data_9B81
# 
_entry.id   9B81 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9B81         pdb_00009b81 10.2210/pdb9b81/pdb 
WWPDB D_1000282827 ?            ?                   
# 
_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       2025-03-26 
_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                        9B81 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-28 
_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              daniel_klein@merck.com 
_pdbx_contact_author.name_first         Daniel 
_pdbx_contact_author.name_last          Klein 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3533-3273 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lu, J.'            1 ? 
'Abeywickrema, P.'  2 ? 
'Heo, M.R.'         3 ? 
'Parthasarathy, G.' 4 ? 
'McCoy, M.'         5 ? 
'Soisson, S.M.'     6 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                7877 
_citation.page_last                 7877 
_citation.title                     'Biostructural, biochemical and biophysical studies of mutant IDH1.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-51692-0 
_citation.pdbx_database_id_PubMed   39251618 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'McCoy, M.A.'        1 0000-0003-3994-6605 
primary 'Lu, J.'             2 ?                   
primary 'Richard Miller, F.' 3 ?                   
primary 'Soisson, S.M.'      4 ?                   
primary 'Lam, M.H.'          5 ?                   
primary 'Fischer, C.'        6 ?                   
# 
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 'Isocitrate dehydrogenase [NADP] cytoplasmic' 48048.605 2  1.1.1.42 ? ? ? 
2 non-polymer syn 
;2-methyl-2-(6-{4-[(2S)-1,1,1-trifluoro-2-hydroxypropan-2-yl]benzoyl}-6,11-dihydro-5H-pyrido[2,3-b][1,5]benzodiazepin-8-yl)propanenitrile
;
480.482   2  ?        ? ? ? 
3 non-polymer syn 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 743.405   2  ?        ? ? ? 
4 non-polymer syn GLYCEROL 92.094    1  ?        ? ? ? 
5 water       nat water 18.015    47 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'IDH,IDH1,Cytosolic NADP-isocitrate dehydrogenase,IDPc,NADP(+)-specific ICDH,Oxalosuccinate decarboxylase' 
# 
_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       
;MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDE
KRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGHHAYGDQYRATDFVVPGPGKVEITYTPSD
GTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFE
AQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQ
KGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDK
LGENLKIKLAQAKLLEHHHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDE
KRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGHHAYGDQYRATDFVVPGPGKVEITYTPSD
GTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFE
AQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQ
KGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDK
LGENLKIKLAQAKLLEHHHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;2-methyl-2-(6-{4-[(2S)-1,1,1-trifluoro-2-hydroxypropan-2-yl]benzoyl}-6,11-dihydro-5H-pyrido[2,3-b][1,5]benzodiazepin-8-yl)propanenitrile
;
A1AI4 
3 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' NAP   
4 GLYCEROL GOL   
5 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LYS n 
1 4   LYS n 
1 5   ILE n 
1 6   SER n 
1 7   GLY n 
1 8   GLY n 
1 9   SER n 
1 10  VAL n 
1 11  VAL n 
1 12  GLU n 
1 13  MET n 
1 14  GLN n 
1 15  GLY n 
1 16  ASP n 
1 17  GLU n 
1 18  MET n 
1 19  THR n 
1 20  ARG n 
1 21  ILE n 
1 22  ILE n 
1 23  TRP n 
1 24  GLU n 
1 25  LEU n 
1 26  ILE n 
1 27  LYS n 
1 28  GLU n 
1 29  LYS n 
1 30  LEU n 
1 31  ILE n 
1 32  PHE n 
1 33  PRO n 
1 34  TYR n 
1 35  VAL n 
1 36  GLU n 
1 37  LEU n 
1 38  ASP n 
1 39  LEU n 
1 40  HIS n 
1 41  SER n 
1 42  TYR n 
1 43  ASP n 
1 44  LEU n 
1 45  GLY n 
1 46  ILE n 
1 47  GLU n 
1 48  ASN n 
1 49  ARG n 
1 50  ASP n 
1 51  ALA n 
1 52  THR n 
1 53  ASN n 
1 54  ASP n 
1 55  GLN n 
1 56  VAL n 
1 57  THR n 
1 58  LYS n 
1 59  ASP n 
1 60  ALA n 
1 61  ALA n 
1 62  GLU n 
1 63  ALA n 
1 64  ILE n 
1 65  LYS n 
1 66  LYS n 
1 67  HIS n 
1 68  ASN n 
1 69  VAL n 
1 70  GLY n 
1 71  VAL n 
1 72  LYS n 
1 73  CYS n 
1 74  ALA n 
1 75  THR n 
1 76  ILE n 
1 77  THR n 
1 78  PRO n 
1 79  ASP n 
1 80  GLU n 
1 81  LYS n 
1 82  ARG n 
1 83  VAL n 
1 84  GLU n 
1 85  GLU n 
1 86  PHE n 
1 87  LYS n 
1 88  LEU n 
1 89  LYS n 
1 90  GLN n 
1 91  MET n 
1 92  TRP n 
1 93  LYS n 
1 94  SER n 
1 95  PRO n 
1 96  ASN n 
1 97  GLY n 
1 98  THR n 
1 99  ILE n 
1 100 ARG n 
1 101 ASN n 
1 102 ILE n 
1 103 LEU n 
1 104 GLY n 
1 105 GLY n 
1 106 THR n 
1 107 VAL n 
1 108 PHE n 
1 109 ARG n 
1 110 GLU n 
1 111 ALA n 
1 112 ILE n 
1 113 ILE n 
1 114 CYS n 
1 115 LYS n 
1 116 ASN n 
1 117 ILE n 
1 118 PRO n 
1 119 ARG n 
1 120 LEU n 
1 121 VAL n 
1 122 SER n 
1 123 GLY n 
1 124 TRP n 
1 125 VAL n 
1 126 LYS n 
1 127 PRO n 
1 128 ILE n 
1 129 ILE n 
1 130 ILE n 
1 131 GLY n 
1 132 HIS n 
1 133 HIS n 
1 134 ALA n 
1 135 TYR n 
1 136 GLY n 
1 137 ASP n 
1 138 GLN n 
1 139 TYR n 
1 140 ARG n 
1 141 ALA n 
1 142 THR n 
1 143 ASP n 
1 144 PHE n 
1 145 VAL n 
1 146 VAL n 
1 147 PRO n 
1 148 GLY n 
1 149 PRO n 
1 150 GLY n 
1 151 LYS n 
1 152 VAL n 
1 153 GLU n 
1 154 ILE n 
1 155 THR n 
1 156 TYR n 
1 157 THR n 
1 158 PRO n 
1 159 SER n 
1 160 ASP n 
1 161 GLY n 
1 162 THR n 
1 163 GLN n 
1 164 LYS n 
1 165 VAL n 
1 166 THR n 
1 167 TYR n 
1 168 LEU n 
1 169 VAL n 
1 170 HIS n 
1 171 ASN n 
1 172 PHE n 
1 173 GLU n 
1 174 GLU n 
1 175 GLY n 
1 176 GLY n 
1 177 GLY n 
1 178 VAL n 
1 179 ALA n 
1 180 MET n 
1 181 GLY n 
1 182 MET n 
1 183 TYR n 
1 184 ASN n 
1 185 GLN n 
1 186 ASP n 
1 187 LYS n 
1 188 SER n 
1 189 ILE n 
1 190 GLU n 
1 191 ASP n 
1 192 PHE n 
1 193 ALA n 
1 194 HIS n 
1 195 SER n 
1 196 SER n 
1 197 PHE n 
1 198 GLN n 
1 199 MET n 
1 200 ALA n 
1 201 LEU n 
1 202 SER n 
1 203 LYS n 
1 204 GLY n 
1 205 TRP n 
1 206 PRO n 
1 207 LEU n 
1 208 TYR n 
1 209 LEU n 
1 210 SER n 
1 211 THR n 
1 212 LYS n 
1 213 ASN n 
1 214 THR n 
1 215 ILE n 
1 216 LEU n 
1 217 LYS n 
1 218 LYS n 
1 219 TYR n 
1 220 ASP n 
1 221 GLY n 
1 222 ARG n 
1 223 PHE n 
1 224 LYS n 
1 225 ASP n 
1 226 ILE n 
1 227 PHE n 
1 228 GLN n 
1 229 GLU n 
1 230 ILE n 
1 231 TYR n 
1 232 ASP n 
1 233 LYS n 
1 234 GLN n 
1 235 TYR n 
1 236 LYS n 
1 237 SER n 
1 238 GLN n 
1 239 PHE n 
1 240 GLU n 
1 241 ALA n 
1 242 GLN n 
1 243 LYS n 
1 244 ILE n 
1 245 TRP n 
1 246 TYR n 
1 247 GLU n 
1 248 HIS n 
1 249 ARG n 
1 250 LEU n 
1 251 ILE n 
1 252 ASP n 
1 253 ASP n 
1 254 MET n 
1 255 VAL n 
1 256 ALA n 
1 257 GLN n 
1 258 ALA n 
1 259 MET n 
1 260 LYS n 
1 261 SER n 
1 262 GLU n 
1 263 GLY n 
1 264 GLY n 
1 265 PHE n 
1 266 ILE n 
1 267 TRP n 
1 268 ALA n 
1 269 CYS n 
1 270 LYS n 
1 271 ASN n 
1 272 TYR n 
1 273 ASP n 
1 274 GLY n 
1 275 ASP n 
1 276 VAL n 
1 277 GLN n 
1 278 SER n 
1 279 ASP n 
1 280 SER n 
1 281 VAL n 
1 282 ALA n 
1 283 GLN n 
1 284 GLY n 
1 285 TYR n 
1 286 GLY n 
1 287 SER n 
1 288 LEU n 
1 289 GLY n 
1 290 MET n 
1 291 MET n 
1 292 THR n 
1 293 SER n 
1 294 VAL n 
1 295 LEU n 
1 296 VAL n 
1 297 CYS n 
1 298 PRO n 
1 299 ASP n 
1 300 GLY n 
1 301 LYS n 
1 302 THR n 
1 303 VAL n 
1 304 GLU n 
1 305 ALA n 
1 306 GLU n 
1 307 ALA n 
1 308 ALA n 
1 309 HIS n 
1 310 GLY n 
1 311 THR n 
1 312 VAL n 
1 313 THR n 
1 314 ARG n 
1 315 HIS n 
1 316 TYR n 
1 317 ARG n 
1 318 MET n 
1 319 TYR n 
1 320 GLN n 
1 321 LYS n 
1 322 GLY n 
1 323 GLN n 
1 324 GLU n 
1 325 THR n 
1 326 SER n 
1 327 THR n 
1 328 ASN n 
1 329 PRO n 
1 330 ILE n 
1 331 ALA n 
1 332 SER n 
1 333 ILE n 
1 334 PHE n 
1 335 ALA n 
1 336 TRP n 
1 337 THR n 
1 338 ARG n 
1 339 GLY n 
1 340 LEU n 
1 341 ALA n 
1 342 HIS n 
1 343 ARG n 
1 344 ALA n 
1 345 LYS n 
1 346 LEU n 
1 347 ASP n 
1 348 ASN n 
1 349 ASN n 
1 350 LYS n 
1 351 GLU n 
1 352 LEU n 
1 353 ALA n 
1 354 PHE n 
1 355 PHE n 
1 356 ALA n 
1 357 ASN n 
1 358 ALA n 
1 359 LEU n 
1 360 GLU n 
1 361 GLU n 
1 362 VAL n 
1 363 SER n 
1 364 ILE n 
1 365 GLU n 
1 366 THR n 
1 367 ILE n 
1 368 GLU n 
1 369 ALA n 
1 370 GLY n 
1 371 PHE n 
1 372 MET n 
1 373 THR n 
1 374 LYS n 
1 375 ASP n 
1 376 LEU n 
1 377 ALA n 
1 378 ALA n 
1 379 CYS n 
1 380 ILE n 
1 381 LYS n 
1 382 GLY n 
1 383 LEU n 
1 384 PRO n 
1 385 ASN n 
1 386 VAL n 
1 387 GLN n 
1 388 ARG n 
1 389 SER n 
1 390 ASP n 
1 391 TYR n 
1 392 LEU n 
1 393 ASN n 
1 394 THR n 
1 395 PHE n 
1 396 GLU n 
1 397 PHE n 
1 398 MET n 
1 399 ASP n 
1 400 LYS n 
1 401 LEU n 
1 402 GLY n 
1 403 GLU n 
1 404 ASN n 
1 405 LEU n 
1 406 LYS n 
1 407 ILE n 
1 408 LYS n 
1 409 LEU n 
1 410 ALA n 
1 411 GLN n 
1 412 ALA n 
1 413 LYS n 
1 414 LEU n 
1 415 LEU n 
1 416 GLU n 
1 417 HIS n 
1 418 HIS n 
1 419 HIS n 
1 420 HIS n 
1 421 HIS n 
1 422 HIS n 
1 423 HIS n 
1 424 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   424 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'IDH1, PICD' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1AI4 non-polymer         . 
;2-methyl-2-(6-{4-[(2S)-1,1,1-trifluoro-2-hydroxypropan-2-yl]benzoyl}-6,11-dihydro-5H-pyrido[2,3-b][1,5]benzodiazepin-8-yl)propanenitrile
;
?                                            'C26 H23 F3 N4 O2'  480.482 
ALA   'L-peptide linking' y ALANINE ?                                            'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE ?                                            'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                                            'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                                            'C4 H7 N O4'        133.103 
CYS   'L-peptide linking' y CYSTEINE ?                                            'C3 H7 N O2 S'      121.158 
GLN   'L-peptide linking' y GLUTAMINE ?                                            'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                                            'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE ?                                            'C2 H5 N O2'        75.067  
GOL   non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL'              'C3 H8 O3'          92.094  
HIS   'L-peptide linking' y HISTIDINE ?                                            'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER ?                                            'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                                            'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE ?                                            'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE ?                                            'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE ?                                            'C5 H11 N O2 S'     149.211 
NAP   non-polymer         . 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 
;2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
;
'C21 H28 N7 O17 P3' 743.405 
PHE   'L-peptide linking' y PHENYLALANINE ?                                            'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE ?                                            'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE ?                                            'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE ?                                            'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                                            'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE ?                                            'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE ?                                            'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   LYS 4   4   4   LYS LYS A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   SER 6   6   6   SER SER A . n 
A 1 7   GLY 7   7   7   GLY GLY A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   SER 9   9   9   SER SER A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  VAL 11  11  11  VAL VAL A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  MET 13  13  13  MET MET A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  MET 18  18  18  MET MET A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  TRP 23  23  23  TRP TRP A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  ILE 26  26  26  ILE ILE A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  TYR 34  34  34  TYR TYR A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  HIS 40  40  40  HIS HIS A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  ASP 43  43  43  ASP ASP A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASN 48  48  48  ASN ASN A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  LYS 66  66  66  LYS LYS A . n 
A 1 67  HIS 67  67  67  HIS HIS A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  LYS 72  72  72  LYS LYS A . n 
A 1 73  CYS 73  73  73  CYS CYS A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  ASP 79  79  79  ASP ASP A . n 
A 1 80  GLU 80  80  80  GLU GLU A . n 
A 1 81  LYS 81  81  81  LYS LYS A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  PHE 86  86  86  PHE PHE A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  GLN 90  90  90  GLN GLN A . n 
A 1 91  MET 91  91  91  MET MET A . n 
A 1 92  TRP 92  92  92  TRP TRP A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 PHE 108 108 108 PHE PHE A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 CYS 114 114 114 CYS CYS A . n 
A 1 115 LYS 115 115 115 LYS LYS A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 PRO 118 118 118 PRO PRO A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 SER 122 122 122 SER SER A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 TRP 124 124 124 TRP TRP A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 ILE 128 128 128 ILE ILE A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 HIS 132 132 132 HIS HIS A . n 
A 1 133 HIS 133 133 133 HIS HIS A . n 
A 1 134 ALA 134 134 ?   ?   ?   A . n 
A 1 135 TYR 135 135 ?   ?   ?   A . n 
A 1 136 GLY 136 136 ?   ?   ?   A . n 
A 1 137 ASP 137 137 ?   ?   ?   A . n 
A 1 138 GLN 138 138 ?   ?   ?   A . n 
A 1 139 TYR 139 139 ?   ?   ?   A . n 
A 1 140 ARG 140 140 140 ARG ARG A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 VAL 145 145 145 VAL VAL A . n 
A 1 146 VAL 146 146 146 VAL VAL A . n 
A 1 147 PRO 147 147 147 PRO PRO A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 ILE 154 154 154 ILE ILE A . n 
A 1 155 THR 155 155 155 THR THR A . n 
A 1 156 TYR 156 156 156 TYR TYR A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 PRO 158 158 158 PRO PRO A . n 
A 1 159 SER 159 159 159 SER SER A . n 
A 1 160 ASP 160 160 160 ASP ASP A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 LYS 164 164 164 LYS LYS A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 HIS 170 170 170 HIS HIS A . n 
A 1 171 ASN 171 171 171 ASN ASN A . n 
A 1 172 PHE 172 172 172 PHE PHE A . n 
A 1 173 GLU 173 173 173 GLU GLU A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 MET 180 180 180 MET MET A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 MET 182 182 182 MET MET A . n 
A 1 183 TYR 183 183 183 TYR TYR A . n 
A 1 184 ASN 184 184 184 ASN ASN A . n 
A 1 185 GLN 185 185 185 GLN GLN A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 LYS 187 187 187 LYS LYS A . n 
A 1 188 SER 188 188 188 SER SER A . n 
A 1 189 ILE 189 189 189 ILE ILE A . n 
A 1 190 GLU 190 190 190 GLU GLU A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 PHE 192 192 192 PHE PHE A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 HIS 194 194 194 HIS HIS A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 PHE 197 197 197 PHE PHE A . n 
A 1 198 GLN 198 198 198 GLN GLN A . n 
A 1 199 MET 199 199 199 MET MET A . n 
A 1 200 ALA 200 200 200 ALA ALA A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 TRP 205 205 205 TRP TRP A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 TYR 208 208 208 TYR TYR A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 THR 211 211 211 THR THR A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 LYS 217 217 217 LYS LYS A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 TYR 219 219 219 TYR TYR A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 ASP 225 225 225 ASP ASP A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 PHE 227 227 227 PHE PHE A . n 
A 1 228 GLN 228 228 228 GLN GLN A . n 
A 1 229 GLU 229 229 229 GLU GLU A . n 
A 1 230 ILE 230 230 230 ILE ILE A . n 
A 1 231 TYR 231 231 231 TYR TYR A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 LYS 233 233 233 LYS LYS A . n 
A 1 234 GLN 234 234 234 GLN GLN A . n 
A 1 235 TYR 235 235 235 TYR TYR A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 SER 237 237 237 SER SER A . n 
A 1 238 GLN 238 238 238 GLN GLN A . n 
A 1 239 PHE 239 239 239 PHE PHE A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 GLN 242 242 242 GLN GLN A . n 
A 1 243 LYS 243 243 243 LYS LYS A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 TRP 245 245 245 TRP TRP A . n 
A 1 246 TYR 246 246 246 TYR TYR A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 HIS 248 248 248 HIS HIS A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 ILE 251 251 251 ILE ILE A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 MET 254 254 254 MET MET A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 GLN 257 257 257 GLN GLN A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 MET 259 259 259 MET MET A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 PHE 265 265 265 PHE PHE A . n 
A 1 266 ILE 266 266 266 ILE ILE A . n 
A 1 267 TRP 267 267 267 TRP TRP A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 CYS 269 269 269 CYS CYS A . n 
A 1 270 LYS 270 270 270 LYS LYS A . n 
A 1 271 ASN 271 271 271 ASN ASN A . n 
A 1 272 TYR 272 272 ?   ?   ?   A . n 
A 1 273 ASP 273 273 ?   ?   ?   A . n 
A 1 274 GLY 274 274 ?   ?   ?   A . n 
A 1 275 ASP 275 275 ?   ?   ?   A . n 
A 1 276 VAL 276 276 ?   ?   ?   A . n 
A 1 277 GLN 277 277 ?   ?   ?   A . n 
A 1 278 SER 278 278 ?   ?   ?   A . n 
A 1 279 ASP 279 279 ?   ?   ?   A . n 
A 1 280 SER 280 280 ?   ?   ?   A . n 
A 1 281 VAL 281 281 ?   ?   ?   A . n 
A 1 282 ALA 282 282 ?   ?   ?   A . n 
A 1 283 GLN 283 283 ?   ?   ?   A . n 
A 1 284 GLY 284 284 ?   ?   ?   A . n 
A 1 285 TYR 285 285 ?   ?   ?   A . n 
A 1 286 GLY 286 286 ?   ?   ?   A . n 
A 1 287 SER 287 287 287 SER SER A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 GLY 289 289 289 GLY GLY A . n 
A 1 290 MET 290 290 290 MET MET A . n 
A 1 291 MET 291 291 291 MET MET A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 VAL 294 294 294 VAL VAL A . n 
A 1 295 LEU 295 295 295 LEU LEU A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 CYS 297 297 297 CYS CYS A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 ASP 299 299 299 ASP ASP A . n 
A 1 300 GLY 300 300 300 GLY GLY A . n 
A 1 301 LYS 301 301 301 LYS LYS A . n 
A 1 302 THR 302 302 302 THR THR A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 GLU 304 304 304 GLU GLU A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 GLU 306 306 306 GLU GLU A . n 
A 1 307 ALA 307 307 307 ALA ALA A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 HIS 309 309 309 HIS HIS A . n 
A 1 310 GLY 310 310 310 GLY GLY A . n 
A 1 311 THR 311 311 311 THR THR A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 THR 313 313 313 THR THR A . n 
A 1 314 ARG 314 314 314 ARG ARG A . n 
A 1 315 HIS 315 315 315 HIS HIS A . n 
A 1 316 TYR 316 316 316 TYR TYR A . n 
A 1 317 ARG 317 317 317 ARG ARG A . n 
A 1 318 MET 318 318 318 MET MET A . n 
A 1 319 TYR 319 319 319 TYR TYR A . n 
A 1 320 GLN 320 320 320 GLN GLN A . n 
A 1 321 LYS 321 321 321 LYS LYS A . n 
A 1 322 GLY 322 322 322 GLY GLY A . n 
A 1 323 GLN 323 323 323 GLN GLN A . n 
A 1 324 GLU 324 324 324 GLU GLU A . n 
A 1 325 THR 325 325 325 THR THR A . n 
A 1 326 SER 326 326 326 SER SER A . n 
A 1 327 THR 327 327 327 THR THR A . n 
A 1 328 ASN 328 328 328 ASN ASN A . n 
A 1 329 PRO 329 329 329 PRO PRO A . n 
A 1 330 ILE 330 330 330 ILE ILE A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 SER 332 332 332 SER SER A . n 
A 1 333 ILE 333 333 333 ILE ILE A . n 
A 1 334 PHE 334 334 334 PHE PHE A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 TRP 336 336 336 TRP TRP A . n 
A 1 337 THR 337 337 337 THR THR A . n 
A 1 338 ARG 338 338 338 ARG ARG A . n 
A 1 339 GLY 339 339 339 GLY GLY A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 ALA 341 341 341 ALA ALA A . n 
A 1 342 HIS 342 342 342 HIS HIS A . n 
A 1 343 ARG 343 343 343 ARG ARG A . n 
A 1 344 ALA 344 344 344 ALA ALA A . n 
A 1 345 LYS 345 345 345 LYS LYS A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 ASP 347 347 347 ASP ASP A . n 
A 1 348 ASN 348 348 348 ASN ASN A . n 
A 1 349 ASN 349 349 349 ASN ASN A . n 
A 1 350 LYS 350 350 350 LYS LYS A . n 
A 1 351 GLU 351 351 351 GLU GLU A . n 
A 1 352 LEU 352 352 352 LEU LEU A . n 
A 1 353 ALA 353 353 353 ALA ALA A . n 
A 1 354 PHE 354 354 354 PHE PHE A . n 
A 1 355 PHE 355 355 355 PHE PHE A . n 
A 1 356 ALA 356 356 356 ALA ALA A . n 
A 1 357 ASN 357 357 357 ASN ASN A . n 
A 1 358 ALA 358 358 358 ALA ALA A . n 
A 1 359 LEU 359 359 359 LEU LEU A . n 
A 1 360 GLU 360 360 360 GLU GLU A . n 
A 1 361 GLU 361 361 361 GLU GLU A . n 
A 1 362 VAL 362 362 362 VAL VAL A . n 
A 1 363 SER 363 363 363 SER SER A . n 
A 1 364 ILE 364 364 364 ILE ILE A . n 
A 1 365 GLU 365 365 365 GLU GLU A . n 
A 1 366 THR 366 366 366 THR THR A . n 
A 1 367 ILE 367 367 367 ILE ILE A . n 
A 1 368 GLU 368 368 368 GLU GLU A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 GLY 370 370 370 GLY GLY A . n 
A 1 371 PHE 371 371 371 PHE PHE A . n 
A 1 372 MET 372 372 372 MET MET A . n 
A 1 373 THR 373 373 373 THR THR A . n 
A 1 374 LYS 374 374 374 LYS LYS A . n 
A 1 375 ASP 375 375 375 ASP ASP A . n 
A 1 376 LEU 376 376 376 LEU LEU A . n 
A 1 377 ALA 377 377 377 ALA ALA A . n 
A 1 378 ALA 378 378 378 ALA ALA A . n 
A 1 379 CYS 379 379 379 CYS CYS A . n 
A 1 380 ILE 380 380 380 ILE ILE A . n 
A 1 381 LYS 381 381 381 LYS LYS A . n 
A 1 382 GLY 382 382 382 GLY GLY A . n 
A 1 383 LEU 383 383 383 LEU LEU A . n 
A 1 384 PRO 384 384 384 PRO PRO A . n 
A 1 385 ASN 385 385 385 ASN ASN A . n 
A 1 386 VAL 386 386 386 VAL VAL A . n 
A 1 387 GLN 387 387 387 GLN GLN A . n 
A 1 388 ARG 388 388 388 ARG ARG A . n 
A 1 389 SER 389 389 389 SER SER A . n 
A 1 390 ASP 390 390 390 ASP ASP A . n 
A 1 391 TYR 391 391 391 TYR TYR A . n 
A 1 392 LEU 392 392 392 LEU LEU A . n 
A 1 393 ASN 393 393 393 ASN ASN A . n 
A 1 394 THR 394 394 394 THR THR A . n 
A 1 395 PHE 395 395 395 PHE PHE A . n 
A 1 396 GLU 396 396 396 GLU GLU A . n 
A 1 397 PHE 397 397 397 PHE PHE A . n 
A 1 398 MET 398 398 398 MET MET A . n 
A 1 399 ASP 399 399 399 ASP ASP A . n 
A 1 400 LYS 400 400 400 LYS LYS A . n 
A 1 401 LEU 401 401 401 LEU LEU A . n 
A 1 402 GLY 402 402 402 GLY GLY A . n 
A 1 403 GLU 403 403 403 GLU GLU A . n 
A 1 404 ASN 404 404 404 ASN ASN A . n 
A 1 405 LEU 405 405 405 LEU LEU A . n 
A 1 406 LYS 406 406 406 LYS LYS A . n 
A 1 407 ILE 407 407 407 ILE ILE A . n 
A 1 408 LYS 408 408 408 LYS LYS A . n 
A 1 409 LEU 409 409 409 LEU LEU A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 GLN 411 411 411 GLN GLN A . n 
A 1 412 ALA 412 412 412 ALA ALA A . n 
A 1 413 LYS 413 413 413 LYS LYS A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 LEU 415 415 ?   ?   ?   A . n 
A 1 416 GLU 416 416 ?   ?   ?   A . n 
A 1 417 HIS 417 417 ?   ?   ?   A . n 
A 1 418 HIS 418 418 ?   ?   ?   A . n 
A 1 419 HIS 419 419 ?   ?   ?   A . n 
A 1 420 HIS 420 420 ?   ?   ?   A . n 
A 1 421 HIS 421 421 ?   ?   ?   A . n 
A 1 422 HIS 422 422 ?   ?   ?   A . n 
A 1 423 HIS 423 423 ?   ?   ?   A . n 
A 1 424 HIS 424 424 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   LYS 4   4   4   LYS LYS B . n 
B 1 5   ILE 5   5   5   ILE ILE B . n 
B 1 6   SER 6   6   6   SER SER B . n 
B 1 7   GLY 7   7   7   GLY GLY B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   SER 9   9   9   SER SER B . n 
B 1 10  VAL 10  10  10  VAL VAL B . n 
B 1 11  VAL 11  11  11  VAL VAL B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  MET 13  13  13  MET MET B . n 
B 1 14  GLN 14  14  14  GLN GLN B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  ASP 16  16  16  ASP ASP B . n 
B 1 17  GLU 17  17  17  GLU GLU B . n 
B 1 18  MET 18  18  18  MET MET B . n 
B 1 19  THR 19  19  19  THR THR B . n 
B 1 20  ARG 20  20  20  ARG ARG B . n 
B 1 21  ILE 21  21  21  ILE ILE B . n 
B 1 22  ILE 22  22  22  ILE ILE B . n 
B 1 23  TRP 23  23  23  TRP TRP B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  ILE 26  26  26  ILE ILE B . n 
B 1 27  LYS 27  27  27  LYS LYS B . n 
B 1 28  GLU 28  28  28  GLU GLU B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  ILE 31  31  31  ILE ILE B . n 
B 1 32  PHE 32  32  32  PHE PHE B . n 
B 1 33  PRO 33  33  33  PRO PRO B . n 
B 1 34  TYR 34  34  34  TYR TYR B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  GLU 36  36  36  GLU GLU B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  ASP 38  38  38  ASP ASP B . n 
B 1 39  LEU 39  39  39  LEU LEU B . n 
B 1 40  HIS 40  40  40  HIS HIS B . n 
B 1 41  SER 41  41  41  SER SER B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  ASP 43  43  43  ASP ASP B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ASN 48  48  48  ASN ASN B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  ASP 50  50  50  ASP ASP B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  THR 52  52  52  THR THR B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  ASP 54  54  54  ASP ASP B . n 
B 1 55  GLN 55  55  55  GLN GLN B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  LYS 58  58  58  LYS LYS B . n 
B 1 59  ASP 59  59  59  ASP ASP B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  ALA 63  63  63  ALA ALA B . n 
B 1 64  ILE 64  64  64  ILE ILE B . n 
B 1 65  LYS 65  65  65  LYS LYS B . n 
B 1 66  LYS 66  66  66  LYS LYS B . n 
B 1 67  HIS 67  67  67  HIS HIS B . n 
B 1 68  ASN 68  68  68  ASN ASN B . n 
B 1 69  VAL 69  69  69  VAL VAL B . n 
B 1 70  GLY 70  70  70  GLY GLY B . n 
B 1 71  VAL 71  71  71  VAL VAL B . n 
B 1 72  LYS 72  72  72  LYS LYS B . n 
B 1 73  CYS 73  73  73  CYS CYS B . n 
B 1 74  ALA 74  74  74  ALA ALA B . n 
B 1 75  THR 75  75  75  THR THR B . n 
B 1 76  ILE 76  76  76  ILE ILE B . n 
B 1 77  THR 77  77  77  THR THR B . n 
B 1 78  PRO 78  78  78  PRO PRO B . n 
B 1 79  ASP 79  79  79  ASP ASP B . n 
B 1 80  GLU 80  80  80  GLU GLU B . n 
B 1 81  LYS 81  81  81  LYS LYS B . n 
B 1 82  ARG 82  82  82  ARG ARG B . n 
B 1 83  VAL 83  83  83  VAL VAL B . n 
B 1 84  GLU 84  84  84  GLU GLU B . n 
B 1 85  GLU 85  85  85  GLU GLU B . n 
B 1 86  PHE 86  86  86  PHE PHE B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  GLN 90  90  90  GLN GLN B . n 
B 1 91  MET 91  91  91  MET MET B . n 
B 1 92  TRP 92  92  92  TRP TRP B . n 
B 1 93  LYS 93  93  93  LYS LYS B . n 
B 1 94  SER 94  94  94  SER SER B . n 
B 1 95  PRO 95  95  95  PRO PRO B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 ARG 100 100 100 ARG ARG B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 ILE 102 102 102 ILE ILE B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 GLY 105 105 105 GLY GLY B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 PHE 108 108 108 PHE PHE B . n 
B 1 109 ARG 109 109 109 ARG ARG B . n 
B 1 110 GLU 110 110 110 GLU GLU B . n 
B 1 111 ALA 111 111 111 ALA ALA B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 CYS 114 114 114 CYS CYS B . n 
B 1 115 LYS 115 115 115 LYS LYS B . n 
B 1 116 ASN 116 116 116 ASN ASN B . n 
B 1 117 ILE 117 117 117 ILE ILE B . n 
B 1 118 PRO 118 118 118 PRO PRO B . n 
B 1 119 ARG 119 119 119 ARG ARG B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 SER 122 122 122 SER SER B . n 
B 1 123 GLY 123 123 123 GLY GLY B . n 
B 1 124 TRP 124 124 124 TRP TRP B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 LYS 126 126 126 LYS LYS B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 ILE 128 128 128 ILE ILE B . n 
B 1 129 ILE 129 129 129 ILE ILE B . n 
B 1 130 ILE 130 130 130 ILE ILE B . n 
B 1 131 GLY 131 131 131 GLY GLY B . n 
B 1 132 HIS 132 132 132 HIS HIS B . n 
B 1 133 HIS 133 133 133 HIS HIS B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 TYR 135 135 ?   ?   ?   B . n 
B 1 136 GLY 136 136 ?   ?   ?   B . n 
B 1 137 ASP 137 137 ?   ?   ?   B . n 
B 1 138 GLN 138 138 ?   ?   ?   B . n 
B 1 139 TYR 139 139 ?   ?   ?   B . n 
B 1 140 ARG 140 140 140 ARG ARG B . n 
B 1 141 ALA 141 141 141 ALA ALA B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 ASP 143 143 143 ASP ASP B . n 
B 1 144 PHE 144 144 144 PHE PHE B . n 
B 1 145 VAL 145 145 145 VAL VAL B . n 
B 1 146 VAL 146 146 146 VAL VAL B . n 
B 1 147 PRO 147 147 147 PRO PRO B . n 
B 1 148 GLY 148 148 148 GLY GLY B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 LYS 151 151 151 LYS LYS B . n 
B 1 152 VAL 152 152 152 VAL VAL B . n 
B 1 153 GLU 153 153 153 GLU GLU B . n 
B 1 154 ILE 154 154 154 ILE ILE B . n 
B 1 155 THR 155 155 155 THR THR B . n 
B 1 156 TYR 156 156 156 TYR TYR B . n 
B 1 157 THR 157 157 157 THR THR B . n 
B 1 158 PRO 158 158 158 PRO PRO B . n 
B 1 159 SER 159 159 159 SER SER B . n 
B 1 160 ASP 160 160 160 ASP ASP B . n 
B 1 161 GLY 161 161 161 GLY GLY B . n 
B 1 162 THR 162 162 162 THR THR B . n 
B 1 163 GLN 163 163 163 GLN GLN B . n 
B 1 164 LYS 164 164 164 LYS LYS B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 THR 166 166 166 THR THR B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 LEU 168 168 168 LEU LEU B . n 
B 1 169 VAL 169 169 169 VAL VAL B . n 
B 1 170 HIS 170 170 170 HIS HIS B . n 
B 1 171 ASN 171 171 171 ASN ASN B . n 
B 1 172 PHE 172 172 172 PHE PHE B . n 
B 1 173 GLU 173 173 173 GLU GLU B . n 
B 1 174 GLU 174 174 174 GLU GLU B . n 
B 1 175 GLY 175 175 175 GLY GLY B . n 
B 1 176 GLY 176 176 176 GLY GLY B . n 
B 1 177 GLY 177 177 177 GLY GLY B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 ALA 179 179 179 ALA ALA B . n 
B 1 180 MET 180 180 180 MET MET B . n 
B 1 181 GLY 181 181 181 GLY GLY B . n 
B 1 182 MET 182 182 182 MET MET B . n 
B 1 183 TYR 183 183 183 TYR TYR B . n 
B 1 184 ASN 184 184 184 ASN ASN B . n 
B 1 185 GLN 185 185 185 GLN GLN B . n 
B 1 186 ASP 186 186 186 ASP ASP B . n 
B 1 187 LYS 187 187 187 LYS LYS B . n 
B 1 188 SER 188 188 188 SER SER B . n 
B 1 189 ILE 189 189 189 ILE ILE B . n 
B 1 190 GLU 190 190 190 GLU GLU B . n 
B 1 191 ASP 191 191 191 ASP ASP B . n 
B 1 192 PHE 192 192 192 PHE PHE B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 HIS 194 194 194 HIS HIS B . n 
B 1 195 SER 195 195 195 SER SER B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 PHE 197 197 197 PHE PHE B . n 
B 1 198 GLN 198 198 198 GLN GLN B . n 
B 1 199 MET 199 199 199 MET MET B . n 
B 1 200 ALA 200 200 200 ALA ALA B . n 
B 1 201 LEU 201 201 201 LEU LEU B . n 
B 1 202 SER 202 202 202 SER SER B . n 
B 1 203 LYS 203 203 203 LYS LYS B . n 
B 1 204 GLY 204 204 204 GLY GLY B . n 
B 1 205 TRP 205 205 205 TRP TRP B . n 
B 1 206 PRO 206 206 206 PRO PRO B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 TYR 208 208 208 TYR TYR B . n 
B 1 209 LEU 209 209 209 LEU LEU B . n 
B 1 210 SER 210 210 210 SER SER B . n 
B 1 211 THR 211 211 211 THR THR B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 THR 214 214 214 THR THR B . n 
B 1 215 ILE 215 215 215 ILE ILE B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 LYS 217 217 217 LYS LYS B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 TYR 219 219 219 TYR TYR B . n 
B 1 220 ASP 220 220 220 ASP ASP B . n 
B 1 221 GLY 221 221 221 GLY GLY B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 LYS 224 224 224 LYS LYS B . n 
B 1 225 ASP 225 225 225 ASP ASP B . n 
B 1 226 ILE 226 226 226 ILE ILE B . n 
B 1 227 PHE 227 227 227 PHE PHE B . n 
B 1 228 GLN 228 228 228 GLN GLN B . n 
B 1 229 GLU 229 229 229 GLU GLU B . n 
B 1 230 ILE 230 230 230 ILE ILE B . n 
B 1 231 TYR 231 231 231 TYR TYR B . n 
B 1 232 ASP 232 232 232 ASP ASP B . n 
B 1 233 LYS 233 233 233 LYS LYS B . n 
B 1 234 GLN 234 234 234 GLN GLN B . n 
B 1 235 TYR 235 235 235 TYR TYR B . n 
B 1 236 LYS 236 236 236 LYS LYS B . n 
B 1 237 SER 237 237 237 SER SER B . n 
B 1 238 GLN 238 238 238 GLN GLN B . n 
B 1 239 PHE 239 239 239 PHE PHE B . n 
B 1 240 GLU 240 240 240 GLU GLU B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 GLN 242 242 242 GLN GLN B . n 
B 1 243 LYS 243 243 243 LYS LYS B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 TRP 245 245 245 TRP TRP B . n 
B 1 246 TYR 246 246 246 TYR TYR B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 HIS 248 248 248 HIS HIS B . n 
B 1 249 ARG 249 249 249 ARG ARG B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 ILE 251 251 251 ILE ILE B . n 
B 1 252 ASP 252 252 252 ASP ASP B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 MET 254 254 254 MET MET B . n 
B 1 255 VAL 255 255 255 VAL VAL B . n 
B 1 256 ALA 256 256 256 ALA ALA B . n 
B 1 257 GLN 257 257 257 GLN GLN B . n 
B 1 258 ALA 258 258 258 ALA ALA B . n 
B 1 259 MET 259 259 259 MET MET B . n 
B 1 260 LYS 260 260 260 LYS LYS B . n 
B 1 261 SER 261 261 261 SER SER B . n 
B 1 262 GLU 262 262 262 GLU GLU B . n 
B 1 263 GLY 263 263 263 GLY GLY B . n 
B 1 264 GLY 264 264 264 GLY GLY B . n 
B 1 265 PHE 265 265 265 PHE PHE B . n 
B 1 266 ILE 266 266 266 ILE ILE B . n 
B 1 267 TRP 267 267 267 TRP TRP B . n 
B 1 268 ALA 268 268 268 ALA ALA B . n 
B 1 269 CYS 269 269 269 CYS CYS B . n 
B 1 270 LYS 270 270 270 LYS LYS B . n 
B 1 271 ASN 271 271 271 ASN ASN B . n 
B 1 272 TYR 272 272 ?   ?   ?   B . n 
B 1 273 ASP 273 273 ?   ?   ?   B . n 
B 1 274 GLY 274 274 ?   ?   ?   B . n 
B 1 275 ASP 275 275 ?   ?   ?   B . n 
B 1 276 VAL 276 276 ?   ?   ?   B . n 
B 1 277 GLN 277 277 ?   ?   ?   B . n 
B 1 278 SER 278 278 ?   ?   ?   B . n 
B 1 279 ASP 279 279 ?   ?   ?   B . n 
B 1 280 SER 280 280 ?   ?   ?   B . n 
B 1 281 VAL 281 281 ?   ?   ?   B . n 
B 1 282 ALA 282 282 ?   ?   ?   B . n 
B 1 283 GLN 283 283 ?   ?   ?   B . n 
B 1 284 GLY 284 284 ?   ?   ?   B . n 
B 1 285 TYR 285 285 ?   ?   ?   B . n 
B 1 286 GLY 286 286 ?   ?   ?   B . n 
B 1 287 SER 287 287 287 SER SER B . n 
B 1 288 LEU 288 288 288 LEU LEU B . n 
B 1 289 GLY 289 289 289 GLY GLY B . n 
B 1 290 MET 290 290 290 MET MET B . n 
B 1 291 MET 291 291 291 MET MET B . n 
B 1 292 THR 292 292 292 THR THR B . n 
B 1 293 SER 293 293 293 SER SER B . n 
B 1 294 VAL 294 294 294 VAL VAL B . n 
B 1 295 LEU 295 295 295 LEU LEU B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 CYS 297 297 297 CYS CYS B . n 
B 1 298 PRO 298 298 298 PRO PRO B . n 
B 1 299 ASP 299 299 299 ASP ASP B . n 
B 1 300 GLY 300 300 300 GLY GLY B . n 
B 1 301 LYS 301 301 301 LYS LYS B . n 
B 1 302 THR 302 302 302 THR THR B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 GLU 304 304 304 GLU GLU B . n 
B 1 305 ALA 305 305 305 ALA ALA B . n 
B 1 306 GLU 306 306 306 GLU GLU B . n 
B 1 307 ALA 307 307 307 ALA ALA B . n 
B 1 308 ALA 308 308 308 ALA ALA B . n 
B 1 309 HIS 309 309 309 HIS HIS B . n 
B 1 310 GLY 310 310 310 GLY GLY B . n 
B 1 311 THR 311 311 311 THR THR B . n 
B 1 312 VAL 312 312 312 VAL VAL B . n 
B 1 313 THR 313 313 313 THR THR B . n 
B 1 314 ARG 314 314 314 ARG ARG B . n 
B 1 315 HIS 315 315 315 HIS HIS B . n 
B 1 316 TYR 316 316 316 TYR TYR B . n 
B 1 317 ARG 317 317 317 ARG ARG B . n 
B 1 318 MET 318 318 318 MET MET B . n 
B 1 319 TYR 319 319 319 TYR TYR B . n 
B 1 320 GLN 320 320 320 GLN GLN B . n 
B 1 321 LYS 321 321 321 LYS LYS B . n 
B 1 322 GLY 322 322 322 GLY GLY B . n 
B 1 323 GLN 323 323 323 GLN GLN B . n 
B 1 324 GLU 324 324 324 GLU GLU B . n 
B 1 325 THR 325 325 325 THR THR B . n 
B 1 326 SER 326 326 326 SER SER B . n 
B 1 327 THR 327 327 327 THR THR B . n 
B 1 328 ASN 328 328 328 ASN ASN B . n 
B 1 329 PRO 329 329 329 PRO PRO B . n 
B 1 330 ILE 330 330 330 ILE ILE B . n 
B 1 331 ALA 331 331 331 ALA ALA B . n 
B 1 332 SER 332 332 332 SER SER B . n 
B 1 333 ILE 333 333 333 ILE ILE B . n 
B 1 334 PHE 334 334 334 PHE PHE B . n 
B 1 335 ALA 335 335 335 ALA ALA B . n 
B 1 336 TRP 336 336 336 TRP TRP B . n 
B 1 337 THR 337 337 337 THR THR B . n 
B 1 338 ARG 338 338 338 ARG ARG B . n 
B 1 339 GLY 339 339 339 GLY GLY B . n 
B 1 340 LEU 340 340 340 LEU LEU B . n 
B 1 341 ALA 341 341 341 ALA ALA B . n 
B 1 342 HIS 342 342 342 HIS HIS B . n 
B 1 343 ARG 343 343 343 ARG ARG B . n 
B 1 344 ALA 344 344 344 ALA ALA B . n 
B 1 345 LYS 345 345 345 LYS LYS B . n 
B 1 346 LEU 346 346 346 LEU LEU B . n 
B 1 347 ASP 347 347 347 ASP ASP B . n 
B 1 348 ASN 348 348 348 ASN ASN B . n 
B 1 349 ASN 349 349 349 ASN ASN B . n 
B 1 350 LYS 350 350 350 LYS LYS B . n 
B 1 351 GLU 351 351 351 GLU GLU B . n 
B 1 352 LEU 352 352 352 LEU LEU B . n 
B 1 353 ALA 353 353 353 ALA ALA B . n 
B 1 354 PHE 354 354 354 PHE PHE B . n 
B 1 355 PHE 355 355 355 PHE PHE B . n 
B 1 356 ALA 356 356 356 ALA ALA B . n 
B 1 357 ASN 357 357 357 ASN ASN B . n 
B 1 358 ALA 358 358 358 ALA ALA B . n 
B 1 359 LEU 359 359 359 LEU LEU B . n 
B 1 360 GLU 360 360 360 GLU GLU B . n 
B 1 361 GLU 361 361 361 GLU GLU B . n 
B 1 362 VAL 362 362 362 VAL VAL B . n 
B 1 363 SER 363 363 363 SER SER B . n 
B 1 364 ILE 364 364 364 ILE ILE B . n 
B 1 365 GLU 365 365 365 GLU GLU B . n 
B 1 366 THR 366 366 366 THR THR B . n 
B 1 367 ILE 367 367 367 ILE ILE B . n 
B 1 368 GLU 368 368 368 GLU GLU B . n 
B 1 369 ALA 369 369 369 ALA ALA B . n 
B 1 370 GLY 370 370 370 GLY GLY B . n 
B 1 371 PHE 371 371 371 PHE PHE B . n 
B 1 372 MET 372 372 372 MET MET B . n 
B 1 373 THR 373 373 373 THR THR B . n 
B 1 374 LYS 374 374 374 LYS LYS B . n 
B 1 375 ASP 375 375 375 ASP ASP B . n 
B 1 376 LEU 376 376 376 LEU LEU B . n 
B 1 377 ALA 377 377 377 ALA ALA B . n 
B 1 378 ALA 378 378 378 ALA ALA B . n 
B 1 379 CYS 379 379 379 CYS CYS B . n 
B 1 380 ILE 380 380 380 ILE ILE B . n 
B 1 381 LYS 381 381 381 LYS LYS B . n 
B 1 382 GLY 382 382 382 GLY GLY B . n 
B 1 383 LEU 383 383 383 LEU LEU B . n 
B 1 384 PRO 384 384 384 PRO PRO B . n 
B 1 385 ASN 385 385 385 ASN ASN B . n 
B 1 386 VAL 386 386 386 VAL VAL B . n 
B 1 387 GLN 387 387 387 GLN GLN B . n 
B 1 388 ARG 388 388 388 ARG ARG B . n 
B 1 389 SER 389 389 389 SER SER B . n 
B 1 390 ASP 390 390 390 ASP ASP B . n 
B 1 391 TYR 391 391 391 TYR TYR B . n 
B 1 392 LEU 392 392 392 LEU LEU B . n 
B 1 393 ASN 393 393 393 ASN ASN B . n 
B 1 394 THR 394 394 394 THR THR B . n 
B 1 395 PHE 395 395 395 PHE PHE B . n 
B 1 396 GLU 396 396 396 GLU GLU B . n 
B 1 397 PHE 397 397 397 PHE PHE B . n 
B 1 398 MET 398 398 398 MET MET B . n 
B 1 399 ASP 399 399 399 ASP ASP B . n 
B 1 400 LYS 400 400 400 LYS LYS B . n 
B 1 401 LEU 401 401 401 LEU LEU B . n 
B 1 402 GLY 402 402 402 GLY GLY B . n 
B 1 403 GLU 403 403 403 GLU GLU B . n 
B 1 404 ASN 404 404 404 ASN ASN B . n 
B 1 405 LEU 405 405 405 LEU LEU B . n 
B 1 406 LYS 406 406 406 LYS LYS B . n 
B 1 407 ILE 407 407 407 ILE ILE B . n 
B 1 408 LYS 408 408 408 LYS LYS B . n 
B 1 409 LEU 409 409 409 LEU LEU B . n 
B 1 410 ALA 410 410 410 ALA ALA B . n 
B 1 411 GLN 411 411 411 GLN GLN B . n 
B 1 412 ALA 412 412 412 ALA ALA B . n 
B 1 413 LYS 413 413 ?   ?   ?   B . n 
B 1 414 LEU 414 414 ?   ?   ?   B . n 
B 1 415 LEU 415 415 ?   ?   ?   B . n 
B 1 416 GLU 416 416 ?   ?   ?   B . n 
B 1 417 HIS 417 417 ?   ?   ?   B . n 
B 1 418 HIS 418 418 ?   ?   ?   B . n 
B 1 419 HIS 419 419 ?   ?   ?   B . n 
B 1 420 HIS 420 420 ?   ?   ?   B . n 
B 1 421 HIS 421 421 ?   ?   ?   B . n 
B 1 422 HIS 422 422 ?   ?   ?   B . n 
B 1 423 HIS 423 423 ?   ?   ?   B . n 
B 1 424 HIS 424 424 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AI4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AI4 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1AI4 1  501 500 A1AI4 UNL A . 
D 3 NAP   1  502 501 NAP   NDP A . 
E 4 GOL   1  503 1   GOL   GOL A . 
F 2 A1AI4 1  500 500 A1AI4 UNL B . 
G 3 NAP   1  501 501 NAP   NDP B . 
H 5 HOH   1  601 44  HOH   HOH A . 
H 5 HOH   2  602 10  HOH   HOH A . 
H 5 HOH   3  603 35  HOH   HOH A . 
H 5 HOH   4  604 24  HOH   HOH A . 
H 5 HOH   5  605 17  HOH   HOH A . 
H 5 HOH   6  606 22  HOH   HOH A . 
H 5 HOH   7  607 30  HOH   HOH A . 
H 5 HOH   8  608 13  HOH   HOH A . 
H 5 HOH   9  609 19  HOH   HOH A . 
H 5 HOH   10 610 33  HOH   HOH A . 
H 5 HOH   11 611 31  HOH   HOH A . 
H 5 HOH   12 612 21  HOH   HOH A . 
H 5 HOH   13 613 34  HOH   HOH A . 
H 5 HOH   14 614 36  HOH   HOH A . 
H 5 HOH   15 615 25  HOH   HOH A . 
H 5 HOH   16 616 2   HOH   HOH A . 
H 5 HOH   17 617 5   HOH   HOH A . 
H 5 HOH   18 618 14  HOH   HOH A . 
H 5 HOH   19 619 6   HOH   HOH A . 
H 5 HOH   20 620 1   HOH   HOH A . 
H 5 HOH   21 621 29  HOH   HOH A . 
H 5 HOH   22 622 37  HOH   HOH A . 
H 5 HOH   23 623 40  HOH   HOH A . 
H 5 HOH   24 624 9   HOH   HOH A . 
H 5 HOH   25 625 15  HOH   HOH A . 
H 5 HOH   26 626 28  HOH   HOH A . 
I 5 HOH   1  601 46  HOH   HOH B . 
I 5 HOH   2  602 45  HOH   HOH B . 
I 5 HOH   3  603 43  HOH   HOH B . 
I 5 HOH   4  604 38  HOH   HOH B . 
I 5 HOH   5  605 47  HOH   HOH B . 
I 5 HOH   6  606 32  HOH   HOH B . 
I 5 HOH   7  607 7   HOH   HOH B . 
I 5 HOH   8  608 23  HOH   HOH B . 
I 5 HOH   9  609 41  HOH   HOH B . 
I 5 HOH   10 610 20  HOH   HOH B . 
I 5 HOH   11 611 3   HOH   HOH B . 
I 5 HOH   12 612 26  HOH   HOH B . 
I 5 HOH   13 613 4   HOH   HOH B . 
I 5 HOH   14 614 16  HOH   HOH B . 
I 5 HOH   15 615 18  HOH   HOH B . 
I 5 HOH   16 616 11  HOH   HOH B . 
I 5 HOH   17 617 39  HOH   HOH B . 
I 5 HOH   18 618 42  HOH   HOH B . 
I 5 HOH   19 619 8   HOH   HOH B . 
I 5 HOH   20 620 12  HOH   HOH B . 
I 5 HOH   21 621 27  HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 3   ? CG  ? A LYS 3   CG  
2   1 Y 1 A LYS 3   ? CD  ? A LYS 3   CD  
3   1 Y 1 A LYS 3   ? CE  ? A LYS 3   CE  
4   1 Y 1 A LYS 3   ? NZ  ? A LYS 3   NZ  
5   1 Y 1 A GLU 80  ? CG  ? A GLU 80  CG  
6   1 Y 1 A GLU 80  ? CD  ? A GLU 80  CD  
7   1 Y 1 A GLU 80  ? OE1 ? A GLU 80  OE1 
8   1 Y 1 A GLU 80  ? OE2 ? A GLU 80  OE2 
9   1 Y 1 A LYS 81  ? CG  ? A LYS 81  CG  
10  1 Y 1 A LYS 81  ? CD  ? A LYS 81  CD  
11  1 Y 1 A LYS 81  ? CE  ? A LYS 81  CE  
12  1 Y 1 A LYS 81  ? NZ  ? A LYS 81  NZ  
13  1 Y 1 A GLU 84  ? CG  ? A GLU 84  CG  
14  1 Y 1 A GLU 84  ? CD  ? A GLU 84  CD  
15  1 Y 1 A GLU 84  ? OE1 ? A GLU 84  OE1 
16  1 Y 1 A GLU 84  ? OE2 ? A GLU 84  OE2 
17  1 Y 1 A LYS 87  ? CG  ? A LYS 87  CG  
18  1 Y 1 A LYS 87  ? CD  ? A LYS 87  CD  
19  1 Y 1 A LYS 87  ? CE  ? A LYS 87  CE  
20  1 Y 1 A LYS 87  ? NZ  ? A LYS 87  NZ  
21  1 Y 1 A LYS 93  ? CG  ? A LYS 93  CG  
22  1 Y 1 A LYS 93  ? CD  ? A LYS 93  CD  
23  1 Y 1 A LYS 93  ? CE  ? A LYS 93  CE  
24  1 Y 1 A LYS 93  ? NZ  ? A LYS 93  NZ  
25  1 Y 1 A ARG 100 ? CG  ? A ARG 100 CG  
26  1 Y 1 A ARG 100 ? CD  ? A ARG 100 CD  
27  1 Y 1 A ARG 100 ? NE  ? A ARG 100 NE  
28  1 Y 1 A ARG 100 ? CZ  ? A ARG 100 CZ  
29  1 Y 1 A ARG 100 ? NH1 ? A ARG 100 NH1 
30  1 Y 1 A ARG 100 ? NH2 ? A ARG 100 NH2 
31  1 Y 1 A ARG 140 ? CG  ? A ARG 140 CG  
32  1 Y 1 A ARG 140 ? CD  ? A ARG 140 CD  
33  1 Y 1 A ARG 140 ? NE  ? A ARG 140 NE  
34  1 Y 1 A ARG 140 ? CZ  ? A ARG 140 CZ  
35  1 Y 1 A ARG 140 ? NH1 ? A ARG 140 NH1 
36  1 Y 1 A ARG 140 ? NH2 ? A ARG 140 NH2 
37  1 Y 1 A GLU 174 ? CG  ? A GLU 174 CG  
38  1 Y 1 A GLU 174 ? CD  ? A GLU 174 CD  
39  1 Y 1 A GLU 174 ? OE1 ? A GLU 174 OE1 
40  1 Y 1 A GLU 174 ? OE2 ? A GLU 174 OE2 
41  1 Y 1 A LYS 187 ? CG  ? A LYS 187 CG  
42  1 Y 1 A LYS 187 ? CD  ? A LYS 187 CD  
43  1 Y 1 A LYS 187 ? CE  ? A LYS 187 CE  
44  1 Y 1 A LYS 187 ? NZ  ? A LYS 187 NZ  
45  1 Y 1 A LYS 212 ? CG  ? A LYS 212 CG  
46  1 Y 1 A LYS 212 ? CD  ? A LYS 212 CD  
47  1 Y 1 A LYS 212 ? CE  ? A LYS 212 CE  
48  1 Y 1 A LYS 212 ? NZ  ? A LYS 212 NZ  
49  1 Y 1 A LYS 233 ? CE  ? A LYS 233 CE  
50  1 Y 1 A LYS 233 ? NZ  ? A LYS 233 NZ  
51  1 Y 1 A LYS 243 ? CG  ? A LYS 243 CG  
52  1 Y 1 A LYS 243 ? CD  ? A LYS 243 CD  
53  1 Y 1 A LYS 243 ? CE  ? A LYS 243 CE  
54  1 Y 1 A LYS 243 ? NZ  ? A LYS 243 NZ  
55  1 Y 1 A ASP 253 ? CG  ? A ASP 253 CG  
56  1 Y 1 A ASP 253 ? OD1 ? A ASP 253 OD1 
57  1 Y 1 A ASP 253 ? OD2 ? A ASP 253 OD2 
58  1 Y 1 A LYS 260 ? CG  ? A LYS 260 CG  
59  1 Y 1 A LYS 260 ? CD  ? A LYS 260 CD  
60  1 Y 1 A LYS 260 ? CE  ? A LYS 260 CE  
61  1 Y 1 A LYS 260 ? NZ  ? A LYS 260 NZ  
62  1 Y 1 A GLU 262 ? CG  ? A GLU 262 CG  
63  1 Y 1 A GLU 262 ? CD  ? A GLU 262 CD  
64  1 Y 1 A GLU 262 ? OE1 ? A GLU 262 OE1 
65  1 Y 1 A GLU 262 ? OE2 ? A GLU 262 OE2 
66  1 Y 1 A LYS 301 ? CG  ? A LYS 301 CG  
67  1 Y 1 A LYS 301 ? CD  ? A LYS 301 CD  
68  1 Y 1 A LYS 301 ? CE  ? A LYS 301 CE  
69  1 Y 1 A LYS 301 ? NZ  ? A LYS 301 NZ  
70  1 Y 1 A ARG 314 ? CG  ? A ARG 314 CG  
71  1 Y 1 A ARG 314 ? CD  ? A ARG 314 CD  
72  1 Y 1 A ARG 314 ? NE  ? A ARG 314 NE  
73  1 Y 1 A ARG 314 ? CZ  ? A ARG 314 CZ  
74  1 Y 1 A ARG 314 ? NH1 ? A ARG 314 NH1 
75  1 Y 1 A ARG 314 ? NH2 ? A ARG 314 NH2 
76  1 Y 1 A LYS 350 ? CG  ? A LYS 350 CG  
77  1 Y 1 A LYS 350 ? CD  ? A LYS 350 CD  
78  1 Y 1 A LYS 350 ? CE  ? A LYS 350 CE  
79  1 Y 1 A LYS 350 ? NZ  ? A LYS 350 NZ  
80  1 Y 1 A GLU 403 ? CG  ? A GLU 403 CG  
81  1 Y 1 A GLU 403 ? CD  ? A GLU 403 CD  
82  1 Y 1 A GLU 403 ? OE1 ? A GLU 403 OE1 
83  1 Y 1 A GLU 403 ? OE2 ? A GLU 403 OE2 
84  1 Y 1 B LYS 3   ? CG  ? B LYS 3   CG  
85  1 Y 1 B LYS 3   ? CD  ? B LYS 3   CD  
86  1 Y 1 B LYS 3   ? CE  ? B LYS 3   CE  
87  1 Y 1 B LYS 3   ? NZ  ? B LYS 3   NZ  
88  1 Y 1 B GLU 47  ? CD  ? B GLU 47  CD  
89  1 Y 1 B GLU 47  ? OE1 ? B GLU 47  OE1 
90  1 Y 1 B GLU 47  ? OE2 ? B GLU 47  OE2 
91  1 Y 1 B GLU 62  ? CG  ? B GLU 62  CG  
92  1 Y 1 B GLU 62  ? CD  ? B GLU 62  CD  
93  1 Y 1 B GLU 62  ? OE1 ? B GLU 62  OE1 
94  1 Y 1 B GLU 62  ? OE2 ? B GLU 62  OE2 
95  1 Y 1 B GLU 80  ? CG  ? B GLU 80  CG  
96  1 Y 1 B GLU 80  ? CD  ? B GLU 80  CD  
97  1 Y 1 B GLU 80  ? OE1 ? B GLU 80  OE1 
98  1 Y 1 B GLU 80  ? OE2 ? B GLU 80  OE2 
99  1 Y 1 B GLU 84  ? CG  ? B GLU 84  CG  
100 1 Y 1 B GLU 84  ? CD  ? B GLU 84  CD  
101 1 Y 1 B GLU 84  ? OE1 ? B GLU 84  OE1 
102 1 Y 1 B GLU 84  ? OE2 ? B GLU 84  OE2 
103 1 Y 1 B LYS 87  ? CE  ? B LYS 87  CE  
104 1 Y 1 B LYS 87  ? NZ  ? B LYS 87  NZ  
105 1 Y 1 B LYS 93  ? CG  ? B LYS 93  CG  
106 1 Y 1 B LYS 93  ? CD  ? B LYS 93  CD  
107 1 Y 1 B LYS 93  ? CE  ? B LYS 93  CE  
108 1 Y 1 B LYS 93  ? NZ  ? B LYS 93  NZ  
109 1 Y 1 B ARG 140 ? CG  ? B ARG 140 CG  
110 1 Y 1 B ARG 140 ? CD  ? B ARG 140 CD  
111 1 Y 1 B ARG 140 ? NE  ? B ARG 140 NE  
112 1 Y 1 B ARG 140 ? CZ  ? B ARG 140 CZ  
113 1 Y 1 B ARG 140 ? NH1 ? B ARG 140 NH1 
114 1 Y 1 B ARG 140 ? NH2 ? B ARG 140 NH2 
115 1 Y 1 B LYS 164 ? CG  ? B LYS 164 CG  
116 1 Y 1 B LYS 164 ? CD  ? B LYS 164 CD  
117 1 Y 1 B LYS 164 ? CE  ? B LYS 164 CE  
118 1 Y 1 B LYS 164 ? NZ  ? B LYS 164 NZ  
119 1 Y 1 B VAL 165 ? CG1 ? B VAL 165 CG1 
120 1 Y 1 B VAL 165 ? CG2 ? B VAL 165 CG2 
121 1 Y 1 B GLU 174 ? CG  ? B GLU 174 CG  
122 1 Y 1 B GLU 174 ? CD  ? B GLU 174 CD  
123 1 Y 1 B GLU 174 ? OE1 ? B GLU 174 OE1 
124 1 Y 1 B GLU 174 ? OE2 ? B GLU 174 OE2 
125 1 Y 1 B LYS 187 ? CG  ? B LYS 187 CG  
126 1 Y 1 B LYS 187 ? CD  ? B LYS 187 CD  
127 1 Y 1 B LYS 187 ? CE  ? B LYS 187 CE  
128 1 Y 1 B LYS 187 ? NZ  ? B LYS 187 NZ  
129 1 Y 1 B SER 202 ? OG  ? B SER 202 OG  
130 1 Y 1 B LYS 212 ? CG  ? B LYS 212 CG  
131 1 Y 1 B LYS 212 ? CD  ? B LYS 212 CD  
132 1 Y 1 B LYS 212 ? CE  ? B LYS 212 CE  
133 1 Y 1 B LYS 212 ? NZ  ? B LYS 212 NZ  
134 1 Y 1 B LYS 233 ? CG  ? B LYS 233 CG  
135 1 Y 1 B LYS 233 ? CD  ? B LYS 233 CD  
136 1 Y 1 B LYS 233 ? CE  ? B LYS 233 CE  
137 1 Y 1 B LYS 233 ? NZ  ? B LYS 233 NZ  
138 1 Y 1 B LYS 236 ? CG  ? B LYS 236 CG  
139 1 Y 1 B LYS 236 ? CD  ? B LYS 236 CD  
140 1 Y 1 B LYS 236 ? CE  ? B LYS 236 CE  
141 1 Y 1 B LYS 236 ? NZ  ? B LYS 236 NZ  
142 1 Y 1 B GLU 240 ? CG  ? B GLU 240 CG  
143 1 Y 1 B GLU 240 ? CD  ? B GLU 240 CD  
144 1 Y 1 B GLU 240 ? OE1 ? B GLU 240 OE1 
145 1 Y 1 B GLU 240 ? OE2 ? B GLU 240 OE2 
146 1 Y 1 B LYS 243 ? CG  ? B LYS 243 CG  
147 1 Y 1 B LYS 243 ? CD  ? B LYS 243 CD  
148 1 Y 1 B LYS 243 ? CE  ? B LYS 243 CE  
149 1 Y 1 B LYS 243 ? NZ  ? B LYS 243 NZ  
150 1 Y 1 B LYS 260 ? CG  ? B LYS 260 CG  
151 1 Y 1 B LYS 260 ? CD  ? B LYS 260 CD  
152 1 Y 1 B LYS 260 ? CE  ? B LYS 260 CE  
153 1 Y 1 B LYS 260 ? NZ  ? B LYS 260 NZ  
154 1 Y 1 B GLU 262 ? CG  ? B GLU 262 CG  
155 1 Y 1 B GLU 262 ? CD  ? B GLU 262 CD  
156 1 Y 1 B GLU 262 ? OE1 ? B GLU 262 OE1 
157 1 Y 1 B GLU 262 ? OE2 ? B GLU 262 OE2 
158 1 Y 1 B LYS 345 ? CE  ? B LYS 345 CE  
159 1 Y 1 B LYS 345 ? NZ  ? B LYS 345 NZ  
160 1 Y 1 B LYS 350 ? CG  ? B LYS 350 CG  
161 1 Y 1 B LYS 350 ? CD  ? B LYS 350 CD  
162 1 Y 1 B LYS 350 ? CE  ? B LYS 350 CE  
163 1 Y 1 B LYS 350 ? NZ  ? B LYS 350 NZ  
164 1 Y 1 B LYS 381 ? CD  ? B LYS 381 CD  
165 1 Y 1 B LYS 381 ? CE  ? B LYS 381 CE  
166 1 Y 1 B LYS 381 ? NZ  ? B LYS 381 NZ  
167 1 Y 1 B GLN 387 ? CG  ? B GLN 387 CG  
168 1 Y 1 B GLN 387 ? CD  ? B GLN 387 CD  
169 1 Y 1 B GLN 387 ? OE1 ? B GLN 387 OE1 
170 1 Y 1 B GLN 387 ? NE2 ? B GLN 387 NE2 
171 1 Y 1 B LYS 406 ? CG  ? B LYS 406 CG  
172 1 Y 1 B LYS 406 ? CD  ? B LYS 406 CD  
173 1 Y 1 B LYS 406 ? CE  ? B LYS 406 CE  
174 1 Y 1 B LYS 406 ? NZ  ? B LYS 406 NZ  
175 1 Y 1 B ALA 412 ? O   ? B ALA 412 O   
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER ? ? ? 2.9.7 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .     2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .     3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .     4 
# 
_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                     9B81 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     82.790 
_cell.length_a_esd                 ? 
_cell.length_b                     82.790 
_cell.length_b_esd                 ? 
_cell.length_c                     302.160 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9B81 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9B81 
_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             2.69 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.34 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Sodium Cacodylate, pH6.5, 0.2M NaCl, 2M Ammonium Sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-03-23 
_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   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9B81 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.56 
_reflns.d_resolution_low                               302 
_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                                     35021 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          24.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.076 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.56 
_reflns_shell.d_res_low                                     2.70 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             67305 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_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                                  0.573 
_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]                            1.9542 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            1.9542 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -3.9083 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               55.43 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.9351 
_refine.correlation_coeff_Fo_to_Fc_free          0.9189 
_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                                 9B81 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.56 
_refine.ls_d_res_low                             35.06 
_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                     35021 
_refine.ls_number_reflns_R_free                  1758 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2029 
_refine.ls_R_factor_R_free                       0.2331 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.251 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.250 
_refine.pdbx_overall_SU_R_Blow_DPI               0.413 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.405 
_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_analyze.entry_id                        9B81 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.321 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.56 
_refine_hist.d_res_low                        35.06 
_refine_hist.number_atoms_solvent             47 
_refine_hist.number_atoms_total               6244 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        6025 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         172 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010 ? 6336 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.24  ? 8610 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2168 ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 164  ? t_trig_c_planes           8.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 935  ? t_gen_planes              8.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 6336 ? t_it                      20.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 2.18  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 19.48 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 848  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 7050 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.56 
_refine_ls_shell.d_res_low                        2.63 
_refine_ls_shell.number_reflns_all                2797 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             135 
_refine_ls_shell.number_reflns_R_work             2662 
_refine_ls_shell.percent_reflns_obs               99.99 
_refine_ls_shell.percent_reflns_R_free            4.83 
_refine_ls_shell.R_factor_all                     0.2218 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2185 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   18 
_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                  0.2898 
# 
_struct.entry_id                     9B81 
_struct.title                        'Crystal structure of wild type IDH1 bound to compound 4' 
_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        9B81 
_struct_keywords.text            OXIDOREDUCTASE 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    IDHC_HUMAN 
_struct_ref.pdbx_db_accession          O75874 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDE
KRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSD
GTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFE
AQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQ
KGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDK
LGENLKIKLAQAKL
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9B81 A 1 ? 414 ? O75874 1 ? 414 ? 1 414 
2 1 9B81 B 1 ? 414 ? O75874 1 ? 414 ? 1 414 
# 
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 9B81 HIS A 132 ? UNP O75874 ARG 132 variant          132 1  
1 9B81 LEU A 415 ? UNP O75874 ?   ?   'expression tag' 415 2  
1 9B81 GLU A 416 ? UNP O75874 ?   ?   'expression tag' 416 3  
1 9B81 HIS A 417 ? UNP O75874 ?   ?   'expression tag' 417 4  
1 9B81 HIS A 418 ? UNP O75874 ?   ?   'expression tag' 418 5  
1 9B81 HIS A 419 ? UNP O75874 ?   ?   'expression tag' 419 6  
1 9B81 HIS A 420 ? UNP O75874 ?   ?   'expression tag' 420 7  
1 9B81 HIS A 421 ? UNP O75874 ?   ?   'expression tag' 421 8  
1 9B81 HIS A 422 ? UNP O75874 ?   ?   'expression tag' 422 9  
1 9B81 HIS A 423 ? UNP O75874 ?   ?   'expression tag' 423 10 
1 9B81 HIS A 424 ? UNP O75874 ?   ?   'expression tag' 424 11 
2 9B81 HIS B 132 ? UNP O75874 ARG 132 variant          132 12 
2 9B81 LEU B 415 ? UNP O75874 ?   ?   'expression tag' 415 13 
2 9B81 GLU B 416 ? UNP O75874 ?   ?   'expression tag' 416 14 
2 9B81 HIS B 417 ? UNP O75874 ?   ?   'expression tag' 417 15 
2 9B81 HIS B 418 ? UNP O75874 ?   ?   'expression tag' 418 16 
2 9B81 HIS B 419 ? UNP O75874 ?   ?   'expression tag' 419 17 
2 9B81 HIS B 420 ? UNP O75874 ?   ?   'expression tag' 420 18 
2 9B81 HIS B 421 ? UNP O75874 ?   ?   'expression tag' 421 19 
2 9B81 HIS B 422 ? UNP O75874 ?   ?   'expression tag' 422 20 
2 9B81 HIS B 423 ? UNP O75874 ?   ?   'expression tag' 423 21 
2 9B81 HIS B 424 ? UNP O75874 ?   ?   'expression tag' 424 22 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6220  ? 
1 MORE         -41   ? 
1 'SSA (A^2)'  33720 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_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 ASP A 16  ? LEU A 30  ? ASP A 16  LEU A 30  1 ? 15 
HELX_P HELX_P2  AA2 GLY A 45  ? THR A 52  ? GLY A 45  THR A 52  1 ? 8  
HELX_P HELX_P3  AA3 ASP A 54  ? ASN A 68  ? ASP A 54  ASN A 68  1 ? 15 
HELX_P HELX_P4  AA4 ASP A 79  ? LYS A 87  ? ASP A 79  LYS A 87  1 ? 9  
HELX_P HELX_P5  AA5 SER A 94  ? GLY A 104 ? SER A 94  GLY A 104 1 ? 11 
HELX_P HELX_P6  AA6 ASP A 186 ? GLY A 204 ? ASP A 186 GLY A 204 1 ? 19 
HELX_P HELX_P7  AA7 LYS A 218 ? TYR A 235 ? LYS A 218 TYR A 235 1 ? 18 
HELX_P HELX_P8  AA8 TYR A 235 ? ALA A 241 ? TYR A 235 ALA A 241 1 ? 7  
HELX_P HELX_P9  AA9 ILE A 251 ? LYS A 260 ? ILE A 251 LYS A 260 1 ? 10 
HELX_P HELX_P10 AB1 SER A 287 ? GLY A 289 ? SER A 287 GLY A 289 5 ? 3  
HELX_P HELX_P11 AB2 VAL A 312 ? LYS A 321 ? VAL A 312 LYS A 321 1 ? 10 
HELX_P HELX_P12 AB3 PRO A 329 ? ASP A 347 ? PRO A 329 ASP A 347 1 ? 19 
HELX_P HELX_P13 AB4 ASN A 349 ? ALA A 369 ? ASN A 349 ALA A 369 1 ? 21 
HELX_P HELX_P14 AB5 THR A 373 ? GLY A 382 ? THR A 373 GLY A 382 1 ? 10 
HELX_P HELX_P15 AB6 LEU A 383 ? VAL A 386 ? LEU A 383 VAL A 386 5 ? 4  
HELX_P HELX_P16 AB7 GLN A 387 ? TYR A 391 ? GLN A 387 TYR A 391 5 ? 5  
HELX_P HELX_P17 AB8 ASN A 393 ? LYS A 413 ? ASN A 393 LYS A 413 1 ? 21 
HELX_P HELX_P18 AB9 ASP B 16  ? LEU B 30  ? ASP B 16  LEU B 30  1 ? 15 
HELX_P HELX_P19 AC1 GLY B 45  ? THR B 52  ? GLY B 45  THR B 52  1 ? 8  
HELX_P HELX_P20 AC2 ASP B 54  ? ASN B 68  ? ASP B 54  ASN B 68  1 ? 15 
HELX_P HELX_P21 AC3 ASP B 79  ? LYS B 87  ? ASP B 79  LYS B 87  1 ? 9  
HELX_P HELX_P22 AC4 SER B 94  ? GLY B 104 ? SER B 94  GLY B 104 1 ? 11 
HELX_P HELX_P23 AC5 ASP B 186 ? GLY B 204 ? ASP B 186 GLY B 204 1 ? 19 
HELX_P HELX_P24 AC6 LEU B 216 ? TYR B 235 ? LEU B 216 TYR B 235 1 ? 20 
HELX_P HELX_P25 AC7 TYR B 235 ? ALA B 241 ? TYR B 235 ALA B 241 1 ? 7  
HELX_P HELX_P26 AC8 ILE B 251 ? SER B 261 ? ILE B 251 SER B 261 1 ? 11 
HELX_P HELX_P27 AC9 VAL B 312 ? LYS B 321 ? VAL B 312 LYS B 321 1 ? 10 
HELX_P HELX_P28 AD1 PRO B 329 ? ASN B 348 ? PRO B 329 ASN B 348 1 ? 20 
HELX_P HELX_P29 AD2 ASN B 349 ? ALA B 369 ? ASN B 349 ALA B 369 1 ? 21 
HELX_P HELX_P30 AD3 THR B 373 ? GLY B 382 ? THR B 373 GLY B 382 1 ? 10 
HELX_P HELX_P31 AD4 LEU B 383 ? VAL B 386 ? LEU B 383 VAL B 386 5 ? 4  
HELX_P HELX_P32 AD5 GLN B 387 ? TYR B 391 ? GLN B 387 TYR B 391 5 ? 5  
HELX_P HELX_P33 AD6 ASN B 393 ? GLN B 411 ? ASN B 393 GLN B 411 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 10 ? 
AA2 ? 4  ? 
AA3 ? 4  ? 
AA4 ? 10 ? 
# 
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  ? anti-parallel 
AA1 5 6  ? anti-parallel 
AA1 6 7  ? anti-parallel 
AA1 7 8  ? parallel      
AA1 8 9  ? parallel      
AA1 9 10 ? parallel      
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA4 1 2  ? parallel      
AA4 2 3  ? parallel      
AA4 3 4  ? parallel      
AA4 4 5  ? anti-parallel 
AA4 5 6  ? anti-parallel 
AA4 6 7  ? anti-parallel 
AA4 7 8  ? parallel      
AA4 8 9  ? parallel      
AA4 9 10 ? 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  VAL A 35  ? ASP A 43  ? VAL A 35  ASP A 43  
AA1 2  ILE A 5   ? GLN A 14  ? ILE A 5   GLN A 14  
AA1 3  VAL A 69  ? LYS A 72  ? VAL A 69  LYS A 72  
AA1 4  VAL A 303 ? ALA A 307 ? VAL A 303 ALA A 307 
AA1 5  MET A 291 ? VAL A 296 ? MET A 291 VAL A 296 
AA1 6  THR A 106 ? ALA A 111 ? THR A 106 ALA A 111 
AA1 7  LYS A 126 ? HIS A 132 ? LYS A 126 HIS A 132 
AA1 8  GLY A 263 ? CYS A 269 ? GLY A 263 CYS A 269 
AA1 9  LEU A 207 ? THR A 211 ? LEU A 207 THR A 211 
AA1 10 TYR A 246 ? LEU A 250 ? TYR A 246 LEU A 250 
AA2 1  ALA A 141 ? VAL A 146 ? ALA A 141 VAL A 146 
AA2 2  GLY A 177 ? GLN A 185 ? GLY A 177 GLN A 185 
AA2 3  GLY B 177 ? GLN B 185 ? GLY B 177 GLN B 185 
AA2 4  ALA B 141 ? VAL B 146 ? ALA B 141 VAL B 146 
AA3 1  VAL A 165 ? PHE A 172 ? VAL A 165 PHE A 172 
AA3 2  GLY A 150 ? PRO A 158 ? GLY A 150 PRO A 158 
AA3 3  GLY B 150 ? PRO B 158 ? GLY B 150 PRO B 158 
AA3 4  VAL B 165 ? PHE B 172 ? VAL B 165 PHE B 172 
AA4 1  VAL B 35  ? ASP B 43  ? VAL B 35  ASP B 43  
AA4 2  ILE B 5   ? GLN B 14  ? ILE B 5   GLN B 14  
AA4 3  VAL B 69  ? LYS B 72  ? VAL B 69  LYS B 72  
AA4 4  VAL B 303 ? ALA B 307 ? VAL B 303 ALA B 307 
AA4 5  MET B 291 ? VAL B 296 ? MET B 291 VAL B 296 
AA4 6  THR B 106 ? ALA B 111 ? THR B 106 ALA B 111 
AA4 7  LYS B 126 ? HIS B 132 ? LYS B 126 HIS B 132 
AA4 8  GLY B 263 ? CYS B 269 ? GLY B 263 CYS B 269 
AA4 9  LEU B 207 ? THR B 211 ? LEU B 207 THR B 211 
AA4 10 TYR B 246 ? LEU B 250 ? TYR B 246 LEU B 250 
# 
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  O GLU A 36  ? O GLU A 36  N ILE A 5   ? N ILE A 5   
AA1 2 3  N VAL A 11  ? N VAL A 11  O VAL A 71  ? O VAL A 71  
AA1 3 4  N LYS A 72  ? N LYS A 72  O ALA A 305 ? O ALA A 305 
AA1 4 5  O GLU A 306 ? O GLU A 306 N SER A 293 ? N SER A 293 
AA1 5 6  O THR A 292 ? O THR A 292 N GLU A 110 ? N GLU A 110 
AA1 6 7  N ARG A 109 ? N ARG A 109 O ILE A 130 ? O ILE A 130 
AA1 7 8  N GLY A 131 ? N GLY A 131 O CYS A 269 ? O CYS A 269 
AA1 8 9  O ALA A 268 ? O ALA A 268 N TYR A 208 ? N TYR A 208 
AA1 9 10 N LEU A 209 ? N LEU A 209 O ARG A 249 ? O ARG A 249 
AA2 1 2  N PHE A 144 ? N PHE A 144 O ALA A 179 ? O ALA A 179 
AA2 2 3  N MET A 180 ? N MET A 180 O MET B 182 ? O MET B 182 
AA2 3 4  O GLY B 181 ? O GLY B 181 N THR B 142 ? N THR B 142 
AA3 1 2  O TYR A 167 ? O TYR A 167 N ILE A 154 ? N ILE A 154 
AA3 2 3  N GLU A 153 ? N GLU A 153 O THR B 155 ? O THR B 155 
AA3 3 4  N VAL B 152 ? N VAL B 152 O VAL B 169 ? O VAL B 169 
AA4 1 2  O TYR B 42  ? O TYR B 42  N GLN B 14  ? N GLN B 14  
AA4 2 3  N VAL B 11  ? N VAL B 11  O VAL B 71  ? O VAL B 71  
AA4 3 4  N LYS B 72  ? N LYS B 72  O ALA B 305 ? O ALA B 305 
AA4 4 5  O GLU B 304 ? O GLU B 304 N LEU B 295 ? N LEU B 295 
AA4 5 6  O VAL B 296 ? O VAL B 296 N THR B 106 ? N THR B 106 
AA4 6 7  N ARG B 109 ? N ARG B 109 O ILE B 130 ? O ILE B 130 
AA4 7 8  N ILE B 129 ? N ILE B 129 O TRP B 267 ? O TRP B 267 
AA4 8 9  O ILE B 266 ? O ILE B 266 N TYR B 208 ? N TYR B 208 
AA4 9 10 N LEU B 209 ? N LEU B 209 O ARG B 249 ? O ARG B 249 
# 
_pdbx_entry_details.entry_id                   9B81 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 17  ? ? 56.37   -128.89 
2  1 ILE A 31  ? ? -93.17  -63.30  
3  1 ASN A 68  ? ? 68.86   -20.19  
4  1 SER A 94  ? ? -38.83  122.97  
5  1 TRP A 124 ? ? -68.64  81.69   
6  1 LEU A 216 ? ? -101.29 63.54   
7  1 ALA A 308 ? ? -90.20  59.68   
8  1 GLU B 17  ? ? 46.74   -132.25 
9  1 ILE B 31  ? ? -99.72  -64.20  
10 1 ASN B 68  ? ? 69.39   -12.01  
11 1 ILE B 215 ? ? -85.16  -86.71  
12 1 GLN B 234 ? ? -161.17 10.26   
13 1 TYR B 235 ? ? -133.68 -33.81  
14 1 GLN B 242 ? ? -145.53 10.94   
15 1 LEU B 288 ? ? 63.78   -44.60  
16 1 ALA B 308 ? ? -93.28  55.35   
17 1 ILE B 380 ? ? -70.12  -74.43  
18 1 ARG B 388 ? ? -38.07  -39.13  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A SER 2   ? A SER 2   
3  1 Y 1 A ALA 134 ? A ALA 134 
4  1 Y 1 A TYR 135 ? A TYR 135 
5  1 Y 1 A GLY 136 ? A GLY 136 
6  1 Y 1 A ASP 137 ? A ASP 137 
7  1 Y 1 A GLN 138 ? A GLN 138 
8  1 Y 1 A TYR 139 ? A TYR 139 
9  1 Y 1 A TYR 272 ? A TYR 272 
10 1 Y 1 A ASP 273 ? A ASP 273 
11 1 Y 1 A GLY 274 ? A GLY 274 
12 1 Y 1 A ASP 275 ? A ASP 275 
13 1 Y 1 A VAL 276 ? A VAL 276 
14 1 Y 1 A GLN 277 ? A GLN 277 
15 1 Y 1 A SER 278 ? A SER 278 
16 1 Y 1 A ASP 279 ? A ASP 279 
17 1 Y 1 A SER 280 ? A SER 280 
18 1 Y 1 A VAL 281 ? A VAL 281 
19 1 Y 1 A ALA 282 ? A ALA 282 
20 1 Y 1 A GLN 283 ? A GLN 283 
21 1 Y 1 A GLY 284 ? A GLY 284 
22 1 Y 1 A TYR 285 ? A TYR 285 
23 1 Y 1 A GLY 286 ? A GLY 286 
24 1 Y 1 A LEU 415 ? A LEU 415 
25 1 Y 1 A GLU 416 ? A GLU 416 
26 1 Y 1 A HIS 417 ? A HIS 417 
27 1 Y 1 A HIS 418 ? A HIS 418 
28 1 Y 1 A HIS 419 ? A HIS 419 
29 1 Y 1 A HIS 420 ? A HIS 420 
30 1 Y 1 A HIS 421 ? A HIS 421 
31 1 Y 1 A HIS 422 ? A HIS 422 
32 1 Y 1 A HIS 423 ? A HIS 423 
33 1 Y 1 A HIS 424 ? A HIS 424 
34 1 Y 1 B MET 1   ? B MET 1   
35 1 Y 1 B SER 2   ? B SER 2   
36 1 Y 1 B TYR 135 ? B TYR 135 
37 1 Y 1 B GLY 136 ? B GLY 136 
38 1 Y 1 B ASP 137 ? B ASP 137 
39 1 Y 1 B GLN 138 ? B GLN 138 
40 1 Y 1 B TYR 139 ? B TYR 139 
41 1 Y 1 B TYR 272 ? B TYR 272 
42 1 Y 1 B ASP 273 ? B ASP 273 
43 1 Y 1 B GLY 274 ? B GLY 274 
44 1 Y 1 B ASP 275 ? B ASP 275 
45 1 Y 1 B VAL 276 ? B VAL 276 
46 1 Y 1 B GLN 277 ? B GLN 277 
47 1 Y 1 B SER 278 ? B SER 278 
48 1 Y 1 B ASP 279 ? B ASP 279 
49 1 Y 1 B SER 280 ? B SER 280 
50 1 Y 1 B VAL 281 ? B VAL 281 
51 1 Y 1 B ALA 282 ? B ALA 282 
52 1 Y 1 B GLN 283 ? B GLN 283 
53 1 Y 1 B GLY 284 ? B GLY 284 
54 1 Y 1 B TYR 285 ? B TYR 285 
55 1 Y 1 B GLY 286 ? B GLY 286 
56 1 Y 1 B LYS 413 ? B LYS 413 
57 1 Y 1 B LEU 414 ? B LEU 414 
58 1 Y 1 B LEU 415 ? B LEU 415 
59 1 Y 1 B GLU 416 ? B GLU 416 
60 1 Y 1 B HIS 417 ? B HIS 417 
61 1 Y 1 B HIS 418 ? B HIS 418 
62 1 Y 1 B HIS 419 ? B HIS 419 
63 1 Y 1 B HIS 420 ? B HIS 420 
64 1 Y 1 B HIS 421 ? B HIS 421 
65 1 Y 1 B HIS 422 ? B HIS 422 
66 1 Y 1 B HIS 423 ? B HIS 423 
67 1 Y 1 B HIS 424 ? B HIS 424 
# 
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 
A1AI4 C32  C N N 1   
A1AI4 C14  C Y N 2   
A1AI4 C18  C Y N 3   
A1AI4 C22  C Y N 4   
A1AI4 C15  C Y N 5   
A1AI4 C19  C Y N 6   
A1AI4 C21  C Y N 7   
A1AI4 C2   C Y N 8   
A1AI4 C3   C Y N 9   
A1AI4 C6   C Y N 10  
A1AI4 C13  C Y N 11  
A1AI4 C17  C Y N 12  
A1AI4 C9   C Y N 13  
A1AI4 C20  C Y N 14  
A1AI4 C1   C Y N 15  
A1AI4 C4   C Y N 16  
A1AI4 C5   C Y N 17  
A1AI4 C10  C Y N 18  
A1AI4 C16  C N N 19  
A1AI4 C8   C N N 20  
A1AI4 C34  C N N 21  
A1AI4 C35  C N N 22  
A1AI4 C24  C N N 23  
A1AI4 C31  C N N 24  
A1AI4 C23  C N S 25  
A1AI4 C26  C N N 26  
A1AI4 N33  N N N 27  
A1AI4 N12  N Y N 28  
A1AI4 N11  N N N 29  
A1AI4 N7   N N N 30  
A1AI4 O30  O N N 31  
A1AI4 O25  O N N 32  
A1AI4 F27  F N N 33  
A1AI4 F28  F N N 34  
A1AI4 F29  F N N 35  
A1AI4 H1   H N N 36  
A1AI4 H2   H N N 37  
A1AI4 H3   H N N 38  
A1AI4 H4   H N N 39  
A1AI4 H5   H N N 40  
A1AI4 H6   H N N 41  
A1AI4 H7   H N N 42  
A1AI4 H8   H N N 43  
A1AI4 H9   H N N 44  
A1AI4 H10  H N N 45  
A1AI4 H11  H N N 46  
A1AI4 H12  H N N 47  
A1AI4 H13  H N N 48  
A1AI4 H14  H N N 49  
A1AI4 H15  H N N 50  
A1AI4 H16  H N N 51  
A1AI4 H17  H N N 52  
A1AI4 H18  H N N 53  
A1AI4 H19  H N N 54  
A1AI4 H20  H N N 55  
A1AI4 H21  H N N 56  
A1AI4 H22  H N N 57  
A1AI4 H23  H N N 58  
ALA   N    N N N 59  
ALA   CA   C N S 60  
ALA   C    C N N 61  
ALA   O    O N N 62  
ALA   CB   C N N 63  
ALA   OXT  O N N 64  
ALA   H    H N N 65  
ALA   H2   H N N 66  
ALA   HA   H N N 67  
ALA   HB1  H N N 68  
ALA   HB2  H N N 69  
ALA   HB3  H N N 70  
ALA   HXT  H N N 71  
ARG   N    N N N 72  
ARG   CA   C N S 73  
ARG   C    C N N 74  
ARG   O    O N N 75  
ARG   CB   C N N 76  
ARG   CG   C N N 77  
ARG   CD   C N N 78  
ARG   NE   N N N 79  
ARG   CZ   C N N 80  
ARG   NH1  N N N 81  
ARG   NH2  N N N 82  
ARG   OXT  O N N 83  
ARG   H    H N N 84  
ARG   H2   H N N 85  
ARG   HA   H N N 86  
ARG   HB2  H N N 87  
ARG   HB3  H N N 88  
ARG   HG2  H N N 89  
ARG   HG3  H N N 90  
ARG   HD2  H N N 91  
ARG   HD3  H N N 92  
ARG   HE   H N N 93  
ARG   HH11 H N N 94  
ARG   HH12 H N N 95  
ARG   HH21 H N N 96  
ARG   HH22 H N N 97  
ARG   HXT  H N N 98  
ASN   N    N N N 99  
ASN   CA   C N S 100 
ASN   C    C N N 101 
ASN   O    O N N 102 
ASN   CB   C N N 103 
ASN   CG   C N N 104 
ASN   OD1  O N N 105 
ASN   ND2  N N N 106 
ASN   OXT  O N N 107 
ASN   H    H N N 108 
ASN   H2   H N N 109 
ASN   HA   H N N 110 
ASN   HB2  H N N 111 
ASN   HB3  H N N 112 
ASN   HD21 H N N 113 
ASN   HD22 H N N 114 
ASN   HXT  H N N 115 
ASP   N    N N N 116 
ASP   CA   C N S 117 
ASP   C    C N N 118 
ASP   O    O N N 119 
ASP   CB   C N N 120 
ASP   CG   C N N 121 
ASP   OD1  O N N 122 
ASP   OD2  O N N 123 
ASP   OXT  O N N 124 
ASP   H    H N N 125 
ASP   H2   H N N 126 
ASP   HA   H N N 127 
ASP   HB2  H N N 128 
ASP   HB3  H N N 129 
ASP   HD2  H N N 130 
ASP   HXT  H N N 131 
CYS   N    N N N 132 
CYS   CA   C N R 133 
CYS   C    C N N 134 
CYS   O    O N N 135 
CYS   CB   C N N 136 
CYS   SG   S N N 137 
CYS   OXT  O N N 138 
CYS   H    H N N 139 
CYS   H2   H N N 140 
CYS   HA   H N N 141 
CYS   HB2  H N N 142 
CYS   HB3  H N N 143 
CYS   HG   H N N 144 
CYS   HXT  H N N 145 
GLN   N    N N N 146 
GLN   CA   C N S 147 
GLN   C    C N N 148 
GLN   O    O N N 149 
GLN   CB   C N N 150 
GLN   CG   C N N 151 
GLN   CD   C N N 152 
GLN   OE1  O N N 153 
GLN   NE2  N N N 154 
GLN   OXT  O N N 155 
GLN   H    H N N 156 
GLN   H2   H N N 157 
GLN   HA   H N N 158 
GLN   HB2  H N N 159 
GLN   HB3  H N N 160 
GLN   HG2  H N N 161 
GLN   HG3  H N N 162 
GLN   HE21 H N N 163 
GLN   HE22 H N N 164 
GLN   HXT  H N N 165 
GLU   N    N N N 166 
GLU   CA   C N S 167 
GLU   C    C N N 168 
GLU   O    O N N 169 
GLU   CB   C N N 170 
GLU   CG   C N N 171 
GLU   CD   C N N 172 
GLU   OE1  O N N 173 
GLU   OE2  O N N 174 
GLU   OXT  O N N 175 
GLU   H    H N N 176 
GLU   H2   H N N 177 
GLU   HA   H N N 178 
GLU   HB2  H N N 179 
GLU   HB3  H N N 180 
GLU   HG2  H N N 181 
GLU   HG3  H N N 182 
GLU   HE2  H N N 183 
GLU   HXT  H N N 184 
GLY   N    N N N 185 
GLY   CA   C N N 186 
GLY   C    C N N 187 
GLY   O    O N N 188 
GLY   OXT  O N N 189 
GLY   H    H N N 190 
GLY   H2   H N N 191 
GLY   HA2  H N N 192 
GLY   HA3  H N N 193 
GLY   HXT  H N N 194 
GOL   C1   C N N 195 
GOL   O1   O N N 196 
GOL   C2   C N N 197 
GOL   O2   O N N 198 
GOL   C3   C N N 199 
GOL   O3   O N N 200 
GOL   H11  H N N 201 
GOL   H12  H N N 202 
GOL   HO1  H N N 203 
GOL   H2   H N N 204 
GOL   HO2  H N N 205 
GOL   H31  H N N 206 
GOL   H32  H N N 207 
GOL   HO3  H N N 208 
HIS   N    N N N 209 
HIS   CA   C N S 210 
HIS   C    C N N 211 
HIS   O    O N N 212 
HIS   CB   C N N 213 
HIS   CG   C Y N 214 
HIS   ND1  N Y N 215 
HIS   CD2  C Y N 216 
HIS   CE1  C Y N 217 
HIS   NE2  N Y N 218 
HIS   OXT  O N N 219 
HIS   H    H N N 220 
HIS   H2   H N N 221 
HIS   HA   H N N 222 
HIS   HB2  H N N 223 
HIS   HB3  H N N 224 
HIS   HD1  H N N 225 
HIS   HD2  H N N 226 
HIS   HE1  H N N 227 
HIS   HE2  H N N 228 
HIS   HXT  H N N 229 
HOH   O    O N N 230 
HOH   H1   H N N 231 
HOH   H2   H N N 232 
ILE   N    N N N 233 
ILE   CA   C N S 234 
ILE   C    C N N 235 
ILE   O    O N N 236 
ILE   CB   C N S 237 
ILE   CG1  C N N 238 
ILE   CG2  C N N 239 
ILE   CD1  C N N 240 
ILE   OXT  O N N 241 
ILE   H    H N N 242 
ILE   H2   H N N 243 
ILE   HA   H N N 244 
ILE   HB   H N N 245 
ILE   HG12 H N N 246 
ILE   HG13 H N N 247 
ILE   HG21 H N N 248 
ILE   HG22 H N N 249 
ILE   HG23 H N N 250 
ILE   HD11 H N N 251 
ILE   HD12 H N N 252 
ILE   HD13 H N N 253 
ILE   HXT  H N N 254 
LEU   N    N N N 255 
LEU   CA   C N S 256 
LEU   C    C N N 257 
LEU   O    O N N 258 
LEU   CB   C N N 259 
LEU   CG   C N N 260 
LEU   CD1  C N N 261 
LEU   CD2  C N N 262 
LEU   OXT  O N N 263 
LEU   H    H N N 264 
LEU   H2   H N N 265 
LEU   HA   H N N 266 
LEU   HB2  H N N 267 
LEU   HB3  H N N 268 
LEU   HG   H N N 269 
LEU   HD11 H N N 270 
LEU   HD12 H N N 271 
LEU   HD13 H N N 272 
LEU   HD21 H N N 273 
LEU   HD22 H N N 274 
LEU   HD23 H N N 275 
LEU   HXT  H N N 276 
LYS   N    N N N 277 
LYS   CA   C N S 278 
LYS   C    C N N 279 
LYS   O    O N N 280 
LYS   CB   C N N 281 
LYS   CG   C N N 282 
LYS   CD   C N N 283 
LYS   CE   C N N 284 
LYS   NZ   N N N 285 
LYS   OXT  O N N 286 
LYS   H    H N N 287 
LYS   H2   H N N 288 
LYS   HA   H N N 289 
LYS   HB2  H N N 290 
LYS   HB3  H N N 291 
LYS   HG2  H N N 292 
LYS   HG3  H N N 293 
LYS   HD2  H N N 294 
LYS   HD3  H N N 295 
LYS   HE2  H N N 296 
LYS   HE3  H N N 297 
LYS   HZ1  H N N 298 
LYS   HZ2  H N N 299 
LYS   HZ3  H N N 300 
LYS   HXT  H N N 301 
MET   N    N N N 302 
MET   CA   C N S 303 
MET   C    C N N 304 
MET   O    O N N 305 
MET   CB   C N N 306 
MET   CG   C N N 307 
MET   SD   S N N 308 
MET   CE   C N N 309 
MET   OXT  O N N 310 
MET   H    H N N 311 
MET   H2   H N N 312 
MET   HA   H N N 313 
MET   HB2  H N N 314 
MET   HB3  H N N 315 
MET   HG2  H N N 316 
MET   HG3  H N N 317 
MET   HE1  H N N 318 
MET   HE2  H N N 319 
MET   HE3  H N N 320 
MET   HXT  H N N 321 
NAP   PA   P N R 322 
NAP   O1A  O N N 323 
NAP   O2A  O N N 324 
NAP   O5B  O N N 325 
NAP   C5B  C N N 326 
NAP   C4B  C N R 327 
NAP   O4B  O N N 328 
NAP   C3B  C N R 329 
NAP   O3B  O N N 330 
NAP   C2B  C N R 331 
NAP   O2B  O N N 332 
NAP   C1B  C N R 333 
NAP   N9A  N Y N 334 
NAP   C8A  C Y N 335 
NAP   N7A  N Y N 336 
NAP   C5A  C Y N 337 
NAP   C6A  C Y N 338 
NAP   N6A  N N N 339 
NAP   N1A  N Y N 340 
NAP   C2A  C Y N 341 
NAP   N3A  N Y N 342 
NAP   C4A  C Y N 343 
NAP   O3   O N N 344 
NAP   PN   P N N 345 
NAP   O1N  O N N 346 
NAP   O2N  O N N 347 
NAP   O5D  O N N 348 
NAP   C5D  C N N 349 
NAP   C4D  C N R 350 
NAP   O4D  O N N 351 
NAP   C3D  C N S 352 
NAP   O3D  O N N 353 
NAP   C2D  C N R 354 
NAP   O2D  O N N 355 
NAP   C1D  C N R 356 
NAP   N1N  N Y N 357 
NAP   C2N  C Y N 358 
NAP   C3N  C Y N 359 
NAP   C7N  C N N 360 
NAP   O7N  O N N 361 
NAP   N7N  N N N 362 
NAP   C4N  C Y N 363 
NAP   C5N  C Y N 364 
NAP   C6N  C Y N 365 
NAP   P2B  P N N 366 
NAP   O1X  O N N 367 
NAP   O2X  O N N 368 
NAP   O3X  O N N 369 
NAP   HOA2 H N N 370 
NAP   H51A H N N 371 
NAP   H52A H N N 372 
NAP   H4B  H N N 373 
NAP   H3B  H N N 374 
NAP   HO3A H N N 375 
NAP   H2B  H N N 376 
NAP   H1B  H N N 377 
NAP   H8A  H N N 378 
NAP   H61A H N N 379 
NAP   H62A H N N 380 
NAP   H2A  H N N 381 
NAP   H51N H N N 382 
NAP   H52N H N N 383 
NAP   H4D  H N N 384 
NAP   H3D  H N N 385 
NAP   HO3N H N N 386 
NAP   H2D  H N N 387 
NAP   HO2N H N N 388 
NAP   H1D  H N N 389 
NAP   H2N  H N N 390 
NAP   H71N H N N 391 
NAP   H72N H N N 392 
NAP   H4N  H N N 393 
NAP   H5N  H N N 394 
NAP   H6N  H N N 395 
NAP   HOP2 H N N 396 
NAP   HOP3 H N N 397 
PHE   N    N N N 398 
PHE   CA   C N S 399 
PHE   C    C N N 400 
PHE   O    O N N 401 
PHE   CB   C N N 402 
PHE   CG   C Y N 403 
PHE   CD1  C Y N 404 
PHE   CD2  C Y N 405 
PHE   CE1  C Y N 406 
PHE   CE2  C Y N 407 
PHE   CZ   C Y N 408 
PHE   OXT  O N N 409 
PHE   H    H N N 410 
PHE   H2   H N N 411 
PHE   HA   H N N 412 
PHE   HB2  H N N 413 
PHE   HB3  H N N 414 
PHE   HD1  H N N 415 
PHE   HD2  H N N 416 
PHE   HE1  H N N 417 
PHE   HE2  H N N 418 
PHE   HZ   H N N 419 
PHE   HXT  H N N 420 
PRO   N    N N N 421 
PRO   CA   C N S 422 
PRO   C    C N N 423 
PRO   O    O N N 424 
PRO   CB   C N N 425 
PRO   CG   C N N 426 
PRO   CD   C N N 427 
PRO   OXT  O N N 428 
PRO   H    H N N 429 
PRO   HA   H N N 430 
PRO   HB2  H N N 431 
PRO   HB3  H N N 432 
PRO   HG2  H N N 433 
PRO   HG3  H N N 434 
PRO   HD2  H N N 435 
PRO   HD3  H N N 436 
PRO   HXT  H N N 437 
SER   N    N N N 438 
SER   CA   C N S 439 
SER   C    C N N 440 
SER   O    O N N 441 
SER   CB   C N N 442 
SER   OG   O N N 443 
SER   OXT  O N N 444 
SER   H    H N N 445 
SER   H2   H N N 446 
SER   HA   H N N 447 
SER   HB2  H N N 448 
SER   HB3  H N N 449 
SER   HG   H N N 450 
SER   HXT  H N N 451 
THR   N    N N N 452 
THR   CA   C N S 453 
THR   C    C N N 454 
THR   O    O N N 455 
THR   CB   C N R 456 
THR   OG1  O N N 457 
THR   CG2  C N N 458 
THR   OXT  O N N 459 
THR   H    H N N 460 
THR   H2   H N N 461 
THR   HA   H N N 462 
THR   HB   H N N 463 
THR   HG1  H N N 464 
THR   HG21 H N N 465 
THR   HG22 H N N 466 
THR   HG23 H N N 467 
THR   HXT  H N N 468 
TRP   N    N N N 469 
TRP   CA   C N S 470 
TRP   C    C N N 471 
TRP   O    O N N 472 
TRP   CB   C N N 473 
TRP   CG   C Y N 474 
TRP   CD1  C Y N 475 
TRP   CD2  C Y N 476 
TRP   NE1  N Y N 477 
TRP   CE2  C Y N 478 
TRP   CE3  C Y N 479 
TRP   CZ2  C Y N 480 
TRP   CZ3  C Y N 481 
TRP   CH2  C Y N 482 
TRP   OXT  O N N 483 
TRP   H    H N N 484 
TRP   H2   H N N 485 
TRP   HA   H N N 486 
TRP   HB2  H N N 487 
TRP   HB3  H N N 488 
TRP   HD1  H N N 489 
TRP   HE1  H N N 490 
TRP   HE3  H N N 491 
TRP   HZ2  H N N 492 
TRP   HZ3  H N N 493 
TRP   HH2  H N N 494 
TRP   HXT  H N N 495 
TYR   N    N N N 496 
TYR   CA   C N S 497 
TYR   C    C N N 498 
TYR   O    O N N 499 
TYR   CB   C N N 500 
TYR   CG   C Y N 501 
TYR   CD1  C Y N 502 
TYR   CD2  C Y N 503 
TYR   CE1  C Y N 504 
TYR   CE2  C Y N 505 
TYR   CZ   C Y N 506 
TYR   OH   O N N 507 
TYR   OXT  O N N 508 
TYR   H    H N N 509 
TYR   H2   H N N 510 
TYR   HA   H N N 511 
TYR   HB2  H N N 512 
TYR   HB3  H N N 513 
TYR   HD1  H N N 514 
TYR   HD2  H N N 515 
TYR   HE1  H N N 516 
TYR   HE2  H N N 517 
TYR   HH   H N N 518 
TYR   HXT  H N N 519 
VAL   N    N N N 520 
VAL   CA   C N S 521 
VAL   C    C N N 522 
VAL   O    O N N 523 
VAL   CB   C N N 524 
VAL   CG1  C N N 525 
VAL   CG2  C N N 526 
VAL   OXT  O N N 527 
VAL   H    H N N 528 
VAL   H2   H N N 529 
VAL   HA   H N N 530 
VAL   HB   H N N 531 
VAL   HG11 H N N 532 
VAL   HG12 H N N 533 
VAL   HG13 H N N 534 
VAL   HG21 H N N 535 
VAL   HG22 H N N 536 
VAL   HG23 H N N 537 
VAL   HXT  H N N 538 
# 
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 
A1AI4 C3  C2   doub Y N 1   
A1AI4 C3  C4   sing Y N 2   
A1AI4 C2  C1   sing Y N 3   
A1AI4 C34 C31  sing N N 4   
A1AI4 N11 C4   sing N N 5   
A1AI4 N11 C10  sing N N 6   
A1AI4 N12 C10  doub Y N 7   
A1AI4 N12 C13  sing Y N 8   
A1AI4 N33 C32  trip N N 9   
A1AI4 C4  C5   doub Y N 10  
A1AI4 C10 C9   sing Y N 11  
A1AI4 C13 C14  doub Y N 12  
A1AI4 C32 C31  sing N N 13  
A1AI4 C9  C8   sing N N 14  
A1AI4 C9  C15  doub Y N 15  
A1AI4 C14 C15  sing Y N 16  
A1AI4 C1  C31  sing N N 17  
A1AI4 C1  C6   doub Y N 18  
A1AI4 C8  N7   sing N N 19  
A1AI4 C31 C35  sing N N 20  
A1AI4 C5  C6   sing Y N 21  
A1AI4 C5  N7   sing N N 22  
A1AI4 N7  C16  sing N N 23  
A1AI4 C16 O30  doub N N 24  
A1AI4 C16 C17  sing N N 25  
A1AI4 C17 C18  doub Y N 26  
A1AI4 C17 C22  sing Y N 27  
A1AI4 C18 C19  sing Y N 28  
A1AI4 C22 C21  doub Y N 29  
A1AI4 C19 C20  doub Y N 30  
A1AI4 C21 C20  sing Y N 31  
A1AI4 C20 C23  sing N N 32  
A1AI4 C24 C23  sing N N 33  
A1AI4 C23 O25  sing N N 34  
A1AI4 C23 C26  sing N N 35  
A1AI4 F28 C26  sing N N 36  
A1AI4 C26 F27  sing N N 37  
A1AI4 C26 F29  sing N N 38  
A1AI4 C14 H1   sing N N 39  
A1AI4 C18 H2   sing N N 40  
A1AI4 C22 H3   sing N N 41  
A1AI4 C15 H4   sing N N 42  
A1AI4 C19 H5   sing N N 43  
A1AI4 C21 H6   sing N N 44  
A1AI4 C2  H7   sing N N 45  
A1AI4 C3  H8   sing N N 46  
A1AI4 C6  H9   sing N N 47  
A1AI4 C13 H10  sing N N 48  
A1AI4 C8  H11  sing N N 49  
A1AI4 C8  H12  sing N N 50  
A1AI4 C34 H13  sing N N 51  
A1AI4 C34 H14  sing N N 52  
A1AI4 C34 H15  sing N N 53  
A1AI4 C35 H16  sing N N 54  
A1AI4 C35 H17  sing N N 55  
A1AI4 C35 H18  sing N N 56  
A1AI4 C24 H19  sing N N 57  
A1AI4 C24 H20  sing N N 58  
A1AI4 C24 H21  sing N N 59  
A1AI4 N11 H22  sing N N 60  
A1AI4 O25 H23  sing N N 61  
ALA   N   CA   sing N N 62  
ALA   N   H    sing N N 63  
ALA   N   H2   sing N N 64  
ALA   CA  C    sing N N 65  
ALA   CA  CB   sing N N 66  
ALA   CA  HA   sing N N 67  
ALA   C   O    doub N N 68  
ALA   C   OXT  sing N N 69  
ALA   CB  HB1  sing N N 70  
ALA   CB  HB2  sing N N 71  
ALA   CB  HB3  sing N N 72  
ALA   OXT HXT  sing N N 73  
ARG   N   CA   sing N N 74  
ARG   N   H    sing N N 75  
ARG   N   H2   sing N N 76  
ARG   CA  C    sing N N 77  
ARG   CA  CB   sing N N 78  
ARG   CA  HA   sing N N 79  
ARG   C   O    doub N N 80  
ARG   C   OXT  sing N N 81  
ARG   CB  CG   sing N N 82  
ARG   CB  HB2  sing N N 83  
ARG   CB  HB3  sing N N 84  
ARG   CG  CD   sing N N 85  
ARG   CG  HG2  sing N N 86  
ARG   CG  HG3  sing N N 87  
ARG   CD  NE   sing N N 88  
ARG   CD  HD2  sing N N 89  
ARG   CD  HD3  sing N N 90  
ARG   NE  CZ   sing N N 91  
ARG   NE  HE   sing N N 92  
ARG   CZ  NH1  sing N N 93  
ARG   CZ  NH2  doub N N 94  
ARG   NH1 HH11 sing N N 95  
ARG   NH1 HH12 sing N N 96  
ARG   NH2 HH21 sing N N 97  
ARG   NH2 HH22 sing N N 98  
ARG   OXT HXT  sing N N 99  
ASN   N   CA   sing N N 100 
ASN   N   H    sing N N 101 
ASN   N   H2   sing N N 102 
ASN   CA  C    sing N N 103 
ASN   CA  CB   sing N N 104 
ASN   CA  HA   sing N N 105 
ASN   C   O    doub N N 106 
ASN   C   OXT  sing N N 107 
ASN   CB  CG   sing N N 108 
ASN   CB  HB2  sing N N 109 
ASN   CB  HB3  sing N N 110 
ASN   CG  OD1  doub N N 111 
ASN   CG  ND2  sing N N 112 
ASN   ND2 HD21 sing N N 113 
ASN   ND2 HD22 sing N N 114 
ASN   OXT HXT  sing N N 115 
ASP   N   CA   sing N N 116 
ASP   N   H    sing N N 117 
ASP   N   H2   sing N N 118 
ASP   CA  C    sing N N 119 
ASP   CA  CB   sing N N 120 
ASP   CA  HA   sing N N 121 
ASP   C   O    doub N N 122 
ASP   C   OXT  sing N N 123 
ASP   CB  CG   sing N N 124 
ASP   CB  HB2  sing N N 125 
ASP   CB  HB3  sing N N 126 
ASP   CG  OD1  doub N N 127 
ASP   CG  OD2  sing N N 128 
ASP   OD2 HD2  sing N N 129 
ASP   OXT HXT  sing N N 130 
CYS   N   CA   sing N N 131 
CYS   N   H    sing N N 132 
CYS   N   H2   sing N N 133 
CYS   CA  C    sing N N 134 
CYS   CA  CB   sing N N 135 
CYS   CA  HA   sing N N 136 
CYS   C   O    doub N N 137 
CYS   C   OXT  sing N N 138 
CYS   CB  SG   sing N N 139 
CYS   CB  HB2  sing N N 140 
CYS   CB  HB3  sing N N 141 
CYS   SG  HG   sing N N 142 
CYS   OXT HXT  sing N N 143 
GLN   N   CA   sing N N 144 
GLN   N   H    sing N N 145 
GLN   N   H2   sing N N 146 
GLN   CA  C    sing N N 147 
GLN   CA  CB   sing N N 148 
GLN   CA  HA   sing N N 149 
GLN   C   O    doub N N 150 
GLN   C   OXT  sing N N 151 
GLN   CB  CG   sing N N 152 
GLN   CB  HB2  sing N N 153 
GLN   CB  HB3  sing N N 154 
GLN   CG  CD   sing N N 155 
GLN   CG  HG2  sing N N 156 
GLN   CG  HG3  sing N N 157 
GLN   CD  OE1  doub N N 158 
GLN   CD  NE2  sing N N 159 
GLN   NE2 HE21 sing N N 160 
GLN   NE2 HE22 sing N N 161 
GLN   OXT HXT  sing N N 162 
GLU   N   CA   sing N N 163 
GLU   N   H    sing N N 164 
GLU   N   H2   sing N N 165 
GLU   CA  C    sing N N 166 
GLU   CA  CB   sing N N 167 
GLU   CA  HA   sing N N 168 
GLU   C   O    doub N N 169 
GLU   C   OXT  sing N N 170 
GLU   CB  CG   sing N N 171 
GLU   CB  HB2  sing N N 172 
GLU   CB  HB3  sing N N 173 
GLU   CG  CD   sing N N 174 
GLU   CG  HG2  sing N N 175 
GLU   CG  HG3  sing N N 176 
GLU   CD  OE1  doub N N 177 
GLU   CD  OE2  sing N N 178 
GLU   OE2 HE2  sing N N 179 
GLU   OXT HXT  sing N N 180 
GLY   N   CA   sing N N 181 
GLY   N   H    sing N N 182 
GLY   N   H2   sing N N 183 
GLY   CA  C    sing N N 184 
GLY   CA  HA2  sing N N 185 
GLY   CA  HA3  sing N N 186 
GLY   C   O    doub N N 187 
GLY   C   OXT  sing N N 188 
GLY   OXT HXT  sing N N 189 
GOL   C1  O1   sing N N 190 
GOL   C1  C2   sing N N 191 
GOL   C1  H11  sing N N 192 
GOL   C1  H12  sing N N 193 
GOL   O1  HO1  sing N N 194 
GOL   C2  O2   sing N N 195 
GOL   C2  C3   sing N N 196 
GOL   C2  H2   sing N N 197 
GOL   O2  HO2  sing N N 198 
GOL   C3  O3   sing N N 199 
GOL   C3  H31  sing N N 200 
GOL   C3  H32  sing N N 201 
GOL   O3  HO3  sing N N 202 
HIS   N   CA   sing N N 203 
HIS   N   H    sing N N 204 
HIS   N   H2   sing N N 205 
HIS   CA  C    sing N N 206 
HIS   CA  CB   sing N N 207 
HIS   CA  HA   sing N N 208 
HIS   C   O    doub N N 209 
HIS   C   OXT  sing N N 210 
HIS   CB  CG   sing N N 211 
HIS   CB  HB2  sing N N 212 
HIS   CB  HB3  sing N N 213 
HIS   CG  ND1  sing Y N 214 
HIS   CG  CD2  doub Y N 215 
HIS   ND1 CE1  doub Y N 216 
HIS   ND1 HD1  sing N N 217 
HIS   CD2 NE2  sing Y N 218 
HIS   CD2 HD2  sing N N 219 
HIS   CE1 NE2  sing Y N 220 
HIS   CE1 HE1  sing N N 221 
HIS   NE2 HE2  sing N N 222 
HIS   OXT HXT  sing N N 223 
HOH   O   H1   sing N N 224 
HOH   O   H2   sing N N 225 
ILE   N   CA   sing N N 226 
ILE   N   H    sing N N 227 
ILE   N   H2   sing N N 228 
ILE   CA  C    sing N N 229 
ILE   CA  CB   sing N N 230 
ILE   CA  HA   sing N N 231 
ILE   C   O    doub N N 232 
ILE   C   OXT  sing N N 233 
ILE   CB  CG1  sing N N 234 
ILE   CB  CG2  sing N N 235 
ILE   CB  HB   sing N N 236 
ILE   CG1 CD1  sing N N 237 
ILE   CG1 HG12 sing N N 238 
ILE   CG1 HG13 sing N N 239 
ILE   CG2 HG21 sing N N 240 
ILE   CG2 HG22 sing N N 241 
ILE   CG2 HG23 sing N N 242 
ILE   CD1 HD11 sing N N 243 
ILE   CD1 HD12 sing N N 244 
ILE   CD1 HD13 sing N N 245 
ILE   OXT HXT  sing N N 246 
LEU   N   CA   sing N N 247 
LEU   N   H    sing N N 248 
LEU   N   H2   sing N N 249 
LEU   CA  C    sing N N 250 
LEU   CA  CB   sing N N 251 
LEU   CA  HA   sing N N 252 
LEU   C   O    doub N N 253 
LEU   C   OXT  sing N N 254 
LEU   CB  CG   sing N N 255 
LEU   CB  HB2  sing N N 256 
LEU   CB  HB3  sing N N 257 
LEU   CG  CD1  sing N N 258 
LEU   CG  CD2  sing N N 259 
LEU   CG  HG   sing N N 260 
LEU   CD1 HD11 sing N N 261 
LEU   CD1 HD12 sing N N 262 
LEU   CD1 HD13 sing N N 263 
LEU   CD2 HD21 sing N N 264 
LEU   CD2 HD22 sing N N 265 
LEU   CD2 HD23 sing N N 266 
LEU   OXT HXT  sing N N 267 
LYS   N   CA   sing N N 268 
LYS   N   H    sing N N 269 
LYS   N   H2   sing N N 270 
LYS   CA  C    sing N N 271 
LYS   CA  CB   sing N N 272 
LYS   CA  HA   sing N N 273 
LYS   C   O    doub N N 274 
LYS   C   OXT  sing N N 275 
LYS   CB  CG   sing N N 276 
LYS   CB  HB2  sing N N 277 
LYS   CB  HB3  sing N N 278 
LYS   CG  CD   sing N N 279 
LYS   CG  HG2  sing N N 280 
LYS   CG  HG3  sing N N 281 
LYS   CD  CE   sing N N 282 
LYS   CD  HD2  sing N N 283 
LYS   CD  HD3  sing N N 284 
LYS   CE  NZ   sing N N 285 
LYS   CE  HE2  sing N N 286 
LYS   CE  HE3  sing N N 287 
LYS   NZ  HZ1  sing N N 288 
LYS   NZ  HZ2  sing N N 289 
LYS   NZ  HZ3  sing N N 290 
LYS   OXT HXT  sing N N 291 
MET   N   CA   sing N N 292 
MET   N   H    sing N N 293 
MET   N   H2   sing N N 294 
MET   CA  C    sing N N 295 
MET   CA  CB   sing N N 296 
MET   CA  HA   sing N N 297 
MET   C   O    doub N N 298 
MET   C   OXT  sing N N 299 
MET   CB  CG   sing N N 300 
MET   CB  HB2  sing N N 301 
MET   CB  HB3  sing N N 302 
MET   CG  SD   sing N N 303 
MET   CG  HG2  sing N N 304 
MET   CG  HG3  sing N N 305 
MET   SD  CE   sing N N 306 
MET   CE  HE1  sing N N 307 
MET   CE  HE2  sing N N 308 
MET   CE  HE3  sing N N 309 
MET   OXT HXT  sing N N 310 
NAP   PA  O1A  doub N N 311 
NAP   PA  O2A  sing N N 312 
NAP   PA  O5B  sing N N 313 
NAP   PA  O3   sing N N 314 
NAP   O2A HOA2 sing N N 315 
NAP   O5B C5B  sing N N 316 
NAP   C5B C4B  sing N N 317 
NAP   C5B H51A sing N N 318 
NAP   C5B H52A sing N N 319 
NAP   C4B O4B  sing N N 320 
NAP   C4B C3B  sing N N 321 
NAP   C4B H4B  sing N N 322 
NAP   O4B C1B  sing N N 323 
NAP   C3B O3B  sing N N 324 
NAP   C3B C2B  sing N N 325 
NAP   C3B H3B  sing N N 326 
NAP   O3B HO3A sing N N 327 
NAP   C2B O2B  sing N N 328 
NAP   C2B C1B  sing N N 329 
NAP   C2B H2B  sing N N 330 
NAP   O2B P2B  sing N N 331 
NAP   C1B N9A  sing N N 332 
NAP   C1B H1B  sing N N 333 
NAP   N9A C8A  sing Y N 334 
NAP   N9A C4A  sing Y N 335 
NAP   C8A N7A  doub Y N 336 
NAP   C8A H8A  sing N N 337 
NAP   N7A C5A  sing Y N 338 
NAP   C5A C6A  sing Y N 339 
NAP   C5A C4A  doub Y N 340 
NAP   C6A N6A  sing N N 341 
NAP   C6A N1A  doub Y N 342 
NAP   N6A H61A sing N N 343 
NAP   N6A H62A sing N N 344 
NAP   N1A C2A  sing Y N 345 
NAP   C2A N3A  doub Y N 346 
NAP   C2A H2A  sing N N 347 
NAP   N3A C4A  sing Y N 348 
NAP   O3  PN   sing N N 349 
NAP   PN  O1N  doub N N 350 
NAP   PN  O2N  sing N N 351 
NAP   PN  O5D  sing N N 352 
NAP   O5D C5D  sing N N 353 
NAP   C5D C4D  sing N N 354 
NAP   C5D H51N sing N N 355 
NAP   C5D H52N sing N N 356 
NAP   C4D O4D  sing N N 357 
NAP   C4D C3D  sing N N 358 
NAP   C4D H4D  sing N N 359 
NAP   O4D C1D  sing N N 360 
NAP   C3D O3D  sing N N 361 
NAP   C3D C2D  sing N N 362 
NAP   C3D H3D  sing N N 363 
NAP   O3D HO3N sing N N 364 
NAP   C2D O2D  sing N N 365 
NAP   C2D C1D  sing N N 366 
NAP   C2D H2D  sing N N 367 
NAP   O2D HO2N sing N N 368 
NAP   C1D N1N  sing N N 369 
NAP   C1D H1D  sing N N 370 
NAP   N1N C2N  sing Y N 371 
NAP   N1N C6N  doub Y N 372 
NAP   C2N C3N  doub Y N 373 
NAP   C2N H2N  sing N N 374 
NAP   C3N C7N  sing N N 375 
NAP   C3N C4N  sing Y N 376 
NAP   C7N O7N  doub N N 377 
NAP   C7N N7N  sing N N 378 
NAP   N7N H71N sing N N 379 
NAP   N7N H72N sing N N 380 
NAP   C4N C5N  doub Y N 381 
NAP   C4N H4N  sing N N 382 
NAP   C5N C6N  sing Y N 383 
NAP   C5N H5N  sing N N 384 
NAP   C6N H6N  sing N N 385 
NAP   P2B O1X  doub N N 386 
NAP   P2B O2X  sing N N 387 
NAP   P2B O3X  sing N N 388 
NAP   O2X HOP2 sing N N 389 
NAP   O3X HOP3 sing N N 390 
PHE   N   CA   sing N N 391 
PHE   N   H    sing N N 392 
PHE   N   H2   sing N N 393 
PHE   CA  C    sing N N 394 
PHE   CA  CB   sing N N 395 
PHE   CA  HA   sing N N 396 
PHE   C   O    doub N N 397 
PHE   C   OXT  sing N N 398 
PHE   CB  CG   sing N N 399 
PHE   CB  HB2  sing N N 400 
PHE   CB  HB3  sing N N 401 
PHE   CG  CD1  doub Y N 402 
PHE   CG  CD2  sing Y N 403 
PHE   CD1 CE1  sing Y N 404 
PHE   CD1 HD1  sing N N 405 
PHE   CD2 CE2  doub Y N 406 
PHE   CD2 HD2  sing N N 407 
PHE   CE1 CZ   doub Y N 408 
PHE   CE1 HE1  sing N N 409 
PHE   CE2 CZ   sing Y N 410 
PHE   CE2 HE2  sing N N 411 
PHE   CZ  HZ   sing N N 412 
PHE   OXT HXT  sing N N 413 
PRO   N   CA   sing N N 414 
PRO   N   CD   sing N N 415 
PRO   N   H    sing N N 416 
PRO   CA  C    sing N N 417 
PRO   CA  CB   sing N N 418 
PRO   CA  HA   sing N N 419 
PRO   C   O    doub N N 420 
PRO   C   OXT  sing N N 421 
PRO   CB  CG   sing N N 422 
PRO   CB  HB2  sing N N 423 
PRO   CB  HB3  sing N N 424 
PRO   CG  CD   sing N N 425 
PRO   CG  HG2  sing N N 426 
PRO   CG  HG3  sing N N 427 
PRO   CD  HD2  sing N N 428 
PRO   CD  HD3  sing N N 429 
PRO   OXT HXT  sing N N 430 
SER   N   CA   sing N N 431 
SER   N   H    sing N N 432 
SER   N   H2   sing N N 433 
SER   CA  C    sing N N 434 
SER   CA  CB   sing N N 435 
SER   CA  HA   sing N N 436 
SER   C   O    doub N N 437 
SER   C   OXT  sing N N 438 
SER   CB  OG   sing N N 439 
SER   CB  HB2  sing N N 440 
SER   CB  HB3  sing N N 441 
SER   OG  HG   sing N N 442 
SER   OXT HXT  sing N N 443 
THR   N   CA   sing N N 444 
THR   N   H    sing N N 445 
THR   N   H2   sing N N 446 
THR   CA  C    sing N N 447 
THR   CA  CB   sing N N 448 
THR   CA  HA   sing N N 449 
THR   C   O    doub N N 450 
THR   C   OXT  sing N N 451 
THR   CB  OG1  sing N N 452 
THR   CB  CG2  sing N N 453 
THR   CB  HB   sing N N 454 
THR   OG1 HG1  sing N N 455 
THR   CG2 HG21 sing N N 456 
THR   CG2 HG22 sing N N 457 
THR   CG2 HG23 sing N N 458 
THR   OXT HXT  sing N N 459 
TRP   N   CA   sing N N 460 
TRP   N   H    sing N N 461 
TRP   N   H2   sing N N 462 
TRP   CA  C    sing N N 463 
TRP   CA  CB   sing N N 464 
TRP   CA  HA   sing N N 465 
TRP   C   O    doub N N 466 
TRP   C   OXT  sing N N 467 
TRP   CB  CG   sing N N 468 
TRP   CB  HB2  sing N N 469 
TRP   CB  HB3  sing N N 470 
TRP   CG  CD1  doub Y N 471 
TRP   CG  CD2  sing Y N 472 
TRP   CD1 NE1  sing Y N 473 
TRP   CD1 HD1  sing N N 474 
TRP   CD2 CE2  doub Y N 475 
TRP   CD2 CE3  sing Y N 476 
TRP   NE1 CE2  sing Y N 477 
TRP   NE1 HE1  sing N N 478 
TRP   CE2 CZ2  sing Y N 479 
TRP   CE3 CZ3  doub Y N 480 
TRP   CE3 HE3  sing N N 481 
TRP   CZ2 CH2  doub Y N 482 
TRP   CZ2 HZ2  sing N N 483 
TRP   CZ3 CH2  sing Y N 484 
TRP   CZ3 HZ3  sing N N 485 
TRP   CH2 HH2  sing N N 486 
TRP   OXT HXT  sing N N 487 
TYR   N   CA   sing N N 488 
TYR   N   H    sing N N 489 
TYR   N   H2   sing N N 490 
TYR   CA  C    sing N N 491 
TYR   CA  CB   sing N N 492 
TYR   CA  HA   sing N N 493 
TYR   C   O    doub N N 494 
TYR   C   OXT  sing N N 495 
TYR   CB  CG   sing N N 496 
TYR   CB  HB2  sing N N 497 
TYR   CB  HB3  sing N N 498 
TYR   CG  CD1  doub Y N 499 
TYR   CG  CD2  sing Y N 500 
TYR   CD1 CE1  sing Y N 501 
TYR   CD1 HD1  sing N N 502 
TYR   CD2 CE2  doub Y N 503 
TYR   CD2 HD2  sing N N 504 
TYR   CE1 CZ   doub Y N 505 
TYR   CE1 HE1  sing N N 506 
TYR   CE2 CZ   sing Y N 507 
TYR   CE2 HE2  sing N N 508 
TYR   CZ  OH   sing N N 509 
TYR   OH  HH   sing N N 510 
TYR   OXT HXT  sing N N 511 
VAL   N   CA   sing N N 512 
VAL   N   H    sing N N 513 
VAL   N   H2   sing N N 514 
VAL   CA  C    sing N N 515 
VAL   CA  CB   sing N N 516 
VAL   CA  HA   sing N N 517 
VAL   C   O    doub N N 518 
VAL   C   OXT  sing N N 519 
VAL   CB  CG1  sing N N 520 
VAL   CB  CG2  sing N N 521 
VAL   CB  HB   sing N N 522 
VAL   CG1 HG11 sing N N 523 
VAL   CG1 HG12 sing N N 524 
VAL   CG1 HG13 sing N N 525 
VAL   CG2 HG21 sing N N 526 
VAL   CG2 HG22 sing N N 527 
VAL   CG2 HG23 sing N N 528 
VAL   OXT HXT  sing N N 529 
# 
_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      PDB 
_pdbx_initial_refinement_model.accession_code   3MAP 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9B81 
_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]   0.012079 
_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]   0.012079 
_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]   0.003310 
_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 
P 
S 
# 
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   . LYS   A 1 3   ? 17.259 6.491   -42.799 1.00 59.22  ? 3   LYS   A N   1 
ATOM   2    C CA  . LYS   A 1 3   ? 18.684 6.159   -42.694 1.00 58.32  ? 3   LYS   A CA  1 
ATOM   3    C C   . LYS   A 1 3   ? 19.088 5.847   -41.240 1.00 60.82  ? 3   LYS   A C   1 
ATOM   4    O O   . LYS   A 1 3   ? 18.454 6.320   -40.285 1.00 61.99  ? 3   LYS   A O   1 
ATOM   5    C CB  . LYS   A 1 3   ? 19.565 7.289   -43.270 1.00 59.89  ? 3   LYS   A CB  1 
ATOM   6    N N   . LYS   A 1 4   ? 20.146 5.045   -41.088 1.00 53.12  ? 4   LYS   A N   1 
ATOM   7    C CA  . LYS   A 1 4   ? 20.702 4.643   -39.795 1.00 49.58  ? 4   LYS   A CA  1 
ATOM   8    C C   . LYS   A 1 4   ? 21.691 5.708   -39.325 1.00 49.78  ? 4   LYS   A C   1 
ATOM   9    O O   . LYS   A 1 4   ? 22.176 6.509   -40.131 1.00 49.99  ? 4   LYS   A O   1 
ATOM   10   C CB  . LYS   A 1 4   ? 21.405 3.285   -39.918 1.00 48.90  ? 4   LYS   A CB  1 
ATOM   11   C CG  . LYS   A 1 4   ? 20.435 2.152   -40.139 1.00 43.31  ? 4   LYS   A CG  1 
ATOM   12   C CD  . LYS   A 1 4   ? 21.120 0.868   -40.524 1.00 39.00  ? 4   LYS   A CD  1 
ATOM   13   C CE  . LYS   A 1 4   ? 20.128 -0.253  -40.620 1.00 45.94  ? 4   LYS   A CE  1 
ATOM   14   N NZ  . LYS   A 1 4   ? 20.781 -1.527  -40.987 1.00 60.40  ? 4   LYS   A NZ  1 
ATOM   15   N N   . ILE   A 1 5   ? 21.993 5.707   -38.027 1.00 41.70  ? 5   ILE   A N   1 
ATOM   16   C CA  . ILE   A 1 5   ? 22.928 6.638   -37.423 1.00 40.18  ? 5   ILE   A CA  1 
ATOM   17   C C   . ILE   A 1 5   ? 24.360 6.219   -37.748 1.00 44.15  ? 5   ILE   A C   1 
ATOM   18   O O   . ILE   A 1 5   ? 24.683 5.021   -37.690 1.00 43.84  ? 5   ILE   A O   1 
ATOM   19   C CB  . ILE   A 1 5   ? 22.695 6.675   -35.878 1.00 42.10  ? 5   ILE   A CB  1 
ATOM   20   C CG1 . ILE   A 1 5   ? 21.236 7.072   -35.531 1.00 42.11  ? 5   ILE   A CG1 1 
ATOM   21   C CG2 . ILE   A 1 5   ? 23.692 7.583   -35.178 1.00 40.55  ? 5   ILE   A CG2 1 
ATOM   22   C CD1 . ILE   A 1 5   ? 20.701 6.483   -34.182 1.00 46.03  ? 5   ILE   A CD1 1 
ATOM   23   N N   . SER   A 1 6   ? 25.225 7.209   -38.052 1.00 40.84  ? 6   SER   A N   1 
ATOM   24   C CA  . SER   A 1 6   ? 26.657 6.991   -38.290 1.00 40.41  ? 6   SER   A CA  1 
ATOM   25   C C   . SER   A 1 6   ? 27.260 7.073   -36.899 1.00 42.72  ? 6   SER   A C   1 
ATOM   26   O O   . SER   A 1 6   ? 27.342 8.159   -36.303 1.00 42.69  ? 6   SER   A O   1 
ATOM   27   C CB  . SER   A 1 6   ? 27.244 8.069   -39.195 1.00 44.11  ? 6   SER   A CB  1 
ATOM   28   O OG  . SER   A 1 6   ? 26.769 7.874   -40.514 1.00 56.74  ? 6   SER   A OG  1 
ATOM   29   N N   . GLY   A 1 7   ? 27.605 5.910   -36.366 1.00 37.09  ? 7   GLY   A N   1 
ATOM   30   C CA  . GLY   A 1 7   ? 28.145 5.783   -35.026 1.00 36.23  ? 7   GLY   A CA  1 
ATOM   31   C C   . GLY   A 1 7   ? 29.631 5.985   -34.881 1.00 40.82  ? 7   GLY   A C   1 
ATOM   32   O O   . GLY   A 1 7   ? 30.112 6.178   -33.764 1.00 43.03  ? 7   GLY   A O   1 
ATOM   33   N N   . GLY   A 1 8   ? 30.368 5.939   -35.980 1.00 35.17  ? 8   GLY   A N   1 
ATOM   34   C CA  . GLY   A 1 8   ? 31.813 6.105   -35.899 1.00 33.89  ? 8   GLY   A CA  1 
ATOM   35   C C   . GLY   A 1 8   ? 32.571 4.862   -35.480 1.00 37.05  ? 8   GLY   A C   1 
ATOM   36   O O   . GLY   A 1 8   ? 32.094 3.730   -35.635 1.00 35.54  ? 8   GLY   A O   1 
ATOM   37   N N   . SER   A 1 9   ? 33.777 5.083   -34.948 1.00 34.92  ? 9   SER   A N   1 
ATOM   38   C CA  . SER   A 1 9   ? 34.735 4.050   -34.569 1.00 34.72  ? 9   SER   A CA  1 
ATOM   39   C C   . SER   A 1 9   ? 34.543 3.337   -33.204 1.00 41.61  ? 9   SER   A C   1 
ATOM   40   O O   . SER   A 1 9   ? 34.698 3.947   -32.138 1.00 42.74  ? 9   SER   A O   1 
ATOM   41   C CB  . SER   A 1 9   ? 36.148 4.573   -34.770 1.00 35.53  ? 9   SER   A CB  1 
ATOM   42   O OG  . SER   A 1 9   ? 37.073 3.601   -34.327 1.00 47.91  ? 9   SER   A OG  1 
ATOM   43   N N   . VAL   A 1 10  ? 34.205 2.030   -33.249 1.00 36.47  ? 10  VAL   A N   1 
ATOM   44   C CA  . VAL   A 1 10  ? 33.969 1.235   -32.040 1.00 34.70  ? 10  VAL   A CA  1 
ATOM   45   C C   . VAL   A 1 10  ? 34.767 -0.053  -32.083 1.00 36.21  ? 10  VAL   A C   1 
ATOM   46   O O   . VAL   A 1 10  ? 34.772 -0.728  -33.109 1.00 35.74  ? 10  VAL   A O   1 
ATOM   47   C CB  . VAL   A 1 10  ? 32.447 0.995   -31.774 1.00 38.04  ? 10  VAL   A CB  1 
ATOM   48   C CG1 . VAL   A 1 10  ? 32.216 0.026   -30.609 1.00 37.55  ? 10  VAL   A CG1 1 
ATOM   49   C CG2 . VAL   A 1 10  ? 31.715 2.315   -31.507 1.00 37.59  ? 10  VAL   A CG2 1 
ATOM   50   N N   . VAL   A 1 11  ? 35.468 -0.380  -30.976 1.00 32.07  ? 11  VAL   A N   1 
ATOM   51   C CA  . VAL   A 1 11  ? 36.243 -1.616  -30.852 1.00 31.98  ? 11  VAL   A CA  1 
ATOM   52   C C   . VAL   A 1 11  ? 35.310 -2.609  -30.164 1.00 38.56  ? 11  VAL   A C   1 
ATOM   53   O O   . VAL   A 1 11  ? 34.814 -2.345  -29.069 1.00 39.15  ? 11  VAL   A O   1 
ATOM   54   C CB  . VAL   A 1 11  ? 37.597 -1.464  -30.109 1.00 35.15  ? 11  VAL   A CB  1 
ATOM   55   C CG1 . VAL   A 1 11  ? 38.387 -2.778  -30.148 1.00 35.15  ? 11  VAL   A CG1 1 
ATOM   56   C CG2 . VAL   A 1 11  ? 38.423 -0.327  -30.696 1.00 34.36  ? 11  VAL   A CG2 1 
ATOM   57   N N   . GLU   A 1 12  ? 35.040 -3.720  -30.823 1.00 36.16  ? 12  GLU   A N   1 
ATOM   58   C CA  . GLU   A 1 12  ? 34.144 -4.755  -30.323 1.00 36.36  ? 12  GLU   A CA  1 
ATOM   59   C C   . GLU   A 1 12  ? 34.896 -6.088  -30.124 1.00 41.36  ? 12  GLU   A C   1 
ATOM   60   O O   . GLU   A 1 12  ? 35.634 -6.525  -31.018 1.00 40.73  ? 12  GLU   A O   1 
ATOM   61   C CB  . GLU   A 1 12  ? 32.952 -4.915  -31.283 1.00 37.18  ? 12  GLU   A CB  1 
ATOM   62   C CG  . GLU   A 1 12  ? 31.926 -5.928  -30.828 1.00 38.22  ? 12  GLU   A CG  1 
ATOM   63   C CD  . GLU   A 1 12  ? 31.722 -7.117  -31.735 1.00 48.33  ? 12  GLU   A CD  1 
ATOM   64   O OE1 . GLU   A 1 12  ? 32.186 -7.089  -32.893 1.00 46.14  ? 12  GLU   A OE1 1 
ATOM   65   O OE2 . GLU   A 1 12  ? 31.063 -8.078  -31.289 1.00 53.61  ? 12  GLU   A OE2 1 
ATOM   66   N N   . MET   A 1 13  ? 34.704 -6.721  -28.939 1.00 37.51  ? 13  MET   A N   1 
ATOM   67   C CA  . MET   A 1 13  ? 35.335 -7.995  -28.603 1.00 36.83  ? 13  MET   A CA  1 
ATOM   68   C C   . MET   A 1 13  ? 34.285 -9.058  -28.303 1.00 40.23  ? 13  MET   A C   1 
ATOM   69   O O   . MET   A 1 13  ? 33.516 -8.934  -27.338 1.00 39.93  ? 13  MET   A O   1 
ATOM   70   C CB  . MET   A 1 13  ? 36.317 -7.847  -27.434 1.00 39.41  ? 13  MET   A CB  1 
ATOM   71   C CG  . MET   A 1 13  ? 37.483 -6.943  -27.728 1.00 43.80  ? 13  MET   A CG  1 
ATOM   72   S SD  . MET   A 1 13  ? 37.966 -5.952  -26.291 1.00 48.45  ? 13  MET   A SD  1 
ATOM   73   C CE  . MET   A 1 13  ? 36.777 -4.588  -26.446 1.00 45.30  ? 13  MET   A CE  1 
ATOM   74   N N   . GLN   A 1 14  ? 34.252 -10.094 -29.145 1.00 37.23  ? 14  GLN   A N   1 
ATOM   75   C CA  . GLN   A 1 14  ? 33.357 -11.247 -29.034 1.00 37.54  ? 14  GLN   A CA  1 
ATOM   76   C C   . GLN   A 1 14  ? 33.892 -12.184 -27.935 1.00 41.40  ? 14  GLN   A C   1 
ATOM   77   O O   . GLN   A 1 14  ? 35.101 -12.283 -27.722 1.00 39.24  ? 14  GLN   A O   1 
ATOM   78   C CB  . GLN   A 1 14  ? 33.245 -11.966 -30.380 1.00 38.98  ? 14  GLN   A CB  1 
ATOM   79   C CG  . GLN   A 1 14  ? 32.284 -11.285 -31.332 1.00 54.21  ? 14  GLN   A CG  1 
ATOM   80   C CD  . GLN   A 1 14  ? 32.692 -11.433 -32.777 1.00 80.67  ? 14  GLN   A CD  1 
ATOM   81   O OE1 . GLN   A 1 14  ? 32.859 -12.541 -33.301 1.00 75.43  ? 14  GLN   A OE1 1 
ATOM   82   N NE2 . GLN   A 1 14  ? 32.851 -10.308 -33.461 1.00 76.64  ? 14  GLN   A NE2 1 
ATOM   83   N N   . GLY   A 1 15  ? 32.988 -12.829 -27.222 1.00 39.87  ? 15  GLY   A N   1 
ATOM   84   C CA  . GLY   A 1 15  ? 33.378 -13.677 -26.109 1.00 39.82  ? 15  GLY   A CA  1 
ATOM   85   C C   . GLY   A 1 15  ? 32.950 -15.111 -26.198 1.00 43.98  ? 15  GLY   A C   1 
ATOM   86   O O   . GLY   A 1 15  ? 32.863 -15.671 -27.289 1.00 43.02  ? 15  GLY   A O   1 
ATOM   87   N N   . ASP   A 1 16  ? 32.640 -15.701 -25.037 1.00 41.63  ? 16  ASP   A N   1 
ATOM   88   C CA  . ASP   A 1 16  ? 32.278 -17.113 -24.945 1.00 40.76  ? 16  ASP   A CA  1 
ATOM   89   C C   . ASP   A 1 16  ? 30.946 -17.462 -24.322 1.00 45.69  ? 16  ASP   A C   1 
ATOM   90   O O   . ASP   A 1 16  ? 30.348 -16.682 -23.551 1.00 46.02  ? 16  ASP   A O   1 
ATOM   91   C CB  . ASP   A 1 16  ? 33.339 -17.827 -24.097 1.00 41.33  ? 16  ASP   A CB  1 
ATOM   92   C CG  . ASP   A 1 16  ? 34.753 -17.772 -24.618 1.00 39.81  ? 16  ASP   A CG  1 
ATOM   93   O OD1 . ASP   A 1 16  ? 35.598 -17.101 -23.972 1.00 36.53  ? 16  ASP   A OD1 1 
ATOM   94   O OD2 . ASP   A 1 16  ? 35.026 -18.420 -25.655 1.00 42.21  ? 16  ASP   A OD2 1 
ATOM   95   N N   . GLU   A 1 17  ? 30.533 -18.709 -24.625 1.00 40.63  ? 17  GLU   A N   1 
ATOM   96   C CA  . GLU   A 1 17  ? 29.382 -19.414 -24.081 1.00 40.68  ? 17  GLU   A CA  1 
ATOM   97   C C   . GLU   A 1 17  ? 28.017 -18.728 -24.228 1.00 43.65  ? 17  GLU   A C   1 
ATOM   98   O O   . GLU   A 1 17  ? 27.673 -18.366 -25.354 1.00 43.07  ? 17  GLU   A O   1 
ATOM   99   C CB  . GLU   A 1 17  ? 29.710 -19.939 -22.656 1.00 41.98  ? 17  GLU   A CB  1 
ATOM   100  C CG  . GLU   A 1 17  ? 31.006 -20.744 -22.649 1.00 50.59  ? 17  GLU   A CG  1 
ATOM   101  C CD  . GLU   A 1 17  ? 31.350 -21.617 -21.454 1.00 72.25  ? 17  GLU   A CD  1 
ATOM   102  O OE1 . GLU   A 1 17  ? 31.423 -21.097 -20.316 1.00 43.28  ? 17  GLU   A OE1 1 
ATOM   103  O OE2 . GLU   A 1 17  ? 31.580 -22.829 -21.671 1.00 73.84  ? 17  GLU   A OE2 1 
ATOM   104  N N   . MET   A 1 18  ? 27.229 -18.581 -23.140 1.00 39.96  ? 18  MET   A N   1 
ATOM   105  C CA  . MET   A 1 18  ? 25.908 -17.949 -23.241 1.00 40.15  ? 18  MET   A CA  1 
ATOM   106  C C   . MET   A 1 18  ? 26.003 -16.472 -23.627 1.00 44.62  ? 18  MET   A C   1 
ATOM   107  O O   . MET   A 1 18  ? 25.161 -15.978 -24.383 1.00 44.61  ? 18  MET   A O   1 
ATOM   108  C CB  . MET   A 1 18  ? 25.053 -18.150 -21.973 1.00 42.19  ? 18  MET   A CB  1 
ATOM   109  C CG  . MET   A 1 18  ? 23.557 -18.098 -22.246 1.00 45.50  ? 18  MET   A CG  1 
ATOM   110  S SD  . MET   A 1 18  ? 23.020 -19.371 -23.411 1.00 50.80  ? 18  MET   A SD  1 
ATOM   111  C CE  . MET   A 1 18  ? 21.640 -18.586 -24.175 1.00 47.48  ? 18  MET   A CE  1 
ATOM   112  N N   . THR   A 1 19  ? 27.050 -15.784 -23.129 1.00 41.23  ? 19  THR   A N   1 
ATOM   113  C CA  . THR   A 1 19  ? 27.302 -14.373 -23.424 1.00 40.22  ? 19  THR   A CA  1 
ATOM   114  C C   . THR   A 1 19  ? 27.578 -14.099 -24.901 1.00 45.66  ? 19  THR   A C   1 
ATOM   115  O O   . THR   A 1 19  ? 27.150 -13.062 -25.385 1.00 48.27  ? 19  THR   A O   1 
ATOM   116  C CB  . THR   A 1 19  ? 28.273 -13.752 -22.443 1.00 36.74  ? 19  THR   A CB  1 
ATOM   117  O OG1 . THR   A 1 19  ? 29.419 -14.596 -22.294 1.00 36.82  ? 19  THR   A OG1 1 
ATOM   118  C CG2 . THR   A 1 19  ? 27.619 -13.464 -21.114 1.00 27.72  ? 19  THR   A CG2 1 
ATOM   119  N N   . ARG   A 1 20  ? 28.251 -15.022 -25.618 1.00 40.82  ? 20  ARG   A N   1 
ATOM   120  C CA  . ARG   A 1 20  ? 28.534 -14.913 -27.046 1.00 40.25  ? 20  ARG   A CA  1 
ATOM   121  C C   . ARG   A 1 20  ? 27.226 -14.971 -27.834 1.00 45.52  ? 20  ARG   A C   1 
ATOM   122  O O   . ARG   A 1 20  ? 27.026 -14.170 -28.753 1.00 45.17  ? 20  ARG   A O   1 
ATOM   123  C CB  . ARG   A 1 20  ? 29.504 -16.008 -27.492 1.00 38.40  ? 20  ARG   A CB  1 
ATOM   124  C CG  . ARG   A 1 20  ? 29.855 -15.975 -28.980 1.00 40.12  ? 20  ARG   A CG  1 
ATOM   125  C CD  . ARG   A 1 20  ? 30.899 -17.010 -29.370 1.00 44.92  ? 20  ARG   A CD  1 
ATOM   126  N NE  . ARG   A 1 20  ? 31.441 -16.725 -30.703 1.00 60.18  ? 20  ARG   A NE  1 
ATOM   127  C CZ  . ARG   A 1 20  ? 32.614 -16.144 -30.957 1.00 68.83  ? 20  ARG   A CZ  1 
ATOM   128  N NH1 . ARG   A 1 20  ? 32.989 -15.918 -32.207 1.00 64.11  ? 20  ARG   A NH1 1 
ATOM   129  N NH2 . ARG   A 1 20  ? 33.426 -15.798 -29.963 1.00 41.30  ? 20  ARG   A NH2 1 
ATOM   130  N N   . ILE   A 1 21  ? 26.316 -15.884 -27.439 1.00 43.29  ? 21  ILE   A N   1 
ATOM   131  C CA  . ILE   A 1 21  ? 24.999 -16.028 -28.077 1.00 43.15  ? 21  ILE   A CA  1 
ATOM   132  C C   . ILE   A 1 21  ? 24.173 -14.744 -27.905 1.00 48.36  ? 21  ILE   A C   1 
ATOM   133  O O   . ILE   A 1 21  ? 23.622 -14.237 -28.895 1.00 49.10  ? 21  ILE   A O   1 
ATOM   134  C CB  . ILE   A 1 21  ? 24.263 -17.316 -27.606 1.00 45.69  ? 21  ILE   A CB  1 
ATOM   135  C CG1 . ILE   A 1 21  ? 24.933 -18.548 -28.233 1.00 46.28  ? 21  ILE   A CG1 1 
ATOM   136  C CG2 . ILE   A 1 21  ? 22.753 -17.299 -27.941 1.00 44.85  ? 21  ILE   A CG2 1 
ATOM   137  C CD1 . ILE   A 1 21  ? 25.180 -19.585 -27.288 1.00 55.97  ? 21  ILE   A CD1 1 
ATOM   138  N N   . ILE   A 1 22  ? 24.110 -14.207 -26.667 1.00 44.24  ? 22  ILE   A N   1 
ATOM   139  C CA  . ILE   A 1 22  ? 23.336 -12.996 -26.439 1.00 44.84  ? 22  ILE   A CA  1 
ATOM   140  C C   . ILE   A 1 22  ? 23.931 -11.732 -27.114 1.00 45.84  ? 22  ILE   A C   1 
ATOM   141  O O   . ILE   A 1 22  ? 23.176 -10.882 -27.607 1.00 45.06  ? 22  ILE   A O   1 
ATOM   142  C CB  . ILE   A 1 22  ? 22.801 -12.823 -24.988 1.00 49.10  ? 22  ILE   A CB  1 
ATOM   143  C CG1 . ILE   A 1 22  ? 23.881 -12.385 -24.039 1.00 51.40  ? 22  ILE   A CG1 1 
ATOM   144  C CG2 . ILE   A 1 22  ? 22.103 -14.078 -24.459 1.00 49.12  ? 22  ILE   A CG2 1 
ATOM   145  C CD1 . ILE   A 1 22  ? 23.599 -11.060 -23.533 1.00 66.57  ? 22  ILE   A CD1 1 
ATOM   146  N N   . TRP   A 1 23  ? 25.279 -11.654 -27.180 1.00 39.82  ? 23  TRP   A N   1 
ATOM   147  C CA  . TRP   A 1 23  ? 26.040 -10.564 -27.795 1.00 39.11  ? 23  TRP   A CA  1 
ATOM   148  C C   . TRP   A 1 23  ? 25.639 -10.411 -29.274 1.00 44.00  ? 23  TRP   A C   1 
ATOM   149  O O   . TRP   A 1 23  ? 25.394 -9.292  -29.729 1.00 44.40  ? 23  TRP   A O   1 
ATOM   150  C CB  . TRP   A 1 23  ? 27.535 -10.846 -27.657 1.00 37.23  ? 23  TRP   A CB  1 
ATOM   151  C CG  . TRP   A 1 23  ? 28.436 -9.671  -27.908 1.00 37.45  ? 23  TRP   A CG  1 
ATOM   152  C CD1 . TRP   A 1 23  ? 29.208 -9.454  -29.012 1.00 39.87  ? 23  TRP   A CD1 1 
ATOM   153  C CD2 . TRP   A 1 23  ? 28.728 -8.598  -26.993 1.00 37.07  ? 23  TRP   A CD2 1 
ATOM   154  N NE1 . TRP   A 1 23  ? 29.979 -8.325  -28.836 1.00 38.73  ? 23  TRP   A NE1 1 
ATOM   155  C CE2 . TRP   A 1 23  ? 29.692 -7.770  -27.614 1.00 39.89  ? 23  TRP   A CE2 1 
ATOM   156  C CE3 . TRP   A 1 23  ? 28.256 -8.246  -25.712 1.00 37.94  ? 23  TRP   A CE3 1 
ATOM   157  C CZ2 . TRP   A 1 23  ? 30.187 -6.611  -27.007 1.00 38.53  ? 23  TRP   A CZ2 1 
ATOM   158  C CZ3 . TRP   A 1 23  ? 28.766 -7.108  -25.101 1.00 38.95  ? 23  TRP   A CZ3 1 
ATOM   159  C CH2 . TRP   A 1 23  ? 29.720 -6.305  -25.746 1.00 39.24  ? 23  TRP   A CH2 1 
ATOM   160  N N   . GLU   A 1 24  ? 25.532 -11.543 -29.997 1.00 40.67  ? 24  GLU   A N   1 
ATOM   161  C CA  . GLU   A 1 24  ? 25.093 -11.609 -31.393 1.00 40.35  ? 24  GLU   A CA  1 
ATOM   162  C C   . GLU   A 1 24  ? 23.659 -11.120 -31.531 1.00 43.76  ? 24  GLU   A C   1 
ATOM   163  O O   . GLU   A 1 24  ? 23.384 -10.376 -32.467 1.00 44.53  ? 24  GLU   A O   1 
ATOM   164  C CB  . GLU   A 1 24  ? 25.248 -13.026 -31.974 1.00 41.47  ? 24  GLU   A CB  1 
ATOM   165  C CG  . GLU   A 1 24  ? 26.696 -13.400 -32.268 1.00 56.61  ? 24  GLU   A CG  1 
ATOM   166  C CD  . GLU   A 1 24  ? 27.523 -12.373 -33.032 1.00 81.73  ? 24  GLU   A CD  1 
ATOM   167  O OE1 . GLU   A 1 24  ? 28.533 -11.883 -32.473 1.00 71.22  ? 24  GLU   A OE1 1 
ATOM   168  O OE2 . GLU   A 1 24  ? 27.156 -12.052 -34.187 1.00 75.31  ? 24  GLU   A OE2 1 
ATOM   169  N N   . LEU   A 1 25  ? 22.763 -11.501 -30.593 1.00 39.85  ? 25  LEU   A N   1 
ATOM   170  C CA  . LEU   A 1 25  ? 21.354 -11.069 -30.573 1.00 40.20  ? 25  LEU   A CA  1 
ATOM   171  C C   . LEU   A 1 25  ? 21.207 -9.566  -30.335 1.00 42.76  ? 25  LEU   A C   1 
ATOM   172  O O   . LEU   A 1 25  ? 20.327 -8.951  -30.924 1.00 41.78  ? 25  LEU   A O   1 
ATOM   173  C CB  . LEU   A 1 25  ? 20.546 -11.815 -29.507 1.00 40.79  ? 25  LEU   A CB  1 
ATOM   174  C CG  . LEU   A 1 25  ? 20.222 -13.273 -29.775 1.00 45.19  ? 25  LEU   A CG  1 
ATOM   175  C CD1 . LEU   A 1 25  ? 19.606 -13.900 -28.567 1.00 44.21  ? 25  LEU   A CD1 1 
ATOM   176  C CD2 . LEU   A 1 25  ? 19.280 -13.420 -30.953 1.00 49.41  ? 25  LEU   A CD2 1 
ATOM   177  N N   . ILE   A 1 26  ? 22.061 -8.983  -29.468 1.00 38.52  ? 26  ILE   A N   1 
ATOM   178  C CA  . ILE   A 1 26  ? 22.073 -7.549  -29.166 1.00 37.01  ? 26  ILE   A CA  1 
ATOM   179  C C   . ILE   A 1 26  ? 22.472 -6.817  -30.460 1.00 39.59  ? 26  ILE   A C   1 
ATOM   180  O O   . ILE   A 1 26  ? 21.798 -5.869  -30.859 1.00 39.27  ? 26  ILE   A O   1 
ATOM   181  C CB  . ILE   A 1 26  ? 23.035 -7.227  -27.966 1.00 39.11  ? 26  ILE   A CB  1 
ATOM   182  C CG1 . ILE   A 1 26  ? 22.501 -7.811  -26.643 1.00 38.22  ? 26  ILE   A CG1 1 
ATOM   183  C CG2 . ILE   A 1 26  ? 23.359 -5.719  -27.831 1.00 38.68  ? 26  ILE   A CG2 1 
ATOM   184  C CD1 . ILE   A 1 26  ? 23.583 -8.084  -25.655 1.00 34.36  ? 26  ILE   A CD1 1 
ATOM   185  N N   . LYS   A 1 27  ? 23.544 -7.275  -31.117 1.00 35.12  ? 27  LYS   A N   1 
ATOM   186  C CA  . LYS   A 1 27  ? 24.032 -6.672  -32.353 1.00 35.22  ? 27  LYS   A CA  1 
ATOM   187  C C   . LYS   A 1 27  ? 22.999 -6.694  -33.468 1.00 42.15  ? 27  LYS   A C   1 
ATOM   188  O O   . LYS   A 1 27  ? 22.740 -5.665  -34.073 1.00 42.68  ? 27  LYS   A O   1 
ATOM   189  C CB  . LYS   A 1 27  ? 25.314 -7.357  -32.796 1.00 36.80  ? 27  LYS   A CB  1 
ATOM   190  C CG  . LYS   A 1 27  ? 26.521 -6.836  -32.057 1.00 34.49  ? 27  LYS   A CG  1 
ATOM   191  C CD  . LYS   A 1 27  ? 27.656 -7.811  -32.024 1.00 38.95  ? 27  LYS   A CD  1 
ATOM   192  C CE  . LYS   A 1 27  ? 28.169 -8.180  -33.378 1.00 40.57  ? 27  LYS   A CE  1 
ATOM   193  N NZ  . LYS   A 1 27  ? 29.415 -8.966  -33.281 1.00 47.64  ? 27  LYS   A NZ  1 
ATOM   194  N N   . GLU   A 1 28  ? 22.391 -7.854  -33.700 1.00 41.05  ? 28  GLU   A N   1 
ATOM   195  C CA  . GLU   A 1 28  ? 21.382 -8.130  -34.716 1.00 42.11  ? 28  GLU   A CA  1 
ATOM   196  C C   . GLU   A 1 28  ? 20.039 -7.422  -34.501 1.00 45.53  ? 28  GLU   A C   1 
ATOM   197  O O   . GLU   A 1 28  ? 19.504 -6.847  -35.446 1.00 45.29  ? 28  GLU   A O   1 
ATOM   198  C CB  . GLU   A 1 28  ? 21.160 -9.670  -34.803 1.00 44.05  ? 28  GLU   A CB  1 
ATOM   199  C CG  . GLU   A 1 28  ? 20.134 -10.128 -35.839 1.00 58.22  ? 28  GLU   A CG  1 
ATOM   200  C CD  . GLU   A 1 28  ? 19.420 -11.446 -35.581 1.00 92.05  ? 28  GLU   A CD  1 
ATOM   201  O OE1 . GLU   A 1 28  ? 19.971 -12.305 -34.852 1.00 89.83  ? 28  GLU   A OE1 1 
ATOM   202  O OE2 . GLU   A 1 28  ? 18.301 -11.618 -36.119 1.00 91.53  ? 28  GLU   A OE2 1 
ATOM   203  N N   . LYS   A 1 29  ? 19.475 -7.517  -33.285 1.00 41.14  ? 29  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 29  ? 18.155 -6.993  -32.937 1.00 39.78  ? 29  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 29  ? 18.102 -5.572  -32.425 1.00 44.48  ? 29  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 29  ? 17.122 -4.868  -32.701 1.00 43.44  ? 29  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 29  ? 17.473 -7.919  -31.899 1.00 40.95  ? 29  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 29  ? 17.378 -9.388  -32.314 1.00 50.40  ? 29  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 29  ? 15.961 -9.943  -32.178 1.00 67.39  ? 29  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 29  ? 15.643 -10.996 -33.226 1.00 84.79  ? 29  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 29  ? 15.661 -10.455 -34.623 1.00 86.92  ? 29  LYS   A NZ  1 
ATOM   212  N N   . LEU   A 1 30  ? 19.125 -5.152  -31.644 1.00 41.28  ? 30  LEU   A N   1 
ATOM   213  C CA  . LEU   A 1 30  ? 19.147 -3.842  -30.990 1.00 40.08  ? 30  LEU   A CA  1 
ATOM   214  C C   . LEU   A 1 30  ? 20.103 -2.789  -31.531 1.00 42.25  ? 30  LEU   A C   1 
ATOM   215  O O   . LEU   A 1 30  ? 19.757 -1.606  -31.518 1.00 41.63  ? 30  LEU   A O   1 
ATOM   216  C CB  . LEU   A 1 30  ? 19.424 -4.058  -29.489 1.00 39.96  ? 30  LEU   A CB  1 
ATOM   217  C CG  . LEU   A 1 30  ? 18.299 -4.458  -28.492 1.00 44.62  ? 30  LEU   A CG  1 
ATOM   218  C CD1 . LEU   A 1 30  ? 17.159 -5.234  -29.103 1.00 45.22  ? 30  LEU   A CD1 1 
ATOM   219  C CD2 . LEU   A 1 30  ? 18.861 -5.260  -27.386 1.00 46.36  ? 30  LEU   A CD2 1 
ATOM   220  N N   . ILE   A 1 31  ? 21.308 -3.190  -31.957 1.00 37.68  ? 31  ILE   A N   1 
ATOM   221  C CA  . ILE   A 1 31  ? 22.312 -2.231  -32.424 1.00 36.76  ? 31  ILE   A CA  1 
ATOM   222  C C   . ILE   A 1 31  ? 22.303 -1.985  -33.927 1.00 41.65  ? 31  ILE   A C   1 
ATOM   223  O O   . ILE   A 1 31  ? 22.063 -0.842  -34.344 1.00 40.23  ? 31  ILE   A O   1 
ATOM   224  C CB  . ILE   A 1 31  ? 23.745 -2.549  -31.900 1.00 38.88  ? 31  ILE   A CB  1 
ATOM   225  C CG1 . ILE   A 1 31  ? 23.816 -2.806  -30.364 1.00 38.21  ? 31  ILE   A CG1 1 
ATOM   226  C CG2 . ILE   A 1 31  ? 24.789 -1.519  -32.414 1.00 38.65  ? 31  ILE   A CG2 1 
ATOM   227  C CD1 . ILE   A 1 31  ? 23.476 -1.618  -29.402 1.00 41.72  ? 31  ILE   A CD1 1 
ATOM   228  N N   . PHE   A 1 32  ? 22.598 -3.054  -34.737 1.00 37.71  ? 32  PHE   A N   1 
ATOM   229  C CA  . PHE   A 1 32  ? 22.669 -2.988  -36.205 1.00 36.35  ? 32  PHE   A CA  1 
ATOM   230  C C   . PHE   A 1 32  ? 21.432 -2.417  -36.943 1.00 41.20  ? 32  PHE   A C   1 
ATOM   231  O O   . PHE   A 1 32  ? 21.635 -1.683  -37.923 1.00 40.72  ? 32  PHE   A O   1 
ATOM   232  C CB  . PHE   A 1 32  ? 23.165 -4.300  -36.831 1.00 36.94  ? 32  PHE   A CB  1 
ATOM   233  C CG  . PHE   A 1 32  ? 24.591 -4.724  -36.536 1.00 37.91  ? 32  PHE   A CG  1 
ATOM   234  C CD1 . PHE   A 1 32  ? 24.991 -6.052  -36.710 1.00 41.50  ? 32  PHE   A CD1 1 
ATOM   235  C CD2 . PHE   A 1 32  ? 25.535 -3.804  -36.080 1.00 38.46  ? 32  PHE   A CD2 1 
ATOM   236  C CE1 . PHE   A 1 32  ? 26.317 -6.442  -36.463 1.00 41.68  ? 32  PHE   A CE1 1 
ATOM   237  C CE2 . PHE   A 1 32  ? 26.854 -4.198  -35.811 1.00 40.99  ? 32  PHE   A CE2 1 
ATOM   238  C CZ  . PHE   A 1 32  ? 27.241 -5.508  -36.020 1.00 39.77  ? 32  PHE   A CZ  1 
ATOM   239  N N   . PRO   A 1 33  ? 20.160 -2.686  -36.519 1.00 38.50  ? 33  PRO   A N   1 
ATOM   240  C CA  . PRO   A 1 33  ? 19.014 -2.100  -37.254 1.00 38.40  ? 33  PRO   A CA  1 
ATOM   241  C C   . PRO   A 1 33  ? 18.915 -0.568  -37.197 1.00 45.13  ? 33  PRO   A C   1 
ATOM   242  O O   . PRO   A 1 33  ? 18.109 0.005   -37.939 1.00 47.36  ? 33  PRO   A O   1 
ATOM   243  C CB  . PRO   A 1 33  ? 17.787 -2.746  -36.598 1.00 39.30  ? 33  PRO   A CB  1 
ATOM   244  C CG  . PRO   A 1 33  ? 18.298 -3.874  -35.800 1.00 43.00  ? 33  PRO   A CG  1 
ATOM   245  C CD  . PRO   A 1 33  ? 19.690 -3.534  -35.403 1.00 38.98  ? 33  PRO   A CD  1 
ATOM   246  N N   . TYR   A 1 34  ? 19.735 0.095   -36.345 1.00 39.52  ? 34  TYR   A N   1 
ATOM   247  C CA  . TYR   A 1 34  ? 19.711 1.548   -36.164 1.00 38.32  ? 34  TYR   A CA  1 
ATOM   248  C C   . TYR   A 1 34  ? 21.063 2.255   -36.282 1.00 43.53  ? 34  TYR   A C   1 
ATOM   249  O O   . TYR   A 1 34  ? 21.100 3.469   -36.522 1.00 44.33  ? 34  TYR   A O   1 
ATOM   250  C CB  . TYR   A 1 34  ? 19.090 1.889   -34.786 1.00 38.19  ? 34  TYR   A CB  1 
ATOM   251  C CG  . TYR   A 1 34  ? 17.762 1.207   -34.556 1.00 38.94  ? 34  TYR   A CG  1 
ATOM   252  C CD1 . TYR   A 1 34  ? 17.656 0.114   -33.700 1.00 40.79  ? 34  TYR   A CD1 1 
ATOM   253  C CD2 . TYR   A 1 34  ? 16.624 1.598   -35.260 1.00 39.55  ? 34  TYR   A CD2 1 
ATOM   254  C CE1 . TYR   A 1 34  ? 16.439 -0.554  -33.522 1.00 41.00  ? 34  TYR   A CE1 1 
ATOM   255  C CE2 . TYR   A 1 34  ? 15.405 0.941   -35.090 1.00 40.35  ? 34  TYR   A CE2 1 
ATOM   256  C CZ  . TYR   A 1 34  ? 15.316 -0.132  -34.216 1.00 46.79  ? 34  TYR   A CZ  1 
ATOM   257  O OH  . TYR   A 1 34  ? 14.112 -0.774  -34.063 1.00 49.70  ? 34  TYR   A OH  1 
ATOM   258  N N   . VAL   A 1 35  ? 22.166 1.532   -36.059 1.00 39.00  ? 35  VAL   A N   1 
ATOM   259  C CA  . VAL   A 1 35  ? 23.484 2.156   -36.080 1.00 37.66  ? 35  VAL   A CA  1 
ATOM   260  C C   . VAL   A 1 35  ? 24.449 1.479   -37.035 1.00 43.83  ? 35  VAL   A C   1 
ATOM   261  O O   . VAL   A 1 35  ? 24.573 0.252   -37.041 1.00 44.55  ? 35  VAL   A O   1 
ATOM   262  C CB  . VAL   A 1 35  ? 24.105 2.300   -34.647 1.00 39.10  ? 35  VAL   A CB  1 
ATOM   263  C CG1 . VAL   A 1 35  ? 25.287 3.264   -34.657 1.00 39.48  ? 35  VAL   A CG1 1 
ATOM   264  C CG2 . VAL   A 1 35  ? 23.080 2.767   -33.618 1.00 37.92  ? 35  VAL   A CG2 1 
ATOM   265  N N   . GLU   A 1 36  ? 25.153 2.297   -37.825 1.00 40.48  ? 36  GLU   A N   1 
ATOM   266  C CA  . GLU   A 1 36  ? 26.209 1.843   -38.728 1.00 39.23  ? 36  GLU   A CA  1 
ATOM   267  C C   . GLU   A 1 36  ? 27.497 2.175   -37.983 1.00 42.03  ? 36  GLU   A C   1 
ATOM   268  O O   . GLU   A 1 36  ? 27.641 3.283   -37.456 1.00 42.19  ? 36  GLU   A O   1 
ATOM   269  C CB  . GLU   A 1 36  ? 26.153 2.561   -40.098 1.00 40.06  ? 36  GLU   A CB  1 
ATOM   270  C CG  . GLU   A 1 36  ? 24.973 2.144   -40.964 1.00 49.99  ? 36  GLU   A CG  1 
ATOM   271  C CD  . GLU   A 1 36  ? 24.905 0.732   -41.533 1.00 66.98  ? 36  GLU   A CD  1 
ATOM   272  O OE1 . GLU   A 1 36  ? 24.011 0.489   -42.380 1.00 68.31  ? 36  GLU   A OE1 1 
ATOM   273  O OE2 . GLU   A 1 36  ? 25.726 -0.130  -41.138 1.00 45.86  ? 36  GLU   A OE2 1 
ATOM   274  N N   . LEU   A 1 37  ? 28.417 1.227   -37.899 1.00 37.31  ? 37  LEU   A N   1 
ATOM   275  C CA  . LEU   A 1 37  ? 29.661 1.495   -37.179 1.00 36.33  ? 37  LEU   A CA  1 
ATOM   276  C C   . LEU   A 1 37  ? 30.885 1.148   -37.999 1.00 39.11  ? 37  LEU   A C   1 
ATOM   277  O O   . LEU   A 1 37  ? 30.828 0.243   -38.826 1.00 37.34  ? 37  LEU   A O   1 
ATOM   278  C CB  . LEU   A 1 37  ? 29.712 0.672   -35.854 1.00 35.42  ? 37  LEU   A CB  1 
ATOM   279  C CG  . LEU   A 1 37  ? 28.684 0.968   -34.773 1.00 37.94  ? 37  LEU   A CG  1 
ATOM   280  C CD1 . LEU   A 1 37  ? 28.574 -0.186  -33.805 1.00 36.61  ? 37  LEU   A CD1 1 
ATOM   281  C CD2 . LEU   A 1 37  ? 28.985 2.279   -34.051 1.00 37.38  ? 37  LEU   A CD2 1 
ATOM   282  N N   . ASP   A 1 38  ? 32.007 1.837   -37.730 1.00 36.78  ? 38  ASP   A N   1 
ATOM   283  C CA  . ASP   A 1 38  ? 33.311 1.530   -38.325 1.00 37.60  ? 38  ASP   A CA  1 
ATOM   284  C C   . ASP   A 1 38  ? 33.819 0.535   -37.292 1.00 42.08  ? 38  ASP   A C   1 
ATOM   285  O O   . ASP   A 1 38  ? 34.494 0.891   -36.314 1.00 41.44  ? 38  ASP   A O   1 
ATOM   286  C CB  . ASP   A 1 38  ? 34.210 2.782   -38.428 1.00 39.54  ? 38  ASP   A CB  1 
ATOM   287  C CG  . ASP   A 1 38  ? 33.722 3.760   -39.476 1.00 47.10  ? 38  ASP   A CG  1 
ATOM   288  O OD1 . ASP   A 1 38  ? 33.119 3.302   -40.489 1.00 45.34  ? 38  ASP   A OD1 1 
ATOM   289  O OD2 . ASP   A 1 38  ? 33.930 4.973   -39.288 1.00 52.95  ? 38  ASP   A OD2 1 
ATOM   290  N N   . LEU   A 1 39  ? 33.377 -0.711  -37.477 1.00 38.25  ? 39  LEU   A N   1 
ATOM   291  C CA  . LEU   A 1 39  ? 33.613 -1.812  -36.574 1.00 37.05  ? 39  LEU   A CA  1 
ATOM   292  C C   . LEU   A 1 39  ? 34.960 -2.520  -36.623 1.00 36.71  ? 39  LEU   A C   1 
ATOM   293  O O   . LEU   A 1 39  ? 35.323 -3.157  -37.617 1.00 33.58  ? 39  LEU   A O   1 
ATOM   294  C CB  . LEU   A 1 39  ? 32.428 -2.781  -36.646 1.00 37.31  ? 39  LEU   A CB  1 
ATOM   295  C CG  . LEU   A 1 39  ? 32.017 -3.456  -35.347 1.00 42.43  ? 39  LEU   A CG  1 
ATOM   296  C CD1 . LEU   A 1 39  ? 31.586 -2.446  -34.287 1.00 42.37  ? 39  LEU   A CD1 1 
ATOM   297  C CD2 . LEU   A 1 39  ? 30.953 -4.495  -35.600 1.00 43.89  ? 39  LEU   A CD2 1 
ATOM   298  N N   . HIS   A 1 40  ? 35.679 -2.403  -35.502 1.00 32.89  ? 40  HIS   A N   1 
ATOM   299  C CA  . HIS   A 1 40  ? 36.963 -3.017  -35.227 1.00 33.02  ? 40  HIS   A CA  1 
ATOM   300  C C   . HIS   A 1 40  ? 36.623 -4.217  -34.338 1.00 37.26  ? 40  HIS   A C   1 
ATOM   301  O O   . HIS   A 1 40  ? 36.622 -4.096  -33.107 1.00 35.73  ? 40  HIS   A O   1 
ATOM   302  C CB  . HIS   A 1 40  ? 37.874 -2.017  -34.489 1.00 34.48  ? 40  HIS   A CB  1 
ATOM   303  C CG  . HIS   A 1 40  ? 38.170 -0.795  -35.297 1.00 37.99  ? 40  HIS   A CG  1 
ATOM   304  N ND1 . HIS   A 1 40  ? 37.540 0.402   -35.045 1.00 40.00  ? 40  HIS   A ND1 1 
ATOM   305  C CD2 . HIS   A 1 40  ? 38.985 -0.644  -36.364 1.00 39.39  ? 40  HIS   A CD2 1 
ATOM   306  C CE1 . HIS   A 1 40  ? 37.989 1.247   -35.965 1.00 39.20  ? 40  HIS   A CE1 1 
ATOM   307  N NE2 . HIS   A 1 40  ? 38.875 0.663   -36.769 1.00 39.31  ? 40  HIS   A NE2 1 
ATOM   308  N N   . SER   A 1 41  ? 36.263 -5.359  -34.979 1.00 35.44  ? 41  SER   A N   1 
ATOM   309  C CA  . SER   A 1 41  ? 35.879 -6.610  -34.305 1.00 35.84  ? 41  SER   A CA  1 
ATOM   310  C C   . SER   A 1 41  ? 37.040 -7.548  -34.102 1.00 38.18  ? 41  SER   A C   1 
ATOM   311  O O   . SER   A 1 41  ? 37.774 -7.836  -35.039 1.00 37.48  ? 41  SER   A O   1 
ATOM   312  C CB  . SER   A 1 41  ? 34.758 -7.347  -35.038 1.00 37.56  ? 41  SER   A CB  1 
ATOM   313  O OG  . SER   A 1 41  ? 33.658 -6.495  -35.289 1.00 49.44  ? 41  SER   A OG  1 
ATOM   314  N N   . TYR   A 1 42  ? 37.178 -8.038  -32.870 1.00 35.05  ? 42  TYR   A N   1 
ATOM   315  C CA  . TYR   A 1 42  ? 38.213 -8.983  -32.435 1.00 34.15  ? 42  TYR   A CA  1 
ATOM   316  C C   . TYR   A 1 42  ? 37.480 -10.123 -31.774 1.00 37.73  ? 42  TYR   A C   1 
ATOM   317  O O   . TYR   A 1 42  ? 36.560 -9.889  -31.008 1.00 38.59  ? 42  TYR   A O   1 
ATOM   318  C CB  . TYR   A 1 42  ? 39.241 -8.294  -31.507 1.00 34.21  ? 42  TYR   A CB  1 
ATOM   319  C CG  . TYR   A 1 42  ? 39.963 -7.177  -32.230 1.00 33.11  ? 42  TYR   A CG  1 
ATOM   320  C CD1 . TYR   A 1 42  ? 39.432 -5.890  -32.273 1.00 34.76  ? 42  TYR   A CD1 1 
ATOM   321  C CD2 . TYR   A 1 42  ? 41.153 -7.416  -32.917 1.00 32.05  ? 42  TYR   A CD2 1 
ATOM   322  C CE1 . TYR   A 1 42  ? 40.063 -4.868  -32.982 1.00 34.74  ? 42  TYR   A CE1 1 
ATOM   323  C CE2 . TYR   A 1 42  ? 41.789 -6.401  -33.637 1.00 31.79  ? 42  TYR   A CE2 1 
ATOM   324  C CZ  . TYR   A 1 42  ? 41.237 -5.126  -33.670 1.00 39.26  ? 42  TYR   A CZ  1 
ATOM   325  O OH  . TYR   A 1 42  ? 41.839 -4.095  -34.369 1.00 40.14  ? 42  TYR   A OH  1 
ATOM   326  N N   . ASP   A 1 43  ? 37.801 -11.346 -32.159 1.00 35.14  ? 43  ASP   A N   1 
ATOM   327  C CA  . ASP   A 1 43  ? 37.148 -12.530 -31.633 1.00 36.09  ? 43  ASP   A CA  1 
ATOM   328  C C   . ASP   A 1 43  ? 37.931 -13.020 -30.405 1.00 42.25  ? 43  ASP   A C   1 
ATOM   329  O O   . ASP   A 1 43  ? 39.016 -13.615 -30.548 1.00 43.45  ? 43  ASP   A O   1 
ATOM   330  C CB  . ASP   A 1 43  ? 37.025 -13.618 -32.731 1.00 37.52  ? 43  ASP   A CB  1 
ATOM   331  C CG  . ASP   A 1 43  ? 36.247 -14.873 -32.321 1.00 45.96  ? 43  ASP   A CG  1 
ATOM   332  O OD1 . ASP   A 1 43  ? 36.043 -15.085 -31.089 1.00 45.32  ? 43  ASP   A OD1 1 
ATOM   333  O OD2 . ASP   A 1 43  ? 35.856 -15.652 -33.226 1.00 49.31  ? 43  ASP   A OD2 1 
ATOM   334  N N   . LEU   A 1 44  ? 37.401 -12.738 -29.199 1.00 37.03  ? 44  LEU   A N   1 
ATOM   335  C CA  . LEU   A 1 44  ? 38.103 -13.164 -27.992 1.00 36.55  ? 44  LEU   A CA  1 
ATOM   336  C C   . LEU   A 1 44  ? 37.578 -14.493 -27.426 1.00 41.80  ? 44  LEU   A C   1 
ATOM   337  O O   . LEU   A 1 44  ? 37.741 -14.783 -26.244 1.00 41.29  ? 44  LEU   A O   1 
ATOM   338  C CB  . LEU   A 1 44  ? 38.306 -12.054 -26.913 1.00 35.56  ? 44  LEU   A CB  1 
ATOM   339  C CG  . LEU   A 1 44  ? 38.945 -10.703 -27.304 1.00 37.36  ? 44  LEU   A CG  1 
ATOM   340  C CD1 . LEU   A 1 44  ? 39.290 -9.903  -26.078 1.00 36.21  ? 44  LEU   A CD1 1 
ATOM   341  C CD2 . LEU   A 1 44  ? 40.165 -10.863 -28.193 1.00 36.33  ? 44  LEU   A CD2 1 
ATOM   342  N N   . GLY   A 1 45  ? 36.994 -15.307 -28.300 1.00 38.95  ? 45  GLY   A N   1 
ATOM   343  C CA  . GLY   A 1 45  ? 36.533 -16.636 -27.941 1.00 39.02  ? 45  GLY   A CA  1 
ATOM   344  C C   . GLY   A 1 45  ? 37.762 -17.443 -27.566 1.00 44.92  ? 45  GLY   A C   1 
ATOM   345  O O   . GLY   A 1 45  ? 38.854 -17.178 -28.086 1.00 44.91  ? 45  GLY   A O   1 
ATOM   346  N N   . ILE   A 1 46  ? 37.616 -18.396 -26.631 1.00 42.05  ? 46  ILE   A N   1 
ATOM   347  C CA  . ILE   A 1 46  ? 38.737 -19.218 -26.148 1.00 41.08  ? 46  ILE   A CA  1 
ATOM   348  C C   . ILE   A 1 46  ? 39.540 -19.878 -27.279 1.00 44.00  ? 46  ILE   A C   1 
ATOM   349  O O   . ILE   A 1 46  ? 40.770 -19.760 -27.317 1.00 43.71  ? 46  ILE   A O   1 
ATOM   350  C CB  . ILE   A 1 46  ? 38.312 -20.185 -24.987 1.00 43.51  ? 46  ILE   A CB  1 
ATOM   351  C CG1 . ILE   A 1 46  ? 39.522 -20.796 -24.238 1.00 43.69  ? 46  ILE   A CG1 1 
ATOM   352  C CG2 . ILE   A 1 46  ? 37.291 -21.250 -25.429 1.00 41.85  ? 46  ILE   A CG2 1 
ATOM   353  C CD1 . ILE   A 1 46  ? 40.346 -19.834 -23.385 1.00 49.78  ? 46  ILE   A CD1 1 
ATOM   354  N N   . GLU   A 1 47  ? 38.829 -20.530 -28.205 1.00 40.22  ? 47  GLU   A N   1 
ATOM   355  C CA  . GLU   A 1 47  ? 39.383 -21.234 -29.362 1.00 39.70  ? 47  GLU   A CA  1 
ATOM   356  C C   . GLU   A 1 47  ? 40.236 -20.292 -30.223 1.00 45.65  ? 47  GLU   A C   1 
ATOM   357  O O   . GLU   A 1 47  ? 41.331 -20.683 -30.639 1.00 46.30  ? 47  GLU   A O   1 
ATOM   358  C CB  . GLU   A 1 47  ? 38.259 -21.875 -30.211 1.00 40.45  ? 47  GLU   A CB  1 
ATOM   359  C CG  . GLU   A 1 47  ? 37.301 -22.789 -29.455 1.00 44.07  ? 47  GLU   A CG  1 
ATOM   360  C CD  . GLU   A 1 47  ? 35.946 -22.197 -29.087 1.00 72.28  ? 47  GLU   A CD  1 
ATOM   361  O OE1 . GLU   A 1 47  ? 34.965 -22.976 -29.047 1.00 61.97  ? 47  GLU   A OE1 1 
ATOM   362  O OE2 . GLU   A 1 47  ? 35.857 -20.969 -28.839 1.00 66.07  ? 47  GLU   A OE2 1 
ATOM   363  N N   . ASN   A 1 48  ? 39.748 -19.046 -30.472 1.00 41.92  ? 48  ASN   A N   1 
ATOM   364  C CA  . ASN   A 1 48  ? 40.481 -18.067 -31.274 1.00 40.70  ? 48  ASN   A CA  1 
ATOM   365  C C   . ASN   A 1 48  ? 41.717 -17.553 -30.582 1.00 43.77  ? 48  ASN   A C   1 
ATOM   366  O O   . ASN   A 1 48  ? 42.748 -17.378 -31.229 1.00 45.42  ? 48  ASN   A O   1 
ATOM   367  C CB  . ASN   A 1 48  ? 39.602 -16.929 -31.775 1.00 39.53  ? 48  ASN   A CB  1 
ATOM   368  C CG  . ASN   A 1 48  ? 40.306 -16.130 -32.846 1.00 46.79  ? 48  ASN   A CG  1 
ATOM   369  O OD1 . ASN   A 1 48  ? 40.798 -16.682 -33.817 1.00 34.91  ? 48  ASN   A OD1 1 
ATOM   370  N ND2 . ASN   A 1 48  ? 40.411 -14.827 -32.676 1.00 36.78  ? 48  ASN   A ND2 1 
ATOM   371  N N   . ARG   A 1 49  ? 41.629 -17.316 -29.275 1.00 38.60  ? 49  ARG   A N   1 
ATOM   372  C CA  . ARG   A 1 49  ? 42.762 -16.869 -28.469 1.00 38.24  ? 49  ARG   A CA  1 
ATOM   373  C C   . ARG   A 1 49  ? 43.852 -17.964 -28.489 1.00 43.23  ? 49  ARG   A C   1 
ATOM   374  O O   . ARG   A 1 49  ? 45.032 -17.650 -28.633 1.00 43.76  ? 49  ARG   A O   1 
ATOM   375  C CB  . ARG   A 1 49  ? 42.316 -16.570 -27.030 1.00 36.09  ? 49  ARG   A CB  1 
ATOM   376  C CG  . ARG   A 1 49  ? 41.717 -15.188 -26.845 1.00 36.12  ? 49  ARG   A CG  1 
ATOM   377  C CD  . ARG   A 1 49  ? 41.334 -14.945 -25.396 1.00 44.43  ? 49  ARG   A CD  1 
ATOM   378  N NE  . ARG   A 1 49  ? 40.053 -15.569 -25.047 1.00 50.11  ? 49  ARG   A NE  1 
ATOM   379  C CZ  . ARG   A 1 49  ? 39.793 -16.169 -23.889 1.00 56.93  ? 49  ARG   A CZ  1 
ATOM   380  N NH1 . ARG   A 1 49  ? 40.729 -16.255 -22.952 1.00 39.80  ? 49  ARG   A NH1 1 
ATOM   381  N NH2 . ARG   A 1 49  ? 38.596 -16.697 -23.663 1.00 40.85  ? 49  ARG   A NH2 1 
ATOM   382  N N   . ASP   A 1 50  ? 43.442 -19.242 -28.389 1.00 39.20  ? 50  ASP   A N   1 
ATOM   383  C CA  . ASP   A 1 50  ? 44.350 -20.380 -28.441 1.00 39.39  ? 50  ASP   A CA  1 
ATOM   384  C C   . ASP   A 1 50  ? 45.048 -20.443 -29.819 1.00 44.14  ? 50  ASP   A C   1 
ATOM   385  O O   . ASP   A 1 50  ? 46.287 -20.422 -29.882 1.00 44.84  ? 50  ASP   A O   1 
ATOM   386  C CB  . ASP   A 1 50  ? 43.589 -21.680 -28.164 1.00 40.81  ? 50  ASP   A CB  1 
ATOM   387  C CG  . ASP   A 1 50  ? 44.485 -22.852 -27.830 1.00 50.41  ? 50  ASP   A CG  1 
ATOM   388  O OD1 . ASP   A 1 50  ? 45.298 -22.728 -26.877 1.00 49.62  ? 50  ASP   A OD1 1 
ATOM   389  O OD2 . ASP   A 1 50  ? 44.369 -23.899 -28.512 1.00 56.48  ? 50  ASP   A OD2 1 
ATOM   390  N N   . ALA   A 1 51  ? 44.251 -20.478 -30.911 1.00 38.28  ? 51  ALA   A N   1 
ATOM   391  C CA  . ALA   A 1 51  ? 44.742 -20.528 -32.287 1.00 37.33  ? 51  ALA   A CA  1 
ATOM   392  C C   . ALA   A 1 51  ? 45.732 -19.388 -32.629 1.00 41.95  ? 51  ALA   A C   1 
ATOM   393  O O   . ALA   A 1 51  ? 46.704 -19.623 -33.340 1.00 40.83  ? 51  ALA   A O   1 
ATOM   394  C CB  . ALA   A 1 51  ? 43.575 -20.522 -33.256 1.00 37.50  ? 51  ALA   A CB  1 
ATOM   395  N N   . THR   A 1 52  ? 45.507 -18.175 -32.101 1.00 39.06  ? 52  THR   A N   1 
ATOM   396  C CA  . THR   A 1 52  ? 46.377 -17.034 -32.379 1.00 38.32  ? 52  THR   A CA  1 
ATOM   397  C C   . THR   A 1 52  ? 47.442 -16.816 -31.296 1.00 44.87  ? 52  THR   A C   1 
ATOM   398  O O   . THR   A 1 52  ? 48.124 -15.787 -31.314 1.00 46.62  ? 52  THR   A O   1 
ATOM   399  C CB  . THR   A 1 52  ? 45.529 -15.756 -32.588 1.00 36.59  ? 52  THR   A CB  1 
ATOM   400  O OG1 . THR   A 1 52  ? 45.049 -15.293 -31.327 1.00 35.43  ? 52  THR   A OG1 1 
ATOM   401  C CG2 . THR   A 1 52  ? 44.377 -15.929 -33.599 1.00 24.83  ? 52  THR   A CG2 1 
ATOM   402  N N   . ASN   A 1 53  ? 47.570 -17.757 -30.344 1.00 41.34  ? 53  ASN   A N   1 
ATOM   403  C CA  . ASN   A 1 53  ? 48.505 -17.693 -29.210 1.00 40.61  ? 53  ASN   A CA  1 
ATOM   404  C C   . ASN   A 1 53  ? 48.326 -16.408 -28.411 1.00 43.47  ? 53  ASN   A C   1 
ATOM   405  O O   . ASN   A 1 53  ? 49.304 -15.758 -28.019 1.00 43.76  ? 53  ASN   A O   1 
ATOM   406  C CB  . ASN   A 1 53  ? 49.967 -17.950 -29.632 1.00 39.50  ? 53  ASN   A CB  1 
ATOM   407  C CG  . ASN   A 1 53  ? 50.190 -19.344 -30.180 1.00 59.29  ? 53  ASN   A CG  1 
ATOM   408  O OD1 . ASN   A 1 53  ? 50.036 -20.349 -29.483 1.00 63.74  ? 53  ASN   A OD1 1 
ATOM   409  N ND2 . ASN   A 1 53  ? 50.561 -19.441 -31.441 1.00 43.31  ? 53  ASN   A ND2 1 
ATOM   410  N N   . ASP   A 1 54  ? 47.051 -16.044 -28.178 1.00 39.42  ? 54  ASP   A N   1 
ATOM   411  C CA  . ASP   A 1 54  ? 46.632 -14.834 -27.445 1.00 39.83  ? 54  ASP   A CA  1 
ATOM   412  C C   . ASP   A 1 54  ? 47.020 -13.500 -28.137 1.00 41.78  ? 54  ASP   A C   1 
ATOM   413  O O   . ASP   A 1 54  ? 47.056 -12.467 -27.479 1.00 42.38  ? 54  ASP   A O   1 
ATOM   414  C CB  . ASP   A 1 54  ? 47.101 -14.863 -25.954 1.00 41.57  ? 54  ASP   A CB  1 
ATOM   415  C CG  . ASP   A 1 54  ? 46.102 -14.264 -24.983 1.00 48.83  ? 54  ASP   A CG  1 
ATOM   416  O OD1 . ASP   A 1 54  ? 44.882 -14.407 -25.221 1.00 49.82  ? 54  ASP   A OD1 1 
ATOM   417  O OD2 . ASP   A 1 54  ? 46.538 -13.646 -23.985 1.00 57.31  ? 54  ASP   A OD2 1 
ATOM   418  N N   . GLN   A 1 55  ? 47.306 -13.516 -29.449 1.00 36.76  ? 55  GLN   A N   1 
ATOM   419  C CA  . GLN   A 1 55  ? 47.672 -12.287 -30.147 1.00 35.85  ? 55  GLN   A CA  1 
ATOM   420  C C   . GLN   A 1 55  ? 46.457 -11.383 -30.327 1.00 40.69  ? 55  GLN   A C   1 
ATOM   421  O O   . GLN   A 1 55  ? 46.572 -10.160 -30.189 1.00 41.97  ? 55  GLN   A O   1 
ATOM   422  C CB  . GLN   A 1 55  ? 48.376 -12.580 -31.473 1.00 36.44  ? 55  GLN   A CB  1 
ATOM   423  C CG  . GLN   A 1 55  ? 48.974 -11.345 -32.118 1.00 39.26  ? 55  GLN   A CG  1 
ATOM   424  C CD  . GLN   A 1 55  ? 49.987 -10.672 -31.242 1.00 45.09  ? 55  GLN   A CD  1 
ATOM   425  O OE1 . GLN   A 1 55  ? 50.950 -11.286 -30.798 1.00 49.10  ? 55  GLN   A OE1 1 
ATOM   426  N NE2 . GLN   A 1 55  ? 49.793 -9.399  -30.967 1.00 35.37  ? 55  GLN   A NE2 1 
ATOM   427  N N   . VAL   A 1 56  ? 45.285 -12.005 -30.582 1.00 35.14  ? 56  VAL   A N   1 
ATOM   428  C CA  . VAL   A 1 56  ? 44.013 -11.327 -30.755 1.00 33.63  ? 56  VAL   A CA  1 
ATOM   429  C C   . VAL   A 1 56  ? 43.712 -10.421 -29.566 1.00 40.57  ? 56  VAL   A C   1 
ATOM   430  O O   . VAL   A 1 56  ? 43.277 -9.295  -29.782 1.00 42.12  ? 56  VAL   A O   1 
ATOM   431  C CB  . VAL   A 1 56  ? 42.880 -12.328 -31.110 1.00 36.58  ? 56  VAL   A CB  1 
ATOM   432  C CG1 . VAL   A 1 56  ? 42.575 -13.316 -29.968 1.00 35.66  ? 56  VAL   A CG1 1 
ATOM   433  C CG2 . VAL   A 1 56  ? 41.626 -11.613 -31.605 1.00 35.96  ? 56  VAL   A CG2 1 
ATOM   434  N N   . THR   A 1 57  ? 43.993 -10.884 -28.313 1.00 36.81  ? 57  THR   A N   1 
ATOM   435  C CA  . THR   A 1 57  ? 43.765 -10.094 -27.105 1.00 35.53  ? 57  THR   A CA  1 
ATOM   436  C C   . THR   A 1 57  ? 44.657 -8.864  -27.062 1.00 39.39  ? 57  THR   A C   1 
ATOM   437  O O   . THR   A 1 57  ? 44.161 -7.774  -26.760 1.00 39.63  ? 57  THR   A O   1 
ATOM   438  C CB  . THR   A 1 57  ? 43.921 -10.948 -25.843 1.00 38.44  ? 57  THR   A CB  1 
ATOM   439  O OG1 . THR   A 1 57  ? 43.113 -12.109 -25.961 1.00 37.31  ? 57  THR   A OG1 1 
ATOM   440  C CG2 . THR   A 1 57  ? 43.542 -10.188 -24.580 1.00 32.54  ? 57  THR   A CG2 1 
ATOM   441  N N   . LYS   A 1 58  ? 45.968 -9.029  -27.352 1.00 36.29  ? 58  LYS   A N   1 
ATOM   442  C CA  . LYS   A 1 58  ? 46.924 -7.910  -27.351 1.00 36.73  ? 58  LYS   A CA  1 
ATOM   443  C C   . LYS   A 1 58  ? 46.527 -6.854  -28.408 1.00 41.33  ? 58  LYS   A C   1 
ATOM   444  O O   . LYS   A 1 58  ? 46.552 -5.660  -28.104 1.00 42.10  ? 58  LYS   A O   1 
ATOM   445  C CB  . LYS   A 1 58  ? 48.372 -8.406  -27.533 1.00 40.43  ? 58  LYS   A CB  1 
ATOM   446  C CG  . LYS   A 1 58  ? 48.912 -9.263  -26.364 1.00 46.63  ? 58  LYS   A CG  1 
ATOM   447  C CD  . LYS   A 1 58  ? 50.338 -9.762  -26.641 1.00 48.42  ? 58  LYS   A CD  1 
ATOM   448  C CE  . LYS   A 1 58  ? 50.490 -11.261 -26.531 1.00 53.05  ? 58  LYS   A CE  1 
ATOM   449  N NZ  . LYS   A 1 58  ? 51.241 -11.850 -27.685 1.00 63.12  ? 58  LYS   A NZ  1 
ATOM   450  N N   . ASP   A 1 59  ? 46.086 -7.301  -29.616 1.00 36.68  ? 59  ASP   A N   1 
ATOM   451  C CA  . ASP   A 1 59  ? 45.629 -6.421  -30.695 1.00 36.18  ? 59  ASP   A CA  1 
ATOM   452  C C   . ASP   A 1 59  ? 44.357 -5.694  -30.322 1.00 39.76  ? 59  ASP   A C   1 
ATOM   453  O O   . ASP   A 1 59  ? 44.234 -4.503  -30.617 1.00 38.90  ? 59  ASP   A O   1 
ATOM   454  C CB  . ASP   A 1 59  ? 45.408 -7.200  -32.010 1.00 37.90  ? 59  ASP   A CB  1 
ATOM   455  C CG  . ASP   A 1 59  ? 46.665 -7.752  -32.650 1.00 45.41  ? 59  ASP   A CG  1 
ATOM   456  O OD1 . ASP   A 1 59  ? 47.775 -7.333  -32.246 1.00 47.79  ? 59  ASP   A OD1 1 
ATOM   457  O OD2 . ASP   A 1 59  ? 46.543 -8.604  -33.540 1.00 47.71  ? 59  ASP   A OD2 1 
ATOM   458  N N   . ALA   A 1 60  ? 43.406 -6.403  -29.686 1.00 37.23  ? 60  ALA   A N   1 
ATOM   459  C CA  . ALA   A 1 60  ? 42.133 -5.809  -29.257 1.00 37.75  ? 60  ALA   A CA  1 
ATOM   460  C C   . ALA   A 1 60  ? 42.383 -4.631  -28.331 1.00 40.59  ? 60  ALA   A C   1 
ATOM   461  O O   . ALA   A 1 60  ? 41.790 -3.579  -28.549 1.00 37.61  ? 60  ALA   A O   1 
ATOM   462  C CB  . ALA   A 1 60  ? 41.235 -6.845  -28.590 1.00 38.61  ? 60  ALA   A CB  1 
ATOM   463  N N   . ALA   A 1 61  ? 43.305 -4.789  -27.340 1.00 39.32  ? 61  ALA   A N   1 
ATOM   464  C CA  . ALA   A 1 61  ? 43.672 -3.724  -26.389 1.00 39.14  ? 61  ALA   A CA  1 
ATOM   465  C C   . ALA   A 1 61  ? 44.392 -2.579  -27.108 1.00 44.39  ? 61  ALA   A C   1 
ATOM   466  O O   . ALA   A 1 61  ? 44.122 -1.416  -26.806 1.00 45.61  ? 61  ALA   A O   1 
ATOM   467  C CB  . ALA   A 1 61  ? 44.529 -4.280  -25.256 1.00 39.43  ? 61  ALA   A CB  1 
ATOM   468  N N   . GLU   A 1 62  ? 45.279 -2.909  -28.073 1.00 40.89  ? 62  GLU   A N   1 
ATOM   469  C CA  . GLU   A 1 62  ? 46.030 -1.967  -28.913 1.00 40.98  ? 62  GLU   A CA  1 
ATOM   470  C C   . GLU   A 1 62  ? 45.013 -1.085  -29.666 1.00 44.63  ? 62  GLU   A C   1 
ATOM   471  O O   . GLU   A 1 62  ? 45.157 0.132   -29.666 1.00 46.67  ? 62  GLU   A O   1 
ATOM   472  C CB  . GLU   A 1 62  ? 46.960 -2.753  -29.885 1.00 42.71  ? 62  GLU   A CB  1 
ATOM   473  C CG  . GLU   A 1 62  ? 47.771 -1.923  -30.877 1.00 56.16  ? 62  GLU   A CG  1 
ATOM   474  C CD  . GLU   A 1 62  ? 48.324 -2.594  -32.136 1.00 86.72  ? 62  GLU   A CD  1 
ATOM   475  O OE1 . GLU   A 1 62  ? 47.885 -3.715  -32.487 1.00 79.59  ? 62  GLU   A OE1 1 
ATOM   476  O OE2 . GLU   A 1 62  ? 49.198 -1.973  -32.787 1.00 81.98  ? 62  GLU   A OE2 1 
ATOM   477  N N   . ALA   A 1 63  ? 43.960 -1.691  -30.245 1.00 39.44  ? 63  ALA   A N   1 
ATOM   478  C CA  . ALA   A 1 63  ? 42.897 -0.983  -30.964 1.00 38.60  ? 63  ALA   A CA  1 
ATOM   479  C C   . ALA   A 1 63  ? 42.059 -0.056  -30.060 1.00 43.91  ? 63  ALA   A C   1 
ATOM   480  O O   . ALA   A 1 63  ? 41.611 0.989   -30.537 1.00 45.67  ? 63  ALA   A O   1 
ATOM   481  C CB  . ALA   A 1 63  ? 41.997 -1.968  -31.701 1.00 38.80  ? 63  ALA   A CB  1 
ATOM   482  N N   . ILE   A 1 64  ? 41.829 -0.427  -28.780 1.00 39.65  ? 64  ILE   A N   1 
ATOM   483  C CA  . ILE   A 1 64  ? 41.063 0.411   -27.833 1.00 39.10  ? 64  ILE   A CA  1 
ATOM   484  C C   . ILE   A 1 64  ? 41.900 1.663   -27.542 1.00 43.57  ? 64  ILE   A C   1 
ATOM   485  O O   . ILE   A 1 64  ? 41.338 2.749   -27.415 1.00 43.35  ? 64  ILE   A O   1 
ATOM   486  C CB  . ILE   A 1 64  ? 40.653 -0.323  -26.521 1.00 41.65  ? 64  ILE   A CB  1 
ATOM   487  C CG1 . ILE   A 1 64  ? 39.754 -1.539  -26.805 1.00 41.56  ? 64  ILE   A CG1 1 
ATOM   488  C CG2 . ILE   A 1 64  ? 39.938 0.634   -25.534 1.00 41.96  ? 64  ILE   A CG2 1 
ATOM   489  C CD1 . ILE   A 1 64  ? 39.678 -2.563  -25.637 1.00 40.04  ? 64  ILE   A CD1 1 
ATOM   490  N N   . LYS   A 1 65  ? 43.242 1.505   -27.451 1.00 39.90  ? 65  LYS   A N   1 
ATOM   491  C CA  . LYS   A 1 65  ? 44.163 2.615   -27.201 1.00 40.45  ? 65  LYS   A CA  1 
ATOM   492  C C   . LYS   A 1 65  ? 44.089 3.622   -28.347 1.00 46.18  ? 65  LYS   A C   1 
ATOM   493  O O   . LYS   A 1 65  ? 44.059 4.827   -28.113 1.00 46.53  ? 65  LYS   A O   1 
ATOM   494  C CB  . LYS   A 1 65  ? 45.601 2.106   -27.016 1.00 42.21  ? 65  LYS   A CB  1 
ATOM   495  C CG  . LYS   A 1 65  ? 46.417 2.890   -25.998 1.00 48.40  ? 65  LYS   A CG  1 
ATOM   496  C CD  . LYS   A 1 65  ? 47.862 2.355   -25.926 1.00 62.09  ? 65  LYS   A CD  1 
ATOM   497  C CE  . LYS   A 1 65  ? 48.387 2.192   -24.514 1.00 82.27  ? 65  LYS   A CE  1 
ATOM   498  N NZ  . LYS   A 1 65  ? 48.489 3.490   -23.784 1.00 93.44  ? 65  LYS   A NZ  1 
ATOM   499  N N   . LYS   A 1 66  ? 44.015 3.112   -29.583 1.00 43.12  ? 66  LYS   A N   1 
ATOM   500  C CA  . LYS   A 1 66  ? 43.934 3.913   -30.786 1.00 41.40  ? 66  LYS   A CA  1 
ATOM   501  C C   . LYS   A 1 66  ? 42.544 4.511   -30.966 1.00 43.30  ? 66  LYS   A C   1 
ATOM   502  O O   . LYS   A 1 66  ? 42.456 5.701   -31.237 1.00 43.79  ? 66  LYS   A O   1 
ATOM   503  C CB  . LYS   A 1 66  ? 44.325 3.052   -32.002 1.00 43.05  ? 66  LYS   A CB  1 
ATOM   504  C CG  . LYS   A 1 66  ? 44.537 3.849   -33.297 1.00 55.48  ? 66  LYS   A CG  1 
ATOM   505  C CD  . LYS   A 1 66  ? 44.878 2.942   -34.488 1.00 63.48  ? 66  LYS   A CD  1 
ATOM   506  C CE  . LYS   A 1 66  ? 45.035 3.691   -35.796 1.00 73.70  ? 66  LYS   A CE  1 
ATOM   507  N NZ  . LYS   A 1 66  ? 43.729 3.914   -36.481 1.00 84.96  ? 66  LYS   A NZ  1 
ATOM   508  N N   . HIS   A 1 67  ? 41.466 3.701   -30.814 1.00 36.86  ? 67  HIS   A N   1 
ATOM   509  C CA  . HIS   A 1 67  ? 40.083 4.130   -31.048 1.00 35.78  ? 67  HIS   A CA  1 
ATOM   510  C C   . HIS   A 1 67  ? 39.222 4.680   -29.910 1.00 40.98  ? 67  HIS   A C   1 
ATOM   511  O O   . HIS   A 1 67  ? 38.126 5.173   -30.189 1.00 40.51  ? 67  HIS   A O   1 
ATOM   512  C CB  . HIS   A 1 67  ? 39.342 3.102   -31.914 1.00 36.62  ? 67  HIS   A CB  1 
ATOM   513  C CG  . HIS   A 1 67  ? 40.041 2.867   -33.231 1.00 40.34  ? 67  HIS   A CG  1 
ATOM   514  N ND1 . HIS   A 1 67  ? 40.796 1.723   -33.458 1.00 41.89  ? 67  HIS   A ND1 1 
ATOM   515  C CD2 . HIS   A 1 67  ? 40.165 3.690   -34.301 1.00 41.65  ? 67  HIS   A CD2 1 
ATOM   516  C CE1 . HIS   A 1 67  ? 41.294 1.863   -34.674 1.00 41.31  ? 67  HIS   A CE1 1 
ATOM   517  N NE2 . HIS   A 1 67  ? 40.946 3.031   -35.216 1.00 41.63  ? 67  HIS   A NE2 1 
ATOM   518  N N   . ASN   A 1 68  ? 39.706 4.606   -28.638 1.00 38.86  ? 68  ASN   A N   1 
ATOM   519  C CA  . ASN   A 1 68  ? 39.062 5.109   -27.406 1.00 38.92  ? 68  ASN   A CA  1 
ATOM   520  C C   . ASN   A 1 68  ? 37.794 4.421   -26.891 1.00 42.67  ? 68  ASN   A C   1 
ATOM   521  O O   . ASN   A 1 68  ? 37.443 4.595   -25.726 1.00 44.51  ? 68  ASN   A O   1 
ATOM   522  C CB  . ASN   A 1 68  ? 38.835 6.624   -27.474 1.00 37.83  ? 68  ASN   A CB  1 
ATOM   523  C CG  . ASN   A 1 68  ? 40.042 7.373   -27.929 1.00 46.64  ? 68  ASN   A CG  1 
ATOM   524  O OD1 . ASN   A 1 68  ? 41.113 7.271   -27.339 1.00 41.56  ? 68  ASN   A OD1 1 
ATOM   525  N ND2 . ASN   A 1 68  ? 39.892 8.116   -29.000 1.00 38.15  ? 68  ASN   A ND2 1 
ATOM   526  N N   . VAL   A 1 69  ? 37.092 3.694   -27.727 1.00 37.06  ? 69  VAL   A N   1 
ATOM   527  C CA  . VAL   A 1 69  ? 35.857 3.052   -27.298 1.00 36.45  ? 69  VAL   A CA  1 
ATOM   528  C C   . VAL   A 1 69  ? 35.949 1.542   -27.477 1.00 39.81  ? 69  VAL   A C   1 
ATOM   529  O O   . VAL   A 1 69  ? 36.136 1.069   -28.596 1.00 38.40  ? 69  VAL   A O   1 
ATOM   530  C CB  . VAL   A 1 69  ? 34.613 3.680   -28.000 1.00 39.65  ? 69  VAL   A CB  1 
ATOM   531  C CG1 . VAL   A 1 69  ? 33.356 2.823   -27.820 1.00 39.55  ? 69  VAL   A CG1 1 
ATOM   532  C CG2 . VAL   A 1 69  ? 34.370 5.097   -27.503 1.00 39.22  ? 69  VAL   A CG2 1 
ATOM   533  N N   . GLY   A 1 70  ? 35.818 0.814   -26.367 1.00 36.56  ? 70  GLY   A N   1 
ATOM   534  C CA  . GLY   A 1 70  ? 35.825 -0.640  -26.369 1.00 36.01  ? 70  GLY   A CA  1 
ATOM   535  C C   . GLY   A 1 70  ? 34.543 -1.188  -25.773 1.00 39.58  ? 70  GLY   A C   1 
ATOM   536  O O   . GLY   A 1 70  ? 34.115 -0.724  -24.715 1.00 38.87  ? 70  GLY   A O   1 
ATOM   537  N N   . VAL   A 1 71  ? 33.902 -2.164  -26.460 1.00 35.91  ? 71  VAL   A N   1 
ATOM   538  C CA  . VAL   A 1 71  ? 32.706 -2.861  -25.964 1.00 35.59  ? 71  VAL   A CA  1 
ATOM   539  C C   . VAL   A 1 71  ? 33.070 -4.352  -25.912 1.00 40.66  ? 71  VAL   A C   1 
ATOM   540  O O   . VAL   A 1 71  ? 33.376 -4.945  -26.961 1.00 42.14  ? 71  VAL   A O   1 
ATOM   541  C CB  . VAL   A 1 71  ? 31.327 -2.513  -26.603 1.00 38.86  ? 71  VAL   A CB  1 
ATOM   542  C CG1 . VAL   A 1 71  ? 30.946 -1.053  -26.355 1.00 38.07  ? 71  VAL   A CG1 1 
ATOM   543  C CG2 . VAL   A 1 71  ? 31.258 -2.849  -28.087 1.00 38.84  ? 71  VAL   A CG2 1 
ATOM   544  N N   . LYS   A 1 72  ? 33.105 -4.944  -24.692 1.00 34.72  ? 72  LYS   A N   1 
ATOM   545  C CA  . LYS   A 1 72  ? 33.534 -6.330  -24.529 1.00 34.03  ? 72  LYS   A CA  1 
ATOM   546  C C   . LYS   A 1 72  ? 32.541 -7.340  -24.010 1.00 39.68  ? 72  LYS   A C   1 
ATOM   547  O O   . LYS   A 1 72  ? 31.816 -7.080  -23.054 1.00 40.09  ? 72  LYS   A O   1 
ATOM   548  C CB  . LYS   A 1 72  ? 34.823 -6.388  -23.695 1.00 35.50  ? 72  LYS   A CB  1 
ATOM   549  C CG  . LYS   A 1 72  ? 35.469 -7.764  -23.655 1.00 35.44  ? 72  LYS   A CG  1 
ATOM   550  C CD  . LYS   A 1 72  ? 36.652 -7.847  -22.715 1.00 38.57  ? 72  LYS   A CD  1 
ATOM   551  C CE  . LYS   A 1 72  ? 37.098 -9.273  -22.528 1.00 44.62  ? 72  LYS   A CE  1 
ATOM   552  N NZ  . LYS   A 1 72  ? 36.106 -10.051 -21.740 1.00 45.50  ? 72  LYS   A NZ  1 
ATOM   553  N N   . CYS   A 1 73  ? 32.543 -8.531  -24.635 1.00 37.26  ? 73  CYS   A N   1 
ATOM   554  C CA  . CYS   A 1 73  ? 31.710 -9.659  -24.225 1.00 36.08  ? 73  CYS   A CA  1 
ATOM   555  C C   . CYS   A 1 73  ? 32.488 -10.454 -23.143 1.00 39.90  ? 73  CYS   A C   1 
ATOM   556  O O   . CYS   A 1 73  ? 33.713 -10.454 -23.129 1.00 39.11  ? 73  CYS   A O   1 
ATOM   557  C CB  . CYS   A 1 73  ? 31.370 -10.529 -25.426 1.00 35.92  ? 73  CYS   A CB  1 
ATOM   558  S SG  . CYS   A 1 73  ? 30.268 -11.921 -25.063 1.00 39.32  ? 73  CYS   A SG  1 
ATOM   559  N N   . ALA   A 1 74  ? 31.782 -11.101 -22.227 1.00 37.78  ? 74  ALA   A N   1 
ATOM   560  C CA  . ALA   A 1 74  ? 32.417 -11.900 -21.188 1.00 37.65  ? 74  ALA   A CA  1 
ATOM   561  C C   . ALA   A 1 74  ? 33.182 -13.063 -21.843 1.00 39.90  ? 74  ALA   A C   1 
ATOM   562  O O   . ALA   A 1 74  ? 32.706 -13.668 -22.808 1.00 38.21  ? 74  ALA   A O   1 
ATOM   563  C CB  . ALA   A 1 74  ? 31.363 -12.422 -20.219 1.00 38.89  ? 74  ALA   A CB  1 
ATOM   564  N N   . THR   A 1 75  ? 34.380 -13.342 -21.327 1.00 37.86  ? 75  THR   A N   1 
ATOM   565  C CA  . THR   A 1 75  ? 35.291 -14.373 -21.828 1.00 38.34  ? 75  THR   A CA  1 
ATOM   566  C C   . THR   A 1 75  ? 35.728 -15.377 -20.746 1.00 45.01  ? 75  THR   A C   1 
ATOM   567  O O   . THR   A 1 75  ? 35.726 -15.056 -19.555 1.00 43.64  ? 75  THR   A O   1 
ATOM   568  C CB  . THR   A 1 75  ? 36.525 -13.686 -22.418 1.00 43.03  ? 75  THR   A CB  1 
ATOM   569  O OG1 . THR   A 1 75  ? 36.982 -12.715 -21.472 1.00 39.43  ? 75  THR   A OG1 1 
ATOM   570  C CG2 . THR   A 1 75  ? 36.238 -13.018 -23.770 1.00 38.48  ? 75  THR   A CG2 1 
ATOM   571  N N   . ILE   A 1 76  ? 36.121 -16.599 -21.175 1.00 44.54  ? 76  ILE   A N   1 
ATOM   572  C CA  . ILE   A 1 76  ? 36.582 -17.660 -20.272 1.00 44.17  ? 76  ILE   A CA  1 
ATOM   573  C C   . ILE   A 1 76  ? 38.022 -17.369 -19.821 1.00 51.82  ? 76  ILE   A C   1 
ATOM   574  O O   . ILE   A 1 76  ? 38.895 -17.177 -20.660 1.00 52.22  ? 76  ILE   A O   1 
ATOM   575  C CB  . ILE   A 1 76  ? 36.483 -19.067 -20.947 1.00 45.95  ? 76  ILE   A CB  1 
ATOM   576  C CG1 . ILE   A 1 76  ? 35.047 -19.459 -21.317 1.00 44.64  ? 76  ILE   A CG1 1 
ATOM   577  C CG2 . ILE   A 1 76  ? 37.164 -20.172 -20.119 1.00 46.41  ? 76  ILE   A CG2 1 
ATOM   578  C CD1 . ILE   A 1 76  ? 34.996 -20.625 -22.410 1.00 41.44  ? 76  ILE   A CD1 1 
ATOM   579  N N   . THR   A 1 77  ? 38.265 -17.330 -18.510 1.00 52.06  ? 77  THR   A N   1 
ATOM   580  C CA  . THR   A 1 77  ? 39.614 -17.185 -17.962 1.00 53.62  ? 77  THR   A CA  1 
ATOM   581  C C   . THR   A 1 77  ? 39.955 -18.665 -17.726 1.00 59.74  ? 77  THR   A C   1 
ATOM   582  O O   . THR   A 1 77  ? 39.306 -19.303 -16.890 1.00 59.69  ? 77  THR   A O   1 
ATOM   583  C CB  . THR   A 1 77  ? 39.669 -16.322 -16.699 1.00 65.50  ? 77  THR   A CB  1 
ATOM   584  O OG1 . THR   A 1 77  ? 39.363 -14.970 -17.048 1.00 72.44  ? 77  THR   A OG1 1 
ATOM   585  C CG2 . THR   A 1 77  ? 41.044 -16.349 -16.057 1.00 65.97  ? 77  THR   A CG2 1 
ATOM   586  N N   . PRO   A 1 78  ? 40.870 -19.270 -18.511 1.00 57.34  ? 78  PRO   A N   1 
ATOM   587  C CA  . PRO   A 1 78  ? 41.121 -20.712 -18.332 1.00 57.62  ? 78  PRO   A CA  1 
ATOM   588  C C   . PRO   A 1 78  ? 41.818 -21.157 -17.040 1.00 61.50  ? 78  PRO   A C   1 
ATOM   589  O O   . PRO   A 1 78  ? 42.614 -20.431 -16.436 1.00 60.48  ? 78  PRO   A O   1 
ATOM   590  C CB  . PRO   A 1 78  ? 41.880 -21.111 -19.598 1.00 58.96  ? 78  PRO   A CB  1 
ATOM   591  C CG  . PRO   A 1 78  ? 42.528 -19.866 -20.060 1.00 62.94  ? 78  PRO   A CG  1 
ATOM   592  C CD  . PRO   A 1 78  ? 41.704 -18.702 -19.593 1.00 58.28  ? 78  PRO   A CD  1 
ATOM   593  N N   . ASP   A 1 79  ? 41.455 -22.376 -16.625 1.00 57.61  ? 79  ASP   A N   1 
ATOM   594  C CA  . ASP   A 1 79  ? 41.956 -23.113 -15.475 1.00 56.56  ? 79  ASP   A CA  1 
ATOM   595  C C   . ASP   A 1 79  ? 42.271 -24.514 -16.016 1.00 58.32  ? 79  ASP   A C   1 
ATOM   596  O O   . ASP   A 1 79  ? 42.146 -24.725 -17.233 1.00 57.28  ? 79  ASP   A O   1 
ATOM   597  C CB  . ASP   A 1 79  ? 40.922 -23.124 -14.317 1.00 58.57  ? 79  ASP   A CB  1 
ATOM   598  C CG  . ASP   A 1 79  ? 39.500 -23.589 -14.633 1.00 68.87  ? 79  ASP   A CG  1 
ATOM   599  O OD1 . ASP   A 1 79  ? 39.338 -24.502 -15.482 1.00 69.59  ? 79  ASP   A OD1 1 
ATOM   600  O OD2 . ASP   A 1 79  ? 38.549 -23.059 -14.009 1.00 72.06  ? 79  ASP   A OD2 1 
ATOM   601  N N   . GLU   A 1 80  ? 42.681 -25.464 -15.139 1.00 53.25  ? 80  GLU   A N   1 
ATOM   602  C CA  . GLU   A 1 80  ? 43.037 -26.834 -15.529 1.00 51.58  ? 80  GLU   A CA  1 
ATOM   603  C C   . GLU   A 1 80  ? 41.892 -27.555 -16.226 1.00 54.24  ? 80  GLU   A C   1 
ATOM   604  O O   . GLU   A 1 80  ? 42.135 -28.283 -17.197 1.00 54.82  ? 80  GLU   A O   1 
ATOM   605  C CB  . GLU   A 1 80  ? 43.558 -27.631 -14.325 1.00 52.74  ? 80  GLU   A CB  1 
ATOM   606  N N   . LYS   A 1 81  ? 40.642 -27.329 -15.757 1.00 48.97  ? 81  LYS   A N   1 
ATOM   607  C CA  . LYS   A 1 81  ? 39.451 -27.952 -16.336 1.00 48.23  ? 81  LYS   A CA  1 
ATOM   608  C C   . LYS   A 1 81  ? 39.202 -27.425 -17.759 1.00 52.50  ? 81  LYS   A C   1 
ATOM   609  O O   . LYS   A 1 81  ? 38.907 -28.227 -18.654 1.00 51.72  ? 81  LYS   A O   1 
ATOM   610  C CB  . LYS   A 1 81  ? 38.229 -27.794 -15.409 1.00 49.86  ? 81  LYS   A CB  1 
ATOM   611  N N   . ARG   A 1 82  ? 39.376 -26.083 -17.979 1.00 49.80  ? 82  ARG   A N   1 
ATOM   612  C CA  . ARG   A 1 82  ? 39.207 -25.445 -19.310 1.00 49.41  ? 82  ARG   A CA  1 
ATOM   613  C C   . ARG   A 1 82  ? 40.305 -25.904 -20.277 1.00 54.25  ? 82  ARG   A C   1 
ATOM   614  O O   . ARG   A 1 82  ? 40.010 -26.193 -21.444 1.00 54.63  ? 82  ARG   A O   1 
ATOM   615  C CB  . ARG   A 1 82  ? 39.156 -23.907 -19.227 1.00 46.78  ? 82  ARG   A CB  1 
ATOM   616  C CG  . ARG   A 1 82  ? 38.028 -23.339 -18.380 1.00 44.15  ? 82  ARG   A CG  1 
ATOM   617  C CD  . ARG   A 1 82  ? 36.663 -23.780 -18.872 1.00 46.71  ? 82  ARG   A CD  1 
ATOM   618  N NE  . ARG   A 1 82  ? 35.624 -22.861 -18.416 1.00 49.01  ? 82  ARG   A NE  1 
ATOM   619  C CZ  . ARG   A 1 82  ? 34.398 -22.815 -18.912 1.00 53.92  ? 82  ARG   A CZ  1 
ATOM   620  N NH1 . ARG   A 1 82  ? 34.039 -23.638 -19.886 1.00 45.07  ? 82  ARG   A NH1 1 
ATOM   621  N NH2 . ARG   A 1 82  ? 33.519 -21.946 -18.439 1.00 48.10  ? 82  ARG   A NH2 1 
ATOM   622  N N   . VAL   A 1 83  ? 41.560 -26.018 -19.776 1.00 50.77  ? 83  VAL   A N   1 
ATOM   623  C CA  . VAL   A 1 83  ? 42.699 -26.505 -20.561 1.00 51.01  ? 83  VAL   A CA  1 
ATOM   624  C C   . VAL   A 1 83  ? 42.370 -27.905 -21.131 1.00 57.01  ? 83  VAL   A C   1 
ATOM   625  O O   . VAL   A 1 83  ? 42.597 -28.130 -22.317 1.00 57.88  ? 83  VAL   A O   1 
ATOM   626  C CB  . VAL   A 1 83  ? 44.059 -26.436 -19.796 1.00 53.76  ? 83  VAL   A CB  1 
ATOM   627  C CG1 . VAL   A 1 83  ? 45.165 -27.177 -20.552 1.00 53.40  ? 83  VAL   A CG1 1 
ATOM   628  C CG2 . VAL   A 1 83  ? 44.475 -24.987 -19.532 1.00 52.71  ? 83  VAL   A CG2 1 
ATOM   629  N N   . GLU   A 1 84  ? 41.770 -28.802 -20.314 1.00 53.50  ? 84  GLU   A N   1 
ATOM   630  C CA  . GLU   A 1 84  ? 41.380 -30.152 -20.749 1.00 53.57  ? 84  GLU   A CA  1 
ATOM   631  C C   . GLU   A 1 84  ? 40.170 -30.118 -21.687 1.00 58.50  ? 84  GLU   A C   1 
ATOM   632  O O   . GLU   A 1 84  ? 40.185 -30.811 -22.707 1.00 59.18  ? 84  GLU   A O   1 
ATOM   633  C CB  . GLU   A 1 84  ? 41.124 -31.087 -19.544 1.00 54.85  ? 84  GLU   A CB  1 
ATOM   634  N N   . GLU   A 1 85  ? 39.134 -29.303 -21.350 1.00 54.14  ? 85  GLU   A N   1 
ATOM   635  C CA  . GLU   A 1 85  ? 37.896 -29.126 -22.125 1.00 53.47  ? 85  GLU   A CA  1 
ATOM   636  C C   . GLU   A 1 85  ? 38.128 -28.699 -23.585 1.00 57.32  ? 85  GLU   A C   1 
ATOM   637  O O   . GLU   A 1 85  ? 37.409 -29.158 -24.477 1.00 57.21  ? 85  GLU   A O   1 
ATOM   638  C CB  . GLU   A 1 85  ? 36.975 -28.099 -21.428 1.00 54.73  ? 85  GLU   A CB  1 
ATOM   639  C CG  . GLU   A 1 85  ? 35.629 -27.893 -22.125 1.00 61.06  ? 85  GLU   A CG  1 
ATOM   640  C CD  . GLU   A 1 85  ? 34.699 -26.812 -21.600 1.00 70.76  ? 85  GLU   A CD  1 
ATOM   641  O OE1 . GLU   A 1 85  ? 35.051 -26.117 -20.618 1.00 69.29  ? 85  GLU   A OE1 1 
ATOM   642  O OE2 . GLU   A 1 85  ? 33.604 -26.662 -22.184 1.00 58.98  ? 85  GLU   A OE2 1 
ATOM   643  N N   . PHE   A 1 86  ? 39.106 -27.803 -23.815 1.00 53.16  ? 86  PHE   A N   1 
ATOM   644  C CA  . PHE   A 1 86  ? 39.409 -27.276 -25.148 1.00 52.34  ? 86  PHE   A CA  1 
ATOM   645  C C   . PHE   A 1 86  ? 40.744 -27.760 -25.697 1.00 60.91  ? 86  PHE   A C   1 
ATOM   646  O O   . PHE   A 1 86  ? 41.053 -27.472 -26.853 1.00 62.34  ? 86  PHE   A O   1 
ATOM   647  C CB  . PHE   A 1 86  ? 39.365 -25.728 -25.137 1.00 52.33  ? 86  PHE   A CB  1 
ATOM   648  C CG  . PHE   A 1 86  ? 38.053 -25.136 -24.668 1.00 51.49  ? 86  PHE   A CG  1 
ATOM   649  C CD1 . PHE   A 1 86  ? 37.931 -24.595 -23.393 1.00 52.29  ? 86  PHE   A CD1 1 
ATOM   650  C CD2 . PHE   A 1 86  ? 36.933 -25.137 -25.497 1.00 50.62  ? 86  PHE   A CD2 1 
ATOM   651  C CE1 . PHE   A 1 86  ? 36.710 -24.063 -22.957 1.00 52.20  ? 86  PHE   A CE1 1 
ATOM   652  C CE2 . PHE   A 1 86  ? 35.714 -24.615 -25.054 1.00 52.01  ? 86  PHE   A CE2 1 
ATOM   653  C CZ  . PHE   A 1 86  ? 35.610 -24.084 -23.790 1.00 49.86  ? 86  PHE   A CZ  1 
ATOM   654  N N   . LYS   A 1 87  ? 41.537 -28.493 -24.885 1.00 58.39  ? 87  LYS   A N   1 
ATOM   655  C CA  . LYS   A 1 87  ? 42.856 -29.004 -25.275 1.00 57.75  ? 87  LYS   A CA  1 
ATOM   656  C C   . LYS   A 1 87  ? 43.769 -27.797 -25.623 1.00 60.66  ? 87  LYS   A C   1 
ATOM   657  O O   . LYS   A 1 87  ? 44.404 -27.749 -26.683 1.00 61.97  ? 87  LYS   A O   1 
ATOM   658  C CB  . LYS   A 1 87  ? 42.754 -30.084 -26.381 1.00 59.58  ? 87  LYS   A CB  1 
ATOM   659  N N   . LEU   A 1 88  ? 43.796 -26.807 -24.701 1.00 53.68  ? 88  LEU   A N   1 
ATOM   660  C CA  . LEU   A 1 88  ? 44.575 -25.575 -24.826 1.00 51.89  ? 88  LEU   A CA  1 
ATOM   661  C C   . LEU   A 1 88  ? 46.071 -25.806 -24.754 1.00 57.58  ? 88  LEU   A C   1 
ATOM   662  O O   . LEU   A 1 88  ? 46.526 -26.687 -24.029 1.00 59.14  ? 88  LEU   A O   1 
ATOM   663  C CB  . LEU   A 1 88  ? 44.181 -24.550 -23.749 1.00 50.75  ? 88  LEU   A CB  1 
ATOM   664  C CG  . LEU   A 1 88  ? 42.722 -24.097 -23.667 1.00 53.53  ? 88  LEU   A CG  1 
ATOM   665  C CD1 . LEU   A 1 88  ? 42.523 -23.226 -22.456 1.00 52.75  ? 88  LEU   A CD1 1 
ATOM   666  C CD2 . LEU   A 1 88  ? 42.277 -23.359 -24.934 1.00 53.93  ? 88  LEU   A CD2 1 
ATOM   667  N N   . LYS   A 1 89  ? 46.835 -24.979 -25.479 1.00 53.37  ? 89  LYS   A N   1 
ATOM   668  C CA  . LYS   A 1 89  ? 48.295 -25.027 -25.521 1.00 52.36  ? 89  LYS   A CA  1 
ATOM   669  C C   . LYS   A 1 89  ? 48.860 -24.455 -24.223 1.00 57.82  ? 89  LYS   A C   1 
ATOM   670  O O   . LYS   A 1 89  ? 49.972 -24.807 -23.823 1.00 59.37  ? 89  LYS   A O   1 
ATOM   671  C CB  . LYS   A 1 89  ? 48.845 -24.182 -26.681 1.00 52.66  ? 89  LYS   A CB  1 
ATOM   672  C CG  . LYS   A 1 89  ? 48.264 -24.463 -28.044 1.00 52.34  ? 89  LYS   A CG  1 
ATOM   673  C CD  . LYS   A 1 89  ? 48.496 -23.245 -28.931 1.00 55.66  ? 89  LYS   A CD  1 
ATOM   674  C CE  . LYS   A 1 89  ? 47.817 -23.352 -30.271 1.00 51.64  ? 89  LYS   A CE  1 
ATOM   675  N NZ  . LYS   A 1 89  ? 48.064 -22.142 -31.094 1.00 61.00  ? 89  LYS   A NZ  1 
ATOM   676  N N   . GLN   A 1 90  ? 48.114 -23.544 -23.588 1.00 52.40  ? 90  GLN   A N   1 
ATOM   677  C CA  . GLN   A 1 90  ? 48.531 -22.891 -22.356 1.00 51.38  ? 90  GLN   A CA  1 
ATOM   678  C C   . GLN   A 1 90  ? 47.324 -22.518 -21.513 1.00 56.71  ? 90  GLN   A C   1 
ATOM   679  O O   . GLN   A 1 90  ? 46.197 -22.483 -22.012 1.00 55.63  ? 90  GLN   A O   1 
ATOM   680  C CB  . GLN   A 1 90  ? 49.262 -21.582 -22.704 1.00 51.98  ? 90  GLN   A CB  1 
ATOM   681  C CG  . GLN   A 1 90  ? 50.743 -21.715 -22.885 1.00 62.39  ? 90  GLN   A CG  1 
ATOM   682  C CD  . GLN   A 1 90  ? 51.358 -20.419 -23.333 1.00 79.53  ? 90  GLN   A CD  1 
ATOM   683  O OE1 . GLN   A 1 90  ? 51.928 -20.333 -24.427 1.00 83.22  ? 90  GLN   A OE1 1 
ATOM   684  N NE2 . GLN   A 1 90  ? 51.261 -19.380 -22.503 1.00 54.73  ? 90  GLN   A NE2 1 
ATOM   685  N N   . MET   A 1 91  ? 47.573 -22.189 -20.232 1.00 55.06  ? 91  MET   A N   1 
ATOM   686  C CA  . MET   A 1 91  ? 46.543 -21.697 -19.331 1.00 54.91  ? 91  MET   A CA  1 
ATOM   687  C C   . MET   A 1 91  ? 46.688 -20.183 -19.549 1.00 55.91  ? 91  MET   A C   1 
ATOM   688  O O   . MET   A 1 91  ? 47.377 -19.496 -18.787 1.00 55.31  ? 91  MET   A O   1 
ATOM   689  C CB  . MET   A 1 91  ? 46.792 -22.108 -17.864 1.00 57.50  ? 91  MET   A CB  1 
ATOM   690  C CG  . MET   A 1 91  ? 45.578 -21.873 -16.985 1.00 61.94  ? 91  MET   A CG  1 
ATOM   691  S SD  . MET   A 1 91  ? 45.766 -22.273 -15.219 1.00 66.84  ? 91  MET   A SD  1 
ATOM   692  C CE  . MET   A 1 91  ? 45.719 -24.076 -15.307 1.00 63.15  ? 91  MET   A CE  1 
ATOM   693  N N   . TRP   A 1 92  ? 46.091 -19.697 -20.658 1.00 49.63  ? 92  TRP   A N   1 
ATOM   694  C CA  . TRP   A 1 92  ? 46.122 -18.298 -21.096 1.00 47.35  ? 92  TRP   A CA  1 
ATOM   695  C C   . TRP   A 1 92  ? 45.641 -17.343 -20.004 1.00 52.02  ? 92  TRP   A C   1 
ATOM   696  O O   . TRP   A 1 92  ? 44.704 -17.656 -19.278 1.00 50.73  ? 92  TRP   A O   1 
ATOM   697  C CB  . TRP   A 1 92  ? 45.301 -18.105 -22.394 1.00 44.45  ? 92  TRP   A CB  1 
ATOM   698  C CG  . TRP   A 1 92  ? 45.713 -18.977 -23.550 1.00 43.78  ? 92  TRP   A CG  1 
ATOM   699  C CD1 . TRP   A 1 92  ? 44.985 -19.981 -24.120 1.00 46.18  ? 92  TRP   A CD1 1 
ATOM   700  C CD2 . TRP   A 1 92  ? 46.950 -18.912 -24.280 1.00 42.90  ? 92  TRP   A CD2 1 
ATOM   701  N NE1 . TRP   A 1 92  ? 45.689 -20.544 -25.162 1.00 45.05  ? 92  TRP   A NE1 1 
ATOM   702  C CE2 . TRP   A 1 92  ? 46.902 -19.915 -25.276 1.00 46.00  ? 92  TRP   A CE2 1 
ATOM   703  C CE3 . TRP   A 1 92  ? 48.099 -18.100 -24.190 1.00 43.39  ? 92  TRP   A CE3 1 
ATOM   704  C CZ2 . TRP   A 1 92  ? 47.965 -20.143 -26.159 1.00 44.80  ? 92  TRP   A CZ2 1 
ATOM   705  C CZ3 . TRP   A 1 92  ? 49.144 -18.319 -25.076 1.00 43.98  ? 92  TRP   A CZ3 1 
ATOM   706  C CH2 . TRP   A 1 92  ? 49.078 -19.337 -26.038 1.00 44.37  ? 92  TRP   A CH2 1 
ATOM   707  N N   . LYS   A 1 93  ? 46.307 -16.185 -19.871 1.00 50.70  ? 93  LYS   A N   1 
ATOM   708  C CA  . LYS   A 1 93  ? 45.933 -15.190 -18.877 1.00 50.69  ? 93  LYS   A CA  1 
ATOM   709  C C   . LYS   A 1 93  ? 44.644 -14.476 -19.307 1.00 56.83  ? 93  LYS   A C   1 
ATOM   710  O O   . LYS   A 1 93  ? 44.448 -14.196 -20.495 1.00 58.71  ? 93  LYS   A O   1 
ATOM   711  C CB  . LYS   A 1 93  ? 47.075 -14.187 -18.659 1.00 52.48  ? 93  LYS   A CB  1 
ATOM   712  N N   . SER   A 1 94  ? 43.771 -14.198 -18.329 1.00 53.00  ? 94  SER   A N   1 
ATOM   713  C CA  . SER   A 1 94  ? 42.488 -13.493 -18.457 1.00 52.05  ? 94  SER   A CA  1 
ATOM   714  C C   . SER   A 1 94  ? 42.595 -12.329 -19.454 1.00 53.76  ? 94  SER   A C   1 
ATOM   715  O O   . SER   A 1 94  ? 43.441 -11.447 -19.256 1.00 53.03  ? 94  SER   A O   1 
ATOM   716  C CB  . SER   A 1 94  ? 42.057 -12.959 -17.087 1.00 54.65  ? 94  SER   A CB  1 
ATOM   717  O OG  . SER   A 1 94  ? 41.202 -11.829 -17.146 1.00 62.24  ? 94  SER   A OG  1 
ATOM   718  N N   . PRO   A 1 95  ? 41.757 -12.300 -20.520 1.00 49.65  ? 95  PRO   A N   1 
ATOM   719  C CA  . PRO   A 1 95  ? 41.837 -11.186 -21.485 1.00 48.81  ? 95  PRO   A CA  1 
ATOM   720  C C   . PRO   A 1 95  ? 41.720 -9.822  -20.805 1.00 52.15  ? 95  PRO   A C   1 
ATOM   721  O O   . PRO   A 1 95  ? 42.455 -8.896  -21.162 1.00 51.70  ? 95  PRO   A O   1 
ATOM   722  C CB  . PRO   A 1 95  ? 40.677 -11.465 -22.447 1.00 50.20  ? 95  PRO   A CB  1 
ATOM   723  C CG  . PRO   A 1 95  ? 40.433 -12.917 -22.337 1.00 54.47  ? 95  PRO   A CG  1 
ATOM   724  C CD  . PRO   A 1 95  ? 40.699 -13.260 -20.904 1.00 50.67  ? 95  PRO   A CD  1 
ATOM   725  N N   . ASN   A 1 96  ? 40.842 -9.725  -19.779 1.00 48.37  ? 96  ASN   A N   1 
ATOM   726  C CA  . ASN   A 1 96  ? 40.587 -8.511  -18.979 1.00 48.39  ? 96  ASN   A CA  1 
ATOM   727  C C   . ASN   A 1 96  ? 41.854 -8.010  -18.311 1.00 52.64  ? 96  ASN   A C   1 
ATOM   728  O O   . ASN   A 1 96  ? 42.047 -6.796  -18.228 1.00 52.64  ? 96  ASN   A O   1 
ATOM   729  C CB  . ASN   A 1 96  ? 39.492 -8.756  -17.942 1.00 49.57  ? 96  ASN   A CB  1 
ATOM   730  C CG  . ASN   A 1 96  ? 38.322 -9.526  -18.508 1.00 75.86  ? 96  ASN   A CG  1 
ATOM   731  O OD1 . ASN   A 1 96  ? 37.540 -8.996  -19.293 1.00 74.32  ? 96  ASN   A OD1 1 
ATOM   732  N ND2 . ASN   A 1 96  ? 38.194 -10.802 -18.145 1.00 65.19  ? 96  ASN   A ND2 1 
ATOM   733  N N   . GLY   A 1 97  ? 42.707 -8.951  -17.876 1.00 49.09  ? 97  GLY   A N   1 
ATOM   734  C CA  . GLY   A 1 97  ? 43.994 -8.692  -17.244 1.00 48.89  ? 97  GLY   A CA  1 
ATOM   735  C C   . GLY   A 1 97  ? 44.976 -8.113  -18.234 1.00 54.67  ? 97  GLY   A C   1 
ATOM   736  O O   . GLY   A 1 97  ? 45.616 -7.094  -17.948 1.00 54.49  ? 97  GLY   A O   1 
ATOM   737  N N   . THR   A 1 98  ? 45.069 -8.751  -19.432 1.00 51.61  ? 98  THR   A N   1 
ATOM   738  C CA  . THR   A 1 98  ? 45.924 -8.320  -20.546 1.00 50.65  ? 98  THR   A CA  1 
ATOM   739  C C   . THR   A 1 98  ? 45.487 -6.904  -20.987 1.00 53.78  ? 98  THR   A C   1 
ATOM   740  O O   . THR   A 1 98  ? 46.340 -6.034  -21.136 1.00 53.50  ? 98  THR   A O   1 
ATOM   741  C CB  . THR   A 1 98  ? 45.793 -9.305  -21.723 1.00 57.31  ? 98  THR   A CB  1 
ATOM   742  O OG1 . THR   A 1 98  ? 46.085 -10.632 -21.302 1.00 57.25  ? 98  THR   A OG1 1 
ATOM   743  C CG2 . THR   A 1 98  ? 46.655 -8.927  -22.912 1.00 56.82  ? 98  THR   A CG2 1 
ATOM   744  N N   . ILE   A 1 99  ? 44.155 -6.685  -21.181 1.00 49.44  ? 99  ILE   A N   1 
ATOM   745  C CA  . ILE   A 1 99  ? 43.590 -5.400  -21.618 1.00 49.00  ? 99  ILE   A CA  1 
ATOM   746  C C   . ILE   A 1 99  ? 43.879 -4.286  -20.608 1.00 53.94  ? 99  ILE   A C   1 
ATOM   747  O O   . ILE   A 1 99  ? 44.420 -3.248  -21.007 1.00 52.92  ? 99  ILE   A O   1 
ATOM   748  C CB  . ILE   A 1 99  ? 42.075 -5.490  -22.044 1.00 51.20  ? 99  ILE   A CB  1 
ATOM   749  C CG1 . ILE   A 1 99  ? 41.884 -6.420  -23.256 1.00 50.49  ? 99  ILE   A CG1 1 
ATOM   750  C CG2 . ILE   A 1 99  ? 41.468 -4.090  -22.341 1.00 51.34  ? 99  ILE   A CG2 1 
ATOM   751  C CD1 . ILE   A 1 99  ? 40.599 -7.077  -23.310 1.00 49.13  ? 99  ILE   A CD1 1 
ATOM   752  N N   . ARG   A 1 100 ? 43.524 -4.512  -19.314 1.00 52.69  ? 100 ARG   A N   1 
ATOM   753  C CA  . ARG   A 1 100 ? 43.715 -3.556  -18.208 1.00 53.67  ? 100 ARG   A CA  1 
ATOM   754  C C   . ARG   A 1 100 ? 45.170 -3.151  -18.075 1.00 57.07  ? 100 ARG   A C   1 
ATOM   755  O O   . ARG   A 1 100 ? 45.451 -1.961  -17.988 1.00 56.78  ? 100 ARG   A O   1 
ATOM   756  C CB  . ARG   A 1 100 ? 43.163 -4.091  -16.875 1.00 54.70  ? 100 ARG   A CB  1 
ATOM   757  N N   . ASN   A 1 101 ? 46.092 -4.127  -18.131 1.00 53.37  ? 101 ASN   A N   1 
ATOM   758  C CA  . ASN   A 1 101 ? 47.531 -3.879  -18.053 1.00 53.39  ? 101 ASN   A CA  1 
ATOM   759  C C   . ASN   A 1 101 ? 48.020 -2.971  -19.168 1.00 56.59  ? 101 ASN   A C   1 
ATOM   760  O O   . ASN   A 1 101 ? 48.873 -2.119  -18.909 1.00 58.68  ? 101 ASN   A O   1 
ATOM   761  C CB  . ASN   A 1 101 ? 48.341 -5.190  -18.042 1.00 58.51  ? 101 ASN   A CB  1 
ATOM   762  C CG  . ASN   A 1 101 ? 48.424 -5.923  -16.705 1.00 93.55  ? 101 ASN   A CG  1 
ATOM   763  O OD1 . ASN   A 1 101 ? 48.989 -7.027  -16.620 1.00 89.82  ? 101 ASN   A OD1 1 
ATOM   764  N ND2 . ASN   A 1 101 ? 47.876 -5.344  -15.625 1.00 83.64  ? 101 ASN   A ND2 1 
ATOM   765  N N   . ILE   A 1 102 ? 47.488 -3.138  -20.401 1.00 49.62  ? 102 ILE   A N   1 
ATOM   766  C CA  . ILE   A 1 102 ? 47.875 -2.317  -21.558 1.00 47.43  ? 102 ILE   A CA  1 
ATOM   767  C C   . ILE   A 1 102 ? 47.336 -0.897  -21.470 1.00 51.30  ? 102 ILE   A C   1 
ATOM   768  O O   . ILE   A 1 102 ? 48.069 0.052   -21.747 1.00 53.78  ? 102 ILE   A O   1 
ATOM   769  C CB  . ILE   A 1 102 ? 47.513 -3.014  -22.910 1.00 49.08  ? 102 ILE   A CB  1 
ATOM   770  C CG1 . ILE   A 1 102 ? 48.504 -4.154  -23.223 1.00 47.98  ? 102 ILE   A CG1 1 
ATOM   771  C CG2 . ILE   A 1 102 ? 47.407 -2.012  -24.101 1.00 47.46  ? 102 ILE   A CG2 1 
ATOM   772  C CD1 . ILE   A 1 102 ? 47.925 -5.250  -24.077 1.00 50.40  ? 102 ILE   A CD1 1 
ATOM   773  N N   . LEU   A 1 103 ? 46.069 -0.744  -21.095 1.00 44.91  ? 103 LEU   A N   1 
ATOM   774  C CA  . LEU   A 1 103 ? 45.447 0.576   -21.050 1.00 43.57  ? 103 LEU   A CA  1 
ATOM   775  C C   . LEU   A 1 103 ? 45.575 1.361   -19.776 1.00 47.49  ? 103 LEU   A C   1 
ATOM   776  O O   . LEU   A 1 103 ? 45.475 2.591   -19.821 1.00 47.81  ? 103 LEU   A O   1 
ATOM   777  C CB  . LEU   A 1 103 ? 43.942 0.447   -21.352 1.00 42.91  ? 103 LEU   A CB  1 
ATOM   778  C CG  . LEU   A 1 103 ? 43.502 -0.286  -22.604 1.00 45.76  ? 103 LEU   A CG  1 
ATOM   779  C CD1 . LEU   A 1 103 ? 42.012 -0.429  -22.596 1.00 45.70  ? 103 LEU   A CD1 1 
ATOM   780  C CD2 . LEU   A 1 103 ? 43.985 0.413   -23.873 1.00 43.41  ? 103 LEU   A CD2 1 
ATOM   781  N N   . GLY   A 1 104 ? 45.688 0.657   -18.646 1.00 42.85  ? 104 GLY   A N   1 
ATOM   782  C CA  . GLY   A 1 104 ? 45.691 1.263   -17.327 1.00 41.27  ? 104 GLY   A CA  1 
ATOM   783  C C   . GLY   A 1 104 ? 44.238 1.585   -17.042 1.00 48.08  ? 104 GLY   A C   1 
ATOM   784  O O   . GLY   A 1 104 ? 43.336 1.016   -17.678 1.00 48.97  ? 104 GLY   A O   1 
ATOM   785  N N   . GLY   A 1 105 ? 43.992 2.511   -16.125 1.00 44.92  ? 105 GLY   A N   1 
ATOM   786  C CA  . GLY   A 1 105 ? 42.626 2.882   -15.795 1.00 44.25  ? 105 GLY   A CA  1 
ATOM   787  C C   . GLY   A 1 105 ? 42.040 2.160   -14.599 1.00 47.44  ? 105 GLY   A C   1 
ATOM   788  O O   . GLY   A 1 105 ? 42.625 1.199   -14.083 1.00 46.95  ? 105 GLY   A O   1 
ATOM   789  N N   . THR   A 1 106 ? 40.841 2.627   -14.182 1.00 43.38  ? 106 THR   A N   1 
ATOM   790  C CA  . THR   A 1 106 ? 40.063 2.181   -13.030 1.00 41.95  ? 106 THR   A CA  1 
ATOM   791  C C   . THR   A 1 106 ? 38.734 1.558   -13.437 1.00 45.15  ? 106 THR   A C   1 
ATOM   792  O O   . THR   A 1 106 ? 37.988 2.146   -14.218 1.00 44.67  ? 106 THR   A O   1 
ATOM   793  C CB  . THR   A 1 106 ? 39.903 3.382   -12.064 1.00 45.80  ? 106 THR   A CB  1 
ATOM   794  O OG1 . THR   A 1 106 ? 41.199 3.908   -11.778 1.00 45.55  ? 106 THR   A OG1 1 
ATOM   795  C CG2 . THR   A 1 106 ? 39.179 3.030   -10.752 1.00 43.52  ? 106 THR   A CG2 1 
ATOM   796  N N   . VAL   A 1 107 ? 38.436 0.373   -12.881 1.00 41.32  ? 107 VAL   A N   1 
ATOM   797  C CA  . VAL   A 1 107 ? 37.186 -0.330  -13.130 1.00 41.05  ? 107 VAL   A CA  1 
ATOM   798  C C   . VAL   A 1 107 ? 36.093 0.227   -12.173 1.00 45.75  ? 107 VAL   A C   1 
ATOM   799  O O   . VAL   A 1 107 ? 36.306 0.304   -10.962 1.00 45.10  ? 107 VAL   A O   1 
ATOM   800  C CB  . VAL   A 1 107 ? 37.347 -1.878  -13.049 1.00 44.67  ? 107 VAL   A CB  1 
ATOM   801  C CG1 . VAL   A 1 107 ? 36.051 -2.595  -13.422 1.00 43.85  ? 107 VAL   A CG1 1 
ATOM   802  C CG2 . VAL   A 1 107 ? 38.489 -2.361  -13.943 1.00 44.44  ? 107 VAL   A CG2 1 
ATOM   803  N N   . PHE   A 1 108 ? 34.951 0.658   -12.741 1.00 41.87  ? 108 PHE   A N   1 
ATOM   804  C CA  . PHE   A 1 108 ? 33.803 1.191   -12.009 1.00 40.81  ? 108 PHE   A CA  1 
ATOM   805  C C   . PHE   A 1 108 ? 32.623 0.259   -12.232 1.00 44.85  ? 108 PHE   A C   1 
ATOM   806  O O   . PHE   A 1 108 ? 32.303 -0.080  -13.380 1.00 43.05  ? 108 PHE   A O   1 
ATOM   807  C CB  . PHE   A 1 108 ? 33.453 2.627   -12.453 1.00 41.73  ? 108 PHE   A CB  1 
ATOM   808  C CG  . PHE   A 1 108 ? 34.452 3.660   -12.007 1.00 42.62  ? 108 PHE   A CG  1 
ATOM   809  C CD1 . PHE   A 1 108 ? 34.337 4.272   -10.763 1.00 45.44  ? 108 PHE   A CD1 1 
ATOM   810  C CD2 . PHE   A 1 108 ? 35.516 4.019   -12.827 1.00 44.43  ? 108 PHE   A CD2 1 
ATOM   811  C CE1 . PHE   A 1 108 ? 35.284 5.212   -10.340 1.00 46.73  ? 108 PHE   A CE1 1 
ATOM   812  C CE2 . PHE   A 1 108 ? 36.448 4.972   -12.415 1.00 47.08  ? 108 PHE   A CE2 1 
ATOM   813  C CZ  . PHE   A 1 108 ? 36.332 5.559   -11.174 1.00 45.82  ? 108 PHE   A CZ  1 
ATOM   814  N N   . ARG   A 1 109 ? 31.994 -0.176  -11.132 1.00 43.22  ? 109 ARG   A N   1 
ATOM   815  C CA  . ARG   A 1 109 ? 30.847 -1.090  -11.168 1.00 43.69  ? 109 ARG   A CA  1 
ATOM   816  C C   . ARG   A 1 109 ? 29.581 -0.339  -10.838 1.00 49.10  ? 109 ARG   A C   1 
ATOM   817  O O   . ARG   A 1 109 ? 29.481 0.280   -9.785  1.00 49.38  ? 109 ARG   A O   1 
ATOM   818  C CB  . ARG   A 1 109 ? 31.072 -2.332  -10.280 1.00 43.97  ? 109 ARG   A CB  1 
ATOM   819  C CG  . ARG   A 1 109 ? 31.900 -3.395  -10.991 1.00 54.70  ? 109 ARG   A CG  1 
ATOM   820  C CD  . ARG   A 1 109 ? 32.404 -4.478  -10.063 1.00 70.73  ? 109 ARG   A CD  1 
ATOM   821  N NE  . ARG   A 1 109 ? 33.156 -5.506  -10.789 1.00 79.91  ? 109 ARG   A NE  1 
ATOM   822  C CZ  . ARG   A 1 109 ? 34.471 -5.478  -10.997 1.00 97.18  ? 109 ARG   A CZ  1 
ATOM   823  N NH1 . ARG   A 1 109 ? 35.204 -4.474  -10.531 1.00 87.17  ? 109 ARG   A NH1 1 
ATOM   824  N NH2 . ARG   A 1 109 ? 35.063 -6.456  -11.673 1.00 84.41  ? 109 ARG   A NH2 1 
ATOM   825  N N   . GLU   A 1 110 ? 28.643 -0.334  -11.770 1.00 47.69  ? 110 GLU   A N   1 
ATOM   826  C CA  . GLU   A 1 110 ? 27.381 0.375   -11.603 1.00 49.02  ? 110 GLU   A CA  1 
ATOM   827  C C   . GLU   A 1 110 ? 26.230 -0.606  -11.779 1.00 55.31  ? 110 GLU   A C   1 
ATOM   828  O O   . GLU   A 1 110 ? 26.298 -1.496  -12.628 1.00 54.75  ? 110 GLU   A O   1 
ATOM   829  C CB  . GLU   A 1 110 ? 27.299 1.534   -12.609 1.00 50.64  ? 110 GLU   A CB  1 
ATOM   830  C CG  . GLU   A 1 110 ? 26.034 2.382   -12.538 1.00 63.78  ? 110 GLU   A CG  1 
ATOM   831  C CD  . GLU   A 1 110 ? 25.949 3.505   -13.554 1.00 89.85  ? 110 GLU   A CD  1 
ATOM   832  O OE1 . GLU   A 1 110 ? 25.020 4.337   -13.440 1.00 93.31  ? 110 GLU   A OE1 1 
ATOM   833  O OE2 . GLU   A 1 110 ? 26.810 3.561   -14.462 1.00 87.41  ? 110 GLU   A OE2 1 
ATOM   834  N N   . ALA   A 1 111 ? 25.185 -0.454  -10.956 1.00 53.79  ? 111 ALA   A N   1 
ATOM   835  C CA  . ALA   A 1 111 ? 24.000 -1.302  -11.022 1.00 53.75  ? 111 ALA   A CA  1 
ATOM   836  C C   . ALA   A 1 111 ? 22.882 -0.623  -11.799 1.00 57.71  ? 111 ALA   A C   1 
ATOM   837  O O   . ALA   A 1 111 ? 22.695 0.594   -11.687 1.00 58.45  ? 111 ALA   A O   1 
ATOM   838  C CB  . ALA   A 1 111 ? 23.519 -1.626  -9.630  1.00 54.42  ? 111 ALA   A CB  1 
ATOM   839  N N   . ILE   A 1 112 ? 22.135 -1.417  -12.577 1.00 52.87  ? 112 ILE   A N   1 
ATOM   840  C CA  . ILE   A 1 112 ? 20.983 -0.953  -13.355 1.00 51.51  ? 112 ILE   A CA  1 
ATOM   841  C C   . ILE   A 1 112 ? 19.783 -1.138  -12.420 1.00 55.89  ? 112 ILE   A C   1 
ATOM   842  O O   . ILE   A 1 112 ? 19.490 -2.248  -11.962 1.00 54.24  ? 112 ILE   A O   1 
ATOM   843  C CB  . ILE   A 1 112 ? 20.832 -1.678  -14.719 1.00 53.25  ? 112 ILE   A CB  1 
ATOM   844  C CG1 . ILE   A 1 112 ? 22.056 -1.430  -15.616 1.00 52.81  ? 112 ILE   A CG1 1 
ATOM   845  C CG2 . ILE   A 1 112 ? 19.558 -1.247  -15.423 1.00 52.25  ? 112 ILE   A CG2 1 
ATOM   846  C CD1 . ILE   A 1 112 ? 23.043 -2.499  -15.670 1.00 56.02  ? 112 ILE   A CD1 1 
ATOM   847  N N   . ILE   A 1 113 ? 19.119 -0.025  -12.117 1.00 53.31  ? 113 ILE   A N   1 
ATOM   848  C CA  . ILE   A 1 113 ? 18.009 0.004   -11.189 1.00 52.51  ? 113 ILE   A CA  1 
ATOM   849  C C   . ILE   A 1 113 ? 16.667 0.054   -11.842 1.00 56.82  ? 113 ILE   A C   1 
ATOM   850  O O   . ILE   A 1 113 ? 16.393 0.926   -12.677 1.00 57.33  ? 113 ILE   A O   1 
ATOM   851  C CB  . ILE   A 1 113 ? 18.210 1.156   -10.168 1.00 55.45  ? 113 ILE   A CB  1 
ATOM   852  C CG1 . ILE   A 1 113 ? 19.504 0.961   -9.375  1.00 55.67  ? 113 ILE   A CG1 1 
ATOM   853  C CG2 . ILE   A 1 113 ? 17.005 1.322   -9.232  1.00 57.02  ? 113 ILE   A CG2 1 
ATOM   854  C CD1 . ILE   A 1 113 ? 19.912 2.145   -8.704  1.00 68.42  ? 113 ILE   A CD1 1 
ATOM   855  N N   . CYS   A 1 114 ? 15.813 -0.876  -11.409 1.00 52.91  ? 114 CYS   A N   1 
ATOM   856  C CA  . CYS   A 1 114 ? 14.421 -1.003  -11.803 1.00 51.77  ? 114 CYS   A CA  1 
ATOM   857  C C   . CYS   A 1 114 ? 13.606 -0.886  -10.519 1.00 55.10  ? 114 CYS   A C   1 
ATOM   858  O O   . CYS   A 1 114 ? 13.898 -1.579  -9.537  1.00 54.13  ? 114 CYS   A O   1 
ATOM   859  C CB  . CYS   A 1 114 ? 14.170 -2.329  -12.512 1.00 51.19  ? 114 CYS   A CB  1 
ATOM   860  S SG  . CYS   A 1 114 ? 15.115 -2.539  -14.037 1.00 54.41  ? 114 CYS   A SG  1 
ATOM   861  N N   . LYS   A 1 115 ? 12.601 0.007   -10.532 1.00 52.10  ? 115 LYS   A N   1 
ATOM   862  C CA  . LYS   A 1 115 ? 11.676 0.301   -9.425  1.00 52.01  ? 115 LYS   A CA  1 
ATOM   863  C C   . LYS   A 1 115 ? 11.002 -0.934  -8.767  1.00 56.05  ? 115 LYS   A C   1 
ATOM   864  O O   . LYS   A 1 115 ? 10.805 -0.934  -7.559  1.00 56.02  ? 115 LYS   A O   1 
ATOM   865  C CB  . LYS   A 1 115 ? 10.624 1.325   -9.880  1.00 54.31  ? 115 LYS   A CB  1 
ATOM   866  C CG  . LYS   A 1 115 ? 11.047 2.782   -9.661  1.00 65.53  ? 115 LYS   A CG  1 
ATOM   867  C CD  . LYS   A 1 115 ? 10.960 3.663   -10.913 1.00 73.55  ? 115 LYS   A CD  1 
ATOM   868  C CE  . LYS   A 1 115 ? 9.558  3.975   -11.383 1.00 83.93  ? 115 LYS   A CE  1 
ATOM   869  N NZ  . LYS   A 1 115 ? 9.564  4.876   -12.572 1.00 94.74  ? 115 LYS   A NZ  1 
ATOM   870  N N   . ASN   A 1 116 ? 10.673 -1.976  -9.556  1.00 52.62  ? 116 ASN   A N   1 
ATOM   871  C CA  . ASN   A 1 116 ? 10.036 -3.225  -9.100  1.00 51.76  ? 116 ASN   A CA  1 
ATOM   872  C C   . ASN   A 1 116 ? 11.049 -4.309  -8.641  1.00 56.96  ? 116 ASN   A C   1 
ATOM   873  O O   . ASN   A 1 116 ? 10.643 -5.359  -8.122  1.00 56.57  ? 116 ASN   A O   1 
ATOM   874  C CB  . ASN   A 1 116 ? 9.107  -3.776  -10.206 1.00 46.51  ? 116 ASN   A CB  1 
ATOM   875  C CG  . ASN   A 1 116 ? 9.803  -4.050  -11.531 1.00 59.20  ? 116 ASN   A CG  1 
ATOM   876  O OD1 . ASN   A 1 116 ? 10.800 -3.404  -11.900 1.00 43.40  ? 116 ASN   A OD1 1 
ATOM   877  N ND2 . ASN   A 1 116 ? 9.287  -5.016  -12.283 1.00 53.13  ? 116 ASN   A ND2 1 
ATOM   878  N N   . ILE   A 1 117 ? 12.357 -4.054  -8.831  1.00 55.13  ? 117 ILE   A N   1 
ATOM   879  C CA  . ILE   A 1 117 ? 13.431 -4.991  -8.462  1.00 55.50  ? 117 ILE   A CA  1 
ATOM   880  C C   . ILE   A 1 117 ? 14.076 -4.559  -7.132  1.00 62.82  ? 117 ILE   A C   1 
ATOM   881  O O   . ILE   A 1 117 ? 14.571 -3.434  -7.038  1.00 62.38  ? 117 ILE   A O   1 
ATOM   882  C CB  . ILE   A 1 117 ? 14.468 -5.183  -9.632  1.00 57.74  ? 117 ILE   A CB  1 
ATOM   883  C CG1 . ILE   A 1 117 ? 13.813 -5.685  -10.957 1.00 57.77  ? 117 ILE   A CG1 1 
ATOM   884  C CG2 . ILE   A 1 117 ? 15.688 -6.024  -9.233  1.00 56.82  ? 117 ILE   A CG2 1 
ATOM   885  C CD1 . ILE   A 1 117 ? 13.142 -7.119  -10.957 1.00 62.37  ? 117 ILE   A CD1 1 
ATOM   886  N N   . PRO   A 1 118 ? 14.080 -5.442  -6.101  1.00 62.32  ? 118 PRO   A N   1 
ATOM   887  C CA  . PRO   A 1 118 ? 14.669 -5.070  -4.797  1.00 62.54  ? 118 PRO   A CA  1 
ATOM   888  C C   . PRO   A 1 118 ? 16.183 -4.875  -4.774  1.00 68.88  ? 118 PRO   A C   1 
ATOM   889  O O   . PRO   A 1 118 ? 16.923 -5.651  -5.396  1.00 68.41  ? 118 PRO   A O   1 
ATOM   890  C CB  . PRO   A 1 118 ? 14.274 -6.239  -3.883  1.00 63.86  ? 118 PRO   A CB  1 
ATOM   891  C CG  . PRO   A 1 118 ? 13.207 -6.976  -4.602  1.00 68.22  ? 118 PRO   A CG  1 
ATOM   892  C CD  . PRO   A 1 118 ? 13.516 -6.805  -6.049  1.00 64.14  ? 118 PRO   A CD  1 
ATOM   893  N N   . ARG   A 1 119 ? 16.638 -3.837  -4.029  1.00 67.13  ? 119 ARG   A N   1 
ATOM   894  C CA  . ARG   A 1 119 ? 18.058 -3.492  -3.814  1.00 67.55  ? 119 ARG   A CA  1 
ATOM   895  C C   . ARG   A 1 119 ? 18.388 -3.815  -2.346  1.00 72.90  ? 119 ARG   A C   1 
ATOM   896  O O   . ARG   A 1 119 ? 17.495 -4.231  -1.598  1.00 71.96  ? 119 ARG   A O   1 
ATOM   897  C CB  . ARG   A 1 119 ? 18.361 -1.978  -4.047  1.00 66.83  ? 119 ARG   A CB  1 
ATOM   898  C CG  . ARG   A 1 119 ? 17.558 -1.250  -5.104  1.00 77.52  ? 119 ARG   A CG  1 
ATOM   899  C CD  . ARG   A 1 119 ? 16.482 -0.391  -4.463  1.00 86.60  ? 119 ARG   A CD  1 
ATOM   900  N NE  . ARG   A 1 119 ? 15.947 0.635   -5.363  1.00 86.40  ? 119 ARG   A NE  1 
ATOM   901  C CZ  . ARG   A 1 119 ? 14.991 0.426   -6.262  1.00 97.46  ? 119 ARG   A CZ  1 
ATOM   902  N NH1 . ARG   A 1 119 ? 14.465 -0.784  -6.412  1.00 75.91  ? 119 ARG   A NH1 1 
ATOM   903  N NH2 . ARG   A 1 119 ? 14.558 1.423   -7.025  1.00 90.00  ? 119 ARG   A NH2 1 
ATOM   904  N N   . LEU   A 1 120 ? 19.659 -3.591  -1.933  1.00 70.97  ? 120 LEU   A N   1 
ATOM   905  C CA  . LEU   A 1 120 ? 20.133 -3.789  -0.562  1.00 71.58  ? 120 LEU   A CA  1 
ATOM   906  C C   . LEU   A 1 120 ? 19.340 -2.814  0.343   1.00 76.02  ? 120 LEU   A C   1 
ATOM   907  O O   . LEU   A 1 120 ? 18.586 -3.260  1.209   1.00 75.44  ? 120 LEU   A O   1 
ATOM   908  C CB  . LEU   A 1 120 ? 21.659 -3.515  -0.496  1.00 71.98  ? 120 LEU   A CB  1 
ATOM   909  C CG  . LEU   A 1 120 ? 22.400 -3.857  0.812   1.00 77.04  ? 120 LEU   A CG  1 
ATOM   910  C CD1 . LEU   A 1 120 ? 22.519 -5.374  1.010   1.00 77.36  ? 120 LEU   A CD1 1 
ATOM   911  C CD2 . LEU   A 1 120 ? 23.789 -3.227  0.832   1.00 78.97  ? 120 LEU   A CD2 1 
ATOM   912  N N   . VAL   A 1 121 ? 19.483 -1.495  0.097   1.00 72.55  ? 121 VAL   A N   1 
ATOM   913  C CA  . VAL   A 1 121 ? 18.779 -0.421  0.800   1.00 72.20  ? 121 VAL   A CA  1 
ATOM   914  C C   . VAL   A 1 121 ? 17.700 0.024   -0.187  1.00 76.96  ? 121 VAL   A C   1 
ATOM   915  O O   . VAL   A 1 121 ? 18.035 0.461   -1.290  1.00 77.79  ? 121 VAL   A O   1 
ATOM   916  C CB  . VAL   A 1 121 ? 19.723 0.763   1.179   1.00 75.89  ? 121 VAL   A CB  1 
ATOM   917  C CG1 . VAL   A 1 121 ? 18.946 1.923   1.807   1.00 75.65  ? 121 VAL   A CG1 1 
ATOM   918  C CG2 . VAL   A 1 121 ? 20.859 0.314   2.092   1.00 75.52  ? 121 VAL   A CG2 1 
ATOM   919  N N   . SER   A 1 122 ? 16.419 -0.096  0.184   1.00 73.63  ? 122 SER   A N   1 
ATOM   920  C CA  . SER   A 1 122 ? 15.301 0.296   -0.685  1.00 73.83  ? 122 SER   A CA  1 
ATOM   921  C C   . SER   A 1 122 ? 15.364 1.780   -1.100  1.00 78.86  ? 122 SER   A C   1 
ATOM   922  O O   . SER   A 1 122 ? 14.884 2.134   -2.183  1.00 78.83  ? 122 SER   A O   1 
ATOM   923  C CB  . SER   A 1 122 ? 13.959 -0.049  -0.043  1.00 77.18  ? 122 SER   A CB  1 
ATOM   924  O OG  . SER   A 1 122 ? 13.732 0.698   1.140   1.00 86.46  ? 122 SER   A OG  1 
ATOM   925  N N   . GLY   A 1 123 ? 15.987 2.608   -0.249  1.00 75.31  ? 123 GLY   A N   1 
ATOM   926  C CA  . GLY   A 1 123 ? 16.173 4.039   -0.473  1.00 74.73  ? 123 GLY   A CA  1 
ATOM   927  C C   . GLY   A 1 123 ? 17.063 4.367   -1.658  1.00 77.29  ? 123 GLY   A C   1 
ATOM   928  O O   . GLY   A 1 123 ? 16.985 5.475   -2.195  1.00 77.03  ? 123 GLY   A O   1 
ATOM   929  N N   . TRP   A 1 124 ? 17.908 3.393   -2.083  1.00 72.43  ? 124 TRP   A N   1 
ATOM   930  C CA  . TRP   A 1 124 ? 18.841 3.509   -3.204  1.00 71.20  ? 124 TRP   A CA  1 
ATOM   931  C C   . TRP   A 1 124 ? 18.115 3.589   -4.548  1.00 74.78  ? 124 TRP   A C   1 
ATOM   932  O O   . TRP   A 1 124 ? 17.969 2.589   -5.256  1.00 74.20  ? 124 TRP   A O   1 
ATOM   933  C CB  . TRP   A 1 124 ? 19.878 2.372   -3.170  1.00 69.39  ? 124 TRP   A CB  1 
ATOM   934  C CG  . TRP   A 1 124 ? 20.880 2.462   -2.051  1.00 69.96  ? 124 TRP   A CG  1 
ATOM   935  C CD1 . TRP   A 1 124 ? 21.035 3.483   -1.157  1.00 72.84  ? 124 TRP   A CD1 1 
ATOM   936  C CD2 . TRP   A 1 124 ? 21.891 1.496   -1.735  1.00 69.61  ? 124 TRP   A CD2 1 
ATOM   937  N NE1 . TRP   A 1 124 ? 22.068 3.203   -0.292  1.00 72.13  ? 124 TRP   A NE1 1 
ATOM   938  C CE2 . TRP   A 1 124 ? 22.617 1.994   -0.628  1.00 73.27  ? 124 TRP   A CE2 1 
ATOM   939  C CE3 . TRP   A 1 124 ? 22.255 0.253   -2.280  1.00 70.74  ? 124 TRP   A CE3 1 
ATOM   940  C CZ2 . TRP   A 1 124 ? 23.689 1.300   -0.061  1.00 72.44  ? 124 TRP   A CZ2 1 
ATOM   941  C CZ3 . TRP   A 1 124 ? 23.312 -0.438  -1.711  1.00 72.21  ? 124 TRP   A CZ3 1 
ATOM   942  C CH2 . TRP   A 1 124 ? 24.018 0.085   -0.616  1.00 72.86  ? 124 TRP   A CH2 1 
ATOM   943  N N   . VAL   A 1 125 ? 17.649 4.803   -4.880  1.00 71.45  ? 125 VAL   A N   1 
ATOM   944  C CA  . VAL   A 1 125 ? 16.916 5.108   -6.116  1.00 71.43  ? 125 VAL   A CA  1 
ATOM   945  C C   . VAL   A 1 125 ? 17.873 5.400   -7.276  1.00 76.33  ? 125 VAL   A C   1 
ATOM   946  O O   . VAL   A 1 125 ? 17.620 4.992   -8.414  1.00 76.28  ? 125 VAL   A O   1 
ATOM   947  C CB  . VAL   A 1 125 ? 15.816 6.197   -5.933  1.00 75.02  ? 125 VAL   A CB  1 
ATOM   948  C CG1 . VAL   A 1 125 ? 14.675 5.676   -5.061  1.00 74.56  ? 125 VAL   A CG1 1 
ATOM   949  C CG2 . VAL   A 1 125 ? 16.382 7.506   -5.370  1.00 74.75  ? 125 VAL   A CG2 1 
ATOM   950  N N   . LYS   A 1 126 ? 18.979 6.100   -6.972  1.00 72.83  ? 126 LYS   A N   1 
ATOM   951  C CA  . LYS   A 1 126 ? 20.021 6.440   -7.939  1.00 71.99  ? 126 LYS   A CA  1 
ATOM   952  C C   . LYS   A 1 126 ? 21.180 5.436   -7.737  1.00 73.09  ? 126 LYS   A C   1 
ATOM   953  O O   . LYS   A 1 126 ? 21.488 5.093   -6.582  1.00 71.39  ? 126 LYS   A O   1 
ATOM   954  C CB  . LYS   A 1 126 ? 20.509 7.897   -7.759  1.00 74.14  ? 126 LYS   A CB  1 
ATOM   955  C CG  . LYS   A 1 126 ? 19.437 8.985   -7.902  1.00 82.54  ? 126 LYS   A CG  1 
ATOM   956  C CD  . LYS   A 1 126 ? 19.913 10.391  -7.459  1.00 87.96  ? 126 LYS   A CD  1 
ATOM   957  C CE  . LYS   A 1 126 ? 20.007 10.621  -5.955  1.00 92.14  ? 126 LYS   A CE  1 
ATOM   958  N NZ  . LYS   A 1 126 ? 18.689 10.562  -5.259  1.00 91.65  ? 126 LYS   A NZ  1 
ATOM   959  N N   . PRO   A 1 127 ? 21.818 4.932   -8.829  1.00 68.15  ? 127 PRO   A N   1 
ATOM   960  C CA  . PRO   A 1 127 ? 22.919 3.960   -8.644  1.00 66.65  ? 127 PRO   A CA  1 
ATOM   961  C C   . PRO   A 1 127 ? 24.137 4.471   -7.878  1.00 65.40  ? 127 PRO   A C   1 
ATOM   962  O O   . PRO   A 1 127 ? 24.415 5.676   -7.823  1.00 64.33  ? 127 PRO   A O   1 
ATOM   963  C CB  . PRO   A 1 127 ? 23.292 3.528   -10.076 1.00 68.83  ? 127 PRO   A CB  1 
ATOM   964  C CG  . PRO   A 1 127 ? 22.187 4.023   -10.965 1.00 73.90  ? 127 PRO   A CG  1 
ATOM   965  C CD  . PRO   A 1 127 ? 21.570 5.206   -10.263 1.00 69.56  ? 127 PRO   A CD  1 
ATOM   966  N N   . ILE   A 1 128 ? 24.853 3.531   -7.261  1.00 58.57  ? 128 ILE   A N   1 
ATOM   967  C CA  . ILE   A 1 128 ? 26.089 3.827   -6.558  1.00 56.10  ? 128 ILE   A CA  1 
ATOM   968  C C   . ILE   A 1 128 ? 27.148 3.210   -7.453  1.00 55.18  ? 128 ILE   A C   1 
ATOM   969  O O   . ILE   A 1 128 ? 27.038 2.035   -7.807  1.00 54.33  ? 128 ILE   A O   1 
ATOM   970  C CB  . ILE   A 1 128 ? 26.127 3.348   -5.086  1.00 58.48  ? 128 ILE   A CB  1 
ATOM   971  C CG1 . ILE   A 1 128 ? 25.112 4.154   -4.255  1.00 58.28  ? 128 ILE   A CG1 1 
ATOM   972  C CG2 . ILE   A 1 128 ? 27.544 3.510   -4.496  1.00 58.07  ? 128 ILE   A CG2 1 
ATOM   973  C CD1 . ILE   A 1 128 ? 24.643 3.495   -3.025  1.00 63.38  ? 128 ILE   A CD1 1 
ATOM   974  N N   . ILE   A 1 129 ? 28.116 4.040   -7.884  1.00 48.38  ? 129 ILE   A N   1 
ATOM   975  C CA  . ILE   A 1 129 ? 29.210 3.653   -8.766  1.00 46.45  ? 129 ILE   A CA  1 
ATOM   976  C C   . ILE   A 1 129 ? 30.460 3.499   -7.913  1.00 50.10  ? 129 ILE   A C   1 
ATOM   977  O O   . ILE   A 1 129 ? 30.989 4.489   -7.383  1.00 48.53  ? 129 ILE   A O   1 
ATOM   978  C CB  . ILE   A 1 129 ? 29.393 4.653   -9.950  1.00 48.48  ? 129 ILE   A CB  1 
ATOM   979  C CG1 . ILE   A 1 129 ? 28.054 4.875   -10.710 1.00 48.64  ? 129 ILE   A CG1 1 
ATOM   980  C CG2 . ILE   A 1 129 ? 30.508 4.182   -10.893 1.00 47.90  ? 129 ILE   A CG2 1 
ATOM   981  C CD1 . ILE   A 1 129 ? 28.039 5.945   -11.853 1.00 53.33  ? 129 ILE   A CD1 1 
ATOM   982  N N   . ILE   A 1 130 ? 30.919 2.239   -7.778  1.00 46.46  ? 130 ILE   A N   1 
ATOM   983  C CA  . ILE   A 1 130 ? 32.102 1.909   -6.989  1.00 45.53  ? 130 ILE   A CA  1 
ATOM   984  C C   . ILE   A 1 130 ? 33.337 1.614   -7.843  1.00 49.09  ? 130 ILE   A C   1 
ATOM   985  O O   . ILE   A 1 130 ? 33.334 0.707   -8.669  1.00 48.44  ? 130 ILE   A O   1 
ATOM   986  C CB  . ILE   A 1 130 ? 31.792 0.832   -5.904  1.00 47.51  ? 130 ILE   A CB  1 
ATOM   987  C CG1 . ILE   A 1 130 ? 30.679 1.348   -4.956  1.00 47.71  ? 130 ILE   A CG1 1 
ATOM   988  C CG2 . ILE   A 1 130 ? 33.057 0.469   -5.119  1.00 45.94  ? 130 ILE   A CG2 1 
ATOM   989  C CD1 . ILE   A 1 130 ? 30.001 0.356   -4.076  1.00 51.61  ? 130 ILE   A CD1 1 
ATOM   990  N N   . GLY   A 1 131 ? 34.381 2.382   -7.612  1.00 47.18  ? 131 GLY   A N   1 
ATOM   991  C CA  . GLY   A 1 131 ? 35.653 2.221   -8.299  1.00 48.42  ? 131 GLY   A CA  1 
ATOM   992  C C   . GLY   A 1 131 ? 36.721 1.701   -7.371  1.00 56.53  ? 131 GLY   A C   1 
ATOM   993  O O   . GLY   A 1 131 ? 36.943 2.256   -6.289  1.00 55.22  ? 131 GLY   A O   1 
ATOM   994  N N   . HIS   A 1 132 ? 37.381 0.622   -7.779  1.00 58.15  ? 132 HIS   A N   1 
ATOM   995  C CA  . HIS   A 1 132 ? 38.436 0.021   -6.975  1.00 59.96  ? 132 HIS   A CA  1 
ATOM   996  C C   . HIS   A 1 132 ? 39.796 0.300   -7.552  1.00 65.59  ? 132 HIS   A C   1 
ATOM   997  O O   . HIS   A 1 132 ? 39.957 0.404   -8.780  1.00 65.42  ? 132 HIS   A O   1 
ATOM   998  C CB  . HIS   A 1 132 ? 38.225 -1.484  -6.809  1.00 61.72  ? 132 HIS   A CB  1 
ATOM   999  C CG  . HIS   A 1 132 ? 37.190 -1.843  -5.794  1.00 65.77  ? 132 HIS   A CG  1 
ATOM   1000 N ND1 . HIS   A 1 132 ? 37.438 -1.722  -4.442  1.00 68.12  ? 132 HIS   A ND1 1 
ATOM   1001 C CD2 . HIS   A 1 132 ? 35.938 -2.326  -5.970  1.00 67.92  ? 132 HIS   A CD2 1 
ATOM   1002 C CE1 . HIS   A 1 132 ? 36.328 -2.120  -3.837  1.00 67.70  ? 132 HIS   A CE1 1 
ATOM   1003 N NE2 . HIS   A 1 132 ? 35.397 -2.490  -4.718  1.00 67.85  ? 132 HIS   A NE2 1 
ATOM   1004 N N   . HIS   A 1 133 ? 40.789 0.406   -6.653  1.00 63.30  ? 133 HIS   A N   1 
ATOM   1005 C CA  . HIS   A 1 133 ? 42.170 0.653   -7.047  1.00 97.07  ? 133 HIS   A CA  1 
ATOM   1006 C C   . HIS   A 1 133 ? 42.828 -0.619  -7.611  1.00 122.60 ? 133 HIS   A C   1 
ATOM   1007 O O   . HIS   A 1 133 ? 42.702 -1.703  -7.036  1.00 76.89  ? 133 HIS   A O   1 
ATOM   1008 C CB  . HIS   A 1 133 ? 42.978 1.237   -5.880  1.00 97.65  ? 133 HIS   A CB  1 
ATOM   1009 C CG  . HIS   A 1 133 ? 44.371 1.596   -6.278  1.00 101.00 ? 133 HIS   A CG  1 
ATOM   1010 N ND1 . HIS   A 1 133 ? 44.621 2.582   -7.215  1.00 102.76 ? 133 HIS   A ND1 1 
ATOM   1011 C CD2 . HIS   A 1 133 ? 45.547 1.059   -5.885  1.00 102.83 ? 133 HIS   A CD2 1 
ATOM   1012 C CE1 . HIS   A 1 133 ? 45.934 2.626   -7.349  1.00 102.16 ? 133 HIS   A CE1 1 
ATOM   1013 N NE2 . HIS   A 1 133 ? 46.534 1.725   -6.573  1.00 102.61 ? 133 HIS   A NE2 1 
ATOM   1014 N N   . ARG   A 1 140 ? 49.796 -7.892  -6.733  1.00 72.67  ? 140 ARG   A N   1 
ATOM   1015 C CA  . ARG   A 1 140 ? 50.670 -6.804  -6.292  1.00 72.58  ? 140 ARG   A CA  1 
ATOM   1016 C C   . ARG   A 1 140 ? 51.224 -6.982  -4.846  1.00 75.37  ? 140 ARG   A C   1 
ATOM   1017 O O   . ARG   A 1 140 ? 51.791 -6.024  -4.291  1.00 74.89  ? 140 ARG   A O   1 
ATOM   1018 C CB  . ARG   A 1 140 ? 49.951 -5.447  -6.453  1.00 73.48  ? 140 ARG   A CB  1 
ATOM   1019 N N   . ALA   A 1 141 ? 51.050 -8.195  -4.240  1.00 70.00  ? 141 ALA   A N   1 
ATOM   1020 C CA  . ALA   A 1 141 ? 51.519 -8.508  -2.874  1.00 68.79  ? 141 ALA   A CA  1 
ATOM   1021 C C   . ALA   A 1 141 ? 52.417 -9.743  -2.833  1.00 70.48  ? 141 ALA   A C   1 
ATOM   1022 O O   . ALA   A 1 141 ? 52.112 -10.768 -3.451  1.00 70.99  ? 141 ALA   A O   1 
ATOM   1023 C CB  . ALA   A 1 141 ? 50.353 -8.671  -1.911  1.00 69.20  ? 141 ALA   A CB  1 
ATOM   1024 N N   . THR   A 1 142 ? 53.534 -9.623  -2.100  1.00 63.44  ? 142 THR   A N   1 
ATOM   1025 C CA  . THR   A 1 142 ? 54.543 -10.656 -1.934  1.00 61.41  ? 142 THR   A CA  1 
ATOM   1026 C C   . THR   A 1 142 ? 54.373 -11.303 -0.562  1.00 60.85  ? 142 THR   A C   1 
ATOM   1027 O O   . THR   A 1 142 ? 54.759 -10.716 0.446   1.00 60.71  ? 142 THR   A O   1 
ATOM   1028 C CB  . THR   A 1 142 ? 55.950 -10.061 -2.150  1.00 70.10  ? 142 THR   A CB  1 
ATOM   1029 O OG1 . THR   A 1 142 ? 55.929 -9.127  -3.237  1.00 75.24  ? 142 THR   A OG1 1 
ATOM   1030 C CG2 . THR   A 1 142 ? 56.973 -11.115 -2.426  1.00 67.34  ? 142 THR   A CG2 1 
ATOM   1031 N N   . ASP   A 1 143 ? 53.802 -12.507 -0.527  1.00 53.80  ? 143 ASP   A N   1 
ATOM   1032 C CA  . ASP   A 1 143 ? 53.579 -13.227 0.715   1.00 52.84  ? 143 ASP   A CA  1 
ATOM   1033 C C   . ASP   A 1 143 ? 54.397 -14.508 0.811   1.00 54.96  ? 143 ASP   A C   1 
ATOM   1034 O O   . ASP   A 1 143 ? 54.645 -15.181 -0.199  1.00 55.51  ? 143 ASP   A O   1 
ATOM   1035 C CB  . ASP   A 1 143 ? 52.081 -13.515 0.916   1.00 54.92  ? 143 ASP   A CB  1 
ATOM   1036 C CG  . ASP   A 1 143 ? 51.470 -14.432 -0.124  1.00 63.39  ? 143 ASP   A CG  1 
ATOM   1037 O OD1 . ASP   A 1 143 ? 50.842 -15.429 0.270   1.00 63.60  ? 143 ASP   A OD1 1 
ATOM   1038 O OD2 . ASP   A 1 143 ? 51.616 -14.144 -1.334  1.00 69.75  ? 143 ASP   A OD2 1 
ATOM   1039 N N   . PHE   A 1 144 ? 54.799 -14.852 2.046   1.00 47.28  ? 144 PHE   A N   1 
ATOM   1040 C CA  . PHE   A 1 144 ? 55.584 -16.045 2.348   1.00 44.62  ? 144 PHE   A CA  1 
ATOM   1041 C C   . PHE   A 1 144 ? 55.324 -16.477 3.769   1.00 49.19  ? 144 PHE   A C   1 
ATOM   1042 O O   . PHE   A 1 144 ? 54.873 -15.670 4.597   1.00 48.49  ? 144 PHE   A O   1 
ATOM   1043 C CB  . PHE   A 1 144 ? 57.101 -15.785 2.148   1.00 44.67  ? 144 PHE   A CB  1 
ATOM   1044 C CG  . PHE   A 1 144 ? 57.699 -14.713 3.037   1.00 44.29  ? 144 PHE   A CG  1 
ATOM   1045 C CD1 . PHE   A 1 144 ? 58.407 -15.053 4.185   1.00 45.45  ? 144 PHE   A CD1 1 
ATOM   1046 C CD2 . PHE   A 1 144 ? 57.566 -13.361 2.716   1.00 44.53  ? 144 PHE   A CD2 1 
ATOM   1047 C CE1 . PHE   A 1 144 ? 58.962 -14.064 5.007   1.00 45.27  ? 144 PHE   A CE1 1 
ATOM   1048 C CE2 . PHE   A 1 144 ? 58.125 -12.373 3.536   1.00 46.60  ? 144 PHE   A CE2 1 
ATOM   1049 C CZ  . PHE   A 1 144 ? 58.830 -12.732 4.668   1.00 44.26  ? 144 PHE   A CZ  1 
ATOM   1050 N N   . VAL   A 1 145 ? 55.653 -17.743 4.069   1.00 46.06  ? 145 VAL   A N   1 
ATOM   1051 C CA  . VAL   A 1 145 ? 55.494 -18.246 5.417   1.00 45.46  ? 145 VAL   A CA  1 
ATOM   1052 C C   . VAL   A 1 145 ? 56.807 -18.080 6.164   1.00 48.72  ? 145 VAL   A C   1 
ATOM   1053 O O   . VAL   A 1 145 ? 57.875 -18.153 5.574   1.00 48.68  ? 145 VAL   A O   1 
ATOM   1054 C CB  . VAL   A 1 145 ? 54.817 -19.653 5.563   1.00 49.32  ? 145 VAL   A CB  1 
ATOM   1055 C CG1 . VAL   A 1 145 ? 53.860 -19.949 4.411   1.00 48.92  ? 145 VAL   A CG1 1 
ATOM   1056 C CG2 . VAL   A 1 145 ? 55.831 -20.775 5.738   1.00 49.00  ? 145 VAL   A CG2 1 
ATOM   1057 N N   . VAL   A 1 146 ? 56.712 -17.816 7.453   1.00 45.36  ? 146 VAL   A N   1 
ATOM   1058 C CA  . VAL   A 1 146 ? 57.840 -17.642 8.352   1.00 44.51  ? 146 VAL   A CA  1 
ATOM   1059 C C   . VAL   A 1 146 ? 57.864 -18.992 9.094   1.00 53.62  ? 146 VAL   A C   1 
ATOM   1060 O O   . VAL   A 1 146 ? 56.974 -19.251 9.926   1.00 54.20  ? 146 VAL   A O   1 
ATOM   1061 C CB  . VAL   A 1 146 ? 57.618 -16.412 9.286   1.00 45.52  ? 146 VAL   A CB  1 
ATOM   1062 C CG1 . VAL   A 1 146 ? 58.709 -16.310 10.354  1.00 44.52  ? 146 VAL   A CG1 1 
ATOM   1063 C CG2 . VAL   A 1 146 ? 57.508 -15.116 8.476   1.00 44.57  ? 146 VAL   A CG2 1 
ATOM   1064 N N   . PRO   A 1 147 ? 58.828 -19.886 8.748   1.00 51.94  ? 147 PRO   A N   1 
ATOM   1065 C CA  . PRO   A 1 147 ? 58.862 -21.220 9.388   1.00 51.62  ? 147 PRO   A CA  1 
ATOM   1066 C C   . PRO   A 1 147 ? 59.097 -21.231 10.896  1.00 55.80  ? 147 PRO   A C   1 
ATOM   1067 O O   . PRO   A 1 147 ? 58.421 -21.975 11.606  1.00 57.76  ? 147 PRO   A O   1 
ATOM   1068 C CB  . PRO   A 1 147 ? 59.942 -21.981 8.602   1.00 53.16  ? 147 PRO   A CB  1 
ATOM   1069 C CG  . PRO   A 1 147 ? 60.797 -20.929 7.997   1.00 57.76  ? 147 PRO   A CG  1 
ATOM   1070 C CD  . PRO   A 1 147 ? 59.913 -19.732 7.754   1.00 53.60  ? 147 PRO   A CD  1 
ATOM   1071 N N   . GLY   A 1 148 ? 60.018 -20.412 11.376  1.00 50.08  ? 148 GLY   A N   1 
ATOM   1072 C CA  . GLY   A 1 148 ? 60.317 -20.351 12.796  1.00 49.59  ? 148 GLY   A CA  1 
ATOM   1073 C C   . GLY   A 1 148 ? 60.861 -19.007 13.220  1.00 54.59  ? 148 GLY   A C   1 
ATOM   1074 O O   . GLY   A 1 148 ? 60.754 -18.041 12.457  1.00 54.42  ? 148 GLY   A O   1 
ATOM   1075 N N   . PRO   A 1 149 ? 61.452 -18.905 14.440  1.00 51.94  ? 149 PRO   A N   1 
ATOM   1076 C CA  . PRO   A 1 149 ? 62.000 -17.610 14.880  1.00 51.68  ? 149 PRO   A CA  1 
ATOM   1077 C C   . PRO   A 1 149 ? 62.994 -17.004 13.894  1.00 55.04  ? 149 PRO   A C   1 
ATOM   1078 O O   . PRO   A 1 149 ? 63.702 -17.719 13.185  1.00 54.79  ? 149 PRO   A O   1 
ATOM   1079 C CB  . PRO   A 1 149 ? 62.656 -17.918 16.231  1.00 53.13  ? 149 PRO   A CB  1 
ATOM   1080 C CG  . PRO   A 1 149 ? 62.057 -19.172 16.685  1.00 57.33  ? 149 PRO   A CG  1 
ATOM   1081 C CD  . PRO   A 1 149 ? 61.674 -19.952 15.460  1.00 53.24  ? 149 PRO   A CD  1 
ATOM   1082 N N   . GLY   A 1 150 ? 63.006 -15.680 13.864  1.00 50.75  ? 150 GLY   A N   1 
ATOM   1083 C CA  . GLY   A 1 150 ? 63.853 -14.890 12.991  1.00 49.43  ? 150 GLY   A CA  1 
ATOM   1084 C C   . GLY   A 1 150 ? 63.250 -13.538 12.696  1.00 51.48  ? 150 GLY   A C   1 
ATOM   1085 O O   . GLY   A 1 150 ? 62.104 -13.261 13.060  1.00 50.82  ? 150 GLY   A O   1 
ATOM   1086 N N   . LYS   A 1 151 ? 64.034 -12.695 12.022  1.00 47.72  ? 151 LYS   A N   1 
ATOM   1087 C CA  . LYS   A 1 151 ? 63.662 -11.342 11.660  1.00 46.80  ? 151 LYS   A CA  1 
ATOM   1088 C C   . LYS   A 1 151 ? 63.101 -11.204 10.252  1.00 49.46  ? 151 LYS   A C   1 
ATOM   1089 O O   . LYS   A 1 151 ? 63.631 -11.782 9.298   1.00 50.92  ? 151 LYS   A O   1 
ATOM   1090 C CB  . LYS   A 1 151 ? 64.867 -10.401 11.820  1.00 49.15  ? 151 LYS   A CB  1 
ATOM   1091 C CG  . LYS   A 1 151 ? 64.903 -9.643  13.137  1.00 66.20  ? 151 LYS   A CG  1 
ATOM   1092 C CD  . LYS   A 1 151 ? 65.886 -8.471  13.070  1.00 76.20  ? 151 LYS   A CD  1 
ATOM   1093 C CE  . LYS   A 1 151 ? 66.106 -7.838  14.428  1.00 88.62  ? 151 LYS   A CE  1 
ATOM   1094 N NZ  . LYS   A 1 151 ? 66.790 -6.518  14.329  1.00 98.36  ? 151 LYS   A NZ  1 
ATOM   1095 N N   . VAL   A 1 152 ? 62.021 -10.423 10.138  1.00 42.67  ? 152 VAL   A N   1 
ATOM   1096 C CA  . VAL   A 1 152 ? 61.392 -10.052 8.875   1.00 40.26  ? 152 VAL   A CA  1 
ATOM   1097 C C   . VAL   A 1 152 ? 61.585 -8.542  8.794   1.00 41.24  ? 152 VAL   A C   1 
ATOM   1098 O O   . VAL   A 1 152 ? 61.159 -7.790  9.685   1.00 39.57  ? 152 VAL   A O   1 
ATOM   1099 C CB  . VAL   A 1 152 ? 59.913 -10.486 8.640   1.00 42.22  ? 152 VAL   A CB  1 
ATOM   1100 C CG1 . VAL   A 1 152 ? 59.394 -9.930  7.309   1.00 41.03  ? 152 VAL   A CG1 1 
ATOM   1101 C CG2 . VAL   A 1 152 ? 59.771 -12.008 8.669   1.00 41.67  ? 152 VAL   A CG2 1 
ATOM   1102 N N   . GLU   A 1 153 ? 62.268 -8.116  7.745   1.00 37.29  ? 153 GLU   A N   1 
ATOM   1103 C CA  . GLU   A 1 153 ? 62.542 -6.709  7.510   1.00 37.35  ? 153 GLU   A CA  1 
ATOM   1104 C C   . GLU   A 1 153 ? 62.094 -6.284  6.134   1.00 40.99  ? 153 GLU   A C   1 
ATOM   1105 O O   . GLU   A 1 153 ? 62.016 -7.091  5.218   1.00 41.04  ? 153 GLU   A O   1 
ATOM   1106 C CB  . GLU   A 1 153 ? 64.040 -6.403  7.679   1.00 38.91  ? 153 GLU   A CB  1 
ATOM   1107 C CG  . GLU   A 1 153 ? 64.587 -6.730  9.059   1.00 49.76  ? 153 GLU   A CG  1 
ATOM   1108 C CD  . GLU   A 1 153 ? 66.065 -6.463  9.226   1.00 71.44  ? 153 GLU   A CD  1 
ATOM   1109 O OE1 . GLU   A 1 153 ? 66.421 -5.658  10.117  1.00 68.75  ? 153 GLU   A OE1 1 
ATOM   1110 O OE2 . GLU   A 1 153 ? 66.866 -7.051  8.464   1.00 70.96  ? 153 GLU   A OE2 1 
ATOM   1111 N N   . ILE   A 1 154 ? 61.815 -5.005  5.986   1.00 37.40  ? 154 ILE   A N   1 
ATOM   1112 C CA  . ILE   A 1 154 ? 61.435 -4.431  4.709   1.00 36.66  ? 154 ILE   A CA  1 
ATOM   1113 C C   . ILE   A 1 154 ? 62.407 -3.289  4.490   1.00 40.62  ? 154 ILE   A C   1 
ATOM   1114 O O   . ILE   A 1 154 ? 62.601 -2.453  5.386   1.00 39.60  ? 154 ILE   A O   1 
ATOM   1115 C CB  . ILE   A 1 154 ? 59.910 -4.117  4.545   1.00 39.18  ? 154 ILE   A CB  1 
ATOM   1116 C CG1 . ILE   A 1 154 ? 59.587 -3.652  3.117   1.00 38.97  ? 154 ILE   A CG1 1 
ATOM   1117 C CG2 . ILE   A 1 154 ? 59.368 -3.169  5.634   1.00 39.39  ? 154 ILE   A CG2 1 
ATOM   1118 C CD1 . ILE   A 1 154 ? 58.109 -3.791  2.713   1.00 44.56  ? 154 ILE   A CD1 1 
ATOM   1119 N N   . THR   A 1 155 ? 63.084 -3.307  3.330   1.00 38.44  ? 155 THR   A N   1 
ATOM   1120 C CA  . THR   A 1 155 ? 64.099 -2.310  3.018   1.00 38.76  ? 155 THR   A CA  1 
ATOM   1121 C C   . THR   A 1 155 ? 63.830 -1.503  1.793   1.00 42.64  ? 155 THR   A C   1 
ATOM   1122 O O   . THR   A 1 155 ? 63.204 -1.980  0.852   1.00 43.09  ? 155 THR   A O   1 
ATOM   1123 C CB  . THR   A 1 155 ? 65.500 -2.943  2.922   1.00 48.60  ? 155 THR   A CB  1 
ATOM   1124 O OG1 . THR   A 1 155 ? 65.516 -3.868  1.836   1.00 55.56  ? 155 THR   A OG1 1 
ATOM   1125 C CG2 . THR   A 1 155 ? 65.938 -3.624  4.214   1.00 45.94  ? 155 THR   A CG2 1 
ATOM   1126 N N   . TYR   A 1 156 ? 64.347 -0.281  1.790   1.00 38.50  ? 156 TYR   A N   1 
ATOM   1127 C CA  . TYR   A 1 156 ? 64.261 0.603   0.646   1.00 38.39  ? 156 TYR   A CA  1 
ATOM   1128 C C   . TYR   A 1 156 ? 65.671 0.993   0.300   1.00 41.71  ? 156 TYR   A C   1 
ATOM   1129 O O   . TYR   A 1 156 ? 66.369 1.600   1.107   1.00 39.93  ? 156 TYR   A O   1 
ATOM   1130 C CB  . TYR   A 1 156 ? 63.352 1.820   0.885   1.00 40.21  ? 156 TYR   A CB  1 
ATOM   1131 C CG  . TYR   A 1 156 ? 63.527 2.919   -0.143  1.00 42.87  ? 156 TYR   A CG  1 
ATOM   1132 C CD1 . TYR   A 1 156 ? 63.962 4.187   0.230   1.00 43.81  ? 156 TYR   A CD1 1 
ATOM   1133 C CD2 . TYR   A 1 156 ? 63.264 2.688   -1.495  1.00 44.07  ? 156 TYR   A CD2 1 
ATOM   1134 C CE1 . TYR   A 1 156 ? 64.147 5.196   -0.714  1.00 41.68  ? 156 TYR   A CE1 1 
ATOM   1135 C CE2 . TYR   A 1 156 ? 63.453 3.688   -2.448  1.00 44.76  ? 156 TYR   A CE2 1 
ATOM   1136 C CZ  . TYR   A 1 156 ? 63.890 4.944   -2.050  1.00 47.90  ? 156 TYR   A CZ  1 
ATOM   1137 O OH  . TYR   A 1 156 ? 64.033 5.950   -2.975  1.00 45.55  ? 156 TYR   A OH  1 
ATOM   1138 N N   . THR   A 1 157 ? 66.108 0.583   -0.894  1.00 40.62  ? 157 THR   A N   1 
ATOM   1139 C CA  . THR   A 1 157 ? 67.439 0.877   -1.402  1.00 39.78  ? 157 THR   A CA  1 
ATOM   1140 C C   . THR   A 1 157 ? 67.278 1.957   -2.466  1.00 43.22  ? 157 THR   A C   1 
ATOM   1141 O O   . THR   A 1 157 ? 66.816 1.650   -3.566  1.00 44.13  ? 157 THR   A O   1 
ATOM   1142 C CB  . THR   A 1 157 ? 68.124 -0.401  -1.918  1.00 45.24  ? 157 THR   A CB  1 
ATOM   1143 O OG1 . THR   A 1 157 ? 68.140 -1.401  -0.881  1.00 49.14  ? 157 THR   A OG1 1 
ATOM   1144 C CG2 . THR   A 1 157 ? 69.551 -0.137  -2.418  1.00 36.53  ? 157 THR   A CG2 1 
ATOM   1145 N N   . PRO   A 1 158 ? 67.619 3.231   -2.174  1.00 38.43  ? 158 PRO   A N   1 
ATOM   1146 C CA  . PRO   A 1 158 ? 67.491 4.278   -3.215  1.00 38.53  ? 158 PRO   A CA  1 
ATOM   1147 C C   . PRO   A 1 158 ? 68.371 3.986   -4.439  1.00 43.42  ? 158 PRO   A C   1 
ATOM   1148 O O   . PRO   A 1 158 ? 69.483 3.486   -4.295  1.00 42.61  ? 158 PRO   A O   1 
ATOM   1149 C CB  . PRO   A 1 158 ? 67.930 5.571   -2.494  1.00 39.34  ? 158 PRO   A CB  1 
ATOM   1150 C CG  . PRO   A 1 158 ? 67.920 5.240   -1.050  1.00 42.37  ? 158 PRO   A CG  1 
ATOM   1151 C CD  . PRO   A 1 158 ? 68.176 3.781   -0.923  1.00 38.15  ? 158 PRO   A CD  1 
ATOM   1152 N N   . SER   A 1 159 ? 67.863 4.284   -5.638  1.00 43.14  ? 159 SER   A N   1 
ATOM   1153 C CA  . SER   A 1 159 ? 68.582 4.049   -6.901  1.00 43.86  ? 159 SER   A CA  1 
ATOM   1154 C C   . SER   A 1 159 ? 69.723 5.034   -7.114  1.00 48.64  ? 159 SER   A C   1 
ATOM   1155 O O   . SER   A 1 159 ? 70.598 4.770   -7.933  1.00 49.92  ? 159 SER   A O   1 
ATOM   1156 C CB  . SER   A 1 159 ? 67.624 4.080   -8.089  1.00 47.65  ? 159 SER   A CB  1 
ATOM   1157 O OG  . SER   A 1 159 ? 66.976 5.336   -8.181  1.00 59.49  ? 159 SER   A OG  1 
ATOM   1158 N N   . ASP   A 1 160 ? 69.731 6.145   -6.364  1.00 44.15  ? 160 ASP   A N   1 
ATOM   1159 C CA  . ASP   A 1 160 ? 70.754 7.176   -6.465  1.00 44.12  ? 160 ASP   A CA  1 
ATOM   1160 C C   . ASP   A 1 160 ? 71.977 6.944   -5.596  1.00 49.63  ? 160 ASP   A C   1 
ATOM   1161 O O   . ASP   A 1 160 ? 72.830 7.831   -5.491  1.00 50.08  ? 160 ASP   A O   1 
ATOM   1162 C CB  . ASP   A 1 160 ? 70.157 8.596   -6.313  1.00 45.73  ? 160 ASP   A CB  1 
ATOM   1163 C CG  . ASP   A 1 160 ? 69.580 8.966   -4.950  1.00 54.78  ? 160 ASP   A CG  1 
ATOM   1164 O OD1 . ASP   A 1 160 ? 69.683 8.139   -4.006  1.00 53.18  ? 160 ASP   A OD1 1 
ATOM   1165 O OD2 . ASP   A 1 160 ? 69.035 10.084  -4.824  1.00 63.99  ? 160 ASP   A OD2 1 
ATOM   1166 N N   . GLY   A 1 161 ? 72.048 5.760   -4.988  1.00 46.13  ? 161 GLY   A N   1 
ATOM   1167 C CA  . GLY   A 1 161 ? 73.152 5.335   -4.137  1.00 45.61  ? 161 GLY   A CA  1 
ATOM   1168 C C   . GLY   A 1 161 ? 73.109 5.800   -2.703  1.00 51.40  ? 161 GLY   A C   1 
ATOM   1169 O O   . GLY   A 1 161 ? 73.933 5.347   -1.896  1.00 50.67  ? 161 GLY   A O   1 
ATOM   1170 N N   . THR   A 1 162 ? 72.149 6.709   -2.360  1.00 49.48  ? 162 THR   A N   1 
ATOM   1171 C CA  . THR   A 1 162 ? 72.000 7.200   -0.983  1.00 49.67  ? 162 THR   A CA  1 
ATOM   1172 C C   . THR   A 1 162 ? 71.645 6.051   -0.005  1.00 55.03  ? 162 THR   A C   1 
ATOM   1173 O O   . THR   A 1 162 ? 71.222 4.973   -0.432  1.00 54.87  ? 162 THR   A O   1 
ATOM   1174 C CB  . THR   A 1 162 ? 71.097 8.441   -0.886  1.00 58.19  ? 162 THR   A CB  1 
ATOM   1175 O OG1 . THR   A 1 162 ? 69.773 8.123   -1.302  1.00 59.52  ? 162 THR   A OG1 1 
ATOM   1176 C CG2 . THR   A 1 162 ? 71.624 9.623   -1.678  1.00 54.84  ? 162 THR   A CG2 1 
ATOM   1177 N N   . GLN   A 1 163 ? 71.871 6.279   1.292   1.00 53.09  ? 163 GLN   A N   1 
ATOM   1178 C CA  . GLN   A 1 163 ? 71.658 5.334   2.386   1.00 53.07  ? 163 GLN   A CA  1 
ATOM   1179 C C   . GLN   A 1 163 ? 70.363 4.519   2.318   1.00 56.11  ? 163 GLN   A C   1 
ATOM   1180 O O   . GLN   A 1 163 ? 69.268 5.069   2.191   1.00 55.37  ? 163 GLN   A O   1 
ATOM   1181 C CB  . GLN   A 1 163 ? 71.793 6.055   3.746   1.00 54.92  ? 163 GLN   A CB  1 
ATOM   1182 C CG  . GLN   A 1 163 ? 71.728 5.140   4.981   1.00 76.16  ? 163 GLN   A CG  1 
ATOM   1183 C CD  . GLN   A 1 163 ? 73.070 4.612   5.417   1.00 100.03 ? 163 GLN   A CD  1 
ATOM   1184 O OE1 . GLN   A 1 163 ? 73.808 3.979   4.650   1.00 98.07  ? 163 GLN   A OE1 1 
ATOM   1185 N NE2 . GLN   A 1 163 ? 73.409 4.853   6.676   1.00 93.06  ? 163 GLN   A NE2 1 
ATOM   1186 N N   . LYS   A 1 164 ? 70.530 3.190   2.412   1.00 52.40  ? 164 LYS   A N   1 
ATOM   1187 C CA  . LYS   A 1 164 ? 69.498 2.162   2.451   1.00 50.95  ? 164 LYS   A CA  1 
ATOM   1188 C C   . LYS   A 1 164 ? 68.703 2.339   3.770   1.00 52.23  ? 164 LYS   A C   1 
ATOM   1189 O O   . LYS   A 1 164 ? 69.297 2.582   4.825   1.00 52.62  ? 164 LYS   A O   1 
ATOM   1190 C CB  . LYS   A 1 164 ? 70.185 0.784   2.438   1.00 52.83  ? 164 LYS   A CB  1 
ATOM   1191 C CG  . LYS   A 1 164 ? 69.256 -0.423  2.318   1.00 65.32  ? 164 LYS   A CG  1 
ATOM   1192 C CD  . LYS   A 1 164 ? 69.844 -1.586  3.090   1.00 72.96  ? 164 LYS   A CD  1 
ATOM   1193 C CE  . LYS   A 1 164 ? 69.518 -2.936  2.501   1.00 87.29  ? 164 LYS   A CE  1 
ATOM   1194 N NZ  . LYS   A 1 164 ? 70.182 -4.034  3.266   1.00 96.42  ? 164 LYS   A NZ  1 
ATOM   1195 N N   . VAL   A 1 165 ? 67.377 2.217   3.702   1.00 45.85  ? 165 VAL   A N   1 
ATOM   1196 C CA  . VAL   A 1 165 ? 66.483 2.348   4.863   1.00 45.11  ? 165 VAL   A CA  1 
ATOM   1197 C C   . VAL   A 1 165 ? 65.935 0.952   5.213   1.00 47.23  ? 165 VAL   A C   1 
ATOM   1198 O O   . VAL   A 1 165 ? 65.478 0.225   4.315   1.00 46.70  ? 165 VAL   A O   1 
ATOM   1199 C CB  . VAL   A 1 165 ? 65.350 3.366   4.575   1.00 49.62  ? 165 VAL   A CB  1 
ATOM   1200 C CG1 . VAL   A 1 165 ? 64.601 3.732   5.838   1.00 49.45  ? 165 VAL   A CG1 1 
ATOM   1201 C CG2 . VAL   A 1 165 ? 65.904 4.621   3.918   1.00 49.90  ? 165 VAL   A CG2 1 
ATOM   1202 N N   . THR   A 1 166 ? 66.007 0.568   6.505   1.00 41.88  ? 166 THR   A N   1 
ATOM   1203 C CA  . THR   A 1 166 ? 65.525 -0.743  6.984   1.00 40.63  ? 166 THR   A CA  1 
ATOM   1204 C C   . THR   A 1 166 ? 64.449 -0.578  8.050   1.00 40.52  ? 166 THR   A C   1 
ATOM   1205 O O   . THR   A 1 166 ? 64.671 0.118   9.033   1.00 38.88  ? 166 THR   A O   1 
ATOM   1206 C CB  . THR   A 1 166 ? 66.686 -1.642  7.474   1.00 45.02  ? 166 THR   A CB  1 
ATOM   1207 O OG1 . THR   A 1 166 ? 67.614 -1.840  6.405   1.00 49.55  ? 166 THR   A OG1 1 
ATOM   1208 C CG2 . THR   A 1 166 ? 66.208 -2.995  7.985   1.00 38.80  ? 166 THR   A CG2 1 
ATOM   1209 N N   . TYR   A 1 167 ? 63.292 -1.209  7.840   1.00 35.38  ? 167 TYR   A N   1 
ATOM   1210 C CA  . TYR   A 1 167 ? 62.169 -1.195  8.780   1.00 35.00  ? 167 TYR   A CA  1 
ATOM   1211 C C   . TYR   A 1 167 ? 61.974 -2.613  9.284   1.00 40.11  ? 167 TYR   A C   1 
ATOM   1212 O O   . TYR   A 1 167 ? 62.007 -3.572  8.498   1.00 39.17  ? 167 TYR   A O   1 
ATOM   1213 C CB  . TYR   A 1 167 ? 60.868 -0.736  8.098   1.00 36.50  ? 167 TYR   A CB  1 
ATOM   1214 C CG  . TYR   A 1 167 ? 60.913 0.688   7.598   1.00 39.73  ? 167 TYR   A CG  1 
ATOM   1215 C CD1 . TYR   A 1 167 ? 61.296 0.977   6.295   1.00 41.79  ? 167 TYR   A CD1 1 
ATOM   1216 C CD2 . TYR   A 1 167 ? 60.583 1.748   8.430   1.00 41.18  ? 167 TYR   A CD2 1 
ATOM   1217 C CE1 . TYR   A 1 167 ? 61.379 2.286   5.841   1.00 43.37  ? 167 TYR   A CE1 1 
ATOM   1218 C CE2 . TYR   A 1 167 ? 60.652 3.065   7.983   1.00 42.58  ? 167 TYR   A CE2 1 
ATOM   1219 C CZ  . TYR   A 1 167 ? 61.056 3.331   6.689   1.00 51.33  ? 167 TYR   A CZ  1 
ATOM   1220 O OH  . TYR   A 1 167 ? 61.107 4.631   6.245   1.00 53.78  ? 167 TYR   A OH  1 
ATOM   1221 N N   . LEU   A 1 168 ? 61.780 -2.760  10.587  1.00 38.87  ? 168 LEU   A N   1 
ATOM   1222 C CA  . LEU   A 1 168 ? 61.520 -4.082  11.133  1.00 39.25  ? 168 LEU   A CA  1 
ATOM   1223 C C   . LEU   A 1 168 ? 60.006 -4.369  10.959  1.00 43.15  ? 168 LEU   A C   1 
ATOM   1224 O O   . LEU   A 1 168 ? 59.172 -3.555  11.391  1.00 42.80  ? 168 LEU   A O   1 
ATOM   1225 C CB  . LEU   A 1 168 ? 61.913 -4.156  12.612  1.00 39.19  ? 168 LEU   A CB  1 
ATOM   1226 C CG  . LEU   A 1 168 ? 61.658 -5.531  13.299  1.00 43.30  ? 168 LEU   A CG  1 
ATOM   1227 C CD1 . LEU   A 1 168 ? 62.592 -6.638  12.752  1.00 41.19  ? 168 LEU   A CD1 1 
ATOM   1228 C CD2 . LEU   A 1 168 ? 61.776 -5.409  14.788  1.00 42.78  ? 168 LEU   A CD2 1 
ATOM   1229 N N   . VAL   A 1 169 ? 59.657 -5.487  10.304  1.00 38.12  ? 169 VAL   A N   1 
ATOM   1230 C CA  . VAL   A 1 169 ? 58.247 -5.827  10.152  1.00 38.39  ? 169 VAL   A CA  1 
ATOM   1231 C C   . VAL   A 1 169 ? 57.847 -6.517  11.470  1.00 45.41  ? 169 VAL   A C   1 
ATOM   1232 O O   . VAL   A 1 169 ? 56.908 -6.082  12.140  1.00 45.44  ? 169 VAL   A O   1 
ATOM   1233 C CB  . VAL   A 1 169 ? 57.904 -6.653  8.883   1.00 41.76  ? 169 VAL   A CB  1 
ATOM   1234 C CG1 . VAL   A 1 169 ? 56.425 -7.018  8.853   1.00 41.45  ? 169 VAL   A CG1 1 
ATOM   1235 C CG2 . VAL   A 1 169 ? 58.287 -5.894  7.615   1.00 41.15  ? 169 VAL   A CG2 1 
ATOM   1236 N N   . HIS   A 1 170 ? 58.606 -7.555  11.851  1.00 43.86  ? 170 HIS   A N   1 
ATOM   1237 C CA  . HIS   A 1 170 ? 58.449 -8.318  13.086  1.00 44.23  ? 170 HIS   A CA  1 
ATOM   1238 C C   . HIS   A 1 170 ? 59.647 -9.194  13.338  1.00 48.72  ? 170 HIS   A C   1 
ATOM   1239 O O   . HIS   A 1 170 ? 60.221 -9.757  12.407  1.00 47.32  ? 170 HIS   A O   1 
ATOM   1240 C CB  . HIS   A 1 170 ? 57.170 -9.197  13.086  1.00 45.07  ? 170 HIS   A CB  1 
ATOM   1241 C CG  . HIS   A 1 170 ? 56.827 -9.797  14.423  1.00 48.70  ? 170 HIS   A CG  1 
ATOM   1242 N ND1 . HIS   A 1 170 ? 56.648 -9.008  15.551  1.00 50.52  ? 170 HIS   A ND1 1 
ATOM   1243 C CD2 . HIS   A 1 170 ? 56.619 -11.092 14.765  1.00 50.71  ? 170 HIS   A CD2 1 
ATOM   1244 C CE1 . HIS   A 1 170 ? 56.356 -9.846  16.534  1.00 49.54  ? 170 HIS   A CE1 1 
ATOM   1245 N NE2 . HIS   A 1 170 ? 56.323 -11.107 16.110  1.00 49.98  ? 170 HIS   A NE2 1 
ATOM   1246 N N   . ASN   A 1 171 ? 60.019 -9.302  14.613  1.00 48.04  ? 171 ASN   A N   1 
ATOM   1247 C CA  . ASN   A 1 171 ? 61.057 -10.200 15.086  1.00 48.51  ? 171 ASN   A CA  1 
ATOM   1248 C C   . ASN   A 1 171 ? 60.278 -11.337 15.768  1.00 53.35  ? 171 ASN   A C   1 
ATOM   1249 O O   . ASN   A 1 171 ? 59.752 -11.148 16.873  1.00 53.64  ? 171 ASN   A O   1 
ATOM   1250 C CB  . ASN   A 1 171 ? 62.022 -9.526  16.066  1.00 49.26  ? 171 ASN   A CB  1 
ATOM   1251 C CG  . ASN   A 1 171 ? 63.117 -10.464 16.559  1.00 80.75  ? 171 ASN   A CG  1 
ATOM   1252 O OD1 . ASN   A 1 171 ? 63.275 -11.617 16.106  1.00 68.80  ? 171 ASN   A OD1 1 
ATOM   1253 N ND2 . ASN   A 1 171 ? 63.907 -9.991  17.509  1.00 79.02  ? 171 ASN   A ND2 1 
ATOM   1254 N N   . PHE   A 1 172 ? 60.145 -12.487 15.085  1.00 49.55  ? 172 PHE   A N   1 
ATOM   1255 C CA  . PHE   A 1 172 ? 59.444 -13.654 15.634  1.00 48.63  ? 172 PHE   A CA  1 
ATOM   1256 C C   . PHE   A 1 172 ? 60.410 -14.322 16.638  1.00 56.94  ? 172 PHE   A C   1 
ATOM   1257 O O   . PHE   A 1 172 ? 61.493 -14.767 16.250  1.00 55.10  ? 172 PHE   A O   1 
ATOM   1258 C CB  . PHE   A 1 172 ? 59.059 -14.639 14.518  1.00 48.98  ? 172 PHE   A CB  1 
ATOM   1259 C CG  . PHE   A 1 172 ? 58.075 -14.142 13.482  1.00 48.66  ? 172 PHE   A CG  1 
ATOM   1260 C CD1 . PHE   A 1 172 ? 58.478 -13.271 12.473  1.00 50.49  ? 172 PHE   A CD1 1 
ATOM   1261 C CD2 . PHE   A 1 172 ? 56.767 -14.599 13.471  1.00 49.25  ? 172 PHE   A CD2 1 
ATOM   1262 C CE1 . PHE   A 1 172 ? 57.575 -12.831 11.499  1.00 50.35  ? 172 PHE   A CE1 1 
ATOM   1263 C CE2 . PHE   A 1 172 ? 55.867 -14.163 12.494  1.00 52.27  ? 172 PHE   A CE2 1 
ATOM   1264 C CZ  . PHE   A 1 172 ? 56.275 -13.278 11.517  1.00 49.86  ? 172 PHE   A CZ  1 
ATOM   1265 N N   . GLU   A 1 173 ? 60.038 -14.334 17.935  1.00 58.31  ? 173 GLU   A N   1 
ATOM   1266 C CA  . GLU   A 1 173 ? 60.846 -14.907 19.015  1.00 59.78  ? 173 GLU   A CA  1 
ATOM   1267 C C   . GLU   A 1 173 ? 60.357 -16.318 19.369  1.00 67.62  ? 173 GLU   A C   1 
ATOM   1268 O O   . GLU   A 1 173 ? 61.146 -17.262 19.325  1.00 67.54  ? 173 GLU   A O   1 
ATOM   1269 C CB  . GLU   A 1 173 ? 60.849 -13.976 20.241  1.00 61.35  ? 173 GLU   A CB  1 
ATOM   1270 C CG  . GLU   A 1 173 ? 61.575 -12.650 20.035  1.00 70.89  ? 173 GLU   A CG  1 
ATOM   1271 C CD  . GLU   A 1 173 ? 61.265 -11.529 21.019  1.00 93.56  ? 173 GLU   A CD  1 
ATOM   1272 O OE1 . GLU   A 1 173 ? 60.788 -11.816 22.144  1.00 88.90  ? 173 GLU   A OE1 1 
ATOM   1273 O OE2 . GLU   A 1 173 ? 61.505 -10.352 20.658  1.00 82.28  ? 173 GLU   A OE2 1 
ATOM   1274 N N   . GLU   A 1 174 ? 59.043 -16.463 19.677  1.00 67.77  ? 174 GLU   A N   1 
ATOM   1275 C CA  . GLU   A 1 174 ? 58.359 -17.732 20.010  1.00 68.35  ? 174 GLU   A CA  1 
ATOM   1276 C C   . GLU   A 1 174 ? 58.348 -18.584 18.749  1.00 72.40  ? 174 GLU   A C   1 
ATOM   1277 O O   . GLU   A 1 174 ? 58.160 -19.803 18.793  1.00 73.61  ? 174 GLU   A O   1 
ATOM   1278 C CB  . GLU   A 1 174 ? 56.921 -17.473 20.494  1.00 69.73  ? 174 GLU   A CB  1 
ATOM   1279 N N   . GLY   A 1 175 ? 58.552 -17.895 17.642  1.00 66.73  ? 175 GLY   A N   1 
ATOM   1280 C CA  . GLY   A 1 175 ? 58.696 -18.433 16.303  1.00 65.56  ? 175 GLY   A CA  1 
ATOM   1281 C C   . GLY   A 1 175 ? 57.557 -19.131 15.636  1.00 65.49  ? 175 GLY   A C   1 
ATOM   1282 O O   . GLY   A 1 175 ? 56.902 -19.989 16.228  1.00 65.37  ? 175 GLY   A O   1 
ATOM   1283 N N   . GLY   A 1 176 ? 57.394 -18.772 14.372  1.00 58.52  ? 176 GLY   A N   1 
ATOM   1284 C CA  . GLY   A 1 176 ? 56.379 -19.308 13.487  1.00 56.62  ? 176 GLY   A CA  1 
ATOM   1285 C C   . GLY   A 1 176 ? 55.372 -18.250 13.121  1.00 56.82  ? 176 GLY   A C   1 
ATOM   1286 O O   . GLY   A 1 176 ? 54.934 -17.485 13.985  1.00 55.97  ? 176 GLY   A O   1 
ATOM   1287 N N   . GLY   A 1 177 ? 55.014 -18.212 11.842  1.00 51.38  ? 177 GLY   A N   1 
ATOM   1288 C CA  . GLY   A 1 177 ? 54.035 -17.263 11.343  1.00 50.57  ? 177 GLY   A CA  1 
ATOM   1289 C C   . GLY   A 1 177 ? 53.978 -17.129 9.842   1.00 53.79  ? 177 GLY   A C   1 
ATOM   1290 O O   . GLY   A 1 177 ? 54.297 -18.058 9.095   1.00 54.21  ? 177 GLY   A O   1 
ATOM   1291 N N   . VAL   A 1 178 ? 53.560 -15.951 9.401   1.00 48.54  ? 178 VAL   A N   1 
ATOM   1292 C CA  . VAL   A 1 178 ? 53.413 -15.628 7.994   1.00 47.43  ? 178 VAL   A CA  1 
ATOM   1293 C C   . VAL   A 1 178 ? 53.717 -14.116 7.790   1.00 49.37  ? 178 VAL   A C   1 
ATOM   1294 O O   . VAL   A 1 178 ? 53.527 -13.342 8.722   1.00 49.34  ? 178 VAL   A O   1 
ATOM   1295 C CB  . VAL   A 1 178 ? 51.999 -16.109 7.512   1.00 51.12  ? 178 VAL   A CB  1 
ATOM   1296 C CG1 . VAL   A 1 178 ? 50.871 -15.231 8.029   1.00 50.64  ? 178 VAL   A CG1 1 
ATOM   1297 C CG2 . VAL   A 1 178 ? 51.931 -16.253 6.007   1.00 51.06  ? 178 VAL   A CG2 1 
ATOM   1298 N N   . ALA   A 1 179 ? 54.232 -13.702 6.613   1.00 44.48  ? 179 ALA   A N   1 
ATOM   1299 C CA  . ALA   A 1 179 ? 54.533 -12.279 6.350   1.00 42.95  ? 179 ALA   A CA  1 
ATOM   1300 C C   . ALA   A 1 179 ? 54.287 -11.868 4.907   1.00 47.03  ? 179 ALA   A C   1 
ATOM   1301 O O   . ALA   A 1 179 ? 54.261 -12.710 4.008   1.00 44.97  ? 179 ALA   A O   1 
ATOM   1302 C CB  . ALA   A 1 179 ? 55.950 -11.914 6.777   1.00 43.00  ? 179 ALA   A CB  1 
ATOM   1303 N N   . MET   A 1 180 ? 54.074 -10.566 4.693   1.00 46.80  ? 180 MET   A N   1 
ATOM   1304 C CA  . MET   A 1 180 ? 53.833 -10.009 3.371   1.00 48.44  ? 180 MET   A CA  1 
ATOM   1305 C C   . MET   A 1 180 ? 54.273 -8.562  3.211   1.00 50.55  ? 180 MET   A C   1 
ATOM   1306 O O   . MET   A 1 180 ? 54.408 -7.841  4.209   1.00 48.92  ? 180 MET   A O   1 
ATOM   1307 C CB  . MET   A 1 180 ? 52.397 -10.252 2.867   1.00 52.11  ? 180 MET   A CB  1 
ATOM   1308 C CG  . MET   A 1 180 ? 51.326 -9.437  3.532   1.00 58.33  ? 180 MET   A CG  1 
ATOM   1309 S SD  . MET   A 1 180 ? 49.819 -9.620  2.520   1.00 66.19  ? 180 MET   A SD  1 
ATOM   1310 C CE  . MET   A 1 180 ? 48.571 -9.081  3.723   1.00 62.79  ? 180 MET   A CE  1 
ATOM   1311 N N   . GLY   A 1 181 ? 54.489 -8.181  1.949   1.00 45.34  ? 181 GLY   A N   1 
ATOM   1312 C CA  . GLY   A 1 181 ? 54.895 -6.863  1.499   1.00 44.40  ? 181 GLY   A CA  1 
ATOM   1313 C C   . GLY   A 1 181 ? 54.012 -6.382  0.362   1.00 50.41  ? 181 GLY   A C   1 
ATOM   1314 O O   . GLY   A 1 181 ? 53.790 -7.101  -0.616  1.00 49.46  ? 181 GLY   A O   1 
ATOM   1315 N N   . MET   A 1 182 ? 53.493 -5.158  0.497   1.00 49.10  ? 182 MET   A N   1 
ATOM   1316 C CA  . MET   A 1 182 ? 52.631 -4.499  -0.469  1.00 50.08  ? 182 MET   A CA  1 
ATOM   1317 C C   . MET   A 1 182 ? 53.243 -3.167  -0.825  1.00 50.86  ? 182 MET   A C   1 
ATOM   1318 O O   . MET   A 1 182 ? 54.030 -2.618  -0.056  1.00 50.03  ? 182 MET   A O   1 
ATOM   1319 C CB  . MET   A 1 182 ? 51.238 -4.258  0.118   1.00 54.51  ? 182 MET   A CB  1 
ATOM   1320 C CG  . MET   A 1 182 ? 50.461 -5.515  0.410   1.00 61.74  ? 182 MET   A CG  1 
ATOM   1321 S SD  . MET   A 1 182 ? 48.709 -5.110  0.628   1.00 69.83  ? 182 MET   A SD  1 
ATOM   1322 C CE  . MET   A 1 182 ? 48.207 -4.824  -1.146  1.00 67.26  ? 182 MET   A CE  1 
ATOM   1323 N N   . TYR   A 1 183 ? 52.871 -2.636  -1.984  1.00 46.24  ? 183 TYR   A N   1 
ATOM   1324 C CA  . TYR   A 1 183 ? 53.373 -1.360  -2.462  1.00 46.20  ? 183 TYR   A CA  1 
ATOM   1325 C C   . TYR   A 1 183 ? 52.326 -0.709  -3.346  1.00 50.67  ? 183 TYR   A C   1 
ATOM   1326 O O   . TYR   A 1 183 ? 51.369 -1.369  -3.751  1.00 49.04  ? 183 TYR   A O   1 
ATOM   1327 C CB  . TYR   A 1 183 ? 54.675 -1.542  -3.284  1.00 46.43  ? 183 TYR   A CB  1 
ATOM   1328 C CG  . TYR   A 1 183 ? 54.417 -2.092  -4.671  1.00 47.37  ? 183 TYR   A CG  1 
ATOM   1329 C CD1 . TYR   A 1 183 ? 54.242 -1.240  -5.759  1.00 49.54  ? 183 TYR   A CD1 1 
ATOM   1330 C CD2 . TYR   A 1 183 ? 54.326 -3.468  -4.894  1.00 47.17  ? 183 TYR   A CD2 1 
ATOM   1331 C CE1 . TYR   A 1 183 ? 53.970 -1.743  -7.033  1.00 52.01  ? 183 TYR   A CE1 1 
ATOM   1332 C CE2 . TYR   A 1 183 ? 54.083 -3.980  -6.164  1.00 47.37  ? 183 TYR   A CE2 1 
ATOM   1333 C CZ  . TYR   A 1 183 ? 53.902 -3.114  -7.232  1.00 57.90  ? 183 TYR   A CZ  1 
ATOM   1334 O OH  . TYR   A 1 183 ? 53.654 -3.613  -8.489  1.00 61.43  ? 183 TYR   A OH  1 
ATOM   1335 N N   . ASN   A 1 184 ? 52.549 0.588   -3.664  1.00 47.34  ? 184 ASN   A N   1 
ATOM   1336 C CA  . ASN   A 1 184 ? 51.748 1.388   -4.566  1.00 47.56  ? 184 ASN   A CA  1 
ATOM   1337 C C   . ASN   A 1 184 ? 52.562 2.537   -5.090  1.00 51.83  ? 184 ASN   A C   1 
ATOM   1338 O O   . ASN   A 1 184 ? 53.114 3.298   -4.297  1.00 51.29  ? 184 ASN   A O   1 
ATOM   1339 C CB  . ASN   A 1 184 ? 50.461 1.875   -3.930  1.00 50.73  ? 184 ASN   A CB  1 
ATOM   1340 C CG  . ASN   A 1 184 ? 49.294 1.540   -4.799  1.00 68.61  ? 184 ASN   A CG  1 
ATOM   1341 O OD1 . ASN   A 1 184 ? 49.138 2.072   -5.897  1.00 64.97  ? 184 ASN   A OD1 1 
ATOM   1342 N ND2 . ASN   A 1 184 ? 48.469 0.626   -4.338  1.00 61.55  ? 184 ASN   A ND2 1 
ATOM   1343 N N   . GLN   A 1 185 ? 52.672 2.645   -6.418  1.00 48.87  ? 185 GLN   A N   1 
ATOM   1344 C CA  . GLN   A 1 185 ? 53.412 3.727   -7.073  1.00 48.75  ? 185 GLN   A CA  1 
ATOM   1345 C C   . GLN   A 1 185 ? 52.514 4.969   -7.119  1.00 52.27  ? 185 GLN   A C   1 
ATOM   1346 O O   . GLN   A 1 185 ? 51.294 4.830   -7.239  1.00 51.12  ? 185 GLN   A O   1 
ATOM   1347 C CB  . GLN   A 1 185 ? 53.854 3.316   -8.503  1.00 50.61  ? 185 GLN   A CB  1 
ATOM   1348 C CG  . GLN   A 1 185 ? 55.210 2.579   -8.583  1.00 73.21  ? 185 GLN   A CG  1 
ATOM   1349 C CD  . GLN   A 1 185 ? 55.797 2.472   -9.990  1.00 94.59  ? 185 GLN   A CD  1 
ATOM   1350 O OE1 . GLN   A 1 185 ? 55.168 1.950   -10.919 1.00 91.98  ? 185 GLN   A OE1 1 
ATOM   1351 N NE2 . GLN   A 1 185 ? 57.030 2.946   -10.179 1.00 82.00  ? 185 GLN   A NE2 1 
ATOM   1352 N N   . ASP   A 1 186 ? 53.116 6.183   -7.028  1.00 50.49  ? 186 ASP   A N   1 
ATOM   1353 C CA  . ASP   A 1 186 ? 52.403 7.482   -7.080  1.00 49.77  ? 186 ASP   A CA  1 
ATOM   1354 C C   . ASP   A 1 186 ? 51.617 7.665   -8.373  1.00 50.94  ? 186 ASP   A C   1 
ATOM   1355 O O   . ASP   A 1 186 ? 50.508 8.181   -8.325  1.00 50.90  ? 186 ASP   A O   1 
ATOM   1356 C CB  . ASP   A 1 186 ? 53.361 8.668   -6.880  1.00 51.46  ? 186 ASP   A CB  1 
ATOM   1357 C CG  . ASP   A 1 186 ? 53.751 8.948   -5.438  1.00 57.25  ? 186 ASP   A CG  1 
ATOM   1358 O OD1 . ASP   A 1 186 ? 54.793 9.626   -5.225  1.00 58.98  ? 186 ASP   A OD1 1 
ATOM   1359 O OD2 . ASP   A 1 186 ? 53.015 8.498   -4.522  1.00 54.00  ? 186 ASP   A OD2 1 
ATOM   1360 N N   . LYS   A 1 187 ? 52.172 7.211   -9.511  1.00 46.27  ? 187 LYS   A N   1 
ATOM   1361 C CA  . LYS   A 1 187 ? 51.528 7.274   -10.821 1.00 45.82  ? 187 LYS   A CA  1 
ATOM   1362 C C   . LYS   A 1 187 ? 50.199 6.536   -10.781 1.00 47.05  ? 187 LYS   A C   1 
ATOM   1363 O O   . LYS   A 1 187 ? 49.221 7.065   -11.296 1.00 46.23  ? 187 LYS   A O   1 
ATOM   1364 C CB  . LYS   A 1 187 ? 52.443 6.716   -11.923 1.00 48.63  ? 187 LYS   A CB  1 
ATOM   1365 N N   . SER   A 1 188 ? 50.145 5.354   -10.122 1.00 43.35  ? 188 SER   A N   1 
ATOM   1366 C CA  . SER   A 1 188 ? 48.904 4.567   -9.983  1.00 43.05  ? 188 SER   A CA  1 
ATOM   1367 C C   . SER   A 1 188 ? 47.864 5.341   -9.180  1.00 46.73  ? 188 SER   A C   1 
ATOM   1368 O O   . SER   A 1 188 ? 46.703 5.359   -9.566  1.00 46.96  ? 188 SER   A O   1 
ATOM   1369 C CB  . SER   A 1 188 ? 49.171 3.219   -9.318  1.00 46.54  ? 188 SER   A CB  1 
ATOM   1370 O OG  . SER   A 1 188 ? 50.155 2.516   -10.055 1.00 59.71  ? 188 SER   A OG  1 
ATOM   1371 N N   . ILE   A 1 189 ? 48.275 5.990   -8.075  1.00 43.32  ? 189 ILE   A N   1 
ATOM   1372 C CA  . ILE   A 1 189 ? 47.362 6.773   -7.237  1.00 43.23  ? 189 ILE   A CA  1 
ATOM   1373 C C   . ILE   A 1 189 ? 46.866 7.979   -8.017  1.00 46.34  ? 189 ILE   A C   1 
ATOM   1374 O O   . ILE   A 1 189 ? 45.694 8.332   -7.902  1.00 46.72  ? 189 ILE   A O   1 
ATOM   1375 C CB  . ILE   A 1 189 ? 47.960 7.171   -5.838  1.00 46.34  ? 189 ILE   A CB  1 
ATOM   1376 C CG1 . ILE   A 1 189 ? 48.557 5.934   -5.094  1.00 45.51  ? 189 ILE   A CG1 1 
ATOM   1377 C CG2 . ILE   A 1 189 ? 46.878 7.876   -4.967  1.00 47.19  ? 189 ILE   A CG2 1 
ATOM   1378 C CD1 . ILE   A 1 189 ? 49.481 6.252   -3.862  1.00 40.56  ? 189 ILE   A CD1 1 
ATOM   1379 N N   . GLU   A 1 190 ? 47.755 8.603   -8.810  1.00 42.74  ? 190 GLU   A N   1 
ATOM   1380 C CA  . GLU   A 1 190 ? 47.439 9.774   -9.638  1.00 43.18  ? 190 GLU   A CA  1 
ATOM   1381 C C   . GLU   A 1 190 ? 46.369 9.414   -10.678 1.00 47.69  ? 190 GLU   A C   1 
ATOM   1382 O O   . GLU   A 1 190 ? 45.367 10.132  -10.799 1.00 48.15  ? 190 GLU   A O   1 
ATOM   1383 C CB  . GLU   A 1 190 ? 48.708 10.355  -10.287 1.00 44.44  ? 190 GLU   A CB  1 
ATOM   1384 C CG  . GLU   A 1 190 ? 49.617 11.065  -9.296  1.00 52.39  ? 190 GLU   A CG  1 
ATOM   1385 C CD  . GLU   A 1 190 ? 51.046 11.361  -9.730  1.00 78.82  ? 190 GLU   A CD  1 
ATOM   1386 O OE1 . GLU   A 1 190 ? 51.414 11.039  -10.885 1.00 64.82  ? 190 GLU   A OE1 1 
ATOM   1387 O OE2 . GLU   A 1 190 ? 51.801 11.922  -8.898  1.00 78.57  ? 190 GLU   A OE2 1 
ATOM   1388 N N   . ASP   A 1 191 ? 46.569 8.273   -11.382 1.00 42.71  ? 191 ASP   A N   1 
ATOM   1389 C CA  . ASP   A 1 191 ? 45.655 7.699   -12.371 1.00 41.74  ? 191 ASP   A CA  1 
ATOM   1390 C C   . ASP   A 1 191 ? 44.308 7.354   -11.741 1.00 47.25  ? 191 ASP   A C   1 
ATOM   1391 O O   . ASP   A 1 191 ? 43.266 7.606   -12.348 1.00 49.15  ? 191 ASP   A O   1 
ATOM   1392 C CB  . ASP   A 1 191 ? 46.288 6.452   -12.999 1.00 42.12  ? 191 ASP   A CB  1 
ATOM   1393 C CG  . ASP   A 1 191 ? 47.472 6.792   -13.874 1.00 49.10  ? 191 ASP   A CG  1 
ATOM   1394 O OD1 . ASP   A 1 191 ? 48.257 5.876   -14.183 1.00 51.40  ? 191 ASP   A OD1 1 
ATOM   1395 O OD2 . ASP   A 1 191 ? 47.622 7.991   -14.245 1.00 51.98  ? 191 ASP   A OD2 1 
ATOM   1396 N N   . PHE   A 1 192 ? 44.333 6.804   -10.514 1.00 41.67  ? 192 PHE   A N   1 
ATOM   1397 C CA  . PHE   A 1 192 ? 43.140 6.445   -9.755  1.00 40.72  ? 192 PHE   A CA  1 
ATOM   1398 C C   . PHE   A 1 192 ? 42.334 7.711   -9.448  1.00 46.20  ? 192 PHE   A C   1 
ATOM   1399 O O   . PHE   A 1 192 ? 41.117 7.713   -9.647  1.00 45.73  ? 192 PHE   A O   1 
ATOM   1400 C CB  . PHE   A 1 192 ? 43.513 5.633   -8.485  1.00 41.46  ? 192 PHE   A CB  1 
ATOM   1401 C CG  . PHE   A 1 192 ? 42.371 5.136   -7.623  1.00 42.38  ? 192 PHE   A CG  1 
ATOM   1402 C CD1 . PHE   A 1 192 ? 42.503 5.062   -6.243  1.00 45.70  ? 192 PHE   A CD1 1 
ATOM   1403 C CD2 . PHE   A 1 192 ? 41.171 4.723   -8.192  1.00 43.45  ? 192 PHE   A CD2 1 
ATOM   1404 C CE1 . PHE   A 1 192 ? 41.445 4.593   -5.446  1.00 46.25  ? 192 PHE   A CE1 1 
ATOM   1405 C CE2 . PHE   A 1 192 ? 40.112 4.271   -7.391  1.00 45.98  ? 192 PHE   A CE2 1 
ATOM   1406 C CZ  . PHE   A 1 192 ? 40.253 4.210   -6.029  1.00 44.01  ? 192 PHE   A CZ  1 
ATOM   1407 N N   . ALA   A 1 193 ? 43.015 8.790   -9.008  1.00 44.26  ? 193 ALA   A N   1 
ATOM   1408 C CA  . ALA   A 1 193 ? 42.376 10.081  -8.723  1.00 44.84  ? 193 ALA   A CA  1 
ATOM   1409 C C   . ALA   A 1 193 ? 41.728 10.641  -10.002 1.00 50.48  ? 193 ALA   A C   1 
ATOM   1410 O O   . ALA   A 1 193 ? 40.537 10.941  -9.988  1.00 51.10  ? 193 ALA   A O   1 
ATOM   1411 C CB  . ALA   A 1 193 ? 43.394 11.072  -8.158  1.00 45.21  ? 193 ALA   A CB  1 
ATOM   1412 N N   . HIS   A 1 194 ? 42.504 10.727  -11.106 1.00 47.79  ? 194 HIS   A N   1 
ATOM   1413 C CA  . HIS   A 1 194 ? 42.087 11.221  -12.422 1.00 47.85  ? 194 HIS   A CA  1 
ATOM   1414 C C   . HIS   A 1 194 ? 40.876 10.492  -12.993 1.00 50.17  ? 194 HIS   A C   1 
ATOM   1415 O O   . HIS   A 1 194 ? 39.888 11.144  -13.337 1.00 49.85  ? 194 HIS   A O   1 
ATOM   1416 C CB  . HIS   A 1 194 ? 43.263 11.231  -13.413 1.00 49.14  ? 194 HIS   A CB  1 
ATOM   1417 C CG  . HIS   A 1 194 ? 44.151 12.428  -13.267 1.00 53.22  ? 194 HIS   A CG  1 
ATOM   1418 N ND1 . HIS   A 1 194 ? 43.646 13.723  -13.347 1.00 55.30  ? 194 HIS   A ND1 1 
ATOM   1419 C CD2 . HIS   A 1 194 ? 45.490 12.494  -13.070 1.00 55.41  ? 194 HIS   A CD2 1 
ATOM   1420 C CE1 . HIS   A 1 194 ? 44.690 14.524  -13.195 1.00 54.99  ? 194 HIS   A CE1 1 
ATOM   1421 N NE2 . HIS   A 1 194 ? 45.821 13.832  -13.028 1.00 55.24  ? 194 HIS   A NE2 1 
ATOM   1422 N N   . SER   A 1 195 ? 40.930 9.153   -13.064 1.00 45.42  ? 195 SER   A N   1 
ATOM   1423 C CA  . SER   A 1 195 ? 39.809 8.362   -13.565 1.00 44.47  ? 195 SER   A CA  1 
ATOM   1424 C C   . SER   A 1 195 ? 38.564 8.631   -12.726 1.00 50.43  ? 195 SER   A C   1 
ATOM   1425 O O   . SER   A 1 195 ? 37.491 8.796   -13.306 1.00 52.45  ? 195 SER   A O   1 
ATOM   1426 C CB  . SER   A 1 195 ? 40.143 6.877   -13.580 1.00 45.53  ? 195 SER   A CB  1 
ATOM   1427 O OG  . SER   A 1 195 ? 41.382 6.625   -14.227 1.00 50.34  ? 195 SER   A OG  1 
ATOM   1428 N N   . SER   A 1 196 ? 38.708 8.728   -11.378 1.00 45.87  ? 196 SER   A N   1 
ATOM   1429 C CA  . SER   A 1 196 ? 37.607 8.992   -10.441 1.00 45.52  ? 196 SER   A CA  1 
ATOM   1430 C C   . SER   A 1 196 ? 36.986 10.379  -10.661 1.00 52.26  ? 196 SER   A C   1 
ATOM   1431 O O   . SER   A 1 196 ? 35.751 10.481  -10.694 1.00 51.70  ? 196 SER   A O   1 
ATOM   1432 C CB  . SER   A 1 196 ? 38.062 8.847   -8.989  1.00 46.69  ? 196 SER   A CB  1 
ATOM   1433 O OG  . SER   A 1 196 ? 38.607 7.569   -8.710  1.00 51.19  ? 196 SER   A OG  1 
ATOM   1434 N N   . PHE   A 1 197 ? 37.835 11.453  -10.801 1.00 49.60  ? 197 PHE   A N   1 
ATOM   1435 C CA  . PHE   A 1 197 ? 37.336 12.817  -11.029 1.00 48.69  ? 197 PHE   A CA  1 
ATOM   1436 C C   . PHE   A 1 197 ? 36.621 12.864  -12.377 1.00 54.53  ? 197 PHE   A C   1 
ATOM   1437 O O   . PHE   A 1 197 ? 35.540 13.441  -12.472 1.00 54.56  ? 197 PHE   A O   1 
ATOM   1438 C CB  . PHE   A 1 197 ? 38.459 13.875  -10.937 1.00 49.41  ? 197 PHE   A CB  1 
ATOM   1439 C CG  . PHE   A 1 197 ? 39.053 14.029  -9.553  1.00 49.51  ? 197 PHE   A CG  1 
ATOM   1440 C CD1 . PHE   A 1 197 ? 40.412 13.827  -9.333  1.00 50.78  ? 197 PHE   A CD1 1 
ATOM   1441 C CD2 . PHE   A 1 197 ? 38.254 14.371  -8.465  1.00 49.46  ? 197 PHE   A CD2 1 
ATOM   1442 C CE1 . PHE   A 1 197 ? 40.949 13.929  -8.045  1.00 50.43  ? 197 PHE   A CE1 1 
ATOM   1443 C CE2 . PHE   A 1 197 ? 38.798 14.471  -7.178  1.00 50.74  ? 197 PHE   A CE2 1 
ATOM   1444 C CZ  . PHE   A 1 197 ? 40.140 14.260  -6.982  1.00 48.00  ? 197 PHE   A CZ  1 
ATOM   1445 N N   . GLN   A 1 198 ? 37.209 12.198  -13.395 1.00 51.80  ? 198 GLN   A N   1 
ATOM   1446 C CA  . GLN   A 1 198 ? 36.685 12.080  -14.751 1.00 51.85  ? 198 GLN   A CA  1 
ATOM   1447 C C   . GLN   A 1 198 ? 35.318 11.401  -14.757 1.00 57.55  ? 198 GLN   A C   1 
ATOM   1448 O O   . GLN   A 1 198 ? 34.409 11.870  -15.441 1.00 58.60  ? 198 GLN   A O   1 
ATOM   1449 C CB  . GLN   A 1 198 ? 37.668 11.300  -15.631 1.00 53.02  ? 198 GLN   A CB  1 
ATOM   1450 C CG  . GLN   A 1 198 ? 38.079 12.059  -16.870 1.00 65.10  ? 198 GLN   A CG  1 
ATOM   1451 C CD  . GLN   A 1 198 ? 39.218 13.008  -16.622 1.00 80.43  ? 198 GLN   A CD  1 
ATOM   1452 O OE1 . GLN   A 1 198 ? 40.277 12.631  -16.097 1.00 79.78  ? 198 GLN   A OE1 1 
ATOM   1453 N NE2 . GLN   A 1 198 ? 39.028 14.262  -17.010 1.00 61.80  ? 198 GLN   A NE2 1 
ATOM   1454 N N   . MET   A 1 199 ? 35.172 10.313  -13.974 1.00 54.15  ? 199 MET   A N   1 
ATOM   1455 C CA  . MET   A 1 199 ? 33.927 9.549   -13.831 1.00 53.28  ? 199 MET   A CA  1 
ATOM   1456 C C   . MET   A 1 199 ? 32.840 10.372  -13.148 1.00 58.17  ? 199 MET   A C   1 
ATOM   1457 O O   . MET   A 1 199 ? 31.677 10.276  -13.545 1.00 59.18  ? 199 MET   A O   1 
ATOM   1458 C CB  . MET   A 1 199 ? 34.187 8.242   -13.065 1.00 55.02  ? 199 MET   A CB  1 
ATOM   1459 C CG  . MET   A 1 199 ? 32.996 7.324   -12.976 1.00 58.10  ? 199 MET   A CG  1 
ATOM   1460 S SD  . MET   A 1 199 ? 32.348 6.847   -14.585 1.00 61.31  ? 199 MET   A SD  1 
ATOM   1461 C CE  . MET   A 1 199 ? 31.213 5.654   -14.125 1.00 58.03  ? 199 MET   A CE  1 
ATOM   1462 N N   . ALA   A 1 200 ? 33.209 11.168  -12.126 1.00 54.52  ? 200 ALA   A N   1 
ATOM   1463 C CA  . ALA   A 1 200 ? 32.256 12.000  -11.387 1.00 54.79  ? 200 ALA   A CA  1 
ATOM   1464 C C   . ALA   A 1 200 ? 31.752 13.165  -12.230 1.00 62.66  ? 200 ALA   A C   1 
ATOM   1465 O O   . ALA   A 1 200 ? 30.581 13.538  -12.104 1.00 62.91  ? 200 ALA   A O   1 
ATOM   1466 C CB  . ALA   A 1 200 ? 32.871 12.508  -10.095 1.00 54.89  ? 200 ALA   A CB  1 
ATOM   1467 N N   . LEU   A 1 201 ? 32.632 13.738  -13.089 1.00 60.03  ? 201 LEU   A N   1 
ATOM   1468 C CA  . LEU   A 1 201 ? 32.279 14.854  -13.961 1.00 60.16  ? 201 LEU   A CA  1 
ATOM   1469 C C   . LEU   A 1 201 ? 31.278 14.371  -15.016 1.00 66.29  ? 201 LEU   A C   1 
ATOM   1470 O O   . LEU   A 1 201 ? 30.198 14.959  -15.160 1.00 66.02  ? 201 LEU   A O   1 
ATOM   1471 C CB  . LEU   A 1 201 ? 33.535 15.478  -14.607 1.00 59.92  ? 201 LEU   A CB  1 
ATOM   1472 C CG  . LEU   A 1 201 ? 34.380 16.410  -13.708 1.00 63.73  ? 201 LEU   A CG  1 
ATOM   1473 C CD1 . LEU   A 1 201 ? 35.651 16.815  -14.394 1.00 62.98  ? 201 LEU   A CD1 1 
ATOM   1474 C CD2 . LEU   A 1 201 ? 33.601 17.652  -13.278 1.00 65.12  ? 201 LEU   A CD2 1 
ATOM   1475 N N   . SER   A 1 202 ? 31.632 13.258  -15.699 1.00 63.34  ? 202 SER   A N   1 
ATOM   1476 C CA  . SER   A 1 202 ? 30.864 12.562  -16.728 1.00 62.80  ? 202 SER   A CA  1 
ATOM   1477 C C   . SER   A 1 202 ? 29.411 12.277  -16.291 1.00 67.82  ? 202 SER   A C   1 
ATOM   1478 O O   . SER   A 1 202 ? 28.505 12.515  -17.084 1.00 69.38  ? 202 SER   A O   1 
ATOM   1479 C CB  . SER   A 1 202 ? 31.573 11.264  -17.108 1.00 64.78  ? 202 SER   A CB  1 
ATOM   1480 O OG  . SER   A 1 202 ? 31.108 10.740  -18.337 1.00 71.60  ? 202 SER   A OG  1 
ATOM   1481 N N   . LYS   A 1 203 ? 29.194 11.799  -15.038 1.00 63.25  ? 203 LYS   A N   1 
ATOM   1482 C CA  . LYS   A 1 203 ? 27.875 11.480  -14.460 1.00 62.51  ? 203 LYS   A CA  1 
ATOM   1483 C C   . LYS   A 1 203 ? 27.229 12.646  -13.713 1.00 68.40  ? 203 LYS   A C   1 
ATOM   1484 O O   . LYS   A 1 203 ? 26.042 12.568  -13.376 1.00 68.51  ? 203 LYS   A O   1 
ATOM   1485 C CB  . LYS   A 1 203 ? 27.948 10.253  -13.525 1.00 63.47  ? 203 LYS   A CB  1 
ATOM   1486 C CG  . LYS   A 1 203 ? 28.152 8.923   -14.246 1.00 73.84  ? 203 LYS   A CG  1 
ATOM   1487 C CD  . LYS   A 1 203 ? 26.849 8.241   -14.675 1.00 78.12  ? 203 LYS   A CD  1 
ATOM   1488 C CE  . LYS   A 1 203 ? 27.125 6.979   -15.464 1.00 85.17  ? 203 LYS   A CE  1 
ATOM   1489 N NZ  . LYS   A 1 203 ? 25.875 6.376   -16.003 1.00 91.37  ? 203 LYS   A NZ  1 
ATOM   1490 N N   . GLY   A 1 204 ? 28.003 13.705  -13.460 1.00 65.68  ? 204 GLY   A N   1 
ATOM   1491 C CA  . GLY   A 1 204 ? 27.541 14.889  -12.740 1.00 65.66  ? 204 GLY   A CA  1 
ATOM   1492 C C   . GLY   A 1 204 ? 27.125 14.558  -11.322 1.00 70.10  ? 204 GLY   A C   1 
ATOM   1493 O O   . GLY   A 1 204 ? 26.124 15.077  -10.820 1.00 69.59  ? 204 GLY   A O   1 
ATOM   1494 N N   . TRP   A 1 205 ? 27.884 13.660  -10.679 1.00 67.56  ? 205 TRP   A N   1 
ATOM   1495 C CA  . TRP   A 1 205 ? 27.618 13.203  -9.319  1.00 67.69  ? 205 TRP   A CA  1 
ATOM   1496 C C   . TRP   A 1 205 ? 28.788 13.512  -8.380  1.00 67.71  ? 205 TRP   A C   1 
ATOM   1497 O O   . TRP   A 1 205 ? 29.926 13.612  -8.860  1.00 67.27  ? 205 TRP   A O   1 
ATOM   1498 C CB  . TRP   A 1 205 ? 27.312 11.689  -9.329  1.00 67.55  ? 205 TRP   A CB  1 
ATOM   1499 C CG  . TRP   A 1 205 ? 25.912 11.337  -9.753  1.00 69.61  ? 205 TRP   A CG  1 
ATOM   1500 C CD1 . TRP   A 1 205 ? 24.845 12.183  -9.851  1.00 72.85  ? 205 TRP   A CD1 1 
ATOM   1501 C CD2 . TRP   A 1 205 ? 25.421 10.032  -10.092 1.00 69.80  ? 205 TRP   A CD2 1 
ATOM   1502 N NE1 . TRP   A 1 205 ? 23.723 11.490  -10.243 1.00 72.78  ? 205 TRP   A NE1 1 
ATOM   1503 C CE2 . TRP   A 1 205 ? 24.047 10.167  -10.400 1.00 74.20  ? 205 TRP   A CE2 1 
ATOM   1504 C CE3 . TRP   A 1 205 ? 26.008 8.757   -10.168 1.00 71.22  ? 205 TRP   A CE3 1 
ATOM   1505 C CZ2 . TRP   A 1 205 ? 23.252 9.078   -10.778 1.00 73.43  ? 205 TRP   A CZ2 1 
ATOM   1506 C CZ3 . TRP   A 1 205 ? 25.217 7.679   -10.545 1.00 72.82  ? 205 TRP   A CZ3 1 
ATOM   1507 C CH2 . TRP   A 1 205 ? 23.860 7.846   -10.854 1.00 73.41  ? 205 TRP   A CH2 1 
ATOM   1508 N N   . PRO   A 1 206 ? 28.553 13.665  -7.049  1.00 61.07  ? 206 PRO   A N   1 
ATOM   1509 C CA  . PRO   A 1 206 ? 29.693 13.909  -6.142  1.00 59.80  ? 206 PRO   A CA  1 
ATOM   1510 C C   . PRO   A 1 206 ? 30.589 12.663  -5.982  1.00 60.24  ? 206 PRO   A C   1 
ATOM   1511 O O   . PRO   A 1 206 ? 30.122 11.526  -6.171  1.00 58.93  ? 206 PRO   A O   1 
ATOM   1512 C CB  . PRO   A 1 206 ? 29.031 14.322  -4.831  1.00 61.44  ? 206 PRO   A CB  1 
ATOM   1513 C CG  . PRO   A 1 206 ? 27.677 13.722  -4.871  1.00 66.24  ? 206 PRO   A CG  1 
ATOM   1514 C CD  . PRO   A 1 206 ? 27.276 13.568  -6.306  1.00 62.02  ? 206 PRO   A CD  1 
ATOM   1515 N N   . LEU   A 1 207 ? 31.881 12.891  -5.659  1.00 53.57  ? 207 LEU   A N   1 
ATOM   1516 C CA  . LEU   A 1 207 ? 32.882 11.842  -5.490  1.00 51.71  ? 207 LEU   A CA  1 
ATOM   1517 C C   . LEU   A 1 207 ? 33.368 11.689  -4.049  1.00 55.66  ? 207 LEU   A C   1 
ATOM   1518 O O   . LEU   A 1 207 ? 33.687 12.680  -3.388  1.00 55.30  ? 207 LEU   A O   1 
ATOM   1519 C CB  . LEU   A 1 207 ? 34.075 12.078  -6.450  1.00 50.80  ? 207 LEU   A CB  1 
ATOM   1520 C CG  . LEU   A 1 207 ? 35.313 11.176  -6.286  1.00 53.73  ? 207 LEU   A CG  1 
ATOM   1521 C CD1 . LEU   A 1 207 ? 35.021 9.730   -6.661  1.00 53.72  ? 207 LEU   A CD1 1 
ATOM   1522 C CD2 . LEU   A 1 207 ? 36.457 11.692  -7.072  1.00 53.18  ? 207 LEU   A CD2 1 
ATOM   1523 N N   . TYR   A 1 208 ? 33.457 10.438  -3.581  1.00 52.00  ? 208 TYR   A N   1 
ATOM   1524 C CA  . TYR   A 1 208 ? 33.954 10.139  -2.242  1.00 52.02  ? 208 TYR   A CA  1 
ATOM   1525 C C   . TYR   A 1 208 ? 35.130 9.174   -2.294  1.00 54.26  ? 208 TYR   A C   1 
ATOM   1526 O O   . TYR   A 1 208 ? 35.108 8.217   -3.061  1.00 53.16  ? 208 TYR   A O   1 
ATOM   1527 C CB  . TYR   A 1 208 ? 32.845 9.585   -1.338  1.00 54.28  ? 208 TYR   A CB  1 
ATOM   1528 C CG  . TYR   A 1 208 ? 31.699 10.549  -1.134  1.00 58.78  ? 208 TYR   A CG  1 
ATOM   1529 C CD1 . TYR   A 1 208 ? 30.503 10.396  -1.827  1.00 61.46  ? 208 TYR   A CD1 1 
ATOM   1530 C CD2 . TYR   A 1 208 ? 31.814 11.626  -0.258  1.00 60.47  ? 208 TYR   A CD2 1 
ATOM   1531 C CE1 . TYR   A 1 208 ? 29.452 11.299  -1.666  1.00 63.25  ? 208 TYR   A CE1 1 
ATOM   1532 C CE2 . TYR   A 1 208 ? 30.769 12.530  -0.082  1.00 61.95  ? 208 TYR   A CE2 1 
ATOM   1533 C CZ  . TYR   A 1 208 ? 29.588 12.363  -0.790  1.00 72.03  ? 208 TYR   A CZ  1 
ATOM   1534 O OH  . TYR   A 1 208 ? 28.551 13.251  -0.622  1.00 75.82  ? 208 TYR   A OH  1 
ATOM   1535 N N   . LEU   A 1 209 ? 36.164 9.432   -1.485  1.00 49.77  ? 209 LEU   A N   1 
ATOM   1536 C CA  . LEU   A 1 209 ? 37.316 8.540   -1.385  1.00 47.90  ? 209 LEU   A CA  1 
ATOM   1537 C C   . LEU   A 1 209 ? 37.274 7.941   0.004   1.00 52.03  ? 209 LEU   A C   1 
ATOM   1538 O O   . LEU   A 1 209 ? 37.228 8.690   0.981   1.00 51.60  ? 209 LEU   A O   1 
ATOM   1539 C CB  . LEU   A 1 209 ? 38.668 9.255   -1.619  1.00 46.83  ? 209 LEU   A CB  1 
ATOM   1540 C CG  . LEU   A 1 209 ? 39.959 8.437   -1.302  1.00 49.26  ? 209 LEU   A CG  1 
ATOM   1541 C CD1 . LEU   A 1 209 ? 40.108 7.194   -2.209  1.00 48.09  ? 209 LEU   A CD1 1 
ATOM   1542 C CD2 . LEU   A 1 209 ? 41.194 9.291   -1.429  1.00 47.81  ? 209 LEU   A CD2 1 
ATOM   1543 N N   . SER   A 1 210 ? 37.266 6.604   0.100   1.00 49.10  ? 210 SER   A N   1 
ATOM   1544 C CA  . SER   A 1 210 ? 37.285 5.936   1.399   1.00 49.42  ? 210 SER   A CA  1 
ATOM   1545 C C   . SER   A 1 210 ? 38.674 5.371   1.620   1.00 55.75  ? 210 SER   A C   1 
ATOM   1546 O O   . SER   A 1 210 ? 39.246 4.747   0.723   1.00 55.90  ? 210 SER   A O   1 
ATOM   1547 C CB  . SER   A 1 210 ? 36.209 4.861   1.530   1.00 52.24  ? 210 SER   A CB  1 
ATOM   1548 O OG  . SER   A 1 210 ? 36.475 3.708   0.749   1.00 62.52  ? 210 SER   A OG  1 
ATOM   1549 N N   . THR   A 1 211 ? 39.226 5.610   2.807   1.00 54.01  ? 211 THR   A N   1 
ATOM   1550 C CA  . THR   A 1 211 ? 40.561 5.149   3.167   1.00 54.76  ? 211 THR   A CA  1 
ATOM   1551 C C   . THR   A 1 211 ? 40.597 4.777   4.670   1.00 62.22  ? 211 THR   A C   1 
ATOM   1552 O O   . THR   A 1 211 ? 39.611 5.000   5.386   1.00 62.33  ? 211 THR   A O   1 
ATOM   1553 C CB  . THR   A 1 211 ? 41.573 6.208   2.640   1.00 58.87  ? 211 THR   A CB  1 
ATOM   1554 O OG1 . THR   A 1 211 ? 42.377 5.665   1.607   1.00 62.95  ? 211 THR   A OG1 1 
ATOM   1555 C CG2 . THR   A 1 211 ? 42.401 6.862   3.699   1.00 52.71  ? 211 THR   A CG2 1 
ATOM   1556 N N   . LYS   A 1 212 ? 41.714 4.179   5.123   1.00 60.11  ? 212 LYS   A N   1 
ATOM   1557 C CA  . LYS   A 1 212 ? 41.973 3.823   6.518   1.00 60.28  ? 212 LYS   A CA  1 
ATOM   1558 C C   . LYS   A 1 212 ? 43.291 4.547   6.935   1.00 63.81  ? 212 LYS   A C   1 
ATOM   1559 O O   . LYS   A 1 212 ? 44.231 3.907   7.419   1.00 62.87  ? 212 LYS   A O   1 
ATOM   1560 C CB  . LYS   A 1 212 ? 42.050 2.292   6.704   1.00 62.77  ? 212 LYS   A CB  1 
ATOM   1561 N N   . ASN   A 1 213 ? 43.341 5.893   6.731   1.00 60.55  ? 213 ASN   A N   1 
ATOM   1562 C CA  . ASN   A 1 213 ? 44.509 6.746   7.033   1.00 61.40  ? 213 ASN   A CA  1 
ATOM   1563 C C   . ASN   A 1 213 ? 44.818 7.005   8.523   1.00 66.57  ? 213 ASN   A C   1 
ATOM   1564 O O   . ASN   A 1 213 ? 45.803 7.676   8.841   1.00 66.32  ? 213 ASN   A O   1 
ATOM   1565 C CB  . ASN   A 1 213 ? 44.495 8.053   6.211   1.00 62.19  ? 213 ASN   A CB  1 
ATOM   1566 C CG  . ASN   A 1 213 ? 43.607 9.159   6.732   1.00 80.94  ? 213 ASN   A CG  1 
ATOM   1567 O OD1 . ASN   A 1 213 ? 42.476 8.946   7.188   1.00 80.12  ? 213 ASN   A OD1 1 
ATOM   1568 N ND2 . ASN   A 1 213 ? 44.109 10.379  6.665   1.00 68.39  ? 213 ASN   A ND2 1 
ATOM   1569 N N   . THR   A 1 214 ? 43.969 6.481   9.414   1.00 63.59  ? 214 THR   A N   1 
ATOM   1570 C CA  . THR   A 1 214 ? 44.082 6.576   10.868  1.00 63.46  ? 214 THR   A CA  1 
ATOM   1571 C C   . THR   A 1 214 ? 45.025 5.476   11.351  1.00 67.63  ? 214 THR   A C   1 
ATOM   1572 O O   . THR   A 1 214 ? 45.760 5.670   12.328  1.00 68.77  ? 214 THR   A O   1 
ATOM   1573 C CB  . THR   A 1 214 ? 42.688 6.400   11.516  1.00 71.32  ? 214 THR   A CB  1 
ATOM   1574 O OG1 . THR   A 1 214 ? 41.990 5.325   10.866  1.00 70.00  ? 214 THR   A OG1 1 
ATOM   1575 C CG2 . THR   A 1 214 ? 41.852 7.681   11.468  1.00 68.85  ? 214 THR   A CG2 1 
ATOM   1576 N N   . ILE   A 1 215 ? 44.986 4.316   10.660  1.00 61.91  ? 215 ILE   A N   1 
ATOM   1577 C CA  . ILE   A 1 215 ? 45.787 3.133   10.945  1.00 61.05  ? 215 ILE   A CA  1 
ATOM   1578 C C   . ILE   A 1 215 ? 47.033 3.125   10.044  1.00 63.19  ? 215 ILE   A C   1 
ATOM   1579 O O   . ILE   A 1 215 ? 48.144 2.943   10.533  1.00 62.99  ? 215 ILE   A O   1 
ATOM   1580 C CB  . ILE   A 1 215 ? 44.902 1.849   10.795  1.00 64.51  ? 215 ILE   A CB  1 
ATOM   1581 C CG1 . ILE   A 1 215 ? 43.615 1.894   11.692  1.00 65.18  ? 215 ILE   A CG1 1 
ATOM   1582 C CG2 . ILE   A 1 215 ? 45.698 0.550   10.996  1.00 65.22  ? 215 ILE   A CG2 1 
ATOM   1583 C CD1 . ILE   A 1 215 ? 43.806 2.047   13.291  1.00 72.29  ? 215 ILE   A CD1 1 
ATOM   1584 N N   . LEU   A 1 216 ? 46.826 3.326   8.733   1.00 57.65  ? 216 LEU   A N   1 
ATOM   1585 C CA  . LEU   A 1 216 ? 47.827 3.353   7.667   1.00 55.14  ? 216 LEU   A CA  1 
ATOM   1586 C C   . LEU   A 1 216 ? 48.106 4.821   7.324   1.00 57.90  ? 216 LEU   A C   1 
ATOM   1587 O O   . LEU   A 1 216 ? 47.831 5.298   6.217   1.00 57.50  ? 216 LEU   A O   1 
ATOM   1588 C CB  . LEU   A 1 216 ? 47.244 2.595   6.460   1.00 54.53  ? 216 LEU   A CB  1 
ATOM   1589 C CG  . LEU   A 1 216 ? 47.719 1.171   6.164   1.00 57.73  ? 216 LEU   A CG  1 
ATOM   1590 C CD1 . LEU   A 1 216 ? 47.972 0.357   7.413   1.00 56.95  ? 216 LEU   A CD1 1 
ATOM   1591 C CD2 . LEU   A 1 216 ? 46.740 0.467   5.246   1.00 57.78  ? 216 LEU   A CD2 1 
ATOM   1592 N N   . LYS   A 1 217 ? 48.640 5.536   8.311   1.00 53.99  ? 217 LYS   A N   1 
ATOM   1593 C CA  . LYS   A 1 217 ? 48.969 6.958   8.239   1.00 53.15  ? 217 LYS   A CA  1 
ATOM   1594 C C   . LYS   A 1 217 ? 49.805 7.348   7.015   1.00 56.59  ? 217 LYS   A C   1 
ATOM   1595 O O   . LYS   A 1 217 ? 49.491 8.345   6.365   1.00 56.94  ? 217 LYS   A O   1 
ATOM   1596 C CB  . LYS   A 1 217 ? 49.633 7.432   9.550   1.00 55.19  ? 217 LYS   A CB  1 
ATOM   1597 C CG  . LYS   A 1 217 ? 48.790 7.215   10.810  1.00 65.82  ? 217 LYS   A CG  1 
ATOM   1598 C CD  . LYS   A 1 217 ? 49.565 7.620   12.066  1.00 76.91  ? 217 LYS   A CD  1 
ATOM   1599 C CE  . LYS   A 1 217 ? 48.730 7.600   13.332  1.00 86.19  ? 217 LYS   A CE  1 
ATOM   1600 N NZ  . LYS   A 1 217 ? 48.524 6.224   13.863  1.00 94.89  ? 217 LYS   A NZ  1 
ATOM   1601 N N   . LYS   A 1 218 ? 50.863 6.580   6.702   1.00 51.41  ? 218 LYS   A N   1 
ATOM   1602 C CA  . LYS   A 1 218 ? 51.736 6.881   5.568   1.00 50.06  ? 218 LYS   A CA  1 
ATOM   1603 C C   . LYS   A 1 218 ? 51.177 6.331   4.247   1.00 53.12  ? 218 LYS   A C   1 
ATOM   1604 O O   . LYS   A 1 218 ? 51.174 7.051   3.246   1.00 53.44  ? 218 LYS   A O   1 
ATOM   1605 C CB  . LYS   A 1 218 ? 53.183 6.406   5.804   1.00 51.85  ? 218 LYS   A CB  1 
ATOM   1606 C CG  . LYS   A 1 218 ? 53.653 6.346   7.258   1.00 62.48  ? 218 LYS   A CG  1 
ATOM   1607 C CD  . LYS   A 1 218 ? 54.200 7.670   7.787   1.00 74.91  ? 218 LYS   A CD  1 
ATOM   1608 C CE  . LYS   A 1 218 ? 54.651 7.578   9.235   1.00 88.96  ? 218 LYS   A CE  1 
ATOM   1609 N NZ  . LYS   A 1 218 ? 53.512 7.452   10.199  1.00 95.11  ? 218 LYS   A NZ  1 
ATOM   1610 N N   . TYR   A 1 219 ? 50.699 5.070   4.256   1.00 47.73  ? 219 TYR   A N   1 
ATOM   1611 C CA  . TYR   A 1 219 ? 50.144 4.362   3.105   1.00 46.52  ? 219 TYR   A CA  1 
ATOM   1612 C C   . TYR   A 1 219 ? 48.848 4.975   2.560   1.00 50.03  ? 219 TYR   A C   1 
ATOM   1613 O O   . TYR   A 1 219 ? 48.810 5.389   1.400   1.00 49.84  ? 219 TYR   A O   1 
ATOM   1614 C CB  . TYR   A 1 219 ? 49.973 2.870   3.424   1.00 47.56  ? 219 TYR   A CB  1 
ATOM   1615 C CG  . TYR   A 1 219 ? 50.067 1.958   2.220   1.00 49.43  ? 219 TYR   A CG  1 
ATOM   1616 C CD1 . TYR   A 1 219 ? 51.201 1.186   1.994   1.00 50.34  ? 219 TYR   A CD1 1 
ATOM   1617 C CD2 . TYR   A 1 219 ? 49.012 1.851   1.314   1.00 50.72  ? 219 TYR   A CD2 1 
ATOM   1618 C CE1 . TYR   A 1 219 ? 51.289 0.337   0.894   1.00 49.86  ? 219 TYR   A CE1 1 
ATOM   1619 C CE2 . TYR   A 1 219 ? 49.090 1.004   0.212   1.00 51.58  ? 219 TYR   A CE2 1 
ATOM   1620 C CZ  . TYR   A 1 219 ? 50.229 0.245   0.011   1.00 55.88  ? 219 TYR   A CZ  1 
ATOM   1621 O OH  . TYR   A 1 219 ? 50.305 -0.591  -1.068  1.00 57.57  ? 219 TYR   A OH  1 
ATOM   1622 N N   . ASP   A 1 220 ? 47.788 5.016   3.379   1.00 46.64  ? 220 ASP   A N   1 
ATOM   1623 C CA  . ASP   A 1 220 ? 46.507 5.577   2.966   1.00 46.39  ? 220 ASP   A CA  1 
ATOM   1624 C C   . ASP   A 1 220 ? 46.495 7.100   2.962   1.00 53.35  ? 220 ASP   A C   1 
ATOM   1625 O O   . ASP   A 1 220 ? 45.619 7.698   2.340   1.00 54.52  ? 220 ASP   A O   1 
ATOM   1626 C CB  . ASP   A 1 220 ? 45.371 4.984   3.785   1.00 47.64  ? 220 ASP   A CB  1 
ATOM   1627 C CG  . ASP   A 1 220 ? 45.060 3.544   3.445   1.00 54.21  ? 220 ASP   A CG  1 
ATOM   1628 O OD1 . ASP   A 1 220 ? 43.929 3.093   3.742   1.00 53.94  ? 220 ASP   A OD1 1 
ATOM   1629 O OD2 . ASP   A 1 220 ? 45.945 2.862   2.892   1.00 61.55  ? 220 ASP   A OD2 1 
ATOM   1630 N N   . GLY   A 1 221 ? 47.478 7.709   3.629   1.00 49.30  ? 221 GLY   A N   1 
ATOM   1631 C CA  . GLY   A 1 221 ? 47.640 9.150   3.689   1.00 48.57  ? 221 GLY   A CA  1 
ATOM   1632 C C   . GLY   A 1 221 ? 48.091 9.686   2.352   1.00 53.54  ? 221 GLY   A C   1 
ATOM   1633 O O   . GLY   A 1 221 ? 47.687 10.788  1.953   1.00 53.29  ? 221 GLY   A O   1 
ATOM   1634 N N   . ARG   A 1 222 ? 48.912 8.883   1.629   1.00 50.81  ? 222 ARG   A N   1 
ATOM   1635 C CA  . ARG   A 1 222 ? 49.422 9.228   0.290   1.00 50.25  ? 222 ARG   A CA  1 
ATOM   1636 C C   . ARG   A 1 222 ? 48.232 9.284   -0.698  1.00 53.18  ? 222 ARG   A C   1 
ATOM   1637 O O   . ARG   A 1 222 ? 48.203 10.140  -1.575  1.00 52.41  ? 222 ARG   A O   1 
ATOM   1638 C CB  . ARG   A 1 222 ? 50.511 8.236   -0.165  1.00 48.71  ? 222 ARG   A CB  1 
ATOM   1639 C CG  . ARG   A 1 222 ? 51.341 8.702   -1.371  1.00 53.38  ? 222 ARG   A CG  1 
ATOM   1640 C CD  . ARG   A 1 222 ? 52.484 9.614   -0.985  1.00 54.74  ? 222 ARG   A CD  1 
ATOM   1641 N NE  . ARG   A 1 222 ? 53.535 9.634   -1.998  1.00 69.26  ? 222 ARG   A NE  1 
ATOM   1642 C CZ  . ARG   A 1 222 ? 54.773 10.071  -1.786  1.00 94.25  ? 222 ARG   A CZ  1 
ATOM   1643 N NH1 . ARG   A 1 222 ? 55.128 10.530  -0.592  1.00 89.22  ? 222 ARG   A NH1 1 
ATOM   1644 N NH2 . ARG   A 1 222 ? 55.669 10.045  -2.765  1.00 83.25  ? 222 ARG   A NH2 1 
ATOM   1645 N N   . PHE   A 1 223 ? 47.232 8.414   -0.498  1.00 49.42  ? 223 PHE   A N   1 
ATOM   1646 C CA  . PHE   A 1 223 ? 46.009 8.376   -1.305  1.00 49.48  ? 223 PHE   A CA  1 
ATOM   1647 C C   . PHE   A 1 223 ? 45.187 9.643   -1.049  1.00 53.80  ? 223 PHE   A C   1 
ATOM   1648 O O   . PHE   A 1 223 ? 44.821 10.322  -2.009  1.00 52.65  ? 223 PHE   A O   1 
ATOM   1649 C CB  . PHE   A 1 223 ? 45.176 7.116   -0.981  1.00 51.08  ? 223 PHE   A CB  1 
ATOM   1650 C CG  . PHE   A 1 223 ? 45.598 5.894   -1.756  1.00 52.55  ? 223 PHE   A CG  1 
ATOM   1651 C CD1 . PHE   A 1 223 ? 46.699 5.139   -1.355  1.00 54.22  ? 223 PHE   A CD1 1 
ATOM   1652 C CD2 . PHE   A 1 223 ? 44.891 5.488   -2.885  1.00 54.12  ? 223 PHE   A CD2 1 
ATOM   1653 C CE1 . PHE   A 1 223 ? 47.098 4.017   -2.082  1.00 54.36  ? 223 PHE   A CE1 1 
ATOM   1654 C CE2 . PHE   A 1 223 ? 45.286 4.355   -3.602  1.00 56.00  ? 223 PHE   A CE2 1 
ATOM   1655 C CZ  . PHE   A 1 223 ? 46.383 3.628   -3.194  1.00 53.49  ? 223 PHE   A CZ  1 
ATOM   1656 N N   . LYS   A 1 224 ? 44.908 9.959   0.250   1.00 51.11  ? 224 LYS   A N   1 
ATOM   1657 C CA  . LYS   A 1 224 ? 44.154 11.143  0.685   1.00 51.09  ? 224 LYS   A CA  1 
ATOM   1658 C C   . LYS   A 1 224 ? 44.811 12.439  0.180   1.00 56.04  ? 224 LYS   A C   1 
ATOM   1659 O O   . LYS   A 1 224 ? 44.098 13.314  -0.311  1.00 55.92  ? 224 LYS   A O   1 
ATOM   1660 C CB  . LYS   A 1 224 ? 43.989 11.176  2.215   1.00 53.20  ? 224 LYS   A CB  1 
ATOM   1661 C CG  . LYS   A 1 224 ? 43.031 12.258  2.675   1.00 62.23  ? 224 LYS   A CG  1 
ATOM   1662 C CD  . LYS   A 1 224 ? 43.073 12.539  4.168   1.00 70.25  ? 224 LYS   A CD  1 
ATOM   1663 C CE  . LYS   A 1 224 ? 43.016 14.023  4.487   1.00 78.58  ? 224 LYS   A CE  1 
ATOM   1664 N NZ  . LYS   A 1 224 ? 41.843 14.722  3.869   1.00 89.31  ? 224 LYS   A NZ  1 
ATOM   1665 N N   . ASP   A 1 225 ? 46.164 12.541  0.282   1.00 53.20  ? 225 ASP   A N   1 
ATOM   1666 C CA  . ASP   A 1 225 ? 46.933 13.708  -0.169  1.00 52.89  ? 225 ASP   A CA  1 
ATOM   1667 C C   . ASP   A 1 225 ? 46.912 13.861  -1.666  1.00 57.41  ? 225 ASP   A C   1 
ATOM   1668 O O   . ASP   A 1 225 ? 46.649 14.960  -2.135  1.00 58.14  ? 225 ASP   A O   1 
ATOM   1669 C CB  . ASP   A 1 225 ? 48.389 13.697  0.355   1.00 54.48  ? 225 ASP   A CB  1 
ATOM   1670 C CG  . ASP   A 1 225 ? 48.558 13.746  1.876   1.00 63.78  ? 225 ASP   A CG  1 
ATOM   1671 O OD1 . ASP   A 1 225 ? 47.586 14.137  2.580   1.00 62.66  ? 225 ASP   A OD1 1 
ATOM   1672 O OD2 . ASP   A 1 225 ? 49.664 13.392  2.365   1.00 69.43  ? 225 ASP   A OD2 1 
ATOM   1673 N N   . ILE   A 1 226 ? 47.184 12.775  -2.425  1.00 54.90  ? 226 ILE   A N   1 
ATOM   1674 C CA  . ILE   A 1 226 ? 47.190 12.806  -3.898  1.00 54.85  ? 226 ILE   A CA  1 
ATOM   1675 C C   . ILE   A 1 226 ? 45.810 13.200  -4.481  1.00 59.52  ? 226 ILE   A C   1 
ATOM   1676 O O   . ILE   A 1 226 ? 45.756 14.005  -5.416  1.00 61.08  ? 226 ILE   A O   1 
ATOM   1677 C CB  . ILE   A 1 226 ? 47.832 11.541  -4.547  1.00 57.36  ? 226 ILE   A CB  1 
ATOM   1678 C CG1 . ILE   A 1 226 ? 49.362 11.534  -4.333  1.00 56.72  ? 226 ILE   A CG1 1 
ATOM   1679 C CG2 . ILE   A 1 226 ? 47.493 11.432  -6.057  1.00 58.26  ? 226 ILE   A CG2 1 
ATOM   1680 C CD1 . ILE   A 1 226 ? 50.035 10.218  -4.598  1.00 58.27  ? 226 ILE   A CD1 1 
ATOM   1681 N N   . PHE   A 1 227 ? 44.714 12.672  -3.911  1.00 53.86  ? 227 PHE   A N   1 
ATOM   1682 C CA  . PHE   A 1 227 ? 43.368 13.003  -4.374  1.00 53.01  ? 227 PHE   A CA  1 
ATOM   1683 C C   . PHE   A 1 227 ? 43.051 14.480  -4.140  1.00 57.53  ? 227 PHE   A C   1 
ATOM   1684 O O   . PHE   A 1 227 ? 42.584 15.127  -5.072  1.00 58.69  ? 227 PHE   A O   1 
ATOM   1685 C CB  . PHE   A 1 227 ? 42.311 12.084  -3.752  1.00 53.98  ? 227 PHE   A CB  1 
ATOM   1686 C CG  . PHE   A 1 227 ? 42.025 10.790  -4.484  1.00 54.66  ? 227 PHE   A CG  1 
ATOM   1687 C CD1 . PHE   A 1 227 ? 43.010 9.812   -4.621  1.00 56.86  ? 227 PHE   A CD1 1 
ATOM   1688 C CD2 . PHE   A 1 227 ? 40.752 10.514  -4.969  1.00 55.71  ? 227 PHE   A CD2 1 
ATOM   1689 C CE1 . PHE   A 1 227 ? 42.736 8.602   -5.269  1.00 57.16  ? 227 PHE   A CE1 1 
ATOM   1690 C CE2 . PHE   A 1 227 ? 40.478 9.302   -5.614  1.00 58.03  ? 227 PHE   A CE2 1 
ATOM   1691 C CZ  . PHE   A 1 227 ? 41.472 8.355   -5.758  1.00 56.10  ? 227 PHE   A CZ  1 
ATOM   1692 N N   . GLN   A 1 228 ? 43.352 15.023  -2.936  1.00 53.50  ? 228 GLN   A N   1 
ATOM   1693 C CA  . GLN   A 1 228 ? 43.134 16.440  -2.604  1.00 53.83  ? 228 GLN   A CA  1 
ATOM   1694 C C   . GLN   A 1 228 ? 43.984 17.379  -3.476  1.00 58.26  ? 228 GLN   A C   1 
ATOM   1695 O O   . GLN   A 1 228 ? 43.441 18.362  -3.987  1.00 57.48  ? 228 GLN   A O   1 
ATOM   1696 C CB  . GLN   A 1 228 ? 43.380 16.742  -1.107  1.00 55.45  ? 228 GLN   A CB  1 
ATOM   1697 C CG  . GLN   A 1 228 ? 42.119 16.788  -0.229  1.00 65.39  ? 228 GLN   A CG  1 
ATOM   1698 C CD  . GLN   A 1 228 ? 41.050 17.765  -0.672  1.00 78.35  ? 228 GLN   A CD  1 
ATOM   1699 O OE1 . GLN   A 1 228 ? 41.317 18.820  -1.269  1.00 73.29  ? 228 GLN   A OE1 1 
ATOM   1700 N NE2 . GLN   A 1 228 ? 39.805 17.430  -0.380  1.00 71.16  ? 228 GLN   A NE2 1 
ATOM   1701 N N   . GLU   A 1 229 ? 45.303 17.062  -3.659  1.00 54.40  ? 229 GLU   A N   1 
ATOM   1702 C CA  . GLU   A 1 229 ? 46.236 17.846  -4.482  1.00 54.26  ? 229 GLU   A CA  1 
ATOM   1703 C C   . GLU   A 1 229 ? 45.723 17.964  -5.908  1.00 60.15  ? 229 GLU   A C   1 
ATOM   1704 O O   . GLU   A 1 229 ? 45.714 19.066  -6.456  1.00 60.34  ? 229 GLU   A O   1 
ATOM   1705 C CB  . GLU   A 1 229 ? 47.644 17.241  -4.464  1.00 55.67  ? 229 GLU   A CB  1 
ATOM   1706 C CG  . GLU   A 1 229 ? 48.459 17.664  -3.251  1.00 71.18  ? 229 GLU   A CG  1 
ATOM   1707 C CD  . GLU   A 1 229 ? 49.528 16.718  -2.725  1.00 97.99  ? 229 GLU   A CD  1 
ATOM   1708 O OE1 . GLU   A 1 229 ? 50.240 16.089  -3.542  1.00 95.62  ? 229 GLU   A OE1 1 
ATOM   1709 O OE2 . GLU   A 1 229 ? 49.661 16.623  -1.482  1.00 93.51  ? 229 GLU   A OE2 1 
ATOM   1710 N N   . ILE   A 1 230 ? 45.260 16.830  -6.496  1.00 56.88  ? 230 ILE   A N   1 
ATOM   1711 C CA  . ILE   A 1 230 ? 44.702 16.779  -7.848  1.00 56.09  ? 230 ILE   A CA  1 
ATOM   1712 C C   . ILE   A 1 230 ? 43.364 17.530  -7.883  1.00 61.45  ? 230 ILE   A C   1 
ATOM   1713 O O   . ILE   A 1 230 ? 43.133 18.314  -8.805  1.00 60.64  ? 230 ILE   A O   1 
ATOM   1714 C CB  . ILE   A 1 230 ? 44.641 15.324  -8.401  1.00 58.06  ? 230 ILE   A CB  1 
ATOM   1715 C CG1 . ILE   A 1 230 ? 46.079 14.781  -8.599  1.00 57.20  ? 230 ILE   A CG1 1 
ATOM   1716 C CG2 . ILE   A 1 230 ? 43.832 15.239  -9.719  1.00 57.32  ? 230 ILE   A CG2 1 
ATOM   1717 C CD1 . ILE   A 1 230 ? 46.201 13.361  -9.035  1.00 57.92  ? 230 ILE   A CD1 1 
ATOM   1718 N N   . TYR   A 1 231 ? 42.504 17.321  -6.863  1.00 60.11  ? 231 TYR   A N   1 
ATOM   1719 C CA  . TYR   A 1 231 ? 41.212 18.009  -6.787  1.00 60.66  ? 231 TYR   A CA  1 
ATOM   1720 C C   . TYR   A 1 231 ? 41.373 19.522  -6.799  1.00 65.25  ? 231 TYR   A C   1 
ATOM   1721 O O   . TYR   A 1 231 ? 40.854 20.174  -7.711  1.00 65.65  ? 231 TYR   A O   1 
ATOM   1722 C CB  . TYR   A 1 231 ? 40.407 17.582  -5.561  1.00 61.62  ? 231 TYR   A CB  1 
ATOM   1723 C CG  . TYR   A 1 231 ? 39.019 18.182  -5.523  1.00 63.52  ? 231 TYR   A CG  1 
ATOM   1724 C CD1 . TYR   A 1 231 ? 38.113 17.962  -6.558  1.00 65.36  ? 231 TYR   A CD1 1 
ATOM   1725 C CD2 . TYR   A 1 231 ? 38.597 18.944  -4.437  1.00 64.51  ? 231 TYR   A CD2 1 
ATOM   1726 C CE1 . TYR   A 1 231 ? 36.828 18.500  -6.521  1.00 66.06  ? 231 TYR   A CE1 1 
ATOM   1727 C CE2 . TYR   A 1 231 ? 37.308 19.475  -4.384  1.00 65.38  ? 231 TYR   A CE2 1 
ATOM   1728 C CZ  . TYR   A 1 231 ? 36.427 19.249  -5.429  1.00 71.85  ? 231 TYR   A CZ  1 
ATOM   1729 O OH  . TYR   A 1 231 ? 35.156 19.760  -5.385  1.00 73.61  ? 231 TYR   A OH  1 
ATOM   1730 N N   . ASP   A 1 232 ? 42.105 20.065  -5.796  1.00 60.93  ? 232 ASP   A N   1 
ATOM   1731 C CA  . ASP   A 1 232 ? 42.383 21.493  -5.627  1.00 59.85  ? 232 ASP   A CA  1 
ATOM   1732 C C   . ASP   A 1 232 ? 43.005 22.117  -6.868  1.00 63.21  ? 232 ASP   A C   1 
ATOM   1733 O O   . ASP   A 1 232 ? 42.572 23.193  -7.270  1.00 64.36  ? 232 ASP   A O   1 
ATOM   1734 C CB  . ASP   A 1 232 ? 43.248 21.757  -4.385  1.00 61.30  ? 232 ASP   A CB  1 
ATOM   1735 C CG  . ASP   A 1 232 ? 42.608 21.427  -3.046  1.00 68.69  ? 232 ASP   A CG  1 
ATOM   1736 O OD1 . ASP   A 1 232 ? 41.360 21.286  -2.995  1.00 69.30  ? 232 ASP   A OD1 1 
ATOM   1737 O OD2 . ASP   A 1 232 ? 43.354 21.324  -2.044  1.00 73.22  ? 232 ASP   A OD2 1 
ATOM   1738 N N   . LYS   A 1 233 ? 43.972 21.440  -7.497  1.00 59.01  ? 233 LYS   A N   1 
ATOM   1739 C CA  . LYS   A 1 233 ? 44.626 21.946  -8.703  1.00 59.28  ? 233 LYS   A CA  1 
ATOM   1740 C C   . LYS   A 1 233 ? 43.788 21.926  -9.992  1.00 66.50  ? 233 LYS   A C   1 
ATOM   1741 O O   . LYS   A 1 233 ? 43.542 22.999  -10.546 1.00 69.08  ? 233 LYS   A O   1 
ATOM   1742 C CB  . LYS   A 1 233 ? 46.013 21.305  -8.936  1.00 61.12  ? 233 LYS   A CB  1 
ATOM   1743 C CG  . LYS   A 1 233 ? 46.710 21.805  -10.214 1.00 73.85  ? 233 LYS   A CG  1 
ATOM   1744 C CD  . LYS   A 1 233 ? 48.051 21.142  -10.484 1.00 82.93  ? 233 LYS   A CD  1 
ATOM   1745 N N   . GLN   A 1 234 ? 43.399 20.741  -10.506 1.00 61.64  ? 234 GLN   A N   1 
ATOM   1746 C CA  . GLN   A 1 234 ? 42.688 20.686  -11.785 1.00 60.67  ? 234 GLN   A CA  1 
ATOM   1747 C C   . GLN   A 1 234 ? 41.196 20.336  -11.835 1.00 62.67  ? 234 GLN   A C   1 
ATOM   1748 O O   . GLN   A 1 234 ? 40.637 20.274  -12.938 1.00 61.38  ? 234 GLN   A O   1 
ATOM   1749 C CB  . GLN   A 1 234 ? 43.512 19.910  -12.842 1.00 61.94  ? 234 GLN   A CB  1 
ATOM   1750 C CG  . GLN   A 1 234 ? 44.034 18.548  -12.390 1.00 73.48  ? 234 GLN   A CG  1 
ATOM   1751 C CD  . GLN   A 1 234 ? 45.340 18.177  -13.060 1.00 89.89  ? 234 GLN   A CD  1 
ATOM   1752 O OE1 . GLN   A 1 234 ? 46.395 18.131  -12.423 1.00 79.78  ? 234 GLN   A OE1 1 
ATOM   1753 N NE2 . GLN   A 1 234 ? 45.305 17.896  -14.359 1.00 85.44  ? 234 GLN   A NE2 1 
ATOM   1754 N N   . TYR   A 1 235 ? 40.534 20.145  -10.678 1.00 58.88  ? 235 TYR   A N   1 
ATOM   1755 C CA  . TYR   A 1 235 ? 39.112 19.765  -10.706 1.00 58.16  ? 235 TYR   A CA  1 
ATOM   1756 C C   . TYR   A 1 235 ? 38.131 20.546  -9.849  1.00 64.10  ? 235 TYR   A C   1 
ATOM   1757 O O   . TYR   A 1 235 ? 36.931 20.453  -10.122 1.00 63.72  ? 235 TYR   A O   1 
ATOM   1758 C CB  . TYR   A 1 235 ? 38.939 18.250  -10.452 1.00 57.75  ? 235 TYR   A CB  1 
ATOM   1759 C CG  . TYR   A 1 235 ? 39.559 17.373  -11.517 1.00 56.44  ? 235 TYR   A CG  1 
ATOM   1760 C CD1 . TYR   A 1 235 ? 40.800 16.775  -11.321 1.00 57.39  ? 235 TYR   A CD1 1 
ATOM   1761 C CD2 . TYR   A 1 235 ? 38.905 17.138  -12.720 1.00 56.82  ? 235 TYR   A CD2 1 
ATOM   1762 C CE1 . TYR   A 1 235 ? 41.372 15.960  -12.297 1.00 57.43  ? 235 TYR   A CE1 1 
ATOM   1763 C CE2 . TYR   A 1 235 ? 39.473 16.333  -13.709 1.00 57.60  ? 235 TYR   A CE2 1 
ATOM   1764 C CZ  . TYR   A 1 235 ? 40.705 15.741  -13.491 1.00 62.98  ? 235 TYR   A CZ  1 
ATOM   1765 O OH  . TYR   A 1 235 ? 41.248 14.928  -14.456 1.00 61.34  ? 235 TYR   A OH  1 
ATOM   1766 N N   . LYS   A 1 236 ? 38.601 21.282  -8.814  1.00 63.01  ? 236 LYS   A N   1 
ATOM   1767 C CA  . LYS   A 1 236 ? 37.724 22.058  -7.917  1.00 64.15  ? 236 LYS   A CA  1 
ATOM   1768 C C   . LYS   A 1 236 ? 36.722 22.933  -8.678  1.00 71.67  ? 236 LYS   A C   1 
ATOM   1769 O O   . LYS   A 1 236 ? 35.525 22.861  -8.390  1.00 71.74  ? 236 LYS   A O   1 
ATOM   1770 C CB  . LYS   A 1 236 ? 38.531 22.882  -6.903  1.00 66.62  ? 236 LYS   A CB  1 
ATOM   1771 C CG  . LYS   A 1 236 ? 37.817 23.050  -5.567  1.00 73.60  ? 236 LYS   A CG  1 
ATOM   1772 C CD  . LYS   A 1 236 ? 38.656 23.844  -4.583  1.00 82.11  ? 236 LYS   A CD  1 
ATOM   1773 C CE  . LYS   A 1 236 ? 38.315 23.521  -3.146  1.00 93.63  ? 236 LYS   A CE  1 
ATOM   1774 N NZ  . LYS   A 1 236 ? 37.014 24.110  -2.723  1.00 98.50  ? 236 LYS   A NZ  1 
ATOM   1775 N N   . SER   A 1 237 ? 37.206 23.713  -9.676  1.00 70.51  ? 237 SER   A N   1 
ATOM   1776 C CA  . SER   A 1 237 ? 36.383 24.590  -10.520 1.00 71.30  ? 237 SER   A CA  1 
ATOM   1777 C C   . SER   A 1 237 ? 35.247 23.828  -11.249 1.00 75.65  ? 237 SER   A C   1 
ATOM   1778 O O   . SER   A 1 237 ? 34.076 24.103  -10.974 1.00 75.97  ? 237 SER   A O   1 
ATOM   1779 C CB  . SER   A 1 237 ? 37.254 25.359  -11.511 1.00 76.32  ? 237 SER   A CB  1 
ATOM   1780 O OG  . SER   A 1 237 ? 37.956 24.479  -12.376 1.00 90.15  ? 237 SER   A OG  1 
ATOM   1781 N N   . GLN   A 1 238 ? 35.594 22.862  -12.140 1.00 71.40  ? 238 GLN   A N   1 
ATOM   1782 C CA  . GLN   A 1 238 ? 34.660 22.030  -12.923 1.00 71.03  ? 238 GLN   A CA  1 
ATOM   1783 C C   . GLN   A 1 238 ? 33.546 21.356  -12.075 1.00 75.90  ? 238 GLN   A C   1 
ATOM   1784 O O   . GLN   A 1 238 ? 32.389 21.303  -12.509 1.00 76.19  ? 238 GLN   A O   1 
ATOM   1785 C CB  . GLN   A 1 238 ? 35.427 20.993  -13.771 1.00 72.13  ? 238 GLN   A CB  1 
ATOM   1786 C CG  . GLN   A 1 238 ? 36.472 21.609  -14.714 1.00 84.09  ? 238 GLN   A CG  1 
ATOM   1787 C CD  . GLN   A 1 238 ? 37.214 20.598  -15.568 1.00 100.88 ? 238 GLN   A CD  1 
ATOM   1788 O OE1 . GLN   A 1 238 ? 36.634 19.907  -16.415 1.00 97.85  ? 238 GLN   A OE1 1 
ATOM   1789 N NE2 . GLN   A 1 238 ? 38.523 20.501  -15.379 1.00 87.79  ? 238 GLN   A NE2 1 
ATOM   1790 N N   . PHE   A 1 239 ? 33.903 20.864  -10.865 1.00 71.92  ? 239 PHE   A N   1 
ATOM   1791 C CA  . PHE   A 1 239 ? 33.010 20.211  -9.896  1.00 70.81  ? 239 PHE   A CA  1 
ATOM   1792 C C   . PHE   A 1 239 ? 32.011 21.223  -9.337  1.00 74.91  ? 239 PHE   A C   1 
ATOM   1793 O O   . PHE   A 1 239 ? 30.809 20.938  -9.304  1.00 74.66  ? 239 PHE   A O   1 
ATOM   1794 C CB  . PHE   A 1 239 ? 33.831 19.570  -8.746  1.00 71.92  ? 239 PHE   A CB  1 
ATOM   1795 C CG  . PHE   A 1 239 ? 34.226 18.123  -8.943  1.00 72.11  ? 239 PHE   A CG  1 
ATOM   1796 C CD1 . PHE   A 1 239 ? 35.126 17.757  -9.938  1.00 74.08  ? 239 PHE   A CD1 1 
ATOM   1797 C CD2 . PHE   A 1 239 ? 33.727 17.130  -8.110  1.00 72.80  ? 239 PHE   A CD2 1 
ATOM   1798 C CE1 . PHE   A 1 239 ? 35.481 16.419  -10.126 1.00 74.26  ? 239 PHE   A CE1 1 
ATOM   1799 C CE2 . PHE   A 1 239 ? 34.082 15.792  -8.300  1.00 74.81  ? 239 PHE   A CE2 1 
ATOM   1800 C CZ  . PHE   A 1 239 ? 34.959 15.448  -9.301  1.00 72.72  ? 239 PHE   A CZ  1 
ATOM   1801 N N   . GLU   A 1 240 ? 32.506 22.406  -8.902  1.00 71.78  ? 240 GLU   A N   1 
ATOM   1802 C CA  . GLU   A 1 240 ? 31.675 23.493  -8.361  1.00 71.74  ? 240 GLU   A CA  1 
ATOM   1803 C C   . GLU   A 1 240 ? 30.726 24.022  -9.443  1.00 75.00  ? 240 GLU   A C   1 
ATOM   1804 O O   . GLU   A 1 240 ? 29.559 24.285  -9.155  1.00 74.38  ? 240 GLU   A O   1 
ATOM   1805 C CB  . GLU   A 1 240 ? 32.539 24.616  -7.765  1.00 73.10  ? 240 GLU   A CB  1 
ATOM   1806 C CG  . GLU   A 1 240 ? 33.124 24.259  -6.405  1.00 82.54  ? 240 GLU   A CG  1 
ATOM   1807 C CD  . GLU   A 1 240 ? 34.159 25.214  -5.835  1.00 99.76  ? 240 GLU   A CD  1 
ATOM   1808 O OE1 . GLU   A 1 240 ? 34.953 25.786  -6.620  1.00 78.54  ? 240 GLU   A OE1 1 
ATOM   1809 O OE2 . GLU   A 1 240 ? 34.182 25.378  -4.591  1.00 93.82  ? 240 GLU   A OE2 1 
ATOM   1810 N N   . ALA   A 1 241 ? 31.220 24.107  -10.698 1.00 71.39  ? 241 ALA   A N   1 
ATOM   1811 C CA  . ALA   A 1 241 ? 30.472 24.534  -11.884 1.00 71.17  ? 241 ALA   A CA  1 
ATOM   1812 C C   . ALA   A 1 241 ? 29.267 23.609  -12.147 1.00 77.06  ? 241 ALA   A C   1 
ATOM   1813 O O   . ALA   A 1 241 ? 28.300 24.036  -12.789 1.00 77.55  ? 241 ALA   A O   1 
ATOM   1814 C CB  . ALA   A 1 241 ? 31.387 24.551  -13.101 1.00 71.36  ? 241 ALA   A CB  1 
ATOM   1815 N N   . GLN   A 1 242 ? 29.326 22.349  -11.647 1.00 73.22  ? 242 GLN   A N   1 
ATOM   1816 C CA  . GLN   A 1 242 ? 28.264 21.351  -11.809 1.00 72.59  ? 242 GLN   A CA  1 
ATOM   1817 C C   . GLN   A 1 242 ? 27.480 21.111  -10.498 1.00 76.96  ? 242 GLN   A C   1 
ATOM   1818 O O   . GLN   A 1 242 ? 26.654 20.199  -10.439 1.00 75.58  ? 242 GLN   A O   1 
ATOM   1819 C CB  . GLN   A 1 242 ? 28.819 20.043  -12.432 1.00 73.38  ? 242 GLN   A CB  1 
ATOM   1820 C CG  . GLN   A 1 242 ? 29.312 20.203  -13.886 1.00 78.92  ? 242 GLN   A CG  1 
ATOM   1821 C CD  . GLN   A 1 242 ? 29.604 18.901  -14.620 1.00 88.44  ? 242 GLN   A CD  1 
ATOM   1822 O OE1 . GLN   A 1 242 ? 28.858 17.916  -14.548 1.00 83.22  ? 242 GLN   A OE1 1 
ATOM   1823 N NE2 . GLN   A 1 242 ? 30.695 18.871  -15.369 1.00 74.95  ? 242 GLN   A NE2 1 
ATOM   1824 N N   . LYS   A 1 243 ? 27.722 21.960  -9.461  1.00 75.58  ? 243 LYS   A N   1 
ATOM   1825 C CA  . LYS   A 1 243 ? 27.103 21.916  -8.115  1.00 76.12  ? 243 LYS   A CA  1 
ATOM   1826 C C   . LYS   A 1 243 ? 27.387 20.563  -7.420  1.00 80.53  ? 243 LYS   A C   1 
ATOM   1827 O O   . LYS   A 1 243 ? 26.565 20.012  -6.670  1.00 79.48  ? 243 LYS   A O   1 
ATOM   1828 C CB  . LYS   A 1 243 ? 25.599 22.272  -8.156  1.00 78.77  ? 243 LYS   A CB  1 
ATOM   1829 N N   . ILE   A 1 244 ? 28.599 20.055  -7.695  1.00 77.70  ? 244 ILE   A N   1 
ATOM   1830 C CA  . ILE   A 1 244 ? 29.161 18.780  -7.248  1.00 77.16  ? 244 ILE   A CA  1 
ATOM   1831 C C   . ILE   A 1 244 ? 30.450 19.060  -6.436  1.00 80.71  ? 244 ILE   A C   1 
ATOM   1832 O O   . ILE   A 1 244 ? 30.987 20.169  -6.508  1.00 82.16  ? 244 ILE   A O   1 
ATOM   1833 C CB  . ILE   A 1 244 ? 29.326 17.901  -8.550  1.00 79.70  ? 244 ILE   A CB  1 
ATOM   1834 C CG1 . ILE   A 1 244 ? 27.975 17.349  -9.075  1.00 79.58  ? 244 ILE   A CG1 1 
ATOM   1835 C CG2 . ILE   A 1 244 ? 30.373 16.823  -8.499  1.00 80.45  ? 244 ILE   A CG2 1 
ATOM   1836 C CD1 . ILE   A 1 244 ? 26.962 16.830  -8.017  1.00 86.43  ? 244 ILE   A CD1 1 
ATOM   1837 N N   . TRP   A 1 245 ? 30.908 18.085  -5.636  1.00 74.20  ? 245 TRP   A N   1 
ATOM   1838 C CA  . TRP   A 1 245 ? 32.102 18.205  -4.792  1.00 72.40  ? 245 TRP   A CA  1 
ATOM   1839 C C   . TRP   A 1 245 ? 32.858 16.860  -4.686  1.00 73.75  ? 245 TRP   A C   1 
ATOM   1840 O O   . TRP   A 1 245 ? 32.378 15.838  -5.179  1.00 73.21  ? 245 TRP   A O   1 
ATOM   1841 C CB  . TRP   A 1 245 ? 31.665 18.645  -3.385  1.00 70.58  ? 245 TRP   A CB  1 
ATOM   1842 C CG  . TRP   A 1 245 ? 30.711 17.674  -2.745  1.00 71.27  ? 245 TRP   A CG  1 
ATOM   1843 C CD1 . TRP   A 1 245 ? 31.027 16.631  -1.924  1.00 74.01  ? 245 TRP   A CD1 1 
ATOM   1844 C CD2 . TRP   A 1 245 ? 29.289 17.632  -2.922  1.00 71.16  ? 245 TRP   A CD2 1 
ATOM   1845 N NE1 . TRP   A 1 245 ? 29.888 15.948  -1.564  1.00 73.28  ? 245 TRP   A NE1 1 
ATOM   1846 C CE2 . TRP   A 1 245 ? 28.805 16.545  -2.159  1.00 74.98  ? 245 TRP   A CE2 1 
ATOM   1847 C CE3 . TRP   A 1 245 ? 28.369 18.421  -3.641  1.00 72.38  ? 245 TRP   A CE3 1 
ATOM   1848 C CZ2 . TRP   A 1 245 ? 27.442 16.213  -2.111  1.00 74.42  ? 245 TRP   A CZ2 1 
ATOM   1849 C CZ3 . TRP   A 1 245 ? 27.022 18.096  -3.588  1.00 73.85  ? 245 TRP   A CZ3 1 
ATOM   1850 C CH2 . TRP   A 1 245 ? 26.568 17.007  -2.827  1.00 74.51  ? 245 TRP   A CH2 1 
ATOM   1851 N N   . TYR   A 1 246 ? 34.029 16.872  -4.028  1.00 68.03  ? 246 TYR   A N   1 
ATOM   1852 C CA  . TYR   A 1 246 ? 34.833 15.687  -3.742  1.00 66.69  ? 246 TYR   A CA  1 
ATOM   1853 C C   . TYR   A 1 246 ? 35.141 15.728  -2.243  1.00 69.23  ? 246 TYR   A C   1 
ATOM   1854 O O   . TYR   A 1 246 ? 35.526 16.787  -1.745  1.00 69.11  ? 246 TYR   A O   1 
ATOM   1855 C CB  . TYR   A 1 246 ? 36.131 15.580  -4.584  1.00 66.95  ? 246 TYR   A CB  1 
ATOM   1856 C CG  . TYR   A 1 246 ? 37.187 14.742  -3.885  1.00 67.29  ? 246 TYR   A CG  1 
ATOM   1857 C CD1 . TYR   A 1 246 ? 38.269 15.343  -3.245  1.00 69.12  ? 246 TYR   A CD1 1 
ATOM   1858 C CD2 . TYR   A 1 246 ? 37.046 13.360  -3.771  1.00 67.19  ? 246 TYR   A CD2 1 
ATOM   1859 C CE1 . TYR   A 1 246 ? 39.201 14.587  -2.536  1.00 69.27  ? 246 TYR   A CE1 1 
ATOM   1860 C CE2 . TYR   A 1 246 ? 37.965 12.597  -3.055  1.00 67.72  ? 246 TYR   A CE2 1 
ATOM   1861 C CZ  . TYR   A 1 246 ? 39.047 13.214  -2.449  1.00 73.21  ? 246 TYR   A CZ  1 
ATOM   1862 O OH  . TYR   A 1 246 ? 39.955 12.467  -1.747  1.00 70.01  ? 246 TYR   A OH  1 
ATOM   1863 N N   . GLU   A 1 247 ? 34.988 14.591  -1.530  1.00 64.35  ? 247 GLU   A N   1 
ATOM   1864 C CA  . GLU   A 1 247 ? 35.255 14.525  -0.087  1.00 63.56  ? 247 GLU   A CA  1 
ATOM   1865 C C   . GLU   A 1 247 ? 35.904 13.208  0.363   1.00 65.40  ? 247 GLU   A C   1 
ATOM   1866 O O   . GLU   A 1 247 ? 35.472 12.139  -0.069  1.00 64.04  ? 247 GLU   A O   1 
ATOM   1867 C CB  . GLU   A 1 247 ? 33.948 14.718  0.710   1.00 65.00  ? 247 GLU   A CB  1 
ATOM   1868 C CG  . GLU   A 1 247 ? 33.414 16.140  0.769   1.00 75.46  ? 247 GLU   A CG  1 
ATOM   1869 C CD  . GLU   A 1 247 ? 32.258 16.384  1.724   1.00 95.94  ? 247 GLU   A CD  1 
ATOM   1870 O OE1 . GLU   A 1 247 ? 31.723 17.517  1.712   1.00 91.92  ? 247 GLU   A OE1 1 
ATOM   1871 O OE2 . GLU   A 1 247 ? 31.889 15.459  2.484   1.00 85.73  ? 247 GLU   A OE2 1 
ATOM   1872 N N   . HIS   A 1 248 ? 36.918 13.285  1.262   1.00 61.22  ? 248 HIS   A N   1 
ATOM   1873 C CA  . HIS   A 1 248 ? 37.557 12.096  1.836   1.00 60.09  ? 248 HIS   A CA  1 
ATOM   1874 C C   . HIS   A 1 248 ? 36.757 11.689  3.084   1.00 65.26  ? 248 HIS   A C   1 
ATOM   1875 O O   . HIS   A 1 248 ? 36.444 12.539  3.918   1.00 65.68  ? 248 HIS   A O   1 
ATOM   1876 C CB  . HIS   A 1 248 ? 39.035 12.327  2.214   1.00 59.88  ? 248 HIS   A CB  1 
ATOM   1877 C CG  . HIS   A 1 248 ? 39.607 11.206  3.047   1.00 62.83  ? 248 HIS   A CG  1 
ATOM   1878 N ND1 . HIS   A 1 248 ? 40.290 10.148  2.470   1.00 64.01  ? 248 HIS   A ND1 1 
ATOM   1879 C CD2 . HIS   A 1 248 ? 39.537 10.992  4.384   1.00 63.92  ? 248 HIS   A CD2 1 
ATOM   1880 C CE1 . HIS   A 1 248 ? 40.622 9.352   3.467   1.00 62.65  ? 248 HIS   A CE1 1 
ATOM   1881 N NE2 . HIS   A 1 248 ? 40.190 9.813   4.633   1.00 63.01  ? 248 HIS   A NE2 1 
ATOM   1882 N N   . ARG   A 1 249 ? 36.447 10.394  3.214   1.00 61.99  ? 249 ARG   A N   1 
ATOM   1883 C CA  . ARG   A 1 249 ? 35.708 9.843   4.346   1.00 62.26  ? 249 ARG   A CA  1 
ATOM   1884 C C   . ARG   A 1 249 ? 36.388 8.552   4.786   1.00 68.67  ? 249 ARG   A C   1 
ATOM   1885 O O   . ARG   A 1 249 ? 36.708 7.722   3.936   1.00 68.50  ? 249 ARG   A O   1 
ATOM   1886 C CB  . ARG   A 1 249 ? 34.238 9.533   3.970   1.00 62.59  ? 249 ARG   A CB  1 
ATOM   1887 C CG  . ARG   A 1 249 ? 33.392 10.703  3.448   1.00 78.37  ? 249 ARG   A CG  1 
ATOM   1888 C CD  . ARG   A 1 249 ? 33.154 11.794  4.480   1.00 90.50  ? 249 ARG   A CD  1 
ATOM   1889 N NE  . ARG   A 1 249 ? 32.213 12.805  3.998   1.00 100.30 ? 249 ARG   A NE  1 
ATOM   1890 C CZ  . ARG   A 1 249 ? 30.927 12.844  4.330   1.00 120.45 ? 249 ARG   A CZ  1 
ATOM   1891 N NH1 . ARG   A 1 249 ? 30.415 11.930  5.147   1.00 109.51 ? 249 ARG   A NH1 1 
ATOM   1892 N NH2 . ARG   A 1 249 ? 30.140 13.797  3.847   1.00 110.08 ? 249 ARG   A NH2 1 
ATOM   1893 N N   . LEU   A 1 250 ? 36.604 8.372   6.106   1.00 66.39  ? 250 LEU   A N   1 
ATOM   1894 C CA  . LEU   A 1 250 ? 37.207 7.155   6.645   1.00 66.64  ? 250 LEU   A CA  1 
ATOM   1895 C C   . LEU   A 1 250 ? 36.188 6.031   6.401   1.00 71.18  ? 250 LEU   A C   1 
ATOM   1896 O O   . LEU   A 1 250 ? 34.983 6.257   6.558   1.00 70.41  ? 250 LEU   A O   1 
ATOM   1897 C CB  . LEU   A 1 250 ? 37.530 7.314   8.152   1.00 66.91  ? 250 LEU   A CB  1 
ATOM   1898 C CG  . LEU   A 1 250 ? 38.931 7.846   8.569   1.00 72.17  ? 250 LEU   A CG  1 
ATOM   1899 C CD1 . LEU   A 1 250 ? 40.057 6.882   8.188   1.00 72.31  ? 250 LEU   A CD1 1 
ATOM   1900 C CD2 . LEU   A 1 250 ? 39.203 9.269   8.068   1.00 75.68  ? 250 LEU   A CD2 1 
ATOM   1901 N N   . ILE   A 1 251 ? 36.665 4.853   5.965   1.00 68.46  ? 251 ILE   A N   1 
ATOM   1902 C CA  . ILE   A 1 251 ? 35.840 3.696   5.618   1.00 69.05  ? 251 ILE   A CA  1 
ATOM   1903 C C   . ILE   A 1 251 ? 34.512 3.510   6.394   1.00 74.12  ? 251 ILE   A C   1 
ATOM   1904 O O   . ILE   A 1 251 ? 33.456 3.530   5.765   1.00 72.70  ? 251 ILE   A O   1 
ATOM   1905 C CB  . ILE   A 1 251 ? 36.680 2.406   5.378   1.00 72.40  ? 251 ILE   A CB  1 
ATOM   1906 C CG1 . ILE   A 1 251 ? 36.374 1.726   4.010   1.00 73.01  ? 251 ILE   A CG1 1 
ATOM   1907 C CG2 . ILE   A 1 251 ? 36.752 1.438   6.574   1.00 73.09  ? 251 ILE   A CG2 1 
ATOM   1908 C CD1 . ILE   A 1 251 ? 34.919 1.150   3.758   1.00 78.57  ? 251 ILE   A CD1 1 
ATOM   1909 N N   . ASP   A 1 252 ? 34.565 3.396   7.738   1.00 72.84  ? 252 ASP   A N   1 
ATOM   1910 C CA  . ASP   A 1 252 ? 33.392 3.215   8.607   1.00 73.43  ? 252 ASP   A CA  1 
ATOM   1911 C C   . ASP   A 1 252 ? 32.363 4.349   8.506   1.00 76.98  ? 252 ASP   A C   1 
ATOM   1912 O O   . ASP   A 1 252 ? 31.160 4.078   8.447   1.00 76.04  ? 252 ASP   A O   1 
ATOM   1913 C CB  . ASP   A 1 252 ? 33.827 2.964   10.054  1.00 76.15  ? 252 ASP   A CB  1 
ATOM   1914 C CG  . ASP   A 1 252 ? 34.578 1.655   10.219  1.00 93.42  ? 252 ASP   A CG  1 
ATOM   1915 O OD1 . ASP   A 1 252 ? 35.804 1.636   9.959   1.00 95.58  ? 252 ASP   A OD1 1 
ATOM   1916 O OD2 . ASP   A 1 252 ? 33.941 0.649   10.603  1.00 100.56 ? 252 ASP   A OD2 1 
ATOM   1917 N N   . ASP   A 1 253 ? 32.838 5.612   8.445   1.00 73.77  ? 253 ASP   A N   1 
ATOM   1918 C CA  . ASP   A 1 253 ? 31.990 6.801   8.302   1.00 73.64  ? 253 ASP   A CA  1 
ATOM   1919 C C   . ASP   A 1 253 ? 31.395 6.862   6.879   1.00 78.31  ? 253 ASP   A C   1 
ATOM   1920 O O   . ASP   A 1 253 ? 30.320 7.440   6.684   1.00 78.64  ? 253 ASP   A O   1 
ATOM   1921 C CB  . ASP   A 1 253 ? 32.786 8.082   8.618   1.00 75.26  ? 253 ASP   A CB  1 
ATOM   1922 N N   . MET   A 1 254 ? 32.100 6.252   5.896   1.00 73.83  ? 254 MET   A N   1 
ATOM   1923 C CA  . MET   A 1 254 ? 31.689 6.197   4.494   1.00 72.70  ? 254 MET   A CA  1 
ATOM   1924 C C   . MET   A 1 254 ? 30.560 5.178   4.269   1.00 76.55  ? 254 MET   A C   1 
ATOM   1925 O O   . MET   A 1 254 ? 29.599 5.497   3.566   1.00 75.84  ? 254 MET   A O   1 
ATOM   1926 C CB  . MET   A 1 254 ? 32.902 5.933   3.579   1.00 74.44  ? 254 MET   A CB  1 
ATOM   1927 C CG  . MET   A 1 254 ? 32.589 6.003   2.098   1.00 77.10  ? 254 MET   A CG  1 
ATOM   1928 S SD  . MET   A 1 254 ? 31.941 7.590   1.540   1.00 80.32  ? 254 MET   A SD  1 
ATOM   1929 C CE  . MET   A 1 254 ? 30.622 7.042   0.507   1.00 76.72  ? 254 MET   A CE  1 
ATOM   1930 N N   . VAL   A 1 255 ? 30.672 3.962   4.853   1.00 73.39  ? 255 VAL   A N   1 
ATOM   1931 C CA  . VAL   A 1 255 ? 29.630 2.937   4.718   1.00 73.17  ? 255 VAL   A CA  1 
ATOM   1932 C C   . VAL   A 1 255 ? 28.351 3.370   5.454   1.00 78.93  ? 255 VAL   A C   1 
ATOM   1933 O O   . VAL   A 1 255 ? 27.253 3.186   4.930   1.00 78.77  ? 255 VAL   A O   1 
ATOM   1934 C CB  . VAL   A 1 255 ? 30.079 1.449   4.920   1.00 76.73  ? 255 VAL   A CB  1 
ATOM   1935 C CG1 . VAL   A 1 255 ? 31.432 1.330   5.613   1.00 76.25  ? 255 VAL   A CG1 1 
ATOM   1936 C CG2 . VAL   A 1 255 ? 29.021 0.592   5.620   1.00 76.49  ? 255 VAL   A CG2 1 
ATOM   1937 N N   . ALA   A 1 256 ? 28.505 4.016   6.629   1.00 76.60  ? 256 ALA   A N   1 
ATOM   1938 C CA  . ALA   A 1 256 ? 27.391 4.535   7.428   1.00 76.55  ? 256 ALA   A CA  1 
ATOM   1939 C C   . ALA   A 1 256 ? 26.626 5.603   6.631   1.00 81.44  ? 256 ALA   A C   1 
ATOM   1940 O O   . ALA   A 1 256 ? 25.393 5.630   6.679   1.00 81.39  ? 256 ALA   A O   1 
ATOM   1941 C CB  . ALA   A 1 256 ? 27.912 5.125   8.730   1.00 77.25  ? 256 ALA   A CB  1 
ATOM   1942 N N   . GLN   A 1 257 ? 27.363 6.465   5.883   1.00 78.24  ? 257 GLN   A N   1 
ATOM   1943 C CA  . GLN   A 1 257 ? 26.804 7.526   5.042   1.00 78.10  ? 257 GLN   A CA  1 
ATOM   1944 C C   . GLN   A 1 257 ? 26.014 6.917   3.872   1.00 82.79  ? 257 GLN   A C   1 
ATOM   1945 O O   . GLN   A 1 257 ? 24.844 7.266   3.687   1.00 82.32  ? 257 GLN   A O   1 
ATOM   1946 C CB  . GLN   A 1 257 ? 27.912 8.483   4.537   1.00 79.13  ? 257 GLN   A CB  1 
ATOM   1947 C CG  . GLN   A 1 257 ? 27.453 9.407   3.404   1.00 90.91  ? 257 GLN   A CG  1 
ATOM   1948 C CD  . GLN   A 1 257 ? 28.407 10.525  3.101   1.00 111.94 ? 257 GLN   A CD  1 
ATOM   1949 O OE1 . GLN   A 1 257 ? 28.178 11.678  3.473   1.00 110.44 ? 257 GLN   A OE1 1 
ATOM   1950 N NE2 . GLN   A 1 257 ? 29.491 10.218  2.411   1.00 103.29 ? 257 GLN   A NE2 1 
ATOM   1951 N N   . ALA   A 1 258 ? 26.669 6.011   3.097   1.00 79.46  ? 258 ALA   A N   1 
ATOM   1952 C CA  . ALA   A 1 258 ? 26.129 5.299   1.929   1.00 78.88  ? 258 ALA   A CA  1 
ATOM   1953 C C   . ALA   A 1 258 ? 24.846 4.535   2.244   1.00 81.07  ? 258 ALA   A C   1 
ATOM   1954 O O   . ALA   A 1 258 ? 23.915 4.562   1.443   1.00 80.38  ? 258 ALA   A O   1 
ATOM   1955 C CB  . ALA   A 1 258 ? 27.177 4.349   1.366   1.00 79.63  ? 258 ALA   A CB  1 
ATOM   1956 N N   . MET   A 1 259 ? 24.793 3.879   3.414   1.00 77.47  ? 259 MET   A N   1 
ATOM   1957 C CA  . MET   A 1 259 ? 23.628 3.115   3.868   1.00 77.41  ? 259 MET   A CA  1 
ATOM   1958 C C   . MET   A 1 259 ? 22.449 4.021   4.260   1.00 81.50  ? 259 MET   A C   1 
ATOM   1959 O O   . MET   A 1 259 ? 21.292 3.600   4.150   1.00 81.28  ? 259 MET   A O   1 
ATOM   1960 C CB  . MET   A 1 259 ? 24.004 2.180   5.022   1.00 79.72  ? 259 MET   A CB  1 
ATOM   1961 C CG  . MET   A 1 259 ? 24.976 1.080   4.622   1.00 83.72  ? 259 MET   A CG  1 
ATOM   1962 S SD  . MET   A 1 259 ? 24.301 -0.149  3.486   1.00 88.41  ? 259 MET   A SD  1 
ATOM   1963 C CE  . MET   A 1 259 ? 23.300 -1.113  4.635   1.00 85.16  ? 259 MET   A CE  1 
ATOM   1964 N N   . LYS   A 1 260 ? 22.745 5.258   4.709   1.00 77.73  ? 260 LYS   A N   1 
ATOM   1965 C CA  . LYS   A 1 260 ? 21.739 6.247   5.111   1.00 77.62  ? 260 LYS   A CA  1 
ATOM   1966 C C   . LYS   A 1 260 ? 21.384 7.200   3.954   1.00 81.71  ? 260 LYS   A C   1 
ATOM   1967 O O   . LYS   A 1 260 ? 20.599 8.130   4.151   1.00 81.81  ? 260 LYS   A O   1 
ATOM   1968 C CB  . LYS   A 1 260 ? 22.228 7.037   6.343   1.00 79.66  ? 260 LYS   A CB  1 
ATOM   1969 N N   . SER   A 1 261 ? 21.961 6.963   2.753   1.00 77.57  ? 261 SER   A N   1 
ATOM   1970 C CA  . SER   A 1 261 ? 21.765 7.785   1.557   1.00 77.20  ? 261 SER   A CA  1 
ATOM   1971 C C   . SER   A 1 261 ? 20.780 7.202   0.544   1.00 80.87  ? 261 SER   A C   1 
ATOM   1972 O O   . SER   A 1 261 ? 20.322 6.063   0.697   1.00 80.73  ? 261 SER   A O   1 
ATOM   1973 C CB  . SER   A 1 261 ? 23.106 8.081   0.886   1.00 80.94  ? 261 SER   A CB  1 
ATOM   1974 O OG  . SER   A 1 261 ? 23.631 6.952   0.207   1.00 88.87  ? 261 SER   A OG  1 
ATOM   1975 N N   . GLU   A 1 262 ? 20.464 8.002   -0.498  1.00 76.80  ? 262 GLU   A N   1 
ATOM   1976 C CA  . GLU   A 1 262 ? 19.553 7.647   -1.589  1.00 76.42  ? 262 GLU   A CA  1 
ATOM   1977 C C   . GLU   A 1 262 ? 20.318 7.255   -2.871  1.00 79.56  ? 262 GLU   A C   1 
ATOM   1978 O O   . GLU   A 1 262 ? 19.703 7.104   -3.935  1.00 80.05  ? 262 GLU   A O   1 
ATOM   1979 C CB  . GLU   A 1 262 ? 18.587 8.812   -1.867  1.00 77.84  ? 262 GLU   A CB  1 
ATOM   1980 N N   . GLY   A 1 263 ? 21.636 7.081   -2.749  1.00 73.80  ? 263 GLY   A N   1 
ATOM   1981 C CA  . GLY   A 1 263 ? 22.505 6.736   -3.867  1.00 72.80  ? 263 GLY   A CA  1 
ATOM   1982 C C   . GLY   A 1 263 ? 22.836 7.958   -4.700  1.00 75.62  ? 263 GLY   A C   1 
ATOM   1983 O O   . GLY   A 1 263 ? 22.669 9.089   -4.232  1.00 76.77  ? 263 GLY   A O   1 
ATOM   1984 N N   . GLY   A 1 264 ? 23.316 7.736   -5.921  1.00 69.60  ? 264 GLY   A N   1 
ATOM   1985 C CA  . GLY   A 1 264 ? 23.667 8.813   -6.843  1.00 68.51  ? 264 GLY   A CA  1 
ATOM   1986 C C   . GLY   A 1 264 ? 25.002 9.478   -6.592  1.00 70.02  ? 264 GLY   A C   1 
ATOM   1987 O O   . GLY   A 1 264 ? 25.115 10.708  -6.658  1.00 69.67  ? 264 GLY   A O   1 
ATOM   1988 N N   . PHE   A 1 265 ? 26.026 8.661   -6.320  1.00 64.20  ? 265 PHE   A N   1 
ATOM   1989 C CA  . PHE   A 1 265 ? 27.386 9.137   -6.074  1.00 62.01  ? 265 PHE   A CA  1 
ATOM   1990 C C   . PHE   A 1 265 ? 28.453 8.151   -6.563  1.00 61.95  ? 265 PHE   A C   1 
ATOM   1991 O O   . PHE   A 1 265 ? 28.163 6.970   -6.783  1.00 60.79  ? 265 PHE   A O   1 
ATOM   1992 C CB  . PHE   A 1 265 ? 27.592 9.484   -4.578  1.00 62.86  ? 265 PHE   A CB  1 
ATOM   1993 C CG  . PHE   A 1 265 ? 27.484 8.325   -3.615  1.00 62.84  ? 265 PHE   A CG  1 
ATOM   1994 C CD1 . PHE   A 1 265 ? 28.610 7.590   -3.256  1.00 64.27  ? 265 PHE   A CD1 1 
ATOM   1995 C CD2 . PHE   A 1 265 ? 26.260 7.986   -3.043  1.00 63.30  ? 265 PHE   A CD2 1 
ATOM   1996 C CE1 . PHE   A 1 265 ? 28.509 6.513   -2.372  1.00 64.31  ? 265 PHE   A CE1 1 
ATOM   1997 C CE2 . PHE   A 1 265 ? 26.161 6.920   -2.146  1.00 65.20  ? 265 PHE   A CE2 1 
ATOM   1998 C CZ  . PHE   A 1 265 ? 27.285 6.190   -1.819  1.00 63.43  ? 265 PHE   A CZ  1 
ATOM   1999 N N   . ILE   A 1 266 ? 29.691 8.656   -6.717  1.00 55.74  ? 266 ILE   A N   1 
ATOM   2000 C CA  . ILE   A 1 266 ? 30.850 7.858   -7.102  1.00 53.73  ? 266 ILE   A CA  1 
ATOM   2001 C C   . ILE   A 1 266 ? 31.625 7.610   -5.816  1.00 55.62  ? 266 ILE   A C   1 
ATOM   2002 O O   . ILE   A 1 266 ? 31.753 8.510   -4.983  1.00 54.87  ? 266 ILE   A O   1 
ATOM   2003 C CB  . ILE   A 1 266 ? 31.752 8.501   -8.203  1.00 55.76  ? 266 ILE   A CB  1 
ATOM   2004 C CG1 . ILE   A 1 266 ? 30.963 9.237   -9.308  1.00 55.10  ? 266 ILE   A CG1 1 
ATOM   2005 C CG2 . ILE   A 1 266 ? 32.767 7.494   -8.778  1.00 56.95  ? 266 ILE   A CG2 1 
ATOM   2006 C CD1 . ILE   A 1 266 ? 30.070 8.467   -10.179 1.00 53.27  ? 266 ILE   A CD1 1 
ATOM   2007 N N   . TRP   A 1 267 ? 32.140 6.399   -5.661  1.00 51.02  ? 267 TRP   A N   1 
ATOM   2008 C CA  . TRP   A 1 267 ? 32.908 5.999   -4.497  1.00 50.14  ? 267 TRP   A CA  1 
ATOM   2009 C C   . TRP   A 1 267 ? 34.227 5.347   -4.942  1.00 53.12  ? 267 TRP   A C   1 
ATOM   2010 O O   . TRP   A 1 267 ? 34.224 4.272   -5.542  1.00 52.68  ? 267 TRP   A O   1 
ATOM   2011 C CB  . TRP   A 1 267 ? 32.037 5.070   -3.625  1.00 49.14  ? 267 TRP   A CB  1 
ATOM   2012 C CG  . TRP   A 1 267 ? 32.617 4.559   -2.330  1.00 50.41  ? 267 TRP   A CG  1 
ATOM   2013 C CD1 . TRP   A 1 267 ? 33.900 4.703   -1.867  1.00 53.30  ? 267 TRP   A CD1 1 
ATOM   2014 C CD2 . TRP   A 1 267 ? 31.933 3.754   -1.368  1.00 50.25  ? 267 TRP   A CD2 1 
ATOM   2015 N NE1 . TRP   A 1 267 ? 34.049 4.040   -0.673  1.00 52.24  ? 267 TRP   A NE1 1 
ATOM   2016 C CE2 . TRP   A 1 267 ? 32.856 3.449   -0.340  1.00 53.95  ? 267 TRP   A CE2 1 
ATOM   2017 C CE3 . TRP   A 1 267 ? 30.621 3.258   -1.271  1.00 51.65  ? 267 TRP   A CE3 1 
ATOM   2018 C CZ2 . TRP   A 1 267 ? 32.500 2.695   0.786   1.00 53.27  ? 267 TRP   A CZ2 1 
ATOM   2019 C CZ3 . TRP   A 1 267 ? 30.268 2.525   -0.151  1.00 53.23  ? 267 TRP   A CZ3 1 
ATOM   2020 C CH2 . TRP   A 1 267 ? 31.201 2.250   0.862   1.00 53.79  ? 267 TRP   A CH2 1 
ATOM   2021 N N   . ALA   A 1 268 ? 35.350 6.021   -4.662  1.00 50.31  ? 268 ALA   A N   1 
ATOM   2022 C CA  . ALA   A 1 268 ? 36.704 5.556   -4.952  1.00 50.36  ? 268 ALA   A CA  1 
ATOM   2023 C C   . ALA   A 1 268 ? 37.162 4.791   -3.694  1.00 56.31  ? 268 ALA   A C   1 
ATOM   2024 O O   . ALA   A 1 268 ? 37.423 5.373   -2.645  1.00 53.70  ? 268 ALA   A O   1 
ATOM   2025 C CB  . ALA   A 1 268 ? 37.617 6.736   -5.257  1.00 50.88  ? 268 ALA   A CB  1 
ATOM   2026 N N   . CYS   A 1 269 ? 37.195 3.467   -3.802  1.00 58.59  ? 269 CYS   A N   1 
ATOM   2027 C CA  . CYS   A 1 269 ? 37.526 2.567   -2.705  1.00 60.80  ? 269 CYS   A CA  1 
ATOM   2028 C C   . CYS   A 1 269 ? 38.964 2.053   -2.672  1.00 65.78  ? 269 CYS   A C   1 
ATOM   2029 O O   . CYS   A 1 269 ? 39.375 1.304   -3.557  1.00 65.96  ? 269 CYS   A O   1 
ATOM   2030 C CB  . CYS   A 1 269 ? 36.516 1.423   -2.667  1.00 62.44  ? 269 CYS   A CB  1 
ATOM   2031 S SG  . CYS   A 1 269 ? 36.669 0.337   -1.231  1.00 67.49  ? 269 CYS   A SG  1 
ATOM   2032 N N   . LYS   A 1 270 ? 39.721 2.452   -1.641  1.00 63.77  ? 270 LYS   A N   1 
ATOM   2033 C CA  . LYS   A 1 270 ? 41.100 1.998   -1.396  1.00 64.34  ? 270 LYS   A CA  1 
ATOM   2034 C C   . LYS   A 1 270 ? 40.990 1.027   -0.206  1.00 71.76  ? 270 LYS   A C   1 
ATOM   2035 O O   . LYS   A 1 270 ? 40.905 1.453   0.961   1.00 72.83  ? 270 LYS   A O   1 
ATOM   2036 C CB  . LYS   A 1 270 ? 42.068 3.181   -1.121  1.00 65.55  ? 270 LYS   A CB  1 
ATOM   2037 C CG  . LYS   A 1 270 ? 43.331 2.880   -0.274  1.00 71.50  ? 270 LYS   A CG  1 
ATOM   2038 C CD  . LYS   A 1 270 ? 44.295 1.853   -0.892  1.00 75.84  ? 270 LYS   A CD  1 
ATOM   2039 C CE  . LYS   A 1 270 ? 45.450 1.496   0.019   1.00 75.77  ? 270 LYS   A CE  1 
ATOM   2040 N NZ  . LYS   A 1 270 ? 45.064 0.588   1.143   1.00 76.13  ? 270 LYS   A NZ  1 
ATOM   2041 N N   . ASN   A 1 271 ? 40.938 -0.275  -0.515  1.00 67.73  ? 271 ASN   A N   1 
ATOM   2042 C CA  . ASN   A 1 271 ? 40.811 -1.315  0.505   1.00 87.75  ? 271 ASN   A CA  1 
ATOM   2043 C C   . ASN   A 1 271 ? 42.116 -2.078  0.705   1.00 123.77 ? 271 ASN   A C   1 
ATOM   2044 O O   . ASN   A 1 271 ? 42.961 -1.653  1.489   1.00 87.88  ? 271 ASN   A O   1 
ATOM   2045 C CB  . ASN   A 1 271 ? 39.666 -2.266  0.155   1.00 86.78  ? 271 ASN   A CB  1 
ATOM   2046 C CG  . ASN   A 1 271 ? 39.733 -2.869  -1.232  1.00 99.51  ? 271 ASN   A CG  1 
ATOM   2047 O OD1 . ASN   A 1 271 ? 40.468 -2.413  -2.127  1.00 90.15  ? 271 ASN   A OD1 1 
ATOM   2048 N ND2 . ASN   A 1 271 ? 38.950 -3.914  -1.440  1.00 89.42  ? 271 ASN   A ND2 1 
ATOM   2049 N N   . SER   A 1 287 ? 21.102 -9.473  -8.386  1.00 65.07  ? 287 SER   A N   1 
ATOM   2050 C CA  . SER   A 1 287 ? 21.460 -10.168 -9.627  1.00 64.48  ? 287 SER   A CA  1 
ATOM   2051 C C   . SER   A 1 287 ? 22.680 -9.549  -10.352 1.00 68.45  ? 287 SER   A C   1 
ATOM   2052 O O   . SER   A 1 287 ? 22.809 -8.316  -10.445 1.00 68.29  ? 287 SER   A O   1 
ATOM   2053 C CB  . SER   A 1 287 ? 20.257 -10.263 -10.572 1.00 65.51  ? 287 SER   A CB  1 
ATOM   2054 O OG  . SER   A 1 287 ? 20.569 -10.970 -11.764 1.00 67.72  ? 287 SER   A OG  1 
ATOM   2055 N N   . LEU   A 1 288 ? 23.556 -10.433 -10.881 1.00 63.50  ? 288 LEU   A N   1 
ATOM   2056 C CA  . LEU   A 1 288 ? 24.765 -10.082 -11.629 1.00 62.87  ? 288 LEU   A CA  1 
ATOM   2057 C C   . LEU   A 1 288 ? 24.428 -9.618  -13.055 1.00 63.45  ? 288 LEU   A C   1 
ATOM   2058 O O   . LEU   A 1 288 ? 25.228 -8.910  -13.690 1.00 62.93  ? 288 LEU   A O   1 
ATOM   2059 C CB  . LEU   A 1 288 ? 25.690 -11.294 -11.700 1.00 63.64  ? 288 LEU   A CB  1 
ATOM   2060 C CG  . LEU   A 1 288 ? 26.574 -11.547 -10.495 1.00 69.73  ? 288 LEU   A CG  1 
ATOM   2061 C CD1 . LEU   A 1 288 ? 27.313 -12.889 -10.645 1.00 69.59  ? 288 LEU   A CD1 1 
ATOM   2062 C CD2 . LEU   A 1 288 ? 27.566 -10.367 -10.267 1.00 73.36  ? 288 LEU   A CD2 1 
ATOM   2063 N N   . GLY   A 1 289 ? 23.243 -10.024 -13.529 1.00 56.59  ? 289 GLY   A N   1 
ATOM   2064 C CA  . GLY   A 1 289 ? 22.718 -9.673  -14.838 1.00 54.52  ? 289 GLY   A CA  1 
ATOM   2065 C C   . GLY   A 1 289 ? 22.415 -8.195  -14.959 1.00 53.53  ? 289 GLY   A C   1 
ATOM   2066 O O   . GLY   A 1 289 ? 22.168 -7.718  -16.071 1.00 52.33  ? 289 GLY   A O   1 
ATOM   2067 N N   . MET   A 1 290 ? 22.460 -7.459  -13.807 1.00 46.96  ? 290 MET   A N   1 
ATOM   2068 C CA  . MET   A 1 290 ? 22.191 -6.014  -13.688 1.00 45.39  ? 290 MET   A CA  1 
ATOM   2069 C C   . MET   A 1 290 ? 23.394 -5.217  -13.241 1.00 50.53  ? 290 MET   A C   1 
ATOM   2070 O O   . MET   A 1 290 ? 23.235 -4.169  -12.611 1.00 50.20  ? 290 MET   A O   1 
ATOM   2071 C CB  . MET   A 1 290 ? 20.984 -5.707  -12.754 1.00 46.63  ? 290 MET   A CB  1 
ATOM   2072 C CG  . MET   A 1 290 ? 19.765 -6.537  -13.026 1.00 48.60  ? 290 MET   A CG  1 
ATOM   2073 S SD  . MET   A 1 290 ? 19.012 -6.113  -14.592 1.00 51.08  ? 290 MET   A SD  1 
ATOM   2074 C CE  . MET   A 1 290 ? 17.927 -4.839  -14.063 1.00 47.83  ? 290 MET   A CE  1 
ATOM   2075 N N   . MET   A 1 291 ? 24.597 -5.693  -13.552 1.00 49.82  ? 291 MET   A N   1 
ATOM   2076 C CA  . MET   A 1 291 ? 25.796 -4.939  -13.208 1.00 50.19  ? 291 MET   A CA  1 
ATOM   2077 C C   . MET   A 1 291 ? 26.753 -4.767  -14.381 1.00 49.75  ? 291 MET   A C   1 
ATOM   2078 O O   . MET   A 1 291 ? 27.074 -5.715  -15.081 1.00 47.27  ? 291 MET   A O   1 
ATOM   2079 C CB  . MET   A 1 291 ? 26.494 -5.419  -11.930 1.00 53.56  ? 291 MET   A CB  1 
ATOM   2080 C CG  . MET   A 1 291 ? 27.449 -4.351  -11.388 1.00 58.90  ? 291 MET   A CG  1 
ATOM   2081 S SD  . MET   A 1 291 ? 27.752 -4.261  -9.611  1.00 64.70  ? 291 MET   A SD  1 
ATOM   2082 C CE  . MET   A 1 291 ? 26.117 -4.025  -9.007  1.00 61.14  ? 291 MET   A CE  1 
ATOM   2083 N N   . THR   A 1 292 ? 27.181 -3.541  -14.600 1.00 46.21  ? 292 THR   A N   1 
ATOM   2084 C CA  . THR   A 1 292 ? 28.110 -3.232  -15.665 1.00 45.64  ? 292 THR   A CA  1 
ATOM   2085 C C   . THR   A 1 292 ? 29.457 -2.881  -15.059 1.00 47.05  ? 292 THR   A C   1 
ATOM   2086 O O   . THR   A 1 292 ? 29.509 -2.392  -13.931 1.00 45.73  ? 292 THR   A O   1 
ATOM   2087 C CB  . THR   A 1 292 ? 27.482 -2.207  -16.623 1.00 57.77  ? 292 THR   A CB  1 
ATOM   2088 O OG1 . THR   A 1 292 ? 27.641 -2.656  -17.978 1.00 53.94  ? 292 THR   A OG1 1 
ATOM   2089 C CG2 . THR   A 1 292 ? 28.023 -0.790  -16.430 1.00 61.02  ? 292 THR   A CG2 1 
ATOM   2090 N N   . SER   A 1 293 ? 30.539 -3.177  -15.789 1.00 44.16  ? 293 SER   A N   1 
ATOM   2091 C CA  . SER   A 1 293 ? 31.923 -2.886  -15.409 1.00 44.92  ? 293 SER   A CA  1 
ATOM   2092 C C   . SER   A 1 293 ? 32.495 -1.979  -16.491 1.00 50.04  ? 293 SER   A C   1 
ATOM   2093 O O   . SER   A 1 293 ? 32.497 -2.350  -17.665 1.00 52.52  ? 293 SER   A O   1 
ATOM   2094 C CB  . SER   A 1 293 ? 32.743 -4.168  -15.339 1.00 50.20  ? 293 SER   A CB  1 
ATOM   2095 O OG  . SER   A 1 293 ? 33.334 -4.319  -14.061 1.00 63.30  ? 293 SER   A OG  1 
ATOM   2096 N N   . VAL   A 1 294 ? 32.952 -0.791  -16.113 1.00 44.26  ? 294 VAL   A N   1 
ATOM   2097 C CA  . VAL   A 1 294 ? 33.520 0.171   -17.047 1.00 42.88  ? 294 VAL   A CA  1 
ATOM   2098 C C   . VAL   A 1 294 ? 34.952 0.533   -16.634 1.00 44.19  ? 294 VAL   A C   1 
ATOM   2099 O O   . VAL   A 1 294 ? 35.178 0.966   -15.507 1.00 43.85  ? 294 VAL   A O   1 
ATOM   2100 C CB  . VAL   A 1 294 ? 32.587 1.415   -17.245 1.00 46.97  ? 294 VAL   A CB  1 
ATOM   2101 C CG1 . VAL   A 1 294 ? 33.232 2.480   -18.128 1.00 46.43  ? 294 VAL   A CG1 1 
ATOM   2102 C CG2 . VAL   A 1 294 ? 31.236 0.995   -17.833 1.00 47.18  ? 294 VAL   A CG2 1 
ATOM   2103 N N   . LEU   A 1 295 ? 35.910 0.330   -17.545 1.00 40.10  ? 295 LEU   A N   1 
ATOM   2104 C CA  . LEU   A 1 295 ? 37.309 0.671   -17.335 1.00 39.71  ? 295 LEU   A CA  1 
ATOM   2105 C C   . LEU   A 1 295 ? 37.466 2.081   -17.900 1.00 46.76  ? 295 LEU   A C   1 
ATOM   2106 O O   . LEU   A 1 295 ? 37.218 2.300   -19.087 1.00 48.30  ? 295 LEU   A O   1 
ATOM   2107 C CB  . LEU   A 1 295 ? 38.256 -0.318  -18.023 1.00 38.93  ? 295 LEU   A CB  1 
ATOM   2108 C CG  . LEU   A 1 295 ? 39.766 0.002   -17.957 1.00 42.67  ? 295 LEU   A CG  1 
ATOM   2109 C CD1 . LEU   A 1 295 ? 40.328 -0.219  -16.568 1.00 42.69  ? 295 LEU   A CD1 1 
ATOM   2110 C CD2 . LEU   A 1 295 ? 40.535 -0.880  -18.889 1.00 43.68  ? 295 LEU   A CD2 1 
ATOM   2111 N N   . VAL   A 1 296 ? 37.814 3.035   -17.029 1.00 42.71  ? 296 VAL   A N   1 
ATOM   2112 C CA  . VAL   A 1 296 ? 37.991 4.456   -17.342 1.00 41.92  ? 296 VAL   A CA  1 
ATOM   2113 C C   . VAL   A 1 296 ? 39.482 4.780   -17.251 1.00 44.44  ? 296 VAL   A C   1 
ATOM   2114 O O   . VAL   A 1 296 ? 40.062 4.693   -16.172 1.00 41.98  ? 296 VAL   A O   1 
ATOM   2115 C CB  . VAL   A 1 296 ? 37.156 5.337   -16.349 1.00 45.64  ? 296 VAL   A CB  1 
ATOM   2116 C CG1 . VAL   A 1 296 ? 37.369 6.826   -16.594 1.00 44.98  ? 296 VAL   A CG1 1 
ATOM   2117 C CG2 . VAL   A 1 296 ? 35.669 4.992   -16.403 1.00 45.57  ? 296 VAL   A CG2 1 
ATOM   2118 N N   . CYS   A 1 297 ? 40.093 5.159   -18.369 1.00 43.17  ? 297 CYS   A N   1 
ATOM   2119 C CA  . CYS   A 1 297 ? 41.509 5.530   -18.402 1.00 44.19  ? 297 CYS   A CA  1 
ATOM   2120 C C   . CYS   A 1 297 ? 41.709 6.943   -17.861 1.00 49.64  ? 297 CYS   A C   1 
ATOM   2121 O O   . CYS   A 1 297 ? 40.782 7.755   -17.962 1.00 49.01  ? 297 CYS   A O   1 
ATOM   2122 C CB  . CYS   A 1 297 ? 42.084 5.367   -19.801 1.00 44.96  ? 297 CYS   A CB  1 
ATOM   2123 S SG  . CYS   A 1 297 ? 42.112 3.651   -20.364 1.00 49.61  ? 297 CYS   A SG  1 
ATOM   2124 N N   . PRO   A 1 298 ? 42.883 7.256   -17.249 1.00 48.08  ? 298 PRO   A N   1 
ATOM   2125 C CA  . PRO   A 1 298 ? 43.073 8.612   -16.678 1.00 48.44  ? 298 PRO   A CA  1 
ATOM   2126 C C   . PRO   A 1 298 ? 42.924 9.804   -17.642 1.00 54.46  ? 298 PRO   A C   1 
ATOM   2127 O O   . PRO   A 1 298 ? 42.524 10.887  -17.189 1.00 54.80  ? 298 PRO   A O   1 
ATOM   2128 C CB  . PRO   A 1 298 ? 44.449 8.540   -15.992 1.00 49.44  ? 298 PRO   A CB  1 
ATOM   2129 C CG  . PRO   A 1 298 ? 45.122 7.359   -16.574 1.00 53.31  ? 298 PRO   A CG  1 
ATOM   2130 C CD  . PRO   A 1 298 ? 44.063 6.394   -17.003 1.00 49.03  ? 298 PRO   A CD  1 
ATOM   2131 N N   . ASP   A 1 299 ? 43.211 9.600   -18.964 1.00 51.12  ? 299 ASP   A N   1 
ATOM   2132 C CA  . ASP   A 1 299 ? 43.116 10.624  -20.032 1.00 50.76  ? 299 ASP   A CA  1 
ATOM   2133 C C   . ASP   A 1 299 ? 41.730 11.235  -20.181 1.00 55.34  ? 299 ASP   A C   1 
ATOM   2134 O O   . ASP   A 1 299 ? 41.606 12.352  -20.663 1.00 55.86  ? 299 ASP   A O   1 
ATOM   2135 C CB  . ASP   A 1 299 ? 43.589 10.068  -21.404 1.00 52.20  ? 299 ASP   A CB  1 
ATOM   2136 C CG  . ASP   A 1 299 ? 42.839 8.852   -21.991 1.00 60.01  ? 299 ASP   A CG  1 
ATOM   2137 O OD1 . ASP   A 1 299 ? 41.785 8.461   -21.431 1.00 56.89  ? 299 ASP   A OD1 1 
ATOM   2138 O OD2 . ASP   A 1 299 ? 43.309 8.298   -23.013 1.00 66.34  ? 299 ASP   A OD2 1 
ATOM   2139 N N   . GLY   A 1 300 ? 40.704 10.486  -19.792 1.00 52.10  ? 300 GLY   A N   1 
ATOM   2140 C CA  . GLY   A 1 300 ? 39.314 10.901  -19.917 1.00 51.28  ? 300 GLY   A CA  1 
ATOM   2141 C C   . GLY   A 1 300 ? 38.753 10.637  -21.304 1.00 53.18  ? 300 GLY   A C   1 
ATOM   2142 O O   . GLY   A 1 300 ? 37.574 10.907  -21.554 1.00 54.17  ? 300 GLY   A O   1 
ATOM   2143 N N   . LYS   A 1 301 ? 39.591 10.100  -22.214 1.00 46.52  ? 301 LYS   A N   1 
ATOM   2144 C CA  . LYS   A 1 301 ? 39.231 9.792   -23.598 1.00 45.44  ? 301 LYS   A CA  1 
ATOM   2145 C C   . LYS   A 1 301 ? 38.948 8.303   -23.848 1.00 47.47  ? 301 LYS   A C   1 
ATOM   2146 O O   . LYS   A 1 301 ? 38.007 7.985   -24.555 1.00 45.20  ? 301 LYS   A O   1 
ATOM   2147 C CB  . LYS   A 1 301 ? 40.305 10.332  -24.565 1.00 46.73  ? 301 LYS   A CB  1 
ATOM   2148 N N   . THR   A 1 302 ? 39.759 7.397   -23.271 1.00 45.30  ? 302 THR   A N   1 
ATOM   2149 C CA  . THR   A 1 302 ? 39.622 5.946   -23.450 1.00 44.70  ? 302 THR   A CA  1 
ATOM   2150 C C   . THR   A 1 302 ? 38.750 5.307   -22.389 1.00 48.95  ? 302 THR   A C   1 
ATOM   2151 O O   . THR   A 1 302 ? 38.946 5.558   -21.204 1.00 49.84  ? 302 THR   A O   1 
ATOM   2152 C CB  . THR   A 1 302 ? 40.983 5.298   -23.627 1.00 44.30  ? 302 THR   A CB  1 
ATOM   2153 O OG1 . THR   A 1 302 ? 41.707 6.032   -24.621 1.00 46.74  ? 302 THR   A OG1 1 
ATOM   2154 C CG2 . THR   A 1 302 ? 40.878 3.868   -24.047 1.00 39.16  ? 302 THR   A CG2 1 
ATOM   2155 N N   . VAL   A 1 303 ? 37.771 4.492   -22.833 1.00 43.99  ? 303 VAL   A N   1 
ATOM   2156 C CA  . VAL   A 1 303 ? 36.785 3.785   -22.007 1.00 42.71  ? 303 VAL   A CA  1 
ATOM   2157 C C   . VAL   A 1 303 ? 36.510 2.418   -22.620 1.00 45.80  ? 303 VAL   A C   1 
ATOM   2158 O O   . VAL   A 1 303 ? 36.339 2.311   -23.846 1.00 45.99  ? 303 VAL   A O   1 
ATOM   2159 C CB  . VAL   A 1 303 ? 35.477 4.628   -21.909 1.00 45.82  ? 303 VAL   A CB  1 
ATOM   2160 C CG1 . VAL   A 1 303 ? 34.223 3.772   -21.716 1.00 45.32  ? 303 VAL   A CG1 1 
ATOM   2161 C CG2 . VAL   A 1 303 ? 35.579 5.723   -20.846 1.00 45.10  ? 303 VAL   A CG2 1 
ATOM   2162 N N   . GLU   A 1 304 ? 36.435 1.384   -21.758 1.00 39.55  ? 304 GLU   A N   1 
ATOM   2163 C CA  . GLU   A 1 304 ? 36.112 0.006   -22.131 1.00 37.73  ? 304 GLU   A CA  1 
ATOM   2164 C C   . GLU   A 1 304 ? 34.953 -0.491  -21.254 1.00 40.39  ? 304 GLU   A C   1 
ATOM   2165 O O   . GLU   A 1 304 ? 35.047 -0.441  -20.028 1.00 39.18  ? 304 GLU   A O   1 
ATOM   2166 C CB  . GLU   A 1 304 ? 37.320 -0.911  -22.000 1.00 38.67  ? 304 GLU   A CB  1 
ATOM   2167 C CG  . GLU   A 1 304 ? 37.073 -2.239  -22.680 1.00 50.77  ? 304 GLU   A CG  1 
ATOM   2168 C CD  . GLU   A 1 304 ? 37.474 -3.468  -21.896 1.00 70.88  ? 304 GLU   A CD  1 
ATOM   2169 O OE1 . GLU   A 1 304 ? 38.034 -3.334  -20.784 1.00 63.83  ? 304 GLU   A OE1 1 
ATOM   2170 O OE2 . GLU   A 1 304 ? 37.225 -4.579  -22.409 1.00 68.86  ? 304 GLU   A OE2 1 
ATOM   2171 N N   . ALA   A 1 305 ? 33.859 -0.955  -21.877 1.00 36.28  ? 305 ALA   A N   1 
ATOM   2172 C CA  . ALA   A 1 305 ? 32.705 -1.415  -21.114 1.00 35.37  ? 305 ALA   A CA  1 
ATOM   2173 C C   . ALA   A 1 305 ? 32.393 -2.881  -21.294 1.00 41.00  ? 305 ALA   A C   1 
ATOM   2174 O O   . ALA   A 1 305 ? 32.577 -3.442  -22.378 1.00 41.87  ? 305 ALA   A O   1 
ATOM   2175 C CB  . ALA   A 1 305 ? 31.477 -0.566  -21.421 1.00 35.48  ? 305 ALA   A CB  1 
ATOM   2176 N N   . GLU   A 1 306 ? 31.934 -3.505  -20.203 1.00 37.24  ? 306 GLU   A N   1 
ATOM   2177 C CA  . GLU   A 1 306 ? 31.520 -4.906  -20.167 1.00 36.82  ? 306 GLU   A CA  1 
ATOM   2178 C C   . GLU   A 1 306 ? 30.569 -5.182  -19.017 1.00 39.21  ? 306 GLU   A C   1 
ATOM   2179 O O   . GLU   A 1 306 ? 30.400 -4.335  -18.139 1.00 39.54  ? 306 GLU   A O   1 
ATOM   2180 C CB  . GLU   A 1 306 ? 32.699 -5.881  -20.185 1.00 38.00  ? 306 GLU   A CB  1 
ATOM   2181 C CG  . GLU   A 1 306 ? 33.709 -5.710  -19.079 1.00 53.21  ? 306 GLU   A CG  1 
ATOM   2182 C CD  . GLU   A 1 306 ? 34.888 -6.646  -19.240 1.00 81.04  ? 306 GLU   A CD  1 
ATOM   2183 O OE1 . GLU   A 1 306 ? 34.672 -7.868  -19.452 1.00 74.79  ? 306 GLU   A OE1 1 
ATOM   2184 O OE2 . GLU   A 1 306 ? 36.034 -6.146  -19.164 1.00 72.99  ? 306 GLU   A OE2 1 
ATOM   2185 N N   . ALA   A 1 307 ? 29.926 -6.350  -19.048 1.00 33.76  ? 307 ALA   A N   1 
ATOM   2186 C CA  . ALA   A 1 307 ? 29.015 -6.820  -18.015 1.00 32.66  ? 307 ALA   A CA  1 
ATOM   2187 C C   . ALA   A 1 307 ? 29.887 -7.253  -16.838 1.00 38.59  ? 307 ALA   A C   1 
ATOM   2188 O O   . ALA   A 1 307 ? 30.980 -7.802  -17.035 1.00 38.06  ? 307 ALA   A O   1 
ATOM   2189 C CB  . ALA   A 1 307 ? 28.223 -8.013  -18.534 1.00 32.79  ? 307 ALA   A CB  1 
ATOM   2190 N N   . ALA   A 1 308 ? 29.422 -7.001  -15.626 1.00 37.44  ? 308 ALA   A N   1 
ATOM   2191 C CA  . ALA   A 1 308 ? 30.155 -7.393  -14.429 1.00 39.69  ? 308 ALA   A CA  1 
ATOM   2192 C C   . ALA   A 1 308 ? 29.700 -8.810  -14.029 1.00 47.26  ? 308 ALA   A C   1 
ATOM   2193 O O   . ALA   A 1 308 ? 29.149 -9.004  -12.947 1.00 51.16  ? 308 ALA   A O   1 
ATOM   2194 C CB  . ALA   A 1 308 ? 29.881 -6.396  -13.298 1.00 40.54  ? 308 ALA   A CB  1 
ATOM   2195 N N   . HIS   A 1 309 ? 29.886 -9.780  -14.925 1.00 40.98  ? 309 HIS   A N   1 
ATOM   2196 C CA  . HIS   A 1 309 ? 29.509 -11.184 -14.763 1.00 39.58  ? 309 HIS   A CA  1 
ATOM   2197 C C   . HIS   A 1 309 ? 30.218 -12.033 -15.815 1.00 44.19  ? 309 HIS   A C   1 
ATOM   2198 O O   . HIS   A 1 309 ? 30.797 -11.486 -16.760 1.00 46.08  ? 309 HIS   A O   1 
ATOM   2199 C CB  . HIS   A 1 309 ? 27.976 -11.400 -14.747 1.00 39.18  ? 309 HIS   A CB  1 
ATOM   2200 C CG  . HIS   A 1 309 ? 27.250 -11.179 -16.048 1.00 41.80  ? 309 HIS   A CG  1 
ATOM   2201 N ND1 . HIS   A 1 309 ? 27.461 -11.996 -17.155 1.00 42.89  ? 309 HIS   A ND1 1 
ATOM   2202 C CD2 . HIS   A 1 309 ? 26.267 -10.297 -16.348 1.00 41.59  ? 309 HIS   A CD2 1 
ATOM   2203 C CE1 . HIS   A 1 309 ? 26.625 -11.564 -18.085 1.00 40.73  ? 309 HIS   A CE1 1 
ATOM   2204 N NE2 . HIS   A 1 309 ? 25.891 -10.546 -17.646 1.00 40.85  ? 309 HIS   A NE2 1 
ATOM   2205 N N   . GLY   A 1 310 ? 30.216 -13.344 -15.622 1.00 38.05  ? 310 GLY   A N   1 
ATOM   2206 C CA  . GLY   A 1 310 ? 30.878 -14.263 -16.536 1.00 37.28  ? 310 GLY   A CA  1 
ATOM   2207 C C   . GLY   A 1 310 ? 30.084 -14.696 -17.747 1.00 40.47  ? 310 GLY   A C   1 
ATOM   2208 O O   . GLY   A 1 310 ? 29.078 -14.076 -18.112 1.00 38.44  ? 310 GLY   A O   1 
ATOM   2209 N N   . THR   A 1 311 ? 30.544 -15.795 -18.358 1.00 38.47  ? 311 THR   A N   1 
ATOM   2210 C CA  . THR   A 1 311 ? 29.993 -16.409 -19.568 1.00 38.51  ? 311 THR   A CA  1 
ATOM   2211 C C   . THR   A 1 311 ? 28.693 -17.207 -19.407 1.00 43.68  ? 311 THR   A C   1 
ATOM   2212 O O   . THR   A 1 311 ? 28.084 -17.603 -20.415 1.00 44.83  ? 311 THR   A O   1 
ATOM   2213 C CB  . THR   A 1 311 ? 31.080 -17.158 -20.310 1.00 45.41  ? 311 THR   A CB  1 
ATOM   2214 O OG1 . THR   A 1 311 ? 31.416 -18.336 -19.577 1.00 48.29  ? 311 THR   A OG1 1 
ATOM   2215 C CG2 . THR   A 1 311 ? 32.313 -16.306 -20.531 1.00 41.34  ? 311 THR   A CG2 1 
ATOM   2216 N N   . VAL   A 1 312 ? 28.256 -17.417 -18.151 1.00 39.84  ? 312 VAL   A N   1 
ATOM   2217 C CA  . VAL   A 1 312 ? 27.023 -18.145 -17.772 1.00 39.55  ? 312 VAL   A CA  1 
ATOM   2218 C C   . VAL   A 1 312 ? 27.008 -19.586 -18.311 1.00 43.28  ? 312 VAL   A C   1 
ATOM   2219 O O   . VAL   A 1 312 ? 26.062 -20.006 -18.999 1.00 42.19  ? 312 VAL   A O   1 
ATOM   2220 C CB  . VAL   A 1 312 ? 25.685 -17.346 -17.992 1.00 42.78  ? 312 VAL   A CB  1 
ATOM   2221 C CG1 . VAL   A 1 312 ? 24.633 -17.752 -16.965 1.00 42.71  ? 312 VAL   A CG1 1 
ATOM   2222 C CG2 . VAL   A 1 312 ? 25.901 -15.831 -17.943 1.00 41.78  ? 312 VAL   A CG2 1 
ATOM   2223 N N   . THR   A 1 313 ? 28.091 -20.331 -17.993 1.00 42.02  ? 313 THR   A N   1 
ATOM   2224 C CA  . THR   A 1 313 ? 28.311 -21.738 -18.382 1.00 43.16  ? 313 THR   A CA  1 
ATOM   2225 C C   . THR   A 1 313 ? 27.061 -22.617 -18.170 1.00 50.43  ? 313 THR   A C   1 
ATOM   2226 O O   . THR   A 1 313 ? 26.659 -23.350 -19.094 1.00 52.00  ? 313 THR   A O   1 
ATOM   2227 C CB  . THR   A 1 313 ? 29.561 -22.334 -17.691 1.00 47.74  ? 313 THR   A CB  1 
ATOM   2228 O OG1 . THR   A 1 313 ? 30.642 -21.400 -17.741 1.00 50.89  ? 313 THR   A OG1 1 
ATOM   2229 C CG2 . THR   A 1 313 ? 30.020 -23.627 -18.338 1.00 44.92  ? 313 THR   A CG2 1 
ATOM   2230 N N   . ARG   A 1 314 ? 26.449 -22.525 -16.969 1.00 46.47  ? 314 ARG   A N   1 
ATOM   2231 C CA  . ARG   A 1 314 ? 25.267 -23.293 -16.585 1.00 47.07  ? 314 ARG   A CA  1 
ATOM   2232 C C   . ARG   A 1 314 ? 24.153 -23.201 -17.625 1.00 51.39  ? 314 ARG   A C   1 
ATOM   2233 O O   . ARG   A 1 314 ? 23.674 -24.244 -18.071 1.00 51.94  ? 314 ARG   A O   1 
ATOM   2234 C CB  . ARG   A 1 314 ? 24.784 -22.926 -15.162 1.00 49.32  ? 314 ARG   A CB  1 
ATOM   2235 N N   . HIS   A 1 315 ? 23.782 -21.971 -18.046 1.00 47.78  ? 315 HIS   A N   1 
ATOM   2236 C CA  . HIS   A 1 315 ? 22.743 -21.750 -19.056 1.00 47.73  ? 315 HIS   A CA  1 
ATOM   2237 C C   . HIS   A 1 315 ? 23.203 -22.232 -20.419 1.00 51.06  ? 315 HIS   A C   1 
ATOM   2238 O O   . HIS   A 1 315 ? 22.390 -22.756 -21.175 1.00 51.32  ? 315 HIS   A O   1 
ATOM   2239 C CB  . HIS   A 1 315 ? 22.325 -20.269 -19.136 1.00 49.06  ? 315 HIS   A CB  1 
ATOM   2240 C CG  . HIS   A 1 315 ? 21.663 -19.709 -17.904 1.00 52.83  ? 315 HIS   A CG  1 
ATOM   2241 N ND1 . HIS   A 1 315 ? 20.967 -18.511 -17.949 1.00 54.52  ? 315 HIS   A ND1 1 
ATOM   2242 C CD2 . HIS   A 1 315 ? 21.620 -20.184 -16.633 1.00 54.19  ? 315 HIS   A CD2 1 
ATOM   2243 C CE1 . HIS   A 1 315 ? 20.530 -18.298 -16.717 1.00 53.42  ? 315 HIS   A CE1 1 
ATOM   2244 N NE2 . HIS   A 1 315 ? 20.896 -19.277 -15.893 1.00 53.70  ? 315 HIS   A NE2 1 
ATOM   2245 N N   . TYR   A 1 316 ? 24.508 -22.056 -20.742 1.00 46.88  ? 316 TYR   A N   1 
ATOM   2246 C CA  . TYR   A 1 316 ? 25.078 -22.482 -22.022 1.00 45.68  ? 316 TYR   A CA  1 
ATOM   2247 C C   . TYR   A 1 316 ? 24.934 -23.995 -22.254 1.00 48.43  ? 316 TYR   A C   1 
ATOM   2248 O O   . TYR   A 1 316 ? 24.555 -24.392 -23.360 1.00 46.71  ? 316 TYR   A O   1 
ATOM   2249 C CB  . TYR   A 1 316 ? 26.534 -22.015 -22.167 1.00 46.31  ? 316 TYR   A CB  1 
ATOM   2250 C CG  . TYR   A 1 316 ? 27.155 -22.359 -23.502 1.00 46.43  ? 316 TYR   A CG  1 
ATOM   2251 C CD1 . TYR   A 1 316 ? 26.594 -21.906 -24.693 1.00 47.71  ? 316 TYR   A CD1 1 
ATOM   2252 C CD2 . TYR   A 1 316 ? 28.307 -23.136 -23.578 1.00 47.50  ? 316 TYR   A CD2 1 
ATOM   2253 C CE1 . TYR   A 1 316 ? 27.165 -22.219 -25.928 1.00 48.33  ? 316 TYR   A CE1 1 
ATOM   2254 C CE2 . TYR   A 1 316 ? 28.898 -23.443 -24.809 1.00 48.19  ? 316 TYR   A CE2 1 
ATOM   2255 C CZ  . TYR   A 1 316 ? 28.319 -22.986 -25.980 1.00 53.24  ? 316 TYR   A CZ  1 
ATOM   2256 O OH  . TYR   A 1 316 ? 28.891 -23.291 -27.188 1.00 54.09  ? 316 TYR   A OH  1 
ATOM   2257 N N   . ARG   A 1 317 ? 25.198 -24.833 -21.211 1.00 45.39  ? 317 ARG   A N   1 
ATOM   2258 C CA  . ARG   A 1 317 ? 25.047 -26.303 -21.293 1.00 45.13  ? 317 ARG   A CA  1 
ATOM   2259 C C   . ARG   A 1 317 ? 23.623 -26.693 -21.653 1.00 51.98  ? 317 ARG   A C   1 
ATOM   2260 O O   . ARG   A 1 317 ? 23.435 -27.603 -22.468 1.00 52.61  ? 317 ARG   A O   1 
ATOM   2261 C CB  . ARG   A 1 317 ? 25.458 -27.002 -19.998 1.00 42.98  ? 317 ARG   A CB  1 
ATOM   2262 C CG  . ARG   A 1 317 ? 26.882 -26.745 -19.539 1.00 45.67  ? 317 ARG   A CG  1 
ATOM   2263 C CD  . ARG   A 1 317 ? 27.902 -27.030 -20.622 1.00 50.54  ? 317 ARG   A CD  1 
ATOM   2264 N NE  . ARG   A 1 317 ? 29.254 -26.828 -20.109 1.00 58.23  ? 317 ARG   A NE  1 
ATOM   2265 C CZ  . ARG   A 1 317 ? 30.311 -26.585 -20.868 1.00 60.95  ? 317 ARG   A CZ  1 
ATOM   2266 N NH1 . ARG   A 1 317 ? 30.183 -26.501 -22.185 1.00 42.92  ? 317 ARG   A NH1 1 
ATOM   2267 N NH2 . ARG   A 1 317 ? 31.505 -26.417 -20.316 1.00 45.95  ? 317 ARG   A NH2 1 
ATOM   2268 N N   . MET   A 1 318 ? 22.619 -25.970 -21.087 1.00 49.87  ? 318 MET   A N   1 
ATOM   2269 C CA  . MET   A 1 318 ? 21.199 -26.176 -21.380 1.00 50.20  ? 318 MET   A CA  1 
ATOM   2270 C C   . MET   A 1 318 ? 20.940 -25.840 -22.845 1.00 55.23  ? 318 MET   A C   1 
ATOM   2271 O O   . MET   A 1 318 ? 20.298 -26.632 -23.545 1.00 54.84  ? 318 MET   A O   1 
ATOM   2272 C CB  . MET   A 1 318 ? 20.308 -25.326 -20.475 1.00 52.84  ? 318 MET   A CB  1 
ATOM   2273 C CG  . MET   A 1 318 ? 20.503 -25.596 -19.022 1.00 57.76  ? 318 MET   A CG  1 
ATOM   2274 S SD  . MET   A 1 318 ? 19.263 -24.689 -18.090 1.00 64.08  ? 318 MET   A SD  1 
ATOM   2275 C CE  . MET   A 1 318 ? 20.140 -24.441 -16.551 1.00 60.49  ? 318 MET   A CE  1 
ATOM   2276 N N   . TYR   A 1 319 ? 21.478 -24.685 -23.322 1.00 52.20  ? 319 TYR   A N   1 
ATOM   2277 C CA  . TYR   A 1 319 ? 21.349 -24.246 -24.716 1.00 52.51  ? 319 TYR   A CA  1 
ATOM   2278 C C   . TYR   A 1 319 ? 21.979 -25.285 -25.663 1.00 59.22  ? 319 TYR   A C   1 
ATOM   2279 O O   . TYR   A 1 319 ? 21.460 -25.516 -26.761 1.00 59.42  ? 319 TYR   A O   1 
ATOM   2280 C CB  . TYR   A 1 319 ? 21.999 -22.864 -24.897 1.00 53.16  ? 319 TYR   A CB  1 
ATOM   2281 C CG  . TYR   A 1 319 ? 21.972 -22.326 -26.313 1.00 53.30  ? 319 TYR   A CG  1 
ATOM   2282 C CD1 . TYR   A 1 319 ? 20.933 -21.508 -26.751 1.00 54.58  ? 319 TYR   A CD1 1 
ATOM   2283 C CD2 . TYR   A 1 319 ? 23.016 -22.588 -27.200 1.00 53.51  ? 319 TYR   A CD2 1 
ATOM   2284 C CE1 . TYR   A 1 319 ? 20.927 -20.972 -28.040 1.00 54.17  ? 319 TYR   A CE1 1 
ATOM   2285 C CE2 . TYR   A 1 319 ? 23.006 -22.083 -28.499 1.00 53.96  ? 319 TYR   A CE2 1 
ATOM   2286 C CZ  . TYR   A 1 319 ? 21.968 -21.264 -28.909 1.00 62.43  ? 319 TYR   A CZ  1 
ATOM   2287 O OH  . TYR   A 1 319 ? 21.969 -20.764 -30.189 1.00 68.02  ? 319 TYR   A OH  1 
ATOM   2288 N N   . GLN   A 1 320 ? 23.098 -25.905 -25.223 1.00 56.80  ? 320 GLN   A N   1 
ATOM   2289 C CA  . GLN   A 1 320 ? 23.825 -26.940 -25.967 1.00 56.64  ? 320 GLN   A CA  1 
ATOM   2290 C C   . GLN   A 1 320 ? 22.956 -28.193 -26.111 1.00 61.75  ? 320 GLN   A C   1 
ATOM   2291 O O   . GLN   A 1 320 ? 22.974 -28.822 -27.168 1.00 61.40  ? 320 GLN   A O   1 
ATOM   2292 C CB  . GLN   A 1 320 ? 25.172 -27.269 -25.297 1.00 57.41  ? 320 GLN   A CB  1 
ATOM   2293 C CG  . GLN   A 1 320 ? 26.228 -26.184 -25.493 1.00 54.94  ? 320 GLN   A CG  1 
ATOM   2294 C CD  . GLN   A 1 320 ? 27.632 -26.699 -25.302 1.00 62.26  ? 320 GLN   A CD  1 
ATOM   2295 O OE1 . GLN   A 1 320 ? 28.106 -26.915 -24.175 1.00 48.65  ? 320 GLN   A OE1 1 
ATOM   2296 N NE2 . GLN   A 1 320 ? 28.337 -26.892 -26.414 1.00 57.24  ? 320 GLN   A NE2 1 
ATOM   2297 N N   . LYS   A 1 321 ? 22.166 -28.523 -25.059 1.00 58.20  ? 321 LYS   A N   1 
ATOM   2298 C CA  . LYS   A 1 321 ? 21.239 -29.666 -25.024 1.00 57.14  ? 321 LYS   A CA  1 
ATOM   2299 C C   . LYS   A 1 321 ? 19.856 -29.280 -25.595 1.00 61.67  ? 321 LYS   A C   1 
ATOM   2300 O O   . LYS   A 1 321 ? 18.894 -30.022 -25.406 1.00 61.55  ? 321 LYS   A O   1 
ATOM   2301 C CB  . LYS   A 1 321 ? 21.088 -30.203 -23.585 1.00 58.44  ? 321 LYS   A CB  1 
ATOM   2302 C CG  . LYS   A 1 321 ? 22.366 -30.798 -23.001 1.00 67.30  ? 321 LYS   A CG  1 
ATOM   2303 C CD  . LYS   A 1 321 ? 22.274 -30.959 -21.486 1.00 73.88  ? 321 LYS   A CD  1 
ATOM   2304 C CE  . LYS   A 1 321 ? 23.629 -31.195 -20.855 1.00 83.33  ? 321 LYS   A CE  1 
ATOM   2305 N NZ  . LYS   A 1 321 ? 23.631 -30.865 -19.400 1.00 91.66  ? 321 LYS   A NZ  1 
ATOM   2306 N N   . GLY   A 1 322 ? 19.770 -28.130 -26.278 1.00 58.49  ? 322 GLY   A N   1 
ATOM   2307 C CA  . GLY   A 1 322 ? 18.535 -27.616 -26.881 1.00 57.80  ? 322 GLY   A CA  1 
ATOM   2308 C C   . GLY   A 1 322 ? 17.431 -27.209 -25.911 1.00 59.39  ? 322 GLY   A C   1 
ATOM   2309 O O   . GLY   A 1 322 ? 16.302 -26.968 -26.344 1.00 59.08  ? 322 GLY   A O   1 
ATOM   2310 N N   . GLN   A 1 323 ? 17.750 -27.129 -24.594 1.00 54.08  ? 323 GLN   A N   1 
ATOM   2311 C CA  . GLN   A 1 323 ? 16.852 -26.759 -23.487 1.00 53.11  ? 323 GLN   A CA  1 
ATOM   2312 C C   . GLN   A 1 323 ? 16.589 -25.239 -23.422 1.00 57.57  ? 323 GLN   A C   1 
ATOM   2313 O O   . GLN   A 1 323 ? 17.450 -24.438 -23.796 1.00 57.57  ? 323 GLN   A O   1 
ATOM   2314 C CB  . GLN   A 1 323 ? 17.434 -27.236 -22.132 1.00 53.75  ? 323 GLN   A CB  1 
ATOM   2315 C CG  . GLN   A 1 323 ? 17.613 -28.763 -21.987 1.00 50.72  ? 323 GLN   A CG  1 
ATOM   2316 C CD  . GLN   A 1 323 ? 18.284 -29.183 -20.685 1.00 77.51  ? 323 GLN   A CD  1 
ATOM   2317 O OE1 . GLN   A 1 323 ? 18.177 -28.532 -19.632 1.00 71.32  ? 323 GLN   A OE1 1 
ATOM   2318 N NE2 . GLN   A 1 323 ? 18.993 -30.302 -20.721 1.00 76.77  ? 323 GLN   A NE2 1 
ATOM   2319 N N   . GLU   A 1 324 ? 15.396 -24.853 -22.931 1.00 53.94  ? 324 GLU   A N   1 
ATOM   2320 C CA  . GLU   A 1 324 ? 14.955 -23.459 -22.779 1.00 52.39  ? 324 GLU   A CA  1 
ATOM   2321 C C   . GLU   A 1 324 ? 15.814 -22.736 -21.741 1.00 55.12  ? 324 GLU   A C   1 
ATOM   2322 O O   . GLU   A 1 324 ? 16.028 -23.259 -20.648 1.00 55.71  ? 324 GLU   A O   1 
ATOM   2323 C CB  . GLU   A 1 324 ? 13.460 -23.405 -22.395 1.00 53.20  ? 324 GLU   A CB  1 
ATOM   2324 C CG  . GLU   A 1 324 ? 12.909 -22.003 -22.204 1.00 59.98  ? 324 GLU   A CG  1 
ATOM   2325 C CD  . GLU   A 1 324 ? 11.430 -21.896 -21.895 1.00 68.42  ? 324 GLU   A CD  1 
ATOM   2326 O OE1 . GLU   A 1 324 ? 11.028 -22.268 -20.770 1.00 68.35  ? 324 GLU   A OE1 1 
ATOM   2327 O OE2 . GLU   A 1 324 ? 10.673 -21.423 -22.774 1.00 50.54  ? 324 GLU   A OE2 1 
ATOM   2328 N N   . THR   A 1 325 ? 16.314 -21.537 -22.089 1.00 49.86  ? 325 THR   A N   1 
ATOM   2329 C CA  . THR   A 1 325 ? 17.147 -20.724 -21.186 1.00 48.04  ? 325 THR   A CA  1 
ATOM   2330 C C   . THR   A 1 325 ? 16.517 -19.362 -20.937 1.00 47.77  ? 325 THR   A C   1 
ATOM   2331 O O   . THR   A 1 325 ? 15.740 -18.894 -21.757 1.00 46.78  ? 325 THR   A O   1 
ATOM   2332 C CB  . THR   A 1 325 ? 18.571 -20.566 -21.732 1.00 54.60  ? 325 THR   A CB  1 
ATOM   2333 O OG1 . THR   A 1 325 ? 18.512 -20.029 -23.051 1.00 54.46  ? 325 THR   A OG1 1 
ATOM   2334 C CG2 . THR   A 1 325 ? 19.341 -21.866 -21.732 1.00 53.68  ? 325 THR   A CG2 1 
ATOM   2335 N N   . SER   A 1 326 ? 16.848 -18.726 -19.812 1.00 42.60  ? 326 SER   A N   1 
ATOM   2336 C CA  . SER   A 1 326 ? 16.345 -17.396 -19.492 1.00 41.64  ? 326 SER   A CA  1 
ATOM   2337 C C   . SER   A 1 326 ? 17.508 -16.609 -18.936 1.00 46.28  ? 326 SER   A C   1 
ATOM   2338 O O   . SER   A 1 326 ? 17.679 -16.529 -17.719 1.00 47.48  ? 326 SER   A O   1 
ATOM   2339 C CB  . SER   A 1 326 ? 15.179 -17.456 -18.514 1.00 42.55  ? 326 SER   A CB  1 
ATOM   2340 O OG  . SER   A 1 326 ? 14.570 -16.178 -18.458 1.00 44.24  ? 326 SER   A OG  1 
ATOM   2341 N N   . THR   A 1 327 ? 18.346 -16.072 -19.841 1.00 41.89  ? 327 THR   A N   1 
ATOM   2342 C CA  . THR   A 1 327 ? 19.544 -15.315 -19.475 1.00 41.66  ? 327 THR   A CA  1 
ATOM   2343 C C   . THR   A 1 327 ? 19.278 -13.815 -19.560 1.00 46.04  ? 327 THR   A C   1 
ATOM   2344 O O   . THR   A 1 327 ? 18.660 -13.349 -20.528 1.00 44.62  ? 327 THR   A O   1 
ATOM   2345 C CB  . THR   A 1 327 ? 20.759 -15.779 -20.302 1.00 50.85  ? 327 THR   A CB  1 
ATOM   2346 O OG1 . THR   A 1 327 ? 20.739 -17.204 -20.416 1.00 52.82  ? 327 THR   A OG1 1 
ATOM   2347 C CG2 . THR   A 1 327 ? 22.086 -15.345 -19.695 1.00 48.58  ? 327 THR   A CG2 1 
ATOM   2348 N N   . ASN   A 1 328 ? 19.729 -13.067 -18.521 1.00 42.81  ? 328 ASN   A N   1 
ATOM   2349 C CA  . ASN   A 1 328 ? 19.549 -11.624 -18.454 1.00 42.60  ? 328 ASN   A CA  1 
ATOM   2350 C C   . ASN   A 1 328 ? 20.566 -10.878 -19.376 1.00 47.33  ? 328 ASN   A C   1 
ATOM   2351 O O   . ASN   A 1 328 ? 21.775 -10.914 -19.125 1.00 46.83  ? 328 ASN   A O   1 
ATOM   2352 C CB  . ASN   A 1 328 ? 19.609 -11.133 -17.006 1.00 38.22  ? 328 ASN   A CB  1 
ATOM   2353 C CG  . ASN   A 1 328 ? 19.038 -9.745  -16.768 1.00 45.17  ? 328 ASN   A CG  1 
ATOM   2354 O OD1 . ASN   A 1 328 ? 18.843 -9.321  -15.635 1.00 46.10  ? 328 ASN   A OD1 1 
ATOM   2355 N ND2 . ASN   A 1 328 ? 18.757 -8.993  -17.804 1.00 32.01  ? 328 ASN   A ND2 1 
ATOM   2356 N N   . PRO   A 1 329 ? 20.090 -10.195 -20.440 1.00 43.56  ? 329 PRO   A N   1 
ATOM   2357 C CA  . PRO   A 1 329 ? 21.025 -9.485  -21.331 1.00 43.24  ? 329 PRO   A CA  1 
ATOM   2358 C C   . PRO   A 1 329 ? 21.316 -8.024  -20.931 1.00 44.84  ? 329 PRO   A C   1 
ATOM   2359 O O   . PRO   A 1 329 ? 22.086 -7.374  -21.628 1.00 44.79  ? 329 PRO   A O   1 
ATOM   2360 C CB  . PRO   A 1 329 ? 20.291 -9.526  -22.677 1.00 44.88  ? 329 PRO   A CB  1 
ATOM   2361 C CG  . PRO   A 1 329 ? 18.838 -9.437  -22.294 1.00 49.08  ? 329 PRO   A CG  1 
ATOM   2362 C CD  . PRO   A 1 329 ? 18.693 -10.046 -20.908 1.00 44.64  ? 329 PRO   A CD  1 
ATOM   2363 N N   . ILE   A 1 330 ? 20.701 -7.508  -19.843 1.00 39.74  ? 330 ILE   A N   1 
ATOM   2364 C CA  . ILE   A 1 330 ? 20.853 -6.112  -19.399 1.00 39.24  ? 330 ILE   A CA  1 
ATOM   2365 C C   . ILE   A 1 330 ? 22.270 -5.628  -19.281 1.00 43.48  ? 330 ILE   A C   1 
ATOM   2366 O O   . ILE   A 1 330 ? 22.621 -4.658  -19.953 1.00 44.04  ? 330 ILE   A O   1 
ATOM   2367 C CB  . ILE   A 1 330 ? 19.896 -5.648  -18.237 1.00 41.55  ? 330 ILE   A CB  1 
ATOM   2368 C CG1 . ILE   A 1 330 ? 18.504 -5.259  -18.777 1.00 41.80  ? 330 ILE   A CG1 1 
ATOM   2369 C CG2 . ILE   A 1 330 ? 20.453 -4.407  -17.502 1.00 40.84  ? 330 ILE   A CG2 1 
ATOM   2370 C CD1 . ILE   A 1 330 ? 17.754 -6.246  -19.479 1.00 49.84  ? 330 ILE   A CD1 1 
ATOM   2371 N N   . ALA   A 1 331 ? 23.092 -6.313  -18.464 1.00 39.54  ? 331 ALA   A N   1 
ATOM   2372 C CA  . ALA   A 1 331 ? 24.488 -5.949  -18.250 1.00 38.24  ? 331 ALA   A CA  1 
ATOM   2373 C C   . ALA   A 1 331 ? 25.227 -5.806  -19.586 1.00 43.02  ? 331 ALA   A C   1 
ATOM   2374 O O   . ALA   A 1 331 ? 25.919 -4.802  -19.787 1.00 43.69  ? 331 ALA   A O   1 
ATOM   2375 C CB  . ALA   A 1 331 ? 25.166 -6.963  -17.350 1.00 38.09  ? 331 ALA   A CB  1 
ATOM   2376 N N   . SER   A 1 332 ? 25.022 -6.777  -20.512 1.00 37.70  ? 332 SER   A N   1 
ATOM   2377 C CA  . SER   A 1 332 ? 25.621 -6.817  -21.843 1.00 36.27  ? 332 SER   A CA  1 
ATOM   2378 C C   . SER   A 1 332 ? 25.112 -5.668  -22.729 1.00 39.93  ? 332 SER   A C   1 
ATOM   2379 O O   . SER   A 1 332 ? 25.903 -5.088  -23.466 1.00 40.92  ? 332 SER   A O   1 
ATOM   2380 C CB  . SER   A 1 332 ? 25.360 -8.162  -22.509 1.00 38.88  ? 332 SER   A CB  1 
ATOM   2381 O OG  . SER   A 1 332 ? 26.013 -9.251  -21.875 1.00 43.93  ? 332 SER   A OG  1 
ATOM   2382 N N   . ILE   A 1 333 ? 23.815 -5.328  -22.649 1.00 34.72  ? 333 ILE   A N   1 
ATOM   2383 C CA  . ILE   A 1 333 ? 23.216 -4.225  -23.412 1.00 33.61  ? 333 ILE   A CA  1 
ATOM   2384 C C   . ILE   A 1 333 ? 23.828 -2.891  -22.950 1.00 38.06  ? 333 ILE   A C   1 
ATOM   2385 O O   . ILE   A 1 333 ? 24.139 -2.039  -23.780 1.00 38.19  ? 333 ILE   A O   1 
ATOM   2386 C CB  . ILE   A 1 333 ? 21.679 -4.248  -23.310 1.00 35.93  ? 333 ILE   A CB  1 
ATOM   2387 C CG1 . ILE   A 1 333 ? 21.106 -5.446  -24.085 1.00 35.44  ? 333 ILE   A CG1 1 
ATOM   2388 C CG2 . ILE   A 1 333 ? 21.076 -2.927  -23.796 1.00 36.74  ? 333 ILE   A CG2 1 
ATOM   2389 C CD1 . ILE   A 1 333 ? 19.644 -5.768  -23.809 1.00 34.34  ? 333 ILE   A CD1 1 
ATOM   2390 N N   . PHE   A 1 334 ? 24.031 -2.743  -21.630 1.00 33.66  ? 334 PHE   A N   1 
ATOM   2391 C CA  . PHE   A 1 334 ? 24.622 -1.559  -21.020 1.00 32.93  ? 334 PHE   A CA  1 
ATOM   2392 C C   . PHE   A 1 334 ? 26.100 -1.413  -21.322 1.00 37.79  ? 334 PHE   A C   1 
ATOM   2393 O O   . PHE   A 1 334 ? 26.615 -0.299  -21.267 1.00 38.61  ? 334 PHE   A O   1 
ATOM   2394 C CB  . PHE   A 1 334 ? 24.285 -1.473  -19.526 1.00 34.74  ? 334 PHE   A CB  1 
ATOM   2395 C CG  . PHE   A 1 334 ? 22.930 -0.848  -19.259 1.00 36.05  ? 334 PHE   A CG  1 
ATOM   2396 C CD1 . PHE   A 1 334 ? 21.762 -1.448  -19.725 1.00 38.10  ? 334 PHE   A CD1 1 
ATOM   2397 C CD2 . PHE   A 1 334 ? 22.826 0.360   -18.575 1.00 37.37  ? 334 PHE   A CD2 1 
ATOM   2398 C CE1 . PHE   A 1 334 ? 20.514 -0.867  -19.490 1.00 38.99  ? 334 PHE   A CE1 1 
ATOM   2399 C CE2 . PHE   A 1 334 ? 21.581 0.941   -18.343 1.00 40.00  ? 334 PHE   A CE2 1 
ATOM   2400 C CZ  . PHE   A 1 334 ? 20.429 0.320   -18.798 1.00 38.37  ? 334 PHE   A CZ  1 
ATOM   2401 N N   . ALA   A 1 335 ? 26.787 -2.519  -21.690 1.00 35.15  ? 335 ALA   A N   1 
ATOM   2402 C CA  . ALA   A 1 335 ? 28.198 -2.478  -22.112 1.00 34.93  ? 335 ALA   A CA  1 
ATOM   2403 C C   . ALA   A 1 335 ? 28.184 -1.657  -23.441 1.00 39.95  ? 335 ALA   A C   1 
ATOM   2404 O O   . ALA   A 1 335 ? 28.929 -0.693  -23.579 1.00 40.27  ? 335 ALA   A O   1 
ATOM   2405 C CB  . ALA   A 1 335 ? 28.710 -3.888  -22.376 1.00 35.03  ? 335 ALA   A CB  1 
ATOM   2406 N N   . TRP   A 1 336 ? 27.260 -2.013  -24.367 1.00 36.30  ? 336 TRP   A N   1 
ATOM   2407 C CA  . TRP   A 1 336 ? 27.051 -1.357  -25.652 1.00 36.55  ? 336 TRP   A CA  1 
ATOM   2408 C C   . TRP   A 1 336 ? 26.639 0.101   -25.461 1.00 39.59  ? 336 TRP   A C   1 
ATOM   2409 O O   . TRP   A 1 336 ? 27.236 0.971   -26.083 1.00 39.88  ? 336 TRP   A O   1 
ATOM   2410 C CB  . TRP   A 1 336 ? 25.996 -2.126  -26.471 1.00 35.60  ? 336 TRP   A CB  1 
ATOM   2411 C CG  . TRP   A 1 336 ? 26.580 -3.288  -27.211 1.00 36.70  ? 336 TRP   A CG  1 
ATOM   2412 C CD1 . TRP   A 1 336 ? 26.594 -4.594  -26.821 1.00 39.31  ? 336 TRP   A CD1 1 
ATOM   2413 C CD2 . TRP   A 1 336 ? 27.306 -3.228  -28.445 1.00 36.76  ? 336 TRP   A CD2 1 
ATOM   2414 N NE1 . TRP   A 1 336 ? 27.255 -5.358  -27.753 1.00 38.14  ? 336 TRP   A NE1 1 
ATOM   2415 C CE2 . TRP   A 1 336 ? 27.729 -4.541  -28.746 1.00 39.68  ? 336 TRP   A CE2 1 
ATOM   2416 C CE3 . TRP   A 1 336 ? 27.644 -2.181  -29.331 1.00 38.05  ? 336 TRP   A CE3 1 
ATOM   2417 C CZ2 . TRP   A 1 336 ? 28.468 -4.843  -29.892 1.00 39.45  ? 336 TRP   A CZ2 1 
ATOM   2418 C CZ3 . TRP   A 1 336 ? 28.371 -2.483  -30.471 1.00 39.40  ? 336 TRP   A CZ3 1 
ATOM   2419 C CH2 . TRP   A 1 336 ? 28.765 -3.801  -30.751 1.00 40.07  ? 336 TRP   A CH2 1 
ATOM   2420 N N   . THR   A 1 337 ? 25.653 0.368   -24.576 1.00 35.35  ? 337 THR   A N   1 
ATOM   2421 C CA  . THR   A 1 337 ? 25.140 1.717   -24.298 1.00 35.04  ? 337 THR   A CA  1 
ATOM   2422 C C   . THR   A 1 337 ? 26.132 2.670   -23.681 1.00 40.51  ? 337 THR   A C   1 
ATOM   2423 O O   . THR   A 1 337 ? 26.182 3.830   -24.086 1.00 41.00  ? 337 THR   A O   1 
ATOM   2424 C CB  . THR   A 1 337 ? 23.763 1.717   -23.638 1.00 38.97  ? 337 THR   A CB  1 
ATOM   2425 O OG1 . THR   A 1 337 ? 23.852 1.155   -22.344 1.00 41.43  ? 337 THR   A OG1 1 
ATOM   2426 C CG2 . THR   A 1 337 ? 22.720 1.003   -24.452 1.00 32.67  ? 337 THR   A CG2 1 
ATOM   2427 N N   . ARG   A 1 338 ? 26.948 2.195   -22.733 1.00 37.06  ? 338 ARG   A N   1 
ATOM   2428 C CA  . ARG   A 1 338 ? 27.969 3.046   -22.145 1.00 36.55  ? 338 ARG   A CA  1 
ATOM   2429 C C   . ARG   A 1 338 ? 29.046 3.377   -23.178 1.00 42.70  ? 338 ARG   A C   1 
ATOM   2430 O O   . ARG   A 1 338 ? 29.484 4.528   -23.238 1.00 43.82  ? 338 ARG   A O   1 
ATOM   2431 C CB  . ARG   A 1 338 ? 28.550 2.414   -20.878 1.00 37.34  ? 338 ARG   A CB  1 
ATOM   2432 C CG  . ARG   A 1 338 ? 27.877 2.951   -19.605 1.00 46.38  ? 338 ARG   A CG  1 
ATOM   2433 C CD  . ARG   A 1 338 ? 26.653 2.157   -19.238 1.00 53.31  ? 338 ARG   A CD  1 
ATOM   2434 N NE  . ARG   A 1 338 ? 25.716 2.937   -18.437 1.00 71.59  ? 338 ARG   A NE  1 
ATOM   2435 C CZ  . ARG   A 1 338 ? 25.335 2.612   -17.205 1.00 86.66  ? 338 ARG   A CZ  1 
ATOM   2436 N NH1 . ARG   A 1 338 ? 24.471 3.376   -16.549 1.00 82.45  ? 338 ARG   A NH1 1 
ATOM   2437 N NH2 . ARG   A 1 338 ? 25.813 1.517   -16.621 1.00 55.14  ? 338 ARG   A NH2 1 
ATOM   2438 N N   . GLY   A 1 339 ? 29.431 2.377   -23.996 1.00 39.05  ? 339 GLY   A N   1 
ATOM   2439 C CA  . GLY   A 1 339 ? 30.408 2.526   -25.067 1.00 38.89  ? 339 GLY   A CA  1 
ATOM   2440 C C   . GLY   A 1 339 ? 29.887 3.514   -26.091 1.00 44.66  ? 339 GLY   A C   1 
ATOM   2441 O O   . GLY   A 1 339 ? 30.566 4.497   -26.397 1.00 45.39  ? 339 GLY   A O   1 
ATOM   2442 N N   . LEU   A 1 340 ? 28.640 3.296   -26.586 1.00 40.81  ? 340 LEU   A N   1 
ATOM   2443 C CA  . LEU   A 1 340 ? 27.997 4.202   -27.550 1.00 39.50  ? 340 LEU   A CA  1 
ATOM   2444 C C   . LEU   A 1 340 ? 27.782 5.624   -27.023 1.00 42.32  ? 340 LEU   A C   1 
ATOM   2445 O O   . LEU   A 1 340 ? 27.919 6.556   -27.803 1.00 42.09  ? 340 LEU   A O   1 
ATOM   2446 C CB  . LEU   A 1 340 ? 26.726 3.618   -28.164 1.00 39.30  ? 340 LEU   A CB  1 
ATOM   2447 C CG  . LEU   A 1 340 ? 26.938 2.406   -29.086 1.00 42.61  ? 340 LEU   A CG  1 
ATOM   2448 C CD1 . LEU   A 1 340 ? 25.618 1.757   -29.439 1.00 41.40  ? 340 LEU   A CD1 1 
ATOM   2449 C CD2 . LEU   A 1 340 ? 27.736 2.780   -30.336 1.00 43.50  ? 340 LEU   A CD2 1 
ATOM   2450 N N   . ALA   A 1 341 ? 27.503 5.801   -25.708 1.00 38.17  ? 341 ALA   A N   1 
ATOM   2451 C CA  . ALA   A 1 341 ? 27.343 7.129   -25.080 1.00 37.10  ? 341 ALA   A CA  1 
ATOM   2452 C C   . ALA   A 1 341 ? 28.712 7.861   -25.017 1.00 42.63  ? 341 ALA   A C   1 
ATOM   2453 O O   . ALA   A 1 341 ? 28.781 9.091   -25.140 1.00 42.26  ? 341 ALA   A O   1 
ATOM   2454 C CB  . ALA   A 1 341 ? 26.778 6.985   -23.673 1.00 36.78  ? 341 ALA   A CB  1 
ATOM   2455 N N   . HIS   A 1 342 ? 29.795 7.095   -24.809 1.00 39.82  ? 342 HIS   A N   1 
ATOM   2456 C CA  . HIS   A 1 342 ? 31.129 7.671   -24.738 1.00 39.31  ? 342 HIS   A CA  1 
ATOM   2457 C C   . HIS   A 1 342 ? 31.578 8.066   -26.123 1.00 44.70  ? 342 HIS   A C   1 
ATOM   2458 O O   . HIS   A 1 342 ? 32.160 9.135   -26.279 1.00 46.64  ? 342 HIS   A O   1 
ATOM   2459 C CB  . HIS   A 1 342 ? 32.125 6.736   -24.042 1.00 39.21  ? 342 HIS   A CB  1 
ATOM   2460 C CG  . HIS   A 1 342 ? 33.460 7.378   -23.818 1.00 42.42  ? 342 HIS   A CG  1 
ATOM   2461 N ND1 . HIS   A 1 342 ? 33.624 8.424   -22.915 1.00 43.78  ? 342 HIS   A ND1 1 
ATOM   2462 C CD2 . HIS   A 1 342 ? 34.652 7.121   -24.409 1.00 43.72  ? 342 HIS   A CD2 1 
ATOM   2463 C CE1 . HIS   A 1 342 ? 34.902 8.748   -22.975 1.00 42.85  ? 342 HIS   A CE1 1 
ATOM   2464 N NE2 . HIS   A 1 342 ? 35.561 7.981   -23.850 1.00 43.36  ? 342 HIS   A NE2 1 
ATOM   2465 N N   . ARG   A 1 343 ? 31.273 7.236   -27.131 1.00 39.97  ? 343 ARG   A N   1 
ATOM   2466 C CA  . ARG   A 1 343 ? 31.601 7.514   -28.532 1.00 39.56  ? 343 ARG   A CA  1 
ATOM   2467 C C   . ARG   A 1 343 ? 30.893 8.819   -28.958 1.00 43.57  ? 343 ARG   A C   1 
ATOM   2468 O O   . ARG   A 1 343 ? 31.534 9.697   -29.515 1.00 44.13  ? 343 ARG   A O   1 
ATOM   2469 C CB  . ARG   A 1 343 ? 31.196 6.317   -29.429 1.00 36.70  ? 343 ARG   A CB  1 
ATOM   2470 C CG  . ARG   A 1 343 ? 31.375 6.521   -30.929 1.00 33.88  ? 343 ARG   A CG  1 
ATOM   2471 C CD  . ARG   A 1 343 ? 32.809 6.329   -31.407 1.00 37.21  ? 343 ARG   A CD  1 
ATOM   2472 N NE  . ARG   A 1 343 ? 33.627 7.529   -31.203 1.00 41.29  ? 343 ARG   A NE  1 
ATOM   2473 C CZ  . ARG   A 1 343 ? 34.953 7.539   -31.065 1.00 50.09  ? 343 ARG   A CZ  1 
ATOM   2474 N NH1 . ARG   A 1 343 ? 35.643 6.403   -31.096 1.00 30.11  ? 343 ARG   A NH1 1 
ATOM   2475 N NH2 . ARG   A 1 343 ? 35.597 8.683   -30.881 1.00 34.45  ? 343 ARG   A NH2 1 
ATOM   2476 N N   . ALA   A 1 344 ? 29.596 8.943   -28.655 1.00 40.36  ? 344 ALA   A N   1 
ATOM   2477 C CA  . ALA   A 1 344 ? 28.755 10.107  -28.943 1.00 40.77  ? 344 ALA   A CA  1 
ATOM   2478 C C   . ALA   A 1 344 ? 29.297 11.376  -28.271 1.00 47.38  ? 344 ALA   A C   1 
ATOM   2479 O O   . ALA   A 1 344 ? 29.303 12.431  -28.907 1.00 48.31  ? 344 ALA   A O   1 
ATOM   2480 C CB  . ALA   A 1 344 ? 27.327 9.850   -28.492 1.00 41.14  ? 344 ALA   A CB  1 
ATOM   2481 N N   . LYS   A 1 345 ? 29.757 11.273  -27.004 1.00 43.74  ? 345 LYS   A N   1 
ATOM   2482 C CA  . LYS   A 1 345 ? 30.337 12.382  -26.250 1.00 43.96  ? 345 LYS   A CA  1 
ATOM   2483 C C   . LYS   A 1 345 ? 31.623 12.879  -26.953 1.00 50.11  ? 345 LYS   A C   1 
ATOM   2484 O O   . LYS   A 1 345 ? 31.761 14.080  -27.187 1.00 51.84  ? 345 LYS   A O   1 
ATOM   2485 C CB  . LYS   A 1 345 ? 30.616 11.957  -24.804 1.00 46.65  ? 345 LYS   A CB  1 
ATOM   2486 C CG  . LYS   A 1 345 ? 30.993 13.110  -23.872 1.00 67.70  ? 345 LYS   A CG  1 
ATOM   2487 C CD  . LYS   A 1 345 ? 32.091 12.723  -22.859 1.00 79.28  ? 345 LYS   A CD  1 
ATOM   2488 C CE  . LYS   A 1 345 ? 31.565 12.319  -21.496 1.00 90.90  ? 345 LYS   A CE  1 
ATOM   2489 N NZ  . LYS   A 1 345 ? 32.668 12.069  -20.522 1.00 99.98  ? 345 LYS   A NZ  1 
ATOM   2490 N N   . LEU   A 1 346 ? 32.529 11.958  -27.326 1.00 46.21  ? 346 LEU   A N   1 
ATOM   2491 C CA  . LEU   A 1 346 ? 33.790 12.286  -28.009 1.00 45.13  ? 346 LEU   A CA  1 
ATOM   2492 C C   . LEU   A 1 346 ? 33.585 12.959  -29.362 1.00 48.60  ? 346 LEU   A C   1 
ATOM   2493 O O   . LEU   A 1 346 ? 34.340 13.853  -29.717 1.00 49.04  ? 346 LEU   A O   1 
ATOM   2494 C CB  . LEU   A 1 346 ? 34.656 11.025  -28.215 1.00 44.49  ? 346 LEU   A CB  1 
ATOM   2495 C CG  . LEU   A 1 346 ? 35.156 10.251  -26.981 1.00 48.24  ? 346 LEU   A CG  1 
ATOM   2496 C CD1 . LEU   A 1 346 ? 36.028 9.065   -27.402 1.00 46.17  ? 346 LEU   A CD1 1 
ATOM   2497 C CD2 . LEU   A 1 346 ? 35.892 11.168  -25.974 1.00 50.15  ? 346 LEU   A CD2 1 
ATOM   2498 N N   . ASP   A 1 347 ? 32.583 12.517  -30.118 1.00 45.10  ? 347 ASP   A N   1 
ATOM   2499 C CA  . ASP   A 1 347 ? 32.292 13.008  -31.470 1.00 44.39  ? 347 ASP   A CA  1 
ATOM   2500 C C   . ASP   A 1 347 ? 31.157 14.040  -31.563 1.00 49.76  ? 347 ASP   A C   1 
ATOM   2501 O O   . ASP   A 1 347 ? 30.768 14.387  -32.681 1.00 50.32  ? 347 ASP   A O   1 
ATOM   2502 C CB  . ASP   A 1 347 ? 31.930 11.805  -32.355 1.00 44.87  ? 347 ASP   A CB  1 
ATOM   2503 C CG  . ASP   A 1 347 ? 32.988 10.745  -32.536 1.00 48.70  ? 347 ASP   A CG  1 
ATOM   2504 O OD1 . ASP   A 1 347 ? 34.120 10.934  -32.030 1.00 51.05  ? 347 ASP   A OD1 1 
ATOM   2505 O OD2 . ASP   A 1 347 ? 32.692 9.731   -33.195 1.00 52.07  ? 347 ASP   A OD2 1 
ATOM   2506 N N   . ASN   A 1 348 ? 30.619 14.518  -30.420 1.00 46.42  ? 348 ASN   A N   1 
ATOM   2507 C CA  . ASN   A 1 348 ? 29.481 15.451  -30.371 1.00 46.43  ? 348 ASN   A CA  1 
ATOM   2508 C C   . ASN   A 1 348 ? 28.366 14.954  -31.325 1.00 47.59  ? 348 ASN   A C   1 
ATOM   2509 O O   . ASN   A 1 348 ? 27.925 15.685  -32.207 1.00 48.06  ? 348 ASN   A O   1 
ATOM   2510 C CB  . ASN   A 1 348 ? 29.910 16.916  -30.617 1.00 49.56  ? 348 ASN   A CB  1 
ATOM   2511 C CG  . ASN   A 1 348 ? 30.939 17.420  -29.628 1.00 87.95  ? 348 ASN   A CG  1 
ATOM   2512 O OD1 . ASN   A 1 348 ? 32.078 17.749  -29.991 1.00 85.07  ? 348 ASN   A OD1 1 
ATOM   2513 N ND2 . ASN   A 1 348 ? 30.569 17.489  -28.353 1.00 84.71  ? 348 ASN   A ND2 1 
ATOM   2514 N N   . ASN   A 1 349 ? 27.962 13.678  -31.153 1.00 42.05  ? 349 ASN   A N   1 
ATOM   2515 C CA  . ASN   A 1 349 ? 26.953 12.969  -31.957 1.00 41.16  ? 349 ASN   A CA  1 
ATOM   2516 C C   . ASN   A 1 349 ? 25.635 12.813  -31.176 1.00 46.61  ? 349 ASN   A C   1 
ATOM   2517 O O   . ASN   A 1 349 ? 25.404 11.806  -30.499 1.00 46.15  ? 349 ASN   A O   1 
ATOM   2518 C CB  . ASN   A 1 349 ? 27.524 11.615  -32.453 1.00 34.35  ? 349 ASN   A CB  1 
ATOM   2519 C CG  . ASN   A 1 349 ? 26.738 10.895  -33.519 1.00 47.85  ? 349 ASN   A CG  1 
ATOM   2520 O OD1 . ASN   A 1 349 ? 25.559 11.165  -33.770 1.00 49.78  ? 349 ASN   A OD1 1 
ATOM   2521 N ND2 . ASN   A 1 349 ? 27.375 9.928   -34.175 1.00 34.08  ? 349 ASN   A ND2 1 
ATOM   2522 N N   . LYS   A 1 350 ? 24.786 13.846  -31.273 1.00 43.93  ? 350 LYS   A N   1 
ATOM   2523 C CA  . LYS   A 1 350 ? 23.482 13.949  -30.615 1.00 42.93  ? 350 LYS   A CA  1 
ATOM   2524 C C   . LYS   A 1 350 ? 22.542 12.772  -30.901 1.00 45.08  ? 350 LYS   A C   1 
ATOM   2525 O O   . LYS   A 1 350 ? 21.878 12.291  -29.986 1.00 45.40  ? 350 LYS   A O   1 
ATOM   2526 C CB  . LYS   A 1 350 ? 22.829 15.315  -30.920 1.00 44.17  ? 350 LYS   A CB  1 
ATOM   2527 N N   . GLU   A 1 351 ? 22.514 12.291  -32.145 1.00 40.72  ? 351 GLU   A N   1 
ATOM   2528 C CA  . GLU   A 1 351 ? 21.669 11.166  -32.575 1.00 40.88  ? 351 GLU   A CA  1 
ATOM   2529 C C   . GLU   A 1 351 ? 22.060 9.851   -31.874 1.00 45.86  ? 351 GLU   A C   1 
ATOM   2530 O O   . GLU   A 1 351 ? 21.175 9.099   -31.446 1.00 44.58  ? 351 GLU   A O   1 
ATOM   2531 C CB  . GLU   A 1 351 ? 21.735 10.986  -34.104 1.00 42.54  ? 351 GLU   A CB  1 
ATOM   2532 C CG  . GLU   A 1 351 ? 21.094 12.110  -34.914 1.00 53.46  ? 351 GLU   A CG  1 
ATOM   2533 C CD  . GLU   A 1 351 ? 21.898 13.385  -35.136 1.00 82.46  ? 351 GLU   A CD  1 
ATOM   2534 O OE1 . GLU   A 1 351 ? 21.276 14.386  -35.561 1.00 94.28  ? 351 GLU   A OE1 1 
ATOM   2535 O OE2 . GLU   A 1 351 ? 23.131 13.397  -34.895 1.00 67.02  ? 351 GLU   A OE2 1 
ATOM   2536 N N   . LEU   A 1 352 ? 23.401 9.582   -31.772 1.00 41.49  ? 352 LEU   A N   1 
ATOM   2537 C CA  . LEU   A 1 352 ? 23.945 8.399   -31.132 1.00 39.67  ? 352 LEU   A CA  1 
ATOM   2538 C C   . LEU   A 1 352 ? 23.776 8.516   -29.634 1.00 42.86  ? 352 LEU   A C   1 
ATOM   2539 O O   . LEU   A 1 352 ? 23.490 7.509   -28.985 1.00 42.84  ? 352 LEU   A O   1 
ATOM   2540 C CB  . LEU   A 1 352 ? 25.417 8.141   -31.509 1.00 39.07  ? 352 LEU   A CB  1 
ATOM   2541 C CG  . LEU   A 1 352 ? 26.002 6.807   -30.970 1.00 41.48  ? 352 LEU   A CG  1 
ATOM   2542 C CD1 . LEU   A 1 352 ? 25.363 5.602   -31.658 1.00 40.36  ? 352 LEU   A CD1 1 
ATOM   2543 C CD2 . LEU   A 1 352 ? 27.519 6.781   -31.042 1.00 39.80  ? 352 LEU   A CD2 1 
ATOM   2544 N N   . ALA   A 1 353 ? 23.949 9.736   -29.079 1.00 38.55  ? 353 ALA   A N   1 
ATOM   2545 C CA  . ALA   A 1 353 ? 23.774 10.012  -27.637 1.00 36.58  ? 353 ALA   A CA  1 
ATOM   2546 C C   . ALA   A 1 353 ? 22.304 9.761   -27.279 1.00 41.50  ? 353 ALA   A C   1 
ATOM   2547 O O   . ALA   A 1 353 ? 22.015 9.170   -26.242 1.00 44.59  ? 353 ALA   A O   1 
ATOM   2548 C CB  . ALA   A 1 353 ? 24.176 11.449  -27.304 1.00 36.21  ? 353 ALA   A CB  1 
ATOM   2549 N N   . PHE   A 1 354 ? 21.383 10.152  -28.158 1.00 35.87  ? 354 PHE   A N   1 
ATOM   2550 C CA  . PHE   A 1 354 ? 19.973 9.912   -27.904 1.00 35.36  ? 354 PHE   A CA  1 
ATOM   2551 C C   . PHE   A 1 354 ? 19.658 8.392   -27.982 1.00 40.73  ? 354 PHE   A C   1 
ATOM   2552 O O   . PHE   A 1 354 ? 18.897 7.882   -27.146 1.00 40.21  ? 354 PHE   A O   1 
ATOM   2553 C CB  . PHE   A 1 354 ? 19.068 10.732  -28.856 1.00 35.86  ? 354 PHE   A CB  1 
ATOM   2554 C CG  . PHE   A 1 354 ? 17.611 10.472  -28.564 1.00 37.05  ? 354 PHE   A CG  1 
ATOM   2555 C CD1 . PHE   A 1 354 ? 16.946 11.191  -27.582 1.00 39.26  ? 354 PHE   A CD1 1 
ATOM   2556 C CD2 . PHE   A 1 354 ? 16.923 9.454   -29.219 1.00 39.57  ? 354 PHE   A CD2 1 
ATOM   2557 C CE1 . PHE   A 1 354 ? 15.610 10.927  -27.288 1.00 39.87  ? 354 PHE   A CE1 1 
ATOM   2558 C CE2 . PHE   A 1 354 ? 15.585 9.181   -28.910 1.00 41.54  ? 354 PHE   A CE2 1 
ATOM   2559 C CZ  . PHE   A 1 354 ? 14.942 9.919   -27.944 1.00 38.99  ? 354 PHE   A CZ  1 
ATOM   2560 N N   . PHE   A 1 355 ? 20.229 7.691   -28.994 1.00 37.01  ? 355 PHE   A N   1 
ATOM   2561 C CA  . PHE   A 1 355 ? 20.023 6.256   -29.187 1.00 36.32  ? 355 PHE   A CA  1 
ATOM   2562 C C   . PHE   A 1 355 ? 20.491 5.475   -27.956 1.00 42.26  ? 355 PHE   A C   1 
ATOM   2563 O O   . PHE   A 1 355 ? 19.728 4.640   -27.457 1.00 42.85  ? 355 PHE   A O   1 
ATOM   2564 C CB  . PHE   A 1 355 ? 20.709 5.737   -30.470 1.00 37.17  ? 355 PHE   A CB  1 
ATOM   2565 C CG  . PHE   A 1 355 ? 20.702 4.227   -30.568 1.00 37.55  ? 355 PHE   A CG  1 
ATOM   2566 C CD1 . PHE   A 1 355 ? 19.577 3.548   -31.032 1.00 38.56  ? 355 PHE   A CD1 1 
ATOM   2567 C CD2 . PHE   A 1 355 ? 21.799 3.481   -30.144 1.00 38.61  ? 355 PHE   A CD2 1 
ATOM   2568 C CE1 . PHE   A 1 355 ? 19.561 2.154   -31.095 1.00 39.02  ? 355 PHE   A CE1 1 
ATOM   2569 C CE2 . PHE   A 1 355 ? 21.779 2.084   -30.201 1.00 40.92  ? 355 PHE   A CE2 1 
ATOM   2570 C CZ  . PHE   A 1 355 ? 20.670 1.431   -30.694 1.00 38.84  ? 355 PHE   A CZ  1 
ATOM   2571 N N   . ALA   A 1 356 ? 21.732 5.747   -27.470 1.00 38.76  ? 356 ALA   A N   1 
ATOM   2572 C CA  . ALA   A 1 356 ? 22.298 5.077   -26.294 1.00 38.77  ? 356 ALA   A CA  1 
ATOM   2573 C C   . ALA   A 1 356 ? 21.392 5.227   -25.072 1.00 44.31  ? 356 ALA   A C   1 
ATOM   2574 O O   . ALA   A 1 356 ? 21.172 4.235   -24.377 1.00 45.52  ? 356 ALA   A O   1 
ATOM   2575 C CB  . ALA   A 1 356 ? 23.701 5.575   -25.997 1.00 39.05  ? 356 ALA   A CB  1 
ATOM   2576 N N   . ASN   A 1 357 ? 20.828 6.435   -24.837 1.00 39.20  ? 357 ASN   A N   1 
ATOM   2577 C CA  . ASN   A 1 357 ? 19.909 6.677   -23.716 1.00 37.84  ? 357 ASN   A CA  1 
ATOM   2578 C C   . ASN   A 1 357 ? 18.612 5.943   -23.917 1.00 41.65  ? 357 ASN   A C   1 
ATOM   2579 O O   . ASN   A 1 357 ? 18.096 5.377   -22.951 1.00 42.67  ? 357 ASN   A O   1 
ATOM   2580 C CB  . ASN   A 1 357 ? 19.599 8.160   -23.553 1.00 36.26  ? 357 ASN   A CB  1 
ATOM   2581 C CG  . ASN   A 1 357 ? 20.669 8.973   -22.906 1.00 51.80  ? 357 ASN   A CG  1 
ATOM   2582 O OD1 . ASN   A 1 357 ? 21.644 8.469   -22.325 1.00 53.15  ? 357 ASN   A OD1 1 
ATOM   2583 N ND2 . ASN   A 1 357 ? 20.502 10.265  -22.998 1.00 41.01  ? 357 ASN   A ND2 1 
ATOM   2584 N N   . ALA   A 1 358 ? 18.064 5.959   -25.155 1.00 37.46  ? 358 ALA   A N   1 
ATOM   2585 C CA  . ALA   A 1 358 ? 16.795 5.286   -25.476 1.00 37.25  ? 358 ALA   A CA  1 
ATOM   2586 C C   . ALA   A 1 358 ? 16.893 3.769   -25.251 1.00 43.58  ? 358 ALA   A C   1 
ATOM   2587 O O   . ALA   A 1 358 ? 15.963 3.180   -24.689 1.00 44.45  ? 358 ALA   A O   1 
ATOM   2588 C CB  . ALA   A 1 358 ? 16.354 5.603   -26.906 1.00 37.52  ? 358 ALA   A CB  1 
ATOM   2589 N N   . LEU   A 1 359 ? 18.031 3.146   -25.631 1.00 39.86  ? 359 LEU   A N   1 
ATOM   2590 C CA  . LEU   A 1 359 ? 18.211 1.711   -25.421 1.00 39.73  ? 359 LEU   A CA  1 
ATOM   2591 C C   . LEU   A 1 359 ? 18.228 1.385   -23.924 1.00 43.60  ? 359 LEU   A C   1 
ATOM   2592 O O   . LEU   A 1 359 ? 17.635 0.390   -23.500 1.00 44.60  ? 359 LEU   A O   1 
ATOM   2593 C CB  . LEU   A 1 359 ? 19.454 1.159   -26.165 1.00 39.64  ? 359 LEU   A CB  1 
ATOM   2594 C CG  . LEU   A 1 359 ? 19.674 -0.377  -26.129 1.00 43.31  ? 359 LEU   A CG  1 
ATOM   2595 C CD1 . LEU   A 1 359 ? 18.360 -1.180  -26.387 1.00 43.30  ? 359 LEU   A CD1 1 
ATOM   2596 C CD2 . LEU   A 1 359 ? 20.758 -0.789  -27.080 1.00 43.12  ? 359 LEU   A CD2 1 
ATOM   2597 N N   . GLU   A 1 360 ? 18.846 2.251   -23.128 1.00 38.57  ? 360 GLU   A N   1 
ATOM   2598 C CA  . GLU   A 1 360 ? 18.899 2.091   -21.682 1.00 38.74  ? 360 GLU   A CA  1 
ATOM   2599 C C   . GLU   A 1 360 ? 17.513 2.192   -21.055 1.00 44.14  ? 360 GLU   A C   1 
ATOM   2600 O O   . GLU   A 1 360 ? 17.144 1.346   -20.234 1.00 44.95  ? 360 GLU   A O   1 
ATOM   2601 C CB  . GLU   A 1 360 ? 19.812 3.144   -21.071 1.00 40.18  ? 360 GLU   A CB  1 
ATOM   2602 C CG  . GLU   A 1 360 ? 21.255 2.942   -21.479 1.00 48.89  ? 360 GLU   A CG  1 
ATOM   2603 C CD  . GLU   A 1 360 ? 22.283 3.645   -20.623 1.00 57.01  ? 360 GLU   A CD  1 
ATOM   2604 O OE1 . GLU   A 1 360 ? 21.879 4.420   -19.729 1.00 43.93  ? 360 GLU   A OE1 1 
ATOM   2605 O OE2 . GLU   A 1 360 ? 23.495 3.415   -20.839 1.00 50.75  ? 360 GLU   A OE2 1 
ATOM   2606 N N   . GLU   A 1 361 ? 16.744 3.219   -21.449 1.00 39.94  ? 361 GLU   A N   1 
ATOM   2607 C CA  . GLU   A 1 361 ? 15.402 3.448   -20.935 1.00 38.48  ? 361 GLU   A CA  1 
ATOM   2608 C C   . GLU   A 1 361 ? 14.461 2.339   -21.327 1.00 41.63  ? 361 GLU   A C   1 
ATOM   2609 O O   . GLU   A 1 361 ? 13.710 1.872   -20.478 1.00 41.82  ? 361 GLU   A O   1 
ATOM   2610 C CB  . GLU   A 1 361 ? 14.879 4.839   -21.318 1.00 39.25  ? 361 GLU   A CB  1 
ATOM   2611 C CG  . GLU   A 1 361 ? 15.677 5.961   -20.672 1.00 45.04  ? 361 GLU   A CG  1 
ATOM   2612 C CD  . GLU   A 1 361 ? 15.761 5.927   -19.154 1.00 64.58  ? 361 GLU   A CD  1 
ATOM   2613 O OE1 . GLU   A 1 361 ? 14.726 5.685   -18.486 1.00 67.80  ? 361 GLU   A OE1 1 
ATOM   2614 O OE2 . GLU   A 1 361 ? 16.875 6.149   -18.630 1.00 48.43  ? 361 GLU   A OE2 1 
ATOM   2615 N N   . VAL   A 1 362 ? 14.534 1.867   -22.568 1.00 37.91  ? 362 VAL   A N   1 
ATOM   2616 C CA  . VAL   A 1 362 ? 13.674 0.764   -23.021 1.00 38.52  ? 362 VAL   A CA  1 
ATOM   2617 C C   . VAL   A 1 362 ? 13.929 -0.561  -22.249 1.00 43.69  ? 362 VAL   A C   1 
ATOM   2618 O O   . VAL   A 1 362 ? 13.000 -1.330  -22.018 1.00 44.87  ? 362 VAL   A O   1 
ATOM   2619 C CB  . VAL   A 1 362 ? 13.669 0.608   -24.558 1.00 42.50  ? 362 VAL   A CB  1 
ATOM   2620 C CG1 . VAL   A 1 362 ? 14.845 -0.217  -25.056 1.00 42.40  ? 362 VAL   A CG1 1 
ATOM   2621 C CG2 . VAL   A 1 362 ? 12.379 -0.007  -25.013 1.00 42.65  ? 362 VAL   A CG2 1 
ATOM   2622 N N   . SER   A 1 363 ? 15.177 -0.786  -21.827 1.00 39.38  ? 363 SER   A N   1 
ATOM   2623 C CA  . SER   A 1 363 ? 15.610 -1.951  -21.059 1.00 38.27  ? 363 SER   A CA  1 
ATOM   2624 C C   . SER   A 1 363 ? 15.022 -1.900  -19.644 1.00 43.80  ? 363 SER   A C   1 
ATOM   2625 O O   . SER   A 1 363 ? 14.435 -2.888  -19.202 1.00 43.88  ? 363 SER   A O   1 
ATOM   2626 C CB  . SER   A 1 363 ? 17.137 -2.034  -21.047 1.00 37.99  ? 363 SER   A CB  1 
ATOM   2627 O OG  . SER   A 1 363 ? 17.602 -2.341  -22.354 1.00 40.14  ? 363 SER   A OG  1 
ATOM   2628 N N   . ILE   A 1 364 ? 15.154 -0.737  -18.953 1.00 40.81  ? 364 ILE   A N   1 
ATOM   2629 C CA  . ILE   A 1 364 ? 14.620 -0.487  -17.610 1.00 40.38  ? 364 ILE   A CA  1 
ATOM   2630 C C   . ILE   A 1 364 ? 13.089 -0.584  -17.694 1.00 44.94  ? 364 ILE   A C   1 
ATOM   2631 O O   . ILE   A 1 364 ? 12.491 -1.385  -16.979 1.00 45.63  ? 364 ILE   A O   1 
ATOM   2632 C CB  . ILE   A 1 364 ? 15.103 0.899   -17.064 1.00 43.63  ? 364 ILE   A CB  1 
ATOM   2633 C CG1 . ILE   A 1 364 ? 16.608 0.874   -16.712 1.00 43.76  ? 364 ILE   A CG1 1 
ATOM   2634 C CG2 . ILE   A 1 364 ? 14.265 1.371   -15.851 1.00 44.40  ? 364 ILE   A CG2 1 
ATOM   2635 C CD1 . ILE   A 1 364 ? 17.348 2.297   -16.744 1.00 40.57  ? 364 ILE   A CD1 1 
ATOM   2636 N N   . GLU   A 1 365 ? 12.469 0.213   -18.586 1.00 41.53  ? 365 GLU   A N   1 
ATOM   2637 C CA  . GLU   A 1 365 ? 11.009 0.263   -18.790 1.00 40.63  ? 365 GLU   A CA  1 
ATOM   2638 C C   . GLU   A 1 365 ? 10.377 -1.070  -19.124 1.00 46.05  ? 365 GLU   A C   1 
ATOM   2639 O O   . GLU   A 1 365 ? 9.257  -1.306  -18.680 1.00 46.66  ? 365 GLU   A O   1 
ATOM   2640 C CB  . GLU   A 1 365 ? 10.611 1.340   -19.798 1.00 40.93  ? 365 GLU   A CB  1 
ATOM   2641 C CG  . GLU   A 1 365 ? 10.876 2.748   -19.284 1.00 44.35  ? 365 GLU   A CG  1 
ATOM   2642 C CD  . GLU   A 1 365 ? 11.091 3.804   -20.355 1.00 61.29  ? 365 GLU   A CD  1 
ATOM   2643 O OE1 . GLU   A 1 365 ? 10.654 3.572   -21.506 1.00 39.22  ? 365 GLU   A OE1 1 
ATOM   2644 O OE2 . GLU   A 1 365 ? 11.682 4.867   -20.041 1.00 48.77  ? 365 GLU   A OE2 1 
ATOM   2645 N N   . THR   A 1 366 ? 11.086 -1.961  -19.862 1.00 42.66  ? 366 THR   A N   1 
ATOM   2646 C CA  . THR   A 1 366 ? 10.550 -3.300  -20.191 1.00 42.25  ? 366 THR   A CA  1 
ATOM   2647 C C   . THR   A 1 366 ? 10.403 -4.148  -18.918 1.00 44.42  ? 366 THR   A C   1 
ATOM   2648 O O   . THR   A 1 366 ? 9.362  -4.782  -18.706 1.00 44.35  ? 366 THR   A O   1 
ATOM   2649 C CB  . THR   A 1 366 ? 11.358 -3.978  -21.326 1.00 42.02  ? 366 THR   A CB  1 
ATOM   2650 O OG1 . THR   A 1 366 ? 11.255 -3.161  -22.504 1.00 41.74  ? 366 THR   A OG1 1 
ATOM   2651 C CG2 . THR   A 1 366 ? 10.876 -5.384  -21.645 1.00 31.20  ? 366 THR   A CG2 1 
ATOM   2652 N N   . ILE   A 1 367 ? 11.441 -4.142  -18.076 1.00 39.55  ? 367 ILE   A N   1 
ATOM   2653 C CA  . ILE   A 1 367 ? 11.446 -4.887  -16.819 1.00 39.34  ? 367 ILE   A CA  1 
ATOM   2654 C C   . ILE   A 1 367 ? 10.368 -4.329  -15.901 1.00 44.86  ? 367 ILE   A C   1 
ATOM   2655 O O   . ILE   A 1 367 ? 9.565  -5.101  -15.361 1.00 45.89  ? 367 ILE   A O   1 
ATOM   2656 C CB  . ILE   A 1 367 ? 12.856 -4.959  -16.191 1.00 41.53  ? 367 ILE   A CB  1 
ATOM   2657 C CG1 . ILE   A 1 367 ? 13.782 -5.808  -17.103 1.00 40.99  ? 367 ILE   A CG1 1 
ATOM   2658 C CG2 . ILE   A 1 367 ? 12.805 -5.525  -14.748 1.00 41.63  ? 367 ILE   A CG2 1 
ATOM   2659 C CD1 . ILE   A 1 367 ? 15.272 -5.533  -16.944 1.00 43.60  ? 367 ILE   A CD1 1 
ATOM   2660 N N   . GLU   A 1 368 ? 10.317 -2.983  -15.793 1.00 39.99  ? 368 GLU   A N   1 
ATOM   2661 C CA  . GLU   A 1 368 ? 9.353  -2.233  -14.993 1.00 39.03  ? 368 GLU   A CA  1 
ATOM   2662 C C   . GLU   A 1 368 ? 7.898  -2.469  -15.366 1.00 43.98  ? 368 GLU   A C   1 
ATOM   2663 O O   . GLU   A 1 368 ? 7.037  -2.306  -14.515 1.00 45.47  ? 368 GLU   A O   1 
ATOM   2664 C CB  . GLU   A 1 368 ? 9.702  -0.752  -14.975 1.00 39.90  ? 368 GLU   A CB  1 
ATOM   2665 C CG  . GLU   A 1 368 ? 10.809 -0.445  -13.973 1.00 42.05  ? 368 GLU   A CG  1 
ATOM   2666 C CD  . GLU   A 1 368 ? 11.310 0.982   -13.920 1.00 48.70  ? 368 GLU   A CD  1 
ATOM   2667 O OE1 . GLU   A 1 368 ? 10.971 1.784   -14.818 1.00 59.95  ? 368 GLU   A OE1 1 
ATOM   2668 O OE2 . GLU   A 1 368 ? 12.062 1.296   -12.975 1.00 47.45  ? 368 GLU   A OE2 1 
ATOM   2669 N N   . ALA   A 1 369 ? 7.629  -2.899  -16.604 1.00 39.92  ? 369 ALA   A N   1 
ATOM   2670 C CA  . ALA   A 1 369 ? 6.293  -3.196  -17.124 1.00 39.53  ? 369 ALA   A CA  1 
ATOM   2671 C C   . ALA   A 1 369 ? 5.863  -4.660  -16.841 1.00 47.54  ? 369 ALA   A C   1 
ATOM   2672 O O   . ALA   A 1 369 ? 4.715  -5.043  -17.116 1.00 48.41  ? 369 ALA   A O   1 
ATOM   2673 C CB  . ALA   A 1 369 ? 6.248  -2.898  -18.621 1.00 39.38  ? 369 ALA   A CB  1 
ATOM   2674 N N   . GLY   A 1 370 ? 6.783  -5.450  -16.285 1.00 45.37  ? 370 GLY   A N   1 
ATOM   2675 C CA  . GLY   A 1 370 ? 6.557  -6.848  -15.934 1.00 44.83  ? 370 GLY   A CA  1 
ATOM   2676 C C   . GLY   A 1 370 ? 7.190  -7.869  -16.859 1.00 49.39  ? 370 GLY   A C   1 
ATOM   2677 O O   . GLY   A 1 370 ? 7.036  -9.069  -16.633 1.00 51.12  ? 370 GLY   A O   1 
ATOM   2678 N N   . PHE   A 1 371 ? 7.906  -7.424  -17.904 1.00 44.63  ? 371 PHE   A N   1 
ATOM   2679 C CA  . PHE   A 1 371 ? 8.560  -8.324  -18.861 1.00 42.56  ? 371 PHE   A CA  1 
ATOM   2680 C C   . PHE   A 1 371 ? 10.019 -8.445  -18.456 1.00 43.22  ? 371 PHE   A C   1 
ATOM   2681 O O   . PHE   A 1 371 ? 10.761 -7.484  -18.589 1.00 42.89  ? 371 PHE   A O   1 
ATOM   2682 C CB  . PHE   A 1 371 ? 8.364  -7.829  -20.302 1.00 43.96  ? 371 PHE   A CB  1 
ATOM   2683 C CG  . PHE   A 1 371 ? 6.902  -7.571  -20.595 1.00 45.59  ? 371 PHE   A CG  1 
ATOM   2684 C CD1 . PHE   A 1 371 ? 6.364  -6.291  -20.469 1.00 48.23  ? 371 PHE   A CD1 1 
ATOM   2685 C CD2 . PHE   A 1 371 ? 6.050  -8.615  -20.944 1.00 47.19  ? 371 PHE   A CD2 1 
ATOM   2686 C CE1 . PHE   A 1 371 ? 5.007  -6.061  -20.690 1.00 48.65  ? 371 PHE   A CE1 1 
ATOM   2687 C CE2 . PHE   A 1 371 ? 4.688  -8.379  -21.173 1.00 49.57  ? 371 PHE   A CE2 1 
ATOM   2688 C CZ  . PHE   A 1 371 ? 4.178  -7.107  -21.041 1.00 47.57  ? 371 PHE   A CZ  1 
ATOM   2689 N N   . MET   A 1 372 ? 10.416 -9.619  -17.922 1.00 37.65  ? 372 MET   A N   1 
ATOM   2690 C CA  . MET   A 1 372 ? 11.763 -9.881  -17.414 1.00 37.17  ? 372 MET   A CA  1 
ATOM   2691 C C   . MET   A 1 372 ? 12.166 -11.365 -17.490 1.00 43.14  ? 372 MET   A C   1 
ATOM   2692 O O   . MET   A 1 372 ? 11.314 -12.225 -17.693 1.00 43.24  ? 372 MET   A O   1 
ATOM   2693 C CB  . MET   A 1 372 ? 11.828 -9.434  -15.946 1.00 39.28  ? 372 MET   A CB  1 
ATOM   2694 C CG  . MET   A 1 372 ? 10.923 -10.272 -15.033 1.00 42.29  ? 372 MET   A CG  1 
ATOM   2695 S SD  . MET   A 1 372 ? 10.647 -9.500  -13.455 1.00 46.26  ? 372 MET   A SD  1 
ATOM   2696 C CE  . MET   A 1 372 ? 9.430  -8.245  -13.877 1.00 43.10  ? 372 MET   A CE  1 
ATOM   2697 N N   . THR   A 1 373 ? 13.465 -11.650 -17.291 1.00 40.80  ? 373 THR   A N   1 
ATOM   2698 C CA  . THR   A 1 373 ? 14.017 -13.007 -17.305 1.00 41.11  ? 373 THR   A CA  1 
ATOM   2699 C C   . THR   A 1 373 ? 13.868 -13.655 -15.916 1.00 45.74  ? 373 THR   A C   1 
ATOM   2700 O O   . THR   A 1 373 ? 13.524 -12.951 -14.950 1.00 46.01  ? 373 THR   A O   1 
ATOM   2701 C CB  . THR   A 1 373 ? 15.445 -13.031 -17.898 1.00 41.04  ? 373 THR   A CB  1 
ATOM   2702 O OG1 . THR   A 1 373 ? 16.268 -12.174 -17.132 1.00 36.77  ? 373 THR   A OG1 1 
ATOM   2703 C CG2 . THR   A 1 373 ? 15.480 -12.629 -19.386 1.00 35.15  ? 373 THR   A CG2 1 
ATOM   2704 N N   . LYS   A 1 374 ? 14.109 -14.987 -15.823 1.00 41.36  ? 374 LYS   A N   1 
ATOM   2705 C CA  . LYS   A 1 374 ? 13.960 -15.767 -14.588 1.00 41.70  ? 374 LYS   A CA  1 
ATOM   2706 C C   . LYS   A 1 374 ? 14.600 -15.225 -13.310 1.00 47.32  ? 374 LYS   A C   1 
ATOM   2707 O O   . LYS   A 1 374 ? 13.928 -15.191 -12.277 1.00 49.80  ? 374 LYS   A O   1 
ATOM   2708 C CB  . LYS   A 1 374 ? 14.261 -17.252 -14.800 1.00 43.83  ? 374 LYS   A CB  1 
ATOM   2709 C CG  . LYS   A 1 374 ? 13.780 -18.149 -13.663 1.00 45.72  ? 374 LYS   A CG  1 
ATOM   2710 C CD  . LYS   A 1 374 ? 14.091 -19.603 -13.958 1.00 51.33  ? 374 LYS   A CD  1 
ATOM   2711 C CE  . LYS   A 1 374 ? 13.937 -20.490 -12.737 1.00 60.42  ? 374 LYS   A CE  1 
ATOM   2712 N NZ  . LYS   A 1 374 ? 14.849 -21.671 -12.811 1.00 71.63  ? 374 LYS   A NZ  1 
ATOM   2713 N N   . ASP   A 1 375 ? 15.874 -14.809 -13.377 1.00 42.03  ? 375 ASP   A N   1 
ATOM   2714 C CA  . ASP   A 1 375 ? 16.661 -14.271 -12.257 1.00 41.21  ? 375 ASP   A CA  1 
ATOM   2715 C C   . ASP   A 1 375 ? 15.998 -13.050 -11.609 1.00 45.15  ? 375 ASP   A C   1 
ATOM   2716 O O   . ASP   A 1 375 ? 16.067 -12.885 -10.390 1.00 44.70  ? 375 ASP   A O   1 
ATOM   2717 C CB  . ASP   A 1 375 ? 18.098 -13.924 -12.729 1.00 42.98  ? 375 ASP   A CB  1 
ATOM   2718 C CG  . ASP   A 1 375 ? 18.178 -12.928 -13.900 1.00 59.49  ? 375 ASP   A CG  1 
ATOM   2719 O OD1 . ASP   A 1 375 ? 17.474 -13.146 -14.924 1.00 60.95  ? 375 ASP   A OD1 1 
ATOM   2720 O OD2 . ASP   A 1 375 ? 18.952 -11.937 -13.794 1.00 63.77  ? 375 ASP   A OD2 1 
ATOM   2721 N N   . LEU   A 1 376 ? 15.359 -12.202 -12.437 1.00 42.09  ? 376 LEU   A N   1 
ATOM   2722 C CA  . LEU   A 1 376 ? 14.679 -10.984 -12.023 1.00 42.38  ? 376 LEU   A CA  1 
ATOM   2723 C C   . LEU   A 1 376 ? 13.357 -11.323 -11.380 1.00 48.96  ? 376 LEU   A C   1 
ATOM   2724 O O   . LEU   A 1 376 ? 13.026 -10.766 -10.327 1.00 48.25  ? 376 LEU   A O   1 
ATOM   2725 C CB  . LEU   A 1 376 ? 14.522 -10.016 -13.206 1.00 42.20  ? 376 LEU   A CB  1 
ATOM   2726 C CG  . LEU   A 1 376 ? 15.837 -9.435  -13.751 1.00 46.66  ? 376 LEU   A CG  1 
ATOM   2727 C CD1 . LEU   A 1 376 ? 15.582 -8.605  -14.954 1.00 47.17  ? 376 LEU   A CD1 1 
ATOM   2728 C CD2 . LEU   A 1 376 ? 16.596 -8.625  -12.687 1.00 48.08  ? 376 LEU   A CD2 1 
ATOM   2729 N N   . ALA   A 1 377 ? 12.621 -12.271 -11.990 1.00 47.27  ? 377 ALA   A N   1 
ATOM   2730 C CA  . ALA   A 1 377 ? 11.354 -12.768 -11.463 1.00 47.74  ? 377 ALA   A CA  1 
ATOM   2731 C C   . ALA   A 1 377 ? 11.645 -13.374 -10.057 1.00 53.10  ? 377 ALA   A C   1 
ATOM   2732 O O   . ALA   A 1 377 ? 10.903 -13.112 -9.108  1.00 52.69  ? 377 ALA   A O   1 
ATOM   2733 C CB  . ALA   A 1 377 ? 10.780 -13.822 -12.407 1.00 48.28  ? 377 ALA   A CB  1 
ATOM   2734 N N   . ALA   A 1 378 ? 12.767 -14.119 -9.925  1.00 50.34  ? 378 ALA   A N   1 
ATOM   2735 C CA  . ALA   A 1 378 ? 13.199 -14.728 -8.667  1.00 50.76  ? 378 ALA   A CA  1 
ATOM   2736 C C   . ALA   A 1 378 ? 13.538 -13.699 -7.599  1.00 57.74  ? 378 ALA   A C   1 
ATOM   2737 O O   . ALA   A 1 378 ? 13.374 -14.009 -6.422  1.00 58.21  ? 378 ALA   A O   1 
ATOM   2738 C CB  . ALA   A 1 378 ? 14.360 -15.687 -8.894  1.00 51.08  ? 378 ALA   A CB  1 
ATOM   2739 N N   . CYS   A 1 379 ? 13.981 -12.478 -7.990  1.00 56.29  ? 379 CYS   A N   1 
ATOM   2740 C CA  . CYS   A 1 379 ? 14.297 -11.394 -7.041  1.00 57.83  ? 379 CYS   A CA  1 
ATOM   2741 C C   . CYS   A 1 379 ? 13.027 -10.913 -6.389  1.00 60.65  ? 379 CYS   A C   1 
ATOM   2742 O O   . CYS   A 1 379 ? 13.030 -10.559 -5.211  1.00 60.36  ? 379 CYS   A O   1 
ATOM   2743 C CB  . CYS   A 1 379 ? 14.998 -10.232 -7.734  1.00 59.83  ? 379 CYS   A CB  1 
ATOM   2744 S SG  . CYS   A 1 379 ? 16.722 -10.544 -8.144  1.00 64.90  ? 379 CYS   A SG  1 
ATOM   2745 N N   . ILE   A 1 380 ? 11.953 -10.857 -7.184  1.00 56.46  ? 380 ILE   A N   1 
ATOM   2746 C CA  . ILE   A 1 380 ? 10.644 -10.404 -6.755  1.00 56.03  ? 380 ILE   A CA  1 
ATOM   2747 C C   . ILE   A 1 380 ? 9.904  -11.459 -5.927  1.00 61.30  ? 380 ILE   A C   1 
ATOM   2748 O O   . ILE   A 1 380 ? 9.522  -11.172 -4.795  1.00 62.03  ? 380 ILE   A O   1 
ATOM   2749 C CB  . ILE   A 1 380 ? 9.801  -9.937  -7.973  1.00 58.11  ? 380 ILE   A CB  1 
ATOM   2750 C CG1 . ILE   A 1 380 ? 10.472 -8.735  -8.698  1.00 57.28  ? 380 ILE   A CG1 1 
ATOM   2751 C CG2 . ILE   A 1 380 ? 8.346  -9.628  -7.551  1.00 58.18  ? 380 ILE   A CG2 1 
ATOM   2752 C CD1 . ILE   A 1 380 ? 9.835  -8.378  -10.044 1.00 54.03  ? 380 ILE   A CD1 1 
ATOM   2753 N N   . LYS   A 1 381 ? 9.694  -12.659 -6.502  1.00 57.63  ? 381 LYS   A N   1 
ATOM   2754 C CA  . LYS   A 1 381 ? 8.926  -13.758 -5.923  1.00 57.46  ? 381 LYS   A CA  1 
ATOM   2755 C C   . LYS   A 1 381 ? 9.666  -14.804 -5.100  1.00 64.29  ? 381 LYS   A C   1 
ATOM   2756 O O   . LYS   A 1 381 ? 9.035  -15.521 -4.318  1.00 66.00  ? 381 LYS   A O   1 
ATOM   2757 C CB  . LYS   A 1 381 ? 8.088  -14.436 -7.029  1.00 59.04  ? 381 LYS   A CB  1 
ATOM   2758 C CG  . LYS   A 1 381 ? 7.049  -13.510 -7.645  1.00 65.46  ? 381 LYS   A CG  1 
ATOM   2759 C CD  . LYS   A 1 381 ? 6.270  -14.173 -8.755  1.00 72.64  ? 381 LYS   A CD  1 
ATOM   2760 C CE  . LYS   A 1 381 ? 5.147  -13.307 -9.287  1.00 76.84  ? 381 LYS   A CE  1 
ATOM   2761 N NZ  . LYS   A 1 381 ? 3.988  -13.247 -8.351  1.00 83.08  ? 381 LYS   A NZ  1 
ATOM   2762 N N   . GLY   A 1 382 ? 10.969 -14.921 -5.289  1.00 60.65  ? 382 GLY   A N   1 
ATOM   2763 C CA  . GLY   A 1 382 ? 11.754 -15.930 -4.587  1.00 60.22  ? 382 GLY   A CA  1 
ATOM   2764 C C   . GLY   A 1 382 ? 11.869 -17.158 -5.462  1.00 62.41  ? 382 GLY   A C   1 
ATOM   2765 O O   . GLY   A 1 382 ? 10.870 -17.581 -6.055  1.00 62.36  ? 382 GLY   A O   1 
ATOM   2766 N N   . LEU   A 1 383 ? 13.081 -17.737 -5.560  1.00 57.20  ? 383 LEU   A N   1 
ATOM   2767 C CA  . LEU   A 1 383 ? 13.332 -18.920 -6.401  1.00 56.48  ? 383 LEU   A CA  1 
ATOM   2768 C C   . LEU   A 1 383 ? 12.340 -20.122 -6.286  1.00 58.95  ? 383 LEU   A C   1 
ATOM   2769 O O   . LEU   A 1 383 ? 11.957 -20.651 -7.331  1.00 59.23  ? 383 LEU   A O   1 
ATOM   2770 C CB  . LEU   A 1 383 ? 14.828 -19.344 -6.417  1.00 56.00  ? 383 LEU   A CB  1 
ATOM   2771 C CG  . LEU   A 1 383 ? 15.279 -20.409 -7.458  1.00 59.04  ? 383 LEU   A CG  1 
ATOM   2772 C CD1 . LEU   A 1 383 ? 14.830 -20.061 -8.900  1.00 58.24  ? 383 LEU   A CD1 1 
ATOM   2773 C CD2 . LEU   A 1 383 ? 16.780 -20.611 -7.402  1.00 58.63  ? 383 LEU   A CD2 1 
ATOM   2774 N N   . PRO   A 1 384 ? 11.876 -20.554 -5.088  1.00 53.92  ? 384 PRO   A N   1 
ATOM   2775 C CA  . PRO   A 1 384 ? 10.929 -21.688 -5.051  1.00 53.08  ? 384 PRO   A CA  1 
ATOM   2776 C C   . PRO   A 1 384 ? 9.507  -21.374 -5.534  1.00 54.09  ? 384 PRO   A C   1 
ATOM   2777 O O   . PRO   A 1 384 ? 8.756  -22.285 -5.865  1.00 52.85  ? 384 PRO   A O   1 
ATOM   2778 C CB  . PRO   A 1 384 ? 10.920 -22.106 -3.570  1.00 54.89  ? 384 PRO   A CB  1 
ATOM   2779 C CG  . PRO   A 1 384 ? 11.967 -21.277 -2.890  1.00 59.31  ? 384 PRO   A CG  1 
ATOM   2780 C CD  . PRO   A 1 384 ? 12.185 -20.074 -3.723  1.00 55.12  ? 384 PRO   A CD  1 
ATOM   2781 N N   . ASN   A 1 385 ? 9.149  -20.092 -5.587  1.00 49.94  ? 385 ASN   A N   1 
ATOM   2782 C CA  . ASN   A 1 385 ? 7.817  -19.594 -5.964  1.00 48.79  ? 385 ASN   A CA  1 
ATOM   2783 C C   . ASN   A 1 385 ? 7.689  -19.143 -7.428  1.00 52.67  ? 385 ASN   A C   1 
ATOM   2784 O O   . ASN   A 1 385 ? 6.593  -18.810 -7.892  1.00 52.06  ? 385 ASN   A O   1 
ATOM   2785 C CB  . ASN   A 1 385 ? 7.423  -18.485 -4.993  1.00 45.67  ? 385 ASN   A CB  1 
ATOM   2786 C CG  . ASN   A 1 385 ? 7.700  -18.846 -3.535  1.00 66.60  ? 385 ASN   A CG  1 
ATOM   2787 O OD1 . ASN   A 1 385 ? 7.244  -19.880 -3.012  1.00 53.92  ? 385 ASN   A OD1 1 
ATOM   2788 N ND2 . ASN   A 1 385 ? 8.479  -18.011 -2.856  1.00 56.92  ? 385 ASN   A ND2 1 
ATOM   2789 N N   . VAL   A 1 386 ? 8.807  -19.164 -8.159  1.00 49.36  ? 386 VAL   A N   1 
ATOM   2790 C CA  . VAL   A 1 386 ? 8.859  -18.766 -9.563  1.00 48.90  ? 386 VAL   A CA  1 
ATOM   2791 C C   . VAL   A 1 386 ? 8.179  -19.786 -10.467 1.00 51.58  ? 386 VAL   A C   1 
ATOM   2792 O O   . VAL   A 1 386 ? 8.570  -20.950 -10.487 1.00 52.09  ? 386 VAL   A O   1 
ATOM   2793 C CB  . VAL   A 1 386 ? 10.325 -18.449 -10.003 1.00 52.41  ? 386 VAL   A CB  1 
ATOM   2794 C CG1 . VAL   A 1 386 ? 10.472 -18.398 -11.523 1.00 52.31  ? 386 VAL   A CG1 1 
ATOM   2795 C CG2 . VAL   A 1 386 ? 10.794 -17.146 -9.382  1.00 51.82  ? 386 VAL   A CG2 1 
ATOM   2796 N N   . GLN   A 1 387 ? 7.185  -19.327 -11.234 1.00 46.40  ? 387 GLN   A N   1 
ATOM   2797 C CA  . GLN   A 1 387 ? 6.445  -20.113 -12.221 1.00 45.18  ? 387 GLN   A CA  1 
ATOM   2798 C C   . GLN   A 1 387 ? 6.887  -19.648 -13.609 1.00 49.43  ? 387 GLN   A C   1 
ATOM   2799 O O   . GLN   A 1 387 ? 7.315  -18.500 -13.758 1.00 49.72  ? 387 GLN   A O   1 
ATOM   2800 C CB  . GLN   A 1 387 ? 4.939  -19.864 -12.091 1.00 45.91  ? 387 GLN   A CB  1 
ATOM   2801 C CG  . GLN   A 1 387 ? 4.340  -20.279 -10.764 1.00 48.40  ? 387 GLN   A CG  1 
ATOM   2802 C CD  . GLN   A 1 387 ? 2.872  -19.961 -10.757 1.00 59.14  ? 387 GLN   A CD  1 
ATOM   2803 O OE1 . GLN   A 1 387 ? 2.057  -20.653 -11.401 1.00 52.85  ? 387 GLN   A OE1 1 
ATOM   2804 N NE2 . GLN   A 1 387 ? 2.507  -18.902 -10.028 1.00 40.73  ? 387 GLN   A NE2 1 
ATOM   2805 N N   . ARG   A 1 388 ? 6.733  -20.515 -14.633 1.00 45.10  ? 388 ARG   A N   1 
ATOM   2806 C CA  . ARG   A 1 388 ? 7.092  -20.224 -16.018 1.00 43.57  ? 388 ARG   A CA  1 
ATOM   2807 C C   . ARG   A 1 388 ? 6.423  -18.955 -16.544 1.00 48.44  ? 388 ARG   A C   1 
ATOM   2808 O O   . ARG   A 1 388 ? 7.041  -18.202 -17.293 1.00 47.97  ? 388 ARG   A O   1 
ATOM   2809 C CB  . ARG   A 1 388 ? 6.809  -21.439 -16.918 1.00 39.82  ? 388 ARG   A CB  1 
ATOM   2810 C CG  . ARG   A 1 388 ? 7.230  -21.284 -18.390 1.00 43.80  ? 388 ARG   A CG  1 
ATOM   2811 C CD  . ARG   A 1 388 ? 8.696  -20.869 -18.566 1.00 45.68  ? 388 ARG   A CD  1 
ATOM   2812 N NE  . ARG   A 1 388 ? 8.994  -20.527 -19.955 1.00 51.40  ? 388 ARG   A NE  1 
ATOM   2813 C CZ  . ARG   A 1 388 ? 8.797  -19.332 -20.504 1.00 59.32  ? 388 ARG   A CZ  1 
ATOM   2814 N NH1 . ARG   A 1 388 ? 8.293  -18.336 -19.784 1.00 38.80  ? 388 ARG   A NH1 1 
ATOM   2815 N NH2 . ARG   A 1 388 ? 9.089  -19.127 -21.780 1.00 46.38  ? 388 ARG   A NH2 1 
ATOM   2816 N N   . SER   A 1 389 ? 5.180  -18.699 -16.113 1.00 46.22  ? 389 SER   A N   1 
ATOM   2817 C CA  . SER   A 1 389 ? 4.392  -17.523 -16.513 1.00 45.49  ? 389 SER   A CA  1 
ATOM   2818 C C   . SER   A 1 389 ? 4.888  -16.206 -15.914 1.00 48.01  ? 389 SER   A C   1 
ATOM   2819 O O   . SER   A 1 389 ? 4.357  -15.155 -16.276 1.00 48.28  ? 389 SER   A O   1 
ATOM   2820 C CB  . SER   A 1 389 ? 2.917  -17.735 -16.169 1.00 48.30  ? 389 SER   A CB  1 
ATOM   2821 O OG  . SER   A 1 389 ? 2.731  -17.900 -14.773 1.00 58.00  ? 389 SER   A OG  1 
ATOM   2822 N N   . ASP   A 1 390 ? 5.873  -16.248 -14.989 1.00 43.75  ? 390 ASP   A N   1 
ATOM   2823 C CA  . ASP   A 1 390 ? 6.397  -15.030 -14.339 1.00 43.36  ? 390 ASP   A CA  1 
ATOM   2824 C C   . ASP   A 1 390 ? 7.559  -14.386 -15.107 1.00 46.57  ? 390 ASP   A C   1 
ATOM   2825 O O   . ASP   A 1 390 ? 7.971  -13.277 -14.774 1.00 46.07  ? 390 ASP   A O   1 
ATOM   2826 C CB  . ASP   A 1 390 ? 6.856  -15.327 -12.889 1.00 44.95  ? 390 ASP   A CB  1 
ATOM   2827 C CG  . ASP   A 1 390 ? 5.805  -15.794 -11.900 1.00 52.43  ? 390 ASP   A CG  1 
ATOM   2828 O OD1 . ASP   A 1 390 ? 6.166  -16.556 -10.976 1.00 52.86  ? 390 ASP   A OD1 1 
ATOM   2829 O OD2 . ASP   A 1 390 ? 4.618  -15.397 -12.048 1.00 55.49  ? 390 ASP   A OD2 1 
ATOM   2830 N N   . TYR   A 1 391 ? 8.092  -15.080 -16.116 1.00 43.36  ? 391 TYR   A N   1 
ATOM   2831 C CA  . TYR   A 1 391 ? 9.229  -14.594 -16.879 1.00 42.98  ? 391 TYR   A CA  1 
ATOM   2832 C C   . TYR   A 1 391 ? 9.200  -14.994 -18.343 1.00 47.79  ? 391 TYR   A C   1 
ATOM   2833 O O   . TYR   A 1 391 ? 8.338  -15.762 -18.768 1.00 47.40  ? 391 TYR   A O   1 
ATOM   2834 C CB  . TYR   A 1 391 ? 10.540 -15.087 -16.212 1.00 43.43  ? 391 TYR   A CB  1 
ATOM   2835 C CG  . TYR   A 1 391 ? 10.757 -16.584 -16.269 1.00 43.23  ? 391 TYR   A CG  1 
ATOM   2836 C CD1 . TYR   A 1 391 ? 11.392 -17.175 -17.356 1.00 44.83  ? 391 TYR   A CD1 1 
ATOM   2837 C CD2 . TYR   A 1 391 ? 10.333 -17.411 -15.232 1.00 44.10  ? 391 TYR   A CD2 1 
ATOM   2838 C CE1 . TYR   A 1 391 ? 11.610 -18.549 -17.410 1.00 46.71  ? 391 TYR   A CE1 1 
ATOM   2839 C CE2 . TYR   A 1 391 ? 10.541 -18.789 -15.274 1.00 44.85  ? 391 TYR   A CE2 1 
ATOM   2840 C CZ  . TYR   A 1 391 ? 11.187 -19.354 -16.362 1.00 52.86  ? 391 TYR   A CZ  1 
ATOM   2841 O OH  . TYR   A 1 391 ? 11.394 -20.711 -16.416 1.00 53.30  ? 391 TYR   A OH  1 
ATOM   2842 N N   . LEU   A 1 392 ? 10.179 -14.488 -19.106 1.00 45.39  ? 392 LEU   A N   1 
ATOM   2843 C CA  . LEU   A 1 392 ? 10.350 -14.789 -20.529 1.00 44.93  ? 392 LEU   A CA  1 
ATOM   2844 C C   . LEU   A 1 392 ? 11.653 -15.547 -20.726 1.00 47.11  ? 392 LEU   A C   1 
ATOM   2845 O O   . LEU   A 1 392 ? 12.604 -15.361 -19.950 1.00 45.40  ? 392 LEU   A O   1 
ATOM   2846 C CB  . LEU   A 1 392 ? 10.417 -13.487 -21.367 1.00 44.99  ? 392 LEU   A CB  1 
ATOM   2847 C CG  . LEU   A 1 392 ? 9.187  -12.547 -21.396 1.00 49.45  ? 392 LEU   A CG  1 
ATOM   2848 C CD1 . LEU   A 1 392 ? 9.510  -11.269 -22.144 1.00 48.66  ? 392 LEU   A CD1 1 
ATOM   2849 C CD2 . LEU   A 1 392 ? 7.981  -13.209 -22.038 1.00 51.94  ? 392 LEU   A CD2 1 
ATOM   2850 N N   . ASN   A 1 393 ? 11.727 -16.375 -21.790 1.00 43.73  ? 393 ASN   A N   1 
ATOM   2851 C CA  . ASN   A 1 393 ? 12.993 -17.048 -22.107 1.00 42.79  ? 393 ASN   A CA  1 
ATOM   2852 C C   . ASN   A 1 393 ? 13.893 -15.982 -22.769 1.00 46.11  ? 393 ASN   A C   1 
ATOM   2853 O O   . ASN   A 1 393 ? 13.415 -14.882 -23.093 1.00 44.78  ? 393 ASN   A O   1 
ATOM   2854 C CB  . ASN   A 1 393 ? 12.809 -18.313 -22.993 1.00 39.11  ? 393 ASN   A CB  1 
ATOM   2855 C CG  . ASN   A 1 393 ? 12.296 -18.121 -24.400 1.00 59.35  ? 393 ASN   A CG  1 
ATOM   2856 O OD1 . ASN   A 1 393 ? 12.682 -17.205 -25.130 1.00 54.60  ? 393 ASN   A OD1 1 
ATOM   2857 N ND2 . ASN   A 1 393 ? 11.414 -19.011 -24.824 1.00 54.61  ? 393 ASN   A ND2 1 
ATOM   2858 N N   . THR   A 1 394 ? 15.171 -16.305 -22.967 1.00 43.94  ? 394 THR   A N   1 
ATOM   2859 C CA  . THR   A 1 394 ? 16.172 -15.430 -23.572 1.00 44.11  ? 394 THR   A CA  1 
ATOM   2860 C C   . THR   A 1 394 ? 15.681 -14.747 -24.849 1.00 50.90  ? 394 THR   A C   1 
ATOM   2861 O O   . THR   A 1 394 ? 15.743 -13.526 -24.960 1.00 51.67  ? 394 THR   A O   1 
ATOM   2862 C CB  . THR   A 1 394 ? 17.452 -16.227 -23.774 1.00 49.49  ? 394 THR   A CB  1 
ATOM   2863 O OG1 . THR   A 1 394 ? 17.863 -16.710 -22.491 1.00 52.72  ? 394 THR   A OG1 1 
ATOM   2864 C CG2 . THR   A 1 394 ? 18.563 -15.399 -24.404 1.00 45.73  ? 394 THR   A CG2 1 
ATOM   2865 N N   . PHE   A 1 395 ? 15.172 -15.526 -25.786 1.00 49.41  ? 395 PHE   A N   1 
ATOM   2866 C CA  . PHE   A 1 395 ? 14.697 -15.020 -27.062 1.00 50.43  ? 395 PHE   A CA  1 
ATOM   2867 C C   . PHE   A 1 395 ? 13.429 -14.183 -26.988 1.00 52.94  ? 395 PHE   A C   1 
ATOM   2868 O O   . PHE   A 1 395 ? 13.344 -13.161 -27.665 1.00 52.99  ? 395 PHE   A O   1 
ATOM   2869 C CB  . PHE   A 1 395 ? 14.615 -16.153 -28.083 1.00 53.38  ? 395 PHE   A CB  1 
ATOM   2870 C CG  . PHE   A 1 395 ? 15.894 -16.965 -28.148 1.00 56.56  ? 395 PHE   A CG  1 
ATOM   2871 C CD1 . PHE   A 1 395 ? 16.034 -18.135 -27.407 1.00 61.20  ? 395 PHE   A CD1 1 
ATOM   2872 C CD2 . PHE   A 1 395 ? 16.959 -16.555 -28.941 1.00 59.59  ? 395 PHE   A CD2 1 
ATOM   2873 C CE1 . PHE   A 1 395 ? 17.220 -18.882 -27.467 1.00 62.87  ? 395 PHE   A CE1 1 
ATOM   2874 C CE2 . PHE   A 1 395 ? 18.142 -17.303 -29.000 1.00 62.94  ? 395 PHE   A CE2 1 
ATOM   2875 C CZ  . PHE   A 1 395 ? 18.266 -18.459 -28.266 1.00 61.47  ? 395 PHE   A CZ  1 
ATOM   2876 N N   . GLU   A 1 396 ? 12.464 -14.588 -26.154 1.00 48.23  ? 396 GLU   A N   1 
ATOM   2877 C CA  . GLU   A 1 396 ? 11.206 -13.859 -25.975 1.00 46.82  ? 396 GLU   A CA  1 
ATOM   2878 C C   . GLU   A 1 396 ? 11.489 -12.484 -25.380 1.00 47.44  ? 396 GLU   A C   1 
ATOM   2879 O O   . GLU   A 1 396 ? 10.883 -11.503 -25.795 1.00 46.14  ? 396 GLU   A O   1 
ATOM   2880 C CB  . GLU   A 1 396 ? 10.250 -14.641 -25.065 1.00 48.05  ? 396 GLU   A CB  1 
ATOM   2881 C CG  . GLU   A 1 396 ? 9.726  -15.931 -25.666 1.00 54.46  ? 396 GLU   A CG  1 
ATOM   2882 C CD  . GLU   A 1 396 ? 8.954  -16.801 -24.693 1.00 70.43  ? 396 GLU   A CD  1 
ATOM   2883 O OE1 . GLU   A 1 396 ? 9.268  -16.781 -23.478 1.00 55.15  ? 396 GLU   A OE1 1 
ATOM   2884 O OE2 . GLU   A 1 396 ? 8.027  -17.508 -25.152 1.00 62.68  ? 396 GLU   A OE2 1 
ATOM   2885 N N   . PHE   A 1 397 ? 12.430 -12.413 -24.423 1.00 43.94  ? 397 PHE   A N   1 
ATOM   2886 C CA  . PHE   A 1 397 ? 12.821 -11.155 -23.793 1.00 43.46  ? 397 PHE   A CA  1 
ATOM   2887 C C   . PHE   A 1 397 ? 13.485 -10.184 -24.773 1.00 47.40  ? 397 PHE   A C   1 
ATOM   2888 O O   . PHE   A 1 397 ? 13.117 -9.015  -24.804 1.00 47.55  ? 397 PHE   A O   1 
ATOM   2889 C CB  . PHE   A 1 397 ? 13.654 -11.376 -22.525 1.00 44.44  ? 397 PHE   A CB  1 
ATOM   2890 C CG  . PHE   A 1 397 ? 13.931 -10.085 -21.795 1.00 45.49  ? 397 PHE   A CG  1 
ATOM   2891 C CD1 . PHE   A 1 397 ? 12.899 -9.369  -21.192 1.00 47.98  ? 397 PHE   A CD1 1 
ATOM   2892 C CD2 . PHE   A 1 397 ? 15.219 -9.573  -21.721 1.00 47.30  ? 397 PHE   A CD2 1 
ATOM   2893 C CE1 . PHE   A 1 397 ? 13.159 -8.169  -20.518 1.00 48.05  ? 397 PHE   A CE1 1 
ATOM   2894 C CE2 . PHE   A 1 397 ? 15.475 -8.373  -21.046 1.00 49.23  ? 397 PHE   A CE2 1 
ATOM   2895 C CZ  . PHE   A 1 397 ? 14.444 -7.680  -20.453 1.00 46.88  ? 397 PHE   A CZ  1 
ATOM   2896 N N   . MET   A 1 398 ? 14.428 -10.679 -25.586 1.00 44.50  ? 398 MET   A N   1 
ATOM   2897 C CA  . MET   A 1 398 ? 15.140 -9.911  -26.611 1.00 44.70  ? 398 MET   A CA  1 
ATOM   2898 C C   . MET   A 1 398 ? 14.149 -9.383  -27.649 1.00 48.67  ? 398 MET   A C   1 
ATOM   2899 O O   . MET   A 1 398 ? 14.244 -8.226  -28.061 1.00 49.83  ? 398 MET   A O   1 
ATOM   2900 C CB  . MET   A 1 398 ? 16.230 -10.770 -27.260 1.00 47.28  ? 398 MET   A CB  1 
ATOM   2901 C CG  . MET   A 1 398 ? 17.487 -10.956 -26.372 1.00 51.65  ? 398 MET   A CG  1 
ATOM   2902 S SD  . MET   A 1 398 ? 18.553 -9.480  -26.149 1.00 56.44  ? 398 MET   A SD  1 
ATOM   2903 C CE  . MET   A 1 398 ? 18.634 -8.868  -27.855 1.00 52.72  ? 398 MET   A CE  1 
ATOM   2904 N N   . ASP   A 1 399 ? 13.164 -10.216 -28.029 1.00 43.94  ? 399 ASP   A N   1 
ATOM   2905 C CA  . ASP   A 1 399 ? 12.097 -9.846  -28.963 1.00 42.46  ? 399 ASP   A CA  1 
ATOM   2906 C C   . ASP   A 1 399 ? 11.259 -8.695  -28.387 1.00 43.28  ? 399 ASP   A C   1 
ATOM   2907 O O   . ASP   A 1 399 ? 10.964 -7.752  -29.117 1.00 42.26  ? 399 ASP   A O   1 
ATOM   2908 C CB  . ASP   A 1 399 ? 11.220 -11.064 -29.301 1.00 44.03  ? 399 ASP   A CB  1 
ATOM   2909 C CG  . ASP   A 1 399 ? 11.889 -12.130 -30.172 1.00 57.86  ? 399 ASP   A CG  1 
ATOM   2910 O OD1 . ASP   A 1 399 ? 12.916 -11.812 -30.827 1.00 61.73  ? 399 ASP   A OD1 1 
ATOM   2911 O OD2 . ASP   A 1 399 ? 11.385 -13.284 -30.200 1.00 60.50  ? 399 ASP   A OD2 1 
ATOM   2912 N N   . LYS   A 1 400 ? 10.934 -8.753  -27.067 1.00 38.99  ? 400 LYS   A N   1 
ATOM   2913 C CA  . LYS   A 1 400 ? 10.163 -7.726  -26.354 1.00 38.92  ? 400 LYS   A CA  1 
ATOM   2914 C C   . LYS   A 1 400 ? 10.915 -6.403  -26.364 1.00 45.74  ? 400 LYS   A C   1 
ATOM   2915 O O   . LYS   A 1 400 ? 10.309 -5.384  -26.718 1.00 47.67  ? 400 LYS   A O   1 
ATOM   2916 C CB  . LYS   A 1 400 ? 9.804  -8.160  -24.910 1.00 40.44  ? 400 LYS   A CB  1 
ATOM   2917 C CG  . LYS   A 1 400 ? 8.758  -7.258  -24.228 1.00 47.92  ? 400 LYS   A CG  1 
ATOM   2918 C CD  . LYS   A 1 400 ? 7.326  -7.500  -24.745 1.00 49.92  ? 400 LYS   A CD  1 
ATOM   2919 C CE  . LYS   A 1 400 ? 6.370  -6.430  -24.306 1.00 57.70  ? 400 LYS   A CE  1 
ATOM   2920 N NZ  . LYS   A 1 400 ? 5.385  -6.090  -25.374 1.00 63.80  ? 400 LYS   A NZ  1 
ATOM   2921 N N   . LEU   A 1 401 ? 12.238 -6.417  -26.011 1.00 40.17  ? 401 LEU   A N   1 
ATOM   2922 C CA  . LEU   A 1 401 ? 13.099 -5.225  -26.021 1.00 39.12  ? 401 LEU   A CA  1 
ATOM   2923 C C   . LEU   A 1 401 ? 13.167 -4.626  -27.413 1.00 43.17  ? 401 LEU   A C   1 
ATOM   2924 O O   . LEU   A 1 401 ? 13.090 -3.404  -27.546 1.00 42.08  ? 401 LEU   A O   1 
ATOM   2925 C CB  . LEU   A 1 401 ? 14.530 -5.555  -25.570 1.00 38.60  ? 401 LEU   A CB  1 
ATOM   2926 C CG  . LEU   A 1 401 ? 14.759 -5.884  -24.132 1.00 41.50  ? 401 LEU   A CG  1 
ATOM   2927 C CD1 . LEU   A 1 401 ? 16.183 -6.206  -23.925 1.00 41.74  ? 401 LEU   A CD1 1 
ATOM   2928 C CD2 . LEU   A 1 401 ? 14.380 -4.738  -23.235 1.00 42.59  ? 401 LEU   A CD2 1 
ATOM   2929 N N   . GLY   A 1 402 ? 13.318 -5.497  -28.426 1.00 42.39  ? 402 GLY   A N   1 
ATOM   2930 C CA  . GLY   A 1 402 ? 13.368 -5.125  -29.842 1.00 43.08  ? 402 GLY   A CA  1 
ATOM   2931 C C   . GLY   A 1 402 ? 12.112 -4.399  -30.290 1.00 47.50  ? 402 GLY   A C   1 
ATOM   2932 O O   . GLY   A 1 402 ? 12.191 -3.344  -30.925 1.00 47.67  ? 402 GLY   A O   1 
ATOM   2933 N N   . GLU   A 1 403 ? 10.943 -4.951  -29.917 1.00 44.75  ? 403 GLU   A N   1 
ATOM   2934 C CA  . GLU   A 1 403 ? 9.622  -4.408  -30.221 1.00 44.72  ? 403 GLU   A CA  1 
ATOM   2935 C C   . GLU   A 1 403 ? 9.441  -3.045  -29.553 1.00 49.17  ? 403 GLU   A C   1 
ATOM   2936 O O   . GLU   A 1 403 ? 8.997  -2.104  -30.199 1.00 50.92  ? 403 GLU   A O   1 
ATOM   2937 C CB  . GLU   A 1 403 ? 8.521  -5.405  -29.805 1.00 45.93  ? 403 GLU   A CB  1 
ATOM   2938 N N   . ASN   A 1 404 ? 9.835  -2.923  -28.280 1.00 44.27  ? 404 ASN   A N   1 
ATOM   2939 C CA  . ASN   A 1 404 ? 9.727  -1.669  -27.536 1.00 42.62  ? 404 ASN   A CA  1 
ATOM   2940 C C   . ASN   A 1 404 ? 10.730 -0.632  -28.005 1.00 45.18  ? 404 ASN   A C   1 
ATOM   2941 O O   . ASN   A 1 404 ? 10.466 0.559   -27.852 1.00 45.00  ? 404 ASN   A O   1 
ATOM   2942 C CB  . ASN   A 1 404 ? 9.866  -1.903  -26.045 1.00 39.00  ? 404 ASN   A CB  1 
ATOM   2943 C CG  . ASN   A 1 404 ? 8.746  -2.658  -25.381 1.00 55.23  ? 404 ASN   A CG  1 
ATOM   2944 O OD1 . ASN   A 1 404 ? 7.592  -2.687  -25.847 1.00 45.65  ? 404 ASN   A OD1 1 
ATOM   2945 N ND2 . ASN   A 1 404 ? 9.073  -3.282  -24.246 1.00 46.27  ? 404 ASN   A ND2 1 
ATOM   2946 N N   . LEU   A 1 405 ? 11.884 -1.068  -28.556 1.00 41.07  ? 405 LEU   A N   1 
ATOM   2947 C CA  . LEU   A 1 405 ? 12.899 -0.148  -29.069 1.00 40.50  ? 405 LEU   A CA  1 
ATOM   2948 C C   . LEU   A 1 405 ? 12.385 0.528   -30.334 1.00 46.20  ? 405 LEU   A C   1 
ATOM   2949 O O   . LEU   A 1 405 ? 12.498 1.746   -30.455 1.00 46.99  ? 405 LEU   A O   1 
ATOM   2950 C CB  . LEU   A 1 405 ? 14.246 -0.859  -29.313 1.00 39.78  ? 405 LEU   A CB  1 
ATOM   2951 C CG  . LEU   A 1 405 ? 15.479 0.002   -29.724 1.00 40.54  ? 405 LEU   A CG  1 
ATOM   2952 C CD1 . LEU   A 1 405 ? 15.744 1.151   -28.733 1.00 38.25  ? 405 LEU   A CD1 1 
ATOM   2953 C CD2 . LEU   A 1 405 ? 16.700 -0.868  -29.853 1.00 38.42  ? 405 LEU   A CD2 1 
ATOM   2954 N N   . LYS   A 1 406 ? 11.776 -0.253  -31.241 1.00 44.08  ? 406 LYS   A N   1 
ATOM   2955 C CA  . LYS   A 1 406 ? 11.186 0.224   -32.497 1.00 44.38  ? 406 LYS   A CA  1 
ATOM   2956 C C   . LYS   A 1 406 ? 10.111 1.275   -32.206 1.00 48.41  ? 406 LYS   A C   1 
ATOM   2957 O O   . LYS   A 1 406 ? 10.089 2.305   -32.873 1.00 50.56  ? 406 LYS   A O   1 
ATOM   2958 C CB  . LYS   A 1 406 ? 10.583 -0.955  -33.276 1.00 47.10  ? 406 LYS   A CB  1 
ATOM   2959 C CG  . LYS   A 1 406 ? 10.218 -0.648  -34.719 1.00 55.67  ? 406 LYS   A CG  1 
ATOM   2960 C CD  . LYS   A 1 406 ? 9.658  -1.883  -35.409 1.00 64.02  ? 406 LYS   A CD  1 
ATOM   2961 C CE  . LYS   A 1 406 ? 9.252  -1.609  -36.842 1.00 76.40  ? 406 LYS   A CE  1 
ATOM   2962 N NZ  . LYS   A 1 406 ? 8.690  -2.822  -37.499 1.00 86.26  ? 406 LYS   A NZ  1 
ATOM   2963 N N   . ILE   A 1 407 ? 9.250  1.031   -31.204 1.00 43.07  ? 407 ILE   A N   1 
ATOM   2964 C CA  . ILE   A 1 407 ? 8.162  1.948   -30.813 1.00 42.39  ? 407 ILE   A CA  1 
ATOM   2965 C C   . ILE   A 1 407 ? 8.702  3.275   -30.297 1.00 46.47  ? 407 ILE   A C   1 
ATOM   2966 O O   . ILE   A 1 407 ? 8.300  4.336   -30.781 1.00 46.01  ? 407 ILE   A O   1 
ATOM   2967 C CB  . ILE   A 1 407 ? 7.160  1.266   -29.835 1.00 44.88  ? 407 ILE   A CB  1 
ATOM   2968 C CG1 . ILE   A 1 407 ? 6.419  0.082   -30.533 1.00 44.64  ? 407 ILE   A CG1 1 
ATOM   2969 C CG2 . ILE   A 1 407 ? 6.167  2.275   -29.273 1.00 44.81  ? 407 ILE   A CG2 1 
ATOM   2970 C CD1 . ILE   A 1 407 ? 5.758  -0.950  -29.561 1.00 49.25  ? 407 ILE   A CD1 1 
ATOM   2971 N N   . LYS   A 1 408 ? 9.646  3.202   -29.347 1.00 43.66  ? 408 LYS   A N   1 
ATOM   2972 C CA  . LYS   A 1 408 ? 10.325 4.333   -28.714 1.00 42.52  ? 408 LYS   A CA  1 
ATOM   2973 C C   . LYS   A 1 408 ? 10.928 5.271   -29.764 1.00 47.69  ? 408 LYS   A C   1 
ATOM   2974 O O   . LYS   A 1 408 ? 10.544 6.437   -29.823 1.00 49.14  ? 408 LYS   A O   1 
ATOM   2975 C CB  . LYS   A 1 408 ? 11.386 3.797   -27.733 1.00 43.46  ? 408 LYS   A CB  1 
ATOM   2976 C CG  . LYS   A 1 408 ? 12.387 4.810   -27.172 1.00 43.30  ? 408 LYS   A CG  1 
ATOM   2977 C CD  . LYS   A 1 408 ? 11.930 5.426   -25.874 1.00 48.57  ? 408 LYS   A CD  1 
ATOM   2978 C CE  . LYS   A 1 408 ? 12.082 4.516   -24.681 1.00 42.36  ? 408 LYS   A CE  1 
ATOM   2979 N NZ  . LYS   A 1 408 ? 11.339 5.084   -23.546 1.00 49.15  ? 408 LYS   A NZ  1 
ATOM   2980 N N   . LEU   A 1 409 ? 11.846 4.756   -30.606 1.00 43.16  ? 409 LEU   A N   1 
ATOM   2981 C CA  . LEU   A 1 409 ? 12.519 5.547   -31.644 1.00 41.69  ? 409 LEU   A CA  1 
ATOM   2982 C C   . LEU   A 1 409 ? 11.564 6.173   -32.667 1.00 46.68  ? 409 LEU   A C   1 
ATOM   2983 O O   . LEU   A 1 409 ? 11.874 7.234   -33.198 1.00 47.99  ? 409 LEU   A O   1 
ATOM   2984 C CB  . LEU   A 1 409 ? 13.679 4.777   -32.309 1.00 40.35  ? 409 LEU   A CB  1 
ATOM   2985 C CG  . LEU   A 1 409 ? 14.762 4.180   -31.382 1.00 42.14  ? 409 LEU   A CG  1 
ATOM   2986 C CD1 . LEU   A 1 409 ? 15.604 3.173   -32.117 1.00 41.34  ? 409 LEU   A CD1 1 
ATOM   2987 C CD2 . LEU   A 1 409 ? 15.636 5.262   -30.720 1.00 39.29  ? 409 LEU   A CD2 1 
ATOM   2988 N N   . ALA   A 1 410 ? 10.394 5.552   -32.908 1.00 43.02  ? 410 ALA   A N   1 
ATOM   2989 C CA  . ALA   A 1 410 ? 9.371  6.093   -33.831 1.00 42.30  ? 410 ALA   A CA  1 
ATOM   2990 C C   . ALA   A 1 410 ? 8.715  7.314   -33.176 1.00 48.19  ? 410 ALA   A C   1 
ATOM   2991 O O   . ALA   A 1 410 ? 8.560  8.363   -33.809 1.00 47.78  ? 410 ALA   A O   1 
ATOM   2992 C CB  . ALA   A 1 410 ? 8.320  5.042   -34.145 1.00 41.74  ? 410 ALA   A CB  1 
ATOM   2993 N N   . GLN   A 1 411 ? 8.367  7.171   -31.881 1.00 45.13  ? 411 GLN   A N   1 
ATOM   2994 C CA  . GLN   A 1 411 ? 7.751  8.217   -31.069 1.00 44.04  ? 411 GLN   A CA  1 
ATOM   2995 C C   . GLN   A 1 411 ? 8.691  9.401   -30.883 1.00 47.70  ? 411 GLN   A C   1 
ATOM   2996 O O   . GLN   A 1 411 ? 8.225  10.525  -30.963 1.00 47.07  ? 411 GLN   A O   1 
ATOM   2997 C CB  . GLN   A 1 411 ? 7.248  7.644   -29.735 1.00 44.77  ? 411 GLN   A CB  1 
ATOM   2998 C CG  . GLN   A 1 411 ? 6.104  6.642   -29.937 1.00 43.70  ? 411 GLN   A CG  1 
ATOM   2999 C CD  . GLN   A 1 411 ? 5.728  5.851   -28.706 1.00 53.09  ? 411 GLN   A CD  1 
ATOM   3000 O OE1 . GLN   A 1 411 ? 6.409  5.853   -27.674 1.00 45.34  ? 411 GLN   A OE1 1 
ATOM   3001 N NE2 . GLN   A 1 411 ? 4.628  5.143   -28.801 1.00 43.20  ? 411 GLN   A NE2 1 
ATOM   3002 N N   . ALA   A 1 412 ? 10.014 9.156   -30.705 1.00 44.93  ? 412 ALA   A N   1 
ATOM   3003 C CA  . ALA   A 1 412 ? 11.043 10.202  -30.530 1.00 45.09  ? 412 ALA   A CA  1 
ATOM   3004 C C   . ALA   A 1 412 ? 11.190 11.189  -31.708 1.00 51.40  ? 412 ALA   A C   1 
ATOM   3005 O O   . ALA   A 1 412 ? 11.660 12.311  -31.497 1.00 50.63  ? 412 ALA   A O   1 
ATOM   3006 C CB  . ALA   A 1 412 ? 12.379 9.564   -30.252 1.00 45.34  ? 412 ALA   A CB  1 
ATOM   3007 N N   . LYS   A 1 413 ? 10.809 10.768  -32.938 1.00 49.63  ? 413 LYS   A N   1 
ATOM   3008 C CA  . LYS   A 1 413 ? 10.891 11.572  -34.168 1.00 50.87  ? 413 LYS   A CA  1 
ATOM   3009 C C   . LYS   A 1 413 ? 10.180 12.962  -34.085 1.00 58.05  ? 413 LYS   A C   1 
ATOM   3010 O O   . LYS   A 1 413 ? 10.414 13.825  -34.937 1.00 58.89  ? 413 LYS   A O   1 
ATOM   3011 C CB  . LYS   A 1 413 ? 10.398 10.759  -35.384 1.00 52.91  ? 413 LYS   A CB  1 
ATOM   3012 C CG  . LYS   A 1 413 ? 11.314 9.588   -35.742 1.00 67.45  ? 413 LYS   A CG  1 
ATOM   3013 C CD  . LYS   A 1 413 ? 10.706 8.688   -36.824 1.00 77.42  ? 413 LYS   A CD  1 
ATOM   3014 C CE  . LYS   A 1 413 ? 11.722 7.759   -37.459 1.00 85.20  ? 413 LYS   A CE  1 
ATOM   3015 N NZ  . LYS   A 1 413 ? 11.980 6.542   -36.637 1.00 90.64  ? 413 LYS   A NZ  1 
ATOM   3016 N N   . LEU   A 1 414 ? 9.351  13.174  -33.045 1.00 54.42  ? 414 LEU   A N   1 
ATOM   3017 C CA  . LEU   A 1 414 ? 8.599  14.403  -32.792 1.00 61.42  ? 414 LEU   A CA  1 
ATOM   3018 C C   . LEU   A 1 414 ? 9.362  15.392  -31.887 1.00 88.20  ? 414 LEU   A C   1 
ATOM   3019 O O   . LEU   A 1 414 ? 10.501 15.146  -31.472 1.00 57.98  ? 414 LEU   A O   1 
ATOM   3020 C CB  . LEU   A 1 414 ? 7.233  14.038  -32.170 1.00 61.30  ? 414 LEU   A CB  1 
ATOM   3021 C CG  . LEU   A 1 414 ? 6.484  12.847  -32.796 1.00 65.52  ? 414 LEU   A CG  1 
ATOM   3022 C CD1 . LEU   A 1 414 ? 5.378  12.370  -31.904 1.00 65.14  ? 414 LEU   A CD1 1 
ATOM   3023 C CD2 . LEU   A 1 414 ? 5.931  13.190  -34.166 1.00 69.44  ? 414 LEU   A CD2 1 
ATOM   3024 N N   . LYS   B 1 3   ? 11.438 -17.260 45.784  1.00 63.42  ? 3   LYS   B N   1 
ATOM   3025 C CA  . LYS   B 1 3   ? 12.846 -16.847 45.763  1.00 63.48  ? 3   LYS   B CA  1 
ATOM   3026 C C   . LYS   B 1 3   ? 13.397 -16.750 44.338  1.00 66.67  ? 3   LYS   B C   1 
ATOM   3027 O O   . LYS   B 1 3   ? 13.014 -17.529 43.456  1.00 68.16  ? 3   LYS   B O   1 
ATOM   3028 C CB  . LYS   B 1 3   ? 13.733 -17.767 46.626  1.00 65.79  ? 3   LYS   B CB  1 
ATOM   3029 N N   . LYS   B 1 4   ? 14.304 -15.790 44.127  1.00 58.97  ? 4   LYS   B N   1 
ATOM   3030 C CA  . LYS   B 1 4   ? 14.946 -15.529 42.841  1.00 56.10  ? 4   LYS   B CA  1 
ATOM   3031 C C   . LYS   B 1 4   ? 16.096 -16.509 42.554  1.00 58.74  ? 4   LYS   B C   1 
ATOM   3032 O O   . LYS   B 1 4   ? 16.624 -17.158 43.463  1.00 58.04  ? 4   LYS   B O   1 
ATOM   3033 C CB  . LYS   B 1 4   ? 15.454 -14.077 42.802  1.00 55.38  ? 4   LYS   B CB  1 
ATOM   3034 C CG  . LYS   B 1 4   ? 14.354 -13.062 43.045  1.00 55.26  ? 4   LYS   B CG  1 
ATOM   3035 C CD  . LYS   B 1 4   ? 14.823 -11.654 42.857  1.00 57.28  ? 4   LYS   B CD  1 
ATOM   3036 C CE  . LYS   B 1 4   ? 13.685 -10.680 42.979  1.00 57.17  ? 4   LYS   B CE  1 
ATOM   3037 N NZ  . LYS   B 1 4   ? 14.188 -9.286  42.912  1.00 67.46  ? 4   LYS   B NZ  1 
ATOM   3038 N N   . ILE   B 1 5   ? 16.487 -16.600 41.280  1.00 54.49  ? 5   ILE   B N   1 
ATOM   3039 C CA  . ILE   B 1 5   ? 17.599 -17.429 40.833  1.00 53.63  ? 5   ILE   B CA  1 
ATOM   3040 C C   . ILE   B 1 5   ? 18.880 -16.703 41.300  1.00 56.70  ? 5   ILE   B C   1 
ATOM   3041 O O   . ILE   B 1 5   ? 18.938 -15.465 41.248  1.00 56.03  ? 5   ILE   B O   1 
ATOM   3042 C CB  . ILE   B 1 5   ? 17.577 -17.592 39.270  1.00 56.24  ? 5   ILE   B CB  1 
ATOM   3043 C CG1 . ILE   B 1 5   ? 16.264 -18.213 38.771  1.00 56.13  ? 5   ILE   B CG1 1 
ATOM   3044 C CG2 . ILE   B 1 5   ? 18.789 -18.389 38.753  1.00 56.57  ? 5   ILE   B CG2 1 
ATOM   3045 C CD1 . ILE   B 1 5   ? 15.799 -17.705 37.416  1.00 63.11  ? 5   ILE   B CD1 1 
ATOM   3046 N N   . SER   B 1 6   ? 19.882 -17.468 41.770  1.00 51.98  ? 6   SER   B N   1 
ATOM   3047 C CA  . SER   B 1 6   ? 21.165 -16.910 42.171  1.00 51.05  ? 6   SER   B CA  1 
ATOM   3048 C C   . SER   B 1 6   ? 22.052 -16.999 40.908  1.00 52.27  ? 6   SER   B C   1 
ATOM   3049 O O   . SER   B 1 6   ? 22.516 -18.081 40.534  1.00 50.83  ? 6   SER   B O   1 
ATOM   3050 C CB  . SER   B 1 6   ? 21.753 -17.678 43.349  1.00 55.44  ? 6   SER   B CB  1 
ATOM   3051 O OG  . SER   B 1 6   ? 21.252 -17.160 44.572  1.00 67.99  ? 6   SER   B OG  1 
ATOM   3052 N N   . GLY   B 1 7   ? 22.204 -15.866 40.231  1.00 47.13  ? 7   GLY   B N   1 
ATOM   3053 C CA  . GLY   B 1 7   ? 22.957 -15.767 38.987  1.00 46.31  ? 7   GLY   B CA  1 
ATOM   3054 C C   . GLY   B 1 7   ? 24.466 -15.667 39.093  1.00 50.63  ? 7   GLY   B C   1 
ATOM   3055 O O   . GLY   B 1 7   ? 25.159 -15.780 38.082  1.00 51.38  ? 7   GLY   B O   1 
ATOM   3056 N N   . GLY   B 1 8   ? 24.986 -15.438 40.286  1.00 45.83  ? 8   GLY   B N   1 
ATOM   3057 C CA  . GLY   B 1 8   ? 26.426 -15.317 40.446  1.00 45.28  ? 8   GLY   B CA  1 
ATOM   3058 C C   . GLY   B 1 8   ? 27.000 -14.006 39.943  1.00 48.30  ? 8   GLY   B C   1 
ATOM   3059 O O   . GLY   B 1 8   ? 26.291 -13.015 39.795  1.00 47.73  ? 8   GLY   B O   1 
ATOM   3060 N N   . SER   B 1 9   ? 28.297 -14.032 39.658  1.00 44.54  ? 9   SER   B N   1 
ATOM   3061 C CA  . SER   B 1 9   ? 29.170 -12.946 39.239  1.00 43.69  ? 9   SER   B CA  1 
ATOM   3062 C C   . SER   B 1 9   ? 29.112 -12.526 37.752  1.00 46.37  ? 9   SER   B C   1 
ATOM   3063 O O   . SER   B 1 9   ? 29.608 -13.238 36.877  1.00 45.20  ? 9   SER   B O   1 
ATOM   3064 C CB  . SER   B 1 9   ? 30.594 -13.260 39.694  1.00 45.85  ? 9   SER   B CB  1 
ATOM   3065 O OG  . SER   B 1 9   ? 31.523 -12.303 39.225  1.00 57.88  ? 9   SER   B OG  1 
ATOM   3066 N N   . VAL   B 1 10  ? 28.540 -11.329 37.489  1.00 41.64  ? 10  VAL   B N   1 
ATOM   3067 C CA  . VAL   B 1 10  ? 28.381 -10.752 36.150  1.00 39.87  ? 10  VAL   B CA  1 
ATOM   3068 C C   . VAL   B 1 10  ? 28.933 -9.323  36.084  1.00 41.97  ? 10  VAL   B C   1 
ATOM   3069 O O   . VAL   B 1 10  ? 28.640 -8.520  36.967  1.00 41.52  ? 10  VAL   B O   1 
ATOM   3070 C CB  . VAL   B 1 10  ? 26.885 -10.806 35.701  1.00 42.71  ? 10  VAL   B CB  1 
ATOM   3071 C CG1 . VAL   B 1 10  ? 26.592 -9.841  34.541  1.00 42.02  ? 10  VAL   B CG1 1 
ATOM   3072 C CG2 . VAL   B 1 10  ? 26.470 -12.230 35.334  1.00 42.26  ? 10  VAL   B CG2 1 
ATOM   3073 N N   . VAL   B 1 11  ? 29.731 -9.008  35.044  1.00 36.74  ? 11  VAL   B N   1 
ATOM   3074 C CA  . VAL   B 1 11  ? 30.241 -7.650  34.842  1.00 35.61  ? 11  VAL   B CA  1 
ATOM   3075 C C   . VAL   B 1 11  ? 29.263 -6.945  33.872  1.00 38.20  ? 11  VAL   B C   1 
ATOM   3076 O O   . VAL   B 1 11  ? 29.045 -7.415  32.758  1.00 38.11  ? 11  VAL   B O   1 
ATOM   3077 C CB  . VAL   B 1 11  ? 31.721 -7.597  34.374  1.00 38.97  ? 11  VAL   B CB  1 
ATOM   3078 C CG1 . VAL   B 1 11  ? 32.147 -6.163  33.991  1.00 38.40  ? 11  VAL   B CG1 1 
ATOM   3079 C CG2 . VAL   B 1 11  ? 32.650 -8.185  35.439  1.00 37.99  ? 11  VAL   B CG2 1 
ATOM   3080 N N   . GLU   B 1 12  ? 28.645 -5.865  34.333  1.00 33.58  ? 12  GLU   B N   1 
ATOM   3081 C CA  . GLU   B 1 12  ? 27.682 -5.061  33.588  1.00 33.77  ? 12  GLU   B CA  1 
ATOM   3082 C C   . GLU   B 1 12  ? 28.262 -3.664  33.312  1.00 38.40  ? 12  GLU   B C   1 
ATOM   3083 O O   . GLU   B 1 12  ? 28.802 -3.032  34.238  1.00 39.67  ? 12  GLU   B O   1 
ATOM   3084 C CB  . GLU   B 1 12  ? 26.408 -4.891  34.423  1.00 35.30  ? 12  GLU   B CB  1 
ATOM   3085 C CG  . GLU   B 1 12  ? 25.318 -4.132  33.689  1.00 46.29  ? 12  GLU   B CG  1 
ATOM   3086 C CD  . GLU   B 1 12  ? 24.761 -2.890  34.348  1.00 54.97  ? 12  GLU   B CD  1 
ATOM   3087 O OE1 . GLU   B 1 12  ? 25.130 -2.591  35.505  1.00 44.75  ? 12  GLU   B OE1 1 
ATOM   3088 O OE2 . GLU   B 1 12  ? 23.940 -2.210  33.693  1.00 49.40  ? 12  GLU   B OE2 1 
ATOM   3089 N N   . MET   B 1 13  ? 28.124 -3.176  32.057  1.00 32.85  ? 13  MET   B N   1 
ATOM   3090 C CA  . MET   B 1 13  ? 28.614 -1.855  31.650  1.00 31.64  ? 13  MET   B CA  1 
ATOM   3091 C C   . MET   B 1 13  ? 27.473 -0.996  31.139  1.00 37.11  ? 13  MET   B C   1 
ATOM   3092 O O   . MET   B 1 13  ? 26.805 -1.406  30.193  1.00 37.11  ? 13  MET   B O   1 
ATOM   3093 C CB  . MET   B 1 13  ? 29.749 -1.970  30.624  1.00 33.31  ? 13  MET   B CB  1 
ATOM   3094 C CG  . MET   B 1 13  ? 31.044 -2.536  31.213  1.00 36.63  ? 13  MET   B CG  1 
ATOM   3095 S SD  . MET   B 1 13  ? 31.946 -3.635  30.065  1.00 40.80  ? 13  MET   B SD  1 
ATOM   3096 C CE  . MET   B 1 13  ? 30.961 -5.162  30.231  1.00 35.52  ? 13  MET   B CE  1 
ATOM   3097 N N   . GLN   B 1 14  ? 27.204 0.167   31.793  1.00 34.28  ? 14  GLN   B N   1 
ATOM   3098 C CA  . GLN   B 1 14  ? 26.125 1.072   31.358  1.00 34.09  ? 14  GLN   B CA  1 
ATOM   3099 C C   . GLN   B 1 14  ? 26.661 1.944   30.258  1.00 37.66  ? 14  GLN   B C   1 
ATOM   3100 O O   . GLN   B 1 14  ? 27.845 2.260   30.265  1.00 37.33  ? 14  GLN   B O   1 
ATOM   3101 C CB  . GLN   B 1 14  ? 25.551 1.941   32.483  1.00 35.64  ? 14  GLN   B CB  1 
ATOM   3102 C CG  . GLN   B 1 14  ? 24.737 1.179   33.522  1.00 56.90  ? 14  GLN   B CG  1 
ATOM   3103 C CD  . GLN   B 1 14  ? 25.270 1.435   34.919  1.00 77.74  ? 14  GLN   B CD  1 
ATOM   3104 O OE1 . GLN   B 1 14  ? 25.184 2.545   35.454  1.00 69.75  ? 14  GLN   B OE1 1 
ATOM   3105 N NE2 . GLN   B 1 14  ? 25.838 0.414   35.544  1.00 74.78  ? 14  GLN   B NE2 1 
ATOM   3106 N N   . GLY   B 1 15  ? 25.792 2.317   29.320  1.00 33.62  ? 15  GLY   B N   1 
ATOM   3107 C CA  . GLY   B 1 15  ? 26.187 3.105   28.176  1.00 32.30  ? 15  GLY   B CA  1 
ATOM   3108 C C   . GLY   B 1 15  ? 25.558 4.457   28.045  1.00 37.83  ? 15  GLY   B C   1 
ATOM   3109 O O   . GLY   B 1 15  ? 25.328 5.165   29.034  1.00 38.25  ? 15  GLY   B O   1 
ATOM   3110 N N   . ASP   B 1 16  ? 25.302 4.828   26.795  1.00 33.40  ? 16  ASP   B N   1 
ATOM   3111 C CA  . ASP   B 1 16  ? 24.798 6.138   26.479  1.00 32.64  ? 16  ASP   B CA  1 
ATOM   3112 C C   . ASP   B 1 16  ? 23.492 6.170   25.735  1.00 37.50  ? 16  ASP   B C   1 
ATOM   3113 O O   . ASP   B 1 16  ? 23.085 5.177   25.115  1.00 36.32  ? 16  ASP   B O   1 
ATOM   3114 C CB  . ASP   B 1 16  ? 25.839 6.859   25.595  1.00 33.33  ? 16  ASP   B CB  1 
ATOM   3115 C CG  . ASP   B 1 16  ? 27.196 7.106   26.209  1.00 36.61  ? 16  ASP   B CG  1 
ATOM   3116 O OD1 . ASP   B 1 16  ? 27.300 7.986   27.075  1.00 38.06  ? 16  ASP   B OD1 1 
ATOM   3117 O OD2 . ASP   B 1 16  ? 28.161 6.439   25.800  1.00 39.67  ? 16  ASP   B OD2 1 
ATOM   3118 N N   . GLU   B 1 17  ? 22.890 7.385   25.739  1.00 33.90  ? 17  GLU   B N   1 
ATOM   3119 C CA  . GLU   B 1 17  ? 21.693 7.789   25.011  1.00 34.27  ? 17  GLU   B CA  1 
ATOM   3120 C C   . GLU   B 1 17  ? 20.517 6.827   25.088  1.00 39.98  ? 17  GLU   B C   1 
ATOM   3121 O O   . GLU   B 1 17  ? 20.191 6.415   26.186  1.00 41.34  ? 17  GLU   B O   1 
ATOM   3122 C CB  . GLU   B 1 17  ? 22.069 8.212   23.570  1.00 35.36  ? 17  GLU   B CB  1 
ATOM   3123 C CG  . GLU   B 1 17  ? 23.102 9.342   23.570  1.00 36.72  ? 17  GLU   B CG  1 
ATOM   3124 C CD  . GLU   B 1 17  ? 23.670 9.784   22.239  1.00 51.33  ? 17  GLU   B CD  1 
ATOM   3125 O OE1 . GLU   B 1 17  ? 23.681 8.977   21.283  1.00 48.96  ? 17  GLU   B OE1 1 
ATOM   3126 O OE2 . GLU   B 1 17  ? 24.108 10.950  22.153  1.00 56.80  ? 17  GLU   B OE2 1 
ATOM   3127 N N   . MET   B 1 18  ? 19.873 6.481   23.956  1.00 37.37  ? 18  MET   B N   1 
ATOM   3128 C CA  . MET   B 1 18  ? 18.710 5.598   23.931  1.00 37.20  ? 18  MET   B CA  1 
ATOM   3129 C C   . MET   B 1 18  ? 18.962 4.224   24.535  1.00 39.72  ? 18  MET   B C   1 
ATOM   3130 O O   . MET   B 1 18  ? 18.105 3.722   25.262  1.00 39.54  ? 18  MET   B O   1 
ATOM   3131 C CB  . MET   B 1 18  ? 18.064 5.531   22.528  1.00 39.82  ? 18  MET   B CB  1 
ATOM   3132 C CG  . MET   B 1 18  ? 16.592 5.074   22.540  1.00 42.50  ? 18  MET   B CG  1 
ATOM   3133 S SD  . MET   B 1 18  ? 15.493 6.210   23.418  1.00 46.38  ? 18  MET   B SD  1 
ATOM   3134 C CE  . MET   B 1 18  ? 14.234 5.036   24.061  1.00 42.88  ? 18  MET   B CE  1 
ATOM   3135 N N   . THR   B 1 19  ? 20.147 3.644   24.276  1.00 35.79  ? 19  THR   B N   1 
ATOM   3136 C CA  . THR   B 1 19  ? 20.555 2.336   24.802  1.00 34.83  ? 19  THR   B CA  1 
ATOM   3137 C C   . THR   B 1 19  ? 20.660 2.326   26.312  1.00 39.44  ? 19  THR   B C   1 
ATOM   3138 O O   . THR   B 1 19  ? 20.344 1.307   26.918  1.00 40.48  ? 19  THR   B O   1 
ATOM   3139 C CB  . THR   B 1 19  ? 21.716 1.740   24.010  1.00 43.27  ? 19  THR   B CB  1 
ATOM   3140 O OG1 . THR   B 1 19  ? 22.779 2.700   23.903  1.00 38.82  ? 19  THR   B OG1 1 
ATOM   3141 C CG2 . THR   B 1 19  ? 21.272 1.269   22.609  1.00 40.59  ? 19  THR   B CG2 1 
ATOM   3142 N N   . ARG   B 1 20  ? 21.041 3.468   26.931  1.00 35.58  ? 20  ARG   B N   1 
ATOM   3143 C CA  . ARG   B 1 20  ? 21.096 3.611   28.383  1.00 35.35  ? 20  ARG   B CA  1 
ATOM   3144 C C   . ARG   B 1 20  ? 19.661 3.481   28.962  1.00 41.04  ? 20  ARG   B C   1 
ATOM   3145 O O   . ARG   B 1 20  ? 19.478 2.810   29.979  1.00 42.19  ? 20  ARG   B O   1 
ATOM   3146 C CB  . ARG   B 1 20  ? 21.735 4.943   28.792  1.00 33.78  ? 20  ARG   B CB  1 
ATOM   3147 C CG  . ARG   B 1 20  ? 21.766 5.152   30.313  1.00 36.35  ? 20  ARG   B CG  1 
ATOM   3148 C CD  . ARG   B 1 20  ? 22.440 6.441   30.728  1.00 45.97  ? 20  ARG   B CD  1 
ATOM   3149 N NE  . ARG   B 1 20  ? 23.880 6.231   30.821  1.00 66.43  ? 20  ARG   B NE  1 
ATOM   3150 C CZ  . ARG   B 1 20  ? 24.541 5.912   31.933  1.00 74.43  ? 20  ARG   B CZ  1 
ATOM   3151 N NH1 . ARG   B 1 20  ? 23.900 5.802   33.092  1.00 48.26  ? 20  ARG   B NH1 1 
ATOM   3152 N NH2 . ARG   B 1 20  ? 25.846 5.717   31.896  1.00 61.18  ? 20  ARG   B NH2 1 
ATOM   3153 N N   . ILE   B 1 21  ? 18.650 4.067   28.291  1.00 38.13  ? 21  ILE   B N   1 
ATOM   3154 C CA  . ILE   B 1 21  ? 17.244 3.991   28.739  1.00 38.44  ? 21  ILE   B CA  1 
ATOM   3155 C C   . ILE   B 1 21  ? 16.711 2.545   28.653  1.00 44.25  ? 21  ILE   B C   1 
ATOM   3156 O O   . ILE   B 1 21  ? 16.285 2.008   29.673  1.00 44.81  ? 21  ILE   B O   1 
ATOM   3157 C CB  . ILE   B 1 21  ? 16.366 5.044   28.001  1.00 41.06  ? 21  ILE   B CB  1 
ATOM   3158 C CG1 . ILE   B 1 21  ? 16.737 6.473   28.439  1.00 40.66  ? 21  ILE   B CG1 1 
ATOM   3159 C CG2 . ILE   B 1 21  ? 14.857 4.771   28.134  1.00 40.60  ? 21  ILE   B CG2 1 
ATOM   3160 C CD1 . ILE   B 1 21  ? 16.682 7.459   27.297  1.00 49.29  ? 21  ILE   B CD1 1 
ATOM   3161 N N   . ILE   B 1 22  ? 16.787 1.911   27.462  1.00 41.20  ? 22  ILE   B N   1 
ATOM   3162 C CA  . ILE   B 1 22  ? 16.327 0.540   27.258  1.00 42.39  ? 22  ILE   B CA  1 
ATOM   3163 C C   . ILE   B 1 22  ? 17.019 -0.504  28.163  1.00 44.53  ? 22  ILE   B C   1 
ATOM   3164 O O   . ILE   B 1 22  ? 16.349 -1.416  28.658  1.00 46.03  ? 22  ILE   B O   1 
ATOM   3165 C CB  . ILE   B 1 22  ? 16.179 0.116   25.764  1.00 46.99  ? 22  ILE   B CB  1 
ATOM   3166 C CG1 . ILE   B 1 22  ? 17.517 -0.049  25.076  1.00 48.46  ? 22  ILE   B CG1 1 
ATOM   3167 C CG2 . ILE   B 1 22  ? 15.254 1.056   24.954  1.00 47.59  ? 22  ILE   B CG2 1 
ATOM   3168 C CD1 . ILE   B 1 22  ? 17.639 -1.357  24.518  1.00 61.91  ? 22  ILE   B CD1 1 
ATOM   3169 N N   . TRP   B 1 23  ? 18.343 -0.345  28.400  1.00 36.01  ? 23  TRP   B N   1 
ATOM   3170 C CA  . TRP   B 1 23  ? 19.162 -1.196  29.261  1.00 32.85  ? 23  TRP   B CA  1 
ATOM   3171 C C   . TRP   B 1 23  ? 18.602 -1.197  30.698  1.00 36.81  ? 23  TRP   B C   1 
ATOM   3172 O O   . TRP   B 1 23  ? 18.514 -2.252  31.315  1.00 36.35  ? 23  TRP   B O   1 
ATOM   3173 C CB  . TRP   B 1 23  ? 20.595 -0.651  29.255  1.00 30.24  ? 23  TRP   B CB  1 
ATOM   3174 C CG  . TRP   B 1 23  ? 21.653 -1.535  29.850  1.00 29.80  ? 23  TRP   B CG  1 
ATOM   3175 C CD1 . TRP   B 1 23  ? 22.214 -1.427  31.091  1.00 31.86  ? 23  TRP   B CD1 1 
ATOM   3176 C CD2 . TRP   B 1 23  ? 22.341 -2.611  29.187  1.00 29.58  ? 23  TRP   B CD2 1 
ATOM   3177 N NE1 . TRP   B 1 23  ? 23.210 -2.368  31.245  1.00 30.99  ? 23  TRP   B NE1 1 
ATOM   3178 C CE2 . TRP   B 1 23  ? 23.314 -3.105  30.089  1.00 32.87  ? 23  TRP   B CE2 1 
ATOM   3179 C CE3 . TRP   B 1 23  ? 22.248 -3.185  27.899  1.00 31.02  ? 23  TRP   B CE3 1 
ATOM   3180 C CZ2 . TRP   B 1 23  ? 24.159 -4.177  29.765  1.00 32.74  ? 23  TRP   B CZ2 1 
ATOM   3181 C CZ3 . TRP   B 1 23  ? 23.099 -4.232  27.566  1.00 33.26  ? 23  TRP   B CZ3 1 
ATOM   3182 C CH2 . TRP   B 1 23  ? 24.043 -4.720  28.491  1.00 34.04  ? 23  TRP   B CH2 1 
ATOM   3183 N N   . GLU   B 1 24  ? 18.232 -0.023  31.231  1.00 35.10  ? 24  GLU   B N   1 
ATOM   3184 C CA  . GLU   B 1 24  ? 17.648 0.077   32.573  1.00 36.51  ? 24  GLU   B CA  1 
ATOM   3185 C C   . GLU   B 1 24  ? 16.291 -0.606  32.609  1.00 39.16  ? 24  GLU   B C   1 
ATOM   3186 O O   . GLU   B 1 24  ? 15.974 -1.268  33.601  1.00 37.86  ? 24  GLU   B O   1 
ATOM   3187 C CB  . GLU   B 1 24  ? 17.522 1.541   33.029  1.00 38.79  ? 24  GLU   B CB  1 
ATOM   3188 C CG  . GLU   B 1 24  ? 18.852 2.121   33.510  1.00 55.16  ? 24  GLU   B CG  1 
ATOM   3189 C CD  . GLU   B 1 24  ? 19.561 1.370   34.628  1.00 77.26  ? 24  GLU   B CD  1 
ATOM   3190 O OE1 . GLU   B 1 24  ? 20.789 1.142   34.504  1.00 59.02  ? 24  GLU   B OE1 1 
ATOM   3191 O OE2 . GLU   B 1 24  ? 18.889 1.011   35.625  1.00 71.67  ? 24  GLU   B OE2 1 
ATOM   3192 N N   . LEU   B 1 25  ? 15.510 -0.468  31.508  1.00 35.76  ? 25  LEU   B N   1 
ATOM   3193 C CA  . LEU   B 1 25  ? 14.208 -1.104  31.355  1.00 36.47  ? 25  LEU   B CA  1 
ATOM   3194 C C   . LEU   B 1 25  ? 14.365 -2.623  31.324  1.00 41.92  ? 25  LEU   B C   1 
ATOM   3195 O O   . LEU   B 1 25  ? 13.535 -3.327  31.889  1.00 42.47  ? 25  LEU   B O   1 
ATOM   3196 C CB  . LEU   B 1 25  ? 13.484 -0.614  30.102  1.00 36.59  ? 25  LEU   B CB  1 
ATOM   3197 C CG  . LEU   B 1 25  ? 12.980 0.816   30.121  1.00 40.80  ? 25  LEU   B CG  1 
ATOM   3198 C CD1 . LEU   B 1 25  ? 12.374 1.177   28.791  1.00 40.95  ? 25  LEU   B CD1 1 
ATOM   3199 C CD2 . LEU   B 1 25  ? 11.978 1.040   31.242  1.00 41.34  ? 25  LEU   B CD2 1 
ATOM   3200 N N   . ILE   B 1 26  ? 15.450 -3.122  30.702  1.00 38.41  ? 26  ILE   B N   1 
ATOM   3201 C CA  . ILE   B 1 26  ? 15.759 -4.554  30.628  1.00 37.26  ? 26  ILE   B CA  1 
ATOM   3202 C C   . ILE   B 1 26  ? 16.047 -5.072  32.039  1.00 43.21  ? 26  ILE   B C   1 
ATOM   3203 O O   . ILE   B 1 26  ? 15.449 -6.057  32.468  1.00 42.56  ? 26  ILE   B O   1 
ATOM   3204 C CB  . ILE   B 1 26  ? 16.906 -4.817  29.617  1.00 38.85  ? 26  ILE   B CB  1 
ATOM   3205 C CG1 . ILE   B 1 26  ? 16.382 -4.664  28.176  1.00 37.85  ? 26  ILE   B CG1 1 
ATOM   3206 C CG2 . ILE   B 1 26  ? 17.571 -6.197  29.849  1.00 39.58  ? 26  ILE   B CG2 1 
ATOM   3207 C CD1 . ILE   B 1 26  ? 17.411 -4.498  27.151  1.00 38.75  ? 26  ILE   B CD1 1 
ATOM   3208 N N   . LYS   B 1 27  ? 16.937 -4.387  32.771  1.00 41.36  ? 27  LYS   B N   1 
ATOM   3209 C CA  . LYS   B 1 27  ? 17.284 -4.775  34.135  1.00 41.42  ? 27  LYS   B CA  1 
ATOM   3210 C C   . LYS   B 1 27  ? 16.071 -4.685  35.085  1.00 45.01  ? 27  LYS   B C   1 
ATOM   3211 O O   . LYS   B 1 27  ? 15.849 -5.579  35.882  1.00 43.46  ? 27  LYS   B O   1 
ATOM   3212 C CB  . LYS   B 1 27  ? 18.431 -3.907  34.664  1.00 43.57  ? 27  LYS   B CB  1 
ATOM   3213 C CG  . LYS   B 1 27  ? 19.718 -3.992  33.856  1.00 42.17  ? 27  LYS   B CG  1 
ATOM   3214 C CD  . LYS   B 1 27  ? 20.902 -3.487  34.669  1.00 38.61  ? 27  LYS   B CD  1 
ATOM   3215 C CE  . LYS   B 1 27  ? 20.850 -2.001  34.803  1.00 32.86  ? 27  LYS   B CE  1 
ATOM   3216 N NZ  . LYS   B 1 27  ? 21.980 -1.457  35.591  1.00 46.81  ? 27  LYS   B NZ  1 
ATOM   3217 N N   . GLU   B 1 28  ? 15.299 -3.617  34.986  1.00 43.56  ? 28  GLU   B N   1 
ATOM   3218 C CA  . GLU   B 1 28  ? 14.130 -3.391  35.837  1.00 44.60  ? 28  GLU   B CA  1 
ATOM   3219 C C   . GLU   B 1 28  ? 12.982 -4.365  35.557  1.00 47.98  ? 28  GLU   B C   1 
ATOM   3220 O O   . GLU   B 1 28  ? 12.406 -4.904  36.500  1.00 48.09  ? 28  GLU   B O   1 
ATOM   3221 C CB  . GLU   B 1 28  ? 13.660 -1.911  35.704  1.00 46.23  ? 28  GLU   B CB  1 
ATOM   3222 C CG  . GLU   B 1 28  ? 12.337 -1.546  36.360  1.00 61.19  ? 28  GLU   B CG  1 
ATOM   3223 C CD  . GLU   B 1 28  ? 11.641 -0.337  35.754  1.00 98.90  ? 28  GLU   B CD  1 
ATOM   3224 O OE1 . GLU   B 1 28  ? 11.842 0.787   36.270  1.00 104.76 ? 28  GLU   B OE1 1 
ATOM   3225 O OE2 . GLU   B 1 28  ? 10.892 -0.512  34.765  1.00 97.09  ? 28  GLU   B OE2 1 
ATOM   3226 N N   . LYS   B 1 29  ? 12.637 -4.560  34.281  1.00 42.77  ? 29  LYS   B N   1 
ATOM   3227 C CA  . LYS   B 1 29  ? 11.498 -5.386  33.876  1.00 41.79  ? 29  LYS   B CA  1 
ATOM   3228 C C   . LYS   B 1 29  ? 11.767 -6.839  33.572  1.00 45.50  ? 29  LYS   B C   1 
ATOM   3229 O O   . LYS   B 1 29  ? 10.873 -7.666  33.749  1.00 45.23  ? 29  LYS   B O   1 
ATOM   3230 C CB  . LYS   B 1 29  ? 10.756 -4.736  32.685  1.00 43.00  ? 29  LYS   B CB  1 
ATOM   3231 C CG  . LYS   B 1 29  ? 10.231 -3.350  33.010  1.00 47.60  ? 29  LYS   B CG  1 
ATOM   3232 C CD  . LYS   B 1 29  ? 9.508  -2.708  31.860  1.00 58.86  ? 29  LYS   B CD  1 
ATOM   3233 C CE  . LYS   B 1 29  ? 8.275  -1.964  32.327  1.00 72.98  ? 29  LYS   B CE  1 
ATOM   3234 N NZ  . LYS   B 1 29  ? 8.573  -0.824  33.243  1.00 79.50  ? 29  LYS   B NZ  1 
ATOM   3235 N N   . LEU   B 1 30  ? 12.969 -7.160  33.088  1.00 41.13  ? 30  LEU   B N   1 
ATOM   3236 C CA  . LEU   B 1 30  ? 13.278 -8.520  32.687  1.00 39.19  ? 30  LEU   B CA  1 
ATOM   3237 C C   . LEU   B 1 30  ? 14.306 -9.271  33.496  1.00 43.33  ? 30  LEU   B C   1 
ATOM   3238 O O   . LEU   B 1 30  ? 14.216 -10.500 33.545  1.00 43.03  ? 30  LEU   B O   1 
ATOM   3239 C CB  . LEU   B 1 30  ? 13.664 -8.551  31.197  1.00 38.54  ? 30  LEU   B CB  1 
ATOM   3240 C CG  . LEU   B 1 30  ? 12.844 -7.733  30.184  1.00 41.65  ? 30  LEU   B CG  1 
ATOM   3241 C CD1 . LEU   B 1 30  ? 13.464 -7.849  28.785  1.00 41.04  ? 30  LEU   B CD1 1 
ATOM   3242 C CD2 . LEU   B 1 30  ? 11.407 -8.200  30.124  1.00 44.85  ? 30  LEU   B CD2 1 
ATOM   3243 N N   . ILE   B 1 31  ? 15.291 -8.586  34.114  1.00 39.88  ? 31  ILE   B N   1 
ATOM   3244 C CA  . ILE   B 1 31  ? 16.331 -9.321  34.849  1.00 39.12  ? 31  ILE   B CA  1 
ATOM   3245 C C   . ILE   B 1 31  ? 16.129 -9.372  36.344  1.00 44.30  ? 31  ILE   B C   1 
ATOM   3246 O O   . ILE   B 1 31  ? 15.958 -10.459 36.913  1.00 44.01  ? 31  ILE   B O   1 
ATOM   3247 C CB  . ILE   B 1 31  ? 17.792 -8.907  34.444  1.00 41.07  ? 31  ILE   B CB  1 
ATOM   3248 C CG1 . ILE   B 1 31  ? 18.008 -8.806  32.903  1.00 40.82  ? 31  ILE   B CG1 1 
ATOM   3249 C CG2 . ILE   B 1 31  ? 18.857 -9.764  35.130  1.00 40.69  ? 31  ILE   B CG2 1 
ATOM   3250 C CD1 . ILE   B 1 31  ? 17.940 -10.092 32.083  1.00 47.83  ? 31  ILE   B CD1 1 
ATOM   3251 N N   . PHE   B 1 32  ? 16.182 -8.191  36.980  1.00 40.72  ? 32  PHE   B N   1 
ATOM   3252 C CA  . PHE   B 1 32  ? 16.052 -7.997  38.422  1.00 39.36  ? 32  PHE   B CA  1 
ATOM   3253 C C   . PHE   B 1 32  ? 14.816 -8.623  39.065  1.00 44.74  ? 32  PHE   B C   1 
ATOM   3254 O O   . PHE   B 1 32  ? 14.972 -9.200  40.141  1.00 46.19  ? 32  PHE   B O   1 
ATOM   3255 C CB  . PHE   B 1 32  ? 16.289 -6.538  38.823  1.00 40.17  ? 32  PHE   B CB  1 
ATOM   3256 C CG  . PHE   B 1 32  ? 17.687 -6.006  38.577  1.00 41.02  ? 32  PHE   B CG  1 
ATOM   3257 C CD1 . PHE   B 1 32  ? 17.978 -4.661  38.764  1.00 43.46  ? 32  PHE   B CD1 1 
ATOM   3258 C CD2 . PHE   B 1 32  ? 18.722 -6.856  38.182  1.00 42.95  ? 32  PHE   B CD2 1 
ATOM   3259 C CE1 . PHE   B 1 32  ? 19.278 -4.173  38.574  1.00 44.39  ? 32  PHE   B CE1 1 
ATOM   3260 C CE2 . PHE   B 1 32  ? 20.015 -6.364  37.965  1.00 45.82  ? 32  PHE   B CE2 1 
ATOM   3261 C CZ  . PHE   B 1 32  ? 20.285 -5.026  38.166  1.00 43.92  ? 32  PHE   B CZ  1 
ATOM   3262 N N   . PRO   B 1 33  ? 13.614 -8.649  38.448  1.00 40.66  ? 33  PRO   B N   1 
ATOM   3263 C CA  . PRO   B 1 33  ? 12.487 -9.333  39.118  1.00 40.31  ? 33  PRO   B CA  1 
ATOM   3264 C C   . PRO   B 1 33  ? 12.657 -10.850 39.280  1.00 46.89  ? 33  PRO   B C   1 
ATOM   3265 O O   . PRO   B 1 33  ? 11.865 -11.450 39.994  1.00 48.71  ? 33  PRO   B O   1 
ATOM   3266 C CB  . PRO   B 1 33  ? 11.285 -9.022  38.213  1.00 41.26  ? 33  PRO   B CB  1 
ATOM   3267 C CG  . PRO   B 1 33  ? 11.708 -7.893  37.362  1.00 45.28  ? 33  PRO   B CG  1 
ATOM   3268 C CD  . PRO   B 1 33  ? 13.180 -8.047  37.170  1.00 41.09  ? 33  PRO   B CD  1 
ATOM   3269 N N   . TYR   B 1 34  ? 13.688 -11.468 38.647  1.00 43.12  ? 34  TYR   B N   1 
ATOM   3270 C CA  . TYR   B 1 34  ? 13.941 -12.923 38.651  1.00 41.46  ? 34  TYR   B CA  1 
ATOM   3271 C C   . TYR   B 1 34  ? 15.339 -13.357 39.020  1.00 46.83  ? 34  TYR   B C   1 
ATOM   3272 O O   . TYR   B 1 34  ? 15.512 -14.500 39.475  1.00 47.43  ? 34  TYR   B O   1 
ATOM   3273 C CB  . TYR   B 1 34  ? 13.632 -13.502 37.253  1.00 40.77  ? 34  TYR   B CB  1 
ATOM   3274 C CG  . TYR   B 1 34  ? 12.261 -13.112 36.762  1.00 41.72  ? 34  TYR   B CG  1 
ATOM   3275 C CD1 . TYR   B 1 34  ? 12.100 -12.114 35.804  1.00 42.21  ? 34  TYR   B CD1 1 
ATOM   3276 C CD2 . TYR   B 1 34  ? 11.112 -13.680 37.315  1.00 42.81  ? 34  TYR   B CD2 1 
ATOM   3277 C CE1 . TYR   B 1 34  ? 10.829 -11.712 35.387  1.00 41.86  ? 34  TYR   B CE1 1 
ATOM   3278 C CE2 . TYR   B 1 34  ? 9.839  -13.293 36.897  1.00 43.58  ? 34  TYR   B CE2 1 
ATOM   3279 C CZ  . TYR   B 1 34  ? 9.701  -12.312 35.932  1.00 48.62  ? 34  TYR   B CZ  1 
ATOM   3280 O OH  . TYR   B 1 34  ? 8.437  -11.959 35.528  1.00 50.89  ? 34  TYR   B OH  1 
ATOM   3281 N N   . VAL   B 1 35  ? 16.347 -12.497 38.757  1.00 42.26  ? 35  VAL   B N   1 
ATOM   3282 C CA  . VAL   B 1 35  ? 17.750 -12.847 39.009  1.00 41.46  ? 35  VAL   B CA  1 
ATOM   3283 C C   . VAL   B 1 35  ? 18.454 -11.881 39.967  1.00 46.19  ? 35  VAL   B C   1 
ATOM   3284 O O   . VAL   B 1 35  ? 18.389 -10.660 39.819  1.00 46.16  ? 35  VAL   B O   1 
ATOM   3285 C CB  . VAL   B 1 35  ? 18.573 -13.047 37.682  1.00 43.76  ? 35  VAL   B CB  1 
ATOM   3286 C CG1 . VAL   B 1 35  ? 19.884 -13.775 37.930  1.00 42.83  ? 35  VAL   B CG1 1 
ATOM   3287 C CG2 . VAL   B 1 35  ? 17.769 -13.786 36.618  1.00 43.57  ? 35  VAL   B CG2 1 
ATOM   3288 N N   . GLU   B 1 36  ? 19.148 -12.460 40.935  1.00 42.69  ? 36  GLU   B N   1 
ATOM   3289 C CA  . GLU   B 1 36  ? 19.968 -11.755 41.901  1.00 41.75  ? 36  GLU   B CA  1 
ATOM   3290 C C   . GLU   B 1 36  ? 21.380 -12.059 41.422  1.00 43.48  ? 36  GLU   B C   1 
ATOM   3291 O O   . GLU   B 1 36  ? 21.748 -13.227 41.203  1.00 41.06  ? 36  GLU   B O   1 
ATOM   3292 C CB  . GLU   B 1 36  ? 19.742 -12.283 43.342  1.00 43.28  ? 36  GLU   B CB  1 
ATOM   3293 C CG  . GLU   B 1 36  ? 18.424 -11.859 43.983  1.00 53.41  ? 36  GLU   B CG  1 
ATOM   3294 C CD  . GLU   B 1 36  ? 18.218 -10.396 44.350  1.00 74.94  ? 36  GLU   B CD  1 
ATOM   3295 O OE1 . GLU   B 1 36  ? 17.269 -10.124 45.122  1.00 74.42  ? 36  GLU   B OE1 1 
ATOM   3296 O OE2 . GLU   B 1 36  ? 18.983 -9.524  43.870  1.00 64.27  ? 36  GLU   B OE2 1 
ATOM   3297 N N   . LEU   B 1 37  ? 22.164 -11.001 41.234  1.00 40.47  ? 37  LEU   B N   1 
ATOM   3298 C CA  . LEU   B 1 37  ? 23.535 -11.113 40.744  1.00 38.86  ? 37  LEU   B CA  1 
ATOM   3299 C C   . LEU   B 1 37  ? 24.496 -10.443 41.675  1.00 42.28  ? 37  LEU   B C   1 
ATOM   3300 O O   . LEU   B 1 37  ? 24.130 -9.483  42.364  1.00 40.67  ? 37  LEU   B O   1 
ATOM   3301 C CB  . LEU   B 1 37  ? 23.642 -10.427 39.353  1.00 37.77  ? 37  LEU   B CB  1 
ATOM   3302 C CG  . LEU   B 1 37  ? 22.809 -11.000 38.228  1.00 41.34  ? 37  LEU   B CG  1 
ATOM   3303 C CD1 . LEU   B 1 37  ? 22.624 -9.993  37.128  1.00 41.44  ? 37  LEU   B CD1 1 
ATOM   3304 C CD2 . LEU   B 1 37  ? 23.428 -12.289 37.682  1.00 43.75  ? 37  LEU   B CD2 1 
ATOM   3305 N N   . ASP   B 1 38  ? 25.740 -10.931 41.680  1.00 40.71  ? 38  ASP   B N   1 
ATOM   3306 C CA  . ASP   B 1 38  ? 26.840 -10.300 42.409  1.00 42.15  ? 38  ASP   B CA  1 
ATOM   3307 C C   . ASP   B 1 38  ? 27.321 -9.418  41.247  1.00 46.14  ? 38  ASP   B C   1 
ATOM   3308 O O   . ASP   B 1 38  ? 28.152 -9.819  40.419  1.00 44.25  ? 38  ASP   B O   1 
ATOM   3309 C CB  . ASP   B 1 38  ? 27.897 -11.330 42.865  1.00 44.74  ? 38  ASP   B CB  1 
ATOM   3310 C CG  . ASP   B 1 38  ? 27.453 -12.166 44.056  1.00 62.72  ? 38  ASP   B CG  1 
ATOM   3311 O OD1 . ASP   B 1 38  ? 26.898 -11.585 45.019  1.00 66.17  ? 38  ASP   B OD1 1 
ATOM   3312 O OD2 . ASP   B 1 38  ? 27.669 -13.396 44.032  1.00 70.61  ? 38  ASP   B OD2 1 
ATOM   3313 N N   . LEU   B 1 39  ? 26.662 -8.251  41.132  1.00 43.03  ? 39  LEU   B N   1 
ATOM   3314 C CA  . LEU   B 1 39  ? 26.851 -7.320  40.042  1.00 41.62  ? 39  LEU   B CA  1 
ATOM   3315 C C   . LEU   B 1 39  ? 28.005 -6.368  40.177  1.00 42.90  ? 39  LEU   B C   1 
ATOM   3316 O O   . LEU   B 1 39  ? 28.105 -5.632  41.156  1.00 41.86  ? 39  LEU   B O   1 
ATOM   3317 C CB  . LEU   B 1 39  ? 25.521 -6.633  39.687  1.00 41.30  ? 39  LEU   B CB  1 
ATOM   3318 C CG  . LEU   B 1 39  ? 25.367 -6.119  38.245  1.00 44.91  ? 39  LEU   B CG  1 
ATOM   3319 C CD1 . LEU   B 1 39  ? 25.330 -7.254  37.224  1.00 42.12  ? 39  LEU   B CD1 1 
ATOM   3320 C CD2 . LEU   B 1 39  ? 24.126 -5.229  38.124  1.00 47.06  ? 39  LEU   B CD2 1 
ATOM   3321 N N   . HIS   B 1 40  ? 28.899 -6.418  39.175  1.00 38.52  ? 40  HIS   B N   1 
ATOM   3322 C CA  . HIS   B 1 40  ? 30.086 -5.580  39.063  1.00 37.68  ? 40  HIS   B CA  1 
ATOM   3323 C C   . HIS   B 1 40  ? 29.708 -4.552  37.999  1.00 39.41  ? 40  HIS   B C   1 
ATOM   3324 O O   . HIS   B 1 40  ? 29.788 -4.828  36.798  1.00 38.73  ? 40  HIS   B O   1 
ATOM   3325 C CB  . HIS   B 1 40  ? 31.306 -6.425  38.664  1.00 38.93  ? 40  HIS   B CB  1 
ATOM   3326 C CG  . HIS   B 1 40  ? 31.591 -7.565  39.595  1.00 42.36  ? 40  HIS   B CG  1 
ATOM   3327 N ND1 . HIS   B 1 40  ? 31.005 -8.803  39.419  1.00 44.26  ? 40  HIS   B ND1 1 
ATOM   3328 C CD2 . HIS   B 1 40  ? 32.403 -7.621  40.673  1.00 43.79  ? 40  HIS   B CD2 1 
ATOM   3329 C CE1 . HIS   B 1 40  ? 31.473 -9.566  40.394  1.00 43.14  ? 40  HIS   B CE1 1 
ATOM   3330 N NE2 . HIS   B 1 40  ? 32.326 -8.902  41.167  1.00 43.39  ? 40  HIS   B NE2 1 
ATOM   3331 N N   . SER   B 1 41  ? 29.200 -3.394  38.445  1.00 35.51  ? 41  SER   B N   1 
ATOM   3332 C CA  . SER   B 1 41  ? 28.742 -2.353  37.527  1.00 35.22  ? 41  SER   B CA  1 
ATOM   3333 C C   . SER   B 1 41  ? 29.738 -1.273  37.313  1.00 38.60  ? 41  SER   B C   1 
ATOM   3334 O O   . SER   B 1 41  ? 30.426 -0.812  38.240  1.00 37.88  ? 41  SER   B O   1 
ATOM   3335 C CB  . SER   B 1 41  ? 27.392 -1.768  37.931  1.00 37.32  ? 41  SER   B CB  1 
ATOM   3336 O OG  . SER   B 1 41  ? 26.375 -2.744  37.829  1.00 42.31  ? 41  SER   B OG  1 
ATOM   3337 N N   . TYR   B 1 42  ? 29.829 -0.900  36.049  1.00 34.86  ? 42  TYR   B N   1 
ATOM   3338 C CA  . TYR   B 1 42  ? 30.713 0.120   35.553  1.00 33.95  ? 42  TYR   B CA  1 
ATOM   3339 C C   . TYR   B 1 42  ? 29.883 0.989   34.681  1.00 38.01  ? 42  TYR   B C   1 
ATOM   3340 O O   . TYR   B 1 42  ? 29.068 0.520   33.868  1.00 38.12  ? 42  TYR   B O   1 
ATOM   3341 C CB  . TYR   B 1 42  ? 31.939 -0.482  34.836  1.00 34.26  ? 42  TYR   B CB  1 
ATOM   3342 C CG  . TYR   B 1 42  ? 32.786 -1.297  35.788  1.00 34.04  ? 42  TYR   B CG  1 
ATOM   3343 C CD1 . TYR   B 1 42  ? 32.496 -2.636  36.034  1.00 36.13  ? 42  TYR   B CD1 1 
ATOM   3344 C CD2 . TYR   B 1 42  ? 33.840 -0.715  36.496  1.00 33.40  ? 42  TYR   B CD2 1 
ATOM   3345 C CE1 . TYR   B 1 42  ? 33.207 -3.372  36.982  1.00 36.65  ? 42  TYR   B CE1 1 
ATOM   3346 C CE2 . TYR   B 1 42  ? 34.588 -1.456  37.424  1.00 33.19  ? 42  TYR   B CE2 1 
ATOM   3347 C CZ  . TYR   B 1 42  ? 34.261 -2.788  37.658  1.00 42.51  ? 42  TYR   B CZ  1 
ATOM   3348 O OH  . TYR   B 1 42  ? 34.952 -3.582  38.537  1.00 48.38  ? 42  TYR   B OH  1 
ATOM   3349 N N   . ASP   B 1 43  ? 30.045 2.273   34.910  1.00 33.39  ? 43  ASP   B N   1 
ATOM   3350 C CA  . ASP   B 1 43  ? 29.320 3.281   34.193  1.00 33.10  ? 43  ASP   B CA  1 
ATOM   3351 C C   . ASP   B 1 43  ? 30.209 3.820   33.046  1.00 38.61  ? 43  ASP   B C   1 
ATOM   3352 O O   . ASP   B 1 43  ? 31.080 4.688   33.247  1.00 38.01  ? 43  ASP   B O   1 
ATOM   3353 C CB  . ASP   B 1 43  ? 28.863 4.360   35.182  1.00 33.79  ? 43  ASP   B CB  1 
ATOM   3354 C CG  . ASP   B 1 43  ? 27.994 5.400   34.555  1.00 37.58  ? 43  ASP   B CG  1 
ATOM   3355 O OD1 . ASP   B 1 43  ? 27.640 5.235   33.393  1.00 33.20  ? 43  ASP   B OD1 1 
ATOM   3356 O OD2 . ASP   B 1 43  ? 27.686 6.397   35.232  1.00 52.10  ? 43  ASP   B OD2 1 
ATOM   3357 N N   . LEU   B 1 44  ? 29.986 3.271   31.843  1.00 34.98  ? 44  LEU   B N   1 
ATOM   3358 C CA  . LEU   B 1 44  ? 30.749 3.673   30.663  1.00 34.47  ? 44  LEU   B CA  1 
ATOM   3359 C C   . LEU   B 1 44  ? 30.070 4.813   29.884  1.00 39.01  ? 44  LEU   B C   1 
ATOM   3360 O O   . LEU   B 1 44  ? 30.373 5.032   28.709  1.00 40.66  ? 44  LEU   B O   1 
ATOM   3361 C CB  . LEU   B 1 44  ? 31.148 2.470   29.752  1.00 33.71  ? 44  LEU   B CB  1 
ATOM   3362 C CG  . LEU   B 1 44  ? 31.912 1.270   30.372  1.00 37.00  ? 44  LEU   B CG  1 
ATOM   3363 C CD1 . LEU   B 1 44  ? 32.519 0.422   29.292  1.00 36.63  ? 44  LEU   B CD1 1 
ATOM   3364 C CD2 . LEU   B 1 44  ? 33.012 1.694   31.325  1.00 37.91  ? 44  LEU   B CD2 1 
ATOM   3365 N N   . GLY   B 1 45  ? 29.171 5.537   30.543  1.00 34.46  ? 45  GLY   B N   1 
ATOM   3366 C CA  . GLY   B 1 45  ? 28.509 6.701   29.950  1.00 33.73  ? 45  GLY   B CA  1 
ATOM   3367 C C   . GLY   B 1 45  ? 29.562 7.761   29.680  1.00 37.70  ? 45  GLY   B C   1 
ATOM   3368 O O   . GLY   B 1 45  ? 30.517 7.877   30.447  1.00 36.97  ? 45  GLY   B O   1 
ATOM   3369 N N   . ILE   B 1 46  ? 29.444 8.494   28.562  1.00 36.75  ? 46  ILE   B N   1 
ATOM   3370 C CA  . ILE   B 1 46  ? 30.414 9.514   28.142  1.00 36.73  ? 46  ILE   B CA  1 
ATOM   3371 C C   . ILE   B 1 46  ? 30.898 10.483  29.233  1.00 41.98  ? 46  ILE   B C   1 
ATOM   3372 O O   . ILE   B 1 46  ? 32.099 10.694  29.371  1.00 42.27  ? 46  ILE   B O   1 
ATOM   3373 C CB  . ILE   B 1 46  ? 30.006 10.196  26.814  1.00 39.55  ? 46  ILE   B CB  1 
ATOM   3374 C CG1 . ILE   B 1 46  ? 31.217 10.910  26.122  1.00 40.04  ? 46  ILE   B CG1 1 
ATOM   3375 C CG2 . ILE   B 1 46  ? 28.773 11.113  26.969  1.00 37.53  ? 46  ILE   B CG2 1 
ATOM   3376 C CD1 . ILE   B 1 46  ? 32.192 10.004  25.468  1.00 46.87  ? 46  ILE   B CD1 1 
ATOM   3377 N N   . GLU   B 1 47  ? 29.967 11.036  30.019  1.00 39.83  ? 47  GLU   B N   1 
ATOM   3378 C CA  . GLU   B 1 47  ? 30.267 11.978  31.104  1.00 39.04  ? 47  GLU   B CA  1 
ATOM   3379 C C   . GLU   B 1 47  ? 31.136 11.314  32.150  1.00 41.47  ? 47  GLU   B C   1 
ATOM   3380 O O   . GLU   B 1 47  ? 32.069 11.943  32.633  1.00 42.81  ? 47  GLU   B O   1 
ATOM   3381 C CB  . GLU   B 1 47  ? 28.979 12.565  31.722  1.00 40.14  ? 47  GLU   B CB  1 
ATOM   3382 C CG  . GLU   B 1 47  ? 28.050 13.260  30.730  1.00 45.46  ? 47  GLU   B CG  1 
ATOM   3383 N N   . ASN   B 1 48  ? 30.872 10.035  32.464  1.00 35.88  ? 48  ASN   B N   1 
ATOM   3384 C CA  . ASN   B 1 48  ? 31.674 9.308   33.441  1.00 34.57  ? 48  ASN   B CA  1 
ATOM   3385 C C   . ASN   B 1 48  ? 33.070 8.924   32.919  1.00 39.02  ? 48  ASN   B C   1 
ATOM   3386 O O   . ASN   B 1 48  ? 34.033 9.029   33.676  1.00 40.17  ? 48  ASN   B O   1 
ATOM   3387 C CB  . ASN   B 1 48  ? 30.914 8.152   34.078  1.00 33.03  ? 48  ASN   B CB  1 
ATOM   3388 C CG  . ASN   B 1 48  ? 31.583 7.643   35.333  1.00 45.40  ? 48  ASN   B CG  1 
ATOM   3389 O OD1 . ASN   B 1 48  ? 31.880 8.397   36.266  1.00 37.16  ? 48  ASN   B OD1 1 
ATOM   3390 N ND2 . ASN   B 1 48  ? 31.845 6.348   35.376  1.00 35.68  ? 48  ASN   B ND2 1 
ATOM   3391 N N   . ARG   B 1 49  ? 33.202 8.517   31.640  1.00 34.29  ? 49  ARG   B N   1 
ATOM   3392 C CA  . ARG   B 1 49  ? 34.517 8.212   31.050  1.00 33.70  ? 49  ARG   B CA  1 
ATOM   3393 C C   . ARG   B 1 49  ? 35.406 9.483   31.082  1.00 38.61  ? 49  ARG   B C   1 
ATOM   3394 O O   . ARG   B 1 49  ? 36.580 9.403   31.463  1.00 37.48  ? 49  ARG   B O   1 
ATOM   3395 C CB  . ARG   B 1 49  ? 34.382 7.681   29.609  1.00 30.74  ? 49  ARG   B CB  1 
ATOM   3396 C CG  . ARG   B 1 49  ? 34.078 6.190   29.532  1.00 28.06  ? 49  ARG   B CG  1 
ATOM   3397 C CD  . ARG   B 1 49  ? 33.888 5.761   28.089  1.00 37.54  ? 49  ARG   B CD  1 
ATOM   3398 N NE  . ARG   B 1 49  ? 32.539 6.015   27.585  1.00 36.28  ? 49  ARG   B NE  1 
ATOM   3399 C CZ  . ARG   B 1 49  ? 32.245 6.454   26.362  1.00 49.13  ? 49  ARG   B CZ  1 
ATOM   3400 N NH1 . ARG   B 1 49  ? 33.209 6.710   25.490  1.00 37.50  ? 49  ARG   B NH1 1 
ATOM   3401 N NH2 . ARG   B 1 49  ? 30.982 6.645   26.006  1.00 35.67  ? 49  ARG   B NH2 1 
ATOM   3402 N N   . ASP   B 1 50  ? 34.824 10.663  30.725  1.00 35.25  ? 50  ASP   B N   1 
ATOM   3403 C CA  . ASP   B 1 50  ? 35.537 11.944  30.767  1.00 34.91  ? 50  ASP   B CA  1 
ATOM   3404 C C   . ASP   B 1 50  ? 36.026 12.278  32.193  1.00 39.51  ? 50  ASP   B C   1 
ATOM   3405 O O   . ASP   B 1 50  ? 37.209 12.540  32.368  1.00 41.21  ? 50  ASP   B O   1 
ATOM   3406 C CB  . ASP   B 1 50  ? 34.658 13.095  30.215  1.00 36.24  ? 50  ASP   B CB  1 
ATOM   3407 C CG  . ASP   B 1 50  ? 35.415 14.374  29.862  1.00 44.90  ? 50  ASP   B CG  1 
ATOM   3408 O OD1 . ASP   B 1 50  ? 36.432 14.288  29.139  1.00 45.74  ? 50  ASP   B OD1 1 
ATOM   3409 O OD2 . ASP   B 1 50  ? 34.981 15.452  30.288  1.00 53.62  ? 50  ASP   B OD2 1 
ATOM   3410 N N   . ALA   B 1 51  ? 35.126 12.248  33.203  1.00 33.80  ? 51  ALA   B N   1 
ATOM   3411 C CA  . ALA   B 1 51  ? 35.442 12.563  34.611  1.00 32.43  ? 51  ALA   B CA  1 
ATOM   3412 C C   . ALA   B 1 51  ? 36.533 11.667  35.208  1.00 37.44  ? 51  ALA   B C   1 
ATOM   3413 O O   . ALA   B 1 51  ? 37.347 12.148  36.007  1.00 36.82  ? 51  ALA   B O   1 
ATOM   3414 C CB  . ALA   B 1 51  ? 34.179 12.472  35.459  1.00 32.24  ? 51  ALA   B CB  1 
ATOM   3415 N N   . THR   B 1 52  ? 36.542 10.365  34.822  1.00 33.28  ? 52  THR   B N   1 
ATOM   3416 C CA  . THR   B 1 52  ? 37.492 9.372   35.308  1.00 33.46  ? 52  THR   B CA  1 
ATOM   3417 C C   . THR   B 1 52  ? 38.747 9.259   34.428  1.00 40.08  ? 52  THR   B C   1 
ATOM   3418 O O   . THR   B 1 52  ? 39.601 8.406   34.698  1.00 40.89  ? 52  THR   B O   1 
ATOM   3419 C CB  . THR   B 1 52  ? 36.793 8.012   35.521  1.00 42.01  ? 52  THR   B CB  1 
ATOM   3420 O OG1 . THR   B 1 52  ? 36.489 7.426   34.258  1.00 44.70  ? 52  THR   B OG1 1 
ATOM   3421 C CG2 . THR   B 1 52  ? 35.519 8.110   36.381  1.00 38.94  ? 52  THR   B CG2 1 
ATOM   3422 N N   . ASN   B 1 53  ? 38.865 10.119  33.381  1.00 36.95  ? 53  ASN   B N   1 
ATOM   3423 C CA  . ASN   B 1 53  ? 39.976 10.118  32.405  1.00 36.20  ? 53  ASN   B CA  1 
ATOM   3424 C C   . ASN   B 1 53  ? 40.111 8.737   31.781  1.00 38.88  ? 53  ASN   B C   1 
ATOM   3425 O O   . ASN   B 1 53  ? 41.219 8.197   31.645  1.00 38.69  ? 53  ASN   B O   1 
ATOM   3426 C CB  . ASN   B 1 53  ? 41.298 10.648  33.011  1.00 34.11  ? 53  ASN   B CB  1 
ATOM   3427 C CG  . ASN   B 1 53  ? 41.160 12.084  33.405  1.00 49.74  ? 53  ASN   B CG  1 
ATOM   3428 O OD1 . ASN   B 1 53  ? 40.651 12.897  32.652  1.00 44.52  ? 53  ASN   B OD1 1 
ATOM   3429 N ND2 . ASN   B 1 53  ? 41.567 12.426  34.601  1.00 43.08  ? 53  ASN   B ND2 1 
ATOM   3430 N N   . ASP   B 1 54  ? 38.939 8.157   31.431  1.00 34.26  ? 54  ASP   B N   1 
ATOM   3431 C CA  . ASP   B 1 54  ? 38.767 6.836   30.825  1.00 34.68  ? 54  ASP   B CA  1 
ATOM   3432 C C   . ASP   B 1 54  ? 39.168 5.643   31.709  1.00 38.13  ? 54  ASP   B C   1 
ATOM   3433 O O   . ASP   B 1 54  ? 39.251 4.521   31.204  1.00 38.32  ? 54  ASP   B O   1 
ATOM   3434 C CB  . ASP   B 1 54  ? 39.404 6.759   29.416  1.00 36.66  ? 54  ASP   B CB  1 
ATOM   3435 C CG  . ASP   B 1 54  ? 38.670 5.834   28.454  1.00 46.03  ? 54  ASP   B CG  1 
ATOM   3436 O OD1 . ASP   B 1 54  ? 37.412 5.755   28.532  1.00 46.71  ? 54  ASP   B OD1 1 
ATOM   3437 O OD2 . ASP   B 1 54  ? 39.343 5.195   27.628  1.00 50.19  ? 54  ASP   B OD2 1 
ATOM   3438 N N   . GLN   B 1 55  ? 39.390 5.875   33.026  1.00 34.15  ? 55  GLN   B N   1 
ATOM   3439 C CA  . GLN   B 1 55  ? 39.787 4.830   33.969  1.00 33.71  ? 55  GLN   B CA  1 
ATOM   3440 C C   . GLN   B 1 55  ? 38.715 3.746   34.182  1.00 37.83  ? 55  GLN   B C   1 
ATOM   3441 O O   . GLN   B 1 55  ? 39.054 2.569   34.362  1.00 38.01  ? 55  GLN   B O   1 
ATOM   3442 C CB  . GLN   B 1 55  ? 40.287 5.433   35.289  1.00 34.45  ? 55  GLN   B CB  1 
ATOM   3443 C CG  . GLN   B 1 55  ? 41.011 4.440   36.204  1.00 37.93  ? 55  GLN   B CG  1 
ATOM   3444 C CD  . GLN   B 1 55  ? 42.148 3.716   35.520  1.00 52.10  ? 55  GLN   B CD  1 
ATOM   3445 O OE1 . GLN   B 1 55  ? 43.057 4.324   34.945  1.00 55.71  ? 55  GLN   B OE1 1 
ATOM   3446 N NE2 . GLN   B 1 55  ? 42.119 2.396   35.557  1.00 38.37  ? 55  GLN   B NE2 1 
ATOM   3447 N N   . VAL   B 1 56  ? 37.434 4.144   34.122  1.00 33.55  ? 56  VAL   B N   1 
ATOM   3448 C CA  . VAL   B 1 56  ? 36.285 3.247   34.270  1.00 33.78  ? 56  VAL   B CA  1 
ATOM   3449 C C   . VAL   B 1 56  ? 36.274 2.125   33.192  1.00 38.90  ? 56  VAL   B C   1 
ATOM   3450 O O   . VAL   B 1 56  ? 35.952 0.972   33.511  1.00 39.42  ? 56  VAL   B O   1 
ATOM   3451 C CB  . VAL   B 1 56  ? 34.947 4.041   34.385  1.00 37.43  ? 56  VAL   B CB  1 
ATOM   3452 C CG1 . VAL   B 1 56  ? 34.622 4.831   33.099  1.00 37.15  ? 56  VAL   B CG1 1 
ATOM   3453 C CG2 . VAL   B 1 56  ? 33.795 3.129   34.793  1.00 36.58  ? 56  VAL   B CG2 1 
ATOM   3454 N N   . THR   B 1 57  ? 36.671 2.469   31.937  1.00 34.51  ? 57  THR   B N   1 
ATOM   3455 C CA  . THR   B 1 57  ? 36.760 1.556   30.793  1.00 34.22  ? 57  THR   B CA  1 
ATOM   3456 C C   . THR   B 1 57  ? 37.802 0.451   31.054  1.00 39.35  ? 57  THR   B C   1 
ATOM   3457 O O   . THR   B 1 57  ? 37.534 -0.738  30.821  1.00 39.69  ? 57  THR   B O   1 
ATOM   3458 C CB  . THR   B 1 57  ? 37.043 2.348   29.523  1.00 40.07  ? 57  THR   B CB  1 
ATOM   3459 O OG1 . THR   B 1 57  ? 36.115 3.426   29.430  1.00 37.01  ? 57  THR   B OG1 1 
ATOM   3460 C CG2 . THR   B 1 57  ? 36.978 1.496   28.272  1.00 38.16  ? 57  THR   B CG2 1 
ATOM   3461 N N   . LYS   B 1 58  ? 38.976 0.854   31.561  1.00 35.27  ? 58  LYS   B N   1 
ATOM   3462 C CA  . LYS   B 1 58  ? 40.077 -0.049  31.890  1.00 34.09  ? 58  LYS   B CA  1 
ATOM   3463 C C   . LYS   B 1 58  ? 39.713 -0.959  33.044  1.00 39.59  ? 58  LYS   B C   1 
ATOM   3464 O O   . LYS   B 1 58  ? 39.980 -2.158  32.958  1.00 41.44  ? 58  LYS   B O   1 
ATOM   3465 C CB  . LYS   B 1 58  ? 41.401 0.721   32.094  1.00 35.46  ? 58  LYS   B CB  1 
ATOM   3466 C CG  . LYS   B 1 58  ? 41.828 1.444   30.809  1.00 34.26  ? 58  LYS   B CG  1 
ATOM   3467 C CD  . LYS   B 1 58  ? 43.068 2.284   30.994  1.00 44.43  ? 58  LYS   B CD  1 
ATOM   3468 C CE  . LYS   B 1 58  ? 42.786 3.751   31.180  1.00 58.40  ? 58  LYS   B CE  1 
ATOM   3469 N NZ  . LYS   B 1 58  ? 43.973 4.458   31.731  1.00 67.80  ? 58  LYS   B NZ  1 
ATOM   3470 N N   . ASP   B 1 59  ? 39.043 -0.423  34.093  1.00 35.97  ? 59  ASP   B N   1 
ATOM   3471 C CA  . ASP   B 1 59  ? 38.589 -1.214  35.240  1.00 34.88  ? 59  ASP   B CA  1 
ATOM   3472 C C   . ASP   B 1 59  ? 37.564 -2.227  34.813  1.00 38.14  ? 59  ASP   B C   1 
ATOM   3473 O O   . ASP   B 1 59  ? 37.604 -3.353  35.301  1.00 39.28  ? 59  ASP   B O   1 
ATOM   3474 C CB  . ASP   B 1 59  ? 37.978 -0.336  36.337  1.00 37.21  ? 59  ASP   B CB  1 
ATOM   3475 C CG  . ASP   B 1 59  ? 38.937 0.581   37.070  1.00 46.47  ? 59  ASP   B CG  1 
ATOM   3476 O OD1 . ASP   B 1 59  ? 40.159 0.465   36.848  1.00 47.00  ? 59  ASP   B OD1 1 
ATOM   3477 O OD2 . ASP   B 1 59  ? 38.459 1.419   37.865  1.00 52.92  ? 59  ASP   B OD2 1 
ATOM   3478 N N   . ALA   B 1 60  ? 36.629 -1.834  33.929  1.00 34.37  ? 60  ALA   B N   1 
ATOM   3479 C CA  . ALA   B 1 60  ? 35.591 -2.730  33.407  1.00 34.81  ? 60  ALA   B CA  1 
ATOM   3480 C C   . ALA   B 1 60  ? 36.271 -3.908  32.684  1.00 39.94  ? 60  ALA   B C   1 
ATOM   3481 O O   . ALA   B 1 60  ? 36.003 -5.058  33.033  1.00 39.03  ? 60  ALA   B O   1 
ATOM   3482 C CB  . ALA   B 1 60  ? 34.663 -1.983  32.459  1.00 35.64  ? 60  ALA   B CB  1 
ATOM   3483 N N   . ALA   B 1 61  ? 37.199 -3.616  31.732  1.00 38.29  ? 61  ALA   B N   1 
ATOM   3484 C CA  . ALA   B 1 61  ? 37.973 -4.619  30.990  1.00 38.40  ? 61  ALA   B CA  1 
ATOM   3485 C C   . ALA   B 1 61  ? 38.684 -5.590  31.946  1.00 41.43  ? 61  ALA   B C   1 
ATOM   3486 O O   . ALA   B 1 61  ? 38.618 -6.791  31.731  1.00 42.18  ? 61  ALA   B O   1 
ATOM   3487 C CB  . ALA   B 1 61  ? 38.984 -3.932  30.090  1.00 39.33  ? 61  ALA   B CB  1 
ATOM   3488 N N   . GLU   B 1 62  ? 39.304 -5.081  33.020  1.00 37.87  ? 62  GLU   B N   1 
ATOM   3489 C CA  . GLU   B 1 62  ? 39.983 -5.905  34.034  1.00 37.39  ? 62  GLU   B CA  1 
ATOM   3490 C C   . GLU   B 1 62  ? 38.998 -6.744  34.827  1.00 41.29  ? 62  GLU   B C   1 
ATOM   3491 O O   . GLU   B 1 62  ? 39.332 -7.855  35.222  1.00 43.71  ? 62  GLU   B O   1 
ATOM   3492 C CB  . GLU   B 1 62  ? 40.850 -5.054  34.975  1.00 38.22  ? 62  GLU   B CB  1 
ATOM   3493 N N   . ALA   B 1 63  ? 37.777 -6.244  35.035  1.00 35.62  ? 63  ALA   B N   1 
ATOM   3494 C CA  . ALA   B 1 63  ? 36.754 -6.985  35.769  1.00 34.39  ? 63  ALA   B CA  1 
ATOM   3495 C C   . ALA   B 1 63  ? 36.234 -8.181  34.933  1.00 41.32  ? 63  ALA   B C   1 
ATOM   3496 O O   . ALA   B 1 63  ? 35.950 -9.246  35.504  1.00 41.84  ? 63  ALA   B O   1 
ATOM   3497 C CB  . ALA   B 1 63  ? 35.625 -6.062  36.174  1.00 34.14  ? 63  ALA   B CB  1 
ATOM   3498 N N   . ILE   B 1 64  ? 36.132 -8.011  33.582  1.00 37.06  ? 64  ILE   B N   1 
ATOM   3499 C CA  . ILE   B 1 64  ? 35.704 -9.074  32.653  1.00 36.52  ? 64  ILE   B CA  1 
ATOM   3500 C C   . ILE   B 1 64  ? 36.792 -10.167 32.641  1.00 41.81  ? 64  ILE   B C   1 
ATOM   3501 O O   . ILE   B 1 64  ? 36.466 -11.345 32.576  1.00 41.22  ? 64  ILE   B O   1 
ATOM   3502 C CB  . ILE   B 1 64  ? 35.384 -8.571  31.211  1.00 38.53  ? 64  ILE   B CB  1 
ATOM   3503 C CG1 . ILE   B 1 64  ? 34.423 -7.360  31.191  1.00 37.07  ? 64  ILE   B CG1 1 
ATOM   3504 C CG2 . ILE   B 1 64  ? 34.816 -9.694  30.350  1.00 39.42  ? 64  ILE   B CG2 1 
ATOM   3505 C CD1 . ILE   B 1 64  ? 34.439 -6.571  29.800  1.00 30.53  ? 64  ILE   B CD1 1 
ATOM   3506 N N   . LYS   B 1 65  ? 38.074 -9.770  32.737  1.00 40.40  ? 65  LYS   B N   1 
ATOM   3507 C CA  . LYS   B 1 65  ? 39.225 -10.676 32.767  1.00 41.60  ? 65  LYS   B CA  1 
ATOM   3508 C C   . LYS   B 1 65  ? 39.137 -11.569 33.993  1.00 46.90  ? 65  LYS   B C   1 
ATOM   3509 O O   . LYS   B 1 65  ? 39.338 -12.777 33.909  1.00 49.17  ? 65  LYS   B O   1 
ATOM   3510 C CB  . LYS   B 1 65  ? 40.539 -9.864  32.786  1.00 45.64  ? 65  LYS   B CB  1 
ATOM   3511 C CG  . LYS   B 1 65  ? 41.723 -10.538 32.096  1.00 57.17  ? 65  LYS   B CG  1 
ATOM   3512 C CD  . LYS   B 1 65  ? 42.735 -9.485  31.620  1.00 69.27  ? 65  LYS   B CD  1 
ATOM   3513 C CE  . LYS   B 1 65  ? 43.984 -10.068 30.990  1.00 89.49  ? 65  LYS   B CE  1 
ATOM   3514 N NZ  . LYS   B 1 65  ? 44.921 -10.654 31.996  1.00 100.01 ? 65  LYS   B NZ  1 
ATOM   3515 N N   . LYS   B 1 66  ? 38.800 -10.968 35.119  1.00 42.40  ? 66  LYS   B N   1 
ATOM   3516 C CA  . LYS   B 1 66  ? 38.656 -11.622 36.404  1.00 41.07  ? 66  LYS   B CA  1 
ATOM   3517 C C   . LYS   B 1 66  ? 37.359 -12.454 36.502  1.00 44.91  ? 66  LYS   B C   1 
ATOM   3518 O O   . LYS   B 1 66  ? 37.427 -13.625 36.873  1.00 45.64  ? 66  LYS   B O   1 
ATOM   3519 C CB  . LYS   B 1 66  ? 38.692 -10.547 37.507  1.00 41.96  ? 66  LYS   B CB  1 
ATOM   3520 C CG  . LYS   B 1 66  ? 39.071 -11.081 38.859  1.00 50.30  ? 66  LYS   B CG  1 
ATOM   3521 C CD  . LYS   B 1 66  ? 38.645 -10.151 39.966  1.00 59.18  ? 66  LYS   B CD  1 
ATOM   3522 C CE  . LYS   B 1 66  ? 38.843 -10.832 41.298  1.00 67.21  ? 66  LYS   B CE  1 
ATOM   3523 N NZ  . LYS   B 1 66  ? 38.018 -10.206 42.357  1.00 76.70  ? 66  LYS   B NZ  1 
ATOM   3524 N N   . HIS   B 1 67  ? 36.191 -11.860 36.172  1.00 39.05  ? 67  HIS   B N   1 
ATOM   3525 C CA  . HIS   B 1 67  ? 34.880 -12.510 36.310  1.00 37.45  ? 67  HIS   B CA  1 
ATOM   3526 C C   . HIS   B 1 67  ? 34.351 -13.365 35.185  1.00 40.97  ? 67  HIS   B C   1 
ATOM   3527 O O   . HIS   B 1 67  ? 33.354 -14.061 35.389  1.00 42.27  ? 67  HIS   B O   1 
ATOM   3528 C CB  . HIS   B 1 67  ? 33.831 -11.548 36.898  1.00 37.66  ? 67  HIS   B CB  1 
ATOM   3529 C CG  . HIS   B 1 67  ? 34.317 -10.929 38.176  1.00 40.66  ? 67  HIS   B CG  1 
ATOM   3530 N ND1 . HIS   B 1 67  ? 34.424 -11.670 39.343  1.00 41.48  ? 67  HIS   B ND1 1 
ATOM   3531 C CD2 . HIS   B 1 67  ? 34.791 -9.680  38.406  1.00 42.56  ? 67  HIS   B CD2 1 
ATOM   3532 C CE1 . HIS   B 1 67  ? 34.932 -10.848 40.243  1.00 41.24  ? 67  HIS   B CE1 1 
ATOM   3533 N NE2 . HIS   B 1 67  ? 35.165 -9.637  39.732  1.00 42.02  ? 67  HIS   B NE2 1 
ATOM   3534 N N   . ASN   B 1 68  ? 35.021 -13.344 34.013  1.00 36.13  ? 68  ASN   B N   1 
ATOM   3535 C CA  . ASN   B 1 68  ? 34.728 -14.140 32.810  1.00 35.25  ? 68  ASN   B CA  1 
ATOM   3536 C C   . ASN   B 1 68  ? 33.456 -13.821 32.022  1.00 39.49  ? 68  ASN   B C   1 
ATOM   3537 O O   . ASN   B 1 68  ? 33.285 -14.345 30.920  1.00 38.67  ? 68  ASN   B O   1 
ATOM   3538 C CB  . ASN   B 1 68  ? 34.796 -15.654 33.129  1.00 35.83  ? 68  ASN   B CB  1 
ATOM   3539 C CG  . ASN   B 1 68  ? 36.065 -16.100 33.803  1.00 49.25  ? 68  ASN   B CG  1 
ATOM   3540 O OD1 . ASN   B 1 68  ? 37.171 -16.020 33.247  1.00 40.45  ? 68  ASN   B OD1 1 
ATOM   3541 N ND2 . ASN   B 1 68  ? 35.927 -16.578 35.023  1.00 41.19  ? 68  ASN   B ND2 1 
ATOM   3542 N N   . VAL   B 1 69  ? 32.545 -13.010 32.583  1.00 38.03  ? 69  VAL   B N   1 
ATOM   3543 C CA  . VAL   B 1 69  ? 31.270 -12.681 31.941  1.00 37.76  ? 69  VAL   B CA  1 
ATOM   3544 C C   . VAL   B 1 69  ? 31.047 -11.180 31.956  1.00 41.13  ? 69  VAL   B C   1 
ATOM   3545 O O   . VAL   B 1 69  ? 30.955 -10.595 33.032  1.00 40.47  ? 69  VAL   B O   1 
ATOM   3546 C CB  . VAL   B 1 69  ? 30.083 -13.464 32.601  1.00 41.68  ? 69  VAL   B CB  1 
ATOM   3547 C CG1 . VAL   B 1 69  ? 28.739 -13.120 31.945  1.00 41.10  ? 69  VAL   B CG1 1 
ATOM   3548 C CG2 . VAL   B 1 69  ? 30.318 -14.973 32.564  1.00 41.45  ? 69  VAL   B CG2 1 
ATOM   3549 N N   . GLY   B 1 70  ? 30.945 -10.583 30.766  1.00 37.94  ? 70  GLY   B N   1 
ATOM   3550 C CA  . GLY   B 1 70  ? 30.700 -9.152  30.589  1.00 37.13  ? 70  GLY   B CA  1 
ATOM   3551 C C   . GLY   B 1 70  ? 29.510 -8.848  29.696  1.00 40.60  ? 70  GLY   B C   1 
ATOM   3552 O O   . GLY   B 1 70  ? 29.394 -9.422  28.613  1.00 40.93  ? 70  GLY   B O   1 
ATOM   3553 N N   . VAL   B 1 71  ? 28.605 -7.949  30.129  1.00 36.66  ? 71  VAL   B N   1 
ATOM   3554 C CA  . VAL   B 1 71  ? 27.424 -7.542  29.337  1.00 35.95  ? 71  VAL   B CA  1 
ATOM   3555 C C   . VAL   B 1 71  ? 27.537 -6.033  29.096  1.00 39.82  ? 71  VAL   B C   1 
ATOM   3556 O O   . VAL   B 1 71  ? 27.578 -5.258  30.045  1.00 41.08  ? 71  VAL   B O   1 
ATOM   3557 C CB  . VAL   B 1 71  ? 26.027 -8.044  29.854  1.00 39.70  ? 71  VAL   B CB  1 
ATOM   3558 C CG1 . VAL   B 1 71  ? 25.959 -9.571  29.886  1.00 39.71  ? 71  VAL   B CG1 1 
ATOM   3559 C CG2 . VAL   B 1 71  ? 25.677 -7.485  31.227  1.00 39.81  ? 71  VAL   B CG2 1 
ATOM   3560 N N   . LYS   B 1 72  ? 27.675 -5.618  27.845  1.00 35.82  ? 72  LYS   B N   1 
ATOM   3561 C CA  . LYS   B 1 72  ? 27.866 -4.203  27.560  1.00 35.79  ? 72  LYS   B CA  1 
ATOM   3562 C C   . LYS   B 1 72  ? 26.759 -3.505  26.772  1.00 39.74  ? 72  LYS   B C   1 
ATOM   3563 O O   . LYS   B 1 72  ? 26.275 -3.996  25.750  1.00 39.84  ? 72  LYS   B O   1 
ATOM   3564 C CB  . LYS   B 1 72  ? 29.261 -3.962  26.913  1.00 36.82  ? 72  LYS   B CB  1 
ATOM   3565 C CG  . LYS   B 1 72  ? 29.630 -2.499  26.713  1.00 26.24  ? 72  LYS   B CG  1 
ATOM   3566 C CD  . LYS   B 1 72  ? 30.873 -2.295  25.885  1.00 31.19  ? 72  LYS   B CD  1 
ATOM   3567 C CE  . LYS   B 1 72  ? 31.098 -0.829  25.627  1.00 29.43  ? 72  LYS   B CE  1 
ATOM   3568 N NZ  . LYS   B 1 72  ? 30.176 -0.326  24.579  1.00 37.84  ? 72  LYS   B NZ  1 
ATOM   3569 N N   . CYS   B 1 73  ? 26.405 -2.323  27.252  1.00 35.19  ? 73  CYS   B N   1 
ATOM   3570 C CA  . CYS   B 1 73  ? 25.436 -1.432  26.647  1.00 34.94  ? 73  CYS   B CA  1 
ATOM   3571 C C   . CYS   B 1 73  ? 26.217 -0.574  25.611  1.00 38.63  ? 73  CYS   B C   1 
ATOM   3572 O O   . CYS   B 1 73  ? 27.395 -0.323  25.808  1.00 38.61  ? 73  CYS   B O   1 
ATOM   3573 C CB  . CYS   B 1 73  ? 24.815 -0.570  27.742  1.00 35.11  ? 73  CYS   B CB  1 
ATOM   3574 S SG  . CYS   B 1 73  ? 23.671 0.689   27.143  1.00 38.94  ? 73  CYS   B SG  1 
ATOM   3575 N N   . ALA   B 1 74  ? 25.583 -0.118  24.531  1.00 36.15  ? 74  ALA   B N   1 
ATOM   3576 C CA  . ALA   B 1 74  ? 26.268 0.716   23.520  1.00 35.43  ? 74  ALA   B CA  1 
ATOM   3577 C C   . ALA   B 1 74  ? 26.762 2.021   24.113  1.00 39.03  ? 74  ALA   B C   1 
ATOM   3578 O O   . ALA   B 1 74  ? 26.136 2.557   25.021  1.00 39.23  ? 74  ALA   B O   1 
ATOM   3579 C CB  . ALA   B 1 74  ? 25.355 0.990   22.342  1.00 35.92  ? 74  ALA   B CB  1 
ATOM   3580 N N   . THR   B 1 75  ? 27.904 2.509   23.625  1.00 35.78  ? 75  THR   B N   1 
ATOM   3581 C CA  . THR   B 1 75  ? 28.566 3.733   24.099  1.00 34.83  ? 75  THR   B CA  1 
ATOM   3582 C C   . THR   B 1 75  ? 28.920 4.696   22.977  1.00 38.91  ? 75  THR   B C   1 
ATOM   3583 O O   . THR   B 1 75  ? 29.138 4.286   21.846  1.00 37.36  ? 75  THR   B O   1 
ATOM   3584 C CB  . THR   B 1 75  ? 29.862 3.377   24.848  1.00 38.33  ? 75  THR   B CB  1 
ATOM   3585 O OG1 . THR   B 1 75  ? 30.568 2.361   24.124  1.00 34.79  ? 75  THR   B OG1 1 
ATOM   3586 C CG2 . THR   B 1 75  ? 29.620 2.958   26.302  1.00 33.25  ? 75  THR   B CG2 1 
ATOM   3587 N N   . ILE   B 1 76  ? 28.984 5.983   23.292  1.00 38.22  ? 76  ILE   B N   1 
ATOM   3588 C CA  . ILE   B 1 76  ? 29.362 6.989   22.307  1.00 38.61  ? 76  ILE   B CA  1 
ATOM   3589 C C   . ILE   B 1 76  ? 30.866 6.883   22.094  1.00 46.57  ? 76  ILE   B C   1 
ATOM   3590 O O   . ILE   B 1 76  ? 31.625 6.923   23.066  1.00 46.33  ? 76  ILE   B O   1 
ATOM   3591 C CB  . ILE   B 1 76  ? 29.009 8.430   22.789  1.00 40.23  ? 76  ILE   B CB  1 
ATOM   3592 C CG1 . ILE   B 1 76  ? 27.499 8.653   22.899  1.00 39.71  ? 76  ILE   B CG1 1 
ATOM   3593 C CG2 . ILE   B 1 76  ? 29.648 9.468   21.876  1.00 38.87  ? 76  ILE   B CG2 1 
ATOM   3594 C CD1 . ILE   B 1 76  ? 27.119 9.864   23.769  1.00 41.64  ? 76  ILE   B CD1 1 
ATOM   3595 N N   . THR   B 1 77  ? 31.292 6.746   20.834  1.00 46.80  ? 77  THR   B N   1 
ATOM   3596 C CA  . THR   B 1 77  ? 32.712 6.771   20.471  1.00 46.94  ? 77  THR   B CA  1 
ATOM   3597 C C   . THR   B 1 77  ? 32.917 8.250   20.069  1.00 49.60  ? 77  THR   B C   1 
ATOM   3598 O O   . THR   B 1 77  ? 32.270 8.720   19.126  1.00 47.71  ? 77  THR   B O   1 
ATOM   3599 C CB  . THR   B 1 77  ? 33.058 5.766   19.377  1.00 54.92  ? 77  THR   B CB  1 
ATOM   3600 O OG1 . THR   B 1 77  ? 32.807 4.459   19.886  1.00 56.32  ? 77  THR   B OG1 1 
ATOM   3601 C CG2 . THR   B 1 77  ? 34.517 5.887   18.912  1.00 51.03  ? 77  THR   B CG2 1 
ATOM   3602 N N   . PRO   B 1 78  ? 33.730 9.013   20.828  1.00 47.20  ? 78  PRO   B N   1 
ATOM   3603 C CA  . PRO   B 1 78  ? 33.904 10.447  20.515  1.00 47.56  ? 78  PRO   B CA  1 
ATOM   3604 C C   . PRO   B 1 78  ? 34.551 10.804  19.171  1.00 52.96  ? 78  PRO   B C   1 
ATOM   3605 O O   . PRO   B 1 78  ? 35.397 10.081  18.653  1.00 52.35  ? 78  PRO   B O   1 
ATOM   3606 C CB  . PRO   B 1 78  ? 34.760 10.967  21.677  1.00 48.81  ? 78  PRO   B CB  1 
ATOM   3607 C CG  . PRO   B 1 78  ? 34.728 9.908   22.714  1.00 52.64  ? 78  PRO   B CG  1 
ATOM   3608 C CD  . PRO   B 1 78  ? 34.524 8.620   22.005  1.00 48.24  ? 78  PRO   B CD  1 
ATOM   3609 N N   . ASP   B 1 79  ? 34.137 11.954  18.628  1.00 51.09  ? 79  ASP   B N   1 
ATOM   3610 C CA  . ASP   B 1 79  ? 34.630 12.595  17.400  1.00 51.10  ? 79  ASP   B CA  1 
ATOM   3611 C C   . ASP   B 1 79  ? 34.651 14.093  17.709  1.00 54.74  ? 79  ASP   B C   1 
ATOM   3612 O O   . ASP   B 1 79  ? 34.282 14.459  18.827  1.00 53.97  ? 79  ASP   B O   1 
ATOM   3613 C CB  . ASP   B 1 79  ? 33.748 12.266  16.178  1.00 53.12  ? 79  ASP   B CB  1 
ATOM   3614 C CG  . ASP   B 1 79  ? 32.287 12.694  16.246  1.00 64.54  ? 79  ASP   B CG  1 
ATOM   3615 O OD1 . ASP   B 1 79  ? 31.483 12.176  15.444  1.00 65.65  ? 79  ASP   B OD1 1 
ATOM   3616 O OD2 . ASP   B 1 79  ? 31.949 13.553  17.100  1.00 68.64  ? 79  ASP   B OD2 1 
ATOM   3617 N N   . GLU   B 1 80  ? 35.048 14.956  16.756  1.00 52.19  ? 80  GLU   B N   1 
ATOM   3618 C CA  . GLU   B 1 80  ? 35.092 16.405  16.994  1.00 51.77  ? 80  GLU   B CA  1 
ATOM   3619 C C   . GLU   B 1 80  ? 33.780 16.974  17.519  1.00 55.03  ? 80  GLU   B C   1 
ATOM   3620 O O   . GLU   B 1 80  ? 33.804 17.764  18.469  1.00 55.71  ? 80  GLU   B O   1 
ATOM   3621 C CB  . GLU   B 1 80  ? 35.593 17.170  15.767  1.00 53.16  ? 80  GLU   B CB  1 
ATOM   3622 N N   . LYS   B 1 81  ? 32.644 16.543  16.937  1.00 50.68  ? 81  LYS   B N   1 
ATOM   3623 C CA  . LYS   B 1 81  ? 31.300 16.989  17.333  1.00 50.56  ? 81  LYS   B CA  1 
ATOM   3624 C C   . LYS   B 1 81  ? 30.946 16.581  18.768  1.00 53.55  ? 81  LYS   B C   1 
ATOM   3625 O O   . LYS   B 1 81  ? 30.344 17.385  19.487  1.00 53.86  ? 81  LYS   B O   1 
ATOM   3626 C CB  . LYS   B 1 81  ? 30.221 16.492  16.351  1.00 53.44  ? 81  LYS   B CB  1 
ATOM   3627 C CG  . LYS   B 1 81  ? 30.456 16.882  14.889  1.00 72.85  ? 81  LYS   B CG  1 
ATOM   3628 C CD  . LYS   B 1 81  ? 29.366 16.339  13.949  1.00 84.46  ? 81  LYS   B CD  1 
ATOM   3629 C CE  . LYS   B 1 81  ? 29.704 14.986  13.347  1.00 89.47  ? 81  LYS   B CE  1 
ATOM   3630 N NZ  . LYS   B 1 81  ? 28.611 14.469  12.475  1.00 89.34  ? 81  LYS   B NZ  1 
ATOM   3631 N N   . ARG   B 1 82  ? 31.321 15.341  19.184  1.00 47.96  ? 82  ARG   B N   1 
ATOM   3632 C CA  . ARG   B 1 82  ? 31.059 14.826  20.545  1.00 46.93  ? 82  ARG   B CA  1 
ATOM   3633 C C   . ARG   B 1 82  ? 31.893 15.564  21.587  1.00 50.51  ? 82  ARG   B C   1 
ATOM   3634 O O   . ARG   B 1 82  ? 31.424 15.795  22.705  1.00 51.78  ? 82  ARG   B O   1 
ATOM   3635 C CB  . ARG   B 1 82  ? 31.259 13.296  20.656  1.00 43.83  ? 82  ARG   B CB  1 
ATOM   3636 C CG  . ARG   B 1 82  ? 30.332 12.449  19.769  1.00 43.70  ? 82  ARG   B CG  1 
ATOM   3637 C CD  . ARG   B 1 82  ? 28.862 12.678  20.079  1.00 45.15  ? 82  ARG   B CD  1 
ATOM   3638 N NE  . ARG   B 1 82  ? 28.032 11.559  19.639  1.00 47.06  ? 82  ARG   B NE  1 
ATOM   3639 C CZ  . ARG   B 1 82  ? 26.764 11.386  19.988  1.00 53.65  ? 82  ARG   B CZ  1 
ATOM   3640 N NH1 . ARG   B 1 82  ? 26.160 12.262  20.774  1.00 40.72  ? 82  ARG   B NH1 1 
ATOM   3641 N NH2 . ARG   B 1 82  ? 26.089 10.332  19.554  1.00 49.26  ? 82  ARG   B NH2 1 
ATOM   3642 N N   . VAL   B 1 83  ? 33.121 15.948  21.203  1.00 44.83  ? 83  VAL   B N   1 
ATOM   3643 C CA  . VAL   B 1 83  ? 34.070 16.695  22.023  1.00 43.82  ? 83  VAL   B CA  1 
ATOM   3644 C C   . VAL   B 1 83  ? 33.458 18.075  22.331  1.00 49.66  ? 83  VAL   B C   1 
ATOM   3645 O O   . VAL   B 1 83  ? 33.506 18.520  23.482  1.00 48.84  ? 83  VAL   B O   1 
ATOM   3646 C CB  . VAL   B 1 83  ? 35.479 16.756  21.361  1.00 46.20  ? 83  VAL   B CB  1 
ATOM   3647 C CG1 . VAL   B 1 83  ? 36.394 17.736  22.080  1.00 45.99  ? 83  VAL   B CG1 1 
ATOM   3648 C CG2 . VAL   B 1 83  ? 36.127 15.374  21.310  1.00 45.40  ? 83  VAL   B CG2 1 
ATOM   3649 N N   . GLU   B 1 84  ? 32.836 18.718  21.317  1.00 47.98  ? 84  GLU   B N   1 
ATOM   3650 C CA  . GLU   B 1 84  ? 32.191 20.027  21.481  1.00 48.79  ? 84  GLU   B CA  1 
ATOM   3651 C C   . GLU   B 1 84  ? 30.889 19.900  22.286  1.00 53.54  ? 84  GLU   B C   1 
ATOM   3652 O O   . GLU   B 1 84  ? 30.593 20.747  23.130  1.00 53.80  ? 84  GLU   B O   1 
ATOM   3653 C CB  . GLU   B 1 84  ? 31.934 20.691  20.110  1.00 50.25  ? 84  GLU   B CB  1 
ATOM   3654 N N   . GLU   B 1 85  ? 30.129 18.823  22.025  1.00 50.16  ? 85  GLU   B N   1 
ATOM   3655 C CA  . GLU   B 1 85  ? 28.844 18.510  22.659  1.00 48.79  ? 85  GLU   B CA  1 
ATOM   3656 C C   . GLU   B 1 85  ? 28.917 18.308  24.163  1.00 51.30  ? 85  GLU   B C   1 
ATOM   3657 O O   . GLU   B 1 85  ? 28.045 18.806  24.869  1.00 50.90  ? 85  GLU   B O   1 
ATOM   3658 C CB  . GLU   B 1 85  ? 28.227 17.251  22.013  1.00 49.52  ? 85  GLU   B CB  1 
ATOM   3659 C CG  . GLU   B 1 85  ? 26.866 16.891  22.592  1.00 52.91  ? 85  GLU   B CG  1 
ATOM   3660 C CD  . GLU   B 1 85  ? 26.135 15.712  21.991  1.00 54.05  ? 85  GLU   B CD  1 
ATOM   3661 O OE1 . GLU   B 1 85  ? 26.659 15.095  21.039  1.00 47.09  ? 85  GLU   B OE1 1 
ATOM   3662 O OE2 . GLU   B 1 85  ? 25.023 15.409  22.473  1.00 49.23  ? 85  GLU   B OE2 1 
ATOM   3663 N N   . PHE   B 1 86  ? 29.904 17.521  24.644  1.00 46.58  ? 86  PHE   B N   1 
ATOM   3664 C CA  . PHE   B 1 86  ? 30.041 17.184  26.068  1.00 45.13  ? 86  PHE   B CA  1 
ATOM   3665 C C   . PHE   B 1 86  ? 31.193 17.892  26.742  1.00 49.47  ? 86  PHE   B C   1 
ATOM   3666 O O   . PHE   B 1 86  ? 31.474 17.621  27.913  1.00 47.94  ? 86  PHE   B O   1 
ATOM   3667 C CB  . PHE   B 1 86  ? 30.179 15.654  26.247  1.00 45.31  ? 86  PHE   B CB  1 
ATOM   3668 C CG  . PHE   B 1 86  ? 29.014 14.860  25.715  1.00 44.58  ? 86  PHE   B CG  1 
ATOM   3669 C CD1 . PHE   B 1 86  ? 29.089 14.228  24.481  1.00 45.02  ? 86  PHE   B CD1 1 
ATOM   3670 C CD2 . PHE   B 1 86  ? 27.833 14.751  26.447  1.00 45.27  ? 86  PHE   B CD2 1 
ATOM   3671 C CE1 . PHE   B 1 86  ? 28.006 13.498  23.988  1.00 45.77  ? 86  PHE   B CE1 1 
ATOM   3672 C CE2 . PHE   B 1 86  ? 26.751 14.019  25.953  1.00 46.54  ? 86  PHE   B CE2 1 
ATOM   3673 C CZ  . PHE   B 1 86  ? 26.842 13.405  24.724  1.00 44.54  ? 86  PHE   B CZ  1 
ATOM   3674 N N   . LYS   B 1 87  ? 31.860 18.797  25.996  1.00 47.51  ? 87  LYS   B N   1 
ATOM   3675 C CA  . LYS   B 1 87  ? 33.018 19.579  26.441  1.00 46.94  ? 87  LYS   B CA  1 
ATOM   3676 C C   . LYS   B 1 87  ? 34.086 18.622  26.999  1.00 49.02  ? 87  LYS   B C   1 
ATOM   3677 O O   . LYS   B 1 87  ? 34.564 18.771  28.129  1.00 50.07  ? 87  LYS   B O   1 
ATOM   3678 C CB  . LYS   B 1 87  ? 32.602 20.722  27.400  1.00 49.10  ? 87  LYS   B CB  1 
ATOM   3679 C CG  . LYS   B 1 87  ? 31.418 21.569  26.909  1.00 62.18  ? 87  LYS   B CG  1 
ATOM   3680 C CD  . LYS   B 1 87  ? 31.774 22.534  25.766  1.00 75.47  ? 87  LYS   B CD  1 
ATOM   3681 N N   . LEU   B 1 88  ? 34.414 17.606  26.177  1.00 43.09  ? 88  LEU   B N   1 
ATOM   3682 C CA  . LEU   B 1 88  ? 35.363 16.532  26.462  1.00 42.34  ? 88  LEU   B CA  1 
ATOM   3683 C C   . LEU   B 1 88  ? 36.788 17.041  26.583  1.00 49.13  ? 88  LEU   B C   1 
ATOM   3684 O O   . LEU   B 1 88  ? 37.191 17.921  25.827  1.00 50.33  ? 88  LEU   B O   1 
ATOM   3685 C CB  . LEU   B 1 88  ? 35.284 15.421  25.389  1.00 41.61  ? 88  LEU   B CB  1 
ATOM   3686 C CG  . LEU   B 1 88  ? 33.976 14.608  25.266  1.00 46.23  ? 88  LEU   B CG  1 
ATOM   3687 C CD1 . LEU   B 1 88  ? 34.139 13.500  24.285  1.00 46.28  ? 88  LEU   B CD1 1 
ATOM   3688 C CD2 . LEU   B 1 88  ? 33.559 13.976  26.594  1.00 49.80  ? 88  LEU   B CD2 1 
ATOM   3689 N N   . LYS   B 1 89  ? 37.553 16.473  27.537  1.00 45.49  ? 89  LYS   B N   1 
ATOM   3690 C CA  . LYS   B 1 89  ? 38.946 16.821  27.818  1.00 44.09  ? 89  LYS   B CA  1 
ATOM   3691 C C   . LYS   B 1 89  ? 39.829 16.340  26.676  1.00 50.22  ? 89  LYS   B C   1 
ATOM   3692 O O   . LYS   B 1 89  ? 40.861 16.957  26.385  1.00 50.76  ? 89  LYS   B O   1 
ATOM   3693 C CB  . LYS   B 1 89  ? 39.422 16.131  29.108  1.00 44.10  ? 89  LYS   B CB  1 
ATOM   3694 C CG  . LYS   B 1 89  ? 38.729 16.546  30.372  1.00 45.50  ? 89  LYS   B CG  1 
ATOM   3695 C CD  . LYS   B 1 89  ? 39.106 15.569  31.504  1.00 44.94  ? 89  LYS   B CD  1 
ATOM   3696 C CE  . LYS   B 1 89  ? 38.211 15.744  32.706  1.00 31.73  ? 89  LYS   B CE  1 
ATOM   3697 N NZ  . LYS   B 1 89  ? 38.593 14.850  33.812  1.00 43.23  ? 89  LYS   B NZ  1 
ATOM   3698 N N   . GLN   B 1 90  ? 39.431 15.202  26.066  1.00 46.25  ? 90  GLN   B N   1 
ATOM   3699 C CA  . GLN   B 1 90  ? 40.118 14.514  24.989  1.00 45.34  ? 90  GLN   B CA  1 
ATOM   3700 C C   . GLN   B 1 90  ? 39.096 13.778  24.127  1.00 51.00  ? 90  GLN   B C   1 
ATOM   3701 O O   . GLN   B 1 90  ? 37.943 13.610  24.530  1.00 50.86  ? 90  GLN   B O   1 
ATOM   3702 C CB  . GLN   B 1 90  ? 41.016 13.442  25.611  1.00 46.33  ? 90  GLN   B CB  1 
ATOM   3703 C CG  . GLN   B 1 90  ? 42.358 13.916  26.122  1.00 58.05  ? 90  GLN   B CG  1 
ATOM   3704 C CD  . GLN   B 1 90  ? 43.149 12.747  26.659  1.00 71.71  ? 90  GLN   B CD  1 
ATOM   3705 O OE1 . GLN   B 1 90  ? 43.402 11.748  25.956  1.00 63.08  ? 90  GLN   B OE1 1 
ATOM   3706 N NE2 . GLN   B 1 90  ? 43.552 12.841  27.927  1.00 60.97  ? 90  GLN   B NE2 1 
ATOM   3707 N N   . MET   B 1 91  ? 39.536 13.295  22.958  1.00 49.02  ? 91  MET   B N   1 
ATOM   3708 C CA  . MET   B 1 91  ? 38.711 12.493  22.065  1.00 49.21  ? 91  MET   B CA  1 
ATOM   3709 C C   . MET   B 1 91  ? 39.040 11.073  22.479  1.00 49.70  ? 91  MET   B C   1 
ATOM   3710 O O   . MET   B 1 91  ? 39.964 10.462  21.939  1.00 50.71  ? 91  MET   B O   1 
ATOM   3711 C CB  . MET   B 1 91  ? 39.081 12.733  20.602  1.00 52.24  ? 91  MET   B CB  1 
ATOM   3712 C CG  . MET   B 1 91  ? 38.026 12.235  19.658  1.00 57.17  ? 91  MET   B CG  1 
ATOM   3713 S SD  . MET   B 1 91  ? 38.436 12.629  17.961  1.00 62.60  ? 91  MET   B SD  1 
ATOM   3714 C CE  . MET   B 1 91  ? 38.214 14.444  17.978  1.00 58.66  ? 91  MET   B CE  1 
ATOM   3715 N N   . TRP   B 1 92  ? 38.335 10.579  23.496  1.00 42.56  ? 92  TRP   B N   1 
ATOM   3716 C CA  . TRP   B 1 92  ? 38.573 9.246   24.079  1.00 40.33  ? 92  TRP   B CA  1 
ATOM   3717 C C   . TRP   B 1 92  ? 38.435 8.118   23.075  1.00 43.53  ? 92  TRP   B C   1 
ATOM   3718 O O   . TRP   B 1 92  ? 37.526 8.147   22.262  1.00 42.10  ? 92  TRP   B O   1 
ATOM   3719 C CB  . TRP   B 1 92  ? 37.664 9.013   25.315  1.00 37.49  ? 92  TRP   B CB  1 
ATOM   3720 C CG  . TRP   B 1 92  ? 37.730 10.101  26.350  1.00 37.22  ? 92  TRP   B CG  1 
ATOM   3721 C CD1 . TRP   B 1 92  ? 36.773 11.039  26.628  1.00 39.88  ? 92  TRP   B CD1 1 
ATOM   3722 C CD2 . TRP   B 1 92  ? 38.843 10.393  27.213  1.00 36.35  ? 92  TRP   B CD2 1 
ATOM   3723 N NE1 . TRP   B 1 92  ? 37.212 11.885  27.628  1.00 38.52  ? 92  TRP   B NE1 1 
ATOM   3724 C CE2 . TRP   B 1 92  ? 38.477 11.504  28.010  1.00 39.67  ? 92  TRP   B CE2 1 
ATOM   3725 C CE3 . TRP   B 1 92  ? 40.123 9.827   27.381  1.00 36.50  ? 92  TRP   B CE3 1 
ATOM   3726 C CZ2 . TRP   B 1 92  ? 39.345 12.056  28.964  1.00 38.34  ? 92  TRP   B CZ2 1 
ATOM   3727 C CZ3 . TRP   B 1 92  ? 40.965 10.362  28.340  1.00 37.11  ? 92  TRP   B CZ3 1 
ATOM   3728 C CH2 . TRP   B 1 92  ? 40.581 11.470  29.110  1.00 37.46  ? 92  TRP   B CH2 1 
ATOM   3729 N N   . LYS   B 1 93  ? 39.330 7.123   23.136  1.00 42.75  ? 93  LYS   B N   1 
ATOM   3730 C CA  . LYS   B 1 93  ? 39.301 5.942   22.253  1.00 43.08  ? 93  LYS   B CA  1 
ATOM   3731 C C   . LYS   B 1 93  ? 37.992 5.185   22.509  1.00 48.86  ? 93  LYS   B C   1 
ATOM   3732 O O   . LYS   B 1 93  ? 37.382 5.363   23.571  1.00 49.19  ? 93  LYS   B O   1 
ATOM   3733 C CB  . LYS   B 1 93  ? 40.518 5.026   22.492  1.00 44.64  ? 93  LYS   B CB  1 
ATOM   3734 N N   . SER   B 1 94  ? 37.540 4.372   21.544  1.00 45.40  ? 94  SER   B N   1 
ATOM   3735 C CA  . SER   B 1 94  ? 36.290 3.651   21.741  1.00 45.23  ? 94  SER   B CA  1 
ATOM   3736 C C   . SER   B 1 94  ? 36.414 2.684   22.909  1.00 46.51  ? 94  SER   B C   1 
ATOM   3737 O O   . SER   B 1 94  ? 37.406 1.952   22.956  1.00 46.29  ? 94  SER   B O   1 
ATOM   3738 C CB  . SER   B 1 94  ? 35.857 2.901   20.476  1.00 48.19  ? 94  SER   B CB  1 
ATOM   3739 O OG  . SER   B 1 94  ? 36.499 1.643   20.332  1.00 54.53  ? 94  SER   B OG  1 
ATOM   3740 N N   . PRO   B 1 95  ? 35.426 2.642   23.840  1.00 41.16  ? 95  PRO   B N   1 
ATOM   3741 C CA  . PRO   B 1 95  ? 35.503 1.652   24.939  1.00 40.02  ? 95  PRO   B CA  1 
ATOM   3742 C C   . PRO   B 1 95  ? 35.672 0.218   24.417  1.00 44.19  ? 95  PRO   B C   1 
ATOM   3743 O O   . PRO   B 1 95  ? 36.392 -0.551  25.025  1.00 43.82  ? 95  PRO   B O   1 
ATOM   3744 C CB  . PRO   B 1 95  ? 34.177 1.838   25.698  1.00 40.90  ? 95  PRO   B CB  1 
ATOM   3745 C CG  . PRO   B 1 95  ? 33.691 3.185   25.311  1.00 45.24  ? 95  PRO   B CG  1 
ATOM   3746 C CD  . PRO   B 1 95  ? 34.179 3.440   23.915  1.00 41.28  ? 95  PRO   B CD  1 
ATOM   3747 N N   . ASN   B 1 96  ? 35.041 -0.120  23.271  1.00 43.10  ? 96  ASN   B N   1 
ATOM   3748 C CA  . ASN   B 1 96  ? 35.082 -1.438  22.601  1.00 43.69  ? 96  ASN   B CA  1 
ATOM   3749 C C   . ASN   B 1 96  ? 36.503 -1.842  22.225  1.00 48.93  ? 96  ASN   B C   1 
ATOM   3750 O O   . ASN   B 1 96  ? 36.889 -2.994  22.454  1.00 50.02  ? 96  ASN   B O   1 
ATOM   3751 C CB  . ASN   B 1 96  ? 34.200 -1.442  21.357  1.00 47.03  ? 96  ASN   B CB  1 
ATOM   3752 C CG  . ASN   B 1 96  ? 32.823 -0.864  21.593  1.00 74.50  ? 96  ASN   B CG  1 
ATOM   3753 O OD1 . ASN   B 1 96  ? 31.909 -1.557  22.045  1.00 68.16  ? 96  ASN   B OD1 1 
ATOM   3754 N ND2 . ASN   B 1 96  ? 32.650 0.427   21.304  1.00 66.51  ? 96  ASN   B ND2 1 
ATOM   3755 N N   . GLY   B 1 97  ? 37.264 -0.892  21.669  1.00 43.93  ? 97  GLY   B N   1 
ATOM   3756 C CA  . GLY   B 1 97  ? 38.656 -1.096  21.287  1.00 43.44  ? 97  GLY   B CA  1 
ATOM   3757 C C   . GLY   B 1 97  ? 39.529 -1.365  22.497  1.00 48.67  ? 97  GLY   B C   1 
ATOM   3758 O O   . GLY   B 1 97  ? 40.312 -2.316  22.486  1.00 50.15  ? 97  GLY   B O   1 
ATOM   3759 N N   . THR   B 1 98  ? 39.377 -0.545  23.561  1.00 44.28  ? 98  THR   B N   1 
ATOM   3760 C CA  . THR   B 1 98  ? 40.113 -0.664  24.823  1.00 43.87  ? 98  THR   B CA  1 
ATOM   3761 C C   . THR   B 1 98  ? 39.885 -2.039  25.455  1.00 48.64  ? 98  THR   B C   1 
ATOM   3762 O O   . THR   B 1 98  ? 40.856 -2.697  25.836  1.00 50.56  ? 98  THR   B O   1 
ATOM   3763 C CB  . THR   B 1 98  ? 39.748 0.498   25.759  1.00 50.30  ? 98  THR   B CB  1 
ATOM   3764 O OG1 . THR   B 1 98  ? 40.030 1.735   25.098  1.00 49.15  ? 98  THR   B OG1 1 
ATOM   3765 C CG2 . THR   B 1 98  ? 40.491 0.443   27.087  1.00 46.80  ? 98  THR   B CG2 1 
ATOM   3766 N N   . ILE   B 1 99  ? 38.608 -2.473  25.534  1.00 42.66  ? 99  ILE   B N   1 
ATOM   3767 C CA  . ILE   B 1 99  ? 38.187 -3.759  26.082  1.00 41.38  ? 99  ILE   B CA  1 
ATOM   3768 C C   . ILE   B 1 99  ? 38.767 -4.906  25.219  1.00 47.31  ? 99  ILE   B C   1 
ATOM   3769 O O   . ILE   B 1 99  ? 39.314 -5.858  25.765  1.00 47.10  ? 99  ILE   B O   1 
ATOM   3770 C CB  . ILE   B 1 99  ? 36.620 -3.804  26.275  1.00 43.32  ? 99  ILE   B CB  1 
ATOM   3771 C CG1 . ILE   B 1 99  ? 36.166 -2.821  27.403  1.00 43.02  ? 99  ILE   B CG1 1 
ATOM   3772 C CG2 . ILE   B 1 99  ? 36.126 -5.228  26.582  1.00 42.27  ? 99  ILE   B CG2 1 
ATOM   3773 C CD1 . ILE   B 1 99  ? 34.620 -2.446  27.463  1.00 39.59  ? 99  ILE   B CD1 1 
ATOM   3774 N N   . ARG   B 1 100 ? 38.656 -4.806  23.887  1.00 46.78  ? 100 ARG   B N   1 
ATOM   3775 C CA  . ARG   B 1 100 ? 39.178 -5.810  22.958  1.00 48.18  ? 100 ARG   B CA  1 
ATOM   3776 C C   . ARG   B 1 100 ? 40.674 -5.964  23.119  1.00 52.76  ? 100 ARG   B C   1 
ATOM   3777 O O   . ARG   B 1 100 ? 41.145 -7.087  23.223  1.00 52.64  ? 100 ARG   B O   1 
ATOM   3778 C CB  . ARG   B 1 100 ? 38.854 -5.451  21.508  1.00 52.22  ? 100 ARG   B CB  1 
ATOM   3779 C CG  . ARG   B 1 100 ? 37.562 -6.078  21.031  1.00 70.18  ? 100 ARG   B CG  1 
ATOM   3780 C CD  . ARG   B 1 100 ? 37.410 -5.969  19.526  1.00 81.69  ? 100 ARG   B CD  1 
ATOM   3781 N NE  . ARG   B 1 100 ? 36.772 -4.717  19.115  1.00 85.51  ? 100 ARG   B NE  1 
ATOM   3782 C CZ  . ARG   B 1 100 ? 37.428 -3.663  18.640  1.00 92.37  ? 100 ARG   B CZ  1 
ATOM   3783 N NH1 . ARG   B 1 100 ? 38.750 -3.695  18.513  1.00 84.96  ? 100 ARG   B NH1 1 
ATOM   3784 N NH2 . ARG   B 1 100 ? 36.767 -2.570  18.284  1.00 66.23  ? 100 ARG   B NH2 1 
ATOM   3785 N N   . ASN   B 1 101 ? 41.411 -4.842  23.174  1.00 49.23  ? 101 ASN   B N   1 
ATOM   3786 C CA  . ASN   B 1 101 ? 42.863 -4.793  23.334  1.00 49.27  ? 101 ASN   B CA  1 
ATOM   3787 C C   . ASN   B 1 101 ? 43.329 -5.460  24.637  1.00 52.13  ? 101 ASN   B C   1 
ATOM   3788 O O   . ASN   B 1 101 ? 44.372 -6.118  24.654  1.00 53.32  ? 101 ASN   B O   1 
ATOM   3789 C CB  . ASN   B 1 101 ? 43.327 -3.333  23.256  1.00 55.49  ? 101 ASN   B CB  1 
ATOM   3790 C CG  . ASN   B 1 101 ? 44.810 -3.130  23.068  1.00 94.22  ? 101 ASN   B CG  1 
ATOM   3791 O OD1 . ASN   B 1 101 ? 45.290 -2.958  21.940  1.00 92.39  ? 101 ASN   B OD1 1 
ATOM   3792 N ND2 . ASN   B 1 101 ? 45.568 -3.128  24.171  1.00 85.33  ? 101 ASN   B ND2 1 
ATOM   3793 N N   . ILE   B 1 102 ? 42.552 -5.310  25.720  1.00 46.71  ? 102 ILE   B N   1 
ATOM   3794 C CA  . ILE   B 1 102 ? 42.867 -5.892  27.028  1.00 44.91  ? 102 ILE   B CA  1 
ATOM   3795 C C   . ILE   B 1 102 ? 42.518 -7.401  27.104  1.00 49.59  ? 102 ILE   B C   1 
ATOM   3796 O O   . ILE   B 1 102 ? 43.245 -8.187  27.718  1.00 49.74  ? 102 ILE   B O   1 
ATOM   3797 C CB  . ILE   B 1 102 ? 42.234 -5.024  28.171  1.00 46.52  ? 102 ILE   B CB  1 
ATOM   3798 C CG1 . ILE   B 1 102 ? 42.953 -3.665  28.279  1.00 46.45  ? 102 ILE   B CG1 1 
ATOM   3799 C CG2 . ILE   B 1 102 ? 42.235 -5.742  29.534  1.00 45.91  ? 102 ILE   B CG2 1 
ATOM   3800 C CD1 . ILE   B 1 102 ? 42.195 -2.540  29.093  1.00 54.14  ? 102 ILE   B CD1 1 
ATOM   3801 N N   . LEU   B 1 103 ? 41.399 -7.790  26.500  1.00 46.12  ? 103 LEU   B N   1 
ATOM   3802 C CA  . LEU   B 1 103 ? 40.930 -9.174  26.525  1.00 45.20  ? 103 LEU   B CA  1 
ATOM   3803 C C   . LEU   B 1 103 ? 41.440 -10.065 25.386  1.00 47.88  ? 103 LEU   B C   1 
ATOM   3804 O O   . LEU   B 1 103 ? 41.770 -11.233 25.623  1.00 46.42  ? 103 LEU   B O   1 
ATOM   3805 C CB  . LEU   B 1 103 ? 39.388 -9.205  26.518  1.00 44.65  ? 103 LEU   B CB  1 
ATOM   3806 C CG  . LEU   B 1 103 ? 38.639 -8.634  27.724  1.00 48.75  ? 103 LEU   B CG  1 
ATOM   3807 C CD1 . LEU   B 1 103 ? 37.139 -8.785  27.529  1.00 48.69  ? 103 LEU   B CD1 1 
ATOM   3808 C CD2 . LEU   B 1 103 ? 39.035 -9.338  29.015  1.00 50.23  ? 103 LEU   B CD2 1 
ATOM   3809 N N   . GLY   B 1 104 ? 41.440 -9.520  24.166  1.00 43.91  ? 104 GLY   B N   1 
ATOM   3810 C CA  . GLY   B 1 104 ? 41.762 -10.253 22.950  1.00 44.01  ? 104 GLY   B CA  1 
ATOM   3811 C C   . GLY   B 1 104 ? 40.552 -11.118 22.614  1.00 50.06  ? 104 GLY   B C   1 
ATOM   3812 O O   . GLY   B 1 104 ? 39.473 -10.938 23.195  1.00 50.96  ? 104 GLY   B O   1 
ATOM   3813 N N   . GLY   B 1 105 ? 40.715 -12.063 21.704  1.00 45.67  ? 105 GLY   B N   1 
ATOM   3814 C CA  . GLY   B 1 105 ? 39.618 -12.943 21.327  1.00 44.50  ? 105 GLY   B CA  1 
ATOM   3815 C C   . GLY   B 1 105 ? 39.021 -12.652 19.971  1.00 46.29  ? 105 GLY   B C   1 
ATOM   3816 O O   . GLY   B 1 105 ? 39.487 -11.767 19.260  1.00 45.37  ? 105 GLY   B O   1 
ATOM   3817 N N   . THR   B 1 106 ? 37.993 -13.423 19.601  1.00 42.12  ? 106 THR   B N   1 
ATOM   3818 C CA  . THR   B 1 106 ? 37.300 -13.340 18.319  1.00 40.66  ? 106 THR   B CA  1 
ATOM   3819 C C   . THR   B 1 106 ? 35.877 -12.863 18.517  1.00 42.90  ? 106 THR   B C   1 
ATOM   3820 O O   . THR   B 1 106 ? 35.160 -13.342 19.396  1.00 42.12  ? 106 THR   B O   1 
ATOM   3821 C CB  . THR   B 1 106 ? 37.371 -14.700 17.601  1.00 47.71  ? 106 THR   B CB  1 
ATOM   3822 O OG1 . THR   B 1 106 ? 38.732 -15.110 17.541  1.00 53.05  ? 106 THR   B OG1 1 
ATOM   3823 C CG2 . THR   B 1 106 ? 36.778 -14.674 16.198  1.00 45.42  ? 106 THR   B CG2 1 
ATOM   3824 N N   . VAL   B 1 107 ? 35.490 -11.906 17.691  1.00 39.15  ? 107 VAL   B N   1 
ATOM   3825 C CA  . VAL   B 1 107 ? 34.168 -11.318 17.692  1.00 38.63  ? 107 VAL   B CA  1 
ATOM   3826 C C   . VAL   B 1 107 ? 33.284 -12.121 16.737  1.00 45.38  ? 107 VAL   B C   1 
ATOM   3827 O O   . VAL   B 1 107 ? 33.620 -12.263 15.560  1.00 44.69  ? 107 VAL   B O   1 
ATOM   3828 C CB  . VAL   B 1 107 ? 34.231 -9.821  17.311  1.00 40.27  ? 107 VAL   B CB  1 
ATOM   3829 C CG1 . VAL   B 1 107 ? 32.840 -9.251  17.111  1.00 39.64  ? 107 VAL   B CG1 1 
ATOM   3830 C CG2 . VAL   B 1 107 ? 34.998 -9.018  18.355  1.00 39.49  ? 107 VAL   B CG2 1 
ATOM   3831 N N   . PHE   B 1 108 ? 32.161 -12.647 17.255  1.00 43.32  ? 108 PHE   B N   1 
ATOM   3832 C CA  . PHE   B 1 108 ? 31.187 -13.383 16.461  1.00 43.07  ? 108 PHE   B CA  1 
ATOM   3833 C C   . PHE   B 1 108 ? 29.903 -12.600 16.439  1.00 46.70  ? 108 PHE   B C   1 
ATOM   3834 O O   . PHE   B 1 108 ? 29.413 -12.223 17.499  1.00 46.56  ? 108 PHE   B O   1 
ATOM   3835 C CB  . PHE   B 1 108 ? 30.923 -14.772 17.055  1.00 44.97  ? 108 PHE   B CB  1 
ATOM   3836 C CG  . PHE   B 1 108 ? 32.096 -15.706 16.956  1.00 46.34  ? 108 PHE   B CG  1 
ATOM   3837 C CD1 . PHE   B 1 108 ? 32.304 -16.463 15.811  1.00 48.36  ? 108 PHE   B CD1 1 
ATOM   3838 C CD2 . PHE   B 1 108 ? 33.001 -15.826 18.009  1.00 48.83  ? 108 PHE   B CD2 1 
ATOM   3839 C CE1 . PHE   B 1 108 ? 33.403 -17.319 15.716  1.00 50.31  ? 108 PHE   B CE1 1 
ATOM   3840 C CE2 . PHE   B 1 108 ? 34.102 -16.685 17.915  1.00 51.35  ? 108 PHE   B CE2 1 
ATOM   3841 C CZ  . PHE   B 1 108 ? 34.295 -17.427 16.771  1.00 49.54  ? 108 PHE   B CZ  1 
ATOM   3842 N N   . ARG   B 1 109 ? 29.353 -12.368 15.244  1.00 44.51  ? 109 ARG   B N   1 
ATOM   3843 C CA  . ARG   B 1 109 ? 28.102 -11.648 15.018  1.00 44.79  ? 109 ARG   B CA  1 
ATOM   3844 C C   . ARG   B 1 109 ? 26.991 -12.631 14.608  1.00 52.82  ? 109 ARG   B C   1 
ATOM   3845 O O   . ARG   B 1 109 ? 27.091 -13.276 13.565  1.00 54.33  ? 109 ARG   B O   1 
ATOM   3846 C CB  . ARG   B 1 109 ? 28.305 -10.507 14.003  1.00 43.70  ? 109 ARG   B CB  1 
ATOM   3847 C CG  . ARG   B 1 109 ? 28.729 -9.208  14.686  1.00 51.56  ? 109 ARG   B CG  1 
ATOM   3848 C CD  . ARG   B 1 109 ? 29.173 -8.126  13.728  1.00 64.46  ? 109 ARG   B CD  1 
ATOM   3849 N NE  . ARG   B 1 109 ? 30.614 -8.194  13.461  1.00 83.97  ? 109 ARG   B NE  1 
ATOM   3850 C CZ  . ARG   B 1 109 ? 31.547 -7.569  14.180  1.00 100.30 ? 109 ARG   B CZ  1 
ATOM   3851 N NH1 . ARG   B 1 109 ? 31.204 -6.822  15.223  1.00 85.07  ? 109 ARG   B NH1 1 
ATOM   3852 N NH2 . ARG   B 1 109 ? 32.831 -7.690  13.861  1.00 86.05  ? 109 ARG   B NH2 1 
ATOM   3853 N N   . GLU   B 1 110 ? 25.956 -12.771 15.462  1.00 50.51  ? 110 GLU   B N   1 
ATOM   3854 C CA  . GLU   B 1 110 ? 24.810 -13.670 15.278  1.00 50.48  ? 110 GLU   B CA  1 
ATOM   3855 C C   . GLU   B 1 110 ? 23.516 -12.876 15.250  1.00 56.29  ? 110 GLU   B C   1 
ATOM   3856 O O   . GLU   B 1 110 ? 23.265 -12.078 16.161  1.00 55.77  ? 110 GLU   B O   1 
ATOM   3857 C CB  . GLU   B 1 110 ? 24.731 -14.731 16.406  1.00 51.60  ? 110 GLU   B CB  1 
ATOM   3858 C CG  . GLU   B 1 110 ? 23.574 -15.714 16.217  1.00 60.03  ? 110 GLU   B CG  1 
ATOM   3859 C CD  . GLU   B 1 110 ? 23.225 -16.715 17.305  1.00 72.27  ? 110 GLU   B CD  1 
ATOM   3860 O OE1 . GLU   B 1 110 ? 22.200 -17.419 17.145  1.00 75.88  ? 110 GLU   B OE1 1 
ATOM   3861 O OE2 . GLU   B 1 110 ? 23.962 -16.805 18.310  1.00 64.86  ? 110 GLU   B OE2 1 
ATOM   3862 N N   . ALA   B 1 111 ? 22.685 -13.130 14.221  1.00 53.60  ? 111 ALA   B N   1 
ATOM   3863 C CA  . ALA   B 1 111 ? 21.393 -12.486 14.034  1.00 53.72  ? 111 ALA   B CA  1 
ATOM   3864 C C   . ALA   B 1 111 ? 20.291 -13.195 14.829  1.00 58.56  ? 111 ALA   B C   1 
ATOM   3865 O O   . ALA   B 1 111 ? 20.429 -14.378 15.152  1.00 61.04  ? 111 ALA   B O   1 
ATOM   3866 C CB  . ALA   B 1 111 ? 21.044 -12.465 12.569  1.00 54.42  ? 111 ALA   B CB  1 
ATOM   3867 N N   . ILE   B 1 112 ? 19.218 -12.467 15.167  1.00 52.23  ? 112 ILE   B N   1 
ATOM   3868 C CA  . ILE   B 1 112 ? 18.079 -13.009 15.911  1.00 51.11  ? 112 ILE   B CA  1 
ATOM   3869 C C   . ILE   B 1 112 ? 17.030 -13.230 14.862  1.00 53.65  ? 112 ILE   B C   1 
ATOM   3870 O O   . ILE   B 1 112 ? 16.576 -12.270 14.221  1.00 51.58  ? 112 ILE   B O   1 
ATOM   3871 C CB  . ILE   B 1 112 ? 17.551 -12.110 17.063  1.00 54.20  ? 112 ILE   B CB  1 
ATOM   3872 C CG1 . ILE   B 1 112 ? 18.667 -11.360 17.883  1.00 54.16  ? 112 ILE   B CG1 1 
ATOM   3873 C CG2 . ILE   B 1 112 ? 16.517 -12.847 17.919  1.00 54.73  ? 112 ILE   B CG2 1 
ATOM   3874 C CD1 . ILE   B 1 112 ? 19.722 -12.143 18.512  1.00 59.93  ? 112 ILE   B CD1 1 
ATOM   3875 N N   . ILE   B 1 113 ? 16.666 -14.512 14.671  1.00 50.44  ? 113 ILE   B N   1 
ATOM   3876 C CA  . ILE   B 1 113 ? 15.731 -14.943 13.642  1.00 49.30  ? 113 ILE   B CA  1 
ATOM   3877 C C   . ILE   B 1 113 ? 14.315 -15.027 14.099  1.00 53.36  ? 113 ILE   B C   1 
ATOM   3878 O O   . ILE   B 1 113 ? 14.008 -15.681 15.097  1.00 53.69  ? 113 ILE   B O   1 
ATOM   3879 C CB  . ILE   B 1 113 ? 16.246 -16.242 12.938  1.00 52.46  ? 113 ILE   B CB  1 
ATOM   3880 C CG1 . ILE   B 1 113 ? 17.648 -16.056 12.314  1.00 52.51  ? 113 ILE   B CG1 1 
ATOM   3881 C CG2 . ILE   B 1 113 ? 15.258 -16.830 11.927  1.00 53.72  ? 113 ILE   B CG2 1 
ATOM   3882 C CD1 . ILE   B 1 113 ? 17.870 -14.701 11.653  1.00 61.16  ? 113 ILE   B CD1 1 
ATOM   3883 N N   . CYS   B 1 114 ? 13.447 -14.356 13.353  1.00 50.37  ? 114 CYS   B N   1 
ATOM   3884 C CA  . CYS   B 1 114 ? 12.015 -14.351 13.573  1.00 50.41  ? 114 CYS   B CA  1 
ATOM   3885 C C   . CYS   B 1 114 ? 11.339 -14.769 12.270  1.00 54.15  ? 114 CYS   B C   1 
ATOM   3886 O O   . CYS   B 1 114 ? 11.667 -14.228 11.211  1.00 53.57  ? 114 CYS   B O   1 
ATOM   3887 C CB  . CYS   B 1 114 ? 11.543 -12.985 14.055  1.00 50.91  ? 114 CYS   B CB  1 
ATOM   3888 S SG  . CYS   B 1 114 ? 11.833 -12.695 15.814  1.00 54.88  ? 114 CYS   B SG  1 
ATOM   3889 N N   . LYS   B 1 115 ? 10.428 -15.763 12.349  1.00 51.25  ? 115 LYS   B N   1 
ATOM   3890 C CA  . LYS   B 1 115 ? 9.665  -16.315 11.213  1.00 50.66  ? 115 LYS   B CA  1 
ATOM   3891 C C   . LYS   B 1 115 ? 8.938  -15.252 10.376  1.00 54.57  ? 115 LYS   B C   1 
ATOM   3892 O O   . LYS   B 1 115 ? 8.943  -15.351 9.143   1.00 55.30  ? 115 LYS   B O   1 
ATOM   3893 C CB  . LYS   B 1 115 ? 8.672  -17.381 11.685  1.00 52.29  ? 115 LYS   B CB  1 
ATOM   3894 C CG  . LYS   B 1 115 ? 9.308  -18.726 12.005  1.00 57.65  ? 115 LYS   B CG  1 
ATOM   3895 C CD  . LYS   B 1 115 ? 8.407  -19.514 12.952  1.00 60.60  ? 115 LYS   B CD  1 
ATOM   3896 C CE  . LYS   B 1 115 ? 8.838  -20.946 13.114  1.00 63.78  ? 115 LYS   B CE  1 
ATOM   3897 N NZ  . LYS   B 1 115 ? 10.104 -21.081 13.875  1.00 71.59  ? 115 LYS   B NZ  1 
ATOM   3898 N N   . ASN   B 1 116 ? 8.339  -14.231 11.037  1.00 48.64  ? 116 ASN   B N   1 
ATOM   3899 C CA  . ASN   B 1 116 ? 7.619  -13.151 10.351  1.00 47.43  ? 116 ASN   B CA  1 
ATOM   3900 C C   . ASN   B 1 116 ? 8.515  -11.986 9.925   1.00 51.21  ? 116 ASN   B C   1 
ATOM   3901 O O   . ASN   B 1 116 ? 8.013  -11.018 9.362   1.00 49.20  ? 116 ASN   B O   1 
ATOM   3902 C CB  . ASN   B 1 116 ? 6.448  -12.635 11.204  1.00 44.23  ? 116 ASN   B CB  1 
ATOM   3903 C CG  . ASN   B 1 116 ? 6.793  -12.142 12.593  1.00 54.55  ? 116 ASN   B CG  1 
ATOM   3904 O OD1 . ASN   B 1 116 ? 7.800  -12.512 13.209  1.00 47.35  ? 116 ASN   B OD1 1 
ATOM   3905 N ND2 . ASN   B 1 116 ? 5.934  -11.311 13.129  1.00 47.19  ? 116 ASN   B ND2 1 
ATOM   3906 N N   . ILE   B 1 117 ? 9.825  -12.052 10.227  1.00 50.04  ? 117 ILE   B N   1 
ATOM   3907 C CA  . ILE   B 1 117 ? 10.765 -10.987 9.874   1.00 50.18  ? 117 ILE   B CA  1 
ATOM   3908 C C   . ILE   B 1 117 ? 11.652 -11.442 8.697   1.00 54.58  ? 117 ILE   B C   1 
ATOM   3909 O O   . ILE   B 1 117 ? 12.356 -12.462 8.811   1.00 53.15  ? 117 ILE   B O   1 
ATOM   3910 C CB  . ILE   B 1 117 ? 11.508 -10.336 11.106  1.00 53.15  ? 117 ILE   B CB  1 
ATOM   3911 C CG1 . ILE   B 1 117 ? 10.650 -9.216  11.773  1.00 54.43  ? 117 ILE   B CG1 1 
ATOM   3912 C CG2 . ILE   B 1 117 ? 12.820 -9.673  10.668  1.00 52.97  ? 117 ILE   B CG2 1 
ATOM   3913 C CD1 . ILE   B 1 117 ? 9.451  -9.557  12.484  1.00 61.09  ? 117 ILE   B CD1 1 
ATOM   3914 N N   . PRO   B 1 118 ? 11.581 -10.716 7.551   1.00 52.33  ? 118 PRO   B N   1 
ATOM   3915 C CA  . PRO   B 1 118 ? 12.372 -11.118 6.371   1.00 53.07  ? 118 PRO   B CA  1 
ATOM   3916 C C   . PRO   B 1 118 ? 13.889 -11.069 6.542   1.00 60.72  ? 118 PRO   B C   1 
ATOM   3917 O O   . PRO   B 1 118 ? 14.415 -10.261 7.312   1.00 60.60  ? 118 PRO   B O   1 
ATOM   3918 C CB  . PRO   B 1 118 ? 11.892 -10.163 5.267   1.00 54.52  ? 118 PRO   B CB  1 
ATOM   3919 C CG  . PRO   B 1 118 ? 11.330 -8.982  5.988   1.00 58.32  ? 118 PRO   B CG  1 
ATOM   3920 C CD  . PRO   B 1 118 ? 10.766 -9.511  7.273   1.00 53.81  ? 118 PRO   B CD  1 
ATOM   3921 N N   . ARG   B 1 119 ? 14.580 -11.958 5.801   1.00 59.96  ? 119 ARG   B N   1 
ATOM   3922 C CA  . ARG   B 1 119 ? 16.034 -12.124 5.745   1.00 59.99  ? 119 ARG   B CA  1 
ATOM   3923 C C   . ARG   B 1 119 ? 16.510 -11.804 4.330   1.00 69.52  ? 119 ARG   B C   1 
ATOM   3924 O O   . ARG   B 1 119 ? 15.686 -11.713 3.411   1.00 68.98  ? 119 ARG   B O   1 
ATOM   3925 C CB  . ARG   B 1 119 ? 16.417 -13.571 6.093   1.00 55.98  ? 119 ARG   B CB  1 
ATOM   3926 C CG  . ARG   B 1 119 ? 16.205 -13.926 7.561   1.00 63.53  ? 119 ARG   B CG  1 
ATOM   3927 C CD  . ARG   B 1 119 ? 15.194 -15.032 7.807   1.00 70.15  ? 119 ARG   B CD  1 
ATOM   3928 N NE  . ARG   B 1 119 ? 14.265 -15.218 6.695   1.00 79.85  ? 119 ARG   B NE  1 
ATOM   3929 C CZ  . ARG   B 1 119 ? 12.945 -15.262 6.815   1.00 98.28  ? 119 ARG   B CZ  1 
ATOM   3930 N NH1 . ARG   B 1 119 ? 12.376 -15.148 8.008   1.00 89.84  ? 119 ARG   B NH1 1 
ATOM   3931 N NH2 . ARG   B 1 119 ? 12.183 -15.426 5.743   1.00 85.16  ? 119 ARG   B NH2 1 
ATOM   3932 N N   . LEU   B 1 120 ? 17.848 -11.648 4.151   1.00 70.29  ? 120 LEU   B N   1 
ATOM   3933 C CA  . LEU   B 1 120 ? 18.496 -11.379 2.856   1.00 70.99  ? 120 LEU   B CA  1 
ATOM   3934 C C   . LEU   B 1 120 ? 18.262 -12.580 1.910   1.00 74.41  ? 120 LEU   B C   1 
ATOM   3935 O O   . LEU   B 1 120 ? 18.152 -12.405 0.692   1.00 73.99  ? 120 LEU   B O   1 
ATOM   3936 C CB  . LEU   B 1 120 ? 20.014 -11.135 3.063   1.00 71.33  ? 120 LEU   B CB  1 
ATOM   3937 C CG  . LEU   B 1 120 ? 20.866 -10.820 1.816   1.00 76.44  ? 120 LEU   B CG  1 
ATOM   3938 C CD1 . LEU   B 1 120 ? 20.530 -9.441  1.231   1.00 76.68  ? 120 LEU   B CD1 1 
ATOM   3939 C CD2 . LEU   B 1 120 ? 22.353 -10.926 2.127   1.00 79.23  ? 120 LEU   B CD2 1 
ATOM   3940 N N   . VAL   B 1 121 ? 18.184 -13.791 2.502   1.00 70.05  ? 121 VAL   B N   1 
ATOM   3941 C CA  . VAL   B 1 121 ? 17.951 -15.078 1.850   1.00 69.54  ? 121 VAL   B CA  1 
ATOM   3942 C C   . VAL   B 1 121 ? 16.871 -15.754 2.699   1.00 74.51  ? 121 VAL   B C   1 
ATOM   3943 O O   . VAL   B 1 121 ? 17.113 -16.079 3.869   1.00 74.77  ? 121 VAL   B O   1 
ATOM   3944 C CB  . VAL   B 1 121 ? 19.274 -15.912 1.724   1.00 72.61  ? 121 VAL   B CB  1 
ATOM   3945 C CG1 . VAL   B 1 121 ? 19.020 -17.408 1.504   1.00 72.12  ? 121 VAL   B CG1 1 
ATOM   3946 C CG2 . VAL   B 1 121 ? 20.191 -15.346 0.640   1.00 72.13  ? 121 VAL   B CG2 1 
ATOM   3947 N N   . SER   B 1 122 ? 15.669 -15.934 2.104   1.00 71.01  ? 122 SER   B N   1 
ATOM   3948 C CA  . SER   B 1 122 ? 14.483 -16.547 2.714   1.00 70.39  ? 122 SER   B CA  1 
ATOM   3949 C C   . SER   B 1 122 ? 14.753 -17.932 3.304   1.00 75.03  ? 122 SER   B C   1 
ATOM   3950 O O   . SER   B 1 122 ? 14.100 -18.322 4.274   1.00 74.67  ? 122 SER   B O   1 
ATOM   3951 C CB  . SER   B 1 122 ? 13.350 -16.623 1.701   1.00 73.37  ? 122 SER   B CB  1 
ATOM   3952 O OG  . SER   B 1 122 ? 13.150 -15.376 1.057   1.00 82.48  ? 122 SER   B OG  1 
ATOM   3953 N N   . GLY   B 1 123 ? 15.714 -18.647 2.719   1.00 72.61  ? 123 GLY   B N   1 
ATOM   3954 C CA  . GLY   B 1 123 ? 16.122 -19.981 3.147   1.00 72.92  ? 123 GLY   B CA  1 
ATOM   3955 C C   . GLY   B 1 123 ? 16.671 -20.053 4.558   1.00 77.85  ? 123 GLY   B C   1 
ATOM   3956 O O   . GLY   B 1 123 ? 16.499 -21.075 5.231   1.00 77.88  ? 123 GLY   B O   1 
ATOM   3957 N N   . TRP   B 1 124 ? 17.328 -18.958 5.018   1.00 74.66  ? 124 TRP   B N   1 
ATOM   3958 C CA  . TRP   B 1 124 ? 17.925 -18.838 6.352   1.00 74.14  ? 124 TRP   B CA  1 
ATOM   3959 C C   . TRP   B 1 124 ? 16.853 -18.925 7.455   1.00 76.80  ? 124 TRP   B C   1 
ATOM   3960 O O   . TRP   B 1 124 ? 16.096 -17.983 7.689   1.00 75.77  ? 124 TRP   B O   1 
ATOM   3961 C CB  . TRP   B 1 124 ? 18.808 -17.578 6.455   1.00 73.03  ? 124 TRP   B CB  1 
ATOM   3962 C CG  . TRP   B 1 124 ? 19.928 -17.504 5.444   1.00 74.30  ? 124 TRP   B CG  1 
ATOM   3963 C CD1 . TRP   B 1 124 ? 20.478 -18.539 4.736   1.00 77.13  ? 124 TRP   B CD1 1 
ATOM   3964 C CD2 . TRP   B 1 124 ? 20.660 -16.328 5.065   1.00 74.22  ? 124 TRP   B CD2 1 
ATOM   3965 N NE1 . TRP   B 1 124 ? 21.477 -18.074 3.914   1.00 76.31  ? 124 TRP   B NE1 1 
ATOM   3966 C CE2 . TRP   B 1 124 ? 21.619 -16.723 4.102   1.00 77.93  ? 124 TRP   B CE2 1 
ATOM   3967 C CE3 . TRP   B 1 124 ? 20.592 -14.972 5.438   1.00 75.48  ? 124 TRP   B CE3 1 
ATOM   3968 C CZ2 . TRP   B 1 124 ? 22.505 -15.810 3.508   1.00 77.28  ? 124 TRP   B CZ2 1 
ATOM   3969 C CZ3 . TRP   B 1 124 ? 21.466 -14.069 4.846   1.00 76.97  ? 124 TRP   B CZ3 1 
ATOM   3970 C CH2 . TRP   B 1 124 ? 22.406 -14.488 3.892   1.00 77.64  ? 124 TRP   B CH2 1 
ATOM   3971 N N   . VAL   B 1 125 ? 16.775 -20.108 8.082   1.00 72.77  ? 125 VAL   B N   1 
ATOM   3972 C CA  . VAL   B 1 125 ? 15.825 -20.482 9.140   1.00 71.86  ? 125 VAL   B CA  1 
ATOM   3973 C C   . VAL   B 1 125 ? 16.572 -20.526 10.479  1.00 73.80  ? 125 VAL   B C   1 
ATOM   3974 O O   . VAL   B 1 125 ? 15.999 -20.223 11.532  1.00 74.54  ? 125 VAL   B O   1 
ATOM   3975 C CB  . VAL   B 1 125 ? 15.120 -21.827 8.759   1.00 75.55  ? 125 VAL   B CB  1 
ATOM   3976 C CG1 . VAL   B 1 125 ? 14.403 -22.483 9.945   1.00 75.30  ? 125 VAL   B CG1 1 
ATOM   3977 C CG2 . VAL   B 1 125 ? 14.156 -21.619 7.593   1.00 75.19  ? 125 VAL   B CG2 1 
ATOM   3978 N N   . LYS   B 1 126 ? 17.847 -20.901 10.429  1.00 67.63  ? 126 LYS   B N   1 
ATOM   3979 C CA  . LYS   B 1 126 ? 18.709 -20.947 11.601  1.00 66.47  ? 126 LYS   B CA  1 
ATOM   3980 C C   . LYS   B 1 126 ? 19.776 -19.848 11.399  1.00 68.43  ? 126 LYS   B C   1 
ATOM   3981 O O   . LYS   B 1 126 ? 20.143 -19.565 10.248  1.00 66.69  ? 126 LYS   B O   1 
ATOM   3982 C CB  . LYS   B 1 126 ? 19.343 -22.336 11.787  1.00 68.86  ? 126 LYS   B CB  1 
ATOM   3983 C CG  . LYS   B 1 126 ? 18.371 -23.509 11.790  1.00 82.65  ? 126 LYS   B CG  1 
ATOM   3984 C CD  . LYS   B 1 126 ? 19.130 -24.822 11.805  1.00 95.19  ? 126 LYS   B CD  1 
ATOM   3985 C CE  . LYS   B 1 126 ? 18.216 -26.021 11.775  1.00 108.54 ? 126 LYS   B CE  1 
ATOM   3986 N NZ  . LYS   B 1 126 ? 18.982 -27.296 11.827  1.00 116.82 ? 126 LYS   B NZ  1 
ATOM   3987 N N   . PRO   B 1 127 ? 20.261 -19.181 12.473  1.00 64.79  ? 127 PRO   B N   1 
ATOM   3988 C CA  . PRO   B 1 127 ? 21.245 -18.102 12.269  1.00 63.90  ? 127 PRO   B CA  1 
ATOM   3989 C C   . PRO   B 1 127 ? 22.610 -18.550 11.759  1.00 62.85  ? 127 PRO   B C   1 
ATOM   3990 O O   . PRO   B 1 127 ? 23.017 -19.691 11.966  1.00 61.22  ? 127 PRO   B O   1 
ATOM   3991 C CB  . PRO   B 1 127 ? 21.359 -17.438 13.657  1.00 66.09  ? 127 PRO   B CB  1 
ATOM   3992 C CG  . PRO   B 1 127 ? 20.176 -17.936 14.445  1.00 70.86  ? 127 PRO   B CG  1 
ATOM   3993 C CD  . PRO   B 1 127 ? 19.920 -19.322 13.903  1.00 66.46  ? 127 PRO   B CD  1 
ATOM   3994 N N   . ILE   B 1 128 ? 23.303 -17.623 11.077  1.00 56.78  ? 128 ILE   B N   1 
ATOM   3995 C CA  . ILE   B 1 128 ? 24.659 -17.801 10.568  1.00 55.16  ? 128 ILE   B CA  1 
ATOM   3996 C C   . ILE   B 1 128 ? 25.525 -16.935 11.488  1.00 54.51  ? 128 ILE   B C   1 
ATOM   3997 O O   . ILE   B 1 128 ? 25.301 -15.726 11.583  1.00 54.46  ? 128 ILE   B O   1 
ATOM   3998 C CB  . ILE   B 1 128 ? 24.800 -17.374 9.082   1.00 58.64  ? 128 ILE   B CB  1 
ATOM   3999 C CG1 . ILE   B 1 128 ? 23.861 -18.190 8.173   1.00 59.40  ? 128 ILE   B CG1 1 
ATOM   4000 C CG2 . ILE   B 1 128 ? 26.273 -17.450 8.611   1.00 58.84  ? 128 ILE   B CG2 1 
ATOM   4001 C CD1 . ILE   B 1 128 ? 23.444 -17.464 6.952   1.00 66.03  ? 128 ILE   B CD1 1 
ATOM   4002 N N   . ILE   B 1 129 ? 26.488 -17.555 12.171  1.00 47.75  ? 129 ILE   B N   1 
ATOM   4003 C CA  . ILE   B 1 129 ? 27.414 -16.888 13.086  1.00 46.33  ? 129 ILE   B CA  1 
ATOM   4004 C C   . ILE   B 1 129 ? 28.722 -16.622 12.352  1.00 51.33  ? 129 ILE   B C   1 
ATOM   4005 O O   . ILE   B 1 129 ? 29.410 -17.564 11.979  1.00 51.00  ? 129 ILE   B O   1 
ATOM   4006 C CB  . ILE   B 1 129 ? 27.575 -17.730 14.376  1.00 48.48  ? 129 ILE   B CB  1 
ATOM   4007 C CG1 . ILE   B 1 129 ? 26.212 -17.861 15.076  1.00 48.02  ? 129 ILE   B CG1 1 
ATOM   4008 C CG2 . ILE   B 1 129 ? 28.658 -17.168 15.305  1.00 49.24  ? 129 ILE   B CG2 1 
ATOM   4009 C CD1 . ILE   B 1 129 ? 26.192 -18.545 16.374  1.00 56.92  ? 129 ILE   B CD1 1 
ATOM   4010 N N   . ILE   B 1 130 ? 29.054 -15.341 12.133  1.00 50.22  ? 130 ILE   B N   1 
ATOM   4011 C CA  . ILE   B 1 130 ? 30.272 -14.906 11.424  1.00 50.31  ? 130 ILE   B CA  1 
ATOM   4012 C C   . ILE   B 1 130 ? 31.362 -14.319 12.352  1.00 55.22  ? 130 ILE   B C   1 
ATOM   4013 O O   . ILE   B 1 130 ? 31.137 -13.321 13.033  1.00 53.34  ? 130 ILE   B O   1 
ATOM   4014 C CB  . ILE   B 1 130 ? 29.935 -14.007 10.199  1.00 52.77  ? 130 ILE   B CB  1 
ATOM   4015 C CG1 . ILE   B 1 130 ? 29.087 -14.791 9.171   1.00 53.02  ? 130 ILE   B CG1 1 
ATOM   4016 C CG2 . ILE   B 1 130 ? 31.201 -13.439 9.546   1.00 53.30  ? 130 ILE   B CG2 1 
ATOM   4017 C CD1 . ILE   B 1 130 ? 28.275 -13.927 8.141   1.00 55.19  ? 130 ILE   B CD1 1 
ATOM   4018 N N   . GLY   B 1 131 ? 32.532 -14.956 12.341  1.00 54.74  ? 131 GLY   B N   1 
ATOM   4019 C CA  . GLY   B 1 131 ? 33.690 -14.554 13.131  1.00 55.67  ? 131 GLY   B CA  1 
ATOM   4020 C C   . GLY   B 1 131 ? 34.846 -14.049 12.292  1.00 61.20  ? 131 GLY   B C   1 
ATOM   4021 O O   . GLY   B 1 131 ? 35.341 -14.775 11.433  1.00 58.70  ? 131 GLY   B O   1 
ATOM   4022 N N   . HIS   B 1 132 ? 35.284 -12.800 12.532  1.00 62.09  ? 132 HIS   B N   1 
ATOM   4023 C CA  . HIS   B 1 132 ? 36.406 -12.209 11.794  1.00 64.16  ? 132 HIS   B CA  1 
ATOM   4024 C C   . HIS   B 1 132 ? 37.688 -12.316 12.596  1.00 70.63  ? 132 HIS   B C   1 
ATOM   4025 O O   . HIS   B 1 132 ? 37.652 -12.196 13.835  1.00 70.70  ? 132 HIS   B O   1 
ATOM   4026 C CB  . HIS   B 1 132 ? 36.118 -10.772 11.344  1.00 65.83  ? 132 HIS   B CB  1 
ATOM   4027 C CG  . HIS   B 1 132 ? 34.997 -10.675 10.354  1.00 70.09  ? 132 HIS   B CG  1 
ATOM   4028 N ND1 . HIS   B 1 132 ? 35.236 -10.693 8.990   1.00 72.33  ? 132 HIS   B ND1 1 
ATOM   4029 C CD2 . HIS   B 1 132 ? 33.660 -10.579 10.566  1.00 72.31  ? 132 HIS   B CD2 1 
ATOM   4030 C CE1 . HIS   B 1 132 ? 34.044 -10.594 8.418   1.00 71.91  ? 132 HIS   B CE1 1 
ATOM   4031 N NE2 . HIS   B 1 132 ? 33.066 -10.525 9.327   1.00 72.17  ? 132 HIS   B NE2 1 
ATOM   4032 N N   . HIS   B 1 133 ? 38.817 -12.570 11.885  1.00 68.44  ? 133 HIS   B N   1 
ATOM   4033 C CA  . HIS   B 1 133 ? 40.138 -12.766 12.484  1.00 69.40  ? 133 HIS   B CA  1 
ATOM   4034 C C   . HIS   B 1 133 ? 40.577 -11.797 13.594  1.00 74.59  ? 133 HIS   B C   1 
ATOM   4035 O O   . HIS   B 1 133 ? 40.525 -10.569 13.420  1.00 74.20  ? 133 HIS   B O   1 
ATOM   4036 C CB  . HIS   B 1 133 ? 41.255 -13.045 11.438  1.00 70.32  ? 133 HIS   B CB  1 
ATOM   4037 C CG  . HIS   B 1 133 ? 42.636 -13.147 12.035  1.00 74.07  ? 133 HIS   B CG  1 
ATOM   4038 N ND1 . HIS   B 1 133 ? 43.664 -12.316 11.619  1.00 75.91  ? 133 HIS   B ND1 1 
ATOM   4039 C CD2 . HIS   B 1 133 ? 43.099 -13.949 13.032  1.00 76.39  ? 133 HIS   B CD2 1 
ATOM   4040 C CE1 . HIS   B 1 133 ? 44.714 -12.641 12.363  1.00 75.65  ? 133 HIS   B CE1 1 
ATOM   4041 N NE2 . HIS   B 1 133 ? 44.420 -13.613 13.234  1.00 76.12  ? 133 HIS   B NE2 1 
ATOM   4042 N N   . ALA   B 1 134 ? 41.000 -12.402 14.741  1.00 70.87  ? 134 ALA   B N   1 
ATOM   4043 C CA  . ALA   B 1 134 ? 41.541 -11.788 15.957  1.00 98.87  ? 134 ALA   B CA  1 
ATOM   4044 C C   . ALA   B 1 134 ? 41.890 -12.881 16.983  1.00 115.98 ? 134 ALA   B C   1 
ATOM   4045 O O   . ALA   B 1 134 ? 42.797 -13.694 16.762  1.00 63.12  ? 134 ALA   B O   1 
ATOM   4046 C CB  . ALA   B 1 134 ? 40.565 -10.777 16.549  1.00 99.54  ? 134 ALA   B CB  1 
ATOM   4047 N N   . ARG   B 1 140 ? 51.183 -3.783  14.278  1.00 71.46  ? 140 ARG   B N   1 
ATOM   4048 C CA  . ARG   B 1 140 ? 50.375 -4.519  13.306  1.00 71.01  ? 140 ARG   B CA  1 
ATOM   4049 C C   . ARG   B 1 140 ? 50.998 -4.526  11.865  1.00 72.82  ? 140 ARG   B C   1 
ATOM   4050 O O   . ARG   B 1 140 ? 51.259 -5.605  11.307  1.00 73.32  ? 140 ARG   B O   1 
ATOM   4051 C CB  . ARG   B 1 140 ? 48.919 -3.992  13.313  1.00 71.61  ? 140 ARG   B CB  1 
ATOM   4052 N N   . ALA   B 1 141 ? 51.227 -3.323  11.278  1.00 65.14  ? 141 ALA   B N   1 
ATOM   4053 C CA  . ALA   B 1 141 ? 51.787 -3.152  9.935   1.00 62.64  ? 141 ALA   B CA  1 
ATOM   4054 C C   . ALA   B 1 141 ? 52.808 -2.016  9.857   1.00 62.68  ? 141 ALA   B C   1 
ATOM   4055 O O   . ALA   B 1 141 ? 52.652 -0.976  10.496  1.00 62.08  ? 141 ALA   B O   1 
ATOM   4056 C CB  . ALA   B 1 141 ? 50.679 -2.930  8.922   1.00 63.07  ? 141 ALA   B CB  1 
ATOM   4057 N N   . THR   B 1 142 ? 53.851 -2.224  9.059   1.00 56.81  ? 142 THR   B N   1 
ATOM   4058 C CA  . THR   B 1 142 ? 54.915 -1.251  8.890   1.00 55.64  ? 142 THR   B CA  1 
ATOM   4059 C C   . THR   B 1 142 ? 54.804 -0.569  7.533   1.00 55.70  ? 142 THR   B C   1 
ATOM   4060 O O   . THR   B 1 142 ? 55.358 -1.061  6.550   1.00 55.44  ? 142 THR   B O   1 
ATOM   4061 C CB  . THR   B 1 142 ? 56.284 -1.895  9.169   1.00 64.54  ? 142 THR   B CB  1 
ATOM   4062 O OG1 . THR   B 1 142 ? 56.203 -2.663  10.371  1.00 66.42  ? 142 THR   B OG1 1 
ATOM   4063 C CG2 . THR   B 1 142 ? 57.382 -0.865  9.297   1.00 63.91  ? 142 THR   B CG2 1 
ATOM   4064 N N   . ASP   B 1 143 ? 54.096 0.576   7.495   1.00 49.21  ? 143 ASP   B N   1 
ATOM   4065 C CA  . ASP   B 1 143 ? 53.886 1.364   6.279   1.00 47.31  ? 143 ASP   B CA  1 
ATOM   4066 C C   . ASP   B 1 143 ? 54.798 2.560   6.261   1.00 48.09  ? 143 ASP   B C   1 
ATOM   4067 O O   . ASP   B 1 143 ? 55.117 3.093   7.320   1.00 49.58  ? 143 ASP   B O   1 
ATOM   4068 C CB  . ASP   B 1 143 ? 52.399 1.741   6.090   1.00 48.90  ? 143 ASP   B CB  1 
ATOM   4069 C CG  . ASP   B 1 143 ? 51.796 2.714   7.096   1.00 51.76  ? 143 ASP   B CG  1 
ATOM   4070 O OD1 . ASP   B 1 143 ? 51.950 2.487   8.319   1.00 50.26  ? 143 ASP   B OD1 1 
ATOM   4071 O OD2 . ASP   B 1 143 ? 51.159 3.683   6.660   1.00 55.89  ? 143 ASP   B OD2 1 
ATOM   4072 N N   . PHE   B 1 144 ? 55.239 2.970   5.062   1.00 40.41  ? 144 PHE   B N   1 
ATOM   4073 C CA  . PHE   B 1 144 ? 56.170 4.082   4.865   1.00 38.40  ? 144 PHE   B CA  1 
ATOM   4074 C C   . PHE   B 1 144 ? 56.114 4.611   3.447   1.00 43.03  ? 144 PHE   B C   1 
ATOM   4075 O O   . PHE   B 1 144 ? 55.655 3.919   2.535   1.00 42.57  ? 144 PHE   B O   1 
ATOM   4076 C CB  . PHE   B 1 144 ? 57.622 3.630   5.190   1.00 39.32  ? 144 PHE   B CB  1 
ATOM   4077 C CG  . PHE   B 1 144 ? 58.137 2.442   4.397   1.00 40.03  ? 144 PHE   B CG  1 
ATOM   4078 C CD1 . PHE   B 1 144 ? 57.850 1.140   4.794   1.00 41.81  ? 144 PHE   B CD1 1 
ATOM   4079 C CD2 . PHE   B 1 144 ? 58.919 2.629   3.263   1.00 41.81  ? 144 PHE   B CD2 1 
ATOM   4080 C CE1 . PHE   B 1 144 ? 58.329 0.048   4.064   1.00 42.72  ? 144 PHE   B CE1 1 
ATOM   4081 C CE2 . PHE   B 1 144 ? 59.397 1.535   2.529   1.00 44.16  ? 144 PHE   B CE2 1 
ATOM   4082 C CZ  . PHE   B 1 144 ? 59.103 0.251   2.938   1.00 41.93  ? 144 PHE   B CZ  1 
ATOM   4083 N N   . VAL   B 1 145 ? 56.608 5.830   3.252   1.00 40.59  ? 145 VAL   B N   1 
ATOM   4084 C CA  . VAL   B 1 145 ? 56.664 6.431   1.925   1.00 40.45  ? 145 VAL   B CA  1 
ATOM   4085 C C   . VAL   B 1 145 ? 57.990 6.067   1.254   1.00 45.15  ? 145 VAL   B C   1 
ATOM   4086 O O   . VAL   B 1 145 ? 59.037 6.062   1.905   1.00 44.08  ? 145 VAL   B O   1 
ATOM   4087 C CB  . VAL   B 1 145 ? 56.267 7.953   1.799   1.00 43.68  ? 145 VAL   B CB  1 
ATOM   4088 C CG1 . VAL   B 1 145 ? 55.525 8.472   3.018   1.00 42.84  ? 145 VAL   B CG1 1 
ATOM   4089 C CG2 . VAL   B 1 145 ? 57.445 8.848   1.445   1.00 43.56  ? 145 VAL   B CG2 1 
ATOM   4090 N N   . VAL   B 1 146 ? 57.923 5.739   -0.046  1.00 42.64  ? 146 VAL   B N   1 
ATOM   4091 C CA  . VAL   B 1 146 ? 59.069 5.388   -0.884  1.00 41.67  ? 146 VAL   B CA  1 
ATOM   4092 C C   . VAL   B 1 146 ? 59.278 6.725   -1.559  1.00 48.95  ? 146 VAL   B C   1 
ATOM   4093 O O   . VAL   B 1 146 ? 58.432 7.110   -2.370  1.00 49.96  ? 146 VAL   B O   1 
ATOM   4094 C CB  . VAL   B 1 146 ? 58.720 4.229   -1.860  1.00 43.04  ? 146 VAL   B CB  1 
ATOM   4095 C CG1 . VAL   B 1 146 ? 59.856 3.957   -2.832  1.00 42.19  ? 146 VAL   B CG1 1 
ATOM   4096 C CG2 . VAL   B 1 146 ? 58.358 2.964   -1.089  1.00 42.33  ? 146 VAL   B CG2 1 
ATOM   4097 N N   . PRO   B 1 147 ? 60.310 7.506   -1.142  1.00 47.40  ? 147 PRO   B N   1 
ATOM   4098 C CA  . PRO   B 1 147 ? 60.483 8.867   -1.690  1.00 47.43  ? 147 PRO   B CA  1 
ATOM   4099 C C   . PRO   B 1 147 ? 60.748 8.983   -3.175  1.00 52.47  ? 147 PRO   B C   1 
ATOM   4100 O O   . PRO   B 1 147 ? 60.322 9.957   -3.770  1.00 53.81  ? 147 PRO   B O   1 
ATOM   4101 C CB  . PRO   B 1 147 ? 61.625 9.466   -0.855  1.00 49.07  ? 147 PRO   B CB  1 
ATOM   4102 C CG  . PRO   B 1 147 ? 61.804 8.555   0.291   1.00 53.79  ? 147 PRO   B CG  1 
ATOM   4103 C CD  . PRO   B 1 147 ? 61.355 7.205   -0.141  1.00 49.27  ? 147 PRO   B CD  1 
ATOM   4104 N N   . GLY   B 1 148 ? 61.431 8.007   -3.753  1.00 49.08  ? 148 GLY   B N   1 
ATOM   4105 C CA  . GLY   B 1 148 ? 61.749 8.003   -5.176  1.00 48.74  ? 148 GLY   B CA  1 
ATOM   4106 C C   . GLY   B 1 148 ? 62.164 6.634   -5.678  1.00 53.16  ? 148 GLY   B C   1 
ATOM   4107 O O   . GLY   B 1 148 ? 61.976 5.648   -4.956  1.00 52.50  ? 148 GLY   B O   1 
ATOM   4108 N N   . PRO   B 1 149 ? 62.751 6.542   -6.912  1.00 49.38  ? 149 PRO   B N   1 
ATOM   4109 C CA  . PRO   B 1 149 ? 63.152 5.229   -7.449  1.00 48.28  ? 149 PRO   B CA  1 
ATOM   4110 C C   . PRO   B 1 149 ? 64.102 4.442   -6.565  1.00 51.28  ? 149 PRO   B C   1 
ATOM   4111 O O   . PRO   B 1 149 ? 64.855 5.023   -5.775  1.00 50.77  ? 149 PRO   B O   1 
ATOM   4112 C CB  . PRO   B 1 149 ? 63.798 5.574   -8.799  1.00 49.74  ? 149 PRO   B CB  1 
ATOM   4113 C CG  . PRO   B 1 149 ? 63.218 6.879   -9.181  1.00 54.13  ? 149 PRO   B CG  1 
ATOM   4114 C CD  . PRO   B 1 149 ? 63.040 7.618   -7.888  1.00 50.19  ? 149 PRO   B CD  1 
ATOM   4115 N N   . GLY   B 1 150 ? 64.053 3.123   -6.716  1.00 46.04  ? 150 GLY   B N   1 
ATOM   4116 C CA  . GLY   B 1 150 ? 64.886 2.205   -5.956  1.00 44.79  ? 150 GLY   B CA  1 
ATOM   4117 C C   . GLY   B 1 150 ? 64.112 0.961   -5.606  1.00 48.05  ? 150 GLY   B C   1 
ATOM   4118 O O   . GLY   B 1 150 ? 62.892 0.934   -5.766  1.00 47.46  ? 150 GLY   B O   1 
ATOM   4119 N N   . LYS   B 1 151 ? 64.799 -0.082  -5.147  1.00 45.08  ? 151 LYS   B N   1 
ATOM   4120 C CA  . LYS   B 1 151 ? 64.074 -1.298  -4.821  1.00 45.47  ? 151 LYS   B CA  1 
ATOM   4121 C C   . LYS   B 1 151 ? 63.629 -1.502  -3.370  1.00 48.07  ? 151 LYS   B C   1 
ATOM   4122 O O   . LYS   B 1 151 ? 64.398 -1.252  -2.431  1.00 49.03  ? 151 LYS   B O   1 
ATOM   4123 C CB  . LYS   B 1 151 ? 64.687 -2.563  -5.463  1.00 48.90  ? 151 LYS   B CB  1 
ATOM   4124 C CG  . LYS   B 1 151 ? 66.124 -2.884  -5.104  1.00 67.47  ? 151 LYS   B CG  1 
ATOM   4125 C CD  . LYS   B 1 151 ? 66.668 -3.960  -6.039  1.00 79.86  ? 151 LYS   B CD  1 
ATOM   4126 C CE  . LYS   B 1 151 ? 68.165 -4.130  -5.922  1.00 96.00  ? 151 LYS   B CE  1 
ATOM   4127 N NZ  . LYS   B 1 151 ? 68.914 -3.078  -6.663  1.00 103.23 ? 151 LYS   B NZ  1 
ATOM   4128 N N   . VAL   B 1 152 ? 62.366 -1.954  -3.208  1.00 40.40  ? 152 VAL   B N   1 
ATOM   4129 C CA  . VAL   B 1 152 ? 61.765 -2.286  -1.922  1.00 38.90  ? 152 VAL   B CA  1 
ATOM   4130 C C   . VAL   B 1 152 ? 61.698 -3.808  -1.898  1.00 43.27  ? 152 VAL   B C   1 
ATOM   4131 O O   . VAL   B 1 152 ? 61.095 -4.443  -2.770  1.00 43.82  ? 152 VAL   B O   1 
ATOM   4132 C CB  . VAL   B 1 152 ? 60.397 -1.614  -1.647  1.00 42.12  ? 152 VAL   B CB  1 
ATOM   4133 C CG1 . VAL   B 1 152 ? 59.762 -2.139  -0.356  1.00 41.19  ? 152 VAL   B CG1 1 
ATOM   4134 C CG2 . VAL   B 1 152 ? 60.532 -0.094  -1.615  1.00 41.69  ? 152 VAL   B CG2 1 
ATOM   4135 N N   . GLU   B 1 153 ? 62.381 -4.383  -0.931  1.00 39.24  ? 153 GLU   B N   1 
ATOM   4136 C CA  . GLU   B 1 153 ? 62.477 -5.813  -0.746  1.00 38.80  ? 153 GLU   B CA  1 
ATOM   4137 C C   . GLU   B 1 153 ? 62.084 -6.146  0.683   1.00 41.68  ? 153 GLU   B C   1 
ATOM   4138 O O   . GLU   B 1 153 ? 62.186 -5.296  1.564   1.00 41.32  ? 153 GLU   B O   1 
ATOM   4139 C CB  . GLU   B 1 153 ? 63.915 -6.296  -1.042  1.00 40.20  ? 153 GLU   B CB  1 
ATOM   4140 C CG  . GLU   B 1 153 ? 64.395 -5.970  -2.449  1.00 51.51  ? 153 GLU   B CG  1 
ATOM   4141 C CD  . GLU   B 1 153 ? 65.883 -6.107  -2.701  1.00 75.21  ? 153 GLU   B CD  1 
ATOM   4142 O OE1 . GLU   B 1 153 ? 66.676 -5.468  -1.971  1.00 72.19  ? 153 GLU   B OE1 1 
ATOM   4143 O OE2 . GLU   B 1 153 ? 66.255 -6.843  -3.643  1.00 71.37  ? 153 GLU   B OE2 1 
ATOM   4144 N N   . ILE   B 1 154 ? 61.615 -7.369  0.896   1.00 37.94  ? 154 ILE   B N   1 
ATOM   4145 C CA  . ILE   B 1 154 ? 61.208 -7.904  2.194   1.00 38.67  ? 154 ILE   B CA  1 
ATOM   4146 C C   . ILE   B 1 154 ? 62.084 -9.129  2.413   1.00 44.25  ? 154 ILE   B C   1 
ATOM   4147 O O   . ILE   B 1 154 ? 62.228 -9.964  1.522   1.00 43.62  ? 154 ILE   B O   1 
ATOM   4148 C CB  . ILE   B 1 154 ? 59.678 -8.144  2.316   1.00 41.51  ? 154 ILE   B CB  1 
ATOM   4149 C CG1 . ILE   B 1 154 ? 59.289 -8.534  3.757   1.00 41.14  ? 154 ILE   B CG1 1 
ATOM   4150 C CG2 . ILE   B 1 154 ? 59.144 -9.137  1.233   1.00 42.60  ? 154 ILE   B CG2 1 
ATOM   4151 C CD1 . ILE   B 1 154 ? 57.835 -8.232  4.135   1.00 45.74  ? 154 ILE   B CD1 1 
ATOM   4152 N N   . THR   B 1 155 ? 62.724 -9.188  3.562   1.00 43.00  ? 155 THR   B N   1 
ATOM   4153 C CA  . THR   B 1 155 ? 63.685 -10.229 3.856   1.00 43.87  ? 155 THR   B CA  1 
ATOM   4154 C C   . THR   B 1 155 ? 63.438 -11.001 5.129   1.00 48.87  ? 155 THR   B C   1 
ATOM   4155 O O   . THR   B 1 155 ? 63.129 -10.418 6.157   1.00 50.40  ? 155 THR   B O   1 
ATOM   4156 C CB  . THR   B 1 155 ? 65.117 -9.618  3.786   1.00 55.98  ? 155 THR   B CB  1 
ATOM   4157 O OG1 . THR   B 1 155 ? 66.106 -10.613 4.075   1.00 61.10  ? 155 THR   B OG1 1 
ATOM   4158 C CG2 . THR   B 1 155 ? 65.304 -8.436  4.730   1.00 55.46  ? 155 THR   B CG2 1 
ATOM   4159 N N   . TYR   B 1 156 ? 63.614 -12.315 5.057   1.00 44.51  ? 156 TYR   B N   1 
ATOM   4160 C CA  . TYR   B 1 156 ? 63.498 -13.202 6.199   1.00 43.66  ? 156 TYR   B CA  1 
ATOM   4161 C C   . TYR   B 1 156 ? 64.873 -13.802 6.479   1.00 48.00  ? 156 TYR   B C   1 
ATOM   4162 O O   . TYR   B 1 156 ? 65.523 -14.337 5.570   1.00 46.77  ? 156 TYR   B O   1 
ATOM   4163 C CB  . TYR   B 1 156 ? 62.437 -14.312 5.998   1.00 43.74  ? 156 TYR   B CB  1 
ATOM   4164 C CG  . TYR   B 1 156 ? 62.438 -15.353 7.107   1.00 44.72  ? 156 TYR   B CG  1 
ATOM   4165 C CD1 . TYR   B 1 156 ? 62.699 -16.694 6.833   1.00 46.44  ? 156 TYR   B CD1 1 
ATOM   4166 C CD2 . TYR   B 1 156 ? 62.227 -14.990 8.436   1.00 44.90  ? 156 TYR   B CD2 1 
ATOM   4167 C CE1 . TYR   B 1 156 ? 62.719 -17.652 7.848   1.00 46.79  ? 156 TYR   B CE1 1 
ATOM   4168 C CE2 . TYR   B 1 156 ? 62.267 -15.936 9.461   1.00 45.63  ? 156 TYR   B CE2 1 
ATOM   4169 C CZ  . TYR   B 1 156 ? 62.499 -17.269 9.162   1.00 51.40  ? 156 TYR   B CZ  1 
ATOM   4170 O OH  . TYR   B 1 156 ? 62.511 -18.211 10.165  1.00 47.60  ? 156 TYR   B OH  1 
ATOM   4171 N N   . THR   B 1 157 ? 65.307 -13.692 7.746   1.00 45.77  ? 157 THR   B N   1 
ATOM   4172 C CA  . THR   B 1 157 ? 66.565 -14.235 8.220   1.00 46.24  ? 157 THR   B CA  1 
ATOM   4173 C C   . THR   B 1 157 ? 66.297 -15.039 9.501   1.00 51.62  ? 157 THR   B C   1 
ATOM   4174 O O   . THR   B 1 157 ? 66.044 -14.436 10.552  1.00 51.71  ? 157 THR   B O   1 
ATOM   4175 C CB  . THR   B 1 157 ? 67.652 -13.161 8.364   1.00 56.51  ? 157 THR   B CB  1 
ATOM   4176 O OG1 . THR   B 1 157 ? 67.701 -12.378 7.176   1.00 61.96  ? 157 THR   B OG1 1 
ATOM   4177 C CG2 . THR   B 1 157 ? 69.031 -13.765 8.607   1.00 54.67  ? 157 THR   B CG2 1 
ATOM   4178 N N   . PRO   B 1 158 ? 66.349 -16.396 9.422   1.00 48.56  ? 158 PRO   B N   1 
ATOM   4179 C CA  . PRO   B 1 158 ? 66.109 -17.217 10.623  1.00 49.22  ? 158 PRO   B CA  1 
ATOM   4180 C C   . PRO   B 1 158 ? 67.114 -16.950 11.728  1.00 53.44  ? 158 PRO   B C   1 
ATOM   4181 O O   . PRO   B 1 158 ? 68.253 -16.609 11.427  1.00 52.36  ? 158 PRO   B O   1 
ATOM   4182 C CB  . PRO   B 1 158 ? 66.255 -18.665 10.116  1.00 51.30  ? 158 PRO   B CB  1 
ATOM   4183 C CG  . PRO   B 1 158 ? 66.192 -18.589 8.635   1.00 55.20  ? 158 PRO   B CG  1 
ATOM   4184 C CD  . PRO   B 1 158 ? 66.627 -17.232 8.235   1.00 50.45  ? 158 PRO   B CD  1 
ATOM   4185 N N   . SER   B 1 159 ? 66.697 -17.116 13.001  1.00 51.86  ? 159 SER   B N   1 
ATOM   4186 C CA  . SER   B 1 159 ? 67.559 -16.913 14.177  1.00 52.79  ? 159 SER   B CA  1 
ATOM   4187 C C   . SER   B 1 159 ? 68.855 -17.757 14.121  1.00 57.75  ? 159 SER   B C   1 
ATOM   4188 O O   . SER   B 1 159 ? 69.920 -17.250 14.477  1.00 56.30  ? 159 SER   B O   1 
ATOM   4189 C CB  . SER   B 1 159 ? 66.782 -17.183 15.459  1.00 57.56  ? 159 SER   B CB  1 
ATOM   4190 O OG  . SER   B 1 159 ? 66.000 -16.050 15.799  1.00 70.28  ? 159 SER   B OG  1 
ATOM   4191 N N   . ASP   B 1 160 ? 68.756 -19.025 13.633  1.00 56.60  ? 160 ASP   B N   1 
ATOM   4192 C CA  . ASP   B 1 160 ? 69.878 -19.958 13.444  1.00 57.42  ? 160 ASP   B CA  1 
ATOM   4193 C C   . ASP   B 1 160 ? 70.929 -19.440 12.405  1.00 62.53  ? 160 ASP   B C   1 
ATOM   4194 O O   . ASP   B 1 160 ? 72.046 -19.954 12.362  1.00 63.30  ? 160 ASP   B O   1 
ATOM   4195 C CB  . ASP   B 1 160 ? 69.372 -21.378 13.084  1.00 59.56  ? 160 ASP   B CB  1 
ATOM   4196 C CG  . ASP   B 1 160 ? 68.535 -21.490 11.817  1.00 76.72  ? 160 ASP   B CG  1 
ATOM   4197 O OD1 . ASP   B 1 160 ? 69.023 -21.078 10.739  1.00 78.46  ? 160 ASP   B OD1 1 
ATOM   4198 O OD2 . ASP   B 1 160 ? 67.400 -22.010 11.898  1.00 85.12  ? 160 ASP   B OD2 1 
ATOM   4199 N N   . GLY   B 1 161 ? 70.539 -18.442 11.599  1.00 58.44  ? 161 GLY   B N   1 
ATOM   4200 C CA  . GLY   B 1 161 ? 71.347 -17.758 10.591  1.00 57.71  ? 161 GLY   B CA  1 
ATOM   4201 C C   . GLY   B 1 161 ? 71.892 -18.583 9.443   1.00 61.54  ? 161 GLY   B C   1 
ATOM   4202 O O   . GLY   B 1 161 ? 72.917 -18.205 8.866   1.00 61.43  ? 161 GLY   B O   1 
ATOM   4203 N N   . THR   B 1 162 ? 71.207 -19.703 9.091   1.00 57.06  ? 162 THR   B N   1 
ATOM   4204 C CA  . THR   B 1 162 ? 71.603 -20.636 8.020   1.00 56.15  ? 162 THR   B CA  1 
ATOM   4205 C C   . THR   B 1 162 ? 70.932 -20.357 6.654   1.00 58.75  ? 162 THR   B C   1 
ATOM   4206 O O   . THR   B 1 162 ? 71.107 -21.139 5.708   1.00 57.50  ? 162 THR   B O   1 
ATOM   4207 C CB  . THR   B 1 162 ? 71.334 -22.098 8.462   1.00 63.66  ? 162 THR   B CB  1 
ATOM   4208 O OG1 . THR   B 1 162 ? 69.923 -22.309 8.581   1.00 61.25  ? 162 THR   B OG1 1 
ATOM   4209 C CG2 . THR   B 1 162 ? 72.068 -22.483 9.754   1.00 62.33  ? 162 THR   B CG2 1 
ATOM   4210 N N   . GLN   B 1 163 ? 70.169 -19.246 6.555   1.00 54.51  ? 163 GLN   B N   1 
ATOM   4211 C CA  . GLN   B 1 163 ? 69.422 -18.862 5.358   1.00 52.78  ? 163 GLN   B CA  1 
ATOM   4212 C C   . GLN   B 1 163 ? 69.114 -17.360 5.373   1.00 56.17  ? 163 GLN   B C   1 
ATOM   4213 O O   . GLN   B 1 163 ? 69.121 -16.724 6.434   1.00 56.63  ? 163 GLN   B O   1 
ATOM   4214 C CB  . GLN   B 1 163 ? 68.103 -19.665 5.349   1.00 53.61  ? 163 GLN   B CB  1 
ATOM   4215 C CG  . GLN   B 1 163 ? 67.277 -19.649 4.063   1.00 63.50  ? 163 GLN   B CG  1 
ATOM   4216 C CD  . GLN   B 1 163 ? 66.332 -20.834 3.965   1.00 76.38  ? 163 GLN   B CD  1 
ATOM   4217 O OE1 . GLN   B 1 163 ? 66.420 -21.811 4.726   1.00 72.68  ? 163 GLN   B OE1 1 
ATOM   4218 N NE2 . GLN   B 1 163 ? 65.409 -20.786 3.008   1.00 60.12  ? 163 GLN   B NE2 1 
ATOM   4219 N N   . LYS   B 1 164 ? 68.851 -16.803 4.180   1.00 50.47  ? 164 LYS   B N   1 
ATOM   4220 C CA  . LYS   B 1 164 ? 68.450 -15.420 3.932   1.00 48.16  ? 164 LYS   B CA  1 
ATOM   4221 C C   . LYS   B 1 164 ? 67.620 -15.412 2.631   1.00 50.03  ? 164 LYS   B C   1 
ATOM   4222 O O   . LYS   B 1 164 ? 68.166 -15.579 1.537   1.00 50.63  ? 164 LYS   B O   1 
ATOM   4223 C CB  . LYS   B 1 164 ? 69.650 -14.464 3.851   1.00 48.55  ? 164 LYS   B CB  1 
ATOM   4224 N N   . VAL   B 1 165 ? 66.305 -15.272 2.760   1.00 42.93  ? 165 VAL   B N   1 
ATOM   4225 C CA  . VAL   B 1 165 ? 65.416 -15.193 1.616   1.00 41.54  ? 165 VAL   B CA  1 
ATOM   4226 C C   . VAL   B 1 165 ? 65.100 -13.704 1.453   1.00 44.27  ? 165 VAL   B C   1 
ATOM   4227 O O   . VAL   B 1 165 ? 64.853 -13.016 2.445   1.00 43.29  ? 165 VAL   B O   1 
ATOM   4228 C CB  . VAL   B 1 165 ? 64.127 -16.047 1.778   1.00 44.85  ? 165 VAL   B CB  1 
ATOM   4229 N N   . THR   B 1 166 ? 65.147 -13.207 0.219   1.00 40.82  ? 166 THR   B N   1 
ATOM   4230 C CA  . THR   B 1 166 ? 64.848 -11.813 -0.127  1.00 41.32  ? 166 THR   B CA  1 
ATOM   4231 C C   . THR   B 1 166 ? 63.849 -11.822 -1.280  1.00 47.02  ? 166 THR   B C   1 
ATOM   4232 O O   . THR   B 1 166 ? 64.111 -12.428 -2.337  1.00 47.35  ? 166 THR   B O   1 
ATOM   4233 C CB  . THR   B 1 166 ? 66.118 -11.025 -0.484  1.00 45.97  ? 166 THR   B CB  1 
ATOM   4234 O OG1 . THR   B 1 166 ? 67.032 -11.095 0.613   1.00 53.09  ? 166 THR   B OG1 1 
ATOM   4235 C CG2 . THR   B 1 166 ? 65.831 -9.577  -0.798  1.00 39.66  ? 166 THR   B CG2 1 
ATOM   4236 N N   . TYR   B 1 167 ? 62.699 -11.178 -1.066  1.00 41.73  ? 167 TYR   B N   1 
ATOM   4237 C CA  . TYR   B 1 167 ? 61.683 -11.099 -2.096  1.00 41.14  ? 167 TYR   B CA  1 
ATOM   4238 C C   . TYR   B 1 167 ? 61.586 -9.657  -2.522  1.00 45.69  ? 167 TYR   B C   1 
ATOM   4239 O O   . TYR   B 1 167 ? 61.614 -8.758  -1.683  1.00 45.17  ? 167 TYR   B O   1 
ATOM   4240 C CB  . TYR   B 1 167 ? 60.312 -11.568 -1.587  1.00 42.26  ? 167 TYR   B CB  1 
ATOM   4241 C CG  . TYR   B 1 167 ? 60.283 -12.951 -0.981  1.00 44.12  ? 167 TYR   B CG  1 
ATOM   4242 C CD1 . TYR   B 1 167 ? 59.982 -14.069 -1.756  1.00 46.13  ? 167 TYR   B CD1 1 
ATOM   4243 C CD2 . TYR   B 1 167 ? 60.533 -13.145 0.377   1.00 44.77  ? 167 TYR   B CD2 1 
ATOM   4244 C CE1 . TYR   B 1 167 ? 59.960 -15.351 -1.202  1.00 46.67  ? 167 TYR   B CE1 1 
ATOM   4245 C CE2 . TYR   B 1 167 ? 60.517 -14.423 0.942   1.00 45.98  ? 167 TYR   B CE2 1 
ATOM   4246 C CZ  . TYR   B 1 167 ? 60.231 -15.523 0.148   1.00 55.58  ? 167 TYR   B CZ  1 
ATOM   4247 O OH  . TYR   B 1 167 ? 60.205 -16.780 0.702   1.00 62.05  ? 167 TYR   B OH  1 
ATOM   4248 N N   . LEU   B 1 168 ? 61.471 -9.426  -3.820  1.00 43.12  ? 168 LEU   B N   1 
ATOM   4249 C CA  . LEU   B 1 168 ? 61.318 -8.075  -4.318  1.00 42.90  ? 168 LEU   B CA  1 
ATOM   4250 C C   . LEU   B 1 168 ? 59.856 -7.698  -4.144  1.00 45.80  ? 168 LEU   B C   1 
ATOM   4251 O O   . LEU   B 1 168 ? 58.983 -8.442  -4.586  1.00 46.17  ? 168 LEU   B O   1 
ATOM   4252 C CB  . LEU   B 1 168 ? 61.711 -7.994  -5.806  1.00 42.90  ? 168 LEU   B CB  1 
ATOM   4253 C CG  . LEU   B 1 168 ? 61.583 -6.605  -6.456  1.00 46.87  ? 168 LEU   B CG  1 
ATOM   4254 C CD1 . LEU   B 1 168 ? 62.642 -5.631  -5.917  1.00 45.36  ? 168 LEU   B CD1 1 
ATOM   4255 C CD2 . LEU   B 1 168 ? 61.610 -6.700  -7.987  1.00 48.85  ? 168 LEU   B CD2 1 
ATOM   4256 N N   . VAL   B 1 169 ? 59.584 -6.568  -3.481  1.00 40.86  ? 169 VAL   B N   1 
ATOM   4257 C CA  . VAL   B 1 169 ? 58.207 -6.118  -3.335  1.00 39.87  ? 169 VAL   B CA  1 
ATOM   4258 C C   . VAL   B 1 169 ? 57.956 -5.365  -4.657  1.00 44.95  ? 169 VAL   B C   1 
ATOM   4259 O O   . VAL   B 1 169 ? 57.020 -5.692  -5.389  1.00 44.85  ? 169 VAL   B O   1 
ATOM   4260 C CB  . VAL   B 1 169 ? 57.956 -5.237  -2.072  1.00 42.77  ? 169 VAL   B CB  1 
ATOM   4261 C CG1 . VAL   B 1 169 ? 56.516 -4.698  -2.053  1.00 42.55  ? 169 VAL   B CG1 1 
ATOM   4262 C CG2 . VAL   B 1 169 ? 58.275 -5.995  -0.775  1.00 41.46  ? 169 VAL   B CG2 1 
ATOM   4263 N N   . HIS   B 1 170 ? 58.840 -4.407  -4.993  1.00 42.09  ? 170 HIS   B N   1 
ATOM   4264 C CA  . HIS   B 1 170 ? 58.737 -3.625  -6.223  1.00 42.06  ? 170 HIS   B CA  1 
ATOM   4265 C C   . HIS   B 1 170 ? 59.977 -2.816  -6.478  1.00 46.82  ? 170 HIS   B C   1 
ATOM   4266 O O   . HIS   B 1 170 ? 60.605 -2.320  -5.541  1.00 44.87  ? 170 HIS   B O   1 
ATOM   4267 C CB  . HIS   B 1 170 ? 57.536 -2.666  -6.162  1.00 43.39  ? 170 HIS   B CB  1 
ATOM   4268 C CG  . HIS   B 1 170 ? 57.236 -1.937  -7.442  1.00 47.96  ? 170 HIS   B CG  1 
ATOM   4269 N ND1 . HIS   B 1 170 ? 56.868 -2.615  -8.603  1.00 50.33  ? 170 HIS   B ND1 1 
ATOM   4270 C CD2 . HIS   B 1 170 ? 57.232 -0.609  -7.699  1.00 49.82  ? 170 HIS   B CD2 1 
ATOM   4271 C CE1 . HIS   B 1 170 ? 56.668 -1.679  -9.515  1.00 49.37  ? 170 HIS   B CE1 1 
ATOM   4272 N NE2 . HIS   B 1 170 ? 56.878 -0.461  -9.020  1.00 49.66  ? 170 HIS   B NE2 1 
ATOM   4273 N N   . ASN   B 1 171 ? 60.319 -2.672  -7.772  1.00 45.93  ? 171 ASN   B N   1 
ATOM   4274 C CA  . ASN   B 1 171 ? 61.423 -1.846  -8.214  1.00 45.96  ? 171 ASN   B CA  1 
ATOM   4275 C C   . ASN   B 1 171 ? 60.729 -0.617  -8.752  1.00 50.08  ? 171 ASN   B C   1 
ATOM   4276 O O   . ASN   B 1 171 ? 60.062 -0.687  -9.791  1.00 50.44  ? 171 ASN   B O   1 
ATOM   4277 C CB  . ASN   B 1 171 ? 62.251 -2.522  -9.284  1.00 48.55  ? 171 ASN   B CB  1 
ATOM   4278 C CG  . ASN   B 1 171 ? 63.675 -2.037  -9.295  1.00 77.84  ? 171 ASN   B CG  1 
ATOM   4279 O OD1 . ASN   B 1 171 ? 63.973 -0.872  -9.583  1.00 71.83  ? 171 ASN   B OD1 1 
ATOM   4280 N ND2 . ASN   B 1 171 ? 64.590 -2.930  -8.968  1.00 75.51  ? 171 ASN   B ND2 1 
ATOM   4281 N N   . PHE   B 1 172 ? 60.805 0.488   -7.985  1.00 45.76  ? 172 PHE   B N   1 
ATOM   4282 C CA  . PHE   B 1 172 ? 60.201 1.777   -8.322  1.00 44.47  ? 172 PHE   B CA  1 
ATOM   4283 C C   . PHE   B 1 172 ? 61.101 2.361   -9.381  1.00 53.08  ? 172 PHE   B C   1 
ATOM   4284 O O   . PHE   B 1 172 ? 62.305 2.500   -9.146  1.00 53.43  ? 172 PHE   B O   1 
ATOM   4285 C CB  . PHE   B 1 172 ? 60.121 2.670   -7.073  1.00 44.53  ? 172 PHE   B CB  1 
ATOM   4286 C CG  . PHE   B 1 172 ? 59.062 2.236   -6.096  1.00 44.58  ? 172 PHE   B CG  1 
ATOM   4287 C CD1 . PHE   B 1 172 ? 57.838 2.895   -6.036  1.00 46.22  ? 172 PHE   B CD1 1 
ATOM   4288 C CD2 . PHE   B 1 172 ? 59.277 1.157   -5.243  1.00 45.33  ? 172 PHE   B CD2 1 
ATOM   4289 C CE1 . PHE   B 1 172 ? 56.847 2.483   -5.145  1.00 46.30  ? 172 PHE   B CE1 1 
ATOM   4290 C CE2 . PHE   B 1 172 ? 58.276 0.735   -4.364  1.00 47.14  ? 172 PHE   B CE2 1 
ATOM   4291 C CZ  . PHE   B 1 172 ? 57.072 1.405   -4.315  1.00 44.73  ? 172 PHE   B CZ  1 
ATOM   4292 N N   . GLU   B 1 173 ? 60.547 2.615   -10.576 1.00 53.79  ? 173 GLU   B N   1 
ATOM   4293 C CA  . GLU   B 1 173 ? 61.313 3.129   -11.727 1.00 54.77  ? 173 GLU   B CA  1 
ATOM   4294 C C   . GLU   B 1 173 ? 60.943 4.550   -12.117 1.00 61.93  ? 173 GLU   B C   1 
ATOM   4295 O O   . GLU   B 1 173 ? 61.836 5.391   -12.187 1.00 62.67  ? 173 GLU   B O   1 
ATOM   4296 C CB  . GLU   B 1 173 ? 61.317 2.131   -12.886 1.00 55.72  ? 173 GLU   B CB  1 
ATOM   4297 C CG  . GLU   B 1 173 ? 62.073 0.871   -12.512 1.00 65.10  ? 173 GLU   B CG  1 
ATOM   4298 C CD  . GLU   B 1 173 ? 62.445 -0.018  -13.675 1.00 92.17  ? 173 GLU   B CD  1 
ATOM   4299 O OE1 . GLU   B 1 173 ? 61.578 -0.802  -14.124 1.00 81.62  ? 173 GLU   B OE1 1 
ATOM   4300 O OE2 . GLU   B 1 173 ? 63.607 0.068   -14.135 1.00 92.48  ? 173 GLU   B OE2 1 
ATOM   4301 N N   . GLU   B 1 174 ? 59.635 4.846   -12.306 1.00 60.15  ? 174 GLU   B N   1 
ATOM   4302 C CA  . GLU   B 1 174 ? 59.183 6.223   -12.566 1.00 61.21  ? 174 GLU   B CA  1 
ATOM   4303 C C   . GLU   B 1 174 ? 59.292 6.902   -11.180 1.00 65.42  ? 174 GLU   B C   1 
ATOM   4304 O O   . GLU   B 1 174 ? 59.261 8.124   -11.049 1.00 65.65  ? 174 GLU   B O   1 
ATOM   4305 C CB  . GLU   B 1 174 ? 57.746 6.270   -13.125 1.00 62.95  ? 174 GLU   B CB  1 
ATOM   4306 N N   . GLY   B 1 175 ? 59.436 6.036   -10.177 1.00 61.63  ? 175 GLY   B N   1 
ATOM   4307 C CA  . GLY   B 1 175 ? 59.695 6.281   -8.766  1.00 60.42  ? 175 GLY   B CA  1 
ATOM   4308 C C   . GLY   B 1 175 ? 58.762 7.123   -7.952  1.00 60.76  ? 175 GLY   B C   1 
ATOM   4309 O O   . GLY   B 1 175 ? 58.144 8.066   -8.449  1.00 62.05  ? 175 GLY   B O   1 
ATOM   4310 N N   . GLY   B 1 176 ? 58.722 6.786   -6.677  1.00 52.63  ? 176 GLY   B N   1 
ATOM   4311 C CA  . GLY   B 1 176 ? 57.898 7.465   -5.703  1.00 50.84  ? 176 GLY   B CA  1 
ATOM   4312 C C   . GLY   B 1 176 ? 56.644 6.674   -5.461  1.00 52.13  ? 176 GLY   B C   1 
ATOM   4313 O O   . GLY   B 1 176 ? 55.964 6.260   -6.404  1.00 52.44  ? 176 GLY   B O   1 
ATOM   4314 N N   . GLY   B 1 177 ? 56.339 6.476   -4.197  1.00 45.61  ? 177 GLY   B N   1 
ATOM   4315 C CA  . GLY   B 1 177 ? 55.145 5.760   -3.824  1.00 43.98  ? 177 GLY   B CA  1 
ATOM   4316 C C   . GLY   B 1 177 ? 55.035 5.462   -2.355  1.00 47.98  ? 177 GLY   B C   1 
ATOM   4317 O O   . GLY   B 1 177 ? 55.466 6.235   -1.492  1.00 47.73  ? 177 GLY   B O   1 
ATOM   4318 N N   . VAL   B 1 178 ? 54.445 4.318   -2.080  1.00 45.02  ? 178 VAL   B N   1 
ATOM   4319 C CA  . VAL   B 1 178 ? 54.188 3.853   -0.735  1.00 44.32  ? 178 VAL   B CA  1 
ATOM   4320 C C   . VAL   B 1 178 ? 54.394 2.325   -0.669  1.00 46.98  ? 178 VAL   B C   1 
ATOM   4321 O O   . VAL   B 1 178 ? 54.275 1.640   -1.681  1.00 46.37  ? 178 VAL   B O   1 
ATOM   4322 C CB  . VAL   B 1 178 ? 52.780 4.403   -0.345  1.00 48.08  ? 178 VAL   B CB  1 
ATOM   4323 C CG1 . VAL   B 1 178 ? 51.624 3.498   -0.743  1.00 47.41  ? 178 VAL   B CG1 1 
ATOM   4324 C CG2 . VAL   B 1 178 ? 52.714 4.845   1.094   1.00 48.06  ? 178 VAL   B CG2 1 
ATOM   4325 N N   . ALA   B 1 179 ? 54.789 1.811   0.492   1.00 44.09  ? 179 ALA   B N   1 
ATOM   4326 C CA  . ALA   B 1 179 ? 55.041 0.383   0.707   1.00 42.65  ? 179 ALA   B CA  1 
ATOM   4327 C C   . ALA   B 1 179 ? 54.793 0.019   2.149   1.00 46.87  ? 179 ALA   B C   1 
ATOM   4328 O O   . ALA   B 1 179 ? 54.887 0.873   3.024   1.00 46.39  ? 179 ALA   B O   1 
ATOM   4329 C CB  . ALA   B 1 179 ? 56.463 0.017   0.317   1.00 42.75  ? 179 ALA   B CB  1 
ATOM   4330 N N   . MET   B 1 180 ? 54.459 -1.247  2.400   1.00 44.39  ? 180 MET   B N   1 
ATOM   4331 C CA  . MET   B 1 180 ? 54.202 -1.730  3.740   1.00 44.69  ? 180 MET   B CA  1 
ATOM   4332 C C   . MET   B 1 180 ? 54.525 -3.186  3.895   1.00 48.01  ? 180 MET   B C   1 
ATOM   4333 O O   . MET   B 1 180 ? 54.495 -3.940  2.917   1.00 47.48  ? 180 MET   B O   1 
ATOM   4334 C CB  . MET   B 1 180 ? 52.757 -1.456  4.193   1.00 47.69  ? 180 MET   B CB  1 
ATOM   4335 C CG  . MET   B 1 180 ? 51.694 -2.199  3.432   1.00 51.93  ? 180 MET   B CG  1 
ATOM   4336 S SD  . MET   B 1 180 ? 50.108 -1.826  4.206   1.00 57.35  ? 180 MET   B SD  1 
ATOM   4337 C CE  . MET   B 1 180 ? 48.999 -2.182  2.855   1.00 54.29  ? 180 MET   B CE  1 
ATOM   4338 N N   . GLY   B 1 181 ? 54.817 -3.551  5.136   1.00 42.86  ? 181 GLY   B N   1 
ATOM   4339 C CA  . GLY   B 1 181 ? 55.109 -4.902  5.559   1.00 42.83  ? 181 GLY   B CA  1 
ATOM   4340 C C   . GLY   B 1 181 ? 54.147 -5.311  6.653   1.00 50.35  ? 181 GLY   B C   1 
ATOM   4341 O O   . GLY   B 1 181 ? 53.953 -4.578  7.627   1.00 48.88  ? 181 GLY   B O   1 
ATOM   4342 N N   . MET   B 1 182 ? 53.506 -6.461  6.488   1.00 51.17  ? 182 MET   B N   1 
ATOM   4343 C CA  . MET   B 1 182 ? 52.600 -6.962  7.506   1.00 53.37  ? 182 MET   B CA  1 
ATOM   4344 C C   . MET   B 1 182 ? 52.778 -8.422  7.774   1.00 54.19  ? 182 MET   B C   1 
ATOM   4345 O O   . MET   B 1 182 ? 53.136 -9.170  6.878   1.00 54.43  ? 182 MET   B O   1 
ATOM   4346 C CB  . MET   B 1 182 ? 51.161 -6.440  7.414   1.00 57.79  ? 182 MET   B CB  1 
ATOM   4347 C CG  . MET   B 1 182 ? 50.238 -7.202  6.530   1.00 64.71  ? 182 MET   B CG  1 
ATOM   4348 S SD  . MET   B 1 182 ? 48.851 -6.122  6.020   1.00 72.94  ? 182 MET   B SD  1 
ATOM   4349 C CE  . MET   B 1 182 ? 48.138 -5.627  7.655   1.00 69.70  ? 182 MET   B CE  1 
ATOM   4350 N N   . TYR   B 1 183 ? 52.596 -8.814  9.019   1.00 48.71  ? 183 TYR   B N   1 
ATOM   4351 C CA  . TYR   B 1 183 ? 52.814 -10.175 9.460   1.00 47.82  ? 183 TYR   B CA  1 
ATOM   4352 C C   . TYR   B 1 183 ? 51.639 -10.693 10.291  1.00 53.57  ? 183 TYR   B C   1 
ATOM   4353 O O   . TYR   B 1 183 ? 50.723 -9.943  10.633  1.00 53.78  ? 183 TYR   B O   1 
ATOM   4354 C CB  . TYR   B 1 183 ? 54.103 -10.202 10.323  1.00 47.20  ? 183 TYR   B CB  1 
ATOM   4355 C CG  . TYR   B 1 183 ? 53.884 -9.596  11.699  1.00 47.32  ? 183 TYR   B CG  1 
ATOM   4356 C CD1 . TYR   B 1 183 ? 53.605 -10.404 12.803  1.00 49.23  ? 183 TYR   B CD1 1 
ATOM   4357 C CD2 . TYR   B 1 183 ? 53.888 -8.215  11.886  1.00 46.28  ? 183 TYR   B CD2 1 
ATOM   4358 C CE1 . TYR   B 1 183 ? 53.360 -9.854  14.058  1.00 48.64  ? 183 TYR   B CE1 1 
ATOM   4359 C CE2 . TYR   B 1 183 ? 53.645 -7.656  13.138  1.00 46.44  ? 183 TYR   B CE2 1 
ATOM   4360 C CZ  . TYR   B 1 183 ? 53.396 -8.481  14.224  1.00 52.43  ? 183 TYR   B CZ  1 
ATOM   4361 O OH  . TYR   B 1 183 ? 53.149 -7.947  15.466  1.00 50.83  ? 183 TYR   B OH  1 
ATOM   4362 N N   . ASN   B 1 184 ? 51.720 -11.978 10.651  1.00 49.75  ? 184 ASN   B N   1 
ATOM   4363 C CA  . ASN   B 1 184 ? 50.769 -12.679 11.484  1.00 49.31  ? 184 ASN   B CA  1 
ATOM   4364 C C   . ASN   B 1 184 ? 51.507 -13.825 12.165  1.00 51.42  ? 184 ASN   B C   1 
ATOM   4365 O O   . ASN   B 1 184 ? 52.130 -14.642 11.483  1.00 51.49  ? 184 ASN   B O   1 
ATOM   4366 C CB  . ASN   B 1 184 ? 49.582 -13.173 10.660  1.00 52.43  ? 184 ASN   B CB  1 
ATOM   4367 C CG  . ASN   B 1 184 ? 48.243 -12.821 11.245  1.00 80.21  ? 184 ASN   B CG  1 
ATOM   4368 O OD1 . ASN   B 1 184 ? 47.964 -13.060 12.425  1.00 68.18  ? 184 ASN   B OD1 1 
ATOM   4369 N ND2 . ASN   B 1 184 ? 47.383 -12.244 10.423  1.00 77.87  ? 184 ASN   B ND2 1 
ATOM   4370 N N   . GLN   B 1 185 ? 51.477 -13.862 13.504  1.00 47.34  ? 185 GLN   B N   1 
ATOM   4371 C CA  . GLN   B 1 185 ? 52.125 -14.926 14.285  1.00 47.18  ? 185 GLN   B CA  1 
ATOM   4372 C C   . GLN   B 1 185 ? 51.204 -16.149 14.317  1.00 51.38  ? 185 GLN   B C   1 
ATOM   4373 O O   . GLN   B 1 185 ? 49.984 -16.012 14.214  1.00 49.77  ? 185 GLN   B O   1 
ATOM   4374 C CB  . GLN   B 1 185 ? 52.445 -14.491 15.729  1.00 48.11  ? 185 GLN   B CB  1 
ATOM   4375 C CG  . GLN   B 1 185 ? 53.041 -13.105 15.873  1.00 70.85  ? 185 GLN   B CG  1 
ATOM   4376 C CD  . GLN   B 1 185 ? 52.152 -12.224 16.715  1.00 93.86  ? 185 GLN   B CD  1 
ATOM   4377 O OE1 . GLN   B 1 185 ? 51.020 -11.871 16.326  1.00 88.50  ? 185 GLN   B OE1 1 
ATOM   4378 N NE2 . GLN   B 1 185 ? 52.653 -11.847 17.890  1.00 82.72  ? 185 GLN   B NE2 1 
ATOM   4379 N N   . ASP   B 1 186 ? 51.788 -17.341 14.478  1.00 50.02  ? 186 ASP   B N   1 
ATOM   4380 C CA  . ASP   B 1 186 ? 51.033 -18.595 14.540  1.00 50.41  ? 186 ASP   B CA  1 
ATOM   4381 C C   . ASP   B 1 186 ? 49.981 -18.623 15.670  1.00 56.27  ? 186 ASP   B C   1 
ATOM   4382 O O   . ASP   B 1 186 ? 48.869 -19.096 15.440  1.00 54.80  ? 186 ASP   B O   1 
ATOM   4383 C CB  . ASP   B 1 186 ? 51.992 -19.790 14.627  1.00 51.47  ? 186 ASP   B CB  1 
ATOM   4384 C CG  . ASP   B 1 186 ? 52.588 -20.228 13.296  1.00 55.79  ? 186 ASP   B CG  1 
ATOM   4385 O OD1 . ASP   B 1 186 ? 52.141 -19.718 12.245  1.00 55.07  ? 186 ASP   B OD1 1 
ATOM   4386 O OD2 . ASP   B 1 186 ? 53.493 -21.092 13.307  1.00 59.98  ? 186 ASP   B OD2 1 
ATOM   4387 N N   . LYS   B 1 187 ? 50.329 -18.070 16.865  1.00 54.71  ? 187 LYS   B N   1 
ATOM   4388 C CA  . LYS   B 1 187 ? 49.464 -18.021 18.051  1.00 54.88  ? 187 LYS   B CA  1 
ATOM   4389 C C   . LYS   B 1 187 ? 48.118 -17.372 17.786  1.00 59.29  ? 187 LYS   B C   1 
ATOM   4390 O O   . LYS   B 1 187 ? 47.108 -17.951 18.169  1.00 60.14  ? 187 LYS   B O   1 
ATOM   4391 C CB  . LYS   B 1 187 ? 50.169 -17.386 19.273  1.00 57.14  ? 187 LYS   B CB  1 
ATOM   4392 N N   . SER   B 1 188 ? 48.087 -16.202 17.109  1.00 54.76  ? 188 SER   B N   1 
ATOM   4393 C CA  . SER   B 1 188 ? 46.821 -15.523 16.811  1.00 53.42  ? 188 SER   B CA  1 
ATOM   4394 C C   . SER   B 1 188 ? 45.979 -16.257 15.782  1.00 56.31  ? 188 SER   B C   1 
ATOM   4395 O O   . SER   B 1 188 ? 44.760 -16.126 15.807  1.00 56.56  ? 188 SER   B O   1 
ATOM   4396 C CB  . SER   B 1 188 ? 47.024 -14.050 16.474  1.00 55.65  ? 188 SER   B CB  1 
ATOM   4397 O OG  . SER   B 1 188 ? 47.721 -13.870 15.258  1.00 65.19  ? 188 SER   B OG  1 
ATOM   4398 N N   . ILE   B 1 189 ? 46.607 -17.064 14.903  1.00 53.11  ? 189 ILE   B N   1 
ATOM   4399 C CA  . ILE   B 1 189 ? 45.861 -17.871 13.921  1.00 52.73  ? 189 ILE   B CA  1 
ATOM   4400 C C   . ILE   B 1 189 ? 45.201 -19.024 14.707  1.00 56.72  ? 189 ILE   B C   1 
ATOM   4401 O O   . ILE   B 1 189 ? 44.050 -19.358 14.435  1.00 56.86  ? 189 ILE   B O   1 
ATOM   4402 C CB  . ILE   B 1 189 ? 46.736 -18.381 12.727  1.00 55.30  ? 189 ILE   B CB  1 
ATOM   4403 C CG1 . ILE   B 1 189 ? 47.354 -17.200 11.933  1.00 54.41  ? 189 ILE   B CG1 1 
ATOM   4404 C CG2 . ILE   B 1 189 ? 45.924 -19.310 11.788  1.00 56.19  ? 189 ILE   B CG2 1 
ATOM   4405 C CD1 . ILE   B 1 189 ? 48.484 -17.581 10.949  1.00 54.76  ? 189 ILE   B CD1 1 
ATOM   4406 N N   . GLU   B 1 190 ? 45.937 -19.596 15.699  1.00 52.70  ? 190 GLU   B N   1 
ATOM   4407 C CA  . GLU   B 1 190 ? 45.512 -20.688 16.583  1.00 52.66  ? 190 GLU   B CA  1 
ATOM   4408 C C   . GLU   B 1 190 ? 44.384 -20.231 17.483  1.00 56.72  ? 190 GLU   B C   1 
ATOM   4409 O O   . GLU   B 1 190 ? 43.397 -20.944 17.614  1.00 56.81  ? 190 GLU   B O   1 
ATOM   4410 C CB  . GLU   B 1 190 ? 46.680 -21.188 17.445  1.00 54.10  ? 190 GLU   B CB  1 
ATOM   4411 C CG  . GLU   B 1 190 ? 47.687 -22.032 16.682  1.00 63.90  ? 190 GLU   B CG  1 
ATOM   4412 C CD  . GLU   B 1 190 ? 49.081 -22.115 17.276  1.00 79.17  ? 190 GLU   B CD  1 
ATOM   4413 O OE1 . GLU   B 1 190 ? 49.934 -22.800 16.664  1.00 83.01  ? 190 GLU   B OE1 1 
ATOM   4414 O OE2 . GLU   B 1 190 ? 49.326 -21.504 18.341  1.00 63.56  ? 190 GLU   B OE2 1 
ATOM   4415 N N   . ASP   B 1 191 ? 44.527 -19.034 18.090  1.00 52.34  ? 191 ASP   B N   1 
ATOM   4416 C CA  . ASP   B 1 191 ? 43.537 -18.405 18.959  1.00 51.33  ? 191 ASP   B CA  1 
ATOM   4417 C C   . ASP   B 1 191 ? 42.206 -18.228 18.225  1.00 56.72  ? 191 ASP   B C   1 
ATOM   4418 O O   . ASP   B 1 191 ? 41.147 -18.469 18.818  1.00 58.06  ? 191 ASP   B O   1 
ATOM   4419 C CB  . ASP   B 1 191 ? 44.062 -17.063 19.487  1.00 52.09  ? 191 ASP   B CB  1 
ATOM   4420 C CG  . ASP   B 1 191 ? 45.135 -17.193 20.550  1.00 60.07  ? 191 ASP   B CG  1 
ATOM   4421 O OD1 . ASP   B 1 191 ? 45.688 -16.147 20.967  1.00 60.91  ? 191 ASP   B OD1 1 
ATOM   4422 O OD2 . ASP   B 1 191 ? 45.425 -18.344 20.970  1.00 64.28  ? 191 ASP   B OD2 1 
ATOM   4423 N N   . PHE   B 1 192 ? 42.273 -17.835 16.927  1.00 51.13  ? 192 PHE   B N   1 
ATOM   4424 C CA  . PHE   B 1 192 ? 41.134 -17.651 16.028  1.00 49.30  ? 192 PHE   B CA  1 
ATOM   4425 C C   . PHE   B 1 192 ? 40.471 -19.016 15.775  1.00 55.40  ? 192 PHE   B C   1 
ATOM   4426 O O   . PHE   B 1 192 ? 39.240 -19.095 15.759  1.00 55.43  ? 192 PHE   B O   1 
ATOM   4427 C CB  . PHE   B 1 192 ? 41.599 -16.986 14.715  1.00 49.50  ? 192 PHE   B CB  1 
ATOM   4428 C CG  . PHE   B 1 192 ? 40.555 -16.734 13.646  1.00 49.38  ? 192 PHE   B CG  1 
ATOM   4429 C CD1 . PHE   B 1 192 ? 40.878 -16.838 12.300  1.00 51.19  ? 192 PHE   B CD1 1 
ATOM   4430 C CD2 . PHE   B 1 192 ? 39.260 -16.357 13.985  1.00 50.34  ? 192 PHE   B CD2 1 
ATOM   4431 C CE1 . PHE   B 1 192 ? 39.918 -16.591 11.312  1.00 51.55  ? 192 PHE   B CE1 1 
ATOM   4432 C CE2 . PHE   B 1 192 ? 38.304 -16.107 12.996  1.00 52.55  ? 192 PHE   B CE2 1 
ATOM   4433 C CZ  . PHE   B 1 192 ? 38.639 -16.226 11.668  1.00 50.35  ? 192 PHE   B CZ  1 
ATOM   4434 N N   . ALA   B 1 193 ? 41.284 -20.087 15.609  1.00 53.03  ? 193 ALA   B N   1 
ATOM   4435 C CA  . ALA   B 1 193 ? 40.791 -21.459 15.409  1.00 53.36  ? 193 ALA   B CA  1 
ATOM   4436 C C   . ALA   B 1 193 ? 40.140 -21.998 16.694  1.00 57.78  ? 193 ALA   B C   1 
ATOM   4437 O O   . ALA   B 1 193 ? 39.036 -22.509 16.622  1.00 57.20  ? 193 ALA   B O   1 
ATOM   4438 C CB  . ALA   B 1 193 ? 41.916 -22.374 14.956  1.00 54.06  ? 193 ALA   B CB  1 
ATOM   4439 N N   . HIS   B 1 194 ? 40.790 -21.836 17.862  1.00 56.52  ? 194 HIS   B N   1 
ATOM   4440 C CA  . HIS   B 1 194 ? 40.260 -22.270 19.163  1.00 57.81  ? 194 HIS   B CA  1 
ATOM   4441 C C   . HIS   B 1 194 ? 38.936 -21.592 19.487  1.00 60.10  ? 194 HIS   B C   1 
ATOM   4442 O O   . HIS   B 1 194 ? 37.978 -22.289 19.810  1.00 59.20  ? 194 HIS   B O   1 
ATOM   4443 C CB  . HIS   B 1 194 ? 41.271 -22.057 20.297  1.00 59.79  ? 194 HIS   B CB  1 
ATOM   4444 C CG  . HIS   B 1 194 ? 42.370 -23.070 20.301  1.00 64.38  ? 194 HIS   B CG  1 
ATOM   4445 N ND1 . HIS   B 1 194 ? 42.103 -24.429 20.221  1.00 66.72  ? 194 HIS   B ND1 1 
ATOM   4446 C CD2 . HIS   B 1 194 ? 43.710 -22.889 20.380  1.00 67.03  ? 194 HIS   B CD2 1 
ATOM   4447 C CE1 . HIS   B 1 194 ? 43.283 -25.025 20.244  1.00 66.70  ? 194 HIS   B CE1 1 
ATOM   4448 N NE2 . HIS   B 1 194 ? 44.280 -24.139 20.341  1.00 67.12  ? 194 HIS   B NE2 1 
ATOM   4449 N N   . SER   B 1 195 ? 38.866 -20.247 19.360  1.00 55.56  ? 195 SER   B N   1 
ATOM   4450 C CA  . SER   B 1 195 ? 37.629 -19.500 19.588  1.00 54.94  ? 195 SER   B CA  1 
ATOM   4451 C C   . SER   B 1 195 ? 36.538 -20.048 18.647  1.00 60.53  ? 195 SER   B C   1 
ATOM   4452 O O   . SER   B 1 195 ? 35.431 -20.331 19.109  1.00 61.51  ? 195 SER   B O   1 
ATOM   4453 C CB  . SER   B 1 195 ? 37.840 -18.004 19.371  1.00 56.86  ? 195 SER   B CB  1 
ATOM   4454 O OG  . SER   B 1 195 ? 38.720 -17.448 20.337  1.00 63.19  ? 195 SER   B OG  1 
ATOM   4455 N N   . SER   B 1 196 ? 36.877 -20.260 17.351  1.00 56.18  ? 196 SER   B N   1 
ATOM   4456 C CA  . SER   B 1 196 ? 35.959 -20.785 16.342  1.00 55.26  ? 196 SER   B CA  1 
ATOM   4457 C C   . SER   B 1 196 ? 35.477 -22.200 16.637  1.00 62.98  ? 196 SER   B C   1 
ATOM   4458 O O   . SER   B 1 196 ? 34.289 -22.466 16.466  1.00 62.87  ? 196 SER   B O   1 
ATOM   4459 C CB  . SER   B 1 196 ? 36.560 -20.693 14.944  1.00 54.34  ? 196 SER   B CB  1 
ATOM   4460 O OG  . SER   B 1 196 ? 36.787 -19.342 14.580  1.00 54.94  ? 196 SER   B OG  1 
ATOM   4461 N N   . PHE   B 1 197 ? 36.380 -23.108 17.061  1.00 62.55  ? 197 PHE   B N   1 
ATOM   4462 C CA  . PHE   B 1 197 ? 36.032 -24.504 17.383  1.00 62.79  ? 197 PHE   B CA  1 
ATOM   4463 C C   . PHE   B 1 197 ? 35.178 -24.582 18.658  1.00 66.58  ? 197 PHE   B C   1 
ATOM   4464 O O   . PHE   B 1 197 ? 34.199 -25.321 18.679  1.00 66.78  ? 197 PHE   B O   1 
ATOM   4465 C CB  . PHE   B 1 197 ? 37.283 -25.412 17.465  1.00 64.44  ? 197 PHE   B CB  1 
ATOM   4466 C CG  . PHE   B 1 197 ? 37.900 -25.757 16.126  1.00 65.32  ? 197 PHE   B CG  1 
ATOM   4467 C CD1 . PHE   B 1 197 ? 39.198 -25.363 15.817  1.00 67.94  ? 197 PHE   B CD1 1 
ATOM   4468 C CD2 . PHE   B 1 197 ? 37.192 -26.490 15.182  1.00 66.43  ? 197 PHE   B CD2 1 
ATOM   4469 C CE1 . PHE   B 1 197 ? 39.761 -25.661 14.570  1.00 68.50  ? 197 PHE   B CE1 1 
ATOM   4470 C CE2 . PHE   B 1 197 ? 37.754 -26.784 13.934  1.00 69.25  ? 197 PHE   B CE2 1 
ATOM   4471 C CZ  . PHE   B 1 197 ? 39.032 -26.365 13.634  1.00 67.09  ? 197 PHE   B CZ  1 
ATOM   4472 N N   . GLN   B 1 198 ? 35.524 -23.792 19.690  1.00 62.35  ? 198 GLN   B N   1 
ATOM   4473 C CA  . GLN   B 1 198 ? 34.784 -23.714 20.951  1.00 62.51  ? 198 GLN   B CA  1 
ATOM   4474 C C   . GLN   B 1 198 ? 33.386 -23.062 20.735  1.00 69.54  ? 198 GLN   B C   1 
ATOM   4475 O O   . GLN   B 1 198 ? 32.436 -23.393 21.465  1.00 69.52  ? 198 GLN   B O   1 
ATOM   4476 C CB  . GLN   B 1 198 ? 35.600 -22.986 22.044  1.00 63.36  ? 198 GLN   B CB  1 
ATOM   4477 C CG  . GLN   B 1 198 ? 36.867 -23.756 22.451  1.00 75.90  ? 198 GLN   B CG  1 
ATOM   4478 C CD  . GLN   B 1 198 ? 37.164 -23.823 23.931  1.00 94.73  ? 198 GLN   B CD  1 
ATOM   4479 O OE1 . GLN   B 1 198 ? 38.311 -23.645 24.354  1.00 91.61  ? 198 GLN   B OE1 1 
ATOM   4480 N NE2 . GLN   B 1 198 ? 36.159 -24.107 24.752  1.00 85.87  ? 198 GLN   B NE2 1 
ATOM   4481 N N   . MET   B 1 199 ? 33.267 -22.154 19.713  1.00 66.32  ? 199 MET   B N   1 
ATOM   4482 C CA  . MET   B 1 199 ? 32.017 -21.481 19.343  1.00 65.66  ? 199 MET   B CA  1 
ATOM   4483 C C   . MET   B 1 199 ? 31.065 -22.494 18.693  1.00 71.04  ? 199 MET   B C   1 
ATOM   4484 O O   . MET   B 1 199 ? 29.869 -22.486 18.992  1.00 70.92  ? 199 MET   B O   1 
ATOM   4485 C CB  . MET   B 1 199 ? 32.277 -20.264 18.420  1.00 67.51  ? 199 MET   B CB  1 
ATOM   4486 C CG  . MET   B 1 199 ? 31.015 -19.479 18.000  1.00 70.64  ? 199 MET   B CG  1 
ATOM   4487 S SD  . MET   B 1 199 ? 29.838 -19.086 19.333  1.00 74.30  ? 199 MET   B SD  1 
ATOM   4488 C CE  . MET   B 1 199 ? 30.049 -17.393 19.472  1.00 70.81  ? 199 MET   B CE  1 
ATOM   4489 N N   . ALA   B 1 200 ? 31.607 -23.375 17.828  1.00 68.47  ? 200 ALA   B N   1 
ATOM   4490 C CA  . ALA   B 1 200 ? 30.856 -24.414 17.117  1.00 68.91  ? 200 ALA   B CA  1 
ATOM   4491 C C   . ALA   B 1 200 ? 30.371 -25.527 18.051  1.00 74.91  ? 200 ALA   B C   1 
ATOM   4492 O O   . ALA   B 1 200 ? 29.353 -26.165 17.764  1.00 74.97  ? 200 ALA   B O   1 
ATOM   4493 C CB  . ALA   B 1 200 ? 31.692 -24.991 15.992  1.00 69.40  ? 200 ALA   B CB  1 
ATOM   4494 N N   . LEU   B 1 201 ? 31.099 -25.760 19.161  1.00 71.17  ? 201 LEU   B N   1 
ATOM   4495 C CA  . LEU   B 1 201 ? 30.720 -26.769 20.138  1.00 70.60  ? 201 LEU   B CA  1 
ATOM   4496 C C   . LEU   B 1 201 ? 29.552 -26.246 20.973  1.00 74.55  ? 201 LEU   B C   1 
ATOM   4497 O O   . LEU   B 1 201 ? 28.525 -26.919 21.048  1.00 75.02  ? 201 LEU   B O   1 
ATOM   4498 C CB  . LEU   B 1 201 ? 31.912 -27.196 21.017  1.00 70.13  ? 201 LEU   B CB  1 
ATOM   4499 C CG  . LEU   B 1 201 ? 32.931 -28.156 20.374  1.00 73.47  ? 201 LEU   B CG  1 
ATOM   4500 C CD1 . LEU   B 1 201 ? 34.167 -28.306 21.245  1.00 73.26  ? 201 LEU   B CD1 1 
ATOM   4501 C CD2 . LEU   B 1 201 ? 32.325 -29.520 20.076  1.00 73.40  ? 201 LEU   B CD2 1 
ATOM   4502 N N   . SER   B 1 202 ? 29.698 -25.033 21.556  1.00 69.70  ? 202 SER   B N   1 
ATOM   4503 C CA  . SER   B 1 202 ? 28.682 -24.352 22.366  1.00 68.57  ? 202 SER   B CA  1 
ATOM   4504 C C   . SER   B 1 202 ? 27.333 -24.185 21.631  1.00 72.66  ? 202 SER   B C   1 
ATOM   4505 O O   . SER   B 1 202 ? 26.288 -24.387 22.247  1.00 73.55  ? 202 SER   B O   1 
ATOM   4506 C CB  . SER   B 1 202 ? 29.193 -22.997 22.849  1.00 69.95  ? 202 SER   B CB  1 
ATOM   4507 N N   . LYS   B 1 203 ? 27.352 -23.836 20.332  1.00 67.93  ? 203 LYS   B N   1 
ATOM   4508 C CA  . LYS   B 1 203 ? 26.135 -23.655 19.526  1.00 67.19  ? 203 LYS   B CA  1 
ATOM   4509 C C   . LYS   B 1 203 ? 25.639 -24.966 18.899  1.00 73.00  ? 203 LYS   B C   1 
ATOM   4510 O O   . LYS   B 1 203 ? 24.482 -25.048 18.467  1.00 72.86  ? 203 LYS   B O   1 
ATOM   4511 C CB  . LYS   B 1 203 ? 26.323 -22.565 18.452  1.00 67.91  ? 203 LYS   B CB  1 
ATOM   4512 C CG  . LYS   B 1 203 ? 26.474 -21.149 19.010  1.00 72.46  ? 203 LYS   B CG  1 
ATOM   4513 C CD  . LYS   B 1 203 ? 25.146 -20.516 19.399  1.00 81.62  ? 203 LYS   B CD  1 
ATOM   4514 C CE  . LYS   B 1 203 ? 25.310 -19.264 20.224  1.00 87.34  ? 203 LYS   B CE  1 
ATOM   4515 N NZ  . LYS   B 1 203 ? 24.016 -18.845 20.839  1.00 93.74  ? 203 LYS   B NZ  1 
ATOM   4516 N N   . GLY   B 1 204 ? 26.517 -25.968 18.863  1.00 70.61  ? 204 GLY   B N   1 
ATOM   4517 C CA  . GLY   B 1 204 ? 26.237 -27.291 18.311  1.00 70.53  ? 204 GLY   B CA  1 
ATOM   4518 C C   . GLY   B 1 204 ? 26.057 -27.364 16.807  1.00 74.62  ? 204 GLY   B C   1 
ATOM   4519 O O   . GLY   B 1 204 ? 25.442 -28.314 16.321  1.00 73.58  ? 204 GLY   B O   1 
ATOM   4520 N N   . TRP   B 1 205 ? 26.611 -26.383 16.057  1.00 72.78  ? 205 TRP   B N   1 
ATOM   4521 C CA  . TRP   B 1 205 ? 26.517 -26.289 14.592  1.00 73.60  ? 205 TRP   B CA  1 
ATOM   4522 C C   . TRP   B 1 205 ? 27.868 -26.475 13.868  1.00 74.74  ? 205 TRP   B C   1 
ATOM   4523 O O   . TRP   B 1 205 ? 28.902 -26.159 14.467  1.00 74.62  ? 205 TRP   B O   1 
ATOM   4524 C CB  . TRP   B 1 205 ? 25.984 -24.905 14.201  1.00 74.02  ? 205 TRP   B CB  1 
ATOM   4525 C CG  . TRP   B 1 205 ? 24.596 -24.563 14.659  1.00 76.50  ? 205 TRP   B CG  1 
ATOM   4526 C CD1 . TRP   B 1 205 ? 23.569 -25.425 14.929  1.00 79.74  ? 205 TRP   B CD1 1 
ATOM   4527 C CD2 . TRP   B 1 205 ? 24.067 -23.245 14.823  1.00 76.77  ? 205 TRP   B CD2 1 
ATOM   4528 N NE1 . TRP   B 1 205 ? 22.442 -24.720 15.289  1.00 79.51  ? 205 TRP   B NE1 1 
ATOM   4529 C CE2 . TRP   B 1 205 ? 22.719 -23.380 15.228  1.00 80.92  ? 205 TRP   B CE2 1 
ATOM   4530 C CE3 . TRP   B 1 205 ? 24.608 -21.957 14.681  1.00 78.39  ? 205 TRP   B CE3 1 
ATOM   4531 C CZ2 . TRP   B 1 205 ? 21.908 -22.276 15.495  1.00 80.42  ? 205 TRP   B CZ2 1 
ATOM   4532 C CZ3 . TRP   B 1 205 ? 23.801 -20.864 14.940  1.00 80.35  ? 205 TRP   B CZ3 1 
ATOM   4533 C CH2 . TRP   B 1 205 ? 22.472 -21.028 15.354  1.00 81.10  ? 205 TRP   B CH2 1 
ATOM   4534 N N   . PRO   B 1 206 ? 27.896 -26.918 12.574  1.00 68.82  ? 206 PRO   B N   1 
ATOM   4535 C CA  . PRO   B 1 206 ? 29.185 -27.054 11.875  1.00 67.91  ? 206 PRO   B CA  1 
ATOM   4536 C C   . PRO   B 1 206 ? 29.948 -25.738 11.660  1.00 70.84  ? 206 PRO   B C   1 
ATOM   4537 O O   . PRO   B 1 206 ? 29.340 -24.691 11.403  1.00 69.46  ? 206 PRO   B O   1 
ATOM   4538 C CB  . PRO   B 1 206 ? 28.801 -27.699 10.531  1.00 69.08  ? 206 PRO   B CB  1 
ATOM   4539 C CG  . PRO   B 1 206 ? 27.398 -27.366 10.326  1.00 73.47  ? 206 PRO   B CG  1 
ATOM   4540 C CD  . PRO   B 1 206 ? 26.781 -27.342 11.697  1.00 69.63  ? 206 PRO   B CD  1 
ATOM   4541 N N   . LEU   B 1 207 ? 31.293 -25.820 11.755  1.00 66.49  ? 207 LEU   B N   1 
ATOM   4542 C CA  . LEU   B 1 207 ? 32.221 -24.715 11.553  1.00 65.50  ? 207 LEU   B CA  1 
ATOM   4543 C C   . LEU   B 1 207 ? 32.843 -24.795 10.174  1.00 70.59  ? 207 LEU   B C   1 
ATOM   4544 O O   . LEU   B 1 207 ? 33.300 -25.849 9.748   1.00 69.57  ? 207 LEU   B O   1 
ATOM   4545 C CB  . LEU   B 1 207 ? 33.317 -24.695 12.637  1.00 65.02  ? 207 LEU   B CB  1 
ATOM   4546 C CG  . LEU   B 1 207 ? 34.502 -23.724 12.459  1.00 68.40  ? 207 LEU   B CG  1 
ATOM   4547 C CD1 . LEU   B 1 207 ? 34.059 -22.271 12.442  1.00 68.15  ? 207 LEU   B CD1 1 
ATOM   4548 C CD2 . LEU   B 1 207 ? 35.522 -23.924 13.533  1.00 68.93  ? 207 LEU   B CD2 1 
ATOM   4549 N N   . TYR   B 1 208 ? 32.876 -23.662 9.494   1.00 69.30  ? 208 TYR   B N   1 
ATOM   4550 C CA  . TYR   B 1 208 ? 33.455 -23.536 8.175   1.00 69.90  ? 208 TYR   B CA  1 
ATOM   4551 C C   . TYR   B 1 208 ? 34.452 -22.372 8.152   1.00 72.31  ? 208 TYR   B C   1 
ATOM   4552 O O   . TYR   B 1 208 ? 34.130 -21.284 8.643   1.00 72.10  ? 208 TYR   B O   1 
ATOM   4553 C CB  . TYR   B 1 208 ? 32.350 -23.273 7.155   1.00 72.83  ? 208 TYR   B CB  1 
ATOM   4554 C CG  . TYR   B 1 208 ? 31.420 -24.435 6.911   1.00 77.57  ? 208 TYR   B CG  1 
ATOM   4555 C CD1 . TYR   B 1 208 ? 30.268 -24.603 7.675   1.00 80.21  ? 208 TYR   B CD1 1 
ATOM   4556 C CD2 . TYR   B 1 208 ? 31.657 -25.339 5.879   1.00 79.15  ? 208 TYR   B CD2 1 
ATOM   4557 C CE1 . TYR   B 1 208 ? 29.396 -25.666 7.445   1.00 82.64  ? 208 TYR   B CE1 1 
ATOM   4558 C CE2 . TYR   B 1 208 ? 30.789 -26.402 5.634   1.00 80.73  ? 208 TYR   B CE2 1 
ATOM   4559 C CZ  . TYR   B 1 208 ? 29.659 -26.563 6.422   1.00 90.85  ? 208 TYR   B CZ  1 
ATOM   4560 O OH  . TYR   B 1 208 ? 28.797 -27.610 6.193   1.00 92.91  ? 208 TYR   B OH  1 
ATOM   4561 N N   . LEU   B 1 209 ? 35.659 -22.598 7.587   1.00 67.29  ? 209 LEU   B N   1 
ATOM   4562 C CA  . LEU   B 1 209 ? 36.675 -21.554 7.438   1.00 66.02  ? 209 LEU   B CA  1 
ATOM   4563 C C   . LEU   B 1 209 ? 36.725 -21.151 5.975   1.00 70.59  ? 209 LEU   B C   1 
ATOM   4564 O O   . LEU   B 1 209 ? 36.898 -22.014 5.117   1.00 70.63  ? 209 LEU   B O   1 
ATOM   4565 C CB  . LEU   B 1 209 ? 38.076 -21.981 7.937   1.00 65.43  ? 209 LEU   B CB  1 
ATOM   4566 C CG  . LEU   B 1 209 ? 39.250 -21.028 7.590   1.00 69.21  ? 209 LEU   B CG  1 
ATOM   4567 C CD1 . LEU   B 1 209 ? 39.209 -19.751 8.418   1.00 69.12  ? 209 LEU   B CD1 1 
ATOM   4568 C CD2 . LEU   B 1 209 ? 40.588 -21.710 7.750   1.00 69.50  ? 209 LEU   B CD2 1 
ATOM   4569 N N   . SER   B 1 210 ? 36.553 -19.848 5.688   1.00 68.04  ? 210 SER   B N   1 
ATOM   4570 C CA  . SER   B 1 210 ? 36.617 -19.320 4.331   1.00 68.27  ? 210 SER   B CA  1 
ATOM   4571 C C   . SER   B 1 210 ? 37.918 -18.553 4.158   1.00 75.66  ? 210 SER   B C   1 
ATOM   4572 O O   . SER   B 1 210 ? 38.373 -17.875 5.088   1.00 74.52  ? 210 SER   B O   1 
ATOM   4573 C CB  . SER   B 1 210 ? 35.397 -18.473 3.979   1.00 70.77  ? 210 SER   B CB  1 
ATOM   4574 O OG  . SER   B 1 210 ? 35.462 -17.128 4.425   1.00 78.46  ? 210 SER   B OG  1 
ATOM   4575 N N   . THR   B 1 211 ? 38.531 -18.694 2.970   1.00 75.76  ? 211 THR   B N   1 
ATOM   4576 C CA  . THR   B 1 211 ? 39.801 -18.065 2.621   1.00 76.98  ? 211 THR   B CA  1 
ATOM   4577 C C   . THR   B 1 211 ? 39.872 -17.692 1.120   1.00 84.93  ? 211 THR   B C   1 
ATOM   4578 O O   . THR   B 1 211 ? 39.055 -18.147 0.314   1.00 83.84  ? 211 THR   B O   1 
ATOM   4579 C CB  . THR   B 1 211 ? 40.965 -18.958 3.151   1.00 83.66  ? 211 THR   B CB  1 
ATOM   4580 O OG1 . THR   B 1 211 ? 41.902 -18.189 3.903   1.00 82.84  ? 211 THR   B OG1 1 
ATOM   4581 C CG2 . THR   B 1 211 ? 41.658 -19.760 2.075   1.00 81.31  ? 211 THR   B CG2 1 
ATOM   4582 N N   . LYS   B 1 212 ? 40.857 -16.851 0.771   1.00 85.60  ? 212 LYS   B N   1 
ATOM   4583 C CA  . LYS   B 1 212 ? 41.146 -16.419 -0.592  1.00 86.97  ? 212 LYS   B CA  1 
ATOM   4584 C C   . LYS   B 1 212 ? 42.612 -16.839 -0.899  1.00 94.26  ? 212 LYS   B C   1 
ATOM   4585 O O   . LYS   B 1 212 ? 43.431 -15.994 -1.280  1.00 94.51  ? 212 LYS   B O   1 
ATOM   4586 C CB  . LYS   B 1 212 ? 40.918 -14.900 -0.745  1.00 89.26  ? 212 LYS   B CB  1 
ATOM   4587 N N   . ASN   B 1 213 ? 42.937 -18.158 -0.703  1.00 92.20  ? 213 ASN   B N   1 
ATOM   4588 C CA  . ASN   B 1 213 ? 44.276 -18.734 -0.939  1.00 92.46  ? 213 ASN   B CA  1 
ATOM   4589 C C   . ASN   B 1 213 ? 44.618 -19.040 -2.402  1.00 97.03  ? 213 ASN   B C   1 
ATOM   4590 O O   . ASN   B 1 213 ? 45.536 -19.816 -2.682  1.00 96.84  ? 213 ASN   B O   1 
ATOM   4591 C CB  . ASN   B 1 213 ? 44.655 -19.878 0.037   1.00 93.36  ? 213 ASN   B CB  1 
ATOM   4592 C CG  . ASN   B 1 213 ? 44.017 -21.231 -0.198  1.00 112.63 ? 213 ASN   B CG  1 
ATOM   4593 O OD1 . ASN   B 1 213 ? 42.847 -21.353 -0.580  1.00 106.17 ? 213 ASN   B OD1 1 
ATOM   4594 N ND2 . ASN   B 1 213 ? 44.780 -22.289 0.054   1.00 101.80 ? 213 ASN   B ND2 1 
ATOM   4595 N N   . THR   B 1 214 ? 43.881 -18.405 -3.329  1.00 93.55  ? 214 THR   B N   1 
ATOM   4596 C CA  . THR   B 1 214 ? 44.099 -18.485 -4.771  1.00 93.04  ? 214 THR   B CA  1 
ATOM   4597 C C   . THR   B 1 214 ? 45.102 -17.342 -5.065  1.00 95.33  ? 214 THR   B C   1 
ATOM   4598 O O   . THR   B 1 214 ? 46.094 -17.543 -5.775  1.00 94.99  ? 214 THR   B O   1 
ATOM   4599 C CB  . THR   B 1 214 ? 42.763 -18.364 -5.550  1.00 100.45 ? 214 THR   B CB  1 
ATOM   4600 O OG1 . THR   B 1 214 ? 41.990 -17.271 -5.041  1.00 101.03 ? 214 THR   B OG1 1 
ATOM   4601 C CG2 . THR   B 1 214 ? 41.946 -19.649 -5.513  1.00 97.32  ? 214 THR   B CG2 1 
ATOM   4602 N N   . ILE   B 1 215 ? 44.842 -16.154 -4.461  1.00 89.59  ? 215 ILE   B N   1 
ATOM   4603 C CA  . ILE   B 1 215 ? 45.648 -14.933 -4.548  1.00 87.82  ? 215 ILE   B CA  1 
ATOM   4604 C C   . ILE   B 1 215 ? 46.765 -15.035 -3.468  1.00 89.91  ? 215 ILE   B C   1 
ATOM   4605 O O   . ILE   B 1 215 ? 47.853 -15.539 -3.767  1.00 89.48  ? 215 ILE   B O   1 
ATOM   4606 C CB  . ILE   B 1 215 ? 44.749 -13.664 -4.385  1.00 90.39  ? 215 ILE   B CB  1 
ATOM   4607 C CG1 . ILE   B 1 215 ? 43.427 -13.773 -5.172  1.00 90.60  ? 215 ILE   B CG1 1 
ATOM   4608 C CG2 . ILE   B 1 215 ? 45.498 -12.381 -4.736  1.00 90.82  ? 215 ILE   B CG2 1 
ATOM   4609 C CD1 . ILE   B 1 215 ? 42.204 -13.885 -4.298  1.00 95.96  ? 215 ILE   B CD1 1 
ATOM   4610 N N   . LEU   B 1 216 ? 46.472 -14.604 -2.211  1.00 84.59  ? 216 LEU   B N   1 
ATOM   4611 C CA  . LEU   B 1 216 ? 47.373 -14.621 -1.044  1.00 82.71  ? 216 LEU   B CA  1 
ATOM   4612 C C   . LEU   B 1 216 ? 47.619 -16.057 -0.552  1.00 82.94  ? 216 LEU   B C   1 
ATOM   4613 O O   . LEU   B 1 216 ? 47.388 -16.374 0.617   1.00 82.47  ? 216 LEU   B O   1 
ATOM   4614 C CB  . LEU   B 1 216 ? 46.769 -13.749 0.077   1.00 82.50  ? 216 LEU   B CB  1 
ATOM   4615 C CG  . LEU   B 1 216 ? 47.670 -12.719 0.740   1.00 86.76  ? 216 LEU   B CG  1 
ATOM   4616 C CD1 . LEU   B 1 216 ? 48.145 -11.674 -0.248  1.00 86.87  ? 216 LEU   B CD1 1 
ATOM   4617 C CD2 . LEU   B 1 216 ? 46.933 -12.022 1.851   1.00 89.31  ? 216 LEU   B CD2 1 
ATOM   4618 N N   . LYS   B 1 217 ? 48.101 -16.910 -1.469  1.00 77.12  ? 217 LYS   B N   1 
ATOM   4619 C CA  . LYS   B 1 217 ? 48.408 -18.323 -1.288  1.00 76.16  ? 217 LYS   B CA  1 
ATOM   4620 C C   . LYS   B 1 217 ? 49.036 -18.689 0.068   1.00 77.72  ? 217 LYS   B C   1 
ATOM   4621 O O   . LYS   B 1 217 ? 48.379 -19.348 0.867   1.00 77.49  ? 217 LYS   B O   1 
ATOM   4622 C CB  . LYS   B 1 217 ? 49.274 -18.838 -2.451  1.00 78.69  ? 217 LYS   B CB  1 
ATOM   4623 C CG  . LYS   B 1 217 ? 48.530 -19.083 -3.760  1.00 90.22  ? 217 LYS   B CG  1 
ATOM   4624 C CD  . LYS   B 1 217 ? 49.465 -19.652 -4.843  1.00 100.45 ? 217 LYS   B CD  1 
ATOM   4625 C CE  . LYS   B 1 217 ? 49.936 -21.074 -4.592  1.00 108.00 ? 217 LYS   B CE  1 
ATOM   4626 N NZ  . LYS   B 1 217 ? 51.414 -21.207 -4.723  1.00 112.66 ? 217 LYS   B NZ  1 
ATOM   4627 N N   . LYS   B 1 218 ? 50.284 -18.259 0.324   1.00 72.34  ? 218 LYS   B N   1 
ATOM   4628 C CA  . LYS   B 1 218 ? 51.030 -18.562 1.553   1.00 71.45  ? 218 LYS   B CA  1 
ATOM   4629 C C   . LYS   B 1 218 ? 50.408 -18.027 2.856   1.00 73.35  ? 218 LYS   B C   1 
ATOM   4630 O O   . LYS   B 1 218 ? 50.379 -18.750 3.861   1.00 73.22  ? 218 LYS   B O   1 
ATOM   4631 C CB  . LYS   B 1 218 ? 52.512 -18.172 1.415   1.00 73.78  ? 218 LYS   B CB  1 
ATOM   4632 C CG  . LYS   B 1 218 ? 53.319 -19.094 0.503   1.00 80.37  ? 218 LYS   B CG  1 
ATOM   4633 C CD  . LYS   B 1 218 ? 53.400 -18.573 -0.924  1.00 85.59  ? 218 LYS   B CD  1 
ATOM   4634 C CE  . LYS   B 1 218 ? 53.530 -19.710 -1.903  1.00 96.70  ? 218 LYS   B CE  1 
ATOM   4635 N NZ  . LYS   B 1 218 ? 53.424 -19.237 -3.305  1.00 109.29 ? 218 LYS   B NZ  1 
ATOM   4636 N N   . TYR   B 1 219 ? 49.906 -16.779 2.832   1.00 67.75  ? 219 TYR   B N   1 
ATOM   4637 C CA  . TYR   B 1 219 ? 49.268 -16.123 3.976   1.00 66.85  ? 219 TYR   B CA  1 
ATOM   4638 C C   . TYR   B 1 219 ? 48.012 -16.880 4.404   1.00 69.68  ? 219 TYR   B C   1 
ATOM   4639 O O   . TYR   B 1 219 ? 47.911 -17.301 5.559   1.00 68.58  ? 219 TYR   B O   1 
ATOM   4640 C CB  . TYR   B 1 219 ? 48.942 -14.657 3.645   1.00 67.55  ? 219 TYR   B CB  1 
ATOM   4641 C CG  . TYR   B 1 219 ? 49.117 -13.697 4.799   1.00 68.13  ? 219 TYR   B CG  1 
ATOM   4642 C CD1 . TYR   B 1 219 ? 50.295 -12.968 4.954   1.00 69.59  ? 219 TYR   B CD1 1 
ATOM   4643 C CD2 . TYR   B 1 219 ? 48.104 -13.508 5.735   1.00 68.64  ? 219 TYR   B CD2 1 
ATOM   4644 C CE1 . TYR   B 1 219 ? 50.461 -12.074 6.013   1.00 69.60  ? 219 TYR   B CE1 1 
ATOM   4645 C CE2 . TYR   B 1 219 ? 48.263 -12.629 6.807   1.00 69.32  ? 219 TYR   B CE2 1 
ATOM   4646 C CZ  . TYR   B 1 219 ? 49.439 -11.906 6.935   1.00 76.57  ? 219 TYR   B CZ  1 
ATOM   4647 O OH  . TYR   B 1 219 ? 49.582 -11.024 7.980   1.00 77.85  ? 219 TYR   B OH  1 
ATOM   4648 N N   . ASP   B 1 220 ? 47.083 -17.081 3.456   1.00 66.09  ? 220 ASP   B N   1 
ATOM   4649 C CA  . ASP   B 1 220 ? 45.824 -17.782 3.686   1.00 65.96  ? 220 ASP   B CA  1 
ATOM   4650 C C   . ASP   B 1 220 ? 45.985 -19.296 3.856   1.00 69.66  ? 220 ASP   B C   1 
ATOM   4651 O O   . ASP   B 1 220 ? 45.217 -19.906 4.599   1.00 70.94  ? 220 ASP   B O   1 
ATOM   4652 C CB  . ASP   B 1 220 ? 44.790 -17.407 2.610   1.00 67.87  ? 220 ASP   B CB  1 
ATOM   4653 C CG  . ASP   B 1 220 ? 44.356 -15.941 2.619   1.00 79.22  ? 220 ASP   B CG  1 
ATOM   4654 O OD1 . ASP   B 1 220 ? 43.410 -15.598 1.875   1.00 79.91  ? 220 ASP   B OD1 1 
ATOM   4655 O OD2 . ASP   B 1 220 ? 44.961 -15.136 3.374   1.00 84.90  ? 220 ASP   B OD2 1 
ATOM   4656 N N   . GLY   B 1 221 ? 46.991 -19.880 3.204   1.00 64.14  ? 221 GLY   B N   1 
ATOM   4657 C CA  . GLY   B 1 221 ? 47.294 -21.307 3.296   1.00 62.50  ? 221 GLY   B CA  1 
ATOM   4658 C C   . GLY   B 1 221 ? 47.690 -21.725 4.699   1.00 64.69  ? 221 GLY   B C   1 
ATOM   4659 O O   . GLY   B 1 221 ? 47.448 -22.864 5.102   1.00 63.86  ? 221 GLY   B O   1 
ATOM   4660 N N   . ARG   B 1 222 ? 48.288 -20.798 5.467   1.00 61.05  ? 222 ARG   B N   1 
ATOM   4661 C CA  . ARG   B 1 222 ? 48.686 -21.066 6.846   1.00 60.30  ? 222 ARG   B CA  1 
ATOM   4662 C C   . ARG   B 1 222 ? 47.468 -21.181 7.747   1.00 64.86  ? 222 ARG   B C   1 
ATOM   4663 O O   . ARG   B 1 222 ? 47.482 -21.977 8.694   1.00 64.33  ? 222 ARG   B O   1 
ATOM   4664 C CB  . ARG   B 1 222 ? 49.645 -20.007 7.369   1.00 56.00  ? 222 ARG   B CB  1 
ATOM   4665 C CG  . ARG   B 1 222 ? 50.972 -20.631 7.710   1.00 58.58  ? 222 ARG   B CG  1 
ATOM   4666 C CD  . ARG   B 1 222 ? 51.343 -20.367 9.135   1.00 56.88  ? 222 ARG   B CD  1 
ATOM   4667 N NE  . ARG   B 1 222 ? 52.763 -20.622 9.371   1.00 71.70  ? 222 ARG   B NE  1 
ATOM   4668 C CZ  . ARG   B 1 222 ? 53.250 -21.730 9.920   1.00 85.72  ? 222 ARG   B CZ  1 
ATOM   4669 N NH1 . ARG   B 1 222 ? 52.432 -22.708 10.297  1.00 79.83  ? 222 ARG   B NH1 1 
ATOM   4670 N NH2 . ARG   B 1 222 ? 54.558 -21.867 10.104  1.00 58.73  ? 222 ARG   B NH2 1 
ATOM   4671 N N   . PHE   B 1 223 ? 46.417 -20.386 7.442   1.00 61.09  ? 223 PHE   B N   1 
ATOM   4672 C CA  . PHE   B 1 223 ? 45.162 -20.384 8.178   1.00 61.25  ? 223 PHE   B CA  1 
ATOM   4673 C C   . PHE   B 1 223 ? 44.474 -21.727 7.949   1.00 66.52  ? 223 PHE   B C   1 
ATOM   4674 O O   . PHE   B 1 223 ? 44.024 -22.341 8.916   1.00 67.16  ? 223 PHE   B O   1 
ATOM   4675 C CB  . PHE   B 1 223 ? 44.273 -19.208 7.740   1.00 63.05  ? 223 PHE   B CB  1 
ATOM   4676 C CG  . PHE   B 1 223 ? 44.551 -17.900 8.450   1.00 64.70  ? 223 PHE   B CG  1 
ATOM   4677 C CD1 . PHE   B 1 223 ? 45.701 -17.168 8.172   1.00 67.35  ? 223 PHE   B CD1 1 
ATOM   4678 C CD2 . PHE   B 1 223 ? 43.648 -17.387 9.374   1.00 66.83  ? 223 PHE   B CD2 1 
ATOM   4679 C CE1 . PHE   B 1 223 ? 45.952 -15.960 8.820   1.00 68.36  ? 223 PHE   B CE1 1 
ATOM   4680 C CE2 . PHE   B 1 223 ? 43.899 -16.177 10.024  1.00 69.48  ? 223 PHE   B CE2 1 
ATOM   4681 C CZ  . PHE   B 1 223 ? 45.051 -15.474 9.746   1.00 67.85  ? 223 PHE   B CZ  1 
ATOM   4682 N N   . LYS   B 1 224 ? 44.442 -22.201 6.676   1.00 62.45  ? 224 LYS   B N   1 
ATOM   4683 C CA  . LYS   B 1 224 ? 43.859 -23.482 6.258   1.00 61.55  ? 224 LYS   B CA  1 
ATOM   4684 C C   . LYS   B 1 224 ? 44.514 -24.642 7.033   1.00 65.76  ? 224 LYS   B C   1 
ATOM   4685 O O   . LYS   B 1 224 ? 43.800 -25.452 7.628   1.00 65.61  ? 224 LYS   B O   1 
ATOM   4686 C CB  . LYS   B 1 224 ? 44.024 -23.657 4.736   1.00 62.42  ? 224 LYS   B CB  1 
ATOM   4687 C CG  . LYS   B 1 224 ? 43.336 -24.879 4.155   1.00 68.53  ? 224 LYS   B CG  1 
ATOM   4688 C CD  . LYS   B 1 224 ? 43.488 -24.954 2.637   1.00 73.02  ? 224 LYS   B CD  1 
ATOM   4689 C CE  . LYS   B 1 224 ? 43.085 -26.311 2.104   1.00 77.88  ? 224 LYS   B CE  1 
ATOM   4690 N NZ  . LYS   B 1 224 ? 43.024 -26.334 0.619   1.00 84.54  ? 224 LYS   B NZ  1 
ATOM   4691 N N   . ASP   B 1 225 ? 45.864 -24.680 7.049   1.00 62.51  ? 225 ASP   B N   1 
ATOM   4692 C CA  . ASP   B 1 225 ? 46.688 -25.697 7.715   1.00 62.40  ? 225 ASP   B CA  1 
ATOM   4693 C C   . ASP   B 1 225 ? 46.589 -25.690 9.248   1.00 66.20  ? 225 ASP   B C   1 
ATOM   4694 O O   . ASP   B 1 225 ? 46.443 -26.758 9.836   1.00 66.16  ? 225 ASP   B O   1 
ATOM   4695 C CB  . ASP   B 1 225 ? 48.165 -25.610 7.259   1.00 64.42  ? 225 ASP   B CB  1 
ATOM   4696 C CG  . ASP   B 1 225 ? 48.453 -25.806 5.766   1.00 75.59  ? 225 ASP   B CG  1 
ATOM   4697 O OD1 . ASP   B 1 225 ? 49.625 -25.626 5.358   1.00 76.77  ? 225 ASP   B OD1 1 
ATOM   4698 O OD2 . ASP   B 1 225 ? 47.509 -26.131 5.007   1.00 79.91  ? 225 ASP   B OD2 1 
ATOM   4699 N N   . ILE   B 1 226 ? 46.678 -24.511 9.895   1.00 62.81  ? 226 ILE   B N   1 
ATOM   4700 C CA  . ILE   B 1 226 ? 46.594 -24.401 11.357  1.00 62.50  ? 226 ILE   B CA  1 
ATOM   4701 C C   . ILE   B 1 226 ? 45.214 -24.857 11.882  1.00 67.82  ? 226 ILE   B C   1 
ATOM   4702 O O   . ILE   B 1 226 ? 45.147 -25.549 12.899  1.00 67.66  ? 226 ILE   B O   1 
ATOM   4703 C CB  . ILE   B 1 226 ? 47.047 -23.004 11.869  1.00 65.22  ? 226 ILE   B CB  1 
ATOM   4704 C CG1 . ILE   B 1 226 ? 48.597 -22.867 11.782  1.00 64.48  ? 226 ILE   B CG1 1 
ATOM   4705 C CG2 . ILE   B 1 226 ? 46.537 -22.715 13.306  1.00 66.35  ? 226 ILE   B CG2 1 
ATOM   4706 C CD1 . ILE   B 1 226 ? 49.170 -21.475 12.061  1.00 58.11  ? 226 ILE   B CD1 1 
ATOM   4707 N N   . PHE   B 1 227 ? 44.131 -24.495 11.178  1.00 64.88  ? 227 PHE   B N   1 
ATOM   4708 C CA  . PHE   B 1 227 ? 42.777 -24.885 11.567  1.00 65.26  ? 227 PHE   B CA  1 
ATOM   4709 C C   . PHE   B 1 227 ? 42.646 -26.413 11.551  1.00 71.54  ? 227 PHE   B C   1 
ATOM   4710 O O   . PHE   B 1 227 ? 42.269 -27.002 12.570  1.00 71.73  ? 227 PHE   B O   1 
ATOM   4711 C CB  . PHE   B 1 227 ? 41.730 -24.214 10.660  1.00 66.70  ? 227 PHE   B CB  1 
ATOM   4712 C CG  . PHE   B 1 227 ? 41.166 -22.896 11.151  1.00 67.70  ? 227 PHE   B CG  1 
ATOM   4713 C CD1 . PHE   B 1 227 ? 41.986 -21.782 11.313  1.00 70.23  ? 227 PHE   B CD1 1 
ATOM   4714 C CD2 . PHE   B 1 227 ? 39.808 -22.758 11.406  1.00 69.22  ? 227 PHE   B CD2 1 
ATOM   4715 C CE1 . PHE   B 1 227 ? 41.461 -20.560 11.746  1.00 70.71  ? 227 PHE   B CE1 1 
ATOM   4716 C CE2 . PHE   B 1 227 ? 39.282 -21.534 11.834  1.00 71.93  ? 227 PHE   B CE2 1 
ATOM   4717 C CZ  . PHE   B 1 227 ? 40.112 -20.442 11.998  1.00 69.80  ? 227 PHE   B CZ  1 
ATOM   4718 N N   . GLN   B 1 228 ? 43.014 -27.047 10.418  1.00 69.28  ? 228 GLN   B N   1 
ATOM   4719 C CA  . GLN   B 1 228 ? 42.986 -28.497 10.223  1.00 69.47  ? 228 GLN   B CA  1 
ATOM   4720 C C   . GLN   B 1 228 ? 43.819 -29.246 11.276  1.00 76.09  ? 228 GLN   B C   1 
ATOM   4721 O O   . GLN   B 1 228 ? 43.333 -30.232 11.820  1.00 76.29  ? 228 GLN   B O   1 
ATOM   4722 C CB  . GLN   B 1 228 ? 43.461 -28.856 8.817   1.00 70.35  ? 228 GLN   B CB  1 
ATOM   4723 C CG  . GLN   B 1 228 ? 42.917 -30.183 8.313   1.00 80.79  ? 228 GLN   B CG  1 
ATOM   4724 C CD  . GLN   B 1 228 ? 41.499 -30.073 7.799   1.00 93.44  ? 228 GLN   B CD  1 
ATOM   4725 O OE1 . GLN   B 1 228 ? 40.595 -30.778 8.263   1.00 87.56  ? 228 GLN   B OE1 1 
ATOM   4726 N NE2 . GLN   B 1 228 ? 41.271 -29.190 6.829   1.00 79.90  ? 228 GLN   B NE2 1 
ATOM   4727 N N   . GLU   B 1 229 ? 45.049 -28.774 11.574  1.00 73.87  ? 229 GLU   B N   1 
ATOM   4728 C CA  . GLU   B 1 229 ? 45.925 -29.408 12.566  1.00 74.67  ? 229 GLU   B CA  1 
ATOM   4729 C C   . GLU   B 1 229 ? 45.284 -29.391 13.950  1.00 80.86  ? 229 GLU   B C   1 
ATOM   4730 O O   . GLU   B 1 229 ? 45.276 -30.422 14.618  1.00 80.32  ? 229 GLU   B O   1 
ATOM   4731 C CB  . GLU   B 1 229 ? 47.323 -28.760 12.595  1.00 76.20  ? 229 GLU   B CB  1 
ATOM   4732 C CG  . GLU   B 1 229 ? 48.186 -29.075 11.381  1.00 89.73  ? 229 GLU   B CG  1 
ATOM   4733 C CD  . GLU   B 1 229 ? 49.511 -28.335 11.337  1.00 116.38 ? 229 GLU   B CD  1 
ATOM   4734 O OE1 . GLU   B 1 229 ? 50.451 -28.756 12.050  1.00 113.83 ? 229 GLU   B OE1 1 
ATOM   4735 O OE2 . GLU   B 1 229 ? 49.611 -27.336 10.587  1.00 108.99 ? 229 GLU   B OE2 1 
ATOM   4736 N N   . ILE   B 1 230 ? 44.724 -28.225 14.363  1.00 79.23  ? 230 ILE   B N   1 
ATOM   4737 C CA  . ILE   B 1 230 ? 44.043 -28.016 15.654  1.00 79.12  ? 230 ILE   B CA  1 
ATOM   4738 C C   . ILE   B 1 230 ? 42.804 -28.934 15.759  1.00 82.19  ? 230 ILE   B C   1 
ATOM   4739 O O   . ILE   B 1 230 ? 42.573 -29.524 16.814  1.00 80.99  ? 230 ILE   B O   1 
ATOM   4740 C CB  . ILE   B 1 230 ? 43.724 -26.499 15.877  1.00 82.16  ? 230 ILE   B CB  1 
ATOM   4741 C CG1 . ILE   B 1 230 ? 45.004 -25.662 16.194  1.00 82.52  ? 230 ILE   B CG1 1 
ATOM   4742 C CG2 . ILE   B 1 230 ? 42.616 -26.256 16.908  1.00 82.59  ? 230 ILE   B CG2 1 
ATOM   4743 C CD1 . ILE   B 1 230 ? 45.733 -25.888 17.617  1.00 91.02  ? 230 ILE   B CD1 1 
ATOM   4744 N N   . TYR   B 1 231 ? 42.041 -29.063 14.650  1.00 78.89  ? 231 TYR   B N   1 
ATOM   4745 C CA  . TYR   B 1 231 ? 40.843 -29.897 14.549  1.00 78.86  ? 231 TYR   B CA  1 
ATOM   4746 C C   . TYR   B 1 231 ? 41.204 -31.360 14.827  1.00 81.66  ? 231 TYR   B C   1 
ATOM   4747 O O   . TYR   B 1 231 ? 40.748 -31.931 15.821  1.00 81.10  ? 231 TYR   B O   1 
ATOM   4748 C CB  . TYR   B 1 231 ? 40.202 -29.732 13.154  1.00 80.41  ? 231 TYR   B CB  1 
ATOM   4749 C CG  . TYR   B 1 231 ? 38.892 -30.467 12.948  1.00 83.50  ? 231 TYR   B CG  1 
ATOM   4750 C CD1 . TYR   B 1 231 ? 37.852 -30.358 13.872  1.00 85.93  ? 231 TYR   B CD1 1 
ATOM   4751 C CD2 . TYR   B 1 231 ? 38.663 -31.216 11.796  1.00 84.49  ? 231 TYR   B CD2 1 
ATOM   4752 C CE1 . TYR   B 1 231 ? 36.631 -31.007 13.672  1.00 87.13  ? 231 TYR   B CE1 1 
ATOM   4753 C CE2 . TYR   B 1 231 ? 37.445 -31.867 11.583  1.00 85.51  ? 231 TYR   B CE2 1 
ATOM   4754 C CZ  . TYR   B 1 231 ? 36.433 -31.763 12.527  1.00 92.00  ? 231 TYR   B CZ  1 
ATOM   4755 O OH  . TYR   B 1 231 ? 35.232 -32.403 12.326  1.00 89.76  ? 231 TYR   B OH  1 
ATOM   4756 N N   . ASP   B 1 232 ? 42.067 -31.937 13.968  1.00 77.18  ? 232 ASP   B N   1 
ATOM   4757 C CA  . ASP   B 1 232 ? 42.565 -33.310 14.036  1.00 75.65  ? 232 ASP   B CA  1 
ATOM   4758 C C   . ASP   B 1 232 ? 43.248 -33.644 15.377  1.00 78.96  ? 232 ASP   B C   1 
ATOM   4759 O O   . ASP   B 1 232 ? 43.118 -34.770 15.846  1.00 78.93  ? 232 ASP   B O   1 
ATOM   4760 C CB  . ASP   B 1 232 ? 43.506 -33.596 12.845  1.00 76.46  ? 232 ASP   B CB  1 
ATOM   4761 C CG  . ASP   B 1 232 ? 42.939 -33.322 11.451  1.00 80.13  ? 232 ASP   B CG  1 
ATOM   4762 O OD1 . ASP   B 1 232 ? 41.735 -33.008 11.345  1.00 80.03  ? 232 ASP   B OD1 1 
ATOM   4763 O OD2 . ASP   B 1 232 ? 43.705 -33.416 10.469  1.00 82.80  ? 232 ASP   B OD2 1 
ATOM   4764 N N   . LYS   B 1 233 ? 43.943 -32.672 16.002  1.00 74.84  ? 233 LYS   B N   1 
ATOM   4765 C CA  . LYS   B 1 233 ? 44.656 -32.880 17.269  1.00 74.32  ? 233 LYS   B CA  1 
ATOM   4766 C C   . LYS   B 1 233 ? 43.879 -32.669 18.575  1.00 77.52  ? 233 LYS   B C   1 
ATOM   4767 O O   . LYS   B 1 233 ? 44.378 -33.090 19.627  1.00 76.91  ? 233 LYS   B O   1 
ATOM   4768 C CB  . LYS   B 1 233 ? 45.991 -32.119 17.296  1.00 76.76  ? 233 LYS   B CB  1 
ATOM   4769 N N   . GLN   B 1 234 ? 42.688 -32.018 18.535  1.00 73.43  ? 234 GLN   B N   1 
ATOM   4770 C CA  . GLN   B 1 234 ? 41.893 -31.781 19.758  1.00 73.00  ? 234 GLN   B CA  1 
ATOM   4771 C C   . GLN   B 1 234 ? 40.406 -31.453 19.568  1.00 76.51  ? 234 GLN   B C   1 
ATOM   4772 O O   . GLN   B 1 234 ? 39.759 -31.079 20.546  1.00 75.99  ? 234 GLN   B O   1 
ATOM   4773 C CB  . GLN   B 1 234 ? 42.580 -30.790 20.746  1.00 74.18  ? 234 GLN   B CB  1 
ATOM   4774 C CG  . GLN   B 1 234 ? 42.987 -29.436 20.159  1.00 82.50  ? 234 GLN   B CG  1 
ATOM   4775 C CD  . GLN   B 1 234 ? 43.723 -28.541 21.144  1.00 96.18  ? 234 GLN   B CD  1 
ATOM   4776 O OE1 . GLN   B 1 234 ? 44.849 -28.089 20.887  1.00 84.61  ? 234 GLN   B OE1 1 
ATOM   4777 N NE2 . GLN   B 1 234 ? 43.103 -28.248 22.292  1.00 88.72  ? 234 GLN   B NE2 1 
ATOM   4778 N N   . TYR   B 1 235 ? 39.854 -31.601 18.344  1.00 73.40  ? 235 TYR   B N   1 
ATOM   4779 C CA  . TYR   B 1 235 ? 38.442 -31.267 18.109  1.00 73.46  ? 235 TYR   B CA  1 
ATOM   4780 C C   . TYR   B 1 235 ? 37.599 -32.260 17.330  1.00 81.87  ? 235 TYR   B C   1 
ATOM   4781 O O   . TYR   B 1 235 ? 36.409 -32.355 17.621  1.00 82.04  ? 235 TYR   B O   1 
ATOM   4782 C CB  . TYR   B 1 235 ? 38.275 -29.836 17.538  1.00 72.54  ? 235 TYR   B CB  1 
ATOM   4783 C CG  . TYR   B 1 235 ? 38.607 -28.746 18.535  1.00 70.64  ? 235 TYR   B CG  1 
ATOM   4784 C CD1 . TYR   B 1 235 ? 39.825 -28.074 18.483  1.00 71.51  ? 235 TYR   B CD1 1 
ATOM   4785 C CD2 . TYR   B 1 235 ? 37.717 -28.406 19.547  1.00 70.68  ? 235 TYR   B CD2 1 
ATOM   4786 C CE1 . TYR   B 1 235 ? 40.147 -27.083 19.410  1.00 69.71  ? 235 TYR   B CE1 1 
ATOM   4787 C CE2 . TYR   B 1 235 ? 38.029 -27.417 20.482  1.00 71.21  ? 235 TYR   B CE2 1 
ATOM   4788 C CZ  . TYR   B 1 235 ? 39.246 -26.756 20.408  1.00 73.44  ? 235 TYR   B CZ  1 
ATOM   4789 O OH  . TYR   B 1 235 ? 39.562 -25.782 21.324  1.00 67.81  ? 235 TYR   B OH  1 
ATOM   4790 N N   . LYS   B 1 236 ? 38.180 -32.979 16.344  1.00 81.62  ? 236 LYS   B N   1 
ATOM   4791 C CA  . LYS   B 1 236 ? 37.472 -33.957 15.493  1.00 82.83  ? 236 LYS   B CA  1 
ATOM   4792 C C   . LYS   B 1 236 ? 36.559 -34.941 16.244  1.00 90.09  ? 236 LYS   B C   1 
ATOM   4793 O O   . LYS   B 1 236 ? 35.465 -35.237 15.757  1.00 90.46  ? 236 LYS   B O   1 
ATOM   4794 C CB  . LYS   B 1 236 ? 38.441 -34.709 14.565  1.00 84.98  ? 236 LYS   B CB  1 
ATOM   4795 N N   . SER   B 1 237 ? 37.007 -35.429 17.426  1.00 87.94  ? 237 SER   B N   1 
ATOM   4796 C CA  . SER   B 1 237 ? 36.275 -36.371 18.281  1.00 88.52  ? 237 SER   B CA  1 
ATOM   4797 C C   . SER   B 1 237 ? 34.883 -35.838 18.618  1.00 93.03  ? 237 SER   B C   1 
ATOM   4798 O O   . SER   B 1 237 ? 33.884 -36.365 18.120  1.00 92.40  ? 237 SER   B O   1 
ATOM   4799 C CB  . SER   B 1 237 ? 37.052 -36.642 19.572  1.00 92.33  ? 237 SER   B CB  1 
ATOM   4800 O OG  . SER   B 1 237 ? 38.085 -37.595 19.388  1.00 101.84 ? 237 SER   B OG  1 
ATOM   4801 N N   . GLN   B 1 238 ? 34.843 -34.765 19.433  1.00 89.80  ? 238 GLN   B N   1 
ATOM   4802 C CA  . GLN   B 1 238 ? 33.651 -34.066 19.909  1.00 89.67  ? 238 GLN   B CA  1 
ATOM   4803 C C   . GLN   B 1 238 ? 32.749 -33.515 18.810  1.00 94.31  ? 238 GLN   B C   1 
ATOM   4804 O O   . GLN   B 1 238 ? 31.547 -33.383 19.037  1.00 94.31  ? 238 GLN   B O   1 
ATOM   4805 C CB  . GLN   B 1 238 ? 34.007 -32.988 20.943  1.00 90.63  ? 238 GLN   B CB  1 
ATOM   4806 C CG  . GLN   B 1 238 ? 35.466 -32.541 20.911  1.00 98.33  ? 238 GLN   B CG  1 
ATOM   4807 C CD  . GLN   B 1 238 ? 35.883 -31.783 22.144  1.00 113.88 ? 238 GLN   B CD  1 
ATOM   4808 O OE1 . GLN   B 1 238 ? 35.101 -31.555 23.078  1.00 108.87 ? 238 GLN   B OE1 1 
ATOM   4809 N NE2 . GLN   B 1 238 ? 37.141 -31.374 22.173  1.00 103.89 ? 238 GLN   B NE2 1 
ATOM   4810 N N   . PHE   B 1 239 ? 33.313 -33.214 17.627  1.00 91.19  ? 239 PHE   B N   1 
ATOM   4811 C CA  . PHE   B 1 239 ? 32.554 -32.703 16.483  1.00 91.33  ? 239 PHE   B CA  1 
ATOM   4812 C C   . PHE   B 1 239 ? 31.732 -33.834 15.869  1.00 96.68  ? 239 PHE   B C   1 
ATOM   4813 O O   . PHE   B 1 239 ? 30.518 -33.691 15.737  1.00 96.29  ? 239 PHE   B O   1 
ATOM   4814 C CB  . PHE   B 1 239 ? 33.482 -32.023 15.450  1.00 92.78  ? 239 PHE   B CB  1 
ATOM   4815 C CG  . PHE   B 1 239 ? 33.684 -30.535 15.654  1.00 93.72  ? 239 PHE   B CG  1 
ATOM   4816 C CD1 . PHE   B 1 239 ? 34.155 -30.037 16.865  1.00 96.23  ? 239 PHE   B CD1 1 
ATOM   4817 C CD2 . PHE   B 1 239 ? 33.434 -29.635 14.625  1.00 95.32  ? 239 PHE   B CD2 1 
ATOM   4818 C CE1 . PHE   B 1 239 ? 34.345 -28.666 17.048  1.00 96.97  ? 239 PHE   B CE1 1 
ATOM   4819 C CE2 . PHE   B 1 239 ? 33.617 -28.263 14.812  1.00 97.81  ? 239 PHE   B CE2 1 
ATOM   4820 C CZ  . PHE   B 1 239 ? 34.070 -27.789 16.022  1.00 95.88  ? 239 PHE   B CZ  1 
ATOM   4821 N N   . GLU   B 1 240 ? 32.389 -34.972 15.543  1.00 94.50  ? 240 GLU   B N   1 
ATOM   4822 C CA  . GLU   B 1 240 ? 31.771 -36.178 14.972  1.00 94.40  ? 240 GLU   B CA  1 
ATOM   4823 C C   . GLU   B 1 240 ? 30.757 -36.801 15.964  1.00 97.81  ? 240 GLU   B C   1 
ATOM   4824 O O   . GLU   B 1 240 ? 29.731 -37.343 15.537  1.00 97.15  ? 240 GLU   B O   1 
ATOM   4825 C CB  . GLU   B 1 240 ? 32.857 -37.197 14.578  1.00 95.69  ? 240 GLU   B CB  1 
ATOM   4826 N N   . ALA   B 1 241 ? 31.046 -36.681 17.287  1.00 93.67  ? 241 ALA   B N   1 
ATOM   4827 C CA  . ALA   B 1 241 ? 30.242 -37.171 18.413  1.00 93.07  ? 241 ALA   B CA  1 
ATOM   4828 C C   . ALA   B 1 241 ? 29.082 -36.212 18.804  1.00 96.53  ? 241 ALA   B C   1 
ATOM   4829 O O   . ALA   B 1 241 ? 28.490 -36.353 19.882  1.00 96.64  ? 241 ALA   B O   1 
ATOM   4830 C CB  . ALA   B 1 241 ? 31.145 -37.436 19.613  1.00 93.72  ? 241 ALA   B CB  1 
ATOM   4831 N N   . GLN   B 1 242 ? 28.765 -35.247 17.923  1.00 91.47  ? 242 GLN   B N   1 
ATOM   4832 C CA  . GLN   B 1 242 ? 27.692 -34.262 18.078  1.00 90.34  ? 242 GLN   B CA  1 
ATOM   4833 C C   . GLN   B 1 242 ? 27.089 -33.961 16.699  1.00 93.36  ? 242 GLN   B C   1 
ATOM   4834 O O   . GLN   B 1 242 ? 26.304 -33.017 16.557  1.00 92.35  ? 242 GLN   B O   1 
ATOM   4835 C CB  . GLN   B 1 242 ? 28.215 -32.980 18.733  1.00 91.42  ? 242 GLN   B CB  1 
ATOM   4836 C CG  . GLN   B 1 242 ? 28.289 -33.018 20.255  1.00 104.14 ? 242 GLN   B CG  1 
ATOM   4837 C CD  . GLN   B 1 242 ? 28.752 -31.698 20.826  1.00 119.28 ? 242 GLN   B CD  1 
ATOM   4838 O OE1 . GLN   B 1 242 ? 28.116 -30.650 20.652  1.00 114.28 ? 242 GLN   B OE1 1 
ATOM   4839 N NE2 . GLN   B 1 242 ? 29.871 -31.724 21.528  1.00 110.04 ? 242 GLN   B NE2 1 
ATOM   4840 N N   . LYS   B 1 243 ? 27.467 -34.787 15.684  1.00 89.79  ? 243 LYS   B N   1 
ATOM   4841 C CA  . LYS   B 1 243 ? 27.054 -34.726 14.275  1.00 90.01  ? 243 LYS   B CA  1 
ATOM   4842 C C   . LYS   B 1 243 ? 27.574 -33.489 13.523  1.00 94.76  ? 243 LYS   B C   1 
ATOM   4843 O O   . LYS   B 1 243 ? 27.250 -33.292 12.351  1.00 94.08  ? 243 LYS   B O   1 
ATOM   4844 C CB  . LYS   B 1 243 ? 25.538 -34.928 14.109  1.00 92.86  ? 243 LYS   B CB  1 
ATOM   4845 N N   . ILE   B 1 244 ? 28.406 -32.681 14.205  1.00 92.29  ? 244 ILE   B N   1 
ATOM   4846 C CA  . ILE   B 1 244 ? 29.051 -31.450 13.727  1.00 91.96  ? 244 ILE   B CA  1 
ATOM   4847 C C   . ILE   B 1 244 ? 30.324 -31.858 12.942  1.00 94.11  ? 244 ILE   B C   1 
ATOM   4848 O O   . ILE   B 1 244 ? 30.721 -33.025 12.969  1.00 93.98  ? 244 ILE   B O   1 
ATOM   4849 C CB  . ILE   B 1 244 ? 29.406 -30.556 14.969  1.00 95.52  ? 244 ILE   B CB  1 
ATOM   4850 C CG1 . ILE   B 1 244 ? 28.210 -30.327 15.914  1.00 96.54  ? 244 ILE   B CG1 1 
ATOM   4851 C CG2 . ILE   B 1 244 ? 30.038 -29.224 14.585  1.00 96.72  ? 244 ILE   B CG2 1 
ATOM   4852 C CD1 . ILE   B 1 244 ? 28.637 -29.815 17.347  1.00 108.46 ? 244 ILE   B CD1 1 
ATOM   4853 N N   . TRP   B 1 245 ? 30.954 -30.890 12.252  1.00 88.82  ? 245 TRP   B N   1 
ATOM   4854 C CA  . TRP   B 1 245 ? 32.182 -31.062 11.476  1.00 87.26  ? 245 TRP   B CA  1 
ATOM   4855 C C   . TRP   B 1 245 ? 32.874 -29.719 11.198  1.00 89.75  ? 245 TRP   B C   1 
ATOM   4856 O O   . TRP   B 1 245 ? 32.271 -28.656 11.386  1.00 89.22  ? 245 TRP   B O   1 
ATOM   4857 C CB  . TRP   B 1 245 ? 31.884 -31.771 10.139  1.00 85.28  ? 245 TRP   B CB  1 
ATOM   4858 C CG  . TRP   B 1 245 ? 30.975 -31.020 9.209   1.00 85.78  ? 245 TRP   B CG  1 
ATOM   4859 C CD1 . TRP   B 1 245 ? 31.342 -30.137 8.238   1.00 88.62  ? 245 TRP   B CD1 1 
ATOM   4860 C CD2 . TRP   B 1 245 ? 29.549 -31.140 9.124   1.00 85.48  ? 245 TRP   B CD2 1 
ATOM   4861 N NE1 . TRP   B 1 245 ? 30.231 -29.680 7.566   1.00 87.95  ? 245 TRP   B NE1 1 
ATOM   4862 C CE2 . TRP   B 1 245 ? 29.117 -30.289 8.082   1.00 89.26  ? 245 TRP   B CE2 1 
ATOM   4863 C CE3 . TRP   B 1 245 ? 28.590 -31.887 9.826   1.00 86.65  ? 245 TRP   B CE3 1 
ATOM   4864 C CZ2 . TRP   B 1 245 ? 27.768 -30.158 7.733   1.00 88.55  ? 245 TRP   B CZ2 1 
ATOM   4865 C CZ3 . TRP   B 1 245 ? 27.253 -31.758 9.479   1.00 87.96  ? 245 TRP   B CZ3 1 
ATOM   4866 C CH2 . TRP   B 1 245 ? 26.854 -30.902 8.446   1.00 88.60  ? 245 TRP   B CH2 1 
ATOM   4867 N N   . TYR   B 1 246 ? 34.141 -29.786 10.744  1.00 84.66  ? 246 TYR   B N   1 
ATOM   4868 C CA  . TYR   B 1 246 ? 34.932 -28.638 10.320  1.00 83.39  ? 246 TYR   B CA  1 
ATOM   4869 C C   . TYR   B 1 246 ? 35.263 -28.871 8.852   1.00 83.69  ? 246 TYR   B C   1 
ATOM   4870 O O   . TYR   B 1 246 ? 35.653 -29.975 8.469   1.00 83.28  ? 246 TYR   B O   1 
ATOM   4871 C CB  . TYR   B 1 246 ? 36.210 -28.383 11.156  1.00 84.98  ? 246 TYR   B CB  1 
ATOM   4872 C CG  . TYR   B 1 246 ? 37.172 -27.449 10.439  1.00 87.36  ? 246 TYR   B CG  1 
ATOM   4873 C CD1 . TYR   B 1 246 ? 36.864 -26.101 10.259  1.00 89.21  ? 246 TYR   B CD1 1 
ATOM   4874 C CD2 . TYR   B 1 246 ? 38.339 -27.934 9.852   1.00 87.99  ? 246 TYR   B CD2 1 
ATOM   4875 C CE1 . TYR   B 1 246 ? 37.705 -25.257 9.535   1.00 89.38  ? 246 TYR   B CE1 1 
ATOM   4876 C CE2 . TYR   B 1 246 ? 39.192 -27.096 9.136   1.00 88.72  ? 246 TYR   B CE2 1 
ATOM   4877 C CZ  . TYR   B 1 246 ? 38.872 -25.757 8.983   1.00 94.87  ? 246 TYR   B CZ  1 
ATOM   4878 O OH  . TYR   B 1 246 ? 39.706 -24.931 8.272   1.00 94.07  ? 246 TYR   B OH  1 
ATOM   4879 N N   . GLU   B 1 247 ? 35.107 -27.837 8.037   1.00 78.21  ? 247 GLU   B N   1 
ATOM   4880 C CA  . GLU   B 1 247 ? 35.374 -27.928 6.618   1.00 77.51  ? 247 GLU   B CA  1 
ATOM   4881 C C   . GLU   B 1 247 ? 35.844 -26.581 6.085   1.00 80.70  ? 247 GLU   B C   1 
ATOM   4882 O O   . GLU   B 1 247 ? 35.193 -25.564 6.328   1.00 79.85  ? 247 GLU   B O   1 
ATOM   4883 C CB  . GLU   B 1 247 ? 34.098 -28.391 5.896   1.00 78.82  ? 247 GLU   B CB  1 
ATOM   4884 C CG  . GLU   B 1 247 ? 34.288 -28.853 4.463   1.00 88.40  ? 247 GLU   B CG  1 
ATOM   4885 C CD  . GLU   B 1 247 ? 32.973 -28.994 3.721   1.00 102.10 ? 247 GLU   B CD  1 
ATOM   4886 O OE1 . GLU   B 1 247 ? 32.706 -28.165 2.820   1.00 97.41  ? 247 GLU   B OE1 1 
ATOM   4887 O OE2 . GLU   B 1 247 ? 32.205 -29.928 4.051   1.00 84.38  ? 247 GLU   B OE2 1 
ATOM   4888 N N   . HIS   B 1 248 ? 36.983 -26.576 5.367   1.00 76.94  ? 248 HIS   B N   1 
ATOM   4889 C CA  . HIS   B 1 248 ? 37.527 -25.365 4.756   1.00 76.38  ? 248 HIS   B CA  1 
ATOM   4890 C C   . HIS   B 1 248 ? 36.886 -25.223 3.395   1.00 80.61  ? 248 HIS   B C   1 
ATOM   4891 O O   . HIS   B 1 248 ? 36.752 -26.210 2.673   1.00 81.24  ? 248 HIS   B O   1 
ATOM   4892 C CB  . HIS   B 1 248 ? 39.064 -25.411 4.626   1.00 76.99  ? 248 HIS   B CB  1 
ATOM   4893 C CG  . HIS   B 1 248 ? 39.596 -24.432 3.623   1.00 80.32  ? 248 HIS   B CG  1 
ATOM   4894 N ND1 . HIS   B 1 248 ? 39.762 -23.098 3.939   1.00 82.15  ? 248 HIS   B ND1 1 
ATOM   4895 C CD2 . HIS   B 1 248 ? 39.925 -24.615 2.322   1.00 82.05  ? 248 HIS   B CD2 1 
ATOM   4896 C CE1 . HIS   B 1 248 ? 40.199 -22.518 2.833   1.00 81.32  ? 248 HIS   B CE1 1 
ATOM   4897 N NE2 . HIS   B 1 248 ? 40.315 -23.388 1.836   1.00 81.74  ? 248 HIS   B NE2 1 
ATOM   4898 N N   . ARG   B 1 249 ? 36.490 -24.006 3.042   1.00 76.85  ? 249 ARG   B N   1 
ATOM   4899 C CA  . ARG   B 1 249 ? 35.882 -23.724 1.754   1.00 76.97  ? 249 ARG   B CA  1 
ATOM   4900 C C   . ARG   B 1 249 ? 36.466 -22.438 1.231   1.00 81.64  ? 249 ARG   B C   1 
ATOM   4901 O O   . ARG   B 1 249 ? 36.835 -21.572 2.019   1.00 80.81  ? 249 ARG   B O   1 
ATOM   4902 C CB  . ARG   B 1 249 ? 34.353 -23.611 1.874   1.00 78.36  ? 249 ARG   B CB  1 
ATOM   4903 C CG  . ARG   B 1 249 ? 33.597 -24.935 1.719   1.00 90.09  ? 249 ARG   B CG  1 
ATOM   4904 C CD  . ARG   B 1 249 ? 32.105 -24.687 1.579   1.00 103.02 ? 249 ARG   B CD  1 
ATOM   4905 N NE  . ARG   B 1 249 ? 31.343 -25.928 1.424   1.00 117.09 ? 249 ARG   B NE  1 
ATOM   4906 C CZ  . ARG   B 1 249 ? 30.118 -26.125 1.905   1.00 133.70 ? 249 ARG   B CZ  1 
ATOM   4907 N NH1 . ARG   B 1 249 ? 29.501 -25.166 2.587   1.00 119.02 ? 249 ARG   B NH1 1 
ATOM   4908 N NH2 . ARG   B 1 249 ? 29.503 -27.285 1.716   1.00 121.61 ? 249 ARG   B NH2 1 
ATOM   4909 N N   . LEU   B 1 250 ? 36.570 -22.309 -0.092  1.00 79.62  ? 250 LEU   B N   1 
ATOM   4910 C CA  . LEU   B 1 250 ? 37.096 -21.089 -0.692  1.00 79.95  ? 250 LEU   B CA  1 
ATOM   4911 C C   . LEU   B 1 250 ? 35.968 -20.068 -0.706  1.00 83.83  ? 250 LEU   B C   1 
ATOM   4912 O O   . LEU   B 1 250 ? 34.796 -20.460 -0.759  1.00 82.88  ? 250 LEU   B O   1 
ATOM   4913 C CB  . LEU   B 1 250 ? 37.619 -21.351 -2.108  1.00 80.35  ? 250 LEU   B CB  1 
ATOM   4914 C CG  . LEU   B 1 250 ? 38.721 -20.406 -2.557  1.00 85.76  ? 250 LEU   B CG  1 
ATOM   4915 C CD1 . LEU   B 1 250 ? 40.086 -21.089 -2.505  1.00 85.93  ? 250 LEU   B CD1 1 
ATOM   4916 C CD2 . LEU   B 1 250 ? 38.409 -19.798 -3.926  1.00 88.34  ? 250 LEU   B CD2 1 
ATOM   4917 N N   . ILE   B 1 251 ? 36.321 -18.768 -0.643  1.00 80.85  ? 251 ILE   B N   1 
ATOM   4918 C CA  . ILE   B 1 251 ? 35.373 -17.649 -0.616  1.00 81.11  ? 251 ILE   B CA  1 
ATOM   4919 C C   . ILE   B 1 251 ? 34.150 -17.791 -1.520  1.00 87.63  ? 251 ILE   B C   1 
ATOM   4920 O O   . ILE   B 1 251 ? 33.022 -17.684 -1.041  1.00 87.63  ? 251 ILE   B O   1 
ATOM   4921 C CB  . ILE   B 1 251 ? 36.055 -16.241 -0.671  1.00 83.90  ? 251 ILE   B CB  1 
ATOM   4922 C CG1 . ILE   B 1 251 ? 35.037 -15.075 -0.526  1.00 83.97  ? 251 ILE   B CG1 1 
ATOM   4923 C CG2 . ILE   B 1 251 ? 36.938 -16.061 -1.911  1.00 84.19  ? 251 ILE   B CG2 1 
ATOM   4924 C CD1 . ILE   B 1 251 ? 34.320 -14.966 0.823   1.00 87.79  ? 251 ILE   B CD1 1 
ATOM   4925 N N   . ASP   B 1 252 ? 34.379 -18.062 -2.805  1.00 86.14  ? 252 ASP   B N   1 
ATOM   4926 C CA  . ASP   B 1 252 ? 33.339 -18.203 -3.820  1.00 86.63  ? 252 ASP   B CA  1 
ATOM   4927 C C   . ASP   B 1 252 ? 32.471 -19.450 -3.668  1.00 91.14  ? 252 ASP   B C   1 
ATOM   4928 O O   . ASP   B 1 252 ? 31.262 -19.358 -3.883  1.00 90.50  ? 252 ASP   B O   1 
ATOM   4929 C CB  . ASP   B 1 252 ? 33.932 -18.027 -5.224  1.00 88.71  ? 252 ASP   B CB  1 
ATOM   4930 C CG  . ASP   B 1 252 ? 34.775 -16.765 -5.319  1.00 101.66 ? 252 ASP   B CG  1 
ATOM   4931 O OD1 . ASP   B 1 252 ? 34.215 -15.654 -5.118  1.00 101.66 ? 252 ASP   B OD1 1 
ATOM   4932 O OD2 . ASP   B 1 252 ? 35.999 -16.885 -5.569  1.00 109.07 ? 252 ASP   B OD2 1 
ATOM   4933 N N   . ASP   B 1 253 ? 33.068 -20.596 -3.261  1.00 88.51  ? 253 ASP   B N   1 
ATOM   4934 C CA  . ASP   B 1 253 ? 32.337 -21.848 -3.026  1.00 88.65  ? 253 ASP   B CA  1 
ATOM   4935 C C   . ASP   B 1 253 ? 31.525 -21.742 -1.721  1.00 92.08  ? 253 ASP   B C   1 
ATOM   4936 O O   . ASP   B 1 253 ? 30.496 -22.413 -1.591  1.00 92.78  ? 253 ASP   B O   1 
ATOM   4937 C CB  . ASP   B 1 253 ? 33.293 -23.064 -2.980  1.00 91.08  ? 253 ASP   B CB  1 
ATOM   4938 C CG  . ASP   B 1 253 ? 32.604 -24.424 -2.858  1.00 105.67 ? 253 ASP   B CG  1 
ATOM   4939 O OD1 . ASP   B 1 253 ? 31.856 -24.804 -3.794  1.00 106.97 ? 253 ASP   B OD1 1 
ATOM   4940 O OD2 . ASP   B 1 253 ? 32.817 -25.110 -1.831  1.00 112.17 ? 253 ASP   B OD2 1 
ATOM   4941 N N   . MET   B 1 254 ? 31.986 -20.891 -0.766  1.00 86.33  ? 254 MET   B N   1 
ATOM   4942 C CA  . MET   B 1 254 ? 31.347 -20.651 0.535   1.00 84.65  ? 254 MET   B CA  1 
ATOM   4943 C C   . MET   B 1 254 ? 30.092 -19.780 0.405   1.00 85.33  ? 254 MET   B C   1 
ATOM   4944 O O   . MET   B 1 254 ? 29.030 -20.165 0.904   1.00 83.83  ? 254 MET   B O   1 
ATOM   4945 C CB  . MET   B 1 254 ? 32.349 -20.019 1.520   1.00 86.74  ? 254 MET   B CB  1 
ATOM   4946 C CG  . MET   B 1 254 ? 31.758 -19.711 2.871   1.00 89.93  ? 254 MET   B CG  1 
ATOM   4947 S SD  . MET   B 1 254 ? 31.509 -21.173 3.885   1.00 94.01  ? 254 MET   B SD  1 
ATOM   4948 C CE  . MET   B 1 254 ? 33.116 -21.318 4.560   1.00 90.98  ? 254 MET   B CE  1 
ATOM   4949 N N   . VAL   B 1 255 ? 30.226 -18.605 -0.249  1.00 80.73  ? 255 VAL   B N   1 
ATOM   4950 C CA  . VAL   B 1 255 ? 29.138 -17.650 -0.472  1.00 80.86  ? 255 VAL   B CA  1 
ATOM   4951 C C   . VAL   B 1 255 ? 28.006 -18.324 -1.283  1.00 86.40  ? 255 VAL   B C   1 
ATOM   4952 O O   . VAL   B 1 255 ? 26.825 -18.054 -1.027  1.00 86.00  ? 255 VAL   B O   1 
ATOM   4953 C CB  . VAL   B 1 255 ? 29.659 -16.313 -1.081  1.00 84.64  ? 255 VAL   B CB  1 
ATOM   4954 C CG1 . VAL   B 1 255 ? 28.521 -15.408 -1.558  1.00 84.37  ? 255 VAL   B CG1 1 
ATOM   4955 C CG2 . VAL   B 1 255 ? 30.542 -15.565 -0.083  1.00 84.43  ? 255 VAL   B CG2 1 
ATOM   4956 N N   . ALA   B 1 256 ? 28.379 -19.242 -2.214  1.00 83.52  ? 256 ALA   B N   1 
ATOM   4957 C CA  . ALA   B 1 256 ? 27.447 -20.006 -3.046  1.00 83.49  ? 256 ALA   B CA  1 
ATOM   4958 C C   . ALA   B 1 256 ? 26.619 -20.991 -2.203  1.00 88.40  ? 256 ALA   B C   1 
ATOM   4959 O O   . ALA   B 1 256 ? 25.385 -20.939 -2.253  1.00 87.91  ? 256 ALA   B O   1 
ATOM   4960 C CB  . ALA   B 1 256 ? 28.204 -20.751 -4.135  1.00 84.13  ? 256 ALA   B CB  1 
ATOM   4961 N N   . GLN   B 1 257 ? 27.300 -21.871 -1.421  1.00 85.57  ? 257 GLN   B N   1 
ATOM   4962 C CA  . GLN   B 1 257 ? 26.677 -22.887 -0.557  1.00 85.67  ? 257 GLN   B CA  1 
ATOM   4963 C C   . GLN   B 1 257 ? 25.804 -22.299 0.561   1.00 89.11  ? 257 GLN   B C   1 
ATOM   4964 O O   . GLN   B 1 257 ? 24.822 -22.934 0.952   1.00 89.17  ? 257 GLN   B O   1 
ATOM   4965 C CB  . GLN   B 1 257 ? 27.725 -23.862 0.024   1.00 87.30  ? 257 GLN   B CB  1 
ATOM   4966 C CG  . GLN   B 1 257 ? 28.346 -24.845 -0.991  1.00 106.58 ? 257 GLN   B CG  1 
ATOM   4967 C CD  . GLN   B 1 257 ? 27.459 -26.018 -1.365  1.00 118.00 ? 257 GLN   B CD  1 
ATOM   4968 O OE1 . GLN   B 1 257 ? 26.865 -26.058 -2.452  1.00 111.21 ? 257 GLN   B OE1 1 
ATOM   4969 N NE2 . GLN   B 1 257 ? 27.358 -27.005 -0.482  1.00 105.71 ? 257 GLN   B NE2 1 
ATOM   4970 N N   . ALA   B 1 258 ? 26.161 -21.103 1.070   1.00 84.34  ? 258 ALA   B N   1 
ATOM   4971 C CA  . ALA   B 1 258 ? 25.428 -20.410 2.130   1.00 83.50  ? 258 ALA   B CA  1 
ATOM   4972 C C   . ALA   B 1 258 ? 24.137 -19.777 1.592   1.00 86.24  ? 258 ALA   B C   1 
ATOM   4973 O O   . ALA   B 1 258 ? 23.151 -19.670 2.329   1.00 85.21  ? 258 ALA   B O   1 
ATOM   4974 C CB  . ALA   B 1 258 ? 26.309 -19.347 2.765   1.00 84.21  ? 258 ALA   B CB  1 
ATOM   4975 N N   . MET   B 1 259 ? 24.149 -19.368 0.304   1.00 82.30  ? 259 MET   B N   1 
ATOM   4976 C CA  . MET   B 1 259 ? 23.011 -18.759 -0.388  1.00 81.83  ? 259 MET   B CA  1 
ATOM   4977 C C   . MET   B 1 259 ? 21.887 -19.761 -0.638  1.00 84.91  ? 259 MET   B C   1 
ATOM   4978 O O   . MET   B 1 259 ? 20.732 -19.359 -0.783  1.00 84.88  ? 259 MET   B O   1 
ATOM   4979 C CB  . MET   B 1 259 ? 23.466 -18.136 -1.708  1.00 84.19  ? 259 MET   B CB  1 
ATOM   4980 C CG  . MET   B 1 259 ? 23.146 -16.674 -1.806  1.00 87.96  ? 259 MET   B CG  1 
ATOM   4981 S SD  . MET   B 1 259 ? 24.033 -15.686 -0.581  1.00 92.19  ? 259 MET   B SD  1 
ATOM   4982 C CE  . MET   B 1 259 ? 23.374 -14.071 -0.945  1.00 89.02  ? 259 MET   B CE  1 
ATOM   4983 N N   . LYS   B 1 260 ? 22.232 -21.060 -0.682  1.00 80.40  ? 260 LYS   B N   1 
ATOM   4984 C CA  . LYS   B 1 260 ? 21.327 -22.189 -0.893  1.00 79.85  ? 260 LYS   B CA  1 
ATOM   4985 C C   . LYS   B 1 260 ? 20.974 -22.881 0.434   1.00 83.32  ? 260 LYS   B C   1 
ATOM   4986 O O   . LYS   B 1 260 ? 20.022 -23.672 0.482   1.00 84.07  ? 260 LYS   B O   1 
ATOM   4987 C CB  . LYS   B 1 260 ? 21.979 -23.206 -1.852  1.00 82.20  ? 260 LYS   B CB  1 
ATOM   4988 N N   . SER   B 1 261 ? 21.744 -22.581 1.501   1.00 78.01  ? 261 SER   B N   1 
ATOM   4989 C CA  . SER   B 1 261 ? 21.611 -23.145 2.850   1.00 76.84  ? 261 SER   B CA  1 
ATOM   4990 C C   . SER   B 1 261 ? 20.407 -22.655 3.654   1.00 78.12  ? 261 SER   B C   1 
ATOM   4991 O O   . SER   B 1 261 ? 19.746 -21.684 3.276   1.00 77.14  ? 261 SER   B O   1 
ATOM   4992 C CB  . SER   B 1 261 ? 22.891 -22.905 3.651   1.00 80.00  ? 261 SER   B CB  1 
ATOM   4993 O OG  . SER   B 1 261 ? 22.834 -23.509 4.934   1.00 87.31  ? 261 SER   B OG  1 
ATOM   4994 N N   . GLU   B 1 262 ? 20.150 -23.350 4.783   1.00 73.23  ? 262 GLU   B N   1 
ATOM   4995 C CA  . GLU   B 1 262 ? 19.102 -23.064 5.760   1.00 72.66  ? 262 GLU   B CA  1 
ATOM   4996 C C   . GLU   B 1 262 ? 19.720 -22.295 6.966   1.00 76.42  ? 262 GLU   B C   1 
ATOM   4997 O O   . GLU   B 1 262 ? 18.996 -21.915 7.899   1.00 76.18  ? 262 GLU   B O   1 
ATOM   4998 C CB  . GLU   B 1 262 ? 18.457 -24.379 6.236   1.00 73.80  ? 262 GLU   B CB  1 
ATOM   4999 N N   . GLY   B 1 263 ? 21.049 -22.089 6.915   1.00 71.05  ? 263 GLY   B N   1 
ATOM   5000 C CA  . GLY   B 1 263 ? 21.840 -21.427 7.948   1.00 69.65  ? 263 GLY   B CA  1 
ATOM   5001 C C   . GLY   B 1 263 ? 22.300 -22.423 8.994   1.00 71.29  ? 263 GLY   B C   1 
ATOM   5002 O O   . GLY   B 1 263 ? 22.556 -23.587 8.670   1.00 72.17  ? 263 GLY   B O   1 
ATOM   5003 N N   . GLY   B 1 264 ? 22.399 -21.976 10.242  1.00 64.69  ? 264 GLY   B N   1 
ATOM   5004 C CA  . GLY   B 1 264 ? 22.803 -22.826 11.357  1.00 63.50  ? 264 GLY   B CA  1 
ATOM   5005 C C   . GLY   B 1 264 ? 24.234 -23.308 11.305  1.00 65.85  ? 264 GLY   B C   1 
ATOM   5006 O O   . GLY   B 1 264 ? 24.487 -24.498 11.507  1.00 64.94  ? 264 GLY   B O   1 
ATOM   5007 N N   . PHE   B 1 265 ? 25.185 -22.382 11.027  1.00 60.57  ? 265 PHE   B N   1 
ATOM   5008 C CA  . PHE   B 1 265 ? 26.613 -22.704 10.961  1.00 58.60  ? 265 PHE   B CA  1 
ATOM   5009 C C   . PHE   B 1 265 ? 27.532 -21.566 11.414  1.00 59.93  ? 265 PHE   B C   1 
ATOM   5010 O O   . PHE   B 1 265 ? 27.149 -20.395 11.352  1.00 58.32  ? 265 PHE   B O   1 
ATOM   5011 C CB  . PHE   B 1 265 ? 27.012 -23.202 9.555   1.00 59.22  ? 265 PHE   B CB  1 
ATOM   5012 C CG  . PHE   B 1 265 ? 26.803 -22.219 8.425   1.00 59.35  ? 265 PHE   B CG  1 
ATOM   5013 C CD1 . PHE   B 1 265 ? 27.793 -21.299 8.087   1.00 61.04  ? 265 PHE   B CD1 1 
ATOM   5014 C CD2 . PHE   B 1 265 ? 25.635 -22.242 7.669   1.00 60.21  ? 265 PHE   B CD2 1 
ATOM   5015 C CE1 . PHE   B 1 265 ? 27.605 -20.403 7.032   1.00 61.60  ? 265 PHE   B CE1 1 
ATOM   5016 C CE2 . PHE   B 1 265 ? 25.449 -21.347 6.611   1.00 62.44  ? 265 PHE   B CE2 1 
ATOM   5017 C CZ  . PHE   B 1 265 ? 26.433 -20.431 6.302   1.00 60.56  ? 265 PHE   B CZ  1 
ATOM   5018 N N   . ILE   B 1 266 ? 28.757 -21.928 11.848  1.00 55.05  ? 266 ILE   B N   1 
ATOM   5019 C CA  . ILE   B 1 266 ? 29.779 -20.975 12.258  1.00 53.95  ? 266 ILE   B CA  1 
ATOM   5020 C C   . ILE   B 1 266 ? 30.675 -20.728 11.050  1.00 59.22  ? 266 ILE   B C   1 
ATOM   5021 O O   . ILE   B 1 266 ? 31.215 -21.668 10.452  1.00 58.15  ? 266 ILE   B O   1 
ATOM   5022 C CB  . ILE   B 1 266 ? 30.565 -21.395 13.515  1.00 56.27  ? 266 ILE   B CB  1 
ATOM   5023 C CG1 . ILE   B 1 266 ? 29.666 -22.079 14.583  1.00 56.62  ? 266 ILE   B CG1 1 
ATOM   5024 C CG2 . ILE   B 1 266 ? 31.370 -20.214 14.086  1.00 56.30  ? 266 ILE   B CG2 1 
ATOM   5025 C CD1 . ILE   B 1 266 ? 28.492 -21.260 15.228  1.00 57.65  ? 266 ILE   B CD1 1 
ATOM   5026 N N   . TRP   B 1 267 ? 30.801 -19.458 10.679  1.00 56.69  ? 267 TRP   B N   1 
ATOM   5027 C CA  . TRP   B 1 267 ? 31.585 -19.039 9.535   1.00 57.05  ? 267 TRP   B CA  1 
ATOM   5028 C C   . TRP   B 1 267 ? 32.799 -18.187 9.944   1.00 60.66  ? 267 TRP   B C   1 
ATOM   5029 O O   . TRP   B 1 267 ? 32.654 -16.994 10.207  1.00 59.02  ? 267 TRP   B O   1 
ATOM   5030 C CB  . TRP   B 1 267 ? 30.651 -18.302 8.573   1.00 56.43  ? 267 TRP   B CB  1 
ATOM   5031 C CG  . TRP   B 1 267 ? 31.229 -17.898 7.249   1.00 58.17  ? 267 TRP   B CG  1 
ATOM   5032 C CD1 . TRP   B 1 267 ? 32.500 -18.104 6.796   1.00 61.12  ? 267 TRP   B CD1 1 
ATOM   5033 C CD2 . TRP   B 1 267 ? 30.534 -17.220 6.198   1.00 58.35  ? 267 TRP   B CD2 1 
ATOM   5034 N NE1 . TRP   B 1 267 ? 32.645 -17.572 5.540   1.00 60.71  ? 267 TRP   B NE1 1 
ATOM   5035 C CE2 . TRP   B 1 267 ? 31.452 -17.027 5.143   1.00 62.20  ? 267 TRP   B CE2 1 
ATOM   5036 C CE3 . TRP   B 1 267 ? 29.221 -16.745 6.047   1.00 59.90  ? 267 TRP   B CE3 1 
ATOM   5037 C CZ2 . TRP   B 1 267 ? 31.100 -16.385 3.950   1.00 61.52  ? 267 TRP   B CZ2 1 
ATOM   5038 C CZ3 . TRP   B 1 267 ? 28.874 -16.114 4.863   1.00 61.69  ? 267 TRP   B CZ3 1 
ATOM   5039 C CH2 . TRP   B 1 267 ? 29.808 -15.945 3.828   1.00 62.22  ? 267 TRP   B CH2 1 
ATOM   5040 N N   . ALA   B 1 268 ? 33.998 -18.812 9.991   1.00 59.21  ? 268 ALA   B N   1 
ATOM   5041 C CA  . ALA   B 1 268 ? 35.267 -18.147 10.330  1.00 59.49  ? 268 ALA   B CA  1 
ATOM   5042 C C   . ALA   B 1 268 ? 35.803 -17.478 9.072   1.00 66.75  ? 268 ALA   B C   1 
ATOM   5043 O O   . ALA   B 1 268 ? 36.044 -18.149 8.074   1.00 65.17  ? 268 ALA   B O   1 
ATOM   5044 C CB  . ALA   B 1 268 ? 36.272 -19.150 10.873  1.00 59.76  ? 268 ALA   B CB  1 
ATOM   5045 N N   . CYS   B 1 269 ? 35.942 -16.147 9.120   1.00 68.05  ? 269 CYS   B N   1 
ATOM   5046 C CA  . CYS   B 1 269 ? 36.390 -15.273 8.036   1.00 70.01  ? 269 CYS   B CA  1 
ATOM   5047 C C   . CYS   B 1 269 ? 37.818 -14.773 8.189   1.00 75.40  ? 269 CYS   B C   1 
ATOM   5048 O O   . CYS   B 1 269 ? 38.178 -14.182 9.212   1.00 74.50  ? 269 CYS   B O   1 
ATOM   5049 C CB  . CYS   B 1 269 ? 35.429 -14.095 7.885   1.00 71.59  ? 269 CYS   B CB  1 
ATOM   5050 S SG  . CYS   B 1 269 ? 34.326 -14.199 6.455   1.00 76.49  ? 269 CYS   B SG  1 
ATOM   5051 N N   . LYS   B 1 270 ? 38.614 -14.963 7.139   1.00 73.73  ? 270 LYS   B N   1 
ATOM   5052 C CA  . LYS   B 1 270 ? 39.978 -14.459 7.034   1.00 73.94  ? 270 LYS   B CA  1 
ATOM   5053 C C   . LYS   B 1 270 ? 39.937 -13.535 5.800   1.00 78.94  ? 270 LYS   B C   1 
ATOM   5054 O O   . LYS   B 1 270 ? 39.741 -14.019 4.676   1.00 78.54  ? 270 LYS   B O   1 
ATOM   5055 C CB  . LYS   B 1 270 ? 41.010 -15.608 6.896   1.00 76.03  ? 270 LYS   B CB  1 
ATOM   5056 C CG  . LYS   B 1 270 ? 42.409 -15.208 6.376   1.00 85.34  ? 270 LYS   B CG  1 
ATOM   5057 C CD  . LYS   B 1 270 ? 43.077 -14.021 7.111   1.00 90.06  ? 270 LYS   B CD  1 
ATOM   5058 C CE  . LYS   B 1 270 ? 44.396 -13.617 6.487   1.00 96.87  ? 270 LYS   B CE  1 
ATOM   5059 N NZ  . LYS   B 1 270 ? 44.248 -13.091 5.100   1.00 104.08 ? 270 LYS   B NZ  1 
ATOM   5060 N N   . ASN   B 1 271 ? 40.067 -12.208 6.020   1.00 76.21  ? 271 ASN   B N   1 
ATOM   5061 C CA  . ASN   B 1 271 ? 40.029 -11.215 4.931   1.00 100.33 ? 271 ASN   B CA  1 
ATOM   5062 C C   . ASN   B 1 271 ? 41.151 -10.171 5.003   1.00 121.18 ? 271 ASN   B C   1 
ATOM   5063 O O   . ASN   B 1 271 ? 41.998 -10.111 4.108   1.00 79.44  ? 271 ASN   B O   1 
ATOM   5064 C CB  . ASN   B 1 271 ? 38.636 -10.557 4.803   1.00 98.57  ? 271 ASN   B CB  1 
ATOM   5065 C CG  . ASN   B 1 271 ? 38.121 -9.840  6.036   1.00 117.23 ? 271 ASN   B CG  1 
ATOM   5066 O OD1 . ASN   B 1 271 ? 38.354 -10.248 7.182   1.00 114.10 ? 271 ASN   B OD1 1 
ATOM   5067 N ND2 . ASN   B 1 271 ? 37.388 -8.756  5.825   1.00 105.09 ? 271 ASN   B ND2 1 
ATOM   5068 N N   . SER   B 1 287 ? 15.222 -4.666  11.647  1.00 74.82  ? 287 SER   B N   1 
ATOM   5069 C CA  . SER   B 1 287 ? 16.649 -4.932  11.487  1.00 74.75  ? 287 SER   B CA  1 
ATOM   5070 C C   . SER   B 1 287 ? 17.496 -4.096  12.444  1.00 77.01  ? 287 SER   B C   1 
ATOM   5071 O O   . SER   B 1 287 ? 16.941 -3.292  13.205  1.00 77.57  ? 287 SER   B O   1 
ATOM   5072 C CB  . SER   B 1 287 ? 17.089 -4.709  10.042  1.00 78.92  ? 287 SER   B CB  1 
ATOM   5073 O OG  . SER   B 1 287 ? 16.641 -5.758  9.200   1.00 88.27  ? 287 SER   B OG  1 
ATOM   5074 N N   . LEU   B 1 288 ? 18.840 -4.307  12.410  1.00 70.19  ? 288 LEU   B N   1 
ATOM   5075 C CA  . LEU   B 1 288 ? 19.882 -3.659  13.235  1.00 68.53  ? 288 LEU   B CA  1 
ATOM   5076 C C   . LEU   B 1 288 ? 19.780 -3.950  14.746  1.00 67.02  ? 288 LEU   B C   1 
ATOM   5077 O O   . LEU   B 1 288 ? 20.793 -4.286  15.374  1.00 65.61  ? 288 LEU   B O   1 
ATOM   5078 C CB  . LEU   B 1 288 ? 20.132 -2.172  12.897  1.00 68.61  ? 288 LEU   B CB  1 
ATOM   5079 C CG  . LEU   B 1 288 ? 21.561 -1.621  13.175  1.00 73.51  ? 288 LEU   B CG  1 
ATOM   5080 C CD1 . LEU   B 1 288 ? 22.673 -2.591  12.718  1.00 73.53  ? 288 LEU   B CD1 1 
ATOM   5081 C CD2 . LEU   B 1 288 ? 21.760 -0.252  12.536  1.00 74.85  ? 288 LEU   B CD2 1 
ATOM   5082 N N   . GLY   B 1 289 ? 18.558 -3.874  15.284  1.00 59.28  ? 289 GLY   B N   1 
ATOM   5083 C CA  . GLY   B 1 289 ? 18.265 -4.185  16.674  1.00 57.98  ? 289 GLY   B CA  1 
ATOM   5084 C C   . GLY   B 1 289 ? 18.090 -5.683  16.864  1.00 58.98  ? 289 GLY   B C   1 
ATOM   5085 O O   . GLY   B 1 289 ? 17.664 -6.134  17.935  1.00 58.15  ? 289 GLY   B O   1 
ATOM   5086 N N   . MET   B 1 290 ? 18.455 -6.460  15.810  1.00 52.79  ? 290 MET   B N   1 
ATOM   5087 C CA  . MET   B 1 290 ? 18.362 -7.916  15.700  1.00 51.26  ? 290 MET   B CA  1 
ATOM   5088 C C   . MET   B 1 290 ? 19.712 -8.624  15.578  1.00 54.91  ? 290 MET   B C   1 
ATOM   5089 O O   . MET   B 1 290 ? 19.761 -9.795  15.185  1.00 53.78  ? 290 MET   B O   1 
ATOM   5090 C CB  . MET   B 1 290 ? 17.441 -8.291  14.523  1.00 52.82  ? 290 MET   B CB  1 
ATOM   5091 C CG  . MET   B 1 290 ? 16.047 -7.768  14.694  1.00 55.61  ? 290 MET   B CG  1 
ATOM   5092 S SD  . MET   B 1 290 ? 15.253 -8.703  15.988  1.00 59.53  ? 290 MET   B SD  1 
ATOM   5093 C CE  . MET   B 1 290 ? 14.319 -7.647  16.528  1.00 56.55  ? 290 MET   B CE  1 
ATOM   5094 N N   . MET   B 1 291 ? 20.804 -7.930  15.919  1.00 51.57  ? 291 MET   B N   1 
ATOM   5095 C CA  . MET   B 1 291 ? 22.117 -8.558  15.868  1.00 51.22  ? 291 MET   B CA  1 
ATOM   5096 C C   . MET   B 1 291 ? 22.975 -8.348  17.108  1.00 49.48  ? 291 MET   B C   1 
ATOM   5097 O O   . MET   B 1 291 ? 23.097 -7.235  17.613  1.00 46.94  ? 291 MET   B O   1 
ATOM   5098 C CB  . MET   B 1 291 ? 22.881 -8.206  14.598  1.00 54.55  ? 291 MET   B CB  1 
ATOM   5099 C CG  . MET   B 1 291 ? 23.972 -9.227  14.299  1.00 60.28  ? 291 MET   B CG  1 
ATOM   5100 S SD  . MET   B 1 291 ? 24.719 -9.079  12.676  1.00 66.00  ? 291 MET   B SD  1 
ATOM   5101 C CE  . MET   B 1 291 ? 23.298 -9.481  11.668  1.00 62.59  ? 291 MET   B CE  1 
ATOM   5102 N N   . THR   B 1 292 ? 23.581 -9.433  17.571  1.00 45.28  ? 292 THR   B N   1 
ATOM   5103 C CA  . THR   B 1 292 ? 24.478 -9.433  18.718  1.00 45.77  ? 292 THR   B CA  1 
ATOM   5104 C C   . THR   B 1 292 ? 25.914 -9.622  18.264  1.00 47.55  ? 292 THR   B C   1 
ATOM   5105 O O   . THR   B 1 292 ? 26.168 -10.061 17.144  1.00 46.03  ? 292 THR   B O   1 
ATOM   5106 C CB  . THR   B 1 292 ? 24.056 -10.447 19.779  1.00 60.81  ? 292 THR   B CB  1 
ATOM   5107 O OG1 . THR   B 1 292 ? 24.330 -11.769 19.310  1.00 67.92  ? 292 THR   B OG1 1 
ATOM   5108 C CG2 . THR   B 1 292 ? 22.608 -10.295 20.171  1.00 58.19  ? 292 THR   B CG2 1 
ATOM   5109 N N   . SER   B 1 293 ? 26.841 -9.257  19.135  1.00 43.93  ? 293 SER   B N   1 
ATOM   5110 C CA  . SER   B 1 293 ? 28.264 -9.341  18.894  1.00 44.73  ? 293 SER   B CA  1 
ATOM   5111 C C   . SER   B 1 293 ? 28.832 -9.940  20.165  1.00 51.48  ? 293 SER   B C   1 
ATOM   5112 O O   . SER   B 1 293 ? 28.519 -9.458  21.252  1.00 55.17  ? 293 SER   B O   1 
ATOM   5113 C CB  . SER   B 1 293 ? 28.811 -7.944  18.625  1.00 49.54  ? 293 SER   B CB  1 
ATOM   5114 O OG  . SER   B 1 293 ? 30.220 -7.922  18.502  1.00 62.70  ? 293 SER   B OG  1 
ATOM   5115 N N   . VAL   B 1 294 ? 29.587 -11.038 20.061  1.00 45.63  ? 294 VAL   B N   1 
ATOM   5116 C CA  . VAL   B 1 294 ? 30.137 -11.683 21.260  1.00 44.50  ? 294 VAL   B CA  1 
ATOM   5117 C C   . VAL   B 1 294 ? 31.657 -11.869 21.121  1.00 47.06  ? 294 VAL   B C   1 
ATOM   5118 O O   . VAL   B 1 294 ? 32.123 -12.456 20.140  1.00 47.40  ? 294 VAL   B O   1 
ATOM   5119 C CB  . VAL   B 1 294 ? 29.397 -13.000 21.665  1.00 48.21  ? 294 VAL   B CB  1 
ATOM   5120 C CG1 . VAL   B 1 294 ? 29.812 -13.457 23.051  1.00 48.33  ? 294 VAL   B CG1 1 
ATOM   5121 C CG2 . VAL   B 1 294 ? 27.883 -12.835 21.624  1.00 48.08  ? 294 VAL   B CG2 1 
ATOM   5122 N N   . LEU   B 1 295 ? 32.419 -11.333 22.081  1.00 41.84  ? 295 LEU   B N   1 
ATOM   5123 C CA  . LEU   B 1 295 ? 33.862 -11.471 22.094  1.00 41.77  ? 295 LEU   B CA  1 
ATOM   5124 C C   . LEU   B 1 295 ? 34.122 -12.794 22.823  1.00 47.69  ? 295 LEU   B C   1 
ATOM   5125 O O   . LEU   B 1 295 ? 33.755 -12.961 23.989  1.00 47.60  ? 295 LEU   B O   1 
ATOM   5126 C CB  . LEU   B 1 295 ? 34.568 -10.274 22.775  1.00 41.18  ? 295 LEU   B CB  1 
ATOM   5127 C CG  . LEU   B 1 295 ? 36.118 -10.287 22.795  1.00 45.72  ? 295 LEU   B CG  1 
ATOM   5128 C CD1 . LEU   B 1 295 ? 36.708 -10.116 21.405  1.00 45.97  ? 295 LEU   B CD1 1 
ATOM   5129 C CD2 . LEU   B 1 295 ? 36.682 -9.186  23.694  1.00 46.35  ? 295 LEU   B CD2 1 
ATOM   5130 N N   . VAL   B 1 296 ? 34.690 -13.752 22.102  1.00 45.05  ? 296 VAL   B N   1 
ATOM   5131 C CA  . VAL   B 1 296 ? 34.990 -15.073 22.644  1.00 45.33  ? 296 VAL   B CA  1 
ATOM   5132 C C   . VAL   B 1 296 ? 36.513 -15.156 22.781  1.00 50.69  ? 296 VAL   B C   1 
ATOM   5133 O O   . VAL   B 1 296 ? 37.244 -15.049 21.793  1.00 49.78  ? 296 VAL   B O   1 
ATOM   5134 C CB  . VAL   B 1 296 ? 34.350 -16.199 21.767  1.00 48.97  ? 296 VAL   B CB  1 
ATOM   5135 C CG1 . VAL   B 1 296 ? 34.719 -17.587 22.274  1.00 48.73  ? 296 VAL   B CG1 1 
ATOM   5136 C CG2 . VAL   B 1 296 ? 32.829 -16.046 21.711  1.00 48.42  ? 296 VAL   B CG2 1 
ATOM   5137 N N   . CYS   B 1 297 ? 36.987 -15.261 24.012  1.00 49.43  ? 297 CYS   B N   1 
ATOM   5138 C CA  . CYS   B 1 297 ? 38.418 -15.355 24.267  1.00 50.83  ? 297 CYS   B CA  1 
ATOM   5139 C C   . CYS   B 1 297 ? 38.883 -16.813 23.977  1.00 58.04  ? 297 CYS   B C   1 
ATOM   5140 O O   . CYS   B 1 297 ? 38.090 -17.750 24.156  1.00 57.22  ? 297 CYS   B O   1 
ATOM   5141 C CB  . CYS   B 1 297 ? 38.742 -14.894 25.687  1.00 51.37  ? 297 CYS   B CB  1 
ATOM   5142 S SG  . CYS   B 1 297 ? 38.321 -13.153 25.998  1.00 55.63  ? 297 CYS   B SG  1 
ATOM   5143 N N   . PRO   B 1 298 ? 40.118 -17.022 23.454  1.00 57.37  ? 298 PRO   B N   1 
ATOM   5144 C CA  . PRO   B 1 298 ? 40.559 -18.405 23.102  1.00 58.05  ? 298 PRO   B CA  1 
ATOM   5145 C C   . PRO   B 1 298 ? 40.484 -19.495 24.185  1.00 63.26  ? 298 PRO   B C   1 
ATOM   5146 O O   . PRO   B 1 298 ? 40.315 -20.674 23.848  1.00 62.41  ? 298 PRO   B O   1 
ATOM   5147 C CB  . PRO   B 1 298 ? 41.982 -18.208 22.565  1.00 59.44  ? 298 PRO   B CB  1 
ATOM   5148 C CG  . PRO   B 1 298 ? 42.408 -16.851 23.087  1.00 63.47  ? 298 PRO   B CG  1 
ATOM   5149 C CD  . PRO   B 1 298 ? 41.161 -16.025 23.131  1.00 58.78  ? 298 PRO   B CD  1 
ATOM   5150 N N   . ASP   B 1 299 ? 40.587 -19.095 25.479  1.00 60.52  ? 299 ASP   B N   1 
ATOM   5151 C CA  . ASP   B 1 299 ? 40.518 -19.967 26.661  1.00 60.32  ? 299 ASP   B CA  1 
ATOM   5152 C C   . ASP   B 1 299 ? 39.150 -20.623 26.861  1.00 65.26  ? 299 ASP   B C   1 
ATOM   5153 O O   . ASP   B 1 299 ? 39.040 -21.557 27.662  1.00 67.48  ? 299 ASP   B O   1 
ATOM   5154 C CB  . ASP   B 1 299 ? 40.916 -19.198 27.936  1.00 62.23  ? 299 ASP   B CB  1 
ATOM   5155 C CG  . ASP   B 1 299 ? 40.450 -17.752 27.964  1.00 75.31  ? 299 ASP   B CG  1 
ATOM   5156 O OD1 . ASP   B 1 299 ? 39.496 -17.442 28.735  1.00 74.02  ? 299 ASP   B OD1 1 
ATOM   5157 O OD2 . ASP   B 1 299 ? 41.033 -16.926 27.216  1.00 83.19  ? 299 ASP   B OD2 1 
ATOM   5158 N N   . GLY   B 1 300 ? 38.124 -20.124 26.165  1.00 58.66  ? 300 GLY   B N   1 
ATOM   5159 C CA  . GLY   B 1 300 ? 36.761 -20.636 26.249  1.00 57.07  ? 300 GLY   B CA  1 
ATOM   5160 C C   . GLY   B 1 300 ? 36.069 -20.301 27.556  1.00 58.63  ? 300 GLY   B C   1 
ATOM   5161 O O   . GLY   B 1 300 ? 34.941 -20.749 27.783  1.00 58.52  ? 300 GLY   B O   1 
ATOM   5162 N N   . LYS   B 1 301 ? 36.733 -19.495 28.417  1.00 52.03  ? 301 LYS   B N   1 
ATOM   5163 C CA  . LYS   B 1 301 ? 36.232 -19.100 29.730  1.00 50.77  ? 301 LYS   B CA  1 
ATOM   5164 C C   . LYS   B 1 301 ? 35.598 -17.711 29.765  1.00 53.50  ? 301 LYS   B C   1 
ATOM   5165 O O   . LYS   B 1 301 ? 34.563 -17.533 30.395  1.00 52.60  ? 301 LYS   B O   1 
ATOM   5166 C CB  . LYS   B 1 301 ? 37.362 -19.183 30.775  1.00 52.43  ? 301 LYS   B CB  1 
ATOM   5167 C CG  . LYS   B 1 301 ? 37.504 -20.537 31.446  1.00 64.46  ? 301 LYS   B CG  1 
ATOM   5168 C CD  . LYS   B 1 301 ? 38.288 -20.423 32.759  1.00 79.80  ? 301 LYS   B CD  1 
ATOM   5169 C CE  . LYS   B 1 301 ? 37.460 -19.909 33.928  1.00 90.14  ? 301 LYS   B CE  1 
ATOM   5170 N NZ  . LYS   B 1 301 ? 38.306 -19.589 35.109  1.00 96.18  ? 301 LYS   B NZ  1 
ATOM   5171 N N   . THR   B 1 302 ? 36.245 -16.729 29.133  1.00 50.02  ? 302 THR   B N   1 
ATOM   5172 C CA  . THR   B 1 302 ? 35.809 -15.342 29.100  1.00 49.92  ? 302 THR   B CA  1 
ATOM   5173 C C   . THR   B 1 302 ? 34.985 -15.005 27.851  1.00 54.24  ? 302 THR   B C   1 
ATOM   5174 O O   . THR   B 1 302 ? 35.342 -15.371 26.730  1.00 53.43  ? 302 THR   B O   1 
ATOM   5175 C CB  . THR   B 1 302 ? 36.999 -14.425 29.361  1.00 59.33  ? 302 THR   B CB  1 
ATOM   5176 O OG1 . THR   B 1 302 ? 37.584 -14.805 30.609  1.00 61.59  ? 302 THR   B OG1 1 
ATOM   5177 C CG2 . THR   B 1 302 ? 36.616 -12.946 29.406  1.00 58.88  ? 302 THR   B CG2 1 
ATOM   5178 N N   . VAL   B 1 303 ? 33.869 -14.303 28.069  1.00 50.68  ? 303 VAL   B N   1 
ATOM   5179 C CA  . VAL   B 1 303 ? 32.940 -13.887 27.025  1.00 49.51  ? 303 VAL   B CA  1 
ATOM   5180 C C   . VAL   B 1 303 ? 32.443 -12.469 27.354  1.00 49.84  ? 303 VAL   B C   1 
ATOM   5181 O O   . VAL   B 1 303 ? 32.174 -12.166 28.520  1.00 49.51  ? 303 VAL   B O   1 
ATOM   5182 C CB  . VAL   B 1 303 ? 31.801 -14.941 26.932  1.00 54.04  ? 303 VAL   B CB  1 
ATOM   5183 C CG1 . VAL   B 1 303 ? 30.450 -14.338 26.570  1.00 53.99  ? 303 VAL   B CG1 1 
ATOM   5184 C CG2 . VAL   B 1 303 ? 32.170 -16.087 25.990  1.00 53.86  ? 303 VAL   B CG2 1 
ATOM   5185 N N   . GLU   B 1 304 ? 32.347 -11.607 26.327  1.00 43.30  ? 304 GLU   B N   1 
ATOM   5186 C CA  . GLU   B 1 304 ? 31.838 -10.243 26.442  1.00 41.94  ? 304 GLU   B CA  1 
ATOM   5187 C C   . GLU   B 1 304 ? 30.762 -10.098 25.378  1.00 43.61  ? 304 GLU   B C   1 
ATOM   5188 O O   . GLU   B 1 304 ? 31.066 -10.190 24.198  1.00 43.95  ? 304 GLU   B O   1 
ATOM   5189 C CB  . GLU   B 1 304 ? 32.949 -9.198  26.268  1.00 43.48  ? 304 GLU   B CB  1 
ATOM   5190 C CG  . GLU   B 1 304 ? 32.585 -7.843  26.847  1.00 57.42  ? 304 GLU   B CG  1 
ATOM   5191 C CD  . GLU   B 1 304 ? 32.211 -6.785  25.834  1.00 84.57  ? 304 GLU   B CD  1 
ATOM   5192 O OE1 . GLU   B 1 304 ? 33.120 -6.278  25.140  1.00 83.04  ? 304 GLU   B OE1 1 
ATOM   5193 O OE2 . GLU   B 1 304 ? 31.008 -6.462  25.732  1.00 88.58  ? 304 GLU   B OE2 1 
ATOM   5194 N N   . ALA   B 1 305 ? 29.505 -9.907  25.789  1.00 38.75  ? 305 ALA   B N   1 
ATOM   5195 C CA  . ALA   B 1 305 ? 28.371 -9.775  24.882  1.00 37.47  ? 305 ALA   B CA  1 
ATOM   5196 C C   . ALA   B 1 305 ? 27.812 -8.378  24.837  1.00 43.12  ? 305 ALA   B C   1 
ATOM   5197 O O   . ALA   B 1 305 ? 27.751 -7.686  25.862  1.00 42.17  ? 305 ALA   B O   1 
ATOM   5198 C CB  . ALA   B 1 305 ? 27.277 -10.749 25.263  1.00 37.64  ? 305 ALA   B CB  1 
ATOM   5199 N N   . GLU   B 1 306 ? 27.378 -7.967  23.631  1.00 40.75  ? 306 GLU   B N   1 
ATOM   5200 C CA  . GLU   B 1 306 ? 26.776 -6.663  23.374  1.00 40.33  ? 306 GLU   B CA  1 
ATOM   5201 C C   . GLU   B 1 306 ? 25.991 -6.667  22.098  1.00 44.54  ? 306 GLU   B C   1 
ATOM   5202 O O   . GLU   B 1 306 ? 26.253 -7.495  21.231  1.00 46.08  ? 306 GLU   B O   1 
ATOM   5203 C CB  . GLU   B 1 306 ? 27.817 -5.515  23.393  1.00 41.51  ? 306 GLU   B CB  1 
ATOM   5204 C CG  . GLU   B 1 306 ? 28.732 -5.383  22.194  1.00 52.32  ? 306 GLU   B CG  1 
ATOM   5205 C CD  . GLU   B 1 306 ? 29.734 -4.251  22.322  1.00 79.84  ? 306 GLU   B CD  1 
ATOM   5206 O OE1 . GLU   B 1 306 ? 29.310 -3.089  22.537  1.00 79.78  ? 306 GLU   B OE1 1 
ATOM   5207 O OE2 . GLU   B 1 306 ? 30.950 -4.528  22.206  1.00 75.10  ? 306 GLU   B OE2 1 
ATOM   5208 N N   . ALA   B 1 307 ? 25.029 -5.735  21.977  1.00 39.93  ? 307 ALA   B N   1 
ATOM   5209 C CA  . ALA   B 1 307 ? 24.223 -5.521  20.775  1.00 38.80  ? 307 ALA   B CA  1 
ATOM   5210 C C   . ALA   B 1 307 ? 25.176 -5.017  19.674  1.00 42.99  ? 307 ALA   B C   1 
ATOM   5211 O O   . ALA   B 1 307 ? 26.114 -4.277  19.966  1.00 41.51  ? 307 ALA   B O   1 
ATOM   5212 C CB  . ALA   B 1 307 ? 23.177 -4.461  21.046  1.00 39.04  ? 307 ALA   B CB  1 
ATOM   5213 N N   . ALA   B 1 308 ? 24.950 -5.426  18.426  1.00 41.93  ? 308 ALA   B N   1 
ATOM   5214 C CA  . ALA   B 1 308 ? 25.787 -4.996  17.298  1.00 42.21  ? 308 ALA   B CA  1 
ATOM   5215 C C   . ALA   B 1 308 ? 25.171 -3.750  16.624  1.00 48.65  ? 308 ALA   B C   1 
ATOM   5216 O O   . ALA   B 1 308 ? 24.888 -3.758  15.426  1.00 52.84  ? 308 ALA   B O   1 
ATOM   5217 C CB  . ALA   B 1 308 ? 25.971 -6.137  16.299  1.00 42.46  ? 308 ALA   B CB  1 
ATOM   5218 N N   . HIS   B 1 309 ? 24.934 -2.696  17.409  1.00 41.48  ? 309 HIS   B N   1 
ATOM   5219 C CA  . HIS   B 1 309 ? 24.376 -1.415  16.961  1.00 39.95  ? 309 HIS   B CA  1 
ATOM   5220 C C   . HIS   B 1 309 ? 24.833 -0.319  17.914  1.00 42.92  ? 309 HIS   B C   1 
ATOM   5221 O O   . HIS   B 1 309 ? 25.392 -0.627  18.961  1.00 43.92  ? 309 HIS   B O   1 
ATOM   5222 C CB  . HIS   B 1 309 ? 22.835 -1.451  16.769  1.00 39.77  ? 309 HIS   B CB  1 
ATOM   5223 C CG  . HIS   B 1 309 ? 22.030 -1.762  17.990  1.00 42.22  ? 309 HIS   B CG  1 
ATOM   5224 N ND1 . HIS   B 1 309 ? 21.999 -0.904  19.077  1.00 43.98  ? 309 HIS   B ND1 1 
ATOM   5225 C CD2 . HIS   B 1 309 ? 21.205 -2.803  18.236  1.00 43.40  ? 309 HIS   B CD2 1 
ATOM   5226 C CE1 . HIS   B 1 309 ? 21.195 -1.471  19.960  1.00 43.25  ? 309 HIS   B CE1 1 
ATOM   5227 N NE2 . HIS   B 1 309 ? 20.684 -2.613  19.493  1.00 43.39  ? 309 HIS   B NE2 1 
ATOM   5228 N N   . GLY   B 1 310 ? 24.625 0.934   17.551  1.00 38.42  ? 310 GLY   B N   1 
ATOM   5229 C CA  . GLY   B 1 310 ? 25.050 2.053   18.384  1.00 37.74  ? 310 GLY   B CA  1 
ATOM   5230 C C   . GLY   B 1 310 ? 24.077 2.484   19.457  1.00 40.26  ? 310 GLY   B C   1 
ATOM   5231 O O   . GLY   B 1 310 ? 23.193 1.727   19.846  1.00 38.95  ? 310 GLY   B O   1 
ATOM   5232 N N   . THR   B 1 311 ? 24.237 3.729   19.928  1.00 37.51  ? 311 THR   B N   1 
ATOM   5233 C CA  . THR   B 1 311 ? 23.433 4.339   20.984  1.00 37.17  ? 311 THR   B CA  1 
ATOM   5234 C C   . THR   B 1 311 ? 22.037 4.784   20.558  1.00 44.17  ? 311 THR   B C   1 
ATOM   5235 O O   . THR   B 1 311 ? 21.223 5.146   21.421  1.00 45.40  ? 311 THR   B O   1 
ATOM   5236 C CB  . THR   B 1 311 ? 24.205 5.451   21.668  1.00 37.09  ? 311 THR   B CB  1 
ATOM   5237 O OG1 . THR   B 1 311 ? 24.448 6.486   20.733  1.00 34.72  ? 311 THR   B OG1 1 
ATOM   5238 C CG2 . THR   B 1 311 ? 25.502 4.967   22.279  1.00 33.25  ? 311 THR   B CG2 1 
ATOM   5239 N N   . VAL   B 1 312 ? 21.756 4.726   19.236  1.00 40.61  ? 312 VAL   B N   1 
ATOM   5240 C CA  . VAL   B 1 312 ? 20.493 5.104   18.587  1.00 40.68  ? 312 VAL   B CA  1 
ATOM   5241 C C   . VAL   B 1 312 ? 20.184 6.581   18.876  1.00 46.38  ? 312 VAL   B C   1 
ATOM   5242 O O   . VAL   B 1 312 ? 19.106 6.894   19.372  1.00 47.39  ? 312 VAL   B O   1 
ATOM   5243 C CB  . VAL   B 1 312 ? 19.299 4.112   18.857  1.00 43.43  ? 312 VAL   B CB  1 
ATOM   5244 C CG1 . VAL   B 1 312 ? 18.267 4.190   17.744  1.00 43.01  ? 312 VAL   B CG1 1 
ATOM   5245 C CG2 . VAL   B 1 312 ? 19.787 2.670   19.000  1.00 42.59  ? 312 VAL   B CG2 1 
ATOM   5246 N N   . THR   B 1 313 ? 21.165 7.479   18.592  1.00 43.82  ? 313 THR   B N   1 
ATOM   5247 C CA  . THR   B 1 313 ? 21.084 8.947   18.807  1.00 43.94  ? 313 THR   B CA  1 
ATOM   5248 C C   . THR   B 1 313 ? 19.734 9.598   18.382  1.00 46.84  ? 313 THR   B C   1 
ATOM   5249 O O   . THR   B 1 313 ? 19.136 10.327  19.179  1.00 46.36  ? 313 THR   B O   1 
ATOM   5250 C CB  . THR   B 1 313 ? 22.339 9.674   18.251  1.00 44.18  ? 313 THR   B CB  1 
ATOM   5251 O OG1 . THR   B 1 313 ? 23.497 9.042   18.789  1.00 43.00  ? 313 THR   B OG1 1 
ATOM   5252 C CG2 . THR   B 1 313 ? 22.385 11.150  18.633  1.00 36.11  ? 313 THR   B CG2 1 
ATOM   5253 N N   . ARG   B 1 314 ? 19.277 9.318   17.140  1.00 41.35  ? 314 ARG   B N   1 
ATOM   5254 C CA  . ARG   B 1 314 ? 18.035 9.804   16.529  1.00 40.89  ? 314 ARG   B CA  1 
ATOM   5255 C C   . ARG   B 1 314 ? 16.837 9.613   17.482  1.00 44.83  ? 314 ARG   B C   1 
ATOM   5256 O O   . ARG   B 1 314 ? 16.087 10.557  17.720  1.00 45.64  ? 314 ARG   B O   1 
ATOM   5257 C CB  . ARG   B 1 314 ? 17.791 9.019   15.231  1.00 44.16  ? 314 ARG   B CB  1 
ATOM   5258 C CG  . ARG   B 1 314 ? 17.729 9.844   13.944  1.00 65.79  ? 314 ARG   B CG  1 
ATOM   5259 C CD  . ARG   B 1 314 ? 16.309 9.984   13.372  1.00 80.64  ? 314 ARG   B CD  1 
ATOM   5260 N NE  . ARG   B 1 314 ? 15.579 8.710   13.315  1.00 82.51  ? 314 ARG   B NE  1 
ATOM   5261 C CZ  . ARG   B 1 314 ? 14.278 8.592   13.069  1.00 96.37  ? 314 ARG   B CZ  1 
ATOM   5262 N NH1 . ARG   B 1 314 ? 13.536 9.671   12.838  1.00 89.52  ? 314 ARG   B NH1 1 
ATOM   5263 N NH2 . ARG   B 1 314 ? 13.705 7.395   13.056  1.00 79.35  ? 314 ARG   B NH2 1 
ATOM   5264 N N   . HIS   B 1 315 ? 16.680 8.395   18.049  1.00 40.47  ? 315 HIS   B N   1 
ATOM   5265 C CA  . HIS   B 1 315 ? 15.610 8.034   18.981  1.00 38.85  ? 315 HIS   B CA  1 
ATOM   5266 C C   . HIS   B 1 315 ? 15.801 8.746   20.311  1.00 41.04  ? 315 HIS   B C   1 
ATOM   5267 O O   . HIS   B 1 315 ? 14.824 9.141   20.949  1.00 40.33  ? 315 HIS   B O   1 
ATOM   5268 C CB  . HIS   B 1 315 ? 15.571 6.515   19.182  1.00 39.50  ? 315 HIS   B CB  1 
ATOM   5269 C CG  . HIS   B 1 315 ? 15.129 5.738   17.981  1.00 43.32  ? 315 HIS   B CG  1 
ATOM   5270 N ND1 . HIS   B 1 315 ? 14.691 4.433   18.097  1.00 45.04  ? 315 HIS   B ND1 1 
ATOM   5271 C CD2 . HIS   B 1 315 ? 15.080 6.099   16.672  1.00 45.28  ? 315 HIS   B CD2 1 
ATOM   5272 C CE1 . HIS   B 1 315 ? 14.382 4.049   16.868  1.00 44.37  ? 315 HIS   B CE1 1 
ATOM   5273 N NE2 . HIS   B 1 315 ? 14.598 5.018   15.980  1.00 44.67  ? 315 HIS   B NE2 1 
ATOM   5274 N N   . TYR   B 1 316 ? 17.058 8.946   20.721  1.00 37.25  ? 316 TYR   B N   1 
ATOM   5275 C CA  . TYR   B 1 316 ? 17.331 9.663   21.971  1.00 37.12  ? 316 TYR   B CA  1 
ATOM   5276 C C   . TYR   B 1 316 ? 16.892 11.134  21.861  1.00 41.42  ? 316 TYR   B C   1 
ATOM   5277 O O   . TYR   B 1 316 ? 16.302 11.667  22.805  1.00 40.02  ? 316 TYR   B O   1 
ATOM   5278 C CB  . TYR   B 1 316 ? 18.811 9.550   22.361  1.00 36.92  ? 316 TYR   B CB  1 
ATOM   5279 C CG  . TYR   B 1 316 ? 19.117 10.192  23.690  1.00 36.96  ? 316 TYR   B CG  1 
ATOM   5280 C CD1 . TYR   B 1 316 ? 18.536 9.716   24.867  1.00 38.87  ? 316 TYR   B CD1 1 
ATOM   5281 C CD2 . TYR   B 1 316 ? 19.983 11.279  23.780  1.00 36.59  ? 316 TYR   B CD2 1 
ATOM   5282 C CE1 . TYR   B 1 316 ? 18.831 10.290  26.101  1.00 38.17  ? 316 TYR   B CE1 1 
ATOM   5283 C CE2 . TYR   B 1 316 ? 20.293 11.854  25.012  1.00 36.85  ? 316 TYR   B CE2 1 
ATOM   5284 C CZ  . TYR   B 1 316 ? 19.716 11.354  26.169  1.00 45.07  ? 316 TYR   B CZ  1 
ATOM   5285 O OH  . TYR   B 1 316 ? 20.005 11.913  27.390  1.00 48.98  ? 316 TYR   B OH  1 
ATOM   5286 N N   . ARG   B 1 317 ? 17.171 11.770  20.694  1.00 39.44  ? 317 ARG   B N   1 
ATOM   5287 C CA  . ARG   B 1 317 ? 16.798 13.157  20.399  1.00 39.83  ? 317 ARG   B CA  1 
ATOM   5288 C C   . ARG   B 1 317 ? 15.268 13.297  20.436  1.00 46.33  ? 317 ARG   B C   1 
ATOM   5289 O O   . ARG   B 1 317 ? 14.765 14.311  20.923  1.00 46.52  ? 317 ARG   B O   1 
ATOM   5290 C CB  . ARG   B 1 317 ? 17.357 13.620  19.033  1.00 37.01  ? 317 ARG   B CB  1 
ATOM   5291 C CG  . ARG   B 1 317 ? 18.884 13.638  18.902  1.00 40.22  ? 317 ARG   B CG  1 
ATOM   5292 C CD  . ARG   B 1 317 ? 19.549 14.618  19.855  1.00 48.62  ? 317 ARG   B CD  1 
ATOM   5293 N NE  . ARG   B 1 317 ? 21.013 14.595  19.761  1.00 46.92  ? 317 ARG   B NE  1 
ATOM   5294 C CZ  . ARG   B 1 317 ? 21.831 14.506  20.805  1.00 48.43  ? 317 ARG   B CZ  1 
ATOM   5295 N NH1 . ARG   B 1 317 ? 21.343 14.411  22.033  1.00 43.45  ? 317 ARG   B NH1 1 
ATOM   5296 N NH2 . ARG   B 1 317 ? 23.143 14.497  20.627  1.00 35.20  ? 317 ARG   B NH2 1 
ATOM   5297 N N   . MET   B 1 318 ? 14.532 12.260  19.945  1.00 43.49  ? 318 MET   B N   1 
ATOM   5298 C CA  . MET   B 1 318 ? 13.059 12.242  19.936  1.00 42.57  ? 318 MET   B CA  1 
ATOM   5299 C C   . MET   B 1 318 ? 12.583 12.196  21.382  1.00 47.59  ? 318 MET   B C   1 
ATOM   5300 O O   . MET   B 1 318 ? 11.704 12.968  21.747  1.00 46.70  ? 318 MET   B O   1 
ATOM   5301 C CB  . MET   B 1 318 ? 12.503 11.060  19.135  1.00 44.12  ? 318 MET   B CB  1 
ATOM   5302 C CG  . MET   B 1 318 ? 12.677 11.188  17.628  1.00 47.53  ? 318 MET   B CG  1 
ATOM   5303 S SD  . MET   B 1 318 ? 12.383 9.603   16.737  1.00 52.25  ? 318 MET   B SD  1 
ATOM   5304 C CE  . MET   B 1 318 ? 10.635 9.322   17.112  1.00 48.31  ? 318 MET   B CE  1 
ATOM   5305 N N   . TYR   B 1 319 ? 13.213 11.328  22.209  1.00 45.43  ? 319 TYR   B N   1 
ATOM   5306 C CA  . TYR   B 1 319 ? 12.944 11.150  23.641  1.00 45.37  ? 319 TYR   B CA  1 
ATOM   5307 C C   . TYR   B 1 319 ? 13.129 12.485  24.396  1.00 47.27  ? 319 TYR   B C   1 
ATOM   5308 O O   . TYR   B 1 319 ? 12.279 12.855  25.213  1.00 46.74  ? 319 TYR   B O   1 
ATOM   5309 C CB  . TYR   B 1 319 ? 13.857 10.051  24.218  1.00 47.77  ? 319 TYR   B CB  1 
ATOM   5310 C CG  . TYR   B 1 319 ? 13.432 9.548   25.577  1.00 52.50  ? 319 TYR   B CG  1 
ATOM   5311 C CD1 . TYR   B 1 319 ? 12.440 8.581   25.706  1.00 55.07  ? 319 TYR   B CD1 1 
ATOM   5312 C CD2 . TYR   B 1 319 ? 14.041 10.017  26.738  1.00 54.37  ? 319 TYR   B CD2 1 
ATOM   5313 C CE1 . TYR   B 1 319 ? 12.035 8.123   26.959  1.00 56.65  ? 319 TYR   B CE1 1 
ATOM   5314 C CE2 . TYR   B 1 319 ? 13.651 9.558   27.997  1.00 55.10  ? 319 TYR   B CE2 1 
ATOM   5315 C CZ  . TYR   B 1 319 ? 12.643 8.618   28.100  1.00 64.24  ? 319 TYR   B CZ  1 
ATOM   5316 O OH  . TYR   B 1 319 ? 12.271 8.149   29.331  1.00 69.88  ? 319 TYR   B OH  1 
ATOM   5317 N N   . GLN   B 1 320 ? 14.209 13.222  24.084  1.00 42.37  ? 320 GLN   B N   1 
ATOM   5318 C CA  . GLN   B 1 320 ? 14.515 14.525  24.698  1.00 41.54  ? 320 GLN   B CA  1 
ATOM   5319 C C   . GLN   B 1 320 ? 13.517 15.607  24.286  1.00 45.65  ? 320 GLN   B C   1 
ATOM   5320 O O   . GLN   B 1 320 ? 13.333 16.564  25.028  1.00 46.08  ? 320 GLN   B O   1 
ATOM   5321 C CB  . GLN   B 1 320 ? 15.928 14.985  24.336  1.00 42.32  ? 320 GLN   B CB  1 
ATOM   5322 C CG  . GLN   B 1 320 ? 17.050 14.140  24.919  1.00 36.48  ? 320 GLN   B CG  1 
ATOM   5323 C CD  . GLN   B 1 320 ? 18.376 14.641  24.426  1.00 51.42  ? 320 GLN   B CD  1 
ATOM   5324 O OE1 . GLN   B 1 320 ? 18.655 14.687  23.224  1.00 49.87  ? 320 GLN   B OE1 1 
ATOM   5325 N NE2 . GLN   B 1 320 ? 19.231 15.019  25.342  1.00 43.43  ? 320 GLN   B NE2 1 
ATOM   5326 N N   . LYS   B 1 321 ? 12.874 15.457  23.111  1.00 41.57  ? 321 LYS   B N   1 
ATOM   5327 C CA  . LYS   B 1 321 ? 11.883 16.401  22.584  1.00 40.34  ? 321 LYS   B CA  1 
ATOM   5328 C C   . LYS   B 1 321 ? 10.449 16.012  22.986  1.00 47.04  ? 321 LYS   B C   1 
ATOM   5329 O O   . LYS   B 1 321 ? 9.488  16.635  22.532  1.00 47.95  ? 321 LYS   B O   1 
ATOM   5330 C CB  . LYS   B 1 321 ? 12.025 16.517  21.057  1.00 41.03  ? 321 LYS   B CB  1 
ATOM   5331 C CG  . LYS   B 1 321 ? 13.253 17.316  20.639  1.00 56.60  ? 321 LYS   B CG  1 
ATOM   5332 C CD  . LYS   B 1 321 ? 13.528 17.189  19.140  1.00 74.40  ? 321 LYS   B CD  1 
ATOM   5333 C CE  . LYS   B 1 321 ? 14.860 17.788  18.727  1.00 80.35  ? 321 LYS   B CE  1 
ATOM   5334 N NZ  . LYS   B 1 321 ? 15.183 17.488  17.302  1.00 83.80  ? 321 LYS   B NZ  1 
ATOM   5335 N N   . GLY   B 1 322 ? 10.316 14.994  23.842  1.00 43.78  ? 322 GLY   B N   1 
ATOM   5336 C CA  . GLY   B 1 322 ? 9.015  14.516  24.295  1.00 43.24  ? 322 GLY   B CA  1 
ATOM   5337 C C   . GLY   B 1 322 ? 8.237  13.702  23.271  1.00 46.04  ? 322 GLY   B C   1 
ATOM   5338 O O   . GLY   B 1 322 ? 7.036  13.495  23.452  1.00 46.02  ? 322 GLY   B O   1 
ATOM   5339 N N   . GLN   B 1 323 ? 8.895  13.217  22.197  1.00 41.29  ? 323 GLN   B N   1 
ATOM   5340 C CA  . GLN   B 1 323 ? 8.228  12.403  21.167  1.00 40.84  ? 323 GLN   B CA  1 
ATOM   5341 C C   . GLN   B 1 323 ? 8.268  10.934  21.523  1.00 46.60  ? 323 GLN   B C   1 
ATOM   5342 O O   . GLN   B 1 323 ? 9.229  10.475  22.137  1.00 46.10  ? 323 GLN   B O   1 
ATOM   5343 C CB  . GLN   B 1 323 ? 8.866  12.575  19.792  1.00 41.03  ? 323 GLN   B CB  1 
ATOM   5344 C CG  . GLN   B 1 323 ? 9.032  14.014  19.345  1.00 41.07  ? 323 GLN   B CG  1 
ATOM   5345 C CD  . GLN   B 1 323 ? 9.726  14.117  18.011  1.00 63.34  ? 323 GLN   B CD  1 
ATOM   5346 O OE1 . GLN   B 1 323 ? 9.641  13.224  17.154  1.00 64.58  ? 323 GLN   B OE1 1 
ATOM   5347 N NE2 . GLN   B 1 323 ? 10.423 15.217  17.800  1.00 52.96  ? 323 GLN   B NE2 1 
ATOM   5348 N N   . GLU   B 1 324 ? 7.217  10.191  21.130  1.00 44.73  ? 324 GLU   B N   1 
ATOM   5349 C CA  . GLU   B 1 324 ? 7.117  8.747   21.355  1.00 44.21  ? 324 GLU   B CA  1 
ATOM   5350 C C   . GLU   B 1 324 ? 8.206  8.049   20.537  1.00 48.34  ? 324 GLU   B C   1 
ATOM   5351 O O   . GLU   B 1 324 ? 8.400  8.381   19.364  1.00 47.95  ? 324 GLU   B O   1 
ATOM   5352 C CB  . GLU   B 1 324 ? 5.760  8.251   20.881  1.00 45.45  ? 324 GLU   B CB  1 
ATOM   5353 C CG  . GLU   B 1 324 ? 5.411  6.854   21.351  1.00 56.06  ? 324 GLU   B CG  1 
ATOM   5354 C CD  . GLU   B 1 324 ? 4.069  6.355   20.853  1.00 66.67  ? 324 GLU   B CD  1 
ATOM   5355 O OE1 . GLU   B 1 324 ? 3.847  6.369   19.619  1.00 50.56  ? 324 GLU   B OE1 1 
ATOM   5356 O OE2 . GLU   B 1 324 ? 3.241  5.943   21.698  1.00 52.65  ? 324 GLU   B OE2 1 
ATOM   5357 N N   . THR   B 1 325 ? 8.927  7.101   21.158  1.00 44.76  ? 325 THR   B N   1 
ATOM   5358 C CA  . THR   B 1 325 ? 9.974  6.353   20.456  1.00 43.63  ? 325 THR   B CA  1 
ATOM   5359 C C   . THR   B 1 325 ? 9.539  4.887   20.350  1.00 46.07  ? 325 THR   B C   1 
ATOM   5360 O O   . THR   B 1 325 ? 8.722  4.408   21.150  1.00 43.14  ? 325 THR   B O   1 
ATOM   5361 C CB  . THR   B 1 325 ? 11.368 6.437   21.156  1.00 43.71  ? 325 THR   B CB  1 
ATOM   5362 O OG1 . THR   B 1 325 ? 11.336 5.748   22.408  1.00 38.88  ? 325 THR   B OG1 1 
ATOM   5363 C CG2 . THR   B 1 325 ? 11.906 7.843   21.302  1.00 34.46  ? 325 THR   B CG2 1 
ATOM   5364 N N   . SER   B 1 326 ? 10.105 4.180   19.359  1.00 43.43  ? 326 SER   B N   1 
ATOM   5365 C CA  . SER   B 1 326 ? 9.876  2.758   19.174  1.00 43.02  ? 326 SER   B CA  1 
ATOM   5366 C C   . SER   B 1 326 ? 11.245 2.155   18.895  1.00 46.63  ? 326 SER   B C   1 
ATOM   5367 O O   . SER   B 1 326 ? 11.638 1.978   17.740  1.00 46.25  ? 326 SER   B O   1 
ATOM   5368 C CB  . SER   B 1 326 ? 8.872  2.485   18.063  1.00 45.26  ? 326 SER   B CB  1 
ATOM   5369 O OG  . SER   B 1 326 ? 8.452  1.132   18.141  1.00 48.97  ? 326 SER   B OG  1 
ATOM   5370 N N   . THR   B 1 327 ? 11.993 1.898   19.976  1.00 43.51  ? 327 THR   B N   1 
ATOM   5371 C CA  . THR   B 1 327 ? 13.350 1.348   19.911  1.00 42.97  ? 327 THR   B CA  1 
ATOM   5372 C C   . THR   B 1 327 ? 13.353 -0.146  20.176  1.00 45.54  ? 327 THR   B C   1 
ATOM   5373 O O   . THR   B 1 327 ? 12.807 -0.605  21.175  1.00 44.18  ? 327 THR   B O   1 
ATOM   5374 C CB  . THR   B 1 327 ? 14.326 2.168   20.790  1.00 46.26  ? 327 THR   B CB  1 
ATOM   5375 O OG1 . THR   B 1 327 ? 14.166 3.546   20.465  1.00 46.74  ? 327 THR   B OG1 1 
ATOM   5376 C CG2 . THR   B 1 327 ? 15.788 1.790   20.570  1.00 40.11  ? 327 THR   B CG2 1 
ATOM   5377 N N   . ASN   B 1 328 ? 13.976 -0.897  19.262  1.00 42.69  ? 328 ASN   B N   1 
ATOM   5378 C CA  . ASN   B 1 328 ? 14.096 -2.347  19.333  1.00 41.89  ? 328 ASN   B CA  1 
ATOM   5379 C C   . ASN   B 1 328 ? 15.113 -2.751  20.413  1.00 44.94  ? 328 ASN   B C   1 
ATOM   5380 O O   . ASN   B 1 328 ? 16.300 -2.449  20.286  1.00 43.93  ? 328 ASN   B O   1 
ATOM   5381 C CB  . ASN   B 1 328 ? 14.485 -2.883  17.967  1.00 40.40  ? 328 ASN   B CB  1 
ATOM   5382 C CG  . ASN   B 1 328 ? 14.378 -4.370  17.784  1.00 49.24  ? 328 ASN   B CG  1 
ATOM   5383 O OD1 . ASN   B 1 328 ? 14.129 -5.160  18.701  1.00 37.36  ? 328 ASN   B OD1 1 
ATOM   5384 N ND2 . ASN   B 1 328 ? 14.580 -4.776  16.566  1.00 38.90  ? 328 ASN   B ND2 1 
ATOM   5385 N N   . PRO   B 1 329 ? 14.656 -3.443  21.484  1.00 41.88  ? 329 PRO   B N   1 
ATOM   5386 C CA  . PRO   B 1 329 ? 15.579 -3.829  22.572  1.00 40.53  ? 329 PRO   B CA  1 
ATOM   5387 C C   . PRO   B 1 329 ? 16.159 -5.238  22.478  1.00 43.23  ? 329 PRO   B C   1 
ATOM   5388 O O   . PRO   B 1 329 ? 16.905 -5.647  23.383  1.00 42.79  ? 329 PRO   B O   1 
ATOM   5389 C CB  . PRO   B 1 329 ? 14.668 -3.759  23.796  1.00 42.38  ? 329 PRO   B CB  1 
ATOM   5390 C CG  . PRO   B 1 329 ? 13.321 -4.234  23.275  1.00 46.71  ? 329 PRO   B CG  1 
ATOM   5391 C CD  . PRO   B 1 329 ? 13.265 -3.853  21.796  1.00 42.72  ? 329 PRO   B CD  1 
ATOM   5392 N N   . ILE   B 1 330 ? 15.798 -5.984  21.414  1.00 39.30  ? 330 ILE   B N   1 
ATOM   5393 C CA  . ILE   B 1 330 ? 16.190 -7.384  21.201  1.00 39.70  ? 330 ILE   B CA  1 
ATOM   5394 C C   . ILE   B 1 330 ? 17.674 -7.687  21.282  1.00 43.06  ? 330 ILE   B C   1 
ATOM   5395 O O   . ILE   B 1 330 ? 18.056 -8.590  22.040  1.00 43.25  ? 330 ILE   B O   1 
ATOM   5396 C CB  . ILE   B 1 330 ? 15.470 -8.042  19.978  1.00 43.02  ? 330 ILE   B CB  1 
ATOM   5397 C CG1 . ILE   B 1 330 ? 13.898 -7.997  20.104  1.00 43.28  ? 330 ILE   B CG1 1 
ATOM   5398 C CG2 . ILE   B 1 330 ? 16.010 -9.455  19.642  1.00 42.94  ? 330 ILE   B CG2 1 
ATOM   5399 C CD1 . ILE   B 1 330 ? 13.220 -8.738  21.292  1.00 44.28  ? 330 ILE   B CD1 1 
ATOM   5400 N N   . ALA   B 1 331 ? 18.505 -6.949  20.501  1.00 37.72  ? 331 ALA   B N   1 
ATOM   5401 C CA  . ALA   B 1 331 ? 19.955 -7.146  20.482  1.00 36.41  ? 331 ALA   B CA  1 
ATOM   5402 C C   . ALA   B 1 331 ? 20.524 -6.956  21.895  1.00 41.12  ? 331 ALA   B C   1 
ATOM   5403 O O   . ALA   B 1 331 ? 21.317 -7.789  22.337  1.00 41.71  ? 331 ALA   B O   1 
ATOM   5404 C CB  . ALA   B 1 331 ? 20.613 -6.218  19.466  1.00 36.46  ? 331 ALA   B CB  1 
ATOM   5405 N N   . SER   B 1 332 ? 20.029 -5.935  22.640  1.00 37.87  ? 332 SER   B N   1 
ATOM   5406 C CA  . SER   B 1 332 ? 20.439 -5.654  24.025  1.00 37.75  ? 332 SER   B CA  1 
ATOM   5407 C C   . SER   B 1 332 ? 20.004 -6.766  24.982  1.00 41.92  ? 332 SER   B C   1 
ATOM   5408 O O   . SER   B 1 332 ? 20.773 -7.088  25.881  1.00 43.49  ? 332 SER   B O   1 
ATOM   5409 C CB  . SER   B 1 332 ? 19.881 -4.320  24.505  1.00 41.26  ? 332 SER   B CB  1 
ATOM   5410 O OG  . SER   B 1 332 ? 20.170 -3.258  23.616  1.00 48.24  ? 332 SER   B OG  1 
ATOM   5411 N N   . ILE   B 1 333 ? 18.785 -7.349  24.804  1.00 37.70  ? 333 ILE   B N   1 
ATOM   5412 C CA  . ILE   B 1 333 ? 18.262 -8.458  25.627  1.00 37.38  ? 333 ILE   B CA  1 
ATOM   5413 C C   . ILE   B 1 333 ? 19.144 -9.668  25.373  1.00 42.79  ? 333 ILE   B C   1 
ATOM   5414 O O   . ILE   B 1 333 ? 19.520 -10.351 26.327  1.00 44.38  ? 333 ILE   B O   1 
ATOM   5415 C CB  . ILE   B 1 333 ? 16.757 -8.782  25.356  1.00 40.79  ? 333 ILE   B CB  1 
ATOM   5416 C CG1 . ILE   B 1 333 ? 15.839 -7.641  25.830  1.00 41.33  ? 333 ILE   B CG1 1 
ATOM   5417 C CG2 . ILE   B 1 333 ? 16.314 -10.128 25.994  1.00 41.54  ? 333 ILE   B CG2 1 
ATOM   5418 C CD1 . ILE   B 1 333 ? 14.558 -7.522  25.053  1.00 47.68  ? 333 ILE   B CD1 1 
ATOM   5419 N N   . PHE   B 1 334 ? 19.491 -9.929  24.093  1.00 39.04  ? 334 PHE   B N   1 
ATOM   5420 C CA  . PHE   B 1 334 ? 20.347 -11.060 23.744  1.00 38.01  ? 334 PHE   B CA  1 
ATOM   5421 C C   . PHE   B 1 334 ? 21.802 -10.925 24.238  1.00 44.20  ? 334 PHE   B C   1 
ATOM   5422 O O   . PHE   B 1 334 ? 22.479 -11.941 24.388  1.00 45.20  ? 334 PHE   B O   1 
ATOM   5423 C CB  . PHE   B 1 334 ? 20.185 -11.509 22.287  1.00 38.53  ? 334 PHE   B CB  1 
ATOM   5424 C CG  . PHE   B 1 334 ? 18.964 -12.364 21.995  1.00 39.30  ? 334 PHE   B CG  1 
ATOM   5425 C CD1 . PHE   B 1 334 ? 17.677 -11.835 22.098  1.00 41.80  ? 334 PHE   B CD1 1 
ATOM   5426 C CD2 . PHE   B 1 334 ? 19.102 -13.685 21.573  1.00 40.47  ? 334 PHE   B CD2 1 
ATOM   5427 C CE1 . PHE   B 1 334 ? 16.551 -12.621 21.809  1.00 42.66  ? 334 PHE   B CE1 1 
ATOM   5428 C CE2 . PHE   B 1 334 ? 17.974 -14.460 21.250  1.00 43.04  ? 334 PHE   B CE2 1 
ATOM   5429 C CZ  . PHE   B 1 334 ? 16.707 -13.932 21.393  1.00 41.33  ? 334 PHE   B CZ  1 
ATOM   5430 N N   . ALA   B 1 335 ? 22.263 -9.684  24.557  1.00 39.89  ? 335 ALA   B N   1 
ATOM   5431 C CA  . ALA   B 1 335 ? 23.588 -9.438  25.145  1.00 38.58  ? 335 ALA   B CA  1 
ATOM   5432 C C   . ALA   B 1 335 ? 23.491 -10.024 26.567  1.00 41.01  ? 335 ALA   B C   1 
ATOM   5433 O O   . ALA   B 1 335 ? 24.352 -10.787 26.987  1.00 40.86  ? 335 ALA   B O   1 
ATOM   5434 C CB  . ALA   B 1 335 ? 23.870 -7.937  25.218  1.00 39.31  ? 335 ALA   B CB  1 
ATOM   5435 N N   . TRP   B 1 336 ? 22.392 -9.720  27.273  1.00 37.47  ? 336 TRP   B N   1 
ATOM   5436 C CA  . TRP   B 1 336 ? 22.127 -10.238 28.617  1.00 37.14  ? 336 TRP   B CA  1 
ATOM   5437 C C   . TRP   B 1 336 ? 21.964 -11.770 28.635  1.00 42.04  ? 336 TRP   B C   1 
ATOM   5438 O O   . TRP   B 1 336 ? 22.620 -12.439 29.442  1.00 41.70  ? 336 TRP   B O   1 
ATOM   5439 C CB  . TRP   B 1 336 ? 20.891 -9.565  29.215  1.00 34.60  ? 336 TRP   B CB  1 
ATOM   5440 C CG  . TRP   B 1 336 ? 21.192 -8.223  29.792  1.00 34.79  ? 336 TRP   B CG  1 
ATOM   5441 C CD1 . TRP   B 1 336 ? 21.058 -7.013  29.176  1.00 37.34  ? 336 TRP   B CD1 1 
ATOM   5442 C CD2 . TRP   B 1 336 ? 21.692 -7.954  31.106  1.00 34.18  ? 336 TRP   B CD2 1 
ATOM   5443 N NE1 . TRP   B 1 336 ? 21.409 -6.004  30.037  1.00 36.27  ? 336 TRP   B NE1 1 
ATOM   5444 C CE2 . TRP   B 1 336 ? 21.805 -6.551  31.230  1.00 37.46  ? 336 TRP   B CE2 1 
ATOM   5445 C CE3 . TRP   B 1 336 ? 22.035 -8.768  32.205  1.00 35.15  ? 336 TRP   B CE3 1 
ATOM   5446 C CZ2 . TRP   B 1 336 ? 22.278 -5.937  32.398  1.00 36.53  ? 336 TRP   B CZ2 1 
ATOM   5447 C CZ3 . TRP   B 1 336 ? 22.496 -8.159  33.362  1.00 36.75  ? 336 TRP   B CZ3 1 
ATOM   5448 C CH2 . TRP   B 1 336 ? 22.617 -6.758  33.450  1.00 37.33  ? 336 TRP   B CH2 1 
ATOM   5449 N N   . THR   B 1 337 ? 21.098 -12.316 27.760  1.00 38.72  ? 337 THR   B N   1 
ATOM   5450 C CA  . THR   B 1 337 ? 20.873 -13.769 27.695  1.00 39.62  ? 337 THR   B CA  1 
ATOM   5451 C C   . THR   B 1 337 ? 22.129 -14.539 27.335  1.00 45.10  ? 337 THR   B C   1 
ATOM   5452 O O   . THR   B 1 337 ? 22.390 -15.560 27.964  1.00 45.09  ? 337 THR   B O   1 
ATOM   5453 C CB  . THR   B 1 337 ? 19.671 -14.150 26.832  1.00 44.16  ? 337 THR   B CB  1 
ATOM   5454 O OG1 . THR   B 1 337 ? 19.876 -13.710 25.488  1.00 41.58  ? 337 THR   B OG1 1 
ATOM   5455 C CG2 . THR   B 1 337 ? 18.365 -13.613 27.381  1.00 41.37  ? 337 THR   B CG2 1 
ATOM   5456 N N   . ARG   B 1 338 ? 22.929 -14.046 26.365  1.00 42.55  ? 338 ARG   B N   1 
ATOM   5457 C CA  . ARG   B 1 338 ? 24.178 -14.735 25.999  1.00 42.52  ? 338 ARG   B CA  1 
ATOM   5458 C C   . ARG   B 1 338 ? 25.163 -14.717 27.148  1.00 47.16  ? 338 ARG   B C   1 
ATOM   5459 O O   . ARG   B 1 338 ? 25.773 -15.750 27.427  1.00 48.71  ? 338 ARG   B O   1 
ATOM   5460 C CB  . ARG   B 1 338 ? 24.804 -14.213 24.696  1.00 40.30  ? 338 ARG   B CB  1 
ATOM   5461 C CG  . ARG   B 1 338 ? 24.393 -15.037 23.479  1.00 47.61  ? 338 ARG   B CG  1 
ATOM   5462 C CD  . ARG   B 1 338 ? 23.150 -14.476 22.827  1.00 56.32  ? 338 ARG   B CD  1 
ATOM   5463 N NE  . ARG   B 1 338 ? 22.435 -15.464 22.027  1.00 72.29  ? 338 ARG   B NE  1 
ATOM   5464 C CZ  . ARG   B 1 338 ? 22.208 -15.359 20.720  1.00 81.72  ? 338 ARG   B CZ  1 
ATOM   5465 N NH1 . ARG   B 1 338 ? 22.653 -14.302 20.041  1.00 50.34  ? 338 ARG   B NH1 1 
ATOM   5466 N NH2 . ARG   B 1 338 ? 21.529 -16.305 20.081  1.00 71.06  ? 338 ARG   B NH2 1 
ATOM   5467 N N   . GLY   B 1 339 ? 25.264 -13.573 27.827  1.00 41.97  ? 339 GLY   B N   1 
ATOM   5468 C CA  . GLY   B 1 339 ? 26.125 -13.400 28.989  1.00 41.68  ? 339 GLY   B CA  1 
ATOM   5469 C C   . GLY   B 1 339 ? 25.711 -14.316 30.124  1.00 45.93  ? 339 GLY   B C   1 
ATOM   5470 O O   . GLY   B 1 339 ? 26.542 -15.059 30.644  1.00 45.38  ? 339 GLY   B O   1 
ATOM   5471 N N   . LEU   B 1 340 ? 24.404 -14.297 30.487  1.00 43.57  ? 340 LEU   B N   1 
ATOM   5472 C CA  . LEU   B 1 340 ? 23.830 -15.139 31.550  1.00 43.12  ? 340 LEU   B CA  1 
ATOM   5473 C C   . LEU   B 1 340 ? 23.918 -16.630 31.219  1.00 48.44  ? 340 LEU   B C   1 
ATOM   5474 O O   . LEU   B 1 340 ? 24.163 -17.431 32.127  1.00 48.18  ? 340 LEU   B O   1 
ATOM   5475 C CB  . LEU   B 1 340 ? 22.392 -14.740 31.905  1.00 42.37  ? 340 LEU   B CB  1 
ATOM   5476 C CG  . LEU   B 1 340 ? 22.164 -13.352 32.514  1.00 44.80  ? 340 LEU   B CG  1 
ATOM   5477 C CD1 . LEU   B 1 340 ? 20.689 -13.091 32.683  1.00 43.81  ? 340 LEU   B CD1 1 
ATOM   5478 C CD2 . LEU   B 1 340 ? 22.891 -13.185 33.843  1.00 45.54  ? 340 LEU   B CD2 1 
ATOM   5479 N N   . ALA   B 1 341 ? 23.763 -16.996 29.917  1.00 45.54  ? 341 ALA   B N   1 
ATOM   5480 C CA  . ALA   B 1 341 ? 23.878 -18.388 29.448  1.00 45.63  ? 341 ALA   B CA  1 
ATOM   5481 C C   . ALA   B 1 341 ? 25.316 -18.887 29.630  1.00 50.07  ? 341 ALA   B C   1 
ATOM   5482 O O   . ALA   B 1 341 ? 25.530 -20.050 29.978  1.00 50.29  ? 341 ALA   B O   1 
ATOM   5483 C CB  . ALA   B 1 341 ? 23.472 -18.504 27.989  1.00 46.04  ? 341 ALA   B CB  1 
ATOM   5484 N N   . HIS   B 1 342 ? 26.297 -18.000 29.416  1.00 46.28  ? 342 HIS   B N   1 
ATOM   5485 C CA  . HIS   B 1 342 ? 27.696 -18.359 29.590  1.00 45.70  ? 342 HIS   B CA  1 
ATOM   5486 C C   . HIS   B 1 342 ? 28.007 -18.498 31.090  1.00 51.00  ? 342 HIS   B C   1 
ATOM   5487 O O   . HIS   B 1 342 ? 28.718 -19.434 31.477  1.00 52.05  ? 342 HIS   B O   1 
ATOM   5488 C CB  . HIS   B 1 342 ? 28.604 -17.336 28.916  1.00 45.63  ? 342 HIS   B CB  1 
ATOM   5489 C CG  . HIS   B 1 342 ? 30.041 -17.717 28.998  1.00 48.38  ? 342 HIS   B CG  1 
ATOM   5490 N ND1 . HIS   B 1 342 ? 30.583 -18.655 28.150  1.00 49.87  ? 342 HIS   B ND1 1 
ATOM   5491 C CD2 . HIS   B 1 342 ? 30.997 -17.291 29.854  1.00 49.51  ? 342 HIS   B CD2 1 
ATOM   5492 C CE1 . HIS   B 1 342 ? 31.852 -18.759 28.502  1.00 49.11  ? 342 HIS   B CE1 1 
ATOM   5493 N NE2 . HIS   B 1 342 ? 32.144 -17.948 29.517  1.00 49.29  ? 342 HIS   B NE2 1 
ATOM   5494 N N   . ARG   B 1 343 ? 27.445 -17.589 31.930  1.00 45.50  ? 343 ARG   B N   1 
ATOM   5495 C CA  . ARG   B 1 343 ? 27.605 -17.620 33.385  1.00 44.97  ? 343 ARG   B CA  1 
ATOM   5496 C C   . ARG   B 1 343 ? 27.043 -18.947 33.950  1.00 50.07  ? 343 ARG   B C   1 
ATOM   5497 O O   . ARG   B 1 343 ? 27.669 -19.562 34.797  1.00 48.58  ? 343 ARG   B O   1 
ATOM   5498 C CB  . ARG   B 1 343 ? 26.904 -16.410 34.036  1.00 42.34  ? 343 ARG   B CB  1 
ATOM   5499 C CG  . ARG   B 1 343 ? 26.927 -16.402 35.573  1.00 39.87  ? 343 ARG   B CG  1 
ATOM   5500 C CD  . ARG   B 1 343 ? 28.216 -15.876 36.153  1.00 36.23  ? 343 ARG   B CD  1 
ATOM   5501 N NE  . ARG   B 1 343 ? 29.277 -16.882 36.260  1.00 41.57  ? 343 ARG   B NE  1 
ATOM   5502 C CZ  . ARG   B 1 343 ? 30.578 -16.599 36.321  1.00 53.12  ? 343 ARG   B CZ  1 
ATOM   5503 N NH1 . ARG   B 1 343 ? 30.997 -15.343 36.242  1.00 39.95  ? 343 ARG   B NH1 1 
ATOM   5504 N NH2 . ARG   B 1 343 ? 31.471 -17.570 36.443  1.00 40.81  ? 343 ARG   B NH2 1 
ATOM   5505 N N   . ALA   B 1 344 ? 25.870 -19.367 33.459  1.00 49.63  ? 344 ALA   B N   1 
ATOM   5506 C CA  . ALA   B 1 344 ? 25.183 -20.607 33.815  1.00 50.04  ? 344 ALA   B CA  1 
ATOM   5507 C C   . ALA   B 1 344 ? 26.043 -21.823 33.410  1.00 54.35  ? 344 ALA   B C   1 
ATOM   5508 O O   . ALA   B 1 344 ? 26.151 -22.765 34.193  1.00 53.25  ? 344 ALA   B O   1 
ATOM   5509 C CB  . ALA   B 1 344 ? 23.837 -20.664 33.112  1.00 50.58  ? 344 ALA   B CB  1 
ATOM   5510 N N   . LYS   B 1 345 ? 26.667 -21.783 32.199  1.00 51.40  ? 345 LYS   B N   1 
ATOM   5511 C CA  . LYS   B 1 345 ? 27.536 -22.848 31.670  1.00 51.29  ? 345 LYS   B CA  1 
ATOM   5512 C C   . LYS   B 1 345 ? 28.787 -22.996 32.543  1.00 58.10  ? 345 LYS   B C   1 
ATOM   5513 O O   . LYS   B 1 345 ? 29.194 -24.122 32.836  1.00 59.21  ? 345 LYS   B O   1 
ATOM   5514 C CB  . LYS   B 1 345 ? 27.929 -22.563 30.210  1.00 52.82  ? 345 LYS   B CB  1 
ATOM   5515 C CG  . LYS   B 1 345 ? 28.424 -23.788 29.450  1.00 56.21  ? 345 LYS   B CG  1 
ATOM   5516 C CD  . LYS   B 1 345 ? 29.004 -23.426 28.096  1.00 59.26  ? 345 LYS   B CD  1 
ATOM   5517 N N   . LEU   B 1 346 ? 29.373 -21.864 32.983  1.00 54.78  ? 346 LEU   B N   1 
ATOM   5518 C CA  . LEU   B 1 346 ? 30.560 -21.856 33.832  1.00 53.92  ? 346 LEU   B CA  1 
ATOM   5519 C C   . LEU   B 1 346 ? 30.290 -22.366 35.238  1.00 58.43  ? 346 LEU   B C   1 
ATOM   5520 O O   . LEU   B 1 346 ? 31.162 -23.001 35.825  1.00 59.47  ? 346 LEU   B O   1 
ATOM   5521 C CB  . LEU   B 1 346 ? 31.179 -20.448 33.909  1.00 53.65  ? 346 LEU   B CB  1 
ATOM   5522 C CG  . LEU   B 1 346 ? 31.953 -19.924 32.686  1.00 57.53  ? 346 LEU   B CG  1 
ATOM   5523 C CD1 . LEU   B 1 346 ? 32.531 -18.559 32.976  1.00 57.04  ? 346 LEU   B CD1 1 
ATOM   5524 C CD2 . LEU   B 1 346 ? 33.104 -20.848 32.302  1.00 57.70  ? 346 LEU   B CD2 1 
ATOM   5525 N N   . ASP   B 1 347 ? 29.105 -22.081 35.785  1.00 54.94  ? 347 ASP   B N   1 
ATOM   5526 C CA  . ASP   B 1 347 ? 28.733 -22.462 37.154  1.00 54.79  ? 347 ASP   B CA  1 
ATOM   5527 C C   . ASP   B 1 347 ? 27.830 -23.710 37.288  1.00 60.22  ? 347 ASP   B C   1 
ATOM   5528 O O   . ASP   B 1 347 ? 27.463 -24.067 38.419  1.00 60.38  ? 347 ASP   B O   1 
ATOM   5529 C CB  . ASP   B 1 347 ? 28.079 -21.249 37.880  1.00 55.75  ? 347 ASP   B CB  1 
ATOM   5530 C CG  . ASP   B 1 347 ? 28.856 -19.942 37.852  1.00 62.09  ? 347 ASP   B CG  1 
ATOM   5531 O OD1 . ASP   B 1 347 ? 29.972 -19.925 37.299  1.00 62.15  ? 347 ASP   B OD1 1 
ATOM   5532 O OD2 . ASP   B 1 347 ? 28.343 -18.936 38.384  1.00 68.75  ? 347 ASP   B OD2 1 
ATOM   5533 N N   . ASN   B 1 348 ? 27.471 -24.363 36.160  1.00 57.07  ? 348 ASN   B N   1 
ATOM   5534 C CA  . ASN   B 1 348 ? 26.570 -25.522 36.122  1.00 57.58  ? 348 ASN   B CA  1 
ATOM   5535 C C   . ASN   B 1 348 ? 25.292 -25.159 36.894  1.00 63.18  ? 348 ASN   B C   1 
ATOM   5536 O O   . ASN   B 1 348 ? 24.885 -25.848 37.837  1.00 64.92  ? 348 ASN   B O   1 
ATOM   5537 C CB  . ASN   B 1 348 ? 27.253 -26.813 36.616  1.00 61.15  ? 348 ASN   B CB  1 
ATOM   5538 C CG  . ASN   B 1 348 ? 28.254 -27.365 35.624  1.00 99.55  ? 348 ASN   B CG  1 
ATOM   5539 O OD1 . ASN   B 1 348 ? 27.918 -27.715 34.480  1.00 99.72  ? 348 ASN   B OD1 1 
ATOM   5540 N ND2 . ASN   B 1 348 ? 29.511 -27.455 36.037  1.00 91.44  ? 348 ASN   B ND2 1 
ATOM   5541 N N   . ASN   B 1 349 ? 24.706 -24.012 36.504  1.00 58.04  ? 349 ASN   B N   1 
ATOM   5542 C CA  . ASN   B 1 349 ? 23.519 -23.405 37.089  1.00 56.69  ? 349 ASN   B CA  1 
ATOM   5543 C C   . ASN   B 1 349 ? 22.349 -23.607 36.133  1.00 59.62  ? 349 ASN   B C   1 
ATOM   5544 O O   . ASN   B 1 349 ? 22.160 -22.835 35.194  1.00 58.92  ? 349 ASN   B O   1 
ATOM   5545 C CB  . ASN   B 1 349 ? 23.805 -21.920 37.374  1.00 53.52  ? 349 ASN   B CB  1 
ATOM   5546 C CG  . ASN   B 1 349 ? 22.753 -21.168 38.154  1.00 62.68  ? 349 ASN   B CG  1 
ATOM   5547 O OD1 . ASN   B 1 349 ? 21.557 -21.503 38.171  1.00 57.56  ? 349 ASN   B OD1 1 
ATOM   5548 N ND2 . ASN   B 1 349 ? 23.186 -20.098 38.799  1.00 47.49  ? 349 ASN   B ND2 1 
ATOM   5549 N N   . LYS   B 1 350 ? 21.580 -24.678 36.372  1.00 56.10  ? 350 LYS   B N   1 
ATOM   5550 C CA  . LYS   B 1 350 ? 20.431 -25.083 35.562  1.00 54.76  ? 350 LYS   B CA  1 
ATOM   5551 C C   . LYS   B 1 350 ? 19.306 -24.052 35.539  1.00 55.00  ? 350 LYS   B C   1 
ATOM   5552 O O   . LYS   B 1 350 ? 18.727 -23.827 34.480  1.00 53.78  ? 350 LYS   B O   1 
ATOM   5553 C CB  . LYS   B 1 350 ? 19.930 -26.481 35.992  1.00 57.39  ? 350 LYS   B CB  1 
ATOM   5554 N N   . GLU   B 1 351 ? 19.007 -23.425 36.697  1.00 50.64  ? 351 GLU   B N   1 
ATOM   5555 C CA  . GLU   B 1 351 ? 17.962 -22.400 36.860  1.00 50.53  ? 351 GLU   B CA  1 
ATOM   5556 C C   . GLU   B 1 351 ? 18.269 -21.157 36.003  1.00 53.64  ? 351 GLU   B C   1 
ATOM   5557 O O   . GLU   B 1 351 ? 17.375 -20.630 35.328  1.00 52.89  ? 351 GLU   B O   1 
ATOM   5558 C CB  . GLU   B 1 351 ? 17.776 -22.009 38.346  1.00 52.08  ? 351 GLU   B CB  1 
ATOM   5559 C CG  . GLU   B 1 351 ? 17.371 -23.146 39.281  1.00 64.71  ? 351 GLU   B CG  1 
ATOM   5560 C CD  . GLU   B 1 351 ? 18.418 -24.202 39.609  1.00 90.29  ? 351 GLU   B CD  1 
ATOM   5561 O OE1 . GLU   B 1 351 ? 18.016 -25.355 39.893  1.00 95.96  ? 351 GLU   B OE1 1 
ATOM   5562 O OE2 . GLU   B 1 351 ? 19.632 -23.888 39.579  1.00 78.55  ? 351 GLU   B OE2 1 
ATOM   5563 N N   . LEU   B 1 352 ? 19.540 -20.701 36.027  1.00 49.32  ? 352 LEU   B N   1 
ATOM   5564 C CA  . LEU   B 1 352 ? 19.970 -19.559 35.236  1.00 48.75  ? 352 LEU   B CA  1 
ATOM   5565 C C   . LEU   B 1 352 ? 19.987 -19.931 33.753  1.00 52.34  ? 352 LEU   B C   1 
ATOM   5566 O O   . LEU   B 1 352 ? 19.553 -19.123 32.927  1.00 54.17  ? 352 LEU   B O   1 
ATOM   5567 C CB  . LEU   B 1 352 ? 21.336 -19.055 35.706  1.00 48.71  ? 352 LEU   B CB  1 
ATOM   5568 C CG  . LEU   B 1 352 ? 21.831 -17.721 35.115  1.00 52.11  ? 352 LEU   B CG  1 
ATOM   5569 C CD1 . LEU   B 1 352 ? 20.866 -16.560 35.427  1.00 51.57  ? 352 LEU   B CD1 1 
ATOM   5570 C CD2 . LEU   B 1 352 ? 23.262 -17.425 35.570  1.00 50.50  ? 352 LEU   B CD2 1 
ATOM   5571 N N   . ALA   B 1 353 ? 20.449 -21.160 33.418  1.00 45.58  ? 353 ALA   B N   1 
ATOM   5572 C CA  . ALA   B 1 353 ? 20.478 -21.651 32.038  1.00 44.09  ? 353 ALA   B CA  1 
ATOM   5573 C C   . ALA   B 1 353 ? 19.068 -21.672 31.483  1.00 48.02  ? 353 ALA   B C   1 
ATOM   5574 O O   . ALA   B 1 353 ? 18.864 -21.270 30.337  1.00 49.35  ? 353 ALA   B O   1 
ATOM   5575 C CB  . ALA   B 1 353 ? 21.114 -23.037 31.960  1.00 44.27  ? 353 ALA   B CB  1 
ATOM   5576 N N   . PHE   B 1 354 ? 18.088 -22.092 32.307  1.00 44.26  ? 354 PHE   B N   1 
ATOM   5577 C CA  . PHE   B 1 354 ? 16.677 -22.145 31.924  1.00 43.66  ? 354 PHE   B CA  1 
ATOM   5578 C C   . PHE   B 1 354 ? 16.131 -20.731 31.704  1.00 49.55  ? 354 PHE   B C   1 
ATOM   5579 O O   . PHE   B 1 354 ? 15.389 -20.512 30.742  1.00 50.21  ? 354 PHE   B O   1 
ATOM   5580 C CB  . PHE   B 1 354 ? 15.836 -22.889 32.980  1.00 44.75  ? 354 PHE   B CB  1 
ATOM   5581 C CG  . PHE   B 1 354 ? 14.370 -22.963 32.611  1.00 45.97  ? 354 PHE   B CG  1 
ATOM   5582 C CD1 . PHE   B 1 354 ? 13.892 -23.983 31.795  1.00 48.29  ? 354 PHE   B CD1 1 
ATOM   5583 C CD2 . PHE   B 1 354 ? 13.473 -21.991 33.051  1.00 47.78  ? 354 PHE   B CD2 1 
ATOM   5584 C CE1 . PHE   B 1 354 ? 12.542 -24.041 31.437  1.00 48.71  ? 354 PHE   B CE1 1 
ATOM   5585 C CE2 . PHE   B 1 354 ? 12.128 -22.036 32.676  1.00 50.68  ? 354 PHE   B CE2 1 
ATOM   5586 C CZ  . PHE   B 1 354 ? 11.673 -23.063 31.870  1.00 48.88  ? 354 PHE   B CZ  1 
ATOM   5587 N N   . PHE   B 1 355 ? 16.497 -19.780 32.597  1.00 45.62  ? 355 PHE   B N   1 
ATOM   5588 C CA  . PHE   B 1 355 ? 16.070 -18.389 32.503  1.00 44.78  ? 355 PHE   B CA  1 
ATOM   5589 C C   . PHE   B 1 355 ? 16.536 -17.734 31.192  1.00 47.00  ? 355 PHE   B C   1 
ATOM   5590 O O   . PHE   B 1 355 ? 15.700 -17.220 30.432  1.00 45.61  ? 355 PHE   B O   1 
ATOM   5591 C CB  . PHE   B 1 355 ? 16.519 -17.565 33.733  1.00 46.16  ? 355 PHE   B CB  1 
ATOM   5592 C CG  . PHE   B 1 355 ? 16.144 -16.104 33.605  1.00 47.42  ? 355 PHE   B CG  1 
ATOM   5593 C CD1 . PHE   B 1 355 ? 14.853 -15.670 33.897  1.00 49.76  ? 355 PHE   B CD1 1 
ATOM   5594 C CD2 . PHE   B 1 355 ? 17.065 -15.169 33.134  1.00 49.20  ? 355 PHE   B CD2 1 
ATOM   5595 C CE1 . PHE   B 1 355 ? 14.500 -14.326 33.748  1.00 50.21  ? 355 PHE   B CE1 1 
ATOM   5596 C CE2 . PHE   B 1 355 ? 16.703 -13.828 32.969  1.00 51.33  ? 355 PHE   B CE2 1 
ATOM   5597 C CZ  . PHE   B 1 355 ? 15.426 -13.416 33.283  1.00 49.33  ? 355 PHE   B CZ  1 
ATOM   5598 N N   . ALA   B 1 356 ? 17.862 -17.749 30.939  1.00 43.51  ? 356 ALA   B N   1 
ATOM   5599 C CA  . ALA   B 1 356 ? 18.460 -17.148 29.740  1.00 43.95  ? 356 ALA   B CA  1 
ATOM   5600 C C   . ALA   B 1 356 ? 17.758 -17.606 28.460  1.00 47.04  ? 356 ALA   B C   1 
ATOM   5601 O O   . ALA   B 1 356 ? 17.372 -16.779 27.645  1.00 47.23  ? 356 ALA   B O   1 
ATOM   5602 C CB  . ALA   B 1 356 ? 19.952 -17.453 29.678  1.00 44.88  ? 356 ALA   B CB  1 
ATOM   5603 N N   . ASN   B 1 357 ? 17.524 -18.908 28.328  1.00 43.10  ? 357 ASN   B N   1 
ATOM   5604 C CA  . ASN   B 1 357 ? 16.844 -19.478 27.172  1.00 42.72  ? 357 ASN   B CA  1 
ATOM   5605 C C   . ASN   B 1 357 ? 15.369 -19.104 27.139  1.00 46.05  ? 357 ASN   B C   1 
ATOM   5606 O O   . ASN   B 1 357 ? 14.862 -18.794 26.058  1.00 46.41  ? 357 ASN   B O   1 
ATOM   5607 C CB  . ASN   B 1 357 ? 17.050 -21.001 27.116  1.00 43.06  ? 357 ASN   B CB  1 
ATOM   5608 C CG  . ASN   B 1 357 ? 16.384 -21.616 25.930  1.00 61.49  ? 357 ASN   B CG  1 
ATOM   5609 O OD1 . ASN   B 1 357 ? 15.345 -22.271 26.062  1.00 59.14  ? 357 ASN   B OD1 1 
ATOM   5610 N ND2 . ASN   B 1 357 ? 16.946 -21.389 24.744  1.00 50.13  ? 357 ASN   B ND2 1 
ATOM   5611 N N   . ALA   B 1 358 ? 14.678 -19.121 28.307  1.00 42.01  ? 358 ALA   B N   1 
ATOM   5612 C CA  . ALA   B 1 358 ? 13.253 -18.751 28.380  1.00 42.09  ? 358 ALA   B CA  1 
ATOM   5613 C C   . ALA   B 1 358 ? 13.023 -17.301 27.923  1.00 47.80  ? 358 ALA   B C   1 
ATOM   5614 O O   . ALA   B 1 358 ? 12.057 -17.051 27.196  1.00 48.60  ? 358 ALA   B O   1 
ATOM   5615 C CB  . ALA   B 1 358 ? 12.700 -18.961 29.782  1.00 42.37  ? 358 ALA   B CB  1 
ATOM   5616 N N   . LEU   B 1 359 ? 13.926 -16.365 28.326  1.00 43.53  ? 359 LEU   B N   1 
ATOM   5617 C CA  . LEU   B 1 359 ? 13.871 -14.946 27.947  1.00 43.16  ? 359 LEU   B CA  1 
ATOM   5618 C C   . LEU   B 1 359 ? 14.104 -14.776 26.430  1.00 47.60  ? 359 LEU   B C   1 
ATOM   5619 O O   . LEU   B 1 359 ? 13.483 -13.901 25.809  1.00 47.80  ? 359 LEU   B O   1 
ATOM   5620 C CB  . LEU   B 1 359 ? 14.830 -14.073 28.820  1.00 42.67  ? 359 LEU   B CB  1 
ATOM   5621 C CG  . LEU   B 1 359 ? 14.856 -12.542 28.589  1.00 47.06  ? 359 LEU   B CG  1 
ATOM   5622 C CD1 . LEU   B 1 359 ? 13.448 -11.906 28.575  1.00 46.80  ? 359 LEU   B CD1 1 
ATOM   5623 C CD2 . LEU   B 1 359 ? 15.745 -11.849 29.596  1.00 48.84  ? 359 LEU   B CD2 1 
ATOM   5624 N N   . GLU   B 1 360 ? 14.968 -15.635 25.833  1.00 43.36  ? 360 GLU   B N   1 
ATOM   5625 C CA  . GLU   B 1 360 ? 15.235 -15.624 24.390  1.00 42.74  ? 360 GLU   B CA  1 
ATOM   5626 C C   . GLU   B 1 360 ? 13.982 -16.084 23.648  1.00 47.83  ? 360 GLU   B C   1 
ATOM   5627 O O   . GLU   B 1 360 ? 13.608 -15.456 22.666  1.00 48.66  ? 360 GLU   B O   1 
ATOM   5628 C CB  . GLU   B 1 360 ? 16.402 -16.544 24.032  1.00 43.92  ? 360 GLU   B CB  1 
ATOM   5629 C CG  . GLU   B 1 360 ? 17.757 -15.992 24.421  1.00 47.58  ? 360 GLU   B CG  1 
ATOM   5630 C CD  . GLU   B 1 360 ? 18.966 -16.662 23.798  1.00 61.42  ? 360 GLU   B CD  1 
ATOM   5631 O OE1 . GLU   B 1 360 ? 18.795 -17.583 22.963  1.00 54.78  ? 360 GLU   B OE1 1 
ATOM   5632 O OE2 . GLU   B 1 360 ? 20.097 -16.251 24.145  1.00 58.08  ? 360 GLU   B OE2 1 
ATOM   5633 N N   . GLU   B 1 361 ? 13.318 -17.162 24.137  1.00 44.11  ? 361 GLU   B N   1 
ATOM   5634 C CA  . GLU   B 1 361 ? 12.085 -17.704 23.557  1.00 43.55  ? 361 GLU   B CA  1 
ATOM   5635 C C   . GLU   B 1 361 ? 10.937 -16.684 23.608  1.00 47.98  ? 361 GLU   B C   1 
ATOM   5636 O O   . GLU   B 1 361 ? 10.244 -16.492 22.603  1.00 48.48  ? 361 GLU   B O   1 
ATOM   5637 C CB  . GLU   B 1 361 ? 11.673 -18.988 24.275  1.00 44.81  ? 361 GLU   B CB  1 
ATOM   5638 C CG  . GLU   B 1 361 ? 12.527 -20.195 23.934  1.00 50.82  ? 361 GLU   B CG  1 
ATOM   5639 C CD  . GLU   B 1 361 ? 12.209 -21.460 24.711  1.00 75.62  ? 361 GLU   B CD  1 
ATOM   5640 O OE1 . GLU   B 1 361 ? 11.559 -21.373 25.781  1.00 66.72  ? 361 GLU   B OE1 1 
ATOM   5641 O OE2 . GLU   B 1 361 ? 12.626 -22.547 24.247  1.00 72.43  ? 361 GLU   B OE2 1 
ATOM   5642 N N   . VAL   B 1 362 ? 10.751 -16.023 24.762  1.00 43.91  ? 362 VAL   B N   1 
ATOM   5643 C CA  . VAL   B 1 362 ? 9.716  -15.004 24.957  1.00 44.03  ? 362 VAL   B CA  1 
ATOM   5644 C C   . VAL   B 1 362 ? 9.872  -13.833 23.970  1.00 47.70  ? 362 VAL   B C   1 
ATOM   5645 O O   . VAL   B 1 362 ? 8.871  -13.319 23.459  1.00 47.45  ? 362 VAL   B O   1 
ATOM   5646 C CB  . VAL   B 1 362 ? 9.634  -14.536 26.430  1.00 47.84  ? 362 VAL   B CB  1 
ATOM   5647 C CG1 . VAL   B 1 362 ? 8.900  -13.206 26.567  1.00 48.09  ? 362 VAL   B CG1 1 
ATOM   5648 C CG2 . VAL   B 1 362 ? 8.954  -15.582 27.280  1.00 47.64  ? 362 VAL   B CG2 1 
ATOM   5649 N N   . SER   B 1 363 ? 11.129 -13.440 23.696  1.00 43.09  ? 363 SER   B N   1 
ATOM   5650 C CA  . SER   B 1 363 ? 11.470 -12.340 22.790  1.00 41.19  ? 363 SER   B CA  1 
ATOM   5651 C C   . SER   B 1 363 ? 11.071 -12.694 21.391  1.00 43.70  ? 363 SER   B C   1 
ATOM   5652 O O   . SER   B 1 363 ? 10.416 -11.889 20.753  1.00 42.76  ? 363 SER   B O   1 
ATOM   5653 C CB  . SER   B 1 363 ? 12.958 -11.997 22.876  1.00 41.39  ? 363 SER   B CB  1 
ATOM   5654 O OG  . SER   B 1 363 ? 13.319 -11.708 24.217  1.00 44.25  ? 363 SER   B OG  1 
ATOM   5655 N N   . ILE   B 1 364 ? 11.426 -13.910 20.923  1.00 42.03  ? 364 ILE   B N   1 
ATOM   5656 C CA  . ILE   B 1 364 ? 11.088 -14.389 19.575  1.00 42.66  ? 364 ILE   B CA  1 
ATOM   5657 C C   . ILE   B 1 364 ? 9.558  -14.559 19.393  1.00 46.62  ? 364 ILE   B C   1 
ATOM   5658 O O   . ILE   B 1 364 ? 8.989  -13.982 18.465  1.00 45.34  ? 364 ILE   B O   1 
ATOM   5659 C CB  . ILE   B 1 364 ? 11.949 -15.612 19.145  1.00 45.85  ? 364 ILE   B CB  1 
ATOM   5660 C CG1 . ILE   B 1 364 ? 13.459 -15.223 19.124  1.00 46.25  ? 364 ILE   B CG1 1 
ATOM   5661 C CG2 . ILE   B 1 364 ? 11.520 -16.122 17.755  1.00 46.58  ? 364 ILE   B CG2 1 
ATOM   5662 C CD1 . ILE   B 1 364 ? 14.459 -16.394 19.305  1.00 46.46  ? 364 ILE   B CD1 1 
ATOM   5663 N N   . GLU   B 1 365 ? 8.914  -15.303 20.313  1.00 44.65  ? 365 GLU   B N   1 
ATOM   5664 C CA  . GLU   B 1 365 ? 7.469  -15.585 20.365  1.00 44.75  ? 365 GLU   B CA  1 
ATOM   5665 C C   . GLU   B 1 365 ? 6.606  -14.345 20.307  1.00 49.92  ? 365 GLU   B C   1 
ATOM   5666 O O   . GLU   B 1 365 ? 5.623  -14.355 19.574  1.00 51.29  ? 365 GLU   B O   1 
ATOM   5667 C CB  . GLU   B 1 365 ? 7.118  -16.410 21.622  1.00 46.01  ? 365 GLU   B CB  1 
ATOM   5668 C CG  . GLU   B 1 365 ? 7.456  -17.887 21.489  1.00 52.36  ? 365 GLU   B CG  1 
ATOM   5669 C CD  . GLU   B 1 365 ? 7.819  -18.651 22.746  1.00 75.50  ? 365 GLU   B CD  1 
ATOM   5670 O OE1 . GLU   B 1 365 ? 7.355  -18.277 23.849  1.00 64.84  ? 365 GLU   B OE1 1 
ATOM   5671 O OE2 . GLU   B 1 365 ? 8.569  -19.646 22.616  1.00 78.21  ? 365 GLU   B OE2 1 
ATOM   5672 N N   . THR   B 1 366 ? 6.962  -13.277 21.071  1.00 46.36  ? 366 THR   B N   1 
ATOM   5673 C CA  . THR   B 1 366 ? 6.232  -11.995 21.103  1.00 45.55  ? 366 THR   B CA  1 
ATOM   5674 C C   . THR   B 1 366 ? 6.231  -11.364 19.709  1.00 48.91  ? 366 THR   B C   1 
ATOM   5675 O O   . THR   B 1 366 ? 5.171  -10.965 19.223  1.00 49.52  ? 366 THR   B O   1 
ATOM   5676 C CB  . THR   B 1 366 ? 6.797  -11.058 22.200  1.00 51.61  ? 366 THR   B CB  1 
ATOM   5677 O OG1 . THR   B 1 366 ? 6.699  -11.713 23.459  1.00 46.17  ? 366 THR   B OG1 1 
ATOM   5678 C CG2 . THR   B 1 366 ? 6.065  -9.714  22.281  1.00 51.60  ? 366 THR   B CG2 1 
ATOM   5679 N N   . ILE   B 1 367 ? 7.411  -11.291 19.063  1.00 44.58  ? 367 ILE   B N   1 
ATOM   5680 C CA  . ILE   B 1 367 ? 7.522  -10.741 17.709  1.00 44.14  ? 367 ILE   B CA  1 
ATOM   5681 C C   . ILE   B 1 367 ? 6.693  -11.605 16.735  1.00 50.86  ? 367 ILE   B C   1 
ATOM   5682 O O   . ILE   B 1 367 ? 5.873  -11.062 15.982  1.00 51.72  ? 367 ILE   B O   1 
ATOM   5683 C CB  . ILE   B 1 367 ? 8.996  -10.523 17.258  1.00 45.77  ? 367 ILE   B CB  1 
ATOM   5684 C CG1 . ILE   B 1 367 ? 9.701  -9.446  18.135  1.00 45.03  ? 367 ILE   B CG1 1 
ATOM   5685 C CG2 . ILE   B 1 367 ? 9.056  -10.149 15.780  1.00 44.04  ? 367 ILE   B CG2 1 
ATOM   5686 C CD1 . ILE   B 1 367 ? 11.227 -9.446  18.073  1.00 45.48  ? 367 ILE   B CD1 1 
ATOM   5687 N N   . GLU   B 1 368 ? 6.877  -12.942 16.787  1.00 47.42  ? 368 GLU   B N   1 
ATOM   5688 C CA  . GLU   B 1 368 ? 6.143  -13.876 15.935  1.00 47.58  ? 368 GLU   B CA  1 
ATOM   5689 C C   . GLU   B 1 368 ? 4.613  -13.775 16.134  1.00 52.05  ? 368 GLU   B C   1 
ATOM   5690 O O   . GLU   B 1 368 ? 3.864  -13.980 15.179  1.00 52.71  ? 368 GLU   B O   1 
ATOM   5691 C CB  . GLU   B 1 368 ? 6.694  -15.305 16.050  1.00 48.91  ? 368 GLU   B CB  1 
ATOM   5692 C CG  . GLU   B 1 368 ? 8.026  -15.496 15.328  1.00 55.96  ? 368 GLU   B CG  1 
ATOM   5693 C CD  . GLU   B 1 368 ? 8.792  -16.785 15.599  1.00 69.75  ? 368 GLU   B CD  1 
ATOM   5694 O OE1 . GLU   B 1 368 ? 8.399  -17.526 16.528  1.00 62.42  ? 368 GLU   B OE1 1 
ATOM   5695 O OE2 . GLU   B 1 368 ? 9.798  -17.048 14.894  1.00 52.43  ? 368 GLU   B OE2 1 
ATOM   5696 N N   . ALA   B 1 369 ? 4.160  -13.365 17.334  1.00 47.80  ? 369 ALA   B N   1 
ATOM   5697 C CA  . ALA   B 1 369 ? 2.735  -13.165 17.639  1.00 47.47  ? 369 ALA   B CA  1 
ATOM   5698 C C   . ALA   B 1 369 ? 2.160  -11.846 17.062  1.00 52.70  ? 369 ALA   B C   1 
ATOM   5699 O O   . ALA   B 1 369 ? 0.968  -11.593 17.212  1.00 53.52  ? 369 ALA   B O   1 
ATOM   5700 C CB  . ALA   B 1 369 ? 2.495  -13.230 19.142  1.00 47.73  ? 369 ALA   B CB  1 
ATOM   5701 N N   . GLY   B 1 370 ? 3.004  -11.037 16.419  1.00 49.06  ? 370 GLY   B N   1 
ATOM   5702 C CA  . GLY   B 1 370 ? 2.631  -9.758  15.809  1.00 48.38  ? 370 GLY   B CA  1 
ATOM   5703 C C   . GLY   B 1 370 ? 2.906  -8.511  16.637  1.00 52.42  ? 370 GLY   B C   1 
ATOM   5704 O O   . GLY   B 1 370 ? 2.511  -7.415  16.238  1.00 51.98  ? 370 GLY   B O   1 
ATOM   5705 N N   . PHE   B 1 371 ? 3.575  -8.652  17.803  1.00 49.50  ? 371 PHE   B N   1 
ATOM   5706 C CA  . PHE   B 1 371 ? 3.900  -7.516  18.686  1.00 48.70  ? 371 PHE   B CA  1 
ATOM   5707 C C   . PHE   B 1 371 ? 5.352  -7.101  18.469  1.00 50.70  ? 371 PHE   B C   1 
ATOM   5708 O O   . PHE   B 1 371 ? 6.274  -7.846  18.790  1.00 49.80  ? 371 PHE   B O   1 
ATOM   5709 C CB  . PHE   B 1 371 ? 3.619  -7.851  20.155  1.00 50.07  ? 371 PHE   B CB  1 
ATOM   5710 C CG  . PHE   B 1 371 ? 2.223  -8.367  20.393  1.00 51.27  ? 371 PHE   B CG  1 
ATOM   5711 C CD1 . PHE   B 1 371 ? 1.987  -9.728  20.559  1.00 53.92  ? 371 PHE   B CD1 1 
ATOM   5712 C CD2 . PHE   B 1 371 ? 1.141  -7.492  20.456  1.00 52.63  ? 371 PHE   B CD2 1 
ATOM   5713 C CE1 . PHE   B 1 371 ? 0.696  -10.204 20.793  1.00 54.39  ? 371 PHE   B CE1 1 
ATOM   5714 C CE2 . PHE   B 1 371 ? -0.150 -7.968  20.690  1.00 55.13  ? 371 PHE   B CE2 1 
ATOM   5715 C CZ  . PHE   B 1 371 ? -0.362 -9.321  20.859  1.00 53.28  ? 371 PHE   B CZ  1 
ATOM   5716 N N   . MET   B 1 372 ? 5.550  -5.928  17.893  1.00 46.22  ? 372 MET   B N   1 
ATOM   5717 C CA  . MET   B 1 372 ? 6.891  -5.482  17.575  1.00 45.76  ? 372 MET   B CA  1 
ATOM   5718 C C   . MET   B 1 372 ? 7.019  -3.969  17.547  1.00 49.08  ? 372 MET   B C   1 
ATOM   5719 O O   . MET   B 1 372 ? 6.006  -3.268  17.544  1.00 48.34  ? 372 MET   B O   1 
ATOM   5720 C CB  . MET   B 1 372 ? 7.279  -6.045  16.196  1.00 47.92  ? 372 MET   B CB  1 
ATOM   5721 C CG  . MET   B 1 372 ? 6.398  -5.540  15.074  1.00 51.11  ? 372 MET   B CG  1 
ATOM   5722 S SD  . MET   B 1 372 ? 6.536  -6.552  13.604  1.00 55.41  ? 372 MET   B SD  1 
ATOM   5723 C CE  . MET   B 1 372 ? 5.726  -8.076  14.196  1.00 52.50  ? 372 MET   B CE  1 
ATOM   5724 N N   . THR   B 1 373 ? 8.281  -3.479  17.491  1.00 44.23  ? 373 THR   B N   1 
ATOM   5725 C CA  . THR   B 1 373 ? 8.618  -2.057  17.414  1.00 43.02  ? 373 THR   B CA  1 
ATOM   5726 C C   . THR   B 1 373 ? 8.534  -1.620  15.942  1.00 46.73  ? 373 THR   B C   1 
ATOM   5727 O O   . THR   B 1 373 ? 8.485  -2.479  15.060  1.00 46.27  ? 373 THR   B O   1 
ATOM   5728 C CB  . THR   B 1 373 ? 9.954  -1.769  18.123  1.00 42.29  ? 373 THR   B CB  1 
ATOM   5729 O OG1 . THR   B 1 373 ? 10.960 -2.617  17.581  1.00 41.65  ? 373 THR   B OG1 1 
ATOM   5730 C CG2 . THR   B 1 373 ? 9.879  -1.988  19.634  1.00 36.03  ? 373 THR   B CG2 1 
ATOM   5731 N N   . LYS   B 1 374 ? 8.493  -0.301  15.685  1.00 43.76  ? 374 LYS   B N   1 
ATOM   5732 C CA  . LYS   B 1 374 ? 8.377  0.297   14.353  1.00 44.23  ? 374 LYS   B CA  1 
ATOM   5733 C C   . LYS   B 1 374 ? 9.330  -0.238  13.284  1.00 47.95  ? 374 LYS   B C   1 
ATOM   5734 O O   . LYS   B 1 374 ? 8.871  -0.538  12.187  1.00 48.30  ? 374 LYS   B O   1 
ATOM   5735 C CB  . LYS   B 1 374 ? 8.407  1.839   14.431  1.00 47.50  ? 374 LYS   B CB  1 
ATOM   5736 C CG  . LYS   B 1 374 ? 7.949  2.544   13.146  1.00 54.58  ? 374 LYS   B CG  1 
ATOM   5737 C CD  . LYS   B 1 374 ? 7.948  4.062   13.287  1.00 60.34  ? 374 LYS   B CD  1 
ATOM   5738 C CE  . LYS   B 1 374 ? 7.200  4.721   12.152  1.00 64.01  ? 374 LYS   B CE  1 
ATOM   5739 N NZ  . LYS   B 1 374 ? 7.756  6.060   11.836  1.00 69.76  ? 374 LYS   B NZ  1 
ATOM   5740 N N   . ASP   B 1 375 ? 10.632 -0.345  13.590  1.00 45.36  ? 375 ASP   B N   1 
ATOM   5741 C CA  . ASP   B 1 375 ? 11.684 -0.843  12.679  1.00 45.41  ? 375 ASP   B CA  1 
ATOM   5742 C C   . ASP   B 1 375 ? 11.361 -2.245  12.086  1.00 50.10  ? 375 ASP   B C   1 
ATOM   5743 O O   . ASP   B 1 375 ? 11.622 -2.489  10.908  1.00 51.12  ? 375 ASP   B O   1 
ATOM   5744 C CB  . ASP   B 1 375 ? 13.053 -0.861  13.393  1.00 47.09  ? 375 ASP   B CB  1 
ATOM   5745 C CG  . ASP   B 1 375 ? 13.130 -1.809  14.583  1.00 65.94  ? 375 ASP   B CG  1 
ATOM   5746 O OD1 . ASP   B 1 375 ? 12.225 -1.745  15.458  1.00 67.14  ? 375 ASP   B OD1 1 
ATOM   5747 O OD2 . ASP   B 1 375 ? 14.098 -2.617  14.643  1.00 72.27  ? 375 ASP   B OD2 1 
ATOM   5748 N N   . LEU   B 1 376 ? 10.791 -3.143  12.903  1.00 45.01  ? 376 LEU   B N   1 
ATOM   5749 C CA  . LEU   B 1 376 ? 10.415 -4.486  12.482  1.00 44.27  ? 376 LEU   B CA  1 
ATOM   5750 C C   . LEU   B 1 376 ? 9.167  -4.448  11.626  1.00 50.22  ? 376 LEU   B C   1 
ATOM   5751 O O   . LEU   B 1 376 ? 9.102  -5.160  10.622  1.00 49.23  ? 376 LEU   B O   1 
ATOM   5752 C CB  . LEU   B 1 376 ? 10.239 -5.416  13.684  1.00 43.53  ? 376 LEU   B CB  1 
ATOM   5753 C CG  . LEU   B 1 376 ? 11.502 -5.718  14.463  1.00 46.91  ? 376 LEU   B CG  1 
ATOM   5754 C CD1 . LEU   B 1 376 ? 11.189 -6.578  15.655  1.00 46.76  ? 376 LEU   B CD1 1 
ATOM   5755 C CD2 . LEU   B 1 376 ? 12.593 -6.322  13.563  1.00 46.08  ? 376 LEU   B CD2 1 
ATOM   5756 N N   . ALA   B 1 377 ? 8.184  -3.593  11.997  1.00 48.73  ? 377 ALA   B N   1 
ATOM   5757 C CA  . ALA   B 1 377 ? 6.955  -3.424  11.217  1.00 49.33  ? 377 ALA   B CA  1 
ATOM   5758 C C   . ALA   B 1 377 ? 7.340  -2.874  9.836   1.00 55.61  ? 377 ALA   B C   1 
ATOM   5759 O O   . ALA   B 1 377 ? 6.783  -3.307  8.817   1.00 55.54  ? 377 ALA   B O   1 
ATOM   5760 C CB  . ALA   B 1 377 ? 5.989  -2.497  11.933  1.00 49.91  ? 377 ALA   B CB  1 
ATOM   5761 N N   . ALA   B 1 378 ? 8.362  -1.983  9.806   1.00 54.02  ? 378 ALA   B N   1 
ATOM   5762 C CA  . ALA   B 1 378 ? 8.921  -1.397  8.575   1.00 54.09  ? 378 ALA   B CA  1 
ATOM   5763 C C   . ALA   B 1 378 ? 9.584  -2.480  7.702   1.00 58.48  ? 378 ALA   B C   1 
ATOM   5764 O O   . ALA   B 1 378 ? 9.496  -2.380  6.487   1.00 58.15  ? 378 ALA   B O   1 
ATOM   5765 C CB  . ALA   B 1 378 ? 9.915  -0.293  8.909   1.00 54.43  ? 378 ALA   B CB  1 
ATOM   5766 N N   . CYS   B 1 379 ? 10.226 -3.513  8.319   1.00 55.59  ? 379 CYS   B N   1 
ATOM   5767 C CA  . CYS   B 1 379 ? 10.853 -4.636  7.603   1.00 56.01  ? 379 CYS   B CA  1 
ATOM   5768 C C   . CYS   B 1 379 ? 9.775  -5.440  6.850   1.00 57.51  ? 379 CYS   B C   1 
ATOM   5769 O O   . CYS   B 1 379 ? 9.973  -5.768  5.686   1.00 56.55  ? 379 CYS   B O   1 
ATOM   5770 C CB  . CYS   B 1 379 ? 11.633 -5.537  8.558   1.00 57.41  ? 379 CYS   B CB  1 
ATOM   5771 S SG  . CYS   B 1 379 ? 13.241 -4.882  9.063   1.00 62.21  ? 379 CYS   B SG  1 
ATOM   5772 N N   . ILE   B 1 380 ? 8.638  -5.743  7.516   1.00 53.22  ? 380 ILE   B N   1 
ATOM   5773 C CA  . ILE   B 1 380 ? 7.519  -6.488  6.933   1.00 52.89  ? 380 ILE   B CA  1 
ATOM   5774 C C   . ILE   B 1 380 ? 6.770  -5.658  5.865   1.00 59.56  ? 380 ILE   B C   1 
ATOM   5775 O O   . ILE   B 1 380 ? 6.936  -5.919  4.674   1.00 59.52  ? 380 ILE   B O   1 
ATOM   5776 C CB  . ILE   B 1 380 ? 6.546  -7.037  8.013   1.00 55.11  ? 380 ILE   B CB  1 
ATOM   5777 C CG1 . ILE   B 1 380 ? 7.279  -7.843  9.103   1.00 54.74  ? 380 ILE   B CG1 1 
ATOM   5778 C CG2 . ILE   B 1 380 ? 5.420  -7.851  7.367   1.00 55.42  ? 380 ILE   B CG2 1 
ATOM   5779 C CD1 . ILE   B 1 380 ? 6.417  -8.158  10.345  1.00 56.13  ? 380 ILE   B CD1 1 
ATOM   5780 N N   . LYS   B 1 381 ? 5.964  -4.656  6.314   1.00 57.15  ? 381 LYS   B N   1 
ATOM   5781 C CA  . LYS   B 1 381 ? 5.097  -3.765  5.531   1.00 56.66  ? 381 LYS   B CA  1 
ATOM   5782 C C   . LYS   B 1 381 ? 5.779  -2.760  4.592   1.00 62.74  ? 381 LYS   B C   1 
ATOM   5783 O O   . LYS   B 1 381 ? 5.231  -2.465  3.528   1.00 63.14  ? 381 LYS   B O   1 
ATOM   5784 C CB  . LYS   B 1 381 ? 4.143  -2.984  6.470   1.00 57.95  ? 381 LYS   B CB  1 
ATOM   5785 C CG  . LYS   B 1 381 ? 3.191  -3.815  7.333   1.00 58.03  ? 381 LYS   B CG  1 
ATOM   5786 N N   . GLY   B 1 382 ? 6.921  -2.212  5.006   1.00 59.72  ? 382 GLY   B N   1 
ATOM   5787 C CA  . GLY   B 1 382 ? 7.627  -1.162  4.274   1.00 58.93  ? 382 GLY   B CA  1 
ATOM   5788 C C   . GLY   B 1 382 ? 7.294  0.163   4.954   1.00 62.93  ? 382 GLY   B C   1 
ATOM   5789 O O   . GLY   B 1 382 ? 6.109  0.501   5.113   1.00 60.85  ? 382 GLY   B O   1 
ATOM   5790 N N   . LEU   B 1 383 ? 8.335  0.913   5.397   1.00 60.44  ? 383 LEU   B N   1 
ATOM   5791 C CA  . LEU   B 1 383 ? 8.199  2.198   6.109   1.00 59.81  ? 383 LEU   B CA  1 
ATOM   5792 C C   . LEU   B 1 383 ? 7.016  3.109   5.694   1.00 65.30  ? 383 LEU   B C   1 
ATOM   5793 O O   . LEU   B 1 383 ? 6.266  3.505   6.592   1.00 65.98  ? 383 LEU   B O   1 
ATOM   5794 C CB  . LEU   B 1 383 ? 9.543  2.948   6.236   1.00 59.28  ? 383 LEU   B CB  1 
ATOM   5795 C CG  . LEU   B 1 383 ? 9.562  4.284   7.015   1.00 63.21  ? 383 LEU   B CG  1 
ATOM   5796 C CD1 . LEU   B 1 383 ? 9.100  4.116   8.467   1.00 63.07  ? 383 LEU   B CD1 1 
ATOM   5797 C CD2 . LEU   B 1 383 ? 10.937 4.924   6.961   1.00 63.50  ? 383 LEU   B CD2 1 
ATOM   5798 N N   . PRO   B 1 384 ? 6.778  3.411   4.383   1.00 61.56  ? 384 PRO   B N   1 
ATOM   5799 C CA  . PRO   B 1 384 ? 5.627  4.269   4.015   1.00 60.77  ? 384 PRO   B CA  1 
ATOM   5800 C C   . PRO   B 1 384 ? 4.237  3.661   4.233   1.00 63.24  ? 384 PRO   B C   1 
ATOM   5801 O O   . PRO   B 1 384 ? 3.248  4.384   4.193   1.00 62.45  ? 384 PRO   B O   1 
ATOM   5802 C CB  . PRO   B 1 384 ? 5.851  4.536   2.520   1.00 62.46  ? 384 PRO   B CB  1 
ATOM   5803 C CG  . PRO   B 1 384 ? 7.269  4.174   2.256   1.00 66.86  ? 384 PRO   B CG  1 
ATOM   5804 C CD  . PRO   B 1 384 ? 7.548  3.043   3.177   1.00 62.82  ? 384 PRO   B CD  1 
ATOM   5805 N N   . ASN   B 1 385 ? 4.156  2.345   4.448   1.00 60.20  ? 385 ASN   B N   1 
ATOM   5806 C CA  . ASN   B 1 385 ? 2.888  1.636   4.661   1.00 59.55  ? 385 ASN   B CA  1 
ATOM   5807 C C   . ASN   B 1 385 ? 2.651  1.305   6.134   1.00 61.97  ? 385 ASN   B C   1 
ATOM   5808 O O   . ASN   B 1 385 ? 1.681  0.604   6.437   1.00 61.93  ? 385 ASN   B O   1 
ATOM   5809 C CB  . ASN   B 1 385 ? 2.840  0.345   3.821   1.00 60.12  ? 385 ASN   B CB  1 
ATOM   5810 C CG  . ASN   B 1 385 ? 3.169  0.526   2.359   1.00 84.37  ? 385 ASN   B CG  1 
ATOM   5811 O OD1 . ASN   B 1 385 ? 4.264  0.184   1.897   1.00 74.96  ? 385 ASN   B OD1 1 
ATOM   5812 N ND2 . ASN   B 1 385 ? 2.224  1.067   1.599   1.00 79.46  ? 385 ASN   B ND2 1 
ATOM   5813 N N   . VAL   B 1 386 ? 3.532  1.791   7.050   1.00 57.04  ? 386 VAL   B N   1 
ATOM   5814 C CA  . VAL   B 1 386 ? 3.427  1.528   8.498   1.00 55.68  ? 386 VAL   B CA  1 
ATOM   5815 C C   . VAL   B 1 386 ? 2.511  2.556   9.174   1.00 58.32  ? 386 VAL   B C   1 
ATOM   5816 O O   . VAL   B 1 386 ? 2.742  3.768   9.062   1.00 59.48  ? 386 VAL   B O   1 
ATOM   5817 C CB  . VAL   B 1 386 ? 4.804  1.400   9.241   1.00 58.63  ? 386 VAL   B CB  1 
ATOM   5818 C CG1 . VAL   B 1 386 ? 4.610  0.995   10.705  1.00 57.89  ? 386 VAL   B CG1 1 
ATOM   5819 C CG2 . VAL   B 1 386 ? 5.740  0.413   8.549   1.00 58.28  ? 386 VAL   B CG2 1 
ATOM   5820 N N   . GLN   B 1 387 ? 1.494  2.062   9.880   1.00 51.95  ? 387 GLN   B N   1 
ATOM   5821 C CA  . GLN   B 1 387 ? 0.543  2.871   10.623  1.00 52.21  ? 387 GLN   B CA  1 
ATOM   5822 C C   . GLN   B 1 387 ? 0.722  2.529   12.112  1.00 58.41  ? 387 GLN   B C   1 
ATOM   5823 O O   . GLN   B 1 387 ? 1.061  1.392   12.431  1.00 59.53  ? 387 GLN   B O   1 
ATOM   5824 C CB  . GLN   B 1 387 ? -0.892 2.578   10.161  1.00 53.31  ? 387 GLN   B CB  1 
ATOM   5825 N N   . ARG   B 1 388 ? 0.495  3.503   13.016  1.00 53.94  ? 388 ARG   B N   1 
ATOM   5826 C CA  . ARG   B 1 388 ? 0.635  3.362   14.468  1.00 52.84  ? 388 ARG   B CA  1 
ATOM   5827 C C   . ARG   B 1 388 ? 0.182  2.015   15.066  1.00 56.07  ? 388 ARG   B C   1 
ATOM   5828 O O   . ARG   B 1 388 ? 0.861  1.488   15.955  1.00 55.65  ? 388 ARG   B O   1 
ATOM   5829 C CB  . ARG   B 1 388 ? 0.048  4.591   15.220  1.00 50.28  ? 388 ARG   B CB  1 
ATOM   5830 C CG  . ARG   B 1 388 ? 0.346  4.655   16.744  1.00 54.33  ? 388 ARG   B CG  1 
ATOM   5831 C CD  . ARG   B 1 388 ? 1.839  4.534   17.115  1.00 48.12  ? 388 ARG   B CD  1 
ATOM   5832 N NE  . ARG   B 1 388 ? 2.026  4.386   18.562  1.00 46.40  ? 388 ARG   B NE  1 
ATOM   5833 C CZ  . ARG   B 1 388 ? 1.977  3.235   19.230  1.00 59.13  ? 388 ARG   B CZ  1 
ATOM   5834 N NH1 . ARG   B 1 388 ? 1.778  2.091   18.585  1.00 49.51  ? 388 ARG   B NH1 1 
ATOM   5835 N NH2 . ARG   B 1 388 ? 2.140  3.219   20.545  1.00 45.26  ? 388 ARG   B NH2 1 
ATOM   5836 N N   . SER   B 1 389 ? -0.929 1.447   14.556  1.00 52.83  ? 389 SER   B N   1 
ATOM   5837 C CA  . SER   B 1 389 ? -1.478 0.164   15.027  1.00 52.52  ? 389 SER   B CA  1 
ATOM   5838 C C   . SER   B 1 389 ? -0.623 -1.063  14.657  1.00 54.76  ? 389 SER   B C   1 
ATOM   5839 O O   . SER   B 1 389 ? -0.808 -2.123  15.257  1.00 55.32  ? 389 SER   B O   1 
ATOM   5840 C CB  . SER   B 1 389 ? -2.929 -0.015  14.572  1.00 55.77  ? 389 SER   B CB  1 
ATOM   5841 O OG  . SER   B 1 389 ? -3.039 -0.199  13.170  1.00 61.99  ? 389 SER   B OG  1 
ATOM   5842 N N   . ASP   B 1 390 ? 0.308  -0.920  13.694  1.00 49.49  ? 390 ASP   B N   1 
ATOM   5843 C CA  . ASP   B 1 390 ? 1.194  -2.005  13.253  1.00 49.91  ? 390 ASP   B CA  1 
ATOM   5844 C C   . ASP   B 1 390 ? 2.351  -2.277  14.219  1.00 55.34  ? 390 ASP   B C   1 
ATOM   5845 O O   . ASP   B 1 390 ? 3.040  -3.297  14.077  1.00 55.25  ? 390 ASP   B O   1 
ATOM   5846 C CB  . ASP   B 1 390 ? 1.744  -1.724  11.840  1.00 51.56  ? 390 ASP   B CB  1 
ATOM   5847 C CG  . ASP   B 1 390 ? 0.669  -1.542  10.787  1.00 62.53  ? 390 ASP   B CG  1 
ATOM   5848 O OD1 . ASP   B 1 390 ? 0.854  -0.691  9.893   1.00 64.14  ? 390 ASP   B OD1 1 
ATOM   5849 O OD2 . ASP   B 1 390 ? -0.366 -2.240  10.867  1.00 69.49  ? 390 ASP   B OD2 1 
ATOM   5850 N N   . TYR   B 1 391 ? 2.572  -1.365  15.194  1.00 51.35  ? 391 TYR   B N   1 
ATOM   5851 C CA  . TYR   B 1 391 ? 3.671  -1.506  16.133  1.00 50.35  ? 391 TYR   B CA  1 
ATOM   5852 C C   . TYR   B 1 391 ? 3.381  -1.105  17.570  1.00 53.41  ? 391 TYR   B C   1 
ATOM   5853 O O   . TYR   B 1 391 ? 2.302  -0.603  17.882  1.00 53.68  ? 391 TYR   B O   1 
ATOM   5854 C CB  . TYR   B 1 391 ? 4.941  -0.809  15.597  1.00 50.63  ? 391 TYR   B CB  1 
ATOM   5855 C CG  . TYR   B 1 391 ? 4.844  0.695   15.447  1.00 51.60  ? 391 TYR   B CG  1 
ATOM   5856 C CD1 . TYR   B 1 391 ? 5.189  1.546   16.496  1.00 53.56  ? 391 TYR   B CD1 1 
ATOM   5857 C CD2 . TYR   B 1 391 ? 4.460  1.270   14.242  1.00 51.83  ? 391 TYR   B CD2 1 
ATOM   5858 C CE1 . TYR   B 1 391 ? 5.123  2.934   16.354  1.00 52.63  ? 391 TYR   B CE1 1 
ATOM   5859 C CE2 . TYR   B 1 391 ? 4.381  2.653   14.092  1.00 52.25  ? 391 TYR   B CE2 1 
ATOM   5860 C CZ  . TYR   B 1 391 ? 4.720  3.482   15.149  1.00 59.11  ? 391 TYR   B CZ  1 
ATOM   5861 O OH  . TYR   B 1 391 ? 4.668  4.847   14.989  1.00 59.70  ? 391 TYR   B OH  1 
ATOM   5862 N N   . LEU   B 1 392 ? 4.376  -1.346  18.442  1.00 48.50  ? 392 LEU   B N   1 
ATOM   5863 C CA  . LEU   B 1 392 ? 4.369  -0.999  19.859  1.00 46.80  ? 392 LEU   B CA  1 
ATOM   5864 C C   . LEU   B 1 392 ? 5.463  0.034   20.109  1.00 48.36  ? 392 LEU   B C   1 
ATOM   5865 O O   . LEU   B 1 392 ? 6.502  -0.012  19.448  1.00 45.86  ? 392 LEU   B O   1 
ATOM   5866 C CB  . LEU   B 1 392 ? 4.617  -2.233  20.744  1.00 46.23  ? 392 LEU   B CB  1 
ATOM   5867 C CG  . LEU   B 1 392 ? 3.511  -3.304  20.820  1.00 50.40  ? 392 LEU   B CG  1 
ATOM   5868 C CD1 . LEU   B 1 392 ? 3.747  -4.234  21.982  1.00 49.26  ? 392 LEU   B CD1 1 
ATOM   5869 C CD2 . LEU   B 1 392 ? 2.130  -2.689  20.969  1.00 52.96  ? 392 LEU   B CD2 1 
ATOM   5870 N N   . ASN   B 1 393 ? 5.240  0.970   21.063  1.00 45.24  ? 393 ASN   B N   1 
ATOM   5871 C CA  . ASN   B 1 393 ? 6.285  1.943   21.408  1.00 44.30  ? 393 ASN   B CA  1 
ATOM   5872 C C   . ASN   B 1 393 ? 7.255  1.239   22.368  1.00 46.83  ? 393 ASN   B C   1 
ATOM   5873 O O   . ASN   B 1 393 ? 6.927  0.158   22.870  1.00 45.57  ? 393 ASN   B O   1 
ATOM   5874 C CB  . ASN   B 1 393 ? 5.722  3.265   21.974  1.00 40.40  ? 393 ASN   B CB  1 
ATOM   5875 C CG  . ASN   B 1 393 ? 5.074  3.225   23.345  1.00 54.49  ? 393 ASN   B CG  1 
ATOM   5876 O OD1 . ASN   B 1 393 ? 5.385  2.404   24.225  1.00 43.92  ? 393 ASN   B OD1 1 
ATOM   5877 N ND2 . ASN   B 1 393 ? 4.158  4.149   23.567  1.00 44.37  ? 393 ASN   B ND2 1 
ATOM   5878 N N   . THR   B 1 394 ? 8.433  1.840   22.617  1.00 43.39  ? 394 THR   B N   1 
ATOM   5879 C CA  . THR   B 1 394 ? 9.489  1.313   23.491  1.00 42.34  ? 394 THR   B CA  1 
ATOM   5880 C C   . THR   B 1 394 ? 8.963  0.670   24.773  1.00 47.54  ? 394 THR   B C   1 
ATOM   5881 O O   . THR   B 1 394 ? 9.306  -0.471  25.078  1.00 48.31  ? 394 THR   B O   1 
ATOM   5882 C CB  . THR   B 1 394 ? 10.524 2.416   23.766  1.00 49.05  ? 394 THR   B CB  1 
ATOM   5883 O OG1 . THR   B 1 394 ? 10.989 2.941   22.524  1.00 54.95  ? 394 THR   B OG1 1 
ATOM   5884 C CG2 . THR   B 1 394 ? 11.706 1.927   24.577  1.00 45.99  ? 394 THR   B CG2 1 
ATOM   5885 N N   . PHE   B 1 395 ? 8.117  1.399   25.510  1.00 45.43  ? 395 PHE   B N   1 
ATOM   5886 C CA  . PHE   B 1 395 ? 7.545  0.964   26.784  1.00 44.67  ? 395 PHE   B CA  1 
ATOM   5887 C C   . PHE   B 1 395 ? 6.481  -0.118  26.605  1.00 49.56  ? 395 PHE   B C   1 
ATOM   5888 O O   . PHE   B 1 395 ? 6.473  -1.097  27.364  1.00 49.45  ? 395 PHE   B O   1 
ATOM   5889 C CB  . PHE   B 1 395 ? 7.037  2.178   27.568  1.00 45.80  ? 395 PHE   B CB  1 
ATOM   5890 C CG  . PHE   B 1 395 ? 8.139  3.162   27.891  1.00 46.35  ? 395 PHE   B CG  1 
ATOM   5891 C CD1 . PHE   B 1 395 ? 8.605  4.057   26.926  1.00 48.57  ? 395 PHE   B CD1 1 
ATOM   5892 C CD2 . PHE   B 1 395 ? 8.721  3.187   29.152  1.00 47.37  ? 395 PHE   B CD2 1 
ATOM   5893 C CE1 . PHE   B 1 395 ? 9.635  4.957   27.220  1.00 49.18  ? 395 PHE   B CE1 1 
ATOM   5894 C CE2 . PHE   B 1 395 ? 9.753  4.090   29.447  1.00 50.03  ? 395 PHE   B CE2 1 
ATOM   5895 C CZ  . PHE   B 1 395 ? 10.204 4.967   28.479  1.00 48.51  ? 395 PHE   B CZ  1 
ATOM   5896 N N   . GLU   B 1 396 ? 5.608  0.030   25.583  1.00 45.71  ? 396 GLU   B N   1 
ATOM   5897 C CA  . GLU   B 1 396 ? 4.557  -0.953  25.287  1.00 44.97  ? 396 GLU   B CA  1 
ATOM   5898 C C   . GLU   B 1 396 ? 5.201  -2.267  24.941  1.00 49.17  ? 396 GLU   B C   1 
ATOM   5899 O O   . GLU   B 1 396 ? 4.766  -3.310  25.442  1.00 51.25  ? 396 GLU   B O   1 
ATOM   5900 C CB  . GLU   B 1 396 ? 3.675  -0.500  24.123  1.00 45.97  ? 396 GLU   B CB  1 
ATOM   5901 C CG  . GLU   B 1 396 ? 2.640  0.549   24.472  1.00 48.70  ? 396 GLU   B CG  1 
ATOM   5902 C CD  . GLU   B 1 396 ? 2.110  1.240   23.235  1.00 67.39  ? 396 GLU   B CD  1 
ATOM   5903 O OE1 . GLU   B 1 396 ? 2.788  1.193   22.181  1.00 45.46  ? 396 GLU   B OE1 1 
ATOM   5904 O OE2 . GLU   B 1 396 ? 1.015  1.835   23.322  1.00 72.64  ? 396 GLU   B OE2 1 
ATOM   5905 N N   . PHE   B 1 397 ? 6.261  -2.223  24.105  1.00 43.09  ? 397 PHE   B N   1 
ATOM   5906 C CA  . PHE   B 1 397 ? 6.976  -3.436  23.739  1.00 42.03  ? 397 PHE   B CA  1 
ATOM   5907 C C   . PHE   B 1 397 ? 7.622  -4.079  24.968  1.00 46.05  ? 397 PHE   B C   1 
ATOM   5908 O O   . PHE   B 1 397 ? 7.401  -5.273  25.187  1.00 46.06  ? 397 PHE   B O   1 
ATOM   5909 C CB  . PHE   B 1 397 ? 7.977  -3.204  22.605  1.00 43.25  ? 397 PHE   B CB  1 
ATOM   5910 C CG  . PHE   B 1 397 ? 8.548  -4.500  22.086  1.00 44.90  ? 397 PHE   B CG  1 
ATOM   5911 C CD1 . PHE   B 1 397 ? 7.739  -5.429  21.438  1.00 47.04  ? 397 PHE   B CD1 1 
ATOM   5912 C CD2 . PHE   B 1 397 ? 9.893  -4.803  22.257  1.00 47.01  ? 397 PHE   B CD2 1 
ATOM   5913 C CE1 . PHE   B 1 397 ? 8.267  -6.637  20.972  1.00 47.55  ? 397 PHE   B CE1 1 
ATOM   5914 C CE2 . PHE   B 1 397 ? 10.419 -6.011  21.779  1.00 49.45  ? 397 PHE   B CE2 1 
ATOM   5915 C CZ  . PHE   B 1 397 ? 9.602  -6.917  21.138  1.00 46.84  ? 397 PHE   B CZ  1 
ATOM   5916 N N   . MET   B 1 398 ? 8.368  -3.290  25.796  1.00 41.87  ? 398 MET   B N   1 
ATOM   5917 C CA  . MET   B 1 398 ? 8.995  -3.805  27.022  1.00 41.84  ? 398 MET   B CA  1 
ATOM   5918 C C   . MET   B 1 398 ? 7.965  -4.409  27.963  1.00 47.02  ? 398 MET   B C   1 
ATOM   5919 O O   . MET   B 1 398 ? 8.236  -5.457  28.547  1.00 47.39  ? 398 MET   B O   1 
ATOM   5920 C CB  . MET   B 1 398 ? 9.819  -2.732  27.753  1.00 44.27  ? 398 MET   B CB  1 
ATOM   5921 C CG  . MET   B 1 398 ? 11.188 -2.443  27.109  1.00 48.00  ? 398 MET   B CG  1 
ATOM   5922 S SD  . MET   B 1 398 ? 12.342 -3.845  27.044  1.00 51.24  ? 398 MET   B SD  1 
ATOM   5923 C CE  . MET   B 1 398 ? 12.452 -4.256  28.722  1.00 47.33  ? 398 MET   B CE  1 
ATOM   5924 N N   . ASP   B 1 399 ? 6.784  -3.765  28.098  1.00 44.83  ? 399 ASP   B N   1 
ATOM   5925 C CA  . ASP   B 1 399 ? 5.680  -4.237  28.949  1.00 45.59  ? 399 ASP   B CA  1 
ATOM   5926 C C   . ASP   B 1 399 ? 5.161  -5.579  28.477  1.00 50.43  ? 399 ASP   B C   1 
ATOM   5927 O O   . ASP   B 1 399 ? 4.941  -6.460  29.318  1.00 51.62  ? 399 ASP   B O   1 
ATOM   5928 C CB  . ASP   B 1 399 ? 4.513  -3.235  28.980  1.00 48.11  ? 399 ASP   B CB  1 
ATOM   5929 C CG  . ASP   B 1 399 ? 4.698  -2.008  29.863  1.00 61.97  ? 399 ASP   B CG  1 
ATOM   5930 O OD1 . ASP   B 1 399 ? 5.498  -2.077  30.826  1.00 60.72  ? 399 ASP   B OD1 1 
ATOM   5931 O OD2 . ASP   B 1 399 ? 4.027  -0.981  29.597  1.00 71.51  ? 399 ASP   B OD2 1 
ATOM   5932 N N   . LYS   B 1 400 ? 4.980  -5.754  27.138  1.00 45.73  ? 400 LYS   B N   1 
ATOM   5933 C CA  . LYS   B 1 400 ? 4.492  -7.024  26.577  1.00 45.02  ? 400 LYS   B CA  1 
ATOM   5934 C C   . LYS   B 1 400 ? 5.469  -8.170  26.826  1.00 50.02  ? 400 LYS   B C   1 
ATOM   5935 O O   . LYS   B 1 400 ? 5.027  -9.283  27.129  1.00 51.13  ? 400 LYS   B O   1 
ATOM   5936 C CB  . LYS   B 1 400 ? 4.098  -6.901  25.091  1.00 45.93  ? 400 LYS   B CB  1 
ATOM   5937 C CG  . LYS   B 1 400 ? 3.278  -8.083  24.565  1.00 53.63  ? 400 LYS   B CG  1 
ATOM   5938 C CD  . LYS   B 1 400 ? 1.797  -7.998  24.956  1.00 63.83  ? 400 LYS   B CD  1 
ATOM   5939 C CE  . LYS   B 1 400 ? 0.963  -9.087  24.324  1.00 68.53  ? 400 LYS   B CE  1 
ATOM   5940 N NZ  . LYS   B 1 400 ? -0.465 -8.685  24.253  1.00 75.98  ? 400 LYS   B NZ  1 
ATOM   5941 N N   . LEU   B 1 401 ? 6.791  -7.887  26.742  1.00 45.57  ? 401 LEU   B N   1 
ATOM   5942 C CA  . LEU   B 1 401 ? 7.846  -8.871  26.991  1.00 44.89  ? 401 LEU   B CA  1 
ATOM   5943 C C   . LEU   B 1 401 ? 7.806  -9.307  28.447  1.00 49.62  ? 401 LEU   B C   1 
ATOM   5944 O O   . LEU   B 1 401 ? 7.833  -10.505 28.714  1.00 50.49  ? 401 LEU   B O   1 
ATOM   5945 C CB  . LEU   B 1 401 ? 9.245  -8.304  26.639  1.00 44.39  ? 401 LEU   B CB  1 
ATOM   5946 C CG  . LEU   B 1 401 ? 9.592  -8.101  25.169  1.00 46.20  ? 401 LEU   B CG  1 
ATOM   5947 C CD1 . LEU   B 1 401 ? 10.941 -7.540  25.047  1.00 45.75  ? 401 LEU   B CD1 1 
ATOM   5948 C CD2 . LEU   B 1 401 ? 9.552  -9.396  24.398  1.00 45.50  ? 401 LEU   B CD2 1 
ATOM   5949 N N   . GLY   B 1 402 ? 7.715  -8.339  29.362  1.00 46.04  ? 402 GLY   B N   1 
ATOM   5950 C CA  . GLY   B 1 402 ? 7.625  -8.585  30.798  1.00 46.31  ? 402 GLY   B CA  1 
ATOM   5951 C C   . GLY   B 1 402 ? 6.418  -9.425  31.187  1.00 52.33  ? 402 GLY   B C   1 
ATOM   5952 O O   . GLY   B 1 402 ? 6.531  -10.301 32.054  1.00 52.94  ? 402 GLY   B O   1 
ATOM   5953 N N   . GLU   B 1 403 ? 5.251  -9.170  30.542  1.00 49.46  ? 403 GLU   B N   1 
ATOM   5954 C CA  . GLU   B 1 403 ? 4.002  -9.912  30.769  1.00 50.37  ? 403 GLU   B CA  1 
ATOM   5955 C C   . GLU   B 1 403 ? 4.200  -11.365 30.325  1.00 55.30  ? 403 GLU   B C   1 
ATOM   5956 O O   . GLU   B 1 403 ? 3.880  -12.296 31.074  1.00 55.54  ? 403 GLU   B O   1 
ATOM   5957 C CB  . GLU   B 1 403 ? 2.843  -9.311  29.953  1.00 52.23  ? 403 GLU   B CB  1 
ATOM   5958 C CG  . GLU   B 1 403 ? 2.149  -8.119  30.592  1.00 71.86  ? 403 GLU   B CG  1 
ATOM   5959 C CD  . GLU   B 1 403 ? 1.198  -7.356  29.681  1.00 101.92 ? 403 GLU   B CD  1 
ATOM   5960 O OE1 . GLU   B 1 403 ? 1.237  -6.102  29.699  1.00 80.03  ? 403 GLU   B OE1 1 
ATOM   5961 O OE2 . GLU   B 1 403 ? 0.417  -8.008  28.947  1.00 104.62 ? 403 GLU   B OE2 1 
ATOM   5962 N N   . ASN   B 1 404 ? 4.743  -11.549 29.099  1.00 51.00  ? 404 ASN   B N   1 
ATOM   5963 C CA  . ASN   B 1 404 ? 4.987  -12.861 28.503  1.00 50.19  ? 404 ASN   B CA  1 
ATOM   5964 C C   . ASN   B 1 404 ? 6.043  -13.682 29.211  1.00 54.48  ? 404 ASN   B C   1 
ATOM   5965 O O   . ASN   B 1 404 ? 5.979  -14.915 29.173  1.00 56.49  ? 404 ASN   B O   1 
ATOM   5966 C CB  . ASN   B 1 404 ? 5.258  -12.740 27.013  1.00 47.41  ? 404 ASN   B CB  1 
ATOM   5967 C CG  . ASN   B 1 404 ? 4.059  -12.353 26.191  1.00 56.36  ? 404 ASN   B CG  1 
ATOM   5968 O OD1 . ASN   B 1 404 ? 4.191  -11.923 25.051  1.00 50.89  ? 404 ASN   B OD1 1 
ATOM   5969 N ND2 . ASN   B 1 404 ? 2.863  -12.501 26.730  1.00 50.67  ? 404 ASN   B ND2 1 
ATOM   5970 N N   . LEU   B 1 405 ? 6.992  -13.008 29.877  1.00 48.88  ? 405 LEU   B N   1 
ATOM   5971 C CA  . LEU   B 1 405 ? 8.049  -13.653 30.642  1.00 47.56  ? 405 LEU   B CA  1 
ATOM   5972 C C   . LEU   B 1 405 ? 7.473  -14.155 31.961  1.00 54.05  ? 405 LEU   B C   1 
ATOM   5973 O O   . LEU   B 1 405 ? 7.823  -15.257 32.385  1.00 54.52  ? 405 LEU   B O   1 
ATOM   5974 C CB  . LEU   B 1 405 ? 9.235  -12.687 30.867  1.00 46.28  ? 405 LEU   B CB  1 
ATOM   5975 C CG  . LEU   B 1 405 ? 10.481 -13.246 31.573  1.00 48.19  ? 405 LEU   B CG  1 
ATOM   5976 C CD1 . LEU   B 1 405 ? 11.129 -14.400 30.778  1.00 47.16  ? 405 LEU   B CD1 1 
ATOM   5977 C CD2 . LEU   B 1 405 ? 11.465 -12.155 31.823  1.00 47.93  ? 405 LEU   B CD2 1 
ATOM   5978 N N   . LYS   B 1 406 ? 6.583  -13.364 32.606  1.00 52.46  ? 406 LYS   B N   1 
ATOM   5979 C CA  . LYS   B 1 406 ? 5.935  -13.753 33.869  1.00 52.70  ? 406 LYS   B CA  1 
ATOM   5980 C C   . LYS   B 1 406 ? 5.168  -15.072 33.651  1.00 55.51  ? 406 LYS   B C   1 
ATOM   5981 O O   . LYS   B 1 406 ? 5.372  -16.028 34.402  1.00 53.74  ? 406 LYS   B O   1 
ATOM   5982 C CB  . LYS   B 1 406 ? 4.996  -12.645 34.375  1.00 55.09  ? 406 LYS   B CB  1 
ATOM   5983 N N   . ILE   B 1 407 ? 4.350  -15.125 32.575  1.00 52.82  ? 407 ILE   B N   1 
ATOM   5984 C CA  . ILE   B 1 407 ? 3.554  -16.289 32.161  1.00 53.29  ? 407 ILE   B CA  1 
ATOM   5985 C C   . ILE   B 1 407 ? 4.466  -17.512 31.918  1.00 60.00  ? 407 ILE   B C   1 
ATOM   5986 O O   . ILE   B 1 407 ? 4.263  -18.542 32.563  1.00 62.14  ? 407 ILE   B O   1 
ATOM   5987 C CB  . ILE   B 1 407 ? 2.633  -15.950 30.941  1.00 56.01  ? 407 ILE   B CB  1 
ATOM   5988 C CG1 . ILE   B 1 407 ? 1.536  -14.930 31.326  1.00 56.10  ? 407 ILE   B CG1 1 
ATOM   5989 C CG2 . ILE   B 1 407 ? 2.015  -17.211 30.335  1.00 56.88  ? 407 ILE   B CG2 1 
ATOM   5990 C CD1 . ILE   B 1 407 ? 0.953  -14.110 30.153  1.00 63.32  ? 407 ILE   B CD1 1 
ATOM   5991 N N   . LYS   B 1 408 ? 5.477  -17.388 31.027  1.00 54.82  ? 408 LYS   B N   1 
ATOM   5992 C CA  . LYS   B 1 408 ? 6.417  -18.462 30.708  1.00 54.06  ? 408 LYS   B CA  1 
ATOM   5993 C C   . LYS   B 1 408 ? 7.170  -18.983 31.935  1.00 60.52  ? 408 LYS   B C   1 
ATOM   5994 O O   . LYS   B 1 408 ? 7.416  -20.189 32.035  1.00 61.65  ? 408 LYS   B O   1 
ATOM   5995 C CB  . LYS   B 1 408 ? 7.381  -18.046 29.570  1.00 55.05  ? 408 LYS   B CB  1 
ATOM   5996 C CG  . LYS   B 1 408 ? 8.450  -19.091 29.214  1.00 55.63  ? 408 LYS   B CG  1 
ATOM   5997 C CD  . LYS   B 1 408 ? 8.834  -19.093 27.738  1.00 64.90  ? 408 LYS   B CD  1 
ATOM   5998 C CE  . LYS   B 1 408 ? 8.284  -20.275 26.979  1.00 73.10  ? 408 LYS   B CE  1 
ATOM   5999 N NZ  . LYS   B 1 408 ? 8.792  -20.325 25.583  1.00 78.10  ? 408 LYS   B NZ  1 
ATOM   6000 N N   . LEU   B 1 409 ? 7.529  -18.093 32.859  1.00 57.87  ? 409 LEU   B N   1 
ATOM   6001 C CA  . LEU   B 1 409 ? 8.251  -18.511 34.056  1.00 58.35  ? 409 LEU   B CA  1 
ATOM   6002 C C   . LEU   B 1 409 ? 7.345  -19.137 35.114  1.00 65.41  ? 409 LEU   B C   1 
ATOM   6003 O O   . LEU   B 1 409 ? 7.754  -20.115 35.748  1.00 65.39  ? 409 LEU   B O   1 
ATOM   6004 C CB  . LEU   B 1 409 ? 9.146  -17.397 34.627  1.00 57.77  ? 409 LEU   B CB  1 
ATOM   6005 C CG  . LEU   B 1 409 ? 10.342 -16.973 33.762  1.00 61.74  ? 409 LEU   B CG  1 
ATOM   6006 C CD1 . LEU   B 1 409 ? 11.104 -15.847 34.423  1.00 61.53  ? 409 LEU   B CD1 1 
ATOM   6007 C CD2 . LEU   B 1 409 ? 11.291 -18.153 33.435  1.00 62.44  ? 409 LEU   B CD2 1 
ATOM   6008 N N   . ALA   B 1 410 ? 6.110  -18.596 35.291  1.00 64.16  ? 410 ALA   B N   1 
ATOM   6009 C CA  . ALA   B 1 410 ? 5.108  -19.115 36.241  1.00 64.82  ? 410 ALA   B CA  1 
ATOM   6010 C C   . ALA   B 1 410 ? 4.757  -20.569 35.855  1.00 71.87  ? 410 ALA   B C   1 
ATOM   6011 O O   . ALA   B 1 410 ? 4.539  -21.407 36.736  1.00 72.51  ? 410 ALA   B O   1 
ATOM   6012 C CB  . ALA   B 1 410 ? 3.857  -18.246 36.222  1.00 65.27  ? 410 ALA   B CB  1 
ATOM   6013 N N   . GLN   B 1 411 ? 4.754  -20.863 34.532  1.00 68.85  ? 411 GLN   B N   1 
ATOM   6014 C CA  . GLN   B 1 411 ? 4.504  -22.182 33.949  1.00 68.87  ? 411 GLN   B CA  1 
ATOM   6015 C C   . GLN   B 1 411 ? 5.826  -23.002 34.020  1.00 74.40  ? 411 GLN   B C   1 
ATOM   6016 O O   . GLN   B 1 411 ? 6.356  -23.451 32.999  1.00 75.53  ? 411 GLN   B O   1 
ATOM   6017 C CB  . GLN   B 1 411 ? 3.973  -22.023 32.503  1.00 69.76  ? 411 GLN   B CB  1 
ATOM   6018 C CG  . GLN   B 1 411 ? 2.571  -21.398 32.429  1.00 71.32  ? 411 GLN   B CG  1 
ATOM   6019 C CD  . GLN   B 1 411 ? 2.120  -20.936 31.052  1.00 85.70  ? 411 GLN   B CD  1 
ATOM   6020 O OE1 . GLN   B 1 411 ? 2.797  -21.104 30.028  1.00 81.54  ? 411 GLN   B OE1 1 
ATOM   6021 N NE2 . GLN   B 1 411 ? 0.940  -20.334 30.998  1.00 73.59  ? 411 GLN   B NE2 1 
ATOM   6022 N N   . ALA   B 1 412 ? 6.355  -23.162 35.251  1.00 70.40  ? 412 ALA   B N   1 
ATOM   6023 C CA  . ALA   B 1 412 ? 7.592  -23.873 35.574  1.00 84.56  ? 412 ALA   B CA  1 
ATOM   6024 C C   . ALA   B 1 412 ? 7.384  -25.380 35.531  1.00 104.16 ? 412 ALA   B C   1 
ATOM   6025 C CB  . ALA   B 1 412 ? 8.078  -23.458 36.955  1.00 85.12  ? 412 ALA   B CB  1 
HETATM 6026 C C32 . A1AI4 C 2 .   ? 31.295 -3.219  -6.273  1.00 62.00  ? 501 A1AI4 A C32 1 
HETATM 6027 C C14 . A1AI4 C 2 .   ? 21.558 0.034   -6.161  1.00 55.51  ? 501 A1AI4 A C14 1 
HETATM 6028 C C18 . A1AI4 C 2 .   ? 26.504 -1.363  -2.728  1.00 75.20  ? 501 A1AI4 A C18 1 
HETATM 6029 C C22 . A1AI4 C 2 .   ? 26.491 -3.701  -2.141  1.00 75.42  ? 501 A1AI4 A C22 1 
HETATM 6030 C C15 . A1AI4 C 2 .   ? 22.168 -1.197  -6.062  1.00 56.70  ? 501 A1AI4 A C15 1 
HETATM 6031 C C19 . A1AI4 C 2 .   ? 27.512 -1.151  -1.817  1.00 77.50  ? 501 A1AI4 A C19 1 
HETATM 6032 C C21 . A1AI4 C 2 .   ? 27.499 -3.464  -1.231  1.00 77.49  ? 501 A1AI4 A C21 1 
HETATM 6033 C C2  . A1AI4 C 2 .   ? 28.978 -1.684  -6.829  1.00 59.05  ? 501 A1AI4 A C2  1 
HETATM 6034 C C3  . A1AI4 C 2 .   ? 27.913 -0.825  -7.000  1.00 57.41  ? 501 A1AI4 A C3  1 
HETATM 6035 C C6  . A1AI4 C 2 .   ? 27.555 -3.145  -5.618  1.00 60.18  ? 501 A1AI4 A C6  1 
HETATM 6036 C C13 . A1AI4 C 2 .   ? 22.358 1.118   -6.441  1.00 53.28  ? 501 A1AI4 A C13 1 
HETATM 6037 C C17 . A1AI4 C 2 .   ? 26.010 -2.642  -2.881  1.00 73.37  ? 501 A1AI4 A C17 1 
HETATM 6038 C C9  . A1AI4 C 2 .   ? 23.539 -1.295  -6.215  1.00 57.16  ? 501 A1AI4 A C9  1 
HETATM 6039 C C20 . A1AI4 C 2 .   ? 28.024 -2.194  -1.062  1.00 79.47  ? 501 A1AI4 A C20 1 
HETATM 6040 C C1  . A1AI4 C 2 .   ? 28.818 -2.864  -6.128  1.00 60.88  ? 501 A1AI4 A C1  1 
HETATM 6041 C C4  . A1AI4 C 2 .   ? 26.659 -1.105  -6.494  1.00 56.63  ? 501 A1AI4 A C4  1 
HETATM 6042 C C5  . A1AI4 C 2 .   ? 26.485 -2.280  -5.771  1.00 59.76  ? 501 A1AI4 A C5  1 
HETATM 6043 C C10 . A1AI4 C 2 .   ? 24.277 -0.146  -6.486  1.00 54.98  ? 501 A1AI4 A C10 1 
HETATM 6044 C C16 . A1AI4 C 2 .   ? 24.943 -2.898  -3.856  1.00 68.52  ? 501 A1AI4 A C16 1 
HETATM 6045 C C8  . A1AI4 C 2 .   ? 24.130 -2.653  -6.113  1.00 57.65  ? 501 A1AI4 A C8  1 
HETATM 6046 C C34 . A1AI4 C 2 .   ? 29.825 -5.083  -6.710  1.00 58.92  ? 501 A1AI4 A C34 1 
HETATM 6047 C C35 . A1AI4 C 2 .   ? 30.079 -4.170  -4.463  1.00 59.71  ? 501 A1AI4 A C35 1 
HETATM 6048 C C24 . A1AI4 C 2 .   ? 30.141 -0.944  -0.543  1.00 81.55  ? 501 A1AI4 A C24 1 
HETATM 6049 C C31 . A1AI4 C 2 .   ? 29.992 -3.802  -5.929  1.00 60.64  ? 501 A1AI4 A C31 1 
HETATM 6050 C C23 . A1AI4 C 2 .   ? 29.123 -1.951  -0.062  1.00 83.08  ? 501 A1AI4 A C23 1 
HETATM 6051 C C26 . A1AI4 C 2 .   ? 28.504 -1.553  1.265   1.00 87.68  ? 501 A1AI4 A C26 1 
HETATM 6052 N N33 . A1AI4 C 2 .   ? 32.337 -2.779  -6.535  1.00 61.92  ? 501 A1AI4 A N33 1 
HETATM 6053 N N12 . A1AI4 C 2 .   ? 23.681 1.051   -6.618  1.00 54.27  ? 501 A1AI4 A N12 1 
HETATM 6054 N N11 . A1AI4 C 2 .   ? 25.672 -0.117  -6.671  1.00 53.33  ? 501 A1AI4 A N11 1 
HETATM 6055 N N7  . A1AI4 C 2 .   ? 25.228 -2.627  -5.199  1.00 62.85  ? 501 A1AI4 A N7  1 
HETATM 6056 O O30 . A1AI4 C 2 .   ? 23.874 -3.327  -3.429  1.00 67.96  ? 501 A1AI4 A O30 1 
HETATM 6057 O O25 . A1AI4 C 2 .   ? 29.890 -3.128  0.136   1.00 84.18  ? 501 A1AI4 A O25 1 
HETATM 6058 F F27 . A1AI4 C 2 .   ? 27.744 -2.579  1.742   1.00 87.38  ? 501 A1AI4 A F27 1 
HETATM 6059 F F28 . A1AI4 C 2 .   ? 27.709 -0.441  1.158   1.00 88.75  ? 501 A1AI4 A F28 1 
HETATM 6060 F F29 . A1AI4 C 2 .   ? 29.464 -1.303  2.197   1.00 90.51  ? 501 A1AI4 A F29 1 
HETATM 6061 P PA  . NAP   D 3 .   ? 28.660 -15.998 -14.206 1.00 87.81  ? 502 NAP   A PA  1 
HETATM 6062 O O1A . NAP   D 3 .   ? 28.780 -14.583 -13.688 1.00 88.22  ? 502 NAP   A O1A 1 
HETATM 6063 O O2A . NAP   D 3 .   ? 28.480 -16.288 -15.640 1.00 88.09  ? 502 NAP   A O2A 1 
HETATM 6064 O O5B . NAP   D 3 .   ? 27.368 -16.690 -13.505 1.00 88.33  ? 502 NAP   A O5B 1 
HETATM 6065 C C5B . NAP   D 3 .   ? 27.349 -17.698 -12.466 1.00 88.73  ? 502 NAP   A C5B 1 
HETATM 6066 C C4B . NAP   D 3 .   ? 25.886 -18.048 -12.186 1.00 88.28  ? 502 NAP   A C4B 1 
HETATM 6067 O O4B . NAP   D 3 .   ? 25.155 -16.819 -11.785 1.00 88.65  ? 502 NAP   A O4B 1 
HETATM 6068 C C3B . NAP   D 3 .   ? 25.199 -18.509 -13.469 1.00 89.17  ? 502 NAP   A C3B 1 
HETATM 6069 O O3B . NAP   D 3 .   ? 25.403 -19.914 -13.692 1.00 89.84  ? 502 NAP   A O3B 1 
HETATM 6070 C C2B . NAP   D 3 .   ? 23.736 -18.154 -13.165 1.00 88.78  ? 502 NAP   A C2B 1 
HETATM 6071 O O2B . NAP   D 3 .   ? 23.200 -19.115 -12.228 1.00 90.57  ? 502 NAP   A O2B 1 
HETATM 6072 C C1B . NAP   D 3 .   ? 23.916 -16.712 -12.597 1.00 88.59  ? 502 NAP   A C1B 1 
HETATM 6073 N N9A . NAP   D 3 .   ? 23.981 -15.591 -13.607 1.00 87.93  ? 502 NAP   A N9A 1 
HETATM 6074 C C8A . NAP   D 3 .   ? 25.100 -14.808 -13.919 1.00 88.66  ? 502 NAP   A C8A 1 
HETATM 6075 N N7A . NAP   D 3 .   ? 24.894 -13.903 -14.856 1.00 89.08  ? 502 NAP   A N7A 1 
HETATM 6076 C C5A . NAP   D 3 .   ? 23.564 -14.067 -15.189 1.00 88.62  ? 502 NAP   A C5A 1 
HETATM 6077 C C6A . NAP   D 3 .   ? 22.735 -13.404 -16.128 1.00 89.58  ? 502 NAP   A C6A 1 
HETATM 6078 N N6A . NAP   D 3 .   ? 23.219 -12.389 -16.924 1.00 90.88  ? 502 NAP   A N6A 1 
HETATM 6079 N N1A . NAP   D 3 .   ? 21.412 -13.798 -16.249 1.00 89.44  ? 502 NAP   A N1A 1 
HETATM 6080 C C2A . NAP   D 3 .   ? 20.929 -14.799 -15.469 1.00 89.10  ? 502 NAP   A C2A 1 
HETATM 6081 N N3A . NAP   D 3 .   ? 21.647 -15.503 -14.542 1.00 88.17  ? 502 NAP   A N3A 1 
HETATM 6082 C C4A . NAP   D 3 .   ? 22.960 -15.102 -14.436 1.00 88.05  ? 502 NAP   A C4A 1 
HETATM 6083 O O3  . NAP   D 3 .   ? 29.847 -16.921 -13.660 1.00 88.25  ? 502 NAP   A O3  1 
HETATM 6084 P PN  . NAP   D 3 .   ? 30.384 -18.417 -13.970 1.00 88.20  ? 502 NAP   A PN  1 
HETATM 6085 O O1N . NAP   D 3 .   ? 31.323 -18.658 -12.790 1.00 88.50  ? 502 NAP   A O1N 1 
HETATM 6086 O O2N . NAP   D 3 .   ? 29.321 -19.416 -14.446 1.00 88.22  ? 502 NAP   A O2N 1 
HETATM 6087 O O5D . NAP   D 3 .   ? 31.217 -18.117 -15.336 1.00 88.27  ? 502 NAP   A O5D 1 
HETATM 6088 C C5D . NAP   D 3 .   ? 31.863 -19.179 -16.032 1.00 88.20  ? 502 NAP   A C5D 1 
HETATM 6089 C C4D . NAP   D 3 .   ? 32.970 -18.613 -16.938 1.00 87.80  ? 502 NAP   A C4D 1 
HETATM 6090 O O4D . NAP   D 3 .   ? 32.865 -17.161 -17.038 1.00 87.87  ? 502 NAP   A O4D 1 
HETATM 6091 C C3D . NAP   D 3 .   ? 34.386 -19.002 -16.459 1.00 88.46  ? 502 NAP   A C3D 1 
HETATM 6092 O O3D . NAP   D 3 .   ? 35.130 -19.947 -17.250 1.00 89.18  ? 502 NAP   A O3D 1 
HETATM 6093 C C2D . NAP   D 3 .   ? 35.054 -17.677 -16.070 1.00 88.74  ? 502 NAP   A C2D 1 
HETATM 6094 O O2D . NAP   D 3 .   ? 36.432 -17.649 -16.494 1.00 89.40  ? 502 NAP   A O2D 1 
HETATM 6095 C C1D . NAP   D 3 .   ? 34.173 -16.610 -16.770 1.00 88.40  ? 502 NAP   A C1D 1 
HETATM 6096 N N1N . NAP   D 3 .   ? 34.085 -15.286 -16.103 1.00 87.18  ? 502 NAP   A N1N 1 
HETATM 6097 C C2N . NAP   D 3 .   ? 34.360 -14.152 -16.916 1.00 87.32  ? 502 NAP   A C2N 1 
HETATM 6098 C C3N . NAP   D 3 .   ? 34.306 -12.867 -16.479 1.00 86.78  ? 502 NAP   A C3N 1 
HETATM 6099 C C7N . NAP   D 3 .   ? 34.603 -11.740 -17.459 1.00 87.58  ? 502 NAP   A C7N 1 
HETATM 6100 O O7N . NAP   D 3 .   ? 34.906 -11.891 -18.652 1.00 87.77  ? 502 NAP   A O7N 1 
HETATM 6101 N N7N . NAP   D 3 .   ? 34.520 -10.468 -16.971 1.00 87.74  ? 502 NAP   A N7N 1 
HETATM 6102 C C4N . NAP   D 3 .   ? 33.941 -12.633 -14.990 1.00 87.23  ? 502 NAP   A C4N 1 
HETATM 6103 C C5N . NAP   D 3 .   ? 33.666 -13.886 -14.136 1.00 87.35  ? 502 NAP   A C5N 1 
HETATM 6104 C C6N . NAP   D 3 .   ? 33.747 -15.108 -14.716 1.00 86.87  ? 502 NAP   A C6N 1 
HETATM 6105 P P2B . NAP   D 3 .   ? 21.739 -19.792 -12.398 1.00 91.45  ? 502 NAP   A P2B 1 
HETATM 6106 O O1X . NAP   D 3 .   ? 20.879 -18.726 -13.091 1.00 91.85  ? 502 NAP   A O1X 1 
HETATM 6107 O O2X . NAP   D 3 .   ? 21.874 -21.137 -13.126 1.00 92.12  ? 502 NAP   A O2X 1 
HETATM 6108 O O3X . NAP   D 3 .   ? 21.465 -19.917 -10.916 1.00 91.37  ? 502 NAP   A O3X 1 
HETATM 6109 C C1  . GOL   E 4 .   ? 15.043 11.500  -31.963 1.00 66.42  ? 503 GOL   A C1  1 
HETATM 6110 O O1  . GOL   E 4 .   ? 14.872 10.979  -33.303 1.00 66.77  ? 503 GOL   A O1  1 
HETATM 6111 C C2  . GOL   E 4 .   ? 16.062 12.648  -31.900 1.00 66.09  ? 503 GOL   A C2  1 
HETATM 6112 O O2  . GOL   E 4 .   ? 15.835 13.457  -30.732 1.00 66.54  ? 503 GOL   A O2  1 
HETATM 6113 C C3  . GOL   E 4 .   ? 17.572 12.203  -31.979 1.00 65.91  ? 503 GOL   A C3  1 
HETATM 6114 O O3  . GOL   E 4 .   ? 18.469 13.349  -31.770 1.00 64.84  ? 503 GOL   A O3  1 
HETATM 6115 C C32 . A1AI4 F 2 .   ? 28.658 -10.139 10.173  1.00 65.51  ? 500 A1AI4 B C32 1 
HETATM 6116 C C14 . A1AI4 F 2 .   ? 19.650 -14.755 8.978   1.00 55.32  ? 500 A1AI4 B C14 1 
HETATM 6117 C C18 . A1AI4 F 2 .   ? 24.880 -12.925 6.095   1.00 69.06  ? 500 A1AI4 B C18 1 
HETATM 6118 C C22 . A1AI4 F 2 .   ? 24.560 -10.729 5.161   1.00 70.72  ? 500 A1AI4 B C22 1 
HETATM 6119 C C15 . A1AI4 F 2 .   ? 20.085 -13.460 8.782   1.00 56.13  ? 500 A1AI4 B C15 1 
HETATM 6120 C C19 . A1AI4 F 2 .   ? 26.021 -13.065 5.335   1.00 72.24  ? 500 A1AI4 B C19 1 
HETATM 6121 C C21 . A1AI4 F 2 .   ? 25.697 -10.892 4.408   1.00 73.83  ? 500 A1AI4 B C21 1 
HETATM 6122 C C2  . A1AI4 F 2 .   ? 26.529 -11.834 10.481  1.00 59.45  ? 500 A1AI4 B C2  1 
HETATM 6123 C C3  . A1AI4 F 2 .   ? 25.566 -12.805 10.634  1.00 58.59  ? 500 A1AI4 B C3  1 
HETATM 6124 C C6  . A1AI4 F 2 .   ? 25.178 -10.762 8.857   1.00 58.84  ? 500 A1AI4 B C6  1 
HETATM 6125 C C13 . A1AI4 F 2 .   ? 20.520 -15.649 9.559   1.00 55.58  ? 500 A1AI4 B C13 1 
HETATM 6126 C C17 . A1AI4 F 2 .   ? 24.167 -11.747 6.001   1.00 68.64  ? 500 A1AI4 B C17 1 
HETATM 6127 C C9  . A1AI4 F 2 .   ? 21.372 -13.110 9.139   1.00 57.35  ? 500 A1AI4 B C9  1 
HETATM 6128 C C20 . A1AI4 F 2 .   ? 26.444 -12.052 4.487   1.00 75.92  ? 500 A1AI4 B C20 1 
HETATM 6129 C C1  . A1AI4 F 2 .   ? 26.356 -10.797 9.588   1.00 60.59  ? 500 A1AI4 B C1  1 
HETATM 6130 C C4  . A1AI4 F 2 .   ? 24.397 -12.766 9.907   1.00 57.62  ? 500 A1AI4 B C4  1 
HETATM 6131 C C5  . A1AI4 F 2 .   ? 24.205 -11.741 8.986   1.00 59.43  ? 500 A1AI4 B C5  1 
HETATM 6132 C C10 . A1AI4 F 2 .   ? 22.197 -14.078 9.704   1.00 58.16  ? 500 A1AI4 B C10 1 
HETATM 6133 C C16 . A1AI4 F 2 .   ? 22.953 -11.502 6.790   1.00 65.85  ? 500 A1AI4 B C16 1 
HETATM 6134 C C8  . A1AI4 F 2 .   ? 21.786 -11.701 8.906   1.00 58.08  ? 500 A1AI4 B C8  1 
HETATM 6135 C C34 . A1AI4 F 2 .   ? 27.012 -8.379  9.867   1.00 62.94  ? 500 A1AI4 B C34 1 
HETATM 6136 C C35 . A1AI4 F 2 .   ? 27.876 -9.710  7.986   1.00 63.28  ? 500 A1AI4 B C35 1 
HETATM 6137 C C24 . A1AI4 F 2 .   ? 28.876 -12.592 4.490   1.00 80.41  ? 500 A1AI4 B C24 1 
HETATM 6138 C C31 . A1AI4 F 2 .   ? 27.452 -9.763  9.439   1.00 63.49  ? 500 A1AI4 B C31 1 
HETATM 6139 C C23 . A1AI4 F 2 .   ? 27.691 -12.162 3.651   1.00 81.04  ? 500 A1AI4 B C23 1 
HETATM 6140 C C26 . A1AI4 F 2 .   ? 27.453 -13.024 2.427   1.00 87.56  ? 500 A1AI4 B C26 1 
HETATM 6141 N N33 . A1AI4 F 2 .   ? 29.614 -10.458 10.748  1.00 68.45  ? 500 A1AI4 B N33 1 
HETATM 6142 N N12 . A1AI4 F 2 .   ? 21.764 -15.333 9.936   1.00 57.37  ? 500 A1AI4 B N12 1 
HETATM 6143 N N11 . A1AI4 F 2 .   ? 23.533 -13.849 10.100  1.00 57.10  ? 500 A1AI4 B N11 1 
HETATM 6144 N N7  . A1AI4 F 2 .   ? 23.023 -11.672 8.182   1.00 61.71  ? 500 A1AI4 B N7  1 
HETATM 6145 O O30 . A1AI4 F 2 .   ? 21.968 -11.127 6.164   1.00 66.17  ? 500 A1AI4 B O30 1 
HETATM 6146 O O25 . A1AI4 F 2 .   ? 28.076 -10.874 3.183   1.00 81.30  ? 500 A1AI4 B O25 1 
HETATM 6147 F F27 . A1AI4 F 2 .   ? 26.399 -12.533 1.712   1.00 89.59  ? 500 A1AI4 B F27 1 
HETATM 6148 F F28 . A1AI4 F 2 .   ? 27.170 -14.320 2.739   1.00 89.11  ? 500 A1AI4 B F28 1 
HETATM 6149 F F29 . A1AI4 F 2 .   ? 28.546 -13.020 1.614   1.00 89.95  ? 500 A1AI4 B F29 1 
HETATM 6150 P PA  . NAP   G 3 .   ? 23.052 3.323   15.635  1.00 72.14  ? 501 NAP   B PA  1 
HETATM 6151 O O1A . NAP   G 3 .   ? 23.357 1.894   15.219  1.00 72.68  ? 501 NAP   B O1A 1 
HETATM 6152 O O2A . NAP   G 3 .   ? 22.843 3.740   17.012  1.00 72.42  ? 501 NAP   B O2A 1 
HETATM 6153 O O5B . NAP   G 3 .   ? 21.670 3.692   14.916  1.00 72.25  ? 501 NAP   B O5B 1 
HETATM 6154 C C5B . NAP   G 3 .   ? 21.598 4.217   13.581  1.00 71.71  ? 501 NAP   B C5B 1 
HETATM 6155 C C4B . NAP   G 3 .   ? 20.142 4.038   13.128  1.00 70.88  ? 501 NAP   B C4B 1 
HETATM 6156 O O4B . NAP   G 3 .   ? 19.858 2.587   12.940  1.00 71.05  ? 501 NAP   B O4B 1 
HETATM 6157 C C3B . NAP   G 3 .   ? 19.084 4.527   14.146  1.00 71.50  ? 501 NAP   B C3B 1 
HETATM 6158 O O3B . NAP   G 3 .   ? 18.847 5.937   14.029  1.00 72.10  ? 501 NAP   B O3B 1 
HETATM 6159 C C2B . NAP   G 3 .   ? 17.882 3.662   13.718  1.00 70.90  ? 501 NAP   B C2B 1 
HETATM 6160 O O2B . NAP   G 3 .   ? 17.392 4.029   12.433  1.00 72.56  ? 501 NAP   B O2B 1 
HETATM 6161 C C1B . NAP   G 3 .   ? 18.562 2.291   13.557  1.00 70.67  ? 501 NAP   B C1B 1 
HETATM 6162 N N9A . NAP   G 3 .   ? 18.688 1.464   14.769  1.00 69.78  ? 501 NAP   B N9A 1 
HETATM 6163 C C8A . NAP   G 3 .   ? 19.845 0.954   15.355  1.00 70.30  ? 501 NAP   B C8A 1 
HETATM 6164 N N7A . NAP   G 3 .   ? 19.584 0.259   16.438  1.00 70.68  ? 501 NAP   B N7A 1 
HETATM 6165 C C5A . NAP   G 3 .   ? 18.198 0.301   16.582  1.00 70.24  ? 501 NAP   B C5A 1 
HETATM 6166 C C6A . NAP   G 3 .   ? 17.272 -0.239  17.536  1.00 71.13  ? 501 NAP   B C6A 1 
HETATM 6167 N N6A . NAP   G 3 .   ? 17.679 -0.992  18.605  1.00 72.30  ? 501 NAP   B N6A 1 
HETATM 6168 N N1A . NAP   G 3 .   ? 15.906 0.011   17.384  1.00 71.04  ? 501 NAP   B N1A 1 
HETATM 6169 C C2A . NAP   G 3 .   ? 15.461 0.749   16.332  1.00 70.68  ? 501 NAP   B C2A 1 
HETATM 6170 N N3A . NAP   G 3 .   ? 16.253 1.314   15.364  1.00 69.83  ? 501 NAP   B N3A 1 
HETATM 6171 C C4A . NAP   G 3 .   ? 17.609 1.054   15.545  1.00 69.79  ? 501 NAP   B C4A 1 
HETATM 6172 O O3  . NAP   G 3 .   ? 24.108 4.312   14.984  1.00 72.76  ? 501 NAP   B O3  1 
HETATM 6173 P PN  . NAP   G 3 .   ? 24.507 5.861   15.055  1.00 72.88  ? 501 NAP   B PN  1 
HETATM 6174 O O1N . NAP   G 3 .   ? 25.591 6.060   14.004  1.00 73.26  ? 501 NAP   B O1N 1 
HETATM 6175 O O2N . NAP   G 3 .   ? 23.271 6.788   15.121  1.00 72.95  ? 501 NAP   B O2N 1 
HETATM 6176 O O5D . NAP   G 3 .   ? 25.322 5.811   16.451  1.00 73.06  ? 501 NAP   B O5D 1 
HETATM 6177 C C5D . NAP   G 3 .   ? 25.283 6.930   17.321  1.00 73.10  ? 501 NAP   B C5D 1 
HETATM 6178 C C4D . NAP   G 3 .   ? 26.300 6.758   18.461  1.00 72.76  ? 501 NAP   B C4D 1 
HETATM 6179 O O4D . NAP   G 3 .   ? 26.432 5.375   18.877  1.00 72.83  ? 501 NAP   B O4D 1 
HETATM 6180 C C3D . NAP   G 3 .   ? 27.681 7.324   18.143  1.00 73.52  ? 501 NAP   B C3D 1 
HETATM 6181 O O3D . NAP   G 3 .   ? 28.068 8.330   19.080  1.00 74.53  ? 501 NAP   B O3D 1 
HETATM 6182 C C2D . NAP   G 3 .   ? 28.595 6.099   17.995  1.00 73.62  ? 501 NAP   B C2D 1 
HETATM 6183 O O2D . NAP   G 3 .   ? 29.930 6.359   18.464  1.00 74.13  ? 501 NAP   B O2D 1 
HETATM 6184 C C1D . NAP   G 3 .   ? 27.851 5.067   18.865  1.00 73.37  ? 501 NAP   B C1D 1 
HETATM 6185 N N1N . NAP   G 3 .   ? 28.101 3.663   18.477  1.00 72.17  ? 501 NAP   B N1N 1 
HETATM 6186 C C2N . NAP   G 3 .   ? 28.417 2.749   19.507  1.00 72.24  ? 501 NAP   B C2N 1 
HETATM 6187 C C3N . NAP   G 3 .   ? 28.654 1.429   19.314  1.00 71.68  ? 501 NAP   B C3N 1 
HETATM 6188 C C7N . NAP   G 3 .   ? 28.977 0.562   20.511  1.00 72.17  ? 501 NAP   B C7N 1 
HETATM 6189 O O7N . NAP   G 3 .   ? 29.058 0.955   21.668  1.00 72.31  ? 501 NAP   B O7N 1 
HETATM 6190 N N7N . NAP   G 3 .   ? 29.192 -0.752  20.244  1.00 72.30  ? 501 NAP   B N7N 1 
HETATM 6191 C C4N . NAP   G 3 .   ? 28.582 0.867   17.859  1.00 72.15  ? 501 NAP   B C4N 1 
HETATM 6192 C C5N . NAP   G 3 .   ? 28.248 1.895   16.768  1.00 72.37  ? 501 NAP   B C5N 1 
HETATM 6193 C C6N . NAP   G 3 .   ? 28.036 3.203   17.122  1.00 71.89  ? 501 NAP   B C6N 1 
HETATM 6194 P P2B . NAP   G 3 .   ? 16.063 4.885   12.216  1.00 73.35  ? 501 NAP   B P2B 1 
HETATM 6195 O O1X . NAP   G 3 .   ? 15.001 4.151   13.058  1.00 73.81  ? 501 NAP   B O1X 1 
HETATM 6196 O O2X . NAP   G 3 .   ? 16.498 6.228   12.680  1.00 74.03  ? 501 NAP   B O2X 1 
HETATM 6197 O O3X . NAP   G 3 .   ? 15.874 4.753   10.708  1.00 73.22  ? 501 NAP   B O3X 1 
HETATM 6198 O O   . HOH   H 5 .   ? 27.403 -21.016 -14.763 1.00 48.24  ? 601 HOH   A O   1 
HETATM 6199 O O   . HOH   H 5 .   ? 36.708 -5.309  -37.898 1.00 39.51  ? 602 HOH   A O   1 
HETATM 6200 O O   . HOH   H 5 .   ? 65.646 -3.541  11.675  1.00 53.68  ? 603 HOH   A O   1 
HETATM 6201 O O   . HOH   H 5 .   ? 2.550  -15.587 -8.482  1.00 49.74  ? 604 HOH   A O   1 
HETATM 6202 O O   . HOH   H 5 .   ? 34.370 8.013   -34.540 1.00 46.19  ? 605 HOH   A O   1 
HETATM 6203 O O   . HOH   H 5 .   ? 18.701 9.084   -32.695 1.00 43.49  ? 606 HOH   A O   1 
HETATM 6204 O O   . HOH   H 5 .   ? 20.738 -6.658  -37.972 1.00 45.95  ? 607 HOH   A O   1 
HETATM 6205 O O   . HOH   H 5 .   ? 29.678 -8.438  -36.037 1.00 34.94  ? 608 HOH   A O   1 
HETATM 6206 O O   . HOH   H 5 .   ? 39.638 -11.267 -34.388 1.00 43.15  ? 609 HOH   A O   1 
HETATM 6207 O O   . HOH   H 5 .   ? 10.723 -18.733 -27.696 1.00 59.35  ? 610 HOH   A O   1 
HETATM 6208 O O   . HOH   H 5 .   ? 19.842 2.591   -13.344 1.00 50.97  ? 611 HOH   A O   1 
HETATM 6209 O O   . HOH   H 5 .   ? 19.493 12.309  -24.918 1.00 41.99  ? 612 HOH   A O   1 
HETATM 6210 O O   . HOH   H 5 .   ? 7.649  -5.696  -7.501  1.00 52.18  ? 613 HOH   A O   1 
HETATM 6211 O O   . HOH   H 5 .   ? 8.518  1.785   -25.697 1.00 58.39  ? 614 HOH   A O   1 
HETATM 6212 O O   . HOH   H 5 .   ? 21.407 3.641   -15.405 1.00 65.12  ? 615 HOH   A O   1 
HETATM 6213 O O   . HOH   H 5 .   ? 30.025 5.538   -39.219 1.00 45.62  ? 616 HOH   A O   1 
HETATM 6214 O O   . HOH   H 5 .   ? 32.945 7.960   -18.425 1.00 51.23  ? 617 HOH   A O   1 
HETATM 6215 O O   . HOH   H 5 .   ? 6.365  -16.475 -21.807 1.00 54.92  ? 618 HOH   A O   1 
HETATM 6216 O O   . HOH   H 5 .   ? 23.633 10.211  -37.990 1.00 42.38  ? 619 HOH   A O   1 
HETATM 6217 O O   . HOH   H 5 .   ? 30.150 -12.590 -29.169 1.00 45.90  ? 620 HOH   A O   1 
HETATM 6218 O O   . HOH   H 5 .   ? 45.585 5.194   -22.258 1.00 67.21  ? 621 HOH   A O   1 
HETATM 6219 O O   . HOH   H 5 .   ? 5.113  -12.383 -18.446 1.00 57.66  ? 622 HOH   A O   1 
HETATM 6220 O O   . HOH   H 5 .   ? 47.291 4.488   -30.181 1.00 56.93  ? 623 HOH   A O   1 
HETATM 6221 O O   . HOH   H 5 .   ? 30.518 9.969   -36.315 1.00 54.32  ? 624 HOH   A O   1 
HETATM 6222 O O   . HOH   H 5 .   ? 26.350 14.945  -27.391 1.00 57.56  ? 625 HOH   A O   1 
HETATM 6223 O O   . HOH   H 5 .   ? 30.282 5.064   -18.089 1.00 62.85  ? 626 HOH   A O   1 
HETATM 6224 O O   . HOH   I 5 .   ? 38.436 3.646   25.835  1.00 38.34  ? 601 HOH   B O   1 
HETATM 6225 O O   . HOH   I 5 .   ? 65.840 -2.817  -0.899  1.00 40.15  ? 602 HOH   B O   1 
HETATM 6226 O O   . HOH   I 5 .   ? 31.626 3.003   21.734  1.00 45.81  ? 603 HOH   B O   1 
HETATM 6227 O O   . HOH   I 5 .   ? 20.718 7.252   15.594  1.00 53.88  ? 604 HOH   B O   1 
HETATM 6228 O O   . HOH   I 5 .   ? 34.137 -16.793 37.014  1.00 47.83  ? 605 HOH   B O   1 
HETATM 6229 O O   . HOH   I 5 .   ? 37.417 0.043   17.975  1.00 53.19  ? 606 HOH   B O   1 
HETATM 6230 O O   . HOH   I 5 .   ? 65.892 -8.982  -5.270  1.00 54.96  ? 607 HOH   B O   1 
HETATM 6231 O O   . HOH   I 5 .   ? 51.791 -25.669 10.133  1.00 60.00  ? 608 HOH   B O   1 
HETATM 6232 O O   . HOH   I 5 .   ? 35.497 -7.240  14.607  1.00 70.13  ? 609 HOH   B O   1 
HETATM 6233 O O   . HOH   I 5 .   ? 65.412 -20.439 13.151  1.00 62.63  ? 610 HOH   B O   1 
HETATM 6234 O O   . HOH   I 5 .   ? 29.552 -3.195  41.322  1.00 37.72  ? 611 HOH   B O   1 
HETATM 6235 O O   . HOH   I 5 .   ? 22.281 -1.610  38.414  1.00 43.20  ? 612 HOH   B O   1 
HETATM 6236 O O   . HOH   I 5 .   ? 31.613 2.747   37.334  1.00 31.68  ? 613 HOH   B O   1 
HETATM 6237 O O   . HOH   I 5 .   ? 30.009 -16.896 39.807  1.00 52.62  ? 614 HOH   B O   1 
HETATM 6238 O O   . HOH   I 5 .   ? 22.937 -1.504  24.096  1.00 45.99  ? 615 HOH   B O   1 
HETATM 6239 O O   . HOH   I 5 .   ? 31.925 15.025  32.813  1.00 46.68  ? 616 HOH   B O   1 
HETATM 6240 O O   . HOH   I 5 .   ? 46.111 3.574   34.013  1.00 60.20  ? 617 HOH   B O   1 
HETATM 6241 O O   . HOH   I 5 .   ? 3.162  -6.034  12.289  1.00 60.90  ? 618 HOH   B O   1 
HETATM 6242 O O   . HOH   I 5 .   ? 24.193 -14.577 43.430  1.00 47.68  ? 619 HOH   B O   1 
HETATM 6243 O O   . HOH   I 5 .   ? 27.587 9.273   32.474  1.00 46.13  ? 620 HOH   B O   1 
HETATM 6244 O O   . HOH   I 5 .   ? 16.445 -10.587 10.402  1.00 72.25  ? 621 HOH   B O   1 
# 
