data_9OG8
# 
_entry.id   9OG8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9OG8         pdb_00009og8 10.2210/pdb9og8/pdb 
WWPDB D_1000295496 ?            ?                   
# 
_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       2025-06-18 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9OG8 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yunsong.tong@abbvie.com 
_pdbx_contact_author.name_first         Yunsong 
_pdbx_contact_author.name_last          Tong 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3414-0768 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pemberton, O.A.' 1 0000-0003-1740-6085 
'Tong, Y.'        2 0000-0003-3414-0768 
'Nocek, B.'       3 0000-0001-8257-0792 
'Tang, H.Y.H.'    4 0000-0001-7600-6263 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Validation, Key Pharmacophores, and X-ray Cocrystal Structures of Novel Biochemically and Cellularly Active WRN Inhibitors Derived from a DNA-Encoded Library Screen.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c03029 
_citation.pdbx_database_id_PubMed   40472162 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Tong, Y.'             1  0000-0003-3414-0768 
primary 'Baker, K.A.'          2  ?                   
primary 'Chapman, A.M.'        3  ?                   
primary 'Elsen, N.L.'          4  0000-0003-1192-7242 
primary 'Fowler, F.'           5  ?                   
primary 'George, M.D.'         6  ?                   
primary 'Gesmundo, N.J.'       7  0000-0003-2882-192X 
primary 'Hatton, H.'           8  ?                   
primary 'Hickey, M.'           9  ?                   
primary 'Hutchins, C.W.'       10 ?                   
primary 'Jeffries, C.L.'       11 ?                   
primary 'Kelly, A.'            12 ?                   
primary 'Korepanova, A.'       13 ?                   
primary 'Miller, I.R.'         14 ?                   
primary 'Nocek, B.'            15 ?                   
primary 'Panchal, S.C.'        16 ?                   
primary 'Pemberton, O.A.'      17 ?                   
primary 'Qiu, W.'              18 ?                   
primary 'Talaty, N.N.'         19 0000-0002-0701-4347 
primary 'Hin Tang, H.Y.'       20 0000-0001-7600-6263 
primary 'Towne, D.'            21 ?                   
primary 'Zhang, M.'            22 ?                   
primary 'Zhao, Y.'             23 ?                   
primary 'Gopalakrishnan, S.M.' 24 ?                   
primary 'Sun, C.'              25 ?                   
primary 'Kort, M.E.'           26 ?                   
primary 'Dart, M.J.'           27 ?                   
primary 'Firestone, A.J.'      28 0000-0001-9902-443X 
# 
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 
;Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
;
48233.812 1   3.1.-.-,5.6.2.4 ? ? ? 
2 non-polymer syn 
;(3R,4S)-N-[(2R)-3-cyclohexyl-1-(methylamino)-1-oxopropan-2-yl]-4-{3-[6-(ethanesulfonamido)-2-oxo-2,3-dihydro-1H-1,3-benzimidazol-1-yl]propanamido}-1-[(2-fluoro-4-methylphenyl)acetyl]piperidine-3-carboxamide
;
755.899   1   ?               ? ? ? 
3 non-polymer syn 'ZINC ION' 65.409    1   ?               ? ? ? 
4 water       nat water 18.015    265 ?               ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'DNA helicase,RecQ-like type 3,RecQ protein-like 2,Werner syndrome protein' 
# 
_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       
;SGSDFLWPAPNEEQVTCLKMYFGHSSFKPVQWKVIHSVLEERRDNVAVMATGYGKSLCFQYPPVYVGKIGLVISPLISLM
EDQVLQLKMSNIPACFLGSAQSENVLTDIKLGKYRIVYVTPEYCSGNMGLLQQLEADIGITLIAVDEAHCISEWGHDFRD
SFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFDRPNLYLEVRRKTGNILQDLQPFLVKTSSHWE
FEGPTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAP
KDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRNEKFRLYKLKMMAKMEKYLHSSRCRRQIILSHFEDKQV
QKASLGIMGTEKCCDNCRSRLDHC
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGSDFLWPAPNEEQVTCLKMYFGHSSFKPVQWKVIHSVLEERRDNVAVMATGYGKSLCFQYPPVYVGKIGLVISPLISLM
EDQVLQLKMSNIPACFLGSAQSENVLTDIKLGKYRIVYVTPEYCSGNMGLLQQLEADIGITLIAVDEAHCISEWGHDFRD
SFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFDRPNLYLEVRRKTGNILQDLQPFLVKTSSHWE
FEGPTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAP
KDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRNEKFRLYKLKMMAKMEKYLHSSRCRRQIILSHFEDKQV
QKASLGIMGTEKCCDNCRSRLDHC
;
_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 
;(3R,4S)-N-[(2R)-3-cyclohexyl-1-(methylamino)-1-oxopropan-2-yl]-4-{3-[6-(ethanesulfonamido)-2-oxo-2,3-dihydro-1H-1,3-benzimidazol-1-yl]propanamido}-1-[(2-fluoro-4-methylphenyl)acetyl]piperidine-3-carboxamide
;
A1CA5 
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   SER n 
1 2   GLY n 
1 3   SER n 
1 4   ASP n 
1 5   PHE n 
1 6   LEU n 
1 7   TRP n 
1 8   PRO n 
1 9   ALA n 
1 10  PRO n 
1 11  ASN n 
1 12  GLU n 
1 13  GLU n 
1 14  GLN n 
1 15  VAL n 
1 16  THR n 
1 17  CYS n 
1 18  LEU n 
1 19  LYS n 
1 20  MET n 
1 21  TYR n 
1 22  PHE n 
1 23  GLY n 
1 24  HIS n 
1 25  SER n 
1 26  SER n 
1 27  PHE n 
1 28  LYS n 
1 29  PRO n 
1 30  VAL n 
1 31  GLN n 
1 32  TRP n 
1 33  LYS n 
1 34  VAL n 
1 35  ILE n 
1 36  HIS n 
1 37  SER n 
1 38  VAL n 
1 39  LEU n 
1 40  GLU n 
1 41  GLU n 
1 42  ARG n 
1 43  ARG n 
1 44  ASP n 
1 45  ASN n 
1 46  VAL n 
1 47  ALA n 
1 48  VAL n 
1 49  MET n 
1 50  ALA n 
1 51  THR n 
1 52  GLY n 
1 53  TYR n 
1 54  GLY n 
1 55  LYS n 
1 56  SER n 
1 57  LEU n 
1 58  CYS n 
1 59  PHE n 
1 60  GLN n 
1 61  TYR n 
1 62  PRO n 
1 63  PRO n 
1 64  VAL n 
1 65  TYR n 
1 66  VAL n 
1 67  GLY n 
1 68  LYS n 
1 69  ILE n 
1 70  GLY n 
1 71  LEU n 
1 72  VAL n 
1 73  ILE n 
1 74  SER n 
1 75  PRO n 
1 76  LEU n 
1 77  ILE n 
1 78  SER n 
1 79  LEU n 
1 80  MET n 
1 81  GLU n 
1 82  ASP n 
1 83  GLN n 
1 84  VAL n 
1 85  LEU n 
1 86  GLN n 
1 87  LEU n 
1 88  LYS n 
1 89  MET n 
1 90  SER n 
1 91  ASN n 
1 92  ILE n 
1 93  PRO n 
1 94  ALA n 
1 95  CYS n 
1 96  PHE n 
1 97  LEU n 
1 98  GLY n 
1 99  SER n 
1 100 ALA n 
1 101 GLN n 
1 102 SER n 
1 103 GLU n 
1 104 ASN n 
1 105 VAL n 
1 106 LEU n 
1 107 THR n 
1 108 ASP n 
1 109 ILE n 
1 110 LYS n 
1 111 LEU n 
1 112 GLY n 
1 113 LYS n 
1 114 TYR n 
1 115 ARG n 
1 116 ILE n 
1 117 VAL n 
1 118 TYR n 
1 119 VAL n 
1 120 THR n 
1 121 PRO n 
1 122 GLU n 
1 123 TYR n 
1 124 CYS n 
1 125 SER n 
1 126 GLY n 
1 127 ASN n 
1 128 MET n 
1 129 GLY n 
1 130 LEU n 
1 131 LEU n 
1 132 GLN n 
1 133 GLN n 
1 134 LEU n 
1 135 GLU n 
1 136 ALA n 
1 137 ASP n 
1 138 ILE n 
1 139 GLY n 
1 140 ILE n 
1 141 THR n 
1 142 LEU n 
1 143 ILE n 
1 144 ALA n 
1 145 VAL n 
1 146 ASP n 
1 147 GLU n 
1 148 ALA n 
1 149 HIS n 
1 150 CYS n 
1 151 ILE n 
1 152 SER n 
1 153 GLU n 
1 154 TRP n 
1 155 GLY n 
1 156 HIS n 
1 157 ASP n 
1 158 PHE n 
1 159 ARG n 
1 160 ASP n 
1 161 SER n 
1 162 PHE n 
1 163 ARG n 
1 164 LYS n 
1 165 LEU n 
1 166 GLY n 
1 167 SER n 
1 168 LEU n 
1 169 LYS n 
1 170 THR n 
1 171 ALA n 
1 172 LEU n 
1 173 PRO n 
1 174 MET n 
1 175 VAL n 
1 176 PRO n 
1 177 ILE n 
1 178 VAL n 
1 179 ALA n 
1 180 LEU n 
1 181 THR n 
1 182 ALA n 
1 183 THR n 
1 184 ALA n 
1 185 SER n 
1 186 SER n 
1 187 SER n 
1 188 ILE n 
1 189 ARG n 
1 190 GLU n 
1 191 ASP n 
1 192 ILE n 
1 193 VAL n 
1 194 ARG n 
1 195 CYS n 
1 196 LEU n 
1 197 ASN n 
1 198 LEU n 
1 199 ARG n 
1 200 ASN n 
1 201 PRO n 
1 202 GLN n 
1 203 ILE n 
1 204 THR n 
1 205 CYS n 
1 206 THR n 
1 207 GLY n 
1 208 PHE n 
1 209 ASP n 
1 210 ARG n 
1 211 PRO n 
1 212 ASN n 
1 213 LEU n 
1 214 TYR n 
1 215 LEU n 
1 216 GLU n 
1 217 VAL n 
1 218 ARG n 
1 219 ARG n 
1 220 LYS n 
1 221 THR n 
1 222 GLY n 
1 223 ASN n 
1 224 ILE n 
1 225 LEU n 
1 226 GLN n 
1 227 ASP n 
1 228 LEU n 
1 229 GLN n 
1 230 PRO n 
1 231 PHE n 
1 232 LEU n 
1 233 VAL n 
1 234 LYS n 
1 235 THR n 
1 236 SER n 
1 237 SER n 
1 238 HIS n 
1 239 TRP n 
1 240 GLU n 
1 241 PHE n 
1 242 GLU n 
1 243 GLY n 
1 244 PRO n 
1 245 THR n 
1 246 ILE n 
1 247 ILE n 
1 248 TYR n 
1 249 CYS n 
1 250 PRO n 
1 251 SER n 
1 252 ARG n 
1 253 LYS n 
1 254 MET n 
1 255 THR n 
1 256 GLN n 
1 257 GLN n 
1 258 VAL n 
1 259 THR n 
1 260 GLY n 
1 261 GLU n 
1 262 LEU n 
1 263 ARG n 
1 264 LYS n 
1 265 LEU n 
1 266 ASN n 
1 267 LEU n 
1 268 SER n 
1 269 CYS n 
1 270 GLY n 
1 271 THR n 
1 272 TYR n 
1 273 HIS n 
1 274 ALA n 
1 275 GLY n 
1 276 MET n 
1 277 SER n 
1 278 PHE n 
1 279 SER n 
1 280 THR n 
1 281 ARG n 
1 282 LYS n 
1 283 ASP n 
1 284 ILE n 
1 285 HIS n 
1 286 HIS n 
1 287 ARG n 
1 288 PHE n 
1 289 VAL n 
1 290 ARG n 
1 291 ASP n 
1 292 GLU n 
1 293 ILE n 
1 294 GLN n 
1 295 CYS n 
1 296 VAL n 
1 297 ILE n 
1 298 ALA n 
1 299 THR n 
1 300 ILE n 
1 301 ALA n 
1 302 PHE n 
1 303 GLY n 
1 304 MET n 
1 305 GLY n 
1 306 ILE n 
1 307 ASN n 
1 308 LYS n 
1 309 ALA n 
1 310 ASP n 
1 311 ILE n 
1 312 ARG n 
1 313 GLN n 
1 314 VAL n 
1 315 ILE n 
1 316 HIS n 
1 317 TYR n 
1 318 GLY n 
1 319 ALA n 
1 320 PRO n 
1 321 LYS n 
1 322 ASP n 
1 323 MET n 
1 324 GLU n 
1 325 SER n 
1 326 TYR n 
1 327 TYR n 
1 328 GLN n 
1 329 GLU n 
1 330 ILE n 
1 331 GLY n 
1 332 ARG n 
1 333 ALA n 
1 334 GLY n 
1 335 ARG n 
1 336 ASP n 
1 337 GLY n 
1 338 LEU n 
1 339 GLN n 
1 340 SER n 
1 341 SER n 
1 342 CYS n 
1 343 HIS n 
1 344 VAL n 
1 345 LEU n 
1 346 TRP n 
1 347 ALA n 
1 348 PRO n 
1 349 ALA n 
1 350 ASP n 
1 351 ILE n 
1 352 ASN n 
1 353 LEU n 
1 354 ASN n 
1 355 ARG n 
1 356 HIS n 
1 357 LEU n 
1 358 LEU n 
1 359 THR n 
1 360 GLU n 
1 361 ILE n 
1 362 ARG n 
1 363 ASN n 
1 364 GLU n 
1 365 LYS n 
1 366 PHE n 
1 367 ARG n 
1 368 LEU n 
1 369 TYR n 
1 370 LYS n 
1 371 LEU n 
1 372 LYS n 
1 373 MET n 
1 374 MET n 
1 375 ALA n 
1 376 LYS n 
1 377 MET n 
1 378 GLU n 
1 379 LYS n 
1 380 TYR n 
1 381 LEU n 
1 382 HIS n 
1 383 SER n 
1 384 SER n 
1 385 ARG n 
1 386 CYS n 
1 387 ARG n 
1 388 ARG n 
1 389 GLN n 
1 390 ILE n 
1 391 ILE n 
1 392 LEU n 
1 393 SER n 
1 394 HIS n 
1 395 PHE n 
1 396 GLU n 
1 397 ASP n 
1 398 LYS n 
1 399 GLN n 
1 400 VAL n 
1 401 GLN n 
1 402 LYS n 
1 403 ALA n 
1 404 SER n 
1 405 LEU n 
1 406 GLY n 
1 407 ILE n 
1 408 MET n 
1 409 GLY n 
1 410 THR n 
1 411 GLU n 
1 412 LYS n 
1 413 CYS n 
1 414 CYS n 
1 415 ASP n 
1 416 ASN n 
1 417 CYS n 
1 418 ARG n 
1 419 SER n 
1 420 ARG n 
1 421 LEU n 
1 422 ASP n 
1 423 HIS n 
1 424 CYS 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                   424 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'WRN, RECQ3, RECQL2' 
_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               'fall armyworm' 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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          baculovirus 
_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 
A1CA5 non-polymer         . 
;(3R,4S)-N-[(2R)-3-cyclohexyl-1-(methylamino)-1-oxopropan-2-yl]-4-{3-[6-(ethanesulfonamido)-2-oxo-2,3-dihydro-1H-1,3-benzimidazol-1-yl]propanamido}-1-[(2-fluoro-4-methylphenyl)acetyl]piperidine-3-carboxamide
;
? 'C37 H50 F N7 O7 S' 755.899 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'        133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'      121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER ? 'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'     149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'        115.130 
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   SER 1   523 523 SER SER A . n 
A 1 2   GLY 2   524 524 GLY GLY A . n 
A 1 3   SER 3   525 525 SER SER A . n 
A 1 4   ASP 4   526 526 ASP ASP A . n 
A 1 5   PHE 5   527 527 PHE PHE A . n 
A 1 6   LEU 6   528 528 LEU LEU A . n 
A 1 7   TRP 7   529 529 TRP TRP A . n 
A 1 8   PRO 8   530 530 PRO PRO A . n 
A 1 9   ALA 9   531 531 ALA ALA A . n 
A 1 10  PRO 10  532 532 PRO PRO A . n 
A 1 11  ASN 11  533 533 ASN ASN A . n 
A 1 12  GLU 12  534 534 GLU GLU A . n 
A 1 13  GLU 13  535 535 GLU GLU A . n 
A 1 14  GLN 14  536 536 GLN GLN A . n 
A 1 15  VAL 15  537 537 VAL VAL A . n 
A 1 16  THR 16  538 538 THR THR A . n 
A 1 17  CYS 17  539 539 CYS CYS A . n 
A 1 18  LEU 18  540 540 LEU LEU A . n 
A 1 19  LYS 19  541 541 LYS LYS A . n 
A 1 20  MET 20  542 542 MET MET A . n 
A 1 21  TYR 21  543 543 TYR TYR A . n 
A 1 22  PHE 22  544 544 PHE PHE A . n 
A 1 23  GLY 23  545 545 GLY GLY A . n 
A 1 24  HIS 24  546 546 HIS HIS A . n 
A 1 25  SER 25  547 547 SER SER A . n 
A 1 26  SER 26  548 548 SER SER A . n 
A 1 27  PHE 27  549 549 PHE PHE A . n 
A 1 28  LYS 28  550 550 LYS LYS A . n 
A 1 29  PRO 29  551 551 PRO PRO A . n 
A 1 30  VAL 30  552 552 VAL VAL A . n 
A 1 31  GLN 31  553 553 GLN GLN A . n 
A 1 32  TRP 32  554 554 TRP TRP A . n 
A 1 33  LYS 33  555 555 LYS LYS A . n 
A 1 34  VAL 34  556 556 VAL VAL A . n 
A 1 35  ILE 35  557 557 ILE ILE A . n 
A 1 36  HIS 36  558 558 HIS HIS A . n 
A 1 37  SER 37  559 559 SER SER A . n 
A 1 38  VAL 38  560 560 VAL VAL A . n 
A 1 39  LEU 39  561 561 LEU LEU A . n 
A 1 40  GLU 40  562 562 GLU GLU A . n 
A 1 41  GLU 41  563 563 GLU GLU A . n 
A 1 42  ARG 42  564 564 ARG ARG A . n 
A 1 43  ARG 43  565 565 ARG ARG A . n 
A 1 44  ASP 44  566 566 ASP ASP A . n 
A 1 45  ASN 45  567 567 ASN ASN A . n 
A 1 46  VAL 46  568 568 VAL VAL A . n 
A 1 47  ALA 47  569 569 ALA ALA A . n 
A 1 48  VAL 48  570 570 VAL VAL A . n 
A 1 49  MET 49  571 571 MET MET A . n 
A 1 50  ALA 50  572 572 ALA ALA A . n 
A 1 51  THR 51  573 573 THR THR A . n 
A 1 52  GLY 52  574 574 GLY GLY A . n 
A 1 53  TYR 53  575 575 TYR TYR A . n 
A 1 54  GLY 54  576 576 GLY GLY A . n 
A 1 55  LYS 55  577 577 LYS LYS A . n 
A 1 56  SER 56  578 578 SER SER A . n 
A 1 57  LEU 57  579 579 LEU LEU A . n 
A 1 58  CYS 58  580 580 CYS CYS A . n 
A 1 59  PHE 59  581 581 PHE PHE A . n 
A 1 60  GLN 60  582 582 GLN GLN A . n 
A 1 61  TYR 61  583 583 TYR TYR A . n 
A 1 62  PRO 62  584 584 PRO PRO A . n 
A 1 63  PRO 63  585 585 PRO PRO A . n 
A 1 64  VAL 64  586 586 VAL VAL A . n 
A 1 65  TYR 65  587 587 TYR TYR A . n 
A 1 66  VAL 66  588 588 VAL VAL A . n 
A 1 67  GLY 67  589 589 GLY GLY A . n 
A 1 68  LYS 68  590 590 LYS LYS A . n 
A 1 69  ILE 69  591 591 ILE ILE A . n 
A 1 70  GLY 70  592 592 GLY GLY A . n 
A 1 71  LEU 71  593 593 LEU LEU A . n 
A 1 72  VAL 72  594 594 VAL VAL A . n 
A 1 73  ILE 73  595 595 ILE ILE A . n 
A 1 74  SER 74  596 596 SER SER A . n 
A 1 75  PRO 75  597 597 PRO PRO A . n 
A 1 76  LEU 76  598 598 LEU LEU A . n 
A 1 77  ILE 77  599 599 ILE ILE A . n 
A 1 78  SER 78  600 600 SER SER A . n 
A 1 79  LEU 79  601 601 LEU LEU A . n 
A 1 80  MET 80  602 602 MET MET A . n 
A 1 81  GLU 81  603 603 GLU GLU A . n 
A 1 82  ASP 82  604 604 ASP ASP A . n 
A 1 83  GLN 83  605 605 GLN GLN A . n 
A 1 84  VAL 84  606 606 VAL VAL A . n 
A 1 85  LEU 85  607 607 LEU LEU A . n 
A 1 86  GLN 86  608 608 GLN GLN A . n 
A 1 87  LEU 87  609 609 LEU LEU A . n 
A 1 88  LYS 88  610 610 LYS LYS A . n 
A 1 89  MET 89  611 611 MET MET A . n 
A 1 90  SER 90  612 612 SER SER A . n 
A 1 91  ASN 91  613 613 ASN ASN A . n 
A 1 92  ILE 92  614 614 ILE ILE A . n 
A 1 93  PRO 93  615 615 PRO PRO A . n 
A 1 94  ALA 94  616 616 ALA ALA A . n 
A 1 95  CYS 95  617 617 CYS CYS A . n 
A 1 96  PHE 96  618 618 PHE PHE A . n 
A 1 97  LEU 97  619 619 LEU LEU A . n 
A 1 98  GLY 98  620 620 GLY GLY A . n 
A 1 99  SER 99  621 621 SER SER A . n 
A 1 100 ALA 100 622 622 ALA ALA A . n 
A 1 101 GLN 101 623 623 GLN GLN A . n 
A 1 102 SER 102 624 624 SER SER A . n 
A 1 103 GLU 103 625 625 GLU GLU A . n 
A 1 104 ASN 104 626 626 ASN ASN A . n 
A 1 105 VAL 105 627 627 VAL VAL A . n 
A 1 106 LEU 106 628 628 LEU LEU A . n 
A 1 107 THR 107 629 629 THR THR A . n 
A 1 108 ASP 108 630 630 ASP ASP A . n 
A 1 109 ILE 109 631 631 ILE ILE A . n 
A 1 110 LYS 110 632 632 LYS LYS A . n 
A 1 111 LEU 111 633 633 LEU LEU A . n 
A 1 112 GLY 112 634 634 GLY GLY A . n 
A 1 113 LYS 113 635 635 LYS LYS A . n 
A 1 114 TYR 114 636 636 TYR TYR A . n 
A 1 115 ARG 115 637 637 ARG ARG A . n 
A 1 116 ILE 116 638 638 ILE ILE A . n 
A 1 117 VAL 117 639 639 VAL VAL A . n 
A 1 118 TYR 118 640 640 TYR TYR A . n 
A 1 119 VAL 119 641 641 VAL VAL A . n 
A 1 120 THR 120 642 642 THR THR A . n 
A 1 121 PRO 121 643 643 PRO PRO A . n 
A 1 122 GLU 122 644 644 GLU GLU A . n 
A 1 123 TYR 123 645 645 TYR TYR A . n 
A 1 124 CYS 124 646 646 CYS CYS A . n 
A 1 125 SER 125 647 647 SER SER A . n 
A 1 126 GLY 126 648 648 GLY GLY A . n 
A 1 127 ASN 127 649 649 ASN ASN A . n 
A 1 128 MET 128 650 650 MET MET A . n 
A 1 129 GLY 129 651 651 GLY GLY A . n 
A 1 130 LEU 130 652 652 LEU LEU A . n 
A 1 131 LEU 131 653 653 LEU LEU A . n 
A 1 132 GLN 132 654 654 GLN GLN A . n 
A 1 133 GLN 133 655 655 GLN GLN A . n 
A 1 134 LEU 134 656 656 LEU LEU A . n 
A 1 135 GLU 135 657 657 GLU GLU A . n 
A 1 136 ALA 136 658 658 ALA ALA A . n 
A 1 137 ASP 137 659 659 ASP ASP A . n 
A 1 138 ILE 138 660 660 ILE ILE A . n 
A 1 139 GLY 139 661 661 GLY GLY A . n 
A 1 140 ILE 140 662 662 ILE ILE A . n 
A 1 141 THR 141 663 663 THR THR A . n 
A 1 142 LEU 142 664 664 LEU LEU A . n 
A 1 143 ILE 143 665 665 ILE ILE A . n 
A 1 144 ALA 144 666 666 ALA ALA A . n 
A 1 145 VAL 145 667 667 VAL VAL A . n 
A 1 146 ASP 146 668 668 ASP ASP A . n 
A 1 147 GLU 147 669 669 GLU GLU A . n 
A 1 148 ALA 148 670 670 ALA ALA A . n 
A 1 149 HIS 149 671 671 HIS HIS A . n 
A 1 150 CYS 150 672 672 CYS CYS A . n 
A 1 151 ILE 151 673 673 ILE ILE A . n 
A 1 152 SER 152 674 674 SER SER A . n 
A 1 153 GLU 153 675 675 GLU GLU A . n 
A 1 154 TRP 154 676 676 TRP TRP A . n 
A 1 155 GLY 155 677 677 GLY GLY A . n 
A 1 156 HIS 156 678 678 HIS HIS A . n 
A 1 157 ASP 157 679 679 ASP ASP A . n 
A 1 158 PHE 158 680 680 PHE PHE A . n 
A 1 159 ARG 159 681 681 ARG ARG A . n 
A 1 160 ASP 160 682 682 ASP ASP A . n 
A 1 161 SER 161 683 683 SER SER A . n 
A 1 162 PHE 162 684 684 PHE PHE A . n 
A 1 163 ARG 163 685 685 ARG ARG A . n 
A 1 164 LYS 164 686 686 LYS LYS A . n 
A 1 165 LEU 165 687 687 LEU LEU A . n 
A 1 166 GLY 166 688 688 GLY GLY A . n 
A 1 167 SER 167 689 689 SER SER A . n 
A 1 168 LEU 168 690 690 LEU LEU A . n 
A 1 169 LYS 169 691 691 LYS LYS A . n 
A 1 170 THR 170 692 692 THR THR A . n 
A 1 171 ALA 171 693 693 ALA ALA A . n 
A 1 172 LEU 172 694 694 LEU LEU A . n 
A 1 173 PRO 173 695 695 PRO PRO A . n 
A 1 174 MET 174 696 696 MET MET A . n 
A 1 175 VAL 175 697 697 VAL VAL A . n 
A 1 176 PRO 176 698 698 PRO PRO A . n 
A 1 177 ILE 177 699 699 ILE ILE A . n 
A 1 178 VAL 178 700 700 VAL VAL A . n 
A 1 179 ALA 179 701 701 ALA ALA A . n 
A 1 180 LEU 180 702 702 LEU LEU A . n 
A 1 181 THR 181 703 703 THR THR A . n 
A 1 182 ALA 182 704 704 ALA ALA A . n 
A 1 183 THR 183 705 705 THR THR A . n 
A 1 184 ALA 184 706 706 ALA ALA A . n 
A 1 185 SER 185 707 707 SER SER A . n 
A 1 186 SER 186 708 708 SER SER A . n 
A 1 187 SER 187 709 709 SER SER A . n 
A 1 188 ILE 188 710 710 ILE ILE A . n 
A 1 189 ARG 189 711 711 ARG ARG A . n 
A 1 190 GLU 190 712 712 GLU GLU A . n 
A 1 191 ASP 191 713 713 ASP ASP A . n 
A 1 192 ILE 192 714 714 ILE ILE A . n 
A 1 193 VAL 193 715 715 VAL VAL A . n 
A 1 194 ARG 194 716 716 ARG ARG A . n 
A 1 195 CYS 195 717 717 CYS CYS A . n 
A 1 196 LEU 196 718 718 LEU LEU A . n 
A 1 197 ASN 197 719 719 ASN ASN A . n 
A 1 198 LEU 198 720 720 LEU LEU A . n 
A 1 199 ARG 199 721 721 ARG ARG A . n 
A 1 200 ASN 200 722 722 ASN ASN A . n 
A 1 201 PRO 201 723 723 PRO PRO A . n 
A 1 202 GLN 202 724 724 GLN GLN A . n 
A 1 203 ILE 203 725 725 ILE ILE A . n 
A 1 204 THR 204 726 726 THR THR A . n 
A 1 205 CYS 205 727 727 CYS CYS A . n 
A 1 206 THR 206 728 728 THR THR A . n 
A 1 207 GLY 207 729 729 GLY GLY A . n 
A 1 208 PHE 208 730 730 PHE PHE A . n 
A 1 209 ASP 209 731 731 ASP ASP A . n 
A 1 210 ARG 210 732 732 ARG ARG A . n 
A 1 211 PRO 211 733 733 PRO PRO A . n 
A 1 212 ASN 212 734 734 ASN ASN A . n 
A 1 213 LEU 213 735 735 LEU LEU A . n 
A 1 214 TYR 214 736 736 TYR TYR A . n 
A 1 215 LEU 215 737 737 LEU LEU A . n 
A 1 216 GLU 216 738 738 GLU GLU A . n 
A 1 217 VAL 217 739 739 VAL VAL A . n 
A 1 218 ARG 218 740 740 ARG ARG A . n 
A 1 219 ARG 219 741 741 ARG ARG A . n 
A 1 220 LYS 220 742 742 LYS LYS A . n 
A 1 221 THR 221 743 743 THR THR A . n 
A 1 222 GLY 222 744 744 GLY GLY A . n 
A 1 223 ASN 223 745 745 ASN ASN A . n 
A 1 224 ILE 224 746 746 ILE ILE A . n 
A 1 225 LEU 225 747 747 LEU LEU A . n 
A 1 226 GLN 226 748 748 GLN GLN A . n 
A 1 227 ASP 227 749 749 ASP ASP A . n 
A 1 228 LEU 228 750 750 LEU LEU A . n 
A 1 229 GLN 229 751 751 GLN GLN A . n 
A 1 230 PRO 230 752 752 PRO PRO A . n 
A 1 231 PHE 231 753 753 PHE PHE A . n 
A 1 232 LEU 232 754 754 LEU LEU A . n 
A 1 233 VAL 233 755 755 VAL VAL A . n 
A 1 234 LYS 234 756 756 LYS LYS A . n 
A 1 235 THR 235 757 757 THR THR A . n 
A 1 236 SER 236 758 ?   ?   ?   A . n 
A 1 237 SER 237 759 ?   ?   ?   A . n 
A 1 238 HIS 238 760 760 HIS HIS A . n 
A 1 239 TRP 239 761 761 TRP TRP A . n 
A 1 240 GLU 240 762 762 GLU GLU A . n 
A 1 241 PHE 241 763 763 PHE PHE A . n 
A 1 242 GLU 242 764 764 GLU GLU A . n 
A 1 243 GLY 243 765 765 GLY GLY A . n 
A 1 244 PRO 244 766 766 PRO PRO A . n 
A 1 245 THR 245 767 767 THR THR A . n 
A 1 246 ILE 246 768 768 ILE ILE A . n 
A 1 247 ILE 247 769 769 ILE ILE A . n 
A 1 248 TYR 248 770 770 TYR TYR A . n 
A 1 249 CYS 249 771 771 CYS CYS A . n 
A 1 250 PRO 250 772 772 PRO PRO A . n 
A 1 251 SER 251 773 773 SER SER A . n 
A 1 252 ARG 252 774 774 ARG ARG A . n 
A 1 253 LYS 253 775 775 LYS LYS A . n 
A 1 254 MET 254 776 776 MET MET A . n 
A 1 255 THR 255 777 777 THR THR A . n 
A 1 256 GLN 256 778 778 GLN GLN A . n 
A 1 257 GLN 257 779 779 GLN GLN A . n 
A 1 258 VAL 258 780 780 VAL VAL A . n 
A 1 259 THR 259 781 781 THR THR A . n 
A 1 260 GLY 260 782 782 GLY GLY A . n 
A 1 261 GLU 261 783 783 GLU GLU A . n 
A 1 262 LEU 262 784 784 LEU LEU A . n 
A 1 263 ARG 263 785 785 ARG ARG A . n 
A 1 264 LYS 264 786 786 LYS LYS A . n 
A 1 265 LEU 265 787 787 LEU LEU A . n 
A 1 266 ASN 266 788 788 ASN ASN A . n 
A 1 267 LEU 267 789 789 LEU LEU A . n 
A 1 268 SER 268 790 790 SER SER A . n 
A 1 269 CYS 269 791 791 CYS CYS A . n 
A 1 270 GLY 270 792 792 GLY GLY A . n 
A 1 271 THR 271 793 793 THR THR A . n 
A 1 272 TYR 272 794 794 TYR TYR A . n 
A 1 273 HIS 273 795 795 HIS HIS A . n 
A 1 274 ALA 274 796 796 ALA ALA A . n 
A 1 275 GLY 275 797 797 GLY GLY A . n 
A 1 276 MET 276 798 798 MET MET A . n 
A 1 277 SER 277 799 799 SER SER A . n 
A 1 278 PHE 278 800 800 PHE PHE A . n 
A 1 279 SER 279 801 801 SER SER A . n 
A 1 280 THR 280 802 802 THR THR A . n 
A 1 281 ARG 281 803 803 ARG ARG A . n 
A 1 282 LYS 282 804 804 LYS LYS A . n 
A 1 283 ASP 283 805 805 ASP ASP A . n 
A 1 284 ILE 284 806 806 ILE ILE A . n 
A 1 285 HIS 285 807 807 HIS HIS A . n 
A 1 286 HIS 286 808 808 HIS HIS A . n 
A 1 287 ARG 287 809 809 ARG ARG A . n 
A 1 288 PHE 288 810 810 PHE PHE A . n 
A 1 289 VAL 289 811 811 VAL VAL A . n 
A 1 290 ARG 290 812 812 ARG ARG A . n 
A 1 291 ASP 291 813 813 ASP ASP A . n 
A 1 292 GLU 292 814 814 GLU GLU A . n 
A 1 293 ILE 293 815 815 ILE ILE A . n 
A 1 294 GLN 294 816 816 GLN GLN A . n 
A 1 295 CYS 295 817 817 CYS CYS A . n 
A 1 296 VAL 296 818 818 VAL VAL A . n 
A 1 297 ILE 297 819 819 ILE ILE A . n 
A 1 298 ALA 298 820 820 ALA ALA A . n 
A 1 299 THR 299 821 821 THR THR A . n 
A 1 300 ILE 300 822 822 ILE ILE A . n 
A 1 301 ALA 301 823 823 ALA ALA A . n 
A 1 302 PHE 302 824 824 PHE PHE A . n 
A 1 303 GLY 303 825 825 GLY GLY A . n 
A 1 304 MET 304 826 826 MET MET A . n 
A 1 305 GLY 305 827 827 GLY GLY A . n 
A 1 306 ILE 306 828 828 ILE ILE A . n 
A 1 307 ASN 307 829 829 ASN ASN A . n 
A 1 308 LYS 308 830 830 LYS LYS A . n 
A 1 309 ALA 309 831 831 ALA ALA A . n 
A 1 310 ASP 310 832 832 ASP ASP A . n 
A 1 311 ILE 311 833 833 ILE ILE A . n 
A 1 312 ARG 312 834 834 ARG ARG A . n 
A 1 313 GLN 313 835 835 GLN GLN A . n 
A 1 314 VAL 314 836 836 VAL VAL A . n 
A 1 315 ILE 315 837 837 ILE ILE A . n 
A 1 316 HIS 316 838 838 HIS HIS A . n 
A 1 317 TYR 317 839 839 TYR TYR A . n 
A 1 318 GLY 318 840 840 GLY GLY A . n 
A 1 319 ALA 319 841 841 ALA ALA A . n 
A 1 320 PRO 320 842 842 PRO PRO A . n 
A 1 321 LYS 321 843 843 LYS LYS A . n 
A 1 322 ASP 322 844 844 ASP ASP A . n 
A 1 323 MET 323 845 845 MET MET A . n 
A 1 324 GLU 324 846 846 GLU GLU A . n 
A 1 325 SER 325 847 847 SER SER A . n 
A 1 326 TYR 326 848 848 TYR TYR A . n 
A 1 327 TYR 327 849 849 TYR TYR A . n 
A 1 328 GLN 328 850 850 GLN GLN A . n 
A 1 329 GLU 329 851 851 GLU GLU A . n 
A 1 330 ILE 330 852 852 ILE ILE A . n 
A 1 331 GLY 331 853 853 GLY GLY A . n 
A 1 332 ARG 332 854 854 ARG ARG A . n 
A 1 333 ALA 333 855 855 ALA ALA A . n 
A 1 334 GLY 334 856 856 GLY GLY A . n 
A 1 335 ARG 335 857 857 ARG ARG A . n 
A 1 336 ASP 336 858 858 ASP ASP A . n 
A 1 337 GLY 337 859 859 GLY GLY A . n 
A 1 338 LEU 338 860 860 LEU LEU A . n 
A 1 339 GLN 339 861 861 GLN GLN A . n 
A 1 340 SER 340 862 862 SER SER A . n 
A 1 341 SER 341 863 863 SER SER A . n 
A 1 342 CYS 342 864 864 CYS CYS A . n 
A 1 343 HIS 343 865 865 HIS HIS A . n 
A 1 344 VAL 344 866 866 VAL VAL A . n 
A 1 345 LEU 345 867 867 LEU LEU A . n 
A 1 346 TRP 346 868 868 TRP TRP A . n 
A 1 347 ALA 347 869 869 ALA ALA A . n 
A 1 348 PRO 348 870 870 PRO PRO A . n 
A 1 349 ALA 349 871 871 ALA ALA A . n 
A 1 350 ASP 350 872 872 ASP ASP A . n 
A 1 351 ILE 351 873 873 ILE ILE A . n 
A 1 352 ASN 352 874 874 ASN ASN A . n 
A 1 353 LEU 353 875 875 LEU LEU A . n 
A 1 354 ASN 354 876 876 ASN ASN A . n 
A 1 355 ARG 355 877 877 ARG ARG A . n 
A 1 356 HIS 356 878 878 HIS HIS A . n 
A 1 357 LEU 357 879 879 LEU LEU A . n 
A 1 358 LEU 358 880 880 LEU LEU A . n 
A 1 359 THR 359 881 881 THR THR A . n 
A 1 360 GLU 360 882 882 GLU GLU A . n 
A 1 361 ILE 361 883 883 ILE ILE A . n 
A 1 362 ARG 362 884 884 ARG ARG A . n 
A 1 363 ASN 363 885 885 ASN ASN A . n 
A 1 364 GLU 364 886 886 GLU GLU A . n 
A 1 365 LYS 365 887 887 LYS LYS A . n 
A 1 366 PHE 366 888 888 PHE PHE A . n 
A 1 367 ARG 367 889 889 ARG ARG A . n 
A 1 368 LEU 368 890 890 LEU LEU A . n 
A 1 369 TYR 369 891 891 TYR TYR A . n 
A 1 370 LYS 370 892 892 LYS LYS A . n 
A 1 371 LEU 371 893 893 LEU LEU A . n 
A 1 372 LYS 372 894 894 LYS LYS A . n 
A 1 373 MET 373 895 895 MET MET A . n 
A 1 374 MET 374 896 896 MET MET A . n 
A 1 375 ALA 375 897 897 ALA ALA A . n 
A 1 376 LYS 376 898 898 LYS LYS A . n 
A 1 377 MET 377 899 899 MET MET A . n 
A 1 378 GLU 378 900 900 GLU GLU A . n 
A 1 379 LYS 379 901 901 LYS LYS A . n 
A 1 380 TYR 380 902 902 TYR TYR A . n 
A 1 381 LEU 381 903 903 LEU LEU A . n 
A 1 382 HIS 382 904 904 HIS HIS A . n 
A 1 383 SER 383 905 905 SER SER A . n 
A 1 384 SER 384 906 906 SER SER A . n 
A 1 385 ARG 385 907 907 ARG ARG A . n 
A 1 386 CYS 386 908 908 CYS CYS A . n 
A 1 387 ARG 387 909 909 ARG ARG A . n 
A 1 388 ARG 388 910 910 ARG ARG A . n 
A 1 389 GLN 389 911 911 GLN GLN A . n 
A 1 390 ILE 390 912 912 ILE ILE A . n 
A 1 391 ILE 391 913 913 ILE ILE A . n 
A 1 392 LEU 392 914 914 LEU LEU A . n 
A 1 393 SER 393 915 915 SER SER A . n 
A 1 394 HIS 394 916 916 HIS HIS A . n 
A 1 395 PHE 395 917 917 PHE PHE A . n 
A 1 396 GLU 396 918 918 GLU GLU A . n 
A 1 397 ASP 397 919 919 ASP ASP A . n 
A 1 398 LYS 398 920 920 LYS LYS A . n 
A 1 399 GLN 399 921 921 GLN GLN A . n 
A 1 400 VAL 400 922 922 VAL VAL A . n 
A 1 401 GLN 401 923 923 GLN GLN A . n 
A 1 402 LYS 402 924 924 LYS LYS A . n 
A 1 403 ALA 403 925 925 ALA ALA A . n 
A 1 404 SER 404 926 926 SER SER A . n 
A 1 405 LEU 405 927 927 LEU LEU A . n 
A 1 406 GLY 406 928 928 GLY GLY A . n 
A 1 407 ILE 407 929 929 ILE ILE A . n 
A 1 408 MET 408 930 930 MET MET A . n 
A 1 409 GLY 409 931 931 GLY GLY A . n 
A 1 410 THR 410 932 932 THR THR A . n 
A 1 411 GLU 411 933 933 GLU GLU A . n 
A 1 412 LYS 412 934 934 LYS LYS A . n 
A 1 413 CYS 413 935 935 CYS CYS A . n 
A 1 414 CYS 414 936 936 CYS CYS A . n 
A 1 415 ASP 415 937 937 ASP ASP A . n 
A 1 416 ASN 416 938 938 ASN ASN A . n 
A 1 417 CYS 417 939 939 CYS CYS A . n 
A 1 418 ARG 418 940 940 ARG ARG A . n 
A 1 419 SER 419 941 941 SER SER A . n 
A 1 420 ARG 420 942 942 ARG ARG A . n 
A 1 421 LEU 421 943 943 LEU LEU A . n 
A 1 422 ASP 422 944 944 ASP ASP A . n 
A 1 423 HIS 423 945 945 HIS HIS A . n 
A 1 424 CYS 424 946 946 CYS CYS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1CA5 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1CA5 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1CA5 1   1001 947  A1CA5 LIG A . 
C 3 ZN    1   1002 948  ZN    ZN  A . 
D 4 HOH   1   1101 1012 HOH   HOH A . 
D 4 HOH   2   1102 1198 HOH   HOH A . 
D 4 HOH   3   1103 1122 HOH   HOH A . 
D 4 HOH   4   1104 1156 HOH   HOH A . 
D 4 HOH   5   1105 1049 HOH   HOH A . 
D 4 HOH   6   1106 1046 HOH   HOH A . 
D 4 HOH   7   1107 1087 HOH   HOH A . 
D 4 HOH   8   1108 979  HOH   HOH A . 
D 4 HOH   9   1109 954  HOH   HOH A . 
D 4 HOH   10  1110 956  HOH   HOH A . 
D 4 HOH   11  1111 1088 HOH   HOH A . 
D 4 HOH   12  1112 1090 HOH   HOH A . 
D 4 HOH   13  1113 1133 HOH   HOH A . 
D 4 HOH   14  1114 1112 HOH   HOH A . 
D 4 HOH   15  1115 1114 HOH   HOH A . 
D 4 HOH   16  1116 999  HOH   HOH A . 
D 4 HOH   17  1117 1164 HOH   HOH A . 
D 4 HOH   18  1118 1008 HOH   HOH A . 
D 4 HOH   19  1119 995  HOH   HOH A . 
D 4 HOH   20  1120 1118 HOH   HOH A . 
D 4 HOH   21  1121 1081 HOH   HOH A . 
D 4 HOH   22  1122 1120 HOH   HOH A . 
D 4 HOH   23  1123 1203 HOH   HOH A . 
D 4 HOH   24  1124 1139 HOH   HOH A . 
D 4 HOH   25  1125 985  HOH   HOH A . 
D 4 HOH   26  1126 1157 HOH   HOH A . 
D 4 HOH   27  1127 1077 HOH   HOH A . 
D 4 HOH   28  1128 1045 HOH   HOH A . 
D 4 HOH   29  1129 1040 HOH   HOH A . 
D 4 HOH   30  1130 986  HOH   HOH A . 
D 4 HOH   31  1131 977  HOH   HOH A . 
D 4 HOH   32  1132 1028 HOH   HOH A . 
D 4 HOH   33  1133 1149 HOH   HOH A . 
D 4 HOH   34  1134 1027 HOH   HOH A . 
D 4 HOH   35  1135 1144 HOH   HOH A . 
D 4 HOH   36  1136 975  HOH   HOH A . 
D 4 HOH   37  1137 1071 HOH   HOH A . 
D 4 HOH   38  1138 1172 HOH   HOH A . 
D 4 HOH   39  1139 1170 HOH   HOH A . 
D 4 HOH   40  1140 1188 HOH   HOH A . 
D 4 HOH   41  1141 1121 HOH   HOH A . 
D 4 HOH   42  1142 1135 HOH   HOH A . 
D 4 HOH   43  1143 1020 HOH   HOH A . 
D 4 HOH   44  1144 973  HOH   HOH A . 
D 4 HOH   45  1145 974  HOH   HOH A . 
D 4 HOH   46  1146 1129 HOH   HOH A . 
D 4 HOH   47  1147 1013 HOH   HOH A . 
D 4 HOH   48  1148 963  HOH   HOH A . 
D 4 HOH   49  1149 1080 HOH   HOH A . 
D 4 HOH   50  1150 996  HOH   HOH A . 
D 4 HOH   51  1151 1085 HOH   HOH A . 
D 4 HOH   52  1152 1092 HOH   HOH A . 
D 4 HOH   53  1153 1034 HOH   HOH A . 
D 4 HOH   54  1154 1061 HOH   HOH A . 
D 4 HOH   55  1155 1010 HOH   HOH A . 
D 4 HOH   56  1156 1029 HOH   HOH A . 
D 4 HOH   57  1157 953  HOH   HOH A . 
D 4 HOH   58  1158 1066 HOH   HOH A . 
D 4 HOH   59  1159 1003 HOH   HOH A . 
D 4 HOH   60  1160 981  HOH   HOH A . 
D 4 HOH   61  1161 1171 HOH   HOH A . 
D 4 HOH   62  1162 1059 HOH   HOH A . 
D 4 HOH   63  1163 1142 HOH   HOH A . 
D 4 HOH   64  1164 1014 HOH   HOH A . 
D 4 HOH   65  1165 978  HOH   HOH A . 
D 4 HOH   66  1166 1119 HOH   HOH A . 
D 4 HOH   67  1167 1006 HOH   HOH A . 
D 4 HOH   68  1168 992  HOH   HOH A . 
D 4 HOH   69  1169 1078 HOH   HOH A . 
D 4 HOH   70  1170 962  HOH   HOH A . 
D 4 HOH   71  1171 1094 HOH   HOH A . 
D 4 HOH   72  1172 1138 HOH   HOH A . 
D 4 HOH   73  1173 1043 HOH   HOH A . 
D 4 HOH   74  1174 952  HOH   HOH A . 
D 4 HOH   75  1175 988  HOH   HOH A . 
D 4 HOH   76  1176 967  HOH   HOH A . 
D 4 HOH   77  1177 1117 HOH   HOH A . 
D 4 HOH   78  1178 1099 HOH   HOH A . 
D 4 HOH   79  1179 1096 HOH   HOH A . 
D 4 HOH   80  1180 1068 HOH   HOH A . 
D 4 HOH   81  1181 1000 HOH   HOH A . 
D 4 HOH   82  1182 1017 HOH   HOH A . 
D 4 HOH   83  1183 1100 HOH   HOH A . 
D 4 HOH   84  1184 958  HOH   HOH A . 
D 4 HOH   85  1185 1053 HOH   HOH A . 
D 4 HOH   86  1186 1113 HOH   HOH A . 
D 4 HOH   87  1187 1195 HOH   HOH A . 
D 4 HOH   88  1188 955  HOH   HOH A . 
D 4 HOH   89  1189 971  HOH   HOH A . 
D 4 HOH   90  1190 1062 HOH   HOH A . 
D 4 HOH   91  1191 1009 HOH   HOH A . 
D 4 HOH   92  1192 1030 HOH   HOH A . 
D 4 HOH   93  1193 950  HOH   HOH A . 
D 4 HOH   94  1194 1035 HOH   HOH A . 
D 4 HOH   95  1195 984  HOH   HOH A . 
D 4 HOH   96  1196 1083 HOH   HOH A . 
D 4 HOH   97  1197 1015 HOH   HOH A . 
D 4 HOH   98  1198 1036 HOH   HOH A . 
D 4 HOH   99  1199 1125 HOH   HOH A . 
D 4 HOH   100 1200 1102 HOH   HOH A . 
D 4 HOH   101 1201 1109 HOH   HOH A . 
D 4 HOH   102 1202 1038 HOH   HOH A . 
D 4 HOH   103 1203 1024 HOH   HOH A . 
D 4 HOH   104 1204 1033 HOH   HOH A . 
D 4 HOH   105 1205 1103 HOH   HOH A . 
D 4 HOH   106 1206 1124 HOH   HOH A . 
D 4 HOH   107 1207 1074 HOH   HOH A . 
D 4 HOH   108 1208 1126 HOH   HOH A . 
D 4 HOH   109 1209 1173 HOH   HOH A . 
D 4 HOH   110 1210 1137 HOH   HOH A . 
D 4 HOH   111 1211 1067 HOH   HOH A . 
D 4 HOH   112 1212 957  HOH   HOH A . 
D 4 HOH   113 1213 961  HOH   HOH A . 
D 4 HOH   114 1214 959  HOH   HOH A . 
D 4 HOH   115 1215 1011 HOH   HOH A . 
D 4 HOH   116 1216 1022 HOH   HOH A . 
D 4 HOH   117 1217 1163 HOH   HOH A . 
D 4 HOH   118 1218 972  HOH   HOH A . 
D 4 HOH   119 1219 1108 HOH   HOH A . 
D 4 HOH   120 1220 949  HOH   HOH A . 
D 4 HOH   121 1221 1197 HOH   HOH A . 
D 4 HOH   122 1222 1116 HOH   HOH A . 
D 4 HOH   123 1223 1076 HOH   HOH A . 
D 4 HOH   124 1224 951  HOH   HOH A . 
D 4 HOH   125 1225 969  HOH   HOH A . 
D 4 HOH   126 1226 965  HOH   HOH A . 
D 4 HOH   127 1227 1021 HOH   HOH A . 
D 4 HOH   128 1228 1056 HOH   HOH A . 
D 4 HOH   129 1229 968  HOH   HOH A . 
D 4 HOH   130 1230 993  HOH   HOH A . 
D 4 HOH   131 1231 1136 HOH   HOH A . 
D 4 HOH   132 1232 1177 HOH   HOH A . 
D 4 HOH   133 1233 1159 HOH   HOH A . 
D 4 HOH   134 1234 980  HOH   HOH A . 
D 4 HOH   135 1235 976  HOH   HOH A . 
D 4 HOH   136 1236 1065 HOH   HOH A . 
D 4 HOH   137 1237 1001 HOH   HOH A . 
D 4 HOH   138 1238 1048 HOH   HOH A . 
D 4 HOH   139 1239 1050 HOH   HOH A . 
D 4 HOH   140 1240 1084 HOH   HOH A . 
D 4 HOH   141 1241 1131 HOH   HOH A . 
D 4 HOH   142 1242 1042 HOH   HOH A . 
D 4 HOH   143 1243 1134 HOH   HOH A . 
D 4 HOH   144 1244 970  HOH   HOH A . 
D 4 HOH   145 1245 960  HOH   HOH A . 
D 4 HOH   146 1246 1037 HOH   HOH A . 
D 4 HOH   147 1247 1044 HOH   HOH A . 
D 4 HOH   148 1248 1018 HOH   HOH A . 
D 4 HOH   149 1249 998  HOH   HOH A . 
D 4 HOH   150 1250 1150 HOH   HOH A . 
D 4 HOH   151 1251 1031 HOH   HOH A . 
D 4 HOH   152 1252 1082 HOH   HOH A . 
D 4 HOH   153 1253 1176 HOH   HOH A . 
D 4 HOH   154 1254 1051 HOH   HOH A . 
D 4 HOH   155 1255 1184 HOH   HOH A . 
D 4 HOH   156 1256 997  HOH   HOH A . 
D 4 HOH   157 1257 1127 HOH   HOH A . 
D 4 HOH   158 1258 1047 HOH   HOH A . 
D 4 HOH   159 1259 1058 HOH   HOH A . 
D 4 HOH   160 1260 1039 HOH   HOH A . 
D 4 HOH   161 1261 1091 HOH   HOH A . 
D 4 HOH   162 1262 1023 HOH   HOH A . 
D 4 HOH   163 1263 1155 HOH   HOH A . 
D 4 HOH   164 1264 1183 HOH   HOH A . 
D 4 HOH   165 1265 966  HOH   HOH A . 
D 4 HOH   166 1266 1104 HOH   HOH A . 
D 4 HOH   167 1267 1152 HOH   HOH A . 
D 4 HOH   168 1268 1193 HOH   HOH A . 
D 4 HOH   169 1269 1128 HOH   HOH A . 
D 4 HOH   170 1270 1007 HOH   HOH A . 
D 4 HOH   171 1271 1123 HOH   HOH A . 
D 4 HOH   172 1272 1093 HOH   HOH A . 
D 4 HOH   173 1273 1019 HOH   HOH A . 
D 4 HOH   174 1274 1063 HOH   HOH A . 
D 4 HOH   175 1275 1106 HOH   HOH A . 
D 4 HOH   176 1276 994  HOH   HOH A . 
D 4 HOH   177 1277 1206 HOH   HOH A . 
D 4 HOH   178 1278 1095 HOH   HOH A . 
D 4 HOH   179 1279 1026 HOH   HOH A . 
D 4 HOH   180 1280 1145 HOH   HOH A . 
D 4 HOH   181 1281 1086 HOH   HOH A . 
D 4 HOH   182 1282 983  HOH   HOH A . 
D 4 HOH   183 1283 989  HOH   HOH A . 
D 4 HOH   184 1284 990  HOH   HOH A . 
D 4 HOH   185 1285 1079 HOH   HOH A . 
D 4 HOH   186 1286 1141 HOH   HOH A . 
D 4 HOH   187 1287 1158 HOH   HOH A . 
D 4 HOH   188 1288 1166 HOH   HOH A . 
D 4 HOH   189 1289 1041 HOH   HOH A . 
D 4 HOH   190 1290 1201 HOH   HOH A . 
D 4 HOH   191 1291 1052 HOH   HOH A . 
D 4 HOH   192 1292 1097 HOH   HOH A . 
D 4 HOH   193 1293 1072 HOH   HOH A . 
D 4 HOH   194 1294 1064 HOH   HOH A . 
D 4 HOH   195 1295 1016 HOH   HOH A . 
D 4 HOH   196 1296 1111 HOH   HOH A . 
D 4 HOH   197 1297 1154 HOH   HOH A . 
D 4 HOH   198 1298 1060 HOH   HOH A . 
D 4 HOH   199 1299 1213 HOH   HOH A . 
D 4 HOH   200 1300 1181 HOH   HOH A . 
D 4 HOH   201 1301 1161 HOH   HOH A . 
D 4 HOH   202 1302 1200 HOH   HOH A . 
D 4 HOH   203 1303 1187 HOH   HOH A . 
D 4 HOH   204 1304 1168 HOH   HOH A . 
D 4 HOH   205 1305 1110 HOH   HOH A . 
D 4 HOH   206 1306 1151 HOH   HOH A . 
D 4 HOH   207 1307 1089 HOH   HOH A . 
D 4 HOH   208 1308 1210 HOH   HOH A . 
D 4 HOH   209 1309 1002 HOH   HOH A . 
D 4 HOH   210 1310 1190 HOH   HOH A . 
D 4 HOH   211 1311 1182 HOH   HOH A . 
D 4 HOH   212 1312 964  HOH   HOH A . 
D 4 HOH   213 1313 1179 HOH   HOH A . 
D 4 HOH   214 1314 1165 HOH   HOH A . 
D 4 HOH   215 1315 1196 HOH   HOH A . 
D 4 HOH   216 1316 1054 HOH   HOH A . 
D 4 HOH   217 1317 1178 HOH   HOH A . 
D 4 HOH   218 1318 1167 HOH   HOH A . 
D 4 HOH   219 1319 1025 HOH   HOH A . 
D 4 HOH   220 1320 1105 HOH   HOH A . 
D 4 HOH   221 1321 991  HOH   HOH A . 
D 4 HOH   222 1322 1194 HOH   HOH A . 
D 4 HOH   223 1323 1204 HOH   HOH A . 
D 4 HOH   224 1324 1147 HOH   HOH A . 
D 4 HOH   225 1325 1143 HOH   HOH A . 
D 4 HOH   226 1326 1160 HOH   HOH A . 
D 4 HOH   227 1327 1175 HOH   HOH A . 
D 4 HOH   228 1328 1005 HOH   HOH A . 
D 4 HOH   229 1329 1211 HOH   HOH A . 
D 4 HOH   230 1330 1202 HOH   HOH A . 
D 4 HOH   231 1331 1107 HOH   HOH A . 
D 4 HOH   232 1332 1075 HOH   HOH A . 
D 4 HOH   233 1333 1069 HOH   HOH A . 
D 4 HOH   234 1334 1073 HOH   HOH A . 
D 4 HOH   235 1335 1162 HOH   HOH A . 
D 4 HOH   236 1336 1132 HOH   HOH A . 
D 4 HOH   237 1337 1189 HOH   HOH A . 
D 4 HOH   238 1338 1148 HOH   HOH A . 
D 4 HOH   239 1339 1098 HOH   HOH A . 
D 4 HOH   240 1340 1070 HOH   HOH A . 
D 4 HOH   241 1341 1199 HOH   HOH A . 
D 4 HOH   242 1342 1004 HOH   HOH A . 
D 4 HOH   243 1343 1140 HOH   HOH A . 
D 4 HOH   244 1344 1192 HOH   HOH A . 
D 4 HOH   245 1345 1174 HOH   HOH A . 
D 4 HOH   246 1346 1032 HOH   HOH A . 
D 4 HOH   247 1347 1209 HOH   HOH A . 
D 4 HOH   248 1348 1057 HOH   HOH A . 
D 4 HOH   249 1349 1055 HOH   HOH A . 
D 4 HOH   250 1350 987  HOH   HOH A . 
D 4 HOH   251 1351 1101 HOH   HOH A . 
D 4 HOH   252 1352 1180 HOH   HOH A . 
D 4 HOH   253 1353 1115 HOH   HOH A . 
D 4 HOH   254 1354 1146 HOH   HOH A . 
D 4 HOH   255 1355 1185 HOH   HOH A . 
D 4 HOH   256 1356 982  HOH   HOH A . 
D 4 HOH   257 1357 1130 HOH   HOH A . 
D 4 HOH   258 1358 1207 HOH   HOH A . 
D 4 HOH   259 1359 1205 HOH   HOH A . 
D 4 HOH   260 1360 1208 HOH   HOH A . 
D 4 HOH   261 1361 1191 HOH   HOH A . 
D 4 HOH   262 1362 1169 HOH   HOH A . 
D 4 HOH   263 1363 1153 HOH   HOH A . 
D 4 HOH   264 1364 1212 HOH   HOH A . 
D 4 HOH   265 1365 1186 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_reference_DOI 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.21.2_5419 ? 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? 0.7.15      ? 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? autoPROC    ? ? ? 1.1.7       ? 3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? 2.8.3       ? 4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 4.3         ? 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9OG8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     64.948 
_cell.length_a_esd                 ? 
_cell.length_b                     68.791 
_cell.length_b_esd                 ? 
_cell.length_c                     107.456 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9OG8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9OG8 
_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             2.49 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.57 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '18.0% w/v PEG 3350, 0.18 M Tri-ammonium citrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            290.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-13 
_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   0.91683 
_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                        'CLSI BEAMLINE 08ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.91683 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08ID-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9OG8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.66 
_reflns.d_resolution_low                               57.94 
_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                                     54814 
_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                           94.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.00 
_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                                0.131 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       644704 
_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                              0.125 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.66 
_reflns_shell.d_res_low                                     1.75 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           37611 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6141 
_reflns_shell.percent_possible_obs                          74.1 
_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                               6.1 
_reflns_shell.pdbx_chi_squared                              0.73 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.0 
_reflns_shell.pdbx_Rrim_I_all                               2.020 
_reflns_shell.pdbx_Rpim_I_all                               0.748 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.690 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.869 
_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                               ? 
_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                                 9OG8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.66 
_refine.ls_d_res_low                             57.94 
_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                     54141 
_refine.ls_number_reflns_R_free                  4907 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.44 
_refine.ls_percent_reflns_R_free                 4.81 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2030 
_refine.ls_R_factor_R_free                       0.2386 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2012 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.91 
_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       ML 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 28.57 
_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                            0.27 
_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.pdbx_number_atoms_protein        3361 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_refine_hist.number_atoms_solvent             265 
_refine_hist.number_atoms_total               3680 
_refine_hist.d_res_high                       1.66 
_refine_hist.d_res_low                        57.94 
# 
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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.012  ? 3494 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 1.184  ? 4720 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 14.005 ? 1345 ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.068  ? 516  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 614  ? f_plane_restr      ? ? ? 
# 
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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.66 1.68  . . 96  1923 54.00  . . . . 0.4345 . . . . . . . . . . . . . . . 0.5041 
'X-RAY DIFFRACTION' 1.68 1.70  . . 106 2132 62.00  . . . . 0.4285 . . . . . . . . . . . . . . . 0.4013 
'X-RAY DIFFRACTION' 1.70 1.72  . . 106 2356 67.00  . . . . 0.4068 . . . . . . . . . . . . . . . 0.3825 
'X-RAY DIFFRACTION' 1.72 1.74  . . 101 2486 70.00  . . . . 0.3978 . . . . . . . . . . . . . . . 0.3898 
'X-RAY DIFFRACTION' 1.74 1.76  . . 129 2636 75.00  . . . . 0.3750 . . . . . . . . . . . . . . . 0.3750 
'X-RAY DIFFRACTION' 1.76 1.79  . . 154 2798 80.00  . . . . 0.3603 . . . . . . . . . . . . . . . 0.3685 
'X-RAY DIFFRACTION' 1.79 1.81  . . 153 2990 85.00  . . . . 0.3401 . . . . . . . . . . . . . . . 0.3752 
'X-RAY DIFFRACTION' 1.81 1.84  . . 193 3109 90.00  . . . . 0.3324 . . . . . . . . . . . . . . . 0.3757 
'X-RAY DIFFRACTION' 1.84 1.87  . . 171 3305 95.00  . . . . 0.3079 . . . . . . . . . . . . . . . 0.3318 
'X-RAY DIFFRACTION' 1.87 1.90  . . 161 3485 99.00  . . . . 0.2841 . . . . . . . . . . . . . . . 0.3238 
'X-RAY DIFFRACTION' 1.90 1.93  . . 180 3472 99.00  . . . . 0.2694 . . . . . . . . . . . . . . . 0.3380 
'X-RAY DIFFRACTION' 1.93 1.97  . . 157 3551 100.00 . . . . 0.2613 . . . . . . . . . . . . . . . 0.2759 
'X-RAY DIFFRACTION' 1.97 2.00  . . 215 3393 100.00 . . . . 0.2450 . . . . . . . . . . . . . . . 0.3271 
'X-RAY DIFFRACTION' 2.00 2.04  . . 183 3501 100.00 . . . . 0.2383 . . . . . . . . . . . . . . . 0.2931 
'X-RAY DIFFRACTION' 2.04 2.09  . . 164 3494 100.00 . . . . 0.2244 . . . . . . . . . . . . . . . 0.2416 
'X-RAY DIFFRACTION' 2.09 2.14  . . 184 3519 100.00 . . . . 0.1993 . . . . . . . . . . . . . . . 0.3155 
'X-RAY DIFFRACTION' 2.14 2.19  . . 176 3481 100.00 . . . . 0.1942 . . . . . . . . . . . . . . . 0.2801 
'X-RAY DIFFRACTION' 2.19 2.25  . . 187 3470 100.00 . . . . 0.1960 . . . . . . . . . . . . . . . 0.2112 
'X-RAY DIFFRACTION' 2.25 2.32  . . 140 3536 100.00 . . . . 0.1912 . . . . . . . . . . . . . . . 0.2548 
'X-RAY DIFFRACTION' 2.32 2.39  . . 192 3493 100.00 . . . . 0.1978 . . . . . . . . . . . . . . . 0.2452 
'X-RAY DIFFRACTION' 2.39 2.48  . . 178 3482 100.00 . . . . 0.1824 . . . . . . . . . . . . . . . 0.2187 
'X-RAY DIFFRACTION' 2.48 2.58  . . 161 3498 100.00 . . . . 0.1893 . . . . . . . . . . . . . . . 0.2719 
'X-RAY DIFFRACTION' 2.58 2.69  . . 172 3514 100.00 . . . . 0.1932 . . . . . . . . . . . . . . . 0.2531 
'X-RAY DIFFRACTION' 2.69 2.83  . . 191 3506 100.00 . . . . 0.1885 . . . . . . . . . . . . . . . 0.2108 
'X-RAY DIFFRACTION' 2.83 3.01  . . 173 3487 100.00 . . . . 0.1856 . . . . . . . . . . . . . . . 0.2116 
'X-RAY DIFFRACTION' 3.01 3.24  . . 167 3523 100.00 . . . . 0.1814 . . . . . . . . . . . . . . . 0.2060 
'X-RAY DIFFRACTION' 3.25 3.57  . . 170 3514 100.00 . . . . 0.1672 . . . . . . . . . . . . . . . 0.2135 
'X-RAY DIFFRACTION' 3.57 4.09  . . 167 3510 100.00 . . . . 0.1475 . . . . . . . . . . . . . . . 0.2126 
'X-RAY DIFFRACTION' 4.09 5.15  . . 189 3465 100.00 . . . . 0.1438 . . . . . . . . . . . . . . . 0.1548 
'X-RAY DIFFRACTION' 5.15 57.94 . . 191 3503 100.00 . . . . 0.1876 . . . . . . . . . . . . . . . 0.2001 
# 
_struct.entry_id                     9OG8 
_struct.title                        'Crystal structure of WRN in complex with compound 43' 
_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        9OG8 
_struct_keywords.text            'Werner syndrome helicase, 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 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    WRN_HUMAN 
_struct_ref.pdbx_db_accession          Q14191 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DFLWPAPNEEQVTCLKMYFGHSSFKPVQWKVIHSVLEERRDNVAVMATGYGKSLCFQYPPVYVGKIGLVISPLISLMEDQ
VLQLKMSNIPACFLGSAQSENVLTDIKLGKYRIVYVTPEYCSGNMGLLQQLEADIGITLIAVDEAHCISEWGHDFRDSFR
KLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFDRPNLYLEVRRKTGNILQDLQPFLVKTSSHWEFEG
PTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDM
ESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRNEKFRLYKLKMMAKMEKYLHSSRCRRQIILSHFEDKQVQKA
SLGIMGTEKCCDNCRSRLDHC
;
_struct_ref.pdbx_align_begin           526 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9OG8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 4 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 424 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q14191 
_struct_ref_seq.db_align_beg                  526 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  946 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       526 
_struct_ref_seq.pdbx_auth_seq_align_end       946 
# 
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 9OG8 SER A 1 ? UNP Q14191 ? ? 'expression tag' 523 1 
1 9OG8 GLY A 2 ? UNP Q14191 ? ? 'expression tag' 524 2 
1 9OG8 SER A 3 ? UNP Q14191 ? ? 'expression tag' 525 3 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 11  ? GLY A 23  ? ASN A 533 GLY A 545 1 ? 13 
HELX_P HELX_P2  AA2 LYS A 28  ? ARG A 42  ? LYS A 550 ARG A 564 1 ? 15 
HELX_P HELX_P3  AA3 LYS A 55  ? GLY A 67  ? LYS A 577 GLY A 589 1 ? 13 
HELX_P HELX_P4  AA4 LEU A 76  ? SER A 90  ? LEU A 598 SER A 612 1 ? 15 
HELX_P HELX_P5  AA5 SER A 102 ? LEU A 111 ? SER A 624 LEU A 633 1 ? 10 
HELX_P HELX_P6  AA6 THR A 120 ? ASN A 127 ? THR A 642 ASN A 649 1 ? 8  
HELX_P HELX_P7  AA7 ASN A 127 ? ILE A 138 ? ASN A 649 ILE A 660 1 ? 12 
HELX_P HELX_P8  AA8 GLU A 147 ? SER A 152 ? GLU A 669 SER A 674 5 ? 6  
HELX_P HELX_P9  AA9 ARG A 159 ? GLY A 166 ? ARG A 681 GLY A 688 5 ? 8  
HELX_P HELX_P10 AB1 SER A 167 ? LEU A 172 ? SER A 689 LEU A 694 1 ? 6  
HELX_P HELX_P11 AB2 SER A 185 ? LEU A 196 ? SER A 707 LEU A 718 1 ? 12 
HELX_P HELX_P12 AB3 ASN A 223 ? GLN A 229 ? ASN A 745 GLN A 751 1 ? 7  
HELX_P HELX_P13 AB4 SER A 251 ? LYS A 264 ? SER A 773 LYS A 786 1 ? 14 
HELX_P HELX_P14 AB5 SER A 277 ? ARG A 290 ? SER A 799 ARG A 812 1 ? 14 
HELX_P HELX_P15 AB6 ILE A 300 ? MET A 304 ? ILE A 822 MET A 826 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 322 ? GLY A 331 ? ASP A 844 GLY A 853 1 ? 10 
HELX_P HELX_P17 AB8 ASP A 350 ? THR A 359 ? ASP A 872 THR A 881 5 ? 10 
HELX_P HELX_P18 AB9 ASN A 363 ? SER A 383 ? ASN A 885 SER A 905 1 ? 21 
HELX_P HELX_P19 AC1 CYS A 386 ? GLU A 396 ? CYS A 908 GLU A 918 1 ? 11 
HELX_P HELX_P20 AC2 ASP A 397 ? SER A 404 ? ASP A 919 SER A 926 1 ? 8  
HELX_P HELX_P21 AC3 CYS A 414 ? ASP A 422 ? CYS A 936 ASP A 944 1 ? 9  
# 
_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 
covale1 covale none ? A CYS 205 SG A ? ? 1_555 B A1CA5 . C39 ? ? A CYS 727 A A1CA5 1001 1_555 ? ? ? ? ? ? ? 1.428 ? ? 
metalc1 metalc ?    ? A CYS 386 SG ? ? ? 1_555 C ZN    . ZN  ? ? A CYS 908 A ZN    1002 1_555 ? ? ? ? ? ? ? 2.361 ? ? 
metalc2 metalc ?    ? A CYS 413 SG ? ? ? 1_555 C ZN    . ZN  ? ? A CYS 935 A ZN    1002 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc3 metalc ?    ? A CYS 414 SG ? ? ? 1_555 C ZN    . ZN  ? ? A CYS 936 A ZN    1002 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc4 metalc ?    ? A CYS 417 SG ? ? ? 1_555 C ZN    . ZN  ? ? A CYS 939 A ZN    1002 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
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 386 ? A CYS 908 ? 1_555 ZN ? C ZN . ? A ZN 1002 ? 1_555 SG ? A CYS 413 ? A CYS 935 ? 1_555 100.5 ? 
2 SG ? A CYS 386 ? A CYS 908 ? 1_555 ZN ? C ZN . ? A ZN 1002 ? 1_555 SG ? A CYS 414 ? A CYS 936 ? 1_555 116.2 ? 
3 SG ? A CYS 413 ? A CYS 935 ? 1_555 ZN ? C ZN . ? A ZN 1002 ? 1_555 SG ? A CYS 414 ? A CYS 936 ? 1_555 118.1 ? 
4 SG ? A CYS 386 ? A CYS 908 ? 1_555 ZN ? C ZN . ? A ZN 1002 ? 1_555 SG ? A CYS 417 ? A CYS 939 ? 1_555 101.7 ? 
5 SG ? A CYS 413 ? A CYS 935 ? 1_555 ZN ? C ZN . ? A ZN 1002 ? 1_555 SG ? A CYS 417 ? A CYS 939 ? 1_555 114.5 ? 
6 SG ? A CYS 414 ? A CYS 936 ? 1_555 ZN ? C ZN . ? A ZN 1002 ? 1_555 SG ? A CYS 417 ? A CYS 939 ? 1_555 105.0 ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      A1CA5 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      205 
_pdbx_modification_feature.modified_residue_label_alt_id      A 
_pdbx_modification_feature.auth_comp_id                       A1CA5 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        1001 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       727 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C39 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        A1CA5 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          TRP 
_struct_mon_prot_cis.label_seq_id           7 
_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           TRP 
_struct_mon_prot_cis.auth_seq_id            529 
_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    8 
_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     530 
_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       -3.48 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 6 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 94  ? PHE A 96  ? ALA A 616 PHE A 618 
AA1 2 ILE A 116 ? VAL A 119 ? ILE A 638 VAL A 641 
AA1 3 ILE A 69  ? ILE A 73  ? ILE A 591 ILE A 595 
AA1 4 ILE A 140 ? VAL A 145 ? ILE A 662 VAL A 667 
AA1 5 ILE A 177 ? THR A 181 ? ILE A 699 THR A 703 
AA1 6 ASN A 45  ? MET A 49  ? ASN A 567 MET A 571 
AA1 7 GLN A 202 ? THR A 206 ? GLN A 724 THR A 728 
AA2 1 LEU A 213 ? ARG A 219 ? LEU A 735 ARG A 741 
AA2 2 SER A 340 ? TRP A 346 ? SER A 862 TRP A 868 
AA2 3 GLN A 313 ? TYR A 317 ? GLN A 835 TYR A 839 
AA2 4 THR A 245 ? TYR A 248 ? THR A 767 TYR A 770 
AA2 5 CYS A 295 ? ALA A 298 ? CYS A 817 ALA A 820 
AA2 6 CYS A 269 ? TYR A 272 ? CYS A 791 TYR A 794 
AA3 1 LEU A 232 ? VAL A 233 ? LEU A 754 VAL A 755 
AA3 2 GLU A 240 ? PHE A 241 ? GLU A 762 PHE A 763 
# 
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 CYS A 95  ? N CYS A 617 O TYR A 118 ? O TYR A 640 
AA1 2 3 O VAL A 119 ? O VAL A 641 N VAL A 72  ? N VAL A 594 
AA1 3 4 N ILE A 73  ? N ILE A 595 O ALA A 144 ? O ALA A 666 
AA1 4 5 N VAL A 145 ? N VAL A 667 O LEU A 180 ? O LEU A 702 
AA1 5 6 O ALA A 179 ? O ALA A 701 N ASN A 45  ? N ASN A 567 
AA1 6 7 N VAL A 48  ? N VAL A 570 O THR A 204 ? O THR A 726 
AA2 1 2 N ARG A 218 ? N ARG A 740 O VAL A 344 ? O VAL A 866 
AA2 2 3 O LEU A 345 ? O LEU A 867 N HIS A 316 ? N HIS A 838 
AA2 3 4 O ILE A 315 ? O ILE A 837 N TYR A 248 ? N TYR A 770 
AA2 4 5 N ILE A 247 ? N ILE A 769 O VAL A 296 ? O VAL A 818 
AA2 5 6 O ILE A 297 ? O ILE A 819 N GLY A 270 ? N GLY A 792 
AA3 1 2 N VAL A 233 ? N VAL A 755 O GLU A 240 ? O GLU A 762 
# 
_pdbx_entry_details.entry_id                   9OG8 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            CYS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             791 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            SG 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            CYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             791 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.715 
_pdbx_validate_rmsd_bond.bond_target_value         1.812 
_pdbx_validate_rmsd_bond.bond_deviation            -0.097 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.016 
_pdbx_validate_rmsd_bond.linker_flag               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 LYS A 590 ? ? -114.46 -130.52 
2 1 ASN A 722 ? ? 39.67   55.40   
3 1 ASP A 832 ? ? -116.60 50.99   
4 1 ILE A 929 ? ? -122.90 -55.55  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     803 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.114 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 SER 758 ? A SER 236 
2 1 Y 1 A SER 759 ? A SER 237 
# 
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 
A1CA5 C4   C  N R 1   
A1CA5 C6   C  N N 2   
A1CA5 C7   C  N R 3   
A1CA5 C8   C  N N 4   
A1CA5 C10  C  N N 5   
A1CA5 C13  C  Y N 6   
A1CA5 C15  C  Y N 7   
A1CA5 C17  C  N N 8   
A1CA5 C21  C  N N 9   
A1CA5 C22  C  N N 10  
A1CA5 C26  C  N N 11  
A1CA5 C1   C  N N 12  
A1CA5 C11  C  N N 13  
A1CA5 C12  C  Y N 14  
A1CA5 C16  C  Y N 15  
A1CA5 C18  C  Y N 16  
A1CA5 C19  C  Y N 17  
A1CA5 C23  C  N S 18  
A1CA5 C25  C  N N 19  
A1CA5 C27  C  N N 20  
A1CA5 C29  C  N N 21  
A1CA5 C3   C  N N 22  
A1CA5 C31  C  Y N 23  
A1CA5 C32  C  Y N 24  
A1CA5 C33  C  Y N 25  
A1CA5 C34  C  Y N 26  
A1CA5 C38  C  N N 27  
A1CA5 C39  C  N N 28  
A1CA5 C41  C  Y N 29  
A1CA5 C42  C  Y N 30  
A1CA5 C46  C  N N 31  
A1CA5 C47  C  N N 32  
A1CA5 C48  C  N N 33  
A1CA5 C49  C  N N 34  
A1CA5 C50  C  N N 35  
A1CA5 C51  C  N N 36  
A1CA5 C52  C  N N 37  
A1CA5 F14  F  N N 38  
A1CA5 N2   N  N N 39  
A1CA5 N24  N  N N 40  
A1CA5 N28  N  N N 41  
A1CA5 N30  N  N N 42  
A1CA5 N35  N  N N 43  
A1CA5 N5   N  N N 44  
A1CA5 N9   N  N N 45  
A1CA5 O20  O  N N 46  
A1CA5 O37  O  N N 47  
A1CA5 O40  O  N N 48  
A1CA5 O43  O  N N 49  
A1CA5 O44  O  N N 50  
A1CA5 O45  O  N N 51  
A1CA5 O53  O  N N 52  
A1CA5 S36  S  N N 53  
A1CA5 H1   H  N N 54  
A1CA5 H2   H  N N 55  
A1CA5 H3   H  N N 56  
A1CA5 H4   H  N N 57  
A1CA5 H5   H  N N 58  
A1CA5 H6   H  N N 59  
A1CA5 H7   H  N N 60  
A1CA5 H8   H  N N 61  
A1CA5 H9   H  N N 62  
A1CA5 H10  H  N N 63  
A1CA5 H11  H  N N 64  
A1CA5 H12  H  N N 65  
A1CA5 H13  H  N N 66  
A1CA5 H14  H  N N 67  
A1CA5 H15  H  N N 68  
A1CA5 H16  H  N N 69  
A1CA5 H17  H  N N 70  
A1CA5 H18  H  N N 71  
A1CA5 H19  H  N N 72  
A1CA5 H20  H  N N 73  
A1CA5 H21  H  N N 74  
A1CA5 H22  H  N N 75  
A1CA5 H23  H  N N 76  
A1CA5 H24  H  N N 77  
A1CA5 H25  H  N N 78  
A1CA5 H26  H  N N 79  
A1CA5 H27  H  N N 80  
A1CA5 H28  H  N N 81  
A1CA5 H29  H  N N 82  
A1CA5 H30  H  N N 83  
A1CA5 H31  H  N N 84  
A1CA5 H32  H  N N 85  
A1CA5 H33  H  N N 86  
A1CA5 H34  H  N N 87  
A1CA5 H35  H  N N 88  
A1CA5 H36  H  N N 89  
A1CA5 H37  H  N N 90  
A1CA5 H38  H  N N 91  
A1CA5 H39  H  N N 92  
A1CA5 H40  H  N N 93  
A1CA5 H41  H  N N 94  
A1CA5 H42  H  N N 95  
A1CA5 H43  H  N N 96  
A1CA5 H44  H  N N 97  
A1CA5 H45  H  N N 98  
A1CA5 H46  H  N N 99  
A1CA5 H47  H  N N 100 
A1CA5 H48  H  N N 101 
A1CA5 H49  H  N N 102 
A1CA5 H50  H  N N 103 
ALA   N    N  N N 104 
ALA   CA   C  N S 105 
ALA   C    C  N N 106 
ALA   O    O  N N 107 
ALA   CB   C  N N 108 
ALA   OXT  O  N N 109 
ALA   H    H  N N 110 
ALA   H2   H  N N 111 
ALA   HA   H  N N 112 
ALA   HB1  H  N N 113 
ALA   HB2  H  N N 114 
ALA   HB3  H  N N 115 
ALA   HXT  H  N N 116 
ARG   N    N  N N 117 
ARG   CA   C  N S 118 
ARG   C    C  N N 119 
ARG   O    O  N N 120 
ARG   CB   C  N N 121 
ARG   CG   C  N N 122 
ARG   CD   C  N N 123 
ARG   NE   N  N N 124 
ARG   CZ   C  N N 125 
ARG   NH1  N  N N 126 
ARG   NH2  N  N N 127 
ARG   OXT  O  N N 128 
ARG   H    H  N N 129 
ARG   H2   H  N N 130 
ARG   HA   H  N N 131 
ARG   HB2  H  N N 132 
ARG   HB3  H  N N 133 
ARG   HG2  H  N N 134 
ARG   HG3  H  N N 135 
ARG   HD2  H  N N 136 
ARG   HD3  H  N N 137 
ARG   HE   H  N N 138 
ARG   HH11 H  N N 139 
ARG   HH12 H  N N 140 
ARG   HH21 H  N N 141 
ARG   HH22 H  N N 142 
ARG   HXT  H  N N 143 
ASN   N    N  N N 144 
ASN   CA   C  N S 145 
ASN   C    C  N N 146 
ASN   O    O  N N 147 
ASN   CB   C  N N 148 
ASN   CG   C  N N 149 
ASN   OD1  O  N N 150 
ASN   ND2  N  N N 151 
ASN   OXT  O  N N 152 
ASN   H    H  N N 153 
ASN   H2   H  N N 154 
ASN   HA   H  N N 155 
ASN   HB2  H  N N 156 
ASN   HB3  H  N N 157 
ASN   HD21 H  N N 158 
ASN   HD22 H  N N 159 
ASN   HXT  H  N N 160 
ASP   N    N  N N 161 
ASP   CA   C  N S 162 
ASP   C    C  N N 163 
ASP   O    O  N N 164 
ASP   CB   C  N N 165 
ASP   CG   C  N N 166 
ASP   OD1  O  N N 167 
ASP   OD2  O  N N 168 
ASP   OXT  O  N N 169 
ASP   H    H  N N 170 
ASP   H2   H  N N 171 
ASP   HA   H  N N 172 
ASP   HB2  H  N N 173 
ASP   HB3  H  N N 174 
ASP   HD2  H  N N 175 
ASP   HXT  H  N N 176 
CYS   N    N  N N 177 
CYS   CA   C  N R 178 
CYS   C    C  N N 179 
CYS   O    O  N N 180 
CYS   CB   C  N N 181 
CYS   SG   S  N N 182 
CYS   OXT  O  N N 183 
CYS   H    H  N N 184 
CYS   H2   H  N N 185 
CYS   HA   H  N N 186 
CYS   HB2  H  N N 187 
CYS   HB3  H  N N 188 
CYS   HG   H  N N 189 
CYS   HXT  H  N N 190 
GLN   N    N  N N 191 
GLN   CA   C  N S 192 
GLN   C    C  N N 193 
GLN   O    O  N N 194 
GLN   CB   C  N N 195 
GLN   CG   C  N N 196 
GLN   CD   C  N N 197 
GLN   OE1  O  N N 198 
GLN   NE2  N  N N 199 
GLN   OXT  O  N N 200 
GLN   H    H  N N 201 
GLN   H2   H  N N 202 
GLN   HA   H  N N 203 
GLN   HB2  H  N N 204 
GLN   HB3  H  N N 205 
GLN   HG2  H  N N 206 
GLN   HG3  H  N N 207 
GLN   HE21 H  N N 208 
GLN   HE22 H  N N 209 
GLN   HXT  H  N N 210 
GLU   N    N  N N 211 
GLU   CA   C  N S 212 
GLU   C    C  N N 213 
GLU   O    O  N N 214 
GLU   CB   C  N N 215 
GLU   CG   C  N N 216 
GLU   CD   C  N N 217 
GLU   OE1  O  N N 218 
GLU   OE2  O  N N 219 
GLU   OXT  O  N N 220 
GLU   H    H  N N 221 
GLU   H2   H  N N 222 
GLU   HA   H  N N 223 
GLU   HB2  H  N N 224 
GLU   HB3  H  N N 225 
GLU   HG2  H  N N 226 
GLU   HG3  H  N N 227 
GLU   HE2  H  N N 228 
GLU   HXT  H  N N 229 
GLY   N    N  N N 230 
GLY   CA   C  N N 231 
GLY   C    C  N N 232 
GLY   O    O  N N 233 
GLY   OXT  O  N N 234 
GLY   H    H  N N 235 
GLY   H2   H  N N 236 
GLY   HA2  H  N N 237 
GLY   HA3  H  N N 238 
GLY   HXT  H  N N 239 
HIS   N    N  N N 240 
HIS   CA   C  N S 241 
HIS   C    C  N N 242 
HIS   O    O  N N 243 
HIS   CB   C  N N 244 
HIS   CG   C  Y N 245 
HIS   ND1  N  Y N 246 
HIS   CD2  C  Y N 247 
HIS   CE1  C  Y N 248 
HIS   NE2  N  Y N 249 
HIS   OXT  O  N N 250 
HIS   H    H  N N 251 
HIS   H2   H  N N 252 
HIS   HA   H  N N 253 
HIS   HB2  H  N N 254 
HIS   HB3  H  N N 255 
HIS   HD1  H  N N 256 
HIS   HD2  H  N N 257 
HIS   HE1  H  N N 258 
HIS   HE2  H  N N 259 
HIS   HXT  H  N N 260 
HOH   O    O  N N 261 
HOH   H1   H  N N 262 
HOH   H2   H  N N 263 
ILE   N    N  N N 264 
ILE   CA   C  N S 265 
ILE   C    C  N N 266 
ILE   O    O  N N 267 
ILE   CB   C  N S 268 
ILE   CG1  C  N N 269 
ILE   CG2  C  N N 270 
ILE   CD1  C  N N 271 
ILE   OXT  O  N N 272 
ILE   H    H  N N 273 
ILE   H2   H  N N 274 
ILE   HA   H  N N 275 
ILE   HB   H  N N 276 
ILE   HG12 H  N N 277 
ILE   HG13 H  N N 278 
ILE   HG21 H  N N 279 
ILE   HG22 H  N N 280 
ILE   HG23 H  N N 281 
ILE   HD11 H  N N 282 
ILE   HD12 H  N N 283 
ILE   HD13 H  N N 284 
ILE   HXT  H  N N 285 
LEU   N    N  N N 286 
LEU   CA   C  N S 287 
LEU   C    C  N N 288 
LEU   O    O  N N 289 
LEU   CB   C  N N 290 
LEU   CG   C  N N 291 
LEU   CD1  C  N N 292 
LEU   CD2  C  N N 293 
LEU   OXT  O  N N 294 
LEU   H    H  N N 295 
LEU   H2   H  N N 296 
LEU   HA   H  N N 297 
LEU   HB2  H  N N 298 
LEU   HB3  H  N N 299 
LEU   HG   H  N N 300 
LEU   HD11 H  N N 301 
LEU   HD12 H  N N 302 
LEU   HD13 H  N N 303 
LEU   HD21 H  N N 304 
LEU   HD22 H  N N 305 
LEU   HD23 H  N N 306 
LEU   HXT  H  N N 307 
LYS   N    N  N N 308 
LYS   CA   C  N S 309 
LYS   C    C  N N 310 
LYS   O    O  N N 311 
LYS   CB   C  N N 312 
LYS   CG   C  N N 313 
LYS   CD   C  N N 314 
LYS   CE   C  N N 315 
LYS   NZ   N  N N 316 
LYS   OXT  O  N N 317 
LYS   H    H  N N 318 
LYS   H2   H  N N 319 
LYS   HA   H  N N 320 
LYS   HB2  H  N N 321 
LYS   HB3  H  N N 322 
LYS   HG2  H  N N 323 
LYS   HG3  H  N N 324 
LYS   HD2  H  N N 325 
LYS   HD3  H  N N 326 
LYS   HE2  H  N N 327 
LYS   HE3  H  N N 328 
LYS   HZ1  H  N N 329 
LYS   HZ2  H  N N 330 
LYS   HZ3  H  N N 331 
LYS   HXT  H  N N 332 
MET   N    N  N N 333 
MET   CA   C  N S 334 
MET   C    C  N N 335 
MET   O    O  N N 336 
MET   CB   C  N N 337 
MET   CG   C  N N 338 
MET   SD   S  N N 339 
MET   CE   C  N N 340 
MET   OXT  O  N N 341 
MET   H    H  N N 342 
MET   H2   H  N N 343 
MET   HA   H  N N 344 
MET   HB2  H  N N 345 
MET   HB3  H  N N 346 
MET   HG2  H  N N 347 
MET   HG3  H  N N 348 
MET   HE1  H  N N 349 
MET   HE2  H  N N 350 
MET   HE3  H  N N 351 
MET   HXT  H  N N 352 
PHE   N    N  N N 353 
PHE   CA   C  N S 354 
PHE   C    C  N N 355 
PHE   O    O  N N 356 
PHE   CB   C  N N 357 
PHE   CG   C  Y N 358 
PHE   CD1  C  Y N 359 
PHE   CD2  C  Y N 360 
PHE   CE1  C  Y N 361 
PHE   CE2  C  Y N 362 
PHE   CZ   C  Y N 363 
PHE   OXT  O  N N 364 
PHE   H    H  N N 365 
PHE   H2   H  N N 366 
PHE   HA   H  N N 367 
PHE   HB2  H  N N 368 
PHE   HB3  H  N N 369 
PHE   HD1  H  N N 370 
PHE   HD2  H  N N 371 
PHE   HE1  H  N N 372 
PHE   HE2  H  N N 373 
PHE   HZ   H  N N 374 
PHE   HXT  H  N N 375 
PRO   N    N  N N 376 
PRO   CA   C  N S 377 
PRO   C    C  N N 378 
PRO   O    O  N N 379 
PRO   CB   C  N N 380 
PRO   CG   C  N N 381 
PRO   CD   C  N N 382 
PRO   OXT  O  N N 383 
PRO   H    H  N N 384 
PRO   HA   H  N N 385 
PRO   HB2  H  N N 386 
PRO   HB3  H  N N 387 
PRO   HG2  H  N N 388 
PRO   HG3  H  N N 389 
PRO   HD2  H  N N 390 
PRO   HD3  H  N N 391 
PRO   HXT  H  N N 392 
SER   N    N  N N 393 
SER   CA   C  N S 394 
SER   C    C  N N 395 
SER   O    O  N N 396 
SER   CB   C  N N 397 
SER   OG   O  N N 398 
SER   OXT  O  N N 399 
SER   H    H  N N 400 
SER   H2   H  N N 401 
SER   HA   H  N N 402 
SER   HB2  H  N N 403 
SER   HB3  H  N N 404 
SER   HG   H  N N 405 
SER   HXT  H  N N 406 
THR   N    N  N N 407 
THR   CA   C  N S 408 
THR   C    C  N N 409 
THR   O    O  N N 410 
THR   CB   C  N R 411 
THR   OG1  O  N N 412 
THR   CG2  C  N N 413 
THR   OXT  O  N N 414 
THR   H    H  N N 415 
THR   H2   H  N N 416 
THR   HA   H  N N 417 
THR   HB   H  N N 418 
THR   HG1  H  N N 419 
THR   HG21 H  N N 420 
THR   HG22 H  N N 421 
THR   HG23 H  N N 422 
THR   HXT  H  N N 423 
TRP   N    N  N N 424 
TRP   CA   C  N S 425 
TRP   C    C  N N 426 
TRP   O    O  N N 427 
TRP   CB   C  N N 428 
TRP   CG   C  Y N 429 
TRP   CD1  C  Y N 430 
TRP   CD2  C  Y N 431 
TRP   NE1  N  Y N 432 
TRP   CE2  C  Y N 433 
TRP   CE3  C  Y N 434 
TRP   CZ2  C  Y N 435 
TRP   CZ3  C  Y N 436 
TRP   CH2  C  Y N 437 
TRP   OXT  O  N N 438 
TRP   H    H  N N 439 
TRP   H2   H  N N 440 
TRP   HA   H  N N 441 
TRP   HB2  H  N N 442 
TRP   HB3  H  N N 443 
TRP   HD1  H  N N 444 
TRP   HE1  H  N N 445 
TRP   HE3  H  N N 446 
TRP   HZ2  H  N N 447 
TRP   HZ3  H  N N 448 
TRP   HH2  H  N N 449 
TRP   HXT  H  N N 450 
TYR   N    N  N N 451 
TYR   CA   C  N S 452 
TYR   C    C  N N 453 
TYR   O    O  N N 454 
TYR   CB   C  N N 455 
TYR   CG   C  Y N 456 
TYR   CD1  C  Y N 457 
TYR   CD2  C  Y N 458 
TYR   CE1  C  Y N 459 
TYR   CE2  C  Y N 460 
TYR   CZ   C  Y N 461 
TYR   OH   O  N N 462 
TYR   OXT  O  N N 463 
TYR   H    H  N N 464 
TYR   H2   H  N N 465 
TYR   HA   H  N N 466 
TYR   HB2  H  N N 467 
TYR   HB3  H  N N 468 
TYR   HD1  H  N N 469 
TYR   HD2  H  N N 470 
TYR   HE1  H  N N 471 
TYR   HE2  H  N N 472 
TYR   HH   H  N N 473 
TYR   HXT  H  N N 474 
VAL   N    N  N N 475 
VAL   CA   C  N S 476 
VAL   C    C  N N 477 
VAL   O    O  N N 478 
VAL   CB   C  N N 479 
VAL   CG1  C  N N 480 
VAL   CG2  C  N N 481 
VAL   OXT  O  N N 482 
VAL   H    H  N N 483 
VAL   H2   H  N N 484 
VAL   HA   H  N N 485 
VAL   HB   H  N N 486 
VAL   HG11 H  N N 487 
VAL   HG12 H  N N 488 
VAL   HG13 H  N N 489 
VAL   HG21 H  N N 490 
VAL   HG22 H  N N 491 
VAL   HG23 H  N N 492 
VAL   HXT  H  N N 493 
ZN    ZN   ZN N N 494 
# 
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 
A1CA5 O40 S36  doub N N 1   
A1CA5 O37 S36  doub N N 2   
A1CA5 S36 C38  sing N N 3   
A1CA5 S36 N35  sing N N 4   
A1CA5 C39 C38  sing N N 5   
A1CA5 N35 C34  sing N N 6   
A1CA5 C41 C34  doub Y N 7   
A1CA5 C41 C42  sing Y N 8   
A1CA5 C34 C33  sing Y N 9   
A1CA5 C42 C31  doub Y N 10  
A1CA5 C33 C32  doub Y N 11  
A1CA5 F14 C13  sing N N 12  
A1CA5 C22 C23  sing N N 13  
A1CA5 C22 C21  sing N N 14  
A1CA5 C15 C13  doub Y N 15  
A1CA5 C15 C16  sing Y N 16  
A1CA5 O44 C25  doub N N 17  
A1CA5 O53 C3   doub N N 18  
A1CA5 C13 C12  sing Y N 19  
A1CA5 C23 C7   sing N N 20  
A1CA5 C23 N24  sing N N 21  
A1CA5 C31 C32  sing Y N 22  
A1CA5 C31 N30  sing N N 23  
A1CA5 C32 N28  sing N N 24  
A1CA5 C17 C16  sing N N 25  
A1CA5 O20 C10  doub N N 26  
A1CA5 C21 N9   sing N N 27  
A1CA5 C16 C18  doub Y N 28  
A1CA5 C48 C49  sing N N 29  
A1CA5 C48 C47  sing N N 30  
A1CA5 C7  C6   sing N N 31  
A1CA5 C7  C8   sing N N 32  
A1CA5 C10 N9   sing N N 33  
A1CA5 C10 C11  sing N N 34  
A1CA5 N5  C4   sing N N 35  
A1CA5 N5  C6   sing N N 36  
A1CA5 C46 C47  sing N N 37  
A1CA5 C46 C4   sing N N 38  
A1CA5 C25 N24  sing N N 39  
A1CA5 C25 C26  sing N N 40  
A1CA5 N9  C8   sing N N 41  
A1CA5 C3  C4   sing N N 42  
A1CA5 C3  N2   sing N N 43  
A1CA5 C49 C50  sing N N 44  
A1CA5 C12 C11  sing N N 45  
A1CA5 C12 C19  doub Y N 46  
A1CA5 C47 C52  sing N N 47  
A1CA5 N30 C29  sing N N 48  
A1CA5 N28 C27  sing N N 49  
A1CA5 N28 C29  sing N N 50  
A1CA5 C6  O45  doub N N 51  
A1CA5 C18 C19  sing Y N 52  
A1CA5 C1  N2   sing N N 53  
A1CA5 C27 C26  sing N N 54  
A1CA5 C29 O43  doub N N 55  
A1CA5 C50 C51  sing N N 56  
A1CA5 C52 C51  sing N N 57  
A1CA5 C4  H1   sing N N 58  
A1CA5 C7  H2   sing N N 59  
A1CA5 C8  H3   sing N N 60  
A1CA5 C8  H4   sing N N 61  
A1CA5 C15 H5   sing N N 62  
A1CA5 C17 H6   sing N N 63  
A1CA5 C17 H7   sing N N 64  
A1CA5 C17 H8   sing N N 65  
A1CA5 C21 H9   sing N N 66  
A1CA5 C21 H10  sing N N 67  
A1CA5 C22 H11  sing N N 68  
A1CA5 C22 H12  sing N N 69  
A1CA5 C26 H13  sing N N 70  
A1CA5 C26 H14  sing N N 71  
A1CA5 C1  H15  sing N N 72  
A1CA5 C1  H16  sing N N 73  
A1CA5 C1  H17  sing N N 74  
A1CA5 C11 H18  sing N N 75  
A1CA5 C11 H19  sing N N 76  
A1CA5 C18 H20  sing N N 77  
A1CA5 C19 H21  sing N N 78  
A1CA5 C23 H22  sing N N 79  
A1CA5 C27 H23  sing N N 80  
A1CA5 C27 H24  sing N N 81  
A1CA5 C33 H25  sing N N 82  
A1CA5 C38 H26  sing N N 83  
A1CA5 C38 H27  sing N N 84  
A1CA5 C39 H28  sing N N 85  
A1CA5 C39 H29  sing N N 86  
A1CA5 C39 H30  sing N N 87  
A1CA5 C41 H31  sing N N 88  
A1CA5 C42 H32  sing N N 89  
A1CA5 C46 H33  sing N N 90  
A1CA5 C46 H34  sing N N 91  
A1CA5 C47 H35  sing N N 92  
A1CA5 C48 H36  sing N N 93  
A1CA5 C48 H37  sing N N 94  
A1CA5 C49 H38  sing N N 95  
A1CA5 C49 H39  sing N N 96  
A1CA5 C50 H40  sing N N 97  
A1CA5 C50 H41  sing N N 98  
A1CA5 C51 H42  sing N N 99  
A1CA5 C51 H43  sing N N 100 
A1CA5 C52 H44  sing N N 101 
A1CA5 C52 H45  sing N N 102 
A1CA5 N2  H46  sing N N 103 
A1CA5 N24 H47  sing N N 104 
A1CA5 N30 H48  sing N N 105 
A1CA5 N35 H49  sing N N 106 
A1CA5 N5  H50  sing N N 107 
ALA   N   CA   sing N N 108 
ALA   N   H    sing N N 109 
ALA   N   H2   sing N N 110 
ALA   CA  C    sing N N 111 
ALA   CA  CB   sing N N 112 
ALA   CA  HA   sing N N 113 
ALA   C   O    doub N N 114 
ALA   C   OXT  sing N N 115 
ALA   CB  HB1  sing N N 116 
ALA   CB  HB2  sing N N 117 
ALA   CB  HB3  sing N N 118 
ALA   OXT HXT  sing N N 119 
ARG   N   CA   sing N N 120 
ARG   N   H    sing N N 121 
ARG   N   H2   sing N N 122 
ARG   CA  C    sing N N 123 
ARG   CA  CB   sing N N 124 
ARG   CA  HA   sing N N 125 
ARG   C   O    doub N N 126 
ARG   C   OXT  sing N N 127 
ARG   CB  CG   sing N N 128 
ARG   CB  HB2  sing N N 129 
ARG   CB  HB3  sing N N 130 
ARG   CG  CD   sing N N 131 
ARG   CG  HG2  sing N N 132 
ARG   CG  HG3  sing N N 133 
ARG   CD  NE   sing N N 134 
ARG   CD  HD2  sing N N 135 
ARG   CD  HD3  sing N N 136 
ARG   NE  CZ   sing N N 137 
ARG   NE  HE   sing N N 138 
ARG   CZ  NH1  sing N N 139 
ARG   CZ  NH2  doub N N 140 
ARG   NH1 HH11 sing N N 141 
ARG   NH1 HH12 sing N N 142 
ARG   NH2 HH21 sing N N 143 
ARG   NH2 HH22 sing N N 144 
ARG   OXT HXT  sing N N 145 
ASN   N   CA   sing N N 146 
ASN   N   H    sing N N 147 
ASN   N   H2   sing N N 148 
ASN   CA  C    sing N N 149 
ASN   CA  CB   sing N N 150 
ASN   CA  HA   sing N N 151 
ASN   C   O    doub N N 152 
ASN   C   OXT  sing N N 153 
ASN   CB  CG   sing N N 154 
ASN   CB  HB2  sing N N 155 
ASN   CB  HB3  sing N N 156 
ASN   CG  OD1  doub N N 157 
ASN   CG  ND2  sing N N 158 
ASN   ND2 HD21 sing N N 159 
ASN   ND2 HD22 sing N N 160 
ASN   OXT HXT  sing N N 161 
ASP   N   CA   sing N N 162 
ASP   N   H    sing N N 163 
ASP   N   H2   sing N N 164 
ASP   CA  C    sing N N 165 
ASP   CA  CB   sing N N 166 
ASP   CA  HA   sing N N 167 
ASP   C   O    doub N N 168 
ASP   C   OXT  sing N N 169 
ASP   CB  CG   sing N N 170 
ASP   CB  HB2  sing N N 171 
ASP   CB  HB3  sing N N 172 
ASP   CG  OD1  doub N N 173 
ASP   CG  OD2  sing N N 174 
ASP   OD2 HD2  sing N N 175 
ASP   OXT HXT  sing N N 176 
CYS   N   CA   sing N N 177 
CYS   N   H    sing N N 178 
CYS   N   H2   sing N N 179 
CYS   CA  C    sing N N 180 
CYS   CA  CB   sing N N 181 
CYS   CA  HA   sing N N 182 
CYS   C   O    doub N N 183 
CYS   C   OXT  sing N N 184 
CYS   CB  SG   sing N N 185 
CYS   CB  HB2  sing N N 186 
CYS   CB  HB3  sing N N 187 
CYS   SG  HG   sing N N 188 
CYS   OXT HXT  sing N N 189 
GLN   N   CA   sing N N 190 
GLN   N   H    sing N N 191 
GLN   N   H2   sing N N 192 
GLN   CA  C    sing N N 193 
GLN   CA  CB   sing N N 194 
GLN   CA  HA   sing N N 195 
GLN   C   O    doub N N 196 
GLN   C   OXT  sing N N 197 
GLN   CB  CG   sing N N 198 
GLN   CB  HB2  sing N N 199 
GLN   CB  HB3  sing N N 200 
GLN   CG  CD   sing N N 201 
GLN   CG  HG2  sing N N 202 
GLN   CG  HG3  sing N N 203 
GLN   CD  OE1  doub N N 204 
GLN   CD  NE2  sing N N 205 
GLN   NE2 HE21 sing N N 206 
GLN   NE2 HE22 sing N N 207 
GLN   OXT HXT  sing N N 208 
GLU   N   CA   sing N N 209 
GLU   N   H    sing N N 210 
GLU   N   H2   sing N N 211 
GLU   CA  C    sing N N 212 
GLU   CA  CB   sing N N 213 
GLU   CA  HA   sing N N 214 
GLU   C   O    doub N N 215 
GLU   C   OXT  sing N N 216 
GLU   CB  CG   sing N N 217 
GLU   CB  HB2  sing N N 218 
GLU   CB  HB3  sing N N 219 
GLU   CG  CD   sing N N 220 
GLU   CG  HG2  sing N N 221 
GLU   CG  HG3  sing N N 222 
GLU   CD  OE1  doub N N 223 
GLU   CD  OE2  sing N N 224 
GLU   OE2 HE2  sing N N 225 
GLU   OXT HXT  sing N N 226 
GLY   N   CA   sing N N 227 
GLY   N   H    sing N N 228 
GLY   N   H2   sing N N 229 
GLY   CA  C    sing N N 230 
GLY   CA  HA2  sing N N 231 
GLY   CA  HA3  sing N N 232 
GLY   C   O    doub N N 233 
GLY   C   OXT  sing N N 234 
GLY   OXT HXT  sing N N 235 
HIS   N   CA   sing N N 236 
HIS   N   H    sing N N 237 
HIS   N   H2   sing N N 238 
HIS   CA  C    sing N N 239 
HIS   CA  CB   sing N N 240 
HIS   CA  HA   sing N N 241 
HIS   C   O    doub N N 242 
HIS   C   OXT  sing N N 243 
HIS   CB  CG   sing N N 244 
HIS   CB  HB2  sing N N 245 
HIS   CB  HB3  sing N N 246 
HIS   CG  ND1  sing Y N 247 
HIS   CG  CD2  doub Y N 248 
HIS   ND1 CE1  doub Y N 249 
HIS   ND1 HD1  sing N N 250 
HIS   CD2 NE2  sing Y N 251 
HIS   CD2 HD2  sing N N 252 
HIS   CE1 NE2  sing Y N 253 
HIS   CE1 HE1  sing N N 254 
HIS   NE2 HE2  sing N N 255 
HIS   OXT HXT  sing N N 256 
HOH   O   H1   sing N N 257 
HOH   O   H2   sing N N 258 
ILE   N   CA   sing N N 259 
ILE   N   H    sing N N 260 
ILE   N   H2   sing N N 261 
ILE   CA  C    sing N N 262 
ILE   CA  CB   sing N N 263 
ILE   CA  HA   sing N N 264 
ILE   C   O    doub N N 265 
ILE   C   OXT  sing N N 266 
ILE   CB  CG1  sing N N 267 
ILE   CB  CG2  sing N N 268 
ILE   CB  HB   sing N N 269 
ILE   CG1 CD1  sing N N 270 
ILE   CG1 HG12 sing N N 271 
ILE   CG1 HG13 sing N N 272 
ILE   CG2 HG21 sing N N 273 
ILE   CG2 HG22 sing N N 274 
ILE   CG2 HG23 sing N N 275 
ILE   CD1 HD11 sing N N 276 
ILE   CD1 HD12 sing N N 277 
ILE   CD1 HD13 sing N N 278 
ILE   OXT HXT  sing N N 279 
LEU   N   CA   sing N N 280 
LEU   N   H    sing N N 281 
LEU   N   H2   sing N N 282 
LEU   CA  C    sing N N 283 
LEU   CA  CB   sing N N 284 
LEU   CA  HA   sing N N 285 
LEU   C   O    doub N N 286 
LEU   C   OXT  sing N N 287 
LEU   CB  CG   sing N N 288 
LEU   CB  HB2  sing N N 289 
LEU   CB  HB3  sing N N 290 
LEU   CG  CD1  sing N N 291 
LEU   CG  CD2  sing N N 292 
LEU   CG  HG   sing N N 293 
LEU   CD1 HD11 sing N N 294 
LEU   CD1 HD12 sing N N 295 
LEU   CD1 HD13 sing N N 296 
LEU   CD2 HD21 sing N N 297 
LEU   CD2 HD22 sing N N 298 
LEU   CD2 HD23 sing N N 299 
LEU   OXT HXT  sing N N 300 
LYS   N   CA   sing N N 301 
LYS   N   H    sing N N 302 
LYS   N   H2   sing N N 303 
LYS   CA  C    sing N N 304 
LYS   CA  CB   sing N N 305 
LYS   CA  HA   sing N N 306 
LYS   C   O    doub N N 307 
LYS   C   OXT  sing N N 308 
LYS   CB  CG   sing N N 309 
LYS   CB  HB2  sing N N 310 
LYS   CB  HB3  sing N N 311 
LYS   CG  CD   sing N N 312 
LYS   CG  HG2  sing N N 313 
LYS   CG  HG3  sing N N 314 
LYS   CD  CE   sing N N 315 
LYS   CD  HD2  sing N N 316 
LYS   CD  HD3  sing N N 317 
LYS   CE  NZ   sing N N 318 
LYS   CE  HE2  sing N N 319 
LYS   CE  HE3  sing N N 320 
LYS   NZ  HZ1  sing N N 321 
LYS   NZ  HZ2  sing N N 322 
LYS   NZ  HZ3  sing N N 323 
LYS   OXT HXT  sing N N 324 
MET   N   CA   sing N N 325 
MET   N   H    sing N N 326 
MET   N   H2   sing N N 327 
MET   CA  C    sing N N 328 
MET   CA  CB   sing N N 329 
MET   CA  HA   sing N N 330 
MET   C   O    doub N N 331 
MET   C   OXT  sing N N 332 
MET   CB  CG   sing N N 333 
MET   CB  HB2  sing N N 334 
MET   CB  HB3  sing N N 335 
MET   CG  SD   sing N N 336 
MET   CG  HG2  sing N N 337 
MET   CG  HG3  sing N N 338 
MET   SD  CE   sing N N 339 
MET   CE  HE1  sing N N 340 
MET   CE  HE2  sing N N 341 
MET   CE  HE3  sing N N 342 
MET   OXT HXT  sing N N 343 
PHE   N   CA   sing N N 344 
PHE   N   H    sing N N 345 
PHE   N   H2   sing N N 346 
PHE   CA  C    sing N N 347 
PHE   CA  CB   sing N N 348 
PHE   CA  HA   sing N N 349 
PHE   C   O    doub N N 350 
PHE   C   OXT  sing N N 351 
PHE   CB  CG   sing N N 352 
PHE   CB  HB2  sing N N 353 
PHE   CB  HB3  sing N N 354 
PHE   CG  CD1  doub Y N 355 
PHE   CG  CD2  sing Y N 356 
PHE   CD1 CE1  sing Y N 357 
PHE   CD1 HD1  sing N N 358 
PHE   CD2 CE2  doub Y N 359 
PHE   CD2 HD2  sing N N 360 
PHE   CE1 CZ   doub Y N 361 
PHE   CE1 HE1  sing N N 362 
PHE   CE2 CZ   sing Y N 363 
PHE   CE2 HE2  sing N N 364 
PHE   CZ  HZ   sing N N 365 
PHE   OXT HXT  sing N N 366 
PRO   N   CA   sing N N 367 
PRO   N   CD   sing N N 368 
PRO   N   H    sing N N 369 
PRO   CA  C    sing N N 370 
PRO   CA  CB   sing N N 371 
PRO   CA  HA   sing N N 372 
PRO   C   O    doub N N 373 
PRO   C   OXT  sing N N 374 
PRO   CB  CG   sing N N 375 
PRO   CB  HB2  sing N N 376 
PRO   CB  HB3  sing N N 377 
PRO   CG  CD   sing N N 378 
PRO   CG  HG2  sing N N 379 
PRO   CG  HG3  sing N N 380 
PRO   CD  HD2  sing N N 381 
PRO   CD  HD3  sing N N 382 
PRO   OXT HXT  sing N N 383 
SER   N   CA   sing N N 384 
SER   N   H    sing N N 385 
SER   N   H2   sing N N 386 
SER   CA  C    sing N N 387 
SER   CA  CB   sing N N 388 
SER   CA  HA   sing N N 389 
SER   C   O    doub N N 390 
SER   C   OXT  sing N N 391 
SER   CB  OG   sing N N 392 
SER   CB  HB2  sing N N 393 
SER   CB  HB3  sing N N 394 
SER   OG  HG   sing N N 395 
SER   OXT HXT  sing N N 396 
THR   N   CA   sing N N 397 
THR   N   H    sing N N 398 
THR   N   H2   sing N N 399 
THR   CA  C    sing N N 400 
THR   CA  CB   sing N N 401 
THR   CA  HA   sing N N 402 
THR   C   O    doub N N 403 
THR   C   OXT  sing N N 404 
THR   CB  OG1  sing N N 405 
THR   CB  CG2  sing N N 406 
THR   CB  HB   sing N N 407 
THR   OG1 HG1  sing N N 408 
THR   CG2 HG21 sing N N 409 
THR   CG2 HG22 sing N N 410 
THR   CG2 HG23 sing N N 411 
THR   OXT HXT  sing N N 412 
TRP   N   CA   sing N N 413 
TRP   N   H    sing N N 414 
TRP   N   H2   sing N N 415 
TRP   CA  C    sing N N 416 
TRP   CA  CB   sing N N 417 
TRP   CA  HA   sing N N 418 
TRP   C   O    doub N N 419 
TRP   C   OXT  sing N N 420 
TRP   CB  CG   sing N N 421 
TRP   CB  HB2  sing N N 422 
TRP   CB  HB3  sing N N 423 
TRP   CG  CD1  doub Y N 424 
TRP   CG  CD2  sing Y N 425 
TRP   CD1 NE1  sing Y N 426 
TRP   CD1 HD1  sing N N 427 
TRP   CD2 CE2  doub Y N 428 
TRP   CD2 CE3  sing Y N 429 
TRP   NE1 CE2  sing Y N 430 
TRP   NE1 HE1  sing N N 431 
TRP   CE2 CZ2  sing Y N 432 
TRP   CE3 CZ3  doub Y N 433 
TRP   CE3 HE3  sing N N 434 
TRP   CZ2 CH2  doub Y N 435 
TRP   CZ2 HZ2  sing N N 436 
TRP   CZ3 CH2  sing Y N 437 
TRP   CZ3 HZ3  sing N N 438 
TRP   CH2 HH2  sing N N 439 
TRP   OXT HXT  sing N N 440 
TYR   N   CA   sing N N 441 
TYR   N   H    sing N N 442 
TYR   N   H2   sing N N 443 
TYR   CA  C    sing N N 444 
TYR   CA  CB   sing N N 445 
TYR   CA  HA   sing N N 446 
TYR   C   O    doub N N 447 
TYR   C   OXT  sing N N 448 
TYR   CB  CG   sing N N 449 
TYR   CB  HB2  sing N N 450 
TYR   CB  HB3  sing N N 451 
TYR   CG  CD1  doub Y N 452 
TYR   CG  CD2  sing Y N 453 
TYR   CD1 CE1  sing Y N 454 
TYR   CD1 HD1  sing N N 455 
TYR   CD2 CE2  doub Y N 456 
TYR   CD2 HD2  sing N N 457 
TYR   CE1 CZ   doub Y N 458 
TYR   CE1 HE1  sing N N 459 
TYR   CE2 CZ   sing Y N 460 
TYR   CE2 HE2  sing N N 461 
TYR   CZ  OH   sing N N 462 
TYR   OH  HH   sing N N 463 
TYR   OXT HXT  sing N N 464 
VAL   N   CA   sing N N 465 
VAL   N   H    sing N N 466 
VAL   N   H2   sing N N 467 
VAL   CA  C    sing N N 468 
VAL   CA  CB   sing N N 469 
VAL   CA  HA   sing N N 470 
VAL   C   O    doub N N 471 
VAL   C   OXT  sing N N 472 
VAL   CB  CG1  sing N N 473 
VAL   CB  CG2  sing N N 474 
VAL   CB  HB   sing N N 475 
VAL   CG1 HG11 sing N N 476 
VAL   CG1 HG12 sing N N 477 
VAL   CG1 HG13 sing N N 478 
VAL   CG2 HG21 sing N N 479 
VAL   CG2 HG22 sing N N 480 
VAL   CG2 HG23 sing N N 481 
VAL   OXT HXT  sing N N 482 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'previous in-house structure' 
# 
_atom_sites.entry_id                    9OG8 
_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]   0.015397 
_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]   0.014537 
_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]   0.009306 
_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 
C  
F  
N  
O  
S  
ZN 
# 
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   . SER   A 1 1   ? 15.885 9.849   2.818   1.00 46.54 ? 523  SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 16.114 10.766  1.706   1.00 48.98 ? 523  SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 16.866 12.021  2.165   1.00 40.42 ? 523  SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 17.156 12.173  3.346   1.00 44.97 ? 523  SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 14.787 11.156  1.071   1.00 37.94 ? 523  SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 14.003 11.839  2.029   1.00 54.35 ? 523  SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 17.171 12.913  1.225   1.00 41.99 ? 524  GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 17.883 14.145  1.529   1.00 40.06 ? 524  GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 19.190 13.901  2.259   1.00 43.86 ? 524  GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.166 13.414  1.672   1.00 35.73 ? 524  GLY   A O   1 
ATOM   11   N  N   . SER   A 1 3   ? 19.215 14.214  3.556   1.00 39.31 ? 525  SER   A N   1 
ATOM   12   C  CA  . SER   A 1 3   ? 20.402 14.030  4.380   1.00 42.39 ? 525  SER   A CA  1 
ATOM   13   C  C   . SER   A 1 3   ? 20.253 12.921  5.427   1.00 42.09 ? 525  SER   A C   1 
ATOM   14   O  O   . SER   A 1 3   ? 21.157 12.751  6.249   1.00 41.58 ? 525  SER   A O   1 
ATOM   15   C  CB  . SER   A 1 3   ? 20.770 15.366  5.048   1.00 40.99 ? 525  SER   A CB  1 
ATOM   16   O  OG  . SER   A 1 3   ? 19.627 16.029  5.577   1.00 40.28 ? 525  SER   A OG  1 
ATOM   17   N  N   . ASP   A 1 4   ? 19.181 12.117  5.366   1.00 31.33 ? 526  ASP   A N   1 
ATOM   18   C  CA  . ASP   A 1 4   ? 18.662 11.424  6.551   1.00 26.80 ? 526  ASP   A CA  1 
ATOM   19   C  C   . ASP   A 1 4   ? 19.661 10.450  7.182   1.00 32.30 ? 526  ASP   A C   1 
ATOM   20   O  O   . ASP   A 1 4   ? 20.013 10.563  8.364   1.00 38.87 ? 526  ASP   A O   1 
ATOM   21   C  CB  . ASP   A 1 4   ? 17.392 10.672  6.174   1.00 32.64 ? 526  ASP   A CB  1 
ATOM   22   C  CG  . ASP   A 1 4   ? 16.152 11.468  6.461   1.00 46.15 ? 526  ASP   A CG  1 
ATOM   23   O  OD1 . ASP   A 1 4   ? 16.284 12.466  7.197   1.00 42.57 ? 526  ASP   A OD1 1 
ATOM   24   O  OD2 . ASP   A 1 4   ? 15.063 11.092  5.959   1.00 47.46 ? 526  ASP   A OD2 1 
ATOM   25   N  N   . PHE   A 1 5   ? 20.061 9.451   6.436   1.00 19.55 ? 527  PHE   A N   1 
ATOM   26   C  CA  . PHE   A 1 5   ? 20.775 8.289   6.976   1.00 20.96 ? 527  PHE   A CA  1 
ATOM   27   C  C   . PHE   A 1 5   ? 22.225 8.269   6.504   1.00 22.07 ? 527  PHE   A C   1 
ATOM   28   O  O   . PHE   A 1 5   ? 22.791 7.210   6.217   1.00 23.72 ? 527  PHE   A O   1 
ATOM   29   C  CB  . PHE   A 1 5   ? 20.059 6.999   6.583   1.00 20.90 ? 527  PHE   A CB  1 
ATOM   30   C  CG  . PHE   A 1 5   ? 18.614 7.001   6.926   1.00 21.61 ? 527  PHE   A CG  1 
ATOM   31   C  CD1 . PHE   A 1 5   ? 18.203 6.751   8.214   1.00 20.16 ? 527  PHE   A CD1 1 
ATOM   32   C  CD2 . PHE   A 1 5   ? 17.662 7.307   5.969   1.00 28.72 ? 527  PHE   A CD2 1 
ATOM   33   C  CE1 . PHE   A 1 5   ? 16.860 6.776   8.554   1.00 19.17 ? 527  PHE   A CE1 1 
ATOM   34   C  CE2 . PHE   A 1 5   ? 16.307 7.343   6.295   1.00 33.49 ? 527  PHE   A CE2 1 
ATOM   35   C  CZ  . PHE   A 1 5   ? 15.909 7.087   7.594   1.00 29.63 ? 527  PHE   A CZ  1 
ATOM   36   N  N   . LEU   A 1 6   ? 22.842 9.447   6.414   1.00 18.72 ? 528  LEU   A N   1 
ATOM   37   C  CA  . LEU   A 1 6   ? 24.193 9.568   5.886   1.00 18.67 ? 528  LEU   A CA  1 
ATOM   38   C  C   . LEU   A 1 6   ? 25.033 10.407  6.827   1.00 23.09 ? 528  LEU   A C   1 
ATOM   39   O  O   . LEU   A 1 6   ? 24.556 11.419  7.345   1.00 24.23 ? 528  LEU   A O   1 
ATOM   40   C  CB  . LEU   A 1 6   ? 24.173 10.208  4.498   1.00 23.50 ? 528  LEU   A CB  1 
ATOM   41   C  CG  . LEU   A 1 6   ? 23.366 9.472   3.422   1.00 20.27 ? 528  LEU   A CG  1 
ATOM   42   C  CD1 . LEU   A 1 6   ? 23.247 10.298  2.151   1.00 25.02 ? 528  LEU   A CD1 1 
ATOM   43   C  CD2 . LEU   A 1 6   ? 24.005 8.091   3.133   1.00 21.06 ? 528  LEU   A CD2 1 
ATOM   44   N  N   . TRP   A 1 7   ? 26.290 9.993   7.042   1.00 24.99 ? 529  TRP   A N   1 
ATOM   45   C  CA  . TRP   A 1 7   ? 27.204 10.735  7.889   1.00 19.99 ? 529  TRP   A CA  1 
ATOM   46   C  C   . TRP   A 1 7   ? 28.566 10.729  7.211   1.00 26.24 ? 529  TRP   A C   1 
ATOM   47   O  O   . TRP   A 1 7   ? 29.062 9.656   6.834   1.00 29.92 ? 529  TRP   A O   1 
ATOM   48   C  CB  . TRP   A 1 7   ? 27.357 10.201  9.312   1.00 25.47 ? 529  TRP   A CB  1 
ATOM   49   C  CG  . TRP   A 1 7   ? 28.129 11.162  10.104  1.00 24.45 ? 529  TRP   A CG  1 
ATOM   50   C  CD1 . TRP   A 1 7   ? 29.462 11.106  10.425  1.00 28.00 ? 529  TRP   A CD1 1 
ATOM   51   C  CD2 . TRP   A 1 7   ? 27.641 12.410  10.616  1.00 25.32 ? 529  TRP   A CD2 1 
ATOM   52   N  NE1 . TRP   A 1 7   ? 29.816 12.239  11.138  1.00 30.28 ? 529  TRP   A NE1 1 
ATOM   53   C  CE2 . TRP   A 1 7   ? 28.714 13.050  11.263  1.00 25.18 ? 529  TRP   A CE2 1 
ATOM   54   C  CE3 . TRP   A 1 7   ? 26.396 13.034  10.600  1.00 24.11 ? 529  TRP   A CE3 1 
ATOM   55   C  CZ2 . TRP   A 1 7   ? 28.570 14.275  11.898  1.00 25.46 ? 529  TRP   A CZ2 1 
ATOM   56   C  CZ3 . TRP   A 1 7   ? 26.255 14.246  11.218  1.00 28.05 ? 529  TRP   A CZ3 1 
ATOM   57   C  CH2 . TRP   A 1 7   ? 27.340 14.858  11.867  1.00 31.04 ? 529  TRP   A CH2 1 
ATOM   58   N  N   . PRO   A 1 8   ? 29.189 11.881  7.037   1.00 26.96 ? 530  PRO   A N   1 
ATOM   59   C  CA  . PRO   A 1 8   ? 28.687 13.222  7.365   1.00 24.98 ? 530  PRO   A CA  1 
ATOM   60   C  C   . PRO   A 1 8   ? 27.480 13.567  6.535   1.00 25.95 ? 530  PRO   A C   1 
ATOM   61   O  O   . PRO   A 1 8   ? 27.262 13.000  5.474   1.00 29.63 ? 530  PRO   A O   1 
ATOM   62   C  CB  . PRO   A 1 8   ? 29.877 14.145  7.051   1.00 32.18 ? 530  PRO   A CB  1 
ATOM   63   C  CG  . PRO   A 1 8   ? 30.802 13.324  6.207   1.00 33.81 ? 530  PRO   A CG  1 
ATOM   64   C  CD  . PRO   A 1 8   ? 30.593 11.903  6.606   1.00 31.57 ? 530  PRO   A CD  1 
ATOM   65   N  N   . ALA   A 1 9   ? 26.668 14.478  7.020   1.00 23.31 ? 531  ALA   A N   1 
ATOM   66   C  CA  . ALA   A 1 9   ? 25.389 14.721  6.386   1.00 22.70 ? 531  ALA   A CA  1 
ATOM   67   C  C   . ALA   A 1 9   ? 25.571 15.627  5.176   1.00 28.30 ? 531  ALA   A C   1 
ATOM   68   O  O   . ALA   A 1 9   ? 26.315 16.611  5.255   1.00 26.78 ? 531  ALA   A O   1 
ATOM   69   C  CB  . ALA   A 1 9   ? 24.414 15.352  7.377   1.00 26.03 ? 531  ALA   A CB  1 
ATOM   70   N  N   . PRO   A 1 10  ? 24.953 15.308  4.042   1.00 21.56 ? 532  PRO   A N   1 
ATOM   71   C  CA  . PRO   A 1 10  ? 24.889 16.277  2.945   1.00 24.71 ? 532  PRO   A CA  1 
ATOM   72   C  C   . PRO   A 1 10  ? 24.284 17.581  3.437   1.00 32.02 ? 532  PRO   A C   1 
ATOM   73   O  O   . PRO   A 1 10  ? 23.331 17.576  4.217   1.00 31.42 ? 532  PRO   A O   1 
ATOM   74   C  CB  . PRO   A 1 10  ? 23.978 15.593  1.923   1.00 24.69 ? 532  PRO   A CB  1 
ATOM   75   C  CG  . PRO   A 1 10  ? 24.174 14.107  2.190   1.00 24.67 ? 532  PRO   A CG  1 
ATOM   76   C  CD  . PRO   A 1 10  ? 24.386 13.994  3.676   1.00 24.94 ? 532  PRO   A CD  1 
ATOM   77   N  N   . ASN   A 1 11  ? 24.849 18.702  2.989   1.00 28.65 ? 533  ASN   A N   1 
ATOM   78   C  CA  . ASN   A 1 11  ? 24.285 19.990  3.378   1.00 31.56 ? 533  ASN   A CA  1 
ATOM   79   C  C   . ASN   A 1 11  ? 23.152 20.385  2.427   1.00 28.84 ? 533  ASN   A C   1 
ATOM   80   O  O   . ASN   A 1 11  ? 22.891 19.731  1.414   1.00 27.68 ? 533  ASN   A O   1 
ATOM   81   C  CB  . ASN   A 1 11  ? 25.382 21.059  3.449   1.00 27.79 ? 533  ASN   A CB  1 
ATOM   82   C  CG  . ASN   A 1 11  ? 26.012 21.358  2.111   1.00 27.90 ? 533  ASN   A CG  1 
ATOM   83   O  OD1 . ASN   A 1 11  ? 25.338 21.396  1.087   1.00 28.14 ? 533  ASN   A OD1 1 
ATOM   84   N  ND2 . ASN   A 1 11  ? 27.322 21.596  2.118   1.00 27.26 ? 533  ASN   A ND2 1 
ATOM   85   N  N   . GLU   A 1 12  ? 22.456 21.477  2.762   1.00 33.40 ? 534  GLU   A N   1 
ATOM   86   C  CA  . GLU   A 1 12  ? 21.249 21.800  2.011   1.00 29.76 ? 534  GLU   A CA  1 
ATOM   87   C  C   . GLU   A 1 12  ? 21.559 22.135  0.553   1.00 24.53 ? 534  GLU   A C   1 
ATOM   88   O  O   . GLU   A 1 12  ? 20.780 21.773  -0.339  1.00 29.47 ? 534  GLU   A O   1 
ATOM   89   C  CB  . GLU   A 1 12  ? 20.484 22.928  2.719   1.00 44.29 ? 534  GLU   A CB  1 
ATOM   90   C  CG  . GLU   A 1 12  ? 19.411 22.367  3.699   1.00 60.14 ? 534  GLU   A CG  1 
ATOM   91   C  CD  . GLU   A 1 12  ? 19.216 23.183  4.988   1.00 64.33 ? 534  GLU   A CD  1 
ATOM   92   O  OE1 . GLU   A 1 12  ? 20.206 23.398  5.721   1.00 60.07 ? 534  GLU   A OE1 1 
ATOM   93   O  OE2 . GLU   A 1 12  ? 18.065 23.590  5.281   1.00 57.45 ? 534  GLU   A OE2 1 
ATOM   94   N  N   . GLU   A 1 13  ? 22.700 22.779  0.285   1.00 28.88 ? 535  GLU   A N   1 
ATOM   95   C  CA  . GLU   A 1 13  ? 23.081 23.062  -1.099  1.00 28.95 ? 535  GLU   A CA  1 
ATOM   96   C  C   . GLU   A 1 13  ? 23.354 21.769  -1.875  1.00 32.29 ? 535  GLU   A C   1 
ATOM   97   O  O   . GLU   A 1 13  ? 23.010 21.653  -3.060  1.00 29.32 ? 535  GLU   A O   1 
ATOM   98   C  CB  . GLU   A 1 13  ? 24.315 23.969  -1.133  1.00 36.28 ? 535  GLU   A CB  1 
ATOM   99   C  CG  . GLU   A 1 13  ? 24.111 25.390  -0.553  1.00 42.22 ? 535  GLU   A CG  1 
ATOM   100  C  CD  . GLU   A 1 13  ? 23.979 25.429  0.970   1.00 52.10 ? 535  GLU   A CD  1 
ATOM   101  O  OE1 . GLU   A 1 13  ? 24.511 24.526  1.673   1.00 41.72 ? 535  GLU   A OE1 1 
ATOM   102  O  OE2 . GLU   A 1 13  ? 23.337 26.382  1.471   1.00 55.70 ? 535  GLU   A OE2 1 
ATOM   103  N  N   . GLN   A 1 14  ? 23.951 20.778  -1.220  1.00 27.42 ? 536  GLN   A N   1 
ATOM   104  C  CA  . GLN   A 1 14  ? 24.244 19.527  -1.916  1.00 20.36 ? 536  GLN   A CA  1 
ATOM   105  C  C   . GLN   A 1 14  ? 22.963 18.792  -2.291  1.00 24.35 ? 536  GLN   A C   1 
ATOM   106  O  O   . GLN   A 1 14  ? 22.841 18.258  -3.407  1.00 24.88 ? 536  GLN   A O   1 
ATOM   107  C  CB  . GLN   A 1 14  ? 25.162 18.663  -1.038  1.00 25.63 ? 536  GLN   A CB  1 
ATOM   108  C  CG  . GLN   A 1 14  ? 26.597 19.221  -0.956  1.00 24.50 ? 536  GLN   A CG  1 
ATOM   109  C  CD  . GLN   A 1 14  ? 27.463 18.559  0.102   1.00 26.73 ? 536  GLN   A CD  1 
ATOM   110  O  OE1 . GLN   A 1 14  ? 26.988 18.178  1.175   1.00 24.67 ? 536  GLN   A OE1 1 
ATOM   111  N  NE2 . GLN   A 1 14  ? 28.751 18.426  -0.197  1.00 25.07 ? 536  GLN   A NE2 1 
ATOM   112  N  N   . VAL   A 1 15  ? 21.977 18.786  -1.382  1.00 24.90 ? 537  VAL   A N   1 
ATOM   113  C  CA  . VAL   A 1 15  ? 20.688 18.166  -1.668  1.00 23.12 ? 537  VAL   A CA  1 
ATOM   114  C  C   . VAL   A 1 15  ? 19.965 18.934  -2.768  1.00 24.00 ? 537  VAL   A C   1 
ATOM   115  O  O   . VAL   A 1 15  ? 19.374 18.340  -3.680  1.00 27.82 ? 537  VAL   A O   1 
ATOM   116  C  CB  . VAL   A 1 15  ? 19.844 18.092  -0.381  1.00 30.89 ? 537  VAL   A CB  1 
ATOM   117  C  CG1 . VAL   A 1 15  ? 18.446 17.544  -0.671  1.00 33.42 ? 537  VAL   A CG1 1 
ATOM   118  C  CG2 . VAL   A 1 15  ? 20.546 17.253  0.672   1.00 26.69 ? 537  VAL   A CG2 1 
ATOM   119  N  N   . THR   A 1 16  ? 19.987 20.264  -2.697  1.00 27.01 ? 538  THR   A N   1 
ATOM   120  C  CA  . THR   A 1 16  ? 19.380 21.053  -3.758  1.00 29.56 ? 538  THR   A CA  1 
ATOM   121  C  C   . THR   A 1 16  ? 19.991 20.727  -5.112  1.00 26.64 ? 538  THR   A C   1 
ATOM   122  O  O   . THR   A 1 16  ? 19.268 20.532  -6.095  1.00 28.68 ? 538  THR   A O   1 
ATOM   123  C  CB  . THR   A 1 16  ? 19.513 22.536  -3.435  1.00 31.81 ? 538  THR   A CB  1 
ATOM   124  O  OG1 . THR   A 1 16  ? 18.612 22.841  -2.366  1.00 31.51 ? 538  THR   A OG1 1 
ATOM   125  C  CG2 . THR   A 1 16  ? 19.189 23.381  -4.651  1.00 33.93 ? 538  THR   A CG2 1 
ATOM   126  N  N   . CYS   A 1 17  ? 21.323 20.663  -5.184  1.00 27.88 ? 539  CYS   A N   1 
ATOM   127  C  CA  . CYS   A 1 17  ? 21.987 20.327  -6.442  1.00 24.81 ? 539  CYS   A CA  1 
ATOM   128  C  C   . CYS   A 1 17  ? 21.538 18.968  -6.955  1.00 24.50 ? 539  CYS   A C   1 
ATOM   129  O  O   . CYS   A 1 17  ? 21.239 18.808  -8.144  1.00 24.98 ? 539  CYS   A O   1 
ATOM   130  C  CB  . CYS   A 1 17  ? 23.508 20.353  -6.249  1.00 26.42 ? 539  CYS   A CB  1 
ATOM   131  S  SG  . CYS   A 1 17  ? 24.447 19.986  -7.730  1.00 29.39 ? 539  CYS   A SG  1 
ATOM   132  N  N   . LEU   A 1 18  ? 21.507 17.963  -6.071  1.00 21.48 ? 540  LEU   A N   1 
ATOM   133  C  CA  . LEU   A 1 18  ? 21.052 16.638  -6.479  1.00 19.86 ? 540  LEU   A CA  1 
ATOM   134  C  C   . LEU   A 1 18  ? 19.649 16.693  -7.079  1.00 26.31 ? 540  LEU   A C   1 
ATOM   135  O  O   . LEU   A 1 18  ? 19.390 16.110  -8.141  1.00 25.16 ? 540  LEU   A O   1 
ATOM   136  C  CB  . LEU   A 1 18  ? 21.078 15.692  -5.280  1.00 21.78 ? 540  LEU   A CB  1 
ATOM   137  C  CG  . LEU   A 1 18  ? 20.807 14.232  -5.595  1.00 24.31 ? 540  LEU   A CG  1 
ATOM   138  C  CD1 . LEU   A 1 18  ? 21.933 13.675  -6.465  1.00 21.53 ? 540  LEU   A CD1 1 
ATOM   139  C  CD2 . LEU   A 1 18  ? 20.706 13.452  -4.309  1.00 23.62 ? 540  LEU   A CD2 1 
ATOM   140  N  N   . LYS   A 1 19  ? 18.730 17.401  -6.412  1.00 29.57 ? 541  LYS   A N   1 
ATOM   141  C  CA  . LYS   A 1 19  ? 17.361 17.504  -6.932  1.00 34.19 ? 541  LYS   A CA  1 
ATOM   142  C  C   . LYS   A 1 19  ? 17.348 18.206  -8.282  1.00 28.15 ? 541  LYS   A C   1 
ATOM   143  O  O   . LYS   A 1 19  ? 16.806 17.690  -9.268  1.00 30.67 ? 541  LYS   A O   1 
ATOM   144  C  CB  . LYS   A 1 19  ? 16.452 18.274  -5.968  1.00 33.97 ? 541  LYS   A CB  1 
ATOM   145  C  CG  . LYS   A 1 19  ? 16.606 17.988  -4.488  1.00 45.01 ? 541  LYS   A CG  1 
ATOM   146  C  CD  . LYS   A 1 19  ? 15.565 17.019  -3.929  1.00 44.98 ? 541  LYS   A CD  1 
ATOM   147  C  CE  . LYS   A 1 19  ? 15.411 17.216  -2.413  1.00 38.13 ? 541  LYS   A CE  1 
ATOM   148  N  NZ  . LYS   A 1 19  ? 14.998 15.981  -1.662  1.00 53.01 ? 541  LYS   A NZ  1 
ATOM   149  N  N   . MET   A 1 20  ? 17.962 19.383  -8.342  1.00 27.79 ? 542  MET   A N   1 
ATOM   150  C  CA  . MET   A 1 20  ? 17.828 20.247  -9.512  1.00 33.04 ? 542  MET   A CA  1 
ATOM   151  C  C   . MET   A 1 20  ? 18.492 19.649  -10.748 1.00 37.35 ? 542  MET   A C   1 
ATOM   152  O  O   . MET   A 1 20  ? 17.941 19.745  -11.856 1.00 26.43 ? 542  MET   A O   1 
ATOM   153  C  CB  . MET   A 1 20  ? 18.411 21.623  -9.207  1.00 33.41 ? 542  MET   A CB  1 
ATOM   154  C  CG  . MET   A 1 20  ? 17.932 22.721  -10.152 1.00 51.01 ? 542  MET   A CG  1 
ATOM   155  S  SD  . MET   A 1 20  ? 19.101 24.099  -10.301 1.00 65.25 ? 542  MET   A SD  1 
ATOM   156  C  CE  . MET   A 1 20  ? 19.449 24.452  -8.579  1.00 42.23 ? 542  MET   A CE  1 
ATOM   157  N  N   . TYR   A 1 21  ? 19.668 19.024  -10.597 1.00 27.23 ? 543  TYR   A N   1 
ATOM   158  C  CA  . TYR   A 1 21  ? 20.382 18.564  -11.778 1.00 21.52 ? 543  TYR   A CA  1 
ATOM   159  C  C   . TYR   A 1 21  ? 20.285 17.069  -12.033 1.00 27.04 ? 543  TYR   A C   1 
ATOM   160  O  O   . TYR   A 1 21  ? 20.585 16.636  -13.151 1.00 31.56 ? 543  TYR   A O   1 
ATOM   161  C  CB  . TYR   A 1 21  ? 21.868 18.960  -11.699 1.00 23.60 ? 543  TYR   A CB  1 
ATOM   162  C  CG  . TYR   A 1 21  ? 22.040 20.440  -11.873 1.00 26.21 ? 543  TYR   A CG  1 
ATOM   163  C  CD1 . TYR   A 1 21  ? 21.845 21.032  -13.117 1.00 28.91 ? 543  TYR   A CD1 1 
ATOM   164  C  CD2 . TYR   A 1 21  ? 22.335 21.259  -10.788 1.00 29.89 ? 543  TYR   A CD2 1 
ATOM   165  C  CE1 . TYR   A 1 21  ? 21.974 22.407  -13.285 1.00 30.93 ? 543  TYR   A CE1 1 
ATOM   166  C  CE2 . TYR   A 1 21  ? 22.472 22.635  -10.951 1.00 32.44 ? 543  TYR   A CE2 1 
ATOM   167  C  CZ  . TYR   A 1 21  ? 22.285 23.196  -12.204 1.00 38.52 ? 543  TYR   A CZ  1 
ATOM   168  O  OH  . TYR   A 1 21  ? 22.404 24.560  -12.382 1.00 43.52 ? 543  TYR   A OH  1 
ATOM   169  N  N   . PHE   A 1 22  ? 19.895 16.263  -11.054 1.00 23.14 ? 544  PHE   A N   1 
ATOM   170  C  CA  . PHE   A 1 22  ? 19.846 14.836  -11.289 1.00 20.66 ? 544  PHE   A CA  1 
ATOM   171  C  C   . PHE   A 1 22  ? 18.483 14.229  -11.016 1.00 26.03 ? 544  PHE   A C   1 
ATOM   172  O  O   . PHE   A 1 22  ? 18.289 13.047  -11.299 1.00 30.19 ? 544  PHE   A O   1 
ATOM   173  C  CB  . PHE   A 1 22  ? 20.927 14.140  -10.451 1.00 23.84 ? 544  PHE   A CB  1 
ATOM   174  C  CG  . PHE   A 1 22  ? 22.316 14.554  -10.846 1.00 23.93 ? 544  PHE   A CG  1 
ATOM   175  C  CD1 . PHE   A 1 22  ? 23.000 13.868  -11.835 1.00 22.15 ? 544  PHE   A CD1 1 
ATOM   176  C  CD2 . PHE   A 1 22  ? 22.917 15.663  -10.267 1.00 25.36 ? 544  PHE   A CD2 1 
ATOM   177  C  CE1 . PHE   A 1 22  ? 24.270 14.269  -12.216 1.00 26.25 ? 544  PHE   A CE1 1 
ATOM   178  C  CE2 . PHE   A 1 22  ? 24.194 16.058  -10.643 1.00 21.71 ? 544  PHE   A CE2 1 
ATOM   179  C  CZ  . PHE   A 1 22  ? 24.860 15.361  -11.624 1.00 21.38 ? 544  PHE   A CZ  1 
ATOM   180  N  N   . GLY   A 1 23  ? 17.534 15.002  -10.509 1.00 27.03 ? 545  GLY   A N   1 
ATOM   181  C  CA  . GLY   A 1 23  ? 16.190 14.475  -10.350 1.00 32.80 ? 545  GLY   A CA  1 
ATOM   182  C  C   . GLY   A 1 23  ? 16.075 13.388  -9.310  1.00 37.77 ? 545  GLY   A C   1 
ATOM   183  O  O   . GLY   A 1 23  ? 15.186 12.537  -9.408  1.00 43.91 ? 545  GLY   A O   1 
ATOM   184  N  N   . HIS   A 1 24  ? 16.962 13.377  -8.320  1.00 31.87 ? 546  HIS   A N   1 
ATOM   185  C  CA  . HIS   A 1 24  ? 16.910 12.394  -7.251  1.00 28.93 ? 546  HIS   A CA  1 
ATOM   186  C  C   . HIS   A 1 24  ? 16.758 13.118  -5.930  1.00 29.65 ? 546  HIS   A C   1 
ATOM   187  O  O   . HIS   A 1 24  ? 17.242 14.241  -5.752  1.00 30.23 ? 546  HIS   A O   1 
ATOM   188  C  CB  . HIS   A 1 24  ? 18.171 11.495  -7.210  1.00 27.26 ? 546  HIS   A CB  1 
ATOM   189  C  CG  . HIS   A 1 24  ? 18.210 10.466  -8.296  1.00 37.96 ? 546  HIS   A CG  1 
ATOM   190  N  ND1 . HIS   A 1 24  ? 19.180 10.451  -9.277  1.00 54.13 ? 546  HIS   A ND1 1 
ATOM   191  C  CD2 . HIS   A 1 24  ? 17.402 9.408   -8.550  1.00 43.71 ? 546  HIS   A CD2 1 
ATOM   192  C  CE1 . HIS   A 1 24  ? 18.964 9.431   -10.091 1.00 52.17 ? 546  HIS   A CE1 1 
ATOM   193  N  NE2 . HIS   A 1 24  ? 17.894 8.780   -9.670  1.00 49.63 ? 546  HIS   A NE2 1 
ATOM   194  N  N   . SER   A 1 25  ? 16.079 12.462  -5.003  1.00 28.72 ? 547  SER   A N   1 
ATOM   195  C  CA  . SER   A 1 25  ? 15.866 13.021  -3.681  1.00 39.29 ? 547  SER   A CA  1 
ATOM   196  C  C   . SER   A 1 25  ? 16.881 12.533  -2.663  1.00 40.05 ? 547  SER   A C   1 
ATOM   197  O  O   . SER   A 1 25  ? 16.919 13.074  -1.552  1.00 38.92 ? 547  SER   A O   1 
ATOM   198  C  CB  . SER   A 1 25  ? 14.463 12.666  -3.191  1.00 40.27 ? 547  SER   A CB  1 
ATOM   199  O  OG  . SER   A 1 25  ? 14.266 11.272  -3.390  1.00 49.74 ? 547  SER   A OG  1 
ATOM   200  N  N   . SER   A 1 26  ? 17.684 11.521  -3.001  1.00 35.51 ? 548  SER   A N   1 
ATOM   201  C  CA  . SER   A 1 26  ? 18.611 10.956  -2.028  1.00 37.69 ? 548  SER   A CA  1 
ATOM   202  C  C   . SER   A 1 26  ? 19.838 10.381  -2.721  1.00 25.75 ? 548  SER   A C   1 
ATOM   203  O  O   . SER   A 1 26  ? 19.754 9.874   -3.842  1.00 22.87 ? 548  SER   A O   1 
ATOM   204  C  CB  . SER   A 1 26  ? 17.933 9.869   -1.179  1.00 38.44 ? 548  SER   A CB  1 
ATOM   205  O  OG  . SER   A 1 26  ? 17.298 8.877   -1.984  1.00 42.33 ? 548  SER   A OG  1 
ATOM   206  N  N   . PHE   A 1 27  ? 20.983 10.492  -2.045  1.00 21.82 ? 549  PHE   A N   1 
ATOM   207  C  CA  . PHE   A 1 27  ? 22.163 9.703   -2.391  1.00 19.96 ? 549  PHE   A CA  1 
ATOM   208  C  C   . PHE   A 1 27  ? 22.059 8.326   -1.750  1.00 22.69 ? 549  PHE   A C   1 
ATOM   209  O  O   . PHE   A 1 27  ? 21.752 8.225   -0.563  1.00 24.68 ? 549  PHE   A O   1 
ATOM   210  C  CB  . PHE   A 1 27  ? 23.445 10.333  -1.842  1.00 17.96 ? 549  PHE   A CB  1 
ATOM   211  C  CG  . PHE   A 1 27  ? 23.642 11.801  -2.180  1.00 21.14 ? 549  PHE   A CG  1 
ATOM   212  C  CD1 . PHE   A 1 27  ? 23.155 12.805  -1.350  1.00 21.70 ? 549  PHE   A CD1 1 
ATOM   213  C  CD2 . PHE   A 1 27  ? 24.366 12.165  -3.297  1.00 22.32 ? 549  PHE   A CD2 1 
ATOM   214  C  CE1 . PHE   A 1 27  ? 23.390 14.152  -1.650  1.00 22.11 ? 549  PHE   A CE1 1 
ATOM   215  C  CE2 . PHE   A 1 27  ? 24.595 13.501  -3.609  1.00 23.05 ? 549  PHE   A CE2 1 
ATOM   216  C  CZ  . PHE   A 1 27  ? 24.102 14.496  -2.784  1.00 21.50 ? 549  PHE   A CZ  1 
ATOM   217  N  N   . LYS   A 1 28  ? 22.398 7.281   -2.499  1.00 19.11 ? 550  LYS   A N   1 
ATOM   218  C  CA  . LYS   A 1 28  ? 22.559 5.972   -1.879  1.00 19.40 ? 550  LYS   A CA  1 
ATOM   219  C  C   . LYS   A 1 28  ? 23.847 5.976   -1.051  1.00 19.32 ? 550  LYS   A C   1 
ATOM   220  O  O   . LYS   A 1 28  ? 24.756 6.770   -1.315  1.00 16.77 ? 550  LYS   A O   1 
ATOM   221  C  CB  . LYS   A 1 28  ? 22.601 4.876   -2.942  1.00 22.65 ? 550  LYS   A CB  1 
ATOM   222  C  CG  . LYS   A 1 28  ? 21.300 4.737   -3.721  1.00 21.55 ? 550  LYS   A CG  1 
ATOM   223  C  CD  . LYS   A 1 28  ? 20.161 4.276   -2.783  1.00 25.64 ? 550  LYS   A CD  1 
ATOM   224  C  CE  . LYS   A 1 28  ? 18.814 4.381   -3.439  1.00 34.27 ? 550  LYS   A CE  1 
ATOM   225  N  NZ  . LYS   A 1 28  ? 17.738 4.027   -2.454  1.00 32.14 ? 550  LYS   A NZ  1 
ATOM   226  N  N   . PRO   A 1 29  ? 23.948 5.122   -0.029  1.00 16.44 ? 551  PRO   A N   1 
ATOM   227  C  CA  . PRO   A 1 29  ? 25.103 5.228   0.876   1.00 18.09 ? 551  PRO   A CA  1 
ATOM   228  C  C   . PRO   A 1 29  ? 26.449 5.129   0.167   1.00 18.06 ? 551  PRO   A C   1 
ATOM   229  O  O   . PRO   A 1 29  ? 27.349 5.937   0.453   1.00 18.55 ? 551  PRO   A O   1 
ATOM   230  C  CB  . PRO   A 1 29  ? 24.866 4.075   1.863   1.00 15.25 ? 551  PRO   A CB  1 
ATOM   231  C  CG  . PRO   A 1 29  ? 23.304 4.026   1.920   1.00 17.85 ? 551  PRO   A CG  1 
ATOM   232  C  CD  . PRO   A 1 29  ? 22.916 4.194   0.484   1.00 16.03 ? 551  PRO   A CD  1 
ATOM   233  N  N   . VAL   A 1 30  ? 26.620 4.185   -0.763  1.00 18.04 ? 552  VAL   A N   1 
ATOM   234  C  CA  . VAL   A 1 30  ? 27.931 4.085   -1.417  1.00 13.32 ? 552  VAL   A CA  1 
ATOM   235  C  C   . VAL   A 1 30  ? 28.185 5.310   -2.297  1.00 16.94 ? 552  VAL   A C   1 
ATOM   236  O  O   . VAL   A 1 30  ? 29.330 5.785   -2.417  1.00 17.59 ? 552  VAL   A O   1 
ATOM   237  C  CB  . VAL   A 1 30  ? 28.062 2.772   -2.215  1.00 13.84 ? 552  VAL   A CB  1 
ATOM   238  C  CG1 . VAL   A 1 30  ? 27.111 2.717   -3.410  1.00 16.05 ? 552  VAL   A CG1 1 
ATOM   239  C  CG2 . VAL   A 1 30  ? 29.534 2.563   -2.662  1.00 17.65 ? 552  VAL   A CG2 1 
ATOM   240  N  N   . GLN   A 1 31  ? 27.131 5.831   -2.930  1.00 13.70 ? 553  GLN   A N   1 
ATOM   241  C  CA  . GLN   A 1 31  ? 27.278 7.009   -3.766  1.00 14.12 ? 553  GLN   A CA  1 
ATOM   242  C  C   . GLN   A 1 31  ? 27.758 8.173   -2.928  1.00 15.77 ? 553  GLN   A C   1 
ATOM   243  O  O   . GLN   A 1 31  ? 28.683 8.891   -3.325  1.00 15.31 ? 553  GLN   A O   1 
ATOM   244  C  CB  . GLN   A 1 31  ? 25.939 7.347   -4.448  1.00 21.19 ? 553  GLN   A CB  1 
ATOM   245  C  CG  . GLN   A 1 31  ? 25.463 6.324   -5.461  1.00 20.13 ? 553  GLN   A CG  1 
ATOM   246  C  CD  . GLN   A 1 31  ? 24.145 6.720   -6.089  1.00 25.10 ? 553  GLN   A CD  1 
ATOM   247  O  OE1 . GLN   A 1 31  ? 23.261 7.250   -5.417  1.00 23.83 ? 553  GLN   A OE1 1 
ATOM   248  N  NE2 . GLN   A 1 31  ? 24.021 6.498   -7.387  1.00 29.42 ? 553  GLN   A NE2 1 
ATOM   249  N  N   . TRP   A 1 32  ? 27.182 8.348   -1.748  1.00 17.64 ? 554  TRP   A N   1 
ATOM   250  C  CA  . TRP   A 1 32  ? 27.640 9.443   -0.857  1.00 16.42 ? 554  TRP   A CA  1 
ATOM   251  C  C   . TRP   A 1 32  ? 29.106 9.221   -0.439  1.00 24.37 ? 554  TRP   A C   1 
ATOM   252  O  O   . TRP   A 1 32  ? 29.872 10.180  -0.441  1.00 18.84 ? 554  TRP   A O   1 
ATOM   253  C  CB  . TRP   A 1 32  ? 26.712 9.628   0.352   1.00 17.04 ? 554  TRP   A CB  1 
ATOM   254  C  CG  . TRP   A 1 32  ? 27.127 10.720  1.284   1.00 19.99 ? 554  TRP   A CG  1 
ATOM   255  C  CD1 . TRP   A 1 32  ? 27.439 10.599  2.605   1.00 20.48 ? 554  TRP   A CD1 1 
ATOM   256  C  CD2 . TRP   A 1 32  ? 27.272 12.112  0.963   1.00 19.04 ? 554  TRP   A CD2 1 
ATOM   257  N  NE1 . TRP   A 1 32  ? 27.776 11.817  3.125   1.00 21.12 ? 554  TRP   A NE1 1 
ATOM   258  C  CE2 . TRP   A 1 32  ? 27.679 12.765  2.143   1.00 18.76 ? 554  TRP   A CE2 1 
ATOM   259  C  CE3 . TRP   A 1 32  ? 27.099 12.867  -0.200  1.00 22.57 ? 554  TRP   A CE3 1 
ATOM   260  C  CZ2 . TRP   A 1 32  ? 27.919 14.136  2.187   1.00 25.36 ? 554  TRP   A CZ2 1 
ATOM   261  C  CZ3 . TRP   A 1 32  ? 27.336 14.221  -0.156  1.00 28.01 ? 554  TRP   A CZ3 1 
ATOM   262  C  CH2 . TRP   A 1 32  ? 27.741 14.844  1.023   1.00 23.53 ? 554  TRP   A CH2 1 
ATOM   263  N  N   . LYS   A 1 33  ? 29.453 7.985   -0.081  1.00 18.28 ? 555  LYS   A N   1 
ATOM   264  C  CA  . LYS   A 1 33  ? 30.841 7.707   0.365   1.00 17.43 ? 555  LYS   A CA  1 
ATOM   265  C  C   . LYS   A 1 33  ? 31.831 8.094   -0.749  1.00 18.87 ? 555  LYS   A C   1 
ATOM   266  O  O   . LYS   A 1 33  ? 32.842 8.705   -0.436  1.00 19.72 ? 555  LYS   A O   1 
ATOM   267  C  CB  . LYS   A 1 33  ? 30.994 6.246   0.806   1.00 21.28 ? 555  LYS   A CB  1 
ATOM   268  C  CG  . LYS   A 1 33  ? 30.181 5.865   2.033   1.00 34.45 ? 555  LYS   A CG  1 
ATOM   269  C  CD  . LYS   A 1 33  ? 30.708 4.649   2.756   1.00 44.48 ? 555  LYS   A CD  1 
ATOM   270  C  CE  . LYS   A 1 33  ? 29.822 4.212   3.905   1.00 43.36 ? 555  LYS   A CE  1 
ATOM   271  N  NZ  . LYS   A 1 33  ? 29.746 5.229   4.979   1.00 45.31 ? 555  LYS   A NZ  1 
ATOM   272  N  N   . VAL   A 1 34  ? 31.548 7.704   -1.991  1.00 13.95 ? 556  VAL   A N   1 
ATOM   273  C  CA  . VAL   A 1 34  ? 32.439 8.104   -3.080  1.00 16.35 ? 556  VAL   A CA  1 
ATOM   274  C  C   . VAL   A 1 34  ? 32.444 9.630   -3.239  1.00 19.55 ? 556  VAL   A C   1 
ATOM   275  O  O   . VAL   A 1 34  ? 33.512 10.272  -3.256  1.00 17.63 ? 556  VAL   A O   1 
ATOM   276  C  CB  . VAL   A 1 34  ? 32.047 7.414   -4.398  1.00 19.18 ? 556  VAL   A CB  1 
ATOM   277  C  CG1 . VAL   A 1 34  ? 32.932 7.959   -5.517  1.00 17.35 ? 556  VAL   A CG1 1 
ATOM   278  C  CG2 . VAL   A 1 34  ? 32.136 5.874   -4.303  1.00 15.72 ? 556  VAL   A CG2 1 
ATOM   279  N  N   . ILE   A 1 35  ? 31.252 10.230  -3.382  1.00 15.73 ? 557  ILE   A N   1 
ATOM   280  C  CA  . ILE   A 1 35  ? 31.155 11.679  -3.641  1.00 18.85 ? 557  ILE   A CA  1 
ATOM   281  C  C   . ILE   A 1 35  ? 31.848 12.478  -2.539  1.00 17.59 ? 557  ILE   A C   1 
ATOM   282  O  O   . ILE   A 1 35  ? 32.601 13.435  -2.800  1.00 18.55 ? 557  ILE   A O   1 
ATOM   283  C  CB  . ILE   A 1 35  ? 29.670 12.092  -3.785  1.00 17.35 ? 557  ILE   A CB  1 
ATOM   284  C  CG1 . ILE   A 1 35  ? 29.095 11.570  -5.111  1.00 16.52 ? 557  ILE   A CG1 1 
ATOM   285  C  CG2 . ILE   A 1 35  ? 29.499 13.632  -3.625  1.00 17.04 ? 557  ILE   A CG2 1 
ATOM   286  C  CD1 . ILE   A 1 35  ? 27.560 11.539  -5.152  1.00 15.95 ? 557  ILE   A CD1 1 
ATOM   287  N  N   . HIS   A 1 36  ? 31.554 12.151  -1.285  1.00 16.20 ? 558  HIS   A N   1 
ATOM   288  C  CA  . HIS   A 1 36  ? 32.132 12.905  -0.182  1.00 22.29 ? 558  HIS   A CA  1 
ATOM   289  C  C   . HIS   A 1 36  ? 33.639 12.726  -0.131  1.00 25.15 ? 558  HIS   A C   1 
ATOM   290  O  O   . HIS   A 1 36  ? 34.376 13.688  0.135   1.00 20.32 ? 558  HIS   A O   1 
ATOM   291  C  CB  . HIS   A 1 36  ? 31.513 12.468  1.151   1.00 23.58 ? 558  HIS   A CB  1 
ATOM   292  C  CG  . HIS   A 1 36  ? 32.060 13.216  2.332   1.00 27.01 ? 558  HIS   A CG  1 
ATOM   293  N  ND1 . HIS   A 1 36  ? 31.585 14.451  2.720   1.00 36.10 ? 558  HIS   A ND1 1 
ATOM   294  C  CD2 . HIS   A 1 36  ? 33.052 12.909  3.199   1.00 27.15 ? 558  HIS   A CD2 1 
ATOM   295  C  CE1 . HIS   A 1 36  ? 32.248 14.862  3.787   1.00 24.60 ? 558  HIS   A CE1 1 
ATOM   296  N  NE2 . HIS   A 1 36  ? 33.145 13.945  4.096   1.00 28.29 ? 558  HIS   A NE2 1 
ATOM   297  N  N   . SER   A 1 37  ? 34.131 11.506  -0.392  1.00 17.53 ? 559  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 35.576 11.329  -0.309  1.00 21.31 ? 559  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 36.282 12.129  -1.395  1.00 21.82 ? 559  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 37.370 12.686  -1.159  1.00 18.58 ? 559  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 35.905 9.848   -0.412  1.00 20.12 ? 559  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 35.638 9.428   -1.719  1.00 23.88 ? 559  SER   A OG  1 
ATOM   303  N  N   . VAL   A 1 38  ? 35.646 12.253  -2.562  1.00 19.18 ? 560  VAL   A N   1 
ATOM   304  C  CA  . VAL   A 1 38  ? 36.190 13.093  -3.638  1.00 22.07 ? 560  VAL   A CA  1 
ATOM   305  C  C   . VAL   A 1 38  ? 36.170 14.570  -3.252  1.00 23.50 ? 560  VAL   A C   1 
ATOM   306  O  O   . VAL   A 1 38  ? 37.178 15.283  -3.388  1.00 21.45 ? 560  VAL   A O   1 
ATOM   307  C  CB  . VAL   A 1 38  ? 35.406 12.859  -4.941  1.00 20.80 ? 560  VAL   A CB  1 
ATOM   308  C  CG1 . VAL   A 1 38  ? 35.746 13.946  -5.949  1.00 20.76 ? 560  VAL   A CG1 1 
ATOM   309  C  CG2 . VAL   A 1 38  ? 35.742 11.457  -5.495  1.00 19.83 ? 560  VAL   A CG2 1 
ATOM   310  N  N   . LEU   A 1 39  ? 35.021 15.060  -2.793  1.00 17.29 ? 561  LEU   A N   1 
ATOM   311  C  CA  . LEU   A 1 39  ? 34.870 16.495  -2.562  1.00 20.07 ? 561  LEU   A CA  1 
ATOM   312  C  C   . LEU   A 1 39  ? 35.676 16.972  -1.358  1.00 21.56 ? 561  LEU   A C   1 
ATOM   313  O  O   . LEU   A 1 39  ? 36.288 18.047  -1.405  1.00 24.65 ? 561  LEU   A O   1 
ATOM   314  C  CB  . LEU   A 1 39  ? 33.391 16.840  -2.389  1.00 21.53 ? 561  LEU   A CB  1 
ATOM   315  C  CG  . LEU   A 1 39  ? 32.454 16.707  -3.599  1.00 20.70 ? 561  LEU   A CG  1 
ATOM   316  C  CD1 . LEU   A 1 39  ? 31.044 16.913  -3.110  1.00 21.81 ? 561  LEU   A CD1 1 
ATOM   317  C  CD2 . LEU   A 1 39  ? 32.762 17.727  -4.690  1.00 25.33 ? 561  LEU   A CD2 1 
ATOM   318  N  N   . GLU   A 1 40  ? 35.704 16.205  -0.274  1.00 19.39 ? 562  GLU   A N   1 
ATOM   319  C  CA  . GLU   A 1 40  ? 36.347 16.677  0.943   1.00 26.64 ? 562  GLU   A CA  1 
ATOM   320  C  C   . GLU   A 1 40  ? 37.745 16.134  1.157   1.00 26.93 ? 562  GLU   A C   1 
ATOM   321  O  O   . GLU   A 1 40  ? 38.580 16.854  1.707   1.00 32.17 ? 562  GLU   A O   1 
ATOM   322  C  CB  . GLU   A 1 40  ? 35.483 16.358  2.163   1.00 26.11 ? 562  GLU   A CB  1 
ATOM   323  C  CG  . GLU   A 1 40  ? 34.077 16.919  2.045   1.00 34.25 ? 562  GLU   A CG  1 
ATOM   324  C  CD  . GLU   A 1 40  ? 34.043 18.431  1.953   1.00 44.45 ? 562  GLU   A CD  1 
ATOM   325  O  OE1 . GLU   A 1 40  ? 34.987 19.071  2.475   1.00 35.62 ? 562  GLU   A OE1 1 
ATOM   326  O  OE2 . GLU   A 1 40  ? 33.075 18.968  1.354   1.00 40.33 ? 562  GLU   A OE2 1 
ATOM   327  N  N   . GLU   A 1 41  ? 38.054 14.897  0.750   1.00 24.15 ? 563  GLU   A N   1 
ATOM   328  C  CA  . GLU   A 1 41  ? 39.387 14.355  0.966   1.00 25.67 ? 563  GLU   A CA  1 
ATOM   329  C  C   . GLU   A 1 41  ? 40.203 14.286  -0.308  1.00 23.32 ? 563  GLU   A C   1 
ATOM   330  O  O   . GLU   A 1 41  ? 41.370 13.871  -0.254  1.00 22.90 ? 563  GLU   A O   1 
ATOM   331  C  CB  . GLU   A 1 41  ? 39.290 12.949  1.585   1.00 28.36 ? 563  GLU   A CB  1 
ATOM   332  C  CG  . GLU   A 1 41  ? 38.537 12.918  2.906   1.00 32.97 ? 563  GLU   A CG  1 
ATOM   333  C  CD  . GLU   A 1 41  ? 38.057 11.523  3.296   1.00 47.52 ? 563  GLU   A CD  1 
ATOM   334  O  OE1 . GLU   A 1 41  ? 38.822 10.552  3.115   1.00 46.94 ? 563  GLU   A OE1 1 
ATOM   335  O  OE2 . GLU   A 1 41  ? 36.905 11.401  3.775   1.00 53.15 ? 563  GLU   A OE2 1 
ATOM   336  N  N   . ARG   A 1 42  ? 39.622 14.657  -1.455  1.00 18.89 ? 564  ARG   A N   1 
ATOM   337  C  CA  . ARG   A 1 42  ? 40.304 14.534  -2.745  1.00 19.63 ? 564  ARG   A CA  1 
ATOM   338  C  C   . ARG   A 1 42  ? 40.922 13.144  -2.904  1.00 26.05 ? 564  ARG   A C   1 
ATOM   339  O  O   . ARG   A 1 42  ? 42.085 12.982  -3.295  1.00 20.42 ? 564  ARG   A O   1 
ATOM   340  C  CB  . ARG   A 1 42  ? 41.378 15.630  -2.898  1.00 22.24 ? 564  ARG   A CB  1 
ATOM   341  C  CG  . ARG   A 1 42  ? 40.873 17.012  -2.462  1.00 25.38 ? 564  ARG   A CG  1 
ATOM   342  C  CD  . ARG   A 1 42  ? 39.693 17.438  -3.340  1.00 24.50 ? 564  ARG   A CD  1 
ATOM   343  N  NE  . ARG   A 1 42  ? 40.130 17.705  -4.708  1.00 31.15 ? 564  ARG   A NE  1 
ATOM   344  C  CZ  . ARG   A 1 42  ? 39.433 17.390  -5.792  1.00 34.95 ? 564  ARG   A CZ  1 
ATOM   345  N  NH1 . ARG   A 1 42  ? 38.266 16.760  -5.702  1.00 20.88 ? 564  ARG   A NH1 1 
ATOM   346  N  NH2 . ARG   A 1 42  ? 39.923 17.701  -6.995  1.00 28.19 ? 564  ARG   A NH2 1 
ATOM   347  N  N   . ARG   A 1 43  ? 40.134 12.116  -2.595  1.00 21.85 ? 565  ARG   A N   1 
ATOM   348  C  CA  . ARG   A 1 43  ? 40.689 10.775  -2.412  1.00 19.08 ? 565  ARG   A CA  1 
ATOM   349  C  C   . ARG   A 1 43  ? 40.411 9.875   -3.611  1.00 20.10 ? 565  ARG   A C   1 
ATOM   350  O  O   . ARG   A 1 43  ? 39.275 9.824   -4.108  1.00 16.53 ? 565  ARG   A O   1 
ATOM   351  C  CB  . ARG   A 1 43  ? 40.119 10.117  -1.154  1.00 24.37 ? 565  ARG   A CB  1 
ATOM   352  C  CG  . ARG   A 1 43  ? 40.881 8.852   -0.732  1.00 21.53 ? 565  ARG   A CG  1 
ATOM   353  C  CD  . ARG   A 1 43  ? 40.308 8.281   0.568   1.00 28.14 ? 565  ARG   A CD  1 
ATOM   354  N  NE  . ARG   A 1 43  ? 40.975 7.043   0.961   1.00 35.50 ? 565  ARG   A NE  1 
ATOM   355  C  CZ  . ARG   A 1 43  ? 40.542 6.211   1.904   1.00 36.64 ? 565  ARG   A CZ  1 
ATOM   356  N  NH1 . ARG   A 1 43  ? 39.429 6.451   2.581   1.00 39.98 ? 565  ARG   A NH1 1 
ATOM   357  N  NH2 . ARG   A 1 43  ? 41.242 5.105   2.171   1.00 33.68 ? 565  ARG   A NH2 1 
ATOM   358  N  N   . ASP   A 1 44  ? 41.441 9.126   -4.041  1.00 18.12 ? 566  ASP   A N   1 
ATOM   359  C  CA  . ASP   A 1 44  ? 41.241 8.110   -5.078  1.00 15.81 ? 566  ASP   A CA  1 
ATOM   360  C  C   . ASP   A 1 44  ? 40.237 7.068   -4.596  1.00 16.42 ? 566  ASP   A C   1 
ATOM   361  O  O   . ASP   A 1 44  ? 40.154 6.777   -3.406  1.00 18.75 ? 566  ASP   A O   1 
ATOM   362  C  CB  . ASP   A 1 44  ? 42.541 7.383   -5.431  1.00 15.13 ? 566  ASP   A CB  1 
ATOM   363  C  CG  . ASP   A 1 44  ? 43.586 8.297   -6.060  1.00 21.80 ? 566  ASP   A CG  1 
ATOM   364  O  OD1 . ASP   A 1 44  ? 43.211 9.241   -6.759  1.00 19.18 ? 566  ASP   A OD1 1 
ATOM   365  O  OD2 . ASP   A 1 44  ? 44.787 8.043   -5.882  1.00 22.21 ? 566  ASP   A OD2 1 
ATOM   366  N  N   . ASN   A 1 45  ? 39.473 6.516   -5.536  1.00 16.16 ? 567  ASN   A N   1 
ATOM   367  C  CA  . ASN   A 1 45  ? 38.476 5.485   -5.251  1.00 15.47 ? 567  ASN   A CA  1 
ATOM   368  C  C   . ASN   A 1 45  ? 38.591 4.352   -6.247  1.00 17.21 ? 567  ASN   A C   1 
ATOM   369  O  O   . ASN   A 1 45  ? 38.880 4.566   -7.427  1.00 19.54 ? 567  ASN   A O   1 
ATOM   370  C  CB  . ASN   A 1 45  ? 37.029 6.008   -5.344  1.00 15.22 ? 567  ASN   A CB  1 
ATOM   371  C  CG  . ASN   A 1 45  ? 36.576 6.668   -4.090  1.00 18.02 ? 567  ASN   A CG  1 
ATOM   372  O  OD1 . ASN   A 1 45  ? 35.800 6.097   -3.325  1.00 19.17 ? 567  ASN   A OD1 1 
ATOM   373  N  ND2 . ASN   A 1 45  ? 37.070 7.877   -3.849  1.00 17.88 ? 567  ASN   A ND2 1 
ATOM   374  N  N   . VAL   A 1 46  ? 38.322 3.141   -5.769  1.00 17.26 ? 568  VAL   A N   1 
ATOM   375  C  CA  . VAL   A 1 46  ? 37.968 2.026   -6.634  1.00 19.92 ? 568  VAL   A CA  1 
ATOM   376  C  C   . VAL   A 1 46  ? 36.587 1.590   -6.177  1.00 16.43 ? 568  VAL   A C   1 
ATOM   377  O  O   . VAL   A 1 46  ? 36.413 1.248   -4.994  1.00 18.31 ? 568  VAL   A O   1 
ATOM   378  C  CB  . VAL   A 1 46  ? 38.962 0.855   -6.543  1.00 18.66 ? 568  VAL   A CB  1 
ATOM   379  C  CG1 . VAL   A 1 46  ? 38.539 -0.256  -7.497  1.00 18.25 ? 568  VAL   A CG1 1 
ATOM   380  C  CG2 . VAL   A 1 46  ? 40.429 1.301   -6.835  1.00 19.63 ? 568  VAL   A CG2 1 
ATOM   381  N  N   . ALA   A 1 47  ? 35.611 1.636   -7.090  1.00 19.15 ? 569  ALA   A N   1 
ATOM   382  C  CA  . ALA   A 1 47  ? 34.210 1.322   -6.802  1.00 16.20 ? 569  ALA   A CA  1 
ATOM   383  C  C   . ALA   A 1 47  ? 33.780 0.165   -7.702  1.00 21.24 ? 569  ALA   A C   1 
ATOM   384  O  O   . ALA   A 1 47  ? 33.628 0.329   -8.925  1.00 20.69 ? 569  ALA   A O   1 
ATOM   385  C  CB  . ALA   A 1 47  ? 33.313 2.557   -6.993  1.00 18.62 ? 569  ALA   A CB  1 
ATOM   386  N  N   . VAL   A 1 48  ? 33.610 -1.005  -7.091  1.00 17.70 ? 570  VAL   A N   1 
ATOM   387  C  CA  . VAL   A 1 48  ? 33.089 -2.186  -7.764  1.00 17.12 ? 570  VAL   A CA  1 
ATOM   388  C  C   . VAL   A 1 48  ? 31.583 -2.185  -7.553  1.00 18.76 ? 570  VAL   A C   1 
ATOM   389  O  O   . VAL   A 1 48  ? 31.111 -2.163  -6.416  1.00 18.61 ? 570  VAL   A O   1 
ATOM   390  C  CB  . VAL   A 1 48  ? 33.735 -3.463  -7.199  1.00 18.29 ? 570  VAL   A CB  1 
ATOM   391  C  CG1 . VAL   A 1 48  ? 33.231 -4.695  -7.926  1.00 26.35 ? 570  VAL   A CG1 1 
ATOM   392  C  CG2 . VAL   A 1 48  ? 35.262 -3.352  -7.271  1.00 26.53 ? 570  VAL   A CG2 1 
ATOM   393  N  N   . MET   A 1 49  ? 30.831 -2.121  -8.641  1.00 20.72 ? 571  MET   A N   1 
ATOM   394  C  CA  . MET   A 1 49  ? 29.372 -2.138  -8.578  1.00 22.19 ? 571  MET   A CA  1 
ATOM   395  C  C   . MET   A 1 49  ? 28.895 -3.301  -9.438  1.00 26.83 ? 571  MET   A C   1 
ATOM   396  O  O   . MET   A 1 49  ? 29.009 -3.257  -10.665 1.00 29.07 ? 571  MET   A O   1 
ATOM   397  C  CB  . MET   A 1 49  ? 28.785 -0.799  -9.019  1.00 22.54 ? 571  MET   A CB  1 
ATOM   398  C  CG  . MET   A 1 49  ? 29.484 0.365   -8.299  1.00 29.31 ? 571  MET   A CG  1 
ATOM   399  S  SD  . MET   A 1 49  ? 28.774 2.024   -8.412  1.00 37.66 ? 571  MET   A SD  1 
ATOM   400  C  CE  . MET   A 1 49  ? 29.122 2.569   -6.754  1.00 32.84 ? 571  MET   A CE  1 
ATOM   401  N  N   . ALA   A 1 50  ? 28.368 -4.341  -8.781  1.00 26.72 ? 572  ALA   A N   1 
ATOM   402  C  CA  . ALA   A 1 50  ? 28.189 -5.648  -9.422  1.00 36.24 ? 572  ALA   A CA  1 
ATOM   403  C  C   . ALA   A 1 50  ? 27.398 -5.573  -10.724 1.00 36.64 ? 572  ALA   A C   1 
ATOM   404  O  O   . ALA   A 1 50  ? 27.696 -6.307  -11.676 1.00 38.42 ? 572  ALA   A O   1 
ATOM   405  C  CB  . ALA   A 1 50  ? 27.501 -6.615  -8.456  1.00 35.52 ? 572  ALA   A CB  1 
ATOM   406  N  N   . THR   A 1 51  ? 26.385 -4.702  -10.787 1.00 34.48 ? 573  THR   A N   1 
ATOM   407  C  CA  . THR   A 1 51  ? 25.530 -4.591  -11.970 1.00 42.89 ? 573  THR   A CA  1 
ATOM   408  C  C   . THR   A 1 51  ? 25.939 -3.480  -12.931 1.00 51.49 ? 573  THR   A C   1 
ATOM   409  O  O   . THR   A 1 51  ? 25.558 -3.537  -14.105 1.00 52.95 ? 573  THR   A O   1 
ATOM   410  C  CB  . THR   A 1 51  ? 24.062 -4.345  -11.579 1.00 43.42 ? 573  THR   A CB  1 
ATOM   411  O  OG1 . THR   A 1 51  ? 23.962 -3.139  -10.812 1.00 39.37 ? 573  THR   A OG1 1 
ATOM   412  C  CG2 . THR   A 1 51  ? 23.497 -5.504  -10.780 1.00 39.69 ? 573  THR   A CG2 1 
ATOM   413  N  N   . GLY   A 1 52  ? 26.687 -2.471  -12.475 1.00 42.61 ? 574  GLY   A N   1 
ATOM   414  C  CA  . GLY   A 1 52  ? 27.001 -1.315  -13.284 1.00 42.09 ? 574  GLY   A CA  1 
ATOM   415  C  C   . GLY   A 1 52  ? 26.030 -0.169  -13.110 1.00 53.84 ? 574  GLY   A C   1 
ATOM   416  O  O   . GLY   A 1 52  ? 26.409 0.993   -13.292 1.00 56.59 ? 574  GLY   A O   1 
ATOM   417  N  N   . TYR   A 1 53  ? 24.781 -0.469  -12.768 1.00 47.22 ? 575  TYR   A N   1 
ATOM   418  C  CA  . TYR   A 1 53  ? 23.849 0.585   -12.413 1.00 48.75 ? 575  TYR   A CA  1 
ATOM   419  C  C   . TYR   A 1 53  ? 24.396 1.382   -11.236 1.00 47.24 ? 575  TYR   A C   1 
ATOM   420  O  O   . TYR   A 1 53  ? 25.185 0.880   -10.430 1.00 56.12 ? 575  TYR   A O   1 
ATOM   421  C  CB  . TYR   A 1 53  ? 22.483 -0.010  -12.063 1.00 52.66 ? 575  TYR   A CB  1 
ATOM   422  C  CG  . TYR   A 1 53  ? 21.858 -0.799  -13.194 1.00 56.45 ? 575  TYR   A CG  1 
ATOM   423  C  CD1 . TYR   A 1 53  ? 21.845 -0.291  -14.487 1.00 60.30 ? 575  TYR   A CD1 1 
ATOM   424  C  CD2 . TYR   A 1 53  ? 21.291 -2.055  -12.975 1.00 54.99 ? 575  TYR   A CD2 1 
ATOM   425  C  CE1 . TYR   A 1 53  ? 21.282 -0.998  -15.528 1.00 62.10 ? 575  TYR   A CE1 1 
ATOM   426  C  CE2 . TYR   A 1 53  ? 20.723 -2.776  -14.017 1.00 50.79 ? 575  TYR   A CE2 1 
ATOM   427  C  CZ  . TYR   A 1 53  ? 20.724 -2.238  -15.292 1.00 61.22 ? 575  TYR   A CZ  1 
ATOM   428  O  OH  . TYR   A 1 53  ? 20.167 -2.925  -16.345 1.00 65.62 ? 575  TYR   A OH  1 
ATOM   429  N  N   . GLY   A 1 54  ? 23.986 2.641   -11.158 1.00 39.75 ? 576  GLY   A N   1 
ATOM   430  C  CA  . GLY   A 1 54  ? 24.298 3.493   -10.036 1.00 43.72 ? 576  GLY   A CA  1 
ATOM   431  C  C   . GLY   A 1 54  ? 25.671 4.135   -10.047 1.00 37.95 ? 576  GLY   A C   1 
ATOM   432  O  O   . GLY   A 1 54  ? 25.974 4.908   -9.130  1.00 41.24 ? 576  GLY   A O   1 
ATOM   433  N  N   . LYS   A 1 55  ? 26.511 3.875   -11.050 1.00 27.84 ? 577  LYS   A N   1 
ATOM   434  C  CA  . LYS   A 1 55  ? 27.836 4.472   -10.974 1.00 30.63 ? 577  LYS   A CA  1 
ATOM   435  C  C   . LYS   A 1 55  ? 27.885 5.892   -11.503 1.00 24.35 ? 577  LYS   A C   1 
ATOM   436  O  O   . LYS   A 1 55  ? 28.747 6.650   -11.054 1.00 24.97 ? 577  LYS   A O   1 
ATOM   437  C  CB  . LYS   A 1 55  ? 28.880 3.617   -11.689 1.00 28.33 ? 577  LYS   A CB  1 
ATOM   438  C  CG  . LYS   A 1 55  ? 28.662 3.288   -13.124 1.00 37.05 ? 577  LYS   A CG  1 
ATOM   439  C  CD  . LYS   A 1 55  ? 29.647 2.152   -13.452 1.00 34.54 ? 577  LYS   A CD  1 
ATOM   440  C  CE  . LYS   A 1 55  ? 29.586 1.693   -14.887 1.00 46.83 ? 577  LYS   A CE  1 
ATOM   441  N  NZ  . LYS   A 1 55  ? 30.471 0.500   -15.091 1.00 53.77 ? 577  LYS   A NZ  1 
ATOM   442  N  N   . SER   A 1 56  ? 26.962 6.286   -12.398 1.00 16.98 ? 578  SER   A N   1 
ATOM   443  C  CA  . SER   A 1 56  ? 27.073 7.580   -13.076 1.00 21.21 ? 578  SER   A CA  1 
ATOM   444  C  C   . SER   A 1 56  ? 27.097 8.742   -12.093 1.00 23.78 ? 578  SER   A C   1 
ATOM   445  O  O   . SER   A 1 56  ? 27.877 9.688   -12.257 1.00 23.39 ? 578  SER   A O   1 
ATOM   446  C  CB  . SER   A 1 56  ? 25.911 7.763   -14.055 1.00 30.09 ? 578  SER   A CB  1 
ATOM   447  O  OG  . SER   A 1 56  ? 26.264 7.216   -15.310 1.00 39.67 ? 578  SER   A OG  1 
ATOM   448  N  N   . LEU   A 1 57  ? 26.240 8.698   -11.075 1.00 23.84 ? 579  LEU   A N   1 
ATOM   449  C  CA  . LEU   A 1 57  ? 26.181 9.805   -10.129 1.00 22.93 ? 579  LEU   A CA  1 
ATOM   450  C  C   . LEU   A 1 57  ? 27.523 10.020  -9.436  1.00 22.21 ? 579  LEU   A C   1 
ATOM   451  O  O   . LEU   A 1 57  ? 27.889 11.168  -9.156  1.00 18.79 ? 579  LEU   A O   1 
ATOM   452  C  CB  . LEU   A 1 57  ? 25.089 9.562   -9.094  1.00 19.44 ? 579  LEU   A CB  1 
ATOM   453  C  CG  . LEU   A 1 57  ? 24.752 10.774  -8.218  1.00 17.39 ? 579  LEU   A CG  1 
ATOM   454  C  CD1 . LEU   A 1 57  ? 24.028 11.868  -9.040  1.00 17.70 ? 579  LEU   A CD1 1 
ATOM   455  C  CD2 . LEU   A 1 57  ? 23.916 10.380  -7.012  1.00 22.64 ? 579  LEU   A CD2 1 
ATOM   456  N  N   . CYS   A 1 58  ? 28.288 8.941   -9.212  1.00 20.09 ? 580  CYS   A N   1 
ATOM   457  C  CA  . CYS   A 1 58  ? 29.546 9.067   -8.486  1.00 21.72 ? 580  CYS   A CA  1 
ATOM   458  C  C   . CYS   A 1 58  ? 30.510 10.000  -9.195  1.00 22.39 ? 580  CYS   A C   1 
ATOM   459  O  O   . CYS   A 1 58  ? 31.279 10.712  -8.541  1.00 21.13 ? 580  CYS   A O   1 
ATOM   460  C  CB  . CYS   A 1 58  ? 30.220 7.707   -8.295  1.00 20.73 ? 580  CYS   A CB  1 
ATOM   461  S  SG  . CYS   A 1 58  ? 29.209 6.582   -7.302  1.00 27.34 ? 580  CYS   A SG  1 
ATOM   462  N  N   . PHE   A 1 59  ? 30.532 9.982   -10.529 1.00 19.27 ? 581  PHE   A N   1 
ATOM   463  C  CA  . PHE   A 1 59  ? 31.483 10.858  -11.209 1.00 20.05 ? 581  PHE   A CA  1 
ATOM   464  C  C   . PHE   A 1 59  ? 30.835 12.076  -11.850 1.00 22.89 ? 581  PHE   A C   1 
ATOM   465  O  O   . PHE   A 1 59  ? 31.545 13.027  -12.188 1.00 23.55 ? 581  PHE   A O   1 
ATOM   466  C  CB  . PHE   A 1 59  ? 32.308 10.087  -12.265 1.00 19.54 ? 581  PHE   A CB  1 
ATOM   467  C  CG  . PHE   A 1 59  ? 31.485 9.397   -13.339 1.00 23.83 ? 581  PHE   A CG  1 
ATOM   468  C  CD1 . PHE   A 1 59  ? 30.965 10.109  -14.411 1.00 21.83 ? 581  PHE   A CD1 1 
ATOM   469  C  CD2 . PHE   A 1 59  ? 31.291 8.020   -13.297 1.00 27.45 ? 581  PHE   A CD2 1 
ATOM   470  C  CE1 . PHE   A 1 59  ? 30.246 9.477   -15.395 1.00 25.53 ? 581  PHE   A CE1 1 
ATOM   471  C  CE2 . PHE   A 1 59  ? 30.562 7.372   -14.289 1.00 25.31 ? 581  PHE   A CE2 1 
ATOM   472  C  CZ  . PHE   A 1 59  ? 30.042 8.093   -15.333 1.00 25.15 ? 581  PHE   A CZ  1 
ATOM   473  N  N   . GLN   A 1 60  ? 29.514 12.093  -11.997 1.00 18.00 ? 582  GLN   A N   1 
ATOM   474  C  CA  . GLN   A 1 60  ? 28.857 13.272  -12.547 1.00 22.36 ? 582  GLN   A CA  1 
ATOM   475  C  C   . GLN   A 1 60  ? 28.571 14.308  -11.478 1.00 20.54 ? 582  GLN   A C   1 
ATOM   476  O  O   . GLN   A 1 60  ? 28.702 15.511  -11.730 1.00 19.00 ? 582  GLN   A O   1 
ATOM   477  C  CB  . GLN   A 1 60  ? 27.550 12.873  -13.249 1.00 20.98 ? 582  GLN   A CB  1 
ATOM   478  C  CG  . GLN   A 1 60  ? 27.801 12.083  -14.537 1.00 22.58 ? 582  GLN   A CG  1 
ATOM   479  C  CD  . GLN   A 1 60  ? 26.524 11.608  -15.187 1.00 26.43 ? 582  GLN   A CD  1 
ATOM   480  O  OE1 . GLN   A 1 60  ? 25.460 11.664  -14.583 1.00 25.08 ? 582  GLN   A OE1 1 
ATOM   481  N  NE2 . GLN   A 1 60  ? 26.624 11.143  -16.426 1.00 25.96 ? 582  GLN   A NE2 1 
ATOM   482  N  N   . TYR   A 1 61  ? 28.169 13.879  -10.289 1.00 18.54 ? 583  TYR   A N   1 
ATOM   483  C  CA  . TYR   A 1 61  ? 27.742 14.856  -9.293  1.00 16.59 ? 583  TYR   A CA  1 
ATOM   484  C  C   . TYR   A 1 61  ? 28.853 15.792  -8.838  1.00 20.32 ? 583  TYR   A C   1 
ATOM   485  O  O   . TYR   A 1 61  ? 28.593 17.008  -8.755  1.00 21.78 ? 583  TYR   A O   1 
ATOM   486  C  CB  . TYR   A 1 61  ? 27.111 14.129  -8.107  1.00 17.36 ? 583  TYR   A CB  1 
ATOM   487  C  CG  . TYR   A 1 61  ? 26.640 15.092  -7.044  1.00 17.12 ? 583  TYR   A CG  1 
ATOM   488  C  CD1 . TYR   A 1 61  ? 27.498 15.493  -6.028  1.00 18.39 ? 583  TYR   A CD1 1 
ATOM   489  C  CD2 . TYR   A 1 61  ? 25.345 15.591  -7.052  1.00 18.09 ? 583  TYR   A CD2 1 
ATOM   490  C  CE1 . TYR   A 1 61  ? 27.095 16.375  -5.060  1.00 18.28 ? 583  TYR   A CE1 1 
ATOM   491  C  CE2 . TYR   A 1 61  ? 24.920 16.472  -6.071  1.00 19.91 ? 583  TYR   A CE2 1 
ATOM   492  C  CZ  . TYR   A 1 61  ? 25.812 16.862  -5.087  1.00 24.02 ? 583  TYR   A CZ  1 
ATOM   493  O  OH  . TYR   A 1 61  ? 25.442 17.722  -4.086  1.00 22.10 ? 583  TYR   A OH  1 
ATOM   494  N  N   . PRO   A 1 62  ? 30.062 15.331  -8.490  1.00 17.92 ? 584  PRO   A N   1 
ATOM   495  C  CA  . PRO   A 1 62  ? 31.049 16.245  -7.861  1.00 17.74 ? 584  PRO   A CA  1 
ATOM   496  C  C   . PRO   A 1 62  ? 31.376 17.461  -8.723  1.00 19.33 ? 584  PRO   A C   1 
ATOM   497  O  O   . PRO   A 1 62  ? 31.313 18.595  -8.219  1.00 20.92 ? 584  PRO   A O   1 
ATOM   498  C  CB  . PRO   A 1 62  ? 32.268 15.344  -7.625  1.00 15.93 ? 584  PRO   A CB  1 
ATOM   499  C  CG  . PRO   A 1 62  ? 31.618 13.963  -7.368  1.00 18.55 ? 584  PRO   A CG  1 
ATOM   500  C  CD  . PRO   A 1 62  ? 30.480 13.915  -8.363  1.00 18.08 ? 584  PRO   A CD  1 
ATOM   501  N  N   . PRO   A 1 63  ? 31.713 17.303  -10.013 1.00 22.22 ? 585  PRO   A N   1 
ATOM   502  C  CA  . PRO   A 1 63  ? 32.042 18.507  -10.795 1.00 19.33 ? 585  PRO   A CA  1 
ATOM   503  C  C   . PRO   A 1 63  ? 30.849 19.415  -10.997 1.00 22.45 ? 585  PRO   A C   1 
ATOM   504  O  O   . PRO   A 1 63  ? 31.023 20.633  -11.108 1.00 21.31 ? 585  PRO   A O   1 
ATOM   505  C  CB  . PRO   A 1 63  ? 32.554 17.955  -12.128 1.00 17.78 ? 585  PRO   A CB  1 
ATOM   506  C  CG  . PRO   A 1 63  ? 32.014 16.591  -12.233 1.00 21.59 ? 585  PRO   A CG  1 
ATOM   507  C  CD  . PRO   A 1 63  ? 31.792 16.082  -10.843 1.00 21.06 ? 585  PRO   A CD  1 
ATOM   508  N  N   . VAL   A 1 64  ? 29.638 18.862  -11.052 1.00 19.22 ? 586  VAL   A N   1 
ATOM   509  C  CA  . VAL   A 1 64  ? 28.453 19.707  -11.186 1.00 18.98 ? 586  VAL   A CA  1 
ATOM   510  C  C   . VAL   A 1 64  ? 28.234 20.524  -9.928  1.00 22.45 ? 586  VAL   A C   1 
ATOM   511  O  O   . VAL   A 1 64  ? 27.930 21.724  -9.990  1.00 25.47 ? 586  VAL   A O   1 
ATOM   512  C  CB  . VAL   A 1 64  ? 27.221 18.848  -11.506 1.00 18.46 ? 586  VAL   A CB  1 
ATOM   513  C  CG1 . VAL   A 1 64  ? 25.952 19.702  -11.382 1.00 22.39 ? 586  VAL   A CG1 1 
ATOM   514  C  CG2 . VAL   A 1 64  ? 27.364 18.278  -12.886 1.00 23.67 ? 586  VAL   A CG2 1 
ATOM   515  N  N   . TYR   A 1 65  ? 28.360 19.892  -8.768  1.00 18.60 ? 587  TYR   A N   1 
ATOM   516  C  CA  . TYR   A 1 65  ? 28.188 20.612  -7.511  1.00 23.81 ? 587  TYR   A CA  1 
ATOM   517  C  C   . TYR   A 1 65  ? 29.174 21.769  -7.393  1.00 27.19 ? 587  TYR   A C   1 
ATOM   518  O  O   . TYR   A 1 65  ? 28.788 22.903  -7.076  1.00 25.65 ? 587  TYR   A O   1 
ATOM   519  C  CB  . TYR   A 1 65  ? 28.346 19.657  -6.324  1.00 22.03 ? 587  TYR   A CB  1 
ATOM   520  C  CG  . TYR   A 1 65  ? 28.285 20.369  -4.997  1.00 24.68 ? 587  TYR   A CG  1 
ATOM   521  C  CD1 . TYR   A 1 65  ? 27.110 21.014  -4.589  1.00 26.52 ? 587  TYR   A CD1 1 
ATOM   522  C  CD2 . TYR   A 1 65  ? 29.410 20.442  -4.165  1.00 24.03 ? 587  TYR   A CD2 1 
ATOM   523  C  CE1 . TYR   A 1 65  ? 27.049 21.685  -3.384  1.00 21.86 ? 587  TYR   A CE1 1 
ATOM   524  C  CE2 . TYR   A 1 65  ? 29.351 21.117  -2.943  1.00 23.36 ? 587  TYR   A CE2 1 
ATOM   525  C  CZ  . TYR   A 1 65  ? 28.167 21.732  -2.572  1.00 27.71 ? 587  TYR   A CZ  1 
ATOM   526  O  OH  . TYR   A 1 65  ? 28.079 22.402  -1.377  1.00 31.96 ? 587  TYR   A OH  1 
ATOM   527  N  N   . VAL   A 1 66  ? 30.459 21.510  -7.628  1.00 22.27 ? 588  VAL   A N   1 
ATOM   528  C  CA  . VAL   A 1 66  ? 31.422 22.585  -7.408  1.00 24.84 ? 588  VAL   A CA  1 
ATOM   529  C  C   . VAL   A 1 66  ? 31.578 23.484  -8.627  1.00 24.96 ? 588  VAL   A C   1 
ATOM   530  O  O   . VAL   A 1 66  ? 32.269 24.513  -8.535  1.00 22.74 ? 588  VAL   A O   1 
ATOM   531  C  CB  . VAL   A 1 66  ? 32.795 22.029  -6.959  1.00 27.83 ? 588  VAL   A CB  1 
ATOM   532  C  CG1 . VAL   A 1 66  ? 32.638 21.248  -5.661  1.00 26.75 ? 588  VAL   A CG1 1 
ATOM   533  C  CG2 . VAL   A 1 66  ? 33.418 21.150  -8.027  1.00 21.94 ? 588  VAL   A CG2 1 
ATOM   534  N  N   . GLY   A 1 67  ? 30.938 23.157  -9.745  1.00 24.16 ? 589  GLY   A N   1 
ATOM   535  C  CA  . GLY   A 1 67  ? 30.998 24.013  -10.920 1.00 25.27 ? 589  GLY   A CA  1 
ATOM   536  C  C   . GLY   A 1 67  ? 32.329 24.042  -11.649 1.00 31.23 ? 589  GLY   A C   1 
ATOM   537  O  O   . GLY   A 1 67  ? 32.681 25.059  -12.250 1.00 27.15 ? 589  GLY   A O   1 
ATOM   538  N  N   . LYS   A 1 68  ? 33.085 22.934  -11.612 1.00 22.48 ? 590  LYS   A N   1 
ATOM   539  C  CA  . LYS   A 1 68  ? 34.379 22.860  -12.290 1.00 21.74 ? 590  LYS   A CA  1 
ATOM   540  C  C   . LYS   A 1 68  ? 34.311 21.833  -13.421 1.00 26.92 ? 590  LYS   A C   1 
ATOM   541  O  O   . LYS   A 1 68  ? 33.381 21.881  -14.226 1.00 31.43 ? 590  LYS   A O   1 
ATOM   542  C  CB  . LYS   A 1 68  ? 35.489 22.525  -11.313 1.00 22.95 ? 590  LYS   A CB  1 
ATOM   543  C  CG  . LYS   A 1 68  ? 35.602 23.467  -10.147 1.00 27.81 ? 590  LYS   A CG  1 
ATOM   544  C  CD  . LYS   A 1 68  ? 35.979 24.863  -10.597 1.00 36.47 ? 590  LYS   A CD  1 
ATOM   545  C  CE  . LYS   A 1 68  ? 36.325 25.734  -9.385  1.00 44.70 ? 590  LYS   A CE  1 
ATOM   546  N  NZ  . LYS   A 1 68  ? 37.409 25.077  -8.581  1.00 50.27 ? 590  LYS   A NZ  1 
ATOM   547  N  N   . ILE   A 1 69  ? 35.275 20.902  -13.503 1.00 20.32 ? 591  ILE   A N   1 
ATOM   548  C  CA  . ILE   A 1 69  ? 35.359 19.939  -14.608 1.00 23.72 ? 591  ILE   A CA  1 
ATOM   549  C  C   . ILE   A 1 69  ? 35.589 18.538  -14.065 1.00 22.24 ? 591  ILE   A C   1 
ATOM   550  O  O   . ILE   A 1 69  ? 36.464 18.334  -13.209 1.00 21.23 ? 591  ILE   A O   1 
ATOM   551  C  CB  . ILE   A 1 69  ? 36.494 20.256  -15.604 1.00 26.52 ? 591  ILE   A CB  1 
ATOM   552  C  CG1 . ILE   A 1 69  ? 36.282 21.592  -16.304 1.00 32.53 ? 591  ILE   A CG1 1 
ATOM   553  C  CG2 . ILE   A 1 69  ? 36.572 19.173  -16.664 1.00 28.33 ? 591  ILE   A CG2 1 
ATOM   554  C  CD1 . ILE   A 1 69  ? 37.383 21.887  -17.355 1.00 31.47 ? 591  ILE   A CD1 1 
ATOM   555  N  N   . GLY   A 1 70  ? 34.850 17.573  -14.599 1.00 19.99 ? 592  GLY   A N   1 
ATOM   556  C  CA  . GLY   A 1 70  ? 35.164 16.174  -14.404 1.00 19.70 ? 592  GLY   A CA  1 
ATOM   557  C  C   . GLY   A 1 70  ? 35.488 15.539  -15.740 1.00 21.78 ? 592  GLY   A C   1 
ATOM   558  O  O   . GLY   A 1 70  ? 34.843 15.836  -16.751 1.00 23.51 ? 592  GLY   A O   1 
ATOM   559  N  N   . LEU   A 1 71  ? 36.521 14.703  -15.748 1.00 16.08 ? 593  LEU   A N   1 
ATOM   560  C  CA  . LEU   A 1 71  ? 36.949 13.992  -16.942 1.00 15.93 ? 593  LEU   A CA  1 
ATOM   561  C  C   . LEU   A 1 71  ? 36.496 12.546  -16.787 1.00 21.21 ? 593  LEU   A C   1 
ATOM   562  O  O   . LEU   A 1 71  ? 36.637 11.979  -15.701 1.00 21.98 ? 593  LEU   A O   1 
ATOM   563  C  CB  . LEU   A 1 71  ? 38.472 14.054  -17.073 1.00 21.73 ? 593  LEU   A CB  1 
ATOM   564  C  CG  . LEU   A 1 71  ? 39.047 13.466  -18.357 1.00 30.62 ? 593  LEU   A CG  1 
ATOM   565  C  CD1 . LEU   A 1 71  ? 38.760 14.390  -19.548 1.00 24.47 ? 593  LEU   A CD1 1 
ATOM   566  C  CD2 . LEU   A 1 71  ? 40.545 13.231  -18.205 1.00 28.92 ? 593  LEU   A CD2 1 
ATOM   567  N  N   . VAL   A 1 72  ? 35.922 11.974  -17.839 1.00 19.91 ? 594  VAL   A N   1 
ATOM   568  C  CA  . VAL   A 1 72  ? 35.445 10.588  -17.811 1.00 19.60 ? 594  VAL   A CA  1 
ATOM   569  C  C   . VAL   A 1 72  ? 36.120 9.852   -18.948 1.00 21.12 ? 594  VAL   A C   1 
ATOM   570  O  O   . VAL   A 1 72  ? 35.928 10.208  -20.115 1.00 23.47 ? 594  VAL   A O   1 
ATOM   571  C  CB  . VAL   A 1 72  ? 33.913 10.491  -17.959 1.00 19.24 ? 594  VAL   A CB  1 
ATOM   572  C  CG1 . VAL   A 1 72  ? 33.452 8.997   -17.959 1.00 20.97 ? 594  VAL   A CG1 1 
ATOM   573  C  CG2 . VAL   A 1 72  ? 33.216 11.309  -16.874 1.00 20.29 ? 594  VAL   A CG2 1 
ATOM   574  N  N   . ILE   A 1 73  ? 36.889 8.818   -18.615 1.00 18.19 ? 595  ILE   A N   1 
ATOM   575  C  CA  . ILE   A 1 73  ? 37.681 8.068   -19.573 1.00 17.27 ? 595  ILE   A CA  1 
ATOM   576  C  C   . ILE   A 1 73  ? 36.998 6.729   -19.777 1.00 22.66 ? 595  ILE   A C   1 
ATOM   577  O  O   . ILE   A 1 73  ? 36.854 5.963   -18.823 1.00 21.58 ? 595  ILE   A O   1 
ATOM   578  C  CB  . ILE   A 1 73  ? 39.120 7.864   -19.074 1.00 19.00 ? 595  ILE   A CB  1 
ATOM   579  C  CG1 . ILE   A 1 73  ? 39.803 9.233   -18.888 1.00 18.33 ? 595  ILE   A CG1 1 
ATOM   580  C  CG2 . ILE   A 1 73  ? 39.908 7.021   -20.068 1.00 24.13 ? 595  ILE   A CG2 1 
ATOM   581  C  CD1 . ILE   A 1 73  ? 41.057 9.161   -18.077 1.00 19.13 ? 595  ILE   A CD1 1 
ATOM   582  N  N   . SER   A 1 74  ? 36.615 6.424   -21.011 1.00 23.04 ? 596  SER   A N   1 
ATOM   583  C  CA  . SER   A 1 74  ? 35.912 5.165   -21.232 1.00 23.24 ? 596  SER   A CA  1 
ATOM   584  C  C   . SER   A 1 74  ? 36.110 4.729   -22.670 1.00 30.78 ? 596  SER   A C   1 
ATOM   585  O  O   . SER   A 1 74  ? 36.294 5.578   -23.550 1.00 25.63 ? 596  SER   A O   1 
ATOM   586  C  CB  . SER   A 1 74  ? 34.415 5.306   -20.927 1.00 23.20 ? 596  SER   A CB  1 
ATOM   587  O  OG  . SER   A 1 74  ? 33.718 4.099   -21.230 1.00 30.98 ? 596  SER   A OG  1 
ATOM   588  N  N   . PRO   A 1 75  ? 36.084 3.421   -22.946 1.00 32.44 ? 597  PRO   A N   1 
ATOM   589  C  CA  . PRO   A 1 75  ? 36.138 2.964   -24.337 1.00 32.74 ? 597  PRO   A CA  1 
ATOM   590  C  C   . PRO   A 1 75  ? 34.768 2.820   -24.969 1.00 32.73 ? 597  PRO   A C   1 
ATOM   591  O  O   . PRO   A 1 75  ? 34.690 2.611   -26.186 1.00 34.52 ? 597  PRO   A O   1 
ATOM   592  C  CB  . PRO   A 1 75  ? 36.850 1.609   -24.219 1.00 32.86 ? 597  PRO   A CB  1 
ATOM   593  C  CG  . PRO   A 1 75  ? 36.462 1.101   -22.887 1.00 30.98 ? 597  PRO   A CG  1 
ATOM   594  C  CD  . PRO   A 1 75  ? 36.199 2.303   -21.996 1.00 29.91 ? 597  PRO   A CD  1 
ATOM   595  N  N   . LEU   A 1 76  ? 33.698 2.962   -24.181 1.00 31.61 ? 598  LEU   A N   1 
ATOM   596  C  CA  . LEU   A 1 76  ? 32.338 2.663   -24.627 1.00 30.89 ? 598  LEU   A CA  1 
ATOM   597  C  C   . LEU   A 1 76  ? 31.765 3.914   -25.277 1.00 30.32 ? 598  LEU   A C   1 
ATOM   598  O  O   . LEU   A 1 76  ? 31.012 4.671   -24.669 1.00 33.23 ? 598  LEU   A O   1 
ATOM   599  C  CB  . LEU   A 1 76  ? 31.481 2.215   -23.453 1.00 29.11 ? 598  LEU   A CB  1 
ATOM   600  C  CG  . LEU   A 1 76  ? 32.041 1.077   -22.605 1.00 33.55 ? 598  LEU   A CG  1 
ATOM   601  C  CD1 . LEU   A 1 76  ? 31.107 0.769   -21.449 1.00 30.20 ? 598  LEU   A CD1 1 
ATOM   602  C  CD2 . LEU   A 1 76  ? 32.264 -0.142  -23.462 1.00 32.13 ? 598  LEU   A CD2 1 
ATOM   603  N  N   . ILE   A 1 77  ? 32.106 4.097   -26.554 1.00 33.96 ? 599  ILE   A N   1 
ATOM   604  C  CA  . ILE   A 1 77  ? 31.808 5.345   -27.257 1.00 33.75 ? 599  ILE   A CA  1 
ATOM   605  C  C   . ILE   A 1 77  ? 30.315 5.654   -27.230 1.00 36.61 ? 599  ILE   A C   1 
ATOM   606  O  O   . ILE   A 1 77  ? 29.898 6.751   -26.842 1.00 34.73 ? 599  ILE   A O   1 
ATOM   607  C  CB  . ILE   A 1 77  ? 32.322 5.277   -28.702 1.00 38.64 ? 599  ILE   A CB  1 
ATOM   608  C  CG1 . ILE   A 1 77  ? 33.808 4.956   -28.714 1.00 42.76 ? 599  ILE   A CG1 1 
ATOM   609  C  CG2 . ILE   A 1 77  ? 32.059 6.600   -29.406 1.00 41.14 ? 599  ILE   A CG2 1 
ATOM   610  C  CD1 . ILE   A 1 77  ? 34.626 6.120   -28.329 1.00 38.23 ? 599  ILE   A CD1 1 
ATOM   611  N  N   . SER   A 1 78  ? 29.491 4.705   -27.676 1.00 32.43 ? 600  SER   A N   1 
ATOM   612  C  CA  . SER   A 1 78  ? 28.075 5.012   -27.819 1.00 36.84 ? 600  SER   A CA  1 
ATOM   613  C  C   . SER   A 1 78  ? 27.445 5.330   -26.473 1.00 30.87 ? 600  SER   A C   1 
ATOM   614  O  O   . SER   A 1 78  ? 26.602 6.226   -26.377 1.00 35.21 ? 600  SER   A O   1 
ATOM   615  C  CB  . SER   A 1 78  ? 27.343 3.864   -28.514 1.00 35.94 ? 600  SER   A CB  1 
ATOM   616  O  OG  . SER   A 1 78  ? 27.490 2.666   -27.782 1.00 40.30 ? 600  SER   A OG  1 
ATOM   617  N  N   . LEU   A 1 79  ? 27.847 4.624   -25.411 1.00 31.26 ? 601  LEU   A N   1 
ATOM   618  C  CA  . LEU   A 1 79  ? 27.253 4.930   -24.111 1.00 30.64 ? 601  LEU   A CA  1 
ATOM   619  C  C   . LEU   A 1 79  ? 27.680 6.315   -23.642 1.00 28.47 ? 601  LEU   A C   1 
ATOM   620  O  O   . LEU   A 1 79  ? 26.881 7.059   -23.060 1.00 30.35 ? 601  LEU   A O   1 
ATOM   621  C  CB  . LEU   A 1 79  ? 27.629 3.871   -23.073 1.00 27.98 ? 601  LEU   A CB  1 
ATOM   622  C  CG  . LEU   A 1 79  ? 27.197 4.249   -21.650 1.00 32.91 ? 601  LEU   A CG  1 
ATOM   623  C  CD1 . LEU   A 1 79  ? 25.702 4.572   -21.591 1.00 49.34 ? 601  LEU   A CD1 1 
ATOM   624  C  CD2 . LEU   A 1 79  ? 27.553 3.168   -20.644 1.00 45.51 ? 601  LEU   A CD2 1 
ATOM   625  N  N   . MET   A 1 80  ? 28.933 6.678   -23.900 1.00 25.54 ? 602  MET   A N   1 
ATOM   626  C  CA  . MET   A 1 80  ? 29.388 8.023   -23.556 1.00 31.89 ? 602  MET   A CA  1 
ATOM   627  C  C   . MET   A 1 80  ? 28.573 9.092   -24.282 1.00 32.76 ? 602  MET   A C   1 
ATOM   628  O  O   . MET   A 1 80  ? 28.169 10.095  -23.678 1.00 28.02 ? 602  MET   A O   1 
ATOM   629  C  CB  . MET   A 1 80  ? 30.872 8.161   -23.870 1.00 28.45 ? 602  MET   A CB  1 
ATOM   630  C  CG  . MET   A 1 80  ? 31.791 7.639   -22.758 1.00 36.72 ? 602  MET   A CG  1 
ATOM   631  S  SD  . MET   A 1 80  ? 33.547 7.919   -23.135 1.00 46.33 ? 602  MET   A SD  1 
ATOM   632  C  CE  . MET   A 1 80  ? 33.614 6.802   -24.509 1.00 27.65 ? 602  MET   A CE  1 
ATOM   633  N  N   . GLU   A 1 81  ? 28.325 8.898   -25.580 1.00 33.10 ? 603  GLU   A N   1 
ATOM   634  C  CA  . GLU   A 1 81  ? 27.506 9.858   -26.320 1.00 34.20 ? 603  GLU   A CA  1 
ATOM   635  C  C   . GLU   A 1 81  ? 26.090 9.921   -25.764 1.00 32.94 ? 603  GLU   A C   1 
ATOM   636  O  O   . GLU   A 1 81  ? 25.488 11.005  -25.672 1.00 29.39 ? 603  GLU   A O   1 
ATOM   637  C  CB  . GLU   A 1 81  ? 27.494 9.489   -27.799 1.00 34.25 ? 603  GLU   A CB  1 
ATOM   638  C  CG  . GLU   A 1 81  ? 28.868 9.616   -28.427 1.00 40.02 ? 603  GLU   A CG  1 
ATOM   639  C  CD  . GLU   A 1 81  ? 28.929 9.026   -29.816 1.00 47.51 ? 603  GLU   A CD  1 
ATOM   640  O  OE1 . GLU   A 1 81  ? 28.041 8.212   -30.157 1.00 50.09 ? 603  GLU   A OE1 1 
ATOM   641  O  OE2 . GLU   A 1 81  ? 29.865 9.375   -30.565 1.00 49.81 ? 603  GLU   A OE2 1 
ATOM   642  N  N   . ASP   A 1 82  ? 25.540 8.763   -25.378 1.00 34.37 ? 604  ASP   A N   1 
ATOM   643  C  CA  . ASP   A 1 82  ? 24.235 8.750   -24.729 1.00 31.71 ? 604  ASP   A CA  1 
ATOM   644  C  C   . ASP   A 1 82  ? 24.238 9.603   -23.471 1.00 32.31 ? 604  ASP   A C   1 
ATOM   645  O  O   . ASP   A 1 82  ? 23.329 10.413  -23.249 1.00 32.76 ? 604  ASP   A O   1 
ATOM   646  C  CB  . ASP   A 1 82  ? 23.829 7.318   -24.387 1.00 35.81 ? 604  ASP   A CB  1 
ATOM   647  C  CG  . ASP   A 1 82  ? 23.357 6.545   -25.590 1.00 51.98 ? 604  ASP   A CG  1 
ATOM   648  O  OD1 . ASP   A 1 82  ? 23.127 7.179   -26.646 1.00 54.91 ? 604  ASP   A OD1 1 
ATOM   649  O  OD2 . ASP   A 1 82  ? 23.233 5.305   -25.478 1.00 56.89 ? 604  ASP   A OD2 1 
ATOM   650  N  N   . GLN   A 1 83  ? 25.265 9.431   -22.632 1.00 33.53 ? 605  GLN   A N   1 
ATOM   651  C  CA  . GLN   A 1 83  ? 25.306 10.167  -21.373 1.00 30.05 ? 605  GLN   A CA  1 
ATOM   652  C  C   . GLN   A 1 83  ? 25.461 11.668  -21.609 1.00 27.28 ? 605  GLN   A C   1 
ATOM   653  O  O   . GLN   A 1 83  ? 24.853 12.477  -20.900 1.00 29.59 ? 605  GLN   A O   1 
ATOM   654  C  CB  . GLN   A 1 83  ? 26.426 9.630   -20.485 1.00 30.97 ? 605  GLN   A CB  1 
ATOM   655  C  CG  . GLN   A 1 83  ? 26.170 8.198   -20.035 1.00 30.74 ? 605  GLN   A CG  1 
ATOM   656  C  CD  . GLN   A 1 83  ? 27.038 7.781   -18.869 1.00 45.39 ? 605  GLN   A CD  1 
ATOM   657  O  OE1 . GLN   A 1 83  ? 28.095 8.368   -18.617 1.00 42.84 ? 605  GLN   A OE1 1 
ATOM   658  N  NE2 . GLN   A 1 83  ? 26.595 6.763   -18.145 1.00 39.79 ? 605  GLN   A NE2 1 
ATOM   659  N  N   . VAL   A 1 84  ? 26.265 12.060  -22.594 1.00 31.54 ? 606  VAL   A N   1 
ATOM   660  C  CA  . VAL   A 1 84  ? 26.320 13.474  -22.964 1.00 26.91 ? 606  VAL   A CA  1 
ATOM   661  C  C   . VAL   A 1 84  ? 24.922 14.001  -23.292 1.00 34.24 ? 606  VAL   A C   1 
ATOM   662  O  O   . VAL   A 1 84  ? 24.530 15.097  -22.851 1.00 29.99 ? 606  VAL   A O   1 
ATOM   663  C  CB  . VAL   A 1 84  ? 27.295 13.676  -24.136 1.00 26.60 ? 606  VAL   A CB  1 
ATOM   664  C  CG1 . VAL   A 1 84  ? 27.120 15.053  -24.715 1.00 29.74 ? 606  VAL   A CG1 1 
ATOM   665  C  CG2 . VAL   A 1 84  ? 28.723 13.464  -23.659 1.00 32.50 ? 606  VAL   A CG2 1 
ATOM   666  N  N   . LEU   A 1 85  ? 24.145 13.234  -24.069 1.00 27.32 ? 607  LEU   A N   1 
ATOM   667  C  CA  . LEU   A 1 85  ? 22.775 13.658  -24.379 1.00 33.23 ? 607  LEU   A CA  1 
ATOM   668  C  C   . LEU   A 1 85  ? 21.947 13.846  -23.114 1.00 28.41 ? 607  LEU   A C   1 
ATOM   669  O  O   . LEU   A 1 85  ? 21.263 14.860  -22.948 1.00 32.27 ? 607  LEU   A O   1 
ATOM   670  C  CB  . LEU   A 1 85  ? 22.101 12.633  -25.290 1.00 33.36 ? 607  LEU   A CB  1 
ATOM   671  C  CG  . LEU   A 1 85  ? 22.377 12.795  -26.777 1.00 39.13 ? 607  LEU   A CG  1 
ATOM   672  C  CD1 . LEU   A 1 85  ? 21.404 11.939  -27.581 1.00 37.74 ? 607  LEU   A CD1 1 
ATOM   673  C  CD2 . LEU   A 1 85  ? 22.292 14.275  -27.170 1.00 41.32 ? 607  LEU   A CD2 1 
ATOM   674  N  N   . GLN   A 1 86  ? 21.969 12.851  -22.222 1.00 33.85 ? 608  GLN   A N   1 
ATOM   675  C  CA  . GLN   A 1 86  ? 21.172 12.930  -20.993 1.00 28.28 ? 608  GLN   A CA  1 
ATOM   676  C  C   . GLN   A 1 86  ? 21.577 14.125  -20.135 1.00 28.74 ? 608  GLN   A C   1 
ATOM   677  O  O   . GLN   A 1 86  ? 20.723 14.842  -19.580 1.00 28.74 ? 608  GLN   A O   1 
ATOM   678  C  CB  . GLN   A 1 86  ? 21.320 11.638  -20.184 1.00 31.88 ? 608  GLN   A CB  1 
ATOM   679  C  CG  . GLN   A 1 86  ? 20.264 10.558  -20.442 1.00 45.61 ? 608  GLN   A CG  1 
ATOM   680  C  CD  . GLN   A 1 86  ? 20.681 9.555   -21.507 1.00 62.06 ? 608  GLN   A CD  1 
ATOM   681  O  OE1 . GLN   A 1 86  ? 21.034 9.932   -22.626 1.00 61.55 ? 608  GLN   A OE1 1 
ATOM   682  N  NE2 . GLN   A 1 86  ? 20.637 8.266   -21.163 1.00 63.16 ? 608  GLN   A NE2 1 
ATOM   683  N  N   . LEU   A 1 87  ? 22.886 14.337  -19.986 1.00 25.70 ? 609  LEU   A N   1 
ATOM   684  C  CA  . LEU   A 1 87  ? 23.365 15.485  -19.235 1.00 25.75 ? 609  LEU   A CA  1 
ATOM   685  C  C   . LEU   A 1 87  ? 22.816 16.769  -19.825 1.00 31.12 ? 609  LEU   A C   1 
ATOM   686  O  O   . LEU   A 1 87  ? 22.295 17.626  -19.103 1.00 28.92 ? 609  LEU   A O   1 
ATOM   687  C  CB  . LEU   A 1 87  ? 24.896 15.510  -19.221 1.00 21.03 ? 609  LEU   A CB  1 
ATOM   688  C  CG  . LEU   A 1 87  ? 25.495 14.363  -18.409 1.00 24.34 ? 609  LEU   A CG  1 
ATOM   689  C  CD1 . LEU   A 1 87  ? 26.966 14.107  -18.770 1.00 26.10 ? 609  LEU   A CD1 1 
ATOM   690  C  CD2 . LEU   A 1 87  ? 25.340 14.683  -16.923 1.00 25.53 ? 609  LEU   A CD2 1 
ATOM   691  N  N   . LYS   A 1 88  ? 22.934 16.927  -21.142 1.00 29.79 ? 610  LYS   A N   1 
ATOM   692  C  CA  . LYS   A 1 88  ? 22.473 18.178  -21.725 1.00 32.24 ? 610  LYS   A CA  1 
ATOM   693  C  C   . LYS   A 1 88  ? 20.967 18.335  -21.541 1.00 35.95 ? 610  LYS   A C   1 
ATOM   694  O  O   . LYS   A 1 88  ? 20.483 19.453  -21.335 1.00 36.51 ? 610  LYS   A O   1 
ATOM   695  C  CB  . LYS   A 1 88  ? 22.907 18.253  -23.191 1.00 37.25 ? 610  LYS   A CB  1 
ATOM   696  C  CG  . LYS   A 1 88  ? 24.442 18.446  -23.329 1.00 30.55 ? 610  LYS   A CG  1 
ATOM   697  C  CD  . LYS   A 1 88  ? 24.903 18.755  -24.750 1.00 38.37 ? 610  LYS   A CD  1 
ATOM   698  C  CE  . LYS   A 1 88  ? 24.726 17.566  -25.670 1.00 42.62 ? 610  LYS   A CE  1 
ATOM   699  N  NZ  . LYS   A 1 88  ? 25.569 17.680  -26.909 1.00 50.21 ? 610  LYS   A NZ  1 
ATOM   700  N  N   . MET   A 1 89  ? 20.229 17.217  -21.522 1.00 33.66 ? 611  MET   A N   1 
ATOM   701  C  CA  . MET   A 1 89  ? 18.800 17.262  -21.202 1.00 37.49 ? 611  MET   A CA  1 
ATOM   702  C  C   . MET   A 1 89  ? 18.546 17.771  -19.789 1.00 36.88 ? 611  MET   A C   1 
ATOM   703  O  O   . MET   A 1 89  ? 17.488 18.354  -19.528 1.00 38.32 ? 611  MET   A O   1 
ATOM   704  C  CB  . MET   A 1 89  ? 18.165 15.876  -21.363 1.00 35.61 ? 611  MET   A CB  1 
ATOM   705  C  CG  . MET   A 1 89  ? 17.795 15.485  -22.783 1.00 44.70 ? 611  MET   A CG  1 
ATOM   706  S  SD  . MET   A 1 89  ? 17.804 13.686  -23.018 1.00 54.27 ? 611  MET   A SD  1 
ATOM   707  C  CE  . MET   A 1 89  ? 16.624 13.152  -21.793 1.00 49.64 ? 611  MET   A CE  1 
ATOM   708  N  N   . SER   A 1 90  ? 19.477 17.539  -18.860 1.00 33.26 ? 612  SER   A N   1 
ATOM   709  C  CA  . SER   A 1 90  ? 19.347 18.064  -17.501 1.00 26.37 ? 612  SER   A CA  1 
ATOM   710  C  C   . SER   A 1 90  ? 19.964 19.451  -17.303 1.00 28.72 ? 612  SER   A C   1 
ATOM   711  O  O   . SER   A 1 90  ? 20.147 19.858  -16.153 1.00 34.01 ? 612  SER   A O   1 
ATOM   712  C  CB  . SER   A 1 90  ? 19.988 17.109  -16.488 1.00 36.89 ? 612  SER   A CB  1 
ATOM   713  O  OG  . SER   A 1 90  ? 19.497 15.785  -16.603 1.00 40.30 ? 612  SER   A OG  1 
ATOM   714  N  N   . ASN   A 1 91  ? 20.297 20.178  -18.373 1.00 33.85 ? 613  ASN   A N   1 
ATOM   715  C  CA  . ASN   A 1 91  ? 20.954 21.490  -18.312 1.00 37.22 ? 613  ASN   A CA  1 
ATOM   716  C  C   . ASN   A 1 91  ? 22.397 21.413  -17.822 1.00 31.79 ? 613  ASN   A C   1 
ATOM   717  O  O   . ASN   A 1 91  ? 22.942 22.410  -17.361 1.00 33.51 ? 613  ASN   A O   1 
ATOM   718  C  CB  . ASN   A 1 91  ? 20.204 22.503  -17.425 1.00 42.10 ? 613  ASN   A CB  1 
ATOM   719  C  CG  . ASN   A 1 91  ? 18.853 22.910  -17.981 1.00 56.53 ? 613  ASN   A CG  1 
ATOM   720  O  OD1 . ASN   A 1 91  ? 18.629 22.910  -19.194 1.00 53.31 ? 613  ASN   A OD1 1 
ATOM   721  N  ND2 . ASN   A 1 91  ? 17.943 23.276  -17.084 1.00 56.34 ? 613  ASN   A ND2 1 
ATOM   722  N  N   . ILE   A 1 92  ? 23.041 20.254  -17.897 1.00 30.35 ? 614  ILE   A N   1 
ATOM   723  C  CA  . ILE   A 1 92  ? 24.441 20.116  -17.505 1.00 23.49 ? 614  ILE   A CA  1 
ATOM   724  C  C   . ILE   A 1 92  ? 25.278 20.154  -18.779 1.00 26.60 ? 614  ILE   A C   1 
ATOM   725  O  O   . ILE   A 1 92  ? 25.175 19.228  -19.598 1.00 27.61 ? 614  ILE   A O   1 
ATOM   726  C  CB  . ILE   A 1 92  ? 24.689 18.815  -16.733 1.00 26.88 ? 614  ILE   A CB  1 
ATOM   727  C  CG1 . ILE   A 1 92  ? 23.871 18.801  -15.442 1.00 24.71 ? 614  ILE   A CG1 1 
ATOM   728  C  CG2 . ILE   A 1 92  ? 26.207 18.627  -16.453 1.00 24.17 ? 614  ILE   A CG2 1 
ATOM   729  C  CD1 . ILE   A 1 92  ? 23.830 17.449  -14.801 1.00 25.31 ? 614  ILE   A CD1 1 
ATOM   730  N  N   . PRO   A 1 93  ? 26.109 21.169  -18.983 1.00 26.97 ? 615  PRO   A N   1 
ATOM   731  C  CA  . PRO   A 1 93  ? 26.976 21.185  -20.167 1.00 24.08 ? 615  PRO   A CA  1 
ATOM   732  C  C   . PRO   A 1 93  ? 27.962 20.028  -20.119 1.00 26.80 ? 615  PRO   A C   1 
ATOM   733  O  O   . PRO   A 1 93  ? 28.649 19.822  -19.120 1.00 28.44 ? 615  PRO   A O   1 
ATOM   734  C  CB  . PRO   A 1 93  ? 27.701 22.532  -20.073 1.00 27.81 ? 615  PRO   A CB  1 
ATOM   735  C  CG  . PRO   A 1 93  ? 27.081 23.275  -18.942 1.00 34.71 ? 615  PRO   A CG  1 
ATOM   736  C  CD  . PRO   A 1 93  ? 26.323 22.319  -18.088 1.00 30.43 ? 615  PRO   A CD  1 
ATOM   737  N  N   . ALA   A 1 94  ? 28.030 19.278  -21.210 1.00 23.51 ? 616  ALA   A N   1 
ATOM   738  C  CA  . ALA   A 1 94  ? 28.919 18.129  -21.289 1.00 23.01 ? 616  ALA   A CA  1 
ATOM   739  C  C   . ALA   A 1 94  ? 29.249 17.914  -22.748 1.00 24.56 ? 616  ALA   A C   1 
ATOM   740  O  O   . ALA   A 1 94  ? 28.480 18.306  -23.636 1.00 26.98 ? 616  ALA   A O   1 
ATOM   741  C  CB  . ALA   A 1 94  ? 28.281 16.870  -20.689 1.00 24.69 ? 616  ALA   A CB  1 
ATOM   742  N  N   . CYS   A 1 95  ? 30.395 17.297  -22.992 1.00 25.69 ? 617  CYS   A N   1 
ATOM   743  C  CA  . CYS   A 1 95  ? 30.747 16.962  -24.361 1.00 22.64 ? 617  CYS   A CA  1 
ATOM   744  C  C   . CYS   A 1 95  ? 31.645 15.738  -24.383 1.00 27.28 ? 617  CYS   A C   1 
ATOM   745  O  O   . CYS   A 1 95  ? 32.216 15.336  -23.368 1.00 29.34 ? 617  CYS   A O   1 
ATOM   746  C  CB  . CYS   A 1 95  ? 31.432 18.127  -25.072 1.00 36.19 ? 617  CYS   A CB  1 
ATOM   747  S  SG  . CYS   A 1 95  ? 33.052 18.469  -24.392 1.00 34.49 ? 617  CYS   A SG  1 
ATOM   748  N  N   . PHE   A 1 96  ? 31.746 15.148  -25.565 1.00 28.81 ? 618  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 96  ? 32.634 14.029  -25.856 1.00 31.30 ? 618  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 96  ? 33.778 14.592  -26.691 1.00 42.37 ? 618  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 96  ? 33.593 14.942  -27.859 1.00 42.10 ? 618  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 96  ? 31.868 12.925  -26.586 1.00 33.77 ? 618  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 96  ? 32.727 11.802  -27.088 1.00 35.03 ? 618  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 96  ? 33.517 11.068  -26.219 1.00 40.43 ? 618  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 96  ? 32.726 11.461  -28.428 1.00 50.35 ? 618  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 96  ? 34.303 10.025  -26.681 1.00 38.20 ? 618  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 96  ? 33.513 10.419  -28.900 1.00 52.23 ? 618  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 96  ? 34.301 9.701   -28.022 1.00 48.28 ? 618  PHE   A CZ  1 
ATOM   759  N  N   . LEU   A 1 97  ? 34.945 14.725  -26.078 1.00 41.96 ? 619  LEU   A N   1 
ATOM   760  C  CA  . LEU   A 1 97  ? 36.090 15.362  -26.713 1.00 41.92 ? 619  LEU   A CA  1 
ATOM   761  C  C   . LEU   A 1 97  ? 36.932 14.312  -27.425 1.00 42.25 ? 619  LEU   A C   1 
ATOM   762  O  O   . LEU   A 1 97  ? 37.369 13.336  -26.808 1.00 43.57 ? 619  LEU   A O   1 
ATOM   763  C  CB  . LEU   A 1 97  ? 36.925 16.105  -25.671 1.00 29.32 ? 619  LEU   A CB  1 
ATOM   764  C  CG  . LEU   A 1 97  ? 38.264 16.616  -26.177 1.00 36.80 ? 619  LEU   A CG  1 
ATOM   765  C  CD1 . LEU   A 1 97  ? 38.063 17.563  -27.352 1.00 46.42 ? 619  LEU   A CD1 1 
ATOM   766  C  CD2 . LEU   A 1 97  ? 38.984 17.308  -25.044 1.00 45.90 ? 619  LEU   A CD2 1 
ATOM   767  N  N   . GLY   A 1 98  ? 37.154 14.514  -28.724 1.00 49.79 ? 620  GLY   A N   1 
ATOM   768  C  CA  . GLY   A 1 98  ? 38.072 13.699  -29.495 1.00 49.26 ? 620  GLY   A CA  1 
ATOM   769  C  C   . GLY   A 1 98  ? 38.811 14.562  -30.503 1.00 56.91 ? 620  GLY   A C   1 
ATOM   770  O  O   . GLY   A 1 98  ? 38.649 15.784  -30.529 1.00 57.06 ? 620  GLY   A O   1 
ATOM   771  N  N   . SER   A 1 99  ? 39.621 13.903  -31.340 1.00 49.09 ? 621  SER   A N   1 
ATOM   772  C  CA  . SER   A 1 99  ? 40.411 14.632  -32.332 1.00 62.06 ? 621  SER   A CA  1 
ATOM   773  C  C   . SER   A 1 99  ? 39.522 15.451  -33.263 1.00 70.69 ? 621  SER   A C   1 
ATOM   774  O  O   . SER   A 1 99  ? 39.856 16.591  -33.610 1.00 65.43 ? 621  SER   A O   1 
ATOM   775  C  CB  . SER   A 1 99  ? 41.266 13.663  -33.147 1.00 67.20 ? 621  SER   A CB  1 
ATOM   776  O  OG  . SER   A 1 99  ? 40.476 12.997  -34.122 1.00 76.56 ? 621  SER   A OG  1 
ATOM   777  N  N   . ALA   A 1 100 ? 38.382 14.887  -33.671 1.00 65.17 ? 622  ALA   A N   1 
ATOM   778  C  CA  . ALA   A 1 100 ? 37.484 15.534  -34.619 1.00 71.06 ? 622  ALA   A CA  1 
ATOM   779  C  C   . ALA   A 1 100 ? 36.717 16.707  -34.026 1.00 76.32 ? 622  ALA   A C   1 
ATOM   780  O  O   . ALA   A 1 100 ? 35.897 17.299  -34.738 1.00 79.84 ? 622  ALA   A O   1 
ATOM   781  C  CB  . ALA   A 1 100 ? 36.493 14.512  -35.180 1.00 69.60 ? 622  ALA   A CB  1 
ATOM   782  N  N   . GLN   A 1 101 ? 36.940 17.065  -32.764 1.00 75.07 ? 623  GLN   A N   1 
ATOM   783  C  CA  . GLN   A 1 101 ? 36.207 18.174  -32.169 1.00 74.73 ? 623  GLN   A CA  1 
ATOM   784  C  C   . GLN   A 1 101 ? 36.830 19.513  -32.553 1.00 71.61 ? 623  GLN   A C   1 
ATOM   785  O  O   . GLN   A 1 101 ? 38.053 19.638  -32.681 1.00 64.29 ? 623  GLN   A O   1 
ATOM   786  C  CB  . GLN   A 1 101 ? 36.143 18.025  -30.647 1.00 57.85 ? 623  GLN   A CB  1 
ATOM   787  C  CG  . GLN   A 1 101 ? 35.030 17.095  -30.166 1.00 60.08 ? 623  GLN   A CG  1 
ATOM   788  C  CD  . GLN   A 1 101 ? 33.628 17.703  -30.268 1.00 68.59 ? 623  GLN   A CD  1 
ATOM   789  O  OE1 . GLN   A 1 101 ? 33.416 18.714  -30.942 1.00 72.46 ? 623  GLN   A OE1 1 
ATOM   790  N  NE2 . GLN   A 1 101 ? 32.663 17.081  -29.585 1.00 60.12 ? 623  GLN   A NE2 1 
ATOM   791  N  N   . SER   A 1 102 ? 35.966 20.515  -32.728 1.00 71.51 ? 624  SER   A N   1 
ATOM   792  C  CA  . SER   A 1 102 ? 36.369 21.816  -33.244 1.00 70.98 ? 624  SER   A CA  1 
ATOM   793  C  C   . SER   A 1 102 ? 37.147 22.623  -32.212 1.00 71.46 ? 624  SER   A C   1 
ATOM   794  O  O   . SER   A 1 102 ? 36.939 22.498  -30.998 1.00 67.37 ? 624  SER   A O   1 
ATOM   795  C  CB  . SER   A 1 102 ? 35.140 22.606  -33.678 1.00 70.47 ? 624  SER   A CB  1 
ATOM   796  O  OG  . SER   A 1 102 ? 34.191 22.652  -32.626 1.00 67.73 ? 624  SER   A OG  1 
ATOM   797  N  N   . GLU   A 1 103 ? 38.037 23.484  -32.718 1.00 66.67 ? 625  GLU   A N   1 
ATOM   798  C  CA  . GLU   A 1 103 ? 38.825 24.346  -31.844 1.00 65.26 ? 625  GLU   A CA  1 
ATOM   799  C  C   . GLU   A 1 103 ? 37.935 25.235  -30.984 1.00 65.86 ? 625  GLU   A C   1 
ATOM   800  O  O   . GLU   A 1 103 ? 38.347 25.659  -29.900 1.00 65.80 ? 625  GLU   A O   1 
ATOM   801  C  CB  . GLU   A 1 103 ? 39.784 25.197  -32.682 1.00 70.19 ? 625  GLU   A CB  1 
ATOM   802  C  CG  . GLU   A 1 103 ? 40.766 26.030  -31.876 1.00 74.74 ? 625  GLU   A CG  1 
ATOM   803  C  CD  . GLU   A 1 103 ? 41.082 27.366  -32.538 1.00 84.50 ? 625  GLU   A CD  1 
ATOM   804  O  OE1 . GLU   A 1 103 ? 40.751 27.539  -33.731 1.00 82.71 ? 625  GLU   A OE1 1 
ATOM   805  O  OE2 . GLU   A 1 103 ? 41.658 28.247  -31.861 1.00 85.77 ? 625  GLU   A OE2 1 
ATOM   806  N  N   . ASN   A 1 104 ? 36.708 25.510  -31.432 1.00 64.34 ? 626  ASN   A N   1 
ATOM   807  C  CA  . ASN   A 1 104 ? 35.780 26.276  -30.602 1.00 68.96 ? 626  ASN   A CA  1 
ATOM   808  C  C   . ASN   A 1 104 ? 35.324 25.469  -29.389 1.00 65.52 ? 626  ASN   A C   1 
ATOM   809  O  O   . ASN   A 1 104 ? 35.219 26.009  -28.279 1.00 55.69 ? 626  ASN   A O   1 
ATOM   810  C  CB  . ASN   A 1 104 ? 34.583 26.734  -31.435 1.00 68.55 ? 626  ASN   A CB  1 
ATOM   811  C  CG  . ASN   A 1 104 ? 34.948 27.830  -32.428 1.00 83.55 ? 626  ASN   A CG  1 
ATOM   812  O  OD1 . ASN   A 1 104 ? 35.815 28.670  -32.160 1.00 82.55 ? 626  ASN   A OD1 1 
ATOM   813  N  ND2 . ASN   A 1 104 ? 34.284 27.828  -33.579 1.00 81.01 ? 626  ASN   A ND2 1 
ATOM   814  N  N   . VAL   A 1 105 ? 35.075 24.168  -29.574 1.00 61.50 ? 627  VAL   A N   1 
ATOM   815  C  CA  . VAL   A 1 105 ? 34.757 23.309  -28.435 1.00 56.55 ? 627  VAL   A CA  1 
ATOM   816  C  C   . VAL   A 1 105 ? 35.960 23.190  -27.507 1.00 44.96 ? 627  VAL   A C   1 
ATOM   817  O  O   . VAL   A 1 105 ? 35.815 23.218  -26.281 1.00 43.34 ? 627  VAL   A O   1 
ATOM   818  C  CB  . VAL   A 1 105 ? 34.270 21.929  -28.915 1.00 61.57 ? 627  VAL   A CB  1 
ATOM   819  C  CG1 . VAL   A 1 105 ? 34.076 20.981  -27.729 1.00 47.12 ? 627  VAL   A CG1 1 
ATOM   820  C  CG2 . VAL   A 1 105 ? 32.971 22.074  -29.692 1.00 62.56 ? 627  VAL   A CG2 1 
ATOM   821  N  N   . LEU   A 1 106 ? 37.163 23.075  -28.074 1.00 36.91 ? 628  LEU   A N   1 
ATOM   822  C  CA  . LEU   A 1 106 ? 38.368 22.979  -27.255 1.00 38.89 ? 628  LEU   A CA  1 
ATOM   823  C  C   . LEU   A 1 106 ? 38.574 24.242  -26.427 1.00 47.24 ? 628  LEU   A C   1 
ATOM   824  O  O   . LEU   A 1 106 ? 38.909 24.176  -25.235 1.00 36.54 ? 628  LEU   A O   1 
ATOM   825  C  CB  . LEU   A 1 106 ? 39.574 22.714  -28.155 1.00 43.37 ? 628  LEU   A CB  1 
ATOM   826  C  CG  . LEU   A 1 106 ? 40.854 22.162  -27.536 1.00 47.64 ? 628  LEU   A CG  1 
ATOM   827  C  CD1 . LEU   A 1 106 ? 40.527 21.238  -26.377 1.00 47.85 ? 628  LEU   A CD1 1 
ATOM   828  C  CD2 . LEU   A 1 106 ? 41.644 21.410  -28.590 1.00 44.46 ? 628  LEU   A CD2 1 
ATOM   829  N  N   . THR   A 1 107 ? 38.366 25.407  -27.040 1.00 41.46 ? 629  THR   A N   1 
ATOM   830  C  CA  . THR   A 1 107 ? 38.474 26.653  -26.302 1.00 33.96 ? 629  THR   A CA  1 
ATOM   831  C  C   . THR   A 1 107 ? 37.413 26.742  -25.218 1.00 32.79 ? 629  THR   A C   1 
ATOM   832  O  O   . THR   A 1 107 ? 37.706 27.138  -24.081 1.00 30.35 ? 629  THR   A O   1 
ATOM   833  C  CB  . THR   A 1 107 ? 38.364 27.828  -27.269 1.00 47.93 ? 629  THR   A CB  1 
ATOM   834  O  OG1 . THR   A 1 107 ? 39.447 27.762  -28.207 1.00 46.00 ? 629  THR   A OG1 1 
ATOM   835  C  CG2 . THR   A 1 107 ? 38.416 29.128  -26.511 1.00 32.65 ? 629  THR   A CG2 1 
ATOM   836  N  N   . ASP   A 1 108 ? 36.180 26.345  -25.540 1.00 38.67 ? 630  ASP   A N   1 
ATOM   837  C  CA  . ASP   A 1 108 ? 35.120 26.315  -24.539 1.00 35.03 ? 630  ASP   A CA  1 
ATOM   838  C  C   . ASP   A 1 108 ? 35.474 25.416  -23.359 1.00 28.40 ? 630  ASP   A C   1 
ATOM   839  O  O   . ASP   A 1 108 ? 35.170 25.746  -22.207 1.00 31.52 ? 630  ASP   A O   1 
ATOM   840  C  CB  . ASP   A 1 108 ? 33.813 25.867  -25.187 1.00 39.96 ? 630  ASP   A CB  1 
ATOM   841  C  CG  . ASP   A 1 108 ? 33.006 27.037  -25.713 1.00 54.47 ? 630  ASP   A CG  1 
ATOM   842  O  OD1 . ASP   A 1 108 ? 33.462 28.188  -25.521 1.00 47.91 ? 630  ASP   A OD1 1 
ATOM   843  O  OD2 . ASP   A 1 108 ? 31.927 26.810  -26.300 1.00 57.95 ? 630  ASP   A OD2 1 
ATOM   844  N  N   . ILE   A 1 109 ? 36.086 24.263  -23.626 1.00 29.36 ? 631  ILE   A N   1 
ATOM   845  C  CA  . ILE   A 1 109 ? 36.518 23.402  -22.526 1.00 27.94 ? 631  ILE   A CA  1 
ATOM   846  C  C   . ILE   A 1 109 ? 37.607 24.089  -21.712 1.00 25.29 ? 631  ILE   A C   1 
ATOM   847  O  O   . ILE   A 1 109 ? 37.577 24.075  -20.474 1.00 26.37 ? 631  ILE   A O   1 
ATOM   848  C  CB  . ILE   A 1 109 ? 37.008 22.040  -23.041 1.00 31.47 ? 631  ILE   A CB  1 
ATOM   849  C  CG1 . ILE   A 1 109 ? 35.879 21.267  -23.720 1.00 26.63 ? 631  ILE   A CG1 1 
ATOM   850  C  CG2 . ILE   A 1 109 ? 37.576 21.246  -21.865 1.00 24.00 ? 631  ILE   A CG2 1 
ATOM   851  C  CD1 . ILE   A 1 109 ? 36.368 20.042  -24.415 1.00 26.33 ? 631  ILE   A CD1 1 
ATOM   852  N  N   . LYS   A 1 110 ? 38.587 24.699  -22.386 1.00 26.99 ? 632  LYS   A N   1 
ATOM   853  C  CA  . LYS   A 1 110 ? 39.622 25.427  -21.653 1.00 29.82 ? 632  LYS   A CA  1 
ATOM   854  C  C   . LYS   A 1 110 ? 39.037 26.598  -20.871 1.00 29.65 ? 632  LYS   A C   1 
ATOM   855  O  O   . LYS   A 1 110 ? 39.567 26.956  -19.817 1.00 29.22 ? 632  LYS   A O   1 
ATOM   856  C  CB  . LYS   A 1 110 ? 40.710 25.925  -22.599 1.00 29.75 ? 632  LYS   A CB  1 
ATOM   857  C  CG  . LYS   A 1 110 ? 41.493 24.820  -23.298 1.00 29.11 ? 632  LYS   A CG  1 
ATOM   858  C  CD  . LYS   A 1 110 ? 42.660 25.401  -24.089 1.00 33.27 ? 632  LYS   A CD  1 
ATOM   859  C  CE  . LYS   A 1 110 ? 43.330 24.339  -24.940 1.00 38.70 ? 632  LYS   A CE  1 
ATOM   860  N  NZ  . LYS   A 1 110 ? 44.282 24.944  -25.918 1.00 43.88 ? 632  LYS   A NZ  1 
ATOM   861  N  N   . LEU   A 1 111 ? 37.942 27.195  -21.350 1.00 28.52 ? 633  LEU   A N   1 
ATOM   862  C  CA  . LEU   A 1 111 ? 37.286 28.260  -20.596 1.00 31.18 ? 633  LEU   A CA  1 
ATOM   863  C  C   . LEU   A 1 111 ? 36.438 27.748  -19.442 1.00 34.01 ? 633  LEU   A C   1 
ATOM   864  O  O   . LEU   A 1 111 ? 35.902 28.565  -18.687 1.00 30.49 ? 633  LEU   A O   1 
ATOM   865  C  CB  . LEU   A 1 111 ? 36.413 29.109  -21.514 1.00 35.35 ? 633  LEU   A CB  1 
ATOM   866  C  CG  . LEU   A 1 111 ? 37.218 29.943  -22.505 1.00 37.83 ? 633  LEU   A CG  1 
ATOM   867  C  CD1 . LEU   A 1 111 ? 36.279 30.651  -23.479 1.00 40.83 ? 633  LEU   A CD1 1 
ATOM   868  C  CD2 . LEU   A 1 111 ? 38.086 30.921  -21.753 1.00 32.44 ? 633  LEU   A CD2 1 
ATOM   869  N  N   . GLY   A 1 112 ? 36.294 26.434  -19.284 1.00 29.45 ? 634  GLY   A N   1 
ATOM   870  C  CA  . GLY   A 1 112 ? 35.527 25.921  -18.168 1.00 25.95 ? 634  GLY   A CA  1 
ATOM   871  C  C   . GLY   A 1 112 ? 34.031 25.914  -18.387 1.00 30.19 ? 634  GLY   A C   1 
ATOM   872  O  O   . GLY   A 1 112 ? 33.268 25.864  -17.416 1.00 29.75 ? 634  GLY   A O   1 
ATOM   873  N  N   . LYS   A 1 113 ? 33.581 25.950  -19.633 1.00 24.56 ? 635  LYS   A N   1 
ATOM   874  C  CA  . LYS   A 1 113 ? 32.146 25.997  -19.869 1.00 29.72 ? 635  LYS   A CA  1 
ATOM   875  C  C   . LYS   A 1 113 ? 31.480 24.625  -19.813 1.00 38.05 ? 635  LYS   A C   1 
ATOM   876  O  O   . LYS   A 1 113 ? 30.250 24.563  -19.722 1.00 27.20 ? 635  LYS   A O   1 
ATOM   877  C  CB  . LYS   A 1 113 ? 31.871 26.663  -21.215 1.00 33.99 ? 635  LYS   A CB  1 
ATOM   878  C  CG  . LYS   A 1 113 ? 32.101 28.186  -21.179 1.00 41.20 ? 635  LYS   A CG  1 
ATOM   879  C  CD  . LYS   A 1 113 ? 31.980 28.791  -22.562 1.00 43.20 ? 635  LYS   A CD  1 
ATOM   880  C  CE  . LYS   A 1 113 ? 32.523 30.211  -22.600 1.00 48.59 ? 635  LYS   A CE  1 
ATOM   881  N  NZ  . LYS   A 1 113 ? 32.713 30.663  -24.006 1.00 49.32 ? 635  LYS   A NZ  1 
ATOM   882  N  N   . TYR   A 1 114 ? 32.253 23.539  -19.836 1.00 26.84 ? 636  TYR   A N   1 
ATOM   883  C  CA  . TYR   A 1 114 ? 31.730 22.177  -19.811 1.00 26.93 ? 636  TYR   A CA  1 
ATOM   884  C  C   . TYR   A 1 114 ? 31.983 21.561  -18.443 1.00 26.45 ? 636  TYR   A C   1 
ATOM   885  O  O   . TYR   A 1 114 ? 33.105 21.614  -17.938 1.00 24.55 ? 636  TYR   A O   1 
ATOM   886  C  CB  . TYR   A 1 114 ? 32.393 21.317  -20.888 1.00 28.32 ? 636  TYR   A CB  1 
ATOM   887  C  CG  . TYR   A 1 114 ? 31.939 21.626  -22.296 1.00 29.95 ? 636  TYR   A CG  1 
ATOM   888  C  CD1 . TYR   A 1 114 ? 30.735 21.135  -22.779 1.00 30.02 ? 636  TYR   A CD1 1 
ATOM   889  C  CD2 . TYR   A 1 114 ? 32.711 22.408  -23.142 1.00 32.02 ? 636  TYR   A CD2 1 
ATOM   890  C  CE1 . TYR   A 1 114 ? 30.315 21.407  -24.062 1.00 34.53 ? 636  TYR   A CE1 1 
ATOM   891  C  CE2 . TYR   A 1 114 ? 32.301 22.683  -24.429 1.00 40.10 ? 636  TYR   A CE2 1 
ATOM   892  C  CZ  . TYR   A 1 114 ? 31.093 22.179  -24.881 1.00 42.85 ? 636  TYR   A CZ  1 
ATOM   893  O  OH  . TYR   A 1 114 ? 30.664 22.437  -26.159 1.00 42.92 ? 636  TYR   A OH  1 
ATOM   894  N  N   . ARG   A 1 115 ? 30.945 20.986  -17.843 1.00 22.35 ? 637  ARG   A N   1 
ATOM   895  C  CA  . ARG   A 1 115 ? 31.129 20.375  -16.534 1.00 23.32 ? 637  ARG   A CA  1 
ATOM   896  C  C   . ARG   A 1 115 ? 31.763 19.006  -16.657 1.00 24.83 ? 637  ARG   A C   1 
ATOM   897  O  O   . ARG   A 1 115 ? 32.510 18.592  -15.773 1.00 24.92 ? 637  ARG   A O   1 
ATOM   898  C  CB  . ARG   A 1 115 ? 29.799 20.220  -15.797 1.00 24.30 ? 637  ARG   A CB  1 
ATOM   899  C  CG  . ARG   A 1 115 ? 29.175 21.522  -15.343 1.00 27.89 ? 637  ARG   A CG  1 
ATOM   900  C  CD  . ARG   A 1 115 ? 29.970 22.147  -14.202 1.00 28.43 ? 637  ARG   A CD  1 
ATOM   901  N  NE  . ARG   A 1 115 ? 29.801 23.589  -14.246 1.00 35.19 ? 637  ARG   A NE  1 
ATOM   902  C  CZ  . ARG   A 1 115 ? 30.549 24.382  -14.994 1.00 40.07 ? 637  ARG   A CZ  1 
ATOM   903  N  NH1 . ARG   A 1 115 ? 31.559 23.909  -15.692 1.00 29.06 ? 637  ARG   A NH1 1 
ATOM   904  N  NH2 . ARG   A 1 115 ? 30.278 25.683  -15.037 1.00 44.69 ? 637  ARG   A NH2 1 
ATOM   905  N  N   . ILE   A 1 116 ? 31.410 18.267  -17.701 1.00 22.37 ? 638  ILE   A N   1 
ATOM   906  C  CA  . ILE   A 1 116 ? 31.807 16.874  -17.840 1.00 23.36 ? 638  ILE   A CA  1 
ATOM   907  C  C   . ILE   A 1 116 ? 32.288 16.664  -19.260 1.00 21.90 ? 638  ILE   A C   1 
ATOM   908  O  O   . ILE   A 1 116 ? 31.570 16.967  -20.227 1.00 25.92 ? 638  ILE   A O   1 
ATOM   909  C  CB  . ILE   A 1 116 ? 30.671 15.903  -17.494 1.00 24.74 ? 638  ILE   A CB  1 
ATOM   910  C  CG1 . ILE   A 1 116 ? 30.279 16.069  -16.024 1.00 22.88 ? 638  ILE   A CG1 1 
ATOM   911  C  CG2 . ILE   A 1 116 ? 31.139 14.474  -17.740 1.00 23.91 ? 638  ILE   A CG2 1 
ATOM   912  C  CD1 . ILE   A 1 116 ? 29.053 15.361  -15.646 1.00 26.68 ? 638  ILE   A CD1 1 
ATOM   913  N  N   . VAL   A 1 117 ? 33.512 16.168  -19.377 1.00 17.88 ? 639  VAL   A N   1 
ATOM   914  C  CA  . VAL   A 1 117 ? 34.171 15.932  -20.643 1.00 17.23 ? 639  VAL   A CA  1 
ATOM   915  C  C   . VAL   A 1 117 ? 34.501 14.447  -20.701 1.00 23.99 ? 639  VAL   A C   1 
ATOM   916  O  O   . VAL   A 1 117 ? 35.266 13.948  -19.868 1.00 22.68 ? 639  VAL   A O   1 
ATOM   917  C  CB  . VAL   A 1 117 ? 35.450 16.774  -20.775 1.00 22.59 ? 639  VAL   A CB  1 
ATOM   918  C  CG1 . VAL   A 1 117 ? 36.070 16.530  -22.113 1.00 22.49 ? 639  VAL   A CG1 1 
ATOM   919  C  CG2 . VAL   A 1 117 ? 35.112 18.261  -20.593 1.00 21.58 ? 639  VAL   A CG2 1 
ATOM   920  N  N   . TYR   A 1 118 ? 33.915 13.753  -21.666 1.00 22.91 ? 640  TYR   A N   1 
ATOM   921  C  CA  . TYR   A 1 118 ? 34.175 12.349  -21.945 1.00 21.62 ? 640  TYR   A CA  1 
ATOM   922  C  C   . TYR   A 1 118 ? 35.256 12.219  -22.999 1.00 25.03 ? 640  TYR   A C   1 
ATOM   923  O  O   . TYR   A 1 118 ? 35.224 12.929  -24.006 1.00 27.72 ? 640  TYR   A O   1 
ATOM   924  C  CB  . TYR   A 1 118 ? 32.904 11.678  -22.462 1.00 27.42 ? 640  TYR   A CB  1 
ATOM   925  C  CG  . TYR   A 1 118 ? 31.826 11.505  -21.441 1.00 27.71 ? 640  TYR   A CG  1 
ATOM   926  C  CD1 . TYR   A 1 118 ? 30.950 12.535  -21.139 1.00 23.95 ? 640  TYR   A CD1 1 
ATOM   927  C  CD2 . TYR   A 1 118 ? 31.694 10.308  -20.771 1.00 24.34 ? 640  TYR   A CD2 1 
ATOM   928  C  CE1 . TYR   A 1 118 ? 29.947 12.352  -20.203 1.00 34.39 ? 640  TYR   A CE1 1 
ATOM   929  C  CE2 . TYR   A 1 118 ? 30.710 10.116  -19.837 1.00 27.15 ? 640  TYR   A CE2 1 
ATOM   930  C  CZ  . TYR   A 1 118 ? 29.844 11.125  -19.554 1.00 32.00 ? 640  TYR   A CZ  1 
ATOM   931  O  OH  . TYR   A 1 118 ? 28.877 10.888  -18.617 1.00 31.27 ? 640  TYR   A OH  1 
ATOM   932  N  N   . VAL   A 1 119 ? 36.205 11.295  -22.779 1.00 22.70 ? 641  VAL   A N   1 
ATOM   933  C  CA  . VAL   A 1 119 ? 37.277 11.018  -23.729 1.00 23.49 ? 641  VAL   A CA  1 
ATOM   934  C  C   . VAL   A 1 119 ? 37.569 9.521   -23.751 1.00 30.03 ? 641  VAL   A C   1 
ATOM   935  O  O   . VAL   A 1 119 ? 37.272 8.791   -22.806 1.00 26.21 ? 641  VAL   A O   1 
ATOM   936  C  CB  . VAL   A 1 119 ? 38.597 11.768  -23.412 1.00 26.90 ? 641  VAL   A CB  1 
ATOM   937  C  CG1 . VAL   A 1 119 ? 38.400 13.275  -23.464 1.00 24.29 ? 641  VAL   A CG1 1 
ATOM   938  C  CG2 . VAL   A 1 119 ? 39.155 11.334  -22.051 1.00 22.67 ? 641  VAL   A CG2 1 
ATOM   939  N  N   . THR   A 1 120 ? 38.185 9.077   -24.833 1.00 23.01 ? 642  THR   A N   1 
ATOM   940  C  CA  . THR   A 1 120 ? 38.691 7.719   -24.883 1.00 28.11 ? 642  THR   A CA  1 
ATOM   941  C  C   . THR   A 1 120 ? 40.041 7.647   -24.191 1.00 29.04 ? 642  THR   A C   1 
ATOM   942  O  O   . THR   A 1 120 ? 40.739 8.653   -24.065 1.00 28.28 ? 642  THR   A O   1 
ATOM   943  C  CB  . THR   A 1 120 ? 38.836 7.254   -26.328 1.00 34.01 ? 642  THR   A CB  1 
ATOM   944  O  OG1 . THR   A 1 120 ? 39.843 8.041   -26.973 1.00 28.17 ? 642  THR   A OG1 1 
ATOM   945  C  CG2 . THR   A 1 120 ? 37.542 7.405   -27.068 1.00 29.19 ? 642  THR   A CG2 1 
ATOM   946  N  N   . PRO   A 1 121 ? 40.444 6.464   -23.736 1.00 29.39 ? 643  PRO   A N   1 
ATOM   947  C  CA  . PRO   A 1 121 ? 41.791 6.343   -23.164 1.00 27.58 ? 643  PRO   A CA  1 
ATOM   948  C  C   . PRO   A 1 121 ? 42.896 6.744   -24.139 1.00 29.95 ? 643  PRO   A C   1 
ATOM   949  O  O   . PRO   A 1 121 ? 43.926 7.290   -23.716 1.00 25.72 ? 643  PRO   A O   1 
ATOM   950  C  CB  . PRO   A 1 121 ? 41.872 4.859   -22.781 1.00 32.91 ? 643  PRO   A CB  1 
ATOM   951  C  CG  . PRO   A 1 121 ? 40.839 4.190   -23.611 1.00 35.47 ? 643  PRO   A CG  1 
ATOM   952  C  CD  . PRO   A 1 121 ? 39.727 5.175   -23.746 1.00 26.34 ? 643  PRO   A CD  1 
ATOM   953  N  N   . GLU   A 1 122 ? 42.696 6.525   -25.438 1.00 32.38 ? 644  GLU   A N   1 
ATOM   954  C  CA  . GLU   A 1 122 ? 43.735 6.869   -26.405 1.00 33.18 ? 644  GLU   A CA  1 
ATOM   955  C  C   . GLU   A 1 122 ? 43.889 8.380   -26.516 1.00 32.45 ? 644  GLU   A C   1 
ATOM   956  O  O   . GLU   A 1 122 ? 45.010 8.908   -26.510 1.00 31.99 ? 644  GLU   A O   1 
ATOM   957  C  CB  . GLU   A 1 122 ? 43.403 6.254   -27.763 1.00 37.40 ? 644  GLU   A CB  1 
ATOM   958  C  CG  . GLU   A 1 122 ? 43.445 4.723   -27.785 1.00 47.63 ? 644  GLU   A CG  1 
ATOM   959  C  CD  . GLU   A 1 122 ? 42.076 4.042   -27.611 1.00 44.93 ? 644  GLU   A CD  1 
ATOM   960  O  OE1 . GLU   A 1 122 ? 41.119 4.665   -27.085 1.00 38.54 ? 644  GLU   A OE1 1 
ATOM   961  O  OE2 . GLU   A 1 122 ? 41.963 2.857   -28.009 1.00 46.15 ? 644  GLU   A OE2 1 
ATOM   962  N  N   . TYR   A 1 123 ? 42.763 9.094   -26.610 1.00 32.82 ? 645  TYR   A N   1 
ATOM   963  C  CA  . TYR   A 1 123 ? 42.822 10.551  -26.641 1.00 31.38 ? 645  TYR   A CA  1 
ATOM   964  C  C   . TYR   A 1 123 ? 43.468 11.087  -25.372 1.00 31.91 ? 645  TYR   A C   1 
ATOM   965  O  O   . TYR   A 1 123 ? 44.342 11.966  -25.414 1.00 32.47 ? 645  TYR   A O   1 
ATOM   966  C  CB  . TYR   A 1 123 ? 41.422 11.129  -26.807 1.00 29.47 ? 645  TYR   A CB  1 
ATOM   967  C  CG  . TYR   A 1 123 ? 41.459 12.637  -26.957 1.00 37.09 ? 645  TYR   A CG  1 
ATOM   968  C  CD1 . TYR   A 1 123 ? 41.510 13.463  -25.845 1.00 35.87 ? 645  TYR   A CD1 1 
ATOM   969  C  CD2 . TYR   A 1 123 ? 41.475 13.232  -28.211 1.00 40.13 ? 645  TYR   A CD2 1 
ATOM   970  C  CE1 . TYR   A 1 123 ? 41.567 14.844  -25.972 1.00 36.41 ? 645  TYR   A CE1 1 
ATOM   971  C  CE2 . TYR   A 1 123 ? 41.526 14.618  -28.349 1.00 43.89 ? 645  TYR   A CE2 1 
ATOM   972  C  CZ  . TYR   A 1 123 ? 41.575 15.416  -27.221 1.00 38.19 ? 645  TYR   A CZ  1 
ATOM   973  O  OH  . TYR   A 1 123 ? 41.627 16.792  -27.330 1.00 38.12 ? 645  TYR   A OH  1 
ATOM   974  N  N   . CYS   A 1 124 ? 43.036 10.562  -24.230 1.00 31.16 ? 646  CYS   A N   1 
ATOM   975  C  CA  . CYS   A 1 124 ? 43.574 10.999  -22.954 1.00 27.48 ? 646  CYS   A CA  1 
ATOM   976  C  C   . CYS   A 1 124 ? 45.090 10.837  -22.915 1.00 34.47 ? 646  CYS   A C   1 
ATOM   977  O  O   . CYS   A 1 124 ? 45.820 11.781  -22.589 1.00 36.17 ? 646  CYS   A O   1 
ATOM   978  C  CB  . CYS   A 1 124 ? 42.876 10.225  -21.839 1.00 26.71 ? 646  CYS   A CB  1 
ATOM   979  S  SG  . CYS   A 1 124 ? 43.451 10.606  -20.205 1.00 38.05 ? 646  CYS   A SG  1 
ATOM   980  N  N   . SER   A 1 125 ? 45.589 9.668   -23.311 1.00 32.78 ? 647  SER   A N   1 
ATOM   981  C  CA  . SER   A 1 125 ? 47.034 9.462   -23.338 1.00 30.78 ? 647  SER   A CA  1 
ATOM   982  C  C   . SER   A 1 125 ? 47.729 10.396  -24.315 1.00 35.99 ? 647  SER   A C   1 
ATOM   983  O  O   . SER   A 1 125 ? 48.900 10.743  -24.116 1.00 32.40 ? 647  SER   A O   1 
ATOM   984  C  CB  . SER   A 1 125 ? 47.350 8.013   -23.702 1.00 36.31 ? 647  SER   A CB  1 
ATOM   985  O  OG  . SER   A 1 125 ? 46.871 7.153   -22.693 1.00 47.45 ? 647  SER   A OG  1 
ATOM   986  N  N   . GLY   A 1 126 ? 47.048 10.789  -25.390 1.00 32.66 ? 648  GLY   A N   1 
ATOM   987  C  CA  . GLY   A 1 126 ? 47.707 11.675  -26.327 1.00 32.65 ? 648  GLY   A CA  1 
ATOM   988  C  C   . GLY   A 1 126 ? 47.666 13.149  -25.957 1.00 34.59 ? 648  GLY   A C   1 
ATOM   989  O  O   . GLY   A 1 126 ? 48.314 13.953  -26.632 1.00 36.73 ? 648  GLY   A O   1 
ATOM   990  N  N   . ASN   A 1 127 ? 46.897 13.521  -24.931 1.00 26.90 ? 649  ASN   A N   1 
ATOM   991  C  CA  . ASN   A 1 127 ? 46.659 14.940  -24.621 1.00 34.81 ? 649  ASN   A CA  1 
ATOM   992  C  C   . ASN   A 1 127 ? 46.804 15.246  -23.120 1.00 28.17 ? 649  ASN   A C   1 
ATOM   993  O  O   . ASN   A 1 127 ? 46.017 15.999  -22.511 1.00 27.22 ? 649  ASN   A O   1 
ATOM   994  C  CB  . ASN   A 1 127 ? 45.289 15.337  -25.140 1.00 32.64 ? 649  ASN   A CB  1 
ATOM   995  C  CG  . ASN   A 1 127 ? 45.211 15.289  -26.647 1.00 37.80 ? 649  ASN   A CG  1 
ATOM   996  O  OD1 . ASN   A 1 127 ? 45.560 16.250  -27.323 1.00 37.82 ? 649  ASN   A OD1 1 
ATOM   997  N  ND2 . ASN   A 1 127 ? 44.750 14.163  -27.185 1.00 37.08 ? 649  ASN   A ND2 1 
ATOM   998  N  N   . MET   A 1 128 ? 47.867 14.707  -22.513 1.00 23.51 ? 650  MET   A N   1 
ATOM   999  C  CA  . MET   A 1 128 ? 48.072 14.944  -21.090 1.00 26.87 ? 650  MET   A CA  1 
ATOM   1000 C  C   . MET   A 1 128 ? 48.305 16.427  -20.810 1.00 23.63 ? 650  MET   A C   1 
ATOM   1001 O  O   . MET   A 1 128 ? 47.889 16.934  -19.766 1.00 23.38 ? 650  MET   A O   1 
ATOM   1002 C  CB  . MET   A 1 128 ? 49.247 14.112  -20.563 1.00 28.14 ? 650  MET   A CB  1 
ATOM   1003 C  CG  . MET   A 1 128 ? 48.988 12.593  -20.430 1.00 44.07 ? 650  MET   A CG  1 
ATOM   1004 S  SD  . MET   A 1 128 ? 47.688 12.177  -19.250 1.00 41.04 ? 650  MET   A SD  1 
ATOM   1005 C  CE  . MET   A 1 128 ? 48.071 13.370  -17.981 1.00 35.63 ? 650  MET   A CE  1 
ATOM   1006 N  N   . GLY   A 1 129 ? 49.006 17.124  -21.710 1.00 23.91 ? 651  GLY   A N   1 
ATOM   1007 C  CA  . GLY   A 1 129 ? 49.277 18.539  -21.475 1.00 25.19 ? 651  GLY   A CA  1 
ATOM   1008 C  C   . GLY   A 1 129 ? 48.001 19.361  -21.417 1.00 26.16 ? 651  GLY   A C   1 
ATOM   1009 O  O   . GLY   A 1 129 ? 47.880 20.294  -20.611 1.00 26.17 ? 651  GLY   A O   1 
ATOM   1010 N  N   . LEU   A 1 130 ? 47.030 19.027  -22.272 1.00 25.12 ? 652  LEU   A N   1 
ATOM   1011 C  CA  . LEU   A 1 130 ? 45.721 19.672  -22.200 1.00 22.74 ? 652  LEU   A CA  1 
ATOM   1012 C  C   . LEU   A 1 130 ? 45.081 19.427  -20.848 1.00 21.70 ? 652  LEU   A C   1 
ATOM   1013 O  O   . LEU   A 1 130 ? 44.550 20.355  -20.221 1.00 21.95 ? 652  LEU   A O   1 
ATOM   1014 C  CB  . LEU   A 1 130 ? 44.808 19.170  -23.320 1.00 22.76 ? 652  LEU   A CB  1 
ATOM   1015 C  CG  . LEU   A 1 130 ? 43.319 19.487  -23.085 1.00 26.90 ? 652  LEU   A CG  1 
ATOM   1016 C  CD1 . LEU   A 1 130 ? 43.022 20.969  -23.293 1.00 25.18 ? 652  LEU   A CD1 1 
ATOM   1017 C  CD2 . LEU   A 1 130 ? 42.380 18.625  -23.942 1.00 34.38 ? 652  LEU   A CD2 1 
ATOM   1018 N  N   . LEU   A 1 131 ? 45.115 18.173  -20.377 1.00 21.38 ? 653  LEU   A N   1 
ATOM   1019 C  CA  . LEU   A 1 131 ? 44.513 17.905  -19.070 1.00 19.95 ? 653  LEU   A CA  1 
ATOM   1020 C  C   . LEU   A 1 131 ? 45.184 18.726  -17.970 1.00 17.93 ? 653  LEU   A C   1 
ATOM   1021 O  O   . LEU   A 1 131 ? 44.517 19.215  -17.052 1.00 19.20 ? 653  LEU   A O   1 
ATOM   1022 C  CB  . LEU   A 1 131 ? 44.610 16.423  -18.718 1.00 21.43 ? 653  LEU   A CB  1 
ATOM   1023 C  CG  . LEU   A 1 131 ? 43.955 15.450  -19.701 1.00 25.88 ? 653  LEU   A CG  1 
ATOM   1024 C  CD1 . LEU   A 1 131 ? 43.845 14.070  -19.060 1.00 27.90 ? 653  LEU   A CD1 1 
ATOM   1025 C  CD2 . LEU   A 1 131 ? 42.612 15.959  -20.148 1.00 26.96 ? 653  LEU   A CD2 1 
ATOM   1026 N  N   . GLN   A 1 132 ? 46.508 18.822  -18.014 1.00 18.30 ? 654  GLN   A N   1 
ATOM   1027 C  CA  . GLN   A 1 132 ? 47.223 19.610  -17.013 1.00 17.50 ? 654  GLN   A CA  1 
ATOM   1028 C  C   . GLN   A 1 132 ? 46.823 21.082  -17.091 1.00 15.01 ? 654  GLN   A C   1 
ATOM   1029 O  O   . GLN   A 1 132 ? 46.699 21.753  -16.063 1.00 18.63 ? 654  GLN   A O   1 
ATOM   1030 C  CB  . GLN   A 1 132 ? 48.736 19.454  -17.199 1.00 17.99 ? 654  GLN   A CB  1 
ATOM   1031 C  CG  . GLN   A 1 132 ? 49.228 18.063  -16.853 1.00 17.32 ? 654  GLN   A CG  1 
ATOM   1032 C  CD  . GLN   A 1 132 ? 50.708 17.924  -17.089 1.00 19.51 ? 654  GLN   A CD  1 
ATOM   1033 O  OE1 . GLN   A 1 132 ? 51.204 18.237  -18.167 1.00 22.60 ? 654  GLN   A OE1 1 
ATOM   1034 N  NE2 . GLN   A 1 132 ? 51.428 17.469  -16.076 1.00 20.93 ? 654  GLN   A NE2 1 
ATOM   1035 N  N   . GLN   A 1 133 ? 46.640 21.606  -18.296 1.00 16.91 ? 655  GLN   A N   1 
ATOM   1036 C  CA  . GLN   A 1 133 ? 46.183 22.989  -18.392 1.00 15.82 ? 655  GLN   A CA  1 
ATOM   1037 C  C   . GLN   A 1 133 ? 44.786 23.150  -17.782 1.00 20.00 ? 655  GLN   A C   1 
ATOM   1038 O  O   . GLN   A 1 133 ? 44.516 24.127  -17.076 1.00 20.71 ? 655  GLN   A O   1 
ATOM   1039 C  CB  . GLN   A 1 133 ? 46.189 23.472  -19.840 1.00 17.82 ? 655  GLN   A CB  1 
ATOM   1040 C  CG  . GLN   A 1 133 ? 45.633 24.901  -19.912 1.00 20.90 ? 655  GLN   A CG  1 
ATOM   1041 C  CD  . GLN   A 1 133 ? 45.811 25.603  -21.244 1.00 25.45 ? 655  GLN   A CD  1 
ATOM   1042 O  OE1 . GLN   A 1 133 ? 46.409 25.072  -22.176 1.00 26.05 ? 655  GLN   A OE1 1 
ATOM   1043 N  NE2 . GLN   A 1 133 ? 45.300 26.840  -21.323 1.00 25.53 ? 655  GLN   A NE2 1 
ATOM   1044 N  N   . LEU   A 1 134 ? 43.885 22.197  -18.026 1.00 18.60 ? 656  LEU   A N   1 
ATOM   1045 C  CA  . LEU   A 1 134 ? 42.553 22.276  -17.416 1.00 19.72 ? 656  LEU   A CA  1 
ATOM   1046 C  C   . LEU   A 1 134 ? 42.650 22.264  -15.901 1.00 19.91 ? 656  LEU   A C   1 
ATOM   1047 O  O   . LEU   A 1 134 ? 41.928 22.993  -15.219 1.00 19.23 ? 656  LEU   A O   1 
ATOM   1048 C  CB  . LEU   A 1 134 ? 41.667 21.117  -17.882 1.00 17.75 ? 656  LEU   A CB  1 
ATOM   1049 C  CG  . LEU   A 1 134 ? 41.381 21.103  -19.380 1.00 19.05 ? 656  LEU   A CG  1 
ATOM   1050 C  CD1 . LEU   A 1 134 ? 40.441 19.931  -19.705 1.00 19.36 ? 656  LEU   A CD1 1 
ATOM   1051 C  CD2 . LEU   A 1 134 ? 40.769 22.453  -19.810 1.00 22.48 ? 656  LEU   A CD2 1 
ATOM   1052 N  N   . GLU   A 1 135 ? 43.548 21.439  -15.356 1.00 18.26 ? 657  GLU   A N   1 
ATOM   1053 C  CA  . GLU   A 1 135 ? 43.743 21.431  -13.907 1.00 19.10 ? 657  GLU   A CA  1 
ATOM   1054 C  C   . GLU   A 1 135 ? 44.288 22.773  -13.418 1.00 22.31 ? 657  GLU   A C   1 
ATOM   1055 O  O   . GLU   A 1 135 ? 43.854 23.286  -12.377 1.00 17.85 ? 657  GLU   A O   1 
ATOM   1056 C  CB  . GLU   A 1 135 ? 44.678 20.278  -13.504 1.00 18.23 ? 657  GLU   A CB  1 
ATOM   1057 C  CG  . GLU   A 1 135 ? 45.318 20.379  -12.101 1.00 23.21 ? 657  GLU   A CG  1 
ATOM   1058 C  CD  . GLU   A 1 135 ? 44.305 20.414  -10.956 1.00 25.39 ? 657  GLU   A CD  1 
ATOM   1059 O  OE1 . GLU   A 1 135 ? 43.134 20.055  -11.161 1.00 26.33 ? 657  GLU   A OE1 1 
ATOM   1060 O  OE2 . GLU   A 1 135 ? 44.666 20.832  -9.837  1.00 25.36 ? 657  GLU   A OE2 1 
ATOM   1061 N  N   . ALA   A 1 136 ? 45.248 23.347  -14.143 1.00 19.30 ? 658  ALA   A N   1 
ATOM   1062 C  CA  . ALA   A 1 136 ? 45.822 24.616  -13.690 1.00 18.33 ? 658  ALA   A CA  1 
ATOM   1063 C  C   . ALA   A 1 136 ? 44.816 25.772  -13.801 1.00 17.10 ? 658  ALA   A C   1 
ATOM   1064 O  O   . ALA   A 1 136 ? 44.752 26.638  -12.916 1.00 19.40 ? 658  ALA   A O   1 
ATOM   1065 C  CB  . ALA   A 1 136 ? 47.093 24.935  -14.491 1.00 16.56 ? 658  ALA   A CB  1 
ATOM   1066 N  N   . ASP   A 1 137 ? 44.035 25.821  -14.876 1.00 19.72 ? 659  ASP   A N   1 
ATOM   1067 C  CA  . ASP   A 1 137 ? 43.193 26.997  -15.135 1.00 20.17 ? 659  ASP   A CA  1 
ATOM   1068 C  C   . ASP   A 1 137 ? 41.851 26.929  -14.429 1.00 21.04 ? 659  ASP   A C   1 
ATOM   1069 O  O   . ASP   A 1 137 ? 41.328 27.952  -13.973 1.00 21.59 ? 659  ASP   A O   1 
ATOM   1070 C  CB  . ASP   A 1 137 ? 42.942 27.150  -16.637 1.00 17.24 ? 659  ASP   A CB  1 
ATOM   1071 C  CG  . ASP   A 1 137 ? 44.144 27.705  -17.378 1.00 22.40 ? 659  ASP   A CG  1 
ATOM   1072 O  OD1 . ASP   A 1 137 ? 45.111 28.089  -16.697 1.00 23.23 ? 659  ASP   A OD1 1 
ATOM   1073 O  OD2 . ASP   A 1 137 ? 44.112 27.767  -18.627 1.00 23.71 ? 659  ASP   A OD2 1 
ATOM   1074 N  N   . ILE   A 1 138 ? 41.262 25.739  -14.374 1.00 20.58 ? 660  ILE   A N   1 
ATOM   1075 C  CA  . ILE   A 1 138 ? 39.903 25.535  -13.885 1.00 16.05 ? 660  ILE   A CA  1 
ATOM   1076 C  C   . ILE   A 1 138 ? 39.901 24.674  -12.632 1.00 23.88 ? 660  ILE   A C   1 
ATOM   1077 O  O   . ILE   A 1 138 ? 39.303 25.035  -11.619 1.00 23.09 ? 660  ILE   A O   1 
ATOM   1078 C  CB  . ILE   A 1 138 ? 39.006 24.905  -14.971 1.00 25.03 ? 660  ILE   A CB  1 
ATOM   1079 C  CG1 . ILE   A 1 138 ? 39.039 25.728  -16.250 1.00 24.33 ? 660  ILE   A CG1 1 
ATOM   1080 C  CG2 . ILE   A 1 138 ? 37.559 24.727  -14.444 1.00 22.10 ? 660  ILE   A CG2 1 
ATOM   1081 C  CD1 . ILE   A 1 138 ? 38.728 27.205  -16.043 1.00 34.74 ? 660  ILE   A CD1 1 
ATOM   1082 N  N   . GLY   A 1 139 ? 40.599 23.536  -12.679 1.00 18.69 ? 661  GLY   A N   1 
ATOM   1083 C  CA  . GLY   A 1 139 ? 40.597 22.573  -11.586 1.00 19.47 ? 661  GLY   A CA  1 
ATOM   1084 C  C   . GLY   A 1 139 ? 39.767 21.354  -11.947 1.00 24.02 ? 661  GLY   A C   1 
ATOM   1085 O  O   . GLY   A 1 139 ? 38.577 21.509  -12.244 1.00 23.40 ? 661  GLY   A O   1 
ATOM   1086 N  N   . ILE   A 1 140 ? 40.365 20.161  -11.954 1.00 18.06 ? 662  ILE   A N   1 
ATOM   1087 C  CA  . ILE   A 1 140 ? 39.646 18.933  -12.304 1.00 20.17 ? 662  ILE   A CA  1 
ATOM   1088 C  C   . ILE   A 1 140 ? 39.155 18.291  -11.013 1.00 19.18 ? 662  ILE   A C   1 
ATOM   1089 O  O   . ILE   A 1 140 ? 39.960 17.849  -10.186 1.00 20.60 ? 662  ILE   A O   1 
ATOM   1090 C  CB  . ILE   A 1 140 ? 40.521 17.961  -13.104 1.00 20.08 ? 662  ILE   A CB  1 
ATOM   1091 C  CG1 . ILE   A 1 140 ? 41.058 18.625  -14.379 1.00 19.05 ? 662  ILE   A CG1 1 
ATOM   1092 C  CG2 . ILE   A 1 140 ? 39.741 16.637  -13.387 1.00 19.01 ? 662  ILE   A CG2 1 
ATOM   1093 C  CD1 . ILE   A 1 140 ? 41.919 17.760  -15.189 1.00 18.60 ? 662  ILE   A CD1 1 
ATOM   1094 N  N   . THR   A 1 141 ? 37.832 18.256  -10.836 1.00 15.50 ? 663  THR   A N   1 
ATOM   1095 C  CA  . THR   A 1 141 ? 37.251 17.692  -9.625  1.00 18.37 ? 663  THR   A CA  1 
ATOM   1096 C  C   . THR   A 1 141 ? 37.620 16.215  -9.471  1.00 17.61 ? 663  THR   A C   1 
ATOM   1097 O  O   . THR   A 1 141 ? 37.940 15.766  -8.369  1.00 17.97 ? 663  THR   A O   1 
ATOM   1098 C  CB  . THR   A 1 141 ? 35.738 17.869  -9.664  1.00 21.90 ? 663  THR   A CB  1 
ATOM   1099 O  OG1 . THR   A 1 141 ? 35.450 19.251  -9.849  1.00 19.52 ? 663  THR   A OG1 1 
ATOM   1100 C  CG2 . THR   A 1 141 ? 35.080 17.405  -8.362  1.00 21.32 ? 663  THR   A CG2 1 
ATOM   1101 N  N   . LEU   A 1 142 ? 37.581 15.459  -10.563 1.00 16.08 ? 664  LEU   A N   1 
ATOM   1102 C  CA  . LEU   A 1 142 ? 37.928 14.037  -10.521 1.00 14.89 ? 664  LEU   A CA  1 
ATOM   1103 C  C   . LEU   A 1 142 ? 38.155 13.578  -11.948 1.00 15.89 ? 664  LEU   A C   1 
ATOM   1104 O  O   . LEU   A 1 142 ? 37.645 14.181  -12.901 1.00 17.85 ? 664  LEU   A O   1 
ATOM   1105 C  CB  . LEU   A 1 142 ? 36.831 13.180  -9.852  1.00 17.12 ? 664  LEU   A CB  1 
ATOM   1106 C  CG  . LEU   A 1 142 ? 35.444 13.215  -10.540 1.00 21.04 ? 664  LEU   A CG  1 
ATOM   1107 C  CD1 . LEU   A 1 142 ? 35.346 12.213  -11.665 1.00 25.60 ? 664  LEU   A CD1 1 
ATOM   1108 C  CD2 . LEU   A 1 142 ? 34.309 12.980  -9.566  1.00 24.38 ? 664  LEU   A CD2 1 
ATOM   1109 N  N   . ILE   A 1 143 ? 38.895 12.486  -12.074 1.00 16.58 ? 665  ILE   A N   1 
ATOM   1110 C  CA  . ILE   A 1 143 ? 39.010 11.730  -13.317 1.00 15.16 ? 665  ILE   A CA  1 
ATOM   1111 C  C   . ILE   A 1 143 ? 38.379 10.373  -13.080 1.00 17.38 ? 665  ILE   A C   1 
ATOM   1112 O  O   . ILE   A 1 143 ? 38.803 9.641   -12.179 1.00 23.96 ? 665  ILE   A O   1 
ATOM   1113 C  CB  . ILE   A 1 143 ? 40.465 11.588  -13.751 1.00 17.53 ? 665  ILE   A CB  1 
ATOM   1114 C  CG1 . ILE   A 1 143 ? 41.061 12.991  -13.981 1.00 14.93 ? 665  ILE   A CG1 1 
ATOM   1115 C  CG2 . ILE   A 1 143 ? 40.556 10.704  -14.976 1.00 17.45 ? 665  ILE   A CG2 1 
ATOM   1116 C  CD1 . ILE   A 1 143 ? 42.590 12.944  -14.049 1.00 18.78 ? 665  ILE   A CD1 1 
ATOM   1117 N  N   . ALA   A 1 144 ? 37.380 10.032  -13.876 1.00 15.99 ? 666  ALA   A N   1 
ATOM   1118 C  CA  . ALA   A 1 144 ? 36.741 8.726   -13.764 1.00 16.95 ? 666  ALA   A CA  1 
ATOM   1119 C  C   . ALA   A 1 144 ? 37.339 7.807   -14.816 1.00 22.20 ? 666  ALA   A C   1 
ATOM   1120 O  O   . ALA   A 1 144 ? 37.503 8.212   -15.967 1.00 20.99 ? 666  ALA   A O   1 
ATOM   1121 C  CB  . ALA   A 1 144 ? 35.223 8.838   -13.956 1.00 17.32 ? 666  ALA   A CB  1 
ATOM   1122 N  N   . VAL   A 1 145 ? 37.680 6.575   -14.430 1.00 19.04 ? 667  VAL   A N   1 
ATOM   1123 C  CA  . VAL   A 1 145 ? 38.148 5.573   -15.384 1.00 21.27 ? 667  VAL   A CA  1 
ATOM   1124 C  C   . VAL   A 1 145 ? 37.103 4.471   -15.368 1.00 20.40 ? 667  VAL   A C   1 
ATOM   1125 O  O   . VAL   A 1 145 ? 37.015 3.723   -14.390 1.00 20.56 ? 667  VAL   A O   1 
ATOM   1126 C  CB  . VAL   A 1 145 ? 39.542 5.041   -15.036 1.00 21.05 ? 667  VAL   A CB  1 
ATOM   1127 C  CG1 . VAL   A 1 145 ? 39.965 3.910   -15.987 1.00 20.70 ? 667  VAL   A CG1 1 
ATOM   1128 C  CG2 . VAL   A 1 145 ? 40.560 6.206   -15.101 1.00 20.15 ? 667  VAL   A CG2 1 
ATOM   1129 N  N   . ASP   A 1 146 ? 36.264 4.418   -16.399 1.00 19.91 ? 668  ASP   A N   1 
ATOM   1130 C  CA  . ASP   A 1 146 ? 35.257 3.375   -16.475 1.00 20.11 ? 668  ASP   A CA  1 
ATOM   1131 C  C   . ASP   A 1 146 ? 35.891 2.127   -17.077 1.00 20.98 ? 668  ASP   A C   1 
ATOM   1132 O  O   . ASP   A 1 146 ? 36.970 2.188   -17.681 1.00 21.32 ? 668  ASP   A O   1 
ATOM   1133 C  CB  . ASP   A 1 146 ? 34.060 3.826   -17.314 1.00 27.32 ? 668  ASP   A CB  1 
ATOM   1134 C  CG  . ASP   A 1 146 ? 32.808 2.972   -17.077 1.00 34.92 ? 668  ASP   A CG  1 
ATOM   1135 O  OD1 . ASP   A 1 146 ? 32.744 2.264   -16.051 1.00 31.38 ? 668  ASP   A OD1 1 
ATOM   1136 O  OD2 . ASP   A 1 146 ? 31.884 2.992   -17.924 1.00 34.96 ? 668  ASP   A OD2 1 
ATOM   1137 N  N   . GLU   A 1 147 ? 35.217 0.987   -16.895 1.00 25.02 ? 669  GLU   A N   1 
ATOM   1138 C  CA  . GLU   A 1 147 ? 35.753 -0.310  -17.329 1.00 26.08 ? 669  GLU   A CA  1 
ATOM   1139 C  C   . GLU   A 1 147 ? 37.188 -0.502  -16.849 1.00 23.05 ? 669  GLU   A C   1 
ATOM   1140 O  O   . GLU   A 1 147 ? 38.058 -0.959  -17.598 1.00 26.50 ? 669  GLU   A O   1 
ATOM   1141 C  CB  . GLU   A 1 147 ? 35.681 -0.445  -18.847 1.00 25.50 ? 669  GLU   A CB  1 
ATOM   1142 C  CG  . GLU   A 1 147 ? 34.288 -0.336  -19.406 1.00 32.35 ? 669  GLU   A CG  1 
ATOM   1143 C  CD  . GLU   A 1 147 ? 33.417 -1.469  -18.956 1.00 34.93 ? 669  GLU   A CD  1 
ATOM   1144 O  OE1 . GLU   A 1 147 ? 33.543 -2.565  -19.529 1.00 40.19 ? 669  GLU   A OE1 1 
ATOM   1145 O  OE2 . GLU   A 1 147 ? 32.621 -1.263  -18.023 1.00 41.80 ? 669  GLU   A OE2 1 
ATOM   1146 N  N   . ALA   A 1 148 ? 37.450 -0.130  -15.591 1.00 23.66 ? 670  ALA   A N   1 
ATOM   1147 C  CA  . ALA   A 1 148 ? 38.834 0.009   -15.139 1.00 20.86 ? 670  ALA   A CA  1 
ATOM   1148 C  C   . ALA   A 1 148 ? 39.560 -1.331  -15.112 1.00 26.58 ? 670  ALA   A C   1 
ATOM   1149 O  O   . ALA   A 1 148 ? 40.792 -1.371  -15.227 1.00 22.99 ? 670  ALA   A O   1 
ATOM   1150 C  CB  . ALA   A 1 148 ? 38.882 0.657   -13.755 1.00 23.00 ? 670  ALA   A CB  1 
ATOM   1151 N  N   . HIS   A 1 149 ? 38.822 -2.429  -14.942 1.00 23.21 ? 671  HIS   A N   1 
ATOM   1152 C  CA  . HIS   A 1 149 ? 39.430 -3.760  -14.999 1.00 25.54 ? 671  HIS   A CA  1 
ATOM   1153 C  C   . HIS   A 1 149 ? 40.178 -4.007  -16.309 1.00 31.63 ? 671  HIS   A C   1 
ATOM   1154 O  O   . HIS   A 1 149 ? 41.061 -4.872  -16.351 1.00 26.12 ? 671  HIS   A O   1 
ATOM   1155 C  CB  . HIS   A 1 149 ? 38.341 -4.817  -14.826 1.00 23.80 ? 671  HIS   A CB  1 
ATOM   1156 C  CG  . HIS   A 1 149 ? 37.305 -4.770  -15.899 1.00 24.08 ? 671  HIS   A CG  1 
ATOM   1157 N  ND1 . HIS   A 1 149 ? 36.252 -3.879  -15.880 1.00 26.84 ? 671  HIS   A ND1 1 
ATOM   1158 C  CD2 . HIS   A 1 149 ? 37.176 -5.482  -17.042 1.00 27.34 ? 671  HIS   A CD2 1 
ATOM   1159 C  CE1 . HIS   A 1 149 ? 35.515 -4.049  -16.964 1.00 30.70 ? 671  HIS   A CE1 1 
ATOM   1160 N  NE2 . HIS   A 1 149 ? 36.057 -5.017  -17.687 1.00 30.52 ? 671  HIS   A NE2 1 
ATOM   1161 N  N   . CYS   A 1 150 ? 39.841 -3.277  -17.377 1.00 27.26 ? 672  CYS   A N   1 
ATOM   1162 C  CA  . CYS   A 1 150 ? 40.549 -3.413  -18.643 1.00 33.11 ? 672  CYS   A CA  1 
ATOM   1163 C  C   . CYS   A 1 150 ? 42.012 -3.010  -18.551 1.00 30.24 ? 672  CYS   A C   1 
ATOM   1164 O  O   . CYS   A 1 150 ? 42.765 -3.274  -19.498 1.00 33.75 ? 672  CYS   A O   1 
ATOM   1165 C  CB  . CYS   A 1 150 ? 39.889 -2.576  -19.734 1.00 25.93 ? 672  CYS   A CB  1 
ATOM   1166 S  SG  . CYS   A 1 150 ? 38.258 -3.094  -20.286 1.00 30.74 ? 672  CYS   A SG  1 
ATOM   1167 N  N   . ILE   A 1 151 ? 42.451 -2.393  -17.448 1.00 22.04 ? 673  ILE   A N   1 
ATOM   1168 C  CA  . ILE   A 1 151 ? 43.878 -2.109  -17.340 1.00 26.24 ? 673  ILE   A CA  1 
ATOM   1169 C  C   . ILE   A 1 151 ? 44.663 -3.337  -16.918 1.00 32.77 ? 673  ILE   A C   1 
ATOM   1170 O  O   . ILE   A 1 151 ? 45.895 -3.327  -16.984 1.00 28.79 ? 673  ILE   A O   1 
ATOM   1171 C  CB  . ILE   A 1 151 ? 44.145 -0.947  -16.363 1.00 25.78 ? 673  ILE   A CB  1 
ATOM   1172 C  CG1 . ILE   A 1 151 ? 45.529 -0.322  -16.605 1.00 28.85 ? 673  ILE   A CG1 1 
ATOM   1173 C  CG2 . ILE   A 1 151 ? 43.996 -1.422  -14.934 1.00 25.64 ? 673  ILE   A CG2 1 
ATOM   1174 C  CD1 . ILE   A 1 151 ? 45.725 1.013   -15.916 1.00 25.13 ? 673  ILE   A CD1 1 
ATOM   1175 N  N   . SER   A 1 152 ? 43.988 -4.406  -16.507 1.00 34.60 ? 674  SER   A N   1 
ATOM   1176 C  CA  . SER   A 1 152 ? 44.660 -5.580  -15.960 1.00 37.83 ? 674  SER   A CA  1 
ATOM   1177 C  C   . SER   A 1 152 ? 44.990 -6.584  -17.062 1.00 32.74 ? 674  SER   A C   1 
ATOM   1178 O  O   . SER   A 1 152 ? 44.094 -7.061  -17.768 1.00 31.79 ? 674  SER   A O   1 
ATOM   1179 C  CB  . SER   A 1 152 ? 43.796 -6.254  -14.901 1.00 38.67 ? 674  SER   A CB  1 
ATOM   1180 O  OG  . SER   A 1 152 ? 44.385 -7.489  -14.537 1.00 41.73 ? 674  SER   A OG  1 
ATOM   1181 N  N   . GLU   A 1 153 ? 46.272 -6.933  -17.185 1.00 41.87 ? 675  GLU   A N   1 
ATOM   1182 C  CA  . GLU   A 1 153 ? 46.655 -7.944  -18.164 1.00 43.46 ? 675  GLU   A CA  1 
ATOM   1183 C  C   . GLU   A 1 153 ? 46.217 -9.338  -17.738 1.00 41.87 ? 675  GLU   A C   1 
ATOM   1184 O  O   . GLU   A 1 153 ? 46.129 -10.234 -18.585 1.00 39.99 ? 675  GLU   A O   1 
ATOM   1185 C  CB  . GLU   A 1 153 ? 48.165 -7.898  -18.407 1.00 43.26 ? 675  GLU   A CB  1 
ATOM   1186 C  CG  . GLU   A 1 153 ? 48.535 -8.169  -19.867 1.00 44.82 ? 675  GLU   A CG  1 
ATOM   1187 C  CD  . GLU   A 1 153 ? 49.744 -7.372  -20.342 1.00 52.96 ? 675  GLU   A CD  1 
ATOM   1188 O  OE1 . GLU   A 1 153 ? 50.251 -6.534  -19.570 1.00 49.83 ? 675  GLU   A OE1 1 
ATOM   1189 O  OE2 . GLU   A 1 153 ? 50.181 -7.585  -21.494 1.00 56.34 ? 675  GLU   A OE2 1 
ATOM   1190 N  N   . TRP   A 1 154 ? 45.901 -9.522  -16.456 1.00 41.58 ? 676  TRP   A N   1 
ATOM   1191 C  CA  . TRP   A 1 154 ? 45.443 -10.800 -15.926 1.00 46.34 ? 676  TRP   A CA  1 
ATOM   1192 C  C   . TRP   A 1 154 ? 43.970 -11.084 -16.192 1.00 47.82 ? 676  TRP   A C   1 
ATOM   1193 O  O   . TRP   A 1 154 ? 43.530 -12.221 -15.977 1.00 47.19 ? 676  TRP   A O   1 
ATOM   1194 C  CB  . TRP   A 1 154 ? 45.693 -10.850 -14.420 1.00 39.60 ? 676  TRP   A CB  1 
ATOM   1195 C  CG  . TRP   A 1 154 ? 47.101 -10.565 -14.047 1.00 38.82 ? 676  TRP   A CG  1 
ATOM   1196 C  CD1 . TRP   A 1 154 ? 47.639 -9.349  -13.737 1.00 46.38 ? 676  TRP   A CD1 1 
ATOM   1197 C  CD2 . TRP   A 1 154 ? 48.166 -11.517 -13.942 1.00 47.16 ? 676  TRP   A CD2 1 
ATOM   1198 N  NE1 . TRP   A 1 154 ? 48.972 -9.487  -13.438 1.00 43.02 ? 676  TRP   A NE1 1 
ATOM   1199 C  CE2 . TRP   A 1 154 ? 49.321 -10.808 -13.559 1.00 43.13 ? 676  TRP   A CE2 1 
ATOM   1200 C  CE3 . TRP   A 1 154 ? 48.254 -12.905 -14.138 1.00 42.68 ? 676  TRP   A CE3 1 
ATOM   1201 C  CZ2 . TRP   A 1 154 ? 50.555 -11.437 -13.364 1.00 39.35 ? 676  TRP   A CZ2 1 
ATOM   1202 C  CZ3 . TRP   A 1 154 ? 49.484 -13.529 -13.947 1.00 38.94 ? 676  TRP   A CZ3 1 
ATOM   1203 C  CH2 . TRP   A 1 154 ? 50.616 -12.789 -13.562 1.00 34.22 ? 676  TRP   A CH2 1 
ATOM   1204 N  N   . GLY   A 1 155 ? 43.193 -10.093 -16.629 1.00 46.45 ? 677  GLY   A N   1 
ATOM   1205 C  CA  . GLY   A 1 155 ? 41.780 -10.281 -16.882 1.00 44.37 ? 677  GLY   A CA  1 
ATOM   1206 C  C   . GLY   A 1 155 ? 41.484 -10.571 -18.346 1.00 50.19 ? 677  GLY   A C   1 
ATOM   1207 O  O   . GLY   A 1 155 ? 42.327 -10.420 -19.226 1.00 58.56 ? 677  GLY   A O   1 
ATOM   1208 N  N   . HIS   A 1 156 ? 40.243 -10.982 -18.597 1.00 53.08 ? 678  HIS   A N   1 
ATOM   1209 C  CA  . HIS   A 1 156 ? 39.863 -11.413 -19.936 1.00 60.16 ? 678  HIS   A CA  1 
ATOM   1210 C  C   . HIS   A 1 156 ? 39.630 -10.257 -20.903 1.00 60.84 ? 678  HIS   A C   1 
ATOM   1211 O  O   . HIS   A 1 156 ? 39.615 -10.489 -22.117 1.00 62.18 ? 678  HIS   A O   1 
ATOM   1212 C  CB  . HIS   A 1 156 ? 38.606 -12.294 -19.878 1.00 67.56 ? 678  HIS   A CB  1 
ATOM   1213 C  CG  . HIS   A 1 156 ? 38.899 -13.765 -19.852 1.00 80.04 ? 678  HIS   A CG  1 
ATOM   1214 N  ND1 . HIS   A 1 156 ? 39.069 -14.511 -21.000 1.00 87.45 ? 678  HIS   A ND1 1 
ATOM   1215 C  CD2 . HIS   A 1 156 ? 39.057 -14.627 -18.818 1.00 79.45 ? 678  HIS   A CD2 1 
ATOM   1216 C  CE1 . HIS   A 1 156 ? 39.317 -15.768 -20.675 1.00 82.64 ? 678  HIS   A CE1 1 
ATOM   1217 N  NE2 . HIS   A 1 156 ? 39.316 -15.865 -19.357 1.00 82.75 ? 678  HIS   A NE2 1 
ATOM   1218 N  N   . ASP   A 1 157 ? 39.461 -9.025  -20.417 1.00 42.01 ? 679  ASP   A N   1 
ATOM   1219 C  CA  . ASP   A 1 157 ? 39.122 -7.906  -21.293 1.00 32.54 ? 679  ASP   A CA  1 
ATOM   1220 C  C   . ASP   A 1 157 ? 40.167 -6.799  -21.222 1.00 40.70 ? 679  ASP   A C   1 
ATOM   1221 O  O   . ASP   A 1 157 ? 39.845 -5.615  -21.262 1.00 42.74 ? 679  ASP   A O   1 
ATOM   1222 C  CB  . ASP   A 1 157 ? 37.740 -7.350  -20.966 1.00 48.69 ? 679  ASP   A CB  1 
ATOM   1223 C  CG  . ASP   A 1 157 ? 37.174 -6.492  -22.096 1.00 66.63 ? 679  ASP   A CG  1 
ATOM   1224 O  OD1 . ASP   A 1 157 ? 37.795 -6.457  -23.184 1.00 67.13 ? 679  ASP   A OD1 1 
ATOM   1225 O  OD2 . ASP   A 1 157 ? 36.106 -5.866  -21.901 1.00 65.01 ? 679  ASP   A OD2 1 
ATOM   1226 N  N   . PHE   A 1 158 ? 41.434 -7.172  -21.117 1.00 33.49 ? 680  PHE   A N   1 
ATOM   1227 C  CA  . PHE   A 1 158 ? 42.504 -6.190  -21.190 1.00 36.00 ? 680  PHE   A CA  1 
ATOM   1228 C  C   . PHE   A 1 158 ? 42.447 -5.406  -22.499 1.00 44.78 ? 680  PHE   A C   1 
ATOM   1229 O  O   . PHE   A 1 158 ? 42.217 -5.968  -23.572 1.00 40.51 ? 680  PHE   A O   1 
ATOM   1230 C  CB  . PHE   A 1 158 ? 43.850 -6.887  -21.060 1.00 36.59 ? 680  PHE   A CB  1 
ATOM   1231 C  CG  . PHE   A 1 158 ? 45.024 -5.975  -21.261 1.00 43.62 ? 680  PHE   A CG  1 
ATOM   1232 C  CD1 . PHE   A 1 158 ? 45.400 -5.081  -20.269 1.00 41.31 ? 680  PHE   A CD1 1 
ATOM   1233 C  CD2 . PHE   A 1 158 ? 45.759 -6.017  -22.435 1.00 39.93 ? 680  PHE   A CD2 1 
ATOM   1234 C  CE1 . PHE   A 1 158 ? 46.494 -4.239  -20.439 1.00 45.79 ? 680  PHE   A CE1 1 
ATOM   1235 C  CE2 . PHE   A 1 158 ? 46.854 -5.176  -22.616 1.00 48.21 ? 680  PHE   A CE2 1 
ATOM   1236 C  CZ  . PHE   A 1 158 ? 47.220 -4.285  -21.618 1.00 46.36 ? 680  PHE   A CZ  1 
ATOM   1237 N  N   . ARG   A 1 159 ? 42.650 -4.093  -22.405 1.00 37.77 ? 681  ARG   A N   1 
ATOM   1238 C  CA  . ARG   A 1 159 ? 42.805 -3.228  -23.567 1.00 34.21 ? 681  ARG   A CA  1 
ATOM   1239 C  C   . ARG   A 1 159 ? 44.134 -2.491  -23.452 1.00 39.24 ? 681  ARG   A C   1 
ATOM   1240 O  O   . ARG   A 1 159 ? 44.402 -1.844  -22.432 1.00 42.12 ? 681  ARG   A O   1 
ATOM   1241 C  CB  . ARG   A 1 159 ? 41.655 -2.222  -23.675 1.00 32.44 ? 681  ARG   A CB  1 
ATOM   1242 C  CG  . ARG   A 1 159 ? 40.259 -2.825  -23.777 1.00 38.68 ? 681  ARG   A CG  1 
ATOM   1243 C  CD  . ARG   A 1 159 ? 39.238 -1.701  -23.649 1.00 36.91 ? 681  ARG   A CD  1 
ATOM   1244 N  NE  . ARG   A 1 159 ? 37.860 -2.144  -23.808 1.00 50.17 ? 681  ARG   A NE  1 
ATOM   1245 C  CZ  . ARG   A 1 159 ? 37.186 -2.079  -24.948 1.00 47.20 ? 681  ARG   A CZ  1 
ATOM   1246 N  NH1 . ARG   A 1 159 ? 37.752 -1.637  -26.060 1.00 50.03 ? 681  ARG   A NH1 1 
ATOM   1247 N  NH2 . ARG   A 1 159 ? 35.912 -2.460  -24.971 1.00 52.55 ? 681  ARG   A NH2 1 
ATOM   1248 N  N   . ASP   A 1 160 ? 44.962 -2.590  -24.499 1.00 38.55 ? 682  ASP   A N   1 
ATOM   1249 C  CA  . ASP   A 1 160 ? 46.259 -1.917  -24.494 1.00 40.27 ? 682  ASP   A CA  1 
ATOM   1250 C  C   . ASP   A 1 160 ? 46.100 -0.419  -24.267 1.00 32.17 ? 682  ASP   A C   1 
ATOM   1251 O  O   . ASP   A 1 160 ? 46.915 0.208   -23.576 1.00 33.29 ? 682  ASP   A O   1 
ATOM   1252 C  CB  . ASP   A 1 160 ? 46.982 -2.176  -25.812 1.00 49.63 ? 682  ASP   A CB  1 
ATOM   1253 C  CG  . ASP   A 1 160 ? 48.457 -2.442  -25.619 1.00 60.78 ? 682  ASP   A CG  1 
ATOM   1254 O  OD1 . ASP   A 1 160 ? 49.160 -1.563  -25.072 1.00 60.40 ? 682  ASP   A OD1 1 
ATOM   1255 O  OD2 . ASP   A 1 160 ? 48.904 -3.547  -25.997 1.00 69.72 ? 682  ASP   A OD2 1 
ATOM   1256 N  N   . SER   A 1 161 ? 45.033 0.157   -24.815 1.00 38.85 ? 683  SER   A N   1 
ATOM   1257 C  CA  . SER   A 1 161 ? 44.728 1.573   -24.631 1.00 34.47 ? 683  SER   A CA  1 
ATOM   1258 C  C   . SER   A 1 161 ? 44.653 2.005   -23.164 1.00 38.33 ? 683  SER   A C   1 
ATOM   1259 O  O   . SER   A 1 161 ? 44.707 3.209   -22.903 1.00 37.24 ? 683  SER   A O   1 
ATOM   1260 C  CB  . SER   A 1 161 ? 43.419 1.906   -25.355 1.00 35.48 ? 683  SER   A CB  1 
ATOM   1261 O  OG  . SER   A 1 161 ? 42.344 1.123   -24.886 1.00 43.35 ? 683  SER   A OG  1 
ATOM   1262 N  N   . PHE   A 1 162 ? 44.556 1.076   -22.203 1.00 32.77 ? 684  PHE   A N   1 
ATOM   1263 C  CA  . PHE   A 1 162 ? 44.498 1.426   -20.782 1.00 29.35 ? 684  PHE   A CA  1 
ATOM   1264 C  C   . PHE   A 1 162 ? 45.874 1.531   -20.114 1.00 32.65 ? 684  PHE   A C   1 
ATOM   1265 O  O   . PHE   A 1 162 ? 45.989 2.160   -19.053 1.00 27.73 ? 684  PHE   A O   1 
ATOM   1266 C  CB  . PHE   A 1 162 ? 43.615 0.406   -20.024 1.00 24.08 ? 684  PHE   A CB  1 
ATOM   1267 C  CG  . PHE   A 1 162 ? 42.127 0.731   -20.060 1.00 26.45 ? 684  PHE   A CG  1 
ATOM   1268 C  CD1 . PHE   A 1 162 ? 41.413 0.689   -21.253 1.00 23.51 ? 684  PHE   A CD1 1 
ATOM   1269 C  CD2 . PHE   A 1 162 ? 41.451 1.074   -18.897 1.00 25.99 ? 684  PHE   A CD2 1 
ATOM   1270 C  CE1 . PHE   A 1 162 ? 40.049 0.987   -21.290 1.00 29.29 ? 684  PHE   A CE1 1 
ATOM   1271 C  CE2 . PHE   A 1 162 ? 40.082 1.366   -18.925 1.00 28.03 ? 684  PHE   A CE2 1 
ATOM   1272 C  CZ  . PHE   A 1 162 ? 39.386 1.329   -20.129 1.00 24.69 ? 684  PHE   A CZ  1 
ATOM   1273 N  N   . ARG   A 1 163 ? 46.923 0.946   -20.709 1.00 40.02 ? 685  ARG   A N   1 
ATOM   1274 C  CA  . ARG   A 1 163 ? 48.233 0.900   -20.056 1.00 36.99 ? 685  ARG   A CA  1 
ATOM   1275 C  C   . ARG   A 1 163 ? 48.732 2.302   -19.714 1.00 26.95 ? 685  ARG   A C   1 
ATOM   1276 O  O   . ARG   A 1 163 ? 49.138 2.589   -18.574 1.00 31.97 ? 685  ARG   A O   1 
ATOM   1277 C  CB  . ARG   A 1 163 ? 49.231 0.194   -20.983 1.00 42.00 ? 685  ARG   A CB  1 
ATOM   1278 C  CG  . ARG   A 1 163 ? 49.987 -0.969  -20.392 1.00 52.82 ? 685  ARG   A CG  1 
ATOM   1279 C  CD  . ARG   A 1 163 ? 51.175 -1.372  -21.297 1.00 53.07 ? 685  ARG   A CD  1 
ATOM   1280 N  NE  . ARG   A 1 163 ? 50.799 -2.166  -22.467 1.00 52.68 ? 685  ARG   A NE  1 
ATOM   1281 C  CZ  . ARG   A 1 163 ? 50.873 -3.491  -22.531 1.00 53.06 ? 685  ARG   A CZ  1 
ATOM   1282 N  NH1 . ARG   A 1 163 ? 51.301 -4.211  -21.505 1.00 62.50 ? 685  ARG   A NH1 1 
ATOM   1283 N  NH2 . ARG   A 1 163 ? 50.512 -4.113  -23.652 1.00 55.12 ? 685  ARG   A NH2 1 
ATOM   1284 N  N   . LYS   A 1 164 ? 48.684 3.199   -20.689 1.00 31.59 ? 686  LYS   A N   1 
ATOM   1285 C  CA  . LYS   A 1 164 ? 49.213 4.537   -20.495 1.00 27.86 ? 686  LYS   A CA  1 
ATOM   1286 C  C   . LYS   A 1 164 ? 48.462 5.319   -19.422 1.00 32.72 ? 686  LYS   A C   1 
ATOM   1287 O  O   . LYS   A 1 164 ? 48.978 6.340   -18.942 1.00 28.44 ? 686  LYS   A O   1 
ATOM   1288 C  CB  . LYS   A 1 164 ? 49.191 5.275   -21.831 1.00 35.40 ? 686  LYS   A CB  1 
ATOM   1289 C  CG  . LYS   A 1 164 ? 50.026 4.575   -22.895 1.00 47.67 ? 686  LYS   A CG  1 
ATOM   1290 C  CD  . LYS   A 1 164 ? 50.055 5.330   -24.223 1.00 45.45 ? 686  LYS   A CD  1 
ATOM   1291 C  CE  . LYS   A 1 164 ? 51.470 5.324   -24.821 1.00 52.85 ? 686  LYS   A CE  1 
ATOM   1292 N  NZ  . LYS   A 1 164 ? 51.517 5.729   -26.260 1.00 51.97 ? 686  LYS   A NZ  1 
ATOM   1293 N  N   . LEU   A 1 165 ? 47.288 4.849   -18.982 1.00 23.70 ? 687  LEU   A N   1 
ATOM   1294 C  CA  . LEU   A 1 165 ? 46.603 5.600   -17.939 1.00 23.08 ? 687  LEU   A CA  1 
ATOM   1295 C  C   . LEU   A 1 165 ? 47.375 5.591   -16.644 1.00 21.38 ? 687  LEU   A C   1 
ATOM   1296 O  O   . LEU   A 1 165 ? 47.080 6.399   -15.756 1.00 22.59 ? 687  LEU   A O   1 
ATOM   1297 C  CB  . LEU   A 1 165 ? 45.195 5.042   -17.733 1.00 20.96 ? 687  LEU   A CB  1 
ATOM   1298 C  CG  . LEU   A 1 165 ? 44.315 5.158   -18.986 1.00 22.92 ? 687  LEU   A CG  1 
ATOM   1299 C  CD1 . LEU   A 1 165 ? 42.866 4.721   -18.698 1.00 23.06 ? 687  LEU   A CD1 1 
ATOM   1300 C  CD2 . LEU   A 1 165 ? 44.341 6.586   -19.512 1.00 25.99 ? 687  LEU   A CD2 1 
ATOM   1301 N  N   . GLY   A 1 166 ? 48.394 4.735   -16.533 1.00 24.63 ? 688  GLY   A N   1 
ATOM   1302 C  CA  . GLY   A 1 166 ? 49.287 4.817   -15.400 1.00 25.47 ? 688  GLY   A CA  1 
ATOM   1303 C  C   . GLY   A 1 166 ? 49.922 6.180   -15.204 1.00 30.20 ? 688  GLY   A C   1 
ATOM   1304 O  O   . GLY   A 1 166 ? 50.360 6.500   -14.100 1.00 36.65 ? 688  GLY   A O   1 
ATOM   1305 N  N   . SER   A 1 167 ? 49.970 7.009   -16.241 1.00 26.49 ? 689  SER   A N   1 
ATOM   1306 C  CA  . SER   A 1 167 ? 50.626 8.301   -16.080 1.00 26.82 ? 689  SER   A CA  1 
ATOM   1307 C  C   . SER   A 1 167 ? 49.706 9.391   -15.546 1.00 32.21 ? 689  SER   A C   1 
ATOM   1308 O  O   . SER   A 1 167 ? 50.211 10.450  -15.134 1.00 35.32 ? 689  SER   A O   1 
ATOM   1309 C  CB  . SER   A 1 167 ? 51.263 8.750   -17.402 1.00 30.85 ? 689  SER   A CB  1 
ATOM   1310 O  OG  . SER   A 1 167 ? 50.360 8.649   -18.470 1.00 41.30 ? 689  SER   A OG  1 
ATOM   1311 N  N   . LEU   A 1 168 ? 48.390 9.152   -15.498 1.00 22.68 ? 690  LEU   A N   1 
ATOM   1312 C  CA  . LEU   A 1 168 ? 47.476 10.174  -14.996 1.00 21.94 ? 690  LEU   A CA  1 
ATOM   1313 C  C   . LEU   A 1 168 ? 47.926 10.676  -13.639 1.00 29.88 ? 690  LEU   A C   1 
ATOM   1314 O  O   . LEU   A 1 168 ? 48.114 11.887  -13.422 1.00 24.98 ? 690  LEU   A O   1 
ATOM   1315 C  CB  . LEU   A 1 168 ? 46.054 9.614   -14.908 1.00 21.13 ? 690  LEU   A CB  1 
ATOM   1316 C  CG  . LEU   A 1 168 ? 45.307 9.345   -16.205 1.00 23.14 ? 690  LEU   A CG  1 
ATOM   1317 C  CD1 . LEU   A 1 168 ? 44.067 8.539   -15.880 1.00 22.50 ? 690  LEU   A CD1 1 
ATOM   1318 C  CD2 . LEU   A 1 168 ? 44.916 10.654  -16.865 1.00 27.39 ? 690  LEU   A CD2 1 
ATOM   1319 N  N   . LYS   A 1 169 ? 48.195 9.744   -12.735 1.00 23.81 ? 691  LYS   A N   1 
ATOM   1320 C  CA  . LYS   A 1 169 ? 48.482 10.129  -11.369 1.00 28.52 ? 691  LYS   A CA  1 
ATOM   1321 C  C   . LYS   A 1 169 ? 49.857 10.771  -11.245 1.00 28.81 ? 691  LYS   A C   1 
ATOM   1322 O  O   . LYS   A 1 169 ? 50.073 11.580  -10.338 1.00 30.73 ? 691  LYS   A O   1 
ATOM   1323 C  CB  . LYS   A 1 169 ? 48.351 8.910   -10.457 1.00 31.68 ? 691  LYS   A CB  1 
ATOM   1324 C  CG  . LYS   A 1 169 ? 48.019 9.248   -9.026  1.00 34.67 ? 691  LYS   A CG  1 
ATOM   1325 C  CD  . LYS   A 1 169 ? 46.593 9.768   -8.858  1.00 33.23 ? 691  LYS   A CD  1 
ATOM   1326 C  CE  . LYS   A 1 169 ? 46.457 10.263  -7.454  1.00 28.90 ? 691  LYS   A CE  1 
ATOM   1327 N  NZ  . LYS   A 1 169 ? 45.188 10.927  -7.185  1.00 24.41 ? 691  LYS   A NZ  1 
ATOM   1328 N  N   . THR   A 1 170 ? 50.789 10.472  -12.155 1.00 25.38 ? 692  THR   A N   1 
ATOM   1329 C  CA  . THR   A 1 170 ? 52.067 11.148  -12.025 1.00 29.70 ? 692  THR   A CA  1 
ATOM   1330 C  C   . THR   A 1 170 ? 52.013 12.516  -12.683 1.00 28.88 ? 692  THR   A C   1 
ATOM   1331 O  O   . THR   A 1 170 ? 52.728 13.423  -12.249 1.00 27.05 ? 692  THR   A O   1 
ATOM   1332 C  CB  . THR   A 1 170 ? 53.218 10.308  -12.591 1.00 29.87 ? 692  THR   A CB  1 
ATOM   1333 O  OG1 . THR   A 1 170 ? 53.056 10.125  -14.000 1.00 34.38 ? 692  THR   A OG1 1 
ATOM   1334 C  CG2 . THR   A 1 170 ? 53.248 8.959   -11.907 1.00 32.84 ? 692  THR   A CG2 1 
ATOM   1335 N  N   . ALA   A 1 171 ? 51.144 12.706  -13.679 1.00 28.53 ? 693  ALA   A N   1 
ATOM   1336 C  CA  . ALA   A 1 171 ? 51.041 14.038  -14.267 1.00 23.61 ? 693  ALA   A CA  1 
ATOM   1337 C  C   . ALA   A 1 171 ? 50.120 14.942  -13.480 1.00 23.72 ? 693  ALA   A C   1 
ATOM   1338 O  O   . ALA   A 1 171 ? 50.246 16.181  -13.558 1.00 19.90 ? 693  ALA   A O   1 
ATOM   1339 C  CB  . ALA   A 1 171 ? 50.546 13.943  -15.711 1.00 25.98 ? 693  ALA   A CB  1 
ATOM   1340 N  N   . LEU   A 1 172 ? 49.165 14.348  -12.757 1.00 17.73 ? 694  LEU   A N   1 
ATOM   1341 C  CA  . LEU   A 1 172 ? 48.140 15.092  -12.026 1.00 17.72 ? 694  LEU   A CA  1 
ATOM   1342 C  C   . LEU   A 1 172 ? 47.975 14.504  -10.632 1.00 21.95 ? 694  LEU   A C   1 
ATOM   1343 O  O   . LEU   A 1 172 ? 46.900 14.014  -10.278 1.00 22.10 ? 694  LEU   A O   1 
ATOM   1344 C  CB  . LEU   A 1 172 ? 46.813 15.052  -12.786 1.00 21.65 ? 694  LEU   A CB  1 
ATOM   1345 C  CG  . LEU   A 1 172 ? 46.893 15.754  -14.139 1.00 26.64 ? 694  LEU   A CG  1 
ATOM   1346 C  CD1 . LEU   A 1 172 ? 45.746 15.328  -15.033 1.00 29.81 ? 694  LEU   A CD1 1 
ATOM   1347 C  CD2 . LEU   A 1 172 ? 46.898 17.249  -13.920 1.00 23.39 ? 694  LEU   A CD2 1 
ATOM   1348 N  N   . PRO   A 1 173 ? 49.027 14.538  -9.805  1.00 27.92 ? 695  PRO   A N   1 
ATOM   1349 C  CA  . PRO   A 1 173 ? 48.976 13.787  -8.537  1.00 25.99 ? 695  PRO   A CA  1 
ATOM   1350 C  C   . PRO   A 1 173 ? 47.951 14.307  -7.545  1.00 24.46 ? 695  PRO   A C   1 
ATOM   1351 O  O   . PRO   A 1 173 ? 47.548 13.550  -6.652  1.00 27.26 ? 695  PRO   A O   1 
ATOM   1352 C  CB  . PRO   A 1 173 ? 50.408 13.908  -7.993  1.00 28.47 ? 695  PRO   A CB  1 
ATOM   1353 C  CG  . PRO   A 1 173 ? 50.919 15.188  -8.596  1.00 31.86 ? 695  PRO   A CG  1 
ATOM   1354 C  CD  . PRO   A 1 173 ? 50.300 15.265  -9.969  1.00 26.75 ? 695  PRO   A CD  1 
ATOM   1355 N  N   . MET   A 1 174 ? 47.498 15.544  -7.673  1.00 21.70 ? 696  MET   A N   1 
ATOM   1356 C  CA  . MET   A 1 174 ? 46.504 16.046  -6.739  1.00 26.41 ? 696  MET   A CA  1 
ATOM   1357 C  C   . MET   A 1 174 ? 45.056 15.746  -7.159  1.00 23.14 ? 696  MET   A C   1 
ATOM   1358 O  O   . MET   A 1 174 ? 44.143 16.020  -6.379  1.00 25.82 ? 696  MET   A O   1 
ATOM   1359 C  CB  . MET   A 1 174 ? 46.674 17.555  -6.553  1.00 30.66 ? 696  MET   A CB  1 
ATOM   1360 C  CG  . MET   A 1 174 ? 46.205 18.402  -7.750  1.00 37.44 ? 696  MET   A CG  1 
ATOM   1361 S  SD  . MET   A 1 174 ? 47.348 18.446  -9.158  1.00 41.04 ? 696  MET   A SD  1 
ATOM   1362 C  CE  . MET   A 1 174 ? 48.817 19.091  -8.363  1.00 43.93 ? 696  MET   A CE  1 
ATOM   1363 N  N   . VAL   A 1 175 ? 44.821 15.223  -8.360  1.00 16.75 ? 697  VAL   A N   1 
ATOM   1364 C  CA  . VAL   A 1 175 ? 43.471 15.032  -8.881  1.00 20.90 ? 697  VAL   A CA  1 
ATOM   1365 C  C   . VAL   A 1 175 ? 43.020 13.623  -8.502  1.00 20.69 ? 697  VAL   A C   1 
ATOM   1366 O  O   . VAL   A 1 175 ? 43.726 12.655  -8.829  1.00 20.16 ? 697  VAL   A O   1 
ATOM   1367 C  CB  . VAL   A 1 175 ? 43.433 15.238  -10.402 1.00 22.33 ? 697  VAL   A CB  1 
ATOM   1368 C  CG1 . VAL   A 1 175 ? 42.045 15.042  -10.939 1.00 16.74 ? 697  VAL   A CG1 1 
ATOM   1369 C  CG2 . VAL   A 1 175 ? 43.945 16.665  -10.764 1.00 19.45 ? 697  VAL   A CG2 1 
ATOM   1370 N  N   . PRO   A 1 176 ? 41.886 13.456  -7.811  1.00 17.68 ? 698  PRO   A N   1 
ATOM   1371 C  CA  . PRO   A 1 176 ? 41.459 12.092  -7.458  1.00 15.79 ? 698  PRO   A CA  1 
ATOM   1372 C  C   . PRO   A 1 176 ? 41.014 11.346  -8.693  1.00 19.61 ? 698  PRO   A C   1 
ATOM   1373 O  O   . PRO   A 1 176 ? 40.391 11.913  -9.591  1.00 19.56 ? 698  PRO   A O   1 
ATOM   1374 C  CB  . PRO   A 1 176 ? 40.293 12.293  -6.484  1.00 22.42 ? 698  PRO   A CB  1 
ATOM   1375 C  CG  . PRO   A 1 176 ? 39.806 13.667  -6.704  1.00 20.84 ? 698  PRO   A CG  1 
ATOM   1376 C  CD  . PRO   A 1 176 ? 40.985 14.488  -7.264  1.00 18.15 ? 698  PRO   A CD  1 
ATOM   1377 N  N   . ILE   A 1 177 ? 41.314 10.051  -8.719  1.00 16.23 ? 699  ILE   A N   1 
ATOM   1378 C  CA  . ILE   A 1 177 ? 40.839 9.157   -9.767  1.00 15.96 ? 699  ILE   A CA  1 
ATOM   1379 C  C   . ILE   A 1 177 ? 39.777 8.262   -9.153  1.00 21.08 ? 699  ILE   A C   1 
ATOM   1380 O  O   . ILE   A 1 177 ? 39.978 7.744   -8.051  1.00 19.99 ? 699  ILE   A O   1 
ATOM   1381 C  CB  . ILE   A 1 177 ? 41.980 8.314   -10.355 1.00 20.92 ? 699  ILE   A CB  1 
ATOM   1382 C  CG1 . ILE   A 1 177 ? 42.959 9.185   -11.153 1.00 20.33 ? 699  ILE   A CG1 1 
ATOM   1383 C  CG2 . ILE   A 1 177 ? 41.427 7.181   -11.213 1.00 19.32 ? 699  ILE   A CG2 1 
ATOM   1384 C  CD1 . ILE   A 1 177 ? 44.163 8.395   -11.653 1.00 24.01 ? 699  ILE   A CD1 1 
ATOM   1385 N  N   . VAL   A 1 178 ? 38.653 8.108   -9.845  1.00 18.21 ? 700  VAL   A N   1 
ATOM   1386 C  CA  . VAL   A 1 178 ? 37.585 7.180   -9.452  1.00 16.11 ? 700  VAL   A CA  1 
ATOM   1387 C  C   . VAL   A 1 178 ? 37.561 6.080   -10.504 1.00 18.39 ? 700  VAL   A C   1 
ATOM   1388 O  O   . VAL   A 1 178 ? 37.115 6.302   -11.635 1.00 17.57 ? 700  VAL   A O   1 
ATOM   1389 C  CB  . VAL   A 1 178 ? 36.225 7.879   -9.333  1.00 20.38 ? 700  VAL   A CB  1 
ATOM   1390 C  CG1 . VAL   A 1 178 ? 35.070 6.860   -9.055  1.00 17.09 ? 700  VAL   A CG1 1 
ATOM   1391 C  CG2 . VAL   A 1 178 ? 36.262 8.993   -8.246  1.00 19.61 ? 700  VAL   A CG2 1 
ATOM   1392 N  N   . ALA   A 1 179 ? 38.053 4.893   -10.149 1.00 16.69 ? 701  ALA   A N   1 
ATOM   1393 C  CA  . ALA   A 1 179 ? 38.083 3.758   -11.066 1.00 19.85 ? 701  ALA   A CA  1 
ATOM   1394 C  C   . ALA   A 1 179 ? 36.829 2.938   -10.824 1.00 18.42 ? 701  ALA   A C   1 
ATOM   1395 O  O   . ALA   A 1 179 ? 36.560 2.560   -9.685  1.00 18.61 ? 701  ALA   A O   1 
ATOM   1396 C  CB  . ALA   A 1 179 ? 39.326 2.902   -10.828 1.00 20.43 ? 701  ALA   A CB  1 
ATOM   1397 N  N   . LEU   A 1 180 ? 36.064 2.685   -11.880 1.00 15.07 ? 702  LEU   A N   1 
ATOM   1398 C  CA  . LEU   A 1 180 ? 34.779 2.001   -11.756 1.00 16.47 ? 702  LEU   A CA  1 
ATOM   1399 C  C   . LEU   A 1 180 ? 34.825 0.667   -12.486 1.00 22.08 ? 702  LEU   A C   1 
ATOM   1400 O  O   . LEU   A 1 180 ? 35.314 0.585   -13.617 1.00 21.54 ? 702  LEU   A O   1 
ATOM   1401 C  CB  . LEU   A 1 180 ? 33.660 2.846   -12.353 1.00 18.85 ? 702  LEU   A CB  1 
ATOM   1402 C  CG  . LEU   A 1 180 ? 33.658 4.269   -11.830 1.00 25.76 ? 702  LEU   A CG  1 
ATOM   1403 C  CD1 . LEU   A 1 180 ? 33.201 5.206   -12.929 1.00 31.76 ? 702  LEU   A CD1 1 
ATOM   1404 C  CD2 . LEU   A 1 180 ? 32.774 4.369   -10.633 1.00 20.22 ? 702  LEU   A CD2 1 
ATOM   1405 N  N   . THR   A 1 181 ? 34.287 -0.374  -11.863 1.00 16.92 ? 703  THR   A N   1 
ATOM   1406 C  CA  . THR   A 1 181 ? 34.233 -1.637  -12.596 1.00 17.83 ? 703  THR   A CA  1 
ATOM   1407 C  C   . THR   A 1 181 ? 33.123 -2.481  -11.993 1.00 22.49 ? 703  THR   A C   1 
ATOM   1408 O  O   . THR   A 1 181 ? 32.690 -2.235  -10.869 1.00 19.10 ? 703  THR   A O   1 
ATOM   1409 C  CB  . THR   A 1 181 ? 35.573 -2.387  -12.550 1.00 23.00 ? 703  THR   A CB  1 
ATOM   1410 O  OG1 . THR   A 1 181 ? 35.422 -3.670  -13.151 1.00 25.73 ? 703  THR   A OG1 1 
ATOM   1411 C  CG2 . THR   A 1 181 ? 36.012 -2.588  -11.143 1.00 21.83 ? 703  THR   A CG2 1 
ATOM   1412 N  N   . ALA   A 1 182 ? 32.648 -3.461  -12.759 1.00 22.86 ? 704  ALA   A N   1 
ATOM   1413 C  CA  . ALA   A 1 182 ? 31.701 -4.430  -12.221 1.00 23.77 ? 704  ALA   A CA  1 
ATOM   1414 C  C   . ALA   A 1 182 ? 32.363 -5.743  -11.841 1.00 31.42 ? 704  ALA   A C   1 
ATOM   1415 O  O   . ALA   A 1 182 ? 31.693 -6.638  -11.321 1.00 37.13 ? 704  ALA   A O   1 
ATOM   1416 C  CB  . ALA   A 1 182 ? 30.570 -4.693  -13.230 1.00 25.18 ? 704  ALA   A CB  1 
ATOM   1417 N  N   . THR   A 1 183 ? 33.648 -5.904  -12.074 1.00 21.26 ? 705  THR   A N   1 
ATOM   1418 C  CA  . THR   A 1 183 ? 34.208 -7.231  -11.888 1.00 28.72 ? 705  THR   A CA  1 
ATOM   1419 C  C   . THR   A 1 183 ? 34.522 -7.474  -10.421 1.00 36.59 ? 705  THR   A C   1 
ATOM   1420 O  O   . THR   A 1 183 ? 35.238 -6.696  -9.788  1.00 37.05 ? 705  THR   A O   1 
ATOM   1421 C  CB  . THR   A 1 183 ? 35.459 -7.413  -12.710 1.00 39.81 ? 705  THR   A CB  1 
ATOM   1422 O  OG1 . THR   A 1 183 ? 36.500 -6.631  -12.104 1.00 37.24 ? 705  THR   A OG1 1 
ATOM   1423 C  CG2 . THR   A 1 183 ? 35.189 -7.005  -14.172 1.00 27.08 ? 705  THR   A CG2 1 
ATOM   1424 N  N   . ALA   A 1 184 ? 34.016 -8.579  -9.895  1.00 33.87 ? 706  ALA   A N   1 
ATOM   1425 C  CA  . ALA   A 1 184 ? 34.214 -8.928  -8.497  1.00 40.24 ? 706  ALA   A CA  1 
ATOM   1426 C  C   . ALA   A 1 184 ? 35.345 -9.951  -8.384  1.00 38.25 ? 706  ALA   A C   1 
ATOM   1427 O  O   . ALA   A 1 184 ? 35.169 -11.116 -8.011  1.00 41.73 ? 706  ALA   A O   1 
ATOM   1428 C  CB  . ALA   A 1 184 ? 32.909 -9.437  -7.897  1.00 47.01 ? 706  ALA   A CB  1 
ATOM   1429 N  N   . SER   A 1 185 ? 36.537 -9.482  -8.734  1.00 42.36 ? 707  SER   A N   1 
ATOM   1430 C  CA  . SER   A 1 185 ? 37.775 -10.228 -8.551  1.00 40.63 ? 707  SER   A CA  1 
ATOM   1431 C  C   . SER   A 1 185 ? 38.694 -9.364  -7.705  1.00 36.81 ? 707  SER   A C   1 
ATOM   1432 O  O   . SER   A 1 185 ? 39.000 -8.231  -8.085  1.00 37.38 ? 707  SER   A O   1 
ATOM   1433 C  CB  . SER   A 1 185 ? 38.419 -10.571 -9.894  1.00 35.25 ? 707  SER   A CB  1 
ATOM   1434 O  OG  . SER   A 1 185 ? 39.766 -10.994 -9.718  1.00 44.91 ? 707  SER   A OG  1 
ATOM   1435 N  N   . SER   A 1 186 ? 39.109 -9.885  -6.548  1.00 34.03 ? 708  SER   A N   1 
ATOM   1436 C  CA  . SER   A 1 186 ? 39.965 -9.112  -5.650  1.00 34.24 ? 708  SER   A CA  1 
ATOM   1437 C  C   . SER   A 1 186 ? 41.337 -8.861  -6.274  1.00 41.81 ? 708  SER   A C   1 
ATOM   1438 O  O   . SER   A 1 186 ? 41.958 -7.817  -6.027  1.00 41.75 ? 708  SER   A O   1 
ATOM   1439 C  CB  . SER   A 1 186 ? 40.128 -9.847  -4.321  1.00 43.85 ? 708  SER   A CB  1 
ATOM   1440 O  OG  . SER   A 1 186 ? 40.796 -11.099 -4.526  1.00 47.20 ? 708  SER   A OG  1 
ATOM   1441 N  N   . SER   A 1 187 ? 41.822 -9.795  -7.090  1.00 33.85 ? 709  SER   A N   1 
ATOM   1442 C  CA  . SER   A 1 187 ? 43.131 -9.611  -7.701  1.00 44.69 ? 709  SER   A CA  1 
ATOM   1443 C  C   . SER   A 1 187 ? 43.071 -8.619  -8.861  1.00 37.88 ? 709  SER   A C   1 
ATOM   1444 O  O   . SER   A 1 187 ? 43.991 -7.809  -9.028  1.00 32.56 ? 709  SER   A O   1 
ATOM   1445 C  CB  . SER   A 1 187 ? 43.705 -10.959 -8.147  1.00 41.80 ? 709  SER   A CB  1 
ATOM   1446 O  OG  . SER   A 1 187 ? 43.000 -11.477 -9.248  1.00 42.38 ? 709  SER   A OG  1 
ATOM   1447 N  N   . ILE   A 1 188 ? 42.004 -8.657  -9.669  1.00 33.62 ? 710  ILE   A N   1 
ATOM   1448 C  CA  . ILE   A 1 188 ? 41.791 -7.587  -10.643 1.00 34.67 ? 710  ILE   A CA  1 
ATOM   1449 C  C   . ILE   A 1 188 ? 41.742 -6.232  -9.945  1.00 30.59 ? 710  ILE   A C   1 
ATOM   1450 O  O   . ILE   A 1 188 ? 42.309 -5.248  -10.428 1.00 29.54 ? 710  ILE   A O   1 
ATOM   1451 C  CB  . ILE   A 1 188 ? 40.514 -7.837  -11.461 1.00 39.36 ? 710  ILE   A CB  1 
ATOM   1452 C  CG1 . ILE   A 1 188 ? 40.661 -9.072  -12.341 1.00 37.28 ? 710  ILE   A CG1 1 
ATOM   1453 C  CG2 . ILE   A 1 188 ? 40.241 -6.640  -12.334 1.00 39.54 ? 710  ILE   A CG2 1 
ATOM   1454 C  CD1 . ILE   A 1 188 ? 41.531 -8.851  -13.558 1.00 43.92 ? 710  ILE   A CD1 1 
ATOM   1455 N  N   . ARG   A 1 189 ? 41.069 -6.156  -8.796  1.00 29.70 ? 711  ARG   A N   1 
ATOM   1456 C  CA  . ARG   A 1 189 ? 40.986 -4.901  -8.058  1.00 29.79 ? 711  ARG   A CA  1 
ATOM   1457 C  C   . ARG   A 1 189 ? 42.365 -4.416  -7.616  1.00 38.92 ? 711  ARG   A C   1 
ATOM   1458 O  O   . ARG   A 1 189 ? 42.705 -3.227  -7.758  1.00 31.49 ? 711  ARG   A O   1 
ATOM   1459 C  CB  . ARG   A 1 189 ? 40.060 -5.093  -6.860  1.00 41.17 ? 711  ARG   A CB  1 
ATOM   1460 C  CG  . ARG   A 1 189 ? 39.653 -3.831  -6.158  1.00 45.77 ? 711  ARG   A CG  1 
ATOM   1461 C  CD  . ARG   A 1 189 ? 38.680 -4.158  -5.032  1.00 36.09 ? 711  ARG   A CD  1 
ATOM   1462 N  NE  . ARG   A 1 189 ? 39.364 -4.791  -3.911  1.00 43.96 ? 711  ARG   A NE  1 
ATOM   1463 C  CZ  . ARG   A 1 189 ? 39.101 -6.012  -3.474  1.00 45.64 ? 711  ARG   A CZ  1 
ATOM   1464 N  NH1 . ARG   A 1 189 ? 38.143 -6.744  -4.017  1.00 37.67 ? 711  ARG   A NH1 1 
ATOM   1465 N  NH2 . ARG   A 1 189 ? 39.818 -6.511  -2.470  1.00 38.90 ? 711  ARG   A NH2 1 
ATOM   1466 N  N   . GLU   A 1 190 ? 43.179 -5.324  -7.056  1.00 29.18 ? 712  GLU   A N   1 
ATOM   1467 C  CA  . GLU   A 1 190 ? 44.539 -4.948  -6.673  1.00 32.59 ? 712  GLU   A CA  1 
ATOM   1468 C  C   . GLU   A 1 190 ? 45.342 -4.489  -7.889  1.00 22.39 ? 712  GLU   A C   1 
ATOM   1469 O  O   . GLU   A 1 190 ? 46.156 -3.567  -7.800  1.00 28.48 ? 712  GLU   A O   1 
ATOM   1470 C  CB  . GLU   A 1 190 ? 45.225 -6.135  -5.973  1.00 38.13 ? 712  GLU   A CB  1 
ATOM   1471 C  CG  . GLU   A 1 190 ? 44.474 -6.609  -4.718  1.00 47.93 ? 712  GLU   A CG  1 
ATOM   1472 C  CD  . GLU   A 1 190 ? 45.016 -7.907  -4.094  1.00 64.45 ? 712  GLU   A CD  1 
ATOM   1473 O  OE1 . GLU   A 1 190 ? 45.510 -8.796  -4.828  1.00 50.88 ? 712  GLU   A OE1 1 
ATOM   1474 O  OE2 . GLU   A 1 190 ? 44.932 -8.038  -2.851  1.00 67.70 ? 712  GLU   A OE2 1 
ATOM   1475 N  N   . ASP   A 1 191 ? 45.105 -5.119  -9.041  1.00 27.27 ? 713  ASP   A N   1 
ATOM   1476 C  CA  . ASP   A 1 191 ? 45.791 -4.731  -10.266 1.00 24.75 ? 713  ASP   A CA  1 
ATOM   1477 C  C   . ASP   A 1 191 ? 45.410 -3.317  -10.691 1.00 29.07 ? 713  ASP   A C   1 
ATOM   1478 O  O   . ASP   A 1 191 ? 46.247 -2.552  -11.178 1.00 25.91 ? 713  ASP   A O   1 
ATOM   1479 C  CB  . ASP   A 1 191 ? 45.438 -5.696  -11.383 1.00 30.27 ? 713  ASP   A CB  1 
ATOM   1480 C  CG  . ASP   A 1 191 ? 46.617 -5.973  -12.269 1.00 50.95 ? 713  ASP   A CG  1 
ATOM   1481 O  OD1 . ASP   A 1 191 ? 47.745 -5.662  -11.848 1.00 50.27 ? 713  ASP   A OD1 1 
ATOM   1482 O  OD2 . ASP   A 1 191 ? 46.429 -6.513  -13.375 1.00 57.25 ? 713  ASP   A OD2 1 
ATOM   1483 N  N   . ILE   A 1 192 ? 44.128 -2.988  -10.586 1.00 21.40 ? 714  ILE   A N   1 
ATOM   1484 C  CA  . ILE   A 1 192 ? 43.675 -1.636  -10.910 1.00 20.55 ? 714  ILE   A CA  1 
ATOM   1485 C  C   . ILE   A 1 192 ? 44.386 -0.624  -10.029 1.00 19.68 ? 714  ILE   A C   1 
ATOM   1486 O  O   . ILE   A 1 192 ? 44.862 0.416   -10.504 1.00 24.48 ? 714  ILE   A O   1 
ATOM   1487 C  CB  . ILE   A 1 192 ? 42.151 -1.540  -10.738 1.00 16.99 ? 714  ILE   A CB  1 
ATOM   1488 C  CG1 . ILE   A 1 192 ? 41.431 -2.397  -11.774 1.00 22.32 ? 714  ILE   A CG1 1 
ATOM   1489 C  CG2 . ILE   A 1 192 ? 41.715 -0.043  -10.779 1.00 20.30 ? 714  ILE   A CG2 1 
ATOM   1490 C  CD1 . ILE   A 1 192 ? 39.918 -2.447  -11.580 1.00 24.33 ? 714  ILE   A CD1 1 
ATOM   1491 N  N   . VAL   A 1 193 ? 44.437 -0.893  -8.720  1.00 22.67 ? 715  VAL   A N   1 
ATOM   1492 C  CA  . VAL   A 1 193 ? 45.097 0.034   -7.804  1.00 25.24 ? 715  VAL   A CA  1 
ATOM   1493 C  C   . VAL   A 1 193 ? 46.557 0.223   -8.197  1.00 28.75 ? 715  VAL   A C   1 
ATOM   1494 O  O   . VAL   A 1 193 ? 47.077 1.347   -8.190  1.00 26.08 ? 715  VAL   A O   1 
ATOM   1495 C  CB  . VAL   A 1 193 ? 44.975 -0.450  -6.347  1.00 26.71 ? 715  VAL   A CB  1 
ATOM   1496 C  CG1 . VAL   A 1 193 ? 45.845 0.392   -5.439  1.00 22.68 ? 715  VAL   A CG1 1 
ATOM   1497 C  CG2 . VAL   A 1 193 ? 43.524 -0.382  -5.885  1.00 23.04 ? 715  VAL   A CG2 1 
ATOM   1498 N  N   . ARG   A 1 194 ? 47.238 -0.879  -8.550  1.00 27.19 ? 716  ARG   A N   1 
ATOM   1499 C  CA  . ARG   A 1 194 ? 48.656 -0.810  -8.898  1.00 28.62 ? 716  ARG   A CA  1 
ATOM   1500 C  C   . ARG   A 1 194 ? 48.881 -0.079  -10.219 1.00 23.28 ? 716  ARG   A C   1 
ATOM   1501 O  O   . ARG   A 1 194 ? 49.712 0.829   -10.304 1.00 26.48 ? 716  ARG   A O   1 
ATOM   1502 C  CB  . ARG   A 1 194 ? 49.231 -2.224  -8.966  1.00 23.77 ? 716  ARG   A CB  1 
ATOM   1503 C  CG  . ARG   A 1 194 ? 50.568 -2.335  -9.673  1.00 40.42 ? 716  ARG   A CG  1 
ATOM   1504 C  CD  . ARG   A 1 194 ? 51.157 -3.751  -9.528  1.00 36.36 ? 716  ARG   A CD  1 
ATOM   1505 N  NE  . ARG   A 1 194 ? 50.534 -4.744  -10.400 1.00 39.67 ? 716  ARG   A NE  1 
ATOM   1506 C  CZ  . ARG   A 1 194 ? 50.794 -4.879  -11.697 1.00 50.16 ? 716  ARG   A CZ  1 
ATOM   1507 N  NH1 . ARG   A 1 194 ? 51.562 -4.017  -12.342 1.00 57.21 ? 716  ARG   A NH1 1 
ATOM   1508 N  NH2 . ARG   A 1 194 ? 50.282 -5.914  -12.363 1.00 57.25 ? 716  ARG   A NH2 1 
ATOM   1509 N  N   . CYS   A 1 195 ? 48.161 -0.473  -11.263 1.00 22.50 ? 717  CYS   A N   1 
ATOM   1510 C  CA  . CYS   A 1 195 ? 48.427 0.061   -12.588 1.00 17.49 ? 717  CYS   A CA  1 
ATOM   1511 C  C   . CYS   A 1 195 ? 48.030 1.527   -12.692 1.00 24.22 ? 717  CYS   A C   1 
ATOM   1512 O  O   . CYS   A 1 195 ? 48.697 2.282   -13.404 1.00 23.20 ? 717  CYS   A O   1 
ATOM   1513 C  CB  . CYS   A 1 195 ? 47.703 -0.750  -13.647 1.00 19.34 ? 717  CYS   A CB  1 
ATOM   1514 S  SG  . CYS   A 1 195 ? 48.354 -2.472  -13.787 1.00 32.74 ? 717  CYS   A SG  1 
ATOM   1515 N  N   . LEU   A 1 196 ? 46.976 1.956   -11.987 1.00 21.68 ? 718  LEU   A N   1 
ATOM   1516 C  CA  . LEU   A 1 196 ? 46.649 3.382   -11.997 1.00 20.69 ? 718  LEU   A CA  1 
ATOM   1517 C  C   . LEU   A 1 196 ? 47.439 4.182   -10.978 1.00 22.05 ? 718  LEU   A C   1 
ATOM   1518 O  O   . LEU   A 1 196 ? 47.256 5.400   -10.913 1.00 23.85 ? 718  LEU   A O   1 
ATOM   1519 C  CB  . LEU   A 1 196 ? 45.146 3.625   -11.753 1.00 19.99 ? 718  LEU   A CB  1 
ATOM   1520 C  CG  . LEU   A 1 196 ? 44.222 3.155   -12.868 1.00 21.92 ? 718  LEU   A CG  1 
ATOM   1521 C  CD1 . LEU   A 1 196 ? 42.730 3.296   -12.517 1.00 19.75 ? 718  LEU   A CD1 1 
ATOM   1522 C  CD2 . LEU   A 1 196 ? 44.540 3.906   -14.151 1.00 23.12 ? 718  LEU   A CD2 1 
ATOM   1523 N  N   . ASN   A 1 197 ? 48.317 3.545   -10.188 1.00 24.28 ? 719  ASN   A N   1 
ATOM   1524 C  CA  . ASN   A 1 197 ? 49.157 4.251   -9.210  1.00 21.17 ? 719  ASN   A CA  1 
ATOM   1525 C  C   . ASN   A 1 197 ? 48.324 5.023   -8.185  1.00 25.17 ? 719  ASN   A C   1 
ATOM   1526 O  O   . ASN   A 1 197 ? 48.708 6.115   -7.737  1.00 21.05 ? 719  ASN   A O   1 
ATOM   1527 C  CB  . ASN   A 1 197 ? 50.155 5.201   -9.909  1.00 25.50 ? 719  ASN   A CB  1 
ATOM   1528 C  CG  . ASN   A 1 197 ? 51.198 4.451   -10.763 1.00 30.80 ? 719  ASN   A CG  1 
ATOM   1529 O  OD1 . ASN   A 1 197 ? 51.911 3.582   -10.274 1.00 30.03 ? 719  ASN   A OD1 1 
ATOM   1530 N  ND2 . ASN   A 1 197 ? 51.276 4.793   -12.042 1.00 32.34 ? 719  ASN   A ND2 1 
ATOM   1531 N  N   . LEU   A 1 198 ? 47.166 4.481   -7.816  1.00 23.82 ? 720  LEU   A N   1 
ATOM   1532 C  CA  . LEU   A 1 198 ? 46.292 5.163   -6.874  1.00 19.46 ? 720  LEU   A CA  1 
ATOM   1533 C  C   . LEU   A 1 198 ? 46.958 5.269   -5.506  1.00 25.96 ? 720  LEU   A C   1 
ATOM   1534 O  O   . LEU   A 1 198 ? 47.798 4.447   -5.126  1.00 25.71 ? 720  LEU   A O   1 
ATOM   1535 C  CB  . LEU   A 1 198 ? 44.958 4.417   -6.752  1.00 16.29 ? 720  LEU   A CB  1 
ATOM   1536 C  CG  . LEU   A 1 198 ? 44.255 4.237   -8.090  1.00 18.45 ? 720  LEU   A CG  1 
ATOM   1537 C  CD1 . LEU   A 1 198 ? 42.859 3.605   -7.896  1.00 17.21 ? 720  LEU   A CD1 1 
ATOM   1538 C  CD2 . LEU   A 1 198 ? 44.142 5.562   -8.826  1.00 19.49 ? 720  LEU   A CD2 1 
ATOM   1539 N  N   . ARG   A 1 199 ? 46.561 6.275   -4.752  1.00 24.90 ? 721  ARG   A N   1 
ATOM   1540 C  CA  . ARG   A 1 199 ? 47.153 6.555   -3.453  1.00 26.74 ? 721  ARG   A CA  1 
ATOM   1541 C  C   . ARG   A 1 199 ? 46.110 6.310   -2.378  1.00 25.14 ? 721  ARG   A C   1 
ATOM   1542 O  O   . ARG   A 1 199 ? 45.125 7.050   -2.288  1.00 24.72 ? 721  ARG   A O   1 
ATOM   1543 C  CB  . ARG   A 1 199 ? 47.680 7.986   -3.393  1.00 29.18 ? 721  ARG   A CB  1 
ATOM   1544 C  CG  . ARG   A 1 199 ? 48.899 8.242   -4.278  1.00 43.63 ? 721  ARG   A CG  1 
ATOM   1545 C  CD  . ARG   A 1 199 ? 50.002 7.208   -4.016  1.00 47.11 ? 721  ARG   A CD  1 
ATOM   1546 N  NE  . ARG   A 1 199 ? 51.321 7.655   -4.454  1.00 67.30 ? 721  ARG   A NE  1 
ATOM   1547 C  CZ  . ARG   A 1 199 ? 52.248 8.163   -3.650  1.00 56.86 ? 721  ARG   A CZ  1 
ATOM   1548 N  NH1 . ARG   A 1 199 ? 52.045 8.283   -2.348  1.00 52.56 ? 721  ARG   A NH1 1 
ATOM   1549 N  NH2 . ARG   A 1 199 ? 53.407 8.561   -4.166  1.00 59.50 ? 721  ARG   A NH2 1 
ATOM   1550 N  N   . ASN   A 1 200 ? 46.348 5.293   -1.551  1.00 26.98 ? 722  ASN   A N   1 
ATOM   1551 C  CA  . ASN   A 1 200 ? 45.489 4.919   -0.431  1.00 30.86 ? 722  ASN   A CA  1 
ATOM   1552 C  C   . ASN   A 1 200 ? 44.000 5.045   -0.798  1.00 24.76 ? 722  ASN   A C   1 
ATOM   1553 O  O   . ASN   A 1 200 ? 43.259 5.763   -0.125  1.00 27.28 ? 722  ASN   A O   1 
ATOM   1554 C  CB  . ASN   A 1 200 ? 45.811 5.763   0.795   1.00 27.22 ? 722  ASN   A CB  1 
ATOM   1555 C  CG  . ASN   A 1 200 ? 45.070 5.305   2.016   1.00 35.90 ? 722  ASN   A CG  1 
ATOM   1556 O  OD1 . ASN   A 1 200 ? 44.875 4.104   2.219   1.00 49.06 ? 722  ASN   A OD1 1 
ATOM   1557 N  ND2 . ASN   A 1 200 ? 44.617 6.256   2.825   1.00 39.25 ? 722  ASN   A ND2 1 
ATOM   1558 N  N   . PRO   A 1 201 ? 43.552 4.391   -1.861  1.00 23.63 ? 723  PRO   A N   1 
ATOM   1559 C  CA  . PRO   A 1 201 ? 42.190 4.666   -2.335  1.00 20.04 ? 723  PRO   A CA  1 
ATOM   1560 C  C   . PRO   A 1 201 ? 41.140 4.131   -1.381  1.00 21.20 ? 723  PRO   A C   1 
ATOM   1561 O  O   . PRO   A 1 201 ? 41.363 3.170   -0.645  1.00 21.70 ? 723  PRO   A O   1 
ATOM   1562 C  CB  . PRO   A 1 201 ? 42.128 3.958   -3.688  1.00 20.58 ? 723  PRO   A CB  1 
ATOM   1563 C  CG  . PRO   A 1 201 ? 43.159 2.831   -3.572  1.00 19.92 ? 723  PRO   A CG  1 
ATOM   1564 C  CD  . PRO   A 1 201 ? 44.247 3.412   -2.715  1.00 20.35 ? 723  PRO   A CD  1 
ATOM   1565 N  N   . GLN   A 1 202 ? 39.987 4.789   -1.386  1.00 21.64 ? 724  GLN   A N   1 
ATOM   1566 C  CA  . GLN   A 1 202 ? 38.794 4.202   -0.780  1.00 17.19 ? 724  GLN   A CA  1 
ATOM   1567 C  C   . GLN   A 1 202 ? 38.286 3.111   -1.702  1.00 17.88 ? 724  GLN   A C   1 
ATOM   1568 O  O   . GLN   A 1 202 ? 38.013 3.370   -2.880  1.00 17.93 ? 724  GLN   A O   1 
ATOM   1569 C  CB  . GLN   A 1 202 ? 37.710 5.250   -0.567  1.00 21.16 ? 724  GLN   A CB  1 
ATOM   1570 C  CG  . GLN   A 1 202 ? 36.438 4.637   -0.002  1.00 18.83 ? 724  GLN   A CG  1 
ATOM   1571 C  CD  . GLN   A 1 202 ? 35.424 5.672   0.379   1.00 25.64 ? 724  GLN   A CD  1 
ATOM   1572 O  OE1 . GLN   A 1 202 ? 35.022 5.756   1.540   1.00 26.48 ? 724  GLN   A OE1 1 
ATOM   1573 N  NE2 . GLN   A 1 202 ? 34.987 6.474   -0.596  1.00 21.27 ? 724  GLN   A NE2 1 
ATOM   1574 N  N   . ILE   A 1 203 ? 38.172 1.889   -1.183  1.00 17.56 ? 725  ILE   A N   1 
ATOM   1575 C  CA  . ILE   A 1 203 ? 37.728 0.753   -1.979  1.00 17.28 ? 725  ILE   A CA  1 
ATOM   1576 C  C   . ILE   A 1 203 ? 36.331 0.372   -1.500  1.00 17.95 ? 725  ILE   A C   1 
ATOM   1577 O  O   . ILE   A 1 203 ? 36.110 0.222   -0.295  1.00 21.96 ? 725  ILE   A O   1 
ATOM   1578 C  CB  . ILE   A 1 203 ? 38.716 -0.418  -1.862  1.00 22.92 ? 725  ILE   A CB  1 
ATOM   1579 C  CG1 . ILE   A 1 203 ? 40.040 -0.018  -2.510  1.00 22.62 ? 725  ILE   A CG1 1 
ATOM   1580 C  CG2 . ILE   A 1 203 ? 38.157 -1.621  -2.539  1.00 24.05 ? 725  ILE   A CG2 1 
ATOM   1581 C  CD1 . ILE   A 1 203 ? 41.042 -1.139  -2.611  1.00 32.81 ? 725  ILE   A CD1 1 
ATOM   1582 N  N   . THR   A 1 204 ? 35.376 0.305   -2.423  1.00 15.90 ? 726  THR   A N   1 
ATOM   1583 C  CA  . THR   A 1 204 ? 34.021 -0.126  -2.080  1.00 17.67 ? 726  THR   A CA  1 
ATOM   1584 C  C   . THR   A 1 204 ? 33.572 -1.210  -3.036  1.00 16.01 ? 726  THR   A C   1 
ATOM   1585 O  O   . THR   A 1 204 ? 33.898 -1.193  -4.232  1.00 15.70 ? 726  THR   A O   1 
ATOM   1586 C  CB  . THR   A 1 204 ? 32.975 1.011   -2.109  1.00 17.99 ? 726  THR   A CB  1 
ATOM   1587 O  OG1 . THR   A 1 204 ? 32.955 1.635   -3.404  1.00 17.16 ? 726  THR   A OG1 1 
ATOM   1588 C  CG2 . THR   A 1 204 ? 33.250 2.049   -1.015  1.00 20.31 ? 726  THR   A CG2 1 
ATOM   1589 N  N   A CYS   A 1 205 ? 32.815 -2.161  -2.498  0.55 16.08 ? 727  CYS   A N   1 
ATOM   1590 N  N   B CYS   A 1 205 ? 32.780 -2.133  -2.502  0.45 16.09 ? 727  CYS   A N   1 
ATOM   1591 C  CA  A CYS   A 1 205 ? 32.243 -3.244  -3.279  0.55 16.71 ? 727  CYS   A CA  1 
ATOM   1592 C  CA  B CYS   A 1 205 ? 32.230 -3.247  -3.257  0.45 16.73 ? 727  CYS   A CA  1 
ATOM   1593 C  C   A CYS   A 1 205 ? 30.764 -3.333  -2.936  0.55 15.52 ? 727  CYS   A C   1 
ATOM   1594 C  C   B CYS   A 1 205 ? 30.751 -3.335  -2.931  0.45 15.53 ? 727  CYS   A C   1 
ATOM   1595 O  O   A CYS   A 1 205 ? 30.419 -3.601  -1.784  0.55 15.56 ? 727  CYS   A O   1 
ATOM   1596 O  O   B CYS   A 1 205 ? 30.390 -3.621  -1.787  0.45 15.58 ? 727  CYS   A O   1 
ATOM   1597 C  CB  A CYS   A 1 205 ? 32.946 -4.557  -2.968  0.55 20.80 ? 727  CYS   A CB  1 
ATOM   1598 C  CB  B CYS   A 1 205 ? 32.932 -4.534  -2.877  0.45 20.79 ? 727  CYS   A CB  1 
ATOM   1599 S  SG  A CYS   A 1 205 ? 32.399 -5.831  -4.014  0.55 25.37 ? 727  CYS   A SG  1 
ATOM   1600 S  SG  B CYS   A 1 205 ? 34.569 -4.679  -3.572  0.45 20.76 ? 727  CYS   A SG  1 
ATOM   1601 N  N   . THR   A 1 206 ? 29.897 -3.073  -3.911  1.00 15.79 ? 728  THR   A N   1 
ATOM   1602 C  CA  . THR   A 1 206 ? 28.457 -2.994  -3.648  1.00 15.81 ? 728  THR   A CA  1 
ATOM   1603 C  C   . THR   A 1 206 ? 27.678 -3.477  -4.864  1.00 15.64 ? 728  THR   A C   1 
ATOM   1604 O  O   . THR   A 1 206 ? 28.252 -3.913  -5.867  1.00 17.79 ? 728  THR   A O   1 
ATOM   1605 C  CB  . THR   A 1 206 ? 28.030 -1.551  -3.305  1.00 18.10 ? 728  THR   A CB  1 
ATOM   1606 O  OG1 . THR   A 1 206 ? 28.350 -0.697  -4.403  1.00 16.77 ? 728  THR   A OG1 1 
ATOM   1607 C  CG2 . THR   A 1 206 ? 28.722 -0.986  -2.041  1.00 17.27 ? 728  THR   A CG2 1 
ATOM   1608 N  N   . GLY   A 1 207 ? 26.338 -3.400  -4.763  1.00 20.42 ? 729  GLY   A N   1 
ATOM   1609 C  CA  . GLY   A 1 207 ? 25.451 -3.761  -5.857  1.00 20.81 ? 729  GLY   A CA  1 
ATOM   1610 C  C   . GLY   A 1 207 ? 24.980 -5.211  -5.884  1.00 23.86 ? 729  GLY   A C   1 
ATOM   1611 O  O   . GLY   A 1 207 ? 24.392 -5.624  -6.885  1.00 29.25 ? 729  GLY   A O   1 
ATOM   1612 N  N   . PHE   A 1 208 ? 25.215 -5.985  -4.825  1.00 24.40 ? 730  PHE   A N   1 
ATOM   1613 C  CA  . PHE   A 1 208 ? 24.882 -7.412  -4.746  1.00 21.77 ? 730  PHE   A CA  1 
ATOM   1614 C  C   . PHE   A 1 208 ? 23.498 -7.660  -4.175  1.00 19.79 ? 730  PHE   A C   1 
ATOM   1615 O  O   . PHE   A 1 208 ? 23.045 -6.929  -3.294  1.00 18.90 ? 730  PHE   A O   1 
ATOM   1616 C  CB  . PHE   A 1 208 ? 25.872 -8.120  -3.832  1.00 19.20 ? 730  PHE   A CB  1 
ATOM   1617 C  CG  . PHE   A 1 208 ? 27.260 -7.859  -4.201  1.00 27.56 ? 730  PHE   A CG  1 
ATOM   1618 C  CD1 . PHE   A 1 208 ? 27.774 -8.423  -5.351  1.00 32.06 ? 730  PHE   A CD1 1 
ATOM   1619 C  CD2 . PHE   A 1 208 ? 28.034 -7.004  -3.445  1.00 27.03 ? 730  PHE   A CD2 1 
ATOM   1620 C  CE1 . PHE   A 1 208 ? 29.058 -8.186  -5.733  1.00 40.38 ? 730  PHE   A CE1 1 
ATOM   1621 C  CE2 . PHE   A 1 208 ? 29.316 -6.757  -3.818  1.00 29.93 ? 730  PHE   A CE2 1 
ATOM   1622 C  CZ  . PHE   A 1 208 ? 29.818 -7.357  -4.982  1.00 29.70 ? 730  PHE   A CZ  1 
ATOM   1623 N  N   . ASP   A 1 209 ? 22.864 -8.758  -4.620  1.00 16.98 ? 731  ASP   A N   1 
ATOM   1624 C  CA  . ASP   A 1 209 ? 21.717 -9.288  -3.877  1.00 18.86 ? 731  ASP   A CA  1 
ATOM   1625 C  C   . ASP   A 1 209 ? 22.035 -10.544 -3.058  1.00 20.16 ? 731  ASP   A C   1 
ATOM   1626 O  O   . ASP   A 1 209 ? 21.195 -10.952 -2.253  1.00 23.97 ? 731  ASP   A O   1 
ATOM   1627 C  CB  . ASP   A 1 209 ? 20.504 -9.542  -4.804  1.00 21.94 ? 731  ASP   A CB  1 
ATOM   1628 C  CG  . ASP   A 1 209 ? 20.800 -10.453 -5.980  1.00 29.26 ? 731  ASP   A CG  1 
ATOM   1629 O  OD1 . ASP   A 1 209 ? 21.974 -10.819 -6.210  1.00 26.64 ? 731  ASP   A OD1 1 
ATOM   1630 O  OD2 . ASP   A 1 209 ? 19.822 -10.810 -6.688  1.00 28.85 ? 731  ASP   A OD2 1 
ATOM   1631 N  N   . ARG   A 1 210 ? 23.240 -11.122 -3.187  1.00 17.10 ? 732  ARG   A N   1 
ATOM   1632 C  CA  . ARG   A 1 210 ? 23.706 -12.270 -2.402  1.00 18.10 ? 732  ARG   A CA  1 
ATOM   1633 C  C   . ARG   A 1 210 ? 22.656 -13.384 -2.296  1.00 16.92 ? 732  ARG   A C   1 
ATOM   1634 O  O   . ARG   A 1 210 ? 22.167 -13.674 -1.200  1.00 16.78 ? 732  ARG   A O   1 
ATOM   1635 C  CB  . ARG   A 1 210 ? 24.118 -11.840 -0.991  1.00 19.69 ? 732  ARG   A CB  1 
ATOM   1636 C  CG  . ARG   A 1 210 ? 25.275 -10.834 -0.905  1.00 19.75 ? 732  ARG   A CG  1 
ATOM   1637 C  CD  . ARG   A 1 210 ? 26.562 -11.283 -1.633  1.00 18.73 ? 732  ARG   A CD  1 
ATOM   1638 N  NE  . ARG   A 1 210 ? 27.084 -12.568 -1.175  1.00 20.88 ? 732  ARG   A NE  1 
ATOM   1639 C  CZ  . ARG   A 1 210 ? 27.788 -12.771 -0.065  1.00 22.41 ? 732  ARG   A CZ  1 
ATOM   1640 N  NH1 . ARG   A 1 210 ? 28.062 -11.792 0.788   1.00 14.75 ? 732  ARG   A NH1 1 
ATOM   1641 N  NH2 . ARG   A 1 210 ? 28.231 -13.996 0.202   1.00 24.37 ? 732  ARG   A NH2 1 
ATOM   1642 N  N   . PRO   A 1 211 ? 22.311 -14.031 -3.400  1.00 18.09 ? 733  PRO   A N   1 
ATOM   1643 C  CA  . PRO   A 1 211 ? 21.224 -15.028 -3.366  1.00 18.24 ? 733  PRO   A CA  1 
ATOM   1644 C  C   . PRO   A 1 211 ? 21.462 -16.189 -2.409  1.00 20.83 ? 733  PRO   A C   1 
ATOM   1645 O  O   . PRO   A 1 211 ? 20.490 -16.831 -1.998  1.00 21.24 ? 733  PRO   A O   1 
ATOM   1646 C  CB  . PRO   A 1 211 ? 21.151 -15.523 -4.810  1.00 20.45 ? 733  PRO   A CB  1 
ATOM   1647 C  CG  . PRO   A 1 211 ? 22.028 -14.680 -5.612  1.00 24.32 ? 733  PRO   A CG  1 
ATOM   1648 C  CD  . PRO   A 1 211 ? 22.940 -13.911 -4.728  1.00 20.85 ? 733  PRO   A CD  1 
ATOM   1649 N  N   . ASN   A 1 212 ? 22.710 -16.488 -2.035  1.00 15.84 ? 734  ASN   A N   1 
ATOM   1650 C  CA  . ASN   A 1 212 ? 22.976 -17.611 -1.149  1.00 18.91 ? 734  ASN   A CA  1 
ATOM   1651 C  C   . ASN   A 1 212 ? 22.900 -17.259 0.337   1.00 20.22 ? 734  ASN   A C   1 
ATOM   1652 O  O   . ASN   A 1 212 ? 23.296 -18.093 1.167   1.00 20.27 ? 734  ASN   A O   1 
ATOM   1653 C  CB  . ASN   A 1 212 ? 24.359 -18.213 -1.457  1.00 19.05 ? 734  ASN   A CB  1 
ATOM   1654 C  CG  . ASN   A 1 212 ? 25.508 -17.228 -1.219  1.00 19.68 ? 734  ASN   A CG  1 
ATOM   1655 O  OD1 . ASN   A 1 212 ? 25.402 -16.025 -1.503  1.00 21.79 ? 734  ASN   A OD1 1 
ATOM   1656 N  ND2 . ASN   A 1 212 ? 26.640 -17.754 -0.716  1.00 18.81 ? 734  ASN   A ND2 1 
ATOM   1657 N  N   . LEU   A 1 213 ? 22.423 -16.061 0.701   1.00 17.15 ? 735  LEU   A N   1 
ATOM   1658 C  CA  . LEU   A 1 213 ? 22.271 -15.671 2.107   1.00 14.08 ? 735  LEU   A CA  1 
ATOM   1659 C  C   . LEU   A 1 213 ? 20.791 -15.685 2.457   1.00 18.52 ? 735  LEU   A C   1 
ATOM   1660 O  O   . LEU   A 1 213 ? 20.038 -14.870 1.936   1.00 16.01 ? 735  LEU   A O   1 
ATOM   1661 C  CB  . LEU   A 1 213 ? 22.837 -14.282 2.381   1.00 17.53 ? 735  LEU   A CB  1 
ATOM   1662 C  CG  . LEU   A 1 213 ? 24.342 -14.113 2.127   1.00 16.66 ? 735  LEU   A CG  1 
ATOM   1663 C  CD1 . LEU   A 1 213 ? 24.771 -12.806 2.697   1.00 17.54 ? 735  LEU   A CD1 1 
ATOM   1664 C  CD2 . LEU   A 1 213 ? 25.095 -15.236 2.797   1.00 18.66 ? 735  LEU   A CD2 1 
ATOM   1665 N  N   . TYR   A 1 214 ? 20.388 -16.583 3.345   1.00 16.32 ? 736  TYR   A N   1 
ATOM   1666 C  CA  . TYR   A 1 214 ? 19.033 -16.597 3.882   1.00 19.52 ? 736  TYR   A CA  1 
ATOM   1667 C  C   . TYR   A 1 214 ? 18.988 -15.690 5.111   1.00 18.21 ? 736  TYR   A C   1 
ATOM   1668 O  O   . TYR   A 1 214 ? 19.841 -15.815 5.986   1.00 17.50 ? 736  TYR   A O   1 
ATOM   1669 C  CB  . TYR   A 1 214 ? 18.615 -18.031 4.254   1.00 16.01 ? 736  TYR   A CB  1 
ATOM   1670 C  CG  . TYR   A 1 214 ? 17.345 -18.044 5.088   1.00 16.74 ? 736  TYR   A CG  1 
ATOM   1671 C  CD1 . TYR   A 1 214 ? 16.110 -17.865 4.487   1.00 17.75 ? 736  TYR   A CD1 1 
ATOM   1672 C  CD2 . TYR   A 1 214 ? 17.384 -18.197 6.477   1.00 17.27 ? 736  TYR   A CD2 1 
ATOM   1673 C  CE1 . TYR   A 1 214 ? 14.928 -17.840 5.233   1.00 20.03 ? 736  TYR   A CE1 1 
ATOM   1674 C  CE2 . TYR   A 1 214 ? 16.204 -18.187 7.240   1.00 18.27 ? 736  TYR   A CE2 1 
ATOM   1675 C  CZ  . TYR   A 1 214 ? 14.981 -17.994 6.598   1.00 18.70 ? 736  TYR   A CZ  1 
ATOM   1676 O  OH  . TYR   A 1 214 ? 13.805 -17.961 7.324   1.00 19.71 ? 736  TYR   A OH  1 
ATOM   1677 N  N   . LEU   A 1 215 ? 17.982 -14.810 5.200   1.00 12.40 ? 737  LEU   A N   1 
ATOM   1678 C  CA  . LEU   A 1 215 ? 17.921 -13.772 6.228   1.00 14.55 ? 737  LEU   A CA  1 
ATOM   1679 C  C   . LEU   A 1 215 ? 16.756 -13.977 7.191   1.00 17.48 ? 737  LEU   A C   1 
ATOM   1680 O  O   . LEU   A 1 215 ? 15.618 -14.161 6.751   1.00 15.56 ? 737  LEU   A O   1 
ATOM   1681 C  CB  . LEU   A 1 215 ? 17.759 -12.398 5.572   1.00 15.67 ? 737  LEU   A CB  1 
ATOM   1682 C  CG  . LEU   A 1 215 ? 18.819 -12.049 4.530   1.00 18.68 ? 737  LEU   A CG  1 
ATOM   1683 C  CD1 . LEU   A 1 215 ? 18.500 -10.669 3.956   1.00 19.21 ? 737  LEU   A CD1 1 
ATOM   1684 C  CD2 . LEU   A 1 215 ? 20.197 -12.040 5.142   1.00 17.58 ? 737  LEU   A CD2 1 
ATOM   1685 N  N   . GLU   A 1 216 ? 17.010 -13.864 8.499   1.00 13.12 ? 738  GLU   A N   1 
ATOM   1686 C  CA  . GLU   A 1 216 ? 15.939 -14.094 9.470   1.00 14.07 ? 738  GLU   A CA  1 
ATOM   1687 C  C   . GLU   A 1 216 ? 16.147 -13.255 10.726  1.00 17.94 ? 738  GLU   A C   1 
ATOM   1688 O  O   . GLU   A 1 216 ? 17.286 -12.998 11.130  1.00 17.24 ? 738  GLU   A O   1 
ATOM   1689 C  CB  . GLU   A 1 216 ? 15.849 -15.594 9.843   1.00 16.05 ? 738  GLU   A CB  1 
ATOM   1690 C  CG  . GLU   A 1 216 ? 14.747 -15.878 10.868  1.00 18.40 ? 738  GLU   A CG  1 
ATOM   1691 C  CD  . GLU   A 1 216 ? 14.473 -17.360 10.998  1.00 26.16 ? 738  GLU   A CD  1 
ATOM   1692 O  OE1 . GLU   A 1 216 ? 14.244 -18.014 9.962   1.00 22.89 ? 738  GLU   A OE1 1 
ATOM   1693 O  OE2 . GLU   A 1 216 ? 14.503 -17.857 12.134  1.00 30.74 ? 738  GLU   A OE2 1 
ATOM   1694 N  N   . VAL   A 1 217 ? 15.049 -12.778 11.318  1.00 15.35 ? 739  VAL   A N   1 
ATOM   1695 C  CA  . VAL   A 1 217 ? 15.079 -12.014 12.562  1.00 12.17 ? 739  VAL   A CA  1 
ATOM   1696 C  C   . VAL   A 1 217 ? 14.176 -12.727 13.563  1.00 17.16 ? 739  VAL   A C   1 
ATOM   1697 O  O   . VAL   A 1 217 ? 13.026 -13.062 13.232  1.00 19.71 ? 739  VAL   A O   1 
ATOM   1698 C  CB  . VAL   A 1 217 ? 14.616 -10.555 12.351  1.00 17.76 ? 739  VAL   A CB  1 
ATOM   1699 C  CG1 . VAL   A 1 217 ? 14.582 -9.785  13.661  1.00 19.02 ? 739  VAL   A CG1 1 
ATOM   1700 C  CG2 . VAL   A 1 217 ? 15.512 -9.832  11.357  1.00 17.67 ? 739  VAL   A CG2 1 
ATOM   1701 N  N   . ARG   A 1 218 ? 14.698 -12.964 14.775  1.00 16.71 ? 740  ARG   A N   1 
ATOM   1702 C  CA  . ARG   A 1 218 ? 13.990 -13.662 15.848  1.00 22.45 ? 740  ARG   A CA  1 
ATOM   1703 C  C   . ARG   A 1 218 ? 14.131 -12.854 17.129  1.00 25.46 ? 740  ARG   A C   1 
ATOM   1704 O  O   . ARG   A 1 218 ? 15.180 -12.251 17.374  1.00 19.16 ? 740  ARG   A O   1 
ATOM   1705 C  CB  . ARG   A 1 218 ? 14.569 -15.105 16.111  1.00 26.20 ? 740  ARG   A CB  1 
ATOM   1706 C  CG  . ARG   A 1 218 ? 14.762 -15.990 14.880  1.00 30.89 ? 740  ARG   A CG  1 
ATOM   1707 C  CD  . ARG   A 1 218 ? 15.422 -17.380 15.201  1.00 26.64 ? 740  ARG   A CD  1 
ATOM   1708 N  NE  . ARG   A 1 218 ? 14.585 -18.230 16.041  1.00 41.36 ? 740  ARG   A NE  1 
ATOM   1709 C  CZ  . ARG   A 1 218 ? 13.477 -18.841 15.625  1.00 52.69 ? 740  ARG   A CZ  1 
ATOM   1710 N  NH1 . ARG   A 1 218 ? 13.053 -18.738 14.373  1.00 42.90 ? 740  ARG   A NH1 1 
ATOM   1711 N  NH2 . ARG   A 1 218 ? 12.767 -19.561 16.491  1.00 40.99 ? 740  ARG   A NH2 1 
ATOM   1712 N  N   . ARG   A 1 219 ? 13.094 -12.870 17.968  1.00 21.96 ? 741  ARG   A N   1 
ATOM   1713 C  CA  . ARG   A 1 219 ? 13.178 -12.203 19.266  1.00 21.18 ? 741  ARG   A CA  1 
ATOM   1714 C  C   . ARG   A 1 219 ? 13.937 -13.063 20.267  1.00 20.25 ? 741  ARG   A C   1 
ATOM   1715 O  O   . ARG   A 1 219 ? 13.838 -14.289 20.259  1.00 23.08 ? 741  ARG   A O   1 
ATOM   1716 C  CB  . ARG   A 1 219 ? 11.780 -11.892 19.810  1.00 22.00 ? 741  ARG   A CB  1 
ATOM   1717 C  CG  . ARG   A 1 219 ? 11.093 -10.730 19.086  1.00 23.06 ? 741  ARG   A CG  1 
ATOM   1718 C  CD  . ARG   A 1 219 ? 11.696 -9.373  19.527  1.00 26.40 ? 741  ARG   A CD  1 
ATOM   1719 N  NE  . ARG   A 1 219 ? 11.439 -9.155  20.944  1.00 29.61 ? 741  ARG   A NE  1 
ATOM   1720 C  CZ  . ARG   A 1 219 ? 10.364 -8.536  21.415  1.00 36.69 ? 741  ARG   A CZ  1 
ATOM   1721 N  NH1 . ARG   A 1 219 ? 9.467  -7.998  20.606  1.00 31.22 ? 741  ARG   A NH1 1 
ATOM   1722 N  NH2 . ARG   A 1 219 ? 10.186 -8.451  22.731  1.00 36.74 ? 741  ARG   A NH2 1 
ATOM   1723 N  N   . LYS   A 1 220 ? 14.699 -12.409 21.134  1.00 22.57 ? 742  LYS   A N   1 
ATOM   1724 C  CA  . LYS   A 1 220 ? 15.426 -13.096 22.195  1.00 19.76 ? 742  LYS   A CA  1 
ATOM   1725 C  C   . LYS   A 1 220 ? 14.466 -13.647 23.234  1.00 28.08 ? 742  LYS   A C   1 
ATOM   1726 O  O   . LYS   A 1 220 ? 13.406 -13.072 23.482  1.00 27.72 ? 742  LYS   A O   1 
ATOM   1727 C  CB  . LYS   A 1 220 ? 16.373 -12.132 22.904  1.00 22.56 ? 742  LYS   A CB  1 
ATOM   1728 C  CG  . LYS   A 1 220 ? 17.613 -11.767 22.163  1.00 19.18 ? 742  LYS   A CG  1 
ATOM   1729 C  CD  . LYS   A 1 220 ? 18.206 -10.547 22.856  1.00 23.96 ? 742  LYS   A CD  1 
ATOM   1730 C  CE  . LYS   A 1 220 ? 19.656 -10.348 22.528  1.00 22.83 ? 742  LYS   A CE  1 
ATOM   1731 N  NZ  . LYS   A 1 220 ? 20.163 -9.116  23.207  1.00 23.19 ? 742  LYS   A NZ  1 
ATOM   1732 N  N   . THR   A 1 221 ? 14.857 -14.761 23.864  1.00 24.74 ? 743  THR   A N   1 
ATOM   1733 C  CA  . THR   A 1 221 ? 14.137 -15.264 25.028  1.00 26.53 ? 743  THR   A CA  1 
ATOM   1734 C  C   . THR   A 1 221 ? 14.705 -14.720 26.324  1.00 30.65 ? 743  THR   A C   1 
ATOM   1735 O  O   . THR   A 1 221 ? 14.042 -14.805 27.360  1.00 39.00 ? 743  THR   A O   1 
ATOM   1736 C  CB  . THR   A 1 221 ? 14.182 -16.794 25.115  1.00 30.29 ? 743  THR   A CB  1 
ATOM   1737 O  OG1 . THR   A 1 221 ? 15.518 -17.215 25.434  1.00 29.80 ? 743  THR   A OG1 1 
ATOM   1738 C  CG2 . THR   A 1 221 ? 13.735 -17.442 23.812  1.00 34.58 ? 743  THR   A CG2 1 
ATOM   1739 N  N   . GLY   A 1 222 ? 15.905 -14.160 26.291  1.00 32.28 ? 744  GLY   A N   1 
ATOM   1740 C  CA  . GLY   A 1 222 ? 16.610 -13.777 27.493  1.00 32.46 ? 744  GLY   A CA  1 
ATOM   1741 C  C   . GLY   A 1 222 ? 17.558 -14.832 28.035  1.00 35.12 ? 744  GLY   A C   1 
ATOM   1742 O  O   . GLY   A 1 222 ? 18.319 -14.541 28.960  1.00 38.80 ? 744  GLY   A O   1 
ATOM   1743 N  N   . ASN   A 1 223 ? 17.525 -16.048 27.514  1.00 32.88 ? 745  ASN   A N   1 
ATOM   1744 C  CA  . ASN   A 1 223 ? 18.425 -17.105 27.956  1.00 25.81 ? 745  ASN   A CA  1 
ATOM   1745 C  C   . ASN   A 1 223 ? 19.369 -17.436 26.807  1.00 27.46 ? 745  ASN   A C   1 
ATOM   1746 O  O   . ASN   A 1 223 ? 18.921 -17.884 25.744  1.00 24.50 ? 745  ASN   A O   1 
ATOM   1747 C  CB  . ASN   A 1 223 ? 17.663 -18.355 28.392  1.00 32.84 ? 745  ASN   A CB  1 
ATOM   1748 C  CG  . ASN   A 1 223 ? 18.601 -19.442 28.877  1.00 40.99 ? 745  ASN   A CG  1 
ATOM   1749 O  OD1 . ASN   A 1 223 ? 19.246 -20.123 28.076  1.00 31.44 ? 745  ASN   A OD1 1 
ATOM   1750 N  ND2 . ASN   A 1 223 ? 18.707 -19.588 30.197  1.00 41.51 ? 745  ASN   A ND2 1 
ATOM   1751 N  N   . ILE   A 1 224 ? 20.670 -17.211 27.023  1.00 27.89 ? 746  ILE   A N   1 
ATOM   1752 C  CA  . ILE   A 1 224 ? 21.636 -17.287 25.926  1.00 22.61 ? 746  ILE   A CA  1 
ATOM   1753 C  C   . ILE   A 1 224 ? 21.616 -18.666 25.284  1.00 24.54 ? 746  ILE   A C   1 
ATOM   1754 O  O   . ILE   A 1 224 ? 21.497 -18.794 24.060  1.00 21.06 ? 746  ILE   A O   1 
ATOM   1755 C  CB  . ILE   A 1 224 ? 23.044 -16.894 26.417  1.00 23.97 ? 746  ILE   A CB  1 
ATOM   1756 C  CG1 . ILE   A 1 224 ? 23.042 -15.402 26.761  1.00 29.18 ? 746  ILE   A CG1 1 
ATOM   1757 C  CG2 . ILE   A 1 224 ? 24.088 -17.153 25.350  1.00 21.25 ? 746  ILE   A CG2 1 
ATOM   1758 C  CD1 . ILE   A 1 224 ? 24.341 -14.891 27.400  1.00 30.15 ? 746  ILE   A CD1 1 
ATOM   1759 N  N   . LEU   A 1 225 ? 21.713 -19.732 26.093  1.00 22.90 ? 747  LEU   A N   1 
ATOM   1760 C  CA  . LEU   A 1 225 ? 21.769 -21.056 25.494  1.00 24.56 ? 747  LEU   A CA  1 
ATOM   1761 C  C   . LEU   A 1 225 ? 20.437 -21.428 24.862  1.00 26.90 ? 747  LEU   A C   1 
ATOM   1762 O  O   . LEU   A 1 225 ? 20.402 -22.063 23.807  1.00 22.70 ? 747  LEU   A O   1 
ATOM   1763 C  CB  . LEU   A 1 225 ? 22.202 -22.105 26.530  1.00 23.80 ? 747  LEU   A CB  1 
ATOM   1764 C  CG  . LEU   A 1 225 ? 23.688 -21.902 26.823  1.00 28.39 ? 747  LEU   A CG  1 
ATOM   1765 C  CD1 . LEU   A 1 225 ? 24.226 -22.915 27.826  1.00 27.99 ? 747  LEU   A CD1 1 
ATOM   1766 C  CD2 . LEU   A 1 225 ? 24.441 -22.013 25.505  1.00 28.23 ? 747  LEU   A CD2 1 
ATOM   1767 N  N   . GLN   A 1 226 ? 19.326 -21.035 25.480  1.00 27.28 ? 748  GLN   A N   1 
ATOM   1768 C  CA  . GLN   A 1 226 ? 18.039 -21.266 24.834  1.00 24.83 ? 748  GLN   A CA  1 
ATOM   1769 C  C   . GLN   A 1 226 ? 17.979 -20.554 23.486  1.00 21.81 ? 748  GLN   A C   1 
ATOM   1770 O  O   . GLN   A 1 226 ? 17.493 -21.116 22.501  1.00 23.78 ? 748  GLN   A O   1 
ATOM   1771 C  CB  . GLN   A 1 226 ? 16.918 -20.796 25.756  1.00 30.07 ? 748  GLN   A CB  1 
ATOM   1772 C  CG  . GLN   A 1 226 ? 15.517 -21.007 25.218  1.00 42.75 ? 748  GLN   A CG  1 
ATOM   1773 C  CD  . GLN   A 1 226 ? 14.465 -20.502 26.188  1.00 50.48 ? 748  GLN   A CD  1 
ATOM   1774 O  OE1 . GLN   A 1 226 ? 14.744 -20.314 27.375  1.00 53.83 ? 748  GLN   A OE1 1 
ATOM   1775 N  NE2 . GLN   A 1 226 ? 13.253 -20.264 25.687  1.00 52.80 ? 748  GLN   A NE2 1 
ATOM   1776 N  N   . ASP   A 1 227 ? 18.551 -19.346 23.408  1.00 19.98 ? 749  ASP   A N   1 
ATOM   1777 C  CA  . ASP   A 1 227 ? 18.533 -18.576 22.164  1.00 22.99 ? 749  ASP   A CA  1 
ATOM   1778 C  C   . ASP   A 1 227 ? 19.413 -19.219 21.097  1.00 19.57 ? 749  ASP   A C   1 
ATOM   1779 O  O   . ASP   A 1 227 ? 19.089 -19.170 19.904  1.00 20.87 ? 749  ASP   A O   1 
ATOM   1780 C  CB  . ASP   A 1 227 ? 19.030 -17.139 22.414  1.00 22.39 ? 749  ASP   A CB  1 
ATOM   1781 C  CG  . ASP   A 1 227 ? 18.025 -16.275 23.148  1.00 27.97 ? 749  ASP   A CG  1 
ATOM   1782 O  OD1 . ASP   A 1 227 ? 16.820 -16.595 23.120  1.00 29.11 ? 749  ASP   A OD1 1 
ATOM   1783 O  OD2 . ASP   A 1 227 ? 18.443 -15.253 23.733  1.00 28.30 ? 749  ASP   A OD2 1 
ATOM   1784 N  N   . LEU   A 1 228 ? 20.553 -19.794 21.498  1.00 21.04 ? 750  LEU   A N   1 
ATOM   1785 C  CA  . LEU   A 1 228 ? 21.537 -20.259 20.527  1.00 25.44 ? 750  LEU   A CA  1 
ATOM   1786 C  C   . LEU   A 1 228 ? 21.435 -21.745 20.207  1.00 25.51 ? 750  LEU   A C   1 
ATOM   1787 O  O   . LEU   A 1 228 ? 21.947 -22.172 19.168  1.00 22.98 ? 750  LEU   A O   1 
ATOM   1788 C  CB  . LEU   A 1 228 ? 22.959 -19.950 21.015  1.00 20.22 ? 750  LEU   A CB  1 
ATOM   1789 C  CG  . LEU   A 1 228 ? 23.194 -18.448 21.136  1.00 21.92 ? 750  LEU   A CG  1 
ATOM   1790 C  CD1 . LEU   A 1 228 ? 24.550 -18.189 21.757  1.00 22.12 ? 750  LEU   A CD1 1 
ATOM   1791 C  CD2 . LEU   A 1 228 ? 23.076 -17.810 19.741  1.00 18.76 ? 750  LEU   A CD2 1 
ATOM   1792 N  N   . GLN   A 1 229 ? 20.768 -22.534 21.040  1.00 23.12 ? 751  GLN   A N   1 
ATOM   1793 C  CA  . GLN   A 1 229 ? 20.711 -23.972 20.786  1.00 29.03 ? 751  GLN   A CA  1 
ATOM   1794 C  C   . GLN   A 1 229 ? 20.142 -24.339 19.426  1.00 27.18 ? 751  GLN   A C   1 
ATOM   1795 O  O   . GLN   A 1 229 ? 20.644 -25.307 18.825  1.00 29.32 ? 751  GLN   A O   1 
ATOM   1796 C  CB  . GLN   A 1 229 ? 19.935 -24.659 21.911  1.00 36.86 ? 751  GLN   A CB  1 
ATOM   1797 C  CG  . GLN   A 1 229 ? 20.870 -25.417 22.842  1.00 49.53 ? 751  GLN   A CG  1 
ATOM   1798 C  CD  . GLN   A 1 229 ? 20.292 -25.608 24.227  1.00 57.26 ? 751  GLN   A CD  1 
ATOM   1799 O  OE1 . GLN   A 1 229 ? 19.074 -25.701 24.394  1.00 52.48 ? 751  GLN   A OE1 1 
ATOM   1800 N  NE2 . GLN   A 1 229 ? 21.164 -25.657 25.234  1.00 44.97 ? 751  GLN   A NE2 1 
ATOM   1801 N  N   . PRO   A 1 230 ? 19.149 -23.641 18.871  1.00 31.60 ? 752  PRO   A N   1 
ATOM   1802 C  CA  . PRO   A 1 230 ? 18.730 -23.961 17.499  1.00 26.54 ? 752  PRO   A CA  1 
ATOM   1803 C  C   . PRO   A 1 230 ? 19.861 -23.949 16.486  1.00 27.39 ? 752  PRO   A C   1 
ATOM   1804 O  O   . PRO   A 1 230 ? 19.749 -24.622 15.454  1.00 32.81 ? 752  PRO   A O   1 
ATOM   1805 C  CB  . PRO   A 1 230 ? 17.693 -22.872 17.197  1.00 31.37 ? 752  PRO   A CB  1 
ATOM   1806 C  CG  . PRO   A 1 230 ? 17.133 -22.539 18.535  1.00 29.14 ? 752  PRO   A CG  1 
ATOM   1807 C  CD  . PRO   A 1 230 ? 18.307 -22.567 19.443  1.00 25.76 ? 752  PRO   A CD  1 
ATOM   1808 N  N   . PHE   A 1 231 ? 20.949 -23.223 16.726  1.00 23.61 ? 753  PHE   A N   1 
ATOM   1809 C  CA  . PHE   A 1 231 ? 22.055 -23.186 15.784  1.00 25.05 ? 753  PHE   A CA  1 
ATOM   1810 C  C   . PHE   A 1 231 ? 23.065 -24.300 16.014  1.00 32.62 ? 753  PHE   A C   1 
ATOM   1811 O  O   . PHE   A 1 231 ? 24.092 -24.340 15.320  1.00 35.69 ? 753  PHE   A O   1 
ATOM   1812 C  CB  . PHE   A 1 231 ? 22.772 -21.847 15.860  1.00 27.28 ? 753  PHE   A CB  1 
ATOM   1813 C  CG  . PHE   A 1 231 ? 21.868 -20.693 15.585  1.00 27.30 ? 753  PHE   A CG  1 
ATOM   1814 C  CD1 . PHE   A 1 231 ? 21.669 -20.262 14.297  1.00 24.11 ? 753  PHE   A CD1 1 
ATOM   1815 C  CD2 . PHE   A 1 231 ? 21.176 -20.084 16.614  1.00 23.27 ? 753  PHE   A CD2 1 
ATOM   1816 C  CE1 . PHE   A 1 231 ? 20.803 -19.215 14.040  1.00 23.93 ? 753  PHE   A CE1 1 
ATOM   1817 C  CE2 . PHE   A 1 231 ? 20.321 -19.047 16.362  1.00 21.98 ? 753  PHE   A CE2 1 
ATOM   1818 C  CZ  . PHE   A 1 231 ? 20.130 -18.621 15.076  1.00 18.20 ? 753  PHE   A CZ  1 
ATOM   1819 N  N   . LEU   A 1 232 ? 22.816 -25.169 16.980  1.00 25.24 ? 754  LEU   A N   1 
ATOM   1820 C  CA  . LEU   A 1 232 ? 23.754 -26.216 17.355  1.00 25.50 ? 754  LEU   A CA  1 
ATOM   1821 C  C   . LEU   A 1 232 ? 23.201 -27.568 16.943  1.00 26.39 ? 754  LEU   A C   1 
ATOM   1822 O  O   . LEU   A 1 232 ? 21.995 -27.744 16.756  1.00 31.44 ? 754  LEU   A O   1 
ATOM   1823 C  CB  . LEU   A 1 232 ? 24.027 -26.207 18.864  1.00 27.47 ? 754  LEU   A CB  1 
ATOM   1824 C  CG  . LEU   A 1 232 ? 24.480 -24.850 19.394  1.00 29.34 ? 754  LEU   A CG  1 
ATOM   1825 C  CD1 . LEU   A 1 232 ? 24.700 -24.881 20.905  1.00 35.22 ? 754  LEU   A CD1 1 
ATOM   1826 C  CD2 . LEU   A 1 232 ? 25.759 -24.475 18.655  1.00 28.64 ? 754  LEU   A CD2 1 
ATOM   1827 N  N   . VAL   A 1 233 ? 24.100 -28.525 16.789  1.00 25.76 ? 755  VAL   A N   1 
ATOM   1828 C  CA  . VAL   A 1 233 ? 23.723 -29.915 16.581  1.00 32.17 ? 755  VAL   A CA  1 
ATOM   1829 C  C   . VAL   A 1 233 ? 24.332 -30.737 17.707  1.00 37.27 ? 755  VAL   A C   1 
ATOM   1830 O  O   . VAL   A 1 233 ? 25.481 -30.507 18.102  1.00 32.22 ? 755  VAL   A O   1 
ATOM   1831 C  CB  . VAL   A 1 233 ? 24.167 -30.416 15.192  1.00 33.59 ? 755  VAL   A CB  1 
ATOM   1832 C  CG1 . VAL   A 1 233 ? 25.592 -30.022 14.914  1.00 40.31 ? 755  VAL   A CG1 1 
ATOM   1833 C  CG2 . VAL   A 1 233 ? 24.005 -31.917 15.086  1.00 43.11 ? 755  VAL   A CG2 1 
ATOM   1834 N  N   . LYS   A 1 234 ? 23.548 -31.666 18.254  1.00 45.56 ? 756  LYS   A N   1 
ATOM   1835 C  CA  . LYS   A 1 234 ? 23.984 -32.492 19.374  1.00 55.75 ? 756  LYS   A CA  1 
ATOM   1836 C  C   . LYS   A 1 234 ? 24.293 -33.920 18.920  1.00 59.39 ? 756  LYS   A C   1 
ATOM   1837 O  O   . LYS   A 1 234 ? 23.845 -34.373 17.861  1.00 55.85 ? 756  LYS   A O   1 
ATOM   1838 C  CB  . LYS   A 1 234 ? 22.927 -32.498 20.485  1.00 52.86 ? 756  LYS   A CB  1 
ATOM   1839 C  CG  . LYS   A 1 234 ? 23.460 -32.810 21.878  1.00 50.81 ? 756  LYS   A CG  1 
ATOM   1840 C  CD  . LYS   A 1 234 ? 22.304 -32.891 22.859  1.00 65.09 ? 756  LYS   A CD  1 
ATOM   1841 C  CE  . LYS   A 1 234 ? 22.738 -33.327 24.252  1.00 66.04 ? 756  LYS   A CE  1 
ATOM   1842 N  NZ  . LYS   A 1 234 ? 21.579 -33.338 25.195  1.00 63.31 ? 756  LYS   A NZ  1 
ATOM   1843 N  N   . THR   A 1 235 ? 25.072 -34.616 19.751  1.00 64.79 ? 757  THR   A N   1 
ATOM   1844 C  CA  . THR   A 1 235 ? 25.569 -35.979 19.512  1.00 66.63 ? 757  THR   A CA  1 
ATOM   1845 C  C   . THR   A 1 235 ? 26.472 -36.064 18.286  1.00 62.83 ? 757  THR   A C   1 
ATOM   1846 O  O   . THR   A 1 235 ? 27.700 -36.085 18.420  1.00 58.46 ? 757  THR   A O   1 
ATOM   1847 C  CB  . THR   A 1 235 ? 24.421 -36.987 19.363  1.00 65.06 ? 757  THR   A CB  1 
ATOM   1848 O  OG1 . THR   A 1 235 ? 23.652 -36.998 20.568  1.00 75.59 ? 757  THR   A OG1 1 
ATOM   1849 C  CG2 . THR   A 1 235 ? 24.966 -38.389 19.113  1.00 77.06 ? 757  THR   A CG2 1 
ATOM   1850 N  N   . HIS   A 1 238 ? 28.032 -35.071 21.952  1.00 50.47 ? 760  HIS   A N   1 
ATOM   1851 C  CA  . HIS   A 1 238 ? 28.557 -33.717 22.172  1.00 49.12 ? 760  HIS   A CA  1 
ATOM   1852 C  C   . HIS   A 1 238 ? 27.911 -32.689 21.232  1.00 46.20 ? 760  HIS   A C   1 
ATOM   1853 O  O   . HIS   A 1 238 ? 27.266 -33.049 20.252  1.00 50.83 ? 760  HIS   A O   1 
ATOM   1854 C  CB  . HIS   A 1 238 ? 30.075 -33.689 21.991  1.00 44.65 ? 760  HIS   A CB  1 
ATOM   1855 C  CG  . HIS   A 1 238 ? 30.509 -33.551 20.564  1.00 56.14 ? 760  HIS   A CG  1 
ATOM   1856 N  ND1 . HIS   A 1 238 ? 31.613 -32.814 20.192  1.00 60.42 ? 760  HIS   A ND1 1 
ATOM   1857 C  CD2 . HIS   A 1 238 ? 29.993 -34.058 19.418  1.00 57.20 ? 760  HIS   A CD2 1 
ATOM   1858 C  CE1 . HIS   A 1 238 ? 31.754 -32.865 18.879  1.00 57.39 ? 760  HIS   A CE1 1 
ATOM   1859 N  NE2 . HIS   A 1 238 ? 30.782 -33.611 18.385  1.00 57.00 ? 760  HIS   A NE2 1 
ATOM   1860 N  N   . TRP   A 1 239 ? 28.104 -31.408 21.509  1.00 37.47 ? 761  TRP   A N   1 
ATOM   1861 C  CA  . TRP   A 1 239 ? 27.508 -30.369 20.685  1.00 37.81 ? 761  TRP   A CA  1 
ATOM   1862 C  C   . TRP   A 1 239 ? 28.530 -29.803 19.710  1.00 38.29 ? 761  TRP   A C   1 
ATOM   1863 O  O   . TRP   A 1 239 ? 29.735 -29.832 19.967  1.00 38.34 ? 761  TRP   A O   1 
ATOM   1864 C  CB  . TRP   A 1 239 ? 26.969 -29.232 21.540  1.00 35.66 ? 761  TRP   A CB  1 
ATOM   1865 C  CG  . TRP   A 1 239 ? 25.983 -29.600 22.601  1.00 42.97 ? 761  TRP   A CG  1 
ATOM   1866 C  CD1 . TRP   A 1 239 ? 26.262 -30.121 23.831  1.00 45.43 ? 761  TRP   A CD1 1 
ATOM   1867 C  CD2 . TRP   A 1 239 ? 24.563 -29.410 22.559  1.00 47.10 ? 761  TRP   A CD2 1 
ATOM   1868 N  NE1 . TRP   A 1 239 ? 25.103 -30.291 24.546  1.00 52.77 ? 761  TRP   A NE1 1 
ATOM   1869 C  CE2 . TRP   A 1 239 ? 24.046 -29.857 23.788  1.00 50.27 ? 761  TRP   A CE2 1 
ATOM   1870 C  CE3 . TRP   A 1 239 ? 23.677 -28.914 21.596  1.00 55.13 ? 761  TRP   A CE3 1 
ATOM   1871 C  CZ2 . TRP   A 1 239 ? 22.686 -29.820 24.084  1.00 59.07 ? 761  TRP   A CZ2 1 
ATOM   1872 C  CZ3 . TRP   A 1 239 ? 22.323 -28.879 21.891  1.00 55.48 ? 761  TRP   A CZ3 1 
ATOM   1873 C  CH2 . TRP   A 1 239 ? 21.842 -29.333 23.122  1.00 61.30 ? 761  TRP   A CH2 1 
ATOM   1874 N  N   . GLU   A 1 240 ? 28.036 -29.275 18.589  1.00 30.40 ? 762  GLU   A N   1 
ATOM   1875 C  CA  . GLU   A 1 240 ? 28.865 -28.459 17.712  1.00 32.84 ? 762  GLU   A CA  1 
ATOM   1876 C  C   . GLU   A 1 240 ? 27.974 -27.507 16.931  1.00 29.94 ? 762  GLU   A C   1 
ATOM   1877 O  O   . GLU   A 1 240 ? 26.748 -27.633 16.923  1.00 26.21 ? 762  GLU   A O   1 
ATOM   1878 C  CB  . GLU   A 1 240 ? 29.723 -29.318 16.775  1.00 40.81 ? 762  GLU   A CB  1 
ATOM   1879 C  CG  . GLU   A 1 240 ? 29.031 -29.819 15.528  1.00 43.36 ? 762  GLU   A CG  1 
ATOM   1880 C  CD  . GLU   A 1 240 ? 30.006 -30.009 14.355  1.00 62.53 ? 762  GLU   A CD  1 
ATOM   1881 O  OE1 . GLU   A 1 240 ? 31.085 -30.619 14.553  1.00 54.63 ? 762  GLU   A OE1 1 
ATOM   1882 O  OE2 . GLU   A 1 240 ? 29.700 -29.531 13.235  1.00 62.53 ? 762  GLU   A OE2 1 
ATOM   1883 N  N   . PHE   A 1 241 ? 28.602 -26.532 16.280  1.00 30.39 ? 763  PHE   A N   1 
ATOM   1884 C  CA  . PHE   A 1 241 ? 27.837 -25.677 15.391  1.00 25.68 ? 763  PHE   A CA  1 
ATOM   1885 C  C   . PHE   A 1 241 ? 27.570 -26.399 14.074  1.00 26.26 ? 763  PHE   A C   1 
ATOM   1886 O  O   . PHE   A 1 241 ? 28.285 -27.322 13.697  1.00 25.61 ? 763  PHE   A O   1 
ATOM   1887 C  CB  . PHE   A 1 241 ? 28.572 -24.359 15.126  1.00 30.49 ? 763  PHE   A CB  1 
ATOM   1888 C  CG  . PHE   A 1 241 ? 28.351 -23.322 16.190  1.00 33.73 ? 763  PHE   A CG  1 
ATOM   1889 C  CD1 . PHE   A 1 241 ? 27.222 -22.528 16.169  1.00 36.38 ? 763  PHE   A CD1 1 
ATOM   1890 C  CD2 . PHE   A 1 241 ? 29.264 -23.163 17.216  1.00 29.41 ? 763  PHE   A CD2 1 
ATOM   1891 C  CE1 . PHE   A 1 241 ? 27.006 -21.586 17.154  1.00 34.63 ? 763  PHE   A CE1 1 
ATOM   1892 C  CE2 . PHE   A 1 241 ? 29.047 -22.230 18.202  1.00 25.43 ? 763  PHE   A CE2 1 
ATOM   1893 C  CZ  . PHE   A 1 241 ? 27.924 -21.441 18.161  1.00 24.98 ? 763  PHE   A CZ  1 
ATOM   1894 N  N   . GLU   A 1 242 ? 26.527 -25.954 13.363  1.00 24.92 ? 764  GLU   A N   1 
ATOM   1895 C  CA  . GLU   A 1 242 ? 26.211 -26.536 12.060  1.00 26.50 ? 764  GLU   A CA  1 
ATOM   1896 C  C   . GLU   A 1 242 ? 27.333 -26.332 11.050  1.00 30.78 ? 764  GLU   A C   1 
ATOM   1897 O  O   . GLU   A 1 242 ? 27.484 -27.129 10.121  1.00 30.84 ? 764  GLU   A O   1 
ATOM   1898 C  CB  . GLU   A 1 242 ? 24.917 -25.928 11.520  1.00 32.65 ? 764  GLU   A CB  1 
ATOM   1899 C  CG  . GLU   A 1 242 ? 23.679 -26.725 11.832  1.00 42.08 ? 764  GLU   A CG  1 
ATOM   1900 C  CD  . GLU   A 1 242 ? 23.286 -27.620 10.683  1.00 62.41 ? 764  GLU   A CD  1 
ATOM   1901 O  OE1 . GLU   A 1 242 ? 23.609 -27.255 9.528   1.00 62.12 ? 764  GLU   A OE1 1 
ATOM   1902 O  OE2 . GLU   A 1 242 ? 22.661 -28.680 10.931  1.00 70.67 ? 764  GLU   A OE2 1 
ATOM   1903 N  N   . GLY   A 1 243 ? 28.096 -25.255 11.186  1.00 24.67 ? 765  GLY   A N   1 
ATOM   1904 C  CA  . GLY   A 1 243 ? 29.160 -24.920 10.267  1.00 18.06 ? 765  GLY   A CA  1 
ATOM   1905 C  C   . GLY   A 1 243 ? 29.898 -23.751 10.888  1.00 17.29 ? 765  GLY   A C   1 
ATOM   1906 O  O   . GLY   A 1 243 ? 29.526 -23.291 11.972  1.00 22.48 ? 765  GLY   A O   1 
ATOM   1907 N  N   . PRO   A 1 244 ? 30.936 -23.233 10.235  1.00 19.85 ? 766  PRO   A N   1 
ATOM   1908 C  CA  . PRO   A 1 244 ? 31.661 -22.096 10.816  1.00 18.03 ? 766  PRO   A CA  1 
ATOM   1909 C  C   . PRO   A 1 244 ? 30.740 -20.898 11.031  1.00 15.98 ? 766  PRO   A C   1 
ATOM   1910 O  O   . PRO   A 1 244 ? 29.941 -20.545 10.162  1.00 18.40 ? 766  PRO   A O   1 
ATOM   1911 C  CB  . PRO   A 1 244 ? 32.746 -21.798 9.777   1.00 18.07 ? 766  PRO   A CB  1 
ATOM   1912 C  CG  . PRO   A 1 244 ? 32.978 -23.180 9.110   1.00 19.32 ? 766  PRO   A CG  1 
ATOM   1913 C  CD  . PRO   A 1 244 ? 31.584 -23.738 9.010   1.00 23.24 ? 766  PRO   A CD  1 
ATOM   1914 N  N   . THR   A 1 245 ? 30.867 -20.271 12.194  1.00 18.17 ? 767  THR   A N   1 
ATOM   1915 C  CA  . THR   A 1 245 ? 29.870 -19.295 12.628  1.00 15.78 ? 767  THR   A CA  1 
ATOM   1916 C  C   . THR   A 1 245 ? 30.559 -18.077 13.199  1.00 19.16 ? 767  THR   A C   1 
ATOM   1917 O  O   . THR   A 1 245 ? 31.553 -18.212 13.925  1.00 20.84 ? 767  THR   A O   1 
ATOM   1918 C  CB  . THR   A 1 245 ? 28.943 -19.927 13.688  1.00 17.39 ? 767  THR   A CB  1 
ATOM   1919 O  OG1 . THR   A 1 245 ? 28.257 -21.046 13.100  1.00 19.74 ? 767  THR   A OG1 1 
ATOM   1920 C  CG2 . THR   A 1 245 ? 27.914 -18.914 14.248  1.00 19.18 ? 767  THR   A CG2 1 
ATOM   1921 N  N   . ILE   A 1 246 ? 30.037 -16.887 12.875  1.00 14.60 ? 768  ILE   A N   1 
ATOM   1922 C  CA  . ILE   A 1 246 ? 30.399 -15.652 13.581  1.00 16.01 ? 768  ILE   A CA  1 
ATOM   1923 C  C   . ILE   A 1 246 ? 29.191 -15.199 14.376  1.00 17.67 ? 768  ILE   A C   1 
ATOM   1924 O  O   . ILE   A 1 246 ? 28.090 -15.108 13.820  1.00 16.95 ? 768  ILE   A O   1 
ATOM   1925 C  CB  . ILE   A 1 246 ? 30.823 -14.508 12.641  1.00 17.69 ? 768  ILE   A CB  1 
ATOM   1926 C  CG1 . ILE   A 1 246 ? 32.029 -14.865 11.778  1.00 25.08 ? 768  ILE   A CG1 1 
ATOM   1927 C  CG2 . ILE   A 1 246 ? 31.211 -13.291 13.461  1.00 21.90 ? 768  ILE   A CG2 1 
ATOM   1928 C  CD1 . ILE   A 1 246 ? 32.277 -13.786 10.717  1.00 25.57 ? 768  ILE   A CD1 1 
ATOM   1929 N  N   . ILE   A 1 247 ? 29.388 -14.893 15.656  1.00 13.50 ? 769  ILE   A N   1 
ATOM   1930 C  CA  . ILE   A 1 247 ? 28.349 -14.254 16.468  1.00 16.04 ? 769  ILE   A CA  1 
ATOM   1931 C  C   . ILE   A 1 247 ? 28.831 -12.850 16.791  1.00 22.97 ? 769  ILE   A C   1 
ATOM   1932 O  O   . ILE   A 1 247 ? 29.805 -12.676 17.532  1.00 18.99 ? 769  ILE   A O   1 
ATOM   1933 C  CB  . ILE   A 1 247 ? 28.071 -15.013 17.766  1.00 20.68 ? 769  ILE   A CB  1 
ATOM   1934 C  CG1 . ILE   A 1 247 ? 27.630 -16.452 17.494  1.00 19.71 ? 769  ILE   A CG1 1 
ATOM   1935 C  CG2 . ILE   A 1 247 ? 27.024 -14.241 18.581  1.00 18.28 ? 769  ILE   A CG2 1 
ATOM   1936 C  CD1 . ILE   A 1 247 ? 27.510 -17.244 18.760  1.00 19.15 ? 769  ILE   A CD1 1 
ATOM   1937 N  N   . TYR   A 1 248 ? 28.139 -11.845 16.273  1.00 16.87 ? 770  TYR   A N   1 
ATOM   1938 C  CA  . TYR   A 1 248 ? 28.444 -10.457 16.573  1.00 17.20 ? 770  TYR   A CA  1 
ATOM   1939 C  C   . TYR   A 1 248 ? 27.672 -10.001 17.803  1.00 19.83 ? 770  TYR   A C   1 
ATOM   1940 O  O   . TYR   A 1 248 ? 26.438 -10.087 17.840  1.00 19.31 ? 770  TYR   A O   1 
ATOM   1941 C  CB  . TYR   A 1 248 ? 28.051 -9.568  15.401  1.00 18.40 ? 770  TYR   A CB  1 
ATOM   1942 C  CG  . TYR   A 1 248 ? 28.809 -9.788  14.121  1.00 20.28 ? 770  TYR   A CG  1 
ATOM   1943 C  CD1 . TYR   A 1 248 ? 30.084 -9.273  13.960  1.00 22.10 ? 770  TYR   A CD1 1 
ATOM   1944 C  CD2 . TYR   A 1 248 ? 28.225 -10.454 13.050  1.00 19.94 ? 770  TYR   A CD2 1 
ATOM   1945 C  CE1 . TYR   A 1 248 ? 30.769 -9.427  12.772  1.00 22.57 ? 770  TYR   A CE1 1 
ATOM   1946 C  CE2 . TYR   A 1 248 ? 28.912 -10.610 11.850  1.00 19.73 ? 770  TYR   A CE2 1 
ATOM   1947 C  CZ  . TYR   A 1 248 ? 30.176 -10.087 11.724  1.00 15.66 ? 770  TYR   A CZ  1 
ATOM   1948 O  OH  . TYR   A 1 248 ? 30.869 -10.194 10.542  1.00 20.42 ? 770  TYR   A OH  1 
ATOM   1949 N  N   . CYS   A 1 249 ? 28.383 -9.438  18.766  1.00 18.43 ? 771  CYS   A N   1 
ATOM   1950 C  CA  . CYS   A 1 249 ? 27.807 -8.921  19.992  1.00 20.78 ? 771  CYS   A CA  1 
ATOM   1951 C  C   . CYS   A 1 249 ? 28.088 -7.431  20.111  1.00 19.29 ? 771  CYS   A C   1 
ATOM   1952 O  O   . CYS   A 1 249 ? 29.122 -6.942  19.631  1.00 20.86 ? 771  CYS   A O   1 
ATOM   1953 C  CB  . CYS   A 1 249 ? 28.375 -9.644  21.222  1.00 21.16 ? 771  CYS   A CB  1 
ATOM   1954 S  SG  . CYS   A 1 249 ? 27.998 -11.404 21.283  1.00 23.25 ? 771  CYS   A SG  1 
ATOM   1955 N  N   . PRO   A 1 250 ? 27.193 -6.676  20.746  1.00 19.64 ? 772  PRO   A N   1 
ATOM   1956 C  CA  . PRO   A 1 250 ? 27.358 -5.219  20.745  1.00 22.49 ? 772  PRO   A CA  1 
ATOM   1957 C  C   . PRO   A 1 250 ? 28.352 -4.707  21.770  1.00 29.66 ? 772  PRO   A C   1 
ATOM   1958 O  O   . PRO   A 1 250 ? 28.704 -3.524  21.711  1.00 30.25 ? 772  PRO   A O   1 
ATOM   1959 C  CB  . PRO   A 1 250 ? 25.940 -4.706  21.033  1.00 24.03 ? 772  PRO   A CB  1 
ATOM   1960 C  CG  . PRO   A 1 250 ? 25.312 -5.779  21.839  1.00 30.30 ? 772  PRO   A CG  1 
ATOM   1961 C  CD  . PRO   A 1 250 ? 25.880 -7.088  21.286  1.00 21.44 ? 772  PRO   A CD  1 
ATOM   1962 N  N   . SER   A 1 251 ? 28.814 -5.538  22.700  1.00 23.31 ? 773  SER   A N   1 
ATOM   1963 C  CA  . SER   A 1 251 ? 29.732 -5.071  23.735  1.00 26.50 ? 773  SER   A CA  1 
ATOM   1964 C  C   . SER   A 1 251 ? 30.676 -6.199  24.107  1.00 24.86 ? 773  SER   A C   1 
ATOM   1965 O  O   . SER   A 1 251 ? 30.363 -7.364  23.923  1.00 23.53 ? 773  SER   A O   1 
ATOM   1966 C  CB  . SER   A 1 251 ? 28.990 -4.620  24.985  1.00 28.02 ? 773  SER   A CB  1 
ATOM   1967 O  OG  . SER   A 1 251 ? 28.320 -5.728  25.577  1.00 28.05 ? 773  SER   A OG  1 
ATOM   1968 N  N   . ARG   A 1 252 ? 31.826 -5.841  24.677  1.00 29.54 ? 774  ARG   A N   1 
ATOM   1969 C  CA  . ARG   A 1 252 ? 32.755 -6.876  25.126  1.00 27.59 ? 774  ARG   A CA  1 
ATOM   1970 C  C   . ARG   A 1 252 ? 32.172 -7.716  26.261  1.00 27.10 ? 774  ARG   A C   1 
ATOM   1971 O  O   . ARG   A 1 252 ? 32.408 -8.930  26.315  1.00 30.92 ? 774  ARG   A O   1 
ATOM   1972 C  CB  . ARG   A 1 252 ? 34.087 -6.236  25.528  1.00 35.10 ? 774  ARG   A CB  1 
ATOM   1973 C  CG  . ARG   A 1 252 ? 34.877 -5.772  24.319  1.00 36.90 ? 774  ARG   A CG  1 
ATOM   1974 C  CD  . ARG   A 1 252 ? 36.246 -5.246  24.682  1.00 49.20 ? 774  ARG   A CD  1 
ATOM   1975 N  NE  . ARG   A 1 252 ? 36.579 -4.112  23.830  1.00 51.64 ? 774  ARG   A NE  1 
ATOM   1976 C  CZ  . ARG   A 1 252 ? 37.664 -3.362  23.963  1.00 56.05 ? 774  ARG   A CZ  1 
ATOM   1977 N  NH1 . ARG   A 1 252 ? 38.575 -3.621  24.889  1.00 59.26 ? 774  ARG   A NH1 1 
ATOM   1978 N  NH2 . ARG   A 1 252 ? 37.837 -2.324  23.151  1.00 52.10 ? 774  ARG   A NH2 1 
ATOM   1979 N  N   . LYS   A 1 253 ? 31.397 -7.109  27.159  1.00 29.93 ? 775  LYS   A N   1 
ATOM   1980 C  CA  . LYS   A 1 253 ? 30.743 -7.886  28.209  1.00 31.26 ? 775  LYS   A CA  1 
ATOM   1981 C  C   . LYS   A 1 253 ? 29.815 -8.958  27.636  1.00 32.39 ? 775  LYS   A C   1 
ATOM   1982 O  O   . LYS   A 1 253 ? 29.807 -10.103 28.105  1.00 32.10 ? 775  LYS   A O   1 
ATOM   1983 C  CB  . LYS   A 1 253 ? 29.969 -6.957  29.136  1.00 31.96 ? 775  LYS   A CB  1 
ATOM   1984 C  CG  . LYS   A 1 253 ? 28.851 -7.632  29.903  1.00 47.44 ? 775  LYS   A CG  1 
ATOM   1985 C  CD  . LYS   A 1 253 ? 28.558 -6.912  31.214  1.00 59.24 ? 775  LYS   A CD  1 
ATOM   1986 C  CE  . LYS   A 1 253 ? 27.226 -6.161  31.184  1.00 65.91 ? 775  LYS   A CE  1 
ATOM   1987 N  NZ  . LYS   A 1 253 ? 26.666 -5.953  32.559  1.00 67.94 ? 775  LYS   A NZ  1 
ATOM   1988 N  N   . MET   A 1 254 ? 29.008 -8.609  26.640  1.00 30.89 ? 776  MET   A N   1 
ATOM   1989 C  CA  . MET   A 1 254 ? 28.137 -9.631  26.070  1.00 22.40 ? 776  MET   A CA  1 
ATOM   1990 C  C   . MET   A 1 254 ? 28.954 -10.654 25.279  1.00 22.26 ? 776  MET   A C   1 
ATOM   1991 O  O   . MET   A 1 254 ? 28.615 -11.838 25.280  1.00 25.47 ? 776  MET   A O   1 
ATOM   1992 C  CB  . MET   A 1 254 ? 27.048 -8.968  25.218  1.00 25.35 ? 776  MET   A CB  1 
ATOM   1993 C  CG  . MET   A 1 254 ? 25.988 -9.917  24.636  1.00 31.01 ? 776  MET   A CG  1 
ATOM   1994 S  SD  . MET   A 1 254 ? 25.136 -11.019 25.803  1.00 36.17 ? 776  MET   A SD  1 
ATOM   1995 C  CE  . MET   A 1 254 ? 24.326 -9.839  26.887  1.00 36.55 ? 776  MET   A CE  1 
ATOM   1996 N  N   . THR   A 1 255 ? 30.044 -10.233 24.628  1.00 25.14 ? 777  THR   A N   1 
ATOM   1997 C  CA  . THR   A 1 255 ? 30.913 -11.212 23.971  1.00 23.82 ? 777  THR   A CA  1 
ATOM   1998 C  C   . THR   A 1 255 ? 31.432 -12.230 24.978  1.00 23.34 ? 777  THR   A C   1 
ATOM   1999 O  O   . THR   A 1 255 ? 31.419 -13.443 24.717  1.00 26.15 ? 777  THR   A O   1 
ATOM   2000 C  CB  . THR   A 1 255 ? 32.075 -10.511 23.258  1.00 27.88 ? 777  THR   A CB  1 
ATOM   2001 O  OG1 . THR   A 1 255 ? 31.614 -10.039 21.991  1.00 31.77 ? 777  THR   A OG1 1 
ATOM   2002 C  CG2 . THR   A 1 255 ? 33.221 -11.466 22.989  1.00 23.82 ? 777  THR   A CG2 1 
ATOM   2003 N  N   . GLN   A 1 256 ? 31.832 -11.764 26.161  1.00 28.94 ? 778  GLN   A N   1 
ATOM   2004 C  CA  . GLN   A 1 256 ? 32.360 -12.694 27.156  1.00 32.15 ? 778  GLN   A CA  1 
ATOM   2005 C  C   . GLN   A 1 256 ? 31.259 -13.585 27.712  1.00 29.89 ? 778  GLN   A C   1 
ATOM   2006 O  O   . GLN   A 1 256 ? 31.469 -14.786 27.894  1.00 26.32 ? 778  GLN   A O   1 
ATOM   2007 C  CB  . GLN   A 1 256 ? 33.079 -11.931 28.270  1.00 29.83 ? 778  GLN   A CB  1 
ATOM   2008 C  CG  . GLN   A 1 256 ? 34.342 -11.216 27.784  1.00 39.69 ? 778  GLN   A CG  1 
ATOM   2009 C  CD  . GLN   A 1 256 ? 35.397 -12.172 27.203  1.00 48.54 ? 778  GLN   A CD  1 
ATOM   2010 O  OE1 . GLN   A 1 256 ? 35.458 -13.354 27.567  1.00 50.08 ? 778  GLN   A OE1 1 
ATOM   2011 N  NE2 . GLN   A 1 256 ? 36.235 -11.656 26.301  1.00 47.43 ? 778  GLN   A NE2 1 
ATOM   2012 N  N   . GLN   A 1 257 ? 30.074 -13.027 27.966  1.00 34.38 ? 779  GLN   A N   1 
ATOM   2013 C  CA  . GLN   A 1 257 ? 28.957 -13.851 28.437  1.00 33.39 ? 779  GLN   A CA  1 
ATOM   2014 C  C   . GLN   A 1 257 ? 28.617 -14.956 27.449  1.00 29.20 ? 779  GLN   A C   1 
ATOM   2015 O  O   . GLN   A 1 257 ? 28.478 -16.128 27.827  1.00 28.15 ? 779  GLN   A O   1 
ATOM   2016 C  CB  . GLN   A 1 257 ? 27.723 -12.990 28.672  1.00 31.89 ? 779  GLN   A CB  1 
ATOM   2017 C  CG  . GLN   A 1 257 ? 27.616 -12.391 30.037  1.00 45.23 ? 779  GLN   A CG  1 
ATOM   2018 C  CD  . GLN   A 1 257 ? 26.433 -11.467 30.132  1.00 47.50 ? 779  GLN   A CD  1 
ATOM   2019 O  OE1 . GLN   A 1 257 ? 25.288 -11.877 29.909  1.00 56.00 ? 779  GLN   A OE1 1 
ATOM   2020 N  NE2 . GLN   A 1 257 ? 26.696 -10.207 30.434  1.00 52.93 ? 779  GLN   A NE2 1 
ATOM   2021 N  N   . VAL   A 1 258 ? 28.438 -14.590 26.176  1.00 26.79 ? 780  VAL   A N   1 
ATOM   2022 C  CA  . VAL   A 1 258 ? 28.097 -15.572 25.151  1.00 24.16 ? 780  VAL   A CA  1 
ATOM   2023 C  C   . VAL   A 1 258 ? 29.183 -16.638 25.055  1.00 24.42 ? 780  VAL   A C   1 
ATOM   2024 O  O   . VAL   A 1 258 ? 28.898 -17.840 25.015  1.00 23.70 ? 780  VAL   A O   1 
ATOM   2025 C  CB  . VAL   A 1 258 ? 27.862 -14.870 23.800  1.00 21.44 ? 780  VAL   A CB  1 
ATOM   2026 C  CG1 . VAL   A 1 258 ? 27.851 -15.894 22.674  1.00 24.61 ? 780  VAL   A CG1 1 
ATOM   2027 C  CG2 . VAL   A 1 258 ? 26.556 -14.047 23.844  1.00 22.81 ? 780  VAL   A CG2 1 
ATOM   2028 N  N   . THR   A 1 259 ? 30.449 -16.216 25.022  1.00 25.95 ? 781  THR   A N   1 
ATOM   2029 C  CA  . THR   A 1 259 ? 31.530 -17.195 24.941  1.00 23.31 ? 781  THR   A CA  1 
ATOM   2030 C  C   . THR   A 1 259 ? 31.518 -18.139 26.135  1.00 25.57 ? 781  THR   A C   1 
ATOM   2031 O  O   . THR   A 1 259 ? 31.680 -19.353 25.971  1.00 25.78 ? 781  THR   A O   1 
ATOM   2032 C  CB  . THR   A 1 259 ? 32.871 -16.476 24.829  1.00 28.04 ? 781  THR   A CB  1 
ATOM   2033 O  OG1 . THR   A 1 259 ? 32.840 -15.609 23.686  1.00 25.45 ? 781  THR   A OG1 1 
ATOM   2034 C  CG2 . THR   A 1 259 ? 34.003 -17.489 24.661  1.00 26.71 ? 781  THR   A CG2 1 
ATOM   2035 N  N   . GLY   A 1 260 ? 31.311 -17.609 27.345  1.00 27.87 ? 782  GLY   A N   1 
ATOM   2036 C  CA  . GLY   A 1 260 ? 31.297 -18.476 28.515  1.00 32.41 ? 782  GLY   A CA  1 
ATOM   2037 C  C   . GLY   A 1 260 ? 30.182 -19.505 28.453  1.00 32.43 ? 782  GLY   A C   1 
ATOM   2038 O  O   . GLY   A 1 260 ? 30.375 -20.685 28.783  1.00 30.28 ? 782  GLY   A O   1 
ATOM   2039 N  N   . GLU   A 1 261 ? 29.004 -19.075 27.989  1.00 24.77 ? 783  GLU   A N   1 
ATOM   2040 C  CA  . GLU   A 1 261 ? 27.880 -19.996 27.863  1.00 28.09 ? 783  GLU   A CA  1 
ATOM   2041 C  C   . GLU   A 1 261 ? 28.179 -21.092 26.852  1.00 30.51 ? 783  GLU   A C   1 
ATOM   2042 O  O   . GLU   A 1 261 ? 27.903 -22.279 27.093  1.00 26.66 ? 783  GLU   A O   1 
ATOM   2043 C  CB  . GLU   A 1 261 ? 26.614 -19.224 27.465  1.00 28.45 ? 783  GLU   A CB  1 
ATOM   2044 C  CG  . GLU   A 1 261 ? 26.053 -18.366 28.573  1.00 30.55 ? 783  GLU   A CG  1 
ATOM   2045 C  CD  . GLU   A 1 261 ? 25.982 -19.121 29.885  1.00 41.67 ? 783  GLU   A CD  1 
ATOM   2046 O  OE1 . GLU   A 1 261 ? 25.109 -20.004 30.018  1.00 35.05 ? 783  GLU   A OE1 1 
ATOM   2047 O  OE2 . GLU   A 1 261 ? 26.832 -18.856 30.766  1.00 45.95 ? 783  GLU   A OE2 1 
ATOM   2048 N  N   . LEU   A 1 262 ? 28.727 -20.715 25.697  1.00 24.42 ? 784  LEU   A N   1 
ATOM   2049 C  CA  . LEU   A 1 262 ? 28.996 -21.730 24.685  1.00 25.79 ? 784  LEU   A CA  1 
ATOM   2050 C  C   . LEU   A 1 262 ? 30.075 -22.689 25.152  1.00 27.56 ? 784  LEU   A C   1 
ATOM   2051 O  O   . LEU   A 1 262 ? 30.028 -23.880 24.822  1.00 28.26 ? 784  LEU   A O   1 
ATOM   2052 C  CB  . LEU   A 1 262 ? 29.419 -21.088 23.366  1.00 26.37 ? 784  LEU   A CB  1 
ATOM   2053 C  CG  . LEU   A 1 262 ? 28.339 -20.265 22.670  1.00 25.98 ? 784  LEU   A CG  1 
ATOM   2054 C  CD1 . LEU   A 1 262 ? 28.948 -19.517 21.466  1.00 26.58 ? 784  LEU   A CD1 1 
ATOM   2055 C  CD2 . LEU   A 1 262 ? 27.149 -21.142 22.271  1.00 24.70 ? 784  LEU   A CD2 1 
ATOM   2056 N  N   . ARG   A 1 263 ? 31.047 -22.197 25.917  1.00 24.22 ? 785  ARG   A N   1 
ATOM   2057 C  CA  . ARG   A 1 263 ? 32.070 -23.095 26.421  1.00 29.73 ? 785  ARG   A CA  1 
ATOM   2058 C  C   . ARG   A 1 263 ? 31.530 -24.035 27.483  1.00 39.56 ? 785  ARG   A C   1 
ATOM   2059 O  O   . ARG   A 1 263 ? 32.124 -25.094 27.701  1.00 30.40 ? 785  ARG   A O   1 
ATOM   2060 C  CB  . ARG   A 1 263 ? 33.260 -22.298 26.937  1.00 28.98 ? 785  ARG   A CB  1 
ATOM   2061 C  CG  . ARG   A 1 263 ? 34.182 -21.877 25.802  1.00 33.65 ? 785  ARG   A CG  1 
ATOM   2062 C  CD  . ARG   A 1 263 ? 35.181 -20.813 26.242  1.00 34.71 ? 785  ARG   A CD  1 
ATOM   2063 N  NE  . ARG   A 1 263 ? 36.086 -20.479 25.153  1.00 34.52 ? 785  ARG   A NE  1 
ATOM   2064 C  CZ  . ARG   A 1 263 ? 36.859 -19.403 25.129  1.00 38.60 ? 785  ARG   A CZ  1 
ATOM   2065 N  NH1 . ARG   A 1 263 ? 36.872 -18.534 26.133  1.00 34.05 ? 785  ARG   A NH1 1 
ATOM   2066 N  NH2 . ARG   A 1 263 ? 37.612 -19.176 24.060  1.00 33.97 ? 785  ARG   A NH2 1 
ATOM   2067 N  N   . LYS   A 1 264 ? 30.409 -23.693 28.131  1.00 32.81 ? 786  LYS   A N   1 
ATOM   2068 C  CA  . LYS   A 1 264 ? 29.759 -24.695 28.977  1.00 31.26 ? 786  LYS   A CA  1 
ATOM   2069 C  C   . LYS   A 1 264 ? 29.350 -25.931 28.188  1.00 35.29 ? 786  LYS   A C   1 
ATOM   2070 O  O   . LYS   A 1 264 ? 29.183 -27.003 28.779  1.00 36.46 ? 786  LYS   A O   1 
ATOM   2071 C  CB  . LYS   A 1 264 ? 28.536 -24.109 29.686  1.00 35.39 ? 786  LYS   A CB  1 
ATOM   2072 C  CG  . LYS   A 1 264 ? 28.887 -23.062 30.737  1.00 39.34 ? 786  LYS   A CG  1 
ATOM   2073 C  CD  . LYS   A 1 264 ? 27.654 -22.534 31.463  1.00 38.29 ? 786  LYS   A CD  1 
ATOM   2074 C  CE  . LYS   A 1 264 ? 28.088 -21.462 32.459  1.00 51.38 ? 786  LYS   A CE  1 
ATOM   2075 N  NZ  . LYS   A 1 264 ? 26.955 -20.738 33.098  1.00 49.36 ? 786  LYS   A NZ  1 
ATOM   2076 N  N   . LEU   A 1 265 ? 29.209 -25.826 26.868  1.00 26.74 ? 787  LEU   A N   1 
ATOM   2077 C  CA  . LEU   A 1 265 ? 28.882 -26.975 26.029  1.00 32.37 ? 787  LEU   A CA  1 
ATOM   2078 C  C   . LEU   A 1 265 ? 30.108 -27.511 25.292  1.00 26.79 ? 787  LEU   A C   1 
ATOM   2079 O  O   . LEU   A 1 265 ? 29.970 -28.304 24.354  1.00 28.93 ? 787  LEU   A O   1 
ATOM   2080 C  CB  . LEU   A 1 265 ? 27.764 -26.612 25.041  1.00 28.34 ? 787  LEU   A CB  1 
ATOM   2081 C  CG  . LEU   A 1 265 ? 26.322 -26.491 25.560  1.00 37.00 ? 787  LEU   A CG  1 
ATOM   2082 C  CD1 . LEU   A 1 265 ? 26.213 -25.549 26.727  1.00 41.77 ? 787  LEU   A CD1 1 
ATOM   2083 C  CD2 . LEU   A 1 265 ? 25.370 -26.040 24.449  1.00 36.95 ? 787  LEU   A CD2 1 
ATOM   2084 N  N   . ASN   A 1 266 ? 31.297 -27.089 25.711  1.00 27.78 ? 788  ASN   A N   1 
ATOM   2085 C  CA  . ASN   A 1 266 ? 32.577 -27.518 25.145  1.00 36.81 ? 788  ASN   A CA  1 
ATOM   2086 C  C   . ASN   A 1 266 ? 32.698 -27.179 23.664  1.00 32.43 ? 788  ASN   A C   1 
ATOM   2087 O  O   . ASN   A 1 266 ? 33.366 -27.883 22.903  1.00 36.39 ? 788  ASN   A O   1 
ATOM   2088 C  CB  . ASN   A 1 266 ? 32.807 -29.009 25.388  1.00 40.84 ? 788  ASN   A CB  1 
ATOM   2089 C  CG  . ASN   A 1 266 ? 32.891 -29.330 26.863  1.00 48.45 ? 788  ASN   A CG  1 
ATOM   2090 O  OD1 . ASN   A 1 266 ? 32.129 -30.146 27.384  1.00 57.52 ? 788  ASN   A OD1 1 
ATOM   2091 N  ND2 . ASN   A 1 266 ? 33.801 -28.653 27.558  1.00 51.04 ? 788  ASN   A ND2 1 
ATOM   2092 N  N   . LEU   A 1 267 ? 32.063 -26.091 23.243  1.00 30.59 ? 789  LEU   A N   1 
ATOM   2093 C  CA  . LEU   A 1 267 ? 32.185 -25.654 21.863  1.00 27.98 ? 789  LEU   A CA  1 
ATOM   2094 C  C   . LEU   A 1 267 ? 33.527 -24.969 21.663  1.00 25.57 ? 789  LEU   A C   1 
ATOM   2095 O  O   . LEU   A 1 267 ? 34.050 -24.301 22.559  1.00 27.32 ? 789  LEU   A O   1 
ATOM   2096 C  CB  . LEU   A 1 267 ? 31.045 -24.699 21.483  1.00 25.02 ? 789  LEU   A CB  1 
ATOM   2097 C  CG  . LEU   A 1 267 ? 29.666 -25.370 21.467  1.00 31.70 ? 789  LEU   A CG  1 
ATOM   2098 C  CD1 . LEU   A 1 267 ? 28.553 -24.342 21.537  1.00 33.19 ? 789  LEU   A CD1 1 
ATOM   2099 C  CD2 . LEU   A 1 267 ? 29.474 -26.239 20.237  1.00 35.11 ? 789  LEU   A CD2 1 
ATOM   2100 N  N   . SER   A 1 268 ? 34.069 -25.127 20.461  1.00 26.11 ? 790  SER   A N   1 
ATOM   2101 C  CA  . SER   A 1 268 ? 35.358 -24.569 20.096  1.00 26.28 ? 790  SER   A CA  1 
ATOM   2102 C  C   . SER   A 1 268 ? 35.152 -23.132 19.634  1.00 27.83 ? 790  SER   A C   1 
ATOM   2103 O  O   . SER   A 1 268 ? 34.686 -22.916 18.514  1.00 27.04 ? 790  SER   A O   1 
ATOM   2104 C  CB  . SER   A 1 268 ? 35.969 -25.411 18.986  1.00 28.09 ? 790  SER   A CB  1 
ATOM   2105 O  OG  . SER   A 1 268 ? 37.312 -25.022 18.786  1.00 41.58 ? 790  SER   A OG  1 
ATOM   2106 N  N   . CYS   A 1 269 ? 35.525 -22.160 20.486  1.00 25.05 ? 791  CYS   A N   1 
ATOM   2107 C  CA  . CYS   A 1 269 ? 35.230 -20.731 20.328  1.00 29.88 ? 791  CYS   A CA  1 
ATOM   2108 C  C   . CYS   A 1 269 ? 36.474 -19.884 20.465  1.00 30.67 ? 791  CYS   A C   1 
ATOM   2109 O  O   . CYS   A 1 269 ? 37.410 -20.243 21.179  1.00 35.32 ? 791  CYS   A O   1 
ATOM   2110 C  CB  . CYS   A 1 269 ? 34.278 -20.189 21.411  1.00 25.10 ? 791  CYS   A CB  1 
ATOM   2111 S  SG  . CYS   A 1 269 ? 32.808 -21.061 21.554  1.00 34.61 ? 791  CYS   A SG  1 
ATOM   2112 N  N   . GLY   A 1 270 ? 36.420 -18.700 19.865  1.00 22.92 ? 792  GLY   A N   1 
ATOM   2113 C  CA  . GLY   A 1 270 ? 37.379 -17.654 20.154  1.00 23.17 ? 792  GLY   A CA  1 
ATOM   2114 C  C   . GLY   A 1 270 ? 36.703 -16.301 20.101  1.00 29.32 ? 792  GLY   A C   1 
ATOM   2115 O  O   . GLY   A 1 270 ? 35.766 -16.093 19.333  1.00 22.73 ? 792  GLY   A O   1 
ATOM   2116 N  N   . THR   A 1 271 ? 37.168 -15.377 20.932  1.00 23.72 ? 793  THR   A N   1 
ATOM   2117 C  CA  . THR   A 1 271 ? 36.628 -14.024 20.881  1.00 24.93 ? 793  THR   A CA  1 
ATOM   2118 C  C   . THR   A 1 271 ? 37.496 -13.138 20.005  1.00 31.12 ? 793  THR   A C   1 
ATOM   2119 O  O   . THR   A 1 271 ? 38.642 -13.466 19.670  1.00 34.28 ? 793  THR   A O   1 
ATOM   2120 C  CB  . THR   A 1 271 ? 36.519 -13.401 22.272  1.00 27.63 ? 793  THR   A CB  1 
ATOM   2121 O  OG1 . THR   A 1 271 ? 37.825 -13.296 22.827  1.00 35.75 ? 793  THR   A OG1 1 
ATOM   2122 C  CG2 . THR   A 1 271 ? 35.707 -14.262 23.175  1.00 25.26 ? 793  THR   A CG2 1 
ATOM   2123 N  N   . TYR   A 1 272 ? 36.943 -11.977 19.652  1.00 23.96 ? 794  TYR   A N   1 
ATOM   2124 C  CA  . TYR   A 1 272 ? 37.600 -11.126 18.660  1.00 22.76 ? 794  TYR   A CA  1 
ATOM   2125 C  C   . TYR   A 1 272 ? 37.100 -9.706  18.890  1.00 27.50 ? 794  TYR   A C   1 
ATOM   2126 O  O   . TYR   A 1 272 ? 35.974 -9.378  18.512  1.00 30.01 ? 794  TYR   A O   1 
ATOM   2127 C  CB  . TYR   A 1 272 ? 37.296 -11.630 17.258  1.00 24.46 ? 794  TYR   A CB  1 
ATOM   2128 C  CG  . TYR   A 1 272 ? 38.060 -11.000 16.115  1.00 26.89 ? 794  TYR   A CG  1 
ATOM   2129 C  CD1 . TYR   A 1 272 ? 39.266 -11.543 15.663  1.00 28.82 ? 794  TYR   A CD1 1 
ATOM   2130 C  CD2 . TYR   A 1 272 ? 37.553 -9.898  15.448  1.00 35.43 ? 794  TYR   A CD2 1 
ATOM   2131 C  CE1 . TYR   A 1 272 ? 39.947 -10.974 14.601  1.00 36.11 ? 794  TYR   A CE1 1 
ATOM   2132 C  CE2 . TYR   A 1 272 ? 38.220 -9.337  14.390  1.00 31.61 ? 794  TYR   A CE2 1 
ATOM   2133 C  CZ  . TYR   A 1 272 ? 39.409 -9.867  13.972  1.00 36.90 ? 794  TYR   A CZ  1 
ATOM   2134 O  OH  . TYR   A 1 272 ? 40.057 -9.283  12.914  1.00 43.46 ? 794  TYR   A OH  1 
ATOM   2135 N  N   . HIS   A 1 273 ? 37.928 -8.882  19.528  1.00 29.97 ? 795  HIS   A N   1 
ATOM   2136 C  CA  . HIS   A 1 273 ? 37.519 -7.526  19.852  1.00 32.32 ? 795  HIS   A CA  1 
ATOM   2137 C  C   . HIS   A 1 273 ? 38.750 -6.636  19.913  1.00 47.27 ? 795  HIS   A C   1 
ATOM   2138 O  O   . HIS   A 1 273 ? 39.888 -7.113  19.887  1.00 39.34 ? 795  HIS   A O   1 
ATOM   2139 C  CB  . HIS   A 1 273 ? 36.738 -7.483  21.167  1.00 31.37 ? 795  HIS   A CB  1 
ATOM   2140 C  CG  . HIS   A 1 273 ? 37.518 -7.957  22.350  1.00 42.12 ? 795  HIS   A CG  1 
ATOM   2141 N  ND1 . HIS   A 1 273 ? 38.517 -7.206  22.933  1.00 45.47 ? 795  HIS   A ND1 1 
ATOM   2142 C  CD2 . HIS   A 1 273 ? 37.447 -9.105  23.062  1.00 44.86 ? 795  HIS   A CD2 1 
ATOM   2143 C  CE1 . HIS   A 1 273 ? 39.029 -7.874  23.951  1.00 48.02 ? 795  HIS   A CE1 1 
ATOM   2144 N  NE2 . HIS   A 1 273 ? 38.398 -9.029  24.052  1.00 52.95 ? 795  HIS   A NE2 1 
ATOM   2145 N  N   . ALA   A 1 274 ? 38.494 -5.326  20.012  1.00 37.26 ? 796  ALA   A N   1 
ATOM   2146 C  CA  . ALA   A 1 274 ? 39.532 -4.303  19.934  1.00 40.69 ? 796  ALA   A CA  1 
ATOM   2147 C  C   . ALA   A 1 274 ? 40.463 -4.302  21.139  1.00 43.66 ? 796  ALA   A C   1 
ATOM   2148 O  O   . ALA   A 1 274 ? 41.565 -3.750  21.054  1.00 43.36 ? 796  ALA   A O   1 
ATOM   2149 C  CB  . ALA   A 1 274 ? 38.887 -2.925  19.781  1.00 40.23 ? 796  ALA   A CB  1 
ATOM   2150 N  N   . GLY   A 1 275 ? 40.055 -4.894  22.258  1.00 46.89 ? 797  GLY   A N   1 
ATOM   2151 C  CA  . GLY   A 1 275 ? 40.958 -4.998  23.391  1.00 45.78 ? 797  GLY   A CA  1 
ATOM   2152 C  C   . GLY   A 1 275 ? 42.133 -5.927  23.177  1.00 57.67 ? 797  GLY   A C   1 
ATOM   2153 O  O   . GLY   A 1 275 ? 43.022 -5.977  24.035  1.00 55.29 ? 797  GLY   A O   1 
ATOM   2154 N  N   . MET   A 1 276 ? 42.165 -6.649  22.060  1.00 48.38 ? 798  MET   A N   1 
ATOM   2155 C  CA  . MET   A 1 276 ? 43.182 -7.663  21.832  1.00 52.67 ? 798  MET   A CA  1 
ATOM   2156 C  C   . MET   A 1 276 ? 44.356 -7.078  21.077  1.00 48.86 ? 798  MET   A C   1 
ATOM   2157 O  O   . MET   A 1 276 ? 44.228 -6.086  20.364  1.00 46.85 ? 798  MET   A O   1 
ATOM   2158 C  CB  . MET   A 1 276 ? 42.612 -8.833  21.040  1.00 42.71 ? 798  MET   A CB  1 
ATOM   2159 C  CG  . MET   A 1 276 ? 41.558 -9.566  21.773  1.00 40.36 ? 798  MET   A CG  1 
ATOM   2160 S  SD  . MET   A 1 276 ? 40.781 -10.882 20.841  1.00 43.19 ? 798  MET   A SD  1 
ATOM   2161 C  CE  . MET   A 1 276 ? 39.817 -11.467 22.168  1.00 36.20 ? 798  MET   A CE  1 
ATOM   2162 N  N   . SER   A 1 277 ? 45.512 -7.711  21.236  1.00 46.74 ? 799  SER   A N   1 
ATOM   2163 C  CA  . SER   A 1 277 ? 46.643 -7.318  20.416  1.00 53.76 ? 799  SER   A CA  1 
ATOM   2164 C  C   . SER   A 1 277 ? 46.380 -7.710  18.969  1.00 54.04 ? 799  SER   A C   1 
ATOM   2165 O  O   . SER   A 1 277 ? 45.672 -8.683  18.686  1.00 44.98 ? 799  SER   A O   1 
ATOM   2166 C  CB  . SER   A 1 277 ? 47.939 -7.969  20.914  1.00 53.85 ? 799  SER   A CB  1 
ATOM   2167 O  OG  . SER   A 1 277 ? 48.098 -9.287  20.407  1.00 54.81 ? 799  SER   A OG  1 
ATOM   2168 N  N   . PHE   A 1 278 ? 46.947 -6.928  18.048  1.00 49.60 ? 800  PHE   A N   1 
ATOM   2169 C  CA  . PHE   A 1 278 ? 46.877 -7.277  16.636  1.00 57.02 ? 800  PHE   A CA  1 
ATOM   2170 C  C   . PHE   A 1 278 ? 47.301 -8.721  16.409  1.00 52.35 ? 800  PHE   A C   1 
ATOM   2171 O  O   . PHE   A 1 278 ? 46.682 -9.445  15.620  1.00 51.58 ? 800  PHE   A O   1 
ATOM   2172 C  CB  . PHE   A 1 278 ? 47.753 -6.325  15.826  1.00 61.86 ? 800  PHE   A CB  1 
ATOM   2173 C  CG  . PHE   A 1 278 ? 47.543 -6.418  14.345  1.00 69.73 ? 800  PHE   A CG  1 
ATOM   2174 C  CD1 . PHE   A 1 278 ? 46.442 -5.819  13.754  1.00 73.40 ? 800  PHE   A CD1 1 
ATOM   2175 C  CD2 . PHE   A 1 278 ? 48.452 -7.089  13.540  1.00 64.50 ? 800  PHE   A CD2 1 
ATOM   2176 C  CE1 . PHE   A 1 278 ? 46.246 -5.895  12.389  1.00 80.52 ? 800  PHE   A CE1 1 
ATOM   2177 C  CE2 . PHE   A 1 278 ? 48.261 -7.169  12.172  1.00 63.39 ? 800  PHE   A CE2 1 
ATOM   2178 C  CZ  . PHE   A 1 278 ? 47.158 -6.571  11.596  1.00 76.00 ? 800  PHE   A CZ  1 
ATOM   2179 N  N   . SER   A 1 279 ? 48.341 -9.168  17.117  1.00 56.29 ? 801  SER   A N   1 
ATOM   2180 C  CA  . SER   A 1 279 ? 48.813 -10.538 16.944  1.00 53.66 ? 801  SER   A CA  1 
ATOM   2181 C  C   . SER   A 1 279 ? 47.795 -11.546 17.460  1.00 42.26 ? 801  SER   A C   1 
ATOM   2182 O  O   . SER   A 1 279 ? 47.591 -12.598 16.844  1.00 40.83 ? 801  SER   A O   1 
ATOM   2183 C  CB  . SER   A 1 279 ? 50.155 -10.725 17.645  1.00 46.15 ? 801  SER   A CB  1 
ATOM   2184 O  OG  . SER   A 1 279 ? 51.142 -9.938  17.012  1.00 71.58 ? 801  SER   A OG  1 
ATOM   2185 N  N   . THR   A 1 280 ? 47.144 -11.232 18.577  1.00 46.32 ? 802  THR   A N   1 
ATOM   2186 C  CA  . THR   A 1 280 ? 46.163 -12.181 19.157  1.00 38.31 ? 802  THR   A CA  1 
ATOM   2187 C  C   . THR   A 1 280 ? 44.981 -12.323 18.185  1.00 37.17 ? 802  THR   A C   1 
ATOM   2188 O  O   . THR   A 1 280 ? 44.471 -13.432 18.042  1.00 35.64 ? 802  THR   A O   1 
ATOM   2189 C  CB  . THR   A 1 280 ? 45.710 -11.735 20.549  1.00 44.54 ? 802  THR   A CB  1 
ATOM   2190 O  OG1 . THR   A 1 280 ? 46.858 -11.683 21.394  1.00 52.09 ? 802  THR   A OG1 1 
ATOM   2191 C  CG2 . THR   A 1 280 ? 44.670 -12.653 21.148  1.00 45.42 ? 802  THR   A CG2 1 
ATOM   2192 N  N   . ARG   A 1 281 ? 44.582 -11.223 17.554  1.00 36.30 ? 803  ARG   A N   1 
ATOM   2193 C  CA  . ARG   A 1 281 ? 43.420 -11.253 16.627  1.00 41.67 ? 803  ARG   A CA  1 
ATOM   2194 C  C   . ARG   A 1 281 ? 43.820 -12.013 15.360  1.00 41.71 ? 803  ARG   A C   1 
ATOM   2195 O  O   . ARG   A 1 281 ? 42.990 -12.778 14.855  1.00 28.84 ? 803  ARG   A O   1 
ATOM   2196 C  CB  . ARG   A 1 281 ? 42.904 -9.838  16.364  1.00 44.47 ? 803  ARG   A CB  1 
ATOM   2197 C  CG  . ARG   A 1 281 ? 42.077 -9.272  17.508  1.00 44.90 ? 803  ARG   A CG  1 
ATOM   2198 C  CD  . ARG   A 1 281 ? 41.384 -7.985  17.117  1.00 49.60 ? 803  ARG   A CD  1 
ATOM   2199 N  NE  . ARG   A 1 281 ? 42.237 -7.182  16.258  1.00 53.29 ? 803  ARG   A NE  1 
ATOM   2200 C  CZ  . ARG   A 1 281 ? 42.727 -5.995  16.583  1.00 60.97 ? 803  ARG   A CZ  1 
ATOM   2201 N  NH1 . ARG   A 1 281 ? 43.082 -5.147  15.636  1.00 62.68 ? 803  ARG   A NH1 1 
ATOM   2202 N  NH2 . ARG   A 1 281 ? 42.861 -5.658  17.853  1.00 70.27 ? 803  ARG   A NH2 1 
ATOM   2203 N  N   . LYS   A 1 282 ? 45.060 -11.836 14.909  1.00 34.99 ? 804  LYS   A N   1 
ATOM   2204 C  CA  . LYS   A 1 282 ? 45.544 -12.631 13.752  1.00 35.40 ? 804  LYS   A CA  1 
ATOM   2205 C  C   . LYS   A 1 282 ? 45.509 -14.115 14.122  1.00 28.34 ? 804  LYS   A C   1 
ATOM   2206 O  O   . LYS   A 1 282 ? 45.106 -14.933 13.302  1.00 28.91 ? 804  LYS   A O   1 
ATOM   2207 C  CB  . LYS   A 1 282 ? 46.960 -12.186 13.391  1.00 40.83 ? 804  LYS   A CB  1 
ATOM   2208 C  CG  . LYS   A 1 282 ? 47.672 -12.969 12.301  1.00 43.60 ? 804  LYS   A CG  1 
ATOM   2209 C  CD  . LYS   A 1 282 ? 49.089 -12.475 12.089  1.00 45.79 ? 804  LYS   A CD  1 
ATOM   2210 C  CE  . LYS   A 1 282 ? 49.724 -13.002 10.820  1.00 57.45 ? 804  LYS   A CE  1 
ATOM   2211 N  NZ  . LYS   A 1 282 ? 51.044 -12.379 10.555  1.00 59.72 ? 804  LYS   A NZ  1 
ATOM   2212 N  N   . ASP   A 1 283 ? 45.911 -14.423 15.344  1.00 31.10 ? 805  ASP   A N   1 
ATOM   2213 C  CA  . ASP   A 1 283 ? 45.939 -15.823 15.734  1.00 27.00 ? 805  ASP   A CA  1 
ATOM   2214 C  C   . ASP   A 1 283 ? 44.538 -16.418 15.727  1.00 30.35 ? 805  ASP   A C   1 
ATOM   2215 O  O   . ASP   A 1 283 ? 44.333 -17.552 15.265  1.00 31.37 ? 805  ASP   A O   1 
ATOM   2216 C  CB  . ASP   A 1 283 ? 46.564 -15.959 17.120  1.00 37.81 ? 805  ASP   A CB  1 
ATOM   2217 C  CG  . ASP   A 1 283 ? 46.826 -17.388 17.493  1.00 43.72 ? 805  ASP   A CG  1 
ATOM   2218 O  OD1 . ASP   A 1 283 ? 47.643 -18.035 16.802  1.00 48.66 ? 805  ASP   A OD1 1 
ATOM   2219 O  OD2 . ASP   A 1 283 ? 46.220 -17.870 18.473  1.00 49.54 ? 805  ASP   A OD2 1 
ATOM   2220 N  N   . ILE   A 1 284 ? 43.567 -15.671 16.258  1.00 26.64 ? 806  ILE   A N   1 
ATOM   2221 C  CA  . ILE   A 1 284 ? 42.188 -16.167 16.289  1.00 29.68 ? 806  ILE   A CA  1 
ATOM   2222 C  C   . ILE   A 1 284 ? 41.647 -16.312 14.873  1.00 22.67 ? 806  ILE   A C   1 
ATOM   2223 O  O   . ILE   A 1 284 ? 41.014 -17.316 14.526  1.00 27.23 ? 806  ILE   A O   1 
ATOM   2224 C  CB  . ILE   A 1 284 ? 41.304 -15.246 17.146  1.00 30.99 ? 806  ILE   A CB  1 
ATOM   2225 C  CG1 . ILE   A 1 284 ? 41.710 -15.344 18.616  1.00 35.40 ? 806  ILE   A CG1 1 
ATOM   2226 C  CG2 . ILE   A 1 284 ? 39.828 -15.632 16.996  1.00 28.45 ? 806  ILE   A CG2 1 
ATOM   2227 C  CD1 . ILE   A 1 284 ? 41.433 -16.712 19.250  1.00 32.57 ? 806  ILE   A CD1 1 
ATOM   2228 N  N   . HIS   A 1 285 ? 41.892 -15.315 14.036  1.00 25.56 ? 807  HIS   A N   1 
ATOM   2229 C  CA  . HIS   A 1 285 ? 41.478 -15.405 12.646  1.00 27.30 ? 807  HIS   A CA  1 
ATOM   2230 C  C   . HIS   A 1 285 ? 42.053 -16.639 11.967  1.00 27.73 ? 807  HIS   A C   1 
ATOM   2231 O  O   . HIS   A 1 285 ? 41.343 -17.351 11.248  1.00 20.98 ? 807  HIS   A O   1 
ATOM   2232 C  CB  . HIS   A 1 285 ? 41.906 -14.141 11.914  1.00 26.19 ? 807  HIS   A CB  1 
ATOM   2233 C  CG  . HIS   A 1 285 ? 41.583 -14.161 10.457  1.00 36.64 ? 807  HIS   A CG  1 
ATOM   2234 N  ND1 . HIS   A 1 285 ? 42.555 -14.151 9.481   1.00 41.39 ? 807  HIS   A ND1 1 
ATOM   2235 C  CD2 . HIS   A 1 285 ? 40.397 -14.207 9.808   1.00 37.41 ? 807  HIS   A CD2 1 
ATOM   2236 C  CE1 . HIS   A 1 285 ? 41.981 -14.195 8.291   1.00 45.47 ? 807  HIS   A CE1 1 
ATOM   2237 N  NE2 . HIS   A 1 285 ? 40.671 -14.227 8.463   1.00 37.19 ? 807  HIS   A NE2 1 
ATOM   2238 N  N   . HIS   A 1 286 ? 43.345 -16.917 12.186  1.00 26.57 ? 808  HIS   A N   1 
ATOM   2239 C  CA  . HIS   A 1 286 ? 43.968 -18.071 11.542  1.00 24.48 ? 808  HIS   A CA  1 
ATOM   2240 C  C   . HIS   A 1 286 ? 43.394 -19.382 12.064  1.00 22.36 ? 808  HIS   A C   1 
ATOM   2241 O  O   . HIS   A 1 286 ? 43.192 -20.325 11.293  1.00 22.19 ? 808  HIS   A O   1 
ATOM   2242 C  CB  . HIS   A 1 286 ? 45.482 -18.038 11.745  1.00 26.80 ? 808  HIS   A CB  1 
ATOM   2243 C  CG  . HIS   A 1 286 ? 46.169 -16.953 10.976  1.00 26.10 ? 808  HIS   A CG  1 
ATOM   2244 N  ND1 . HIS   A 1 286 ? 45.597 -16.326 9.892   1.00 39.18 ? 808  HIS   A ND1 1 
ATOM   2245 C  CD2 . HIS   A 1 286 ? 47.393 -16.393 11.129  1.00 35.28 ? 808  HIS   A CD2 1 
ATOM   2246 C  CE1 . HIS   A 1 286 ? 46.430 -15.418 9.418   1.00 36.36 ? 808  HIS   A CE1 1 
ATOM   2247 N  NE2 . HIS   A 1 286 ? 47.527 -15.439 10.151  1.00 37.35 ? 808  HIS   A NE2 1 
ATOM   2248 N  N   . ARG   A 1 287 ? 43.125 -19.475 13.365  1.00 21.31 ? 809  ARG   A N   1 
ATOM   2249 C  CA  . ARG   A 1 287 ? 42.526 -20.719 13.853  1.00 24.02 ? 809  ARG   A CA  1 
ATOM   2250 C  C   . ARG   A 1 287 ? 41.094 -20.897 13.349  1.00 18.69 ? 809  ARG   A C   1 
ATOM   2251 O  O   . ARG   A 1 287 ? 40.638 -22.028 13.154  1.00 22.26 ? 809  ARG   A O   1 
ATOM   2252 C  CB  . ARG   A 1 287 ? 42.596 -20.762 15.381  1.00 32.27 ? 809  ARG   A CB  1 
ATOM   2253 C  CG  . ARG   A 1 287 ? 44.060 -20.813 15.836  1.00 32.60 ? 809  ARG   A CG  1 
ATOM   2254 C  CD  . ARG   A 1 287 ? 44.281 -20.824 17.334  1.00 41.57 ? 809  ARG   A CD  1 
ATOM   2255 N  NE  . ARG   A 1 287 ? 45.680 -20.496 17.609  1.00 48.45 ? 809  ARG   A NE  1 
ATOM   2256 C  CZ  . ARG   A 1 287 ? 46.692 -21.359 17.595  1.00 46.48 ? 809  ARG   A CZ  1 
ATOM   2257 N  NH1 . ARG   A 1 287 ? 46.500 -22.659 17.413  1.00 45.94 ? 809  ARG   A NH1 1 
ATOM   2258 N  NH2 . ARG   A 1 287 ? 47.931 -20.908 17.777  1.00 49.02 ? 809  ARG   A NH2 1 
ATOM   2259 N  N   . PHE   A 1 288 ? 40.383 -19.796 13.106  1.00 21.33 ? 810  PHE   A N   1 
ATOM   2260 C  CA  . PHE   A 1 288 ? 39.052 -19.896 12.504  1.00 22.72 ? 810  PHE   A CA  1 
ATOM   2261 C  C   . PHE   A 1 288 ? 39.156 -20.377 11.063  1.00 20.68 ? 810  PHE   A C   1 
ATOM   2262 O  O   . PHE   A 1 288 ? 38.423 -21.281 10.632  1.00 18.55 ? 810  PHE   A O   1 
ATOM   2263 C  CB  . PHE   A 1 288 ? 38.388 -18.523 12.594  1.00 15.68 ? 810  PHE   A CB  1 
ATOM   2264 C  CG  . PHE   A 1 288 ? 36.931 -18.492 12.226  1.00 17.97 ? 810  PHE   A CG  1 
ATOM   2265 C  CD1 . PHE   A 1 288 ? 36.072 -19.528 12.583  1.00 21.33 ? 810  PHE   A CD1 1 
ATOM   2266 C  CD2 . PHE   A 1 288 ? 36.418 -17.392 11.544  1.00 20.14 ? 810  PHE   A CD2 1 
ATOM   2267 C  CE1 . PHE   A 1 288 ? 34.733 -19.461 12.262  1.00 19.58 ? 810  PHE   A CE1 1 
ATOM   2268 C  CE2 . PHE   A 1 288 ? 35.075 -17.327 11.213  1.00 19.30 ? 810  PHE   A CE2 1 
ATOM   2269 C  CZ  . PHE   A 1 288 ? 34.228 -18.352 11.583  1.00 19.67 ? 810  PHE   A CZ  1 
ATOM   2270 N  N   . VAL   A 1 289 ? 40.087 -19.798 10.307  1.00 19.04 ? 811  VAL   A N   1 
ATOM   2271 C  CA  . VAL   A 1 289 ? 40.235 -20.176 8.904   1.00 22.21 ? 811  VAL   A CA  1 
ATOM   2272 C  C   . VAL   A 1 289 ? 40.520 -21.663 8.780   1.00 24.22 ? 811  VAL   A C   1 
ATOM   2273 O  O   . VAL   A 1 289 ? 39.939 -22.351 7.932   1.00 21.50 ? 811  VAL   A O   1 
ATOM   2274 C  CB  . VAL   A 1 289 ? 41.338 -19.339 8.225   1.00 20.52 ? 811  VAL   A CB  1 
ATOM   2275 C  CG1 . VAL   A 1 289 ? 41.681 -19.964 6.884   1.00 21.41 ? 811  VAL   A CG1 1 
ATOM   2276 C  CG2 . VAL   A 1 289 ? 40.848 -17.903 8.005   1.00 19.31 ? 811  VAL   A CG2 1 
ATOM   2277 N  N   . ARG   A 1 290 ? 41.381 -22.197 9.637   1.00 23.95 ? 812  ARG   A N   1 
ATOM   2278 C  CA  . ARG   A 1 290 ? 41.729 -23.606 9.487   1.00 21.80 ? 812  ARG   A CA  1 
ATOM   2279 C  C   . ARG   A 1 290 ? 40.785 -24.526 10.248  1.00 26.22 ? 812  ARG   A C   1 
ATOM   2280 O  O   . ARG   A 1 290 ? 41.028 -25.738 10.307  1.00 27.33 ? 812  ARG   A O   1 
ATOM   2281 C  CB  . ARG   A 1 290 ? 43.183 -23.849 9.912   1.00 24.51 ? 812  ARG   A CB  1 
ATOM   2282 C  CG  . ARG   A 1 290 ? 43.441 -23.881 11.415  1.00 29.99 ? 812  ARG   A CG  1 
ATOM   2283 C  CD  . ARG   A 1 290 ? 44.961 -24.109 11.698  1.00 39.60 ? 812  ARG   A CD  1 
ATOM   2284 N  NE  . ARG   A 1 290 ? 45.296 -24.238 13.118  1.00 33.59 ? 812  ARG   A NE  1 
ATOM   2285 C  CZ  . ARG   A 1 290 ? 46.495 -24.582 13.577  1.00 47.81 ? 812  ARG   A CZ  1 
ATOM   2286 N  NH1 . ARG   A 1 290 ? 47.515 -24.796 12.759  1.00 36.54 ? 812  ARG   A NH1 1 
ATOM   2287 N  NH2 . ARG   A 1 290 ? 46.678 -24.719 14.891  1.00 36.25 ? 812  ARG   A NH2 1 
ATOM   2288 N  N   . ASP   A 1 291 ? 39.710 -23.976 10.814  1.00 25.19 ? 813  ASP   A N   1 
ATOM   2289 C  CA  . ASP   A 1 291 ? 38.655 -24.707 11.517  1.00 23.58 ? 813  ASP   A CA  1 
ATOM   2290 C  C   . ASP   A 1 291 ? 39.140 -25.347 12.813  1.00 25.28 ? 813  ASP   A C   1 
ATOM   2291 O  O   . ASP   A 1 291 ? 38.545 -26.306 13.284  1.00 29.01 ? 813  ASP   A O   1 
ATOM   2292 C  CB  . ASP   A 1 291 ? 37.999 -25.755 10.613  1.00 22.84 ? 813  ASP   A CB  1 
ATOM   2293 C  CG  . ASP   A 1 291 ? 37.521 -25.159 9.304   1.00 35.62 ? 813  ASP   A CG  1 
ATOM   2294 O  OD1 . ASP   A 1 291 ? 36.804 -24.139 9.339   1.00 25.25 ? 813  ASP   A OD1 1 
ATOM   2295 O  OD2 . ASP   A 1 291 ? 37.873 -25.690 8.242   1.00 30.39 ? 813  ASP   A OD2 1 
ATOM   2296 N  N   . GLU   A 1 292 ? 40.204 -24.826 13.413  1.00 22.54 ? 814  GLU   A N   1 
ATOM   2297 C  CA  . GLU   A 1 292 ? 40.514 -25.204 14.788  1.00 27.21 ? 814  GLU   A CA  1 
ATOM   2298 C  C   . GLU   A 1 292 ? 39.490 -24.646 15.759  1.00 34.04 ? 814  GLU   A C   1 
ATOM   2299 O  O   . GLU   A 1 292 ? 39.233 -25.255 16.801  1.00 26.96 ? 814  GLU   A O   1 
ATOM   2300 C  CB  . GLU   A 1 292 ? 41.897 -24.708 15.195  1.00 32.10 ? 814  GLU   A CB  1 
ATOM   2301 C  CG  . GLU   A 1 292 ? 42.281 -25.157 16.607  1.00 39.87 ? 814  GLU   A CG  1 
ATOM   2302 C  CD  . GLU   A 1 292 ? 43.497 -24.444 17.122  1.00 46.26 ? 814  GLU   A CD  1 
ATOM   2303 O  OE1 . GLU   A 1 292 ? 44.362 -24.103 16.287  1.00 40.77 ? 814  GLU   A OE1 1 
ATOM   2304 O  OE2 . GLU   A 1 292 ? 43.577 -24.209 18.348  1.00 49.53 ? 814  GLU   A OE2 1 
ATOM   2305 N  N   . ILE   A 1 293 ? 38.939 -23.470 15.472  1.00 25.54 ? 815  ILE   A N   1 
ATOM   2306 C  CA  . ILE   A 1 293 ? 37.792 -22.959 16.209  1.00 25.65 ? 815  ILE   A CA  1 
ATOM   2307 C  C   . ILE   A 1 293 ? 36.606 -22.913 15.257  1.00 25.23 ? 815  ILE   A C   1 
ATOM   2308 O  O   . ILE   A 1 293 ? 36.752 -22.631 14.062  1.00 22.11 ? 815  ILE   A O   1 
ATOM   2309 C  CB  . ILE   A 1 293 ? 38.049 -21.578 16.854  1.00 27.43 ? 815  ILE   A CB  1 
ATOM   2310 C  CG1 . ILE   A 1 293 ? 38.268 -20.493 15.817  1.00 36.51 ? 815  ILE   A CG1 1 
ATOM   2311 C  CG2 . ILE   A 1 293 ? 39.243 -21.616 17.810  1.00 30.22 ? 815  ILE   A CG2 1 
ATOM   2312 C  CD1 . ILE   A 1 293 ? 38.427 -19.099 16.430  1.00 37.19 ? 815  ILE   A CD1 1 
ATOM   2313 N  N   . GLN   A 1 294 ? 35.445 -23.255 15.776  1.00 20.74 ? 816  GLN   A N   1 
ATOM   2314 C  CA  . GLN   A 1 294 ? 34.252 -23.288 14.948  1.00 17.37 ? 816  GLN   A CA  1 
ATOM   2315 C  C   . GLN   A 1 294 ? 33.491 -21.979 14.981  1.00 20.70 ? 816  GLN   A C   1 
ATOM   2316 O  O   . GLN   A 1 294 ? 32.729 -21.690 14.049  1.00 21.39 ? 816  GLN   A O   1 
ATOM   2317 C  CB  . GLN   A 1 294 ? 33.342 -24.414 15.423  1.00 23.07 ? 816  GLN   A CB  1 
ATOM   2318 C  CG  . GLN   A 1 294 ? 32.263 -24.792 14.443  1.00 29.99 ? 816  GLN   A CG  1 
ATOM   2319 C  CD  . GLN   A 1 294 ? 31.584 -26.089 14.828  1.00 44.74 ? 816  GLN   A CD  1 
ATOM   2320 O  OE1 . GLN   A 1 294 ? 31.584 -26.489 16.000  1.00 44.51 ? 816  GLN   A OE1 1 
ATOM   2321 N  NE2 . GLN   A 1 294 ? 31.016 -26.767 13.838  1.00 44.68 ? 816  GLN   A NE2 1 
ATOM   2322 N  N   . CYS   A 1 295 ? 33.662 -21.188 16.031  1.00 18.34 ? 817  CYS   A N   1 
ATOM   2323 C  CA  . CYS   A 1 295 ? 32.823 -20.016 16.220  1.00 18.62 ? 817  CYS   A CA  1 
ATOM   2324 C  C   . CYS   A 1 295 ? 33.663 -18.855 16.726  1.00 21.80 ? 817  CYS   A C   1 
ATOM   2325 O  O   . CYS   A 1 295 ? 34.405 -18.993 17.706  1.00 23.97 ? 817  CYS   A O   1 
ATOM   2326 C  CB  . CYS   A 1 295 ? 31.689 -20.318 17.200  1.00 21.37 ? 817  CYS   A CB  1 
ATOM   2327 S  SG  . CYS   A 1 295 ? 30.655 -18.842 17.558  1.00 23.68 ? 817  CYS   A SG  1 
ATOM   2328 N  N   . VAL   A 1 296 ? 33.566 -17.718 16.048  1.00 19.29 ? 818  VAL   A N   1 
ATOM   2329 C  CA  . VAL   A 1 296 ? 34.203 -16.492 16.513  1.00 17.35 ? 818  VAL   A CA  1 
ATOM   2330 C  C   . VAL   A 1 296 ? 33.105 -15.598 17.067  1.00 22.26 ? 818  VAL   A C   1 
ATOM   2331 O  O   . VAL   A 1 296 ? 32.113 -15.326 16.378  1.00 25.03 ? 818  VAL   A O   1 
ATOM   2332 C  CB  . VAL   A 1 296 ? 34.992 -15.787 15.397  1.00 19.48 ? 818  VAL   A CB  1 
ATOM   2333 C  CG1 . VAL   A 1 296 ? 35.451 -14.388 15.858  1.00 21.50 ? 818  VAL   A CG1 1 
ATOM   2334 C  CG2 . VAL   A 1 296 ? 36.191 -16.624 14.998  1.00 20.70 ? 818  VAL   A CG2 1 
ATOM   2335 N  N   . ILE   A 1 297 ? 33.262 -15.163 18.309  1.00 17.95 ? 819  ILE   A N   1 
ATOM   2336 C  CA  . ILE   A 1 297 ? 32.344 -14.205 18.922  1.00 17.74 ? 819  ILE   A CA  1 
ATOM   2337 C  C   . ILE   A 1 297 ? 33.052 -12.855 18.933  1.00 22.54 ? 819  ILE   A C   1 
ATOM   2338 O  O   . ILE   A 1 297 ? 34.110 -12.698 19.559  1.00 24.60 ? 819  ILE   A O   1 
ATOM   2339 C  CB  . ILE   A 1 297 ? 31.935 -14.630 20.336  1.00 18.51 ? 819  ILE   A CB  1 
ATOM   2340 C  CG1 . ILE   A 1 297 ? 31.347 -16.048 20.347  1.00 21.22 ? 819  ILE   A CG1 1 
ATOM   2341 C  CG2 . ILE   A 1 297 ? 30.901 -13.624 20.914  1.00 21.36 ? 819  ILE   A CG2 1 
ATOM   2342 C  CD1 . ILE   A 1 297 ? 32.386 -17.173 20.508  1.00 23.47 ? 819  ILE   A CD1 1 
ATOM   2343 N  N   . ALA   A 1 298 ? 32.470 -11.872 18.259  1.00 17.34 ? 820  ALA   A N   1 
ATOM   2344 C  CA  . ALA   A 1 298 ? 33.194 -10.670 17.861  1.00 18.52 ? 820  ALA   A CA  1 
ATOM   2345 C  C   . ALA   A 1 298 ? 32.422 -9.418  18.222  1.00 25.15 ? 820  ALA   A C   1 
ATOM   2346 O  O   . ALA   A 1 298 ? 31.188 -9.387  18.104  1.00 22.65 ? 820  ALA   A O   1 
ATOM   2347 C  CB  . ALA   A 1 298 ? 33.437 -10.664 16.356  1.00 19.41 ? 820  ALA   A CB  1 
ATOM   2348 N  N   . THR   A 1 299 ? 33.154 -8.338  18.500  1.00 21.13 ? 821  THR   A N   1 
ATOM   2349 C  CA  . THR   A 1 299 ? 32.507 -7.012  18.684  1.00 20.03 ? 821  THR   A CA  1 
ATOM   2350 C  C   . THR   A 1 299 ? 33.069 -6.051  17.633  1.00 32.59 ? 821  THR   A C   1 
ATOM   2351 O  O   . THR   A 1 299 ? 32.567 -4.922  17.549  1.00 47.32 ? 821  THR   A O   1 
ATOM   2352 C  CB  . THR   A 1 299 ? 32.727 -6.419  20.078  1.00 25.86 ? 821  THR   A CB  1 
ATOM   2353 O  OG1 . THR   A 1 299 ? 34.105 -6.063  20.194  1.00 39.55 ? 821  THR   A OG1 1 
ATOM   2354 C  CG2 . THR   A 1 299 ? 32.328 -7.364  21.186  1.00 24.51 ? 821  THR   A CG2 1 
ATOM   2355 N  N   . ILE   A 1 300 ? 34.038 -6.483  16.848  1.00 30.39 ? 822  ILE   A N   1 
ATOM   2356 C  CA  . ILE   A 1 300 ? 34.727 -5.586  15.875  1.00 36.22 ? 822  ILE   A CA  1 
ATOM   2357 C  C   . ILE   A 1 300 ? 33.758 -5.080  14.802  1.00 34.58 ? 822  ILE   A C   1 
ATOM   2358 O  O   . ILE   A 1 300 ? 33.086 -5.890  14.158  1.00 32.70 ? 822  ILE   A O   1 
ATOM   2359 C  CB  . ILE   A 1 300 ? 35.945 -6.301  15.255  1.00 36.65 ? 822  ILE   A CB  1 
ATOM   2360 C  CG1 . ILE   A 1 300 ? 37.038 -5.322  14.822  1.00 41.48 ? 822  ILE   A CG1 1 
ATOM   2361 C  CG2 . ILE   A 1 300 ? 35.521 -7.229  14.127  1.00 41.79 ? 822  ILE   A CG2 1 
ATOM   2362 C  CD1 . ILE   A 1 300 ? 38.139 -5.158  15.848  1.00 35.80 ? 822  ILE   A CD1 1 
ATOM   2363 N  N   . ALA   A 1 301 ? 33.753 -3.762  14.597  1.00 37.29 ? 823  ALA   A N   1 
ATOM   2364 C  CA  . ALA   A 1 301 ? 32.843 -3.147  13.610  1.00 34.44 ? 823  ALA   A CA  1 
ATOM   2365 C  C   . ALA   A 1 301 ? 33.047 -3.724  12.210  1.00 38.89 ? 823  ALA   A C   1 
ATOM   2366 O  O   . ALA   A 1 301 ? 34.203 -3.887  11.813  1.00 30.97 ? 823  ALA   A O   1 
ATOM   2367 C  CB  . ALA   A 1 301 ? 33.068 -1.662  13.583  1.00 40.68 ? 823  ALA   A CB  1 
ATOM   2368 N  N   . PHE   A 1 302 ? 31.945 -4.009  11.520  1.00 27.78 ? 824  PHE   A N   1 
ATOM   2369 C  CA  . PHE   A 1 302 ? 32.028 -4.447  10.110  1.00 29.39 ? 824  PHE   A CA  1 
ATOM   2370 C  C   . PHE   A 1 302 ? 32.620 -5.845  9.994   1.00 26.28 ? 824  PHE   A C   1 
ATOM   2371 O  O   . PHE   A 1 302 ? 32.758 -6.328  8.873   1.00 29.07 ? 824  PHE   A O   1 
ATOM   2372 C  CB  . PHE   A 1 302 ? 32.880 -3.448  9.333   1.00 25.71 ? 824  PHE   A CB  1 
ATOM   2373 C  CG  . PHE   A 1 302 ? 32.517 -2.006  9.576   1.00 30.89 ? 824  PHE   A CG  1 
ATOM   2374 C  CD1 . PHE   A 1 302 ? 31.247 -1.654  9.999   1.00 30.62 ? 824  PHE   A CD1 1 
ATOM   2375 C  CD2 . PHE   A 1 302 ? 33.453 -1.001  9.403   1.00 34.81 ? 824  PHE   A CD2 1 
ATOM   2376 C  CE1 . PHE   A 1 302 ? 30.919 -0.329  10.234  1.00 35.73 ? 824  PHE   A CE1 1 
ATOM   2377 C  CE2 . PHE   A 1 302 ? 33.123 0.324   9.636   1.00 32.61 ? 824  PHE   A CE2 1 
ATOM   2378 C  CZ  . PHE   A 1 302 ? 31.857 0.657   10.052  1.00 36.51 ? 824  PHE   A CZ  1 
ATOM   2379 N  N   . GLY   A 1 303 ? 32.907 -6.484  11.127  1.00 26.88 ? 825  GLY   A N   1 
ATOM   2380 C  CA  . GLY   A 1 303 ? 33.600 -7.744  10.981  1.00 27.39 ? 825  GLY   A CA  1 
ATOM   2381 C  C   . GLY   A 1 303 ? 34.992 -7.588  10.404  1.00 37.32 ? 825  GLY   A C   1 
ATOM   2382 O  O   . GLY   A 1 303 ? 35.537 -8.550  9.852   1.00 33.21 ? 825  GLY   A O   1 
ATOM   2383 N  N   . MET   A 1 304 ? 35.586 -6.394  10.517  1.00 27.45 ? 826  MET   A N   1 
ATOM   2384 C  CA  . MET   A 1 304 ? 36.866 -6.138  9.864   1.00 30.29 ? 826  MET   A CA  1 
ATOM   2385 C  C   . MET   A 1 304 ? 37.886 -7.190  10.247  1.00 29.00 ? 826  MET   A C   1 
ATOM   2386 O  O   . MET   A 1 304 ? 38.078 -7.492  11.425  1.00 25.74 ? 826  MET   A O   1 
ATOM   2387 C  CB  . MET   A 1 304 ? 37.393 -4.753  10.226  1.00 35.43 ? 826  MET   A CB  1 
ATOM   2388 C  CG  . MET   A 1 304 ? 36.655 -3.623  9.520   1.00 46.78 ? 826  MET   A CG  1 
ATOM   2389 S  SD  . MET   A 1 304 ? 36.589 -3.857  7.726   1.00 64.91 ? 826  MET   A SD  1 
ATOM   2390 C  CE  . MET   A 1 304 ? 38.313 -4.147  7.327   1.00 40.83 ? 826  MET   A CE  1 
ATOM   2391 N  N   . GLY   A 1 305 ? 38.512 -7.772  9.237   1.00 27.22 ? 827  GLY   A N   1 
ATOM   2392 C  CA  . GLY   A 1 305 ? 39.533 -8.755  9.471   1.00 34.44 ? 827  GLY   A CA  1 
ATOM   2393 C  C   . GLY   A 1 305 ? 39.058 -10.187 9.540   1.00 35.20 ? 827  GLY   A C   1 
ATOM   2394 O  O   . GLY   A 1 305 ? 39.906 -11.087 9.508   1.00 30.44 ? 827  GLY   A O   1 
ATOM   2395 N  N   . ILE   A 1 306 ? 37.749 -10.450 9.609   1.00 30.08 ? 828  ILE   A N   1 
ATOM   2396 C  CA  . ILE   A 1 306 ? 37.266 -11.843 9.647   1.00 24.32 ? 828  ILE   A CA  1 
ATOM   2397 C  C   . ILE   A 1 306 ? 36.950 -12.259 8.215   1.00 26.87 ? 828  ILE   A C   1 
ATOM   2398 O  O   . ILE   A 1 306 ? 35.816 -12.129 7.721   1.00 25.68 ? 828  ILE   A O   1 
ATOM   2399 C  CB  . ILE   A 1 306 ? 36.076 -12.031 10.578  1.00 25.44 ? 828  ILE   A CB  1 
ATOM   2400 C  CG1 . ILE   A 1 306 ? 36.369 -11.432 11.936  1.00 23.81 ? 828  ILE   A CG1 1 
ATOM   2401 C  CG2 . ILE   A 1 306 ? 35.810 -13.497 10.754  1.00 30.19 ? 828  ILE   A CG2 1 
ATOM   2402 C  CD1 . ILE   A 1 306 ? 35.283 -11.683 12.930  1.00 33.87 ? 828  ILE   A CD1 1 
ATOM   2403 N  N   . ASN   A 1 307 ? 37.949 -12.840 7.571   1.00 18.69 ? 829  ASN   A N   1 
ATOM   2404 C  CA  . ASN   A 1 307 ? 37.928 -13.199 6.162   1.00 16.96 ? 829  ASN   A CA  1 
ATOM   2405 C  C   . ASN   A 1 307 ? 38.042 -14.714 6.059   1.00 21.10 ? 829  ASN   A C   1 
ATOM   2406 O  O   . ASN   A 1 307 ? 39.123 -15.270 6.270   1.00 19.61 ? 829  ASN   A O   1 
ATOM   2407 C  CB  . ASN   A 1 307 ? 39.092 -12.501 5.449   1.00 19.94 ? 829  ASN   A CB  1 
ATOM   2408 C  CG  . ASN   A 1 307 ? 38.896 -11.007 5.372   1.00 26.99 ? 829  ASN   A CG  1 
ATOM   2409 O  OD1 . ASN   A 1 307 ? 37.855 -10.556 4.933   1.00 24.11 ? 829  ASN   A OD1 1 
ATOM   2410 N  ND2 . ASN   A 1 307 ? 39.884 -10.232 5.826   1.00 26.04 ? 829  ASN   A ND2 1 
ATOM   2411 N  N   . LYS   A 1 308 ? 36.948 -15.377 5.712   1.00 17.18 ? 830  LYS   A N   1 
ATOM   2412 C  CA  . LYS   A 1 308 ? 36.943 -16.831 5.618   1.00 18.42 ? 830  LYS   A CA  1 
ATOM   2413 C  C   . LYS   A 1 308 ? 35.937 -17.229 4.553   1.00 20.08 ? 830  LYS   A C   1 
ATOM   2414 O  O   . LYS   A 1 308 ? 34.871 -16.618 4.452   1.00 20.94 ? 830  LYS   A O   1 
ATOM   2415 C  CB  . LYS   A 1 308 ? 36.605 -17.456 6.982   1.00 19.36 ? 830  LYS   A CB  1 
ATOM   2416 C  CG  . LYS   A 1 308 ? 36.472 -18.967 6.984   1.00 17.91 ? 830  LYS   A CG  1 
ATOM   2417 C  CD  . LYS   A 1 308 ? 36.397 -19.485 8.427   1.00 18.55 ? 830  LYS   A CD  1 
ATOM   2418 C  CE  . LYS   A 1 308 ? 35.953 -20.947 8.496   1.00 20.65 ? 830  LYS   A CE  1 
ATOM   2419 N  NZ  . LYS   A 1 308 ? 36.890 -21.924 7.823   1.00 18.61 ? 830  LYS   A NZ  1 
ATOM   2420 N  N   . ALA   A 1 309 ? 36.291 -18.220 3.730   1.00 17.36 ? 831  ALA   A N   1 
ATOM   2421 C  CA  . ALA   A 1 309 ? 35.467 -18.492 2.556   1.00 17.19 ? 831  ALA   A CA  1 
ATOM   2422 C  C   . ALA   A 1 309 ? 34.150 -19.179 2.904   1.00 24.01 ? 831  ALA   A C   1 
ATOM   2423 O  O   . ALA   A 1 309 ? 33.138 -18.967 2.220   1.00 18.20 ? 831  ALA   A O   1 
ATOM   2424 C  CB  . ALA   A 1 309 ? 36.243 -19.353 1.572   1.00 19.02 ? 831  ALA   A CB  1 
ATOM   2425 N  N   . ASP   A 1 310 ? 34.149 -20.011 3.941   1.00 17.10 ? 832  ASP   A N   1 
ATOM   2426 C  CA  . ASP   A 1 310 ? 33.043 -20.922 4.198   1.00 17.38 ? 832  ASP   A CA  1 
ATOM   2427 C  C   . ASP   A 1 310 ? 32.351 -20.612 5.518   1.00 19.55 ? 832  ASP   A C   1 
ATOM   2428 O  O   . ASP   A 1 310 ? 32.145 -21.506 6.345   1.00 19.62 ? 832  ASP   A O   1 
ATOM   2429 C  CB  . ASP   A 1 310 ? 33.554 -22.378 4.161   1.00 17.04 ? 832  ASP   A CB  1 
ATOM   2430 C  CG  . ASP   A 1 310 ? 34.684 -22.642 5.153   1.00 23.21 ? 832  ASP   A CG  1 
ATOM   2431 O  OD1 . ASP   A 1 310 ? 35.464 -21.728 5.501   1.00 23.24 ? 832  ASP   A OD1 1 
ATOM   2432 O  OD2 . ASP   A 1 310 ? 34.813 -23.802 5.573   1.00 23.67 ? 832  ASP   A OD2 1 
ATOM   2433 N  N   . ILE   A 1 311 ? 31.973 -19.351 5.732   1.00 14.84 ? 833  ILE   A N   1 
ATOM   2434 C  CA  . ILE   A 1 311 ? 31.188 -19.013 6.911   1.00 14.26 ? 833  ILE   A CA  1 
ATOM   2435 C  C   . ILE   A 1 311 ? 29.736 -19.354 6.598   1.00 15.85 ? 833  ILE   A C   1 
ATOM   2436 O  O   . ILE   A 1 311 ? 29.113 -18.750 5.719   1.00 16.13 ? 833  ILE   A O   1 
ATOM   2437 C  CB  . ILE   A 1 311 ? 31.345 -17.542 7.311   1.00 16.15 ? 833  ILE   A CB  1 
ATOM   2438 C  CG1 . ILE   A 1 311 ? 32.769 -17.291 7.807   1.00 18.09 ? 833  ILE   A CG1 1 
ATOM   2439 C  CG2 . ILE   A 1 311 ? 30.372 -17.197 8.437   1.00 15.69 ? 833  ILE   A CG2 1 
ATOM   2440 C  CD1 . ILE   A 1 311 ? 33.047 -15.829 8.099   1.00 17.89 ? 833  ILE   A CD1 1 
ATOM   2441 N  N   . ARG   A 1 312 ? 29.204 -20.341 7.300   1.00 14.60 ? 834  ARG   A N   1 
ATOM   2442 C  CA  . ARG   A 1 312 ? 27.874 -20.859 7.011   1.00 15.71 ? 834  ARG   A CA  1 
ATOM   2443 C  C   . ARG   A 1 312 ? 26.786 -20.137 7.784   1.00 14.19 ? 834  ARG   A C   1 
ATOM   2444 O  O   . ARG   A 1 312 ? 25.624 -20.165 7.363   1.00 16.17 ? 834  ARG   A O   1 
ATOM   2445 C  CB  . ARG   A 1 312 ? 27.799 -22.364 7.345   1.00 20.19 ? 834  ARG   A CB  1 
ATOM   2446 C  CG  . ARG   A 1 312 ? 28.648 -23.298 6.433   1.00 16.66 ? 834  ARG   A CG  1 
ATOM   2447 C  CD  . ARG   A 1 312 ? 27.941 -23.574 5.096   1.00 17.04 ? 834  ARG   A CD  1 
ATOM   2448 N  NE  . ARG   A 1 312 ? 27.915 -22.418 4.209   1.00 17.04 ? 834  ARG   A NE  1 
ATOM   2449 C  CZ  . ARG   A 1 312 ? 28.891 -22.088 3.374   1.00 18.98 ? 834  ARG   A CZ  1 
ATOM   2450 N  NH1 . ARG   A 1 312 ? 30.000 -22.792 3.301   1.00 16.99 ? 834  ARG   A NH1 1 
ATOM   2451 N  NH2 . ARG   A 1 312 ? 28.744 -21.027 2.581   1.00 14.27 ? 834  ARG   A NH2 1 
ATOM   2452 N  N   . GLN   A 1 313 ? 27.121 -19.541 8.921   1.00 15.66 ? 835  GLN   A N   1 
ATOM   2453 C  CA  . GLN   A 1 313 ? 26.154 -18.887 9.792   1.00 14.97 ? 835  GLN   A CA  1 
ATOM   2454 C  C   . GLN   A 1 313 ? 26.719 -17.595 10.377  1.00 18.90 ? 835  GLN   A C   1 
ATOM   2455 O  O   . GLN   A 1 313 ? 27.842 -17.565 10.908  1.00 15.49 ? 835  GLN   A O   1 
ATOM   2456 C  CB  . GLN   A 1 313 ? 25.752 -19.824 10.935  1.00 17.58 ? 835  GLN   A CB  1 
ATOM   2457 C  CG  . GLN   A 1 313 ? 24.728 -19.207 11.914  1.00 21.52 ? 835  GLN   A CG  1 
ATOM   2458 C  CD  . GLN   A 1 313 ? 23.310 -19.124 11.334  1.00 23.66 ? 835  GLN   A CD  1 
ATOM   2459 O  OE1 . GLN   A 1 313 ? 22.737 -20.130 10.931  1.00 21.68 ? 835  GLN   A OE1 1 
ATOM   2460 N  NE2 . GLN   A 1 313 ? 22.738 -17.914 11.313  1.00 20.30 ? 835  GLN   A NE2 1 
ATOM   2461 N  N   . VAL   A 1 314 ? 25.945 -16.522 10.274  1.00 15.42 ? 836  VAL   A N   1 
ATOM   2462 C  CA  . VAL   A 1 314 ? 26.194 -15.286 11.011  1.00 14.15 ? 836  VAL   A CA  1 
ATOM   2463 C  C   . VAL   A 1 314 ? 25.023 -15.091 11.952  1.00 17.01 ? 836  VAL   A C   1 
ATOM   2464 O  O   . VAL   A 1 314 ? 23.867 -15.242 11.545  1.00 18.92 ? 836  VAL   A O   1 
ATOM   2465 C  CB  . VAL   A 1 314 ? 26.361 -14.076 10.076  1.00 18.09 ? 836  VAL   A CB  1 
ATOM   2466 C  CG1 . VAL   A 1 314 ? 26.225 -12.759 10.859  1.00 18.61 ? 836  VAL   A CG1 1 
ATOM   2467 C  CG2 . VAL   A 1 314 ? 27.739 -14.106 9.415   1.00 14.85 ? 836  VAL   A CG2 1 
ATOM   2468 N  N   . ILE   A 1 315 ? 25.313 -14.783 13.206  1.00 16.59 ? 837  ILE   A N   1 
ATOM   2469 C  CA  . ILE   A 1 315 ? 24.292 -14.440 14.184  1.00 17.28 ? 837  ILE   A CA  1 
ATOM   2470 C  C   . ILE   A 1 315 ? 24.634 -13.079 14.759  1.00 19.78 ? 837  ILE   A C   1 
ATOM   2471 O  O   . ILE   A 1 315 ? 25.749 -12.883 15.247  1.00 17.82 ? 837  ILE   A O   1 
ATOM   2472 C  CB  . ILE   A 1 315 ? 24.225 -15.483 15.308  1.00 16.41 ? 837  ILE   A CB  1 
ATOM   2473 C  CG1 . ILE   A 1 315 ? 24.076 -16.885 14.734  1.00 19.79 ? 837  ILE   A CG1 1 
ATOM   2474 C  CG2 . ILE   A 1 315 ? 23.097 -15.149 16.272  1.00 16.47 ? 837  ILE   A CG2 1 
ATOM   2475 C  CD1 . ILE   A 1 315 ? 24.212 -17.965 15.787  1.00 22.19 ? 837  ILE   A CD1 1 
ATOM   2476 N  N   . HIS   A 1 316 ? 23.690 -12.136 14.705  1.00 14.81 ? 838  HIS   A N   1 
ATOM   2477 C  CA  . HIS   A 1 316 ? 23.801 -10.928 15.499  1.00 16.25 ? 838  HIS   A CA  1 
ATOM   2478 C  C   . HIS   A 1 316 ? 23.105 -11.182 16.817  1.00 17.35 ? 838  HIS   A C   1 
ATOM   2479 O  O   . HIS   A 1 316 ? 21.877 -11.294 16.849  1.00 19.41 ? 838  HIS   A O   1 
ATOM   2480 C  CB  . HIS   A 1 316 ? 23.185 -9.739  14.763  1.00 14.42 ? 838  HIS   A CB  1 
ATOM   2481 C  CG  . HIS   A 1 316 ? 24.140 -9.101  13.807  1.00 14.80 ? 838  HIS   A CG  1 
ATOM   2482 N  ND1 . HIS   A 1 316 ? 24.282 -9.534  12.509  1.00 15.35 ? 838  HIS   A ND1 1 
ATOM   2483 C  CD2 . HIS   A 1 316 ? 25.007 -8.071  13.964  1.00 16.45 ? 838  HIS   A CD2 1 
ATOM   2484 C  CE1 . HIS   A 1 316 ? 25.193 -8.789  11.898  1.00 16.07 ? 838  HIS   A CE1 1 
ATOM   2485 N  NE2 . HIS   A 1 316 ? 25.656 -7.897  12.761  1.00 15.69 ? 838  HIS   A NE2 1 
ATOM   2486 N  N   . TYR   A 1 317 ? 23.871 -11.291 17.908  1.00 14.65 ? 839  TYR   A N   1 
ATOM   2487 C  CA  . TYR   A 1 317 ? 23.248 -11.525 19.210  1.00 17.11 ? 839  TYR   A CA  1 
ATOM   2488 C  C   . TYR   A 1 317 ? 23.041 -10.163 19.843  1.00 22.04 ? 839  TYR   A C   1 
ATOM   2489 O  O   . TYR   A 1 317 ? 23.923 -9.622  20.512  1.00 18.12 ? 839  TYR   A O   1 
ATOM   2490 C  CB  . TYR   A 1 317 ? 24.061 -12.456 20.106  1.00 20.50 ? 839  TYR   A CB  1 
ATOM   2491 C  CG  . TYR   A 1 317 ? 23.221 -12.919 21.263  1.00 20.68 ? 839  TYR   A CG  1 
ATOM   2492 C  CD1 . TYR   A 1 317 ? 22.170 -13.819 21.055  1.00 25.30 ? 839  TYR   A CD1 1 
ATOM   2493 C  CD2 . TYR   A 1 317 ? 23.406 -12.410 22.541  1.00 22.65 ? 839  TYR   A CD2 1 
ATOM   2494 C  CE1 . TYR   A 1 317 ? 21.350 -14.219 22.088  1.00 22.02 ? 839  TYR   A CE1 1 
ATOM   2495 C  CE2 . TYR   A 1 317 ? 22.590 -12.822 23.593  1.00 20.44 ? 839  TYR   A CE2 1 
ATOM   2496 C  CZ  . TYR   A 1 317 ? 21.573 -13.721 23.351  1.00 25.68 ? 839  TYR   A CZ  1 
ATOM   2497 O  OH  . TYR   A 1 317 ? 20.761 -14.123 24.369  1.00 29.73 ? 839  TYR   A OH  1 
ATOM   2498 N  N   . GLY   A 1 318 ? 21.850 -9.619  19.634  1.00 17.47 ? 840  GLY   A N   1 
ATOM   2499 C  CA  . GLY   A 1 318 ? 21.503 -8.250  19.942  1.00 18.30 ? 840  GLY   A CA  1 
ATOM   2500 C  C   . GLY   A 1 318 ? 21.354 -7.433  18.674  1.00 19.69 ? 840  GLY   A C   1 
ATOM   2501 O  O   . GLY   A 1 318 ? 22.007 -7.692  17.652  1.00 17.22 ? 840  GLY   A O   1 
ATOM   2502 N  N   . ALA   A 1 319 ? 20.482 -6.431  18.733  1.00 16.33 ? 841  ALA   A N   1 
ATOM   2503 C  CA  . ALA   A 1 319 ? 20.288 -5.556  17.588  1.00 14.69 ? 841  ALA   A CA  1 
ATOM   2504 C  C   . ALA   A 1 319 ? 21.633 -5.035  17.086  1.00 14.34 ? 841  ALA   A C   1 
ATOM   2505 O  O   . ALA   A 1 319 ? 22.469 -4.617  17.890  1.00 17.58 ? 841  ALA   A O   1 
ATOM   2506 C  CB  . ALA   A 1 319 ? 19.403 -4.369  17.977  1.00 11.63 ? 841  ALA   A CB  1 
ATOM   2507 N  N   . PRO   A 1 320 ? 21.864 -5.027  15.777  1.00 16.74 ? 842  PRO   A N   1 
ATOM   2508 C  CA  . PRO   A 1 320 ? 23.079 -4.414  15.234  1.00 19.21 ? 842  PRO   A CA  1 
ATOM   2509 C  C   . PRO   A 1 320 ? 23.062 -2.909  15.443  1.00 17.60 ? 842  PRO   A C   1 
ATOM   2510 O  O   . PRO   A 1 320 ? 22.036 -2.305  15.764  1.00 17.42 ? 842  PRO   A O   1 
ATOM   2511 C  CB  . PRO   A 1 320 ? 23.035 -4.751  13.737  1.00 17.30 ? 842  PRO   A CB  1 
ATOM   2512 C  CG  . PRO   A 1 320 ? 21.896 -5.755  13.585  1.00 17.18 ? 842  PRO   A CG  1 
ATOM   2513 C  CD  . PRO   A 1 320 ? 20.947 -5.463  14.717  1.00 16.79 ? 842  PRO   A CD  1 
ATOM   2514 N  N   . LYS   A 1 321 ? 24.222 -2.307  15.210  1.00 17.25 ? 843  LYS   A N   1 
ATOM   2515 C  CA  . LYS   A 1 321 ? 24.399 -0.877  15.467  1.00 16.68 ? 843  LYS   A CA  1 
ATOM   2516 C  C   . LYS   A 1 321 ? 23.583 -0.034  14.496  1.00 20.03 ? 843  LYS   A C   1 
ATOM   2517 O  O   . LYS   A 1 321 ? 22.892 0.906   14.906  1.00 18.38 ? 843  LYS   A O   1 
ATOM   2518 C  CB  . LYS   A 1 321 ? 25.884 -0.517  15.387  1.00 18.92 ? 843  LYS   A CB  1 
ATOM   2519 C  CG  . LYS   A 1 321 ? 26.195 0.839   15.972  1.00 22.70 ? 843  LYS   A CG  1 
ATOM   2520 C  CD  . LYS   A 1 321 ? 27.665 1.156   15.906  1.00 32.92 ? 843  LYS   A CD  1 
ATOM   2521 C  CE  . LYS   A 1 321 ? 27.971 1.968   14.662  1.00 40.15 ? 843  LYS   A CE  1 
ATOM   2522 N  NZ  . LYS   A 1 321 ? 29.129 2.887   14.870  1.00 47.22 ? 843  LYS   A NZ  1 
ATOM   2523 N  N   . ASP   A 1 322 ? 23.643 -0.347  13.210  1.00 17.53 ? 844  ASP   A N   1 
ATOM   2524 C  CA  . ASP   A 1 322 ? 22.856 0.365   12.202  1.00 17.79 ? 844  ASP   A CA  1 
ATOM   2525 C  C   . ASP   A 1 322 ? 22.912 -0.446  10.921  1.00 18.51 ? 844  ASP   A C   1 
ATOM   2526 O  O   . ASP   A 1 322 ? 23.597 -1.474  10.844  1.00 17.69 ? 844  ASP   A O   1 
ATOM   2527 C  CB  . ASP   A 1 322 ? 23.351 1.809   11.983  1.00 16.98 ? 844  ASP   A CB  1 
ATOM   2528 C  CG  . ASP   A 1 322 ? 24.823 1.884   11.623  1.00 22.73 ? 844  ASP   A CG  1 
ATOM   2529 O  OD1 . ASP   A 1 322 ? 25.280 1.196   10.683  1.00 23.42 ? 844  ASP   A OD1 1 
ATOM   2530 O  OD2 . ASP   A 1 322 ? 25.542 2.655   12.286  1.00 28.85 ? 844  ASP   A OD2 1 
ATOM   2531 N  N   . MET   A 1 323 ? 22.159 -0.002  9.913   1.00 17.20 ? 845  MET   A N   1 
ATOM   2532 C  CA  . MET   A 1 323 ? 22.066 -0.804  8.698   1.00 18.73 ? 845  MET   A CA  1 
ATOM   2533 C  C   . MET   A 1 323 ? 23.416 -0.923  7.985   1.00 17.35 ? 845  MET   A C   1 
ATOM   2534 O  O   . MET   A 1 323 ? 23.696 -1.956  7.364   1.00 14.79 ? 845  MET   A O   1 
ATOM   2535 C  CB  . MET   A 1 323 ? 21.003 -0.225  7.758   1.00 16.03 ? 845  MET   A CB  1 
ATOM   2536 C  CG  . MET   A 1 323 ? 19.574 -0.360  8.293   1.00 17.74 ? 845  MET   A CG  1 
ATOM   2537 S  SD  . MET   A 1 323 ? 19.015 -2.067  8.346   1.00 24.22 ? 845  MET   A SD  1 
ATOM   2538 C  CE  . MET   A 1 323 ? 18.791 -2.373  6.615   1.00 23.20 ? 845  MET   A CE  1 
ATOM   2539 N  N   . GLU   A 1 324 ? 24.273 0.100   8.058   1.00 16.54 ? 846  GLU   A N   1 
ATOM   2540 C  CA  . GLU   A 1 324 ? 25.566 -0.023  7.381   1.00 12.95 ? 846  GLU   A CA  1 
ATOM   2541 C  C   . GLU   A 1 324 ? 26.445 -1.063  8.054   1.00 17.08 ? 846  GLU   A C   1 
ATOM   2542 O  O   . GLU   A 1 324 ? 27.093 -1.879  7.381   1.00 17.68 ? 846  GLU   A O   1 
ATOM   2543 C  CB  . GLU   A 1 324 ? 26.290 1.328   7.343   1.00 19.11 ? 846  GLU   A CB  1 
ATOM   2544 C  CG  . GLU   A 1 324 ? 25.602 2.287   6.415   1.00 21.73 ? 846  GLU   A CG  1 
ATOM   2545 C  CD  . GLU   A 1 324 ? 26.418 3.527   6.136   1.00 29.54 ? 846  GLU   A CD  1 
ATOM   2546 O  OE1 . GLU   A 1 324 ? 27.623 3.543   6.476   1.00 23.78 ? 846  GLU   A OE1 1 
ATOM   2547 O  OE2 . GLU   A 1 324 ? 25.851 4.476   5.555   1.00 29.21 ? 846  GLU   A OE2 1 
ATOM   2548 N  N   . SER   A 1 325 ? 26.509 -1.042  9.377   1.00 16.87 ? 847  SER   A N   1 
ATOM   2549 C  CA  . SER   A 1 325 ? 27.331 -2.058  10.026  1.00 16.83 ? 847  SER   A CA  1 
ATOM   2550 C  C   . SER   A 1 325 ? 26.733 -3.448  9.815   1.00 17.60 ? 847  SER   A C   1 
ATOM   2551 O  O   . SER   A 1 325 ? 27.464 -4.403  9.528   1.00 18.66 ? 847  SER   A O   1 
ATOM   2552 C  CB  . SER   A 1 325 ? 27.512 -1.730  11.510  1.00 23.25 ? 847  SER   A CB  1 
ATOM   2553 O  OG  . SER   A 1 325 ? 26.281 -1.633  12.179  1.00 39.51 ? 847  SER   A OG  1 
ATOM   2554 N  N   . TYR   A 1 326 ? 25.413 -3.565  9.903   1.00 14.63 ? 848  TYR   A N   1 
ATOM   2555 C  CA  . TYR   A 1 326 ? 24.745 -4.842  9.651   1.00 13.99 ? 848  TYR   A CA  1 
ATOM   2556 C  C   . TYR   A 1 326 ? 25.085 -5.386  8.272   1.00 16.70 ? 848  TYR   A C   1 
ATOM   2557 O  O   . TYR   A 1 326 ? 25.436 -6.561  8.123   1.00 18.59 ? 848  TYR   A O   1 
ATOM   2558 C  CB  . TYR   A 1 326 ? 23.248 -4.634  9.786   1.00 17.97 ? 848  TYR   A CB  1 
ATOM   2559 C  CG  . TYR   A 1 326 ? 22.372 -5.805  9.438   1.00 16.86 ? 848  TYR   A CG  1 
ATOM   2560 C  CD1 . TYR   A 1 326 ? 22.456 -6.995  10.140  1.00 14.86 ? 848  TYR   A CD1 1 
ATOM   2561 C  CD2 . TYR   A 1 326 ? 21.407 -5.699  8.443   1.00 16.41 ? 848  TYR   A CD2 1 
ATOM   2562 C  CE1 . TYR   A 1 326 ? 21.600 -8.051  9.842   1.00 15.75 ? 848  TYR   A CE1 1 
ATOM   2563 C  CE2 . TYR   A 1 326 ? 20.560 -6.752  8.143   1.00 16.05 ? 848  TYR   A CE2 1 
ATOM   2564 C  CZ  . TYR   A 1 326 ? 20.686 -7.931  8.842   1.00 16.76 ? 848  TYR   A CZ  1 
ATOM   2565 O  OH  . TYR   A 1 326 ? 19.839 -8.977  8.554   1.00 18.16 ? 848  TYR   A OH  1 
ATOM   2566 N  N   . TYR   A 1 327 ? 24.946 -4.549  7.245   1.00 14.65 ? 849  TYR   A N   1 
ATOM   2567 C  CA  . TYR   A 1 327 ? 25.277 -4.935  5.874   1.00 16.65 ? 849  TYR   A CA  1 
ATOM   2568 C  C   . TYR   A 1 327 ? 26.690 -5.494  5.790   1.00 17.43 ? 849  TYR   A C   1 
ATOM   2569 O  O   . TYR   A 1 327 ? 26.914 -6.588  5.246   1.00 15.29 ? 849  TYR   A O   1 
ATOM   2570 C  CB  . TYR   A 1 327 ? 25.145 -3.697  4.992   1.00 16.23 ? 849  TYR   A CB  1 
ATOM   2571 C  CG  . TYR   A 1 327 ? 25.442 -3.794  3.507   1.00 16.94 ? 849  TYR   A CG  1 
ATOM   2572 C  CD1 . TYR   A 1 327 ? 24.432 -4.097  2.595   1.00 13.29 ? 849  TYR   A CD1 1 
ATOM   2573 C  CD2 . TYR   A 1 327 ? 26.704 -3.441  3.003   1.00 15.85 ? 849  TYR   A CD2 1 
ATOM   2574 C  CE1 . TYR   A 1 327 ? 24.678 -4.098  1.224   1.00 14.09 ? 849  TYR   A CE1 1 
ATOM   2575 C  CE2 . TYR   A 1 327 ? 26.949 -3.446  1.641   1.00 17.36 ? 849  TYR   A CE2 1 
ATOM   2576 C  CZ  . TYR   A 1 327 ? 25.935 -3.784  0.763   1.00 15.82 ? 849  TYR   A CZ  1 
ATOM   2577 O  OH  . TYR   A 1 327 ? 26.174 -3.795  -0.594  1.00 18.01 ? 849  TYR   A OH  1 
ATOM   2578 N  N   . GLN   A 1 328 ? 27.658 -4.742  6.321   1.00 15.93 ? 850  GLN   A N   1 
ATOM   2579 C  CA  . GLN   A 1 328 ? 29.040 -5.217  6.246   1.00 14.37 ? 850  GLN   A CA  1 
ATOM   2580 C  C   . GLN   A 1 328 ? 29.222 -6.521  7.020   1.00 15.39 ? 850  GLN   A C   1 
ATOM   2581 O  O   . GLN   A 1 328 ? 29.959 -7.413  6.594   1.00 16.44 ? 850  GLN   A O   1 
ATOM   2582 C  CB  . GLN   A 1 328 ? 29.977 -4.124  6.757   1.00 16.99 ? 850  GLN   A CB  1 
ATOM   2583 C  CG  . GLN   A 1 328 ? 29.755 -2.824  5.970   1.00 20.50 ? 850  GLN   A CG  1 
ATOM   2584 C  CD  . GLN   A 1 328 ? 30.582 -1.659  6.467   1.00 30.42 ? 850  GLN   A CD  1 
ATOM   2585 O  OE1 . GLN   A 1 328 ? 31.795 -1.635  6.301   1.00 29.71 ? 850  GLN   A OE1 1 
ATOM   2586 N  NE2 . GLN   A 1 328 ? 29.919 -0.676  7.066   1.00 26.79 ? 850  GLN   A NE2 1 
ATOM   2587 N  N   . GLU   A 1 329 ? 28.522 -6.674  8.131   1.00 15.81 ? 851  GLU   A N   1 
ATOM   2588 C  CA  . GLU   A 1 329 ? 28.811 -7.795  9.014   1.00 15.85 ? 851  GLU   A CA  1 
ATOM   2589 C  C   . GLU   A 1 329 ? 28.207 -9.082  8.477   1.00 17.60 ? 851  GLU   A C   1 
ATOM   2590 O  O   . GLU   A 1 329 ? 28.839 -10.142 8.533   1.00 16.17 ? 851  GLU   A O   1 
ATOM   2591 C  CB  . GLU   A 1 329 ? 28.295 -7.476  10.423  1.00 18.54 ? 851  GLU   A CB  1 
ATOM   2592 C  CG  . GLU   A 1 329 ? 29.236 -6.460  11.120  1.00 19.70 ? 851  GLU   A CG  1 
ATOM   2593 C  CD  . GLU   A 1 329 ? 28.612 -5.628  12.229  1.00 22.81 ? 851  GLU   A CD  1 
ATOM   2594 O  OE1 . GLU   A 1 329 ? 27.450 -5.846  12.609  1.00 22.29 ? 851  GLU   A OE1 1 
ATOM   2595 O  OE2 . GLU   A 1 329 ? 29.307 -4.710  12.730  1.00 26.64 ? 851  GLU   A OE2 1 
ATOM   2596 N  N   . ILE   A 1 330 ? 26.986 -9.014  7.942   1.00 16.30 ? 852  ILE   A N   1 
ATOM   2597 C  CA  . ILE   A 1 330 ? 26.451 -10.228 7.329   1.00 13.79 ? 852  ILE   A CA  1 
ATOM   2598 C  C   . ILE   A 1 330 ? 27.090 -10.493 5.979   1.00 13.88 ? 852  ILE   A C   1 
ATOM   2599 O  O   . ILE   A 1 330 ? 27.100 -11.645 5.528   1.00 15.02 ? 852  ILE   A O   1 
ATOM   2600 C  CB  . ILE   A 1 330 ? 24.919 -10.204 7.149   1.00 13.63 ? 852  ILE   A CB  1 
ATOM   2601 C  CG1 . ILE   A 1 330 ? 24.510 -9.111  6.146   1.00 15.98 ? 852  ILE   A CG1 1 
ATOM   2602 C  CG2 . ILE   A 1 330 ? 24.201 -10.021 8.483   1.00 16.39 ? 852  ILE   A CG2 1 
ATOM   2603 C  CD1 . ILE   A 1 330 ? 23.003 -9.168  5.876   1.00 20.26 ? 852  ILE   A CD1 1 
ATOM   2604 N  N   . GLY   A 1 331 ? 27.648 -9.484  5.305   1.00 13.59 ? 853  GLY   A N   1 
ATOM   2605 C  CA  . GLY   A 1 331 ? 28.261 -9.829  4.025   1.00 13.46 ? 853  GLY   A CA  1 
ATOM   2606 C  C   . GLY   A 1 331 ? 29.479 -10.733 4.144   1.00 13.83 ? 853  GLY   A C   1 
ATOM   2607 O  O   . GLY   A 1 331 ? 29.938 -11.261 3.130   1.00 15.96 ? 853  GLY   A O   1 
ATOM   2608 N  N   . ARG   A 1 332 ? 30.017 -10.881 5.351   1.00 14.77 ? 854  ARG   A N   1 
ATOM   2609 C  CA  . ARG   A 1 332 ? 31.138 -11.779 5.615   1.00 15.37 ? 854  ARG   A CA  1 
ATOM   2610 C  C   . ARG   A 1 332 ? 30.766 -13.233 5.366   1.00 15.13 ? 854  ARG   A C   1 
ATOM   2611 O  O   . ARG   A 1 332 ? 31.660 -14.068 5.182   1.00 16.47 ? 854  ARG   A O   1 
ATOM   2612 C  CB  . ARG   A 1 332 ? 31.594 -11.625 7.066   1.00 15.01 ? 854  ARG   A CB  1 
ATOM   2613 C  CG  . ARG   A 1 332 ? 32.094 -10.232 7.413   1.00 19.70 ? 854  ARG   A CG  1 
ATOM   2614 C  CD  . ARG   A 1 332 ? 33.527 -10.033 6.978   1.00 19.17 ? 854  ARG   A CD  1 
ATOM   2615 N  NE  . ARG   A 1 332 ? 33.874 -8.614  7.029   1.00 23.62 ? 854  ARG   A NE  1 
ATOM   2616 C  CZ  . ARG   A 1 332 ? 35.012 -8.103  6.564   1.00 22.78 ? 854  ARG   A CZ  1 
ATOM   2617 N  NH1 . ARG   A 1 332 ? 35.964 -8.869  6.065   1.00 23.37 ? 854  ARG   A NH1 1 
ATOM   2618 N  NH2 . ARG   A 1 332 ? 35.185 -6.789  6.581   1.00 26.47 ? 854  ARG   A NH2 1 
ATOM   2619 N  N   . ALA   A 1 333 ? 29.472 -13.556 5.359   1.00 13.10 ? 855  ALA   A N   1 
ATOM   2620 C  CA  . ALA   A 1 333 ? 29.025 -14.932 5.241   1.00 15.76 ? 855  ALA   A CA  1 
ATOM   2621 C  C   . ALA   A 1 333 ? 29.053 -15.402 3.792   1.00 16.25 ? 855  ALA   A C   1 
ATOM   2622 O  O   . ALA   A 1 333 ? 28.887 -14.609 2.858   1.00 15.80 ? 855  ALA   A O   1 
ATOM   2623 C  CB  . ALA   A 1 333 ? 27.589 -15.068 5.790   1.00 13.68 ? 855  ALA   A CB  1 
ATOM   2624 N  N   . GLY   A 1 334 ? 29.152 -16.725 3.616   1.00 14.87 ? 856  GLY   A N   1 
ATOM   2625 C  CA  . GLY   A 1 334 ? 28.852 -17.346 2.327   1.00 14.75 ? 856  GLY   A CA  1 
ATOM   2626 C  C   . GLY   A 1 334 ? 29.718 -16.893 1.164   1.00 18.27 ? 856  GLY   A C   1 
ATOM   2627 O  O   . GLY   A 1 334 ? 29.246 -16.874 0.021   1.00 15.90 ? 856  GLY   A O   1 
ATOM   2628 N  N   . ARG   A 1 335 ? 30.989 -16.566 1.406   1.00 17.45 ? 857  ARG   A N   1 
ATOM   2629 C  CA  . ARG   A 1 335 ? 31.801 -16.038 0.312   1.00 16.25 ? 857  ARG   A CA  1 
ATOM   2630 C  C   . ARG   A 1 335 ? 32.109 -17.102 -0.727  1.00 18.53 ? 857  ARG   A C   1 
ATOM   2631 O  O   . ARG   A 1 335 ? 32.361 -16.771 -1.891  1.00 20.95 ? 857  ARG   A O   1 
ATOM   2632 C  CB  . ARG   A 1 335 ? 33.071 -15.406 0.878   1.00 13.53 ? 857  ARG   A CB  1 
ATOM   2633 C  CG  . ARG   A 1 335 ? 32.718 -14.105 1.617   1.00 16.46 ? 857  ARG   A CG  1 
ATOM   2634 C  CD  . ARG   A 1 335 ? 33.865 -13.541 2.410   1.00 17.61 ? 857  ARG   A CD  1 
ATOM   2635 N  NE  . ARG   A 1 335 ? 34.907 -12.989 1.539   1.00 17.14 ? 857  ARG   A NE  1 
ATOM   2636 C  CZ  . ARG   A 1 335 ? 35.893 -12.221 1.988   1.00 18.96 ? 857  ARG   A CZ  1 
ATOM   2637 N  NH1 . ARG   A 1 335 ? 36.001 -11.929 3.277   1.00 15.90 ? 857  ARG   A NH1 1 
ATOM   2638 N  NH2 . ARG   A 1 335 ? 36.781 -11.721 1.120   1.00 17.11 ? 857  ARG   A NH2 1 
ATOM   2639 N  N   . ASP   A 1 336 ? 32.033 -18.371 -0.353  1.00 16.57 ? 858  ASP   A N   1 
ATOM   2640 C  CA  . ASP   A 1 336 ? 32.249 -19.448 -1.307  1.00 20.36 ? 858  ASP   A CA  1 
ATOM   2641 C  C   . ASP   A 1 336 ? 31.038 -19.706 -2.200  1.00 24.47 ? 858  ASP   A C   1 
ATOM   2642 O  O   . ASP   A 1 336 ? 31.091 -20.605 -3.046  1.00 20.82 ? 858  ASP   A O   1 
ATOM   2643 C  CB  . ASP   A 1 336 ? 32.638 -20.718 -0.554  1.00 17.31 ? 858  ASP   A CB  1 
ATOM   2644 C  CG  . ASP   A 1 336 ? 31.578 -21.161 0.456   1.00 23.26 ? 858  ASP   A CG  1 
ATOM   2645 O  OD1 . ASP   A 1 336 ? 30.448 -20.620 0.451   1.00 19.21 ? 858  ASP   A OD1 1 
ATOM   2646 O  OD2 . ASP   A 1 336 ? 31.870 -22.069 1.265   1.00 22.53 ? 858  ASP   A OD2 1 
ATOM   2647 N  N   . GLY   A 1 337 ? 29.951 -18.946 -2.054  1.00 18.42 ? 859  GLY   A N   1 
ATOM   2648 C  CA  . GLY   A 1 337 ? 28.780 -19.167 -2.875  1.00 18.91 ? 859  GLY   A CA  1 
ATOM   2649 C  C   . GLY   A 1 337 ? 27.845 -20.255 -2.405  1.00 19.73 ? 859  GLY   A C   1 
ATOM   2650 O  O   . GLY   A 1 337 ? 26.788 -20.446 -3.020  1.00 22.64 ? 859  GLY   A O   1 
ATOM   2651 N  N   . LEU   A 1 338 ? 28.192 -21.005 -1.364  1.00 19.40 ? 860  LEU   A N   1 
ATOM   2652 C  CA  . LEU   A 1 338 ? 27.306 -22.036 -0.847  1.00 21.34 ? 860  LEU   A CA  1 
ATOM   2653 C  C   . LEU   A 1 338 ? 26.286 -21.429 0.117   1.00 19.00 ? 860  LEU   A C   1 
ATOM   2654 O  O   . LEU   A 1 338 ? 26.435 -20.297 0.597   1.00 17.17 ? 860  LEU   A O   1 
ATOM   2655 C  CB  . LEU   A 1 338 ? 28.102 -23.136 -0.132  1.00 19.16 ? 860  LEU   A CB  1 
ATOM   2656 C  CG  . LEU   A 1 338 ? 29.160 -23.805 -1.005  1.00 26.27 ? 860  LEU   A CG  1 
ATOM   2657 C  CD1 . LEU   A 1 338 ? 29.980 -24.802 -0.204  1.00 29.12 ? 860  LEU   A CD1 1 
ATOM   2658 C  CD2 . LEU   A 1 338 ? 28.457 -24.491 -2.160  1.00 26.72 ? 860  LEU   A CD2 1 
ATOM   2659 N  N   . GLN   A 1 339 ? 25.244 -22.213 0.421   1.00 20.06 ? 861  GLN   A N   1 
ATOM   2660 C  CA  . GLN   A 1 339 ? 24.134 -21.682 1.208   1.00 19.56 ? 861  GLN   A CA  1 
ATOM   2661 C  C   . GLN   A 1 339 ? 24.609 -21.322 2.608   1.00 19.53 ? 861  GLN   A C   1 
ATOM   2662 O  O   . GLN   A 1 339 ? 25.274 -22.129 3.272   1.00 18.64 ? 861  GLN   A O   1 
ATOM   2663 C  CB  . GLN   A 1 339 ? 23.003 -22.714 1.287   1.00 18.33 ? 861  GLN   A CB  1 
ATOM   2664 C  CG  . GLN   A 1 339 ? 21.787 -22.220 2.089   1.00 21.78 ? 861  GLN   A CG  1 
ATOM   2665 C  CD  . GLN   A 1 339 ? 21.016 -21.124 1.367   1.00 23.75 ? 861  GLN   A CD  1 
ATOM   2666 O  OE1 . GLN   A 1 339 ? 20.909 -19.982 1.848   1.00 23.77 ? 861  GLN   A OE1 1 
ATOM   2667 N  NE2 . GLN   A 1 339 ? 20.503 -21.453 0.206   1.00 18.15 ? 861  GLN   A NE2 1 
ATOM   2668 N  N   . SER   A 1 340 ? 24.231 -20.122 3.070   1.00 15.01 ? 862  SER   A N   1 
ATOM   2669 C  CA  . SER   A 1 340 ? 24.512 -19.650 4.417   1.00 16.73 ? 862  SER   A CA  1 
ATOM   2670 C  C   . SER   A 1 340 ? 23.263 -18.969 4.978   1.00 15.51 ? 862  SER   A C   1 
ATOM   2671 O  O   . SER   A 1 340 ? 22.330 -18.661 4.249   1.00 16.74 ? 862  SER   A O   1 
ATOM   2672 C  CB  . SER   A 1 340 ? 25.720 -18.679 4.424   1.00 17.36 ? 862  SER   A CB  1 
ATOM   2673 O  OG  . SER   A 1 340 ? 26.906 -19.352 3.932   1.00 16.31 ? 862  SER   A OG  1 
ATOM   2674 N  N   . SER   A 1 341 ? 23.256 -18.719 6.282   1.00 14.48 ? 863  SER   A N   1 
ATOM   2675 C  CA  . SER   A 1 341 ? 22.142 -18.049 6.948   1.00 16.31 ? 863  SER   A CA  1 
ATOM   2676 C  C   . SER   A 1 341 ? 22.662 -16.918 7.813   1.00 14.59 ? 863  SER   A C   1 
ATOM   2677 O  O   . SER   A 1 341 ? 23.740 -17.031 8.397   1.00 15.18 ? 863  SER   A O   1 
ATOM   2678 C  CB  . SER   A 1 341 ? 21.369 -19.009 7.849   1.00 15.48 ? 863  SER   A CB  1 
ATOM   2679 O  OG  . SER   A 1 341 ? 20.762 -19.988 7.052   1.00 21.58 ? 863  SER   A OG  1 
ATOM   2680 N  N   . CYS   A 1 342 ? 21.882 -15.833 7.900   1.00 13.51 ? 864  CYS   A N   1 
ATOM   2681 C  CA  . CYS   A 1 342 ? 22.223 -14.683 8.738   1.00 14.32 ? 864  CYS   A CA  1 
ATOM   2682 C  C   . CYS   A 1 342 ? 21.019 -14.384 9.612   1.00 16.28 ? 864  CYS   A C   1 
ATOM   2683 O  O   . CYS   A 1 342 ? 19.984 -13.962 9.097   1.00 18.27 ? 864  CYS   A O   1 
ATOM   2684 C  CB  . CYS   A 1 342 ? 22.592 -13.472 7.882   1.00 15.70 ? 864  CYS   A CB  1 
ATOM   2685 S  SG  . CYS   A 1 342 ? 23.882 -13.866 6.662   1.00 18.49 ? 864  CYS   A SG  1 
ATOM   2686 N  N   . HIS   A 1 343 ? 21.143 -14.631 10.918  1.00 15.13 ? 865  HIS   A N   1 
ATOM   2687 C  CA  . HIS   A 1 343 ? 20.054 -14.439 11.869  1.00 17.50 ? 865  HIS   A CA  1 
ATOM   2688 C  C   . HIS   A 1 343 ? 20.369 -13.270 12.788  1.00 18.86 ? 865  HIS   A C   1 
ATOM   2689 O  O   . HIS   A 1 343 ? 21.488 -13.153 13.268  1.00 16.55 ? 865  HIS   A O   1 
ATOM   2690 C  CB  . HIS   A 1 343 ? 19.845 -15.695 12.735  1.00 18.90 ? 865  HIS   A CB  1 
ATOM   2691 C  CG  . HIS   A 1 343 ? 19.136 -16.815 12.031  1.00 19.03 ? 865  HIS   A CG  1 
ATOM   2692 N  ND1 . HIS   A 1 343 ? 19.714 -17.539 11.013  1.00 22.57 ? 865  HIS   A ND1 1 
ATOM   2693 C  CD2 . HIS   A 1 343 ? 17.898 -17.339 12.207  1.00 18.67 ? 865  HIS   A CD2 1 
ATOM   2694 C  CE1 . HIS   A 1 343 ? 18.863 -18.454 10.580  1.00 19.82 ? 865  HIS   A CE1 1 
ATOM   2695 N  NE2 . HIS   A 1 343 ? 17.748 -18.349 11.284  1.00 20.29 ? 865  HIS   A NE2 1 
ATOM   2696 N  N   . VAL   A 1 344 ? 19.381 -12.422 13.071  1.00 16.23 ? 866  VAL   A N   1 
ATOM   2697 C  CA  . VAL   A 1 344 ? 19.477 -11.451 14.156  1.00 13.79 ? 866  VAL   A CA  1 
ATOM   2698 C  C   . VAL   A 1 344 ? 18.588 -11.954 15.277  1.00 18.29 ? 866  VAL   A C   1 
ATOM   2699 O  O   . VAL   A 1 344 ? 17.429 -12.313 15.030  1.00 19.80 ? 866  VAL   A O   1 
ATOM   2700 C  CB  . VAL   A 1 344 ? 19.015 -10.041 13.740  1.00 16.18 ? 866  VAL   A CB  1 
ATOM   2701 C  CG1 . VAL   A 1 344 ? 19.170 -9.097  14.928  1.00 15.68 ? 866  VAL   A CG1 1 
ATOM   2702 C  CG2 . VAL   A 1 344 ? 19.784 -9.561  12.507  1.00 14.59 ? 866  VAL   A CG2 1 
ATOM   2703 N  N   . LEU   A 1 345 ? 19.109 -11.946 16.500  1.00 13.63 ? 867  LEU   A N   1 
ATOM   2704 C  CA  . LEU   A 1 345 ? 18.335 -12.185 17.712  1.00 17.57 ? 867  LEU   A CA  1 
ATOM   2705 C  C   . LEU   A 1 345 ? 18.280 -10.850 18.441  1.00 19.08 ? 867  LEU   A C   1 
ATOM   2706 O  O   . LEU   A 1 345 ? 19.328 -10.253 18.696  1.00 19.98 ? 867  LEU   A O   1 
ATOM   2707 C  CB  . LEU   A 1 345 ? 19.005 -13.254 18.585  1.00 20.63 ? 867  LEU   A CB  1 
ATOM   2708 C  CG  . LEU   A 1 345 ? 18.669 -14.724 18.313  1.00 21.13 ? 867  LEU   A CG  1 
ATOM   2709 C  CD1 . LEU   A 1 345 ? 18.585 -15.061 16.841  1.00 26.96 ? 867  LEU   A CD1 1 
ATOM   2710 C  CD2 . LEU   A 1 345 ? 19.678 -15.631 18.983  1.00 21.00 ? 867  LEU   A CD2 1 
ATOM   2711 N  N   . TRP   A 1 346 ? 17.083 -10.336 18.721  1.00 16.58 ? 868  TRP   A N   1 
ATOM   2712 C  CA  . TRP   A 1 346 ? 17.032 -8.979  19.258  1.00 16.84 ? 868  TRP   A CA  1 
ATOM   2713 C  C   . TRP   A 1 346 ? 15.939 -8.840  20.314  1.00 20.00 ? 868  TRP   A C   1 
ATOM   2714 O  O   . TRP   A 1 346 ? 15.047 -9.683  20.432  1.00 22.39 ? 868  TRP   A O   1 
ATOM   2715 C  CB  . TRP   A 1 346 ? 16.817 -7.936  18.139  1.00 20.08 ? 868  TRP   A CB  1 
ATOM   2716 C  CG  . TRP   A 1 346 ? 15.404 -7.896  17.643  1.00 21.49 ? 868  TRP   A CG  1 
ATOM   2717 C  CD1 . TRP   A 1 346 ? 14.748 -8.884  16.962  1.00 23.35 ? 868  TRP   A CD1 1 
ATOM   2718 C  CD2 . TRP   A 1 346 ? 14.461 -6.821  17.797  1.00 23.93 ? 868  TRP   A CD2 1 
ATOM   2719 N  NE1 . TRP   A 1 346 ? 13.455 -8.496  16.686  1.00 19.44 ? 868  TRP   A NE1 1 
ATOM   2720 C  CE2 . TRP   A 1 346 ? 13.259 -7.231  17.184  1.00 19.37 ? 868  TRP   A CE2 1 
ATOM   2721 C  CE3 . TRP   A 1 346 ? 14.521 -5.551  18.391  1.00 24.20 ? 868  TRP   A CE3 1 
ATOM   2722 C  CZ2 . TRP   A 1 346 ? 12.114 -6.416  17.152  1.00 26.42 ? 868  TRP   A CZ2 1 
ATOM   2723 C  CZ3 . TRP   A 1 346 ? 13.385 -4.742  18.361  1.00 25.34 ? 868  TRP   A CZ3 1 
ATOM   2724 C  CH2 . TRP   A 1 346 ? 12.201 -5.176  17.740  1.00 25.13 ? 868  TRP   A CH2 1 
ATOM   2725 N  N   . ALA   A 1 347 ? 16.021 -7.757  21.085  1.00 18.41 ? 869  ALA   A N   1 
ATOM   2726 C  CA  . ALA   A 1 347 ? 14.954 -7.327  21.991  1.00 20.17 ? 869  ALA   A CA  1 
ATOM   2727 C  C   . ALA   A 1 347 ? 14.867 -5.808  21.950  1.00 27.48 ? 869  ALA   A C   1 
ATOM   2728 O  O   . ALA   A 1 347 ? 15.857 -5.140  21.646  1.00 19.59 ? 869  ALA   A O   1 
ATOM   2729 C  CB  . ALA   A 1 347 ? 15.181 -7.798  23.437  1.00 20.51 ? 869  ALA   A CB  1 
ATOM   2730 N  N   . PRO   A 1 348 ? 13.684 -5.236  22.200  1.00 25.55 ? 870  PRO   A N   1 
ATOM   2731 C  CA  . PRO   A 1 348 ? 13.580 -3.771  22.225  1.00 23.98 ? 870  PRO   A CA  1 
ATOM   2732 C  C   . PRO   A 1 348 ? 14.499 -3.106  23.238  1.00 26.48 ? 870  PRO   A C   1 
ATOM   2733 O  O   . PRO   A 1 348 ? 14.909 -1.962  23.011  1.00 24.71 ? 870  PRO   A O   1 
ATOM   2734 C  CB  . PRO   A 1 348 ? 12.094 -3.543  22.553  1.00 25.47 ? 870  PRO   A CB  1 
ATOM   2735 C  CG  . PRO   A 1 348 ? 11.421 -4.689  21.860  1.00 24.13 ? 870  PRO   A CG  1 
ATOM   2736 C  CD  . PRO   A 1 348 ? 12.368 -5.875  22.058  1.00 24.37 ? 870  PRO   A CD  1 
ATOM   2737 N  N   . ALA   A 1 349 ? 14.872 -3.797  24.321  1.00 20.24 ? 871  ALA   A N   1 
ATOM   2738 C  CA  . ALA   A 1 349 ? 15.776 -3.267  25.330  1.00 25.80 ? 871  ALA   A CA  1 
ATOM   2739 C  C   . ALA   A 1 349 ? 17.255 -3.360  24.935  1.00 24.73 ? 871  ALA   A C   1 
ATOM   2740 O  O   . ALA   A 1 349 ? 18.111 -3.022  25.753  1.00 23.89 ? 871  ALA   A O   1 
ATOM   2741 C  CB  . ALA   A 1 349 ? 15.563 -3.995  26.662  1.00 27.06 ? 871  ALA   A CB  1 
ATOM   2742 N  N   . ASP   A 1 350 ? 17.571 -3.800  23.719  1.00 21.59 ? 872  ASP   A N   1 
ATOM   2743 C  CA  . ASP   A 1 350 ? 18.969 -3.938  23.309  1.00 21.09 ? 872  ASP   A CA  1 
ATOM   2744 C  C   . ASP   A 1 350 ? 19.704 -2.590  23.320  1.00 19.69 ? 872  ASP   A C   1 
ATOM   2745 O  O   . ASP   A 1 350 ? 19.114 -1.522  23.084  1.00 20.86 ? 872  ASP   A O   1 
ATOM   2746 C  CB  . ASP   A 1 350 ? 19.039 -4.560  21.906  1.00 18.80 ? 872  ASP   A CB  1 
ATOM   2747 C  CG  . ASP   A 1 350 ? 18.853 -6.079  21.904  1.00 22.27 ? 872  ASP   A CG  1 
ATOM   2748 O  OD1 . ASP   A 1 350 ? 18.802 -6.714  22.976  1.00 22.85 ? 872  ASP   A OD1 1 
ATOM   2749 O  OD2 . ASP   A 1 350 ? 18.732 -6.651  20.805  1.00 19.97 ? 872  ASP   A OD2 1 
ATOM   2750 N  N   . ILE   A 1 351 ? 21.028 -2.662  23.556  1.00 18.21 ? 873  ILE   A N   1 
ATOM   2751 C  CA  . ILE   A 1 351 ? 21.877 -1.469  23.671  1.00 24.73 ? 873  ILE   A CA  1 
ATOM   2752 C  C   . ILE   A 1 351 ? 21.765 -0.594  22.435  1.00 25.93 ? 873  ILE   A C   1 
ATOM   2753 O  O   . ILE   A 1 351 ? 21.672 0.646   22.527  1.00 19.96 ? 873  ILE   A O   1 
ATOM   2754 C  CB  . ILE   A 1 351 ? 23.346 -1.883  23.911  1.00 24.92 ? 873  ILE   A CB  1 
ATOM   2755 C  CG1 . ILE   A 1 351 ? 23.521 -2.334  25.353  1.00 37.48 ? 873  ILE   A CG1 1 
ATOM   2756 C  CG2 . ILE   A 1 351 ? 24.320 -0.733  23.594  1.00 37.27 ? 873  ILE   A CG2 1 
ATOM   2757 C  CD1 . ILE   A 1 351 ? 24.828 -3.076  25.582  1.00 45.43 ? 873  ILE   A CD1 1 
ATOM   2758 N  N   . ASN   A 1 352 ? 21.813 -1.214  21.256  1.00 17.81 ? 874  ASN   A N   1 
ATOM   2759 C  CA  . ASN   A 1 352 ? 21.844 -0.415  20.044  1.00 19.52 ? 874  ASN   A CA  1 
ATOM   2760 C  C   . ASN   A 1 352 ? 20.492 0.192   19.699  1.00 20.84 ? 874  ASN   A C   1 
ATOM   2761 O  O   . ASN   A 1 352 ? 20.405 0.916   18.701  1.00 24.50 ? 874  ASN   A O   1 
ATOM   2762 C  CB  . ASN   A 1 352 ? 22.391 -1.254  18.889  1.00 18.47 ? 874  ASN   A CB  1 
ATOM   2763 C  CG  . ASN   A 1 352 ? 23.891 -1.432  18.996  1.00 23.33 ? 874  ASN   A CG  1 
ATOM   2764 O  OD1 . ASN   A 1 352 ? 24.582 -0.550  19.534  1.00 26.28 ? 874  ASN   A OD1 1 
ATOM   2765 N  ND2 . ASN   A 1 352 ? 24.413 -2.546  18.488  1.00 20.39 ? 874  ASN   A ND2 1 
ATOM   2766 N  N   . LEU   A 1 353 ? 19.455 -0.064  20.496  1.00 19.48 ? 875  LEU   A N   1 
ATOM   2767 C  CA  . LEU   A 1 353 ? 18.174 0.609   20.334  1.00 24.44 ? 875  LEU   A CA  1 
ATOM   2768 C  C   . LEU   A 1 353 ? 17.849 1.530   21.503  1.00 17.87 ? 875  LEU   A C   1 
ATOM   2769 O  O   . LEU   A 1 353 ? 16.709 1.984   21.627  1.00 18.87 ? 875  LEU   A O   1 
ATOM   2770 C  CB  . LEU   A 1 353 ? 17.052 -0.413  20.158  1.00 18.88 ? 875  LEU   A CB  1 
ATOM   2771 C  CG  . LEU   A 1 353 ? 17.290 -1.396  18.999  1.00 25.92 ? 875  LEU   A CG  1 
ATOM   2772 C  CD1 . LEU   A 1 353 ? 16.181 -2.432  18.884  1.00 25.47 ? 875  LEU   A CD1 1 
ATOM   2773 C  CD2 . LEU   A 1 353 ? 17.488 -0.656  17.681  1.00 25.33 ? 875  LEU   A CD2 1 
ATOM   2774 N  N   . ASN   A 1 354 ? 18.798 1.773   22.388  1.00 18.96 ? 876  ASN   A N   1 
ATOM   2775 C  CA  . ASN   A 1 354 ? 18.532 2.593   23.564  1.00 20.80 ? 876  ASN   A CA  1 
ATOM   2776 C  C   . ASN   A 1 354 ? 18.818 4.056   23.206  1.00 23.53 ? 876  ASN   A C   1 
ATOM   2777 O  O   . ASN   A 1 354 ? 19.971 4.480   23.140  1.00 22.44 ? 876  ASN   A O   1 
ATOM   2778 C  CB  . ASN   A 1 354 ? 19.368 2.102   24.738  1.00 22.18 ? 876  ASN   A CB  1 
ATOM   2779 C  CG  . ASN   A 1 354 ? 19.089 2.878   26.009  1.00 28.98 ? 876  ASN   A CG  1 
ATOM   2780 O  OD1 . ASN   A 1 354 ? 18.406 3.900   25.985  1.00 23.73 ? 876  ASN   A OD1 1 
ATOM   2781 N  ND2 . ASN   A 1 354 ? 19.632 2.411   27.121  1.00 31.23 ? 876  ASN   A ND2 1 
ATOM   2782 N  N   . ARG   A 1 355 ? 17.761 4.836   22.975  1.00 19.34 ? 877  ARG   A N   1 
ATOM   2783 C  CA  . ARG   A 1 355 ? 17.948 6.234   22.606  1.00 19.94 ? 877  ARG   A CA  1 
ATOM   2784 C  C   . ARG   A 1 355 ? 18.551 7.052   23.733  1.00 20.89 ? 877  ARG   A C   1 
ATOM   2785 O  O   . ARG   A 1 355 ? 19.136 8.103   23.469  1.00 22.05 ? 877  ARG   A O   1 
ATOM   2786 C  CB  . ARG   A 1 355 ? 16.609 6.856   22.168  1.00 18.63 ? 877  ARG   A CB  1 
ATOM   2787 C  CG  . ARG   A 1 355 ? 16.255 6.508   20.731  1.00 19.85 ? 877  ARG   A CG  1 
ATOM   2788 C  CD  . ARG   A 1 355 ? 15.792 5.056   20.559  1.00 18.78 ? 877  ARG   A CD  1 
ATOM   2789 N  NE  . ARG   A 1 355 ? 15.136 4.915   19.266  1.00 18.93 ? 877  ARG   A NE  1 
ATOM   2790 C  CZ  . ARG   A 1 355 ? 14.635 3.795   18.776  1.00 22.82 ? 877  ARG   A CZ  1 
ATOM   2791 N  NH1 . ARG   A 1 355 ? 14.828 2.630   19.379  1.00 24.03 ? 877  ARG   A NH1 1 
ATOM   2792 N  NH2 . ARG   A 1 355 ? 13.893 3.849   17.665  1.00 19.08 ? 877  ARG   A NH2 1 
ATOM   2793 N  N   . HIS   A 1 356 ? 18.441 6.597   24.978  1.00 23.46 ? 878  HIS   A N   1 
ATOM   2794 C  CA  . HIS   A 1 356 ? 19.006 7.384   26.068  1.00 25.04 ? 878  HIS   A CA  1 
ATOM   2795 C  C   . HIS   A 1 356 ? 20.519 7.492   25.950  1.00 32.34 ? 878  HIS   A C   1 
ATOM   2796 O  O   . HIS   A 1 356 ? 21.101 8.490   26.388  1.00 34.76 ? 878  HIS   A O   1 
ATOM   2797 C  CB  . HIS   A 1 356 ? 18.589 6.793   27.409  1.00 32.07 ? 878  HIS   A CB  1 
ATOM   2798 C  CG  . HIS   A 1 356 ? 17.109 6.812   27.621  1.00 39.88 ? 878  HIS   A CG  1 
ATOM   2799 N  ND1 . HIS   A 1 356 ? 16.440 7.930   28.069  1.00 39.75 ? 878  HIS   A ND1 1 
ATOM   2800 C  CD2 . HIS   A 1 356 ? 16.163 5.866   27.407  1.00 37.76 ? 878  HIS   A CD2 1 
ATOM   2801 C  CE1 . HIS   A 1 356 ? 15.147 7.666   28.139  1.00 41.07 ? 878  HIS   A CE1 1 
ATOM   2802 N  NE2 . HIS   A 1 356 ? 14.951 6.423   27.740  1.00 40.24 ? 878  HIS   A NE2 1 
ATOM   2803 N  N   . LEU   A 1 357 ? 21.167 6.511   25.311  1.00 30.51 ? 879  LEU   A N   1 
ATOM   2804 C  CA  . LEU   A 1 357 ? 22.610 6.589   25.110  1.00 29.86 ? 879  LEU   A CA  1 
ATOM   2805 C  C   . LEU   A 1 357 ? 23.013 7.718   24.174  1.00 33.89 ? 879  LEU   A C   1 
ATOM   2806 O  O   . LEU   A 1 357 ? 24.204 8.011   24.062  1.00 31.60 ? 879  LEU   A O   1 
ATOM   2807 C  CB  . LEU   A 1 357 ? 23.125 5.255   24.574  1.00 27.00 ? 879  LEU   A CB  1 
ATOM   2808 C  CG  . LEU   A 1 357 ? 22.666 4.078   25.438  1.00 37.77 ? 879  LEU   A CG  1 
ATOM   2809 C  CD1 . LEU   A 1 357 ? 23.169 2.737   24.899  1.00 34.66 ? 879  LEU   A CD1 1 
ATOM   2810 C  CD2 . LEU   A 1 357 ? 23.109 4.282   26.879  1.00 38.48 ? 879  LEU   A CD2 1 
ATOM   2811 N  N   . LEU   A 1 358 ? 22.059 8.351   23.492  1.00 28.53 ? 880  LEU   A N   1 
ATOM   2812 C  CA  . LEU   A 1 358 ? 22.384 9.385   22.526  1.00 27.92 ? 880  LEU   A CA  1 
ATOM   2813 C  C   . LEU   A 1 358 ? 22.159 10.788  23.068  1.00 28.28 ? 880  LEU   A C   1 
ATOM   2814 O  O   . LEU   A 1 358 ? 22.520 11.761  22.397  1.00 25.66 ? 880  LEU   A O   1 
ATOM   2815 C  CB  . LEU   A 1 358 ? 21.548 9.185   21.253  1.00 23.61 ? 880  LEU   A CB  1 
ATOM   2816 C  CG  . LEU   A 1 358 ? 21.678 7.820   20.581  1.00 22.25 ? 880  LEU   A CG  1 
ATOM   2817 C  CD1 . LEU   A 1 358 ? 20.777 7.768   19.345  1.00 19.70 ? 880  LEU   A CD1 1 
ATOM   2818 C  CD2 . LEU   A 1 358 ? 23.135 7.462   20.199  1.00 19.68 ? 880  LEU   A CD2 1 
ATOM   2819 N  N   . THR   A 1 359 ? 21.609 10.910  24.274  1.00 27.73 ? 881  THR   A N   1 
ATOM   2820 C  CA  . THR   A 1 359 ? 21.141 12.210  24.740  1.00 30.03 ? 881  THR   A CA  1 
ATOM   2821 C  C   . THR   A 1 359 ? 22.285 13.207  24.825  1.00 35.16 ? 881  THR   A C   1 
ATOM   2822 O  O   . THR   A 1 359 ? 22.152 14.355  24.388  1.00 38.01 ? 881  THR   A O   1 
ATOM   2823 C  CB  . THR   A 1 359 ? 20.447 12.057  26.092  1.00 34.81 ? 881  THR   A CB  1 
ATOM   2824 O  OG1 . THR   A 1 359 ? 19.311 11.196  25.939  1.00 39.31 ? 881  THR   A OG1 1 
ATOM   2825 C  CG2 . THR   A 1 359 ? 19.970 13.427  26.623  1.00 40.01 ? 881  THR   A CG2 1 
ATOM   2826 N  N   . GLU   A 1 360 ? 23.435 12.763  25.317  1.00 32.66 ? 882  GLU   A N   1 
ATOM   2827 C  CA  . GLU   A 1 360 ? 24.552 13.653  25.600  1.00 33.78 ? 882  GLU   A CA  1 
ATOM   2828 C  C   . GLU   A 1 360 ? 25.319 14.083  24.362  1.00 40.81 ? 882  GLU   A C   1 
ATOM   2829 O  O   . GLU   A 1 360 ? 26.266 14.869  24.494  1.00 44.38 ? 882  GLU   A O   1 
ATOM   2830 C  CB  . GLU   A 1 360 ? 25.513 12.983  26.589  1.00 33.61 ? 882  GLU   A CB  1 
ATOM   2831 C  CG  . GLU   A 1 360 ? 24.857 12.493  27.870  1.00 49.79 ? 882  GLU   A CG  1 
ATOM   2832 C  CD  . GLU   A 1 360 ? 24.386 13.596  28.823  1.00 60.86 ? 882  GLU   A CD  1 
ATOM   2833 O  OE1 . GLU   A 1 360 ? 24.374 13.327  30.044  1.00 67.56 ? 882  GLU   A OE1 1 
ATOM   2834 O  OE2 . GLU   A 1 360 ? 24.015 14.713  28.379  1.00 65.00 ? 882  GLU   A OE2 1 
ATOM   2835 N  N   . ILE   A 1 361 ? 24.961 13.595  23.173  1.00 25.90 ? 883  ILE   A N   1 
ATOM   2836 C  CA  . ILE   A 1 361 ? 25.699 13.990  21.982  1.00 29.64 ? 883  ILE   A CA  1 
ATOM   2837 C  C   . ILE   A 1 361 ? 25.512 15.481  21.764  1.00 28.35 ? 883  ILE   A C   1 
ATOM   2838 O  O   . ILE   A 1 361 ? 24.384 15.981  21.758  1.00 25.36 ? 883  ILE   A O   1 
ATOM   2839 C  CB  . ILE   A 1 361 ? 25.232 13.177  20.768  1.00 28.31 ? 883  ILE   A CB  1 
ATOM   2840 C  CG1 . ILE   A 1 361 ? 25.677 11.718  20.924  1.00 23.56 ? 883  ILE   A CG1 1 
ATOM   2841 C  CG2 . ILE   A 1 361 ? 25.756 13.822  19.489  1.00 22.79 ? 883  ILE   A CG2 1 
ATOM   2842 C  CD1 . ILE   A 1 361 ? 25.064 10.757  19.917  1.00 21.95 ? 883  ILE   A CD1 1 
ATOM   2843 N  N   . ARG   A 1 362 ? 26.620 16.204  21.606  1.00 29.03 ? 884  ARG   A N   1 
ATOM   2844 C  CA  . ARG   A 1 362 ? 26.535 17.658  21.511  1.00 32.17 ? 884  ARG   A CA  1 
ATOM   2845 C  C   . ARG   A 1 362 ? 26.235 18.143  20.092  1.00 25.12 ? 884  ARG   A C   1 
ATOM   2846 O  O   . ARG   A 1 362 ? 25.501 19.122  19.912  1.00 30.73 ? 884  ARG   A O   1 
ATOM   2847 C  CB  . ARG   A 1 362 ? 27.835 18.273  22.013  1.00 40.46 ? 884  ARG   A CB  1 
ATOM   2848 C  CG  . ARG   A 1 362 ? 27.740 18.733  23.442  1.00 53.31 ? 884  ARG   A CG  1 
ATOM   2849 C  CD  . ARG   A 1 362 ? 26.847 19.949  23.525  1.00 54.65 ? 884  ARG   A CD  1 
ATOM   2850 N  NE  . ARG   A 1 362 ? 27.608 21.175  23.741  1.00 59.79 ? 884  ARG   A NE  1 
ATOM   2851 C  CZ  . ARG   A 1 362 ? 27.117 22.393  23.562  1.00 60.44 ? 884  ARG   A CZ  1 
ATOM   2852 N  NH1 . ARG   A 1 362 ? 25.884 22.582  23.121  1.00 63.55 ? 884  ARG   A NH1 1 
ATOM   2853 N  NH2 . ARG   A 1 362 ? 27.884 23.448  23.825  1.00 64.79 ? 884  ARG   A NH2 1 
ATOM   2854 N  N   . ASN   A 1 363 ? 26.822 17.505  19.085  1.00 24.79 ? 885  ASN   A N   1 
ATOM   2855 C  CA  . ASN   A 1 363 ? 26.601 17.877  17.686  1.00 23.88 ? 885  ASN   A CA  1 
ATOM   2856 C  C   . ASN   A 1 363 ? 25.169 17.501  17.302  1.00 24.49 ? 885  ASN   A C   1 
ATOM   2857 O  O   . ASN   A 1 363 ? 24.847 16.317  17.248  1.00 23.14 ? 885  ASN   A O   1 
ATOM   2858 C  CB  . ASN   A 1 363 ? 27.633 17.152  16.820  1.00 20.66 ? 885  ASN   A CB  1 
ATOM   2859 C  CG  . ASN   A 1 363 ? 27.525 17.482  15.346  1.00 28.18 ? 885  ASN   A CG  1 
ATOM   2860 O  OD1 . ASN   A 1 363 ? 26.446 17.719  14.818  1.00 33.30 ? 885  ASN   A OD1 1 
ATOM   2861 N  ND2 . ASN   A 1 363 ? 28.669 17.470  14.655  1.00 35.84 ? 885  ASN   A ND2 1 
ATOM   2862 N  N   . GLU   A 1 364 ? 24.310 18.501  17.043  1.00 22.50 ? 886  GLU   A N   1 
ATOM   2863 C  CA  . GLU   A 1 364 ? 22.896 18.228  16.759  1.00 26.14 ? 886  GLU   A CA  1 
ATOM   2864 C  C   . GLU   A 1 364 ? 22.729 17.355  15.529  1.00 21.46 ? 886  GLU   A C   1 
ATOM   2865 O  O   . GLU   A 1 364 ? 21.849 16.482  15.495  1.00 20.34 ? 886  GLU   A O   1 
ATOM   2866 C  CB  . GLU   A 1 364 ? 22.114 19.529  16.534  1.00 27.33 ? 886  GLU   A CB  1 
ATOM   2867 C  CG  . GLU   A 1 364 ? 21.957 20.426  17.721  1.00 48.17 ? 886  GLU   A CG  1 
ATOM   2868 C  CD  . GLU   A 1 364 ? 21.109 21.651  17.390  1.00 51.95 ? 886  GLU   A CD  1 
ATOM   2869 O  OE1 . GLU   A 1 364 ? 20.230 22.010  18.206  1.00 59.34 ? 886  GLU   A OE1 1 
ATOM   2870 O  OE2 . GLU   A 1 364 ? 21.311 22.236  16.302  1.00 51.08 ? 886  GLU   A OE2 1 
ATOM   2871 N  N   . LYS   A 1 365 ? 23.544 17.599  14.493  1.00 23.75 ? 887  LYS   A N   1 
ATOM   2872 C  CA  . LYS   A 1 365 ? 23.416 16.832  13.259  1.00 23.52 ? 887  LYS   A CA  1 
ATOM   2873 C  C   . LYS   A 1 365 ? 23.773 15.370  13.488  1.00 24.16 ? 887  LYS   A C   1 
ATOM   2874 O  O   . LYS   A 1 365 ? 23.095 14.468  12.985  1.00 20.20 ? 887  LYS   A O   1 
ATOM   2875 C  CB  . LYS   A 1 365 ? 24.301 17.439  12.172  1.00 27.70 ? 887  LYS   A CB  1 
ATOM   2876 C  CG  . LYS   A 1 365 ? 24.003 18.922  11.892  1.00 30.08 ? 887  LYS   A CG  1 
ATOM   2877 C  CD  . LYS   A 1 365 ? 24.793 19.429  10.674  1.00 33.37 ? 887  LYS   A CD  1 
ATOM   2878 C  CE  . LYS   A 1 365 ? 26.288 19.178  10.792  1.00 48.41 ? 887  LYS   A CE  1 
ATOM   2879 N  NZ  . LYS   A 1 365 ? 27.043 19.472  9.513   1.00 44.05 ? 887  LYS   A NZ  1 
ATOM   2880 N  N   . PHE   A 1 366 ? 24.822 15.121  14.267  1.00 21.82 ? 888  PHE   A N   1 
ATOM   2881 C  CA  . PHE   A 1 366 ? 25.201 13.747  14.566  1.00 19.80 ? 888  PHE   A CA  1 
ATOM   2882 C  C   . PHE   A 1 366 ? 24.164 13.061  15.436  1.00 20.73 ? 888  PHE   A C   1 
ATOM   2883 O  O   . PHE   A 1 366 ? 23.906 11.862  15.266  1.00 18.66 ? 888  PHE   A O   1 
ATOM   2884 C  CB  . PHE   A 1 366 ? 26.562 13.712  15.260  1.00 16.98 ? 888  PHE   A CB  1 
ATOM   2885 C  CG  . PHE   A 1 366 ? 27.138 12.334  15.337  1.00 19.56 ? 888  PHE   A CG  1 
ATOM   2886 C  CD1 . PHE   A 1 366 ? 27.373 11.630  14.182  1.00 19.82 ? 888  PHE   A CD1 1 
ATOM   2887 C  CD2 . PHE   A 1 366 ? 27.391 11.727  16.565  1.00 25.42 ? 888  PHE   A CD2 1 
ATOM   2888 C  CE1 . PHE   A 1 366 ? 27.895 10.323  14.229  1.00 25.55 ? 888  PHE   A CE1 1 
ATOM   2889 C  CE2 . PHE   A 1 366 ? 27.912 10.439  16.628  1.00 24.16 ? 888  PHE   A CE2 1 
ATOM   2890 C  CZ  . PHE   A 1 366 ? 28.173 9.741   15.455  1.00 24.13 ? 888  PHE   A CZ  1 
ATOM   2891 N  N   . ARG   A 1 367 ? 23.599 13.784  16.412  1.00 19.34 ? 889  ARG   A N   1 
ATOM   2892 C  CA  . ARG   A 1 367 ? 22.573 13.174  17.252  1.00 17.21 ? 889  ARG   A CA  1 
ATOM   2893 C  C   . ARG   A 1 367 ? 21.388 12.759  16.405  1.00 21.00 ? 889  ARG   A C   1 
ATOM   2894 O  O   . ARG   A 1 367 ? 20.846 11.655  16.573  1.00 16.54 ? 889  ARG   A O   1 
ATOM   2895 C  CB  . ARG   A 1 367 ? 22.128 14.131  18.357  1.00 18.86 ? 889  ARG   A CB  1 
ATOM   2896 C  CG  . ARG   A 1 367 ? 21.349 13.438  19.471  1.00 25.15 ? 889  ARG   A CG  1 
ATOM   2897 C  CD  . ARG   A 1 367 ? 20.630 14.434  20.360  1.00 28.66 ? 889  ARG   A CD  1 
ATOM   2898 N  NE  . ARG   A 1 367 ? 21.526 15.475  20.842  1.00 37.04 ? 889  ARG   A NE  1 
ATOM   2899 C  CZ  . ARG   A 1 367 ? 21.332 16.780  20.705  1.00 40.67 ? 889  ARG   A CZ  1 
ATOM   2900 N  NH1 . ARG   A 1 367 ? 20.266 17.265  20.081  1.00 33.21 ? 889  ARG   A NH1 1 
ATOM   2901 N  NH2 . ARG   A 1 367 ? 22.224 17.621  21.220  1.00 33.46 ? 889  ARG   A NH2 1 
ATOM   2902 N  N   . LEU   A 1 368 ? 20.967 13.634  15.478  1.00 19.26 ? 890  LEU   A N   1 
ATOM   2903 C  CA  . LEU   A 1 368 ? 19.877 13.255  14.581  1.00 21.04 ? 890  LEU   A CA  1 
ATOM   2904 C  C   . LEU   A 1 368 ? 20.251 12.034  13.755  1.00 20.67 ? 890  LEU   A C   1 
ATOM   2905 O  O   . LEU   A 1 368 ? 19.430 11.122  13.554  1.00 17.17 ? 890  LEU   A O   1 
ATOM   2906 C  CB  . LEU   A 1 368 ? 19.530 14.427  13.657  1.00 19.83 ? 890  LEU   A CB  1 
ATOM   2907 C  CG  . LEU   A 1 368 ? 18.401 14.161  12.656  1.00 23.96 ? 890  LEU   A CG  1 
ATOM   2908 C  CD1 . LEU   A 1 368 ? 17.104 13.760  13.383  1.00 18.86 ? 890  LEU   A CD1 1 
ATOM   2909 C  CD2 . LEU   A 1 368 ? 18.197 15.389  11.756  1.00 21.37 ? 890  LEU   A CD2 1 
ATOM   2910 N  N   . TYR   A 1 369 ? 21.472 12.008  13.233  1.00 16.21 ? 891  TYR   A N   1 
ATOM   2911 C  CA  . TYR   A 1 369 ? 21.892 10.852  12.437  1.00 17.06 ? 891  TYR   A CA  1 
ATOM   2912 C  C   . TYR   A 1 369 ? 21.817 9.569   13.261  1.00 17.95 ? 891  TYR   A C   1 
ATOM   2913 O  O   . TYR   A 1 369 ? 21.276 8.545   12.805  1.00 17.89 ? 891  TYR   A O   1 
ATOM   2914 C  CB  . TYR   A 1 369 ? 23.300 11.083  11.895  1.00 17.04 ? 891  TYR   A CB  1 
ATOM   2915 C  CG  . TYR   A 1 369 ? 23.949 9.840   11.343  1.00 18.47 ? 891  TYR   A CG  1 
ATOM   2916 C  CD1 . TYR   A 1 369 ? 23.583 9.331   10.094  1.00 19.86 ? 891  TYR   A CD1 1 
ATOM   2917 C  CD2 . TYR   A 1 369 ? 24.939 9.192   12.060  1.00 19.88 ? 891  TYR   A CD2 1 
ATOM   2918 C  CE1 . TYR   A 1 369 ? 24.187 8.188   9.582   1.00 23.20 ? 891  TYR   A CE1 1 
ATOM   2919 C  CE2 . TYR   A 1 369 ? 25.563 8.047   11.549  1.00 23.79 ? 891  TYR   A CE2 1 
ATOM   2920 C  CZ  . TYR   A 1 369 ? 25.182 7.558   10.314  1.00 22.88 ? 891  TYR   A CZ  1 
ATOM   2921 O  OH  . TYR   A 1 369 ? 25.777 6.426   9.800   1.00 24.68 ? 891  TYR   A OH  1 
ATOM   2922 N  N   . LYS   A 1 370 ? 22.329 9.602   14.486  1.00 15.53 ? 892  LYS   A N   1 
ATOM   2923 C  CA  . LYS   A 1 370 ? 22.296 8.386   15.307  1.00 16.71 ? 892  LYS   A CA  1 
ATOM   2924 C  C   . LYS   A 1 370 ? 20.860 7.966   15.638  1.00 17.00 ? 892  LYS   A C   1 
ATOM   2925 O  O   . LYS   A 1 370 ? 20.530 6.769   15.623  1.00 16.19 ? 892  LYS   A O   1 
ATOM   2926 C  CB  . LYS   A 1 370 ? 23.120 8.590   16.586  1.00 17.31 ? 892  LYS   A CB  1 
ATOM   2927 C  CG  . LYS   A 1 370 ? 24.625 8.822   16.341  1.00 18.16 ? 892  LYS   A CG  1 
ATOM   2928 C  CD  . LYS   A 1 370 ? 25.307 7.550   15.823  1.00 19.73 ? 892  LYS   A CD  1 
ATOM   2929 C  CE  . LYS   A 1 370 ? 25.464 6.486   16.925  1.00 26.38 ? 892  LYS   A CE  1 
ATOM   2930 N  NZ  . LYS   A 1 370 ? 26.205 5.246   16.438  1.00 24.38 ? 892  LYS   A NZ  1 
ATOM   2931 N  N   . LEU   A 1 371 ? 19.971 8.936   15.899  1.00 15.63 ? 893  LEU   A N   1 
ATOM   2932 C  CA  . LEU   A 1 371 ? 18.582 8.592   16.203  1.00 12.72 ? 893  LEU   A CA  1 
ATOM   2933 C  C   . LEU   A 1 371 ? 17.873 8.014   14.984  1.00 16.81 ? 893  LEU   A C   1 
ATOM   2934 O  O   . LEU   A 1 371 ? 17.080 7.060   15.097  1.00 17.57 ? 893  LEU   A O   1 
ATOM   2935 C  CB  . LEU   A 1 371 ? 17.824 9.844   16.694  1.00 16.53 ? 893  LEU   A CB  1 
ATOM   2936 C  CG  . LEU   A 1 371 ? 18.246 10.336  18.083  1.00 15.42 ? 893  LEU   A CG  1 
ATOM   2937 C  CD1 . LEU   A 1 371 ? 17.819 11.803  18.267  1.00 16.83 ? 893  LEU   A CD1 1 
ATOM   2938 C  CD2 . LEU   A 1 371 ? 17.565 9.474   19.102  1.00 18.37 ? 893  LEU   A CD2 1 
ATOM   2939 N  N   . LYS   A 1 372 ? 18.148 8.577   13.806  1.00 14.10 ? 894  LYS   A N   1 
ATOM   2940 C  CA  . LYS   A 1 372 ? 17.587 8.047   12.570  1.00 13.38 ? 894  LYS   A CA  1 
ATOM   2941 C  C   . LYS   A 1 372 ? 18.085 6.635   12.300  1.00 18.47 ? 894  LYS   A C   1 
ATOM   2942 O  O   . LYS   A 1 372 ? 17.319 5.768   11.852  1.00 15.57 ? 894  LYS   A O   1 
ATOM   2943 C  CB  . LYS   A 1 372 ? 17.951 8.979   11.414  1.00 15.99 ? 894  LYS   A CB  1 
ATOM   2944 C  CG  . LYS   A 1 372 ? 17.140 10.304  11.476  1.00 15.64 ? 894  LYS   A CG  1 
ATOM   2945 C  CD  . LYS   A 1 372 ? 16.082 10.303  10.424  1.00 20.83 ? 894  LYS   A CD  1 
ATOM   2946 C  CE  . LYS   A 1 372 ? 15.238 11.553  10.493  1.00 24.86 ? 894  LYS   A CE  1 
ATOM   2947 N  NZ  . LYS   A 1 372 ? 14.211 11.503  9.404   1.00 30.22 ? 894  LYS   A NZ  1 
ATOM   2948 N  N   . MET   A 1 373 ? 19.370 6.387   12.551  1.00 17.59 ? 895  MET   A N   1 
ATOM   2949 C  CA  . MET   A 1 373 ? 19.916 5.058   12.284  1.00 16.77 ? 895  MET   A CA  1 
ATOM   2950 C  C   . MET   A 1 373 ? 19.344 4.027   13.248  1.00 14.96 ? 895  MET   A C   1 
ATOM   2951 O  O   . MET   A 1 373 ? 19.085 2.882   12.852  1.00 15.96 ? 895  MET   A O   1 
ATOM   2952 C  CB  . MET   A 1 373 ? 21.447 5.102   12.353  1.00 18.92 ? 895  MET   A CB  1 
ATOM   2953 C  CG  . MET   A 1 373 ? 22.184 5.739   11.131  1.00 22.10 ? 895  MET   A CG  1 
ATOM   2954 S  SD  . MET   A 1 373 ? 21.727 5.219   9.439   1.00 24.13 ? 895  MET   A SD  1 
ATOM   2955 C  CE  . MET   A 1 373 ? 23.220 4.488   8.792   1.00 24.29 ? 895  MET   A CE  1 
ATOM   2956 N  N   . MET   A 1 374 ? 19.096 4.414   14.506  1.00 15.95 ? 896  MET   A N   1 
ATOM   2957 C  CA  . MET   A 1 374 ? 18.423 3.495   15.432  1.00 16.91 ? 896  MET   A CA  1 
ATOM   2958 C  C   . MET   A 1 374 ? 17.021 3.169   14.963  1.00 18.41 ? 896  MET   A C   1 
ATOM   2959 O  O   . MET   A 1 374 ? 16.589 2.001   14.989  1.00 18.83 ? 896  MET   A O   1 
ATOM   2960 C  CB  . MET   A 1 374 ? 18.306 4.071   16.840  1.00 18.42 ? 896  MET   A CB  1 
ATOM   2961 C  CG  . MET   A 1 374 ? 19.500 4.053   17.669  1.00 23.66 ? 896  MET   A CG  1 
ATOM   2962 S  SD  . MET   A 1 374 ? 19.020 4.237   19.412  1.00 23.45 ? 896  MET   A SD  1 
ATOM   2963 C  CE  . MET   A 1 374 ? 20.706 4.116   19.989  1.00 24.51 ? 896  MET   A CE  1 
ATOM   2964 N  N   . ALA   A 1 375 ? 16.247 4.209   14.639  1.00 15.31 ? 897  ALA   A N   1 
ATOM   2965 C  CA  . ALA   A 1 375 ? 14.884 3.977   14.167  1.00 16.58 ? 897  ALA   A CA  1 
ATOM   2966 C  C   . ALA   A 1 375 ? 14.881 3.067   12.947  1.00 17.26 ? 897  ALA   A C   1 
ATOM   2967 O  O   . ALA   A 1 375 ? 14.088 2.132   12.871  1.00 16.94 ? 897  ALA   A O   1 
ATOM   2968 C  CB  . ALA   A 1 375 ? 14.198 5.309   13.846  1.00 17.94 ? 897  ALA   A CB  1 
ATOM   2969 N  N   . LYS   A 1 376 ? 15.751 3.333   11.974  1.00 15.74 ? 898  LYS   A N   1 
ATOM   2970 C  CA  . LYS   A 1 376 ? 15.766 2.527   10.756  1.00 15.71 ? 898  LYS   A CA  1 
ATOM   2971 C  C   . LYS   A 1 376 ? 16.112 1.069   11.056  1.00 16.91 ? 898  LYS   A C   1 
ATOM   2972 O  O   . LYS   A 1 376 ? 15.483 0.146   10.512  1.00 15.79 ? 898  LYS   A O   1 
ATOM   2973 C  CB  . LYS   A 1 376 ? 16.764 3.104   9.754   1.00 18.00 ? 898  LYS   A CB  1 
ATOM   2974 C  CG  . LYS   A 1 376 ? 16.843 2.302   8.459   1.00 19.33 ? 898  LYS   A CG  1 
ATOM   2975 C  CD  . LYS   A 1 376 ? 17.647 3.053   7.411   1.00 28.35 ? 898  LYS   A CD  1 
ATOM   2976 C  CE  . LYS   A 1 376 ? 16.724 3.798   6.441   1.00 35.58 ? 898  LYS   A CE  1 
ATOM   2977 N  NZ  . LYS   A 1 376 ? 15.969 2.878   5.531   1.00 43.46 ? 898  LYS   A NZ  1 
ATOM   2978 N  N   . MET   A 1 377 ? 17.111 0.838   11.919  1.00 14.63 ? 899  MET   A N   1 
ATOM   2979 C  CA  . MET   A 1 377 ? 17.445 -0.536  12.320  1.00 20.71 ? 899  MET   A CA  1 
ATOM   2980 C  C   . MET   A 1 377 ? 16.249 -1.227  12.977  1.00 20.45 ? 899  MET   A C   1 
ATOM   2981 O  O   . MET   A 1 377 ? 15.923 -2.394  12.678  1.00 19.02 ? 899  MET   A O   1 
ATOM   2982 C  CB  . MET   A 1 377 ? 18.648 -0.512  13.280  1.00 15.35 ? 899  MET   A CB  1 
ATOM   2983 C  CG  . MET   A 1 377 ? 19.277 -1.906  13.591  1.00 16.45 ? 899  MET   A CG  1 
ATOM   2984 S  SD  . MET   A 1 377 ? 20.158 -2.507  12.104  1.00 25.07 ? 899  MET   A SD  1 
ATOM   2985 C  CE  . MET   A 1 377 ? 18.915 -3.726  11.640  1.00 17.01 ? 899  MET   A CE  1 
ATOM   2986 N  N   . GLU   A 1 378 ? 15.600 -0.537  13.905  1.00 17.30 ? 900  GLU   A N   1 
ATOM   2987 C  CA  . GLU   A 1 378 ? 14.462 -1.142  14.596  1.00 17.60 ? 900  GLU   A CA  1 
ATOM   2988 C  C   . GLU   A 1 378 ? 13.309 -1.429  13.639  1.00 19.65 ? 900  GLU   A C   1 
ATOM   2989 O  O   . GLU   A 1 378 ? 12.631 -2.459  13.767  1.00 18.64 ? 900  GLU   A O   1 
ATOM   2990 C  CB  . GLU   A 1 378 ? 13.992 -0.238  15.740  1.00 22.72 ? 900  GLU   A CB  1 
ATOM   2991 C  CG  . GLU   A 1 378 ? 12.861 -0.874  16.517  1.00 26.06 ? 900  GLU   A CG  1 
ATOM   2992 C  CD  . GLU   A 1 378 ? 12.641 -0.271  17.903  1.00 41.00 ? 900  GLU   A CD  1 
ATOM   2993 O  OE1 . GLU   A 1 378 ? 12.909 0.931   18.104  1.00 26.65 ? 900  GLU   A OE1 1 
ATOM   2994 O  OE2 . GLU   A 1 378 ? 12.169 -1.015  18.795  1.00 42.09 ? 900  GLU   A OE2 1 
ATOM   2995 N  N   . LYS   A 1 379 ? 13.072 -0.530  12.672  1.00 19.51 ? 901  LYS   A N   1 
ATOM   2996 C  CA  . LYS   A 1 379 ? 12.007 -0.753  11.708  1.00 18.36 ? 901  LYS   A CA  1 
ATOM   2997 C  C   . LYS   A 1 379 ? 12.307 -1.966  10.843  1.00 19.49 ? 901  LYS   A C   1 
ATOM   2998 O  O   . LYS   A 1 379 ? 11.395 -2.717  10.485  1.00 16.49 ? 901  LYS   A O   1 
ATOM   2999 C  CB  . LYS   A 1 379 ? 11.797 0.470   10.817  1.00 21.26 ? 901  LYS   A CB  1 
ATOM   3000 C  CG  . LYS   A 1 379 ? 11.478 1.780   11.541  1.00 31.60 ? 901  LYS   A CG  1 
ATOM   3001 C  CD  . LYS   A 1 379 ? 10.847 1.615   12.953  1.00 44.27 ? 901  LYS   A CD  1 
ATOM   3002 C  CE  . LYS   A 1 379 ? 11.306 2.745   13.915  1.00 35.89 ? 901  LYS   A CE  1 
ATOM   3003 N  NZ  . LYS   A 1 379 ? 11.027 2.436   15.358  1.00 43.59 ? 901  LYS   A NZ  1 
ATOM   3004 N  N   . TYR   A 1 380 ? 13.574 -2.163  10.486  1.00 15.51 ? 902  TYR   A N   1 
ATOM   3005 C  CA  . TYR   A 1 380 ? 13.947 -3.374  9.768   1.00 16.88 ? 902  TYR   A CA  1 
ATOM   3006 C  C   . TYR   A 1 380 ? 13.649 -4.603  10.605  1.00 14.39 ? 902  TYR   A C   1 
ATOM   3007 O  O   . TYR   A 1 380 ? 13.102 -5.594  10.102  1.00 15.26 ? 902  TYR   A O   1 
ATOM   3008 C  CB  . TYR   A 1 380 ? 15.440 -3.348  9.409   1.00 17.97 ? 902  TYR   A CB  1 
ATOM   3009 C  CG  . TYR   A 1 380 ? 15.978 -4.673  8.894   1.00 17.07 ? 902  TYR   A CG  1 
ATOM   3010 C  CD1 . TYR   A 1 380 ? 15.796 -5.051  7.570   1.00 17.63 ? 902  TYR   A CD1 1 
ATOM   3011 C  CD2 . TYR   A 1 380 ? 16.711 -5.537  9.729   1.00 18.24 ? 902  TYR   A CD2 1 
ATOM   3012 C  CE1 . TYR   A 1 380 ? 16.325 -6.260  7.078   1.00 20.33 ? 902  TYR   A CE1 1 
ATOM   3013 C  CE2 . TYR   A 1 380 ? 17.245 -6.757  9.242   1.00 16.87 ? 902  TYR   A CE2 1 
ATOM   3014 C  CZ  . TYR   A 1 380 ? 17.038 -7.100  7.915   1.00 20.42 ? 902  TYR   A CZ  1 
ATOM   3015 O  OH  . TYR   A 1 380 ? 17.521 -8.292  7.401   1.00 17.60 ? 902  TYR   A OH  1 
ATOM   3016 N  N   . LEU   A 1 381 ? 14.016 -4.559  11.882  1.00 15.49 ? 903  LEU   A N   1 
ATOM   3017 C  CA  . LEU   A 1 381 ? 13.914 -5.765  12.702  1.00 16.37 ? 903  LEU   A CA  1 
ATOM   3018 C  C   . LEU   A 1 381 ? 12.462 -6.141  12.964  1.00 20.05 ? 903  LEU   A C   1 
ATOM   3019 O  O   . LEU   A 1 381 ? 12.122 -7.330  13.024  1.00 17.56 ? 903  LEU   A O   1 
ATOM   3020 C  CB  . LEU   A 1 381 ? 14.652 -5.561  14.025  1.00 16.92 ? 903  LEU   A CB  1 
ATOM   3021 C  CG  . LEU   A 1 381 ? 16.185 -5.431  13.926  1.00 17.42 ? 903  LEU   A CG  1 
ATOM   3022 C  CD1 . LEU   A 1 381 ? 16.754 -5.055  15.301  1.00 21.30 ? 903  LEU   A CD1 1 
ATOM   3023 C  CD2 . LEU   A 1 381 ? 16.779 -6.763  13.393  1.00 17.92 ? 903  LEU   A CD2 1 
ATOM   3024 N  N   . HIS   A 1 382 ? 11.599 -5.146  13.111  1.00 16.62 ? 904  HIS   A N   1 
ATOM   3025 C  CA  . HIS   A 1 382 ? 10.171 -5.350  13.376  1.00 20.97 ? 904  HIS   A CA  1 
ATOM   3026 C  C   . HIS   A 1 382 ? 9.355  -5.613  12.113  1.00 23.85 ? 904  HIS   A C   1 
ATOM   3027 O  O   . HIS   A 1 382 ? 8.177  -5.981  12.212  1.00 24.29 ? 904  HIS   A O   1 
ATOM   3028 C  CB  . HIS   A 1 382 ? 9.623  -4.097  14.093  1.00 29.39 ? 904  HIS   A CB  1 
ATOM   3029 C  CG  . HIS   A 1 382 ? 8.282  -4.285  14.727  1.00 47.56 ? 904  HIS   A CG  1 
ATOM   3030 N  ND1 . HIS   A 1 382 ? 8.128  -4.653  16.049  1.00 54.78 ? 904  HIS   A ND1 1 
ATOM   3031 C  CD2 . HIS   A 1 382 ? 7.029  -4.134  14.230  1.00 54.28 ? 904  HIS   A CD2 1 
ATOM   3032 C  CE1 . HIS   A 1 382 ? 6.839  -4.727  16.336  1.00 52.99 ? 904  HIS   A CE1 1 
ATOM   3033 N  NE2 . HIS   A 1 382 ? 6.151  -4.418  15.250  1.00 54.31 ? 904  HIS   A NE2 1 
ATOM   3034 N  N   . SER   A 1 383 ? 9.939  -5.440  10.929  1.00 18.87 ? 905  SER   A N   1 
ATOM   3035 C  CA  . SER   A 1 383 ? 9.159  -5.409  9.698   1.00 18.23 ? 905  SER   A CA  1 
ATOM   3036 C  C   . SER   A 1 383 ? 8.558  -6.768  9.355   1.00 18.25 ? 905  SER   A C   1 
ATOM   3037 O  O   . SER   A 1 383 ? 9.112  -7.823  9.681   1.00 18.45 ? 905  SER   A O   1 
ATOM   3038 C  CB  . SER   A 1 383 ? 10.033 -4.949  8.533   1.00 18.80 ? 905  SER   A CB  1 
ATOM   3039 O  OG  . SER   A 1 383 ? 9.257  -4.824  7.359   1.00 19.73 ? 905  SER   A OG  1 
ATOM   3040 N  N   . SER   A 1 384 ? 7.473  -6.717  8.570   1.00 18.89 ? 906  SER   A N   1 
ATOM   3041 C  CA  . SER   A 1 384 ? 6.840  -7.936  8.018   1.00 19.57 ? 906  SER   A CA  1 
ATOM   3042 C  C   . SER   A 1 384 ? 7.246  -8.048  6.546   1.00 19.42 ? 906  SER   A C   1 
ATOM   3043 O  O   . SER   A 1 384 ? 6.876  -9.015  5.902   1.00 22.26 ? 906  SER   A O   1 
ATOM   3044 C  CB  . SER   A 1 384 ? 5.333  -7.875  8.142   1.00 25.14 ? 906  SER   A CB  1 
ATOM   3045 O  OG  . SER   A 1 384 ? 4.929  -7.836  9.498   1.00 39.11 ? 906  SER   A OG  1 
ATOM   3046 N  N   . ARG   A 1 385 ? 7.982  -7.061  6.047   1.00 20.08 ? 907  ARG   A N   1 
ATOM   3047 C  CA  . ARG   A 1 385 ? 8.336  -7.062  4.608   1.00 19.31 ? 907  ARG   A CA  1 
ATOM   3048 C  C   . ARG   A 1 385 ? 9.591  -7.892  4.357   1.00 15.72 ? 907  ARG   A C   1 
ATOM   3049 O  O   . ARG   A 1 385 ? 10.311 -8.201  5.298   1.00 18.43 ? 907  ARG   A O   1 
ATOM   3050 C  CB  . ARG   A 1 385 ? 8.594  -5.652  4.079   1.00 22.79 ? 907  ARG   A CB  1 
ATOM   3051 C  CG  . ARG   A 1 385 ? 7.398  -4.724  4.228   1.00 34.30 ? 907  ARG   A CG  1 
ATOM   3052 C  CD  . ARG   A 1 385 ? 7.746  -3.283  3.934   1.00 45.85 ? 907  ARG   A CD  1 
ATOM   3053 N  NE  . ARG   A 1 385 ? 6.682  -2.393  4.370   1.00 69.29 ? 907  ARG   A NE  1 
ATOM   3054 C  CZ  . ARG   A 1 385 ? 6.735  -1.070  4.286   1.00 75.04 ? 907  ARG   A CZ  1 
ATOM   3055 N  NH1 . ARG   A 1 385 ? 5.821  -0.331  4.889   1.00 64.99 ? 907  ARG   A NH1 1 
ATOM   3056 N  NH2 . ARG   A 1 385 ? 7.708  -0.493  3.604   1.00 73.29 ? 907  ARG   A NH2 1 
ATOM   3057 N  N   . CYS   A 1 386 ? 9.782  -8.245  3.093   1.00 17.23 ? 908  CYS   A N   1 
ATOM   3058 C  CA  . CYS   A 1 386 ? 10.975 -9.006  2.729   1.00 17.87 ? 908  CYS   A CA  1 
ATOM   3059 C  C   . CYS   A 1 386 ? 12.233 -8.310  3.242   1.00 19.72 ? 908  CYS   A C   1 
ATOM   3060 O  O   . CYS   A 1 386 ? 12.456 -7.139  2.951   1.00 17.92 ? 908  CYS   A O   1 
ATOM   3061 C  CB  . CYS   A 1 386 ? 11.028 -9.138  1.205   1.00 18.95 ? 908  CYS   A CB  1 
ATOM   3062 S  SG  . CYS   A 1 386 ? 12.561 -9.796  0.495   1.00 15.06 ? 908  CYS   A SG  1 
ATOM   3063 N  N   . ARG   A 1 387 ? 13.064 -9.048  3.992   1.00 16.03 ? 909  ARG   A N   1 
ATOM   3064 C  CA  . ARG   A 1 387 ? 14.294 -8.485  4.554   1.00 18.82 ? 909  ARG   A CA  1 
ATOM   3065 C  C   . ARG   A 1 387 ? 15.246 -8.021  3.453   1.00 18.49 ? 909  ARG   A C   1 
ATOM   3066 O  O   . ARG   A 1 387 ? 15.897 -6.972  3.559   1.00 16.45 ? 909  ARG   A O   1 
ATOM   3067 C  CB  . ARG   A 1 387 ? 14.987 -9.540  5.417   1.00 18.38 ? 909  ARG   A CB  1 
ATOM   3068 C  CG  . ARG   A 1 387 ? 14.111 -10.252 6.436   1.00 19.18 ? 909  ARG   A CG  1 
ATOM   3069 C  CD  . ARG   A 1 387 ? 13.707 -9.361  7.612   1.00 20.35 ? 909  ARG   A CD  1 
ATOM   3070 N  NE  . ARG   A 1 387 ? 12.981 -10.159 8.593   1.00 15.58 ? 909  ARG   A NE  1 
ATOM   3071 C  CZ  . ARG   A 1 387 ? 12.327 -9.687  9.651   1.00 19.07 ? 909  ARG   A CZ  1 
ATOM   3072 N  NH1 . ARG   A 1 387 ? 12.327 -8.412  9.951   1.00 19.95 ? 909  ARG   A NH1 1 
ATOM   3073 N  NH2 . ARG   A 1 387 ? 11.651 -10.530 10.425  1.00 22.76 ? 909  ARG   A NH2 1 
ATOM   3074 N  N   . ARG   A 1 388 ? 15.362 -8.824  2.401   1.00 16.88 ? 910  ARG   A N   1 
ATOM   3075 C  CA  . ARG   A 1 388 ? 16.273 -8.483  1.318   1.00 15.59 ? 910  ARG   A CA  1 
ATOM   3076 C  C   . ARG   A 1 388 ? 15.811 -7.225  0.589   1.00 18.41 ? 910  ARG   A C   1 
ATOM   3077 O  O   . ARG   A 1 388 ? 16.629 -6.382  0.204   1.00 15.95 ? 910  ARG   A O   1 
ATOM   3078 C  CB  . ARG   A 1 388 ? 16.367 -9.679  0.371   1.00 13.37 ? 910  ARG   A CB  1 
ATOM   3079 C  CG  . ARG   A 1 388 ? 17.286 -9.475  -0.810  1.00 18.21 ? 910  ARG   A CG  1 
ATOM   3080 C  CD  . ARG   A 1 388 ? 17.484 -10.813 -1.521  1.00 16.52 ? 910  ARG   A CD  1 
ATOM   3081 N  NE  . ARG   A 1 388 ? 18.728 -11.416 -1.085  1.00 23.76 ? 910  ARG   A NE  1 
ATOM   3082 C  CZ  . ARG   A 1 388 ? 18.860 -12.346 -0.150  1.00 21.82 ? 910  ARG   A CZ  1 
ATOM   3083 N  NH1 . ARG   A 1 388 ? 17.805 -12.900 0.449   1.00 19.02 ? 910  ARG   A NH1 1 
ATOM   3084 N  NH2 . ARG   A 1 388 ? 20.080 -12.732 0.194   1.00 19.56 ? 910  ARG   A NH2 1 
ATOM   3085 N  N   . GLN   A 1 389 ? 14.500 -7.075  0.395   1.00 12.67 ? 911  GLN   A N   1 
ATOM   3086 C  CA  . GLN   A 1 389 ? 13.988 -5.874  -0.252  1.00 16.82 ? 911  GLN   A CA  1 
ATOM   3087 C  C   . GLN   A 1 389 ? 14.284 -4.640  0.580   1.00 15.32 ? 911  GLN   A C   1 
ATOM   3088 O  O   . GLN   A 1 389 ? 14.614 -3.585  0.031   1.00 17.02 ? 911  GLN   A O   1 
ATOM   3089 C  CB  . GLN   A 1 389 ? 12.477 -5.998  -0.499  1.00 15.47 ? 911  GLN   A CB  1 
ATOM   3090 C  CG  . GLN   A 1 389 ? 11.905 -4.765  -1.185  1.00 20.72 ? 911  GLN   A CG  1 
ATOM   3091 C  CD  . GLN   A 1 389 ? 12.555 -4.537  -2.533  1.00 34.66 ? 911  GLN   A CD  1 
ATOM   3092 O  OE1 . GLN   A 1 389 ? 12.434 -5.372  -3.430  1.00 40.98 ? 911  GLN   A OE1 1 
ATOM   3093 N  NE2 . GLN   A 1 389 ? 13.280 -3.415  -2.680  1.00 36.06 ? 911  GLN   A NE2 1 
ATOM   3094 N  N   . ILE   A 1 390 ? 14.182 -4.743  1.908   1.00 15.61 ? 912  ILE   A N   1 
ATOM   3095 C  CA  . ILE   A 1 390 ? 14.490 -3.587  2.754   1.00 14.85 ? 912  ILE   A CA  1 
ATOM   3096 C  C   . ILE   A 1 390 ? 15.944 -3.184  2.554   1.00 14.25 ? 912  ILE   A C   1 
ATOM   3097 O  O   . ILE   A 1 390 ? 16.273 -2.004  2.366   1.00 14.48 ? 912  ILE   A O   1 
ATOM   3098 C  CB  . ILE   A 1 390 ? 14.203 -3.899  4.236   1.00 13.61 ? 912  ILE   A CB  1 
ATOM   3099 C  CG1 . ILE   A 1 390 ? 12.719 -4.279  4.413   1.00 16.31 ? 912  ILE   A CG1 1 
ATOM   3100 C  CG2 . ILE   A 1 390 ? 14.588 -2.639  5.134   1.00 15.41 ? 912  ILE   A CG2 1 
ATOM   3101 C  CD1 . ILE   A 1 390 ? 12.354 -4.727  5.825   1.00 17.16 ? 912  ILE   A CD1 1 
ATOM   3102 N  N   . ILE   A 1 391 ? 16.837 -4.179  2.580   1.00 14.46 ? 913  ILE   A N   1 
ATOM   3103 C  CA  . ILE   A 1 391 ? 18.268 -3.895  2.418   1.00 11.69 ? 913  ILE   A CA  1 
ATOM   3104 C  C   . ILE   A 1 391 ? 18.533 -3.255  1.058   1.00 13.71 ? 913  ILE   A C   1 
ATOM   3105 O  O   . ILE   A 1 391 ? 19.190 -2.207  0.957   1.00 17.20 ? 913  ILE   A O   1 
ATOM   3106 C  CB  . ILE   A 1 391 ? 19.059 -5.196  2.612   1.00 15.55 ? 913  ILE   A CB  1 
ATOM   3107 C  CG1 . ILE   A 1 391 ? 18.912 -5.652  4.060   1.00 14.92 ? 913  ILE   A CG1 1 
ATOM   3108 C  CG2 . ILE   A 1 391 ? 20.553 -5.026  2.254   1.00 16.24 ? 913  ILE   A CG2 1 
ATOM   3109 C  CD1 . ILE   A 1 391 ? 19.391 -7.153  4.249   1.00 14.61 ? 913  ILE   A CD1 1 
ATOM   3110 N  N   . LEU   A 1 392 ? 18.011 -3.860  -0.011  1.00 14.25 ? 914  LEU   A N   1 
ATOM   3111 C  CA  . LEU   A 1 392 ? 18.314 -3.351  -1.342  1.00 16.09 ? 914  LEU   A CA  1 
ATOM   3112 C  C   . LEU   A 1 392 ? 17.711 -1.979  -1.566  1.00 20.14 ? 914  LEU   A C   1 
ATOM   3113 O  O   . LEU   A 1 392 ? 18.300 -1.173  -2.295  1.00 17.67 ? 914  LEU   A O   1 
ATOM   3114 C  CB  . LEU   A 1 392 ? 17.818 -4.300  -2.436  1.00 18.00 ? 914  LEU   A CB  1 
ATOM   3115 C  CG  . LEU   A 1 392 ? 18.511 -5.672  -2.485  1.00 19.88 ? 914  LEU   A CG  1 
ATOM   3116 C  CD1 . LEU   A 1 392 ? 17.797 -6.603  -3.458  1.00 20.18 ? 914  LEU   A CD1 1 
ATOM   3117 C  CD2 . LEU   A 1 392 ? 20.028 -5.533  -2.818  1.00 21.76 ? 914  LEU   A CD2 1 
ATOM   3118 N  N   . SER   A 1 393 ? 16.539 -1.707  -0.975  1.00 19.73 ? 915  SER   A N   1 
ATOM   3119 C  CA  . SER   A 1 393 ? 15.938 -0.388  -1.102  1.00 17.39 ? 915  SER   A CA  1 
ATOM   3120 C  C   . SER   A 1 393 ? 16.762 0.658   -0.384  1.00 18.69 ? 915  SER   A C   1 
ATOM   3121 O  O   . SER   A 1 393 ? 16.856 1.797   -0.845  1.00 23.31 ? 915  SER   A O   1 
ATOM   3122 C  CB  . SER   A 1 393 ? 14.529 -0.372  -0.534  1.00 17.68 ? 915  SER   A CB  1 
ATOM   3123 O  OG  . SER   A 1 393 ? 13.685 -0.991  -1.453  1.00 26.72 ? 915  SER   A OG  1 
ATOM   3124 N  N   . HIS   A 1 394 ? 17.332 0.306   0.766   1.00 15.84 ? 916  HIS   A N   1 
ATOM   3125 C  CA  . HIS   A 1 394 ? 18.165 1.283   1.452   1.00 17.81 ? 916  HIS   A CA  1 
ATOM   3126 C  C   . HIS   A 1 394 ? 19.479 1.523   0.711   1.00 20.13 ? 916  HIS   A C   1 
ATOM   3127 O  O   . HIS   A 1 394 ? 19.944 2.670   0.607   1.00 17.55 ? 916  HIS   A O   1 
ATOM   3128 C  CB  . HIS   A 1 394 ? 18.447 0.835   2.877   1.00 18.29 ? 916  HIS   A CB  1 
ATOM   3129 C  CG  . HIS   A 1 394 ? 19.290 1.810   3.624   1.00 22.02 ? 916  HIS   A CG  1 
ATOM   3130 N  ND1 . HIS   A 1 394 ? 18.816 3.038   4.021   1.00 28.12 ? 916  HIS   A ND1 1 
ATOM   3131 C  CD2 . HIS   A 1 394 ? 20.600 1.775   3.980   1.00 19.23 ? 916  HIS   A CD2 1 
ATOM   3132 C  CE1 . HIS   A 1 394 ? 19.786 3.706   4.628   1.00 30.25 ? 916  HIS   A CE1 1 
ATOM   3133 N  NE2 . HIS   A 1 394 ? 20.878 2.961   4.617   1.00 20.58 ? 916  HIS   A NE2 1 
ATOM   3134 N  N   . PHE   A 1 395 ? 20.111 0.459   0.216   1.00 16.08 ? 917  PHE   A N   1 
ATOM   3135 C  CA  . PHE   A 1 395 ? 21.477 0.578   -0.286  1.00 15.20 ? 917  PHE   A CA  1 
ATOM   3136 C  C   . PHE   A 1 395 ? 21.587 0.803   -1.781  1.00 16.89 ? 917  PHE   A C   1 
ATOM   3137 O  O   . PHE   A 1 395 ? 22.601 1.340   -2.236  1.00 17.25 ? 917  PHE   A O   1 
ATOM   3138 C  CB  . PHE   A 1 395 ? 22.273 -0.692  0.094   1.00 16.55 ? 917  PHE   A CB  1 
ATOM   3139 C  CG  . PHE   A 1 395 ? 22.649 -0.712  1.535   1.00 19.63 ? 917  PHE   A CG  1 
ATOM   3140 C  CD1 . PHE   A 1 395 ? 23.745 0.031   1.980   1.00 14.17 ? 917  PHE   A CD1 1 
ATOM   3141 C  CD2 . PHE   A 1 395 ? 21.877 -1.414  2.451   1.00 15.57 ? 917  PHE   A CD2 1 
ATOM   3142 C  CE1 . PHE   A 1 395 ? 24.075 0.049   3.335   1.00 17.52 ? 917  PHE   A CE1 1 
ATOM   3143 C  CE2 . PHE   A 1 395 ? 22.183 -1.404  3.799   1.00 16.32 ? 917  PHE   A CE2 1 
ATOM   3144 C  CZ  . PHE   A 1 395 ? 23.292 -0.671  4.248   1.00 16.27 ? 917  PHE   A CZ  1 
ATOM   3145 N  N   . GLU   A 1 396 ? 20.621 0.369   -2.586  1.00 19.21 ? 918  GLU   A N   1 
ATOM   3146 C  CA  . GLU   A 1 396 ? 20.840 0.324   -4.022  1.00 19.98 ? 918  GLU   A CA  1 
ATOM   3147 C  C   . GLU   A 1 396 ? 19.777 1.122   -4.753  1.00 23.07 ? 918  GLU   A C   1 
ATOM   3148 O  O   . GLU   A 1 396 ? 18.658 1.298   -4.257  1.00 21.60 ? 918  GLU   A O   1 
ATOM   3149 C  CB  . GLU   A 1 396 ? 20.844 -1.103  -4.534  1.00 16.67 ? 918  GLU   A CB  1 
ATOM   3150 C  CG  . GLU   A 1 396 ? 21.863 -1.994  -3.818  1.00 16.00 ? 918  GLU   A CG  1 
ATOM   3151 C  CD  . GLU   A 1 396 ? 23.317 -1.618  -4.089  1.00 22.06 ? 918  GLU   A CD  1 
ATOM   3152 O  OE1 . GLU   A 1 396 ? 23.623 -0.852  -5.037  1.00 20.60 ? 918  GLU   A OE1 1 
ATOM   3153 O  OE2 . GLU   A 1 396 ? 24.173 -2.128  -3.348  1.00 18.80 ? 918  GLU   A OE2 1 
ATOM   3154 N  N   . ASP   A 1 397 ? 20.124 1.608   -5.945  1.00 22.84 ? 919  ASP   A N   1 
ATOM   3155 C  CA  . ASP   A 1 397 ? 19.066 2.308   -6.652  1.00 29.51 ? 919  ASP   A CA  1 
ATOM   3156 C  C   . ASP   A 1 397 ? 18.108 1.294   -7.283  1.00 27.82 ? 919  ASP   A C   1 
ATOM   3157 O  O   . ASP   A 1 397 ? 18.329 0.079   -7.271  1.00 27.40 ? 919  ASP   A O   1 
ATOM   3158 C  CB  . ASP   A 1 397 ? 19.635 3.313   -7.661  1.00 32.30 ? 919  ASP   A CB  1 
ATOM   3159 C  CG  . ASP   A 1 397 ? 20.176 2.684   -8.928  1.00 36.12 ? 919  ASP   A CG  1 
ATOM   3160 O  OD1 . ASP   A 1 397 ? 20.037 1.472   -9.159  1.00 40.29 ? 919  ASP   A OD1 1 
ATOM   3161 O  OD2 . ASP   A 1 397 ? 20.768 3.438   -9.728  1.00 47.09 ? 919  ASP   A OD2 1 
ATOM   3162 N  N   . LYS   A 1 398 ? 17.040 1.816   -7.861  1.00 30.11 ? 920  LYS   A N   1 
ATOM   3163 C  CA  . LYS   A 1 398 ? 15.903 0.976   -8.220  1.00 30.01 ? 920  LYS   A CA  1 
ATOM   3164 C  C   . LYS   A 1 398 ? 16.268 -0.031  -9.302  1.00 33.56 ? 920  LYS   A C   1 
ATOM   3165 O  O   . LYS   A 1 398 ? 15.755 -1.154  -9.290  1.00 36.58 ? 920  LYS   A O   1 
ATOM   3166 C  CB  . LYS   A 1 398 ? 14.726 1.867   -8.644  1.00 33.02 ? 920  LYS   A CB  1 
ATOM   3167 C  CG  . LYS   A 1 398 ? 14.115 2.710   -7.504  1.00 48.14 ? 920  LYS   A CG  1 
ATOM   3168 C  CD  . LYS   A 1 398 ? 15.066 3.790   -6.895  1.00 59.23 ? 920  LYS   A CD  1 
ATOM   3169 C  CE  . LYS   A 1 398 ? 15.771 4.651   -7.947  1.00 50.19 ? 920  LYS   A CE  1 
ATOM   3170 N  NZ  . LYS   A 1 398 ? 16.983 5.282   -7.370  1.00 47.46 ? 920  LYS   A NZ  1 
ATOM   3171 N  N   . GLN   A 1 399 ? 17.182 0.329   -10.209 1.00 34.71 ? 921  GLN   A N   1 
ATOM   3172 C  CA  . GLN   A 1 399 ? 17.595 -0.608  -11.252 1.00 42.26 ? 921  GLN   A CA  1 
ATOM   3173 C  C   . GLN   A 1 399 ? 18.228 -1.865  -10.661 1.00 43.02 ? 921  GLN   A C   1 
ATOM   3174 O  O   . GLN   A 1 399 ? 17.976 -2.983  -11.134 1.00 39.39 ? 921  GLN   A O   1 
ATOM   3175 C  CB  . GLN   A 1 399 ? 18.567 0.073   -12.214 1.00 41.88 ? 921  GLN   A CB  1 
ATOM   3176 C  CG  . GLN   A 1 399 ? 18.087 1.427   -12.727 1.00 59.40 ? 921  GLN   A CG  1 
ATOM   3177 C  CD  . GLN   A 1 399 ? 19.074 2.081   -13.693 1.00 73.04 ? 921  GLN   A CD  1 
ATOM   3178 O  OE1 . GLN   A 1 399 ? 19.530 3.211   -13.473 1.00 70.51 ? 921  GLN   A OE1 1 
ATOM   3179 N  NE2 . GLN   A 1 399 ? 19.411 1.366   -14.772 1.00 67.93 ? 921  GLN   A NE2 1 
ATOM   3180 N  N   . VAL   A 1 400 ? 19.072 -1.704  -9.640  1.00 43.70 ? 922  VAL   A N   1 
ATOM   3181 C  CA  . VAL   A 1 400 ? 19.683 -2.868  -9.006  1.00 35.43 ? 922  VAL   A CA  1 
ATOM   3182 C  C   . VAL   A 1 400 ? 18.607 -3.758  -8.417  1.00 37.21 ? 922  VAL   A C   1 
ATOM   3183 O  O   . VAL   A 1 400 ? 18.609 -4.984  -8.600  1.00 41.93 ? 922  VAL   A O   1 
ATOM   3184 C  CB  . VAL   A 1 400 ? 20.697 -2.429  -7.936  1.00 34.54 ? 922  VAL   A CB  1 
ATOM   3185 C  CG1 . VAL   A 1 400 ? 21.322 -3.661  -7.272  1.00 33.02 ? 922  VAL   A CG1 1 
ATOM   3186 C  CG2 . VAL   A 1 400 ? 21.749 -1.522  -8.558  1.00 34.66 ? 922  VAL   A CG2 1 
ATOM   3187 N  N   . GLN   A 1 401 ? 17.651 -3.149  -7.723  1.00 36.50 ? 923  GLN   A N   1 
ATOM   3188 C  CA  . GLN   A 1 401 ? 16.592 -3.926  -7.102  1.00 37.44 ? 923  GLN   A CA  1 
ATOM   3189 C  C   . GLN   A 1 401 ? 15.788 -4.689  -8.148  1.00 43.41 ? 923  GLN   A C   1 
ATOM   3190 O  O   . GLN   A 1 401 ? 15.446 -5.857  -7.942  1.00 45.10 ? 923  GLN   A O   1 
ATOM   3191 C  CB  . GLN   A 1 401 ? 15.686 -3.006  -6.276  1.00 42.52 ? 923  GLN   A CB  1 
ATOM   3192 C  CG  . GLN   A 1 401 ? 16.438 -1.946  -5.447  1.00 31.63 ? 923  GLN   A CG  1 
ATOM   3193 C  CD  . GLN   A 1 401 ? 15.474 -0.947  -4.838  1.00 39.51 ? 923  GLN   A CD  1 
ATOM   3194 O  OE1 . GLN   A 1 401 ? 14.331 -1.295  -4.536  1.00 29.60 ? 923  GLN   A OE1 1 
ATOM   3195 N  NE2 . GLN   A 1 401 ? 15.918 0.307   -4.671  1.00 30.73 ? 923  GLN   A NE2 1 
ATOM   3196 N  N   . LYS   A 1 402 ? 15.497 -4.050  -9.290  1.00 35.45 ? 924  LYS   A N   1 
ATOM   3197 C  CA  . LYS   A 1 402 ? 14.675 -4.693  -10.316 1.00 41.24 ? 924  LYS   A CA  1 
ATOM   3198 C  C   . LYS   A 1 402 ? 15.452 -5.763  -11.062 1.00 36.46 ? 924  LYS   A C   1 
ATOM   3199 O  O   . LYS   A 1 402 ? 14.855 -6.680  -11.635 1.00 40.33 ? 924  LYS   A O   1 
ATOM   3200 C  CB  . LYS   A 1 402 ? 14.149 -3.658  -11.320 1.00 46.29 ? 924  LYS   A CB  1 
ATOM   3201 C  CG  . LYS   A 1 402 ? 13.065 -2.720  -10.798 1.00 54.27 ? 924  LYS   A CG  1 
ATOM   3202 C  CD  . LYS   A 1 402 ? 11.663 -3.195  -11.184 1.00 68.97 ? 924  LYS   A CD  1 
ATOM   3203 C  CE  . LYS   A 1 402 ? 10.665 -2.044  -11.140 1.00 67.00 ? 924  LYS   A CE  1 
ATOM   3204 N  NZ  . LYS   A 1 402 ? 10.935 -1.136  -9.991  1.00 66.39 ? 924  LYS   A NZ  1 
ATOM   3205 N  N   . ALA   A 1 403 ? 16.775 -5.639  -11.094 1.00 33.60 ? 925  ALA   A N   1 
ATOM   3206 C  CA  . ALA   A 1 403 ? 17.627 -6.615  -11.750 1.00 33.02 ? 925  ALA   A CA  1 
ATOM   3207 C  C   . ALA   A 1 403 ? 17.728 -7.909  -10.962 1.00 38.86 ? 925  ALA   A C   1 
ATOM   3208 O  O   . ALA   A 1 403 ? 18.122 -8.932  -11.531 1.00 38.67 ? 925  ALA   A O   1 
ATOM   3209 C  CB  . ALA   A 1 403 ? 19.029 -6.029  -11.950 1.00 29.71 ? 925  ALA   A CB  1 
ATOM   3210 N  N   . SER   A 1 404 ? 17.415 -7.874  -9.663  1.00 33.21 ? 926  SER   A N   1 
ATOM   3211 C  CA  . SER   A 1 404 ? 17.496 -9.074  -8.836  1.00 35.34 ? 926  SER   A CA  1 
ATOM   3212 C  C   . SER   A 1 404 ? 16.506 -10.115 -9.344  1.00 34.46 ? 926  SER   A C   1 
ATOM   3213 O  O   . SER   A 1 404 ? 15.330 -9.814  -9.563  1.00 33.00 ? 926  SER   A O   1 
ATOM   3214 C  CB  . SER   A 1 404 ? 17.202 -8.729  -7.376  1.00 29.36 ? 926  SER   A CB  1 
ATOM   3215 O  OG  . SER   A 1 404 ? 17.330 -9.882  -6.576  1.00 27.61 ? 926  SER   A OG  1 
ATOM   3216 N  N   . LEU   A 1 405 ? 16.985 -11.332 -9.562  1.00 28.72 ? 927  LEU   A N   1 
ATOM   3217 C  CA  . LEU   A 1 405 ? 16.151 -12.364 -10.157 1.00 27.71 ? 927  LEU   A CA  1 
ATOM   3218 C  C   . LEU   A 1 405 ? 16.396 -13.693 -9.462  1.00 33.23 ? 927  LEU   A C   1 
ATOM   3219 O  O   . LEU   A 1 405 ? 17.541 -14.141 -9.347  1.00 37.38 ? 927  LEU   A O   1 
ATOM   3220 C  CB  . LEU   A 1 405 ? 16.448 -12.489 -11.656 1.00 31.62 ? 927  LEU   A CB  1 
ATOM   3221 C  CG  . LEU   A 1 405 ? 15.692 -13.611 -12.365 1.00 39.28 ? 927  LEU   A CG  1 
ATOM   3222 C  CD1 . LEU   A 1 405 ? 14.264 -13.152 -12.674 1.00 38.53 ? 927  LEU   A CD1 1 
ATOM   3223 C  CD2 . LEU   A 1 405 ? 16.421 -14.051 -13.630 1.00 43.25 ? 927  LEU   A CD2 1 
ATOM   3224 N  N   . GLY   A 1 406 ? 15.327 -14.319 -8.989  1.00 26.66 ? 928  GLY   A N   1 
ATOM   3225 C  CA  . GLY   A 1 406 ? 15.416 -15.681 -8.524  1.00 28.36 ? 928  GLY   A CA  1 
ATOM   3226 C  C   . GLY   A 1 406 ? 15.677 -15.884 -7.050  1.00 24.51 ? 928  GLY   A C   1 
ATOM   3227 O  O   . GLY   A 1 406 ? 15.878 -17.031 -6.641  1.00 28.01 ? 928  GLY   A O   1 
ATOM   3228 N  N   . ILE   A 1 407 ? 15.681 -14.829 -6.221  1.00 21.81 ? 929  ILE   A N   1 
ATOM   3229 C  CA  . ILE   A 1 407 ? 15.819 -15.004 -4.778  1.00 19.19 ? 929  ILE   A CA  1 
ATOM   3230 C  C   . ILE   A 1 407 ? 14.648 -14.387 -4.005  1.00 19.43 ? 929  ILE   A C   1 
ATOM   3231 O  O   . ILE   A 1 407 ? 14.002 -15.064 -3.194  1.00 16.93 ? 929  ILE   A O   1 
ATOM   3232 C  CB  . ILE   A 1 407 ? 17.178 -14.468 -4.259  1.00 18.38 ? 929  ILE   A CB  1 
ATOM   3233 C  CG1 . ILE   A 1 407 ? 17.244 -14.647 -2.743  1.00 18.03 ? 929  ILE   A CG1 1 
ATOM   3234 C  CG2 . ILE   A 1 407 ? 17.462 -13.024 -4.683  1.00 22.10 ? 929  ILE   A CG2 1 
ATOM   3235 C  CD1 . ILE   A 1 407 ? 17.141 -16.085 -2.343  1.00 21.29 ? 929  ILE   A CD1 1 
ATOM   3236 N  N   . MET   A 1 408 ? 14.374 -13.093 -4.208  1.00 19.68 ? 930  MET   A N   1 
ATOM   3237 C  CA  . MET   A 1 408 ? 13.301 -12.466 -3.435  1.00 17.95 ? 930  MET   A CA  1 
ATOM   3238 C  C   . MET   A 1 408 ? 11.964 -13.158 -3.726  1.00 17.98 ? 930  MET   A C   1 
ATOM   3239 O  O   . MET   A 1 408 ? 11.673 -13.520 -4.865  1.00 19.20 ? 930  MET   A O   1 
ATOM   3240 C  CB  . MET   A 1 408 ? 13.207 -10.968 -3.740  1.00 17.96 ? 930  MET   A CB  1 
ATOM   3241 C  CG  . MET   A 1 408 ? 14.359 -10.184 -3.089  1.00 24.12 ? 930  MET   A CG  1 
ATOM   3242 S  SD  . MET   A 1 408 ? 14.130 -8.403  -3.163  1.00 22.42 ? 930  MET   A SD  1 
ATOM   3243 C  CE  . MET   A 1 408 ? 14.336 -8.200  -4.930  1.00 23.22 ? 930  MET   A CE  1 
ATOM   3244 N  N   . GLY   A 1 409 ? 11.149 -13.323 -2.698  1.00 16.40 ? 931  GLY   A N   1 
ATOM   3245 C  CA  . GLY   A 1 409 ? 9.867  -13.979 -2.892  1.00 15.84 ? 931  GLY   A CA  1 
ATOM   3246 C  C   . GLY   A 1 409 ? 9.918  -15.487 -2.889  1.00 21.64 ? 931  GLY   A C   1 
ATOM   3247 O  O   . GLY   A 1 409 ? 8.889  -16.114 -3.138  1.00 19.04 ? 931  GLY   A O   1 
ATOM   3248 N  N   . THR   A 1 410 ? 11.078 -16.097 -2.632  1.00 16.41 ? 932  THR   A N   1 
ATOM   3249 C  CA  . THR   A 1 410 ? 11.201 -17.552 -2.574  1.00 18.00 ? 932  THR   A CA  1 
ATOM   3250 C  C   . THR   A 1 410 ? 11.496 -18.003 -1.146  1.00 20.39 ? 932  THR   A C   1 
ATOM   3251 O  O   . THR   A 1 410 ? 11.875 -17.209 -0.281  1.00 19.11 ? 932  THR   A O   1 
ATOM   3252 C  CB  . THR   A 1 410 ? 12.307 -18.061 -3.504  1.00 20.25 ? 932  THR   A CB  1 
ATOM   3253 O  OG1 . THR   A 1 410 ? 13.590 -17.748 -2.940  1.00 17.93 ? 932  THR   A OG1 1 
ATOM   3254 C  CG2 . THR   A 1 410 ? 12.183 -17.464 -4.900  1.00 22.24 ? 932  THR   A CG2 1 
ATOM   3255 N  N   . GLU   A 1 411 ? 11.353 -19.312 -0.918  1.00 17.80 ? 933  GLU   A N   1 
ATOM   3256 C  CA  . GLU   A 1 411 ? 11.631 -19.909 0.392   1.00 20.90 ? 933  GLU   A CA  1 
ATOM   3257 C  C   . GLU   A 1 411 ? 13.066 -19.705 0.850   1.00 20.51 ? 933  GLU   A C   1 
ATOM   3258 O  O   . GLU   A 1 411 ? 13.316 -19.695 2.062   1.00 23.41 ? 933  GLU   A O   1 
ATOM   3259 C  CB  . GLU   A 1 411 ? 11.289 -21.418 0.372   1.00 21.32 ? 933  GLU   A CB  1 
ATOM   3260 C  CG  . GLU   A 1 411 ? 9.832  -21.594 0.788   1.00 27.18 ? 933  GLU   A CG  1 
ATOM   3261 C  CD  . GLU   A 1 411 ? 9.164  -22.887 0.383   1.00 56.71 ? 933  GLU   A CD  1 
ATOM   3262 O  OE1 . GLU   A 1 411 ? 9.882  -23.839 0.009   1.00 51.06 ? 933  GLU   A OE1 1 
ATOM   3263 O  OE2 . GLU   A 1 411 ? 7.895  -22.931 0.440   1.00 39.15 ? 933  GLU   A OE2 1 
ATOM   3264 N  N   . LYS   A 1 412 ? 14.008 -19.524 -0.071  1.00 20.87 ? 934  LYS   A N   1 
ATOM   3265 C  CA  . LYS   A 1 412 ? 15.411 -19.322 0.272   1.00 17.00 ? 934  LYS   A CA  1 
ATOM   3266 C  C   . LYS   A 1 412 ? 15.755 -17.868 0.623   1.00 17.44 ? 934  LYS   A C   1 
ATOM   3267 O  O   . LYS   A 1 412 ? 16.879 -17.607 1.047   1.00 16.80 ? 934  LYS   A O   1 
ATOM   3268 C  CB  . LYS   A 1 412 ? 16.298 -19.796 -0.897  1.00 21.08 ? 934  LYS   A CB  1 
ATOM   3269 C  CG  . LYS   A 1 412 ? 16.272 -21.336 -1.152  1.00 33.97 ? 934  LYS   A CG  1 
ATOM   3270 C  CD  . LYS   A 1 412 ? 14.883 -21.976 -1.499  1.00 44.87 ? 934  LYS   A CD  1 
ATOM   3271 C  CE  . LYS   A 1 412 ? 14.179 -21.358 -2.726  1.00 37.22 ? 934  LYS   A CE  1 
ATOM   3272 N  NZ  . LYS   A 1 412 ? 12.995 -22.150 -3.214  1.00 44.81 ? 934  LYS   A NZ  1 
ATOM   3273 N  N   . CYS   A 1 413 ? 14.821 -16.918 0.490   1.00 16.40 ? 935  CYS   A N   1 
ATOM   3274 C  CA  . CYS   A 1 413 ? 15.176 -15.497 0.616   1.00 14.31 ? 935  CYS   A CA  1 
ATOM   3275 C  C   . CYS   A 1 413 ? 15.245 -15.059 2.069   1.00 13.74 ? 935  CYS   A C   1 
ATOM   3276 O  O   . CYS   A 1 413 ? 16.313 -14.682 2.566   1.00 14.16 ? 935  CYS   A O   1 
ATOM   3277 C  CB  . CYS   A 1 413 ? 14.168 -14.627 -0.139  1.00 16.40 ? 935  CYS   A CB  1 
ATOM   3278 S  SG  . CYS   A 1 413 ? 14.456 -12.842 0.135   1.00 16.23 ? 935  CYS   A SG  1 
ATOM   3279 N  N   . CYS   A 1 414 ? 14.119 -15.117 2.781   1.00 14.91 ? 936  CYS   A N   1 
ATOM   3280 C  CA  . CYS   A 1 414 ? 14.087 -14.609 4.146   1.00 14.24 ? 936  CYS   A CA  1 
ATOM   3281 C  C   . CYS   A 1 414 ? 12.875 -15.168 4.874   1.00 15.54 ? 936  CYS   A C   1 
ATOM   3282 O  O   . CYS   A 1 414 ? 11.990 -15.784 4.265   1.00 15.62 ? 936  CYS   A O   1 
ATOM   3283 C  CB  . CYS   A 1 414 ? 14.070 -13.075 4.161   1.00 15.51 ? 936  CYS   A CB  1 
ATOM   3284 S  SG  . CYS   A 1 414 ? 12.498 -12.316 3.542   1.00 15.15 ? 936  CYS   A SG  1 
ATOM   3285 N  N   . ASP   A 1 415 ? 12.838 -14.934 6.195   1.00 13.59 ? 937  ASP   A N   1 
ATOM   3286 C  CA  . ASP   A 1 415 ? 11.740 -15.459 7.008   1.00 16.20 ? 937  ASP   A CA  1 
ATOM   3287 C  C   . ASP   A 1 415 ? 10.389 -14.918 6.556   1.00 19.99 ? 937  ASP   A C   1 
ATOM   3288 O  O   . ASP   A 1 415 ? 9.397  -15.656 6.553   1.00 16.11 ? 937  ASP   A O   1 
ATOM   3289 C  CB  . ASP   A 1 415 ? 11.974 -15.168 8.499   1.00 18.54 ? 937  ASP   A CB  1 
ATOM   3290 C  CG  . ASP   A 1 415 ? 12.278 -13.681 8.810   1.00 18.61 ? 937  ASP   A CG  1 
ATOM   3291 O  OD1 . ASP   A 1 415 ? 12.427 -12.852 7.894   1.00 18.03 ? 937  ASP   A OD1 1 
ATOM   3292 O  OD2 . ASP   A 1 415 ? 12.377 -13.346 10.009  1.00 15.36 ? 937  ASP   A OD2 1 
ATOM   3293 N  N   . ASN   A 1 416 ? 10.318 -13.630 6.180   1.00 17.05 ? 938  ASN   A N   1 
ATOM   3294 C  CA  . ASN   A 1 416 ? 9.035  -13.056 5.801   1.00 16.01 ? 938  ASN   A CA  1 
ATOM   3295 C  C   . ASN   A 1 416 ? 8.567  -13.579 4.446   1.00 16.64 ? 938  ASN   A C   1 
ATOM   3296 O  O   . ASN   A 1 416 ? 7.370  -13.809 4.247   1.00 17.16 ? 938  ASN   A O   1 
ATOM   3297 C  CB  . ASN   A 1 416 ? 9.127  -11.513 5.839   1.00 16.09 ? 938  ASN   A CB  1 
ATOM   3298 C  CG  . ASN   A 1 416 ? 9.166  -10.999 7.263   1.00 20.55 ? 938  ASN   A CG  1 
ATOM   3299 O  OD1 . ASN   A 1 416 ? 8.659  -11.670 8.168   1.00 20.23 ? 938  ASN   A OD1 1 
ATOM   3300 N  ND2 . ASN   A 1 416 ? 9.786  -9.829  7.488   1.00 17.97 ? 938  ASN   A ND2 1 
ATOM   3301 N  N   . CYS   A 1 417 ? 9.494  -13.818 3.505   1.00 16.98 ? 939  CYS   A N   1 
ATOM   3302 C  CA  . CYS   A 1 417 ? 9.083  -14.428 2.243   1.00 14.84 ? 939  CYS   A CA  1 
ATOM   3303 C  C   . CYS   A 1 417 ? 8.565  -15.852 2.475   1.00 16.80 ? 939  CYS   A C   1 
ATOM   3304 O  O   . CYS   A 1 417 ? 7.551  -16.271 1.877   1.00 17.14 ? 939  CYS   A O   1 
ATOM   3305 C  CB  . CYS   A 1 417 ? 10.249 -14.447 1.249   1.00 17.17 ? 939  CYS   A CB  1 
ATOM   3306 S  SG  . CYS   A 1 417 ? 10.566 -12.826 0.478   1.00 15.82 ? 939  CYS   A SG  1 
ATOM   3307 N  N   . ARG   A 1 418 ? 9.259  -16.603 3.346   1.00 16.06 ? 940  ARG   A N   1 
ATOM   3308 C  CA  . ARG   A 1 418 ? 8.807  -17.947 3.703   1.00 16.91 ? 940  ARG   A CA  1 
ATOM   3309 C  C   . ARG   A 1 418 ? 7.417  -17.905 4.287   1.00 20.53 ? 940  ARG   A C   1 
ATOM   3310 O  O   . ARG   A 1 418 ? 6.552  -18.691 3.897   1.00 18.80 ? 940  ARG   A O   1 
ATOM   3311 C  CB  . ARG   A 1 418 ? 9.746  -18.597 4.711   1.00 16.69 ? 940  ARG   A CB  1 
ATOM   3312 C  CG  . ARG   A 1 418 ? 10.924 -19.254 4.107   1.00 24.79 ? 940  ARG   A CG  1 
ATOM   3313 C  CD  . ARG   A 1 418 ? 11.671 -20.005 5.192   1.00 25.40 ? 940  ARG   A CD  1 
ATOM   3314 N  NE  . ARG   A 1 418 ? 12.945 -20.464 4.677   1.00 28.26 ? 940  ARG   A NE  1 
ATOM   3315 C  CZ  . ARG   A 1 418 ? 13.841 -21.106 5.407   1.00 29.39 ? 940  ARG   A CZ  1 
ATOM   3316 N  NH1 . ARG   A 1 418 ? 13.669 -21.282 6.707   1.00 31.84 ? 940  ARG   A NH1 1 
ATOM   3317 N  NH2 . ARG   A 1 418 ? 14.932 -21.586 4.816   1.00 33.73 ? 940  ARG   A NH2 1 
ATOM   3318 N  N   . SER   A 1 419 ? 7.195  -17.010 5.253   1.00 16.92 ? 941  SER   A N   1 
ATOM   3319 C  CA  . SER   A 1 419 ? 5.881  -16.895 5.879   1.00 21.58 ? 941  SER   A CA  1 
ATOM   3320 C  C   . SER   A 1 419 ? 4.792  -16.555 4.867   1.00 25.98 ? 941  SER   A C   1 
ATOM   3321 O  O   . SER   A 1 419 ? 3.647  -17.006 5.013   1.00 21.75 ? 941  SER   A O   1 
ATOM   3322 C  CB  . SER   A 1 419 ? 5.927  -15.833 6.984   1.00 22.97 ? 941  SER   A CB  1 
ATOM   3323 O  OG  . SER   A 1 419 ? 5.825  -14.528 6.426   1.00 34.38 ? 941  SER   A OG  1 
ATOM   3324 N  N   . ARG   A 1 420 ? 5.111  -15.789 3.823   1.00 20.94 ? 942  ARG   A N   1 
ATOM   3325 C  CA  . ARG   A 1 420 ? 4.045  -15.506 2.861   1.00 17.92 ? 942  ARG   A CA  1 
ATOM   3326 C  C   . ARG   A 1 420 ? 3.781  -16.653 1.894   1.00 19.03 ? 942  ARG   A C   1 
ATOM   3327 O  O   . ARG   A 1 420 ? 2.804  -16.590 1.133   1.00 20.75 ? 942  ARG   A O   1 
ATOM   3328 C  CB  . ARG   A 1 420 ? 4.350  -14.238 2.071   1.00 21.47 ? 942  ARG   A CB  1 
ATOM   3329 C  CG  . ARG   A 1 420 ? 3.732  -13.009 2.715   1.00 28.32 ? 942  ARG   A CG  1 
ATOM   3330 C  CD  . ARG   A 1 420 ? 3.959  -11.790 1.857   1.00 29.74 ? 942  ARG   A CD  1 
ATOM   3331 N  NE  . ARG   A 1 420 ? 5.315  -11.326 2.063   1.00 30.81 ? 942  ARG   A NE  1 
ATOM   3332 C  CZ  . ARG   A 1 420 ? 5.670  -10.541 3.069   1.00 30.57 ? 942  ARG   A CZ  1 
ATOM   3333 N  NH1 . ARG   A 1 420 ? 4.798  -10.156 3.986   1.00 37.81 ? 942  ARG   A NH1 1 
ATOM   3334 N  NH2 . ARG   A 1 420 ? 6.922  -10.110 3.143   1.00 36.85 ? 942  ARG   A NH2 1 
ATOM   3335 N  N   . LEU   A 1 421 ? 4.620  -17.681 1.881   1.00 17.87 ? 943  LEU   A N   1 
ATOM   3336 C  CA  . LEU   A 1 421 ? 4.319  -18.858 1.079   1.00 22.13 ? 943  LEU   A CA  1 
ATOM   3337 C  C   . LEU   A 1 421 ? 3.595  -19.952 1.859   1.00 21.07 ? 943  LEU   A C   1 
ATOM   3338 O  O   . LEU   A 1 421 ? 2.987  -20.829 1.244   1.00 23.57 ? 943  LEU   A O   1 
ATOM   3339 C  CB  . LEU   A 1 421 ? 5.607  -19.449 0.502   1.00 17.09 ? 943  LEU   A CB  1 
ATOM   3340 C  CG  . LEU   A 1 421 ? 6.237  -18.594 -0.596  1.00 19.25 ? 943  LEU   A CG  1 
ATOM   3341 C  CD1 . LEU   A 1 421 ? 7.732  -18.907 -0.712  1.00 15.65 ? 943  LEU   A CD1 1 
ATOM   3342 C  CD2 . LEU   A 1 421 ? 5.536  -18.786 -1.941  1.00 16.56 ? 943  LEU   A CD2 1 
ATOM   3343 N  N   . ASP   A 1 422 ? 3.682  -19.934 3.188   1.00 21.83 ? 944  ASP   A N   1 
ATOM   3344 C  CA  . ASP   A 1 422 ? 3.127  -20.982 4.036   1.00 22.02 ? 944  ASP   A CA  1 
ATOM   3345 C  C   . ASP   A 1 422 ? 1.723  -20.620 4.440   1.00 35.45 ? 944  ASP   A C   1 
ATOM   3346 O  O   . ASP   A 1 422 ? 1.137  -19.657 3.950   1.00 37.28 ? 944  ASP   A O   1 
ATOM   3347 C  CB  . ASP   A 1 422 ? 3.924  -21.149 5.317   1.00 39.44 ? 944  ASP   A CB  1 
ATOM   3348 C  CG  . ASP   A 1 422 ? 5.194  -21.827 5.099   1.00 37.24 ? 944  ASP   A CG  1 
ATOM   3349 O  OD1 . ASP   A 1 422 ? 5.374  -22.365 3.973   1.00 41.89 ? 944  ASP   A OD1 1 
ATOM   3350 O  OD2 . ASP   A 1 422 ? 6.016  -21.796 6.050   1.00 31.30 ? 944  ASP   A OD2 1 
ATOM   3351 N  N   . HIS   A 1 423 ? 1.173  -21.352 5.379   1.00 40.56 ? 945  HIS   A N   1 
ATOM   3352 C  CA  . HIS   A 1 423 ? -0.181 -21.013 5.740   1.00 61.69 ? 945  HIS   A CA  1 
ATOM   3353 C  C   . HIS   A 1 423 ? -0.163 -19.790 6.635   1.00 62.85 ? 945  HIS   A C   1 
ATOM   3354 O  O   . HIS   A 1 423 ? 0.665  -19.687 7.552   1.00 57.83 ? 945  HIS   A O   1 
ATOM   3355 C  CB  . HIS   A 1 423 ? -0.897 -22.165 6.405   1.00 59.86 ? 945  HIS   A CB  1 
ATOM   3356 C  CG  . HIS   A 1 423 ? -2.354 -22.154 6.118   1.00 62.69 ? 945  HIS   A CG  1 
ATOM   3357 N  ND1 . HIS   A 1 423 ? -3.305 -22.446 7.069   1.00 56.34 ? 945  HIS   A ND1 1 
ATOM   3358 C  CD2 . HIS   A 1 423 ? -3.026 -21.840 4.985   1.00 45.85 ? 945  HIS   A CD2 1 
ATOM   3359 C  CE1 . HIS   A 1 423 ? -4.505 -22.335 6.528   1.00 66.49 ? 945  HIS   A CE1 1 
ATOM   3360 N  NE2 . HIS   A 1 423 ? -4.364 -21.972 5.265   1.00 61.44 ? 945  HIS   A NE2 1 
ATOM   3361 N  N   . CYS   A 1 424 ? -1.052 -18.849 6.323   1.00 60.31 ? 946  CYS   A N   1 
ATOM   3362 C  CA  . CYS   A 1 424 ? -1.154 -17.573 7.013   1.00 62.67 ? 946  CYS   A CA  1 
ATOM   3363 C  C   . CYS   A 1 424 ? -2.574 -17.407 7.561   1.00 80.99 ? 946  CYS   A C   1 
ATOM   3364 O  O   . CYS   A 1 424 ? -3.291 -16.457 7.213   1.00 77.33 ? 946  CYS   A O   1 
ATOM   3365 C  CB  . CYS   A 1 424 ? -0.803 -16.413 6.068   1.00 58.61 ? 946  CYS   A CB  1 
ATOM   3366 S  SG  . CYS   A 1 424 ? 0.672  -16.660 4.991   1.00 50.40 ? 946  CYS   A SG  1 
ATOM   3367 O  OXT . CYS   A 1 424 ? -3.043 -18.233 8.352   1.00 77.18 ? 946  CYS   A OXT 1 
HETATM 3368 C  C4  . A1CA5 B 2 .   ? 31.595 -2.099  1.750   1.00 16.51 ? 1001 A1CA5 A C4  1 
HETATM 3369 C  C6  . A1CA5 B 2 .   ? 30.555 -4.282  1.885   1.00 13.83 ? 1001 A1CA5 A C6  1 
HETATM 3370 C  C7  . A1CA5 B 2 .   ? 30.030 -5.464  1.097   1.00 14.60 ? 1001 A1CA5 A C7  1 
HETATM 3371 C  C8  . A1CA5 B 2 .   ? 29.138 -6.347  1.974   1.00 15.51 ? 1001 A1CA5 A C8  1 
HETATM 3372 C  C10 . A1CA5 B 2 .   ? 27.485 -8.014  1.149   1.00 15.93 ? 1001 A1CA5 A C10 1 
HETATM 3373 C  C13 . A1CA5 B 2 .   ? 24.441 -7.438  0.283   1.00 18.89 ? 1001 A1CA5 A C13 1 
HETATM 3374 C  C15 . A1CA5 B 2 .   ? 23.164 -7.812  -0.052  1.00 18.74 ? 1001 A1CA5 A C15 1 
HETATM 3375 C  C17 . A1CA5 B 2 .   ? 20.971 -8.895  0.545   1.00 19.13 ? 1001 A1CA5 A C17 1 
HETATM 3376 C  C21 . A1CA5 B 2 .   ? 29.878 -8.349  0.743   1.00 15.00 ? 1001 A1CA5 A C21 1 
HETATM 3377 C  C22 . A1CA5 B 2 .   ? 30.719 -7.512  -0.202  1.00 15.43 ? 1001 A1CA5 A C22 1 
HETATM 3378 C  C26 . A1CA5 B 2 .   ? 34.415 -6.984  2.411   1.00 13.74 ? 1001 A1CA5 A C26 1 
HETATM 3379 C  C1  . A1CA5 B 2 .   ? 35.338 -2.566  2.231   1.00 29.16 ? 1001 A1CA5 A C1  1 
HETATM 3380 C  C11 . A1CA5 B 2 .   ? 26.402 -7.209  1.841   1.00 13.52 ? 1001 A1CA5 A C11 1 
HETATM 3381 C  C12 . A1CA5 B 2 .   ? 25.017 -7.709  1.503   1.00 15.33 ? 1001 A1CA5 A C12 1 
HETATM 3382 C  C16 . A1CA5 B 2 .   ? 22.391 -8.505  0.867   1.00 18.40 ? 1001 A1CA5 A C16 1 
HETATM 3383 C  C18 . A1CA5 B 2 .   ? 22.949 -8.795  2.102   1.00 23.41 ? 1001 A1CA5 A C18 1 
HETATM 3384 C  C19 . A1CA5 B 2 .   ? 24.238 -8.406  2.418   1.00 21.25 ? 1001 A1CA5 A C19 1 
HETATM 3385 C  C23 . A1CA5 B 2 .   ? 31.210 -6.255  0.503   1.00 15.97 ? 1001 A1CA5 A C23 1 
HETATM 3386 C  C25 . A1CA5 B 2 .   ? 33.513 -6.640  1.250   1.00 20.98 ? 1001 A1CA5 A C25 1 
HETATM 3387 C  C27 . A1CA5 B 2 .   ? 35.010 -8.380  2.277   1.00 18.15 ? 1001 A1CA5 A C27 1 
HETATM 3388 C  C29 . A1CA5 B 2 .   ? 33.045 -9.901  2.622   1.00 15.42 ? 1001 A1CA5 A C29 1 
HETATM 3389 C  C3  . A1CA5 B 2 .   ? 33.067 -2.327  1.408   1.00 17.60 ? 1001 A1CA5 A C3  1 
HETATM 3390 C  C31 . A1CA5 B 2 .   ? 32.692 -10.576 0.507   1.00 14.47 ? 1001 A1CA5 A C31 1 
HETATM 3391 C  C32 . A1CA5 B 2 .   ? 33.828 -9.771  0.508   1.00 14.80 ? 1001 A1CA5 A C32 1 
HETATM 3392 C  C33 . A1CA5 B 2 .   ? 34.541 -9.522  -0.647  1.00 20.06 ? 1001 A1CA5 A C33 1 
HETATM 3393 C  C34 . A1CA5 B 2 .   ? 34.093 -10.105 -1.826  1.00 17.95 ? 1001 A1CA5 A C34 1 
HETATM 3394 C  C38 . A1CA5 B 2 .   ? 34.284 -7.514  -3.693  1.00 26.04 ? 1001 A1CA5 A C38 1 
HETATM 3395 C  C39 . A1CA5 B 2 .   ? 32.850 -7.185  -3.969  1.00 31.84 ? 1001 A1CA5 A C39 1 
HETATM 3396 C  C41 . A1CA5 B 2 .   ? 32.946 -10.906 -1.837  1.00 22.00 ? 1001 A1CA5 A C41 1 
HETATM 3397 C  C42 . A1CA5 B 2 .   ? 32.238 -11.151 -0.670  1.00 15.53 ? 1001 A1CA5 A C42 1 
HETATM 3398 C  C46 . A1CA5 B 2 .   ? 31.154 -0.727  1.232   1.00 16.76 ? 1001 A1CA5 A C46 1 
HETATM 3399 C  C47 . A1CA5 B 2 .   ? 29.709 -0.352  1.552   1.00 13.58 ? 1001 A1CA5 A C47 1 
HETATM 3400 C  C48 . A1CA5 B 2 .   ? 29.406 1.068   1.080   1.00 14.98 ? 1001 A1CA5 A C48 1 
HETATM 3401 C  C49 . A1CA5 B 2 .   ? 27.997 1.520   1.449   1.00 18.60 ? 1001 A1CA5 A C49 1 
HETATM 3402 C  C50 . A1CA5 B 2 .   ? 27.757 1.400   2.938   1.00 19.55 ? 1001 A1CA5 A C50 1 
HETATM 3403 C  C51 . A1CA5 B 2 .   ? 28.016 -0.014  3.407   1.00 16.80 ? 1001 A1CA5 A C51 1 
HETATM 3404 C  C52 . A1CA5 B 2 .   ? 29.428 -0.462  3.045   1.00 15.60 ? 1001 A1CA5 A C52 1 
HETATM 3405 F  F14 . A1CA5 B 2 .   ? 25.188 -6.803  -0.634  1.00 23.78 ? 1001 A1CA5 A F14 1 
HETATM 3406 N  N2  . A1CA5 B 2 .   ? 33.917 -2.346  2.423   1.00 20.73 ? 1001 A1CA5 A N2  1 
HETATM 3407 N  N24 . A1CA5 B 2 .   ? 32.207 -6.574  1.517   1.00 16.83 ? 1001 A1CA5 A N24 1 
HETATM 3408 N  N28 . A1CA5 B 2 .   ? 34.025 -9.360  1.818   1.00 19.18 ? 1001 A1CA5 A N28 1 
HETATM 3409 N  N30 . A1CA5 B 2 .   ? 32.238 -10.638 1.810   1.00 15.77 ? 1001 A1CA5 A N30 1 
HETATM 3410 N  N35 . A1CA5 B 2 .   ? 34.936 -10.045 -2.972  1.00 29.81 ? 1001 A1CA5 A N35 1 
HETATM 3411 N  N5  . A1CA5 B 2 .   ? 30.834 -3.189  1.169   1.00 14.60 ? 1001 A1CA5 A N5  1 
HETATM 3412 N  N9  . A1CA5 B 2 .   ? 28.753 -7.574  1.274   1.00 14.97 ? 1001 A1CA5 A N9  1 
HETATM 3413 O  O20 . A1CA5 B 2 .   ? 27.212 -9.033  0.547   1.00 15.13 ? 1001 A1CA5 A O20 1 
HETATM 3414 O  O37 . A1CA5 B 2 .   ? 36.006 -9.034  -4.929  1.00 36.83 ? 1001 A1CA5 A O37 1 
HETATM 3415 O  O40 . A1CA5 B 2 .   ? 33.639 -9.697  -4.971  1.00 37.51 ? 1001 A1CA5 A O40 1 
HETATM 3416 O  O43 . A1CA5 B 2 .   ? 32.956 -9.760  3.830   1.00 17.56 ? 1001 A1CA5 A O43 1 
HETATM 3417 O  O44 . A1CA5 B 2 .   ? 33.964 -6.434  0.134   1.00 19.69 ? 1001 A1CA5 A O44 1 
HETATM 3418 O  O45 . A1CA5 B 2 .   ? 30.682 -4.331  3.100   1.00 16.75 ? 1001 A1CA5 A O45 1 
HETATM 3419 O  O53 . A1CA5 B 2 .   ? 33.414 -2.471  0.246   1.00 17.84 ? 1001 A1CA5 A O53 1 
HETATM 3420 S  S36 . A1CA5 B 2 .   ? 34.740 -9.111  -4.279  1.00 28.50 ? 1001 A1CA5 A S36 1 
HETATM 3421 ZN ZN  . ZN    C 3 .   ? 12.592 -12.027 1.266   1.00 16.18 ? 1002 ZN    A ZN  1 
HETATM 3422 O  O   . HOH   D 4 .   ? 20.409 20.521  19.865  1.00 40.86 ? 1101 HOH   A O   1 
HETATM 3423 O  O   . HOH   D 4 .   ? 47.147 -9.027  -6.379  1.00 48.32 ? 1102 HOH   A O   1 
HETATM 3424 O  O   . HOH   D 4 .   ? 23.105 24.725  -16.432 1.00 39.14 ? 1103 HOH   A O   1 
HETATM 3425 O  O   . HOH   D 4 .   ? 42.998 12.666  1.230   1.00 43.91 ? 1104 HOH   A O   1 
HETATM 3426 O  O   . HOH   D 4 .   ? 29.996 22.176  0.303   1.00 34.05 ? 1105 HOH   A O   1 
HETATM 3427 O  O   . HOH   D 4 .   ? 22.918 -12.094 -8.238  1.00 34.03 ? 1106 HOH   A O   1 
HETATM 3428 O  O   . HOH   D 4 .   ? 20.109 11.195  0.361   1.00 37.27 ? 1107 HOH   A O   1 
HETATM 3429 O  O   . HOH   D 4 .   ? 22.326 12.547  8.542   1.00 24.99 ? 1108 HOH   A O   1 
HETATM 3430 O  O   . HOH   D 4 .   ? 20.593 -11.222 9.602   1.00 17.51 ? 1109 HOH   A O   1 
HETATM 3431 O  O   . HOH   D 4 .   ? 24.150 -4.433  -2.167  1.00 18.04 ? 1110 HOH   A O   1 
HETATM 3432 O  O   . HOH   D 4 .   ? 26.364 3.725   18.542  1.00 37.27 ? 1111 HOH   A O   1 
HETATM 3433 O  O   . HOH   D 4 .   ? 28.444 26.445  -19.683 1.00 38.54 ? 1112 HOH   A O   1 
HETATM 3434 O  O   . HOH   D 4 .   ? 36.450 -5.722  -0.244  1.00 41.48 ? 1113 HOH   A O   1 
HETATM 3435 O  O   . HOH   D 4 .   ? 48.296 -6.022  -15.139 1.00 38.91 ? 1114 HOH   A O   1 
HETATM 3436 O  O   . HOH   D 4 .   ? 25.989 -18.975 -5.051  1.00 39.34 ? 1115 HOH   A O   1 
HETATM 3437 O  O   . HOH   D 4 .   ? 47.332 7.073   -12.950 1.00 28.55 ? 1116 HOH   A O   1 
HETATM 3438 O  O   . HOH   D 4 .   ? 33.403 -3.300  5.021   1.00 42.99 ? 1117 HOH   A O   1 
HETATM 3439 O  O   . HOH   D 4 .   ? 40.178 -13.133 -2.947  1.00 29.40 ? 1118 HOH   A O   1 
HETATM 3440 O  O   . HOH   D 4 .   ? 23.667 -22.553 11.466  1.00 27.06 ? 1119 HOH   A O   1 
HETATM 3441 O  O   . HOH   D 4 .   ? 38.086 10.816  -27.226 1.00 40.34 ? 1120 HOH   A O   1 
HETATM 3442 O  O   . HOH   D 4 .   ? 29.298 -6.621  16.999  1.00 36.45 ? 1121 HOH   A O   1 
HETATM 3443 O  O   . HOH   D 4 .   ? 12.344 -16.459 28.562  1.00 41.55 ? 1122 HOH   A O   1 
HETATM 3444 O  O   . HOH   D 4 .   ? 28.802 20.865  -27.222 1.00 51.14 ? 1123 HOH   A O   1 
HETATM 3445 O  O   . HOH   D 4 .   ? 37.418 8.485   2.203   1.00 42.17 ? 1124 HOH   A O   1 
HETATM 3446 O  O   . HOH   D 4 .   ? 26.003 -0.224  -6.052  1.00 25.98 ? 1125 HOH   A O   1 
HETATM 3447 O  O   . HOH   D 4 .   ? 21.249 4.283   -26.931 1.00 44.52 ? 1126 HOH   A O   1 
HETATM 3448 O  O   . HOH   D 4 .   ? 36.917 -6.835  -7.186  1.00 35.97 ? 1127 HOH   A O   1 
HETATM 3449 O  O   . HOH   D 4 .   ? 20.286 -23.967 -0.653  1.00 33.85 ? 1128 HOH   A O   1 
HETATM 3450 O  O   . HOH   D 4 .   ? 37.389 -24.417 5.903   1.00 32.86 ? 1129 HOH   A O   1 
HETATM 3451 O  O   . HOH   D 4 .   ? 33.608 -23.990 0.614   1.00 26.43 ? 1130 HOH   A O   1 
HETATM 3452 O  O   . HOH   D 4 .   ? 16.907 -0.295  23.956  1.00 24.60 ? 1131 HOH   A O   1 
HETATM 3453 O  O   . HOH   D 4 .   ? 19.136 5.179   1.111   1.00 32.00 ? 1132 HOH   A O   1 
HETATM 3454 O  O   . HOH   D 4 .   ? 19.115 15.539  8.166   1.00 43.95 ? 1133 HOH   A O   1 
HETATM 3455 O  O   . HOH   D 4 .   ? 27.169 4.675   11.285  1.00 30.33 ? 1134 HOH   A O   1 
HETATM 3456 O  O   . HOH   D 4 .   ? 29.108 8.074   4.660   1.00 43.29 ? 1135 HOH   A O   1 
HETATM 3457 O  O   . HOH   D 4 .   ? 26.516 -4.189  14.510  1.00 22.95 ? 1136 HOH   A O   1 
HETATM 3458 O  O   . HOH   D 4 .   ? 44.352 13.937  -4.392  1.00 35.71 ? 1137 HOH   A O   1 
HETATM 3459 O  O   . HOH   D 4 .   ? 19.947 -12.218 -8.981  1.00 45.94 ? 1138 HOH   A O   1 
HETATM 3460 O  O   . HOH   D 4 .   ? 42.064 -27.813 8.936   1.00 44.78 ? 1139 HOH   A O   1 
HETATM 3461 O  O   . HOH   D 4 .   ? 24.623 14.653  32.387  1.00 46.72 ? 1140 HOH   A O   1 
HETATM 3462 O  O   . HOH   D 4 .   ? 46.342 4.758   -24.400 1.00 41.05 ? 1141 HOH   A O   1 
HETATM 3463 O  O   . HOH   D 4 .   ? 25.152 10.410  24.878  1.00 40.50 ? 1142 HOH   A O   1 
HETATM 3464 O  O   . HOH   D 4 .   ? 28.977 -2.878  14.697  1.00 31.40 ? 1143 HOH   A O   1 
HETATM 3465 O  O   . HOH   D 4 .   ? 24.790 4.407   14.210  1.00 22.72 ? 1144 HOH   A O   1 
HETATM 3466 O  O   . HOH   D 4 .   ? 22.287 2.297   17.153  1.00 22.86 ? 1145 HOH   A O   1 
HETATM 3467 O  O   . HOH   D 4 .   ? 20.540 -12.574 26.583  1.00 41.99 ? 1146 HOH   A O   1 
HETATM 3468 O  O   . HOH   D 4 .   ? 23.252 10.065  26.883  1.00 41.21 ? 1147 HOH   A O   1 
HETATM 3469 O  O   . HOH   D 4 .   ? 31.463 -7.540  4.276   1.00 18.71 ? 1148 HOH   A O   1 
HETATM 3470 O  O   . HOH   D 4 .   ? 35.529 20.054  -3.067  1.00 36.64 ? 1149 HOH   A O   1 
HETATM 3471 O  O   . HOH   D 4 .   ? 8.752  -2.117  10.724  1.00 27.09 ? 1150 HOH   A O   1 
HETATM 3472 O  O   . HOH   D 4 .   ? 32.674 -2.674  -15.692 1.00 37.64 ? 1151 HOH   A O   1 
HETATM 3473 O  O   . HOH   D 4 .   ? 40.011 7.499   -29.644 1.00 38.15 ? 1152 HOH   A O   1 
HETATM 3474 O  O   . HOH   D 4 .   ? 26.368 6.935   6.632   1.00 33.13 ? 1153 HOH   A O   1 
HETATM 3475 O  O   . HOH   D 4 .   ? 30.723 17.617  1.720   1.00 36.42 ? 1154 HOH   A O   1 
HETATM 3476 O  O   . HOH   D 4 .   ? 8.246  -22.678 -2.263  1.00 29.35 ? 1155 HOH   A O   1 
HETATM 3477 O  O   . HOH   D 4 .   ? 23.969 10.330  -12.708 1.00 31.99 ? 1156 HOH   A O   1 
HETATM 3478 O  O   . HOH   D 4 .   ? 19.495 -18.059 0.245   1.00 17.57 ? 1157 HOH   A O   1 
HETATM 3479 O  O   . HOH   D 4 .   ? 28.222 18.502  -26.361 1.00 35.74 ? 1158 HOH   A O   1 
HETATM 3480 O  O   . HOH   D 4 .   ? 22.427 14.645  10.329  1.00 28.69 ? 1159 HOH   A O   1 
HETATM 3481 O  O   . HOH   D 4 .   ? 41.267 -15.685 4.607   1.00 25.36 ? 1160 HOH   A O   1 
HETATM 3482 O  O   . HOH   D 4 .   ? 27.166 0.202   20.075  1.00 44.33 ? 1161 HOH   A O   1 
HETATM 3483 O  O   . HOH   D 4 .   ? 15.465 -16.674 20.733  1.00 35.71 ? 1162 HOH   A O   1 
HETATM 3484 O  O   . HOH   D 4 .   ? 48.349 -2.246  -17.583 1.00 43.25 ? 1163 HOH   A O   1 
HETATM 3485 O  O   . HOH   D 4 .   ? 12.655 -13.717 -9.212  1.00 30.52 ? 1164 HOH   A O   1 
HETATM 3486 O  O   . HOH   D 4 .   ? 23.106 4.538   5.429   1.00 24.88 ? 1165 HOH   A O   1 
HETATM 3487 O  O   . HOH   D 4 .   ? 21.283 14.266  -15.163 1.00 40.42 ? 1166 HOH   A O   1 
HETATM 3488 O  O   . HOH   D 4 .   ? 25.530 -24.837 2.852   1.00 28.86 ? 1167 HOH   A O   1 
HETATM 3489 O  O   . HOH   D 4 .   ? 22.226 -21.927 5.754   1.00 26.42 ? 1168 HOH   A O   1 
HETATM 3490 O  O   . HOH   D 4 .   ? 10.459 -7.286  -3.623  1.00 35.92 ? 1169 HOH   A O   1 
HETATM 3491 O  O   . HOH   D 4 .   ? 35.033 3.462   -3.590  1.00 19.33 ? 1170 HOH   A O   1 
HETATM 3492 O  O   . HOH   D 4 .   ? 30.483 -5.949  15.075  1.00 38.59 ? 1171 HOH   A O   1 
HETATM 3493 O  O   . HOH   D 4 .   ? 38.649 -9.763  2.407   1.00 41.71 ? 1172 HOH   A O   1 
HETATM 3494 O  O   . HOH   D 4 .   ? 43.317 1.346   0.062   1.00 34.22 ? 1173 HOH   A O   1 
HETATM 3495 O  O   . HOH   D 4 .   ? 32.102 -16.566 4.082   1.00 17.45 ? 1174 HOH   A O   1 
HETATM 3496 O  O   . HOH   D 4 .   ? 22.967 1.233   -6.731  1.00 26.47 ? 1175 HOH   A O   1 
HETATM 3497 O  O   . HOH   D 4 .   ? 6.419  -15.122 -3.889  1.00 21.61 ? 1176 HOH   A O   1 
HETATM 3498 O  O   . HOH   D 4 .   ? 29.008 3.059   8.824   1.00 40.28 ? 1177 HOH   A O   1 
HETATM 3499 O  O   . HOH   D 4 .   ? 20.424 7.039   1.558   1.00 38.90 ? 1178 HOH   A O   1 
HETATM 3500 O  O   . HOH   D 4 .   ? 10.946 2.200   19.593  1.00 37.90 ? 1179 HOH   A O   1 
HETATM 3501 O  O   . HOH   D 4 .   ? 13.323 -8.031  -8.874  1.00 35.85 ? 1180 HOH   A O   1 
HETATM 3502 O  O   . HOH   D 4 .   ? 41.862 19.403  -8.784  1.00 27.94 ? 1181 HOH   A O   1 
HETATM 3503 O  O   . HOH   D 4 .   ? 16.732 -18.312 18.716  1.00 29.96 ? 1182 HOH   A O   1 
HETATM 3504 O  O   . HOH   D 4 .   ? 50.718 8.012   -7.479  1.00 38.77 ? 1183 HOH   A O   1 
HETATM 3505 O  O   . HOH   D 4 .   ? 25.525 -0.911  -1.251  1.00 17.89 ? 1184 HOH   A O   1 
HETATM 3506 O  O   . HOH   D 4 .   ? 12.841 9.082   9.346   1.00 34.75 ? 1185 HOH   A O   1 
HETATM 3507 O  O   . HOH   D 4 .   ? 44.256 29.875  -20.438 1.00 39.10 ? 1186 HOH   A O   1 
HETATM 3508 O  O   . HOH   D 4 .   ? 8.874  -2.068  7.436   1.00 47.08 ? 1187 HOH   A O   1 
HETATM 3509 O  O   . HOH   D 4 .   ? 30.968 0.172   -4.780  1.00 18.05 ? 1188 HOH   A O   1 
HETATM 3510 O  O   . HOH   D 4 .   ? 43.999 9.527   -2.883  1.00 22.37 ? 1189 HOH   A O   1 
HETATM 3511 O  O   . HOH   D 4 .   ? 17.831 -6.747  25.590  1.00 35.20 ? 1190 HOH   A O   1 
HETATM 3512 O  O   . HOH   D 4 .   ? 9.217  -17.775 8.360   1.00 29.08 ? 1191 HOH   A O   1 
HETATM 3513 O  O   . HOH   D 4 .   ? 20.081 -9.857  25.897  1.00 32.33 ? 1192 HOH   A O   1 
HETATM 3514 O  O   . HOH   D 4 .   ? 25.004 1.832   -0.898  1.00 16.35 ? 1193 HOH   A O   1 
HETATM 3515 O  O   . HOH   D 4 .   ? 46.414 27.040  -10.706 1.00 32.35 ? 1194 HOH   A O   1 
HETATM 3516 O  O   . HOH   D 4 .   ? 15.225 -11.725 -6.575  1.00 25.89 ? 1195 HOH   A O   1 
HETATM 3517 O  O   . HOH   D 4 .   ? 49.100 2.297   -6.359  1.00 36.56 ? 1196 HOH   A O   1 
HETATM 3518 O  O   . HOH   D 4 .   ? 34.990 23.052  -19.499 1.00 30.01 ? 1197 HOH   A O   1 
HETATM 3519 O  O   . HOH   D 4 .   ? 37.721 27.349  -11.619 1.00 33.02 ? 1198 HOH   A O   1 
HETATM 3520 O  O   . HOH   D 4 .   ? 46.688 26.005  -24.806 1.00 40.82 ? 1199 HOH   A O   1 
HETATM 3521 O  O   . HOH   D 4 .   ? 41.290 -7.288  -17.759 1.00 40.06 ? 1200 HOH   A O   1 
HETATM 3522 O  O   . HOH   D 4 .   ? 32.972 -25.846 6.127   1.00 39.22 ? 1201 HOH   A O   1 
HETATM 3523 O  O   . HOH   D 4 .   ? 50.094 13.269  -23.841 1.00 33.23 ? 1202 HOH   A O   1 
HETATM 3524 O  O   . HOH   D 4 .   ? 26.020 12.882  -27.696 1.00 31.06 ? 1203 HOH   A O   1 
HETATM 3525 O  O   . HOH   D 4 .   ? 9.660  -9.120  12.116  1.00 33.10 ? 1204 HOH   A O   1 
HETATM 3526 O  O   . HOH   D 4 .   ? 32.952 -26.830 18.439  1.00 39.43 ? 1205 HOH   A O   1 
HETATM 3527 O  O   . HOH   D 4 .   ? 35.168 -18.083 28.333  1.00 41.00 ? 1206 HOH   A O   1 
HETATM 3528 O  O   . HOH   D 4 .   ? 27.592 6.395   3.583   1.00 35.76 ? 1207 HOH   A O   1 
HETATM 3529 O  O   . HOH   D 4 .   ? 45.329 28.684  -23.456 1.00 41.19 ? 1208 HOH   A O   1 
HETATM 3530 O  O   . HOH   D 4 .   ? 48.744 3.806   -1.502  1.00 45.19 ? 1209 HOH   A O   1 
HETATM 3531 O  O   . HOH   D 4 .   ? 18.321 10.207  28.388  1.00 41.68 ? 1210 HOH   A O   1 
HETATM 3532 O  O   . HOH   D 4 .   ? 32.473 -21.446 30.511  1.00 36.34 ? 1211 HOH   A O   1 
HETATM 3533 O  O   . HOH   D 4 .   ? 22.753 -11.662 11.229  1.00 18.07 ? 1212 HOH   A O   1 
HETATM 3534 O  O   . HOH   D 4 .   ? 47.753 27.298  -17.315 1.00 19.27 ? 1213 HOH   A O   1 
HETATM 3535 O  O   . HOH   D 4 .   ? 7.161  -15.106 -0.671  1.00 18.56 ? 1214 HOH   A O   1 
HETATM 3536 O  O   . HOH   D 4 .   ? 15.204 4.090   23.929  1.00 29.40 ? 1215 HOH   A O   1 
HETATM 3537 O  O   . HOH   D 4 .   ? 42.963 24.800  -10.159 1.00 31.38 ? 1216 HOH   A O   1 
HETATM 3538 O  O   . HOH   D 4 .   ? 34.186 -15.643 28.644  1.00 43.87 ? 1217 HOH   A O   1 
HETATM 3539 O  O   . HOH   D 4 .   ? 24.870 -7.740  17.592  1.00 22.43 ? 1218 HOH   A O   1 
HETATM 3540 O  O   . HOH   D 4 .   ? 31.811 -26.869 11.118  1.00 38.14 ? 1219 HOH   A O   1 
HETATM 3541 O  O   . HOH   D 4 .   ? 34.560 -13.407 5.518   1.00 15.33 ? 1220 HOH   A O   1 
HETATM 3542 O  O   . HOH   D 4 .   ? 30.638 2.247   -28.540 1.00 47.90 ? 1221 HOH   A O   1 
HETATM 3543 O  O   . HOH   D 4 .   ? 43.559 -10.939 -3.858  1.00 40.24 ? 1222 HOH   A O   1 
HETATM 3544 O  O   . HOH   D 4 .   ? 36.260 -22.581 23.239  1.00 36.23 ? 1223 HOH   A O   1 
HETATM 3545 O  O   . HOH   D 4 .   ? 20.302 2.212   10.364  1.00 16.99 ? 1224 HOH   A O   1 
HETATM 3546 O  O   . HOH   D 4 .   ? 23.027 -8.719  23.064  1.00 21.64 ? 1225 HOH   A O   1 
HETATM 3547 O  O   . HOH   D 4 .   ? 14.746 0.286   3.114   1.00 19.45 ? 1226 HOH   A O   1 
HETATM 3548 O  O   . HOH   D 4 .   ? 42.233 25.775  -19.428 1.00 30.67 ? 1227 HOH   A O   1 
HETATM 3549 O  O   . HOH   D 4 .   ? 7.838  -7.841  1.044   1.00 34.95 ? 1228 HOH   A O   1 
HETATM 3550 O  O   . HOH   D 4 .   ? 22.472 4.684   15.817  1.00 21.82 ? 1229 HOH   A O   1 
HETATM 3551 O  O   . HOH   D 4 .   ? 12.732 -10.307 23.229  1.00 27.01 ? 1230 HOH   A O   1 
HETATM 3552 O  O   . HOH   D 4 .   ? 26.548 -14.382 -3.546  1.00 41.17 ? 1231 HOH   A O   1 
HETATM 3553 O  O   . HOH   D 4 .   ? 30.027 -3.651  17.193  1.00 46.49 ? 1232 HOH   A O   1 
HETATM 3554 O  O   . HOH   D 4 .   ? 47.375 -3.272  -5.226  1.00 43.89 ? 1233 HOH   A O   1 
HETATM 3555 O  O   . HOH   D 4 .   ? 35.345 -23.275 11.649  1.00 24.67 ? 1234 HOH   A O   1 
HETATM 3556 O  O   . HOH   D 4 .   ? 25.174 -11.176 -5.302  1.00 23.56 ? 1235 HOH   A O   1 
HETATM 3557 O  O   . HOH   D 4 .   ? 10.928 -14.937 11.906  1.00 35.94 ? 1236 HOH   A O   1 
HETATM 3558 O  O   . HOH   D 4 .   ? 37.167 20.632  -8.012  1.00 28.15 ? 1237 HOH   A O   1 
HETATM 3559 O  O   . HOH   D 4 .   ? 25.038 21.276  17.141  1.00 33.72 ? 1238 HOH   A O   1 
HETATM 3560 O  O   . HOH   D 4 .   ? 12.438 -11.958 -7.151  1.00 34.15 ? 1239 HOH   A O   1 
HETATM 3561 O  O   . HOH   D 4 .   ? 25.448 -1.705  -8.814  1.00 38.22 ? 1240 HOH   A O   1 
HETATM 3562 O  O   . HOH   D 4 .   ? 42.596 18.547  -5.921  1.00 41.41 ? 1241 HOH   A O   1 
HETATM 3563 O  O   . HOH   D 4 .   ? 34.312 26.138  -14.358 1.00 33.31 ? 1242 HOH   A O   1 
HETATM 3564 O  O   . HOH   D 4 .   ? 25.703 -22.375 13.104  1.00 41.07 ? 1243 HOH   A O   1 
HETATM 3565 O  O   . HOH   D 4 .   ? 52.801 16.295  -12.056 1.00 22.28 ? 1244 HOH   A O   1 
HETATM 3566 O  O   . HOH   D 4 .   ? 22.156 -4.055  20.697  1.00 18.81 ? 1245 HOH   A O   1 
HETATM 3567 O  O   . HOH   D 4 .   ? 27.058 23.047  -12.395 1.00 33.17 ? 1246 HOH   A O   1 
HETATM 3568 O  O   . HOH   D 4 .   ? 10.615 -11.723 14.062  1.00 33.87 ? 1247 HOH   A O   1 
HETATM 3569 O  O   . HOH   D 4 .   ? 11.312 -9.366  14.961  1.00 30.39 ? 1248 HOH   A O   1 
HETATM 3570 O  O   . HOH   D 4 .   ? 22.345 -19.593 28.908  1.00 28.07 ? 1249 HOH   A O   1 
HETATM 3571 O  O   . HOH   D 4 .   ? 23.117 22.655  5.319   1.00 42.06 ? 1250 HOH   A O   1 
HETATM 3572 O  O   . HOH   D 4 .   ? 54.046 13.259  -9.672  1.00 32.24 ? 1251 HOH   A O   1 
HETATM 3573 O  O   . HOH   D 4 .   ? 27.901 16.201  8.999   1.00 36.85 ? 1252 HOH   A O   1 
HETATM 3574 O  O   . HOH   D 4 .   ? 49.259 -16.617 14.855  1.00 46.58 ? 1253 HOH   A O   1 
HETATM 3575 O  O   . HOH   D 4 .   ? 29.865 16.024  -27.597 1.00 33.63 ? 1254 HOH   A O   1 
HETATM 3576 O  O   . HOH   D 4 .   ? 29.157 -16.737 30.591  1.00 46.52 ? 1255 HOH   A O   1 
HETATM 3577 O  O   . HOH   D 4 .   ? 24.839 -24.819 -0.813  1.00 27.69 ? 1256 HOH   A O   1 
HETATM 3578 O  O   . HOH   D 4 .   ? 25.981 23.677  -7.013  1.00 40.87 ? 1257 HOH   A O   1 
HETATM 3579 O  O   . HOH   D 4 .   ? 13.615 0.055   21.354  1.00 34.27 ? 1258 HOH   A O   1 
HETATM 3580 O  O   . HOH   D 4 .   ? 15.725 -20.441 10.600  1.00 34.89 ? 1259 HOH   A O   1 
HETATM 3581 O  O   . HOH   D 4 .   ? 37.445 -8.862  -2.075  1.00 33.48 ? 1260 HOH   A O   1 
HETATM 3582 O  O   . HOH   D 4 .   ? 19.910 -19.774 -2.113  1.00 38.12 ? 1261 HOH   A O   1 
HETATM 3583 O  O   . HOH   D 4 .   ? 24.087 6.723   -10.914 1.00 31.14 ? 1262 HOH   A O   1 
HETATM 3584 O  O   . HOH   D 4 .   ? 21.473 6.624   -8.821  1.00 41.99 ? 1263 HOH   A O   1 
HETATM 3585 O  O   . HOH   D 4 .   ? 19.560 -9.843  -13.914 1.00 45.30 ? 1264 HOH   A O   1 
HETATM 3586 O  O   . HOH   D 4 .   ? 45.205 11.891  -11.372 1.00 20.95 ? 1265 HOH   A O   1 
HETATM 3587 O  O   . HOH   D 4 .   ? 18.437 13.021  9.109   1.00 38.99 ? 1266 HOH   A O   1 
HETATM 3588 O  O   . HOH   D 4 .   ? 22.832 -7.861  -7.963  1.00 42.69 ? 1267 HOH   A O   1 
HETATM 3589 O  O   . HOH   D 4 .   ? 49.682 -13.965 15.306  1.00 67.15 ? 1268 HOH   A O   1 
HETATM 3590 O  O   . HOH   D 4 .   ? 42.506 -11.220 6.704   1.00 40.93 ? 1269 HOH   A O   1 
HETATM 3591 O  O   . HOH   D 4 .   ? 5.922  -4.215  8.410   1.00 29.35 ? 1270 HOH   A O   1 
HETATM 3592 O  O   . HOH   D 4 .   ? 9.906  -2.477  17.593  1.00 40.17 ? 1271 HOH   A O   1 
HETATM 3593 O  O   . HOH   D 4 .   ? 8.244  -14.212 9.607   1.00 38.47 ? 1272 HOH   A O   1 
HETATM 3594 O  O   . HOH   D 4 .   ? 38.968 1.418   1.620   1.00 30.87 ? 1273 HOH   A O   1 
HETATM 3595 O  O   . HOH   D 4 .   ? 14.325 -0.116  7.800   1.00 35.34 ? 1274 HOH   A O   1 
HETATM 3596 O  O   . HOH   D 4 .   ? 18.719 -21.173 8.850   1.00 37.66 ? 1275 HOH   A O   1 
HETATM 3597 O  O   . HOH   D 4 .   ? 9.956  -20.717 -3.136  1.00 27.05 ? 1276 HOH   A O   1 
HETATM 3598 O  O   . HOH   D 4 .   ? 39.634 -28.063 7.894   1.00 51.50 ? 1277 HOH   A O   1 
HETATM 3599 O  O   . HOH   D 4 .   ? 28.617 17.717  3.723   1.00 38.04 ? 1278 HOH   A O   1 
HETATM 3600 O  O   . HOH   D 4 .   ? 27.355 -2.965  18.142  1.00 32.23 ? 1279 HOH   A O   1 
HETATM 3601 O  O   . HOH   D 4 .   ? 2.547  -17.412 8.038   1.00 43.05 ? 1280 HOH   A O   1 
HETATM 3602 O  O   . HOH   D 4 .   ? 29.090 15.737  19.918  1.00 36.65 ? 1281 HOH   A O   1 
HETATM 3603 O  O   . HOH   D 4 .   ? 30.836 -25.482 4.317   1.00 25.45 ? 1282 HOH   A O   1 
HETATM 3604 O  O   . HOH   D 4 .   ? 8.021  -11.143 0.556   1.00 25.88 ? 1283 HOH   A O   1 
HETATM 3605 O  O   . HOH   D 4 .   ? 12.994 -5.948  25.225  1.00 27.47 ? 1284 HOH   A O   1 
HETATM 3606 O  O   . HOH   D 4 .   ? 10.836 -14.452 22.800  1.00 36.63 ? 1285 HOH   A O   1 
HETATM 3607 O  O   . HOH   D 4 .   ? 21.065 19.084  5.497   1.00 42.69 ? 1286 HOH   A O   1 
HETATM 3608 O  O   . HOH   D 4 .   ? -5.289 -24.041 8.673   1.00 44.85 ? 1287 HOH   A O   1 
HETATM 3609 O  O   . HOH   D 4 .   ? 43.088 -1.160  -26.706 1.00 44.13 ? 1288 HOH   A O   1 
HETATM 3610 O  O   . HOH   D 4 .   ? 28.228 1.952   11.102  1.00 32.51 ? 1289 HOH   A O   1 
HETATM 3611 O  O   . HOH   D 4 .   ? 13.981 1.908   22.918  1.00 48.20 ? 1290 HOH   A O   1 
HETATM 3612 O  O   . HOH   D 4 .   ? 16.396 4.524   2.982   1.00 34.53 ? 1291 HOH   A O   1 
HETATM 3613 O  O   . HOH   D 4 .   ? 10.370 -13.772 16.998  1.00 38.30 ? 1292 HOH   A O   1 
HETATM 3614 O  O   . HOH   D 4 .   ? 45.749 11.425  -4.230  1.00 35.82 ? 1293 HOH   A O   1 
HETATM 3615 O  O   . HOH   D 4 .   ? 39.440 -16.552 22.615  1.00 36.55 ? 1294 HOH   A O   1 
HETATM 3616 O  O   . HOH   D 4 .   ? 35.871 -3.709  -1.156  1.00 30.45 ? 1295 HOH   A O   1 
HETATM 3617 O  O   . HOH   D 4 .   ? 47.924 18.129  -25.105 1.00 39.39 ? 1296 HOH   A O   1 
HETATM 3618 O  O   . HOH   D 4 .   ? 31.328 -4.054  27.765  1.00 44.08 ? 1297 HOH   A O   1 
HETATM 3619 O  O   . HOH   D 4 .   ? 38.842 -21.711 5.070   1.00 35.50 ? 1298 HOH   A O   1 
HETATM 3620 O  O   . HOH   D 4 .   ? 7.455  -7.225  23.669  1.00 53.46 ? 1299 HOH   A O   1 
HETATM 3621 O  O   . HOH   D 4 .   ? 24.816 18.824  6.929   1.00 45.40 ? 1300 HOH   A O   1 
HETATM 3622 O  O   . HOH   D 4 .   ? 22.539 12.220  -15.648 1.00 43.87 ? 1301 HOH   A O   1 
HETATM 3623 O  O   . HOH   D 4 .   ? 21.042 -12.944 29.232  1.00 47.99 ? 1302 HOH   A O   1 
HETATM 3624 O  O   . HOH   D 4 .   ? 20.117 -0.959  27.108  1.00 45.47 ? 1303 HOH   A O   1 
HETATM 3625 O  O   . HOH   D 4 .   ? 29.256 6.121   16.727  1.00 45.08 ? 1304 HOH   A O   1 
HETATM 3626 O  O   . HOH   D 4 .   ? 21.807 -16.796 29.976  1.00 38.76 ? 1305 HOH   A O   1 
HETATM 3627 O  O   . HOH   D 4 .   ? 25.691 2.415   -7.150  1.00 42.45 ? 1306 HOH   A O   1 
HETATM 3628 O  O   . HOH   D 4 .   ? 24.186 2.592   19.098  1.00 37.24 ? 1307 HOH   A O   1 
HETATM 3629 O  O   . HOH   D 4 .   ? 40.503 29.746  -18.549 1.00 48.11 ? 1308 HOH   A O   1 
HETATM 3630 O  O   . HOH   D 4 .   ? 6.251  -12.370 -0.826  1.00 28.66 ? 1309 HOH   A O   1 
HETATM 3631 O  O   . HOH   D 4 .   ? 4.958  -4.910  10.863  1.00 47.03 ? 1310 HOH   A O   1 
HETATM 3632 O  O   . HOH   D 4 .   ? 15.347 2.806   26.447  1.00 46.85 ? 1311 HOH   A O   1 
HETATM 3633 O  O   . HOH   D 4 .   ? 22.165 -5.766  23.394  1.00 19.29 ? 1312 HOH   A O   1 
HETATM 3634 O  O   . HOH   D 4 .   ? 18.829 -24.174 27.335  1.00 44.49 ? 1313 HOH   A O   1 
HETATM 3635 O  O   . HOH   D 4 .   ? 16.192 -22.311 8.755   1.00 45.58 ? 1314 HOH   A O   1 
HETATM 3636 O  O   . HOH   D 4 .   ? 43.656 -14.823 -9.109  1.00 46.68 ? 1315 HOH   A O   1 
HETATM 3637 O  O   . HOH   D 4 .   ? 19.288 9.262   3.115   1.00 35.31 ? 1316 HOH   A O   1 
HETATM 3638 O  O   . HOH   D 4 .   ? 50.494 16.588  -24.740 1.00 44.29 ? 1317 HOH   A O   1 
HETATM 3639 O  O   . HOH   D 4 .   ? 11.069 -17.751 26.560  1.00 45.20 ? 1318 HOH   A O   1 
HETATM 3640 O  O   . HOH   D 4 .   ? 14.796 2.741   1.845   1.00 31.74 ? 1319 HOH   A O   1 
HETATM 3641 O  O   . HOH   D 4 .   ? 9.276  -10.646 -4.298  1.00 38.45 ? 1320 HOH   A O   1 
HETATM 3642 O  O   . HOH   D 4 .   ? 13.245 4.880   9.799   1.00 26.87 ? 1321 HOH   A O   1 
HETATM 3643 O  O   . HOH   D 4 .   ? 43.084 9.723   -30.226 1.00 47.92 ? 1322 HOH   A O   1 
HETATM 3644 O  O   . HOH   D 4 .   ? 45.340 -13.593 7.119   1.00 48.02 ? 1323 HOH   A O   1 
HETATM 3645 O  O   . HOH   D 4 .   ? 29.861 24.930  -4.156  1.00 42.94 ? 1324 HOH   A O   1 
HETATM 3646 O  O   . HOH   D 4 .   ? 23.338 22.985  -21.027 1.00 43.39 ? 1325 HOH   A O   1 
HETATM 3647 O  O   . HOH   D 4 .   ? 26.122 23.942  -14.827 1.00 44.28 ? 1326 HOH   A O   1 
HETATM 3648 O  O   . HOH   D 4 .   ? 33.943 10.706  5.962   1.00 44.97 ? 1327 HOH   A O   1 
HETATM 3649 O  O   . HOH   D 4 .   ? 26.563 -5.599  17.211  1.00 28.35 ? 1328 HOH   A O   1 
HETATM 3650 O  O   . HOH   D 4 .   ? 28.958 26.516  -24.002 1.00 53.40 ? 1329 HOH   A O   1 
HETATM 3651 O  O   . HOH   D 4 .   ? 36.956 -26.607 23.213  1.00 47.64 ? 1330 HOH   A O   1 
HETATM 3652 O  O   . HOH   D 4 .   ? 25.070 -9.558  -7.973  1.00 38.59 ? 1331 HOH   A O   1 
HETATM 3653 O  O   . HOH   D 4 .   ? 39.892 21.420  -8.351  1.00 36.05 ? 1332 HOH   A O   1 
HETATM 3654 O  O   . HOH   D 4 .   ? 34.175 -25.797 11.844  1.00 35.98 ? 1333 HOH   A O   1 
HETATM 3655 O  O   . HOH   D 4 .   ? 11.748 -1.154  6.953   1.00 36.12 ? 1334 HOH   A O   1 
HETATM 3656 O  O   . HOH   D 4 .   ? 30.292 17.349  9.481   1.00 43.24 ? 1335 HOH   A O   1 
HETATM 3657 O  O   . HOH   D 4 .   ? 15.172 22.084  -8.281  1.00 41.47 ? 1336 HOH   A O   1 
HETATM 3658 O  O   . HOH   D 4 .   ? 33.342 21.095  -1.903  1.00 46.99 ? 1337 HOH   A O   1 
HETATM 3659 O  O   . HOH   D 4 .   ? 24.603 11.357  -29.497 1.00 43.72 ? 1338 HOH   A O   1 
HETATM 3660 O  O   . HOH   D 4 .   ? 16.159 0.589   26.383  1.00 38.09 ? 1339 HOH   A O   1 
HETATM 3661 O  O   . HOH   D 4 .   ? 3.966  -11.130 -1.718  1.00 36.64 ? 1340 HOH   A O   1 
HETATM 3662 O  O   . HOH   D 4 .   ? 29.605 12.981  23.286  1.00 48.56 ? 1341 HOH   A O   1 
HETATM 3663 O  O   . HOH   D 4 .   ? 10.420 -9.404  -2.038  1.00 28.76 ? 1342 HOH   A O   1 
HETATM 3664 O  O   . HOH   D 4 .   ? 44.347 10.525  -0.248  1.00 41.81 ? 1343 HOH   A O   1 
HETATM 3665 O  O   . HOH   D 4 .   ? 38.033 10.178  -29.975 1.00 47.27 ? 1344 HOH   A O   1 
HETATM 3666 O  O   . HOH   D 4 .   ? 37.053 20.677  -5.309  1.00 45.77 ? 1345 HOH   A O   1 
HETATM 3667 O  O   . HOH   D 4 .   ? 9.300  -8.608  16.404  1.00 31.72 ? 1346 HOH   A O   1 
HETATM 3668 O  O   . HOH   D 4 .   ? 18.084 10.705  -25.428 1.00 51.39 ? 1347 HOH   A O   1 
HETATM 3669 O  O   . HOH   D 4 .   ? 1.097  -10.153 2.124   1.00 35.61 ? 1348 HOH   A O   1 
HETATM 3670 O  O   . HOH   D 4 .   ? 32.479 -26.107 2.056   1.00 34.34 ? 1349 HOH   A O   1 
HETATM 3671 O  O   . HOH   D 4 .   ? 22.153 18.861  8.096   1.00 26.56 ? 1350 HOH   A O   1 
HETATM 3672 O  O   . HOH   D 4 .   ? 28.836 13.423  -28.168 1.00 39.26 ? 1351 HOH   A O   1 
HETATM 3673 O  O   . HOH   D 4 .   ? 8.542  -0.625  13.517  1.00 45.99 ? 1352 HOH   A O   1 
HETATM 3674 O  O   . HOH   D 4 .   ? 25.217 25.019  -4.724  1.00 39.89 ? 1353 HOH   A O   1 
HETATM 3675 O  O   . HOH   D 4 .   ? 43.365 -24.798 6.740   1.00 42.69 ? 1354 HOH   A O   1 
HETATM 3676 O  O   . HOH   D 4 .   ? 17.555 20.211  2.209   1.00 46.65 ? 1355 HOH   A O   1 
HETATM 3677 O  O   . HOH   D 4 .   ? 21.079 16.877  9.651   1.00 25.44 ? 1356 HOH   A O   1 
HETATM 3678 O  O   . HOH   D 4 .   ? 28.198 10.774  24.358  1.00 41.88 ? 1357 HOH   A O   1 
HETATM 3679 O  O   . HOH   D 4 .   ? 27.236 24.170  -23.848 1.00 51.50 ? 1358 HOH   A O   1 
HETATM 3680 O  O   . HOH   D 4 .   ? 21.144 -8.010  27.480  1.00 49.76 ? 1359 HOH   A O   1 
HETATM 3681 O  O   . HOH   D 4 .   ? 47.344 0.749   -1.358  1.00 50.92 ? 1360 HOH   A O   1 
HETATM 3682 O  O   . HOH   D 4 .   ? 29.783 7.131   12.145  1.00 45.87 ? 1361 HOH   A O   1 
HETATM 3683 O  O   . HOH   D 4 .   ? 22.176 -25.831 -0.709  1.00 46.02 ? 1362 HOH   A O   1 
HETATM 3684 O  O   . HOH   D 4 .   ? 22.009 -25.625 4.063   1.00 44.24 ? 1363 HOH   A O   1 
HETATM 3685 O  O   . HOH   D 4 .   ? 32.479 24.006  -2.860  1.00 52.53 ? 1364 HOH   A O   1 
HETATM 3686 O  O   . HOH   D 4 .   ? 29.569 12.018  20.190  1.00 46.51 ? 1365 HOH   A O   1 
# 
