 333 ? 16.48603  14.40980 26.66871  1.000 63.98598  ? 315 TYR A CG  1 
ATOM   2210 C  CD1 . TYR A 1 333 ? 16.62823  14.44595 25.28786  1.000 68.35899  ? 315 TYR A CD1 1 
ATOM   2211 C  CD2 . TYR A 1 333 ? 17.63743  14.45596 27.44480  1.000 67.65467  ? 315 TYR A CD2 1 
ATOM   2212 C  CE1 . TYR A 1 333 ? 17.87505  14.52592 24.69879  1.000 64.70729  ? 315 TYR A CE1 1 
ATOM   2213 C  CE2 . TYR A 1 333 ? 18.89039  14.53465 26.86482  1.000 74.83447  ? 315 TYR A CE2 1 
ATOM   2214 C  CZ  . TYR A 1 333 ? 19.00267  14.57012 25.48983  1.000 77.63221  ? 315 TYR A CZ  1 
ATOM   2215 O  OH  . TYR A 1 333 ? 20.24499  14.64785 24.90045  1.000 80.74421  ? 315 TYR A OH  1 
ATOM   2216 N  N   . ASN A 1 334 ? 12.68026  12.33312 27.55582  1.000 46.48295  ? 316 ASN A N   1 
ATOM   2217 C  CA  . ASN A 1 334 ? 11.67465  11.89947 28.51117  1.000 50.37572  ? 316 ASN A CA  1 
ATOM   2218 C  C   . ASN A 1 334 ? 11.96715  12.50497 29.88348  1.000 52.77035  ? 316 ASN A C   1 
ATOM   2219 O  O   . ASN A 1 334 ? 13.09906  12.88084 30.19632  1.000 51.31783  ? 316 ASN A O   1 
ATOM   2220 C  CB  . ASN A 1 334 ? 11.63339  10.37292 28.59889  1.000 49.71033  ? 316 ASN A CB  1 
ATOM   2221 C  CG  . ASN A 1 334 ? 12.97218  9.77518  28.97925  1.000 59.29590  ? 316 ASN A CG  1 
ATOM   2222 O  OD1 . ASN A 1 334 ? 13.94430  9.87588  28.23030  1.000 54.61172  ? 316 ASN A OD1 1 
ATOM   2223 N  ND2 . ASN A 1 334 ? 13.03010  9.14642  30.15057  1.000 59.22956  ? 316 ASN A ND2 1 
ATOM   2224 N  N   . VAL A 1 335 ? 10.92745  12.60382 30.70593  1.000 55.24390  ? 317 VAL A N   1 
ATOM   2225 C  CA  . VAL A 1 335 ? 11.05864  13.22749 32.01838  1.000 54.33129  ? 317 VAL A CA  1 
ATOM   2226 C  C   . VAL A 1 335 ? 11.56513  12.18963 33.01029  1.000 59.59954  ? 317 VAL A C   1 
ATOM   2227 O  O   . VAL A 1 335 ? 10.96075  11.12480 33.17505  1.000 68.45511  ? 317 VAL A O   1 
ATOM   2228 C  CB  . VAL A 1 335 ? 9.72833   13.83458 32.48407  1.000 53.69025  ? 317 VAL A CB  1 
ATOM   2229 C  CG1 . VAL A 1 335 ? 9.84977   14.33212 33.92341  1.000 45.72872  ? 317 VAL A CG1 1 
ATOM   2230 C  CG2 . VAL A 1 335 ? 9.31074   14.96953 31.56091  1.000 46.31723  ? 317 VAL A CG2 1 
ATOM   2231 N  N   . LEU A 1 336 ? 12.67387  12.49827 33.67091  1.000 61.09232  ? 318 LEU A N   1 
ATOM   2232 C  CA  . LEU A 1 336 ? 13.21169  11.61185 34.69325  1.000 66.48444  ? 318 LEU A CA  1 
ATOM   2233 C  C   . LEU A 1 336 ? 12.49493  11.85002 36.01373  1.000 66.76395  ? 318 LEU A C   1 
ATOM   2234 O  O   . LEU A 1 336 ? 12.49335  12.98292 36.50755  1.000 74.07044  ? 318 LEU A O   1 
ATOM   2235 C  CB  . LEU A 1 336 ? 14.70470  11.83904 34.87674  1.000 72.79755  ? 318 LEU A CB  1 
ATOM   2236 C  CG  . LEU A 1 336 ? 15.62378  11.35321 33.76009  1.000 74.82065  ? 318 LEU A CG  1 
ATOM   2237 C  CD1 . LEU A 1 336 ? 17.07958  11.53468 34.16426  1.000 76.34010  ? 318 LEU A CD1 1 
ATOM   2238 C  CD2 . LEU A 1 336 ? 15.32999  9.90361  33.41313  1.000 80.55347  ? 318 LEU A CD2 1 
ATOM   2239 N  N   . PRO A 1 337 ? 11.89285  10.83191 36.61739  1.000 74.60810  ? 319 PRO A N   1 
ATOM   2240 C  CA  . PRO A 1 337 ? 11.27420  11.01228 37.93216  1.000 74.41190  ? 319 PRO A CA  1 
ATOM   2241 C  C   . PRO A 1 337 ? 12.31594  11.02721 39.04256  1.000 69.78751  ? 319 PRO A C   1 
ATOM   2242 O  O   . PRO A 1 337 ? 13.45901  10.59931 38.87226  1.000 74.89609  ? 319 PRO A O   1 
ATOM   2243 C  CB  . PRO A 1 337 ? 10.35410  9.79498  38.05697  1.000 73.06039  ? 319 PRO A CB  1 
ATOM   2244 C  CG  . PRO A 1 337 ? 11.03465  8.74451  37.24076  1.000 75.94566  ? 319 PRO A CG  1 
ATOM   2245 C  CD  . PRO A 1 337 ? 11.71924  9.46257  36.10133  1.000 63.73156  ? 319 PRO A CD  1 
ATOM   2246 N  N   . ASN A 1 338 ? 11.89378  11.53912 40.19951  1.000 58.38499  ? 320 ASN A N   1 
ATOM   2247 C  CA  . ASN A 1 338 ? 12.73821  11.58980 41.39077  1.000 56.78220  ? 320 ASN A CA  1 
ATOM   2248 C  C   . ASN A 1 338 ? 11.87605  11.17593 42.57960  1.000 68.28177  ? 320 ASN A C   1 
ATOM   2249 O  O   . ASN A 1 338 ? 11.06457  11.96851 43.06925  1.000 65.57634  ? 320 ASN A O   1 
ATOM   2250 C  CB  . ASN A 1 338 ? 13.33999  12.97622 41.59212  1.000 60.84307  ? 320 ASN A CB  1 
ATOM   2251 C  CG  . ASN A 1 338 ? 14.36064  13.01083 42.71942  1.000 65.45209  ? 320 ASN A CG  1 
ATOM   2252 O  OD1 . ASN A 1 338 ? 13.99975  13.11152 43.88989  1.000 65.54950  ? 320 ASN A OD1 1 
ATOM   2253 N  ND2 . ASN A 1 338 ? 15.64202  12.92674 42.36939  1.000 59.39174  ? 320 ASN A ND2 1 
ATOM   2254 N  N   . LYS A 1 339 ? 12.07192  9.93715  43.04554  1.000 70.89678  ? 321 LYS A N   1 
ATOM   2255 C  CA  . LYS A 1 339 ? 11.19132  9.36361  44.06175  1.000 71.35271  ? 321 LYS A CA  1 
ATOM   2256 C  C   . LYS A 1 339 ? 11.15791  10.21351 45.32556  1.000 72.34861  ? 321 LYS A C   1 
ATOM   2257 O  O   . LYS A 1 339 ? 10.08342  10.45372 45.88947  1.000 73.92578  ? 321 LYS A O   1 
ATOM   2258 C  CB  . LYS A 1 339 ? 11.63145  7.93680  44.39094  1.000 65.49409  ? 321 LYS A CB  1 
ATOM   2259 N  N   . SER A 1 340 ? 12.32276  10.67471 45.78937  1.000 65.86522  ? 322 SER A N   1 
ATOM   2260 C  CA  . SER A 1 340 ? 12.36908  11.44975 47.02646  1.000 66.84095  ? 322 SER A CA  1 
ATOM   2261 C  C   . SER A 1 340 ? 11.59293  12.75328 46.88562  1.000 67.81312  ? 322 SER A C   1 
ATOM   2262 O  O   . SER A 1 340 ? 10.77652  13.10141 47.74719  1.000 60.46886  ? 322 SER A O   1 
ATOM   2263 C  CB  . SER A 1 340 ? 13.82100  11.72572 47.42165  1.000 67.13625  ? 322 SER A CB  1 
ATOM   2264 O  OG  . SER A 1 340 ? 14.64048  10.59288 47.18759  1.000 68.04051  ? 322 SER A OG  1 
ATOM   2265 N  N   . LEU A 1 341 ? 11.82907  13.48396 45.79388  1.000 61.80040  ? 323 LEU A N   1 
ATOM   2266 C  CA  . LEU A 1 341 ? 11.13902  14.75318 45.58971  1.000 62.83779  ? 323 LEU A CA  1 
ATOM   2267 C  C   . LEU A 1 341 ? 9.63826   14.54981 45.41763  1.000 64.98173  ? 323 LEU A C   1 
ATOM   2268 O  O   . LEU A 1 341 ? 8.83630   15.31243 45.97045  1.000 62.93023  ? 323 LEU A O   1 
ATOM   2269 C  CB  . LEU A 1 341 ? 11.72963  15.47483 44.38008  1.000 64.18918  ? 323 LEU A CB  1 
ATOM   2270 C  CG  . LEU A 1 341 ? 11.54309  16.98935 44.29328  1.000 62.36274  ? 323 LEU A CG  1 
ATOM   2271 C  CD1 . LEU A 1 341 ? 11.80330  17.65992 45.63087  1.000 50.59694  ? 323 LEU A CD1 1 
ATOM   2272 C  CD2 . LEU A 1 341 ? 12.45499  17.55090 43.21586  1.000 61.62603  ? 323 LEU A CD2 1 
ATOM   2273 N  N   . TRP A 1 342 ? 9.23847   13.52177 44.66450  1.000 66.00529  ? 324 TRP A N   1 
ATOM   2274 C  CA  . TRP A 1 342 ? 7.81597   13.28331 44.43707  1.000 66.91200  ? 324 TRP A CA  1 
ATOM   2275 C  C   . TRP A 1 342 ? 7.10971   12.85141 45.71838  1.000 68.46895  ? 324 TRP A C   1 
ATOM   2276 O  O   . TRP A 1 342 ? 5.98788   13.29401 45.99414  1.000 67.35729  ? 324 TRP A O   1 
ATOM   2277 C  CB  . TRP A 1 342 ? 7.62975   12.23662 43.33838  1.000 73.67571  ? 324 TRP A CB  1 
ATOM   2278 N  N   . LYS A 1 343 ? 7.74785   11.98969 46.51513  1.000 68.47605  ? 325 LYS A N   1 
ATOM   2279 C  CA  . LYS A 1 343 ? 7.13466   11.55566 47.76598  1.000 68.30391  ? 325 LYS A CA  1 
ATOM   2280 C  C   . LYS A 1 343 ? 7.00692   12.71465 48.74607  1.000 69.31401  ? 325 LYS A C   1 
ATOM   2281 O  O   . LYS A 1 343 ? 6.02775   12.79571 49.49724  1.000 79.12457  ? 325 LYS A O   1 
ATOM   2282 C  CB  . LYS A 1 343 ? 7.94240   10.41242 48.38207  1.000 69.32288  ? 325 LYS A CB  1 
ATOM   2283 N  N   . ALA A 1 344 ? 7.98461   13.62271 48.75396  1.000 63.89615  ? 326 ALA A N   1 
ATOM   2284 C  CA  . ALA A 1 344 ? 7.87928   14.80048 49.60689  1.000 68.43071  ? 326 ALA A CA  1 
ATOM   2285 C  C   . ALA A 1 344 ? 6.80146   15.75004 49.10505  1.000 65.23239  ? 326 ALA A C   1 
ATOM   2286 O  O   . ALA A 1 344 ? 6.11799   16.39338 49.91034  1.000 63.55002  ? 326 ALA A O   1 
ATOM   2287 C  CB  . ALA A 1 344 ? 9.22845   15.51655 49.69145  1.000 60.57039  ? 326 ALA A CB  1 
ATOM   2288 N  N   . TYR A 1 345 ? 6.62711   15.84206 47.78437  1.000 68.56846  ? 327 TYR A N   1 
ATOM   2289 C  CA  . TYR A 1 345 ? 5.59134   16.71152 47.23597  1.000 67.54360  ? 327 TYR A CA  1 
ATOM   2290 C  C   . TYR A 1 345 ? 4.19762   16.17905 47.54871  1.000 65.37940  ? 327 TYR A C   1 
ATOM   2291 O  O   . TYR A 1 345 ? 3.29588   16.95256 47.89336  1.000 64.59967  ? 327 TYR A O   1 
ATOM   2292 C  CB  . TYR A 1 345 ? 5.78133   16.87096 45.72625  1.000 63.39918  ? 327 TYR A CB  1 
ATOM   2293 C  CG  . TYR A 1 345 ? 4.64268   17.59525 45.04128  1.000 63.62690  ? 327 TYR A CG  1 
ATOM   2294 C  CD1 . TYR A 1 345 ? 4.59087   18.98395 45.01725  1.000 56.99106  ? 327 TYR A CD1 1 
ATOM   2295 C  CD2 . TYR A 1 345 ? 3.61617   16.89016 44.42384  1.000 60.10009  ? 327 TYR A CD2 1 
ATOM   2296 C  CE1 . TYR A 1 345 ? 3.55225   19.64976 44.39223  1.000 52.08818  ? 327 TYR A CE1 1 
ATOM   2297 C  CE2 . TYR A 1 345 ? 2.57258   17.54716 43.80125  1.000 64.23493  ? 327 TYR A CE2 1 
ATOM   2298 C  CZ  . TYR A 1 345 ? 2.54551   18.92595 43.78680  1.000 60.07466  ? 327 TYR A CZ  1 
ATOM   2299 O  OH  . TYR A 1 345 ? 1.50414   19.57892 43.16508  1.000 62.33761  ? 327 TYR A OH  1 
ATOM   2300 N  N   A MET A 1 346 ? 3.99909   14.86371 47.43470  0.567 67.73990  ? 328 MET A N   1 
ATOM   2301 N  N   B MET A 1 346 ? 4.00309   14.86171 47.43311  0.433 67.78225  ? 328 MET A N   1 
ATOM   2302 C  CA  A MET A 1 346 ? 2.68042   14.29816 47.70210  0.567 70.21547  ? 328 MET A CA  1 
ATOM   2303 C  CA  B MET A 1 346 ? 2.69296   14.27736 47.70683  0.433 70.23302  ? 328 MET A CA  1 
ATOM   2304 C  C   A MET A 1 346 ? 2.28598   14.45067 49.16565  0.567 71.82119  ? 328 MET A C   1 
ATOM   2305 C  C   B MET A 1 346 ? 2.29109   14.47469 49.16281  0.433 71.81580  ? 328 MET A C   1 
ATOM   2306 O  O   A MET A 1 346 ? 1.10227   14.63885 49.46834  0.567 73.36847  ? 328 MET A O   1 
ATOM   2307 O  O   B MET A 1 346 ? 1.11517   14.71275 49.46283  0.433 73.34336  ? 328 MET A O   1 
ATOM   2308 C  CB  A MET A 1 346 ? 2.64351   12.82699 47.28763  0.567 72.05906  ? 328 MET A CB  1 
ATOM   2309 C  CB  B MET A 1 346 ? 2.69358   12.78979 47.35012  0.433 72.07826  ? 328 MET A CB  1 
ATOM   2310 C  CG  A MET A 1 346 ? 2.32920   12.61599 45.81512  0.567 74.31739  ? 328 MET A CG  1 
ATOM   2311 C  CG  B MET A 1 346 ? 2.81025   12.50565 45.86231  0.433 74.66193  ? 328 MET A CG  1 
ATOM   2312 S  SD  A MET A 1 346 ? 2.06285   10.88804 45.37727  0.567 81.65952  ? 328 MET A SD  1 
ATOM   2313 S  SD  B MET A 1 346 ? 2.67032   10.75323 45.45483  0.433 81.64676  ? 328 MET A SD  1 
ATOM   2314 C  CE  A MET A 1 346 ? 0.49536   10.58053 46.18369  0.567 84.27844  ? 328 MET A CE  1 
ATOM   2315 C  CE  B MET A 1 346 ? 3.80912   10.03624 46.63667  0.433 76.06397  ? 328 MET A CE  1 
ATOM   2316 N  N   . GLU A 1 347 ? 3.25516   14.38151 50.08270  1.000 72.11723  ? 329 GLU A N   1 
ATOM   2317 C  CA  . GLU A 1 347 ? 2.94474   14.55443 51.49718  1.000 64.27534  ? 329 GLU A CA  1 
ATOM   2318 C  C   . GLU A 1 347 ? 2.48079   15.97402 51.80243  1.000 69.63395  ? 329 GLU A C   1 
ATOM   2319 O  O   . GLU A 1 347 ? 1.65978   16.17465 52.70432  1.000 74.53072  ? 329 GLU A O   1 
ATOM   2320 C  CB  . GLU A 1 347 ? 4.16215   14.19694 52.35123  1.000 70.90251  ? 329 GLU A CB  1 
ATOM   2321 N  N   . ASN A 1 348 ? 2.98681   16.96888 51.06997  1.000 69.51977  ? 330 ASN A N   1 
ATOM   2322 C  CA  . ASN A 1 348 ? 2.50077   18.33162 51.25887  1.000 63.00928  ? 330 ASN A CA  1 
ATOM   2323 C  C   . ASN A 1 348 ? 1.11394   18.50288 50.64966  1.000 71.93331  ? 330 ASN A C   1 
ATOM   2324 O  O   . ASN A 1 348 ? 0.20375   19.03762 51.29359  1.000 60.44449  ? 330 ASN A O   1 
ATOM   2325 C  CB  . ASN A 1 348 ? 3.48162   19.33392 50.65544  1.000 58.62083  ? 330 ASN A CB  1 
ATOM   2326 C  CG  . ASN A 1 348 ? 4.76242   19.45104 51.45821  1.000 67.47546  ? 330 ASN A CG  1 
ATOM   2327 O  OD1 . ASN A 1 348 ? 4.74349   19.85296 52.62088  1.000 66.06360  ? 330 ASN A OD1 1 
ATOM   2328 N  ND2 . ASN A 1 348 ? 5.88652   19.10293 50.83757  1.000 62.02611  ? 330 ASN A ND2 1 
ATOM   2329 N  N   . GLY A 1 349 ? 0.93031   18.03595 49.41248  1.000 62.22330  ? 331 GLY A N   1 
ATOM   2330 C  CA  . GLY A 1 349 ? -0.35937  18.19008 48.75591  1.000 71.15942  ? 331 GLY A CA  1 
ATOM   2331 C  C   . GLY A 1 349 ? -1.49759  17.55452 49.53207  1.000 75.18449  ? 331 GLY A C   1 
ATOM   2332 O  O   . GLY A 1 349 ? -2.59974  18.10540 49.59813  1.000 72.56173  ? 331 GLY A O   1 
ATOM   2333 N  N   . ARG A 1 350 ? -1.24389  16.39120 50.13949  1.000 75.29698  ? 332 ARG A N   1 
ATOM   2334 C  CA  . ARG A 1 350 ? -2.26467  15.74737 50.96024  1.000 78.86191  ? 332 ARG A CA  1 
ATOM   2335 C  C   . ARG A 1 350 ? -2.69103  16.63737 52.11900  1.000 75.09376  ? 332 ARG A C   1 
ATOM   2336 O  O   . ARG A 1 350 ? -3.86078  16.61884 52.51852  1.000 81.29728  ? 332 ARG A O   1 
ATOM   2337 C  CB  . ARG A 1 350 ? -1.75475  14.40270 51.48210  1.000 69.68017  ? 332 ARG A CB  1 
ATOM   2338 C  CG  . ARG A 1 350 ? -1.92100  13.25336 50.49522  1.000 79.80784  ? 332 ARG A CG  1 
ATOM   2339 C  CD  . ARG A 1 350 ? -0.87668  12.16868 50.72220  1.000 87.48159  ? 332 ARG A CD  1 
ATOM   2340 N  NE  . ARG A 1 350 ? -1.09258  11.00934 49.86401  1.000 100.98758 ? 332 ARG A NE  1 
ATOM   2341 C  CZ  . ARG A 1 350 ? -0.22752  10.01465 49.71699  1.000 104.83407 ? 332 ARG A CZ  1 
ATOM   2342 N  NH1 . ARG A 1 350 ? 0.92639   10.00115 50.36497  1.000 101.51911 ? 332 ARG A NH1 1 
ATOM   2343 N  NH2 . ARG A 1 350 ? -0.52630  9.00982  48.89719  1.000 96.27616  ? 332 ARG A NH2 1 
ATOM   2344 N  N   . LYS A 1 351 ? -1.76576  17.42600 52.66674  1.000 70.06211  ? 333 LYS A N   1 
ATOM   2345 C  CA  . LYS A 1 351 ? -2.14018  18.36453 53.71747  1.000 74.46960  ? 333 LYS A CA  1 
ATOM   2346 C  C   . LYS A 1 351 ? -2.97661  19.51330 53.16729  1.000 79.52820  ? 333 LYS A C   1 
ATOM   2347 O  O   . LYS A 1 351 ? -3.87329  20.00822 53.86040  1.000 79.00695  ? 333 LYS A O   1 
ATOM   2348 C  CB  . LYS A 1 351 ? -0.89087  18.90223 54.41640  1.000 80.69680  ? 333 LYS A CB  1 
ATOM   2349 C  CG  . LYS A 1 351 ? -0.12876  17.86304 55.22362  1.000 78.52094  ? 333 LYS A CG  1 
ATOM   2350 C  CD  . LYS A 1 351 ? 0.73300   18.51073 56.29529  1.000 85.28079  ? 333 LYS A CD  1 
ATOM   2351 C  CE  . LYS A 1 351 ? 2.13022   17.90705 56.31185  1.000 90.89981  ? 333 LYS A CE  1 
ATOM   2352 N  NZ  . LYS A 1 351 ? 2.15936   16.59610 57.02202  1.000 96.39260  ? 333 LYS A NZ  1 
ATOM   2353 N  N   . LEU A 1 352 ? -2.70078  19.95336 51.93353  1.000 78.52897  ? 334 LEU A N   1 
ATOM   2354 C  CA  . LEU A 1 352 ? -3.50465  21.00359 51.31850  1.000 75.59386  ? 334 LEU A CA  1 
ATOM   2355 C  C   . LEU A 1 352 ? -4.87471  20.51592 50.87833  1.000 72.39753  ? 334 LEU A C   1 
ATOM   2356 O  O   . LEU A 1 352 ? -5.72789  21.34720 50.55145  1.000 74.39839  ? 334 LEU A O   1 
ATOM   2357 C  CB  . LEU A 1 352 ? -2.79296  21.61815 50.10806  1.000 61.67556  ? 334 LEU A CB  1 
ATOM   2358 C  CG  . LEU A 1 352 ? -1.65686  22.62181 50.33321  1.000 72.17106  ? 334 LEU A CG  1 
ATOM   2359 C  CD1 . LEU A 1 352 ? -2.04652  23.66590 51.37687  1.000 61.29225  ? 334 LEU A CD1 1 
ATOM   2360 C  CD2 . LEU A 1 352 ? -0.34928  21.95191 50.69006  1.000 70.09357  ? 334 LEU A CD2 1 
ATOM   2361 N  N   . GLY A 1 353 ? -5.10355  19.20749 50.85983  1.000 77.17587  ? 335 GLY A N   1 
ATOM   2362 C  CA  . GLY A 1 353 ? -6.36600  18.65208 50.42696  1.000 78.60489  ? 335 GLY A CA  1 
ATOM   2363 C  C   . GLY A 1 353 ? -6.37587  18.10357 49.01910  1.000 86.50560  ? 335 GLY A C   1 
ATOM   2364 O  O   . GLY A 1 353 ? -7.45787  17.81997 48.49367  1.000 89.13335  ? 335 GLY A O   1 
ATOM   2365 N  N   . ILE A 1 354 ? -5.21440  17.94575 48.39261  1.000 78.76795  ? 336 ILE A N   1 
ATOM   2366 C  CA  . ILE A 1 354 ? -5.14403  17.43686 47.02747  1.000 82.37776  ? 336 ILE A CA  1 
ATOM   2367 C  C   . ILE A 1 354 ? -5.20965  15.91661 47.06054  1.000 78.38014  ? 336 ILE A C   1 
ATOM   2368 O  O   . ILE A 1 354 ? -4.46427  15.26732 47.80327  1.000 86.07094  ? 336 ILE A O   1 
ATOM   2369 C  CB  . ILE A 1 354 ? -3.86015  17.91745 46.33075  1.000 73.74620  ? 336 ILE A CB  1 
ATOM   2370 C  CG1 . ILE A 1 354 ? -3.86984  19.43724 46.17243  1.000 67.82184  ? 336 ILE A CG1 1 
ATOM   2371 C  CG2 . ILE A 1 354 ? -3.71150  17.25213 44.96961  1.000 74.31052  ? 336 ILE A CG2 1 
ATOM   2372 C  CD1 . ILE A 1 354 ? -2.49262  20.04688 46.08389  1.000 67.80611  ? 336 ILE A CD1 1 
ATOM   2373 N  N   . GLU A 1 355 ? -6.09910  15.34413 46.25577  1.000 74.37960  ? 337 GLU A N   1 
ATOM   2374 C  CA  . GLU A 1 355 ? -6.20188  13.89910 46.10918  1.000 79.45333  ? 337 GLU A CA  1 
ATOM   2375 C  C   . GLU A 1 355 ? -5.54491  13.48213 44.80027  1.000 81.66415  ? 337 GLU A C   1 
ATOM   2376 O  O   . GLU A 1 355 ? -5.83571  14.05398 43.74432  1.000 80.18333  ? 337 GLU A O   1 
ATOM   2377 C  CB  . GLU A 1 355 ? -7.66172  13.44288 46.14578  1.000 71.69149  ? 337 GLU A CB  1 
ATOM   2378 N  N   . PHE A 1 356 ? -4.66272  12.49151 44.87458  1.000 83.16381  ? 338 PHE A N   1 
ATOM   2379 C  CA  . PHE A 1 356 ? -3.90062  12.02344 43.72749  1.000 80.65276  ? 338 PHE A CA  1 
ATOM   2380 C  C   . PHE A 1 356 ? -4.47240  10.71110 43.19852  1.000 98.01541  ? 338 PHE A C   1 
ATOM   2381 O  O   . PHE A 1 356 ? -5.29299  10.05149 43.84120  1.000 105.79872 ? 338 PHE A O   1 
ATOM   2382 C  CB  . PHE A 1 356 ? -2.42497  11.85180 44.10166  1.000 82.76620  ? 338 PHE A CB  1 
ATOM   2383 C  CG  . PHE A 1 356 ? -1.78601  13.10106 44.64111  1.000 84.64232  ? 338 PHE A CG  1 
ATOM   2384 C  CD1 . PHE A 1 356 ? -1.84785  13.40119 45.99274  1.000 77.67682  ? 338 PHE A CD1 1 
ATOM   2385 C  CD2 . PHE A 1 356 ? -1.11845  13.97352 43.79675  1.000 90.27356  ? 338 PHE A CD2 1 
ATOM   2386 C  CE1 . PHE A 1 356 ? -1.26117  14.54918 46.49204  1.000 77.75303  ? 338 PHE A CE1 1 
ATOM   2387 C  CE2 . PHE A 1 356 ? -0.52711  15.12387 44.29096  1.000 84.88335  ? 338 PHE A CE2 1 
ATOM   2388 C  CZ  . PHE A 1 356 ? -0.59858  15.41105 45.64061  1.000 75.77067  ? 338 PHE A CZ  1 
ATOM   2389 N  N   . ILE A 1 357 ? -4.02133  10.33627 42.00475  1.000 94.86429  ? 339 ILE A N   1 
ATOM   2390 C  CA  . ILE A 1 357 ? -4.46161  9.09943  41.37231  1.000 94.34396  ? 339 ILE A CA  1 
ATOM   2391 C  C   . ILE A 1 357 ? -3.58189  7.93784  41.82417  1.000 98.61615  ? 339 ILE A C   1 
ATOM   2392 O  O   . ILE A 1 357 ? -3.90588  6.77185  41.59400  1.000 103.65622 ? 339 ILE A O   1 
ATOM   2393 C  CB  . ILE A 1 357 ? -4.45718  9.22444  39.83710  1.000 93.49105  ? 339 ILE A CB  1 
ATOM   2394 C  CG1 . ILE A 1 357 ? -3.12690  9.79941  39.34951  1.000 93.40974  ? 339 ILE A CG1 1 
ATOM   2395 C  CG2 . ILE A 1 357 ? -5.61257  10.09649 39.37043  1.000 96.88910  ? 339 ILE A CG2 1 
ATOM   2396 N  N   . PRO A 1 366 ? 0.29582   12.52378 29.34513  1.000 105.47220 ? 348 PRO A N   1 
ATOM   2397 C  CA  . PRO A 1 366 ? -0.35646  13.82901 29.49702  1.000 101.69534 ? 348 PRO A CA  1 
ATOM   2398 C  C   . PRO A 1 366 ? -0.55921  14.53043 28.16125  1.000 110.07109 ? 348 PRO A C   1 
ATOM   2399 O  O   . PRO A 1 366 ? -0.99790  13.89432 27.20348  1.000 123.50966 ? 348 PRO A O   1 
ATOM   2400 C  CB  . PRO A 1 366 ? 0.62174   14.61762 30.37980  1.000 98.45114  ? 348 PRO A CB  1 
ATOM   2401 C  CG  . PRO A 1 366 ? 1.68147   13.62826 30.80878  1.000 100.16369 ? 348 PRO A CG  1 
ATOM   2402 C  CD  . PRO A 1 366 ? 1.70442   12.57538 29.75923  1.000 95.59126  ? 348 PRO A CD  1 
ATOM   2403 N  N   . SER A 1 367 ? -0.24324  15.82685 28.10283  1.000 104.57156 ? 349 SER A N   1 
ATOM   2404 C  CA  . SER A 1 367 ? -0.39369  16.56448 26.85217  1.000 106.49042 ? 349 SER A CA  1 
ATOM   2405 C  C   . SER A 1 367 ? 0.45161   15.94857 25.74091  1.000 111.34351 ? 349 SER A C   1 
ATOM   2406 O  O   . SER A 1 367 ? -0.00606  15.83105 24.59823  1.000 107.97539 ? 349 SER A O   1 
ATOM   2407 C  CB  . SER A 1 367 ? -0.03005  18.03454 27.06277  1.000 81.47178  ? 349 SER A CB  1 
ATOM   2408 N  N   . GLY A 1 368 ? 1.68021   15.53671 26.05669  1.000 104.67788 ? 350 GLY A N   1 
ATOM   2409 C  CA  . GLY A 1 368 ? 2.52578   14.87289 25.08035  1.000 96.36230  ? 350 GLY A CA  1 
ATOM   2410 C  C   . GLY A 1 368 ? 3.97051   14.70716 25.51202  1.000 92.57673  ? 350 GLY A C   1 
ATOM   2411 O  O   . GLY A 1 368 ? 4.29292   13.82352 26.31262  1.000 88.74820  ? 350 GLY A O   1 
ATOM   2412 N  N   A SER A 1 369 ? 4.85222   15.54872 24.97448  0.369 81.89021  ? 351 SER A N   1 
ATOM   2413 N  N   B SER A 1 369 ? 4.85209   15.54524 24.97217  0.631 81.94079  ? 351 SER A N   1 
ATOM   2414 C  CA  A SER A 1 369 ? 6.26059   15.56740 25.34191  0.369 68.56571  ? 351 SER A CA  1 
ATOM   2415 C  CA  B SER A 1 369 ? 6.25824   15.56932 25.34442  0.631 68.40180  ? 351 SER A CA  1 
ATOM   2416 C  C   A SER A 1 369 ? 6.69105   17.01079 25.55215  0.369 64.38557  ? 351 SER A C   1 
ATOM   2417 C  C   B SER A 1 369 ? 6.67616   17.01374 25.56554  0.631 64.29984  ? 351 SER A C   1 
ATOM   2418 O  O   A SER A 1 369 ? 6.25869   17.90715 24.82112  0.369 67.76068  ? 351 SER A O   1 
ATOM   2419 O  O   B SER A 1 369 ? 6.22247   17.91362 24.85202  0.631 67.80233  ? 351 SER A O   1 
ATOM   2420 C  CB  A SER A 1 369 ? 7.13479   14.89839 24.26845  0.369 70.06368  ? 351 SER A CB  1 
ATOM   2421 C  CB  B SER A 1 369 ? 7.13836   14.92007 24.26836  0.631 70.04517  ? 351 SER A CB  1 
ATOM   2422 O  OG  A SER A 1 369 ? 7.67870   15.85130 23.37105  0.369 65.56757  ? 351 SER A OG  1 
ATOM   2423 O  OG  B SER A 1 369 ? 6.85532   13.53722 24.14647  0.631 74.52033  ? 351 SER A OG  1 
ATOM   2424 N  N   . THR A 1 370 ? 7.54030   17.23311 26.55333  1.000 57.32360  ? 352 THR A N   1 
ATOM   2425 C  CA  . THR A 1 370 ? 7.93673   18.57576 26.95229  1.000 53.97408  ? 352 THR A CA  1 
ATOM   2426 C  C   . THR A 1 370 ? 9.44978   18.68554 27.06606  1.000 52.07997  ? 352 THR A C   1 
ATOM   2427 O  O   . THR A 1 370 ? 10.13879  17.72021 27.40779  1.000 47.04511  ? 352 THR A O   1 
ATOM   2428 C  CB  . THR A 1 370 ? 7.29864   18.97037 28.29338  1.000 47.21184  ? 352 THR A CB  1 
ATOM   2429 O  OG1 . THR A 1 370 ? 7.86902   20.20150 28.74989  1.000 46.98751  ? 352 THR A OG1 1 
ATOM   2430 C  CG2 . THR A 1 370 ? 7.53331   17.89128 29.33626  1.000 42.77681  ? 352 THR A CG2 1 
ATOM   2431 N  N   . ASP A 1 371 ? 9.95979   19.88903 26.79323  1.000 49.35531  ? 353 ASP A N   1 
ATOM   2432 C  CA  . ASP A 1 371 ? 11.38489  20.14702 26.94073  1.000 45.17684  ? 353 ASP A CA  1 
ATOM   2433 C  C   . ASP A 1 371 ? 11.83523  20.15323 28.39965  1.000 53.00133  ? 353 ASP A C   1 
ATOM   2434 O  O   . ASP A 1 371 ? 13.04105  20.24445 28.65476  1.000 46.51422  ? 353 ASP A O   1 
ATOM   2435 C  CB  . ASP A 1 371 ? 11.76057  21.47085 26.26369  1.000 41.80222  ? 353 ASP A CB  1 
ATOM   2436 C  CG  . ASP A 1 371 ? 10.98008  22.65775 26.80723  1.000 46.25472  ? 353 ASP A CG  1 
ATOM   2437 O  OD1 . ASP A 1 371 ? 10.05765  22.45139 27.62687  1.000 41.22868  ? 353 ASP A OD1 1 
ATOM   2438 O  OD2 . ASP A 1 371 ? 11.29444  23.80393 26.41306  1.000 40.55701  ? 353 ASP A OD2 1 
ATOM   2439 N  N   . PHE A 1 372 ? 10.91083  20.05325 29.36032  1.000 37.18194  ? 354 PHE A N   1 
ATOM   2440 C  CA  . PHE A 1 372 ? 11.32452  19.85083 30.74459  1.000 49.72242  ? 354 PHE A CA  1 
ATOM   2441 C  C   . PHE A 1 372 ? 12.06147  18.52978 30.92703  1.000 43.73723  ? 354 PHE A C   1 
ATOM   2442 O  O   . PHE A 1 372 ? 12.85097  18.39732 31.87015  1.000 47.11725  ? 354 PHE A O   1 
ATOM   2443 C  CB  . PHE A 1 372 ? 10.11653  19.90302 31.68510  1.000 46.10808  ? 354 PHE A CB  1 
ATOM   2444 C  CG  . PHE A 1 372 ? 10.47511  19.75206 33.14406  1.000 43.54651  ? 354 PHE A CG  1 
ATOM   2445 C  CD1 . PHE A 1 372 ? 10.27249  18.54738 33.80238  1.000 39.32267  ? 354 PHE A CD1 1 
ATOM   2446 C  CD2 . PHE A 1 372 ? 11.01070  20.81601 33.85486  1.000 42.91245  ? 354 PHE A CD2 1 
ATOM   2447 C  CE1 . PHE A 1 372 ? 10.59950  18.40382 35.13962  1.000 46.01132  ? 354 PHE A CE1 1 
ATOM   2448 C  CE2 . PHE A 1 372 ? 11.34139  20.68100 35.19618  1.000 40.61373  ? 354 PHE A CE2 1 
ATOM   2449 C  CZ  . PHE A 1 372 ? 11.13268  19.47193 35.83952  1.000 45.13781  ? 354 PHE A CZ  1 
ATOM   2450 N  N   . GLY A 1 373 ? 11.81515  17.54912 30.05345  1.000 44.27413  ? 355 GLY A N   1 
ATOM   2451 C  CA  . GLY A 1 373 ? 12.57383  16.30955 30.11305  1.000 48.09715  ? 355 GLY A CA  1 
ATOM   2452 C  C   . GLY A 1 373 ? 14.06402  16.53322 29.93660  1.000 49.60663  ? 355 GLY A C   1 
ATOM   2453 O  O   . GLY A 1 373 ? 14.88185  15.88132 30.59286  1.000 50.19025  ? 355 GLY A O   1 
ATOM   2454 N  N   . ASN A 1 374 ? 14.43820  17.46235 29.05036  1.000 41.21754  ? 356 ASN A N   1 
ATOM   2455 C  CA  . ASN A 1 374 ? 15.84643  17.82397 28.91553  1.000 50.23145  ? 356 ASN A CA  1 
ATOM   2456 C  C   . ASN A 1 374 ? 16.36808  18.47182 30.19091  1.000 53.87441  ? 356 ASN A C   1 
ATOM   2457 O  O   . ASN A 1 374 ? 17.51821  18.24540 30.58630  1.000 49.40629  ? 356 ASN A O   1 
ATOM   2458 C  CB  . ASN A 1 374 ? 16.03948  18.76036 27.72465  1.000 50.46033  ? 356 ASN A CB  1 
ATOM   2459 C  CG  . ASN A 1 374 ? 15.54202  18.15868 26.42667  1.000 58.45948  ? 356 ASN A CG  1 
ATOM   2460 O  OD1 . ASN A 1 374 ? 14.35588  17.86044 26.28086  1.000 53.41057  ? 356 ASN A OD1 1 
ATOM   2461 N  ND2 . ASN A 1 374 ? 16.44766  17.98062 25.47324  1.000 48.50639  ? 356 ASN A ND2 1 
ATOM   2462 N  N   . VAL A 1 375 ? 15.53558  19.27874 30.84925  1.000 52.58315  ? 357 VAL A N   1 
ATOM   2463 C  CA  . VAL A 1 375 ? 15.93747  19.88118 32.11504  1.000 47.81027  ? 357 VAL A CA  1 
ATOM   2464 C  C   . VAL A 1 375 ? 16.14066  18.80275 33.17231  1.000 52.41964  ? 357 VAL A C   1 
ATOM   2465 O  O   . VAL A 1 375 ? 17.17467  18.76527 33.85043  1.000 50.08291  ? 357 VAL A O   1 
ATOM   2466 C  CB  . VAL A 1 375 ? 14.90381  20.93067 32.56182  1.000 50.30698  ? 357 VAL A CB  1 
ATOM   2467 C  CG1 . VAL A 1 375 ? 15.14945  21.34670 34.00930  1.000 45.39442  ? 357 VAL A CG1 1 
ATOM   2468 C  CG2 . VAL A 1 375 ? 14.94912  22.14006 31.63601  1.000 47.42514  ? 357 VAL A CG2 1 
ATOM   2469 N  N   . SER A 1 376 ? 15.17027  17.89071 33.30778  1.000 48.78825  ? 358 SER A N   1 
ATOM   2470 C  CA  . SER A 1 376 ? 15.23468  16.85478 34.33624  1.000 48.06339  ? 358 SER A CA  1 
ATOM   2471 C  C   . SER A 1 376 ? 16.42934  15.92447 34.16999  1.000 50.66913  ? 358 SER A C   1 
ATOM   2472 O  O   . SER A 1 376 ? 16.72488  15.15819 35.09355  1.000 52.25895  ? 358 SER A O   1 
ATOM   2473 C  CB  . SER A 1 376 ? 13.94108  16.03239 34.33973  1.000 44.09766  ? 358 SER A CB  1 
ATOM   2474 O  OG  . SER A 1 376 ? 13.86181  15.19160 33.19716  1.000 53.49924  ? 358 SER A OG  1 
ATOM   2475 N  N   . PHE A 1 377 ? 17.11196  15.96309 33.02222  1.000 47.40766  ? 359 PHE A N   1 
ATOM   2476 C  CA  . PHE A 1 377 ? 18.31786  15.16829 32.82470  1.000 59.24069  ? 359 PHE A CA  1 
ATOM   2477 C  C   . PHE A 1 377 ? 19.56384  15.84896 33.37188  1.000 51.47706  ? 359 PHE A C   1 
ATOM   2478 O  O   . PHE A 1 377 ? 20.59236  15.18452 33.53476  1.000 59.79694  ? 359 PHE A O   1 
ATOM   2479 C  CB  . PHE A 1 377 ? 18.53365  14.87194 31.33607  1.000 57.70568  ? 359 PHE A CB  1 
ATOM   2480 C  CG  . PHE A 1 377 ? 18.09699  13.49575 30.91645  1.000 66.56399  ? 359 PHE A CG  1 
ATOM   2481 C  CD1 . PHE A 1 377 ? 19.03616  12.52311 30.60789  1.000 67.11838  ? 359 PHE A CD1 1 
ATOM   2482 C  CD2 . PHE A 1 377 ? 16.75088  13.18458 30.79095  1.000 62.32119  ? 359 PHE A CD2 1 
ATOM   2483 C  CE1 . PHE A 1 377 ? 18.64252  11.25493 30.21223  1.000 64.13695  ? 359 PHE A CE1 1 
ATOM   2484 C  CE2 . PHE A 1 377 ? 16.35035  11.91817 30.39141  1.000 67.27643  ? 359 PHE A CE2 1 
ATOM   2485 C  CZ  . PHE A 1 377 ? 17.29883  10.95278 30.10271  1.000 72.57747  ? 359 PHE A CZ  1 
ATOM   2486 N  N   . VAL A 1 378 ? 19.50449  17.15170 33.63967  1.000 53.79970  ? 360 VAL A N   1 
ATOM   2487 C  CA  . VAL A 1 378 ? 20.65164  17.87524 34.17367  1.000 59.85149  ? 360 VAL A CA  1 
ATOM   2488 C  C   . VAL A 1 378 ? 20.40284  18.45072 35.56344  1.000 53.72411  ? 360 VAL A C   1 
ATOM   2489 O  O   . VAL A 1 378 ? 21.37314  18.69851 36.29735  1.000 60.01257  ? 360 VAL A O   1 
ATOM   2490 C  CB  . VAL A 1 378 ? 21.10372  18.99301 33.20871  1.000 55.84944  ? 360 VAL A CB  1 
ATOM   2491 C  CG1 . VAL A 1 378 ? 21.50954  18.40353 31.86931  1.000 52.54135  ? 360 VAL A CG1 1 
ATOM   2492 C  CG2 . VAL A 1 378 ? 20.00456  20.02190 33.02244  1.000 54.24358  ? 360 VAL A CG2 1 
ATOM   2493 N  N   . VAL A 1 379 ? 19.15677  18.68732 35.95806  1.000 61.65160  ? 361 VAL A N   1 
ATOM   2494 C  CA  . VAL A 1 379 ? 18.83751  19.14117 37.30859  1.000 57.25543  ? 361 VAL A CA  1 
ATOM   2495 C  C   . VAL A 1 379 ? 17.72121  18.25517 37.84719  1.000 59.07854  ? 361 VAL A C   1 
ATOM   2496 O  O   . VAL A 1 379 ? 16.75322  17.97765 37.12311  1.000 54.13645  ? 361 VAL A O   1 
ATOM   2497 C  CB  . VAL A 1 379 ? 18.42006  20.62064 37.32838  1.000 59.98792  ? 361 VAL A CB  1 
ATOM   2498 C  CG1 . VAL A 1 379 ? 18.21373  21.09279 38.75872  1.000 59.45888  ? 361 VAL A CG1 1 
ATOM   2499 C  CG2 . VAL A 1 379 ? 19.45128  21.48594 36.62422  1.000 59.38432  ? 361 VAL A CG2 1 
ATOM   2500 N  N   . PRO A 1 380 ? 17.81934  17.77201 39.08388  1.000 56.46328  ? 362 PRO A N   1 
ATOM   2501 C  CA  . PRO A 1 380 ? 16.66947  17.09720 39.70531  1.000 59.75905  ? 362 PRO A CA  1 
ATOM   2502 C  C   . PRO A 1 380 ? 15.45685  18.01908 39.73476  1.000 56.23345  ? 362 PRO A C   1 
ATOM   2503 O  O   . PRO A 1 380 ? 15.54986  19.18094 40.13929  1.000 57.23784  ? 362 PRO A O   1 
ATOM   2504 C  CB  . PRO A 1 380 ? 17.16556  16.77241 41.12211  1.000 51.93676  ? 362 PRO A CB  1 
ATOM   2505 C  CG  . PRO A 1 380 ? 18.66004  16.80745 41.04142  1.000 55.46925  ? 362 PRO A CG  1 
ATOM   2506 C  CD  . PRO A 1 380 ? 19.01018  17.78594 39.95380  1.000 55.71131  ? 362 PRO A CD  1 
ATOM   2507 N  N   . GLY A 1 381 ? 14.30911  17.49364 39.29804  1.000 50.31570  ? 363 GLY A N   1 
ATOM   2508 C  CA  . GLY A 1 381 ? 13.09748  18.28905 39.25221  1.000 58.46557  ? 363 GLY A CA  1 
ATOM   2509 C  C   . GLY A 1 381 ? 11.84343  17.44989 39.37896  1.000 53.43430  ? 363 GLY A C   1 
ATOM   2510 O  O   . GLY A 1 381 ? 11.88630  16.21718 39.36779  1.000 56.35593  ? 363 GLY A O   1 
ATOM   2511 N  N   . ILE A 1 382 ? 10.71434  18.14691 39.52193  1.000 49.02284  ? 364 ILE A N   1 
ATOM   2512 C  CA  . ILE A 1 382 ? 9.39200   17.53277 39.49245  1.000 49.64956  ? 364 ILE A CA  1 
ATOM   2513 C  C   . ILE A 1 382 ? 8.47408   18.39695 38.64583  1.000 52.16279  ? 364 ILE A C   1 
ATOM   2514 O  O   . ILE A 1 382 ? 8.60074   19.62479 38.60702  1.000 49.71919  ? 364 ILE A O   1 
ATOM   2515 C  CB  . ILE A 1 382 ? 8.77083   17.33822 40.89072  1.000 51.76886  ? 364 ILE A CB  1 
ATOM   2516 C  CG1 . ILE A 1 382 ? 8.88698   18.62713 41.70944  1.000 51.45329  ? 364 ILE A CG1 1 
ATOM   2517 C  CG2 . ILE A 1 382 ? 9.38513   16.13344 41.58349  1.000 65.02157  ? 364 ILE A CG2 1 
ATOM   2518 C  CD1 . ILE A 1 382 ? 7.77188   18.80975 42.71912  1.000 58.86680  ? 364 ILE A CD1 1 
ATOM   2519 N  N   . HIS A 1 383 ? 7.52820   17.73724 37.98153  1.000 50.50333  ? 365 HIS A N   1 
ATOM   2520 C  CA  . HIS A 1 383 ? 6.63449   18.38054 37.01853  1.000 46.47872  ? 365 HIS A CA  1 
ATOM   2521 C  C   . HIS A 1 383 ? 5.21455   17.86640 37.24829  1.000 49.56254  ? 365 HIS A C   1 
ATOM   2522 O  O   . HIS A 1 383 ? 4.61636   17.23055 36.37578  1.000 60.65817  ? 365 HIS A O   1 
ATOM   2523 C  CB  . HIS A 1 383 ? 7.12871   18.09514 35.59746  1.000 47.48621  ? 365 HIS A CB  1 
ATOM   2524 C  CG  . HIS A 1 383 ? 6.31827   18.73274 34.51051  1.000 52.77538  ? 365 HIS A CG  1 
ATOM   2525 N  ND1 . HIS A 1 383 ? 5.01884   18.36249 34.23194  1.000 53.47661  ? 365 HIS A ND1 1 
ATOM   2526 C  CD2 . HIS A 1 383 ? 6.64111   19.68311 33.60112  1.000 50.81753  ? 365 HIS A CD2 1 
ATOM   2527 C  CE1 . HIS A 1 383 ? 4.56921   19.07519 33.21440  1.000 52.81275  ? 365 HIS A CE1 1 
ATOM   2528 N  NE2 . HIS A 1 383 ? 5.53332   19.88430 32.81315  1.000 56.26984  ? 365 HIS A NE2 1 
ATOM   2529 N  N   . PRO A 1 384 ? 4.64867   18.10963 38.43187  1.000 49.40434  ? 366 PRO A N   1 
ATOM   2530 C  CA  . PRO A 1 384 ? 3.32020   17.56121 38.72832  1.000 54.44791  ? 366 PRO A CA  1 
ATOM   2531 C  C   . PRO A 1 384 ? 2.23337   18.19000 37.87198  1.000 56.66146  ? 366 PRO A C   1 
ATOM   2532 O  O   . PRO A 1 384 ? 2.30406   19.35891 37.48361  1.000 52.13883  ? 366 PRO A O   1 
ATOM   2533 C  CB  . PRO A 1 384 ? 3.11655   17.89989 40.20902  1.000 49.58582  ? 366 PRO A CB  1 
ATOM   2534 C  CG  . PRO A 1 384 ? 3.97520   19.09820 40.43653  1.000 53.35592  ? 366 PRO A CG  1 
ATOM   2535 C  CD  . PRO A 1 384 ? 5.18061   18.88790 39.56756  1.000 45.78953  ? 366 PRO A CD  1 
ATOM   2536 N  N   . TYR A 1 385 ? 1.21892   17.38628 37.57550  1.000 52.42537  ? 367 TYR A N   1 
ATOM   2537 C  CA  . TYR A 1 385 ? 0.03142   17.84480 36.87262  1.000 54.60567  ? 367 TYR A CA  1 
ATOM   2538 C  C   . TYR A 1 385 ? -1.10115  18.02075 37.87360  1.000 56.34747  ? 367 TYR A C   1 
ATOM   2539 O  O   . TYR A 1 385 ? -1.25189  17.21526 38.79674  1.000 67.85909  ? 367 TYR A O   1 
ATOM   2540 C  CB  . TYR A 1 385 ? -0.36937  16.85389 35.77735  1.000 50.19932  ? 367 TYR A CB  1 
ATOM   2541 C  CG  . TYR A 1 385 ? 0.63385   16.75648 34.64794  1.000 55.79084  ? 367 TYR A CG  1 
ATOM   2542 C  CD1 . TYR A 1 385 ? 1.70106   15.86611 34.71049  1.000 56.72490  ? 367 TYR A CD1 1 
ATOM   2543 C  CD2 . TYR A 1 385 ? 0.51580   17.56027 33.51997  1.000 55.47944  ? 367 TYR A CD2 1 
ATOM   2544 C  CE1 . TYR A 1 385 ? 2.62333   15.77895 33.67735  1.000 59.45494  ? 367 TYR A CE1 1 
ATOM   2545 C  CE2 . TYR A 1 385 ? 1.42801   17.48037 32.48444  1.000 59.56224  ? 367 TYR A CE2 1 
ATOM   2546 C  CZ  . TYR A 1 385 ? 2.47856   16.58818 32.56629  1.000 67.09925  ? 367 TYR A CZ  1 
ATOM   2547 O  OH  . TYR A 1 385 ? 3.38128   16.51415 31.53063  1.000 60.80374  ? 367 TYR A OH  1 
ATOM   2548 N  N   . PHE A 1 386 ? -1.88806  19.08152 37.70324  1.000 50.26613  ? 368 PHE A N   1 
ATOM   2549 C  CA  . PHE A 1 386 ? -2.97314  19.37128 38.62987  1.000 63.42832  ? 368 PHE A CA  1 
ATOM   2550 C  C   . PHE A 1 386 ? -4.25906  19.67230 37.87211  1.000 59.95484  ? 368 PHE A C   1 
ATOM   2551 O  O   . PHE A 1 386 ? -4.23851  20.13542 36.72846  1.000 57.20376  ? 368 PHE A O   1 
ATOM   2552 C  CB  . PHE A 1 386 ? -2.62888  20.54649 39.56452  1.000 49.28525  ? 368 PHE A CB  1 
ATOM   2553 C  CG  . PHE A 1 386 ? -2.32151  21.83388 38.84599  1.000 49.37415  ? 368 PHE A CG  1 
ATOM   2554 C  CD1 . PHE A 1 386 ? -1.06977  22.05606 38.29860  1.000 52.69911  ? 368 PHE A CD1 1 
ATOM   2555 C  CD2 . PHE A 1 386 ? -3.28178  22.82901 38.73616  1.000 52.08257  ? 368 PHE A CD2 1 
ATOM   2556 C  CE1 . PHE A 1 386 ? -0.77979  23.24230 37.64554  1.000 52.21946  ? 368 PHE A CE1 1 
ATOM   2557 C  CE2 . PHE A 1 386 ? -2.99841  24.01846 38.08560  1.000 52.92528  ? 368 PHE A CE2 1 
ATOM   2558 C  CZ  . PHE A 1 386 ? -1.74425  24.22344 37.53814  1.000 52.44421  ? 368 PHE A CZ  1 
ATOM   2559 N  N   . HIS A 1 387 ? -5.37764  19.40843 38.53916  1.000 64.56721  ? 369 HIS A N   1 
ATOM   2560 C  CA  . HIS A 1 387 ? -6.71226  19.61377 37.99458  1.000 59.99180  ? 369 HIS A CA  1 
ATOM   2561 C  C   . HIS A 1 387 ? -7.22692  20.99884 38.36929  1.000 64.44572  ? 369 HIS A C   1 
ATOM   2562 O  O   . HIS A 1 387 ? -6.92453  21.51523 39.44856  1.000 57.80702  ? 369 HIS A O   1 
ATOM   2563 C  CB  . HIS A 1 387 ? -7.62229  18.48247 38.49735  1.000 74.57522  ? 369 HIS A CB  1 
ATOM   2564 C  CG  . HIS A 1 387 ? -9.08582  18.80460 38.56708  1.000 73.14253  ? 369 HIS A CG  1 
ATOM   2565 N  ND1 . HIS A 1 387 ? -9.63929  19.54651 39.58869  1.000 90.60087  ? 369 HIS A ND1 1 
ATOM   2566 C  CD2 . HIS A 1 387 ? -10.11712 18.44299 37.76512  1.000 86.93494  ? 369 HIS A CD2 1 
ATOM   2567 C  CE1 . HIS A 1 387 ? -10.94480 19.64029 39.40487  1.000 84.00474  ? 369 HIS A CE1 1 
ATOM   2568 N  NE2 . HIS A 1 387 ? -11.26144 18.97700 38.30703  1.000 80.36216  ? 369 HIS A NE2 1 
ATOM   2569 N  N   . ILE A 1 388 ? -8.00090  21.60144 37.46404  1.000 54.14110  ? 370 ILE A N   1 
ATOM   2570 C  CA  . ILE A 1 388 ? -8.38790  23.00157 37.58167  1.000 54.86316  ? 370 ILE A CA  1 
ATOM   2571 C  C   . ILE A 1 388 ? -9.90590  23.19635 37.54298  1.000 65.31343  ? 370 ILE A C   1 
ATOM   2572 O  O   . ILE A 1 388 ? -10.37567 24.29224 37.26887  1.000 61.18089  ? 370 ILE A O   1 
ATOM   2573 C  CB  . ILE A 1 388 ? -7.69961  23.85910 36.50329  1.000 55.57941  ? 370 ILE A CB  1 
ATOM   2574 C  CG1 . ILE A 1 388 ? -8.28145  23.55099 35.11625  1.000 48.38948  ? 370 ILE A CG1 1 
ATOM   2575 C  CG2 . ILE A 1 388 ? -6.18363  23.68048 36.55183  1.000 54.91610  ? 370 ILE A CG2 1 
ATOM   2576 C  CD1 . ILE A 1 388 ? -7.72768  24.41974 34.00527  1.000 52.36322  ? 370 ILE A CD1 1 
ATOM   2577 N  N   . GLY A 1 389 ? -10.68722 22.16285 37.83297  1.000 59.35507  ? 371 GLY A N   1 
ATOM   2578 C  CA  . GLY A 1 389 ? -12.12923 22.31884 37.91414  1.000 76.38608  ? 371 GLY A CA  1 
ATOM   2579 C  C   . GLY A 1 389 ? -12.88920 22.03572 36.63973  1.000 76.72733  ? 371 GLY A C   1 
ATOM   2580 O  O   . GLY A 1 389 ? -14.04204 22.46849 36.51251  1.000 85.15774  ? 371 GLY A O   1 
ATOM   2581 N  N   . SER A 1 390 ? -12.29297 21.30977 35.69845  1.000 73.25653  ? 372 SER A N   1 
ATOM   2582 C  CA  . SER A 1 390 ? -12.91209 21.07940 34.40565  1.000 77.73141  ? 372 SER A CA  1 
ATOM   2583 C  C   . SER A 1 390 ? -12.65315 19.65090 33.95323  1.000 80.12766  ? 372 SER A C   1 
ATOM   2584 O  O   . SER A 1 390 ? -11.67579 19.01641 34.36045  1.000 73.99104  ? 372 SER A O   1 
ATOM   2585 C  CB  . SER A 1 390 ? -12.38364 22.06350 33.35551  1.000 71.89561  ? 372 SER A CB  1 
ATOM   2586 O  OG  . SER A 1 390 ? -12.91976 21.78079 32.07597  1.000 83.04892  ? 372 SER A OG  1 
ATOM   2587 N  N   . ASN A 1 391 ? -13.54986 19.15124 33.10733  1.000 80.83842  ? 373 ASN A N   1 
ATOM   2588 C  CA  . ASN A 1 391 ? -13.38542 17.85904 32.46074  1.000 75.09277  ? 373 ASN A CA  1 
ATOM   2589 C  C   . ASN A 1 391 ? -12.87147 17.98805 31.03587  1.000 73.97185  ? 373 ASN A C   1 
ATOM   2590 O  O   . ASN A 1 391 ? -12.59679 16.96795 30.39442  1.000 79.04601  ? 373 ASN A O   1 
ATOM   2591 C  CB  . ASN A 1 391 ? -14.71108 17.09097 32.46700  1.000 84.93727  ? 373 ASN A CB  1 
ATOM   2592 C  CG  . ASN A 1 391 ? -15.20842 16.80536 33.86807  1.000 90.64484  ? 373 ASN A CG  1 
ATOM   2593 O  OD1 . ASN A 1 391 ? -14.45452 16.33941 34.72355  1.000 91.56331  ? 373 ASN A OD1 1 
ATOM   2594 N  ND2 . ASN A 1 391 ? -16.48432 17.08003 34.11056  1.000 95.90355  ? 373 ASN A ND2 1 
ATOM   2595 N  N   . ALA A 1 392 ? -12.73189 19.21354 30.53213  1.000 64.11736  ? 374 ALA A N   1 
ATOM   2596 C  CA  . ALA A 1 392 ? -12.24814 19.41903 29.17561  1.000 64.84587  ? 374 ALA A CA  1 
ATOM   2597 C  C   . ALA A 1 392 ? -10.83647 18.87110 29.02687  1.000 67.94991  ? 374 ALA A C   1 
ATOM   2598 O  O   . ALA A 1 392 ? -10.08579 18.74981 29.99799  1.000 67.45682  ? 374 ALA A O   1 
ATOM   2599 C  CB  . ALA A 1 392 ? -12.27400 20.90498 28.81525  1.000 64.30631  ? 374 ALA A CB  1 
ATOM   2600 N  N   . LEU A 1 393 ? -10.48311 18.53196 27.79401  1.000 65.96180  ? 375 LEU A N   1 
ATOM   2601 C  CA  . LEU A 1 393 ? -9.17673  17.97430 27.49215  1.000 76.50465  ? 375 LEU A CA  1 
ATOM   2602 C  C   . LEU A 1 393 ? -8.20390  19.08533 27.11981  1.000 70.93063  ? 375 LEU A C   1 
ATOM   2603 O  O   . LEU A 1 393 ? -8.59709  20.12834 26.58993  1.000 67.26673  ? 375 LEU A O   1 
ATOM   2604 C  CB  . LEU A 1 393 ? -9.27310  16.95593 26.35131  1.000 78.00411  ? 375 LEU A CB  1 
ATOM   2605 C  CG  . LEU A 1 393 ? -9.93694  15.60352 26.63998  1.000 68.70317  ? 375 LEU A CG  1 
ATOM   2606 C  CD1 . LEU A 1 393 ? -9.44679  15.03716 27.96674  1.000 79.18525  ? 375 LEU A CD1 1 
ATOM   2607 C  CD2 . LEU A 1 393 ? -11.45835 15.68736 26.61201  1.000 87.42173  ? 375 LEU A CD2 1 
ATOM   2608 N  N   . ASN A 1 394 ? -6.92459  18.85190 27.40773  1.000 65.11296  ? 376 ASN A N   1 
ATOM   2609 C  CA  . ASN A 1 394 ? -5.89212  19.80675 27.03084  1.000 62.59716  ? 376 ASN A CA  1 
ATOM   2610 C  C   . ASN A 1 394 ? -5.84398  19.96946 25.51491  1.000 65.52126  ? 376 ASN A C   1 
ATOM   2611 O  O   . ASN A 1 394 ? -6.15437  19.04623 24.75675  1.000 70.74140  ? 376 ASN A O   1 
ATOM   2612 C  CB  . ASN A 1 394 ? -4.52661  19.35377 27.55255  1.000 64.32128  ? 376 ASN A CB  1 
ATOM   2613 C  CG  . ASN A 1 394 ? -4.25589  19.82684 28.96957  1.000 70.38566  ? 376 ASN A CG  1 
ATOM   2614 O  OD1 . ASN A 1 394 ? -4.89370  19.37043 29.91834  1.000 58.11593  ? 376 ASN A OD1 1 
ATOM   2615 N  ND2 . ASN A 1 394 ? -3.30327  20.74449 29.12001  1.000 62.45849  ? 376 ASN A ND2 1 
ATOM   2616 N  N   . HIS A 1 395 ? -5.46216  21.17210 25.08170  1.000 63.62715  ? 377 HIS A N   1 
ATOM   2617 C  CA  . HIS A 1 395 ? -5.31014  21.51297 23.66536  1.000 61.40825  ? 377 HIS A CA  1 
ATOM   2618 C  C   . HIS A 1 395 ? -6.64241  21.45605 22.91354  1.000 69.48175  ? 377 HIS A C   1 
ATOM   2619 O  O   . HIS A 1 395 ? -6.67459  21.23808 21.69987  1.000 72.42584  ? 377 HIS A O   1 
ATOM   2620 C  CB  . HIS A 1 395 ? -4.25099  20.63005 22.99091  1.000 60.73456  ? 377 HIS A CB  1 
ATOM   2621 C  CG  . HIS A 1 395 ? -2.86083  20.85719 23.51037  1.000 76.55653  ? 377 HIS A CG  1 
ATOM   2622 N  ND1 . HIS A 1 395 ? -1.74294  20.79179 22.70560  1.000 75.19593  ? 377 HIS A ND1 1 
ATOM   2623 C  CD2 . HIS A 1 395 ? -2.41024  21.15923 24.75330  1.000 72.64698  ? 377 HIS A CD2 1 
ATOM   2624 C  CE1 . HIS A 1 395 ? -0.66458  21.03779 23.43002  1.000 72.86693  ? 377 HIS A CE1 1 
ATOM   2625 N  NE2 . HIS A 1 395 ? -1.04197  21.26478 24.67579  1.000 75.45179  ? 377 HIS A NE2 1 
ATOM   2626 N  N   . THR A 1 396 ? -7.75269  21.66116 23.62474  1.000 64.44252  ? 378 THR A N   1 
ATOM   2627 C  CA  . THR A 1 396 ? -9.05646  21.86133 23.00975  1.000 65.76816  ? 378 THR A CA  1 
ATOM   2628 C  C   . THR A 1 396 ? -9.58360  23.24276 23.37641  1.000 66.06493  ? 378 THR A C   1 
ATOM   2629 O  O   . THR A 1 396 ? -9.14086  23.86475 24.34608  1.000 64.43551  ? 378 THR A O   1 
ATOM   2630 C  CB  . THR A 1 396 ? -10.08274 20.79417 23.43706  1.000 60.41570  ? 378 THR A CB  1 
ATOM   2631 O  OG1 . THR A 1 396 ? -10.53044 21.05491 24.77509  1.000 63.89202  ? 378 THR A OG1 1 
ATOM   2632 C  CG2 . THR A 1 396 ? -9.48740  19.39872 23.36227  1.000 62.03520  ? 378 THR A CG2 1 
ATOM   2633 N  N   . GLU A 1 397 ? -10.55142 23.70800 22.58377  1.000 64.03310  ? 379 GLU A N   1 
ATOM   2634 C  CA  . GLU A 1 397 ? -11.11463 25.03966 22.78126  1.000 70.38202  ? 379 GLU A CA  1 
ATOM   2635 C  C   . GLU A 1 397 ? -11.73892 25.18660 24.16452  1.000 68.86792  ? 379 GLU A C   1 
ATOM   2636 O  O   . GLU A 1 397 ? -11.65470 26.25538 24.77980  1.000 61.96609  ? 379 GLU A O   1 
ATOM   2637 C  CB  . GLU A 1 397 ? -12.15700 25.32679 21.69876  1.000 76.78227  ? 379 GLU A CB  1 
ATOM   2638 C  CG  . GLU A 1 397 ? -11.76707 26.41917 20.72480  1.000 78.08619  ? 379 GLU A CG  1 
ATOM   2639 C  CD  . GLU A 1 397 ? -12.74263 26.54105 19.57138  1.000 88.74115  ? 379 GLU A CD  1 
ATOM   2640 O  OE1 . GLU A 1 397 ? -13.88813 26.05597 19.70378  1.000 84.08971  ? 379 GLU A OE1 1 
ATOM   2641 O  OE2 . GLU A 1 397 ? -12.36428 27.12192 18.53227  1.000 94.89585  ? 379 GLU A OE2 1 
ATOM   2642 N  N   . GLN A 1 398 ? -12.38572 24.13089 24.66488  1.000 66.20165  ? 380 GLN A N   1 
ATOM   2643 C  CA  . GLN A 1 398 ? -13.02986 24.21732 25.96953  1.000 65.54592  ? 380 GLN A CA  1 
ATOM   2644 C  C   . GLN A 1 398 ? -12.02492 24.29027 27.11009  1.000 67.12599  ? 380 GLN A C   1 
ATOM   2645 O  O   . GLN A 1 398 ? -12.37221 24.78181 28.18858  1.000 61.42712  ? 380 GLN A O   1 
ATOM   2646 C  CB  . GLN A 1 398 ? -13.97759 23.03416 26.17348  1.000 74.52188  ? 380 GLN A CB  1 
ATOM   2647 C  CG  . GLN A 1 398 ? -15.24567 23.12323 25.34154  1.000 64.93941  ? 380 GLN A CG  1 
ATOM   2648 C  CD  . GLN A 1 398 ? -16.47339 22.62784 26.08019  1.000 75.68202  ? 380 GLN A CD  1 
ATOM   2649 O  OE1 . GLN A 1 398 ? -16.62865 22.85793 27.27829  1.000 78.65579  ? 380 GLN A OE1 1 
ATOM   2650 N  NE2 . GLN A 1 398 ? -17.36239 21.95128 25.35978  1.000 81.26577  ? 380 GLN A NE2 1 
ATOM   2651 N  N   . TYR A 1 399 ? -10.78938 23.82457 26.90396  1.000 57.23718  ? 381 TYR A N   1 
ATOM   2652 C  CA  . TYR A 1 399 ? -9.78552  23.99799 27.94599  1.000 60.17416  ? 381 TYR A CA  1 
ATOM   2653 C  C   . TYR A 1 399 ? -9.33965  25.44833 28.05514  1.000 60.70411  ? 381 TYR A C   1 
ATOM   2654 O  O   . TYR A 1 399 ? -9.04492  25.91758 29.16071  1.000 54.70952  ? 381 TYR A O   1 
ATOM   2655 C  CB  . TYR A 1 399 ? -8.58401  23.08797 27.70324  1.000 52.44835  ? 381 TYR A CB  1 
ATOM   2656 C  CG  . TYR A 1 399 ? -7.87979  22.70736 28.98628  1.000 59.76255  ? 381 TYR A CG  1 
ATOM   2657 C  CD1 . TYR A 1 399 ? -8.39246  21.71653 29.81483  1.000 57.25442  ? 381 TYR A CD1 1 
ATOM   2658 C  CD2 . TYR A 1 399 ? -6.70498  23.34275 29.37211  1.000 55.78920  ? 381 TYR A CD2 1 
ATOM   2659 C  CE1 . TYR A 1 399 ? -7.75689  21.37087 30.99596  1.000 58.25006  ? 381 TYR A CE1 1 
ATOM   2660 C  CE2 . TYR A 1 399 ? -6.05945  23.00191 30.54299  1.000 60.47155  ? 381 TYR A CE2 1 
ATOM   2661 C  CZ  . TYR A 1 399 ? -6.58681  22.01781 31.35437  1.000 71.06282  ? 381 TYR A CZ  1 
ATOM   2662 O  OH  . TYR A 1 399 ? -5.93234  21.69213 32.52411  1.000 58.26193  ? 381 TYR A OH  1 
ATOM   2663 N  N   . THR A 1 400 ? -9.28325  26.17088 26.93057  1.000 57.75917  ? 382 THR A N   1 
ATOM   2664 C  CA  . THR A 1 400 ? -8.98810  27.60051 26.99033  1.000 59.07835  ? 382 THR A CA  1 
ATOM   2665 C  C   . THR A 1 400 ? -9.97737  28.31893 27.89759  1.000 62.22253  ? 382 THR A C   1 
ATOM   2666 O  O   . THR A 1 400 ? -9.59963  29.22284 28.65418  1.000 54.07641  ? 382 THR A O   1 
ATOM   2667 C  CB  . THR A 1 400 ? -9.01625  28.21132 25.58736  1.000 61.15995  ? 382 THR A CB  1 
ATOM   2668 O  OG1 . THR A 1 400 ? -8.01092  27.59828 24.77005  1.000 51.49376  ? 382 THR A OG1 1 
ATOM   2669 C  CG2 . THR A 1 400 ? -8.75823  29.70707 25.65452  1.000 54.55002  ? 382 THR A CG2 1 
ATOM   2670 N  N   . GLU A 1 401 ? -11.24904 27.91482 27.84393  1.000 56.63346  ? 383 GLU A N   1 
ATOM   2671 C  CA  . GLU A 1 401 ? -12.25939 28.49846 28.71814  1.000 59.98853  ? 383 GLU A CA  1 
ATOM   2672 C  C   . GLU A 1 401 ? -11.91357 28.25784 30.18205  1.000 59.16923  ? 383 GLU A C   1 
ATOM   2673 O  O   . GLU A 1 401 ? -11.96375 29.17889 31.00693  1.000 54.25171  ? 383 GLU A O   1 
ATOM   2674 C  CB  . GLU A 1 401 ? -13.62910 27.90301 28.39804  1.000 53.10816  ? 383 GLU A CB  1 
ATOM   2675 C  CG  . GLU A 1 401 ? -14.21152 28.31209 27.05808  1.000 54.55508  ? 383 GLU A CG  1 
ATOM   2676 C  CD  . GLU A 1 401 ? -15.53105 27.60879 26.77813  1.000 70.74154  ? 383 GLU A CD  1 
ATOM   2677 O  OE1 . GLU A 1 401 ? -16.04530 26.92990 27.69505  1.000 64.74294  ? 383 GLU A OE1 1 
ATOM   2678 O  OE2 . GLU A 1 401 ? -16.05700 27.73337 25.64943  1.000 71.84789  ? 383 GLU A OE2 1 
ATOM   2679 N  N   . ALA A 1 402 ? -11.56500 27.01320 30.52187  1.000 53.77749  ? 384 ALA A N   1 
ATOM   2680 C  CA  . ALA A 1 402 ? -11.24834 26.67816 31.90485  1.000 54.41064  ? 384 ALA A CA  1 
ATOM   2681 C  C   . ALA A 1 402 ? -9.98696  27.38937 32.36990  1.000 55.25673  ? 384 ALA A C   1 
ATOM   2682 O  O   . ALA A 1 402 ? -9.93711  27.90479 33.49367  1.000 55.87565  ? 384 ALA A O   1 
ATOM   2683 C  CB  . ALA A 1 402 ? -11.09173 25.16542 32.05463  1.000 53.16255  ? 384 ALA A CB  1 
ATOM   2684 N  N   . ALA A 1 403 ? -8.96459  27.43352 31.51142  1.000 49.65526  ? 385 ALA A N   1 
ATOM   2685 C  CA  . ALA A 1 403 ? -7.68368  28.02374 31.88533  1.000 51.68653  ? 385 ALA A CA  1 
ATOM   2686 C  C   . ALA A 1 403 ? -7.83032  29.47472 32.32102  1.000 54.62167  ? 385 ALA A C   1 
ATOM   2687 O  O   . ALA A 1 403 ? -7.09774  29.93186 33.20484  1.000 51.84209  ? 385 ALA A O   1 
ATOM   2688 C  CB  . ALA A 1 403 ? -6.70151  27.91754 30.71744  1.000 41.67605  ? 385 ALA A CB  1 
ATOM   2689 N  N   . GLY A 1 404 ? -8.76497  30.21030 31.72425  1.000 57.03200  ? 386 GLY A N   1 
ATOM   2690 C  CA  . GLY A 1 404 ? -8.98429  31.59770 32.06466  1.000 56.75792  ? 386 GLY A CA  1 
ATOM   2691 C  C   . GLY A 1 404 ? -10.09378 31.84285 33.05502  1.000 55.87084  ? 386 GLY A C   1 
ATOM   2692 O  O   . GLY A 1 404 ? -10.34626 32.99809 33.40981  1.000 61.46935  ? 386 GLY A O   1 
ATOM   2693 N  N   . SER A 1 405 ? -10.75871 30.79013 33.52138  1.000 63.62505  ? 387 SER A N   1 
ATOM   2694 C  CA  . SER A 1 405 ? -11.90998 30.92836 34.39689  1.000 62.64433  ? 387 SER A CA  1 
ATOM   2695 C  C   . SER A 1 405 ? -11.48839 31.36672 35.79529  1.000 63.85740  ? 387 SER A C   1 
ATOM   2696 O  O   . SER A 1 405 ? -10.34810 31.17352 36.22528  1.000 60.69268  ? 387 SER A O   1 
ATOM   2697 C  CB  . SER A 1 405 ? -12.66652 29.60431 34.48742  1.000 66.15685  ? 387 SER A CB  1 
ATOM   2698 O  OG  . SER A 1 405 ? -11.83638 28.59478 35.04256  1.000 70.64906  ? 387 SER A OG  1 
ATOM   2699 N  N   . GLN A 1 406 ? -12.44220 31.95906 36.51349  1.000 58.87469  ? 388 GLN A N   1 
ATOM   2700 C  CA  . GLN A 1 406 ? -12.21528 32.27153 37.91909  1.000 68.63296  ? 388 GLN A CA  1 
ATOM   2701 C  C   . GLN A 1 406 ? -12.06586 31.00466 38.75183  1.000 70.65420  ? 388 GLN A C   1 
ATOM   2702 O  O   . GLN A 1 406 ? -11.31449 30.99442 39.73503  1.000 67.17277  ? 388 GLN A O   1 
ATOM   2703 C  CB  . GLN A 1 406 ? -13.36067 33.13203 38.45701  1.000 65.54480  ? 388 GLN A CB  1 
ATOM   2704 C  CG  . GLN A 1 406 ? -13.14827 33.62589 39.87669  1.000 74.72869  ? 388 GLN A CG  1 
ATOM   2705 C  CD  . GLN A 1 406 ? -11.81244 34.32886 40.04555  1.000 92.69946  ? 388 GLN A CD  1 
ATOM   2706 O  OE1 . GLN A 1 406 ? -11.38886 35.09683 39.17987  1.000 94.03263  ? 388 GLN A OE1 1 
ATOM   2707 N  NE2 . GLN A 1 406 ? -11.14330 34.07277 41.16686  1.000 83.26678  ? 388 GLN A NE2 1 
ATOM   2708 N  N   . GLU A 1 407 ? -12.75432 29.92607 38.36247  1.000 66.63247  ? 389 GLU A N   1 
ATOM   2709 C  CA  . GLU A 1 407 ? -12.73976 28.69995 39.15504  1.000 68.95748  ? 389 GLU A CA  1 
ATOM   2710 C  C   . GLU A 1 407 ? -11.36401 28.03809 39.15068  1.000 73.73759  ? 389 GLU A C   1 
ATOM   2711 O  O   . GLU A 1 407 ? -10.99599 27.37282 40.12666  1.000 69.85573  ? 389 GLU A O   1 
ATOM   2712 C  CB  . GLU A 1 407 ? -13.83032 27.74697 38.64391  1.000 82.74903  ? 389 GLU A CB  1 
ATOM   2713 C  CG  . GLU A 1 407 ? -13.48582 26.25712 38.63601  1.000 89.11039  ? 389 GLU A CG  1 
ATOM   2714 C  CD  . GLU A 1 407 ? -14.62671 25.39224 38.10470  1.000 92.36456  ? 389 GLU A CD  1 
ATOM   2715 O  OE1 . GLU A 1 407 ? -15.08451 25.62708 36.96522  1.000 81.94919  ? 389 GLU A OE1 1 
ATOM   2716 O  OE2 . GLU A 1 407 ? -15.07059 24.47775 38.83298  1.000 96.20708  ? 389 GLU A OE2 1 
ATOM   2717 N  N   . ALA A 1 408 ? -10.57636 28.23578 38.08864  1.000 61.00167  ? 390 ALA A N   1 
ATOM   2718 C  CA  . ALA A 1 408 ? -9.24945  27.63206 38.02671  1.000 62.34256  ? 390 ALA A CA  1 
ATOM   2719 C  C   . ALA A 1 408 ? -8.25266  28.28497 38.97927  1.000 55.04002  ? 390 ALA A C   1 
ATOM   2720 O  O   . ALA A 1 408 ? -7.20622  27.68887 39.25824  1.000 56.80315  ? 390 ALA A O   1 
ATOM   2721 C  CB  . ALA A 1 408 ? -8.70540  27.69674 36.59956  1.000 55.92529  ? 390 ALA A CB  1 
ATOM   2722 N  N   . GLN A 1 409 ? -8.54660  29.48609 39.48541  1.000 58.15568  ? 391 GLN A N   1 
ATOM   2723 C  CA  . GLN A 1 409 ? -7.57035  30.20379 40.30559  1.000 67.78197  ? 391 GLN A CA  1 
ATOM   2724 C  C   . GLN A 1 409 ? -7.31779  29.49789 41.63529  1.000 65.57823  ? 391 GLN A C   1 
ATOM   2725 O  O   . GLN A 1 409 ? -6.18253  29.47991 42.12728  1.000 56.21027  ? 391 GLN A O   1 
ATOM   2726 C  CB  . GLN A 1 409 ? -8.03848  31.64003 40.54192  1.000 59.67540  ? 391 GLN A CB  1 
ATOM   2727 C  CG  . GLN A 1 409 ? -7.79493  32.56247 39.35898  1.000 55.56848  ? 391 GLN A CG  1 
ATOM   2728 C  CD  . GLN A 1 409 ? -6.34808  32.55415 38.91739  1.000 62.82788  ? 391 GLN A CD  1 
ATOM   2729 O  OE1 . GLN A 1 409 ? -6.02632  32.14305 37.79858  1.000 65.06947  ? 391 GLN A OE1 1 
ATOM   2730 N  NE2 . GLN A 1 409 ? -5.46091  33.00677 39.79825  1.000 50.97571  ? 391 GLN A NE2 1 
ATOM   2731 N  N   . PHE A 1 410 ? -8.35892  28.91075 42.23121  1.000 62.00579  ? 392 PHE A N   1 
ATOM   2732 C  CA  . PHE A 1 410 ? -8.19227  28.22058 43.50818  1.000 65.46334  ? 392 PHE A CA  1 
ATOM   2733 C  C   . PHE A 1 410 ? -7.23733  27.03903 43.37580  1.000 62.04457  ? 392 PHE A C   1 
ATOM   2734 O  O   . PHE A 1 410 ? -6.30781  26.88147 44.17609  1.000 61.91900  ? 392 PHE A O   1 
ATOM   2735 C  CB  . PHE A 1 410 ? -9.55290  27.75756 44.03464  1.000 69.53289  ? 392 PHE A CB  1 
ATOM   2736 C  CG  . PHE A 1 410 ? -9.46208  26.71855 45.11841  1.000 71.84978  ? 392 PHE A CG  1 
ATOM   2737 C  CD1 . PHE A 1 410 ? -9.15245  27.08345 46.42376  1.000 73.29381  ? 392 PHE A CD1 1 
ATOM   2738 C  CD2 . PHE A 1 410 ? -9.68437  25.37730 44.83529  1.000 60.25997  ? 392 PHE A CD2 1 
ATOM   2739 C  CE1 . PHE A 1 410 ? -9.06724  26.13127 47.42914  1.000 63.49280  ? 392 PHE A CE1 1 
ATOM   2740 C  CE2 . PHE A 1 410 ? -9.59966  24.41848 45.83655  1.000 70.67569  ? 392 PHE A CE2 1 
ATOM   2741 C  CZ  . PHE A 1 410 ? -9.29271  24.79756 47.13650  1.000 67.68842  ? 392 PHE A CZ  1 
ATOM   2742 N  N   . TYR A 1 411 ? -7.45280  26.19439 42.36457  1.000 67.32925  ? 393 TYR A N   1 
ATOM   2743 C  CA  . TYR A 1 411 ? -6.59326  25.03006 42.17498  1.000 62.49950  ? 393 TYR A CA  1 
ATOM   2744 C  C   . TYR A 1 411 ? -5.15995  25.43016 41.84285  1.000 62.23779  ? 393 TYR A C   1 
ATOM   2745 O  O   . TYR A 1 411 ? -4.21204  24.75082 42.25941  1.000 48.56304  ? 393 TYR A O   1 
ATOM   2746 C  CB  . TYR A 1 411 ? -7.16276  24.14120 41.07012  1.000 60.53715  ? 393 TYR A CB  1 
ATOM   2747 C  CG  . TYR A 1 411 ? -8.58121  23.67495 41.32682  1.000 71.76010  ? 393 TYR A CG  1 
ATOM   2748 C  CD1 . TYR A 1 411 ? -8.83358  22.53536 42.08094  1.000 69.13038  ? 393 TYR A CD1 1 
ATOM   2749 C  CD2 . TYR A 1 411 ? -9.66750  24.37215 40.81030  1.000 69.59142  ? 393 TYR A CD2 1 
ATOM   2750 C  CE1 . TYR A 1 411 ? -10.13250 22.10406 42.31839  1.000 76.49207  ? 393 TYR A CE1 1 
ATOM   2751 C  CE2 . TYR A 1 411 ? -10.96853 23.94944 41.04120  1.000 75.57257  ? 393 TYR A CE2 1 
ATOM   2752 C  CZ  . TYR A 1 411 ? -11.19632 22.81455 41.79601  1.000 72.03251  ? 393 TYR A CZ  1 
ATOM   2753 O  OH  . TYR A 1 411 ? -12.48968 22.39415 42.02788  1.000 79.01084  ? 393 TYR A OH  1 
ATOM   2754 N  N   . THR A 1 412 ? -4.98120  26.52035 41.09466  1.000 58.54381  ? 394 THR A N   1 
ATOM   2755 C  CA  . THR A 1 412 ? -3.63788  26.95073 40.72207  1.000 50.62699  ? 394 THR A CA  1 
ATOM   2756 C  C   . THR A 1 412 ? -2.85083  27.40708 41.94558  1.000 53.80478  ? 394 THR A C   1 
ATOM   2757 O  O   . THR A 1 412 ? -1.70308  26.99340 42.15006  1.000 48.04036  ? 394 THR A O   1 
ATOM   2758 C  CB  . THR A 1 412 ? -3.72026  28.06624 39.67876  1.000 50.70548  ? 394 THR A CB  1 
ATOM   2759 O  OG1 . THR A 1 412 ? -4.54692  27.63827 38.58492  1.000 53.69533  ? 394 THR A OG1 1 
ATOM   2760 C  CG2 . THR A 1 412 ? -2.33482  28.43032 39.16292  1.000 40.08346  ? 394 THR A CG2 1 
ATOM   2761 N  N   . LEU A 1 413 ? -3.45310  28.26092 42.77371  1.000 50.17229  ? 395 LEU A N   1 
ATOM   2762 C  CA  . LEU A 1 413 ? -2.76092  28.72309 43.96888  1.000 59.87699  ? 395 LEU A CA  1 
ATOM   2763 C  C   . LEU A 1 413 ? -2.52125  27.58464 44.94917  1.000 56.90834  ? 395 LEU A C   1 
ATOM   2764 O  O   . LEU A 1 413 ? -1.49615  27.57137 45.63916  1.000 56.34871  ? 395 LEU A O   1 
ATOM   2765 C  CB  . LEU A 1 413 ? -3.55140  29.85056 44.62743  1.000 47.33650  ? 395 LEU A CB  1 
ATOM   2766 C  CG  . LEU A 1 413 ? -3.69519  31.06970 43.71479  1.000 58.76287  ? 395 LEU A CG  1 
ATOM   2767 C  CD1 . LEU A 1 413 ? -4.48286  32.17550 44.38740  1.000 58.05729  ? 395 LEU A CD1 1 
ATOM   2768 C  CD2 . LEU A 1 413 ? -2.32330  31.56913 43.27649  1.000 51.84979  ? 395 LEU A CD2 1 
ATOM   2769 N  N   . ARG A 1 414 ? -3.43227  26.61088 45.00115  1.000 55.52255  ? 396 ARG A N   1 
ATOM   2770 C  CA  . ARG A 1 414 ? -3.25875  25.47886 45.90561  1.000 56.11261  ? 396 ARG A CA  1 
ATOM   2771 C  C   . ARG A 1 414 ? -2.01950  24.66742 45.54020  1.000 55.98256  ? 396 ARG A C   1 
ATOM   2772 O  O   . ARG A 1 414 ? -1.21125  24.32072 46.40900  1.000 55.71862  ? 396 ARG A O   1 
ATOM   2773 C  CB  . ARG A 1 414 ? -4.51112  24.60191 45.88658  1.000 54.07012  ? 396 ARG A CB  1 
ATOM   2774 C  CG  . ARG A 1 414 ? -4.43393  23.39314 46.80068  1.000 64.48563  ? 396 ARG A CG  1 
ATOM   2775 C  CD  . ARG A 1 414 ? -5.78543  22.71331 46.93819  1.000 60.97957  ? 396 ARG A CD  1 
ATOM   2776 N  NE  . ARG A 1 414 ? -6.06134  21.82481 45.81521  1.000 71.05538  ? 396 ARG A NE  1 
ATOM   2777 C  CZ  . ARG A 1 414 ? -7.22558  21.22550 45.60467  1.000 77.27933  ? 396 ARG A CZ  1 
ATOM   2778 N  NH1 . ARG A 1 414 ? -8.24702  21.39391 46.42911  1.000 67.29463  ? 396 ARG A NH1 1 
ATOM   2779 N  NH2 . ARG A 1 414 ? -7.36929  20.43942 44.53939  1.000 68.26717  ? 396 ARG A NH2 1 
ATOM   2780 N  N   . THR A 1 415 ? -1.84821  24.36001 44.25160  1.000 52.92681  ? 397 THR A N   1 
ATOM   2781 C  CA  . THR A 1 415 ? -0.67864  23.59663 43.82886  1.000 48.41686  ? 397 THR A CA  1 
ATOM   2782 C  C   . THR A 1 415 ? 0.60227   24.41532 43.96430  1.000 52.45445  ? 397 THR A C   1 
ATOM   2783 O  O   . THR A 1 415 ? 1.66988   23.85728 44.24755  1.000 57.06318  ? 397 THR A O   1 
ATOM   2784 C  CB  . THR A 1 415 ? -0.87534  23.10142 42.39191  1.000 56.68272  ? 397 THR A CB  1 
ATOM   2785 O  OG1 . THR A 1 415 ? -1.93954  22.13817 42.36260  1.000 48.11429  ? 397 THR A OG1 1 
ATOM   2786 C  CG2 . THR A 1 415 ? 0.39134   22.45603 41.85037  1.000 43.55962  ? 397 THR A CG2 1 
ATOM   2787 N  N   . ALA A 1 416 ? 0.51999   25.73510 43.78915  1.000 49.33886  ? 398 ALA A N   1 
ATOM   2788 C  CA  . ALA A 1 416 ? 1.67992   26.57564 44.06281  1.000 55.23951  ? 398 ALA A CA  1 
ATOM   2789 C  C   . ALA A 1 416 ? 2.08146   26.48611 45.53051  1.000 58.69076  ? 398 ALA A C   1 
ATOM   2790 O  O   . ALA A 1 416 ? 3.27518   26.48370 45.85756  1.000 48.79170  ? 398 ALA A O   1 
ATOM   2791 C  CB  . ALA A 1 416 ? 1.38715   28.02272 43.66943  1.000 46.73643  ? 398 ALA A CB  1 
ATOM   2792 N  N   . LYS A 1 417 ? 1.09227   26.41159 46.42791  1.000 50.87364  ? 399 LYS A N   1 
ATOM   2793 C  CA  . LYS A 1 417 ? 1.37811   26.18972 47.84154  1.000 48.80292  ? 399 LYS A CA  1 
ATOM   2794 C  C   . LYS A 1 417 ? 2.11891   24.87603 48.05042  1.000 51.69932  ? 399 LYS A C   1 
ATOM   2795 O  O   . LYS A 1 417 ? 3.05622   24.80261 48.85385  1.000 53.66997  ? 399 LYS A O   1 
ATOM   2796 C  CB  . LYS A 1 417 ? 0.08059   26.19219 48.64976  1.000 52.31885  ? 399 LYS A CB  1 
ATOM   2797 C  CG  . LYS A 1 417 ? -0.51589  27.56238 48.93034  1.000 54.30766  ? 399 LYS A CG  1 
ATOM   2798 C  CD  . LYS A 1 417 ? -1.95373  27.40612 49.43508  1.000 63.01386  ? 399 LYS A CD  1 
ATOM   2799 C  CE  . LYS A 1 417 ? -2.60302  28.74096 49.76658  1.000 58.25848  ? 399 LYS A CE  1 
ATOM   2800 N  NZ  . LYS A 1 417 ? -4.00116  28.57060 50.28841  1.000 57.84045  ? 399 LYS A NZ  1 
ATOM   2801 N  N   . ALA A 1 418 ? 1.71279   23.82604 47.33288  1.000 47.84379  ? 400 ALA A N   1 
ATOM   2802 C  CA  . ALA A 1 418 ? 2.37057   22.53273 47.48201  1.000 53.35335  ? 400 ALA A CA  1 
ATOM   2803 C  C   . ALA A 1 418 ? 3.81742   22.58779 47.00689  1.000 54.98087  ? 400 ALA A C   1 
ATOM   2804 O  O   . ALA A 1 418 ? 4.70743   22.01772 47.65090  1.000 52.35935  ? 400 ALA A O   1 
ATOM   2805 C  CB  . ALA A 1 418 ? 1.59333   21.45953 46.72512  1.000 52.98091  ? 400 ALA A CB  1 
ATOM   2806 N  N   . LEU A 1 419 ? 4.07402   23.27410 45.88854  1.000 51.16071  ? 401 LEU A N   1 
ATOM   2807 C  CA  . LEU A 1 419 ? 5.44583   23.41945 45.40641  1.000 52.65328  ? 401 LEU A CA  1 
ATOM   2808 C  C   . LEU A 1 419 ? 6.30866   24.16450 46.41752  1.000 49.70889  ? 401 LEU A C   1 
ATOM   2809 O  O   . LEU A 1 419 ? 7.43666   23.75259 46.71004  1.000 53.14486  ? 401 LEU A O   1 
ATOM   2810 C  CB  . LEU A 1 419 ? 5.46016   24.14784 44.06349  1.000 50.17388  ? 401 LEU A CB  1 
ATOM   2811 C  CG  . LEU A 1 419 ? 5.18393   23.32034 42.80915  1.000 49.88033  ? 401 LEU A CG  1 
ATOM   2812 C  CD1 . LEU A 1 419 ? 5.50973   24.13180 41.56677  1.000 48.46893  ? 401 LEU A CD1 1 
ATOM   2813 C  CD2 . LEU A 1 419 ? 5.96463   22.02024 42.83071  1.000 48.66466  ? 401 LEU A CD2 1 
ATOM   2814 N  N   . ALA A 1 420 ? 5.79073   25.26999 46.96247  1.000 52.44348  ? 402 ALA A N   1 
ATOM   2815 C  CA  . ALA A 1 420 ? 6.58453   26.09436 47.86978  1.000 51.65481  ? 402 ALA A CA  1 
ATOM   2816 C  C   . ALA A 1 420 ? 6.94448   25.33584 49.14057  1.000 56.59248  ? 402 ALA A C   1 
ATOM   2817 O  O   . ALA A 1 420 ? 8.08552   25.41481 49.61556  1.000 47.47908  ? 402 ALA A O   1 
ATOM   2818 C  CB  . ALA A 1 420 ? 5.83349   27.38082 48.20912  1.000 49.45685  ? 402 ALA A CB  1 
ATOM   2819 N  N   . MET A 1 421 ? 5.98537   24.59705 49.70869  1.000 52.78558  ? 403 MET A N   1 
ATOM   2820 C  CA  . MET A 1 421 ? 6.28548   23.79615 50.89147  1.000 62.06941  ? 403 MET A CA  1 
ATOM   2821 C  C   . MET A 1 421 ? 7.31018   22.71656 50.57394  1.000 58.77638  ? 403 MET A C   1 
ATOM   2822 O  O   . MET A 1 421 ? 8.16885   22.40090 51.40624  1.000 58.99838  ? 403 MET A O   1 
ATOM   2823 C  CB  . MET A 1 421 ? 5.01040   23.16949 51.46027  1.000 54.30979  ? 403 MET A CB  1 
ATOM   2824 C  CG  . MET A 1 421 ? 3.94354   24.16945 51.87421  1.000 63.11732  ? 403 MET A CG  1 
ATOM   2825 S  SD  . MET A 1 421 ? 2.43632   23.36714 52.46509  1.000 71.20169  ? 403 MET A SD  1 
ATOM   2826 C  CE  . MET A 1 421 ? 1.51292   24.78061 53.06890  1.000 67.25218  ? 403 MET A CE  1 
ATOM   2827 N  N   . THR A 1 422 ? 7.23393   22.13838 49.37336  1.000 51.16038  ? 404 THR A N   1 
ATOM   2828 C  CA  . THR A 1 422 ? 8.21870   21.14237 48.96680  1.000 55.00935  ? 404 THR A CA  1 
ATOM   2829 C  C   . THR A 1 422 ? 9.60658   21.76197 48.85551  1.000 58.29341  ? 404 THR A C   1 
ATOM   2830 O  O   . THR A 1 422 ? 10.60722  21.13570 49.22458  1.000 58.13306  ? 404 THR A O   1 
ATOM   2831 C  CB  . THR A 1 422 ? 7.79713   20.50758 47.64208  1.000 53.92572  ? 404 THR A CB  1 
ATOM   2832 O  OG1 . THR A 1 422 ? 6.47328   19.97712 47.77339  1.000 59.65292  ? 404 THR A OG1 1 
ATOM   2833 C  CG2 . THR A 1 422 ? 8.75211   19.38812 47.24215  1.000 56.39051  ? 404 THR A CG2 1 
ATOM   2834 N  N   . ALA A 1 423 ? 9.68679   22.99861 48.35878  1.000 51.16191  ? 405 ALA A N   1 
ATOM   2835 C  CA  . ALA A 1 423 ? 10.96653  23.69871 48.34487  1.000 54.27334  ? 405 ALA A CA  1 
ATOM   2836 C  C   . ALA A 1 423 ? 11.47867  23.92778 49.76255  1.000 59.04196  ? 405 ALA A C   1 
ATOM   2837 O  O   . ALA A 1 423 ? 12.68309  23.82474 50.01929  1.000 55.79249  ? 405 ALA A O   1 
ATOM   2838 C  CB  . ALA A 1 423 ? 10.83435  25.02596 47.59677  1.000 50.86251  ? 405 ALA A CB  1 
ATOM   2839 N  N   . LEU A 1 424 ? 10.57662  24.23147 50.70007  1.000 50.87114  ? 406 LEU A N   1 
ATOM   2840 C  CA  . LEU A 1 424 ? 10.99379  24.41267 52.08649  1.000 55.83264  ? 406 LEU A CA  1 
ATOM   2841 C  C   . LEU A 1 424 ? 11.53670  23.11432 52.67303  1.000 59.05312  ? 406 LEU A C   1 
ATOM   2842 O  O   . LEU A 1 424 ? 12.49120  23.13348 53.45890  1.000 54.39618  ? 406 LEU A O   1 
ATOM   2843 C  CB  . LEU A 1 424 ? 9.82822   24.94194 52.92270  1.000 53.70050  ? 406 LEU A CB  1 
ATOM   2844 C  CG  . LEU A 1 424 ? 9.42753   26.39310 52.64643  1.000 54.56145  ? 406 LEU A CG  1 
ATOM   2845 C  CD1 . LEU A 1 424 ? 8.18725   26.77818 53.43474  1.000 57.27665  ? 406 LEU A CD1 1 
ATOM   2846 C  CD2 . LEU A 1 424 ? 10.58150  27.33605 52.95743  1.000 48.08250  ? 406 LEU A CD2 1 
ATOM   2847 N  N   . ASP A 1 425 ? 10.95385  21.97449 52.28823  1.000 58.65276  ? 407 ASP A N   1 
ATOM   2848 C  CA  . ASP A 1 425 ? 11.47539  20.68277 52.72997  1.000 60.58035  ? 407 ASP A CA  1 
ATOM   2849 C  C   . ASP A 1 425 ? 12.93448  20.50730 52.31908  1.000 67.98664  ? 407 ASP A C   1 
ATOM   2850 O  O   . ASP A 1 425 ? 13.78166  20.13022 53.13787  1.000 59.81062  ? 407 ASP A O   1 
ATOM   2851 C  CB  . ASP A 1 425 ? 10.62290  19.54573 52.16014  1.000 61.00386  ? 407 ASP A CB  1 
ATOM   2852 C  CG  . ASP A 1 425 ? 9.35391   19.30536 52.95892  1.000 68.94308  ? 407 ASP A CG  1 
ATOM   2853 O  OD1 . ASP A 1 425 ? 9.34813   19.58806 54.17576  1.000 63.56619  ? 407 ASP A OD1 1 
ATOM   2854 O  OD2 . ASP A 1 425 ? 8.36339   18.82164 52.36889  1.000 69.51623  ? 407 ASP A OD2 1 
ATOM   2855 N  N   . VAL A 1 426 ? 13.24701  20.78137 51.04887  1.000 57.23866  ? 408 VAL A N   1 
ATOM   2856 C  CA  . VAL A 1 426 ? 14.61649  20.61727 50.56701  1.000 61.32033  ? 408 VAL A CA  1 
ATOM   2857 C  C   . VAL A 1 426 ? 15.56750  21.53111 51.33046  1.000 58.96557  ? 408 VAL A C   1 
ATOM   2858 O  O   . VAL A 1 426 ? 16.71489  21.16433 51.61205  1.000 65.91579  ? 408 VAL A O   1 
ATOM   2859 C  CB  . VAL A 1 426 ? 14.68045  20.87640 49.04869  1.000 64.81605  ? 408 VAL A CB  1 
ATOM   2860 C  CG1 . VAL A 1 426 ? 16.10446  20.72806 48.54128  1.000 57.68320  ? 408 VAL A CG1 1 
ATOM   2861 C  CG2 . VAL A 1 426 ? 13.74618  19.93153 48.31073  1.000 56.74996  ? 408 VAL A CG2 1 
ATOM   2862 N  N   . ILE A 1 427 ? 15.09921  22.72359 51.69832  1.000 57.78079  ? 409 ILE A N   1 
ATOM   2863 C  CA  . ILE A 1 427 ? 15.97455  23.70011 52.33627  1.000 57.05188  ? 409 ILE A CA  1 
ATOM   2864 C  C   . ILE A 1 427 ? 16.37810  23.23983 53.73413  1.000 65.29225  ? 409 ILE A C   1 
ATOM   2865 O  O   . ILE A 1 427 ? 17.52912  23.41893 54.15257  1.000 68.36901  ? 409 ILE A O   1 
ATOM   2866 C  CB  . ILE A 1 427 ? 15.28909  25.07881 52.36547  1.000 56.94716  ? 409 ILE A CB  1 
ATOM   2867 C  CG1 . ILE A 1 427 ? 15.18501  25.65293 50.95002  1.000 54.36935  ? 409 ILE A CG1 1 
ATOM   2868 C  CG2 . ILE A 1 427 ? 16.03584  26.03450 53.27883  1.000 56.72135  ? 409 ILE A CG2 1 
ATOM   2869 C  CD1 . ILE A 1 427 ? 14.28051  26.86519 50.85316  1.000 51.45211  ? 409 ILE A CD1 1 
ATOM   2870 N  N   . PHE A 1 428 ? 15.45562  22.62128 54.46971  1.000 60.68072  ? 410 PHE A N   1 
ATOM   2871 C  CA  . PHE A 1 428 ? 15.66002  22.34944 55.88584  1.000 64.91070  ? 410 PHE A CA  1 
ATOM   2872 C  C   . PHE A 1 428 ? 15.87093  20.87723 56.21242  1.000 71.40458  ? 410 PHE A C   1 
ATOM   2873 O  O   . PHE A 1 428 ? 16.12738  20.54981 57.37742  1.000 72.32218  ? 410 PHE A O   1 
ATOM   2874 C  CB  . PHE A 1 428 ? 14.47979  22.89638 56.69509  1.000 63.74375  ? 410 PHE A CB  1 
ATOM   2875 C  CG  . PHE A 1 428 ? 14.45061  24.39370 56.77202  1.000 63.43904  ? 410 PHE A CG  1 
ATOM   2876 C  CD1 . PHE A 1 428 ? 15.24977  25.06855 57.68084  1.000 62.41434  ? 410 PHE A CD1 1 
ATOM   2877 C  CD2 . PHE A 1 428 ? 13.63835  25.12894 55.92343  1.000 59.20252  ? 410 PHE A CD2 1 
ATOM   2878 C  CE1 . PHE A 1 428 ? 15.23166  26.45004 57.74981  1.000 66.14962  ? 410 PHE A CE1 1 
ATOM   2879 C  CE2 . PHE A 1 428 ? 13.61540  26.51115 55.98666  1.000 63.76145  ? 410 PHE A CE2 1 
ATOM   2880 C  CZ  . PHE A 1 428 ? 14.41282  27.17246 56.90206  1.000 67.21555  ? 410 PHE A CZ  1 
ATOM   2881 N  N   . LYS A 1 429 ? 15.78812  19.98286 55.22701  1.000 66.03873  ? 411 LYS A N   1 
ATOM   2882 C  CA  . LYS A 1 429 ? 16.01473  18.55260 55.43328  1.000 71.94343  ? 411 LYS A CA  1 
ATOM   2883 C  C   . LYS A 1 429 ? 17.21197  18.12243 54.59613  1.000 71.37125  ? 411 LYS A C   1 
ATOM   2884 O  O   . LYS A 1 429 ? 17.05646  17.73902 53.42595  1.000 81.03221  ? 411 LYS A O   1 
ATOM   2885 C  CB  . LYS A 1 429 ? 14.77175  17.74059 55.07551  1.000 68.71785  ? 411 LYS A CB  1 
ATOM   2886 C  CG  . LYS A 1 429 ? 13.60368  17.95638 56.02446  1.000 69.88207  ? 411 LYS A CG  1 
ATOM   2887 C  CD  . LYS A 1 429 ? 12.52338  16.90363 55.82406  1.000 78.84434  ? 411 LYS A CD  1 
ATOM   2888 C  CE  . LYS A 1 429 ? 11.19054  17.36179 56.40403  1.000 84.79792  ? 411 LYS A CE  1 
ATOM   2889 N  NZ  . LYS A 1 429 ? 10.05926  16.49304 55.97268  1.000 79.70847  ? 411 LYS A NZ  1 
ATOM   2890 N  N   . PRO A 1 430 ? 18.42703  18.17481 55.14938  1.000 77.71040  ? 412 PRO A N   1 
ATOM   2891 C  CA  . PRO A 1 430 ? 19.59842  17.72482 54.37599  1.000 75.37573  ? 412 PRO A CA  1 
ATOM   2892 C  C   . PRO A 1 430 ? 19.51611  16.26655 53.96544  1.000 80.98219  ? 412 PRO A C   1 
ATOM   2893 O  O   . PRO A 1 430 ? 20.02128  15.90128 52.89426  1.000 74.31240  ? 412 PRO A O   1 
ATOM   2894 C  CB  . PRO A 1 430 ? 20.77384  17.97836 55.33149  1.000 66.14905  ? 412 PRO A CB  1 
ATOM   2895 C  CG  . PRO A 1 430 ? 20.26045  18.98067 56.32770  1.000 72.53424  ? 412 PRO A CG  1 
ATOM   2896 C  CD  . PRO A 1 430 ? 18.79704  18.68801 56.47949  1.000 72.19350  ? 412 PRO A CD  1 
ATOM   2897 N  N   . GLU A 1 431 ? 18.88689  15.42129 54.78806  1.000 81.67591  ? 413 GLU A N   1 
ATOM   2898 C  CA  . GLU A 1 431 ? 18.67102  14.03044 54.40309  1.000 83.95624  ? 413 GLU A CA  1 
ATOM   2899 C  C   . GLU A 1 431 ? 17.83413  13.92737 53.13550  1.000 78.97181  ? 413 GLU A C   1 
ATOM   2900 O  O   . GLU A 1 431 ? 18.03827  13.01303 52.32864  1.000 81.28204  ? 413 GLU A O   1 
ATOM   2901 C  CB  . GLU A 1 431 ? 18.00169  13.26727 55.54677  1.000 81.86619  ? 413 GLU A CB  1 
ATOM   2902 C  CG  . GLU A 1 431 ? 17.74150  14.10964 56.78974  1.000 77.97282  ? 413 GLU A CG  1 
ATOM   2903 C  CD  . GLU A 1 431 ? 16.39150  14.79942 56.76273  1.000 71.65777  ? 413 GLU A CD  1 
ATOM   2904 N  N   . LEU A 1 432 ? 16.89586  14.85595 52.93793  1.000 72.24206  ? 414 LEU A N   1 
ATOM   2905 C  CA  . LEU A 1 432 ? 16.11212  14.85644 51.70836  1.000 74.86950  ? 414 LEU A CA  1 
ATOM   2906 C  C   . LEU A 1 432 ? 16.96775  15.24514 50.50838  1.000 72.22156  ? 414 LEU A C   1 
ATOM   2907 O  O   . LEU A 1 432 ? 16.86888  14.62248 49.44552  1.000 71.60702  ? 414 LEU A O   1 
ATOM   2908 C  CB  . LEU A 1 432 ? 14.91672  15.79925 51.84688  1.000 68.20811  ? 414 LEU A CB  1 
ATOM   2909 C  CG  . LEU A 1 432 ? 14.03899  15.96065 50.60254  1.000 72.53546  ? 414 LEU A CG  1 
ATOM   2910 C  CD1 . LEU A 1 432 ? 13.54378  14.61192 50.10954  1.000 67.55916  ? 414 LEU A CD1 1 
ATOM   2911 C  CD2 . LEU A 1 432 ? 12.87029  16.88812 50.88680  1.000 72.25455  ? 414 LEU A CD2 1 
ATOM   2912 N  N   . LEU A 1 433 ? 17.81944  16.26372 50.66275  1.000 74.83607  ? 415 LEU A N   1 
ATOM   2913 C  CA  . LEU A 1 433 ? 18.63617  16.73502 49.54631  1.000 64.65168  ? 415 LEU A CA  1 
ATOM   2914 C  C   . LEU A 1 433 ? 19.54241  15.62832 49.02013  1.000 64.47213  ? 415 LEU A C   1 
ATOM   2915 O  O   . LEU A 1 433 ? 19.64657  15.41983 47.80531  1.000 70.24020  ? 415 LEU A O   1 
ATOM   2916 C  CB  . LEU A 1 433 ? 19.45704  17.95284 49.97577  1.000 62.12725  ? 415 LEU A CB  1 
ATOM   2917 C  CG  . LEU A 1 433 ? 20.25139  18.70701 48.90434  1.000 65.06551  ? 415 LEU A CG  1 
ATOM   2918 C  CD1 . LEU A 1 433 ? 19.39620  19.01669 47.67887  1.000 61.83618  ? 415 LEU A CD1 1 
ATOM   2919 C  CD2 . LEU A 1 433 ? 20.83890  19.98474 49.48398  1.000 63.08424  ? 415 LEU A CD2 1 
ATOM   2920 N  N   . GLU A 1 434 ? 20.20435  14.90142 49.92184  1.000 72.09845  ? 416 GLU A N   1 
ATOM   2921 C  CA  . GLU A 1 434 ? 21.01540  13.76896 49.48863  1.000 68.23969  ? 416 GLU A CA  1 
ATOM   2922 C  C   . GLU A 1 434 ? 20.15514  12.67361 48.87243  1.000 70.83204  ? 416 GLU A C   1 
ATOM   2923 O  O   . GLU A 1 434 ? 20.58524  12.00908 47.92163  1.000 76.81882  ? 416 GLU A O   1 
ATOM   2924 C  CB  . GLU A 1 434 ? 21.82382  13.21759 50.66307  1.000 70.07292  ? 416 GLU A CB  1 
ATOM   2925 N  N   . GLY A 1 435 ? 18.94117  12.47526 49.38996  1.000 72.23989  ? 417 GLY A N   1 
ATOM   2926 C  CA  . GLY A 1 435 ? 18.04546  11.50010 48.78842  1.000 74.56722  ? 417 GLY A CA  1 
ATOM   2927 C  C   . GLY A 1 435 ? 17.64732  11.86925 47.37189  1.000 72.42904  ? 417 GLY A C   1 
ATOM   2928 O  O   . GLY A 1 435 ? 17.55141  11.00278 46.49763  1.000 71.93550  ? 417 GLY A O   1 
ATOM   2929 N  N   . ILE A 1 436 ? 17.40798  13.16101 47.12484  1.000 67.91140  ? 418 ILE A N   1 
ATOM   2930 C  CA  . ILE A 1 436 ? 17.10823  13.61112 45.76728  1.000 70.39038  ? 418 ILE A CA  1 
ATOM   2931 C  C   . ILE A 1 436 ? 18.31394  13.40308 44.86219  1.000 67.82035  ? 418 ILE A C   1 
ATOM   2932 O  O   . ILE A 1 436 ? 18.17837  12.99828 43.70069  1.000 70.53242  ? 418 ILE A O   1 
ATOM   2933 C  CB  . ILE A 1 436 ? 16.65916  15.08501 45.76739  1.000 64.96066  ? 418 ILE A CB  1 
ATOM   2934 C  CG1 . ILE A 1 436 ? 15.54803  15.32355 46.78690  1.000 61.83151  ? 418 ILE A CG1 1 
ATOM   2935 C  CG2 . ILE A 1 436 ? 16.20098  15.50152 44.38317  1.000 74.46094  ? 418 ILE A CG2 1 
ATOM   2936 C  CD1 . ILE A 1 436 ? 15.44794  16.75957 47.24310  1.000 64.72357  ? 418 ILE A CD1 1 
ATOM   2937 N  N   . ARG A 1 437 ? 19.51282  13.67052 45.38037  1.000 66.66429  ? 419 ARG A N   1 
ATOM   2938 C  CA  . ARG A 1 437 ? 20.71150  13.54379 44.56227  1.000 70.24798  ? 419 ARG A CA  1 
ATOM   2939 C  C   . ARG A 1 437 ? 21.05757  12.08606 44.29077  1.000 74.41160  ? 419 ARG A C   1 
ATOM   2940 O  O   . ARG A 1 437 ? 21.56354  11.76387 43.20896  1.000 72.32637  ? 419 ARG A O   1 
ATOM   2941 C  CB  . ARG A 1 437 ? 21.87311  14.26894 45.23787  1.000 61.32466  ? 419 ARG A CB  1 
ATOM   2942 C  CG  . ARG A 1 437 ? 21.73248  15.77801 45.16310  1.000 65.00102  ? 419 ARG A CG  1 
ATOM   2943 C  CD  . ARG A 1 437 ? 22.70676  16.49912 46.06805  1.000 65.69458  ? 419 ARG A CD  1 
ATOM   2944 N  NE  . ARG A 1 437 ? 22.71767  17.93024 45.79028  1.000 66.24344  ? 419 ARG A NE  1 
ATOM   2945 C  CZ  . ARG A 1 437 ? 23.18446  18.85155 46.62112  1.000 72.95984  ? 419 ARG A CZ  1 
ATOM   2946 N  NH1 . ARG A 1 437 ? 23.68116  18.52743 47.80433  1.000 65.53235  ? 419 ARG A NH1 1 
ATOM   2947 N  NH2 . ARG A 1 437 ? 23.15246  20.13013 46.25528  1.000 71.69720  ? 419 ARG A NH2 1 
ATOM   2948 N  N   . GLU A 1 438 ? 20.78556  11.19498 45.24734  1.000 71.82635  ? 420 GLU A N   1 
ATOM   2949 C  CA  . GLU A 1 438 ? 21.00552  9.77108  45.01686  1.000 71.89109  ? 420 GLU A CA  1 
ATOM   2950 C  C   . GLU A 1 438 ? 20.07076  9.24215  43.93436  1.000 75.47145  ? 420 GLU A C   1 
ATOM   2951 O  O   . GLU A 1 438 ? 20.51558  8.59572  42.97750  1.000 72.96515  ? 420 GLU A O   1 
ATOM   2952 C  CB  . GLU A 1 438 ? 20.82247  8.99385  46.32240  1.000 71.49999  ? 420 GLU A CB  1 
ATOM   2953 N  N   . ASP A 1 439 ? 18.76820  9.51909  44.06352  1.000 78.48322  ? 421 ASP A N   1 
ATOM   2954 C  CA  . ASP A 1 439 ? 17.80514  9.05996  43.06498  1.000 78.19516  ? 421 ASP A CA  1 
ATOM   2955 C  C   . ASP A 1 439 ? 18.09099  9.65202  41.69247  1.000 75.68538  ? 421 ASP A C   1 
ATOM   2956 O  O   . ASP A 1 439 ? 17.86874  8.98992  40.67194  1.000 85.24189  ? 421 ASP A O   1 
ATOM   2957 C  CB  . ASP A 1 439 ? 16.38213  9.41916  43.49612  1.000 75.89076  ? 421 ASP A CB  1 
ATOM   2958 C  CG  . ASP A 1 439 ? 15.98165  8.76577  44.80160  1.000 79.40739  ? 421 ASP A CG  1 
ATOM   2959 O  OD1 . ASP A 1 439 ? 16.73387  7.89759  45.29130  1.000 85.42386  ? 421 ASP A OD1 1 
ATOM   2960 O  OD2 . ASP A 1 439 ? 14.90873  9.11905  45.33418  1.000 76.20710  ? 421 ASP A OD2 1 
ATOM   2961 N  N   . PHE A 1 440 ? 18.56668  10.89781 41.64696  1.000 71.75628  ? 422 PHE A N   1 
ATOM   2962 C  CA  . PHE A 1 440 ? 18.89885  11.52076 40.37054  1.000 72.93384  ? 422 PHE A CA  1 
ATOM   2963 C  C   . PHE A 1 440 ? 20.09917  10.84153 39.72466  1.000 84.46906  ? 422 PHE A C   1 
ATOM   2964 O  O   . PHE A 1 440 ? 20.12615  10.64533 38.50267  1.000 74.77219  ? 422 PHE A O   1 
ATOM   2965 C  CB  . PHE A 1 440 ? 19.16885  13.01166 40.57698  1.000 65.52538  ? 422 PHE A CB  1 
ATOM   2966 C  CG  . PHE A 1 440 ? 19.63830  13.72684 39.34076  1.000 62.90877  ? 422 PHE A CG  1 
ATOM   2967 C  CD1 . PHE A 1 440 ? 18.77265  13.94940 38.28150  1.000 48.85599  ? 422 PHE A CD1 1 
ATOM   2968 C  CD2 . PHE A 1 440 ? 20.94282  14.19034 39.24606  1.000 56.62410  ? 422 PHE A CD2 1 
ATOM   2969 C  CE1 . PHE A 1 440 ? 19.19920  14.61203 37.14460  1.000 57.06820  ? 422 PHE A CE1 1 
ATOM   2970 C  CE2 . PHE A 1 440 ? 21.37743  14.85437 38.11211  1.000 61.51695  ? 422 PHE A CE2 1 
ATOM   2971 C  CZ  . PHE A 1 440 ? 20.50438  15.06440 37.05813  1.000 59.75095  ? 422 PHE A CZ  1 
ATOM   2972 N  N   . LYS A 1 441 ? 21.09604  10.46809 40.53373  1.000 77.83826  ? 423 LYS A N   1 
ATOM   2973 C  CA  . LYS A 1 441 ? 22.29588  9.83189  39.99949  1.000 74.49986  ? 423 LYS A CA  1 
ATOM   2974 C  C   . LYS A 1 441 ? 21.99224  8.44458  39.44561  1.000 77.84956  ? 423 LYS A C   1 
ATOM   2975 O  O   . LYS A 1 441 ? 22.49159  8.07587  38.37651  1.000 85.29922  ? 423 LYS A O   1 
ATOM   2976 C  CB  . LYS A 1 441 ? 23.37202  9.75402  41.08492  1.000 74.92588  ? 423 LYS A CB  1 
ATOM   2977 N  N   . LEU A 1 442 ? 21.17129  7.66486  40.15373  1.000 83.31189  ? 424 LEU A N   1 
ATOM   2978 C  CA  . LEU A 1 442 ? 20.88882  6.29720  39.72579  1.000 80.06806  ? 424 LEU A CA  1 
ATOM   2979 C  C   . LEU A 1 442 ? 20.06714  6.27621  38.44266  1.000 90.83973  ? 424 LEU A C   1 
ATOM   2980 O  O   . LEU A 1 442 ? 20.37099  5.51884  37.51306  1.000 94.66452  ? 424 LEU A O   1 
ATOM   2981 C  CB  . LEU A 1 442 ? 20.16948  5.53617  40.83961  1.000 86.96472  ? 424 LEU A CB  1 
ATOM   2982 N  N   . LYS A 1 443 ? 19.01757  7.10077  38.37264  1.000 88.78570  ? 425 LYS A N   1 
ATOM   2983 C  CA  . LYS A 1 443 ? 18.21258  7.15981  37.15678  1.000 86.22004  ? 425 LYS A CA  1 
ATOM   2984 C  C   . LYS A 1 443 ? 19.04697  7.58009  35.95444  1.000 83.70231  ? 425 LYS A C   1 
ATOM   2985 O  O   . LYS A 1 443 ? 18.75269  7.17741  34.82335  1.000 85.15886  ? 425 LYS A O   1 
ATOM   2986 C  CB  . LYS A 1 443 ? 17.03263  8.11494  37.34749  1.000 83.57264  ? 425 LYS A CB  1 
ATOM   2987 C  CG  . LYS A 1 443 ? 15.85772  7.51089  38.10043  1.000 81.31605  ? 425 LYS A CG  1 
ATOM   2988 N  N   . LEU A 1 444 ? 20.09749  8.37242  36.17825  1.000 84.59186  ? 426 LEU A N   1 
ATOM   2989 C  CA  . LEU A 1 444 ? 20.94686  8.80578  35.07425  1.000 87.21103  ? 426 LEU A CA  1 
ATOM   2990 C  C   . LEU A 1 444 ? 21.73549  7.64664  34.47510  1.000 93.09059  ? 426 LEU A C   1 
ATOM   2991 O  O   . LEU A 1 444 ? 22.00758  7.64590  33.26894  1.000 96.88800  ? 426 LEU A O   1 
ATOM   2992 C  CB  . LEU A 1 444 ? 21.89633  9.90569  35.54757  1.000 83.14399  ? 426 LEU A CB  1 
ATOM   2993 C  CG  . LEU A 1 444 ? 21.52782  11.33692 35.14935  1.000 84.18034  ? 426 LEU A CG  1 
ATOM   2994 C  CD1 . LEU A 1 444 ? 22.69421  12.28112 35.40672  1.000 76.58501  ? 426 LEU A CD1 1 
ATOM   2995 C  CD2 . LEU A 1 444 ? 21.08528  11.40289 33.69460  1.000 69.69306  ? 426 LEU A CD2 1 
ATOM   2996 N  N   . GLN A 1 445 ? 22.11146  6.65650  35.29120  1.000 85.28922  ? 427 GLN A N   1 
ATOM   2997 C  CA  . GLN A 1 445 ? 22.85061  5.51288  34.76359  1.000 89.87875  ? 427 GLN A CA  1 
ATOM   2998 C  C   . GLN A 1 445 ? 21.94646  4.58784  33.95677  1.000 95.11684  ? 427 GLN A C   1 
ATOM   2999 O  O   . GLN A 1 445 ? 22.35445  4.07822  32.90624  1.000 96.37718  ? 427 GLN A O   1 
ATOM   3000 C  CB  . GLN A 1 445 ? 23.52626  4.74196  35.89838  1.000 89.62810  ? 427 GLN A CB  1 
ATOM   3001 C  CG  . GLN A 1 445 ? 23.96456  5.59983  37.07008  1.000 90.16060  ? 427 GLN A CG  1 
ATOM   3002 N  N   . GLU A 1 446 ? 20.71621  4.35803  34.42787  1.000 96.94458  ? 428 GLU A N   1 
ATOM   3003 C  CA  . GLU A 1 446 ? 19.79499  3.48196  33.70895  1.000 91.02809  ? 428 GLU A CA  1 
ATOM   3004 C  C   . GLU A 1 446 ? 19.44471  4.01399  32.32636  1.000 94.17566  ? 428 GLU A C   1 
ATOM   3005 O  O   . GLU A 1 446 ? 19.07628  3.22696  31.44785  1.000 108.36941 ? 428 GLU A O   1 
ATOM   3006 C  CB  . GLU A 1 446 ? 18.51573  3.27024  34.51998  1.000 87.93283  ? 428 GLU A CB  1 
ATOM   3007 C  CG  . GLU A 1 446 ? 18.73441  3.17181  36.02043  1.000 95.90590  ? 428 GLU A CG  1 
ATOM   3008 C  CD  . GLU A 1 446 ? 17.44215  3.30401  36.80179  1.000 99.17601  ? 428 GLU A CD  1 
ATOM   3009 O  OE1 . GLU A 1 446 ? 16.37549  2.96249  36.24774  1.000 102.66226 ? 428 GLU A OE1 1 
ATOM   3010 O  OE2 . GLU A 1 446 ? 17.49208  3.74806  37.96867  1.000 104.91753 ? 428 GLU A OE2 1 
ATOM   3011 N  N   . GLU A 1 447 ? 19.54529  5.32647  32.11054  1.000 93.44793  ? 429 GLU A N   1 
ATOM   3012 C  CA  . GLU A 1 447 ? 19.35785  5.91304  30.78932  1.000 95.99556  ? 429 GLU A CA  1 
ATOM   3013 C  C   . GLU A 1 447 ? 20.67106  6.05631  30.02686  1.000 102.09143 ? 429 GLU A C   1 
ATOM   3014 O  O   . GLU A 1 447 ? 20.81804  6.98735  29.22274  1.000 106.71303 ? 429 GLU A O   1 
ATOM   3015 C  CB  . GLU A 1 447 ? 18.65396  7.26559  30.91009  1.000 87.06050  ? 429 GLU A CB  1 
ATOM   3016 C  CG  . GLU A 1 447 ? 17.42123  7.24937  31.80982  1.000 85.39568  ? 429 GLU A CG  1 
ATOM   3017 C  CD  . GLU A 1 447 ? 16.13614  6.93684  31.05733  1.000 88.97731  ? 429 GLU A CD  1 
ATOM   3018 O  OE1 . GLU A 1 447 ? 16.00167  7.36437  29.88880  1.000 82.38162  ? 429 GLU A OE1 1 
ATOM   3019 O  OE2 . GLU A 1 447 ? 15.25425  6.27090  31.64011  1.000 79.86280  ? 429 GLU A OE2 1 
ATOM   3020 N  N   . GLN A 1 448 ? 21.62477  5.15571  30.26506  1.000 100.17843 ? 430 GLN A N   1 
ATOM   3021 C  CA  . GLN A 1 448 ? 22.93156  5.16162  29.60445  1.000 105.32629 ? 430 GLN A CA  1 
ATOM   3022 C  C   . GLN A 1 448 ? 23.64770  6.49960  29.77026  1.000 109.72436 ? 430 GLN A C   1 
ATOM   3023 O  O   . GLN A 1 448 ? 24.41322  6.69042  30.71573  1.000 107.48555 ? 430 GLN A O   1 
ATOM   3024 C  CB  . GLN A 1 448 ? 22.78793  4.82152  28.11721  1.000 92.55793  ? 430 GLN A CB  1 
HETATM 3025 P  P   . PO4 B 2 .   ? 5.51380   19.61197 20.95264  1.000 111.50541 ? 501 PO4 A P   1 
HETATM 3026 O  O1  . PO4 B 2 .   ? 5.69732   19.72239 19.45569  1.000 85.25294  ? 501 PO4 A O1  1 
HETATM 3027 O  O2  . PO4 B 2 .   ? 4.09845   20.00078 21.30634  1.000 83.82263  ? 501 PO4 A O2  1 
HETATM 3028 O  O3  . PO4 B 2 .   ? 5.76586   18.18791 21.39329  1.000 90.59290  ? 501 PO4 A O3  1 
HETATM 3029 O  O4  . PO4 B 2 .   ? 6.48120   20.53459 21.66173  1.000 86.08998  ? 501 PO4 A O4  1 
HETATM 3030 P  P   . PO4 C 2 .   ? -0.06676  34.46998 62.02962  0.50  132.94876 ? 502 PO4 A P   1 
HETATM 3031 O  O1  . PO4 C 2 .   ? 0.38329   35.21311 60.79301  0.617 120.03177 ? 502 PO4 A O1  1 
HETATM 3032 O  O2  . PO4 C 2 .   ? -0.59611  35.45352 63.04765  0.617 121.57588 ? 502 PO4 A O2  1 
HETATM 3033 O  O3  . PO4 C 2 .   ? -1.16094  33.49418 61.66234  0.617 118.23112 ? 502 PO4 A O3  1 
HETATM 3034 O  O4  . PO4 C 2 .   ? 1.10640   33.71852 62.61556  0.617 118.28567 ? 502 PO4 A O4  1 
HETATM 3035 ZN ZN  . ZN  D 3 .   ? 0.82485   21.93872 25.83055  0.436 41.61438  ? 503 ZN  A ZN  1 
HETATM 3036 ZN ZN  . ZN  E 3 .   ? 1.83642   22.39162 27.96592  0.600 37.59260  ? 504 ZN  A ZN  1 
HETATM 3037 O  O   . HOH F 4 .   ? 26.87586  22.22256 38.16044  1.000 72.22584  ? 601 HOH A O   1 
HETATM 3038 O  O   . HOH F 4 .   ? 18.30166  39.64826 47.74144  1.000 66.37782  ? 602 HOH A O   1 
HETATM 3039 O  O   . HOH F 4 .   ? 20.01371  11.09444 1.88993   1.000 58.00102  ? 603 HOH A O   1 
HETATM 3040 O  O   . HOH F 4 .   ? -4.29345  22.06659 43.16239  1.000 62.34587  ? 604 HOH A O   1 
HETATM 3041 O  O   . HOH F 4 .   ? 8.62882   0.56193  25.72283  1.000 56.82200  ? 605 HOH A O   1 
HETATM 3042 O  O   . HOH F 4 .   ? -5.88131  20.31457 41.84413  1.000 58.01585  ? 606 HOH A O   1 
HETATM 3043 O  O   . HOH F 4 .   ? 17.41534  8.39566  10.85627  1.000 60.18165  ? 607 HOH A O   1 
HETATM 3044 O  O   . HOH F 4 .   ? 22.25929  27.87600 36.88023  1.000 50.29109  ? 608 HOH A O   1 
HETATM 3045 O  O   . HOH F 4 .   ? -11.05519 30.85915 42.28686  1.000 65.98807  ? 609 HOH A O   1 
HETATM 3046 O  O   . HOH F 4 .   ? 6.84545   16.66468 52.36264  1.000 64.36955  ? 610 HOH A O   1 
HETATM 3047 O  O   . HOH F 4 .   ? 6.58364   29.30955 27.30919  1.000 41.84348  ? 611 HOH A O   1 
HETATM 3048 O  O   . HOH F 4 .   ? 3.49442   28.14473 21.19325  1.000 48.72183  ? 612 HOH A O   1 
HETATM 3049 O  O   . HOH F 4 .   ? -7.85205  31.22611 35.44270  1.000 56.71358  ? 613 HOH A O   1 
HETATM 3050 O  O   . HOH F 4 .   ? -0.21916  41.18147 38.37362  1.000 58.69446  ? 614 HOH A O   1 
HETATM 3051 O  O   . HOH F 4 .   ? 2.20491   -5.42123 9.58374   1.000 47.68931  ? 615 HOH A O   1 
HETATM 3052 O  O   . HOH F 4 .   ? 12.50779  34.68787 22.85293  1.000 59.49955  ? 616 HOH A O   1 
HETATM 3053 O  O   . HOH F 4 .   ? 3.84687   22.60251 28.87907  1.000 47.36815  ? 617 HOH A O   1 
HETATM 3054 O  O   . HOH F 4 .   ? 9.87187   26.19101 27.14547  1.000 43.15884  ? 618 HOH A O   1 
HETATM 3055 O  O   . HOH F 4 .   ? 0.65308   2.75245  15.37595  1.000 49.21577  ? 619 HOH A O   1 
HETATM 3056 O  O   . HOH F 4 .   ? 9.46162   6.46034  -9.75670  1.000 43.36732  ? 620 HOH A O   1 
HETATM 3057 O  O   . HOH F 4 .   ? -15.62498 24.78471 21.31700  1.000 83.03942  ? 621 HOH A O   1 
HETATM 3058 O  O   . HOH F 4 .   ? -6.05284  34.53983 41.93818  1.000 62.26882  ? 622 HOH A O   1 
HETATM 3059 O  O   . HOH F 4 .   ? 6.35516   21.36676 30.65600  1.000 52.21739  ? 623 HOH A O   1 
HETATM 3060 O  O   . HOH F 4 .   ? 5.97006   30.86938 16.65025  1.000 65.74073  ? 624 HOH A O   1 
HETATM 3061 O  O   . HOH F 4 .   ? -1.71250  27.28112 26.95272  1.000 48.47909  ? 625 HOH A O   1 
HETATM 3062 O  O   . HOH F 4 .   ? 2.77210   21.03911 26.77207  1.000 43.60609  ? 626 HOH A O   1 
HETATM 3063 O  O   . HOH F 4 .   ? -0.04926  26.48277 25.06825  1.000 51.94362  ? 627 HOH A O   1 
HETATM 3064 O  O   . HOH F 4 .   ? 9.14022   14.87749 27.23465  1.000 49.03524  ? 628 HOH A O   1 
HETATM 3065 O  O   . HOH F 4 .   ? 5.48723   18.61208 -5.84229  1.000 61.20216  ? 629 HOH A O   1 
HETATM 3066 O  O   . HOH F 4 .   ? 14.10871  -1.27484 21.95692  1.000 62.30947  ? 630 HOH A O   1 
HETATM 3067 O  O   . HOH F 4 .   ? 0.80602   34.18854 25.49756  1.000 52.05723  ? 631 HOH A O   1 
HETATM 3068 O  O   . HOH F 4 .   ? 6.08018   19.92425 57.52019  1.000 65.53352  ? 632 HOH A O   1 
HETATM 3069 O  O   . HOH F 4 .   ? 21.35825  19.10541 43.26080  1.000 56.47834  ? 633 HOH A O   1 
HETATM 3070 O  O   . HOH F 4 .   ? 1.56128   5.64695  16.66381  1.000 46.15741  ? 634 HOH A O   1 
HETATM 3071 O  O   . HOH F 4 .   ? 5.44253   26.41765 36.92881  1.000 40.19093  ? 635 HOH A O   1 
HETATM 3072 O  O   . HOH F 4 .   ? -0.44748  9.45240  9.46666   1.000 59.15459  ? 636 HOH A O   1 
HETATM 3073 O  O   . HOH F 4 .   ? -7.04927  33.99224 34.57628  1.000 58.73821  ? 637 HOH A O   1 
HETATM 3074 O  O   . HOH F 4 .   ? -5.22133  26.47298 48.79355  1.000 71.62615  ? 638 HOH A O   1 
HETATM 3075 O  O   . HOH F 4 .   ? 25.51239  24.60592 27.80426  1.000 57.98229  ? 639 HOH A O   1 
HETATM 3076 O  O   . HOH F 4 .   ? 25.91115  24.55368 42.97498  1.000 81.42111  ? 640 HOH A O   1 
HETATM 3077 O  O   . HOH F 4 .   ? 1.85662   7.14596  9.24948   1.000 47.40569  ? 641 HOH A O   1 
HETATM 3078 O  O   . HOH F 4 .   ? 26.91537  23.65119 40.13221  1.000 70.27886  ? 642 HOH A O   1 
HETATM 3079 O  O   . HOH F 4 .   ? 19.61435  17.81513 28.66686  1.000 58.17527  ? 643 HOH A O   1 
HETATM 3080 O  O   . HOH F 4 .   ? 0.48537   4.97430  9.14059   1.000 37.61855  ? 644 HOH A O   1 
HETATM 3081 O  O   . HOH F 4 .   ? 1.49642   9.47763  28.91681  1.000 77.64033  ? 645 HOH A O   1 
HETATM 3082 O  O   . HOH F 4 .   ? 2.91218   17.70362 -9.98532  1.000 62.00525  ? 646 HOH A O   1 
HETATM 3083 O  O   . HOH F 4 .   ? -8.70408  18.56847 42.44567  1.000 78.11314  ? 647 HOH A O   1 
HETATM 3084 O  O   . HOH F 4 .   ? 2.08679   24.11561 64.33534  1.000 81.73908  ? 648 HOH A O   1 
HETATM 3085 O  O   . HOH F 4 .   ? -13.54382 22.09683 22.89754  1.000 65.37152  ? 649 HOH A O   1 
HETATM 3086 O  O   . HOH F 4 .   ? -12.42344 28.99019 24.03920  1.000 65.09838  ? 650 HOH A O   1 
HETATM 3087 O  O   . HOH F 4 .   ? 7.90931   38.80914 46.72994  1.000 62.18511  ? 651 HOH A O   1 
HETATM 3088 O  O   . HOH F 4 .   ? 8.28752   -2.00806 7.38618   1.000 38.32585  ? 652 HOH A O   1 
HETATM 3089 O  O   . HOH F 4 .   ? -0.87318  18.60577 2.78424   1.000 62.11690  ? 653 HOH A O   1 
HETATM 3090 O  O   . HOH F 4 .   ? 19.10712  9.41596  -1.49004  1.000 54.62722  ? 654 HOH A O   1 
HETATM 3091 O  O   . HOH F 4 .   ? 22.64545  24.45534 31.64399  1.000 55.17445  ? 655 HOH A O   1 
HETATM 3092 O  O   . HOH F 4 .   ? -11.27022 22.25202 20.04888  1.000 57.10806  ? 656 HOH A O   1 
HETATM 3093 O  O   . HOH F 4 .   ? 5.56745   0.00000  0.00000   0.50  40.02893  ? 657 HOH A O   1 
HETATM 3094 O  O   . HOH F 4 .   ? -10.68774 29.06800 22.26670  1.000 73.53266  ? 658 HOH A O   1 
HETATM 3095 O  O   . HOH F 4 .   ? 16.71146  11.22768 11.66805  1.000 53.48814  ? 659 HOH A O   1 
HETATM 3096 O  O   . HOH F 4 .   ? 28.65833  25.49840 55.40033  1.000 106.11798 ? 660 HOH A O   1 
HETATM 3097 O  O   . HOH F 4 .   ? 19.41839  18.83623 26.03449  1.000 50.00674  ? 661 HOH A O   1 
HETATM 3098 O  O   . HOH F 4 .   ? 24.67772  30.73055 38.93744  1.000 65.45112  ? 662 HOH A O   1 
HETATM 3099 O  O   . HOH F 4 .   ? 17.63724  10.18947 -8.39522  1.000 58.31509  ? 663 HOH A O   1 
HETATM 3100 O  O   . HOH F 4 .   ? 19.67204  12.10957 4.10775   1.000 52.87418  ? 664 HOH A O   1 
HETATM 3101 O  O   . HOH F 4 .   ? -2.29088  40.95043 45.64880  1.000 53.59838  ? 665 HOH A O   1 
HETATM 3102 O  O   . HOH F 4 .   ? 2.89135   44.15430 37.70991  1.000 58.32154  ? 666 HOH A O   1 
HETATM 3103 O  O   . HOH F 4 .   ? 28.44225  24.33383 37.74130  1.000 72.82748  ? 667 HOH A O   1 
HETATM 3104 O  O   . HOH F 4 .   ? -8.49527  17.02330 44.86444  1.000 73.48162  ? 668 HOH A O   1 
HETATM 3105 O  O   . HOH F 4 .   ? 2.48565   35.65021 18.49831  1.000 59.85949  ? 669 HOH A O   1 
HETATM 3106 O  O   . HOH F 4 .   ? -2.55826  20.37350 19.52006  1.000 70.46521  ? 670 HOH A O   1 
HETATM 3107 O  O   . HOH F 4 .   ? 17.05308  44.38529 39.18837  1.000 68.31013  ? 671 HOH A O   1 
HETATM 3108 O  O   . HOH F 4 .   ? -1.19515  5.94390  17.28053  1.000 58.72139  ? 672 HOH A O   1 
HETATM 3109 O  O   . HOH F 4 .   ? 9.02259   20.78353 18.56715  1.000 66.22354  ? 673 HOH A O   1 
HETATM 3110 O  O   . HOH F 4 .   ? 23.42344  36.85392 57.51965  1.000 82.13748  ? 674 HOH A O   1 
HETATM 3111 O  O   . HOH F 4 .   ? 9.61108   -5.01003 11.86431  1.000 53.74981  ? 675 HOH A O   1 
HETATM 3112 O  O   . HOH F 4 .   ? 19.26020  16.25091 -0.38107  1.000 62.82790  ? 676 HOH A O   1 
HETATM 3113 O  O   . HOH F 4 .   ? 27.80500  21.29780 36.04494  1.000 75.80275  ? 677 HOH A O   1 
HETATM 3114 O  O   . HOH F 4 .   ? 11.76921  -3.27513 10.81017  1.000 54.37225  ? 678 HOH A O   1 
HETATM 3115 O  O   . HOH F 4 .   ? 0.30178   41.55305 35.84347  1.000 63.68881  ? 679 HOH A O   1 
HETATM 3116 O  O   . HOH F 4 .   ? 21.50159  20.18310 24.82028  1.000 69.33694  ? 680 HOH A O   1 
HETATM 3117 O  O   . HOH F 4 .   ? 1.68711   42.44835 39.96105  1.000 58.14255  ? 681 HOH A O   1 
HETATM 3118 O  O   . HOH F 4 .   ? 15.25470  39.26641 53.87958  1.000 65.58824  ? 682 HOH A O   1 
HETATM 3119 O  O   . HOH F 4 .   ? 4.12045   33.50418 15.66857  1.000 71.71621  ? 683 HOH A O   1 
HETATM 3120 O  O   . HOH F 4 .   ? 7.05722   9.62541  41.68688  1.000 72.06111  ? 684 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . LEU A 32  ? 1.14796 1.05499 0.50076 -0.31213 0.08356  -0.09755 14  LEU A N   
2    C  CA  . LEU A 32  ? 1.65405 1.57348 0.98891 -0.34603 0.11039  -0.11196 14  LEU A CA  
3    C  C   . LEU A 32  ? 1.62464 1.58970 1.00068 -0.34146 0.12098  -0.12937 14  LEU A C   
4    O  O   . LEU A 32  ? 1.57490 1.57697 1.01298 -0.31499 0.11593  -0.13398 14  LEU A O   
5    C  CB  . LEU A 32  ? 1.40119 1.25761 0.64155 -0.37317 0.10737  -0.10332 14  LEU A CB  
6    C  CG  . LEU A 32  ? 1.61072 1.40536 0.79293 -0.37634 0.09169  -0.08385 14  LEU A CG  
7    N  N   . TYR A 33  ? 1.48870 1.44810 0.82634 -0.36899 0.13630  -0.13940 15  TYR A N   
8    C  CA  . TYR A 33  ? 1.62232 1.62037 0.99026 -0.36838 0.14774  -0.15704 15  TYR A CA  
9    C  C   . TYR A 33  ? 1.73253 1.70876 1.08049 -0.34954 0.12472  -0.14941 15  TYR A C   
10   O  O   . TYR A 33  ? 1.68609 1.64889 0.99516 -0.36356 0.12724  -0.15440 15  TYR A O   
11   C  CB  . TYR A 33  ? 1.51193 1.51446 0.85436 -0.40408 0.17253  -0.17079 15  TYR A CB  
12   C  CG  . TYR A 33  ? 1.33529 1.34282 0.68287 -0.42637 0.18930  -0.17347 15  TYR A CG  
13   C  CD1 . TYR A 33  ? 1.32425 1.38959 0.73644 -0.42432 0.20741  -0.19100 15  TYR A CD1 
14   C  CD2 . TYR A 33  ? 1.37131 1.32521 0.65977 -0.44901 0.18607  -0.15967 15  TYR A CD2 
15   C  CE1 . TYR A 33  ? 1.34616 1.42020 0.76605 -0.44477 0.22152  -0.19563 15  TYR A CE1 
16   C  CE2 . TYR A 33  ? 1.42934 1.38869 0.72293 -0.47175 0.20157  -0.16398 15  TYR A CE2 
17   C  CZ  . TYR A 33  ? 1.38320 1.40498 0.74366 -0.46982 0.21916  -0.18249 15  TYR A CZ  
18   O  OH  . TYR A 33  ? 1.50740 1.53836 0.87545 -0.49230 0.23325  -0.18893 15  TYR A OH  
19   N  N   . PHE A 34  ? 1.63657 1.61144 1.01248 -0.31777 0.10211  -0.13846 16  PHE A N   
20   C  CA  . PHE A 34  ? 1.64861 1.60664 1.01057 -0.29712 0.07760  -0.13208 16  PHE A CA  
21   C  C   . PHE A 34  ? 1.55764 1.56203 0.99332 -0.26995 0.07446  -0.14012 16  PHE A C   
22   O  O   . PHE A 34  ? 1.51157 1.54418 1.00061 -0.25858 0.08025  -0.14182 16  PHE A O   
23   C  CB  . PHE A 34  ? 1.66492 1.57162 0.98131 -0.28459 0.04987  -0.11217 16  PHE A CB  
24   C  CG  . PHE A 34  ? 1.77684 1.62387 1.00471 -0.30972 0.04727  -0.10287 16  PHE A CG  
25   C  CD1 . PHE A 34  ? 1.70245 1.53022 0.90357 -0.33427 0.06238  -0.09914 16  PHE A CD1 
26   C  CD2 . PHE A 34  ? 1.76095 1.56924 0.92935 -0.30993 0.02962  -0.09849 16  PHE A CD2 
27   C  CE1 . PHE A 34  ? 1.62861 1.39816 0.75453 -0.35676 0.06032  -0.08920 16  PHE A CE1 
28   C  CE2 . PHE A 34  ? 1.67681 1.42614 0.77129 -0.32956 0.02611  -0.08767 16  PHE A CE2 
29   C  CZ  . PHE A 34  ? 1.63867 1.36857 0.71773 -0.35195 0.04173  -0.08217 16  PHE A CZ  
30   N  N   . GLN A 35  ? 1.51699 1.52682 0.95195 -0.26093 0.06525  -0.14539 17  GLN A N   
31   C  CA  . GLN A 35  ? 1.54110 1.59062 1.03801 -0.23916 0.06330  -0.15441 17  GLN A CA  
32   C  C   . GLN A 35  ? 1.49736 1.54956 1.02655 -0.21342 0.04589  -0.14459 17  GLN A C   
33   O  O   . GLN A 35  ? 1.56096 1.58753 1.06386 -0.20031 0.02199  -0.13420 17  GLN A O   
34   C  CB  . GLN A 35  ? 1.30040 1.34892 0.78075 -0.23579 0.05350  -0.16059 17  GLN A CB  
35   N  N   . GLY A 36  ? 1.43980 1.52258 1.02470 -0.20558 0.05707  -0.14887 18  GLY A N   
36   C  CA  . GLY A 36  ? 1.40504 1.49332 1.02351 -0.18295 0.04331  -0.14122 18  GLY A CA  
37   C  C   . GLY A 36  ? 1.29235 1.34984 0.88394 -0.18134 0.03189  -0.12540 18  GLY A C   
38   O  O   . GLY A 36  ? 1.29481 1.34138 0.88714 -0.16260 0.01121  -0.11708 18  GLY A O   
39   N  N   . SER A 37  ? 1.33039 1.37438 0.89804 -0.20121 0.04524  -0.12254 19  SER A N   
40   C  CA  . SER A 37  ? 1.28308 1.29465 0.82223 -0.20211 0.03603  -0.10781 19  SER A CA  
41   C  C   . SER A 37  ? 1.10111 1.13421 0.69243 -0.18614 0.03607  -0.10511 19  SER A C   
42   O  O   . SER A 37  ? 1.04568 1.11694 0.69012 -0.18128 0.04911  -0.11534 19  SER A O   
43   C  CB  . SER A 37  ? 1.23484 1.22686 0.73197 -0.23217 0.05292  -0.10746 19  SER A CB  
44   N  N   . LEU A 38  ? 1.00737 1.01249 0.58022 -0.17723 0.02023  -0.09133 20  LEU A N   
45   C  CA  . LEU A 38  ? 1.02635 1.04754 0.64216 -0.16485 0.02076  -0.08777 20  LEU A CA  
46   C  C   . LEU A 38  ? 1.05112 1.09037 0.68474 -0.18241 0.04394  -0.09318 20  LEU A C   
47   O  O   . LEU A 38  ? 0.97320 1.04350 0.65845 -0.17329 0.05136  -0.09804 20  LEU A O   
48   C  CB  . LEU A 38  ? 0.87599 0.86048 0.46268 -0.15382 -0.00019 -0.07271 20  LEU A CB  
49   C  CG  . LEU A 38  ? 1.07890 1.07143 0.69877 -0.14360 -0.00079 -0.06691 20  LEU A CG  
50   C  CD1 . LEU A 38  ? 0.91106 0.94141 0.59209 -0.12268 -0.00295 -0.07335 20  LEU A CD1 
51   C  CD2 . LEU A 38  ? 1.09997 1.04876 0.67895 -0.13591 -0.02111 -0.05264 20  LEU A CD2 
52   N  N   . GLU A 39  ? 0.92531 0.94572 0.51534 -0.20828 0.05548  -0.09374 21  GLU A N   
53   C  CA  . GLU A 39  ? 1.04518 1.08980 0.65382 -0.22706 0.07897  -0.10329 21  GLU A CA  
54   C  C   . GLU A 39  ? 0.97857 1.07155 0.63876 -0.22414 0.09468  -0.12157 21  GLU A C   
55   O  O   . GLU A 39  ? 0.93997 1.06528 0.64130 -0.22483 0.10829  -0.13101 21  GLU A O   
56   C  CB  . GLU A 39  ? 0.95784 0.97340 0.50557 -0.25907 0.08987  -0.10290 21  GLU A CB  
57   N  N   . LEU A 40  ? 0.97893 1.07652 0.63689 -0.21971 0.09190  -0.12754 22  LEU A N   
58   C  CA  . LEU A 40  ? 0.99525 1.13377 0.69867 -0.21570 0.10562  -0.14510 22  LEU A CA  
59   C  C   . LEU A 40  ? 0.98189 1.14161 0.73977 -0.18943 0.09834  -0.14533 22  LEU A C   
60   O  O   . LEU A 40  ? 0.95054 1.14173 0.75163 -0.18456 0.11013  -0.15769 22  LEU A O   
61   C  CB  . LEU A 40  ? 0.92068 1.05512 0.60144 -0.22094 0.10539  -0.15161 22  LEU A CB  
62   C  CG  . LEU A 40  ? 1.14863 1.27281 0.78404 -0.25047 0.12004  -0.15826 22  LEU A CG  
63   N  N   . LEU A 41  ? 0.84072 0.98278 0.59555 -0.17229 0.07861  -0.13295 23  LEU A N   
64   C  CA  . LEU A 41  ? 0.92496 1.08360 0.72634 -0.15057 0.07249  -0.13270 23  LEU A CA  
65   C  C   . LEU A 41  ? 0.81290 0.98054 0.63924 -0.14826 0.07772  -0.13004 23  LEU A C   
66   O  O   . LEU A 41  ? 0.70895 0.89855 0.57787 -0.13651 0.08199  -0.13651 23  LEU A O   
67   C  CB  . LEU A 41  ? 0.82266 0.96343 0.61431 -0.13511 0.05114  -0.12208 23  LEU A CB  
68   C  CG  . LEU A 41  ? 1.00471 1.13943 0.77511 -0.13409 0.04252  -0.12557 23  LEU A CG  
69   C  CD1 . LEU A 41  ? 1.01953 1.14067 0.78282 -0.11769 0.02020  -0.11701 23  LEU A CD1 
70   C  CD2 . LEU A 41  ? 0.99761 1.15926 0.80058 -0.13132 0.05274  -0.14024 23  LEU A CD2 
71   N  N   . LYS A 42  ? 0.82048 0.96847 0.61766 -0.15963 0.07675  -0.12065 24  LYS A N   
72   C  CA  . LYS A 42  ? 0.79086 0.94849 0.60922 -0.16020 0.08260  -0.11919 24  LYS A CA  
73   C  C   . LYS A 42  ? 0.83506 1.02776 0.68386 -0.16807 0.10214  -0.13669 24  LYS A C   
74   O  O   . LYS A 42  ? 0.79668 1.01036 0.68469 -0.15768 0.10504  -0.14112 24  LYS A O   
75   C  CB  . LYS A 42  ? 0.76867 0.89545 0.54285 -0.17511 0.07956  -0.10731 24  LYS A CB  
76   C  CG  . LYS A 42  ? 0.79383 0.88776 0.54621 -0.16143 0.05786  -0.09070 24  LYS A CG  
77   C  CD  . LYS A 42  ? 0.82009 0.87725 0.52424 -0.17582 0.05434  -0.07902 24  LYS A CD  
78   C  CE  . LYS A 42  ? 0.83955 0.86466 0.52457 -0.15845 0.03105  -0.06429 24  LYS A CE  
79   N  NZ  . LYS A 42  ? 0.87976 0.86525 0.51889 -0.17032 0.02682  -0.05252 24  LYS A NZ  
80   N  N   . LEU A 43  ? 0.79657 0.99648 0.62750 -0.18558 0.11496  -0.14806 25  LEU A N   
81   C  CA  . LEU A 43  ? 0.81508 1.05267 0.67753 -0.19120 0.13313  -0.16842 25  LEU A CA  
82   C  C   . LEU A 43  ? 0.74306 1.00187 0.65056 -0.16860 0.13103  -0.17763 25  LEU A C   
83   O  O   . LEU A 43  ? 0.72469 1.01051 0.67070 -0.16020 0.13753  -0.18941 25  LEU A O   
84   C  CB  . LEU A 43  ? 0.79381 1.03409 0.62572 -0.21511 0.14736  -0.17973 25  LEU A CB  
85   C  CG  . LEU A 43  ? 0.80678 1.08956 0.67158 -0.22020 0.16633  -0.20470 25  LEU A CG  
86   C  CD1 . LEU A 43  ? 0.65000 0.95736 0.53148 -0.23126 0.17848  -0.21413 25  LEU A CD1 
87   C  CD2 . LEU A 43  ? 0.76688 1.04931 0.60094 -0.24046 0.17795  -0.21523 25  LEU A CD2 
88   N  N   . ARG A 44  ? 0.59032 0.83574 0.49142 -0.15869 0.12137  -0.17330 26  ARG A N   
89   C  CA  . ARG A 44  ? 0.84769 1.10620 0.78464 -0.13957 0.11937  -0.18127 26  ARG A CA  
90   C  C   . ARG A 44  ? 0.72650 0.98740 0.69499 -0.12176 0.11209  -0.17574 26  ARG A C   
91   O  O   . ARG A 44  ? 0.68849 0.96662 0.68996 -0.11002 0.11627  -0.18710 26  ARG A O   
92   C  CB  . ARG A 44  ? 0.80522 1.04725 0.72687 -0.13427 0.10921  -0.17621 26  ARG A CB  
93   C  CG  . ARG A 44  ? 0.87698 1.13215 0.81950 -0.12672 0.11464  -0.19085 26  ARG A CG  
94   C  CD  . ARG A 44  ? 0.91118 1.15299 0.83306 -0.12725 0.10676  -0.18817 26  ARG A CD  
95   N  N   . SER A 45  ? 0.65803 0.89983 0.61467 -0.11901 0.10048  -0.15888 27  SER A N   
96   C  CA  . SER A 45  ? 0.70338 0.94544 0.68674 -0.10344 0.09340  -0.15287 27  SER A CA  
97   C  C   . SER A 45  ? 0.66879 0.93224 0.67501 -0.10463 0.10253  -0.16153 27  SER A C   
98   O  O   . SER A 45  ? 0.62174 0.89357 0.65817 -0.08933 0.10012  -0.16506 27  SER A O   
99   C  CB  . SER A 45  ? 0.54824 0.76689 0.51249 -0.10167 0.07994  -0.13466 27  SER A CB  
100  O  OG  . SER A 45  ? 0.64566 0.85790 0.58830 -0.11580 0.08295  -0.12904 27  SER A OG  
101  N  N   . ALA A 46  ? 0.66746 0.93955 0.65787 -0.12342 0.11281  -0.16602 28  ALA A N   
102  C  CA  . ALA A 46  ? 0.68039 0.97996 0.69489 -0.12637 0.12269  -0.17826 28  ALA A CA  
103  C  C   . ALA A 46  ? 0.67397 1.00265 0.71938 -0.11807 0.13143  -0.20013 28  ALA A C   
104  O  O   . ALA A 46  ? 0.68541 1.03488 0.76390 -0.10565 0.13199  -0.21032 28  ALA A O   
105  C  CB  . ALA A 46  ? 0.51681 0.81839 0.50330 -0.15259 0.13335  -0.17943 28  ALA A CB  
106  N  N   . GLU A 47  ? 0.59191 0.92152 0.62598 -0.12365 0.13727  -0.20838 29  GLU A N   
107  C  CA  . GLU A 47  ? 0.61930 0.97248 0.68080 -0.11360 0.14423  -0.22947 29  GLU A CA  
108  C  C   . GLU A 47  ? 0.62607 0.96807 0.71054 -0.08784 0.13261  -0.22707 29  GLU A C   
109  O  O   . GLU A 47  ? 0.65874 1.01762 0.77265 -0.07272 0.13361  -0.24211 29  GLU A O   
110  C  CB  . GLU A 47  ? 0.57490 0.92736 0.61535 -0.12611 0.15247  -0.23732 29  GLU A CB  
111  C  CG  . GLU A 47  ? 0.74019 1.10955 0.76147 -0.15242 0.16810  -0.24751 29  GLU A CG  
112  C  CD  . GLU A 47  ? 0.87305 1.23387 0.86490 -0.16643 0.17419  -0.25103 29  GLU A CD  
113  O  OE1 . GLU A 47  ? 0.92301 1.26148 0.90475 -0.15715 0.16414  -0.24157 29  GLU A OE1 
114  O  OE2 . GLU A 47  ? 0.83730 1.21488 0.81572 -0.18783 0.18947  -0.26438 29  GLU A OE2 
115  N  N   A CYS A 48  ? 0.62878 0.94146 0.69836 -0.08272 0.12114  -0.20950 30  CYS A N   
116  N  N   B CYS A 48  ? 0.62990 0.94255 0.69929 -0.08284 0.12118  -0.20949 30  CYS A N   
117  C  CA  A CYS A 48  ? 0.61376 0.91189 0.69935 -0.06241 0.11146  -0.20691 30  CYS A CA  
118  C  CA  B CYS A 48  ? 0.61706 0.91472 0.70203 -0.06265 0.11130  -0.20644 30  CYS A CA  
119  C  C   A CYS A 48  ? 0.64361 0.94427 0.75097 -0.04923 0.10525  -0.20398 30  CYS A C   
120  C  C   B CYS A 48  ? 0.64020 0.94086 0.74739 -0.04935 0.10529  -0.20396 30  CYS A C   
121  O  O   A CYS A 48  ? 0.63823 0.93322 0.76298 -0.03154 0.10022  -0.20944 30  CYS A O   
122  O  O   B CYS A 48  ? 0.63349 0.92895 0.75829 -0.03170 0.10045  -0.20978 30  CYS A O   
123  C  CB  A CYS A 48  ? 0.62474 0.89627 0.69016 -0.06307 0.10198  -0.19102 30  CYS A CB  
124  C  CB  B CYS A 48  ? 0.62548 0.89661 0.68978 -0.06373 0.10170  -0.19001 30  CYS A CB  
125  S  SG  A CYS A 48  ? 0.68228 0.94874 0.72878 -0.07092 0.10598  -0.19777 30  CYS A SG  
126  S  SG  B CYS A 48  ? 0.52523 0.77441 0.60173 -0.04517 0.09088  -0.18453 30  CYS A SG  
127  N  N   . ILE A 49  ? 0.56159 0.86763 0.66515 -0.05783 0.10501  -0.19556 31  ILE A N   
128  C  CA  . ILE A 49  ? 0.59201 0.90275 0.71609 -0.04643 0.09930  -0.19357 31  ILE A CA  
129  C  C   . ILE A 49  ? 0.64034 0.98360 0.79169 -0.04058 0.10624  -0.21525 31  ILE A C   
130  O  O   . ILE A 49  ? 0.55127 0.89692 0.72487 -0.02171 0.09934  -0.22084 31  ILE A O   
131  C  CB  . ILE A 49  ? 0.55859 0.86267 0.66787 -0.05820 0.09663  -0.17776 31  ILE A CB  
132  C  CG1 . ILE A 49  ? 0.53010 0.80318 0.62254 -0.05442 0.08514  -0.15841 31  ILE A CG1 
133  C  CG2 . ILE A 49  ? 0.52407 0.84402 0.65532 -0.05224 0.09521  -0.18099 31  ILE A CG2 
134  C  CD1 . ILE A 49  ? 0.47916 0.74004 0.54850 -0.06667 0.08184  -0.14321 31  ILE A CD1 
135  N  N   . ASP A 50  ? 0.65446 1.02340 0.80360 -0.05633 0.11950  -0.22928 32  ASP A N   
136  C  CA  . ASP A 50  ? 0.67053 1.07722 0.84879 -0.05091 0.12689  -0.25418 32  ASP A CA  
137  C  C   . ASP A 50  ? 0.68402 1.08937 0.87987 -0.02862 0.12282  -0.26854 32  ASP A C   
138  O  O   . ASP A 50  ? 0.68686 1.10964 0.91055 -0.01012 0.11863  -0.28383 32  ASP A O   
139  C  CB  . ASP A 50  ? 0.57907 1.01334 0.74812 -0.07588 0.14397  -0.26765 32  ASP A CB  
140  C  CG  . ASP A 50  ? 0.72258 1.16214 0.87736 -0.09741 0.14905  -0.25929 32  ASP A CG  
141  O  OD1 . ASP A 50  ? 0.67073 1.10997 0.83780 -0.08966 0.14132  -0.25223 32  ASP A OD1 
142  O  OD2 . ASP A 50  ? 0.75830 1.19948 0.88636 -0.12298 0.16078  -0.25985 32  ASP A OD2 
143  N  N   . GLU A 51  ? 0.61283 0.99594 0.79107 -0.02945 0.12298  -0.26452 33  GLU A N   
144  C  CA  . GLU A 51  ? 0.67390 1.04792 0.86257 -0.00967 0.11898  -0.27686 33  GLU A CA  
145  C  C   . GLU A 51  ? 0.59134 0.93910 0.78778 0.01328  0.10371  -0.26891 33  GLU A C   
146  O  O   . GLU A 51  ? 0.64023 0.98549 0.85112 0.03413  0.09835  -0.28330 33  GLU A O   
147  C  CB  . GLU A 51  ? 0.62830 0.98097 0.79288 -0.01832 0.12217  -0.27189 33  GLU A CB  
148  C  CG  . GLU A 51  ? 0.75933 1.08455 0.92366 0.00008  0.11486  -0.27533 33  GLU A CG  
149  C  CD  . GLU A 51  ? 1.02095 1.30802 1.16787 0.00199  0.10441  -0.25354 33  GLU A CD  
150  O  OE1 . GLU A 51  ? 1.00008 1.28286 1.13288 -0.01189 0.10347  -0.23653 33  GLU A OE1 
151  O  OE2 . GLU A 51  ? 1.03701 1.29733 1.18277 0.01713  0.09704  -0.25453 33  GLU A OE2 
152  N  N   . ALA A 52  ? 0.65920 0.98506 0.84388 0.01011  0.09609  -0.24690 34  ALA A N   
153  C  CA  . ALA A 52  ? 0.68771 0.98527 0.87445 0.02824  0.08253  -0.23780 34  ALA A CA  
154  C  C   . ALA A 52  ? 0.62741 0.94068 0.83396 0.03781  0.07651  -0.23955 34  ALA A C   
155  O  O   . ALA A 52  ? 0.65091 0.93981 0.85563 0.04982  0.06506  -0.22896 34  ALA A O   
156  C  CB  . ALA A 52  ? 0.54131 0.80739 0.70513 0.01974  0.07771  -0.21496 34  ALA A CB  
157  N  N   . ALA A 53  ? 0.59420 0.94820 0.81861 0.03134  0.08447  -0.25375 35  ALA A N   
158  C  CA  . ALA A 53  ? 0.64071 1.01449 0.88458 0.03752  0.07960  -0.25645 35  ALA A CA  
159  C  C   . ALA A 53  ? 0.63812 1.00231 0.89806 0.06674  0.06560  -0.26587 35  ALA A C   
160  O  O   . ALA A 53  ? 0.66165 1.01518 0.92489 0.07586  0.05496  -0.25667 35  ALA A O   
161  C  CB  . ALA A 53  ? 0.59279 1.01601 0.85377 0.02360  0.09267  -0.27517 35  ALA A CB  
162  N  N   . GLU A 54  ? 0.56394 0.92866 0.83118 0.08231  0.06449  -0.28435 36  GLU A N   
163  C  CA  . GLU A 54  ? 0.63637 0.98927 0.91555 0.11254  0.04935  -0.29586 36  GLU A CA  
164  C  C   . GLU A 54  ? 0.68460 0.98241 0.93994 0.12202  0.03576  -0.27445 36  GLU A C   
165  O  O   . GLU A 54  ? 0.69574 0.98447 0.95605 0.13660  0.02301  -0.27120 36  GLU A O   
166  C  CB  . GLU A 54  ? 0.52622 0.88317 0.81197 0.12713  0.05048  -0.31902 36  GLU A CB  
167  N  N   . ARG A 55  ? 0.62327 0.88482 0.85172 0.11248  0.03868  -0.26061 37  ARG A N   
168  C  CA  . ARG A 55  ? 0.68516 0.89548 0.88939 0.11815  0.02798  -0.24263 37  ARG A CA  
169  C  C   . ARG A 55  ? 0.62162 0.82959 0.82113 0.10517  0.02683  -0.22157 37  ARG A C   
170  O  O   . ARG A 55  ? 0.62440 0.79899 0.81107 0.11289  0.01634  -0.20998 37  ARG A O   
171  C  CB  . ARG A 55  ? 0.57732 0.75344 0.75562 0.11023  0.03241  -0.23726 37  ARG A CB  
172  C  CG  . ARG A 55  ? 0.68505 0.87277 0.85471 0.08430  0.04496  -0.22637 37  ARG A CG  
173  C  CD  . ARG A 55  ? 0.65588 0.81121 0.80199 0.07910  0.04780  -0.22470 37  ARG A CD  
174  N  NE  . ARG A 55  ? 0.71751 0.88098 0.85349 0.05665  0.05687  -0.21453 37  ARG A NE  
175  C  CZ  . ARG A 55  ? 0.84218 1.03078 0.98092 0.04529  0.06717  -0.22241 37  ARG A CZ  
176  N  NH1 . ARG A 55  ? 0.65649 0.86910 0.81034 0.05205  0.07192  -0.24132 37  ARG A NH1 
177  N  NH2 . ARG A 55  ? 0.68104 0.87132 0.80653 0.02706  0.07230  -0.21226 37  ARG A NH2 
178  N  N   . LEU A 56  ? 0.55001 0.78971 0.75666 0.08547  0.03713  -0.21676 38  LEU A N   
179  C  CA  . LEU A 56  ? 0.51954 0.75783 0.72269 0.07540  0.03501  -0.19881 38  LEU A CA  
180  C  C   . LEU A 56  ? 0.61750 0.87126 0.83973 0.08852  0.02654  -0.20406 38  LEU A C   
181  O  O   . LEU A 56  ? 0.44571 0.68096 0.66167 0.09079  0.01847  -0.19021 38  LEU A O   
182  C  CB  . LEU A 56  ? 0.44865 0.71087 0.64901 0.05178  0.04691  -0.19300 38  LEU A CB  
183  C  CG  . LEU A 56  ? 0.52482 0.76686 0.70201 0.03752  0.05134  -0.18066 38  LEU A CG  
184  C  CD1 . LEU A 56  ? 0.45364 0.72014 0.62644 0.01788  0.06267  -0.18200 38  LEU A CD1 
185  C  CD2 . LEU A 56  ? 0.47623 0.69159 0.63944 0.03457  0.04437  -0.16083 38  LEU A CD2 
186  N  N   . GLY A 57  ? 0.55567 0.84590 0.80224 0.09706  0.02829  -0.22559 39  GLY A N   
187  C  CA  . GLY A 57  ? 0.50205 0.80977 0.76911 0.11257  0.01842  -0.23441 39  GLY A CA  
188  C  C   . GLY A 57  ? 0.56520 0.83237 0.82238 0.13747  0.00098  -0.23224 39  GLY A C   
189  O  O   . GLY A 57  ? 0.57738 0.83619 0.83570 0.14545  -0.00966 -0.22537 39  GLY A O   
190  N  N   . ALA A 58  ? 0.60897 0.84666 0.85239 0.14904  -0.00225 -0.23783 40  ALA A N   
191  C  CA  . ALA A 58  ? 0.68825 0.87597 0.91190 0.17020  -0.01861 -0.23417 40  ALA A CA  
192  C  C   . ALA A 58  ? 0.72097 0.86952 0.91881 0.15910  -0.02148 -0.20876 40  ALA A C   
193  O  O   . ALA A 58  ? 0.73568 0.85557 0.92275 0.17247  -0.03527 -0.20311 40  ALA A O   
194  C  CB  . ALA A 58  ? 0.52068 0.67850 0.72772 0.17935  -0.01905 -0.24309 40  ALA A CB  
195  N  N   . LEU A 59  ? 0.65414 0.80172 0.84137 0.13507  -0.00913 -0.19444 41  LEU A N   
196  C  CA  . LEU A 59  ? 0.63539 0.75237 0.80150 0.12358  -0.01062 -0.17299 41  LEU A CA  
197  C  C   . LEU A 59  ? 0.60008 0.73198 0.77784 0.12410  -0.01619 -0.16571 41  LEU A C   
198  O  O   . LEU A 59  ? 0.57382 0.67411 0.73640 0.12916  -0.02559 -0.15518 41  LEU A O   
199  C  CB  . LEU A 59  ? 0.57916 0.70158 0.73697 0.10002  0.00254  -0.16293 41  LEU A CB  
200  C  CG  . LEU A 59  ? 0.64044 0.74653 0.78403 0.08580  0.00307  -0.14349 41  LEU A CG  
201  C  CD1 . LEU A 59  ? 0.61172 0.66944 0.73085 0.09182  -0.00519 -0.13652 41  LEU A CD1 
202  C  CD2 . LEU A 59  ? 0.62675 0.74135 0.76379 0.06670  0.01385  -0.13806 41  LEU A CD2 
203  N  N   . SER A 60  ? 0.61835 0.79709 0.82075 0.11719  -0.00982 -0.17177 42  SER A N   
204  C  CA  . SER A 60  ? 0.56651 0.76162 0.78056 0.11665  -0.01445 -0.16671 42  SER A CA  
205  C  C   . SER A 60  ? 0.63605 0.82327 0.85680 0.14131  -0.03039 -0.17613 42  SER A C   
206  O  O   . SER A 60  ? 0.54866 0.71966 0.76288 0.14493  -0.03942 -0.16594 42  SER A O   
207  C  CB  . SER A 60  ? 0.49187 0.73749 0.72813 0.10282  -0.00343 -0.17452 42  SER A CB  
208  O  OG  . SER A 60  ? 0.45156 0.71906 0.70431 0.10675  -0.00898 -0.17744 42  SER A OG  
209  N  N   . ARG A 61  ? 0.48900 0.68656 0.72167 0.15964  -0.03507 -0.19643 43  ARG A N   
210  C  CA  . ARG A 61  ? 0.58822 0.77920 0.82731 0.18693  -0.05295 -0.20824 43  ARG A CA  
211  C  C   . ARG A 61  ? 0.63177 0.75796 0.83526 0.19763  -0.06643 -0.19451 43  ARG A C   
212  O  O   . ARG A 61  ? 0.66620 0.77770 0.86569 0.21252  -0.08152 -0.19322 43  ARG A O   
213  C  CB  . ARG A 61  ? 0.57640 0.79014 0.83417 0.20574  -0.05557 -0.23461 43  ARG A CB  
214  C  CG  . ARG A 61  ? 0.58430 0.83706 0.87292 0.22687  -0.06728 -0.25615 43  ARG A CG  
215  C  CD  . ARG A 61  ? 0.70463 0.98492 1.01433 0.24497  -0.06849 -0.28497 43  ARG A CD  
216  N  NE  . ARG A 61  ? 0.81099 1.12390 1.13140 0.22280  -0.04717 -0.29042 43  ARG A NE  
217  C  CZ  . ARG A 61  ? 0.78681 1.07810 1.09218 0.22130  -0.04093 -0.29186 43  ARG A CZ  
218  N  NH1 . ARG A 61  ? 0.74585 0.98224 1.02444 0.24009  -0.05350 -0.28928 43  ARG A NH1 
219  N  NH2 . ARG A 61  ? 0.67640 0.99938 0.99071 0.19939  -0.02161 -0.29620 43  ARG A NH2 
220  N  N   . ALA A 62  ? 0.70192 0.78817 0.87719 0.18873  -0.06088 -0.18486 44  ALA A N   
221  C  CA  . ALA A 62  ? 0.66956 0.69114 0.80600 0.19475  -0.07134 -0.17315 44  ALA A CA  
222  C  C   . ALA A 62  ? 0.70712 0.71483 0.83206 0.18238  -0.07252 -0.15386 44  ALA A C   
223  O  O   . ALA A 62  ? 0.75824 0.72490 0.85967 0.19307  -0.08604 -0.14801 44  ALA A O   
224  C  CB  . ALA A 62  ? 0.70336 0.69130 0.81377 0.18315  -0.06218 -0.16887 44  ALA A CB  
225  N  N   . ILE A 63  ? 0.64985 0.68887 0.78856 0.16026  -0.05914 -0.14426 45  ILE A N   
226  C  CA  . ILE A 63  ? 0.62207 0.65088 0.75176 0.14839  -0.05951 -0.12723 45  ILE A CA  
227  C  C   . ILE A 63  ? 0.72797 0.78262 0.87799 0.15866  -0.06885 -0.13071 45  ILE A C   
228  O  O   . ILE A 63  ? 0.67056 0.70038 0.80620 0.16200  -0.07821 -0.12141 45  ILE A O   
229  C  CB  . ILE A 63  ? 0.50757 0.55637 0.64164 0.12329  -0.04367 -0.11675 45  ILE A CB  
230  C  CG1 . ILE A 63  ? 0.65593 0.67892 0.76920 0.11349  -0.03584 -0.11438 45  ILE A CG1 
231  C  CG2 . ILE A 63  ? 0.52807 0.57086 0.65610 0.11240  -0.04417 -0.10130 45  ILE A CG2 
232  C  CD1 . ILE A 63  ? 0.52440 0.57204 0.64453 0.09294  -0.02209 -0.10875 45  ILE A CD1 
233  N  N   . TRP A 64  ? 0.65852 0.76409 0.84141 0.16247  -0.06592 -0.14535 46  TRP A N   
234  C  CA  . TRP A 64  ? 0.60026 0.73713 0.80542 0.16999  -0.07342 -0.15141 46  TRP A CA  
235  C  C   . TRP A 64  ? 0.64569 0.75745 0.84297 0.19747  -0.09424 -0.15915 46  TRP A C   
236  O  O   . TRP A 64  ? 0.56362 0.67132 0.75966 0.20226  -0.10425 -0.15413 46  TRP A O   
237  C  CB  . TRP A 64  ? 0.59106 0.78875 0.83166 0.16634  -0.06430 -0.16920 46  TRP A CB  
238  C  CG  . TRP A 64  ? 0.63547 0.87331 0.90182 0.16957  -0.06904 -0.17807 46  TRP A CG  
239  C  CD1 . TRP A 64  ? 0.52935 0.78885 0.80264 0.15018  -0.06118 -0.16910 46  TRP A CD1 
240  C  CD2 . TRP A 64  ? 0.43421 0.69637 0.72263 0.19367  -0.08307 -0.19943 46  TRP A CD2 
241  N  NE1 . TRP A 64  ? 0.58909 0.88523 0.88713 0.15839  -0.06812 -0.18318 46  TRP A NE1 
242  C  CE2 . TRP A 64  ? 0.46229 0.76338 0.77181 0.18561  -0.08196 -0.20262 46  TRP A CE2 
243  C  CE3 . TRP A 64  ? 0.48857 0.74262 0.78010 0.22223  -0.09748 -0.21722 46  TRP A CE3 
244  C  CZ2 . TRP A 64  ? 0.50539 0.84247 0.84196 0.20441  -0.09430 -0.22405 46  TRP A CZ2 
245  C  CZ3 . TRP A 64  ? 0.57104 0.85960 0.88927 0.24364  -0.11136 -0.23869 46  TRP A CZ3 
246  C  CH2 . TRP A 64  ? 0.56118 0.89318 0.90306 0.23423  -0.10944 -0.24242 46  TRP A CH2 
247  N  N   . SER A 65  ? 0.60110 0.69259 0.79018 0.21649  -0.10208 -0.17145 47  SER A N   
248  C  CA  . SER A 65  ? 0.72009 0.78659 0.90014 0.24650  -0.12454 -0.18156 47  SER A CA  
249  C  C   . SER A 65  ? 0.82752 0.82554 0.96270 0.24847  -0.13567 -0.16350 47  SER A C   
250  O  O   . SER A 65  ? 0.86533 0.83828 0.98788 0.27155  -0.15611 -0.16819 47  SER A O   
251  C  CB  . SER A 65  ? 0.70312 0.76380 0.88427 0.26727  -0.13031 -0.20081 47  SER A CB  
252  O  OG  . SER A 65  ? 0.84082 0.85814 0.99129 0.25637  -0.12164 -0.19110 47  SER A OG  
253  N  N   . GLN A 66  ? 0.86045 0.82804 0.97023 0.22483  -0.12314 -0.14446 48  GLN A N   
254  C  CA  . GLN A 66  ? 0.83517 0.73849 0.90008 0.22121  -0.13003 -0.12819 48  GLN A CA  
255  C  C   . GLN A 66  ? 0.79373 0.70627 0.85887 0.19477  -0.11733 -0.11044 48  GLN A C   
256  O  O   . GLN A 66  ? 0.90671 0.80048 0.95433 0.17424  -0.10434 -0.09962 48  GLN A O   
257  C  CB  . GLN A 66  ? 0.90738 0.75674 0.93484 0.21896  -0.12765 -0.12620 48  GLN A CB  
258  C  CG  . GLN A 66  ? 0.98914 0.76275 0.96327 0.22295  -0.14013 -0.11617 48  GLN A CG  
259  C  CD  . GLN A 66  ? 1.10097 0.81880 1.03664 0.22698  -0.14184 -0.11976 48  GLN A CD  
260  O  OE1 . GLN A 66  ? 1.10616 0.84071 1.05729 0.23767  -0.14056 -0.13370 48  GLN A OE1 
261  N  NE2 . GLN A 66  ? 1.10869 0.75885 0.99204 0.21659  -0.14376 -0.10784 48  GLN A NE2 
262  N  N   . PRO A 67  ? 0.75728 0.69969 0.84244 0.19513  -0.12120 -0.10856 49  PRO A N   
263  C  CA  . PRO A 67  ? 0.64047 0.59403 0.72778 0.17141  -0.10952 -0.09315 49  PRO A CA  
264  C  C   . PRO A 67  ? 0.80385 0.70075 0.84954 0.16157  -0.11079 -0.07794 49  PRO A C   
265  O  O   . PRO A 67  ? 0.84902 0.70269 0.86645 0.17466  -0.12574 -0.07676 49  PRO A O   
266  C  CB  . PRO A 67  ? 0.71414 0.70531 0.82775 0.17799  -0.11676 -0.09714 49  PRO A CB  
267  C  CG  . PRO A 67  ? 0.60533 0.58520 0.71694 0.20712  -0.13728 -0.11092 49  PRO A CG  
268  C  CD  . PRO A 67  ? 0.67283 0.64000 0.77908 0.21802  -0.13736 -0.12196 49  PRO A CD  
269  N  N   . GLU A 68  ? 0.83815 0.73556 0.87892 0.13812  -0.09528 -0.06749 50  GLU A N   
270  C  CA  . GLU A 68  ? 0.78098 0.63292 0.78582 0.12391  -0.09242 -0.05547 50  GLU A CA  
271  C  C   . GLU A 68  ? 0.75490 0.63120 0.77210 0.10488  -0.08200 -0.04555 50  GLU A C   
272  O  O   . GLU A 68  ? 0.74599 0.66559 0.79183 0.09745  -0.07254 -0.04660 50  GLU A O   
273  C  CB  . GLU A 68  ? 0.82786 0.64997 0.80908 0.11419  -0.08368 -0.05643 50  GLU A CB  
274  C  CG  . GLU A 68  ? 0.83688 0.62231 0.79658 0.13242  -0.09460 -0.06540 50  GLU A CG  
275  C  CD  . GLU A 68  ? 0.89000 0.65095 0.82919 0.12095  -0.08421 -0.06761 50  GLU A CD  
276  O  OE1 . GLU A 68  ? 0.93083 0.72955 0.89474 0.11115  -0.07133 -0.07081 50  GLU A OE1 
277  O  OE2 . GLU A 68  ? 0.95542 0.65718 0.85101 0.12100  -0.08917 -0.06642 50  GLU A OE2 
278  N  N   . LEU A 69  ? 0.79559 0.64061 0.78776 0.09697  -0.08415 -0.03636 51  LEU A N   
279  C  CA  . LEU A 69  ? 0.77379 0.63793 0.77553 0.08188  -0.07683 -0.02799 51  LEU A CA  
280  C  C   . LEU A 69  ? 0.77286 0.63373 0.76638 0.06133  -0.06208 -0.02488 51  LEU A C   
281  O  O   . LEU A 69  ? 0.79121 0.63445 0.77050 0.05684  -0.05685 -0.02882 51  LEU A O   
282  C  CB  . LEU A 69  ? 0.84263 0.67858 0.82343 0.08384  -0.08657 -0.02142 51  LEU A CB  
283  C  CG  . LEU A 69  ? 0.83488 0.67997 0.82668 0.10386  -0.10249 -0.02509 51  LEU A CG  
284  C  CD1 . LEU A 69  ? 0.83305 0.64882 0.80110 0.10260  -0.11097 -0.01737 51  LEU A CD1 
285  C  CD2 . LEU A 69  ? 0.77940 0.68311 0.81429 0.10546  -0.09886 -0.02936 51  LEU A CD2 
286  N  N   . ALA A 70  ? 0.76387 0.64274 0.76663 0.04915  -0.05587 -0.01911 52  ALA A N   
287  C  CA  . ALA A 70  ? 0.79029 0.67647 0.79231 0.03174  -0.04314 -0.01878 52  ALA A CA  
288  C  C   . ALA A 70  ? 0.82064 0.66534 0.78820 0.02045  -0.03872 -0.02029 52  ALA A C   
289  O  O   . ALA A 70  ? 0.93567 0.74293 0.87488 0.01901  -0.04377 -0.01681 52  ALA A O   
290  C  CB  . ALA A 70  ? 0.68081 0.58591 0.69374 0.02369  -0.04037 -0.01333 52  ALA A CB  
291  N  N   . TYR A 71  ? 0.68831 0.53851 0.65594 0.01118  -0.02912 -0.02606 53  TYR A N   
292  C  CA  . TYR A 71  ? 0.85269 0.66850 0.78878 -0.00399 -0.02175 -0.02987 53  TYR A CA  
293  C  C   . TYR A 71  ? 0.87725 0.64255 0.77915 0.00355  -0.02944 -0.03036 53  TYR A C   
294  O  O   . TYR A 71  ? 0.86822 0.59462 0.73527 -0.01019 -0.02394 -0.03300 53  TYR A O   
295  C  CB  . TYR A 71  ? 0.73181 0.53817 0.65356 -0.02114 -0.01566 -0.02797 53  TYR A CB  
296  C  CG  . TYR A 71  ? 0.75093 0.60332 0.70302 -0.02789 -0.00876 -0.02974 53  TYR A CG  
297  C  CD1 . TYR A 71  ? 0.72546 0.60346 0.69086 -0.03669 0.00048  -0.03796 53  TYR A CD1 
298  C  CD2 . TYR A 71  ? 0.72256 0.59092 0.68813 -0.02453 -0.01267 -0.02401 53  TYR A CD2 
299  C  CE1 . TYR A 71  ? 0.66863 0.58573 0.65925 -0.03983 0.00404  -0.04066 53  TYR A CE1 
300  C  CE2 . TYR A 71  ? 0.64670 0.55212 0.63645 -0.02864 -0.00811 -0.02619 53  TYR A CE2 
301  C  CZ  . TYR A 71  ? 0.64947 0.57848 0.65125 -0.03524 -0.00055 -0.03465 53  TYR A CZ  
302  O  OH  . TYR A 71  ? 0.64118 0.60449 0.66483 -0.03636 0.00133  -0.03786 53  TYR A OH  
303  N  N   . GLU A 72  ? 0.90367 0.66831 0.81357 0.02508  -0.04234 -0.02929 54  GLU A N   
304  C  CA  . GLU A 72  ? 0.89431 0.61165 0.77324 0.03762  -0.05298 -0.03133 54  GLU A CA  
305  C  C   . GLU A 72  ? 0.94435 0.67778 0.84113 0.05260  -0.05561 -0.03930 54  GLU A C   
306  O  O   . GLU A 72  ? 0.93213 0.63494 0.81176 0.06983  -0.06766 -0.04284 54  GLU A O   
307  C  CB  . GLU A 72  ? 0.98394 0.68187 0.85280 0.05324  -0.06899 -0.02632 54  GLU A CB  
308  C  CG  . GLU A 72  ? 1.05218 0.72328 0.89440 0.03868  -0.06762 -0.01870 54  GLU A CG  
309  C  CD  . GLU A 72  ? 1.27059 0.88960 1.06503 0.01811  -0.05920 -0.01906 54  GLU A CD  
310  O  OE1 . GLU A 72  ? 1.23165 0.80659 0.99415 0.02324  -0.06412 -0.02225 54  GLU A OE1 
311  O  OE2 . GLU A 72  ? 1.31870 0.94055 1.10643 -0.00393 -0.04733 -0.01734 54  GLU A OE2 
312  N  N   . GLU A 73  ? 0.84401 0.62332 0.77301 0.04708  -0.04534 -0.04304 55  GLU A N   
313  C  CA  . GLU A 73  ? 0.77119 0.57264 0.72069 0.05979  -0.04638 -0.05121 55  GLU A CA  
314  C  C   . GLU A 73  ? 0.84810 0.61772 0.77220 0.05400  -0.04118 -0.05745 55  GLU A C   
315  O  O   . GLU A 73  ? 0.92742 0.72100 0.86570 0.04656  -0.03137 -0.06260 55  GLU A O   
316  C  CB  . GLU A 73  ? 0.66087 0.52038 0.65015 0.05522  -0.03819 -0.05187 55  GLU A CB  
317  C  CG  . GLU A 73  ? 0.69736 0.58254 0.70449 0.05288  -0.03950 -0.04439 55  GLU A CG  
318  C  CD  . GLU A 73  ? 0.70415 0.59170 0.70601 0.03363  -0.03018 -0.03940 55  GLU A CD  
319  O  OE1 . GLU A 73  ? 0.67839 0.54048 0.65718 0.02120  -0.02385 -0.04148 55  GLU A OE1 
320  O  OE2 . GLU A 73  ? 0.61922 0.53432 0.63950 0.03066  -0.02914 -0.03475 55  GLU A OE2 
321  N  N   . HIS A 74  ? 0.87540 0.58660 0.75785 0.05744  -0.04867 -0.05704 56  HIS A N   
322  C  CA  . HIS A 74  ? 0.99825 0.67001 0.84905 0.05055  -0.04408 -0.06282 56  HIS A CA  
323  C  C   . HIS A 74  ? 1.07220 0.75530 0.93821 0.06936  -0.04889 -0.07255 56  HIS A C   
324  O  O   . HIS A 74  ? 1.05933 0.74534 0.92431 0.06077  -0.03934 -0.07884 56  HIS A O   
325  C  CB  . HIS A 74  ? 1.07668 0.67491 0.87137 0.04844  -0.05162 -0.05924 56  HIS A CB  
326  C  CG  . HIS A 74  ? 1.12266 0.70858 0.90085 0.03091  -0.04770 -0.05065 56  HIS A CG  
327  N  ND1 . HIS A 74  ? 1.10067 0.68827 0.86885 0.00195  -0.03102 -0.05081 56  HIS A ND1 
328  C  CD2 . HIS A 74  ? 1.15169 0.72600 0.92271 0.03802  -0.05808 -0.04325 56  HIS A CD2 
329  C  CE1 . HIS A 74  ? 1.20041 0.77803 0.95614 -0.00822 -0.03063 -0.04415 56  HIS A CE1 
330  N  NE2 . HIS A 74  ? 1.21233 0.78002 0.96827 0.01302  -0.04693 -0.03859 56  HIS A NE2 
331  N  N   . HIS A 75  ? 0.98537 0.67735 0.86655 0.09485  -0.06351 -0.07562 57  HIS A N   
332  C  CA  . HIS A 75  ? 1.03990 0.74648 0.93789 0.11371  -0.06810 -0.08766 57  HIS A CA  
333  C  C   . HIS A 75  ? 0.89064 0.66182 0.83284 0.10663  -0.05543 -0.09190 57  HIS A C   
334  O  O   . HIS A 75  ? 0.89424 0.67185 0.84054 0.10675  -0.04969 -0.10053 57  HIS A O   
335  C  CB  . HIS A 75  ? 1.05018 0.75745 0.95737 0.14292  -0.08712 -0.09299 57  HIS A CB  
336  C  CG  . HIS A 75  ? 1.00986 0.74729 0.94468 0.16262  -0.09089 -0.10823 57  HIS A CG  
337  N  ND1 . HIS A 75  ? 1.07309 0.77422 0.98510 0.17405  -0.09561 -0.11800 57  HIS A ND1 
338  C  CD2 . HIS A 75  ? 0.98836 0.78885 0.97047 0.17128  -0.08955 -0.11662 57  HIS A CD2 
339  C  CE1 . HIS A 75  ? 1.10935 0.85269 1.05620 0.19039  -0.09737 -0.13249 57  HIS A CE1 
340  N  NE2 . HIS A 75  ? 1.05045 0.85504 1.03985 0.18788  -0.09313 -0.13217 57  HIS A NE2 
341  N  N   . ALA A 76  ? 0.78234 0.59839 0.75451 0.10017  -0.05135 -0.08596 58  ALA A N   
342  C  CA  . ALA A 76  ? 0.76459 0.63496 0.77125 0.09168  -0.03995 -0.08855 58  ALA A CA  
343  C  C   . ALA A 76  ? 0.76907 0.63525 0.76483 0.07118  -0.02654 -0.08775 58  ALA A C   
344  O  O   . ALA A 76  ? 0.73967 0.63319 0.75142 0.06789  -0.01903 -0.09403 58  ALA A O   
345  C  CB  . ALA A 76  ? 0.64177 0.55011 0.67354 0.08712  -0.03896 -0.08107 58  ALA A CB  
346  N  N   . HIS A 77  ? 0.82892 0.66255 0.79719 0.05629  -0.02314 -0.08144 59  HIS A N   
347  C  CA  . HIS A 77  ? 0.88736 0.71833 0.84511 0.03617  -0.01060 -0.08363 59  HIS A CA  
348  C  C   . HIS A 77  ? 0.89477 0.70037 0.83487 0.03893  -0.00901 -0.09311 59  HIS A C   
349  O  O   . HIS A 77  ? 0.83275 0.65879 0.78173 0.02946  0.00038  -0.09881 59  HIS A O   
350  C  CB  . HIS A 77  ? 0.88300 0.68430 0.81366 0.01851  -0.00663 -0.07793 59  HIS A CB  
351  C  CG  . HIS A 77  ? 0.90205 0.69708 0.81828 -0.00305 0.00603  -0.08343 59  HIS A CG  
352  N  ND1 . HIS A 77  ? 0.96796 0.71449 0.84644 -0.01067 0.00872  -0.08849 59  HIS A ND1 
353  C  CD2 . HIS A 77  ? 0.77637 0.60784 0.71017 -0.01850 0.01611  -0.08604 59  HIS A CD2 
354  C  CE1 . HIS A 77  ? 0.97566 0.73222 0.85093 -0.03191 0.02140  -0.09454 59  HIS A CE1 
355  N  NE2 . HIS A 77  ? 0.91873 0.72834 0.82871 -0.03579 0.02535  -0.09369 59  HIS A NE2 
356  N  N   . ARG A 78  ? 0.96043 0.71955 0.87369 0.05287  -0.01920 -0.09537 60  ARG A N   
357  C  CA  . ARG A 78  ? 0.95373 0.68424 0.84798 0.05826  -0.01935 -0.10509 60  ARG A CA  
358  C  C   . ARG A 78  ? 0.92165 0.69718 0.85147 0.07122  -0.01861 -0.11431 60  ARG A C   
359  O  O   . ARG A 78  ? 0.86316 0.64387 0.79267 0.06443  -0.01034 -0.12175 60  ARG A O   
360  C  CB  . ARG A 78  ? 1.11412 0.78286 0.97070 0.07483  -0.03384 -0.10581 60  ARG A CB  
361  C  CG  . ARG A 78  ? 1.29568 0.89932 1.09844 0.05700  -0.03098 -0.10147 60  ARG A CG  
362  C  CD  . ARG A 78  ? 1.30354 0.83842 1.06253 0.07585  -0.04769 -0.10242 60  ARG A CD  
363  N  NE  . ARG A 78  ? 1.44834 0.98776 1.21752 0.09608  -0.06332 -0.09731 60  ARG A NE  
364  C  CZ  . ARG A 78  ? 1.35844 0.86402 1.09957 0.08997  -0.06841 -0.08747 60  ARG A CZ  
365  N  NH1 . ARG A 78  ? 1.42392 0.88834 1.12427 0.06305  -0.05829 -0.08206 60  ARG A NH1 
366  N  NH2 . ARG A 78  ? 1.24118 0.75612 0.99539 0.11001  -0.08338 -0.08419 60  ARG A NH2 
367  N  N   . VAL A 79  ? 0.90366 0.71323 0.86372 0.08812  -0.02634 -0.11496 61  VAL A N   
368  C  CA  . VAL A 79  ? 0.88199 0.73476 0.87448 0.09926  -0.02497 -0.12567 61  VAL A CA  
369  C  C   . VAL A 79  ? 0.82096 0.71588 0.83355 0.08076  -0.01062 -0.12492 61  VAL A C   
370  O  O   . VAL A 79  ? 0.80788 0.71762 0.82803 0.08042  -0.00469 -0.13434 61  VAL A O   
371  C  CB  . VAL A 79  ? 0.84725 0.73110 0.86775 0.11707  -0.03469 -0.12761 61  VAL A CB  
372  C  CG1 . VAL A 79  ? 0.79712 0.73131 0.85195 0.12348  -0.03020 -0.13999 61  VAL A CG1 
373  C  CG2 . VAL A 79  ? 0.89624 0.73852 0.89654 0.13940  -0.05166 -0.13110 61  VAL A CG2 
374  N  N   . LEU A 80  ? 0.77760 0.69067 0.79731 0.06601  -0.00582 -0.11437 62  LEU A N   
375  C  CA  . LEU A 80  ? 0.74874 0.70084 0.78616 0.05149  0.00461  -0.11363 62  LEU A CA  
376  C  C   . LEU A 80  ? 0.75735 0.69423 0.77676 0.03629  0.01327  -0.11714 62  LEU A C   
377  O  O   . LEU A 80  ? 0.68987 0.65169 0.71979 0.03058  0.02008  -0.12270 62  LEU A O   
378  C  CB  . LEU A 80  ? 0.70599 0.67919 0.75473 0.04311  0.00500  -0.10257 62  LEU A CB  
379  C  CG  . LEU A 80  ? 0.66669 0.67192 0.74025 0.05255  0.00064  -0.10077 62  LEU A CG  
380  C  CD1 . LEU A 80  ? 0.57536 0.58412 0.65112 0.04733  -0.00199 -0.08926 62  LEU A CD1 
381  C  CD2 . LEU A 80  ? 0.63130 0.67556 0.72376 0.04814  0.00746  -0.10551 62  LEU A CD2 
382  N  N   . THR A 81  ? 0.72275 0.61888 0.71335 0.02790  0.01362  -0.11475 63  THR A N   
383  C  CA  . THR A 81  ? 0.75391 0.63548 0.72611 0.01138  0.02274  -0.12036 63  THR A CA  
384  C  C   . THR A 81  ? 0.82446 0.69103 0.78818 0.01896  0.02348  -0.13115 63  THR A C   
385  O  O   . THR A 81  ? 0.87678 0.75778 0.84293 0.00887  0.03168  -0.13786 63  THR A O   
386  C  CB  . THR A 81  ? 0.83681 0.67487 0.77592 -0.00186 0.02431  -0.11715 63  THR A CB  
387  O  OG1 . THR A 81  ? 0.93534 0.72896 0.85201 0.01202  0.01413  -0.11433 63  THR A OG1 
388  C  CG2 . THR A 81  ? 0.68511 0.54571 0.63493 -0.01389 0.02699  -0.10990 63  THR A CG2 
389  N  N   . HIS A 82  ? 0.93657 0.77480 0.89046 0.03798  0.01401  -0.13404 64  HIS A N   
390  C  CA  . HIS A 82  ? 1.01445 0.83941 0.96211 0.04864  0.01330  -0.14599 64  HIS A CA  
391  C  C   . HIS A 82  ? 0.94228 0.82066 0.92506 0.05345  0.01754  -0.15281 64  HIS A C   
392  O  O   . HIS A 82  ? 0.89980 0.77962 0.88050 0.05233  0.02285  -0.16291 64  HIS A O   
393  C  CB  . HIS A 82  ? 1.01471 0.79992 0.94598 0.07191  -0.00064 -0.14908 64  HIS A CB  
394  C  CG  . HIS A 82  ? 1.23675 0.95490 1.12084 0.06660  -0.00472 -0.14466 64  HIS A CG  
395  N  ND1 . HIS A 82  ? 1.25084 0.92848 1.11439 0.08439  -0.01950 -0.14194 64  HIS A ND1 
396  C  CD2 . HIS A 82  ? 1.31210 0.99525 1.16265 0.04402  0.00424  -0.14332 64  HIS A CD2 
397  C  CE1 . HIS A 82  ? 1.30459 0.92058 1.12017 0.07240  -0.01943 -0.13780 64  HIS A CE1 
398  N  NE2 . HIS A 82  ? 1.34097 0.96026 1.14843 0.04667  -0.00415 -0.13909 64  HIS A NE2 
399  N  N   . PHE A 83  ? 0.81537 0.73556 0.82748 0.05716  0.01590  -0.14778 65  PHE A N   
400  C  CA  . PHE A 83  ? 0.74067 0.70893 0.78137 0.05858  0.02089  -0.15405 65  PHE A CA  
401  C  C   . PHE A 83  ? 0.75836 0.74382 0.79824 0.03993  0.03169  -0.15485 65  PHE A C   
402  O  O   . PHE A 83  ? 0.74477 0.74419 0.78971 0.03985  0.03696  -0.16488 65  PHE A O   
403  C  CB  . PHE A 83  ? 0.63949 0.64327 0.70497 0.06149  0.01803  -0.14725 65  PHE A CB  
404  C  CG  . PHE A 83  ? 0.66000 0.70937 0.75023 0.06116  0.02356  -0.15419 65  PHE A CG  
405  C  CD1 . PHE A 83  ? 0.65906 0.73434 0.75409 0.04496  0.03154  -0.14987 65  PHE A CD1 
406  C  CD2 . PHE A 83  ? 0.71332 0.77917 0.82021 0.07682  0.02043  -0.16639 65  PHE A CD2 
407  C  CE1 . PHE A 83  ? 0.70240 0.81401 0.81355 0.04215  0.03714  -0.15588 65  PHE A CE1 
408  C  CE2 . PHE A 83  ? 0.64125 0.74951 0.76877 0.07310  0.02755  -0.17439 65  PHE A CE2 
409  C  CZ  . PHE A 83  ? 0.62567 0.75425 0.75288 0.05458  0.03637  -0.16826 65  PHE A CZ  
410  N  N   . PHE A 84  ? 0.73564 0.72171 0.76949 0.02454  0.03453  -0.14575 66  PHE A N   
411  C  CA  . PHE A 84  ? 0.82658 0.83186 0.86081 0.00852  0.04252  -0.14770 66  PHE A CA  
412  C  C   . PHE A 84  ? 0.79008 0.76742 0.80200 0.00015  0.04785  -0.15628 66  PHE A C   
413  O  O   . PHE A 84  ? 0.76989 0.76454 0.78349 -0.00945 0.05417  -0.16232 66  PHE A O   
414  C  CB  . PHE A 84  ? 0.68306 0.70242 0.72096 -0.00283 0.04236  -0.13801 66  PHE A CB  
415  C  CG  . PHE A 84  ? 0.69376 0.74582 0.75202 0.00122  0.03915  -0.13077 66  PHE A CG  
416  C  CD1 . PHE A 84  ? 0.65836 0.74090 0.72622 -0.00307 0.04217  -0.13261 66  PHE A CD1 
417  C  CD2 . PHE A 84  ? 0.61332 0.66232 0.67738 0.00830  0.03308  -0.12228 66  PHE A CD2 
418  C  CE1 . PHE A 84  ? 0.63487 0.74096 0.71488 -0.00146 0.03961  -0.12586 66  PHE A CE1 
419  C  CE2 . PHE A 84  ? 0.61985 0.69595 0.69953 0.01020  0.03083  -0.11608 66  PHE A CE2 
420  C  CZ  . PHE A 84  ? 0.58903 0.69205 0.67525 0.00478  0.03431  -0.11777 66  PHE A CZ  
421  N  N   . GLU A 85  ? 0.85014 0.78204 0.83811 0.00302  0.04512  -0.15717 67  GLU A N   
422  C  CA  . GLU A 85  ? 0.90661 0.80549 0.86833 -0.00567 0.05050  -0.16603 67  GLU A CA  
423  C  C   . GLU A 85  ? 0.99086 0.88845 0.95474 0.00645  0.05077  -0.17735 67  GLU A C   
424  O  O   . GLU A 85  ? 1.01639 0.90429 0.96714 -0.00285 0.05751  -0.18613 67  GLU A O   
425  C  CB  . GLU A 85  ? 0.86641 0.70937 0.79450 -0.00738 0.04714  -0.16318 67  GLU A CB  
426  C  CG  . GLU A 85  ? 1.01126 0.84623 0.92406 -0.03098 0.05401  -0.16012 67  GLU A CG  
427  C  CD  . GLU A 85  ? 1.17773 0.97011 1.06522 -0.03203 0.04932  -0.15261 67  GLU A CD  
428  O  OE1 . GLU A 85  ? 1.17741 0.93706 1.05262 -0.01375 0.03954  -0.15032 67  GLU A OE1 
429  O  OE2 . GLU A 85  ? 1.06857 0.86118 0.94825 -0.05086 0.05495  -0.15013 67  GLU A OE2 
430  N  N   . ARG A 86  ? 0.88645 0.79638 0.86783 0.02653  0.04399  -0.17901 68  ARG A N   
431  C  CA  . ARG A 86  ? 0.98783 0.89934 0.97386 0.04015  0.04379  -0.19240 68  ARG A CA  
432  C  C   . ARG A 86  ? 0.95846 0.92151 0.97065 0.03569  0.05109  -0.19767 68  ARG A C   
433  O  O   . ARG A 86  ? 0.86837 0.83695 0.88440 0.04295  0.05367  -0.21062 68  ARG A O   
434  C  CB  . ARG A 86  ? 0.96061 0.86101 0.95270 0.06527  0.03214  -0.19563 68  ARG A CB  
435  C  CG  . ARG A 86  ? 1.19669 1.03359 1.15367 0.07613  0.02367  -0.19855 68  ARG A CG  
436  C  CD  . ARG A 86  ? 1.40512 1.22848 1.36453 0.09800  0.00916  -0.19582 68  ARG A CD  
437  N  NE  . ARG A 86  ? 1.46719 1.22370 1.38426 0.10006  0.00103  -0.19056 68  ARG A NE  
438  C  CZ  . ARG A 86  ? 1.40012 1.13242 1.30841 0.11568  -0.01257 -0.18551 68  ARG A CZ  
439  N  NH1 . ARG A 86  ? 1.38872 1.16093 1.33058 0.13117  -0.01966 -0.18590 68  ARG A NH1 
440  N  NH2 . ARG A 86  ? 1.36120 1.02625 1.22343 0.11445  -0.01910 -0.18048 68  ARG A NH2 
441  N  N   . GLU A 87  ? 0.87294 0.87077 0.90020 0.02414  0.05405  -0.18856 69  GLU A N   
442  C  CA  . GLU A 87  ? 0.83236 0.87240 0.87679 0.01795  0.06039  -0.19234 69  GLU A CA  
443  C  C   . GLU A 87  ? 0.88709 0.92268 0.91868 0.00670  0.06803  -0.20129 69  GLU A C   
444  O  O   . GLU A 87  ? 0.89733 0.91649 0.91286 -0.00636 0.07019  -0.19868 69  GLU A O   
445  C  CB  . GLU A 87  ? 0.69215 0.75965 0.74658 0.00756  0.06012  -0.17993 69  GLU A CB  
446  C  CG  . GLU A 87  ? 0.75139 0.83403 0.82239 0.01695  0.05460  -0.17296 69  GLU A CG  
447  C  CD  . GLU A 87  ? 0.79201 0.90299 0.88056 0.02436  0.05724  -0.18231 69  GLU A CD  
448  O  OE1 . GLU A 87  ? 0.69735 0.83233 0.78844 0.01473  0.06404  -0.18617 69  GLU A OE1 
449  O  OE2 . GLU A 87  ? 0.72366 0.83383 0.82278 0.03930  0.05244  -0.18699 69  GLU A OE2 
450  N  N   . PRO A 88  ? 0.94908 1.00063 0.98745 0.01017  0.07283  -0.21326 70  PRO A N   
451  C  CA  . PRO A 88  ? 0.89152 0.93513 0.91595 0.00060  0.07985  -0.22315 70  PRO A CA  
452  C  C   . PRO A 88  ? 0.86692 0.93812 0.89225 -0.01727 0.08455  -0.21915 70  PRO A C   
453  O  O   . PRO A 88  ? 0.86309 0.96548 0.90160 -0.01951 0.08406  -0.21328 70  PRO A O   
454  C  CB  . PRO A 88  ? 0.76052 0.81524 0.79469 0.01254  0.08278  -0.23826 70  PRO A CB  
455  C  CG  . PRO A 88  ? 0.87659 0.95027 0.93225 0.02738  0.07752  -0.23714 70  PRO A CG  
456  C  CD  . PRO A 88  ? 0.84367 0.92320 0.90315 0.02191  0.07286  -0.22007 70  PRO A CD  
457  N  N   . PRO A 89  ? 0.89453 0.95374 0.90383 -0.03050 0.08849  -0.22294 71  PRO A N   
458  C  CA  . PRO A 89  ? 0.93601 0.95438 0.92340 -0.03304 0.09044  -0.22966 71  PRO A CA  
459  C  C   . PRO A 89  ? 1.04684 1.03626 1.02357 -0.03363 0.08561  -0.22055 71  PRO A C   
460  O  O   . PRO A 89  ? 0.96330 0.96999 0.94989 -0.03734 0.08228  -0.20996 71  PRO A O   
461  C  CB  . PRO A 89  ? 0.91794 0.94619 0.89577 -0.05165 0.09695  -0.23586 71  PRO A CB  
462  C  CG  . PRO A 89  ? 0.97113 1.04273 0.96470 -0.05438 0.09763  -0.23458 71  PRO A CG  
463  C  CD  . PRO A 89  ? 0.93290 1.01991 0.94267 -0.04515 0.09137  -0.22251 71  PRO A CD  
464  N  N   . ALA A 90  ? 1.14319 1.08575 1.09679 -0.03037 0.08494  -0.22475 72  ALA A N   
465  C  CA  . ALA A 90  ? 1.18176 1.09135 1.11958 -0.03236 0.08080  -0.21638 72  ALA A CA  
466  C  C   . ALA A 90  ? 1.16564 1.08795 1.10043 -0.05422 0.08535  -0.21249 72  ALA A C   
467  O  O   . ALA A 90  ? 1.10302 1.03627 1.03292 -0.06992 0.09235  -0.22037 72  ALA A O   
468  C  CB  . ALA A 90  ? 1.35156 1.20102 1.25549 -0.02854 0.07983  -0.22272 72  ALA A CB  
469  N  N   . ALA A 91  ? 1.14978 1.07380 1.08926 -0.05458 0.08099  -0.20179 73  ALA A N   
470  C  CA  . ALA A 91  ? 1.07380 1.01359 1.01446 -0.07246 0.08394  -0.19908 73  ALA A CA  
471  C  C   . ALA A 91  ? 0.94368 0.93637 0.90856 -0.07727 0.08434  -0.19987 73  ALA A C   
472  O  O   . ALA A 91  ? 0.94345 0.95480 0.91136 -0.09113 0.08613  -0.20165 73  ALA A O   
473  C  CB  . ALA A 91  ? 1.06896 0.97647 0.97999 -0.09306 0.09214  -0.20794 73  ALA A CB  
474  N  N   . SER A 92  ? 0.91044 0.92749 0.89111 -0.06624 0.08222  -0.19969 74  SER A N   
475  C  CA  . SER A 92  ? 0.70045 0.76105 0.69823 -0.06960 0.08037  -0.19826 74  SER A CA  
476  C  C   . SER A 92  ? 0.77198 0.84974 0.78347 -0.06560 0.07340  -0.18657 74  SER A C   
477  O  O   . SER A 92  ? 0.84215 0.94790 0.86169 -0.07107 0.07039  -0.18596 74  SER A O   
478  C  CB  . SER A 92  ? 0.78379 0.86189 0.78984 -0.06133 0.08086  -0.20073 74  SER A CB  
479  O  OG  . SER A 92  ? 0.86184 0.93540 0.87668 -0.04605 0.07767  -0.19525 74  SER A OG  
480  N  N   . TRP A 93  ? 0.72344 0.78414 0.73682 -0.05514 0.06972  -0.17809 75  TRP A N   
481  C  CA  . TRP A 93  ? 0.65092 0.71943 0.67282 -0.05355 0.06416  -0.16790 75  TRP A CA  
482  C  C   . TRP A 93  ? 0.78018 0.82661 0.78831 -0.06513 0.06712  -0.17021 75  TRP A C   
483  O  O   . TRP A 93  ? 0.82306 0.83183 0.81258 -0.06603 0.07002  -0.17242 75  TRP A O   
484  C  CB  . TRP A 93  ? 0.66398 0.72546 0.69370 -0.03835 0.05899  -0.15864 75  TRP A CB  
485  C  CG  . TRP A 93  ? 0.67879 0.76777 0.72340 -0.03066 0.05666  -0.15546 75  TRP A CG  
486  C  CD1 . TRP A 93  ? 0.60699 0.69977 0.65510 -0.02372 0.05919  -0.16097 75  TRP A CD1 
487  C  CD2 . TRP A 93  ? 0.65935 0.77354 0.71424 -0.03054 0.05188  -0.14714 75  TRP A CD2 
488  N  NE1 . TRP A 93  ? 0.66095 0.78044 0.71994 -0.02196 0.05778  -0.15679 75  TRP A NE1 
489  C  CE2 . TRP A 93  ? 0.62807 0.75790 0.68913 -0.02591 0.05279  -0.14743 75  TRP A CE2 
490  C  CE3 . TRP A 93  ? 0.64015 0.76388 0.69800 -0.03398 0.04687  -0.14055 75  TRP A CE3 
491  C  CZ2 . TRP A 93  ? 0.65054 0.79982 0.71581 -0.02635 0.04907  -0.14000 75  TRP A CZ2 
492  C  CZ3 . TRP A 93  ? 0.60929 0.75232 0.67299 -0.03130 0.04157  -0.13324 75  TRP A CZ3 
493  C  CH2 . TRP A 93  ? 0.65291 0.80595 0.71794 -0.02836 0.04279  -0.13232 75  TRP A CH2 
494  N  N   . ALA A 94  ? 0.64316 0.71168 0.65823 -0.07426 0.06620  -0.17095 76  ALA A N   
495  C  CA  . ALA A 94  ? 0.70041 0.75420 0.70415 -0.08818 0.07055  -0.17503 76  ALA A CA  
496  C  C   . ALA A 94  ? 0.72379 0.76291 0.72824 -0.08116 0.06601  -0.16363 76  ALA A C   
497  O  O   . ALA A 94  ? 0.77387 0.83768 0.79504 -0.07583 0.06013  -0.15732 76  ALA A O   
498  C  CB  . ALA A 94  ? 0.66477 0.75451 0.67910 -0.10014 0.07133  -0.18436 76  ALA A CB  
499  N  N   . VAL A 95  ? 0.66439 0.66061 0.64813 -0.08062 0.06779  -0.16115 77  VAL A N   
500  C  CA  . VAL A 95  ? 0.61690 0.59447 0.59835 -0.07191 0.06231  -0.15010 77  VAL A CA  
501  C  C   . VAL A 95  ? 0.78019 0.73858 0.74427 -0.08868 0.06734  -0.15237 77  VAL A C   
502  O  O   . VAL A 95  ? 0.87700 0.80644 0.81547 -0.10400 0.07512  -0.16064 77  VAL A O   
503  C  CB  . VAL A 95  ? 0.72513 0.66670 0.69373 -0.05704 0.05818  -0.14624 77  VAL A CB  
504  C  CG1 . VAL A 95  ? 0.64763 0.57526 0.61671 -0.04620 0.05061  -0.13507 77  VAL A CG1 
505  C  CG2 . VAL A 95  ? 0.69142 0.65496 0.67683 -0.04395 0.05602  -0.14831 77  VAL A CG2 
506  N  N   . GLN A 96  ? 0.80160 0.77439 0.77733 -0.08719 0.06365  -0.14571 78  GLN A N   
507  C  CA  . GLN A 96  ? 0.76176 0.71785 0.72190 -0.10283 0.06859  -0.14759 78  GLN A CA  
508  C  C   . GLN A 96  ? 0.77075 0.69826 0.72205 -0.09190 0.06188  -0.13478 78  GLN A C   
509  O  O   . GLN A 96  ? 0.72555 0.67665 0.69780 -0.08171 0.05541  -0.12680 78  GLN A O   
510  C  CB  . GLN A 96  ? 0.74549 0.74714 0.72791 -0.11153 0.07022  -0.15406 78  GLN A CB  
511  C  CG  . GLN A 96  ? 0.84128 0.87330 0.83193 -0.12313 0.07582  -0.16917 78  GLN A CG  
512  C  CD  . GLN A 96  ? 0.88261 0.96672 0.90468 -0.11425 0.06859  -0.17117 78  GLN A CD  
513  O  OE1 . GLN A 96  ? 0.76073 0.87055 0.79506 -0.11972 0.06831  -0.17730 78  GLN A OE1 
514  N  NE2 . GLN A 96  ? 0.88350 0.98164 0.91653 -0.10030 0.06226  -0.16686 78  GLN A NE2 
515  N  N   . PRO A 97  ? 0.83275 0.70771 0.75139 -0.09303 0.06211  -0.13261 79  PRO A N   
516  C  CA  . PRO A 97  ? 0.86913 0.71518 0.77666 -0.08249 0.05430  -0.12129 79  PRO A CA  
517  C  C   . PRO A 97  ? 0.85202 0.69388 0.74993 -0.09884 0.05894  -0.12074 79  PRO A C   
518  O  O   . PRO A 97  ? 0.92230 0.77269 0.81387 -0.12093 0.06963  -0.13117 79  PRO A O   
519  C  CB  . PRO A 97  ? 0.95278 0.73947 0.82271 -0.07878 0.05207  -0.12155 79  PRO A CB  
520  C  CG  . PRO A 97  ? 0.95385 0.72893 0.80418 -0.09961 0.06368  -0.13373 79  PRO A CG  
521  C  CD  . PRO A 97  ? 0.87389 0.70979 0.76092 -0.10329 0.06836  -0.14072 79  PRO A CD  
522  N  N   . HIS A 98  ? 0.82751 0.65854 0.72539 -0.08808 0.05098  -0.10985 80  HIS A N   
523  C  CA  . HIS A 98  ? 0.97652 0.80092 0.86425 -0.10166 0.05445  -0.10827 80  HIS A CA  
524  C  C   . HIS A 98  ? 0.93060 0.80856 0.84751 -0.11287 0.06103  -0.11637 80  HIS A C   
525  O  O   . HIS A 98  ? 0.91307 0.79113 0.81966 -0.13319 0.06992  -0.12391 80  HIS A O   
526  C  CB  . HIS A 98  ? 0.98588 0.75298 0.82445 -0.12194 0.06184  -0.11222 80  HIS A CB  
527  C  CG  . HIS A 98  ? 1.09046 0.79965 0.89540 -0.10943 0.05364  -0.10640 80  HIS A CG  
528  N  ND1 . HIS A 98  ? 1.06112 0.74625 0.85973 -0.08927 0.04019  -0.09491 80  HIS A ND1 
529  C  CD2 . HIS A 98  ? 1.08845 0.75890 0.86401 -0.11270 0.05576  -0.11177 80  HIS A CD2 
530  C  CE1 . HIS A 98  ? 1.12620 0.76110 0.89375 -0.07893 0.03323  -0.09412 80  HIS A CE1 
531  N  NE2 . HIS A 98  ? 1.13751 0.76057 0.88944 -0.09280 0.04260  -0.10382 80  HIS A NE2 
532  N  N   . TYR A 99  ? 0.86676 0.78994 0.81883 -0.09936 0.05617  -0.11597 81  TYR A N   
533  C  CA  . TYR A 99  ? 0.79709 0.77061 0.77681 -0.10482 0.05872  -0.12424 81  TYR A CA  
534  C  C   . TYR A 99  ? 0.84818 0.83283 0.83709 -0.10395 0.05594  -0.11973 81  TYR A C   
535  O  O   . TYR A 99  ? 0.75254 0.74422 0.75552 -0.08686 0.04651  -0.10815 81  TYR A O   
536  C  CB  . TYR A 99  ? 0.81494 0.82381 0.82203 -0.08892 0.05197  -0.12266 81  TYR A CB  
537  C  CG  . TYR A 99  ? 0.81622 0.87308 0.84820 -0.09127 0.05150  -0.13182 81  TYR A CG  
538  C  CD1 . TYR A 99  ? 0.87008 0.95290 0.92354 -0.07693 0.04218  -0.12498 81  TYR A CD1 
539  C  CD2 . TYR A 99  ? 0.74588 0.82102 0.77830 -0.10735 0.05945  -0.14846 81  TYR A CD2 
540  C  CE1 . TYR A 99  ? 0.75364 0.87607 0.82666 -0.07597 0.03901  -0.13395 81  TYR A CE1 
541  C  CE2 . TYR A 99  ? 0.81605 0.93692 0.87218 -0.10656 0.05658  -0.15893 81  TYR A CE2 
542  C  CZ  . TYR A 99  ? 0.82405 0.96679 0.89960 -0.08952 0.04544  -0.15135 81  TYR A CZ  
543  O  OH  . TYR A 99  ? 1.02998 1.21404 1.12604 -0.08568 0.03992  -0.16223 81  TYR A OH  
544  N  N   . GLN A 100 ? 0.74648 0.73320 0.72674 -0.12388 0.06507  -0.13021 82  GLN A N   
545  C  CA  . GLN A 100 ? 0.77126 0.76987 0.75899 -0.12642 0.06461  -0.12951 82  GLN A CA  
546  C  C   . GLN A 100 ? 0.80481 0.76121 0.77113 -0.12096 0.05997  -0.11472 82  GLN A C   
547  O  O   . GLN A 100 ? 0.88607 0.82054 0.83095 -0.13642 0.06625  -0.11694 82  GLN A O   
548  C  CB  . GLN A 100 ? 0.71143 0.75799 0.73583 -0.11023 0.05575  -0.12896 82  GLN A CB  
549  C  CG  . GLN A 100 ? 0.87015 0.95785 0.91490 -0.11160 0.05676  -0.14322 82  GLN A CG  
550  C  CD  . GLN A 100 ? 0.90978 1.01578 0.95297 -0.13471 0.06873  -0.16426 82  GLN A CD  
551  O  OE1 . GLN A 100 ? 0.99393 1.09595 1.02988 -0.14790 0.07525  -0.16961 82  GLN A OE1 
552  N  NE2 . GLN A 100 ? 0.83734 0.96487 0.88700 -0.14108 0.07234  -0.17760 82  GLN A NE2 
553  N  N   . LEU A 101 ? 0.89929 0.84523 0.87062 -0.09977 0.04902  -0.10085 83  LEU A N   
554  C  CA  . LEU A 101 ? 0.73922 0.64467 0.68928 -0.09328 0.04312  -0.08862 83  LEU A CA  
555  C  C   . LEU A 101 ? 0.84710 0.70665 0.76762 -0.09096 0.04170  -0.08619 83  LEU A C   
556  O  O   . LEU A 101 ? 0.82679 0.69297 0.75256 -0.08738 0.04265  -0.09063 83  LEU A O   
557  C  CB  . LEU A 101 ? 0.70811 0.63181 0.68217 -0.07162 0.03139  -0.07677 83  LEU A CB  
558  C  CG  . LEU A 101 ? 0.77472 0.72909 0.76928 -0.07150 0.03017  -0.07612 83  LEU A CG  
559  C  CD1 . LEU A 101 ? 0.67648 0.65083 0.69423 -0.05171 0.01966  -0.06590 83  LEU A CD1 
560  C  CD2 . LEU A 101 ? 0.67806 0.60595 0.65099 -0.08247 0.03292  -0.07422 83  LEU A CD2 
561  N  N   . PRO A 102 ? 0.83524 0.64546 0.72211 -0.09225 0.03854  -0.07975 84  PRO A N   
562  C  CA  . PRO A 102 ? 0.78928 0.54975 0.64369 -0.08736 0.03474  -0.07819 84  PRO A CA  
563  C  C   . PRO A 102 ? 0.85874 0.63139 0.73413 -0.06208 0.02420  -0.07426 84  PRO A C   
564  O  O   . PRO A 102 ? 0.85892 0.61160 0.72110 -0.05915 0.02433  -0.07871 84  PRO A O   
565  C  CB  . PRO A 102 ? 0.90984 0.61863 0.72693 -0.08885 0.02931  -0.07032 84  PRO A CB  
566  C  CG  . PRO A 102 ? 0.85469 0.58084 0.67471 -0.10776 0.03816  -0.07289 84  PRO A CG  
567  C  CD  . PRO A 102 ? 0.81905 0.61243 0.69026 -0.10101 0.03913  -0.07567 84  PRO A CD  
568  N  N   . THR A 103 ? 0.74778 0.55236 0.65430 -0.04496 0.01580  -0.06726 85  THR A N   
569  C  CA  . THR A 103 ? 0.74038 0.56078 0.66786 -0.02336 0.00727  -0.06552 85  THR A CA  
570  C  C   . THR A 103 ? 0.79918 0.67274 0.76304 -0.02177 0.01114  -0.06889 85  THR A C   
571  O  O   . THR A 103 ? 0.70952 0.60135 0.69210 -0.00682 0.00604  -0.06844 85  THR A O   
572  C  CB  . THR A 103 ? 0.76424 0.58229 0.69884 -0.00591 -0.00495 -0.05688 85  THR A CB  
573  O  OG1 . THR A 103 ? 0.76605 0.61746 0.72307 -0.00944 -0.00380 -0.05204 85  THR A OG1 
574  C  CG2 . THR A 103 ? 0.80504 0.56653 0.69992 -0.00503 -0.01154 -0.05321 85  THR A CG2 
575  N  N   . ALA A 104 ? 0.70959 0.60824 0.68262 -0.03661 0.01946  -0.07339 86  ALA A N   
576  C  CA  . ALA A 104 ? 0.59085 0.53355 0.59173 -0.03496 0.02156  -0.07722 86  ALA A CA  
577  C  C   . ALA A 104 ? 0.65305 0.59305 0.64673 -0.04173 0.02801  -0.08695 86  ALA A C   
578  O  O   . ALA A 104 ? 0.75949 0.66517 0.72610 -0.05184 0.03287  -0.09175 86  ALA A O   
579  C  CB  . ALA A 104 ? 0.55994 0.53280 0.57535 -0.04393 0.02457  -0.07919 86  ALA A CB  
580  N  N   . PHE A 105 ? 0.65903 0.63267 0.67390 -0.03700 0.02802  -0.08984 87  PHE A N   
581  C  CA  . PHE A 105 ? 0.58207 0.55740 0.59249 -0.04281 0.03377  -0.09933 87  PHE A CA  
582  C  C   . PHE A 105 ? 0.61941 0.63786 0.65270 -0.04248 0.03388  -0.10278 87  PHE A C   
583  O  O   . PHE A 105 ? 0.58742 0.62937 0.63754 -0.03539 0.02848  -0.09675 87  PHE A O   
584  C  CB  . PHE A 105 ? 0.63998 0.59272 0.64182 -0.03111 0.03092  -0.09933 87  PHE A CB  
585  C  CG  . PHE A 105 ? 0.64901 0.62904 0.67385 -0.01607 0.02575  -0.09621 87  PHE A CG  
586  C  CD1 . PHE A 105 ? 0.62127 0.62603 0.65719 -0.01668 0.02896  -0.10204 87  PHE A CD1 
587  C  CD2 . PHE A 105 ? 0.61318 0.59395 0.64675 -0.00303 0.01831  -0.08854 87  PHE A CD2 
588  C  CE1 . PHE A 105 ? 0.60452 0.63269 0.65770 -0.00622 0.02589  -0.10011 87  PHE A CE1 
589  C  CE2 . PHE A 105 ? 0.61421 0.62127 0.66749 0.00732  0.01548  -0.08768 87  PHE A CE2 
590  C  CZ  . PHE A 105 ? 0.56998 0.59990 0.63197 0.00490  0.01982  -0.09339 87  PHE A CZ  
591  N  N   . ARG A 106 ? 0.59664 0.62194 0.62705 -0.05031 0.03943  -0.11270 88  ARG A N   
592  C  CA  . ARG A 106 ? 0.59666 0.65882 0.64378 -0.05007 0.03850  -0.11731 88  ARG A CA  
593  C  C   . ARG A 106 ? 0.60444 0.66436 0.64631 -0.05136 0.04251  -0.12447 88  ARG A C   
594  O  O   . ARG A 106 ? 0.63058 0.66848 0.65557 -0.06137 0.04915  -0.13200 88  ARG A O   
595  C  CB  . ARG A 106 ? 0.65889 0.74288 0.71127 -0.06198 0.04096  -0.12622 88  ARG A CB  
596  C  CG  . ARG A 106 ? 0.53766 0.65782 0.60450 -0.06015 0.03746  -0.13260 88  ARG A CG  
597  C  CD  . ARG A 106 ? 0.69903 0.84429 0.77467 -0.06847 0.03759  -0.14330 88  ARG A CD  
598  N  NE  . ARG A 106 ? 0.78429 0.96379 0.87347 -0.06241 0.03008  -0.14904 88  ARG A NE  
599  C  CZ  . ARG A 106 ? 0.77986 0.98693 0.88166 -0.06154 0.02487  -0.15720 88  ARG A CZ  
600  N  NH1 . ARG A 106 ? 0.63385 0.84198 0.73873 -0.06810 0.02815  -0.16127 88  ARG A NH1 
601  N  NH2 . ARG A 106 ? 0.72368 0.95725 0.83394 -0.05332 0.01548  -0.16238 88  ARG A NH2 
602  N  N   . ALA A 107 ? 0.52894 0.60922 0.58232 -0.04266 0.03899  -0.12247 89  ALA A N   
603  C  CA  . ALA A 107 ? 0.55747 0.63954 0.60748 -0.04332 0.04270  -0.12950 89  ALA A CA  
604  C  C   . ALA A 107 ? 0.58783 0.70278 0.64779 -0.04412 0.03995  -0.13233 89  ALA A C   
605  O  O   . ALA A 107 ? 0.59556 0.72621 0.66426 -0.03728 0.03341  -0.12488 89  ALA A O   
606  C  CB  . ALA A 107 ? 0.44283 0.51274 0.49325 -0.03113 0.04146  -0.12566 89  ALA A CB  
607  N  N   . GLU A 108 ? 0.62255 0.74493 0.67805 -0.05265 0.04426  -0.14324 90  GLU A N   
608  C  CA  . GLU A 108 ? 0.63976 0.79130 0.70115 -0.05367 0.04022  -0.14770 90  GLU A CA  
609  C  C   . GLU A 108 ? 0.70551 0.85842 0.76071 -0.05639 0.04464  -0.15486 90  GLU A C   
610  O  O   . GLU A 108 ? 0.63173 0.76712 0.67780 -0.06294 0.05225  -0.16211 90  GLU A O   
611  C  CB  . GLU A 108 ? 0.49862 0.66802 0.56397 -0.06276 0.03946  -0.15763 90  GLU A CB  
612  C  CG  . GLU A 108 ? 0.74336 0.91355 0.81506 -0.06197 0.03645  -0.15370 90  GLU A CG  
613  C  CD  . GLU A 108 ? 0.82005 1.02044 0.90169 -0.06651 0.03250  -0.16520 90  GLU A CD  
614  O  OE1 . GLU A 108 ? 0.82141 1.03862 0.90333 -0.07396 0.03442  -0.17843 90  GLU A OE1 
615  O  OE2 . GLU A 108 ? 0.72330 0.93229 0.81332 -0.06206 0.02708  -0.16244 90  GLU A OE2 
616  N  N   . TRP A 109 ? 0.59412 0.76486 0.65096 -0.05206 0.03974  -0.15298 91  TRP A N   
617  C  CA  . TRP A 109 ? 0.62425 0.80047 0.67460 -0.05574 0.04333  -0.16054 91  TRP A CA  
618  C  C   . TRP A 109 ? 0.63051 0.83028 0.67934 -0.05562 0.03509  -0.16246 91  TRP A C   
619  O  O   . TRP A 109 ? 0.63192 0.83852 0.68188 -0.04880 0.02610  -0.15414 91  TRP A O   
620  C  CB  . TRP A 109 ? 0.67007 0.83694 0.71845 -0.04997 0.04720  -0.15655 91  TRP A CB  
621  C  CG  . TRP A 109 ? 0.66917 0.84290 0.71038 -0.05439 0.05144  -0.16496 91  TRP A CG  
622  C  CD1 . TRP A 109 ? 0.70322 0.86601 0.73901 -0.05901 0.05947  -0.17517 91  TRP A CD1 
623  C  CD2 . TRP A 109 ? 0.65764 0.84753 0.69272 -0.05528 0.04765  -0.16410 91  TRP A CD2 
624  N  NE1 . TRP A 109 ? 0.80255 0.97719 0.83229 -0.06265 0.06154  -0.18117 91  TRP A NE1 
625  C  CE2 . TRP A 109 ? 0.67266 0.86351 0.70081 -0.06092 0.05437  -0.17433 91  TRP A CE2 
626  C  CE3 . TRP A 109 ? 0.65555 0.85502 0.68635 -0.05221 0.03884  -0.15559 91  TRP A CE3 
627  C  CZ2 . TRP A 109 ? 0.68892 0.89161 0.70654 -0.06432 0.05295  -0.17623 91  TRP A CZ2 
628  C  CZ3 . TRP A 109 ? 0.66532 0.87253 0.68239 -0.05548 0.03675  -0.15696 91  TRP A CZ3 
629  C  CH2 . TRP A 109 ? 0.67369 0.88335 0.68458 -0.06185 0.04397  -0.16717 91  TRP A CH2 
630  N  N   . GLU A 110 ? 0.60180 0.81110 0.64542 -0.06270 0.03732  -0.17372 92  GLU A N   
631  C  CA  . GLU A 110 ? 0.69341 0.92261 0.73178 -0.06188 0.02838  -0.17721 92  GLU A CA  
632  C  C   . GLU A 110 ? 0.77621 1.00671 0.80534 -0.06902 0.03465  -0.18640 92  GLU A C   
633  O  O   . GLU A 110 ? 0.80305 1.02167 0.83189 -0.07560 0.04540  -0.19296 92  GLU A O   
634  C  CB  . GLU A 110 ? 0.66046 0.91028 0.70689 -0.06305 0.02074  -0.18605 92  GLU A CB  
635  C  CG  . GLU A 110 ? 0.73679 0.99637 0.78538 -0.07569 0.02794  -0.20293 92  GLU A CG  
636  C  CD  . GLU A 110 ? 0.81536 1.09191 0.87660 -0.08025 0.02633  -0.21282 92  GLU A CD  
637  O  OE1 . GLU A 110 ? 0.77049 1.06988 0.83904 -0.07236 0.01359  -0.21562 92  GLU A OE1 
638  O  OE2 . GLU A 110 ? 0.85917 1.12485 0.92118 -0.09187 0.03767  -0.21868 92  GLU A OE2 
639  N  N   . PRO A 111 ? 0.76365 1.00465 0.78186 -0.06784 0.02781  -0.18698 93  PRO A N   
640  C  CA  . PRO A 111 ? 0.83933 1.08441 0.84816 -0.07570 0.03306  -0.19746 93  PRO A CA  
641  C  C   . PRO A 111 ? 0.92636 1.18403 0.94115 -0.08440 0.03521  -0.21270 93  PRO A C   
642  O  O   . PRO A 111 ? 0.95998 1.23734 0.98095 -0.08295 0.02555  -0.21823 93  PRO A O   
643  C  CB  . PRO A 111 ? 0.72539 0.97838 0.71810 -0.07210 0.02167  -0.19400 93  PRO A CB  
644  C  CG  . PRO A 111 ? 0.78042 1.02407 0.77055 -0.06340 0.01504  -0.17905 93  PRO A CG  
645  C  CD  . PRO A 111 ? 0.70220 0.94569 0.71116 -0.05956 0.01522  -0.17693 93  PRO A CD  
646  N  N   . PRO A 112 ? 1.17044 1.41755 1.18310 -0.09384 0.04776  -0.22140 94  PRO A N   
647  C  CA  . PRO A 112 ? 1.23396 1.48985 1.24928 -0.10618 0.05247  -0.23715 94  PRO A CA  
648  C  C   . PRO A 112 ? 1.14745 1.42570 1.15697 -0.11219 0.04838  -0.25001 94  PRO A C   
649  O  O   . PRO A 112 ? 1.16414 1.43690 1.16513 -0.12156 0.05702  -0.25922 94  PRO A O   
650  C  CB  . PRO A 112 ? 1.03798 1.26449 1.04707 -0.11279 0.06687  -0.23941 94  PRO A CB  
651  C  CG  . PRO A 112 ? 1.02955 1.23698 1.03886 -0.10081 0.06769  -0.22516 94  PRO A CG  
652  C  CD  . PRO A 112 ? 1.06203 1.28610 1.07003 -0.09328 0.05854  -0.21793 94  PRO A CD  
653  N  N   . GLU A 113 ? 1.29187 1.59505 1.30525 -0.10574 0.03378  -0.25153 95  GLU A N   
654  C  CA  . GLU A 113 ? 1.20120 1.52913 1.20966 -0.10827 0.02528  -0.26424 95  GLU A CA  
655  C  C   . GLU A 113 ? 1.34292 1.69489 1.35913 -0.09641 0.00673  -0.26514 95  GLU A C   
656  O  O   . GLU A 113 ? 1.45603 1.79865 1.47296 -0.08457 -0.00046 -0.25118 95  GLU A O   
657  C  CB  . GLU A 113 ? 1.21450 1.53246 1.20342 -0.10716 0.02499  -0.25960 95  GLU A CB  
658  C  CG  . GLU A 113 ? 1.10134 1.41539 1.08369 -0.12117 0.03818  -0.27206 95  GLU A CG  
659  C  CD  . GLU A 113 ? 1.09121 1.39576 1.05459 -0.12153 0.04008  -0.26888 95  GLU A CD  
660  O  OE1 . GLU A 113 ? 1.23193 1.54047 1.18287 -0.11384 0.02774  -0.26172 95  GLU A OE1 
661  O  OE2 . GLU A 113 ? 0.88460 1.17615 0.84295 -0.13020 0.05382  -0.27462 95  GLU A OE2 
662  N  N   . ALA A 114 ? 1.18054 1.56406 1.20280 -0.09906 -0.00151 -0.28305 96  ALA A N   
663  C  CA  . ALA A 114 ? 1.29763 1.71001 1.33545 -0.08927 -0.01669 -0.29102 96  ALA A CA  
664  C  C   . ALA A 114 ? 1.25562 1.68791 1.28495 -0.07500 -0.03955 -0.29630 96  ALA A C   
665  O  O   . ALA A 114 ? 1.37314 1.81314 1.40660 -0.05883 -0.05600 -0.29329 96  ALA A O   
666  C  CB  . ALA A 114 ? 1.18694 1.62659 1.24526 -0.10417 -0.00764 -0.31255 96  ALA A CB  
667  N  N   . ARG A 115 ? 1.13662 1.57685 1.15318 -0.07992 -0.04214 -0.30543 97  ARG A N   
668  C  CA  . ARG A 115 ? 1.02774 1.48025 1.02931 -0.06570 -0.06542 -0.30935 97  ARG A CA  
669  C  C   . ARG A 115 ? 1.07834 1.57291 1.09998 -0.05456 -0.08386 -0.32903 97  ARG A C   
670  O  O   . ARG A 115 ? 1.08654 1.60818 1.10692 -0.05292 -0.09566 -0.34644 97  ARG A O   
671  C  CB  . ARG A 115 ? 1.21056 1.62877 1.18602 -0.05120 -0.07645 -0.28625 97  ARG A CB  
672  N  N   . ALA A 116 ? 1.31395 1.81576 1.35418 -0.04569 -0.08759 -0.32754 98  ALA A N   
673  C  CA  . ALA A 116 ? 1.40310 1.94695 1.46705 -0.03356 -0.10409 -0.34736 98  ALA A CA  
674  C  C   . ALA A 116 ? 1.46496 2.00925 1.51111 -0.00726 -0.13519 -0.34609 98  ALA A C   
675  O  O   . ALA A 116 ? 1.29241 1.85369 1.33097 -0.00233 -0.14827 -0.35837 98  ALA A O   
676  C  CB  . ALA A 116 ? 1.07833 1.66723 1.16557 -0.04896 -0.09650 -0.37613 98  ALA A CB  
677  N  N   . PRO A 117 ? 1.62643 2.14754 1.66346 0.01078  -0.14753 -0.33004 99  PRO A N   
678  C  CA  . PRO A 117 ? 1.52854 2.03897 1.54156 0.03717  -0.17841 -0.32643 99  PRO A CA  
679  C  C   . PRO A 117 ? 1.48752 2.03477 1.52742 0.05610  -0.19445 -0.34513 99  PRO A C   
680  O  O   . PRO A 117 ? 1.40657 1.96534 1.47042 0.06209  -0.19243 -0.34766 99  PRO A O   
681  C  CB  . PRO A 117 ? 1.48816 1.95295 1.48319 0.04447  -0.17765 -0.29937 99  PRO A CB  
682  C  CG  . PRO A 117 ? 1.41286 1.87017 1.42705 0.02298  -0.14692 -0.29049 99  PRO A CG  
683  C  CD  . PRO A 117 ? 1.56024 2.06033 1.60686 0.00662  -0.13269 -0.31419 99  PRO A CD  
684  N  N   . PRO A 121 ? 1.22049 1.64983 1.23171 0.10290  -0.21388 -0.27534 103 PRO A N   
685  C  CA  . PRO A 121 ? 1.22655 1.66374 1.25190 0.07485  -0.18444 -0.27438 103 PRO A CA  
686  C  C   . PRO A 121 ? 1.29880 1.73052 1.34545 0.06046  -0.16064 -0.26511 103 PRO A C   
687  O  O   . PRO A 121 ? 1.31534 1.76376 1.38258 0.04003  -0.13862 -0.27209 103 PRO A O   
688  C  CB  . PRO A 121 ? 1.19266 1.68502 1.24758 0.07086  -0.18555 -0.30480 103 PRO A CB  
689  C  CG  . PRO A 121 ? 1.21251 1.71380 1.25500 0.09699  -0.21678 -0.31565 103 PRO A CG  
690  C  CD  . PRO A 121 ? 1.11127 1.58215 1.13757 0.11871  -0.23396 -0.30185 103 PRO A CD  
691  N  N   . ARG A 122 ? 1.11020 1.51582 1.14883 0.07094  -0.16577 -0.24971 104 ARG A N   
692  C  CA  . ARG A 122 ? 1.05822 1.45679 1.11467 0.05938  -0.14583 -0.24045 104 ARG A CA  
693  C  C   . ARG A 122 ? 0.93873 1.29501 0.97248 0.04656  -0.13020 -0.21582 104 ARG A C   
694  O  O   . ARG A 122 ? 0.92244 1.24414 0.92376 0.05436  -0.14033 -0.19952 104 ARG A O   
695  C  CB  . ARG A 122 ? 0.89362 1.28963 0.95603 0.07681  -0.15886 -0.23872 104 ARG A CB  
696  N  N   . PRO A 123 ? 0.79457 1.15120 0.84210 0.02704  -0.10628 -0.21361 105 PRO A N   
697  C  CA  . PRO A 123 ? 0.77715 1.09852 0.80681 0.01687  -0.09231 -0.19331 105 PRO A CA  
698  C  C   . PRO A 123 ? 0.73737 1.03333 0.76169 0.02288  -0.09301 -0.17598 105 PRO A C   
699  O  O   . PRO A 123 ? 0.71798 1.02377 0.75833 0.03040  -0.09773 -0.17937 105 PRO A O   
700  C  CB  . PRO A 123 ? 0.76016 1.09084 0.80859 -0.00209 -0.06946 -0.19942 105 PRO A CB  
701  C  CG  . PRO A 123 ? 0.82787 1.19750 0.89821 -0.00520 -0.07101 -0.22325 105 PRO A CG  
702  C  CD  . PRO A 123 ? 0.84776 1.23541 0.92538 0.01301  -0.09122 -0.23086 105 PRO A CD  
703  N  N   . LEU A 124 ? 0.67623 0.94081 0.67771 0.01836  -0.08759 -0.15856 106 LEU A N   
704  C  CA  . LEU A 124 ? 0.73597 0.97534 0.73020 0.02090  -0.08613 -0.14185 106 LEU A CA  
705  C  C   . LEU A 124 ? 0.66192 0.90216 0.67800 0.00942  -0.06612 -0.13855 106 LEU A C   
706  O  O   . LEU A 124 ? 0.67844 0.91880 0.69766 -0.00234 -0.05171 -0.13997 106 LEU A O   
707  C  CB  . LEU A 124 ? 0.72343 0.93084 0.68194 0.01873  -0.08849 -0.12706 106 LEU A CB  
708  C  CG  . LEU A 124 ? 0.84539 1.02444 0.78789 0.02230  -0.09174 -0.11087 106 LEU A CG  
709  C  CD1 . LEU A 124 ? 0.74896 0.92645 0.68840 0.03998  -0.11184 -0.11294 106 LEU A CD1 
710  C  CD2 . LEU A 124 ? 0.85866 1.00754 0.76279 0.01508  -0.09137 -0.09913 106 LEU A CD2 
711  N  N   . HIS A 125 ? 0.63216 0.87110 0.66135 0.01376  -0.06630 -0.13474 107 HIS A N   
712  C  CA  . HIS A 125 ? 0.54880 0.78414 0.59485 0.00491  -0.05024 -0.13072 107 HIS A CA  
713  C  C   . HIS A 125 ? 0.47684 0.68669 0.51131 0.00591  -0.04835 -0.11327 107 HIS A C   
714  O  O   . HIS A 125 ? 0.61163 0.81238 0.63921 0.01488  -0.05891 -0.10670 107 HIS A O   
715  C  CB  . HIS A 125 ? 0.57146 0.82474 0.64013 0.00641  -0.05018 -0.14045 107 HIS A CB  
716  C  CG  . HIS A 125 ? 0.71209 0.99274 0.79544 -0.00034 -0.04644 -0.15972 107 HIS A CG  
717  N  ND1 . HIS A 125 ? 0.71793 1.01641 0.79713 0.00314  -0.05585 -0.17145 107 HIS A ND1 
718  C  CD2 . HIS A 125 ? 0.59180 0.88411 0.69164 -0.01181 -0.03422 -0.17016 107 HIS A CD2 
719  C  CE1 . HIS A 125 ? 0.69611 1.01967 0.79164 -0.00636 -0.04885 -0.18916 107 HIS A CE1 
720  N  NE2 . HIS A 125 ? 0.58778 0.90651 0.69445 -0.01656 -0.03509 -0.18857 107 HIS A NE2 
721  N  N   . LEU A 126 ? 0.43713 0.63665 0.47005 -0.00308 -0.03511 -0.10742 108 LEU A N   
722  C  CA  . LEU A 126 ? 0.44928 0.62997 0.47369 -0.00437 -0.03143 -0.09377 108 LEU A CA  
723  C  C   . LEU A 126 ? 0.49993 0.67938 0.54321 -0.00809 -0.01970 -0.09223 108 LEU A C   
724  O  O   . LEU A 126 ? 0.52281 0.70569 0.57429 -0.01390 -0.00949 -0.09829 108 LEU A O   
725  C  CB  . LEU A 126 ? 0.54289 0.71483 0.54822 -0.01113 -0.02688 -0.09036 108 LEU A CB  
726  C  CG  . LEU A 126 ? 0.66082 0.82544 0.63829 -0.00871 -0.03904 -0.08964 108 LEU A CG  
727  C  CD1 . LEU A 126 ? 0.64048 0.79284 0.59639 -0.01881 -0.03185 -0.08481 108 LEU A CD1 
728  C  CD2 . LEU A 126 ? 0.70104 0.85249 0.66502 0.00151  -0.05450 -0.08278 108 LEU A CD2 
729  N  N   . GLY A 127 ? 0.43488 0.60637 0.48206 -0.00426 -0.02203 -0.08418 109 GLY A N   
730  C  CA  . GLY A 127 ? 0.46102 0.62883 0.52337 -0.00609 -0.01381 -0.08235 109 GLY A CA  
731  C  C   . GLY A 127 ? 0.47642 0.63369 0.53630 -0.00768 -0.00865 -0.07339 109 GLY A C   
732  O  O   . GLY A 127 ? 0.45237 0.60306 0.49925 -0.00747 -0.01283 -0.06594 109 GLY A O   
733  N  N   . PHE A 128 ? 0.50243 0.65728 0.57318 -0.00948 0.00001  -0.07536 110 PHE A N   
734  C  CA  . PHE A 128 ? 0.47666 0.62670 0.55086 -0.00927 0.00446  -0.07030 110 PHE A CA  
735  C  C   . PHE A 128 ? 0.50543 0.64750 0.59089 -0.00590 0.00595  -0.06930 110 PHE A C   
736  O  O   . PHE A 128 ? 0.50253 0.63998 0.59107 -0.00667 0.00925  -0.07548 110 PHE A O   
737  C  CB  . PHE A 128 ? 0.51549 0.67066 0.58964 -0.01254 0.01230  -0.07646 110 PHE A CB  
738  C  CG  . PHE A 128 ? 0.57280 0.73338 0.63206 -0.01788 0.01189  -0.07788 110 PHE A CG  
739  C  CD1 . PHE A 128 ? 0.54686 0.71131 0.60026 -0.01931 0.01002  -0.08402 110 PHE A CD1 
740  C  CD2 . PHE A 128 ? 0.50230 0.66329 0.55107 -0.02295 0.01362  -0.07387 110 PHE A CD2 
741  C  CE1 . PHE A 128 ? 0.61101 0.77772 0.64730 -0.02383 0.00835  -0.08512 110 PHE A CE1 
742  C  CE2 . PHE A 128 ? 0.61386 0.77464 0.64283 -0.02957 0.01328  -0.07475 110 PHE A CE2 
743  C  CZ  . PHE A 128 ? 0.54164 0.70434 0.56386 -0.02908 0.00991  -0.07989 110 PHE A CZ  
744  N  N   . LEU A 129 ? 0.40672 0.54453 0.49501 -0.00332 0.00353  -0.06172 111 LEU A N   
745  C  CA  . LEU A 129 ? 0.47434 0.60213 0.56972 0.00008  0.00308  -0.05950 111 LEU A CA  
746  C  C   . LEU A 129 ? 0.47055 0.59590 0.57276 0.00387  0.00617  -0.06066 111 LEU A C   
747  O  O   . LEU A 129 ? 0.42002 0.55539 0.52468 0.00330  0.00778  -0.06042 111 LEU A O   
748  C  CB  . LEU A 129 ? 0.42162 0.54646 0.51609 0.00150  -0.00291 -0.05135 111 LEU A CB  
749  C  CG  . LEU A 129 ? 0.47357 0.60256 0.56220 0.00122  -0.00870 -0.05140 111 LEU A CG  
750  C  CD1 . LEU A 129 ? 0.42739 0.55104 0.51509 0.00406  -0.01464 -0.04411 111 LEU A CD1 
751  C  CD2 . LEU A 129 ? 0.34061 0.47297 0.43255 -0.00088 -0.00692 -0.06039 111 LEU A CD2 
752  N  N   . CYS A 130 ? 0.40871 0.52006 0.51229 0.00749  0.00658  -0.06311 112 CYS A N   
753  C  CA  . CYS A 130 ? 0.50784 0.61380 0.61715 0.01494  0.00610  -0.06523 112 CYS A CA  
754  C  C   . CYS A 130 ? 0.60355 0.69509 0.71184 0.01840  0.00102  -0.05883 112 CYS A C   
755  O  O   . CYS A 130 ? 0.53167 0.60659 0.63111 0.01548  0.00057  -0.05753 112 CYS A O   
756  C  CB  . CYS A 130 ? 0.53850 0.63249 0.64382 0.01822  0.00892  -0.07412 112 CYS A CB  
757  S  SG  . CYS A 130 ? 0.53318 0.64425 0.64009 0.01466  0.01548  -0.08333 112 CYS A SG  
758  N  N   . GLU A 131 ? 0.62523 0.72419 0.74170 0.02288  -0.00214 -0.05585 113 GLU A N   
759  C  CA  . GLU A 131 ? 0.48404 0.56915 0.59954 0.02773  -0.00776 -0.05096 113 GLU A CA  
760  C  C   . GLU A 131 ? 0.60073 0.67919 0.71991 0.03921  -0.01148 -0.05741 113 GLU A C   
761  O  O   . GLU A 131 ? 0.47512 0.56884 0.60361 0.04341  -0.00941 -0.06583 113 GLU A O   
762  C  CB  . GLU A 131 ? 0.50720 0.60436 0.62849 0.02531  -0.01014 -0.04391 113 GLU A CB  
763  C  CG  . GLU A 131 ? 0.47729 0.57760 0.59283 0.01722  -0.00930 -0.03785 113 GLU A CG  
764  C  CD  . GLU A 131 ? 0.59843 0.70432 0.71536 0.01499  -0.01215 -0.03084 113 GLU A CD  
765  O  OE1 . GLU A 131 ? 0.53733 0.64790 0.66150 0.01811  -0.01383 -0.03108 113 GLU A OE1 
766  O  OE2 . GLU A 131 ? 0.49898 0.60432 0.60912 0.01062  -0.01338 -0.02610 113 GLU A OE2 
767  N  N   . TYR A 132 ? 0.59996 0.65443 0.71021 0.04488  -0.01768 -0.05451 114 TYR A N   
768  C  CA  . TYR A 132 ? 0.51928 0.56219 0.62918 0.05902  -0.02428 -0.06149 114 TYR A CA  
769  C  C   . TYR A 132 ? 0.61835 0.63801 0.71850 0.06607  -0.03370 -0.05666 114 TYR A C   
770  O  O   . TYR A 132 ? 0.59907 0.59678 0.68988 0.07875  -0.04140 -0.06176 114 TYR A O   
771  C  CB  . TYR A 132 ? 0.49974 0.52058 0.59568 0.06131  -0.02236 -0.06820 114 TYR A CB  
772  C  CG  . TYR A 132 ? 0.60497 0.60813 0.68378 0.04762  -0.01584 -0.06445 114 TYR A CG  
773  C  CD1 . TYR A 132 ? 0.70094 0.66695 0.75580 0.04430  -0.01791 -0.06107 114 TYR A CD1 
774  C  CD2 . TYR A 132 ? 0.57527 0.59905 0.66033 0.03727  -0.00771 -0.06583 114 TYR A CD2 
775  C  CE1 . TYR A 132 ? 0.70111 0.65573 0.74197 0.02954  -0.01051 -0.06070 114 TYR A CE1 
776  C  CE2 . TYR A 132 ? 0.65363 0.66689 0.72623 0.02532  -0.00236 -0.06537 114 TYR A CE2 
777  C  CZ  . TYR A 132 ? 0.67522 0.65621 0.72733 0.02076  -0.00299 -0.06363 114 TYR A CZ  
778  O  OH  . TYR A 132 ? 0.65254 0.62777 0.69387 0.00658  0.00382  -0.06607 114 TYR A OH  
779  N  N   . ASP A 133 ? 0.47456 0.49575 0.57435 0.05947  -0.03444 -0.04764 115 ASP A N   
780  C  CA  . ASP A 133 ? 0.70598 0.70539 0.79532 0.06541  -0.04345 -0.04309 115 ASP A CA  
781  C  C   . ASP A 133 ? 0.60983 0.63479 0.71891 0.07386  -0.04962 -0.04549 115 ASP A C   
782  O  O   . ASP A 133 ? 0.53448 0.59182 0.66147 0.06763  -0.04434 -0.04582 115 ASP A O   
783  C  CB  . ASP A 133 ? 0.59087 0.57652 0.66753 0.05283  -0.04042 -0.03347 115 ASP A CB  
784  C  CG  . ASP A 133 ? 0.60107 0.61608 0.69310 0.04353  -0.03477 -0.02916 115 ASP A CG  
785  O  OD1 . ASP A 133 ? 0.60269 0.63908 0.70521 0.04012  -0.02899 -0.03240 115 ASP A OD1 
786  O  OD2 . ASP A 133 ? 0.60934 0.62267 0.69983 0.03970  -0.03665 -0.02259 115 ASP A OD2 
787  N  N   . ALA A 134 ? 0.64954 0.65816 0.75269 0.08734  -0.06121 -0.04784 116 ALA A N   
788  C  CA  . ALA A 134 ? 0.71934 0.75399 0.84236 0.09730  -0.06867 -0.05359 116 ALA A CA  
789  C  C   . ALA A 134 ? 0.76871 0.79656 0.88648 0.09335  -0.07332 -0.04438 116 ALA A C   
790  O  O   . ALA A 134 ? 0.62626 0.63515 0.72855 0.08149  -0.06889 -0.03386 116 ALA A O   
791  C  CB  . ALA A 134 ? 0.71252 0.73772 0.83502 0.11858  -0.08103 -0.06537 116 ALA A CB  
792  N  N   . LEU A 135 ? 0.62073 0.66677 0.75272 0.10333  -0.08232 -0.05006 117 LEU A N   
793  C  CA  . LEU A 135 ? 0.68635 0.72992 0.81564 0.10032  -0.08739 -0.04301 117 LEU A CA  
794  C  C   . LEU A 135 ? 0.75756 0.77661 0.87406 0.11801  -0.10434 -0.04607 117 LEU A C   
795  O  O   . LEU A 135 ? 0.74071 0.76344 0.86343 0.13576  -0.11378 -0.05813 117 LEU A O   
796  C  CB  . LEU A 135 ? 0.60980 0.69805 0.76567 0.09374  -0.08314 -0.04724 117 LEU A CB  
797  C  CG  . LEU A 135 ? 0.69575 0.79953 0.85582 0.07477  -0.06856 -0.04103 117 LEU A CG  
798  C  CD1 . LEU A 135 ? 0.66360 0.80848 0.84558 0.06765  -0.06368 -0.04821 117 LEU A CD1 
799  C  CD2 . LEU A 135 ? 0.55465 0.63487 0.69723 0.06397  -0.06619 -0.02702 117 LEU A CD2 
800  N  N   . PRO A 136 ? 0.77069 0.76337 0.86774 0.11449  -0.10941 -0.03619 118 PRO A N   
801  C  CA  . PRO A 136 ? 0.74375 0.70590 0.82163 0.13115  -0.12709 -0.03789 118 PRO A CA  
802  C  C   . PRO A 136 ? 0.67643 0.67418 0.78069 0.14756  -0.13912 -0.05109 118 PRO A C   
803  O  O   . PRO A 136 ? 0.70255 0.73800 0.83018 0.13999  -0.13521 -0.05264 118 PRO A O   
804  C  CB  . PRO A 136 ? 0.68915 0.62486 0.74469 0.11879  -0.12642 -0.02456 118 PRO A CB  
805  C  CG  . PRO A 136 ? 0.91777 0.86014 0.97520 0.09765  -0.10847 -0.01667 118 PRO A CG  
806  C  CD  . PRO A 136 ? 0.75235 0.73964 0.84167 0.09570  -0.09982 -0.02376 118 PRO A CD  
807  N  N   . GLY A 137 ? 0.73306 0.71870 0.83275 0.17001  -0.15397 -0.06201 119 GLY A N   
808  C  CA  . GLY A 137 ? 0.88013 0.89921 1.00444 0.18951  -0.16867 -0.07798 119 GLY A CA  
809  C  C   . GLY A 137 ? 0.87248 0.95001 1.03800 0.19279  -0.16236 -0.09577 119 GLY A C   
810  O  O   . GLY A 137 ? 0.90416 0.99528 1.08251 0.21534  -0.17518 -0.11322 119 GLY A O   
811  N  N   . ILE A 138 ? 0.71549 0.82700 0.90024 0.17047  -0.14297 -0.09263 120 ILE A N   
812  C  CA  . ILE A 138 ? 0.73720 0.90512 0.95831 0.16852  -0.13459 -0.10961 120 ILE A CA  
813  C  C   . ILE A 138 ? 0.69358 0.85992 0.91509 0.16738  -0.12470 -0.11332 120 ILE A C   
814  O  O   . ILE A 138 ? 0.73452 0.94529 0.98371 0.16619  -0.11746 -0.12895 120 ILE A O   
815  C  CB  . ILE A 138 ? 0.70589 0.90958 0.94347 0.14400  -0.11959 -0.10565 120 ILE A CB  
816  C  CG1 . ILE A 138 ? 0.74593 0.91751 0.95936 0.12371  -0.10767 -0.08378 120 ILE A CG1 
817  C  CG2 . ILE A 138 ? 0.74752 0.97243 0.99717 0.14735  -0.12947 -0.11116 120 ILE A CG2 
818  C  CD1 . ILE A 138 ? 0.55169 0.74757 0.77376 0.10154  -0.09555 -0.07834 120 ILE A CD1 
819  N  N   . GLY A 139 ? 0.63582 0.75365 0.82706 0.16625  -0.12344 -0.10077 121 GLY A N   
820  C  CA  . GLY A 139 ? 0.52432 0.63820 0.71394 0.16528  -0.11479 -0.10450 121 GLY A CA  
821  C  C   . GLY A 139 ? 0.65698 0.79084 0.85372 0.14071  -0.09471 -0.09732 121 GLY A C   
822  O  O   . GLY A 139 ? 0.56721 0.69178 0.75390 0.12417  -0.08806 -0.08257 121 GLY A O   
823  N  N   . HIS A 140 ? 0.52287 0.68337 0.73561 0.13893  -0.08578 -0.10845 122 HIS A N   
824  C  CA  . HIS A 140 ? 0.67106 0.84489 0.88520 0.11715  -0.06831 -0.10204 122 HIS A CA  
825  C  C   . HIS A 140 ? 0.60565 0.82436 0.84142 0.10289  -0.05976 -0.10689 122 HIS A C   
826  O  O   . HIS A 140 ? 0.58659 0.83802 0.83758 0.09502  -0.04958 -0.11758 122 HIS A O   
827  C  CB  . HIS A 140 ? 0.56175 0.73672 0.77681 0.12017  -0.06245 -0.11060 122 HIS A CB  
828  C  CG  . HIS A 140 ? 0.66392 0.79426 0.85113 0.11767  -0.06102 -0.09893 122 HIS A CG  
829  N  ND1 . HIS A 140 ? 0.59507 0.71276 0.76856 0.09943  -0.05167 -0.08411 122 HIS A ND1 
830  C  CD2 . HIS A 140 ? 0.57192 0.66675 0.74108 0.13056  -0.06801 -0.10114 122 HIS A CD2 
831  C  CE1 . HIS A 140 ? 0.63188 0.71342 0.78322 0.09983  -0.05178 -0.07897 122 HIS A CE1 
832  N  NE2 . HIS A 140 ? 0.59853 0.66303 0.74466 0.11733  -0.06104 -0.08829 122 HIS A NE2 
833  N  N   . ALA A 141 ? 0.59724 0.81440 0.83088 0.09771  -0.06337 -0.09882 123 ALA A N   
834  C  CA  . ALA A 141 ? 0.49652 0.75004 0.74558 0.08266  -0.05600 -0.10266 123 ALA A CA  
835  C  C   . ALA A 141 ? 0.57821 0.82909 0.81539 0.05952  -0.04150 -0.09105 123 ALA A C   
836  O  O   . ALA A 141 ? 0.59589 0.87112 0.83939 0.04392  -0.03383 -0.09357 123 ALA A O   
837  C  CB  . ALA A 141 ? 0.54406 0.79394 0.79284 0.08557  -0.06571 -0.09830 123 ALA A CB  
838  N  N   . CYS A 142 ? 0.47232 0.69304 0.69048 0.05683  -0.03828 -0.07929 124 CYS A N   
839  C  CA  . CYS A 142 ? 0.55600 0.77346 0.76197 0.03875  -0.02692 -0.07048 124 CYS A CA  
840  C  C   . CYS A 142 ? 0.53966 0.76680 0.74748 0.03663  -0.01903 -0.07811 124 CYS A C   
841  O  O   . CYS A 142 ? 0.44944 0.67103 0.64434 0.02346  -0.01107 -0.07139 124 CYS A O   
842  C  CB  . CYS A 142 ? 0.48335 0.66468 0.66799 0.03627  -0.02913 -0.05345 124 CYS A CB  
843  S  SG  . CYS A 142 ? 0.70683 0.88116 0.87442 0.01723  -0.02042 -0.04166 124 CYS A SG  
844  N  N   . GLY A 143 ? 0.42739 0.66775 0.64966 0.05023  -0.02202 -0.09262 125 GLY A N   
845  C  CA  . GLY A 143 ? 0.44679 0.69735 0.67150 0.04854  -0.01431 -0.10137 125 GLY A CA  
846  C  C   . GLY A 143 ? 0.53296 0.75228 0.73806 0.04743  -0.01270 -0.09075 125 GLY A C   
847  O  O   . GLY A 143 ? 0.49683 0.72210 0.69731 0.03818  -0.00393 -0.09243 125 GLY A O   
848  N  N   . HIS A 144 ? 0.47894 0.66556 0.67124 0.05538  -0.02062 -0.08090 126 HIS A N   
849  C  CA  . HIS A 144 ? 0.42062 0.58079 0.59522 0.05215  -0.01823 -0.07282 126 HIS A CA  
850  C  C   . HIS A 144 ? 0.49250 0.65002 0.66765 0.05958  -0.01653 -0.08304 126 HIS A C   
851  O  O   . HIS A 144 ? 0.51088 0.65767 0.67483 0.05296  -0.01124 -0.07983 126 HIS A O   
852  C  CB  . HIS A 144 ? 0.45105 0.57855 0.61089 0.05594  -0.02541 -0.06216 126 HIS A CB  
853  C  CG  . HIS A 144 ? 0.47709 0.60155 0.63068 0.04513  -0.02434 -0.05016 126 HIS A CG  
854  N  ND1 . HIS A 144 ? 0.55566 0.65429 0.69476 0.04328  -0.02704 -0.04077 126 HIS A ND1 
855  C  CD2 . HIS A 144 ? 0.42763 0.57007 0.58556 0.03516  -0.02071 -0.04705 126 HIS A CD2 
856  C  CE1 . HIS A 144 ? 0.59194 0.69463 0.72930 0.03484  -0.02596 -0.03290 126 HIS A CE1 
857  N  NE2 . HIS A 144 ? 0.47610 0.60243 0.62284 0.02990  -0.02255 -0.03576 126 HIS A NE2 
858  N  N   . ASN A 145 ? 0.42254 0.59037 0.61066 0.07392  -0.02155 -0.09653 127 ASN A N   
859  C  CA  . ASN A 145 ? 0.49777 0.66621 0.68772 0.08121  -0.01939 -0.10841 127 ASN A CA  
860  C  C   . ASN A 145 ? 0.50487 0.69929 0.70022 0.06702  -0.00672 -0.11282 127 ASN A C   
861  O  O   . ASN A 145 ? 0.44070 0.62699 0.62841 0.06537  -0.00204 -0.11554 127 ASN A O   
862  C  CB  . ASN A 145 ? 0.51996 0.70099 0.72612 0.10093  -0.02814 -0.12494 127 ASN A CB  
863  C  CG  . ASN A 145 ? 0.49770 0.72387 0.72927 0.09829  -0.02590 -0.13533 127 ASN A CG  
864  O  OD1 . ASN A 145 ? 0.50231 0.73319 0.73665 0.09479  -0.02934 -0.12884 127 ASN A OD1 
865  N  ND2 . ASN A 145 ? 0.49139 0.75186 0.74111 0.09841  -0.01923 -0.15280 127 ASN A ND2 
866  N  N   . LEU A 146 ? 0.43168 0.65490 0.63684 0.05521  -0.00085 -0.11361 128 LEU A N   
867  C  CA  . LEU A 146 ? 0.50196 0.74483 0.70569 0.03948  0.01113  -0.11698 128 LEU A CA  
868  C  C   . LEU A 146 ? 0.47699 0.69828 0.65866 0.02700  0.01427  -0.10160 128 LEU A C   
869  O  O   . LEU A 146 ? 0.48864 0.71467 0.66270 0.01776  0.02166  -0.10363 128 LEU A O   
870  C  CB  . LEU A 146 ? 0.40606 0.68220 0.62167 0.02815  0.01705  -0.12346 128 LEU A CB  
871  C  CG  . LEU A 146 ? 0.39765 0.70435 0.63973 0.03997  0.01359  -0.14187 128 LEU A CG  
872  C  CD1 . LEU A 146 ? 0.32794 0.66840 0.57960 0.02370  0.02150  -0.14845 128 LEU A CD1 
873  C  CD2 . LEU A 146 ? 0.34433 0.66600 0.59956 0.05138  0.01525  -0.16056 128 LEU A CD2 
874  N  N   . ILE A 147 ? 0.42261 0.62143 0.59395 0.02720  0.00821  -0.08766 129 ILE A N   
875  C  CA  . ILE A 147 ? 0.46979 0.65112 0.62306 0.01840  0.00941  -0.07605 129 ILE A CA  
876  C  C   . ILE A 147 ? 0.53007 0.69689 0.67675 0.02248  0.01003  -0.07890 129 ILE A C   
877  O  O   . ILE A 147 ? 0.53068 0.69762 0.66774 0.01462  0.01428  -0.07793 129 ILE A O   
878  C  CB  . ILE A 147 ? 0.53001 0.69421 0.67650 0.01841  0.00305  -0.06340 129 ILE A CB  
879  C  CG1 . ILE A 147 ? 0.41931 0.59665 0.56965 0.01216  0.00324  -0.06064 129 ILE A CG1 
880  C  CG2 . ILE A 147 ? 0.45434 0.60394 0.58527 0.01214  0.00291  -0.05480 129 ILE A CG2 
881  C  CD1 . ILE A 147 ? 0.43196 0.59297 0.57388 0.01063  -0.00223 -0.04830 129 ILE A CD1 
882  N  N   . ALA A 148 ? 0.49813 0.64980 0.64697 0.03440  0.00525  -0.08278 130 ALA A N   
883  C  CA  . ALA A 148 ? 0.47468 0.61051 0.61498 0.03689  0.00682  -0.08731 130 ALA A CA  
884  C  C   . ALA A 148 ? 0.50631 0.66101 0.65205 0.03476  0.01387  -0.09852 130 ALA A C   
885  O  O   . ALA A 148 ? 0.51345 0.66394 0.64995 0.02847  0.01828  -0.09939 130 ALA A O   
886  C  CB  . ALA A 148 ? 0.50575 0.61716 0.64240 0.05025  -0.00014 -0.09058 130 ALA A CB  
887  N  N   . GLU A 149 ? 0.44963 0.62767 0.61101 0.03929  0.01529  -0.10872 131 GLU A N   
888  C  CA  . GLU A 149 ? 0.46266 0.66153 0.63045 0.03671  0.02306  -0.12179 131 GLU A CA  
889  C  C   . GLU A 149 ? 0.40949 0.61859 0.56687 0.01928  0.03092  -0.11688 131 GLU A C   
890  O  O   . GLU A 149 ? 0.41508 0.62386 0.56505 0.01462  0.03602  -0.12113 131 GLU A O   
891  C  CB  . GLU A 149 ? 0.36113 0.58913 0.55031 0.04345  0.02355  -0.13584 131 GLU A CB  
892  C  CG  . GLU A 149 ? 0.46853 0.71475 0.66787 0.04797  0.02921  -0.15432 131 GLU A CG  
893  C  CD  . GLU A 149 ? 0.44074 0.72727 0.66329 0.04874  0.03308  -0.17080 131 GLU A CD  
894  O  OE1 . GLU A 149 ? 0.38278 0.68002 0.61567 0.05093  0.02850  -0.16947 131 GLU A OE1 
895  O  OE2 . GLU A 149 ? 0.38839 0.69796 0.61957 0.04649  0.04116  -0.18672 131 GLU A OE2 
896  N  N   . VAL A 150 ? 0.45670 0.67185 0.61035 0.00970  0.03111  -0.10795 132 VAL A N   
897  C  CA  . VAL A 150 ? 0.49676 0.71617 0.63479 -0.00611 0.03670  -0.10312 132 VAL A CA  
898  C  C   . VAL A 150 ? 0.51576 0.71485 0.63706 -0.00796 0.03357  -0.09464 132 VAL A C   
899  O  O   . VAL A 150 ? 0.48068 0.68168 0.58909 -0.01654 0.03751  -0.09581 132 VAL A O   
900  C  CB  . VAL A 150 ? 0.54050 0.76434 0.67415 -0.01518 0.03634  -0.09541 132 VAL A CB  
901  C  CG1 . VAL A 150 ? 0.61248 0.81359 0.73485 -0.01366 0.02808  -0.08008 132 VAL A CG1 
902  C  CG2 . VAL A 150 ? 0.65649 0.89007 0.77473 -0.03267 0.04469  -0.09712 132 VAL A CG2 
903  N  N   . GLY A 151 ? 0.51975 0.70061 0.64064 -0.00057 0.02664  -0.08772 133 GLY A N   
904  C  CA  . GLY A 151 ? 0.42378 0.59129 0.53254 -0.00272 0.02427  -0.08340 133 GLY A CA  
905  C  C   . GLY A 151 ? 0.55289 0.71911 0.66106 -0.00141 0.02839  -0.09312 133 GLY A C   
906  O  O   . GLY A 151 ? 0.51701 0.68366 0.61481 -0.00744 0.02966  -0.09393 133 GLY A O   
907  N  N   . ALA A 152 ? 0.53971 0.70294 0.65750 0.00732  0.02950  -0.10129 134 ALA A N   
908  C  CA  . ALA A 152 ? 0.56661 0.72638 0.68222 0.00886  0.03371  -0.11169 134 ALA A CA  
909  C  C   . ALA A 152 ? 0.51664 0.69710 0.63226 0.00181  0.04097  -0.11935 134 ALA A C   
910  O  O   . ALA A 152 ? 0.55890 0.73852 0.66586 -0.00339 0.04453  -0.12364 134 ALA A O   
911  C  CB  . ALA A 152 ? 0.48911 0.63719 0.61185 0.02209  0.03137  -0.11935 134 ALA A CB  
912  N  N   . ALA A 153 ? 0.46747 0.66716 0.59149 -0.00020 0.04390  -0.12204 135 ALA A N   
913  C  CA  . ALA A 153 ? 0.45944 0.67923 0.58210 -0.00912 0.05261  -0.13133 135 ALA A CA  
914  C  C   . ALA A 153 ? 0.54051 0.75718 0.64197 -0.02281 0.05374  -0.12352 135 ALA A C   
915  O  O   . ALA A 153 ? 0.52937 0.74983 0.62179 -0.02903 0.05878  -0.12972 135 ALA A O   
916  C  CB  . ALA A 153 ? 0.45601 0.69894 0.59203 -0.01092 0.05657  -0.13767 135 ALA A CB  
917  N  N   . ALA A 154 ? 0.48880 0.69689 0.58040 -0.02661 0.04798  -0.11040 136 ALA A N   
918  C  CA  . ALA A 154 ? 0.55904 0.75946 0.62726 -0.03627 0.04553  -0.10287 136 ALA A CA  
919  C  C   . ALA A 154 ? 0.52508 0.71833 0.58715 -0.03420 0.04300  -0.10510 136 ALA A C   
920  O  O   . ALA A 154 ? 0.57472 0.76957 0.62122 -0.04173 0.04495  -0.10781 136 ALA A O   
921  C  CB  . ALA A 154 ? 0.46179 0.65002 0.52163 -0.03607 0.03715  -0.08936 136 ALA A CB  
922  N  N   . ALA A 155 ? 0.54284 0.72766 0.61521 -0.02545 0.03905  -0.10487 137 ALA A N   
923  C  CA  . ALA A 155 ? 0.59175 0.77147 0.65893 -0.02566 0.03756  -0.10864 137 ALA A CA  
924  C  C   . ALA A 155 ? 0.58135 0.76664 0.64935 -0.02772 0.04550  -0.12084 137 ALA A C   
925  O  O   . ALA A 155 ? 0.64400 0.83081 0.70154 -0.03295 0.04600  -0.12481 137 ALA A O   
926  C  CB  . ALA A 155 ? 0.43784 0.60581 0.51302 -0.01940 0.03371  -0.10693 137 ALA A CB  
927  N  N   . LEU A 156 ? 0.55031 0.73936 0.63095 -0.02261 0.05091  -0.12820 138 LEU A N   
928  C  CA  . LEU A 156 ? 0.56849 0.76398 0.65034 -0.02356 0.05853  -0.14139 138 LEU A CA  
929  C  C   . LEU A 156 ? 0.61500 0.82440 0.68449 -0.03530 0.06368  -0.14382 138 LEU A C   
930  O  O   . LEU A 156 ? 0.59973 0.81036 0.66013 -0.04040 0.06717  -0.15050 138 LEU A O   
931  C  CB  . LEU A 156 ? 0.57917 0.77926 0.67800 -0.01349 0.06154  -0.15054 138 LEU A CB  
932  C  CG  . LEU A 156 ? 0.66749 0.84885 0.76961 -0.00271 0.06010  -0.15757 138 LEU A CG  
933  C  CD1 . LEU A 156 ? 0.65278 0.81168 0.75002 0.00022  0.05279  -0.14706 138 LEU A CD1 
934  C  CD2 . LEU A 156 ? 0.58042 0.76801 0.69824 0.01007  0.06084  -0.16890 138 LEU A CD2 
935  N  N   . GLY A 157 ? 0.57362 0.79113 0.63931 -0.04123 0.06441  -0.13852 139 GLY A N   
936  C  CA  . GLY A 157 ? 0.56183 0.78733 0.60937 -0.05500 0.06996  -0.14050 139 GLY A CA  
937  C  C   . GLY A 157 ? 0.67608 0.88978 0.69955 -0.06070 0.06352  -0.13362 139 GLY A C   
938  O  O   . GLY A 157 ? 0.64243 0.85890 0.64995 -0.06965 0.06773  -0.13901 139 GLY A O   
939  N  N   . VAL A 158 ? 0.64184 0.84348 0.66249 -0.05499 0.05265  -0.12304 140 VAL A N   
940  C  CA  . VAL A 158 ? 0.65700 0.85057 0.65756 -0.05720 0.04400  -0.11885 140 VAL A CA  
941  C  C   . VAL A 158 ? 0.73233 0.93045 0.73565 -0.05704 0.04653  -0.12926 140 VAL A C   
942  O  O   . VAL A 158 ? 0.67892 0.87752 0.66369 -0.06355 0.04561  -0.13233 140 VAL A O   
943  C  CB  . VAL A 158 ? 0.59286 0.77743 0.59510 -0.04928 0.03196  -0.10895 140 VAL A CB  
944  C  CG1 . VAL A 158 ? 0.52484 0.70641 0.51187 -0.04822 0.02160  -0.10896 140 VAL A CG1 
945  C  CG2 . VAL A 158 ? 0.69613 0.87277 0.68948 -0.05096 0.02880  -0.09830 140 VAL A CG2 
946  N  N   . ARG A 159 ? 0.59584 0.79446 0.61910 -0.05038 0.04960  -0.13499 141 ARG A N   
947  C  CA  . ARG A 159 ? 0.70022 0.89985 0.72413 -0.05168 0.05266  -0.14532 141 ARG A CA  
948  C  C   . ARG A 159 ? 0.67254 0.87959 0.68937 -0.05856 0.06193  -0.15517 141 ARG A C   
949  O  O   . ARG A 159 ? 0.68445 0.89374 0.68915 -0.06425 0.06194  -0.16073 141 ARG A O   
950  C  CB  . ARG A 159 ? 0.65666 0.84807 0.69690 -0.04488 0.05524  -0.14952 141 ARG A CB  
951  C  CG  . ARG A 159 ? 0.72033 0.90900 0.75920 -0.04755 0.06174  -0.16214 141 ARG A CG  
952  C  CD  . ARG A 159 ? 0.69225 0.86404 0.73867 -0.04233 0.06333  -0.16565 141 ARG A CD  
953  N  NE  . ARG A 159 ? 0.69965 0.86440 0.74146 -0.04482 0.07025  -0.17819 141 ARG A NE  
954  C  CZ  . ARG A 159 ? 0.78071 0.92414 0.82066 -0.04263 0.07250  -0.18343 141 ARG A CZ  
955  N  NH1 . ARG A 159 ? 0.78764 0.91477 0.82938 -0.03871 0.06874  -0.17732 141 ARG A NH1 
956  N  NH2 . ARG A 159 ? 0.86131 0.99637 0.89404 -0.04529 0.07870  -0.19519 141 ARG A NH2 
957  N  N   . GLY A 160 ? 0.68579 0.89915 0.71079 -0.05838 0.06991  -0.15900 142 GLY A N   
958  C  CA  . GLY A 160 ? 0.66594 0.88964 0.68656 -0.06528 0.08011  -0.17085 142 GLY A CA  
959  C  C   . GLY A 160 ? 0.69785 0.92384 0.69225 -0.07839 0.08022  -0.16818 142 GLY A C   
960  O  O   . GLY A 160 ? 0.83215 1.06321 0.81637 -0.08587 0.08654  -0.17760 142 GLY A O   
961  N  N   . ALA A 161 ? 0.64948 0.86838 0.62925 -0.08149 0.07282  -0.15548 143 ALA A N   
962  C  CA  . ALA A 161 ? 0.75105 0.96334 0.69780 -0.09345 0.07035  -0.15142 143 ALA A CA  
963  C  C   . ALA A 161 ? 0.82553 1.03161 0.75814 -0.09187 0.06064  -0.15132 143 ALA A C   
964  O  O   . ALA A 161 ? 0.90962 1.11337 0.81786 -0.10114 0.06137  -0.15478 143 ALA A O   
965  C  CB  . ALA A 161 ? 0.68653 0.88664 0.61737 -0.09610 0.06365  -0.13782 143 ALA A CB  
966  N  N   . LEU A 162 ? 0.72805 0.93282 0.67528 -0.08108 0.05170  -0.14876 144 LEU A N   
967  C  CA  . LEU A 162 ? 0.85774 1.06278 0.79701 -0.07912 0.04230  -0.15164 144 LEU A CA  
968  C  C   . LEU A 162 ? 0.92519 1.13898 0.87530 -0.08132 0.05051  -0.16534 144 LEU A C   
969  O  O   . LEU A 162 ? 0.92355 1.14055 0.86200 -0.08427 0.04569  -0.17083 144 LEU A O   
970  C  CB  . LEU A 162 ? 0.76823 0.97194 0.71937 -0.06867 0.03043  -0.14578 144 LEU A CB  
971  C  CG  . LEU A 162 ? 0.77810 0.97055 0.71666 -0.06469 0.01985  -0.13256 144 LEU A CG  
972  C  CD1 . LEU A 162 ? 0.57298 0.76747 0.53029 -0.05417 0.01160  -0.12917 144 LEU A CD1 
973  C  CD2 . LEU A 162 ? 0.69470 0.87656 0.59828 -0.06721 0.00806  -0.12894 144 LEU A CD2 
974  N  N   . GLU A 163 ? 0.87920 1.09542 0.84978 -0.07920 0.06167  -0.17162 145 GLU A N   
975  C  CA  . GLU A 163 ? 0.88348 1.10247 0.86039 -0.08122 0.06965  -0.18496 145 GLU A CA  
976  C  C   . GLU A 163 ? 0.98225 1.20687 0.94275 -0.09108 0.07698  -0.19307 145 GLU A C   
977  O  O   . GLU A 163 ? 1.10345 1.33032 1.05788 -0.09555 0.07884  -0.20243 145 GLU A O   
978  C  CB  . GLU A 163 ? 0.78377 0.99822 0.78209 -0.07400 0.07745  -0.18959 145 GLU A CB  
979  C  CG  . GLU A 163 ? 0.88070 1.08525 0.88825 -0.06990 0.07555  -0.19248 145 GLU A CG  
980  C  CD  . GLU A 163 ? 0.96717 1.15960 0.98920 -0.06115 0.08042  -0.19512 145 GLU A CD  
981  O  OE1 . GLU A 163 ? 1.01016 1.20712 1.03877 -0.05713 0.08570  -0.19821 145 GLU A OE1 
982  O  OE2 . GLU A 163 ? 1.08369 1.26184 1.10908 -0.05855 0.07862  -0.19516 145 GLU A OE2 
983  N  N   . GLY A 164 ? 1.03559 1.26293 0.98785 -0.09629 0.08216  -0.19070 146 GLY A N   
984  C  CA  . GLY A 164 ? 1.09892 1.33149 1.03271 -0.10823 0.09041  -0.19870 146 GLY A CA  
985  C  C   . GLY A 164 ? 1.32207 1.54684 1.22214 -0.11646 0.08093  -0.19149 146 GLY A C   
986  O  O   . GLY A 164 ? 1.43159 1.65214 1.30853 -0.12693 0.08389  -0.18814 146 GLY A O   
987  N  N   . LEU A 165 ? 1.28452 1.50649 1.17950 -0.11219 0.06905  -0.19017 147 LEU A N   
988  C  CA  . LEU A 165 ? 1.30716 1.52050 1.16989 -0.11576 0.05586  -0.18435 147 LEU A CA  
989  C  C   . LEU A 165 ? 1.34766 1.56810 1.20590 -0.11744 0.05254  -0.19493 147 LEU A C   
990  O  O   . LEU A 165 ? 1.27849 1.50770 1.15971 -0.11143 0.05171  -0.20114 147 LEU A O   
991  C  CB  . LEU A 165 ? 1.19723 1.40245 1.05880 -0.10530 0.03944  -0.17178 147 LEU A CB  
992  C  CG  . LEU A 165 ? 1.03396 1.22101 0.86754 -0.10873 0.03385  -0.15878 147 LEU A CG  
993  N  N   . PRO A 166 ? 1.43772 1.65368 1.26480 -0.12699 0.05098  -0.19787 148 PRO A N   
994  C  CA  . PRO A 166 ? 1.47421 1.69834 1.29612 -0.12894 0.04687  -0.20870 148 PRO A CA  
995  C  C   . PRO A 166 ? 1.51152 1.73571 1.32372 -0.11997 0.02537  -0.20511 148 PRO A C   
996  O  O   . PRO A 166 ? 1.50649 1.74531 1.34039 -0.11411 0.02090  -0.21263 148 PRO A O   
997  C  CB  . PRO A 166 ? 1.46208 1.68018 1.25211 -0.14329 0.05416  -0.21315 148 PRO A CB  
998  C  CG  . PRO A 166 ? 1.45943 1.66311 1.23003 -0.14954 0.05800  -0.20256 148 PRO A CG  
999  C  CD  . PRO A 166 ? 1.52686 1.72842 1.31877 -0.13823 0.05311  -0.19184 148 PRO A CD  
1000 N  N   . ARG A 167 ? 1.54440 1.75160 1.32228 -0.11921 0.01185  -0.19506 149 ARG A N   
1001 C  CA  . ARG A 167 ? 1.56049 1.76556 1.32691 -0.10701 -0.01167 -0.19180 149 ARG A CA  
1002 C  C   . ARG A 167 ? 1.47932 1.69803 1.28269 -0.09415 -0.01618 -0.19102 149 ARG A C   
1003 O  O   . ARG A 167 ? 1.29266 1.50502 1.10981 -0.09213 -0.00942 -0.18217 149 ARG A O   
1004 C  CB  . ARG A 167 ? 1.35975 1.53499 1.08224 -0.10653 -0.02456 -0.17805 149 ARG A CB  
1005 N  N   . PRO A 168 ? 1.46391 1.70299 1.28416 -0.08686 -0.02632 -0.20148 150 PRO A N   
1006 C  CA  . PRO A 168 ? 1.44349 1.69801 1.29891 -0.07781 -0.02821 -0.20353 150 PRO A CA  
1007 C  C   . PRO A 168 ? 1.35542 1.59484 1.20961 -0.06854 -0.03484 -0.18871 150 PRO A C   
1008 O  O   . PRO A 168 ? 1.30877 1.53287 1.13552 -0.06080 -0.05195 -0.18086 150 PRO A O   
1009 C  CB  . PRO A 168 ? 1.35363 1.62994 1.21229 -0.07022 -0.04577 -0.21632 150 PRO A CB  
1010 C  CG  . PRO A 168 ? 1.39532 1.66900 1.22417 -0.07695 -0.04982 -0.22260 150 PRO A CG  
1011 C  CD  . PRO A 168 ? 1.28315 1.53621 1.09468 -0.09016 -0.03214 -0.21523 150 PRO A CD  
1012 N  N   . PRO A 169 ? 1.42438 1.66451 1.30489 -0.06886 -0.02241 -0.18457 151 PRO A N   
1013 C  CA  . PRO A 169 ? 1.29649 1.52091 1.17449 -0.06222 -0.02640 -0.17013 151 PRO A CA  
1014 C  C   . PRO A 169 ? 1.14763 1.37955 1.03407 -0.04785 -0.04445 -0.17014 151 PRO A C   
1015 O  O   . PRO A 169 ? 1.11109 1.36672 1.01800 -0.04441 -0.04869 -0.18304 151 PRO A O   
1016 C  CB  . PRO A 169 ? 1.20867 1.43468 1.11416 -0.06672 -0.00766 -0.16870 151 PRO A CB  
1017 C  CG  . PRO A 169 ? 1.28931 1.53270 1.21640 -0.07103 0.00077  -0.18304 151 PRO A CG  
1018 C  CD  . PRO A 169 ? 1.36836 1.62114 1.27930 -0.07471 -0.00593 -0.19345 151 PRO A CD  
1019 N  N   . PRO A 170 ? 1.19657 1.40961 1.06691 -0.03972 -0.05551 -0.15754 152 PRO A N   
1020 C  CA  . PRO A 170 ? 1.16377 1.38412 1.04309 -0.02415 -0.07325 -0.15880 152 PRO A CA  
1021 C  C   . PRO A 170 ? 0.98172 1.22288 0.90196 -0.02341 -0.06383 -0.16438 152 PRO A C   
1022 O  O   . PRO A 170 ? 0.82996 1.06835 0.76554 -0.03232 -0.04567 -0.16095 152 PRO A O   
1023 C  CB  . PRO A 170 ? 1.12610 1.31468 0.97747 -0.01882 -0.08208 -0.14220 152 PRO A CB  
1024 C  CG  . PRO A 170 ? 1.11036 1.27581 0.92782 -0.03236 -0.07380 -0.13499 152 PRO A CG  
1025 C  CD  . PRO A 170 ? 1.17458 1.35843 1.01551 -0.04551 -0.05213 -0.14314 152 PRO A CD  
1026 N  N   . PRO A 171 ? 0.88467 1.14699 0.82241 -0.01302 -0.07595 -0.17443 153 PRO A N   
1027 C  CA  . PRO A 171 ? 0.91741 1.19870 0.89059 -0.01534 -0.06592 -0.18118 153 PRO A CA  
1028 C  C   . PRO A 171 ? 0.80081 1.06460 0.77974 -0.01303 -0.06066 -0.16678 153 PRO A C   
1029 O  O   . PRO A 171 ? 0.84066 1.09683 0.81328 -0.00106 -0.07428 -0.16042 153 PRO A O   
1030 C  CB  . PRO A 171 ? 0.92255 1.23224 0.90913 -0.00411 -0.08255 -0.19665 153 PRO A CB  
1031 C  CG  . PRO A 171 ? 0.91755 1.22646 0.87809 0.00329  -0.10010 -0.20084 153 PRO A CG  
1032 C  CD  . PRO A 171 ? 0.95560 1.22616 0.88065 0.00143  -0.09988 -0.18195 153 PRO A CD  
1033 N  N   . VAL A 172 ? 0.74914 1.00528 0.73869 -0.02343 -0.04202 -0.16219 154 VAL A N   
1034 C  CA  . VAL A 172 ? 0.75648 0.99718 0.75231 -0.02209 -0.03613 -0.14942 154 VAL A CA  
1035 C  C   . VAL A 172 ? 0.67953 0.92602 0.69947 -0.02943 -0.02103 -0.15448 154 VAL A C   
1036 O  O   . VAL A 172 ? 0.72023 0.97067 0.74380 -0.03860 -0.01026 -0.16284 154 VAL A O   
1037 C  CB  . VAL A 172 ? 0.76555 0.98341 0.74110 -0.02641 -0.03036 -0.13634 154 VAL A CB  
1038 C  CG1 . VAL A 172 ? 0.62533 0.83136 0.61035 -0.02550 -0.02398 -0.12527 154 VAL A CG1 
1039 C  CG2 . VAL A 172 ? 0.84073 1.04473 0.78383 -0.02178 -0.04501 -0.13039 154 VAL A CG2 
1040 N  N   . LYS A 173 ? 0.63396 0.87752 0.66694 -0.02561 -0.02075 -0.14950 155 LYS A N   
1041 C  CA  . LYS A 173 ? 0.61550 0.85461 0.66401 -0.03219 -0.00734 -0.15069 155 LYS A CA  
1042 C  C   . LYS A 173 ? 0.63732 0.85754 0.68531 -0.02860 -0.00441 -0.13596 155 LYS A C   
1043 O  O   . LYS A 173 ? 0.65655 0.87399 0.70381 -0.02110 -0.01315 -0.12831 155 LYS A O   
1044 C  CB  . LYS A 173 ? 0.57343 0.82877 0.63813 -0.03360 -0.00857 -0.16138 155 LYS A CB  
1045 C  CG  . LYS A 173 ? 0.71403 0.95893 0.78725 -0.04309 0.00539  -0.16345 155 LYS A CG  
1046 C  CD  . LYS A 173 ? 0.73675 0.99777 0.82297 -0.04772 0.00557  -0.17486 155 LYS A CD  
1047 C  CE  . LYS A 173 ? 0.88698 1.16229 0.97524 -0.06122 0.01305  -0.19277 155 LYS A CE  
1048 N  NZ  . LYS A 173 ? 0.81849 1.11966 0.92077 -0.06653 0.01187  -0.20808 155 LYS A NZ  
1049 N  N   . VAL A 174 ? 0.51515 0.72318 0.56359 -0.03318 0.00710  -0.13334 156 VAL A N   
1050 C  CA  . VAL A 174 ? 0.54204 0.73605 0.59332 -0.02997 0.01050  -0.12233 156 VAL A CA  
1051 C  C   . VAL A 174 ? 0.58779 0.77501 0.65139 -0.03043 0.01487  -0.12319 156 VAL A C   
1052 O  O   . VAL A 174 ? 0.59072 0.77246 0.65629 -0.03602 0.02283  -0.13083 156 VAL A O   
1053 C  CB  . VAL A 174 ? 0.54828 0.73588 0.59530 -0.03278 0.01936  -0.12178 156 VAL A CB  
1054 C  CG1 . VAL A 174 ? 0.45587 0.63404 0.50936 -0.02887 0.02230  -0.11334 156 VAL A CG1 
1055 C  CG2 . VAL A 174 ? 0.46684 0.65894 0.49720 -0.03536 0.01629  -0.12116 156 VAL A CG2 
1056 N  N   . VAL A 175 ? 0.51084 0.69483 0.57909 -0.02537 0.00970  -0.11531 157 VAL A N   
1057 C  CA  . VAL A 175 ? 0.48087 0.65695 0.55738 -0.02653 0.01282  -0.11535 157 VAL A CA  
1058 C  C   . VAL A 175 ? 0.55328 0.71452 0.63162 -0.02163 0.01411  -0.10447 157 VAL A C   
1059 O  O   . VAL A 175 ? 0.48068 0.64318 0.55752 -0.01675 0.00863  -0.09574 157 VAL A O   
1060 C  CB  . VAL A 175 ? 0.54597 0.73458 0.62832 -0.02507 0.00553  -0.11826 157 VAL A CB  
1061 C  CG1 . VAL A 175 ? 0.45211 0.63102 0.54015 -0.02867 0.01017  -0.11828 157 VAL A CG1 
1062 C  CG2 . VAL A 175 ? 0.55155 0.76028 0.63511 -0.02920 0.00337  -0.13211 157 VAL A CG2 
1063 N  N   . VAL A 176 ? 0.52580 0.67129 0.60517 -0.02298 0.02057  -0.10566 158 VAL A N   
1064 C  CA  . VAL A 176 ? 0.48698 0.61909 0.56928 -0.01715 0.02039  -0.09750 158 VAL A CA  
1065 C  C   . VAL A 176 ? 0.60046 0.71982 0.68250 -0.01913 0.02016  -0.09626 158 VAL A C   
1066 O  O   . VAL A 176 ? 0.56394 0.67430 0.64007 -0.02652 0.02486  -0.10372 158 VAL A O   
1067 C  CB  . VAL A 176 ? 0.60303 0.72450 0.68433 -0.01405 0.02555  -0.10065 158 VAL A CB  
1068 C  CG1 . VAL A 176 ? 0.48639 0.59762 0.57250 -0.00621 0.02330  -0.09417 158 VAL A CG1 
1069 C  CG2 . VAL A 176 ? 0.57070 0.70696 0.65184 -0.01447 0.02761  -0.10380 158 VAL A CG2 
1070 N  N   . LEU A 177 ? 0.46141 0.57875 0.54750 -0.01438 0.01549  -0.08740 159 LEU A N   
1071 C  CA  . LEU A 177 ? 0.44365 0.54881 0.52831 -0.01658 0.01513  -0.08541 159 LEU A CA  
1072 C  C   . LEU A 177 ? 0.52840 0.61678 0.61265 -0.00977 0.01340  -0.07758 159 LEU A C   
1073 O  O   . LEU A 177 ? 0.46285 0.55921 0.55361 -0.00376 0.00930  -0.07059 159 LEU A O   
1074 C  CB  . LEU A 177 ? 0.43902 0.55944 0.52938 -0.01652 0.00971  -0.08362 159 LEU A CB  
1075 C  CG  . LEU A 177 ? 0.36617 0.50463 0.45888 -0.02239 0.00970  -0.09453 159 LEU A CG  
1076 C  CD1 . LEU A 177 ? 0.42727 0.58010 0.52658 -0.01772 0.00177  -0.09319 159 LEU A CD1 
1077 C  CD2 . LEU A 177 ? 0.51960 0.64911 0.60702 -0.03408 0.01791  -0.10421 159 LEU A CD2 
1078 N  N   . GLY A 178 ? 0.51471 0.57834 0.58895 -0.01112 0.01596  -0.07939 160 GLY A N   
1079 C  CA  . GLY A 178 ? 0.49953 0.54571 0.57166 -0.00358 0.01196  -0.07278 160 GLY A CA  
1080 C  C   . GLY A 178 ? 0.57853 0.62159 0.65001 -0.00647 0.00935  -0.06687 160 GLY A C   
1081 O  O   . GLY A 178 ? 0.59850 0.63078 0.66010 -0.01598 0.01286  -0.07033 160 GLY A O   
1082 N  N   . THR A 179 ? 0.49451 0.54757 0.57565 0.00000  0.00415  -0.05916 161 THR A N   
1083 C  CA  . THR A 179 ? 0.56438 0.61623 0.64585 -0.00208 0.00140  -0.05370 161 THR A CA  
1084 C  C   . THR A 179 ? 0.63373 0.66726 0.71117 0.00410  -0.00296 -0.04748 161 THR A C   
1085 O  O   . THR A 179 ? 0.52811 0.57160 0.61514 0.01129  -0.00718 -0.04269 161 THR A O   
1086 C  CB  . THR A 179 ? 0.54595 0.62095 0.63816 -0.00024 -0.00212 -0.04988 161 THR A CB  
1087 O  OG1 . THR A 179 ? 0.50558 0.58628 0.60361 0.00629  -0.00507 -0.04446 161 THR A OG1 
1088 C  CG2 . THR A 179 ? 0.46939 0.56158 0.56376 -0.00356 -0.00049 -0.05645 161 THR A CG2 
1089 N  N   . PRO A 180 ? 0.66394 0.66997 0.72530 0.00068  -0.00234 -0.04793 162 PRO A N   
1090 C  CA  . PRO A 180 ? 0.57093 0.55677 0.62546 0.00809  -0.00863 -0.04229 162 PRO A CA  
1091 C  C   . PRO A 180 ? 0.58871 0.58329 0.64993 0.00760  -0.01188 -0.03527 162 PRO A C   
1092 O  O   . PRO A 180 ? 0.51126 0.52421 0.58059 0.00211  -0.00961 -0.03501 162 PRO A O   
1093 C  CB  . PRO A 180 ? 0.68859 0.63656 0.71639 0.00173  -0.00669 -0.04483 162 PRO A CB  
1094 C  CG  . PRO A 180 ? 0.72386 0.67838 0.74784 -0.01340 0.00240  -0.05127 162 PRO A CG  
1095 C  CD  . PRO A 180 ? 0.62003 0.61058 0.66568 -0.01156 0.00428  -0.05460 162 PRO A CD  
1096 N  N   . ALA A 181 ? 0.60171 0.58254 0.65910 0.01496  -0.01851 -0.03039 163 ALA A N   
1097 C  CA  . ALA A 181 ? 0.70692 0.68664 0.76441 0.01354  -0.02179 -0.02388 163 ALA A CA  
1098 C  C   . ALA A 181 ? 0.61972 0.62919 0.69537 0.01295  -0.02153 -0.02086 163 ALA A C   
1099 O  O   . ALA A 181 ? 0.69950 0.71444 0.77555 0.00658  -0.01954 -0.01993 163 ALA A O   
1100 C  CB  . ALA A 181 ? 0.63435 0.59292 0.67323 0.00173  -0.01757 -0.02462 163 ALA A CB  
1101 N  N   . GLU A 182 ? 0.57719 0.60453 0.66601 0.01947  -0.02374 -0.02040 164 GLU A N   
1102 C  CA  . GLU A 182 ? 0.60185 0.64926 0.70067 0.01779  -0.02419 -0.01650 164 GLU A CA  
1103 C  C   . GLU A 182 ? 0.58444 0.62894 0.68431 0.01946  -0.02909 -0.01053 164 GLU A C   
1104 O  O   . GLU A 182 ? 0.66499 0.71361 0.76499 0.01576  -0.02961 -0.00637 164 GLU A O   
1105 C  CB  . GLU A 182 ? 0.50060 0.56732 0.60896 0.01973  -0.02256 -0.01924 164 GLU A CB  
1106 C  CG  . GLU A 182 ? 0.43214 0.51256 0.54257 0.01547  -0.02246 -0.01521 164 GLU A CG  
1107 C  CD  . GLU A 182 ? 0.61408 0.69866 0.72825 0.01555  -0.02544 -0.01089 164 GLU A CD  
1108 O  OE1 . GLU A 182 ? 0.53212 0.61916 0.65309 0.02035  -0.02735 -0.01360 164 GLU A OE1 
1109 O  OE2 . GLU A 182 ? 0.48161 0.56658 0.59110 0.01129  -0.02658 -0.00577 164 GLU A OE2 
1110 N  N   . GLU A 183 ? 0.67735 0.71457 0.77746 0.02607  -0.03372 -0.01092 165 GLU A N   
1111 C  CA  . GLU A 183 ? 0.79938 0.83700 0.90180 0.02784  -0.03897 -0.00643 165 GLU A CA  
1112 C  C   . GLU A 183 ? 0.81119 0.82886 0.90077 0.02371  -0.04037 -0.00164 165 GLU A C   
1113 O  O   . GLU A 183 ? 0.91465 0.93359 1.00534 0.02278  -0.04356 0.00279  165 GLU A O   
1114 C  CB  . GLU A 183 ? 0.76674 0.80503 0.87423 0.03814  -0.04542 -0.01060 165 GLU A CB  
1115 C  CG  . GLU A 183 ? 0.68078 0.74334 0.80354 0.04197  -0.04337 -0.01824 165 GLU A CG  
1116 C  CD  . GLU A 183 ? 0.73975 0.82850 0.87500 0.03615  -0.04095 -0.01803 165 GLU A CD  
1117 O  OE1 . GLU A 183 ? 0.77689 0.86274 0.90833 0.03032  -0.04171 -0.01124 165 GLU A OE1 
1118 O  OE2 . GLU A 183 ? 0.59026 0.70131 0.73727 0.03617  -0.03766 -0.02545 165 GLU A OE2 
1119 N  N   . ASP A 184 ? 0.78202 0.78194 0.85860 0.01947  -0.03709 -0.00349 166 ASP A N   
1120 C  CA  . ASP A 184 ? 0.81532 0.79613 0.87756 0.01303  -0.03663 -0.00107 166 ASP A CA  
1121 C  C   . ASP A 184 ? 0.72507 0.69999 0.77888 0.00393  -0.02898 -0.00645 166 ASP A C   
1122 O  O   . ASP A 184 ? 0.83094 0.79612 0.87760 0.00378  -0.02669 -0.01073 166 ASP A O   
1123 C  CB  . ASP A 184 ? 0.92290 0.87688 0.96929 0.01776  -0.04348 0.00104  166 ASP A CB  
1124 C  CG  . ASP A 184 ? 1.06949 0.99719 1.09385 0.00820  -0.04147 0.00265  166 ASP A CG  
1125 O  OD1 . ASP A 184 ? 1.14569 1.08117 1.17144 -0.00188 -0.03446 0.00094  166 ASP A OD1 
1126 O  OD2 . ASP A 184 ? 1.21775 1.11607 1.22175 0.01101  -0.04745 0.00455  166 ASP A OD2 
1127 N  N   . GLY A 185 ? 0.70436 0.68621 0.75925 -0.00369 -0.02509 -0.00782 167 GLY A N   
1128 C  CA  . GLY A 185 ? 0.69682 0.67970 0.74686 -0.01358 -0.01736 -0.01604 167 GLY A CA  
1129 C  C   . GLY A 185 ? 0.80098 0.81168 0.86742 -0.01212 -0.01542 -0.02119 167 GLY A C   
1130 O  O   . GLY A 185 ? 0.77027 0.79506 0.84249 -0.01596 -0.01326 -0.02681 167 GLY A O   
1131 N  N   . GLY A 186 ? 0.78136 0.80028 0.85468 -0.00585 -0.01692 -0.02046 168 GLY A N   
1132 C  CA  . GLY A 186 ? 0.67285 0.71410 0.75719 -0.00427 -0.01619 -0.02488 168 GLY A CA  
1133 C  C   . GLY A 186 ? 0.69227 0.73616 0.77389 -0.01062 -0.01006 -0.03456 168 GLY A C   
1134 O  O   . GLY A 186 ? 0.61152 0.66580 0.69514 -0.01698 -0.00661 -0.04309 168 GLY A O   
1135 N  N   . GLY A 187 ? 0.59851 0.63494 0.67636 -0.00905 -0.00859 -0.03501 169 GLY A N   
1136 C  CA  . GLY A 187 ? 0.61656 0.65153 0.68882 -0.01647 -0.00220 -0.04425 169 GLY A CA  
1137 C  C   . GLY A 187 ? 0.62653 0.68835 0.71047 -0.01684 -0.00144 -0.05152 169 GLY A C   
1138 O  O   . GLY A 187 ? 0.60784 0.67571 0.69004 -0.02555 0.00417  -0.06203 169 GLY A O   
1139 N  N   . LYS A 188 ? 0.52395 0.60085 0.61745 -0.00823 -0.00732 -0.04684 170 LYS A N   
1140 C  CA  . LYS A 188 ? 0.51246 0.61103 0.61295 -0.00660 -0.00940 -0.05325 170 LYS A CA  
1141 C  C   . LYS A 188 ? 0.60891 0.72054 0.71446 -0.00959 -0.00988 -0.06201 170 LYS A C   
1142 O  O   . LYS A 188 ? 0.54905 0.67877 0.65993 -0.01178 -0.00913 -0.07355 170 LYS A O   
1143 C  CB  . LYS A 188 ? 0.45506 0.55923 0.55722 0.00186  -0.01630 -0.04542 170 LYS A CB  
1144 C  CG  . LYS A 188 ? 0.46322 0.56139 0.56329 0.00361  -0.01464 -0.03996 170 LYS A CG  
1145 C  CD  . LYS A 188 ? 0.49517 0.59884 0.59290 0.00747  -0.01937 -0.03409 170 LYS A CD  
1146 C  CE  . LYS A 188 ? 0.49518 0.59714 0.59343 0.00752  -0.01643 -0.03058 170 LYS A CE  
1147 N  NZ  . LYS A 188 ? 0.48966 0.58193 0.59184 0.00887  -0.01508 -0.02841 170 LYS A NZ  
1148 N  N   . ILE A 189 ? 0.59423 0.69913 0.69920 -0.00980 -0.01107 -0.05846 171 ILE A N   
1149 C  CA  . ILE A 189 ? 0.58440 0.70426 0.69600 -0.01207 -0.01128 -0.06866 171 ILE A CA  
1150 C  C   . ILE A 189 ? 0.62121 0.74484 0.73083 -0.02634 -0.00114 -0.08208 171 ILE A C   
1151 O  O   . ILE A 189 ? 0.54762 0.69591 0.66716 -0.02931 0.00004  -0.09718 171 ILE A O   
1152 C  CB  . ILE A 189 ? 0.55680 0.66666 0.66670 -0.00973 -0.01421 -0.06149 171 ILE A CB  
1153 C  CG1 . ILE A 189 ? 0.57549 0.68348 0.68574 0.00236  -0.02394 -0.05085 171 ILE A CG1 
1154 C  CG2 . ILE A 189 ? 0.55105 0.67650 0.66796 -0.01384 -0.01235 -0.07450 171 ILE A CG2 
1155 C  CD1 . ILE A 189 ? 0.59111 0.68534 0.69752 0.00383  -0.02638 -0.04163 171 ILE A CD1 
1156 N  N   . ASP A 190 ? 0.56908 0.66767 0.66416 -0.03568 0.00595  -0.07809 172 ASP A N   
1157 C  CA  . ASP A 190 ? 0.60136 0.69662 0.68752 -0.05219 0.01666  -0.09037 172 ASP A CA  
1158 C  C   . ASP A 190 ? 0.69120 0.80588 0.78436 -0.05370 0.01849  -0.10076 172 ASP A C   
1159 O  O   . ASP A 190 ? 0.66984 0.80198 0.76623 -0.06570 0.02544  -0.11702 172 ASP A O   
1160 C  CB  . ASP A 190 ? 0.60374 0.65961 0.66616 -0.05949 0.02132  -0.08245 172 ASP A CB  
1161 C  CG  . ASP A 190 ? 0.75454 0.79014 0.80937 -0.05534 0.01708  -0.07067 172 ASP A CG  
1162 O  OD1 . ASP A 190 ? 0.89926 0.94914 0.96343 -0.05430 0.01528  -0.07228 172 ASP A OD1 
1163 O  OD2 . ASP A 190 ? 0.73532 0.74108 0.77482 -0.05224 0.01477  -0.06087 172 ASP A OD2 
1164 N  N   . LEU A 191 ? 0.64298 0.75704 0.73873 -0.04272 0.01276  -0.09292 173 LEU A N   
1165 C  CA  . LEU A 191 ? 0.58205 0.71401 0.68332 -0.04348 0.01362  -0.10215 173 LEU A CA  
1166 C  C   . LEU A 191 ? 0.52777 0.69472 0.64610 -0.03713 0.00705  -0.11287 173 LEU A C   
1167 O  O   . LEU A 191 ? 0.50063 0.68943 0.62535 -0.04280 0.00971  -0.12791 173 LEU A O   
1168 C  CB  . LEU A 191 ? 0.55956 0.68150 0.65775 -0.03413 0.00968  -0.09159 173 LEU A CB  
1169 C  CG  . LEU A 191 ? 0.62025 0.71194 0.70284 -0.03883 0.01544  -0.08674 173 LEU A CG  
1170 C  CD1 . LEU A 191 ? 0.60454 0.69472 0.68844 -0.02951 0.01220  -0.08069 173 LEU A CD1 
1171 C  CD2 . LEU A 191 ? 0.58151 0.66590 0.65283 -0.05489 0.02545  -0.09904 173 LEU A CD2 
1172 N  N   . ILE A 192 ? 0.45919 0.63100 0.58387 -0.02474 -0.00247 -0.10636 174 ILE A N   
1173 C  CA  . ILE A 192 ? 0.51630 0.71699 0.65434 -0.01548 -0.01146 -0.11719 174 ILE A CA  
1174 C  C   . ILE A 192 ? 0.55403 0.77834 0.70269 -0.02586 -0.00512 -0.13714 174 ILE A C   
1175 O  O   . ILE A 192 ? 0.50646 0.76181 0.66782 -0.02397 -0.00827 -0.15424 174 ILE A O   
1176 C  CB  . ILE A 192 ? 0.52914 0.72263 0.66656 -0.00095 -0.02276 -0.10586 174 ILE A CB  
1177 C  CG1 . ILE A 192 ? 0.54236 0.71809 0.66902 0.00676  -0.02821 -0.08981 174 ILE A CG1 
1178 C  CG2 . ILE A 192 ? 0.45537 0.67447 0.60398 0.01072  -0.03382 -0.11871 174 ILE A CG2 
1179 C  CD1 . ILE A 192 ? 0.44753 0.60969 0.56826 0.01673  -0.03693 -0.07739 174 ILE A CD1 
1180 N  N   . GLU A 193 ? 0.55924 0.77032 0.70216 -0.03785 0.00404  -0.13670 175 GLU A N   
1181 C  CA  . GLU A 193 ? 0.55307 0.78640 0.70404 -0.05150 0.01257  -0.15693 175 GLU A CA  
1182 C  C   . GLU A 193 ? 0.57565 0.82003 0.72468 -0.06894 0.02375  -0.17233 175 GLU A C   
1183 O  O   . GLU A 193 ? 0.62984 0.90502 0.79056 -0.07977 0.02988  -0.19444 175 GLU A O   
1184 C  CB  . GLU A 193 ? 0.49564 0.70595 0.63459 -0.06267 0.02059  -0.15137 175 GLU A CB  
1185 C  CG  . GLU A 193 ? 0.63105 0.84009 0.77586 -0.04869 0.01123  -0.14328 175 GLU A CG  
1186 C  CD  . GLU A 193 ? 0.70040 0.88229 0.83015 -0.05950 0.01846  -0.13530 175 GLU A CD  
1187 O  OE1 . GLU A 193 ? 0.77243 0.93315 0.88425 -0.07739 0.02993  -0.13558 175 GLU A OE1 
1188 O  OE2 . GLU A 193 ? 0.79136 0.97000 0.92418 -0.05016 0.01208  -0.12866 175 GLU A OE2 
1189 N  N   . ALA A 194 ? 0.46871 0.68996 0.60345 -0.07263 0.02702  -0.16286 176 ALA A N   
1190 C  CA  . ALA A 194 ? 0.53278 0.76200 0.66366 -0.08840 0.03676  -0.17684 176 ALA A CA  
1191 C  C   . ALA A 194 ? 0.47696 0.73804 0.62387 -0.07755 0.02823  -0.18594 176 ALA A C   
1192 O  O   . ALA A 194 ? 0.46481 0.73675 0.61061 -0.08978 0.03534  -0.19879 176 ALA A O   
1193 C  CB  . ALA A 194 ? 0.42087 0.60650 0.52597 -0.09719 0.04403  -0.16377 176 ALA A CB  
1194 N  N   . GLY A 195 ? 0.49792 0.77135 0.65635 -0.05571 0.01290  -0.17983 177 GLY A N   
1195 C  CA  . GLY A 195 ? 0.49728 0.79557 0.66569 -0.04392 0.00250  -0.18713 177 GLY A CA  
1196 C  C   . GLY A 195 ? 0.54284 0.81990 0.69830 -0.03999 0.00077  -0.17309 177 GLY A C   
1197 O  O   . GLY A 195 ? 0.54530 0.84039 0.70485 -0.03549 -0.00468 -0.18077 177 GLY A O   
1198 N  N   . ALA A 196 ? 0.42446 0.66538 0.56487 -0.04097 0.00472  -0.15401 178 ALA A N   
1199 C  CA  . ALA A 196 ? 0.62670 0.84969 0.75622 -0.03860 0.00495  -0.14334 178 ALA A CA  
1200 C  C   . ALA A 196 ? 0.55349 0.78410 0.68436 -0.02207 -0.00844 -0.13690 178 ALA A C   
1201 O  O   . ALA A 196 ? 0.47640 0.70402 0.60106 -0.02160 -0.00842 -0.13494 178 ALA A O   
1202 C  CB  . ALA A 196 ? 0.46642 0.65316 0.58241 -0.04039 0.01007  -0.12671 178 ALA A CB  
1203 N  N   . PHE A 197 ? 0.46757 0.70469 0.60299 -0.00928 -0.01977 -0.13381 179 PHE A N   
1204 C  CA  . PHE A 197 ? 0.48822 0.72270 0.61664 0.00538  -0.03308 -0.12566 179 PHE A CA  
1205 C  C   . PHE A 197 ? 0.59567 0.85708 0.73082 0.01572  -0.04592 -0.14024 179 PHE A C   
1206 O  O   . PHE A 197 ? 0.64708 0.90231 0.77082 0.02808  -0.05872 -0.13438 179 PHE A O   
1207 C  CB  . PHE A 197 ? 0.42022 0.63465 0.54211 0.01354  -0.03861 -0.11013 179 PHE A CB  
1208 C  CG  . PHE A 197 ? 0.55682 0.74628 0.67165 0.00694  -0.02941 -0.09560 179 PHE A CG  
1209 C  CD1 . PHE A 197 ? 0.48131 0.66259 0.59984 -0.00159 -0.02025 -0.09528 179 PHE A CD1 
1210 C  CD2 . PHE A 197 ? 0.45156 0.62619 0.55496 0.00925  -0.03039 -0.08371 179 PHE A CD2 
1211 C  CE1 . PHE A 197 ? 0.59249 0.75101 0.70424 -0.00473 -0.01451 -0.08327 179 PHE A CE1 
1212 C  CE2 . PHE A 197 ? 0.44532 0.60244 0.54568 0.00499  -0.02310 -0.07352 179 PHE A CE2 
1213 C  CZ  . PHE A 197 ? 0.51363 0.66261 0.61857 -0.00051 -0.01628 -0.07328 179 PHE A CZ  
1214 N  N   . THR A 198 ? 0.50070 0.79138 0.65231 0.01060  -0.04319 -0.16027 180 THR A N   
1215 C  CA  . THR A 198 ? 0.57378 0.89497 0.73571 0.02341  -0.05753 -0.17727 180 THR A CA  
1216 C  C   . THR A 198 ? 0.47719 0.80539 0.63156 0.02873  -0.06571 -0.18093 180 THR A C   
1217 O  O   . THR A 198 ? 0.58469 0.92848 0.74006 0.04487  -0.08288 -0.19008 180 THR A O   
1218 C  CB  . THR A 198 ? 0.57675 0.93383 0.76080 0.01366  -0.05033 -0.20150 180 THR A CB  
1219 O  OG1 . THR A 198 ? 0.55161 0.91001 0.73533 -0.00774 -0.03310 -0.20715 180 THR A OG1 
1220 C  CG2 . THR A 198 ? 0.57699 0.93042 0.76769 0.01184  -0.04611 -0.20038 180 THR A CG2 
1221 N  N   . ASN A 199 ? 0.58339 0.89938 0.72883 0.01665  -0.05497 -0.17481 181 ASN A N   
1222 C  CA  . ASN A 199 ? 0.52113 0.84426 0.65878 0.01918  -0.06088 -0.17927 181 ASN A CA  
1223 C  C   . ASN A 199 ? 0.50386 0.79440 0.61865 0.02052  -0.06100 -0.15897 181 ASN A C   
1224 O  O   . ASN A 199 ? 0.60971 0.90091 0.71592 0.01716  -0.06025 -0.16062 181 ASN A O   
1225 C  CB  . ASN A 199 ? 0.59866 0.94239 0.74661 0.00214  -0.04768 -0.19549 181 ASN A CB  
1226 C  CG  . ASN A 199 ? 0.67280 1.04328 0.82311 0.00742  -0.05793 -0.21123 181 ASN A CG  
1227 O  OD1 . ASN A 199 ? 0.70796 1.09229 0.85934 0.02512  -0.07645 -0.21734 181 ASN A OD1 
1228 N  ND2 . ASN A 199 ? 0.78042 1.15624 0.92954 -0.00699 -0.04709 -0.21822 181 ASN A ND2 
1229 N  N   . LEU A 200 ? 0.57989 0.84386 0.68493 0.02403  -0.06112 -0.14133 182 LEU A N   
1230 C  CA  . LEU A 200 ? 0.46912 0.70595 0.55302 0.02430  -0.06111 -0.12439 182 LEU A CA  
1231 C  C   . LEU A 200 ? 0.50524 0.73058 0.56927 0.03890  -0.07933 -0.11883 182 LEU A C   
1232 O  O   . LEU A 200 ? 0.60447 0.83089 0.67029 0.05041  -0.09063 -0.12054 182 LEU A O   
1233 C  CB  . LEU A 200 ? 0.45713 0.67234 0.54044 0.01834  -0.05058 -0.10980 182 LEU A CB  
1234 C  CG  . LEU A 200 ? 0.43060 0.64377 0.52356 0.00516  -0.03389 -0.11105 182 LEU A CG  
1235 C  CD1 . LEU A 200 ? 0.47948 0.67107 0.56995 0.00383  -0.02831 -0.09664 182 LEU A CD1 
1236 C  CD2 . LEU A 200 ? 0.45479 0.66865 0.54209 -0.00176 -0.02734 -0.11444 182 LEU A CD2 
1237 N  N   . ASP A 201 ? 0.60097 0.81240 0.64298 0.03812  -0.08231 -0.11258 183 ASP A N   
1238 C  CA  . ASP A 201 ? 0.58139 0.77254 0.59511 0.04992  -0.09960 -0.10576 183 ASP A CA  
1239 C  C   . ASP A 201 ? 0.62917 0.78736 0.62184 0.04587  -0.09629 -0.08704 183 ASP A C   
1240 O  O   . ASP A 201 ? 0.66197 0.79920 0.63491 0.05547  -0.10926 -0.08023 183 ASP A O   
1241 C  CB  . ASP A 201 ? 0.60810 0.80011 0.60363 0.05034  -0.10622 -0.11052 183 ASP A CB  
1242 C  CG  . ASP A 201 ? 0.64595 0.87304 0.66132 0.05515  -0.11183 -0.13104 183 ASP A CG  
1243 O  OD1 . ASP A 201 ? 0.58724 0.82652 0.60706 0.07062  -0.12839 -0.14111 183 ASP A OD1 
1244 O  OD2 . ASP A 201 ? 0.61005 0.85344 0.63681 0.04347  -0.09976 -0.13854 183 ASP A OD2 
1245 N  N   . VAL A 202 ? 0.56247 0.71588 0.55830 0.03190  -0.07950 -0.08006 184 VAL A N   
1246 C  CA  . VAL A 202 ? 0.55769 0.68718 0.53873 0.02528  -0.07353 -0.06539 184 VAL A CA  
1247 C  C   . VAL A 202 ? 0.52307 0.66210 0.52847 0.01582  -0.05633 -0.06453 184 VAL A C   
1248 O  O   . VAL A 202 ? 0.51618 0.67145 0.53803 0.01106  -0.04755 -0.07293 184 VAL A O   
1249 C  CB  . VAL A 202 ? 0.62419 0.73457 0.57300 0.01796  -0.07341 -0.05910 184 VAL A CB  
1250 C  CG1 . VAL A 202 ? 0.69698 0.78429 0.62868 0.00980  -0.06798 -0.04622 184 VAL A CG1 
1251 C  CG2 . VAL A 202 ? 0.71165 0.80993 0.63207 0.02794  -0.09196 -0.06141 184 VAL A CG2 
1252 N  N   . VAL A 203 ? 0.47843 0.60521 0.48397 0.01349  -0.05240 -0.05484 185 VAL A N   
1253 C  CA  . VAL A 203 ? 0.55989 0.69250 0.58563 0.00708  -0.03897 -0.05372 185 VAL A CA  
1254 C  C   . VAL A 203 ? 0.51734 0.63736 0.53209 -0.00023 -0.03295 -0.04448 185 VAL A C   
1255 O  O   . VAL A 203 ? 0.51215 0.61563 0.50792 -0.00012 -0.03903 -0.03649 185 VAL A O   
1256 C  CB  . VAL A 203 ? 0.51416 0.65122 0.55832 0.01180  -0.03989 -0.05473 185 VAL A CB  
1257 C  CG1 . VAL A 203 ? 0.49868 0.62163 0.53180 0.01781  -0.04947 -0.04685 185 VAL A CG1 
1258 C  CG2 . VAL A 203 ? 0.48144 0.61965 0.54146 0.00631  -0.02809 -0.05355 185 VAL A CG2 
1259 N  N   . PHE A 204 ? 0.46832 0.59628 0.49413 -0.00683 -0.02108 -0.04715 186 PHE A N   
1260 C  CA  . PHE A 204 ? 0.54070 0.66532 0.56120 -0.01487 -0.01354 -0.04301 186 PHE A CA  
1261 C  C   . PHE A 204 ? 0.53588 0.66811 0.57962 -0.01388 -0.00632 -0.04415 186 PHE A C   
1262 O  O   . PHE A 204 ? 0.49061 0.62903 0.55061 -0.00981 -0.00371 -0.04976 186 PHE A O   
1263 C  CB  . PHE A 204 ? 0.56172 0.69201 0.57319 -0.02299 -0.00633 -0.04842 186 PHE A CB  
1264 C  CG  . PHE A 204 ? 0.51134 0.63141 0.49528 -0.02486 -0.01359 -0.04751 186 PHE A CG  
1265 C  CD1 . PHE A 204 ? 0.53364 0.66051 0.51913 -0.01992 -0.01816 -0.05425 186 PHE A CD1 
1266 C  CD2 . PHE A 204 ? 0.66208 0.76397 0.61559 -0.03255 -0.01595 -0.04064 186 PHE A CD2 
1267 C  CE1 . PHE A 204 ? 0.72167 0.83880 0.68052 -0.02001 -0.02685 -0.05414 186 PHE A CE1 
1268 C  CE2 . PHE A 204 ? 0.71582 0.80237 0.63803 -0.03357 -0.02439 -0.03936 186 PHE A CE2 
1269 C  CZ  . PHE A 204 ? 0.66082 0.75578 0.58654 -0.02606 -0.03069 -0.04615 186 PHE A CZ  
1270 N  N   . MET A 205 ? 0.47274 0.60277 0.51516 -0.01827 -0.00344 -0.03952 187 MET A N   
1271 C  CA  . MET A 205 ? 0.50244 0.64183 0.56507 -0.01713 0.00268  -0.04231 187 MET A CA  
1272 C  C   . MET A 205 ? 0.53849 0.67963 0.59454 -0.02583 0.00640  -0.03960 187 MET A C   
1273 O  O   . MET A 205 ? 0.46991 0.59909 0.50284 -0.03313 0.00401  -0.03377 187 MET A O   
1274 C  CB  . MET A 205 ? 0.42015 0.55453 0.49612 -0.00876 -0.00176 -0.03963 187 MET A CB  
1275 C  CG  . MET A 205 ? 0.59760 0.72247 0.66842 -0.00851 -0.00724 -0.03088 187 MET A CG  
1276 S  SD  . MET A 205 ? 0.53876 0.65912 0.62552 -0.00080 -0.01002 -0.02932 187 MET A SD  
1277 C  CE  . MET A 205 ? 0.47950 0.60754 0.57803 -0.00155 -0.00597 -0.03025 187 MET A CE  
1278 N  N   . ALA A 206 ? 0.42272 0.57789 0.49735 -0.02527 0.01186  -0.04502 188 ALA A N   
1279 C  CA  . ALA A 206 ? 0.52731 0.69054 0.59971 -0.03520 0.01688  -0.04580 188 ALA A CA  
1280 C  C   . ALA A 206 ? 0.51706 0.69113 0.61264 -0.02828 0.01622  -0.04867 188 ALA A C   
1281 O  O   . ALA A 206 ? 0.48102 0.65762 0.59332 -0.01648 0.01387  -0.05273 188 ALA A O   
1282 C  CB  . ALA A 206 ? 0.41712 0.59632 0.48606 -0.04617 0.02704  -0.05577 188 ALA A CB  
1283 N  N   . HIS A 207 ? 0.47966 0.65812 0.57319 -0.03643 0.01801  -0.04710 189 HIS A N   
1284 C  CA  . HIS A 207 ? 0.59572 0.78284 0.70849 -0.02984 0.01520  -0.04870 189 HIS A CA  
1285 C  C   . HIS A 207 ? 0.54134 0.75352 0.66343 -0.04000 0.02260  -0.05871 189 HIS A C   
1286 O  O   . HIS A 207 ? 0.56942 0.77904 0.67349 -0.05645 0.02765  -0.05623 189 HIS A O   
1287 C  CB  . HIS A 207 ? 0.44229 0.60832 0.54484 -0.02821 0.00762  -0.03598 189 HIS A CB  
1288 C  CG  . HIS A 207 ? 0.66956 0.83775 0.78960 -0.01800 0.00229  -0.03583 189 HIS A CG  
1289 N  ND1 . HIS A 207 ? 0.65075 0.84003 0.78863 -0.01717 0.00396  -0.04455 189 HIS A ND1 
1290 C  CD2 . HIS A 207 ? 0.54871 0.70054 0.66953 -0.00868 -0.00499 -0.02893 189 HIS A CD2 
1291 C  CE1 . HIS A 207 ? 0.54312 0.72589 0.69003 -0.00659 -0.00341 -0.04176 189 HIS A CE1 
1292 N  NE2 . HIS A 207 ? 0.62793 0.78695 0.76356 -0.00247 -0.00809 -0.03195 189 HIS A NE2 
1293 N  N   . PRO A 208 ? 0.50584 0.74178 0.65418 -0.03098 0.02302  -0.07125 190 PRO A N   
1294 C  CA  . PRO A 208 ? 0.52809 0.79555 0.68979 -0.04053 0.03028  -0.08478 190 PRO A CA  
1295 C  C   . PRO A 208 ? 0.55748 0.82368 0.71763 -0.04666 0.02770  -0.07944 190 PRO A C   
1296 O  O   . PRO A 208 ? 0.49892 0.75151 0.66366 -0.03473 0.01809  -0.07158 190 PRO A O   
1297 C  CB  . PRO A 208 ? 0.44990 0.74009 0.64110 -0.02292 0.02721  -0.10009 190 PRO A CB  
1298 C  CG  . PRO A 208 ? 0.49550 0.75789 0.68548 -0.00508 0.01557  -0.08952 190 PRO A CG  
1299 C  CD  . PRO A 208 ? 0.46406 0.69840 0.62924 -0.01158 0.01638  -0.07536 190 PRO A CD  
1300 N  N   A SER A 209 ? 0.51236 0.79148 0.66343 -0.06731 0.03717  -0.08427 191 SER A N   
1301 N  N   B SER A 209 ? 0.54565 0.82470 0.69664 -0.06734 0.03717  -0.08423 191 SER A N   
1302 C  CA  A SER A 209 ? 0.57845 0.85623 0.72474 -0.07710 0.03656  -0.08034 191 SER A CA  
1303 C  CA  B SER A 209 ? 0.57862 0.85645 0.72499 -0.07706 0.03654  -0.08035 191 SER A CA  
1304 C  C   A SER A 209 ? 0.61286 0.92899 0.77125 -0.09420 0.04786  -0.09857 191 SER A C   
1305 C  C   B SER A 209 ? 0.61235 0.92854 0.77088 -0.09411 0.04780  -0.09858 191 SER A C   
1306 O  O   A SER A 209 ? 0.58142 0.93435 0.76942 -0.08659 0.05008  -0.11705 191 SER A O   
1307 O  O   B SER A 209 ? 0.58055 0.93357 0.76882 -0.08642 0.04995  -0.11705 191 SER A O   
1308 C  CB  A SER A 209 ? 0.61078 0.84939 0.71901 -0.08946 0.03584  -0.06262 191 SER A CB  
1309 C  CB  B SER A 209 ? 0.59773 0.83658 0.70607 -0.08958 0.03589  -0.06270 191 SER A CB  
1310 O  OG  A SER A 209 ? 0.61096 0.84496 0.71151 -0.10003 0.03572  -0.05891 191 SER A OG  
1311 O  OG  B SER A 209 ? 0.64421 0.87731 0.72681 -0.10866 0.04583  -0.06432 191 SER A OG  
1312 N  N   . GLN A 210 ? 0.66563 0.97342 0.80036 -0.11767 0.05506  -0.09504 192 GLN A N   
1313 C  CA  . GLN A 210 ? 0.71735 1.06130 0.85930 -0.13964 0.06829  -0.11342 192 GLN A CA  
1314 C  C   . GLN A 210 ? 0.86276 1.19637 0.97014 -0.16785 0.08278  -0.11468 192 GLN A C   
1315 O  O   . GLN A 210 ? 0.93722 1.30700 1.05323 -0.18662 0.09662  -0.13437 192 GLN A O   
1316 C  CB  . GLN A 210 ? 0.63639 0.98272 0.77824 -0.14879 0.06695  -0.11216 192 GLN A CB  
1317 C  CG  . GLN A 210 ? 0.58197 0.95170 0.76170 -0.12552 0.05509  -0.11831 192 GLN A CG  
1318 C  CD  . GLN A 210 ? 0.85403 1.18604 1.02852 -0.10237 0.03969  -0.09838 192 GLN A CD  
1319 O  OE1 . GLN A 210 ? 0.89100 1.18549 1.03784 -0.10780 0.03653  -0.08068 192 GLN A OE1 
1320 N  NE2 . GLN A 210 ? 0.87441 1.21503 1.07357 -0.07698 0.03020  -0.10232 192 GLN A NE2 
1321 N  N   . GLU A 211 ? 0.93745 1.22317 1.00501 -0.17143 0.07962  -0.09564 193 GLU A N   
1322 C  CA  . GLU A 211 ? 1.07079 1.33738 1.09759 -0.19694 0.09100  -0.09470 193 GLU A CA  
1323 C  C   . GLU A 211 ? 1.03092 1.26550 1.03880 -0.18385 0.08345  -0.08173 193 GLU A C   
1324 O  O   . GLU A 211 ? 0.87374 1.10131 0.89941 -0.15778 0.07075  -0.07373 193 GLU A O   
1325 C  CB  . GLU A 211 ? 0.99236 1.22484 0.97603 -0.22148 0.09452  -0.08487 193 GLU A CB  
1326 N  N   . ASN A 212 ? 1.09918 1.31427 1.06903 -0.20346 0.09162  -0.08066 194 ASN A N   
1327 C  CA  . ASN A 212 ? 1.03661 1.22318 0.98532 -0.19374 0.08493  -0.07042 194 ASN A CA  
1328 C  C   . ASN A 212 ? 1.13155 1.26067 1.02993 -0.19760 0.07521  -0.05023 194 ASN A C   
1329 O  O   . ASN A 212 ? 1.22513 1.32886 1.08094 -0.22275 0.08190  -0.04759 194 ASN A O   
1330 C  CB  . ASN A 212 ? 0.97585 1.17678 0.91334 -0.21090 0.09862  -0.08309 194 ASN A CB  
1331 C  CG  . ASN A 212 ? 0.89096 1.14988 0.87833 -0.20572 0.10776  -0.10576 194 ASN A CG  
1332 O  OD1 . ASN A 212 ? 0.70457 0.98090 0.72907 -0.17934 0.09934  -0.10816 194 ASN A OD1 
1333 N  ND2 . ASN A 212 ? 0.95302 1.24105 0.93952 -0.23132 0.12500  -0.12382 194 ASN A ND2 
1334 N  N   . ALA A 213 ? 1.08732 1.19527 0.98893 -0.17305 0.05935  -0.03739 195 ALA A N   
1335 C  CA  . ALA A 213 ? 1.06840 1.12460 0.92709 -0.17073 0.04703  -0.02028 195 ALA A CA  
1336 C  C   . ALA A 213 ? 1.02777 1.07283 0.89086 -0.14696 0.03370  -0.01371 195 ALA A C   
1337 O  O   . ALA A 213 ? 0.99664 1.06598 0.90053 -0.12699 0.02933  -0.01653 195 ALA A O   
1338 C  CB  . ALA A 213 ? 1.02183 1.06644 0.88384 -0.16640 0.04045  -0.01279 195 ALA A CB  
1339 N  N   . ALA A 214 ? 1.13993 1.14712 0.95875 -0.14982 0.02695  -0.00579 196 ALA A N   
1340 C  CA  . ALA A 214 ? 1.03917 1.03726 0.86044 -0.12813 0.01349  -0.00132 196 ALA A CA  
1341 C  C   . ALA A 214 ? 1.07453 1.06227 0.90893 -0.10662 -0.00123 0.00661  196 ALA A C   
1342 O  O   . ALA A 214 ? 0.97492 0.97045 0.82821 -0.08744 -0.01001 0.00616  196 ALA A O   
1343 C  CB  . ALA A 214 ? 0.98884 0.94726 0.75641 -0.13540 0.00753  0.00445  196 ALA A CB  
1344 N  N   . TYR A 215 ? 1.17604 1.14739 1.00034 -0.11084 -0.00326 0.01254  197 TYR A N   
1345 C  CA  . TYR A 215 ? 1.17817 1.14107 1.01508 -0.09217 -0.01580 0.01874  197 TYR A CA  
1346 C  C   . TYR A 215 ? 1.14924 1.11326 0.99138 -0.10157 -0.01068 0.02037  197 TYR A C   
1347 O  O   . TYR A 215 ? 1.03958 0.99128 0.85517 -0.12334 -0.00213 0.02043  197 TYR A O   
1348 C  CB  . TYR A 215 ? 1.02787 0.94773 0.82531 -0.08168 -0.03270 0.02733  197 TYR A CB  
1349 C  CG  . TYR A 215 ? 1.23561 1.13842 1.03369 -0.06827 -0.04439 0.03335  197 TYR A CG  
1350 C  CD1 . TYR A 215 ? 1.33642 1.20699 1.10260 -0.07927 -0.04531 0.04011  197 TYR A CD1 
1351 C  CD2 . TYR A 215 ? 1.19850 1.11767 1.02820 -0.04618 -0.05350 0.03104  197 TYR A CD2 
1352 C  CE1 . TYR A 215 ? 1.28953 1.14466 1.05660 -0.06652 -0.05587 0.04468  197 TYR A CE1 
1353 C  CE2 . TYR A 215 ? 1.08841 0.99476 0.91993 -0.03451 -0.06320 0.03465  197 TYR A CE2 
1354 C  CZ  . TYR A 215 ? 1.17898 1.05337 0.97980 -0.04372 -0.06476 0.04161  197 TYR A CZ  
1355 O  OH  . TYR A 215 ? 1.28410 1.14553 1.08663 -0.03169 -0.07435 0.04439  197 TYR A OH  
1356 N  N   . LEU A 216 ? 1.08839 1.06722 0.96346 -0.08664 -0.01538 0.02089  198 LEU A N   
1357 C  CA  . LEU A 216 ? 1.15014 1.12869 1.03102 -0.09224 -0.01326 0.02299  198 LEU A CA  
1358 C  C   . LEU A 216 ? 1.13199 1.10112 1.02398 -0.07272 -0.02572 0.02837  198 LEU A C   
1359 O  O   . LEU A 216 ? 1.09542 1.08011 1.01282 -0.05602 -0.03053 0.02579  198 LEU A O   
1360 C  CB  . LEU A 216 ? 1.01969 1.04043 0.93927 -0.09826 -0.00139 0.01325  198 LEU A CB  
1361 C  CG  . LEU A 216 ? 0.97585 1.00762 0.88395 -0.12317 0.01282  0.00587  198 LEU A CG  
1362 C  CD1 . LEU A 216 ? 0.89166 0.96600 0.84044 -0.12531 0.02092  -0.00517 198 LEU A CD1 
1363 C  CD2 . LEU A 216 ? 0.99615 0.98846 0.85616 -0.14183 0.01325  0.01315  198 LEU A CD2 
1364 N  N   . PRO A 217 ? 1.25427 1.19802 1.12662 -0.07578 -0.03028 0.03473  199 PRO A N   
1365 C  CA  . PRO A 217 ? 1.17865 1.11066 1.05704 -0.05745 -0.04256 0.03874  199 PRO A CA  
1366 C  C   . PRO A 217 ? 1.07339 1.03654 0.99549 -0.04816 -0.04044 0.03500  199 PRO A C   
1367 O  O   . PRO A 217 ? 1.13036 1.10073 1.06204 -0.05536 -0.03580 0.03520  199 PRO A O   
1368 C  CB  . PRO A 217 ? 1.07527 0.96898 0.91628 -0.06634 -0.04645 0.04587  199 PRO A CB  
1369 C  CG  . PRO A 217 ? 1.22837 1.10553 1.03403 -0.08944 -0.03783 0.04664  199 PRO A CG  
1370 C  CD  . PRO A 217 ? 1.21750 1.13815 1.05558 -0.09749 -0.02443 0.03777  199 PRO A CD  
1371 N  N   . ASP A 218 ? 0.95218 0.93191 0.89806 -0.03311 -0.04404 0.03116  200 ASP A N   
1372 C  CA  . ASP A 218 ? 0.86062 0.85979 0.83902 -0.02347 -0.04417 0.02849  200 ASP A CA  
1373 C  C   . ASP A 218 ? 0.79756 0.78053 0.77045 -0.01110 -0.05468 0.03056  200 ASP A C   
1374 O  O   . ASP A 218 ? 0.74568 0.71787 0.70629 -0.00192 -0.06284 0.02936  200 ASP A O   
1375 C  CB  . ASP A 218 ? 0.77814 0.80239 0.78231 -0.01711 -0.04051 0.02179  200 ASP A CB  
1376 C  CG  . ASP A 218 ? 0.91691 0.96157 0.93306 -0.02643 -0.03050 0.01729  200 ASP A CG  
1377 O  OD1 . ASP A 218 ? 1.03682 1.09343 1.06738 -0.03021 -0.02653 0.01591  200 ASP A OD1 
1378 O  OD2 . ASP A 218 ? 0.88484 0.93499 0.89654 -0.02926 -0.02716 0.01383  200 ASP A OD2 
1379 N  N   . MET A 219 ? 0.75287 0.73591 0.73545 -0.01024 -0.05498 0.03218  201 MET A N   
1380 C  CA  . MET A 219 ? 0.71910 0.68645 0.69498 -0.00018 -0.06406 0.03306  201 MET A CA  
1381 C  C   . MET A 219 ? 0.68876 0.67512 0.69064 0.01091  -0.06515 0.02631  201 MET A C   
1382 O  O   . MET A 219 ? 0.70353 0.71053 0.72650 0.00950  -0.05860 0.02281  201 MET A O   
1383 C  CB  . MET A 219 ? 0.76985 0.72524 0.73925 -0.00691 -0.06327 0.03785  201 MET A CB  
1384 C  CG  . MET A 219 ? 0.77945 0.70838 0.71533 -0.01919 -0.06320 0.04375  201 MET A CG  
1385 S  SD  . MET A 219 ? 0.89428 0.80588 0.81991 -0.02621 -0.06367 0.04828  201 MET A SD  
1386 C  CE  . MET A 219 ? 0.69238 0.63820 0.64782 -0.03823 -0.05186 0.04554  201 MET A CE  
1387 N  N   . ALA A 220 ? 0.58417 0.56214 0.58244 0.02154  -0.07350 0.02326  202 ALA A N   
1388 C  CA  . ALA A 220 ? 0.64690 0.64295 0.66822 0.02838  -0.07277 0.01533  202 ALA A CA  
1389 C  C   . ALA A 220 ? 0.69547 0.69481 0.72823 0.02223  -0.06700 0.01792  202 ALA A C   
1390 O  O   . ALA A 220 ? 0.64341 0.63042 0.66627 0.01576  -0.06633 0.02482  202 ALA A O   
1391 C  CB  . ALA A 220 ? 0.59686 0.58741 0.61320 0.04168  -0.08330 0.00830  202 ALA A CB  
1392 N  N   . GLU A 221 ? 0.66681 0.68163 0.71814 0.02308  -0.06276 0.01179  203 GLU A N   
1393 C  CA  . GLU A 221 ? 0.68708 0.70256 0.74615 0.01738  -0.05802 0.01411  203 GLU A CA  
1394 C  C   . GLU A 221 ? 0.71622 0.73922 0.78517 0.01955  -0.05653 0.00562  203 GLU A C   
1395 O  O   . GLU A 221 ? 0.70180 0.73742 0.77850 0.02215  -0.05518 -0.00316 203 GLU A O   
1396 C  CB  . GLU A 221 ? 0.68457 0.70765 0.75153 0.01135  -0.05183 0.01677  203 GLU A CB  
1397 C  CG  . GLU A 221 ? 0.75727 0.77783 0.82872 0.00728  -0.04953 0.01927  203 GLU A CG  
1398 C  CD  . GLU A 221 ? 0.71853 0.74523 0.79654 0.00490  -0.04647 0.02054  203 GLU A CD  
1399 O  OE1 . GLU A 221 ? 0.89221 0.92530 0.97060 0.00366  -0.04554 0.02152  203 GLU A OE1 
1400 O  OE2 . GLU A 221 ? 0.78033 0.80419 0.86132 0.00450  -0.04542 0.01966  203 GLU A OE2 
1401 N  N   . HIS A 222 ? 0.71756 0.73372 0.78547 0.01683  -0.05602 0.00718  204 HIS A N   
1402 C  CA  . HIS A 222 ? 0.62429 0.64638 0.69905 0.01519  -0.05257 -0.00116 204 HIS A CA  
1403 C  C   . HIS A 222 ? 0.69297 0.70641 0.76535 0.00721  -0.04863 0.00448  204 HIS A C   
1404 O  O   . HIS A 222 ? 0.67362 0.67678 0.73975 0.00597  -0.05143 0.01190  204 HIS A O   
1405 C  CB  . HIS A 222 ? 0.68937 0.71081 0.76261 0.02218  -0.05793 -0.00795 204 HIS A CB  
1406 C  CG  . HIS A 222 ? 0.69988 0.73056 0.78069 0.01859  -0.05295 -0.01880 204 HIS A CG  
1407 N  ND1 . HIS A 222 ? 0.67693 0.72512 0.76778 0.01508  -0.04693 -0.03075 204 HIS A ND1 
1408 C  CD2 . HIS A 222 ? 0.72124 0.74636 0.79963 0.01603  -0.05208 -0.02067 204 HIS A CD2 
1409 C  CE1 . HIS A 222 ? 0.66254 0.71595 0.75626 0.00929  -0.04180 -0.03999 204 HIS A CE1 
1410 N  NE2 . HIS A 222 ? 0.64747 0.68713 0.73405 0.01041  -0.04505 -0.03394 204 HIS A NE2 
1411 N  N   . ASP A 223 ? 0.73921 0.75456 0.81373 0.00137  -0.04270 0.00069  205 ASP A N   
1412 C  CA  . ASP A 223 ? 0.66031 0.66302 0.72788 -0.00521 -0.04058 0.00526  205 ASP A CA  
1413 C  C   . ASP A 223 ? 0.67255 0.67214 0.73610 -0.01088 -0.03707 -0.00132 205 ASP A C   
1414 O  O   . ASP A 223 ? 0.66519 0.67678 0.73430 -0.01163 -0.03359 -0.01260 205 ASP A O   
1415 C  CB  . ASP A 223 ? 0.64084 0.63911 0.70565 -0.00852 -0.03717 0.00551  205 ASP A CB  
1416 C  CG  . ASP A 223 ? 0.68346 0.68606 0.75310 -0.00326 -0.04012 0.01077  205 ASP A CG  
1417 O  OD1 . ASP A 223 ? 0.68060 0.68782 0.75333 0.00021  -0.04397 0.01533  205 ASP A OD1 
1418 O  OD2 . ASP A 223 ? 0.80265 0.80291 0.87121 -0.00363 -0.03806 0.00948  205 ASP A OD2 
1419 N  N   . VAL A 224 ? 0.68522 0.67066 0.73949 -0.01527 -0.03793 0.00425  206 VAL A N   
1420 C  CA  . VAL A 224 ? 0.59558 0.57596 0.64312 -0.02268 -0.03376 -0.00175 206 VAL A CA  
1421 C  C   . VAL A 224 ? 0.67000 0.62942 0.70160 -0.02942 -0.03418 0.00522  206 VAL A C   
1422 O  O   . VAL A 224 ? 0.63584 0.58818 0.66545 -0.02527 -0.04037 0.01462  206 VAL A O   
1423 C  CB  . VAL A 224 ? 0.59793 0.58346 0.64998 -0.01787 -0.03709 -0.00433 206 VAL A CB  
1424 C  CG1 . VAL A 224 ? 0.73244 0.70425 0.77693 -0.01778 -0.04232 0.00632  206 VAL A CG1 
1425 C  CG2 . VAL A 224 ? 0.71334 0.70562 0.76589 -0.02377 -0.03089 -0.01756 206 VAL A CG2 
1426 N  N   . THR A 225 ? 0.70838 0.65820 0.72734 -0.04033 -0.02771 -0.00084 207 THR A N   
1427 C  CA  . THR A 225 ? 0.70489 0.62974 0.70250 -0.04764 -0.02876 0.00477  207 THR A CA  
1428 C  C   . THR A 225 ? 0.73207 0.65551 0.72372 -0.05586 -0.02431 -0.00117 207 THR A C   
1429 O  O   . THR A 225 ? 0.67465 0.60931 0.66919 -0.06334 -0.01555 -0.01381 207 THR A O   
1430 C  CB  . THR A 225 ? 0.72595 0.63097 0.70394 -0.05616 -0.02457 0.00350  207 THR A CB  
1431 O  OG1 . THR A 225 ? 0.81768 0.72116 0.79986 -0.04678 -0.03034 0.00950  207 THR A OG1 
1432 C  CG2 . THR A 225 ? 0.67494 0.54851 0.62399 -0.06472 -0.02621 0.00812  207 THR A CG2 
1433 N  N   . VAL A 226 ? 0.72329 0.63562 0.70782 -0.05481 -0.03008 0.00621  208 VAL A N   
1434 C  CA  . VAL A 226 ? 0.63727 0.54821 0.61674 -0.06139 -0.02681 0.00124  208 VAL A CA  
1435 C  C   . VAL A 226 ? 0.71870 0.60142 0.67000 -0.07251 -0.02651 0.00527  208 VAL A C   
1436 O  O   . VAL A 226 ? 0.73434 0.60093 0.67552 -0.06812 -0.03554 0.01596  208 VAL A O   
1437 C  CB  . VAL A 226 ? 0.65199 0.57095 0.64338 -0.05205 -0.03379 0.00588  208 VAL A CB  
1438 C  CG1 . VAL A 226 ? 0.58712 0.50394 0.57305 -0.05818 -0.03037 -0.00039 208 VAL A CG1 
1439 C  CG2 . VAL A 226 ? 0.56325 0.50229 0.57506 -0.04089 -0.03578 0.00327  208 VAL A CG2 
1440 N  N   . LYS A 227 ? 0.69075 0.56795 0.62846 -0.08698 -0.01655 -0.00454 209 LYS A N   
1441 C  CA  . LYS A 227 ? 0.76694 0.61270 0.67132 -0.10046 -0.01509 -0.00174 209 LYS A CA  
1442 C  C   . LYS A 227 ? 0.68516 0.53400 0.58607 -0.10896 -0.00987 -0.00868 209 LYS A C   
1443 O  O   . LYS A 227 ? 0.69990 0.57183 0.61560 -0.11313 -0.00047 -0.02296 209 LYS A O   
1444 C  CB  . LYS A 227 ? 0.75376 0.58253 0.63535 -0.11544 -0.00567 -0.00780 209 LYS A CB  
1445 C  CG  . LYS A 227 ? 0.87483 0.68923 0.75021 -0.10785 -0.01234 0.00053  209 LYS A CG  
1446 C  CD  . LYS A 227 ? 0.83056 0.62635 0.68165 -0.12400 -0.00199 -0.00646 209 LYS A CD  
1447 C  CE  . LYS A 227 ? 0.88672 0.67047 0.73500 -0.11392 -0.00909 0.00069  209 LYS A CE  
1448 N  NZ  . LYS A 227 ? 0.86784 0.63019 0.69004 -0.13015 0.00095  -0.00595 209 LYS A NZ  
1449 N  N   . TYR A 228 ? 0.70263 0.52975 0.58471 -0.11072 -0.01656 -0.00003 210 TYR A N   
1450 C  CA  . TYR A 228 ? 0.76042 0.58669 0.63577 -0.11931 -0.01224 -0.00560 210 TYR A CA  
1451 C  C   . TYR A 228 ? 0.76098 0.55371 0.59580 -0.13848 -0.00702 -0.00621 210 TYR A C   
1452 O  O   . TYR A 228 ? 0.84044 0.60197 0.64865 -0.13894 -0.01484 0.00443  210 TYR A O   
1453 C  CB  . TYR A 228 ? 0.70108 0.52859 0.58482 -0.10799 -0.02374 0.00399  210 TYR A CB  
1454 C  CG  . TYR A 228 ? 0.66077 0.51664 0.57751 -0.09356 -0.02656 0.00235  210 TYR A CG  
1455 C  CD1 . TYR A 228 ? 0.60082 0.47598 0.53267 -0.09328 -0.01981 -0.01031 210 TYR A CD1 
1456 C  CD2 . TYR A 228 ? 0.66377 0.52545 0.59412 -0.08025 -0.03640 0.01237  210 TYR A CD2 
1457 C  CE1 . TYR A 228 ? 0.67701 0.57041 0.63224 -0.07913 -0.02437 -0.01125 210 TYR A CE1 
1458 C  CE2 . TYR A 228 ? 0.64862 0.52976 0.60195 -0.06932 -0.03882 0.01148  210 TYR A CE2 
1459 C  CZ  . TYR A 228 ? 0.68057 0.57449 0.64407 -0.06832 -0.03354 0.00048  210 TYR A CZ  
1460 O  OH  . TYR A 228 ? 0.59450 0.50043 0.57436 -0.05652 -0.03779 0.00006  210 TYR A OH  
1461 N  N   . TYR A 229 ? 0.86964 0.66750 0.69784 -0.15406 0.00568  -0.01963 211 TYR A N   
1462 C  CA  . TYR A 229 ? 0.86054 0.62603 0.64648 -0.17666 0.01362  -0.02254 211 TYR A CA  
1463 C  C   . TYR A 229 ? 0.87753 0.64378 0.65791 -0.18392 0.01666  -0.02743 211 TYR A C   
1464 O  O   . TYR A 229 ? 0.82103 0.61967 0.62808 -0.18292 0.02442  -0.04138 211 TYR A O   
1465 C  CB  . TYR A 229 ? 0.85769 0.62942 0.63641 -0.19564 0.03101  -0.03862 211 TYR A CB  
1466 C  CG  . TYR A 229 ? 0.98048 0.75669 0.76847 -0.18942 0.03011  -0.03683 211 TYR A CG  
1467 C  CD1 . TYR A 229 ? 1.08355 0.81897 0.83481 -0.19605 0.02675  -0.02719 211 TYR A CD1 
1468 C  CD2 . TYR A 229 ? 0.95295 0.77144 0.78363 -0.17654 0.03187  -0.04530 211 TYR A CD2 
1469 C  CE1 . TYR A 229 ? 1.05001 0.78846 0.80888 -0.19063 0.02627  -0.02624 211 TYR A CE1 
1470 C  CE2 . TYR A 229 ? 0.95985 0.78270 0.79832 -0.17162 0.03133  -0.04409 211 TYR A CE2 
1471 C  CZ  . TYR A 229 ? 0.98905 0.77273 0.79251 -0.17912 0.02917  -0.03472 211 TYR A CZ  
1472 O  OH  . TYR A 229 ? 1.10021 0.88722 0.91072 -0.17433 0.02887  -0.03408 211 TYR A OH  
1473 N  N   . GLY A 230 ? 0.84247 0.57230 0.58711 -0.19041 0.00976  -0.01702 212 GLY A N   
1474 C  CA  . GLY A 230 ? 0.81394 0.54017 0.54800 -0.19950 0.01289  -0.02131 212 GLY A CA  
1475 C  C   . GLY A 230 ? 1.11490 0.80379 0.79853 -0.22569 0.02196  -0.02478 212 GLY A C   
1476 O  O   . GLY A 230 ? 1.02943 0.71277 0.69688 -0.24382 0.03602  -0.03516 212 GLY A O   
1477 N  N   . LYS A 231 ? 1.24159 0.90353 0.89764 -0.22939 0.01430  -0.01671 213 LYS A N   
1478 C  CA  . LYS A 231 ? 1.40403 1.02272 1.00447 -0.25435 0.02059  -0.01773 213 LYS A CA  
1479 C  C   . LYS A 231 ? 1.45569 1.03656 1.02549 -0.24623 0.00070  -0.00003 213 LYS A C   
1480 O  O   . LYS A 231 ? 1.39643 0.99437 0.98982 -0.23084 -0.01008 0.00524  213 LYS A O   
1481 C  CB  . LYS A 231 ? 1.27666 0.91185 0.87666 -0.27451 0.03889  -0.03607 213 LYS A CB  
1482 N  N   . ALA A 232 ? 1.59873 1.12726 1.11449 -0.25643 -0.00480 0.00822  214 ALA A N   
1483 C  CA  . ALA A 232 ? 1.51454 1.00478 0.99856 -0.24570 -0.02698 0.02419  214 ALA A CA  
1484 C  C   . ALA A 232 ? 1.48923 0.95703 0.93911 -0.26157 -0.02561 0.02295  214 ALA A C   
1485 O  O   . ALA A 232 ? 1.51806 0.99055 0.95815 -0.28510 -0.00580 0.00966  214 ALA A O   
1486 C  CB  . ALA A 232 ? 1.42953 0.86760 0.86599 -0.24659 -0.03664 0.03355  214 ALA A CB  
1487 N  N   . TYR A 238 ? 1.46377 0.84364 0.78295 -0.29949 -0.05232 0.03152  220 TYR A N   
1488 C  CA  . TYR A 238 ? 1.68058 1.09224 1.04203 -0.27392 -0.07001 0.03784  220 TYR A CA  
1489 C  C   . TYR A 238 ? 1.70327 1.17125 1.13320 -0.25789 -0.06283 0.03274  220 TYR A C   
1490 O  O   . TYR A 238 ? 1.73350 1.22074 1.18073 -0.26778 -0.04279 0.02174  220 TYR A O   
1491 C  CB  . TYR A 238 ? 1.65535 1.07095 1.01114 -0.28256 -0.06911 0.03398  220 TYR A CB  
1492 N  N   . PRO A 239 ? 1.64109 1.13535 1.10831 -0.23396 -0.07920 0.03960  221 PRO A N   
1493 C  CA  . PRO A 239 ? 1.46879 1.00951 0.99416 -0.21870 -0.07417 0.03647  221 PRO A CA  
1494 C  C   . PRO A 239 ? 1.47667 1.05264 1.03584 -0.22553 -0.05500 0.02336  221 PRO A C   
1495 O  O   . PRO A 239 ? 1.28342 0.89146 0.88284 -0.21585 -0.04840 0.01908  221 PRO A O   
1496 C  CB  . PRO A 239 ? 1.23761 0.79488 0.78706 -0.19671 -0.09533 0.04518  221 PRO A CB  
1497 C  CG  . PRO A 239 ? 1.42462 0.95772 0.94050 -0.20255 -0.10673 0.04840  221 PRO A CG  
1498 C  CD  . PRO A 239 ? 1.59243 1.07538 1.04939 -0.21965 -0.10373 0.04964  221 PRO A CD  
1499 N  N   . TRP A 240 ? 1.57242 1.14266 1.11572 -0.24068 -0.04681 0.01611  222 TRP A N   
1500 C  CA  . TRP A 240 ? 1.39299 0.99441 0.96569 -0.24626 -0.02864 0.00094  222 TRP A CA  
1501 C  C   . TRP A 240 ? 1.48657 1.09727 1.06466 -0.25533 -0.01094 -0.01048 222 TRP A C   
1502 O  O   . TRP A 240 ? 1.51582 1.16183 1.13525 -0.24606 -0.00317 -0.01929 222 TRP A O   
1503 C  CB  . TRP A 240 ? 1.36517 0.95552 0.91453 -0.26323 -0.02151 -0.00685 222 TRP A CB  
1504 C  CG  . TRP A 240 ? 1.41774 0.96856 0.91958 -0.27105 -0.03481 0.00346  222 TRP A CG  
1505 C  CD1 . TRP A 240 ? 1.49448 1.00985 0.94532 -0.29403 -0.02797 0.00021  222 TRP A CD1 
1506 C  CD2 . TRP A 240 ? 1.59603 1.13966 1.09600 -0.25630 -0.05748 0.01699  222 TRP A CD2 
1507 N  NE1 . TRP A 240 ? 1.68249 1.16549 1.09748 -0.29284 -0.04665 0.01223  222 TRP A NE1 
1508 C  CE2 . TRP A 240 ? 1.62398 1.12626 1.07051 -0.26911 -0.06529 0.02179  222 TRP A CE2 
1509 C  CE3 . TRP A 240 ? 1.61637 1.18533 1.15366 -0.23453 -0.07172 0.02415  222 TRP A CE3 
1510 C  CZ2 . TRP A 240 ? 1.68247 1.17064 1.11467 -0.25829 -0.08843 0.03274  222 TRP A CZ2 
1511 C  CZ3 . TRP A 240 ? 1.60743 1.16554 1.13231 -0.22594 -0.09270 0.03378  222 TRP A CZ3 
1512 C  CH2 . TRP A 240 ? 1.55049 1.06977 1.02463 -0.23654 -0.10169 0.03766  222 TRP A CH2 
1513 N  N   . GLU A 241 ? 1.59899 1.17644 1.13284 -0.27408 -0.00490 -0.01098 223 GLU A N   
1514 C  CA  . GLU A 241 ? 1.71845 1.30140 1.25194 -0.28562 0.01157  -0.02163 223 GLU A CA  
1515 C  C   . GLU A 241 ? 1.62895 1.21256 1.17640 -0.26844 0.00084  -0.01054 223 GLU A C   
1516 O  O   . GLU A 241 ? 1.73686 1.28569 1.24816 -0.27505 -0.00266 -0.00341 223 GLU A O   
1517 C  CB  . GLU A 241 ? 1.52546 1.06768 1.00025 -0.31552 0.02289  -0.02638 223 GLU A CB  
1518 N  N   . GLY A 242 ? 1.35446 0.97543 0.95246 -0.24611 -0.00491 -0.00914 224 GLY A N   
1519 C  CA  . GLY A 242 ? 1.21568 0.84219 0.83165 -0.22860 -0.01511 0.00055  224 GLY A CA  
1520 C  C   . GLY A 242 ? 1.07124 0.74242 0.74096 -0.21240 -0.01157 -0.00533 224 GLY A C   
1521 O  O   . GLY A 242 ? 1.06774 0.76235 0.76549 -0.20281 -0.01341 -0.00791 224 GLY A O   
1522 N  N   . LEU A 243 ? 1.03112 0.71089 0.71190 -0.20972 -0.00689 -0.00753 225 LEU A N   
1523 C  CA  . LEU A 243 ? 0.99252 0.70846 0.71933 -0.19163 -0.00777 -0.00956 225 LEU A CA  
1524 C  C   . LEU A 243 ? 0.91841 0.62638 0.64866 -0.17574 -0.02348 0.00591  225 LEU A C   
1525 O  O   . LEU A 243 ? 0.96121 0.64628 0.66812 -0.17985 -0.02514 0.01050  225 LEU A O   
1526 C  CB  . LEU A 243 ? 0.95140 0.68815 0.69195 -0.19924 0.00865  -0.02540 225 LEU A CB  
1527 C  CG  . LEU A 243 ? 1.04771 0.80103 0.79134 -0.21363 0.02501  -0.04536 225 LEU A CG  
1528 C  CD1 . LEU A 243 ? 1.06807 0.85018 0.83197 -0.21861 0.03976  -0.06357 225 LEU A CD1 
1529 C  CD2 . LEU A 243 ? 0.90433 0.67707 0.67332 -0.20086 0.02036  -0.04804 225 LEU A CD2 
1530 N  N   . ASN A 244 ? 0.85165 0.57758 0.60928 -0.15855 -0.03450 0.01267  226 ASN A N   
1531 C  CA  . ASN A 244 ? 0.77221 0.49471 0.53481 -0.14370 -0.05015 0.02546  226 ASN A CA  
1532 C  C   . ASN A 244 ? 0.79532 0.54248 0.58958 -0.13184 -0.04811 0.02433  226 ASN A C   
1533 O  O   . ASN A 244 ? 0.72989 0.50302 0.55493 -0.12218 -0.04803 0.02254  226 ASN A O   
1534 C  CB  . ASN A 244 ? 0.86168 0.59083 0.63364 -0.13546 -0.06207 0.03167  226 ASN A CB  
1535 C  CG  . ASN A 244 ? 0.88481 0.60849 0.65516 -0.12305 -0.07913 0.04210  226 ASN A CG  
1536 O  OD1 . ASN A 244 ? 0.72954 0.45840 0.51010 -0.11393 -0.08209 0.04471  226 ASN A OD1 
1537 N  ND2 . ASN A 244 ? 0.82104 0.53647 0.57978 -0.12209 -0.09082 0.04653  226 ASN A ND2 
1538 N  N   . ALA A 245 ? 0.67461 0.41003 0.45769 -0.13299 -0.04697 0.02563  227 ALA A N   
1539 C  CA  . ALA A 245 ? 0.77869 0.53568 0.58928 -0.12209 -0.04569 0.02490  227 ALA A CA  
1540 C  C   . ALA A 245 ? 0.76756 0.53661 0.59821 -0.10474 -0.05961 0.03427  227 ALA A C   
1541 O  O   . ALA A 245 ? 0.66416 0.45614 0.52217 -0.09521 -0.05846 0.03338  227 ALA A O   
1542 C  CB  . ALA A 245 ? 0.82263 0.56106 0.61288 -0.12921 -0.04079 0.02357  227 ALA A CB  
1543 N  N   . LEU A 246 ? 0.66105 0.41679 0.47861 -0.10093 -0.07270 0.04181  228 LEU A N   
1544 C  CA  . LEU A 246 ? 0.68776 0.46208 0.52805 -0.08639 -0.08438 0.04715  228 LEU A CA  
1545 C  C   . LEU A 246 ? 0.66442 0.46377 0.53015 -0.08502 -0.08110 0.04485  228 LEU A C   
1546 O  O   . LEU A 246 ? 0.68905 0.51001 0.57958 -0.07640 -0.08266 0.04577  228 LEU A O   
1547 C  CB  . LEU A 246 ? 0.74328 0.50059 0.56447 -0.08176 -0.10038 0.05295  228 LEU A CB  
1548 C  CG  . LEU A 246 ? 0.73908 0.52003 0.58419 -0.06825 -0.11283 0.05522  228 LEU A CG  
1549 C  CD1 . LEU A 246 ? 0.58667 0.38714 0.45604 -0.05806 -0.11176 0.05468  228 LEU A CD1 
1550 C  CD2 . LEU A 246 ? 0.68098 0.44461 0.50535 -0.06169 -0.13029 0.05820  228 LEU A CD2 
1551 N  N   . ASP A 247 ? 0.69562 0.48949 0.55246 -0.09422 -0.07639 0.04152  229 ASP A N   
1552 C  CA  . ASP A 247 ? 0.64969 0.46081 0.52563 -0.09328 -0.07248 0.03836  229 ASP A CA  
1553 C  C   . ASP A 247 ? 0.59980 0.42745 0.49674 -0.08779 -0.06462 0.03360  229 ASP A C   
1554 O  O   . ASP A 247 ? 0.61839 0.46003 0.53305 -0.08118 -0.06632 0.03473  229 ASP A O   
1555 C  CB  . ASP A 247 ? 0.66057 0.46129 0.52224 -0.10390 -0.06665 0.03303  229 ASP A CB  
1556 C  CG  . ASP A 247 ? 0.81138 0.59796 0.65397 -0.10883 -0.07557 0.03766  229 ASP A CG  
1557 O  OD1 . ASP A 247 ? 0.66090 0.43815 0.49032 -0.11812 -0.07131 0.03360  229 ASP A OD1 
1558 O  OD2 . ASP A 247 ? 0.70252 0.48860 0.54371 -0.10276 -0.08735 0.04406  229 ASP A OD2 
1559 N  N   . ALA A 248 ? 0.55159 0.37677 0.44446 -0.09146 -0.05605 0.02752  230 ALA A N   
1560 C  CA  . ALA A 248 ? 0.69292 0.53563 0.60585 -0.08545 -0.04965 0.02130  230 ALA A CA  
1561 C  C   . ALA A 248 ? 0.60353 0.45765 0.53261 -0.07463 -0.05578 0.02788  230 ALA A C   
1562 O  O   . ALA A 248 ? 0.65052 0.51806 0.59634 -0.06744 -0.05551 0.02654  230 ALA A O   
1563 C  CB  . ALA A 248 ? 0.63903 0.47943 0.54429 -0.09323 -0.03959 0.01263  230 ALA A CB  
1564 N  N   . ALA A 249 ? 0.53659 0.38370 0.45869 -0.07299 -0.06199 0.03440  231 ALA A N   
1565 C  CA  . ALA A 249 ? 0.64057 0.50083 0.57884 -0.06314 -0.06717 0.03882  231 ALA A CA  
1566 C  C   . ALA A 249 ? 0.62988 0.50197 0.58030 -0.05960 -0.07257 0.04225  231 ALA A C   
1567 O  O   . ALA A 249 ? 0.58837 0.47414 0.55412 -0.05447 -0.07167 0.04240  231 ALA A O   
1568 C  CB  . ALA A 249 ? 0.55640 0.40543 0.48345 -0.06040 -0.07435 0.04333  231 ALA A CB  
1569 N  N   . VAL A 250 ? 0.61707 0.48274 0.55827 -0.06392 -0.07782 0.04448  232 VAL A N   
1570 C  CA  . VAL A 250 ? 0.58507 0.46176 0.53534 -0.06390 -0.08211 0.04650  232 VAL A CA  
1571 C  C   . VAL A 250 ? 0.56423 0.44160 0.51855 -0.06560 -0.07601 0.04395  232 VAL A C   
1572 O  O   . VAL A 250 ? 0.63476 0.52056 0.59753 -0.06442 -0.07653 0.04527  232 VAL A O   
1573 C  CB  . VAL A 250 ? 0.61149 0.48155 0.54993 -0.06885 -0.08935 0.04801  232 VAL A CB  
1574 C  CG1 . VAL A 250 ? 0.59746 0.47873 0.54341 -0.07278 -0.09134 0.04801  232 VAL A CG1 
1575 C  CG2 . VAL A 250 ? 0.61396 0.48293 0.54814 -0.06318 -0.09922 0.05005  232 VAL A CG2 
1576 N  N   . LEU A 251 ? 0.58372 0.45068 0.52990 -0.06845 -0.07046 0.03922  233 LEU A N   
1577 C  CA  . LEU A 251 ? 0.59804 0.46268 0.54618 -0.06679 -0.06692 0.03523  233 LEU A CA  
1578 C  C   . LEU A 251 ? 0.58364 0.45683 0.54363 -0.05820 -0.06504 0.03365  233 LEU A C   
1579 O  O   . LEU A 251 ? 0.50972 0.37999 0.47010 -0.05496 -0.06623 0.03401  233 LEU A O   
1580 C  CB  . LEU A 251 ? 0.54918 0.40498 0.48869 -0.07015 -0.06168 0.02745  233 LEU A CB  
1581 C  CG  . LEU A 251 ? 0.67181 0.51624 0.59646 -0.07945 -0.06311 0.02827  233 LEU A CG  
1582 C  CD1 . LEU A 251 ? 0.62838 0.46670 0.54543 -0.08355 -0.05598 0.01840  233 LEU A CD1 
1583 C  CD2 . LEU A 251 ? 0.53232 0.37235 0.45399 -0.08189 -0.06756 0.03195  233 LEU A CD2 
1584 N  N   . ALA A 252 ? 0.52523 0.40596 0.49159 -0.05507 -0.06245 0.03183  234 ALA A N   
1585 C  CA  . ALA A 252 ? 0.66805 0.55854 0.64592 -0.04710 -0.06138 0.03042  234 ALA A CA  
1586 C  C   . ALA A 252 ? 0.51973 0.41543 0.50234 -0.04564 -0.06567 0.03750  234 ALA A C   
1587 O  O   . ALA A 252 ? 0.55687 0.45249 0.54126 -0.04139 -0.06619 0.03760  234 ALA A O   
1588 C  CB  . ALA A 252 ? 0.49013 0.38719 0.47226 -0.04644 -0.05741 0.02715  234 ALA A CB  
1589 N  N   . TYR A 253 ? 0.54329 0.44323 0.52644 -0.04932 -0.06918 0.04224  235 TYR A N   
1590 C  CA  . TYR A 253 ? 0.54993 0.46000 0.53945 -0.05010 -0.07217 0.04598  235 TYR A CA  
1591 C  C   . TYR A 253 ? 0.63072 0.53313 0.61229 -0.05582 -0.07217 0.04698  235 TYR A C   
1592 O  O   . TYR A 253 ? 0.63032 0.53428 0.61198 -0.05657 -0.07132 0.04825  235 TYR A O   
1593 C  CB  . TYR A 253 ? 0.55426 0.47236 0.54654 -0.05161 -0.07752 0.04760  235 TYR A CB  
1594 C  CG  . TYR A 253 ? 0.61155 0.54847 0.61668 -0.04973 -0.08007 0.04775  235 TYR A CG  
1595 C  CD1 . TYR A 253 ? 0.53399 0.48150 0.54210 -0.05676 -0.08104 0.04701  235 TYR A CD1 
1596 C  CD2 . TYR A 253 ? 0.58014 0.52506 0.59386 -0.04218 -0.08094 0.04705  235 TYR A CD2 
1597 C  CE1 . TYR A 253 ? 0.54334 0.51266 0.56492 -0.05653 -0.08217 0.04427  235 TYR A CE1 
1598 C  CE2 . TYR A 253 ? 0.61853 0.58322 0.64557 -0.03988 -0.08311 0.04513  235 TYR A CE2 
1599 C  CZ  . TYR A 253 ? 0.58812 0.56682 0.62015 -0.04718 -0.08344 0.04309  235 TYR A CZ  
1600 O  OH  . TYR A 253 ? 0.59763 0.60031 0.64450 -0.04639 -0.08429 0.03843  235 TYR A OH  
1601 N  N   . ASN A 254 ? 0.59019 0.48107 0.56129 -0.06114 -0.07285 0.04630  236 ASN A N   
1602 C  CA  . ASN A 254 ? 0.53400 0.41198 0.49304 -0.06745 -0.07274 0.04692  236 ASN A CA  
1603 C  C   . ASN A 254 ? 0.61568 0.47900 0.56733 -0.06083 -0.07145 0.04522  236 ASN A C   
1604 O  O   . ASN A 254 ? 0.58779 0.43962 0.52820 -0.06419 -0.07191 0.04731  236 ASN A O   
1605 C  CB  . ASN A 254 ? 0.56550 0.43288 0.51428 -0.07356 -0.07365 0.04561  236 ASN A CB  
1606 C  CG  . ASN A 254 ? 0.65304 0.53265 0.60531 -0.08041 -0.07742 0.04698  236 ASN A CG  
1607 O  OD1 . ASN A 254 ? 0.56109 0.45575 0.52089 -0.08408 -0.07912 0.04771  236 ASN A OD1 
1608 N  ND2 . ASN A 254 ? 0.57176 0.44577 0.51798 -0.08211 -0.07913 0.04592  236 ASN A ND2 
1609 N  N   . ASN A 255 ? 0.51561 0.37846 0.47158 -0.05172 -0.07026 0.04030  237 ASN A N   
1610 C  CA  . ASN A 255 ? 0.66825 0.52000 0.61916 -0.04203 -0.07137 0.03606  237 ASN A CA  
1611 C  C   . ASN A 255 ? 0.61213 0.46632 0.56419 -0.03838 -0.07263 0.03943  237 ASN A C   
1612 O  O   . ASN A 255 ? 0.59976 0.43522 0.53658 -0.03555 -0.07582 0.04024  237 ASN A O   
1613 C  CB  . ASN A 255 ? 0.60981 0.47009 0.57055 -0.03392 -0.06903 0.02701  237 ASN A CB  
1614 C  CG  . ASN A 255 ? 0.62633 0.48142 0.58233 -0.03815 -0.06689 0.02175  237 ASN A CG  
1615 O  OD1 . ASN A 255 ? 0.59230 0.43336 0.53599 -0.04433 -0.06850 0.02443  237 ASN A OD1 
1616 N  ND2 . ASN A 255 ? 0.55891 0.42527 0.52329 -0.03663 -0.06237 0.01336  237 ASN A ND2 
1617 N  N   . LEU A 256 ? 0.61029 0.48431 0.57720 -0.03834 -0.07059 0.04122  238 LEU A N   
1618 C  CA  . LEU A 256 ? 0.60369 0.48169 0.57207 -0.03571 -0.07099 0.04371  238 LEU A CA  
1619 C  C   . LEU A 256 ? 0.62126 0.49340 0.57862 -0.04689 -0.07077 0.04911  238 LEU A C   
1620 O  O   . LEU A 256 ? 0.66398 0.52490 0.60910 -0.04736 -0.07149 0.05106  238 LEU A O   
1621 C  CB  . LEU A 256 ? 0.61727 0.51732 0.60393 -0.03286 -0.06859 0.04310  238 LEU A CB  
1622 C  CG  . LEU A 256 ? 0.62749 0.53439 0.62337 -0.02523 -0.06681 0.03652  238 LEU A CG  
1623 C  CD1 . LEU A 256 ? 0.66122 0.58257 0.66841 -0.02693 -0.06431 0.03720  238 LEU A CD1 
1624 C  CD2 . LEU A 256 ? 0.54984 0.45637 0.54653 -0.01521 -0.06835 0.03200  238 LEU A CD2 
1625 N  N   . SER A 257 ? 0.57769 0.45717 0.53752 -0.05701 -0.06975 0.05052  239 SER A N   
1626 C  CA  . SER A 257 ? 0.51822 0.39974 0.47129 -0.07027 -0.06800 0.05268  239 SER A CA  
1627 C  C   . SER A 257 ? 0.67715 0.52784 0.60226 -0.07677 -0.06827 0.05453  239 SER A C   
1628 O  O   . SER A 257 ? 0.61106 0.45446 0.52303 -0.08505 -0.06606 0.05630  239 SER A O   
1629 C  CB  . SER A 257 ? 0.61428 0.51155 0.57635 -0.07839 -0.06840 0.05141  239 SER A CB  
1630 O  OG  . SER A 257 ? 0.62860 0.54848 0.61102 -0.07141 -0.07003 0.04994  239 SER A OG  
1631 N  N   . VAL A 258 ? 0.62950 0.45895 0.54206 -0.07378 -0.07091 0.05363  240 VAL A N   
1632 C  CA  . VAL A 258 ? 0.72473 0.51839 0.60607 -0.07859 -0.07263 0.05523  240 VAL A CA  
1633 C  C   . VAL A 258 ? 0.65196 0.42644 0.52035 -0.06635 -0.07678 0.05561  240 VAL A C   
1634 O  O   . VAL A 258 ? 0.63705 0.37967 0.47487 -0.07131 -0.07869 0.05844  240 VAL A O   
1635 C  CB  . VAL A 258 ? 0.72433 0.49993 0.59556 -0.07759 -0.07496 0.05288  240 VAL A CB  
1636 C  CG1 . VAL A 258 ? 0.62423 0.42030 0.50845 -0.08885 -0.07202 0.05231  240 VAL A CG1 
1637 C  CG2 . VAL A 258 ? 0.57101 0.34593 0.45131 -0.05907 -0.07868 0.04756  240 VAL A CG2 
1638 N  N   . PHE A 259 ? 0.64496 0.43665 0.53353 -0.05102 -0.07860 0.05232  241 PHE A N   
1639 C  CA  . PHE A 259 ? 0.69875 0.47751 0.57823 -0.03809 -0.08368 0.05123  241 PHE A CA  
1640 C  C   . PHE A 259 ? 0.74779 0.52505 0.61744 -0.04662 -0.08133 0.05625  241 PHE A C   
1641 O  O   . PHE A 259 ? 0.64955 0.40246 0.49723 -0.04042 -0.08657 0.05736  241 PHE A O   
1642 C  CB  . PHE A 259 ? 0.64240 0.44634 0.54882 -0.02284 -0.08449 0.04472  241 PHE A CB  
1643 C  CG  . PHE A 259 ? 0.75391 0.55364 0.65693 -0.00952 -0.08975 0.04223  241 PHE A CG  
1644 C  CD1 . PHE A 259 ? 0.69540 0.46255 0.57253 0.00110  -0.09895 0.04027  241 PHE A CD1 
1645 C  CD2 . PHE A 259 ? 0.70024 0.52657 0.62395 -0.00676 -0.08667 0.04136  241 PHE A CD2 
1646 C  CE1 . PHE A 259 ? 0.80002 0.56308 0.67275 0.01476  -0.10578 0.03733  241 PHE A CE1 
1647 C  CE2 . PHE A 259 ? 0.75541 0.57923 0.67601 0.00505  -0.09186 0.03851  241 PHE A CE2 
1648 C  CZ  . PHE A 259 ? 0.79910 0.59223 0.69463 0.01615  -0.10184 0.03638  241 PHE A CZ  
1649 N  N   . ARG A 260 ? 0.70778 0.50988 0.59160 -0.06050 -0.07418 0.05821  242 ARG A N   
1650 C  CA  . ARG A 260 ? 0.67807 0.48404 0.55543 -0.06983 -0.07032 0.06067  242 ARG A CA  
1651 C  C   . ARG A 260 ? 0.68806 0.45307 0.52329 -0.08088 -0.07128 0.06443  242 ARG A C   
1652 O  O   . ARG A 260 ? 0.69124 0.44403 0.50968 -0.08261 -0.07144 0.06651  242 ARG A O   
1653 C  CB  . ARG A 260 ? 0.51816 0.35925 0.41819 -0.08284 -0.06308 0.05911  242 ARG A CB  
1654 C  CG  . ARG A 260 ? 0.57229 0.44792 0.50755 -0.07159 -0.06310 0.05616  242 ARG A CG  
1655 C  CD  . ARG A 260 ? 0.54976 0.45707 0.50541 -0.08119 -0.05913 0.05319  242 ARG A CD  
1656 N  NE  . ARG A 260 ? 0.63071 0.56186 0.61282 -0.06964 -0.06099 0.05097  242 ARG A NE  
1657 C  CZ  . ARG A 260 ? 0.64748 0.59244 0.64285 -0.06144 -0.06036 0.04979  242 ARG A CZ  
1658 N  NH1 . ARG A 260 ? 0.53538 0.47660 0.52292 -0.06298 -0.05793 0.05040  242 ARG A NH1 
1659 N  NH2 . ARG A 260 ? 0.47601 0.43574 0.48957 -0.05226 -0.06232 0.04798  242 ARG A NH2 
1660 N  N   . GLN A 261 ? 0.71603 0.45539 0.52984 -0.08882 -0.07221 0.06536  243 GLN A N   
1661 C  CA  . GLN A 261 ? 0.73747 0.42999 0.50415 -0.10101 -0.07322 0.06914  243 GLN A CA  
1662 C  C   . GLN A 261 ? 0.83889 0.49401 0.57846 -0.08364 -0.08381 0.07092  243 GLN A C   
1663 O  O   . GLN A 261 ? 0.82032 0.43795 0.51933 -0.09261 -0.08504 0.07497  243 GLN A O   
1664 C  CB  . GLN A 261 ? 0.73797 0.40751 0.48643 -0.11060 -0.07318 0.06907  243 GLN A CB  
1665 C  CG  . GLN A 261 ? 0.79406 0.41047 0.48830 -0.12765 -0.07290 0.07293  243 GLN A CG  
1666 C  CD  . GLN A 261 ? 0.80641 0.39946 0.48211 -0.13797 -0.07243 0.07228  243 GLN A CD  
1667 O  OE1 . GLN A 261 ? 0.77804 0.38955 0.47891 -0.12837 -0.07442 0.06910  243 GLN A OE1 
1668 N  NE2 . GLN A 261 ? 0.83652 0.38668 0.46517 -0.15923 -0.06924 0.07498  243 GLN A NE2 
1669 N  N   . GLN A 262 ? 0.74547 0.41018 0.50522 -0.05941 -0.09176 0.06682  244 GLN A N   
1670 C  CA  . GLN A 262 ? 0.85844 0.49349 0.59721 -0.03935 -0.10400 0.06557  244 GLN A CA  
1671 C  C   . GLN A 262 ? 0.86994 0.53202 0.63037 -0.02828 -0.10501 0.06375  244 GLN A C   
1672 O  O   . GLN A 262 ? 0.85202 0.49620 0.59987 -0.00974 -0.11616 0.06103  244 GLN A O   
1673 C  CB  . GLN A 262 ? 0.84370 0.47120 0.58854 -0.01898 -0.11309 0.05859  244 GLN A CB  
1674 C  CG  . GLN A 262 ? 0.84024 0.42356 0.54950 -0.02477 -0.11660 0.06008  244 GLN A CG  
1675 C  CD  . GLN A 262 ? 0.82199 0.42538 0.54694 -0.04374 -0.10565 0.06123  244 GLN A CD  
1676 O  OE1 . GLN A 262 ? 0.72678 0.37130 0.49126 -0.04023 -0.10112 0.05697  244 GLN A OE1 
1677 N  NE2 . GLN A 262 ? 0.80670 0.38007 0.49844 -0.06507 -0.10140 0.06646  244 GLN A NE2 
1678 N  N   . MET A 263 ? 0.69109 0.39528 0.48312 -0.03806 -0.09470 0.06414  245 MET A N   
1679 C  CA  . MET A 263 ? 0.78725 0.51535 0.59753 -0.02994 -0.09457 0.06253  245 MET A CA  
1680 C  C   . MET A 263 ? 0.87301 0.57150 0.64678 -0.03760 -0.09616 0.06753  245 MET A C   
1681 O  O   . MET A 263 ? 0.86665 0.54194 0.61106 -0.05788 -0.09095 0.07232  245 MET A O   
1682 C  CB  . MET A 263 ? 0.72444 0.50002 0.57349 -0.03877 -0.08370 0.06143  245 MET A CB  
1683 C  CG  . MET A 263 ? 0.78988 0.59245 0.67136 -0.03242 -0.08209 0.05706  245 MET A CG  
1684 S  SD  . MET A 263 ? 0.81487 0.66583 0.73791 -0.03271 -0.07465 0.05444  245 MET A SD  
1685 C  CE  . MET A 263 ? 0.76920 0.62561 0.68431 -0.04611 -0.06891 0.05755  245 MET A CE  
1686 N  N   . LYS A 264 ? 0.91071 0.60962 0.68438 -0.02292 -0.10293 0.06562  246 LYS A N   
1687 C  CA  . LYS A 264 ? 0.93162 0.60579 0.67181 -0.03112 -0.10366 0.07032  246 LYS A CA  
1688 C  C   . LYS A 264 ? 0.81925 0.52356 0.57455 -0.05361 -0.08844 0.07194  246 LYS A C   
1689 O  O   . LYS A 264 ? 0.86097 0.61172 0.66010 -0.05247 -0.08149 0.06809  246 LYS A O   
1690 C  CB  . LYS A 264 ? 0.94222 0.61863 0.68537 -0.01017 -0.11396 0.06664  246 LYS A CB  
1691 C  CG  . LYS A 264 ? 1.11443 0.74517 0.82215 0.00952  -0.13187 0.06515  246 LYS A CG  
1692 C  CD  . LYS A 264 ? 1.08964 0.70815 0.78005 0.02182  -0.14197 0.06424  246 LYS A CD  
1693 C  CE  . LYS A 264 ? 1.20461 0.78000 0.86218 0.04618  -0.16298 0.06048  246 LYS A CE  
1694 N  NZ  . LYS A 264 ? 1.24800 0.85968 0.94483 0.07317  -0.17206 0.04740  246 LYS A NZ  
1695 N  N   . PRO A 265 ? 0.93203 0.61040 0.65057 -0.07455 -0.08307 0.07631  247 PRO A N   
1696 C  CA  . PRO A 265 ? 0.83779 0.54944 0.57302 -0.09739 -0.06767 0.07453  247 PRO A CA  
1697 C  C   . PRO A 265 ? 0.84808 0.60253 0.61899 -0.09084 -0.06358 0.07052  247 PRO A C   
1698 O  O   . PRO A 265 ? 0.91062 0.70372 0.70918 -0.10300 -0.05246 0.06626  247 PRO A O   
1699 C  CB  . PRO A 265 ? 0.93498 0.60332 0.61551 -0.12096 -0.06352 0.07867  247 PRO A CB  
1700 C  CG  . PRO A 265 ? 1.01456 0.63010 0.65223 -0.10525 -0.07868 0.08361  247 PRO A CG  
1701 C  CD  . PRO A 265 ? 1.05114 0.66816 0.70925 -0.07796 -0.09123 0.08171  247 PRO A CD  
1702 N  N   . THR A 266 ? 0.81644 0.56645 0.58844 -0.07125 -0.07279 0.07038  248 THR A N   
1703 C  CA  . THR A 266 ? 0.83489 0.62333 0.63957 -0.06458 -0.06920 0.06623  248 THR A CA  
1704 C  C   . THR A 266 ? 0.87021 0.69674 0.72211 -0.04896 -0.06988 0.06142  248 THR A C   
1705 O  O   . THR A 266 ? 0.89068 0.74843 0.77023 -0.04388 -0.06646 0.05760  248 THR A O   
1706 C  CB  . THR A 266 ? 0.88485 0.65133 0.66662 -0.05277 -0.07851 0.06731  248 THR A CB  
1707 O  OG1 . THR A 266 ? 0.90841 0.65618 0.68535 -0.03036 -0.09294 0.06632  248 THR A OG1 
1708 C  CG2 . THR A 266 ? 0.77603 0.49975 0.50438 -0.07040 -0.07750 0.07260  248 THR A CG2 
1709 N  N   . TRP A 267 ? 0.72879 0.55105 0.58757 -0.04246 -0.07377 0.06122  249 TRP A N   
1710 C  CA  . TRP A 267 ? 0.73281 0.58545 0.62973 -0.02965 -0.07414 0.05651  249 TRP A CA  
1711 C  C   . TRP A 267 ? 0.65835 0.54126 0.58171 -0.04043 -0.06491 0.05531  249 TRP A C   
1712 O  O   . TRP A 267 ? 0.71824 0.59823 0.63201 -0.05647 -0.05961 0.05699  249 TRP A O   
1713 C  CB  . TRP A 267 ? 0.80772 0.64273 0.69937 -0.01740 -0.08255 0.05511  249 TRP A CB  
1714 C  CG  . TRP A 267 ? 0.84931 0.65946 0.72035 -0.00138 -0.09445 0.05311  249 TRP A CG  
1715 C  CD1 . TRP A 267 ? 0.83738 0.63709 0.69198 0.00257  -0.09886 0.05367  249 TRP A CD1 
1716 C  CD2 . TRP A 267 ? 0.87988 0.67310 0.74427 0.01428  -0.10478 0.04867  249 TRP A CD2 
1717 N  NE1 . TRP A 267 ? 0.88515 0.66210 0.72300 0.02109  -0.11277 0.04987  249 TRP A NE1 
1718 C  CE2 . TRP A 267 ? 0.92926 0.70313 0.77406 0.02911  -0.11659 0.04596  249 TRP A CE2 
1719 C  CE3 . TRP A 267 ? 0.78087 0.57416 0.65390 0.01772  -0.10560 0.04556  249 TRP A CE3 
1720 C  CZ2 . TRP A 267 ? 0.86794 0.62466 0.70369 0.04903  -0.13008 0.03891  249 TRP A CZ2 
1721 C  CZ3 . TRP A 267 ? 0.87668 0.65336 0.74099 0.03577  -0.11723 0.03871  249 TRP A CZ3 
1722 C  CH2 . TRP A 267 ? 0.95909 0.71872 0.80599 0.05212  -0.12977 0.03479  249 TRP A CH2 
1723 N  N   . ARG A 268 ? 0.60838 0.51954 0.56342 -0.03162 -0.06358 0.05134  250 ARG A N   
1724 C  CA  . ARG A 268 ? 0.70430 0.64223 0.68336 -0.03764 -0.05776 0.04944  250 ARG A CA  
1725 C  C   . ARG A 268 ? 0.67318 0.61988 0.67078 -0.02773 -0.06009 0.04722  250 ARG A C   
1726 O  O   . ARG A 268 ? 0.63654 0.58468 0.64042 -0.01676 -0.06260 0.04435  250 ARG A O   
1727 C  CB  . ARG A 268 ? 0.66549 0.62796 0.66016 -0.03979 -0.05250 0.04625  250 ARG A CB  
1728 C  CG  . ARG A 268 ? 0.59636 0.55477 0.57372 -0.05352 -0.04762 0.04666  250 ARG A CG  
1729 C  CD  . ARG A 268 ? 0.56227 0.51791 0.52986 -0.06984 -0.04368 0.04688  250 ARG A CD  
1730 N  NE  . ARG A 268 ? 0.73670 0.68998 0.68624 -0.08700 -0.03671 0.04540  250 ARG A NE  
1731 C  CZ  . ARG A 268 ? 0.75248 0.67121 0.66438 -0.09525 -0.03736 0.05006  250 ARG A CZ  
1732 N  NH1 . ARG A 268 ? 0.78999 0.67436 0.67992 -0.08487 -0.04638 0.05590  250 ARG A NH1 
1733 N  NH2 . ARG A 268 ? 0.81132 0.72877 0.70523 -0.11440 -0.02911 0.04772  250 ARG A NH2 
1734 N  N   . VAL A 269 ? 0.63645 0.58925 0.64130 -0.03298 -0.05898 0.04752  251 VAL A N   
1735 C  CA  . VAL A 269 ? 0.58911 0.54629 0.60615 -0.02673 -0.06063 0.04585  251 VAL A CA  
1736 C  C   . VAL A 269 ? 0.62062 0.59522 0.65167 -0.03115 -0.05929 0.04497  251 VAL A C   
1737 O  O   . VAL A 269 ? 0.63827 0.61556 0.66615 -0.04044 -0.05861 0.04552  251 VAL A O   
1738 C  CB  . VAL A 269 ? 0.65508 0.59252 0.65911 -0.02615 -0.06388 0.04683  251 VAL A CB  
1739 C  CG1 . VAL A 269 ? 0.46075 0.40345 0.47527 -0.02369 -0.06401 0.04474  251 VAL A CG1 
1740 C  CG2 . VAL A 269 ? 0.63959 0.56139 0.63195 -0.01702 -0.06787 0.04501  251 VAL A CG2 
1741 N  N   . HIS A 270 ? 0.57102 0.55637 0.61573 -0.02452 -0.05956 0.04259  252 HIS A N   
1742 C  CA  . HIS A 270 ? 0.57779 0.57648 0.63376 -0.02458 -0.06125 0.04083  252 HIS A CA  
1743 C  C   . HIS A 270 ? 0.63686 0.62807 0.69343 -0.01861 -0.06349 0.04047  252 HIS A C   
1744 O  O   . HIS A 270 ? 0.58414 0.56998 0.63958 -0.01453 -0.06140 0.03924  252 HIS A O   
1745 C  CB  . HIS A 270 ? 0.48094 0.49874 0.54910 -0.02293 -0.05966 0.03708  252 HIS A CB  
1746 C  CG  . HIS A 270 ? 0.59229 0.61743 0.65715 -0.03180 -0.05556 0.03622  252 HIS A CG  
1747 N  ND1 . HIS A 270 ? 0.63832 0.66398 0.70015 -0.03169 -0.05199 0.03587  252 HIS A ND1 
1748 C  CD2 . HIS A 270 ? 0.46968 0.50055 0.53088 -0.04312 -0.05380 0.03501  252 HIS A CD2 
1749 C  CE1 . HIS A 270 ? 0.69096 0.71964 0.74485 -0.04303 -0.04809 0.03510  252 HIS A CE1 
1750 N  NE2 . HIS A 270 ? 0.59707 0.62944 0.65060 -0.05096 -0.04849 0.03417  252 HIS A NE2 
1751 N  N   . GLY A 271 ? 0.59461 0.58492 0.65096 -0.01926 -0.06768 0.04069  253 GLY A N   
1752 C  CA  . GLY A 271 ? 0.66825 0.64518 0.71793 -0.01621 -0.06973 0.04090  253 GLY A CA  
1753 C  C   . GLY A 271 ? 0.59889 0.57455 0.64650 -0.01528 -0.07679 0.04104  253 GLY A C   
1754 O  O   . GLY A 271 ? 0.53631 0.52392 0.58949 -0.01804 -0.07983 0.04018  253 GLY A O   
1755 N  N   . ILE A 272 ? 0.47705 0.43673 0.51415 -0.01217 -0.07961 0.04134  254 ILE A N   
1756 C  CA  . ILE A 272 ? 0.65841 0.61031 0.68798 -0.00876 -0.08882 0.04151  254 ILE A CA  
1757 C  C   . ILE A 272 ? 0.63130 0.55725 0.63953 -0.01391 -0.08829 0.04398  254 ILE A C   
1758 O  O   . ILE A 272 ? 0.63964 0.55600 0.64110 -0.01892 -0.08036 0.04354  254 ILE A O   
1759 C  CB  . ILE A 272 ? 0.64850 0.60050 0.67996 0.00186  -0.09536 0.03870  254 ILE A CB  
1760 C  CG1 . ILE A 272 ? 0.65206 0.58469 0.67118 0.00185  -0.09030 0.03932  254 ILE A CG1 
1761 C  CG2 . ILE A 272 ? 0.64981 0.63112 0.70371 0.00602  -0.09511 0.03402  254 ILE A CG2 
1762 C  CD1 . ILE A 272 ? 0.71836 0.63323 0.72489 0.01097  -0.09858 0.03806  254 ILE A CD1 
1763 N  N   . ILE A 273 ? 0.54973 0.46594 0.54719 -0.01312 -0.09687 0.04514  255 ILE A N   
1764 C  CA  . ILE A 273 ? 0.55546 0.44308 0.52739 -0.01848 -0.09764 0.04727  255 ILE A CA  
1765 C  C   . ILE A 273 ? 0.68059 0.54650 0.63508 -0.01117 -0.10560 0.04754  255 ILE A C   
1766 O  O   . ILE A 273 ? 0.69522 0.55797 0.64558 -0.00218 -0.11864 0.04727  255 ILE A O   
1767 C  CB  . ILE A 273 ? 0.59991 0.48519 0.56551 -0.02266 -0.10288 0.04869  255 ILE A CB  
1768 C  CG1 . ILE A 273 ? 0.60835 0.50891 0.58661 -0.03007 -0.09493 0.04832  255 ILE A CG1 
1769 C  CG2 . ILE A 273 ? 0.56983 0.42281 0.50502 -0.02907 -0.10385 0.05066  255 ILE A CG2 
1770 C  CD1 . ILE A 273 ? 0.53066 0.43169 0.50478 -0.03489 -0.09967 0.04905  255 ILE A CD1 
1771 N  N   . LYS A 274 ? 0.74801 0.59831 0.69118 -0.01456 -0.09844 0.04698  256 LYS A N   
1772 C  CA  . LYS A 274 ? 0.68259 0.50569 0.60391 -0.00869 -0.10527 0.04735  256 LYS A CA  
1773 C  C   . LYS A 274 ? 0.80452 0.59106 0.69037 -0.01178 -0.11352 0.05051  256 LYS A C   
1774 O  O   . LYS A 274 ? 0.82178 0.59058 0.69284 -0.00023 -0.12833 0.05136  256 LYS A O   
1775 C  CB  . LYS A 274 ? 0.82813 0.64240 0.74333 -0.01549 -0.09361 0.04516  256 LYS A CB  
1776 C  CG  . LYS A 274 ? 0.83702 0.62048 0.72789 -0.01032 -0.09938 0.04525  256 LYS A CG  
1777 C  CD  . LYS A 274 ? 0.98406 0.78195 0.89212 0.00814  -0.11136 0.04376  256 LYS A CD  
1778 C  CE  . LYS A 274 ? 1.02771 0.79313 0.91132 0.01464  -0.11684 0.04291  256 LYS A CE  
1779 N  NZ  . LYS A 274 ? 1.10823 0.84905 0.96857 -0.00172 -0.10331 0.04274  256 LYS A NZ  
1780 N  N   . ASN A 275 ? 0.80294 0.57722 0.67350 -0.02662 -0.10491 0.05130  257 ASN A N   
1781 C  CA  . ASN A 275 ? 0.80576 0.54226 0.63786 -0.03332 -0.11047 0.05422  257 ASN A CA  
1782 C  C   . ASN A 275 ? 0.78333 0.53271 0.62230 -0.03998 -0.10891 0.05469  257 ASN A C   
1783 O  O   . ASN A 275 ? 0.75589 0.51860 0.60489 -0.05120 -0.09537 0.05173  257 ASN A O   
1784 C  CB  . ASN A 275 ? 0.69110 0.39507 0.49077 -0.04932 -0.09897 0.05279  257 ASN A CB  
1785 C  CG  . ASN A 275 ? 0.95687 0.60997 0.70616 -0.05488 -0.10727 0.05661  257 ASN A CG  
1786 O  OD1 . ASN A 275 ? 0.94237 0.58717 0.67982 -0.05603 -0.11441 0.05925  257 ASN A OD1 
1787 N  ND2 . ASN A 275 ? 0.96793 0.58340 0.68364 -0.05928 -0.10650 0.05690  257 ASN A ND2 
1788 N  N   . GLY A 276 ? 0.80368 0.54960 0.63734 -0.03224 -0.12346 0.05711  258 GLY A N   
1789 C  CA  . GLY A 276 ? 0.67509 0.43135 0.51318 -0.03866 -0.12306 0.05743  258 GLY A CA  
1790 C  C   . GLY A 276 ? 0.82745 0.54837 0.62745 -0.04260 -0.13281 0.06045  258 GLY A C   
1791 O  O   . GLY A 276 ? 0.75921 0.48867 0.56259 -0.04188 -0.13987 0.06082  258 GLY A O   
1792 N  N   . GLY A 277 ? 0.84258 0.52147 0.60312 -0.04817 -0.13312 0.06241  259 GLY A N   
1793 C  CA  . GLY A 277 ? 0.90293 0.53968 0.61852 -0.05292 -0.14293 0.06591  259 GLY A CA  
1794 C  C   . GLY A 277 ? 0.96275 0.56265 0.64722 -0.03899 -0.16113 0.06894  259 GLY A C   
1795 O  O   . GLY A 277 ? 1.02866 0.64160 0.73196 -0.02302 -0.16804 0.06745  259 GLY A O   
1796 N  N   . VAL A 278 ? 1.07260 0.62297 0.70562 -0.04520 -0.16940 0.07276  260 VAL A N   
1797 C  CA  . VAL A 278 ? 1.25315 0.75590 0.84483 -0.03215 -0.18857 0.07600  260 VAL A CA  
1798 C  C   . VAL A 278 ? 1.25746 0.73984 0.82446 -0.02160 -0.21123 0.07833  260 VAL A C   
1799 O  O   . VAL A 278 ? 1.38353 0.86382 0.95176 0.00254  -0.23406 0.07700  260 VAL A O   
1800 C  CB  . VAL A 278 ? 1.38410 0.83102 0.92254 -0.05075 -0.17802 0.07852  260 VAL A CB  
1801 C  CG1 . VAL A 278 ? 1.19028 0.65216 0.75012 -0.05125 -0.16503 0.07533  260 VAL A CG1 
1802 C  CG2 . VAL A 278 ? 1.40261 0.84043 0.92194 -0.07921 -0.15894 0.07774  260 VAL A CG2 
1803 N  N   . LYS A 279 ? 1.19526 0.66484 0.74100 -0.03871 -0.20576 0.08030  261 LYS A N   
1804 C  CA  . LYS A 279 ? 1.15518 0.60367 0.67397 -0.03119 -0.22655 0.08242  261 LYS A CA  
1805 C  C   . LYS A 279 ? 1.11074 0.59503 0.65517 -0.04327 -0.21701 0.08041  261 LYS A C   
1806 O  O   . LYS A 279 ? 1.12515 0.61641 0.67338 -0.06533 -0.19408 0.07952  261 LYS A O   
1807 C  CB  . LYS A 279 ? 1.28077 0.65174 0.72196 -0.04175 -0.23345 0.08845  261 LYS A CB  
1808 N  N   . PRO A 280 ? 1.14734 0.65532 0.70951 -0.02916 -0.23436 0.07816  262 PRO A N   
1809 C  CA  . PRO A 280 ? 1.13890 0.68205 0.72707 -0.04051 -0.22526 0.07572  262 PRO A CA  
1810 C  C   . PRO A 280 ? 1.23010 0.73560 0.77357 -0.06200 -0.21850 0.07903  262 PRO A C   
1811 O  O   . PRO A 280 ? 1.31456 0.84519 0.87760 -0.07634 -0.20372 0.07658  262 PRO A O   
1812 C  CB  . PRO A 280 ? 1.15654 0.72991 0.76872 -0.01977 -0.24805 0.07109  262 PRO A CB  
1813 C  CG  . PRO A 280 ? 1.18428 0.75166 0.79711 0.00437  -0.26616 0.06909  262 PRO A CG  
1814 C  CD  . PRO A 280 ? 1.25512 0.76267 0.81740 -0.00158 -0.26308 0.07567  262 PRO A CD  
1815 N  N   . ASN A 281 ? 1.35313 0.79716 0.83480 -0.06513 -0.22888 0.08399  263 ASN A N   
1816 C  CA  . ASN A 281 ? 1.36781 0.77443 0.80304 -0.08728 -0.22249 0.08643  263 ASN A CA  
1817 C  C   . ASN A 281 ? 1.33289 0.72684 0.75460 -0.11466 -0.19372 0.08505  263 ASN A C   
1818 O  O   . ASN A 281 ? 1.38521 0.75505 0.77344 -0.13636 -0.18380 0.08462  263 ASN A O   
1819 C  CB  . ASN A 281 ? 1.38813 0.72880 0.75555 -0.08096 -0.24641 0.09215  263 ASN A CB  
1820 C  CG  . ASN A 281 ? 1.56617 0.87484 0.91302 -0.06415 -0.25955 0.09458  263 ASN A CG  
1821 O  OD1 . ASN A 281 ? 1.66960 1.01015 1.05451 -0.03888 -0.27340 0.09178  263 ASN A OD1 
1822 N  ND2 . ASN A 281 ? 1.77795 1.03518 1.07636 -0.07900 -0.25058 0.09332  263 ASN A ND2 
1823 N  N   . ILE A 282 ? 1.33936 0.75105 0.78662 -0.11459 -0.18009 0.08276  264 ILE A N   
1824 C  CA  . ILE A 282 ? 1.32083 0.73402 0.76693 -0.13884 -0.15229 0.07794  264 ILE A CA  
1825 C  C   . ILE A 282 ? 1.21515 0.69383 0.72929 -0.13515 -0.13793 0.07171  264 ILE A C   
1826 O  O   . ILE A 282 ? 1.22540 0.73539 0.77901 -0.11624 -0.14434 0.07210  264 ILE A O   
1827 C  CB  . ILE A 282 ? 1.16911 0.54435 0.58277 -0.14407 -0.14781 0.07929  264 ILE A CB  
1828 N  N   . ILE A 283 ? 1.13877 0.63634 0.66448 -0.15269 -0.11937 0.06532  265 ILE A N   
1829 C  CA  . ILE A 283 ? 1.10138 0.65365 0.68459 -0.14963 -0.10599 0.05889  265 ILE A CA  
1830 C  C   . ILE A 283 ? 1.09216 0.65371 0.69049 -0.14885 -0.09531 0.05587  265 ILE A C   
1831 O  O   . ILE A 283 ? 1.09538 0.63131 0.66364 -0.16598 -0.08285 0.05213  265 ILE A O   
1832 C  CB  . ILE A 283 ? 1.07006 0.63530 0.65746 -0.16766 -0.08893 0.05073  265 ILE A CB  
1833 C  CG1 . ILE A 283 ? 1.25339 0.81932 0.83703 -0.16536 -0.10008 0.05350  265 ILE A CG1 
1834 C  CG2 . ILE A 283 ? 1.01949 0.63194 0.65788 -0.16466 -0.07449 0.04275  265 ILE A CG2 
1835 N  N   . PRO A 284 ? 1.04314 0.63974 0.68497 -0.13106 -0.09939 0.05668  266 PRO A N   
1836 C  CA  . PRO A 284 ? 0.94828 0.55198 0.60263 -0.12907 -0.09122 0.05428  266 PRO A CA  
1837 C  C   . PRO A 284 ? 0.93888 0.55939 0.60431 -0.14597 -0.06841 0.04375  266 PRO A C   
1838 O  O   . PRO A 284 ? 0.89594 0.55000 0.59297 -0.14633 -0.06053 0.03789  266 PRO A O   
1839 C  CB  . PRO A 284 ? 0.90184 0.54501 0.60341 -0.10776 -0.09975 0.05631  266 PRO A CB  
1840 C  CG  . PRO A 284 ? 0.98458 0.63115 0.68806 -0.09763 -0.11650 0.06072  266 PRO A CG  
1841 C  CD  . PRO A 284 ? 1.00597 0.63596 0.68460 -0.11356 -0.11160 0.05924  266 PRO A CD  
1842 N  N   . SER A 285 ? 0.86799 0.46409 0.50556 -0.16007 -0.05826 0.04004  267 SER A N   
1843 C  CA  . SER A 285 ? 1.03891 0.65422 0.68763 -0.17649 -0.03653 0.02689  267 SER A CA  
1844 C  C   . SER A 285 ? 0.95878 0.59877 0.63751 -0.16840 -0.03155 0.02342  267 SER A C   
1845 O  O   . SER A 285 ? 0.99317 0.64974 0.68083 -0.18104 -0.01466 0.01110  267 SER A O   
1846 C  CB  . SER A 285 ? 1.05044 0.62511 0.64666 -0.20323 -0.02504 0.02180  267 SER A CB  
1847 O  OG  . SER A 285 ? 1.07038 0.60344 0.62920 -0.20501 -0.03084 0.02829  267 SER A OG  
1848 N  N   . TYR A 286 ? 0.96938 0.61453 0.66465 -0.14785 -0.04581 0.03243  268 TYR A N   
1849 C  CA  . TYR A 286 ? 0.91196 0.57957 0.63480 -0.13933 -0.04224 0.02989  268 TYR A CA  
1850 C  C   . TYR A 286 ? 0.83881 0.52963 0.59482 -0.11555 -0.05687 0.03756  268 TYR A C   
1851 O  O   . TYR A 286 ? 0.92906 0.60376 0.67328 -0.10510 -0.07281 0.04594  268 TYR A O   
1852 C  CB  . TYR A 286 ? 0.97066 0.60154 0.65782 -0.14714 -0.04083 0.03100  268 TYR A CB  
1853 C  CG  . TYR A 286 ? 0.95304 0.60377 0.66619 -0.13674 -0.03954 0.02960  268 TYR A CG  
1854 C  CD1 . TYR A 286 ? 0.98042 0.65805 0.71380 -0.14634 -0.02289 0.01779  268 TYR A CD1 
1855 C  CD2 . TYR A 286 ? 0.95974 0.60432 0.67789 -0.11696 -0.05533 0.03846  268 TYR A CD2 
1856 C  CE1 . TYR A 286 ? 0.95919 0.65452 0.71501 -0.13718 -0.02208 0.01640  268 TYR A CE1 
1857 C  CE2 . TYR A 286 ? 0.98001 0.64245 0.72094 -0.10818 -0.05361 0.03671  268 TYR A CE2 
1858 C  CZ  . TYR A 286 ? 0.95594 0.64231 0.71447 -0.11874 -0.03699 0.02645  268 TYR A CZ  
1859 O  OH  . TYR A 286 ? 0.98272 0.68634 0.76256 -0.11035 -0.03567 0.02464  268 TYR A OH  
1860 N  N   . SER A 287 ? 0.77860 0.50775 0.57494 -0.10763 -0.05152 0.03329  269 SER A N   
1861 C  CA  . SER A 287 ? 0.75604 0.50831 0.58285 -0.08849 -0.06209 0.03874  269 SER A CA  
1862 C  C   . SER A 287 ? 0.75593 0.53168 0.60776 -0.08465 -0.05428 0.03378  269 SER A C   
1863 O  O   . SER A 287 ? 0.76977 0.55293 0.62353 -0.09523 -0.04104 0.02475  269 SER A O   
1864 C  CB  . SER A 287 ? 0.66668 0.44246 0.51659 -0.08266 -0.06603 0.04007  269 SER A CB  
1865 O  OG  . SER A 287 ? 0.73150 0.53329 0.60521 -0.08515 -0.05513 0.03267  269 SER A OG  
1866 N  N   . GLU A 288 ? 0.71674 0.50646 0.58838 -0.06970 -0.06260 0.03822  270 GLU A N   
1867 C  CA  . GLU A 288 ? 0.70004 0.50809 0.59142 -0.06548 -0.05684 0.03447  270 GLU A CA  
1868 C  C   . GLU A 288 ? 0.68190 0.51657 0.60325 -0.05069 -0.06403 0.03800  270 GLU A C   
1869 O  O   . GLU A 288 ? 0.66208 0.49372 0.58312 -0.04152 -0.07553 0.04321  270 GLU A O   
1870 C  CB  . GLU A 288 ? 0.73799 0.51993 0.60606 -0.06769 -0.05716 0.03493  270 GLU A CB  
1871 C  CG  . GLU A 288 ? 0.77264 0.57248 0.66079 -0.06112 -0.05382 0.03213  270 GLU A CG  
1872 C  CD  . GLU A 288 ? 0.86222 0.63148 0.72397 -0.06262 -0.05548 0.03300  270 GLU A CD  
1873 O  OE1 . GLU A 288 ? 0.96176 0.69555 0.78655 -0.07544 -0.05290 0.03266  270 GLU A OE1 
1874 O  OE2 . GLU A 288 ? 0.93140 0.70930 0.80638 -0.05171 -0.05929 0.03378  270 GLU A OE2 
1875 N  N   . LEU A 289 ? 0.59732 0.45792 0.54301 -0.04871 -0.05753 0.03388  271 LEU A N   
1876 C  CA  . LEU A 289 ? 0.67714 0.56062 0.64710 -0.03805 -0.06199 0.03646  271 LEU A CA  
1877 C  C   . LEU A 289 ? 0.65753 0.55281 0.63949 -0.03443 -0.05728 0.03304  271 LEU A C   
1878 O  O   . LEU A 289 ? 0.75021 0.64398 0.72833 -0.04061 -0.04897 0.02679  271 LEU A O   
1879 C  CB  . LEU A 289 ? 0.56992 0.46814 0.55273 -0.03837 -0.06053 0.03574  271 LEU A CB  
1880 C  CG  . LEU A 289 ? 0.70485 0.59327 0.67697 -0.04312 -0.06402 0.03812  271 LEU A CG  
1881 C  CD1 . LEU A 289 ? 0.67345 0.55166 0.63292 -0.05282 -0.05635 0.03227  271 LEU A CD1 
1882 C  CD2 . LEU A 289 ? 0.52686 0.42869 0.51186 -0.04046 -0.06672 0.04015  271 LEU A CD2 
1883 N  N   . ILE A 290 ? 0.64524 0.55419 0.64192 -0.02546 -0.06211 0.03576  272 ILE A N   
1884 C  CA  . ILE A 290 ? 0.69175 0.61333 0.70054 -0.02148 -0.05837 0.03290  272 ILE A CA  
1885 C  C   . ILE A 290 ? 0.65976 0.60242 0.68695 -0.01654 -0.05974 0.03431  272 ILE A C   
1886 O  O   . ILE A 290 ? 0.69731 0.64645 0.72991 -0.01327 -0.06548 0.03752  272 ILE A O   
1887 C  CB  . ILE A 290 ? 0.71079 0.62287 0.71355 -0.01645 -0.06232 0.03371  272 ILE A CB  
1888 C  CG1 . ILE A 290 ? 0.67685 0.55829 0.65214 -0.02253 -0.06264 0.03375  272 ILE A CG1 
1889 C  CG2 . ILE A 290 ? 0.71928 0.64279 0.73235 -0.01441 -0.05691 0.02981  272 ILE A CG2 
1890 C  CD1 . ILE A 290 ? 0.73440 0.59862 0.69768 -0.01648 -0.06795 0.03433  272 ILE A CD1 
1891 N  N   . TYR A 291 ? 0.66742 0.62018 0.70231 -0.01653 -0.05480 0.03079  273 TYR A N   
1892 C  CA  . TYR A 291 ? 0.56613 0.53096 0.61040 -0.01346 -0.05607 0.03239  273 TYR A CA  
1893 C  C   . TYR A 291 ? 0.55626 0.53147 0.60823 -0.00960 -0.05322 0.02900  273 TYR A C   
1894 O  O   . TYR A 291 ? 0.67602 0.65184 0.72814 -0.01001 -0.04920 0.02356  273 TYR A O   
1895 C  CB  . TYR A 291 ? 0.51547 0.47623 0.55580 -0.01538 -0.05598 0.03157  273 TYR A CB  
1896 C  CG  . TYR A 291 ? 0.63270 0.58748 0.66772 -0.01897 -0.05977 0.03634  273 TYR A CG  
1897 C  CD1 . TYR A 291 ? 0.69132 0.63594 0.71798 -0.02310 -0.06081 0.03694  273 TYR A CD1 
1898 C  CD2 . TYR A 291 ? 0.57365 0.53138 0.60919 -0.01992 -0.06194 0.03968  273 TYR A CD2 
1899 C  CE1 . TYR A 291 ? 0.66341 0.60406 0.68555 -0.02658 -0.06471 0.04048  273 TYR A CE1 
1900 C  CE2 . TYR A 291 ? 0.63366 0.58737 0.66422 -0.02513 -0.06464 0.04269  273 TYR A CE2 
1901 C  CZ  . TYR A 291 ? 0.69307 0.63976 0.71852 -0.02770 -0.06639 0.04293  273 TYR A CZ  
1902 O  OH  . TYR A 291 ? 0.58774 0.53195 0.60864 -0.03301 -0.06953 0.04515  273 TYR A OH  
1903 N  N   . TYR A 292 ? 0.54816 0.53123 0.60471 -0.00748 -0.05486 0.03152  274 TYR A N   
1904 C  CA  . TYR A 292 ? 0.63496 0.62557 0.69535 -0.00389 -0.05337 0.02885  274 TYR A CA  
1905 C  C   . TYR A 292 ? 0.62259 0.60967 0.67668 -0.00390 -0.05604 0.03173  274 TYR A C   
1906 O  O   . TYR A 292 ? 0.64649 0.63051 0.69639 -0.00858 -0.05739 0.03616  274 TYR A O   
1907 C  CB  . TYR A 292 ? 0.68481 0.68469 0.75217 -0.00227 -0.05196 0.02847  274 TYR A CB  
1908 C  CG  . TYR A 292 ? 0.73347 0.74127 0.80425 -0.00379 -0.05327 0.03150  274 TYR A CG  
1909 C  CD1 . TYR A 292 ? 0.86691 0.87852 0.94229 -0.00367 -0.05554 0.03183  274 TYR A CD1 
1910 C  CD2 . TYR A 292 ? 0.84346 0.85540 0.91173 -0.00561 -0.05241 0.03243  274 TYR A CD2 
1911 C  CE1 . TYR A 292 ? 0.90153 0.92704 0.98368 -0.00565 -0.05604 0.03103  274 TYR A CE1 
1912 C  CE2 . TYR A 292 ? 0.86954 0.89131 0.94043 -0.01034 -0.05143 0.03294  274 TYR A CE2 
1913 C  CZ  . TYR A 292 ? 0.95093 0.98268 1.03127 -0.01045 -0.05276 0.03119  274 TYR A CZ  
1914 O  OH  . TYR A 292 ? 0.91518 0.96305 1.00164 -0.01565 -0.05118 0.02830  274 TYR A OH  
1915 N  N   . PHE A 293 ? 0.56812 0.55397 0.61924 0.00108  -0.05736 0.02831  275 PHE A N   
1916 C  CA  . PHE A 293 ? 0.65514 0.62947 0.69308 0.00257  -0.06166 0.03083  275 PHE A CA  
1917 C  C   . PHE A 293 ? 0.64286 0.62037 0.67790 0.00547  -0.06244 0.03032  275 PHE A C   
1918 O  O   . PHE A 293 ? 0.67928 0.66893 0.72427 0.00954  -0.06076 0.02525  275 PHE A O   
1919 C  CB  . PHE A 293 ? 0.62592 0.59109 0.65832 0.00916  -0.06596 0.02595  275 PHE A CB  
1920 C  CG  . PHE A 293 ? 0.59186 0.55777 0.62942 0.00654  -0.06364 0.02332  275 PHE A CG  
1921 C  CD1 . PHE A 293 ? 0.70156 0.65975 0.73424 -0.00074 -0.06305 0.02930  275 PHE A CD1 
1922 C  CD2 . PHE A 293 ? 0.71267 0.68795 0.75898 0.00996  -0.06161 0.01363  275 PHE A CD2 
1923 C  CE1 . PHE A 293 ? 0.70899 0.66556 0.74326 -0.00372 -0.06128 0.02710  275 PHE A CE1 
1924 C  CE2 . PHE A 293 ? 0.75789 0.73209 0.80544 0.00516  -0.05833 0.01067  275 PHE A CE2 
1925 C  CZ  . PHE A 293 ? 0.61480 0.57798 0.65520 -0.00125 -0.05857 0.01814  275 PHE A CZ  
1926 N  N   . ARG A 294 ? 0.61158 0.57612 0.63001 0.00185  -0.06464 0.03524  276 ARG A N   
1927 C  CA  . ARG A 294 ? 0.59995 0.56306 0.60978 0.00269  -0.06552 0.03554  276 ARG A CA  
1928 C  C   . ARG A 294 ? 0.69023 0.62611 0.67220 0.00465  -0.07268 0.03845  276 ARG A C   
1929 O  O   . ARG A 294 ? 0.75729 0.67515 0.72414 -0.00089 -0.07397 0.04268  276 ARG A O   
1930 C  CB  . ARG A 294 ? 0.68108 0.65499 0.69436 -0.00768 -0.05903 0.03815  276 ARG A CB  
1931 C  CG  . ARG A 294 ? 0.76379 0.76005 0.79826 -0.00529 -0.05454 0.03392  276 ARG A CG  
1932 C  CD  . ARG A 294 ? 0.74152 0.75159 0.78417 -0.01356 -0.04918 0.03414  276 ARG A CD  
1933 N  NE  . ARG A 294 ? 0.93858 0.96410 1.00072 -0.00913 -0.04723 0.03035  276 ARG A NE  
1934 C  CZ  . ARG A 294 ? 1.02573 1.06712 1.09894 -0.01046 -0.04388 0.02695  276 ARG A CZ  
1935 N  NH1 . ARG A 294 ? 1.08577 1.13498 1.15567 -0.01802 -0.04029 0.02575  276 ARG A NH1 
1936 N  NH2 . ARG A 294 ? 1.07866 1.12671 1.16448 -0.00450 -0.04411 0.02372  276 ARG A NH2 
1937 N  N   . ALA A 295 ? 0.69285 0.62326 0.66539 0.01261  -0.07808 0.03596  277 ALA A N   
1938 C  CA  . ALA A 295 ? 0.79240 0.69121 0.73262 0.01691  -0.08748 0.03853  277 ALA A CA  
1939 C  C   . ALA A 295 ? 0.80164 0.69937 0.73201 0.02028  -0.09044 0.03741  277 ALA A C   
1940 O  O   . ALA A 295 ? 0.75456 0.67832 0.70764 0.02456  -0.08751 0.03176  277 ALA A O   
1941 C  CB  . ALA A 295 ? 0.73285 0.62127 0.67067 0.03215  -0.09763 0.03279  277 ALA A CB  
1942 N  N   . PRO A 296 ? 0.75945 0.62466 0.65297 0.01741  -0.09621 0.04263  278 PRO A N   
1943 C  CA  . PRO A 296 ? 0.87913 0.74068 0.75893 0.01857  -0.09878 0.04229  278 PRO A CA  
1944 C  C   . PRO A 296 ? 0.80937 0.67733 0.69550 0.03879  -0.11042 0.03383  278 PRO A C   
1945 O  O   . PRO A 296 ? 0.85311 0.72657 0.73573 0.04030  -0.11162 0.03197  278 PRO A O   
1946 C  CB  . PRO A 296 ? 0.72527 0.54193 0.55605 0.00885  -0.10277 0.05041  278 PRO A CB  
1947 C  CG  . PRO A 296 ? 0.91767 0.71058 0.73540 0.01023  -0.10735 0.05304  278 PRO A CG  
1948 C  CD  . PRO A 296 ? 0.81232 0.64070 0.67164 0.00865  -0.09853 0.04977  278 PRO A CD  
1949 N  N   . SER A 297 ? 0.82569 0.69574 0.72189 0.05390  -0.11879 0.02702  279 SER A N   
1950 C  CA  . SER A 297 ? 0.80095 0.68416 0.70761 0.07326  -0.12980 0.01527  279 SER A CA  
1951 C  C   . SER A 297 ? 0.75252 0.66617 0.69484 0.08015  -0.12702 0.00453  279 SER A C   
1952 O  O   . SER A 297 ? 0.78866 0.70273 0.73903 0.07298  -0.12035 0.00758  279 SER A O   
1953 C  CB  . SER A 297 ? 0.84216 0.68698 0.71137 0.08908  -0.14884 0.01447  279 SER A CB  
1954 O  OG  . SER A 297 ? 0.84797 0.67369 0.70886 0.09569  -0.15493 0.01384  279 SER A OG  
1955 N  N   . MET A 298 ? 0.73170 0.67170 0.69438 0.09277  -0.13175 -0.00922 280 MET A N   
1956 C  CA  . MET A 298 ? 0.80079 0.77144 0.79570 0.09673  -0.12766 -0.02201 280 MET A CA  
1957 C  C   . MET A 298 ? 0.79929 0.75536 0.78659 0.10953  -0.13805 -0.02761 280 MET A C   
1958 O  O   . MET A 298 ? 0.79666 0.76582 0.80169 0.10588  -0.13128 -0.03210 280 MET A O   
1959 C  CB  . MET A 298 ? 0.76171 0.76688 0.77988 0.10449  -0.12895 -0.03775 280 MET A CB  
1960 C  CG  . MET A 298 ? 0.90762 0.93028 0.93750 0.09096  -0.11666 -0.03424 280 MET A CG  
1961 S  SD  . MET A 298 ? 1.03190 1.06599 1.08060 0.07132  -0.09753 -0.02779 280 MET A SD  
1962 C  CE  . MET A 298 ? 0.70838 0.76620 0.78043 0.07530  -0.09558 -0.04448 280 MET A CE  
1963 N  N   . LYS A 299 ? 0.72673 0.65278 0.68492 0.12485  -0.15509 -0.02773 281 LYS A N   
1964 C  CA  . LYS A 299 ? 0.76638 0.67422 0.71422 0.13927  -0.16671 -0.03372 281 LYS A CA  
1965 C  C   . LYS A 299 ? 0.82082 0.70290 0.75426 0.12521  -0.15906 -0.02023 281 LYS A C   
1966 O  O   . LYS A 299 ? 0.76087 0.64780 0.70532 0.12814  -0.15806 -0.02632 281 LYS A O   
1967 C  CB  . LYS A 299 ? 0.72290 0.59623 0.63579 0.15991  -0.18876 -0.03583 281 LYS A CB  
1968 N  N   . GLU A 300 ? 0.76521 0.62215 0.67471 0.10888  -0.15304 -0.00337 282 GLU A N   
1969 C  CA  . GLU A 300 ? 0.83162 0.67037 0.73092 0.09307  -0.14434 0.00794  282 GLU A CA  
1970 C  C   . GLU A 300 ? 0.78016 0.65516 0.71631 0.08119  -0.12877 0.00603  282 GLU A C   
1971 O  O   . GLU A 300 ? 0.72965 0.59977 0.66794 0.07608  -0.12497 0.00769  282 GLU A O   
1972 C  CB  . GLU A 300 ? 0.84089 0.65169 0.70935 0.07618  -0.13989 0.02311  282 GLU A CB  
1973 C  CG  . GLU A 300 ? 0.90340 0.66095 0.72113 0.08217  -0.15417 0.02863  282 GLU A CG  
1974 C  CD  . GLU A 300 ? 1.01122 0.74260 0.79686 0.06054  -0.14675 0.04210  282 GLU A CD  
1975 O  OE1 . GLU A 300 ? 1.11641 0.83155 0.88893 0.04392  -0.13898 0.04968  282 GLU A OE1 
1976 O  OE2 . GLU A 300 ? 1.08890 0.81784 0.86268 0.05899  -0.14805 0.04385  282 GLU A OE2 
1977 N  N   . LEU A 301 ? 0.68830 0.59653 0.65044 0.07662  -0.12027 0.00247  283 LEU A N   
1978 C  CA  . LEU A 301 ? 0.68151 0.61700 0.67187 0.06539  -0.10676 0.00125  283 LEU A CA  
1979 C  C   . LEU A 301 ? 0.70584 0.65704 0.71417 0.07290  -0.10742 -0.01167 283 LEU A C   
1980 O  O   . LEU A 301 ? 0.66401 0.62071 0.68193 0.06344  -0.09909 -0.01010 283 LEU A O   
1981 C  CB  . LEU A 301 ? 0.59013 0.55205 0.59940 0.05975  -0.09865 -0.00058 283 LEU A CB  
1982 C  CG  . LEU A 301 ? 0.72031 0.70296 0.75188 0.04811  -0.08587 -0.00082 283 LEU A CG  
1983 C  CD1 . LEU A 301 ? 0.72211 0.69150 0.74562 0.03560  -0.08042 0.01170  283 LEU A CD1 
1984 C  CD2 . LEU A 301 ? 0.68307 0.68770 0.72996 0.04483  -0.07953 -0.00471 283 LEU A CD2 
1985 N  N   . GLN A 302 ? 0.66216 0.62168 0.67482 0.08982  -0.11754 -0.02582 284 GLN A N   
1986 C  CA  . GLN A 302 ? 0.70084 0.67900 0.73173 0.09670  -0.11767 -0.04142 284 GLN A CA  
1987 C  C   . GLN A 302 ? 0.71175 0.66349 0.72649 0.09907  -0.12213 -0.03772 284 GLN A C   
1988 O  O   . GLN A 302 ? 0.64080 0.60414 0.66880 0.09447  -0.11555 -0.04388 284 GLN A O   
1989 C  CB  . GLN A 302 ? 0.64956 0.64722 0.69103 0.11595  -0.12880 -0.06052 284 GLN A CB  
1990 N  N   . VAL A 303 ? 0.71979 0.63335 0.70275 0.10481  -0.13287 -0.02791 285 VAL A N   
1991 C  CA  . VAL A 303 ? 0.69348 0.57676 0.65651 0.10533  -0.13686 -0.02339 285 VAL A CA  
1992 C  C   . VAL A 303 ? 0.72193 0.60436 0.68776 0.08381  -0.12279 -0.01114 285 VAL A C   
1993 O  O   . VAL A 303 ? 0.74563 0.62805 0.71620 0.08068  -0.11937 -0.01383 285 VAL A O   
1994 C  CB  . VAL A 303 ? 0.71317 0.54956 0.63468 0.11364  -0.15109 -0.01500 285 VAL A CB  
1995 C  CG1 . VAL A 303 ? 0.72541 0.52575 0.62182 0.10949  -0.15308 -0.00805 285 VAL A CG1 
1996 C  CG2 . VAL A 303 ? 0.69729 0.53203 0.61443 0.13940  -0.16873 -0.02937 285 VAL A CG2 
1997 N  N   . LEU A 304 ? 0.75727 0.64065 0.72086 0.06945  -0.11505 0.00106  286 LEU A N   
1998 C  CA  . LEU A 304 ? 0.68562 0.57203 0.65398 0.05109  -0.10348 0.01081  286 LEU A CA  
1999 C  C   . LEU A 304 ? 0.72527 0.64120 0.72165 0.04689  -0.09446 0.00339  286 LEU A C   
2000 O  O   . LEU A 304 ? 0.66903 0.58237 0.66654 0.03796  -0.08935 0.00654  286 LEU A O   
2001 C  CB  . LEU A 304 ? 0.71625 0.60441 0.68103 0.03939  -0.09784 0.02115  286 LEU A CB  
2002 C  CG  . LEU A 304 ? 0.73969 0.64036 0.71580 0.02309  -0.08689 0.02829  286 LEU A CG  
2003 C  CD1 . LEU A 304 ? 0.71159 0.59337 0.67369 0.01447  -0.08634 0.03403  286 LEU A CD1 
2004 C  CD2 . LEU A 304 ? 0.66446 0.56959 0.63801 0.01510  -0.08293 0.03456  286 LEU A CD2 
2005 N  N   . THR A 305 ? 0.67930 0.62162 0.69564 0.05193  -0.09230 -0.00696 287 THR A N   
2006 C  CA  . THR A 305 ? 0.67078 0.63684 0.70793 0.04516  -0.08275 -0.01474 287 THR A CA  
2007 C  C   . THR A 305 ? 0.69709 0.66416 0.73710 0.04989  -0.08416 -0.02574 287 THR A C   
2008 O  O   . THR A 305 ? 0.63135 0.60400 0.67717 0.03958  -0.07604 -0.02687 287 THR A O   
2009 C  CB  . THR A 305 ? 0.57594 0.56840 0.63056 0.04733  -0.07940 -0.02474 287 THR A CB  
2010 O  OG1 . THR A 305 ? 0.64669 0.63831 0.69917 0.04142  -0.07661 -0.01450 287 THR A OG1 
2011 C  CG2 . THR A 305 ? 0.64296 0.65571 0.71335 0.03804  -0.06881 -0.03451 287 THR A CG2 
2012 N  N   . LYS A 306 ? 0.61047 0.57046 0.64450 0.06604  -0.09517 -0.03457 288 LYS A N   
2013 C  CA  . LYS A 306 ? 0.70740 0.67081 0.74598 0.07255  -0.09706 -0.04785 288 LYS A CA  
2014 C  C   . LYS A 306 ? 0.68559 0.62280 0.70743 0.06482  -0.09608 -0.03726 288 LYS A C   
2015 O  O   . LYS A 306 ? 0.68487 0.62930 0.71362 0.05941  -0.09021 -0.04390 288 LYS A O   
2016 C  CB  . LYS A 306 ? 0.68427 0.64575 0.72010 0.09531  -0.11173 -0.06153 288 LYS A CB  
2017 C  CG  . LYS A 306 ? 0.76731 0.72164 0.80045 0.10591  -0.11763 -0.07341 288 LYS A CG  
2018 C  CD  . LYS A 306 ? 0.83080 0.82166 0.89086 0.10041  -0.10689 -0.09214 288 LYS A CD  
2019 C  CE  . LYS A 306 ? 0.86376 0.84723 0.92086 0.10932  -0.11142 -0.10376 288 LYS A CE  
2020 N  NZ  . LYS A 306 ? 0.86162 0.87849 0.94139 0.09892  -0.09816 -0.12102 288 LYS A NZ  
2021 N  N   . LYS A 307 ? 0.68109 0.58820 0.67971 0.06233  -0.10093 -0.02166 289 LYS A N   
2022 C  CA  . LYS A 307 ? 0.66489 0.54862 0.64741 0.05269  -0.09929 -0.01206 289 LYS A CA  
2023 C  C   . LYS A 307 ? 0.68421 0.58199 0.67813 0.03496  -0.08726 -0.00575 289 LYS A C   
2024 O  O   . LYS A 307 ? 0.72673 0.61899 0.71788 0.02809  -0.08400 -0.00546 289 LYS A O   
2025 C  CB  . LYS A 307 ? 0.69800 0.54805 0.65173 0.05029  -0.10537 0.00173  289 LYS A CB  
2026 C  CG  . LYS A 307 ? 0.87395 0.70205 0.80840 0.06779  -0.11912 -0.00222 289 LYS A CG  
2027 C  CD  . LYS A 307 ? 1.00849 0.79529 0.91154 0.07239  -0.12802 0.00001  289 LYS A CD  
2028 C  CE  . LYS A 307 ? 0.84106 0.59773 0.71743 0.09090  -0.14410 -0.00276 289 LYS A CE  
2029 N  NZ  . LYS A 307 ? 1.05506 0.76046 0.89067 0.09169  -0.15248 0.00310  289 LYS A NZ  
2030 N  N   . ALA A 308 ? 0.71101 0.62486 0.71576 0.02829  -0.08162 -0.00105 290 ALA A N   
2031 C  CA  . ALA A 308 ? 0.69700 0.62154 0.71029 0.01452  -0.07257 0.00354  290 ALA A CA  
2032 C  C   . ALA A 308 ? 0.68595 0.62540 0.71069 0.01246  -0.06666 -0.00851 290 ALA A C   
2033 O  O   . ALA A 308 ? 0.71343 0.64929 0.73518 0.00243  -0.06198 -0.00609 290 ALA A O   
2034 C  CB  . ALA A 308 ? 0.56778 0.50447 0.58903 0.01053  -0.06908 0.00900  290 ALA A CB  
2035 N  N   . GLU A 309 ? 0.59144 0.54854 0.62840 0.02083  -0.06662 -0.02279 291 GLU A N   
2036 C  CA  . GLU A 309 ? 0.63289 0.60700 0.68039 0.01672  -0.05943 -0.03763 291 GLU A CA  
2037 C  C   . GLU A 309 ? 0.68694 0.64985 0.72701 0.01673  -0.06054 -0.04143 291 GLU A C   
2038 O  O   . GLU A 309 ? 0.68610 0.65198 0.72574 0.00504  -0.05252 -0.04487 291 GLU A O   
2039 C  CB  . GLU A 309 ? 0.64807 0.64676 0.71162 0.02725  -0.06059 -0.05559 291 GLU A CB  
2040 C  CG  . GLU A 309 ? 0.73826 0.75498 0.81243 0.02857  -0.05676 -0.07629 291 GLU A CG  
2041 C  CD  . GLU A 309 ? 0.98365 1.03403 1.07699 0.02619  -0.04962 -0.09508 291 GLU A CD  
2042 O  OE1 . GLU A 309 ? 0.98330 1.05019 1.08342 0.01551  -0.03936 -0.10976 291 GLU A OE1 
2043 O  OE2 . GLU A 309 ? 1.01130 1.07193 1.11179 0.03349  -0.05362 -0.09611 291 GLU A OE2 
2044 N  N   . ASP A 310 ? 0.58147 0.52790 0.61207 0.02920  -0.07063 -0.04082 292 ASP A N   
2045 C  CA  . ASP A 310 ? 0.67626 0.60773 0.69702 0.02929  -0.07228 -0.04330 292 ASP A CA  
2046 C  C   . ASP A 310 ? 0.66661 0.58311 0.67570 0.01307  -0.06736 -0.02860 292 ASP A C   
2047 O  O   . ASP A 310 ? 0.64820 0.56350 0.65495 0.00550  -0.06255 -0.03272 292 ASP A O   
2048 C  CB  . ASP A 310 ? 0.66504 0.57287 0.67087 0.04518  -0.08525 -0.04284 292 ASP A CB  
2049 C  CG  . ASP A 310 ? 0.75473 0.67688 0.77137 0.06494  -0.09305 -0.06102 292 ASP A CG  
2050 O  OD1 . ASP A 310 ? 0.71628 0.67148 0.75518 0.06448  -0.08654 -0.07674 292 ASP A OD1 
2051 O  OD2 . ASP A 310 ? 0.73650 0.63605 0.73760 0.08057  -0.10610 -0.06054 292 ASP A OD2 
2052 N  N   . CYS A 311 ? 0.59682 0.50370 0.59892 0.00762  -0.06872 -0.01287 293 CYS A N   
2053 C  CA  . CYS A 311 ? 0.62825 0.52511 0.62165 -0.00605 -0.06577 -0.00097 293 CYS A CA  
2054 C  C   . CYS A 311 ? 0.66473 0.57402 0.66455 -0.01680 -0.05759 -0.00322 293 CYS A C   
2055 O  O   . CYS A 311 ? 0.58123 0.48258 0.57293 -0.02603 -0.05540 -0.00051 293 CYS A O   
2056 C  CB  . CYS A 311 ? 0.59837 0.48929 0.58686 -0.00922 -0.06848 0.01251  293 CYS A CB  
2057 S  SG  . CYS A 311 ? 0.63728 0.50149 0.60518 -0.00474 -0.07664 0.01859  293 CYS A SG  
2058 N  N   . PHE A 312 ? 0.51074 0.43658 0.52170 -0.01653 -0.05322 -0.00842 294 PHE A N   
2059 C  CA  . PHE A 312 ? 0.58708 0.51775 0.59715 -0.02829 -0.04537 -0.01057 294 PHE A CA  
2060 C  C   . PHE A 312 ? 0.66623 0.60105 0.67522 -0.03319 -0.03927 -0.02437 294 PHE A C   
2061 O  O   . PHE A 312 ? 0.62532 0.55165 0.62296 -0.04542 -0.03455 -0.02297 294 PHE A O   
2062 C  CB  . PHE A 312 ? 0.58776 0.53197 0.60675 -0.02839 -0.04157 -0.01335 294 PHE A CB  
2063 C  CG  . PHE A 312 ? 0.67860 0.61940 0.69786 -0.02615 -0.04587 -0.00050 294 PHE A CG  
2064 C  CD1 . PHE A 312 ? 0.63698 0.56587 0.64731 -0.03158 -0.04863 0.01124  294 PHE A CD1 
2065 C  CD2 . PHE A 312 ? 0.59649 0.54814 0.62566 -0.01826 -0.04751 -0.00185 294 PHE A CD2 
2066 C  CE1 . PHE A 312 ? 0.59741 0.52786 0.61083 -0.02905 -0.05231 0.02000  294 PHE A CE1 
2067 C  CE2 . PHE A 312 ? 0.68709 0.63738 0.71694 -0.01702 -0.05045 0.00835  294 PHE A CE2 
2068 C  CZ  . PHE A 312 ? 0.62443 0.56537 0.64744 -0.02238 -0.05251 0.01857  294 PHE A CZ  
2069 N  N   . ARG A 313 ? 0.58354 0.53146 0.60334 -0.02335 -0.03988 -0.03899 295 ARG A N   
2070 C  CA  . ARG A 313 ? 0.61859 0.57604 0.64072 -0.02767 -0.03326 -0.05577 295 ARG A CA  
2071 C  C   . ARG A 313 ? 0.64455 0.58405 0.65422 -0.02950 -0.03586 -0.05237 295 ARG A C   
2072 O  O   . ARG A 313 ? 0.56473 0.50482 0.56872 -0.04057 -0.02840 -0.06006 295 ARG A O   
2073 C  CB  . ARG A 313 ? 0.59049 0.57125 0.63073 -0.01386 -0.03491 -0.07534 295 ARG A CB  
2074 C  CG  . ARG A 313 ? 0.71921 0.72192 0.77269 -0.01479 -0.03048 -0.08220 295 ARG A CG  
2075 C  CD  . ARG A 313 ? 0.79503 0.82980 0.86836 -0.00782 -0.02760 -0.10848 295 ARG A CD  
2076 N  NE  . ARG A 313 ? 0.79995 0.85567 0.88568 -0.00860 -0.02433 -0.11454 295 ARG A NE  
2077 C  CZ  . ARG A 313 ? 0.74964 0.81694 0.83534 -0.02696 -0.01120 -0.12080 295 ARG A CZ  
2078 N  NH1 . ARG A 313 ? 0.77255 0.83277 0.84541 -0.04620 0.00003  -0.12307 295 ARG A NH1 
2079 N  NH2 . ARG A 313 ? 0.73301 0.81628 0.82833 -0.02709 -0.00926 -0.12479 295 ARG A NH2 
2080 N  N   . ALA A 314 ? 0.53268 0.45465 0.53538 -0.02090 -0.04554 -0.04120 296 ALA A N   
2081 C  CA  . ALA A 314 ? 0.58720 0.49034 0.57627 -0.02399 -0.04791 -0.03763 296 ALA A CA  
2082 C  C   . ALA A 314 ? 0.64324 0.53737 0.62029 -0.04079 -0.04321 -0.02786 296 ALA A C   
2083 O  O   . ALA A 314 ? 0.61425 0.50156 0.58234 -0.04831 -0.03995 -0.03201 296 ALA A O   
2084 C  CB  . ALA A 314 ? 0.52415 0.40721 0.50369 -0.01529 -0.05807 -0.02674 296 ALA A CB  
2085 N  N   . ALA A 315 ? 0.57494 0.46823 0.55063 -0.04581 -0.04378 -0.01569 297 ALA A N   
2086 C  CA  . ALA A 315 ? 0.62202 0.50500 0.58449 -0.05881 -0.04221 -0.00705 297 ALA A CA  
2087 C  C   . ALA A 315 ? 0.66806 0.55314 0.62357 -0.07032 -0.03279 -0.01725 297 ALA A C   
2088 O  O   . ALA A 315 ? 0.60583 0.47785 0.54533 -0.08086 -0.03136 -0.01506 297 ALA A O   
2089 C  CB  . ALA A 315 ? 0.46476 0.34815 0.42860 -0.05872 -0.04578 0.00479  297 ALA A CB  
2090 N  N   . ALA A 316 ? 0.66698 0.56842 0.63273 -0.06994 -0.02586 -0.02944 298 ALA A N   
2091 C  CA  . ALA A 316 ? 0.57483 0.48005 0.53286 -0.08401 -0.01451 -0.04227 298 ALA A CA  
2092 C  C   . ALA A 316 ? 0.69053 0.59737 0.64699 -0.08608 -0.01113 -0.05428 298 ALA A C   
2093 O  O   . ALA A 316 ? 0.67144 0.56722 0.61015 -0.10083 -0.00515 -0.05625 298 ALA A O   
2094 C  CB  . ALA A 316 ? 0.57681 0.50442 0.54928 -0.08364 -0.00719 -0.05594 298 ALA A CB  
2095 N  N   . LEU A 317 ? 0.56272 0.48059 0.53506 -0.07085 -0.01571 -0.06266 299 LEU A N   
2096 C  CA  . LEU A 317 ? 0.55870 0.47735 0.53027 -0.06990 -0.01384 -0.07537 299 LEU A CA  
2097 C  C   . LEU A 317 ? 0.62864 0.52210 0.58010 -0.07751 -0.01730 -0.06252 299 LEU A C   
2098 O  O   . LEU A 317 ? 0.66430 0.55403 0.60529 -0.08837 -0.01086 -0.07048 299 LEU A O   
2099 C  CB  . LEU A 317 ? 0.57364 0.50085 0.56115 -0.04859 -0.02208 -0.08429 299 LEU A CB  
2100 C  CG  . LEU A 317 ? 0.74093 0.66581 0.72759 -0.04271 -0.02307 -0.09788 299 LEU A CG  
2101 C  CD1 . LEU A 317 ? 0.68686 0.63313 0.67879 -0.05438 -0.00971 -0.11999 299 LEU A CD1 
2102 C  CD2 . LEU A 317 ? 0.58207 0.50957 0.58010 -0.01868 -0.03419 -0.10596 299 LEU A CD2 
2103 N  N   . ALA A 318 ? 0.57236 0.45027 0.51828 -0.07311 -0.02695 -0.04399 300 ALA A N   
2104 C  CA  . ALA A 318 ? 0.66942 0.52701 0.59850 -0.07983 -0.03118 -0.03326 300 ALA A CA  
2105 C  C   . ALA A 318 ? 0.62647 0.47455 0.53756 -0.09662 -0.02689 -0.02814 300 ALA A C   
2106 O  O   . ALA A 318 ? 0.60793 0.44332 0.50370 -0.10549 -0.02635 -0.02763 300 ALA A O   
2107 C  CB  . ALA A 318 ? 0.63010 0.47836 0.55927 -0.07298 -0.04136 -0.01747 300 ALA A CB  
2108 N  N   . SER A 319 ? 0.63044 0.48111 0.53990 -0.10102 -0.02459 -0.02434 301 SER A N   
2109 C  CA  . SER A 319 ? 0.66147 0.49551 0.54753 -0.11538 -0.02309 -0.01803 301 SER A CA  
2110 C  C   . SER A 319 ? 0.73670 0.57060 0.61010 -0.13059 -0.01010 -0.03207 301 SER A C   
2111 O  O   . SER A 319 ? 0.69540 0.50920 0.54206 -0.14475 -0.00837 -0.02890 301 SER A O   
2112 C  CB  . SER A 319 ? 0.70791 0.53845 0.59287 -0.11263 -0.02817 -0.00676 301 SER A CB  
2113 O  OG  . SER A 319 ? 0.66964 0.51448 0.56616 -0.11128 -0.02101 -0.01506 301 SER A OG  
2114 N  N   . GLY A 320 ? 0.68658 0.54276 0.57728 -0.12869 -0.00107 -0.04868 302 GLY A N   
2115 C  CA  . GLY A 320 ? 0.58776 0.44954 0.46886 -0.14554 0.01348  -0.06513 302 GLY A CA  
2116 C  C   . GLY A 320 ? 0.80934 0.67026 0.68299 -0.15487 0.01975  -0.06552 302 GLY A C   
2117 O  O   . GLY A 320 ? 0.83788 0.70148 0.69936 -0.17296 0.03356  -0.07962 302 GLY A O   
2118 N  N   . CYS A 321 ? 0.61220 0.46899 0.49130 -0.14454 0.01089  -0.05159 303 CYS A N   
2119 C  CA  . CYS A 321 ? 0.73537 0.58765 0.60589 -0.15191 0.01542  -0.05061 303 CYS A CA  
2120 C  C   . CYS A 321 ? 0.72187 0.60756 0.62103 -0.14622 0.02245  -0.06646 303 CYS A C   
2121 O  O   . CYS A 321 ? 0.73763 0.64729 0.66438 -0.13087 0.01918  -0.07411 303 CYS A O   
2122 C  CB  . CYS A 321 ? 0.67774 0.51247 0.54290 -0.14174 0.00204  -0.03018 303 CYS A CB  
2123 S  SG  . CYS A 321 ? 0.78997 0.58800 0.62227 -0.14596 -0.00925 -0.01301 303 CYS A SG  
2124 N  N   . THR A 322 ? 0.65923 0.54404 0.54896 -0.15873 0.03137  -0.07184 304 THR A N   
2125 C  CA  . THR A 322 ? 0.74519 0.66014 0.66102 -0.15258 0.03573  -0.08395 304 THR A CA  
2126 C  C   . THR A 322 ? 0.78764 0.69412 0.70768 -0.13977 0.02514  -0.06708 304 THR A C   
2127 O  O   . THR A 322 ? 0.77326 0.65045 0.67298 -0.13935 0.01685  -0.04888 304 THR A O   
2128 C  CB  . THR A 322 ? 0.69674 0.61904 0.60091 -0.17598 0.05336  -0.10234 304 THR A CB  
2129 O  OG1 . THR A 322 ? 0.81876 0.70317 0.68555 -0.19154 0.05501  -0.08964 304 THR A OG1 
2130 C  CG2 . THR A 322 ? 0.69797 0.62926 0.59637 -0.19096 0.06511  -0.12033 304 THR A CG2 
2131 N  N   . VAL A 323 ? 0.69108 0.62496 0.63823 -0.12845 0.02481  -0.07464 305 VAL A N   
2132 C  CA  . VAL A 323 ? 0.65935 0.59060 0.61570 -0.11371 0.01439  -0.06032 305 VAL A CA  
2133 C  C   . VAL A 323 ? 0.70288 0.65537 0.67299 -0.11485 0.02082  -0.07163 305 VAL A C   
2134 O  O   . VAL A 323 ? 0.70671 0.68946 0.69548 -0.11564 0.02807  -0.09183 305 VAL A O   
2135 C  CB  . VAL A 323 ? 0.65112 0.59107 0.62763 -0.09245 0.00186  -0.05313 305 VAL A CB  
2136 C  CG1 . VAL A 323 ? 0.60855 0.57800 0.60893 -0.08324 0.00369  -0.07164 305 VAL A CG1 
2137 C  CG2 . VAL A 323 ? 0.63287 0.57117 0.61744 -0.07984 -0.00728 -0.03965 305 VAL A CG2 
2138 N  N   . GLU A 324 ? 0.70149 0.63937 0.66280 -0.11453 0.01775  -0.06006 306 GLU A N   
2139 C  CA  . GLU A 324 ? 0.73999 0.69612 0.71512 -0.11277 0.02129  -0.06742 306 GLU A CA  
2140 C  C   . GLU A 324 ? 0.79035 0.75021 0.78189 -0.09212 0.00840  -0.05415 306 GLU A C   
2141 O  O   . GLU A 324 ? 0.83568 0.77286 0.81557 -0.08755 0.00011  -0.03685 306 GLU A O   
2142 C  CB  . GLU A 324 ? 0.80897 0.74227 0.75672 -0.13137 0.02971  -0.06656 306 GLU A CB  
2143 C  CG  . GLU A 324 ? 0.89657 0.83801 0.85426 -0.12582 0.02871  -0.06574 306 GLU A CG  
2144 C  CD  . GLU A 324 ? 1.11441 1.03444 1.04394 -0.14661 0.03933  -0.06951 306 GLU A CD  
2145 O  OE1 . GLU A 324 ? 1.24953 1.18268 1.17546 -0.16544 0.05386  -0.08819 306 GLU A OE1 
2146 O  OE2 . GLU A 324 ? 1.09149 0.98136 1.00156 -0.14445 0.03322  -0.05510 306 GLU A OE2 
2147 N  N   . ILE A 325 ? 0.74007 0.72896 0.75765 -0.07984 0.00638  -0.06356 307 ILE A N   
2148 C  CA  . ILE A 325 ? 0.72639 0.71942 0.75734 -0.06239 -0.00436 -0.05315 307 ILE A CA  
2149 C  C   . ILE A 325 ? 0.73811 0.74588 0.77742 -0.06378 -0.00002 -0.06045 307 ILE A C   
2150 O  O   . ILE A 325 ? 0.80656 0.84211 0.86252 -0.06252 0.00410  -0.07811 307 ILE A O   
2151 C  CB  . ILE A 325 ? 0.73674 0.74406 0.78465 -0.04577 -0.01270 -0.05650 307 ILE A CB  
2152 C  CG1 . ILE A 325 ? 0.66141 0.65062 0.69870 -0.04528 -0.01718 -0.04758 307 ILE A CG1 
2153 C  CG2 . ILE A 325 ? 0.66214 0.67301 0.71987 -0.03070 -0.02211 -0.04814 307 ILE A CG2 
2154 C  CD1 . ILE A 325 ? 0.65625 0.65222 0.70392 -0.03023 -0.02530 -0.05123 307 ILE A CD1 
2155 N  N   . LYS A 326 ? 0.69123 0.68172 0.71946 -0.06587 -0.00136 -0.04850 308 LYS A N   
2156 C  CA  . LYS A 326 ? 0.77858 0.77748 0.80994 -0.06964 0.00358  -0.05429 308 LYS A CA  
2157 C  C   . LYS A 326 ? 0.71238 0.71517 0.75540 -0.05388 -0.00593 -0.04398 308 LYS A C   
2158 O  O   . LYS A 326 ? 0.73200 0.71545 0.76590 -0.05004 -0.01187 -0.02894 308 LYS A O   
2159 C  CB  . LYS A 326 ? 0.78593 0.75696 0.78967 -0.08665 0.01076  -0.05091 308 LYS A CB  
2160 C  CG  . LYS A 326 ? 0.81396 0.78910 0.81683 -0.09264 0.01670  -0.05701 308 LYS A CG  
2161 C  CD  . LYS A 326 ? 0.94454 0.88774 0.91353 -0.11316 0.02566  -0.05738 308 LYS A CD  
2162 N  N   . GLY A 327 ? 0.78119 0.80993 0.84386 -0.04483 -0.00765 -0.05348 309 GLY A N   
2163 C  CA  . GLY A 327 ? 0.67834 0.71030 0.74915 -0.03208 -0.01547 -0.04512 309 GLY A CA  
2164 C  C   . GLY A 327 ? 0.68384 0.70933 0.74851 -0.03801 -0.01134 -0.04258 309 GLY A C   
2165 O  O   . GLY A 327 ? 0.70293 0.72427 0.75799 -0.05197 -0.00204 -0.05020 309 GLY A O   
2166 N  N   . GLY A 328 ? 0.72793 0.75070 0.79591 -0.02833 -0.01791 -0.03227 310 GLY A N   
2167 C  CA  . GLY A 328 ? 0.77665 0.79306 0.83960 -0.03159 -0.01512 -0.03006 310 GLY A CA  
2168 C  C   . GLY A 328 ? 0.76075 0.79692 0.83207 -0.03598 -0.00885 -0.04458 310 GLY A C   
2169 O  O   . GLY A 328 ? 0.64053 0.70060 0.72626 -0.03193 -0.00943 -0.05628 310 GLY A O   
2170 N  N   . ALA A 329 ? 0.85514 0.88073 0.91655 -0.04376 -0.00356 -0.04491 311 ALA A N   
2171 C  CA  . ALA A 329 ? 0.97502 1.01854 1.04242 -0.05090 0.00371  -0.05953 311 ALA A CA  
2172 C  C   . ALA A 329 ? 0.87050 0.93977 0.95785 -0.03739 -0.00272 -0.06289 311 ALA A C   
2173 O  O   . ALA A 329 ? 0.74296 0.83869 0.84338 -0.03818 -0.00042 -0.07849 311 ALA A O   
2174 C  CB  . ALA A 329 ? 0.92985 0.95042 0.97829 -0.06145 0.00970  -0.05747 311 ALA A CB  
2175 N  N   . HIS A 330 ? 0.90952 0.97200 0.99838 -0.02536 -0.01106 -0.04968 312 HIS A N   
2176 C  CA  . HIS A 330 ? 0.79972 0.87943 0.90049 -0.01383 -0.01753 -0.05084 312 HIS A CA  
2177 C  C   . HIS A 330 ? 0.78560 0.85881 0.88626 -0.00231 -0.02707 -0.03895 312 HIS A C   
2178 O  O   . HIS A 330 ? 0.90393 0.96029 0.99720 -0.00239 -0.02841 -0.02666 312 HIS A O   
2179 C  CB  . HIS A 330 ? 0.92065 0.99733 1.01888 -0.01514 -0.01528 -0.04856 312 HIS A CB  
2180 C  CG  . HIS A 330 ? 0.99823 1.07967 1.09395 -0.02759 -0.00574 -0.06093 312 HIS A CG  
2181 N  ND1 . HIS A 330 ? 0.87097 0.97694 0.97683 -0.03237 -0.00189 -0.07809 312 HIS A ND1 
2182 C  CD2 . HIS A 330 ? 0.97544 1.03946 1.05813 -0.03688 0.00074  -0.05994 312 HIS A CD2 
2183 C  CE1 . HIS A 330 ? 1.01137 1.11591 1.11041 -0.04666 0.00806  -0.08712 312 HIS A CE1 
2184 N  NE2 . HIS A 330 ? 1.14188 1.21788 1.22469 -0.04952 0.00958  -0.07551 312 HIS A NE2 
2185 N  N   . ASP A 331 ? 0.73115 0.81686 0.83838 0.00744  -0.03417 -0.04382 313 ASP A N   
2186 C  CA  . ASP A 331 ? 0.65891 0.73475 0.76058 0.01709  -0.04326 -0.03314 313 ASP A CA  
2187 C  C   . ASP A 331 ? 0.71623 0.79262 0.81542 0.02049  -0.04569 -0.02848 313 ASP A C   
2188 O  O   . ASP A 331 ? 0.59464 0.68518 0.69942 0.02175  -0.04509 -0.03724 313 ASP A O   
2189 C  CB  . ASP A 331 ? 0.73546 0.81769 0.83926 0.02754  -0.05167 -0.04042 313 ASP A CB  
2190 C  CG  . ASP A 331 ? 0.74893 0.82341 0.85083 0.02591  -0.05135 -0.03991 313 ASP A CG  
2191 O  OD1 . ASP A 331 ? 0.70372 0.76733 0.80151 0.01619  -0.04498 -0.03309 313 ASP A OD1 
2192 O  OD2 . ASP A 331 ? 0.75764 0.83593 0.86104 0.03537  -0.05844 -0.04703 313 ASP A OD2 
2193 N  N   . PHE A 332 ? 0.69641 0.75912 0.78728 0.02063  -0.04771 -0.01598 314 PHE A N   
2194 C  CA  . PHE A 332 ? 0.60635 0.66902 0.69270 0.02225  -0.04925 -0.01184 314 PHE A CA  
2195 C  C   . PHE A 332 ? 0.68936 0.74539 0.76417 0.03018  -0.05875 -0.01018 314 PHE A C   
2196 O  O   . PHE A 332 ? 0.66373 0.70707 0.73003 0.03271  -0.06364 -0.00590 314 PHE A O   
2197 C  CB  . PHE A 332 ? 0.70941 0.76398 0.79293 0.01688  -0.04565 -0.00215 314 PHE A CB  
2198 C  CG  . PHE A 332 ? 0.76966 0.82677 0.85990 0.01223  -0.03886 -0.00405 314 PHE A CG  
2199 C  CD1 . PHE A 332 ? 0.69614 0.75609 0.79013 0.00921  -0.03472 -0.01181 314 PHE A CD1 
2200 C  CD2 . PHE A 332 ? 0.85657 0.91188 0.94739 0.01056  -0.03684 0.00071  314 PHE A CD2 
2201 C  CE1 . PHE A 332 ? 0.70695 0.76096 0.80002 0.00458  -0.02939 -0.01288 314 PHE A CE1 
2202 C  CE2 . PHE A 332 ? 0.78595 0.83888 0.87974 0.00906  -0.03293 -0.00150 314 PHE A CE2 
2203 C  CZ  . PHE A 332 ? 0.87671 0.92546 0.96904 0.00605  -0.02956 -0.00732 314 PHE A CZ  
2204 N  N   . TYR A 333 ? 0.64275 0.70402 0.71400 0.03411  -0.06201 -0.01360 315 TYR A N   
2205 C  CA  . TYR A 333 ? 0.64958 0.69912 0.70381 0.04265  -0.07296 -0.01236 315 TYR A CA  
2206 C  C   . TYR A 333 ? 0.66335 0.69556 0.69872 0.03652  -0.07234 -0.00099 315 TYR A C   
2207 O  O   . TYR A 333 ? 0.58394 0.62233 0.62458 0.02797  -0.06386 0.00208  315 TYR A O   
2208 C  CB  . TYR A 333 ? 0.65091 0.71450 0.70831 0.05073  -0.07860 -0.02334 315 TYR A CB  
2209 C  CG  . TYR A 333 ? 0.75780 0.84135 0.83203 0.05773  -0.08126 -0.03837 315 TYR A CG  
2210 C  CD1 . TYR A 333 ? 0.80763 0.89614 0.89355 0.05381  -0.07575 -0.04133 315 TYR A CD1 
2211 C  CD2 . TYR A 333 ? 0.79758 0.89704 0.87595 0.06756  -0.08915 -0.05126 315 TYR A CD2 
2212 C  CE1 . TYR A 333 ? 0.74906 0.85890 0.85062 0.05773  -0.07634 -0.05744 315 TYR A CE1 
2213 C  CE2 . TYR A 333 ? 0.87426 0.99813 0.97099 0.07303  -0.09083 -0.06845 315 TYR A CE2 
2214 C  CZ  . TYR A 333 ? 0.90388 1.03344 1.01235 0.06720  -0.08353 -0.07185 315 TYR A CZ  
2215 O  OH  . TYR A 333 ? 0.92806 1.08476 1.05509 0.07022  -0.08337 -0.09117 315 TYR A OH  
2216 N  N   . ASN A 334 ? 0.58172 0.59118 0.59324 0.04051  -0.08136 0.00397  316 ASN A N   
2217 C  CA  . ASN A 334 ? 0.64496 0.63624 0.63284 0.03226  -0.08042 0.01277  316 ASN A CA  
2218 C  C   . ASN A 334 ? 0.67500 0.67236 0.65768 0.03309  -0.08121 0.00940  316 ASN A C   
2219 O  O   . ASN A 334 ? 0.64977 0.65937 0.64070 0.04315  -0.08689 0.00061  316 ASN A O   
2220 C  CB  . ASN A 334 ? 0.65818 0.61626 0.61433 0.03509  -0.09039 0.01879  316 ASN A CB  
2221 C  CG  . ASN A 334 ? 0.78654 0.73511 0.73133 0.05240  -0.10565 0.01222  316 ASN A CG  
2222 O  OD1 . ASN A 334 ? 0.71534 0.67973 0.67993 0.06338  -0.10963 0.00304  316 ASN A OD1 
2223 N  ND2 . ASN A 334 ? 0.80543 0.72808 0.71695 0.05492  -0.11472 0.01561  316 ASN A ND2 
2224 N  N   . VAL A 335 ? 0.71284 0.70387 0.68231 0.02144  -0.07492 0.01498  317 VAL A N   
2225 C  CA  . VAL A 335 ? 0.70137 0.69806 0.66491 0.01993  -0.07395 0.01201  317 VAL A CA  
2226 C  C   . VAL A 335 ? 0.78985 0.75785 0.71681 0.02530  -0.08670 0.01454  317 VAL A C   
2227 O  O   . VAL A 335 ? 0.92218 0.86045 0.81836 0.01878  -0.08918 0.02248  317 VAL A O   
2228 C  CB  . VAL A 335 ? 0.68962 0.69464 0.65573 0.00486  -0.06100 0.01446  317 VAL A CB  
2229 C  CG1 . VAL A 335 ? 0.59179 0.59900 0.54669 0.00222  -0.06011 0.01149  317 VAL A CG1 
2230 C  CG2 . VAL A 335 ? 0.57645 0.60694 0.57645 0.00348  -0.05157 0.01070  317 VAL A CG2 
2231 N  N   . LEU A 336 ? 0.80623 0.78112 0.73389 0.03684  -0.09538 0.00720  318 LEU A N   
2232 C  CA  . LEU A 336 ? 0.89647 0.84261 0.78703 0.04460  -0.11016 0.00862  318 LEU A CA  
2233 C  C   . LEU A 336 ? 0.91152 0.84705 0.77816 0.03146  -0.10465 0.01292  318 LEU A C   
2234 O  O   . LEU A 336 ? 0.98904 0.95028 0.87502 0.02773  -0.09670 0.00749  318 LEU A O   
2235 C  CB  . LEU A 336 ? 0.96731 0.92893 0.86974 0.06351  -0.12315 -0.00338 318 LEU A CB  
2236 C  CG  . LEU A 336 ? 0.98493 0.95398 0.90393 0.07866  -0.13201 -0.01066 318 LEU A CG  
2237 C  CD1 . LEU A 336 ? 0.99467 0.98228 0.92362 0.09689  -0.14567 -0.02564 318 LEU A CD1 
2238 C  CD2 . LEU A 336 ? 1.08127 1.01085 0.96854 0.08241  -0.14157 -0.00220 318 LEU A CD2 
2239 N  N   . PRO A 337 ? 1.03837 0.93528 0.86112 0.02297  -0.10798 0.02181  319 PRO A N   
2240 C  CA  . PRO A 337 ? 1.04884 0.93407 0.84440 0.00865  -0.10238 0.02464  319 PRO A CA  
2241 C  C   . PRO A 337 ? 1.00099 0.87531 0.77531 0.02120  -0.11719 0.02058  319 PRO A C   
2242 O  O   . PRO A 337 ? 1.06872 0.93650 0.84048 0.04159  -0.13457 0.01625  319 PRO A O   
2243 C  CB  . PRO A 337 ? 1.06065 0.90368 0.81163 -0.00642 -0.10115 0.03491  319 PRO A CB  
2244 C  CG  . PRO A 337 ? 1.10920 0.92766 0.84873 0.00911  -0.11632 0.03741  319 PRO A CG  
2245 C  CD  . PRO A 337 ? 0.92300 0.78259 0.71592 0.02393  -0.11594 0.02928  319 PRO A CD  
2246 N  N   . ASN A 338 ? 0.86138 0.73588 0.62111 0.00901  -0.11032 0.02050  320 ASN A N   
2247 C  CA  . ASN A 338 ? 0.85334 0.71580 0.58832 0.01812  -0.12360 0.01708  320 ASN A CA  
2248 C  C   . ASN A 338 ? 1.02726 0.85518 0.71195 -0.00183 -0.11866 0.02443  320 ASN A C   
2249 O  O   . ASN A 338 ? 0.98284 0.83077 0.67800 -0.01930 -0.10147 0.02250  320 ASN A O   
2250 C  CB  . ASN A 338 ? 0.87576 0.78363 0.65237 0.02416  -0.11904 0.00574  320 ASN A CB  
2251 C  CG  . ASN A 338 ? 0.94401 0.84378 0.69909 0.03638  -0.13510 0.00023  320 ASN A CG  
2252 O  OD1 . ASN A 338 ? 0.96050 0.84474 0.68535 0.02557  -0.13300 0.00271  320 ASN A OD1 
2253 N  ND2 . ASN A 338 ? 0.85791 0.77002 0.62869 0.05872  -0.15131 -0.00875 320 ASN A ND2 
2254 N  N   . LYS A 339 ? 1.09719 0.87151 0.72505 0.00076  -0.13405 0.03186  321 LYS A N   
2255 C  CA  . LYS A 339 ? 1.13596 0.86840 0.70672 -0.02222 -0.12845 0.03986  321 LYS A CA  
2256 C  C   . LYS A 339 ? 1.14672 0.89128 0.71092 -0.03084 -0.12277 0.03532  321 LYS A C   
2257 O  O   . LYS A 339 ? 1.17049 0.91595 0.72240 -0.05652 -0.10449 0.03645  321 LYS A O   
2258 C  CB  . LYS A 339 ? 1.10611 0.77169 0.61067 -0.01430 -0.14997 0.04817  321 LYS A CB  
2259 N  N   . SER A 340 ? 1.05780 0.81404 0.63073 -0.01024 -0.13789 0.02854  322 SER A N   
2260 C  CA  . SER A 340 ? 1.07019 0.83556 0.63391 -0.01757 -0.13410 0.02399  322 SER A CA  
2261 C  C   . SER A 340 ? 1.04831 0.86593 0.66236 -0.03263 -0.10909 0.01723  322 SER A C   
2262 O  O   . SER A 340 ? 0.96096 0.77789 0.55869 -0.05382 -0.09475 0.01685  322 SER A O   
2263 C  CB  . SER A 340 ? 1.06893 0.84310 0.63883 0.00887  -0.15574 0.01587  322 SER A CB  
2264 O  OG  . SER A 340 ? 1.10318 0.83966 0.64239 0.03011  -0.18084 0.01876  322 SER A OG  
2265 N  N   . LEU A 341 ? 0.93775 0.79924 0.61115 -0.02195 -0.10385 0.01103  323 LEU A N   
2266 C  CA  . LEU A 341 ? 0.92043 0.82726 0.63986 -0.03274 -0.08281 0.00415  323 LEU A CA  
2267 C  C   . LEU A 341 ? 0.94990 0.85464 0.66447 -0.05620 -0.06389 0.00799  323 LEU A C   
2268 O  O   . LEU A 341 ? 0.91385 0.83909 0.63812 -0.07159 -0.04758 0.00258  323 LEU A O   
2269 C  CB  . LEU A 341 ? 0.90626 0.85111 0.68153 -0.01696 -0.08278 -0.00227 323 LEU A CB  
2270 C  CG  . LEU A 341 ? 0.85357 0.84196 0.67398 -0.01999 -0.06804 -0.01176 323 LEU A CG  
2271 C  CD1 . LEU A 341 ? 0.70725 0.70017 0.51504 -0.02393 -0.06729 -0.01760 323 LEU A CD1 
2272 C  CD2 . LEU A 341 ? 0.82153 0.83643 0.68355 -0.00376 -0.07237 -0.01804 323 LEU A CD2 
2273 N  N   . TRP A 342 ? 0.97527 0.85721 0.67542 -0.05937 -0.06576 0.01562  324 TRP A N   
2274 C  CA  . TRP A 342 ? 0.98694 0.87083 0.68458 -0.08244 -0.04784 0.01720  324 TRP A CA  
2275 C  C   . TRP A 342 ? 1.03320 0.88894 0.67937 -0.10660 -0.04032 0.01895  324 TRP A C   
2276 O  O   . TRP A 342 ? 1.00845 0.88619 0.66463 -0.12719 -0.02092 0.01285  324 TRP A O   
2277 C  CB  . TRP A 342 ? 1.08135 0.94531 0.77268 -0.08072 -0.05241 0.02461  324 TRP A CB  
2278 N  N   . LYS A 343 ? 1.06870 0.87521 0.65787 -0.10450 -0.05581 0.02605  325 LYS A N   
2279 C  CA  . LYS A 343 ? 1.09679 0.86968 0.62878 -0.12935 -0.04908 0.02826  325 LYS A CA  
2280 C  C   . LYS A 343 ? 1.09411 0.89809 0.64142 -0.13618 -0.03830 0.01869  325 LYS A C   
2281 O  O   . LYS A 343 ? 1.22499 1.02905 0.75233 -0.16279 -0.02109 0.01484  325 LYS A O   
2282 C  CB  . LYS A 343 ? 1.15454 0.86177 0.61764 -0.12218 -0.07150 0.03835  325 LYS A CB  
2283 N  N   . ALA A 344 ? 1.00459 0.83616 0.58701 -0.11377 -0.04735 0.01336  326 ALA A N   
2284 C  CA  . ALA A 344 ? 1.04548 0.90838 0.64620 -0.11928 -0.03678 0.00347  326 ALA A CA  
2285 C  C   . ALA A 344 ? 0.97109 0.88367 0.62377 -0.12987 -0.01417 -0.00626 326 ALA A C   
2286 O  O   . ALA A 344 ? 0.94351 0.87383 0.59727 -0.14613 0.00110  -0.01465 326 ALA A O   
2287 C  CB  . ALA A 344 ? 0.93250 0.81196 0.55694 -0.09366 -0.05216 -0.00078 326 ALA A CB  
2288 N  N   . TYR A 345 ? 0.99201 0.92668 0.68660 -0.12019 -0.01255 -0.00621 327 TYR A N   
2289 C  CA  . TYR A 345 ? 0.94831 0.92746 0.69058 -0.12708 0.00585  -0.01590 327 TYR A CA  
2290 C  C   . TYR A 345 ? 0.92866 0.90503 0.65043 -0.15512 0.02280  -0.01874 327 TYR A C   
2291 O  O   . TYR A 345 ? 0.90022 0.91010 0.64417 -0.16711 0.03957  -0.03096 327 TYR A O   
2292 C  CB  . TYR A 345 ? 0.87507 0.87293 0.66088 -0.10981 0.00148  -0.01440 327 TYR A CB  
2293 C  CG  . TYR A 345 ? 0.85034 0.88749 0.67970 -0.11523 0.01727  -0.02352 327 TYR A CG  
2294 C  CD1 . TYR A 345 ? 0.74092 0.81368 0.61080 -0.10698 0.02353  -0.03411 327 TYR A CD1 
2295 C  CD2 . TYR A 345 ? 0.80595 0.84335 0.63422 -0.12797 0.02489  -0.02255 327 TYR A CD2 
2296 C  CE1 . TYR A 345 ? 0.65523 0.76116 0.56273 -0.10864 0.03511  -0.04346 327 TYR A CE1 
2297 C  CE2 . TYR A 345 ? 0.83208 0.90759 0.70097 -0.13064 0.03712  -0.03276 327 TYR A CE2 
2298 C  CZ  . TYR A 345 ? 0.75520 0.86409 0.66327 -0.11965 0.04128  -0.04320 327 TYR A CZ  
2299 O  OH  . TYR A 345 ? 0.75934 0.90349 0.70571 -0.11921 0.05075  -0.05430 327 TYR A OH  
2300 N  N   A MET A 346 ? 0.98587 0.92305 0.66489 -0.16642 0.01900  -0.00918 328 MET A N   
2301 N  N   B MET A 346 ? 0.98646 0.92353 0.66543 -0.16635 0.01892  -0.00914 328 MET A N   
2302 C  CA  A MET A 346 ? 1.02552 0.95985 0.68250 -0.19668 0.03646  -0.01317 328 MET A CA  
2303 C  CA  B MET A 346 ? 1.02642 0.95973 0.68239 -0.19669 0.03620  -0.01292 328 MET A CA  
2304 C  C   A MET A 346 ? 1.06057 0.98698 0.68132 -0.21949 0.04762  -0.01937 328 MET A C   
2305 C  C   B MET A 346 ? 1.05989 0.98713 0.68165 -0.21914 0.04764  -0.01953 328 MET A C   
2306 O  O   A MET A 346 ? 1.06967 1.02122 0.69678 -0.24320 0.06791  -0.03123 328 MET A O   
2307 O  O   B MET A 346 ? 1.06750 1.02157 0.69764 -0.24215 0.06796  -0.03175 328 MET A O   
2308 C  CB  A MET A 346 ? 1.07969 0.96643 0.69179 -0.20501 0.02929  -0.00096 328 MET A CB  
2309 C  CB  B MET A 346 ? 1.08223 0.96579 0.69062 -0.20508 0.02852  -0.00039 328 MET A CB  
2310 C  CG  A MET A 346 ? 1.08943 0.99474 0.73955 -0.19625 0.02902  0.00022  328 MET A CG  
2311 C  CG  B MET A 346 ? 1.10081 0.99340 0.74260 -0.18880 0.02152  0.00419  328 MET A CG  
2312 S  SD  A MET A 346 ? 1.21896 1.06928 0.81445 -0.21141 0.02449  0.01235  328 MET A SD  
2313 S  SD  B MET A 346 ? 1.22810 1.06158 0.81252 -0.20131 0.01462  0.01731  328 MET A SD  
2314 C  CE  A MET A 346 ? 1.26013 1.11527 0.82681 -0.25543 0.05052  0.00192  328 MET A CE  
2315 C  CE  B MET A 346 ? 1.20402 0.97074 0.71532 -0.19609 -0.00505 0.02869  328 MET A CE  
2316 N  N   . GLU A 347 ? 1.08764 0.98158 0.67091 -0.21283 0.03464  -0.01311 329 GLU A N   
2317 C  CA  . GLU A 347 ? 1.00417 0.88811 0.54989 -0.23441 0.04451  -0.01866 329 GLU A CA  
2318 C  C   . GLU A 347 ? 1.03594 0.97718 0.63265 -0.23458 0.05992  -0.03529 329 GLU A C   
2319 O  O   . GLU A 347 ? 1.09982 1.05090 0.68111 -0.25951 0.07740  -0.04570 329 GLU A O   
2320 C  CB  . GLU A 347 ? 1.12077 0.95708 0.61613 -0.22339 0.02397  -0.00840 329 GLU A CB  
2321 N  N   . ASN A 348 ? 1.00296 0.98053 0.65794 -0.20800 0.05412  -0.03891 330 ASN A N   
2322 C  CA  . ASN A 348 ? 0.88764 0.91601 0.59042 -0.20642 0.06785  -0.05503 330 ASN A CA  
2323 C  C   . ASN A 348 ? 0.97616 1.04309 0.71389 -0.21880 0.08593  -0.06737 330 ASN A C   
2324 O  O   . ASN A 348 ? 0.81792 0.91377 0.56493 -0.23529 0.10346  -0.08294 330 ASN A O   
2325 C  CB  . ASN A 348 ? 0.81032 0.85910 0.55791 -0.17607 0.05596  -0.05505 330 ASN A CB  
2326 C  CG  . ASN A 348 ? 0.93916 0.96410 0.66050 -0.16534 0.04112  -0.04945 330 ASN A CG  
2327 O  OD1 . ASN A 348 ? 0.92798 0.95231 0.62982 -0.17573 0.04666  -0.05542 330 ASN A OD1 
2328 N  ND2 . ASN A 348 ? 0.87582 0.88335 0.59754 -0.14432 0.02200  -0.03951 330 ASN A ND2 
2329 N  N   . GLY A 349 ? 0.84573 0.91516 0.60331 -0.21087 0.08155  -0.06209 331 GLY A N   
2330 C  CA  . GLY A 349 ? 0.93405 1.04245 0.72723 -0.22006 0.09631  -0.07480 331 GLY A CA  
2331 C  C   . GLY A 349 ? 0.99542 1.10424 0.75701 -0.25520 0.11490  -0.08416 331 GLY A C   
2332 O  O   . GLY A 349 ? 0.93670 1.09070 0.72961 -0.26584 0.13150  -0.10319 331 GLY A O   
2333 N  N   . ARG A 350 ? 1.03536 1.09301 0.73258 -0.27400 0.11219  -0.07226 332 ARG A N   
2334 C  CA  . ARG A 350 ? 1.09597 1.14705 0.75338 -0.31208 0.13112  -0.08090 332 ARG A CA  
2335 C  C   . ARG A 350 ? 1.03705 1.11685 0.69932 -0.32501 0.14639  -0.09787 332 ARG A C   
2336 O  O   . ARG A 350 ? 1.10573 1.21382 0.76938 -0.35260 0.16768  -0.11546 332 ARG A O   
2337 C  CB  . ARG A 350 ? 1.03008 1.00952 0.60793 -0.32800 0.12260  -0.06321 332 ARG A CB  
2338 C  CG  . ARG A 350 ? 1.17239 1.12530 0.73465 -0.33173 0.11730  -0.05264 332 ARG A CG  
2339 C  CD  . ARG A 350 ? 1.31693 1.19462 0.81235 -0.32693 0.09715  -0.03107 332 ARG A CD  
2340 N  NE  . ARG A 350 ? 1.50530 1.35267 0.97910 -0.33342 0.09329  -0.02173 332 ARG A NE  
2341 C  CZ  . ARG A 350 ? 1.59118 1.37600 1.01604 -0.32360 0.07347  -0.00369 332 ARG A CZ  
2342 N  NH1 . ARG A 350 ? 1.57269 1.31944 0.96513 -0.30593 0.05443  0.00659  332 ARG A NH1 
2343 N  NH2 . ARG A 350 ? 1.49636 1.25695 0.90474 -0.33068 0.07190  0.00296  332 ARG A NH2 
2344 N  N   . LYS A 351 ? 0.97351 1.04906 0.63948 -0.30629 0.13651  -0.09465 333 LYS A N   
2345 C  CA  . LYS A 351 ? 1.01660 1.12155 0.69136 -0.31612 0.15060  -0.11154 333 LYS A CA  
2346 C  C   . LYS A 351 ? 1.03415 1.20631 0.78124 -0.30521 0.16176  -0.13266 333 LYS A C   
2347 O  O   . LYS A 351 ? 1.01239 1.21948 0.77004 -0.32287 0.18052  -0.15325 333 LYS A O   
2348 C  CB  . LYS A 351 ? 1.10823 1.19028 0.76759 -0.29847 0.13608  -0.10271 333 LYS A CB  
2349 C  CG  . LYS A 351 ? 1.12816 1.14438 0.71090 -0.30971 0.12472  -0.08560 333 LYS A CG  
2350 C  CD  . LYS A 351 ? 1.22345 1.22840 0.78843 -0.30234 0.11760  -0.08503 333 LYS A CD  
2351 C  CE  . LYS A 351 ? 1.32445 1.27752 0.85181 -0.28293 0.09097  -0.06505 333 LYS A CE  
2352 N  NZ  . LYS A 351 ? 1.44277 1.33216 0.88755 -0.30530 0.08660  -0.05327 333 LYS A NZ  
2353 N  N   . LEU A 352 ? 0.99954 1.18927 0.79493 -0.27599 0.15000  -0.12895 334 LEU A N   
2354 C  CA  . LEU A 352 ? 0.92175 1.16890 0.78158 -0.26289 0.15741  -0.14829 334 LEU A CA  
2355 C  C   . LEU A 352 ? 0.86528 1.14469 0.74081 -0.28190 0.17221  -0.16318 334 LEU A C   
2356 O  O   . LEU A 352 ? 0.85656 1.18771 0.78253 -0.27422 0.17997  -0.18395 334 LEU A O   
2357 C  CB  . LEU A 352 ? 0.73076 0.98138 0.63126 -0.22738 0.13996  -0.13945 334 LEU A CB  
2358 C  CG  . LEU A 352 ? 0.86323 1.10547 0.77347 -0.20394 0.12838  -0.13427 334 LEU A CG  
2359 C  CD1 . LEU A 352 ? 0.71252 0.98231 0.63399 -0.20900 0.14073  -0.15290 334 LEU A CD1 
2360 C  CD2 . LEU A 352 ? 0.86843 1.06104 0.73377 -0.20173 0.11392  -0.11361 334 LEU A CD2 
2361 N  N   . GLY A 353 ? 0.94974 1.19973 0.78286 -0.30587 0.17560  -0.15435 335 GLY A N   
2362 C  CA  . GLY A 353 ? 0.95402 1.23362 0.79898 -0.32694 0.19005  -0.16871 335 GLY A CA  
2363 C  C   . GLY A 353 ? 1.04916 1.32491 0.91274 -0.31358 0.17905  -0.15861 335 GLY A C   
2364 O  O   . GLY A 353 ? 1.06364 1.37371 0.94932 -0.32605 0.18957  -0.17317 335 GLY A O   
2365 N  N   . ILE A 354 ? 0.96625 1.20404 0.82253 -0.28925 0.15860  -0.13588 336 ILE A N   
2366 C  CA  . ILE A 354 ? 1.00834 1.24043 0.88121 -0.27573 0.14762  -0.12574 336 ILE A CA  
2367 C  C   . ILE A 354 ? 0.99091 1.17876 0.80842 -0.30134 0.14937  -0.11342 336 ILE A C   
2368 O  O   . ILE A 354 ? 1.12452 1.26012 0.88566 -0.31041 0.14406  -0.09860 336 ILE A O   
2369 C  CB  . ILE A 354 ? 0.90055 1.11251 0.78896 -0.24044 0.12630  -0.10881 336 ILE A CB  
2370 C  CG1 . ILE A 354 ? 0.79456 1.04673 0.73563 -0.21630 0.12492  -0.12144 336 ILE A CG1 
2371 C  CG2 . ILE A 354 ? 0.90884 1.10850 0.80613 -0.22937 0.11528  -0.09702 336 ILE A CG2 
2372 C  CD1 . ILE A 354 ? 0.80170 1.03045 0.74418 -0.19055 0.10881  -0.10780 336 ILE A CD1 
2373 N  N   . GLU A 355 ? 0.92954 1.13591 0.76063 -0.31260 0.15581  -0.11997 337 GLU A N   
2374 C  CA  . GLU A 355 ? 1.02514 1.18833 0.80540 -0.33621 0.15709  -0.10852 337 GLU A CA  
2375 C  C   . GLU A 355 ? 1.05673 1.19837 0.84776 -0.31196 0.13854  -0.09121 337 GLU A C   
2376 O  O   . GLU A 355 ? 1.00691 1.18739 0.85231 -0.29210 0.13456  -0.09762 337 GLU A O   
2377 C  CB  . GLU A 355 ? 0.91428 1.11204 0.69763 -0.37036 0.17884  -0.12912 337 GLU A CB  
2378 N  N   . PHE A 356 ? 1.11455 1.19317 0.85213 -0.31302 0.12657  -0.07018 338 PHE A N   
2379 C  CA  . PHE A 356 ? 1.08976 1.14290 0.83178 -0.29014 0.10838  -0.05355 338 PHE A CA  
2380 C  C   . PHE A 356 ? 1.32841 1.35662 1.03911 -0.31242 0.11260  -0.04947 338 PHE A C   
2381 O  O   . PHE A 356 ? 1.44230 1.46144 1.11612 -0.34751 0.12847  -0.05669 338 PHE A O   
2382 C  CB  . PHE A 356 ? 1.14482 1.14698 0.85294 -0.27086 0.08931  -0.03478 338 PHE A CB  
2383 C  CG  . PHE A 356 ? 1.15235 1.17610 0.88757 -0.25067 0.08505  -0.03860 338 PHE A CG  
2384 C  CD1 . PHE A 356 ? 1.07430 1.09373 0.78333 -0.26555 0.09335  -0.04433 338 PHE A CD1 
2385 C  CD2 . PHE A 356 ? 1.19998 1.24619 0.98381 -0.21862 0.07336  -0.03680 338 PHE A CD2 
2386 C  CE1 . PHE A 356 ? 1.06080 1.09954 0.79392 -0.24779 0.08968  -0.04835 338 PHE A CE1 
2387 C  CE2 . PHE A 356 ? 1.11856 1.18219 0.92443 -0.20219 0.07021  -0.04086 338 PHE A CE2 
2388 C  CZ  . PHE A 356 ? 1.01227 1.07286 0.79381 -0.21624 0.07816  -0.04667 338 PHE A CZ  
2389 N  N   . ILE A 357 ? 1.28800 1.30428 1.01213 -0.29315 0.09890  -0.03845 339 ILE A N   
2390 C  CA  . ILE A 357 ? 1.29943 1.28966 0.99555 -0.31087 0.10079  -0.03345 339 ILE A CA  
2391 C  C   . ILE A 357 ? 1.40387 1.31601 1.02708 -0.31575 0.08910  -0.01417 339 ILE A C   
2392 O  O   . ILE A 357 ? 1.49397 1.36914 1.07535 -0.33583 0.09138  -0.00882 339 ILE A O   
2393 C  CB  . ILE A 357 ? 1.26453 1.27903 1.00867 -0.28865 0.09192  -0.03188 339 ILE A CB  
2394 C  CG1 . ILE A 357 ? 1.25989 1.26430 1.02495 -0.25059 0.07189  -0.01941 339 ILE A CG1 
2395 C  CG2 . ILE A 357 ? 1.26350 1.34927 1.06857 -0.29016 0.10417  -0.05292 339 ILE A CG2 
2396 N  N   . PRO A 366 ? 1.30701 1.38267 1.31779 -0.08026 -0.00511 0.00851  348 PRO A N   
2397 C  CA  . PRO A 366 ? 1.23679 1.34795 1.27922 -0.07532 -0.00035 -0.00271 348 PRO A CA  
2398 C  C   . PRO A 366 ? 1.32782 1.45456 1.39981 -0.06128 -0.00564 -0.00518 348 PRO A C   
2399 O  O   . PRO A 366 ? 1.49789 1.62361 1.57131 -0.06438 -0.00762 -0.00346 348 PRO A O   
2400 C  CB  . PRO A 366 ? 1.19840 1.30398 1.23832 -0.06593 -0.00222 -0.00179 348 PRO A CB  
2401 C  CG  . PRO A 366 ? 1.24326 1.31319 1.24932 -0.06735 -0.00794 0.00869  348 PRO A CG  
2402 C  CD  . PRO A 366 ? 1.19434 1.24675 1.19094 -0.06864 -0.01277 0.01550  348 PRO A CD  
2403 N  N   . SER A 367 ? 1.24792 1.38563 1.33969 -0.04669 -0.00820 -0.00915 349 SER A N   
2404 C  CA  . SER A 367 ? 1.26272 1.40778 1.37565 -0.03318 -0.01439 -0.01094 349 SER A CA  
2405 C  C   . SER A 367 ? 1.33544 1.45646 1.43864 -0.02874 -0.02136 -0.00035 349 SER A C   
2406 O  O   . SER A 367 ? 1.28913 1.41283 1.40061 -0.02601 -0.02523 -0.00023 349 SER A O   
2407 C  CB  . SER A 367 ? 0.93940 1.09010 1.06606 -0.01962 -0.01610 -0.01576 349 SER A CB  
2408 N  N   . GLY A 368 ? 1.26413 1.36306 1.35009 -0.02752 -0.02353 0.00719  350 GLY A N   
2409 C  CA  . GLY A 368 ? 1.16853 1.24712 1.24568 -0.02354 -0.02956 0.01489  350 GLY A CA  
2410 C  C   . GLY A 368 ? 1.13060 1.19201 1.19488 -0.01818 -0.03304 0.01882  350 GLY A C   
2411 O  O   . GLY A 368 ? 1.09345 1.14122 1.13736 -0.02305 -0.03382 0.02204  350 GLY A O   
2412 N  N   A SER A 369 ? 0.99209 1.05315 1.06622 -0.00844 -0.03562 0.01752  351 SER A N   
2413 N  N   B SER A 369 ? 0.99275 1.05377 1.06685 -0.00845 -0.03563 0.01754  351 SER A N   
2414 C  CA  A SER A 369 ? 0.82831 0.88091 0.89597 -0.00271 -0.03870 0.01742  351 SER A CA  
2415 C  CA  B SER A 369 ? 0.82622 0.87885 0.89389 -0.00272 -0.03868 0.01742  351 SER A CA  
2416 C  C   A SER A 369 ? 0.76778 0.83044 0.84814 0.00227  -0.03615 0.01162  351 SER A C   
2417 C  C   B SER A 369 ? 0.76665 0.82944 0.84702 0.00221  -0.03610 0.01160  351 SER A C   
2418 O  O   A SER A 369 ? 0.80542 0.87230 0.89687 0.00438  -0.03475 0.00954  351 SER A O   
2419 O  O   B SER A 369 ? 0.80580 0.87304 0.89734 0.00428  -0.03464 0.00948  351 SER A O   
2420 C  CB  A SER A 369 ? 0.85254 0.89300 0.91656 0.00153  -0.04381 0.01984  351 SER A CB  
2421 C  CB  B SER A 369 ? 0.85217 0.89282 0.91641 0.00158  -0.04376 0.01976  351 SER A CB  
2422 O  OG  A SER A 369 ? 0.79023 0.83464 0.86640 0.00579  -0.04299 0.01635  351 SER A OG  
2423 O  OG  B SER A 369 ? 0.91865 0.94539 0.96739 -0.00237 -0.04687 0.02498  351 SER A OG  
2424 N  N   . THR A 370 ? 0.67940 0.74327 0.75536 0.00425  -0.03638 0.00872  352 THR A N   
2425 C  CA  . THR A 370 ? 0.63100 0.70357 0.71620 0.00689  -0.03305 0.00253  352 THR A CA  
2426 C  C   . THR A 370 ? 0.60767 0.67964 0.69149 0.01082  -0.03561 -0.00171 352 THR A C   
2427 O  O   . THR A 370 ? 0.54850 0.61603 0.62298 0.01338  -0.04105 -0.00096 352 THR A O   
2428 C  CB  . THR A 370 ? 0.54274 0.62431 0.62678 0.00362  -0.02901 -0.00013 352 THR A CB  
2429 O  OG1 . THR A 370 ? 0.53578 0.62329 0.62624 0.00637  -0.02634 -0.00645 352 THR A OG1 
2430 C  CG2 . THR A 370 ? 0.49470 0.56975 0.56087 0.00024  -0.03160 0.00283  352 THR A CG2 
2431 N  N   . ASP A 371 ? 0.56911 0.64513 0.66103 0.01131  -0.03208 -0.00755 353 ASP A N   
2432 C  CA  . ASP A 371 ? 0.51394 0.59527 0.60731 0.01274  -0.03273 -0.01493 353 ASP A CA  
2433 C  C   . ASP A 371 ? 0.61159 0.70100 0.70122 0.01440  -0.03435 -0.01874 353 ASP A C   
2434 O  O   . ASP A 371 ? 0.52595 0.62366 0.61772 0.01666  -0.03647 -0.02654 353 ASP A O   
2435 C  CB  . ASP A 371 ? 0.46995 0.55006 0.56828 0.00910  -0.02693 -0.02068 353 ASP A CB  
2436 C  CG  . ASP A 371 ? 0.52665 0.60507 0.62575 0.00794  -0.02250 -0.02154 353 ASP A CG  
2437 O  OD1 . ASP A 371 ? 0.46152 0.54405 0.56093 0.00954  -0.02298 -0.01845 353 ASP A OD1 
2438 O  OD2 . ASP A 371 ? 0.45721 0.52896 0.55481 0.00474  -0.01824 -0.02629 353 ASP A OD2 
2439 N  N   . PHE A 372 ? 0.41339 0.50213 0.49722 0.01269  -0.03337 -0.01485 354 PHE A N   
2440 C  CA  . PHE A 372 ? 0.57409 0.66629 0.64884 0.01368  -0.03613 -0.01725 354 PHE A CA  
2441 C  C   . PHE A 372 ? 0.50521 0.58963 0.56698 0.01925  -0.04606 -0.01554 354 PHE A C   
2442 O  O   . PHE A 372 ? 0.54963 0.63665 0.60396 0.02338  -0.05156 -0.02000 354 PHE A O   
2443 C  CB  . PHE A 372 ? 0.53068 0.62244 0.59878 0.00827  -0.03193 -0.01391 354 PHE A CB  
2444 C  CG  . PHE A 372 ? 0.50264 0.59481 0.55712 0.00753  -0.03420 -0.01598 354 PHE A CG  
2445 C  CD1 . PHE A 372 ? 0.46126 0.53954 0.49329 0.00563  -0.03946 -0.01026 354 PHE A CD1 
2446 C  CD2 . PHE A 372 ? 0.48904 0.59204 0.54940 0.00788  -0.03131 -0.02364 354 PHE A CD2 
2447 C  CE1 . PHE A 372 ? 0.55326 0.62736 0.56760 0.00473  -0.04263 -0.01169 354 PHE A CE1 
2448 C  CE2 . PHE A 372 ? 0.46458 0.56756 0.51100 0.00718  -0.03406 -0.02573 354 PHE A CE2 
2449 C  CZ  . PHE A 372 ? 0.53480 0.62276 0.55747 0.00591  -0.04012 -0.01951 354 PHE A CZ  
2450 N  N   . GLY A 373 ? 0.51713 0.59057 0.57451 0.02047  -0.04957 -0.00977 355 GLY A N   
2451 C  CA  . GLY A 373 ? 0.57367 0.63630 0.61751 0.02807  -0.06043 -0.00930 355 GLY A CA  
2452 C  C   . GLY A 373 ? 0.58449 0.66106 0.63927 0.03665  -0.06555 -0.02071 355 GLY A C   
2453 O  O   . GLY A 373 ? 0.59617 0.67020 0.64063 0.04580  -0.07620 -0.02488 355 GLY A O   
2454 N  N   . ASN A 374 ? 0.46696 0.55802 0.54109 0.03344  -0.05838 -0.02717 356 ASN A N   
2455 C  CA  . ASN A 374 ? 0.57073 0.68058 0.65726 0.03771  -0.06033 -0.04120 356 ASN A CA  
2456 C  C   . ASN A 374 ? 0.61279 0.73486 0.69933 0.03877  -0.06140 -0.04845 356 ASN A C   
2457 O  O   . ASN A 374 ? 0.55041 0.68638 0.64042 0.04671  -0.06916 -0.05983 356 ASN A O   
2458 C  CB  . ASN A 374 ? 0.56602 0.68408 0.66716 0.02943  -0.05014 -0.04628 356 ASN A CB  
2459 C  CG  . ASN A 374 ? 0.67171 0.77763 0.77185 0.02803  -0.04933 -0.03952 356 ASN A CG  
2460 O  OD1 . ASN A 374 ? 0.61538 0.70610 0.70787 0.02589  -0.04857 -0.02764 356 ASN A OD1 
2461 N  ND2 . ASN A 374 ? 0.53990 0.65476 0.64836 0.02835  -0.04904 -0.04859 356 ASN A ND2 
2462 N  N   . VAL A 375 ? 0.59856 0.71736 0.68201 0.03156  -0.05426 -0.04347 357 VAL A N   
2463 C  CA  . VAL A 375 ? 0.53552 0.66416 0.61690 0.03167  -0.05488 -0.04969 357 VAL A CA  
2464 C  C   . VAL A 375 ? 0.60329 0.72280 0.66562 0.04049  -0.06761 -0.04729 357 VAL A C   
2465 O  O   . VAL A 375 ? 0.56997 0.70096 0.63198 0.04774  -0.07570 -0.05720 357 VAL A O   
2466 C  CB  . VAL A 375 ? 0.56817 0.69375 0.64952 0.02265  -0.04443 -0.04530 357 VAL A CB  
2467 C  CG1 . VAL A 375 ? 0.50598 0.63811 0.58070 0.02253  -0.04568 -0.04986 357 VAL A CG1 
2468 C  CG2 . VAL A 375 ? 0.52557 0.65585 0.62052 0.01573  -0.03434 -0.04994 357 VAL A CG2 
2469 N  N   . SER A 376 ? 0.57097 0.66809 0.61468 0.03964  -0.07018 -0.03489 358 SER A N   
2470 C  CA  . SER A 376 ? 0.57707 0.65573 0.59339 0.04563  -0.08201 -0.03078 358 SER A CA  
2471 C  C   . SER A 376 ? 0.61225 0.68910 0.62385 0.06109  -0.09774 -0.03761 358 SER A C   
2472 O  O   . SER A 376 ? 0.64643 0.70638 0.63279 0.06927  -0.11079 -0.03654 358 SER A O   
2473 C  CB  . SER A 376 ? 0.54243 0.59549 0.53758 0.03810  -0.07971 -0.01709 358 SER A CB  
2474 O  OG  . SER A 376 ? 0.66459 0.70761 0.66052 0.04124  -0.08269 -0.01305 358 SER A OG  
2475 N  N   . PHE A 377 ? 0.55848 0.65103 0.59176 0.06559  -0.09741 -0.04549 359 PHE A N   
2476 C  CA  . PHE A 377 ? 0.70614 0.80414 0.74060 0.08176  -0.11217 -0.05623 359 PHE A CA  
2477 C  C   . PHE A 377 ? 0.59224 0.72082 0.64284 0.08812  -0.11640 -0.07399 359 PHE A C   
2478 O  O   . PHE A 377 ? 0.69547 0.83113 0.74541 0.10437  -0.13178 -0.08544 359 PHE A O   
2479 C  CB  . PHE A 377 ? 0.67882 0.78351 0.73022 0.08267  -0.10905 -0.05943 359 PHE A CB  
2480 C  CG  . PHE A 377 ? 0.80784 0.88270 0.83859 0.08909  -0.11777 -0.04965 359 PHE A CG  
2481 C  CD1 . PHE A 377 ? 0.81599 0.88962 0.84459 0.10605  -0.13253 -0.05885 359 PHE A CD1 
2482 C  CD2 . PHE A 377 ? 0.76807 0.81751 0.78235 0.07805  -0.11107 -0.03306 359 PHE A CD2 
2483 C  CE1 . PHE A 377 ? 0.79607 0.83816 0.80268 0.11193  -0.14078 -0.05003 359 PHE A CE1 
2484 C  CE2 . PHE A 377 ? 0.84747 0.86804 0.84069 0.08172  -0.11817 -0.02464 359 PHE A CE2 
2485 C  CZ  . PHE A 377 ? 0.91851 0.93283 0.90627 0.09863  -0.13308 -0.03236 359 PHE A CZ  
2486 N  N   . VAL A 378 ? 0.61061 0.75788 0.67565 0.07629  -0.10376 -0.07796 360 VAL A N   
2487 C  CA  . VAL A 378 ? 0.67196 0.84980 0.75232 0.07921  -0.10597 -0.09577 360 VAL A CA  
2488 C  C   . VAL A 378 ? 0.59960 0.77452 0.66714 0.07556  -0.10588 -0.09344 360 VAL A C   
2489 O  O   . VAL A 378 ? 0.67099 0.86603 0.74318 0.08219  -0.11367 -0.10736 360 VAL A O   
2490 C  CB  . VAL A 378 ? 0.60288 0.80784 0.71130 0.06702  -0.09080 -0.10727 360 VAL A CB  
2491 C  CG1 . VAL A 378 ? 0.55496 0.76583 0.67554 0.07031  -0.09124 -0.11247 360 VAL A CG1 
2492 C  CG2 . VAL A 378 ? 0.58685 0.77993 0.69423 0.05027  -0.07401 -0.09585 360 VAL A CG2 
2493 N  N   . VAL A 379 ? 0.71205 0.86560 0.76483 0.06510  -0.09730 -0.07826 361 VAL A N   
2494 C  CA  . VAL A 379 ? 0.66293 0.81172 0.70080 0.06094  -0.09679 -0.07589 361 VAL A CA  
2495 C  C   . VAL A 379 ? 0.70793 0.82237 0.71441 0.05901  -0.09983 -0.05935 361 VAL A C   
2496 O  O   . VAL A 379 ? 0.65025 0.75109 0.65560 0.05229  -0.09230 -0.04873 361 VAL A O   
2497 C  CB  . VAL A 379 ? 0.68771 0.85015 0.74140 0.04626  -0.07936 -0.07810 361 VAL A CB  
2498 C  CG1 . VAL A 379 ? 0.68635 0.84693 0.72589 0.04262  -0.07915 -0.07817 361 VAL A CG1 
2499 C  CG2 . VAL A 379 ? 0.66169 0.85272 0.74193 0.04371  -0.07381 -0.09388 361 VAL A CG2 
2500 N  N   . PRO A 380 ? 0.68934 0.78816 0.66784 0.06354  -0.11069 -0.05742 362 PRO A N   
2501 C  CA  . PRO A 380 ? 0.75350 0.81879 0.69828 0.05569  -0.10967 -0.04261 362 PRO A CA  
2502 C  C   . PRO A 380 ? 0.70347 0.77491 0.65823 0.03817  -0.09003 -0.03749 362 PRO A C   
2503 O  O   . PRO A 380 ? 0.70413 0.79599 0.67466 0.03298  -0.08155 -0.04453 362 PRO A O   
2504 C  CB  . PRO A 380 ? 0.66929 0.72081 0.58326 0.06183  -0.12338 -0.04468 362 PRO A CB  
2505 C  CG  . PRO A 380 ? 0.70134 0.77516 0.63108 0.07937  -0.13785 -0.06002 362 PRO A CG  
2506 C  CD  . PRO A 380 ? 0.67733 0.78788 0.65156 0.07556  -0.12504 -0.06982 362 PRO A CD  
2507 N  N   . GLY A 381 ? 0.63731 0.69156 0.58290 0.02953  -0.08327 -0.02656 363 GLY A N   
2508 C  CA  . GLY A 381 ? 0.73380 0.79659 0.69104 0.01526  -0.06625 -0.02388 363 GLY A CA  
2509 C  C   . GLY A 381 ? 0.68517 0.72589 0.61920 0.00406  -0.06177 -0.01356 363 GLY A C   
2510 O  O   . GLY A 381 ? 0.74020 0.75420 0.64686 0.00615  -0.07120 -0.00670 363 GLY A O   
2511 N  N   . ILE A 382 ? 0.62203 0.67427 0.56634 -0.00828 -0.04719 -0.01404 364 ILE A N   
2512 C  CA  . ILE A 382 ? 0.63808 0.67942 0.56896 -0.02169 -0.03934 -0.00787 364 ILE A CA  
2513 C  C   . ILE A 382 ? 0.65080 0.71597 0.61518 -0.02526 -0.02705 -0.01144 364 ILE A C   
2514 O  O   . ILE A 382 ? 0.60499 0.69052 0.59359 -0.02175 -0.02191 -0.01868 364 ILE A O   
2515 C  CB  . ILE A 382 ? 0.67891 0.70883 0.57925 -0.03576 -0.03440 -0.00742 364 ILE A CB  
2516 C  CG1 . ILE A 382 ? 0.66265 0.71468 0.57766 -0.03667 -0.02770 -0.01650 364 ILE A CG1 
2517 C  CG2 . ILE A 382 ? 0.87389 0.86747 0.72916 -0.03410 -0.04813 -0.00074 364 ILE A CG2 
2518 C  CD1 . ILE A 382 ? 0.76011 0.81502 0.66154 -0.05413 -0.01504 -0.01947 364 ILE A CD1 
2519 N  N   . HIS A 383 ? 0.63183 0.69219 0.59488 -0.03217 -0.02318 -0.00686 365 HIS A N   
2520 C  CA  . HIS A 383 ? 0.56405 0.64475 0.55717 -0.03298 -0.01486 -0.01018 365 HIS A CA  
2521 C  C   . HIS A 383 ? 0.60504 0.68823 0.58988 -0.04849 -0.00569 -0.01051 365 HIS A C   
2522 O  O   . HIS A 383 ? 0.74541 0.82634 0.73298 -0.05169 -0.00515 -0.00718 365 HIS A O   
2523 C  CB  . HIS A 383 ? 0.57380 0.65053 0.57993 -0.02303 -0.02147 -0.00610 365 HIS A CB  
2524 C  CG  . HIS A 383 ? 0.62647 0.71920 0.65955 -0.02181 -0.01584 -0.00876 365 HIS A CG  
2525 N  ND1 . HIS A 383 ? 0.63243 0.73131 0.66813 -0.03059 -0.00996 -0.00886 365 HIS A ND1 
2526 C  CD2 . HIS A 383 ? 0.59117 0.69280 0.64686 -0.01288 -0.01622 -0.01191 365 HIS A CD2 
2527 C  CE1 . HIS A 383 ? 0.61146 0.72346 0.67173 -0.02464 -0.00857 -0.01210 365 HIS A CE1 
2528 N  NE2 . HIS A 383 ? 0.65238 0.76306 0.72256 -0.01422 -0.01232 -0.01314 365 HIS A NE2 
2529 N  N   . PRO A 384 ? 0.60457 0.69390 0.57867 -0.05994 0.00239  -0.01583 366 PRO A N   
2530 C  CA  . PRO A 384 ? 0.67007 0.76427 0.63442 -0.07814 0.01277  -0.01870 366 PRO A CA  
2531 C  C   . PRO A 384 ? 0.67592 0.80082 0.67613 -0.07704 0.01999  -0.02714 366 PRO A C   
2532 O  O   . PRO A 384 ? 0.60256 0.74620 0.63228 -0.06438 0.01979  -0.03326 366 PRO A O   
2533 C  CB  . PRO A 384 ? 0.61307 0.71030 0.56067 -0.08954 0.02024  -0.02485 366 PRO A CB  
2534 C  CG  . PRO A 384 ? 0.65094 0.75903 0.61731 -0.07476 0.01663  -0.02888 366 PRO A CG  
2535 C  CD  . PRO A 384 ? 0.55881 0.65240 0.52858 -0.05862 0.00339  -0.02089 366 PRO A CD  
2536 N  N   . TYR A 385 ? 0.62302 0.75097 0.61794 -0.09055 0.02564  -0.02807 367 TYR A N   
2537 C  CA  . TYR A 385 ? 0.62918 0.78935 0.65623 -0.09098 0.03204  -0.03855 367 TYR A CA  
2538 C  C   . TYR A 385 ? 0.64291 0.82765 0.67039 -0.10832 0.04597  -0.05246 367 TYR A C   
2539 O  O   . TYR A 385 ? 0.80480 0.97466 0.79888 -0.12787 0.05222  -0.05085 367 TYR A O   
2540 C  CB  . TYR A 385 ? 0.57639 0.72948 0.60148 -0.09484 0.02929  -0.03298 367 TYR A CB  
2541 C  CG  . TYR A 385 ? 0.65186 0.78636 0.68158 -0.07770 0.01679  -0.02200 367 TYR A CG  
2542 C  CD1 . TYR A 385 ? 0.68477 0.78502 0.68550 -0.07624 0.00855  -0.00983 367 TYR A CD1 
2543 C  CD2 . TYR A 385 ? 0.63210 0.78243 0.69343 -0.06278 0.01279  -0.02505 367 TYR A CD2 
2544 C  CE1 . TYR A 385 ? 0.72136 0.80909 0.72857 -0.06131 -0.00177 -0.00257 367 TYR A CE1 
2545 C  CE2 . TYR A 385 ? 0.68862 0.82227 0.75220 -0.04995 0.00310  -0.01623 367 TYR A CE2 
2546 C  CZ  . TYR A 385 ? 0.80194 0.90705 0.84047 -0.04977 -0.00333 -0.00579 367 TYR A CZ  
2547 O  OH  . TYR A 385 ? 0.72470 0.81771 0.76785 -0.03772 -0.01186 0.00028  367 TYR A OH  
2548 N  N   . PHE A 386 ? 0.54200 0.76281 0.60507 -0.10119 0.05054  -0.06713 368 PHE A N   
2549 C  CA  . PHE A 386 ? 0.69632 0.94767 0.76601 -0.11585 0.06421  -0.08426 368 PHE A CA  
2550 C  C   . PHE A 386 ? 0.62716 0.91816 0.73269 -0.11343 0.06773  -0.10000 368 PHE A C   
2551 O  O   . PHE A 386 ? 0.58254 0.87849 0.71245 -0.09428 0.05808  -0.09890 368 PHE A O   
2552 C  CB  . PHE A 386 ? 0.51177 0.77193 0.58891 -0.10821 0.06658  -0.09164 368 PHE A CB  
2553 C  CG  . PHE A 386 ? 0.49928 0.76851 0.60821 -0.08255 0.05810  -0.09471 368 PHE A CG  
2554 C  CD1 . PHE A 386 ? 0.55239 0.79403 0.65591 -0.06761 0.04664  -0.08078 368 PHE A CD1 
2555 C  CD2 . PHE A 386 ? 0.51095 0.81505 0.65290 -0.07383 0.06149  -0.11294 368 PHE A CD2 
2556 C  CE1 . PHE A 386 ? 0.53777 0.78233 0.66401 -0.04743 0.04000  -0.08360 368 PHE A CE1 
2557 C  CE2 . PHE A 386 ? 0.51434 0.81844 0.67814 -0.05042 0.05264  -0.11518 368 PHE A CE2 
2558 C  CZ  . PHE A 386 ? 0.52223 0.79442 0.67600 -0.03873 0.04254  -0.09979 368 PHE A CZ  
2559 N  N   . HIS A 387 ? 0.67553 0.99512 0.78261 -0.13362 0.08154  -0.11597 369 HIS A N   
2560 C  CA  . HIS A 387 ? 0.59085 0.95582 0.73275 -0.13405 0.08615  -0.13565 369 HIS A CA  
2561 C  C   . HIS A 387 ? 0.62346 1.02528 0.79990 -0.11923 0.08807  -0.15574 369 HIS A C   
2562 O  O   . HIS A 387 ? 0.54294 0.94300 0.71046 -0.12244 0.09398  -0.15922 369 HIS A O   
2563 C  CB  . HIS A 387 ? 0.77778 1.15487 0.90086 -0.16710 0.10127  -0.14403 369 HIS A CB  
2564 C  CG  . HIS A 387 ? 0.72868 1.16422 0.88618 -0.17501 0.11220  -0.17245 369 HIS A CG  
2565 N  ND1 . HIS A 387 ? 0.93399 1.40310 1.10533 -0.18019 0.12342  -0.19297 369 HIS A ND1 
2566 C  CD2 . HIS A 387 ? 0.88426 1.35337 1.06550 -0.17939 0.11381  -0.18574 369 HIS A CD2 
2567 C  CE1 . HIS A 387 ? 0.82161 1.34454 1.02565 -0.18644 0.13131  -0.21883 369 HIS A CE1 
2568 N  NE2 . HIS A 387 ? 0.77266 1.29726 0.98347 -0.18617 0.12543  -0.21509 369 HIS A NE2 
2569 N  N   . ILE A 388 ? 0.46977 0.90315 0.68420 -0.10176 0.08183  -0.16937 370 ILE A N   
2570 C  CA  . ILE A 388 ? 0.45899 0.91972 0.70585 -0.08015 0.07848  -0.18707 370 ILE A CA  
2571 C  C   . ILE A 388 ? 0.56005 1.07898 0.84258 -0.08195 0.08465  -0.21671 370 ILE A C   
2572 O  O   . ILE A 388 ? 0.48925 1.03211 0.80324 -0.05815 0.07712  -0.23286 370 ILE A O   
2573 C  CB  . ILE A 388 ? 0.47280 0.90917 0.72979 -0.04924 0.06034  -0.17610 370 ILE A CB  
2574 C  CG1 . ILE A 388 ? 0.37259 0.81873 0.64725 -0.03929 0.05029  -0.17722 370 ILE A CG1 
2575 C  CG2 . ILE A 388 ? 0.49189 0.87753 0.71714 -0.04860 0.05534  -0.15043 370 ILE A CG2 
2576 C  CD1 . ILE A 388 ? 0.42906 0.85011 0.71039 -0.01050 0.03274  -0.16823 370 ILE A CD1 
2577 N  N   . GLY A 389 ? 0.47864 1.02083 0.75575 -0.10996 0.09807  -0.22583 371 GLY A N   
2578 C  CA  . GLY A 389 ? 0.66179 1.26623 0.97430 -0.11499 0.10614  -0.25783 371 GLY A CA  
2579 C  C   . GLY A 389 ? 0.64915 1.27813 0.98801 -0.10551 0.09683  -0.26566 371 GLY A C   
2580 O  O   . GLY A 389 ? 0.72455 1.40900 1.10205 -0.09856 0.09764  -0.29486 371 GLY A O   
2581 N  N   . SER A 390 ? 0.62403 1.21553 0.94385 -0.10473 0.08769  -0.24212 372 SER A N   
2582 C  CA  . SER A 390 ? 0.66712 1.27675 1.00957 -0.09373 0.07686  -0.24722 372 SER A CA  
2583 C  C   . SER A 390 ? 0.71649 1.29892 1.02908 -0.11724 0.08070  -0.22899 372 SER A C   
2584 O  O   . SER A 390 ? 0.66786 1.20293 0.94053 -0.13090 0.08450  -0.20589 372 SER A O   
2585 C  CB  . SER A 390 ? 0.59665 1.18332 0.95174 -0.05571 0.05473  -0.23734 372 SER A CB  
2586 O  OG  . SER A 390 ? 0.72835 1.32706 1.10007 -0.04564 0.04315  -0.24012 372 SER A OG  
2587 N  N   . ASN A 391 ? 0.70884 1.32181 1.04083 -0.12086 0.07873  -0.24086 373 ASN A N   
2588 C  CA  . ASN A 391 ? 0.65271 1.24066 0.95981 -0.13947 0.07992  -0.22502 373 ASN A CA  
2589 C  C   . ASN A 391 ? 0.64604 1.20709 0.95746 -0.11366 0.05987  -0.20827 373 ASN A C   
2590 O  O   . ASN A 391 ? 0.72612 1.26103 1.01624 -0.12534 0.05876  -0.19295 373 ASN A O   
2591 C  CB  . ASN A 391 ? 0.75568 1.39424 1.07731 -0.16597 0.09304  -0.24945 373 ASN A CB  
2592 C  CG  . ASN A 391 ? 0.82434 1.48552 1.13424 -0.19825 0.11571  -0.26568 373 ASN A CG  
2593 O  OD1 . ASN A 391 ? 0.86420 1.48295 1.13184 -0.21668 0.12473  -0.24853 373 ASN A OD1 
2594 N  ND2 . ASN A 391 ? 0.87219 1.57265 1.19906 -0.19824 0.11991  -0.29349 373 ASN A ND2 
2595 N  N   . ALA A 392 ? 0.51245 1.07618 0.84754 -0.07980 0.04424  -0.21107 374 ALA A N   
2596 C  CA  . ALA A 392 ? 0.53088 1.06649 0.86649 -0.05624 0.02548  -0.19593 374 ALA A CA  
2597 C  C   . ALA A 392 ? 0.60370 1.07778 0.90031 -0.06091 0.02390  -0.16442 374 ALA A C   
2598 O  O   . ALA A 392 ? 0.61336 1.06352 0.88617 -0.07184 0.03247  -0.15415 374 ALA A O   
2599 C  CB  . ALA A 392 ? 0.51470 1.05502 0.87362 -0.02082 0.00969  -0.20394 374 ALA A CB  
2600 N  N   . LEU A 393 ? 0.58856 1.03863 0.87906 -0.05205 0.01228  -0.15052 375 LEU A N   
2601 C  CA  . LEU A 393 ? 0.75100 1.14738 1.00845 -0.05467 0.00956  -0.12347 375 LEU A CA  
2602 C  C   . LEU A 393 ? 0.69082 1.05749 0.94673 -0.02892 -0.00265 -0.11253 375 LEU A C   
2603 O  O   . LEU A 393 ? 0.63330 1.01232 0.91021 -0.00673 -0.01346 -0.12221 375 LEU A O   
2604 C  CB  . LEU A 393 ? 0.77626 1.16168 1.02586 -0.06121 0.00502  -0.11495 375 LEU A CB  
2605 C  CG  . LEU A 393 ? 0.65801 1.05640 0.89600 -0.09174 0.01796  -0.11966 375 LEU A CG  
2606 C  CD1 . LEU A 393 ? 0.80753 1.18603 1.01512 -0.11373 0.03192  -0.11299 375 LEU A CD1 
2607 C  CD2 . LEU A 393 ? 0.86468 1.32199 1.13496 -0.09787 0.02224  -0.14708 375 LEU A CD2 
2608 N  N   . ASN A 394 ? 0.63965 0.96584 0.86850 -0.03232 -0.00126 -0.09333 376 ASN A N   
2609 C  CA  . ASN A 394 ? 0.61941 0.91574 0.84327 -0.01248 -0.01086 -0.08284 376 ASN A CA  
2610 C  C   . ASN A 394 ? 0.65981 0.94246 0.88724 0.00230  -0.02423 -0.07727 376 ASN A C   
2611 O  O   . ASN A 394 ? 0.72642 1.01001 0.95142 -0.00529 -0.02568 -0.07392 376 ASN A O   
2612 C  CB  . ASN A 394 ? 0.66261 0.92302 0.85829 -0.02052 -0.00701 -0.06536 376 ASN A CB  
2613 C  CG  . ASN A 394 ? 0.73951 1.00407 0.93075 -0.02506 0.00125  -0.06965 376 ASN A CG  
2614 O  OD1 . ASN A 394 ? 0.57797 0.86241 0.76776 -0.04125 0.01178  -0.07823 376 ASN A OD1 
2615 N  ND2 . ASN A 394 ? 0.64694 0.89213 0.83406 -0.01257 -0.00278 -0.06435 376 ASN A ND2 
2616 N  N   . HIS A 395 ? 0.64001 0.90734 0.87019 0.02256  -0.03389 -0.07660 377 HIS A N   
2617 C  CA  . HIS A 395 ? 0.61985 0.86643 0.84695 0.03716  -0.04724 -0.07067 377 HIS A CA  
2618 C  C   . HIS A 395 ? 0.70556 0.98130 0.95313 0.04447  -0.05531 -0.08438 377 HIS A C   
2619 O  O   . HIS A 395 ? 0.74887 1.01130 0.99168 0.04998  -0.06484 -0.07874 377 HIS A O   
2620 C  CB  . HIS A 395 ? 0.62952 0.84370 0.83442 0.02821  -0.04686 -0.05198 377 HIS A CB  
2621 C  CG  . HIS A 395 ? 0.84529 1.03129 1.03222 0.02592  -0.04258 -0.04070 377 HIS A CG  
2622 N  ND1 . HIS A 395 ? 0.84446 0.99816 1.01448 0.02762  -0.04630 -0.02785 377 HIS A ND1 
2623 C  CD2 . HIS A 395 ? 0.79603 0.98407 0.98015 0.02174  -0.03492 -0.04212 377 HIS A CD2 
2624 C  CE1 . HIS A 395 ? 0.82308 0.96285 0.98268 0.02491  -0.04132 -0.02293 377 HIS A CE1 
2625 N  NE2 . HIS A 395 ? 0.84696 1.00581 1.01406 0.02177  -0.03495 -0.03069 377 HIS A NE2 
2626 N  N   . THR A 396 ? 0.61986 0.93772 0.89094 0.04456  -0.05173 -0.10408 378 THR A N   
2627 C  CA  . THR A 396 ? 0.61694 0.96923 0.91272 0.05607  -0.06130 -0.12234 378 THR A CA  
2628 C  C   . THR A 396 ? 0.61004 0.97706 0.92307 0.07865  -0.06923 -0.13951 378 THR A C   
2629 O  O   . THR A 396 ? 0.59262 0.95346 0.90217 0.07930  -0.06276 -0.14012 378 THR A O   
2630 C  CB  . THR A 396 ? 0.52824 0.92646 0.84082 0.03539  -0.05017 -0.13614 378 THR A CB  
2631 O  OG1 . THR A 396 ? 0.55722 0.98712 0.88326 0.02772  -0.03819 -0.15163 378 THR A OG1 
2632 C  CG2 . THR A 396 ? 0.56314 0.94114 0.85277 0.01066  -0.04015 -0.11894 378 THR A CG2 
2633 N  N   . GLU A 397 ? 0.57190 0.95814 0.90293 0.09822  -0.08444 -0.15445 379 GLU A N   
2634 C  CA  . GLU A 397 ? 0.64375 1.04065 0.98979 0.12444  -0.09598 -0.17231 379 GLU A CA  
2635 C  C   . GLU A 397 ? 0.60119 1.04412 0.97136 0.11735  -0.08282 -0.19278 379 GLU A C   
2636 O  O   . GLU A 397 ? 0.51458 0.95271 0.88714 0.13190  -0.08511 -0.20043 379 GLU A O   
2637 C  CB  . GLU A 397 ? 0.71335 1.12826 1.07577 0.14667  -0.11598 -0.18734 379 GLU A CB  
2638 C  CG  . GLU A 397 ? 0.75412 1.11866 1.09414 0.17428  -0.13722 -0.17928 379 GLU A CG  
2639 C  CD  . GLU A 397 ? 0.88111 1.25868 1.23197 0.19531  -0.15867 -0.19182 379 GLU A CD  
2640 O  OE1 . GLU A 397 ? 0.79113 1.22783 1.17606 0.19385  -0.15825 -0.21387 379 GLU A OE1 
2641 O  OE2 . GLU A 397 ? 0.98436 1.31303 1.30822 0.21239  -0.17596 -0.18054 379 GLU A OE2 
2642 N  N   . GLN A 398 ? 0.54755 1.03415 0.93367 0.09377  -0.06842 -0.20276 380 GLN A N   
2643 C  CA  . GLN A 398 ? 0.51691 1.04925 0.92429 0.08348  -0.05414 -0.22395 380 GLN A CA  
2644 C  C   . GLN A 398 ? 0.55290 1.05897 0.93861 0.06901  -0.03939 -0.21020 380 GLN A C   
2645 O  O   . GLN A 398 ? 0.46751 0.99995 0.86649 0.06768  -0.03082 -0.22639 380 GLN A O   
2646 C  CB  . GLN A 398 ? 0.60796 1.19071 1.03282 0.05787  -0.04116 -0.23859 380 GLN A CB  
2647 C  CG  . GLN A 398 ? 0.46043 1.08908 0.91789 0.07308  -0.05444 -0.26285 380 GLN A CG  
2648 C  CD  . GLN A 398 ? 0.57582 1.25295 1.04681 0.05262  -0.03874 -0.28716 380 GLN A CD  
2649 O  OE1 . GLN A 398 ? 0.60726 1.30070 1.08060 0.04207  -0.02464 -0.29793 380 GLN A OE1 
2650 N  NE2 . GLN A 398 ? 0.63700 1.33596 1.11476 0.04635  -0.04098 -0.29665 380 GLN A NE2 
2651 N  N   . TYR A 399 ? 0.45486 0.91156 0.80833 0.05882  -0.03673 -0.18235 381 TYR A N   
2652 C  CA  . TYR A 399 ? 0.50719 0.93863 0.84052 0.04891  -0.02579 -0.17046 381 TYR A CA  
2653 C  C   . TYR A 399 ? 0.52214 0.93096 0.85339 0.07293  -0.03514 -0.17151 381 TYR A C   
2654 O  O   . TYR A 399 ? 0.44653 0.85676 0.77543 0.06915  -0.02625 -0.17508 381 TYR A O   
2655 C  CB  . TYR A 399 ? 0.43408 0.82294 0.73578 0.03317  -0.02164 -0.14342 381 TYR A CB  
2656 C  CG  . TYR A 399 ? 0.53595 0.91520 0.81956 0.01361  -0.00668 -0.13594 381 TYR A CG  
2657 C  CD1 . TYR A 399 ? 0.49686 0.90018 0.77836 -0.01183 0.00807  -0.14222 381 TYR A CD1 
2658 C  CD2 . TYR A 399 ? 0.50302 0.84773 0.76898 0.01962  -0.00755 -0.12337 381 TYR A CD2 
2659 C  CE1 . TYR A 399 ? 0.52118 0.91101 0.78105 -0.02911 0.02009  -0.13510 381 TYR A CE1 
2660 C  CE2 . TYR A 399 ? 0.57089 0.90707 0.81968 0.00337  0.00415  -0.11729 381 TYR A CE2 
2661 C  CZ  . TYR A 399 ? 0.69950 1.05651 0.94405 -0.02012 0.01719  -0.12260 381 TYR A CZ  
2662 O  OH  . TYR A 399 ? 0.54932 0.89268 0.77168 -0.03548 0.02712  -0.11600 381 TYR A OH  
2663 N  N   . THR A 400 ? 0.49380 0.87849 0.82230 0.09664  -0.05298 -0.16847 382 THR A N   
2664 C  CA  . THR A 400 ? 0.52055 0.88052 0.84364 0.11974  -0.06287 -0.17161 382 THR A CA  
2665 C  C   . THR A 400 ? 0.53719 0.93935 0.88763 0.12997  -0.06111 -0.19870 382 THR A C   
2666 O  O   . THR A 400 ? 0.43999 0.82960 0.78507 0.13659  -0.05876 -0.20163 382 THR A O   
2667 C  CB  . THR A 400 ? 0.56073 0.88904 0.87404 0.14325  -0.08365 -0.16727 382 THR A CB  
2668 O  OG1 . THR A 400 ? 0.46040 0.74890 0.74722 0.13248  -0.08374 -0.14289 382 THR A OG1 
2669 C  CG2 . THR A 400 ? 0.49139 0.78801 0.79324 0.16644  -0.09435 -0.17115 382 THR A CG2 
2670 N  N   . GLU A 401 ? 0.43872 0.89358 0.81951 0.13046  -0.06155 -0.22037 383 GLU A N   
2671 C  CA  . GLU A 401 ? 0.45476 0.95861 0.86592 0.13855  -0.05840 -0.25006 383 GLU A CA  
2672 C  C   . GLU A 401 ? 0.44145 0.95773 0.84897 0.11460  -0.03665 -0.25064 383 GLU A C   
2673 O  O   . GLU A 401 ? 0.37518 0.89727 0.78886 0.12409  -0.03455 -0.26298 383 GLU A O   
2674 C  CB  . GLU A 401 ? 0.33622 0.90028 0.78137 0.13744  -0.05993 -0.27407 383 GLU A CB  
2675 C  CG  . GLU A 401 ? 0.35637 0.91138 0.80509 0.16448  -0.08358 -0.27880 383 GLU A CG  
2676 C  CD  . GLU A 401 ? 0.54092 1.14010 1.00684 0.15505  -0.08174 -0.29710 383 GLU A CD  
2677 O  OE1 . GLU A 401 ? 0.44768 1.08706 0.92520 0.12942  -0.06226 -0.30939 383 GLU A OE1 
2678 O  OE2 . GLU A 401 ? 0.55754 1.14956 1.02279 0.17226  -0.09943 -0.29977 383 GLU A OE2 
2679 N  N   . ALA A 402 ? 0.37698 0.89467 0.77165 0.08358  -0.02097 -0.23753 384 ALA A N   
2680 C  CA  . ALA A 402 ? 0.38538 0.91104 0.77094 0.05918  -0.00113 -0.23716 384 ALA A CA  
2681 C  C   . ALA A 402 ? 0.42039 0.89878 0.78034 0.06414  -0.00136 -0.21971 384 ALA A C   
2682 O  O   . ALA A 402 ? 0.42451 0.91262 0.78590 0.06059  0.00786  -0.22885 384 ALA A O   
2683 C  CB  . ALA A 402 ? 0.37470 0.90115 0.74408 0.02665  0.01258  -0.22478 384 ALA A CB  
2684 N  N   . ALA A 403 ? 0.37370 0.80261 0.71037 0.07130  -0.01128 -0.19607 385 ALA A N   
2685 C  CA  . ALA A 403 ? 0.42231 0.80757 0.73398 0.07297  -0.01069 -0.17973 385 ALA A CA  
2686 C  C   . ALA A 403 ? 0.45744 0.84109 0.77684 0.09360  -0.01584 -0.19392 385 ALA A C   
2687 O  O   . ALA A 403 ? 0.43190 0.79972 0.73814 0.08858  -0.00870 -0.18976 385 ALA A O   
2688 C  CB  . ALA A 403 ? 0.31869 0.65678 0.60803 0.07859  -0.02126 -0.15686 385 ALA A CB  
2689 N  N   . GLY A 404 ? 0.47628 0.87500 0.81567 0.11768  -0.02911 -0.21143 386 GLY A N   
2690 C  CA  . GLY A 404 ? 0.47243 0.86650 0.81761 0.14037  -0.03634 -0.22649 386 GLY A CA  
2691 C  C   . GLY A 404 ? 0.43252 0.88174 0.80857 0.14181  -0.02871 -0.25588 386 GLY A C   
2692 O  O   . GLY A 404 ? 0.50146 0.94986 0.88424 0.16190  -0.03466 -0.27123 386 GLY A O   
2693 N  N   . SER A 405 ? 0.50938 1.00550 0.90259 0.11992  -0.01504 -0.26521 387 SER A N   
2694 C  CA  . SER A 405 ? 0.46651 1.02227 0.89142 0.11807  -0.00606 -0.29648 387 SER A CA  
2695 C  C   . SER A 405 ? 0.48466 1.04015 0.90148 0.10685  0.00867  -0.30005 387 SER A C   
2696 O  O   . SER A 405 ? 0.46714 0.98467 0.85423 0.09196  0.01587  -0.27741 387 SER A O   
2697 C  CB  . SER A 405 ? 0.49084 1.09262 0.93020 0.09198  0.00677  -0.30434 387 SER A CB  
2698 O  OG  . SER A 405 ? 0.56436 1.14492 0.97506 0.06013  0.02248  -0.28224 387 SER A OG  
2699 N  N   . GLN A 406 ? 0.39692 0.99820 0.84184 0.11459  0.01278  -0.33079 388 GLN A N   
2700 C  CA  . GLN A 406 ? 0.51927 1.12923 0.95924 0.10062  0.02910  -0.33802 388 GLN A CA  
2701 C  C   . GLN A 406 ? 0.54433 1.16935 0.97086 0.06067  0.05100  -0.33038 388 GLN A C   
2702 O  O   . GLN A 406 ? 0.51443 1.11995 0.91788 0.04419  0.06268  -0.32011 388 GLN A O   
2703 C  CB  . GLN A 406 ? 0.46485 1.10342 0.92214 0.11236  0.02589  -0.36689 388 GLN A CB  
2704 C  CG  . GLN A 406 ? 0.58072 1.22577 1.03286 0.10127  0.04062  -0.37575 388 GLN A CG  
2705 C  CD  . GLN A 406 ? 0.82858 1.43047 1.26311 0.11207  0.03960  -0.35973 388 GLN A CD  
2706 O  OE1 . GLN A 406 ? 0.86115 1.42373 1.28794 0.13867  0.02157  -0.35089 388 GLN A OE1 
2707 N  NE2 . GLN A 406 ? 0.71754 1.31298 1.13324 0.08763  0.05685  -0.35167 388 GLN A NE2 
2708 N  N   . GLU A 407 ? 0.47981 1.13532 0.91661 0.04443  0.05593  -0.33482 389 GLU A N   
2709 C  CA  . GLU A 407 ? 0.51070 1.17854 0.93083 0.00522  0.07678  -0.33002 389 GLU A CA  
2710 C  C   . GLU A 407 ? 0.60548 1.21400 0.98222 -0.00946 0.07766  -0.29359 389 GLU A C   
2711 O  O   . GLU A 407 ? 0.56719 1.16818 0.91883 -0.03740 0.09300  -0.28622 389 GLU A O   
2712 C  CB  . GLU A 407 ? 0.67267 1.36987 1.10155 -0.00891 0.07848  -0.34002 389 GLU A CB  
2713 C  CG  . GLU A 407 ? 0.76260 1.45336 1.16984 -0.04243 0.09163  -0.32328 389 GLU A CG  
2714 C  CD  . GLU A 407 ? 0.79272 1.50995 1.20676 -0.05559 0.09289  -0.33508 389 GLU A CD  
2715 O  OE1 . GLU A 407 ? 0.65230 1.37572 1.08568 -0.03288 0.07638  -0.33917 389 GLU A OE1 
2716 O  OE2 . GLU A 407 ? 0.84298 1.57251 1.23993 -0.08931 0.11034  -0.34073 389 GLU A OE2 
2717 N  N   . ALA A 408 ? 0.46218 1.02755 0.82805 0.00933  0.06095  -0.27182 390 ALA A N   
2718 C  CA  . ALA A 408 ? 0.50888 1.02239 0.83746 -0.00222 0.06067  -0.24019 390 ALA A CA  
2719 C  C   . ALA A 408 ? 0.43258 0.91797 0.74072 -0.00273 0.06440  -0.23180 390 ALA A C   
2720 O  O   . ALA A 408 ? 0.47656 0.92766 0.75404 -0.01662 0.06716  -0.21004 390 ALA A O   
2721 C  CB  . ALA A 408 ? 0.44055 0.91965 0.76471 0.01676  0.04301  -0.22217 390 ALA A CB  
2722 N  N   . GLN A 409 ? 0.46208 0.96135 0.78622 0.01281  0.06376  -0.24956 391 GLN A N   
2723 C  CA  . GLN A 409 ? 0.59984 1.07073 0.90483 0.01386  0.06610  -0.24193 391 GLN A CA  
2724 C  C   . GLN A 409 ? 0.57735 1.05315 0.86118 -0.01572 0.08327  -0.23958 391 GLN A C   
2725 O  O   . GLN A 409 ? 0.47922 0.92086 0.73565 -0.02224 0.08406  -0.22238 391 GLN A O   
2726 C  CB  . GLN A 409 ? 0.48574 0.96991 0.81174 0.03728  0.06152  -0.26338 391 GLN A CB  
2727 C  CG  . GLN A 409 ? 0.44262 0.89676 0.77198 0.06768  0.04208  -0.25847 391 GLN A CG  
2728 C  CD  . GLN A 409 ? 0.56318 0.96254 0.86145 0.06649  0.03612  -0.23000 391 GLN A CD  
2729 O  OE1 . GLN A 409 ? 0.60115 0.97870 0.89250 0.07085  0.02650  -0.21475 391 GLN A OE1 
2730 N  NE2 . GLN A 409 ? 0.42591 0.80504 0.70589 0.05984  0.04218  -0.22418 391 GLN A NE2 
2731 N  N   . PHE A 410 ? 0.51471 1.03228 0.80895 -0.03465 0.09696  -0.25768 392 PHE A N   
2732 C  CA  . PHE A 410 ? 0.56692 1.08531 0.83508 -0.06506 0.11366  -0.25610 392 PHE A CA  
2733 C  C   . PHE A 410 ? 0.55009 1.02709 0.78024 -0.08183 0.11228  -0.22765 392 PHE A C   
2734 O  O   . PHE A 410 ? 0.56860 1.01633 0.76772 -0.09222 0.11509  -0.21418 392 PHE A O   
2735 C  CB  . PHE A 410 ? 0.59530 1.16645 0.88018 -0.08510 0.12958  -0.28226 392 PHE A CB  
2736 C  CG  . PHE A 410 ? 0.63853 1.20362 0.88781 -0.12201 0.14675  -0.27747 392 PHE A CG  
2737 C  CD1 . PHE A 410 ? 0.66428 1.22525 0.89530 -0.13391 0.15734  -0.28177 392 PHE A CD1 
2738 C  CD2 . PHE A 410 ? 0.50004 1.05954 0.73002 -0.14536 0.15187  -0.26856 392 PHE A CD2 
2739 C  CE1 . PHE A 410 ? 0.55696 1.10654 0.74893 -0.16825 0.17207  -0.27685 392 PHE A CE1 
2740 C  CE2 . PHE A 410 ? 0.64999 1.19579 0.83957 -0.17997 0.16676  -0.26356 392 PHE A CE2 
2741 C  CZ  . PHE A 410 ? 0.62080 1.16078 0.79027 -0.19135 0.17655  -0.26754 392 PHE A CZ  
2742 N  N   . TYR A 411 ? 0.61747 1.09147 0.84926 -0.08346 0.10689  -0.21919 393 TYR A N   
2743 C  CA  . TYR A 411 ? 0.58139 1.01577 0.77754 -0.09743 0.10442  -0.19373 393 TYR A CA  
2744 C  C   . TYR A 411 ? 0.59764 0.98825 0.77887 -0.08067 0.09120  -0.17216 393 TYR A C   
2745 O  O   . TYR A 411 ? 0.44659 0.80432 0.59426 -0.09171 0.09062  -0.15460 393 TYR A O   
2746 C  CB  . TYR A 411 ? 0.55145 0.99312 0.75557 -0.10046 0.10084  -0.19101 393 TYR A CB  
2747 C  CG  . TYR A 411 ? 0.67279 1.16121 0.89256 -0.11954 0.11454  -0.21408 393 TYR A CG  
2748 C  CD1 . TYR A 411 ? 0.65067 1.13618 0.83979 -0.15331 0.12917  -0.21317 393 TYR A CD1 
2749 C  CD2 . TYR A 411 ? 0.61533 1.15014 0.87868 -0.10416 0.11246  -0.23813 393 TYR A CD2 
2750 C  CE1 . TYR A 411 ? 0.72454 1.25486 0.92695 -0.17460 0.14382  -0.23634 393 TYR A CE1 
2751 C  CE2 . TYR A 411 ? 0.66859 1.25292 0.94991 -0.12225 0.12550  -0.26268 393 TYR A CE2 
2752 C  CZ  . TYR A 411 ? 0.63414 1.21740 0.88536 -0.15912 0.14237  -0.26203 393 TYR A CZ  
2753 O  OH  . TYR A 411 ? 0.69985 1.33422 0.96798 -0.18072 0.15735  -0.28840 393 TYR A OH  
2754 N  N   . THR A 412 ? 0.54393 0.93273 0.74774 -0.05442 0.08015  -0.17434 394 THR A N   
2755 C  CA  . THR A 412 ? 0.46113 0.81101 0.65146 -0.04097 0.06920  -0.15639 394 THR A CA  
2756 C  C   . THR A 412 ? 0.51165 0.84907 0.68361 -0.04673 0.07425  -0.15502 394 THR A C   
2757 O  O   . THR A 412 ? 0.45704 0.76463 0.60365 -0.05140 0.07066  -0.13840 394 THR A O   
2758 C  CB  . THR A 412 ? 0.45523 0.80274 0.66861 -0.01442 0.05750  -0.16075 394 THR A CB  
2759 O  OG1 . THR A 412 ? 0.48257 0.84449 0.71312 -0.00891 0.05219  -0.16385 394 THR A OG1 
2760 C  CG2 . THR A 412 ? 0.33938 0.64666 0.53695 -0.00448 0.04775  -0.14283 394 THR A CG2 
2761 N  N   . LEU A 413 ? 0.45322 0.81477 0.63833 -0.04571 0.08201  -0.17383 395 LEU A N   
2762 C  CA  . LEU A 413 ? 0.58539 0.93665 0.75301 -0.05192 0.08727  -0.17386 395 LEU A CA  
2763 C  C   . LEU A 413 ? 0.56135 0.90442 0.69648 -0.07765 0.09573  -0.16612 395 LEU A C   
2764 O  O   . LEU A 413 ? 0.57049 0.88972 0.68079 -0.08201 0.09418  -0.15601 395 LEU A O   
2765 C  CB  . LEU A 413 ? 0.40976 0.78997 0.59884 -0.04549 0.09430  -0.19749 395 LEU A CB  
2766 C  CG  . LEU A 413 ? 0.54678 0.92529 0.76065 -0.01758 0.08340  -0.20463 395 LEU A CG  
2767 C  CD1 . LEU A 413 ? 0.52213 0.92756 0.75622 -0.00889 0.08897  -0.22949 395 LEU A CD1 
2768 C  CD2 . LEU A 413 ? 0.47835 0.81547 0.67624 -0.00709 0.07311  -0.18704 395 LEU A CD2 
2769 N  N   . ARG A 414 ? 0.53916 0.89923 0.67122 -0.09514 0.10390  -0.17088 396 ARG A N   
2770 C  CA  . ARG A 414 ? 0.56458 0.90937 0.65807 -0.12135 0.11162  -0.16306 396 ARG A CA  
2771 C  C   . ARG A 414 ? 0.58731 0.88869 0.65108 -0.11973 0.09957  -0.13824 396 ARG A C   
2772 O  O   . ARG A 414 ? 0.60365 0.87963 0.63378 -0.12869 0.09865  -0.12892 396 ARG A O   
2773 C  CB  . ARG A 414 ? 0.52991 0.89965 0.62486 -0.14196 0.12323  -0.17391 396 ARG A CB  
2774 C  CG  . ARG A 414 ? 0.68475 1.03270 0.73272 -0.17210 0.13202  -0.16625 396 ARG A CG  
2775 C  CD  . ARG A 414 ? 0.62956 1.00777 0.67961 -0.19685 0.14761  -0.18239 396 ARG A CD  
2776 N  NE  . ARG A 414 ? 0.75782 1.13113 0.81083 -0.19773 0.14242  -0.17440 396 ARG A NE  
2777 C  CZ  . ARG A 414 ? 0.82431 1.22637 0.88558 -0.21626 0.15366  -0.18832 396 ARG A CZ  
2778 N  NH1 . ARG A 414 ? 0.68268 1.12306 0.75115 -0.23636 0.17152  -0.21223 396 ARG A NH1 
2779 N  NH2 . ARG A 414 ? 0.71224 1.10649 0.77511 -0.21561 0.14748  -0.17956 396 ARG A NH2 
2780 N  N   . THR A 415 ? 0.54748 0.84038 0.62312 -0.10732 0.08935  -0.12846 397 THR A N   
2781 C  CA  . THR A 415 ? 0.51104 0.76637 0.56220 -0.10398 0.07758  -0.10741 397 THR A CA  
2782 C  C   . THR A 415 ? 0.56806 0.80670 0.61827 -0.08848 0.06867  -0.10122 397 THR A C   
2783 O  O   . THR A 415 ? 0.64457 0.85567 0.66790 -0.08975 0.06130  -0.08835 397 THR A O   
2784 C  CB  . THR A 415 ? 0.61153 0.86491 0.67724 -0.09551 0.07020  -0.10055 397 THR A CB  
2785 O  OG1 . THR A 415 ? 0.50116 0.76622 0.56074 -0.11393 0.07862  -0.10507 397 THR A OG1 
2786 C  CG2 . THR A 415 ? 0.46369 0.68165 0.50973 -0.08845 0.05738  -0.08130 397 THR A CG2 
2787 N  N   . ALA A 416 ? 0.51421 0.76856 0.59188 -0.07392 0.06879  -0.11149 398 ALA A N   
2788 C  CA  . ALA A 416 ? 0.59474 0.83488 0.66924 -0.06349 0.06304  -0.10831 398 ALA A CA  
2789 C  C   . ALA A 416 ? 0.64900 0.88356 0.69741 -0.07643 0.06808  -0.10970 398 ALA A C   
2790 O  O   . ALA A 416 ? 0.53564 0.75090 0.56732 -0.07355 0.06087  -0.10152 398 ALA A O   
2791 C  CB  . ALA A 416 ? 0.47292 0.72656 0.57630 -0.04761 0.06327  -0.12030 398 ALA A CB  
2792 N  N   . LYS A 417 ? 0.54525 0.79806 0.58966 -0.09127 0.08044  -0.12142 399 LYS A N   
2793 C  CA  . LYS A 417 ? 0.53207 0.77660 0.54562 -0.10676 0.08587  -0.12225 399 LYS A CA  
2794 C  C   . LYS A 417 ? 0.59291 0.80467 0.56676 -0.11596 0.07812  -0.10536 399 LYS A C   
2795 O  O   . LYS A 417 ? 0.63306 0.82539 0.58077 -0.11749 0.07268  -0.09973 399 LYS A O   
2796 C  CB  . LYS A 417 ? 0.56753 0.83819 0.58216 -0.12447 0.10216  -0.13874 399 LYS A CB  
2797 C  CG  . LYS A 417 ? 0.57207 0.87328 0.61810 -0.11609 0.10985  -0.15859 399 LYS A CG  
2798 C  CD  . LYS A 417 ? 0.66825 1.00314 0.72284 -0.13278 0.12593  -0.17764 399 LYS A CD  
2799 C  CE  . LYS A 417 ? 0.58662 0.95393 0.67301 -0.12293 0.13307  -0.20025 399 LYS A CE  
2800 N  NZ  . LYS A 417 ? 0.56455 0.97101 0.66211 -0.13985 0.14953  -0.22241 399 LYS A NZ  
2801 N  N   . ALA A 418 ? 0.54874 0.75277 0.51633 -0.12118 0.07640  -0.09787 400 ALA A N   
2802 C  CA  . ALA A 418 ? 0.64406 0.81224 0.57089 -0.12838 0.06771  -0.08221 400 ALA A CA  
2803 C  C   . ALA A 418 ? 0.67151 0.81991 0.59760 -0.10929 0.05104  -0.07084 400 ALA A C   
2804 O  O   . ALA A 418 ? 0.65848 0.78021 0.55073 -0.11050 0.04195  -0.06265 400 ALA A O   
2805 C  CB  . ALA A 418 ? 0.64226 0.80645 0.56432 -0.13778 0.06991  -0.07778 400 ALA A CB  
2806 N  N   . LEU A 419 ? 0.60705 0.76811 0.56872 -0.09178 0.04649  -0.07152 401 LEU A N   
2807 C  CA  . LEU A 419 ? 0.62950 0.77735 0.59373 -0.07579 0.03294  -0.06408 401 LEU A CA  
2808 C  C   . LEU A 419 ? 0.59488 0.74245 0.55138 -0.07344 0.03099  -0.06868 401 LEU A C   
2809 O  O   . LEU A 419 ? 0.65050 0.78105 0.58772 -0.06854 0.01950  -0.06262 401 LEU A O   
2810 C  CB  . LEU A 419 ? 0.58165 0.74235 0.58238 -0.06119 0.03116  -0.06580 401 LEU A CB  
2811 C  CG  . LEU A 419 ? 0.57800 0.73251 0.58472 -0.05803 0.02673  -0.05778 401 LEU A CG  
2812 C  CD1 . LEU A 419 ? 0.54825 0.70917 0.58418 -0.04308 0.02292  -0.05871 401 LEU A CD1 
2813 C  CD2 . LEU A 419 ? 0.58134 0.70928 0.55841 -0.05926 0.01617  -0.04573 401 LEU A CD2 
2814 N  N   . ALA A 420 ? 0.61775 0.78520 0.58966 -0.07602 0.04145  -0.08080 402 ALA A N   
2815 C  CA  . ALA A 420 ? 0.60892 0.77775 0.57598 -0.07401 0.04048  -0.08640 402 ALA A CA  
2816 C  C   . ALA A 420 ? 0.69091 0.84206 0.61728 -0.08529 0.03733  -0.08256 402 ALA A C   
2817 O  O   . ALA A 420 ? 0.58296 0.72466 0.49637 -0.07970 0.02753  -0.08080 402 ALA A O   
2818 C  CB  . ALA A 420 ? 0.56610 0.75750 0.55553 -0.07485 0.05277  -0.10093 402 ALA A CB  
2819 N  N   . MET A 421 ? 0.65203 0.79785 0.55574 -0.10199 0.04529  -0.08220 403 MET A N   
2820 C  CA  . MET A 421 ? 0.79371 0.91453 0.65012 -0.11435 0.04162  -0.07724 403 MET A CA  
2821 C  C   . MET A 421 ? 0.77080 0.86082 0.60161 -0.10550 0.02325  -0.06349 403 MET A C   
2822 O  O   . MET A 421 ? 0.79107 0.86059 0.59000 -0.10413 0.01233  -0.06008 403 MET A O   
2823 C  CB  . MET A 421 ? 0.70375 0.82228 0.53750 -0.13743 0.05545  -0.08009 403 MET A CB  
2824 C  CG  . MET A 421 ? 0.79558 0.94822 0.65438 -0.14640 0.07376  -0.09701 403 MET A CG  
2825 S  SD  . MET A 421 ? 0.90481 1.06105 0.73948 -0.17654 0.09185  -0.10379 403 MET A SD  
2826 C  CE  . MET A 421 ? 0.82814 1.02954 0.69760 -0.18068 0.11021  -0.12749 403 MET A CE  
2827 N  N   . THR A 422 ? 0.67114 0.75761 0.51511 -0.09827 0.01863  -0.05652 404 THR A N   
2828 C  CA  . THR A 422 ? 0.73563 0.79506 0.55941 -0.08722 0.00065  -0.04535 404 THR A CA  
2829 C  C   . THR A 422 ? 0.76903 0.83667 0.60919 -0.06880 -0.01175 -0.04828 404 THR A C   
2830 O  O   . THR A 422 ? 0.78235 0.82963 0.59681 -0.06064 -0.02787 -0.04404 404 THR A O   
2831 C  CB  . THR A 422 ? 0.71741 0.77526 0.55626 -0.08374 0.00011  -0.03906 404 THR A CB  
2832 O  OG1 . THR A 422 ? 0.79540 0.85025 0.62089 -0.10298 0.01295  -0.03888 404 THR A OG1 
2833 C  CG2 . THR A 422 ? 0.76623 0.79444 0.58192 -0.07237 -0.01841 -0.02857 404 THR A CG2 
2834 N  N   . ALA A 423 ? 0.65533 0.75205 0.53653 -0.06225 -0.00487 -0.05683 405 ALA A N   
2835 C  CA  . ALA A 423 ? 0.68638 0.79355 0.58221 -0.04934 -0.01355 -0.06229 405 ALA A CA  
2836 C  C   . ALA A 423 ? 0.75660 0.85926 0.62746 -0.05329 -0.01711 -0.06694 405 ALA A C   
2837 O  O   . ALA A 423 ? 0.71875 0.81873 0.58238 -0.04308 -0.03117 -0.06865 405 ALA A O   
2838 C  CB  . ALA A 423 ? 0.62087 0.75353 0.55814 -0.04528 -0.00363 -0.07060 405 ALA A CB  
2839 N  N   . LEU A 424 ? 0.65718 0.76081 0.51489 -0.06814 -0.00473 -0.07049 406 LEU A N   
2840 C  CA  . LEU A 424 ? 0.73154 0.82845 0.56139 -0.07369 -0.00759 -0.07457 406 LEU A CA  
2841 C  C   . LEU A 424 ? 0.79978 0.86222 0.58175 -0.07270 -0.02428 -0.06522 406 LEU A C   
2842 O  O   . LEU A 424 ? 0.74949 0.80500 0.51232 -0.06677 -0.03681 -0.06768 406 LEU A O   
2843 C  CB  . LEU A 424 ? 0.70349 0.80870 0.52819 -0.09144 0.01060  -0.08125 406 LEU A CB  
2844 C  CG  . LEU A 424 ? 0.69008 0.82647 0.55654 -0.08980 0.02440  -0.09341 406 LEU A CG  
2845 C  CD1 . LEU A 424 ? 0.72246 0.86906 0.58472 -0.10628 0.04196  -0.10190 406 LEU A CD1 
2846 C  CD2 . LEU A 424 ? 0.60107 0.74748 0.47837 -0.08078 0.01845  -0.10063 406 LEU A CD2 
2847 N  N   . ASP A 425 ? 0.80988 0.84851 0.57015 -0.07777 -0.02583 -0.05501 407 ASP A N   
2848 C  CA  . ASP A 425 ? 0.86450 0.86257 0.57471 -0.07491 -0.04373 -0.04532 407 ASP A CA  
2849 C  C   . ASP A 425 ? 0.95512 0.95390 0.67416 -0.05108 -0.06540 -0.04608 407 ASP A C   
2850 O  O   . ASP A 425 ? 0.86870 0.84847 0.55536 -0.04359 -0.08240 -0.04617 407 ASP A O   
2851 C  CB  . ASP A 425 ? 0.88499 0.85792 0.57496 -0.08393 -0.04091 -0.03489 407 ASP A CB  
2852 C  CG  . ASP A 425 ? 1.00026 0.96032 0.65895 -0.11072 -0.02417 -0.03438 407 ASP A CG  
2853 O  OD1 . ASP A 425 ? 0.94359 0.89660 0.57503 -0.12121 -0.02142 -0.03828 407 ASP A OD1 
2854 O  OD2 . ASP A 425 ? 1.00739 0.96560 0.66831 -0.12243 -0.01334 -0.03121 407 ASP A OD2 
2855 N  N   . VAL A 426 ? 0.79692 0.81858 0.55931 -0.03896 -0.06540 -0.04808 408 VAL A N   
2856 C  CA  . VAL A 426 ? 0.84207 0.87047 0.61735 -0.01770 -0.08405 -0.05181 408 VAL A CA  
2857 C  C   . VAL A 426 ? 0.80196 0.85188 0.58659 -0.01216 -0.08891 -0.06389 408 VAL A C   
2858 O  O   . VAL A 426 ? 0.89463 0.94143 0.66844 0.00298  -0.10865 -0.06820 408 VAL A O   
2859 C  CB  . VAL A 426 ? 0.86365 0.91484 0.68423 -0.01011 -0.07909 -0.05314 408 VAL A CB  
2860 C  CG1 . VAL A 426 ? 0.76410 0.82731 0.60028 0.00982  -0.09640 -0.06003 408 VAL A CG1 
2861 C  CG2 . VAL A 426 ? 0.77192 0.80212 0.58219 -0.01568 -0.07516 -0.04167 408 VAL A CG2 
2862 N  N   . ILE A 427 ? 0.77300 0.84525 0.57715 -0.02380 -0.07173 -0.07082 409 ILE A N   
2863 C  CA  . ILE A 427 ? 0.75217 0.84703 0.56851 -0.02036 -0.07411 -0.08335 409 ILE A CA  
2864 C  C   . ILE A 427 ? 0.87882 0.95216 0.64983 -0.02064 -0.08757 -0.08318 409 ILE A C   
2865 O  O   . ILE A 427 ? 0.91415 0.99821 0.68536 -0.00922 -0.10211 -0.09212 409 ILE A O   
2866 C  CB  . ILE A 427 ? 0.73335 0.85212 0.57827 -0.03269 -0.05226 -0.09055 409 ILE A CB  
2867 C  CG1 . ILE A 427 ? 0.67979 0.81820 0.56780 -0.02875 -0.04333 -0.09257 409 ILE A CG1 
2868 C  CG2 . ILE A 427 ? 0.72396 0.85969 0.57151 -0.03339 -0.05321 -0.10284 409 ILE A CG2 
2869 C  CD1 . ILE A 427 ? 0.63034 0.78340 0.54120 -0.03900 -0.02324 -0.09780 409 ILE A CD1 
2870 N  N   . PHE A 428 ? 0.84453 0.88688 0.57417 -0.03426 -0.08341 -0.07399 410 PHE A N   
2871 C  CA  . PHE A 428 ? 0.92192 0.94061 0.60378 -0.03915 -0.09256 -0.07376 410 PHE A CA  
2872 C  C   . PHE A 428 ? 1.03850 1.00941 0.66514 -0.03308 -0.11311 -0.06263 410 PHE A C   
2873 O  O   . PHE A 428 ? 1.07481 1.01886 0.65424 -0.03535 -0.12437 -0.06156 410 PHE A O   
2874 C  CB  . PHE A 428 ? 0.91156 0.92930 0.58111 -0.06293 -0.07080 -0.07440 410 PHE A CB  
2875 C  CG  . PHE A 428 ? 0.88056 0.93796 0.59188 -0.06691 -0.05520 -0.08733 410 PHE A CG  
2876 C  CD1 . PHE A 428 ? 0.86541 0.93372 0.57233 -0.06453 -0.06110 -0.09705 410 PHE A CD1 
2877 C  CD2 . PHE A 428 ? 0.80495 0.88652 0.55796 -0.07217 -0.03589 -0.09029 410 PHE A CD2 
2878 C  CE1 . PHE A 428 ? 0.89012 0.99098 0.63229 -0.06892 -0.04664 -0.10916 410 PHE A CE1 
2879 C  CE2 . PHE A 428 ? 0.84148 0.95307 0.62809 -0.07467 -0.02292 -0.10221 410 PHE A CE2 
2880 C  CZ  . PHE A 428 ? 0.88429 1.00466 0.66494 -0.07377 -0.02767 -0.11148 410 PHE A CZ  
2881 N  N   . LYS A 429 ? 0.97507 0.93123 0.60288 -0.02511 -0.11927 -0.05446 411 LYS A N   
2882 C  CA  . LYS A 429 ? 1.08478 0.99050 0.65824 -0.01746 -0.14018 -0.04391 411 LYS A CA  
2883 C  C   . LYS A 429 ? 1.06753 0.98227 0.66199 0.01058  -0.16221 -0.04808 411 LYS A C   
2884 O  O   . LYS A 429 ? 1.18056 1.09979 0.79850 0.01592  -0.15988 -0.04439 411 LYS A O   
2885 C  CB  . LYS A 429 ? 1.06247 0.93724 0.61125 -0.03507 -0.12771 -0.03106 411 LYS A CB  
2886 C  CG  . LYS A 429 ? 1.09142 0.95345 0.61034 -0.06413 -0.10767 -0.02874 411 LYS A CG  
2887 C  CD  . LYS A 429 ? 1.23032 1.05396 0.71145 -0.08236 -0.09957 -0.01698 411 LYS A CD  
2888 C  CE  . LYS A 429 ? 1.30478 1.13703 0.78013 -0.11334 -0.07211 -0.01968 411 LYS A CE  
2889 N  NZ  . LYS A 429 ? 1.25512 1.06439 0.70905 -0.13294 -0.05979 -0.01187 411 LYS A NZ  
2890 N  N   . PRO A 430 ? 1.14805 1.06839 0.73621 0.02914  -0.18396 -0.05748 412 PRO A N   
2891 C  CA  . PRO A 430 ? 1.10707 1.04024 0.71662 0.05674  -0.20571 -0.06489 412 PRO A CA  
2892 C  C   . PRO A 430 ? 1.20696 1.09216 0.77783 0.06739  -0.22233 -0.05331 412 PRO A C   
2893 O  O   . PRO A 430 ? 1.10836 1.00729 0.70788 0.08395  -0.23006 -0.05688 412 PRO A O   
2894 C  CB  . PRO A 430 ? 0.99025 0.93362 0.58949 0.07232  -0.22696 -0.07792 412 PRO A CB  
2895 C  CG  . PRO A 430 ? 1.06929 1.02281 0.66387 0.05104  -0.20946 -0.07973 412 PRO A CG  
2896 C  CD  . PRO A 430 ? 1.08612 1.00609 0.65082 0.02596  -0.18943 -0.06399 412 PRO A CD  
2897 N  N   . GLU A 431 ? 1.25754 1.08453 0.76124 0.05694  -0.22741 -0.04000 413 GLU A N   
2898 C  CA  . GLU A 431 ? 1.31861 1.09237 0.77897 0.06321  -0.24086 -0.02767 413 GLU A CA  
2899 C  C   . GLU A 431 ? 1.24028 1.02622 0.73407 0.05238  -0.22058 -0.02124 413 GLU A C   
2900 O  O   . GLU A 431 ? 1.27794 1.04414 0.76626 0.06595  -0.23248 -0.01713 413 GLU A O   
2901 C  CB  . GLU A 431 ? 1.34199 1.04853 0.72002 0.04663  -0.24478 -0.01435 413 GLU A CB  
2902 C  CG  . GLU A 431 ? 1.29516 1.00911 0.65834 0.02864  -0.23410 -0.01764 413 GLU A CG  
2903 C  CD  . GLU A 431 ? 1.20249 0.93577 0.58441 -0.00460 -0.19840 -0.01421 413 GLU A CD  
2904 N  N   . LEU A 432 ? 1.13277 0.95100 0.66110 0.02934  -0.19109 -0.02126 414 LEU A N   
2905 C  CA  . LEU A 432 ? 1.14888 0.98319 0.71263 0.02054  -0.17278 -0.01682 414 LEU A CA  
2906 C  C   . LEU A 432 ? 1.08076 0.95885 0.70448 0.04084  -0.17713 -0.02676 414 LEU A C   
2907 O  O   . LEU A 432 ? 1.07125 0.94371 0.70578 0.04685  -0.17861 -0.02246 414 LEU A O   
2908 C  CB  . LEU A 432 ? 1.04897 0.90810 0.63453 -0.00624 -0.14264 -0.01683 414 LEU A CB  
2909 C  CG  . LEU A 432 ? 1.08309 0.96403 0.70890 -0.01510 -0.12341 -0.01415 414 LEU A CG  
2910 C  CD1 . LEU A 432 ? 1.04625 0.88409 0.63660 -0.01836 -0.12848 -0.00199 414 LEU A CD1 
2911 C  CD2 . LEU A 432 ? 1.06550 0.97034 0.70950 -0.03871 -0.09671 -0.01679 414 LEU A CD2 
2912 N  N   . LEU A 433 ? 1.08698 1.00827 0.74818 0.04986  -0.17853 -0.04086 415 LEU A N   
2913 C  CA  . LEU A 433 ? 0.92457 0.88985 0.64204 0.06471  -0.17962 -0.05240 415 LEU A CA  
2914 C  C   . LEU A 433 ? 0.93093 0.88045 0.63827 0.08946  -0.20455 -0.05451 415 LEU A C   
2915 O  O   . LEU A 433 ? 0.98927 0.95284 0.72670 0.09577  -0.20210 -0.05572 415 LEU A O   
2916 C  CB  . LEU A 433 ? 0.86697 0.87639 0.61719 0.06784  -0.17798 -0.06851 415 LEU A CB  
2917 C  CG  . LEU A 433 ? 0.86800 0.92719 0.67701 0.07610  -0.17349 -0.08282 415 LEU A CG  
2918 C  CD1 . LEU A 433 ? 0.81352 0.88275 0.65323 0.06422  -0.15239 -0.07644 415 LEU A CD1 
2919 C  CD2 . LEU A 433 ? 0.82207 0.91910 0.65574 0.07210  -0.16755 -0.09756 415 LEU A CD2 
2920 N  N   . GLU A 434 ? 1.05242 0.97122 0.71577 0.10465  -0.22971 -0.05568 416 GLU A N   
2921 C  CA  . GLU A 434 ? 1.01544 0.91363 0.66373 0.13074  -0.25597 -0.05830 416 GLU A CA  
2922 C  C   . GLU A 434 ? 1.07363 0.92581 0.69186 0.12484  -0.25373 -0.04186 416 GLU A C   
2923 O  O   . GLU A 434 ? 1.14551 0.99704 0.77622 0.14132  -0.26407 -0.04449 416 GLU A O   
2924 C  CB  . GLU A 434 ? 1.06446 0.93288 0.66511 0.14936  -0.28554 -0.06264 416 GLU A CB  
2925 N  N   . GLY A 435 ? 1.11675 0.93208 0.69596 0.10032  -0.23949 -0.02636 417 GLY A N   
2926 C  CA  . GLY A 435 ? 1.16862 0.94362 0.72097 0.09040  -0.23417 -0.01186 417 GLY A CA  
2927 C  C   . GLY A 435 ? 1.11009 0.92302 0.71887 0.08508  -0.21535 -0.01289 417 GLY A C   
2928 O  O   . GLY A 435 ? 1.11197 0.90551 0.71574 0.09133  -0.22030 -0.00776 417 GLY A O   
2929 N  N   . ILE A 436 ? 1.01862 0.88290 0.67881 0.07365  -0.19421 -0.01956 418 ILE A N   
2930 C  CA  . ILE A 436 ? 1.02084 0.92033 0.73335 0.07002  -0.17800 -0.02146 418 ILE A CA  
2931 C  C   . ILE A 436 ? 0.97063 0.89242 0.71382 0.09449  -0.19307 -0.03278 418 ILE A C   
2932 O  O   . ILE A 436 ? 0.99824 0.92241 0.75926 0.09729  -0.19011 -0.03060 418 ILE A O   
2933 C  CB  . ILE A 436 ? 0.92314 0.86695 0.67812 0.05447  -0.15473 -0.02705 418 ILE A CB  
2934 C  CG1 . ILE A 436 ? 0.89890 0.82550 0.62491 0.03177  -0.14075 -0.01961 418 ILE A CG1 
2935 C  CG2 . ILE A 436 ? 1.01963 0.99025 0.81929 0.04944  -0.13871 -0.02700 418 ILE A CG2 
2936 C  CD1 . ILE A 436 ? 0.91254 0.87725 0.66941 0.02259  -0.12556 -0.02843 418 ILE A CD1 
2937 N  N   . ARG A 437 ? 0.94732 0.88799 0.69763 0.11206  -0.20930 -0.04662 419 ARG A N   
2938 C  CA  . ARG A 437 ? 0.97174 0.94185 0.75551 0.13449  -0.22260 -0.06173 419 ARG A CA  
2939 C  C   . ARG A 437 ? 1.04881 0.97905 0.79945 0.15448  -0.24572 -0.05843 419 ARG A C   
2940 O  O   . ARG A 437 ? 1.00756 0.95482 0.78569 0.16709  -0.24981 -0.06592 419 ARG A O   
2941 C  CB  . ARG A 437 ? 0.84044 0.84678 0.64284 0.14641  -0.23295 -0.08021 419 ARG A CB  
2942 C  CG  . ARG A 437 ? 0.85754 0.90965 0.70255 0.12874  -0.20954 -0.08712 419 ARG A CG  
2943 C  CD  . ARG A 437 ? 0.85344 0.93496 0.70770 0.13559  -0.21811 -0.10357 419 ARG A CD  
2944 N  NE  . ARG A 437 ? 0.83130 0.95689 0.72876 0.11987  -0.19615 -0.11244 419 ARG A NE  
2945 C  CZ  . ARG A 437 ? 0.90549 1.05547 0.81119 0.11593  -0.19444 -0.12355 419 ARG A CZ  
2946 N  NH1 . ARG A 437 ? 0.82545 0.96335 0.70113 0.12671  -0.21350 -0.12746 419 ARG A NH1 
2947 N  NH2 . ARG A 437 ? 0.86596 1.05030 0.80790 0.10072  -0.17375 -0.13097 419 ARG A NH2 
2948 N  N   . GLU A 438 ? 1.05525 0.92964 0.74419 0.15694  -0.26080 -0.04764 420 GLU A N   
2949 C  CA  . GLU A 438 ? 1.08566 0.91150 0.73438 0.17498  -0.28306 -0.04276 420 GLU A CA  
2950 C  C   . GLU A 438 ? 1.13613 0.94478 0.78667 0.16178  -0.26826 -0.03016 420 GLU A C   
2951 O  O   . GLU A 438 ? 1.10010 0.90906 0.76318 0.17779  -0.27760 -0.03475 420 GLU A O   
2952 C  CB  . GLU A 438 ? 1.12709 0.88875 0.70083 0.17648  -0.30090 -0.03237 420 GLU A CB  
2953 N  N   . ASP A 439 ? 1.18193 0.97837 0.82170 0.13258  -0.24499 -0.01589 421 ASP A N   
2954 C  CA  . ASP A 439 ? 1.18174 0.96509 0.82422 0.11829  -0.23019 -0.00490 421 ASP A CA  
2955 C  C   . ASP A 439 ? 1.11093 0.94661 0.81816 0.12249  -0.21914 -0.01413 421 ASP A C   
2956 O  O   . ASP A 439 ? 1.23416 1.05936 0.94528 0.12439  -0.21834 -0.01023 421 ASP A O   
2957 C  CB  . ASP A 439 ? 1.16104 0.93402 0.78844 0.08615  -0.20626 0.00751  421 ASP A CB  
2958 C  CG  . ASP A 439 ? 1.24783 0.96423 0.80507 0.07651  -0.21406 0.01732  421 ASP A CG  
2959 O  OD1 . ASP A 439 ? 1.35225 1.02765 0.86582 0.09567  -0.23985 0.01726  421 ASP A OD1 
2960 O  OD2 . ASP A 439 ? 1.21311 0.92517 0.75724 0.04973  -0.19471 0.02415  421 ASP A OD2 
2961 N  N   . PHE A 440 ? 1.02736 0.91666 0.78239 0.12227  -0.20997 -0.02632 422 PHE A N   
2962 C  CA  . PHE A 440 ? 1.00799 0.94372 0.81944 0.12425  -0.19919 -0.03583 422 PHE A CA  
2963 C  C   . PHE A 440 ? 1.14782 1.09116 0.97047 0.15020  -0.21893 -0.04870 422 PHE A C   
2964 O  O   . PHE A 440 ? 1.01256 0.96832 0.86013 0.15189  -0.21374 -0.05076 422 PHE A O   
2965 C  CB  . PHE A 440 ? 0.88444 0.86898 0.73624 0.11644  -0.18544 -0.04641 422 PHE A CB  
2966 C  CG  . PHE A 440 ? 0.81905 0.84810 0.72310 0.11713  -0.17496 -0.05769 422 PHE A CG  
2967 C  CD1 . PHE A 440 ? 0.63386 0.66649 0.55596 0.10316  -0.15724 -0.04979 422 PHE A CD1 
2968 C  CD2 . PHE A 440 ? 0.71696 0.78426 0.65024 0.13048  -0.18268 -0.07731 422 PHE A CD2 
2969 C  CE1 . PHE A 440 ? 0.71225 0.78008 0.67600 0.10221  -0.14771 -0.05954 422 PHE A CE1 
2970 C  CE2 . PHE A 440 ? 0.75165 0.85734 0.72838 0.12745  -0.17133 -0.08841 422 PHE A CE2 
2971 C  CZ  . PHE A 440 ? 0.72580 0.82895 0.71551 0.11311  -0.15393 -0.07867 422 PHE A CZ  
2972 N  N   . LYS A 441 ? 1.07222 1.00889 0.87639 0.17129  -0.24236 -0.05869 423 LYS A N   
2973 C  CA  . LYS A 441 ? 1.02173 0.97026 0.83866 0.19897  -0.26323 -0.07484 423 LYS A CA  
2974 C  C   . LYS A 441 ? 1.09138 0.99159 0.87495 0.20814  -0.27473 -0.06509 423 LYS A C   
2975 O  O   . LYS A 441 ? 1.17173 1.08856 0.98069 0.22024  -0.27821 -0.07453 423 LYS A O   
2976 C  CB  . LYS A 441 ? 1.03086 0.98263 0.83335 0.22104  -0.28788 -0.08878 423 LYS A CB  
2977 N  N   . LEU A 442 ? 1.20056 1.03962 0.92529 0.20084  -0.27980 -0.04690 424 LEU A N   
2978 C  CA  . LEU A 442 ? 1.19074 0.97604 0.87544 0.20860  -0.29187 -0.03739 424 LEU A CA  
2979 C  C   . LEU A 442 ? 1.31598 1.11015 1.02537 0.19134  -0.27042 -0.02952 424 LEU A C   
2980 O  O   . LEU A 442 ? 1.36538 1.15211 1.07933 0.20441  -0.27827 -0.03319 424 LEU A O   
2981 C  CB  . LEU A 442 ? 1.32630 1.04110 0.93687 0.19988  -0.30003 -0.01996 424 LEU A CB  
2982 N  N   . LYS A 443 ? 1.27926 1.08959 1.00460 0.16297  -0.24410 -0.01969 425 LYS A N   
2983 C  CA  . LYS A 443 ? 1.23483 1.05625 0.98489 0.14720  -0.22460 -0.01316 425 LYS A CA  
2984 C  C   . LYS A 443 ? 1.16824 1.03877 0.97330 0.15904  -0.22244 -0.02858 425 LYS A C   
2985 O  O   . LYS A 443 ? 1.18328 1.05249 0.99988 0.15637  -0.21642 -0.02595 425 LYS A O   
2986 C  CB  . LYS A 443 ? 1.19189 1.02913 0.95436 0.11840  -0.19892 -0.00386 425 LYS A CB  
2987 C  CG  . LYS A 443 ? 1.19697 0.98539 0.90728 0.09896  -0.19414 0.01245  425 LYS A CG  
2988 N  N   . LEU A 444 ? 1.15416 1.06809 0.99186 0.17066  -0.22682 -0.04569 426 LEU A N   
2989 C  CA  . LEU A 444 ? 1.15444 1.11667 1.04251 0.17886  -0.22326 -0.06278 426 LEU A CA  
2990 C  C   . LEU A 444 ? 1.23526 1.18487 1.11688 0.20327  -0.24320 -0.07229 426 LEU A C   
2991 O  O   . LEU A 444 ? 1.26459 1.23884 1.17787 0.20446  -0.23664 -0.08040 426 LEU A O   
2992 C  CB  . LEU A 444 ? 1.07563 1.08682 0.99665 0.18311  -0.22282 -0.08067 426 LEU A CB  
2993 C  CG  . LEU A 444 ? 1.06299 1.11338 1.02210 0.16070  -0.19716 -0.08155 426 LEU A CG  
2994 C  CD1 . LEU A 444 ? 0.93910 1.03899 0.93179 0.16637  -0.19817 -0.10334 426 LEU A CD1 
2995 C  CD2 . LEU A 444 ? 0.86876 0.92817 0.85110 0.15005  -0.18174 -0.07828 426 LEU A CD2 
2996 N  N   . GLN A 445 ? 1.16412 1.07353 1.00295 0.22328  -0.26813 -0.07206 427 GLN A N   
2997 C  CA  . GLN A 445 ? 1.23080 1.12393 1.06025 0.24954  -0.28953 -0.08205 427 GLN A CA  
2998 C  C   . GLN A 445 ? 1.31957 1.16983 1.12460 0.24070  -0.28418 -0.06600 427 GLN A C   
2999 O  O   . GLN A 445 ? 1.32664 1.18586 1.14939 0.25185  -0.28760 -0.07502 427 GLN A O   
3000 C  CB  . GLN A 445 ? 1.25323 1.11090 1.04133 0.27262  -0.31611 -0.08704 427 GLN A CB  
3001 C  CG  . GLN A 445 ? 1.25079 1.13144 1.04347 0.27329  -0.31923 -0.09387 427 GLN A CG  
3002 N  N   . GLU A 446 ? 1.37112 1.17650 1.13583 0.21954  -0.27508 -0.04365 428 GLU A N   
3003 C  CA  . GLU A 446 ? 1.31799 1.08293 1.05773 0.20821  -0.26897 -0.02887 428 GLU A CA  
3004 C  C   . GLU A 446 ? 1.32830 1.13351 1.11644 0.19409  -0.24713 -0.03043 428 GLU A C   
3005 O  O   . GLU A 446 ? 1.51849 1.30162 1.29743 0.19257  -0.24610 -0.02525 428 GLU A O   
3006 C  CB  . GLU A 446 ? 1.31069 1.02839 1.00197 0.18384  -0.26012 -0.00749 428 GLU A CB  
3007 C  CG  . GLU A 446 ? 1.43662 1.12322 1.08415 0.18969  -0.27515 -0.00500 428 GLU A CG  
3008 C  CD  . GLU A 446 ? 1.49997 1.15664 1.11163 0.15937  -0.25940 0.01296  428 GLU A CD  
3009 O  OE1 . GLU A 446 ? 1.55327 1.19236 1.15507 0.13812  -0.24408 0.02478  428 GLU A OE1 
3010 O  OE2 . GLU A 446 ? 1.57986 1.23272 1.17380 0.15617  -0.26204 0.01383  428 GLU A OE2 
3011 N  N   . GLU A 447 ? 1.28489 1.14499 1.12072 0.18333  -0.23016 -0.03733 429 GLU A N   
3012 C  CA  . GLU A 447 ? 1.29012 1.18750 1.16977 0.17175  -0.21146 -0.04062 429 GLU A CA  
3013 C  C   . GLU A 447 ? 1.34030 1.27972 1.25898 0.18995  -0.21780 -0.06333 429 GLU A C   
3014 O  O   . GLU A 447 ? 1.37067 1.35322 1.33072 0.17937  -0.20145 -0.07094 429 GLU A O   
3015 C  CB  . GLU A 447 ? 1.15892 1.08587 1.06311 0.14840  -0.18905 -0.03508 429 GLU A CB  
3016 C  CG  . GLU A 447 ? 1.15988 1.05460 1.03017 0.13039  -0.18210 -0.01703 429 GLU A CG  
3017 C  CD  . GLU A 447 ? 1.21346 1.09061 1.07666 0.11123  -0.16796 -0.00285 429 GLU A CD  
3018 O  OE1 . GLU A 447 ? 1.11023 1.01344 1.00646 0.10554  -0.15637 -0.00547 429 GLU A OE1 
3019 O  OE2 . GLU A 447 ? 1.12476 0.96191 0.94776 0.10069  -0.16828 0.01014  429 GLU A OE2 
3020 N  N   . GLN A 448 ? 1.32498 1.25183 1.22951 0.21683  -0.24142 -0.07548 430 GLN A N   
3021 C  CA  . GLN A 448 ? 1.36381 1.33304 1.30507 0.23644  -0.24953 -0.10103 430 GLN A CA  
3022 C  C   . GLN A 448 ? 1.38485 1.41435 1.36983 0.23122  -0.23953 -0.11760 430 GLN A C   
3023 O  O   . GLN A 448 ? 1.35194 1.39513 1.33689 0.24553  -0.25324 -0.12961 430 GLN A O   
3024 C  CB  . GLN A 448 ? 1.19343 1.16988 1.15348 0.23140  -0.23946 -0.10293 430 GLN A CB  
3025 P  P   . PO4 B .   ? 1.36403 1.40911 1.46355 0.01251  -0.04101 0.01046  501 PO4 A P   
3026 O  O1  . PO4 B .   ? 1.03928 1.06825 1.13169 0.01260  -0.04410 0.01292  501 PO4 A O1  
3027 O  O2  . PO4 B .   ? 1.00616 1.06370 1.11502 0.01595  -0.04241 0.00737  501 PO4 A O2  
3028 O  O3  . PO4 B .   ? 1.09870 1.14809 1.19533 0.00803  -0.04062 0.01392  501 PO4 A O3  
3029 O  O4  . PO4 B .   ? 1.04321 1.08674 1.14108 0.01296  -0.03724 0.00602  501 PO4 A O4  
3030 P  P   . PO4 C .   ? 1.58604 1.95369 1.51172 -0.21023 0.20490  -0.28566 502 PO4 A P   
3031 O  O1  . PO4 C .   ? 1.41120 1.77601 1.37346 -0.18016 0.19132  -0.28065 502 PO4 A O1  
3032 O  O2  . PO4 C .   ? 1.43148 1.82331 1.36454 -0.21670 0.22008  -0.31019 502 PO4 A O2  
3033 O  O3  . PO4 C .   ? 1.39328 1.77735 1.32162 -0.22409 0.21388  -0.28893 502 PO4 A O3  
3034 O  O4  . PO4 C .   ? 1.42958 1.75847 1.30627 -0.22050 0.19401  -0.26450 502 PO4 A O4  
3035 ZN ZN  . ZN  D .   ? 0.43183 0.56739 0.58194 0.02021  -0.02910 -0.02435 503 ZN  A ZN  
3036 ZN ZN  . ZN  E .   ? 0.38266 0.52108 0.52461 0.01357  -0.01920 -0.02708 504 ZN  A ZN  
3037 O  O   . HOH F .   ? 0.73443 1.11189 0.89793 0.07782  -0.11621 -0.21311 601 HOH A O   
3038 O  O   . HOH F .   ? 0.76697 0.95786 0.79723 -0.08712 0.05933  -0.20182 602 HOH A O   
3039 O  O   . HOH F .   ? 0.70488 0.75448 0.74442 -0.09905 0.03070  -0.12769 603 HOH A O   
3040 O  O   . HOH F .   ? 0.65446 0.98116 0.73324 -0.14244 0.10382  -0.13822 604 HOH A O   
3041 O  O   . HOH F .   ? 0.91808 0.60082 0.64008 0.00136  -0.12220 0.06601  605 HOH A O   
3042 O  O   . HOH F .   ? 0.59097 0.93848 0.67489 -0.16550 0.11032  -0.14289 606 HOH A O   
3043 O  O   . HOH F .   ? 0.71874 0.76042 0.80747 0.02411  -0.05240 -0.06636 607 HOH A O   
3044 O  O   . HOH F .   ? 0.50119 0.77505 0.63460 -0.01505 -0.02104 -0.15844 608 HOH A O   
3045 O  O   . HOH F .   ? 0.50036 1.12451 0.88237 0.00326  0.09573  -0.33035 609 HOH A O   
3046 O  O   . HOH F .   ? 0.98736 0.88510 0.57329 -0.15697 -0.00505 -0.01708 610 HOH A O   
3047 O  O   . HOH F .   ? 0.48990 0.51910 0.58086 0.03026  -0.01788 -0.03989 611 HOH A O   
3048 O  O   . HOH F .   ? 0.60429 0.57357 0.67334 0.05730  -0.05657 -0.01966 612 HOH A O   
3049 O  O   . HOH F .   ? 0.47120 0.88434 0.79931 0.09034  0.00668  -0.22490 613 HOH A O   
3050 O  O   . HOH F .   ? 0.67139 0.74876 0.80997 0.13189  -0.00050 -0.20170 614 HOH A O   
3051 O  O   . HOH F .   ? 0.77596 0.47263 0.56339 -0.10437 -0.07423 0.06212  615 HOH A O   
3052 O  O   . HOH F .   ? 0.83518 0.66520 0.76033 -0.04629 0.01165  -0.05590 616 HOH A O   
3053 O  O   . HOH F .   ? 0.51823 0.63847 0.64308 0.01056  -0.01672 -0.02182 617 HOH A O   
3054 O  O   . HOH F .   ? 0.49586 0.55399 0.58999 0.00740  -0.01293 -0.03071 618 HOH A O   
3055 O  O   . HOH F .   ? 0.67388 0.58161 0.61449 -0.08781 -0.05207 0.05353  619 HOH A O   
3056 O  O   . HOH F .   ? 0.69138 0.46040 0.49597 -0.14968 -0.02821 -0.00073 620 HOH A O   
3057 O  O   . HOH F .   ? 0.72124 1.27287 1.16100 0.15780  -0.12708 -0.25199 621 HOH A O   
3058 O  O   . HOH F .   ? 0.55336 0.96588 0.84669 0.06210  0.05732  -0.25953 622 HOH A O   
3059 O  O   . HOH F .   ? 0.59344 0.70094 0.68964 0.00164  -0.01685 -0.01491 623 HOH A O   
3060 O  O   . HOH F .   ? 0.92630 0.71559 0.85596 0.03298  -0.06336 -0.00577 624 HOH A O   
3061 O  O   . HOH F .   ? 0.49799 0.65722 0.68678 0.07288  -0.04146 -0.07264 625 HOH A O   
3062 O  O   . HOH F .   ? 0.47070 0.58758 0.59856 0.00916  -0.02395 -0.01331 626 HOH A O   
3063 O  O   . HOH F .   ? 0.56924 0.67768 0.72669 0.06440  -0.04660 -0.04702 627 HOH A O   
3064 O  O   . HOH F .   ? 0.59396 0.63206 0.63710 0.00949  -0.04979 0.01332  628 HOH A O   
3065 O  O   . HOH F .   ? 1.02196 0.61299 0.69045 -0.09515 -0.10106 0.05885  629 HOH A O   
3066 O  O   . HOH F .   ? 0.96311 0.65802 0.74635 0.11184  -0.17916 0.01861  630 HOH A O   
3067 O  O   . HOH F .   ? 0.64907 0.60426 0.72461 0.11899  -0.06863 -0.07573 631 HOH A O   
3068 O  O   . HOH F .   ? 1.00013 0.94594 0.54391 -0.21072 0.03817  -0.05784 632 HOH A O   
3069 O  O   . HOH F .   ? 0.67715 0.82969 0.63908 0.08990  -0.14966 -0.10305 633 HOH A O   
3070 O  O   . HOH F .   ? 0.60448 0.55791 0.59139 -0.06216 -0.05207 0.04874  634 HOH A O   
3071 O  O   . HOH F .   ? 0.42056 0.57983 0.52668 -0.00489 0.01289  -0.05987 635 HOH A O   
3072 O  O   . HOH F .   ? 0.72793 0.73489 0.78479 -0.03574 -0.07610 0.03893  636 HOH A O   
3073 O  O   . HOH F .   ? 0.52974 0.86534 0.83670 0.14085  -0.02079 -0.22431 637 HOH A O   
3074 O  O   . HOH F .   ? 0.73476 1.15266 0.83405 -0.15835 0.15098  -0.21545 638 HOH A O   
3075 O  O   . HOH F .   ? 0.55958 0.88775 0.75574 -0.03366 -0.00388 -0.20248 639 HOH A O   
3076 O  O   . HOH F .   ? 0.87747 1.23145 0.98471 0.05961  -0.11479 -0.20142 640 HOH A O   
3077 O  O   . HOH F .   ? 0.60491 0.56634 0.62995 -0.04315 -0.06882 0.04689  641 HOH A O   
3078 O  O   . HOH F .   ? 0.71086 1.09667 0.86275 0.06593  -0.11227 -0.21774 642 HOH A O   
3079 O  O   . HOH F .   ? 0.64020 0.81023 0.75996 0.05334  -0.07185 -0.08585 643 HOH A O   
3080 O  O   . HOH F .   ? 0.48885 0.44344 0.49705 -0.06326 -0.06729 0.04774  644 HOH A O   
3081 O  O   . HOH F .   ? 1.00826 0.99851 0.94321 -0.08926 -0.01812 0.03048  645 HOH A O   
3082 O  O   . HOH F .   ? 1.08816 0.60216 0.66560 -0.09085 -0.14883 0.07336  646 HOH A O   
3083 O  O   . HOH F .   ? 0.82776 1.23763 0.90255 -0.23234 0.14706  -0.17935 647 HOH A O   
3084 O  O   . HOH F .   ? 1.18195 1.24286 0.68091 -0.34119 0.15632  -0.15257 648 HOH A O   
3085 O  O   . HOH F .   ? 0.52071 1.04360 0.91951 0.07405  -0.07312 -0.20576 649 HOH A O   
3086 O  O   . HOH F .   ? 0.55972 0.97433 0.93939 0.20023  -0.12505 -0.22589 650 HOH A O   
3087 O  O   . HOH F .   ? 0.71167 0.86704 0.78405 -0.01575 0.06841  -0.17382 651 HOH A O   
3088 O  O   . HOH F .   ? 0.58877 0.37482 0.49262 -0.01358 -0.08773 0.02966  652 HOH A O   
3089 O  O   . HOH F .   ? 0.86008 0.70348 0.79660 0.02938  -0.14844 0.04207  653 HOH A O   
3090 O  O   . HOH F .   ? 0.69130 0.69557 0.68871 -0.11845 0.03507  -0.12136 654 HOH A O   
3091 O  O   . HOH F .   ? 0.55683 0.82420 0.71535 0.00016  -0.02923 -0.15012 655 HOH A O   
3092 O  O   . HOH F .   ? 0.48485 0.87115 0.81385 0.09672  -0.10254 -0.14729 656 HOH A O   
3093 O  O   . HOH F .   ? 0.58641 0.41973 0.51478 0.00000  0.00000  0.03189  657 HOH A O   
3094 O  O   . HOH F .   ? 0.72364 1.03114 1.03914 0.20179  -0.13875 -0.18110 658 HOH A O   
3095 O  O   . HOH F .   ? 0.63223 0.67895 0.72113 0.00282  -0.03815 -0.05448 659 HOH A O   
3096 O  O   . HOH F .   ? 1.25396 1.60686 1.17118 0.09766  -0.22595 -0.24720 660 HOH A O   
3097 O  O   . HOH F .   ? 0.53162 0.70191 0.66650 0.03006  -0.04884 -0.08768 661 HOH A O   
3098 O  O   . HOH F .   ? 0.66951 1.00342 0.81392 -0.04615 -0.00578 -0.20895 662 HOH A O   
3099 O  O   . HOH F .   ? 0.83822 0.70613 0.67136 -0.21571 0.06492  -0.10537 663 HOH A O   
3100 O  O   . HOH F .   ? 0.63317 0.68881 0.68700 -0.08337 0.02116  -0.11504 664 HOH A O   
3101 O  O   . HOH F .   ? 0.51745 0.78974 0.72931 0.08807  0.06415  -0.27708 665 HOH A O   
3102 O  O   . HOH F .   ? 0.75387 0.67471 0.78738 0.11622  -0.00102 -0.18668 666 HOH A O   
3103 O  O   . HOH F .   ? 0.70454 1.15184 0.91073 0.04641  -0.09076 -0.25351 667 HOH A O   
3104 O  O   . HOH F .   ? 0.82384 1.17630 0.79183 -0.29651 0.17198  -0.17161 668 HOH A O   
3105 O  O   . HOH F .   ? 0.89147 0.59888 0.78404 0.11134  -0.10802 -0.03378 669 HOH A O   
3106 O  O   . HOH F .   ? 0.79189 0.92714 0.95833 0.03932  -0.06701 -0.02247 670 HOH A O   
3107 O  O   . HOH F .   ? 0.91077 0.84570 0.83900 -0.11142 0.08692  -0.18690 671 HOH A O   
3108 O  O   . HOH F .   ? 0.74226 0.74272 0.74616 -0.08846 -0.04042 0.03774  672 HOH A O   
3109 O  O   . HOH F .   ? 0.81216 0.81814 0.88589 0.00193  -0.03452 0.00459  673 HOH A O   
3110 O  O   . HOH F .   ? 0.93858 1.28150 0.90077 -0.08466 -0.01657 -0.25560 674 HOH A O   
3111 O  O   . HOH F .   ? 0.85984 0.52355 0.65886 0.02297  -0.12339 0.03409  675 HOH A O   
3112 O  O   . HOH F .   ? 0.84929 0.78179 0.75609 -0.18922 0.06686  -0.10572 676 HOH A O   
3113 O  O   . HOH F .   ? 0.75940 1.16558 0.95518 0.08474  -0.11648 -0.23130 677 HOH A O   
3114 O  O   . HOH F .   ? 0.81583 0.55983 0.69023 0.04944  -0.12096 0.00902  678 HOH A O   
3115 O  O   . HOH F .   ? 0.77381 0.77295 0.87312 0.14464  -0.02172 -0.18138 679 HOH A O   
3116 O  O   . HOH F .   ? 0.75342 0.96802 0.91304 0.00992  -0.03161 -0.12296 680 HOH A O   
3117 O  O   . HOH F .   ? 0.68789 0.73054 0.79072 0.10797  0.01618  -0.20128 681 HOH A O   
3118 O  O   . HOH F .   ? 0.76140 0.97758 0.75307 -0.08473 0.06527  -0.20629 682 HOH A O   
3119 O  O   . HOH F .   ? 1.05741 0.74698 0.92050 0.06844  -0.09640 -0.00904 683 HOH A O   
3120 O  O   . HOH F .   ? 1.09967 0.89622 0.74210 -0.08775 -0.06174 0.04172  684 HOH A O   
# 
