CNRS Nantes University UFIP UFIP
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***  pha  ***

elNémo ID: 21041221150957117

Job options:

ID        	=	 21041221150957117
JOBID     	=	 pha
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -200
DQMAX     	=	 200
DQSTEP    	=	 20
DOGRAPHS  	=	 0

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER pha

data_6QY6
# 
_entry.id   6QY6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.336 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   6QY6         
WWPDB D_1292101116 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6QY6 
_pdbx_database_status.recvd_initial_deposition_date   2019-03-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'de Wijn, R.' 1 0000-0002-8342-1008 
'Rollet, K.'  2 0000-0002-1613-5220 
'Bluhm, A.'   3 ?                   
'Hennig, O.'  4 ?                   
'Betat, H.'   5 ?                   
'Moerl, M.'   6 0000-0003-0972-9386 
'Lorber, B.'  7 0000-0002-4672-9652 
'Sauter, C.'  8 0000-0002-8766-287X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;CCA-addition in the cold: functional and structural characterization of
the CCA-adding enzyme from Planococcus halocryophilus
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'De Wijn, R.' 1 0000-0002-8342-1008 
primary 'Hennig, O.'  2 ?                   
primary 'Ernst, F.'   3 0000-0001-5064-0928 
primary 'Betat, H.'   4 ?                   
primary 'Moerl, M.'   5 0000-0003-0972-9386 
primary 'Sauter, C.'  6 0000-0002-8766-287X 
# 
_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                     6QY6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     70.031 
_cell.length_a_esd                 ? 
_cell.length_b                     70.031 
_cell.length_b_esd                 ? 
_cell.length_c                     291.590 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         6QY6 
_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   ? 
# 
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 'CCA-adding enzyme' 48498.266 1   2.7.7.72 ? ? ? 
2 non-polymer nat 'PHOSPHATE ION'     94.971    1   ?        ? ? ? 
3 non-polymer syn GLYCEROL            92.094    2   ?        ? ? ? 
4 non-polymer syn 'ACETATE ION'       59.044    3   ?        ? ? ? 
5 water       nat water               18.015    238 ?        ? ? ? 
# 
_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       
;MHHHHHHSSGLVPRGSGMKETAAAKFERQHMDSPDLGTDDDDKMNTAIKVIHTLKAAGFEAYIVGGAVRDLLLGKTPHDV
DVASSALPQQVKVLFDRTVDTGIDHGTVLVLLDGEGIEVTTFRTESSYSDNRRPDSVEFVLSLEEDLRRRDFTINAMAMT
EDLKIIDPFGGKEDLKNKVIRAVGDPDERFEEDALRMLRAIRFSGQLDFIIDMKTLLSIRRHARLIRFIAVERLKSEIDK
IFVNPSMQKSMAYLKDSVLTRFLPVGGLFEVDWITYHTDGNPTYGWLYLLHQQKRQFTDIKDYRFSNEEKRLIEKSLELT
ALNTWDQWTFYKYTLKQLEMASRVTGKKKDLAAIKRQLPIQSRSELAVDGWDLIEWSGAKSGPWLKVWIEKIERLIVYGI
LKNDKELIKDWFEDEYHSHT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHSSGLVPRGSGMKETAAAKFERQHMDSPDLGTDDDDKMNTAIKVIHTLKAAGFEAYIVGGAVRDLLLGKTPHDV
DVASSALPQQVKVLFDRTVDTGIDHGTVLVLLDGEGIEVTTFRTESSYSDNRRPDSVEFVLSLEEDLRRRDFTINAMAMT
EDLKIIDPFGGKEDLKNKVIRAVGDPDERFEEDALRMLRAIRFSGQLDFIIDMKTLLSIRRHARLIRFIAVERLKSEIDK
IFVNPSMQKSMAYLKDSVLTRFLPVGGLFEVDWITYHTDGNPTYGWLYLLHQQKRQFTDIKDYRFSNEEKRLIEKSLELT
ALNTWDQWTFYKYTLKQLEMASRVTGKKKDLAAIKRQLPIQSRSELAVDGWDLIEWSGAKSGPWLKVWIEKIERLIVYGI
LKNDKELIKDWFEDEYHSHT
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
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   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   SER n 
1 9   SER n 
1 10  GLY n 
1 11  LEU n 
1 12  VAL n 
1 13  PRO n 
1 14  ARG n 
1 15  GLY n 
1 16  SER n 
1 17  GLY n 
1 18  MET n 
1 19  LYS n 
1 20  GLU n 
1 21  THR n 
1 22  ALA n 
1 23  ALA n 
1 24  ALA n 
1 25  LYS n 
1 26  PHE n 
1 27  GLU n 
1 28  ARG n 
1 29  GLN n 
1 30  HIS n 
1 31  MET n 
1 32  ASP n 
1 33  SER n 
1 34  PRO n 
1 35  ASP n 
1 36  LEU n 
1 37  GLY n 
1 38  THR n 
1 39  ASP n 
1 40  ASP n 
1 41  ASP n 
1 42  ASP n 
1 43  LYS n 
1 44  MET n 
1 45  ASN n 
1 46  THR n 
1 47  ALA n 
1 48  ILE n 
1 49  LYS n 
1 50  VAL n 
1 51  ILE n 
1 52  HIS n 
1 53  THR n 
1 54  LEU n 
1 55  LYS n 
1 56  ALA n 
1 57  ALA n 
1 58  GLY n 
1 59  PHE n 
1 60  GLU n 
1 61  ALA n 
1 62  TYR n 
1 63  ILE n 
1 64  VAL n 
1 65  GLY n 
1 66  GLY n 
1 67  ALA n 
1 68  VAL n 
1 69  ARG n 
1 70  ASP n 
1 71  LEU n 
1 72  LEU n 
1 73  LEU n 
1 74  GLY n 
1 75  LYS n 
1 76  THR n 
1 77  PRO n 
1 78  HIS n 
1 79  ASP n 
1 80  VAL n 
1 81  ASP n 
1 82  VAL n 
1 83  ALA n 
1 84  SER n 
1 85  SER n 
1 86  ALA n 
1 87  LEU n 
1 88  PRO n 
1 89  GLN n 
1 90  GLN n 
1 91  VAL n 
1 92  LYS n 
1 93  VAL n 
1 94  LEU n 
1 95  PHE n 
1 96  ASP n 
1 97  ARG n 
1 98  THR n 
1 99  VAL n 
1 100 ASP n 
1 101 THR n 
1 102 GLY n 
1 103 ILE n 
1 104 ASP n 
1 105 HIS n 
1 106 GLY n 
1 107 THR n 
1 108 VAL n 
1 109 LEU n 
1 110 VAL n 
1 111 LEU n 
1 112 LEU n 
1 113 ASP n 
1 114 GLY n 
1 115 GLU n 
1 116 GLY n 
1 117 ILE n 
1 118 GLU n 
1 119 VAL n 
1 120 THR n 
1 121 THR n 
1 122 PHE n 
1 123 ARG n 
1 124 THR n 
1 125 GLU n 
1 126 SER n 
1 127 SER n 
1 128 TYR n 
1 129 SER n 
1 130 ASP n 
1 131 ASN n 
1 132 ARG n 
1 133 ARG n 
1 134 PRO n 
1 135 ASP n 
1 136 SER n 
1 137 VAL n 
1 138 GLU n 
1 139 PHE n 
1 140 VAL n 
1 141 LEU n 
1 142 SER n 
1 143 LEU n 
1 144 GLU n 
1 145 GLU n 
1 146 ASP n 
1 147 LEU n 
1 148 ARG n 
1 149 ARG n 
1 150 ARG n 
1 151 ASP n 
1 152 PHE n 
1 153 THR n 
1 154 ILE n 
1 155 ASN n 
1 156 ALA n 
1 157 MET n 
1 158 ALA n 
1 159 MET n 
1 160 THR n 
1 161 GLU n 
1 162 ASP n 
1 163 LEU n 
1 164 LYS n 
1 165 ILE n 
1 166 ILE n 
1 167 ASP n 
1 168 PRO n 
1 169 PHE n 
1 170 GLY n 
1 171 GLY n 
1 172 LYS n 
1 173 GLU n 
1 174 ASP n 
1 175 LEU n 
1 176 LYS n 
1 177 ASN n 
1 178 LYS n 
1 179 VAL n 
1 180 ILE n 
1 181 ARG n 
1 182 ALA n 
1 183 VAL n 
1 184 GLY n 
1 185 ASP n 
1 186 PRO n 
1 187 ASP n 
1 188 GLU n 
1 189 ARG n 
1 190 PHE n 
1 191 GLU n 
1 192 GLU n 
1 193 ASP n 
1 194 ALA n 
1 195 LEU n 
1 196 ARG n 
1 197 MET n 
1 198 LEU n 
1 199 ARG n 
1 200 ALA n 
1 201 ILE n 
1 202 ARG n 
1 203 PHE n 
1 204 SER n 
1 205 GLY n 
1 206 GLN n 
1 207 LEU n 
1 208 ASP n 
1 209 PHE n 
1 210 ILE n 
1 211 ILE n 
1 212 ASP n 
1 213 MET n 
1 214 LYS n 
1 215 THR n 
1 216 LEU n 
1 217 LEU n 
1 218 SER n 
1 219 ILE n 
1 220 ARG n 
1 221 ARG n 
1 222 HIS n 
1 223 ALA n 
1 224 ARG n 
1 225 LEU n 
1 226 ILE n 
1 227 ARG n 
1 228 PHE n 
1 229 ILE n 
1 230 ALA n 
1 231 VAL n 
1 232 GLU n 
1 233 ARG n 
1 234 LEU n 
1 235 LYS n 
1 236 SER n 
1 237 GLU n 
1 238 ILE n 
1 239 ASP n 
1 240 LYS n 
1 241 ILE n 
1 242 PHE n 
1 243 VAL n 
1 244 ASN n 
1 245 PRO n 
1 246 SER n 
1 247 MET n 
1 248 GLN n 
1 249 LYS n 
1 250 SER n 
1 251 MET n 
1 252 ALA n 
1 253 TYR n 
1 254 LEU n 
1 255 LYS n 
1 256 ASP n 
1 257 SER n 
1 258 VAL n 
1 259 LEU n 
1 260 THR n 
1 261 ARG n 
1 262 PHE n 
1 263 LEU n 
1 264 PRO n 
1 265 VAL n 
1 266 GLY n 
1 267 GLY n 
1 268 LEU n 
1 269 PHE n 
1 270 GLU n 
1 271 VAL n 
1 272 ASP n 
1 273 TRP n 
1 274 ILE n 
1 275 THR n 
1 276 TYR n 
1 277 HIS n 
1 278 THR n 
1 279 ASP n 
1 280 GLY n 
1 281 ASN n 
1 282 PRO n 
1 283 THR n 
1 284 TYR n 
1 285 GLY n 
1 286 TRP n 
1 287 LEU n 
1 288 TYR n 
1 289 LEU n 
1 290 LEU n 
1 291 HIS n 
1 292 GLN n 
1 293 GLN n 
1 294 LYS n 
1 295 ARG n 
1 296 GLN n 
1 297 PHE n 
1 298 THR n 
1 299 ASP n 
1 300 ILE n 
1 301 LYS n 
1 302 ASP n 
1 303 TYR n 
1 304 ARG n 
1 305 PHE n 
1 306 SER n 
1 307 ASN n 
1 308 GLU n 
1 309 GLU n 
1 310 LYS n 
1 311 ARG n 
1 312 LEU n 
1 313 ILE n 
1 314 GLU n 
1 315 LYS n 
1 316 SER n 
1 317 LEU n 
1 318 GLU n 
1 319 LEU n 
1 320 THR n 
1 321 ALA n 
1 322 LEU n 
1 323 ASN n 
1 324 THR n 
1 325 TRP n 
1 326 ASP n 
1 327 GLN n 
1 328 TRP n 
1 329 THR n 
1 330 PHE n 
1 331 TYR n 
1 332 LYS n 
1 333 TYR n 
1 334 THR n 
1 335 LEU n 
1 336 LYS n 
1 337 GLN n 
1 338 LEU n 
1 339 GLU n 
1 340 MET n 
1 341 ALA n 
1 342 SER n 
1 343 ARG n 
1 344 VAL n 
1 345 THR n 
1 346 GLY n 
1 347 LYS n 
1 348 LYS n 
1 349 LYS n 
1 350 ASP n 
1 351 LEU n 
1 352 ALA n 
1 353 ALA n 
1 354 ILE n 
1 355 LYS n 
1 356 ARG n 
1 357 GLN n 
1 358 LEU n 
1 359 PRO n 
1 360 ILE n 
1 361 GLN n 
1 362 SER n 
1 363 ARG n 
1 364 SER n 
1 365 GLU n 
1 366 LEU n 
1 367 ALA n 
1 368 VAL n 
1 369 ASP n 
1 370 GLY n 
1 371 TRP n 
1 372 ASP n 
1 373 LEU n 
1 374 ILE n 
1 375 GLU n 
1 376 TRP n 
1 377 SER n 
1 378 GLY n 
1 379 ALA n 
1 380 LYS n 
1 381 SER n 
1 382 GLY n 
1 383 PRO n 
1 384 TRP n 
1 385 LEU n 
1 386 LYS n 
1 387 VAL n 
1 388 TRP n 
1 389 ILE n 
1 390 GLU n 
1 391 LYS n 
1 392 ILE n 
1 393 GLU n 
1 394 ARG n 
1 395 LEU n 
1 396 ILE n 
1 397 VAL n 
1 398 TYR n 
1 399 GLY n 
1 400 ILE n 
1 401 LEU n 
1 402 LYS n 
1 403 ASN n 
1 404 ASP n 
1 405 LYS n 
1 406 GLU n 
1 407 LEU n 
1 408 ILE n 
1 409 LYS n 
1 410 ASP n 
1 411 TRP n 
1 412 PHE n 
1 413 GLU n 
1 414 ASP n 
1 415 GLU n 
1 416 TYR n 
1 417 HIS n 
1 418 SER n 
1 419 HIS n 
1 420 THR 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                   420 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 BBI08_05760 
_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      'Planococcus halocryophilus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1215089 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   'pET-30 Ek/LIC' 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET-30(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1C7DQ98_9BACL 
_struct_ref.pdbx_db_accession          A0A1C7DQ98 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MNTAIKVIHTLKAAGFEAYIVGGAVRDLLLGKTPHDVDVASSALPQQVKVLFDRTVDTGIDHGTVLVLLDGEGIEVTTFR
TESSYSDNRRPDSVEFVLSLEEDLRRRDFTINAMAMTEDLKIIDPFGGKEDLKNKVIRAVGDPDERFEEDALRMLRAIRF
SGQLDFIIDMKTLLSIRRHARLIRFIAVERLKSEIDKIFVNPSMQKSMAYLKDSVLTRFLPVGGLFEVDWITYHTDGNPT
YGWLYLLHQQKRQFTDIKDYRFSNEEKRLIEKSLELTALNTWDQWTFYKYTLKQLEMASRVTGKKKDLAAIKRQLPIQSR
SELAVDGWDLIEWSGAKSGPWLKVWIEKIERLIVYGILKNDKELIKDWFEDEYHSHT
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              6QY6 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 44 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 420 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A1C7DQ98 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  377 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       377 
# 
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 6QY6 MET A 1  ? UNP A0A1C7DQ98 ? ? 'initiating methionine' -42 1  
1 6QY6 HIS A 2  ? UNP A0A1C7DQ98 ? ? 'expression tag'        -41 2  
1 6QY6 HIS A 3  ? UNP A0A1C7DQ98 ? ? 'expression tag'        -40 3  
1 6QY6 HIS A 4  ? UNP A0A1C7DQ98 ? ? 'expression tag'        -39 4  
1 6QY6 HIS A 5  ? UNP A0A1C7DQ98 ? ? 'expression tag'        -38 5  
1 6QY6 HIS A 6  ? UNP A0A1C7DQ98 ? ? 'expression tag'        -37 6  
1 6QY6 HIS A 7  ? UNP A0A1C7DQ98 ? ? 'expression tag'        -36 7  
1 6QY6 SER A 8  ? UNP A0A1C7DQ98 ? ? 'expression tag'        -35 8  
1 6QY6 SER A 9  ? UNP A0A1C7DQ98 ? ? 'expression tag'        -34 9  
1 6QY6 GLY A 10 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -33 10 
1 6QY6 LEU A 11 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -32 11 
1 6QY6 VAL A 12 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -31 12 
1 6QY6 PRO A 13 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -30 13 
1 6QY6 ARG A 14 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -29 14 
1 6QY6 GLY A 15 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -28 15 
1 6QY6 SER A 16 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -27 16 
1 6QY6 GLY A 17 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -26 17 
1 6QY6 MET A 18 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -25 18 
1 6QY6 LYS A 19 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -24 19 
1 6QY6 GLU A 20 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -23 20 
1 6QY6 THR A 21 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -22 21 
1 6QY6 ALA A 22 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -21 22 
1 6QY6 ALA A 23 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -20 23 
1 6QY6 ALA A 24 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -19 24 
1 6QY6 LYS A 25 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -18 25 
1 6QY6 PHE A 26 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -17 26 
1 6QY6 GLU A 27 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -16 27 
1 6QY6 ARG A 28 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -15 28 
1 6QY6 GLN A 29 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -14 29 
1 6QY6 HIS A 30 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -13 30 
1 6QY6 MET A 31 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -12 31 
1 6QY6 ASP A 32 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -11 32 
1 6QY6 SER A 33 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -10 33 
1 6QY6 PRO A 34 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -9  34 
1 6QY6 ASP A 35 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -8  35 
1 6QY6 LEU A 36 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -7  36 
1 6QY6 GLY A 37 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -6  37 
1 6QY6 THR A 38 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -5  38 
1 6QY6 ASP A 39 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -4  39 
1 6QY6 ASP A 40 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -3  40 
1 6QY6 ASP A 41 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -2  41 
1 6QY6 ASP A 42 ? UNP A0A1C7DQ98 ? ? 'expression tag'        -1  42 
1 6QY6 LYS A 43 ? UNP A0A1C7DQ98 ? ? 'expression tag'        0   43 
# 
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 
ACT non-polymer         . 'ACETATE ION'   ?                               'C2 H3 O2 -1'    59.044  
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 
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 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION' ?                               'O4 P -3'        94.971  
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
# 
_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                   6QY6 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            3.62 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         65.98 
_exptl_crystal.description                 bipyramid 
_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_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            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;protein solution at 4.5 mg/mL in 50 mM Tris-HCl pH7.5, 200 mM NaCl, 5 mM MgCl2;
reservoir solution: 100 mM Sodium acetate; pH 4.5 
1 M di-Ammonium hydrogen phosphate
;
_exptl_crystal_grow.pdbx_pH_range   '4.5 - 7.5' 
# 
_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         2016-09-16 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_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                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate            44.8 
_reflns.entry_id                         6QY6 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.8 
_reflns.d_resolution_low                 50 
_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                       68555 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             99.9 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  13.0 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            19.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.074 
_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                     1 
_reflns.pdbx_R_split                     ? 
_reflns.pdbx_CC_star                     ? 
# 
_reflns_shell.d_res_high                  1.8 
_reflns_shell.d_res_low                   1.91 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         0.66 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           10787 
_reflns_shell.percent_possible_all        99.3 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_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             12.9 
_reflns_shell.pdbx_Rsym_value             ? 
_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             2.648 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                0.59 
_reflns_shell.pdbx_R_split                ? 
_reflns_shell.pdbx_CC_star                ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 6QY6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.800 
_refine.ls_d_res_low                             39.926 
_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                     68408 
_refine.ls_number_reflns_R_free                  3420 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.71 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2083 
_refine.ls_R_factor_R_free                       0.2321 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2070 
_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.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_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                      1MIV 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 27.60 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.34 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3043 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             238 
_refine_hist.number_atoms_total               3310 
_refine_hist.d_res_high                       1.800 
_refine_hist.d_res_low                        39.926 
# 
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' ? 0.007  ? 3125 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.794  ? 4211 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.922 ? 1169 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.051  ? 468  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 531  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 1.8000 1.8257  . . 131 2496 96.00  . . . 0.5147 . 0.4769 . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.8257 1.8530  . . 141 2650 99.00  . . . 0.5017 . 0.4753 . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.8530 1.8819  . . 140 2657 100.00 . . . 0.5029 . 0.4231 . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.8819 1.9128  . . 141 2665 100.00 . . . 0.4451 . 0.3656 . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.9128 1.9458  . . 140 2684 100.00 . . . 0.3403 . 0.3418 . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.9458 1.9812  . . 139 2656 100.00 . . . 0.4023 . 0.3119 . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.9812 2.0193  . . 140 2644 100.00 . . . 0.3159 . 0.2717 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.0193 2.0605  . . 141 2712 100.00 . . . 0.3105 . 0.2625 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.0605 2.1053  . . 140 2643 100.00 . . . 0.2698 . 0.2496 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.1053 2.1543  . . 141 2679 100.00 . . . 0.2878 . 0.2421 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.1543 2.2081  . . 142 2686 100.00 . . . 0.2996 . 0.2436 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.2081 2.2678  . . 141 2689 100.00 . . . 0.2753 . 0.2458 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.2678 2.3345  . . 143 2709 100.00 . . . 0.2528 . 0.2285 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.3345 2.4099  . . 142 2696 100.00 . . . 0.2376 . 0.2154 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.4099 2.4960  . . 140 2680 100.00 . . . 0.2781 . 0.2161 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.4960 2.5959  . . 143 2712 100.00 . . . 0.2193 . 0.2161 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.5959 2.7140  . . 143 2706 100.00 . . . 0.2564 . 0.2110 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.7140 2.8571  . . 143 2720 100.00 . . . 0.2413 . 0.2142 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.8571 3.0360  . . 144 2748 100.00 . . . 0.2385 . 0.2148 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.0360 3.2704  . . 144 2728 100.00 . . . 0.2371 . 0.2185 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.2704 3.5993  . . 146 2767 100.00 . . . 0.2262 . 0.2051 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.5993 4.1196  . . 149 2816 100.00 . . . 0.1897 . 0.1736 . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.1196 5.1885  . . 147 2813 100.00 . . . 0.1725 . 0.1572 . . . . . . . . . . 
'X-RAY DIFFRACTION' 5.1885 39.9362 . . 159 3032 100.00 . . . 0.2039 . 0.1815 . . . . . . . . . . 
# 
_struct.entry_id                     6QY6 
_struct.title                        'Crystal structure of the CCA-adding enzyme of a psychrophilic organism' 
_struct.pdbx_descriptor              'CCA-adding enzyme (E.C.2.7.7.72)' 
_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        6QY6 
_struct_keywords.text            'tRNA maturation, tRNA nucleotidyltransferase, psychrophilic enzyme, RNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'RNA BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
# 
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 42  ? ALA A 57  ? ASP A -1  ALA A 14  1 ? 16 
HELX_P HELX_P2  AA2 GLY A 65  ? LEU A 73  ? GLY A 22  LEU A 30  1 ? 9  
HELX_P HELX_P3  AA3 LEU A 87  ? PHE A 95  ? LEU A 44  PHE A 52  1 ? 9  
HELX_P HELX_P4  AA4 ASP A 100 ? HIS A 105 ? ASP A 57  HIS A 62  5 ? 6  
HELX_P HELX_P5  AA5 SER A 142 ? ARG A 148 ? SER A 99  ARG A 105 1 ? 7  
HELX_P HELX_P6  AA6 PHE A 152 ? ALA A 156 ? PHE A 109 ALA A 113 5 ? 5  
HELX_P HELX_P7  AA7 GLY A 170 ? LYS A 178 ? GLY A 127 LYS A 135 1 ? 9  
HELX_P HELX_P8  AA8 ASP A 185 ? ASP A 193 ? ASP A 142 ASP A 150 1 ? 9  
HELX_P HELX_P9  AA9 ALA A 194 ? ASP A 208 ? ALA A 151 ASP A 165 1 ? 15 
HELX_P HELX_P10 AB1 ASP A 212 ? ALA A 223 ? ASP A 169 ALA A 180 1 ? 12 
HELX_P HELX_P11 AB2 ARG A 224 ? ILE A 229 ? ARG A 181 ILE A 186 5 ? 6  
HELX_P HELX_P12 AB3 ALA A 230 ? ASN A 244 ? ALA A 187 ASN A 201 1 ? 15 
HELX_P HELX_P13 AB4 SER A 246 ? SER A 257 ? SER A 203 SER A 214 1 ? 12 
HELX_P HELX_P14 AB5 VAL A 258 ? LEU A 263 ? VAL A 215 LEU A 220 1 ? 6  
HELX_P HELX_P15 AB6 VAL A 265 ? GLU A 270 ? VAL A 222 GLU A 227 5 ? 6  
HELX_P HELX_P16 AB7 ASN A 281 ? GLN A 293 ? ASN A 238 GLN A 250 1 ? 13 
HELX_P HELX_P17 AB8 GLN A 296 ? ARG A 304 ? GLN A 253 ARG A 261 5 ? 9  
HELX_P HELX_P18 AB9 SER A 306 ? LEU A 322 ? SER A 263 LEU A 279 1 ? 17 
HELX_P HELX_P19 AC1 ASP A 326 ? TYR A 333 ? ASP A 283 TYR A 290 1 ? 8  
HELX_P HELX_P20 AC2 THR A 334 ? GLY A 346 ? THR A 291 GLY A 303 1 ? 13 
HELX_P HELX_P21 AC3 ASP A 350 ? GLN A 357 ? ASP A 307 GLN A 314 1 ? 8  
HELX_P HELX_P22 AC4 SER A 362 ? LEU A 366 ? SER A 319 LEU A 323 5 ? 5  
HELX_P HELX_P23 AC5 ASP A 369 ? GLY A 378 ? ASP A 326 GLY A 335 1 ? 10 
HELX_P HELX_P24 AC6 PRO A 383 ? TYR A 398 ? PRO A 340 TYR A 355 1 ? 16 
HELX_P HELX_P25 AC7 ASP A 404 ? TYR A 416 ? ASP A 361 TYR A 373 1 ? 13 
# 
_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 ? 7 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 98  ? VAL A 99  ? THR A 55  VAL A 56  
AA1 2 THR A 107 ? LEU A 112 ? THR A 64  LEU A 69  
AA1 3 GLU A 115 ? THR A 121 ? GLU A 72  THR A 78  
AA1 4 ASP A 81  ? SER A 84  ? ASP A 38  SER A 41  
AA1 5 ALA A 61  ? VAL A 64  ? ALA A 18  VAL A 21  
AA1 6 ALA A 158 ? MET A 159 ? ALA A 115 MET A 116 
AA1 7 ILE A 165 ? ILE A 166 ? ILE A 122 ILE A 123 
AA2 1 ARG A 123 ? GLU A 125 ? ARG A 80  GLU A 82  
AA2 2 VAL A 137 ? PHE A 139 ? VAL A 94  PHE A 96  
AA3 1 VAL A 179 ? ILE A 180 ? VAL A 136 ILE A 137 
AA3 2 ILE A 210 ? ILE A 211 ? ILE A 167 ILE A 168 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 99  ? N VAL A 56  O LEU A 109 ? O LEU A 66  
AA1 2 3 N VAL A 108 ? N VAL A 65  O VAL A 119 ? O VAL A 76  
AA1 3 4 O THR A 120 ? O THR A 77  N VAL A 82  ? N VAL A 39  
AA1 4 5 O ALA A 83  ? O ALA A 40  N TYR A 62  ? N TYR A 19  
AA1 5 6 N ILE A 63  ? N ILE A 20  O MET A 159 ? O MET A 116 
AA1 6 7 N ALA A 158 ? N ALA A 115 O ILE A 166 ? O ILE A 123 
AA2 1 2 N THR A 124 ? N THR A 81  O GLU A 138 ? O GLU A 95  
AA3 1 2 N ILE A 180 ? N ILE A 137 O ILE A 210 ? O ILE A 167 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A PO4 501 ? 9  'binding site for residue PO4 A 501' 
AC2 Software A GOL 502 ? 10 'binding site for residue GOL A 502' 
AC3 Software A GOL 503 ? 6  'binding site for residue GOL A 503' 
AC4 Software A ACT 504 ? 2  'binding site for residue ACT A 504' 
AC5 Software A ACT 505 ? 2  'binding site for residue ACT A 505' 
AC6 Software A ACT 506 ? 4  'binding site for residue ACT A 506' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 9  ARG A 311 ? ARG A 268 . ? 1_555 ? 
2  AC1 9  LYS A 315 ? LYS A 272 . ? 1_555 ? 
3  AC1 9  LYS A 332 ? LYS A 289 . ? 1_555 ? 
4  AC1 9  TYR A 333 ? TYR A 290 . ? 1_555 ? 
5  AC1 9  THR A 334 ? THR A 291 . ? 1_555 ? 
6  AC1 9  GLN A 337 ? GLN A 294 . ? 1_555 ? 
7  AC1 9  GOL C .   ? GOL A 502 . ? 1_555 ? 
8  AC1 9  GOL D .   ? GOL A 503 . ? 1_555 ? 
9  AC1 9  HOH H .   ? HOH A 608 . ? 1_555 ? 
10 AC2 10 TYR A 331 ? TYR A 288 . ? 1_555 ? 
11 AC2 10 LYS A 332 ? LYS A 289 . ? 1_555 ? 
12 AC2 10 TYR A 333 ? TYR A 290 . ? 1_555 ? 
13 AC2 10 LYS A 355 ? LYS A 312 . ? 1_555 ? 
14 AC2 10 PO4 B .   ? PO4 A 501 . ? 1_555 ? 
15 AC2 10 HOH H .   ? HOH A 624 . ? 1_555 ? 
16 AC2 10 HOH H .   ? HOH A 643 . ? 1_555 ? 
17 AC2 10 HOH H .   ? HOH A 660 . ? 1_555 ? 
18 AC2 10 HOH H .   ? HOH A 718 . ? 1_555 ? 
19 AC2 10 HOH H .   ? HOH A 724 . ? 1_555 ? 
20 AC3 6  LYS A 315 ? LYS A 272 . ? 1_555 ? 
21 AC3 6  GLU A 318 ? GLU A 275 . ? 1_555 ? 
22 AC3 6  LYS A 332 ? LYS A 289 . ? 1_555 ? 
23 AC3 6  TYR A 333 ? TYR A 290 . ? 1_555 ? 
24 AC3 6  PO4 B .   ? PO4 A 501 . ? 1_555 ? 
25 AC3 6  HOH H .   ? HOH A 755 . ? 1_555 ? 
26 AC4 2  VAL A 137 ? VAL A 94  . ? 1_555 ? 
27 AC4 2  PHE A 139 ? PHE A 96  . ? 1_555 ? 
28 AC5 2  ARG A 311 ? ARG A 268 . ? 1_555 ? 
29 AC5 2  LYS A 315 ? LYS A 272 . ? 1_555 ? 
30 AC6 4  ARG A 69  ? ARG A 26  . ? 1_555 ? 
31 AC6 4  HIS A 78  ? HIS A 35  . ? 1_555 ? 
32 AC6 4  ARG A 202 ? ARG A 159 . ? 1_555 ? 
33 AC6 4  GLN A 206 ? GLN A 163 . ? 1_555 ? 
# 
_atom_sites.entry_id                    6QY6 
_atom_sites.fract_transf_matrix[1][1]   0.014279 
_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]   0.014279 
_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]   0.003429 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
H 
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   . ASP A 1 40  ? 26.425 47.897  42.420 1.00 76.62  ?  -3  ASP A N   1 
ATOM   2    C CA  . ASP A 1 40  ? 25.816 46.937  41.516 1.00 76.07  ?  -3  ASP A CA  1 
ATOM   3    C C   . ASP A 1 40  ? 24.837 47.626  40.583 1.00 73.26  ?  -3  ASP A C   1 
ATOM   4    O O   . ASP A 1 40  ? 24.913 48.848  40.348 1.00 60.99  ?  -3  ASP A O   1 
ATOM   5    C CB  . ASP A 1 40  ? 25.089 45.833  42.291 1.00 66.67  ?  -3  ASP A CB  1 
ATOM   6    C CG  . ASP A 1 40  ? 25.941 45.225  43.387 1.00 82.66  ?  -3  ASP A CG  1 
ATOM   7    O OD1 . ASP A 1 40  ? 27.157 45.013  43.170 1.00 78.31  ?  -3  ASP A OD1 1 
ATOM   8    O OD2 . ASP A 1 40  ? 25.388 44.966  44.478 1.00 95.11  ?  -3  ASP A OD2 1 
ATOM   9    N N   . ASP A 1 41  ? 23.915 46.815  40.055 1.00 72.62  ?  -2  ASP A N   1 
ATOM   10   C CA  . ASP A 1 41  ? 22.860 47.335  39.202 1.00 66.56  ?  -2  ASP A CA  1 
ATOM   11   C C   . ASP A 1 41  ? 22.023 48.375  39.927 1.00 64.50  ?  -2  ASP A C   1 
ATOM   12   O O   . ASP A 1 41  ? 21.281 49.120  39.274 1.00 50.01  ?  -2  ASP A O   1 
ATOM   13   C CB  . ASP A 1 41  ? 21.963 46.199  38.701 1.00 65.29  ?  -2  ASP A CB  1 
ATOM   14   C CG  . ASP A 1 41  ? 21.070 45.639  39.793 1.00 80.96  ?  -2  ASP A CG  1 
ATOM   15   O OD1 . ASP A 1 41  ? 21.602 45.257  40.863 1.00 81.92  ?  -2  ASP A OD1 1 
ATOM   16   O OD2 . ASP A 1 41  ? 19.831 45.597  39.591 1.00 80.53  ?  -2  ASP A OD2 1 
ATOM   17   N N   . ASP A 1 42  ? 22.114 48.445  41.265 1.00 45.91  ?  -1  ASP A N   1 
ATOM   18   C CA  . ASP A 1 42  ? 21.468 49.530  41.982 1.00 43.41  ?  -1  ASP A CA  1 
ATOM   19   C C   . ASP A 1 42  ? 22.423 50.458  42.724 1.00 37.15  ?  -1  ASP A C   1 
ATOM   20   O O   . ASP A 1 42  ? 22.015 51.575  43.057 1.00 38.22  ?  -1  ASP A O   1 
ATOM   21   C CB  . ASP A 1 42  ? 20.436 48.989  42.983 1.00 52.58  ?  -1  ASP A CB  1 
ATOM   22   C CG  . ASP A 1 42  ? 19.207 48.415  42.300 1.00 64.65  ?  -1  ASP A CG  1 
ATOM   23   O OD1 . ASP A 1 42  ? 19.149 48.435  41.047 1.00 52.07  ?  -1  ASP A OD1 1 
ATOM   24   O OD2 . ASP A 1 42  ? 18.301 47.943  43.021 1.00 59.35  ?  -1  ASP A OD2 1 
ATOM   25   N N   . LYS A 1 43  ? 23.670 50.048  42.976 1.00 39.45  ?  0   LYS A N   1 
ATOM   26   C CA  . LYS A 1 43  ? 24.557 50.869  43.801 1.00 39.91  ?  0   LYS A CA  1 
ATOM   27   C C   . LYS A 1 43  ? 24.897 52.184  43.117 1.00 32.40  ?  0   LYS A C   1 
ATOM   28   O O   . LYS A 1 43  ? 24.809 53.249  43.736 1.00 34.97  ?  0   LYS A O   1 
ATOM   29   C CB  . LYS A 1 43  ? 25.841 50.116  44.137 1.00 46.01  ?  0   LYS A CB  1 
ATOM   30   C CG  . LYS A 1 43  ? 25.688 49.015  45.157 1.00 56.04  ?  0   LYS A CG  1 
ATOM   31   C CD  . LYS A 1 43  ? 27.040 48.721  45.792 1.00 64.70  ?  0   LYS A CD  1 
ATOM   32   C CE  . LYS A 1 43  ? 26.982 47.539  46.754 1.00 80.11  ?  0   LYS A CE  1 
ATOM   33   N NZ  . LYS A 1 43  ? 26.954 46.237  46.021 1.00 75.75  ?  0   LYS A NZ  1 
ATOM   34   N N   . MET A 1 44  ? 25.320 52.133  41.845 1.00 32.21  ?  1   MET A N   1 
ATOM   35   C CA  . MET A 1 44  ? 25.661 53.367  41.142 1.00 34.48  ?  1   MET A CA  1 
ATOM   36   C C   . MET A 1 44  ? 24.465 54.316  41.080 1.00 36.19  ?  1   MET A C   1 
ATOM   37   O O   . MET A 1 44  ? 24.610 55.524  41.296 1.00 33.07  ?  1   MET A O   1 
ATOM   38   C CB  . MET A 1 44  ? 26.170 53.070  39.721 1.00 30.22  ?  1   MET A CB  1 
ATOM   39   C CG  . MET A 1 44  ? 27.604 52.552  39.629 1.00 44.47  ?  1   MET A CG  1 
ATOM   40   S SD  . MET A 1 44  ? 28.810 53.708  40.371 1.00 51.93  ?  1   MET A SD  1 
ATOM   41   C CE  . MET A 1 44  ? 28.335 55.232  39.562 1.00 50.77  ?  1   MET A CE  1 
ATOM   42   N N   . ASN A 1 45  ? 23.276 53.791  40.756 1.00 32.79  ?  2   ASN A N   1 
ATOM   43   C CA  . ASN A 1 45  ? 22.087 54.638  40.731 1.00 30.31  ?  2   ASN A CA  1 
ATOM   44   C C   . ASN A 1 45  ? 21.861 55.303  42.075 1.00 31.88  ?  2   ASN A C   1 
ATOM   45   O O   . ASN A 1 45  ? 21.523 56.491  42.144 1.00 33.32  ?  2   ASN A O   1 
ATOM   46   C CB  . ASN A 1 45  ? 20.856 53.822  40.345 1.00 32.06  ?  2   ASN A CB  1 
ATOM   47   C CG  . ASN A 1 45  ? 20.897 53.355  38.903 1.00 35.66  ?  2   ASN A CG  1 
ATOM   48   O OD1 . ASN A 1 45  ? 21.632 53.905  38.070 1.00 35.94  ?  2   ASN A OD1 1 
ATOM   49   N ND2 . ASN A 1 45  ? 20.111 52.330  38.596 1.00 33.23  ?  2   ASN A ND2 1 
ATOM   50   N N   . THR A 1 46  ? 22.009 54.541  43.157 1.00 28.26  ?  3   THR A N   1 
ATOM   51   C CA  . THR A 1 46  ? 21.786 55.109  44.478 1.00 31.96  ?  3   THR A CA  1 
ATOM   52   C C   . THR A 1 46  ? 22.814 56.193  44.780 1.00 34.15  ?  3   THR A C   1 
ATOM   53   O O   . THR A 1 46  ? 22.469 57.250  45.317 1.00 33.52  ?  3   THR A O   1 
ATOM   54   C CB  . THR A 1 46  ? 21.827 53.998  45.529 1.00 35.77  ?  3   THR A CB  1 
ATOM   55   O OG1 . THR A 1 46  ? 20.863 52.999  45.181 1.00 35.46  ?  3   THR A OG1 1 
ATOM   56   C CG2 . THR A 1 46  ? 21.503 54.555  46.946 1.00 34.49  ?  3   THR A CG2 1 
ATOM   57   N N   . ALA A 1 47  ? 24.078 55.964  44.413 1.00 32.16  ?  4   ALA A N   1 
ATOM   58   C CA  . ALA A 1 47  ? 25.098 56.990  44.629 1.00 31.10  ?  4   ALA A CA  1 
ATOM   59   C C   . ALA A 1 47  ? 24.782 58.259  43.838 1.00 31.75  ?  4   ALA A C   1 
ATOM   60   O O   . ALA A 1 47  ? 24.951 59.372  44.351 1.00 34.90  ?  4   ALA A O   1 
ATOM   61   C CB  . ALA A 1 47  ? 26.481 56.446  44.265 1.00 32.72  ?  4   ALA A CB  1 
ATOM   62   N N   . ILE A 1 48  ? 24.318 58.118  42.592 1.00 29.81  ?  5   ILE A N   1 
ATOM   63   C CA  . ILE A 1 48  ? 23.900 59.288  41.815 1.00 34.19  ?  5   ILE A CA  1 
ATOM   64   C C   . ILE A 1 48  ? 22.780 60.033  42.542 1.00 38.10  ?  5   ILE A C   1 
ATOM   65   O O   . ILE A 1 48  ? 22.786 61.268  42.628 1.00 35.29  ?  5   ILE A O   1 
ATOM   66   C CB  . ILE A 1 48  ? 23.478 58.872  40.388 1.00 33.46  ?  5   ILE A CB  1 
ATOM   67   C CG1 . ILE A 1 48  ? 24.682 58.369  39.573 1.00 41.95  ?  5   ILE A CG1 1 
ATOM   68   C CG2 . ILE A 1 48  ? 22.779 60.018  39.664 1.00 34.53  ?  5   ILE A CG2 1 
ATOM   69   C CD1 . ILE A 1 48  ? 25.599 59.487  39.034 1.00 47.62  ?  5   ILE A CD1 1 
ATOM   70   N N   . LYS A 1 49  ? 21.819 59.293  43.103 1.00 37.45  ?  6   LYS A N   1 
ATOM   71   C CA  . LYS A 1 49  ? 20.756 59.925  43.882 1.00 37.50  ?  6   LYS A CA  1 
ATOM   72   C C   . LYS A 1 49  ? 21.316 60.635  45.120 1.00 35.24  ?  6   LYS A C   1 
ATOM   73   O O   . LYS A 1 49  ? 20.889 61.745  45.458 1.00 34.71  ?  6   LYS A O   1 
ATOM   74   C CB  . LYS A 1 49  ? 19.714 58.869  44.272 1.00 41.04  ?  6   LYS A CB  1 
ATOM   75   C CG  . LYS A 1 49  ? 18.566 59.376  45.142 1.00 50.61  ?  6   LYS A CG  1 
ATOM   76   C CD  . LYS A 1 49  ? 17.446 58.316  45.265 1.00 54.36  ?  6   LYS A CD  1 
ATOM   77   C CE  . LYS A 1 49  ? 16.964 57.848  43.887 1.00 51.38  ?  6   LYS A CE  1 
ATOM   78   N NZ  . LYS A 1 49  ? 15.868 56.812  43.949 1.00 48.60  ?  6   LYS A NZ  1 
ATOM   79   N N   . VAL A 1 50  ? 22.270 60.007  45.811 1.00 33.66  ?  7   VAL A N   1 
ATOM   80   C CA  . VAL A 1 50  ? 22.900 60.644  46.967 1.00 35.22  ?  7   VAL A CA  1 
ATOM   81   C C   . VAL A 1 50  ? 23.598 61.933  46.546 1.00 37.16  ?  7   VAL A C   1 
ATOM   82   O O   . VAL A 1 50  ? 23.449 62.986  47.174 1.00 34.24  ?  7   VAL A O   1 
ATOM   83   C CB  . VAL A 1 50  ? 23.874 59.657  47.640 1.00 37.28  ?  7   VAL A CB  1 
ATOM   84   C CG1 . VAL A 1 50  ? 24.853 60.389  48.571 1.00 33.18  ?  7   VAL A CG1 1 
ATOM   85   C CG2 . VAL A 1 50  ? 23.094 58.566  48.399 1.00 36.21  ?  7   VAL A CG2 1 
ATOM   86   N N   . ILE A 1 51  ? 24.357 61.871  45.456 1.00 32.09  ?  8   ILE A N   1 
ATOM   87   C CA  . ILE A 1 51  ? 25.039 63.054  44.949 1.00 35.91  ?  8   ILE A CA  1 
ATOM   88   C C   . ILE A 1 51  ? 24.033 64.155  44.619 1.00 38.45  ?  8   ILE A C   1 
ATOM   89   O O   . ILE A 1 51  ? 24.222 65.318  44.991 1.00 37.71  ?  8   ILE A O   1 
ATOM   90   C CB  . ILE A 1 51  ? 25.895 62.662  43.732 1.00 37.54  ?  8   ILE A CB  1 
ATOM   91   C CG1 . ILE A 1 51  ? 27.147 61.907  44.224 1.00 34.39  ?  8   ILE A CG1 1 
ATOM   92   C CG2 . ILE A 1 51  ? 26.180 63.861  42.825 1.00 38.27  ?  8   ILE A CG2 1 
ATOM   93   C CD1 . ILE A 1 51  ? 27.959 61.298  43.089 1.00 41.85  ?  8   ILE A CD1 1 
ATOM   94   N N   . HIS A 1 52  ? 22.947 63.802  43.916 1.00 38.07  ?  9   HIS A N   1 
ATOM   95   C CA  . HIS A 1 52  ? 21.929 64.793  43.567 1.00 35.70  ?  9   HIS A CA  1 
ATOM   96   C C   . HIS A 1 52  ? 21.378 65.477  44.812 1.00 42.95  ?  9   HIS A C   1 
ATOM   97   O O   . HIS A 1 52  ? 21.157 66.695  44.817 1.00 42.22  ?  9   HIS A O   1 
ATOM   98   C CB  . HIS A 1 52  ? 20.793 64.132  42.780 1.00 43.36  ?  9   HIS A CB  1 
ATOM   99   C CG  . HIS A 1 52  ? 19.841 65.107  42.153 1.00 54.87  ?  9   HIS A CG  1 
ATOM   100  N ND1 . HIS A 1 52  ? 20.139 65.802  41.001 1.00 58.27  ?  9   HIS A ND1 1 
ATOM   101  C CD2 . HIS A 1 52  ? 18.601 65.509  42.523 1.00 52.42  ?  9   HIS A CD2 1 
ATOM   102  C CE1 . HIS A 1 52  ? 19.124 66.588  40.684 1.00 59.51  ?  9   HIS A CE1 1 
ATOM   103  N NE2 . HIS A 1 52  ? 18.178 66.429  41.592 1.00 55.22  ?  9   HIS A NE2 1 
ATOM   104  N N   . THR A 1 53  ? 21.160 64.709  45.880 1.00 38.72  ?  10  THR A N   1 
ATOM   105  C CA  . THR A 1 53  ? 20.627 65.279  47.113 1.00 41.13  ?  10  THR A CA  1 
ATOM   106  C C   . THR A 1 53  ? 21.633 66.204  47.782 1.00 49.40  ?  10  THR A C   1 
ATOM   107  O O   . THR A 1 53  ? 21.263 67.278  48.276 1.00 44.11  ?  10  THR A O   1 
ATOM   108  C CB  . THR A 1 53  ? 20.224 64.166  48.075 1.00 40.77  ?  10  THR A CB  1 
ATOM   109  O OG1 . THR A 1 53  ? 19.207 63.356  47.473 1.00 43.37  ?  10  THR A OG1 1 
ATOM   110  C CG2 . THR A 1 53  ? 19.717 64.756  49.385 1.00 41.67  ?  10  THR A CG2 1 
ATOM   111  N N   . LEU A 1 54  ? 22.902 65.792  47.843 1.00 40.02  ?  11  LEU A N   1 
ATOM   112  C CA  . LEU A 1 54  ? 23.924 66.648  48.438 1.00 38.51  ?  11  LEU A CA  1 
ATOM   113  C C   . LEU A 1 54  ? 24.059 67.958  47.676 1.00 41.23  ?  11  LEU A C   1 
ATOM   114  O O   . LEU A 1 54  ? 24.220 69.021  48.285 1.00 42.70  ?  11  LEU A O   1 
ATOM   115  C CB  . LEU A 1 54  ? 25.268 65.926  48.472 1.00 39.24  ?  11  LEU A CB  1 
ATOM   116  C CG  . LEU A 1 54  ? 25.365 64.843  49.539 1.00 35.06  ?  11  LEU A CG  1 
ATOM   117  C CD1 . LEU A 1 54  ? 26.452 63.851  49.145 1.00 36.96  ?  11  LEU A CD1 1 
ATOM   118  C CD2 . LEU A 1 54  ? 25.638 65.452  50.913 1.00 40.35  ?  11  LEU A CD2 1 
ATOM   119  N N   . LYS A 1 55  ? 24.003 67.898  46.345 1.00 38.31  ?  12  LYS A N   1 
ATOM   120  C CA  . LYS A 1 55  ? 24.157 69.105  45.533 1.00 45.18  ?  12  LYS A CA  1 
ATOM   121  C C   . LYS A 1 55  ? 22.918 69.992  45.599 1.00 48.14  ?  12  LYS A C   1 
ATOM   122  O O   . LYS A 1 55  ? 23.033 71.220  45.591 1.00 45.38  ?  12  LYS A O   1 
ATOM   123  C CB  . LYS A 1 55  ? 24.471 68.727  44.090 1.00 40.23  ?  12  LYS A CB  1 
ATOM   124  C CG  . LYS A 1 55  ? 25.859 68.119  43.939 1.00 43.05  ?  12  LYS A CG  1 
ATOM   125  C CD  . LYS A 1 55  ? 26.084 67.562  42.557 1.00 37.89  ?  12  LYS A CD  1 
ATOM   126  C CE  . LYS A 1 55  ? 26.074 68.653  41.520 1.00 42.29  ?  12  LYS A CE  1 
ATOM   127  N NZ  . LYS A 1 55  ? 26.219 68.013  40.200 1.00 47.36  ?  12  LYS A NZ  1 
ATOM   128  N N   . ALA A 1 56  ? 21.727 69.394  45.678 1.00 51.88  ?  13  ALA A N   1 
ATOM   129  C CA  . ALA A 1 56  ? 20.522 70.197  45.874 1.00 53.45  ?  13  ALA A CA  1 
ATOM   130  C C   . ALA A 1 56  ? 20.629 71.065  47.121 1.00 49.38  ?  13  ALA A C   1 
ATOM   131  O O   . ALA A 1 56  ? 20.073 72.169  47.158 1.00 54.06  ?  13  ALA A O   1 
ATOM   132  C CB  . ALA A 1 56  ? 19.285 69.298  45.951 1.00 45.36  ?  13  ALA A CB  1 
ATOM   133  N N   . ALA A 1 57  ? 21.345 70.596  48.140 1.00 45.05  ?  14  ALA A N   1 
ATOM   134  C CA  . ALA A 1 57  ? 21.590 71.353  49.358 1.00 40.64  ?  14  ALA A CA  1 
ATOM   135  C C   . ALA A 1 57  ? 22.812 72.271  49.262 1.00 47.08  ?  14  ALA A C   1 
ATOM   136  O O   . ALA A 1 57  ? 23.240 72.817  50.286 1.00 50.06  ?  14  ALA A O   1 
ATOM   137  C CB  . ALA A 1 57  ? 21.749 70.398  50.544 1.00 40.10  ?  14  ALA A CB  1 
ATOM   138  N N   . GLY A 1 58  ? 23.388 72.439  48.071 1.00 47.73  ?  15  GLY A N   1 
ATOM   139  C CA  . GLY A 1 58  ? 24.505 73.344  47.868 1.00 50.22  ?  15  GLY A CA  1 
ATOM   140  C C   . GLY A 1 58  ? 25.897 72.758  48.042 1.00 51.33  ?  15  GLY A C   1 
ATOM   141  O O   . GLY A 1 58  ? 26.880 73.501  47.923 1.00 47.31  ?  15  GLY A O   1 
ATOM   142  N N   . PHE A 1 59  ? 26.024 71.465  48.327 1.00 43.04  ?  16  PHE A N   1 
ATOM   143  C CA  . PHE A 1 59  ? 27.341 70.875  48.503 1.00 36.58  ?  16  PHE A CA  1 
ATOM   144  C C   . PHE A 1 59  ? 27.866 70.315  47.182 1.00 36.17  ?  16  PHE A C   1 
ATOM   145  O O   . PHE A 1 59  ? 27.106 70.015  46.260 1.00 45.82  ?  16  PHE A O   1 
ATOM   146  C CB  . PHE A 1 59  ? 27.303 69.765  49.557 1.00 35.30  ?  16  PHE A CB  1 
ATOM   147  C CG  . PHE A 1 59  ? 26.804 70.229  50.895 1.00 44.12  ?  16  PHE A CG  1 
ATOM   148  C CD1 . PHE A 1 59  ? 27.607 71.013  51.709 1.00 45.65  ?  16  PHE A CD1 1 
ATOM   149  C CD2 . PHE A 1 59  ? 25.530 69.892  51.331 1.00 41.24  ?  16  PHE A CD2 1 
ATOM   150  C CE1 . PHE A 1 59  ? 27.145 71.455  52.942 1.00 46.51  ?  16  PHE A CE1 1 
ATOM   151  C CE2 . PHE A 1 59  ? 25.063 70.328  52.564 1.00 43.04  ?  16  PHE A CE2 1 
ATOM   152  C CZ  . PHE A 1 59  ? 25.871 71.107  53.366 1.00 44.10  ?  16  PHE A CZ  1 
ATOM   153  N N   . GLU A 1 60  ? 29.187 70.176  47.106 1.00 40.66  ?  17  GLU A N   1 
ATOM   154  C CA  . GLU A 1 60  ? 29.806 69.404  46.032 1.00 41.50  ?  17  GLU A CA  1 
ATOM   155  C C   . GLU A 1 60  ? 29.740 67.921  46.364 1.00 34.54  ?  17  GLU A C   1 
ATOM   156  O O   . GLU A 1 60  ? 29.882 67.525  47.526 1.00 37.70  ?  17  GLU A O   1 
ATOM   157  C CB  . GLU A 1 60  ? 31.278 69.771  45.855 1.00 39.05  ?  17  GLU A CB  1 
ATOM   158  C CG  . GLU A 1 60  ? 31.596 71.195  45.503 1.00 44.64  ?  17  GLU A CG  1 
ATOM   159  C CD  . GLU A 1 60  ? 33.098 71.427  45.554 1.00 52.08  ?  17  GLU A CD  1 
ATOM   160  O OE1 . GLU A 1 60  ? 33.556 72.156  46.458 1.00 64.43  ?  17  GLU A OE1 1 
ATOM   161  O OE2 . GLU A 1 60  ? 33.825 70.831  44.726 1.00 49.79  ?  17  GLU A OE2 1 
ATOM   162  N N   . ALA A 1 61  ? 29.583 67.092  45.329 1.00 33.41  ?  18  ALA A N   1 
ATOM   163  C CA  . ALA A 1 61  ? 29.636 65.659  45.570 1.00 32.16  ?  18  ALA A CA  1 
ATOM   164  C C   . ALA A 1 61  ? 30.004 64.929  44.282 1.00 28.84  ?  18  ALA A C   1 
ATOM   165  O O   . ALA A 1 61  ? 29.627 65.347  43.184 1.00 32.00  ?  18  ALA A O   1 
ATOM   166  C CB  . ALA A 1 61  ? 28.305 65.150  46.143 1.00 33.94  ?  18  ALA A CB  1 
ATOM   167  N N   . TYR A 1 62  ? 30.758 63.840  44.443 1.00 31.44  ?  19  TYR A N   1 
ATOM   168  C CA  . TYR A 1 62  ? 31.325 63.080  43.334 1.00 31.54  ?  19  TYR A CA  1 
ATOM   169  C C   . TYR A 1 62  ? 31.384 61.607  43.711 1.00 33.74  ?  19  TYR A C   1 
ATOM   170  O O   . TYR A 1 62  ? 31.543 61.262  44.883 1.00 30.68  ?  19  TYR A O   1 
ATOM   171  C CB  . TYR A 1 62  ? 32.752 63.537  42.993 1.00 33.42  ?  19  TYR A CB  1 
ATOM   172  C CG  . TYR A 1 62  ? 32.931 65.031  42.898 1.00 31.95  ?  19  TYR A CG  1 
ATOM   173  C CD1 . TYR A 1 62  ? 33.222 65.791  44.032 1.00 36.17  ?  19  TYR A CD1 1 
ATOM   174  C CD2 . TYR A 1 62  ? 32.814 65.687  41.678 1.00 35.27  ?  19  TYR A CD2 1 
ATOM   175  C CE1 . TYR A 1 62  ? 33.385 67.163  43.948 1.00 36.27  ?  19  TYR A CE1 1 
ATOM   176  C CE2 . TYR A 1 62  ? 32.976 67.063  41.584 1.00 35.89  ?  19  TYR A CE2 1 
ATOM   177  C CZ  . TYR A 1 62  ? 33.257 67.791  42.724 1.00 38.34  ?  19  TYR A CZ  1 
ATOM   178  O OH  . TYR A 1 62  ? 33.412 69.153  42.638 1.00 41.89  ?  19  TYR A OH  1 
ATOM   179  N N   . ILE A 1 63  ? 31.286 60.740  42.699 1.00 28.70  ?  20  ILE A N   1 
ATOM   180  C CA  . ILE A 1 63  ? 31.770 59.374  42.856 1.00 31.75  ?  20  ILE A CA  1 
ATOM   181  C C   . ILE A 1 63  ? 33.289 59.412  42.862 1.00 31.00  ?  20  ILE A C   1 
ATOM   182  O O   . ILE A 1 63  ? 33.905 60.107  42.045 1.00 31.71  ?  20  ILE A O   1 
ATOM   183  C CB  . ILE A 1 63  ? 31.285 58.471  41.709 1.00 30.44  ?  20  ILE A CB  1 
ATOM   184  C CG1 . ILE A 1 63  ? 29.782 58.640  41.453 1.00 41.52  ?  20  ILE A CG1 1 
ATOM   185  C CG2 . ILE A 1 63  ? 31.657 57.023  41.992 1.00 33.30  ?  20  ILE A CG2 1 
ATOM   186  C CD1 . ILE A 1 63  ? 28.944 57.992  42.466 1.00 44.46  ?  20  ILE A CD1 1 
ATOM   187  N N   . VAL A 1 64  ? 33.903 58.650  43.756 1.00 27.58  ?  21  VAL A N   1 
ATOM   188  C CA  . VAL A 1 64  ? 35.349 58.712  43.922 1.00 31.17  ?  21  VAL A CA  1 
ATOM   189  C C   . VAL A 1 64  ? 35.915 57.309  44.111 1.00 32.49  ?  21  VAL A C   1 
ATOM   190  O O   . VAL A 1 64  ? 35.224 56.394  44.561 1.00 34.82  ?  21  VAL A O   1 
ATOM   191  C CB  . VAL A 1 64  ? 35.727 59.641  45.102 1.00 36.04  ?  21  VAL A CB  1 
ATOM   192  C CG1 . VAL A 1 64  ? 35.348 59.008  46.455 1.00 33.87  ?  21  VAL A CG1 1 
ATOM   193  C CG2 . VAL A 1 64  ? 37.187 59.994  45.050 1.00 43.70  ?  21  VAL A CG2 1 
ATOM   194  N N   . GLY A 1 65  ? 37.177 57.133  43.722 1.00 38.93  ?  22  GLY A N   1 
ATOM   195  C CA  . GLY A 1 65  ? 37.902 55.922  44.056 1.00 38.94  ?  22  GLY A CA  1 
ATOM   196  C C   . GLY A 1 65  ? 37.560 54.692  43.232 1.00 31.00  ?  22  GLY A C   1 
ATOM   197  O O   . GLY A 1 65  ? 37.438 54.772  42.008 1.00 33.91  ?  22  GLY A O   1 
ATOM   198  N N   . GLY A 1 66  ? 37.394 53.547  43.904 1.00 35.94  ?  23  GLY A N   1 
ATOM   199  C CA  . GLY A 1 66  ? 37.344 52.279  43.189 1.00 37.62  ?  23  GLY A CA  1 
ATOM   200  C C   . GLY A 1 66  ? 36.195 52.183  42.203 1.00 40.64  ?  23  GLY A C   1 
ATOM   201  O O   . GLY A 1 66  ? 36.318 51.531  41.159 1.00 36.62  ?  23  GLY A O   1 
ATOM   202  N N   . ALA A 1 67  ? 35.068 52.827  42.512 1.00 34.37  ?  24  ALA A N   1 
ATOM   203  C CA  . ALA A 1 67  ? 33.921 52.747  41.615 1.00 36.19  ?  24  ALA A CA  1 
ATOM   204  C C   . ALA A 1 67  ? 34.232 53.376  40.262 1.00 35.87  ?  24  ALA A C   1 
ATOM   205  O O   . ALA A 1 67  ? 33.807 52.856  39.227 1.00 38.74  ?  24  ALA A O   1 
ATOM   206  C CB  . ALA A 1 67  ? 32.695 53.402  42.258 1.00 41.06  ?  24  ALA A CB  1 
ATOM   207  N N   . VAL A 1 68  ? 34.965 54.501  40.246 1.00 33.35  ?  25  VAL A N   1 
ATOM   208  C CA  . VAL A 1 68  ? 35.333 55.124  38.974 1.00 35.36  ?  25  VAL A CA  1 
ATOM   209  C C   . VAL A 1 68  ? 36.256 54.198  38.194 1.00 41.75  ?  25  VAL A C   1 
ATOM   210  O O   . VAL A 1 68  ? 36.088 53.986  36.987 1.00 36.35  ?  25  VAL A O   1 
ATOM   211  C CB  . VAL A 1 68  ? 35.991 56.498  39.199 1.00 33.26  ?  25  VAL A CB  1 
ATOM   212  C CG1 . VAL A 1 68  ? 36.216 57.198  37.854 1.00 34.42  ?  25  VAL A CG1 1 
ATOM   213  C CG2 . VAL A 1 68  ? 35.156 57.374  40.159 1.00 35.33  ?  25  VAL A CG2 1 
ATOM   214  N N   . ARG A 1 69  ? 37.250 53.634  38.883 1.00 40.30  ?  26  ARG A N   1 
ATOM   215  C CA  . ARG A 1 69  ? 38.128 52.648  38.265 1.00 42.58  ?  26  ARG A CA  1 
ATOM   216  C C   . ARG A 1 69  ? 37.328 51.493  37.666 1.00 42.06  ?  26  ARG A C   1 
ATOM   217  O O   . ARG A 1 69  ? 37.505 51.138  36.496 1.00 42.90  ?  26  ARG A O   1 
ATOM   218  C CB  . ARG A 1 69  ? 39.118 52.126  39.308 1.00 35.50  ?  26  ARG A CB  1 
ATOM   219  C CG  . ARG A 1 69  ? 39.952 50.961  38.825 1.00 41.69  ?  26  ARG A CG  1 
ATOM   220  C CD  . ARG A 1 69  ? 39.704 49.752  39.703 1.00 54.32  ?  26  ARG A CD  1 
ATOM   221  N NE  . ARG A 1 69  ? 40.212 50.035  41.018 1.00 47.01  ?  26  ARG A NE  1 
ATOM   222  C CZ  . ARG A 1 69  ? 39.724 49.581  42.168 1.00 40.20  ?  26  ARG A CZ  1 
ATOM   223  N NH1 . ARG A 1 69  ? 38.665 48.780  42.218 1.00 46.09  ?  26  ARG A NH1 1 
ATOM   224  N NH2 . ARG A 1 69  ? 40.308 49.963  43.288 1.00 36.60  ?  26  ARG A NH2 1 
ATOM   225  N N   . ASP A 1 70  ? 36.452 50.882  38.465 1.00 40.68  ?  27  ASP A N   1 
ATOM   226  C CA  . ASP A 1 70  ? 35.698 49.739  37.961 1.00 44.47  ?  27  ASP A CA  1 
ATOM   227  C C   . ASP A 1 70  ? 34.809 50.145  36.792 1.00 50.21  ?  27  ASP A C   1 
ATOM   228  O O   . ASP A 1 70  ? 34.766 49.451  35.766 1.00 47.42  ?  27  ASP A O   1 
ATOM   229  C CB  . ASP A 1 70  ? 34.886 49.108  39.086 1.00 43.68  ?  27  ASP A CB  1 
ATOM   230  C CG  . ASP A 1 70  ? 35.768 48.516  40.170 1.00 51.66  ?  27  ASP A CG  1 
ATOM   231  O OD1 . ASP A 1 70  ? 36.948 48.220  39.876 1.00 53.33  ?  27  ASP A OD1 1 
ATOM   232  O OD2 . ASP A 1 70  ? 35.295 48.359  41.313 1.00 60.67  ?  27  ASP A OD2 1 
ATOM   233  N N   . LEU A 1 71  ? 34.112 51.279  36.915 1.00 47.31  ?  28  LEU A N   1 
ATOM   234  C CA  . LEU A 1 71  ? 33.321 51.792  35.798 1.00 44.34  ?  28  LEU A CA  1 
ATOM   235  C C   . LEU A 1 71  ? 34.149 51.887  34.525 1.00 54.74  ?  28  LEU A C   1 
ATOM   236  O O   . LEU A 1 71  ? 33.732 51.412  33.460 1.00 50.42  ?  28  LEU A O   1 
ATOM   237  C CB  . LEU A 1 71  ? 32.742 53.162  36.140 1.00 45.64  ?  28  LEU A CB  1 
ATOM   238  C CG  . LEU A 1 71  ? 31.281 53.210  36.567 1.00 63.09  ?  28  LEU A CG  1 
ATOM   239  C CD1 . LEU A 1 71  ? 30.747 54.640  36.469 1.00 51.55  ?  28  LEU A CD1 1 
ATOM   240  C CD2 . LEU A 1 71  ? 30.455 52.249  35.710 1.00 61.63  ?  28  LEU A CD2 1 
ATOM   241  N N   . LEU A 1 72  ? 35.315 52.536  34.605 1.00 38.24  ?  29  LEU A N   1 
ATOM   242  C CA  . LEU A 1 72  ? 36.125 52.716  33.408 1.00 45.82  ?  29  LEU A CA  1 
ATOM   243  C C   . LEU A 1 72  ? 36.662 51.392  32.879 1.00 48.28  ?  29  LEU A C   1 
ATOM   244  O O   . LEU A 1 72  ? 36.974 51.291  31.688 1.00 50.96  ?  29  LEU A O   1 
ATOM   245  C CB  . LEU A 1 72  ? 37.273 53.689  33.685 1.00 42.09  ?  29  LEU A CB  1 
ATOM   246  C CG  . LEU A 1 72  ? 36.867 55.158  33.847 1.00 48.24  ?  29  LEU A CG  1 
ATOM   247  C CD1 . LEU A 1 72  ? 37.992 55.984  34.443 1.00 43.25  ?  29  LEU A CD1 1 
ATOM   248  C CD2 . LEU A 1 72  ? 36.435 55.750  32.512 1.00 47.09  ?  29  LEU A CD2 1 
ATOM   249  N N   . LEU A 1 73  ? 36.766 50.379  33.731 1.00 44.79  ?  30  LEU A N   1 
ATOM   250  C CA  . LEU A 1 73  ? 37.172 49.048  33.301 1.00 51.04  ?  30  LEU A CA  1 
ATOM   251  C C   . LEU A 1 73  ? 36.013 48.223  32.762 1.00 54.10  ?  30  LEU A C   1 
ATOM   252  O O   . LEU A 1 73  ? 36.208 47.050  32.432 1.00 52.83  ?  30  LEU A O   1 
ATOM   253  C CB  . LEU A 1 73  ? 37.827 48.294  34.459 1.00 47.66  ?  30  LEU A CB  1 
ATOM   254  C CG  . LEU A 1 73  ? 39.205 48.796  34.901 1.00 48.48  ?  30  LEU A CG  1 
ATOM   255  C CD1 . LEU A 1 73  ? 39.692 48.014  36.100 1.00 43.03  ?  30  LEU A CD1 1 
ATOM   256  C CD2 . LEU A 1 73  ? 40.218 48.700  33.770 1.00 45.96  ?  30  LEU A CD2 1 
ATOM   257  N N   . GLY A 1 74  ? 34.816 48.792  32.687 1.00 54.64  ?  31  GLY A N   1 
ATOM   258  C CA  . GLY A 1 74  ? 33.664 48.023  32.267 1.00 57.93  ?  31  GLY A CA  1 
ATOM   259  C C   . GLY A 1 74  ? 33.242 46.959  33.253 1.00 60.65  ?  31  GLY A C   1 
ATOM   260  O O   . GLY A 1 74  ? 32.684 45.937  32.845 1.00 67.49  ?  31  GLY A O   1 
ATOM   261  N N   . LYS A 1 75  ? 33.502 47.162  34.543 1.00 49.57  ?  32  LYS A N   1 
ATOM   262  C CA  . LYS A 1 75  ? 33.082 46.244  35.589 1.00 48.52  ?  32  LYS A CA  1 
ATOM   263  C C   . LYS A 1 75  ? 32.035 46.905  36.474 1.00 60.57  ?  32  LYS A C   1 
ATOM   264  O O   . LYS A 1 75  ? 31.868 48.128  36.476 1.00 51.68  ?  32  LYS A O   1 
ATOM   265  C CB  . LYS A 1 75  ? 34.272 45.787  36.445 1.00 56.52  ?  32  LYS A CB  1 
ATOM   266  C CG  . LYS A 1 75  ? 35.352 45.037  35.684 1.00 63.33  ?  32  LYS A CG  1 
ATOM   267  C CD  . LYS A 1 75  ? 36.237 44.236  36.636 1.00 74.74  ?  32  LYS A CD  1 
ATOM   268  C CE  . LYS A 1 75  ? 37.128 45.129  37.481 1.00 66.08  ?  32  LYS A CE  1 
ATOM   269  N NZ  . LYS A 1 75  ? 37.890 44.343  38.508 1.00 73.69  ?  32  LYS A NZ  1 
ATOM   270  N N   . THR A 1 76  ? 31.340 46.073  37.253 1.00 59.02  ?  33  THR A N   1 
ATOM   271  C CA  . THR A 1 76  ? 30.301 46.547  38.152 1.00 57.78  ?  33  THR A CA  1 
ATOM   272  C C   . THR A 1 76  ? 30.888 46.766  39.535 1.00 61.32  ?  33  THR A C   1 
ATOM   273  O O   . THR A 1 76  ? 31.397 45.810  40.138 1.00 55.99  ?  33  THR A O   1 
ATOM   274  C CB  . THR A 1 76  ? 29.150 45.548  38.218 1.00 67.97  ?  33  THR A CB  1 
ATOM   275  O OG1 . THR A 1 76  ? 28.519 45.464  36.933 1.00 65.68  ?  33  THR A OG1 1 
ATOM   276  C CG2 . THR A 1 76  ? 28.128 45.976  39.263 1.00 60.90  ?  33  THR A CG2 1 
ATOM   277  N N   . PRO A 1 77  ? 30.832 47.983  40.076 1.00 62.17  ?  34  PRO A N   1 
ATOM   278  C CA  . PRO A 1 77  ? 31.503 48.255  41.354 1.00 50.10  ?  34  PRO A CA  1 
ATOM   279  C C   . PRO A 1 77  ? 30.955 47.407  42.497 1.00 56.55  ?  34  PRO A C   1 
ATOM   280  O O   . PRO A 1 77  ? 29.753 47.154  42.595 1.00 62.54  ?  34  PRO A O   1 
ATOM   281  C CB  . PRO A 1 77  ? 31.229 49.748  41.580 1.00 54.32  ?  34  PRO A CB  1 
ATOM   282  C CG  . PRO A 1 77  ? 31.033 50.308  40.198 1.00 51.58  ?  34  PRO A CG  1 
ATOM   283  C CD  . PRO A 1 77  ? 30.359 49.213  39.413 1.00 51.27  ?  34  PRO A CD  1 
ATOM   284  N N   . HIS A 1 78  ? 31.864 46.966  43.372 1.00 57.23  ?  35  HIS A N   1 
ATOM   285  C CA  . HIS A 1 78  ? 31.461 46.306  44.610 1.00 63.29  ?  35  HIS A CA  1 
ATOM   286  C C   . HIS A 1 78  ? 31.073 47.326  45.673 1.00 65.56  ?  35  HIS A C   1 
ATOM   287  O O   . HIS A 1 78  ? 30.143 47.099  46.456 1.00 59.53  ?  35  HIS A O   1 
ATOM   288  C CB  . HIS A 1 78  ? 32.595 45.416  45.127 1.00 74.68  ?  35  HIS A CB  1 
ATOM   289  C CG  . HIS A 1 78  ? 33.837 46.172  45.502 1.00 94.16  ?  35  HIS A CG  1 
ATOM   290  N ND1 . HIS A 1 78  ? 34.039 46.700  46.761 1.00 91.24  ?  35  HIS A ND1 1 
ATOM   291  C CD2 . HIS A 1 78  ? 34.937 46.496  44.778 1.00 93.14  ?  35  HIS A CD2 1 
ATOM   292  C CE1 . HIS A 1 78  ? 35.212 47.310  46.800 1.00 81.41  ?  35  HIS A CE1 1 
ATOM   293  N NE2 . HIS A 1 78  ? 35.776 47.201  45.609 1.00 89.99  ?  35  HIS A NE2 1 
ATOM   294  N N   . ASP A 1 79  ? 31.790 48.442  45.723 1.00 61.90  ?  36  ASP A N   1 
ATOM   295  C CA  . ASP A 1 79  ? 31.466 49.550  46.602 1.00 60.42  ?  36  ASP A CA  1 
ATOM   296  C C   . ASP A 1 79  ? 31.498 50.832  45.793 1.00 51.91  ?  36  ASP A C   1 
ATOM   297  O O   . ASP A 1 79  ? 32.274 50.963  44.844 1.00 46.67  ?  36  ASP A O   1 
ATOM   298  C CB  . ASP A 1 79  ? 32.439 49.660  47.768 1.00 59.72  ?  36  ASP A CB  1 
ATOM   299  C CG  . ASP A 1 79  ? 32.324 48.506  48.723 1.00 64.80  ?  36  ASP A CG  1 
ATOM   300  O OD1 . ASP A 1 79  ? 31.204 48.240  49.207 1.00 71.75  ?  36  ASP A OD1 1 
ATOM   301  O OD2 . ASP A 1 79  ? 33.352 47.856  48.980 1.00 79.42  ?  36  ASP A OD2 1 
ATOM   302  N N   . VAL A 1 80  ? 30.635 51.771  46.160 1.00 48.31  ?  37  VAL A N   1 
ATOM   303  C CA  . VAL A 1 80  ? 30.609 53.075  45.525 1.00 44.85  ?  37  VAL A CA  1 
ATOM   304  C C   . VAL A 1 80  ? 30.740 54.099  46.641 1.00 45.79  ?  37  VAL A C   1 
ATOM   305  O O   . VAL A 1 80  ? 29.858 54.205  47.500 1.00 48.98  ?  37  VAL A O   1 
ATOM   306  C CB  . VAL A 1 80  ? 29.343 53.300  44.689 1.00 44.06  ?  37  VAL A CB  1 
ATOM   307  C CG1 . VAL A 1 80  ? 29.413 54.630  43.961 1.00 37.36  ?  37  VAL A CG1 1 
ATOM   308  C CG2 . VAL A 1 80  ? 29.179 52.169  43.681 1.00 47.40  ?  37  VAL A CG2 1 
ATOM   309  N N   . ASP A 1 81  ? 31.867 54.804  46.667 1.00 39.48  ?  38  ASP A N   1 
ATOM   310  C CA  . ASP A 1 81  ? 32.117 55.863  47.632 1.00 35.54  ?  38  ASP A CA  1 
ATOM   311  C C   . ASP A 1 81  ? 31.810 57.211  46.999 1.00 34.85  ?  38  ASP A C   1 
ATOM   312  O O   . ASP A 1 81  ? 32.009 57.420  45.794 1.00 33.48  ?  38  ASP A O   1 
ATOM   313  C CB  . ASP A 1 81  ? 33.566 55.851  48.114 1.00 38.82  ?  38  ASP A CB  1 
ATOM   314  C CG  . ASP A 1 81  ? 33.948 54.546  48.787 1.00 56.39  ?  38  ASP A CG  1 
ATOM   315  O OD1 . ASP A 1 81  ? 33.042 53.836  49.276 1.00 57.84  ?  38  ASP A OD1 1 
ATOM   316  O OD2 . ASP A 1 81  ? 35.159 54.222  48.819 1.00 65.92  ?  38  ASP A OD2 1 
ATOM   317  N N   . VAL A 1 82  ? 31.306 58.120  47.822 1.00 29.88  ?  39  VAL A N   1 
ATOM   318  C CA  . VAL A 1 82  ? 30.997 59.478  47.412 1.00 29.33  ?  39  VAL A CA  1 
ATOM   319  C C   . VAL A 1 82  ? 31.855 60.417  48.249 1.00 34.76  ?  39  VAL A C   1 
ATOM   320  O O   . VAL A 1 82  ? 31.870 60.316  49.479 1.00 37.91  ?  39  VAL A O   1 
ATOM   321  C CB  . VAL A 1 82  ? 29.498 59.787  47.577 1.00 30.72  ?  39  VAL A CB  1 
ATOM   322  C CG1 . VAL A 1 82  ? 29.228 61.284  47.399 1.00 32.13  ?  39  VAL A CG1 1 
ATOM   323  C CG2 . VAL A 1 82  ? 28.673 58.972  46.572 1.00 31.05  ?  39  VAL A CG2 1 
ATOM   324  N N   . ALA A 1 83  ? 32.571 61.311  47.580 1.00 31.80  ?  40  ALA A N   1 
ATOM   325  C CA  . ALA A 1 83  ? 33.318 62.382  48.217 1.00 33.46  ?  40  ALA A CA  1 
ATOM   326  C C   . ALA A 1 83  ? 32.487 63.656  48.139 1.00 34.67  ?  40  ALA A C   1 
ATOM   327  O O   . ALA A 1 83  ? 31.886 63.948  47.102 1.00 32.49  ?  40  ALA A O   1 
ATOM   328  C CB  . ALA A 1 83  ? 34.680 62.584  47.533 1.00 32.81  ?  40  ALA A CB  1 
ATOM   329  N N   . SER A 1 84  ? 32.440 64.412  49.240 1.00 30.19  ?  41  SER A N   1 
ATOM   330  C CA  . SER A 1 84  ? 31.572 65.580  49.252 1.00 34.61  ?  41  SER A CA  1 
ATOM   331  C C   . SER A 1 84  ? 32.196 66.702  50.077 1.00 31.58  ?  41  SER A C   1 
ATOM   332  O O   . SER A 1 84  ? 32.983 66.451  50.991 1.00 33.61  ?  41  SER A O   1 
ATOM   333  C CB  . SER A 1 84  ? 30.193 65.211  49.812 1.00 34.52  ?  41  SER A CB  1 
ATOM   334  O OG  . SER A 1 84  ? 29.369 66.351  49.920 1.00 36.26  ?  41  SER A OG  1 
ATOM   335  N N   . SER A 1 85  ? 31.812 67.944  49.764 1.00 32.47  ?  42  SER A N   1 
ATOM   336  C CA  . SER A 1 85  ? 32.184 69.059  50.635 1.00 40.12  ?  42  SER A CA  1 
ATOM   337  C C   . SER A 1 85  ? 31.344 69.098  51.909 1.00 44.74  ?  42  SER A C   1 
ATOM   338  O O   . SER A 1 85  ? 31.736 69.761  52.885 1.00 40.22  ?  42  SER A O   1 
ATOM   339  C CB  . SER A 1 85  ? 32.067 70.396  49.889 1.00 37.26  ?  42  SER A CB  1 
ATOM   340  O OG  . SER A 1 85  ? 30.733 70.685  49.516 1.00 35.95  ?  42  SER A OG  1 
ATOM   341  N N   . ALA A 1 86  ? 30.226 68.373  51.944 1.00 36.89  ?  43  ALA A N   1 
ATOM   342  C CA  . ALA A 1 86  ? 29.439 68.299  53.176 1.00 39.52  ?  43  ALA A CA  1 
ATOM   343  C C   . ALA A 1 86  ? 30.240 67.661  54.298 1.00 41.07  ?  43  ALA A C   1 
ATOM   344  O O   . ALA A 1 86  ? 31.012 66.721  54.091 1.00 39.24  ?  43  ALA A O   1 
ATOM   345  C CB  . ALA A 1 86  ? 28.145 67.509  52.955 1.00 34.91  ?  43  ALA A CB  1 
ATOM   346  N N   . LEU A 1 87  ? 30.042 68.176  55.509 1.00 39.84  ?  44  LEU A N   1 
ATOM   347  C CA  . LEU A 1 87  ? 30.612 67.550  56.682 1.00 36.69  ?  44  LEU A CA  1 
ATOM   348  C C   . LEU A 1 87  ? 29.663 66.492  57.222 1.00 33.17  ?  44  LEU A C   1 
ATOM   349  O O   . LEU A 1 87  ? 28.468 66.505  56.917 1.00 43.99  ?  44  LEU A O   1 
ATOM   350  C CB  . LEU A 1 87  ? 30.895 68.611  57.748 1.00 36.05  ?  44  LEU A CB  1 
ATOM   351  C CG  . LEU A 1 87  ? 31.926 69.649  57.312 1.00 39.40  ?  44  LEU A CG  1 
ATOM   352  C CD1 . LEU A 1 87  ? 31.803 70.922  58.171 1.00 49.36  ?  44  LEU A CD1 1 
ATOM   353  C CD2 . LEU A 1 87  ? 33.320 69.044  57.428 1.00 37.48  ?  44  LEU A CD2 1 
ATOM   354  N N   . PRO A 1 88  ? 30.172 65.549  58.010 1.00 34.97  ?  45  PRO A N   1 
ATOM   355  C CA  . PRO A 1 88  ? 29.345 64.392  58.397 1.00 44.95  ?  45  PRO A CA  1 
ATOM   356  C C   . PRO A 1 88  ? 27.981 64.747  58.965 1.00 45.83  ?  45  PRO A C   1 
ATOM   357  O O   . PRO A 1 88  ? 26.992 64.092  58.616 1.00 42.27  ?  45  PRO A O   1 
ATOM   358  C CB  . PRO A 1 88  ? 30.224 63.678  59.427 1.00 41.75  ?  45  PRO A CB  1 
ATOM   359  C CG  . PRO A 1 88  ? 31.620 64.015  58.994 1.00 37.83  ?  45  PRO A CG  1 
ATOM   360  C CD  . PRO A 1 88  ? 31.564 65.418  58.467 1.00 37.55  ?  45  PRO A CD  1 
ATOM   361  N N   . GLN A 1 89  ? 27.881 65.764  59.829 1.00 45.83  ?  46  GLN A N   1 
ATOM   362  C CA  . GLN A 1 89  ? 26.576 66.056  60.413 1.00 39.89  ?  46  GLN A CA  1 
ATOM   363  C C   . GLN A 1 89  ? 25.642 66.689  59.397 1.00 42.50  ?  46  GLN A C   1 
ATOM   364  O O   . GLN A 1 89  ? 24.420 66.521  59.495 1.00 45.20  ?  46  GLN A O   1 
ATOM   365  C CB  . GLN A 1 89  ? 26.735 66.944  61.654 1.00 43.65  ?  46  GLN A CB  1 
ATOM   366  C CG  . GLN A 1 89  ? 27.314 66.190  62.825 1.00 36.82  ?  46  GLN A CG  1 
ATOM   367  C CD  . GLN A 1 89  ? 26.386 65.088  63.336 1.00 42.85  ?  46  GLN A CD  1 
ATOM   368  O OE1 . GLN A 1 89  ? 25.166 65.151  63.154 1.00 47.68  ?  46  GLN A OE1 1 
ATOM   369  N NE2 . GLN A 1 89  ? 26.965 64.065  63.956 1.00 40.19  ?  46  GLN A NE2 1 
ATOM   370  N N   . GLN A 1 90  ? 26.188 67.396  58.404 1.00 38.09  ?  47  GLN A N   1 
ATOM   371  C CA  . GLN A 1 90  ? 25.346 67.913  57.334 1.00 41.88  ?  47  GLN A CA  1 
ATOM   372  C C   . GLN A 1 90  ? 24.819 66.790  56.448 1.00 43.79  ?  47  GLN A C   1 
ATOM   373  O O   . GLN A 1 90  ? 23.701 66.891  55.928 1.00 42.50  ?  47  GLN A O   1 
ATOM   374  C CB  . GLN A 1 90  ? 26.117 68.944  56.507 1.00 38.01  ?  47  GLN A CB  1 
ATOM   375  C CG  . GLN A 1 90  ? 26.677 70.083  57.377 1.00 47.32  ?  47  GLN A CG  1 
ATOM   376  C CD  . GLN A 1 90  ? 27.576 71.031  56.617 1.00 47.69  ?  47  GLN A CD  1 
ATOM   377  O OE1 . GLN A 1 90  ? 28.574 70.618  56.028 1.00 45.59  ?  47  GLN A OE1 1 
ATOM   378  N NE2 . GLN A 1 90  ? 27.226 72.320  56.625 1.00 46.10  ?  47  GLN A NE2 1 
ATOM   379  N N   . VAL A 1 91  ? 25.595 65.716  56.264 1.00 40.81  ?  48  VAL A N   1 
ATOM   380  C CA  . VAL A 1 91  ? 25.082 64.576  55.504 1.00 42.10  ?  48  VAL A CA  1 
ATOM   381  C C   . VAL A 1 91  ? 23.887 63.969  56.228 1.00 43.33  ?  48  VAL A C   1 
ATOM   382  O O   . VAL A 1 91  ? 22.840 63.708  55.626 1.00 43.82  ?  48  VAL A O   1 
ATOM   383  C CB  . VAL A 1 91  ? 26.181 63.525  55.264 1.00 40.25  ?  48  VAL A CB  1 
ATOM   384  C CG1 . VAL A 1 91  ? 25.598 62.331  54.488 1.00 38.17  ?  48  VAL A CG1 1 
ATOM   385  C CG2 . VAL A 1 91  ? 27.347 64.126  54.486 1.00 35.98  ?  48  VAL A CG2 1 
ATOM   386  N N   . LYS A 1 92  ? 24.013 63.790  57.547 1.00 45.35  ?  49  LYS A N   1 
ATOM   387  C CA  . LYS A 1 92  ? 22.948 63.161  58.325 1.00 56.89  ?  49  LYS A CA  1 
ATOM   388  C C   . LYS A 1 92  ? 21.659 63.969  58.276 1.00 53.08  ?  49  LYS A C   1 
ATOM   389  O O   . LYS A 1 92  ? 20.566 63.395  58.338 1.00 54.68  ?  49  LYS A O   1 
ATOM   390  C CB  . LYS A 1 92  ? 23.410 62.959  59.764 1.00 48.31  ?  49  LYS A CB  1 
ATOM   391  C CG  . LYS A 1 92  ? 24.562 61.966  59.891 1.00 49.21  ?  49  LYS A CG  1 
ATOM   392  C CD  . LYS A 1 92  ? 25.219 62.016  61.260 1.00 51.53  ?  49  LYS A CD  1 
ATOM   393  C CE  . LYS A 1 92  ? 24.497 61.138  62.267 1.00 59.41  ?  49  LYS A CE  1 
ATOM   394  N NZ  . LYS A 1 92  ? 23.030 61.346  62.249 1.00 64.50  ?  49  LYS A NZ  1 
ATOM   395  N N   . VAL A 1 93  ? 21.764 65.291  58.134 1.00 49.22  ?  50  VAL A N   1 
ATOM   396  C CA  . VAL A 1 93  ? 20.580 66.135  58.021 1.00 48.00  ?  50  VAL A CA  1 
ATOM   397  C C   . VAL A 1 93  ? 19.803 65.825  56.753 1.00 53.88  ?  50  VAL A C   1 
ATOM   398  O O   . VAL A 1 93  ? 18.571 65.948  56.722 1.00 48.05  ?  50  VAL A O   1 
ATOM   399  C CB  . VAL A 1 93  ? 20.997 67.621  58.076 1.00 53.12  ?  50  VAL A CB  1 
ATOM   400  C CG1 . VAL A 1 93  ? 19.900 68.512  57.511 1.00 50.91  ?  50  VAL A CG1 1 
ATOM   401  C CG2 . VAL A 1 93  ? 21.347 68.023  59.503 1.00 48.57  ?  50  VAL A CG2 1 
ATOM   402  N N   . LEU A 1 94  ? 20.498 65.427  55.685 1.00 47.39  ?  51  LEU A N   1 
ATOM   403  C CA  . LEU A 1 94  ? 19.890 65.290  54.373 1.00 46.04  ?  51  LEU A CA  1 
ATOM   404  C C   . LEU A 1 94  ? 19.348 63.896  54.083 1.00 41.66  ?  51  LEU A C   1 
ATOM   405  O O   . LEU A 1 94  ? 18.652 63.723  53.077 1.00 48.69  ?  51  LEU A O   1 
ATOM   406  C CB  . LEU A 1 94  ? 20.908 65.666  53.288 1.00 42.89  ?  51  LEU A CB  1 
ATOM   407  C CG  . LEU A 1 94  ? 21.402 67.114  53.332 1.00 47.04  ?  51  LEU A CG  1 
ATOM   408  C CD1 . LEU A 1 94  ? 22.462 67.357  52.265 1.00 46.39  ?  51  LEU A CD1 1 
ATOM   409  C CD2 . LEU A 1 94  ? 20.235 68.067  53.147 1.00 44.00  ?  51  LEU A CD2 1 
ATOM   410  N N   . PHE A 1 95  ? 19.654 62.901  54.907 1.00 41.64  ?  52  PHE A N   1 
ATOM   411  C CA  . PHE A 1 95  ? 19.227 61.531  54.654 1.00 45.19  ?  52  PHE A CA  1 
ATOM   412  C C   . PHE A 1 95  ? 18.596 60.935  55.905 1.00 49.20  ?  52  PHE A C   1 
ATOM   413  O O   . PHE A 1 95  ? 19.122 61.090  57.010 1.00 49.63  ?  52  PHE A O   1 
ATOM   414  C CB  . PHE A 1 95  ? 20.403 60.665  54.202 1.00 39.90  ?  52  PHE A CB  1 
ATOM   415  C CG  . PHE A 1 95  ? 21.030 61.140  52.926 1.00 40.16  ?  52  PHE A CG  1 
ATOM   416  C CD1 . PHE A 1 95  ? 20.463 60.810  51.707 1.00 41.03  ?  52  PHE A CD1 1 
ATOM   417  C CD2 . PHE A 1 95  ? 22.166 61.931  52.947 1.00 38.86  ?  52  PHE A CD2 1 
ATOM   418  C CE1 . PHE A 1 95  ? 21.027 61.250  50.515 1.00 41.08  ?  52  PHE A CE1 1 
ATOM   419  C CE2 . PHE A 1 95  ? 22.744 62.382  51.756 1.00 40.56  ?  52  PHE A CE2 1 
ATOM   420  C CZ  . PHE A 1 95  ? 22.165 62.041  50.537 1.00 40.63  ?  52  PHE A CZ  1 
ATOM   421  N N   . ASP A 1 96  ? 17.478 60.228  55.714 1.00 52.05  ?  53  ASP A N   1 
ATOM   422  C CA  . ASP A 1 96  ? 16.728 59.703  56.855 1.00 59.18  ?  53  ASP A CA  1 
ATOM   423  C C   . ASP A 1 96  ? 17.540 58.685  57.644 1.00 54.23  ?  53  ASP A C   1 
ATOM   424  O O   . ASP A 1 96  ? 17.490 58.662  58.879 1.00 53.24  ?  53  ASP A O   1 
ATOM   425  C CB  . ASP A 1 96  ? 15.422 59.068  56.380 1.00 60.11  ?  53  ASP A CB  1 
ATOM   426  C CG  . ASP A 1 96  ? 14.560 60.028  55.590 1.00 67.58  ?  53  ASP A CG  1 
ATOM   427  O OD1 . ASP A 1 96  ? 14.574 61.237  55.905 1.00 71.41  ?  53  ASP A OD1 1 
ATOM   428  O OD2 . ASP A 1 96  ? 13.868 59.572  54.651 1.00 73.52  ?  53  ASP A OD2 1 
ATOM   429  N N   . ARG A 1 97  ? 18.286 57.826  56.953 1.00 49.80  ?  54  ARG A N   1 
ATOM   430  C CA  . ARG A 1 97  ? 18.909 56.665  57.578 1.00 48.47  ?  54  ARG A CA  1 
ATOM   431  C C   . ARG A 1 97  ? 20.396 56.654  57.261 1.00 51.37  ?  54  ARG A C   1 
ATOM   432  O O   . ARG A 1 97  ? 20.794 56.451  56.105 1.00 41.96  ?  54  ARG A O   1 
ATOM   433  C CB  . ARG A 1 97  ? 18.226 55.379  57.117 1.00 51.57  ?  54  ARG A CB  1 
ATOM   434  C CG  . ARG A 1 97  ? 16.728 55.393  57.412 1.00 59.13  ?  54  ARG A CG  1 
ATOM   435  C CD  . ARG A 1 97  ? 16.045 54.082  57.050 1.00 73.74  ?  54  ARG A CD  1 
ATOM   436  N NE  . ARG A 1 97  ? 16.664 52.932  57.706 1.00 73.80  ?  54  ARG A NE  1 
ATOM   437  C CZ  . ARG A 1 97  ? 17.273 51.945  57.054 1.00 73.35  ?  54  ARG A CZ  1 
ATOM   438  N NH1 . ARG A 1 97  ? 17.337 51.970  55.727 1.00 68.90  ?  54  ARG A NH1 1 
ATOM   439  N NH2 . ARG A 1 97  ? 17.812 50.933  57.723 1.00 67.10  ?  54  ARG A NH2 1 
ATOM   440  N N   . THR A 1 98  ? 21.208 56.883  58.287 1.00 42.16  ?  55  THR A N   1 
ATOM   441  C CA  . THR A 1 98  ? 22.656 56.871  58.169 1.00 43.45  ?  55  THR A CA  1 
ATOM   442  C C   . THR A 1 98  ? 23.242 56.027  59.288 1.00 43.32  ?  55  THR A C   1 
ATOM   443  O O   . THR A 1 98  ? 22.602 55.787  60.312 1.00 50.10  ?  55  THR A O   1 
ATOM   444  C CB  . THR A 1 98  ? 23.252 58.281  58.236 1.00 48.00  ?  55  THR A CB  1 
ATOM   445  O OG1 . THR A 1 98  ? 22.953 58.856  59.513 1.00 52.41  ?  55  THR A OG1 1 
ATOM   446  C CG2 . THR A 1 98  ? 22.692 59.169  57.141 1.00 43.58  ?  55  THR A CG2 1 
ATOM   447  N N   . VAL A 1 99  ? 24.473 55.579  59.078 1.00 44.47  ?  56  VAL A N   1 
ATOM   448  C CA  . VAL A 1 99  ? 25.237 54.837  60.073 1.00 46.05  ?  56  VAL A CA  1 
ATOM   449  C C   . VAL A 1 99  ? 26.517 55.614  60.325 1.00 56.10  ?  56  VAL A C   1 
ATOM   450  O O   . VAL A 1 99  ? 27.202 56.004  59.372 1.00 44.51  ?  56  VAL A O   1 
ATOM   451  C CB  . VAL A 1 99  ? 25.541 53.402  59.607 1.00 48.35  ?  56  VAL A CB  1 
ATOM   452  C CG1 . VAL A 1 99  ? 26.460 52.701  60.597 1.00 56.41  ?  56  VAL A CG1 1 
ATOM   453  C CG2 . VAL A 1 99  ? 24.246 52.619  59.412 1.00 49.06  ?  56  VAL A CG2 1 
ATOM   454  N N   . ASP A 1 100 ? 26.843 55.830  61.604 1.00 43.31  ?  57  ASP A N   1 
ATOM   455  C CA  . ASP A 1 100 ? 27.785 56.869  62.009 1.00 54.50  ?  57  ASP A CA  1 
ATOM   456  C C   . ASP A 1 100 ? 29.145 56.338  62.433 1.00 54.44  ?  57  ASP A C   1 
ATOM   457  O O   . ASP A 1 100 ? 29.941 57.098  62.994 1.00 62.50  ?  57  ASP A O   1 
ATOM   458  C CB  . ASP A 1 100 ? 27.193 57.697  63.153 1.00 55.97  ?  57  ASP A CB  1 
ATOM   459  C CG  . ASP A 1 100 ? 25.913 58.405  62.757 1.00 61.20  ?  57  ASP A CG  1 
ATOM   460  O OD1 . ASP A 1 100 ? 25.605 58.463  61.547 1.00 65.61  ?  57  ASP A OD1 1 
ATOM   461  O OD2 . ASP A 1 100 ? 25.206 58.899  63.658 1.00 70.28  ?  57  ASP A OD2 1 
ATOM   462  N N   . THR A 1 101 ? 29.441 55.067  62.172 1.00 50.64  ?  58  THR A N   1 
ATOM   463  C CA  . THR A 1 101 ? 30.688 54.470  62.644 1.00 57.22  ?  58  THR A CA  1 
ATOM   464  C C   . THR A 1 101 ? 31.900 55.354  62.342 1.00 68.14  ?  58  THR A C   1 
ATOM   465  O O   . THR A 1 101 ? 32.651 55.732  63.249 1.00 63.91  ?  58  THR A O   1 
ATOM   466  C CB  . THR A 1 101 ? 30.869 53.092  62.006 1.00 67.54  ?  58  THR A CB  1 
ATOM   467  O OG1 . THR A 1 101 ? 31.561 53.240  60.756 1.00 68.02  ?  58  THR A OG1 1 
ATOM   468  C CG2 . THR A 1 101 ? 29.513 52.446  61.754 1.00 58.73  ?  58  THR A CG2 1 
ATOM   469  N N   . GLY A 1 102 ? 32.112 55.685  61.065 1.00 54.42  ?  59  GLY A N   1 
ATOM   470  C CA  . GLY A 1 102 ? 33.331 56.355  60.651 1.00 50.48  ?  59  GLY A CA  1 
ATOM   471  C C   . GLY A 1 102 ? 33.313 57.870  60.701 1.00 54.04  ?  59  GLY A C   1 
ATOM   472  O O   . GLY A 1 102 ? 34.109 58.523  60.020 1.00 48.29  ?  59  GLY A O   1 
ATOM   473  N N   . ILE A 1 103 ? 32.431 58.442  61.522 1.00 50.13  ?  60  ILE A N   1 
ATOM   474  C CA  . ILE A 1 103 ? 32.249 59.892  61.530 1.00 54.09  ?  60  ILE A CA  1 
ATOM   475  C C   . ILE A 1 103 ? 33.555 60.610  61.846 1.00 66.04  ?  60  ILE A C   1 
ATOM   476  O O   . ILE A 1 103 ? 33.855 61.661  61.260 1.00 57.27  ?  60  ILE A O   1 
ATOM   477  C CB  . ILE A 1 103 ? 31.145 60.288  62.522 1.00 57.40  ?  60  ILE A CB  1 
ATOM   478  C CG1 . ILE A 1 103 ? 29.778 60.122  61.876 1.00 54.05  ?  60  ILE A CG1 1 
ATOM   479  C CG2 . ILE A 1 103 ? 31.351 61.718  62.986 1.00 66.78  ?  60  ILE A CG2 1 
ATOM   480  C CD1 . ILE A 1 103 ? 28.655 60.678  62.705 1.00 66.11  ?  60  ILE A CD1 1 
ATOM   481  N N   . ASP A 1 104 ? 34.336 60.078  62.794 1.00 62.82  ?  61  ASP A N   1 
ATOM   482  C CA  . ASP A 1 104 ? 35.606 60.709  63.153 1.00 66.98  ?  61  ASP A CA  1 
ATOM   483  C C   . ASP A 1 104 ? 36.516 60.851  61.949 1.00 64.59  ?  61  ASP A C   1 
ATOM   484  O O   . ASP A 1 104 ? 37.334 61.777  61.892 1.00 66.44  ?  61  ASP A O   1 
ATOM   485  C CB  . ASP A 1 104 ? 36.332 59.897  64.227 1.00 70.16  ?  61  ASP A CB  1 
ATOM   486  C CG  . ASP A 1 104 ? 35.492 59.673  65.454 1.00 83.01  ?  61  ASP A CG  1 
ATOM   487  O OD1 . ASP A 1 104 ? 34.727 60.592  65.822 1.00 73.92  ?  61  ASP A OD1 1 
ATOM   488  O OD2 . ASP A 1 104 ? 35.601 58.577  66.050 1.00 89.03  ?  61  ASP A OD2 1 
ATOM   489  N N   . HIS A 1 105 ? 36.415 59.930  60.999 1.00 61.21  ?  62  HIS A N   1 
ATOM   490  C CA  . HIS A 1 105 ? 37.232 59.955  59.799 1.00 66.71  ?  62  HIS A CA  1 
ATOM   491  C C   . HIS A 1 105 ? 36.548 60.675  58.644 1.00 54.91  ?  62  HIS A C   1 
ATOM   492  O O   . HIS A 1 105 ? 37.082 60.675  57.530 1.00 51.78  ?  62  HIS A O   1 
ATOM   493  C CB  . HIS A 1 105 ? 37.609 58.526  59.394 1.00 65.79  ?  62  HIS A CB  1 
ATOM   494  C CG  . HIS A 1 105 ? 38.567 57.868  60.340 1.00 81.95  ?  62  HIS A CG  1 
ATOM   495  N ND1 . HIS A 1 105 ? 38.854 58.385  61.586 1.00 84.57  ?  62  HIS A ND1 1 
ATOM   496  C CD2 . HIS A 1 105 ? 39.314 56.744  60.218 1.00 89.88  ?  62  HIS A CD2 1 
ATOM   497  C CE1 . HIS A 1 105 ? 39.730 57.604  62.194 1.00 91.92  ?  62  HIS A CE1 1 
ATOM   498  N NE2 . HIS A 1 105 ? 40.025 56.601  61.385 1.00 100.35 ?  62  HIS A NE2 1 
ATOM   499  N N   . GLY A 1 106 ? 35.396 61.298  58.891 1.00 47.77  ?  63  GLY A N   1 
ATOM   500  C CA  . GLY A 1 106 ? 34.679 62.041  57.876 1.00 52.11  ?  63  GLY A CA  1 
ATOM   501  C C   . GLY A 1 106 ? 33.670 61.245  57.080 1.00 42.27  ?  63  GLY A C   1 
ATOM   502  O O   . GLY A 1 106 ? 33.111 61.784  56.113 1.00 44.01  ?  63  GLY A O   1 
ATOM   503  N N   . THR A 1 107 ? 33.405 59.994  57.457 1.00 42.83  ?  64  THR A N   1 
ATOM   504  C CA  . THR A 1 107 ? 32.557 59.097  56.677 1.00 42.43  ?  64  THR A CA  1 
ATOM   505  C C   . THR A 1 107 ? 31.223 58.853  57.368 1.00 42.70  ?  64  THR A C   1 
ATOM   506  O O   . THR A 1 107 ? 31.172 58.573  58.574 1.00 43.88  ?  64  THR A O   1 
ATOM   507  C CB  . THR A 1 107 ? 33.244 57.756  56.424 1.00 49.05  ?  64  THR A CB  1 
ATOM   508  O OG1 . THR A 1 107 ? 34.431 57.964  55.654 1.00 47.19  ?  64  THR A OG1 1 
ATOM   509  C CG2 . THR A 1 107 ? 32.305 56.817  55.650 1.00 48.87  ?  64  THR A CG2 1 
ATOM   510  N N   . VAL A 1 108 ? 30.158 58.940  56.581 1.00 40.18  ?  65  VAL A N   1 
ATOM   511  C CA  . VAL A 1 108 ? 28.793 58.639  56.975 1.00 38.72  ?  65  VAL A CA  1 
ATOM   512  C C   . VAL A 1 108 ? 28.242 57.639  55.967 1.00 43.95  ?  65  VAL A C   1 
ATOM   513  O O   . VAL A 1 108 ? 28.309 57.885  54.758 1.00 38.28  ?  65  VAL A O   1 
ATOM   514  C CB  . VAL A 1 108 ? 27.939 59.919  56.988 1.00 40.40  ?  65  VAL A CB  1 
ATOM   515  C CG1 . VAL A 1 108 ? 26.454 59.591  57.102 1.00 40.64  ?  65  VAL A CG1 1 
ATOM   516  C CG2 . VAL A 1 108 ? 28.406 60.853  58.122 1.00 46.98  ?  65  VAL A CG2 1 
ATOM   517  N N   . LEU A 1 109 ? 27.709 56.514  56.446 1.00 42.64  ?  66  LEU A N   1 
ATOM   518  C CA  . LEU A 1 109 ? 27.081 55.542  55.548 1.00 44.99  ?  66  LEU A CA  1 
ATOM   519  C C   . LEU A 1 109 ? 25.604 55.895  55.373 1.00 42.19  ?  66  LEU A C   1 
ATOM   520  O O   . LEU A 1 109 ? 24.853 55.970  56.353 1.00 40.74  ?  66  LEU A O   1 
ATOM   521  C CB  . LEU A 1 109 ? 27.233 54.110  56.063 1.00 39.57  ?  66  LEU A CB  1 
ATOM   522  C CG  . LEU A 1 109 ? 26.588 53.021  55.186 1.00 42.95  ?  66  LEU A CG  1 
ATOM   523  C CD1 . LEU A 1 109 ? 27.308 52.911  53.850 1.00 35.18  ?  66  LEU A CD1 1 
ATOM   524  C CD2 . LEU A 1 109 ? 26.570 51.670  55.886 1.00 45.03  ?  66  LEU A CD2 1 
ATOM   525  N N   . VAL A 1 110 ? 25.192 56.110  54.127 1.00 35.13  ?  67  VAL A N   1 
ATOM   526  C CA  . VAL A 1 110 ? 23.825 56.493  53.798 1.00 36.35  ?  67  VAL A CA  1 
ATOM   527  C C   . VAL A 1 110 ? 23.071 55.254  53.330 1.00 44.36  ?  67  VAL A C   1 
ATOM   528  O O   . VAL A 1 110 ? 23.536 54.531  52.440 1.00 42.24  ?  67  VAL A O   1 
ATOM   529  C CB  . VAL A 1 110 ? 23.803 57.597  52.726 1.00 34.85  ?  67  VAL A CB  1 
ATOM   530  C CG1 . VAL A 1 110 ? 22.395 57.801  52.199 1.00 36.65  ?  67  VAL A CG1 1 
ATOM   531  C CG2 . VAL A 1 110 ? 24.377 58.907  53.291 1.00 35.00  ?  67  VAL A CG2 1 
ATOM   532  N N   . LEU A 1 111 ? 21.915 54.999  53.935 1.00 41.22  ?  68  LEU A N   1 
ATOM   533  C CA  . LEU A 1 111 ? 21.076 53.860  53.581 1.00 37.81  ?  68  LEU A CA  1 
ATOM   534  C C   . LEU A 1 111 ? 19.924 54.371  52.737 1.00 40.89  ?  68  LEU A C   1 
ATOM   535  O O   . LEU A 1 111 ? 19.124 55.186  53.204 1.00 44.99  ?  68  LEU A O   1 
ATOM   536  C CB  . LEU A 1 111 ? 20.562 53.142  54.830 1.00 48.47  ?  68  LEU A CB  1 
ATOM   537  C CG  . LEU A 1 111 ? 21.655 52.592  55.745 1.00 42.58  ?  68  LEU A CG  1 
ATOM   538  C CD1 . LEU A 1 111 ? 21.050 51.928  56.982 1.00 54.90  ?  68  LEU A CD1 1 
ATOM   539  C CD2 . LEU A 1 111 ? 22.552 51.620  54.985 1.00 41.00  ?  68  LEU A CD2 1 
ATOM   540  N N   . LEU A 1 112 ? 19.864 53.930  51.485 1.00 38.70  ?  69  LEU A N   1 
ATOM   541  C CA  . LEU A 1 112 ? 18.888 54.466  50.553 1.00 42.96  ?  69  LEU A CA  1 
ATOM   542  C C   . LEU A 1 112 ? 18.596 53.417  49.491 1.00 47.21  ?  69  LEU A C   1 
ATOM   543  O O   . LEU A 1 112 ? 19.517 52.758  48.999 1.00 40.62  ?  69  LEU A O   1 
ATOM   544  C CB  . LEU A 1 112 ? 19.410 55.758  49.909 1.00 41.39  ?  69  LEU A CB  1 
ATOM   545  C CG  . LEU A 1 112 ? 18.468 56.569  49.027 1.00 46.95  ?  69  LEU A CG  1 
ATOM   546  C CD1 . LEU A 1 112 ? 17.307 57.060  49.866 1.00 51.57  ?  69  LEU A CD1 1 
ATOM   547  C CD2 . LEU A 1 112 ? 19.215 57.735  48.398 1.00 40.57  ?  69  LEU A CD2 1 
ATOM   548  N N   . ASP A 1 113 ? 17.314 53.273  49.141 1.00 44.13  ?  70  ASP A N   1 
ATOM   549  C CA  . ASP A 1 113 ? 16.879 52.345  48.092 1.00 46.48  ?  70  ASP A CA  1 
ATOM   550  C C   . ASP A 1 113 ? 17.466 50.952  48.295 1.00 45.41  ?  70  ASP A C   1 
ATOM   551  O O   . ASP A 1 113 ? 17.804 50.254  47.337 1.00 44.72  ?  70  ASP A O   1 
ATOM   552  C CB  . ASP A 1 113 ? 17.241 52.871  46.705 1.00 46.35  ?  70  ASP A CB  1 
ATOM   553  C CG  . ASP A 1 113 ? 16.513 54.153  46.355 1.00 46.50  ?  70  ASP A CG  1 
ATOM   554  O OD1 . ASP A 1 113 ? 15.808 54.684  47.225 1.00 48.29  ?  70  ASP A OD1 1 
ATOM   555  O OD2 . ASP A 1 113 ? 16.655 54.626  45.199 1.00 48.03  ?  70  ASP A OD2 1 
ATOM   556  N N   . GLY A 1 114 ? 17.606 50.545  49.552 1.00 40.96  ?  71  GLY A N   1 
ATOM   557  C CA  . GLY A 1 114 ? 18.142 49.231  49.844 1.00 45.95  ?  71  GLY A CA  1 
ATOM   558  C C   . GLY A 1 114 ? 19.635 49.070  49.658 1.00 48.87  ?  71  GLY A C   1 
ATOM   559  O O   . GLY A 1 114 ? 20.121 47.934  49.671 1.00 51.52  ?  71  GLY A O   1 
ATOM   560  N N   . GLU A 1 115 ? 20.380 50.158  49.487 1.00 40.86  ?  72  GLU A N   1 
ATOM   561  C CA  . GLU A 1 115 ? 21.825 50.113  49.322 1.00 41.84  ?  72  GLU A CA  1 
ATOM   562  C C   . GLU A 1 115 ? 22.486 50.942  50.413 1.00 40.49  ?  72  GLU A C   1 
ATOM   563  O O   . GLU A 1 115 ? 21.838 51.721  51.113 1.00 42.47  ?  72  GLU A O   1 
ATOM   564  C CB  . GLU A 1 115 ? 22.241 50.635  47.938 1.00 41.15  ?  72  GLU A CB  1 
ATOM   565  C CG  . GLU A 1 115 ? 21.558 49.924  46.786 1.00 40.66  ?  72  GLU A CG  1 
ATOM   566  C CD  . GLU A 1 115 ? 22.032 48.492  46.636 1.00 50.98  ?  72  GLU A CD  1 
ATOM   567  O OE1 . GLU A 1 115 ? 23.089 48.144  47.214 1.00 47.62  ?  72  GLU A OE1 1 
ATOM   568  O OE2 . GLU A 1 115 ? 21.349 47.711  45.941 1.00 54.10  ?  72  GLU A OE2 1 
ATOM   569  N N   . GLY A 1 116 ? 23.795 50.771  50.546 1.00 41.61  ?  73  GLY A N   1 
ATOM   570  C CA  . GLY A 1 116 ? 24.575 51.598  51.443 1.00 41.74  ?  73  GLY A CA  1 
ATOM   571  C C   . GLY A 1 116 ? 25.667 52.327  50.688 1.00 41.46  ?  73  GLY A C   1 
ATOM   572  O O   . GLY A 1 116 ? 26.514 51.691  50.051 1.00 40.00  ?  73  GLY A O   1 
ATOM   573  N N   . ILE A 1 117 ? 25.648 53.657  50.732 1.00 36.34  ?  74  ILE A N   1 
ATOM   574  C CA  . ILE A 1 117 ? 26.636 54.491  50.049 1.00 34.80  ?  74  ILE A CA  1 
ATOM   575  C C   . ILE A 1 117 ? 27.452 55.228  51.110 1.00 39.16  ?  74  ILE A C   1 
ATOM   576  O O   . ILE A 1 117 ? 26.896 56.000  51.903 1.00 38.35  ?  74  ILE A O   1 
ATOM   577  C CB  . ILE A 1 117 ? 25.958 55.474  49.087 1.00 31.66  ?  74  ILE A CB  1 
ATOM   578  C CG1 . ILE A 1 117 ? 25.038 54.719  48.115 1.00 36.02  ?  74  ILE A CG1 1 
ATOM   579  C CG2 . ILE A 1 117 ? 26.999 56.326  48.335 1.00 34.89  ?  74  ILE A CG2 1 
ATOM   580  C CD1 . ILE A 1 117 ? 25.765 53.683  47.286 1.00 35.33  ?  74  ILE A CD1 1 
ATOM   581  N N   . GLU A 1 118 ? 28.764 55.001  51.129 1.00 35.03  ?  75  GLU A N   1 
ATOM   582  C CA  . GLU A 1 118 ? 29.623 55.772  52.020 1.00 36.63  ?  75  GLU A CA  1 
ATOM   583  C C   . GLU A 1 118 ? 29.809 57.181  51.471 1.00 40.26  ?  75  GLU A C   1 
ATOM   584  O O   . GLU A 1 118 ? 30.188 57.360  50.308 1.00 38.94  ?  75  GLU A O   1 
ATOM   585  C CB  . GLU A 1 118 ? 30.976 55.099  52.184 1.00 38.71  ?  75  GLU A CB  1 
ATOM   586  C CG  . GLU A 1 118 ? 30.910 53.680  52.699 1.00 54.13  ?  75  GLU A CG  1 
ATOM   587  C CD  . GLU A 1 118 ? 32.179 53.286  53.420 1.00 71.03  ?  75  GLU A CD  1 
ATOM   588  O OE1 . GLU A 1 118 ? 33.260 53.795  53.045 1.00 74.29  ?  75  GLU A OE1 1 
ATOM   589  O OE2 . GLU A 1 118 ? 32.090 52.485  54.376 1.00 80.42  ?  75  GLU A OE2 1 
ATOM   590  N N   . VAL A 1 119 ? 29.524 58.180  52.300 1.00 35.14  ?  76  VAL A N   1 
ATOM   591  C CA  . VAL A 1 119 ? 29.721 59.584  51.946 1.00 32.44  ?  76  VAL A CA  1 
ATOM   592  C C   . VAL A 1 119 ? 30.827 60.123  52.839 1.00 42.18  ?  76  VAL A C   1 
ATOM   593  O O   . VAL A 1 119 ? 30.696 60.123  54.075 1.00 34.23  ?  76  VAL A O   1 
ATOM   594  C CB  . VAL A 1 119 ? 28.431 60.400  52.108 1.00 33.98  ?  76  VAL A CB  1 
ATOM   595  C CG1 . VAL A 1 119 ? 28.679 61.875  51.762 1.00 33.20  ?  76  VAL A CG1 1 
ATOM   596  C CG2 . VAL A 1 119 ? 27.302 59.796  51.266 1.00 32.52  ?  76  VAL A CG2 1 
ATOM   597  N N   . THR A 1 120 ? 31.925 60.559  52.230 1.00 32.93  ?  77  THR A N   1 
ATOM   598  C CA  . THR A 1 120 ? 33.101 60.975  52.989 1.00 38.43  ?  77  THR A CA  1 
ATOM   599  C C   . THR A 1 120 ? 33.471 62.410  52.644 1.00 36.92  ?  77  THR A C   1 
ATOM   600  O O   . THR A 1 120 ? 33.579 62.763  51.469 1.00 33.56  ?  77  THR A O   1 
ATOM   601  C CB  . THR A 1 120 ? 34.278 60.035  52.717 1.00 43.31  ?  77  THR A CB  1 
ATOM   602  O OG1 . THR A 1 120 ? 33.904 58.700  53.085 1.00 41.35  ?  77  THR A OG1 1 
ATOM   603  C CG2 . THR A 1 120 ? 35.512 60.463  53.522 1.00 39.54  ?  77  THR A CG2 1 
ATOM   604  N N   . THR A 1 121 ? 33.669 63.240  53.668 1.00 33.79  ?  78  THR A N   1 
ATOM   605  C CA  . THR A 1 121 ? 34.074 64.613  53.420 1.00 28.91  ?  78  THR A CA  1 
ATOM   606  C C   . THR A 1 121 ? 35.492 64.634  52.856 1.00 30.96  ?  78  THR A C   1 
ATOM   607  O O   . THR A 1 121 ? 36.298 63.753  53.146 1.00 35.49  ?  78  THR A O   1 
ATOM   608  C CB  . THR A 1 121 ? 34.002 65.439  54.719 1.00 34.48  ?  78  THR A CB  1 
ATOM   609  O OG1 . THR A 1 121 ? 33.796 66.814  54.386 1.00 40.75  ?  78  THR A OG1 1 
ATOM   610  C CG2 . THR A 1 121 ? 35.294 65.327  55.478 1.00 40.50  ?  78  THR A CG2 1 
ATOM   611  N N   . PHE A 1 122 ? 35.776 65.618  51.995 1.00 33.85  ?  79  PHE A N   1 
ATOM   612  C CA  . PHE A 1 122 ? 37.139 65.820  51.505 1.00 35.62  ?  79  PHE A CA  1 
ATOM   613  C C   . PHE A 1 122 ? 38.111 65.764  52.680 1.00 38.11  ?  79  PHE A C   1 
ATOM   614  O O   . PHE A 1 122 ? 37.991 66.548  53.626 1.00 37.15  ?  79  PHE A O   1 
ATOM   615  C CB  . PHE A 1 122 ? 37.273 67.178  50.805 1.00 36.58  ?  79  PHE A CB  1 
ATOM   616  C CG  . PHE A 1 122 ? 36.319 67.413  49.659 1.00 37.09  ?  79  PHE A CG  1 
ATOM   617  C CD1 . PHE A 1 122 ? 35.882 66.377  48.841 1.00 33.78  ?  79  PHE A CD1 1 
ATOM   618  C CD2 . PHE A 1 122 ? 35.901 68.706  49.370 1.00 38.19  ?  79  PHE A CD2 1 
ATOM   619  C CE1 . PHE A 1 122 ? 35.022 66.632  47.767 1.00 35.61  ?  79  PHE A CE1 1 
ATOM   620  C CE2 . PHE A 1 122 ? 35.048 68.969  48.300 1.00 36.91  ?  79  PHE A CE2 1 
ATOM   621  C CZ  . PHE A 1 122 ? 34.603 67.929  47.501 1.00 35.79  ?  79  PHE A CZ  1 
ATOM   622  N N   . ARG A 1 123 ? 39.076 64.846  52.635 1.00 35.01  ?  80  ARG A N   1 
ATOM   623  C CA  . ARG A 1 123 ? 39.947 64.662  53.790 1.00 36.56  ?  80  ARG A CA  1 
ATOM   624  C C   . ARG A 1 123 ? 41.304 64.137  53.352 1.00 41.70  ?  80  ARG A C   1 
ATOM   625  O O   . ARG A 1 123 ? 41.467 63.593  52.255 1.00 38.08  ?  80  ARG A O   1 
ATOM   626  C CB  . ARG A 1 123 ? 39.332 63.674  54.793 1.00 34.62  ?  80  ARG A CB  1 
ATOM   627  C CG  . ARG A 1 123 ? 39.262 62.292  54.175 1.00 47.21  ?  80  ARG A CG  1 
ATOM   628  C CD  . ARG A 1 123 ? 38.985 61.198  55.158 1.00 56.27  ?  80  ARG A CD  1 
ATOM   629  N NE  . ARG A 1 123 ? 39.011 59.902  54.484 1.00 62.19  ?  80  ARG A NE  1 
ATOM   630  C CZ  . ARG A 1 123 ? 38.546 58.777  55.015 1.00 63.22  ?  80  ARG A CZ  1 
ATOM   631  N NH1 . ARG A 1 123 ? 38.015 58.791  56.228 1.00 64.23  ?  80  ARG A NH1 1 
ATOM   632  N NH2 . ARG A 1 123 ? 38.609 57.642  54.332 1.00 60.18  ?  80  ARG A NH2 1 
ATOM   633  N N   . THR A 1 124 ? 42.282 64.293  54.236 1.00 35.58  ?  81  THR A N   1 
ATOM   634  C CA  . THR A 1 124 ? 43.537 63.572  54.144 1.00 35.03  ?  81  THR A CA  1 
ATOM   635  C C   . THR A 1 124 ? 43.772 62.829  55.448 1.00 48.14  ?  81  THR A C   1 
ATOM   636  O O   . THR A 1 124 ? 43.268 63.220  56.506 1.00 52.76  ?  81  THR A O   1 
ATOM   637  C CB  . THR A 1 124 ? 44.729 64.488  53.874 1.00 48.22  ?  81  THR A CB  1 
ATOM   638  O OG1 . THR A 1 124 ? 44.988 65.274  55.043 1.00 52.17  ?  81  THR A OG1 1 
ATOM   639  C CG2 . THR A 1 124 ? 44.457 65.394  52.688 1.00 45.12  ?  81  THR A CG2 1 
ATOM   640  N N   . GLU A 1 125 ? 44.538 61.751  55.361 1.00 49.04  ?  82  GLU A N   1 
ATOM   641  C CA  . GLU A 1 125 ? 44.890 60.948  56.518 1.00 56.64  ?  82  GLU A CA  1 
ATOM   642  C C   . GLU A 1 125 ? 46.394 60.734  56.545 1.00 64.23  ?  82  GLU A C   1 
ATOM   643  O O   . GLU A 1 125 ? 47.075 60.809  55.518 1.00 71.94  ?  82  GLU A O   1 
ATOM   644  C CB  . GLU A 1 125 ? 44.191 59.591  56.499 1.00 52.80  ?  82  GLU A CB  1 
ATOM   645  C CG  . GLU A 1 125 ? 42.699 59.654  56.652 1.00 61.47  ?  82  GLU A CG  1 
ATOM   646  C CD  . GLU A 1 125 ? 42.076 58.275  56.647 1.00 78.25  ?  82  GLU A CD  1 
ATOM   647  O OE1 . GLU A 1 125 ? 42.134 57.596  55.595 1.00 77.17  ?  82  GLU A OE1 1 
ATOM   648  O OE2 . GLU A 1 125 ? 41.547 57.862  57.703 1.00 77.80  ?  82  GLU A OE2 1 
ATOM   649  N N   . SER A 1 126 ? 46.904 60.460  57.740 1.00 71.23  ?  83  SER A N   1 
ATOM   650  C CA  . SER A 1 126 ? 48.276 60.002  57.893 1.00 79.24  ?  83  SER A CA  1 
ATOM   651  C C   . SER A 1 126 ? 48.346 59.164  59.157 1.00 79.94  ?  83  SER A C   1 
ATOM   652  O O   . SER A 1 126 ? 47.663 59.457  60.141 1.00 80.40  ?  83  SER A O   1 
ATOM   653  C CB  . SER A 1 126 ? 49.269 61.168  57.957 1.00 78.51  ?  83  SER A CB  1 
ATOM   654  O OG  . SER A 1 126 ? 50.558 60.755  57.533 1.00 80.90  ?  83  SER A OG  1 
ATOM   655  N N   . SER A 1 127 ? 49.157 58.115  59.117 1.00 84.37  ?  84  SER A N   1 
ATOM   656  C CA  . SER A 1 127 ? 49.298 57.187  60.230 1.00 96.83  ?  84  SER A CA  1 
ATOM   657  C C   . SER A 1 127 ? 50.636 57.435  60.910 1.00 115.74 ?  84  SER A C   1 
ATOM   658  O O   . SER A 1 127 ? 51.690 57.302  60.277 1.00 104.26 ?  84  SER A O   1 
ATOM   659  C CB  . SER A 1 127 ? 49.206 55.738  59.752 1.00 80.79  ?  84  SER A CB  1 
ATOM   660  O OG  . SER A 1 127 ? 48.047 55.526  58.969 1.00 77.14  ?  84  SER A OG  1 
ATOM   661  N N   . TYR A 1 128 ? 50.592 57.805  62.188 1.00 128.29 ?  85  TYR A N   1 
ATOM   662  C CA  . TYR A 1 128 ? 51.811 57.832  62.977 1.00 134.65 ?  85  TYR A CA  1 
ATOM   663  C C   . TYR A 1 128 ? 52.407 56.427  63.039 1.00 136.37 ?  85  TYR A C   1 
ATOM   664  O O   . TYR A 1 128 ? 51.741 55.428  62.753 1.00 129.96 ?  85  TYR A O   1 
ATOM   665  C CB  . TYR A 1 128 ? 51.535 58.360  64.385 1.00 137.93 ?  85  TYR A CB  1 
ATOM   666  C CG  . TYR A 1 128 ? 50.864 59.717  64.427 1.00 139.24 ?  85  TYR A CG  1 
ATOM   667  C CD1 . TYR A 1 128 ? 51.582 60.879  64.178 1.00 143.03 ?  85  TYR A CD1 1 
ATOM   668  C CD2 . TYR A 1 128 ? 49.515 59.834  64.730 1.00 131.34 ?  85  TYR A CD2 1 
ATOM   669  C CE1 . TYR A 1 128 ? 50.971 62.120  64.222 1.00 139.92 ?  85  TYR A CE1 1 
ATOM   670  C CE2 . TYR A 1 128 ? 48.897 61.067  64.777 1.00 124.91 ?  85  TYR A CE2 1 
ATOM   671  C CZ  . TYR A 1 128 ? 49.628 62.206  64.523 1.00 129.90 ?  85  TYR A CZ  1 
ATOM   672  O OH  . TYR A 1 128 ? 49.012 63.434  64.570 1.00 122.53 ?  85  TYR A OH  1 
ATOM   673  N N   . SER A 1 129 ? 53.682 56.355  63.419 1.00 137.76 ?  86  SER A N   1 
ATOM   674  C CA  . SER A 1 129 ? 54.369 55.069  63.416 1.00 128.03 ?  86  SER A CA  1 
ATOM   675  C C   . SER A 1 129 ? 53.786 54.090  64.428 1.00 132.63 ?  86  SER A C   1 
ATOM   676  O O   . SER A 1 129 ? 53.957 52.877  64.262 1.00 113.18 ?  86  SER A O   1 
ATOM   677  C CB  . SER A 1 129 ? 55.860 55.268  63.682 1.00 113.83 ?  86  SER A CB  1 
ATOM   678  O OG  . SER A 1 129 ? 56.072 55.914  64.923 1.00 131.42 ?  86  SER A OG  1 
ATOM   679  N N   . ASP A 1 130 ? 53.102 54.576  65.463 1.00 144.76 ?  87  ASP A N   1 
ATOM   680  C CA  . ASP A 1 130 ? 52.557 53.724  66.520 1.00 144.75 ?  87  ASP A CA  1 
ATOM   681  C C   . ASP A 1 130 ? 51.061 53.544  66.279 1.00 141.08 ?  87  ASP A C   1 
ATOM   682  O O   . ASP A 1 130 ? 50.262 54.441  66.559 1.00 144.38 ?  87  ASP A O   1 
ATOM   683  C CB  . ASP A 1 130 ? 52.837 54.322  67.894 1.00 151.05 ?  87  ASP A CB  1 
ATOM   684  C CG  . ASP A 1 130 ? 52.495 53.371  69.024 1.00 154.27 ?  87  ASP A CG  1 
ATOM   685  O OD1 . ASP A 1 130 ? 51.396 52.779  68.995 1.00 150.29 -1 87  ASP A OD1 1 
ATOM   686  O OD2 . ASP A 1 130 ? 53.331 53.207  69.937 1.00 158.64 ?  87  ASP A OD2 1 
ATOM   687  N N   . ASN A 1 131 ? 50.685 52.375  65.767 1.00 133.68 ?  88  ASN A N   1 
ATOM   688  C CA  . ASN A 1 131 ? 49.289 52.082  65.459 1.00 120.22 ?  88  ASN A CA  1 
ATOM   689  C C   . ASN A 1 131 ? 48.494 51.803  66.731 1.00 113.29 ?  88  ASN A C   1 
ATOM   690  O O   . ASN A 1 131 ? 47.417 51.210  66.682 1.00 103.90 ?  88  ASN A O   1 
ATOM   691  C CB  . ASN A 1 131 ? 49.190 50.896  64.491 1.00 89.99  ?  88  ASN A CB  1 
ATOM   692  C CG  . ASN A 1 131 ? 49.676 49.592  65.102 1.00 74.95  ?  88  ASN A CG  1 
ATOM   693  O OD1 . ASN A 1 131 ? 49.216 49.181  66.163 1.00 83.32  ?  88  ASN A OD1 1 
ATOM   694  N ND2 . ASN A 1 131 ? 50.612 48.937  64.429 1.00 60.56  ?  88  ASN A ND2 1 
ATOM   695  N N   . SER A 1 136 ? 44.964 60.292  62.418 1.00 67.01  ?  93  SER A N   1 
ATOM   696  C CA  . SER A 1 136 ? 45.185 61.723  62.218 1.00 77.18  ?  93  SER A CA  1 
ATOM   697  C C   . SER A 1 136 ? 44.534 62.205  60.924 1.00 63.51  ?  93  SER A C   1 
ATOM   698  O O   . SER A 1 136 ? 45.168 62.233  59.870 1.00 70.92  ?  93  SER A O   1 
ATOM   699  C CB  . SER A 1 136 ? 46.680 62.040  62.198 1.00 84.88  ?  93  SER A CB  1 
ATOM   700  O OG  . SER A 1 136 ? 47.268 61.648  60.969 1.00 91.63  ?  93  SER A OG  1 
ATOM   701  N N   . VAL A 1 137 ? 43.267 62.597  61.017 1.00 62.15  ?  94  VAL A N   1 
ATOM   702  C CA  . VAL A 1 137 ? 42.454 62.947  59.859 1.00 57.45  ?  94  VAL A CA  1 
ATOM   703  C C   . VAL A 1 137 ? 42.334 64.461  59.783 1.00 57.46  ?  94  VAL A C   1 
ATOM   704  O O   . VAL A 1 137 ? 42.053 65.120  60.788 1.00 56.00  ?  94  VAL A O   1 
ATOM   705  C CB  . VAL A 1 137 ? 41.069 62.286  59.949 1.00 61.83  ?  94  VAL A CB  1 
ATOM   706  C CG1 . VAL A 1 137 ? 40.276 62.517  58.672 1.00 53.88  ?  94  VAL A CG1 1 
ATOM   707  C CG2 . VAL A 1 137 ? 41.218 60.801  60.259 1.00 62.80  ?  94  VAL A CG2 1 
ATOM   708  N N   . GLU A 1 138 ? 42.553 65.019  58.597 1.00 48.90  ?  95  GLU A N   1 
ATOM   709  C CA  . GLU A 1 138 ? 42.354 66.442  58.353 1.00 49.02  ?  95  GLU A CA  1 
ATOM   710  C C   . GLU A 1 138 ? 41.263 66.625  57.311 1.00 47.41  ?  95  GLU A C   1 
ATOM   711  O O   . GLU A 1 138 ? 41.434 66.221  56.155 1.00 41.61  ?  95  GLU A O   1 
ATOM   712  C CB  . GLU A 1 138 ? 43.640 67.114  57.869 1.00 52.96  ?  95  GLU A CB  1 
ATOM   713  C CG  . GLU A 1 138 ? 44.745 67.177  58.892 1.00 62.95  ?  95  GLU A CG  1 
ATOM   714  C CD  . GLU A 1 138 ? 45.821 68.158  58.484 1.00 79.68  ?  95  GLU A CD  1 
ATOM   715  O OE1 . GLU A 1 138 ? 45.700 68.739  57.378 1.00 81.84  ?  95  GLU A OE1 1 
ATOM   716  O OE2 . GLU A 1 138 ? 46.779 68.351  59.263 1.00 90.48  ?  95  GLU A OE2 1 
ATOM   717  N N   . PHE A 1 139 ? 40.159 67.246  57.703 1.00 39.52  ?  96  PHE A N   1 
ATOM   718  C CA  . PHE A 1 139 ? 39.196 67.683  56.704 1.00 47.24  ?  96  PHE A CA  1 
ATOM   719  C C   . PHE A 1 139 ? 39.811 68.808  55.880 1.00 48.04  ?  96  PHE A C   1 
ATOM   720  O O   . PHE A 1 139 ? 40.464 69.707  56.420 1.00 47.49  ?  96  PHE A O   1 
ATOM   721  C CB  . PHE A 1 139 ? 37.892 68.138  57.367 1.00 46.33  ?  96  PHE A CB  1 
ATOM   722  C CG  . PHE A 1 139 ? 37.174 67.044  58.123 1.00 42.87  ?  96  PHE A CG  1 
ATOM   723  C CD1 . PHE A 1 139 ? 37.613 65.730  58.065 1.00 39.84  ?  96  PHE A CD1 1 
ATOM   724  C CD2 . PHE A 1 139 ? 36.055 67.334  58.885 1.00 38.84  ?  96  PHE A CD2 1 
ATOM   725  C CE1 . PHE A 1 139 ? 36.960 64.728  58.759 1.00 42.16  ?  96  PHE A CE1 1 
ATOM   726  C CE2 . PHE A 1 139 ? 35.387 66.333  59.584 1.00 41.91  ?  96  PHE A CE2 1 
ATOM   727  C CZ  . PHE A 1 139 ? 35.836 65.025  59.519 1.00 43.83  ?  96  PHE A CZ  1 
ATOM   728  N N   . VAL A 1 140 ? 39.643 68.728  54.559 1.00 43.92  ?  97  VAL A N   1 
ATOM   729  C CA  . VAL A 1 140 ? 40.179 69.715  53.633 1.00 42.88  ?  97  VAL A CA  1 
ATOM   730  C C   . VAL A 1 140 ? 39.018 70.279  52.824 1.00 42.63  ?  97  VAL A C   1 
ATOM   731  O O   . VAL A 1 140 ? 37.914 69.727  52.804 1.00 43.14  ?  97  VAL A O   1 
ATOM   732  C CB  . VAL A 1 140 ? 41.289 69.139  52.716 1.00 47.83  ?  97  VAL A CB  1 
ATOM   733  C CG1 . VAL A 1 140 ? 42.477 68.655  53.558 1.00 44.47  ?  97  VAL A CG1 1 
ATOM   734  C CG2 . VAL A 1 140 ? 40.762 68.002  51.809 1.00 37.11  ?  97  VAL A CG2 1 
ATOM   735  N N   . LEU A 1 141 ? 39.264 71.415  52.175 1.00 38.34  ?  98  LEU A N   1 
ATOM   736  C CA  . LEU A 1 141 ? 38.172 72.179  51.591 1.00 43.74  ?  98  LEU A CA  1 
ATOM   737  C C   . LEU A 1 141 ? 37.951 71.915  50.108 1.00 43.11  ?  98  LEU A C   1 
ATOM   738  O O   . LEU A 1 141 ? 36.943 72.382  49.567 1.00 47.69  ?  98  LEU A O   1 
ATOM   739  C CB  . LEU A 1 141 ? 38.389 73.685  51.811 1.00 44.13  ?  98  LEU A CB  1 
ATOM   740  C CG  . LEU A 1 141 ? 38.241 74.156  53.262 1.00 52.11  ?  98  LEU A CG  1 
ATOM   741  C CD1 . LEU A 1 141 ? 38.364 75.670  53.371 1.00 46.99  ?  98  LEU A CD1 1 
ATOM   742  C CD2 . LEU A 1 141 ? 36.916 73.686  53.855 1.00 46.97  ?  98  LEU A CD2 1 
ATOM   743  N N   . SER A 1 142 ? 38.841 71.183  49.436 1.00 43.39  ?  99  SER A N   1 
ATOM   744  C CA  . SER A 1 142 ? 38.686 70.932  48.010 1.00 37.54  ?  99  SER A CA  1 
ATOM   745  C C   . SER A 1 142 ? 38.834 69.448  47.698 1.00 40.03  ?  99  SER A C   1 
ATOM   746  O O   . SER A 1 142 ? 39.472 68.690  48.430 1.00 38.01  ?  99  SER A O   1 
ATOM   747  C CB  . SER A 1 142 ? 39.716 71.704  47.172 1.00 46.57  ?  99  SER A CB  1 
ATOM   748  O OG  . SER A 1 142 ? 41.025 71.216  47.437 1.00 47.75  ?  99  SER A OG  1 
ATOM   749  N N   . LEU A 1 143 ? 38.270 69.058  46.556 1.00 37.08  ?  100 LEU A N   1 
ATOM   750  C CA  . LEU A 1 143 ? 38.398 67.681  46.086 1.00 38.17  ?  100 LEU A CA  1 
ATOM   751  C C   . LEU A 1 143 ? 39.849 67.326  45.781 1.00 39.98  ?  100 LEU A C   1 
ATOM   752  O O   . LEU A 1 143 ? 40.323 66.239  46.139 1.00 34.57  ?  100 LEU A O   1 
ATOM   753  C CB  . LEU A 1 143 ? 37.541 67.483  44.835 1.00 34.27  ?  100 LEU A CB  1 
ATOM   754  C CG  . LEU A 1 143 ? 37.719 66.131  44.131 1.00 34.30  ?  100 LEU A CG  1 
ATOM   755  C CD1 . LEU A 1 143 ? 37.325 64.976  45.045 1.00 32.76  ?  100 LEU A CD1 1 
ATOM   756  C CD2 . LEU A 1 143 ? 36.928 66.084  42.832 1.00 32.02  ?  100 LEU A CD2 1 
ATOM   757  N N   . GLU A 1 144 ? 40.560 68.221  45.087 1.00 39.73  ?  101 GLU A N   1 
ATOM   758  C CA  . GLU A 1 144 ? 41.916 67.912  44.648 1.00 44.91  ?  101 GLU A CA  1 
ATOM   759  C C   . GLU A 1 144 ? 42.866 67.713  45.820 1.00 35.17  ?  101 GLU A C   1 
ATOM   760  O O   . GLU A 1 144 ? 43.795 66.905  45.722 1.00 42.71  ?  101 GLU A O   1 
ATOM   761  C CB  . GLU A 1 144 ? 42.437 69.012  43.720 1.00 54.22  ?  101 GLU A CB  1 
ATOM   762  C CG  . GLU A 1 144 ? 42.351 68.664  42.219 1.00 67.86  ?  101 GLU A CG  1 
ATOM   763  C CD  . GLU A 1 144 ? 40.976 68.936  41.593 1.00 81.25  ?  101 GLU A CD  1 
ATOM   764  O OE1 . GLU A 1 144 ? 40.002 69.190  42.341 1.00 78.96  ?  101 GLU A OE1 1 
ATOM   765  O OE2 . GLU A 1 144 ? 40.871 68.900  40.343 1.00 73.36  ?  101 GLU A OE2 1 
ATOM   766  N N   . GLU A 1 145 ? 42.659 68.432  46.927 1.00 38.93  ?  102 GLU A N   1 
ATOM   767  C CA  . GLU A 1 145 ? 43.465 68.193  48.126 1.00 36.90  ?  102 GLU A CA  1 
ATOM   768  C C   . GLU A 1 145 ? 43.271 66.777  48.644 1.00 42.93  ?  102 GLU A C   1 
ATOM   769  O O   . GLU A 1 145 ? 44.201 66.179  49.202 1.00 43.61  ?  102 GLU A O   1 
ATOM   770  C CB  . GLU A 1 145 ? 43.105 69.190  49.224 1.00 46.34  ?  102 GLU A CB  1 
ATOM   771  C CG  . GLU A 1 145 ? 43.686 70.579  49.073 1.00 49.48  ?  102 GLU A CG  1 
ATOM   772  C CD  . GLU A 1 145 ? 43.048 71.532  50.054 1.00 50.76  ?  102 GLU A CD  1 
ATOM   773  O OE1 . GLU A 1 145 ? 41.931 72.007  49.761 1.00 56.33  ?  102 GLU A OE1 1 
ATOM   774  O OE2 . GLU A 1 145 ? 43.628 71.773  51.136 1.00 58.28  ?  102 GLU A OE2 1 
ATOM   775  N N   . ASP A 1 146 ? 42.050 66.244  48.519 1.00 37.64  ?  103 ASP A N   1 
ATOM   776  C CA  . ASP A 1 146 ? 41.790 64.858  48.901 1.00 35.81  ?  103 ASP A CA  1 
ATOM   777  C C   . ASP A 1 146 ? 42.428 63.890  47.903 1.00 32.70  ?  103 ASP A C   1 
ATOM   778  O O   . ASP A 1 146 ? 43.158 62.966  48.291 1.00 36.03  ?  103 ASP A O   1 
ATOM   779  C CB  . ASP A 1 146 ? 40.270 64.648  49.011 1.00 34.35  ?  103 ASP A CB  1 
ATOM   780  C CG  . ASP A 1 146 ? 39.879 63.235  49.425 1.00 45.83  ?  103 ASP A CG  1 
ATOM   781  O OD1 . ASP A 1 146 ? 40.407 62.265  48.836 1.00 46.49  ?  103 ASP A OD1 1 
ATOM   782  O OD2 . ASP A 1 146 ? 39.015 63.092  50.331 1.00 35.51  ?  103 ASP A OD2 1 
ATOM   783  N N   . LEU A 1 147 ? 42.190 64.103  46.605 1.00 32.35  ?  104 LEU A N   1 
ATOM   784  C CA  . LEU A 1 147 ? 42.682 63.150  45.617 1.00 39.29  ?  104 LEU A CA  1 
ATOM   785  C C   . LEU A 1 147 ? 44.203 63.035  45.636 1.00 40.03  ?  104 LEU A C   1 
ATOM   786  O O   . LEU A 1 147 ? 44.742 61.947  45.395 1.00 32.98  ?  104 LEU A O   1 
ATOM   787  C CB  . LEU A 1 147 ? 42.202 63.538  44.211 1.00 36.69  ?  104 LEU A CB  1 
ATOM   788  C CG  . LEU A 1 147 ? 40.689 63.506  43.942 1.00 40.00  ?  104 LEU A CG  1 
ATOM   789  C CD1 . LEU A 1 147 ? 40.383 63.943  42.500 1.00 33.12  ?  104 LEU A CD1 1 
ATOM   790  C CD2 . LEU A 1 147 ? 40.117 62.122  44.213 1.00 35.76  ?  104 LEU A CD2 1 
ATOM   791  N N   . ARG A 1 148 ? 44.913 64.128  45.913 1.00 34.87  ?  105 ARG A N   1 
ATOM   792  C CA  . ARG A 1 148 ? 46.360 64.101  45.717 1.00 39.83  ?  105 ARG A CA  1 
ATOM   793  C C   . ARG A 1 148 ? 47.091 63.311  46.793 1.00 42.59  ?  105 ARG A C   1 
ATOM   794  O O   . ARG A 1 148 ? 48.305 63.095  46.671 1.00 37.67  ?  105 ARG A O   1 
ATOM   795  C CB  . ARG A 1 148 ? 46.913 65.528  45.628 1.00 44.22  ?  105 ARG A CB  1 
ATOM   796  C CG  . ARG A 1 148 ? 46.945 66.310  46.922 1.00 46.21  ?  105 ARG A CG  1 
ATOM   797  C CD  . ARG A 1 148 ? 47.369 67.743  46.626 1.00 48.09  ?  105 ARG A CD  1 
ATOM   798  N NE  . ARG A 1 148 ? 47.489 68.529  47.848 1.00 63.70  ?  105 ARG A NE  1 
ATOM   799  C CZ  . ARG A 1 148 ? 47.588 69.854  47.873 1.00 65.32  ?  105 ARG A CZ  1 
ATOM   800  N NH1 . ARG A 1 148 ? 47.580 70.545  46.737 1.00 63.96  ?  105 ARG A NH1 1 
ATOM   801  N NH2 . ARG A 1 148 ? 47.693 70.487  49.030 1.00 63.17  ?  105 ARG A NH2 1 
ATOM   802  N N   . ARG A 1 149 ? 46.387 62.834  47.816 1.00 36.20  ?  106 ARG A N   1 
ATOM   803  C CA  . ARG A 1 149 ? 46.995 61.988  48.833 1.00 40.94  ?  106 ARG A CA  1 
ATOM   804  C C   . ARG A 1 149 ? 46.459 60.557  48.822 1.00 39.17  ?  106 ARG A C   1 
ATOM   805  O O   . ARG A 1 149 ? 46.737 59.796  49.758 1.00 37.96  ?  106 ARG A O   1 
ATOM   806  C CB  . ARG A 1 149 ? 46.808 62.636  50.204 1.00 40.96  ?  106 ARG A CB  1 
ATOM   807  C CG  . ARG A 1 149 ? 47.102 64.135  50.166 1.00 48.09  ?  106 ARG A CG  1 
ATOM   808  C CD  . ARG A 1 149 ? 48.569 64.395  50.385 1.00 50.39  ?  106 ARG A CD  1 
ATOM   809  N NE  . ARG A 1 149 ? 48.889 64.079  51.771 1.00 61.28  ?  106 ARG A NE  1 
ATOM   810  C CZ  . ARG A 1 149 ? 48.885 64.964  52.763 1.00 71.94  ?  106 ARG A CZ  1 
ATOM   811  N NH1 . ARG A 1 149 ? 48.598 66.241  52.518 1.00 72.35  ?  106 ARG A NH1 1 
ATOM   812  N NH2 . ARG A 1 149 ? 49.172 64.571  53.998 1.00 59.02  ?  106 ARG A NH2 1 
ATOM   813  N N   . ARG A 1 150 ? 45.731 60.157  47.777 1.00 36.21  ?  107 ARG A N   1 
ATOM   814  C CA  . ARG A 1 150 ? 45.277 58.779  47.679 1.00 34.07  ?  107 ARG A CA  1 
ATOM   815  C C   . ARG A 1 150 ? 46.424 57.887  47.210 1.00 29.87  ?  107 ARG A C   1 
ATOM   816  O O   . ARG A 1 150 ? 47.491 58.366  46.826 1.00 36.07  ?  107 ARG A O   1 
ATOM   817  C CB  . ARG A 1 150 ? 44.054 58.685  46.753 1.00 35.53  ?  107 ARG A CB  1 
ATOM   818  C CG  . ARG A 1 150 ? 42.822 59.305  47.417 1.00 36.86  ?  107 ARG A CG  1 
ATOM   819  C CD  . ARG A 1 150 ? 41.549 59.219  46.596 1.00 44.02  ?  107 ARG A CD  1 
ATOM   820  N NE  . ARG A 1 150 ? 40.470 59.891  47.325 1.00 42.20  ?  107 ARG A NE  1 
ATOM   821  C CZ  . ARG A 1 150 ? 39.378 59.293  47.791 1.00 40.12  ?  107 ARG A CZ  1 
ATOM   822  N NH1 . ARG A 1 150 ? 39.168 57.990  47.590 1.00 36.12  ?  107 ARG A NH1 1 
ATOM   823  N NH2 . ARG A 1 150 ? 38.479 60.011  48.439 1.00 36.64  ?  107 ARG A NH2 1 
ATOM   824  N N   . ASP A 1 151 ? 46.207 56.571  47.258 1.00 28.97  ?  108 ASP A N   1 
ATOM   825  C CA  . ASP A 1 151 ? 47.330 55.656  47.094 1.00 30.39  ?  108 ASP A CA  1 
ATOM   826  C C   . ASP A 1 151 ? 47.810 55.610  45.640 1.00 32.82  ?  108 ASP A C   1 
ATOM   827  O O   . ASP A 1 151 ? 48.977 55.900  45.363 1.00 32.60  ?  108 ASP A O   1 
ATOM   828  C CB  . ASP A 1 151 ? 46.997 54.261  47.642 1.00 31.94  ?  108 ASP A CB  1 
ATOM   829  C CG  . ASP A 1 151 ? 45.693 53.662  47.111 1.00 41.53  ?  108 ASP A CG  1 
ATOM   830  O OD1 . ASP A 1 151 ? 45.047 54.195  46.167 1.00 35.09  ?  108 ASP A OD1 1 
ATOM   831  O OD2 . ASP A 1 151 ? 45.326 52.596  47.654 1.00 37.28  ?  108 ASP A OD2 1 
ATOM   832  N N   . PHE A 1 152 ? 46.925 55.301  44.697 1.00 29.02  ?  109 PHE A N   1 
ATOM   833  C CA  . PHE A 1 152 ? 47.354 55.057  43.314 1.00 28.99  ?  109 PHE A CA  1 
ATOM   834  C C   . PHE A 1 152 ? 46.492 55.834  42.327 1.00 34.72  ?  109 PHE A C   1 
ATOM   835  O O   . PHE A 1 152 ? 45.322 56.133  42.594 1.00 28.65  ?  109 PHE A O   1 
ATOM   836  C CB  . PHE A 1 152 ? 47.325 53.545  43.005 1.00 29.09  ?  109 PHE A CB  1 
ATOM   837  C CG  . PHE A 1 152 ? 48.086 52.730  44.013 1.00 32.75  ?  109 PHE A CG  1 
ATOM   838  C CD1 . PHE A 1 152 ? 49.466 52.833  44.090 1.00 31.40  ?  109 PHE A CD1 1 
ATOM   839  C CD2 . PHE A 1 152 ? 47.420 51.916  44.926 1.00 32.21  ?  109 PHE A CD2 1 
ATOM   840  C CE1 . PHE A 1 152 ? 50.190 52.126  45.065 1.00 38.44  ?  109 PHE A CE1 1 
ATOM   841  C CE2 . PHE A 1 152 ? 48.142 51.191  45.902 1.00 38.14  ?  109 PHE A CE2 1 
ATOM   842  C CZ  . PHE A 1 152 ? 49.520 51.303  45.968 1.00 33.07  ?  109 PHE A CZ  1 
ATOM   843  N N   . THR A 1 153 ? 47.085 56.150  41.159 1.00 30.07  ?  110 THR A N   1 
ATOM   844  C CA  . THR A 1 153 ? 46.412 57.040  40.224 1.00 30.41  ?  110 THR A CA  1 
ATOM   845  C C   . THR A 1 153 ? 45.050 56.486  39.803 1.00 29.92  ?  110 THR A C   1 
ATOM   846  O O   . THR A 1 153 ? 44.089 57.245  39.651 1.00 35.34  ?  110 THR A O   1 
ATOM   847  C CB  . THR A 1 153 ? 47.295 57.295  38.991 1.00 30.23  ?  110 THR A CB  1 
ATOM   848  O OG1 . THR A 1 153 ? 47.537 56.056  38.316 1.00 30.73  ?  110 THR A OG1 1 
ATOM   849  C CG2 . THR A 1 153 ? 48.619 57.933  39.408 1.00 30.24  ?  110 THR A CG2 1 
ATOM   850  N N   . ILE A 1 154 ? 44.937 55.168  39.641 1.00 30.08  ?  111 ILE A N   1 
ATOM   851  C CA  . ILE A 1 154 ? 43.669 54.604  39.190 1.00 32.46  ?  111 ILE A CA  1 
ATOM   852  C C   . ILE A 1 154 ? 42.599 54.675  40.277 1.00 33.92  ?  111 ILE A C   1 
ATOM   853  O O   . ILE A 1 154 ? 41.407 54.514  39.989 1.00 31.39  ?  111 ILE A O   1 
ATOM   854  C CB  . ILE A 1 154 ? 43.848 53.155  38.728 1.00 34.61  ?  111 ILE A CB  1 
ATOM   855  C CG1 . ILE A 1 154 ? 44.408 52.312  39.867 1.00 33.60  ?  111 ILE A CG1 1 
ATOM   856  C CG2 . ILE A 1 154 ? 44.737 53.088  37.453 1.00 33.50  ?  111 ILE A CG2 1 
ATOM   857  C CD1 . ILE A 1 154 ? 44.599 50.873  39.507 1.00 35.75  ?  111 ILE A CD1 1 
ATOM   858  N N   . ASN A 1 155 ? 42.993 54.921  41.520 1.00 31.21  ?  112 ASN A N   1 
ATOM   859  C CA  . ASN A 1 155 ? 42.060 55.092  42.625 1.00 25.90  ?  112 ASN A CA  1 
ATOM   860  C C   . ASN A 1 155 ? 41.855 56.551  42.992 1.00 31.29  ?  112 ASN A C   1 
ATOM   861  O O   . ASN A 1 155 ? 41.216 56.840  44.020 1.00 31.97  ?  112 ASN A O   1 
ATOM   862  C CB  . ASN A 1 155 ? 42.560 54.334  43.865 1.00 32.70  ?  112 ASN A CB  1 
ATOM   863  C CG  . ASN A 1 155 ? 42.673 52.845  43.637 1.00 34.69  ?  112 ASN A CG  1 
ATOM   864  O OD1 . ASN A 1 155 ? 41.965 52.277  42.814 1.00 34.96  ?  112 ASN A OD1 1 
ATOM   865  N ND2 . ASN A 1 155 ? 43.560 52.194  44.388 1.00 36.18  ?  112 ASN A ND2 1 
ATOM   866  N N   . ALA A 1 156 ? 42.419 57.472  42.215 1.00 25.88  ?  113 ALA A N   1 
ATOM   867  C CA  . ALA A 1 156 ? 42.437 58.892  42.549 1.00 30.07  ?  113 ALA A CA  1 
ATOM   868  C C   . ALA A 1 156 ? 41.649 59.713  41.529 1.00 33.00  ?  113 ALA A C   1 
ATOM   869  O O   . ALA A 1 156 ? 41.992 60.861  41.237 1.00 31.90  ?  113 ALA A O   1 
ATOM   870  C CB  . ALA A 1 156 ? 43.878 59.405  42.659 1.00 31.84  ?  113 ALA A CB  1 
ATOM   871  N N   . MET A 1 157 ? 40.603 59.124  40.972 1.00 31.17  ?  114 MET A N   1 
ATOM   872  C CA  . MET A 1 157 ? 39.723 59.805  40.039 1.00 30.51  ?  114 MET A CA  1 
ATOM   873  C C   . MET A 1 157 ? 38.363 60.048  40.679 1.00 33.67  ?  114 MET A C   1 
ATOM   874  O O   . MET A 1 157 ? 37.971 59.381  41.642 1.00 30.68  ?  114 MET A O   1 
ATOM   875  C CB  . MET A 1 157 ? 39.568 58.984  38.755 1.00 28.13  ?  114 MET A CB  1 
ATOM   876  C CG  . MET A 1 157 ? 40.903 58.705  38.087 1.00 40.65  ?  114 MET A CG  1 
ATOM   877  S SD  . MET A 1 157 ? 40.748 57.852  36.500 1.00 37.17  ?  114 MET A SD  1 
ATOM   878  C CE  . MET A 1 157 ? 40.311 56.206  36.997 1.00 31.88  ?  114 MET A CE  1 
ATOM   879  N N   . ALA A 1 158 ? 37.651 61.039  40.147 1.00 32.34  ?  115 ALA A N   1 
ATOM   880  C CA  . ALA A 1 158 ? 36.294 61.336  40.575 1.00 29.55  ?  115 ALA A CA  1 
ATOM   881  C C   . ALA A 1 158 ? 35.395 61.386  39.349 1.00 35.84  ?  115 ALA A C   1 
ATOM   882  O O   . ALA A 1 158 ? 35.856 61.604  38.230 1.00 34.80  ?  115 ALA A O   1 
ATOM   883  C CB  . ALA A 1 158 ? 36.204 62.663  41.329 1.00 29.67  ?  115 ALA A CB  1 
ATOM   884  N N   . MET A 1 159 ? 34.102 61.176  39.565 1.00 32.09  ?  116 MET A N   1 
ATOM   885  C CA  . MET A 1 159 ? 33.132 61.283  38.482 1.00 34.11  ?  116 MET A CA  1 
ATOM   886  C C   . MET A 1 159 ? 31.966 62.135  38.942 1.00 34.35  ?  116 MET A C   1 
ATOM   887  O O   . MET A 1 159 ? 31.431 61.935  40.039 1.00 31.68  ?  116 MET A O   1 
ATOM   888  C CB  . MET A 1 159 ? 32.614 59.925  38.016 1.00 34.17  ?  116 MET A CB  1 
ATOM   889  C CG  . MET A 1 159 ? 31.725 60.074  36.772 1.00 35.79  ?  116 MET A CG  1 
ATOM   890  S SD  . MET A 1 159 ? 31.230 58.492  36.086 1.00 42.90  ?  116 MET A SD  1 
ATOM   891  C CE  . MET A 1 159 ? 30.096 57.922  37.322 1.00 38.07  ?  116 MET A CE  1 
ATOM   892  N N   . THR A 1 160 ? 31.586 63.088  38.106 1.00 31.61  ?  117 THR A N   1 
ATOM   893  C CA  . THR A 1 160 ? 30.475 63.960  38.422 1.00 34.74  ?  117 THR A CA  1 
ATOM   894  C C   . THR A 1 160 ? 29.153 63.269  38.106 1.00 37.34  ?  117 THR A C   1 
ATOM   895  O O   . THR A 1 160 ? 29.095 62.242  37.420 1.00 36.11  ?  117 THR A O   1 
ATOM   896  C CB  . THR A 1 160 ? 30.563 65.264  37.631 1.00 39.90  ?  117 THR A CB  1 
ATOM   897  O OG1 . THR A 1 160 ? 30.341 64.976  36.251 1.00 40.40  ?  117 THR A OG1 1 
ATOM   898  C CG2 . THR A 1 160 ? 31.927 65.901  37.776 1.00 39.21  ?  117 THR A CG2 1 
ATOM   899  N N   . GLU A 1 161 ? 28.076 63.877  38.606 1.00 36.73  ?  118 GLU A N   1 
ATOM   900  C CA  . GLU A 1 161 ? 26.724 63.429  38.294 1.00 36.25  ?  118 GLU A CA  1 
ATOM   901  C C   . GLU A 1 161 ? 26.507 63.290  36.793 1.00 40.19  ?  118 GLU A C   1 
ATOM   902  O O   . GLU A 1 161 ? 25.757 62.413  36.350 1.00 43.33  ?  118 GLU A O   1 
ATOM   903  C CB  . GLU A 1 161 ? 25.726 64.423  38.895 1.00 41.76  ?  118 GLU A CB  1 
ATOM   904  C CG  . GLU A 1 161 ? 24.346 63.857  39.157 1.00 52.52  ?  118 GLU A CG  1 
ATOM   905  C CD  . GLU A 1 161 ? 23.368 64.903  39.689 1.00 54.62  ?  118 GLU A CD  1 
ATOM   906  O OE1 . GLU A 1 161 ? 23.808 66.026  40.027 1.00 50.48  ?  118 GLU A OE1 1 
ATOM   907  O OE2 . GLU A 1 161 ? 22.156 64.595  39.757 1.00 52.84  ?  118 GLU A OE2 1 
ATOM   908  N N   . ASP A 1 162 ? 27.164 64.126  35.991 1.00 37.70  ?  119 ASP A N   1 
ATOM   909  C CA  . ASP A 1 162 ? 26.999 64.099  34.542 1.00 43.26  ?  119 ASP A CA  1 
ATOM   910  C C   . ASP A 1 162 ? 28.050 63.254  33.837 1.00 42.97  ?  119 ASP A C   1 
ATOM   911  O O   . ASP A 1 162 ? 28.259 63.443  32.636 1.00 43.60  ?  119 ASP A O   1 
ATOM   912  C CB  . ASP A 1 162 ? 27.047 65.513  33.972 1.00 41.77  ?  119 ASP A CB  1 
ATOM   913  C CG  . ASP A 1 162 ? 25.965 66.390  34.514 1.00 57.44  ?  119 ASP A CG  1 
ATOM   914  O OD1 . ASP A 1 162 ? 24.809 65.918  34.582 1.00 63.92  ?  119 ASP A OD1 1 
ATOM   915  O OD2 . ASP A 1 162 ? 26.274 67.548  34.880 1.00 62.81  ?  119 ASP A OD2 1 
ATOM   916  N N   . LEU A 1 163 ? 28.737 62.365  34.560 1.00 40.44  ?  120 LEU A N   1 
ATOM   917  C CA  . LEU A 1 163 ? 29.697 61.401  34.022 1.00 38.74  ?  120 LEU A CA  1 
ATOM   918  C C   . LEU A 1 163 ? 31.032 62.013  33.609 1.00 42.64  ?  120 LEU A C   1 
ATOM   919  O O   . LEU A 1 163 ? 31.828 61.341  32.941 1.00 45.06  ?  120 LEU A O   1 
ATOM   920  C CB  . LEU A 1 163 ? 29.126 60.637  32.815 1.00 41.39  ?  120 LEU A CB  1 
ATOM   921  C CG  . LEU A 1 163 ? 27.754 59.976  32.971 1.00 50.99  ?  120 LEU A CG  1 
ATOM   922  C CD1 . LEU A 1 163 ? 27.386 59.198  31.714 1.00 53.01  ?  120 LEU A CD1 1 
ATOM   923  C CD2 . LEU A 1 163 ? 27.712 59.084  34.174 1.00 43.53  ?  120 LEU A CD2 1 
ATOM   924  N N   . LYS A 1 164 ? 31.307 63.262  33.956 1.00 39.55  ?  121 LYS A N   1 
ATOM   925  C CA  . LYS A 1 164 ? 32.618 63.815  33.658 1.00 40.74  ?  121 LYS A CA  1 
ATOM   926  C C   . LYS A 1 164 ? 33.644 63.221  34.618 1.00 41.35  ?  121 LYS A C   1 
ATOM   927  O O   . LYS A 1 164 ? 33.407 63.163  35.828 1.00 35.74  ?  121 LYS A O   1 
ATOM   928  C CB  . LYS A 1 164 ? 32.597 65.334  33.776 1.00 39.62  ?  121 LYS A CB  1 
ATOM   929  C CG  . LYS A 1 164 ? 31.738 66.022  32.722 1.00 58.83  ?  121 LYS A CG  1 
ATOM   930  C CD  . LYS A 1 164 ? 30.982 67.202  33.333 1.00 75.72  ?  121 LYS A CD  1 
ATOM   931  C CE  . LYS A 1 164 ? 29.867 66.716  34.266 1.00 58.37  ?  121 LYS A CE  1 
ATOM   932  N NZ  . LYS A 1 164 ? 29.552 67.677  35.340 1.00 51.92  ?  121 LYS A NZ  1 
ATOM   933  N N   . ILE A 1 165 ? 34.776 62.775  34.078 1.00 39.08  ?  122 ILE A N   1 
ATOM   934  C CA  . ILE A 1 165 ? 35.859 62.235  34.894 1.00 40.78  ?  122 ILE A CA  1 
ATOM   935  C C   . ILE A 1 165 ? 36.810 63.362  35.264 1.00 41.71  ?  122 ILE A C   1 
ATOM   936  O O   . ILE A 1 165 ? 37.315 64.081  34.397 1.00 38.72  ?  122 ILE A O   1 
ATOM   937  C CB  . ILE A 1 165 ? 36.606 61.105  34.167 1.00 41.85  ?  122 ILE A CB  1 
ATOM   938  C CG1 . ILE A 1 165 ? 35.636 60.009  33.710 1.00 44.78  ?  122 ILE A CG1 1 
ATOM   939  C CG2 . ILE A 1 165 ? 37.683 60.502  35.084 1.00 38.64  ?  122 ILE A CG2 1 
ATOM   940  C CD1 . ILE A 1 165 ? 35.085 59.190  34.829 1.00 41.78  ?  122 ILE A CD1 1 
ATOM   941  N N   . ILE A 1 166 ? 37.050 63.517  36.557 1.00 29.95  ?  123 ILE A N   1 
ATOM   942  C CA  . ILE A 1 166 ? 38.075 64.408  37.078 1.00 34.63  ?  123 ILE A CA  1 
ATOM   943  C C   . ILE A 1 166 ? 39.292 63.541  37.370 1.00 39.08  ?  123 ILE A C   1 
ATOM   944  O O   . ILE A 1 166 ? 39.216 62.620  38.194 1.00 33.09  ?  123 ILE A O   1 
ATOM   945  C CB  . ILE A 1 166 ? 37.584 65.144  38.338 1.00 37.37  ?  123 ILE A CB  1 
ATOM   946  C CG1 . ILE A 1 166 ? 36.347 65.994  38.000 1.00 39.89  ?  123 ILE A CG1 1 
ATOM   947  C CG2 . ILE A 1 166 ? 38.720 65.989  38.954 1.00 32.38  ?  123 ILE A CG2 1 
ATOM   948  C CD1 . ILE A 1 166 ? 35.508 66.441  39.200 1.00 39.36  ?  123 ILE A CD1 1 
ATOM   949  N N   . ASP A 1 167 ? 40.406 63.803  36.683 1.00 35.66  ?  124 ASP A N   1 
ATOM   950  C CA  . ASP A 1 167 ? 41.563 62.903  36.697 1.00 37.68  ?  124 ASP A CA  1 
ATOM   951  C C   . ASP A 1 167 ? 42.855 63.706  36.691 1.00 39.89  ?  124 ASP A C   1 
ATOM   952  O O   . ASP A 1 167 ? 43.611 63.695  35.709 1.00 40.84  ?  124 ASP A O   1 
ATOM   953  C CB  . ASP A 1 167 ? 41.503 61.949  35.504 1.00 37.82  ?  124 ASP A CB  1 
ATOM   954  C CG  . ASP A 1 167 ? 42.670 60.978  35.465 1.00 39.77  ?  124 ASP A CG  1 
ATOM   955  O OD1 . ASP A 1 167 ? 43.217 60.653  36.546 1.00 38.59  ?  124 ASP A OD1 1 
ATOM   956  O OD2 . ASP A 1 167 ? 43.032 60.531  34.352 1.00 37.02  ?  124 ASP A OD2 1 
ATOM   957  N N   . PRO A 1 168 ? 43.169 64.401  37.788 1.00 37.48  ?  125 PRO A N   1 
ATOM   958  C CA  . PRO A 1 168 ? 44.372 65.247  37.798 1.00 38.67  ?  125 PRO A CA  1 
ATOM   959  C C   . PRO A 1 168 ? 45.685 64.474  37.684 1.00 48.04  ?  125 PRO A C   1 
ATOM   960  O O   . PRO A 1 168 ? 46.690 65.071  37.278 1.00 43.53  ?  125 PRO A O   1 
ATOM   961  C CB  . PRO A 1 168 ? 44.276 65.992  39.135 1.00 45.57  ?  125 PRO A CB  1 
ATOM   962  C CG  . PRO A 1 168 ? 43.424 65.112  39.998 1.00 45.05  ?  125 PRO A CG  1 
ATOM   963  C CD  . PRO A 1 168 ? 42.429 64.474  39.064 1.00 40.73  ?  125 PRO A CD  1 
ATOM   964  N N   . PHE A 1 169 ? 45.719 63.176  37.994 1.00 38.20  ?  126 PHE A N   1 
ATOM   965  C CA  . PHE A 1 169 ? 46.987 62.456  38.087 1.00 37.03  ?  126 PHE A CA  1 
ATOM   966  C C   . PHE A 1 169 ? 47.135 61.362  37.036 1.00 44.25  ?  126 PHE A C   1 
ATOM   967  O O   . PHE A 1 169 ? 48.010 60.496  37.159 1.00 45.67  ?  126 PHE A O   1 
ATOM   968  C CB  . PHE A 1 169 ? 47.150 61.917  39.504 1.00 39.99  ?  126 PHE A CB  1 
ATOM   969  C CG  . PHE A 1 169 ? 46.947 62.976  40.530 1.00 42.79  ?  126 PHE A CG  1 
ATOM   970  C CD1 . PHE A 1 169 ? 47.864 64.009  40.653 1.00 52.76  ?  126 PHE A CD1 1 
ATOM   971  C CD2 . PHE A 1 169 ? 45.811 62.995  41.315 1.00 46.27  ?  126 PHE A CD2 1 
ATOM   972  C CE1 . PHE A 1 169 ? 47.674 65.017  41.571 1.00 50.90  ?  126 PHE A CE1 1 
ATOM   973  C CE2 . PHE A 1 169 ? 45.611 64.007  42.237 1.00 44.71  ?  126 PHE A CE2 1 
ATOM   974  C CZ  . PHE A 1 169 ? 46.547 65.020  42.360 1.00 51.56  ?  126 PHE A CZ  1 
ATOM   975  N N   . GLY A 1 170 ? 46.337 61.414  35.972 1.00 42.79  ?  127 GLY A N   1 
ATOM   976  C CA  . GLY A 1 170 ? 46.521 60.502  34.863 1.00 35.79  ?  127 GLY A CA  1 
ATOM   977  C C   . GLY A 1 170 ? 46.104 59.087  35.154 1.00 41.03  ?  127 GLY A C   1 
ATOM   978  O O   . GLY A 1 170 ? 46.650 58.151  34.555 1.00 39.71  ?  127 GLY A O   1 
ATOM   979  N N   . GLY A 1 171 ? 45.147 58.898  36.071 1.00 35.24  ?  128 GLY A N   1 
ATOM   980  C CA  . GLY A 1 171 ? 44.608 57.570  36.293 1.00 33.86  ?  128 GLY A CA  1 
ATOM   981  C C   . GLY A 1 171 ? 44.029 56.944  35.036 1.00 33.77  ?  128 GLY A C   1 
ATOM   982  O O   . GLY A 1 171 ? 44.106 55.725  34.856 1.00 32.61  ?  128 GLY A O   1 
ATOM   983  N N   . LYS A 1 172 ? 43.431 57.757  34.157 1.00 35.41  ?  129 LYS A N   1 
ATOM   984  C CA  . LYS A 1 172 ? 42.853 57.208  32.932 1.00 41.38  ?  129 LYS A CA  1 
ATOM   985  C C   . LYS A 1 172 ? 43.916 56.496  32.102 1.00 38.80  ?  129 LYS A C   1 
ATOM   986  O O   . LYS A 1 172 ? 43.705 55.379  31.613 1.00 36.46  ?  129 LYS A O   1 
ATOM   987  C CB  . LYS A 1 172 ? 42.185 58.320  32.109 1.00 42.86  ?  129 LYS A CB  1 
ATOM   988  C CG  . LYS A 1 172 ? 40.777 58.706  32.571 1.00 48.79  ?  129 LYS A CG  1 
ATOM   989  C CD  . LYS A 1 172 ? 40.132 59.759  31.644 1.00 48.24  ?  129 LYS A CD  1 
ATOM   990  C CE  . LYS A 1 172 ? 38.780 59.262  31.138 1.00 61.15  ?  129 LYS A CE  1 
ATOM   991  N NZ  . LYS A 1 172 ? 37.989 60.296  30.376 1.00 61.95  ?  129 LYS A NZ  1 
ATOM   992  N N   . GLU A 1 173 ? 45.068 57.139  31.927 1.00 34.87  ?  130 GLU A N   1 
ATOM   993  C CA  . GLU A 1 173 ? 46.115 56.537  31.108 1.00 40.04  ?  130 GLU A CA  1 
ATOM   994  C C   . GLU A 1 173 ? 46.746 55.347  31.813 1.00 34.93  ?  130 GLU A C   1 
ATOM   995  O O   . GLU A 1 173 ? 47.041 54.331  31.174 1.00 34.62  ?  130 GLU A O   1 
ATOM   996  C CB  . GLU A 1 173 ? 47.174 57.580  30.745 1.00 41.92  ?  130 GLU A CB  1 
ATOM   997  C CG  . GLU A 1 173 ? 46.593 58.801  30.055 1.00 57.53  ?  130 GLU A CG  1 
ATOM   998  C CD  . GLU A 1 173 ? 45.555 58.437  28.999 1.00 79.22  ?  130 GLU A CD  1 
ATOM   999  O OE1 . GLU A 1 173 ? 45.920 57.764  28.004 1.00 79.10  ?  130 GLU A OE1 1 
ATOM   1000 O OE2 . GLU A 1 173 ? 44.366 58.816  29.169 1.00 71.96  ?  130 GLU A OE2 1 
ATOM   1001 N N   . ASP A 1 174 ? 46.942 55.428  33.141 1.00 34.28  ?  131 ASP A N   1 
ATOM   1002 C CA  . ASP A 1 174 ? 47.462 54.251  33.829 1.00 31.79  ?  131 ASP A CA  1 
ATOM   1003 C C   . ASP A 1 174 ? 46.468 53.098  33.786 1.00 29.78  ?  131 ASP A C   1 
ATOM   1004 O O   . ASP A 1 174 ? 46.873 51.934  33.710 1.00 33.38  ?  131 ASP A O   1 
ATOM   1005 C CB  . ASP A 1 174 ? 47.839 54.599  35.280 1.00 28.40  ?  131 ASP A CB  1 
ATOM   1006 C CG  . ASP A 1 174 ? 49.093 55.435  35.355 1.00 40.05  ?  131 ASP A CG  1 
ATOM   1007 O OD1 . ASP A 1 174 ? 49.930 55.327  34.417 1.00 41.60  ?  131 ASP A OD1 1 
ATOM   1008 O OD2 . ASP A 1 174 ? 49.249 56.208  36.324 1.00 38.47  ?  131 ASP A OD2 1 
ATOM   1009 N N   . LEU A 1 175 ? 45.170 53.389  33.834 1.00 30.66  ?  132 LEU A N   1 
ATOM   1010 C CA  . LEU A 1 175 ? 44.193 52.312  33.718 1.00 31.36  ?  132 LEU A CA  1 
ATOM   1011 C C   . LEU A 1 175 ? 44.281 51.656  32.343 1.00 37.98  ?  132 LEU A C   1 
ATOM   1012 O O   . LEU A 1 175 ? 44.276 50.426  32.223 1.00 39.94  ?  132 LEU A O   1 
ATOM   1013 C CB  . LEU A 1 175 ? 42.787 52.863  33.961 1.00 36.65  ?  132 LEU A CB  1 
ATOM   1014 C CG  . LEU A 1 175 ? 41.662 51.904  34.370 1.00 51.79  ?  132 LEU A CG  1 
ATOM   1015 C CD1 . LEU A 1 175 ? 41.959 51.218  35.705 1.00 44.69  ?  132 LEU A CD1 1 
ATOM   1016 C CD2 . LEU A 1 175 ? 40.338 52.643  34.471 1.00 53.01  ?  132 LEU A CD2 1 
ATOM   1017 N N   . LYS A 1 176 ? 44.387 52.473  31.302 1.00 36.25  ?  133 LYS A N   1 
ATOM   1018 C CA  . LYS A 1 176 ? 44.497 51.954  29.937 1.00 38.05  ?  133 LYS A CA  1 
ATOM   1019 C C   . LYS A 1 176 ? 45.756 51.113  29.773 1.00 36.95  ?  133 LYS A C   1 
ATOM   1020 O O   . LYS A 1 176 ? 45.713 50.021  29.196 1.00 39.86  ?  133 LYS A O   1 
ATOM   1021 C CB  . LYS A 1 176 ? 44.487 53.122  28.955 1.00 33.87  ?  133 LYS A CB  1 
ATOM   1022 C CG  . LYS A 1 176 ? 44.574 52.721  27.473 1.00 44.59  ?  133 LYS A CG  1 
ATOM   1023 C CD  . LYS A 1 176 ? 44.772 53.955  26.584 1.00 55.53  ?  133 LYS A CD  1 
ATOM   1024 C CE  . LYS A 1 176 ? 44.881 53.575  25.101 1.00 69.02  ?  133 LYS A CE  1 
ATOM   1025 N NZ  . LYS A 1 176 ? 45.994 52.609  24.834 1.00 68.09  ?  133 LYS A NZ  1 
ATOM   1026 N N   . ASN A 1 177 ? 46.879 51.584  30.316 1.00 37.87  ?  134 ASN A N   1 
ATOM   1027 C CA  . ASN A 1 177 ? 48.144 50.867  30.226 1.00 37.14  ?  134 ASN A CA  1 
ATOM   1028 C C   . ASN A 1 177 ? 48.291 49.761  31.268 1.00 41.87  ?  134 ASN A C   1 
ATOM   1029 O O   . ASN A 1 177 ? 49.287 49.032  31.228 1.00 37.78  ?  134 ASN A O   1 
ATOM   1030 C CB  . ASN A 1 177 ? 49.301 51.859  30.343 1.00 35.71  ?  134 ASN A CB  1 
ATOM   1031 C CG  . ASN A 1 177 ? 49.336 52.845  29.183 1.00 44.03  ?  134 ASN A CG  1 
ATOM   1032 O OD1 . ASN A 1 177 ? 48.789 52.570  28.119 1.00 41.84  ?  134 ASN A OD1 1 
ATOM   1033 N ND2 . ASN A 1 177 ? 49.961 53.999  29.392 1.00 40.55  ?  134 ASN A ND2 1 
ATOM   1034 N N   . LYS A 1 178 ? 47.331 49.618  32.192 1.00 34.32  ?  135 LYS A N   1 
ATOM   1035 C CA  . LYS A 1 178 ? 47.341 48.542  33.188 1.00 36.29  ?  135 LYS A CA  1 
ATOM   1036 C C   . LYS A 1 178 ? 48.511 48.714  34.164 1.00 31.44  ?  135 LYS A C   1 
ATOM   1037 O O   . LYS A 1 178 ? 49.279 47.784  34.402 1.00 35.04  ?  135 LYS A O   1 
ATOM   1038 C CB  . LYS A 1 178 ? 47.386 47.167  32.519 1.00 36.85  ?  135 LYS A CB  1 
ATOM   1039 C CG  . LYS A 1 178 ? 46.192 46.859  31.598 1.00 43.98  ?  135 LYS A CG  1 
ATOM   1040 C CD  . LYS A 1 178 ? 46.484 45.601  30.767 1.00 47.79  ?  135 LYS A CD  1 
ATOM   1041 C CE  . LYS A 1 178 ? 45.302 44.642  30.733 1.00 65.77  ?  135 LYS A CE  1 
ATOM   1042 N NZ  . LYS A 1 178 ? 45.656 43.302  31.324 1.00 67.19  ?  135 LYS A NZ  1 
ATOM   1043 N N   . VAL A 1 179 ? 48.646 49.923  34.717 1.00 32.82  ?  136 VAL A N   1 
ATOM   1044 C CA  . VAL A 1 179 ? 49.767 50.283  35.584 1.00 29.80  ?  136 VAL A CA  1 
ATOM   1045 C C   . VAL A 1 179 ? 49.238 50.730  36.949 1.00 29.98  ?  136 VAL A C   1 
ATOM   1046 O O   . VAL A 1 179 ? 48.380 51.615  37.027 1.00 33.25  ?  136 VAL A O   1 
ATOM   1047 C CB  . VAL A 1 179 ? 50.637 51.387  34.954 1.00 36.68  ?  136 VAL A CB  1 
ATOM   1048 C CG1 . VAL A 1 179 ? 51.710 51.849  35.925 1.00 34.16  ?  136 VAL A CG1 1 
ATOM   1049 C CG2 . VAL A 1 179 ? 51.306 50.878  33.657 1.00 30.53  ?  136 VAL A CG2 1 
ATOM   1050 N N   . ILE A 1 180 ? 49.786 50.144  38.009 1.00 29.62  ?  137 ILE A N   1 
ATOM   1051 C CA  . ILE A 1 180 ? 49.581 50.605  39.390 1.00 30.44  ?  137 ILE A CA  1 
ATOM   1052 C C   . ILE A 1 180 ? 50.714 51.565  39.726 1.00 28.98  ?  137 ILE A C   1 
ATOM   1053 O O   . ILE A 1 180 ? 51.867 51.150  39.865 1.00 33.50  ?  137 ILE A O   1 
ATOM   1054 C CB  . ILE A 1 180 ? 49.546 49.427  40.366 1.00 27.13  ?  137 ILE A CB  1 
ATOM   1055 C CG1 . ILE A 1 180 ? 48.339 48.546  40.070 1.00 30.93  ?  137 ILE A CG1 1 
ATOM   1056 C CG2 . ILE A 1 180 ? 49.471 49.923  41.841 1.00 24.54  ?  137 ILE A CG2 1 
ATOM   1057 C CD1 . ILE A 1 180 ? 48.552 47.121  40.432 1.00 32.83  ?  137 ILE A CD1 1 
ATOM   1058 N N   . ARG A 1 181 ? 50.393 52.850  39.822 1.00 28.61  ?  138 ARG A N   1 
ATOM   1059 C CA  . ARG A 1 181 ? 51.370 53.915  40.024 1.00 34.06  ?  138 ARG A CA  1 
ATOM   1060 C C   . ARG A 1 181 ? 50.938 54.756  41.214 1.00 34.07  ?  138 ARG A C   1 
ATOM   1061 O O   . ARG A 1 181 ? 49.786 55.207  41.272 1.00 28.98  ?  138 ARG A O   1 
ATOM   1062 C CB  . ARG A 1 181 ? 51.484 54.814  38.778 1.00 32.42  ?  138 ARG A CB  1 
ATOM   1063 C CG  . ARG A 1 181 ? 52.511 55.945  38.919 1.00 35.71  ?  138 ARG A CG  1 
ATOM   1064 C CD  . ARG A 1 181 ? 52.343 57.043  37.847 1.00 41.09  ?  138 ARG A CD  1 
ATOM   1065 N NE  . ARG A 1 181 ? 52.137 56.500  36.503 1.00 39.80  ?  138 ARG A NE  1 
ATOM   1066 C CZ  . ARG A 1 181 ? 53.099 56.345  35.592 1.00 49.55  ?  138 ARG A CZ  1 
ATOM   1067 N NH1 . ARG A 1 181 ? 54.356 56.689  35.868 1.00 39.97  ?  138 ARG A NH1 1 
ATOM   1068 N NH2 . ARG A 1 181 ? 52.804 55.842  34.397 1.00 42.21  ?  138 ARG A NH2 1 
ATOM   1069 N N   . ALA A 1 182 ? 51.852 54.975  42.159 1.00 34.41  ?  139 ALA A N   1 
ATOM   1070 C CA  . ALA A 1 182 ? 51.526 55.842  43.282 1.00 34.72  ?  139 ALA A CA  1 
ATOM   1071 C C   . ALA A 1 182 ? 51.160 57.235  42.779 1.00 40.63  ?  139 ALA A C   1 
ATOM   1072 O O   . ALA A 1 182 ? 51.704 57.717  41.782 1.00 38.04  ?  139 ALA A O   1 
ATOM   1073 C CB  . ALA A 1 182 ? 52.709 55.922  44.257 1.00 35.52  ?  139 ALA A CB  1 
ATOM   1074 N N   . VAL A 1 183 ? 50.218 57.882  43.472 1.00 33.79  ?  140 VAL A N   1 
ATOM   1075 C CA  . VAL A 1 183 ? 49.890 59.274  43.184 1.00 33.32  ?  140 VAL A CA  1 
ATOM   1076 C C   . VAL A 1 183 ? 51.045 60.164  43.621 1.00 39.49  ?  140 VAL A C   1 
ATOM   1077 O O   . VAL A 1 183 ? 51.477 60.120  44.782 1.00 36.60  ?  140 VAL A O   1 
ATOM   1078 C CB  . VAL A 1 183 ? 48.595 59.696  43.900 1.00 36.80  ?  140 VAL A CB  1 
ATOM   1079 C CG1 . VAL A 1 183 ? 48.354 61.208  43.739 1.00 33.61  ?  140 VAL A CG1 1 
ATOM   1080 C CG2 . VAL A 1 183 ? 47.386 58.880  43.409 1.00 31.46  ?  140 VAL A CG2 1 
ATOM   1081 N N   . GLY A 1 184 ? 51.544 60.980  42.700 1.00 39.10  ?  141 GLY A N   1 
ATOM   1082 C CA  . GLY A 1 184 ? 52.576 61.941  43.061 1.00 38.61  ?  141 GLY A CA  1 
ATOM   1083 C C   . GLY A 1 184 ? 53.872 61.241  43.425 1.00 37.86  ?  141 GLY A C   1 
ATOM   1084 O O   . GLY A 1 184 ? 54.309 60.300  42.756 1.00 41.42  ?  141 GLY A O   1 
ATOM   1085 N N   . ASP A 1 185 ? 54.484 61.680  44.514 1.00 42.05  ?  142 ASP A N   1 
ATOM   1086 C CA  . ASP A 1 185 ? 55.745 61.108  44.967 1.00 42.52  ?  142 ASP A CA  1 
ATOM   1087 C C   . ASP A 1 185 ? 55.493 59.795  45.703 1.00 38.83  ?  142 ASP A C   1 
ATOM   1088 O O   . ASP A 1 185 ? 54.931 59.805  46.803 1.00 38.16  ?  142 ASP A O   1 
ATOM   1089 C CB  . ASP A 1 185 ? 56.473 62.109  45.870 1.00 41.99  ?  142 ASP A CB  1 
ATOM   1090 C CG  . ASP A 1 185 ? 57.821 61.596  46.353 1.00 43.39  ?  142 ASP A CG  1 
ATOM   1091 O OD1 . ASP A 1 185 ? 58.163 60.421  46.095 1.00 45.54  ?  142 ASP A OD1 1 
ATOM   1092 O OD2 . ASP A 1 185 ? 58.547 62.383  46.984 1.00 53.50  ?  142 ASP A OD2 1 
ATOM   1093 N N   . PRO A 1 186 ? 55.882 58.648  45.136 1.00 33.56  ?  143 PRO A N   1 
ATOM   1094 C CA  . PRO A 1 186 ? 55.614 57.375  45.824 1.00 34.46  ?  143 PRO A CA  1 
ATOM   1095 C C   . PRO A 1 186 ? 56.200 57.320  47.222 1.00 42.37  ?  143 PRO A C   1 
ATOM   1096 O O   . PRO A 1 186 ? 55.613 56.677  48.111 1.00 35.97  ?  143 PRO A O   1 
ATOM   1097 C CB  . PRO A 1 186 ? 56.259 56.328  44.907 1.00 37.59  ?  143 PRO A CB  1 
ATOM   1098 C CG  . PRO A 1 186 ? 57.174 57.112  43.999 1.00 43.10  ?  143 PRO A CG  1 
ATOM   1099 C CD  . PRO A 1 186 ? 56.572 58.461  43.850 1.00 38.63  ?  143 PRO A CD  1 
ATOM   1100 N N   . ASP A 1 187 ? 57.351 57.965  47.442 1.00 39.81  ?  144 ASP A N   1 
ATOM   1101 C CA  . ASP A 1 187 ? 57.935 57.976  48.781 1.00 40.13  ?  144 ASP A CA  1 
ATOM   1102 C C   . ASP A 1 187 ? 56.972 58.580  49.797 1.00 42.89  ?  144 ASP A C   1 
ATOM   1103 O O   . ASP A 1 187 ? 56.837 58.062  50.909 1.00 38.79  ?  144 ASP A O   1 
ATOM   1104 C CB  . ASP A 1 187 ? 59.259 58.743  48.788 1.00 41.27  ?  144 ASP A CB  1 
ATOM   1105 C CG  . ASP A 1 187 ? 60.280 58.174  47.816 1.00 45.93  ?  144 ASP A CG  1 
ATOM   1106 O OD1 . ASP A 1 187 ? 60.205 56.972  47.454 1.00 45.64  ?  144 ASP A OD1 1 
ATOM   1107 O OD2 . ASP A 1 187 ? 61.168 58.946  47.411 1.00 53.46  ?  144 ASP A OD2 1 
ATOM   1108 N N   . GLU A 1 188 ? 56.290 59.672  49.433 1.00 39.42  ?  145 GLU A N   1 
ATOM   1109 C CA  . GLU A 1 188 ? 55.337 60.285  50.353 1.00 40.19  ?  145 GLU A CA  1 
ATOM   1110 C C   . GLU A 1 188 ? 54.138 59.374  50.599 1.00 42.25  ?  145 GLU A C   1 
ATOM   1111 O O   . GLU A 1 188 ? 53.694 59.210  51.740 1.00 38.44  ?  145 GLU A O   1 
ATOM   1112 C CB  . GLU A 1 188 ? 54.875 61.644  49.819 1.00 42.71  ?  145 GLU A CB  1 
ATOM   1113 C CG  . GLU A 1 188 ? 55.961 62.722  49.830 1.00 53.02  ?  145 GLU A CG  1 
ATOM   1114 C CD  . GLU A 1 188 ? 55.571 63.985  49.056 1.00 60.84  ?  145 GLU A CD  1 
ATOM   1115 O OE1 . GLU A 1 188 ? 54.356 64.264  48.898 1.00 64.65  ?  145 GLU A OE1 1 
ATOM   1116 O OE2 . GLU A 1 188 ? 56.490 64.695  48.593 1.00 67.75  ?  145 GLU A OE2 1 
ATOM   1117 N N   . ARG A 1 189 ? 53.582 58.786  49.538 1.00 38.59  ?  146 ARG A N   1 
ATOM   1118 C CA  . ARG A 1 189 ? 52.412 57.931  49.719 1.00 36.35  ?  146 ARG A CA  1 
ATOM   1119 C C   . ARG A 1 189 ? 52.725 56.763  50.646 1.00 36.92  ?  146 ARG A C   1 
ATOM   1120 O O   . ARG A 1 189 ? 51.889 56.375  51.466 1.00 40.79  ?  146 ARG A O   1 
ATOM   1121 C CB  . ARG A 1 189 ? 51.908 57.412  48.371 1.00 35.80  ?  146 ARG A CB  1 
ATOM   1122 C CG  . ARG A 1 189 ? 51.512 58.498  47.375 1.00 33.27  ?  146 ARG A CG  1 
ATOM   1123 C CD  . ARG A 1 189 ? 50.314 59.333  47.843 1.00 34.16  ?  146 ARG A CD  1 
ATOM   1124 N NE  . ARG A 1 189 ? 50.684 60.423  48.755 1.00 39.74  ?  146 ARG A NE  1 
ATOM   1125 C CZ  . ARG A 1 189 ? 51.296 61.542  48.379 1.00 39.32  ?  146 ARG A CZ  1 
ATOM   1126 N NH1 . ARG A 1 189 ? 51.634 61.723  47.099 1.00 39.55  ?  146 ARG A NH1 1 
ATOM   1127 N NH2 . ARG A 1 189 ? 51.585 62.471  49.279 1.00 39.38  ?  146 ARG A NH2 1 
ATOM   1128 N N   . PHE A 1 190 ? 53.920 56.190  50.535 1.00 35.31  ?  147 PHE A N   1 
ATOM   1129 C CA  . PHE A 1 190 ? 54.237 55.015  51.340 1.00 33.49  ?  147 PHE A CA  1 
ATOM   1130 C C   . PHE A 1 190 ? 54.599 55.387  52.770 1.00 40.47  ?  147 PHE A C   1 
ATOM   1131 O O   . PHE A 1 190 ? 54.343 54.601  53.696 1.00 38.88  ?  147 PHE A O   1 
ATOM   1132 C CB  . PHE A 1 190 ? 55.354 54.224  50.663 1.00 36.46  ?  147 PHE A CB  1 
ATOM   1133 C CG  . PHE A 1 190 ? 54.915 53.593  49.362 1.00 37.36  ?  147 PHE A CG  1 
ATOM   1134 C CD1 . PHE A 1 190 ? 53.646 53.031  49.261 1.00 31.72  ?  147 PHE A CD1 1 
ATOM   1135 C CD2 . PHE A 1 190 ? 55.739 53.595  48.244 1.00 36.55  ?  147 PHE A CD2 1 
ATOM   1136 C CE1 . PHE A 1 190 ? 53.214 52.455  48.075 1.00 36.38  ?  147 PHE A CE1 1 
ATOM   1137 C CE2 . PHE A 1 190 ? 55.313 53.024  47.049 1.00 33.59  ?  147 PHE A CE2 1 
ATOM   1138 C CZ  . PHE A 1 190 ? 54.059 52.454  46.955 1.00 37.03  ?  147 PHE A CZ  1 
ATOM   1139 N N   . GLU A 1 191 ? 55.163 56.578  52.970 1.00 37.41  ?  148 GLU A N   1 
ATOM   1140 C CA  . GLU A 1 191 ? 55.393 57.071  54.324 1.00 37.88  ?  148 GLU A CA  1 
ATOM   1141 C C   . GLU A 1 191 ? 54.085 57.455  55.002 1.00 44.46  ?  148 GLU A C   1 
ATOM   1142 O O   . GLU A 1 191 ? 53.972 57.350  56.227 1.00 37.85  ?  148 GLU A O   1 
ATOM   1143 C CB  . GLU A 1 191 ? 56.362 58.257  54.287 1.00 39.02  ?  148 GLU A CB  1 
ATOM   1144 C CG  . GLU A 1 191 ? 57.771 57.853  53.845 1.00 45.11  ?  148 GLU A CG  1 
ATOM   1145 C CD  . GLU A 1 191 ? 58.625 59.026  53.374 1.00 56.49  ?  148 GLU A CD  1 
ATOM   1146 O OE1 . GLU A 1 191 ? 58.380 60.165  53.821 1.00 67.19  ?  148 GLU A OE1 1 
ATOM   1147 O OE2 . GLU A 1 191 ? 59.539 58.807  52.541 1.00 62.33  ?  148 GLU A OE2 1 
ATOM   1148 N N   . GLU A 1 192 ? 53.080 57.884  54.232 1.00 37.90  ?  149 GLU A N   1 
ATOM   1149 C CA  . GLU A 1 192 ? 51.785 58.196  54.832 1.00 43.97  ?  149 GLU A CA  1 
ATOM   1150 C C   . GLU A 1 192 ? 51.091 56.938  55.346 1.00 47.44  ?  149 GLU A C   1 
ATOM   1151 O O   . GLU A 1 192 ? 50.457 56.965  56.410 1.00 43.99  ?  149 GLU A O   1 
ATOM   1152 C CB  . GLU A 1 192 ? 50.896 58.928  53.828 1.00 35.17  ?  149 GLU A CB  1 
ATOM   1153 C CG  . GLU A 1 192 ? 51.291 60.367  53.599 1.00 41.07  ?  149 GLU A CG  1 
ATOM   1154 C CD  . GLU A 1 192 ? 50.812 60.895  52.257 1.00 42.67  ?  149 GLU A CD  1 
ATOM   1155 O OE1 . GLU A 1 192 ? 50.140 60.141  51.515 1.00 41.68  ?  149 GLU A OE1 1 
ATOM   1156 O OE2 . GLU A 1 192 ? 51.107 62.064  51.950 1.00 38.47  ?  149 GLU A OE2 1 
ATOM   1157 N N   . ASP A 1 193 ? 51.196 55.829  54.609 1.00 38.15  ?  150 ASP A N   1 
ATOM   1158 C CA  . ASP A 1 193 ? 50.611 54.561  55.055 1.00 34.33  ?  150 ASP A CA  1 
ATOM   1159 C C   . ASP A 1 193 ? 51.367 53.412  54.385 1.00 37.48  ?  150 ASP A C   1 
ATOM   1160 O O   . ASP A 1 193 ? 51.139 53.115  53.203 1.00 34.11  ?  150 ASP A O   1 
ATOM   1161 C CB  . ASP A 1 193 ? 49.121 54.502  54.754 1.00 30.60  ?  150 ASP A CB  1 
ATOM   1162 C CG  . ASP A 1 193 ? 48.482 53.179  55.208 1.00 37.18  ?  150 ASP A CG  1 
ATOM   1163 O OD1 . ASP A 1 193 ? 49.144 52.400  55.932 1.00 39.76  ?  150 ASP A OD1 1 
ATOM   1164 O OD2 . ASP A 1 193 ? 47.314 52.928  54.844 1.00 44.70  ?  150 ASP A OD2 1 
ATOM   1165 N N   . ALA A 1 194 ? 52.243 52.767  55.157 1.00 36.19  ?  151 ALA A N   1 
ATOM   1166 C CA  . ALA A 1 194 ? 53.072 51.685  54.640 1.00 34.85  ?  151 ALA A CA  1 
ATOM   1167 C C   . ALA A 1 194 ? 52.253 50.507  54.130 1.00 32.05  ?  151 ALA A C   1 
ATOM   1168 O O   . ALA A 1 194 ? 52.753 49.740  53.295 1.00 32.94  ?  151 ALA A O   1 
ATOM   1169 C CB  . ALA A 1 194 ? 54.066 51.211  55.723 1.00 31.96  ?  151 ALA A CB  1 
ATOM   1170 N N   . LEU A 1 195 ? 51.009 50.343  54.592 1.00 29.31  ?  152 LEU A N   1 
ATOM   1171 C CA  . LEU A 1 195 ? 50.194 49.250  54.077 1.00 30.47  ?  152 LEU A CA  1 
ATOM   1172 C C   . LEU A 1 195 ? 49.991 49.396  52.573 1.00 27.86  ?  152 LEU A C   1 
ATOM   1173 O O   . LEU A 1 195 ? 49.800 48.403  51.878 1.00 32.20  ?  152 LEU A O   1 
ATOM   1174 C CB  . LEU A 1 195 ? 48.838 49.193  54.787 1.00 31.66  ?  152 LEU A CB  1 
ATOM   1175 C CG  . LEU A 1 195 ? 47.908 48.068  54.317 1.00 40.73  ?  152 LEU A CG  1 
ATOM   1176 C CD1 . LEU A 1 195 ? 48.431 46.675  54.679 1.00 32.85  ?  152 LEU A CD1 1 
ATOM   1177 C CD2 . LEU A 1 195 ? 46.502 48.252  54.840 1.00 48.18  ?  152 LEU A CD2 1 
ATOM   1178 N N   . ARG A 1 196 ? 50.057 50.621  52.066 1.00 29.63  ?  153 ARG A N   1 
ATOM   1179 C CA  . ARG A 1 196 ? 49.895 50.845  50.622 1.00 29.45  ?  153 ARG A CA  1 
ATOM   1180 C C   . ARG A 1 196 ? 50.916 50.070  49.803 1.00 35.55  ?  153 ARG A C   1 
ATOM   1181 O O   . ARG A 1 196 ? 50.648 49.721  48.643 1.00 33.07  ?  153 ARG A O   1 
ATOM   1182 C CB  . ARG A 1 196 ? 50.010 52.330  50.338 1.00 29.65  ?  153 ARG A CB  1 
ATOM   1183 C CG  . ARG A 1 196 ? 48.827 53.117  50.812 1.00 29.65  ?  153 ARG A CG  1 
ATOM   1184 C CD  . ARG A 1 196 ? 49.160 54.562  50.817 1.00 31.35  ?  153 ARG A CD  1 
ATOM   1185 N NE  . ARG A 1 196 ? 47.969 55.382  51.007 1.00 32.93  ?  153 ARG A NE  1 
ATOM   1186 C CZ  . ARG A 1 196 ? 47.998 56.706  50.990 1.00 38.02  ?  153 ARG A CZ  1 
ATOM   1187 N NH1 . ARG A 1 196 ? 49.142 57.338  50.817 1.00 37.01  ?  153 ARG A NH1 1 
ATOM   1188 N NH2 . ARG A 1 196 ? 46.900 57.404  51.170 1.00 36.58  ?  153 ARG A NH2 1 
ATOM   1189 N N   . MET A 1 197 ? 52.108 49.823  50.361 1.00 30.78  ?  154 MET A N   1 
ATOM   1190 C CA  . MET A 1 197 ? 53.089 49.031  49.630 1.00 33.73  ?  154 MET A CA  1 
ATOM   1191 C C   . MET A 1 197 ? 52.558 47.635  49.348 1.00 33.37  ?  154 MET A C   1 
ATOM   1192 O O   . MET A 1 197 ? 52.730 47.105  48.248 1.00 31.18  ?  154 MET A O   1 
ATOM   1193 C CB  . MET A 1 197 ? 54.412 48.950  50.408 1.00 28.54  ?  154 MET A CB  1 
ATOM   1194 C CG  . MET A 1 197 ? 55.107 50.257  50.609 1.00 35.28  ?  154 MET A CG  1 
ATOM   1195 S SD  . MET A 1 197 ? 56.725 50.032  51.416 1.00 35.72  ?  154 MET A SD  1 
ATOM   1196 C CE  . MET A 1 197 ? 56.210 49.707  53.113 1.00 30.38  ?  154 MET A CE  1 
ATOM   1197 N N   . LEU A 1 198 ? 51.899 47.033  50.317 1.00 32.76  ?  155 LEU A N   1 
ATOM   1198 C CA  . LEU A 1 198 ? 51.341 45.705  50.149 1.00 29.09  ?  155 LEU A CA  1 
ATOM   1199 C C   . LEU A 1 198 ? 50.087 45.753  49.304 1.00 29.44  ?  155 LEU A C   1 
ATOM   1200 O O   . LEU A 1 198 ? 49.797 44.865  48.562 1.00 33.34  ?  155 LEU A O   1 
ATOM   1201 C CB  . LEU A 1 198 ? 51.052 45.074  51.493 1.00 28.18  ?  155 LEU A CB  1 
ATOM   1202 C CG  . LEU A 1 198 ? 50.490 43.677  51.518 1.00 30.53  ?  155 LEU A CG  1 
ATOM   1203 C CD1 . LEU A 1 198 ? 51.325 42.690  50.752 1.00 31.73  ?  155 LEU A CD1 1 
ATOM   1204 C CD2 . LEU A 1 198 ? 50.244 43.215  52.939 1.00 30.76  ?  155 LEU A CD2 1 
ATOM   1205 N N   . ARG A 1 199 ? 49.353 46.832  49.430 1.00 31.88  ?  156 ARG A N   1 
ATOM   1206 C CA  . ARG A 1 199 ? 48.154 47.013  48.653 1.00 29.58  ?  156 ARG A CA  1 
ATOM   1207 C C   . ARG A 1 199 ? 48.487 47.058  47.170 1.00 31.94  ?  156 ARG A C   1 
ATOM   1208 O O   . ARG A 1 199 ? 47.742 46.590  46.375 1.00 30.42  ?  156 ARG A O   1 
ATOM   1209 C CB  . ARG A 1 199 ? 47.434 48.278  49.058 1.00 30.37  ?  156 ARG A CB  1 
ATOM   1210 C CG  . ARG A 1 199 ? 45.941 48.214  48.911 1.00 39.15  ?  156 ARG A CG  1 
ATOM   1211 C CD  . ARG A 1 199 ? 45.234 48.892  50.060 1.00 55.46  ?  156 ARG A CD  1 
ATOM   1212 N NE  . ARG A 1 199 ? 45.261 50.308  49.907 1.00 52.20  ?  156 ARG A NE  1 
ATOM   1213 C CZ  . ARG A 1 199 ? 45.108 51.162  50.890 1.00 47.87  ?  156 ARG A CZ  1 
ATOM   1214 N NH1 . ARG A 1 199 ? 44.904 50.736  52.112 1.00 44.40  ?  156 ARG A NH1 1 
ATOM   1215 N NH2 . ARG A 1 199 ? 45.172 52.447  50.642 1.00 47.66  ?  156 ARG A NH2 1 
ATOM   1216 N N   . ALA A 1 200 ? 49.622 47.624  46.819 1.00 30.41  ?  157 ALA A N   1 
ATOM   1217 C CA  . ALA A 1 200 ? 50.028 47.675  45.433 1.00 35.84  ?  157 ALA A CA  1 
ATOM   1218 C C   . ALA A 1 200 ? 50.135 46.258  44.914 1.00 35.80  ?  157 ALA A C   1 
ATOM   1219 O O   . ALA A 1 200 ? 49.666 45.983  43.856 1.00 30.60  ?  157 ALA A O   1 
ATOM   1220 C CB  . ALA A 1 200 ? 51.323 48.418  45.264 1.00 33.13  ?  157 ALA A CB  1 
ATOM   1221 N N   . ILE A 1 201 ? 50.743 45.373  45.694 1.00 32.69  ?  158 ILE A N   1 
ATOM   1222 C CA  . ILE A 1 201 ? 50.865 43.968  45.299 1.00 34.06  ?  158 ILE A CA  1 
ATOM   1223 C C   . ILE A 1 201 ? 49.489 43.353  45.108 1.00 35.85  ?  158 ILE A C   1 
ATOM   1224 O O   . ILE A 1 201 ? 49.232 42.640  44.131 1.00 35.08  ?  158 ILE A O   1 
ATOM   1225 C CB  . ILE A 1 201 ? 51.655 43.162  46.350 1.00 37.54  ?  158 ILE A CB  1 
ATOM   1226 C CG1 . ILE A 1 201 ? 52.904 43.893  46.864 1.00 48.35  ?  158 ILE A CG1 1 
ATOM   1227 C CG2 . ILE A 1 201 ? 51.927 41.760  45.836 1.00 35.61  ?  158 ILE A CG2 1 
ATOM   1228 C CD1 . ILE A 1 201 ? 53.908 44.259  45.831 1.00 39.43  ?  158 ILE A CD1 1 
ATOM   1229 N N   . ARG A 1 202 ? 48.594 43.571  46.078 1.00 31.18  ?  159 ARG A N   1 
ATOM   1230 C CA  . ARG A 1 202 ? 47.257 43.002  45.970 1.00 30.83  ?  159 ARG A CA  1 
ATOM   1231 C C   . ARG A 1 202 ? 46.546 43.497  44.707 1.00 32.80  ?  159 ARG A C   1 
ATOM   1232 O O   . ARG A 1 202 ? 45.887 42.714  44.009 1.00 33.66  ?  159 ARG A O   1 
ATOM   1233 C CB  . ARG A 1 202 ? 46.447 43.337  47.227 1.00 33.98  ?  159 ARG A CB  1 
ATOM   1234 C CG  . ARG A 1 202 ? 45.090 42.650  47.276 1.00 38.59  ?  159 ARG A CG  1 
ATOM   1235 C CD  . ARG A 1 202 ? 43.979 43.630  46.906 1.00 32.94  ?  159 ARG A CD  1 
ATOM   1236 N NE  . ARG A 1 202 ? 43.744 44.592  47.972 1.00 38.23  ?  159 ARG A NE  1 
ATOM   1237 C CZ  . ARG A 1 202 ? 42.767 45.491  47.964 1.00 40.93  ?  159 ARG A CZ  1 
ATOM   1238 N NH1 . ARG A 1 202 ? 41.924 45.555  46.935 1.00 37.43  ?  159 ARG A NH1 1 
ATOM   1239 N NH2 . ARG A 1 202 ? 42.623 46.316  48.988 1.00 37.58  ?  159 ARG A NH2 1 
ATOM   1240 N N   . PHE A 1 203 ? 46.644 44.799  44.409 1.00 31.02  ?  160 PHE A N   1 
ATOM   1241 C CA  . PHE A 1 203 ? 45.961 45.317  43.221 1.00 32.15  ?  160 PHE A CA  1 
ATOM   1242 C C   . PHE A 1 203 ? 46.516 44.691  41.949 1.00 32.83  ?  160 PHE A C   1 
ATOM   1243 O O   . PHE A 1 203 ? 45.765 44.448  40.997 1.00 34.59  ?  160 PHE A O   1 
ATOM   1244 C CB  . PHE A 1 203 ? 46.074 46.840  43.146 1.00 31.12  ?  160 PHE A CB  1 
ATOM   1245 C CG  . PHE A 1 203 ? 45.053 47.565  43.978 1.00 35.37  ?  160 PHE A CG  1 
ATOM   1246 C CD1 . PHE A 1 203 ? 43.714 47.198  43.937 1.00 36.41  ?  160 PHE A CD1 1 
ATOM   1247 C CD2 . PHE A 1 203 ? 45.438 48.608  44.814 1.00 31.05  ?  160 PHE A CD2 1 
ATOM   1248 C CE1 . PHE A 1 203 ? 42.766 47.875  44.715 1.00 38.69  ?  160 PHE A CE1 1 
ATOM   1249 C CE2 . PHE A 1 203 ? 44.507 49.282  45.602 1.00 31.19  ?  160 PHE A CE2 1 
ATOM   1250 C CZ  . PHE A 1 203 ? 43.166 48.910  45.548 1.00 37.25  ?  160 PHE A CZ  1 
ATOM   1251 N N   . SER A 1 204 ? 47.830 44.443  41.903 1.00 32.17  ?  161 SER A N   1 
ATOM   1252 C CA  . SER A 1 204 ? 48.429 43.898  40.682 1.00 36.00  ?  161 SER A CA  1 
ATOM   1253 C C   . SER A 1 204 ? 47.763 42.590  40.281 1.00 38.32  ?  161 SER A C   1 
ATOM   1254 O O   . SER A 1 204 ? 47.491 42.366  39.096 1.00 36.75  ?  161 SER A O   1 
ATOM   1255 C CB  . SER A 1 204 ? 49.940 43.701  40.853 1.00 31.86  ?  161 SER A CB  1 
ATOM   1256 O OG  . SER A 1 204 ? 50.247 42.623  41.749 1.00 39.02  ?  161 SER A OG  1 
ATOM   1257 N N   . GLY A 1 205 ? 47.494 41.713  41.249 1.00 37.75  ?  162 GLY A N   1 
ATOM   1258 C CA  . GLY A 1 205 ? 46.806 40.460  40.988 1.00 36.10  ?  162 GLY A CA  1 
ATOM   1259 C C   . GLY A 1 205 ? 45.321 40.643  40.740 1.00 42.35  ?  162 GLY A C   1 
ATOM   1260 O O   . GLY A 1 205 ? 44.755 40.080  39.790 1.00 42.87  ?  162 GLY A O   1 
ATOM   1261 N N   . GLN A 1 206 ? 44.680 41.446  41.590 1.00 36.71  ?  163 GLN A N   1 
ATOM   1262 C CA  . GLN A 1 206 ? 43.254 41.723  41.439 1.00 35.76  ?  163 GLN A CA  1 
ATOM   1263 C C   . GLN A 1 206 ? 42.921 42.225  40.035 1.00 40.70  ?  163 GLN A C   1 
ATOM   1264 O O   . GLN A 1 206 ? 41.906 41.832  39.447 1.00 37.92  ?  163 GLN A O   1 
ATOM   1265 C CB  . GLN A 1 206 ? 42.813 42.749  42.485 1.00 42.26  ?  163 GLN A CB  1 
ATOM   1266 C CG  . GLN A 1 206 ? 41.367 43.223  42.360 1.00 38.30  ?  163 GLN A CG  1 
ATOM   1267 C CD  . GLN A 1 206 ? 40.999 44.250  43.421 1.00 41.28  ?  163 GLN A CD  1 
ATOM   1268 O OE1 . GLN A 1 206 ? 41.490 44.191  44.541 1.00 40.17  ?  163 GLN A OE1 1 
ATOM   1269 N NE2 . GLN A 1 206 ? 40.149 45.211  43.059 1.00 40.81  ?  163 GLN A NE2 1 
ATOM   1270 N N   . LEU A 1 207 ? 43.753 43.107  39.495 1.00 35.25  ?  164 LEU A N   1 
ATOM   1271 C CA  . LEU A 1 207 ? 43.465 43.776  38.236 1.00 39.07  ?  164 LEU A CA  1 
ATOM   1272 C C   . LEU A 1 207 ? 44.246 43.210  37.055 1.00 39.08  ?  164 LEU A C   1 
ATOM   1273 O O   . LEU A 1 207 ? 44.008 43.635  35.917 1.00 37.42  ?  164 LEU A O   1 
ATOM   1274 C CB  . LEU A 1 207 ? 43.770 45.273  38.368 1.00 31.00  ?  164 LEU A CB  1 
ATOM   1275 C CG  . LEU A 1 207 ? 43.084 46.012  39.534 1.00 35.34  ?  164 LEU A CG  1 
ATOM   1276 C CD1 . LEU A 1 207 ? 43.630 47.415  39.642 1.00 31.35  ?  164 LEU A CD1 1 
ATOM   1277 C CD2 . LEU A 1 207 ? 41.579 46.047  39.342 1.00 39.55  ?  164 LEU A CD2 1 
ATOM   1278 N N   . ASP A 1 208 ? 45.172 42.288  37.294 1.00 35.67  ?  165 ASP A N   1 
ATOM   1279 C CA  . ASP A 1 208 ? 46.168 41.892  36.296 1.00 41.28  ?  165 ASP A CA  1 
ATOM   1280 C C   . ASP A 1 208 ? 46.882 43.114  35.705 1.00 40.82  ?  165 ASP A C   1 
ATOM   1281 O O   . ASP A 1 208 ? 46.995 43.278  34.488 1.00 39.46  ?  165 ASP A O   1 
ATOM   1282 C CB  . ASP A 1 208 ? 45.534 41.040  35.193 1.00 39.31  ?  165 ASP A CB  1 
ATOM   1283 C CG  . ASP A 1 208 ? 46.576 40.314  34.343 1.00 48.79  ?  165 ASP A CG  1 
ATOM   1284 O OD1 . ASP A 1 208 ? 47.670 39.991  34.863 1.00 55.16  ?  165 ASP A OD1 1 
ATOM   1285 O OD2 . ASP A 1 208 ? 46.305 40.080  33.146 1.00 60.02  ?  165 ASP A OD2 1 
ATOM   1286 N N   . PHE A 1 209 ? 47.356 43.988  36.585 1.00 35.71  ?  166 PHE A N   1 
ATOM   1287 C CA  . PHE A 1 209 ? 48.204 45.117  36.228 1.00 32.70  ?  166 PHE A CA  1 
ATOM   1288 C C   . PHE A 1 209 ? 49.634 44.860  36.683 1.00 39.08  ?  166 PHE A C   1 
ATOM   1289 O O   . PHE A 1 209 ? 49.889 44.055  37.584 1.00 38.17  ?  166 PHE A O   1 
ATOM   1290 C CB  . PHE A 1 209 ? 47.739 46.427  36.878 1.00 30.61  ?  166 PHE A CB  1 
ATOM   1291 C CG  . PHE A 1 209 ? 46.482 47.022  36.294 1.00 35.95  ?  166 PHE A CG  1 
ATOM   1292 C CD1 . PHE A 1 209 ? 45.620 46.277  35.493 1.00 39.04  ?  166 PHE A CD1 1 
ATOM   1293 C CD2 . PHE A 1 209 ? 46.179 48.355  36.543 1.00 31.27  ?  166 PHE A CD2 1 
ATOM   1294 C CE1 . PHE A 1 209 ? 44.466 46.851  34.970 1.00 36.40  ?  166 PHE A CE1 1 
ATOM   1295 C CE2 . PHE A 1 209 ? 45.033 48.938  36.021 1.00 38.00  ?  166 PHE A CE2 1 
ATOM   1296 C CZ  . PHE A 1 209 ? 44.174 48.186  35.230 1.00 37.53  ?  166 PHE A CZ  1 
ATOM   1297 N N   . ILE A 1 210 ? 50.559 45.607  36.096 1.00 34.20  ?  167 ILE A N   1 
ATOM   1298 C CA  . ILE A 1 210 ? 51.931 45.657  36.573 1.00 34.74  ?  167 ILE A CA  1 
ATOM   1299 C C   . ILE A 1 210 ? 52.072 46.826  37.531 1.00 33.81  ?  167 ILE A C   1 
ATOM   1300 O O   . ILE A 1 210 ? 51.292 47.786  37.515 1.00 34.35  ?  167 ILE A O   1 
ATOM   1301 C CB  . ILE A 1 210 ? 52.954 45.796  35.421 1.00 40.30  ?  167 ILE A CB  1 
ATOM   1302 C CG1 . ILE A 1 210 ? 52.765 47.150  34.727 1.00 39.73  ?  167 ILE A CG1 1 
ATOM   1303 C CG2 . ILE A 1 210 ? 52.854 44.613  34.456 1.00 43.08  ?  167 ILE A CG2 1 
ATOM   1304 C CD1 . ILE A 1 210 ? 54.066 47.791  34.240 1.00 53.21  ?  167 ILE A CD1 1 
ATOM   1305 N N   . ILE A 1 211 ? 53.106 46.768  38.364 1.00 33.44  ?  168 ILE A N   1 
ATOM   1306 C CA  . ILE A 1 211 ? 53.428 47.884  39.236 1.00 30.81  ?  168 ILE A CA  1 
ATOM   1307 C C   . ILE A 1 211 ? 54.419 48.800  38.542 1.00 33.55  ?  168 ILE A C   1 
ATOM   1308 O O   . ILE A 1 211 ? 55.485 48.356  38.089 1.00 35.50  ?  168 ILE A O   1 
ATOM   1309 C CB  . ILE A 1 211 ? 53.986 47.395  40.585 1.00 30.03  ?  168 ILE A CB  1 
ATOM   1310 C CG1 . ILE A 1 211 ? 52.971 46.453  41.239 1.00 33.84  ?  168 ILE A CG1 1 
ATOM   1311 C CG2 . ILE A 1 211 ? 54.299 48.603  41.468 1.00 29.54  ?  168 ILE A CG2 1 
ATOM   1312 C CD1 . ILE A 1 211 ? 53.445 45.845  42.576 1.00 33.20  ?  168 ILE A CD1 1 
ATOM   1313 N N   . ASP A 1 212 ? 54.077 50.083  38.497 1.00 33.12  ?  169 ASP A N   1 
ATOM   1314 C CA  . ASP A 1 212 ? 54.942 51.123  37.961 1.00 33.39  ?  169 ASP A CA  1 
ATOM   1315 C C   . ASP A 1 212 ? 56.365 51.017  38.503 1.00 39.04  ?  169 ASP A C   1 
ATOM   1316 O O   . ASP A 1 212 ? 56.577 50.910  39.715 1.00 29.63  ?  169 ASP A O   1 
ATOM   1317 C CB  . ASP A 1 212 ? 54.348 52.480  38.323 1.00 30.99  ?  169 ASP A CB  1 
ATOM   1318 C CG  . ASP A 1 212 ? 55.305 53.626  38.062 1.00 36.63  ?  169 ASP A CG  1 
ATOM   1319 O OD1 . ASP A 1 212 ? 55.601 53.887  36.869 1.00 39.44  ?  169 ASP A OD1 1 
ATOM   1320 O OD2 . ASP A 1 212 ? 55.734 54.282  39.042 1.00 34.24  ?  169 ASP A OD2 1 
ATOM   1321 N N   . MET A 1 213 ? 57.347 51.131  37.600 1.00 33.61  ?  170 MET A N   1 
ATOM   1322 C CA  . MET A 1 213 ? 58.742 50.912  37.979 1.00 35.09  ?  170 MET A CA  1 
ATOM   1323 C C   . MET A 1 213 ? 59.176 51.850  39.096 1.00 35.04  ?  170 MET A C   1 
ATOM   1324 O O   . MET A 1 213 ? 59.717 51.410  40.118 1.00 34.07  ?  170 MET A O   1 
ATOM   1325 C CB  . MET A 1 213 ? 59.653 51.072  36.750 1.00 32.03  ?  170 MET A CB  1 
ATOM   1326 C CG  . MET A 1 213 ? 61.128 50.976  37.074 1.00 48.98  ?  170 MET A CG  1 
ATOM   1327 S SD  . MET A 1 213 ? 61.505 49.349  37.744 1.00 48.75  ?  170 MET A SD  1 
ATOM   1328 C CE  . MET A 1 213 ? 61.171 48.307  36.309 1.00 54.83  ?  170 MET A CE  1 
ATOM   1329 N N   . LYS A 1 214 ? 58.958 53.154  38.932 1.00 34.31  ?  171 LYS A N   1 
ATOM   1330 C CA  . LYS A 1 214 ? 59.377 54.069  39.984 1.00 32.67  ?  171 LYS A CA  1 
ATOM   1331 C C   . LYS A 1 214 ? 58.657 53.749  41.291 1.00 37.27  ?  171 LYS A C   1 
ATOM   1332 O O   . LYS A 1 214 ? 59.245 53.835  42.378 1.00 35.28  ?  171 LYS A O   1 
ATOM   1333 C CB  . LYS A 1 214 ? 59.114 55.517  39.569 1.00 36.83  ?  171 LYS A CB  1 
ATOM   1334 C CG  . LYS A 1 214 ? 59.538 56.530  40.623 1.00 43.77  ?  171 LYS A CG  1 
ATOM   1335 C CD  . LYS A 1 214 ? 59.094 57.948  40.262 1.00 52.43  ?  171 LYS A CD  1 
ATOM   1336 C CE  . LYS A 1 214 ? 59.621 58.949  41.288 1.00 64.93  ?  171 LYS A CE  1 
ATOM   1337 N NZ  . LYS A 1 214 ? 59.138 60.327  41.022 1.00 69.51  ?  171 LYS A NZ  1 
ATOM   1338 N N   . THR A 1 215 ? 57.383 53.367  41.199 1.00 34.90  ?  172 THR A N   1 
ATOM   1339 C CA  . THR A 1 215 ? 56.629 52.978  42.393 1.00 34.17  ?  172 THR A CA  1 
ATOM   1340 C C   . THR A 1 215 ? 57.228 51.735  43.047 1.00 34.35  ?  172 THR A C   1 
ATOM   1341 O O   . THR A 1 215 ? 57.411 51.688  44.272 1.00 34.42  ?  172 THR A O   1 
ATOM   1342 C CB  . THR A 1 215 ? 55.158 52.751  42.020 1.00 32.71  ?  172 THR A CB  1 
ATOM   1343 O OG1 . THR A 1 215 ? 54.582 54.011  41.619 1.00 32.20  ?  172 THR A OG1 1 
ATOM   1344 C CG2 . THR A 1 215 ? 54.372 52.173  43.233 1.00 32.27  ?  172 THR A CG2 1 
ATOM   1345 N N   . LEU A 1 216 ? 57.518 50.710  42.250 1.00 29.11  ?  173 LEU A N   1 
ATOM   1346 C CA  . LEU A 1 216 ? 58.099 49.481  42.787 1.00 33.95  ?  173 LEU A CA  1 
ATOM   1347 C C   . LEU A 1 216 ? 59.457 49.738  43.444 1.00 37.41  ?  173 LEU A C   1 
ATOM   1348 O O   . LEU A 1 216 ? 59.733 49.228  44.540 1.00 35.37  ?  173 LEU A O   1 
ATOM   1349 C CB  . LEU A 1 216 ? 58.221 48.437  41.676 1.00 34.85  ?  173 LEU A CB  1 
ATOM   1350 C CG  . LEU A 1 216 ? 58.737 47.033  42.012 1.00 38.67  ?  173 LEU A CG  1 
ATOM   1351 C CD1 . LEU A 1 216 ? 57.878 46.367  43.080 1.00 33.20  ?  173 LEU A CD1 1 
ATOM   1352 C CD2 . LEU A 1 216 ? 58.751 46.208  40.734 1.00 36.91  ?  173 LEU A CD2 1 
ATOM   1353 N N   . LEU A 1 217 ? 60.318 50.531  42.797 1.00 33.17  ?  174 LEU A N   1 
ATOM   1354 C CA  . LEU A 1 217 ? 61.605 50.866  43.409 1.00 40.92  ?  174 LEU A CA  1 
ATOM   1355 C C   . LEU A 1 217 ? 61.410 51.587  44.737 1.00 40.88  ?  174 LEU A C   1 
ATOM   1356 O O   . LEU A 1 217 ? 62.185 51.391  45.683 1.00 37.68  ?  174 LEU A O   1 
ATOM   1357 C CB  . LEU A 1 217 ? 62.441 51.719  42.450 1.00 33.93  ?  174 LEU A CB  1 
ATOM   1358 C CG  . LEU A 1 217 ? 62.820 51.046  41.129 1.00 37.30  ?  174 LEU A CG  1 
ATOM   1359 C CD1 . LEU A 1 217 ? 63.523 52.039  40.186 1.00 38.63  ?  174 LEU A CD1 1 
ATOM   1360 C CD2 . LEU A 1 217 ? 63.687 49.796  41.345 1.00 39.54  ?  174 LEU A CD2 1 
ATOM   1361 N N   . SER A 1 218 ? 60.389 52.439  44.823 1.00 34.96  ?  175 SER A N   1 
ATOM   1362 C CA  . SER A 1 218 ? 60.094 53.106  46.082 1.00 38.69  ?  175 SER A CA  1 
ATOM   1363 C C   . SER A 1 218 ? 59.649 52.108  47.147 1.00 41.00  ?  175 SER A C   1 
ATOM   1364 O O   . SER A 1 218 ? 60.008 52.252  48.319 1.00 38.98  ?  175 SER A O   1 
ATOM   1365 C CB  . SER A 1 218 ? 59.035 54.191  45.872 1.00 35.71  ?  175 SER A CB  1 
ATOM   1366 O OG  . SER A 1 218 ? 58.710 54.834  47.096 1.00 39.15  ?  175 SER A OG  1 
ATOM   1367 N N   . ILE A 1 219 ? 58.865 51.091  46.773 1.00 34.03  ?  176 ILE A N   1 
ATOM   1368 C CA  . ILE A 1 219 ? 58.513 50.063  47.752 1.00 40.75  ?  176 ILE A CA  1 
ATOM   1369 C C   . ILE A 1 219 ? 59.768 49.384  48.284 1.00 39.03  ?  176 ILE A C   1 
ATOM   1370 O O   . ILE A 1 219 ? 59.908 49.162  49.497 1.00 34.77  ?  176 ILE A O   1 
ATOM   1371 C CB  . ILE A 1 219 ? 57.550 49.036  47.143 1.00 37.53  ?  176 ILE A CB  1 
ATOM   1372 C CG1 . ILE A 1 219 ? 56.240 49.721  46.733 1.00 33.17  ?  176 ILE A CG1 1 
ATOM   1373 C CG2 . ILE A 1 219 ? 57.299 47.880  48.151 1.00 34.38  ?  176 ILE A CG2 1 
ATOM   1374 C CD1 . ILE A 1 219 ? 55.275 48.766  46.039 1.00 32.59  ?  176 ILE A CD1 1 
ATOM   1375 N N   . ARG A 1 220 ? 60.693 49.035  47.383 1.00 35.65  ?  177 ARG A N   1 
ATOM   1376 C CA  . ARG A 1 220 ? 61.930 48.379  47.796 1.00 39.25  ?  177 ARG A CA  1 
ATOM   1377 C C   . ARG A 1 220 ? 62.694 49.238  48.794 1.00 39.31  ?  177 ARG A C   1 
ATOM   1378 O O   . ARG A 1 220 ? 63.211 48.720  49.791 1.00 37.50  ?  177 ARG A O   1 
ATOM   1379 C CB  . ARG A 1 220 ? 62.813 48.060  46.582 1.00 39.20  ?  177 ARG A CB  1 
ATOM   1380 C CG  . ARG A 1 220 ? 62.193 47.085  45.585 1.00 39.16  ?  177 ARG A CG  1 
ATOM   1381 C CD  . ARG A 1 220 ? 63.249 46.412  44.692 1.00 45.76  ?  177 ARG A CD  1 
ATOM   1382 N NE  . ARG A 1 220 ? 64.305 47.338  44.295 1.00 49.48  ?  177 ARG A NE  1 
ATOM   1383 C CZ  . ARG A 1 220 ? 65.370 46.998  43.570 1.00 61.83  ?  177 ARG A CZ  1 
ATOM   1384 N NH1 . ARG A 1 220 ? 65.528 45.743  43.165 1.00 54.03  ?  177 ARG A NH1 1 
ATOM   1385 N NH2 . ARG A 1 220 ? 66.283 47.915  43.250 1.00 59.29  ?  177 ARG A NH2 1 
ATOM   1386 N N   . ARG A 1 221 ? 62.747 50.556  48.565 1.00 38.91  ?  178 ARG A N   1 
ATOM   1387 C CA  . ARG A 1 221 ? 63.446 51.437  49.499 1.00 38.32  ?  178 ARG A CA  1 
ATOM   1388 C C   . ARG A 1 221 ? 62.722 51.552  50.832 1.00 46.92  ?  178 ARG A C   1 
ATOM   1389 O O   . ARG A 1 221 ? 63.378 51.740  51.864 1.00 39.55  ?  178 ARG A O   1 
ATOM   1390 C CB  . ARG A 1 221 ? 63.632 52.836  48.904 1.00 41.95  ?  178 ARG A CB  1 
ATOM   1391 C CG  . ARG A 1 221 ? 64.587 52.890  47.713 1.00 49.00  ?  178 ARG A CG  1 
ATOM   1392 C CD  . ARG A 1 221 ? 64.969 54.326  47.373 1.00 47.74  ?  178 ARG A CD  1 
ATOM   1393 N NE  . ARG A 1 221 ? 63.796 55.113  46.999 1.00 52.21  ?  178 ARG A NE  1 
ATOM   1394 C CZ  . ARG A 1 221 ? 63.276 55.139  45.777 1.00 54.98  ?  178 ARG A CZ  1 
ATOM   1395 N NH1 . ARG A 1 221 ? 63.835 54.428  44.798 1.00 56.12  ?  178 ARG A NH1 1 
ATOM   1396 N NH2 . ARG A 1 221 ? 62.204 55.880  45.528 1.00 51.19  ?  178 ARG A NH2 1 
ATOM   1397 N N   . HIS A 1 222 ? 61.388 51.453  50.847 1.00 39.49  ?  179 HIS A N   1 
ATOM   1398 C CA  . HIS A 1 222 ? 60.626 51.685  52.072 1.00 36.72  ?  179 HIS A CA  1 
ATOM   1399 C C   . HIS A 1 222 ? 60.059 50.413  52.688 1.00 34.18  ?  179 HIS A C   1 
ATOM   1400 O O   . HIS A 1 222 ? 59.243 50.509  53.612 1.00 36.45  ?  179 HIS A O   1 
ATOM   1401 C CB  . HIS A 1 222 ? 59.482 52.674  51.818 1.00 35.77  ?  179 HIS A CB  1 
ATOM   1402 C CG  . HIS A 1 222 ? 59.945 54.039  51.427 1.00 44.17  ?  179 HIS A CG  1 
ATOM   1403 N ND1 . HIS A 1 222 ? 60.384 54.334  50.150 1.00 45.09  ?  179 HIS A ND1 1 
ATOM   1404 C CD2 . HIS A 1 222 ? 60.049 55.186  52.137 1.00 43.24  ?  179 HIS A CD2 1 
ATOM   1405 C CE1 . HIS A 1 222 ? 60.732 55.606  50.093 1.00 44.47  ?  179 HIS A CE1 1 
ATOM   1406 N NE2 . HIS A 1 222 ? 60.540 56.145  51.284 1.00 49.94  ?  179 HIS A NE2 1 
ATOM   1407 N N   . ALA A 1 223 ? 60.466 49.233  52.208 1.00 32.37  ?  180 ALA A N   1 
ATOM   1408 C CA  . ALA A 1 223 ? 59.840 47.986  52.641 1.00 33.78  ?  180 ALA A CA  1 
ATOM   1409 C C   . ALA A 1 223 ? 59.895 47.816  54.154 1.00 38.45  ?  180 ALA A C   1 
ATOM   1410 O O   . ALA A 1 223 ? 58.982 47.236  54.749 1.00 34.20  ?  180 ALA A O   1 
ATOM   1411 C CB  . ALA A 1 223 ? 60.524 46.796  51.980 1.00 31.81  ?  180 ALA A CB  1 
ATOM   1412 N N   . ARG A 1 224 ? 60.979 48.270  54.779 1.00 39.25  ?  181 ARG A N   1 
ATOM   1413 C CA  . ARG A 1 224 ? 61.137 48.095  56.220 1.00 35.13  ?  181 ARG A CA  1 
ATOM   1414 C C   . ARG A 1 224 ? 60.013 48.777  56.995 1.00 39.72  ?  181 ARG A C   1 
ATOM   1415 O O   . ARG A 1 224 ? 59.687 48.359  58.117 1.00 41.03  ?  181 ARG A O   1 
ATOM   1416 C CB  . ARG A 1 224 ? 62.516 48.629  56.627 1.00 38.11  ?  181 ARG A CB  1 
ATOM   1417 C CG  . ARG A 1 224 ? 62.801 48.604  58.112 1.00 59.62  ?  181 ARG A CG  1 
ATOM   1418 C CD  . ARG A 1 224 ? 64.230 49.060  58.415 1.00 63.69  ?  181 ARG A CD  1 
ATOM   1419 N NE  . ARG A 1 224 ? 64.439 49.250  59.851 1.00 75.68  ?  181 ARG A NE  1 
ATOM   1420 C CZ  . ARG A 1 224 ? 64.310 48.284  60.759 1.00 69.06  ?  181 ARG A CZ  1 
ATOM   1421 N NH1 . ARG A 1 224 ? 63.960 47.062  60.381 1.00 57.43  ?  181 ARG A NH1 1 
ATOM   1422 N NH2 . ARG A 1 224 ? 64.522 48.537  62.047 1.00 69.64  ?  181 ARG A NH2 1 
ATOM   1423 N N   . LEU A 1 225 ? 59.396 49.818  56.422 1.00 35.06  ?  182 LEU A N   1 
ATOM   1424 C CA  . LEU A 1 225 ? 58.300 50.484  57.112 1.00 36.55  ?  182 LEU A CA  1 
ATOM   1425 C C   . LEU A 1 225 ? 57.088 49.578  57.329 1.00 34.85  ?  182 LEU A C   1 
ATOM   1426 O O   . LEU A 1 225 ? 56.194 49.945  58.101 1.00 36.98  ?  182 LEU A O   1 
ATOM   1427 C CB  . LEU A 1 225 ? 57.870 51.735  56.349 1.00 36.65  ?  182 LEU A CB  1 
ATOM   1428 C CG  . LEU A 1 225 ? 58.855 52.899  56.234 1.00 41.62  ?  182 LEU A CG  1 
ATOM   1429 C CD1 . LEU A 1 225 ? 58.194 54.038  55.503 1.00 37.00  ?  182 LEU A CD1 1 
ATOM   1430 C CD2 . LEU A 1 225 ? 59.335 53.356  57.623 1.00 39.21  ?  182 LEU A CD2 1 
ATOM   1431 N N   . ILE A 1 226 ? 57.036 48.413  56.683 1.00 29.68  ?  183 ILE A N   1 
ATOM   1432 C CA  . ILE A 1 226 ? 55.886 47.537  56.854 1.00 32.67  ?  183 ILE A CA  1 
ATOM   1433 C C   . ILE A 1 226 ? 55.813 47.012  58.286 1.00 36.79  ?  183 ILE A C   1 
ATOM   1434 O O   . ILE A 1 226 ? 54.757 46.532  58.709 1.00 33.19  ?  183 ILE A O   1 
ATOM   1435 C CB  . ILE A 1 226 ? 55.933 46.360  55.861 1.00 36.71  ?  183 ILE A CB  1 
ATOM   1436 C CG1 . ILE A 1 226 ? 54.529 45.768  55.645 1.00 36.08  ?  183 ILE A CG1 1 
ATOM   1437 C CG2 . ILE A 1 226 ? 56.918 45.278  56.351 1.00 34.43  ?  183 ILE A CG2 1 
ATOM   1438 C CD1 . ILE A 1 226 ? 53.619 46.632  54.777 1.00 35.73  ?  183 ILE A CD1 1 
ATOM   1439 N N   . ARG A 1 227 ? 56.919 47.083  59.036 1.00 36.96  ?  184 ARG A N   1 
ATOM   1440 C CA  . ARG A 1 227 ? 56.918 46.613  60.422 1.00 39.31  ?  184 ARG A CA  1 
ATOM   1441 C C   . ARG A 1 227 ? 55.974 47.411  61.305 1.00 42.81  ?  184 ARG A C   1 
ATOM   1442 O O   . ARG A 1 227 ? 55.580 46.925  62.378 1.00 37.92  ?  184 ARG A O   1 
ATOM   1443 C CB  . ARG A 1 227 ? 58.332 46.675  61.015 1.00 39.28  ?  184 ARG A CB  1 
ATOM   1444 C CG  . ARG A 1 227 ? 58.878 48.081  61.232 1.00 37.96  ?  184 ARG A CG  1 
ATOM   1445 C CD  . ARG A 1 227 ? 60.340 47.999  61.680 1.00 49.84  ?  184 ARG A CD  1 
ATOM   1446 N NE  . ARG A 1 227 ? 60.885 49.254  62.206 1.00 45.87  ?  184 ARG A NE  1 
ATOM   1447 C CZ  . ARG A 1 227 ? 61.353 50.245  61.446 1.00 61.65  ?  184 ARG A CZ  1 
ATOM   1448 N NH1 . ARG A 1 227 ? 61.318 50.140  60.122 1.00 52.40  ?  184 ARG A NH1 1 
ATOM   1449 N NH2 . ARG A 1 227 ? 61.850 51.345  61.999 1.00 57.00  ?  184 ARG A NH2 1 
ATOM   1450 N N   . PHE A 1 228 ? 55.618 48.624  60.902 1.00 32.60  ?  185 PHE A N   1 
ATOM   1451 C CA  . PHE A 1 228 ? 54.735 49.450  61.710 1.00 36.80  ?  185 PHE A CA  1 
ATOM   1452 C C   . PHE A 1 228 ? 53.257 49.141  61.507 1.00 43.05  ?  185 PHE A C   1 
ATOM   1453 O O   . PHE A 1 228 ? 52.421 49.688  62.232 1.00 42.56  ?  185 PHE A O   1 
ATOM   1454 C CB  . PHE A 1 228 ? 55.008 50.925  61.417 1.00 37.55  ?  185 PHE A CB  1 
ATOM   1455 C CG  . PHE A 1 228 ? 56.373 51.378  61.851 1.00 44.86  ?  185 PHE A CG  1 
ATOM   1456 C CD1 . PHE A 1 228 ? 56.700 51.427  63.198 1.00 47.32  ?  185 PHE A CD1 1 
ATOM   1457 C CD2 . PHE A 1 228 ? 57.331 51.750  60.923 1.00 42.49  ?  185 PHE A CD2 1 
ATOM   1458 C CE1 . PHE A 1 228 ? 57.952 51.843  63.615 1.00 50.32  ?  185 PHE A CE1 1 
ATOM   1459 C CE2 . PHE A 1 228 ? 58.593 52.173  61.335 1.00 50.41  ?  185 PHE A CE2 1 
ATOM   1460 C CZ  . PHE A 1 228 ? 58.899 52.214  62.691 1.00 49.62  ?  185 PHE A CZ  1 
ATOM   1461 N N   . ILE A 1 229 ? 52.901 48.278  60.562 1.00 36.79  ?  186 ILE A N   1 
ATOM   1462 C CA  . ILE A 1 229 ? 51.503 48.057  60.220 1.00 30.66  ?  186 ILE A CA  1 
ATOM   1463 C C   . ILE A 1 229 ? 50.935 46.940  61.083 1.00 32.96  ?  186 ILE A C   1 
ATOM   1464 O O   . ILE A 1 229 ? 51.550 45.875  61.230 1.00 35.45  ?  186 ILE A O   1 
ATOM   1465 C CB  . ILE A 1 229 ? 51.356 47.736  58.720 1.00 29.95  ?  186 ILE A CB  1 
ATOM   1466 C CG1 . ILE A 1 229 ? 51.943 48.905  57.921 1.00 29.78  ?  186 ILE A CG1 1 
ATOM   1467 C CG2 . ILE A 1 229 ? 49.896 47.506  58.378 1.00 30.04  ?  186 ILE A CG2 1 
ATOM   1468 C CD1 . ILE A 1 229 ? 51.248 50.213  58.209 1.00 31.78  ?  186 ILE A CD1 1 
ATOM   1469 N N   . ALA A 1 230 ? 49.753 47.185  61.649 1.00 37.55  ?  187 ALA A N   1 
ATOM   1470 C CA  . ALA A 1 230 ? 49.049 46.168  62.419 1.00 37.96  ?  187 ALA A CA  1 
ATOM   1471 C C   . ALA A 1 230 ? 48.903 44.889  61.607 1.00 40.18  ?  187 ALA A C   1 
ATOM   1472 O O   . ALA A 1 230 ? 48.530 44.920  60.428 1.00 38.59  ?  187 ALA A O   1 
ATOM   1473 C CB  . ALA A 1 230 ? 47.674 46.691  62.843 1.00 35.27  ?  187 ALA A CB  1 
ATOM   1474 N N   . VAL A 1 231 ? 49.207 43.763  62.248 1.00 36.62  ?  188 VAL A N   1 
ATOM   1475 C CA  . VAL A 1 231 ? 49.236 42.473  61.569 1.00 31.41  ?  188 VAL A CA  1 
ATOM   1476 C C   . VAL A 1 231 ? 47.862 42.112  61.007 1.00 41.82  ?  188 VAL A C   1 
ATOM   1477 O O   . VAL A 1 231 ? 47.765 41.441  59.967 1.00 39.04  ?  188 VAL A O   1 
ATOM   1478 C CB  . VAL A 1 231 ? 49.799 41.412  62.542 1.00 40.47  ?  188 VAL A CB  1 
ATOM   1479 C CG1 . VAL A 1 231 ? 48.724 40.903  63.529 1.00 39.04  ?  188 VAL A CG1 1 
ATOM   1480 C CG2 . VAL A 1 231 ? 50.459 40.268  61.803 1.00 42.87  ?  188 VAL A CG2 1 
ATOM   1481 N N   . GLU A 1 232 ? 46.781 42.594  61.634 1.00 36.39  ?  189 GLU A N   1 
ATOM   1482 C CA  . GLU A 1 232 ? 45.447 42.345  61.085 1.00 33.78  ?  189 GLU A CA  1 
ATOM   1483 C C   . GLU A 1 232 ? 45.296 42.930  59.682 1.00 32.99  ?  189 GLU A C   1 
ATOM   1484 O O   . GLU A 1 232 ? 44.649 42.325  58.816 1.00 38.71  ?  189 GLU A O   1 
ATOM   1485 C CB  . GLU A 1 232 ? 44.373 42.928  62.000 1.00 41.72  ?  189 GLU A CB  1 
ATOM   1486 C CG  . GLU A 1 232 ? 44.288 42.266  63.385 1.00 44.10  ?  189 GLU A CG  1 
ATOM   1487 C CD  . GLU A 1 232 ? 45.375 42.726  64.352 1.00 54.15  ?  189 GLU A CD  1 
ATOM   1488 O OE1 . GLU A 1 232 ? 46.137 43.675  64.029 1.00 42.89  ?  189 GLU A OE1 1 
ATOM   1489 O OE2 . GLU A 1 232 ? 45.458 42.141  65.458 1.00 51.96  ?  189 GLU A OE2 1 
ATOM   1490 N N   . ARG A 1 233 ? 45.839 44.131  59.455 1.00 33.58  ?  190 ARG A N   1 
ATOM   1491 C CA  . ARG A 1 233 ? 45.769 44.742  58.125 1.00 35.85  ?  190 ARG A CA  1 
ATOM   1492 C C   . ARG A 1 233 ? 46.634 43.982  57.124 1.00 37.31  ?  190 ARG A C   1 
ATOM   1493 O O   . ARG A 1 233 ? 46.258 43.833  55.952 1.00 35.76  ?  190 ARG A O   1 
ATOM   1494 C CB  . ARG A 1 233 ? 46.199 46.211  58.198 1.00 35.56  ?  190 ARG A CB  1 
ATOM   1495 C CG  . ARG A 1 233 ? 45.287 47.105  59.037 1.00 42.78  ?  190 ARG A CG  1 
ATOM   1496 C CD  . ARG A 1 233 ? 45.781 48.561  59.011 1.00 40.97  ?  190 ARG A CD  1 
ATOM   1497 N NE  . ARG A 1 233 ? 45.438 49.239  57.763 1.00 46.03  ?  190 ARG A NE  1 
ATOM   1498 C CZ  . ARG A 1 233 ? 46.175 50.191  57.185 1.00 51.84  ?  190 ARG A CZ  1 
ATOM   1499 N NH1 . ARG A 1 233 ? 47.325 50.579  57.725 1.00 44.72  ?  190 ARG A NH1 1 
ATOM   1500 N NH2 . ARG A 1 233 ? 45.768 50.748  56.048 1.00 46.25  ?  190 ARG A NH2 1 
ATOM   1501 N N   . LEU A 1 234 ? 47.798 43.492  57.563 1.00 32.56  ?  191 LEU A N   1 
ATOM   1502 C CA  . LEU A 1 234 ? 48.628 42.666  56.689 1.00 35.68  ?  191 LEU A CA  1 
ATOM   1503 C C   . LEU A 1 234 ? 47.904 41.381  56.300 1.00 37.82  ?  191 LEU A C   1 
ATOM   1504 O O   . LEU A 1 234 ? 47.897 40.987  55.124 1.00 32.07  ?  191 LEU A O   1 
ATOM   1505 C CB  . LEU A 1 234 ? 49.958 42.353  57.377 1.00 34.13  ?  191 LEU A CB  1 
ATOM   1506 C CG  . LEU A 1 234 ? 50.822 43.555  57.754 1.00 34.92  ?  191 LEU A CG  1 
ATOM   1507 C CD1 . LEU A 1 234 ? 52.063 43.101  58.546 1.00 32.43  ?  191 LEU A CD1 1 
ATOM   1508 C CD2 . LEU A 1 234 ? 51.232 44.354  56.503 1.00 32.25  ?  191 LEU A CD2 1 
ATOM   1509 N N   . LYS A 1 235 ? 47.271 40.711  57.274 1.00 31.46  ?  192 LYS A N   1 
ATOM   1510 C CA  . LYS A 1 235 ? 46.616 39.446  56.954 1.00 35.02  ?  192 LYS A CA  1 
ATOM   1511 C C   . LYS A 1 235 ? 45.436 39.673  56.017 1.00 33.22  ?  192 LYS A C   1 
ATOM   1512 O O   . LYS A 1 235 ? 45.178 38.863  55.115 1.00 35.12  ?  192 LYS A O   1 
ATOM   1513 C CB  . LYS A 1 235 ? 46.163 38.720  58.235 1.00 33.40  ?  192 LYS A CB  1 
ATOM   1514 C CG  . LYS A 1 235 ? 45.507 37.368  57.923 1.00 34.45  ?  192 LYS A CG  1 
ATOM   1515 C CD  . LYS A 1 235 ? 44.980 36.646  59.157 1.00 42.62  ?  192 LYS A CD  1 
ATOM   1516 C CE  . LYS A 1 235 ? 44.365 35.307  58.748 1.00 41.03  ?  192 LYS A CE  1 
ATOM   1517 N NZ  . LYS A 1 235 ? 43.004 35.518  58.165 1.00 40.99  ?  192 LYS A NZ  1 
ATOM   1518 N N   . SER A 1 236 ? 44.739 40.794  56.180 1.00 31.25  ?  193 SER A N   1 
ATOM   1519 C CA  . SER A 1 236 ? 43.612 41.086  55.305 1.00 33.56  ?  193 SER A CA  1 
ATOM   1520 C C   . SER A 1 236 ? 44.062 41.208  53.852 1.00 36.10  ?  193 SER A C   1 
ATOM   1521 O O   . SER A 1 236 ? 43.430 40.652  52.949 1.00 32.69  ?  193 SER A O   1 
ATOM   1522 C CB  . SER A 1 236 ? 42.919 42.366  55.765 1.00 35.53  ?  193 SER A CB  1 
ATOM   1523 O OG  . SER A 1 236 ? 41.903 42.709  54.852 1.00 45.94  ?  193 SER A OG  1 
ATOM   1524 N N   . GLU A 1 237 ? 45.156 41.936  53.610 1.00 33.25  ?  194 GLU A N   1 
ATOM   1525 C CA  . GLU A 1 237 ? 45.660 42.083  52.245 1.00 32.51  ?  194 GLU A CA  1 
ATOM   1526 C C   . GLU A 1 237 ? 46.168 40.759  51.695 1.00 34.95  ?  194 GLU A C   1 
ATOM   1527 O O   . GLU A 1 237 ? 45.948 40.446  50.521 1.00 31.46  ?  194 GLU A O   1 
ATOM   1528 C CB  . GLU A 1 237 ? 46.771 43.132  52.191 1.00 31.04  ?  194 GLU A CB  1 
ATOM   1529 C CG  . GLU A 1 237 ? 46.287 44.555  52.347 1.00 34.04  ?  194 GLU A CG  1 
ATOM   1530 C CD  . GLU A 1 237 ? 45.321 44.942  51.244 1.00 43.36  ?  194 GLU A CD  1 
ATOM   1531 O OE1 . GLU A 1 237 ? 45.641 44.685  50.063 1.00 36.21  ?  194 GLU A OE1 1 
ATOM   1532 O OE2 . GLU A 1 237 ? 44.242 45.488  51.557 1.00 42.88  ?  194 GLU A OE2 1 
ATOM   1533 N N   . ILE A 1 238 ? 46.861 39.974  52.523 1.00 32.75  ?  195 ILE A N   1 
ATOM   1534 C CA  . ILE A 1 238 ? 47.407 38.700  52.069 1.00 33.24  ?  195 ILE A CA  1 
ATOM   1535 C C   . ILE A 1 238 ? 46.288 37.717  51.766 1.00 36.16  ?  195 ILE A C   1 
ATOM   1536 O O   . ILE A 1 238 ? 46.342 36.978  50.770 1.00 32.48  ?  195 ILE A O   1 
ATOM   1537 C CB  . ILE A 1 238 ? 48.388 38.144  53.119 1.00 32.06  ?  195 ILE A CB  1 
ATOM   1538 C CG1 . ILE A 1 238 ? 49.651 39.005  53.168 1.00 35.83  ?  195 ILE A CG1 1 
ATOM   1539 C CG2 . ILE A 1 238 ? 48.725 36.680  52.850 1.00 29.56  ?  195 ILE A CG2 1 
ATOM   1540 C CD1 . ILE A 1 238 ? 50.551 38.654  54.360 1.00 36.53  ?  195 ILE A CD1 1 
ATOM   1541 N N   . ASP A 1 239 ? 45.237 37.715  52.595 1.00 31.46  ?  196 ASP A N   1 
ATOM   1542 C CA  . ASP A 1 239 ? 44.090 36.861  52.315 1.00 33.15  ?  196 ASP A CA  1 
ATOM   1543 C C   . ASP A 1 239 ? 43.479 37.193  50.957 1.00 31.75  ?  196 ASP A C   1 
ATOM   1544 O O   . ASP A 1 239 ? 43.058 36.289  50.227 1.00 34.52  ?  196 ASP A O   1 
ATOM   1545 C CB  . ASP A 1 239 ? 43.032 36.995  53.415 1.00 34.07  ?  196 ASP A CB  1 
ATOM   1546 C CG  . ASP A 1 239 ? 43.436 36.299  54.714 1.00 38.37  ?  196 ASP A CG  1 
ATOM   1547 O OD1 . ASP A 1 239 ? 44.348 35.447  54.695 1.00 33.76  ?  196 ASP A OD1 1 
ATOM   1548 O OD2 . ASP A 1 239 ? 42.823 36.604  55.763 1.00 36.92  ?  196 ASP A OD2 1 
ATOM   1549 N N   . LYS A 1 240 ? 43.394 38.484  50.620 1.00 32.79  ?  197 LYS A N   1 
ATOM   1550 C CA  . LYS A 1 240 ? 42.876 38.887  49.308 1.00 34.41  ?  197 LYS A CA  1 
ATOM   1551 C C   . LYS A 1 240 ? 43.766 38.365  48.187 1.00 33.59  ?  197 LYS A C   1 
ATOM   1552 O O   . LYS A 1 240 ? 43.276 37.811  47.190 1.00 35.13  ?  197 LYS A O   1 
ATOM   1553 C CB  . LYS A 1 240 ? 42.762 40.412  49.222 1.00 30.97  ?  197 LYS A CB  1 
ATOM   1554 C CG  . LYS A 1 240 ? 41.643 41.042  50.043 1.00 35.13  ?  197 LYS A CG  1 
ATOM   1555 C CD  . LYS A 1 240 ? 41.660 42.560  49.859 1.00 36.57  ?  197 LYS A CD  1 
ATOM   1556 C CE  . LYS A 1 240 ? 40.883 43.278  50.948 1.00 49.81  ?  197 LYS A CE  1 
ATOM   1557 N NZ  . LYS A 1 240 ? 39.503 42.740  51.050 1.00 53.26  ?  197 LYS A NZ  1 
ATOM   1558 N N   . ILE A 1 241 ? 45.084 38.542  48.333 1.00 31.92  ?  198 ILE A N   1 
ATOM   1559 C CA  . ILE A 1 241 ? 46.027 38.014  47.347 1.00 33.47  ?  198 ILE A CA  1 
ATOM   1560 C C   . ILE A 1 241 ? 45.826 36.519  47.146 1.00 39.08  ?  198 ILE A C   1 
ATOM   1561 O O   . ILE A 1 241 ? 45.791 36.030  46.011 1.00 33.34  ?  198 ILE A O   1 
ATOM   1562 C CB  . ILE A 1 241 ? 47.470 38.341  47.771 1.00 33.21  ?  198 ILE A CB  1 
ATOM   1563 C CG1 . ILE A 1 241 ? 47.693 39.845  47.674 1.00 32.97  ?  198 ILE A CG1 1 
ATOM   1564 C CG2 . ILE A 1 241 ? 48.471 37.519  46.932 1.00 33.53  ?  198 ILE A CG2 1 
ATOM   1565 C CD1 . ILE A 1 241 ? 48.909 40.374  48.447 1.00 35.69  ?  198 ILE A CD1 1 
ATOM   1566 N N   . PHE A 1 242 ? 45.680 35.764  48.241 1.00 29.92  ?  199 PHE A N   1 
ATOM   1567 C CA  . PHE A 1 242 ? 45.574 34.309  48.140 1.00 28.98  ?  199 PHE A CA  1 
ATOM   1568 C C   . PHE A 1 242 ? 44.362 33.839  47.335 1.00 33.01  ?  199 PHE A C   1 
ATOM   1569 O O   . PHE A 1 242 ? 44.385 32.716  46.821 1.00 40.54  ?  199 PHE A O   1 
ATOM   1570 C CB  . PHE A 1 242 ? 45.509 33.677  49.554 1.00 29.09  ?  199 PHE A CB  1 
ATOM   1571 C CG  . PHE A 1 242 ? 46.846 33.575  50.245 1.00 33.67  ?  199 PHE A CG  1 
ATOM   1572 C CD1 . PHE A 1 242 ? 48.021 33.784  49.552 1.00 34.40  ?  199 PHE A CD1 1 
ATOM   1573 C CD2 . PHE A 1 242 ? 46.926 33.243  51.600 1.00 32.41  ?  199 PHE A CD2 1 
ATOM   1574 C CE1 . PHE A 1 242 ? 49.246 33.677  50.165 1.00 37.44  ?  199 PHE A CE1 1 
ATOM   1575 C CE2 . PHE A 1 242 ? 48.149 33.140  52.215 1.00 35.25  ?  199 PHE A CE2 1 
ATOM   1576 C CZ  . PHE A 1 242 ? 49.315 33.359  51.507 1.00 33.75  ?  199 PHE A CZ  1 
ATOM   1577 N N   . VAL A 1 243 ? 43.288 34.625  47.251 1.00 34.95  ?  200 VAL A N   1 
ATOM   1578 C CA  . VAL A 1 243 ? 42.096 34.203  46.514 1.00 36.73  ?  200 VAL A CA  1 
ATOM   1579 C C   . VAL A 1 243 ? 41.921 34.951  45.202 1.00 39.83  ?  200 VAL A C   1 
ATOM   1580 O O   . VAL A 1 243 ? 40.976 34.646  44.453 1.00 37.28  ?  200 VAL A O   1 
ATOM   1581 C CB  . VAL A 1 243 ? 40.818 34.330  47.368 1.00 38.46  ?  200 VAL A CB  1 
ATOM   1582 C CG1 . VAL A 1 243 ? 40.973 33.547  48.676 1.00 35.14  ?  200 VAL A CG1 1 
ATOM   1583 C CG2 . VAL A 1 243 ? 40.458 35.797  47.628 1.00 35.12  ?  200 VAL A CG2 1 
ATOM   1584 N N   . ASN A 1 244 ? 42.799 35.903  44.887 1.00 36.35  ?  201 ASN A N   1 
ATOM   1585 C CA  . ASN A 1 244 ? 42.669 36.698  43.668 1.00 36.71  ?  201 ASN A CA  1 
ATOM   1586 C C   . ASN A 1 244 ? 43.401 36.058  42.499 1.00 39.27  ?  201 ASN A C   1 
ATOM   1587 O O   . ASN A 1 244 ? 44.271 35.195  42.676 1.00 34.84  ?  201 ASN A O   1 
ATOM   1588 C CB  . ASN A 1 244 ? 43.217 38.106  43.890 1.00 39.08  ?  201 ASN A CB  1 
ATOM   1589 C CG  . ASN A 1 244 ? 42.219 39.029  44.559 1.00 46.11  ?  201 ASN A CG  1 
ATOM   1590 O OD1 . ASN A 1 244 ? 41.047 38.690  44.716 1.00 47.98  ?  201 ASN A OD1 1 
ATOM   1591 N ND2 . ASN A 1 244 ? 42.680 40.216  44.944 1.00 43.00  ?  201 ASN A ND2 1 
ATOM   1592 N N   . PRO A 1 245 ? 43.077 36.483  41.274 1.00 39.30  ?  202 PRO A N   1 
ATOM   1593 C CA  . PRO A 1 245 ? 43.790 35.981  40.093 1.00 41.50  ?  202 PRO A CA  1 
ATOM   1594 C C   . PRO A 1 245 ? 45.263 36.369  40.111 1.00 46.93  ?  202 PRO A C   1 
ATOM   1595 O O   . PRO A 1 245 ? 45.720 37.190  40.911 1.00 42.80  ?  202 PRO A O   1 
ATOM   1596 C CB  . PRO A 1 245 ? 43.068 36.645  38.908 1.00 41.69  ?  202 PRO A CB  1 
ATOM   1597 C CG  . PRO A 1 245 ? 41.822 37.249  39.448 1.00 40.43  ?  202 PRO A CG  1 
ATOM   1598 C CD  . PRO A 1 245 ? 42.006 37.436  40.942 1.00 35.56  ?  202 PRO A CD  1 
ATOM   1599 N N   . SER A 1 246 ? 46.010 35.757  39.185 1.00 40.62  ?  203 SER A N   1 
ATOM   1600 C CA  . SER A 1 246 ? 47.438 36.032  38.993 1.00 46.20  ?  203 SER A CA  1 
ATOM   1601 C C   . SER A 1 246 ? 48.191 36.052  40.317 1.00 41.51  ?  203 SER A C   1 
ATOM   1602 O O   . SER A 1 246 ? 49.051 36.902  40.557 1.00 38.92  ?  203 SER A O   1 
ATOM   1603 C CB  . SER A 1 246 ? 47.656 37.358  38.258 1.00 45.12  ?  203 SER A CB  1 
ATOM   1604 O OG  . SER A 1 246 ? 46.957 37.401  37.028 1.00 46.54  ?  203 SER A OG  1 
ATOM   1605 N N   . MET A 1 247 ? 47.867 35.121  41.207 1.00 44.88  ?  204 MET A N   1 
ATOM   1606 C CA  . MET A 1 247 ? 48.492 35.216  42.517 1.00 38.20  ?  204 MET A CA  1 
ATOM   1607 C C   . MET A 1 247 ? 49.980 34.889  42.437 1.00 43.48  ?  204 MET A C   1 
ATOM   1608 O O   . MET A 1 247 ? 50.772 35.433  43.216 1.00 41.58  ?  204 MET A O   1 
ATOM   1609 C CB  . MET A 1 247 ? 47.755 34.324  43.523 1.00 41.86  ?  204 MET A CB  1 
ATOM   1610 C CG  . MET A 1 247 ? 48.039 32.858  43.376 1.00 38.51  ?  204 MET A CG  1 
ATOM   1611 S SD  . MET A 1 247 ? 49.504 32.404  44.317 1.00 42.32  ?  204 MET A SD  1 
ATOM   1612 C CE  . MET A 1 247 ? 49.112 33.062  45.967 1.00 34.98  ?  204 MET A CE  1 
ATOM   1613 N N   . GLN A 1 248 ? 50.390 34.042  41.484 1.00 42.17  ?  205 GLN A N   1 
ATOM   1614 C CA  . GLN A 1 248 ? 51.815 33.739  41.349 1.00 43.90  ?  205 GLN A CA  1 
ATOM   1615 C C   . GLN A 1 248 ? 52.621 34.988  41.009 1.00 43.06  ?  205 GLN A C   1 
ATOM   1616 O O   . GLN A 1 248 ? 53.739 35.167  41.508 1.00 40.02  ?  205 GLN A O   1 
ATOM   1617 C CB  . GLN A 1 248 ? 52.049 32.660  40.294 1.00 43.46  ?  205 GLN A CB  1 
ATOM   1618 C CG  . GLN A 1 248 ? 51.513 31.287  40.655 1.00 40.85  ?  205 GLN A CG  1 
ATOM   1619 C CD  . GLN A 1 248 ? 50.009 31.182  40.464 1.00 46.31  ?  205 GLN A CD  1 
ATOM   1620 O OE1 . GLN A 1 248 ? 49.378 32.069  39.876 1.00 45.56  ?  205 GLN A OE1 1 
ATOM   1621 N NE2 . GLN A 1 248 ? 49.425 30.097  40.962 1.00 49.51  ?  205 GLN A NE2 1 
ATOM   1622 N N   . LYS A 1 249 ? 52.077 35.857  40.149 1.00 42.77  ?  206 LYS A N   1 
ATOM   1623 C CA  . LYS A 1 249 ? 52.699 37.159  39.913 1.00 42.40  ?  206 LYS A CA  1 
ATOM   1624 C C   . LYS A 1 249 ? 52.702 38.023  41.175 1.00 41.24  ?  206 LYS A C   1 
ATOM   1625 O O   . LYS A 1 249 ? 53.680 38.730  41.445 1.00 35.44  ?  206 LYS A O   1 
ATOM   1626 C CB  . LYS A 1 249 ? 51.985 37.883  38.772 1.00 44.73  ?  206 LYS A CB  1 
ATOM   1627 C CG  . LYS A 1 249 ? 52.221 37.198  37.420 1.00 47.39  ?  206 LYS A CG  1 
ATOM   1628 C CD  . LYS A 1 249 ? 51.328 37.733  36.289 1.00 62.65  ?  206 LYS A CD  1 
ATOM   1629 C CE  . LYS A 1 249 ? 51.560 36.939  35.000 1.00 65.04  ?  206 LYS A CE  1 
ATOM   1630 N NZ  . LYS A 1 249 ? 50.740 37.420  33.845 1.00 57.12  ?  206 LYS A NZ  1 
ATOM   1631 N N   . SER A 1 250 ? 51.601 38.025  41.930 1.00 37.97  ?  207 SER A N   1 
ATOM   1632 C CA  . SER A 1 250 ? 51.574 38.780  43.184 1.00 38.25  ?  207 SER A CA  1 
ATOM   1633 C C   . SER A 1 250 ? 52.680 38.334  44.131 1.00 35.26  ?  207 SER A C   1 
ATOM   1634 O O   . SER A 1 250 ? 53.326 39.166  44.783 1.00 33.69  ?  207 SER A O   1 
ATOM   1635 C CB  . SER A 1 250 ? 50.215 38.622  43.865 1.00 43.02  ?  207 SER A CB  1 
ATOM   1636 O OG  . SER A 1 250 ? 49.168 39.029  43.009 1.00 41.52  ?  207 SER A OG  1 
ATOM   1637 N N   . MET A 1 251 ? 52.892 37.023  44.250 1.00 36.26  ?  208 MET A N   1 
ATOM   1638 C CA  . MET A 1 251 ? 53.877 36.544  45.214 1.00 36.48  ?  208 MET A CA  1 
ATOM   1639 C C   . MET A 1 251 ? 55.289 36.829  44.724 1.00 41.46  ?  208 MET A C   1 
ATOM   1640 O O   . MET A 1 251 ? 56.200 37.025  45.533 1.00 34.29  ?  208 MET A O   1 
ATOM   1641 C CB  . MET A 1 251 ? 53.670 35.053  45.480 1.00 35.55  ?  208 MET A CB  1 
ATOM   1642 C CG  . MET A 1 251 ? 52.243 34.704  45.933 1.00 38.95  ?  208 MET A CG  1 
ATOM   1643 S SD  . MET A 1 251 ? 51.800 35.590  47.468 1.00 40.26  ?  208 MET A SD  1 
ATOM   1644 C CE  . MET A 1 251 ? 53.235 35.131  48.408 1.00 36.85  ?  208 MET A CE  1 
ATOM   1645 N N   . ALA A 1 252 ? 55.479 36.884  43.400 1.00 36.86  ?  209 ALA A N   1 
ATOM   1646 C CA  . ALA A 1 252 ? 56.753 37.336  42.858 1.00 35.33  ?  209 ALA A CA  1 
ATOM   1647 C C   . ALA A 1 252 ? 57.002 38.803  43.191 1.00 32.93  ?  209 ALA A C   1 
ATOM   1648 O O   . ALA A 1 252 ? 58.131 39.183  43.522 1.00 36.85  ?  209 ALA A O   1 
ATOM   1649 C CB  . ALA A 1 252 ? 56.794 37.106  41.337 1.00 37.61  ?  209 ALA A CB  1 
ATOM   1650 N N   . TYR A 1 253 ? 55.969 39.650  43.095 1.00 28.64  ?  210 TYR A N   1 
ATOM   1651 C CA  . TYR A 1 253 ? 56.136 41.041  43.496 1.00 28.96  ?  210 TYR A CA  1 
ATOM   1652 C C   . TYR A 1 253 ? 56.386 41.143  44.994 1.00 34.92  ?  210 TYR A C   1 
ATOM   1653 O O   . TYR A 1 253 ? 57.122 42.025  45.451 1.00 34.17  ?  210 TYR A O   1 
ATOM   1654 C CB  . TYR A 1 253 ? 54.893 41.859  43.143 1.00 31.92  ?  210 TYR A CB  1 
ATOM   1655 C CG  . TYR A 1 253 ? 54.841 42.483  41.756 1.00 36.48  ?  210 TYR A CG  1 
ATOM   1656 C CD1 . TYR A 1 253 ? 55.954 43.103  41.194 1.00 35.41  ?  210 TYR A CD1 1 
ATOM   1657 C CD2 . TYR A 1 253 ? 53.648 42.495  41.040 1.00 35.73  ?  210 TYR A CD2 1 
ATOM   1658 C CE1 . TYR A 1 253 ? 55.877 43.700  39.906 1.00 38.16  ?  210 TYR A CE1 1 
ATOM   1659 C CE2 . TYR A 1 253 ? 53.562 43.071  39.777 1.00 38.72  ?  210 TYR A CE2 1 
ATOM   1660 C CZ  . TYR A 1 253 ? 54.672 43.676  39.220 1.00 36.83  ?  210 TYR A CZ  1 
ATOM   1661 O OH  . TYR A 1 253 ? 54.552 44.250  37.970 1.00 43.23  ?  210 TYR A OH  1 
ATOM   1662 N N   . LEU A 1 254 ? 55.775 40.252  45.766 1.00 33.11  ?  211 LEU A N   1 
ATOM   1663 C CA  . LEU A 1 254 ? 56.001 40.267  47.212 1.00 33.43  ?  211 LEU A CA  1 
ATOM   1664 C C   . LEU A 1 254 ? 57.484 40.098  47.529 1.00 33.73  ?  211 LEU A C   1 
ATOM   1665 O O   . LEU A 1 254 ? 58.028 40.783  48.405 1.00 36.17  ?  211 LEU A O   1 
ATOM   1666 C CB  . LEU A 1 254 ? 55.170 39.167  47.872 1.00 31.37  ?  211 LEU A CB  1 
ATOM   1667 C CG  . LEU A 1 254 ? 54.925 39.375  49.375 1.00 33.44  ?  211 LEU A CG  1 
ATOM   1668 C CD1 . LEU A 1 254 ? 53.994 40.583  49.552 1.00 31.93  ?  211 LEU A CD1 1 
ATOM   1669 C CD2 . LEU A 1 254 ? 54.336 38.124  49.978 1.00 32.43  ?  211 LEU A CD2 1 
ATOM   1670 N N   . LYS A 1 255 ? 58.149 39.181  46.821 1.00 36.37  ?  212 LYS A N   1 
ATOM   1671 C CA  . LYS A 1 255 ? 59.587 38.972  46.972 1.00 39.98  ?  212 LYS A CA  1 
ATOM   1672 C C   . LYS A 1 255 ? 60.387 40.105  46.334 1.00 40.38  ?  212 LYS A C   1 
ATOM   1673 O O   . LYS A 1 255 ? 61.283 40.680  46.967 1.00 37.13  ?  212 LYS A O   1 
ATOM   1674 C CB  . LYS A 1 255 ? 59.963 37.623  46.352 1.00 40.44  ?  212 LYS A CB  1 
ATOM   1675 C CG  . LYS A 1 255 ? 61.446 37.251  46.374 1.00 40.20  ?  212 LYS A CG  1 
ATOM   1676 C CD  . LYS A 1 255 ? 61.607 35.824  45.852 1.00 40.03  ?  212 LYS A CD  1 
ATOM   1677 C CE  . LYS A 1 255 ? 63.002 35.251  46.098 1.00 49.48  ?  212 LYS A CE  1 
ATOM   1678 N NZ  . LYS A 1 255 ? 64.074 35.932  45.311 1.00 60.04  ?  212 LYS A NZ  1 
ATOM   1679 N N   . ASP A 1 256 ? 60.070 40.443  45.074 1.00 37.99  ?  213 ASP A N   1 
ATOM   1680 C CA  . ASP A 1 256 ? 60.845 41.446  44.346 1.00 38.88  ?  213 ASP A CA  1 
ATOM   1681 C C   . ASP A 1 256 ? 60.754 42.816  44.993 1.00 36.36  ?  213 ASP A C   1 
ATOM   1682 O O   . ASP A 1 256 ? 61.660 43.638  44.829 1.00 38.02  ?  213 ASP A O   1 
ATOM   1683 C CB  . ASP A 1 256 ? 60.364 41.564  42.883 1.00 36.10  ?  213 ASP A CB  1 
ATOM   1684 C CG  . ASP A 1 256 ? 60.459 40.273  42.110 1.00 49.66  ?  213 ASP A CG  1 
ATOM   1685 O OD1 . ASP A 1 256 ? 61.099 39.313  42.588 1.00 47.41  ?  213 ASP A OD1 1 
ATOM   1686 O OD2 . ASP A 1 256 ? 59.886 40.237  40.985 1.00 60.00  ?  213 ASP A OD2 1 
ATOM   1687 N N   . SER A 1 257 ? 59.654 43.108  45.683 1.00 31.60  ?  214 SER A N   1 
ATOM   1688 C CA  . SER A 1 257 ? 59.479 44.401  46.327 1.00 30.94  ?  214 SER A CA  1 
ATOM   1689 C C   . SER A 1 257 ? 60.248 44.537  47.643 1.00 30.92  ?  214 SER A C   1 
ATOM   1690 O O   . SER A 1 257 ? 60.236 45.632  48.217 1.00 29.28  ?  214 SER A O   1 
ATOM   1691 C CB  . SER A 1 257 ? 57.994 44.642  46.613 1.00 36.33  ?  214 SER A CB  1 
ATOM   1692 O OG  . SER A 1 257 ? 57.559 43.719  47.611 1.00 32.16  ?  214 SER A OG  1 
ATOM   1693 N N   . VAL A 1 258 ? 60.860 43.458  48.120 1.00 32.87  ?  215 VAL A N   1 
ATOM   1694 C CA  . VAL A 1 258 ? 61.570 43.365  49.400 1.00 35.94  ?  215 VAL A CA  1 
ATOM   1695 C C   . VAL A 1 258 ? 60.594 43.291  50.581 1.00 36.99  ?  215 VAL A C   1 
ATOM   1696 O O   . VAL A 1 258 ? 61.028 43.272  51.738 1.00 35.36  ?  215 VAL A O   1 
ATOM   1697 C CB  . VAL A 1 258 ? 62.570 44.543  49.556 1.00 33.87  ?  215 VAL A CB  1 
ATOM   1698 C CG1 . VAL A 1 258 ? 63.434 44.384  50.804 1.00 36.43  ?  215 VAL A CG1 1 
ATOM   1699 C CG2 . VAL A 1 258 ? 63.500 44.618  48.316 1.00 34.83  ?  215 VAL A CG2 1 
ATOM   1700 N N   . LEU A 1 259 ? 59.292 43.116  50.308 1.00 34.73  ?  216 LEU A N   1 
ATOM   1701 C CA  . LEU A 1 259 ? 58.362 43.011  51.438 1.00 35.92  ?  216 LEU A CA  1 
ATOM   1702 C C   . LEU A 1 259 ? 58.545 41.664  52.150 1.00 33.38  ?  216 LEU A C   1 
ATOM   1703 O O   . LEU A 1 259 ? 58.366 41.605  53.378 1.00 34.22  ?  216 LEU A O   1 
ATOM   1704 C CB  . LEU A 1 259 ? 56.901 43.188  50.986 1.00 31.44  ?  216 LEU A CB  1 
ATOM   1705 C CG  . LEU A 1 259 ? 56.531 44.655  50.705 1.00 32.71  ?  216 LEU A CG  1 
ATOM   1706 C CD1 . LEU A 1 259 ? 55.155 44.769  50.020 1.00 35.57  ?  216 LEU A CD1 1 
ATOM   1707 C CD2 . LEU A 1 259 ? 56.579 45.506  51.976 1.00 32.82  ?  216 LEU A CD2 1 
ATOM   1708 N N   . THR A 1 260 ? 58.894 40.584  51.440 1.00 31.88  ?  217 THR A N   1 
ATOM   1709 C CA  . THR A 1 260 ? 59.133 39.311  52.136 1.00 35.38  ?  217 THR A CA  1 
ATOM   1710 C C   . THR A 1 260 ? 60.343 39.365  53.078 1.00 39.20  ?  217 THR A C   1 
ATOM   1711 O O   . THR A 1 260 ? 60.451 38.523  53.983 1.00 35.79  ?  217 THR A O   1 
ATOM   1712 C CB  . THR A 1 260 ? 59.320 38.148  51.154 1.00 34.56  ?  217 THR A CB  1 
ATOM   1713 O OG1 . THR A 1 260 ? 60.447 38.407  50.298 1.00 36.13  ?  217 THR A OG1 1 
ATOM   1714 C CG2 . THR A 1 260 ? 58.052 37.946  50.304 1.00 35.38  ?  217 THR A CG2 1 
ATOM   1715 N N   . ARG A 1 261 ? 61.245 40.336  52.900 1.00 36.32  ?  218 ARG A N   1 
ATOM   1716 C CA  . ARG A 1 261 ? 62.355 40.487  53.842 1.00 32.99  ?  218 ARG A CA  1 
ATOM   1717 C C   . ARG A 1 261 ? 61.872 40.926  55.216 1.00 38.12  ?  218 ARG A C   1 
ATOM   1718 O O   . ARG A 1 261 ? 62.497 40.574  56.221 1.00 38.25  ?  218 ARG A O   1 
ATOM   1719 C CB  . ARG A 1 261 ? 63.387 41.499  53.325 1.00 36.57  ?  218 ARG A CB  1 
ATOM   1720 C CG  . ARG A 1 261 ? 64.607 41.692  54.239 1.00 39.61  ?  218 ARG A CG  1 
ATOM   1721 C CD  . ARG A 1 261 ? 65.767 42.373  53.501 1.00 38.05  ?  218 ARG A CD  1 
ATOM   1722 N NE  . ARG A 1 261 ? 66.271 41.552  52.398 1.00 36.33  ?  218 ARG A NE  1 
ATOM   1723 C CZ  . ARG A 1 261 ? 67.185 40.596  52.535 1.00 41.62  ?  218 ARG A CZ  1 
ATOM   1724 N NH1 . ARG A 1 261 ? 67.712 40.333  53.732 1.00 43.67  ?  218 ARG A NH1 1 
ATOM   1725 N NH2 . ARG A 1 261 ? 67.576 39.900  51.487 1.00 37.61  ?  218 ARG A NH2 1 
ATOM   1726 N N   . PHE A 1 262 ? 60.774 41.690  55.278 1.00 33.27  ?  219 PHE A N   1 
ATOM   1727 C CA  . PHE A 1 262 ? 60.386 42.418  56.482 1.00 33.87  ?  219 PHE A CA  1 
ATOM   1728 C C   . PHE A 1 262 ? 58.997 42.085  57.013 1.00 37.63  ?  219 PHE A C   1 
ATOM   1729 O O   . PHE A 1 262 ? 58.744 42.317  58.206 1.00 35.10  ?  219 PHE A O   1 
ATOM   1730 C CB  . PHE A 1 262 ? 60.469 43.932  56.238 1.00 33.26  ?  219 PHE A CB  1 
ATOM   1731 C CG  . PHE A 1 262 ? 61.853 44.413  55.886 1.00 42.09  ?  219 PHE A CG  1 
ATOM   1732 C CD1 . PHE A 1 262 ? 62.870 44.413  56.842 1.00 37.41  ?  219 PHE A CD1 1 
ATOM   1733 C CD2 . PHE A 1 262 ? 62.142 44.864  54.593 1.00 36.43  ?  219 PHE A CD2 1 
ATOM   1734 C CE1 . PHE A 1 262 ? 64.149 44.858  56.524 1.00 39.09  ?  219 PHE A CE1 1 
ATOM   1735 C CE2 . PHE A 1 262 ? 63.412 45.322  54.261 1.00 38.74  ?  219 PHE A CE2 1 
ATOM   1736 C CZ  . PHE A 1 262 ? 64.425 45.321  55.227 1.00 40.79  ?  219 PHE A CZ  1 
ATOM   1737 N N   . LEU A 1 263 ? 58.108 41.525  56.196 1.00 34.45  ?  220 LEU A N   1 
ATOM   1738 C CA  . LEU A 1 263 ? 56.839 41.033  56.713 1.00 33.04  ?  220 LEU A CA  1 
ATOM   1739 C C   . LEU A 1 263 ? 57.085 40.037  57.845 1.00 32.75  ?  220 LEU A C   1 
ATOM   1740 O O   . LEU A 1 263 ? 58.109 39.352  57.868 1.00 31.18  ?  220 LEU A O   1 
ATOM   1741 C CB  . LEU A 1 263 ? 56.032 40.344  55.606 1.00 31.90  ?  220 LEU A CB  1 
ATOM   1742 C CG  . LEU A 1 263 ? 55.355 41.293  54.615 1.00 32.15  ?  220 LEU A CG  1 
ATOM   1743 C CD1 . LEU A 1 263 ? 54.910 40.513  53.389 1.00 30.24  ?  220 LEU A CD1 1 
ATOM   1744 C CD2 . LEU A 1 263 ? 54.180 42.037  55.244 1.00 30.08  ?  220 LEU A CD2 1 
ATOM   1745 N N   . PRO A 1 264 ? 56.143 39.904  58.774 1.00 35.41  ?  221 PRO A N   1 
ATOM   1746 C CA  . PRO A 1 264 ? 56.255 38.834  59.779 1.00 38.00  ?  221 PRO A CA  1 
ATOM   1747 C C   . PRO A 1 264 ? 56.462 37.496  59.083 1.00 39.67  ?  221 PRO A C   1 
ATOM   1748 O O   . PRO A 1 264 ? 55.766 37.166  58.115 1.00 32.91  ?  221 PRO A O   1 
ATOM   1749 C CB  . PRO A 1 264 ? 54.915 38.903  60.530 1.00 33.61  ?  221 PRO A CB  1 
ATOM   1750 C CG  . PRO A 1 264 ? 54.461 40.343  60.358 1.00 35.10  ?  221 PRO A CG  1 
ATOM   1751 C CD  . PRO A 1 264 ? 54.911 40.691  58.930 1.00 32.03  ?  221 PRO A CD  1 
ATOM   1752 N N   . VAL A 1 265 ? 57.461 36.744  59.565 1.00 31.01  ?  222 VAL A N   1 
ATOM   1753 C CA  . VAL A 1 265 ? 57.983 35.527  58.946 1.00 32.67  ?  222 VAL A CA  1 
ATOM   1754 C C   . VAL A 1 265 ? 57.912 35.606  57.417 1.00 32.57  ?  222 VAL A C   1 
ATOM   1755 O O   . VAL A 1 265 ? 57.563 34.626  56.754 1.00 31.73  ?  222 VAL A O   1 
ATOM   1756 C CB  . VAL A 1 265 ? 57.280 34.256  59.469 1.00 34.81  ?  222 VAL A CB  1 
ATOM   1757 C CG1 . VAL A 1 265 ? 57.655 34.018  60.958 1.00 34.52  ?  222 VAL A CG1 1 
ATOM   1758 C CG2 . VAL A 1 265 ? 55.752 34.317  59.298 1.00 36.19  ?  222 VAL A CG2 1 
ATOM   1759 N N   . GLY A 1 266 ? 58.302 36.753  56.856 1.00 34.17  ?  223 GLY A N   1 
ATOM   1760 C CA  . GLY A 1 266 ? 58.058 37.000  55.433 1.00 31.81  ?  223 GLY A CA  1 
ATOM   1761 C C   . GLY A 1 266 ? 58.740 36.022  54.497 1.00 34.18  ?  223 GLY A C   1 
ATOM   1762 O O   . GLY A 1 266 ? 58.268 35.792  53.373 1.00 34.35  ?  223 GLY A O   1 
ATOM   1763 N N   . GLY A 1 267 ? 59.866 35.451  54.916 1.00 36.28  ?  224 GLY A N   1 
ATOM   1764 C CA  . GLY A 1 267 ? 60.560 34.512  54.048 1.00 33.99  ?  224 GLY A CA  1 
ATOM   1765 C C   . GLY A 1 267 ? 59.740 33.286  53.711 1.00 39.47  ?  224 GLY A C   1 
ATOM   1766 O O   . GLY A 1 267 ? 59.946 32.665  52.661 1.00 36.54  ?  224 GLY A O   1 
ATOM   1767 N N   . LEU A 1 268 ? 58.795 32.922  54.587 1.00 33.24  ?  225 LEU A N   1 
ATOM   1768 C CA  . LEU A 1 268 ? 57.946 31.760  54.361 1.00 34.56  ?  225 LEU A CA  1 
ATOM   1769 C C   . LEU A 1 268 ? 57.032 31.911  53.152 1.00 37.13  ?  225 LEU A C   1 
ATOM   1770 O O   . LEU A 1 268 ? 56.514 30.900  52.669 1.00 38.58  ?  225 LEU A O   1 
ATOM   1771 C CB  . LEU A 1 268 ? 57.087 31.475  55.588 1.00 35.39  ?  225 LEU A CB  1 
ATOM   1772 C CG  . LEU A 1 268 ? 57.880 31.272  56.876 1.00 38.54  ?  225 LEU A CG  1 
ATOM   1773 C CD1 . LEU A 1 268 ? 56.927 30.878  58.000 1.00 38.43  ?  225 LEU A CD1 1 
ATOM   1774 C CD2 . LEU A 1 268 ? 58.963 30.227  56.663 1.00 37.83  ?  225 LEU A CD2 1 
ATOM   1775 N N   . PHE A 1 269 ? 56.783 33.138  52.684 1.00 33.78  ?  226 PHE A N   1 
ATOM   1776 C CA  . PHE A 1 269 ? 55.984 33.309  51.471 1.00 32.49  ?  226 PHE A CA  1 
ATOM   1777 C C   . PHE A 1 269 ? 56.747 32.953  50.204 1.00 43.59  ?  226 PHE A C   1 
ATOM   1778 O O   . PHE A 1 269 ? 56.128 32.864  49.135 1.00 40.36  ?  226 PHE A O   1 
ATOM   1779 C CB  . PHE A 1 269 ? 55.484 34.745  51.347 1.00 31.25  ?  226 PHE A CB  1 
ATOM   1780 C CG  . PHE A 1 269 ? 54.570 35.167  52.473 1.00 38.18  ?  226 PHE A CG  1 
ATOM   1781 C CD1 . PHE A 1 269 ? 53.279 34.668  52.554 1.00 36.32  ?  226 PHE A CD1 1 
ATOM   1782 C CD2 . PHE A 1 269 ? 55.011 36.050  53.442 1.00 37.08  ?  226 PHE A CD2 1 
ATOM   1783 C CE1 . PHE A 1 269 ? 52.440 35.035  53.591 1.00 36.53  ?  226 PHE A CE1 1 
ATOM   1784 C CE2 . PHE A 1 269 ? 54.175 36.428  54.490 1.00 41.42  ?  226 PHE A CE2 1 
ATOM   1785 C CZ  . PHE A 1 269 ? 52.885 35.917  54.557 1.00 35.46  ?  226 PHE A CZ  1 
ATOM   1786 N N   . GLU A 1 270 ? 58.060 32.758  50.289 1.00 41.64  ?  227 GLU A N   1 
ATOM   1787 C CA  . GLU A 1 270 ? 58.881 32.492  49.104 1.00 42.38  ?  227 GLU A CA  1 
ATOM   1788 C C   . GLU A 1 270 ? 58.914 30.995  48.796 1.00 45.47  ?  227 GLU A C   1 
ATOM   1789 O O   . GLU A 1 270 ? 59.952 30.341  48.825 1.00 55.88  ?  227 GLU A O   1 
ATOM   1790 C CB  . GLU A 1 270 ? 60.284 33.049  49.304 1.00 39.83  ?  227 GLU A CB  1 
ATOM   1791 C CG  . GLU A 1 270 ? 60.319 34.555  49.593 1.00 33.44  ?  227 GLU A CG  1 
ATOM   1792 C CD  . GLU A 1 270 ? 61.736 35.088  49.680 1.00 41.78  ?  227 GLU A CD  1 
ATOM   1793 O OE1 . GLU A 1 270 ? 62.681 34.275  49.573 1.00 43.92  ?  227 GLU A OE1 1 
ATOM   1794 O OE2 . GLU A 1 270 ? 61.904 36.312  49.858 1.00 41.37  ?  227 GLU A OE2 1 
ATOM   1795 N N   . VAL A 1 271 ? 57.737 30.451  48.517 1.00 44.26  ?  228 VAL A N   1 
ATOM   1796 C CA  . VAL A 1 271 ? 57.598 29.064  48.115 1.00 41.08  ?  228 VAL A CA  1 
ATOM   1797 C C   . VAL A 1 271 ? 57.258 29.044  46.628 1.00 42.59  ?  228 VAL A C   1 
ATOM   1798 O O   . VAL A 1 271 ? 56.983 30.074  46.017 1.00 49.43  ?  228 VAL A O   1 
ATOM   1799 C CB  . VAL A 1 271 ? 56.534 28.313  48.949 1.00 48.98  ?  228 VAL A CB  1 
ATOM   1800 C CG1 . VAL A 1 271 ? 56.933 28.255  50.402 1.00 46.74  ?  228 VAL A CG1 1 
ATOM   1801 C CG2 . VAL A 1 271 ? 55.173 28.983  48.814 1.00 47.22  ?  228 VAL A CG2 1 
ATOM   1802 N N   . ASP A 1 272 ? 57.289 27.856  46.045 1.00 44.22  ?  229 ASP A N   1 
ATOM   1803 C CA  . ASP A 1 272 ? 56.854 27.689  44.664 1.00 48.01  ?  229 ASP A CA  1 
ATOM   1804 C C   . ASP A 1 272 ? 55.331 27.643  44.650 1.00 48.24  ?  229 ASP A C   1 
ATOM   1805 O O   . ASP A 1 272 ? 54.727 26.707  45.188 1.00 52.17  ?  229 ASP A O   1 
ATOM   1806 C CB  . ASP A 1 272 ? 57.457 26.421  44.073 1.00 47.59  ?  229 ASP A CB  1 
ATOM   1807 C CG  . ASP A 1 272 ? 57.197 26.289  42.579 1.00 53.89  ?  229 ASP A CG  1 
ATOM   1808 O OD1 . ASP A 1 272 ? 56.436 27.107  42.022 1.00 49.87  ?  229 ASP A OD1 1 
ATOM   1809 O OD2 . ASP A 1 272 ? 57.761 25.358  41.966 1.00 59.97  ?  229 ASP A OD2 1 
ATOM   1810 N N   . TRP A 1 273 ? 54.707 28.657  44.059 1.00 34.92  ?  230 TRP A N   1 
ATOM   1811 C CA  . TRP A 1 273 ? 53.258 28.758  44.024 1.00 37.43  ?  230 TRP A CA  1 
ATOM   1812 C C   . TRP A 1 273 ? 52.641 28.167  42.758 1.00 44.22  ?  230 TRP A C   1 
ATOM   1813 O O   . TRP A 1 273 ? 51.426 28.290  42.566 1.00 37.25  ?  230 TRP A O   1 
ATOM   1814 C CB  . TRP A 1 273 ? 52.842 30.222  44.175 1.00 38.19  ?  230 TRP A CB  1 
ATOM   1815 C CG  . TRP A 1 273 ? 53.112 30.767  45.570 1.00 36.02  ?  230 TRP A CG  1 
ATOM   1816 C CD1 . TRP A 1 273 ? 54.205 31.475  45.982 1.00 35.62  ?  230 TRP A CD1 1 
ATOM   1817 C CD2 . TRP A 1 273 ? 52.266 30.619  46.719 1.00 33.50  ?  230 TRP A CD2 1 
ATOM   1818 N NE1 . TRP A 1 273 ? 54.086 31.787  47.330 1.00 36.30  ?  230 TRP A NE1 1 
ATOM   1819 C CE2 . TRP A 1 273 ? 52.902 31.274  47.798 1.00 37.81  ?  230 TRP A CE2 1 
ATOM   1820 C CE3 . TRP A 1 273 ? 51.029 30.001  46.935 1.00 33.85  ?  230 TRP A CE3 1 
ATOM   1821 C CZ2 . TRP A 1 273 ? 52.338 31.321  49.088 1.00 36.35  ?  230 TRP A CZ2 1 
ATOM   1822 C CZ3 . TRP A 1 273 ? 50.464 30.057  48.215 1.00 34.56  ?  230 TRP A CZ3 1 
ATOM   1823 C CH2 . TRP A 1 273 ? 51.123 30.710  49.269 1.00 38.57  ?  230 TRP A CH2 1 
ATOM   1824 N N   . ILE A 1 274 ? 53.439 27.521  41.900 1.00 41.42  ?  231 ILE A N   1 
ATOM   1825 C CA  . ILE A 1 274 ? 52.929 27.117  40.587 1.00 50.54  ?  231 ILE A CA  1 
ATOM   1826 C C   . ILE A 1 274 ? 51.729 26.181  40.723 1.00 50.48  ?  231 ILE A C   1 
ATOM   1827 O O   . ILE A 1 274 ? 50.727 26.339  40.015 1.00 45.94  ?  231 ILE A O   1 
ATOM   1828 C CB  . ILE A 1 274 ? 54.049 26.498  39.725 1.00 49.10  ?  231 ILE A CB  1 
ATOM   1829 C CG1 . ILE A 1 274 ? 53.492 26.070  38.364 1.00 54.85  ?  231 ILE A CG1 1 
ATOM   1830 C CG2 . ILE A 1 274 ? 54.671 25.318  40.414 1.00 53.01  ?  231 ILE A CG2 1 
ATOM   1831 C CD1 . ILE A 1 274 ? 52.716 27.171  37.662 1.00 56.65  ?  231 ILE A CD1 1 
ATOM   1832 N N   . THR A 1 275 ? 51.784 25.215  41.647 1.00 45.38  ?  232 THR A N   1 
ATOM   1833 C CA  . THR A 1 275 ? 50.694 24.250  41.769 1.00 45.46  ?  232 THR A CA  1 
ATOM   1834 C C   . THR A 1 275 ? 49.606 24.684  42.761 1.00 49.34  ?  232 THR A C   1 
ATOM   1835 O O   . THR A 1 275 ? 48.757 23.864  43.127 1.00 46.12  ?  232 THR A O   1 
ATOM   1836 C CB  . THR A 1 275 ? 51.233 22.863  42.155 1.00 50.18  ?  232 THR A CB  1 
ATOM   1837 O OG1 . THR A 1 275 ? 51.788 22.895  43.475 1.00 49.28  ?  232 THR A OG1 1 
ATOM   1838 C CG2 . THR A 1 275 ? 52.304 22.394  41.170 1.00 51.62  ?  232 THR A CG2 1 
ATOM   1839 N N   . TYR A 1 276 ? 49.594 25.946  43.180 1.00 45.70  ?  233 TYR A N   1 
ATOM   1840 C CA  . TYR A 1 276 ? 48.540 26.476  44.037 1.00 44.33  ?  233 TYR A CA  1 
ATOM   1841 C C   . TYR A 1 276 ? 47.376 26.981  43.197 1.00 45.75  ?  233 TYR A C   1 
ATOM   1842 O O   . TYR A 1 276 ? 47.570 27.787  42.280 1.00 43.82  ?  233 TYR A O   1 
ATOM   1843 C CB  . TYR A 1 276 ? 49.070 27.617  44.899 1.00 42.22  ?  233 TYR A CB  1 
ATOM   1844 C CG  . TYR A 1 276 ? 47.997 28.355  45.674 1.00 42.38  ?  233 TYR A CG  1 
ATOM   1845 C CD1 . TYR A 1 276 ? 47.533 27.871  46.899 1.00 37.80  ?  233 TYR A CD1 1 
ATOM   1846 C CD2 . TYR A 1 276 ? 47.463 29.541  45.195 1.00 38.32  ?  233 TYR A CD2 1 
ATOM   1847 C CE1 . TYR A 1 276 ? 46.559 28.551  47.610 1.00 33.62  ?  233 TYR A CE1 1 
ATOM   1848 C CE2 . TYR A 1 276 ? 46.487 30.231  45.897 1.00 41.33  ?  233 TYR A CE2 1 
ATOM   1849 C CZ  . TYR A 1 276 ? 46.041 29.730  47.112 1.00 39.51  ?  233 TYR A CZ  1 
ATOM   1850 O OH  . TYR A 1 276 ? 45.077 30.411  47.813 1.00 37.37  ?  233 TYR A OH  1 
ATOM   1851 N N   . HIS A 1 277 ? 46.170 26.517  43.521 1.00 36.67  ?  234 HIS A N   1 
ATOM   1852 C CA  . HIS A 1 277 ? 44.942 26.990  42.892 1.00 44.34  ?  234 HIS A CA  1 
ATOM   1853 C C   . HIS A 1 277 ? 43.921 27.252  43.985 1.00 37.61  ?  234 HIS A C   1 
ATOM   1854 O O   . HIS A 1 277 ? 43.518 26.321  44.688 1.00 39.77  ?  234 HIS A O   1 
ATOM   1855 C CB  . HIS A 1 277 ? 44.398 25.968  41.890 1.00 42.22  ?  234 HIS A CB  1 
ATOM   1856 C CG  . HIS A 1 277 ? 45.422 25.497  40.906 1.00 57.61  ?  234 HIS A CG  1 
ATOM   1857 N ND1 . HIS A 1 277 ? 45.714 26.188  39.749 1.00 51.97  ?  234 HIS A ND1 1 
ATOM   1858 C CD2 . HIS A 1 277 ? 46.249 24.424  40.926 1.00 57.18  ?  234 HIS A CD2 1 
ATOM   1859 C CE1 . HIS A 1 277 ? 46.671 25.554  39.094 1.00 56.43  ?  234 HIS A CE1 1 
ATOM   1860 N NE2 . HIS A 1 277 ? 47.015 24.483  39.787 1.00 50.48  ?  234 HIS A NE2 1 
ATOM   1861 N N   . THR A 1 278 ? 43.482 28.502  44.107 1.00 40.29  ?  235 THR A N   1 
ATOM   1862 C CA  . THR A 1 278 ? 42.593 28.863  45.204 1.00 43.57  ?  235 THR A CA  1 
ATOM   1863 C C   . THR A 1 278 ? 41.302 28.052  45.149 1.00 49.64  ?  235 THR A C   1 
ATOM   1864 O O   . THR A 1 278 ? 40.756 27.784  44.071 1.00 44.62  ?  235 THR A O   1 
ATOM   1865 C CB  . THR A 1 278 ? 42.286 30.362  45.158 1.00 40.59  ?  235 THR A CB  1 
ATOM   1866 O OG1 . THR A 1 278 ? 41.412 30.711  46.234 1.00 40.08  ?  235 THR A OG1 1 
ATOM   1867 C CG2 . THR A 1 278 ? 41.626 30.749  43.832 1.00 40.10  ?  235 THR A CG2 1 
ATOM   1868 N N   . ASP A 1 279 ? 40.826 27.634  46.324 1.00 39.54  ?  236 ASP A N   1 
ATOM   1869 C CA  . ASP A 1 279 ? 39.458 27.151  46.466 1.00 43.65  ?  236 ASP A CA  1 
ATOM   1870 C C   . ASP A 1 279 ? 38.492 28.265  46.855 1.00 45.27  ?  236 ASP A C   1 
ATOM   1871 O O   . ASP A 1 279 ? 37.364 27.978  47.271 1.00 43.80  ?  236 ASP A O   1 
ATOM   1872 C CB  . ASP A 1 279 ? 39.391 26.012  47.494 1.00 39.56  ?  236 ASP A CB  1 
ATOM   1873 C CG  . ASP A 1 279 ? 39.709 26.475  48.904 1.00 51.21  ?  236 ASP A CG  1 
ATOM   1874 O OD1 . ASP A 1 279 ? 40.098 27.651  49.079 1.00 44.03  ?  236 ASP A OD1 1 
ATOM   1875 O OD2 . ASP A 1 279 ? 39.570 25.656  49.846 1.00 50.80  ?  236 ASP A OD2 1 
ATOM   1876 N N   . GLY A 1 280 ? 38.913 29.529  46.746 1.00 41.37  ?  237 GLY A N   1 
ATOM   1877 C CA  . GLY A 1 280 ? 38.127 30.644  47.226 1.00 38.18  ?  237 GLY A CA  1 
ATOM   1878 C C   . GLY A 1 280 ? 38.241 30.932  48.713 1.00 45.02  ?  237 GLY A C   1 
ATOM   1879 O O   . GLY A 1 280 ? 37.693 31.941  49.176 1.00 41.23  ?  237 GLY A O   1 
ATOM   1880 N N   . ASN A 1 281 ? 38.919 30.079  49.478 1.00 39.51  ?  238 ASN A N   1 
ATOM   1881 C CA  . ASN A 1 281 ? 39.091 30.269  50.914 1.00 40.28  ?  238 ASN A CA  1 
ATOM   1882 C C   . ASN A 1 281 ? 40.530 30.678  51.181 1.00 34.62  ?  238 ASN A C   1 
ATOM   1883 O O   . ASN A 1 281 ? 41.443 29.891  50.897 1.00 38.58  ?  238 ASN A O   1 
ATOM   1884 C CB  . ASN A 1 281 ? 38.748 28.977  51.656 1.00 40.03  ?  238 ASN A CB  1 
ATOM   1885 C CG  . ASN A 1 281 ? 38.925 29.082  53.162 1.00 44.80  ?  238 ASN A CG  1 
ATOM   1886 O OD1 . ASN A 1 281 ? 39.352 30.111  53.697 1.00 41.46  ?  238 ASN A OD1 1 
ATOM   1887 N ND2 . ASN A 1 281 ? 38.585 28.002  53.859 1.00 47.10  ?  238 ASN A ND2 1 
ATOM   1888 N N   . PRO A 1 282 ? 40.796 31.878  51.694 1.00 36.89  ?  239 PRO A N   1 
ATOM   1889 C CA  . PRO A 1 282 ? 42.199 32.272  51.897 1.00 35.78  ?  239 PRO A CA  1 
ATOM   1890 C C   . PRO A 1 282 ? 42.963 31.328  52.804 1.00 40.13  ?  239 PRO A C   1 
ATOM   1891 O O   . PRO A 1 282 ? 44.195 31.247  52.694 1.00 37.14  ?  239 PRO A O   1 
ATOM   1892 C CB  . PRO A 1 282 ? 42.096 33.681  52.499 1.00 36.57  ?  239 PRO A CB  1 
ATOM   1893 C CG  . PRO A 1 282 ? 40.664 33.804  53.004 1.00 43.79  ?  239 PRO A CG  1 
ATOM   1894 C CD  . PRO A 1 282 ? 39.848 32.940  52.072 1.00 34.70  ?  239 PRO A CD  1 
ATOM   1895 N N   . THR A 1 283 ? 42.276 30.609  53.699 1.00 36.98  ?  240 THR A N   1 
ATOM   1896 C CA  . THR A 1 283 ? 42.973 29.680  54.575 1.00 35.61  ?  240 THR A CA  1 
ATOM   1897 C C   . THR A 1 283 ? 43.769 28.657  53.784 1.00 36.64  ?  240 THR A C   1 
ATOM   1898 O O   . THR A 1 283 ? 44.837 28.218  54.230 1.00 35.07  ?  240 THR A O   1 
ATOM   1899 C CB  . THR A 1 283 ? 41.973 28.982  55.497 1.00 36.72  ?  240 THR A CB  1 
ATOM   1900 O OG1 . THR A 1 283 ? 41.234 29.982  56.199 1.00 38.99  ?  240 THR A OG1 1 
ATOM   1901 C CG2 . THR A 1 283 ? 42.702 28.107  56.508 1.00 34.86  ?  240 THR A CG2 1 
ATOM   1902 N N   . TYR A 1 284 ? 43.280 28.275  52.600 1.00 35.95  ?  241 TYR A N   1 
ATOM   1903 C CA  . TYR A 1 284 ? 44.008 27.296  51.806 1.00 37.03  ?  241 TYR A CA  1 
ATOM   1904 C C   . TYR A 1 284 ? 45.377 27.826  51.379 1.00 33.23  ?  241 TYR A C   1 
ATOM   1905 O O   . TYR A 1 284 ? 46.322 27.046  51.237 1.00 31.68  ?  241 TYR A O   1 
ATOM   1906 C CB  . TYR A 1 284 ? 43.181 26.875  50.583 1.00 35.23  ?  241 TYR A CB  1 
ATOM   1907 C CG  . TYR A 1 284 ? 43.927 25.893  49.722 1.00 38.88  ?  241 TYR A CG  1 
ATOM   1908 C CD1 . TYR A 1 284 ? 44.355 24.683  50.243 1.00 41.20  ?  241 TYR A CD1 1 
ATOM   1909 C CD2 . TYR A 1 284 ? 44.226 26.180  48.384 1.00 38.72  ?  241 TYR A CD2 1 
ATOM   1910 C CE1 . TYR A 1 284 ? 45.055 23.777  49.477 1.00 41.28  ?  241 TYR A CE1 1 
ATOM   1911 C CE2 . TYR A 1 284 ? 44.934 25.282  47.615 1.00 32.46  ?  241 TYR A CE2 1 
ATOM   1912 C CZ  . TYR A 1 284 ? 45.343 24.086  48.157 1.00 39.42  ?  241 TYR A CZ  1 
ATOM   1913 O OH  . TYR A 1 284 ? 46.044 23.185  47.391 1.00 44.71  ?  241 TYR A OH  1 
ATOM   1914 N N   . GLY A 1 285 ? 45.514 29.141  51.191 1.00 35.55  ?  242 GLY A N   1 
ATOM   1915 C CA  . GLY A 1 285 ? 46.829 29.695  50.881 1.00 35.93  ?  242 GLY A CA  1 
ATOM   1916 C C   . GLY A 1 285 ? 47.820 29.521  52.020 1.00 39.11  ?  242 GLY A C   1 
ATOM   1917 O O   . GLY A 1 285 ? 48.985 29.174  51.807 1.00 33.12  ?  242 GLY A O   1 
ATOM   1918 N N   . TRP A 1 286 ? 47.371 29.754  53.252 1.00 33.27  ?  243 TRP A N   1 
ATOM   1919 C CA  . TRP A 1 286 ? 48.256 29.549  54.392 1.00 28.61  ?  243 TRP A CA  1 
ATOM   1920 C C   . TRP A 1 286 ? 48.613 28.077  54.561 1.00 29.34  ?  243 TRP A C   1 
ATOM   1921 O O   . TRP A 1 286 ? 49.768 27.746  54.847 1.00 37.44  ?  243 TRP A O   1 
ATOM   1922 C CB  . TRP A 1 286 ? 47.590 30.102  55.647 1.00 27.96  ?  243 TRP A CB  1 
ATOM   1923 C CG  . TRP A 1 286 ? 47.368 31.571  55.617 1.00 29.21  ?  243 TRP A CG  1 
ATOM   1924 C CD1 . TRP A 1 286 ? 46.202 32.222  55.317 1.00 30.95  ?  243 TRP A CD1 1 
ATOM   1925 C CD2 . TRP A 1 286 ? 48.333 32.588  55.906 1.00 26.40  ?  243 TRP A CD2 1 
ATOM   1926 N NE1 . TRP A 1 286 ? 46.383 33.582  55.424 1.00 32.96  ?  243 TRP A NE1 1 
ATOM   1927 C CE2 . TRP A 1 286 ? 47.684 33.831  55.772 1.00 29.79  ?  243 TRP A CE2 1 
ATOM   1928 C CE3 . TRP A 1 286 ? 49.683 32.569  56.253 1.00 31.97  ?  243 TRP A CE3 1 
ATOM   1929 C CZ2 . TRP A 1 286 ? 48.339 35.042  55.979 1.00 32.32  ?  243 TRP A CZ2 1 
ATOM   1930 C CZ3 . TRP A 1 286 ? 50.331 33.778  56.474 1.00 30.48  ?  243 TRP A CZ3 1 
ATOM   1931 C CH2 . TRP A 1 286 ? 49.662 34.993  56.344 1.00 31.98  ?  243 TRP A CH2 1 
ATOM   1932 N N   . LEU A 1 287 ? 47.644 27.176  54.367 1.00 32.33  ?  244 LEU A N   1 
ATOM   1933 C CA  . LEU A 1 287 ? 47.927 25.745  54.435 1.00 31.90  ?  244 LEU A CA  1 
ATOM   1934 C C   . LEU A 1 287 ? 48.919 25.314  53.356 1.00 35.90  ?  244 LEU A C   1 
ATOM   1935 O O   . LEU A 1 287 ? 49.847 24.539  53.616 1.00 34.10  ?  244 LEU A O   1 
ATOM   1936 C CB  . LEU A 1 287 ? 46.630 24.951  54.300 1.00 37.62  ?  244 LEU A CB  1 
ATOM   1937 C CG  . LEU A 1 287 ? 46.865 23.439  54.215 1.00 43.40  ?  244 LEU A CG  1 
ATOM   1938 C CD1 . LEU A 1 287 ? 47.208 22.841  55.589 1.00 39.93  ?  244 LEU A CD1 1 
ATOM   1939 C CD2 . LEU A 1 287 ? 45.683 22.734  53.614 1.00 44.48  ?  244 LEU A CD2 1 
ATOM   1940 N N   . TYR A 1 288 ? 48.718 25.821  52.144 1.00 35.92  ?  245 TYR A N   1 
ATOM   1941 C CA  . TYR A 1 288 ? 49.593 25.498  51.025 1.00 35.73  ?  245 TYR A CA  1 
ATOM   1942 C C   . TYR A 1 288 ? 50.998 26.027  51.284 1.00 34.17  ?  245 TYR A C   1 
ATOM   1943 O O   . TYR A 1 288 ? 51.986 25.431  50.855 1.00 46.37  ?  245 TYR A O   1 
ATOM   1944 C CB  . TYR A 1 288 ? 49.040 26.084  49.724 1.00 35.02  ?  245 TYR A CB  1 
ATOM   1945 C CG  . TYR A 1 288 ? 49.932 25.862  48.524 1.00 39.09  ?  245 TYR A CG  1 
ATOM   1946 C CD1 . TYR A 1 288 ? 51.069 26.634  48.328 1.00 40.83  ?  245 TYR A CD1 1 
ATOM   1947 C CD2 . TYR A 1 288 ? 49.638 24.880  47.588 1.00 39.57  ?  245 TYR A CD2 1 
ATOM   1948 C CE1 . TYR A 1 288 ? 51.888 26.434  47.232 1.00 39.87  ?  245 TYR A CE1 1 
ATOM   1949 C CE2 . TYR A 1 288 ? 50.450 24.673  46.489 1.00 40.91  ?  245 TYR A CE2 1 
ATOM   1950 C CZ  . TYR A 1 288 ? 51.574 25.453  46.316 1.00 47.48  ?  245 TYR A CZ  1 
ATOM   1951 O OH  . TYR A 1 288 ? 52.386 25.250  45.224 1.00 43.85  ?  245 TYR A OH  1 
ATOM   1952 N N   . LEU A 1 289 ? 51.078 27.150  51.990 1.00 34.21  ?  246 LEU A N   1 
ATOM   1953 C CA  . LEU A 1 289 ? 52.360 27.761  52.315 1.00 39.63  ?  246 LEU A CA  1 
ATOM   1954 C C   . LEU A 1 289 ? 53.121 26.902  53.317 1.00 45.39  ?  246 LEU A C   1 
ATOM   1955 O O   . LEU A 1 289 ? 54.328 26.699  53.186 1.00 38.93  ?  246 LEU A O   1 
ATOM   1956 C CB  . LEU A 1 289 ? 52.156 29.170  52.876 1.00 44.83  ?  246 LEU A CB  1 
ATOM   1957 C CG  . LEU A 1 289 ? 53.418 29.911  53.323 1.00 56.21  ?  246 LEU A CG  1 
ATOM   1958 C CD1 . LEU A 1 289 ? 53.248 31.413  53.153 1.00 58.40  ?  246 LEU A CD1 1 
ATOM   1959 C CD2 . LEU A 1 289 ? 53.761 29.566  54.764 1.00 39.89  ?  246 LEU A CD2 1 
ATOM   1960 N N   . LEU A 1 290 ? 52.407 26.399  54.319 1.00 38.11  ?  247 LEU A N   1 
ATOM   1961 C CA  . LEU A 1 290 ? 53.016 25.554  55.346 1.00 38.79  ?  247 LEU A CA  1 
ATOM   1962 C C   . LEU A 1 290 ? 53.363 24.175  54.794 1.00 38.65  ?  247 LEU A C   1 
ATOM   1963 O O   . LEU A 1 290 ? 54.460 23.657  55.031 1.00 41.66  ?  247 LEU A O   1 
ATOM   1964 C CB  . LEU A 1 290 ? 52.076 25.426  56.544 1.00 37.39  ?  247 LEU A CB  1 
ATOM   1965 C CG  . LEU A 1 290 ? 51.923 26.719  57.339 1.00 36.98  ?  247 LEU A CG  1 
ATOM   1966 C CD1 . LEU A 1 290 ? 50.871 26.554  58.437 1.00 36.93  ?  247 LEU A CD1 1 
ATOM   1967 C CD2 . LEU A 1 290 ? 53.281 27.115  57.912 1.00 33.61  ?  247 LEU A CD2 1 
ATOM   1968 N N   . HIS A 1 291 ? 52.437 23.567  54.053 1.00 40.24  ?  248 HIS A N   1 
ATOM   1969 C CA  . HIS A 1 291 ? 52.659 22.209  53.567 1.00 45.27  ?  248 HIS A CA  1 
ATOM   1970 C C   . HIS A 1 291 ? 53.868 22.143  52.644 1.00 48.36  ?  248 HIS A C   1 
ATOM   1971 O O   . HIS A 1 291 ? 54.682 21.216  52.734 1.00 43.87  ?  248 HIS A O   1 
ATOM   1972 C CB  . HIS A 1 291 ? 51.416 21.705  52.840 1.00 43.55  ?  248 HIS A CB  1 
ATOM   1973 C CG  . HIS A 1 291 ? 51.571 20.324  52.289 1.00 46.18  ?  248 HIS A CG  1 
ATOM   1974 N ND1 . HIS A 1 291 ? 51.835 20.080  50.960 1.00 45.25  ?  248 HIS A ND1 1 
ATOM   1975 C CD2 . HIS A 1 291 ? 51.522 19.114  52.892 1.00 44.10  ?  248 HIS A CD2 1 
ATOM   1976 C CE1 . HIS A 1 291 ? 51.930 18.777  50.763 1.00 46.12  ?  248 HIS A CE1 1 
ATOM   1977 N NE2 . HIS A 1 291 ? 51.746 18.168  51.921 1.00 51.63  ?  248 HIS A NE2 1 
ATOM   1978 N N   . GLN A 1 292 ? 53.994 23.122  51.748 1.00 42.09  ?  249 GLN A N   1 
ATOM   1979 C CA  . GLN A 1 292 ? 55.106 23.152  50.807 1.00 47.65  ?  249 GLN A CA  1 
ATOM   1980 C C   . GLN A 1 292 ? 56.450 23.135  51.511 1.00 49.34  ?  249 GLN A C   1 
ATOM   1981 O O   . GLN A 1 292 ? 57.422 22.599  50.972 1.00 55.55  ?  249 GLN A O   1 
ATOM   1982 C CB  . GLN A 1 292 ? 55.007 24.395  49.935 1.00 48.72  ?  249 GLN A CB  1 
ATOM   1983 C CG  . GLN A 1 292 ? 53.975 24.277  48.858 1.00 58.05  ?  249 GLN A CG  1 
ATOM   1984 C CD  . GLN A 1 292 ? 54.514 23.511  47.674 1.00 61.97  ?  249 GLN A CD  1 
ATOM   1985 O OE1 . GLN A 1 292 ? 55.519 23.910  47.079 1.00 63.18  ?  249 GLN A OE1 1 
ATOM   1986 N NE2 . GLN A 1 292 ? 53.873 22.392  47.343 1.00 43.85  ?  249 GLN A NE2 1 
ATOM   1987 N N   . GLN A 1 293 ? 56.536 23.746  52.689 1.00 44.29  ?  250 GLN A N   1 
ATOM   1988 C CA  . GLN A 1 293 ? 57.794 23.881  53.404 1.00 43.68  ?  250 GLN A CA  1 
ATOM   1989 C C   . GLN A 1 293 ? 57.931 22.901  54.550 1.00 41.40  ?  250 GLN A C   1 
ATOM   1990 O O   . GLN A 1 293 ? 58.909 22.989  55.290 1.00 44.06  ?  250 GLN A O   1 
ATOM   1991 C CB  . GLN A 1 293 ? 57.945 25.298  53.957 1.00 50.28  ?  250 GLN A CB  1 
ATOM   1992 C CG  . GLN A 1 293 ? 57.985 26.344  52.903 1.00 57.08  ?  250 GLN A CG  1 
ATOM   1993 C CD  . GLN A 1 293 ? 57.917 27.729  53.477 1.00 43.86  ?  250 GLN A CD  1 
ATOM   1994 O OE1 . GLN A 1 293 ? 58.942 28.346  53.751 1.00 51.58  ?  250 GLN A OE1 1 
ATOM   1995 N NE2 . GLN A 1 293 ? 56.703 28.244  53.638 1.00 41.38  ?  250 GLN A NE2 1 
ATOM   1996 N N   . LYS A 1 294 ? 56.969 21.995  54.730 1.00 42.17  ?  251 LYS A N   1 
ATOM   1997 C CA  . LYS A 1 294 ? 56.981 21.059  55.855 1.00 45.59  ?  251 LYS A CA  1 
ATOM   1998 C C   . LYS A 1 294 ? 57.047 21.796  57.192 1.00 48.23  ?  251 LYS A C   1 
ATOM   1999 O O   . LYS A 1 294 ? 57.776 21.402  58.103 1.00 48.51  ?  251 LYS A O   1 
ATOM   2000 C CB  . LYS A 1 294 ? 58.139 20.066  55.738 1.00 51.11  ?  251 LYS A CB  1 
ATOM   2001 C CG  . LYS A 1 294 ? 58.113 19.183  54.509 1.00 56.98  ?  251 LYS A CG  1 
ATOM   2002 C CD  . LYS A 1 294 ? 59.340 18.279  54.495 1.00 67.22  ?  251 LYS A CD  1 
ATOM   2003 C CE  . LYS A 1 294 ? 59.067 16.957  53.787 1.00 75.55  ?  251 LYS A CE  1 
ATOM   2004 N NZ  . LYS A 1 294 ? 58.622 17.137  52.379 1.00 71.28  ?  251 LYS A NZ  1 
ATOM   2005 N N   . ARG A 1 295 ? 56.283 22.876  57.319 1.00 47.77  ?  252 ARG A N   1 
ATOM   2006 C CA  . ARG A 1 295 ? 56.223 23.610  58.575 1.00 40.67  ?  252 ARG A CA  1 
ATOM   2007 C C   . ARG A 1 295 ? 54.839 23.500  59.204 1.00 44.22  ?  252 ARG A C   1 
ATOM   2008 O O   . ARG A 1 295 ? 53.867 23.066  58.580 1.00 39.51  ?  252 ARG A O   1 
ATOM   2009 C CB  . ARG A 1 295 ? 56.619 25.076  58.372 1.00 44.93  ?  252 ARG A CB  1 
ATOM   2010 C CG  . ARG A 1 295 ? 58.105 25.244  58.020 1.00 49.21  ?  252 ARG A CG  1 
ATOM   2011 C CD  . ARG A 1 295 ? 58.516 26.699  57.867 1.00 47.84  ?  252 ARG A CD  1 
ATOM   2012 N NE  . ARG A 1 295 ? 59.970 26.860  57.779 1.00 51.23  ?  252 ARG A NE  1 
ATOM   2013 C CZ  . ARG A 1 295 ? 60.775 26.942  58.838 1.00 52.82  ?  252 ARG A CZ  1 
ATOM   2014 N NH1 . ARG A 1 295 ? 60.272 26.875  60.060 1.00 47.84  ?  252 ARG A NH1 1 
ATOM   2015 N NH2 . ARG A 1 295 ? 62.082 27.091  58.678 1.00 54.75  ?  252 ARG A NH2 1 
ATOM   2016 N N   . GLN A 1 296 ? 54.765 23.902  60.469 1.00 43.64  ?  253 GLN A N   1 
ATOM   2017 C CA  . GLN A 1 296 ? 53.565 23.784  61.285 1.00 41.72  ?  253 GLN A CA  1 
ATOM   2018 C C   . GLN A 1 296 ? 52.950 25.154  61.535 1.00 39.83  ?  253 GLN A C   1 
ATOM   2019 O O   . GLN A 1 296 ? 53.563 26.192  61.284 1.00 39.00  ?  253 GLN A O   1 
ATOM   2020 C CB  . GLN A 1 296 ? 53.895 23.109  62.622 1.00 41.91  ?  253 GLN A CB  1 
ATOM   2021 C CG  . GLN A 1 296 ? 54.602 21.786  62.460 1.00 48.57  ?  253 GLN A CG  1 
ATOM   2022 C CD  . GLN A 1 296 ? 53.714 20.731  61.847 1.00 56.05  ?  253 GLN A CD  1 
ATOM   2023 O OE1 . GLN A 1 296 ? 52.615 20.466  62.337 1.00 64.35  ?  253 GLN A OE1 1 
ATOM   2024 N NE2 . GLN A 1 296 ? 54.182 20.120  60.762 1.00 54.62  ?  253 GLN A NE2 1 
ATOM   2025 N N   . PHE A 1 297 ? 51.730 25.145  62.083 1.00 37.79  ?  254 PHE A N   1 
ATOM   2026 C CA  . PHE A 1 297 ? 50.975 26.387  62.213 1.00 38.20  ?  254 PHE A CA  1 
ATOM   2027 C C   . PHE A 1 297 ? 51.685 27.402  63.100 1.00 37.28  ?  254 PHE A C   1 
ATOM   2028 O O   . PHE A 1 297 ? 51.555 28.614  62.879 1.00 34.45  ?  254 PHE A O   1 
ATOM   2029 C CB  . PHE A 1 297 ? 49.571 26.101  62.754 1.00 37.18  ?  254 PHE A CB  1 
ATOM   2030 C CG  . PHE A 1 297 ? 48.833 27.335  63.176 1.00 39.16  ?  254 PHE A CG  1 
ATOM   2031 C CD1 . PHE A 1 297 ? 48.072 28.045  62.266 1.00 37.83  ?  254 PHE A CD1 1 
ATOM   2032 C CD2 . PHE A 1 297 ? 48.922 27.800  64.490 1.00 36.29  ?  254 PHE A CD2 1 
ATOM   2033 C CE1 . PHE A 1 297 ? 47.409 29.209  62.655 1.00 36.27  ?  254 PHE A CE1 1 
ATOM   2034 C CE2 . PHE A 1 297 ? 48.272 28.951  64.876 1.00 37.49  ?  254 PHE A CE2 1 
ATOM   2035 C CZ  . PHE A 1 297 ? 47.510 29.659  63.964 1.00 38.05  ?  254 PHE A CZ  1 
ATOM   2036 N N   . THR A 1 298 ? 52.406 26.945  64.132 1.00 35.86  ?  255 THR A N   1 
ATOM   2037 C CA  . THR A 1 298 ? 53.056 27.895  65.027 1.00 37.37  ?  255 THR A CA  1 
ATOM   2038 C C   . THR A 1 298 ? 53.937 28.873  64.264 1.00 36.51  ?  255 THR A C   1 
ATOM   2039 O O   . THR A 1 298 ? 54.118 30.017  64.692 1.00 37.12  ?  255 THR A O   1 
ATOM   2040 C CB  . THR A 1 298 ? 53.892 27.164  66.092 1.00 44.19  ?  255 THR A CB  1 
ATOM   2041 O OG1 . THR A 1 298 ? 54.347 28.113  67.061 1.00 43.41  ?  255 THR A OG1 1 
ATOM   2042 C CG2 . THR A 1 298 ? 55.109 26.480  65.465 1.00 40.19  ?  255 THR A CG2 1 
ATOM   2043 N N   . ASP A 1 299 ? 54.469 28.454  63.118 1.00 40.54  ?  256 ASP A N   1 
ATOM   2044 C CA  . ASP A 1 299 ? 55.357 29.322  62.357 1.00 37.68  ?  256 ASP A CA  1 
ATOM   2045 C C   . ASP A 1 299 ? 54.653 30.550  61.783 1.00 34.34  ?  256 ASP A C   1 
ATOM   2046 O O   . ASP A 1 299 ? 55.325 31.543  61.492 1.00 37.40  ?  256 ASP A O   1 
ATOM   2047 C CB  . ASP A 1 299 ? 56.023 28.511  61.248 1.00 39.31  ?  256 ASP A CB  1 
ATOM   2048 C CG  . ASP A 1 299 ? 57.126 27.610  61.775 1.00 44.85  ?  256 ASP A CG  1 
ATOM   2049 O OD1 . ASP A 1 299 ? 57.600 27.855  62.902 1.00 44.18  ?  256 ASP A OD1 1 
ATOM   2050 O OD2 . ASP A 1 299 ? 57.522 26.666  61.065 1.00 49.36  ?  256 ASP A OD2 1 
ATOM   2051 N N   . ILE A 1 300 ? 53.331 30.531  61.621 1.00 33.42  ?  257 ILE A N   1 
ATOM   2052 C CA  . ILE A 1 300 ? 52.624 31.694  61.092 1.00 32.64  ?  257 ILE A CA  1 
ATOM   2053 C C   . ILE A 1 300 ? 51.721 32.344  62.132 1.00 34.90  ?  257 ILE A C   1 
ATOM   2054 O O   . ILE A 1 300 ? 50.926 33.226  61.789 1.00 34.75  ?  257 ILE A O   1 
ATOM   2055 C CB  . ILE A 1 300 ? 51.820 31.349  59.820 1.00 34.34  ?  257 ILE A CB  1 
ATOM   2056 C CG1 . ILE A 1 300 ? 50.905 30.140  60.051 1.00 31.46  ?  257 ILE A CG1 1 
ATOM   2057 C CG2 . ILE A 1 300 ? 52.763 31.085  58.634 1.00 35.92  ?  257 ILE A CG2 1 
ATOM   2058 C CD1 . ILE A 1 300 ? 49.954 29.864  58.869 1.00 32.03  ?  257 ILE A CD1 1 
ATOM   2059 N N   . LYS A 1 301 ? 51.834 31.961  63.407 1.00 36.03  ?  258 LYS A N   1 
ATOM   2060 C CA  . LYS A 1 301 ? 50.828 32.433  64.355 1.00 32.81  ?  258 LYS A CA  1 
ATOM   2061 C C   . LYS A 1 301 ? 50.903 33.940  64.590 1.00 32.26  ?  258 LYS A C   1 
ATOM   2062 O O   . LYS A 1 301 ? 49.935 34.523  65.097 1.00 36.18  ?  258 LYS A O   1 
ATOM   2063 C CB  . LYS A 1 301 ? 50.941 31.663  65.679 1.00 33.41  ?  258 LYS A CB  1 
ATOM   2064 C CG  . LYS A 1 301 ? 52.200 31.897  66.476 1.00 39.44  ?  258 LYS A CG  1 
ATOM   2065 C CD  . LYS A 1 301 ? 52.049 31.243  67.871 1.00 43.75  ?  258 LYS A CD  1 
ATOM   2066 C CE  . LYS A 1 301 ? 53.217 31.546  68.798 1.00 45.11  ?  258 LYS A CE  1 
ATOM   2067 N NZ  . LYS A 1 301 ? 52.958 31.007  70.173 1.00 56.24  ?  258 LYS A NZ  1 
ATOM   2068 N N   . ASP A 1 302 ? 52.006 34.588  64.209 1.00 34.74  ?  259 ASP A N   1 
ATOM   2069 C CA  . ASP A 1 302 ? 52.084 36.047  64.281 1.00 37.55  ?  259 ASP A CA  1 
ATOM   2070 C C   . ASP A 1 302 ? 50.903 36.741  63.598 1.00 39.17  ?  259 ASP A C   1 
ATOM   2071 O O   . ASP A 1 302 ? 50.572 37.875  63.960 1.00 35.26  ?  259 ASP A O   1 
ATOM   2072 C CB  . ASP A 1 302 ? 53.370 36.563  63.623 1.00 38.37  ?  259 ASP A CB  1 
ATOM   2073 C CG  . ASP A 1 302 ? 54.613 36.326  64.450 1.00 56.46  ?  259 ASP A CG  1 
ATOM   2074 O OD1 . ASP A 1 302 ? 54.520 36.313  65.694 1.00 44.01  ?  259 ASP A OD1 1 
ATOM   2075 O OD2 . ASP A 1 302 ? 55.696 36.188  63.828 1.00 53.57  ?  259 ASP A OD2 1 
ATOM   2076 N N   . TYR A 1 303 ? 50.296 36.118  62.568 1.00 32.04  ?  260 TYR A N   1 
ATOM   2077 C CA  . TYR A 1 303 ? 49.215 36.782  61.836 1.00 31.22  ?  260 TYR A CA  1 
ATOM   2078 C C   . TYR A 1 303 ? 47.863 36.742  62.550 1.00 36.72  ?  260 TYR A C   1 
ATOM   2079 O O   . TYR A 1 303 ? 46.885 37.282  62.018 1.00 34.77  ?  260 TYR A O   1 
ATOM   2080 C CB  . TYR A 1 303 ? 49.094 36.194  60.418 1.00 31.89  ?  260 TYR A CB  1 
ATOM   2081 C CG  . TYR A 1 303 ? 50.227 36.709  59.555 1.00 33.04  ?  260 TYR A CG  1 
ATOM   2082 C CD1 . TYR A 1 303 ? 50.144 37.958  58.957 1.00 33.08  ?  260 TYR A CD1 1 
ATOM   2083 C CD2 . TYR A 1 303 ? 51.403 35.976  59.399 1.00 33.83  ?  260 TYR A CD2 1 
ATOM   2084 C CE1 . TYR A 1 303 ? 51.191 38.461  58.179 1.00 34.93  ?  260 TYR A CE1 1 
ATOM   2085 C CE2 . TYR A 1 303 ? 52.459 36.466  58.624 1.00 34.34  ?  260 TYR A CE2 1 
ATOM   2086 C CZ  . TYR A 1 303 ? 52.339 37.709  58.020 1.00 37.40  ?  260 TYR A CZ  1 
ATOM   2087 O OH  . TYR A 1 303 ? 53.371 38.211  57.275 1.00 37.16  ?  260 TYR A OH  1 
ATOM   2088 N N   . ARG A 1 304 ? 47.781 36.146  63.743 1.00 37.68  ?  261 ARG A N   1 
ATOM   2089 C CA  . ARG A 1 304 ? 46.605 36.273  64.606 1.00 38.67  ?  261 ARG A CA  1 
ATOM   2090 C C   . ARG A 1 304 ? 45.355 35.692  63.942 1.00 32.94  ?  261 ARG A C   1 
ATOM   2091 O O   . ARG A 1 304 ? 44.352 36.372  63.707 1.00 37.79  ?  261 ARG A O   1 
ATOM   2092 C CB  . ARG A 1 304 ? 46.400 37.733  65.023 1.00 40.00  ?  261 ARG A CB  1 
ATOM   2093 C CG  . ARG A 1 304 ? 47.551 38.241  65.899 1.00 38.85  ?  261 ARG A CG  1 
ATOM   2094 C CD  . ARG A 1 304 ? 47.353 39.665  66.386 1.00 43.71  ?  261 ARG A CD  1 
ATOM   2095 N NE  . ARG A 1 304 ? 48.440 40.066  67.277 1.00 53.37  ?  261 ARG A NE  1 
ATOM   2096 C CZ  . ARG A 1 304 ? 48.639 41.309  67.711 1.00 61.33  ?  261 ARG A CZ  1 
ATOM   2097 N NH1 . ARG A 1 304 ? 47.825 42.295  67.335 1.00 57.85  ?  261 ARG A NH1 1 
ATOM   2098 N NH2 . ARG A 1 304 ? 49.661 41.568  68.519 1.00 60.16  ?  261 ARG A NH2 1 
ATOM   2099 N N   . PHE A 1 305 ? 45.438 34.401  63.654 1.00 35.02  ?  262 PHE A N   1 
ATOM   2100 C CA  . PHE A 1 305 ? 44.295 33.664  63.144 1.00 32.56  ?  262 PHE A CA  1 
ATOM   2101 C C   . PHE A 1 305 ? 43.239 33.491  64.226 1.00 39.72  ?  262 PHE A C   1 
ATOM   2102 O O   . PHE A 1 305 ? 43.549 33.436  65.418 1.00 34.68  ?  262 PHE A O   1 
ATOM   2103 C CB  . PHE A 1 305 ? 44.738 32.295  62.648 1.00 37.65  ?  262 PHE A CB  1 
ATOM   2104 C CG  . PHE A 1 305 ? 45.616 32.366  61.438 1.00 32.63  ?  262 PHE A CG  1 
ATOM   2105 C CD1 . PHE A 1 305 ? 46.980 32.528  61.577 1.00 35.18  ?  262 PHE A CD1 1 
ATOM   2106 C CD2 . PHE A 1 305 ? 45.069 32.308  60.170 1.00 43.48  ?  262 PHE A CD2 1 
ATOM   2107 C CE1 . PHE A 1 305 ? 47.803 32.615  60.470 1.00 37.49  ?  262 PHE A CE1 1 
ATOM   2108 C CE2 . PHE A 1 305 ? 45.888 32.387  59.056 1.00 35.24  ?  262 PHE A CE2 1 
ATOM   2109 C CZ  . PHE A 1 305 ? 47.255 32.551  59.218 1.00 34.81  ?  262 PHE A CZ  1 
ATOM   2110 N N   . SER A 1 306 ? 41.986 33.400  63.793 1.00 38.36  ?  263 SER A N   1 
ATOM   2111 C CA  . SER A 1 306 ? 40.924 32.984  64.696 1.00 45.82  ?  263 SER A CA  1 
ATOM   2112 C C   . SER A 1 306 ? 41.127 31.528  65.104 1.00 42.47  ?  263 SER A C   1 
ATOM   2113 O O   . SER A 1 306 ? 41.799 30.752  64.422 1.00 35.84  ?  263 SER A O   1 
ATOM   2114 C CB  . SER A 1 306 ? 39.561 33.141  64.028 1.00 39.79  ?  263 SER A CB  1 
ATOM   2115 O OG  . SER A 1 306 ? 39.430 32.232  62.946 1.00 45.29  ?  263 SER A OG  1 
ATOM   2116 N N   . ASN A 1 307 ? 40.526 31.147  66.236 1.00 42.21  ?  264 ASN A N   1 
ATOM   2117 C CA  . ASN A 1 307 ? 40.615 29.747  66.634 1.00 42.60  ?  264 ASN A CA  1 
ATOM   2118 C C   . ASN A 1 307 ? 40.063 28.833  65.550 1.00 38.12  ?  264 ASN A C   1 
ATOM   2119 O O   . ASN A 1 307 ? 40.583 27.732  65.345 1.00 38.56  ?  264 ASN A O   1 
ATOM   2120 C CB  . ASN A 1 307 ? 39.886 29.528  67.961 1.00 45.60  ?  264 ASN A CB  1 
ATOM   2121 C CG  . ASN A 1 307 ? 40.629 30.134  69.128 1.00 52.86  ?  264 ASN A CG  1 
ATOM   2122 O OD1 . ASN A 1 307 ? 41.866 30.121  69.172 1.00 54.29  ?  264 ASN A OD1 1 
ATOM   2123 N ND2 . ASN A 1 307 ? 39.885 30.674  70.080 1.00 59.72  ?  264 ASN A ND2 1 
ATOM   2124 N N   . GLU A 1 308 ? 39.034 29.288  64.827 1.00 37.95  ?  265 GLU A N   1 
ATOM   2125 C CA  . GLU A 1 308 ? 38.431 28.482  63.775 1.00 44.70  ?  265 GLU A CA  1 
ATOM   2126 C C   . GLU A 1 308 ? 39.392 28.303  62.600 1.00 45.48  ?  265 GLU A C   1 
ATOM   2127 O O   . GLU A 1 308 ? 39.562 27.189  62.084 1.00 41.49  ?  265 GLU A O   1 
ATOM   2128 C CB  . GLU A 1 308 ? 37.119 29.129  63.313 1.00 49.63  ?  265 GLU A CB  1 
ATOM   2129 C CG  . GLU A 1 308 ? 36.028 29.235  64.406 1.00 57.95  ?  265 GLU A CG  1 
ATOM   2130 C CD  . GLU A 1 308 ? 36.385 30.189  65.555 1.00 65.16  ?  265 GLU A CD  1 
ATOM   2131 O OE1 . GLU A 1 308 ? 37.073 31.215  65.317 1.00 51.31  ?  265 GLU A OE1 1 
ATOM   2132 O OE2 . GLU A 1 308 ? 35.980 29.906  66.711 1.00 68.73  ?  265 GLU A OE2 1 
ATOM   2133 N N   . GLU A 1 309 ? 40.026 29.390  62.159 1.00 40.57  ?  266 GLU A N   1 
ATOM   2134 C CA  . GLU A 1 309 ? 41.011 29.272  61.084 1.00 40.25  ?  266 GLU A CA  1 
ATOM   2135 C C   . GLU A 1 309 ? 42.180 28.405  61.518 1.00 37.89  ?  266 GLU A C   1 
ATOM   2136 O O   . GLU A 1 309 ? 42.638 27.532  60.772 1.00 36.08  ?  266 GLU A O   1 
ATOM   2137 C CB  . GLU A 1 309 ? 41.538 30.642  60.676 1.00 40.38  ?  266 GLU A CB  1 
ATOM   2138 C CG  . GLU A 1 309 ? 40.543 31.666  60.242 1.00 53.81  ?  266 GLU A CG  1 
ATOM   2139 C CD  . GLU A 1 309 ? 41.244 32.990  59.993 1.00 58.11  ?  266 GLU A CD  1 
ATOM   2140 O OE1 . GLU A 1 309 ? 41.392 33.791  60.955 1.00 44.40  ?  266 GLU A OE1 1 
ATOM   2141 O OE2 . GLU A 1 309 ? 41.701 33.187  58.845 1.00 54.16  ?  266 GLU A OE2 1 
ATOM   2142 N N   . LYS A 1 310 ? 42.699 28.657  62.723 1.00 34.57  ?  267 LYS A N   1 
ATOM   2143 C CA  . LYS A 1 310 ? 43.828 27.879  63.216 1.00 31.56  ?  267 LYS A CA  1 
ATOM   2144 C C   . LYS A 1 310 ? 43.496 26.393  63.239 1.00 40.34  ?  267 LYS A C   1 
ATOM   2145 O O   . LYS A 1 310 ? 44.329 25.557  62.867 1.00 34.79  ?  267 LYS A O   1 
ATOM   2146 C CB  . LYS A 1 310 ? 44.230 28.378  64.608 1.00 33.46  ?  267 LYS A CB  1 
ATOM   2147 C CG  . LYS A 1 310 ? 45.089 27.404  65.405 1.00 38.02  ?  267 LYS A CG  1 
ATOM   2148 C CD  . LYS A 1 310 ? 45.457 28.011  66.766 1.00 38.78  ?  267 LYS A CD  1 
ATOM   2149 C CE  . LYS A 1 310 ? 46.171 27.002  67.659 1.00 48.74  ?  267 LYS A CE  1 
ATOM   2150 N NZ  . LYS A 1 310 ? 46.577 27.606  68.966 1.00 45.06  ?  267 LYS A NZ  1 
ATOM   2151 N N   . ARG A 1 311 ? 42.276 26.043  63.664 1.00 41.36  ?  268 ARG A N   1 
ATOM   2152 C CA  . ARG A 1 311 ? 41.891 24.637  63.711 1.00 37.63  ?  268 ARG A CA  1 
ATOM   2153 C C   . ARG A 1 311 ? 41.875 24.026  62.315 1.00 36.92  ?  268 ARG A C   1 
ATOM   2154 O O   . ARG A 1 311 ? 42.395 22.927  62.105 1.00 36.62  ?  268 ARG A O   1 
ATOM   2155 C CB  . ARG A 1 311 ? 40.522 24.476  64.371 1.00 43.06  ?  268 ARG A CB  1 
ATOM   2156 C CG  . ARG A 1 311 ? 40.269 23.050  64.852 1.00 45.03  ?  268 ARG A CG  1 
ATOM   2157 C CD  . ARG A 1 311 ? 38.848 22.838  65.384 1.00 38.76  ?  268 ARG A CD  1 
ATOM   2158 N NE  . ARG A 1 311 ? 38.703 21.482  65.896 1.00 38.78  ?  268 ARG A NE  1 
ATOM   2159 C CZ  . ARG A 1 311 ? 39.051 21.116  67.127 1.00 47.97  ?  268 ARG A CZ  1 
ATOM   2160 N NH1 . ARG A 1 311 ? 39.547 22.019  67.962 1.00 43.72  ?  268 ARG A NH1 1 
ATOM   2161 N NH2 . ARG A 1 311 ? 38.908 19.853  67.518 1.00 43.71  ?  268 ARG A NH2 1 
ATOM   2162 N N   . LEU A 1 312 ? 41.254 24.717  61.356 1.00 36.89  ?  269 LEU A N   1 
ATOM   2163 C CA  . LEU A 1 312 ? 41.225 24.232  59.976 1.00 37.33  ?  269 LEU A CA  1 
ATOM   2164 C C   . LEU A 1 312 ? 42.630 23.934  59.472 1.00 35.73  ?  269 LEU A C   1 
ATOM   2165 O O   . LEU A 1 312 ? 42.886 22.865  58.906 1.00 38.43  ?  269 LEU A O   1 
ATOM   2166 C CB  . LEU A 1 312 ? 40.527 25.254  59.076 1.00 38.70  ?  269 LEU A CB  1 
ATOM   2167 C CG  . LEU A 1 312 ? 40.386 24.857  57.602 1.00 36.15  ?  269 LEU A CG  1 
ATOM   2168 C CD1 . LEU A 1 312 ? 39.776 23.454  57.497 1.00 37.52  ?  269 LEU A CD1 1 
ATOM   2169 C CD2 . LEU A 1 312 ? 39.543 25.876  56.856 1.00 34.98  ?  269 LEU A CD2 1 
ATOM   2170 N N   . ILE A 1 313 ? 43.567 24.857  59.701 1.00 34.87  ?  270 ILE A N   1 
ATOM   2171 C CA  . ILE A 1 313 ? 44.948 24.641  59.267 1.00 37.82  ?  270 ILE A CA  1 
ATOM   2172 C C   . ILE A 1 313 ? 45.573 23.457  60.001 1.00 42.01  ?  270 ILE A C   1 
ATOM   2173 O O   . ILE A 1 313 ? 46.136 22.549  59.380 1.00 35.08  ?  270 ILE A O   1 
ATOM   2174 C CB  . ILE A 1 313 ? 45.777 25.922  59.463 1.00 37.14  ?  270 ILE A CB  1 
ATOM   2175 C CG1 . ILE A 1 313 ? 45.213 27.053  58.609 1.00 35.32  ?  270 ILE A CG1 1 
ATOM   2176 C CG2 . ILE A 1 313 ? 47.247 25.662  59.130 1.00 35.09  ?  270 ILE A CG2 1 
ATOM   2177 C CD1 . ILE A 1 313 ? 45.799 28.417  58.931 1.00 32.99  ?  270 ILE A CD1 1 
ATOM   2178 N N   . GLU A 1 314 ? 45.524 23.464  61.342 1.00 34.09  ?  271 GLU A N   1 
ATOM   2179 C CA  . GLU A 1 314 ? 46.219 22.423  62.094 1.00 32.69  ?  271 GLU A CA  1 
ATOM   2180 C C   . GLU A 1 314 ? 45.664 21.037  61.790 1.00 36.91  ?  271 GLU A C   1 
ATOM   2181 O O   . GLU A 1 314 ? 46.428 20.076  61.632 1.00 35.17  ?  271 GLU A O   1 
ATOM   2182 C CB  . GLU A 1 314 ? 46.129 22.706  63.597 1.00 33.40  ?  271 GLU A CB  1 
ATOM   2183 C CG  . GLU A 1 314 ? 46.980 23.887  64.035 1.00 38.62  ?  271 GLU A CG  1 
ATOM   2184 C CD  . GLU A 1 314 ? 47.023 24.033  65.546 1.00 46.05  ?  271 GLU A CD  1 
ATOM   2185 O OE1 . GLU A 1 314 ? 45.976 23.818  66.197 1.00 38.43  ?  271 GLU A OE1 1 
ATOM   2186 O OE2 . GLU A 1 314 ? 48.110 24.349  66.070 1.00 48.81  ?  271 GLU A OE2 1 
ATOM   2187 N N   . LYS A 1 315 ? 44.336 20.902  61.723 1.00 34.68  ?  272 LYS A N   1 
ATOM   2188 C CA  . LYS A 1 315 ? 43.767 19.583  61.465 1.00 36.97  ?  272 LYS A CA  1 
ATOM   2189 C C   . LYS A 1 315 ? 44.046 19.143  60.023 1.00 39.85  ?  272 LYS A C   1 
ATOM   2190 O O   . LYS A 1 315 ? 44.341 17.969  59.769 1.00 36.53  ?  272 LYS A O   1 
ATOM   2191 C CB  . LYS A 1 315 ? 42.268 19.593  61.777 1.00 32.02  ?  272 LYS A CB  1 
ATOM   2192 C CG  . LYS A 1 315 ? 41.943 20.005  63.258 1.00 34.89  ?  272 LYS A CG  1 
ATOM   2193 C CD  . LYS A 1 315 ? 42.583 19.071  64.292 1.00 38.22  ?  272 LYS A CD  1 
ATOM   2194 C CE  . LYS A 1 315 ? 42.239 19.494  65.745 1.00 36.47  ?  272 LYS A CE  1 
ATOM   2195 N NZ  . LYS A 1 315 ? 42.921 18.614  66.738 1.00 39.43  ?  272 LYS A NZ  1 
ATOM   2196 N N   . SER A 1 316 ? 44.003 20.079  59.076 1.00 34.96  ?  273 SER A N   1 
ATOM   2197 C CA  . SER A 1 316 ? 44.359 19.734  57.694 1.00 37.00  ?  273 SER A CA  1 
ATOM   2198 C C   . SER A 1 316 ? 45.801 19.247  57.594 1.00 40.46  ?  273 SER A C   1 
ATOM   2199 O O   . SER A 1 316 ? 46.077 18.237  56.931 1.00 41.92  ?  273 SER A O   1 
ATOM   2200 C CB  . SER A 1 316 ? 44.123 20.930  56.779 1.00 37.72  ?  273 SER A CB  1 
ATOM   2201 O OG  . SER A 1 316 ? 42.740 21.211  56.691 1.00 41.63  ?  273 SER A OG  1 
ATOM   2202 N N   . LEU A 1 317 ? 46.737 19.943  58.251 1.00 38.76  ?  274 LEU A N   1 
ATOM   2203 C CA  . LEU A 1 317 ? 48.133 19.513  58.218 1.00 38.04  ?  274 LEU A CA  1 
ATOM   2204 C C   . LEU A 1 317 ? 48.305 18.122  58.815 1.00 47.08  ?  274 LEU A C   1 
ATOM   2205 O O   . LEU A 1 317 ? 49.078 17.309  58.289 1.00 40.43  ?  274 LEU A O   1 
ATOM   2206 C CB  . LEU A 1 317 ? 49.027 20.504  58.958 1.00 42.66  ?  274 LEU A CB  1 
ATOM   2207 C CG  . LEU A 1 317 ? 49.546 21.752  58.255 1.00 43.09  ?  274 LEU A CG  1 
ATOM   2208 C CD1 . LEU A 1 317 ? 50.479 22.466  59.194 1.00 49.86  ?  274 LEU A CD1 1 
ATOM   2209 C CD2 . LEU A 1 317 ? 50.258 21.408  56.938 1.00 42.23  ?  274 LEU A CD2 1 
ATOM   2210 N N   . GLU A 1 318 ? 47.621 17.840  59.935 1.00 43.67  ?  275 GLU A N   1 
ATOM   2211 C CA  . GLU A 1 318 ? 47.648 16.494  60.508 1.00 44.07  ?  275 GLU A CA  1 
ATOM   2212 C C   . GLU A 1 318 ? 47.278 15.457  59.465 1.00 39.42  ?  275 GLU A C   1 
ATOM   2213 O O   . GLU A 1 318 ? 47.938 14.420  59.336 1.00 40.91  ?  275 GLU A O   1 
ATOM   2214 C CB  . GLU A 1 318 ? 46.676 16.375  61.685 1.00 39.72  ?  275 GLU A CB  1 
ATOM   2215 C CG  . GLU A 1 318 ? 47.097 17.036  62.946 1.00 43.52  ?  275 GLU A CG  1 
ATOM   2216 C CD  . GLU A 1 318 ? 46.109 16.786  64.090 1.00 50.19  ?  275 GLU A CD  1 
ATOM   2217 O OE1 . GLU A 1 318 ? 45.036 16.163  63.865 1.00 40.13  ?  275 GLU A OE1 1 
ATOM   2218 O OE2 . GLU A 1 318 ? 46.409 17.225  65.215 1.00 50.34  ?  275 GLU A OE2 1 
ATOM   2219 N N   . LEU A 1 319 ? 46.192 15.709  58.735 1.00 36.04  ?  276 LEU A N   1 
ATOM   2220 C CA  . LEU A 1 319 ? 45.743 14.746  57.740 1.00 42.86  ?  276 LEU A CA  1 
ATOM   2221 C C   . LEU A 1 319 ? 46.800 14.543  56.661 1.00 47.27  ?  276 LEU A C   1 
ATOM   2222 O O   . LEU A 1 319 ? 46.977 13.423  56.162 1.00 45.84  ?  276 LEU A O   1 
ATOM   2223 C CB  . LEU A 1 319 ? 44.423 15.205  57.131 1.00 37.18  ?  276 LEU A CB  1 
ATOM   2224 C CG  . LEU A 1 319 ? 43.198 15.093  58.051 1.00 38.32  ?  276 LEU A CG  1 
ATOM   2225 C CD1 . LEU A 1 319 ? 42.033 15.875  57.484 1.00 34.67  ?  276 LEU A CD1 1 
ATOM   2226 C CD2 . LEU A 1 319 ? 42.803 13.637  58.249 1.00 38.60  ?  276 LEU A CD2 1 
ATOM   2227 N N   . THR A 1 320 ? 47.535 15.603  56.302 1.00 43.13  ?  277 THR A N   1 
ATOM   2228 C CA  . THR A 1 320 ? 48.530 15.428  55.247 1.00 42.53  ?  277 THR A CA  1 
ATOM   2229 C C   . THR A 1 320 ? 49.679 14.551  55.712 1.00 49.06  ?  277 THR A C   1 
ATOM   2230 O O   . THR A 1 320 ? 50.349 13.934  54.877 1.00 50.78  ?  277 THR A O   1 
ATOM   2231 C CB  . THR A 1 320 ? 49.077 16.770  54.752 1.00 39.99  ?  277 THR A CB  1 
ATOM   2232 O OG1 . THR A 1 320 ? 49.846 17.394  55.781 1.00 40.17  ?  277 THR A OG1 1 
ATOM   2233 C CG2 . THR A 1 320 ? 47.956 17.691  54.317 1.00 41.78  ?  277 THR A CG2 1 
ATOM   2234 N N   . ALA A 1 321 ? 49.913 14.474  57.020 1.00 38.36  ?  278 ALA A N   1 
ATOM   2235 C CA  . ALA A 1 321 ? 50.956 13.623  57.569 1.00 49.61  ?  278 ALA A CA  1 
ATOM   2236 C C   . ALA A 1 321 ? 50.454 12.236  57.950 1.00 52.92  ?  278 ALA A C   1 
ATOM   2237 O O   . ALA A 1 321 ? 51.254 11.403  58.391 1.00 57.49  ?  278 ALA A O   1 
ATOM   2238 C CB  . ALA A 1 321 ? 51.597 14.294  58.787 1.00 42.63  ?  278 ALA A CB  1 
ATOM   2239 N N   . LEU A 1 322 ? 49.157 11.972  57.797 1.00 50.15  ?  279 LEU A N   1 
ATOM   2240 C CA  . LEU A 1 322 ? 48.570 10.685  58.156 1.00 52.48  ?  279 LEU A CA  1 
ATOM   2241 C C   . LEU A 1 322 ? 48.690 9.743   56.966 1.00 56.51  ?  279 LEU A C   1 
ATOM   2242 O O   . LEU A 1 322 ? 48.154 10.023  55.889 1.00 52.66  ?  279 LEU A O   1 
ATOM   2243 C CB  . LEU A 1 322 ? 47.108 10.853  58.571 1.00 48.98  ?  279 LEU A CB  1 
ATOM   2244 C CG  . LEU A 1 322 ? 46.388 9.616   59.110 1.00 56.98  ?  279 LEU A CG  1 
ATOM   2245 C CD1 . LEU A 1 322 ? 47.117 9.039   60.324 1.00 58.65  ?  279 LEU A CD1 1 
ATOM   2246 C CD2 . LEU A 1 322 ? 44.947 9.962   59.457 1.00 43.91  ?  279 LEU A CD2 1 
ATOM   2247 N N   . ASN A 1 323 ? 49.381 8.619   57.162 1.00 55.93  ?  280 ASN A N   1 
ATOM   2248 C CA  . ASN A 1 323 ? 49.734 7.795   56.012 1.00 67.05  ?  280 ASN A CA  1 
ATOM   2249 C C   . ASN A 1 323 ? 48.502 7.171   55.365 1.00 63.84  ?  280 ASN A C   1 
ATOM   2250 O O   . ASN A 1 323 ? 48.403 7.119   54.136 1.00 63.56  ?  280 ASN A O   1 
ATOM   2251 C CB  . ASN A 1 323 ? 50.739 6.721   56.419 1.00 70.88  ?  280 ASN A CB  1 
ATOM   2252 C CG  . ASN A 1 323 ? 51.431 6.104   55.224 1.00 86.60  ?  280 ASN A CG  1 
ATOM   2253 O OD1 . ASN A 1 323 ? 51.431 4.883   55.051 1.00 90.49  ?  280 ASN A OD1 1 
ATOM   2254 N ND2 . ASN A 1 323 ? 52.007 6.950   54.373 1.00 80.87  ?  280 ASN A ND2 1 
ATOM   2255 N N   . THR A 1 324 ? 47.552 6.695   56.163 1.00 64.96  ?  281 THR A N   1 
ATOM   2256 C CA  . THR A 1 324 ? 46.341 6.084   55.627 1.00 62.74  ?  281 THR A CA  1 
ATOM   2257 C C   . THR A 1 324 ? 45.123 6.604   56.373 1.00 46.80  ?  281 THR A C   1 
ATOM   2258 O O   . THR A 1 324 ? 45.110 6.636   57.608 1.00 50.12  ?  281 THR A O   1 
ATOM   2259 C CB  . THR A 1 324 ? 46.402 4.559   55.721 1.00 66.21  ?  281 THR A CB  1 
ATOM   2260 O OG1 . THR A 1 324 ? 46.903 4.194   57.011 1.00 76.38  ?  281 THR A OG1 1 
ATOM   2261 C CG2 . THR A 1 324 ? 47.317 3.993   54.641 1.00 58.47  ?  281 THR A CG2 1 
ATOM   2262 N N   . TRP A 1 325 ? 44.119 7.031   55.612 1.00 48.36  ?  282 TRP A N   1 
ATOM   2263 C CA  . TRP A 1 325 ? 42.839 7.457   56.154 1.00 43.51  ?  282 TRP A CA  1 
ATOM   2264 C C   . TRP A 1 325 ? 41.875 6.278   56.100 1.00 50.09  ?  282 TRP A C   1 
ATOM   2265 O O   . TRP A 1 325 ? 41.812 5.564   55.095 1.00 43.77  ?  282 TRP A O   1 
ATOM   2266 C CB  . TRP A 1 325 ? 42.269 8.635   55.362 1.00 37.99  ?  282 TRP A CB  1 
ATOM   2267 C CG  . TRP A 1 325 ? 43.176 9.839   55.223 1.00 37.36  ?  282 TRP A CG  1 
ATOM   2268 C CD1 . TRP A 1 325 ? 44.440 9.989   55.720 1.00 38.79  ?  282 TRP A CD1 1 
ATOM   2269 C CD2 . TRP A 1 325 ? 42.871 11.062  54.532 1.00 37.95  ?  282 TRP A CD2 1 
ATOM   2270 N NE1 . TRP A 1 325 ? 44.934 11.224  55.386 1.00 41.32  ?  282 TRP A NE1 1 
ATOM   2271 C CE2 . TRP A 1 325 ? 43.993 11.902  54.657 1.00 38.13  ?  282 TRP A CE2 1 
ATOM   2272 C CE3 . TRP A 1 325 ? 41.754 11.526  53.825 1.00 39.56  ?  282 TRP A CE3 1 
ATOM   2273 C CZ2 . TRP A 1 325 ? 44.034 13.184  54.103 1.00 41.80  ?  282 TRP A CZ2 1 
ATOM   2274 C CZ3 . TRP A 1 325 ? 41.795 12.801  53.274 1.00 44.26  ?  282 TRP A CZ3 1 
ATOM   2275 C CH2 . TRP A 1 325 ? 42.931 13.612  53.414 1.00 38.81  ?  282 TRP A CH2 1 
ATOM   2276 N N   . ASP A 1 326 ? 41.142 6.058   57.185 1.00 41.56  ?  283 ASP A N   1 
ATOM   2277 C CA  . ASP A 1 326 ? 40.150 4.992   57.226 1.00 46.53  ?  283 ASP A CA  1 
ATOM   2278 C C   . ASP A 1 326 ? 38.852 5.573   57.795 1.00 42.89  ?  283 ASP A C   1 
ATOM   2279 O O   . ASP A 1 326 ? 38.665 6.795   57.876 1.00 37.88  ?  283 ASP A O   1 
ATOM   2280 C CB  . ASP A 1 326 ? 40.708 3.784   57.999 1.00 41.10  ?  283 ASP A CB  1 
ATOM   2281 C CG  . ASP A 1 326 ? 40.771 4.011   59.502 1.00 45.50  ?  283 ASP A CG  1 
ATOM   2282 O OD1 . ASP A 1 326 ? 40.497 5.150   59.953 1.00 42.80  ?  283 ASP A OD1 1 
ATOM   2283 O OD2 . ASP A 1 326 ? 41.103 3.046   60.238 1.00 44.96  ?  283 ASP A OD2 1 
ATOM   2284 N N   . GLN A 1 327 ? 37.922 4.688   58.167 1.00 42.16  ?  284 GLN A N   1 
ATOM   2285 C CA  . GLN A 1 327 ? 36.605 5.132   58.622 1.00 39.63  ?  284 GLN A CA  1 
ATOM   2286 C C   . GLN A 1 327 ? 36.722 6.075   59.812 1.00 33.78  ?  284 GLN A C   1 
ATOM   2287 O O   . GLN A 1 327 ? 35.939 7.023   59.941 1.00 36.35  ?  284 GLN A O   1 
ATOM   2288 C CB  . GLN A 1 327 ? 35.732 3.929   58.991 1.00 32.78  ?  284 GLN A CB  1 
ATOM   2289 C CG  . GLN A 1 327 ? 35.186 3.167   57.786 1.00 43.22  ?  284 GLN A CG  1 
ATOM   2290 C CD  . GLN A 1 327 ? 36.190 2.186   57.197 1.00 41.87  ?  284 GLN A CD  1 
ATOM   2291 O OE1 . GLN A 1 327 ? 37.293 2.002   57.725 1.00 38.21  ?  284 GLN A OE1 1 
ATOM   2292 N NE2 . GLN A 1 327 ? 35.801 1.537   56.100 1.00 46.69  ?  284 GLN A NE2 1 
ATOM   2293 N N   . TRP A 1 328 ? 37.696 5.827   60.686 1.00 36.58  ?  285 TRP A N   1 
ATOM   2294 C CA  . TRP A 1 328 ? 37.849 6.643   61.888 1.00 39.52  ?  285 TRP A CA  1 
ATOM   2295 C C   . TRP A 1 328 ? 38.391 8.024   61.536 1.00 40.60  ?  285 TRP A C   1 
ATOM   2296 O O   . TRP A 1 328 ? 38.010 9.027   62.150 1.00 36.19  ?  285 TRP A O   1 
ATOM   2297 C CB  . TRP A 1 328 ? 38.756 5.920   62.883 1.00 34.15  ?  285 TRP A CB  1 
ATOM   2298 C CG  . TRP A 1 328 ? 38.822 6.562   64.237 1.00 40.87  ?  285 TRP A CG  1 
ATOM   2299 C CD1 . TRP A 1 328 ? 39.891 7.204   64.793 1.00 39.54  ?  285 TRP A CD1 1 
ATOM   2300 C CD2 . TRP A 1 328 ? 37.765 6.626   65.201 1.00 37.28  ?  285 TRP A CD2 1 
ATOM   2301 N NE1 . TRP A 1 328 ? 39.562 7.666   66.053 1.00 36.55  ?  285 TRP A NE1 1 
ATOM   2302 C CE2 . TRP A 1 328 ? 38.263 7.320   66.324 1.00 40.37  ?  285 TRP A CE2 1 
ATOM   2303 C CE3 . TRP A 1 328 ? 36.446 6.163   65.220 1.00 37.29  ?  285 TRP A CE3 1 
ATOM   2304 C CZ2 . TRP A 1 328 ? 37.485 7.559   67.464 1.00 39.06  ?  285 TRP A CZ2 1 
ATOM   2305 C CZ3 . TRP A 1 328 ? 35.676 6.394   66.349 1.00 39.53  ?  285 TRP A CZ3 1 
ATOM   2306 C CH2 . TRP A 1 328 ? 36.197 7.089   67.456 1.00 34.80  ?  285 TRP A CH2 1 
ATOM   2307 N N   . THR A 1 329 ? 39.257 8.094   60.521 1.00 38.94  ?  286 THR A N   1 
ATOM   2308 C CA  . THR A 1 329 ? 39.696 9.382   59.994 1.00 32.90  ?  286 THR A CA  1 
ATOM   2309 C C   . THR A 1 329 ? 38.516 10.198  59.490 1.00 35.60  ?  286 THR A C   1 
ATOM   2310 O O   . THR A 1 329 ? 38.371 11.378  59.826 1.00 32.41  ?  286 THR A O   1 
ATOM   2311 C CB  . THR A 1 329 ? 40.688 9.169   58.840 1.00 40.79  ?  286 THR A CB  1 
ATOM   2312 O OG1 . THR A 1 329 ? 41.714 8.249   59.234 1.00 36.91  ?  286 THR A OG1 1 
ATOM   2313 C CG2 . THR A 1 329 ? 41.304 10.494  58.426 1.00 36.35  ?  286 THR A CG2 1 
ATOM   2314 N N   . PHE A 1 330 ? 37.695 9.600   58.619 1.00 33.14  ?  287 PHE A N   1 
ATOM   2315 C CA  . PHE A 1 330 ? 36.574 10.332  58.038 1.00 35.00  ?  287 PHE A CA  1 
ATOM   2316 C C   . PHE A 1 330 ? 35.530 10.684  59.086 1.00 34.16  ?  287 PHE A C   1 
ATOM   2317 O O   . PHE A 1 330 ? 34.823 11.686  58.939 1.00 34.18  ?  287 PHE A O   1 
ATOM   2318 C CB  . PHE A 1 330 ? 35.936 9.520   56.917 1.00 39.46  ?  287 PHE A CB  1 
ATOM   2319 C CG  . PHE A 1 330 ? 36.682 9.617   55.617 1.00 38.97  ?  287 PHE A CG  1 
ATOM   2320 C CD1 . PHE A 1 330 ? 37.802 8.838   55.387 1.00 41.05  ?  287 PHE A CD1 1 
ATOM   2321 C CD2 . PHE A 1 330 ? 36.276 10.510  54.643 1.00 36.57  ?  287 PHE A CD2 1 
ATOM   2322 C CE1 . PHE A 1 330 ? 38.498 8.935   54.182 1.00 35.56  ?  287 PHE A CE1 1 
ATOM   2323 C CE2 . PHE A 1 330 ? 36.968 10.613  53.446 1.00 40.41  ?  287 PHE A CE2 1 
ATOM   2324 C CZ  . PHE A 1 330 ? 38.081 9.826   53.227 1.00 39.04  ?  287 PHE A CZ  1 
ATOM   2325 N N   . TYR A 1 331 ? 35.413 9.864   60.125 1.00 36.20  ?  288 TYR A N   1 
ATOM   2326 C CA  . TYR A 1 331 ? 34.453 10.130  61.192 1.00 34.38  ?  288 TYR A CA  1 
ATOM   2327 C C   . TYR A 1 331 ? 34.867 11.346  62.013 1.00 37.50  ?  288 TYR A C   1 
ATOM   2328 O O   . TYR A 1 331 ? 34.056 12.251  62.249 1.00 39.27  ?  288 TYR A O   1 
ATOM   2329 C CB  . TYR A 1 331 ? 34.334 8.897   62.083 1.00 36.27  ?  288 TYR A CB  1 
ATOM   2330 C CG  . TYR A 1 331 ? 33.445 9.066   63.305 1.00 36.43  ?  288 TYR A CG  1 
ATOM   2331 C CD1 . TYR A 1 331 ? 32.062 9.132   63.178 1.00 33.78  ?  288 TYR A CD1 1 
ATOM   2332 C CD2 . TYR A 1 331 ? 33.993 9.126   64.576 1.00 34.85  ?  288 TYR A CD2 1 
ATOM   2333 C CE1 . TYR A 1 331 ? 31.238 9.256   64.306 1.00 35.85  ?  288 TYR A CE1 1 
ATOM   2334 C CE2 . TYR A 1 331 ? 33.177 9.251   65.714 1.00 33.86  ?  288 TYR A CE2 1 
ATOM   2335 C CZ  . TYR A 1 331 ? 31.811 9.319   65.566 1.00 38.97  ?  288 TYR A CZ  1 
ATOM   2336 O OH  . TYR A 1 331 ? 31.006 9.450   66.685 1.00 36.33  ?  288 TYR A OH  1 
ATOM   2337 N N   . LYS A 1 332 ? 36.132 11.387  62.445 1.00 34.10  ?  289 LYS A N   1 
ATOM   2338 C CA  . LYS A 1 332 ? 36.595 12.336  63.463 1.00 36.22  ?  289 LYS A CA  1 
ATOM   2339 C C   . LYS A 1 332 ? 36.959 13.701  62.896 1.00 41.63  ?  289 LYS A C   1 
ATOM   2340 O O   . LYS A 1 332 ? 36.797 14.713  63.590 1.00 35.23  ?  289 LYS A O   1 
ATOM   2341 C CB  . LYS A 1 332 ? 37.806 11.769  64.219 1.00 32.98  ?  289 LYS A CB  1 
ATOM   2342 C CG  . LYS A 1 332 ? 37.498 10.573  65.113 1.00 39.13  ?  289 LYS A CG  1 
ATOM   2343 C CD  . LYS A 1 332 ? 36.600 10.941  66.320 1.00 36.01  ?  289 LYS A CD  1 
ATOM   2344 C CE  . LYS A 1 332 ? 37.355 11.722  67.392 1.00 40.48  ?  289 LYS A CE  1 
ATOM   2345 N NZ  . LYS A 1 332 ? 36.463 12.029  68.564 1.00 39.68  ?  289 LYS A NZ  1 
ATOM   2346 N N   . TYR A 1 333 ? 37.457 13.760  61.662 1.00 35.50  ?  290 TYR A N   1 
ATOM   2347 C CA  . TYR A 1 333 ? 37.778 15.027  61.026 1.00 36.73  ?  290 TYR A CA  1 
ATOM   2348 C C   . TYR A 1 333 ? 36.568 15.576  60.276 1.00 35.37  ?  290 TYR A C   1 
ATOM   2349 O O   . TYR A 1 333 ? 35.666 14.839  59.872 1.00 38.00  ?  290 TYR A O   1 
ATOM   2350 C CB  . TYR A 1 333 ? 38.955 14.862  60.064 1.00 33.97  ?  290 TYR A CB  1 
ATOM   2351 C CG  . TYR A 1 333 ? 40.271 14.645  60.748 1.00 35.58  ?  290 TYR A CG  1 
ATOM   2352 C CD1 . TYR A 1 333 ? 40.649 13.381  61.185 1.00 33.12  ?  290 TYR A CD1 1 
ATOM   2353 C CD2 . TYR A 1 333 ? 41.138 15.710  60.984 1.00 34.25  ?  290 TYR A CD2 1 
ATOM   2354 C CE1 . TYR A 1 333 ? 41.852 13.180  61.809 1.00 36.27  ?  290 TYR A CE1 1 
ATOM   2355 C CE2 . TYR A 1 333 ? 42.345 15.513  61.613 1.00 32.34  ?  290 TYR A CE2 1 
ATOM   2356 C CZ  . TYR A 1 333 ? 42.695 14.244  62.021 1.00 33.20  ?  290 TYR A CZ  1 
ATOM   2357 O OH  . TYR A 1 333 ? 43.893 14.037  62.642 1.00 36.57  ?  290 TYR A OH  1 
ATOM   2358 N N   . THR A 1 334 ? 36.565 16.891  60.081 1.00 35.79  ?  291 THR A N   1 
ATOM   2359 C CA  . THR A 1 334 ? 35.480 17.515  59.354 1.00 32.29  ?  291 THR A CA  1 
ATOM   2360 C C   . THR A 1 334 ? 35.706 17.366  57.850 1.00 38.69  ?  291 THR A C   1 
ATOM   2361 O O   . THR A 1 334 ? 36.821 17.115  57.376 1.00 35.69  ?  291 THR A O   1 
ATOM   2362 C CB  . THR A 1 334 ? 35.345 18.998  59.706 1.00 38.70  ?  291 THR A CB  1 
ATOM   2363 O OG1 . THR A 1 334 ? 36.440 19.729  59.153 1.00 36.39  ?  291 THR A OG1 1 
ATOM   2364 C CG2 . THR A 1 334 ? 35.351 19.193  61.236 1.00 38.91  ?  291 THR A CG2 1 
ATOM   2365 N N   . LEU A 1 335 ? 34.613 17.505  57.105 1.00 35.63  ?  292 LEU A N   1 
ATOM   2366 C CA  . LEU A 1 335 ? 34.691 17.372  55.654 1.00 38.32  ?  292 LEU A CA  1 
ATOM   2367 C C   . LEU A 1 335 ? 35.553 18.476  55.043 1.00 39.78  ?  292 LEU A C   1 
ATOM   2368 O O   . LEU A 1 335 ? 36.316 18.235  54.097 1.00 42.66  ?  292 LEU A O   1 
ATOM   2369 C CB  . LEU A 1 335 ? 33.281 17.391  55.066 1.00 34.88  ?  292 LEU A CB  1 
ATOM   2370 C CG  . LEU A 1 335 ? 33.213 17.291  53.541 1.00 35.41  ?  292 LEU A CG  1 
ATOM   2371 C CD1 . LEU A 1 335 ? 33.904 16.012  53.111 1.00 39.16  ?  292 LEU A CD1 1 
ATOM   2372 C CD2 . LEU A 1 335 ? 31.766 17.315  53.096 1.00 40.01  ?  292 LEU A CD2 1 
ATOM   2373 N N   . LYS A 1 336 ? 35.447 19.697  55.567 1.00 35.83  ?  293 LYS A N   1 
ATOM   2374 C CA  . LYS A 1 336 ? 36.306 20.773  55.084 1.00 40.69  ?  293 LYS A CA  1 
ATOM   2375 C C   . LYS A 1 336 ? 37.784 20.466  55.334 1.00 40.58  ?  293 LYS A C   1 
ATOM   2376 O O   . LYS A 1 336 ? 38.642 20.784  54.502 1.00 39.36  ?  293 LYS A O   1 
ATOM   2377 C CB  . LYS A 1 336 ? 35.891 22.095  55.731 1.00 39.74  ?  293 LYS A CB  1 
ATOM   2378 C CG  . LYS A 1 336 ? 36.718 23.275  55.293 1.00 49.99  ?  293 LYS A CG  1 
ATOM   2379 C CD  . LYS A 1 336 ? 35.870 24.540  55.148 1.00 56.16  ?  293 LYS A CD  1 
ATOM   2380 C CE  . LYS A 1 336 ? 35.517 25.157  56.493 1.00 68.10  ?  293 LYS A CE  1 
ATOM   2381 N NZ  . LYS A 1 336 ? 34.999 26.553  56.346 1.00 72.19  ?  293 LYS A NZ  1 
ATOM   2382 N N   . GLN A 1 337 ? 38.103 19.828  56.462 1.00 37.03  ?  294 GLN A N   1 
ATOM   2383 C CA  . GLN A 1 337 ? 39.489 19.444  56.733 1.00 36.08  ?  294 GLN A CA  1 
ATOM   2384 C C   . GLN A 1 337 ? 39.971 18.357  55.776 1.00 40.51  ?  294 GLN A C   1 
ATOM   2385 O O   . GLN A 1 337 ? 41.071 18.450  55.216 1.00 38.22  ?  294 GLN A O   1 
ATOM   2386 C CB  . GLN A 1 337 ? 39.627 18.967  58.178 1.00 34.85  ?  294 GLN A CB  1 
ATOM   2387 C CG  . GLN A 1 337 ? 39.441 20.090  59.182 1.00 35.87  ?  294 GLN A CG  1 
ATOM   2388 C CD  . GLN A 1 337 ? 39.134 19.586  60.589 1.00 38.18  ?  294 GLN A CD  1 
ATOM   2389 O OE1 . GLN A 1 337 ? 39.159 18.379  60.856 1.00 35.56  ?  294 GLN A OE1 1 
ATOM   2390 N NE2 . GLN A 1 337 ? 38.838 20.519  61.497 1.00 34.19  ?  294 GLN A NE2 1 
ATOM   2391 N N   . LEU A 1 338 ? 39.183 17.294  55.613 1.00 36.43  ?  295 LEU A N   1 
ATOM   2392 C CA  . LEU A 1 338 ? 39.531 16.259  54.644 1.00 37.44  ?  295 LEU A CA  1 
ATOM   2393 C C   . LEU A 1 338 ? 39.697 16.845  53.242 1.00 39.21  ?  295 LEU A C   1 
ATOM   2394 O O   . LEU A 1 338 ? 40.655 16.514  52.534 1.00 40.31  ?  295 LEU A O   1 
ATOM   2395 C CB  . LEU A 1 338 ? 38.460 15.167  54.646 1.00 35.83  ?  295 LEU A CB  1 
ATOM   2396 C CG  . LEU A 1 338 ? 38.288 14.430  55.984 1.00 36.09  ?  295 LEU A CG  1 
ATOM   2397 C CD1 . LEU A 1 338 ? 36.882 13.866  56.142 1.00 35.35  ?  295 LEU A CD1 1 
ATOM   2398 C CD2 . LEU A 1 338 ? 39.311 13.322  56.101 1.00 36.64  ?  295 LEU A CD2 1 
ATOM   2399 N N   . GLU A 1 339 ? 38.780 17.723  52.831 1.00 35.79  ?  296 GLU A N   1 
ATOM   2400 C CA  . GLU A 1 339 ? 38.857 18.307  51.495 1.00 40.20  ?  296 GLU A CA  1 
ATOM   2401 C C   . GLU A 1 339 ? 40.099 19.175  51.338 1.00 46.79  ?  296 GLU A C   1 
ATOM   2402 O O   . GLU A 1 339 ? 40.784 19.105  50.311 1.00 39.76  ?  296 GLU A O   1 
ATOM   2403 C CB  . GLU A 1 339 ? 37.593 19.112  51.201 1.00 38.05  ?  296 GLU A CB  1 
ATOM   2404 C CG  . GLU A 1 339 ? 36.371 18.250  50.950 1.00 44.76  ?  296 GLU A CG  1 
ATOM   2405 C CD  . GLU A 1 339 ? 35.093 19.057  50.733 1.00 51.70  ?  296 GLU A CD  1 
ATOM   2406 O OE1 . GLU A 1 339 ? 35.059 20.256  51.095 1.00 52.88  ?  296 GLU A OE1 1 
ATOM   2407 O OE2 . GLU A 1 339 ? 34.113 18.485  50.204 1.00 56.12  ?  296 GLU A OE2 1 
ATOM   2408 N N   . MET A 1 340 ? 40.425 19.990  52.346 1.00 37.50  ?  297 MET A N   1 
ATOM   2409 C CA  . MET A 1 340 ? 41.597 20.848  52.212 1.00 37.49  ?  297 MET A CA  1 
ATOM   2410 C C   . MET A 1 340 ? 42.883 20.033  52.218 1.00 39.41  ?  297 MET A C   1 
ATOM   2411 O O   . MET A 1 340 ? 43.811 20.322  51.449 1.00 41.09  ?  297 MET A O   1 
ATOM   2412 C CB  . MET A 1 340 ? 41.623 21.905  53.323 1.00 40.14  ?  297 MET A CB  1 
ATOM   2413 C CG  . MET A 1 340 ? 42.706 22.945  53.085 1.00 52.36  ?  297 MET A CG  1 
ATOM   2414 S SD  . MET A 1 340 ? 42.576 24.493  54.010 1.00 50.38  ?  297 MET A SD  1 
ATOM   2415 C CE  . MET A 1 340 ? 40.961 25.055  53.515 1.00 37.58  ?  297 MET A CE  1 
ATOM   2416 N N   . ALA A 1 341 ? 42.967 19.018  53.085 1.00 35.35  ?  298 ALA A N   1 
ATOM   2417 C CA  . ALA A 1 341 ? 44.129 18.140  53.062 1.00 34.57  ?  298 ALA A CA  1 
ATOM   2418 C C   . ALA A 1 341 ? 44.243 17.421  51.719 1.00 37.00  ?  298 ALA A C   1 
ATOM   2419 O O   . ALA A 1 341 ? 45.342 17.302  51.166 1.00 40.84  ?  298 ALA A O   1 
ATOM   2420 C CB  . ALA A 1 341 ? 44.058 17.125  54.198 1.00 39.03  ?  298 ALA A CB  1 
ATOM   2421 N N   . SER A 1 342 ? 43.124 16.918  51.191 1.00 40.04  ?  299 SER A N   1 
ATOM   2422 C CA  . SER A 1 342 ? 43.166 16.268  49.878 1.00 43.29  ?  299 SER A CA  1 
ATOM   2423 C C   . SER A 1 342 ? 43.629 17.237  48.799 1.00 49.77  ?  299 SER A C   1 
ATOM   2424 O O   . SER A 1 342 ? 44.424 16.874  47.923 1.00 47.97  ?  299 SER A O   1 
ATOM   2425 C CB  . SER A 1 342 ? 41.795 15.703  49.507 1.00 42.94  ?  299 SER A CB  1 
ATOM   2426 O OG  . SER A 1 342 ? 41.410 14.669  50.398 1.00 51.18  ?  299 SER A OG  1 
ATOM   2427 N N   . ARG A 1 343 ? 43.140 18.475  48.846 1.00 44.79  ?  300 ARG A N   1 
ATOM   2428 C CA  . ARG A 1 343 ? 43.486 19.445  47.815 1.00 42.83  ?  300 ARG A CA  1 
ATOM   2429 C C   . ARG A 1 343 ? 44.982 19.729  47.813 1.00 46.95  ?  300 ARG A C   1 
ATOM   2430 O O   . ARG A 1 343 ? 45.611 19.779  46.749 1.00 46.16  ?  300 ARG A O   1 
ATOM   2431 C CB  . ARG A 1 343 ? 42.679 20.731  48.018 1.00 38.84  ?  300 ARG A CB  1 
ATOM   2432 C CG  . ARG A 1 343 ? 42.881 21.769  46.941 1.00 41.98  ?  300 ARG A CG  1 
ATOM   2433 C CD  . ARG A 1 343 ? 42.087 23.032  47.212 1.00 38.53  ?  300 ARG A CD  1 
ATOM   2434 N NE  . ARG A 1 343 ? 42.089 23.860  46.015 1.00 43.40  ?  300 ARG A NE  1 
ATOM   2435 C CZ  . ARG A 1 343 ? 41.182 23.771  45.047 1.00 54.84  ?  300 ARG A CZ  1 
ATOM   2436 N NH1 . ARG A 1 343 ? 40.183 22.900  45.152 1.00 40.69  ?  300 ARG A NH1 1 
ATOM   2437 N NH2 . ARG A 1 343 ? 41.279 24.547  43.969 1.00 42.10  ?  300 ARG A NH2 1 
ATOM   2438 N N   . VAL A 1 344 ? 45.582 19.890  48.992 1.00 38.50  ?  301 VAL A N   1 
ATOM   2439 C CA  . VAL A 1 344 ? 46.992 20.263  49.038 1.00 43.13  ?  301 VAL A CA  1 
ATOM   2440 C C   . VAL A 1 344 ? 47.918 19.079  48.772 1.00 50.97  ?  301 VAL A C   1 
ATOM   2441 O O   . VAL A 1 344 ? 49.104 19.289  48.485 1.00 44.28  ?  301 VAL A O   1 
ATOM   2442 C CB  . VAL A 1 344 ? 47.342 20.935  50.380 1.00 49.10  ?  301 VAL A CB  1 
ATOM   2443 C CG1 . VAL A 1 344 ? 47.539 19.897  51.475 1.00 40.80  ?  301 VAL A CG1 1 
ATOM   2444 C CG2 . VAL A 1 344 ? 48.584 21.817  50.237 1.00 42.74  ?  301 VAL A CG2 1 
ATOM   2445 N N   . THR A 1 345 ? 47.423 17.842  48.852 1.00 42.33  ?  302 THR A N   1 
ATOM   2446 C CA  . THR A 1 345 ? 48.228 16.668  48.534 1.00 49.89  ?  302 THR A CA  1 
ATOM   2447 C C   . THR A 1 345 ? 47.914 16.094  47.156 1.00 52.52  ?  302 THR A C   1 
ATOM   2448 O O   . THR A 1 345 ? 48.540 15.107  46.760 1.00 51.83  ?  302 THR A O   1 
ATOM   2449 C CB  . THR A 1 345 ? 48.034 15.559  49.574 1.00 46.50  ?  302 THR A CB  1 
ATOM   2450 O OG1 . THR A 1 345 ? 46.671 15.125  49.556 1.00 48.15  ?  302 THR A OG1 1 
ATOM   2451 C CG2 . THR A 1 345 ? 48.421 16.032  50.978 1.00 50.82  ?  302 THR A CG2 1 
ATOM   2452 N N   . GLY A 1 346 ? 46.939 16.657  46.443 1.00 50.54  ?  303 GLY A N   1 
ATOM   2453 C CA  . GLY A 1 346 ? 46.623 16.234  45.093 1.00 56.37  ?  303 GLY A CA  1 
ATOM   2454 C C   . GLY A 1 346 ? 45.555 15.165  44.949 1.00 67.30  ?  303 GLY A C   1 
ATOM   2455 O O   . GLY A 1 346 ? 45.224 14.805  43.810 1.00 66.31  ?  303 GLY A O   1 
ATOM   2456 N N   . LYS A 1 347 ? 45.009 14.634  46.046 1.00 57.51  ?  304 LYS A N   1 
ATOM   2457 C CA  . LYS A 1 347 ? 44.000 13.586  45.923 1.00 63.01  ?  304 LYS A CA  1 
ATOM   2458 C C   . LYS A 1 347 ? 42.710 14.146  45.327 1.00 71.36  ?  304 LYS A C   1 
ATOM   2459 O O   . LYS A 1 347 ? 42.445 15.352  45.360 1.00 66.20  ?  304 LYS A O   1 
ATOM   2460 C CB  . LYS A 1 347 ? 43.692 12.937  47.275 1.00 66.01  ?  304 LYS A CB  1 
ATOM   2461 C CG  . LYS A 1 347 ? 44.905 12.483  48.068 1.00 65.96  ?  304 LYS A CG  1 
ATOM   2462 C CD  . LYS A 1 347 ? 46.016 11.959  47.182 1.00 58.81  ?  304 LYS A CD  1 
ATOM   2463 C CE  . LYS A 1 347 ? 47.225 11.589  48.033 1.00 58.61  ?  304 LYS A CE  1 
ATOM   2464 N NZ  . LYS A 1 347 ? 48.482 11.576  47.232 1.00 70.14  ?  304 LYS A NZ  1 
ATOM   2465 N N   . LYS A 1 348 ? 41.893 13.239  44.776 1.00 69.91  ?  305 LYS A N   1 
ATOM   2466 C CA  . LYS A 1 348 ? 40.645 13.647  44.142 1.00 73.72  ?  305 LYS A CA  1 
ATOM   2467 C C   . LYS A 1 348 ? 39.471 12.752  44.538 1.00 82.44  ?  305 LYS A C   1 
ATOM   2468 O O   . LYS A 1 348 ? 38.487 12.674  43.790 1.00 81.98  ?  305 LYS A O   1 
ATOM   2469 C CB  . LYS A 1 348 ? 40.788 13.649  42.614 1.00 78.45  ?  305 LYS A CB  1 
ATOM   2470 C CG  . LYS A 1 348 ? 42.172 14.041  42.094 1.00 80.61  ?  305 LYS A CG  1 
ATOM   2471 C CD  . LYS A 1 348 ? 42.378 15.552  42.049 1.00 84.16  ?  305 LYS A CD  1 
ATOM   2472 C CE  . LYS A 1 348 ? 43.657 15.906  41.287 1.00 77.42  ?  305 LYS A CE  1 
ATOM   2473 N NZ  . LYS A 1 348 ? 43.897 17.379  41.207 1.00 74.86  ?  305 LYS A NZ  1 
ATOM   2474 N N   . LYS A 1 349 ? 39.537 12.084  45.688 1.00 75.85  ?  306 LYS A N   1 
ATOM   2475 C CA  . LYS A 1 349 ? 38.470 11.173  46.076 1.00 66.67  ?  306 LYS A CA  1 
ATOM   2476 C C   . LYS A 1 349 ? 37.158 11.924  46.306 1.00 60.66  ?  306 LYS A C   1 
ATOM   2477 O O   . LYS A 1 349 ? 37.116 13.152  46.425 1.00 60.74  ?  306 LYS A O   1 
ATOM   2478 C CB  . LYS A 1 349 ? 38.857 10.399  47.336 1.00 67.18  ?  306 LYS A CB  1 
ATOM   2479 C CG  . LYS A 1 349 ? 40.086 9.527   47.169 1.00 66.93  ?  306 LYS A CG  1 
ATOM   2480 C CD  . LYS A 1 349 ? 40.692 9.143   48.513 1.00 74.21  ?  306 LYS A CD  1 
ATOM   2481 C CE  . LYS A 1 349 ? 41.478 10.298  49.137 1.00 76.27  ?  306 LYS A CE  1 
ATOM   2482 N NZ  . LYS A 1 349 ? 42.239 9.874   50.355 1.00 64.94  ?  306 LYS A NZ  1 
ATOM   2483 N N   . ASP A 1 350 ? 36.067 11.158  46.363 1.00 60.57  ?  307 ASP A N   1 
ATOM   2484 C CA  . ASP A 1 350 ? 34.755 11.701  46.711 1.00 64.68  ?  307 ASP A CA  1 
ATOM   2485 C C   . ASP A 1 350 ? 34.622 11.620  48.231 1.00 54.70  ?  307 ASP A C   1 
ATOM   2486 O O   . ASP A 1 350 ? 34.046 10.690  48.798 1.00 48.05  ?  307 ASP A O   1 
ATOM   2487 C CB  . ASP A 1 350 ? 33.649 10.940  45.990 1.00 66.13  ?  307 ASP A CB  1 
ATOM   2488 C CG  . ASP A 1 350 ? 32.257 11.490  46.290 1.00 71.92  ?  307 ASP A CG  1 
ATOM   2489 O OD1 . ASP A 1 350 ? 32.130 12.512  47.009 1.00 64.62  ?  307 ASP A OD1 1 
ATOM   2490 O OD2 . ASP A 1 350 ? 31.282 10.882  45.798 1.00 76.34  ?  307 ASP A OD2 1 
ATOM   2491 N N   . LEU A 1 351 ? 35.197 12.622  48.897 1.00 57.52  ?  308 LEU A N   1 
ATOM   2492 C CA  . LEU A 1 351 ? 35.266 12.602  50.354 1.00 46.32  ?  308 LEU A CA  1 
ATOM   2493 C C   . LEU A 1 351 ? 33.880 12.671  50.977 1.00 48.30  ?  308 LEU A C   1 
ATOM   2494 O O   . LEU A 1 351 ? 33.593 11.964  51.956 1.00 45.99  ?  308 LEU A O   1 
ATOM   2495 C CB  . LEU A 1 351 ? 36.142 13.757  50.829 1.00 47.95  ?  308 LEU A CB  1 
ATOM   2496 C CG  . LEU A 1 351 ? 37.547 13.671  50.229 1.00 46.96  ?  308 LEU A CG  1 
ATOM   2497 C CD1 . LEU A 1 351 ? 38.330 14.951  50.462 1.00 44.72  ?  308 LEU A CD1 1 
ATOM   2498 C CD2 . LEU A 1 351 ? 38.287 12.466  50.784 1.00 45.58  ?  308 LEU A CD2 1 
ATOM   2499 N N   . ALA A 1 352 ? 33.002 13.509  50.424 1.00 44.66  ?  309 ALA A N   1 
ATOM   2500 C CA  . ALA A 1 352 ? 31.675 13.680  51.007 1.00 47.70  ?  309 ALA A CA  1 
ATOM   2501 C C   . ALA A 1 352 ? 30.915 12.360  51.059 1.00 55.28  ?  309 ALA A C   1 
ATOM   2502 O O   . ALA A 1 352 ? 30.207 12.078  52.035 1.00 47.02  ?  309 ALA A O   1 
ATOM   2503 C CB  . ALA A 1 352 ? 30.885 14.724  50.219 1.00 48.94  ?  309 ALA A CB  1 
ATOM   2504 N N   . ALA A 1 353 ? 31.049 11.535  50.018 1.00 51.14  ?  310 ALA A N   1 
ATOM   2505 C CA  . ALA A 1 353 ? 30.315 10.276  49.976 1.00 49.35  ?  310 ALA A CA  1 
ATOM   2506 C C   . ALA A 1 353 ? 30.855 9.283   50.996 1.00 43.90  ?  310 ALA A C   1 
ATOM   2507 O O   . ALA A 1 353 ? 30.086 8.531   51.608 1.00 48.52  ?  310 ALA A O   1 
ATOM   2508 C CB  . ALA A 1 353 ? 30.371 9.680   48.566 1.00 52.85  ?  310 ALA A CB  1 
ATOM   2509 N N   . ILE A 1 354 ? 32.174 9.259   51.190 1.00 39.80  ?  311 ILE A N   1 
ATOM   2510 C CA  . ILE A 1 354 ? 32.756 8.321   52.140 1.00 39.25  ?  311 ILE A CA  1 
ATOM   2511 C C   . ILE A 1 354 ? 32.320 8.663   53.562 1.00 39.29  ?  311 ILE A C   1 
ATOM   2512 O O   . ILE A 1 354 ? 31.944 7.779   54.339 1.00 42.25  ?  311 ILE A O   1 
ATOM   2513 C CB  . ILE A 1 354 ? 34.285 8.315   51.998 1.00 46.23  ?  311 ILE A CB  1 
ATOM   2514 C CG1 . ILE A 1 354 ? 34.680 7.892   50.571 1.00 46.82  ?  311 ILE A CG1 1 
ATOM   2515 C CG2 . ILE A 1 354 ? 34.918 7.411   53.043 1.00 42.13  ?  311 ILE A CG2 1 
ATOM   2516 C CD1 . ILE A 1 354 ? 36.154 8.086   50.278 1.00 47.04  ?  311 ILE A CD1 1 
ATOM   2517 N N   . LYS A 1 355 ? 32.367 9.949   53.918 1.00 40.00  ?  312 LYS A N   1 
ATOM   2518 C CA  . LYS A 1 355 ? 31.941 10.370  55.254 1.00 39.81  ?  312 LYS A CA  1 
ATOM   2519 C C   . LYS A 1 355 ? 30.449 10.137  55.432 1.00 41.44  ?  312 LYS A C   1 
ATOM   2520 O O   . LYS A 1 355 ? 30.000 9.664   56.485 1.00 41.98  ?  312 LYS A O   1 
ATOM   2521 C CB  . LYS A 1 355 ? 32.305 11.847  55.472 1.00 38.27  ?  312 LYS A CB  1 
ATOM   2522 C CG  . LYS A 1 355 ? 32.095 12.398  56.903 1.00 38.35  ?  312 LYS A CG  1 
ATOM   2523 C CD  . LYS A 1 355 ? 32.846 13.722  57.082 1.00 38.58  ?  312 LYS A CD  1 
ATOM   2524 C CE  . LYS A 1 355 ? 32.552 14.380  58.432 1.00 35.55  ?  312 LYS A CE  1 
ATOM   2525 N NZ  . LYS A 1 355 ? 32.973 13.544  59.599 1.00 35.48  ?  312 LYS A NZ  1 
ATOM   2526 N N   . ARG A 1 356 ? 29.669 10.425  54.389 1.00 42.95  ?  313 ARG A N   1 
ATOM   2527 C CA  . ARG A 1 356 ? 28.226 10.259  54.466 1.00 42.64  ?  313 ARG A CA  1 
ATOM   2528 C C   . ARG A 1 356 ? 27.831 8.807   54.720 1.00 47.79  ?  313 ARG A C   1 
ATOM   2529 O O   . ARG A 1 356 ? 26.840 8.549   55.412 1.00 44.97  ?  313 ARG A O   1 
ATOM   2530 C CB  . ARG A 1 356 ? 27.593 10.794  53.179 1.00 52.82  ?  313 ARG A CB  1 
ATOM   2531 C CG  . ARG A 1 356 ? 26.093 10.587  53.068 1.00 62.77  ?  313 ARG A CG  1 
ATOM   2532 C CD  . ARG A 1 356 ? 25.501 11.369  51.883 1.00 63.86  ?  313 ARG A CD  1 
ATOM   2533 N NE  . ARG A 1 356 ? 26.354 11.360  50.694 1.00 72.10  ?  313 ARG A NE  1 
ATOM   2534 C CZ  . ARG A 1 356 ? 26.994 12.427  50.216 1.00 71.64  ?  313 ARG A CZ  1 
ATOM   2535 N NH1 . ARG A 1 356 ? 26.880 13.605  50.823 1.00 63.91  ?  313 ARG A NH1 1 
ATOM   2536 N NH2 . ARG A 1 356 ? 27.741 12.320  49.124 1.00 67.65  ?  313 ARG A NH2 1 
ATOM   2537 N N   . GLN A 1 357 ? 28.603 7.847   54.211 1.00 45.07  ?  314 GLN A N   1 
ATOM   2538 C CA  . GLN A 1 357 ? 28.245 6.436   54.321 1.00 44.72  ?  314 GLN A CA  1 
ATOM   2539 C C   . GLN A 1 357 ? 28.803 5.748   55.563 1.00 44.04  ?  314 GLN A C   1 
ATOM   2540 O O   . GLN A 1 357 ? 28.767 4.515   55.642 1.00 41.50  ?  314 GLN A O   1 
ATOM   2541 C CB  . GLN A 1 357 ? 28.701 5.689   53.073 1.00 49.45  ?  314 GLN A CB  1 
ATOM   2542 C CG  . GLN A 1 357 ? 28.047 6.231   51.841 1.00 57.41  ?  314 GLN A CG  1 
ATOM   2543 C CD  . GLN A 1 357 ? 27.194 5.201   51.151 1.00 68.45  ?  314 GLN A CD  1 
ATOM   2544 O OE1 . GLN A 1 357 ? 26.245 4.649   51.733 1.00 62.68  ?  314 GLN A OE1 1 
ATOM   2545 N NE2 . GLN A 1 357 ? 27.533 4.918   49.900 1.00 60.62  ?  314 GLN A NE2 1 
ATOM   2546 N N   . LEU A 1 358 ? 29.310 6.501   56.530 1.00 41.48  ?  315 LEU A N   1 
ATOM   2547 C CA  . LEU A 1 358 ? 29.687 5.907   57.797 1.00 40.27  ?  315 LEU A CA  1 
ATOM   2548 C C   . LEU A 1 358 ? 28.430 5.477   58.554 1.00 37.70  ?  315 LEU A C   1 
ATOM   2549 O O   . LEU A 1 358 ? 27.344 6.010   58.311 1.00 39.88  ?  315 LEU A O   1 
ATOM   2550 C CB  . LEU A 1 358 ? 30.494 6.903   58.626 1.00 35.47  ?  315 LEU A CB  1 
ATOM   2551 C CG  . LEU A 1 358 ? 31.837 7.292   58.009 1.00 44.70  ?  315 LEU A CG  1 
ATOM   2552 C CD1 . LEU A 1 358 ? 32.468 8.457   58.777 1.00 41.99  ?  315 LEU A CD1 1 
ATOM   2553 C CD2 . LEU A 1 358 ? 32.791 6.084   57.964 1.00 38.29  ?  315 LEU A CD2 1 
ATOM   2554 N N   . PRO A 1 359 ? 28.544 4.498   59.455 1.00 38.73  ?  316 PRO A N   1 
ATOM   2555 C CA  . PRO A 1 359 ? 27.355 4.058   60.210 1.00 47.07  ?  316 PRO A CA  1 
ATOM   2556 C C   . PRO A 1 359 ? 26.741 5.156   61.060 1.00 46.82  ?  316 PRO A C   1 
ATOM   2557 O O   . PRO A 1 359 ? 25.515 5.188   61.234 1.00 41.73  ?  316 PRO A O   1 
ATOM   2558 C CB  . PRO A 1 359 ? 27.895 2.919   61.082 1.00 39.03  ?  316 PRO A CB  1 
ATOM   2559 C CG  . PRO A 1 359 ? 29.103 2.459   60.394 1.00 41.45  ?  316 PRO A CG  1 
ATOM   2560 C CD  . PRO A 1 359 ? 29.710 3.640   59.718 1.00 37.36  ?  316 PRO A CD  1 
ATOM   2561 N N   . ILE A 1 360 ? 27.562 6.055   61.602 1.00 40.39  ?  317 ILE A N   1 
ATOM   2562 C CA  . ILE A 1 360 ? 27.084 7.227   62.325 1.00 39.67  ?  317 ILE A CA  1 
ATOM   2563 C C   . ILE A 1 360 ? 27.946 8.417   61.928 1.00 38.66  ?  317 ILE A C   1 
ATOM   2564 O O   . ILE A 1 360 ? 29.047 8.269   61.395 1.00 40.97  ?  317 ILE A O   1 
ATOM   2565 C CB  . ILE A 1 360 ? 27.111 7.020   63.852 1.00 41.90  ?  317 ILE A CB  1 
ATOM   2566 C CG1 . ILE A 1 360 ? 28.531 6.680   64.327 1.00 39.97  ?  317 ILE A CG1 1 
ATOM   2567 C CG2 . ILE A 1 360 ? 26.103 5.939   64.254 1.00 45.83  ?  317 ILE A CG2 1 
ATOM   2568 C CD1 . ILE A 1 360 ? 28.691 6.682   65.875 1.00 39.93  ?  317 ILE A CD1 1 
ATOM   2569 N N   . GLN A 1 361 ? 27.416 9.614   62.164 1.00 39.73  ?  318 GLN A N   1 
ATOM   2570 C CA  . GLN A 1 361 ? 28.130 10.840  61.836 1.00 39.75  ?  318 GLN A CA  1 
ATOM   2571 C C   . GLN A 1 361 ? 28.838 11.470  63.024 1.00 36.04  ?  318 GLN A C   1 
ATOM   2572 O O   . GLN A 1 361 ? 29.856 12.141  62.832 1.00 36.48  ?  318 GLN A O   1 
ATOM   2573 C CB  . GLN A 1 361 ? 27.171 11.869  61.226 1.00 40.82  ?  318 GLN A CB  1 
ATOM   2574 C CG  . GLN A 1 361 ? 26.660 11.478  59.852 1.00 39.05  ?  318 GLN A CG  1 
ATOM   2575 C CD  . GLN A 1 361 ? 27.798 11.259  58.872 1.00 43.41  ?  318 GLN A CD  1 
ATOM   2576 O OE1 . GLN A 1 361 ? 28.641 12.138  58.679 1.00 42.77  ?  318 GLN A OE1 1 
ATOM   2577 N NE2 . GLN A 1 361 ? 27.840 10.075  58.264 1.00 43.25  ?  318 GLN A NE2 1 
ATOM   2578 N N   . SER A 1 362 ? 28.342 11.286  64.248 1.00 39.46  ?  319 SER A N   1 
ATOM   2579 C CA  . SER A 1 362 ? 28.978 11.962  65.367 1.00 38.01  ?  319 SER A CA  1 
ATOM   2580 C C   . SER A 1 362 ? 28.567 11.310  66.679 1.00 38.16  ?  319 SER A C   1 
ATOM   2581 O O   . SER A 1 362 ? 27.647 10.492  66.740 1.00 41.46  ?  319 SER A O   1 
ATOM   2582 C CB  . SER A 1 362 ? 28.644 13.459  65.380 1.00 42.93  ?  319 SER A CB  1 
ATOM   2583 O OG  . SER A 1 362 ? 27.289 13.677  65.735 1.00 44.33  ?  319 SER A OG  1 
ATOM   2584 N N   . ARG A 1 363 ? 29.274 11.715  67.734 1.00 34.34  ?  320 ARG A N   1 
ATOM   2585 C CA  . ARG A 1 363 ? 29.111 11.129  69.064 1.00 36.86  ?  320 ARG A CA  1 
ATOM   2586 C C   . ARG A 1 363 ? 27.667 11.187  69.551 1.00 38.86  ?  320 ARG A C   1 
ATOM   2587 O O   . ARG A 1 363 ? 27.221 10.296  70.288 1.00 36.74  ?  320 ARG A O   1 
ATOM   2588 C CB  . ARG A 1 363 ? 30.048 11.847  70.039 1.00 36.78  ?  320 ARG A CB  1 
ATOM   2589 C CG  . ARG A 1 363 ? 29.779 11.613  71.532 1.00 41.89  ?  320 ARG A CG  1 
ATOM   2590 C CD  . ARG A 1 363 ? 30.128 10.195  71.936 1.00 42.37  ?  320 ARG A CD  1 
ATOM   2591 N NE  . ARG A 1 363 ? 31.550 9.899   71.753 1.00 41.16  ?  320 ARG A NE  1 
ATOM   2592 C CZ  . ARG A 1 363 ? 32.482 10.087  72.685 1.00 41.36  ?  320 ARG A CZ  1 
ATOM   2593 N NH1 . ARG A 1 363 ? 32.146 10.580  73.874 1.00 40.55  ?  320 ARG A NH1 1 
ATOM   2594 N NH2 . ARG A 1 363 ? 33.750 9.784   72.436 1.00 36.08  ?  320 ARG A NH2 1 
ATOM   2595 N N   . SER A 1 364 ? 26.916 12.215  69.160 1.00 43.69  ?  321 SER A N   1 
ATOM   2596 C CA  . SER A 1 364 ? 25.565 12.353  69.692 1.00 49.59  ?  321 SER A CA  1 
ATOM   2597 C C   . SER A 1 364 ? 24.644 11.236  69.227 1.00 50.91  ?  321 SER A C   1 
ATOM   2598 O O   . SER A 1 364 ? 23.599 11.015  69.846 1.00 43.17  ?  321 SER A O   1 
ATOM   2599 C CB  . SER A 1 364 ? 24.982 13.710  69.311 1.00 46.72  ?  321 SER A CB  1 
ATOM   2600 O OG  . SER A 1 364 ? 25.126 13.940  67.931 1.00 55.71  ?  321 SER A OG  1 
ATOM   2601 N N   . GLU A 1 365 ? 25.004 10.520  68.162 1.00 40.56  ?  322 GLU A N   1 
ATOM   2602 C CA  . GLU A 1 365 ? 24.213 9.368   67.748 1.00 40.40  ?  322 GLU A CA  1 
ATOM   2603 C C   . GLU A 1 365 ? 24.533 8.107   68.531 1.00 37.27  ?  322 GLU A C   1 
ATOM   2604 O O   . GLU A 1 365 ? 23.787 7.126   68.417 1.00 41.28  ?  322 GLU A O   1 
ATOM   2605 C CB  . GLU A 1 365 ? 24.435 9.086   66.258 1.00 37.39  ?  322 GLU A CB  1 
ATOM   2606 C CG  . GLU A 1 365 ? 23.910 10.162  65.346 1.00 41.21  ?  322 GLU A CG  1 
ATOM   2607 C CD  . GLU A 1 365 ? 24.343 9.930   63.903 1.00 44.32  ?  322 GLU A CD  1 
ATOM   2608 O OE1 . GLU A 1 365 ? 23.991 8.880   63.330 1.00 48.57  ?  322 GLU A OE1 1 
ATOM   2609 O OE2 . GLU A 1 365 ? 25.048 10.790  63.359 1.00 49.28  ?  322 GLU A OE2 1 
ATOM   2610 N N   . LEU A 1 366 ? 25.623 8.088   69.291 1.00 35.48  ?  323 LEU A N   1 
ATOM   2611 C CA  . LEU A 1 366 ? 26.005 6.873   69.995 1.00 40.60  ?  323 LEU A CA  1 
ATOM   2612 C C   . LEU A 1 366 ? 24.882 6.424   70.929 1.00 48.66  ?  323 LEU A C   1 
ATOM   2613 O O   . LEU A 1 366 ? 24.278 7.234   71.638 1.00 44.94  ?  323 LEU A O   1 
ATOM   2614 C CB  . LEU A 1 366 ? 27.294 7.101   70.783 1.00 39.55  ?  323 LEU A CB  1 
ATOM   2615 C CG  . LEU A 1 366 ? 28.123 5.842   71.046 1.00 45.82  ?  323 LEU A CG  1 
ATOM   2616 C CD1 . LEU A 1 366 ? 28.468 5.182   69.722 1.00 44.85  ?  323 LEU A CD1 1 
ATOM   2617 C CD2 . LEU A 1 366 ? 29.388 6.165   71.808 1.00 38.21  ?  323 LEU A CD2 1 
ATOM   2618 N N   . ALA A 1 367 ? 24.607 5.119   70.931 1.00 40.44  ?  324 ALA A N   1 
ATOM   2619 C CA  . ALA A 1 367 ? 23.484 4.558   71.679 1.00 45.48  ?  324 ALA A CA  1 
ATOM   2620 C C   . ALA A 1 367 ? 23.797 4.310   73.150 1.00 42.59  ?  324 ALA A C   1 
ATOM   2621 O O   . ALA A 1 367 ? 22.965 3.721   73.848 1.00 50.14  ?  324 ALA A O   1 
ATOM   2622 C CB  . ALA A 1 367 ? 23.022 3.245   71.040 1.00 40.48  ?  324 ALA A CB  1 
ATOM   2623 N N   . VAL A 1 368 ? 24.956 4.747   73.639 1.00 38.28  ?  325 VAL A N   1 
ATOM   2624 C CA  . VAL A 1 368 ? 25.372 4.489   75.010 1.00 39.90  ?  325 VAL A CA  1 
ATOM   2625 C C   . VAL A 1 368 ? 26.137 5.711   75.497 1.00 45.41  ?  325 VAL A C   1 
ATOM   2626 O O   . VAL A 1 368 ? 26.743 6.435   74.705 1.00 43.68  ?  325 VAL A O   1 
ATOM   2627 C CB  . VAL A 1 368 ? 26.233 3.204   75.083 1.00 43.09  ?  325 VAL A CB  1 
ATOM   2628 C CG1 . VAL A 1 368 ? 27.639 3.463   74.526 1.00 45.61  ?  325 VAL A CG1 1 
ATOM   2629 C CG2 . VAL A 1 368 ? 26.298 2.661   76.478 1.00 50.61  ?  325 VAL A CG2 1 
ATOM   2630 N N   . ASP A 1 369 ? 26.108 5.953   76.808 1.00 40.22  ?  326 ASP A N   1 
ATOM   2631 C CA  . ASP A 1 369 ? 26.904 7.034   77.364 1.00 35.45  ?  326 ASP A CA  1 
ATOM   2632 C C   . ASP A 1 369 ? 27.538 6.548   78.661 1.00 41.18  ?  326 ASP A C   1 
ATOM   2633 O O   . ASP A 1 369 ? 27.333 5.407   79.081 1.00 40.24  ?  326 ASP A O   1 
ATOM   2634 C CB  . ASP A 1 369 ? 26.062 8.311   77.521 1.00 43.42  ?  326 ASP A CB  1 
ATOM   2635 C CG  . ASP A 1 369 ? 25.011 8.210   78.620 1.00 44.99  ?  326 ASP A CG  1 
ATOM   2636 O OD1 . ASP A 1 369 ? 25.066 7.281   79.447 1.00 42.41  ?  326 ASP A OD1 1 
ATOM   2637 O OD2 . ASP A 1 369 ? 24.125 9.084   78.648 1.00 54.55  ?  326 ASP A OD2 1 
ATOM   2638 N N   . GLY A 1 370 ? 28.344 7.416   79.281 1.00 37.74  ?  327 GLY A N   1 
ATOM   2639 C CA  . GLY A 1 370 ? 29.120 7.003   80.439 1.00 36.48  ?  327 GLY A CA  1 
ATOM   2640 C C   . GLY A 1 370 ? 28.277 6.481   81.589 1.00 33.39  ?  327 GLY A C   1 
ATOM   2641 O O   . GLY A 1 370 ? 28.726 5.626   82.351 1.00 35.94  ?  327 GLY A O   1 
ATOM   2642 N N   . TRP A 1 371 ? 27.055 6.970   81.733 1.00 35.65  ?  328 TRP A N   1 
ATOM   2643 C CA  . TRP A 1 371 ? 26.249 6.495   82.857 1.00 38.96  ?  328 TRP A CA  1 
ATOM   2644 C C   . TRP A 1 371 ? 25.727 5.079   82.620 1.00 42.67  ?  328 TRP A C   1 
ATOM   2645 O O   . TRP A 1 371 ? 25.533 4.328   83.582 1.00 37.84  ?  328 TRP A O   1 
ATOM   2646 C CB  . TRP A 1 371 ? 25.110 7.477   83.143 1.00 44.77  ?  328 TRP A CB  1 
ATOM   2647 C CG  . TRP A 1 371 ? 25.631 8.735   83.821 1.00 45.33  ?  328 TRP A CG  1 
ATOM   2648 C CD1 . TRP A 1 371 ? 25.937 8.886   85.157 1.00 41.35  ?  328 TRP A CD1 1 
ATOM   2649 C CD2 . TRP A 1 371 ? 25.925 9.993   83.200 1.00 40.12  ?  328 TRP A CD2 1 
ATOM   2650 N NE1 . TRP A 1 371 ? 26.406 10.160  85.391 1.00 43.48  ?  328 TRP A NE1 1 
ATOM   2651 C CE2 . TRP A 1 371 ? 26.406 10.861  84.213 1.00 45.80  ?  328 TRP A CE2 1 
ATOM   2652 C CE3 . TRP A 1 371 ? 25.830 10.476  81.882 1.00 40.33  ?  328 TRP A CE3 1 
ATOM   2653 C CZ2 . TRP A 1 371 ? 26.783 12.182  83.954 1.00 42.12  ?  328 TRP A CZ2 1 
ATOM   2654 C CZ3 . TRP A 1 371 ? 26.209 11.789  81.627 1.00 49.13  ?  328 TRP A CZ3 1 
ATOM   2655 C CH2 . TRP A 1 371 ? 26.684 12.626  82.663 1.00 47.84  ?  328 TRP A CH2 1 
ATOM   2656 N N   . ASP A 1 372 ? 25.532 4.682   81.358 1.00 39.23  ?  329 ASP A N   1 
ATOM   2657 C CA  . ASP A 1 372 ? 25.304 3.271   81.059 1.00 40.09  ?  329 ASP A CA  1 
ATOM   2658 C C   . ASP A 1 372 ? 26.474 2.423   81.536 1.00 35.25  ?  329 ASP A C   1 
ATOM   2659 O O   . ASP A 1 372 ? 26.283 1.373   82.158 1.00 38.34  ?  329 ASP A O   1 
ATOM   2660 C CB  . ASP A 1 372 ? 25.087 3.066   79.554 1.00 36.04  ?  329 ASP A CB  1 
ATOM   2661 C CG  . ASP A 1 372 ? 23.828 3.732   79.044 1.00 42.04  ?  329 ASP A CG  1 
ATOM   2662 O OD1 . ASP A 1 372 ? 22.752 3.575   79.666 1.00 43.11  ?  329 ASP A OD1 1 
ATOM   2663 O OD2 . ASP A 1 372 ? 23.906 4.414   78.000 1.00 42.44  ?  329 ASP A OD2 1 
ATOM   2664 N N   . LEU A 1 373 ? 27.704 2.870   81.266 1.00 33.84  ?  330 LEU A N   1 
ATOM   2665 C CA  . LEU A 1 373 ? 28.861 2.088   81.684 1.00 34.27  ?  330 LEU A CA  1 
ATOM   2666 C C   . LEU A 1 373 ? 28.981 2.045   83.207 1.00 38.30  ?  330 LEU A C   1 
ATOM   2667 O O   . LEU A 1 373 ? 29.390 1.026   83.777 1.00 38.18  ?  330 LEU A O   1 
ATOM   2668 C CB  . LEU A 1 373 ? 30.141 2.649   81.073 1.00 33.68  ?  330 LEU A CB  1 
ATOM   2669 C CG  . LEU A 1 373 ? 30.230 2.788   79.542 1.00 41.79  ?  330 LEU A CG  1 
ATOM   2670 C CD1 . LEU A 1 373 ? 31.678 2.967   79.116 1.00 37.23  ?  330 LEU A CD1 1 
ATOM   2671 C CD2 . LEU A 1 373 ? 29.605 1.594   78.856 1.00 41.27  ?  330 LEU A CD2 1 
ATOM   2672 N N   . ILE A 1 374 ? 28.664 3.149   83.883 1.00 38.38  ?  331 ILE A N   1 
ATOM   2673 C CA  . ILE A 1 374 ? 28.653 3.126   85.347 1.00 35.27  ?  331 ILE A CA  1 
ATOM   2674 C C   . ILE A 1 374 ? 27.697 2.045   85.850 1.00 33.82  ?  331 ILE A C   1 
ATOM   2675 O O   . ILE A 1 374 ? 28.049 1.232   86.715 1.00 43.09  ?  331 ILE A O   1 
ATOM   2676 C CB  . ILE A 1 374 ? 28.298 4.519   85.903 1.00 37.22  ?  331 ILE A CB  1 
ATOM   2677 C CG1 . ILE A 1 374 ? 29.447 5.499   85.658 1.00 36.32  ?  331 ILE A CG1 1 
ATOM   2678 C CG2 . ILE A 1 374 ? 27.987 4.456   87.415 1.00 36.18  ?  331 ILE A CG2 1 
ATOM   2679 C CD1 . ILE A 1 374 ? 29.060 6.981   85.850 1.00 34.79  ?  331 ILE A CD1 1 
ATOM   2680 N N   . GLU A 1 375 ? 26.473 2.017   85.315 1.00 41.20  ?  332 GLU A N   1 
ATOM   2681 C CA  . GLU A 1 375 ? 25.502 1.003   85.731 1.00 41.71  ?  332 GLU A CA  1 
ATOM   2682 C C   . GLU A 1 375 ? 26.045 -0.405  85.517 1.00 46.67  ?  332 GLU A C   1 
ATOM   2683 O O   . GLU A 1 375 ? 26.047 -1.233  86.440 1.00 40.21  ?  332 GLU A O   1 
ATOM   2684 C CB  . GLU A 1 375 ? 24.190 1.182   84.965 1.00 43.31  ?  332 GLU A CB  1 
ATOM   2685 C CG  . GLU A 1 375 ? 23.347 2.339   85.445 1.00 61.43  ?  332 GLU A CG  1 
ATOM   2686 C CD  . GLU A 1 375 ? 23.128 2.302   86.956 1.00 68.36  ?  332 GLU A CD  1 
ATOM   2687 O OE1 . GLU A 1 375 ? 22.356 1.433   87.430 1.00 68.95  ?  332 GLU A OE1 1 
ATOM   2688 O OE2 . GLU A 1 375 ? 23.748 3.128   87.663 1.00 48.17  ?  332 GLU A OE2 1 
ATOM   2689 N N   . TRP A 1 376 ? 26.513 -0.693  84.295 1.00 41.56  ?  333 TRP A N   1 
ATOM   2690 C CA  . TRP A 1 376 ? 26.932 -2.046  83.946 1.00 43.29  ?  333 TRP A CA  1 
ATOM   2691 C C   . TRP A 1 376 ? 28.188 -2.462  84.698 1.00 41.91  ?  333 TRP A C   1 
ATOM   2692 O O   . TRP A 1 376 ? 28.331 -3.628  85.077 1.00 45.58  ?  333 TRP A O   1 
ATOM   2693 C CB  . TRP A 1 376 ? 27.162 -2.144  82.435 1.00 41.89  ?  333 TRP A CB  1 
ATOM   2694 C CG  . TRP A 1 376 ? 25.958 -1.770  81.621 1.00 41.34  ?  333 TRP A CG  1 
ATOM   2695 C CD1 . TRP A 1 376 ? 24.657 -1.799  82.027 1.00 41.04  ?  333 TRP A CD1 1 
ATOM   2696 C CD2 . TRP A 1 376 ? 25.945 -1.301  80.267 1.00 40.76  ?  333 TRP A CD2 1 
ATOM   2697 N NE1 . TRP A 1 376 ? 23.836 -1.382  81.016 1.00 43.73  ?  333 TRP A NE1 1 
ATOM   2698 C CE2 . TRP A 1 376 ? 24.597 -1.075  79.919 1.00 44.92  ?  333 TRP A CE2 1 
ATOM   2699 C CE3 . TRP A 1 376 ? 26.939 -1.052  79.317 1.00 40.20  ?  333 TRP A CE3 1 
ATOM   2700 C CZ2 . TRP A 1 376 ? 24.215 -0.608  78.666 1.00 48.05  ?  333 TRP A CZ2 1 
ATOM   2701 C CZ3 . TRP A 1 376 ? 26.557 -0.598  78.062 1.00 41.54  ?  333 TRP A CZ3 1 
ATOM   2702 C CH2 . TRP A 1 376 ? 25.206 -0.377  77.750 1.00 44.10  ?  333 TRP A CH2 1 
ATOM   2703 N N   . SER A 1 377 ? 29.126 -1.538  84.898 1.00 42.15  ?  334 SER A N   1 
ATOM   2704 C CA  . SER A 1 377 ? 30.370 -1.895  85.568 1.00 40.03  ?  334 SER A CA  1 
ATOM   2705 C C   . SER A 1 377 ? 30.213 -2.000  87.076 1.00 41.30  ?  334 SER A C   1 
ATOM   2706 O O   . SER A 1 377 ? 30.982 -2.721  87.718 1.00 43.45  ?  334 SER A O   1 
ATOM   2707 C CB  . SER A 1 377 ? 31.457 -0.864  85.273 1.00 50.19  ?  334 SER A CB  1 
ATOM   2708 O OG  . SER A 1 377 ? 31.084 0.416   85.771 1.00 43.78  ?  334 SER A OG  1 
ATOM   2709 N N   . GLY A 1 378 ? 29.262 -1.274  87.657 1.00 44.22  ?  335 GLY A N   1 
ATOM   2710 C CA  . GLY A 1 378 ? 29.278 -1.108  89.098 1.00 42.35  ?  335 GLY A CA  1 
ATOM   2711 C C   . GLY A 1 378 ? 30.432 -0.282  89.617 1.00 45.85  ?  335 GLY A C   1 
ATOM   2712 O O   . GLY A 1 378 ? 30.657 -0.244  90.835 1.00 43.81  ?  335 GLY A O   1 
ATOM   2713 N N   . ALA A 1 379 ? 31.171 0.387   88.734 1.00 44.81  ?  336 ALA A N   1 
ATOM   2714 C CA  . ALA A 1 379 ? 32.295 1.230   89.120 1.00 43.58  ?  336 ALA A CA  1 
ATOM   2715 C C   . ALA A 1 379 ? 31.897 2.706   89.117 1.00 40.87  ?  336 ALA A C   1 
ATOM   2716 O O   . ALA A 1 379 ? 30.979 3.123   88.402 1.00 41.41  ?  336 ALA A O   1 
ATOM   2717 C CB  . ALA A 1 379 ? 33.484 1.012   88.179 1.00 43.48  ?  336 ALA A CB  1 
ATOM   2718 N N   . LYS A 1 380 ? 32.609 3.495   89.919 1.00 44.04  ?  337 LYS A N   1 
ATOM   2719 C CA  . LYS A 1 380 ? 32.308 4.915   90.036 1.00 40.54  ?  337 LYS A CA  1 
ATOM   2720 C C   . LYS A 1 380 ? 32.805 5.681   88.815 1.00 35.51  ?  337 LYS A C   1 
ATOM   2721 O O   . LYS A 1 380 ? 33.791 5.304   88.176 1.00 38.90  ?  337 LYS A O   1 
ATOM   2722 C CB  . LYS A 1 380 ? 32.944 5.506   91.293 1.00 41.07  ?  337 LYS A CB  1 
ATOM   2723 C CG  . LYS A 1 380 ? 32.455 4.880   92.603 1.00 34.56  ?  337 LYS A CG  1 
ATOM   2724 C CD  . LYS A 1 380 ? 33.172 5.497   93.795 1.00 41.21  ?  337 LYS A CD  1 
ATOM   2725 C CE  . LYS A 1 380 ? 32.515 5.079   95.121 1.00 36.24  ?  337 LYS A CE  1 
ATOM   2726 N NZ  . LYS A 1 380 ? 33.327 5.550   96.265 1.00 36.87  ?  337 LYS A NZ  1 
ATOM   2727 N N   . SER A 1 381 ? 32.128 6.787   88.523 1.00 35.41  ?  338 SER A N   1 
ATOM   2728 C CA  . SER A 1 381 ? 32.521 7.647   87.413 1.00 38.96  ?  338 SER A CA  1 
ATOM   2729 C C   . SER A 1 381 ? 33.989 8.062   87.525 1.00 42.72  ?  338 SER A C   1 
ATOM   2730 O O   . SER A 1 381 ? 34.499 8.333   88.615 1.00 36.32  ?  338 SER A O   1 
ATOM   2731 C CB  . SER A 1 381 ? 31.613 8.879   87.372 1.00 34.69  ?  338 SER A CB  1 
ATOM   2732 O OG  . SER A 1 381 ? 32.103 9.866   86.472 1.00 38.46  ?  338 SER A OG  1 
ATOM   2733 N N   . GLY A 1 382 ? 34.678 8.095   86.382 1.00 34.05  ?  339 GLY A N   1 
ATOM   2734 C CA  . GLY A 1 382 ? 36.065 8.505   86.345 1.00 32.66  ?  339 GLY A CA  1 
ATOM   2735 C C   . GLY A 1 382 ? 36.535 8.688   84.917 1.00 37.30  ?  339 GLY A C   1 
ATOM   2736 O O   . GLY A 1 382 ? 35.763 8.500   83.973 1.00 33.47  ?  339 GLY A O   1 
ATOM   2737 N N   . PRO A 1 383 ? 37.799 9.079   84.724 1.00 38.46  ?  340 PRO A N   1 
ATOM   2738 C CA  . PRO A 1 383 ? 38.317 9.208   83.348 1.00 35.49  ?  340 PRO A CA  1 
ATOM   2739 C C   . PRO A 1 383 ? 38.253 7.914   82.550 1.00 40.74  ?  340 PRO A C   1 
ATOM   2740 O O   . PRO A 1 383 ? 38.293 7.967   81.312 1.00 39.06  ?  340 PRO A O   1 
ATOM   2741 C CB  . PRO A 1 383 ? 39.769 9.663   83.555 1.00 38.21  ?  340 PRO A CB  1 
ATOM   2742 C CG  . PRO A 1 383 ? 39.764 10.330  84.922 1.00 40.12  ?  340 PRO A CG  1 
ATOM   2743 C CD  . PRO A 1 383 ? 38.762 9.558   85.730 1.00 37.93  ?  340 PRO A CD  1 
ATOM   2744 N N   . TRP A 1 384 ? 38.146 6.755   83.212 1.00 40.47  ?  341 TRP A N   1 
ATOM   2745 C CA  . TRP A 1 384 ? 38.075 5.495   82.474 1.00 39.63  ?  341 TRP A CA  1 
ATOM   2746 C C   . TRP A 1 384 ? 36.895 5.468   81.514 1.00 40.64  ?  341 TRP A C   1 
ATOM   2747 O O   . TRP A 1 384 ? 36.955 4.793   80.477 1.00 42.09  ?  341 TRP A O   1 
ATOM   2748 C CB  . TRP A 1 384 ? 38.000 4.320   83.447 1.00 38.16  ?  341 TRP A CB  1 
ATOM   2749 C CG  . TRP A 1 384 ? 36.705 4.214   84.200 1.00 38.13  ?  341 TRP A CG  1 
ATOM   2750 C CD1 . TRP A 1 384 ? 36.373 4.854   85.371 1.00 39.06  ?  341 TRP A CD1 1 
ATOM   2751 C CD2 . TRP A 1 384 ? 35.577 3.401   83.858 1.00 42.15  ?  341 TRP A CD2 1 
ATOM   2752 N NE1 . TRP A 1 384 ? 35.106 4.495   85.761 1.00 40.84  ?  341 TRP A NE1 1 
ATOM   2753 C CE2 . TRP A 1 384 ? 34.597 3.601   84.855 1.00 37.24  ?  341 TRP A CE2 1 
ATOM   2754 C CE3 . TRP A 1 384 ? 35.297 2.523   82.803 1.00 38.83  ?  341 TRP A CE3 1 
ATOM   2755 C CZ2 . TRP A 1 384 ? 33.361 2.955   84.830 1.00 39.19  ?  341 TRP A CZ2 1 
ATOM   2756 C CZ3 . TRP A 1 384 ? 34.065 1.883   82.777 1.00 43.42  ?  341 TRP A CZ3 1 
ATOM   2757 C CH2 . TRP A 1 384 ? 33.111 2.103   83.785 1.00 46.30  ?  341 TRP A CH2 1 
ATOM   2758 N N   . LEU A 1 385 ? 35.826 6.206   81.820 1.00 37.39  ?  342 LEU A N   1 
ATOM   2759 C CA  . LEU A 1 385 ? 34.646 6.180   80.961 1.00 38.32  ?  342 LEU A CA  1 
ATOM   2760 C C   . LEU A 1 385 ? 34.974 6.640   79.547 1.00 39.87  ?  342 LEU A C   1 
ATOM   2761 O O   . LEU A 1 385 ? 34.471 6.073   78.568 1.00 37.34  ?  342 LEU A O   1 
ATOM   2762 C CB  . LEU A 1 385 ? 33.538 7.053   81.550 1.00 36.49  ?  342 LEU A CB  1 
ATOM   2763 C CG  . LEU A 1 385 ? 32.910 6.542   82.853 1.00 37.47  ?  342 LEU A CG  1 
ATOM   2764 C CD1 . LEU A 1 385 ? 31.997 7.626   83.409 1.00 31.00  ?  342 LEU A CD1 1 
ATOM   2765 C CD2 . LEU A 1 385 ? 32.137 5.236   82.612 1.00 32.57  ?  342 LEU A CD2 1 
ATOM   2766 N N   . LYS A 1 386 ? 35.799 7.682   79.417 1.00 34.63  ?  343 LYS A N   1 
ATOM   2767 C CA  . LYS A 1 386 ? 36.127 8.184   78.083 1.00 39.15  ?  343 LYS A CA  1 
ATOM   2768 C C   . LYS A 1 386 ? 36.872 7.133   77.271 1.00 37.67  ?  343 LYS A C   1 
ATOM   2769 O O   . LYS A 1 386 ? 36.631 6.983   76.063 1.00 36.34  ?  343 LYS A O   1 
ATOM   2770 C CB  . LYS A 1 386 ? 36.964 9.456   78.192 1.00 37.81  ?  343 LYS A CB  1 
ATOM   2771 C CG  . LYS A 1 386 ? 36.262 10.612  78.909 1.00 47.63  ?  343 LYS A CG  1 
ATOM   2772 C CD  . LYS A 1 386 ? 37.186 11.829  79.057 1.00 49.93  ?  343 LYS A CD  1 
ATOM   2773 C CE  . LYS A 1 386 ? 36.601 12.860  80.029 1.00 59.71  ?  343 LYS A CE  1 
ATOM   2774 N NZ  . LYS A 1 386 ? 37.495 14.054  80.197 1.00 58.84  ?  343 LYS A NZ  1 
ATOM   2775 N N   . VAL A 1 387 ? 37.796 6.417   77.913 1.00 37.41  ?  344 VAL A N   1 
ATOM   2776 C CA  . VAL A 1 387 ? 38.535 5.352   77.239 1.00 40.32  ?  344 VAL A CA  1 
ATOM   2777 C C   . VAL A 1 387 ? 37.574 4.302   76.698 1.00 45.80  ?  344 VAL A C   1 
ATOM   2778 O O   . VAL A 1 387 ? 37.671 3.878   75.537 1.00 38.46  ?  344 VAL A O   1 
ATOM   2779 C CB  . VAL A 1 387 ? 39.564 4.729   78.198 1.00 41.33  ?  344 VAL A CB  1 
ATOM   2780 C CG1 . VAL A 1 387 ? 40.282 3.565   77.528 1.00 44.92  ?  344 VAL A CG1 1 
ATOM   2781 C CG2 . VAL A 1 387 ? 40.567 5.790   78.688 1.00 41.91  ?  344 VAL A CG2 1 
ATOM   2782 N N   . TRP A 1 388 ? 36.615 3.881   77.525 1.00 38.03  ?  345 TRP A N   1 
ATOM   2783 C CA  . TRP A 1 388 ? 35.720 2.805   77.121 1.00 38.60  ?  345 TRP A CA  1 
ATOM   2784 C C   . TRP A 1 388 ? 34.648 3.281   76.148 1.00 37.95  ?  345 TRP A C   1 
ATOM   2785 O O   . TRP A 1 388 ? 34.291 2.545   75.219 1.00 38.31  ?  345 TRP A O   1 
ATOM   2786 C CB  . TRP A 1 388 ? 35.111 2.144   78.360 1.00 34.77  ?  345 TRP A CB  1 
ATOM   2787 C CG  . TRP A 1 388 ? 36.084 1.173   78.954 1.00 38.48  ?  345 TRP A CG  1 
ATOM   2788 C CD1 . TRP A 1 388 ? 37.118 1.457   79.798 1.00 39.33  ?  345 TRP A CD1 1 
ATOM   2789 C CD2 . TRP A 1 388 ? 36.151 -0.234  78.694 1.00 41.43  ?  345 TRP A CD2 1 
ATOM   2790 N NE1 . TRP A 1 388 ? 37.816 0.307   80.094 1.00 46.71  ?  345 TRP A NE1 1 
ATOM   2791 C CE2 . TRP A 1 388 ? 37.241 -0.744  79.428 1.00 47.00  ?  345 TRP A CE2 1 
ATOM   2792 C CE3 . TRP A 1 388 ? 35.391 -1.112  77.911 1.00 43.93  ?  345 TRP A CE3 1 
ATOM   2793 C CZ2 . TRP A 1 388 ? 37.587 -2.099  79.411 1.00 52.70  ?  345 TRP A CZ2 1 
ATOM   2794 C CZ3 . TRP A 1 388 ? 35.740 -2.459  77.891 1.00 49.00  ?  345 TRP A CZ3 1 
ATOM   2795 C CH2 . TRP A 1 388 ? 36.827 -2.937  78.641 1.00 51.51  ?  345 TRP A CH2 1 
ATOM   2796 N N   . ILE A 1 389 ? 34.140 4.508   76.302 1.00 32.59  ?  346 ILE A N   1 
ATOM   2797 C CA  . ILE A 1 389 ? 33.202 5.002   75.300 1.00 31.88  ?  346 ILE A CA  1 
ATOM   2798 C C   . ILE A 1 389 ? 33.872 5.043   73.927 1.00 35.46  ?  346 ILE A C   1 
ATOM   2799 O O   . ILE A 1 389 ? 33.244 4.743   72.903 1.00 38.24  ?  346 ILE A O   1 
ATOM   2800 C CB  . ILE A 1 389 ? 32.638 6.379   75.691 1.00 32.88  ?  346 ILE A CB  1 
ATOM   2801 C CG1 . ILE A 1 389 ? 31.689 6.245   76.891 1.00 34.74  ?  346 ILE A CG1 1 
ATOM   2802 C CG2 . ILE A 1 389 ? 31.874 6.986   74.512 1.00 32.98  ?  346 ILE A CG2 1 
ATOM   2803 C CD1 . ILE A 1 389 ? 30.407 5.465   76.567 1.00 37.96  ?  346 ILE A CD1 1 
ATOM   2804 N N   . GLU A 1 390 ? 35.157 5.406   73.879 1.00 36.16  ?  347 GLU A N   1 
ATOM   2805 C CA  . GLU A 1 390 ? 35.815 5.485   72.574 1.00 39.06  ?  347 GLU A CA  1 
ATOM   2806 C C   . GLU A 1 390 ? 36.021 4.102   71.961 1.00 36.58  ?  347 GLU A C   1 
ATOM   2807 O O   . GLU A 1 390 ? 35.891 3.943   70.739 1.00 37.12  ?  347 GLU A O   1 
ATOM   2808 C CB  . GLU A 1 390 ? 37.149 6.224   72.665 1.00 40.23  ?  347 GLU A CB  1 
ATOM   2809 C CG  . GLU A 1 390 ? 37.876 6.243   71.311 1.00 44.38  ?  347 GLU A CG  1 
ATOM   2810 C CD  . GLU A 1 390 ? 38.986 7.277   71.217 1.00 52.52  ?  347 GLU A CD  1 
ATOM   2811 O OE1 . GLU A 1 390 ? 38.719 8.465   71.491 1.00 53.39  ?  347 GLU A OE1 1 
ATOM   2812 O OE2 . GLU A 1 390 ? 40.122 6.898   70.852 1.00 53.89  ?  347 GLU A OE2 1 
ATOM   2813 N N   . LYS A 1 391 ? 36.373 3.099   72.774 1.00 38.96  ?  348 LYS A N   1 
ATOM   2814 C CA  . LYS A 1 391 ? 36.441 1.728   72.259 1.00 39.13  ?  348 LYS A CA  1 
ATOM   2815 C C   . LYS A 1 391 ? 35.137 1.355   71.575 1.00 41.74  ?  348 LYS A C   1 
ATOM   2816 O O   . LYS A 1 391 ? 35.126 0.836   70.450 1.00 36.69  ?  348 LYS A O   1 
ATOM   2817 C CB  . LYS A 1 391 ? 36.726 0.728   73.386 1.00 45.06  ?  348 LYS A CB  1 
ATOM   2818 C CG  . LYS A 1 391 ? 38.121 0.728   73.986 1.00 48.14  ?  348 LYS A CG  1 
ATOM   2819 C CD  . LYS A 1 391 ? 38.213 -0.400  75.037 1.00 55.64  ?  348 LYS A CD  1 
ATOM   2820 C CE  . LYS A 1 391 ? 39.391 -0.235  75.993 1.00 52.17  ?  348 LYS A CE  1 
ATOM   2821 N NZ  . LYS A 1 391 ? 40.651 0.121   75.269 1.00 61.71  ?  348 LYS A NZ  1 
ATOM   2822 N N   . ILE A 1 392 ? 34.018 1.615   72.258 1.00 37.70  ?  349 ILE A N   1 
ATOM   2823 C CA  . ILE A 1 392 ? 32.701 1.308   71.714 1.00 34.59  ?  349 ILE A CA  1 
ATOM   2824 C C   . ILE A 1 392 ? 32.437 2.141   70.472 1.00 39.82  ?  349 ILE A C   1 
ATOM   2825 O O   . ILE A 1 392 ? 31.942 1.632   69.456 1.00 40.16  ?  349 ILE A O   1 
ATOM   2826 C CB  . ILE A 1 392 ? 31.622 1.524   72.796 1.00 34.49  ?  349 ILE A CB  1 
ATOM   2827 C CG1 . ILE A 1 392 ? 31.737 0.453   73.870 1.00 35.11  ?  349 ILE A CG1 1 
ATOM   2828 C CG2 . ILE A 1 392 ? 30.216 1.532   72.191 1.00 38.25  ?  349 ILE A CG2 1 
ATOM   2829 C CD1 . ILE A 1 392 ? 31.080 0.867   75.217 1.00 36.40  ?  349 ILE A CD1 1 
ATOM   2830 N N   . GLU A 1 393 ? 32.782 3.433   70.522 1.00 35.66  ?  350 GLU A N   1 
ATOM   2831 C CA  . GLU A 1 393 ? 32.566 4.304   69.370 1.00 33.34  ?  350 GLU A CA  1 
ATOM   2832 C C   . GLU A 1 393 ? 33.306 3.791   68.133 1.00 35.11  ?  350 GLU A C   1 
ATOM   2833 O O   . GLU A 1 393 ? 32.765 3.812   67.023 1.00 33.75  ?  350 GLU A O   1 
ATOM   2834 C CB  . GLU A 1 393 ? 33.020 5.722   69.708 1.00 29.48  ?  350 GLU A CB  1 
ATOM   2835 C CG  . GLU A 1 393 ? 32.545 6.796   68.743 1.00 34.17  ?  350 GLU A CG  1 
ATOM   2836 C CD  . GLU A 1 393 ? 32.930 8.185   69.238 1.00 34.07  ?  350 GLU A CD  1 
ATOM   2837 O OE1 . GLU A 1 393 ? 33.913 8.276   70.000 1.00 36.21  ?  350 GLU A OE1 1 
ATOM   2838 O OE2 . GLU A 1 393 ? 32.252 9.169   68.878 1.00 35.76  ?  350 GLU A OE2 1 
ATOM   2839 N N   . ARG A 1 394 ? 34.551 3.344   68.305 1.00 37.15  ?  351 ARG A N   1 
ATOM   2840 C CA  . ARG A 1 394 ? 35.317 2.840   67.169 1.00 41.85  ?  351 ARG A CA  1 
ATOM   2841 C C   . ARG A 1 394 ? 34.642 1.618   66.555 1.00 43.10  ?  351 ARG A C   1 
ATOM   2842 O O   . ARG A 1 394 ? 34.516 1.512   65.328 1.00 38.01  ?  351 ARG A O   1 
ATOM   2843 C CB  . ARG A 1 394 ? 36.736 2.500   67.613 1.00 40.44  ?  351 ARG A CB  1 
ATOM   2844 C CG  . ARG A 1 394 ? 37.639 3.694   67.812 1.00 37.15  ?  351 ARG A CG  1 
ATOM   2845 C CD  . ARG A 1 394 ? 38.999 3.236   68.294 1.00 44.36  ?  351 ARG A CD  1 
ATOM   2846 N NE  . ARG A 1 394 ? 39.868 4.362   68.609 1.00 48.98  ?  351 ARG A NE  1 
ATOM   2847 C CZ  . ARG A 1 394 ? 40.730 4.901   67.752 1.00 56.49  ?  351 ARG A CZ  1 
ATOM   2848 N NH1 . ARG A 1 394 ? 40.846 4.408   66.519 1.00 45.09  ?  351 ARG A NH1 1 
ATOM   2849 N NH2 . ARG A 1 394 ? 41.479 5.931   68.132 1.00 56.91  ?  351 ARG A NH2 1 
ATOM   2850 N N   . LEU A 1 395 ? 34.203 0.683   67.401 1.00 40.97  ?  352 LEU A N   1 
ATOM   2851 C CA  . LEU A 1 395 ? 33.569 -0.533  66.907 1.00 44.13  ?  352 LEU A CA  1 
ATOM   2852 C C   . LEU A 1 395 ? 32.276 -0.233  66.167 1.00 45.06  ?  352 LEU A C   1 
ATOM   2853 O O   . LEU A 1 395 ? 31.922 -0.953  65.227 1.00 43.27  ?  352 LEU A O   1 
ATOM   2854 C CB  . LEU A 1 395 ? 33.316 -1.497  68.065 1.00 39.01  ?  352 LEU A CB  1 
ATOM   2855 C CG  . LEU A 1 395 ? 34.579 -2.054  68.725 1.00 47.05  ?  352 LEU A CG  1 
ATOM   2856 C CD1 . LEU A 1 395 ? 34.211 -2.861  69.944 1.00 42.47  ?  352 LEU A CD1 1 
ATOM   2857 C CD2 . LEU A 1 395 ? 35.387 -2.900  67.736 1.00 50.52  ?  352 LEU A CD2 1 
ATOM   2858 N N   . ILE A 1 396 ? 31.565 0.821   66.567 1.00 37.27  ?  353 ILE A N   1 
ATOM   2859 C CA  . ILE A 1 396 ? 30.376 1.242   65.837 1.00 36.11  ?  353 ILE A CA  1 
ATOM   2860 C C   . ILE A 1 396 ? 30.755 1.925   64.521 1.00 40.07  ?  353 ILE A C   1 
ATOM   2861 O O   . ILE A 1 396 ? 30.132 1.678   63.483 1.00 41.24  ?  353 ILE A O   1 
ATOM   2862 C CB  . ILE A 1 396 ? 29.507 2.155   66.724 1.00 35.23  ?  353 ILE A CB  1 
ATOM   2863 C CG1 . ILE A 1 396 ? 28.736 1.330   67.766 1.00 44.11  ?  353 ILE A CG1 1 
ATOM   2864 C CG2 . ILE A 1 396 ? 28.563 2.968   65.884 1.00 36.24  ?  353 ILE A CG2 1 
ATOM   2865 C CD1 . ILE A 1 396 ? 28.091 2.185   68.830 1.00 50.71  ?  353 ILE A CD1 1 
ATOM   2866 N N   . VAL A 1 397 ? 31.779 2.783   64.533 1.00 37.09  ?  354 VAL A N   1 
ATOM   2867 C CA  . VAL A 1 397 ? 32.144 3.500   63.311 1.00 35.35  ?  354 VAL A CA  1 
ATOM   2868 C C   . VAL A 1 397 ? 32.732 2.546   62.271 1.00 35.37  ?  354 VAL A C   1 
ATOM   2869 O O   . VAL A 1 397 ? 32.535 2.736   61.066 1.00 39.09  ?  354 VAL A O   1 
ATOM   2870 C CB  . VAL A 1 397 ? 33.109 4.657   63.636 1.00 39.78  ?  354 VAL A CB  1 
ATOM   2871 C CG1 . VAL A 1 397 ? 33.724 5.223   62.356 1.00 37.58  ?  354 VAL A CG1 1 
ATOM   2872 C CG2 . VAL A 1 397 ? 32.372 5.761   64.384 1.00 35.08  ?  354 VAL A CG2 1 
ATOM   2873 N N   . TYR A 1 398 ? 33.448 1.513   62.704 1.00 38.95  ?  355 TYR A N   1 
ATOM   2874 C CA  . TYR A 1 398 ? 33.909 0.490   61.770 1.00 43.03  ?  355 TYR A CA  1 
ATOM   2875 C C   . TYR A 1 398 ? 32.821 -0.513  61.405 1.00 48.85  ?  355 TYR A C   1 
ATOM   2876 O O   . TYR A 1 398 ? 33.097 -1.463  60.662 1.00 49.96  ?  355 TYR A O   1 
ATOM   2877 C CB  . TYR A 1 398 ? 35.112 -0.249  62.347 1.00 37.85  ?  355 TYR A CB  1 
ATOM   2878 C CG  . TYR A 1 398 ? 36.382 0.559   62.351 1.00 39.28  ?  355 TYR A CG  1 
ATOM   2879 C CD1 . TYR A 1 398 ? 37.008 0.913   61.163 1.00 42.69  ?  355 TYR A CD1 1 
ATOM   2880 C CD2 . TYR A 1 398 ? 36.977 0.938   63.540 1.00 37.95  ?  355 TYR A CD2 1 
ATOM   2881 C CE1 . TYR A 1 398 ? 38.179 1.645   61.169 1.00 42.07  ?  355 TYR A CE1 1 
ATOM   2882 C CE2 . TYR A 1 398 ? 38.137 1.669   63.554 1.00 39.05  ?  355 TYR A CE2 1 
ATOM   2883 C CZ  . TYR A 1 398 ? 38.740 2.017   62.363 1.00 41.96  ?  355 TYR A CZ  1 
ATOM   2884 O OH  . TYR A 1 398 ? 39.907 2.745   62.395 1.00 41.82  ?  355 TYR A OH  1 
ATOM   2885 N N   . GLY A 1 399 ? 31.599 -0.322  61.889 1.00 40.01  ?  356 GLY A N   1 
ATOM   2886 C CA  . GLY A 1 399 ? 30.509 -1.210  61.528 1.00 40.77  ?  356 GLY A CA  1 
ATOM   2887 C C   . GLY A 1 399 ? 30.681 -2.620  62.036 1.00 45.80  ?  356 GLY A C   1 
ATOM   2888 O O   . GLY A 1 399 ? 30.139 -3.554  61.439 1.00 45.73  ?  356 GLY A O   1 
ATOM   2889 N N   . ILE A 1 400 ? 31.436 -2.803  63.117 1.00 36.03  ?  357 ILE A N   1 
ATOM   2890 C CA  . ILE A 1 400 ? 31.607 -4.114  63.727 1.00 39.74  ?  357 ILE A CA  1 
ATOM   2891 C C   . ILE A 1 400 ? 30.548 -4.375  64.791 1.00 48.97  ?  357 ILE A C   1 
ATOM   2892 O O   . ILE A 1 400 ? 29.932 -5.443  64.822 1.00 41.26  ?  357 ILE A O   1 
ATOM   2893 C CB  . ILE A 1 400 ? 33.027 -4.234  64.307 1.00 40.55  ?  357 ILE A CB  1 
ATOM   2894 C CG1 . ILE A 1 400 ? 34.038 -4.325  63.162 1.00 42.76  ?  357 ILE A CG1 1 
ATOM   2895 C CG2 . ILE A 1 400 ? 33.109 -5.433  65.244 1.00 40.05  ?  357 ILE A CG2 1 
ATOM   2896 C CD1 . ILE A 1 400 ? 35.462 -4.075  63.554 1.00 43.61  ?  357 ILE A CD1 1 
ATOM   2897 N N   . LEU A 1 401 ? 30.326 -3.411  65.680 1.00 42.47  ?  358 LEU A N   1 
ATOM   2898 C CA  . LEU A 1 401 ? 29.323 -3.515  66.732 1.00 39.52  ?  358 LEU A CA  1 
ATOM   2899 C C   . LEU A 1 401 ? 28.114 -2.664  66.360 1.00 38.20  ?  358 LEU A C   1 
ATOM   2900 O O   . LEU A 1 401 ? 28.263 -1.532  65.892 1.00 43.58  ?  358 LEU A O   1 
ATOM   2901 C CB  . LEU A 1 401 ? 29.926 -3.055  68.062 1.00 47.83  ?  358 LEU A CB  1 
ATOM   2902 C CG  . LEU A 1 401 ? 29.116 -2.983  69.354 1.00 42.61  ?  358 LEU A CG  1 
ATOM   2903 C CD1 . LEU A 1 401 ? 28.625 -4.351  69.763 1.00 44.98  ?  358 LEU A CD1 1 
ATOM   2904 C CD2 . LEU A 1 401 ? 30.023 -2.396  70.422 1.00 41.33  ?  358 LEU A CD2 1 
ATOM   2905 N N   . LYS A 1 402 ? 26.914 -3.213  66.545 1.00 35.36  ?  359 LYS A N   1 
ATOM   2906 C CA  . LYS A 1 402 ? 25.714 -2.459  66.199 1.00 38.15  ?  359 LYS A CA  1 
ATOM   2907 C C   . LYS A 1 402 ? 25.487 -1.324  67.201 1.00 40.46  ?  359 LYS A C   1 
ATOM   2908 O O   . LYS A 1 402 ? 25.772 -1.467  68.394 1.00 41.43  ?  359 LYS A O   1 
ATOM   2909 C CB  . LYS A 1 402 ? 24.492 -3.379  66.163 1.00 40.84  ?  359 LYS A CB  1 
ATOM   2910 C CG  . LYS A 1 402 ? 23.256 -2.715  65.597 1.00 42.77  ?  359 LYS A CG  1 
ATOM   2911 C CD  . LYS A 1 402 ? 22.089 -3.691  65.482 1.00 43.88  ?  359 LYS A CD  1 
ATOM   2912 C CE  . LYS A 1 402 ? 20.914 -3.032  64.771 1.00 53.78  ?  359 LYS A CE  1 
ATOM   2913 N NZ  . LYS A 1 402 ? 19.754 -3.958  64.591 1.00 58.24  ?  359 LYS A NZ  1 
ATOM   2914 N N   . ASN A 1 403 ? 24.985 -0.187  66.708 1.00 39.45  ?  360 ASN A N   1 
ATOM   2915 C CA  . ASN A 1 403 ? 24.739 0.982   67.564 1.00 49.39  ?  360 ASN A CA  1 
ATOM   2916 C C   . ASN A 1 403 ? 23.394 0.781   68.264 1.00 34.97  ?  360 ASN A C   1 
ATOM   2917 O O   . ASN A 1 403 ? 22.383 1.417   67.960 1.00 40.06  ?  360 ASN A O   1 
ATOM   2918 C CB  . ASN A 1 403 ? 24.773 2.279   66.764 1.00 42.55  ?  360 ASN A CB  1 
ATOM   2919 C CG  . ASN A 1 403 ? 24.734 3.527   67.656 1.00 41.96  ?  360 ASN A CG  1 
ATOM   2920 O OD1 . ASN A 1 403 ? 25.256 3.527   68.778 1.00 41.03  ?  360 ASN A OD1 1 
ATOM   2921 N ND2 . ASN A 1 403 ? 24.116 4.592   67.154 1.00 40.06  ?  360 ASN A ND2 1 
ATOM   2922 N N   . ASP A 1 404 ? 23.409 -0.153  69.207 1.00 43.73  ?  361 ASP A N   1 
ATOM   2923 C CA  . ASP A 1 404 ? 22.219 -0.618  69.908 1.00 47.41  ?  361 ASP A CA  1 
ATOM   2924 C C   . ASP A 1 404 ? 22.582 -0.850  71.365 1.00 37.48  ?  361 ASP A C   1 
ATOM   2925 O O   . ASP A 1 404 ? 23.533 -1.580  71.662 1.00 41.13  ?  361 ASP A O   1 
ATOM   2926 C CB  . ASP A 1 404 ? 21.679 -1.909  69.269 1.00 47.01  ?  361 ASP A CB  1 
ATOM   2927 C CG  . ASP A 1 404 ? 20.619 -2.577  70.114 1.00 50.04  ?  361 ASP A CG  1 
ATOM   2928 O OD1 . ASP A 1 404 ? 20.980 -3.338  71.039 1.00 51.92  ?  361 ASP A OD1 1 
ATOM   2929 O OD2 . ASP A 1 404 ? 19.426 -2.307  69.868 1.00 56.35  ?  361 ASP A OD2 1 
ATOM   2930 N N   . LYS A 1 405 ? 21.826 -0.230  72.276 1.00 46.61  ?  362 LYS A N   1 
ATOM   2931 C CA  . LYS A 1 405 ? 22.237 -0.244  73.678 1.00 44.02  ?  362 LYS A CA  1 
ATOM   2932 C C   . LYS A 1 405 ? 22.380 -1.668  74.208 1.00 40.67  ?  362 LYS A C   1 
ATOM   2933 O O   . LYS A 1 405 ? 23.364 -1.990  74.885 1.00 43.85  ?  362 LYS A O   1 
ATOM   2934 C CB  . LYS A 1 405 ? 21.248 0.557   74.527 1.00 43.00  ?  362 LYS A CB  1 
ATOM   2935 C CG  . LYS A 1 405 ? 21.617 0.584   76.009 1.00 47.35  ?  362 LYS A CG  1 
ATOM   2936 C CD  . LYS A 1 405 ? 20.839 1.656   76.778 1.00 53.53  ?  362 LYS A CD  1 
ATOM   2937 C CE  . LYS A 1 405 ? 21.227 3.062   76.318 1.00 52.60  ?  362 LYS A CE  1 
ATOM   2938 N NZ  . LYS A 1 405 ? 20.902 4.097   77.354 1.00 71.90  ?  362 LYS A NZ  1 
ATOM   2939 N N   . GLU A 1 406 ? 21.420 -2.543  73.902 1.00 42.67  ?  363 GLU A N   1 
ATOM   2940 C CA  . GLU A 1 406 ? 21.485 -3.893  74.457 1.00 46.05  ?  363 GLU A CA  1 
ATOM   2941 C C   . GLU A 1 406 ? 22.677 -4.664  73.900 1.00 43.63  ?  363 GLU A C   1 
ATOM   2942 O O   . GLU A 1 406 ? 23.372 -5.370  74.641 1.00 45.78  ?  363 GLU A O   1 
ATOM   2943 C CB  . GLU A 1 406 ? 20.178 -4.636  74.184 1.00 58.70  ?  363 GLU A CB  1 
ATOM   2944 C CG  . GLU A 1 406 ? 19.920 -5.815  75.128 1.00 62.03  ?  363 GLU A CG  1 
ATOM   2945 C CD  . GLU A 1 406 ? 19.945 -5.412  76.604 1.00 72.74  ?  363 GLU A CD  1 
ATOM   2946 O OE1 . GLU A 1 406 ? 20.386 -6.233  77.439 1.00 72.11  ?  363 GLU A OE1 1 
ATOM   2947 O OE2 . GLU A 1 406 ? 19.529 -4.277  76.929 1.00 62.52  ?  363 GLU A OE2 1 
ATOM   2948 N N   . LEU A 1 407 ? 22.939 -4.537  72.597 1.00 47.37  ?  364 LEU A N   1 
ATOM   2949 C CA  . LEU A 1 407 ? 24.081 -5.238  72.024 1.00 40.85  ?  364 LEU A CA  1 
ATOM   2950 C C   . LEU A 1 407 ? 25.393 -4.661  72.537 1.00 43.29  ?  364 LEU A C   1 
ATOM   2951 O O   . LEU A 1 407 ? 26.343 -5.406  72.808 1.00 42.44  ?  364 LEU A O   1 
ATOM   2952 C CB  . LEU A 1 407 ? 23.999 -5.194  70.500 1.00 43.71  ?  364 LEU A CB  1 
ATOM   2953 C CG  . LEU A 1 407 ? 22.792 -5.994  70.005 1.00 49.87  ?  364 LEU A CG  1 
ATOM   2954 C CD1 . LEU A 1 407 ? 22.582 -5.825  68.510 1.00 52.95  ?  364 LEU A CD1 1 
ATOM   2955 C CD2 . LEU A 1 407 ? 22.983 -7.463  70.360 1.00 47.02  ?  364 LEU A CD2 1 
ATOM   2956 N N   . ILE A 1 408 ? 25.462 -3.337  72.709 1.00 46.28  ?  365 ILE A N   1 
ATOM   2957 C CA  . ILE A 1 408 ? 26.645 -2.747  73.336 1.00 41.43  ?  365 ILE A CA  1 
ATOM   2958 C C   . ILE A 1 408 ? 26.809 -3.281  74.753 1.00 38.60  ?  365 ILE A C   1 
ATOM   2959 O O   . ILE A 1 408 ? 27.923 -3.598  75.190 1.00 42.21  ?  365 ILE A O   1 
ATOM   2960 C CB  . ILE A 1 408 ? 26.559 -1.206  73.307 1.00 38.71  ?  365 ILE A CB  1 
ATOM   2961 C CG1 . ILE A 1 408 ? 26.589 -0.694  71.860 1.00 40.75  ?  365 ILE A CG1 1 
ATOM   2962 C CG2 . ILE A 1 408 ? 27.691 -0.589  74.123 1.00 38.46  ?  365 ILE A CG2 1 
ATOM   2963 C CD1 . ILE A 1 408 ? 26.126 0.744   71.709 1.00 39.33  ?  365 ILE A CD1 1 
ATOM   2964 N N   . LYS A 1 409 ? 25.699 -3.410  75.488 1.00 40.86  ?  366 LYS A N   1 
ATOM   2965 C CA  . LYS A 1 409 ? 25.764 -3.952  76.849 1.00 42.86  ?  366 LYS A CA  1 
ATOM   2966 C C   . LYS A 1 409 ? 26.373 -5.351  76.850 1.00 40.86  ?  366 LYS A C   1 
ATOM   2967 O O   . LYS A 1 409 ? 27.287 -5.646  77.631 1.00 45.03  ?  366 LYS A O   1 
ATOM   2968 C CB  . LYS A 1 409 ? 24.363 -3.965  77.467 1.00 40.99  ?  366 LYS A CB  1 
ATOM   2969 C CG  . LYS A 1 409 ? 24.297 -4.330  78.953 1.00 49.46  ?  366 LYS A CG  1 
ATOM   2970 C CD  . LYS A 1 409 ? 22.836 -4.373  79.398 1.00 48.29  ?  366 LYS A CD  1 
ATOM   2971 C CE  . LYS A 1 409 ? 22.700 -4.538  80.907 1.00 52.12  ?  366 LYS A CE  1 
ATOM   2972 N NZ  . LYS A 1 409 ? 23.458 -5.712  81.397 1.00 59.92  ?  366 LYS A NZ  1 
ATOM   2973 N N   . ASP A 1 410 ? 25.884 -6.224  75.964 1.00 50.49  ?  367 ASP A N   1 
ATOM   2974 C CA  . ASP A 1 410 ? 26.462 -7.560  75.826 1.00 50.69  ?  367 ASP A CA  1 
ATOM   2975 C C   . ASP A 1 410 ? 27.962 -7.485  75.576 1.00 45.70  ?  367 ASP A C   1 
ATOM   2976 O O   . ASP A 1 410 ? 28.751 -8.168  76.236 1.00 49.78  ?  367 ASP A O   1 
ATOM   2977 C CB  . ASP A 1 410 ? 25.768 -8.315  74.687 1.00 52.06  ?  367 ASP A CB  1 
ATOM   2978 C CG  . ASP A 1 410 ? 24.287 -8.511  74.939 1.00 53.50  ?  367 ASP A CG  1 
ATOM   2979 O OD1 . ASP A 1 410 ? 23.869 -8.499  76.119 1.00 61.49  ?  367 ASP A OD1 1 
ATOM   2980 O OD2 . ASP A 1 410 ? 23.538 -8.672  73.954 1.00 70.07  ?  367 ASP A OD2 1 
ATOM   2981 N N   . TRP A 1 411 ? 28.375 -6.644  74.626 1.00 45.03  ?  368 TRP A N   1 
ATOM   2982 C CA  . TRP A 1 411 ? 29.796 -6.504  74.331 1.00 47.37  ?  368 TRP A CA  1 
ATOM   2983 C C   . TRP A 1 411 ? 30.566 -6.041  75.559 1.00 49.71  ?  368 TRP A C   1 
ATOM   2984 O O   . TRP A 1 411 ? 31.637 -6.575  75.878 1.00 51.47  ?  368 TRP A O   1 
ATOM   2985 C CB  . TRP A 1 411 ? 30.007 -5.527  73.168 1.00 43.51  ?  368 TRP A CB  1 
ATOM   2986 C CG  . TRP A 1 411 ? 31.469 -5.307  72.864 1.00 53.20  ?  368 TRP A CG  1 
ATOM   2987 C CD1 . TRP A 1 411 ? 32.231 -5.995  71.957 1.00 50.94  ?  368 TRP A CD1 1 
ATOM   2988 C CD2 . TRP A 1 411 ? 32.349 -4.354  73.483 1.00 53.61  ?  368 TRP A CD2 1 
ATOM   2989 N NE1 . TRP A 1 411 ? 33.523 -5.524  71.971 1.00 52.52  ?  368 TRP A NE1 1 
ATOM   2990 C CE2 . TRP A 1 411 ? 33.623 -4.519  72.897 1.00 56.09  ?  368 TRP A CE2 1 
ATOM   2991 C CE3 . TRP A 1 411 ? 32.183 -3.376  74.474 1.00 51.79  ?  368 TRP A CE3 1 
ATOM   2992 C CZ2 . TRP A 1 411 ? 34.724 -3.745  73.269 1.00 51.44  ?  368 TRP A CZ2 1 
ATOM   2993 C CZ3 . TRP A 1 411 ? 33.280 -2.606  74.843 1.00 46.40  ?  368 TRP A CZ3 1 
ATOM   2994 C CH2 . TRP A 1 411 ? 34.534 -2.797  74.243 1.00 51.19  ?  368 TRP A CH2 1 
ATOM   2995 N N   . PHE A 1 412 ? 30.037 -5.038  76.261 1.00 52.46  ?  369 PHE A N   1 
ATOM   2996 C CA  . PHE A 1 412 ? 30.776 -4.455  77.377 1.00 46.61  ?  369 PHE A CA  1 
ATOM   2997 C C   . PHE A 1 412 ? 30.959 -5.457  78.510 1.00 48.26  ?  369 PHE A C   1 
ATOM   2998 O O   . PHE A 1 412 ? 32.061 -5.606  79.051 1.00 50.37  ?  369 PHE A O   1 
ATOM   2999 C CB  . PHE A 1 412 ? 30.067 -3.198  77.878 1.00 45.01  ?  369 PHE A CB  1 
ATOM   3000 C CG  . PHE A 1 412 ? 30.747 -2.557  79.045 1.00 42.82  ?  369 PHE A CG  1 
ATOM   3001 C CD1 . PHE A 1 412 ? 31.874 -1.770  78.859 1.00 43.24  ?  369 PHE A CD1 1 
ATOM   3002 C CD2 . PHE A 1 412 ? 30.271 -2.754  80.335 1.00 43.68  ?  369 PHE A CD2 1 
ATOM   3003 C CE1 . PHE A 1 412 ? 32.517 -1.177  79.944 1.00 42.19  ?  369 PHE A CE1 1 
ATOM   3004 C CE2 . PHE A 1 412 ? 30.903 -2.162  81.423 1.00 41.94  ?  369 PHE A CE2 1 
ATOM   3005 C CZ  . PHE A 1 412 ? 32.022 -1.373  81.232 1.00 42.50  ?  369 PHE A CZ  1 
ATOM   3006 N N   . GLU A 1 413 ? 29.886 -6.150  78.891 1.00 52.93  ?  370 GLU A N   1 
ATOM   3007 C CA  . GLU A 1 413 ? 29.995 -7.089  80.000 1.00 59.22  ?  370 GLU A CA  1 
ATOM   3008 C C   . GLU A 1 413 ? 30.987 -8.201  79.689 1.00 60.90  ?  370 GLU A C   1 
ATOM   3009 O O   . GLU A 1 413 ? 31.697 -8.670  80.587 1.00 61.07  ?  370 GLU A O   1 
ATOM   3010 C CB  . GLU A 1 413 ? 28.615 -7.651  80.336 1.00 59.45  ?  370 GLU A CB  1 
ATOM   3011 C CG  . GLU A 1 413 ? 27.626 -6.551  80.685 1.00 62.06  ?  370 GLU A CG  1 
ATOM   3012 C CD  . GLU A 1 413 ? 26.313 -7.075  81.214 1.00 68.20  ?  370 GLU A CD  1 
ATOM   3013 O OE1 . GLU A 1 413 ? 25.852 -6.563  82.257 1.00 64.25  ?  370 GLU A OE1 1 
ATOM   3014 O OE2 . GLU A 1 413 ? 25.744 -7.992  80.583 1.00 72.16  ?  370 GLU A OE2 1 
ATOM   3015 N N   . ASP A 1 414 ? 31.071 -8.620  78.427 1.00 53.89  ?  371 ASP A N   1 
ATOM   3016 C CA  . ASP A 1 414 ? 32.095 -9.586  78.045 1.00 59.10  ?  371 ASP A CA  1 
ATOM   3017 C C   . ASP A 1 414 ? 33.496 -8.985  78.157 1.00 63.22  ?  371 ASP A C   1 
ATOM   3018 O O   . ASP A 1 414 ? 34.381 -9.568  78.796 1.00 62.75  ?  371 ASP A O   1 
ATOM   3019 C CB  . ASP A 1 414 ? 31.835 -10.097 76.626 1.00 65.35  ?  371 ASP A CB  1 
ATOM   3020 C CG  . ASP A 1 414 ? 32.919 -11.044 76.143 1.00 73.93  ?  371 ASP A CG  1 
ATOM   3021 O OD1 . ASP A 1 414 ? 32.969 -12.191 76.634 1.00 80.17  ?  371 ASP A OD1 1 
ATOM   3022 O OD2 . ASP A 1 414 ? 33.732 -10.641 75.284 1.00 79.22  ?  371 ASP A OD2 1 
ATOM   3023 N N   . GLU A 1 415 ? 33.715 -7.811  77.551 1.00 56.49  ?  372 GLU A N   1 
ATOM   3024 C CA  . GLU A 1 415 ? 35.064 -7.248  77.485 1.00 52.65  ?  372 GLU A CA  1 
ATOM   3025 C C   . GLU A 1 415 ? 35.541 -6.701  78.826 1.00 57.68  ?  372 GLU A C   1 
ATOM   3026 O O   . GLU A 1 415 ? 36.747 -6.710  79.099 1.00 52.94  ?  372 GLU A O   1 
ATOM   3027 C CB  . GLU A 1 415 ? 35.124 -6.145  76.429 1.00 56.58  ?  372 GLU A CB  1 
ATOM   3028 C CG  . GLU A 1 415 ? 35.026 -6.654  74.998 1.00 69.04  ?  372 GLU A CG  1 
ATOM   3029 C CD  . GLU A 1 415 ? 36.333 -7.243  74.495 1.00 68.57  ?  372 GLU A CD  1 
ATOM   3030 O OE1 . GLU A 1 415 ? 37.410 -6.761  74.913 1.00 65.38  ?  372 GLU A OE1 1 
ATOM   3031 O OE2 . GLU A 1 415 ? 36.280 -8.189  73.678 1.00 83.16  ?  372 GLU A OE2 1 
ATOM   3032 N N   . TYR A 1 416 ? 34.630 -6.216  79.663 1.00 58.37  ?  373 TYR A N   1 
ATOM   3033 C CA  . TYR A 1 416 ? 35.003 -5.596  80.933 1.00 56.10  ?  373 TYR A CA  1 
ATOM   3034 C C   . TYR A 1 416 ? 35.140 -6.636  82.043 1.00 55.49  ?  373 TYR A C   1 
ATOM   3035 O O   . TYR A 1 416 ? 36.079 -6.585  82.833 1.00 60.47  ?  373 TYR A O   1 
ATOM   3036 C CB  . TYR A 1 416 ? 33.966 -4.539  81.320 1.00 52.67  ?  373 TYR A CB  1 
ATOM   3037 C CG  . TYR A 1 416 ? 34.298 -3.736  82.566 1.00 56.55  ?  373 TYR A CG  1 
ATOM   3038 C CD1 . TYR A 1 416 ? 35.085 -2.593  82.492 1.00 49.69  ?  373 TYR A CD1 1 
ATOM   3039 C CD2 . TYR A 1 416 ? 33.797 -4.107  83.809 1.00 54.24  ?  373 TYR A CD2 1 
ATOM   3040 C CE1 . TYR A 1 416 ? 35.377 -1.845  83.631 1.00 54.56  ?  373 TYR A CE1 1 
ATOM   3041 C CE2 . TYR A 1 416 ? 34.082 -3.368  84.949 1.00 53.11  ?  373 TYR A CE2 1 
ATOM   3042 C CZ  . TYR A 1 416 ? 34.872 -2.242  84.852 1.00 57.97  ?  373 TYR A CZ  1 
ATOM   3043 O OH  . TYR A 1 416 ? 35.150 -1.516  85.985 1.00 54.21  ?  373 TYR A OH  1 
HETATM 3044 P P   . PO4 B 2 .   ? 38.197 18.044  64.221 1.00 36.78  ?  501 PO4 A P   1 
HETATM 3045 O O1  . PO4 B 2 .   ? 39.346 17.626  63.318 1.00 37.60  ?  501 PO4 A O1  1 
HETATM 3046 O O2  . PO4 B 2 .   ? 36.941 17.328  63.790 1.00 38.40  ?  501 PO4 A O2  1 
HETATM 3047 O O3  . PO4 B 2 .   ? 37.940 19.533  64.109 1.00 35.16  ?  501 PO4 A O3  1 
HETATM 3048 O O4  . PO4 B 2 .   ? 38.602 17.659  65.632 1.00 34.46  ?  501 PO4 A O4  1 
HETATM 3049 C C1  . GOL C 3 .   ? 33.595 15.613  62.346 1.00 41.14  ?  502 GOL A C1  1 
HETATM 3050 O O1  . GOL C 3 .   ? 32.579 15.888  61.424 1.00 42.59  ?  502 GOL A O1  1 
HETATM 3051 C C2  . GOL C 3 .   ? 33.110 15.962  63.761 1.00 52.65  ?  502 GOL A C2  1 
HETATM 3052 O O2  . GOL C 3 .   ? 31.753 15.635  63.923 1.00 53.82  ?  502 GOL A O2  1 
HETATM 3053 C C3  . GOL C 3 .   ? 33.893 15.121  64.771 1.00 52.34  ?  502 GOL A C3  1 
HETATM 3054 O O3  . GOL C 3 .   ? 34.658 15.938  65.604 1.00 61.74  ?  502 GOL A O3  1 
HETATM 3055 H H11 . GOL C 3 .   ? 33.823 14.671  62.305 1.00 49.37  ?  502 GOL A H11 1 
HETATM 3056 H H12 . GOL C 3 .   ? 34.378 16.144  62.132 1.00 49.37  ?  502 GOL A H12 1 
HETATM 3057 H HO1 . GOL C 3 .   ? 32.921 16.194  60.709 1.00 51.11  ?  502 GOL A HO1 1 
HETATM 3058 H H2  . GOL C 3 .   ? 33.241 16.914  63.898 1.00 63.18  ?  502 GOL A H2  1 
HETATM 3059 H HO2 . GOL C 3 .   ? 31.278 16.152  63.444 1.00 64.58  ?  502 GOL A HO2 1 
HETATM 3060 H H31 . GOL C 3 .   ? 34.480 14.514  64.293 1.00 62.81  ?  502 GOL A H31 1 
HETATM 3061 H H32 . GOL C 3 .   ? 33.270 14.610  65.311 1.00 62.81  ?  502 GOL A H32 1 
HETATM 3062 H HO3 . GOL C 3 .   ? 35.239 15.466  66.007 1.00 74.09  ?  502 GOL A HO3 1 
HETATM 3063 C C1  . GOL D 3 .   ? 40.144 14.427  65.057 1.00 41.95  ?  503 GOL A C1  1 
HETATM 3064 O O1  . GOL D 3 .   ? 39.869 13.720  66.235 1.00 39.39  ?  503 GOL A O1  1 
HETATM 3065 C C2  . GOL D 3 .   ? 41.228 15.484  65.296 1.00 40.92  ?  503 GOL A C2  1 
HETATM 3066 O O2  . GOL D 3 .   ? 40.807 16.431  66.250 1.00 39.22  ?  503 GOL A O2  1 
HETATM 3067 C C3  . GOL D 3 .   ? 42.547 14.881  65.783 1.00 41.79  ?  503 GOL A C3  1 
HETATM 3068 O O3  . GOL D 3 .   ? 43.451 15.920  66.087 1.00 43.23  ?  503 GOL A O3  1 
HETATM 3069 H H11 . GOL D 3 .   ? 40.450 13.806  64.378 1.00 50.33  ?  503 GOL A H11 1 
HETATM 3070 H H12 . GOL D 3 .   ? 39.334 14.865  64.753 1.00 50.33  ?  503 GOL A H12 1 
HETATM 3071 H HO1 . GOL D 3 .   ? 40.544 13.249  66.447 1.00 47.27  ?  503 GOL A HO1 1 
HETATM 3072 H H2  . GOL D 3 .   ? 41.376 15.905  64.435 1.00 49.10  ?  503 GOL A H2  1 
HETATM 3073 H HO2 . GOL D 3 .   ? 40.177 16.900  65.926 1.00 47.06  ?  503 GOL A HO2 1 
HETATM 3074 H H31 . GOL D 3 .   ? 42.922 14.319  65.087 1.00 50.15  ?  503 GOL A H31 1 
HETATM 3075 H H32 . GOL D 3 .   ? 42.386 14.348  66.577 1.00 50.15  ?  503 GOL A H32 1 
HETATM 3076 H HO3 . GOL D 3 .   ? 43.997 15.655  66.682 1.00 51.88  ?  503 GOL A HO3 1 
HETATM 3077 C C   . ACT E 4 .   ? 39.457 67.406  61.928 1.00 61.33  ?  504 ACT A C   1 
HETATM 3078 O O   . ACT E 4 .   ? 39.722 67.990  60.824 1.00 52.61  ?  504 ACT A O   1 
HETATM 3079 O OXT . ACT E 4 .   ? 39.410 68.058  63.003 1.00 62.86  -1 504 ACT A OXT 1 
HETATM 3080 C CH3 . ACT E 4 .   ? 39.203 65.901  62.000 1.00 60.78  ?  504 ACT A CH3 1 
HETATM 3081 H H1  . ACT E 4 .   ? 38.824 65.678  62.865 1.00 72.94  ?  504 ACT A H1  1 
HETATM 3082 H H2  . ACT E 4 .   ? 40.041 65.426  61.883 1.00 72.94  ?  504 ACT A H2  1 
HETATM 3083 H H3  . ACT E 4 .   ? 38.585 65.643  61.299 1.00 72.94  ?  504 ACT A H3  1 
HETATM 3084 C C   . ACT F 4 .   ? 40.947 19.655  70.787 1.00 71.18  ?  505 ACT A C   1 
HETATM 3085 O O   . ACT F 4 .   ? 41.685 19.558  69.762 1.00 66.49  -1 505 ACT A O   1 
HETATM 3086 O OXT . ACT F 4 .   ? 41.150 18.918  71.787 1.00 74.79  ?  505 ACT A OXT 1 
HETATM 3087 C CH3 . ACT F 4 .   ? 39.800 20.664  70.828 1.00 58.56  ?  505 ACT A CH3 1 
HETATM 3088 H H1  . ACT F 4 .   ? 40.041 21.403  71.408 1.00 70.27  ?  505 ACT A H1  1 
HETATM 3089 H H2  . ACT F 4 .   ? 39.002 20.232  71.170 1.00 70.27  ?  505 ACT A H2  1 
HETATM 3090 H H3  . ACT F 4 .   ? 39.630 20.997  69.933 1.00 70.27  ?  505 ACT A H3  1 
HETATM 3091 C C   . ACT G 4 .   ? 39.388 48.309  46.269 1.00 57.11  ?  506 ACT A C   1 
HETATM 3092 O O   . ACT G 4 .   ? 39.412 49.506  45.858 1.00 53.53  ?  506 ACT A O   1 
HETATM 3093 O OXT . ACT G 4 .   ? 39.714 48.020  47.460 1.00 57.41  -1 506 ACT A OXT 1 
HETATM 3094 C CH3 . ACT G 4 .   ? 38.963 47.204  45.307 1.00 48.48  ?  506 ACT A CH3 1 
HETATM 3095 H H1  . ACT G 4 .   ? 38.883 46.367  45.791 1.00 58.18  ?  506 ACT A H1  1 
HETATM 3096 H H2  . ACT G 4 .   ? 39.629 47.111  44.608 1.00 58.18  ?  506 ACT A H2  1 
HETATM 3097 H H3  . ACT G 4 .   ? 38.108 47.431  44.911 1.00 58.18  ?  506 ACT A H3  1 
HETATM 3098 O O   . HOH H 5 .   ? 45.075 54.538  51.451 1.00 58.77  ?  601 HOH A O   1 
HETATM 3099 O O   . HOH H 5 .   ? 64.770 44.929  59.829 1.00 49.06  ?  602 HOH A O   1 
HETATM 3100 O O   . HOH H 5 .   ? 43.637 23.594  66.506 1.00 51.18  ?  603 HOH A O   1 
HETATM 3101 O O   . HOH H 5 .   ? 20.799 62.842  38.895 1.00 55.54  ?  604 HOH A O   1 
HETATM 3102 O O   . HOH H 5 .   ? 57.343 24.421  61.845 1.00 45.55  ?  605 HOH A O   1 
HETATM 3103 O O   . HOH H 5 .   ? 61.450 55.370  43.234 1.00 47.55  ?  606 HOH A O   1 
HETATM 3104 O O   . HOH H 5 .   ? 25.917 7.967   58.859 1.00 44.72  ?  607 HOH A O   1 
HETATM 3105 O O   . HOH H 5 .   ? 35.712 20.639  64.333 1.00 48.43  ?  608 HOH A O   1 
HETATM 3106 O O   . HOH H 5 .   ? 44.356 9.252   51.526 1.00 63.07  ?  609 HOH A O   1 
HETATM 3107 O O   . HOH H 5 .   ? 25.393 13.136  64.199 1.00 47.92  ?  610 HOH A O   1 
HETATM 3108 O O   . HOH H 5 .   ? 43.825 47.853  52.258 1.00 41.84  ?  611 HOH A O   1 
HETATM 3109 O O   . HOH H 5 .   ? 38.214 9.876   73.507 1.00 49.89  ?  612 HOH A O   1 
HETATM 3110 O O   . HOH H 5 .   ? 55.397 33.424  42.242 1.00 49.02  ?  613 HOH A O   1 
HETATM 3111 O O   . HOH H 5 .   ? 61.245 48.888  64.673 1.00 59.18  ?  614 HOH A O   1 
HETATM 3112 O O   . HOH H 5 .   ? 23.779 8.578   60.835 1.00 50.58  ?  615 HOH A O   1 
HETATM 3113 O O   . HOH H 5 .   ? 23.195 66.146  61.917 1.00 49.79  ?  616 HOH A O   1 
HETATM 3114 O O   . HOH H 5 .   ? 20.919 68.335  42.886 1.00 49.78  ?  617 HOH A O   1 
HETATM 3115 O O   . HOH H 5 .   ? 52.923 63.326  53.212 1.00 52.52  ?  618 HOH A O   1 
HETATM 3116 O O   . HOH H 5 .   ? 38.585 45.216  40.799 1.00 54.38  ?  619 HOH A O   1 
HETATM 3117 O O   . HOH H 5 .   ? 24.882 48.688  48.943 1.00 49.58  ?  620 HOH A O   1 
HETATM 3118 O O   . HOH H 5 .   ? 20.604 61.973  61.765 1.00 56.42  ?  621 HOH A O   1 
HETATM 3119 O O   . HOH H 5 .   ? 30.538 64.415  53.082 1.00 39.37  ?  622 HOH A O   1 
HETATM 3120 O O   . HOH H 5 .   ? 48.843 20.154  62.514 1.00 46.02  ?  623 HOH A O   1 
HETATM 3121 O O   . HOH H 5 .   ? 35.352 14.371  67.529 1.00 51.75  ?  624 HOH A O   1 
HETATM 3122 O O   . HOH H 5 .   ? 36.117 22.289  59.371 1.00 39.63  ?  625 HOH A O   1 
HETATM 3123 O O   . HOH H 5 .   ? 44.951 19.578  44.241 1.00 47.53  ?  626 HOH A O   1 
HETATM 3124 O O   . HOH H 5 .   ? 47.683 53.563  39.074 1.00 29.66  ?  627 HOH A O   1 
HETATM 3125 O O   . HOH H 5 .   ? 40.600 70.344  58.949 1.00 48.39  ?  628 HOH A O   1 
HETATM 3126 O O   . HOH H 5 .   ? 39.795 3.839   74.014 1.00 41.40  ?  629 HOH A O   1 
HETATM 3127 O O   . HOH H 5 .   ? 50.756 54.761  32.002 1.00 40.98  ?  630 HOH A O   1 
HETATM 3128 O O   . HOH H 5 .   ? 31.067 11.829  60.150 1.00 35.97  ?  631 HOH A O   1 
HETATM 3129 O O   . HOH H 5 .   ? 27.935 8.760   74.434 1.00 44.64  ?  632 HOH A O   1 
HETATM 3130 O O   . HOH H 5 .   ? 36.078 22.676  51.197 1.00 58.35  ?  633 HOH A O   1 
HETATM 3131 O O   . HOH H 5 .   ? 42.851 51.746  47.899 1.00 42.77  ?  634 HOH A O   1 
HETATM 3132 O O   . HOH H 5 .   ? 58.153 54.314  36.373 1.00 33.08  ?  635 HOH A O   1 
HETATM 3133 O O   . HOH H 5 .   ? 38.390 25.796  52.198 1.00 49.91  ?  636 HOH A O   1 
HETATM 3134 O O   . HOH H 5 .   ? 40.643 34.171  41.882 1.00 47.90  ?  637 HOH A O   1 
HETATM 3135 O O   . HOH H 5 .   ? 18.445 57.604  54.013 1.00 43.89  ?  638 HOH A O   1 
HETATM 3136 O O   . HOH H 5 .   ? 28.386 13.039  56.210 1.00 43.58  ?  639 HOH A O   1 
HETATM 3137 O O   . HOH H 5 .   ? 18.090 61.309  48.718 1.00 54.00  ?  640 HOH A O   1 
HETATM 3138 O O   . HOH H 5 .   ? 25.525 -0.877  89.012 1.00 48.45  ?  641 HOH A O   1 
HETATM 3139 O O   . HOH H 5 .   ? 30.613 62.518  55.622 1.00 43.95  ?  642 HOH A O   1 
HETATM 3140 O O   . HOH H 5 .   ? 30.241 16.881  65.709 1.00 52.61  ?  643 HOH A O   1 
HETATM 3141 O O   . HOH H 5 .   ? 38.729 29.652  57.016 1.00 55.09  ?  644 HOH A O   1 
HETATM 3142 O O   . HOH H 5 .   ? 54.111 58.483  40.827 1.00 43.97  ?  645 HOH A O   1 
HETATM 3143 O O   . HOH H 5 .   ? 40.550 55.925  46.425 1.00 35.95  ?  646 HOH A O   1 
HETATM 3144 O O   . HOH H 5 .   ? 54.657 33.648  62.980 1.00 43.52  ?  647 HOH A O   1 
HETATM 3145 O O   . HOH H 5 .   ? 34.247 53.951  44.999 1.00 36.45  ?  648 HOH A O   1 
HETATM 3146 O O   . HOH H 5 .   ? 44.817 35.043  67.130 1.00 46.62  ?  649 HOH A O   1 
HETATM 3147 O O   . HOH H 5 .   ? 27.634 67.284  37.165 1.00 45.75  ?  650 HOH A O   1 
HETATM 3148 O O   . HOH H 5 .   ? 38.488 31.707  55.664 1.00 53.96  ?  651 HOH A O   1 
HETATM 3149 O O   . HOH H 5 .   ? 48.603 54.211  26.009 1.00 50.79  ?  652 HOH A O   1 
HETATM 3150 O O   . HOH H 5 .   ? 40.636 38.130  55.495 1.00 51.47  ?  653 HOH A O   1 
HETATM 3151 O O   . HOH H 5 .   ? 43.848 61.301  39.074 1.00 39.14  ?  654 HOH A O   1 
HETATM 3152 O O   . HOH H 5 .   ? 42.598 29.541  48.369 1.00 36.83  ?  655 HOH A O   1 
HETATM 3153 O O   . HOH H 5 .   ? 29.763 10.665  85.411 1.00 42.00  ?  656 HOH A O   1 
HETATM 3154 O O   . HOH H 5 .   ? 39.605 18.622  47.936 1.00 49.67  ?  657 HOH A O   1 
HETATM 3155 O O   . HOH H 5 .   ? 51.522 39.491  65.897 1.00 41.14  ?  658 HOH A O   1 
HETATM 3156 O O   . HOH H 5 .   ? 38.204 13.084  70.335 1.00 47.12  ?  659 HOH A O   1 
HETATM 3157 O O   . HOH H 5 .   ? 31.515 18.310  60.881 1.00 46.53  ?  660 HOH A O   1 
HETATM 3158 O O   . HOH H 5 .   ? 37.517 25.424  62.063 1.00 48.63  ?  661 HOH A O   1 
HETATM 3159 O O   . HOH H 5 .   ? 47.502 60.155  52.924 1.00 41.34  ?  662 HOH A O   1 
HETATM 3160 O O   . HOH H 5 .   ? 43.317 62.009  50.821 1.00 37.56  ?  663 HOH A O   1 
HETATM 3161 O O   . HOH H 5 .   ? 42.705 71.245  56.305 1.00 47.56  ?  664 HOH A O   1 
HETATM 3162 O O   . HOH H 5 .   ? 62.479 40.027  49.490 1.00 36.58  ?  665 HOH A O   1 
HETATM 3163 O O   . HOH H 5 .   ? 60.277 59.887  44.456 1.00 60.84  ?  666 HOH A O   1 
HETATM 3164 O O   . HOH H 5 .   ? 36.498 62.040  50.459 1.00 39.91  ?  667 HOH A O   1 
HETATM 3165 O O   . HOH H 5 .   ? 57.005 35.287  47.481 1.00 43.35  ?  668 HOH A O   1 
HETATM 3166 O O   . HOH H 5 .   ? 18.944 68.016  49.532 1.00 47.59  ?  669 HOH A O   1 
HETATM 3167 O O   . HOH H 5 .   ? 20.604 60.257  59.671 1.00 55.95  ?  670 HOH A O   1 
HETATM 3168 O O   . HOH H 5 .   ? 32.015 4.727   98.526 1.00 52.63  ?  671 HOH A O   1 
HETATM 3169 O O   . HOH H 5 .   ? 28.992 -1.338  92.717 1.00 55.66  ?  672 HOH A O   1 
HETATM 3170 O O   . HOH H 5 .   ? 62.715 52.173  58.927 1.00 59.69  ?  673 HOH A O   1 
HETATM 3171 O O   . HOH H 5 .   ? 37.871 23.044  61.037 1.00 48.74  ?  674 HOH A O   1 
HETATM 3172 O O   . HOH H 5 .   ? 34.552 72.625  50.891 1.00 50.53  ?  675 HOH A O   1 
HETATM 3173 O O   . HOH H 5 .   ? 35.750 68.994  54.329 1.00 44.19  ?  676 HOH A O   1 
HETATM 3174 O O   . HOH H 5 .   ? 33.604 11.555  68.701 1.00 37.81  ?  677 HOH A O   1 
HETATM 3175 O O   . HOH H 5 .   ? 42.839 40.355  59.450 1.00 44.12  ?  678 HOH A O   1 
HETATM 3176 O O   . HOH H 5 .   ? 45.530 40.052  44.604 1.00 39.06  ?  679 HOH A O   1 
HETATM 3177 O O   . HOH H 5 .   ? 34.255 70.853  53.094 1.00 42.31  ?  680 HOH A O   1 
HETATM 3178 O O   . HOH H 5 .   ? 23.519 61.043  35.506 1.00 50.19  ?  681 HOH A O   1 
HETATM 3179 O O   . HOH H 5 .   ? 36.326 9.768   70.135 1.00 37.84  ?  682 HOH A O   1 
HETATM 3180 O O   . HOH H 5 .   ? 34.771 10.431  82.272 1.00 44.07  ?  683 HOH A O   1 
HETATM 3181 O O   . HOH H 5 .   ? 63.162 49.734  53.936 1.00 44.08  ?  684 HOH A O   1 
HETATM 3182 O O   . HOH H 5 .   ? 48.026 25.716  70.365 1.00 55.65  ?  685 HOH A O   1 
HETATM 3183 O O   . HOH H 5 .   ? 40.142 9.458   79.902 1.00 41.41  ?  686 HOH A O   1 
HETATM 3184 O O   . HOH H 5 .   ? 44.532 30.584  42.621 1.00 43.99  ?  687 HOH A O   1 
HETATM 3185 O O   . HOH H 5 .   ? 61.089 27.237  55.095 1.00 49.55  ?  688 HOH A O   1 
HETATM 3186 O O   . HOH H 5 .   ? 46.573 37.582  43.516 1.00 39.36  ?  689 HOH A O   1 
HETATM 3187 O O   . HOH H 5 .   ? 37.190 56.153  48.208 1.00 48.69  ?  690 HOH A O   1 
HETATM 3188 O O   . HOH H 5 .   ? 38.610 33.269  44.897 1.00 48.51  ?  691 HOH A O   1 
HETATM 3189 O O   . HOH H 5 .   ? 33.350 57.684  50.564 1.00 45.76  ?  692 HOH A O   1 
HETATM 3190 O O   . HOH H 5 .   ? 58.005 29.701  64.935 1.00 41.56  ?  693 HOH A O   1 
HETATM 3191 O O   . HOH H 5 .   ? 42.547 8.560   61.864 1.00 41.62  ?  694 HOH A O   1 
HETATM 3192 O O   . HOH H 5 .   ? 35.753 9.131   74.537 1.00 39.19  ?  695 HOH A O   1 
HETATM 3193 O O   . HOH H 5 .   ? 32.080 5.007   54.206 1.00 48.08  ?  696 HOH A O   1 
HETATM 3194 O O   . HOH H 5 .   ? 42.038 26.416  67.315 1.00 47.05  ?  697 HOH A O   1 
HETATM 3195 O O   . HOH H 5 .   ? 28.868 14.855  59.241 1.00 47.94  ?  698 HOH A O   1 
HETATM 3196 O O   . HOH H 5 .   ? 49.788 58.810  35.488 1.00 47.36  ?  699 HOH A O   1 
HETATM 3197 O O   . HOH H 5 .   ? 22.709 6.498   80.711 1.00 55.35  ?  700 HOH A O   1 
HETATM 3198 O O   . HOH H 5 .   ? 46.336 23.860  44.700 1.00 39.77  ?  701 HOH A O   1 
HETATM 3199 O O   . HOH H 5 .   ? 30.047 -7.584  66.607 1.00 57.28  ?  702 HOH A O   1 
HETATM 3200 O O   . HOH H 5 .   ? 42.327 5.758   61.970 1.00 46.19  ?  703 HOH A O   1 
HETATM 3201 O O   . HOH H 5 .   ? 36.594 70.855  45.233 1.00 41.60  ?  704 HOH A O   1 
HETATM 3202 O O   . HOH H 5 .   ? 39.538 56.377  40.909 1.00 31.41  ?  705 HOH A O   1 
HETATM 3203 O O   . HOH H 5 .   ? 44.348 32.720  43.975 1.00 43.43  ?  706 HOH A O   1 
HETATM 3204 O O   . HOH H 5 .   ? 55.777 30.541  42.290 1.00 48.37  ?  707 HOH A O   1 
HETATM 3205 O O   . HOH H 5 .   ? 41.545 27.898  41.387 1.00 52.30  ?  708 HOH A O   1 
HETATM 3206 O O   . HOH H 5 .   ? 53.670 20.521  57.412 1.00 51.22  ?  709 HOH A O   1 
HETATM 3207 O O   . HOH H 5 .   ? 27.935 -0.106  63.493 1.00 43.14  ?  710 HOH A O   1 
HETATM 3208 O O   . HOH H 5 .   ? 36.364 4.626   89.090 1.00 50.94  ?  711 HOH A O   1 
HETATM 3209 O O   . HOH H 5 .   ? 55.583 57.041  38.486 1.00 41.79  ?  712 HOH A O   1 
HETATM 3210 O O   . HOH H 5 .   ? 28.746 65.901  40.563 1.00 39.05  ?  713 HOH A O   1 
HETATM 3211 O O   . HOH H 5 .   ? 44.595 38.929  61.971 1.00 44.51  ?  714 HOH A O   1 
HETATM 3212 O O   . HOH H 5 .   ? 65.054 41.049  49.898 1.00 39.48  ?  715 HOH A O   1 
HETATM 3213 O O   . HOH H 5 .   ? 40.084 33.865  56.626 1.00 48.92  ?  716 HOH A O   1 
HETATM 3214 O O   . HOH H 5 .   ? 49.440 43.390  33.068 1.00 50.72  ?  717 HOH A O   1 
HETATM 3215 O O   . HOH H 5 .   ? 32.224 12.767  64.347 1.00 40.54  ?  718 HOH A O   1 
HETATM 3216 O O   . HOH H 5 .   ? 41.518 44.823  35.263 1.00 48.34  ?  719 HOH A O   1 
HETATM 3217 O O   . HOH H 5 .   ? 50.073 44.058  64.932 1.00 41.18  ?  720 HOH A O   1 
HETATM 3218 O O   . HOH H 5 .   ? 17.248 62.000  51.314 1.00 46.41  ?  721 HOH A O   1 
HETATM 3219 O O   . HOH H 5 .   ? 47.429 33.046  65.161 1.00 39.39  ?  722 HOH A O   1 
HETATM 3220 O O   . HOH H 5 .   ? 32.078 18.037  58.273 1.00 40.84  ?  723 HOH A O   1 
HETATM 3221 O O   . HOH H 5 .   ? 29.772 15.321  61.898 1.00 50.93  ?  724 HOH A O   1 
HETATM 3222 O O   . HOH H 5 .   ? 23.255 51.174  39.413 1.00 38.60  ?  725 HOH A O   1 
HETATM 3223 O O   . HOH H 5 .   ? 58.225 37.561  62.189 1.00 50.20  ?  726 HOH A O   1 
HETATM 3224 O O   . HOH H 5 .   ? 17.488 51.429  52.262 1.00 50.66  ?  727 HOH A O   1 
HETATM 3225 O O   . HOH H 5 .   ? 40.763 39.696  53.291 1.00 40.54  ?  728 HOH A O   1 
HETATM 3226 O O   . HOH H 5 .   ? 50.490 64.282  45.258 1.00 45.75  ?  729 HOH A O   1 
HETATM 3227 O O   . HOH H 5 .   ? 51.804 15.340  52.364 1.00 58.96  ?  730 HOH A O   1 
HETATM 3228 O O   . HOH H 5 .   ? 47.770 44.941  66.011 1.00 49.53  ?  731 HOH A O   1 
HETATM 3229 O O   . HOH H 5 .   ? 41.721 72.458  53.215 1.00 55.30  ?  732 HOH A O   1 
HETATM 3230 O O   . HOH H 5 .   ? 22.498 46.509  43.608 1.00 56.04  ?  733 HOH A O   1 
HETATM 3231 O O   . HOH H 5 .   ? 40.921 36.980  59.482 1.00 56.70  ?  734 HOH A O   1 
HETATM 3232 O O   . HOH H 5 .   ? 19.531 1.357   71.615 1.00 47.16  ?  735 HOH A O   1 
HETATM 3233 O O   . HOH H 5 .   ? 45.818 55.705  60.765 1.00 67.26  ?  736 HOH A O   1 
HETATM 3234 O O   . HOH H 5 .   ? 56.711 43.279  36.350 1.00 55.55  ?  737 HOH A O   1 
HETATM 3235 O O   . HOH H 5 .   ? 39.336 6.406   85.799 1.00 42.25  ?  738 HOH A O   1 
HETATM 3236 O O   . HOH H 5 .   ? 22.637 4.254   64.719 1.00 50.94  ?  739 HOH A O   1 
HETATM 3237 O O   . HOH H 5 .   ? 40.637 66.048  34.907 1.00 44.72  ?  740 HOH A O   1 
HETATM 3238 O O   . HOH H 5 .   ? 38.226 22.791  52.483 1.00 46.64  ?  741 HOH A O   1 
HETATM 3239 O O   . HOH H 5 .   ? 50.365 22.702  62.784 1.00 43.31  ?  742 HOH A O   1 
HETATM 3240 O O   . HOH H 5 .   ? 46.433 67.517  50.450 1.00 46.10  ?  743 HOH A O   1 
HETATM 3241 O O   . HOH H 5 .   ? 54.081 44.528  61.794 1.00 54.44  ?  744 HOH A O   1 
HETATM 3242 O O   . HOH H 5 .   ? 39.757 22.792  50.183 1.00 44.15  ?  745 HOH A O   1 
HETATM 3243 O O   . HOH H 5 .   ? 24.698 73.501  57.386 1.00 51.11  ?  746 HOH A O   1 
HETATM 3244 O O   . HOH H 5 .   ? 26.498 -5.959  67.356 1.00 47.05  ?  747 HOH A O   1 
HETATM 3245 O O   . HOH H 5 .   ? 46.070 32.908  40.711 1.00 47.09  ?  748 HOH A O   1 
HETATM 3246 O O   . HOH H 5 .   ? 18.474 53.736  43.128 1.00 45.95  ?  749 HOH A O   1 
HETATM 3247 O O   . HOH H 5 .   ? 41.025 9.300   67.948 1.00 46.88  ?  750 HOH A O   1 
HETATM 3248 O O   . HOH H 5 .   ? 46.216 67.824  54.404 1.00 57.23  ?  751 HOH A O   1 
HETATM 3249 O O   . HOH H 5 .   ? 39.690 40.230  40.421 1.00 54.49  ?  752 HOH A O   1 
HETATM 3250 O O   . HOH H 5 .   ? 36.040 59.453  49.915 1.00 45.20  ?  753 HOH A O   1 
HETATM 3251 O O   . HOH H 5 .   ? 27.975 14.838  68.490 1.00 52.68  ?  754 HOH A O   1 
HETATM 3252 O O   . HOH H 5 .   ? 41.102 11.142  65.701 1.00 40.89  ?  755 HOH A O   1 
HETATM 3253 O O   . HOH H 5 .   ? 37.253 32.340  61.014 1.00 62.05  ?  756 HOH A O   1 
HETATM 3254 O O   . HOH H 5 .   ? 37.622 -0.460  69.673 1.00 46.94  ?  757 HOH A O   1 
HETATM 3255 O O   . HOH H 5 .   ? 44.141 45.706  55.227 1.00 51.07  ?  758 HOH A O   1 
HETATM 3256 O O   . HOH H 5 .   ? 39.669 24.933  68.067 1.00 47.31  ?  759 HOH A O   1 
HETATM 3257 O O   . HOH H 5 .   ? 34.791 2.413   91.538 1.00 49.93  ?  760 HOH A O   1 
HETATM 3258 O O   . HOH H 5 .   ? 18.153 62.492  44.740 1.00 51.57  ?  761 HOH A O   1 
HETATM 3259 O O   . HOH H 5 .   ? 18.517 51.459  40.891 1.00 39.89  ?  762 HOH A O   1 
HETATM 3260 O O   . HOH H 5 .   ? 35.127 62.952  31.176 1.00 46.73  ?  763 HOH A O   1 
HETATM 3261 O O   . HOH H 5 .   ? 48.517 29.775  68.629 1.00 46.08  ?  764 HOH A O   1 
HETATM 3262 O O   . HOH H 5 .   ? 50.604 18.525  61.459 1.00 53.39  ?  765 HOH A O   1 
HETATM 3263 O O   . HOH H 5 .   ? 60.653 21.934  58.442 1.00 62.87  ?  766 HOH A O   1 
HETATM 3264 O O   . HOH H 5 .   ? 33.037 20.313  57.149 1.00 40.12  ?  767 HOH A O   1 
HETATM 3265 O O   . HOH H 5 .   ? 43.425 7.141   66.273 1.00 54.61  ?  768 HOH A O   1 
HETATM 3266 O O   . HOH H 5 .   ? 52.055 24.303  65.425 1.00 45.47  ?  769 HOH A O   1 
HETATM 3267 O O   . HOH H 5 .   ? 64.941 50.572  44.939 1.00 46.26  ?  770 HOH A O   1 
HETATM 3268 O O   . HOH H 5 .   ? 50.898 60.837  39.803 1.00 50.01  ?  771 HOH A O   1 
HETATM 3269 O O   . HOH H 5 .   ? 50.407 34.657  38.003 1.00 47.39  ?  772 HOH A O   1 
HETATM 3270 O O   . HOH H 5 .   ? 19.678 57.637  60.727 1.00 51.46  ?  773 HOH A O   1 
HETATM 3271 O O   . HOH H 5 .   ? 30.280 73.147  51.130 1.00 54.48  ?  774 HOH A O   1 
HETATM 3272 O O   . HOH H 5 .   ? 55.356 39.913  39.285 1.00 48.00  ?  775 HOH A O   1 
HETATM 3273 O O   . HOH H 5 .   ? 44.973 60.610  52.641 1.00 43.05  ?  776 HOH A O   1 
HETATM 3274 O O   . HOH H 5 .   ? 38.584 53.744  46.636 1.00 52.36  ?  777 HOH A O   1 
HETATM 3275 O O   . HOH H 5 .   ? 50.311 41.098  37.623 1.00 41.99  ?  778 HOH A O   1 
HETATM 3276 O O   . HOH H 5 .   ? 53.222 64.122  46.138 1.00 45.37  ?  779 HOH A O   1 
HETATM 3277 O O   . HOH H 5 .   ? 68.028 42.050  56.161 1.00 41.14  ?  780 HOH A O   1 
HETATM 3278 O O   . HOH H 5 .   ? 54.648 55.110  58.094 1.00 64.61  ?  781 HOH A O   1 
HETATM 3279 O O   . HOH H 5 .   ? 39.070 33.292  67.769 1.00 48.82  ?  782 HOH A O   1 
HETATM 3280 O O   . HOH H 5 .   ? 22.263 10.592  80.475 1.00 58.50  ?  783 HOH A O   1 
HETATM 3281 O O   . HOH H 5 .   ? 21.847 7.064   64.430 1.00 49.08  ?  784 HOH A O   1 
HETATM 3282 O O   . HOH H 5 .   ? 48.384 49.726  60.768 1.00 48.56  ?  785 HOH A O   1 
HETATM 3283 O O   . HOH H 5 .   ? 32.002 12.848  67.098 1.00 38.02  ?  786 HOH A O   1 
HETATM 3284 O O   . HOH H 5 .   ? 30.470 72.265  54.337 1.00 56.01  ?  787 HOH A O   1 
HETATM 3285 O O   . HOH H 5 .   ? 40.610 10.092  63.291 1.00 38.78  ?  788 HOH A O   1 
HETATM 3286 O O   . HOH H 5 .   ? 52.832 53.832  57.940 1.00 40.66  ?  789 HOH A O   1 
HETATM 3287 O O   . HOH H 5 .   ? 25.197 0.371   63.724 1.00 44.10  ?  790 HOH A O   1 
HETATM 3288 O O   . HOH H 5 .   ? 28.813 10.399  78.766 1.00 46.03  ?  791 HOH A O   1 
HETATM 3289 O O   . HOH H 5 .   ? 16.954 59.427  52.796 1.00 52.53  ?  792 HOH A O   1 
HETATM 3290 O O   . HOH H 5 .   ? 24.642 62.757  65.502 1.00 50.23  ?  793 HOH A O   1 
HETATM 3291 O O   . HOH H 5 .   ? 33.091 2.626   55.040 1.00 48.90  ?  794 HOH A O   1 
HETATM 3292 O O   . HOH H 5 .   ? 25.773 1.796   89.617 1.00 43.78  ?  795 HOH A O   1 
HETATM 3293 O O   . HOH H 5 .   ? 44.149 55.787  49.478 1.00 51.62  ?  796 HOH A O   1 
HETATM 3294 O O   . HOH H 5 .   ? 48.735 57.028  64.604 1.00 132.97 ?  797 HOH A O   1 
HETATM 3295 O O   . HOH H 5 .   ? 22.843 69.863  55.343 1.00 48.53  ?  798 HOH A O   1 
HETATM 3296 O O   . HOH H 5 .   ? 40.044 3.068   71.488 1.00 46.31  ?  799 HOH A O   1 
HETATM 3297 O O   . HOH H 5 .   ? 30.977 49.886  33.129 1.00 60.67  ?  800 HOH A O   1 
HETATM 3298 O O   . HOH H 5 .   ? 51.733 41.782  66.133 1.00 46.62  ?  801 HOH A O   1 
HETATM 3299 O O   . HOH H 5 .   ? 29.610 68.624  42.547 1.00 40.54  ?  802 HOH A O   1 
HETATM 3300 O O   . HOH H 5 .   ? 30.573 55.070  58.336 1.00 58.96  ?  803 HOH A O   1 
HETATM 3301 O O   . HOH H 5 .   ? 43.460 27.007  69.423 1.00 55.07  ?  804 HOH A O   1 
HETATM 3302 O O   . HOH H 5 .   ? 57.419 45.993  37.030 1.00 48.68  ?  805 HOH A O   1 
HETATM 3303 O O   . HOH H 5 .   ? 47.861 12.402  53.197 1.00 59.86  ?  806 HOH A O   1 
HETATM 3304 O O   . HOH H 5 .   ? 29.540 68.435  39.912 1.00 49.17  ?  807 HOH A O   1 
HETATM 3305 O O   . HOH H 5 .   ? 33.659 12.938  71.165 1.00 43.88  ?  808 HOH A O   1 
HETATM 3306 O O   . HOH H 5 .   ? 20.663 66.865  37.672 1.00 51.85  ?  809 HOH A O   1 
HETATM 3307 O O   . HOH H 5 .   ? 37.800 26.381  66.835 1.00 58.45  ?  810 HOH A O   1 
HETATM 3308 O O   . HOH H 5 .   ? 49.925 58.886  33.264 1.00 52.96  ?  811 HOH A O   1 
HETATM 3309 O O   . HOH H 5 .   ? 44.956 55.423  53.479 1.00 56.26  ?  812 HOH A O   1 
HETATM 3310 O O   . HOH H 5 .   ? 31.625 51.658  30.508 1.00 68.37  ?  813 HOH A O   1 
HETATM 3311 O O   . HOH H 5 .   ? 29.896 10.308  80.941 1.00 49.49  ?  814 HOH A O   1 
HETATM 3312 O O   . HOH H 5 .   ? 63.172 29.622  56.005 1.00 64.57  ?  815 HOH A O   1 
HETATM 3313 O O   . HOH H 5 .   ? 32.796 53.606  30.418 1.00 53.88  ?  816 HOH A O   1 
HETATM 3314 O O   . HOH H 5 .   ? 50.513 28.038  67.792 1.00 48.14  ?  817 HOH A O   1 
HETATM 3315 O O   . HOH H 5 .   ? 23.263 69.191  62.147 1.00 44.63  ?  818 HOH A O   1 
HETATM 3316 O O   . HOH H 5 .   ? 55.141 40.103  64.049 1.00 51.49  ?  819 HOH A O   1 
HETATM 3317 O O   . HOH H 5 .   ? 33.613 22.502  59.095 1.00 51.77  ?  820 HOH A O   1 
HETATM 3318 O O   . HOH H 5 .   ? 49.464 51.982  60.853 1.00 54.69  ?  821 HOH A O   1 
HETATM 3319 O O   . HOH H 5 .   ? 32.441 9.511   77.769 1.00 49.94  ?  822 HOH A O   1 
HETATM 3320 O O   . HOH H 5 .   ? 32.880 10.403  80.118 1.00 44.67  ?  823 HOH A O   1 
HETATM 3321 O O   . HOH H 5 .   ? 38.449 7.133   88.656 1.00 59.68  ?  824 HOH A O   1 
HETATM 3322 O O   . HOH H 5 .   ? 23.421 71.144  58.153 1.00 53.21  ?  825 HOH A O   1 
HETATM 3323 O O   . HOH H 5 .   ? 46.938 31.660  67.455 1.00 45.38  ?  826 HOH A O   1 
HETATM 3324 O O   . HOH H 5 .   ? 68.253 45.213  53.694 1.00 52.96  ?  827 HOH A O   1 
HETATM 3325 O O   . HOH H 5 .   ? 39.788 0.512   70.667 1.00 48.43  ?  828 HOH A O   1 
HETATM 3326 O O   . HOH H 5 .   ? 38.399 -0.541  67.152 1.00 50.67  ?  829 HOH A O   1 
HETATM 3327 O O   . HOH H 5 .   ? 40.568 9.758   77.155 1.00 50.66  ?  830 HOH A O   1 
HETATM 3328 O O   . HOH H 5 .   ? 37.724 2.007   88.385 1.00 55.05  ?  831 HOH A O   1 
HETATM 3329 O O   . HOH H 5 .   ? 17.894 61.867  42.144 1.00 47.96  ?  832 HOH A O   1 
HETATM 3330 O O   . HOH H 5 .   ? 36.075 25.425  64.279 1.00 59.73  ?  833 HOH A O   1 
HETATM 3331 O O   . HOH H 5 .   ? 32.474 74.508  51.246 1.00 49.22  ?  834 HOH A O   1 
HETATM 3332 O O   . HOH H 5 .   ? 57.082 23.426  64.584 1.00 51.89  ?  835 HOH A O   1 
HETATM 3333 O O   . HOH H 5 .   ? 29.922 16.539  56.934 1.00 55.00  ?  836 HOH A O   1 
HETATM 3334 O O   . HOH H 5 .   ? 21.206 71.340  54.389 1.00 54.07  ?  837 HOH A O   1 
HETATM 3335 O O   . HOH H 5 .   ? 54.968 22.962  65.903 1.00 52.36  ?  838 HOH A O   1 
# 
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   -42 ?   ?   ?   A . n 
A 1 2   HIS 2   -41 ?   ?   ?   A . n 
A 1 3   HIS 3   -40 ?   ?   ?   A . n 
A 1 4   HIS 4   -39 ?   ?   ?   A . n 
A 1 5   HIS 5   -38 ?   ?   ?   A . n 
A 1 6   HIS 6   -37 ?   ?   ?   A . n 
A 1 7   HIS 7   -36 ?   ?   ?   A . n 
A 1 8   SER 8   -35 ?   ?   ?   A . n 
A 1 9   SER 9   -34 ?   ?   ?   A . n 
A 1 10  GLY 10  -33 ?   ?   ?   A . n 
A 1 11  LEU 11  -32 ?   ?   ?   A . n 
A 1 12  VAL 12  -31 ?   ?   ?   A . n 
A 1 13  PRO 13  -30 ?   ?   ?   A . n 
A 1 14  ARG 14  -29 ?   ?   ?   A . n 
A 1 15  GLY 15  -28 ?   ?   ?   A . n 
A 1 16  SER 16  -27 ?   ?   ?   A . n 
A 1 17  GLY 17  -26 ?   ?   ?   A . n 
A 1 18  MET 18  -25 ?   ?   ?   A . n 
A 1 19  LYS 19  -24 ?   ?   ?   A . n 
A 1 20  GLU 20  -23 ?   ?   ?   A . n 
A 1 21  THR 21  -22 ?   ?   ?   A . n 
A 1 22  ALA 22  -21 ?   ?   ?   A . n 
A 1 23  ALA 23  -20 ?   ?   ?   A . n 
A 1 24  ALA 24  -19 ?   ?   ?   A . n 
A 1 25  LYS 25  -18 ?   ?   ?   A . n 
A 1 26  PHE 26  -17 ?   ?   ?   A . n 
A 1 27  GLU 27  -16 ?   ?   ?   A . n 
A 1 28  ARG 28  -15 ?   ?   ?   A . n 
A 1 29  GLN 29  -14 ?   ?   ?   A . n 
A 1 30  HIS 30  -13 ?   ?   ?   A . n 
A 1 31  MET 31  -12 ?   ?   ?   A . n 
A 1 32  ASP 32  -11 ?   ?   ?   A . n 
A 1 33  SER 33  -10 ?   ?   ?   A . n 
A 1 34  PRO 34  -9  ?   ?   ?   A . n 
A 1 35  ASP 35  -8  ?   ?   ?   A . n 
A 1 36  LEU 36  -7  ?   ?   ?   A . n 
A 1 37  GLY 37  -6  ?   ?   ?   A . n 
A 1 38  THR 38  -5  ?   ?   ?   A . n 
A 1 39  ASP 39  -4  ?   ?   ?   A . n 
A 1 40  ASP 40  -3  -3  ASP ASP A . n 
A 1 41  ASP 41  -2  -2  ASP ASP A . n 
A 1 42  ASP 42  -1  -1  ASP ASP A . n 
A 1 43  LYS 43  0   0   LYS LYS A . n 
A 1 44  MET 44  1   1   MET MET A . n 
A 1 45  ASN 45  2   2   ASN ASN A . n 
A 1 46  THR 46  3   3   THR THR A . n 
A 1 47  ALA 47  4   4   ALA ALA A . n 
A 1 48  ILE 48  5   5   ILE ILE A . n 
A 1 49  LYS 49  6   6   LYS LYS A . n 
A 1 50  VAL 50  7   7   VAL VAL A . n 
A 1 51  ILE 51  8   8   ILE ILE A . n 
A 1 52  HIS 52  9   9   HIS HIS A . n 
A 1 53  THR 53  10  10  THR THR A . n 
A 1 54  LEU 54  11  11  LEU LEU A . n 
A 1 55  LYS 55  12  12  LYS LYS A . n 
A 1 56  ALA 56  13  13  ALA ALA A . n 
A 1 57  ALA 57  14  14  ALA ALA A . n 
A 1 58  GLY 58  15  15  GLY GLY A . n 
A 1 59  PHE 59  16  16  PHE PHE A . n 
A 1 60  GLU 60  17  17  GLU GLU A . n 
A 1 61  ALA 61  18  18  ALA ALA A . n 
A 1 62  TYR 62  19  19  TYR TYR A . n 
A 1 63  ILE 63  20  20  ILE ILE A . n 
A 1 64  VAL 64  21  21  VAL VAL A . n 
A 1 65  GLY 65  22  22  GLY GLY A . n 
A 1 66  GLY 66  23  23  GLY GLY A . n 
A 1 67  ALA 67  24  24  ALA ALA A . n 
A 1 68  VAL 68  25  25  VAL VAL A . n 
A 1 69  ARG 69  26  26  ARG ARG A . n 
A 1 70  ASP 70  27  27  ASP ASP A . n 
A 1 71  LEU 71  28  28  LEU LEU A . n 
A 1 72  LEU 72  29  29  LEU LEU A . n 
A 1 73  LEU 73  30  30  LEU LEU A . n 
A 1 74  GLY 74  31  31  GLY GLY A . n 
A 1 75  LYS 75  32  32  LYS LYS A . n 
A 1 76  THR 76  33  33  THR THR A . n 
A 1 77  PRO 77  34  34  PRO PRO A . n 
A 1 78  HIS 78  35  35  HIS HIS A . n 
A 1 79  ASP 79  36  36  ASP ASP A . n 
A 1 80  VAL 80  37  37  VAL VAL A . n 
A 1 81  ASP 81  38  38  ASP ASP A . n 
A 1 82  VAL 82  39  39  VAL VAL A . n 
A 1 83  ALA 83  40  40  ALA ALA A . n 
A 1 84  SER 84  41  41  SER SER A . n 
A 1 85  SER 85  42  42  SER SER A . n 
A 1 86  ALA 86  43  43  ALA ALA A . n 
A 1 87  LEU 87  44  44  LEU LEU A . n 
A 1 88  PRO 88  45  45  PRO PRO A . n 
A 1 89  GLN 89  46  46  GLN GLN A . n 
A 1 90  GLN 90  47  47  GLN GLN A . n 
A 1 91  VAL 91  48  48  VAL VAL A . n 
A 1 92  LYS 92  49  49  LYS LYS A . n 
A 1 93  VAL 93  50  50  VAL VAL A . n 
A 1 94  LEU 94  51  51  LEU LEU A . n 
A 1 95  PHE 95  52  52  PHE PHE A . n 
A 1 96  ASP 96  53  53  ASP ASP A . n 
A 1 97  ARG 97  54  54  ARG ARG A . n 
A 1 98  THR 98  55  55  THR THR A . n 
A 1 99  VAL 99  56  56  VAL VAL A . n 
A 1 100 ASP 100 57  57  ASP ASP A . n 
A 1 101 THR 101 58  58  THR THR A . n 
A 1 102 GLY 102 59  59  GLY GLY A . n 
A 1 103 ILE 103 60  60  ILE ILE A . n 
A 1 104 ASP 104 61  61  ASP ASP A . n 
A 1 105 HIS 105 62  62  HIS HIS A . n 
A 1 106 GLY 106 63  63  GLY GLY A . n 
A 1 107 THR 107 64  64  THR THR A . n 
A 1 108 VAL 108 65  65  VAL VAL A . n 
A 1 109 LEU 109 66  66  LEU LEU A . n 
A 1 110 VAL 110 67  67  VAL VAL A . n 
A 1 111 LEU 111 68  68  LEU LEU A . n 
A 1 112 LEU 112 69  69  LEU LEU A . n 
A 1 113 ASP 113 70  70  ASP ASP A . n 
A 1 114 GLY 114 71  71  GLY GLY A . n 
A 1 115 GLU 115 72  72  GLU GLU A . n 
A 1 116 GLY 116 73  73  GLY GLY A . n 
A 1 117 ILE 117 74  74  ILE ILE A . n 
A 1 118 GLU 118 75  75  GLU GLU A . n 
A 1 119 VAL 119 76  76  VAL VAL A . n 
A 1 120 THR 120 77  77  THR THR A . n 
A 1 121 THR 121 78  78  THR THR A . n 
A 1 122 PHE 122 79  79  PHE PHE A . n 
A 1 123 ARG 123 80  80  ARG ARG A . n 
A 1 124 THR 124 81  81  THR THR A . n 
A 1 125 GLU 125 82  82  GLU GLU A . n 
A 1 126 SER 126 83  83  SER SER A . n 
A 1 127 SER 127 84  84  SER SER A . n 
A 1 128 TYR 128 85  85  TYR TYR A . n 
A 1 129 SER 129 86  86  SER SER A . n 
A 1 130 ASP 130 87  87  ASP ASP A . n 
A 1 131 ASN 131 88  88  ASN ASN A . n 
A 1 132 ARG 132 89  ?   ?   ?   A . n 
A 1 133 ARG 133 90  ?   ?   ?   A . n 
A 1 134 PRO 134 91  ?   ?   ?   A . n 
A 1 135 ASP 135 92  ?   ?   ?   A . n 
A 1 136 SER 136 93  93  SER SER A . n 
A 1 137 VAL 137 94  94  VAL VAL A . n 
A 1 138 GLU 138 95  95  GLU GLU A . n 
A 1 139 PHE 139 96  96  PHE PHE A . n 
A 1 140 VAL 140 97  97  VAL VAL A . n 
A 1 141 LEU 141 98  98  LEU LEU A . n 
A 1 142 SER 142 99  99  SER SER A . n 
A 1 143 LEU 143 100 100 LEU LEU A . n 
A 1 144 GLU 144 101 101 GLU GLU A . n 
A 1 145 GLU 145 102 102 GLU GLU A . n 
A 1 146 ASP 146 103 103 ASP ASP A . n 
A 1 147 LEU 147 104 104 LEU LEU A . n 
A 1 148 ARG 148 105 105 ARG ARG A . n 
A 1 149 ARG 149 106 106 ARG ARG A . n 
A 1 150 ARG 150 107 107 ARG ARG A . n 
A 1 151 ASP 151 108 108 ASP ASP A . n 
A 1 152 PHE 152 109 109 PHE PHE A . n 
A 1 153 THR 153 110 110 THR THR A . n 
A 1 154 ILE 154 111 111 ILE ILE A . n 
A 1 155 ASN 155 112 112 ASN ASN A . n 
A 1 156 ALA 156 113 113 ALA ALA A . n 
A 1 157 MET 157 114 114 MET MET A . n 
A 1 158 ALA 158 115 115 ALA ALA A . n 
A 1 159 MET 159 116 116 MET MET A . n 
A 1 160 THR 160 117 117 THR THR A . n 
A 1 161 GLU 161 118 118 GLU GLU A . n 
A 1 162 ASP 162 119 119 ASP ASP A . n 
A 1 163 LEU 163 120 120 LEU LEU A . n 
A 1 164 LYS 164 121 121 LYS LYS A . n 
A 1 165 ILE 165 122 122 ILE ILE A . n 
A 1 166 ILE 166 123 123 ILE ILE A . n 
A 1 167 ASP 167 124 124 ASP ASP A . n 
A 1 168 PRO 168 125 125 PRO PRO A . n 
A 1 169 PHE 169 126 126 PHE PHE A . n 
A 1 170 GLY 170 127 127 GLY GLY A . n 
A 1 171 GLY 171 128 128 GLY GLY A . n 
A 1 172 LYS 172 129 129 LYS LYS A . n 
A 1 173 GLU 173 130 130 GLU GLU A . n 
A 1 174 ASP 174 131 131 ASP ASP A . n 
A 1 175 LEU 175 132 132 LEU LEU A . n 
A 1 176 LYS 176 133 133 LYS LYS A . n 
A 1 177 ASN 177 134 134 ASN ASN A . n 
A 1 178 LYS 178 135 135 LYS LYS A . n 
A 1 179 VAL 179 136 136 VAL VAL A . n 
A 1 180 ILE 180 137 137 ILE ILE A . n 
A 1 181 ARG 181 138 138 ARG ARG A . n 
A 1 182 ALA 182 139 139 ALA ALA A . n 
A 1 183 VAL 183 140 140 VAL VAL A . n 
A 1 184 GLY 184 141 141 GLY GLY A . n 
A 1 185 ASP 185 142 142 ASP ASP A . n 
A 1 186 PRO 186 143 143 PRO PRO A . n 
A 1 187 ASP 187 144 144 ASP ASP A . n 
A 1 188 GLU 188 145 145 GLU GLU A . n 
A 1 189 ARG 189 146 146 ARG ARG A . n 
A 1 190 PHE 190 147 147 PHE PHE A . n 
A 1 191 GLU 191 148 148 GLU GLU A . n 
A 1 192 GLU 192 149 149 GLU GLU A . n 
A 1 193 ASP 193 150 150 ASP ASP A . n 
A 1 194 ALA 194 151 151 ALA ALA A . n 
A 1 195 LEU 195 152 152 LEU LEU A . n 
A 1 196 ARG 196 153 153 ARG ARG A . n 
A 1 197 MET 197 154 154 MET MET A . n 
A 1 198 LEU 198 155 155 LEU LEU A . n 
A 1 199 ARG 199 156 156 ARG ARG A . n 
A 1 200 ALA 200 157 157 ALA ALA A . n 
A 1 201 ILE 201 158 158 ILE ILE A . n 
A 1 202 ARG 202 159 159 ARG ARG A . n 
A 1 203 PHE 203 160 160 PHE PHE A . n 
A 1 204 SER 204 161 161 SER SER A . n 
A 1 205 GLY 205 162 162 GLY GLY A . n 
A 1 206 GLN 206 163 163 GLN GLN A . n 
A 1 207 LEU 207 164 164 LEU LEU A . n 
A 1 208 ASP 208 165 165 ASP ASP A . n 
A 1 209 PHE 209 166 166 PHE PHE A . n 
A 1 210 ILE 210 167 167 ILE ILE A . n 
A 1 211 ILE 211 168 168 ILE ILE A . n 
A 1 212 ASP 212 169 169 ASP ASP A . n 
A 1 213 MET 213 170 170 MET MET A . n 
A 1 214 LYS 214 171 171 LYS LYS A . n 
A 1 215 THR 215 172 172 THR THR A . n 
A 1 216 LEU 216 173 173 LEU LEU A . n 
A 1 217 LEU 217 174 174 LEU LEU A . n 
A 1 218 SER 218 175 175 SER SER A . n 
A 1 219 ILE 219 176 176 ILE ILE A . n 
A 1 220 ARG 220 177 177 ARG ARG A . n 
A 1 221 ARG 221 178 178 ARG ARG A . n 
A 1 222 HIS 222 179 179 HIS HIS A . n 
A 1 223 ALA 223 180 180 ALA ALA A . n 
A 1 224 ARG 224 181 181 ARG ARG A . n 
A 1 225 LEU 225 182 182 LEU LEU A . n 
A 1 226 ILE 226 183 183 ILE ILE A . n 
A 1 227 ARG 227 184 184 ARG ARG A . n 
A 1 228 PHE 228 185 185 PHE PHE A . n 
A 1 229 ILE 229 186 186 ILE ILE A . n 
A 1 230 ALA 230 187 187 ALA ALA A . n 
A 1 231 VAL 231 188 188 VAL VAL A . n 
A 1 232 GLU 232 189 189 GLU GLU A . n 
A 1 233 ARG 233 190 190 ARG ARG A . n 
A 1 234 LEU 234 191 191 LEU LEU A . n 
A 1 235 LYS 235 192 192 LYS LYS A . n 
A 1 236 SER 236 193 193 SER SER A . n 
A 1 237 GLU 237 194 194 GLU GLU A . n 
A 1 238 ILE 238 195 195 ILE ILE A . n 
A 1 239 ASP 239 196 196 ASP ASP A . n 
A 1 240 LYS 240 197 197 LYS LYS A . n 
A 1 241 ILE 241 198 198 ILE ILE A . n 
A 1 242 PHE 242 199 199 PHE PHE A . n 
A 1 243 VAL 243 200 200 VAL VAL A . n 
A 1 244 ASN 244 201 201 ASN ASN A . n 
A 1 245 PRO 245 202 202 PRO PRO A . n 
A 1 246 SER 246 203 203 SER SER A . n 
A 1 247 MET 247 204 204 MET MET A . n 
A 1 248 GLN 248 205 205 GLN GLN A . n 
A 1 249 LYS 249 206 206 LYS LYS A . n 
A 1 250 SER 250 207 207 SER SER A . n 
A 1 251 MET 251 208 208 MET MET A . n 
A 1 252 ALA 252 209 209 ALA ALA A . n 
A 1 253 TYR 253 210 210 TYR TYR A . n 
A 1 254 LEU 254 211 211 LEU LEU A . n 
A 1 255 LYS 255 212 212 LYS LYS A . n 
A 1 256 ASP 256 213 213 ASP ASP A . n 
A 1 257 SER 257 214 214 SER SER A . n 
A 1 258 VAL 258 215 215 VAL VAL A . n 
A 1 259 LEU 259 216 216 LEU LEU A . n 
A 1 260 THR 260 217 217 THR THR A . n 
A 1 261 ARG 261 218 218 ARG ARG A . n 
A 1 262 PHE 262 219 219 PHE PHE A . n 
A 1 263 LEU 263 220 220 LEU LEU A . n 
A 1 264 PRO 264 221 221 PRO PRO A . n 
A 1 265 VAL 265 222 222 VAL VAL A . n 
A 1 266 GLY 266 223 223 GLY GLY A . n 
A 1 267 GLY 267 224 224 GLY GLY A . n 
A 1 268 LEU 268 225 225 LEU LEU A . n 
A 1 269 PHE 269 226 226 PHE PHE A . n 
A 1 270 GLU 270 227 227 GLU GLU A . n 
A 1 271 VAL 271 228 228 VAL VAL A . n 
A 1 272 ASP 272 229 229 ASP ASP A . n 
A 1 273 TRP 273 230 230 TRP TRP A . n 
A 1 274 ILE 274 231 231 ILE ILE A . n 
A 1 275 THR 275 232 232 THR THR A . n 
A 1 276 TYR 276 233 233 TYR TYR A . n 
A 1 277 HIS 277 234 234 HIS HIS A . n 
A 1 278 THR 278 235 235 THR THR A . n 
A 1 279 ASP 279 236 236 ASP ASP A . n 
A 1 280 GLY 280 237 237 GLY GLY A . n 
A 1 281 ASN 281 238 238 ASN ASN A . n 
A 1 282 PRO 282 239 239 PRO PRO A . n 
A 1 283 THR 283 240 240 THR THR A . n 
A 1 284 TYR 284 241 241 TYR TYR A . n 
A 1 285 GLY 285 242 242 GLY GLY A . n 
A 1 286 TRP 286 243 243 TRP TRP A . n 
A 1 287 LEU 287 244 244 LEU LEU A . n 
A 1 288 TYR 288 245 245 TYR TYR A . n 
A 1 289 LEU 289 246 246 LEU LEU A . n 
A 1 290 LEU 290 247 247 LEU LEU A . n 
A 1 291 HIS 291 248 248 HIS HIS A . n 
A 1 292 GLN 292 249 249 GLN GLN A . n 
A 1 293 GLN 293 250 250 GLN GLN A . n 
A 1 294 LYS 294 251 251 LYS LYS A . n 
A 1 295 ARG 295 252 252 ARG ARG A . n 
A 1 296 GLN 296 253 253 GLN GLN A . n 
A 1 297 PHE 297 254 254 PHE PHE A . n 
A 1 298 THR 298 255 255 THR THR A . n 
A 1 299 ASP 299 256 256 ASP ASP A . n 
A 1 300 ILE 300 257 257 ILE ILE A . n 
A 1 301 LYS 301 258 258 LYS LYS A . n 
A 1 302 ASP 302 259 259 ASP ASP A . n 
A 1 303 TYR 303 260 260 TYR TYR A . n 
A 1 304 ARG 304 261 261 ARG ARG A . n 
A 1 305 PHE 305 262 262 PHE PHE A . n 
A 1 306 SER 306 263 263 SER SER A . n 
A 1 307 ASN 307 264 264 ASN ASN A . n 
A 1 308 GLU 308 265 265 GLU GLU A . n 
A 1 309 GLU 309 266 266 GLU GLU A . n 
A 1 310 LYS 310 267 267 LYS LYS A . n 
A 1 311 ARG 311 268 268 ARG ARG A . n 
A 1 312 LEU 312 269 269 LEU LEU A . n 
A 1 313 ILE 313 270 270 ILE ILE A . n 
A 1 314 GLU 314 271 271 GLU GLU A . n 
A 1 315 LYS 315 272 272 LYS LYS A . n 
A 1 316 SER 316 273 273 SER SER A . n 
A 1 317 LEU 317 274 274 LEU LEU A . n 
A 1 318 GLU 318 275 275 GLU GLU A . n 
A 1 319 LEU 319 276 276 LEU LEU A . n 
A 1 320 THR 320 277 277 THR THR A . n 
A 1 321 ALA 321 278 278 ALA ALA A . n 
A 1 322 LEU 322 279 279 LEU LEU A . n 
A 1 323 ASN 323 280 280 ASN ASN A . n 
A 1 324 THR 324 281 281 THR THR A . n 
A 1 325 TRP 325 282 282 TRP TRP A . n 
A 1 326 ASP 326 283 283 ASP ASP A . n 
A 1 327 GLN 327 284 284 GLN GLN A . n 
A 1 328 TRP 328 285 285 TRP TRP A . n 
A 1 329 THR 329 286 286 THR THR A . n 
A 1 330 PHE 330 287 287 PHE PHE A . n 
A 1 331 TYR 331 288 288 TYR TYR A . n 
A 1 332 LYS 332 289 289 LYS LYS A . n 
A 1 333 TYR 333 290 290 TYR TYR A . n 
A 1 334 THR 334 291 291 THR THR A . n 
A 1 335 LEU 335 292 292 LEU LEU A . n 
A 1 336 LYS 336 293 293 LYS LYS A . n 
A 1 337 GLN 337 294 294 GLN GLN A . n 
A 1 338 LEU 338 295 295 LEU LEU A . n 
A 1 339 GLU 339 296 296 GLU GLU A . n 
A 1 340 MET 340 297 297 MET MET A . n 
A 1 341 ALA 341 298 298 ALA ALA A . n 
A 1 342 SER 342 299 299 SER SER A . n 
A 1 343 ARG 343 300 300 ARG ARG A . n 
A 1 344 VAL 344 301 301 VAL VAL A . n 
A 1 345 THR 345 302 302 THR THR A . n 
A 1 346 GLY 346 303 303 GLY GLY A . n 
A 1 347 LYS 347 304 304 LYS LYS A . n 
A 1 348 LYS 348 305 305 LYS LYS A . n 
A 1 349 LYS 349 306 306 LYS LYS A . n 
A 1 350 ASP 350 307 307 ASP ASP A . n 
A 1 351 LEU 351 308 308 LEU LEU A . n 
A 1 352 ALA 352 309 309 ALA ALA A . n 
A 1 353 ALA 353 310 310 ALA ALA A . n 
A 1 354 ILE 354 311 311 ILE ILE A . n 
A 1 355 LYS 355 312 312 LYS LYS A . n 
A 1 356 ARG 356 313 313 ARG ARG A . n 
A 1 357 GLN 357 314 314 GLN GLN A . n 
A 1 358 LEU 358 315 315 LEU LEU A . n 
A 1 359 PRO 359 316 316 PRO PRO A . n 
A 1 360 ILE 360 317 317 ILE ILE A . n 
A 1 361 GLN 361 318 318 GLN GLN A . n 
A 1 362 SER 362 319 319 SER SER A . n 
A 1 363 ARG 363 320 320 ARG ARG A . n 
A 1 364 SER 364 321 321 SER SER A . n 
A 1 365 GLU 365 322 322 GLU GLU A . n 
A 1 366 LEU 366 323 323 LEU LEU A . n 
A 1 367 ALA 367 324 324 ALA ALA A . n 
A 1 368 VAL 368 325 325 VAL VAL A . n 
A 1 369 ASP 369 326 326 ASP ASP A . n 
A 1 370 GLY 370 327 327 GLY GLY A . n 
A 1 371 TRP 371 328 328 TRP TRP A . n 
A 1 372 ASP 372 329 329 ASP ASP A . n 
A 1 373 LEU 373 330 330 LEU LEU A . n 
A 1 374 ILE 374 331 331 ILE ILE A . n 
A 1 375 GLU 375 332 332 GLU GLU A . n 
A 1 376 TRP 376 333 333 TRP TRP A . n 
A 1 377 SER 377 334 334 SER SER A . n 
A 1 378 GLY 378 335 335 GLY GLY A . n 
A 1 379 ALA 379 336 336 ALA ALA A . n 
A 1 380 LYS 380 337 337 LYS LYS A . n 
A 1 381 SER 381 338 338 SER SER A . n 
A 1 382 GLY 382 339 339 GLY GLY A . n 
A 1 383 PRO 383 340 340 PRO PRO A . n 
A 1 384 TRP 384 341 341 TRP TRP A . n 
A 1 385 LEU 385 342 342 LEU LEU A . n 
A 1 386 LYS 386 343 343 LYS LYS A . n 
A 1 387 VAL 387 344 344 VAL VAL A . n 
A 1 388 TRP 388 345 345 TRP TRP A . n 
A 1 389 ILE 389 346 346 ILE ILE A . n 
A 1 390 GLU 390 347 347 GLU GLU A . n 
A 1 391 LYS 391 348 348 LYS LYS A . n 
A 1 392 ILE 392 349 349 ILE ILE A . n 
A 1 393 GLU 393 350 350 GLU GLU A . n 
A 1 394 ARG 394 351 351 ARG ARG A . n 
A 1 395 LEU 395 352 352 LEU LEU A . n 
A 1 396 ILE 396 353 353 ILE ILE A . n 
A 1 397 VAL 397 354 354 VAL VAL A . n 
A 1 398 TYR 398 355 355 TYR TYR A . n 
A 1 399 GLY 399 356 356 GLY GLY A . n 
A 1 400 ILE 400 357 357 ILE ILE A . n 
A 1 401 LEU 401 358 358 LEU LEU A . n 
A 1 402 LYS 402 359 359 LYS LYS A . n 
A 1 403 ASN 403 360 360 ASN ASN A . n 
A 1 404 ASP 404 361 361 ASP ASP A . n 
A 1 405 LYS 405 362 362 LYS LYS A . n 
A 1 406 GLU 406 363 363 GLU GLU A . n 
A 1 407 LEU 407 364 364 LEU LEU A . n 
A 1 408 ILE 408 365 365 ILE ILE A . n 
A 1 409 LYS 409 366 366 LYS LYS A . n 
A 1 410 ASP 410 367 367 ASP ASP A . n 
A 1 411 TRP 411 368 368 TRP TRP A . n 
A 1 412 PHE 412 369 369 PHE PHE A . n 
A 1 413 GLU 413 370 370 GLU GLU A . n 
A 1 414 ASP 414 371 371 ASP ASP A . n 
A 1 415 GLU 415 372 372 GLU GLU A . n 
A 1 416 TYR 416 373 373 TYR TYR A . n 
A 1 417 HIS 417 374 ?   ?   ?   A . n 
A 1 418 SER 418 375 ?   ?   ?   A . n 
A 1 419 HIS 419 376 ?   ?   ?   A . n 
A 1 420 THR 420 377 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 PO4 1   501 501 PO4 PO4 A . 
C 3 GOL 1   502 601 GOL GOL A . 
D 3 GOL 1   503 801 GOL GOL A . 
E 4 ACT 1   504 901 ACT ACT A . 
F 4 ACT 1   505 921 ACT ACT A . 
G 4 ACT 1   506 931 ACT ACT A . 
H 5 HOH 1   601 383 HOH HOH A . 
H 5 HOH 2   602 233 HOH HOH A . 
H 5 HOH 3   603 157 HOH HOH A . 
H 5 HOH 4   604 172 HOH HOH A . 
H 5 HOH 5   605 33  HOH HOH A . 
H 5 HOH 6   606 100 HOH HOH A . 
H 5 HOH 7   607 94  HOH HOH A . 
H 5 HOH 8   608 303 HOH HOH A . 
H 5 HOH 9   609 340 HOH HOH A . 
H 5 HOH 10  610 59  HOH HOH A . 
H 5 HOH 11  611 15  HOH HOH A . 
H 5 HOH 12  612 98  HOH HOH A . 
H 5 HOH 13  613 143 HOH HOH A . 
H 5 HOH 14  614 232 HOH HOH A . 
H 5 HOH 15  615 226 HOH HOH A . 
H 5 HOH 16  616 80  HOH HOH A . 
H 5 HOH 17  617 112 HOH HOH A . 
H 5 HOH 18  618 73  HOH HOH A . 
H 5 HOH 19  619 168 HOH HOH A . 
H 5 HOH 20  620 111 HOH HOH A . 
H 5 HOH 21  621 315 HOH HOH A . 
H 5 HOH 22  622 85  HOH HOH A . 
H 5 HOH 23  623 63  HOH HOH A . 
H 5 HOH 24  624 127 HOH HOH A . 
H 5 HOH 25  625 68  HOH HOH A . 
H 5 HOH 26  626 257 HOH HOH A . 
H 5 HOH 27  627 2   HOH HOH A . 
H 5 HOH 28  628 220 HOH HOH A . 
H 5 HOH 29  629 39  HOH HOH A . 
H 5 HOH 30  630 41  HOH HOH A . 
H 5 HOH 31  631 9   HOH HOH A . 
H 5 HOH 32  632 371 HOH HOH A . 
H 5 HOH 33  633 275 HOH HOH A . 
H 5 HOH 34  634 42  HOH HOH A . 
H 5 HOH 35  635 19  HOH HOH A . 
H 5 HOH 36  636 306 HOH HOH A . 
H 5 HOH 37  637 171 HOH HOH A . 
H 5 HOH 38  638 61  HOH HOH A . 
H 5 HOH 39  639 123 HOH HOH A . 
H 5 HOH 40  640 154 HOH HOH A . 
H 5 HOH 41  641 190 HOH HOH A . 
H 5 HOH 42  642 65  HOH HOH A . 
H 5 HOH 43  643 278 HOH HOH A . 
H 5 HOH 44  644 131 HOH HOH A . 
H 5 HOH 45  645 175 HOH HOH A . 
H 5 HOH 46  646 8   HOH HOH A . 
H 5 HOH 47  647 44  HOH HOH A . 
H 5 HOH 48  648 3   HOH HOH A . 
H 5 HOH 49  649 353 HOH HOH A . 
H 5 HOH 50  650 72  HOH HOH A . 
H 5 HOH 51  651 158 HOH HOH A . 
H 5 HOH 52  652 185 HOH HOH A . 
H 5 HOH 53  653 381 HOH HOH A . 
H 5 HOH 54  654 5   HOH HOH A . 
H 5 HOH 55  655 4   HOH HOH A . 
H 5 HOH 56  656 58  HOH HOH A . 
H 5 HOH 57  657 179 HOH HOH A . 
H 5 HOH 58  658 76  HOH HOH A . 
H 5 HOH 59  659 141 HOH HOH A . 
H 5 HOH 60  660 248 HOH HOH A . 
H 5 HOH 61  661 120 HOH HOH A . 
H 5 HOH 62  662 106 HOH HOH A . 
H 5 HOH 63  663 10  HOH HOH A . 
H 5 HOH 64  664 302 HOH HOH A . 
H 5 HOH 65  665 6   HOH HOH A . 
H 5 HOH 66  666 337 HOH HOH A . 
H 5 HOH 67  667 16  HOH HOH A . 
H 5 HOH 68  668 262 HOH HOH A . 
H 5 HOH 69  669 160 HOH HOH A . 
H 5 HOH 70  670 307 HOH HOH A . 
H 5 HOH 71  671 364 HOH HOH A . 
H 5 HOH 72  672 151 HOH HOH A . 
H 5 HOH 73  673 318 HOH HOH A . 
H 5 HOH 74  674 105 HOH HOH A . 
H 5 HOH 75  675 89  HOH HOH A . 
H 5 HOH 76  676 22  HOH HOH A . 
H 5 HOH 77  677 20  HOH HOH A . 
H 5 HOH 78  678 109 HOH HOH A . 
H 5 HOH 79  679 18  HOH HOH A . 
H 5 HOH 80  680 27  HOH HOH A . 
H 5 HOH 81  681 91  HOH HOH A . 
H 5 HOH 82  682 11  HOH HOH A . 
H 5 HOH 83  683 88  HOH HOH A . 
H 5 HOH 84  684 133 HOH HOH A . 
H 5 HOH 85  685 375 HOH HOH A . 
H 5 HOH 86  686 40  HOH HOH A . 
H 5 HOH 87  687 38  HOH HOH A . 
H 5 HOH 88  688 50  HOH HOH A . 
H 5 HOH 89  689 17  HOH HOH A . 
H 5 HOH 90  690 356 HOH HOH A . 
H 5 HOH 91  691 69  HOH HOH A . 
H 5 HOH 92  692 24  HOH HOH A . 
H 5 HOH 93  693 53  HOH HOH A . 
H 5 HOH 94  694 28  HOH HOH A . 
H 5 HOH 95  695 46  HOH HOH A . 
H 5 HOH 96  696 87  HOH HOH A . 
H 5 HOH 97  697 148 HOH HOH A . 
H 5 HOH 98  698 130 HOH HOH A . 
H 5 HOH 99  699 107 HOH HOH A . 
H 5 HOH 100 700 182 HOH HOH A . 
H 5 HOH 101 701 52  HOH HOH A . 
H 5 HOH 102 702 162 HOH HOH A . 
H 5 HOH 103 703 84  HOH HOH A . 
H 5 HOH 104 704 57  HOH HOH A . 
H 5 HOH 105 705 1   HOH HOH A . 
H 5 HOH 106 706 67  HOH HOH A . 
H 5 HOH 107 707 128 HOH HOH A . 
H 5 HOH 108 708 204 HOH HOH A . 
H 5 HOH 109 709 43  HOH HOH A . 
H 5 HOH 110 710 14  HOH HOH A . 
H 5 HOH 111 711 269 HOH HOH A . 
H 5 HOH 112 712 29  HOH HOH A . 
H 5 HOH 113 713 12  HOH HOH A . 
H 5 HOH 114 714 201 HOH HOH A . 
H 5 HOH 115 715 32  HOH HOH A . 
H 5 HOH 116 716 203 HOH HOH A . 
H 5 HOH 117 717 102 HOH HOH A . 
H 5 HOH 118 718 13  HOH HOH A . 
H 5 HOH 119 719 342 HOH HOH A . 
H 5 HOH 120 720 110 HOH HOH A . 
H 5 HOH 121 721 71  HOH HOH A . 
H 5 HOH 122 722 60  HOH HOH A . 
H 5 HOH 123 723 26  HOH HOH A . 
H 5 HOH 124 724 145 HOH HOH A . 
H 5 HOH 125 725 7   HOH HOH A . 
H 5 HOH 126 726 139 HOH HOH A . 
H 5 HOH 127 727 92  HOH HOH A . 
H 5 HOH 128 728 99  HOH HOH A . 
H 5 HOH 129 729 156 HOH HOH A . 
H 5 HOH 130 730 155 HOH HOH A . 
H 5 HOH 131 731 83  HOH HOH A . 
H 5 HOH 132 732 49  HOH HOH A . 
H 5 HOH 133 733 167 HOH HOH A . 
H 5 HOH 134 734 159 HOH HOH A . 
H 5 HOH 135 735 77  HOH HOH A . 
H 5 HOH 136 736 372 HOH HOH A . 
H 5 HOH 137 737 195 HOH HOH A . 
H 5 HOH 138 738 37  HOH HOH A . 
H 5 HOH 139 739 81  HOH HOH A . 
H 5 HOH 140 740 173 HOH HOH A . 
H 5 HOH 141 741 255 HOH HOH A . 
H 5 HOH 142 742 54  HOH HOH A . 
H 5 HOH 143 743 48  HOH HOH A . 
H 5 HOH 144 744 169 HOH HOH A . 
H 5 HOH 145 745 200 HOH HOH A . 
H 5 HOH 146 746 35  HOH HOH A . 
H 5 HOH 147 747 47  HOH HOH A . 
H 5 HOH 148 748 70  HOH HOH A . 
H 5 HOH 149 749 97  HOH HOH A . 
H 5 HOH 150 750 78  HOH HOH A . 
H 5 HOH 151 751 121 HOH HOH A . 
H 5 HOH 152 752 217 HOH HOH A . 
H 5 HOH 153 753 183 HOH HOH A . 
H 5 HOH 154 754 228 HOH HOH A . 
H 5 HOH 155 755 82  HOH HOH A . 
H 5 HOH 156 756 343 HOH HOH A . 
H 5 HOH 157 757 104 HOH HOH A . 
H 5 HOH 158 758 304 HOH HOH A . 
H 5 HOH 159 759 90  HOH HOH A . 
H 5 HOH 160 760 66  HOH HOH A . 
H 5 HOH 161 761 114 HOH HOH A . 
H 5 HOH 162 762 23  HOH HOH A . 
H 5 HOH 163 763 119 HOH HOH A . 
H 5 HOH 164 764 142 HOH HOH A . 
H 5 HOH 165 765 174 HOH HOH A . 
H 5 HOH 166 766 177 HOH HOH A . 
H 5 HOH 167 767 45  HOH HOH A . 
H 5 HOH 168 768 194 HOH HOH A . 
H 5 HOH 169 769 74  HOH HOH A . 
H 5 HOH 170 770 75  HOH HOH A . 
H 5 HOH 171 771 380 HOH HOH A . 
H 5 HOH 172 772 245 HOH HOH A . 
H 5 HOH 173 773 197 HOH HOH A . 
H 5 HOH 174 774 115 HOH HOH A . 
H 5 HOH 175 775 288 HOH HOH A . 
H 5 HOH 176 776 51  HOH HOH A . 
H 5 HOH 177 777 56  HOH HOH A . 
H 5 HOH 178 778 132 HOH HOH A . 
H 5 HOH 179 779 36  HOH HOH A . 
H 5 HOH 180 780 34  HOH HOH A . 
H 5 HOH 181 781 339 HOH HOH A . 
H 5 HOH 182 782 101 HOH HOH A . 
H 5 HOH 183 783 237 HOH HOH A . 
H 5 HOH 184 784 284 HOH HOH A . 
H 5 HOH 185 785 135 HOH HOH A . 
H 5 HOH 186 786 30  HOH HOH A . 
H 5 HOH 187 787 129 HOH HOH A . 
H 5 HOH 188 788 25  HOH HOH A . 
H 5 HOH 189 789 301 HOH HOH A . 
H 5 HOH 190 790 31  HOH HOH A . 
H 5 HOH 191 791 305 HOH HOH A . 
H 5 HOH 192 792 95  HOH HOH A . 
H 5 HOH 193 793 261 HOH HOH A . 
H 5 HOH 194 794 86  HOH HOH A . 
H 5 HOH 195 795 116 HOH HOH A . 
H 5 HOH 196 796 384 HOH HOH A . 
H 5 HOH 197 797 366 HOH HOH A . 
H 5 HOH 198 798 124 HOH HOH A . 
H 5 HOH 199 799 103 HOH HOH A . 
H 5 HOH 200 800 362 HOH HOH A . 
H 5 HOH 201 801 125 HOH HOH A . 
H 5 HOH 202 802 21  HOH HOH A . 
H 5 HOH 203 803 321 HOH HOH A . 
H 5 HOH 204 804 314 HOH HOH A . 
H 5 HOH 205 805 208 HOH HOH A . 
H 5 HOH 206 806 150 HOH HOH A . 
H 5 HOH 207 807 79  HOH HOH A . 
H 5 HOH 208 808 122 HOH HOH A . 
H 5 HOH 209 809 313 HOH HOH A . 
H 5 HOH 210 810 252 HOH HOH A . 
H 5 HOH 211 811 206 HOH HOH A . 
H 5 HOH 212 812 382 HOH HOH A . 
H 5 HOH 213 813 363 HOH HOH A . 
H 5 HOH 214 814 184 HOH HOH A . 
H 5 HOH 215 815 270 HOH HOH A . 
H 5 HOH 216 816 355 HOH HOH A . 
H 5 HOH 217 817 113 HOH HOH A . 
H 5 HOH 218 818 126 HOH HOH A . 
H 5 HOH 219 819 369 HOH HOH A . 
H 5 HOH 220 820 243 HOH HOH A . 
H 5 HOH 221 821 310 HOH HOH A . 
H 5 HOH 222 822 186 HOH HOH A . 
H 5 HOH 223 823 62  HOH HOH A . 
H 5 HOH 224 824 118 HOH HOH A . 
H 5 HOH 225 825 144 HOH HOH A . 
H 5 HOH 226 826 117 HOH HOH A . 
H 5 HOH 227 827 264 HOH HOH A . 
H 5 HOH 228 828 202 HOH HOH A . 
H 5 HOH 229 829 282 HOH HOH A . 
H 5 HOH 230 830 166 HOH HOH A . 
H 5 HOH 231 831 361 HOH HOH A . 
H 5 HOH 232 832 55  HOH HOH A . 
H 5 HOH 233 833 163 HOH HOH A . 
H 5 HOH 234 834 134 HOH HOH A . 
H 5 HOH 235 835 108 HOH HOH A . 
H 5 HOH 236 836 187 HOH HOH A . 
H 5 HOH 237 837 242 HOH HOH A . 
H 5 HOH 238 838 213 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
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)' 1260  ? 
1 MORE         -11   ? 
1 'SSA (A^2)'  18920 ? 
# 
_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_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2020-03-25 
2 'Structure model' 1 1 2020-12-16 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Structure summary' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            struct 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_struct.title' 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.13_2998: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? 20160617           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? 20160617           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.13_2998          4 
# 
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 VAL A 222 ? ? 33.38 44.22 
2 1 ARG A 261 ? ? 62.26 60.69 
# 
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 -42 ? A MET 1   
2  1 Y 1 A HIS -41 ? A HIS 2   
3  1 Y 1 A HIS -40 ? A HIS 3   
4  1 Y 1 A HIS -39 ? A HIS 4   
5  1 Y 1 A HIS -38 ? A HIS 5   
6  1 Y 1 A HIS -37 ? A HIS 6   
7  1 Y 1 A HIS -36 ? A HIS 7   
8  1 Y 1 A SER -35 ? A SER 8   
9  1 Y 1 A SER -34 ? A SER 9   
10 1 Y 1 A GLY -33 ? A GLY 10  
11 1 Y 1 A LEU -32 ? A LEU 11  
12 1 Y 1 A VAL -31 ? A VAL 12  
13 1 Y 1 A PRO -30 ? A PRO 13  
14 1 Y 1 A ARG -29 ? A ARG 14  
15 1 Y 1 A GLY -28 ? A GLY 15  
16 1 Y 1 A SER -27 ? A SER 16  
17 1 Y 1 A GLY -26 ? A GLY 17  
18 1 Y 1 A MET -25 ? A MET 18  
19 1 Y 1 A LYS -24 ? A LYS 19  
20 1 Y 1 A GLU -23 ? A GLU 20  
21 1 Y 1 A THR -22 ? A THR 21  
22 1 Y 1 A ALA -21 ? A ALA 22  
23 1 Y 1 A ALA -20 ? A ALA 23  
24 1 Y 1 A ALA -19 ? A ALA 24  
25 1 Y 1 A LYS -18 ? A LYS 25  
26 1 Y 1 A PHE -17 ? A PHE 26  
27 1 Y 1 A GLU -16 ? A GLU 27  
28 1 Y 1 A ARG -15 ? A ARG 28  
29 1 Y 1 A GLN -14 ? A GLN 29  
30 1 Y 1 A HIS -13 ? A HIS 30  
31 1 Y 1 A MET -12 ? A MET 31  
32 1 Y 1 A ASP -11 ? A ASP 32  
33 1 Y 1 A SER -10 ? A SER 33  
34 1 Y 1 A PRO -9  ? A PRO 34  
35 1 Y 1 A ASP -8  ? A ASP 35  
36 1 Y 1 A LEU -7  ? A LEU 36  
37 1 Y 1 A GLY -6  ? A GLY 37  
38 1 Y 1 A THR -5  ? A THR 38  
39 1 Y 1 A ASP -4  ? A ASP 39  
40 1 Y 1 A ARG 89  ? A ARG 132 
41 1 Y 1 A ARG 90  ? A ARG 133 
42 1 Y 1 A PRO 91  ? A PRO 134 
43 1 Y 1 A ASP 92  ? A ASP 135 
44 1 Y 1 A HIS 374 ? A HIS 417 
45 1 Y 1 A SER 375 ? A SER 418 
46 1 Y 1 A HIS 376 ? A HIS 419 
47 1 Y 1 A THR 377 ? A THR 420 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'French National Research Agency'                         France ANR-10-LABX-0036_NETRNA 1 
'French Infrastructure for Integrated Structural Biology' France ANR-10-INSB-05          2 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PHOSPHATE ION' PO4 
3 GLYCEROL        GOL 
4 'ACETATE ION'   ACT 
5 water           HOH 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 SAXS             ? 
2 1 'gel filtration' ? 
# 



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.