data_5AG1
# 
_entry.id   5AG1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5AG1         
PDBE  EBI-62853    
WWPDB D_1290062853 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          5AG0 
_pdbx_database_related.content_type   unspecified 
_pdbx_database_related.details        'DYP-TYPE PEROXIDASE OF AURICULARIA AURICULA-JUDAE ( AAUDYPI) CRYSTALLIZED AT PH 6.5' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        5AG1 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2015-01-27 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Strittmatter, E.' 1 
'Piontek, K.'      2 
'Plattner, D.A.'   3 
# 
_citation.id                        primary 
_citation.title                     'Crystallographic Trapping of a Covalently Modified Heme in a Dye-Decolorizing Peroxidase' 
_citation.journal_abbrev            'To be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Strittmatter, E.' 1 
primary 'Piontek, K.'      2 
primary 'Plattner, D.A.'   3 
# 
_cell.entry_id           5AG1 
_cell.length_a           66.000 
_cell.length_b           46.780 
_cell.length_c           148.150 
_cell.angle_alpha        90.00 
_cell.angle_beta         100.53 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         5AG1 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
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     nat 'DYE-DECOLORIZING PEROXIDASE' 46805.855 2   1.11.1.19 ? 'DYP-TYPE PEROXIDASE DOMAIN, RESIDUES 64-509' 
;INCLUDING THE TWO PROTEIN CHAINS, THE CO- FACTOR DELTA-MESO NITROHEME, CARBOHYDRATE MOLECULES, CACODYLATE, FORMATE, GLYCEROL, NITRITE, AND WATER MOLECULES.
;
2 non-polymer syn 'CACODYLATE ION'              136.989   2   ?         ? ?                                             ? 
3 non-polymer syn GLYCEROL                      92.094    8   ?         ? ?                                             ? 
4 non-polymer man N-ACETYL-D-GLUCOSAMINE        221.208   6   ?         ? ?                                             ? 
5 non-polymer syn 'DELTA-MESO NITROHEME'        659.469   2   ?         ? ?                                             ? 
6 non-polymer syn 'FORMIC ACID'                 46.025    1   ?         ? ?                                             ? 
7 non-polymer syn 'NITRITE ION'                 46.005    2   ?         ? ?                                             ? 
8 water       nat water                         18.015    893 ?         ? ?                                             ? 
# 
_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       
;SLNTDDIQGDILVGMHKQKQLFYFFAINDPATFKTHLASDIAPVVASVTQLSNVATQPLVALNIAFSNTGLLALGVTDNL
GDSLFANGQAKDATSFKESTSSWVPQFAGTGIHGVIILASDTTDLIDQQVASIESTFGSSISKLYSLSASIRPGNEAGHE
MFGFLDGIAQPAINGFNTPLPGQNIVDAGVIITGATNDPITRPSWAVGGSFLAFRQLEQLVPEFNKYLLDNAPAGSGSLQ
ARADLLGARMVGRWKSGAPIDLTPTADDPALGADAQRNNNFTYSHAGFDLGSDQSHCPFSAHIRKTRPRADLGGSLTPPN
LSAGANSIMRSGIPYGPEVTSAESASNTTTQERGLAFVAYQAQLSQGFHFLQQTWADNANFPPGKTPATVGLDPIIGQNN
GQPRVVNGLLPSNSSASLSIPQFVVSHGGEYFFSPPISAIGGRLSA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SLNTDDIQGDILVGMHKQKQLFYFFAINDPATFKTHLASDIAPVVASVTQLSNVATQPLVALNIAFSNTGLLALGVTDNL
GDSLFANGQAKDATSFKESTSSWVPQFAGTGIHGVIILASDTTDLIDQQVASIESTFGSSISKLYSLSASIRPGNEAGHE
MFGFLDGIAQPAINGFNTPLPGQNIVDAGVIITGATNDPITRPSWAVGGSFLAFRQLEQLVPEFNKYLLDNAPAGSGSLQ
ARADLLGARMVGRWKSGAPIDLTPTADDPALGADAQRNNNFTYSHAGFDLGSDQSHCPFSAHIRKTRPRADLGGSLTPPN
LSAGANSIMRSGIPYGPEVTSAESASNTTTQERGLAFVAYQAQLSQGFHFLQQTWADNANFPPGKTPATVGLDPIIGQNN
GQPRVVNGLLPSNSSASLSIPQFVVSHGGEYFFSPPISAIGGRLSA
;
_entity_poly.pdbx_strand_id                 A,B 
_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   SER n 
1 2   LEU n 
1 3   ASN n 
1 4   THR n 
1 5   ASP n 
1 6   ASP n 
1 7   ILE n 
1 8   GLN n 
1 9   GLY n 
1 10  ASP n 
1 11  ILE n 
1 12  LEU n 
1 13  VAL n 
1 14  GLY n 
1 15  MET n 
1 16  HIS n 
1 17  LYS n 
1 18  GLN n 
1 19  LYS n 
1 20  GLN n 
1 21  LEU n 
1 22  PHE n 
1 23  TYR n 
1 24  PHE n 
1 25  PHE n 
1 26  ALA n 
1 27  ILE n 
1 28  ASN n 
1 29  ASP n 
1 30  PRO n 
1 31  ALA n 
1 32  THR n 
1 33  PHE n 
1 34  LYS n 
1 35  THR n 
1 36  HIS n 
1 37  LEU n 
1 38  ALA n 
1 39  SER n 
1 40  ASP n 
1 41  ILE n 
1 42  ALA n 
1 43  PRO n 
1 44  VAL n 
1 45  VAL n 
1 46  ALA n 
1 47  SER n 
1 48  VAL n 
1 49  THR n 
1 50  GLN n 
1 51  LEU n 
1 52  SER n 
1 53  ASN n 
1 54  VAL n 
1 55  ALA n 
1 56  THR n 
1 57  GLN n 
1 58  PRO n 
1 59  LEU n 
1 60  VAL n 
1 61  ALA n 
1 62  LEU n 
1 63  ASN n 
1 64  ILE n 
1 65  ALA n 
1 66  PHE n 
1 67  SER n 
1 68  ASN n 
1 69  THR n 
1 70  GLY n 
1 71  LEU n 
1 72  LEU n 
1 73  ALA n 
1 74  LEU n 
1 75  GLY n 
1 76  VAL n 
1 77  THR n 
1 78  ASP n 
1 79  ASN n 
1 80  LEU n 
1 81  GLY n 
1 82  ASP n 
1 83  SER n 
1 84  LEU n 
1 85  PHE n 
1 86  ALA n 
1 87  ASN n 
1 88  GLY n 
1 89  GLN n 
1 90  ALA n 
1 91  LYS n 
1 92  ASP n 
1 93  ALA n 
1 94  THR n 
1 95  SER n 
1 96  PHE n 
1 97  LYS n 
1 98  GLU n 
1 99  SER n 
1 100 THR n 
1 101 SER n 
1 102 SER n 
1 103 TRP n 
1 104 VAL n 
1 105 PRO n 
1 106 GLN n 
1 107 PHE n 
1 108 ALA n 
1 109 GLY n 
1 110 THR n 
1 111 GLY n 
1 112 ILE n 
1 113 HIS n 
1 114 GLY n 
1 115 VAL n 
1 116 ILE n 
1 117 ILE n 
1 118 LEU n 
1 119 ALA n 
1 120 SER n 
1 121 ASP n 
1 122 THR n 
1 123 THR n 
1 124 ASP n 
1 125 LEU n 
1 126 ILE n 
1 127 ASP n 
1 128 GLN n 
1 129 GLN n 
1 130 VAL n 
1 131 ALA n 
1 132 SER n 
1 133 ILE n 
1 134 GLU n 
1 135 SER n 
1 136 THR n 
1 137 PHE n 
1 138 GLY n 
1 139 SER n 
1 140 SER n 
1 141 ILE n 
1 142 SER n 
1 143 LYS n 
1 144 LEU n 
1 145 TYR n 
1 146 SER n 
1 147 LEU n 
1 148 SER n 
1 149 ALA n 
1 150 SER n 
1 151 ILE n 
1 152 ARG n 
1 153 PRO n 
1 154 GLY n 
1 155 ASN n 
1 156 GLU n 
1 157 ALA n 
1 158 GLY n 
1 159 HIS n 
1 160 GLU n 
1 161 MET n 
1 162 PHE n 
1 163 GLY n 
1 164 PHE n 
1 165 LEU n 
1 166 ASP n 
1 167 GLY n 
1 168 ILE n 
1 169 ALA n 
1 170 GLN n 
1 171 PRO n 
1 172 ALA n 
1 173 ILE n 
1 174 ASN n 
1 175 GLY n 
1 176 PHE n 
1 177 ASN n 
1 178 THR n 
1 179 PRO n 
1 180 LEU n 
1 181 PRO n 
1 182 GLY n 
1 183 GLN n 
1 184 ASN n 
1 185 ILE n 
1 186 VAL n 
1 187 ASP n 
1 188 ALA n 
1 189 GLY n 
1 190 VAL n 
1 191 ILE n 
1 192 ILE n 
1 193 THR n 
1 194 GLY n 
1 195 ALA n 
1 196 THR n 
1 197 ASN n 
1 198 ASP n 
1 199 PRO n 
1 200 ILE n 
1 201 THR n 
1 202 ARG n 
1 203 PRO n 
1 204 SER n 
1 205 TRP n 
1 206 ALA n 
1 207 VAL n 
1 208 GLY n 
1 209 GLY n 
1 210 SER n 
1 211 PHE n 
1 212 LEU n 
1 213 ALA n 
1 214 PHE n 
1 215 ARG n 
1 216 GLN n 
1 217 LEU n 
1 218 GLU n 
1 219 GLN n 
1 220 LEU n 
1 221 VAL n 
1 222 PRO n 
1 223 GLU n 
1 224 PHE n 
1 225 ASN n 
1 226 LYS n 
1 227 TYR n 
1 228 LEU n 
1 229 LEU n 
1 230 ASP n 
1 231 ASN n 
1 232 ALA n 
1 233 PRO n 
1 234 ALA n 
1 235 GLY n 
1 236 SER n 
1 237 GLY n 
1 238 SER n 
1 239 LEU n 
1 240 GLN n 
1 241 ALA n 
1 242 ARG n 
1 243 ALA n 
1 244 ASP n 
1 245 LEU n 
1 246 LEU n 
1 247 GLY n 
1 248 ALA n 
1 249 ARG n 
1 250 MET n 
1 251 VAL n 
1 252 GLY n 
1 253 ARG n 
1 254 TRP n 
1 255 LYS n 
1 256 SER n 
1 257 GLY n 
1 258 ALA n 
1 259 PRO n 
1 260 ILE n 
1 261 ASP n 
1 262 LEU n 
1 263 THR n 
1 264 PRO n 
1 265 THR n 
1 266 ALA n 
1 267 ASP n 
1 268 ASP n 
1 269 PRO n 
1 270 ALA n 
1 271 LEU n 
1 272 GLY n 
1 273 ALA n 
1 274 ASP n 
1 275 ALA n 
1 276 GLN n 
1 277 ARG n 
1 278 ASN n 
1 279 ASN n 
1 280 ASN n 
1 281 PHE n 
1 282 THR n 
1 283 TYR n 
1 284 SER n 
1 285 HIS n 
1 286 ALA n 
1 287 GLY n 
1 288 PHE n 
1 289 ASP n 
1 290 LEU n 
1 291 GLY n 
1 292 SER n 
1 293 ASP n 
1 294 GLN n 
1 295 SER n 
1 296 HIS n 
1 297 CYS n 
1 298 PRO n 
1 299 PHE n 
1 300 SER n 
1 301 ALA n 
1 302 HIS n 
1 303 ILE n 
1 304 ARG n 
1 305 LYS n 
1 306 THR n 
1 307 ARG n 
1 308 PRO n 
1 309 ARG n 
1 310 ALA n 
1 311 ASP n 
1 312 LEU n 
1 313 GLY n 
1 314 GLY n 
1 315 SER n 
1 316 LEU n 
1 317 THR n 
1 318 PRO n 
1 319 PRO n 
1 320 ASN n 
1 321 LEU n 
1 322 SER n 
1 323 ALA n 
1 324 GLY n 
1 325 ALA n 
1 326 ASN n 
1 327 SER n 
1 328 ILE n 
1 329 MET n 
1 330 ARG n 
1 331 SER n 
1 332 GLY n 
1 333 ILE n 
1 334 PRO n 
1 335 TYR n 
1 336 GLY n 
1 337 PRO n 
1 338 GLU n 
1 339 VAL n 
1 340 THR n 
1 341 SER n 
1 342 ALA n 
1 343 GLU n 
1 344 SER n 
1 345 ALA n 
1 346 SER n 
1 347 ASN n 
1 348 THR n 
1 349 THR n 
1 350 THR n 
1 351 GLN n 
1 352 GLU n 
1 353 ARG n 
1 354 GLY n 
1 355 LEU n 
1 356 ALA n 
1 357 PHE n 
1 358 VAL n 
1 359 ALA n 
1 360 TYR n 
1 361 GLN n 
1 362 ALA n 
1 363 GLN n 
1 364 LEU n 
1 365 SER n 
1 366 GLN n 
1 367 GLY n 
1 368 PHE n 
1 369 HIS n 
1 370 PHE n 
1 371 LEU n 
1 372 GLN n 
1 373 GLN n 
1 374 THR n 
1 375 TRP n 
1 376 ALA n 
1 377 ASP n 
1 378 ASN n 
1 379 ALA n 
1 380 ASN n 
1 381 PHE n 
1 382 PRO n 
1 383 PRO n 
1 384 GLY n 
1 385 LYS n 
1 386 THR n 
1 387 PRO n 
1 388 ALA n 
1 389 THR n 
1 390 VAL n 
1 391 GLY n 
1 392 LEU n 
1 393 ASP n 
1 394 PRO n 
1 395 ILE n 
1 396 ILE n 
1 397 GLY n 
1 398 GLN n 
1 399 ASN n 
1 400 ASN n 
1 401 GLY n 
1 402 GLN n 
1 403 PRO n 
1 404 ARG n 
1 405 VAL n 
1 406 VAL n 
1 407 ASN n 
1 408 GLY n 
1 409 LEU n 
1 410 LEU n 
1 411 PRO n 
1 412 SER n 
1 413 ASN n 
1 414 SER n 
1 415 SER n 
1 416 ALA n 
1 417 SER n 
1 418 LEU n 
1 419 SER n 
1 420 ILE n 
1 421 PRO n 
1 422 GLN n 
1 423 PHE n 
1 424 VAL n 
1 425 VAL n 
1 426 SER n 
1 427 HIS n 
1 428 GLY n 
1 429 GLY n 
1 430 GLU n 
1 431 TYR n 
1 432 PHE n 
1 433 PHE n 
1 434 SER n 
1 435 PRO n 
1 436 PRO n 
1 437 ILE n 
1 438 SER n 
1 439 ALA n 
1 440 ILE n 
1 441 GLY n 
1 442 GLY n 
1 443 ARG n 
1 444 LEU n 
1 445 SER n 
1 446 ALA n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                'EAR FUNGUS' 
_entity_src_nat.pdbx_organism_scientific   'AURICULARIA AURICULA-JUDAE' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      29892 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     SXM9-C021 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    'GERMAN COLLECTION OF MICROORGANISMS (DSM), ACCESS NUMBER DSM 11326' 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    I2DBY1_9HOMO 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          I2DBY1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5AG1 A 1 ? 446 ? I2DBY1 64 ? 509 ? 3 448 
2 1 5AG1 B 1 ? 446 ? I2DBY1 64 ? 509 ? 3 448 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ?                               'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE               ?                               'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE             ?                               'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ?                               'C4 H7 N O4'       133.103 
CAC non-polymer         . 'CACODYLATE ION'       dimethylarsinate                'C2 H6 As O2 -1'   136.989 
CYS 'L-peptide linking' y CYSTEINE               ?                               'C3 H7 N O2 S'     121.158 
FMT non-polymer         . 'FORMIC ACID'          ?                               'C H2 O2'          46.025  
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 
N7H non-polymer         . 'DELTA-MESO NITROHEME' ?                               'C34 H29 Fe N5 O6' 659.469 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ?                               'C8 H15 N O6'      221.208 
NO2 non-polymer         . 'NITRITE ION'          ?                               'N O2 -1'          46.005  
PHE 'L-peptide linking' y PHENYLALANINE          ?                               'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                ?                               'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                 ?                               'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE              ?                               'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ?                               'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE               ?                               'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                 ?                               'C5 H11 N O2'      117.146 
# 
_exptl.entry_id          5AG1 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.2 
_exptl_crystal.density_percent_sol   44 
_exptl_crystal.description           NONE 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
'0.17 M SODIUM ACETATE TRIHYDRATE, 0.085 M SODIUM CACODYLATE PH 6.5, 25% (W/V) PEG 8000, 15% (V/V) GLYCEROL' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315r' 
_diffrn_detector.pdbx_collection_date   2013-06-28 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.939 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID14-4' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID14-4 
_diffrn_source.pdbx_wavelength             0.939 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     5AG1 
_reflns.observed_criterion_sigma_I   -3.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.57 
_reflns.d_resolution_high            1.85 
_reflns.number_obs                   75411 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.2 
_reflns.pdbx_Rmerge_I_obs            0.10 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        10.11 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              3.2 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             1.85 
_reflns_shell.d_res_low              1.96 
_reflns_shell.percent_possible_all   91.4 
_reflns_shell.Rmerge_I_obs           0.51 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.10 
_reflns_shell.pdbx_redundancy        2.8 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 5AG1 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     71625 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             44.57 
_refine.ls_d_res_high                            1.85 
_refine.ls_percent_reflns_obs                    98.41 
_refine.ls_R_factor_obs                          0.17655 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.17451 
_refine.ls_R_factor_R_free                       0.21547 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  3770 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.954 
_refine.correlation_coeff_Fo_to_Fc_free          0.930 
_refine.B_iso_mean                               16.212 
_refine.aniso_B[1][1]                            -0.33 
_refine.aniso_B[2][2]                            0.17 
_refine.aniso_B[3][3]                            0.38 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.65 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  
;HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY PROTEIN WAS TREATED WITH PROLI NONOATE AND PERACETIC ACID PRIOR TO CRYSTALLIZATION.
;
_refine.pdbx_starting_model                      'PDB ENTRY 4AU9' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.145 
_refine.pdbx_overall_ESU_R_Free                  0.135 
_refine.overall_SU_ML                            0.093 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             3.131 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6604 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         243 
_refine_hist.number_atoms_solvent             893 
_refine_hist.number_atoms_total               7740 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        44.57 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.003  0.019  ? 7097 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          0.674  1.985  ? 9708 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.781  5.000  ? 910  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       37.936 25.000 ? 292  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       11.719 15.000 ? 994  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       22.795 15.000 ? 28   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.051  0.200  ? 1086 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.021  ? 5521 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.862  1.918  ? 3616 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.343  3.231  ? 4534 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.212  2.048  ? 3481 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.850 
_refine_ls_shell.d_res_low                        1.898 
_refine_ls_shell.number_reflns_R_work             4603 
_refine_ls_shell.R_factor_R_work                  0.291 
_refine_ls_shell.percent_reflns_obs               86.49 
_refine_ls_shell.R_factor_R_free                  0.315 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             242 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  5AG1 
_struct.title                     'DyP-type peroxidase of Auricularia auricula-judae (AauDyPI) with meso- nitrated heme' 
_struct.pdbx_descriptor           'DYE-DECOLORIZING PEROXIDASE (E.C.1.11.1.19)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        5AG1 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'OXIDOREDUCTASE, DYP, FUNGAL, HEME, GLYCOPROTEIN, NITRATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 5 ? 
M N N 6 ? 
N N N 7 ? 
O N N 2 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 3 ? 
S N N 3 ? 
T N N 4 ? 
U N N 4 ? 
V N N 5 ? 
W N N 7 ? 
X N N 8 ? 
Y N N 8 ? 
# 
_struct_biol.id   1 
# 
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  1  GLN A 8   ? VAL A 13  ? GLN A 10  VAL A 15  1 ? 6  
HELX_P HELX_P2  2  ASP A 29  ? ASP A 40  ? ASP A 31  ASP A 42  1 ? 12 
HELX_P HELX_P3  3  ILE A 41  ? VAL A 44  ? ILE A 43  VAL A 46  5 ? 4  
HELX_P HELX_P4  4  SER A 47  ? SER A 52  ? SER A 49  SER A 54  1 ? 6  
HELX_P HELX_P5  5  ASN A 53  ? GLN A 57  ? ASN A 55  GLN A 59  5 ? 5  
HELX_P HELX_P6  6  SER A 67  ? LEU A 74  ? SER A 69  LEU A 76  1 ? 8  
HELX_P HELX_P7  7  ASP A 82  ? GLY A 88  ? ASP A 84  GLY A 90  1 ? 7  
HELX_P HELX_P8  8  GLY A 88  ? ALA A 93  ? GLY A 90  ALA A 95  1 ? 6  
HELX_P HELX_P9  9  THR A 94  ? LYS A 97  ? THR A 96  LYS A 99  5 ? 4  
HELX_P HELX_P10 10 SER A 99  ? TRP A 103 ? SER A 101 TRP A 105 5 ? 5  
HELX_P HELX_P11 11 VAL A 104 ? ALA A 108 ? VAL A 106 ALA A 110 5 ? 5  
HELX_P HELX_P12 12 THR A 122 ? GLY A 138 ? THR A 124 GLY A 140 1 ? 17 
HELX_P HELX_P13 13 PRO A 153 ? ALA A 157 ? PRO A 155 ALA A 159 5 ? 5  
HELX_P HELX_P14 14 ASP A 187 ? ILE A 191 ? ASP A 189 ILE A 193 5 ? 5  
HELX_P HELX_P15 15 PRO A 203 ? VAL A 207 ? PRO A 205 VAL A 209 5 ? 5  
HELX_P HELX_P16 16 LEU A 220 ? ALA A 232 ? LEU A 222 ALA A 234 1 ? 13 
HELX_P HELX_P17 17 SER A 238 ? GLY A 252 ? SER A 240 GLY A 254 1 ? 15 
HELX_P HELX_P18 18 ASP A 268 ? ALA A 273 ? ASP A 270 ALA A 275 1 ? 6  
HELX_P HELX_P19 19 ALA A 301 ? ARG A 307 ? ALA A 303 ARG A 309 1 ? 7  
HELX_P HELX_P20 20 PRO A 308 ? GLY A 313 ? PRO A 310 GLY A 315 5 ? 6  
HELX_P HELX_P21 21 ALA A 323 ? SER A 327 ? ALA A 325 SER A 329 5 ? 5  
HELX_P HELX_P22 22 THR A 340 ? ASN A 347 ? THR A 342 ASN A 349 1 ? 8  
HELX_P HELX_P23 23 GLY A 367 ? THR A 374 ? GLY A 369 THR A 376 1 ? 8  
HELX_P HELX_P24 24 PRO A 436 ? GLY A 441 ? PRO A 438 GLY A 443 1 ? 6  
HELX_P HELX_P25 25 GLY A 442 ? ALA A 446 ? GLY A 444 ALA A 448 5 ? 5  
HELX_P HELX_P26 26 GLN B 8   ? VAL B 13  ? GLN B 10  VAL B 15  1 ? 6  
HELX_P HELX_P27 27 ASP B 29  ? ASP B 40  ? ASP B 31  ASP B 42  1 ? 12 
HELX_P HELX_P28 28 ILE B 41  ? VAL B 44  ? ILE B 43  VAL B 46  5 ? 4  
HELX_P HELX_P29 29 SER B 47  ? ASN B 53  ? SER B 49  ASN B 55  1 ? 7  
HELX_P HELX_P30 30 VAL B 54  ? GLN B 57  ? VAL B 56  GLN B 59  5 ? 4  
HELX_P HELX_P31 31 SER B 67  ? LEU B 74  ? SER B 69  LEU B 76  1 ? 8  
HELX_P HELX_P32 32 ASP B 82  ? GLY B 88  ? ASP B 84  GLY B 90  1 ? 7  
HELX_P HELX_P33 33 GLY B 88  ? ALA B 93  ? GLY B 90  ALA B 95  1 ? 6  
HELX_P HELX_P34 34 THR B 94  ? LYS B 97  ? THR B 96  LYS B 99  5 ? 4  
HELX_P HELX_P35 35 SER B 99  ? TRP B 103 ? SER B 101 TRP B 105 5 ? 5  
HELX_P HELX_P36 36 VAL B 104 ? ALA B 108 ? VAL B 106 ALA B 110 5 ? 5  
HELX_P HELX_P37 37 THR B 122 ? GLY B 138 ? THR B 124 GLY B 140 1 ? 17 
HELX_P HELX_P38 38 PRO B 153 ? ALA B 157 ? PRO B 155 ALA B 159 5 ? 5  
HELX_P HELX_P39 39 ASP B 187 ? ILE B 191 ? ASP B 189 ILE B 193 5 ? 5  
HELX_P HELX_P40 40 PRO B 203 ? VAL B 207 ? PRO B 205 VAL B 209 5 ? 5  
HELX_P HELX_P41 41 LEU B 220 ? ALA B 232 ? LEU B 222 ALA B 234 1 ? 13 
HELX_P HELX_P42 42 SER B 238 ? GLY B 252 ? SER B 240 GLY B 254 1 ? 15 
HELX_P HELX_P43 43 ASP B 268 ? ASP B 274 ? ASP B 270 ASP B 276 1 ? 7  
HELX_P HELX_P44 44 ALA B 301 ? ARG B 307 ? ALA B 303 ARG B 309 1 ? 7  
HELX_P HELX_P45 45 PRO B 308 ? GLY B 313 ? PRO B 310 GLY B 315 5 ? 6  
HELX_P HELX_P46 46 ALA B 323 ? SER B 327 ? ALA B 325 SER B 329 5 ? 5  
HELX_P HELX_P47 47 THR B 340 ? ASN B 347 ? THR B 342 ASN B 349 1 ? 8  
HELX_P HELX_P48 48 GLY B 367 ? THR B 374 ? GLY B 369 THR B 376 1 ? 8  
HELX_P HELX_P49 49 PRO B 436 ? GLY B 441 ? PRO B 438 GLY B 443 1 ? 6  
HELX_P HELX_P50 50 GLY B 442 ? ALA B 446 ? GLY B 444 ALA B 448 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
covale1 covale ? ? A ASN 280 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 282  A NAG 1454 1_555 ? ? ? ? ? ? ? 1.435 ? 
metalc1 metalc ? ? A HIS 302 NE2 ? ? ? 1_555 L N7H . FE ? ? A HIS 304  A N7H 1458 1_555 ? ? ? ? ? ? ? 1.887 ? 
covale2 covale ? ? A ASN 347 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 349  A NAG 1455 1_555 ? ? ? ? ? ? ? 1.435 ? 
covale3 covale ? ? A ASN 413 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 415  A NAG 1456 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale4 covale ? ? H NAG .   O4  ? ? ? 1_555 I NAG . C1 ? ? A NAG 1454 A NAG 1457 1_555 ? ? ? ? ? ? ? 1.437 ? 
metalc2 metalc ? ? L N7H .   FE  ? ? ? 1_555 N NO2 . O1 ? ? A N7H 1458 A NO2 1460 1_555 ? ? ? ? ? ? ? 2.261 ? 
covale5 covale ? ? B ASN 280 ND2 ? ? ? 1_555 T NAG . C1 ? ? B ASN 282  B NAG 1454 1_555 ? ? ? ? ? ? ? 1.440 ? 
metalc3 metalc ? ? B HIS 302 NE2 ? ? ? 1_555 V N7H . FE ? ? B HIS 304  B N7H 1456 1_555 ? ? ? ? ? ? ? 1.880 ? 
covale6 covale ? ? B ASN 347 ND2 ? ? ? 1_555 U NAG . C1 ? ? B ASN 349  B NAG 1455 1_555 ? ? ? ? ? ? ? 1.438 ? 
metalc4 metalc ? ? V N7H .   FE  ? ? ? 1_555 W NO2 . O1 ? ? B N7H 1456 B NO2 1457 1_555 ? ? ? ? ? ? ? 2.341 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 318 A . ? PRO 320 A PRO 319 A ? PRO 321 A 1 4.43   
2 PHE 381 A . ? PHE 383 A PRO 382 A ? PRO 384 A 1 1.94   
3 THR 386 A . ? THR 388 A PRO 387 A ? PRO 389 A 1 -3.28  
4 ALA 286 B . ? ALA 288 B GLY 287 B ? GLY 289 B 1 -19.77 
5 PRO 318 B . ? PRO 320 B PRO 319 B ? PRO 321 B 1 -0.84  
6 PHE 381 B . ? PHE 383 B PRO 382 B ? PRO 384 B 1 5.89   
7 THR 386 B . ? THR 388 B PRO 387 B ? PRO 389 B 1 -2.47  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 4 ? 
AB ? 2 ? 
AC ? 2 ? 
AD ? 2 ? 
AE ? 4 ? 
AF ? 4 ? 
AG ? 2 ? 
BA ? 4 ? 
BB ? 2 ? 
BC ? 2 ? 
BD ? 2 ? 
BE ? 4 ? 
BF ? 4 ? 
BG ? 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 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AB 1 2 ? parallel      
AC 1 2 ? anti-parallel 
AD 1 2 ? parallel      
AE 1 2 ? anti-parallel 
AE 2 3 ? anti-parallel 
AE 3 4 ? parallel      
AF 1 2 ? anti-parallel 
AF 2 3 ? anti-parallel 
AF 3 4 ? anti-parallel 
AG 1 2 ? anti-parallel 
BA 1 2 ? anti-parallel 
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BB 1 2 ? parallel      
BC 1 2 ? anti-parallel 
BD 1 2 ? parallel      
BE 1 2 ? anti-parallel 
BE 2 3 ? anti-parallel 
BE 3 4 ? parallel      
BF 1 2 ? anti-parallel 
BF 2 3 ? anti-parallel 
BF 3 4 ? anti-parallel 
BG 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA 1 ALA A 61  ? PHE A 66  ? ALA A 63  PHE A 68  
AA 2 GLY A 114 ? SER A 120 ? GLY A 116 SER A 122 
AA 3 LYS A 19  ? ILE A 27  ? LYS A 21  ILE A 29  
AA 4 ILE A 141 ? SER A 150 ? ILE A 143 SER A 152 
AB 1 ALA A 172 ? ILE A 173 ? ALA A 174 ILE A 175 
AB 2 ILE A 185 ? VAL A 186 ? ILE A 187 VAL A 188 
AC 1 MET A 329 ? ARG A 330 ? MET A 331 ARG A 332 
AC 2 GLY A 354 ? GLN A 361 ? GLY A 356 GLN A 363 
AD 1 ILE A 333 ? TYR A 335 ? ILE A 335 TYR A 337 
AD 2 GLY A 354 ? GLN A 361 ? GLY A 356 GLN A 363 
AE 1 VAL A 424 ? SER A 434 ? VAL A 426 SER A 436 
AE 2 SER A 210 ? GLN A 219 ? SER A 212 GLN A 221 
AE 3 GLY A 354 ? GLN A 361 ? GLY A 356 GLN A 363 
AE 4 ILE A 333 ? TYR A 335 ? ILE A 335 TYR A 337 
AF 1 VAL A 424 ? SER A 434 ? VAL A 426 SER A 436 
AF 2 SER A 210 ? GLN A 219 ? SER A 212 GLN A 221 
AF 3 GLY A 354 ? GLN A 361 ? GLY A 356 GLN A 363 
AF 4 MET A 329 ? ARG A 330 ? MET A 331 ARG A 332 
AG 1 ARG A 404 ? ASN A 407 ? ARG A 406 ASN A 409 
AG 2 SER A 417 ? ILE A 420 ? SER A 419 ILE A 422 
BA 1 VAL B 60  ? PHE B 66  ? VAL B 62  PHE B 68  
BA 2 GLY B 114 ? SER B 120 ? GLY B 116 SER B 122 
BA 3 LYS B 19  ? ILE B 27  ? LYS B 21  ILE B 29  
BA 4 ILE B 141 ? SER B 150 ? ILE B 143 SER B 152 
BB 1 ALA B 172 ? ILE B 173 ? ALA B 174 ILE B 175 
BB 2 ILE B 185 ? VAL B 186 ? ILE B 187 VAL B 188 
BC 1 MET B 329 ? ARG B 330 ? MET B 331 ARG B 332 
BC 2 GLY B 354 ? GLN B 361 ? GLY B 356 GLN B 363 
BD 1 ILE B 333 ? TYR B 335 ? ILE B 335 TYR B 337 
BD 2 GLY B 354 ? GLN B 361 ? GLY B 356 GLN B 363 
BE 1 VAL B 424 ? SER B 434 ? VAL B 426 SER B 436 
BE 2 SER B 210 ? GLN B 219 ? SER B 212 GLN B 221 
BE 3 GLY B 354 ? GLN B 361 ? GLY B 356 GLN B 363 
BE 4 ILE B 333 ? TYR B 335 ? ILE B 335 TYR B 337 
BF 1 VAL B 424 ? SER B 434 ? VAL B 426 SER B 436 
BF 2 SER B 210 ? GLN B 219 ? SER B 212 GLN B 221 
BF 3 GLY B 354 ? GLN B 361 ? GLY B 356 GLN B 363 
BF 4 MET B 329 ? ARG B 330 ? MET B 331 ARG B 332 
BG 1 ARG B 404 ? ASN B 407 ? ARG B 406 ASN B 409 
BG 2 SER B 417 ? ILE B 420 ? SER B 419 ILE B 422 
# 
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 
AA 1 2 N ALA A 65  ? N ALA A 67  O VAL A 115 ? O VAL A 117 
AA 2 3 N SER A 120 ? N SER A 122 O LYS A 19  ? O LYS A 21  
AA 3 4 N ALA A 26  ? N ALA A 28  O SER A 142 ? O SER A 144 
AB 1 2 O ALA A 172 ? O ALA A 174 N VAL A 186 ? N VAL A 188 
AC 1 2 N MET A 329 ? N MET A 331 O TYR A 360 ? O TYR A 362 
AD 1 2 N TYR A 335 ? N TYR A 337 O GLY A 354 ? O GLY A 356 
AE 1 2 N SER A 434 ? N SER A 436 O SER A 210 ? O SER A 212 
AE 2 3 N LEU A 217 ? N LEU A 219 O LEU A 355 ? O LEU A 357 
AE 3 4 N ALA A 356 ? N ALA A 358 O ILE A 333 ? O ILE A 335 
AF 1 2 N SER A 434 ? N SER A 436 O SER A 210 ? O SER A 212 
AF 2 3 N LEU A 217 ? N LEU A 219 O LEU A 355 ? O LEU A 357 
AF 3 4 N TYR A 360 ? N TYR A 362 O MET A 329 ? O MET A 331 
AG 1 2 N VAL A 406 ? N VAL A 408 O LEU A 418 ? O LEU A 420 
BA 1 2 N ALA B 65  ? N ALA B 67  O VAL B 115 ? O VAL B 117 
BA 2 3 N SER B 120 ? N SER B 122 O LYS B 19  ? O LYS B 21  
BA 3 4 N ALA B 26  ? N ALA B 28  O SER B 142 ? O SER B 144 
BB 1 2 O ALA B 172 ? O ALA B 174 N VAL B 186 ? N VAL B 188 
BC 1 2 N MET B 329 ? N MET B 331 O TYR B 360 ? O TYR B 362 
BD 1 2 N TYR B 335 ? N TYR B 337 O GLY B 354 ? O GLY B 356 
BE 1 2 N SER B 434 ? N SER B 436 O SER B 210 ? O SER B 212 
BE 2 3 N LEU B 217 ? N LEU B 219 O LEU B 355 ? O LEU B 357 
BE 3 4 N ALA B 356 ? N ALA B 358 O ILE B 333 ? O ILE B 335 
BF 1 2 N SER B 434 ? N SER B 436 O SER B 210 ? O SER B 212 
BF 2 3 N LEU B 217 ? N LEU B 219 O LEU B 355 ? O LEU B 357 
BF 3 4 N TYR B 360 ? N TYR B 362 O MET B 329 ? O MET B 331 
BG 1 2 N VAL B 406 ? N VAL B 408 O LEU B 418 ? O LEU B 420 
# 
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 ? ? ? ? 4  'BINDING SITE FOR RESIDUE CAC A 1449'                                                      
AC2 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE CAC B 1449'                                                      
AC3 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE GOL A 1450'                                                      
AC4 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE GOL B 1450'                                                      
AC5 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE GOL A 1451'                                                      
AC6 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE GOL B 1451'                                                      
AC7 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE GOL B 1452'                                                      
AC8 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE GOL B 1453'                                                      
AC9 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE GOL A 1452'                                                      
BC1 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE GOL A 1453'                                                      
BC2 Software ? ? ? ? 24 'BINDING SITE FOR RESIDUE N7H A 1458'                                                      
BC3 Software ? ? ? ? 25 'BINDING SITE FOR RESIDUE N7H B 1456'                                                      
BC4 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE FMT A 1459'                                                      
BC5 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NO2 A 1460'                                                      
BC6 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NO2 B 1457'                                                      
BC7 Software ? ? ? ? 6  'Binding site for Poly-Saccharide residues NAG A1454 through NAG A1457 bound to ASN A 282' 
BC8 Software ? ? ? ? 6  'Binding site for Mono-Saccharide NAG A1455 bound to ASN A 349'                            
BC9 Software ? ? ? ? 7  'Binding site for Mono-Saccharide NAG A1456 bound to ASN A 415'                            
CC1 Software ? ? ? ? 7  'Binding site for Mono-Saccharide NAG B1454 bound to ASN B 282'                            
CC2 Software ? ? ? ? 5  'Binding site for Mono-Saccharide NAG B1455 bound to ASN B 349'                            
# 
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 4  SER A 284 ? SER A 286  . ? 1_555 ? 
2   AC1 4  HIS A 285 ? HIS A 287  . ? 1_555 ? 
3   AC1 4  ALA A 286 ? ALA A 288  . ? 1_555 ? 
4   AC1 4  HOH X .   ? HOH A 2375 . ? 1_555 ? 
5   AC2 2  HIS B 285 ? HIS B 287  . ? 1_555 ? 
6   AC2 2  ALA B 286 ? ALA B 288  . ? 1_555 ? 
7   AC3 8  ASP A 124 ? ASP A 126  . ? 1_555 ? 
8   AC3 8  GLN A 128 ? GLN A 130  . ? 1_555 ? 
9   AC3 8  HOH X .   ? HOH A 2218 . ? 1_555 ? 
10  AC3 8  HOH X .   ? HOH A 2474 . ? 1_555 ? 
11  AC3 8  HOH X .   ? HOH A 2475 . ? 1_555 ? 
12  AC3 8  SER B 150 ? SER B 152  . ? 1_555 ? 
13  AC3 8  PRO B 337 ? PRO B 339  . ? 1_555 ? 
14  AC3 8  GOL S .   ? GOL B 1453 . ? 1_555 ? 
15  AC4 10 LYS A 19  ? LYS A 21   . ? 1_555 ? 
16  AC4 10 SER A 150 ? SER A 152  . ? 1_555 ? 
17  AC4 10 PRO A 337 ? PRO A 339  . ? 1_555 ? 
18  AC4 10 GLU A 338 ? GLU A 340  . ? 1_555 ? 
19  AC4 10 HOH X .   ? HOH A 2244 . ? 1_555 ? 
20  AC4 10 HOH X .   ? HOH A 2410 . ? 1_555 ? 
21  AC4 10 HOH X .   ? HOH A 2412 . ? 1_555 ? 
22  AC4 10 ASP B 124 ? ASP B 126  . ? 1_555 ? 
23  AC4 10 ASP B 127 ? ASP B 129  . ? 1_555 ? 
24  AC4 10 GLN B 128 ? GLN B 130  . ? 1_555 ? 
25  AC5 8  ARG A 152 ? ARG A 154  . ? 1_555 ? 
26  AC5 8  GLU A 156 ? GLU A 158  . ? 1_555 ? 
27  AC5 8  PHE A 162 ? PHE A 164  . ? 1_555 ? 
28  AC5 8  GLY A 163 ? GLY A 165  . ? 1_555 ? 
29  AC5 8  ASN A 225 ? ASN A 227  . ? 1_555 ? 
30  AC5 8  LYS A 255 ? LYS A 257  . ? 1_555 ? 
31  AC5 8  HOH X .   ? HOH A 2307 . ? 1_555 ? 
32  AC5 8  HOH X .   ? HOH A 2476 . ? 1_555 ? 
33  AC6 5  ARG A 443 ? ARG A 445  . ? 1_645 ? 
34  AC6 5  PRO B 199 ? PRO B 201  . ? 1_555 ? 
35  AC6 5  ILE B 200 ? ILE B 202  . ? 1_555 ? 
36  AC6 5  THR B 201 ? THR B 203  . ? 1_555 ? 
37  AC6 5  HOH Y .   ? HOH B 2407 . ? 1_555 ? 
38  AC7 10 ARG B 249 ? ARG B 251  . ? 1_555 ? 
39  AC7 10 SER B 292 ? SER B 294  . ? 1_555 ? 
40  AC7 10 ASP B 293 ? ASP B 295  . ? 1_555 ? 
41  AC7 10 GLN B 294 ? GLN B 296  . ? 1_555 ? 
42  AC7 10 SER B 295 ? SER B 297  . ? 1_555 ? 
43  AC7 10 GLY B 408 ? GLY B 410  . ? 1_555 ? 
44  AC7 10 LEU B 410 ? LEU B 412  . ? 1_555 ? 
45  AC7 10 PRO B 411 ? PRO B 413  . ? 1_555 ? 
46  AC7 10 SER B 414 ? SER B 416  . ? 1_555 ? 
47  AC7 10 HOH Y .   ? HOH B 2317 . ? 1_555 ? 
48  AC8 7  GOL D .   ? GOL A 1450 . ? 1_555 ? 
49  AC8 7  HOH X .   ? HOH A 2211 . ? 1_555 ? 
50  AC8 7  SER B 148 ? SER B 150  . ? 1_555 ? 
51  AC8 7  SER B 150 ? SER B 152  . ? 1_555 ? 
52  AC8 7  TYR B 335 ? TYR B 337  . ? 1_555 ? 
53  AC8 7  GLY B 336 ? GLY B 338  . ? 1_555 ? 
54  AC8 7  HOH Y .   ? HOH B 2180 . ? 1_555 ? 
55  AC9 4  ALA A 270 ? ALA A 272  . ? 1_555 ? 
56  AC9 4  ASP A 274 ? ASP A 276  . ? 1_555 ? 
57  AC9 4  ARG A 277 ? ARG A 279  . ? 1_555 ? 
58  AC9 4  HOH X .   ? HOH A 2358 . ? 1_555 ? 
59  BC1 5  GLY A 194 ? GLY A 196  . ? 1_555 ? 
60  BC1 5  ALA A 195 ? ALA A 197  . ? 1_555 ? 
61  BC1 5  THR A 196 ? THR A 198  . ? 1_555 ? 
62  BC1 5  ASN A 197 ? ASN A 199  . ? 1_555 ? 
63  BC1 5  ASP A 198 ? ASP A 200  . ? 1_555 ? 
64  BC2 24 GLU A 160 ? GLU A 162  . ? 1_555 ? 
65  BC2 24 PHE A 164 ? PHE A 166  . ? 1_555 ? 
66  BC2 24 LEU A 165 ? LEU A 167  . ? 1_555 ? 
67  BC2 24 ASP A 166 ? ASP A 168  . ? 1_555 ? 
68  BC2 24 GLY A 167 ? GLY A 169  . ? 1_555 ? 
69  BC2 24 ILE A 168 ? ILE A 170  . ? 1_555 ? 
70  BC2 24 ALA A 169 ? ALA A 171  . ? 1_555 ? 
71  BC2 24 GLN A 219 ? GLN A 221  . ? 1_555 ? 
72  BC2 24 VAL A 251 ? VAL A 253  . ? 1_555 ? 
73  BC2 24 ARG A 253 ? ARG A 255  . ? 1_555 ? 
74  BC2 24 HIS A 302 ? HIS A 304  . ? 1_555 ? 
75  BC2 24 THR A 306 ? THR A 308  . ? 1_555 ? 
76  BC2 24 ARG A 307 ? ARG A 309  . ? 1_555 ? 
77  BC2 24 ARG A 309 ? ARG A 311  . ? 1_555 ? 
78  BC2 24 ARG A 330 ? ARG A 332  . ? 1_555 ? 
79  BC2 24 LEU A 355 ? LEU A 357  . ? 1_555 ? 
80  BC2 24 PHE A 357 ? PHE A 359  . ? 1_555 ? 
81  BC2 24 PHE A 368 ? PHE A 370  . ? 1_555 ? 
82  BC2 24 ILE A 396 ? ILE A 398  . ? 1_555 ? 
83  BC2 24 NO2 N .   ? NO2 A 1460 . ? 1_555 ? 
84  BC2 24 HOH X .   ? HOH A 2339 . ? 1_555 ? 
85  BC2 24 HOH X .   ? HOH A 2365 . ? 1_555 ? 
86  BC2 24 HOH X .   ? HOH A 2372 . ? 1_555 ? 
87  BC2 24 HOH X .   ? HOH A 2483 . ? 1_555 ? 
88  BC3 25 GLU B 160 ? GLU B 162  . ? 1_555 ? 
89  BC3 25 PHE B 164 ? PHE B 166  . ? 1_555 ? 
90  BC3 25 LEU B 165 ? LEU B 167  . ? 1_555 ? 
91  BC3 25 ASP B 166 ? ASP B 168  . ? 1_555 ? 
92  BC3 25 GLY B 167 ? GLY B 169  . ? 1_555 ? 
93  BC3 25 ILE B 168 ? ILE B 170  . ? 1_555 ? 
94  BC3 25 ALA B 169 ? ALA B 171  . ? 1_555 ? 
95  BC3 25 LEU B 217 ? LEU B 219  . ? 1_555 ? 
96  BC3 25 GLN B 219 ? GLN B 221  . ? 1_555 ? 
97  BC3 25 VAL B 251 ? VAL B 253  . ? 1_555 ? 
98  BC3 25 ARG B 253 ? ARG B 255  . ? 1_555 ? 
99  BC3 25 HIS B 302 ? HIS B 304  . ? 1_555 ? 
100 BC3 25 THR B 306 ? THR B 308  . ? 1_555 ? 
101 BC3 25 ARG B 307 ? ARG B 309  . ? 1_555 ? 
102 BC3 25 ARG B 309 ? ARG B 311  . ? 1_555 ? 
103 BC3 25 ARG B 330 ? ARG B 332  . ? 1_555 ? 
104 BC3 25 PHE B 357 ? PHE B 359  . ? 1_555 ? 
105 BC3 25 PHE B 368 ? PHE B 370  . ? 1_555 ? 
106 BC3 25 ILE B 396 ? ILE B 398  . ? 1_555 ? 
107 BC3 25 VAL B 424 ? VAL B 426  . ? 1_555 ? 
108 BC3 25 NO2 W .   ? NO2 B 1457 . ? 1_555 ? 
109 BC3 25 HOH Y .   ? HOH B 2273 . ? 1_555 ? 
110 BC3 25 HOH Y .   ? HOH B 2302 . ? 1_555 ? 
111 BC3 25 HOH Y .   ? HOH B 2309 . ? 1_555 ? 
112 BC3 25 HOH Y .   ? HOH B 2409 . ? 1_555 ? 
113 BC4 2  ASN A 28  ? ASN A 30   . ? 1_555 ? 
114 BC4 2  SER A 139 ? SER A 141  . ? 1_555 ? 
115 BC5 6  ASP A 166 ? ASP A 168  . ? 1_555 ? 
116 BC5 6  ARG A 330 ? ARG A 332  . ? 1_555 ? 
117 BC5 6  LEU A 355 ? LEU A 357  . ? 1_555 ? 
118 BC5 6  PHE A 357 ? PHE A 359  . ? 1_555 ? 
119 BC5 6  N7H L .   ? N7H A 1458 . ? 1_555 ? 
120 BC5 6  HOH X .   ? HOH A 2259 . ? 1_555 ? 
121 BC6 6  ASP B 166 ? ASP B 168  . ? 1_555 ? 
122 BC6 6  ARG B 330 ? ARG B 332  . ? 1_555 ? 
123 BC6 6  PHE B 357 ? PHE B 359  . ? 1_555 ? 
124 BC6 6  N7H V .   ? N7H B 1456 . ? 1_555 ? 
125 BC6 6  HOH Y .   ? HOH B 2201 . ? 1_555 ? 
126 BC6 6  HOH Y .   ? HOH B 2344 . ? 1_555 ? 
127 BC7 6  GLN A 276 ? GLN A 278  . ? 1_555 ? 
128 BC7 6  ASN A 280 ? ASN A 282  . ? 1_555 ? 
129 BC7 6  PRO A 318 ? PRO A 320  . ? 1_555 ? 
130 BC7 6  HOH X .   ? HOH A 2367 . ? 1_555 ? 
131 BC7 6  HOH X .   ? HOH A 2477 . ? 1_555 ? 
132 BC7 6  HOH X .   ? HOH A 2478 . ? 1_555 ? 
133 BC8 6  LYS A 226 ? LYS A 228  . ? 1_555 ? 
134 BC8 6  ASP A 230 ? ASP A 232  . ? 1_555 ? 
135 BC8 6  ALA A 345 ? ALA A 347  . ? 1_555 ? 
136 BC8 6  ASN A 347 ? ASN A 349  . ? 1_555 ? 
137 BC8 6  HOH X .   ? HOH A 2309 . ? 1_555 ? 
138 BC8 6  HOH X .   ? HOH A 2479 . ? 1_555 ? 
139 BC9 7  ASN A 413 ? ASN A 415  . ? 1_555 ? 
140 BC9 7  SER A 415 ? SER A 417  . ? 1_555 ? 
141 BC9 7  HOH X .   ? HOH A 2459 . ? 1_555 ? 
142 BC9 7  HOH X .   ? HOH A 2463 . ? 1_555 ? 
143 BC9 7  HOH X .   ? HOH A 2480 . ? 1_555 ? 
144 BC9 7  HOH X .   ? HOH A 2481 . ? 1_555 ? 
145 BC9 7  HOH X .   ? HOH A 2482 . ? 1_555 ? 
146 CC1 7  GLN B 276 ? GLN B 278  . ? 1_555 ? 
147 CC1 7  ARG B 277 ? ARG B 279  . ? 1_555 ? 
148 CC1 7  ASN B 280 ? ASN B 282  . ? 1_555 ? 
149 CC1 7  PRO B 318 ? PRO B 320  . ? 1_555 ? 
150 CC1 7  HOH Y .   ? HOH B 2304 . ? 1_555 ? 
151 CC1 7  HOH Y .   ? HOH B 2306 . ? 1_555 ? 
152 CC1 7  HOH Y .   ? HOH B 2408 . ? 1_555 ? 
153 CC2 5  LYS B 226 ? LYS B 228  . ? 1_555 ? 
154 CC2 5  ASP B 230 ? ASP B 232  . ? 1_555 ? 
155 CC2 5  ALA B 345 ? ALA B 347  . ? 1_555 ? 
156 CC2 5  ASN B 347 ? ASN B 349  . ? 1_555 ? 
157 CC2 5  HOH Y .   ? HOH B 2352 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          5AG1 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    5AG1 
_atom_sites.fract_transf_matrix[1][1]   0.015152 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002816 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021377 
_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]   0.006866 
_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 
AS 
C  
FE 
N  
O  
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   . SER A 1 1   ? 67.463  16.212  25.220  1.00 50.17 ? 3    SER A N   1 
ATOM   2    C  CA  . SER A 1 1   ? 68.955  16.173  25.220  1.00 50.71 ? 3    SER A CA  1 
ATOM   3    C  C   . SER A 1 1   ? 69.479  15.148  26.222  1.00 44.72 ? 3    SER A C   1 
ATOM   4    O  O   . SER A 1 1   ? 68.910  14.973  27.300  1.00 46.68 ? 3    SER A O   1 
ATOM   5    C  CB  . SER A 1 1   ? 69.527  17.557  25.532  1.00 51.50 ? 3    SER A CB  1 
ATOM   6    O  OG  . SER A 1 1   ? 68.892  18.124  26.664  1.00 53.89 ? 3    SER A OG  1 
ATOM   7    N  N   . LEU A 1 2   ? 70.571  14.480  25.861  1.00 37.51 ? 4    LEU A N   1 
ATOM   8    C  CA  . LEU A 1 2   ? 71.069  13.346  26.633  1.00 32.20 ? 4    LEU A CA  1 
ATOM   9    C  C   . LEU A 1 2   ? 71.763  13.794  27.914  1.00 29.15 ? 4    LEU A C   1 
ATOM   10   O  O   . LEU A 1 2   ? 72.576  14.717  27.903  1.00 28.45 ? 4    LEU A O   1 
ATOM   11   C  CB  . LEU A 1 2   ? 72.035  12.508  25.792  1.00 31.04 ? 4    LEU A CB  1 
ATOM   12   C  CG  . LEU A 1 2   ? 71.451  11.734  24.610  1.00 29.28 ? 4    LEU A CG  1 
ATOM   13   C  CD1 . LEU A 1 2   ? 72.568  11.127  23.778  1.00 26.01 ? 4    LEU A CD1 1 
ATOM   14   C  CD2 . LEU A 1 2   ? 70.484  10.661  25.087  1.00 28.96 ? 4    LEU A CD2 1 
ATOM   15   N  N   . ASN A 1 3   ? 71.456  13.116  29.014  1.00 24.97 ? 5    ASN A N   1 
ATOM   16   C  CA  . ASN A 1 3   ? 72.227  13.266  30.238  1.00 22.73 ? 5    ASN A CA  1 
ATOM   17   C  C   . ASN A 1 3   ? 73.383  12.271  30.278  1.00 21.18 ? 5    ASN A C   1 
ATOM   18   O  O   . ASN A 1 3   ? 73.217  11.133  30.720  1.00 18.02 ? 5    ASN A O   1 
ATOM   19   C  CB  . ASN A 1 3   ? 71.330  13.080  31.461  1.00 21.02 ? 5    ASN A CB  1 
ATOM   20   C  CG  . ASN A 1 3   ? 72.084  13.243  32.765  1.00 22.95 ? 5    ASN A CG  1 
ATOM   21   O  OD1 . ASN A 1 3   ? 73.260  13.607  32.775  1.00 24.11 ? 5    ASN A OD1 1 
ATOM   22   N  ND2 . ASN A 1 3   ? 71.413  12.962  33.874  1.00 22.66 ? 5    ASN A ND2 1 
ATOM   23   N  N   . THR A 1 4   ? 74.549  12.699  29.806  1.00 19.22 ? 6    THR A N   1 
ATOM   24   C  CA  . THR A 1 4   ? 75.662  11.779  29.603  1.00 19.06 ? 6    THR A CA  1 
ATOM   25   C  C   . THR A 1 4   ? 76.367  11.452  30.911  1.00 18.23 ? 6    THR A C   1 
ATOM   26   O  O   . THR A 1 4   ? 77.210  10.559  30.962  1.00 17.00 ? 6    THR A O   1 
ATOM   27   C  CB  . THR A 1 4   ? 76.679  12.318  28.579  1.00 20.61 ? 6    THR A CB  1 
ATOM   28   O  OG1 . THR A 1 4   ? 77.286  13.517  29.080  1.00 22.11 ? 6    THR A OG1 1 
ATOM   29   C  CG2 . THR A 1 4   ? 75.995  12.609  27.256  1.00 22.44 ? 6    THR A CG2 1 
ATOM   30   N  N   . ASP A 1 5   ? 76.018  12.182  31.965  1.00 17.90 ? 7    ASP A N   1 
ATOM   31   C  CA  . ASP A 1 5   ? 76.437  11.829  33.314  1.00 18.80 ? 7    ASP A CA  1 
ATOM   32   C  C   . ASP A 1 5   ? 75.831  10.494  33.735  1.00 18.18 ? 7    ASP A C   1 
ATOM   33   O  O   . ASP A 1 5   ? 76.359  9.816   34.615  1.00 19.09 ? 7    ASP A O   1 
ATOM   34   C  CB  . ASP A 1 5   ? 76.004  12.907  34.311  1.00 20.76 ? 7    ASP A CB  1 
ATOM   35   C  CG  . ASP A 1 5   ? 76.926  14.112  34.311  1.00 23.51 ? 7    ASP A CG  1 
ATOM   36   O  OD1 . ASP A 1 5   ? 77.974  14.072  33.634  1.00 22.35 ? 7    ASP A OD1 1 
ATOM   37   O  OD2 . ASP A 1 5   ? 76.600  15.102  34.999  1.00 25.30 ? 7    ASP A OD2 1 
ATOM   38   N  N   . ASP A 1 6   ? 74.688  10.155  33.146  1.00 16.01 ? 8    ASP A N   1 
ATOM   39   C  CA  . ASP A 1 6   ? 73.877  9.046   33.631  1.00 14.97 ? 8    ASP A CA  1 
ATOM   40   C  C   . ASP A 1 6   ? 73.889  7.852   32.678  1.00 13.92 ? 8    ASP A C   1 
ATOM   41   O  O   . ASP A 1 6   ? 73.290  6.820   32.963  1.00 14.71 ? 8    ASP A O   1 
ATOM   42   C  CB  . ASP A 1 6   ? 72.435  9.502   33.875  1.00 15.36 ? 8    ASP A CB  1 
ATOM   43   C  CG  . ASP A 1 6   ? 71.713  8.635   34.890  1.00 15.58 ? 8    ASP A CG  1 
ATOM   44   O  OD1 . ASP A 1 6   ? 72.368  8.153   35.839  1.00 15.83 ? 8    ASP A OD1 1 
ATOM   45   O  OD2 . ASP A 1 6   ? 70.485  8.451   34.753  1.00 16.39 ? 8    ASP A OD2 1 
ATOM   46   N  N   . ILE A 1 7   ? 74.540  8.013   31.531  1.00 11.85 ? 9    ILE A N   1 
ATOM   47   C  CA  . ILE A 1 7   ? 74.624  6.941   30.549  1.00 10.69 ? 9    ILE A CA  1 
ATOM   48   C  C   . ILE A 1 7   ? 75.964  6.227   30.684  1.00 10.25 ? 9    ILE A C   1 
ATOM   49   O  O   . ILE A 1 7   ? 77.006  6.873   30.793  1.00 10.16 ? 9    ILE A O   1 
ATOM   50   C  CB  . ILE A 1 7   ? 74.476  7.483   29.115  1.00 10.74 ? 9    ILE A CB  1 
ATOM   51   C  CG1 . ILE A 1 7   ? 73.155  8.246   28.965  1.00 11.52 ? 9    ILE A CG1 1 
ATOM   52   C  CG2 . ILE A 1 7   ? 74.567  6.354   28.099  1.00 10.49 ? 9    ILE A CG2 1 
ATOM   53   C  CD1 . ILE A 1 7   ? 72.991  8.921   27.619  1.00 11.90 ? 9    ILE A CD1 1 
ATOM   54   N  N   . GLN A 1 8   ? 75.934  4.898   30.685  1.00 9.73  ? 10   GLN A N   1 
ATOM   55   C  CA  . GLN A 1 8   ? 77.159  4.112   30.816  1.00 9.85  ? 10   GLN A CA  1 
ATOM   56   C  C   . GLN A 1 8   ? 78.078  4.295   29.609  1.00 10.15 ? 10   GLN A C   1 
ATOM   57   O  O   . GLN A 1 8   ? 77.622  4.343   28.470  1.00 9.87  ? 10   GLN A O   1 
ATOM   58   C  CB  . GLN A 1 8   ? 76.828  2.631   31.035  1.00 9.60  ? 10   GLN A CB  1 
ATOM   59   C  CG  . GLN A 1 8   ? 76.088  2.369   32.338  1.00 9.80  ? 10   GLN A CG  1 
ATOM   60   C  CD  . GLN A 1 8   ? 76.180  0.923   32.786  1.00 9.94  ? 10   GLN A CD  1 
ATOM   61   O  OE1 . GLN A 1 8   ? 77.268  0.354   32.865  1.00 9.52  ? 10   GLN A OE1 1 
ATOM   62   N  NE2 . GLN A 1 8   ? 75.034  0.320   33.082  1.00 9.99  ? 10   GLN A NE2 1 
ATOM   63   N  N   . GLY A 1 9   ? 79.377  4.420   29.872  1.00 10.90 ? 11   GLY A N   1 
ATOM   64   C  CA  . GLY A 1 9   ? 80.322  4.899   28.869  1.00 10.89 ? 11   GLY A CA  1 
ATOM   65   C  C   . GLY A 1 9   ? 80.388  4.059   27.607  1.00 10.66 ? 11   GLY A C   1 
ATOM   66   O  O   . GLY A 1 9   ? 80.483  4.594   26.506  1.00 11.76 ? 11   GLY A O   1 
ATOM   67   N  N   . ASP A 1 10  ? 80.354  2.740   27.761  1.00 12.01 ? 12   ASP A N   1 
ATOM   68   C  CA  . ASP A 1 10  ? 80.561  1.838   26.629  1.00 11.55 ? 12   ASP A CA  1 
ATOM   69   C  C   . ASP A 1 10  ? 79.509  2.033   25.537  1.00 11.71 ? 12   ASP A C   1 
ATOM   70   O  O   . ASP A 1 10  ? 79.776  1.788   24.360  1.00 11.55 ? 12   ASP A O   1 
ATOM   71   C  CB  . ASP A 1 10  ? 80.577  0.376   27.090  1.00 11.96 ? 12   ASP A CB  1 
ATOM   72   C  CG  . ASP A 1 10  ? 81.193  -0.558  26.053  1.00 11.98 ? 12   ASP A CG  1 
ATOM   73   O  OD1 . ASP A 1 10  ? 82.235  -0.199  25.466  1.00 12.16 ? 12   ASP A OD1 1 
ATOM   74   O  OD2 . ASP A 1 10  ? 80.640  -1.652  25.828  1.00 11.91 ? 12   ASP A OD2 1 
ATOM   75   N  N   . ILE A 1 11  ? 78.313  2.465   25.933  1.00 11.82 ? 13   ILE A N   1 
ATOM   76   C  CA  . ILE A 1 11  ? 77.189  2.576   25.005  1.00 11.84 ? 13   ILE A CA  1 
ATOM   77   C  C   . ILE A 1 11  ? 77.472  3.563   23.874  1.00 12.35 ? 13   ILE A C   1 
ATOM   78   O  O   . ILE A 1 11  ? 77.238  3.259   22.704  1.00 11.99 ? 13   ILE A O   1 
ATOM   79   C  CB  . ILE A 1 11  ? 75.885  2.982   25.729  1.00 11.95 ? 13   ILE A CB  1 
ATOM   80   C  CG1 . ILE A 1 11  ? 75.558  1.990   26.845  1.00 11.89 ? 13   ILE A CG1 1 
ATOM   81   C  CG2 . ILE A 1 11  ? 74.729  3.059   24.746  1.00 11.91 ? 13   ILE A CG2 1 
ATOM   82   C  CD1 . ILE A 1 11  ? 74.542  2.504   27.845  1.00 12.04 ? 13   ILE A CD1 1 
ATOM   83   N  N   . LEU A 1 12  ? 78.025  4.723   24.219  1.00 12.73 ? 14   LEU A N   1 
ATOM   84   C  CA  . LEU A 1 12  ? 78.136  5.818   23.258  1.00 13.39 ? 14   LEU A CA  1 
ATOM   85   C  C   . LEU A 1 12  ? 79.570  6.145   22.842  1.00 15.16 ? 14   LEU A C   1 
ATOM   86   O  O   . LEU A 1 12  ? 79.796  6.675   21.755  1.00 15.16 ? 14   LEU A O   1 
ATOM   87   C  CB  . LEU A 1 12  ? 77.429  7.070   23.781  1.00 12.53 ? 14   LEU A CB  1 
ATOM   88   C  CG  . LEU A 1 12  ? 75.903  6.973   23.857  1.00 12.95 ? 14   LEU A CG  1 
ATOM   89   C  CD1 . LEU A 1 12  ? 75.305  8.235   24.467  1.00 13.82 ? 14   LEU A CD1 1 
ATOM   90   C  CD2 . LEU A 1 12  ? 75.317  6.706   22.477  1.00 12.44 ? 14   LEU A CD2 1 
ATOM   91   N  N   . VAL A 1 13  ? 80.538  5.845   23.701  1.00 16.26 ? 15   VAL A N   1 
ATOM   92   C  CA  . VAL A 1 13  ? 81.920  6.233   23.416  1.00 17.68 ? 15   VAL A CA  1 
ATOM   93   C  C   . VAL A 1 13  ? 82.933  5.094   23.492  1.00 19.44 ? 15   VAL A C   1 
ATOM   94   O  O   . VAL A 1 13  ? 84.071  5.239   23.043  1.00 21.54 ? 15   VAL A O   1 
ATOM   95   C  CB  . VAL A 1 13  ? 82.384  7.422   24.281  1.00 17.04 ? 15   VAL A CB  1 
ATOM   96   C  CG1 . VAL A 1 13  ? 81.565  8.665   23.959  1.00 17.04 ? 15   VAL A CG1 1 
ATOM   97   C  CG2 . VAL A 1 13  ? 82.298  7.086   25.761  1.00 17.04 ? 15   VAL A CG2 1 
ATOM   98   N  N   . GLY A 1 14  ? 82.518  3.956   24.038  1.00 19.05 ? 16   GLY A N   1 
ATOM   99   C  CA  . GLY A 1 14  ? 83.429  2.832   24.234  1.00 20.35 ? 16   GLY A CA  1 
ATOM   100  C  C   . GLY A 1 14  ? 84.326  3.021   25.444  1.00 20.67 ? 16   GLY A C   1 
ATOM   101  O  O   . GLY A 1 14  ? 84.400  4.114   26.004  1.00 21.70 ? 16   GLY A O   1 
ATOM   102  N  N   . MET A 1 15  ? 85.026  1.959   25.832  1.00 19.56 ? 17   MET A N   1 
ATOM   103  C  CA  . MET A 1 15  ? 85.741  1.925   27.109  1.00 21.46 ? 17   MET A CA  1 
ATOM   104  C  C   . MET A 1 15  ? 87.100  2.627   27.061  1.00 23.38 ? 17   MET A C   1 
ATOM   105  O  O   . MET A 1 15  ? 87.626  3.043   28.094  1.00 25.20 ? 17   MET A O   1 
ATOM   106  C  CB  . MET A 1 15  ? 85.908  0.482   27.596  1.00 20.51 ? 17   MET A CB  1 
ATOM   107  C  CG  . MET A 1 15  ? 84.613  -0.187  28.032  1.00 22.10 ? 17   MET A CG  1 
ATOM   108  S  SD  . MET A 1 15  ? 83.692  0.777   29.250  1.00 25.79 ? 17   MET A SD  1 
ATOM   109  C  CE  . MET A 1 15  ? 83.816  -0.278  30.692  1.00 20.29 ? 17   MET A CE  1 
ATOM   110  N  N   . HIS A 1 16  ? 87.672  2.736   25.867  1.00 24.03 ? 18   HIS A N   1 
ATOM   111  C  CA  . HIS A 1 16  ? 88.927  3.465   25.675  1.00 26.57 ? 18   HIS A CA  1 
ATOM   112  C  C   . HIS A 1 16  ? 90.123  2.800   26.356  1.00 24.00 ? 18   HIS A C   1 
ATOM   113  O  O   . HIS A 1 16  ? 91.018  3.489   26.843  1.00 24.90 ? 18   HIS A O   1 
ATOM   114  C  CB  . HIS A 1 16  ? 88.799  4.905   26.182  1.00 29.50 ? 18   HIS A CB  1 
ATOM   115  C  CG  . HIS A 1 16  ? 87.862  5.751   25.378  1.00 35.56 ? 18   HIS A CG  1 
ATOM   116  N  ND1 . HIS A 1 16  ? 86.983  6.642   25.956  1.00 40.33 ? 18   HIS A ND1 1 
ATOM   117  C  CD2 . HIS A 1 16  ? 87.664  5.840   24.041  1.00 41.03 ? 18   HIS A CD2 1 
ATOM   118  C  CE1 . HIS A 1 16  ? 86.284  7.244   25.010  1.00 41.91 ? 18   HIS A CE1 1 
ATOM   119  N  NE2 . HIS A 1 16  ? 86.676  6.774   23.839  1.00 43.00 ? 18   HIS A NE2 1 
ATOM   120  N  N   . LYS A 1 17  ? 90.138  1.471   26.402  1.00 20.28 ? 19   LYS A N   1 
ATOM   121  C  CA  . LYS A 1 17  ? 91.198  0.760   27.116  1.00 18.80 ? 19   LYS A CA  1 
ATOM   122  C  C   . LYS A 1 17  ? 91.787  -0.384  26.296  1.00 17.65 ? 19   LYS A C   1 
ATOM   123  O  O   . LYS A 1 17  ? 91.110  -0.961  25.443  1.00 16.46 ? 19   LYS A O   1 
ATOM   124  C  CB  . LYS A 1 17  ? 90.695  0.240   28.464  1.00 18.04 ? 19   LYS A CB  1 
ATOM   125  C  CG  . LYS A 1 17  ? 90.300  1.329   29.448  1.00 19.67 ? 19   LYS A CG  1 
ATOM   126  C  CD  . LYS A 1 17  ? 91.517  2.012   30.056  1.00 20.58 ? 19   LYS A CD  1 
ATOM   127  C  CE  . LYS A 1 17  ? 91.125  2.856   31.263  1.00 21.16 ? 19   LYS A CE  1 
ATOM   128  N  NZ  . LYS A 1 17  ? 92.240  3.725   31.737  1.00 21.56 ? 19   LYS A NZ  1 
ATOM   129  N  N   . GLN A 1 18  ? 93.039  -0.726  26.590  1.00 16.60 ? 20   GLN A N   1 
ATOM   130  C  CA  . GLN A 1 18  ? 93.744  -1.803  25.896  1.00 17.02 ? 20   GLN A CA  1 
ATOM   131  C  C   . GLN A 1 18  ? 93.081  -3.157  26.112  1.00 14.87 ? 20   GLN A C   1 
ATOM   132  O  O   . GLN A 1 18  ? 93.037  -3.988  25.203  1.00 13.56 ? 20   GLN A O   1 
ATOM   133  C  CB  . GLN A 1 18  ? 95.201  -1.878  26.365  1.00 18.93 ? 20   GLN A CB  1 
ATOM   134  C  CG  . GLN A 1 18  ? 96.142  -0.922  25.653  1.00 22.32 ? 20   GLN A CG  1 
ATOM   135  C  CD  . GLN A 1 18  ? 96.299  -1.251  24.182  1.00 23.66 ? 20   GLN A CD  1 
ATOM   136  O  OE1 . GLN A 1 18  ? 96.653  -2.374  23.818  1.00 30.49 ? 20   GLN A OE1 1 
ATOM   137  N  NE2 . GLN A 1 18  ? 96.024  -0.276  23.327  1.00 23.75 ? 20   GLN A NE2 1 
ATOM   138  N  N   . LYS A 1 19  ? 92.631  -3.398  27.339  1.00 13.76 ? 21   LYS A N   1 
ATOM   139  C  CA  . LYS A 1 19  ? 92.151  -4.716  27.738  1.00 13.22 ? 21   LYS A CA  1 
ATOM   140  C  C   . LYS A 1 19  ? 90.704  -4.646  28.223  1.00 12.62 ? 21   LYS A C   1 
ATOM   141  O  O   . LYS A 1 19  ? 90.303  -3.677  28.869  1.00 12.00 ? 21   LYS A O   1 
ATOM   142  C  CB  . LYS A 1 19  ? 93.037  -5.287  28.849  1.00 13.66 ? 21   LYS A CB  1 
ATOM   143  C  CG  . LYS A 1 19  ? 94.521  -5.303  28.522  1.00 13.64 ? 21   LYS A CG  1 
ATOM   144  C  CD  . LYS A 1 19  ? 94.824  -6.250  27.371  1.00 13.07 ? 21   LYS A CD  1 
ATOM   145  C  CE  . LYS A 1 19  ? 96.315  -6.292  27.077  1.00 13.94 ? 21   LYS A CE  1 
ATOM   146  N  NZ  . LYS A 1 19  ? 96.655  -7.394  26.137  1.00 15.34 ? 21   LYS A NZ  1 
ATOM   147  N  N   . GLN A 1 20  ? 89.931  -5.685  27.921  1.00 12.47 ? 22   GLN A N   1 
ATOM   148  C  CA  . GLN A 1 20  ? 88.601  -5.835  28.496  1.00 12.49 ? 22   GLN A CA  1 
ATOM   149  C  C   . GLN A 1 20  ? 88.355  -7.244  29.008  1.00 12.54 ? 22   GLN A C   1 
ATOM   150  O  O   . GLN A 1 20  ? 88.820  -8.224  28.423  1.00 12.69 ? 22   GLN A O   1 
ATOM   151  C  CB  . GLN A 1 20  ? 87.519  -5.455  27.481  1.00 13.16 ? 22   GLN A CB  1 
ATOM   152  C  CG  . GLN A 1 20  ? 87.250  -3.963  27.419  1.00 13.39 ? 22   GLN A CG  1 
ATOM   153  C  CD  . GLN A 1 20  ? 86.167  -3.595  26.426  1.00 12.63 ? 22   GLN A CD  1 
ATOM   154  O  OE1 . GLN A 1 20  ? 85.112  -4.237  26.358  1.00 13.01 ? 22   GLN A OE1 1 
ATOM   155  N  NE2 . GLN A 1 20  ? 86.408  -2.538  25.671  1.00 12.75 ? 22   GLN A NE2 1 
ATOM   156  N  N   . LEU A 1 21  ? 87.634  -7.330  30.120  1.00 11.30 ? 23   LEU A N   1 
ATOM   157  C  CA  . LEU A 1 21  ? 87.099  -8.593  30.597  1.00 11.15 ? 23   LEU A CA  1 
ATOM   158  C  C   . LEU A 1 21  ? 85.580  -8.520  30.632  1.00 11.48 ? 23   LEU A C   1 
ATOM   159  O  O   . LEU A 1 21  ? 85.004  -7.583  31.190  1.00 10.82 ? 23   LEU A O   1 
ATOM   160  C  CB  . LEU A 1 21  ? 87.638  -8.908  31.997  1.00 11.22 ? 23   LEU A CB  1 
ATOM   161  C  CG  . LEU A 1 21  ? 87.129  -10.206 32.623  1.00 11.20 ? 23   LEU A CG  1 
ATOM   162  C  CD1 . LEU A 1 21  ? 87.736  -11.407 31.910  1.00 11.29 ? 23   LEU A CD1 1 
ATOM   163  C  CD2 . LEU A 1 21  ? 87.447  -10.241 34.113  1.00 11.49 ? 23   LEU A CD2 1 
ATOM   164  N  N   . PHE A 1 22  ? 84.935  -9.501  30.012  1.00 10.87 ? 24   PHE A N   1 
ATOM   165  C  CA  . PHE A 1 22  ? 83.511  -9.708  30.193  1.00 10.00 ? 24   PHE A CA  1 
ATOM   166  C  C   . PHE A 1 22  ? 83.279  -10.791 31.241  1.00 10.44 ? 24   PHE A C   1 
ATOM   167  O  O   . PHE A 1 22  ? 83.587  -11.965 31.020  1.00 10.22 ? 24   PHE A O   1 
ATOM   168  C  CB  . PHE A 1 22  ? 82.846  -10.091 28.871  1.00 9.37  ? 24   PHE A CB  1 
ATOM   169  C  CG  . PHE A 1 22  ? 83.016  -9.063  27.787  1.00 10.45 ? 24   PHE A CG  1 
ATOM   170  C  CD1 . PHE A 1 22  ? 84.125  -9.090  26.957  1.00 10.20 ? 24   PHE A CD1 1 
ATOM   171  C  CD2 . PHE A 1 22  ? 82.059  -8.075  27.589  1.00 9.87  ? 24   PHE A CD2 1 
ATOM   172  C  CE1 . PHE A 1 22  ? 84.284  -8.149  25.955  1.00 10.22 ? 24   PHE A CE1 1 
ATOM   173  C  CE2 . PHE A 1 22  ? 82.206  -7.141  26.582  1.00 9.47  ? 24   PHE A CE2 1 
ATOM   174  C  CZ  . PHE A 1 22  ? 83.321  -7.176  25.763  1.00 9.95  ? 24   PHE A CZ  1 
ATOM   175  N  N   . TYR A 1 23  ? 82.773  -10.371 32.394  1.00 10.04 ? 25   TYR A N   1 
ATOM   176  C  CA  . TYR A 1 23  ? 82.627  -11.236 33.561  1.00 10.93 ? 25   TYR A CA  1 
ATOM   177  C  C   . TYR A 1 23  ? 81.141  -11.548 33.734  1.00 10.61 ? 25   TYR A C   1 
ATOM   178  O  O   . TYR A 1 23  ? 80.361  -10.681 34.114  1.00 10.44 ? 25   TYR A O   1 
ATOM   179  C  CB  . TYR A 1 23  ? 83.167  -10.495 34.791  1.00 11.27 ? 25   TYR A CB  1 
ATOM   180  C  CG  . TYR A 1 23  ? 83.146  -11.255 36.103  1.00 12.82 ? 25   TYR A CG  1 
ATOM   181  C  CD1 . TYR A 1 23  ? 82.012  -11.261 36.907  1.00 13.32 ? 25   TYR A CD1 1 
ATOM   182  C  CD2 . TYR A 1 23  ? 84.305  -11.840 36.607  1.00 13.33 ? 25   TYR A CD2 1 
ATOM   183  C  CE1 . TYR A 1 23  ? 82.016  -11.879 38.148  1.00 13.98 ? 25   TYR A CE1 1 
ATOM   184  C  CE2 . TYR A 1 23  ? 84.315  -12.469 37.840  1.00 13.85 ? 25   TYR A CE2 1 
ATOM   185  C  CZ  . TYR A 1 23  ? 83.167  -12.494 38.603  1.00 14.70 ? 25   TYR A CZ  1 
ATOM   186  O  OH  . TYR A 1 23  ? 83.178  -13.100 39.844  1.00 14.47 ? 25   TYR A OH  1 
ATOM   187  N  N   . PHE A 1 24  ? 80.740  -12.759 33.360  1.00 10.73 ? 26   PHE A N   1 
ATOM   188  C  CA  . PHE A 1 24  ? 79.332  -13.139 33.398  1.00 10.59 ? 26   PHE A CA  1 
ATOM   189  C  C   . PHE A 1 24  ? 79.010  -13.835 34.715  1.00 11.26 ? 26   PHE A C   1 
ATOM   190  O  O   . PHE A 1 24  ? 79.657  -14.817 35.084  1.00 10.99 ? 26   PHE A O   1 
ATOM   191  C  CB  . PHE A 1 24  ? 78.985  -14.056 32.226  1.00 10.38 ? 26   PHE A CB  1 
ATOM   192  C  CG  . PHE A 1 24  ? 79.294  -13.464 30.879  1.00 10.36 ? 26   PHE A CG  1 
ATOM   193  C  CD1 . PHE A 1 24  ? 78.392  -12.616 30.258  1.00 9.94  ? 26   PHE A CD1 1 
ATOM   194  C  CD2 . PHE A 1 24  ? 80.480  -13.767 30.230  1.00 10.50 ? 26   PHE A CD2 1 
ATOM   195  C  CE1 . PHE A 1 24  ? 78.665  -12.080 29.015  1.00 9.88  ? 26   PHE A CE1 1 
ATOM   196  C  CE2 . PHE A 1 24  ? 80.757  -13.240 28.983  1.00 10.01 ? 26   PHE A CE2 1 
ATOM   197  C  CZ  . PHE A 1 24  ? 79.848  -12.394 28.375  1.00 10.44 ? 26   PHE A CZ  1 
ATOM   198  N  N   . PHE A 1 25  ? 78.003  -13.324 35.414  1.00 11.48 ? 27   PHE A N   1 
ATOM   199  C  CA  . PHE A 1 25  ? 77.756  -13.731 36.788  1.00 11.85 ? 27   PHE A CA  1 
ATOM   200  C  C   . PHE A 1 25  ? 76.329  -14.208 37.025  1.00 11.91 ? 27   PHE A C   1 
ATOM   201  O  O   . PHE A 1 25  ? 75.420  -13.911 36.250  1.00 10.67 ? 27   PHE A O   1 
ATOM   202  C  CB  . PHE A 1 25  ? 78.101  -12.595 37.759  1.00 11.69 ? 27   PHE A CB  1 
ATOM   203  C  CG  . PHE A 1 25  ? 77.230  -11.377 37.608  1.00 11.51 ? 27   PHE A CG  1 
ATOM   204  C  CD1 . PHE A 1 25  ? 76.024  -11.280 38.284  1.00 11.79 ? 27   PHE A CD1 1 
ATOM   205  C  CD2 . PHE A 1 25  ? 77.641  -10.307 36.822  1.00 11.70 ? 27   PHE A CD2 1 
ATOM   206  C  CE1 . PHE A 1 25  ? 75.231  -10.150 38.164  1.00 11.55 ? 27   PHE A CE1 1 
ATOM   207  C  CE2 . PHE A 1 25  ? 76.858  -9.175  36.698  1.00 11.43 ? 27   PHE A CE2 1 
ATOM   208  C  CZ  . PHE A 1 25  ? 75.648  -9.097  37.369  1.00 12.21 ? 27   PHE A CZ  1 
ATOM   209  N  N   . ALA A 1 26  ? 76.142  -14.940 38.118  1.00 12.87 ? 28   ALA A N   1 
ATOM   210  C  CA  . ALA A 1 26  ? 74.813  -15.182 38.659  1.00 12.96 ? 28   ALA A CA  1 
ATOM   211  C  C   . ALA A 1 26  ? 74.670  -14.485 40.008  1.00 13.49 ? 28   ALA A C   1 
ATOM   212  O  O   . ALA A 1 26  ? 75.660  -14.240 40.702  1.00 12.15 ? 28   ALA A O   1 
ATOM   213  C  CB  . ALA A 1 26  ? 74.560  -16.676 38.800  1.00 13.18 ? 28   ALA A CB  1 
ATOM   214  N  N   . ILE A 1 27  ? 73.438  -14.126 40.352  1.00 14.41 ? 29   ILE A N   1 
ATOM   215  C  CA  . ILE A 1 27  ? 73.148  -13.544 41.656  1.00 15.58 ? 29   ILE A CA  1 
ATOM   216  C  C   . ILE A 1 27  ? 72.652  -14.635 42.600  1.00 16.93 ? 29   ILE A C   1 
ATOM   217  O  O   . ILE A 1 27  ? 71.667  -15.312 42.314  1.00 17.78 ? 29   ILE A O   1 
ATOM   218  C  CB  . ILE A 1 27  ? 72.083  -12.435 41.552  1.00 15.41 ? 29   ILE A CB  1 
ATOM   219  C  CG1 . ILE A 1 27  ? 72.558  -11.327 40.609  1.00 15.08 ? 29   ILE A CG1 1 
ATOM   220  C  CG2 . ILE A 1 27  ? 71.773  -11.868 42.930  1.00 15.82 ? 29   ILE A CG2 1 
ATOM   221  C  CD1 . ILE A 1 27  ? 71.436  -10.502 40.014  1.00 16.05 ? 29   ILE A CD1 1 
ATOM   222  N  N   . ASN A 1 28  ? 73.376  -14.851 43.692  1.00 19.25 ? 30   ASN A N   1 
ATOM   223  C  CA  . ASN A 1 28  ? 73.033  -15.925 44.616  1.00 22.21 ? 30   ASN A CA  1 
ATOM   224  C  C   . ASN A 1 28  ? 72.151  -15.425 45.753  1.00 23.18 ? 30   ASN A C   1 
ATOM   225  O  O   . ASN A 1 28  ? 71.211  -16.102 46.174  1.00 25.09 ? 30   ASN A O   1 
ATOM   226  C  CB  . ASN A 1 28  ? 74.300  -16.570 45.180  1.00 23.02 ? 30   ASN A CB  1 
ATOM   227  C  CG  . ASN A 1 28  ? 75.136  -17.245 44.111  1.00 22.84 ? 30   ASN A CG  1 
ATOM   228  O  OD1 . ASN A 1 28  ? 74.604  -17.840 43.174  1.00 25.34 ? 30   ASN A OD1 1 
ATOM   229  N  ND2 . ASN A 1 28  ? 76.453  -17.154 44.246  1.00 23.99 ? 30   ASN A ND2 1 
ATOM   230  N  N   . ASP A 1 29  ? 72.466  -14.232 46.244  1.00 22.14 ? 31   ASP A N   1 
ATOM   231  C  CA  . ASP A 1 29  ? 71.765  -13.649 47.379  1.00 22.25 ? 31   ASP A CA  1 
ATOM   232  C  C   . ASP A 1 29  ? 71.407  -12.200 47.049  1.00 20.22 ? 31   ASP A C   1 
ATOM   233  O  O   . ASP A 1 29  ? 72.250  -11.312 47.154  1.00 18.26 ? 31   ASP A O   1 
ATOM   234  C  CB  . ASP A 1 29  ? 72.654  -13.715 48.623  1.00 23.45 ? 31   ASP A CB  1 
ATOM   235  C  CG  . ASP A 1 29  ? 71.985  -13.143 49.858  1.00 26.86 ? 31   ASP A CG  1 
ATOM   236  O  OD1 . ASP A 1 29  ? 70.815  -12.716 49.771  1.00 28.02 ? 31   ASP A OD1 1 
ATOM   237  O  OD2 . ASP A 1 29  ? 72.640  -13.114 50.920  1.00 29.96 ? 31   ASP A OD2 1 
ATOM   238  N  N   . PRO A 1 30  ? 70.169  -11.976 46.584  1.00 19.97 ? 32   PRO A N   1 
ATOM   239  C  CA  . PRO A 1 30  ? 69.707  -10.671 46.115  1.00 18.55 ? 32   PRO A CA  1 
ATOM   240  C  C   . PRO A 1 30  ? 69.988  -9.559  47.118  1.00 17.28 ? 32   PRO A C   1 
ATOM   241  O  O   . PRO A 1 30  ? 70.494  -8.501  46.745  1.00 16.21 ? 32   PRO A O   1 
ATOM   242  C  CB  . PRO A 1 30  ? 68.198  -10.866 45.975  1.00 19.05 ? 32   PRO A CB  1 
ATOM   243  C  CG  . PRO A 1 30  ? 68.031  -12.314 45.694  1.00 21.43 ? 32   PRO A CG  1 
ATOM   244  C  CD  . PRO A 1 30  ? 69.158  -13.030 46.386  1.00 19.64 ? 32   PRO A CD  1 
ATOM   245  N  N   . ALA A 1 31  ? 69.642  -9.793  48.379  1.00 17.40 ? 33   ALA A N   1 
ATOM   246  C  CA  . ALA A 1 31  ? 69.714  -8.753  49.397  1.00 16.87 ? 33   ALA A CA  1 
ATOM   247  C  C   . ALA A 1 31  ? 71.145  -8.266  49.580  1.00 15.96 ? 33   ALA A C   1 
ATOM   248  O  O   . ALA A 1 31  ? 71.407  -7.064  49.586  1.00 16.03 ? 33   ALA A O   1 
ATOM   249  C  CB  . ALA A 1 31  ? 69.153  -9.260  50.717  1.00 17.24 ? 33   ALA A CB  1 
ATOM   250  N  N   . THR A 1 32  ? 72.068  -9.209  49.733  1.00 15.64 ? 34   THR A N   1 
ATOM   251  C  CA  . THR A 1 32  ? 73.475  -8.883  49.906  1.00 15.12 ? 34   THR A CA  1 
ATOM   252  C  C   . THR A 1 32  ? 74.047  -8.296  48.622  1.00 14.27 ? 34   THR A C   1 
ATOM   253  O  O   . THR A 1 32  ? 74.813  -7.330  48.655  1.00 13.56 ? 34   THR A O   1 
ATOM   254  C  CB  . THR A 1 32  ? 74.287  -10.126 50.316  1.00 15.93 ? 34   THR A CB  1 
ATOM   255  O  OG1 . THR A 1 32  ? 73.911  -10.526 51.639  1.00 15.70 ? 34   THR A OG1 1 
ATOM   256  C  CG2 . THR A 1 32  ? 75.777  -9.828  50.287  1.00 15.26 ? 34   THR A CG2 1 
ATOM   257  N  N   . PHE A 1 33  ? 73.657  -8.873  47.489  1.00 14.18 ? 35   PHE A N   1 
ATOM   258  C  CA  . PHE A 1 33  ? 74.082  -8.365  46.188  1.00 13.96 ? 35   PHE A CA  1 
ATOM   259  C  C   . PHE A 1 33  ? 73.713  -6.890  46.045  1.00 14.11 ? 35   PHE A C   1 
ATOM   260  O  O   . PHE A 1 33  ? 74.542  -6.065  45.654  1.00 13.36 ? 35   PHE A O   1 
ATOM   261  C  CB  . PHE A 1 33  ? 73.442  -9.182  45.064  1.00 14.36 ? 35   PHE A CB  1 
ATOM   262  C  CG  . PHE A 1 33  ? 73.958  -8.845  43.693  1.00 14.08 ? 35   PHE A CG  1 
ATOM   263  C  CD1 . PHE A 1 33  ? 73.377  -7.830  42.949  1.00 14.70 ? 35   PHE A CD1 1 
ATOM   264  C  CD2 . PHE A 1 33  ? 75.010  -9.558  43.139  1.00 14.68 ? 35   PHE A CD2 1 
ATOM   265  C  CE1 . PHE A 1 33  ? 73.846  -7.517  41.688  1.00 14.79 ? 35   PHE A CE1 1 
ATOM   266  C  CE2 . PHE A 1 33  ? 75.487  -9.250  41.877  1.00 15.58 ? 35   PHE A CE2 1 
ATOM   267  C  CZ  . PHE A 1 33  ? 74.901  -8.230  41.148  1.00 15.69 ? 35   PHE A CZ  1 
ATOM   268  N  N   . LYS A 1 34  ? 72.469  -6.564  46.388  1.00 14.10 ? 36   LYS A N   1 
ATOM   269  C  CA  . LYS A 1 34  ? 71.963  -5.203  46.250  1.00 14.20 ? 36   LYS A CA  1 
ATOM   270  C  C   . LYS A 1 34  ? 72.765  -4.229  47.108  1.00 14.74 ? 36   LYS A C   1 
ATOM   271  O  O   . LYS A 1 34  ? 73.115  -3.136  46.661  1.00 14.00 ? 36   LYS A O   1 
ATOM   272  C  CB  . LYS A 1 34  ? 70.484  -5.144  46.639  1.00 15.48 ? 36   LYS A CB  1 
ATOM   273  C  CG  . LYS A 1 34  ? 69.533  -5.650  45.567  1.00 16.45 ? 36   LYS A CG  1 
ATOM   274  C  CD  . LYS A 1 34  ? 68.130  -5.819  46.132  1.00 18.21 ? 36   LYS A CD  1 
ATOM   275  C  CE  . LYS A 1 34  ? 67.125  -6.185  45.054  1.00 19.20 ? 36   LYS A CE  1 
ATOM   276  N  NZ  . LYS A 1 34  ? 66.742  -5.005  44.230  1.00 18.95 ? 36   LYS A NZ  1 
ATOM   277  N  N   . THR A 1 35  ? 73.047  -4.626  48.345  1.00 14.85 ? 37   THR A N   1 
ATOM   278  C  CA  . THR A 1 35  ? 73.813  -3.785  49.257  1.00 15.82 ? 37   THR A CA  1 
ATOM   279  C  C   . THR A 1 35  ? 75.122  -3.356  48.612  1.00 14.84 ? 37   THR A C   1 
ATOM   280  O  O   . THR A 1 35  ? 75.497  -2.186  48.655  1.00 15.49 ? 37   THR A O   1 
ATOM   281  C  CB  . THR A 1 35  ? 74.126  -4.519  50.575  1.00 17.98 ? 37   THR A CB  1 
ATOM   282  O  OG1 . THR A 1 35  ? 72.906  -4.801  51.269  1.00 18.77 ? 37   THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 35  ? 75.026  -3.666  51.459  1.00 17.53 ? 37   THR A CG2 1 
ATOM   284  N  N   . HIS A 1 36  ? 75.803  -4.309  47.986  1.00 14.99 ? 38   HIS A N   1 
ATOM   285  C  CA  . HIS A 1 36  ? 77.117  -4.055  47.418  1.00 15.18 ? 38   HIS A CA  1 
ATOM   286  C  C   . HIS A 1 36  ? 77.041  -3.448  46.023  1.00 14.76 ? 38   HIS A C   1 
ATOM   287  O  O   . HIS A 1 36  ? 77.922  -2.688  45.621  1.00 15.42 ? 38   HIS A O   1 
ATOM   288  C  CB  . HIS A 1 36  ? 77.946  -5.337  47.413  1.00 15.62 ? 38   HIS A CB  1 
ATOM   289  C  CG  . HIS A 1 36  ? 78.365  -5.777  48.780  1.00 16.45 ? 38   HIS A CG  1 
ATOM   290  N  ND1 . HIS A 1 36  ? 79.262  -5.065  49.545  1.00 17.00 ? 38   HIS A ND1 1 
ATOM   291  C  CD2 . HIS A 1 36  ? 77.949  -6.809  49.550  1.00 16.74 ? 38   HIS A CD2 1 
ATOM   292  C  CE1 . HIS A 1 36  ? 79.410  -5.660  50.715  1.00 18.50 ? 38   HIS A CE1 1 
ATOM   293  N  NE2 . HIS A 1 36  ? 78.628  -6.724  50.742  1.00 16.82 ? 38   HIS A NE2 1 
ATOM   294  N  N   . LEU A 1 37  ? 75.977  -3.769  45.294  1.00 14.13 ? 39   LEU A N   1 
ATOM   295  C  CA  . LEU A 1 37  ? 75.710  -3.110  44.022  1.00 13.82 ? 39   LEU A CA  1 
ATOM   296  C  C   . LEU A 1 37  ? 75.648  -1.598  44.222  1.00 14.21 ? 39   LEU A C   1 
ATOM   297  O  O   . LEU A 1 37  ? 76.222  -0.834  43.446  1.00 13.87 ? 39   LEU A O   1 
ATOM   298  C  CB  . LEU A 1 37  ? 74.405  -3.622  43.415  1.00 14.11 ? 39   LEU A CB  1 
ATOM   299  C  CG  . LEU A 1 37  ? 74.044  -3.101  42.022  1.00 14.44 ? 39   LEU A CG  1 
ATOM   300  C  CD1 . LEU A 1 37  ? 75.100  -3.516  41.006  1.00 14.66 ? 39   LEU A CD1 1 
ATOM   301  C  CD2 . LEU A 1 37  ? 72.668  -3.598  41.606  1.00 13.65 ? 39   LEU A CD2 1 
ATOM   302  N  N   . ALA A 1 38  ? 74.994  -1.176  45.300  1.00 13.72 ? 40   ALA A N   1 
ATOM   303  C  CA  . ALA A 1 38  ? 74.841  0.243   45.587  1.00 15.60 ? 40   ALA A CA  1 
ATOM   304  C  C   . ALA A 1 38  ? 76.129  0.869   46.128  1.00 16.83 ? 40   ALA A C   1 
ATOM   305  O  O   . ALA A 1 38  ? 76.488  1.986   45.757  1.00 18.12 ? 40   ALA A O   1 
ATOM   306  C  CB  . ALA A 1 38  ? 73.687  0.469   46.553  1.00 15.83 ? 40   ALA A CB  1 
ATOM   307  N  N   A SER A 1 39  ? 76.822  0.141   46.998  0.50 17.53 ? 41   SER A N   1 
ATOM   308  N  N   B SER A 1 39  ? 76.826  0.134   46.990  0.50 17.38 ? 41   SER A N   1 
ATOM   309  C  CA  A SER A 1 39  ? 77.956  0.700   47.727  0.50 18.05 ? 41   SER A CA  1 
ATOM   310  C  CA  B SER A 1 39  ? 77.953  0.690   47.732  0.50 17.84 ? 41   SER A CA  1 
ATOM   311  C  C   A SER A 1 39  ? 79.258  0.602   46.939  0.50 18.35 ? 41   SER A C   1 
ATOM   312  C  C   B SER A 1 39  ? 79.260  0.594   46.952  0.50 18.23 ? 41   SER A C   1 
ATOM   313  O  O   A SER A 1 39  ? 80.086  1.510   46.981  0.50 18.93 ? 41   SER A O   1 
ATOM   314  O  O   B SER A 1 39  ? 80.093  1.497   47.010  0.50 18.83 ? 41   SER A O   1 
ATOM   315  C  CB  A SER A 1 39  ? 78.114  0.013   49.086  0.50 19.45 ? 41   SER A CB  1 
ATOM   316  C  CB  B SER A 1 39  ? 78.101  -0.010  49.086  0.50 18.95 ? 41   SER A CB  1 
ATOM   317  O  OG  A SER A 1 39  ? 77.010  0.288   49.929  0.50 19.69 ? 41   SER A OG  1 
ATOM   318  O  OG  B SER A 1 39  ? 78.591  -1.331  48.926  0.50 19.10 ? 41   SER A OG  1 
ATOM   319  N  N   . ASP A 1 40  ? 79.445  -0.513  46.241  1.00 18.38 ? 42   ASP A N   1 
ATOM   320  C  CA  . ASP A 1 40  ? 80.734  -0.825  45.639  1.00 19.54 ? 42   ASP A CA  1 
ATOM   321  C  C   . ASP A 1 40  ? 80.760  -0.596  44.133  1.00 19.28 ? 42   ASP A C   1 
ATOM   322  O  O   . ASP A 1 40  ? 81.780  -0.189  43.580  1.00 20.06 ? 42   ASP A O   1 
ATOM   323  C  CB  . ASP A 1 40  ? 81.142  -2.263  45.956  1.00 21.22 ? 42   ASP A CB  1 
ATOM   324  C  CG  . ASP A 1 40  ? 81.385  -2.485  47.436  1.00 24.67 ? 42   ASP A CG  1 
ATOM   325  O  OD1 . ASP A 1 40  ? 81.807  -1.530  48.122  1.00 26.15 ? 42   ASP A OD1 1 
ATOM   326  O  OD2 . ASP A 1 40  ? 81.159  -3.617  47.910  1.00 27.18 ? 42   ASP A OD2 1 
ATOM   327  N  N   . ILE A 1 41  ? 79.645  -0.874  43.469  1.00 17.20 ? 43   ILE A N   1 
ATOM   328  C  CA  . ILE A 1 41  ? 79.616  -0.827  42.014  1.00 16.15 ? 43   ILE A CA  1 
ATOM   329  C  C   . ILE A 1 41  ? 79.141  0.530   41.502  1.00 15.17 ? 43   ILE A C   1 
ATOM   330  O  O   . ILE A 1 41  ? 79.844  1.193   40.744  1.00 15.32 ? 43   ILE A O   1 
ATOM   331  C  CB  . ILE A 1 41  ? 78.745  -1.951  41.423  1.00 16.02 ? 43   ILE A CB  1 
ATOM   332  C  CG1 . ILE A 1 41  ? 79.296  -3.324  41.824  1.00 16.94 ? 43   ILE A CG1 1 
ATOM   333  C  CG2 . ILE A 1 41  ? 78.667  -1.822  39.910  1.00 15.51 ? 43   ILE A CG2 1 
ATOM   334  C  CD1 . ILE A 1 41  ? 80.653  -3.649  41.235  1.00 17.44 ? 43   ILE A CD1 1 
ATOM   335  N  N   . ALA A 1 42  ? 77.971  0.959   41.961  1.00 15.28 ? 44   ALA A N   1 
ATOM   336  C  CA  . ALA A 1 42  ? 77.347  2.180   41.457  1.00 16.47 ? 44   ALA A CA  1 
ATOM   337  C  C   . ALA A 1 42  ? 78.308  3.367   41.392  1.00 16.19 ? 44   ALA A C   1 
ATOM   338  O  O   . ALA A 1 42  ? 78.376  4.051   40.373  1.00 15.61 ? 44   ALA A O   1 
ATOM   339  C  CB  . ALA A 1 42  ? 76.114  2.531   42.275  1.00 16.96 ? 44   ALA A CB  1 
ATOM   340  N  N   . PRO A 1 43  ? 79.048  3.622   42.484  1.00 16.69 ? 45   PRO A N   1 
ATOM   341  C  CA  . PRO A 1 43  ? 79.906  4.804   42.539  1.00 18.13 ? 45   PRO A CA  1 
ATOM   342  C  C   . PRO A 1 43  ? 81.048  4.783   41.529  1.00 17.21 ? 45   PRO A C   1 
ATOM   343  O  O   . PRO A 1 43  ? 81.647  5.822   41.266  1.00 20.73 ? 45   PRO A O   1 
ATOM   344  C  CB  . PRO A 1 43  ? 80.468  4.765   43.965  1.00 18.33 ? 45   PRO A CB  1 
ATOM   345  C  CG  . PRO A 1 43  ? 79.453  4.004   44.746  1.00 17.75 ? 45   PRO A CG  1 
ATOM   346  C  CD  . PRO A 1 43  ? 78.928  2.965   43.796  1.00 17.10 ? 45   PRO A CD  1 
ATOM   347  N  N   . VAL A 1 44  ? 81.376  3.612   40.991  1.00 17.14 ? 46   VAL A N   1 
ATOM   348  C  CA  . VAL A 1 44  ? 82.540  3.493   40.111  1.00 16.36 ? 46   VAL A CA  1 
ATOM   349  C  C   . VAL A 1 44  ? 82.177  3.102   38.684  1.00 15.74 ? 46   VAL A C   1 
ATOM   350  O  O   . VAL A 1 44  ? 83.045  2.730   37.895  1.00 16.22 ? 46   VAL A O   1 
ATOM   351  C  CB  . VAL A 1 44  ? 83.587  2.502   40.656  1.00 16.73 ? 46   VAL A CB  1 
ATOM   352  C  CG1 . VAL A 1 44  ? 84.158  2.997   41.978  1.00 17.16 ? 46   VAL A CG1 1 
ATOM   353  C  CG2 . VAL A 1 44  ? 82.990  1.112   40.803  1.00 16.69 ? 46   VAL A CG2 1 
ATOM   354  N  N   . VAL A 1 45  ? 80.890  3.157   38.361  1.00 14.88 ? 47   VAL A N   1 
ATOM   355  C  CA  . VAL A 1 45  ? 80.449  2.922   36.988  1.00 13.97 ? 47   VAL A CA  1 
ATOM   356  C  C   . VAL A 1 45  ? 80.782  4.134   36.129  1.00 14.05 ? 47   VAL A C   1 
ATOM   357  O  O   . VAL A 1 45  ? 80.374  5.254   36.439  1.00 14.83 ? 47   VAL A O   1 
ATOM   358  C  CB  . VAL A 1 45  ? 78.934  2.651   36.913  1.00 13.50 ? 47   VAL A CB  1 
ATOM   359  C  CG1 . VAL A 1 45  ? 78.488  2.511   35.463  1.00 12.61 ? 47   VAL A CG1 1 
ATOM   360  C  CG2 . VAL A 1 45  ? 78.582  1.407   37.713  1.00 14.36 ? 47   VAL A CG2 1 
ATOM   361  N  N   . ALA A 1 46  ? 81.519  3.907   35.047  1.00 12.97 ? 48   ALA A N   1 
ATOM   362  C  CA  . ALA A 1 46  ? 82.031  5.001   34.229  1.00 13.17 ? 48   ALA A CA  1 
ATOM   363  C  C   . ALA A 1 46  ? 80.972  5.520   33.262  1.00 12.67 ? 48   ALA A C   1 
ATOM   364  O  O   . ALA A 1 46  ? 80.358  4.747   32.524  1.00 11.51 ? 48   ALA A O   1 
ATOM   365  C  CB  . ALA A 1 46  ? 83.273  4.560   33.468  1.00 12.38 ? 48   ALA A CB  1 
ATOM   366  N  N   . SER A 1 47  ? 80.775  6.834   33.263  1.00 12.57 ? 49   SER A N   1 
ATOM   367  C  CA  . SER A 1 47  ? 79.751  7.460   32.436  1.00 12.51 ? 49   SER A CA  1 
ATOM   368  C  C   . SER A 1 47  ? 80.340  7.901   31.107  1.00 12.92 ? 49   SER A C   1 
ATOM   369  O  O   . SER A 1 47  ? 81.558  7.927   30.935  1.00 13.86 ? 49   SER A O   1 
ATOM   370  C  CB  . SER A 1 47  ? 79.151  8.669   33.154  1.00 12.71 ? 49   SER A CB  1 
ATOM   371  O  OG  . SER A 1 47  ? 80.114  9.699   33.282  1.00 13.76 ? 49   SER A OG  1 
ATOM   372  N  N   . VAL A 1 48  ? 79.470  8.261   30.172  1.00 12.84 ? 50   VAL A N   1 
ATOM   373  C  CA  . VAL A 1 48  ? 79.910  8.858   28.920  1.00 13.48 ? 50   VAL A CA  1 
ATOM   374  C  C   . VAL A 1 48  ? 80.687  10.145  29.184  1.00 14.00 ? 50   VAL A C   1 
ATOM   375  O  O   . VAL A 1 48  ? 81.773  10.353  28.638  1.00 14.36 ? 50   VAL A O   1 
ATOM   376  C  CB  . VAL A 1 48  ? 78.720  9.141   27.986  1.00 13.92 ? 50   VAL A CB  1 
ATOM   377  C  CG1 . VAL A 1 48  ? 79.161  9.980   26.799  1.00 13.22 ? 50   VAL A CG1 1 
ATOM   378  C  CG2 . VAL A 1 48  ? 78.091  7.834   27.521  1.00 13.27 ? 50   VAL A CG2 1 
ATOM   379  N  N   . THR A 1 49  ? 80.153  10.989  30.058  1.00 14.47 ? 51   THR A N   1 
ATOM   380  C  CA  . THR A 1 49  ? 80.855  12.206  30.449  1.00 15.80 ? 51   THR A CA  1 
ATOM   381  C  C   . THR A 1 49  ? 82.280  11.879  30.891  1.00 16.21 ? 51   THR A C   1 
ATOM   382  O  O   . THR A 1 49  ? 83.248  12.490  30.433  1.00 15.94 ? 51   THR A O   1 
ATOM   383  C  CB  . THR A 1 49  ? 80.130  12.935  31.596  1.00 16.55 ? 51   THR A CB  1 
ATOM   384  O  OG1 . THR A 1 49  ? 78.786  13.237  31.199  1.00 18.34 ? 51   THR A OG1 1 
ATOM   385  C  CG2 . THR A 1 49  ? 80.854  14.229  31.948  1.00 17.24 ? 51   THR A CG2 1 
ATOM   386  N  N   . GLN A 1 50  ? 82.396  10.905  31.785  1.00 16.22 ? 52   GLN A N   1 
ATOM   387  C  CA  . GLN A 1 50  ? 83.665  10.578  32.415  1.00 17.55 ? 52   GLN A CA  1 
ATOM   388  C  C   . GLN A 1 50  ? 84.691  10.113  31.385  1.00 17.99 ? 52   GLN A C   1 
ATOM   389  O  O   . GLN A 1 50  ? 85.842  10.559  31.395  1.00 16.96 ? 52   GLN A O   1 
ATOM   390  C  CB  . GLN A 1 50  ? 83.448  9.492   33.462  1.00 19.96 ? 52   GLN A CB  1 
ATOM   391  C  CG  . GLN A 1 50  ? 84.585  9.318   34.448  1.00 23.97 ? 52   GLN A CG  1 
ATOM   392  C  CD  . GLN A 1 50  ? 84.292  8.221   35.448  1.00 29.19 ? 52   GLN A CD  1 
ATOM   393  O  OE1 . GLN A 1 50  ? 83.138  7.821   35.621  1.00 31.25 ? 52   GLN A OE1 1 
ATOM   394  N  NE2 . GLN A 1 50  ? 85.332  7.717   36.102  1.00 31.12 ? 52   GLN A NE2 1 
ATOM   395  N  N   . LEU A 1 51  ? 84.258  9.234   30.483  1.00 16.93 ? 53   LEU A N   1 
ATOM   396  C  CA  . LEU A 1 51  ? 85.148  8.630   29.499  1.00 17.02 ? 53   LEU A CA  1 
ATOM   397  C  C   . LEU A 1 51  ? 85.450  9.571   28.337  1.00 17.82 ? 53   LEU A C   1 
ATOM   398  O  O   . LEU A 1 51  ? 86.390  9.345   27.579  1.00 19.03 ? 53   LEU A O   1 
ATOM   399  C  CB  . LEU A 1 51  ? 84.562  7.316   28.971  1.00 17.21 ? 53   LEU A CB  1 
ATOM   400  C  CG  . LEU A 1 51  ? 84.447  6.159   29.967  1.00 17.36 ? 53   LEU A CG  1 
ATOM   401  C  CD1 . LEU A 1 51  ? 84.031  4.871   29.269  1.00 17.15 ? 53   LEU A CD1 1 
ATOM   402  C  CD2 . LEU A 1 51  ? 85.755  5.959   30.716  1.00 18.93 ? 53   LEU A CD2 1 
ATOM   403  N  N   . SER A 1 52  ? 84.638  10.612  28.184  1.00 17.16 ? 54   SER A N   1 
ATOM   404  C  CA  . SER A 1 52  ? 84.830  11.572  27.098  1.00 19.23 ? 54   SER A CA  1 
ATOM   405  C  C   . SER A 1 52  ? 85.878  12.628  27.447  1.00 20.00 ? 54   SER A C   1 
ATOM   406  O  O   . SER A 1 52  ? 86.278  13.419  26.596  1.00 21.18 ? 54   SER A O   1 
ATOM   407  C  CB  . SER A 1 52  ? 83.507  12.250  26.738  1.00 18.33 ? 54   SER A CB  1 
ATOM   408  O  OG  . SER A 1 52  ? 82.552  11.300  26.302  1.00 19.17 ? 54   SER A OG  1 
ATOM   409  N  N   . ASN A 1 53  ? 86.310  12.641  28.703  1.00 20.45 ? 55   ASN A N   1 
ATOM   410  C  CA  . ASN A 1 53  ? 87.297  13.611  29.170  1.00 21.66 ? 55   ASN A CA  1 
ATOM   411  C  C   . ASN A 1 53  ? 88.658  12.949  29.382  1.00 20.72 ? 55   ASN A C   1 
ATOM   412  O  O   . ASN A 1 53  ? 88.794  12.057  30.218  1.00 22.13 ? 55   ASN A O   1 
ATOM   413  C  CB  . ASN A 1 53  ? 86.811  14.260  30.469  1.00 21.23 ? 55   ASN A CB  1 
ATOM   414  C  CG  . ASN A 1 53  ? 87.688  15.416  30.915  1.00 23.12 ? 55   ASN A CG  1 
ATOM   415  O  OD1 . ASN A 1 53  ? 88.895  15.428  30.674  1.00 22.75 ? 55   ASN A OD1 1 
ATOM   416  N  ND2 . ASN A 1 53  ? 87.086  16.381  31.602  1.00 23.08 ? 55   ASN A ND2 1 
ATOM   417  N  N   . VAL A 1 54  ? 89.659  13.384  28.622  1.00 20.92 ? 56   VAL A N   1 
ATOM   418  C  CA  . VAL A 1 54  ? 90.984  12.769  28.682  1.00 20.38 ? 56   VAL A CA  1 
ATOM   419  C  C   . VAL A 1 54  ? 91.606  12.893  30.069  1.00 19.81 ? 56   VAL A C   1 
ATOM   420  O  O   . VAL A 1 54  ? 92.488  12.118  30.434  1.00 21.86 ? 56   VAL A O   1 
ATOM   421  C  CB  . VAL A 1 54  ? 91.951  13.370  27.640  1.00 22.02 ? 56   VAL A CB  1 
ATOM   422  C  CG1 . VAL A 1 54  ? 91.481  13.056  26.227  1.00 21.93 ? 56   VAL A CG1 1 
ATOM   423  C  CG2 . VAL A 1 54  ? 92.094  14.870  27.846  1.00 20.71 ? 56   VAL A CG2 1 
ATOM   424  N  N   . ALA A 1 55  ? 91.128  13.854  30.851  1.00 19.01 ? 57   ALA A N   1 
ATOM   425  C  CA  . ALA A 1 55  ? 91.712  14.127  32.157  1.00 18.41 ? 57   ALA A CA  1 
ATOM   426  C  C   . ALA A 1 55  ? 91.040  13.335  33.275  1.00 18.15 ? 57   ALA A C   1 
ATOM   427  O  O   . ALA A 1 55  ? 91.473  13.399  34.423  1.00 18.80 ? 57   ALA A O   1 
ATOM   428  C  CB  . ALA A 1 55  ? 91.669  15.619  32.458  1.00 18.34 ? 57   ALA A CB  1 
ATOM   429  N  N   . THR A 1 56  ? 89.970  12.614  32.947  1.00 19.16 ? 58   THR A N   1 
ATOM   430  C  CA  . THR A 1 56  ? 89.196  11.892  33.960  1.00 19.38 ? 58   THR A CA  1 
ATOM   431  C  C   . THR A 1 56  ? 88.997  10.421  33.606  1.00 20.38 ? 58   THR A C   1 
ATOM   432  O  O   . THR A 1 56  ? 87.967  9.829   33.929  1.00 19.57 ? 58   THR A O   1 
ATOM   433  C  CB  . THR A 1 56  ? 87.814  12.537  34.210  1.00 20.48 ? 58   THR A CB  1 
ATOM   434  O  OG1 . THR A 1 56  ? 87.078  12.595  32.981  1.00 20.68 ? 58   THR A OG1 1 
ATOM   435  C  CG2 . THR A 1 56  ? 87.964  13.944  34.778  1.00 19.94 ? 58   THR A CG2 1 
ATOM   436  N  N   . GLN A 1 57  ? 89.992  9.828   32.955  1.00 21.51 ? 59   GLN A N   1 
ATOM   437  C  CA  . GLN A 1 57  ? 89.976  8.394   32.689  1.00 21.98 ? 59   GLN A CA  1 
ATOM   438  C  C   . GLN A 1 57  ? 90.189  7.622   33.982  1.00 19.62 ? 59   GLN A C   1 
ATOM   439  O  O   . GLN A 1 57  ? 91.185  7.827   34.669  1.00 21.70 ? 59   GLN A O   1 
ATOM   440  C  CB  . GLN A 1 57  ? 91.065  8.027   31.677  1.00 24.22 ? 59   GLN A CB  1 
ATOM   441  C  CG  . GLN A 1 57  ? 90.938  8.746   30.344  1.00 24.84 ? 59   GLN A CG  1 
ATOM   442  C  CD  . GLN A 1 57  ? 89.621  8.450   29.654  1.00 26.13 ? 59   GLN A CD  1 
ATOM   443  O  OE1 . GLN A 1 57  ? 88.817  9.351   29.408  1.00 25.11 ? 59   GLN A OE1 1 
ATOM   444  N  NE2 . GLN A 1 57  ? 89.386  7.179   29.352  1.00 27.73 ? 59   GLN A NE2 1 
ATOM   445  N  N   . PRO A 1 58  ? 89.255  6.721   34.318  1.00 19.00 ? 60   PRO A N   1 
ATOM   446  C  CA  . PRO A 1 58  ? 89.453  5.857   35.477  1.00 17.97 ? 60   PRO A CA  1 
ATOM   447  C  C   . PRO A 1 58  ? 90.567  4.844   35.228  1.00 16.94 ? 60   PRO A C   1 
ATOM   448  O  O   . PRO A 1 58  ? 90.806  4.455   34.087  1.00 15.58 ? 60   PRO A O   1 
ATOM   449  C  CB  . PRO A 1 58  ? 88.109  5.137   35.606  1.00 17.70 ? 60   PRO A CB  1 
ATOM   450  C  CG  . PRO A 1 58  ? 87.566  5.110   34.218  1.00 17.59 ? 60   PRO A CG  1 
ATOM   451  C  CD  . PRO A 1 58  ? 88.036  6.379   33.564  1.00 18.87 ? 60   PRO A CD  1 
ATOM   452  N  N   . LEU A 1 59  ? 91.231  4.420   36.297  1.00 16.23 ? 61   LEU A N   1 
ATOM   453  C  CA  . LEU A 1 59  ? 92.241  3.372   36.215  1.00 16.73 ? 61   LEU A CA  1 
ATOM   454  C  C   . LEU A 1 59  ? 91.630  2.100   35.633  1.00 15.32 ? 61   LEU A C   1 
ATOM   455  O  O   . LEU A 1 59  ? 92.188  1.481   34.725  1.00 15.39 ? 61   LEU A O   1 
ATOM   456  C  CB  . LEU A 1 59  ? 92.812  3.094   37.607  1.00 17.04 ? 61   LEU A CB  1 
ATOM   457  C  CG  . LEU A 1 59  ? 94.069  2.227   37.714  1.00 18.51 ? 61   LEU A CG  1 
ATOM   458  C  CD1 . LEU A 1 59  ? 95.155  2.722   36.772  1.00 18.81 ? 61   LEU A CD1 1 
ATOM   459  C  CD2 . LEU A 1 59  ? 94.572  2.221   39.150  1.00 19.15 ? 61   LEU A CD2 1 
ATOM   460  N  N   . VAL A 1 60  ? 90.471  1.724   36.158  1.00 14.63 ? 62   VAL A N   1 
ATOM   461  C  CA  . VAL A 1 60  ? 89.670  0.659   35.568  1.00 14.10 ? 62   VAL A CA  1 
ATOM   462  C  C   . VAL A 1 60  ? 88.271  1.183   35.259  1.00 13.55 ? 62   VAL A C   1 
ATOM   463  O  O   . VAL A 1 60  ? 87.575  1.669   36.148  1.00 13.11 ? 62   VAL A O   1 
ATOM   464  C  CB  . VAL A 1 60  ? 89.567  -0.554  36.512  1.00 13.87 ? 62   VAL A CB  1 
ATOM   465  C  CG1 . VAL A 1 60  ? 88.706  -1.644  35.887  1.00 13.77 ? 62   VAL A CG1 1 
ATOM   466  C  CG2 . VAL A 1 60  ? 90.956  -1.089  36.832  1.00 14.12 ? 62   VAL A CG2 1 
ATOM   467  N  N   . ALA A 1 61  ? 87.898  1.156   33.984  1.00 12.48 ? 63   ALA A N   1 
ATOM   468  C  CA  . ALA A 1 61  ? 86.545  1.509   33.577  1.00 12.11 ? 63   ALA A CA  1 
ATOM   469  C  C   . ALA A 1 61  ? 85.613  0.323   33.801  1.00 12.36 ? 63   ALA A C   1 
ATOM   470  O  O   . ALA A 1 61  ? 85.916  -0.801  33.393  1.00 12.99 ? 63   ALA A O   1 
ATOM   471  C  CB  . ALA A 1 61  ? 86.520  1.941   32.116  1.00 11.55 ? 63   ALA A CB  1 
ATOM   472  N  N   . LEU A 1 62  ? 84.516  0.560   34.511  1.00 11.12 ? 64   LEU A N   1 
ATOM   473  C  CA  . LEU A 1 62  ? 83.554  -0.501  34.791  1.00 11.38 ? 64   LEU A CA  1 
ATOM   474  C  C   . LEU A 1 62  ? 82.166  -0.163  34.257  1.00 10.78 ? 64   LEU A C   1 
ATOM   475  O  O   . LEU A 1 62  ? 81.646  0.926   34.495  1.00 10.75 ? 64   LEU A O   1 
ATOM   476  C  CB  . LEU A 1 62  ? 83.493  -0.796  36.293  1.00 11.39 ? 64   LEU A CB  1 
ATOM   477  C  CG  . LEU A 1 62  ? 82.589  -1.948  36.746  1.00 12.84 ? 64   LEU A CG  1 
ATOM   478  C  CD1 . LEU A 1 62  ? 83.048  -2.496  38.092  1.00 15.08 ? 64   LEU A CD1 1 
ATOM   479  C  CD2 . LEU A 1 62  ? 81.138  -1.494  36.825  1.00 12.21 ? 64   LEU A CD2 1 
ATOM   480  N  N   . ASN A 1 63  ? 81.577  -1.103  33.526  1.00 10.76 ? 65   ASN A N   1 
ATOM   481  C  CA  . ASN A 1 63  ? 80.171  -1.025  33.150  1.00 10.21 ? 65   ASN A CA  1 
ATOM   482  C  C   . ASN A 1 63  ? 79.473  -2.301  33.605  1.00 10.01 ? 65   ASN A C   1 
ATOM   483  O  O   . ASN A 1 63  ? 80.129  -3.318  33.838  1.00 10.00 ? 65   ASN A O   1 
ATOM   484  C  CB  . ASN A 1 63  ? 80.035  -0.879  31.631  1.00 10.27 ? 65   ASN A CB  1 
ATOM   485  C  CG  . ASN A 1 63  ? 80.036  0.570   31.168  1.00 10.81 ? 65   ASN A CG  1 
ATOM   486  O  OD1 . ASN A 1 63  ? 79.624  0.865   30.046  1.00 10.44 ? 65   ASN A OD1 1 
ATOM   487  N  ND2 . ASN A 1 63  ? 80.522  1.477   32.016  1.00 10.51 ? 65   ASN A ND2 1 
ATOM   488  N  N   . ILE A 1 64  ? 78.152  -2.251  33.747  1.00 9.89  ? 66   ILE A N   1 
ATOM   489  C  CA  . ILE A 1 64  ? 77.401  -3.425  34.197  1.00 9.78  ? 66   ILE A CA  1 
ATOM   490  C  C   . ILE A 1 64  ? 76.036  -3.537  33.522  1.00 9.91  ? 66   ILE A C   1 
ATOM   491  O  O   . ILE A 1 64  ? 75.353  -2.538  33.305  1.00 10.43 ? 66   ILE A O   1 
ATOM   492  C  CB  . ILE A 1 64  ? 77.239  -3.443  35.732  1.00 10.09 ? 66   ILE A CB  1 
ATOM   493  C  CG1 . ILE A 1 64  ? 76.596  -4.755  36.188  1.00 10.23 ? 66   ILE A CG1 1 
ATOM   494  C  CG2 . ILE A 1 64  ? 76.427  -2.243  36.201  1.00 10.20 ? 66   ILE A CG2 1 
ATOM   495  C  CD1 . ILE A 1 64  ? 76.835  -5.075  37.647  1.00 10.66 ? 66   ILE A CD1 1 
ATOM   496  N  N   . ALA A 1 65  ? 75.661  -4.756  33.155  1.00 9.56  ? 67   ALA A N   1 
ATOM   497  C  CA  . ALA A 1 65  ? 74.406  -4.987  32.454  1.00 9.67  ? 67   ALA A CA  1 
ATOM   498  C  C   . ALA A 1 65  ? 73.752  -6.271  32.946  1.00 9.73  ? 67   ALA A C   1 
ATOM   499  O  O   . ALA A 1 65  ? 74.438  -7.200  33.382  1.00 9.58  ? 67   ALA A O   1 
ATOM   500  C  CB  . ALA A 1 65  ? 74.638  -5.041  30.948  1.00 9.30  ? 67   ALA A CB  1 
ATOM   501  N  N   . PHE A 1 66  ? 72.423  -6.304  32.906  1.00 9.59  ? 68   PHE A N   1 
ATOM   502  C  CA  . PHE A 1 66  ? 71.660  -7.404  33.480  1.00 9.80  ? 68   PHE A CA  1 
ATOM   503  C  C   . PHE A 1 66  ? 70.807  -8.105  32.428  1.00 9.99  ? 68   PHE A C   1 
ATOM   504  O  O   . PHE A 1 66  ? 70.227  -7.459  31.555  1.00 9.21  ? 68   PHE A O   1 
ATOM   505  C  CB  . PHE A 1 66  ? 70.780  -6.897  34.630  1.00 10.16 ? 68   PHE A CB  1 
ATOM   506  C  CG  . PHE A 1 66  ? 71.563  -6.362  35.797  1.00 10.15 ? 68   PHE A CG  1 
ATOM   507  C  CD1 . PHE A 1 66  ? 71.990  -7.208  36.805  1.00 10.54 ? 68   PHE A CD1 1 
ATOM   508  C  CD2 . PHE A 1 66  ? 71.928  -5.025  35.851  1.00 10.65 ? 68   PHE A CD2 1 
ATOM   509  C  CE1 . PHE A 1 66  ? 72.744  -6.732  37.859  1.00 10.30 ? 68   PHE A CE1 1 
ATOM   510  C  CE2 . PHE A 1 66  ? 72.688  -4.542  36.900  1.00 10.53 ? 68   PHE A CE2 1 
ATOM   511  C  CZ  . PHE A 1 66  ? 73.093  -5.396  37.908  1.00 10.45 ? 68   PHE A CZ  1 
ATOM   512  N  N   . SER A 1 67  ? 70.760  -9.434  32.497  1.00 10.01 ? 69   SER A N   1 
ATOM   513  C  CA  . SER A 1 67  ? 69.861  -10.206 31.648  1.00 9.96  ? 69   SER A CA  1 
ATOM   514  C  C   . SER A 1 67  ? 68.447  -10.081 32.191  1.00 10.26 ? 69   SER A C   1 
ATOM   515  O  O   . SER A 1 67  ? 68.246  -9.576  33.295  1.00 9.87  ? 69   SER A O   1 
ATOM   516  C  CB  . SER A 1 67  ? 70.266  -11.679 31.653  1.00 10.40 ? 69   SER A CB  1 
ATOM   517  O  OG  . SER A 1 67  ? 69.959  -12.271 32.907  1.00 10.95 ? 69   SER A OG  1 
ATOM   518  N  N   . ASN A 1 68  ? 67.480  -10.618 31.456  1.00 10.68 ? 70   ASN A N   1 
ATOM   519  C  CA  . ASN A 1 68  ? 66.111  -10.686 31.956  1.00 11.34 ? 70   ASN A CA  1 
ATOM   520  C  C   . ASN A 1 68  ? 66.020  -11.464 33.266  1.00 11.44 ? 70   ASN A C   1 
ATOM   521  O  O   . ASN A 1 68  ? 65.364  -11.028 34.211  1.00 10.70 ? 70   ASN A O   1 
ATOM   522  C  CB  . ASN A 1 68  ? 65.178  -11.301 30.915  1.00 11.40 ? 70   ASN A CB  1 
ATOM   523  C  CG  . ASN A 1 68  ? 63.783  -11.539 31.457  1.00 12.01 ? 70   ASN A CG  1 
ATOM   524  O  OD1 . ASN A 1 68  ? 63.042  -10.594 31.721  1.00 12.59 ? 70   ASN A OD1 1 
ATOM   525  N  ND2 . ASN A 1 68  ? 63.436  -12.806 31.673  1.00 11.76 ? 70   ASN A ND2 1 
ATOM   526  N  N   . THR A 1 69  ? 66.695  -12.608 33.329  1.00 11.74 ? 71   THR A N   1 
ATOM   527  C  CA  . THR A 1 69  ? 66.647  -13.433 34.533  1.00 11.69 ? 71   THR A CA  1 
ATOM   528  C  C   . THR A 1 69  ? 67.371  -12.779 35.705  1.00 11.72 ? 71   THR A C   1 
ATOM   529  O  O   . THR A 1 69  ? 66.978  -12.950 36.860  1.00 11.97 ? 71   THR A O   1 
ATOM   530  C  CB  . THR A 1 69  ? 67.200  -14.850 34.292  1.00 12.45 ? 71   THR A CB  1 
ATOM   531  O  OG1 . THR A 1 69  ? 68.435  -14.770 33.574  1.00 13.69 ? 71   THR A OG1 1 
ATOM   532  C  CG2 . THR A 1 69  ? 66.204  -15.680 33.493  1.00 11.83 ? 71   THR A CG2 1 
ATOM   533  N  N   . GLY A 1 70  ? 68.407  -12.003 35.400  1.00 10.84 ? 72   GLY A N   1 
ATOM   534  C  CA  . GLY A 1 70  ? 69.087  -11.197 36.402  1.00 10.63 ? 72   GLY A CA  1 
ATOM   535  C  C   . GLY A 1 70  ? 68.183  -10.146 37.017  1.00 11.07 ? 72   GLY A C   1 
ATOM   536  O  O   . GLY A 1 70  ? 68.182  -9.954  38.232  1.00 11.01 ? 72   GLY A O   1 
ATOM   537  N  N   . LEU A 1 71  ? 67.410  -9.462  36.178  1.00 11.22 ? 73   LEU A N   1 
ATOM   538  C  CA  . LEU A 1 71  ? 66.438  -8.489  36.672  1.00 11.94 ? 73   LEU A CA  1 
ATOM   539  C  C   . LEU A 1 71  ? 65.389  -9.167  37.544  1.00 12.74 ? 73   LEU A C   1 
ATOM   540  O  O   . LEU A 1 71  ? 65.056  -8.680  38.632  1.00 13.65 ? 73   LEU A O   1 
ATOM   541  C  CB  . LEU A 1 71  ? 65.772  -7.745  35.511  1.00 11.95 ? 73   LEU A CB  1 
ATOM   542  C  CG  . LEU A 1 71  ? 66.677  -6.765  34.757  1.00 11.99 ? 73   LEU A CG  1 
ATOM   543  C  CD1 . LEU A 1 71  ? 65.943  -6.134  33.583  1.00 11.45 ? 73   LEU A CD1 1 
ATOM   544  C  CD2 . LEU A 1 71  ? 67.220  -5.693  35.693  1.00 11.93 ? 73   LEU A CD2 1 
ATOM   545  N  N   . LEU A 1 72  ? 64.913  -10.324 37.097  1.00 12.77 ? 74   LEU A N   1 
ATOM   546  C  CA  . LEU A 1 72  ? 63.967  -11.099 37.889  1.00 13.97 ? 74   LEU A CA  1 
ATOM   547  C  C   . LEU A 1 72  ? 64.552  -11.492 39.245  1.00 14.70 ? 74   LEU A C   1 
ATOM   548  O  O   . LEU A 1 72  ? 63.860  -11.452 40.260  1.00 14.32 ? 74   LEU A O   1 
ATOM   549  C  CB  . LEU A 1 72  ? 63.503  -12.337 37.123  1.00 13.99 ? 74   LEU A CB  1 
ATOM   550  C  CG  . LEU A 1 72  ? 62.595  -12.060 35.922  1.00 13.76 ? 74   LEU A CG  1 
ATOM   551  C  CD1 . LEU A 1 72  ? 62.154  -13.361 35.269  1.00 14.28 ? 74   LEU A CD1 1 
ATOM   552  C  CD2 . LEU A 1 72  ? 61.388  -11.241 36.349  1.00 14.12 ? 74   LEU A CD2 1 
ATOM   553  N  N   . ALA A 1 73  ? 65.834  -11.845 39.264  1.00 14.67 ? 75   ALA A N   1 
ATOM   554  C  CA  . ALA A 1 73  ? 66.482  -12.264 40.503  1.00 14.67 ? 75   ALA A CA  1 
ATOM   555  C  C   . ALA A 1 73  ? 66.559  -11.106 41.493  1.00 14.74 ? 75   ALA A C   1 
ATOM   556  O  O   . ALA A 1 73  ? 66.573  -11.313 42.708  1.00 14.82 ? 75   ALA A O   1 
ATOM   557  C  CB  . ALA A 1 73  ? 67.870  -12.822 40.218  1.00 14.12 ? 75   ALA A CB  1 
ATOM   558  N  N   . LEU A 1 74  ? 66.615  -9.887  40.964  1.00 14.99 ? 76   LEU A N   1 
ATOM   559  C  CA  . LEU A 1 74  ? 66.672  -8.685  41.789  1.00 15.08 ? 76   LEU A CA  1 
ATOM   560  C  C   . LEU A 1 74  ? 65.274  -8.189  42.162  1.00 15.61 ? 76   LEU A C   1 
ATOM   561  O  O   . LEU A 1 74  ? 65.124  -7.116  42.749  1.00 16.97 ? 76   LEU A O   1 
ATOM   562  C  CB  . LEU A 1 74  ? 67.439  -7.573  41.066  1.00 14.49 ? 76   LEU A CB  1 
ATOM   563  C  CG  . LEU A 1 74  ? 68.950  -7.737  40.896  1.00 15.06 ? 76   LEU A CG  1 
ATOM   564  C  CD1 . LEU A 1 74  ? 69.506  -6.642  39.997  1.00 15.47 ? 76   LEU A CD1 1 
ATOM   565  C  CD2 . LEU A 1 74  ? 69.658  -7.739  42.242  1.00 14.85 ? 76   LEU A CD2 1 
ATOM   566  N  N   . GLY A 1 75  ? 64.255  -8.962  41.808  1.00 14.94 ? 77   GLY A N   1 
ATOM   567  C  CA  . GLY A 1 75  ? 62.875  -8.594  42.121  1.00 16.10 ? 77   GLY A CA  1 
ATOM   568  C  C   . GLY A 1 75  ? 62.314  -7.520  41.207  1.00 16.83 ? 77   GLY A C   1 
ATOM   569  O  O   . GLY A 1 75  ? 61.262  -6.944  41.486  1.00 17.04 ? 77   GLY A O   1 
ATOM   570  N  N   . VAL A 1 76  ? 63.008  -7.252  40.106  1.00 15.15 ? 78   VAL A N   1 
ATOM   571  C  CA  . VAL A 1 76  ? 62.543  -6.260  39.144  1.00 15.13 ? 78   VAL A CA  1 
ATOM   572  C  C   . VAL A 1 76  ? 61.737  -6.925  38.034  1.00 15.95 ? 78   VAL A C   1 
ATOM   573  O  O   . VAL A 1 76  ? 62.298  -7.562  37.141  1.00 15.66 ? 78   VAL A O   1 
ATOM   574  C  CB  . VAL A 1 76  ? 63.711  -5.459  38.535  1.00 15.38 ? 78   VAL A CB  1 
ATOM   575  C  CG1 . VAL A 1 76  ? 63.188  -4.445  37.528  1.00 15.29 ? 78   VAL A CG1 1 
ATOM   576  C  CG2 . VAL A 1 76  ? 64.512  -4.765  39.633  1.00 14.43 ? 78   VAL A CG2 1 
ATOM   577  N  N   . THR A 1 77  ? 60.416  -6.799  38.117  1.00 15.48 ? 79   THR A N   1 
ATOM   578  C  CA  . THR A 1 77  ? 59.512  -7.585  37.284  1.00 16.28 ? 79   THR A CA  1 
ATOM   579  C  C   . THR A 1 77  ? 58.876  -6.726  36.194  1.00 16.37 ? 79   THR A C   1 
ATOM   580  O  O   . THR A 1 77  ? 58.037  -7.203  35.427  1.00 15.96 ? 79   THR A O   1 
ATOM   581  C  CB  . THR A 1 77  ? 58.395  -8.225  38.126  1.00 17.28 ? 79   THR A CB  1 
ATOM   582  O  OG1 . THR A 1 77  ? 57.717  -7.204  38.866  1.00 16.82 ? 79   THR A OG1 1 
ATOM   583  C  CG2 . THR A 1 77  ? 58.975  -9.247  39.101  1.00 17.31 ? 79   THR A CG2 1 
ATOM   584  N  N   . ASP A 1 78  ? 59.299  -5.466  36.121  1.00 14.37 ? 80   ASP A N   1 
ATOM   585  C  CA  . ASP A 1 78  ? 58.778  -4.520  35.138  1.00 14.86 ? 80   ASP A CA  1 
ATOM   586  C  C   . ASP A 1 78  ? 58.984  -5.010  33.706  1.00 14.48 ? 80   ASP A C   1 
ATOM   587  O  O   . ASP A 1 78  ? 59.974  -5.679  33.400  1.00 14.53 ? 80   ASP A O   1 
ATOM   588  C  CB  . ASP A 1 78  ? 59.448  -3.151  35.299  1.00 14.75 ? 80   ASP A CB  1 
ATOM   589  C  CG  . ASP A 1 78  ? 59.348  -2.608  36.713  1.00 15.48 ? 80   ASP A CG  1 
ATOM   590  O  OD1 . ASP A 1 78  ? 58.520  -3.120  37.498  1.00 19.10 ? 80   ASP A OD1 1 
ATOM   591  O  OD2 . ASP A 1 78  ? 60.084  -1.651  37.036  1.00 15.18 ? 80   ASP A OD2 1 
ATOM   592  N  N   . ASN A 1 79  ? 58.067  -4.625  32.826  1.00 14.10 ? 81   ASN A N   1 
ATOM   593  C  CA  . ASN A 1 79  ? 58.203  -4.866  31.393  1.00 14.14 ? 81   ASN A CA  1 
ATOM   594  C  C   . ASN A 1 79  ? 59.137  -3.839  30.746  1.00 14.45 ? 81   ASN A C   1 
ATOM   595  O  O   . ASN A 1 79  ? 58.815  -2.654  30.681  1.00 14.30 ? 81   ASN A O   1 
ATOM   596  C  CB  . ASN A 1 79  ? 56.822  -4.809  30.735  1.00 13.98 ? 81   ASN A CB  1 
ATOM   597  C  CG  . ASN A 1 79  ? 56.849  -5.199  29.271  1.00 14.27 ? 81   ASN A CG  1 
ATOM   598  O  OD1 . ASN A 1 79  ? 57.910  -5.407  28.686  1.00 15.15 ? 81   ASN A OD1 1 
ATOM   599  N  ND2 . ASN A 1 79  ? 55.670  -5.295  28.668  1.00 14.30 ? 81   ASN A ND2 1 
ATOM   600  N  N   . LEU A 1 80  ? 60.292  -4.302  30.271  1.00 14.03 ? 82   LEU A N   1 
ATOM   601  C  CA  . LEU A 1 80  ? 61.271  -3.425  29.628  1.00 13.59 ? 82   LEU A CA  1 
ATOM   602  C  C   . LEU A 1 80  ? 60.886  -3.111  28.187  1.00 13.02 ? 82   LEU A C   1 
ATOM   603  O  O   . LEU A 1 80  ? 61.506  -2.267  27.545  1.00 13.71 ? 82   LEU A O   1 
ATOM   604  C  CB  . LEU A 1 80  ? 62.667  -4.057  29.664  1.00 14.44 ? 82   LEU A CB  1 
ATOM   605  C  CG  . LEU A 1 80  ? 63.538  -3.803  30.898  1.00 15.33 ? 82   LEU A CG  1 
ATOM   606  C  CD1 . LEU A 1 80  ? 64.047  -2.372  30.900  1.00 17.28 ? 82   LEU A CD1 1 
ATOM   607  C  CD2 . LEU A 1 80  ? 62.782  -4.110  32.183  1.00 15.15 ? 82   LEU A CD2 1 
ATOM   608  N  N   . GLY A 1 81  ? 59.891  -3.826  27.670  1.00 12.22 ? 83   GLY A N   1 
ATOM   609  C  CA  . GLY A 1 81  ? 59.319  -3.513  26.366  1.00 12.51 ? 83   GLY A CA  1 
ATOM   610  C  C   . GLY A 1 81  ? 60.068  -4.152  25.213  1.00 12.57 ? 83   GLY A C   1 
ATOM   611  O  O   . GLY A 1 81  ? 59.925  -3.737  24.062  1.00 13.51 ? 83   GLY A O   1 
ATOM   612  N  N   . ASP A 1 82  ? 60.841  -5.189  25.514  1.00 12.37 ? 84   ASP A N   1 
ATOM   613  C  CA  . ASP A 1 82  ? 61.616  -5.882  24.487  1.00 12.41 ? 84   ASP A CA  1 
ATOM   614  C  C   . ASP A 1 82  ? 61.465  -7.394  24.632  1.00 12.12 ? 84   ASP A C   1 
ATOM   615  O  O   . ASP A 1 82  ? 62.028  -7.998  25.544  1.00 11.90 ? 84   ASP A O   1 
ATOM   616  C  CB  . ASP A 1 82  ? 63.091  -5.481  24.574  1.00 12.61 ? 84   ASP A CB  1 
ATOM   617  C  CG  . ASP A 1 82  ? 63.870  -5.849  23.322  1.00 13.44 ? 84   ASP A CG  1 
ATOM   618  O  OD1 . ASP A 1 82  ? 64.052  -7.061  23.070  1.00 13.11 ? 84   ASP A OD1 1 
ATOM   619  O  OD2 . ASP A 1 82  ? 64.296  -4.925  22.592  1.00 13.00 ? 84   ASP A OD2 1 
ATOM   620  N  N   A SER A 1 83  ? 60.665  -7.981  23.746  0.50 12.17 ? 85   SER A N   1 
ATOM   621  N  N   B SER A 1 83  ? 60.718  -8.012  23.724  0.50 12.07 ? 85   SER A N   1 
ATOM   622  C  CA  A SER A 1 83  ? 60.366  -9.409  23.782  0.50 12.28 ? 85   SER A CA  1 
ATOM   623  C  CA  B SER A 1 83  ? 60.386  -9.427  23.866  0.50 11.91 ? 85   SER A CA  1 
ATOM   624  C  C   A SER A 1 83  ? 61.642  -10.234 23.667  0.50 11.71 ? 85   SER A C   1 
ATOM   625  C  C   B SER A 1 83  ? 61.557  -10.353 23.533  0.50 11.51 ? 85   SER A C   1 
ATOM   626  O  O   A SER A 1 83  ? 61.870  -11.162 24.446  0.50 11.73 ? 85   SER A O   1 
ATOM   627  O  O   B SER A 1 83  ? 61.640  -11.466 24.052  0.50 11.40 ? 85   SER A O   1 
ATOM   628  C  CB  A SER A 1 83  ? 59.409  -9.773  22.643  0.50 13.40 ? 85   SER A CB  1 
ATOM   629  C  CB  B SER A 1 83  ? 59.149  -9.784  23.042  0.50 12.61 ? 85   SER A CB  1 
ATOM   630  O  OG  A SER A 1 83  ? 59.062  -11.146 22.684  0.50 14.42 ? 85   SER A OG  1 
ATOM   631  O  OG  B SER A 1 83  ? 57.964  -9.459  23.750  0.50 12.89 ? 85   SER A OG  1 
ATOM   632  N  N   . LEU A 1 84  ? 62.475  -9.882  22.694  1.00 11.25 ? 86   LEU A N   1 
ATOM   633  C  CA  . LEU A 1 84  ? 63.722  -10.603 22.449  1.00 10.59 ? 86   LEU A CA  1 
ATOM   634  C  C   . LEU A 1 84  ? 64.603  -10.628 23.696  1.00 10.43 ? 86   LEU A C   1 
ATOM   635  O  O   . LEU A 1 84  ? 65.135  -11.673 24.071  1.00 10.20 ? 86   LEU A O   1 
ATOM   636  C  CB  . LEU A 1 84  ? 64.483  -9.980  21.278  1.00 10.21 ? 86   LEU A CB  1 
ATOM   637  C  CG  . LEU A 1 84  ? 63.841  -10.116 19.894  1.00 11.10 ? 86   LEU A CG  1 
ATOM   638  C  CD1 . LEU A 1 84  ? 64.673  -9.390  18.848  1.00 10.79 ? 86   LEU A CD1 1 
ATOM   639  C  CD2 . LEU A 1 84  ? 63.663  -11.580 19.518  1.00 10.84 ? 86   LEU A CD2 1 
ATOM   640  N  N   . PHE A 1 85  ? 64.761  -9.473  24.335  1.00 10.37 ? 87   PHE A N   1 
ATOM   641  C  CA  . PHE A 1 85  ? 65.479  -9.402  25.606  1.00 10.64 ? 87   PHE A CA  1 
ATOM   642  C  C   . PHE A 1 85  ? 64.875  -10.350 26.636  1.00 10.88 ? 87   PHE A C   1 
ATOM   643  O  O   . PHE A 1 85  ? 65.596  -11.056 27.340  1.00 11.36 ? 87   PHE A O   1 
ATOM   644  C  CB  . PHE A 1 85  ? 65.490  -7.968  26.148  1.00 10.31 ? 87   PHE A CB  1 
ATOM   645  C  CG  . PHE A 1 85  ? 65.983  -7.858  27.566  1.00 10.30 ? 87   PHE A CG  1 
ATOM   646  C  CD1 . PHE A 1 85  ? 67.313  -8.104  27.876  1.00 10.45 ? 87   PHE A CD1 1 
ATOM   647  C  CD2 . PHE A 1 85  ? 65.120  -7.490  28.586  1.00 10.18 ? 87   PHE A CD2 1 
ATOM   648  C  CE1 . PHE A 1 85  ? 67.770  -7.994  29.180  1.00 10.34 ? 87   PHE A CE1 1 
ATOM   649  C  CE2 . PHE A 1 85  ? 65.571  -7.380  29.890  1.00 10.16 ? 87   PHE A CE2 1 
ATOM   650  C  CZ  . PHE A 1 85  ? 66.897  -7.632  30.188  1.00 9.96  ? 87   PHE A CZ  1 
ATOM   651  N  N   . ALA A 1 86  ? 63.550  -10.374 26.713  1.00 10.85 ? 88   ALA A N   1 
ATOM   652  C  CA  . ALA A 1 86  ? 62.869  -11.177 27.722  1.00 12.01 ? 88   ALA A CA  1 
ATOM   653  C  C   . ALA A 1 86  ? 63.103  -12.668 27.492  1.00 12.26 ? 88   ALA A C   1 
ATOM   654  O  O   . ALA A 1 86  ? 63.357  -13.417 28.434  1.00 12.86 ? 88   ALA A O   1 
ATOM   655  C  CB  . ALA A 1 86  ? 61.380  -10.861 27.744  1.00 12.59 ? 88   ALA A CB  1 
ATOM   656  N  N   . ASN A 1 87  ? 63.050  -13.088 26.232  1.00 13.51 ? 89   ASN A N   1 
ATOM   657  C  CA  . ASN A 1 87  ? 63.219  -14.498 25.887  1.00 14.37 ? 89   ASN A CA  1 
ATOM   658  C  C   . ASN A 1 87  ? 64.663  -14.991 25.996  1.00 13.46 ? 89   ASN A C   1 
ATOM   659  O  O   . ASN A 1 87  ? 64.907  -16.182 26.191  1.00 12.74 ? 89   ASN A O   1 
ATOM   660  C  CB  . ASN A 1 87  ? 62.669  -14.778 24.489  1.00 15.55 ? 89   ASN A CB  1 
ATOM   661  C  CG  . ASN A 1 87  ? 61.159  -14.868 24.471  1.00 18.34 ? 89   ASN A CG  1 
ATOM   662  O  OD1 . ASN A 1 87  ? 60.549  -15.401 25.397  1.00 20.65 ? 89   ASN A OD1 1 
ATOM   663  N  ND2 . ASN A 1 87  ? 60.547  -14.352 23.414  1.00 19.27 ? 89   ASN A ND2 1 
ATOM   664  N  N   . GLY A 1 88  ? 65.618  -14.074 25.860  1.00 12.72 ? 90   GLY A N   1 
ATOM   665  C  CA  . GLY A 1 88  ? 67.032  -14.440 25.910  1.00 12.58 ? 90   GLY A CA  1 
ATOM   666  C  C   . GLY A 1 88  ? 67.563  -14.876 24.558  1.00 12.16 ? 90   GLY A C   1 
ATOM   667  O  O   . GLY A 1 88  ? 66.808  -15.346 23.711  1.00 12.64 ? 90   GLY A O   1 
ATOM   668  N  N   . GLN A 1 89  ? 68.872  -14.745 24.359  1.00 12.08 ? 91   GLN A N   1 
ATOM   669  C  CA  . GLN A 1 89  ? 69.459  -14.955 23.041  1.00 11.03 ? 91   GLN A CA  1 
ATOM   670  C  C   . GLN A 1 89  ? 69.402  -16.412 22.593  1.00 11.53 ? 91   GLN A C   1 
ATOM   671  O  O   . GLN A 1 89  ? 69.288  -16.692 21.401  1.00 11.07 ? 91   GLN A O   1 
ATOM   672  C  CB  . GLN A 1 89  ? 70.901  -14.444 22.984  1.00 10.69 ? 91   GLN A CB  1 
ATOM   673  C  CG  . GLN A 1 89  ? 71.428  -14.293 21.565  1.00 10.44 ? 91   GLN A CG  1 
ATOM   674  C  CD  . GLN A 1 89  ? 72.889  -13.887 21.521  1.00 10.24 ? 91   GLN A CD  1 
ATOM   675  O  OE1 . GLN A 1 89  ? 73.753  -14.688 21.174  1.00 10.26 ? 91   GLN A OE1 1 
ATOM   676  N  NE2 . GLN A 1 89  ? 73.174  -12.650 21.909  1.00 10.58 ? 91   GLN A NE2 1 
ATOM   677  N  N   . ALA A 1 90  ? 69.473  -17.336 23.546  1.00 12.15 ? 92   ALA A N   1 
ATOM   678  C  CA  . ALA A 1 90  ? 69.431  -18.759 23.215  1.00 12.99 ? 92   ALA A CA  1 
ATOM   679  C  C   . ALA A 1 90  ? 68.164  -19.120 22.441  1.00 13.39 ? 92   ALA A C   1 
ATOM   680  O  O   . ALA A 1 90  ? 68.213  -19.877 21.475  1.00 14.02 ? 92   ALA A O   1 
ATOM   681  C  CB  . ALA A 1 90  ? 69.567  -19.613 24.469  1.00 12.12 ? 92   ALA A CB  1 
ATOM   682  N  N   . LYS A 1 91  ? 67.035  -18.545 22.840  1.00 14.46 ? 93   LYS A N   1 
ATOM   683  C  CA  . LYS A 1 91  ? 65.776  -18.776 22.133  1.00 14.52 ? 93   LYS A CA  1 
ATOM   684  C  C   . LYS A 1 91  ? 65.788  -18.149 20.737  1.00 15.05 ? 93   LYS A C   1 
ATOM   685  O  O   . LYS A 1 91  ? 65.017  -18.538 19.860  1.00 15.16 ? 93   LYS A O   1 
ATOM   686  C  CB  . LYS A 1 91  ? 64.599  -18.227 22.940  1.00 15.37 ? 93   LYS A CB  1 
ATOM   687  C  CG  . LYS A 1 91  ? 64.153  -19.130 24.078  1.00 17.79 ? 93   LYS A CG  1 
ATOM   688  C  CD  . LYS A 1 91  ? 62.642  -19.081 24.240  1.00 20.82 ? 93   LYS A CD  1 
ATOM   689  C  CE  . LYS A 1 91  ? 62.226  -19.287 25.688  1.00 20.91 ? 93   LYS A CE  1 
ATOM   690  N  NZ  . LYS A 1 91  ? 63.087  -20.286 26.378  1.00 20.33 ? 93   LYS A NZ  1 
ATOM   691  N  N   . ASP A 1 92  ? 66.672  -17.179 20.536  1.00 13.93 ? 94   ASP A N   1 
ATOM   692  C  CA  . ASP A 1 92  ? 66.718  -16.434 19.284  1.00 14.41 ? 94   ASP A CA  1 
ATOM   693  C  C   . ASP A 1 92  ? 67.617  -17.102 18.238  1.00 14.26 ? 94   ASP A C   1 
ATOM   694  O  O   . ASP A 1 92  ? 67.683  -16.651 17.097  1.00 15.19 ? 94   ASP A O   1 
ATOM   695  C  CB  . ASP A 1 92  ? 67.187  -15.000 19.547  1.00 13.93 ? 94   ASP A CB  1 
ATOM   696  C  CG  . ASP A 1 92  ? 66.627  -14.003 18.548  1.00 13.80 ? 94   ASP A CG  1 
ATOM   697  O  OD1 . ASP A 1 92  ? 65.617  -14.313 17.880  1.00 14.18 ? 94   ASP A OD1 1 
ATOM   698  O  OD2 . ASP A 1 92  ? 67.182  -12.890 18.454  1.00 13.10 ? 94   ASP A OD2 1 
ATOM   699  N  N   . ALA A 1 93  ? 68.306  -18.174 18.621  1.00 14.39 ? 95   ALA A N   1 
ATOM   700  C  CA  . ALA A 1 93  ? 69.323  -18.769 17.747  1.00 15.17 ? 95   ALA A CA  1 
ATOM   701  C  C   . ALA A 1 93  ? 68.749  -19.243 16.413  1.00 15.76 ? 95   ALA A C   1 
ATOM   702  O  O   . ALA A 1 93  ? 69.402  -19.135 15.373  1.00 15.72 ? 95   ALA A O   1 
ATOM   703  C  CB  . ALA A 1 93  ? 70.053  -19.906 18.451  1.00 14.84 ? 95   ALA A CB  1 
ATOM   704  N  N   A THR A 1 94  ? 67.536  -19.787 16.451  0.50 15.78 ? 96   THR A N   1 
ATOM   705  N  N   B THR A 1 94  ? 67.528  -19.768 16.443  0.50 16.11 ? 96   THR A N   1 
ATOM   706  C  CA  A THR A 1 94  ? 66.884  -20.278 15.242  0.50 15.96 ? 96   THR A CA  1 
ATOM   707  C  CA  B THR A 1 94  ? 66.900  -20.284 15.231  0.50 16.32 ? 96   THR A CA  1 
ATOM   708  C  C   A THR A 1 94  ? 66.698  -19.153 14.232  0.50 15.64 ? 96   THR A C   1 
ATOM   709  C  C   B THR A 1 94  ? 66.611  -19.169 14.230  0.50 15.83 ? 96   THR A C   1 
ATOM   710  O  O   A THR A 1 94  ? 66.808  -19.366 13.025  0.50 14.98 ? 96   THR A O   1 
ATOM   711  O  O   B THR A 1 94  ? 66.581  -19.404 13.021  0.50 15.21 ? 96   THR A O   1 
ATOM   712  C  CB  A THR A 1 94  ? 65.512  -20.902 15.551  0.50 16.75 ? 96   THR A CB  1 
ATOM   713  C  CB  B THR A 1 94  ? 65.601  -21.049 15.543  0.50 17.37 ? 96   THR A CB  1 
ATOM   714  O  OG1 A THR A 1 94  ? 65.633  -21.805 16.657  0.50 16.94 ? 96   THR A OG1 1 
ATOM   715  O  OG1 B THR A 1 94  ? 64.745  -20.234 16.354  0.50 17.40 ? 96   THR A OG1 1 
ATOM   716  C  CG2 A THR A 1 94  ? 64.985  -21.654 14.339  0.50 16.37 ? 96   THR A CG2 1 
ATOM   717  C  CG2 B THR A 1 94  ? 65.911  -22.341 16.282  0.50 17.80 ? 96   THR A CG2 1 
ATOM   718  N  N   . SER A 1 95  ? 66.421  -17.953 14.735  1.00 15.35 ? 97   SER A N   1 
ATOM   719  C  CA  . SER A 1 95  ? 66.218  -16.787 13.876  1.00 15.07 ? 97   SER A CA  1 
ATOM   720  C  C   . SER A 1 95  ? 67.448  -16.511 13.019  1.00 15.74 ? 97   SER A C   1 
ATOM   721  O  O   . SER A 1 95  ? 67.345  -15.905 11.954  1.00 16.31 ? 97   SER A O   1 
ATOM   722  C  CB  . SER A 1 95  ? 65.901  -15.545 14.712  1.00 15.30 ? 97   SER A CB  1 
ATOM   723  O  OG  . SER A 1 95  ? 64.708  -15.714 15.450  1.00 16.20 ? 97   SER A OG  1 
ATOM   724  N  N   . PHE A 1 96  ? 68.615  -16.901 13.524  1.00 14.43 ? 98   PHE A N   1 
ATOM   725  C  CA  . PHE A 1 96  ? 69.875  -16.625 12.848  1.00 14.34 ? 98   PHE A CA  1 
ATOM   726  C  C   . PHE A 1 96  ? 70.372  -17.862 12.116  1.00 14.74 ? 98   PHE A C   1 
ATOM   727  O  O   . PHE A 1 96  ? 71.489  -17.884 11.603  1.00 14.44 ? 98   PHE A O   1 
ATOM   728  C  CB  . PHE A 1 96  ? 70.929  -16.155 13.853  1.00 14.40 ? 98   PHE A CB  1 
ATOM   729  C  CG  . PHE A 1 96  ? 70.483  -14.997 14.699  1.00 13.17 ? 98   PHE A CG  1 
ATOM   730  C  CD1 . PHE A 1 96  ? 69.698  -13.993 14.159  1.00 12.83 ? 98   PHE A CD1 1 
ATOM   731  C  CD2 . PHE A 1 96  ? 70.860  -14.906 16.026  1.00 13.14 ? 98   PHE A CD2 1 
ATOM   732  C  CE1 . PHE A 1 96  ? 69.291  -12.923 14.931  1.00 13.08 ? 98   PHE A CE1 1 
ATOM   733  C  CE2 . PHE A 1 96  ? 70.452  -13.841 16.807  1.00 12.88 ? 98   PHE A CE2 1 
ATOM   734  C  CZ  . PHE A 1 96  ? 69.672  -12.846 16.256  1.00 13.54 ? 98   PHE A CZ  1 
ATOM   735  N  N   . LYS A 1 97  ? 69.542  -18.900 12.097  1.00 14.41 ? 99   LYS A N   1 
ATOM   736  C  CA  . LYS A 1 97  ? 69.886  -20.135 11.411  1.00 15.37 ? 99   LYS A CA  1 
ATOM   737  C  C   . LYS A 1 97  ? 71.202  -20.696 11.929  1.00 14.62 ? 99   LYS A C   1 
ATOM   738  O  O   . LYS A 1 97  ? 72.072  -21.086 11.153  1.00 13.55 ? 99   LYS A O   1 
ATOM   739  C  CB  . LYS A 1 97  ? 69.975  -19.899 9.904   1.00 15.74 ? 99   LYS A CB  1 
ATOM   740  C  CG  . LYS A 1 97  ? 68.661  -19.487 9.263   1.00 17.21 ? 99   LYS A CG  1 
ATOM   741  C  CD  . LYS A 1 97  ? 68.773  -19.529 7.748   1.00 19.77 ? 99   LYS A CD  1 
ATOM   742  C  CE  . LYS A 1 97  ? 67.569  -18.889 7.077   1.00 20.20 ? 99   LYS A CE  1 
ATOM   743  N  NZ  . LYS A 1 97  ? 67.681  -18.975 5.595   1.00 21.81 ? 99   LYS A NZ  1 
ATOM   744  N  N   . GLU A 1 98  ? 71.353  -20.718 13.248  1.00 14.78 ? 100  GLU A N   1 
ATOM   745  C  CA  . GLU A 1 98  ? 72.524  -21.327 13.860  1.00 15.80 ? 100  GLU A CA  1 
ATOM   746  C  C   . GLU A 1 98  ? 72.123  -22.352 14.911  1.00 16.54 ? 100  GLU A C   1 
ATOM   747  O  O   . GLU A 1 98  ? 71.014  -22.311 15.444  1.00 16.74 ? 100  GLU A O   1 
ATOM   748  C  CB  . GLU A 1 98  ? 73.451  -20.263 14.461  1.00 15.44 ? 100  GLU A CB  1 
ATOM   749  C  CG  . GLU A 1 98  ? 72.957  -19.643 15.760  1.00 14.84 ? 100  GLU A CG  1 
ATOM   750  C  CD  . GLU A 1 98  ? 73.811  -18.467 16.209  1.00 15.01 ? 100  GLU A CD  1 
ATOM   751  O  OE1 . GLU A 1 98  ? 74.048  -17.551 15.392  1.00 14.55 ? 100  GLU A OE1 1 
ATOM   752  O  OE2 . GLU A 1 98  ? 74.234  -18.446 17.386  1.00 14.62 ? 100  GLU A OE2 1 
ATOM   753  N  N   . SER A 1 99  ? 73.021  -23.297 15.167  1.00 17.82 ? 101  SER A N   1 
ATOM   754  C  CA  . SER A 1 99  ? 72.791  -24.331 16.163  1.00 18.97 ? 101  SER A CA  1 
ATOM   755  C  C   . SER A 1 99  ? 73.496  -23.966 17.467  1.00 18.72 ? 101  SER A C   1 
ATOM   756  O  O   . SER A 1 99  ? 74.589  -23.402 17.452  1.00 19.93 ? 101  SER A O   1 
ATOM   757  C  CB  . SER A 1 99  ? 73.302  -25.677 15.641  1.00 20.95 ? 101  SER A CB  1 
ATOM   758  O  OG  . SER A 1 99  ? 73.380  -26.634 16.681  1.00 22.72 ? 101  SER A OG  1 
ATOM   759  N  N   . THR A 1 100 ? 72.866  -24.288 18.592  1.00 17.87 ? 102  THR A N   1 
ATOM   760  C  CA  . THR A 1 100 ? 73.474  -24.062 19.899  1.00 17.26 ? 102  THR A CA  1 
ATOM   761  C  C   . THR A 1 100 ? 74.474  -25.158 20.258  1.00 16.91 ? 102  THR A C   1 
ATOM   762  O  O   . THR A 1 100 ? 75.039  -25.161 21.352  1.00 15.93 ? 102  THR A O   1 
ATOM   763  C  CB  . THR A 1 100 ? 72.415  -23.973 21.012  1.00 18.43 ? 102  THR A CB  1 
ATOM   764  O  OG1 . THR A 1 100 ? 71.523  -25.090 20.915  1.00 17.58 ? 102  THR A OG1 1 
ATOM   765  C  CG2 . THR A 1 100 ? 71.622  -22.677 20.892  1.00 18.38 ? 102  THR A CG2 1 
ATOM   766  N  N   . SER A 1 101 ? 74.694  -26.085 19.332  1.00 17.11 ? 103  SER A N   1 
ATOM   767  C  CA  . SER A 1 101 ? 75.717  -27.102 19.519  1.00 16.62 ? 103  SER A CA  1 
ATOM   768  C  C   . SER A 1 101 ? 77.111  -26.481 19.607  1.00 15.92 ? 103  SER A C   1 
ATOM   769  O  O   . SER A 1 101 ? 77.980  -27.000 20.298  1.00 15.49 ? 103  SER A O   1 
ATOM   770  C  CB  . SER A 1 101 ? 75.655  -28.153 18.406  1.00 17.42 ? 103  SER A CB  1 
ATOM   771  O  OG  . SER A 1 101 ? 75.958  -27.587 17.143  1.00 18.88 ? 103  SER A OG  1 
ATOM   772  N  N   . SER A 1 102 ? 77.308  -25.345 18.945  1.00 15.99 ? 104  SER A N   1 
ATOM   773  C  CA  . SER A 1 102 ? 78.601  -24.661 18.989  1.00 15.70 ? 104  SER A CA  1 
ATOM   774  C  C   . SER A 1 102 ? 78.712  -23.642 20.126  1.00 14.94 ? 104  SER A C   1 
ATOM   775  O  O   . SER A 1 102 ? 79.762  -23.028 20.316  1.00 14.51 ? 104  SER A O   1 
ATOM   776  C  CB  . SER A 1 102 ? 78.891  -23.980 17.652  1.00 16.36 ? 104  SER A CB  1 
ATOM   777  O  OG  . SER A 1 102 ? 77.898  -23.013 17.355  1.00 18.58 ? 104  SER A OG  1 
ATOM   778  N  N   . TRP A 1 103 ? 77.632  -23.470 20.882  1.00 13.62 ? 105  TRP A N   1 
ATOM   779  C  CA  . TRP A 1 103 ? 77.559  -22.411 21.884  1.00 12.86 ? 105  TRP A CA  1 
ATOM   780  C  C   . TRP A 1 103 ? 78.393  -22.735 23.124  1.00 13.15 ? 105  TRP A C   1 
ATOM   781  O  O   . TRP A 1 103 ? 78.482  -23.893 23.536  1.00 12.82 ? 105  TRP A O   1 
ATOM   782  C  CB  . TRP A 1 103 ? 76.103  -22.172 22.291  1.00 12.82 ? 105  TRP A CB  1 
ATOM   783  C  CG  . TRP A 1 103 ? 75.361  -21.248 21.378  1.00 12.87 ? 105  TRP A CG  1 
ATOM   784  C  CD1 . TRP A 1 103 ? 75.410  -21.226 20.015  1.00 13.13 ? 105  TRP A CD1 1 
ATOM   785  C  CD2 . TRP A 1 103 ? 74.424  -20.235 21.763  1.00 12.19 ? 105  TRP A CD2 1 
ATOM   786  N  NE1 . TRP A 1 103 ? 74.581  -20.244 19.527  1.00 13.28 ? 105  TRP A NE1 1 
ATOM   787  C  CE2 . TRP A 1 103 ? 73.966  -19.620 20.580  1.00 12.61 ? 105  TRP A CE2 1 
ATOM   788  C  CE3 . TRP A 1 103 ? 73.949  -19.771 22.995  1.00 12.35 ? 105  TRP A CE3 1 
ATOM   789  C  CZ2 . TRP A 1 103 ? 73.056  -18.563 20.590  1.00 11.72 ? 105  TRP A CZ2 1 
ATOM   790  C  CZ3 . TRP A 1 103 ? 73.052  -18.710 23.006  1.00 11.91 ? 105  TRP A CZ3 1 
ATOM   791  C  CH2 . TRP A 1 103 ? 72.608  -18.125 21.809  1.00 12.26 ? 105  TRP A CH2 1 
ATOM   792  N  N   . VAL A 1 104 ? 78.977  -21.707 23.735  1.00 12.01 ? 106  VAL A N   1 
ATOM   793  C  CA  . VAL A 1 104 ? 79.432  -21.813 25.121  1.00 12.37 ? 106  VAL A CA  1 
ATOM   794  C  C   . VAL A 1 104 ? 78.275  -22.326 25.978  1.00 12.52 ? 106  VAL A C   1 
ATOM   795  O  O   . VAL A 1 104 ? 77.173  -21.782 25.925  1.00 12.22 ? 106  VAL A O   1 
ATOM   796  C  CB  . VAL A 1 104 ? 79.909  -20.453 25.665  1.00 11.70 ? 106  VAL A CB  1 
ATOM   797  C  CG1 . VAL A 1 104 ? 80.297  -20.565 27.134  1.00 11.33 ? 106  VAL A CG1 1 
ATOM   798  C  CG2 . VAL A 1 104 ? 81.074  -19.926 24.839  1.00 11.42 ? 106  VAL A CG2 1 
ATOM   799  N  N   . PRO A 1 105 ? 78.505  -23.410 26.735  1.00 12.82 ? 107  PRO A N   1 
ATOM   800  C  CA  . PRO A 1 105 ? 77.395  -24.021 27.463  1.00 13.35 ? 107  PRO A CA  1 
ATOM   801  C  C   . PRO A 1 105 ? 76.677  -23.017 28.361  1.00 12.62 ? 107  PRO A C   1 
ATOM   802  O  O   . PRO A 1 105 ? 75.448  -23.015 28.427  1.00 12.06 ? 107  PRO A O   1 
ATOM   803  C  CB  . PRO A 1 105 ? 78.083  -25.097 28.305  1.00 14.37 ? 107  PRO A CB  1 
ATOM   804  C  CG  . PRO A 1 105 ? 79.281  -25.480 27.498  1.00 13.73 ? 107  PRO A CG  1 
ATOM   805  C  CD  . PRO A 1 105 ? 79.728  -24.230 26.789  1.00 13.34 ? 107  PRO A CD  1 
ATOM   806  N  N   . GLN A 1 106 ? 77.442  -22.150 29.014  1.00 13.20 ? 108  GLN A N   1 
ATOM   807  C  CA  . GLN A 1 106 ? 76.877  -21.134 29.899  1.00 13.08 ? 108  GLN A CA  1 
ATOM   808  C  C   . GLN A 1 106 ? 75.923  -20.172 29.184  1.00 12.50 ? 108  GLN A C   1 
ATOM   809  O  O   . GLN A 1 106 ? 75.008  -19.631 29.804  1.00 12.67 ? 108  GLN A O   1 
ATOM   810  C  CB  . GLN A 1 106 ? 77.990  -20.358 30.607  1.00 12.78 ? 108  GLN A CB  1 
ATOM   811  C  CG  . GLN A 1 106 ? 78.792  -21.184 31.605  1.00 13.34 ? 108  GLN A CG  1 
ATOM   812  C  CD  . GLN A 1 106 ? 80.049  -21.787 31.001  1.00 13.63 ? 108  GLN A CD  1 
ATOM   813  O  OE1 . GLN A 1 106 ? 80.013  -22.387 29.927  1.00 13.78 ? 108  GLN A OE1 1 
ATOM   814  N  NE2 . GLN A 1 106 ? 81.169  -21.633 31.695  1.00 13.97 ? 108  GLN A NE2 1 
ATOM   815  N  N   . PHE A 1 107 ? 76.124  -19.971 27.883  1.00 12.04 ? 109  PHE A N   1 
ATOM   816  C  CA  . PHE A 1 107 ? 75.243  -19.092 27.105  1.00 11.91 ? 109  PHE A CA  1 
ATOM   817  C  C   . PHE A 1 107 ? 73.959  -19.801 26.690  1.00 12.47 ? 109  PHE A C   1 
ATOM   818  O  O   . PHE A 1 107 ? 72.949  -19.154 26.403  1.00 12.67 ? 109  PHE A O   1 
ATOM   819  C  CB  . PHE A 1 107 ? 75.942  -18.560 25.848  1.00 11.34 ? 109  PHE A CB  1 
ATOM   820  C  CG  . PHE A 1 107 ? 76.961  -17.483 26.113  1.00 11.67 ? 109  PHE A CG  1 
ATOM   821  C  CD1 . PHE A 1 107 ? 76.746  -16.522 27.085  1.00 11.95 ? 109  PHE A CD1 1 
ATOM   822  C  CD2 . PHE A 1 107 ? 78.107  -17.397 25.337  1.00 11.57 ? 109  PHE A CD2 1 
ATOM   823  C  CE1 . PHE A 1 107 ? 77.681  -15.524 27.316  1.00 12.21 ? 109  PHE A CE1 1 
ATOM   824  C  CE2 . PHE A 1 107 ? 79.045  -16.402 25.559  1.00 11.22 ? 109  PHE A CE2 1 
ATOM   825  C  CZ  . PHE A 1 107 ? 78.838  -15.472 26.561  1.00 11.85 ? 109  PHE A CZ  1 
ATOM   826  N  N   . ALA A 1 108 ? 74.021  -21.122 26.570  1.00 13.39 ? 110  ALA A N   1 
ATOM   827  C  CA  . ALA A 1 108 ? 72.896  -21.881 26.026  1.00 13.49 ? 110  ALA A CA  1 
ATOM   828  C  C   . ALA A 1 108 ? 71.865  -22.166 27.114  1.00 15.54 ? 110  ALA A C   1 
ATOM   829  O  O   . ALA A 1 108 ? 71.726  -23.299 27.580  1.00 15.48 ? 110  ALA A O   1 
ATOM   830  C  CB  . ALA A 1 108 ? 73.379  -23.171 25.382  1.00 13.20 ? 110  ALA A CB  1 
ATOM   831  N  N   . GLY A 1 109 ? 71.152  -21.120 27.516  1.00 15.75 ? 111  GLY A N   1 
ATOM   832  C  CA  . GLY A 1 109 ? 70.337  -21.147 28.725  1.00 15.91 ? 111  GLY A CA  1 
ATOM   833  C  C   . GLY A 1 109 ? 70.049  -19.734 29.190  1.00 15.77 ? 111  GLY A C   1 
ATOM   834  O  O   . GLY A 1 109 ? 70.351  -18.771 28.483  1.00 15.96 ? 111  GLY A O   1 
ATOM   835  N  N   . THR A 1 110 ? 69.503  -19.602 30.395  1.00 15.50 ? 112  THR A N   1 
ATOM   836  C  CA  . THR A 1 110 ? 69.282  -18.286 30.988  1.00 15.30 ? 112  THR A CA  1 
ATOM   837  C  C   . THR A 1 110 ? 69.801  -18.214 32.421  1.00 14.73 ? 112  THR A C   1 
ATOM   838  O  O   . THR A 1 110 ? 69.294  -17.445 33.241  1.00 15.00 ? 112  THR A O   1 
ATOM   839  C  CB  . THR A 1 110 ? 67.792  -17.899 30.960  1.00 16.02 ? 112  THR A CB  1 
ATOM   840  O  OG1 . THR A 1 110 ? 67.022  -18.896 31.644  1.00 16.22 ? 112  THR A OG1 1 
ATOM   841  C  CG2 . THR A 1 110 ? 67.301  -17.778 29.526  1.00 16.75 ? 112  THR A CG2 1 
ATOM   842  N  N   . GLY A 1 111 ? 70.839  -18.993 32.707  1.00 14.33 ? 113  GLY A N   1 
ATOM   843  C  CA  . GLY A 1 111 ? 71.469  -18.981 34.021  1.00 13.57 ? 113  GLY A CA  1 
ATOM   844  C  C   . GLY A 1 111 ? 72.271  -17.720 34.293  1.00 12.92 ? 113  GLY A C   1 
ATOM   845  O  O   . GLY A 1 111 ? 72.448  -17.323 35.446  1.00 12.24 ? 113  GLY A O   1 
ATOM   846  N  N   . ILE A 1 112 ? 72.758  -17.082 33.233  1.00 12.15 ? 114  ILE A N   1 
ATOM   847  C  CA  . ILE A 1 112 ? 73.514  -15.841 33.387  1.00 11.28 ? 114  ILE A CA  1 
ATOM   848  C  C   . ILE A 1 112 ? 72.606  -14.661 33.724  1.00 11.24 ? 114  ILE A C   1 
ATOM   849  O  O   . ILE A 1 112 ? 71.670  -14.347 32.986  1.00 11.61 ? 114  ILE A O   1 
ATOM   850  C  CB  . ILE A 1 112 ? 74.341  -15.508 32.131  1.00 11.18 ? 114  ILE A CB  1 
ATOM   851  C  CG1 . ILE A 1 112 ? 75.460  -16.534 31.944  1.00 11.04 ? 114  ILE A CG1 1 
ATOM   852  C  CG2 . ILE A 1 112 ? 74.923  -14.105 32.239  1.00 10.38 ? 114  ILE A CG2 1 
ATOM   853  C  CD1 . ILE A 1 112 ? 76.128  -16.447 30.587  1.00 11.30 ? 114  ILE A CD1 1 
ATOM   854  N  N   . HIS A 1 113 ? 72.920  -13.989 34.827  1.00 10.89 ? 115  HIS A N   1 
ATOM   855  C  CA  . HIS A 1 113 ? 72.093  -12.905 35.336  1.00 11.02 ? 115  HIS A CA  1 
ATOM   856  C  C   . HIS A 1 113 ? 72.604  -11.529 34.918  1.00 10.25 ? 115  HIS A C   1 
ATOM   857  O  O   . HIS A 1 113 ? 71.864  -10.546 34.964  1.00 9.83  ? 115  HIS A O   1 
ATOM   858  C  CB  . HIS A 1 113 ? 71.985  -12.987 36.859  1.00 11.11 ? 115  HIS A CB  1 
ATOM   859  C  CG  . HIS A 1 113 ? 71.157  -14.137 37.340  1.00 11.67 ? 115  HIS A CG  1 
ATOM   860  N  ND1 . HIS A 1 113 ? 71.196  -14.592 38.640  1.00 12.32 ? 115  HIS A ND1 1 
ATOM   861  C  CD2 . HIS A 1 113 ? 70.284  -14.940 36.686  1.00 12.12 ? 115  HIS A CD2 1 
ATOM   862  C  CE1 . HIS A 1 113 ? 70.374  -15.619 38.770  1.00 12.23 ? 115  HIS A CE1 1 
ATOM   863  N  NE2 . HIS A 1 113 ? 69.813  -15.853 37.597  1.00 13.22 ? 115  HIS A NE2 1 
ATOM   864  N  N   . GLY A 1 114 ? 73.863  -11.457 34.504  1.00 9.67  ? 116  GLY A N   1 
ATOM   865  C  CA  . GLY A 1 114 ? 74.443  -10.176 34.119  1.00 9.16  ? 116  GLY A CA  1 
ATOM   866  C  C   . GLY A 1 114 ? 75.866  -10.267 33.618  1.00 8.79  ? 116  GLY A C   1 
ATOM   867  O  O   . GLY A 1 114 ? 76.476  -11.335 33.628  1.00 8.37  ? 116  GLY A O   1 
ATOM   868  N  N   . VAL A 1 115 ? 76.396  -9.132  33.180  1.00 9.22  ? 117  VAL A N   1 
ATOM   869  C  CA  . VAL A 1 115 ? 77.797  -9.042  32.810  1.00 9.21  ? 117  VAL A CA  1 
ATOM   870  C  C   . VAL A 1 115 ? 78.413  -7.777  33.396  1.00 9.27  ? 117  VAL A C   1 
ATOM   871  O  O   . VAL A 1 115 ? 77.802  -6.704  33.372  1.00 9.42  ? 117  VAL A O   1 
ATOM   872  C  CB  . VAL A 1 115 ? 77.986  -9.078  31.278  1.00 9.23  ? 117  VAL A CB  1 
ATOM   873  C  CG1 . VAL A 1 115 ? 77.257  -7.918  30.616  1.00 9.27  ? 117  VAL A CG1 1 
ATOM   874  C  CG2 . VAL A 1 115 ? 79.465  -9.067  30.920  1.00 8.80  ? 117  VAL A CG2 1 
ATOM   875  N  N   . ILE A 1 116 ? 79.573  -7.935  34.022  1.00 9.22  ? 118  ILE A N   1 
ATOM   876  C  CA  . ILE A 1 116 ? 80.423  -6.802  34.339  1.00 9.65  ? 118  ILE A CA  1 
ATOM   877  C  C   . ILE A 1 116 ? 81.483  -6.655  33.255  1.00 10.10 ? 118  ILE A C   1 
ATOM   878  O  O   . ILE A 1 116 ? 82.189  -7.617  32.923  1.00 9.93  ? 118  ILE A O   1 
ATOM   879  C  CB  . ILE A 1 116 ? 81.093  -6.951  35.720  1.00 10.01 ? 118  ILE A CB  1 
ATOM   880  C  CG1 . ILE A 1 116 ? 80.032  -7.137  36.808  1.00 9.87  ? 118  ILE A CG1 1 
ATOM   881  C  CG2 . ILE A 1 116 ? 81.946  -5.730  36.034  1.00 10.05 ? 118  ILE A CG2 1 
ATOM   882  C  CD1 . ILE A 1 116 ? 80.610  -7.356  38.192  1.00 10.58 ? 118  ILE A CD1 1 
ATOM   883  N  N   . ILE A 1 117 ? 81.535  -5.472  32.653  1.00 10.47 ? 119  ILE A N   1 
ATOM   884  C  CA  . ILE A 1 117 ? 82.601  -5.134  31.718  1.00 11.14 ? 119  ILE A CA  1 
ATOM   885  C  C   . ILE A 1 117 ? 83.675  -4.355  32.468  1.00 11.95 ? 119  ILE A C   1 
ATOM   886  O  O   . ILE A 1 117 ? 83.404  -3.284  33.016  1.00 12.01 ? 119  ILE A O   1 
ATOM   887  C  CB  . ILE A 1 117 ? 82.077  -4.275  30.549  1.00 11.49 ? 119  ILE A CB  1 
ATOM   888  C  CG1 . ILE A 1 117 ? 80.951  -4.998  29.809  1.00 12.10 ? 119  ILE A CG1 1 
ATOM   889  C  CG2 . ILE A 1 117 ? 83.203  -3.932  29.585  1.00 11.93 ? 119  ILE A CG2 1 
ATOM   890  C  CD1 . ILE A 1 117 ? 80.315  -4.158  28.720  1.00 12.63 ? 119  ILE A CD1 1 
ATOM   891  N  N   . LEU A 1 118 ? 84.849  -4.963  32.599  1.00 12.04 ? 120  LEU A N   1 
ATOM   892  C  CA  . LEU A 1 118 ? 86.015  -4.287  33.160  1.00 12.48 ? 120  LEU A CA  1 
ATOM   893  C  C   . LEU A 1 118 ? 86.992  -3.969  32.041  1.00 12.35 ? 120  LEU A C   1 
ATOM   894  O  O   . LEU A 1 118 ? 87.271  -4.817  31.202  1.00 12.61 ? 120  LEU A O   1 
ATOM   895  C  CB  . LEU A 1 118 ? 86.700  -5.169  34.207  1.00 12.15 ? 120  LEU A CB  1 
ATOM   896  C  CG  . LEU A 1 118 ? 85.845  -5.589  35.403  1.00 13.50 ? 120  LEU A CG  1 
ATOM   897  C  CD1 . LEU A 1 118 ? 86.726  -6.132  36.519  1.00 14.29 ? 120  LEU A CD1 1 
ATOM   898  C  CD2 . LEU A 1 118 ? 85.036  -4.404  35.902  1.00 14.00 ? 120  LEU A CD2 1 
ATOM   899  N  N   . ALA A 1 119 ? 87.492  -2.739  32.023  1.00 12.57 ? 121  ALA A N   1 
ATOM   900  C  CA  . ALA A 1 119 ? 88.420  -2.309  30.988  1.00 11.92 ? 121  ALA A CA  1 
ATOM   901  C  C   . ALA A 1 119 ? 89.581  -1.537  31.602  1.00 12.89 ? 121  ALA A C   1 
ATOM   902  O  O   . ALA A 1 119 ? 89.378  -0.614  32.385  1.00 13.70 ? 121  ALA A O   1 
ATOM   903  C  CB  . ALA A 1 119 ? 87.701  -1.453  29.961  1.00 12.52 ? 121  ALA A CB  1 
ATOM   904  N  N   . SER A 1 120 ? 90.800  -1.936  31.260  1.00 12.93 ? 122  SER A N   1 
ATOM   905  C  CA  . SER A 1 120 ? 91.990  -1.264  31.762  1.00 14.31 ? 122  SER A CA  1 
ATOM   906  C  C   . SER A 1 120 ? 93.129  -1.461  30.776  1.00 15.28 ? 122  SER A C   1 
ATOM   907  O  O   . SER A 1 120 ? 93.027  -2.262  29.849  1.00 14.88 ? 122  SER A O   1 
ATOM   908  C  CB  . SER A 1 120 ? 92.380  -1.817  33.136  1.00 13.54 ? 122  SER A CB  1 
ATOM   909  O  OG  . SER A 1 120 ? 93.300  -0.955  33.783  1.00 12.82 ? 122  SER A OG  1 
ATOM   910  N  N   . ASP A 1 121 ? 94.207  -0.710  30.950  1.00 17.35 ? 123  ASP A N   1 
ATOM   911  C  CA  . ASP A 1 121 ? 95.313  -0.808  30.013  1.00 18.75 ? 123  ASP A CA  1 
ATOM   912  C  C   . ASP A 1 121 ? 96.232  -1.980  30.332  1.00 17.70 ? 123  ASP A C   1 
ATOM   913  O  O   . ASP A 1 121 ? 97.088  -2.335  29.530  1.00 18.24 ? 123  ASP A O   1 
ATOM   914  C  CB  . ASP A 1 121 ? 96.080  0.509   29.920  1.00 20.29 ? 123  ASP A CB  1 
ATOM   915  C  CG  . ASP A 1 121 ? 95.344  1.546   29.089  1.00 21.98 ? 123  ASP A CG  1 
ATOM   916  O  OD1 . ASP A 1 121 ? 94.607  1.147   28.157  1.00 18.90 ? 123  ASP A OD1 1 
ATOM   917  O  OD2 . ASP A 1 121 ? 95.470  2.752   29.389  1.00 22.68 ? 123  ASP A OD2 1 
ATOM   918  N  N   . THR A 1 122 ? 95.996  -2.626  31.470  1.00 18.27 ? 124  THR A N   1 
ATOM   919  C  CA  . THR A 1 122 ? 96.677  -3.879  31.785  1.00 17.92 ? 124  THR A CA  1 
ATOM   920  C  C   . THR A 1 122 ? 95.717  -4.917  32.360  1.00 17.87 ? 124  THR A C   1 
ATOM   921  O  O   . THR A 1 122 ? 94.720  -4.572  32.996  1.00 18.55 ? 124  THR A O   1 
ATOM   922  C  CB  . THR A 1 122 ? 97.835  -3.671  32.780  1.00 18.65 ? 124  THR A CB  1 
ATOM   923  O  OG1 . THR A 1 122 ? 97.313  -3.581  34.110  1.00 19.15 ? 124  THR A OG1 1 
ATOM   924  C  CG2 . THR A 1 122 ? 98.612  -2.404  32.451  1.00 19.54 ? 124  THR A CG2 1 
ATOM   925  N  N   . THR A 1 123 ? 96.040  -6.192  32.170  1.00 17.03 ? 125  THR A N   1 
ATOM   926  C  CA  . THR A 1 123 ? 95.219  -7.260  32.723  1.00 17.50 ? 125  THR A CA  1 
ATOM   927  C  C   . THR A 1 123 ? 95.434  -7.424  34.226  1.00 17.03 ? 125  THR A C   1 
ATOM   928  O  O   . THR A 1 123 ? 94.562  -7.930  34.926  1.00 15.88 ? 125  THR A O   1 
ATOM   929  C  CB  . THR A 1 123 ? 95.450  -8.601  32.004  1.00 18.37 ? 125  THR A CB  1 
ATOM   930  O  OG1 . THR A 1 123 ? 96.815  -9.000  32.155  1.00 19.83 ? 125  THR A OG1 1 
ATOM   931  C  CG2 . THR A 1 123 ? 95.127  -8.475  30.522  1.00 18.15 ? 125  THR A CG2 1 
ATOM   932  N  N   . ASP A 1 124 ? 96.580  -6.966  34.724  1.00 16.72 ? 126  ASP A N   1 
ATOM   933  C  CA  . ASP A 1 124 ? 96.838  -6.973  36.165  1.00 17.69 ? 126  ASP A CA  1 
ATOM   934  C  C   . ASP A 1 124 ? 95.836  -6.096  36.904  1.00 15.54 ? 126  ASP A C   1 
ATOM   935  O  O   . ASP A 1 124 ? 95.329  -6.473  37.957  1.00 15.62 ? 126  ASP A O   1 
ATOM   936  C  CB  . ASP A 1 124 ? 98.263  -6.500  36.472  1.00 19.35 ? 126  ASP A CB  1 
ATOM   937  C  CG  . ASP A 1 124 ? 99.282  -7.620  36.395  1.00 21.21 ? 126  ASP A CG  1 
ATOM   938  O  OD1 . ASP A 1 124 ? 98.901  -8.756  36.043  1.00 23.12 ? 126  ASP A OD1 1 
ATOM   939  O  OD2 . ASP A 1 124 ? 100.466 -7.369  36.708  1.00 22.75 ? 126  ASP A OD2 1 
ATOM   940  N  N   . LEU A 1 125 ? 95.572  -4.910  36.364  1.00 15.82 ? 127  LEU A N   1 
ATOM   941  C  CA  . LEU A 1 125 ? 94.610  -4.000  36.978  1.00 15.00 ? 127  LEU A CA  1 
ATOM   942  C  C   . LEU A 1 125 ? 93.197  -4.580  36.954  1.00 14.55 ? 127  LEU A C   1 
ATOM   943  O  O   . LEU A 1 125 ? 92.469  -4.509  37.943  1.00 14.27 ? 127  LEU A O   1 
ATOM   944  C  CB  . LEU A 1 125 ? 94.650  -2.627  36.304  1.00 14.90 ? 127  LEU A CB  1 
ATOM   945  C  CG  . LEU A 1 125 ? 95.917  -1.809  36.572  1.00 14.99 ? 127  LEU A CG  1 
ATOM   946  C  CD1 . LEU A 1 125 ? 95.978  -0.579  35.678  1.00 15.50 ? 127  LEU A CD1 1 
ATOM   947  C  CD2 . LEU A 1 125 ? 96.013  -1.419  38.040  1.00 14.97 ? 127  LEU A CD2 1 
ATOM   948  N  N   . ILE A 1 126 ? 92.834  -5.205  35.839  1.00 13.62 ? 128  ILE A N   1 
ATOM   949  C  CA  . ILE A 1 126 ? 91.554  -5.898  35.741  1.00 13.05 ? 128  ILE A CA  1 
ATOM   950  C  C   . ILE A 1 126 ? 91.441  -7.000  36.795  1.00 13.20 ? 128  ILE A C   1 
ATOM   951  O  O   . ILE A 1 126 ? 90.454  -7.077  37.523  1.00 12.19 ? 128  ILE A O   1 
ATOM   952  C  CB  . ILE A 1 126 ? 91.345  -6.501  34.336  1.00 12.43 ? 128  ILE A CB  1 
ATOM   953  C  CG1 . ILE A 1 126 ? 91.142  -5.381  33.312  1.00 12.34 ? 128  ILE A CG1 1 
ATOM   954  C  CG2 . ILE A 1 126 ? 90.163  -7.463  34.335  1.00 12.20 ? 128  ILE A CG2 1 
ATOM   955  C  CD1 . ILE A 1 126 ? 90.832  -5.867  31.913  1.00 12.38 ? 128  ILE A CD1 1 
ATOM   956  N  N   . ASP A 1 127 ? 92.469  -7.836  36.887  1.00 13.50 ? 129  ASP A N   1 
ATOM   957  C  CA  . ASP A 1 127 ? 92.430  -8.989  37.777  1.00 14.84 ? 129  ASP A CA  1 
ATOM   958  C  C   . ASP A 1 127 ? 92.264  -8.575  39.236  1.00 13.62 ? 129  ASP A C   1 
ATOM   959  O  O   . ASP A 1 127 ? 91.579  -9.248  40.003  1.00 13.28 ? 129  ASP A O   1 
ATOM   960  C  CB  . ASP A 1 127 ? 93.681  -9.853  37.607  1.00 17.01 ? 129  ASP A CB  1 
ATOM   961  C  CG  . ASP A 1 127 ? 93.645  -10.692 36.341  1.00 19.79 ? 129  ASP A CG  1 
ATOM   962  O  OD1 . ASP A 1 127 ? 92.549  -10.873 35.770  1.00 22.80 ? 129  ASP A OD1 1 
ATOM   963  O  OD2 . ASP A 1 127 ? 94.714  -11.183 35.924  1.00 23.38 ? 129  ASP A OD2 1 
ATOM   964  N  N   . GLN A 1 128 ? 92.896  -7.473  39.623  1.00 12.92 ? 130  GLN A N   1 
ATOM   965  C  CA  . GLN A 1 128 ? 92.810  -7.021  41.004  1.00 13.97 ? 130  GLN A CA  1 
ATOM   966  C  C   . GLN A 1 128 ? 91.426  -6.451  41.293  1.00 13.71 ? 130  GLN A C   1 
ATOM   967  O  O   . GLN A 1 128 ? 90.895  -6.607  42.391  1.00 12.63 ? 130  GLN A O   1 
ATOM   968  C  CB  . GLN A 1 128 ? 93.889  -5.982  41.309  1.00 13.44 ? 130  GLN A CB  1 
ATOM   969  C  CG  . GLN A 1 128 ? 94.084  -5.731  42.795  1.00 13.84 ? 130  GLN A CG  1 
ATOM   970  C  CD  . GLN A 1 128 ? 94.495  -6.983  43.549  1.00 14.70 ? 130  GLN A CD  1 
ATOM   971  O  OE1 . GLN A 1 128 ? 95.391  -7.716  43.121  1.00 14.44 ? 130  GLN A OE1 1 
ATOM   972  N  NE2 . GLN A 1 128 ? 93.854  -7.225  44.689  1.00 13.87 ? 130  GLN A NE2 1 
ATOM   973  N  N   . GLN A 1 129 ? 90.840  -5.814  40.285  1.00 13.17 ? 131  GLN A N   1 
ATOM   974  C  CA  . GLN A 1 129 ? 89.486  -5.279  40.395  1.00 14.50 ? 131  GLN A CA  1 
ATOM   975  C  C   . GLN A 1 129 ? 88.470  -6.409  40.544  1.00 13.43 ? 131  GLN A C   1 
ATOM   976  O  O   . GLN A 1 129 ? 87.543  -6.316  41.346  1.00 13.80 ? 131  GLN A O   1 
ATOM   977  C  CB  . GLN A 1 129 ? 89.159  -4.408  39.177  1.00 15.33 ? 131  GLN A CB  1 
ATOM   978  C  CG  . GLN A 1 129 ? 87.804  -3.720  39.234  1.00 17.41 ? 131  GLN A CG  1 
ATOM   979  C  CD  . GLN A 1 129 ? 87.674  -2.770  40.408  1.00 20.12 ? 131  GLN A CD  1 
ATOM   980  O  OE1 . GLN A 1 129 ? 86.867  -2.990  41.311  1.00 24.90 ? 131  GLN A OE1 1 
ATOM   981  N  NE2 . GLN A 1 129 ? 88.480  -1.714  40.409  1.00 21.41 ? 131  GLN A NE2 1 
ATOM   982  N  N   . VAL A 1 130 ? 88.683  -7.501  39.814  1.00 13.48 ? 132  VAL A N   1 
ATOM   983  C  CA  . VAL A 1 130 ? 87.868  -8.702  39.988  1.00 13.30 ? 132  VAL A CA  1 
ATOM   984  C  C   . VAL A 1 130 ? 87.993  -9.257  41.405  1.00 13.51 ? 132  VAL A C   1 
ATOM   985  O  O   . VAL A 1 130 ? 86.993  -9.562  42.043  1.00 13.01 ? 132  VAL A O   1 
ATOM   986  C  CB  . VAL A 1 130 ? 88.241  -9.807  38.983  1.00 13.29 ? 132  VAL A CB  1 
ATOM   987  C  CG1 . VAL A 1 130 ? 87.474  -11.084 39.296  1.00 13.29 ? 132  VAL A CG1 1 
ATOM   988  C  CG2 . VAL A 1 130 ? 87.953  -9.349  37.561  1.00 13.54 ? 132  VAL A CG2 1 
ATOM   989  N  N   . ALA A 1 131 ? 89.225  -9.404  41.885  1.00 13.04 ? 133  ALA A N   1 
ATOM   990  C  CA  . ALA A 1 131 ? 89.457  -9.877  43.249  1.00 13.98 ? 133  ALA A CA  1 
ATOM   991  C  C   . ALA A 1 131 ? 88.712  -9.015  44.266  1.00 14.37 ? 133  ALA A C   1 
ATOM   992  O  O   . ALA A 1 131 ? 88.102  -9.530  45.200  1.00 15.49 ? 133  ALA A O   1 
ATOM   993  C  CB  . ALA A 1 131 ? 90.949  -9.893  43.559  1.00 13.13 ? 133  ALA A CB  1 
ATOM   994  N  N   . SER A 1 132 ? 88.779  -7.699  44.088  1.00 14.66 ? 134  SER A N   1 
ATOM   995  C  CA  . SER A 1 132 ? 88.090  -6.773  44.980  1.00 16.50 ? 134  SER A CA  1 
ATOM   996  C  C   . SER A 1 132 ? 86.577  -6.977  44.919  1.00 15.77 ? 134  SER A C   1 
ATOM   997  O  O   . SER A 1 132 ? 85.906  -7.056  45.949  1.00 15.55 ? 134  SER A O   1 
ATOM   998  C  CB  . SER A 1 132 ? 88.446  -5.327  44.629  1.00 18.08 ? 134  SER A CB  1 
ATOM   999  O  OG  . SER A 1 132 ? 87.608  -4.419  45.321  1.00 22.33 ? 134  SER A OG  1 
ATOM   1000 N  N   . ILE A 1 133 ? 86.048  -7.102  43.707  1.00 14.49 ? 135  ILE A N   1 
ATOM   1001 C  CA  . ILE A 1 133 ? 84.617  -7.310  43.530  1.00 14.76 ? 135  ILE A CA  1 
ATOM   1002 C  C   . ILE A 1 133 ? 84.153  -8.615  44.173  1.00 14.90 ? 135  ILE A C   1 
ATOM   1003 O  O   . ILE A 1 133 ? 83.168  -8.633  44.909  1.00 16.24 ? 135  ILE A O   1 
ATOM   1004 C  CB  . ILE A 1 133 ? 84.213  -7.270  42.044  1.00 15.04 ? 135  ILE A CB  1 
ATOM   1005 C  CG1 . ILE A 1 133 ? 84.206  -5.823  41.541  1.00 14.05 ? 135  ILE A CG1 1 
ATOM   1006 C  CG2 . ILE A 1 133 ? 82.854  -7.928  41.845  1.00 14.28 ? 135  ILE A CG2 1 
ATOM   1007 C  CD1 . ILE A 1 133 ? 84.306  -5.693  40.034  1.00 13.88 ? 135  ILE A CD1 1 
ATOM   1008 N  N   . GLU A 1 134 ? 84.895  -9.694  43.939  1.00 14.52 ? 136  GLU A N   1 
ATOM   1009 C  CA  . GLU A 1 134 ? 84.545  -10.992 44.511  1.00 14.33 ? 136  GLU A CA  1 
ATOM   1010 C  C   . GLU A 1 134 ? 84.673  -10.983 46.033  1.00 14.56 ? 136  GLU A C   1 
ATOM   1011 O  O   . GLU A 1 134 ? 83.910  -11.649 46.730  1.00 14.50 ? 136  GLU A O   1 
ATOM   1012 C  CB  . GLU A 1 134 ? 85.401  -12.108 43.900  1.00 14.14 ? 136  GLU A CB  1 
ATOM   1013 C  CG  . GLU A 1 134 ? 85.161  -12.317 42.410  1.00 14.55 ? 136  GLU A CG  1 
ATOM   1014 C  CD  . GLU A 1 134 ? 85.879  -13.535 41.860  1.00 15.90 ? 136  GLU A CD  1 
ATOM   1015 O  OE1 . GLU A 1 134 ? 86.801  -14.042 42.534  1.00 15.99 ? 136  GLU A OE1 1 
ATOM   1016 O  OE2 . GLU A 1 134 ? 85.530  -13.980 40.745  1.00 17.47 ? 136  GLU A OE2 1 
ATOM   1017 N  N   . SER A 1 135 ? 85.599  -10.177 46.542  1.00 14.78 ? 137  SER A N   1 
ATOM   1018 C  CA  . SER A 1 135 ? 85.853  -10.119 47.978  1.00 16.71 ? 137  SER A CA  1 
ATOM   1019 C  C   . SER A 1 135 ? 84.763  -9.345  48.716  1.00 17.40 ? 137  SER A C   1 
ATOM   1020 O  O   . SER A 1 135 ? 84.386  -9.706  49.830  1.00 18.52 ? 137  SER A O   1 
ATOM   1021 C  CB  . SER A 1 135 ? 87.230  -9.510  48.264  1.00 16.64 ? 137  SER A CB  1 
ATOM   1022 O  OG  . SER A 1 135 ? 87.220  -8.100  48.099  1.00 18.00 ? 137  SER A OG  1 
ATOM   1023 N  N   . THR A 1 136 ? 84.240  -8.298  48.086  1.00 17.51 ? 138  THR A N   1 
ATOM   1024 C  CA  . THR A 1 136 ? 83.178  -7.507  48.704  1.00 19.54 ? 138  THR A CA  1 
ATOM   1025 C  C   . THR A 1 136 ? 81.814  -8.178  48.572  1.00 17.59 ? 138  THR A C   1 
ATOM   1026 O  O   . THR A 1 136 ? 81.033  -8.206  49.523  1.00 17.58 ? 138  THR A O   1 
ATOM   1027 C  CB  . THR A 1 136 ? 83.113  -6.071  48.141  1.00 21.86 ? 138  THR A CB  1 
ATOM   1028 O  OG1 . THR A 1 136 ? 82.738  -6.110  46.760  1.00 25.17 ? 138  THR A OG1 1 
ATOM   1029 C  CG2 . THR A 1 136 ? 84.461  -5.378  48.277  1.00 20.53 ? 138  THR A CG2 1 
ATOM   1030 N  N   . PHE A 1 137 ? 81.542  -8.746  47.401  1.00 16.38 ? 139  PHE A N   1 
ATOM   1031 C  CA  . PHE A 1 137 ? 80.264  -9.406  47.151  1.00 15.57 ? 139  PHE A CA  1 
ATOM   1032 C  C   . PHE A 1 137 ? 80.188  -10.761 47.839  1.00 16.63 ? 139  PHE A C   1 
ATOM   1033 O  O   . PHE A 1 137 ? 79.109  -11.212 48.217  1.00 15.93 ? 139  PHE A O   1 
ATOM   1034 C  CB  . PHE A 1 137 ? 80.023  -9.572  45.649  1.00 15.26 ? 139  PHE A CB  1 
ATOM   1035 C  CG  . PHE A 1 137 ? 79.427  -8.359  44.993  1.00 15.10 ? 139  PHE A CG  1 
ATOM   1036 C  CD1 . PHE A 1 137 ? 80.236  -7.328  44.545  1.00 15.10 ? 139  PHE A CD1 1 
ATOM   1037 C  CD2 . PHE A 1 137 ? 78.055  -8.243  44.841  1.00 14.54 ? 139  PHE A CD2 1 
ATOM   1038 C  CE1 . PHE A 1 137 ? 79.689  -6.206  43.948  1.00 15.44 ? 139  PHE A CE1 1 
ATOM   1039 C  CE2 . PHE A 1 137 ? 77.502  -7.131  44.233  1.00 14.62 ? 139  PHE A CE2 1 
ATOM   1040 C  CZ  . PHE A 1 137 ? 78.318  -6.106  43.797  1.00 14.45 ? 139  PHE A CZ  1 
ATOM   1041 N  N   . GLY A 1 138 ? 81.335  -11.422 47.971  1.00 17.48 ? 140  GLY A N   1 
ATOM   1042 C  CA  . GLY A 1 138 ? 81.386  -12.747 48.578  1.00 18.84 ? 140  GLY A CA  1 
ATOM   1043 C  C   . GLY A 1 138 ? 80.517  -13.756 47.854  1.00 19.07 ? 140  GLY A C   1 
ATOM   1044 O  O   . GLY A 1 138 ? 80.479  -13.794 46.624  1.00 19.34 ? 140  GLY A O   1 
ATOM   1045 N  N   . SER A 1 139 ? 79.784  -14.554 48.622  1.00 19.60 ? 141  SER A N   1 
ATOM   1046 C  CA  . SER A 1 139 ? 79.003  -15.650 48.062  1.00 19.15 ? 141  SER A CA  1 
ATOM   1047 C  C   . SER A 1 139 ? 77.719  -15.182 47.379  1.00 18.44 ? 141  SER A C   1 
ATOM   1048 O  O   . SER A 1 139 ? 76.981  -15.995 46.828  1.00 19.97 ? 141  SER A O   1 
ATOM   1049 C  CB  . SER A 1 139 ? 78.659  -16.660 49.157  1.00 21.71 ? 141  SER A CB  1 
ATOM   1050 O  OG  . SER A 1 139 ? 77.979  -16.020 50.224  1.00 23.88 ? 141  SER A OG  1 
ATOM   1051 N  N   . SER A 1 140 ? 77.429  -13.885 47.444  1.00 16.83 ? 142  SER A N   1 
ATOM   1052 C  CA  . SER A 1 140 ? 76.208  -13.359 46.829  1.00 17.36 ? 142  SER A CA  1 
ATOM   1053 C  C   . SER A 1 140 ? 76.325  -13.312 45.308  1.00 17.78 ? 142  SER A C   1 
ATOM   1054 O  O   . SER A 1 140 ? 75.330  -13.140 44.604  1.00 18.20 ? 142  SER A O   1 
ATOM   1055 C  CB  . SER A 1 140 ? 75.864  -11.974 47.380  1.00 16.33 ? 142  SER A CB  1 
ATOM   1056 O  OG  . SER A 1 140 ? 76.729  -10.980 46.854  1.00 17.59 ? 142  SER A OG  1 
ATOM   1057 N  N   . ILE A 1 141 ? 77.546  -13.474 44.810  1.00 16.88 ? 143  ILE A N   1 
ATOM   1058 C  CA  . ILE A 1 141 ? 77.799  -13.489 43.374  1.00 17.88 ? 143  ILE A CA  1 
ATOM   1059 C  C   . ILE A 1 141 ? 78.526  -14.772 42.985  1.00 18.49 ? 143  ILE A C   1 
ATOM   1060 O  O   . ILE A 1 141 ? 79.318  -15.304 43.765  1.00 18.17 ? 143  ILE A O   1 
ATOM   1061 C  CB  . ILE A 1 141 ? 78.642  -12.273 42.945  1.00 18.37 ? 143  ILE A CB  1 
ATOM   1062 C  CG1 . ILE A 1 141 ? 78.612  -12.099 41.427  1.00 19.32 ? 143  ILE A CG1 1 
ATOM   1063 C  CG2 . ILE A 1 141 ? 80.074  -12.406 43.442  1.00 19.46 ? 143  ILE A CG2 1 
ATOM   1064 C  CD1 . ILE A 1 141 ? 79.252  -10.810 40.956  1.00 19.50 ? 143  ILE A CD1 1 
ATOM   1065 N  N   . SER A 1 142 ? 78.200  -15.300 41.809  1.00 18.94 ? 144  SER A N   1 
ATOM   1066 C  CA  . SER A 1 142 ? 78.939  -16.421 41.234  1.00 18.72 ? 144  SER A CA  1 
ATOM   1067 C  C   . SER A 1 142 ? 79.388  -16.097 39.816  1.00 18.34 ? 144  SER A C   1 
ATOM   1068 O  O   . SER A 1 142 ? 78.591  -15.649 38.990  1.00 16.05 ? 144  SER A O   1 
ATOM   1069 C  CB  . SER A 1 142 ? 78.081  -17.688 41.219  1.00 19.69 ? 144  SER A CB  1 
ATOM   1070 O  OG  . SER A 1 142 ? 78.190  -18.392 42.443  1.00 22.53 ? 144  SER A OG  1 
ATOM   1071 N  N   . LYS A 1 143 ? 80.664  -16.335 39.537  1.00 17.63 ? 145  LYS A N   1 
ATOM   1072 C  CA  . LYS A 1 143 ? 81.182  -16.209 38.184  1.00 17.31 ? 145  LYS A CA  1 
ATOM   1073 C  C   . LYS A 1 143 ? 80.862  -17.469 37.389  1.00 16.69 ? 145  LYS A C   1 
ATOM   1074 O  O   . LYS A 1 143 ? 81.277  -18.567 37.761  1.00 17.24 ? 145  LYS A O   1 
ATOM   1075 C  CB  . LYS A 1 143 ? 82.693  -15.977 38.213  1.00 19.22 ? 145  LYS A CB  1 
ATOM   1076 C  CG  . LYS A 1 143 ? 83.358  -16.056 36.848  1.00 21.55 ? 145  LYS A CG  1 
ATOM   1077 C  CD  . LYS A 1 143 ? 84.858  -15.842 36.960  1.00 25.90 ? 145  LYS A CD  1 
ATOM   1078 C  CE  . LYS A 1 143 ? 85.603  -16.505 35.815  1.00 28.81 ? 145  LYS A CE  1 
ATOM   1079 N  NZ  . LYS A 1 143 ? 87.078  -16.352 35.970  1.00 32.01 ? 145  LYS A NZ  1 
ATOM   1080 N  N   . LEU A 1 144 ? 80.110  -17.313 36.305  1.00 13.89 ? 146  LEU A N   1 
ATOM   1081 C  CA  . LEU A 1 144 ? 79.690  -18.461 35.509  1.00 13.27 ? 146  LEU A CA  1 
ATOM   1082 C  C   . LEU A 1 144 ? 80.582  -18.642 34.288  1.00 12.27 ? 146  LEU A C   1 
ATOM   1083 O  O   . LEU A 1 144 ? 80.796  -19.759 33.830  1.00 11.71 ? 146  LEU A O   1 
ATOM   1084 C  CB  . LEU A 1 144 ? 78.231  -18.320 35.066  1.00 13.49 ? 146  LEU A CB  1 
ATOM   1085 C  CG  . LEU A 1 144 ? 77.145  -18.234 36.139  1.00 13.54 ? 146  LEU A CG  1 
ATOM   1086 C  CD1 . LEU A 1 144 ? 75.779  -18.201 35.472  1.00 13.51 ? 146  LEU A CD1 1 
ATOM   1087 C  CD2 . LEU A 1 144 ? 77.239  -19.403 37.108  1.00 14.74 ? 146  LEU A CD2 1 
ATOM   1088 N  N   . TYR A 1 145 ? 81.049  -17.529 33.733  1.00 11.98 ? 147  TYR A N   1 
ATOM   1089 C  CA  . TYR A 1 145 ? 81.874  -17.541 32.529  1.00 11.55 ? 147  TYR A CA  1 
ATOM   1090 C  C   . TYR A 1 145 ? 82.539  -16.181 32.402  1.00 12.02 ? 147  TYR A C   1 
ATOM   1091 O  O   . TYR A 1 145 ? 82.036  -15.183 32.922  1.00 11.88 ? 147  TYR A O   1 
ATOM   1092 C  CB  . TYR A 1 145 ? 81.015  -17.816 31.286  1.00 11.27 ? 147  TYR A CB  1 
ATOM   1093 C  CG  . TYR A 1 145 ? 81.793  -17.856 29.980  1.00 10.77 ? 147  TYR A CG  1 
ATOM   1094 C  CD1 . TYR A 1 145 ? 82.820  -18.775 29.787  1.00 10.89 ? 147  TYR A CD1 1 
ATOM   1095 C  CD2 . TYR A 1 145 ? 81.472  -17.006 28.926  1.00 11.25 ? 147  TYR A CD2 1 
ATOM   1096 C  CE1 . TYR A 1 145 ? 83.514  -18.834 28.590  1.00 11.32 ? 147  TYR A CE1 1 
ATOM   1097 C  CE2 . TYR A 1 145 ? 82.177  -17.041 27.733  1.00 10.83 ? 147  TYR A CE2 1 
ATOM   1098 C  CZ  . TYR A 1 145 ? 83.194  -17.961 27.567  1.00 11.49 ? 147  TYR A CZ  1 
ATOM   1099 O  OH  . TYR A 1 145 ? 83.893  -18.011 26.376  1.00 11.70 ? 147  TYR A OH  1 
ATOM   1100 N  N   . SER A 1 146 ? 83.683  -16.141 31.735  1.00 11.96 ? 148  SER A N   1 
ATOM   1101 C  CA  . SER A 1 146 ? 84.294  -14.866 31.404  1.00 12.48 ? 148  SER A CA  1 
ATOM   1102 C  C   . SER A 1 146 ? 85.043  -14.958 30.086  1.00 12.28 ? 148  SER A C   1 
ATOM   1103 O  O   . SER A 1 146 ? 85.424  -16.044 29.651  1.00 11.97 ? 148  SER A O   1 
ATOM   1104 C  CB  . SER A 1 146 ? 85.232  -14.408 32.523  1.00 12.80 ? 148  SER A CB  1 
ATOM   1105 O  OG  . SER A 1 146 ? 86.386  -15.226 32.581  1.00 13.30 ? 148  SER A OG  1 
ATOM   1106 N  N   . LEU A 1 147 ? 85.217  -13.813 29.439  1.00 11.25 ? 149  LEU A N   1 
ATOM   1107 C  CA  . LEU A 1 147 ? 85.982  -13.745 28.207  1.00 10.86 ? 149  LEU A CA  1 
ATOM   1108 C  C   . LEU A 1 147 ? 86.933  -12.553 28.243  1.00 10.99 ? 149  LEU A C   1 
ATOM   1109 O  O   . LEU A 1 147 ? 86.505  -11.416 28.445  1.00 10.95 ? 149  LEU A O   1 
ATOM   1110 C  CB  . LEU A 1 147 ? 85.038  -13.644 27.007  1.00 10.60 ? 149  LEU A CB  1 
ATOM   1111 C  CG  . LEU A 1 147 ? 85.700  -13.668 25.628  1.00 10.20 ? 149  LEU A CG  1 
ATOM   1112 C  CD1 . LEU A 1 147 ? 86.438  -14.980 25.413  1.00 9.60  ? 149  LEU A CD1 1 
ATOM   1113 C  CD2 . LEU A 1 147 ? 84.677  -13.432 24.527  1.00 10.08 ? 149  LEU A CD2 1 
ATOM   1114 N  N   . SER A 1 148 ? 88.225  -12.824 28.076  1.00 10.87 ? 150  SER A N   1 
ATOM   1115 C  CA  . SER A 1 148 ? 89.235  -11.769 27.984  1.00 11.25 ? 150  SER A CA  1 
ATOM   1116 C  C   . SER A 1 148 ? 89.414  -11.306 26.543  1.00 11.95 ? 150  SER A C   1 
ATOM   1117 O  O   . SER A 1 148 ? 89.439  -12.119 25.620  1.00 13.64 ? 150  SER A O   1 
ATOM   1118 C  CB  . SER A 1 148 ? 90.576  -12.260 28.539  1.00 11.93 ? 150  SER A CB  1 
ATOM   1119 O  OG  . SER A 1 148 ? 90.471  -12.592 29.913  1.00 12.58 ? 150  SER A OG  1 
ATOM   1120 N  N   . ALA A 1 149 ? 89.533  -9.996  26.356  1.00 11.41 ? 151  ALA A N   1 
ATOM   1121 C  CA  . ALA A 1 149 ? 89.703  -9.412  25.032  1.00 10.82 ? 151  ALA A CA  1 
ATOM   1122 C  C   . ALA A 1 149 ? 90.790  -8.342  25.089  1.00 10.73 ? 151  ALA A C   1 
ATOM   1123 O  O   . ALA A 1 149 ? 91.129  -7.848  26.162  1.00 10.50 ? 151  ALA A O   1 
ATOM   1124 C  CB  . ALA A 1 149 ? 88.392  -8.803  24.554  1.00 10.37 ? 151  ALA A CB  1 
ATOM   1125 N  N   A SER A 1 150 ? 91.309  -7.961  23.929  0.50 11.28 ? 152  SER A N   1 
ATOM   1126 N  N   B SER A 1 150 ? 91.355  -8.012  23.933  0.50 10.53 ? 152  SER A N   1 
ATOM   1127 C  CA  A SER A 1 150 ? 92.311  -6.905  23.866  0.50 11.78 ? 152  SER A CA  1 
ATOM   1128 C  CA  B SER A 1 150 ? 92.408  -7.006  23.862  0.50 10.77 ? 152  SER A CA  1 
ATOM   1129 C  C   A SER A 1 150 ? 92.387  -6.281  22.482  0.50 11.89 ? 152  SER A C   1 
ATOM   1130 C  C   B SER A 1 150 ? 92.454  -6.349  22.490  0.50 10.95 ? 152  SER A C   1 
ATOM   1131 O  O   A SER A 1 150 ? 92.123  -6.940  21.477  0.50 11.93 ? 152  SER A O   1 
ATOM   1132 O  O   B SER A 1 150 ? 92.153  -6.980  21.478  0.50 11.07 ? 152  SER A O   1 
ATOM   1133 C  CB  A SER A 1 150 ? 93.682  -7.446  24.270  0.50 12.47 ? 152  SER A CB  1 
ATOM   1134 C  CB  B SER A 1 150 ? 93.768  -7.627  24.193  0.50 11.22 ? 152  SER A CB  1 
ATOM   1135 O  OG  A SER A 1 150 ? 93.870  -8.760  23.777  0.50 14.14 ? 152  SER A OG  1 
ATOM   1136 O  OG  B SER A 1 150 ? 94.817  -6.684  24.040  0.50 10.14 ? 152  SER A OG  1 
ATOM   1137 N  N   A ILE A 1 151 ? 92.737  -5.001  22.440  0.50 12.17 ? 153  ILE A N   1 
ATOM   1138 N  N   B ILE A 1 151 ? 92.813  -5.070  22.468  0.50 11.21 ? 153  ILE A N   1 
ATOM   1139 C  CA  A ILE A 1 151 ? 93.211  -4.390  21.210  0.50 12.68 ? 153  ILE A CA  1 
ATOM   1140 C  CA  B ILE A 1 151 ? 93.219  -4.416  21.233  0.50 11.68 ? 153  ILE A CA  1 
ATOM   1141 C  C   A ILE A 1 151 ? 94.394  -5.201  20.692  0.50 12.73 ? 153  ILE A C   1 
ATOM   1142 C  C   B ILE A 1 151 ? 94.455  -5.123  20.685  0.50 12.28 ? 153  ILE A C   1 
ATOM   1143 O  O   A ILE A 1 151 ? 95.174  -5.742  21.476  0.50 12.50 ? 153  ILE A O   1 
ATOM   1144 O  O   B ILE A 1 151 ? 95.334  -5.526  21.448  0.50 12.39 ? 153  ILE A O   1 
ATOM   1145 C  CB  A ILE A 1 151 ? 93.652  -2.933  21.444  0.50 12.95 ? 153  ILE A CB  1 
ATOM   1146 C  CB  B ILE A 1 151 ? 93.534  -2.928  21.472  0.50 11.75 ? 153  ILE A CB  1 
ATOM   1147 C  CG1 A ILE A 1 151 ? 92.601  -2.186  22.270  0.50 13.54 ? 153  ILE A CG1 1 
ATOM   1148 C  CG1 B ILE A 1 151 ? 92.282  -2.195  21.963  0.50 11.84 ? 153  ILE A CG1 1 
ATOM   1149 C  CG2 A ILE A 1 151 ? 93.897  -2.228  20.119  0.50 13.00 ? 153  ILE A CG2 1 
ATOM   1150 C  CG2 B ILE A 1 151 ? 94.078  -2.284  20.205  0.50 11.79 ? 153  ILE A CG2 1 
ATOM   1151 C  CD1 A ILE A 1 151 ? 91.310  -1.920  21.528  0.50 14.67 ? 153  ILE A CD1 1 
ATOM   1152 C  CD1 B ILE A 1 151 ? 92.490  -0.717  22.216  0.50 12.43 ? 153  ILE A CD1 1 
ATOM   1153 N  N   . ARG A 1 152 ? 94.489  -5.333  19.373  1.00 11.97 ? 154  ARG A N   1 
ATOM   1154 C  CA  . ARG A 1 152 ? 95.560  -6.111  18.766  1.00 12.39 ? 154  ARG A CA  1 
ATOM   1155 C  C   . ARG A 1 152 ? 96.871  -5.324  18.787  1.00 13.59 ? 154  ARG A C   1 
ATOM   1156 O  O   . ARG A 1 152 ? 96.862  -4.109  18.991  1.00 13.63 ? 154  ARG A O   1 
ATOM   1157 C  CB  . ARG A 1 152 ? 95.177  -6.553  17.352  1.00 11.74 ? 154  ARG A CB  1 
ATOM   1158 C  CG  . ARG A 1 152 ? 94.033  -7.561  17.329  1.00 11.68 ? 154  ARG A CG  1 
ATOM   1159 C  CD  . ARG A 1 152 ? 93.807  -8.133  15.939  1.00 11.78 ? 154  ARG A CD  1 
ATOM   1160 N  NE  . ARG A 1 152 ? 95.029  -8.711  15.395  1.00 12.40 ? 154  ARG A NE  1 
ATOM   1161 C  CZ  . ARG A 1 152 ? 95.428  -8.569  14.136  1.00 13.54 ? 154  ARG A CZ  1 
ATOM   1162 N  NH1 . ARG A 1 152 ? 94.700  -7.858  13.280  1.00 12.98 ? 154  ARG A NH1 1 
ATOM   1163 N  NH2 . ARG A 1 152 ? 96.576  -9.104  13.746  1.00 13.81 ? 154  ARG A NH2 1 
ATOM   1164 N  N   . PRO A 1 153 ? 98.008  -6.028  18.674  1.00 14.91 ? 155  PRO A N   1 
ATOM   1165 C  CA  . PRO A 1 153 ? 99.287  -5.390  18.989  1.00 17.17 ? 155  PRO A CA  1 
ATOM   1166 C  C   . PRO A 1 153 ? 99.837  -4.526  17.856  1.00 17.92 ? 155  PRO A C   1 
ATOM   1167 O  O   . PRO A 1 153 ? 99.495  -4.728  16.687  1.00 17.24 ? 155  PRO A O   1 
ATOM   1168 C  CB  . PRO A 1 153 ? 100.219 -6.575  19.261  1.00 16.82 ? 155  PRO A CB  1 
ATOM   1169 C  CG  . PRO A 1 153 ? 99.601  -7.723  18.541  1.00 17.16 ? 155  PRO A CG  1 
ATOM   1170 C  CD  . PRO A 1 153 ? 98.121  -7.494  18.600  1.00 16.30 ? 155  PRO A CD  1 
ATOM   1171 N  N   . GLY A 1 154 ? 100.663 -3.551  18.219  1.00 18.48 ? 156  GLY A N   1 
ATOM   1172 C  CA  . GLY A 1 154 ? 101.468 -2.821  17.248  1.00 20.92 ? 156  GLY A CA  1 
ATOM   1173 C  C   . GLY A 1 154 ? 100.643 -2.091  16.208  1.00 21.36 ? 156  GLY A C   1 
ATOM   1174 O  O   . GLY A 1 154 ? 99.725  -1.343  16.541  1.00 22.51 ? 156  GLY A O   1 
ATOM   1175 N  N   . ASN A 1 155 ? 100.974 -2.316  14.942  1.00 23.48 ? 157  ASN A N   1 
ATOM   1176 C  CA  . ASN A 1 155 ? 100.324 -1.617  13.841  1.00 24.55 ? 157  ASN A CA  1 
ATOM   1177 C  C   . ASN A 1 155 ? 98.930  -2.165  13.562  1.00 21.32 ? 157  ASN A C   1 
ATOM   1178 O  O   . ASN A 1 155 ? 98.164  -1.582  12.795  1.00 22.03 ? 157  ASN A O   1 
ATOM   1179 C  CB  . ASN A 1 155 ? 101.185 -1.697  12.579  1.00 26.98 ? 157  ASN A CB  1 
ATOM   1180 C  CG  . ASN A 1 155 ? 102.476 -0.911  12.706  1.00 32.06 ? 157  ASN A CG  1 
ATOM   1181 O  OD1 . ASN A 1 155 ? 102.550 0.066   13.452  1.00 34.21 ? 157  ASN A OD1 1 
ATOM   1182 N  ND2 . ASN A 1 155 ? 103.501 -1.331  11.973  1.00 35.24 ? 157  ASN A ND2 1 
ATOM   1183 N  N   . GLU A 1 156 ? 98.601  -3.283  14.197  1.00 19.17 ? 158  GLU A N   1 
ATOM   1184 C  CA  . GLU A 1 156 ? 97.280  -3.878  14.046  1.00 17.26 ? 158  GLU A CA  1 
ATOM   1185 C  C   . GLU A 1 156 ? 96.302  -3.383  15.107  1.00 15.07 ? 158  GLU A C   1 
ATOM   1186 O  O   . GLU A 1 156 ? 95.163  -3.836  15.163  1.00 13.71 ? 158  GLU A O   1 
ATOM   1187 C  CB  . GLU A 1 156 ? 97.366  -5.406  14.065  1.00 17.00 ? 158  GLU A CB  1 
ATOM   1188 C  CG  . GLU A 1 156 ? 98.075  -6.004  12.857  1.00 18.51 ? 158  GLU A CG  1 
ATOM   1189 C  CD  . GLU A 1 156 ? 97.278  -5.863  11.570  1.00 19.78 ? 158  GLU A CD  1 
ATOM   1190 O  OE1 . GLU A 1 156 ? 96.054  -6.098  11.589  1.00 18.90 ? 158  GLU A OE1 1 
ATOM   1191 O  OE2 . GLU A 1 156 ? 97.879  -5.536  10.527  1.00 21.03 ? 158  GLU A OE2 1 
ATOM   1192 N  N   . ALA A 1 157 ? 96.743  -2.449  15.947  1.00 14.83 ? 159  ALA A N   1 
ATOM   1193 C  CA  . ALA A 1 157 ? 95.834  -1.825  16.907  1.00 14.66 ? 159  ALA A CA  1 
ATOM   1194 C  C   . ALA A 1 157 ? 94.656  -1.174  16.186  1.00 14.50 ? 159  ALA A C   1 
ATOM   1195 O  O   . ALA A 1 157 ? 94.841  -0.354  15.283  1.00 13.73 ? 159  ALA A O   1 
ATOM   1196 C  CB  . ALA A 1 157 ? 96.567  -0.804  17.766  1.00 14.57 ? 159  ALA A CB  1 
ATOM   1197 N  N   . GLY A 1 158 ? 93.444  -1.543  16.587  1.00 12.93 ? 160  GLY A N   1 
ATOM   1198 C  CA  . GLY A 1 158 ? 92.241  -1.021  15.948  1.00 12.57 ? 160  GLY A CA  1 
ATOM   1199 C  C   . GLY A 1 158 ? 91.733  -1.927  14.842  1.00 12.88 ? 160  GLY A C   1 
ATOM   1200 O  O   . GLY A 1 158 ? 90.630  -1.737  14.331  1.00 13.20 ? 160  GLY A O   1 
ATOM   1201 N  N   . HIS A 1 159 ? 92.529  -2.930  14.487  1.00 12.28 ? 161  HIS A N   1 
ATOM   1202 C  CA  . HIS A 1 159 ? 92.110  -3.927  13.502  1.00 12.78 ? 161  HIS A CA  1 
ATOM   1203 C  C   . HIS A 1 159 ? 91.535  -5.161  14.201  1.00 11.86 ? 161  HIS A C   1 
ATOM   1204 O  O   . HIS A 1 159 ? 91.954  -5.513  15.301  1.00 12.16 ? 161  HIS A O   1 
ATOM   1205 C  CB  . HIS A 1 159 ? 93.292  -4.320  12.608  1.00 12.93 ? 161  HIS A CB  1 
ATOM   1206 C  CG  . HIS A 1 159 ? 93.879  -3.174  11.843  1.00 13.30 ? 161  HIS A CG  1 
ATOM   1207 N  ND1 . HIS A 1 159 ? 93.902  -3.133  10.466  1.00 13.86 ? 161  HIS A ND1 1 
ATOM   1208 C  CD2 . HIS A 1 159 ? 94.460  -2.023  12.262  1.00 13.43 ? 161  HIS A CD2 1 
ATOM   1209 C  CE1 . HIS A 1 159 ? 94.466  -2.005  10.069  1.00 14.00 ? 161  HIS A CE1 1 
ATOM   1210 N  NE2 . HIS A 1 159 ? 94.820  -1.317  11.139  1.00 13.71 ? 161  HIS A NE2 1 
ATOM   1211 N  N   . GLU A 1 160 ? 90.556  -5.807  13.578  1.00 12.23 ? 162  GLU A N   1 
ATOM   1212 C  CA  . GLU A 1 160 ? 90.069  -7.076  14.110  1.00 11.95 ? 162  GLU A CA  1 
ATOM   1213 C  C   . GLU A 1 160 ? 90.886  -8.240  13.553  1.00 11.23 ? 162  GLU A C   1 
ATOM   1214 O  O   . GLU A 1 160 ? 91.880  -8.025  12.856  1.00 10.60 ? 162  GLU A O   1 
ATOM   1215 C  CB  . GLU A 1 160 ? 88.569  -7.254  13.865  1.00 12.26 ? 162  GLU A CB  1 
ATOM   1216 C  CG  . GLU A 1 160 ? 88.142  -7.062  12.425  1.00 13.26 ? 162  GLU A CG  1 
ATOM   1217 C  CD  . GLU A 1 160 ? 88.725  -8.121  11.519  1.00 13.39 ? 162  GLU A CD  1 
ATOM   1218 O  OE1 . GLU A 1 160 ? 88.385  -9.310  11.704  1.00 15.18 ? 162  GLU A OE1 1 
ATOM   1219 O  OE2 . GLU A 1 160 ? 89.542  -7.767  10.643  1.00 13.68 ? 162  GLU A OE2 1 
ATOM   1220 N  N   . MET A 1 161 ? 90.519  -9.464  13.922  1.00 11.04 ? 163  MET A N   1 
ATOM   1221 C  CA  . MET A 1 161 ? 91.410  -10.605 13.723  1.00 10.99 ? 163  MET A CA  1 
ATOM   1222 C  C   . MET A 1 161 ? 91.661  -10.936 12.249  1.00 10.70 ? 163  MET A C   1 
ATOM   1223 O  O   . MET A 1 161 ? 92.680  -11.539 11.917  1.00 10.91 ? 163  MET A O   1 
ATOM   1224 C  CB  . MET A 1 161 ? 90.914  -11.837 14.487  1.00 11.19 ? 163  MET A CB  1 
ATOM   1225 C  CG  . MET A 1 161 ? 91.263  -11.837 15.974  1.00 11.40 ? 163  MET A CG  1 
ATOM   1226 S  SD  . MET A 1 161 ? 93.029  -12.026 16.294  1.00 12.63 ? 163  MET A SD  1 
ATOM   1227 C  CE  . MET A 1 161 ? 93.101  -11.890 18.083  1.00 11.41 ? 163  MET A CE  1 
ATOM   1228 N  N   . PHE A 1 162 ? 90.732  -10.564 11.371  1.00 11.08 ? 164  PHE A N   1 
ATOM   1229 C  CA  . PHE A 1 162 ? 90.927  -10.785 9.935   1.00 11.05 ? 164  PHE A CA  1 
ATOM   1230 C  C   . PHE A 1 162 ? 91.925  -9.787  9.357   1.00 11.20 ? 164  PHE A C   1 
ATOM   1231 O  O   . PHE A 1 162 ? 92.396  -9.958  8.232   1.00 12.71 ? 164  PHE A O   1 
ATOM   1232 C  CB  . PHE A 1 162 ? 89.607  -10.680 9.160   1.00 10.93 ? 164  PHE A CB  1 
ATOM   1233 C  CG  . PHE A 1 162 ? 88.722  -11.889 9.282   1.00 10.30 ? 164  PHE A CG  1 
ATOM   1234 C  CD1 . PHE A 1 162 ? 89.263  -13.156 9.440   1.00 10.14 ? 164  PHE A CD1 1 
ATOM   1235 C  CD2 . PHE A 1 162 ? 87.346  -11.760 9.190   1.00 10.28 ? 164  PHE A CD2 1 
ATOM   1236 C  CE1 . PHE A 1 162 ? 88.443  -14.261 9.573   1.00 9.93  ? 164  PHE A CE1 1 
ATOM   1237 C  CE2 . PHE A 1 162 ? 86.521  -12.864 9.300   1.00 10.18 ? 164  PHE A CE2 1 
ATOM   1238 C  CZ  . PHE A 1 162 ? 87.071  -14.116 9.493   1.00 9.98  ? 164  PHE A CZ  1 
ATOM   1239 N  N   . GLY A 1 163 ? 92.175  -8.703  10.088  1.00 11.00 ? 165  GLY A N   1 
ATOM   1240 C  CA  . GLY A 1 163 ? 93.169  -7.713  9.674   1.00 11.46 ? 165  GLY A CA  1 
ATOM   1241 C  C   . GLY A 1 163 ? 92.602  -6.354  9.301   1.00 11.20 ? 165  GLY A C   1 
ATOM   1242 O  O   . GLY A 1 163 ? 93.348  -5.434  8.963   1.00 11.33 ? 165  GLY A O   1 
ATOM   1243 N  N   . PHE A 1 164 ? 91.282  -6.215  9.380   1.00 10.25 ? 166  PHE A N   1 
ATOM   1244 C  CA  . PHE A 1 164 ? 90.614  -5.019  8.873   1.00 9.67  ? 166  PHE A CA  1 
ATOM   1245 C  C   . PHE A 1 164 ? 90.441  -3.977  9.969   1.00 10.09 ? 166  PHE A C   1 
ATOM   1246 O  O   . PHE A 1 164 ? 90.092  -4.317  11.098  1.00 10.04 ? 166  PHE A O   1 
ATOM   1247 C  CB  . PHE A 1 164 ? 89.253  -5.382  8.277   1.00 9.36  ? 166  PHE A CB  1 
ATOM   1248 C  CG  . PHE A 1 164 ? 89.345  -6.195  7.019   1.00 9.08  ? 166  PHE A CG  1 
ATOM   1249 C  CD1 . PHE A 1 164 ? 89.592  -7.557  7.076   1.00 8.79  ? 166  PHE A CD1 1 
ATOM   1250 C  CD2 . PHE A 1 164 ? 89.234  -5.590  5.780   1.00 8.79  ? 166  PHE A CD2 1 
ATOM   1251 C  CE1 . PHE A 1 164 ? 89.696  -8.306  5.919   1.00 8.52  ? 166  PHE A CE1 1 
ATOM   1252 C  CE2 . PHE A 1 164 ? 89.338  -6.331  4.619   1.00 8.57  ? 166  PHE A CE2 1 
ATOM   1253 C  CZ  . PHE A 1 164 ? 89.578  -7.690  4.689   1.00 8.43  ? 166  PHE A CZ  1 
ATOM   1254 N  N   . LEU A 1 165 ? 90.711  -2.716  9.640   1.00 10.26 ? 167  LEU A N   1 
ATOM   1255 C  CA  . LEU A 1 165 ? 90.427  -1.619  10.553  1.00 11.56 ? 167  LEU A CA  1 
ATOM   1256 C  C   . LEU A 1 165 ? 88.945  -1.609  10.898  1.00 12.87 ? 167  LEU A C   1 
ATOM   1257 O  O   . LEU A 1 165 ? 88.086  -1.698  10.015  1.00 11.82 ? 167  LEU A O   1 
ATOM   1258 C  CB  . LEU A 1 165 ? 90.839  -0.271  9.951   1.00 11.80 ? 167  LEU A CB  1 
ATOM   1259 C  CG  . LEU A 1 165 ? 90.805  0.939   10.894  1.00 12.00 ? 167  LEU A CG  1 
ATOM   1260 C  CD1 . LEU A 1 165 ? 91.851  0.811   11.991  1.00 12.08 ? 167  LEU A CD1 1 
ATOM   1261 C  CD2 . LEU A 1 165 ? 91.009  2.229   10.112  1.00 11.76 ? 167  LEU A CD2 1 
ATOM   1262 N  N   A ASP A 1 166 ? 88.657  -1.468  12.188  0.50 13.79 ? 168  ASP A N   1 
ATOM   1263 N  N   B ASP A 1 166 ? 88.646  -1.553  12.188  0.50 14.18 ? 168  ASP A N   1 
ATOM   1264 C  CA  A ASP A 1 166 ? 87.302  -1.602  12.708  0.50 15.96 ? 168  ASP A CA  1 
ATOM   1265 C  CA  B ASP A 1 166 ? 87.265  -1.562  12.638  0.50 16.19 ? 168  ASP A CA  1 
ATOM   1266 C  C   A ASP A 1 166 ? 86.962  -0.421  13.617  0.50 17.28 ? 168  ASP A C   1 
ATOM   1267 C  C   B ASP A 1 166 ? 86.923  -0.250  13.330  0.50 17.18 ? 168  ASP A C   1 
ATOM   1268 O  O   A ASP A 1 166 ? 87.856  0.218   14.176  0.50 19.33 ? 168  ASP A O   1 
ATOM   1269 O  O   B ASP A 1 166 ? 87.767  0.640   13.451  0.50 18.01 ? 168  ASP A O   1 
ATOM   1270 C  CB  A ASP A 1 166 ? 87.167  -2.917  13.480  0.50 17.12 ? 168  ASP A CB  1 
ATOM   1271 C  CB  B ASP A 1 166 ? 87.018  -2.741  13.580  0.50 17.28 ? 168  ASP A CB  1 
ATOM   1272 C  CG  A ASP A 1 166 ? 85.739  -3.209  13.888  0.50 18.07 ? 168  ASP A CG  1 
ATOM   1273 C  CG  B ASP A 1 166 ? 87.713  -2.573  14.912  0.50 17.14 ? 168  ASP A CG  1 
ATOM   1274 O  OD1 A ASP A 1 166 ? 84.820  -2.554  13.350  0.50 17.87 ? 168  ASP A OD1 1 
ATOM   1275 O  OD1 B ASP A 1 166 ? 87.768  -1.431  15.415  0.50 18.35 ? 168  ASP A OD1 1 
ATOM   1276 O  OD2 A ASP A 1 166 ? 85.539  -4.091  14.749  0.50 19.61 ? 168  ASP A OD2 1 
ATOM   1277 O  OD2 B ASP A 1 166 ? 88.200  -3.583  15.459  0.50 19.34 ? 168  ASP A OD2 1 
ATOM   1278 N  N   . GLY A 1 167 ? 85.673  -0.127  13.754  1.00 17.66 ? 169  GLY A N   1 
ATOM   1279 C  CA  . GLY A 1 167 ? 85.235  1.033   14.523  1.00 18.40 ? 169  GLY A CA  1 
ATOM   1280 C  C   . GLY A 1 167 ? 85.336  2.344   13.764  1.00 18.82 ? 169  GLY A C   1 
ATOM   1281 O  O   . GLY A 1 167 ? 85.506  3.405   14.364  1.00 20.15 ? 169  GLY A O   1 
ATOM   1282 N  N   . ILE A 1 168 ? 85.214  2.278   12.443  1.00 16.10 ? 170  ILE A N   1 
ATOM   1283 C  CA  . ILE A 1 168 ? 85.121  3.483   11.628  1.00 15.22 ? 170  ILE A CA  1 
ATOM   1284 C  C   . ILE A 1 168 ? 83.703  4.053   11.661  1.00 14.55 ? 170  ILE A C   1 
ATOM   1285 O  O   . ILE A 1 168 ? 83.511  5.253   11.844  1.00 14.38 ? 170  ILE A O   1 
ATOM   1286 C  CB  . ILE A 1 168 ? 85.505  3.198   10.162  1.00 15.13 ? 170  ILE A CB  1 
ATOM   1287 C  CG1 . ILE A 1 168 ? 86.952  2.707   10.073  1.00 16.06 ? 170  ILE A CG1 1 
ATOM   1288 C  CG2 . ILE A 1 168 ? 85.282  4.432   9.300   1.00 14.51 ? 170  ILE A CG2 1 
ATOM   1289 C  CD1 . ILE A 1 168 ? 87.285  2.013   8.767   1.00 15.11 ? 170  ILE A CD1 1 
ATOM   1290 N  N   . ALA A 1 169 ? 82.716  3.183   11.460  1.00 12.82 ? 171  ALA A N   1 
ATOM   1291 C  CA  . ALA A 1 169 ? 81.347  3.614   11.193  1.00 12.43 ? 171  ALA A CA  1 
ATOM   1292 C  C   . ALA A 1 169 ? 80.452  3.445   12.417  1.00 11.52 ? 171  ALA A C   1 
ATOM   1293 O  O   . ALA A 1 169 ? 80.355  2.358   12.981  1.00 11.69 ? 171  ALA A O   1 
ATOM   1294 C  CB  . ALA A 1 169 ? 80.776  2.845   10.012  1.00 12.10 ? 171  ALA A CB  1 
ATOM   1295 N  N   . GLN A 1 170 ? 79.820  4.536   12.838  1.00 10.71 ? 172  GLN A N   1 
ATOM   1296 C  CA  . GLN A 1 170 ? 78.804  4.487   13.885  1.00 10.57 ? 172  GLN A CA  1 
ATOM   1297 C  C   . GLN A 1 170 ? 77.728  5.503   13.532  1.00 10.41 ? 172  GLN A C   1 
ATOM   1298 O  O   . GLN A 1 170 ? 78.011  6.488   12.851  1.00 10.46 ? 172  GLN A O   1 
ATOM   1299 C  CB  . GLN A 1 170 ? 79.410  4.856   15.244  1.00 10.27 ? 172  GLN A CB  1 
ATOM   1300 C  CG  . GLN A 1 170 ? 80.687  4.116   15.604  1.00 11.41 ? 172  GLN A CG  1 
ATOM   1301 C  CD  . GLN A 1 170 ? 80.419  2.786   16.278  1.00 11.84 ? 172  GLN A CD  1 
ATOM   1302 O  OE1 . GLN A 1 170 ? 79.294  2.287   16.269  1.00 11.20 ? 172  GLN A OE1 1 
ATOM   1303 N  NE2 . GLN A 1 170 ? 81.460  2.196   16.857  1.00 13.92 ? 172  GLN A NE2 1 
ATOM   1304 N  N   . PRO A 1 171 ? 76.492  5.278   13.999  1.00 10.23 ? 173  PRO A N   1 
ATOM   1305 C  CA  . PRO A 1 171 ? 75.502  6.336   13.824  1.00 10.47 ? 173  PRO A CA  1 
ATOM   1306 C  C   . PRO A 1 171 ? 75.878  7.550   14.663  1.00 10.94 ? 173  PRO A C   1 
ATOM   1307 O  O   . PRO A 1 171 ? 76.412  7.405   15.765  1.00 10.84 ? 173  PRO A O   1 
ATOM   1308 C  CB  . PRO A 1 171 ? 74.209  5.700   14.344  1.00 10.22 ? 173  PRO A CB  1 
ATOM   1309 C  CG  . PRO A 1 171 ? 74.666  4.665   15.320  1.00 10.26 ? 173  PRO A CG  1 
ATOM   1310 C  CD  . PRO A 1 171 ? 75.977  4.147   14.790  1.00 9.85  ? 173  PRO A CD  1 
ATOM   1311 N  N   . ALA A 1 172 ? 75.660  8.741   14.117  1.00 11.56 ? 174  ALA A N   1 
ATOM   1312 C  CA  . ALA A 1 172 ? 75.736  9.954   14.916  1.00 12.36 ? 174  ALA A CA  1 
ATOM   1313 C  C   . ALA A 1 172 ? 74.375  10.220  15.547  1.00 13.08 ? 174  ALA A C   1 
ATOM   1314 O  O   . ALA A 1 172 ? 73.344  10.106  14.885  1.00 12.82 ? 174  ALA A O   1 
ATOM   1315 C  CB  . ALA A 1 172 ? 76.160  11.134  14.054  1.00 12.68 ? 174  ALA A CB  1 
ATOM   1316 N  N   A ILE A 1 173 ? 74.384  10.577  16.827  0.50 13.59 ? 175  ILE A N   1 
ATOM   1317 N  N   B ILE A 1 173 ? 74.372  10.564  16.830  0.50 13.55 ? 175  ILE A N   1 
ATOM   1318 C  CA  A ILE A 1 173 ? 73.163  10.917  17.545  0.50 14.17 ? 175  ILE A CA  1 
ATOM   1319 C  CA  B ILE A 1 173 ? 73.133  10.893  17.524  0.50 14.09 ? 175  ILE A CA  1 
ATOM   1320 C  C   A ILE A 1 173 ? 72.851  12.404  17.395  0.50 14.86 ? 175  ILE A C   1 
ATOM   1321 C  C   B ILE A 1 173 ? 72.825  12.385  17.431  0.50 14.86 ? 175  ILE A C   1 
ATOM   1322 O  O   A ILE A 1 173 ? 73.627  13.254  17.829  0.50 15.25 ? 175  ILE A O   1 
ATOM   1323 O  O   B ILE A 1 173 ? 73.584  13.218  17.924  0.50 15.43 ? 175  ILE A O   1 
ATOM   1324 C  CB  A ILE A 1 173 ? 73.291  10.587  19.043  0.50 13.99 ? 175  ILE A CB  1 
ATOM   1325 C  CB  B ILE A 1 173 ? 73.177  10.462  19.002  0.50 13.77 ? 175  ILE A CB  1 
ATOM   1326 C  CG1 A ILE A 1 173 ? 73.813  9.161   19.233  0.50 14.81 ? 175  ILE A CG1 1 
ATOM   1327 C  CG1 B ILE A 1 173 ? 73.026  8.942   19.116  0.50 13.93 ? 175  ILE A CG1 1 
ATOM   1328 C  CG2 A ILE A 1 173 ? 71.958  10.786  19.749  0.50 13.60 ? 175  ILE A CG2 1 
ATOM   1329 C  CG2 B ILE A 1 173 ? 72.082  11.164  19.792  0.50 13.99 ? 175  ILE A CG2 1 
ATOM   1330 C  CD1 A ILE A 1 173 ? 72.907  8.095   18.656  0.50 14.09 ? 175  ILE A CD1 1 
ATOM   1331 C  CD1 B ILE A 1 173 ? 73.152  8.418   20.529  0.50 12.74 ? 175  ILE A CD1 1 
ATOM   1332 N  N   . ASN A 1 174 ? 71.719  12.709  16.770  1.00 15.26 ? 176  ASN A N   1 
ATOM   1333 C  CA  . ASN A 1 174 ? 71.307  14.096  16.566  1.00 17.05 ? 176  ASN A CA  1 
ATOM   1334 C  C   . ASN A 1 174 ? 71.307  14.878  17.877  1.00 17.64 ? 176  ASN A C   1 
ATOM   1335 O  O   . ASN A 1 174 ? 70.764  14.420  18.882  1.00 17.88 ? 176  ASN A O   1 
ATOM   1336 C  CB  . ASN A 1 174 ? 69.919  14.141  15.920  1.00 18.89 ? 176  ASN A CB  1 
ATOM   1337 C  CG  . ASN A 1 174 ? 69.548  15.525  15.424  1.00 21.62 ? 176  ASN A CG  1 
ATOM   1338 O  OD1 . ASN A 1 174 ? 70.394  16.270  14.926  1.00 21.37 ? 176  ASN A OD1 1 
ATOM   1339 N  ND2 . ASN A 1 174 ? 68.271  15.873  15.548  1.00 21.28 ? 176  ASN A ND2 1 
ATOM   1340 N  N   . GLY A 1 175 ? 71.966  16.032  17.878  1.00 18.32 ? 177  GLY A N   1 
ATOM   1341 C  CA  . GLY A 1 175 ? 72.024  16.873  19.068  1.00 19.19 ? 177  GLY A CA  1 
ATOM   1342 C  C   . GLY A 1 175 ? 73.137  16.492  20.027  1.00 20.14 ? 177  GLY A C   1 
ATOM   1343 O  O   . GLY A 1 175 ? 73.399  17.206  20.992  1.00 21.93 ? 177  GLY A O   1 
ATOM   1344 N  N   . PHE A 1 176 ? 73.793  15.363  19.763  1.00 18.52 ? 178  PHE A N   1 
ATOM   1345 C  CA  . PHE A 1 176 ? 74.922  14.926  20.577  1.00 18.10 ? 178  PHE A CA  1 
ATOM   1346 C  C   . PHE A 1 176 ? 76.229  14.928  19.792  1.00 18.67 ? 178  PHE A C   1 
ATOM   1347 O  O   . PHE A 1 176 ? 77.177  15.630  20.147  1.00 16.88 ? 178  PHE A O   1 
ATOM   1348 C  CB  . PHE A 1 176 ? 74.665  13.533  21.153  1.00 19.26 ? 178  PHE A CB  1 
ATOM   1349 C  CG  . PHE A 1 176 ? 75.789  13.015  22.005  1.00 20.25 ? 178  PHE A CG  1 
ATOM   1350 C  CD1 . PHE A 1 176 ? 76.185  13.699  23.141  1.00 20.24 ? 178  PHE A CD1 1 
ATOM   1351 C  CD2 . PHE A 1 176 ? 76.445  11.840  21.672  1.00 19.31 ? 178  PHE A CD2 1 
ATOM   1352 C  CE1 . PHE A 1 176 ? 77.220  13.226  23.928  1.00 21.27 ? 178  PHE A CE1 1 
ATOM   1353 C  CE2 . PHE A 1 176 ? 77.481  11.362  22.453  1.00 19.94 ? 178  PHE A CE2 1 
ATOM   1354 C  CZ  . PHE A 1 176 ? 77.867  12.054  23.584  1.00 20.34 ? 178  PHE A CZ  1 
ATOM   1355 N  N   . ASN A 1 177 ? 76.287  14.112  18.743  1.00 17.92 ? 179  ASN A N   1 
ATOM   1356 C  CA  . ASN A 1 177 ? 77.472  14.040  17.895  1.00 18.70 ? 179  ASN A CA  1 
ATOM   1357 C  C   . ASN A 1 177 ? 77.446  15.126  16.827  1.00 19.43 ? 179  ASN A C   1 
ATOM   1358 O  O   . ASN A 1 177 ? 76.393  15.441  16.280  1.00 21.89 ? 179  ASN A O   1 
ATOM   1359 C  CB  . ASN A 1 177 ? 77.570  12.666  17.223  1.00 18.42 ? 179  ASN A CB  1 
ATOM   1360 C  CG  . ASN A 1 177 ? 77.643  11.524  18.221  1.00 19.41 ? 179  ASN A CG  1 
ATOM   1361 O  OD1 . ASN A 1 177 ? 76.742  10.689  18.292  1.00 17.98 ? 179  ASN A OD1 1 
ATOM   1362 N  ND2 . ASN A 1 177 ? 78.738  11.460  18.972  1.00 20.06 ? 179  ASN A ND2 1 
ATOM   1363 N  N   . THR A 1 178 ? 78.605  15.704  16.538  1.00 19.97 ? 180  THR A N   1 
ATOM   1364 C  CA  . THR A 1 178 ? 78.772  16.465  15.309  1.00 20.39 ? 180  THR A CA  1 
ATOM   1365 C  C   . THR A 1 178 ? 79.149  15.504  14.191  1.00 19.47 ? 180  THR A C   1 
ATOM   1366 O  O   . THR A 1 178 ? 80.207  14.880  14.236  1.00 19.39 ? 180  THR A O   1 
ATOM   1367 C  CB  . THR A 1 178 ? 79.860  17.546  15.453  1.00 22.21 ? 180  THR A CB  1 
ATOM   1368 O  OG1 . THR A 1 178 ? 79.452  18.505  16.437  1.00 23.19 ? 180  THR A OG1 1 
ATOM   1369 C  CG2 . THR A 1 178 ? 80.081  18.257  14.123  1.00 23.22 ? 180  THR A CG2 1 
ATOM   1370 N  N   . PRO A 1 179 ? 78.251  15.335  13.214  1.00 18.73 ? 181  PRO A N   1 
ATOM   1371 C  CA  . PRO A 1 179 ? 78.361  14.242  12.253  1.00 17.94 ? 181  PRO A CA  1 
ATOM   1372 C  C   . PRO A 1 179 ? 79.592  14.369  11.363  1.00 17.45 ? 181  PRO A C   1 
ATOM   1373 O  O   . PRO A 1 179 ? 80.018  15.480  11.044  1.00 16.97 ? 181  PRO A O   1 
ATOM   1374 C  CB  . PRO A 1 179 ? 77.083  14.379  11.417  1.00 17.93 ? 181  PRO A CB  1 
ATOM   1375 C  CG  . PRO A 1 179 ? 76.132  15.123  12.294  1.00 18.05 ? 181  PRO A CG  1 
ATOM   1376 C  CD  . PRO A 1 179 ? 76.992  16.082  13.059  1.00 18.42 ? 181  PRO A CD  1 
ATOM   1377 N  N   . LEU A 1 180 ? 80.175  13.229  11.005  1.00 15.33 ? 182  LEU A N   1 
ATOM   1378 C  CA  . LEU A 1 180 ? 81.247  13.177  10.017  1.00 15.42 ? 182  LEU A CA  1 
ATOM   1379 C  C   . LEU A 1 180 ? 80.666  13.003  8.619   1.00 13.99 ? 182  LEU A C   1 
ATOM   1380 O  O   . LEU A 1 180 ? 79.542  12.529  8.466   1.00 13.76 ? 182  LEU A O   1 
ATOM   1381 C  CB  . LEU A 1 180 ? 82.189  12.013  10.324  1.00 15.15 ? 182  LEU A CB  1 
ATOM   1382 C  CG  . LEU A 1 180 ? 82.863  12.039  11.697  1.00 16.14 ? 182  LEU A CG  1 
ATOM   1383 C  CD1 . LEU A 1 180 ? 83.310  10.641  12.102  1.00 15.68 ? 182  LEU A CD1 1 
ATOM   1384 C  CD2 . LEU A 1 180 ? 84.037  13.007  11.692  1.00 16.32 ? 182  LEU A CD2 1 
ATOM   1385 N  N   . PRO A 1 181 ? 81.444  13.362  7.589   1.00 13.97 ? 183  PRO A N   1 
ATOM   1386 C  CA  . PRO A 1 181 ? 80.973  13.218  6.217   1.00 13.93 ? 183  PRO A CA  1 
ATOM   1387 C  C   . PRO A 1 181 ? 80.518  11.792  5.905   1.00 13.13 ? 183  PRO A C   1 
ATOM   1388 O  O   . PRO A 1 181 ? 81.298  10.848  6.048   1.00 14.01 ? 183  PRO A O   1 
ATOM   1389 C  CB  . PRO A 1 181 ? 82.209  13.573  5.394   1.00 13.62 ? 183  PRO A CB  1 
ATOM   1390 C  CG  . PRO A 1 181 ? 82.935  14.564  6.242   1.00 13.57 ? 183  PRO A CG  1 
ATOM   1391 C  CD  . PRO A 1 181 ? 82.692  14.144  7.670   1.00 13.97 ? 183  PRO A CD  1 
ATOM   1392 N  N   . GLY A 1 182 ? 79.263  11.647  5.492   1.00 12.47 ? 184  GLY A N   1 
ATOM   1393 C  CA  . GLY A 1 182 ? 78.711  10.343  5.125   1.00 11.44 ? 184  GLY A CA  1 
ATOM   1394 C  C   . GLY A 1 182 ? 78.014  9.625   6.268   1.00 11.14 ? 184  GLY A C   1 
ATOM   1395 O  O   . GLY A 1 182 ? 77.237  8.698   6.046   1.00 11.36 ? 184  GLY A O   1 
ATOM   1396 N  N   . GLN A 1 183 ? 78.296  10.051  7.495   1.00 11.27 ? 185  GLN A N   1 
ATOM   1397 C  CA  . GLN A 1 183 ? 77.779  9.384   8.687   1.00 11.33 ? 185  GLN A CA  1 
ATOM   1398 C  C   . GLN A 1 183 ? 76.260  9.524   8.772   1.00 11.88 ? 185  GLN A C   1 
ATOM   1399 O  O   . GLN A 1 183 ? 75.718  10.598  8.518   1.00 11.54 ? 185  GLN A O   1 
ATOM   1400 C  CB  . GLN A 1 183 ? 78.422  9.986   9.940   1.00 11.73 ? 185  GLN A CB  1 
ATOM   1401 C  CG  . GLN A 1 183 ? 78.318  9.120   11.182  1.00 12.19 ? 185  GLN A CG  1 
ATOM   1402 C  CD  . GLN A 1 183 ? 78.920  9.777   12.414  1.00 13.20 ? 185  GLN A CD  1 
ATOM   1403 O  OE1 . GLN A 1 183 ? 79.284  10.956  12.396  1.00 13.73 ? 185  GLN A OE1 1 
ATOM   1404 N  NE2 . GLN A 1 183 ? 79.021  9.016   13.497  1.00 11.84 ? 185  GLN A NE2 1 
ATOM   1405 N  N   . ASN A 1 184 ? 75.573  8.445   9.142   1.00 12.10 ? 186  ASN A N   1 
ATOM   1406 C  CA  . ASN A 1 184 ? 74.130  8.523   9.380   1.00 12.41 ? 186  ASN A CA  1 
ATOM   1407 C  C   . ASN A 1 184 ? 73.820  9.327   10.641  1.00 13.18 ? 186  ASN A C   1 
ATOM   1408 O  O   . ASN A 1 184 ? 74.633  9.396   11.562  1.00 12.21 ? 186  ASN A O   1 
ATOM   1409 C  CB  . ASN A 1 184 ? 73.501  7.127   9.466   1.00 11.92 ? 186  ASN A CB  1 
ATOM   1410 C  CG  . ASN A 1 184 ? 72.043  7.112   9.031   1.00 12.46 ? 186  ASN A CG  1 
ATOM   1411 O  OD1 . ASN A 1 184 ? 71.437  8.161   8.811   1.00 12.13 ? 186  ASN A OD1 1 
ATOM   1412 N  ND2 . ASN A 1 184 ? 71.479  5.916   8.884   1.00 12.37 ? 186  ASN A ND2 1 
ATOM   1413 N  N   . ILE A 1 185 ? 72.653  9.964   10.654  1.00 14.11 ? 187  ILE A N   1 
ATOM   1414 C  CA  . ILE A 1 185 ? 72.231  10.781  11.785  1.00 14.40 ? 187  ILE A CA  1 
ATOM   1415 C  C   . ILE A 1 185 ? 70.872  10.293  12.270  1.00 14.51 ? 187  ILE A C   1 
ATOM   1416 O  O   . ILE A 1 185 ? 69.922  10.211  11.493  1.00 14.53 ? 187  ILE A O   1 
ATOM   1417 C  CB  . ILE A 1 185 ? 72.134  12.270  11.394  1.00 14.76 ? 187  ILE A CB  1 
ATOM   1418 C  CG1 . ILE A 1 185 ? 73.471  12.758  10.827  1.00 14.94 ? 187  ILE A CG1 1 
ATOM   1419 C  CG2 . ILE A 1 185 ? 71.716  13.113  12.589  1.00 14.10 ? 187  ILE A CG2 1 
ATOM   1420 C  CD1 . ILE A 1 185 ? 73.369  14.062  10.064  1.00 16.59 ? 187  ILE A CD1 1 
ATOM   1421 N  N   . VAL A 1 186 ? 70.796  9.922   13.543  1.00 14.07 ? 188  VAL A N   1 
ATOM   1422 C  CA  . VAL A 1 186 ? 69.613  9.245   14.066  1.00 13.79 ? 188  VAL A CA  1 
ATOM   1423 C  C   . VAL A 1 186 ? 69.132  9.889   15.360  1.00 13.76 ? 188  VAL A C   1 
ATOM   1424 O  O   . VAL A 1 186 ? 69.890  10.577  16.041  1.00 13.99 ? 188  VAL A O   1 
ATOM   1425 C  CB  . VAL A 1 186 ? 69.880  7.746   14.325  1.00 13.61 ? 188  VAL A CB  1 
ATOM   1426 C  CG1 . VAL A 1 186 ? 70.439  7.079   13.079  1.00 13.46 ? 188  VAL A CG1 1 
ATOM   1427 C  CG2 . VAL A 1 186 ? 70.831  7.567   15.500  1.00 13.33 ? 188  VAL A CG2 1 
ATOM   1428 N  N   . ASP A 1 187 ? 67.865  9.661   15.691  1.00 14.52 ? 189  ASP A N   1 
ATOM   1429 C  CA  . ASP A 1 187 ? 67.325  10.068  16.982  1.00 14.11 ? 189  ASP A CA  1 
ATOM   1430 C  C   . ASP A 1 187 ? 68.001  9.287   18.105  1.00 12.86 ? 189  ASP A C   1 
ATOM   1431 O  O   . ASP A 1 187 ? 68.323  8.109   17.948  1.00 12.19 ? 189  ASP A O   1 
ATOM   1432 C  CB  . ASP A 1 187 ? 65.814  9.829   17.026  1.00 15.74 ? 189  ASP A CB  1 
ATOM   1433 C  CG  . ASP A 1 187 ? 65.043  10.764  16.107  1.00 18.34 ? 189  ASP A CG  1 
ATOM   1434 O  OD1 . ASP A 1 187 ? 65.440  11.941  15.980  1.00 20.36 ? 189  ASP A OD1 1 
ATOM   1435 O  OD2 . ASP A 1 187 ? 64.025  10.324  15.531  1.00 19.43 ? 189  ASP A OD2 1 
ATOM   1436 N  N   . ALA A 1 188 ? 68.222  9.949   19.235  1.00 11.92 ? 190  ALA A N   1 
ATOM   1437 C  CA  . ALA A 1 188 ? 68.847  9.305   20.385  1.00 11.18 ? 190  ALA A CA  1 
ATOM   1438 C  C   . ALA A 1 188 ? 68.099  8.038   20.794  1.00 10.81 ? 190  ALA A C   1 
ATOM   1439 O  O   . ALA A 1 188 ? 68.705  7.069   21.254  1.00 9.82  ? 190  ALA A O   1 
ATOM   1440 C  CB  . ALA A 1 188 ? 68.930  10.271  21.555  1.00 10.91 ? 190  ALA A CB  1 
ATOM   1441 N  N   . GLY A 1 189 ? 66.780  8.056   20.624  1.00 10.56 ? 191  GLY A N   1 
ATOM   1442 C  CA  . GLY A 1 189 ? 65.930  6.942   21.047  1.00 10.88 ? 191  GLY A CA  1 
ATOM   1443 C  C   . GLY A 1 189 ? 66.119  5.669   20.239  1.00 10.29 ? 191  GLY A C   1 
ATOM   1444 O  O   . GLY A 1 189 ? 65.538  4.633   20.557  1.00 10.36 ? 191  GLY A O   1 
ATOM   1445 N  N   . VAL A 1 190 ? 66.894  5.754   19.161  1.00 10.00 ? 192  VAL A N   1 
ATOM   1446 C  CA  . VAL A 1 190 ? 67.298  4.560   18.422  1.00 9.51  ? 192  VAL A CA  1 
ATOM   1447 C  C   . VAL A 1 190 ? 68.302  3.731   19.231  1.00 9.37  ? 192  VAL A C   1 
ATOM   1448 O  O   . VAL A 1 190 ? 68.299  2.495   19.174  1.00 8.96  ? 192  VAL A O   1 
ATOM   1449 C  CB  . VAL A 1 190 ? 67.886  4.923   17.044  1.00 9.57  ? 192  VAL A CB  1 
ATOM   1450 C  CG1 . VAL A 1 190 ? 68.532  3.706   16.393  1.00 9.71  ? 192  VAL A CG1 1 
ATOM   1451 C  CG2 . VAL A 1 190 ? 66.804  5.499   16.141  1.00 9.47  ? 192  VAL A CG2 1 
ATOM   1452 N  N   . ILE A 1 191 ? 69.107  4.419   20.036  1.00 8.57  ? 193  ILE A N   1 
ATOM   1453 C  CA  . ILE A 1 191 ? 70.162  3.782   20.815  1.00 8.79  ? 193  ILE A CA  1 
ATOM   1454 C  C   . ILE A 1 191 ? 69.816  3.728   22.304  1.00 8.94  ? 193  ILE A C   1 
ATOM   1455 O  O   . ILE A 1 191 ? 70.054  2.719   22.968  1.00 9.01  ? 193  ILE A O   1 
ATOM   1456 C  CB  . ILE A 1 191 ? 71.507  4.526   20.642  1.00 8.61  ? 193  ILE A CB  1 
ATOM   1457 C  CG1 . ILE A 1 191 ? 71.922  4.556   19.168  1.00 8.40  ? 193  ILE A CG1 1 
ATOM   1458 C  CG2 . ILE A 1 191 ? 72.588  3.883   21.497  1.00 8.85  ? 193  ILE A CG2 1 
ATOM   1459 C  CD1 . ILE A 1 191 ? 71.784  3.226   18.456  1.00 8.60  ? 193  ILE A CD1 1 
ATOM   1460 N  N   . ILE A 1 192 ? 69.255  4.820   22.818  1.00 8.70  ? 194  ILE A N   1 
ATOM   1461 C  CA  . ILE A 1 192 ? 69.029  4.979   24.255  1.00 8.98  ? 194  ILE A CA  1 
ATOM   1462 C  C   . ILE A 1 192 ? 67.548  4.788   24.572  1.00 9.62  ? 194  ILE A C   1 
ATOM   1463 O  O   . ILE A 1 192 ? 66.699  5.496   24.029  1.00 9.28  ? 194  ILE A O   1 
ATOM   1464 C  CB  . ILE A 1 192 ? 69.462  6.383   24.741  1.00 9.01  ? 194  ILE A CB  1 
ATOM   1465 C  CG1 . ILE A 1 192 ? 70.944  6.631   24.441  1.00 9.23  ? 194  ILE A CG1 1 
ATOM   1466 C  CG2 . ILE A 1 192 ? 69.185  6.553   26.228  1.00 8.81  ? 194  ILE A CG2 1 
ATOM   1467 C  CD1 . ILE A 1 192 ? 71.877  5.663   25.139  1.00 8.98  ? 194  ILE A CD1 1 
ATOM   1468 N  N   . THR A 1 193 ? 67.240  3.854   25.467  1.00 9.92  ? 195  THR A N   1 
ATOM   1469 C  CA  . THR A 1 193 ? 65.849  3.580   25.820  1.00 10.68 ? 195  THR A CA  1 
ATOM   1470 C  C   . THR A 1 193 ? 65.225  4.772   26.539  1.00 11.30 ? 195  THR A C   1 
ATOM   1471 O  O   . THR A 1 193 ? 65.799  5.311   27.485  1.00 10.49 ? 195  THR A O   1 
ATOM   1472 C  CB  . THR A 1 193 ? 65.704  2.320   26.697  1.00 10.82 ? 195  THR A CB  1 
ATOM   1473 O  OG1 . THR A 1 193 ? 66.623  2.384   27.795  1.00 10.34 ? 195  THR A OG1 1 
ATOM   1474 C  CG2 . THR A 1 193 ? 65.963  1.061   25.881  1.00 10.12 ? 195  THR A CG2 1 
ATOM   1475 N  N   . GLY A 1 194 ? 64.061  5.199   26.062  1.00 11.87 ? 196  GLY A N   1 
ATOM   1476 C  CA  . GLY A 1 194 ? 63.359  6.320   26.673  1.00 13.17 ? 196  GLY A CA  1 
ATOM   1477 C  C   . GLY A 1 194 ? 63.835  7.655   26.136  1.00 13.36 ? 196  GLY A C   1 
ATOM   1478 O  O   . GLY A 1 194 ? 63.336  8.705   26.539  1.00 13.26 ? 196  GLY A O   1 
ATOM   1479 N  N   . ALA A 1 195 ? 64.812  7.617   25.234  1.00 13.81 ? 197  ALA A N   1 
ATOM   1480 C  CA  . ALA A 1 195 ? 65.350  8.839   24.647  1.00 14.37 ? 197  ALA A CA  1 
ATOM   1481 C  C   . ALA A 1 195 ? 64.498  9.306   23.474  1.00 13.75 ? 197  ALA A C   1 
ATOM   1482 O  O   . ALA A 1 195 ? 63.491  8.687   23.143  1.00 13.19 ? 197  ALA A O   1 
ATOM   1483 C  CB  . ALA A 1 195 ? 66.792  8.635   24.212  1.00 14.45 ? 197  ALA A CB  1 
ATOM   1484 N  N   . THR A 1 196 ? 64.921  10.395  22.842  1.00 14.92 ? 198  THR A N   1 
ATOM   1485 C  CA  . THR A 1 196 ? 64.116  11.061  21.820  1.00 16.25 ? 198  THR A CA  1 
ATOM   1486 C  C   . THR A 1 196 ? 63.580  10.107  20.760  1.00 15.65 ? 198  THR A C   1 
ATOM   1487 O  O   . THR A 1 196 ? 64.347  9.458   20.047  1.00 15.57 ? 198  THR A O   1 
ATOM   1488 C  CB  . THR A 1 196 ? 64.911  12.181  21.127  1.00 16.69 ? 198  THR A CB  1 
ATOM   1489 O  OG1 . THR A 1 196 ? 65.392  13.101  22.111  1.00 17.89 ? 198  THR A OG1 1 
ATOM   1490 C  CG2 . THR A 1 196 ? 64.028  12.925  20.132  1.00 17.70 ? 198  THR A CG2 1 
ATOM   1491 N  N   . ASN A 1 197 ? 62.256  10.049  20.650  1.00 16.04 ? 199  ASN A N   1 
ATOM   1492 C  CA  . ASN A 1 197 ? 61.590  9.273   19.607  1.00 15.56 ? 199  ASN A CA  1 
ATOM   1493 C  C   . ASN A 1 197 ? 61.779  7.761   19.713  1.00 14.51 ? 199  ASN A C   1 
ATOM   1494 O  O   . ASN A 1 197 ? 61.584  7.038   18.739  1.00 14.23 ? 199  ASN A O   1 
ATOM   1495 C  CB  . ASN A 1 197 ? 61.989  9.773   18.218  1.00 17.79 ? 199  ASN A CB  1 
ATOM   1496 C  CG  . ASN A 1 197 ? 61.458  11.162  17.929  1.00 20.16 ? 199  ASN A CG  1 
ATOM   1497 O  OD1 . ASN A 1 197 ? 60.687  11.719  18.714  1.00 21.62 ? 199  ASN A OD1 1 
ATOM   1498 N  ND2 . ASN A 1 197 ? 61.869  11.731  16.804  1.00 20.46 ? 199  ASN A ND2 1 
ATOM   1499 N  N   . ASP A 1 198 ? 62.124  7.284   20.906  1.00 12.90 ? 200  ASP A N   1 
ATOM   1500 C  CA  . ASP A 1 198 ? 61.893  5.888   21.261  1.00 12.72 ? 200  ASP A CA  1 
ATOM   1501 C  C   . ASP A 1 198 ? 60.405  5.699   21.534  1.00 12.66 ? 200  ASP A C   1 
ATOM   1502 O  O   . ASP A 1 198 ? 59.864  6.312   22.452  1.00 13.10 ? 200  ASP A O   1 
ATOM   1503 C  CB  . ASP A 1 198 ? 62.717  5.505   22.499  1.00 12.50 ? 200  ASP A CB  1 
ATOM   1504 C  CG  . ASP A 1 198 ? 62.451  4.084   22.969  1.00 12.40 ? 200  ASP A CG  1 
ATOM   1505 O  OD1 . ASP A 1 198 ? 61.849  3.301   22.204  1.00 12.05 ? 200  ASP A OD1 1 
ATOM   1506 O  OD2 . ASP A 1 198 ? 62.843  3.748   24.110  1.00 11.89 ? 200  ASP A OD2 1 
ATOM   1507 N  N   . PRO A 1 199 ? 59.726  4.901   20.693  1.00 12.81 ? 201  PRO A N   1 
ATOM   1508 C  CA  . PRO A 1 199 ? 58.271  4.797   20.732  1.00 12.85 ? 201  PRO A CA  1 
ATOM   1509 C  C   . PRO A 1 199 ? 57.781  3.812   21.789  1.00 12.86 ? 201  PRO A C   1 
ATOM   1510 O  O   . PRO A 1 199 ? 56.586  3.772   22.087  1.00 11.66 ? 201  PRO A O   1 
ATOM   1511 C  CB  . PRO A 1 199 ? 57.926  4.276   19.337  1.00 13.40 ? 201  PRO A CB  1 
ATOM   1512 C  CG  . PRO A 1 199 ? 59.116  3.468   18.947  1.00 13.83 ? 201  PRO A CG  1 
ATOM   1513 C  CD  . PRO A 1 199 ? 60.302  4.177   19.544  1.00 13.21 ? 201  PRO A CD  1 
ATOM   1514 N  N   . ILE A 1 200 ? 58.697  3.017   22.335  1.00 12.20 ? 202  ILE A N   1 
ATOM   1515 C  CA  . ILE A 1 200 ? 58.338  1.953   23.267  1.00 11.79 ? 202  ILE A CA  1 
ATOM   1516 C  C   . ILE A 1 200 ? 58.323  2.461   24.708  1.00 11.99 ? 202  ILE A C   1 
ATOM   1517 O  O   . ILE A 1 200 ? 59.301  3.042   25.181  1.00 11.37 ? 202  ILE A O   1 
ATOM   1518 C  CB  . ILE A 1 200 ? 59.337  0.784   23.177  1.00 11.80 ? 202  ILE A CB  1 
ATOM   1519 C  CG1 . ILE A 1 200 ? 59.494  0.315   21.726  1.00 11.50 ? 202  ILE A CG1 1 
ATOM   1520 C  CG2 . ILE A 1 200 ? 58.929  -0.348  24.110  1.00 12.33 ? 202  ILE A CG2 1 
ATOM   1521 C  CD1 . ILE A 1 200 ? 58.188  0.154   20.973  1.00 11.72 ? 202  ILE A CD1 1 
ATOM   1522 N  N   . THR A 1 201 ? 57.225  2.217   25.416  1.00 11.83 ? 203  THR A N   1 
ATOM   1523 C  CA  . THR A 1 201 ? 57.147  2.584   26.824  1.00 11.04 ? 203  THR A CA  1 
ATOM   1524 C  C   . THR A 1 201 ? 58.159  1.787   27.642  1.00 11.32 ? 203  THR A C   1 
ATOM   1525 O  O   . THR A 1 201 ? 58.249  0.565   27.507  1.00 10.93 ? 203  THR A O   1 
ATOM   1526 C  CB  . THR A 1 201 ? 55.740  2.337   27.394  1.00 11.03 ? 203  THR A CB  1 
ATOM   1527 O  OG1 . THR A 1 201 ? 54.791  3.165   26.712  1.00 11.03 ? 203  THR A OG1 1 
ATOM   1528 C  CG2 . THR A 1 201 ? 55.707  2.650   28.890  1.00 11.08 ? 203  THR A CG2 1 
ATOM   1529 N  N   . ARG A 1 202 ? 58.922  2.488   28.481  1.00 10.52 ? 204  ARG A N   1 
ATOM   1530 C  CA  . ARG A 1 202 ? 59.874  1.848   29.390  1.00 10.08 ? 204  ARG A CA  1 
ATOM   1531 C  C   . ARG A 1 202 ? 59.530  2.157   30.845  1.00 10.08 ? 204  ARG A C   1 
ATOM   1532 O  O   . ARG A 1 202 ? 58.871  3.154   31.126  1.00 10.20 ? 204  ARG A O   1 
ATOM   1533 C  CB  . ARG A 1 202 ? 61.293  2.340   29.101  1.00 9.97  ? 204  ARG A CB  1 
ATOM   1534 C  CG  . ARG A 1 202 ? 61.604  2.504   27.621  1.00 10.05 ? 204  ARG A CG  1 
ATOM   1535 C  CD  . ARG A 1 202 ? 61.908  1.166   26.967  1.00 10.20 ? 204  ARG A CD  1 
ATOM   1536 N  NE  . ARG A 1 202 ? 62.256  1.327   25.555  1.00 9.95  ? 204  ARG A NE  1 
ATOM   1537 C  CZ  . ARG A 1 202 ? 62.503  0.319   24.724  1.00 10.31 ? 204  ARG A CZ  1 
ATOM   1538 N  NH1 . ARG A 1 202 ? 62.437  -0.934  25.155  1.00 10.07 ? 204  ARG A NH1 1 
ATOM   1539 N  NH2 . ARG A 1 202 ? 62.792  0.565   23.452  1.00 10.31 ? 204  ARG A NH2 1 
ATOM   1540 N  N   . PRO A 1 203 ? 60.008  1.320   31.780  1.00 9.89  ? 205  PRO A N   1 
ATOM   1541 C  CA  . PRO A 1 203 ? 60.015  1.729   33.183  1.00 10.14 ? 205  PRO A CA  1 
ATOM   1542 C  C   . PRO A 1 203 ? 60.823  3.010   33.344  1.00 10.06 ? 205  PRO A C   1 
ATOM   1543 O  O   . PRO A 1 203 ? 61.838  3.182   32.677  1.00 9.48  ? 205  PRO A O   1 
ATOM   1544 C  CB  . PRO A 1 203 ? 60.732  0.572   33.889  1.00 10.02 ? 205  PRO A CB  1 
ATOM   1545 C  CG  . PRO A 1 203 ? 60.623  -0.588  32.956  1.00 10.32 ? 205  PRO A CG  1 
ATOM   1546 C  CD  . PRO A 1 203 ? 60.628  0.001   31.576  1.00 10.40 ? 205  PRO A CD  1 
ATOM   1547 N  N   . SER A 1 204 ? 60.375  3.904   34.220  1.00 10.56 ? 206  SER A N   1 
ATOM   1548 C  CA  . SER A 1 204 ? 61.056  5.183   34.402  1.00 11.01 ? 206  SER A CA  1 
ATOM   1549 C  C   . SER A 1 204 ? 62.547  5.028   34.726  1.00 11.46 ? 206  SER A C   1 
ATOM   1550 O  O   . SER A 1 204 ? 63.375  5.813   34.253  1.00 11.21 ? 206  SER A O   1 
ATOM   1551 C  CB  . SER A 1 204 ? 60.358  6.018   35.478  1.00 11.20 ? 206  SER A CB  1 
ATOM   1552 O  OG  . SER A 1 204 ? 60.283  5.306   36.700  1.00 11.59 ? 206  SER A OG  1 
ATOM   1553 N  N   . TRP A 1 205 ? 62.888  4.015   35.520  1.00 11.11 ? 207  TRP A N   1 
ATOM   1554 C  CA  . TRP A 1 205 ? 64.279  3.809   35.949  1.00 11.31 ? 207  TRP A CA  1 
ATOM   1555 C  C   . TRP A 1 205 ? 65.190  3.357   34.808  1.00 11.34 ? 207  TRP A C   1 
ATOM   1556 O  O   . TRP A 1 205 ? 66.416  3.410   34.924  1.00 11.29 ? 207  TRP A O   1 
ATOM   1557 C  CB  . TRP A 1 205 ? 64.354  2.805   37.105  1.00 11.34 ? 207  TRP A CB  1 
ATOM   1558 C  CG  . TRP A 1 205 ? 63.788  1.459   36.770  1.00 11.21 ? 207  TRP A CG  1 
ATOM   1559 C  CD1 . TRP A 1 205 ? 62.530  1.002   37.049  1.00 11.05 ? 207  TRP A CD1 1 
ATOM   1560 C  CD2 . TRP A 1 205 ? 64.460  0.391   36.089  1.00 11.61 ? 207  TRP A CD2 1 
ATOM   1561 N  NE1 . TRP A 1 205 ? 62.376  -0.277  36.573  1.00 10.92 ? 207  TRP A NE1 1 
ATOM   1562 C  CE2 . TRP A 1 205 ? 63.543  -0.674  35.977  1.00 11.65 ? 207  TRP A CE2 1 
ATOM   1563 C  CE3 . TRP A 1 205 ? 65.742  0.237   35.553  1.00 11.50 ? 207  TRP A CE3 1 
ATOM   1564 C  CZ2 . TRP A 1 205 ? 63.873  -1.883  35.365  1.00 12.00 ? 207  TRP A CZ2 1 
ATOM   1565 C  CZ3 . TRP A 1 205 ? 66.067  -0.960  34.941  1.00 11.86 ? 207  TRP A CZ3 1 
ATOM   1566 C  CH2 . TRP A 1 205 ? 65.134  -2.002  34.847  1.00 11.97 ? 207  TRP A CH2 1 
ATOM   1567 N  N   . ALA A 1 206 ? 64.589  2.916   33.707  1.00 10.98 ? 208  ALA A N   1 
ATOM   1568 C  CA  . ALA A 1 206 ? 65.352  2.387   32.582  1.00 11.18 ? 208  ALA A CA  1 
ATOM   1569 C  C   . ALA A 1 206 ? 65.620  3.436   31.498  1.00 10.61 ? 208  ALA A C   1 
ATOM   1570 O  O   . ALA A 1 206 ? 66.278  3.151   30.496  1.00 10.91 ? 208  ALA A O   1 
ATOM   1571 C  CB  . ALA A 1 206 ? 64.651  1.171   31.990  1.00 10.86 ? 208  ALA A CB  1 
ATOM   1572 N  N   . VAL A 1 207 ? 65.122  4.651   31.706  1.00 10.59 ? 209  VAL A N   1 
ATOM   1573 C  CA  . VAL A 1 207 ? 65.369  5.745   30.772  1.00 10.55 ? 209  VAL A CA  1 
ATOM   1574 C  C   . VAL A 1 207 ? 66.829  6.195   30.838  1.00 10.64 ? 209  VAL A C   1 
ATOM   1575 O  O   . VAL A 1 207 ? 67.314  6.604   31.892  1.00 11.57 ? 209  VAL A O   1 
ATOM   1576 C  CB  . VAL A 1 207 ? 64.448  6.950   31.053  1.00 11.01 ? 209  VAL A CB  1 
ATOM   1577 C  CG1 . VAL A 1 207 ? 64.812  8.123   30.153  1.00 11.54 ? 209  VAL A CG1 1 
ATOM   1578 C  CG2 . VAL A 1 207 ? 62.991  6.554   30.863  1.00 10.92 ? 209  VAL A CG2 1 
ATOM   1579 N  N   . GLY A 1 208 ? 67.522  6.108   29.706  1.00 9.96  ? 210  GLY A N   1 
ATOM   1580 C  CA  . GLY A 1 208 ? 68.957  6.371   29.661  1.00 9.80  ? 210  GLY A CA  1 
ATOM   1581 C  C   . GLY A 1 208 ? 69.793  5.111   29.496  1.00 9.48  ? 210  GLY A C   1 
ATOM   1582 O  O   . GLY A 1 208 ? 71.022  5.178   29.427  1.00 9.40  ? 210  GLY A O   1 
ATOM   1583 N  N   . GLY A 1 209 ? 69.129  3.959   29.450  1.00 9.22  ? 211  GLY A N   1 
ATOM   1584 C  CA  . GLY A 1 209 ? 69.816  2.679   29.258  1.00 8.77  ? 211  GLY A CA  1 
ATOM   1585 C  C   . GLY A 1 209 ? 69.925  2.258   27.801  1.00 9.11  ? 211  GLY A C   1 
ATOM   1586 O  O   . GLY A 1 209 ? 69.603  3.025   26.893  1.00 8.83  ? 211  GLY A O   1 
ATOM   1587 N  N   . SER A 1 210 ? 70.411  1.041   27.575  1.00 8.77  ? 212  SER A N   1 
ATOM   1588 C  CA  . SER A 1 210 ? 70.484  0.479   26.233  1.00 8.74  ? 212  SER A CA  1 
ATOM   1589 C  C   . SER A 1 210 ? 70.538  -1.045  26.322  1.00 8.56  ? 212  SER A C   1 
ATOM   1590 O  O   . SER A 1 210 ? 71.012  -1.598  27.311  1.00 8.39  ? 212  SER A O   1 
ATOM   1591 C  CB  . SER A 1 210 ? 71.720  1.012   25.503  1.00 8.88  ? 212  SER A CB  1 
ATOM   1592 O  OG  . SER A 1 210 ? 71.657  0.742   24.112  1.00 9.44  ? 212  SER A OG  1 
ATOM   1593 N  N   . PHE A 1 211 ? 70.023  -1.723  25.304  1.00 8.68  ? 213  PHE A N   1 
ATOM   1594 C  CA  . PHE A 1 211 ? 70.190  -3.166  25.217  1.00 9.02  ? 213  PHE A CA  1 
ATOM   1595 C  C   . PHE A 1 211 ? 71.531  -3.534  24.601  1.00 9.00  ? 213  PHE A C   1 
ATOM   1596 O  O   . PHE A 1 211 ? 71.891  -3.060  23.521  1.00 9.77  ? 213  PHE A O   1 
ATOM   1597 C  CB  . PHE A 1 211 ? 69.035  -3.818  24.457  1.00 9.03  ? 213  PHE A CB  1 
ATOM   1598 C  CG  . PHE A 1 211 ? 67.720  -3.731  25.179  1.00 9.82  ? 213  PHE A CG  1 
ATOM   1599 C  CD1 . PHE A 1 211 ? 67.469  -4.527  26.284  1.00 10.26 ? 213  PHE A CD1 1 
ATOM   1600 C  CD2 . PHE A 1 211 ? 66.769  -2.802  24.799  1.00 10.03 ? 213  PHE A CD2 1 
ATOM   1601 C  CE1 . PHE A 1 211 ? 66.277  -4.422  26.977  1.00 10.76 ? 213  PHE A CE1 1 
ATOM   1602 C  CE2 . PHE A 1 211 ? 65.571  -2.696  25.482  1.00 10.60 ? 213  PHE A CE2 1 
ATOM   1603 C  CZ  . PHE A 1 211 ? 65.329  -3.502  26.578  1.00 10.85 ? 213  PHE A CZ  1 
ATOM   1604 N  N   . LEU A 1 212 ? 72.257  -4.388  25.309  1.00 9.04  ? 214  LEU A N   1 
ATOM   1605 C  CA  . LEU A 1 212 ? 73.579  -4.835  24.910  1.00 8.98  ? 214  LEU A CA  1 
ATOM   1606 C  C   . LEU A 1 212 ? 73.459  -6.247  24.347  1.00 8.66  ? 214  LEU A C   1 
ATOM   1607 O  O   . LEU A 1 212 ? 73.070  -7.170  25.058  1.00 9.28  ? 214  LEU A O   1 
ATOM   1608 C  CB  . LEU A 1 212 ? 74.499  -4.836  26.135  1.00 8.75  ? 214  LEU A CB  1 
ATOM   1609 C  CG  . LEU A 1 212 ? 76.008  -5.039  25.965  1.00 8.81  ? 214  LEU A CG  1 
ATOM   1610 C  CD1 . LEU A 1 212 ? 76.690  -4.941  27.322  1.00 9.09  ? 214  LEU A CD1 1 
ATOM   1611 C  CD2 . LEU A 1 212 ? 76.320  -6.372  25.300  1.00 8.75  ? 214  LEU A CD2 1 
ATOM   1612 N  N   . ALA A 1 213 ? 73.683  -6.392  23.044  1.00 8.68  ? 215  ALA A N   1 
ATOM   1613 C  CA  . ALA A 1 213 ? 73.723  -7.712  22.429  1.00 8.58  ? 215  ALA A CA  1 
ATOM   1614 C  C   . ALA A 1 213 ? 75.164  -8.201  22.371  1.00 8.66  ? 215  ALA A C   1 
ATOM   1615 O  O   . ALA A 1 213 ? 75.988  -7.649  21.637  1.00 8.84  ? 215  ALA A O   1 
ATOM   1616 C  CB  . ALA A 1 213 ? 73.110  -7.677  21.033  1.00 8.42  ? 215  ALA A CB  1 
ATOM   1617 N  N   . PHE A 1 214 ? 75.475  -9.196  23.194  1.00 8.60  ? 216  PHE A N   1 
ATOM   1618 C  CA  . PHE A 1 214 ? 76.811  -9.775  23.223  1.00 8.73  ? 216  PHE A CA  1 
ATOM   1619 C  C   . PHE A 1 214 ? 76.863  -11.050 22.390  1.00 8.68  ? 216  PHE A C   1 
ATOM   1620 O  O   . PHE A 1 214 ? 75.986  -11.910 22.504  1.00 8.53  ? 216  PHE A O   1 
ATOM   1621 C  CB  . PHE A 1 214 ? 77.247  -10.070 24.661  1.00 8.76  ? 216  PHE A CB  1 
ATOM   1622 C  CG  . PHE A 1 214 ? 78.632  -10.642 24.761  1.00 8.81  ? 216  PHE A CG  1 
ATOM   1623 C  CD1 . PHE A 1 214 ? 78.843  -12.005 24.624  1.00 8.85  ? 216  PHE A CD1 1 
ATOM   1624 C  CD2 . PHE A 1 214 ? 79.732  -9.808  24.898  1.00 8.68  ? 216  PHE A CD2 1 
ATOM   1625 C  CE1 . PHE A 1 214 ? 80.120  -12.532 24.670  1.00 8.81  ? 216  PHE A CE1 1 
ATOM   1626 C  CE2 . PHE A 1 214 ? 81.012  -10.330 24.949  1.00 8.84  ? 216  PHE A CE2 1 
ATOM   1627 C  CZ  . PHE A 1 214 ? 81.207  -11.693 24.820  1.00 9.08  ? 216  PHE A CZ  1 
ATOM   1628 N  N   . ARG A 1 215 ? 77.894  -11.162 21.557  1.00 8.66  ? 217  ARG A N   1 
ATOM   1629 C  CA  . ARG A 1 215 ? 78.123  -12.352 20.746  1.00 8.76  ? 217  ARG A CA  1 
ATOM   1630 C  C   . ARG A 1 215 ? 79.601  -12.740 20.772  1.00 9.16  ? 217  ARG A C   1 
ATOM   1631 O  O   . ARG A 1 215 ? 80.473  -11.932 20.438  1.00 8.78  ? 217  ARG A O   1 
ATOM   1632 C  CB  . ARG A 1 215 ? 77.687  -12.114 19.294  1.00 8.58  ? 217  ARG A CB  1 
ATOM   1633 C  CG  . ARG A 1 215 ? 76.214  -11.775 19.122  1.00 9.01  ? 217  ARG A CG  1 
ATOM   1634 C  CD  . ARG A 1 215 ? 75.365  -13.030 18.998  1.00 8.72  ? 217  ARG A CD  1 
ATOM   1635 N  NE  . ARG A 1 215 ? 75.402  -13.586 17.646  1.00 8.91  ? 217  ARG A NE  1 
ATOM   1636 C  CZ  . ARG A 1 215 ? 74.922  -14.781 17.318  1.00 9.43  ? 217  ARG A CZ  1 
ATOM   1637 N  NH1 . ARG A 1 215 ? 74.408  -15.568 18.253  1.00 9.02  ? 217  ARG A NH1 1 
ATOM   1638 N  NH2 . ARG A 1 215 ? 74.983  -15.204 16.060  1.00 9.75  ? 217  ARG A NH2 1 
ATOM   1639 N  N   . GLN A 1 216 ? 79.880  -13.983 21.154  1.00 8.64  ? 218  GLN A N   1 
ATOM   1640 C  CA  . GLN A 1 216 ? 81.230  -14.513 21.035  1.00 8.80  ? 218  GLN A CA  1 
ATOM   1641 C  C   . GLN A 1 216 ? 81.389  -15.133 19.656  1.00 8.89  ? 218  GLN A C   1 
ATOM   1642 O  O   . GLN A 1 216 ? 80.892  -16.231 19.401  1.00 8.65  ? 218  GLN A O   1 
ATOM   1643 C  CB  . GLN A 1 216 ? 81.502  -15.560 22.115  1.00 9.25  ? 218  GLN A CB  1 
ATOM   1644 C  CG  . GLN A 1 216 ? 82.922  -16.116 22.087  1.00 9.50  ? 218  GLN A CG  1 
ATOM   1645 C  CD  . GLN A 1 216 ? 83.228  -16.993 23.288  1.00 10.91 ? 218  GLN A CD  1 
ATOM   1646 O  OE1 . GLN A 1 216 ? 82.798  -16.707 24.408  1.00 11.11 ? 218  GLN A OE1 1 
ATOM   1647 N  NE2 . GLN A 1 216 ? 83.996  -18.055 23.065  1.00 11.80 ? 218  GLN A NE2 1 
ATOM   1648 N  N   . LEU A 1 217 ? 82.033  -14.400 18.755  1.00 8.31  ? 219  LEU A N   1 
ATOM   1649 C  CA  . LEU A 1 217 ? 82.128  -14.818 17.364  1.00 8.38  ? 219  LEU A CA  1 
ATOM   1650 C  C   . LEU A 1 217 ? 83.544  -15.270 17.022  1.00 8.71  ? 219  LEU A C   1 
ATOM   1651 O  O   . LEU A 1 217 ? 84.430  -14.443 16.808  1.00 8.43  ? 219  LEU A O   1 
ATOM   1652 C  CB  . LEU A 1 217 ? 81.701  -13.674 16.440  1.00 8.00  ? 219  LEU A CB  1 
ATOM   1653 C  CG  . LEU A 1 217 ? 80.267  -13.177 16.652  1.00 8.15  ? 219  LEU A CG  1 
ATOM   1654 C  CD1 . LEU A 1 217 ? 79.930  -12.047 15.691  1.00 8.38  ? 219  LEU A CD1 1 
ATOM   1655 C  CD2 . LEU A 1 217 ? 79.272  -14.320 16.517  1.00 8.00  ? 219  LEU A CD2 1 
ATOM   1656 N  N   . GLU A 1 218 ? 83.755  -16.583 16.971  1.00 9.18  ? 220  GLU A N   1 
ATOM   1657 C  CA  . GLU A 1 218 ? 85.061  -17.116 16.611  1.00 9.86  ? 220  GLU A CA  1 
ATOM   1658 C  C   . GLU A 1 218 ? 85.348  -16.828 15.147  1.00 9.90  ? 220  GLU A C   1 
ATOM   1659 O  O   . GLU A 1 218 ? 84.466  -16.952 14.300  1.00 10.15 ? 220  GLU A O   1 
ATOM   1660 C  CB  . GLU A 1 218 ? 85.141  -18.624 16.862  1.00 11.28 ? 220  GLU A CB  1 
ATOM   1661 C  CG  . GLU A 1 218 ? 86.378  -19.258 16.236  1.00 11.64 ? 220  GLU A CG  1 
ATOM   1662 C  CD  . GLU A 1 218 ? 86.604  -20.693 16.667  1.00 13.36 ? 220  GLU A CD  1 
ATOM   1663 O  OE1 . GLU A 1 218 ? 85.621  -21.371 17.036  1.00 13.65 ? 220  GLU A OE1 1 
ATOM   1664 O  OE2 . GLU A 1 218 ? 87.764  -21.155 16.594  1.00 13.49 ? 220  GLU A OE2 1 
ATOM   1665 N  N   . GLN A 1 219 ? 86.573  -16.405 14.860  1.00 9.60  ? 221  GLN A N   1 
ATOM   1666 C  CA  . GLN A 1 219 ? 86.986  -16.167 13.485  1.00 9.36  ? 221  GLN A CA  1 
ATOM   1667 C  C   . GLN A 1 219 ? 88.043  -17.178 13.066  1.00 9.38  ? 221  GLN A C   1 
ATOM   1668 O  O   . GLN A 1 219 ? 89.017  -17.396 13.781  1.00 9.70  ? 221  GLN A O   1 
ATOM   1669 C  CB  . GLN A 1 219 ? 87.515  -14.744 13.330  1.00 9.62  ? 221  GLN A CB  1 
ATOM   1670 C  CG  . GLN A 1 219 ? 86.446  -13.679 13.511  1.00 9.67  ? 221  GLN A CG  1 
ATOM   1671 C  CD  . GLN A 1 219 ? 87.020  -12.278 13.564  1.00 10.47 ? 221  GLN A CD  1 
ATOM   1672 O  OE1 . GLN A 1 219 ? 87.105  -11.669 14.631  1.00 10.67 ? 221  GLN A OE1 1 
ATOM   1673 N  NE2 . GLN A 1 219 ? 87.417  -11.760 12.410  1.00 10.67 ? 221  GLN A NE2 1 
ATOM   1674 N  N   . LEU A 1 220 ? 87.829  -17.815 11.919  1.00 9.31  ? 222  LEU A N   1 
ATOM   1675 C  CA  . LEU A 1 220 ? 88.768  -18.801 11.404  1.00 9.26  ? 222  LEU A CA  1 
ATOM   1676 C  C   . LEU A 1 220 ? 89.711  -18.147 10.403  1.00 8.93  ? 222  LEU A C   1 
ATOM   1677 O  O   . LEU A 1 220 ? 89.468  -18.172 9.198   1.00 8.65  ? 222  LEU A O   1 
ATOM   1678 C  CB  . LEU A 1 220 ? 88.019  -19.961 10.746  1.00 9.27  ? 222  LEU A CB  1 
ATOM   1679 C  CG  . LEU A 1 220 ? 86.971  -20.654 11.619  1.00 9.70  ? 222  LEU A CG  1 
ATOM   1680 C  CD1 . LEU A 1 220 ? 86.199  -21.677 10.795  1.00 9.37  ? 222  LEU A CD1 1 
ATOM   1681 C  CD2 . LEU A 1 220 ? 87.636  -21.318 12.818  1.00 9.47  ? 222  LEU A CD2 1 
ATOM   1682 N  N   . VAL A 1 221 ? 90.771  -17.540 10.922  1.00 8.60  ? 223  VAL A N   1 
ATOM   1683 C  CA  . VAL A 1 221 ? 91.577  -16.603 10.152  1.00 8.96  ? 223  VAL A CA  1 
ATOM   1684 C  C   . VAL A 1 221 ? 92.418  -17.300 9.081   1.00 9.13  ? 223  VAL A C   1 
ATOM   1685 O  O   . VAL A 1 221 ? 92.406  -16.895 7.915   1.00 9.40  ? 223  VAL A O   1 
ATOM   1686 C  CB  . VAL A 1 221 ? 92.457  -15.733 11.074  1.00 8.59  ? 223  VAL A CB  1 
ATOM   1687 C  CG1 . VAL A 1 221 ? 93.309  -14.770 10.256  1.00 8.25  ? 223  VAL A CG1 1 
ATOM   1688 C  CG2 . VAL A 1 221 ? 91.579  -14.970 12.057  1.00 8.61  ? 223  VAL A CG2 1 
ATOM   1689 N  N   . PRO A 1 222 ? 93.126  -18.375 9.461   1.00 9.29  ? 224  PRO A N   1 
ATOM   1690 C  CA  . PRO A 1 222 ? 93.914  -19.100 8.463   1.00 9.56  ? 224  PRO A CA  1 
ATOM   1691 C  C   . PRO A 1 222 ? 93.038  -19.665 7.347   1.00 9.66  ? 224  PRO A C   1 
ATOM   1692 O  O   . PRO A 1 222 ? 93.436  -19.656 6.181   1.00 9.60  ? 224  PRO A O   1 
ATOM   1693 C  CB  . PRO A 1 222 ? 94.541  -20.237 9.275   1.00 9.89  ? 224  PRO A CB  1 
ATOM   1694 C  CG  . PRO A 1 222 ? 94.616  -19.698 10.666  1.00 9.55  ? 224  PRO A CG  1 
ATOM   1695 C  CD  . PRO A 1 222 ? 93.375  -18.866 10.828  1.00 9.30  ? 224  PRO A CD  1 
ATOM   1696 N  N   . GLU A 1 223 ? 91.839  -20.117 7.703   1.00 10.05 ? 225  GLU A N   1 
ATOM   1697 C  CA  . GLU A 1 223 ? 90.895  -20.651 6.726   1.00 10.63 ? 225  GLU A CA  1 
ATOM   1698 C  C   . GLU A 1 223 ? 90.369  -19.553 5.791   1.00 10.44 ? 225  GLU A C   1 
ATOM   1699 O  O   . GLU A 1 223 ? 90.275  -19.746 4.579   1.00 11.03 ? 225  GLU A O   1 
ATOM   1700 C  CB  . GLU A 1 223 ? 89.737  -21.362 7.437   1.00 10.49 ? 225  GLU A CB  1 
ATOM   1701 C  CG  . GLU A 1 223 ? 90.134  -22.656 8.139   1.00 10.70 ? 225  GLU A CG  1 
ATOM   1702 C  CD  . GLU A 1 223 ? 90.593  -22.452 9.577   1.00 11.10 ? 225  GLU A CD  1 
ATOM   1703 O  OE1 . GLU A 1 223 ? 91.003  -21.324 9.942   1.00 11.15 ? 225  GLU A OE1 1 
ATOM   1704 O  OE2 . GLU A 1 223 ? 90.581  -23.439 10.343  1.00 11.23 ? 225  GLU A OE2 1 
ATOM   1705 N  N   . PHE A 1 224 ? 90.061  -18.393 6.363   1.00 10.43 ? 226  PHE A N   1 
ATOM   1706 C  CA  . PHE A 1 224 ? 89.682  -17.211 5.593   1.00 10.35 ? 226  PHE A CA  1 
ATOM   1707 C  C   . PHE A 1 224 ? 90.766  -16.856 4.577   1.00 10.71 ? 226  PHE A C   1 
ATOM   1708 O  O   . PHE A 1 224 ? 90.494  -16.704 3.381   1.00 10.04 ? 226  PHE A O   1 
ATOM   1709 C  CB  . PHE A 1 224 ? 89.442  -16.041 6.554   1.00 10.43 ? 226  PHE A CB  1 
ATOM   1710 C  CG  . PHE A 1 224 ? 89.126  -14.733 5.879   1.00 10.51 ? 226  PHE A CG  1 
ATOM   1711 C  CD1 . PHE A 1 224 ? 87.861  -14.485 5.376   1.00 11.31 ? 226  PHE A CD1 1 
ATOM   1712 C  CD2 . PHE A 1 224 ? 90.058  -13.706 5.867   1.00 10.76 ? 226  PHE A CD2 1 
ATOM   1713 C  CE1 . PHE A 1 224 ? 87.545  -13.256 4.824   1.00 11.42 ? 226  PHE A CE1 1 
ATOM   1714 C  CE2 . PHE A 1 224 ? 89.757  -12.479 5.302   1.00 11.25 ? 226  PHE A CE2 1 
ATOM   1715 C  CZ  . PHE A 1 224 ? 88.494  -12.250 4.786   1.00 11.26 ? 226  PHE A CZ  1 
ATOM   1716 N  N   . ASN A 1 225 ? 92.004  -16.767 5.050   1.00 10.36 ? 227  ASN A N   1 
ATOM   1717 C  CA  . ASN A 1 225 ? 93.107  -16.359 4.195   1.00 9.80  ? 227  ASN A CA  1 
ATOM   1718 C  C   . ASN A 1 225 ? 93.378  -17.359 3.076   1.00 9.52  ? 227  ASN A C   1 
ATOM   1719 O  O   . ASN A 1 225 ? 93.645  -16.971 1.941   1.00 8.54  ? 227  ASN A O   1 
ATOM   1720 C  CB  . ASN A 1 225 ? 94.365  -16.101 5.027   1.00 9.83  ? 227  ASN A CB  1 
ATOM   1721 C  CG  . ASN A 1 225 ? 94.269  -14.819 5.833   1.00 10.23 ? 227  ASN A CG  1 
ATOM   1722 O  OD1 . ASN A 1 225 ? 93.584  -13.878 5.433   1.00 11.17 ? 227  ASN A OD1 1 
ATOM   1723 N  ND2 . ASN A 1 225 ? 94.935  -14.784 6.982   1.00 10.20 ? 227  ASN A ND2 1 
ATOM   1724 N  N   . LYS A 1 226 ? 93.269  -18.645 3.390   1.00 9.89  ? 228  LYS A N   1 
ATOM   1725 C  CA  . LYS A 1 226 ? 93.399  -19.688 2.378   1.00 10.41 ? 228  LYS A CA  1 
ATOM   1726 C  C   . LYS A 1 226 ? 92.306  -19.582 1.316   1.00 10.21 ? 228  LYS A C   1 
ATOM   1727 O  O   . LYS A 1 226 ? 92.583  -19.685 0.117   1.00 9.88  ? 228  LYS A O   1 
ATOM   1728 C  CB  . LYS A 1 226 ? 93.384  -21.074 3.025   1.00 11.17 ? 228  LYS A CB  1 
ATOM   1729 C  CG  . LYS A 1 226 ? 93.463  -22.226 2.032   1.00 12.77 ? 228  LYS A CG  1 
ATOM   1730 C  CD  . LYS A 1 226 ? 93.340  -23.570 2.733   1.00 13.55 ? 228  LYS A CD  1 
ATOM   1731 C  CE  . LYS A 1 226 ? 93.083  -24.692 1.739   1.00 15.22 ? 228  LYS A CE  1 
ATOM   1732 N  NZ  . LYS A 1 226 ? 94.253  -24.900 0.842   1.00 16.06 ? 228  LYS A NZ  1 
ATOM   1733 N  N   . TYR A 1 227 ? 91.068  -19.364 1.753   1.00 10.27 ? 229  TYR A N   1 
ATOM   1734 C  CA  . TYR A 1 227 ? 89.953  -19.236 0.820   1.00 10.84 ? 229  TYR A CA  1 
ATOM   1735 C  C   . TYR A 1 227 ? 90.173  -18.091 -0.161  1.00 11.01 ? 229  TYR A C   1 
ATOM   1736 O  O   . TYR A 1 227 ? 89.917  -18.227 -1.360  1.00 11.14 ? 229  TYR A O   1 
ATOM   1737 C  CB  . TYR A 1 227 ? 88.622  -19.051 1.556   1.00 11.46 ? 229  TYR A CB  1 
ATOM   1738 C  CG  . TYR A 1 227 ? 87.428  -19.086 0.631   1.00 12.19 ? 229  TYR A CG  1 
ATOM   1739 C  CD1 . TYR A 1 227 ? 87.032  -17.949 -0.067  1.00 11.53 ? 229  TYR A CD1 1 
ATOM   1740 C  CD2 . TYR A 1 227 ? 86.727  -20.268 0.413   1.00 12.20 ? 229  TYR A CD2 1 
ATOM   1741 C  CE1 . TYR A 1 227 ? 85.969  -17.986 -0.949  1.00 11.69 ? 229  TYR A CE1 1 
ATOM   1742 C  CE2 . TYR A 1 227 ? 85.661  -20.314 -0.466  1.00 12.27 ? 229  TYR A CE2 1 
ATOM   1743 C  CZ  . TYR A 1 227 ? 85.284  -19.170 -1.139  1.00 12.15 ? 229  TYR A CZ  1 
ATOM   1744 O  OH  . TYR A 1 227 ? 84.247  -19.216 -2.040  1.00 12.64 ? 229  TYR A OH  1 
ATOM   1745 N  N   . LEU A 1 228 ? 90.650  -16.962 0.350   1.00 11.21 ? 230  LEU A N   1 
ATOM   1746 C  CA  . LEU A 1 228 ? 90.953  -15.817 -0.504  1.00 11.29 ? 230  LEU A CA  1 
ATOM   1747 C  C   . LEU A 1 228 ? 92.011  -16.144 -1.557  1.00 11.68 ? 230  LEU A C   1 
ATOM   1748 O  O   . LEU A 1 228 ? 91.863  -15.785 -2.731  1.00 12.50 ? 230  LEU A O   1 
ATOM   1749 C  CB  . LEU A 1 228 ? 91.375  -14.609 0.335   1.00 10.62 ? 230  LEU A CB  1 
ATOM   1750 C  CG  . LEU A 1 228 ? 90.332  -14.089 1.329   1.00 10.70 ? 230  LEU A CG  1 
ATOM   1751 C  CD1 . LEU A 1 228 ? 90.843  -12.849 2.045   1.00 10.95 ? 230  LEU A CD1 1 
ATOM   1752 C  CD2 . LEU A 1 228 ? 89.009  -13.798 0.635   1.00 10.71 ? 230  LEU A CD2 1 
ATOM   1753 N  N   . LEU A 1 229 ? 93.066  -16.842 -1.143  1.00 12.12 ? 231  LEU A N   1 
ATOM   1754 C  CA  . LEU A 1 229 ? 94.111  -17.266 -2.071  1.00 12.52 ? 231  LEU A CA  1 
ATOM   1755 C  C   . LEU A 1 229 ? 93.549  -18.197 -3.141  1.00 12.87 ? 231  LEU A C   1 
ATOM   1756 O  O   . LEU A 1 229 ? 93.848  -18.050 -4.327  1.00 12.99 ? 231  LEU A O   1 
ATOM   1757 C  CB  . LEU A 1 229 ? 95.244  -17.980 -1.324  1.00 13.20 ? 231  LEU A CB  1 
ATOM   1758 C  CG  . LEU A 1 229 ? 96.330  -17.134 -0.654  1.00 14.19 ? 231  LEU A CG  1 
ATOM   1759 C  CD1 . LEU A 1 229 ? 97.415  -18.038 -0.084  1.00 14.69 ? 231  LEU A CD1 1 
ATOM   1760 C  CD2 . LEU A 1 229 ? 96.931  -16.136 -1.633  1.00 13.53 ? 231  LEU A CD2 1 
ATOM   1761 N  N   . ASP A 1 230 ? 92.757  -19.174 -2.711  1.00 13.00 ? 232  ASP A N   1 
ATOM   1762 C  CA  . ASP A 1 230 ? 92.288  -20.229 -3.606  1.00 14.32 ? 232  ASP A CA  1 
ATOM   1763 C  C   . ASP A 1 230 ? 91.210  -19.740 -4.568  1.00 14.18 ? 232  ASP A C   1 
ATOM   1764 O  O   . ASP A 1 230 ? 91.045  -20.289 -5.656  1.00 14.67 ? 232  ASP A O   1 
ATOM   1765 C  CB  . ASP A 1 230 ? 91.769  -21.420 -2.805  1.00 14.61 ? 232  ASP A CB  1 
ATOM   1766 C  CG  . ASP A 1 230 ? 92.881  -22.191 -2.128  1.00 15.64 ? 232  ASP A CG  1 
ATOM   1767 O  OD1 . ASP A 1 230 ? 94.062  -21.926 -2.432  1.00 15.99 ? 232  ASP A OD1 1 
ATOM   1768 O  OD2 . ASP A 1 230 ? 92.575  -23.055 -1.283  1.00 17.21 ? 232  ASP A OD2 1 
ATOM   1769 N  N   . ASN A 1 231 ? 90.494  -18.692 -4.176  1.00 12.91 ? 233  ASN A N   1 
ATOM   1770 C  CA  . ASN A 1 231 ? 89.361  -18.219 -4.957  1.00 12.73 ? 233  ASN A CA  1 
ATOM   1771 C  C   . ASN A 1 231 ? 89.564  -16.821 -5.531  1.00 12.77 ? 233  ASN A C   1 
ATOM   1772 O  O   . ASN A 1 231 ? 88.657  -16.259 -6.143  1.00 13.91 ? 233  ASN A O   1 
ATOM   1773 C  CB  . ASN A 1 231 ? 88.081  -18.277 -4.123  1.00 12.31 ? 233  ASN A CB  1 
ATOM   1774 C  CG  . ASN A 1 231 ? 87.659  -19.697 -3.810  1.00 12.85 ? 233  ASN A CG  1 
ATOM   1775 O  OD1 . ASN A 1 231 ? 87.019  -20.359 -4.627  1.00 13.08 ? 233  ASN A OD1 1 
ATOM   1776 N  ND2 . ASN A 1 231 ? 88.062  -20.193 -2.645  1.00 12.11 ? 233  ASN A ND2 1 
ATOM   1777 N  N   . ALA A 1 232 ? 90.755  -16.266 -5.330  1.00 12.98 ? 234  ALA A N   1 
ATOM   1778 C  CA  . ALA A 1 232 ? 91.113  -14.981 -5.922  1.00 13.04 ? 234  ALA A CA  1 
ATOM   1779 C  C   . ALA A 1 232 ? 90.750  -14.970 -7.403  1.00 13.70 ? 234  ALA A C   1 
ATOM   1780 O  O   . ALA A 1 232 ? 91.077  -15.905 -8.130  1.00 12.61 ? 234  ALA A O   1 
ATOM   1781 C  CB  . ALA A 1 232 ? 92.601  -14.715 -5.746  1.00 12.10 ? 234  ALA A CB  1 
ATOM   1782 N  N   . PRO A 1 233 ? 90.093  -13.897 -7.860  1.00 14.96 ? 235  PRO A N   1 
ATOM   1783 C  CA  . PRO A 1 233 ? 89.765  -13.799 -9.281  1.00 15.25 ? 235  PRO A CA  1 
ATOM   1784 C  C   . PRO A 1 233 ? 91.025  -13.767 -10.144 1.00 15.86 ? 235  PRO A C   1 
ATOM   1785 O  O   . PRO A 1 233 ? 92.060  -13.266 -9.708  1.00 14.61 ? 235  PRO A O   1 
ATOM   1786 C  CB  . PRO A 1 233 ? 89.029  -12.459 -9.376  1.00 16.34 ? 235  PRO A CB  1 
ATOM   1787 C  CG  . PRO A 1 233 ? 89.564  -11.657 -8.236  1.00 17.03 ? 235  PRO A CG  1 
ATOM   1788 C  CD  . PRO A 1 233 ? 89.824  -12.643 -7.134  1.00 15.50 ? 235  PRO A CD  1 
ATOM   1789 N  N   . ALA A 1 234 ? 90.941  -14.325 -11.348 1.00 16.73 ? 236  ALA A N   1 
ATOM   1790 C  CA  . ALA A 1 234 ? 91.985  -14.138 -12.350 1.00 16.04 ? 236  ALA A CA  1 
ATOM   1791 C  C   . ALA A 1 234 ? 92.280  -12.651 -12.536 1.00 15.99 ? 236  ALA A C   1 
ATOM   1792 O  O   . ALA A 1 234 ? 91.448  -11.801 -12.216 1.00 16.90 ? 236  ALA A O   1 
ATOM   1793 C  CB  . ALA A 1 234 ? 91.565  -14.764 -13.671 1.00 17.29 ? 236  ALA A CB  1 
ATOM   1794 N  N   . GLY A 1 235 ? 93.466  -12.338 -13.043 1.00 14.73 ? 237  GLY A N   1 
ATOM   1795 C  CA  . GLY A 1 235 ? 93.830  -10.948 -13.300 1.00 14.73 ? 237  GLY A CA  1 
ATOM   1796 C  C   . GLY A 1 235 ? 95.327  -10.751 -13.413 1.00 14.91 ? 237  GLY A C   1 
ATOM   1797 O  O   . GLY A 1 235 ? 96.107  -11.631 -13.036 1.00 14.49 ? 237  GLY A O   1 
ATOM   1798 N  N   . SER A 1 236 ? 95.730  -9.594  -13.932 1.00 14.13 ? 238  SER A N   1 
ATOM   1799 C  CA  . SER A 1 236 ? 97.143  -9.305  -14.157 1.00 14.61 ? 238  SER A CA  1 
ATOM   1800 C  C   . SER A 1 236 ? 97.864  -8.878  -12.881 1.00 14.03 ? 238  SER A C   1 
ATOM   1801 O  O   . SER A 1 236 ? 99.093  -8.848  -12.839 1.00 15.06 ? 238  SER A O   1 
ATOM   1802 C  CB  . SER A 1 236 ? 97.312  -8.236  -15.241 1.00 14.61 ? 238  SER A CB  1 
ATOM   1803 O  OG  . SER A 1 236 ? 96.634  -7.043  -14.888 1.00 15.26 ? 238  SER A OG  1 
ATOM   1804 N  N   . GLY A 1 237 ? 97.100  -8.547  -11.846 1.00 13.91 ? 239  GLY A N   1 
ATOM   1805 C  CA  . GLY A 1 237 ? 97.677  -8.251  -10.537 1.00 12.73 ? 239  GLY A CA  1 
ATOM   1806 C  C   . GLY A 1 237 ? 98.380  -9.467  -9.964  1.00 12.47 ? 239  GLY A C   1 
ATOM   1807 O  O   . GLY A 1 237 ? 98.203  -10.584 -10.454 1.00 13.17 ? 239  GLY A O   1 
ATOM   1808 N  N   . SER A 1 238 ? 99.181  -9.258  -8.925  1.00 10.95 ? 240  SER A N   1 
ATOM   1809 C  CA  . SER A 1 238 ? 99.829  -10.375 -8.248  1.00 11.35 ? 240  SER A CA  1 
ATOM   1810 C  C   . SER A 1 238 ? 98.782  -11.226 -7.537  1.00 10.81 ? 240  SER A C   1 
ATOM   1811 O  O   . SER A 1 238 ? 97.660  -10.780 -7.301  1.00 9.39  ? 240  SER A O   1 
ATOM   1812 C  CB  . SER A 1 238 ? 100.878 -9.877  -7.251  1.00 10.94 ? 240  SER A CB  1 
ATOM   1813 O  OG  . SER A 1 238 ? 100.272 -9.228  -6.145  1.00 10.04 ? 240  SER A OG  1 
ATOM   1814 N  N   . LEU A 1 239 ? 99.145  -12.460 -7.210  1.00 10.72 ? 241  LEU A N   1 
ATOM   1815 C  CA  . LEU A 1 239 ? 98.244  -13.324 -6.466  1.00 10.71 ? 241  LEU A CA  1 
ATOM   1816 C  C   . LEU A 1 239 ? 97.796  -12.672 -5.162  1.00 10.32 ? 241  LEU A C   1 
ATOM   1817 O  O   . LEU A 1 239 ? 96.627  -12.736 -4.807  1.00 10.04 ? 241  LEU A O   1 
ATOM   1818 C  CB  . LEU A 1 239 ? 98.900  -14.674 -6.178  1.00 11.13 ? 241  LEU A CB  1 
ATOM   1819 C  CG  . LEU A 1 239 ? 98.028  -15.638 -5.374  1.00 11.15 ? 241  LEU A CG  1 
ATOM   1820 C  CD1 . LEU A 1 239 ? 96.755  -15.971 -6.140  1.00 11.27 ? 241  LEU A CD1 1 
ATOM   1821 C  CD2 . LEU A 1 239 ? 98.807  -16.897 -5.032  1.00 11.37 ? 241  LEU A CD2 1 
ATOM   1822 N  N   . GLN A 1 240 ? 98.726  -12.054 -4.442  1.00 11.04 ? 242  GLN A N   1 
ATOM   1823 C  CA  . GLN A 1 240 ? 98.377  -11.450 -3.162  1.00 11.69 ? 242  GLN A CA  1 
ATOM   1824 C  C   . GLN A 1 240 ? 97.402  -10.301 -3.362  1.00 11.24 ? 242  GLN A C   1 
ATOM   1825 O  O   . GLN A 1 240 ? 96.463  -10.131 -2.583  1.00 11.49 ? 242  GLN A O   1 
ATOM   1826 C  CB  . GLN A 1 240 ? 99.609  -10.955 -2.409  1.00 13.14 ? 242  GLN A CB  1 
ATOM   1827 C  CG  . GLN A 1 240 ? 99.297  -10.533 -0.979  1.00 13.80 ? 242  GLN A CG  1 
ATOM   1828 C  CD  . GLN A 1 240 ? 98.853  -11.699 -0.116  1.00 14.63 ? 242  GLN A CD  1 
ATOM   1829 O  OE1 . GLN A 1 240 ? 97.737  -11.714 0.411   1.00 18.39 ? 242  GLN A OE1 1 
ATOM   1830 N  NE2 . GLN A 1 240 ? 99.713  -12.703 0.004   1.00 14.35 ? 242  GLN A NE2 1 
ATOM   1831 N  N   . ALA A 1 241 ? 97.629  -9.518  -4.413  1.00 10.49 ? 243  ALA A N   1 
ATOM   1832 C  CA  . ALA A 1 241 ? 96.788  -8.366  -4.698  1.00 9.90  ? 243  ALA A CA  1 
ATOM   1833 C  C   . ALA A 1 241 ? 95.363  -8.819  -4.972  1.00 9.80  ? 243  ALA A C   1 
ATOM   1834 O  O   . ALA A 1 241 ? 94.407  -8.212  -4.492  1.00 10.01 ? 243  ALA A O   1 
ATOM   1835 C  CB  . ALA A 1 241 ? 97.336  -7.583  -5.881  1.00 9.56  ? 243  ALA A CB  1 
ATOM   1836 N  N   . ARG A 1 242 ? 95.226  -9.902  -5.730  1.00 9.59  ? 244  ARG A N   1 
ATOM   1837 C  CA  . ARG A 1 242 ? 93.910  -10.379 -6.133  1.00 9.57  ? 244  ARG A CA  1 
ATOM   1838 C  C   . ARG A 1 242 ? 93.190  -11.109 -4.999  1.00 9.44  ? 244  ARG A C   1 
ATOM   1839 O  O   . ARG A 1 242 ? 91.964  -11.034 -4.882  1.00 8.88  ? 244  ARG A O   1 
ATOM   1840 C  CB  . ARG A 1 242 ? 94.011  -11.249 -7.390  1.00 10.46 ? 244  ARG A CB  1 
ATOM   1841 C  CG  . ARG A 1 242 ? 94.553  -10.491 -8.599  1.00 10.59 ? 244  ARG A CG  1 
ATOM   1842 C  CD  . ARG A 1 242 ? 94.635  -11.364 -9.843  1.00 11.66 ? 244  ARG A CD  1 
ATOM   1843 N  NE  . ARG A 1 242 ? 95.830  -12.210 -9.862  1.00 12.07 ? 244  ARG A NE  1 
ATOM   1844 C  CZ  . ARG A 1 242 ? 95.827  -13.517 -9.614  1.00 12.10 ? 244  ARG A CZ  1 
ATOM   1845 N  NH1 . ARG A 1 242 ? 94.698  -14.136 -9.292  1.00 11.67 ? 244  ARG A NH1 1 
ATOM   1846 N  NH2 . ARG A 1 242 ? 96.956  -14.206 -9.675  1.00 12.93 ? 244  ARG A NH2 1 
ATOM   1847 N  N   . ALA A 1 243 ? 93.957  -11.774 -4.137  1.00 8.98  ? 245  ALA A N   1 
ATOM   1848 C  CA  . ALA A 1 243 ? 93.404  -12.316 -2.894  1.00 9.22  ? 245  ALA A CA  1 
ATOM   1849 C  C   . ALA A 1 243 ? 92.919  -11.194 -1.981  1.00 9.71  ? 245  ALA A C   1 
ATOM   1850 O  O   . ALA A 1 243 ? 91.819  -11.261 -1.427  1.00 9.85  ? 245  ALA A O   1 
ATOM   1851 C  CB  . ALA A 1 243 ? 94.436  -13.173 -2.177  1.00 8.82  ? 245  ALA A CB  1 
ATOM   1852 N  N   . ASP A 1 244 ? 93.759  -10.179 -1.804  1.00 10.20 ? 246  ASP A N   1 
ATOM   1853 C  CA  . ASP A 1 244 ? 93.407  -9.028  -0.980  1.00 10.39 ? 246  ASP A CA  1 
ATOM   1854 C  C   . ASP A 1 244 ? 92.141  -8.359  -1.510  1.00 9.84  ? 246  ASP A C   1 
ATOM   1855 O  O   . ASP A 1 244 ? 91.299  -7.893  -0.735  1.00 9.97  ? 246  ASP A O   1 
ATOM   1856 C  CB  . ASP A 1 244 ? 94.550  -8.006  -0.965  1.00 11.38 ? 246  ASP A CB  1 
ATOM   1857 C  CG  . ASP A 1 244 ? 95.709  -8.420  -0.071  1.00 12.58 ? 246  ASP A CG  1 
ATOM   1858 O  OD1 . ASP A 1 244 ? 95.622  -9.456  0.624   1.00 14.15 ? 246  ASP A OD1 1 
ATOM   1859 O  OD2 . ASP A 1 244 ? 96.717  -7.686  -0.058  1.00 12.85 ? 246  ASP A OD2 1 
ATOM   1860 N  N   . LEU A 1 245 ? 92.041  -8.259  -2.834  1.00 9.18  ? 247  LEU A N   1 
ATOM   1861 C  CA  . LEU A 1 245 ? 90.878  -7.661  -3.474  1.00 9.10  ? 247  LEU A CA  1 
ATOM   1862 C  C   . LEU A 1 245 ? 89.600  -8.420  -3.113  1.00 8.98  ? 247  LEU A C   1 
ATOM   1863 O  O   . LEU A 1 245 ? 88.574  -7.813  -2.803  1.00 8.40  ? 247  LEU A O   1 
ATOM   1864 C  CB  . LEU A 1 245 ? 91.063  -7.618  -4.996  1.00 9.16  ? 247  LEU A CB  1 
ATOM   1865 C  CG  . LEU A 1 245 ? 89.824  -7.272  -5.822  1.00 9.87  ? 247  LEU A CG  1 
ATOM   1866 C  CD1 . LEU A 1 245 ? 89.381  -5.840  -5.560  1.00 9.76  ? 247  LEU A CD1 1 
ATOM   1867 C  CD2 . LEU A 1 245 ? 90.089  -7.499  -7.304  1.00 10.49 ? 247  LEU A CD2 1 
ATOM   1868 N  N   . LEU A 1 246 ? 89.671  -9.747  -3.120  1.00 8.51  ? 248  LEU A N   1 
ATOM   1869 C  CA  . LEU A 1 246 ? 88.493  -10.551 -2.804  1.00 8.66  ? 248  LEU A CA  1 
ATOM   1870 C  C   . LEU A 1 246 ? 88.076  -10.360 -1.349  1.00 8.75  ? 248  LEU A C   1 
ATOM   1871 O  O   . LEU A 1 246 ? 86.891  -10.205 -1.052  1.00 9.07  ? 248  LEU A O   1 
ATOM   1872 C  CB  . LEU A 1 246 ? 88.734  -12.031 -3.111  1.00 8.18  ? 248  LEU A CB  1 
ATOM   1873 C  CG  . LEU A 1 246 ? 87.543  -12.978 -2.902  1.00 8.32  ? 248  LEU A CG  1 
ATOM   1874 C  CD1 . LEU A 1 246 ? 86.344  -12.585 -3.754  1.00 8.31  ? 248  LEU A CD1 1 
ATOM   1875 C  CD2 . LEU A 1 246 ? 87.950  -14.415 -3.175  1.00 7.95  ? 248  LEU A CD2 1 
ATOM   1876 N  N   . GLY A 1 247 ? 89.057  -10.336 -0.451  1.00 8.74  ? 249  GLY A N   1 
ATOM   1877 C  CA  . GLY A 1 247 ? 88.806  -10.017 0.950   1.00 8.31  ? 249  GLY A CA  1 
ATOM   1878 C  C   . GLY A 1 247 ? 88.085  -8.692  1.106   1.00 8.49  ? 249  GLY A C   1 
ATOM   1879 O  O   . GLY A 1 247 ? 87.105  -8.590  1.845   1.00 8.21  ? 249  GLY A O   1 
ATOM   1880 N  N   . ALA A 1 248 ? 88.576  -7.668  0.415   1.00 8.42  ? 250  ALA A N   1 
ATOM   1881 C  CA  . ALA A 1 248 ? 88.004  -6.331  0.534   1.00 8.47  ? 250  ALA A CA  1 
ATOM   1882 C  C   . ALA A 1 248 ? 86.583  -6.288  -0.019  1.00 8.60  ? 250  ALA A C   1 
ATOM   1883 O  O   . ALA A 1 248 ? 85.725  -5.576  0.496   1.00 8.28  ? 250  ALA A O   1 
ATOM   1884 C  CB  . ALA A 1 248 ? 88.886  -5.309  -0.167  1.00 8.25  ? 250  ALA A CB  1 
ATOM   1885 N  N   . ARG A 1 249 ? 86.336  -7.044  -1.080  1.00 9.47  ? 251  ARG A N   1 
ATOM   1886 C  CA  . ARG A 1 249 ? 85.009  -7.063  -1.678  1.00 9.75  ? 251  ARG A CA  1 
ATOM   1887 C  C   . ARG A 1 249 ? 83.990  -7.822  -0.828  1.00 9.37  ? 251  ARG A C   1 
ATOM   1888 O  O   . ARG A 1 249 ? 82.794  -7.536  -0.883  1.00 9.33  ? 251  ARG A O   1 
ATOM   1889 C  CB  . ARG A 1 249 ? 85.068  -7.576  -3.120  1.00 11.51 ? 251  ARG A CB  1 
ATOM   1890 C  CG  . ARG A 1 249 ? 85.513  -6.490  -4.092  1.00 12.60 ? 251  ARG A CG  1 
ATOM   1891 C  CD  . ARG A 1 249 ? 85.529  -6.946  -5.538  1.00 13.35 ? 251  ARG A CD  1 
ATOM   1892 N  NE  . ARG A 1 249 ? 84.197  -7.240  -6.060  1.00 13.06 ? 251  ARG A NE  1 
ATOM   1893 C  CZ  . ARG A 1 249 ? 83.408  -6.362  -6.678  1.00 12.74 ? 251  ARG A CZ  1 
ATOM   1894 N  NH1 . ARG A 1 249 ? 83.757  -5.084  -6.771  1.00 13.34 ? 251  ARG A NH1 1 
ATOM   1895 N  NH2 . ARG A 1 249 ? 82.234  -6.756  -7.151  1.00 11.91 ? 251  ARG A NH2 1 
ATOM   1896 N  N   . MET A 1 250 ? 84.475  -8.727  0.019   1.00 8.98  ? 252  MET A N   1 
ATOM   1897 C  CA  . MET A 1 250 ? 83.626  -9.360  1.027   1.00 9.19  ? 252  MET A CA  1 
ATOM   1898 C  C   . MET A 1 250 ? 83.264  -8.404  2.158   1.00 8.61  ? 252  MET A C   1 
ATOM   1899 O  O   . MET A 1 250 ? 82.134  -8.404  2.643   1.00 8.74  ? 252  MET A O   1 
ATOM   1900 C  CB  . MET A 1 250 ? 84.304  -10.604 1.607   1.00 9.90  ? 252  MET A CB  1 
ATOM   1901 C  CG  . MET A 1 250 ? 84.255  -11.812 0.692   1.00 11.04 ? 252  MET A CG  1 
ATOM   1902 S  SD  . MET A 1 250 ? 85.089  -13.236 1.422   1.00 12.93 ? 252  MET A SD  1 
ATOM   1903 C  CE  . MET A 1 250 ? 85.204  -14.305 -0.009  1.00 12.02 ? 252  MET A CE  1 
ATOM   1904 N  N   . VAL A 1 251 ? 84.239  -7.624  2.610   1.00 8.43  ? 253  VAL A N   1 
ATOM   1905 C  CA  . VAL A 1 251 ? 84.034  -6.747  3.757   1.00 8.36  ? 253  VAL A CA  1 
ATOM   1906 C  C   . VAL A 1 251 ? 83.335  -5.454  3.340   1.00 8.11  ? 253  VAL A C   1 
ATOM   1907 O  O   . VAL A 1 251 ? 82.422  -4.984  4.022   1.00 7.52  ? 253  VAL A O   1 
ATOM   1908 C  CB  . VAL A 1 251 ? 85.367  -6.415  4.461   1.00 8.56  ? 253  VAL A CB  1 
ATOM   1909 C  CG1 . VAL A 1 251 ? 85.157  -5.364  5.541   1.00 8.37  ? 253  VAL A CG1 1 
ATOM   1910 C  CG2 . VAL A 1 251 ? 85.988  -7.675  5.048   1.00 8.33  ? 253  VAL A CG2 1 
ATOM   1911 N  N   . GLY A 1 252 ? 83.752  -4.904  2.203   1.00 7.84  ? 254  GLY A N   1 
ATOM   1912 C  CA  . GLY A 1 252 ? 83.320  -3.572  1.781   1.00 7.96  ? 254  GLY A CA  1 
ATOM   1913 C  C   . GLY A 1 252 ? 84.350  -2.499  2.086   1.00 7.89  ? 254  GLY A C   1 
ATOM   1914 O  O   . GLY A 1 252 ? 84.167  -1.335  1.733   1.00 7.92  ? 254  GLY A O   1 
ATOM   1915 N  N   . ARG A 1 253 ? 85.419  -2.887  2.776   1.00 7.81  ? 255  ARG A N   1 
ATOM   1916 C  CA  . ARG A 1 253 ? 86.557  -1.998  3.019   1.00 7.98  ? 255  ARG A CA  1 
ATOM   1917 C  C   . ARG A 1 253 ? 87.858  -2.770  2.845   1.00 8.41  ? 255  ARG A C   1 
ATOM   1918 O  O   . ARG A 1 253 ? 87.902  -3.975  3.076   1.00 8.44  ? 255  ARG A O   1 
ATOM   1919 C  CB  . ARG A 1 253 ? 86.514  -1.427  4.443   1.00 7.89  ? 255  ARG A CB  1 
ATOM   1920 C  CG  . ARG A 1 253 ? 85.303  -0.571  4.756   1.00 7.93  ? 255  ARG A CG  1 
ATOM   1921 C  CD  . ARG A 1 253 ? 85.441  0.097   6.118   1.00 8.25  ? 255  ARG A CD  1 
ATOM   1922 N  NE  . ARG A 1 253 ? 84.318  0.993   6.382   1.00 8.06  ? 255  ARG A NE  1 
ATOM   1923 C  CZ  . ARG A 1 253 ? 84.279  2.273   6.027   1.00 8.39  ? 255  ARG A CZ  1 
ATOM   1924 N  NH1 . ARG A 1 253 ? 85.324  2.831   5.427   1.00 8.44  ? 255  ARG A NH1 1 
ATOM   1925 N  NH2 . ARG A 1 253 ? 83.194  2.999   6.276   1.00 8.28  ? 255  ARG A NH2 1 
ATOM   1926 N  N   . TRP A 1 254 ? 88.918  -2.071  2.450   1.00 8.90  ? 256  TRP A N   1 
ATOM   1927 C  CA  . TRP A 1 254 ? 90.265  -2.621  2.534   1.00 8.99  ? 256  TRP A CA  1 
ATOM   1928 C  C   . TRP A 1 254 ? 90.719  -2.634  3.990   1.00 9.17  ? 256  TRP A C   1 
ATOM   1929 O  O   . TRP A 1 254 ? 90.098  -2.007  4.843   1.00 9.15  ? 256  TRP A O   1 
ATOM   1930 C  CB  . TRP A 1 254 ? 91.230  -1.791  1.686   1.00 9.29  ? 256  TRP A CB  1 
ATOM   1931 C  CG  . TRP A 1 254 ? 90.840  -1.744  0.244   1.00 9.52  ? 256  TRP A CG  1 
ATOM   1932 C  CD1 . TRP A 1 254 ? 90.002  -0.848  -0.348  1.00 9.60  ? 256  TRP A CD1 1 
ATOM   1933 C  CD2 . TRP A 1 254 ? 91.233  -2.665  -0.778  1.00 9.70  ? 256  TRP A CD2 1 
ATOM   1934 N  NE1 . TRP A 1 254 ? 89.880  -1.127  -1.688  1.00 9.86  ? 256  TRP A NE1 1 
ATOM   1935 C  CE2 . TRP A 1 254 ? 90.618  -2.246  -1.976  1.00 10.19 ? 256  TRP A CE2 1 
ATOM   1936 C  CE3 . TRP A 1 254 ? 92.066  -3.789  -0.803  1.00 9.30  ? 256  TRP A CE3 1 
ATOM   1937 C  CZ2 . TRP A 1 254 ? 90.788  -2.926  -3.181  1.00 10.16 ? 256  TRP A CZ2 1 
ATOM   1938 C  CZ3 . TRP A 1 254 ? 92.226  -4.470  -1.999  1.00 9.48  ? 256  TRP A CZ3 1 
ATOM   1939 C  CH2 . TRP A 1 254 ? 91.599  -4.030  -3.174  1.00 9.34  ? 256  TRP A CH2 1 
ATOM   1940 N  N   . LYS A 1 255 ? 91.790  -3.365  4.275   1.00 9.89  ? 257  LYS A N   1 
ATOM   1941 C  CA  . LYS A 1 255 ? 92.255  -3.511  5.650   1.00 10.02 ? 257  LYS A CA  1 
ATOM   1942 C  C   . LYS A 1 255 ? 92.649  -2.175  6.282   1.00 10.14 ? 257  LYS A C   1 
ATOM   1943 O  O   . LYS A 1 255 ? 92.628  -2.028  7.502   1.00 10.81 ? 257  LYS A O   1 
ATOM   1944 C  CB  . LYS A 1 255 ? 93.416  -4.505  5.724   1.00 11.16 ? 257  LYS A CB  1 
ATOM   1945 C  CG  . LYS A 1 255 ? 93.002  -5.944  5.461   1.00 12.00 ? 257  LYS A CG  1 
ATOM   1946 C  CD  . LYS A 1 255 ? 94.186  -6.893  5.550   1.00 12.99 ? 257  LYS A CD  1 
ATOM   1947 C  CE  . LYS A 1 255 ? 93.741  -8.329  5.328   1.00 14.83 ? 257  LYS A CE  1 
ATOM   1948 N  NZ  . LYS A 1 255 ? 94.878  -9.288  5.395   1.00 16.00 ? 257  LYS A NZ  1 
ATOM   1949 N  N   . SER A 1 256 ? 92.980  -1.195  5.449   1.00 10.00 ? 258  SER A N   1 
ATOM   1950 C  CA  . SER A 1 256 ? 93.362  0.123   5.949   1.00 10.20 ? 258  SER A CA  1 
ATOM   1951 C  C   . SER A 1 256 ? 92.137  0.882   6.448   1.00 9.94  ? 258  SER A C   1 
ATOM   1952 O  O   . SER A 1 256 ? 92.263  1.907   7.120   1.00 10.18 ? 258  SER A O   1 
ATOM   1953 C  CB  . SER A 1 256 ? 94.035  0.931   4.844   1.00 10.79 ? 258  SER A CB  1 
ATOM   1954 O  OG  . SER A 1 256 ? 93.055  1.495   3.992   1.00 10.85 ? 258  SER A OG  1 
ATOM   1955 N  N   . GLY A 1 257 ? 90.956  0.396   6.085   1.00 9.68  ? 259  GLY A N   1 
ATOM   1956 C  CA  . GLY A 1 257 ? 89.719  1.120   6.354   1.00 10.31 ? 259  GLY A CA  1 
ATOM   1957 C  C   . GLY A 1 257 ? 89.160  1.863   5.152   1.00 10.28 ? 259  GLY A C   1 
ATOM   1958 O  O   . GLY A 1 257 ? 88.027  2.344   5.187   1.00 10.37 ? 259  GLY A O   1 
ATOM   1959 N  N   . ALA A 1 258 ? 89.950  1.980   4.090   1.00 10.47 ? 260  ALA A N   1 
ATOM   1960 C  CA  . ALA A 1 258 ? 89.463  2.632   2.876   1.00 10.35 ? 260  ALA A CA  1 
ATOM   1961 C  C   . ALA A 1 258 ? 88.259  1.876   2.321   1.00 10.06 ? 260  ALA A C   1 
ATOM   1962 O  O   . ALA A 1 258 ? 88.324  0.665   2.115   1.00 10.03 ? 260  ALA A O   1 
ATOM   1963 C  CB  . ALA A 1 258 ? 90.567  2.731   1.832   1.00 10.44 ? 260  ALA A CB  1 
ATOM   1964 N  N   . PRO A 1 259 ? 87.135  2.584   2.126   1.00 10.00 ? 261  PRO A N   1 
ATOM   1965 C  CA  . PRO A 1 259 ? 85.932  1.964   1.574   1.00 10.02 ? 261  PRO A CA  1 
ATOM   1966 C  C   . PRO A 1 259 ? 86.116  1.627   0.098   1.00 10.48 ? 261  PRO A C   1 
ATOM   1967 O  O   . PRO A 1 259 ? 86.536  2.483   -0.683  1.00 10.76 ? 261  PRO A O   1 
ATOM   1968 C  CB  . PRO A 1 259 ? 84.871  3.056   1.739   1.00 10.26 ? 261  PRO A CB  1 
ATOM   1969 C  CG  . PRO A 1 259 ? 85.639  4.333   1.713   1.00 10.17 ? 261  PRO A CG  1 
ATOM   1970 C  CD  . PRO A 1 259 ? 86.952  4.024   2.384   1.00 9.89  ? 261  PRO A CD  1 
ATOM   1971 N  N   . ILE A 1 260 ? 85.843  0.381   -0.277  1.00 10.19 ? 262  ILE A N   1 
ATOM   1972 C  CA  . ILE A 1 260 ? 86.082  -0.046  -1.651  1.00 10.60 ? 262  ILE A CA  1 
ATOM   1973 C  C   . ILE A 1 260 ? 85.210  0.745   -2.619  1.00 10.78 ? 262  ILE A C   1 
ATOM   1974 O  O   . ILE A 1 260 ? 85.578  0.944   -3.774  1.00 11.05 ? 262  ILE A O   1 
ATOM   1975 C  CB  . ILE A 1 260 ? 85.838  -1.554  -1.848  1.00 10.83 ? 262  ILE A CB  1 
ATOM   1976 C  CG1 . ILE A 1 260 ? 84.359  -1.899  -1.659  1.00 10.36 ? 262  ILE A CG1 1 
ATOM   1977 C  CG2 . ILE A 1 260 ? 86.708  -2.363  -0.903  1.00 10.98 ? 262  ILE A CG2 1 
ATOM   1978 C  CD1 . ILE A 1 260 ? 84.047  -3.353  -1.935  1.00 11.07 ? 262  ILE A CD1 1 
ATOM   1979 N  N   . ASP A 1 261 ? 84.062  1.211   -2.137  1.00 10.90 ? 263  ASP A N   1 
ATOM   1980 C  CA  . ASP A 1 261 ? 83.166  2.016   -2.959  1.00 11.67 ? 263  ASP A CA  1 
ATOM   1981 C  C   . ASP A 1 261 ? 83.879  3.225   -3.547  1.00 12.89 ? 263  ASP A C   1 
ATOM   1982 O  O   . ASP A 1 261 ? 83.583  3.647   -4.666  1.00 13.53 ? 263  ASP A O   1 
ATOM   1983 C  CB  . ASP A 1 261 ? 81.951  2.479   -2.155  1.00 11.82 ? 263  ASP A CB  1 
ATOM   1984 C  CG  . ASP A 1 261 ? 80.877  3.098   -3.032  1.00 12.46 ? 263  ASP A CG  1 
ATOM   1985 O  OD1 . ASP A 1 261 ? 80.368  2.394   -3.928  1.00 12.24 ? 263  ASP A OD1 1 
ATOM   1986 O  OD2 . ASP A 1 261 ? 80.536  4.282   -2.822  1.00 12.98 ? 263  ASP A OD2 1 
ATOM   1987 N  N   . LEU A 1 262 ? 84.795  3.801   -2.775  1.00 12.69 ? 264  LEU A N   1 
ATOM   1988 C  CA  . LEU A 1 262 ? 85.547  4.970   -3.225  1.00 13.49 ? 264  LEU A CA  1 
ATOM   1989 C  C   . LEU A 1 262 ? 86.886  4.609   -3.869  1.00 13.86 ? 264  LEU A C   1 
ATOM   1990 O  O   . LEU A 1 262 ? 87.523  5.453   -4.501  1.00 13.71 ? 264  LEU A O   1 
ATOM   1991 C  CB  . LEU A 1 262 ? 85.765  5.945   -2.067  1.00 13.04 ? 264  LEU A CB  1 
ATOM   1992 C  CG  . LEU A 1 262 ? 84.500  6.531   -1.436  1.00 13.58 ? 264  LEU A CG  1 
ATOM   1993 C  CD1 . LEU A 1 262 ? 84.853  7.429   -0.260  1.00 13.88 ? 264  LEU A CD1 1 
ATOM   1994 C  CD2 . LEU A 1 262 ? 83.692  7.296   -2.474  1.00 14.41 ? 264  LEU A CD2 1 
ATOM   1995 N  N   . THR A 1 263 ? 87.327  3.370   -3.677  1.00 12.99 ? 265  THR A N   1 
ATOM   1996 C  CA  . THR A 1 263 ? 88.583  2.907   -4.264  1.00 13.44 ? 265  THR A CA  1 
ATOM   1997 C  C   . THR A 1 263 ? 88.517  1.421   -4.625  1.00 12.81 ? 265  THR A C   1 
ATOM   1998 O  O   . THR A 1 263 ? 89.026  0.572   -3.895  1.00 12.26 ? 265  THR A O   1 
ATOM   1999 C  CB  . THR A 1 263 ? 89.792  3.200   -3.347  1.00 13.73 ? 265  THR A CB  1 
ATOM   2000 O  OG1 . THR A 1 263 ? 90.989  2.682   -3.941  1.00 15.09 ? 265  THR A OG1 1 
ATOM   2001 C  CG2 . THR A 1 263 ? 89.601  2.575   -1.968  1.00 12.67 ? 265  THR A CG2 1 
ATOM   2002 N  N   . PRO A 1 264 ? 87.875  1.107   -5.762  1.00 12.89 ? 266  PRO A N   1 
ATOM   2003 C  CA  . PRO A 1 264 ? 87.364  -0.244  -5.997  1.00 12.70 ? 266  PRO A CA  1 
ATOM   2004 C  C   . PRO A 1 264 ? 88.443  -1.269  -6.334  1.00 13.34 ? 266  PRO A C   1 
ATOM   2005 O  O   . PRO A 1 264 ? 88.210  -2.465  -6.186  1.00 12.75 ? 266  PRO A O   1 
ATOM   2006 C  CB  . PRO A 1 264 ? 86.414  -0.063  -7.189  1.00 13.32 ? 266  PRO A CB  1 
ATOM   2007 C  CG  . PRO A 1 264 ? 86.060  1.389   -7.188  1.00 14.27 ? 266  PRO A CG  1 
ATOM   2008 C  CD  . PRO A 1 264 ? 87.288  2.091   -6.688  1.00 13.14 ? 266  PRO A CD  1 
ATOM   2009 N  N   . THR A 1 265 ? 89.603  -0.811  -6.800  1.00 13.95 ? 267  THR A N   1 
ATOM   2010 C  CA  . THR A 1 265 ? 90.597  -1.719  -7.371  1.00 15.17 ? 267  THR A CA  1 
ATOM   2011 C  C   . THR A 1 265 ? 91.849  -1.900  -6.509  1.00 15.97 ? 267  THR A C   1 
ATOM   2012 O  O   . THR A 1 265 ? 92.555  -2.900  -6.636  1.00 16.71 ? 267  THR A O   1 
ATOM   2013 C  CB  . THR A 1 265 ? 90.997  -1.317  -8.807  1.00 16.33 ? 267  THR A CB  1 
ATOM   2014 O  OG1 . THR A 1 265 ? 91.590  -0.012  -8.799  1.00 20.16 ? 267  THR A OG1 1 
ATOM   2015 C  CG2 . THR A 1 265 ? 89.781  -1.308  -9.718  1.00 15.99 ? 267  THR A CG2 1 
ATOM   2016 N  N   . ALA A 1 266 ? 92.107  -0.952  -5.612  1.00 15.73 ? 268  ALA A N   1 
ATOM   2017 C  CA  . ALA A 1 266 ? 93.268  -1.046  -4.728  1.00 16.12 ? 268  ALA A CA  1 
ATOM   2018 C  C   . ALA A 1 266 ? 93.042  -0.325  -3.405  1.00 14.15 ? 268  ALA A C   1 
ATOM   2019 O  O   . ALA A 1 266 ? 92.208  0.578   -3.312  1.00 13.85 ? 268  ALA A O   1 
ATOM   2020 C  CB  . ALA A 1 266 ? 94.514  -0.513  -5.419  1.00 17.56 ? 268  ALA A CB  1 
ATOM   2021 N  N   . ASP A 1 267 ? 93.770  -0.753  -2.377  1.00 13.85 ? 269  ASP A N   1 
ATOM   2022 C  CA  . ASP A 1 267 ? 93.742  -0.077  -1.085  1.00 13.26 ? 269  ASP A CA  1 
ATOM   2023 C  C   . ASP A 1 267 ? 94.292  1.335   -1.240  1.00 14.72 ? 269  ASP A C   1 
ATOM   2024 O  O   . ASP A 1 267 ? 95.066  1.613   -2.157  1.00 14.89 ? 269  ASP A O   1 
ATOM   2025 C  CB  . ASP A 1 267 ? 94.558  -0.858  -0.047  1.00 13.37 ? 269  ASP A CB  1 
ATOM   2026 C  CG  . ASP A 1 267 ? 94.250  -0.437  1.384   1.00 12.79 ? 269  ASP A CG  1 
ATOM   2027 O  OD1 . ASP A 1 267 ? 93.570  0.590   1.580   1.00 13.06 ? 269  ASP A OD1 1 
ATOM   2028 O  OD2 . ASP A 1 267 ? 94.693  -1.135  2.320   1.00 13.80 ? 269  ASP A OD2 1 
ATOM   2029 N  N   . ASP A 1 268 ? 93.854  2.228   -0.361  1.00 15.10 ? 270  ASP A N   1 
ATOM   2030 C  CA  . ASP A 1 268 ? 94.311  3.613   -0.355  1.00 15.19 ? 270  ASP A CA  1 
ATOM   2031 C  C   . ASP A 1 268 ? 94.472  4.036   1.099   1.00 14.81 ? 270  ASP A C   1 
ATOM   2032 O  O   . ASP A 1 268 ? 93.519  4.496   1.719   1.00 13.38 ? 270  ASP A O   1 
ATOM   2033 C  CB  . ASP A 1 268 ? 93.285  4.508   -1.059  1.00 14.53 ? 270  ASP A CB  1 
ATOM   2034 C  CG  . ASP A 1 268 ? 93.673  5.981   -1.046  1.00 16.19 ? 270  ASP A CG  1 
ATOM   2035 O  OD1 . ASP A 1 268 ? 94.553  6.378   -0.254  1.00 16.06 ? 270  ASP A OD1 1 
ATOM   2036 O  OD2 . ASP A 1 268 ? 93.073  6.753   -1.823  1.00 17.17 ? 270  ASP A OD2 1 
ATOM   2037 N  N   . PRO A 1 269 ? 95.664  3.799   1.668   1.00 15.09 ? 271  PRO A N   1 
ATOM   2038 C  CA  . PRO A 1 269 ? 95.878  3.909   3.106   1.00 14.83 ? 271  PRO A CA  1 
ATOM   2039 C  C   . PRO A 1 269 ? 95.646  5.320   3.644   1.00 14.32 ? 271  PRO A C   1 
ATOM   2040 O  O   . PRO A 1 269 ? 95.180  5.478   4.772   1.00 13.70 ? 271  PRO A O   1 
ATOM   2041 C  CB  . PRO A 1 269 ? 97.345  3.507   3.272   1.00 15.81 ? 271  PRO A CB  1 
ATOM   2042 C  CG  . PRO A 1 269 ? 97.610  2.598   2.119   1.00 17.49 ? 271  PRO A CG  1 
ATOM   2043 C  CD  . PRO A 1 269 ? 96.809  3.172   0.985   1.00 15.99 ? 271  PRO A CD  1 
ATOM   2044 N  N   . ALA A 1 270 ? 95.990  6.335   2.858   1.00 13.71 ? 272  ALA A N   1 
ATOM   2045 C  CA  . ALA A 1 270 ? 95.742  7.715   3.269   1.00 14.39 ? 272  ALA A CA  1 
ATOM   2046 C  C   . ALA A 1 270 ? 94.245  7.963   3.435   1.00 13.99 ? 272  ALA A C   1 
ATOM   2047 O  O   . ALA A 1 270 ? 93.814  8.637   4.370   1.00 13.29 ? 272  ALA A O   1 
ATOM   2048 C  CB  . ALA A 1 270 ? 96.343  8.692   2.268   1.00 14.03 ? 272  ALA A CB  1 
ATOM   2049 N  N   . LEU A 1 271 ? 93.454  7.394   2.532   1.00 13.40 ? 273  LEU A N   1 
ATOM   2050 C  CA  . LEU A 1 271 ? 92.004  7.496   2.611   1.00 13.81 ? 273  LEU A CA  1 
ATOM   2051 C  C   . LEU A 1 271 ? 91.461  6.731   3.819   1.00 13.87 ? 273  LEU A C   1 
ATOM   2052 O  O   . LEU A 1 271 ? 90.560  7.204   4.514   1.00 14.27 ? 273  LEU A O   1 
ATOM   2053 C  CB  . LEU A 1 271 ? 91.375  6.965   1.323   1.00 14.19 ? 273  LEU A CB  1 
ATOM   2054 C  CG  . LEU A 1 271 ? 89.879  6.649   1.332   1.00 14.71 ? 273  LEU A CG  1 
ATOM   2055 C  CD1 . LEU A 1 271 ? 89.068  7.881   1.707   1.00 15.35 ? 273  LEU A CD1 1 
ATOM   2056 C  CD2 . LEU A 1 271 ? 89.463  6.124   -0.036  1.00 14.89 ? 273  LEU A CD2 1 
ATOM   2057 N  N   . GLY A 1 272 ? 92.011  5.547   4.065   1.00 13.54 ? 274  GLY A N   1 
ATOM   2058 C  CA  . GLY A 1 272 ? 91.552  4.711   5.168   1.00 12.97 ? 274  GLY A CA  1 
ATOM   2059 C  C   . GLY A 1 272 ? 91.694  5.388   6.518   1.00 14.05 ? 274  GLY A C   1 
ATOM   2060 O  O   . GLY A 1 272 ? 90.884  5.175   7.417   1.00 14.64 ? 274  GLY A O   1 
ATOM   2061 N  N   . ALA A 1 273 ? 92.721  6.218   6.655   1.00 14.81 ? 275  ALA A N   1 
ATOM   2062 C  CA  . ALA A 1 273 ? 93.058  6.816   7.942   1.00 16.73 ? 275  ALA A CA  1 
ATOM   2063 C  C   . ALA A 1 273 ? 92.298  8.116   8.186   1.00 17.80 ? 275  ALA A C   1 
ATOM   2064 O  O   . ALA A 1 273 ? 92.335  8.669   9.285   1.00 19.74 ? 275  ALA A O   1 
ATOM   2065 C  CB  . ALA A 1 273 ? 94.558  7.051   8.037   1.00 15.99 ? 275  ALA A CB  1 
ATOM   2066 N  N   . ASP A 1 274 ? 91.606  8.596   7.158   1.00 16.57 ? 276  ASP A N   1 
ATOM   2067 C  CA  . ASP A 1 274 ? 91.039  9.939   7.180   1.00 17.12 ? 276  ASP A CA  1 
ATOM   2068 C  C   . ASP A 1 274 ? 89.546  9.904   7.500   1.00 15.55 ? 276  ASP A C   1 
ATOM   2069 O  O   . ASP A 1 274 ? 88.724  9.639   6.626   1.00 14.49 ? 276  ASP A O   1 
ATOM   2070 C  CB  . ASP A 1 274 ? 91.274  10.640  5.838   1.00 17.82 ? 276  ASP A CB  1 
ATOM   2071 C  CG  . ASP A 1 274 ? 90.866  12.104  5.863   1.00 19.63 ? 276  ASP A CG  1 
ATOM   2072 O  OD1 . ASP A 1 274 ? 90.210  12.524  6.840   1.00 19.26 ? 276  ASP A OD1 1 
ATOM   2073 O  OD2 . ASP A 1 274 ? 91.210  12.837  4.908   1.00 20.98 ? 276  ASP A OD2 1 
ATOM   2074 N  N   . ALA A 1 275 ? 89.205  10.210  8.749   1.00 14.25 ? 277  ALA A N   1 
ATOM   2075 C  CA  . ALA A 1 275 ? 87.824  10.137  9.214   1.00 14.22 ? 277  ALA A CA  1 
ATOM   2076 C  C   . ALA A 1 275 ? 86.916  11.104  8.464   1.00 14.18 ? 277  ALA A C   1 
ATOM   2077 O  O   . ALA A 1 275 ? 85.700  10.940  8.449   1.00 14.15 ? 277  ALA A O   1 
ATOM   2078 C  CB  . ALA A 1 275 ? 87.753  10.395  10.711  1.00 14.84 ? 277  ALA A CB  1 
ATOM   2079 N  N   . GLN A 1 276 ? 87.513  12.109  7.834   1.00 15.33 ? 278  GLN A N   1 
ATOM   2080 C  CA  . GLN A 1 276 ? 86.749  13.069  7.052   1.00 14.93 ? 278  GLN A CA  1 
ATOM   2081 C  C   . GLN A 1 276 ? 86.407  12.544  5.657   1.00 14.52 ? 278  GLN A C   1 
ATOM   2082 O  O   . GLN A 1 276 ? 85.590  13.136  4.954   1.00 14.54 ? 278  GLN A O   1 
ATOM   2083 C  CB  . GLN A 1 276 ? 87.501  14.399  6.953   1.00 17.92 ? 278  GLN A CB  1 
ATOM   2084 C  CG  . GLN A 1 276 ? 87.620  15.144  8.273   1.00 18.54 ? 278  GLN A CG  1 
ATOM   2085 C  CD  . GLN A 1 276 ? 86.285  15.665  8.768   1.00 19.40 ? 278  GLN A CD  1 
ATOM   2086 O  OE1 . GLN A 1 276 ? 85.484  16.192  7.994   1.00 20.06 ? 278  GLN A OE1 1 
ATOM   2087 N  NE2 . GLN A 1 276 ? 86.042  15.529  10.066  1.00 20.40 ? 278  GLN A NE2 1 
ATOM   2088 N  N   . ARG A 1 277 ? 87.005  11.419  5.267   1.00 13.55 ? 279  ARG A N   1 
ATOM   2089 C  CA  . ARG A 1 277 ? 86.789  10.877  3.924   1.00 13.32 ? 279  ARG A CA  1 
ATOM   2090 C  C   . ARG A 1 277 ? 86.306  9.426   3.897   1.00 12.85 ? 279  ARG A C   1 
ATOM   2091 O  O   . ARG A 1 277 ? 85.613  9.016   2.962   1.00 11.86 ? 279  ARG A O   1 
ATOM   2092 C  CB  . ARG A 1 277 ? 88.056  11.012  3.080   1.00 15.60 ? 279  ARG A CB  1 
ATOM   2093 C  CG  . ARG A 1 277 ? 88.451  12.446  2.770   1.00 16.64 ? 279  ARG A CG  1 
ATOM   2094 C  CD  . ARG A 1 277 ? 89.386  12.493  1.573   1.00 20.50 ? 279  ARG A CD  1 
ATOM   2095 N  NE  . ARG A 1 277 ? 90.698  11.936  1.891   1.00 22.55 ? 279  ARG A NE  1 
ATOM   2096 C  CZ  . ARG A 1 277 ? 91.410  11.178  1.063   1.00 23.35 ? 279  ARG A CZ  1 
ATOM   2097 N  NH1 . ARG A 1 277 ? 90.934  10.872  -0.138  1.00 22.95 ? 279  ARG A NH1 1 
ATOM   2098 N  NH2 . ARG A 1 277 ? 92.600  10.728  1.435   1.00 23.68 ? 279  ARG A NH2 1 
ATOM   2099 N  N   . ASN A 1 278 ? 86.704  8.639   4.894   1.00 11.23 ? 280  ASN A N   1 
ATOM   2100 C  CA  . ASN A 1 278 ? 86.590  7.188   4.792   1.00 11.21 ? 280  ASN A CA  1 
ATOM   2101 C  C   . ASN A 1 278 ? 85.159  6.666   4.966   1.00 11.27 ? 280  ASN A C   1 
ATOM   2102 O  O   . ASN A 1 278 ? 84.903  5.475   4.796   1.00 11.27 ? 280  ASN A O   1 
ATOM   2103 C  CB  . ASN A 1 278 ? 87.554  6.489   5.756   1.00 10.91 ? 280  ASN A CB  1 
ATOM   2104 C  CG  . ASN A 1 278 ? 87.235  6.771   7.210   1.00 11.31 ? 280  ASN A CG  1 
ATOM   2105 O  OD1 . ASN A 1 278 ? 86.192  7.338   7.526   1.00 11.94 ? 280  ASN A OD1 1 
ATOM   2106 N  ND2 . ASN A 1 278 ? 88.115  6.338   8.106   1.00 10.78 ? 280  ASN A ND2 1 
ATOM   2107 N  N   . ASN A 1 279 ? 84.227  7.564   5.273   1.00 10.37 ? 281  ASN A N   1 
ATOM   2108 C  CA  . ASN A 1 279 ? 82.812  7.196   5.345   1.00 10.34 ? 281  ASN A CA  1 
ATOM   2109 C  C   . ASN A 1 279 ? 81.930  8.043   4.429   1.00 10.49 ? 281  ASN A C   1 
ATOM   2110 O  O   . ASN A 1 279 ? 80.701  7.961   4.470   1.00 9.97  ? 281  ASN A O   1 
ATOM   2111 C  CB  . ASN A 1 279 ? 82.307  7.265   6.785   1.00 10.37 ? 281  ASN A CB  1 
ATOM   2112 C  CG  . ASN A 1 279 ? 81.268  6.202   7.085   1.00 10.38 ? 281  ASN A CG  1 
ATOM   2113 O  OD1 . ASN A 1 279 ? 81.208  5.170   6.414   1.00 9.76  ? 281  ASN A OD1 1 
ATOM   2114 N  ND2 . ASN A 1 279 ? 80.441  6.452   8.090   1.00 10.11 ? 281  ASN A ND2 1 
ATOM   2115 N  N   . ASN A 1 280 ? 82.576  8.819   3.568   1.00 10.71 ? 282  ASN A N   1 
ATOM   2116 C  CA  . ASN A 1 280 ? 81.893  9.810   2.752   1.00 11.47 ? 282  ASN A CA  1 
ATOM   2117 C  C   . ASN A 1 280 ? 81.395  9.224   1.426   1.00 11.51 ? 282  ASN A C   1 
ATOM   2118 O  O   . ASN A 1 280 ? 81.877  9.590   0.351   1.00 11.72 ? 282  ASN A O   1 
ATOM   2119 C  CB  . ASN A 1 280 ? 82.831  10.996  2.507   1.00 12.98 ? 282  ASN A CB  1 
ATOM   2120 C  CG  . ASN A 1 280 ? 82.132  12.172  1.860   1.00 14.96 ? 282  ASN A CG  1 
ATOM   2121 O  OD1 . ASN A 1 280 ? 80.948  12.418  2.094   1.00 14.56 ? 282  ASN A OD1 1 
ATOM   2122 N  ND2 . ASN A 1 280 ? 82.876  12.923  1.061   1.00 16.95 ? 282  ASN A ND2 1 
ATOM   2123 N  N   . PHE A 1 281 ? 80.424  8.316   1.510   1.00 10.67 ? 283  PHE A N   1 
ATOM   2124 C  CA  . PHE A 1 281 ? 79.886  7.643   0.327   1.00 10.72 ? 283  PHE A CA  1 
ATOM   2125 C  C   . PHE A 1 281 ? 78.480  7.095   0.580   1.00 10.50 ? 283  PHE A C   1 
ATOM   2126 O  O   . PHE A 1 281 ? 78.074  6.914   1.728   1.00 10.31 ? 283  PHE A O   1 
ATOM   2127 C  CB  . PHE A 1 281 ? 80.817  6.508   -0.120  1.00 10.56 ? 283  PHE A CB  1 
ATOM   2128 C  CG  . PHE A 1 281 ? 80.942  5.392   0.884   1.00 10.36 ? 283  PHE A CG  1 
ATOM   2129 C  CD1 . PHE A 1 281 ? 81.881  5.458   1.898   1.00 10.27 ? 283  PHE A CD1 1 
ATOM   2130 C  CD2 . PHE A 1 281 ? 80.123  4.274   0.808   1.00 10.43 ? 283  PHE A CD2 1 
ATOM   2131 C  CE1 . PHE A 1 281 ? 81.992  4.441   2.830   1.00 10.24 ? 283  PHE A CE1 1 
ATOM   2132 C  CE2 . PHE A 1 281 ? 80.232  3.251   1.734   1.00 9.77  ? 283  PHE A CE2 1 
ATOM   2133 C  CZ  . PHE A 1 281 ? 81.173  3.332   2.741   1.00 9.80  ? 283  PHE A CZ  1 
ATOM   2134 N  N   . THR A 1 282 ? 77.759  6.802   -0.501  1.00 11.09 ? 284  THR A N   1 
ATOM   2135 C  CA  . THR A 1 282 ? 76.366  6.358   -0.411  1.00 11.45 ? 284  THR A CA  1 
ATOM   2136 C  C   . THR A 1 282 ? 76.128  5.073   -1.201  1.00 11.59 ? 284  THR A C   1 
ATOM   2137 O  O   . THR A 1 282 ? 75.062  4.462   -1.094  1.00 10.87 ? 284  THR A O   1 
ATOM   2138 C  CB  . THR A 1 282 ? 75.396  7.427   -0.949  1.00 11.95 ? 284  THR A CB  1 
ATOM   2139 O  OG1 . THR A 1 282 ? 75.564  7.550   -2.367  1.00 13.55 ? 284  THR A OG1 1 
ATOM   2140 C  CG2 . THR A 1 282 ? 75.653  8.775   -0.293  1.00 11.29 ? 284  THR A CG2 1 
ATOM   2141 N  N   . TYR A 1 283 ? 77.132  4.677   -1.984  1.00 11.36 ? 285  TYR A N   1 
ATOM   2142 C  CA  . TYR A 1 283 ? 77.026  3.588   -2.959  1.00 11.02 ? 285  TYR A CA  1 
ATOM   2143 C  C   . TYR A 1 283 ? 76.556  4.042   -4.342  1.00 12.08 ? 285  TYR A C   1 
ATOM   2144 O  O   . TYR A 1 283 ? 76.595  3.272   -5.301  1.00 12.03 ? 285  TYR A O   1 
ATOM   2145 C  CB  . TYR A 1 283 ? 76.171  2.429   -2.434  1.00 11.12 ? 285  TYR A CB  1 
ATOM   2146 C  CG  . TYR A 1 283 ? 76.781  1.743   -1.226  1.00 10.74 ? 285  TYR A CG  1 
ATOM   2147 C  CD1 . TYR A 1 283 ? 78.092  1.283   -1.257  1.00 10.50 ? 285  TYR A CD1 1 
ATOM   2148 C  CD2 . TYR A 1 283 ? 76.063  1.597   -0.049  1.00 10.30 ? 285  TYR A CD2 1 
ATOM   2149 C  CE1 . TYR A 1 283 ? 78.666  0.687   -0.149  1.00 10.49 ? 285  TYR A CE1 1 
ATOM   2150 C  CE2 . TYR A 1 283 ? 76.628  0.997   1.065   1.00 9.75  ? 285  TYR A CE2 1 
ATOM   2151 C  CZ  . TYR A 1 283 ? 77.928  0.546   1.008   1.00 10.12 ? 285  TYR A CZ  1 
ATOM   2152 O  OH  . TYR A 1 283 ? 78.505  -0.039  2.112   1.00 10.00 ? 285  TYR A OH  1 
ATOM   2153 N  N   . SER A 1 284 ? 76.121  5.295   -4.441  1.00 12.81 ? 286  SER A N   1 
ATOM   2154 C  CA  . SER A 1 284 ? 75.752  5.875   -5.726  1.00 12.87 ? 286  SER A CA  1 
ATOM   2155 C  C   . SER A 1 284 ? 76.973  6.390   -6.486  1.00 13.68 ? 286  SER A C   1 
ATOM   2156 O  O   . SER A 1 284 ? 77.946  6.850   -5.883  1.00 12.14 ? 286  SER A O   1 
ATOM   2157 C  CB  . SER A 1 284 ? 74.741  7.005   -5.531  1.00 14.78 ? 286  SER A CB  1 
ATOM   2158 O  OG  . SER A 1 284 ? 74.426  7.622   -6.765  1.00 16.68 ? 286  SER A OG  1 
ATOM   2159 N  N   . HIS A 1 285 ? 76.922  6.291   -7.811  1.00 13.78 ? 287  HIS A N   1 
ATOM   2160 C  CA  . HIS A 1 285 ? 78.013  6.749   -8.662  1.00 13.84 ? 287  HIS A CA  1 
ATOM   2161 C  C   . HIS A 1 285 ? 77.447  7.294   -9.964  1.00 14.76 ? 287  HIS A C   1 
ATOM   2162 O  O   . HIS A 1 285 ? 76.642  6.633   -10.620 1.00 14.44 ? 287  HIS A O   1 
ATOM   2163 C  CB  . HIS A 1 285 ? 78.986  5.600   -8.961  1.00 13.64 ? 287  HIS A CB  1 
ATOM   2164 C  CG  . HIS A 1 285 ? 79.644  5.040   -7.739  1.00 13.70 ? 287  HIS A CG  1 
ATOM   2165 N  ND1 . HIS A 1 285 ? 80.731  5.640   -7.141  1.00 13.73 ? 287  HIS A ND1 1 
ATOM   2166 C  CD2 . HIS A 1 285 ? 79.331  3.973   -6.967  1.00 13.52 ? 287  HIS A CD2 1 
ATOM   2167 C  CE1 . HIS A 1 285 ? 81.069  4.958   -6.062  1.00 13.79 ? 287  HIS A CE1 1 
ATOM   2168 N  NE2 . HIS A 1 285 ? 80.226  3.950   -5.926  1.00 13.09 ? 287  HIS A NE2 1 
ATOM   2169 N  N   . ALA A 1 286 ? 77.853  8.506   -10.327 1.00 15.90 ? 288  ALA A N   1 
ATOM   2170 C  CA  . ALA A 1 286 ? 77.406  9.106   -11.580 1.00 15.87 ? 288  ALA A CA  1 
ATOM   2171 C  C   . ALA A 1 286 ? 77.769  8.212   -12.759 1.00 16.43 ? 288  ALA A C   1 
ATOM   2172 O  O   . ALA A 1 286 ? 78.887  7.706   -12.846 1.00 16.69 ? 288  ALA A O   1 
ATOM   2173 C  CB  . ALA A 1 286 ? 78.006  10.495  -11.754 1.00 18.17 ? 288  ALA A CB  1 
ATOM   2174 N  N   . GLY A 1 287 ? 76.801  7.981   -13.638 1.00 17.41 ? 289  GLY A N   1 
ATOM   2175 C  CA  . GLY A 1 287 ? 77.028  7.179   -14.834 1.00 19.19 ? 289  GLY A CA  1 
ATOM   2176 C  C   . GLY A 1 287 ? 76.753  5.700   -14.628 1.00 19.61 ? 289  GLY A C   1 
ATOM   2177 O  O   . GLY A 1 287 ? 76.814  4.914   -15.574 1.00 20.09 ? 289  GLY A O   1 
ATOM   2178 N  N   . PHE A 1 288 ? 76.456  5.315   -13.390 1.00 17.92 ? 290  PHE A N   1 
ATOM   2179 C  CA  . PHE A 1 288 ? 76.228  3.907   -13.064 1.00 17.40 ? 290  PHE A CA  1 
ATOM   2180 C  C   . PHE A 1 288 ? 74.831  3.671   -12.499 1.00 16.89 ? 290  PHE A C   1 
ATOM   2181 O  O   . PHE A 1 288 ? 74.311  4.483   -11.734 1.00 16.39 ? 290  PHE A O   1 
ATOM   2182 C  CB  . PHE A 1 288 ? 77.279  3.401   -12.073 1.00 17.04 ? 290  PHE A CB  1 
ATOM   2183 C  CG  . PHE A 1 288 ? 78.677  3.397   -12.620 1.00 16.60 ? 290  PHE A CG  1 
ATOM   2184 C  CD1 . PHE A 1 288 ? 79.460  4.540   -12.565 1.00 16.91 ? 290  PHE A CD1 1 
ATOM   2185 C  CD2 . PHE A 1 288 ? 79.218  2.245   -13.167 1.00 16.52 ? 290  PHE A CD2 1 
ATOM   2186 C  CE1 . PHE A 1 288 ? 80.750  4.538   -13.064 1.00 17.76 ? 290  PHE A CE1 1 
ATOM   2187 C  CE2 . PHE A 1 288 ? 80.510  2.234   -13.660 1.00 16.87 ? 290  PHE A CE2 1 
ATOM   2188 C  CZ  . PHE A 1 288 ? 81.278  3.381   -13.604 1.00 17.20 ? 290  PHE A CZ  1 
ATOM   2189 N  N   . ASP A 1 289 ? 74.243  2.536   -12.860 1.00 17.66 ? 291  ASP A N   1 
ATOM   2190 C  CA  . ASP A 1 289 ? 72.915  2.166   -12.388 1.00 18.83 ? 291  ASP A CA  1 
ATOM   2191 C  C   . ASP A 1 289 ? 72.994  1.510   -11.010 1.00 17.14 ? 291  ASP A C   1 
ATOM   2192 O  O   . ASP A 1 289 ? 73.537  0.417   -10.865 1.00 15.46 ? 291  ASP A O   1 
ATOM   2193 C  CB  . ASP A 1 289 ? 72.254  1.219   -13.391 1.00 20.65 ? 291  ASP A CB  1 
ATOM   2194 C  CG  . ASP A 1 289 ? 70.973  0.612   -12.865 1.00 24.54 ? 291  ASP A CG  1 
ATOM   2195 O  OD1 . ASP A 1 289 ? 70.186  1.335   -12.216 1.00 28.51 ? 291  ASP A OD1 1 
ATOM   2196 O  OD2 . ASP A 1 289 ? 70.746  -0.591  -13.111 1.00 26.37 ? 291  ASP A OD2 1 
ATOM   2197 N  N   . LEU A 1 290 ? 72.458  2.188   -10.002 1.00 15.68 ? 292  LEU A N   1 
ATOM   2198 C  CA  . LEU A 1 290 ? 72.571  1.723   -8.620  1.00 15.27 ? 292  LEU A CA  1 
ATOM   2199 C  C   . LEU A 1 290 ? 72.085  0.285   -8.481  1.00 15.08 ? 292  LEU A C   1 
ATOM   2200 O  O   . LEU A 1 290 ? 72.630  -0.492  -7.696  1.00 15.39 ? 292  LEU A O   1 
ATOM   2201 C  CB  . LEU A 1 290 ? 71.790  2.641   -7.678  1.00 14.98 ? 292  LEU A CB  1 
ATOM   2202 C  CG  . LEU A 1 290 ? 71.907  2.369   -6.175  1.00 15.18 ? 292  LEU A CG  1 
ATOM   2203 C  CD1 . LEU A 1 290 ? 73.309  2.686   -5.680  1.00 15.33 ? 292  LEU A CD1 1 
ATOM   2204 C  CD2 . LEU A 1 290 ? 70.874  3.176   -5.402  1.00 14.96 ? 292  LEU A CD2 1 
ATOM   2205 N  N   . GLY A 1 291 ? 71.080  -0.073  -9.273  1.00 14.73 ? 293  GLY A N   1 
ATOM   2206 C  CA  . GLY A 1 291 ? 70.416  -1.366  -9.149  1.00 13.29 ? 293  GLY A CA  1 
ATOM   2207 C  C   . GLY A 1 291 ? 71.207  -2.550  -9.678  1.00 13.68 ? 293  GLY A C   1 
ATOM   2208 O  O   . GLY A 1 291 ? 70.926  -3.696  -9.323  1.00 12.67 ? 293  GLY A O   1 
ATOM   2209 N  N   . SER A 1 292 ? 72.196  -2.285  -10.529 1.00 14.07 ? 294  SER A N   1 
ATOM   2210 C  CA  . SER A 1 292 ? 72.928  -3.364  -11.192 1.00 14.00 ? 294  SER A CA  1 
ATOM   2211 C  C   . SER A 1 292 ? 74.446  -3.267  -11.044 1.00 13.35 ? 294  SER A C   1 
ATOM   2212 O  O   . SER A 1 292 ? 75.161  -4.238  -11.286 1.00 13.68 ? 294  SER A O   1 
ATOM   2213 C  CB  . SER A 1 292 ? 72.545  -3.449  -12.673 1.00 14.88 ? 294  SER A CB  1 
ATOM   2214 O  OG  . SER A 1 292 ? 72.963  -2.292  -13.370 1.00 14.97 ? 294  SER A OG  1 
ATOM   2215 N  N   . ASP A 1 293 ? 74.941  -2.092  -10.672 1.00 12.97 ? 295  ASP A N   1 
ATOM   2216 C  CA  . ASP A 1 293 ? 76.379  -1.855  -10.660 1.00 12.49 ? 295  ASP A CA  1 
ATOM   2217 C  C   . ASP A 1 293 ? 77.020  -2.405  -9.389  1.00 12.21 ? 295  ASP A C   1 
ATOM   2218 O  O   . ASP A 1 293 ? 76.790  -1.892  -8.298  1.00 11.30 ? 295  ASP A O   1 
ATOM   2219 C  CB  . ASP A 1 293 ? 76.683  -0.360  -10.794 1.00 13.01 ? 295  ASP A CB  1 
ATOM   2220 C  CG  . ASP A 1 293 ? 78.160  -0.049  -10.625 1.00 13.57 ? 295  ASP A CG  1 
ATOM   2221 O  OD1 . ASP A 1 293 ? 78.993  -0.815  -11.153 1.00 14.19 ? 295  ASP A OD1 1 
ATOM   2222 O  OD2 . ASP A 1 293 ? 78.490  0.950   -9.948  1.00 14.37 ? 295  ASP A OD2 1 
ATOM   2223 N  N   . GLN A 1 294 ? 77.824  -3.452  -9.537  1.00 11.27 ? 296  GLN A N   1 
ATOM   2224 C  CA  . GLN A 1 294 ? 78.573  -3.996  -8.412  1.00 11.56 ? 296  GLN A CA  1 
ATOM   2225 C  C   . GLN A 1 294 ? 80.071  -3.831  -8.609  1.00 11.70 ? 296  GLN A C   1 
ATOM   2226 O  O   . GLN A 1 294 ? 80.868  -4.477  -7.926  1.00 11.32 ? 296  GLN A O   1 
ATOM   2227 C  CB  . GLN A 1 294 ? 78.225  -5.469  -8.195  1.00 10.92 ? 296  GLN A CB  1 
ATOM   2228 C  CG  . GLN A 1 294 ? 76.779  -5.677  -7.773  1.00 10.71 ? 296  GLN A CG  1 
ATOM   2229 C  CD  . GLN A 1 294 ? 76.490  -7.095  -7.337  1.00 10.93 ? 296  GLN A CD  1 
ATOM   2230 O  OE1 . GLN A 1 294 ? 76.803  -7.486  -6.209  1.00 10.96 ? 296  GLN A OE1 1 
ATOM   2231 N  NE2 . GLN A 1 294 ? 75.808  -7.847  -8.194  1.00 11.62 ? 296  GLN A NE2 1 
ATOM   2232 N  N   . SER A 1 295 ? 80.451  -2.967  -9.547  1.00 11.67 ? 297  SER A N   1 
ATOM   2233 C  CA  . SER A 1 295 ? 81.861  -2.785  -9.885  1.00 12.37 ? 297  SER A CA  1 
ATOM   2234 C  C   . SER A 1 295 ? 82.611  -1.992  -8.817  1.00 12.81 ? 297  SER A C   1 
ATOM   2235 O  O   . SER A 1 295 ? 83.830  -2.106  -8.687  1.00 12.97 ? 297  SER A O   1 
ATOM   2236 C  CB  . SER A 1 295 ? 82.010  -2.109  -11.249 1.00 12.89 ? 297  SER A CB  1 
ATOM   2237 O  OG  . SER A 1 295 ? 81.659  -0.739  -11.179 1.00 13.05 ? 297  SER A OG  1 
ATOM   2238 N  N   . HIS A 1 296 ? 81.884  -1.189  -8.048  1.00 12.57 ? 298  HIS A N   1 
ATOM   2239 C  CA  . HIS A 1 296 ? 82.503  -0.430  -6.966  1.00 12.66 ? 298  HIS A CA  1 
ATOM   2240 C  C   . HIS A 1 296 ? 82.468  -1.218  -5.657  1.00 12.11 ? 298  HIS A C   1 
ATOM   2241 O  O   . HIS A 1 296 ? 83.466  -1.297  -4.940  1.00 11.95 ? 298  HIS A O   1 
ATOM   2242 C  CB  . HIS A 1 296 ? 81.816  0.928   -6.800  1.00 12.55 ? 298  HIS A CB  1 
ATOM   2243 C  CG  . HIS A 1 296 ? 81.949  1.820   -7.997  1.00 13.26 ? 298  HIS A CG  1 
ATOM   2244 N  ND1 . HIS A 1 296 ? 81.099  1.746   -9.079  1.00 13.79 ? 298  HIS A ND1 1 
ATOM   2245 C  CD2 . HIS A 1 296 ? 82.827  2.814   -8.276  1.00 13.95 ? 298  HIS A CD2 1 
ATOM   2246 C  CE1 . HIS A 1 296 ? 81.453  2.647   -9.979  1.00 14.19 ? 298  HIS A CE1 1 
ATOM   2247 N  NE2 . HIS A 1 296 ? 82.497  3.311   -9.515  1.00 14.44 ? 298  HIS A NE2 1 
ATOM   2248 N  N   . CYS A 1 297 ? 81.321  -1.823  -5.370  1.00 11.68 ? 299  CYS A N   1 
ATOM   2249 C  CA  . CYS A 1 297 ? 81.141  -2.614  -4.156  1.00 11.45 ? 299  CYS A CA  1 
ATOM   2250 C  C   . CYS A 1 297 ? 80.007  -3.614  -4.372  1.00 11.42 ? 299  CYS A C   1 
ATOM   2251 O  O   . CYS A 1 297 ? 78.929  -3.239  -4.833  1.00 11.57 ? 299  CYS A O   1 
ATOM   2252 C  CB  . CYS A 1 297 ? 80.828  -1.700  -2.965  1.00 11.07 ? 299  CYS A CB  1 
ATOM   2253 S  SG  . CYS A 1 297 ? 80.608  -2.543  -1.374  1.00 11.31 ? 299  CYS A SG  1 
ATOM   2254 N  N   . PRO A 1 298 ? 80.262  -4.900  -4.083  1.00 11.44 ? 300  PRO A N   1 
ATOM   2255 C  CA  . PRO A 1 298 ? 79.218  -5.917  -4.203  1.00 10.95 ? 300  PRO A CA  1 
ATOM   2256 C  C   . PRO A 1 298 ? 78.003  -5.548  -3.362  1.00 10.73 ? 300  PRO A C   1 
ATOM   2257 O  O   . PRO A 1 298 ? 78.154  -4.999  -2.269  1.00 10.50 ? 300  PRO A O   1 
ATOM   2258 C  CB  . PRO A 1 298 ? 79.880  -7.172  -3.625  1.00 11.54 ? 300  PRO A CB  1 
ATOM   2259 C  CG  . PRO A 1 298 ? 81.348  -6.933  -3.766  1.00 11.84 ? 300  PRO A CG  1 
ATOM   2260 C  CD  . PRO A 1 298 ? 81.532  -5.457  -3.587  1.00 11.10 ? 300  PRO A CD  1 
ATOM   2261 N  N   . PHE A 1 299 ? 76.810  -5.887  -3.842  1.00 10.49 ? 301  PHE A N   1 
ATOM   2262 C  CA  . PHE A 1 299 ? 75.605  -5.728  -3.033  1.00 10.23 ? 301  PHE A CA  1 
ATOM   2263 C  C   . PHE A 1 299 ? 75.706  -6.561  -1.754  1.00 10.09 ? 301  PHE A C   1 
ATOM   2264 O  O   . PHE A 1 299 ? 75.039  -6.277  -0.760  1.00 9.90  ? 301  PHE A O   1 
ATOM   2265 C  CB  . PHE A 1 299 ? 74.358  -6.126  -3.831  1.00 10.02 ? 301  PHE A CB  1 
ATOM   2266 C  CG  . PHE A 1 299 ? 74.175  -5.347  -5.108  1.00 10.07 ? 301  PHE A CG  1 
ATOM   2267 C  CD1 . PHE A 1 299 ? 74.504  -4.002  -5.171  1.00 9.99  ? 301  PHE A CD1 1 
ATOM   2268 C  CD2 . PHE A 1 299 ? 73.633  -5.951  -6.230  1.00 10.14 ? 301  PHE A CD2 1 
ATOM   2269 C  CE1 . PHE A 1 299 ? 74.336  -3.286  -6.345  1.00 10.44 ? 301  PHE A CE1 1 
ATOM   2270 C  CE2 . PHE A 1 299 ? 73.455  -5.240  -7.405  1.00 10.13 ? 301  PHE A CE2 1 
ATOM   2271 C  CZ  . PHE A 1 299 ? 73.801  -3.904  -7.461  1.00 10.02 ? 301  PHE A CZ  1 
ATOM   2272 N  N   . SER A 1 300 ? 76.590  -7.553  -1.768  1.00 9.81  ? 302  SER A N   1 
ATOM   2273 C  CA  . SER A 1 300 ? 76.662  -8.536  -0.693  1.00 9.61  ? 302  SER A CA  1 
ATOM   2274 C  C   . SER A 1 300 ? 77.730  -8.231  0.360   1.00 8.92  ? 302  SER A C   1 
ATOM   2275 O  O   . SER A 1 300 ? 77.851  -8.948  1.351   1.00 8.76  ? 302  SER A O   1 
ATOM   2276 C  CB  . SER A 1 300 ? 76.892  -9.932  -1.272  1.00 9.61  ? 302  SER A CB  1 
ATOM   2277 O  OG  . SER A 1 300 ? 77.936  -9.913  -2.227  1.00 10.17 ? 302  SER A OG  1 
ATOM   2278 N  N   . ALA A 1 301 ? 78.530  -7.195  0.129   1.00 9.22  ? 303  ALA A N   1 
ATOM   2279 C  CA  . ALA A 1 301 ? 79.596  -6.836  1.064   1.00 8.69  ? 303  ALA A CA  1 
ATOM   2280 C  C   . ALA A 1 301 ? 79.058  -6.588  2.478   1.00 8.65  ? 303  ALA A C   1 
ATOM   2281 O  O   . ALA A 1 301 ? 77.969  -6.028  2.639   1.00 8.67  ? 303  ALA A O   1 
ATOM   2282 C  CB  . ALA A 1 301 ? 80.349  -5.614  0.554   1.00 8.81  ? 303  ALA A CB  1 
ATOM   2283 N  N   . HIS A 1 302 ? 79.824  -6.998  3.493   1.00 8.42  ? 304  HIS A N   1 
ATOM   2284 C  CA  . HIS A 1 302 ? 79.410  -6.876  4.911   1.00 8.21  ? 304  HIS A CA  1 
ATOM   2285 C  C   . HIS A 1 302 ? 78.804  -5.511  5.229   1.00 7.80  ? 304  HIS A C   1 
ATOM   2286 O  O   . HIS A 1 302 ? 77.681  -5.428  5.714   1.00 7.55  ? 304  HIS A O   1 
ATOM   2287 C  CB  . HIS A 1 302 ? 80.585  -7.178  5.862   1.00 8.37  ? 304  HIS A CB  1 
ATOM   2288 C  CG  . HIS A 1 302 ? 80.285  -6.965  7.326   1.00 8.60  ? 304  HIS A CG  1 
ATOM   2289 N  ND1 . HIS A 1 302 ? 79.254  -7.605  7.979   1.00 8.80  ? 304  HIS A ND1 1 
ATOM   2290 C  CD2 . HIS A 1 302 ? 80.966  -6.287  8.285   1.00 8.89  ? 304  HIS A CD2 1 
ATOM   2291 C  CE1 . HIS A 1 302 ? 79.275  -7.281  9.264   1.00 8.88  ? 304  HIS A CE1 1 
ATOM   2292 N  NE2 . HIS A 1 302 ? 80.312  -6.490  9.480   1.00 8.95  ? 304  HIS A NE2 1 
ATOM   2293 N  N   . ILE A 1 303 ? 79.555  -4.440  4.996   1.00 7.58  ? 305  ILE A N   1 
ATOM   2294 C  CA  . ILE A 1 303 ? 79.090  -3.122  5.419   1.00 7.57  ? 305  ILE A CA  1 
ATOM   2295 C  C   . ILE A 1 303 ? 77.879  -2.631  4.627   1.00 8.12  ? 305  ILE A C   1 
ATOM   2296 O  O   . ILE A 1 303 ? 77.066  -1.859  5.142   1.00 8.19  ? 305  ILE A O   1 
ATOM   2297 C  CB  . ILE A 1 303 ? 80.211  -2.059  5.428   1.00 7.57  ? 305  ILE A CB  1 
ATOM   2298 C  CG1 . ILE A 1 303 ? 80.733  -1.784  4.015   1.00 7.78  ? 305  ILE A CG1 1 
ATOM   2299 C  CG2 . ILE A 1 303 ? 81.336  -2.467  6.367   1.00 7.16  ? 305  ILE A CG2 1 
ATOM   2300 C  CD1 . ILE A 1 303 ? 81.457  -0.458  3.902   1.00 7.54  ? 305  ILE A CD1 1 
ATOM   2301 N  N   . ARG A 1 304 ? 77.738  -3.113  3.395   1.00 8.30  ? 306  ARG A N   1 
ATOM   2302 C  CA  . ARG A 1 304 ? 76.588  -2.762  2.564   1.00 8.67  ? 306  ARG A CA  1 
ATOM   2303 C  C   . ARG A 1 304 ? 75.343  -3.519  3.021   1.00 8.98  ? 306  ARG A C   1 
ATOM   2304 O  O   . ARG A 1 304 ? 74.230  -2.995  2.975   1.00 9.02  ? 306  ARG A O   1 
ATOM   2305 C  CB  . ARG A 1 304 ? 76.883  -3.057  1.087   1.00 9.07  ? 306  ARG A CB  1 
ATOM   2306 C  CG  . ARG A 1 304 ? 75.844  -2.507  0.120   1.00 9.40  ? 306  ARG A CG  1 
ATOM   2307 C  CD  . ARG A 1 304 ? 76.416  -2.354  -1.285  1.00 10.20 ? 306  ARG A CD  1 
ATOM   2308 N  NE  . ARG A 1 304 ? 75.490  -1.660  -2.174  1.00 10.21 ? 306  ARG A NE  1 
ATOM   2309 C  CZ  . ARG A 1 304 ? 75.804  -1.205  -3.383  1.00 10.39 ? 306  ARG A CZ  1 
ATOM   2310 N  NH1 . ARG A 1 304 ? 77.024  -1.384  -3.871  1.00 10.85 ? 306  ARG A NH1 1 
ATOM   2311 N  NH2 . ARG A 1 304 ? 74.897  -0.561  -4.104  1.00 10.39 ? 306  ARG A NH2 1 
ATOM   2312 N  N   . LYS A 1 305 ? 75.548  -4.738  3.510   1.00 8.87  ? 307  LYS A N   1 
ATOM   2313 C  CA  . LYS A 1 305 ? 74.457  -5.536  4.063   1.00 9.28  ? 307  LYS A CA  1 
ATOM   2314 C  C   . LYS A 1 305 ? 73.946  -4.956  5.379   1.00 9.71  ? 307  LYS A C   1 
ATOM   2315 O  O   . LYS A 1 305 ? 72.754  -5.047  5.678   1.00 10.92 ? 307  LYS A O   1 
ATOM   2316 C  CB  . LYS A 1 305 ? 74.907  -6.984  4.274   1.00 8.88  ? 307  LYS A CB  1 
ATOM   2317 C  CG  . LYS A 1 305 ? 74.900  -7.822  3.006   1.00 8.95  ? 307  LYS A CG  1 
ATOM   2318 C  CD  . LYS A 1 305 ? 73.508  -8.363  2.714   1.00 8.91  ? 307  LYS A CD  1 
ATOM   2319 C  CE  . LYS A 1 305 ? 73.574  -9.677  1.951   1.00 9.18  ? 307  LYS A CE  1 
ATOM   2320 N  NZ  . LYS A 1 305 ? 72.243  -10.340 1.881   1.00 9.61  ? 307  LYS A NZ  1 
ATOM   2321 N  N   . THR A 1 306 ? 74.847  -4.380  6.171   1.00 8.61  ? 308  THR A N   1 
ATOM   2322 C  CA  . THR A 1 306 ? 74.496  -3.943  7.519   1.00 8.45  ? 308  THR A CA  1 
ATOM   2323 C  C   . THR A 1 306 ? 74.158  -2.455  7.620   1.00 8.54  ? 308  THR A C   1 
ATOM   2324 O  O   . THR A 1 306 ? 73.479  -2.039  8.559   1.00 8.53  ? 308  THR A O   1 
ATOM   2325 C  CB  . THR A 1 306 ? 75.580  -4.303  8.547   1.00 8.12  ? 308  THR A CB  1 
ATOM   2326 O  OG1 . THR A 1 306 ? 76.836  -3.756  8.131   1.00 8.51  ? 308  THR A OG1 1 
ATOM   2327 C  CG2 . THR A 1 306 ? 75.705  -5.820  8.675   1.00 8.12  ? 308  THR A CG2 1 
ATOM   2328 N  N   . ARG A 1 307 ? 74.663  -1.659  6.681   1.00 8.44  ? 309  ARG A N   1 
ATOM   2329 C  CA  . ARG A 1 307 ? 74.128  -0.312  6.439   1.00 8.74  ? 309  ARG A CA  1 
ATOM   2330 C  C   . ARG A 1 307 ? 73.977  -0.046  4.941   1.00 8.97  ? 309  ARG A C   1 
ATOM   2331 O  O   . ARG A 1 307 ? 74.950  0.278   4.261   1.00 9.91  ? 309  ARG A O   1 
ATOM   2332 C  CB  . ARG A 1 307 ? 74.994  0.773   7.094   1.00 8.90  ? 309  ARG A CB  1 
ATOM   2333 C  CG  . ARG A 1 307 ? 74.358  2.163   7.040   1.00 8.78  ? 309  ARG A CG  1 
ATOM   2334 C  CD  . ARG A 1 307 ? 75.361  3.305   7.170   1.00 8.80  ? 309  ARG A CD  1 
ATOM   2335 N  NE  . ARG A 1 307 ? 74.742  4.579   6.797   1.00 9.06  ? 309  ARG A NE  1 
ATOM   2336 C  CZ  . ARG A 1 307 ? 75.399  5.719   6.594   1.00 9.12  ? 309  ARG A CZ  1 
ATOM   2337 N  NH1 . ARG A 1 307 ? 76.701  5.796   6.824   1.00 8.91  ? 309  ARG A NH1 1 
ATOM   2338 N  NH2 . ARG A 1 307 ? 74.738  6.800   6.192   1.00 9.37  ? 309  ARG A NH2 1 
ATOM   2339 N  N   . PRO A 1 308 ? 72.757  -0.225  4.418   1.00 8.97  ? 310  PRO A N   1 
ATOM   2340 C  CA  . PRO A 1 308 ? 72.503  -0.242  2.976   1.00 9.08  ? 310  PRO A CA  1 
ATOM   2341 C  C   . PRO A 1 308 ? 72.683  1.118   2.305   1.00 9.21  ? 310  PRO A C   1 
ATOM   2342 O  O   . PRO A 1 308 ? 72.852  1.187   1.086   1.00 9.37  ? 310  PRO A O   1 
ATOM   2343 C  CB  . PRO A 1 308 ? 71.037  -0.676  2.883   1.00 9.49  ? 310  PRO A CB  1 
ATOM   2344 C  CG  . PRO A 1 308 ? 70.783  -1.426  4.148   1.00 9.96  ? 310  PRO A CG  1 
ATOM   2345 C  CD  . PRO A 1 308 ? 71.613  -0.739  5.190   1.00 9.27  ? 310  PRO A CD  1 
ATOM   2346 N  N   . ARG A 1 309 ? 72.596  2.188   3.089   1.00 9.09  ? 311  ARG A N   1 
ATOM   2347 C  CA  . ARG A 1 309 ? 72.638  3.544   2.551   1.00 9.44  ? 311  ARG A CA  1 
ATOM   2348 C  C   . ARG A 1 309 ? 71.665  3.720   1.380   1.00 10.00 ? 311  ARG A C   1 
ATOM   2349 O  O   . ARG A 1 309 ? 70.470  3.452   1.521   1.00 10.05 ? 311  ARG A O   1 
ATOM   2350 C  CB  . ARG A 1 309 ? 74.080  3.942   2.189   1.00 9.49  ? 311  ARG A CB  1 
ATOM   2351 C  CG  . ARG A 1 309 ? 75.054  3.712   3.341   1.00 9.36  ? 311  ARG A CG  1 
ATOM   2352 C  CD  . ARG A 1 309 ? 76.476  4.192   3.064   1.00 9.02  ? 311  ARG A CD  1 
ATOM   2353 N  NE  . ARG A 1 309 ? 77.388  3.663   4.077   1.00 9.41  ? 311  ARG A NE  1 
ATOM   2354 C  CZ  . ARG A 1 309 ? 78.419  4.321   4.599   1.00 9.31  ? 311  ARG A CZ  1 
ATOM   2355 N  NH1 . ARG A 1 309 ? 78.727  5.542   4.177   1.00 8.80  ? 311  ARG A NH1 1 
ATOM   2356 N  NH2 . ARG A 1 309 ? 79.154  3.749   5.544   1.00 9.51  ? 311  ARG A NH2 1 
ATOM   2357 N  N   . ALA A 1 310 ? 72.162  4.173   0.233   1.00 10.14 ? 312  ALA A N   1 
ATOM   2358 C  CA  . ALA A 1 310 ? 71.279  4.501   -0.890  1.00 10.63 ? 312  ALA A CA  1 
ATOM   2359 C  C   . ALA A 1 310 ? 70.484  3.302   -1.407  1.00 10.95 ? 312  ALA A C   1 
ATOM   2360 O  O   . ALA A 1 310 ? 69.527  3.469   -2.163  1.00 10.29 ? 312  ALA A O   1 
ATOM   2361 C  CB  . ALA A 1 310 ? 72.060  5.150   -2.024  1.00 10.42 ? 312  ALA A CB  1 
ATOM   2362 N  N   . ASP A 1 311 ? 70.882  2.095   -1.009  1.00 11.25 ? 313  ASP A N   1 
ATOM   2363 C  CA  . ASP A 1 311 ? 70.167  0.888   -1.428  1.00 11.53 ? 313  ASP A CA  1 
ATOM   2364 C  C   . ASP A 1 311 ? 68.736  0.876   -0.900  1.00 12.24 ? 313  ASP A C   1 
ATOM   2365 O  O   . ASP A 1 311 ? 67.866  0.207   -1.458  1.00 12.82 ? 313  ASP A O   1 
ATOM   2366 C  CB  . ASP A 1 311 ? 70.899  -0.376  -0.964  1.00 11.29 ? 313  ASP A CB  1 
ATOM   2367 C  CG  . ASP A 1 311 ? 72.073  -0.734  -1.856  1.00 12.53 ? 313  ASP A CG  1 
ATOM   2368 O  OD1 . ASP A 1 311 ? 72.201  -0.145  -2.955  1.00 12.74 ? 313  ASP A OD1 1 
ATOM   2369 O  OD2 . ASP A 1 311 ? 72.864  -1.620  -1.460  1.00 12.79 ? 313  ASP A OD2 1 
ATOM   2370 N  N   . LEU A 1 312 ? 68.502  1.589   0.196   1.00 12.54 ? 314  LEU A N   1 
ATOM   2371 C  CA  . LEU A 1 312 ? 67.152  1.714   0.741   1.00 13.25 ? 314  LEU A CA  1 
ATOM   2372 C  C   . LEU A 1 312 ? 66.586  3.106   0.497   1.00 13.50 ? 314  LEU A C   1 
ATOM   2373 O  O   . LEU A 1 312 ? 65.740  3.582   1.252   1.00 14.27 ? 314  LEU A O   1 
ATOM   2374 C  CB  . LEU A 1 312 ? 67.124  1.375   2.234   1.00 13.51 ? 314  LEU A CB  1 
ATOM   2375 C  CG  . LEU A 1 312 ? 67.226  -0.115  2.582   1.00 13.97 ? 314  LEU A CG  1 
ATOM   2376 C  CD1 . LEU A 1 312 ? 67.100  -0.340  4.084   1.00 14.11 ? 314  LEU A CD1 1 
ATOM   2377 C  CD2 . LEU A 1 312 ? 66.173  -0.918  1.835   1.00 14.10 ? 314  LEU A CD2 1 
ATOM   2378 N  N   . GLY A 1 313 ? 67.064  3.752   -0.562  1.00 13.65 ? 315  GLY A N   1 
ATOM   2379 C  CA  . GLY A 1 313 ? 66.528  5.037   -0.991  1.00 14.77 ? 315  GLY A CA  1 
ATOM   2380 C  C   . GLY A 1 313 ? 67.198  6.215   -0.312  1.00 14.47 ? 315  GLY A C   1 
ATOM   2381 O  O   . GLY A 1 313 ? 68.236  6.068   0.336   1.00 14.56 ? 315  GLY A O   1 
ATOM   2382 N  N   . GLY A 1 314 ? 66.596  7.391   -0.454  1.00 13.94 ? 316  GLY A N   1 
ATOM   2383 C  CA  . GLY A 1 314 ? 67.150  8.601   0.135   1.00 13.52 ? 316  GLY A CA  1 
ATOM   2384 C  C   . GLY A 1 314 ? 68.178  9.260   -0.763  1.00 13.75 ? 316  GLY A C   1 
ATOM   2385 O  O   . GLY A 1 314 ? 68.181  9.055   -1.977  1.00 13.28 ? 316  GLY A O   1 
ATOM   2386 N  N   . SER A 1 315 ? 69.051  10.060  -0.163  1.00 13.21 ? 317  SER A N   1 
ATOM   2387 C  CA  . SER A 1 315 ? 69.983  10.885  -0.921  1.00 14.37 ? 317  SER A CA  1 
ATOM   2388 C  C   . SER A 1 315 ? 71.060  10.049  -1.607  1.00 14.62 ? 317  SER A C   1 
ATOM   2389 O  O   . SER A 1 315 ? 71.633  9.140   -1.006  1.00 13.76 ? 317  SER A O   1 
ATOM   2390 C  CB  . SER A 1 315 ? 70.632  11.924  -0.009  1.00 14.83 ? 317  SER A CB  1 
ATOM   2391 O  OG  . SER A 1 315 ? 71.480  12.785  -0.746  1.00 16.20 ? 317  SER A OG  1 
ATOM   2392 N  N   . LEU A 1 316 ? 71.349  10.382  -2.861  1.00 15.06 ? 318  LEU A N   1 
ATOM   2393 C  CA  . LEU A 1 316 ? 72.437  9.745   -3.594  1.00 15.35 ? 318  LEU A CA  1 
ATOM   2394 C  C   . LEU A 1 316 ? 73.770  10.429  -3.308  1.00 15.36 ? 318  LEU A C   1 
ATOM   2395 O  O   . LEU A 1 316 ? 74.834  9.849   -3.528  1.00 15.54 ? 318  LEU A O   1 
ATOM   2396 C  CB  . LEU A 1 316 ? 72.145  9.752   -5.100  1.00 16.21 ? 318  LEU A CB  1 
ATOM   2397 C  CG  . LEU A 1 316 ? 70.829  9.098   -5.528  1.00 17.18 ? 318  LEU A CG  1 
ATOM   2398 C  CD1 . LEU A 1 316 ? 70.750  8.964   -7.041  1.00 17.95 ? 318  LEU A CD1 1 
ATOM   2399 C  CD2 . LEU A 1 316 ? 70.653  7.745   -4.861  1.00 17.90 ? 318  LEU A CD2 1 
ATOM   2400 N  N   . THR A 1 317 ? 73.709  11.651  -2.788  1.00 15.20 ? 319  THR A N   1 
ATOM   2401 C  CA  . THR A 1 317 ? 74.906  12.335  -2.304  1.00 16.04 ? 319  THR A CA  1 
ATOM   2402 C  C   . THR A 1 317 ? 74.980  12.282  -0.781  1.00 16.27 ? 319  THR A C   1 
ATOM   2403 O  O   . THR A 1 317 ? 73.952  12.297  -0.104  1.00 17.05 ? 319  THR A O   1 
ATOM   2404 C  CB  . THR A 1 317 ? 74.943  13.811  -2.755  1.00 17.26 ? 319  THR A CB  1 
ATOM   2405 O  OG1 . THR A 1 317 ? 73.814  14.504  -2.211  1.00 16.97 ? 319  THR A OG1 1 
ATOM   2406 C  CG2 . THR A 1 317 ? 74.907  13.908  -4.273  1.00 17.36 ? 319  THR A CG2 1 
ATOM   2407 N  N   . PRO A 1 318 ? 76.201  12.213  -0.234  1.00 16.51 ? 320  PRO A N   1 
ATOM   2408 C  CA  . PRO A 1 318 ? 76.377  12.109  1.213   1.00 16.86 ? 320  PRO A CA  1 
ATOM   2409 C  C   . PRO A 1 318 ? 75.891  13.373  1.918   1.00 17.32 ? 320  PRO A C   1 
ATOM   2410 O  O   . PRO A 1 318 ? 76.097  14.478  1.416   1.00 16.92 ? 320  PRO A O   1 
ATOM   2411 C  CB  . PRO A 1 318 ? 77.896  11.961  1.378   1.00 17.27 ? 320  PRO A CB  1 
ATOM   2412 C  CG  . PRO A 1 318 ? 78.409  11.570  0.031   1.00 16.74 ? 320  PRO A CG  1 
ATOM   2413 C  CD  . PRO A 1 318 ? 77.487  12.229  -0.948  1.00 16.34 ? 320  PRO A CD  1 
ATOM   2414 N  N   . PRO A 1 319 ? 75.261  13.210  3.077   1.00 17.06 ? 321  PRO A N   1 
ATOM   2415 C  CA  . PRO A 1 319 ? 75.121  11.905  3.704   1.00 16.32 ? 321  PRO A CA  1 
ATOM   2416 C  C   . PRO A 1 319 ? 73.785  11.258  3.358   1.00 15.81 ? 321  PRO A C   1 
ATOM   2417 O  O   . PRO A 1 319 ? 72.750  11.925  3.370   1.00 15.63 ? 321  PRO A O   1 
ATOM   2418 C  CB  . PRO A 1 319 ? 75.161  12.240  5.195   1.00 16.72 ? 321  PRO A CB  1 
ATOM   2419 C  CG  . PRO A 1 319 ? 74.553  13.601  5.278   1.00 16.63 ? 321  PRO A CG  1 
ATOM   2420 C  CD  . PRO A 1 319 ? 74.905  14.310  3.994   1.00 17.01 ? 321  PRO A CD  1 
ATOM   2421 N  N   . ASN A 1 320 ? 73.809  9.962   3.065   1.00 13.49 ? 322  ASN A N   1 
ATOM   2422 C  CA  . ASN A 1 320 ? 72.578  9.194   2.982   1.00 12.22 ? 322  ASN A CA  1 
ATOM   2423 C  C   . ASN A 1 320 ? 72.048  8.866   4.375   1.00 12.29 ? 322  ASN A C   1 
ATOM   2424 O  O   . ASN A 1 320 ? 72.816  8.514   5.270   1.00 11.61 ? 322  ASN A O   1 
ATOM   2425 C  CB  . ASN A 1 320 ? 72.790  7.911   2.177   1.00 11.60 ? 322  ASN A CB  1 
ATOM   2426 C  CG  . ASN A 1 320 ? 71.531  7.069   2.089   1.00 11.83 ? 322  ASN A CG  1 
ATOM   2427 O  OD1 . ASN A 1 320 ? 71.228  6.293   2.995   1.00 11.98 ? 322  ASN A OD1 1 
ATOM   2428 N  ND2 . ASN A 1 320 ? 70.770  7.249   1.017   1.00 12.17 ? 322  ASN A ND2 1 
ATOM   2429 N  N   . LEU A 1 321 ? 70.735  8.982   4.553   1.00 12.28 ? 323  LEU A N   1 
ATOM   2430 C  CA  . LEU A 1 321 ? 70.141  8.934   5.890   1.00 12.46 ? 323  LEU A CA  1 
ATOM   2431 C  C   . LEU A 1 321 ? 69.121  7.809   6.056   1.00 12.43 ? 323  LEU A C   1 
ATOM   2432 O  O   . LEU A 1 321 ? 68.355  7.797   7.023   1.00 11.62 ? 323  LEU A O   1 
ATOM   2433 C  CB  . LEU A 1 321 ? 69.495  10.277  6.238   1.00 12.90 ? 323  LEU A CB  1 
ATOM   2434 C  CG  . LEU A 1 321 ? 70.437  11.478  6.349   1.00 13.34 ? 323  LEU A CG  1 
ATOM   2435 C  CD1 . LEU A 1 321 ? 69.651  12.748  6.646   1.00 14.41 ? 323  LEU A CD1 1 
ATOM   2436 C  CD2 . LEU A 1 321 ? 71.493  11.228  7.416   1.00 13.44 ? 323  LEU A CD2 1 
ATOM   2437 N  N   . SER A 1 322 ? 69.146  6.845   5.140   1.00 11.72 ? 324  SER A N   1 
ATOM   2438 C  CA  . SER A 1 322 ? 68.167  5.759   5.136   1.00 11.38 ? 324  SER A CA  1 
ATOM   2439 C  C   . SER A 1 322 ? 68.298  4.856   6.359   1.00 12.05 ? 324  SER A C   1 
ATOM   2440 O  O   . SER A 1 322 ? 69.393  4.684   6.901   1.00 12.55 ? 324  SER A O   1 
ATOM   2441 C  CB  . SER A 1 322 ? 68.302  4.917   3.863   1.00 11.82 ? 324  SER A CB  1 
ATOM   2442 O  OG  . SER A 1 322 ? 69.393  4.015   3.973   1.00 11.60 ? 324  SER A OG  1 
ATOM   2443 N  N   . ALA A 1 323 ? 67.181  4.247   6.756   1.00 10.98 ? 325  ALA A N   1 
ATOM   2444 C  CA  . ALA A 1 323 ? 67.186  3.143   7.713   1.00 11.34 ? 325  ALA A CA  1 
ATOM   2445 C  C   . ALA A 1 323 ? 67.874  3.503   9.025   1.00 11.29 ? 325  ALA A C   1 
ATOM   2446 O  O   . ALA A 1 323 ? 68.607  2.691   9.593   1.00 11.06 ? 325  ALA A O   1 
ATOM   2447 C  CB  . ALA A 1 323 ? 67.830  1.905   7.099   1.00 11.00 ? 325  ALA A CB  1 
ATOM   2448 N  N   . GLY A 1 324 ? 67.639  4.719   9.506   1.00 11.42 ? 326  GLY A N   1 
ATOM   2449 C  CA  . GLY A 1 324 ? 68.285  5.190   10.725  1.00 10.85 ? 326  GLY A CA  1 
ATOM   2450 C  C   . GLY A 1 324 ? 67.860  4.390   11.938  1.00 11.55 ? 326  GLY A C   1 
ATOM   2451 O  O   . GLY A 1 324 ? 68.644  4.181   12.867  1.00 11.57 ? 326  GLY A O   1 
ATOM   2452 N  N   . ALA A 1 325 ? 66.617  3.921   11.921  1.00 11.55 ? 327  ALA A N   1 
ATOM   2453 C  CA  . ALA A 1 325 ? 66.083  3.146   13.033  1.00 11.83 ? 327  ALA A CA  1 
ATOM   2454 C  C   . ALA A 1 325 ? 66.739  1.770   13.125  1.00 11.73 ? 327  ALA A C   1 
ATOM   2455 O  O   . ALA A 1 325 ? 66.623  1.091   14.145  1.00 11.38 ? 327  ALA A O   1 
ATOM   2456 C  CB  . ALA A 1 325 ? 64.573  3.007   12.911  1.00 12.04 ? 327  ALA A CB  1 
ATOM   2457 N  N   . ASN A 1 326 ? 67.409  1.355   12.054  1.00 11.59 ? 328  ASN A N   1 
ATOM   2458 C  CA  . ASN A 1 326 ? 68.136  0.085   12.062  1.00 12.07 ? 328  ASN A CA  1 
ATOM   2459 C  C   . ASN A 1 326 ? 69.631  0.232   12.359  1.00 12.37 ? 328  ASN A C   1 
ATOM   2460 O  O   . ASN A 1 326 ? 70.436  -0.623  11.988  1.00 12.13 ? 328  ASN A O   1 
ATOM   2461 C  CB  . ASN A 1 326 ? 67.910  -0.673  10.748  1.00 12.35 ? 328  ASN A CB  1 
ATOM   2462 C  CG  . ASN A 1 326 ? 66.437  -0.903  10.455  1.00 12.99 ? 328  ASN A CG  1 
ATOM   2463 O  OD1 . ASN A 1 326 ? 65.893  -0.374  9.483   1.00 13.51 ? 328  ASN A OD1 1 
ATOM   2464 N  ND2 . ASN A 1 326 ? 65.778  -1.673  11.312  1.00 13.38 ? 328  ASN A ND2 1 
ATOM   2465 N  N   . SER A 1 327 ? 69.995  1.311   13.045  1.00 11.58 ? 329  SER A N   1 
ATOM   2466 C  CA  . SER A 1 327 ? 71.388  1.549   13.416  1.00 11.12 ? 329  SER A CA  1 
ATOM   2467 C  C   . SER A 1 327 ? 71.751  0.867   14.735  1.00 10.59 ? 329  SER A C   1 
ATOM   2468 O  O   . SER A 1 327 ? 70.915  0.746   15.628  1.00 10.85 ? 329  SER A O   1 
ATOM   2469 C  CB  . SER A 1 327 ? 71.659  3.051   13.519  1.00 11.42 ? 329  SER A CB  1 
ATOM   2470 O  OG  . SER A 1 327 ? 71.309  3.705   12.311  1.00 12.15 ? 329  SER A OG  1 
ATOM   2471 N  N   . ILE A 1 328 ? 72.998  0.417   14.844  1.00 9.75  ? 330  ILE A N   1 
ATOM   2472 C  CA  . ILE A 1 328 ? 73.544  -0.047  16.118  1.00 9.40  ? 330  ILE A CA  1 
ATOM   2473 C  C   . ILE A 1 328 ? 74.841  0.693   16.442  1.00 9.41  ? 330  ILE A C   1 
ATOM   2474 O  O   . ILE A 1 328 ? 75.584  1.074   15.538  1.00 8.80  ? 330  ILE A O   1 
ATOM   2475 C  CB  . ILE A 1 328 ? 73.836  -1.560  16.086  1.00 9.20  ? 330  ILE A CB  1 
ATOM   2476 C  CG1 . ILE A 1 328 ? 74.791  -1.891  14.934  1.00 8.80  ? 330  ILE A CG1 1 
ATOM   2477 C  CG2 . ILE A 1 328 ? 72.541  -2.349  15.952  1.00 9.44  ? 330  ILE A CG2 1 
ATOM   2478 C  CD1 . ILE A 1 328 ? 75.316  -3.313  14.957  1.00 8.30  ? 330  ILE A CD1 1 
ATOM   2479 N  N   . MET A 1 329 ? 75.103  0.905   17.731  1.00 9.64  ? 331  MET A N   1 
ATOM   2480 C  CA  . MET A 1 329 ? 76.435  1.304   18.180  1.00 10.68 ? 331  MET A CA  1 
ATOM   2481 C  C   . MET A 1 329 ? 77.267  0.058   18.467  1.00 10.17 ? 331  MET A C   1 
ATOM   2482 O  O   . MET A 1 329 ? 76.812  -0.843  19.171  1.00 10.08 ? 331  MET A O   1 
ATOM   2483 C  CB  . MET A 1 329 ? 76.346  2.159   19.446  1.00 11.85 ? 331  MET A CB  1 
ATOM   2484 C  CG  . MET A 1 329 ? 75.759  3.544   19.229  1.00 12.90 ? 331  MET A CG  1 
ATOM   2485 S  SD  . MET A 1 329 ? 76.872  4.680   18.375  1.00 14.83 ? 331  MET A SD  1 
ATOM   2486 C  CE  . MET A 1 329 ? 78.457  4.227   19.069  1.00 15.32 ? 331  MET A CE  1 
ATOM   2487 N  N   . ARG A 1 330 ? 78.470  -0.002  17.901  1.00 9.71  ? 332  ARG A N   1 
ATOM   2488 C  CA  . ARG A 1 330 ? 79.326  -1.180  18.043  1.00 9.93  ? 332  ARG A CA  1 
ATOM   2489 C  C   . ARG A 1 330 ? 80.493  -0.909  18.987  1.00 10.37 ? 332  ARG A C   1 
ATOM   2490 O  O   . ARG A 1 330 ? 81.220  0.071   18.818  1.00 10.58 ? 332  ARG A O   1 
ATOM   2491 C  CB  . ARG A 1 330 ? 79.848  -1.632  16.675  1.00 9.87  ? 332  ARG A CB  1 
ATOM   2492 C  CG  . ARG A 1 330 ? 78.795  -2.310  15.809  1.00 9.64  ? 332  ARG A CG  1 
ATOM   2493 C  CD  . ARG A 1 330 ? 79.319  -2.593  14.406  1.00 11.24 ? 332  ARG A CD  1 
ATOM   2494 N  NE  . ARG A 1 330 ? 79.886  -1.393  13.798  1.00 10.28 ? 332  ARG A NE  1 
ATOM   2495 C  CZ  . ARG A 1 330 ? 81.125  -1.306  13.328  1.00 10.77 ? 332  ARG A CZ  1 
ATOM   2496 N  NH1 . ARG A 1 330 ? 81.922  -2.364  13.350  1.00 11.63 ? 332  ARG A NH1 1 
ATOM   2497 N  NH2 . ARG A 1 330 ? 81.568  -0.156  12.841  1.00 11.20 ? 332  ARG A NH2 1 
ATOM   2498 N  N   . SER A 1 331 ? 80.659  -1.765  19.991  1.00 10.67 ? 333  SER A N   1 
ATOM   2499 C  CA  . SER A 1 331 ? 81.787  -1.638  20.911  1.00 11.21 ? 333  SER A CA  1 
ATOM   2500 C  C   . SER A 1 331 ? 82.538  -2.954  21.054  1.00 10.77 ? 333  SER A C   1 
ATOM   2501 O  O   . SER A 1 331 ? 83.009  -3.293  22.142  1.00 10.48 ? 333  SER A O   1 
ATOM   2502 C  CB  . SER A 1 331 ? 81.318  -1.164  22.285  1.00 12.32 ? 333  SER A CB  1 
ATOM   2503 O  OG  . SER A 1 331 ? 80.614  0.061   22.184  1.00 15.54 ? 333  SER A OG  1 
ATOM   2504 N  N   . GLY A 1 332 ? 82.647  -3.689  19.954  1.00 10.35 ? 334  GLY A N   1 
ATOM   2505 C  CA  . GLY A 1 332 ? 83.287  -5.001  19.976  1.00 10.47 ? 334  GLY A CA  1 
ATOM   2506 C  C   . GLY A 1 332 ? 84.789  -4.884  20.128  1.00 10.61 ? 334  GLY A C   1 
ATOM   2507 O  O   . GLY A 1 332 ? 85.366  -3.824  19.871  1.00 11.41 ? 334  GLY A O   1 
ATOM   2508 N  N   . ILE A 1 333 ? 85.426  -5.979  20.531  1.00 10.14 ? 335  ILE A N   1 
ATOM   2509 C  CA  . ILE A 1 333 ? 86.865  -5.988  20.754  1.00 10.06 ? 335  ILE A CA  1 
ATOM   2510 C  C   . ILE A 1 333 ? 87.388  -7.401  20.533  1.00 9.57  ? 335  ILE A C   1 
ATOM   2511 O  O   . ILE A 1 333 ? 86.704  -8.374  20.853  1.00 8.86  ? 335  ILE A O   1 
ATOM   2512 C  CB  . ILE A 1 333 ? 87.217  -5.488  22.176  1.00 10.48 ? 335  ILE A CB  1 
ATOM   2513 C  CG1 . ILE A 1 333 ? 88.723  -5.567  22.427  1.00 10.98 ? 335  ILE A CG1 1 
ATOM   2514 C  CG2 . ILE A 1 333 ? 86.439  -6.258  23.233  1.00 10.41 ? 335  ILE A CG2 1 
ATOM   2515 C  CD1 . ILE A 1 333 ? 89.168  -4.858  23.690  1.00 12.29 ? 335  ILE A CD1 1 
ATOM   2516 N  N   . PRO A 1 334 ? 88.552  -7.524  19.877  1.00 9.88  ? 336  PRO A N   1 
ATOM   2517 C  CA  . PRO A 1 334 ? 89.020  -8.861  19.513  1.00 9.74  ? 336  PRO A CA  1 
ATOM   2518 C  C   . PRO A 1 334 ? 89.411  -9.677  20.743  1.00 10.06 ? 336  PRO A C   1 
ATOM   2519 O  O   . PRO A 1 334 ? 89.741  -9.105  21.782  1.00 10.26 ? 336  PRO A O   1 
ATOM   2520 C  CB  . PRO A 1 334 ? 90.247  -8.577  18.639  1.00 9.68  ? 336  PRO A CB  1 
ATOM   2521 C  CG  . PRO A 1 334 ? 90.004  -7.213  18.080  1.00 10.18 ? 336  PRO A CG  1 
ATOM   2522 C  CD  . PRO A 1 334 ? 89.288  -6.463  19.168  1.00 10.78 ? 336  PRO A CD  1 
ATOM   2523 N  N   . TYR A 1 335 ? 89.328  -11.002 20.641  1.00 10.07 ? 337  TYR A N   1 
ATOM   2524 C  CA  . TYR A 1 335 ? 89.773  -11.874 21.727  1.00 9.94  ? 337  TYR A CA  1 
ATOM   2525 C  C   . TYR A 1 335 ? 90.657  -12.999 21.206  1.00 9.83  ? 337  TYR A C   1 
ATOM   2526 O  O   . TYR A 1 335 ? 90.673  -13.284 20.007  1.00 9.35  ? 337  TYR A O   1 
ATOM   2527 C  CB  . TYR A 1 335 ? 88.582  -12.436 22.519  1.00 10.26 ? 337  TYR A CB  1 
ATOM   2528 C  CG  . TYR A 1 335 ? 87.807  -13.536 21.817  1.00 10.53 ? 337  TYR A CG  1 
ATOM   2529 C  CD1 . TYR A 1 335 ? 86.717  -13.236 21.010  1.00 10.35 ? 337  TYR A CD1 1 
ATOM   2530 C  CD2 . TYR A 1 335 ? 88.128  -14.877 22.009  1.00 10.53 ? 337  TYR A CD2 1 
ATOM   2531 C  CE1 . TYR A 1 335 ? 85.998  -14.231 20.376  1.00 10.84 ? 337  TYR A CE1 1 
ATOM   2532 C  CE2 . TYR A 1 335 ? 87.416  -15.881 21.374  1.00 11.56 ? 337  TYR A CE2 1 
ATOM   2533 C  CZ  . TYR A 1 335 ? 86.345  -15.551 20.563  1.00 11.52 ? 337  TYR A CZ  1 
ATOM   2534 O  OH  . TYR A 1 335 ? 85.623  -16.538 19.929  1.00 11.89 ? 337  TYR A OH  1 
ATOM   2535 N  N   . GLY A 1 336 ? 91.421  -13.608 22.107  1.00 9.61  ? 338  GLY A N   1 
ATOM   2536 C  CA  . GLY A 1 336 ? 92.252  -14.751 21.752  1.00 9.33  ? 338  GLY A CA  1 
ATOM   2537 C  C   . GLY A 1 336 ? 93.654  -14.369 21.321  1.00 9.93  ? 338  GLY A C   1 
ATOM   2538 O  O   . GLY A 1 336 ? 93.968  -13.186 21.174  1.00 10.33 ? 338  GLY A O   1 
ATOM   2539 N  N   . PRO A 1 337 ? 94.508  -15.377 21.095  1.00 10.19 ? 339  PRO A N   1 
ATOM   2540 C  CA  . PRO A 1 337 ? 95.878  -15.122 20.680  1.00 10.63 ? 339  PRO A CA  1 
ATOM   2541 C  C   . PRO A 1 337 ? 95.947  -14.713 19.215  1.00 10.71 ? 339  PRO A C   1 
ATOM   2542 O  O   . PRO A 1 337 ? 95.049  -15.028 18.436  1.00 10.81 ? 339  PRO A O   1 
ATOM   2543 C  CB  . PRO A 1 337 ? 96.553  -16.480 20.876  1.00 10.12 ? 339  PRO A CB  1 
ATOM   2544 C  CG  . PRO A 1 337 ? 95.458  -17.463 20.644  1.00 10.36 ? 339  PRO A CG  1 
ATOM   2545 C  CD  . PRO A 1 337 ? 94.216  -16.817 21.197  1.00 10.03 ? 339  PRO A CD  1 
ATOM   2546 N  N   . GLU A 1 338 ? 97.011  -14.009 18.852  1.00 10.91 ? 340  GLU A N   1 
ATOM   2547 C  CA  . GLU A 1 338 ? 97.350  -13.821 17.450  1.00 11.09 ? 340  GLU A CA  1 
ATOM   2548 C  C   . GLU A 1 338 ? 97.497  -15.169 16.749  1.00 10.85 ? 340  GLU A C   1 
ATOM   2549 O  O   . GLU A 1 338 ? 97.727  -16.192 17.394  1.00 10.24 ? 340  GLU A O   1 
ATOM   2550 C  CB  . GLU A 1 338 ? 98.637  -13.009 17.331  1.00 11.59 ? 340  GLU A CB  1 
ATOM   2551 C  CG  . GLU A 1 338 ? 98.485  -11.574 17.811  1.00 11.82 ? 340  GLU A CG  1 
ATOM   2552 C  CD  . GLU A 1 338 ? 97.637  -10.741 16.868  1.00 12.44 ? 340  GLU A CD  1 
ATOM   2553 O  OE1 . GLU A 1 338 ? 98.049  -10.567 15.705  1.00 13.67 ? 340  GLU A OE1 1 
ATOM   2554 O  OE2 . GLU A 1 338 ? 96.553  -10.277 17.281  1.00 13.36 ? 340  GLU A OE2 1 
ATOM   2555 N  N   . VAL A 1 339 ? 97.303  -15.176 15.433  1.00 10.58 ? 341  VAL A N   1 
ATOM   2556 C  CA  . VAL A 1 339 ? 97.493  -16.384 14.644  1.00 9.88  ? 341  VAL A CA  1 
ATOM   2557 C  C   . VAL A 1 339 ? 98.926  -16.892 14.801  1.00 10.26 ? 341  VAL A C   1 
ATOM   2558 O  O   . VAL A 1 339 ? 99.887  -16.137 14.634  1.00 9.50  ? 341  VAL A O   1 
ATOM   2559 C  CB  . VAL A 1 339 ? 97.210  -16.132 13.148  1.00 9.92  ? 341  VAL A CB  1 
ATOM   2560 C  CG1 . VAL A 1 339 ? 97.422  -17.410 12.351  1.00 9.87  ? 341  VAL A CG1 1 
ATOM   2561 C  CG2 . VAL A 1 339 ? 95.793  -15.606 12.956  1.00 10.31 ? 341  VAL A CG2 1 
ATOM   2562 N  N   . THR A 1 340 ? 99.064  -18.166 15.149  1.00 10.51 ? 342  THR A N   1 
ATOM   2563 C  CA  . THR A 1 340 ? 100.383 -18.756 15.354  1.00 11.22 ? 342  THR A CA  1 
ATOM   2564 C  C   . THR A 1 340 ? 100.995 -19.236 14.043  1.00 12.52 ? 342  THR A C   1 
ATOM   2565 O  O   . THR A 1 340 ? 100.298 -19.380 13.037  1.00 12.17 ? 342  THR A O   1 
ATOM   2566 C  CB  . THR A 1 340 ? 100.330 -19.926 16.347  1.00 11.17 ? 342  THR A CB  1 
ATOM   2567 O  OG1 . THR A 1 340 ? 99.493  -20.962 15.820  1.00 11.10 ? 342  THR A OG1 1 
ATOM   2568 C  CG2 . THR A 1 340 ? 99.779  -19.462 17.686  1.00 11.07 ? 342  THR A CG2 1 
ATOM   2569 N  N   . SER A 1 341 ? 102.301 -19.486 14.061  1.00 13.33 ? 343  SER A N   1 
ATOM   2570 C  CA  . SER A 1 341 ? 103.005 -19.911 12.854  1.00 14.51 ? 343  SER A CA  1 
ATOM   2571 C  C   . SER A 1 341 ? 102.514 -21.271 12.360  1.00 12.93 ? 343  SER A C   1 
ATOM   2572 O  O   . SER A 1 341 ? 102.337 -21.470 11.161  1.00 13.38 ? 343  SER A O   1 
ATOM   2573 C  CB  . SER A 1 341 ? 104.519 -19.930 13.084  1.00 15.68 ? 343  SER A CB  1 
ATOM   2574 O  OG  . SER A 1 341 ? 104.840 -20.655 14.256  1.00 19.65 ? 343  SER A OG  1 
ATOM   2575 N  N   . ALA A 1 342 ? 102.250 -22.186 13.288  1.00 12.54 ? 344  ALA A N   1 
ATOM   2576 C  CA  . ALA A 1 342 ? 101.755 -23.516 12.929  1.00 12.56 ? 344  ALA A CA  1 
ATOM   2577 C  C   . ALA A 1 342 ? 100.370 -23.448 12.289  1.00 12.42 ? 344  ALA A C   1 
ATOM   2578 O  O   . ALA A 1 342 ? 100.054 -24.216 11.378  1.00 12.46 ? 344  ALA A O   1 
ATOM   2579 C  CB  . ALA A 1 342 ? 101.727 -24.424 14.150  1.00 12.66 ? 344  ALA A CB  1 
ATOM   2580 N  N   . GLU A 1 343 ? 99.538  -22.537 12.779  1.00 11.79 ? 345  GLU A N   1 
ATOM   2581 C  CA  . GLU A 1 343 ? 98.199  -22.371 12.226  1.00 12.88 ? 345  GLU A CA  1 
ATOM   2582 C  C   . GLU A 1 343 ? 98.260  -21.750 10.836  1.00 13.14 ? 345  GLU A C   1 
ATOM   2583 O  O   . GLU A 1 343 ? 97.581  -22.199 9.913   1.00 12.32 ? 345  GLU A O   1 
ATOM   2584 C  CB  . GLU A 1 343 ? 97.348  -21.499 13.144  1.00 12.01 ? 345  GLU A CB  1 
ATOM   2585 C  CG  . GLU A 1 343 ? 96.954  -22.172 14.447  1.00 12.06 ? 345  GLU A CG  1 
ATOM   2586 C  CD  . GLU A 1 343 ? 96.294  -21.204 15.402  1.00 12.18 ? 345  GLU A CD  1 
ATOM   2587 O  OE1 . GLU A 1 343 ? 97.001  -20.305 15.906  1.00 11.24 ? 345  GLU A OE1 1 
ATOM   2588 O  OE2 . GLU A 1 343 ? 95.064  -21.316 15.608  1.00 12.20 ? 345  GLU A OE2 1 
ATOM   2589 N  N   . SER A 1 344 ? 99.084  -20.720 10.692  1.00 13.72 ? 346  SER A N   1 
ATOM   2590 C  CA  . SER A 1 344 ? 99.233  -20.052 9.411   1.00 16.09 ? 346  SER A CA  1 
ATOM   2591 C  C   . SER A 1 344 ? 99.746  -21.028 8.359   1.00 16.72 ? 346  SER A C   1 
ATOM   2592 O  O   . SER A 1 344 ? 99.318  -20.994 7.207   1.00 16.37 ? 346  SER A O   1 
ATOM   2593 C  CB  . SER A 1 344 ? 100.180 -18.857 9.532   1.00 18.41 ? 346  SER A CB  1 
ATOM   2594 O  OG  . SER A 1 344 ? 100.259 -18.153 8.304   1.00 22.77 ? 346  SER A OG  1 
ATOM   2595 N  N   . ALA A 1 345 ? 100.646 -21.914 8.775   1.00 15.77 ? 347  ALA A N   1 
ATOM   2596 C  CA  . ALA A 1 345 ? 101.273 -22.869 7.871   1.00 15.63 ? 347  ALA A CA  1 
ATOM   2597 C  C   . ALA A 1 345 ? 100.306 -23.967 7.436   1.00 15.11 ? 347  ALA A C   1 
ATOM   2598 O  O   . ALA A 1 345 ? 100.284 -24.366 6.272   1.00 16.21 ? 347  ALA A O   1 
ATOM   2599 C  CB  . ALA A 1 345 ? 102.503 -23.477 8.530   1.00 15.86 ? 347  ALA A CB  1 
ATOM   2600 N  N   . SER A 1 346 ? 99.503  -24.450 8.377   1.00 14.21 ? 348  SER A N   1 
ATOM   2601 C  CA  . SER A 1 346 ? 98.589  -25.558 8.120   1.00 13.48 ? 348  SER A CA  1 
ATOM   2602 C  C   . SER A 1 346 ? 97.266  -25.084 7.521   1.00 12.46 ? 348  SER A C   1 
ATOM   2603 O  O   . SER A 1 346 ? 96.470  -25.893 7.045   1.00 12.23 ? 348  SER A O   1 
ATOM   2604 C  CB  . SER A 1 346 ? 98.308  -26.312 9.419   1.00 13.68 ? 348  SER A CB  1 
ATOM   2605 O  OG  . SER A 1 346 ? 97.518  -25.520 10.286  1.00 13.98 ? 348  SER A OG  1 
ATOM   2606 N  N   . ASN A 1 347 ? 97.021  -23.778 7.583   1.00 12.17 ? 349  ASN A N   1 
ATOM   2607 C  CA  . ASN A 1 347 ? 95.731  -23.205 7.192   1.00 12.51 ? 349  ASN A CA  1 
ATOM   2608 C  C   . ASN A 1 347 ? 94.588  -23.604 8.112   1.00 12.57 ? 349  ASN A C   1 
ATOM   2609 O  O   . ASN A 1 347 ? 93.418  -23.481 7.742   1.00 12.61 ? 349  ASN A O   1 
ATOM   2610 C  CB  . ASN A 1 347 ? 95.368  -23.598 5.762   1.00 12.56 ? 349  ASN A CB  1 
ATOM   2611 C  CG  . ASN A 1 347 ? 96.408  -23.163 4.757   1.00 13.92 ? 349  ASN A CG  1 
ATOM   2612 O  OD1 . ASN A 1 347 ? 96.917  -22.044 4.813   1.00 13.06 ? 349  ASN A OD1 1 
ATOM   2613 N  ND2 . ASN A 1 347 ? 96.739  -24.055 3.835   1.00 15.71 ? 349  ASN A ND2 1 
ATOM   2614 N  N   . THR A 1 348 ? 94.926  -24.061 9.313   1.00 12.15 ? 350  THR A N   1 
ATOM   2615 C  CA  . THR A 1 348 ? 93.950  -24.695 10.194  1.00 13.10 ? 350  THR A CA  1 
ATOM   2616 C  C   . THR A 1 348 ? 94.000  -24.082 11.589  1.00 12.50 ? 350  THR A C   1 
ATOM   2617 O  O   . THR A 1 348 ? 95.033  -24.122 12.259  1.00 13.36 ? 350  THR A O   1 
ATOM   2618 C  CB  . THR A 1 348 ? 94.208  -26.210 10.311  1.00 14.20 ? 350  THR A CB  1 
ATOM   2619 O  OG1 . THR A 1 348 ? 94.082  -26.818 9.020   1.00 14.68 ? 350  THR A OG1 1 
ATOM   2620 C  CG2 . THR A 1 348 ? 93.217  -26.854 11.275  1.00 13.89 ? 350  THR A CG2 1 
ATOM   2621 N  N   . THR A 1 349 ? 92.878  -23.510 12.013  1.00 11.34 ? 351  THR A N   1 
ATOM   2622 C  CA  . THR A 1 349 ? 92.745  -22.964 13.360  1.00 10.88 ? 351  THR A CA  1 
ATOM   2623 C  C   . THR A 1 349 ? 92.787  -24.058 14.422  1.00 10.85 ? 351  THR A C   1 
ATOM   2624 O  O   . THR A 1 349 ? 92.077  -25.061 14.319  1.00 10.46 ? 351  THR A O   1 
ATOM   2625 C  CB  . THR A 1 349 ? 91.420  -22.193 13.510  1.00 10.49 ? 351  THR A CB  1 
ATOM   2626 O  OG1 . THR A 1 349 ? 91.385  -21.116 12.569  1.00 9.94  ? 351  THR A OG1 1 
ATOM   2627 C  CG2 . THR A 1 349 ? 91.273  -21.640 14.928  1.00 10.36 ? 351  THR A CG2 1 
ATOM   2628 N  N   . THR A 1 350 ? 93.601  -23.847 15.453  1.00 10.75 ? 352  THR A N   1 
ATOM   2629 C  CA  . THR A 1 350 ? 93.566  -24.693 16.643  1.00 11.05 ? 352  THR A CA  1 
ATOM   2630 C  C   . THR A 1 350 ? 93.316  -23.879 17.906  1.00 11.06 ? 352  THR A C   1 
ATOM   2631 O  O   . THR A 1 350 ? 92.844  -24.409 18.907  1.00 11.24 ? 352  THR A O   1 
ATOM   2632 C  CB  . THR A 1 350 ? 94.873  -25.492 16.827  1.00 11.35 ? 352  THR A CB  1 
ATOM   2633 O  OG1 . THR A 1 350 ? 95.962  -24.592 17.067  1.00 11.52 ? 352  THR A OG1 1 
ATOM   2634 C  CG2 . THR A 1 350 ? 95.172  -26.339 15.598  1.00 11.43 ? 352  THR A CG2 1 
ATOM   2635 N  N   . GLN A 1 351 ? 93.653  -22.594 17.862  1.00 11.22 ? 353  GLN A N   1 
ATOM   2636 C  CA  . GLN A 1 351 ? 93.473  -21.724 19.016  1.00 11.42 ? 353  GLN A CA  1 
ATOM   2637 C  C   . GLN A 1 351 ? 92.312  -20.765 18.771  1.00 11.56 ? 353  GLN A C   1 
ATOM   2638 O  O   . GLN A 1 351 ? 92.297  -20.046 17.770  1.00 11.57 ? 353  GLN A O   1 
ATOM   2639 C  CB  . GLN A 1 351 ? 94.758  -20.942 19.292  1.00 11.19 ? 353  GLN A CB  1 
ATOM   2640 C  CG  . GLN A 1 351 ? 96.028  -21.777 19.163  1.00 11.96 ? 353  GLN A CG  1 
ATOM   2641 C  CD  . GLN A 1 351 ? 96.047  -22.957 20.114  1.00 12.26 ? 353  GLN A CD  1 
ATOM   2642 O  OE1 . GLN A 1 351 ? 96.157  -24.110 19.691  1.00 11.64 ? 353  GLN A OE1 1 
ATOM   2643 N  NE2 . GLN A 1 351 ? 95.899  -22.678 21.405  1.00 11.50 ? 353  GLN A NE2 1 
ATOM   2644 N  N   . GLU A 1 352 ? 91.321  -20.778 19.657  1.00 12.00 ? 354  GLU A N   1 
ATOM   2645 C  CA  . GLU A 1 352 ? 90.132  -19.967 19.423  1.00 11.98 ? 354  GLU A CA  1 
ATOM   2646 C  C   . GLU A 1 352 ? 90.448  -18.485 19.541  1.00 11.38 ? 354  GLU A C   1 
ATOM   2647 O  O   . GLU A 1 352 ? 90.997  -18.029 20.549  1.00 10.54 ? 354  GLU A O   1 
ATOM   2648 C  CB  . GLU A 1 352 ? 88.976  -20.338 20.355  1.00 13.82 ? 354  GLU A CB  1 
ATOM   2649 C  CG  . GLU A 1 352 ? 87.691  -19.600 19.995  1.00 15.47 ? 354  GLU A CG  1 
ATOM   2650 C  CD  . GLU A 1 352 ? 86.578  -19.800 21.003  1.00 17.11 ? 354  GLU A CD  1 
ATOM   2651 O  OE1 . GLU A 1 352 ? 86.710  -20.684 21.873  1.00 18.47 ? 354  GLU A OE1 1 
ATOM   2652 O  OE2 . GLU A 1 352 ? 85.570  -19.065 20.923  1.00 16.65 ? 354  GLU A OE2 1 
ATOM   2653 N  N   . ARG A 1 353 ? 90.119  -17.749 18.486  1.00 10.55 ? 355  ARG A N   1 
ATOM   2654 C  CA  . ARG A 1 353 ? 90.233  -16.297 18.476  1.00 9.87  ? 355  ARG A CA  1 
ATOM   2655 C  C   . ARG A 1 353 ? 89.016  -15.737 17.753  1.00 9.62  ? 355  ARG A C   1 
ATOM   2656 O  O   . ARG A 1 353 ? 88.315  -16.461 17.045  1.00 9.55  ? 355  ARG A O   1 
ATOM   2657 C  CB  . ARG A 1 353 ? 91.511  -15.870 17.748  1.00 10.03 ? 355  ARG A CB  1 
ATOM   2658 C  CG  . ARG A 1 353 ? 91.624  -16.408 16.329  1.00 10.12 ? 355  ARG A CG  1 
ATOM   2659 C  CD  . ARG A 1 353 ? 92.946  -16.014 15.683  1.00 10.57 ? 355  ARG A CD  1 
ATOM   2660 N  NE  . ARG A 1 353 ? 94.086  -16.556 16.419  1.00 10.28 ? 355  ARG A NE  1 
ATOM   2661 C  CZ  . ARG A 1 353 ? 94.563  -17.785 16.255  1.00 10.42 ? 355  ARG A CZ  1 
ATOM   2662 N  NH1 . ARG A 1 353 ? 94.023  -18.593 15.349  1.00 9.40  ? 355  ARG A NH1 1 
ATOM   2663 N  NH2 . ARG A 1 353 ? 95.586  -18.202 16.991  1.00 9.79  ? 355  ARG A NH2 1 
ATOM   2664 N  N   . GLY A 1 354 ? 88.761  -14.449 17.920  1.00 8.52  ? 356  GLY A N   1 
ATOM   2665 C  CA  . GLY A 1 354 ? 87.706  -13.815 17.149  1.00 8.63  ? 356  GLY A CA  1 
ATOM   2666 C  C   . GLY A 1 354 ? 87.341  -12.442 17.659  1.00 8.78  ? 356  GLY A C   1 
ATOM   2667 O  O   . GLY A 1 354 ? 88.213  -11.653 18.029  1.00 8.65  ? 356  GLY A O   1 
ATOM   2668 N  N   . LEU A 1 355 ? 86.042  -12.166 17.669  1.00 8.23  ? 357  LEU A N   1 
ATOM   2669 C  CA  . LEU A 1 355 ? 85.524  -10.862 18.064  1.00 8.11  ? 357  LEU A CA  1 
ATOM   2670 C  C   . LEU A 1 355 ? 84.537  -11.027 19.210  1.00 7.98  ? 357  LEU A C   1 
ATOM   2671 O  O   . LEU A 1 355 ? 83.569  -11.788 19.107  1.00 7.80  ? 357  LEU A O   1 
ATOM   2672 C  CB  . LEU A 1 355 ? 84.827  -10.191 16.876  1.00 8.00  ? 357  LEU A CB  1 
ATOM   2673 C  CG  . LEU A 1 355 ? 84.292  -8.780  17.122  1.00 8.58  ? 357  LEU A CG  1 
ATOM   2674 C  CD1 . LEU A 1 355 ? 85.453  -7.810  17.297  1.00 9.05  ? 357  LEU A CD1 1 
ATOM   2675 C  CD2 . LEU A 1 355 ? 83.395  -8.335  15.978  1.00 8.68  ? 357  LEU A CD2 1 
ATOM   2676 N  N   . ALA A 1 356 ? 84.806  -10.351 20.320  1.00 7.66  ? 358  ALA A N   1 
ATOM   2677 C  CA  . ALA A 1 356 ? 83.793  -10.174 21.354  1.00 8.01  ? 358  ALA A CA  1 
ATOM   2678 C  C   . ALA A 1 356 ? 82.833  -9.075  20.917  1.00 8.32  ? 358  ALA A C   1 
ATOM   2679 O  O   . ALA A 1 356 ? 83.084  -7.887  21.141  1.00 8.31  ? 358  ALA A O   1 
ATOM   2680 C  CB  . ALA A 1 356 ? 84.444  -9.829  22.688  1.00 7.87  ? 358  ALA A CB  1 
ATOM   2681 N  N   . PHE A 1 357 ? 81.782  -9.475  20.207  1.00 8.87  ? 359  PHE A N   1 
ATOM   2682 C  CA  . PHE A 1 357 ? 80.912  -8.527  19.527  1.00 9.01  ? 359  PHE A CA  1 
ATOM   2683 C  C   . PHE A 1 357 ? 79.949  -7.900  20.524  1.00 9.11  ? 359  PHE A C   1 
ATOM   2684 O  O   . PHE A 1 357 ? 79.321  -8.604  21.313  1.00 9.46  ? 359  PHE A O   1 
ATOM   2685 C  CB  . PHE A 1 357 ? 80.139  -9.225  18.407  1.00 8.95  ? 359  PHE A CB  1 
ATOM   2686 C  CG  . PHE A 1 357 ? 79.174  -8.330  17.688  1.00 9.26  ? 359  PHE A CG  1 
ATOM   2687 C  CD1 . PHE A 1 357 ? 79.581  -7.586  16.593  1.00 9.59  ? 359  PHE A CD1 1 
ATOM   2688 C  CD2 . PHE A 1 357 ? 77.847  -8.253  18.091  1.00 9.73  ? 359  PHE A CD2 1 
ATOM   2689 C  CE1 . PHE A 1 357 ? 78.693  -6.763  15.927  1.00 9.71  ? 359  PHE A CE1 1 
ATOM   2690 C  CE2 . PHE A 1 357 ? 76.949  -7.447  17.416  1.00 9.94  ? 359  PHE A CE2 1 
ATOM   2691 C  CZ  . PHE A 1 357 ? 77.374  -6.696  16.336  1.00 9.58  ? 359  PHE A CZ  1 
ATOM   2692 N  N   . VAL A 1 358 ? 79.877  -6.572  20.520  1.00 9.04  ? 360  VAL A N   1 
ATOM   2693 C  CA  . VAL A 1 358 ? 78.951  -5.853  21.384  1.00 9.32  ? 360  VAL A CA  1 
ATOM   2694 C  C   . VAL A 1 358 ? 78.196  -4.821  20.549  1.00 9.55  ? 360  VAL A C   1 
ATOM   2695 O  O   . VAL A 1 358 ? 78.807  -3.972  19.901  1.00 9.45  ? 360  VAL A O   1 
ATOM   2696 C  CB  . VAL A 1 358 ? 79.695  -5.145  22.538  1.00 9.86  ? 360  VAL A CB  1 
ATOM   2697 C  CG1 . VAL A 1 358 ? 78.713  -4.426  23.453  1.00 9.79  ? 360  VAL A CG1 1 
ATOM   2698 C  CG2 . VAL A 1 358 ? 80.531  -6.142  23.329  1.00 9.25  ? 360  VAL A CG2 1 
ATOM   2699 N  N   . ALA A 1 359 ? 76.873  -4.940  20.515  1.00 8.98  ? 361  ALA A N   1 
ATOM   2700 C  CA  . ALA A 1 359 ? 76.040  -3.952  19.838  1.00 9.21  ? 361  ALA A CA  1 
ATOM   2701 C  C   . ALA A 1 359 ? 75.044  -3.360  20.818  1.00 9.24  ? 361  ALA A C   1 
ATOM   2702 O  O   . ALA A 1 359 ? 74.397  -4.094  21.570  1.00 9.04  ? 361  ALA A O   1 
ATOM   2703 C  CB  . ALA A 1 359 ? 75.310  -4.583  18.660  1.00 8.97  ? 361  ALA A CB  1 
ATOM   2704 N  N   . TYR A 1 360 ? 74.920  -2.035  20.798  1.00 8.77  ? 362  TYR A N   1 
ATOM   2705 C  CA  . TYR A 1 360 ? 73.922  -1.344  21.599  1.00 9.19  ? 362  TYR A CA  1 
ATOM   2706 C  C   . TYR A 1 360 ? 72.803  -0.786  20.724  1.00 9.23  ? 362  TYR A C   1 
ATOM   2707 O  O   . TYR A 1 360 ? 73.047  -0.300  19.613  1.00 8.80  ? 362  TYR A O   1 
ATOM   2708 C  CB  . TYR A 1 360 ? 74.563  -0.216  22.412  1.00 8.78  ? 362  TYR A CB  1 
ATOM   2709 C  CG  . TYR A 1 360 ? 75.505  -0.691  23.500  1.00 9.00  ? 362  TYR A CG  1 
ATOM   2710 C  CD1 . TYR A 1 360 ? 75.020  -1.141  24.723  1.00 9.12  ? 362  TYR A CD1 1 
ATOM   2711 C  CD2 . TYR A 1 360 ? 76.882  -0.689  23.301  1.00 8.90  ? 362  TYR A CD2 1 
ATOM   2712 C  CE1 . TYR A 1 360 ? 75.883  -1.558  25.723  1.00 9.44  ? 362  TYR A CE1 1 
ATOM   2713 C  CE2 . TYR A 1 360 ? 77.751  -1.101  24.295  1.00 9.02  ? 362  TYR A CE2 1 
ATOM   2714 C  CZ  . TYR A 1 360 ? 77.248  -1.527  25.506  1.00 9.56  ? 362  TYR A CZ  1 
ATOM   2715 O  OH  . TYR A 1 360 ? 78.118  -1.941  26.489  1.00 10.59 ? 362  TYR A OH  1 
ATOM   2716 N  N   . GLN A 1 361 ? 71.577  -0.886  21.230  1.00 9.26  ? 363  GLN A N   1 
ATOM   2717 C  CA  . GLN A 1 361 ? 70.387  -0.375  20.553  1.00 9.51  ? 363  GLN A CA  1 
ATOM   2718 C  C   . GLN A 1 361 ? 69.242  -0.289  21.559  1.00 9.25  ? 363  GLN A C   1 
ATOM   2719 O  O   . GLN A 1 361 ? 69.264  -0.961  22.592  1.00 9.20  ? 363  GLN A O   1 
ATOM   2720 C  CB  . GLN A 1 361 ? 69.979  -1.302  19.407  1.00 9.48  ? 363  GLN A CB  1 
ATOM   2721 C  CG  . GLN A 1 361 ? 69.698  -2.730  19.851  1.00 9.64  ? 363  GLN A CG  1 
ATOM   2722 C  CD  . GLN A 1 361 ? 70.915  -3.627  19.743  1.00 9.48  ? 363  GLN A CD  1 
ATOM   2723 O  OE1 . GLN A 1 361 ? 71.293  -4.040  18.650  1.00 10.02 ? 363  GLN A OE1 1 
ATOM   2724 N  NE2 . GLN A 1 361 ? 71.526  -3.947  20.881  1.00 9.20  ? 363  GLN A NE2 1 
ATOM   2725 N  N   . ALA A 1 362 ? 68.241  0.532   21.249  1.00 9.04  ? 364  ALA A N   1 
ATOM   2726 C  CA  . ALA A 1 362 ? 67.062  0.656   22.100  1.00 9.32  ? 364  ALA A CA  1 
ATOM   2727 C  C   . ALA A 1 362 ? 66.055  -0.455  21.835  1.00 9.61  ? 364  ALA A C   1 
ATOM   2728 O  O   . ALA A 1 362 ? 65.284  -0.828  22.722  1.00 9.57  ? 364  ALA A O   1 
ATOM   2729 C  CB  . ALA A 1 362 ? 66.410  2.017   21.916  1.00 9.34  ? 364  ALA A CB  1 
ATOM   2730 N  N   . GLN A 1 363 ? 66.036  -0.953  20.600  1.00 9.77  ? 365  GLN A N   1 
ATOM   2731 C  CA  . GLN A 1 363 ? 65.190  -2.093  20.248  1.00 9.92  ? 365  GLN A CA  1 
ATOM   2732 C  C   . GLN A 1 363 ? 66.003  -3.194  19.572  1.00 9.67  ? 365  GLN A C   1 
ATOM   2733 O  O   . GLN A 1 363 ? 66.485  -3.022  18.452  1.00 10.50 ? 365  GLN A O   1 
ATOM   2734 C  CB  . GLN A 1 363 ? 64.052  -1.655  19.326  1.00 10.60 ? 365  GLN A CB  1 
ATOM   2735 C  CG  . GLN A 1 363 ? 63.097  -0.646  19.945  1.00 10.98 ? 365  GLN A CG  1 
ATOM   2736 C  CD  . GLN A 1 363 ? 62.003  -0.215  18.985  1.00 12.26 ? 365  GLN A CD  1 
ATOM   2737 O  OE1 . GLN A 1 363 ? 61.972  0.933   18.533  1.00 12.77 ? 365  GLN A OE1 1 
ATOM   2738 N  NE2 . GLN A 1 363 ? 61.106  -1.141  18.656  1.00 11.33 ? 365  GLN A NE2 1 
ATOM   2739 N  N   . LEU A 1 364 ? 66.128  -4.334  20.240  1.00 9.28  ? 366  LEU A N   1 
ATOM   2740 C  CA  . LEU A 1 364 ? 66.819  -5.480  19.655  1.00 9.86  ? 366  LEU A CA  1 
ATOM   2741 C  C   . LEU A 1 364 ? 66.202  -5.915  18.328  1.00 10.55 ? 366  LEU A C   1 
ATOM   2742 O  O   . LEU A 1 364 ? 66.911  -6.332  17.413  1.00 10.62 ? 366  LEU A O   1 
ATOM   2743 C  CB  . LEU A 1 364 ? 66.864  -6.647  20.640  1.00 9.61  ? 366  LEU A CB  1 
ATOM   2744 C  CG  . LEU A 1 364 ? 67.816  -6.446  21.823  1.00 10.19 ? 366  LEU A CG  1 
ATOM   2745 C  CD1 . LEU A 1 364 ? 67.469  -7.382  22.976  1.00 10.33 ? 366  LEU A CD1 1 
ATOM   2746 C  CD2 . LEU A 1 364 ? 69.260  -6.639  21.389  1.00 9.49  ? 366  LEU A CD2 1 
ATOM   2747 N  N   . SER A 1 365 ? 64.890  -5.754  18.196  1.00 10.66 ? 367  SER A N   1 
ATOM   2748 C  CA  . SER A 1 365 ? 64.200  -6.213  16.993  1.00 11.25 ? 367  SER A CA  1 
ATOM   2749 C  C   . SER A 1 365 ? 64.532  -5.353  15.778  1.00 11.81 ? 367  SER A C   1 
ATOM   2750 O  O   . SER A 1 365 ? 64.324  -5.775  14.638  1.00 11.37 ? 367  SER A O   1 
ATOM   2751 C  CB  . SER A 1 365 ? 62.687  -6.241  17.212  1.00 11.07 ? 367  SER A CB  1 
ATOM   2752 O  OG  . SER A 1 365 ? 62.171  -4.927  17.277  1.00 11.31 ? 367  SER A OG  1 
ATOM   2753 N  N   . GLN A 1 366 ? 65.024  -4.140  16.030  1.00 12.04 ? 368  GLN A N   1 
ATOM   2754 C  CA  . GLN A 1 366 ? 65.355  -3.196  14.963  1.00 13.39 ? 368  GLN A CA  1 
ATOM   2755 C  C   . GLN A 1 366 ? 66.858  -3.144  14.699  1.00 11.99 ? 368  GLN A C   1 
ATOM   2756 O  O   . GLN A 1 366 ? 67.296  -2.680  13.647  1.00 11.14 ? 368  GLN A O   1 
ATOM   2757 C  CB  . GLN A 1 366 ? 64.850  -1.795  15.310  1.00 14.75 ? 368  GLN A CB  1 
ATOM   2758 C  CG  . GLN A 1 366 ? 63.350  -1.718  15.533  1.00 16.60 ? 368  GLN A CG  1 
ATOM   2759 C  CD  . GLN A 1 366 ? 62.558  -2.057  14.286  1.00 18.97 ? 368  GLN A CD  1 
ATOM   2760 O  OE1 . GLN A 1 366 ? 62.667  -1.378  13.265  1.00 21.30 ? 368  GLN A OE1 1 
ATOM   2761 N  NE2 . GLN A 1 366 ? 61.747  -3.107  14.365  1.00 21.44 ? 368  GLN A NE2 1 
ATOM   2762 N  N   . GLY A 1 367 ? 67.639  -3.618  15.664  1.00 11.00 ? 369  GLY A N   1 
ATOM   2763 C  CA  . GLY A 1 367 ? 69.090  -3.502  15.605  1.00 10.36 ? 369  GLY A CA  1 
ATOM   2764 C  C   . GLY A 1 367 ? 69.767  -4.799  15.216  1.00 10.44 ? 369  GLY A C   1 
ATOM   2765 O  O   . GLY A 1 367 ? 69.567  -5.312  14.111  1.00 10.58 ? 369  GLY A O   1 
ATOM   2766 N  N   . PHE A 1 368 ? 70.565  -5.339  16.133  1.00 9.97  ? 370  PHE A N   1 
ATOM   2767 C  CA  . PHE A 1 368 ? 71.384  -6.506  15.838  1.00 9.79  ? 370  PHE A CA  1 
ATOM   2768 C  C   . PHE A 1 368 ? 70.570  -7.644  15.222  1.00 10.20 ? 370  PHE A C   1 
ATOM   2769 O  O   . PHE A 1 368 ? 70.953  -8.206  14.194  1.00 9.64  ? 370  PHE A O   1 
ATOM   2770 C  CB  . PHE A 1 368 ? 72.098  -7.001  17.097  1.00 9.93  ? 370  PHE A CB  1 
ATOM   2771 C  CG  . PHE A 1 368 ? 72.515  -8.441  17.020  1.00 10.17 ? 370  PHE A CG  1 
ATOM   2772 C  CD1 . PHE A 1 368 ? 73.604  -8.820  16.254  1.00 10.51 ? 370  PHE A CD1 1 
ATOM   2773 C  CD2 . PHE A 1 368 ? 71.767  -9.427  17.645  1.00 10.62 ? 370  PHE A CD2 1 
ATOM   2774 C  CE1 . PHE A 1 368 ? 73.967  -10.149 16.145  1.00 10.57 ? 370  PHE A CE1 1 
ATOM   2775 C  CE2 . PHE A 1 368 ? 72.132  -10.757 17.552  1.00 10.91 ? 370  PHE A CE2 1 
ATOM   2776 C  CZ  . PHE A 1 368 ? 73.228  -11.121 16.791  1.00 10.87 ? 370  PHE A CZ  1 
ATOM   2777 N  N   . HIS A 1 369 ? 69.458  -7.988  15.862  1.00 10.00 ? 371  HIS A N   1 
ATOM   2778 C  CA  . HIS A 1 369 ? 68.637  -9.117  15.428  1.00 10.55 ? 371  HIS A CA  1 
ATOM   2779 C  C   . HIS A 1 369 ? 68.130  -8.893  14.006  1.00 10.78 ? 371  HIS A C   1 
ATOM   2780 O  O   . HIS A 1 369 ? 68.182  -9.794  13.164  1.00 10.89 ? 371  HIS A O   1 
ATOM   2781 C  CB  . HIS A 1 369 ? 67.471  -9.323  16.406  1.00 11.18 ? 371  HIS A CB  1 
ATOM   2782 C  CG  . HIS A 1 369 ? 66.409  -10.255 15.906  1.00 11.84 ? 371  HIS A CG  1 
ATOM   2783 N  ND1 . HIS A 1 369 ? 66.213  -11.512 16.437  1.00 11.90 ? 371  HIS A ND1 1 
ATOM   2784 C  CD2 . HIS A 1 369 ? 65.439  -10.086 14.976  1.00 12.77 ? 371  HIS A CD2 1 
ATOM   2785 C  CE1 . HIS A 1 369 ? 65.194  -12.092 15.828  1.00 12.42 ? 371  HIS A CE1 1 
ATOM   2786 N  NE2 . HIS A 1 369 ? 64.705  -11.247 14.938  1.00 13.97 ? 371  HIS A NE2 1 
ATOM   2787 N  N   . PHE A 1 370 ? 67.708  -7.663  13.725  1.00 10.63 ? 372  PHE A N   1 
ATOM   2788 C  CA  . PHE A 1 370 ? 67.216  -7.295  12.400  1.00 11.17 ? 372  PHE A CA  1 
ATOM   2789 C  C   . PHE A 1 370 ? 68.322  -7.381  11.352  1.00 10.66 ? 372  PHE A C   1 
ATOM   2790 O  O   . PHE A 1 370 ? 68.141  -7.984  10.292  1.00 10.68 ? 372  PHE A O   1 
ATOM   2791 C  CB  . PHE A 1 370 ? 66.633  -5.878  12.430  1.00 11.69 ? 372  PHE A CB  1 
ATOM   2792 C  CG  . PHE A 1 370 ? 65.847  -5.516  11.202  1.00 13.04 ? 372  PHE A CG  1 
ATOM   2793 C  CD1 . PHE A 1 370 ? 64.545  -5.966  11.040  1.00 13.34 ? 372  PHE A CD1 1 
ATOM   2794 C  CD2 . PHE A 1 370 ? 66.408  -4.730  10.209  1.00 12.87 ? 372  PHE A CD2 1 
ATOM   2795 C  CE1 . PHE A 1 370 ? 63.820  -5.641  9.907   1.00 13.85 ? 372  PHE A CE1 1 
ATOM   2796 C  CE2 . PHE A 1 370 ? 65.683  -4.390  9.082   1.00 12.93 ? 372  PHE A CE2 1 
ATOM   2797 C  CZ  . PHE A 1 370 ? 64.384  -4.840  8.933   1.00 13.44 ? 372  PHE A CZ  1 
ATOM   2798 N  N   . LEU A 1 371 ? 69.462  -6.760  11.645  1.00 10.25 ? 373  LEU A N   1 
ATOM   2799 C  CA  . LEU A 1 371 ? 70.602  -6.776  10.734  1.00 10.52 ? 373  LEU A CA  1 
ATOM   2800 C  C   . LEU A 1 371 ? 71.027  -8.202  10.389  1.00 10.09 ? 373  LEU A C   1 
ATOM   2801 O  O   . LEU A 1 371 ? 71.327  -8.510  9.233   1.00 10.34 ? 373  LEU A O   1 
ATOM   2802 C  CB  . LEU A 1 371 ? 71.784  -5.999  11.328  1.00 10.54 ? 373  LEU A CB  1 
ATOM   2803 C  CG  . LEU A 1 371 ? 71.912  -4.517  10.947  1.00 10.75 ? 373  LEU A CG  1 
ATOM   2804 C  CD1 . LEU A 1 371 ? 70.576  -3.804  11.085  1.00 10.79 ? 373  LEU A CD1 1 
ATOM   2805 C  CD2 . LEU A 1 371 ? 72.971  -3.825  11.800  1.00 10.44 ? 373  LEU A CD2 1 
ATOM   2806 N  N   . GLN A 1 372 ? 71.069  -9.068  11.395  1.00 10.19 ? 374  GLN A N   1 
ATOM   2807 C  CA  . GLN A 1 372 ? 71.499  -10.444 11.180  1.00 10.29 ? 374  GLN A CA  1 
ATOM   2808 C  C   . GLN A 1 372 ? 70.481  -11.231 10.354  1.00 10.85 ? 374  GLN A C   1 
ATOM   2809 O  O   . GLN A 1 372 ? 70.837  -11.874 9.367   1.00 10.90 ? 374  GLN A O   1 
ATOM   2810 C  CB  . GLN A 1 372 ? 71.764  -11.146 12.512  1.00 10.23 ? 374  GLN A CB  1 
ATOM   2811 C  CG  . GLN A 1 372 ? 72.211  -12.593 12.369  1.00 10.29 ? 374  GLN A CG  1 
ATOM   2812 C  CD  . GLN A 1 372 ? 73.648  -12.717 11.895  1.00 10.31 ? 374  GLN A CD  1 
ATOM   2813 O  OE1 . GLN A 1 372 ? 74.576  -12.234 12.548  1.00 10.30 ? 374  GLN A OE1 1 
ATOM   2814 N  NE2 . GLN A 1 372 ? 73.836  -13.343 10.742  1.00 10.61 ? 374  GLN A NE2 1 
ATOM   2815 N  N   . GLN A 1 373 ? 69.218  -11.184 10.763  1.00 10.68 ? 375  GLN A N   1 
ATOM   2816 C  CA  . GLN A 1 373 ? 68.202  -12.055 10.173  1.00 11.42 ? 375  GLN A CA  1 
ATOM   2817 C  C   . GLN A 1 373 ? 67.651  -11.513 8.857   1.00 11.36 ? 375  GLN A C   1 
ATOM   2818 O  O   . GLN A 1 373 ? 67.581  -12.231 7.858   1.00 11.68 ? 375  GLN A O   1 
ATOM   2819 C  CB  . GLN A 1 373 ? 67.056  -12.314 11.154  1.00 12.29 ? 375  GLN A CB  1 
ATOM   2820 C  CG  . GLN A 1 373 ? 65.899  -13.089 10.535  1.00 13.79 ? 375  GLN A CG  1 
ATOM   2821 C  CD  . GLN A 1 373 ? 64.737  -13.280 11.487  1.00 16.39 ? 375  GLN A CD  1 
ATOM   2822 O  OE1 . GLN A 1 373 ? 64.141  -14.358 11.552  1.00 18.96 ? 375  GLN A OE1 1 
ATOM   2823 N  NE2 . GLN A 1 373 ? 64.398  -12.231 12.220  1.00 15.91 ? 375  GLN A NE2 1 
ATOM   2824 N  N   . THR A 1 374 ? 67.246  -10.250 8.858   1.00 11.12 ? 376  THR A N   1 
ATOM   2825 C  CA  . THR A 1 374 ? 66.468  -9.722  7.746   1.00 11.26 ? 376  THR A CA  1 
ATOM   2826 C  C   . THR A 1 374 ? 67.358  -9.233  6.610   1.00 11.03 ? 376  THR A C   1 
ATOM   2827 O  O   . THR A 1 374 ? 66.949  -9.228  5.452   1.00 11.22 ? 376  THR A O   1 
ATOM   2828 C  CB  . THR A 1 374 ? 65.500  -8.612  8.200   1.00 11.71 ? 376  THR A CB  1 
ATOM   2829 O  OG1 . THR A 1 374 ? 64.625  -9.133  9.208   1.00 12.88 ? 376  THR A OG1 1 
ATOM   2830 C  CG2 . THR A 1 374 ? 64.661  -8.126  7.030   1.00 11.93 ? 376  THR A CG2 1 
ATOM   2831 N  N   . TRP A 1 375 ? 68.596  -8.871  6.937   1.00 10.75 ? 377  TRP A N   1 
ATOM   2832 C  CA  . TRP A 1 375 ? 69.505  -8.317  5.938   1.00 10.34 ? 377  TRP A CA  1 
ATOM   2833 C  C   . TRP A 1 375 ? 70.632  -9.280  5.576   1.00 9.82  ? 377  TRP A C   1 
ATOM   2834 O  O   . TRP A 1 375 ? 70.701  -9.764  4.446   1.00 9.65  ? 377  TRP A O   1 
ATOM   2835 C  CB  . TRP A 1 375 ? 70.072  -6.979  6.409   1.00 10.45 ? 377  TRP A CB  1 
ATOM   2836 C  CG  . TRP A 1 375 ? 69.059  -5.876  6.404   1.00 10.77 ? 377  TRP A CG  1 
ATOM   2837 C  CD1 . TRP A 1 375 ? 67.779  -5.938  5.931   1.00 11.33 ? 377  TRP A CD1 1 
ATOM   2838 C  CD2 . TRP A 1 375 ? 69.256  -4.529  6.853   1.00 10.81 ? 377  TRP A CD2 1 
ATOM   2839 N  NE1 . TRP A 1 375 ? 67.161  -4.716  6.078   1.00 11.07 ? 377  TRP A NE1 1 
ATOM   2840 C  CE2 . TRP A 1 375 ? 68.046  -3.836  6.644   1.00 10.93 ? 377  TRP A CE2 1 
ATOM   2841 C  CE3 . TRP A 1 375 ? 70.331  -3.849  7.432   1.00 10.36 ? 377  TRP A CE3 1 
ATOM   2842 C  CZ2 . TRP A 1 375 ? 67.884  -2.494  6.990   1.00 11.18 ? 377  TRP A CZ2 1 
ATOM   2843 C  CZ3 . TRP A 1 375 ? 70.171  -2.515  7.767   1.00 10.79 ? 377  TRP A CZ3 1 
ATOM   2844 C  CH2 . TRP A 1 375 ? 68.961  -1.849  7.533   1.00 10.73 ? 377  TRP A CH2 1 
ATOM   2845 N  N   . ALA A 1 376 ? 71.496  -9.574  6.544   1.00 9.38  ? 378  ALA A N   1 
ATOM   2846 C  CA  . ALA A 1 376 ? 72.668  -10.416 6.302   1.00 9.34  ? 378  ALA A CA  1 
ATOM   2847 C  C   . ALA A 1 376 ? 72.303  -11.824 5.827   1.00 9.39  ? 378  ALA A C   1 
ATOM   2848 O  O   . ALA A 1 376 ? 72.998  -12.402 4.992   1.00 9.13  ? 378  ALA A O   1 
ATOM   2849 C  CB  . ALA A 1 376 ? 73.539  -10.485 7.552   1.00 8.72  ? 378  ALA A CB  1 
ATOM   2850 N  N   . ASP A 1 377 ? 71.228  -12.379 6.379   1.00 10.08 ? 379  ASP A N   1 
ATOM   2851 C  CA  . ASP A 1 377 ? 70.868  -13.774 6.133   1.00 11.18 ? 379  ASP A CA  1 
ATOM   2852 C  C   . ASP A 1 377 ? 69.862  -13.903 4.995   1.00 11.14 ? 379  ASP A C   1 
ATOM   2853 O  O   . ASP A 1 377 ? 69.373  -14.998 4.702   1.00 11.36 ? 379  ASP A O   1 
ATOM   2854 C  CB  . ASP A 1 377 ? 70.286  -14.405 7.399   1.00 11.86 ? 379  ASP A CB  1 
ATOM   2855 C  CG  . ASP A 1 377 ? 71.340  -14.680 8.457   1.00 12.24 ? 379  ASP A CG  1 
ATOM   2856 O  OD1 . ASP A 1 377 ? 72.544  -14.502 8.169   1.00 13.34 ? 379  ASP A OD1 1 
ATOM   2857 O  OD2 . ASP A 1 377 ? 70.962  -15.073 9.582   1.00 13.10 ? 379  ASP A OD2 1 
ATOM   2858 N  N   . ASN A 1 378 ? 69.543  -12.776 4.369   1.00 10.76 ? 380  ASN A N   1 
ATOM   2859 C  CA  . ASN A 1 378 ? 68.496  -12.721 3.359   1.00 10.82 ? 380  ASN A CA  1 
ATOM   2860 C  C   . ASN A 1 378 ? 69.096  -12.571 1.963   1.00 11.29 ? 380  ASN A C   1 
ATOM   2861 O  O   . ASN A 1 378 ? 69.686  -11.539 1.641   1.00 11.07 ? 380  ASN A O   1 
ATOM   2862 C  CB  . ASN A 1 378 ? 67.559  -11.550 3.672   1.00 10.73 ? 380  ASN A CB  1 
ATOM   2863 C  CG  . ASN A 1 378 ? 66.455  -11.382 2.649   1.00 11.27 ? 380  ASN A CG  1 
ATOM   2864 O  OD1 . ASN A 1 378 ? 66.465  -12.003 1.586   1.00 10.79 ? 380  ASN A OD1 1 
ATOM   2865 N  ND2 . ASN A 1 378 ? 65.509  -10.500 2.955   1.00 12.30 ? 380  ASN A ND2 1 
ATOM   2866 N  N   . ALA A 1 379 ? 68.966  -13.616 1.149   1.00 11.00 ? 381  ALA A N   1 
ATOM   2867 C  CA  . ALA A 1 379 ? 69.628  -13.674 -0.152  1.00 11.82 ? 381  ALA A CA  1 
ATOM   2868 C  C   . ALA A 1 379 ? 69.036  -12.698 -1.163  1.00 11.77 ? 381  ALA A C   1 
ATOM   2869 O  O   . ALA A 1 379 ? 69.598  -12.496 -2.237  1.00 11.77 ? 381  ALA A O   1 
ATOM   2870 C  CB  . ALA A 1 379 ? 69.597  -15.091 -0.707  1.00 11.60 ? 381  ALA A CB  1 
ATOM   2871 N  N   . ASN A 1 380 ? 67.899  -12.099 -0.824  1.00 13.58 ? 382  ASN A N   1 
ATOM   2872 C  CA  . ASN A 1 380 ? 67.320  -11.055 -1.663  1.00 14.63 ? 382  ASN A CA  1 
ATOM   2873 C  C   . ASN A 1 380 ? 67.344  -9.684  -0.999  1.00 14.04 ? 382  ASN A C   1 
ATOM   2874 O  O   . ASN A 1 380 ? 66.487  -8.843  -1.265  1.00 12.91 ? 382  ASN A O   1 
ATOM   2875 C  CB  . ASN A 1 380 ? 65.891  -11.416 -2.073  1.00 17.36 ? 382  ASN A CB  1 
ATOM   2876 C  CG  . ASN A 1 380 ? 65.848  -12.393 -3.232  1.00 20.95 ? 382  ASN A CG  1 
ATOM   2877 O  OD1 . ASN A 1 380 ? 65.312  -13.495 -3.110  1.00 24.51 ? 382  ASN A OD1 1 
ATOM   2878 N  ND2 . ASN A 1 380 ? 66.428  -11.999 -4.363  1.00 21.22 ? 382  ASN A ND2 1 
ATOM   2879 N  N   . PHE A 1 381 ? 68.319  -9.469  -0.123  1.00 12.67 ? 383  PHE A N   1 
ATOM   2880 C  CA  . PHE A 1 381 ? 68.591  -8.134  0.388   1.00 12.21 ? 383  PHE A CA  1 
ATOM   2881 C  C   . PHE A 1 381 ? 70.009  -7.705  0.026   1.00 12.15 ? 383  PHE A C   1 
ATOM   2882 O  O   . PHE A 1 381 ? 70.947  -8.487  0.171   1.00 11.50 ? 383  PHE A O   1 
ATOM   2883 C  CB  . PHE A 1 381 ? 68.404  -8.083  1.907   1.00 12.16 ? 383  PHE A CB  1 
ATOM   2884 C  CG  . PHE A 1 381 ? 68.486  -6.695  2.465   1.00 12.18 ? 383  PHE A CG  1 
ATOM   2885 C  CD1 . PHE A 1 381 ? 67.361  -5.884  2.494   1.00 12.45 ? 383  PHE A CD1 1 
ATOM   2886 C  CD2 . PHE A 1 381 ? 69.710  -6.150  2.813   1.00 12.09 ? 383  PHE A CD2 1 
ATOM   2887 C  CE1 . PHE A 1 381 ? 67.444  -4.574  2.927   1.00 12.21 ? 383  PHE A CE1 1 
ATOM   2888 C  CE2 . PHE A 1 381 ? 69.803  -4.837  3.240   1.00 12.66 ? 383  PHE A CE2 1 
ATOM   2889 C  CZ  . PHE A 1 381 ? 68.669  -4.049  3.295   1.00 11.93 ? 383  PHE A CZ  1 
ATOM   2890 N  N   . PRO A 1 382 ? 70.174  -6.467  -0.437  1.00 11.99 ? 384  PRO A N   1 
ATOM   2891 C  CA  . PRO A 1 382 ? 69.081  -5.504  -0.572  1.00 12.05 ? 384  PRO A CA  1 
ATOM   2892 C  C   . PRO A 1 382 ? 68.123  -5.836  -1.717  1.00 11.91 ? 384  PRO A C   1 
ATOM   2893 O  O   . PRO A 1 382 ? 68.486  -6.574  -2.629  1.00 11.89 ? 384  PRO A O   1 
ATOM   2894 C  CB  . PRO A 1 382 ? 69.817  -4.193  -0.886  1.00 12.11 ? 384  PRO A CB  1 
ATOM   2895 C  CG  . PRO A 1 382 ? 71.098  -4.632  -1.520  1.00 12.08 ? 384  PRO A CG  1 
ATOM   2896 C  CD  . PRO A 1 382 ? 71.481  -5.863  -0.752  1.00 11.82 ? 384  PRO A CD  1 
ATOM   2897 N  N   . PRO A 1 383 ? 66.912  -5.257  -1.685  1.00 13.08 ? 385  PRO A N   1 
ATOM   2898 C  CA  . PRO A 1 383 ? 65.886  -5.532  -2.688  1.00 13.37 ? 385  PRO A CA  1 
ATOM   2899 C  C   . PRO A 1 383 ? 66.114  -4.757  -3.986  1.00 14.45 ? 385  PRO A C   1 
ATOM   2900 O  O   . PRO A 1 383 ? 66.878  -3.793  -4.006  1.00 14.29 ? 385  PRO A O   1 
ATOM   2901 C  CB  . PRO A 1 383 ? 64.603  -5.059  -2.006  1.00 14.30 ? 385  PRO A CB  1 
ATOM   2902 C  CG  . PRO A 1 383 ? 65.049  -3.970  -1.090  1.00 13.70 ? 385  PRO A CG  1 
ATOM   2903 C  CD  . PRO A 1 383 ? 66.432  -4.345  -0.630  1.00 13.41 ? 385  PRO A CD  1 
ATOM   2904 N  N   . GLY A 1 384 ? 65.472  -5.198  -5.064  1.00 14.96 ? 386  GLY A N   1 
ATOM   2905 C  CA  . GLY A 1 384 ? 65.418  -4.425  -6.302  1.00 15.04 ? 386  GLY A CA  1 
ATOM   2906 C  C   . GLY A 1 384 ? 66.720  -4.383  -7.080  1.00 15.68 ? 386  GLY A C   1 
ATOM   2907 O  O   . GLY A 1 384 ? 66.932  -3.484  -7.896  1.00 16.35 ? 386  GLY A O   1 
ATOM   2908 N  N   . LYS A 1 385 ? 67.584  -5.370  -6.859  1.00 15.06 ? 387  LYS A N   1 
ATOM   2909 C  CA  . LYS A 1 385 ? 68.851  -5.442  -7.586  1.00 14.49 ? 387  LYS A CA  1 
ATOM   2910 C  C   . LYS A 1 385 ? 68.755  -6.351  -8.812  1.00 14.94 ? 387  LYS A C   1 
ATOM   2911 O  O   . LYS A 1 385 ? 67.831  -7.156  -8.933  1.00 15.33 ? 387  LYS A O   1 
ATOM   2912 C  CB  . LYS A 1 385 ? 69.983  -5.914  -6.666  1.00 14.35 ? 387  LYS A CB  1 
ATOM   2913 C  CG  . LYS A 1 385 ? 70.242  -5.010  -5.469  1.00 13.93 ? 387  LYS A CG  1 
ATOM   2914 C  CD  . LYS A 1 385 ? 70.497  -3.574  -5.896  1.00 14.01 ? 387  LYS A CD  1 
ATOM   2915 C  CE  . LYS A 1 385 ? 71.129  -2.772  -4.768  1.00 13.63 ? 387  LYS A CE  1 
ATOM   2916 N  NZ  . LYS A 1 385 ? 71.296  -1.334  -5.121  1.00 13.57 ? 387  LYS A NZ  1 
ATOM   2917 N  N   . THR A 1 386 ? 69.709  -6.199  -9.725  1.00 14.50 ? 388  THR A N   1 
ATOM   2918 C  CA  . THR A 1 386 ? 69.877  -7.130  -10.838 1.00 15.73 ? 388  THR A CA  1 
ATOM   2919 C  C   . THR A 1 386 ? 71.332  -7.592  -10.884 1.00 14.90 ? 388  THR A C   1 
ATOM   2920 O  O   . THR A 1 386 ? 72.232  -6.767  -10.995 1.00 16.22 ? 388  THR A O   1 
ATOM   2921 C  CB  . THR A 1 386 ? 69.548  -6.447  -12.180 1.00 15.58 ? 388  THR A CB  1 
ATOM   2922 O  OG1 . THR A 1 386 ? 68.225  -5.897  -12.130 1.00 17.24 ? 388  THR A OG1 1 
ATOM   2923 C  CG2 . THR A 1 386 ? 69.642  -7.442  -13.329 1.00 16.69 ? 388  THR A CG2 1 
ATOM   2924 N  N   . PRO A 1 387 ? 71.571  -8.896  -10.772 1.00 15.28 ? 389  PRO A N   1 
ATOM   2925 C  CA  . PRO A 1 387 ? 70.524  -9.885  -10.540 1.00 14.81 ? 389  PRO A CA  1 
ATOM   2926 C  C   . PRO A 1 387 ? 69.892  -9.743  -9.158  1.00 15.15 ? 389  PRO A C   1 
ATOM   2927 O  O   . PRO A 1 387 ? 70.514  -9.200  -8.243  1.00 14.71 ? 389  PRO A O   1 
ATOM   2928 C  CB  . PRO A 1 387 ? 71.281  -11.215 -10.627 1.00 15.18 ? 389  PRO A CB  1 
ATOM   2929 C  CG  . PRO A 1 387 ? 72.435  -10.929 -11.529 1.00 15.70 ? 389  PRO A CG  1 
ATOM   2930 C  CD  . PRO A 1 387 ? 72.825  -9.506  -11.251 1.00 14.80 ? 389  PRO A CD  1 
ATOM   2931 N  N   . ALA A 1 388 ? 68.679  -10.269 -9.009  1.00 14.46 ? 390  ALA A N   1 
ATOM   2932 C  CA  . ALA A 1 388 ? 67.904  -10.106 -7.786  1.00 14.80 ? 390  ALA A CA  1 
ATOM   2933 C  C   . ALA A 1 388 ? 68.525  -10.833 -6.600  1.00 14.29 ? 390  ALA A C   1 
ATOM   2934 O  O   . ALA A 1 388 ? 68.403  -10.384 -5.460  1.00 13.83 ? 390  ALA A O   1 
ATOM   2935 C  CB  . ALA A 1 388 ? 66.471  -10.574 -8.001  1.00 15.40 ? 390  ALA A CB  1 
ATOM   2936 N  N   . THR A 1 389 ? 69.160  -11.972 -6.869  1.00 14.26 ? 391  THR A N   1 
ATOM   2937 C  CA  . THR A 1 389 ? 69.781  -12.769 -5.815  1.00 14.08 ? 391  THR A CA  1 
ATOM   2938 C  C   . THR A 1 389 ? 71.137  -12.203 -5.411  1.00 13.88 ? 391  THR A C   1 
ATOM   2939 O  O   . THR A 1 389 ? 72.149  -12.447 -6.074  1.00 13.73 ? 391  THR A O   1 
ATOM   2940 C  CB  . THR A 1 389 ? 69.952  -14.240 -6.236  1.00 15.38 ? 391  THR A CB  1 
ATOM   2941 O  OG1 . THR A 1 389 ? 68.729  -14.723 -6.808  1.00 16.37 ? 391  THR A OG1 1 
ATOM   2942 C  CG2 . THR A 1 389 ? 70.317  -15.103 -5.030  1.00 15.17 ? 391  THR A CG2 1 
ATOM   2943 N  N   . VAL A 1 390 ? 71.151  -11.464 -4.306  1.00 11.98 ? 392  VAL A N   1 
ATOM   2944 C  CA  . VAL A 1 390 ? 72.376  -10.886 -3.778  1.00 11.57 ? 392  VAL A CA  1 
ATOM   2945 C  C   . VAL A 1 390 ? 73.228  -11.965 -3.109  1.00 11.07 ? 392  VAL A C   1 
ATOM   2946 O  O   . VAL A 1 390 ? 74.456  -11.953 -3.202  1.00 11.37 ? 392  VAL A O   1 
ATOM   2947 C  CB  . VAL A 1 390 ? 72.060  -9.774  -2.762  1.00 11.77 ? 392  VAL A CB  1 
ATOM   2948 C  CG1 . VAL A 1 390 ? 73.305  -9.394  -1.973  1.00 11.62 ? 392  VAL A CG1 1 
ATOM   2949 C  CG2 . VAL A 1 390 ? 71.469  -8.564  -3.475  1.00 12.30 ? 392  VAL A CG2 1 
ATOM   2950 N  N   . GLY A 1 391 ? 72.562  -12.929 -2.482  1.00 10.44 ? 393  GLY A N   1 
ATOM   2951 C  CA  . GLY A 1 391 ? 73.246  -13.924 -1.672  1.00 10.20 ? 393  GLY A CA  1 
ATOM   2952 C  C   . GLY A 1 391 ? 73.440  -13.405 -0.262  1.00 9.42  ? 393  GLY A C   1 
ATOM   2953 O  O   . GLY A 1 391 ? 72.930  -12.337 0.089   1.00 9.31  ? 393  GLY A O   1 
ATOM   2954 N  N   . LEU A 1 392 ? 74.166  -14.164 0.552   1.00 9.16  ? 394  LEU A N   1 
ATOM   2955 C  CA  . LEU A 1 392 ? 74.306  -13.842 1.967   1.00 9.63  ? 394  LEU A CA  1 
ATOM   2956 C  C   . LEU A 1 392 ? 75.529  -12.964 2.233   1.00 9.79  ? 394  LEU A C   1 
ATOM   2957 O  O   . LEU A 1 392 ? 76.438  -12.890 1.409   1.00 10.72 ? 394  LEU A O   1 
ATOM   2958 C  CB  . LEU A 1 392 ? 74.388  -15.123 2.800   1.00 9.70  ? 394  LEU A CB  1 
ATOM   2959 C  CG  . LEU A 1 392 ? 73.242  -16.121 2.615   1.00 10.03 ? 394  LEU A CG  1 
ATOM   2960 C  CD1 . LEU A 1 392 ? 73.305  -17.201 3.684   1.00 10.00 ? 394  LEU A CD1 1 
ATOM   2961 C  CD2 . LEU A 1 392 ? 71.891  -15.423 2.636   1.00 10.00 ? 394  LEU A CD2 1 
ATOM   2962 N  N   . ASP A 1 393 ? 75.533  -12.294 3.382   1.00 9.77  ? 395  ASP A N   1 
ATOM   2963 C  CA  . ASP A 1 393 ? 76.730  -11.639 3.912   1.00 10.07 ? 395  ASP A CA  1 
ATOM   2964 C  C   . ASP A 1 393 ? 77.855  -12.662 4.073   1.00 9.68  ? 395  ASP A C   1 
ATOM   2965 O  O   . ASP A 1 393 ? 77.721  -13.617 4.837   1.00 10.52 ? 395  ASP A O   1 
ATOM   2966 C  CB  . ASP A 1 393 ? 76.402  -10.998 5.269   1.00 10.13 ? 395  ASP A CB  1 
ATOM   2967 C  CG  . ASP A 1 393 ? 77.515  -10.098 5.790   1.00 10.63 ? 395  ASP A CG  1 
ATOM   2968 O  OD1 . ASP A 1 393 ? 78.687  -10.526 5.790   1.00 10.36 ? 395  ASP A OD1 1 
ATOM   2969 O  OD2 . ASP A 1 393 ? 77.199  -8.990  6.277   1.00 10.59 ? 395  ASP A OD2 1 
ATOM   2970 N  N   . PRO A 1 394 ? 78.969  -12.466 3.351   1.00 9.16  ? 396  PRO A N   1 
ATOM   2971 C  CA  . PRO A 1 394 ? 80.056  -13.444 3.346   1.00 8.99  ? 396  PRO A CA  1 
ATOM   2972 C  C   . PRO A 1 394 ? 80.790  -13.500 4.684   1.00 9.07  ? 396  PRO A C   1 
ATOM   2973 O  O   . PRO A 1 394 ? 81.442  -14.499 4.985   1.00 9.56  ? 396  PRO A O   1 
ATOM   2974 C  CB  . PRO A 1 394 ? 80.984  -12.930 2.240   1.00 9.09  ? 396  PRO A CB  1 
ATOM   2975 C  CG  . PRO A 1 394 ? 80.723  -11.461 2.192   1.00 9.17  ? 396  PRO A CG  1 
ATOM   2976 C  CD  . PRO A 1 394 ? 79.256  -11.314 2.477   1.00 9.03  ? 396  PRO A CD  1 
ATOM   2977 N  N   . ILE A 1 395 ? 80.644  -12.456 5.495   1.00 8.48  ? 397  ILE A N   1 
ATOM   2978 C  CA  . ILE A 1 395 ? 81.309  -12.399 6.796   1.00 8.79  ? 397  ILE A CA  1 
ATOM   2979 C  C   . ILE A 1 395 ? 80.454  -13.003 7.909   1.00 8.95  ? 397  ILE A C   1 
ATOM   2980 O  O   . ILE A 1 395 ? 80.921  -13.866 8.650   1.00 10.07 ? 397  ILE A O   1 
ATOM   2981 C  CB  . ILE A 1 395 ? 81.731  -10.957 7.163   1.00 8.49  ? 397  ILE A CB  1 
ATOM   2982 C  CG1 . ILE A 1 395 ? 82.653  -10.376 6.082   1.00 7.95  ? 397  ILE A CG1 1 
ATOM   2983 C  CG2 . ILE A 1 395 ? 82.400  -10.911 8.530   1.00 8.46  ? 397  ILE A CG2 1 
ATOM   2984 C  CD1 . ILE A 1 395 ? 83.933  -11.159 5.872   1.00 8.33  ? 397  ILE A CD1 1 
ATOM   2985 N  N   . ILE A 1 396 ? 79.201  -12.568 8.021   1.00 9.08  ? 398  ILE A N   1 
ATOM   2986 C  CA  . ILE A 1 396 ? 78.352  -13.021 9.126   1.00 9.18  ? 398  ILE A CA  1 
ATOM   2987 C  C   . ILE A 1 396 ? 77.110  -13.796 8.692   1.00 9.53  ? 398  ILE A C   1 
ATOM   2988 O  O   . ILE A 1 396 ? 76.370  -14.297 9.531   1.00 9.36  ? 398  ILE A O   1 
ATOM   2989 C  CB  . ILE A 1 396 ? 77.921  -11.862 10.039  1.00 9.45  ? 398  ILE A CB  1 
ATOM   2990 C  CG1 . ILE A 1 396 ? 77.098  -10.833 9.255   1.00 9.06  ? 398  ILE A CG1 1 
ATOM   2991 C  CG2 . ILE A 1 396 ? 79.133  -11.226 10.705  1.00 9.10  ? 398  ILE A CG2 1 
ATOM   2992 C  CD1 . ILE A 1 396 ? 76.244  -9.948  10.138  1.00 9.74  ? 398  ILE A CD1 1 
ATOM   2993 N  N   . GLY A 1 397 ? 76.887  -13.895 7.385   1.00 9.62  ? 399  GLY A N   1 
ATOM   2994 C  CA  . GLY A 1 397 ? 75.715  -14.595 6.867   1.00 10.38 ? 399  GLY A CA  1 
ATOM   2995 C  C   . GLY A 1 397 ? 75.681  -16.058 7.268   1.00 10.41 ? 399  GLY A C   1 
ATOM   2996 O  O   . GLY A 1 397 ? 76.694  -16.750 7.198   1.00 10.32 ? 399  GLY A O   1 
ATOM   2997 N  N   . GLN A 1 398 ? 74.515  -16.528 7.704   1.00 11.44 ? 400  GLN A N   1 
ATOM   2998 C  CA  . GLN A 1 398 ? 74.383  -17.897 8.198   1.00 12.22 ? 400  GLN A CA  1 
ATOM   2999 C  C   . GLN A 1 398 ? 73.254  -18.653 7.499   1.00 13.60 ? 400  GLN A C   1 
ATOM   3000 O  O   . GLN A 1 398 ? 72.220  -18.076 7.159   1.00 12.41 ? 400  GLN A O   1 
ATOM   3001 C  CB  . GLN A 1 398 ? 74.184  -17.913 9.718   1.00 13.31 ? 400  GLN A CB  1 
ATOM   3002 C  CG  . GLN A 1 398 ? 75.378  -17.380 10.498  1.00 12.99 ? 400  GLN A CG  1 
ATOM   3003 C  CD  . GLN A 1 398 ? 75.266  -17.599 11.997  1.00 14.19 ? 400  GLN A CD  1 
ATOM   3004 O  OE1 . GLN A 1 398 ? 76.267  -17.835 12.674  1.00 15.67 ? 400  GLN A OE1 1 
ATOM   3005 N  NE2 . GLN A 1 398 ? 74.054  -17.487 12.528  1.00 13.91 ? 400  GLN A NE2 1 
ATOM   3006 N  N   . ASN A 1 399 ? 73.483  -19.938 7.250   1.00 13.73 ? 401  ASN A N   1 
ATOM   3007 C  CA  . ASN A 1 399 ? 72.437  -20.823 6.744   1.00 15.42 ? 401  ASN A CA  1 
ATOM   3008 C  C   . ASN A 1 399 ? 72.579  -22.229 7.319   1.00 15.93 ? 401  ASN A C   1 
ATOM   3009 O  O   . ASN A 1 399 ? 72.864  -23.183 6.593   1.00 16.20 ? 401  ASN A O   1 
ATOM   3010 C  CB  . ASN A 1 399 ? 72.455  -20.870 5.213   1.00 16.48 ? 401  ASN A CB  1 
ATOM   3011 C  CG  . ASN A 1 399 ? 71.228  -21.557 4.637   1.00 18.25 ? 401  ASN A CG  1 
ATOM   3012 O  OD1 . ASN A 1 399 ? 70.128  -21.458 5.187   1.00 20.53 ? 401  ASN A OD1 1 
ATOM   3013 N  ND2 . ASN A 1 399 ? 71.414  -22.268 3.534   1.00 17.38 ? 401  ASN A ND2 1 
ATOM   3014 N  N   . ASN A 1 400 ? 72.447  -22.328 8.639   1.00 16.22 ? 402  ASN A N   1 
ATOM   3015 C  CA  . ASN A 1 400 ? 72.460  -23.609 9.337   1.00 18.33 ? 402  ASN A CA  1 
ATOM   3016 C  C   . ASN A 1 400 ? 73.663  -24.485 9.011   1.00 17.66 ? 402  ASN A C   1 
ATOM   3017 O  O   . ASN A 1 400 ? 73.513  -25.661 8.689   1.00 18.57 ? 402  ASN A O   1 
ATOM   3018 C  CB  . ASN A 1 400 ? 71.162  -24.373 9.081   1.00 19.43 ? 402  ASN A CB  1 
ATOM   3019 C  CG  . ASN A 1 400 ? 69.954  -23.663 9.651   1.00 20.73 ? 402  ASN A CG  1 
ATOM   3020 O  OD1 . ASN A 1 400 ? 69.860  -23.448 10.861  1.00 23.18 ? 402  ASN A OD1 1 
ATOM   3021 N  ND2 . ASN A 1 400 ? 69.035  -23.266 8.780   1.00 23.67 ? 402  ASN A ND2 1 
ATOM   3022 N  N   . GLY A 1 401 ? 74.855  -23.913 9.132   1.00 17.81 ? 403  GLY A N   1 
ATOM   3023 C  CA  . GLY A 1 401 ? 76.091  -24.675 9.000   1.00 20.92 ? 403  GLY A CA  1 
ATOM   3024 C  C   . GLY A 1 401 ? 76.510  -24.897 7.561   1.00 21.86 ? 403  GLY A C   1 
ATOM   3025 O  O   . GLY A 1 401 ? 77.660  -25.247 7.289   1.00 25.28 ? 403  GLY A O   1 
ATOM   3026 N  N   . GLN A 1 402 ? 75.577  -24.689 6.636   1.00 20.53 ? 404  GLN A N   1 
ATOM   3027 C  CA  . GLN A 1 402 ? 75.844  -24.883 5.214   1.00 20.65 ? 404  GLN A CA  1 
ATOM   3028 C  C   . GLN A 1 402 ? 76.741  -23.775 4.667   1.00 18.39 ? 404  GLN A C   1 
ATOM   3029 O  O   . GLN A 1 402 ? 76.744  -22.660 5.186   1.00 16.37 ? 404  GLN A O   1 
ATOM   3030 C  CB  . GLN A 1 402 ? 74.530  -24.924 4.430   1.00 22.35 ? 404  GLN A CB  1 
ATOM   3031 C  CG  . GLN A 1 402 ? 73.652  -26.122 4.750   1.00 25.11 ? 404  GLN A CG  1 
ATOM   3032 C  CD  . GLN A 1 402 ? 74.272  -27.433 4.307   1.00 28.51 ? 404  GLN A CD  1 
ATOM   3033 O  OE1 . GLN A 1 402 ? 74.313  -27.743 3.116   1.00 33.16 ? 404  GLN A OE1 1 
ATOM   3034 N  NE2 . GLN A 1 402 ? 74.764  -28.208 5.266   1.00 29.94 ? 404  GLN A NE2 1 
ATOM   3035 N  N   . PRO A 1 403 ? 77.513  -24.081 3.614   1.00 17.27 ? 405  PRO A N   1 
ATOM   3036 C  CA  . PRO A 1 403 ? 78.250  -23.016 2.936   1.00 16.23 ? 405  PRO A CA  1 
ATOM   3037 C  C   . PRO A 1 403 ? 77.286  -21.930 2.465   1.00 14.53 ? 405  PRO A C   1 
ATOM   3038 O  O   . PRO A 1 403 ? 76.148  -22.233 2.115   1.00 14.39 ? 405  PRO A O   1 
ATOM   3039 C  CB  . PRO A 1 403 ? 78.877  -23.728 1.727   1.00 17.71 ? 405  PRO A CB  1 
ATOM   3040 C  CG  . PRO A 1 403 ? 78.800  -25.190 2.032   1.00 18.43 ? 405  PRO A CG  1 
ATOM   3041 C  CD  . PRO A 1 403 ? 77.578  -25.359 2.886   1.00 18.71 ? 405  PRO A CD  1 
ATOM   3042 N  N   . ARG A 1 404 ? 77.723  -20.674 2.498   1.00 12.74 ? 406  ARG A N   1 
ATOM   3043 C  CA  . ARG A 1 404 ? 76.877  -19.562 2.071   1.00 11.61 ? 406  ARG A CA  1 
ATOM   3044 C  C   . ARG A 1 404 ? 77.066  -19.289 0.583   1.00 11.53 ? 406  ARG A C   1 
ATOM   3045 O  O   . ARG A 1 404 ? 78.194  -19.254 0.089   1.00 11.09 ? 406  ARG A O   1 
ATOM   3046 C  CB  . ARG A 1 404 ? 77.197  -18.297 2.876   1.00 11.40 ? 406  ARG A CB  1 
ATOM   3047 C  CG  . ARG A 1 404 ? 76.849  -18.384 4.356   1.00 11.17 ? 406  ARG A CG  1 
ATOM   3048 C  CD  . ARG A 1 404 ? 77.918  -19.110 5.164   1.00 11.44 ? 406  ARG A CD  1 
ATOM   3049 N  NE  . ARG A 1 404 ? 79.282  -18.702 4.820   1.00 11.45 ? 406  ARG A NE  1 
ATOM   3050 C  CZ  . ARG A 1 404 ? 79.790  -17.493 5.039   1.00 11.87 ? 406  ARG A CZ  1 
ATOM   3051 N  NH1 . ARG A 1 404 ? 79.045  -16.538 5.587   1.00 11.28 ? 406  ARG A NH1 1 
ATOM   3052 N  NH2 . ARG A 1 404 ? 81.047  -17.234 4.700   1.00 11.61 ? 406  ARG A NH2 1 
ATOM   3053 N  N   . VAL A 1 405 ? 75.959  -19.134 -0.134  1.00 10.79 ? 407  VAL A N   1 
ATOM   3054 C  CA  . VAL A 1 405 ? 76.021  -18.719 -1.530  1.00 10.63 ? 407  VAL A CA  1 
ATOM   3055 C  C   . VAL A 1 405 ? 76.026  -17.200 -1.611  1.00 10.23 ? 407  VAL A C   1 
ATOM   3056 O  O   . VAL A 1 405 ? 75.079  -16.543 -1.181  1.00 10.40 ? 407  VAL A O   1 
ATOM   3057 C  CB  . VAL A 1 405 ? 74.842  -19.281 -2.346  1.00 11.51 ? 407  VAL A CB  1 
ATOM   3058 C  CG1 . VAL A 1 405 ? 74.900  -18.776 -3.780  1.00 12.32 ? 407  VAL A CG1 1 
ATOM   3059 C  CG2 . VAL A 1 405 ? 74.852  -20.804 -2.309  1.00 11.94 ? 407  VAL A CG2 1 
ATOM   3060 N  N   . VAL A 1 406 ? 77.120  -16.647 -2.119  1.00 9.99  ? 408  VAL A N   1 
ATOM   3061 C  CA  . VAL A 1 406 ? 77.301  -15.202 -2.163  1.00 9.92  ? 408  VAL A CA  1 
ATOM   3062 C  C   . VAL A 1 406 ? 77.603  -14.749 -3.587  1.00 10.24 ? 408  VAL A C   1 
ATOM   3063 O  O   . VAL A 1 406 ? 78.548  -15.228 -4.219  1.00 9.87  ? 408  VAL A O   1 
ATOM   3064 C  CB  . VAL A 1 406 ? 78.436  -14.751 -1.222  1.00 9.81  ? 408  VAL A CB  1 
ATOM   3065 C  CG1 . VAL A 1 406 ? 78.484  -13.230 -1.125  1.00 9.53  ? 408  VAL A CG1 1 
ATOM   3066 C  CG2 . VAL A 1 406 ? 78.262  -15.372 0.157   1.00 9.44  ? 408  VAL A CG2 1 
ATOM   3067 N  N   . ASN A 1 407 ? 76.779  -13.844 -4.104  1.00 10.65 ? 409  ASN A N   1 
ATOM   3068 C  CA  . ASN A 1 407 ? 76.948  -13.366 -5.471  1.00 10.97 ? 409  ASN A CA  1 
ATOM   3069 C  C   . ASN A 1 407 ? 77.560  -11.970 -5.523  1.00 10.67 ? 409  ASN A C   1 
ATOM   3070 O  O   . ASN A 1 407 ? 77.572  -11.248 -4.526  1.00 9.77  ? 409  ASN A O   1 
ATOM   3071 C  CB  . ASN A 1 407 ? 75.610  -13.383 -6.211  1.00 11.88 ? 409  ASN A CB  1 
ATOM   3072 C  CG  . ASN A 1 407 ? 75.003  -14.771 -6.284  1.00 13.27 ? 409  ASN A CG  1 
ATOM   3073 O  OD1 . ASN A 1 407 ? 73.786  -14.925 -6.406  1.00 15.94 ? 409  ASN A OD1 1 
ATOM   3074 N  ND2 . ASN A 1 407 ? 75.849  -15.789 -6.226  1.00 12.59 ? 409  ASN A ND2 1 
ATOM   3075 N  N   . GLY A 1 408 ? 78.098  -11.608 -6.682  1.00 10.15 ? 410  GLY A N   1 
ATOM   3076 C  CA  . GLY A 1 408 ? 78.528  -10.233 -6.915  1.00 10.30 ? 410  GLY A CA  1 
ATOM   3077 C  C   . GLY A 1 408 ? 79.973  -9.944  -6.551  1.00 10.68 ? 410  GLY A C   1 
ATOM   3078 O  O   . GLY A 1 408 ? 80.476  -8.857  -6.837  1.00 10.25 ? 410  GLY A O   1 
ATOM   3079 N  N   . LEU A 1 409 ? 80.656  -10.918 -5.953  1.00 10.36 ? 411  LEU A N   1 
ATOM   3080 C  CA  . LEU A 1 409 ? 81.992  -10.684 -5.391  1.00 10.74 ? 411  LEU A CA  1 
ATOM   3081 C  C   . LEU A 1 409 ? 83.059  -10.476 -6.464  1.00 11.40 ? 411  LEU A C   1 
ATOM   3082 O  O   . LEU A 1 409 ? 84.047  -9.770  -6.242  1.00 11.74 ? 411  LEU A O   1 
ATOM   3083 C  CB  . LEU A 1 409 ? 82.411  -11.837 -4.476  1.00 10.69 ? 411  LEU A CB  1 
ATOM   3084 C  CG  . LEU A 1 409 ? 81.634  -12.016 -3.170  1.00 10.53 ? 411  LEU A CG  1 
ATOM   3085 C  CD1 . LEU A 1 409 ? 82.167  -13.215 -2.394  1.00 10.48 ? 411  LEU A CD1 1 
ATOM   3086 C  CD2 . LEU A 1 409 ? 81.691  -10.755 -2.319  1.00 10.11 ? 411  LEU A CD2 1 
ATOM   3087 N  N   . LEU A 1 410 ? 82.871  -11.118 -7.613  1.00 11.50 ? 412  LEU A N   1 
ATOM   3088 C  CA  . LEU A 1 410 ? 83.857  -11.088 -8.686  1.00 12.33 ? 412  LEU A CA  1 
ATOM   3089 C  C   . LEU A 1 410 ? 83.544  -9.977  -9.683  1.00 12.85 ? 412  LEU A C   1 
ATOM   3090 O  O   . LEU A 1 410 ? 82.535  -10.033 -10.385 1.00 12.27 ? 412  LEU A O   1 
ATOM   3091 C  CB  . LEU A 1 410 ? 83.898  -12.438 -9.406  1.00 12.78 ? 412  LEU A CB  1 
ATOM   3092 C  CG  . LEU A 1 410 ? 84.248  -13.658 -8.550  1.00 13.14 ? 412  LEU A CG  1 
ATOM   3093 C  CD1 . LEU A 1 410 ? 84.263  -14.919 -9.398  1.00 14.50 ? 412  LEU A CD1 1 
ATOM   3094 C  CD2 . LEU A 1 410 ? 85.589  -13.465 -7.856  1.00 13.39 ? 412  LEU A CD2 1 
ATOM   3095 N  N   . PRO A 1 411 ? 84.427  -8.971  -9.764  1.00 13.78 ? 413  PRO A N   1 
ATOM   3096 C  CA  . PRO A 1 411 ? 84.188  -7.770  -10.560 1.00 14.22 ? 413  PRO A CA  1 
ATOM   3097 C  C   . PRO A 1 411 ? 83.819  -8.049  -12.019 1.00 14.38 ? 413  PRO A C   1 
ATOM   3098 O  O   . PRO A 1 411 ? 83.012  -7.321  -12.597 1.00 14.40 ? 413  PRO A O   1 
ATOM   3099 C  CB  . PRO A 1 411 ? 85.529  -7.034  -10.476 1.00 14.53 ? 413  PRO A CB  1 
ATOM   3100 C  CG  . PRO A 1 411 ? 86.065  -7.431  -9.144  1.00 14.00 ? 413  PRO A CG  1 
ATOM   3101 C  CD  . PRO A 1 411 ? 85.681  -8.879  -8.997  1.00 13.85 ? 413  PRO A CD  1 
ATOM   3102 N  N   . SER A 1 412 ? 84.371  -9.113  -12.597 1.00 14.07 ? 414  SER A N   1 
ATOM   3103 C  CA  . SER A 1 412 ? 84.218  -9.361  -14.033 1.00 14.70 ? 414  SER A CA  1 
ATOM   3104 C  C   . SER A 1 412 ? 82.874  -9.990  -14.417 1.00 14.93 ? 414  SER A C   1 
ATOM   3105 O  O   . SER A 1 412 ? 82.514  -10.027 -15.593 1.00 14.52 ? 414  SER A O   1 
ATOM   3106 C  CB  . SER A 1 412 ? 85.369  -10.224 -14.556 1.00 15.07 ? 414  SER A CB  1 
ATOM   3107 O  OG  . SER A 1 412 ? 85.266  -11.548 -14.071 1.00 16.36 ? 414  SER A OG  1 
ATOM   3108 N  N   . ASN A 1 413 ? 82.146  -10.494 -13.426 1.00 13.79 ? 415  ASN A N   1 
ATOM   3109 C  CA  . ASN A 1 413 ? 80.865  -11.159 -13.663 1.00 13.26 ? 415  ASN A CA  1 
ATOM   3110 C  C   . ASN A 1 413 ? 80.024  -11.161 -12.393 1.00 13.44 ? 415  ASN A C   1 
ATOM   3111 O  O   . ASN A 1 413 ? 80.223  -11.995 -11.511 1.00 12.44 ? 415  ASN A O   1 
ATOM   3112 C  CB  . ASN A 1 413 ? 81.092  -12.598 -14.142 1.00 14.15 ? 415  ASN A CB  1 
ATOM   3113 C  CG  . ASN A 1 413 ? 79.796  -13.325 -14.455 1.00 15.28 ? 415  ASN A CG  1 
ATOM   3114 O  OD1 . ASN A 1 413 ? 78.707  -12.760 -14.344 1.00 14.35 ? 415  ASN A OD1 1 
ATOM   3115 N  ND2 . ASN A 1 413 ? 79.910  -14.591 -14.852 1.00 17.42 ? 415  ASN A ND2 1 
ATOM   3116 N  N   . SER A 1 414 ? 79.099  -10.211 -12.298 1.00 13.20 ? 416  SER A N   1 
ATOM   3117 C  CA  . SER A 1 414 ? 78.308  -10.030 -11.087 1.00 14.06 ? 416  SER A CA  1 
ATOM   3118 C  C   . SER A 1 414 ? 77.347  -11.187 -10.862 1.00 13.30 ? 416  SER A C   1 
ATOM   3119 O  O   . SER A 1 414 ? 76.797  -11.340 -9.773  1.00 14.65 ? 416  SER A O   1 
ATOM   3120 C  CB  . SER A 1 414 ? 77.542  -8.704  -11.128 1.00 14.33 ? 416  SER A CB  1 
ATOM   3121 O  OG  . SER A 1 414 ? 76.490  -8.740  -12.082 1.00 14.76 ? 416  SER A OG  1 
ATOM   3122 N  N   . SER A 1 415 ? 77.163  -12.012 -11.888 1.00 13.39 ? 417  SER A N   1 
ATOM   3123 C  CA  . SER A 1 415 ? 76.316  -13.191 -11.765 1.00 13.77 ? 417  SER A CA  1 
ATOM   3124 C  C   . SER A 1 415 ? 77.058  -14.373 -11.153 1.00 13.77 ? 417  SER A C   1 
ATOM   3125 O  O   . SER A 1 415 ? 76.438  -15.356 -10.758 1.00 14.22 ? 417  SER A O   1 
ATOM   3126 C  CB  . SER A 1 415 ? 75.731  -13.584 -13.123 1.00 13.52 ? 417  SER A CB  1 
ATOM   3127 O  OG  . SER A 1 415 ? 74.802  -12.615 -13.570 1.00 14.25 ? 417  SER A OG  1 
ATOM   3128 N  N   . ALA A 1 416 ? 78.383  -14.285 -11.085 1.00 13.54 ? 418  ALA A N   1 
ATOM   3129 C  CA  . ALA A 1 416 ? 79.186  -15.406 -10.598 1.00 14.11 ? 418  ALA A CA  1 
ATOM   3130 C  C   . ALA A 1 416 ? 78.973  -15.636 -9.102  1.00 14.32 ? 418  ALA A C   1 
ATOM   3131 O  O   . ALA A 1 416 ? 79.129  -14.716 -8.296  1.00 14.32 ? 418  ALA A O   1 
ATOM   3132 C  CB  . ALA A 1 416 ? 80.659  -15.182 -10.900 1.00 13.85 ? 418  ALA A CB  1 
ATOM   3133 N  N   . SER A 1 417 ? 78.617  -16.866 -8.742  1.00 13.70 ? 419  SER A N   1 
ATOM   3134 C  CA  . SER A 1 417 ? 78.375  -17.238 -7.351  1.00 14.11 ? 419  SER A CA  1 
ATOM   3135 C  C   . SER A 1 417 ? 79.637  -17.799 -6.712  1.00 13.46 ? 419  SER A C   1 
ATOM   3136 O  O   . SER A 1 417 ? 80.403  -18.510 -7.357  1.00 13.52 ? 419  SER A O   1 
ATOM   3137 C  CB  . SER A 1 417 ? 77.273  -18.302 -7.267  1.00 15.40 ? 419  SER A CB  1 
ATOM   3138 O  OG  . SER A 1 417 ? 75.993  -17.742 -7.488  1.00 16.04 ? 419  SER A OG  1 
ATOM   3139 N  N   . LEU A 1 418 ? 79.824  -17.516 -5.429  1.00 13.61 ? 420  LEU A N   1 
ATOM   3140 C  CA  . LEU A 1 418 ? 80.778  -18.266 -4.623  1.00 13.26 ? 420  LEU A CA  1 
ATOM   3141 C  C   . LEU A 1 418 ? 80.054  -18.999 -3.505  1.00 13.52 ? 420  LEU A C   1 
ATOM   3142 O  O   . LEU A 1 418 ? 79.125  -18.465 -2.893  1.00 12.61 ? 420  LEU A O   1 
ATOM   3143 C  CB  . LEU A 1 418 ? 81.856  -17.345 -4.043  1.00 13.83 ? 420  LEU A CB  1 
ATOM   3144 C  CG  . LEU A 1 418 ? 82.885  -16.777 -5.023  1.00 13.99 ? 420  LEU A CG  1 
ATOM   3145 C  CD1 . LEU A 1 418 ? 83.992  -16.045 -4.278  1.00 14.46 ? 420  LEU A CD1 1 
ATOM   3146 C  CD2 . LEU A 1 418 ? 83.456  -17.881 -5.897  1.00 14.31 ? 420  LEU A CD2 1 
ATOM   3147 N  N   . SER A 1 419 ? 80.454  -20.243 -3.277  1.00 13.28 ? 421  SER A N   1 
ATOM   3148 C  CA  . SER A 1 419 ? 79.935  -21.023 -2.166  1.00 13.88 ? 421  SER A CA  1 
ATOM   3149 C  C   . SER A 1 419 ? 80.963  -21.020 -1.045  1.00 13.96 ? 421  SER A C   1 
ATOM   3150 O  O   . SER A 1 419 ? 82.044  -21.585 -1.187  1.00 14.48 ? 421  SER A O   1 
ATOM   3151 C  CB  . SER A 1 419 ? 79.651  -22.455 -2.615  1.00 15.66 ? 421  SER A CB  1 
ATOM   3152 O  OG  . SER A 1 419 ? 79.206  -23.243 -1.527  1.00 17.58 ? 421  SER A OG  1 
ATOM   3153 N  N   . ILE A 1 420 ? 80.649  -20.331 0.045   1.00 12.52 ? 422  ILE A N   1 
ATOM   3154 C  CA  . ILE A 1 420 ? 81.662  -19.980 1.032   1.00 11.89 ? 422  ILE A CA  1 
ATOM   3155 C  C   . ILE A 1 420 ? 81.357  -20.622 2.380   1.00 11.59 ? 422  ILE A C   1 
ATOM   3156 O  O   . ILE A 1 420 ? 80.274  -20.430 2.932   1.00 11.82 ? 422  ILE A O   1 
ATOM   3157 C  CB  . ILE A 1 420 ? 81.766  -18.453 1.204   1.00 11.53 ? 422  ILE A CB  1 
ATOM   3158 C  CG1 . ILE A 1 420 ? 81.698  -17.758 -0.160  1.00 11.14 ? 422  ILE A CG1 1 
ATOM   3159 C  CG2 . ILE A 1 420 ? 83.050  -18.083 1.930   1.00 11.60 ? 422  ILE A CG2 1 
ATOM   3160 C  CD1 . ILE A 1 420 ? 81.979  -16.271 -0.100  1.00 10.65 ? 422  ILE A CD1 1 
ATOM   3161 N  N   . PRO A 1 421 ? 82.304  -21.416 2.900   1.00 12.00 ? 423  PRO A N   1 
ATOM   3162 C  CA  . PRO A 1 421 ? 82.190  -21.938 4.258   1.00 12.58 ? 423  PRO A CA  1 
ATOM   3163 C  C   . PRO A 1 421 ? 82.147  -20.786 5.247   1.00 13.19 ? 423  PRO A C   1 
ATOM   3164 O  O   . PRO A 1 421 ? 82.663  -19.705 4.959   1.00 13.06 ? 423  PRO A O   1 
ATOM   3165 C  CB  . PRO A 1 421 ? 83.490  -22.736 4.444   1.00 13.03 ? 423  PRO A CB  1 
ATOM   3166 C  CG  . PRO A 1 421 ? 84.009  -22.977 3.068   1.00 13.82 ? 423  PRO A CG  1 
ATOM   3167 C  CD  . PRO A 1 421 ? 83.577  -21.788 2.265   1.00 12.60 ? 423  PRO A CD  1 
ATOM   3168 N  N   . GLN A 1 422 ? 81.529  -21.007 6.402   1.00 14.41 ? 424  GLN A N   1 
ATOM   3169 C  CA  . GLN A 1 422 ? 81.561  -20.011 7.460   1.00 14.57 ? 424  GLN A CA  1 
ATOM   3170 C  C   . GLN A 1 422 ? 83.004  -19.748 7.886   1.00 14.67 ? 424  GLN A C   1 
ATOM   3171 O  O   . GLN A 1 422 ? 83.764  -20.687 8.128   1.00 15.78 ? 424  GLN A O   1 
ATOM   3172 C  CB  . GLN A 1 422 ? 80.734  -20.476 8.658   1.00 15.57 ? 424  GLN A CB  1 
ATOM   3173 C  CG  . GLN A 1 422 ? 79.231  -20.389 8.450   1.00 16.01 ? 424  GLN A CG  1 
ATOM   3174 C  CD  . GLN A 1 422 ? 78.460  -20.546 9.746   1.00 17.81 ? 424  GLN A CD  1 
ATOM   3175 O  OE1 . GLN A 1 422 ? 78.885  -20.061 10.795  1.00 18.66 ? 424  GLN A OE1 1 
ATOM   3176 N  NE2 . GLN A 1 422 ? 77.321  -21.224 9.680   1.00 16.19 ? 424  GLN A NE2 1 
ATOM   3177 N  N   . PHE A 1 423 ? 83.380  -18.473 7.943   1.00 14.07 ? 425  PHE A N   1 
ATOM   3178 C  CA  . PHE A 1 423 ? 84.655  -18.058 8.530   1.00 14.30 ? 425  PHE A CA  1 
ATOM   3179 C  C   . PHE A 1 423 ? 84.434  -17.539 9.942   1.00 12.89 ? 425  PHE A C   1 
ATOM   3180 O  O   . PHE A 1 423 ? 85.383  -17.339 10.697  1.00 11.69 ? 425  PHE A O   1 
ATOM   3181 C  CB  . PHE A 1 423 ? 85.291  -16.946 7.699   1.00 15.87 ? 425  PHE A CB  1 
ATOM   3182 C  CG  . PHE A 1 423 ? 85.459  -17.289 6.250   1.00 17.77 ? 425  PHE A CG  1 
ATOM   3183 C  CD1 . PHE A 1 423 ? 86.099  -18.455 5.874   1.00 18.34 ? 425  PHE A CD1 1 
ATOM   3184 C  CD2 . PHE A 1 423 ? 85.022  -16.416 5.264   1.00 20.42 ? 425  PHE A CD2 1 
ATOM   3185 C  CE1 . PHE A 1 423 ? 86.268  -18.770 4.538   1.00 18.66 ? 425  PHE A CE1 1 
ATOM   3186 C  CE2 . PHE A 1 423 ? 85.200  -16.716 3.927   1.00 20.11 ? 425  PHE A CE2 1 
ATOM   3187 C  CZ  . PHE A 1 423 ? 85.828  -17.894 3.564   1.00 19.38 ? 425  PHE A CZ  1 
ATOM   3188 N  N   . VAL A 1 424 ? 83.178  -17.243 10.254  1.00 12.46 ? 426  VAL A N   1 
ATOM   3189 C  CA  . VAL A 1 424 ? 82.796  -16.784 11.581  1.00 11.89 ? 426  VAL A CA  1 
ATOM   3190 C  C   . VAL A 1 424 ? 81.844  -17.801 12.196  1.00 12.40 ? 426  VAL A C   1 
ATOM   3191 O  O   . VAL A 1 424 ? 80.850  -18.180 11.578  1.00 13.16 ? 426  VAL A O   1 
ATOM   3192 C  CB  . VAL A 1 424 ? 82.085  -15.420 11.512  1.00 11.78 ? 426  VAL A CB  1 
ATOM   3193 C  CG1 . VAL A 1 424 ? 81.555  -15.028 12.883  1.00 13.17 ? 426  VAL A CG1 1 
ATOM   3194 C  CG2 . VAL A 1 424 ? 83.034  -14.357 10.981  1.00 12.07 ? 426  VAL A CG2 1 
ATOM   3195 N  N   . VAL A 1 425 ? 82.163  -18.252 13.404  1.00 11.53 ? 427  VAL A N   1 
ATOM   3196 C  CA  . VAL A 1 425 ? 81.376  -19.280 14.066  1.00 10.89 ? 427  VAL A CA  1 
ATOM   3197 C  C   . VAL A 1 425 ? 80.818  -18.721 15.366  1.00 11.03 ? 427  VAL A C   1 
ATOM   3198 O  O   . VAL A 1 425 ? 81.574  -18.310 16.249  1.00 10.20 ? 427  VAL A O   1 
ATOM   3199 C  CB  . VAL A 1 425 ? 82.228  -20.530 14.370  1.00 11.18 ? 427  VAL A CB  1 
ATOM   3200 C  CG1 . VAL A 1 425 ? 81.414  -21.558 15.143  1.00 11.40 ? 427  VAL A CG1 1 
ATOM   3201 C  CG2 . VAL A 1 425 ? 82.768  -21.133 13.078  1.00 12.11 ? 427  VAL A CG2 1 
ATOM   3202 N  N   . SER A 1 426 ? 79.494  -18.637 15.450  1.00 11.41 ? 428  SER A N   1 
ATOM   3203 C  CA  . SER A 1 426 ? 78.851  -18.180 16.671  1.00 10.84 ? 428  SER A CA  1 
ATOM   3204 C  C   . SER A 1 426 ? 79.005  -19.197 17.786  1.00 10.78 ? 428  SER A C   1 
ATOM   3205 O  O   . SER A 1 426 ? 78.618  -20.357 17.646  1.00 11.55 ? 428  SER A O   1 
ATOM   3206 C  CB  . SER A 1 426 ? 77.368  -17.888 16.447  1.00 10.84 ? 428  SER A CB  1 
ATOM   3207 O  OG  . SER A 1 426 ? 76.746  -17.535 17.674  1.00 10.59 ? 428  SER A OG  1 
ATOM   3208 N  N   . HIS A 1 427 ? 79.552  -18.748 18.905  1.00 11.17 ? 429  HIS A N   1 
ATOM   3209 C  CA  . HIS A 1 427 ? 79.508  -19.526 20.131  1.00 12.01 ? 429  HIS A CA  1 
ATOM   3210 C  C   . HIS A 1 427 ? 78.486  -18.929 21.083  1.00 11.27 ? 429  HIS A C   1 
ATOM   3211 O  O   . HIS A 1 427 ? 78.506  -19.190 22.285  1.00 10.63 ? 429  HIS A O   1 
ATOM   3212 C  CB  . HIS A 1 427 ? 80.895  -19.602 20.767  1.00 13.13 ? 429  HIS A CB  1 
ATOM   3213 C  CG  . HIS A 1 427 ? 81.895  -20.332 19.925  1.00 14.26 ? 429  HIS A CG  1 
ATOM   3214 N  ND1 . HIS A 1 427 ? 81.667  -21.600 19.436  1.00 17.31 ? 429  HIS A ND1 1 
ATOM   3215 C  CD2 . HIS A 1 427 ? 83.086  -19.942 19.415  1.00 15.46 ? 429  HIS A CD2 1 
ATOM   3216 C  CE1 . HIS A 1 427 ? 82.694  -21.977 18.695  1.00 17.63 ? 429  HIS A CE1 1 
ATOM   3217 N  NE2 . HIS A 1 427 ? 83.569  -20.988 18.666  1.00 15.42 ? 429  HIS A NE2 1 
ATOM   3218 N  N   . GLY A 1 428 ? 77.580  -18.137 20.517  1.00 11.06 ? 430  GLY A N   1 
ATOM   3219 C  CA  . GLY A 1 428 ? 76.418  -17.653 21.235  1.00 10.86 ? 430  GLY A CA  1 
ATOM   3220 C  C   . GLY A 1 428 ? 76.721  -16.415 22.048  1.00 11.50 ? 430  GLY A C   1 
ATOM   3221 O  O   . GLY A 1 428 ? 77.736  -15.744 21.833  1.00 11.27 ? 430  GLY A O   1 
ATOM   3222 N  N   . GLY A 1 429 ? 75.864  -16.147 23.025  1.00 10.74 ? 431  GLY A N   1 
ATOM   3223 C  CA  . GLY A 1 429 ? 75.919  -14.903 23.778  1.00 10.39 ? 431  GLY A CA  1 
ATOM   3224 C  C   . GLY A 1 429 ? 74.623  -14.681 24.526  1.00 10.41 ? 431  GLY A C   1 
ATOM   3225 O  O   . GLY A 1 429 ? 73.850  -15.614 24.744  1.00 10.07 ? 431  GLY A O   1 
ATOM   3226 N  N   . GLU A 1 430 ? 74.379  -13.439 24.921  1.00 10.34 ? 432  GLU A N   1 
ATOM   3227 C  CA  . GLU A 1 430 ? 73.169  -13.115 25.649  1.00 10.42 ? 432  GLU A CA  1 
ATOM   3228 C  C   . GLU A 1 430 ? 72.765  -11.681 25.345  1.00 10.07 ? 432  GLU A C   1 
ATOM   3229 O  O   . GLU A 1 430 ? 73.576  -10.890 24.843  1.00 9.54  ? 432  GLU A O   1 
ATOM   3230 C  CB  . GLU A 1 430 ? 73.378  -13.327 27.154  1.00 10.68 ? 432  GLU A CB  1 
ATOM   3231 C  CG  . GLU A 1 430 ? 72.124  -13.186 28.010  1.00 11.66 ? 432  GLU A CG  1 
ATOM   3232 C  CD  . GLU A 1 430 ? 70.932  -13.963 27.471  1.00 12.44 ? 432  GLU A CD  1 
ATOM   3233 O  OE1 . GLU A 1 430 ? 70.223  -13.438 26.586  1.00 12.16 ? 432  GLU A OE1 1 
ATOM   3234 O  OE2 . GLU A 1 430 ? 70.657  -15.068 27.988  1.00 13.45 ? 432  GLU A OE2 1 
ATOM   3235 N  N   . TYR A 1 431 ? 71.484  -11.392 25.550  1.00 9.09  ? 433  TYR A N   1 
ATOM   3236 C  CA  . TYR A 1 431 ? 70.975  -10.029 25.517  1.00 9.10  ? 433  TYR A CA  1 
ATOM   3237 C  C   . TYR A 1 431 ? 70.913  -9.464  26.930  1.00 8.66  ? 433  TYR A C   1 
ATOM   3238 O  O   . TYR A 1 431 ? 70.335  -10.080 27.825  1.00 8.54  ? 433  TYR A O   1 
ATOM   3239 C  CB  . TYR A 1 431 ? 69.575  -10.002 24.901  1.00 8.81  ? 433  TYR A CB  1 
ATOM   3240 C  CG  . TYR A 1 431 ? 69.508  -10.485 23.467  1.00 8.74  ? 433  TYR A CG  1 
ATOM   3241 C  CD1 . TYR A 1 431 ? 70.477  -10.119 22.539  1.00 9.10  ? 433  TYR A CD1 1 
ATOM   3242 C  CD2 . TYR A 1 431 ? 68.448  -11.268 23.031  1.00 8.90  ? 433  TYR A CD2 1 
ATOM   3243 C  CE1 . TYR A 1 431 ? 70.400  -10.537 21.220  1.00 8.96  ? 433  TYR A CE1 1 
ATOM   3244 C  CE2 . TYR A 1 431 ? 68.359  -11.688 21.716  1.00 8.98  ? 433  TYR A CE2 1 
ATOM   3245 C  CZ  . TYR A 1 431 ? 69.341  -11.328 20.817  1.00 8.94  ? 433  TYR A CZ  1 
ATOM   3246 O  OH  . TYR A 1 431 ? 69.246  -11.750 19.509  1.00 9.38  ? 433  TYR A OH  1 
ATOM   3247 N  N   . PHE A 1 432 ? 71.502  -8.286  27.121  1.00 8.74  ? 434  PHE A N   1 
ATOM   3248 C  CA  . PHE A 1 432 ? 71.500  -7.627  28.426  1.00 8.96  ? 434  PHE A CA  1 
ATOM   3249 C  C   . PHE A 1 432 ? 70.855  -6.247  28.327  1.00 8.97  ? 434  PHE A C   1 
ATOM   3250 O  O   . PHE A 1 432 ? 70.668  -5.714  27.232  1.00 9.06  ? 434  PHE A O   1 
ATOM   3251 C  CB  . PHE A 1 432 ? 72.929  -7.476  28.959  1.00 8.69  ? 434  PHE A CB  1 
ATOM   3252 C  CG  . PHE A 1 432 ? 73.665  -8.780  29.119  1.00 9.06  ? 434  PHE A CG  1 
ATOM   3253 C  CD1 . PHE A 1 432 ? 74.411  -9.300  28.077  1.00 9.20  ? 434  PHE A CD1 1 
ATOM   3254 C  CD2 . PHE A 1 432 ? 73.654  -9.455  30.331  1.00 9.01  ? 434  PHE A CD2 1 
ATOM   3255 C  CE1 . PHE A 1 432 ? 75.116  -10.482 28.230  1.00 9.38  ? 434  PHE A CE1 1 
ATOM   3256 C  CE2 . PHE A 1 432 ? 74.348  -10.643 30.491  1.00 9.25  ? 434  PHE A CE2 1 
ATOM   3257 C  CZ  . PHE A 1 432 ? 75.082  -11.158 29.438  1.00 9.02  ? 434  PHE A CZ  1 
ATOM   3258 N  N   . PHE A 1 433 ? 70.507  -5.681  29.478  1.00 9.24  ? 435  PHE A N   1 
ATOM   3259 C  CA  . PHE A 1 433 ? 70.142  -4.271  29.557  1.00 9.43  ? 435  PHE A CA  1 
ATOM   3260 C  C   . PHE A 1 433 ? 71.159  -3.511  30.397  1.00 9.32  ? 435  PHE A C   1 
ATOM   3261 O  O   . PHE A 1 433 ? 71.337  -3.802  31.580  1.00 8.60  ? 435  PHE A O   1 
ATOM   3262 C  CB  . PHE A 1 433 ? 68.748  -4.107  30.161  1.00 9.66  ? 435  PHE A CB  1 
ATOM   3263 C  CG  . PHE A 1 433 ? 68.276  -2.682  30.208  1.00 9.64  ? 435  PHE A CG  1 
ATOM   3264 C  CD1 . PHE A 1 433 ? 68.037  -1.983  29.036  1.00 9.58  ? 435  PHE A CD1 1 
ATOM   3265 C  CD2 . PHE A 1 433 ? 68.110  -2.032  31.419  1.00 9.83  ? 435  PHE A CD2 1 
ATOM   3266 C  CE1 . PHE A 1 433 ? 67.616  -0.666  29.072  1.00 9.93  ? 435  PHE A CE1 1 
ATOM   3267 C  CE2 . PHE A 1 433 ? 67.697  -0.714  31.462  1.00 9.74  ? 435  PHE A CE2 1 
ATOM   3268 C  CZ  . PHE A 1 433 ? 67.454  -0.030  30.287  1.00 10.06 ? 435  PHE A CZ  1 
ATOM   3269 N  N   . SER A 1 434 ? 71.846  -2.561  29.771  1.00 9.79  ? 436  SER A N   1 
ATOM   3270 C  CA  . SER A 1 434 ? 72.719  -1.652  30.498  1.00 9.97  ? 436  SER A CA  1 
ATOM   3271 C  C   . SER A 1 434 ? 71.895  -0.481  30.998  1.00 9.52  ? 436  SER A C   1 
ATOM   3272 O  O   . SER A 1 434 ? 71.429  0.337   30.208  1.00 8.82  ? 436  SER A O   1 
ATOM   3273 C  CB  . SER A 1 434 ? 73.846  -1.143  29.600  1.00 10.93 ? 436  SER A CB  1 
ATOM   3274 O  OG  . SER A 1 434 ? 74.578  -2.219  29.040  1.00 13.88 ? 436  SER A OG  1 
ATOM   3275 N  N   . PRO A 1 435 ? 71.642  -0.442  32.310  1.00 9.66  ? 437  PRO A N   1 
ATOM   3276 C  CA  . PRO A 1 435 ? 70.774  0.589   32.855  1.00 9.23  ? 437  PRO A CA  1 
ATOM   3277 C  C   . PRO A 1 435 ? 71.501  1.924   32.923  1.00 9.49  ? 437  PRO A C   1 
ATOM   3278 O  O   . PRO A 1 435 ? 72.730  1.960   32.868  1.00 8.79  ? 437  PRO A O   1 
ATOM   3279 C  CB  . PRO A 1 435 ? 70.469  0.077   34.263  1.00 9.69  ? 437  PRO A CB  1 
ATOM   3280 C  CG  . PRO A 1 435 ? 71.657  -0.745  34.626  1.00 10.09 ? 437  PRO A CG  1 
ATOM   3281 C  CD  . PRO A 1 435 ? 72.170  -1.346  33.346  1.00 9.63  ? 437  PRO A CD  1 
ATOM   3282 N  N   . PRO A 1 436 ? 70.744  3.025   33.017  1.00 9.34  ? 438  PRO A N   1 
ATOM   3283 C  CA  . PRO A 1 436 ? 71.350  4.297   33.392  1.00 9.73  ? 438  PRO A CA  1 
ATOM   3284 C  C   . PRO A 1 436 ? 71.992  4.178   34.769  1.00 10.20 ? 438  PRO A C   1 
ATOM   3285 O  O   . PRO A 1 436 ? 71.559  3.367   35.584  1.00 10.04 ? 438  PRO A O   1 
ATOM   3286 C  CB  . PRO A 1 436 ? 70.156  5.254   33.448  1.00 9.46  ? 438  PRO A CB  1 
ATOM   3287 C  CG  . PRO A 1 436 ? 68.983  4.377   33.727  1.00 9.88  ? 438  PRO A CG  1 
ATOM   3288 C  CD  . PRO A 1 436 ? 69.272  3.070   33.043  1.00 9.70  ? 438  PRO A CD  1 
ATOM   3289 N  N   . ILE A 1 437 ? 73.024  4.972   35.023  1.00 10.79 ? 439  ILE A N   1 
ATOM   3290 C  CA  . ILE A 1 437 ? 73.807  4.808   36.239  1.00 11.23 ? 439  ILE A CA  1 
ATOM   3291 C  C   . ILE A 1 437 ? 72.957  5.023   37.488  1.00 11.86 ? 439  ILE A C   1 
ATOM   3292 O  O   . ILE A 1 437 ? 73.115  4.320   38.487  1.00 12.33 ? 439  ILE A O   1 
ATOM   3293 C  CB  . ILE A 1 437 ? 75.039  5.734   36.242  1.00 11.43 ? 439  ILE A CB  1 
ATOM   3294 C  CG1 . ILE A 1 437 ? 75.961  5.367   35.075  1.00 11.67 ? 439  ILE A CG1 1 
ATOM   3295 C  CG2 . ILE A 1 437 ? 75.780  5.626   37.566  1.00 12.01 ? 439  ILE A CG2 1 
ATOM   3296 C  CD1 . ILE A 1 437 ? 77.003  6.417   34.740  1.00 11.40 ? 439  ILE A CD1 1 
ATOM   3297 N  N   . SER A 1 438 ? 72.000  5.942   37.392  1.00 12.45 ? 440  SER A N   1 
ATOM   3298 C  CA  . SER A 1 438 ? 71.096  6.245   38.496  1.00 12.41 ? 440  SER A CA  1 
ATOM   3299 C  C   . SER A 1 438 ? 70.309  5.025   38.966  1.00 12.24 ? 440  SER A C   1 
ATOM   3300 O  O   . SER A 1 438 ? 69.964  4.922   40.138  1.00 12.17 ? 440  SER A O   1 
ATOM   3301 C  CB  . SER A 1 438 ? 70.136  7.373   38.108  1.00 13.15 ? 440  SER A CB  1 
ATOM   3302 O  OG  . SER A 1 438 ? 69.450  7.059   36.907  1.00 14.04 ? 440  SER A OG  1 
ATOM   3303 N  N   . ALA A 1 439 ? 70.057  4.086   38.060  1.00 11.87 ? 441  ALA A N   1 
ATOM   3304 C  CA  . ALA A 1 439 ? 69.243  2.915   38.386  1.00 11.90 ? 441  ALA A CA  1 
ATOM   3305 C  C   . ALA A 1 439 ? 70.038  1.859   39.155  1.00 12.03 ? 441  ALA A C   1 
ATOM   3306 O  O   . ALA A 1 439 ? 69.463  1.018   39.843  1.00 12.33 ? 441  ALA A O   1 
ATOM   3307 C  CB  . ALA A 1 439 ? 68.647  2.314   37.119  1.00 11.72 ? 441  ALA A CB  1 
ATOM   3308 N  N   . ILE A 1 440 ? 71.361  1.906   39.035  1.00 12.47 ? 442  ILE A N   1 
ATOM   3309 C  CA  . ILE A 1 440 ? 72.213  0.867   39.603  1.00 12.51 ? 442  ILE A CA  1 
ATOM   3310 C  C   . ILE A 1 440 ? 72.179  0.901   41.129  1.00 13.41 ? 442  ILE A C   1 
ATOM   3311 O  O   . ILE A 1 440 ? 71.861  -0.102  41.774  1.00 14.14 ? 442  ILE A O   1 
ATOM   3312 C  CB  . ILE A 1 440 ? 73.662  0.977   39.088  1.00 12.77 ? 442  ILE A CB  1 
ATOM   3313 C  CG1 . ILE A 1 440 ? 73.706  0.688   37.586  1.00 13.09 ? 442  ILE A CG1 1 
ATOM   3314 C  CG2 . ILE A 1 440 ? 74.574  0.011   39.832  1.00 12.51 ? 442  ILE A CG2 1 
ATOM   3315 C  CD1 . ILE A 1 440 ? 74.950  1.203   36.897  1.00 14.84 ? 442  ILE A CD1 1 
ATOM   3316 N  N   . GLY A 1 441 ? 72.410  2.081   41.694  1.00 14.18 ? 443  GLY A N   1 
ATOM   3317 C  CA  . GLY A 1 441 ? 72.227  2.294   43.126  1.00 15.87 ? 443  GLY A CA  1 
ATOM   3318 C  C   . GLY A 1 441 ? 70.835  2.789   43.479  1.00 16.38 ? 443  GLY A C   1 
ATOM   3319 O  O   . GLY A 1 441 ? 70.523  2.999   44.653  1.00 16.25 ? 443  GLY A O   1 
ATOM   3320 N  N   . GLY A 1 442 ? 70.003  2.991   42.461  1.00 15.30 ? 444  GLY A N   1 
ATOM   3321 C  CA  . GLY A 1 442 ? 68.597  3.328   42.664  1.00 14.36 ? 444  GLY A CA  1 
ATOM   3322 C  C   . GLY A 1 442 ? 67.695  2.106   42.682  1.00 13.39 ? 444  GLY A C   1 
ATOM   3323 O  O   . GLY A 1 442 ? 67.767  1.288   43.602  1.00 14.48 ? 444  GLY A O   1 
ATOM   3324 N  N   . ARG A 1 443 ? 66.869  1.959   41.647  1.00 12.66 ? 445  ARG A N   1 
ATOM   3325 C  CA  . ARG A 1 443 ? 65.871  0.888   41.605  1.00 11.82 ? 445  ARG A CA  1 
ATOM   3326 C  C   . ARG A 1 443 ? 66.473  -0.498  41.799  1.00 12.01 ? 445  ARG A C   1 
ATOM   3327 O  O   . ARG A 1 443 ? 65.913  -1.327  42.514  1.00 12.57 ? 445  ARG A O   1 
ATOM   3328 C  CB  . ARG A 1 443 ? 65.071  0.925   40.299  1.00 12.15 ? 445  ARG A CB  1 
ATOM   3329 C  CG  . ARG A 1 443 ? 64.131  -0.261  40.114  1.00 11.72 ? 445  ARG A CG  1 
ATOM   3330 C  CD  . ARG A 1 443 ? 63.065  -0.302  41.197  1.00 12.13 ? 445  ARG A CD  1 
ATOM   3331 N  NE  . ARG A 1 443 ? 62.247  -1.513  41.132  1.00 12.18 ? 445  ARG A NE  1 
ATOM   3332 C  CZ  . ARG A 1 443 ? 62.472  -2.609  41.852  1.00 11.87 ? 445  ARG A CZ  1 
ATOM   3333 N  NH1 . ARG A 1 443 ? 63.503  -2.656  42.681  1.00 12.18 ? 445  ARG A NH1 1 
ATOM   3334 N  NH2 . ARG A 1 443 ? 61.667  -3.658  41.740  1.00 10.93 ? 445  ARG A NH2 1 
ATOM   3335 N  N   . LEU A 1 444 ? 67.592  -0.765  41.134  1.00 12.25 ? 446  LEU A N   1 
ATOM   3336 C  CA  . LEU A 1 444 ? 68.135  -2.121  41.098  1.00 12.69 ? 446  LEU A CA  1 
ATOM   3337 C  C   . LEU A 1 444 ? 68.703  -2.557  42.448  1.00 13.23 ? 446  LEU A C   1 
ATOM   3338 O  O   . LEU A 1 444 ? 68.816  -3.750  42.722  1.00 14.06 ? 446  LEU A O   1 
ATOM   3339 C  CB  . LEU A 1 444 ? 69.189  -2.260  39.997  1.00 12.83 ? 446  LEU A CB  1 
ATOM   3340 C  CG  . LEU A 1 444 ? 68.666  -1.980  38.583  1.00 13.00 ? 446  LEU A CG  1 
ATOM   3341 C  CD1 . LEU A 1 444 ? 69.756  -2.192  37.545  1.00 13.51 ? 446  LEU A CD1 1 
ATOM   3342 C  CD2 . LEU A 1 444 ? 67.458  -2.853  38.284  1.00 12.55 ? 446  LEU A CD2 1 
ATOM   3343 N  N   . SER A 1 445 ? 69.019  -1.588  43.301  1.00 13.39 ? 447  SER A N   1 
ATOM   3344 C  CA  . SER A 1 445 ? 69.508  -1.881  44.646  1.00 15.03 ? 447  SER A CA  1 
ATOM   3345 C  C   . SER A 1 445 ? 68.397  -1.817  45.691  1.00 16.30 ? 447  SER A C   1 
ATOM   3346 O  O   . SER A 1 445 ? 68.635  -2.067  46.875  1.00 17.53 ? 447  SER A O   1 
ATOM   3347 C  CB  . SER A 1 445 ? 70.630  -0.912  45.029  1.00 15.06 ? 447  SER A CB  1 
ATOM   3348 O  OG  . SER A 1 445 ? 71.770  -1.097  44.209  1.00 15.48 ? 447  SER A OG  1 
ATOM   3349 N  N   . ALA A 1 446 ? 67.189  -1.472  45.257  1.00 17.64 ? 448  ALA A N   1 
ATOM   3350 C  CA  . ALA A 1 446 ? 66.086  -1.221  46.184  1.00 20.35 ? 448  ALA A CA  1 
ATOM   3351 C  C   . ALA A 1 446 ? 65.378  -2.507  46.610  1.00 24.21 ? 448  ALA A C   1 
ATOM   3352 O  O   . ALA A 1 446 ? 64.964  -2.640  47.762  1.00 28.57 ? 448  ALA A O   1 
ATOM   3353 C  CB  . ALA A 1 446 ? 65.091  -0.241  45.581  1.00 18.32 ? 448  ALA A CB  1 
ATOM   3354 O  OXT . ALA A 1 446 ? 65.201  -3.440  45.823  1.00 24.05 ? 448  ALA A OXT 1 
ATOM   3355 N  N   . LEU B 1 2   ? 131.789 -27.589 35.165  1.00 27.18 ? 4    LEU B N   1 
ATOM   3356 C  CA  . LEU B 1 2   ? 130.300 -27.508 35.067  1.00 25.44 ? 4    LEU B CA  1 
ATOM   3357 C  C   . LEU B 1 2   ? 129.860 -26.846 33.763  1.00 24.00 ? 4    LEU B C   1 
ATOM   3358 O  O   . LEU B 1 2   ? 130.162 -25.678 33.513  1.00 23.29 ? 4    LEU B O   1 
ATOM   3359 C  CB  . LEU B 1 2   ? 129.718 -26.757 36.269  1.00 26.10 ? 4    LEU B CB  1 
ATOM   3360 C  CG  . LEU B 1 2   ? 128.206 -26.894 36.475  1.00 24.98 ? 4    LEU B CG  1 
ATOM   3361 C  CD1 . LEU B 1 2   ? 127.841 -28.318 36.870  1.00 24.23 ? 4    LEU B CD1 1 
ATOM   3362 C  CD2 . LEU B 1 2   ? 127.702 -25.906 37.515  1.00 24.55 ? 4    LEU B CD2 1 
ATOM   3363 N  N   . ASN B 1 3   ? 129.153 -27.604 32.932  1.00 20.95 ? 5    ASN B N   1 
ATOM   3364 C  CA  . ASN B 1 3   ? 128.712 -27.118 31.630  1.00 20.34 ? 5    ASN B CA  1 
ATOM   3365 C  C   . ASN B 1 3   ? 127.370 -26.400 31.726  1.00 20.07 ? 5    ASN B C   1 
ATOM   3366 O  O   . ASN B 1 3   ? 126.317 -27.004 31.521  1.00 20.46 ? 5    ASN B O   1 
ATOM   3367 C  CB  . ASN B 1 3   ? 128.614 -28.283 30.645  1.00 20.13 ? 5    ASN B CB  1 
ATOM   3368 C  CG  . ASN B 1 3   ? 128.215 -27.841 29.251  1.00 20.02 ? 5    ASN B CG  1 
ATOM   3369 O  OD1 . ASN B 1 3   ? 128.036 -26.651 28.987  1.00 20.56 ? 5    ASN B OD1 1 
ATOM   3370 N  ND2 . ASN B 1 3   ? 128.065 -28.803 28.351  1.00 22.41 ? 5    ASN B ND2 1 
ATOM   3371 N  N   . THR B 1 4   ? 127.411 -25.112 32.048  1.00 19.46 ? 6    THR B N   1 
ATOM   3372 C  CA  . THR B 1 4   ? 126.192 -24.361 32.330  1.00 18.57 ? 6    THR B CA  1 
ATOM   3373 C  C   . THR B 1 4   ? 125.403 -24.062 31.059  1.00 17.90 ? 6    THR B C   1 
ATOM   3374 O  O   . THR B 1 4   ? 124.248 -23.635 31.123  1.00 17.75 ? 6    THR B O   1 
ATOM   3375 C  CB  . THR B 1 4   ? 126.496 -23.041 33.067  1.00 18.72 ? 6    THR B CB  1 
ATOM   3376 O  OG1 . THR B 1 4   ? 127.394 -22.253 32.280  1.00 18.71 ? 6    THR B OG1 1 
ATOM   3377 C  CG2 . THR B 1 4   ? 127.127 -23.318 34.428  1.00 18.76 ? 6    THR B CG2 1 
ATOM   3378 N  N   . ASP B 1 5   ? 126.033 -24.266 29.907  1.00 17.79 ? 7    ASP B N   1 
ATOM   3379 C  CA  . ASP B 1 5   ? 125.341 -24.151 28.628  1.00 17.52 ? 7    ASP B CA  1 
ATOM   3380 C  C   . ASP B 1 5   ? 124.261 -25.218 28.494  1.00 16.32 ? 7    ASP B C   1 
ATOM   3381 O  O   . ASP B 1 5   ? 123.344 -25.081 27.685  1.00 16.55 ? 7    ASP B O   1 
ATOM   3382 C  CB  . ASP B 1 5   ? 126.322 -24.297 27.461  1.00 19.42 ? 7    ASP B CB  1 
ATOM   3383 C  CG  . ASP B 1 5   ? 127.264 -23.115 27.331  1.00 22.43 ? 7    ASP B CG  1 
ATOM   3384 O  OD1 . ASP B 1 5   ? 127.159 -22.163 28.135  1.00 21.90 ? 7    ASP B OD1 1 
ATOM   3385 O  OD2 . ASP B 1 5   ? 128.119 -23.146 26.422  1.00 24.07 ? 7    ASP B OD2 1 
ATOM   3386 N  N   . ASP B 1 6   ? 124.422 -26.319 29.221  1.00 14.33 ? 8    ASP B N   1 
ATOM   3387 C  CA  . ASP B 1 6   ? 123.553 -27.478 29.031  1.00 13.74 ? 8    ASP B CA  1 
ATOM   3388 C  C   . ASP B 1 6   ? 122.572 -27.657 30.186  1.00 12.49 ? 8    ASP B C   1 
ATOM   3389 O  O   . ASP B 1 6   ? 121.790 -28.608 30.205  1.00 12.01 ? 8    ASP B O   1 
ATOM   3390 C  CB  . ASP B 1 6   ? 124.380 -28.752 28.826  1.00 14.07 ? 8    ASP B CB  1 
ATOM   3391 C  CG  . ASP B 1 6   ? 123.597 -29.847 28.125  1.00 15.30 ? 8    ASP B CG  1 
ATOM   3392 O  OD1 . ASP B 1 6   ? 122.696 -29.519 27.320  1.00 14.19 ? 8    ASP B OD1 1 
ATOM   3393 O  OD2 . ASP B 1 6   ? 123.872 -31.037 28.391  1.00 15.66 ? 8    ASP B OD2 1 
ATOM   3394 N  N   . ILE B 1 7   ? 122.612 -26.732 31.142  1.00 10.89 ? 9    ILE B N   1 
ATOM   3395 C  CA  . ILE B 1 7   ? 121.743 -26.795 32.314  1.00 10.11 ? 9    ILE B CA  1 
ATOM   3396 C  C   . ILE B 1 7   ? 120.606 -25.790 32.174  1.00 9.61  ? 9    ILE B C   1 
ATOM   3397 O  O   . ILE B 1 7   ? 120.825 -24.643 31.780  1.00 9.46  ? 9    ILE B O   1 
ATOM   3398 C  CB  . ILE B 1 7   ? 122.523 -26.506 33.612  1.00 9.87  ? 9    ILE B CB  1 
ATOM   3399 C  CG1 . ILE B 1 7   ? 123.638 -27.538 33.797  1.00 10.15 ? 9    ILE B CG1 1 
ATOM   3400 C  CG2 . ILE B 1 7   ? 121.594 -26.518 34.817  1.00 9.17  ? 9    ILE B CG2 1 
ATOM   3401 C  CD1 . ILE B 1 7   ? 124.558 -27.243 34.958  1.00 9.96  ? 9    ILE B CD1 1 
ATOM   3402 N  N   . GLN B 1 8   ? 119.385 -26.228 32.464  1.00 8.89  ? 10   GLN B N   1 
ATOM   3403 C  CA  . GLN B 1 8   ? 118.230 -25.348 32.340  1.00 8.97  ? 10   GLN B CA  1 
ATOM   3404 C  C   . GLN B 1 8   ? 118.276 -24.202 33.341  1.00 9.13  ? 10   GLN B C   1 
ATOM   3405 O  O   . GLN B 1 8   ? 118.578 -24.402 34.518  1.00 9.20  ? 10   GLN B O   1 
ATOM   3406 C  CB  . GLN B 1 8   ? 116.927 -26.134 32.481  1.00 8.93  ? 10   GLN B CB  1 
ATOM   3407 C  CG  . GLN B 1 8   ? 116.700 -27.132 31.359  1.00 8.74  ? 10   GLN B CG  1 
ATOM   3408 C  CD  . GLN B 1 8   ? 115.253 -27.566 31.252  1.00 8.94  ? 10   GLN B CD  1 
ATOM   3409 O  OE1 . GLN B 1 8   ? 114.346 -26.733 31.224  1.00 8.53  ? 10   GLN B OE1 1 
ATOM   3410 N  NE2 . GLN B 1 8   ? 115.028 -28.875 31.196  1.00 9.25  ? 10   GLN B NE2 1 
ATOM   3411 N  N   . GLY B 1 9   ? 117.924 -23.009 32.876  1.00 9.12  ? 11   GLY B N   1 
ATOM   3412 C  CA  . GLY B 1 9   ? 118.225 -21.777 33.601  1.00 9.28  ? 11   GLY B CA  1 
ATOM   3413 C  C   . GLY B 1 9   ? 117.596 -21.666 34.978  1.00 9.46  ? 11   GLY B C   1 
ATOM   3414 O  O   . GLY B 1 9   ? 118.202 -21.111 35.893  1.00 9.74  ? 11   GLY B O   1 
ATOM   3415 N  N   . ASP B 1 10  ? 116.374 -22.171 35.129  1.00 9.63  ? 12   ASP B N   1 
ATOM   3416 C  CA  . ASP B 1 10  ? 115.633 -21.993 36.382  1.00 10.00 ? 12   ASP B CA  1 
ATOM   3417 C  C   . ASP B 1 10  ? 116.323 -22.701 37.545  1.00 10.06 ? 12   ASP B C   1 
ATOM   3418 O  O   . ASP B 1 10  ? 116.149 -22.327 38.704  1.00 11.04 ? 12   ASP B O   1 
ATOM   3419 C  CB  . ASP B 1 10  ? 114.186 -22.485 36.242  1.00 10.18 ? 12   ASP B CB  1 
ATOM   3420 C  CG  . ASP B 1 10  ? 113.291 -22.022 37.388  1.00 11.24 ? 12   ASP B CG  1 
ATOM   3421 O  OD1 . ASP B 1 10  ? 113.407 -20.849 37.805  1.00 11.52 ? 12   ASP B OD1 1 
ATOM   3422 O  OD2 . ASP B 1 10  ? 112.432 -22.816 37.840  1.00 11.15 ? 12   ASP B OD2 1 
ATOM   3423 N  N   . ILE B 1 11  ? 117.078 -23.748 37.234  1.00 10.19 ? 13   ILE B N   1 
ATOM   3424 C  CA  . ILE B 1 11  ? 117.695 -24.574 38.266  1.00 10.45 ? 13   ILE B CA  1 
ATOM   3425 C  C   . ILE B 1 11  ? 118.707 -23.805 39.117  1.00 11.32 ? 13   ILE B C   1 
ATOM   3426 O  O   . ILE B 1 11  ? 118.658 -23.852 40.351  1.00 11.82 ? 13   ILE B O   1 
ATOM   3427 C  CB  . ILE B 1 11  ? 118.360 -25.823 37.661  1.00 10.13 ? 13   ILE B CB  1 
ATOM   3428 C  CG1 . ILE B 1 11  ? 117.319 -26.670 36.926  1.00 9.69  ? 13   ILE B CG1 1 
ATOM   3429 C  CG2 . ILE B 1 11  ? 119.048 -26.641 38.742  1.00 10.07 ? 13   ILE B CG2 1 
ATOM   3430 C  CD1 . ILE B 1 11  ? 117.912 -27.679 35.971  1.00 9.30  ? 13   ILE B CD1 1 
ATOM   3431 N  N   . LEU B 1 12  ? 119.599 -23.071 38.459  1.00 11.76 ? 14   LEU B N   1 
ATOM   3432 C  CA  . LEU B 1 12  ? 120.723 -22.441 39.149  1.00 13.05 ? 14   LEU B CA  1 
ATOM   3433 C  C   . LEU B 1 12  ? 120.603 -20.923 39.284  1.00 14.59 ? 14   LEU B C   1 
ATOM   3434 O  O   . LEU B 1 12  ? 121.230 -20.329 40.162  1.00 14.49 ? 14   LEU B O   1 
ATOM   3435 C  CB  . LEU B 1 12  ? 122.048 -22.807 38.475  1.00 13.33 ? 14   LEU B CB  1 
ATOM   3436 C  CG  . LEU B 1 12  ? 122.481 -24.270 38.592  1.00 13.42 ? 14   LEU B CG  1 
ATOM   3437 C  CD1 . LEU B 1 12  ? 123.881 -24.457 38.027  1.00 13.63 ? 14   LEU B CD1 1 
ATOM   3438 C  CD2 . LEU B 1 12  ? 122.407 -24.739 40.039  1.00 12.76 ? 14   LEU B CD2 1 
ATOM   3439 N  N   . VAL B 1 13  ? 119.823 -20.289 38.413  1.00 14.83 ? 15   VAL B N   1 
ATOM   3440 C  CA  . VAL B 1 13  ? 119.734 -18.829 38.429  1.00 15.91 ? 15   VAL B CA  1 
ATOM   3441 C  C   . VAL B 1 13  ? 118.322 -18.283 38.637  1.00 16.26 ? 15   VAL B C   1 
ATOM   3442 O  O   . VAL B 1 13  ? 118.157 -17.150 39.077  1.00 17.83 ? 15   VAL B O   1 
ATOM   3443 C  CB  . VAL B 1 13  ? 120.359 -18.186 37.173  1.00 16.69 ? 15   VAL B CB  1 
ATOM   3444 C  CG1 . VAL B 1 13  ? 121.782 -18.681 36.966  1.00 17.56 ? 15   VAL B CG1 1 
ATOM   3445 C  CG2 . VAL B 1 13  ? 119.507 -18.457 35.946  1.00 17.71 ? 15   VAL B CG2 1 
ATOM   3446 N  N   . GLY B 1 14  ? 117.309 -19.074 38.302  1.00 15.50 ? 16   GLY B N   1 
ATOM   3447 C  CA  . GLY B 1 14  ? 115.932 -18.580 38.280  1.00 16.55 ? 16   GLY B CA  1 
ATOM   3448 C  C   . GLY B 1 14  ? 115.593 -17.904 36.963  1.00 17.73 ? 16   GLY B C   1 
ATOM   3449 O  O   . GLY B 1 14  ? 116.482 -17.588 36.176  1.00 18.63 ? 16   GLY B O   1 
ATOM   3450 N  N   . MET B 1 15  ? 114.307 -17.678 36.719  1.00 18.31 ? 17   MET B N   1 
ATOM   3451 C  CA  . MET B 1 15  ? 113.849 -17.203 35.414  1.00 20.38 ? 17   MET B CA  1 
ATOM   3452 C  C   . MET B 1 15  ? 114.085 -15.705 35.195  1.00 22.77 ? 17   MET B C   1 
ATOM   3453 O  O   . MET B 1 15  ? 114.197 -15.248 34.057  1.00 24.49 ? 17   MET B O   1 
ATOM   3454 C  CB  . MET B 1 15  ? 112.372 -17.541 35.207  1.00 19.12 ? 17   MET B CB  1 
ATOM   3455 C  CG  . MET B 1 15  ? 112.097 -19.021 34.991  1.00 18.81 ? 17   MET B CG  1 
ATOM   3456 S  SD  . MET B 1 15  ? 113.190 -19.754 33.757  1.00 19.52 ? 17   MET B SD  1 
ATOM   3457 C  CE  . MET B 1 15  ? 112.017 -20.668 32.759  1.00 17.33 ? 17   MET B CE  1 
ATOM   3458 N  N   . HIS B 1 16  ? 114.110 -14.941 36.282  1.00 24.55 ? 18   HIS B N   1 
ATOM   3459 C  CA  . HIS B 1 16  ? 114.429 -13.517 36.207  1.00 29.24 ? 18   HIS B CA  1 
ATOM   3460 C  C   . HIS B 1 16  ? 113.376 -12.715 35.445  1.00 25.63 ? 18   HIS B C   1 
ATOM   3461 O  O   . HIS B 1 16  ? 113.715 -11.791 34.706  1.00 27.86 ? 18   HIS B O   1 
ATOM   3462 C  CB  . HIS B 1 16  ? 115.797 -13.308 35.550  1.00 31.99 ? 18   HIS B CB  1 
ATOM   3463 C  CG  . HIS B 1 16  ? 116.946 -13.362 36.508  1.00 37.86 ? 18   HIS B CG  1 
ATOM   3464 N  ND1 . HIS B 1 16  ? 117.958 -14.291 36.404  1.00 42.38 ? 18   HIS B ND1 1 
ATOM   3465 C  CD2 . HIS B 1 16  ? 117.245 -12.598 37.586  1.00 39.37 ? 18   HIS B CD2 1 
ATOM   3466 C  CE1 . HIS B 1 16  ? 118.831 -14.098 37.377  1.00 41.69 ? 18   HIS B CE1 1 
ATOM   3467 N  NE2 . HIS B 1 16  ? 118.422 -13.077 38.108  1.00 40.91 ? 18   HIS B NE2 1 
ATOM   3468 N  N   . LYS B 1 17  ? 112.105 -13.073 35.612  1.00 23.10 ? 19   LYS B N   1 
ATOM   3469 C  CA  . LYS B 1 17  ? 111.026 -12.380 34.909  1.00 19.43 ? 19   LYS B CA  1 
ATOM   3470 C  C   . LYS B 1 17  ? 109.863 -12.031 35.835  1.00 18.95 ? 19   LYS B C   1 
ATOM   3471 O  O   . LYS B 1 17  ? 109.684 -12.649 36.884  1.00 17.01 ? 19   LYS B O   1 
ATOM   3472 C  CB  . LYS B 1 17  ? 110.527 -13.215 33.726  1.00 19.48 ? 19   LYS B CB  1 
ATOM   3473 C  CG  . LYS B 1 17  ? 111.604 -13.565 32.710  1.00 19.99 ? 19   LYS B CG  1 
ATOM   3474 C  CD  . LYS B 1 17  ? 111.968 -12.364 31.851  1.00 20.85 ? 19   LYS B CD  1 
ATOM   3475 C  CE  . LYS B 1 17  ? 112.788 -12.784 30.642  1.00 21.87 ? 19   LYS B CE  1 
ATOM   3476 N  NZ  . LYS B 1 17  ? 112.965 -11.672 29.667  1.00 21.53 ? 19   LYS B NZ  1 
ATOM   3477 N  N   . GLN B 1 18  ? 109.066 -11.046 35.428  1.00 17.37 ? 20   GLN B N   1 
ATOM   3478 C  CA  . GLN B 1 18  ? 107.951 -10.570 36.237  1.00 17.53 ? 20   GLN B CA  1 
ATOM   3479 C  C   . GLN B 1 18  ? 106.846 -11.614 36.341  1.00 15.16 ? 20   GLN B C   1 
ATOM   3480 O  O   . GLN B 1 18  ? 106.227 -11.769 37.394  1.00 14.44 ? 20   GLN B O   1 
ATOM   3481 C  CB  . GLN B 1 18  ? 107.381 -9.273  35.654  1.00 19.68 ? 20   GLN B CB  1 
ATOM   3482 C  CG  . GLN B 1 18  ? 108.251 -8.051  35.899  1.00 22.73 ? 20   GLN B CG  1 
ATOM   3483 C  CD  . GLN B 1 18  ? 108.280 -7.648  37.360  1.00 24.65 ? 20   GLN B CD  1 
ATOM   3484 O  OE1 . GLN B 1 18  ? 107.240 -7.574  38.018  1.00 29.48 ? 20   GLN B OE1 1 
ATOM   3485 N  NE2 . GLN B 1 18  ? 109.475 -7.396  37.879  1.00 26.62 ? 20   GLN B NE2 1 
ATOM   3486 N  N   . LYS B 1 19  ? 106.577 -12.300 35.235  1.00 12.71 ? 21   LYS B N   1 
ATOM   3487 C  CA  . LYS B 1 19  ? 105.488 -13.269 35.186  1.00 12.03 ? 21   LYS B CA  1 
ATOM   3488 C  C   . LYS B 1 19  ? 106.024 -14.664 34.889  1.00 11.00 ? 21   LYS B C   1 
ATOM   3489 O  O   . LYS B 1 19  ? 107.004 -14.822 34.157  1.00 10.71 ? 21   LYS B O   1 
ATOM   3490 C  CB  . LYS B 1 19  ? 104.454 -12.877 34.124  1.00 12.29 ? 21   LYS B CB  1 
ATOM   3491 C  CG  . LYS B 1 19  ? 104.009 -11.423 34.175  1.00 13.30 ? 21   LYS B CG  1 
ATOM   3492 C  CD  . LYS B 1 19  ? 103.209 -11.122 35.433  1.00 14.87 ? 21   LYS B CD  1 
ATOM   3493 C  CE  . LYS B 1 19  ? 102.677 -9.697  35.416  1.00 18.12 ? 21   LYS B CE  1 
ATOM   3494 N  NZ  . LYS B 1 19  ? 101.904 -9.391  36.651  1.00 18.06 ? 21   LYS B NZ  1 
ATOM   3495 N  N   . GLN B 1 20  ? 105.384 -15.673 35.468  1.00 11.06 ? 22   GLN B N   1 
ATOM   3496 C  CA  . GLN B 1 20  ? 105.631 -17.058 35.078  1.00 10.75 ? 22   GLN B CA  1 
ATOM   3497 C  C   . GLN B 1 20  ? 104.316 -17.804 34.933  1.00 10.24 ? 22   GLN B C   1 
ATOM   3498 O  O   . GLN B 1 20  ? 103.345 -17.513 35.631  1.00 10.81 ? 22   GLN B O   1 
ATOM   3499 C  CB  . GLN B 1 20  ? 106.521 -17.767 36.106  1.00 11.23 ? 22   GLN B CB  1 
ATOM   3500 C  CG  . GLN B 1 20  ? 107.937 -17.221 36.186  1.00 12.27 ? 22   GLN B CG  1 
ATOM   3501 C  CD  . GLN B 1 20  ? 108.874 -18.110 36.992  1.00 12.45 ? 22   GLN B CD  1 
ATOM   3502 O  OE1 . GLN B 1 20  ? 109.943 -17.674 37.412  1.00 15.20 ? 22   GLN B OE1 1 
ATOM   3503 N  NE2 . GLN B 1 20  ? 108.481 -19.364 37.201  1.00 12.68 ? 22   GLN B NE2 1 
ATOM   3504 N  N   . LEU B 1 21  ? 104.294 -18.769 34.023  1.00 9.97  ? 23   LEU B N   1 
ATOM   3505 C  CA  . LEU B 1 21  ? 103.205 -19.727 33.943  1.00 9.67  ? 23   LEU B CA  1 
ATOM   3506 C  C   . LEU B 1 21  ? 103.758 -21.131 34.150  1.00 9.42  ? 23   LEU B C   1 
ATOM   3507 O  O   . LEU B 1 21  ? 104.795 -21.482 33.589  1.00 9.71  ? 23   LEU B O   1 
ATOM   3508 C  CB  . LEU B 1 21  ? 102.522 -19.637 32.578  1.00 10.07 ? 23   LEU B CB  1 
ATOM   3509 C  CG  . LEU B 1 21  ? 101.367 -20.614 32.343  1.00 10.52 ? 23   LEU B CG  1 
ATOM   3510 C  CD1 . LEU B 1 21  ? 100.166 -20.211 33.177  1.00 10.82 ? 23   LEU B CD1 1 
ATOM   3511 C  CD2 . LEU B 1 21  ? 101.004 -20.669 30.865  1.00 11.30 ? 23   LEU B CD2 1 
ATOM   3512 N  N   . PHE B 1 22  ? 103.082 -21.917 34.982  1.00 9.24  ? 24   PHE B N   1 
ATOM   3513 C  CA  . PHE B 1 22  ? 103.348 -23.348 35.079  1.00 9.02  ? 24   PHE B CA  1 
ATOM   3514 C  C   . PHE B 1 22  ? 102.266 -24.110 34.323  1.00 8.84  ? 24   PHE B C   1 
ATOM   3515 O  O   . PHE B 1 22  ? 101.092 -24.067 34.691  1.00 9.14  ? 24   PHE B O   1 
ATOM   3516 C  CB  . PHE B 1 22  ? 103.383 -23.787 36.549  1.00 9.03  ? 24   PHE B CB  1 
ATOM   3517 C  CG  . PHE B 1 22  ? 104.478 -23.137 37.349  1.00 9.04  ? 24   PHE B CG  1 
ATOM   3518 C  CD1 . PHE B 1 22  ? 104.265 -21.922 37.984  1.00 8.98  ? 24   PHE B CD1 1 
ATOM   3519 C  CD2 . PHE B 1 22  ? 105.724 -23.735 37.456  1.00 9.01  ? 24   PHE B CD2 1 
ATOM   3520 C  CE1 . PHE B 1 22  ? 105.270 -21.325 38.723  1.00 9.23  ? 24   PHE B CE1 1 
ATOM   3521 C  CE2 . PHE B 1 22  ? 106.739 -23.136 38.182  1.00 9.08  ? 24   PHE B CE2 1 
ATOM   3522 C  CZ  . PHE B 1 22  ? 106.510 -21.930 38.818  1.00 9.35  ? 24   PHE B CZ  1 
ATOM   3523 N  N   . TYR B 1 23  ? 102.664 -24.772 33.243  1.00 8.89  ? 25   TYR B N   1 
ATOM   3524 C  CA  . TYR B 1 23  ? 101.723 -25.414 32.331  1.00 8.61  ? 25   TYR B CA  1 
ATOM   3525 C  C   . TYR B 1 23  ? 101.890 -26.923 32.452  1.00 8.39  ? 25   TYR B C   1 
ATOM   3526 O  O   . TYR B 1 23  ? 102.890 -27.474 32.002  1.00 7.67  ? 25   TYR B O   1 
ATOM   3527 C  CB  . TYR B 1 23  ? 102.021 -24.966 30.893  1.00 8.85  ? 25   TYR B CB  1 
ATOM   3528 C  CG  . TYR B 1 23  ? 101.060 -25.472 29.834  1.00 9.64  ? 25   TYR B CG  1 
ATOM   3529 C  CD1 . TYR B 1 23  ? 101.262 -26.697 29.208  1.00 10.13 ? 25   TYR B CD1 1 
ATOM   3530 C  CD2 . TYR B 1 23  ? 100.010 -24.678 29.387  1.00 10.38 ? 25   TYR B CD2 1 
ATOM   3531 C  CE1 . TYR B 1 23  ? 100.414 -27.139 28.205  1.00 10.19 ? 25   TYR B CE1 1 
ATOM   3532 C  CE2 . TYR B 1 23  ? 99.157  -25.112 28.385  1.00 10.41 ? 25   TYR B CE2 1 
ATOM   3533 C  CZ  . TYR B 1 23  ? 99.363  -26.341 27.797  1.00 11.17 ? 25   TYR B CZ  1 
ATOM   3534 O  OH  . TYR B 1 23  ? 98.521  -26.770 26.792  1.00 12.33 ? 25   TYR B OH  1 
ATOM   3535 N  N   . PHE B 1 24  ? 100.935 -27.581 33.103  1.00 8.39  ? 26   PHE B N   1 
ATOM   3536 C  CA  . PHE B 1 24  ? 101.060 -29.009 33.388  1.00 8.58  ? 26   PHE B CA  1 
ATOM   3537 C  C   . PHE B 1 24  ? 100.321 -29.822 32.333  1.00 8.62  ? 26   PHE B C   1 
ATOM   3538 O  O   . PHE B 1 24  ? 99.136  -29.599 32.087  1.00 8.79  ? 26   PHE B O   1 
ATOM   3539 C  CB  . PHE B 1 24  ? 100.522 -29.335 34.783  1.00 8.62  ? 26   PHE B CB  1 
ATOM   3540 C  CG  . PHE B 1 24  ? 101.233 -28.611 35.891  1.00 8.65  ? 26   PHE B CG  1 
ATOM   3541 C  CD1 . PHE B 1 24  ? 102.404 -29.122 36.432  1.00 8.54  ? 26   PHE B CD1 1 
ATOM   3542 C  CD2 . PHE B 1 24  ? 100.747 -27.405 36.372  1.00 8.58  ? 26   PHE B CD2 1 
ATOM   3543 C  CE1 . PHE B 1 24  ? 103.074 -28.446 37.439  1.00 8.26  ? 26   PHE B CE1 1 
ATOM   3544 C  CE2 . PHE B 1 24  ? 101.408 -26.728 37.383  1.00 8.51  ? 26   PHE B CE2 1 
ATOM   3545 C  CZ  . PHE B 1 24  ? 102.575 -27.248 37.913  1.00 8.32  ? 26   PHE B CZ  1 
ATOM   3546 N  N   . PHE B 1 25  ? 101.027 -30.756 31.703  1.00 8.88  ? 27   PHE B N   1 
ATOM   3547 C  CA  . PHE B 1 25  ? 100.516 -31.408 30.499  1.00 9.31  ? 27   PHE B CA  1 
ATOM   3548 C  C   . PHE B 1 25  ? 100.560 -32.932 30.572  1.00 9.38  ? 27   PHE B C   1 
ATOM   3549 O  O   . PHE B 1 25  ? 101.302 -33.507 31.371  1.00 8.66  ? 27   PHE B O   1 
ATOM   3550 C  CB  . PHE B 1 25  ? 101.254 -30.911 29.251  1.00 9.36  ? 27   PHE B CB  1 
ATOM   3551 C  CG  . PHE B 1 25  ? 102.718 -31.265 29.222  1.00 9.34  ? 27   PHE B CG  1 
ATOM   3552 C  CD1 . PHE B 1 25  ? 103.146 -32.453 28.649  1.00 9.54  ? 27   PHE B CD1 1 
ATOM   3553 C  CD2 . PHE B 1 25  ? 103.668 -30.395 29.736  1.00 9.40  ? 27   PHE B CD2 1 
ATOM   3554 C  CE1 . PHE B 1 25  ? 104.490 -32.775 28.601  1.00 9.34  ? 27   PHE B CE1 1 
ATOM   3555 C  CE2 . PHE B 1 25  ? 105.016 -30.707 29.688  1.00 9.43  ? 27   PHE B CE2 1 
ATOM   3556 C  CZ  . PHE B 1 25  ? 105.427 -31.906 29.128  1.00 9.51  ? 27   PHE B CZ  1 
ATOM   3557 N  N   . ALA B 1 26  ? 99.717  -33.572 29.766  1.00 9.89  ? 28   ALA B N   1 
ATOM   3558 C  CA  . ALA B 1 26  ? 99.855  -34.990 29.458  1.00 10.80 ? 28   ALA B CA  1 
ATOM   3559 C  C   . ALA B 1 26  ? 100.310 -35.166 28.014  1.00 11.71 ? 28   ALA B C   1 
ATOM   3560 O  O   . ALA B 1 26  ? 100.034 -34.324 27.159  1.00 12.00 ? 28   ALA B O   1 
ATOM   3561 C  CB  . ALA B 1 26  ? 98.532  -35.714 29.680  1.00 11.09 ? 28   ALA B CB  1 
ATOM   3562 N  N   . ILE B 1 27  ? 101.032 -36.252 27.760  1.00 12.07 ? 29   ILE B N   1 
ATOM   3563 C  CA  . ILE B 1 27  ? 101.438 -36.622 26.411  1.00 13.10 ? 29   ILE B CA  1 
ATOM   3564 C  C   . ILE B 1 27  ? 100.475 -37.674 25.862  1.00 15.01 ? 29   ILE B C   1 
ATOM   3565 O  O   . ILE B 1 27  ? 100.229 -38.691 26.511  1.00 15.14 ? 29   ILE B O   1 
ATOM   3566 C  CB  . ILE B 1 27  ? 102.870 -37.199 26.409  1.00 13.17 ? 29   ILE B CB  1 
ATOM   3567 C  CG1 . ILE B 1 27  ? 103.873 -36.129 26.851  1.00 13.07 ? 29   ILE B CG1 1 
ATOM   3568 C  CG2 . ILE B 1 27  ? 103.228 -37.749 25.034  1.00 12.60 ? 29   ILE B CG2 1 
ATOM   3569 C  CD1 . ILE B 1 27  ? 105.171 -36.685 27.396  1.00 13.30 ? 29   ILE B CD1 1 
ATOM   3570 N  N   . ASN B 1 28  ? 99.926  -37.426 24.675  1.00 16.42 ? 30   ASN B N   1 
ATOM   3571 C  CA  . ASN B 1 28  ? 98.930  -38.328 24.090  1.00 19.08 ? 30   ASN B CA  1 
ATOM   3572 C  C   . ASN B 1 28  ? 99.507  -39.246 23.020  1.00 21.70 ? 30   ASN B C   1 
ATOM   3573 O  O   . ASN B 1 28  ? 99.072  -40.388 22.867  1.00 26.47 ? 30   ASN B O   1 
ATOM   3574 C  CB  . ASN B 1 28  ? 97.762  -37.535 23.503  1.00 18.28 ? 30   ASN B CB  1 
ATOM   3575 C  CG  . ASN B 1 28  ? 97.080  -36.664 24.533  1.00 19.00 ? 30   ASN B CG  1 
ATOM   3576 O  OD1 . ASN B 1 28  ? 96.849  -37.092 25.661  1.00 21.83 ? 30   ASN B OD1 1 
ATOM   3577 N  ND2 . ASN B 1 28  ? 96.802  -35.418 24.167  1.00 18.38 ? 30   ASN B ND2 1 
ATOM   3578 N  N   . ASP B 1 29  ? 100.460 -38.725 22.259  1.00 19.79 ? 31   ASP B N   1 
ATOM   3579 C  CA  . ASP B 1 29  ? 100.968 -39.406 21.078  1.00 19.43 ? 31   ASP B CA  1 
ATOM   3580 C  C   . ASP B 1 29  ? 102.477 -39.213 21.009  1.00 18.62 ? 31   ASP B C   1 
ATOM   3581 O  O   . ASP B 1 29  ? 102.954 -38.204 20.490  1.00 17.07 ? 31   ASP B O   1 
ATOM   3582 C  CB  . ASP B 1 29  ? 100.293 -38.838 19.828  1.00 20.51 ? 31   ASP B CB  1 
ATOM   3583 C  CG  . ASP B 1 29  ? 100.943 -39.302 18.542  1.00 22.18 ? 31   ASP B CG  1 
ATOM   3584 O  OD1 . ASP B 1 29  ? 101.930 -40.066 18.595  1.00 22.18 ? 31   ASP B OD1 1 
ATOM   3585 O  OD2 . ASP B 1 29  ? 100.467 -38.883 17.466  1.00 27.63 ? 31   ASP B OD2 1 
ATOM   3586 N  N   . PRO B 1 30  ? 103.230 -40.149 21.609  1.00 18.08 ? 32   PRO B N   1 
ATOM   3587 C  CA  . PRO B 1 30  ? 104.661 -40.003 21.849  1.00 17.48 ? 32   PRO B CA  1 
ATOM   3588 C  C   . PRO B 1 30  ? 105.450 -39.640 20.595  1.00 15.99 ? 32   PRO B C   1 
ATOM   3589 O  O   . PRO B 1 30  ? 106.296 -38.745 20.637  1.00 14.80 ? 32   PRO B O   1 
ATOM   3590 C  CB  . PRO B 1 30  ? 105.066 -41.387 22.352  1.00 17.39 ? 32   PRO B CB  1 
ATOM   3591 C  CG  . PRO B 1 30  ? 103.849 -41.883 23.052  1.00 17.56 ? 32   PRO B CG  1 
ATOM   3592 C  CD  . PRO B 1 30  ? 102.671 -41.325 22.300  1.00 18.82 ? 32   PRO B CD  1 
ATOM   3593 N  N   . ALA B 1 31  ? 105.184 -40.330 19.490  1.00 15.48 ? 33   ALA B N   1 
ATOM   3594 C  CA  . ALA B 1 31  ? 105.932 -40.096 18.259  1.00 15.30 ? 33   ALA B CA  1 
ATOM   3595 C  C   . ALA B 1 31  ? 105.776 -38.652 17.790  1.00 14.35 ? 33   ALA B C   1 
ATOM   3596 O  O   . ALA B 1 31  ? 106.755 -37.987 17.451  1.00 13.56 ? 33   ALA B O   1 
ATOM   3597 C  CB  . ALA B 1 31  ? 105.494 -41.067 17.170  1.00 15.66 ? 33   ALA B CB  1 
ATOM   3598 N  N   . THR B 1 32  ? 104.539 -38.167 17.784  1.00 14.35 ? 34   THR B N   1 
ATOM   3599 C  CA  . THR B 1 32  ? 104.264 -36.782 17.412  1.00 13.86 ? 34   THR B CA  1 
ATOM   3600 C  C   . THR B 1 32  ? 104.870 -35.813 18.425  1.00 12.93 ? 34   THR B C   1 
ATOM   3601 O  O   . THR B 1 32  ? 105.544 -34.858 18.049  1.00 11.69 ? 34   THR B O   1 
ATOM   3602 C  CB  . THR B 1 32  ? 102.750 -36.521 17.288  1.00 15.79 ? 34   THR B CB  1 
ATOM   3603 O  OG1 . THR B 1 32  ? 102.187 -37.423 16.327  1.00 15.32 ? 34   THR B OG1 1 
ATOM   3604 C  CG2 . THR B 1 32  ? 102.483 -35.084 16.853  1.00 14.24 ? 34   THR B CG2 1 
ATOM   3605 N  N   . PHE B 1 33  ? 104.640 -36.075 19.710  1.00 12.64 ? 35   PHE B N   1 
ATOM   3606 C  CA  . PHE B 1 33  ? 105.221 -35.258 20.776  1.00 11.78 ? 35   PHE B CA  1 
ATOM   3607 C  C   . PHE B 1 33  ? 106.734 -35.120 20.611  1.00 12.16 ? 35   PHE B C   1 
ATOM   3608 O  O   . PHE B 1 33  ? 107.281 -34.023 20.699  1.00 10.92 ? 35   PHE B O   1 
ATOM   3609 C  CB  . PHE B 1 33  ? 104.899 -35.855 22.150  1.00 11.93 ? 35   PHE B CB  1 
ATOM   3610 C  CG  . PHE B 1 33  ? 105.309 -34.980 23.303  1.00 12.45 ? 35   PHE B CG  1 
ATOM   3611 C  CD1 . PHE B 1 33  ? 104.448 -34.010 23.794  1.00 12.76 ? 35   PHE B CD1 1 
ATOM   3612 C  CD2 . PHE B 1 33  ? 106.559 -35.116 23.885  1.00 13.21 ? 35   PHE B CD2 1 
ATOM   3613 C  CE1 . PHE B 1 33  ? 104.828 -33.194 24.845  1.00 12.93 ? 35   PHE B CE1 1 
ATOM   3614 C  CE2 . PHE B 1 33  ? 106.944 -34.303 24.937  1.00 13.24 ? 35   PHE B CE2 1 
ATOM   3615 C  CZ  . PHE B 1 33  ? 106.080 -33.334 25.409  1.00 13.19 ? 35   PHE B CZ  1 
ATOM   3616 N  N   . LYS B 1 34  ? 107.406 -36.242 20.373  1.00 12.08 ? 36   LYS B N   1 
ATOM   3617 C  CA  . LYS B 1 34  ? 108.860 -36.257 20.284  1.00 12.10 ? 36   LYS B CA  1 
ATOM   3618 C  C   . LYS B 1 34  ? 109.386 -35.372 19.162  1.00 11.66 ? 36   LYS B C   1 
ATOM   3619 O  O   . LYS B 1 34  ? 110.393 -34.692 19.328  1.00 10.93 ? 36   LYS B O   1 
ATOM   3620 C  CB  . LYS B 1 34  ? 109.376 -37.684 20.103  1.00 12.47 ? 36   LYS B CB  1 
ATOM   3621 C  CG  . LYS B 1 34  ? 109.337 -38.524 21.368  1.00 13.76 ? 36   LYS B CG  1 
ATOM   3622 C  CD  . LYS B 1 34  ? 109.577 -39.990 21.035  1.00 15.52 ? 36   LYS B CD  1 
ATOM   3623 C  CE  . LYS B 1 34  ? 109.741 -40.830 22.290  1.00 16.39 ? 36   LYS B CE  1 
ATOM   3624 N  NZ  . LYS B 1 34  ? 111.052 -40.560 22.946  1.00 16.97 ? 36   LYS B NZ  1 
ATOM   3625 N  N   . THR B 1 35  ? 108.738 -35.422 18.002  1.00 12.33 ? 37   THR B N   1 
ATOM   3626 C  CA  . THR B 1 35  ? 109.164 -34.598 16.875  1.00 12.56 ? 37   THR B CA  1 
ATOM   3627 C  C   . THR B 1 35  ? 109.182 -33.121 17.253  1.00 11.89 ? 37   THR B C   1 
ATOM   3628 O  O   . THR B 1 35  ? 110.149 -32.409 16.979  1.00 11.45 ? 37   THR B O   1 
ATOM   3629 C  CB  . THR B 1 35  ? 108.258 -34.789 15.643  1.00 14.14 ? 37   THR B CB  1 
ATOM   3630 O  OG1 . THR B 1 35  ? 108.306 -36.154 15.221  1.00 17.20 ? 37   THR B OG1 1 
ATOM   3631 C  CG2 . THR B 1 35  ? 108.725 -33.909 14.505  1.00 16.11 ? 37   THR B CG2 1 
ATOM   3632 N  N   . HIS B 1 36  ? 108.103 -32.660 17.876  1.00 11.38 ? 38   HIS B N   1 
ATOM   3633 C  CA  . HIS B 1 36  ? 107.980 -31.253 18.223  1.00 11.07 ? 38   HIS B CA  1 
ATOM   3634 C  C   . HIS B 1 36  ? 108.796 -30.876 19.460  1.00 11.22 ? 38   HIS B C   1 
ATOM   3635 O  O   . HIS B 1 36  ? 109.245 -29.740 19.588  1.00 11.15 ? 38   HIS B O   1 
ATOM   3636 C  CB  . HIS B 1 36  ? 106.510 -30.866 18.391  1.00 11.44 ? 38   HIS B CB  1 
ATOM   3637 C  CG  . HIS B 1 36  ? 105.709 -31.013 17.135  1.00 11.27 ? 38   HIS B CG  1 
ATOM   3638 N  ND1 . HIS B 1 36  ? 105.936 -30.241 16.017  1.00 11.41 ? 38   HIS B ND1 1 
ATOM   3639 C  CD2 . HIS B 1 36  ? 104.734 -31.889 16.796  1.00 11.43 ? 38   HIS B CD2 1 
ATOM   3640 C  CE1 . HIS B 1 36  ? 105.109 -30.609 15.055  1.00 11.29 ? 38   HIS B CE1 1 
ATOM   3641 N  NE2 . HIS B 1 36  ? 104.374 -31.613 15.500  1.00 11.37 ? 38   HIS B NE2 1 
ATOM   3642 N  N   . LEU B 1 37  ? 109.025 -31.840 20.349  1.00 11.26 ? 39   LEU B N   1 
ATOM   3643 C  CA  . LEU B 1 37  ? 109.953 -31.625 21.458  1.00 11.28 ? 39   LEU B CA  1 
ATOM   3644 C  C   . LEU B 1 37  ? 111.329 -31.236 20.917  1.00 12.02 ? 39   LEU B C   1 
ATOM   3645 O  O   . LEU B 1 37  ? 111.961 -30.295 21.404  1.00 12.04 ? 39   LEU B O   1 
ATOM   3646 C  CB  . LEU B 1 37  ? 110.053 -32.877 22.334  1.00 10.63 ? 39   LEU B CB  1 
ATOM   3647 C  CG  . LEU B 1 37  ? 110.816 -32.724 23.654  1.00 10.60 ? 39   LEU B CG  1 
ATOM   3648 C  CD1 . LEU B 1 37  ? 110.131 -31.721 24.578  1.00 9.88  ? 39   LEU B CD1 1 
ATOM   3649 C  CD2 . LEU B 1 37  ? 110.978 -34.068 24.344  1.00 9.87  ? 39   LEU B CD2 1 
ATOM   3650 N  N   . ALA B 1 38  ? 111.759 -31.924 19.865  1.00 12.32 ? 40   ALA B N   1 
ATOM   3651 C  CA  . ALA B 1 38  ? 113.086 -31.705 19.296  1.00 12.96 ? 40   ALA B CA  1 
ATOM   3652 C  C   . ALA B 1 38  ? 113.148 -30.474 18.397  1.00 13.66 ? 40   ALA B C   1 
ATOM   3653 O  O   . ALA B 1 38  ? 114.101 -29.701 18.462  1.00 13.23 ? 40   ALA B O   1 
ATOM   3654 C  CB  . ALA B 1 38  ? 113.552 -32.938 18.537  1.00 13.88 ? 40   ALA B CB  1 
ATOM   3655 N  N   A SER B 1 39  ? 112.123 -30.295 17.570  0.50 13.72 ? 41   SER B N   1 
ATOM   3656 N  N   B SER B 1 39  ? 112.157 -30.319 17.524  0.50 13.49 ? 41   SER B N   1 
ATOM   3657 C  CA  A SER B 1 39  ? 112.157 -29.271 16.532  0.50 14.35 ? 41   SER B CA  1 
ATOM   3658 C  CA  B SER B 1 39  ? 112.179 -29.234 16.545  0.50 14.01 ? 41   SER B CA  1 
ATOM   3659 C  C   A SER B 1 39  ? 111.655 -27.914 17.019  0.50 14.51 ? 41   SER B C   1 
ATOM   3660 C  C   B SER B 1 39  ? 111.847 -27.893 17.188  0.50 14.05 ? 41   SER B C   1 
ATOM   3661 O  O   A SER B 1 39  ? 111.973 -26.884 16.427  0.50 15.22 ? 41   SER B O   1 
ATOM   3662 O  O   B SER B 1 39  ? 112.455 -26.872 16.870  0.50 14.44 ? 41   SER B O   1 
ATOM   3663 C  CB  A SER B 1 39  ? 111.376 -29.723 15.293  0.50 14.24 ? 41   SER B CB  1 
ATOM   3664 C  CB  B SER B 1 39  ? 111.203 -29.515 15.401  0.50 14.01 ? 41   SER B CB  1 
ATOM   3665 O  OG  A SER B 1 39  ? 109.996 -29.880 15.579  0.50 14.24 ? 41   SER B OG  1 
ATOM   3666 O  OG  B SER B 1 39  ? 111.432 -30.792 14.836  0.50 13.19 ? 41   SER B OG  1 
ATOM   3667 N  N   . ASP B 1 40  ? 110.886 -27.905 18.105  1.00 14.33 ? 42   ASP B N   1 
ATOM   3668 C  CA  . ASP B 1 40  ? 110.214 -26.682 18.523  1.00 15.04 ? 42   ASP B CA  1 
ATOM   3669 C  C   . ASP B 1 40  ? 110.504 -26.236 19.956  1.00 14.85 ? 42   ASP B C   1 
ATOM   3670 O  O   . ASP B 1 40  ? 110.612 -25.042 20.224  1.00 16.28 ? 42   ASP B O   1 
ATOM   3671 C  CB  . ASP B 1 40  ? 108.711 -26.778 18.256  1.00 15.60 ? 42   ASP B CB  1 
ATOM   3672 C  CG  . ASP B 1 40  ? 108.397 -26.897 16.772  1.00 17.37 ? 42   ASP B CG  1 
ATOM   3673 O  OD1 . ASP B 1 40  ? 108.626 -25.912 16.037  1.00 18.79 ? 42   ASP B OD1 1 
ATOM   3674 O  OD2 . ASP B 1 40  ? 107.995 -27.993 16.325  1.00 17.79 ? 42   ASP B OD2 1 
ATOM   3675 N  N   . ILE B 1 41  ? 110.659 -27.189 20.867  1.00 13.71 ? 43   ILE B N   1 
ATOM   3676 C  CA  . ILE B 1 41  ? 110.988 -26.853 22.251  1.00 13.23 ? 43   ILE B CA  1 
ATOM   3677 C  C   . ILE B 1 41  ? 112.495 -26.753 22.485  1.00 13.17 ? 43   ILE B C   1 
ATOM   3678 O  O   . ILE B 1 41  ? 112.987 -25.742 22.985  1.00 13.00 ? 43   ILE B O   1 
ATOM   3679 C  CB  . ILE B 1 41  ? 110.362 -27.846 23.247  1.00 13.06 ? 43   ILE B CB  1 
ATOM   3680 C  CG1 . ILE B 1 41  ? 108.839 -27.842 23.112  1.00 13.03 ? 43   ILE B CG1 1 
ATOM   3681 C  CG2 . ILE B 1 41  ? 110.763 -27.493 24.673  1.00 12.55 ? 43   ILE B CG2 1 
ATOM   3682 C  CD1 . ILE B 1 41  ? 108.199 -26.509 23.441  1.00 13.30 ? 43   ILE B CD1 1 
ATOM   3683 N  N   . ALA B 1 42  ? 113.227 -27.796 22.109  1.00 13.54 ? 44   ALA B N   1 
ATOM   3684 C  CA  . ALA B 1 42  ? 114.654 -27.886 22.410  1.00 13.74 ? 44   ALA B CA  1 
ATOM   3685 C  C   . ALA B 1 42  ? 115.429 -26.598 22.119  1.00 14.20 ? 44   ALA B C   1 
ATOM   3686 O  O   . ALA B 1 42  ? 116.220 -26.153 22.949  1.00 13.97 ? 44   ALA B O   1 
ATOM   3687 C  CB  . ALA B 1 42  ? 115.286 -29.064 21.684  1.00 13.58 ? 44   ALA B CB  1 
ATOM   3688 N  N   . PRO B 1 43  ? 115.227 -26.012 20.926  1.00 14.10 ? 45   PRO B N   1 
ATOM   3689 C  CA  . PRO B 1 43  ? 116.078 -24.897 20.510  1.00 14.74 ? 45   PRO B CA  1 
ATOM   3690 C  C   . PRO B 1 43  ? 115.799 -23.607 21.280  1.00 14.89 ? 45   PRO B C   1 
ATOM   3691 O  O   . PRO B 1 43  ? 116.580 -22.663 21.189  1.00 15.69 ? 45   PRO B O   1 
ATOM   3692 C  CB  . PRO B 1 43  ? 115.721 -24.710 19.028  1.00 16.05 ? 45   PRO B CB  1 
ATOM   3693 C  CG  . PRO B 1 43  ? 115.114 -26.006 18.608  1.00 15.64 ? 45   PRO B CG  1 
ATOM   3694 C  CD  . PRO B 1 43  ? 114.391 -26.509 19.821  1.00 14.53 ? 45   PRO B CD  1 
ATOM   3695 N  N   . VAL B 1 44  ? 114.703 -23.568 22.033  1.00 13.98 ? 46   VAL B N   1 
ATOM   3696 C  CA  . VAL B 1 44  ? 114.322 -22.350 22.750  1.00 14.35 ? 46   VAL B CA  1 
ATOM   3697 C  C   . VAL B 1 44  ? 114.303 -22.522 24.274  1.00 14.08 ? 46   VAL B C   1 
ATOM   3698 O  O   . VAL B 1 44  ? 113.795 -21.662 24.995  1.00 14.54 ? 46   VAL B O   1 
ATOM   3699 C  CB  . VAL B 1 44  ? 112.953 -21.816 22.281  1.00 14.57 ? 46   VAL B CB  1 
ATOM   3700 C  CG1 . VAL B 1 44  ? 112.994 -21.472 20.799  1.00 15.82 ? 46   VAL B CG1 1 
ATOM   3701 C  CG2 . VAL B 1 44  ? 111.856 -22.832 22.564  1.00 14.55 ? 46   VAL B CG2 1 
ATOM   3702 N  N   . VAL B 1 45  ? 114.869 -23.620 24.767  1.00 12.42 ? 47   VAL B N   1 
ATOM   3703 C  CA  . VAL B 1 45  ? 115.037 -23.791 26.211  1.00 12.24 ? 47   VAL B CA  1 
ATOM   3704 C  C   . VAL B 1 45  ? 116.172 -22.910 26.730  1.00 12.68 ? 47   VAL B C   1 
ATOM   3705 O  O   . VAL B 1 45  ? 117.269 -22.906 26.173  1.00 12.52 ? 47   VAL B O   1 
ATOM   3706 C  CB  . VAL B 1 45  ? 115.302 -25.262 26.585  1.00 12.20 ? 47   VAL B CB  1 
ATOM   3707 C  CG1 . VAL B 1 45  ? 115.436 -25.414 28.094  1.00 12.23 ? 47   VAL B CG1 1 
ATOM   3708 C  CG2 . VAL B 1 45  ? 114.186 -26.150 26.056  1.00 12.15 ? 47   VAL B CG2 1 
ATOM   3709 N  N   . ALA B 1 46  ? 115.886 -22.131 27.770  1.00 12.21 ? 48   ALA B N   1 
ATOM   3710 C  CA  . ALA B 1 46  ? 116.854 -21.180 28.314  1.00 11.92 ? 48   ALA B CA  1 
ATOM   3711 C  C   . ALA B 1 46  ? 117.853 -21.869 29.239  1.00 11.53 ? 48   ALA B C   1 
ATOM   3712 O  O   . ALA B 1 46  ? 117.461 -22.564 30.177  1.00 10.71 ? 48   ALA B O   1 
ATOM   3713 C  CB  . ALA B 1 46  ? 116.132 -20.063 29.058  1.00 11.67 ? 48   ALA B CB  1 
ATOM   3714 N  N   . SER B 1 47  ? 119.136 -21.602 29.021  1.00 11.51 ? 49   SER B N   1 
ATOM   3715 C  CA  . SER B 1 47  ? 120.202 -22.196 29.825  1.00 12.31 ? 49   SER B CA  1 
ATOM   3716 C  C   . SER B 1 47  ? 120.623 -21.305 30.994  1.00 13.38 ? 49   SER B C   1 
ATOM   3717 O  O   . SER B 1 47  ? 120.294 -20.120 31.040  1.00 14.52 ? 49   SER B O   1 
ATOM   3718 C  CB  . SER B 1 47  ? 121.419 -22.497 28.949  1.00 12.79 ? 49   SER B CB  1 
ATOM   3719 O  OG  . SER B 1 47  ? 122.106 -21.303 28.611  1.00 12.21 ? 49   SER B OG  1 
ATOM   3720 N  N   . VAL B 1 48  ? 121.383 -21.880 31.921  1.00 14.37 ? 50   VAL B N   1 
ATOM   3721 C  CA  . VAL B 1 48  ? 121.957 -21.128 33.033  1.00 15.25 ? 50   VAL B CA  1 
ATOM   3722 C  C   . VAL B 1 48  ? 122.917 -20.046 32.539  1.00 16.57 ? 50   VAL B C   1 
ATOM   3723 O  O   . VAL B 1 48  ? 122.904 -18.920 33.039  1.00 17.32 ? 50   VAL B O   1 
ATOM   3724 C  CB  . VAL B 1 48  ? 122.689 -22.062 34.016  1.00 15.39 ? 50   VAL B CB  1 
ATOM   3725 C  CG1 . VAL B 1 48  ? 123.632 -21.271 34.912  1.00 14.21 ? 50   VAL B CG1 1 
ATOM   3726 C  CG2 . VAL B 1 48  ? 121.686 -22.852 34.844  1.00 14.61 ? 50   VAL B CG2 1 
ATOM   3727 N  N   . THR B 1 49  ? 123.724 -20.380 31.535  1.00 16.98 ? 51   THR B N   1 
ATOM   3728 C  CA  . THR B 1 49  ? 124.627 -19.407 30.923  1.00 18.41 ? 51   THR B CA  1 
ATOM   3729 C  C   . THR B 1 49  ? 123.842 -18.210 30.403  1.00 19.44 ? 51   THR B C   1 
ATOM   3730 O  O   . THR B 1 49  ? 124.163 -17.060 30.704  1.00 20.04 ? 51   THR B O   1 
ATOM   3731 C  CB  . THR B 1 49  ? 125.418 -20.023 29.751  1.00 18.53 ? 51   THR B CB  1 
ATOM   3732 O  OG1 . THR B 1 49  ? 126.135 -21.177 30.206  1.00 18.82 ? 51   THR B OG1 1 
ATOM   3733 C  CG2 . THR B 1 49  ? 126.409 -19.008 29.187  1.00 18.69 ? 51   THR B CG2 1 
ATOM   3734 N  N   . GLN B 1 50  ? 122.801 -18.499 29.630  1.00 19.19 ? 52   GLN B N   1 
ATOM   3735 C  CA  . GLN B 1 50  ? 121.939 -17.476 29.057  1.00 21.42 ? 52   GLN B CA  1 
ATOM   3736 C  C   . GLN B 1 50  ? 121.391 -16.523 30.116  1.00 21.45 ? 52   GLN B C   1 
ATOM   3737 O  O   . GLN B 1 50  ? 121.465 -15.303 29.963  1.00 21.85 ? 52   GLN B O   1 
ATOM   3738 C  CB  . GLN B 1 50  ? 120.780 -18.141 28.318  1.00 24.36 ? 52   GLN B CB  1 
ATOM   3739 C  CG  . GLN B 1 50  ? 120.160 -17.302 27.217  1.00 28.67 ? 52   GLN B CG  1 
ATOM   3740 C  CD  . GLN B 1 50  ? 119.421 -18.155 26.204  1.00 33.86 ? 52   GLN B CD  1 
ATOM   3741 O  OE1 . GLN B 1 50  ? 119.515 -19.385 26.226  1.00 35.00 ? 52   GLN B OE1 1 
ATOM   3742 N  NE2 . GLN B 1 50  ? 118.692 -17.508 25.302  1.00 34.77 ? 52   GLN B NE2 1 
ATOM   3743 N  N   . LEU B 1 51  ? 120.800 -17.084 31.166  1.00 19.39 ? 53   LEU B N   1 
ATOM   3744 C  CA  . LEU B 1 51  ? 120.108 -16.282 32.170  1.00 20.43 ? 53   LEU B CA  1 
ATOM   3745 C  C   . LEU B 1 51  ? 121.073 -15.647 33.175  1.00 21.47 ? 53   LEU B C   1 
ATOM   3746 O  O   . LEU B 1 51  ? 120.707 -14.714 33.887  1.00 22.55 ? 53   LEU B O   1 
ATOM   3747 C  CB  . LEU B 1 51  ? 119.047 -17.117 32.895  1.00 18.46 ? 53   LEU B CB  1 
ATOM   3748 C  CG  . LEU B 1 51  ? 117.949 -17.750 32.036  1.00 17.73 ? 53   LEU B CG  1 
ATOM   3749 C  CD1 . LEU B 1 51  ? 116.858 -18.358 32.909  1.00 17.83 ? 53   LEU B CD1 1 
ATOM   3750 C  CD2 . LEU B 1 51  ? 117.352 -16.732 31.078  1.00 17.78 ? 53   LEU B CD2 1 
ATOM   3751 N  N   . SER B 1 52  ? 122.305 -16.148 33.218  1.00 22.13 ? 54   SER B N   1 
ATOM   3752 C  CA  . SER B 1 52  ? 123.315 -15.650 34.152  1.00 22.35 ? 54   SER B CA  1 
ATOM   3753 C  C   . SER B 1 52  ? 123.744 -14.225 33.814  1.00 23.68 ? 54   SER B C   1 
ATOM   3754 O  O   . SER B 1 52  ? 124.235 -13.491 34.674  1.00 24.60 ? 54   SER B O   1 
ATOM   3755 C  CB  . SER B 1 52  ? 124.542 -16.568 34.159  1.00 24.04 ? 54   SER B CB  1 
ATOM   3756 O  OG  . SER B 1 52  ? 124.316 -17.717 34.954  1.00 24.96 ? 54   SER B OG  1 
ATOM   3757 N  N   . ASN B 1 53  ? 123.590 -13.852 32.549  1.00 22.84 ? 55   ASN B N   1 
ATOM   3758 C  CA  . ASN B 1 53  ? 123.918 -12.506 32.106  1.00 24.56 ? 55   ASN B CA  1 
ATOM   3759 C  C   . ASN B 1 53  ? 122.658 -11.763 31.695  1.00 23.60 ? 55   ASN B C   1 
ATOM   3760 O  O   . ASN B 1 53  ? 121.929 -12.211 30.811  1.00 24.13 ? 55   ASN B O   1 
ATOM   3761 C  CB  . ASN B 1 53  ? 124.898 -12.545 30.927  1.00 24.15 ? 55   ASN B CB  1 
ATOM   3762 C  CG  . ASN B 1 53  ? 125.959 -13.619 31.078  1.00 23.92 ? 55   ASN B CG  1 
ATOM   3763 O  OD1 . ASN B 1 53  ? 126.763 -13.590 32.008  1.00 23.49 ? 55   ASN B OD1 1 
ATOM   3764 N  ND2 . ASN B 1 53  ? 125.991 -14.552 30.135  1.00 26.55 ? 55   ASN B ND2 1 
ATOM   3765 N  N   . VAL B 1 54  ? 122.411 -10.618 32.323  1.00 24.16 ? 56   VAL B N   1 
ATOM   3766 C  CA  . VAL B 1 54  ? 121.271 -9.789  31.952  1.00 23.76 ? 56   VAL B CA  1 
ATOM   3767 C  C   . VAL B 1 54  ? 121.233 -9.567  30.444  1.00 24.14 ? 56   VAL B C   1 
ATOM   3768 O  O   . VAL B 1 54  ? 120.161 -9.486  29.843  1.00 23.52 ? 56   VAL B O   1 
ATOM   3769 C  CB  . VAL B 1 54  ? 121.295 -8.428  32.671  1.00 24.91 ? 56   VAL B CB  1 
ATOM   3770 C  CG1 . VAL B 1 54  ? 120.279 -7.482  32.045  1.00 24.21 ? 56   VAL B CG1 1 
ATOM   3771 C  CG2 . VAL B 1 54  ? 121.021 -8.611  34.158  1.00 24.28 ? 56   VAL B CG2 1 
ATOM   3772 N  N   . ALA B 1 55  ? 122.412 -9.508  29.833  1.00 23.18 ? 57   ALA B N   1 
ATOM   3773 C  CA  . ALA B 1 55  ? 122.530 -9.151  28.425  1.00 23.36 ? 57   ALA B CA  1 
ATOM   3774 C  C   . ALA B 1 55  ? 121.925 -10.203 27.500  1.00 22.91 ? 57   ALA B C   1 
ATOM   3775 O  O   . ALA B 1 55  ? 121.442 -9.878  26.416  1.00 22.45 ? 57   ALA B O   1 
ATOM   3776 C  CB  . ALA B 1 55  ? 123.986 -8.897  28.063  1.00 24.01 ? 57   ALA B CB  1 
ATOM   3777 N  N   . THR B 1 56  ? 121.967 -11.465 27.920  1.00 21.67 ? 58   THR B N   1 
ATOM   3778 C  CA  . THR B 1 56  ? 121.595 -12.574 27.040  1.00 20.83 ? 58   THR B CA  1 
ATOM   3779 C  C   . THR B 1 56  ? 120.270 -13.221 27.431  1.00 21.89 ? 58   THR B C   1 
ATOM   3780 O  O   . THR B 1 56  ? 119.888 -14.253 26.880  1.00 21.91 ? 58   THR B O   1 
ATOM   3781 C  CB  . THR B 1 56  ? 122.687 -13.659 27.000  1.00 20.51 ? 58   THR B CB  1 
ATOM   3782 O  OG1 . THR B 1 56  ? 123.117 -13.956 28.334  1.00 20.69 ? 58   THR B OG1 1 
ATOM   3783 C  CG2 . THR B 1 56  ? 123.881 -13.184 26.180  1.00 19.71 ? 58   THR B CG2 1 
ATOM   3784 N  N   . GLN B 1 57  ? 119.569 -12.613 28.381  1.00 22.04 ? 59   GLN B N   1 
ATOM   3785 C  CA  . GLN B 1 57  ? 118.247 -13.095 28.767  1.00 23.76 ? 59   GLN B CA  1 
ATOM   3786 C  C   . GLN B 1 57  ? 117.227 -12.872 27.653  1.00 22.25 ? 59   GLN B C   1 
ATOM   3787 O  O   . GLN B 1 57  ? 117.158 -11.788 27.077  1.00 24.52 ? 59   GLN B O   1 
ATOM   3788 C  CB  . GLN B 1 57  ? 117.796 -12.432 30.068  1.00 23.54 ? 59   GLN B CB  1 
ATOM   3789 C  CG  . GLN B 1 57  ? 118.667 -12.808 31.256  1.00 25.18 ? 59   GLN B CG  1 
ATOM   3790 C  CD  . GLN B 1 57  ? 118.335 -12.023 32.506  1.00 28.07 ? 59   GLN B CD  1 
ATOM   3791 O  OE1 . GLN B 1 57  ? 118.846 -12.314 33.589  1.00 30.50 ? 59   GLN B OE1 1 
ATOM   3792 N  NE2 . GLN B 1 57  ? 117.484 -11.014 32.363  1.00 25.99 ? 59   GLN B NE2 1 
ATOM   3793 N  N   . PRO B 1 58  ? 116.443 -13.913 27.334  1.00 22.00 ? 60   PRO B N   1 
ATOM   3794 C  CA  . PRO B 1 58  ? 115.529 -13.898 26.199  1.00 21.00 ? 60   PRO B CA  1 
ATOM   3795 C  C   . PRO B 1 58  ? 114.216 -13.191 26.520  1.00 21.64 ? 60   PRO B C   1 
ATOM   3796 O  O   . PRO B 1 58  ? 113.904 -12.963 27.687  1.00 22.82 ? 60   PRO B O   1 
ATOM   3797 C  CB  . PRO B 1 58  ? 115.264 -15.381 25.965  1.00 20.36 ? 60   PRO B CB  1 
ATOM   3798 C  CG  . PRO B 1 58  ? 115.324 -15.970 27.331  1.00 19.67 ? 60   PRO B CG  1 
ATOM   3799 C  CD  . PRO B 1 58  ? 116.362 -15.178 28.087  1.00 20.99 ? 60   PRO B CD  1 
ATOM   3800 N  N   . LEU B 1 59  ? 113.435 -12.897 25.486  1.00 20.73 ? 61   LEU B N   1 
ATOM   3801 C  CA  . LEU B 1 59  ? 112.129 -12.270 25.654  1.00 22.00 ? 61   LEU B CA  1 
ATOM   3802 C  C   . LEU B 1 59  ? 111.196 -13.171 26.458  1.00 21.42 ? 61   LEU B C   1 
ATOM   3803 O  O   . LEU B 1 59  ? 110.561 -12.729 27.416  1.00 20.27 ? 61   LEU B O   1 
ATOM   3804 C  CB  . LEU B 1 59  ? 111.512 -11.970 24.289  1.00 24.53 ? 61   LEU B CB  1 
ATOM   3805 C  CG  . LEU B 1 59  ? 110.370 -10.953 24.232  1.00 27.18 ? 61   LEU B CG  1 
ATOM   3806 C  CD1 . LEU B 1 59  ? 110.686 -9.731  25.082  1.00 27.97 ? 61   LEU B CD1 1 
ATOM   3807 C  CD2 . LEU B 1 59  ? 110.105 -10.552 22.790  1.00 27.82 ? 61   LEU B CD2 1 
ATOM   3808 N  N   . VAL B 1 60  ? 111.101 -14.431 26.045  1.00 18.63 ? 62   VAL B N   1 
ATOM   3809 C  CA  . VAL B 1 60  ? 110.420 -15.450 26.831  1.00 16.90 ? 62   VAL B CA  1 
ATOM   3810 C  C   . VAL B 1 60  ? 111.400 -16.554 27.215  1.00 15.69 ? 62   VAL B C   1 
ATOM   3811 O  O   . VAL B 1 60  ? 112.049 -17.148 26.353  1.00 16.70 ? 62   VAL B O   1 
ATOM   3812 C  CB  . VAL B 1 60  ? 109.227 -16.055 26.066  1.00 16.97 ? 62   VAL B CB  1 
ATOM   3813 C  CG1 . VAL B 1 60  ? 108.533 -17.116 26.909  1.00 17.15 ? 62   VAL B CG1 1 
ATOM   3814 C  CG2 . VAL B 1 60  ? 108.244 -14.964 25.669  1.00 18.50 ? 62   VAL B CG2 1 
ATOM   3815 N  N   . ALA B 1 61  ? 111.552 -16.781 28.515  1.00 14.18 ? 63   ALA B N   1 
ATOM   3816 C  CA  . ALA B 1 61  ? 112.362 -17.887 29.003  1.00 13.48 ? 63   ALA B CA  1 
ATOM   3817 C  C   . ALA B 1 61  ? 111.507 -19.138 29.179  1.00 13.63 ? 63   ALA B C   1 
ATOM   3818 O  O   . ALA B 1 61  ? 110.428 -19.090 29.769  1.00 13.78 ? 63   ALA B O   1 
ATOM   3819 C  CB  . ALA B 1 61  ? 113.041 -17.513 30.309  1.00 12.65 ? 63   ALA B CB  1 
ATOM   3820 N  N   . LEU B 1 62  ? 111.982 -20.256 28.642  1.00 12.55 ? 64   LEU B N   1 
ATOM   3821 C  CA  . LEU B 1 62  ? 111.233 -21.499 28.714  1.00 11.41 ? 64   LEU B CA  1 
ATOM   3822 C  C   . LEU B 1 62  ? 112.094 -22.605 29.315  1.00 10.46 ? 64   LEU B C   1 
ATOM   3823 O  O   . LEU B 1 62  ? 113.248 -22.783 28.922  1.00 10.50 ? 64   LEU B O   1 
ATOM   3824 C  CB  . LEU B 1 62  ? 110.729 -21.901 27.324  1.00 11.49 ? 64   LEU B CB  1 
ATOM   3825 C  CG  . LEU B 1 62  ? 109.866 -23.162 27.226  1.00 11.58 ? 64   LEU B CG  1 
ATOM   3826 C  CD1 . LEU B 1 62  ? 109.002 -23.130 25.973  1.00 12.86 ? 64   LEU B CD1 1 
ATOM   3827 C  CD2 . LEU B 1 62  ? 110.733 -24.411 27.244  1.00 11.82 ? 64   LEU B CD2 1 
ATOM   3828 N  N   . ASN B 1 63  ? 111.553 -23.282 30.325  1.00 8.89  ? 65   ASN B N   1 
ATOM   3829 C  CA  . ASN B 1 63  ? 112.120 -24.531 30.830  1.00 8.27  ? 65   ASN B CA  1 
ATOM   3830 C  C   . ASN B 1 63  ? 111.070 -25.636 30.734  1.00 7.87  ? 65   ASN B C   1 
ATOM   3831 O  O   . ASN B 1 63  ? 109.874 -25.358 30.647  1.00 7.53  ? 65   ASN B O   1 
ATOM   3832 C  CB  . ASN B 1 63  ? 112.555 -24.370 32.294  1.00 8.06  ? 65   ASN B CB  1 
ATOM   3833 C  CG  . ASN B 1 63  ? 113.965 -23.812 32.437  1.00 8.29  ? 65   ASN B CG  1 
ATOM   3834 O  OD1 . ASN B 1 63  ? 114.536 -23.827 33.528  1.00 8.01  ? 65   ASN B OD1 1 
ATOM   3835 N  ND2 . ASN B 1 63  ? 114.536 -23.331 31.337  1.00 7.92  ? 65   ASN B ND2 1 
ATOM   3836 N  N   . ILE B 1 64  ? 111.506 -26.889 30.778  1.00 7.58  ? 66   ILE B N   1 
ATOM   3837 C  CA  . ILE B 1 64  ? 110.565 -28.003 30.728  1.00 7.38  ? 66   ILE B CA  1 
ATOM   3838 C  C   . ILE B 1 64  ? 111.046 -29.186 31.568  1.00 7.80  ? 66   ILE B C   1 
ATOM   3839 O  O   . ILE B 1 64  ? 112.243 -29.463 31.637  1.00 8.94  ? 66   ILE B O   1 
ATOM   3840 C  CB  . ILE B 1 64  ? 110.304 -28.446 29.273  1.00 7.41  ? 66   ILE B CB  1 
ATOM   3841 C  CG1 . ILE B 1 64  ? 109.205 -29.511 29.215  1.00 7.29  ? 66   ILE B CG1 1 
ATOM   3842 C  CG2 . ILE B 1 64  ? 111.590 -28.929 28.619  1.00 7.44  ? 66   ILE B CG2 1 
ATOM   3843 C  CD1 . ILE B 1 64  ? 108.718 -29.815 27.810  1.00 7.13  ? 66   ILE B CD1 1 
ATOM   3844 N  N   . ALA B 1 65  ? 110.116 -29.853 32.243  1.00 7.93  ? 67   ALA B N   1 
ATOM   3845 C  CA  . ALA B 1 65  ? 110.469 -30.959 33.128  1.00 7.75  ? 67   ALA B CA  1 
ATOM   3846 C  C   . ALA B 1 65  ? 109.437 -32.071 33.023  1.00 7.81  ? 67   ALA B C   1 
ATOM   3847 O  O   . ALA B 1 65  ? 108.281 -31.826 32.682  1.00 7.30  ? 67   ALA B O   1 
ATOM   3848 C  CB  . ALA B 1 65  ? 110.588 -30.474 34.568  1.00 7.72  ? 67   ALA B CB  1 
ATOM   3849 N  N   . PHE B 1 66  ? 109.867 -33.298 33.290  1.00 8.02  ? 68   PHE B N   1 
ATOM   3850 C  CA  . PHE B 1 66  ? 108.996 -34.448 33.114  1.00 8.31  ? 68   PHE B CA  1 
ATOM   3851 C  C   . PHE B 1 66  ? 108.833 -35.233 34.402  1.00 8.41  ? 68   PHE B C   1 
ATOM   3852 O  O   . PHE B 1 66  ? 109.778 -35.380 35.179  1.00 8.08  ? 68   PHE B O   1 
ATOM   3853 C  CB  . PHE B 1 66  ? 109.522 -35.353 32.006  1.00 8.47  ? 68   PHE B CB  1 
ATOM   3854 C  CG  . PHE B 1 66  ? 109.538 -34.699 30.657  1.00 9.03  ? 68   PHE B CG  1 
ATOM   3855 C  CD1 . PHE B 1 66  ? 110.619 -33.926 30.261  1.00 9.20  ? 68   PHE B CD1 1 
ATOM   3856 C  CD2 . PHE B 1 66  ? 108.452 -34.816 29.804  1.00 9.38  ? 68   PHE B CD2 1 
ATOM   3857 C  CE1 . PHE B 1 66  ? 110.641 -33.332 29.013  1.00 9.60  ? 68   PHE B CE1 1 
ATOM   3858 C  CE2 . PHE B 1 66  ? 108.455 -34.198 28.566  1.00 10.05 ? 68   PHE B CE2 1 
ATOM   3859 C  CZ  . PHE B 1 66  ? 109.557 -33.465 28.166  1.00 10.20 ? 68   PHE B CZ  1 
ATOM   3860 N  N   . SER B 1 67  ? 107.625 -35.736 34.621  1.00 8.45  ? 69   SER B N   1 
ATOM   3861 C  CA  . SER B 1 67  ? 107.376 -36.649 35.721  1.00 8.42  ? 69   SER B CA  1 
ATOM   3862 C  C   . SER B 1 67  ? 107.847 -38.041 35.331  1.00 8.72  ? 69   SER B C   1 
ATOM   3863 O  O   . SER B 1 67  ? 108.178 -38.299 34.171  1.00 8.33  ? 69   SER B O   1 
ATOM   3864 C  CB  . SER B 1 67  ? 105.885 -36.696 36.052  1.00 8.35  ? 69   SER B CB  1 
ATOM   3865 O  OG  . SER B 1 67  ? 105.178 -37.382 35.036  1.00 8.20  ? 69   SER B OG  1 
ATOM   3866 N  N   . ASN B 1 68  ? 107.854 -38.941 36.304  1.00 8.74  ? 70   ASN B N   1 
ATOM   3867 C  CA  . ASN B 1 68  ? 108.143 -40.339 36.035  1.00 9.79  ? 70   ASN B CA  1 
ATOM   3868 C  C   . ASN B 1 68  ? 107.244 -40.901 34.933  1.00 9.27  ? 70   ASN B C   1 
ATOM   3869 O  O   . ASN B 1 68  ? 107.724 -41.536 33.993  1.00 9.28  ? 70   ASN B O   1 
ATOM   3870 C  CB  . ASN B 1 68  ? 108.001 -41.166 37.315  1.00 9.91  ? 70   ASN B CB  1 
ATOM   3871 C  CG  . ASN B 1 68  ? 108.215 -42.648 37.078  1.00 11.02 ? 70   ASN B CG  1 
ATOM   3872 O  OD1 . ASN B 1 68  ? 109.328 -43.087 36.780  1.00 11.41 ? 70   ASN B OD1 1 
ATOM   3873 N  ND2 . ASN B 1 68  ? 107.146 -43.430 37.212  1.00 10.90 ? 70   ASN B ND2 1 
ATOM   3874 N  N   . THR B 1 69  ? 105.942 -40.640 35.031  1.00 9.40  ? 71   THR B N   1 
ATOM   3875 C  CA  . THR B 1 69  ? 104.999 -41.182 34.058  1.00 9.38  ? 71   THR B CA  1 
ATOM   3876 C  C   . THR B 1 69  ? 105.143 -40.521 32.691  1.00 9.62  ? 71   THR B C   1 
ATOM   3877 O  O   . THR B 1 69  ? 104.791 -41.110 31.670  1.00 10.56 ? 71   THR B O   1 
ATOM   3878 C  CB  . THR B 1 69  ? 103.537 -41.077 34.535  1.00 9.58  ? 71   THR B CB  1 
ATOM   3879 O  OG1 . THR B 1 69  ? 103.250 -39.728 34.925  1.00 10.12 ? 71   THR B OG1 1 
ATOM   3880 C  CG2 . THR B 1 69  ? 103.292 -42.014 35.704  1.00 9.77  ? 71   THR B CG2 1 
ATOM   3881 N  N   . GLY B 1 70  ? 105.663 -39.298 32.673  1.00 9.34  ? 72   GLY B N   1 
ATOM   3882 C  CA  . GLY B 1 70  ? 105.976 -38.623 31.417  1.00 9.55  ? 72   GLY B CA  1 
ATOM   3883 C  C   . GLY B 1 70  ? 107.154 -39.260 30.704  1.00 9.88  ? 72   GLY B C   1 
ATOM   3884 O  O   . GLY B 1 70  ? 107.094 -39.538 29.505  1.00 9.57  ? 72   GLY B O   1 
ATOM   3885 N  N   . LEU B 1 71  ? 108.222 -39.519 31.451  1.00 10.07 ? 73   LEU B N   1 
ATOM   3886 C  CA  . LEU B 1 71  ? 109.356 -40.271 30.922  1.00 9.99  ? 73   LEU B CA  1 
ATOM   3887 C  C   . LEU B 1 71  ? 108.921 -41.636 30.391  1.00 9.98  ? 73   LEU B C   1 
ATOM   3888 O  O   . LEU B 1 71  ? 109.336 -42.048 29.309  1.00 10.19 ? 73   LEU B O   1 
ATOM   3889 C  CB  . LEU B 1 71  ? 110.449 -40.431 31.984  1.00 9.68  ? 73   LEU B CB  1 
ATOM   3890 C  CG  . LEU B 1 71  ? 111.203 -39.155 32.386  1.00 9.97  ? 73   LEU B CG  1 
ATOM   3891 C  CD1 . LEU B 1 71  ? 112.306 -39.460 33.387  1.00 10.33 ? 73   LEU B CD1 1 
ATOM   3892 C  CD2 . LEU B 1 71  ? 111.768 -38.423 31.177  1.00 9.52  ? 73   LEU B CD2 1 
ATOM   3893 N  N   . LEU B 1 72  ? 108.070 -42.327 31.143  1.00 10.24 ? 74   LEU B N   1 
ATOM   3894 C  CA  . LEU B 1 72  ? 107.572 -43.633 30.710  1.00 10.60 ? 74   LEU B CA  1 
ATOM   3895 C  C   . LEU B 1 72  ? 106.743 -43.526 29.432  1.00 10.54 ? 74   LEU B C   1 
ATOM   3896 O  O   . LEU B 1 72  ? 106.856 -44.369 28.541  1.00 10.37 ? 74   LEU B O   1 
ATOM   3897 C  CB  . LEU B 1 72  ? 106.774 -44.318 31.821  1.00 11.02 ? 74   LEU B CB  1 
ATOM   3898 C  CG  . LEU B 1 72  ? 107.623 -44.809 32.998  1.00 11.79 ? 74   LEU B CG  1 
ATOM   3899 C  CD1 . LEU B 1 72  ? 106.763 -45.417 34.097  1.00 13.04 ? 74   LEU B CD1 1 
ATOM   3900 C  CD2 . LEU B 1 72  ? 108.680 -45.794 32.523  1.00 12.07 ? 74   LEU B CD2 1 
ATOM   3901 N  N   . ALA B 1 73  ? 105.947 -42.465 29.329  1.00 10.01 ? 75   ALA B N   1 
ATOM   3902 C  CA  . ALA B 1 73  ? 105.159 -42.208 28.130  1.00 10.32 ? 75   ALA B CA  1 
ATOM   3903 C  C   . ALA B 1 73  ? 106.053 -42.036 26.906  1.00 10.53 ? 75   ALA B C   1 
ATOM   3904 O  O   . ALA B 1 73  ? 105.659 -42.364 25.787  1.00 11.20 ? 75   ALA B O   1 
ATOM   3905 C  CB  . ALA B 1 73  ? 104.280 -40.978 28.324  1.00 10.28 ? 75   ALA B CB  1 
ATOM   3906 N  N   . LEU B 1 74  ? 107.247 -41.496 27.126  1.00 10.76 ? 76   LEU B N   1 
ATOM   3907 C  CA  . LEU B 1 74  ? 108.210 -41.272 26.052  1.00 11.26 ? 76   LEU B CA  1 
ATOM   3908 C  C   . LEU B 1 74  ? 109.052 -42.513 25.769  1.00 12.06 ? 76   LEU B C   1 
ATOM   3909 O  O   . LEU B 1 74  ? 109.913 -42.503 24.888  1.00 13.02 ? 76   LEU B O   1 
ATOM   3910 C  CB  . LEU B 1 74  ? 109.126 -40.094 26.399  1.00 11.17 ? 76   LEU B CB  1 
ATOM   3911 C  CG  . LEU B 1 74  ? 108.453 -38.722 26.442  1.00 11.40 ? 76   LEU B CG  1 
ATOM   3912 C  CD1 . LEU B 1 74  ? 109.425 -37.649 26.909  1.00 11.22 ? 76   LEU B CD1 1 
ATOM   3913 C  CD2 . LEU B 1 74  ? 107.873 -38.376 25.078  1.00 12.24 ? 76   LEU B CD2 1 
ATOM   3914 N  N   . GLY B 1 75  ? 108.788 -43.587 26.505  1.00 11.94 ? 77   GLY B N   1 
ATOM   3915 C  CA  . GLY B 1 75  ? 109.525 -44.831 26.319  1.00 12.16 ? 77   GLY B CA  1 
ATOM   3916 C  C   . GLY B 1 75  ? 110.880 -44.808 26.999  1.00 12.62 ? 77   GLY B C   1 
ATOM   3917 O  O   . GLY B 1 75  ? 111.742 -45.642 26.720  1.00 13.20 ? 77   GLY B O   1 
ATOM   3918 N  N   . VAL B 1 76  ? 111.069 -43.858 27.906  1.00 12.18 ? 78   VAL B N   1 
ATOM   3919 C  CA  . VAL B 1 76  ? 112.307 -43.785 28.665  1.00 12.76 ? 78   VAL B CA  1 
ATOM   3920 C  C   . VAL B 1 76  ? 112.166 -44.542 29.978  1.00 13.23 ? 78   VAL B C   1 
ATOM   3921 O  O   . VAL B 1 76  ? 111.536 -44.059 30.920  1.00 12.88 ? 78   VAL B O   1 
ATOM   3922 C  CB  . VAL B 1 76  ? 112.720 -42.328 28.941  1.00 12.51 ? 78   VAL B CB  1 
ATOM   3923 C  CG1 . VAL B 1 76  ? 114.069 -42.288 29.642  1.00 12.84 ? 78   VAL B CG1 1 
ATOM   3924 C  CG2 . VAL B 1 76  ? 112.769 -41.541 27.640  1.00 12.07 ? 78   VAL B CG2 1 
ATOM   3925 N  N   . THR B 1 77  ? 112.740 -45.741 30.025  1.00 13.52 ? 79   THR B N   1 
ATOM   3926 C  CA  . THR B 1 77  ? 112.541 -46.646 31.151  1.00 14.49 ? 79   THR B CA  1 
ATOM   3927 C  C   . THR B 1 77  ? 113.750 -46.660 32.082  1.00 14.33 ? 79   THR B C   1 
ATOM   3928 O  O   . THR B 1 77  ? 113.787 -47.416 33.055  1.00 14.19 ? 79   THR B O   1 
ATOM   3929 C  CB  . THR B 1 77  ? 112.271 -48.083 30.669  1.00 15.16 ? 79   THR B CB  1 
ATOM   3930 O  OG1 . THR B 1 77  ? 113.319 -48.492 29.782  1.00 15.35 ? 79   THR B OG1 1 
ATOM   3931 C  CG2 . THR B 1 77  ? 110.940 -48.160 29.938  1.00 15.60 ? 79   THR B CG2 1 
ATOM   3932 N  N   . ASP B 1 78  ? 114.740 -45.827 31.776  1.00 14.54 ? 80   ASP B N   1 
ATOM   3933 C  CA  . ASP B 1 78  ? 115.970 -45.774 32.560  1.00 14.45 ? 80   ASP B CA  1 
ATOM   3934 C  C   . ASP B 1 78  ? 115.667 -45.383 33.997  1.00 13.91 ? 80   ASP B C   1 
ATOM   3935 O  O   . ASP B 1 78  ? 114.780 -44.568 34.251  1.00 13.92 ? 80   ASP B O   1 
ATOM   3936 C  CB  . ASP B 1 78  ? 116.949 -44.765 31.958  1.00 14.92 ? 80   ASP B CB  1 
ATOM   3937 C  CG  . ASP B 1 78  ? 117.344 -45.112 30.538  1.00 16.64 ? 80   ASP B CG  1 
ATOM   3938 O  OD1 . ASP B 1 78  ? 117.006 -46.226 30.076  1.00 18.89 ? 80   ASP B OD1 1 
ATOM   3939 O  OD2 . ASP B 1 78  ? 118.002 -44.274 29.888  1.00 15.68 ? 80   ASP B OD2 1 
ATOM   3940 N  N   . ASN B 1 79  ? 116.414 -45.961 34.933  1.00 13.65 ? 81   ASN B N   1 
ATOM   3941 C  CA  . ASN B 1 79  ? 116.308 -45.589 36.339  1.00 14.04 ? 81   ASN B CA  1 
ATOM   3942 C  C   . ASN B 1 79  ? 117.102 -44.318 36.633  1.00 14.25 ? 81   ASN B C   1 
ATOM   3943 O  O   . ASN B 1 79  ? 118.320 -44.285 36.457  1.00 12.27 ? 81   ASN B O   1 
ATOM   3944 C  CB  . ASN B 1 79  ? 116.802 -46.733 37.231  1.00 15.65 ? 81   ASN B CB  1 
ATOM   3945 C  CG  . ASN B 1 79  ? 116.487 -46.509 38.700  1.00 18.24 ? 81   ASN B CG  1 
ATOM   3946 O  OD1 . ASN B 1 79  ? 116.233 -45.383 39.129  1.00 18.29 ? 81   ASN B OD1 1 
ATOM   3947 N  ND2 . ASN B 1 79  ? 116.511 -47.584 39.482  1.00 20.16 ? 81   ASN B ND2 1 
ATOM   3948 N  N   . LEU B 1 80  ? 116.403 -43.270 37.062  1.00 13.30 ? 82   LEU B N   1 
ATOM   3949 C  CA  . LEU B 1 80  ? 117.032 -41.976 37.326  1.00 14.12 ? 82   LEU B CA  1 
ATOM   3950 C  C   . LEU B 1 80  ? 117.680 -41.953 38.710  1.00 14.01 ? 82   LEU B C   1 
ATOM   3951 O  O   . LEU B 1 80  ? 118.365 -40.993 39.069  1.00 14.32 ? 82   LEU B O   1 
ATOM   3952 C  CB  . LEU B 1 80  ? 115.998 -40.850 37.217  1.00 14.48 ? 82   LEU B CB  1 
ATOM   3953 C  CG  . LEU B 1 80  ? 115.668 -40.276 35.835  1.00 15.70 ? 82   LEU B CG  1 
ATOM   3954 C  CD1 . LEU B 1 80  ? 116.750 -39.306 35.386  1.00 19.64 ? 82   LEU B CD1 1 
ATOM   3955 C  CD2 . LEU B 1 80  ? 115.458 -41.366 34.793  1.00 15.65 ? 82   LEU B CD2 1 
ATOM   3956 N  N   . GLY B 1 81  ? 117.440 -43.001 39.491  1.00 13.17 ? 83   GLY B N   1 
ATOM   3957 C  CA  . GLY B 1 81  ? 118.110 -43.172 40.779  1.00 13.28 ? 83   GLY B CA  1 
ATOM   3958 C  C   . GLY B 1 81  ? 117.405 -42.499 41.942  1.00 13.00 ? 83   GLY B C   1 
ATOM   3959 O  O   . GLY B 1 81  ? 117.969 -42.364 43.029  1.00 13.06 ? 83   GLY B O   1 
ATOM   3960 N  N   . ASP B 1 82  ? 116.162 -42.087 41.723  1.00 12.89 ? 84   ASP B N   1 
ATOM   3961 C  CA  . ASP B 1 82  ? 115.402 -41.394 42.758  1.00 11.93 ? 84   ASP B CA  1 
ATOM   3962 C  C   . ASP B 1 82  ? 114.030 -42.030 42.954  1.00 11.73 ? 84   ASP B C   1 
ATOM   3963 O  O   . ASP B 1 82  ? 113.131 -41.839 42.140  1.00 11.83 ? 84   ASP B O   1 
ATOM   3964 C  CB  . ASP B 1 82  ? 115.258 -39.911 42.404  1.00 11.63 ? 84   ASP B CB  1 
ATOM   3965 C  CG  . ASP B 1 82  ? 114.914 -39.056 43.607  1.00 11.51 ? 84   ASP B CG  1 
ATOM   3966 O  OD1 . ASP B 1 82  ? 113.750 -39.100 44.048  1.00 11.18 ? 84   ASP B OD1 1 
ATOM   3967 O  OD2 . ASP B 1 82  ? 115.808 -38.340 44.106  1.00 11.30 ? 84   ASP B OD2 1 
ATOM   3968 N  N   A SER B 1 83  ? 113.883 -42.794 44.033  0.50 11.70 ? 85   SER B N   1 
ATOM   3969 N  N   B SER B 1 83  ? 113.869 -42.760 44.055  0.50 11.59 ? 85   SER B N   1 
ATOM   3970 C  CA  A SER B 1 83  ? 112.643 -43.513 44.302  0.50 11.74 ? 85   SER B CA  1 
ATOM   3971 C  CA  B SER B 1 83  ? 112.649 -43.523 44.308  0.50 11.54 ? 85   SER B CA  1 
ATOM   3972 C  C   A SER B 1 83  ? 111.469 -42.561 44.495  0.50 11.31 ? 85   SER B C   1 
ATOM   3973 C  C   B SER B 1 83  ? 111.448 -42.627 44.612  0.50 11.32 ? 85   SER B C   1 
ATOM   3974 O  O   A SER B 1 83  ? 110.362 -42.823 44.023  0.50 11.59 ? 85   SER B O   1 
ATOM   3975 O  O   B SER B 1 83  ? 110.307 -42.985 44.315  0.50 11.81 ? 85   SER B O   1 
ATOM   3976 C  CB  A SER B 1 83  ? 112.792 -44.404 45.536  0.50 11.85 ? 85   SER B CB  1 
ATOM   3977 C  CB  B SER B 1 83  ? 112.868 -44.527 45.444  0.50 11.44 ? 85   SER B CB  1 
ATOM   3978 O  OG  A SER B 1 83  ? 111.561 -45.030 45.850  0.50 12.64 ? 85   SER B OG  1 
ATOM   3979 O  OG  B SER B 1 83  ? 113.644 -45.632 45.007  0.50 11.28 ? 85   SER B OG  1 
ATOM   3980 N  N   . LEU B 1 84  ? 111.703 -41.474 45.221  1.00 11.07 ? 86   LEU B N   1 
ATOM   3981 C  CA  . LEU B 1 84  ? 110.642 -40.509 45.500  1.00 11.33 ? 86   LEU B CA  1 
ATOM   3982 C  C   . LEU B 1 84  ? 110.086 -39.918 44.206  1.00 11.01 ? 86   LEU B C   1 
ATOM   3983 O  O   . LEU B 1 84  ? 108.873 -39.804 44.032  1.00 10.61 ? 86   LEU B O   1 
ATOM   3984 C  CB  . LEU B 1 84  ? 111.147 -39.400 46.423  1.00 10.52 ? 86   LEU B CB  1 
ATOM   3985 C  CG  . LEU B 1 84  ? 111.351 -39.811 47.884  1.00 11.41 ? 86   LEU B CG  1 
ATOM   3986 C  CD1 . LEU B 1 84  ? 112.073 -38.710 48.645  1.00 11.19 ? 86   LEU B CD1 1 
ATOM   3987 C  CD2 . LEU B 1 84  ? 110.020 -40.138 48.546  1.00 11.10 ? 86   LEU B CD2 1 
ATOM   3988 N  N   . PHE B 1 85  ? 110.983 -39.559 43.294  1.00 10.69 ? 87   PHE B N   1 
ATOM   3989 C  CA  . PHE B 1 85  ? 110.578 -39.090 41.975  1.00 10.38 ? 87   PHE B CA  1 
ATOM   3990 C  C   . PHE B 1 85  ? 109.767 -40.157 41.245  1.00 10.71 ? 87   PHE B C   1 
ATOM   3991 O  O   . PHE B 1 85  ? 108.715 -39.870 40.678  1.00 10.72 ? 87   PHE B O   1 
ATOM   3992 C  CB  . PHE B 1 85  ? 111.803 -38.693 41.149  1.00 9.45  ? 87   PHE B CB  1 
ATOM   3993 C  CG  . PHE B 1 85  ? 111.530 -38.564 39.674  1.00 9.12  ? 87   PHE B CG  1 
ATOM   3994 C  CD1 . PHE B 1 85  ? 110.913 -37.434 39.166  1.00 9.23  ? 87   PHE B CD1 1 
ATOM   3995 C  CD2 . PHE B 1 85  ? 111.941 -39.550 38.791  1.00 9.46  ? 87   PHE B CD2 1 
ATOM   3996 C  CE1 . PHE B 1 85  ? 110.687 -37.301 37.807  1.00 9.52  ? 87   PHE B CE1 1 
ATOM   3997 C  CE2 . PHE B 1 85  ? 111.701 -39.433 37.431  1.00 9.26  ? 87   PHE B CE2 1 
ATOM   3998 C  CZ  . PHE B 1 85  ? 111.084 -38.302 36.937  1.00 9.27  ? 87   PHE B CZ  1 
ATOM   3999 N  N   . ALA B 1 86  ? 110.251 -41.392 41.275  1.00 10.83 ? 88   ALA B N   1 
ATOM   4000 C  CA  . ALA B 1 86  ? 109.586 -42.476 40.563  1.00 11.72 ? 88   ALA B CA  1 
ATOM   4001 C  C   . ALA B 1 86  ? 108.139 -42.640 41.016  1.00 12.12 ? 88   ALA B C   1 
ATOM   4002 O  O   . ALA B 1 86  ? 107.253 -42.885 40.204  1.00 11.83 ? 88   ALA B O   1 
ATOM   4003 C  CB  . ALA B 1 86  ? 110.355 -43.777 40.734  1.00 12.31 ? 88   ALA B CB  1 
ATOM   4004 N  N   . ASN B 1 87  ? 107.901 -42.479 42.314  1.00 12.73 ? 89   ASN B N   1 
ATOM   4005 C  CA  . ASN B 1 87  ? 106.602 -42.799 42.887  1.00 14.33 ? 89   ASN B CA  1 
ATOM   4006 C  C   . ASN B 1 87  ? 105.616 -41.630 42.893  1.00 13.34 ? 89   ASN B C   1 
ATOM   4007 O  O   . ASN B 1 87  ? 104.409 -41.829 43.017  1.00 14.17 ? 89   ASN B O   1 
ATOM   4008 C  CB  . ASN B 1 87  ? 106.774 -43.382 44.288  1.00 15.52 ? 89   ASN B CB  1 
ATOM   4009 C  CG  . ASN B 1 87  ? 107.375 -44.773 44.260  1.00 17.89 ? 89   ASN B CG  1 
ATOM   4010 O  OD1 . ASN B 1 87  ? 106.879 -45.659 43.561  1.00 20.71 ? 89   ASN B OD1 1 
ATOM   4011 N  ND2 . ASN B 1 87  ? 108.488 -44.954 44.960  1.00 17.96 ? 89   ASN B ND2 1 
ATOM   4012 N  N   . GLY B 1 88  ? 106.126 -40.421 42.681  1.00 12.39 ? 90   GLY B N   1 
ATOM   4013 C  CA  . GLY B 1 88  ? 105.271 -39.239 42.564  1.00 11.84 ? 90   GLY B CA  1 
ATOM   4014 C  C   . GLY B 1 88  ? 104.984 -38.607 43.912  1.00 11.91 ? 90   GLY B C   1 
ATOM   4015 O  O   . GLY B 1 88  ? 105.045 -39.273 44.946  1.00 11.17 ? 90   GLY B O   1 
ATOM   4016 N  N   . GLN B 1 89  ? 104.668 -37.315 43.907  1.00 11.46 ? 91   GLN B N   1 
ATOM   4017 C  CA  . GLN B 1 89  ? 104.487 -36.589 45.159  1.00 11.60 ? 91   GLN B CA  1 
ATOM   4018 C  C   . GLN B 1 89  ? 103.216 -36.998 45.910  1.00 11.84 ? 91   GLN B C   1 
ATOM   4019 O  O   . GLN B 1 89  ? 103.196 -37.018 47.141  1.00 12.04 ? 91   GLN B O   1 
ATOM   4020 C  CB  . GLN B 1 89  ? 104.524 -35.077 44.932  1.00 11.67 ? 91   GLN B CB  1 
ATOM   4021 C  CG  . GLN B 1 89  ? 104.610 -34.270 46.218  1.00 12.44 ? 91   GLN B CG  1 
ATOM   4022 C  CD  . GLN B 1 89  ? 104.442 -32.783 45.988  1.00 12.80 ? 91   GLN B CD  1 
ATOM   4023 O  OE1 . GLN B 1 89  ? 103.469 -32.180 46.443  1.00 13.80 ? 91   GLN B OE1 1 
ATOM   4024 N  NE2 . GLN B 1 89  ? 105.400 -32.176 45.291  1.00 12.33 ? 91   GLN B NE2 1 
ATOM   4025 N  N   . ALA B 1 90  ? 102.165 -37.350 45.177  1.00 12.06 ? 92   ALA B N   1 
ATOM   4026 C  CA  . ALA B 1 90  ? 100.920 -37.760 45.821  1.00 13.17 ? 92   ALA B CA  1 
ATOM   4027 C  C   . ALA B 1 90  ? 101.150 -38.925 46.787  1.00 13.90 ? 92   ALA B C   1 
ATOM   4028 O  O   . ALA B 1 90  ? 100.639 -38.922 47.907  1.00 13.67 ? 92   ALA B O   1 
ATOM   4029 C  CB  . ALA B 1 90  ? 99.862  -38.115 44.787  1.00 12.88 ? 92   ALA B CB  1 
ATOM   4030 N  N   . LYS B 1 91  ? 101.960 -39.893 46.367  1.00 15.12 ? 93   LYS B N   1 
ATOM   4031 C  CA  . LYS B 1 91  ? 102.287 -41.032 47.218  1.00 16.12 ? 93   LYS B CA  1 
ATOM   4032 C  C   . LYS B 1 91  ? 103.187 -40.638 48.383  1.00 15.84 ? 93   LYS B C   1 
ATOM   4033 O  O   . LYS B 1 91  ? 103.246 -41.333 49.397  1.00 14.99 ? 93   LYS B O   1 
ATOM   4034 C  CB  . LYS B 1 91  ? 102.934 -42.151 46.401  1.00 18.79 ? 93   LYS B CB  1 
ATOM   4035 C  CG  . LYS B 1 91  ? 102.020 -43.348 46.191  1.00 21.01 ? 93   LYS B CG  1 
ATOM   4036 C  CD  . LYS B 1 91  ? 102.134 -43.903 44.783  1.00 25.87 ? 93   LYS B CD  1 
ATOM   4037 C  CE  . LYS B 1 91  ? 100.849 -44.602 44.368  1.00 28.18 ? 93   LYS B CE  1 
ATOM   4038 N  NZ  . LYS B 1 91  ? 100.754 -44.754 42.888  1.00 32.19 ? 93   LYS B NZ  1 
ATOM   4039 N  N   . ASP B 1 92  ? 103.877 -39.513 48.238  1.00 14.64 ? 94   ASP B N   1 
ATOM   4040 C  CA  . ASP B 1 92  ? 104.796 -39.050 49.268  1.00 14.75 ? 94   ASP B CA  1 
ATOM   4041 C  C   . ASP B 1 92  ? 104.107 -38.165 50.309  1.00 14.87 ? 94   ASP B C   1 
ATOM   4042 O  O   . ASP B 1 92  ? 104.718 -37.777 51.300  1.00 14.89 ? 94   ASP B O   1 
ATOM   4043 C  CB  . ASP B 1 92  ? 105.963 -38.296 48.625  1.00 15.58 ? 94   ASP B CB  1 
ATOM   4044 C  CG  . ASP B 1 92  ? 107.152 -38.166 49.548  1.00 15.92 ? 94   ASP B CG  1 
ATOM   4045 O  OD1 . ASP B 1 92  ? 107.308 -39.027 50.443  1.00 15.57 ? 94   ASP B OD1 1 
ATOM   4046 O  OD2 . ASP B 1 92  ? 107.944 -37.214 49.359  1.00 15.30 ? 94   ASP B OD2 1 
ATOM   4047 N  N   . ALA B 1 93  ? 102.837 -37.844 50.079  1.00 14.94 ? 95   ALA B N   1 
ATOM   4048 C  CA  . ALA B 1 93  ? 102.146 -36.840 50.884  1.00 16.39 ? 95   ALA B CA  1 
ATOM   4049 C  C   . ALA B 1 93  ? 102.068 -37.231 52.361  1.00 16.54 ? 95   ALA B C   1 
ATOM   4050 O  O   . ALA B 1 93  ? 102.121 -36.374 53.242  1.00 15.37 ? 95   ALA B O   1 
ATOM   4051 C  CB  . ALA B 1 93  ? 100.757 -36.572 50.326  1.00 17.31 ? 95   ALA B CB  1 
ATOM   4052 N  N   . THR B 1 94  ? 101.964 -38.527 52.632  1.00 18.89 ? 96   THR B N   1 
ATOM   4053 C  CA  . THR B 1 94  ? 101.878 -39.000 54.013  1.00 18.82 ? 96   THR B CA  1 
ATOM   4054 C  C   . THR B 1 94  ? 103.154 -38.697 54.793  1.00 18.15 ? 96   THR B C   1 
ATOM   4055 O  O   . THR B 1 94  ? 103.119 -38.548 56.014  1.00 19.36 ? 96   THR B O   1 
ATOM   4056 C  CB  . THR B 1 94  ? 101.579 -40.507 54.084  1.00 21.15 ? 96   THR B CB  1 
ATOM   4057 O  OG1 . THR B 1 94  ? 102.463 -41.209 53.203  1.00 23.26 ? 96   THR B OG1 1 
ATOM   4058 C  CG2 . THR B 1 94  ? 100.138 -40.784 53.678  1.00 21.37 ? 96   THR B CG2 1 
ATOM   4059 N  N   . SER B 1 95  ? 104.273 -38.579 54.083  1.00 17.59 ? 97   SER B N   1 
ATOM   4060 C  CA  . SER B 1 95  ? 105.543 -38.214 54.708  1.00 17.44 ? 97   SER B CA  1 
ATOM   4061 C  C   . SER B 1 95  ? 105.457 -36.842 55.361  1.00 17.60 ? 97   SER B C   1 
ATOM   4062 O  O   . SER B 1 95  ? 106.212 -36.533 56.281  1.00 19.09 ? 97   SER B O   1 
ATOM   4063 C  CB  . SER B 1 95  ? 106.678 -38.220 53.678  1.00 17.07 ? 97   SER B CB  1 
ATOM   4064 O  OG  . SER B 1 95  ? 106.794 -39.483 53.053  1.00 16.30 ? 97   SER B OG  1 
ATOM   4065 N  N   . PHE B 1 96  ? 104.547 -36.012 54.862  1.00 16.82 ? 98   PHE B N   1 
ATOM   4066 C  CA  . PHE B 1 96  ? 104.426 -34.642 55.337  1.00 17.19 ? 98   PHE B CA  1 
ATOM   4067 C  C   . PHE B 1 96  ? 103.175 -34.478 56.194  1.00 18.53 ? 98   PHE B C   1 
ATOM   4068 O  O   . PHE B 1 96  ? 102.746 -33.361 56.486  1.00 18.51 ? 98   PHE B O   1 
ATOM   4069 C  CB  . PHE B 1 96  ? 104.408 -33.669 54.156  1.00 17.00 ? 98   PHE B CB  1 
ATOM   4070 C  CG  . PHE B 1 96  ? 105.460 -33.957 53.122  1.00 16.45 ? 98   PHE B CG  1 
ATOM   4071 C  CD1 . PHE B 1 96  ? 106.754 -34.279 53.501  1.00 16.64 ? 98   PHE B CD1 1 
ATOM   4072 C  CD2 . PHE B 1 96  ? 105.158 -33.902 51.770  1.00 16.80 ? 98   PHE B CD2 1 
ATOM   4073 C  CE1 . PHE B 1 96  ? 107.726 -34.545 52.555  1.00 17.78 ? 98   PHE B CE1 1 
ATOM   4074 C  CE2 . PHE B 1 96  ? 106.126 -34.166 50.817  1.00 17.39 ? 98   PHE B CE2 1 
ATOM   4075 C  CZ  . PHE B 1 96  ? 107.412 -34.487 51.210  1.00 16.60 ? 98   PHE B CZ  1 
ATOM   4076 N  N   . LYS B 1 97  ? 102.616 -35.604 56.625  1.00 19.81 ? 99   LYS B N   1 
ATOM   4077 C  CA  . LYS B 1 97  ? 101.412 -35.600 57.442  1.00 19.50 ? 99   LYS B CA  1 
ATOM   4078 C  C   . LYS B 1 97  ? 100.352 -34.694 56.832  1.00 19.59 ? 99   LYS B C   1 
ATOM   4079 O  O   . LYS B 1 97  ? 99.809  -33.810 57.495  1.00 19.95 ? 99   LYS B O   1 
ATOM   4080 C  CB  . LYS B 1 97  ? 101.738 -35.176 58.873  1.00 20.83 ? 99   LYS B CB  1 
ATOM   4081 C  CG  . LYS B 1 97  ? 102.776 -36.066 59.537  1.00 21.02 ? 99   LYS B CG  1 
ATOM   4082 C  CD  . LYS B 1 97  ? 103.036 -35.646 60.972  1.00 23.90 ? 99   LYS B CD  1 
ATOM   4083 C  CE  . LYS B 1 97  ? 104.015 -36.595 61.644  1.00 26.42 ? 99   LYS B CE  1 
ATOM   4084 N  NZ  . LYS B 1 97  ? 104.491 -36.061 62.949  1.00 31.08 ? 99   LYS B NZ  1 
ATOM   4085 N  N   . GLU B 1 98  ? 100.084 -34.909 55.551  1.00 19.32 ? 100  GLU B N   1 
ATOM   4086 C  CA  . GLU B 1 98  ? 99.016  -34.200 54.869  1.00 20.14 ? 100  GLU B CA  1 
ATOM   4087 C  C   . GLU B 1 98  ? 98.224  -35.157 53.987  1.00 19.83 ? 100  GLU B C   1 
ATOM   4088 O  O   . GLU B 1 98  ? 98.731  -36.200 53.563  1.00 20.84 ? 100  GLU B O   1 
ATOM   4089 C  CB  . GLU B 1 98  ? 99.576  -33.037 54.045  1.00 20.73 ? 100  GLU B CB  1 
ATOM   4090 C  CG  . GLU B 1 98  ? 99.875  -33.375 52.594  1.00 19.56 ? 100  GLU B CG  1 
ATOM   4091 C  CD  . GLU B 1 98  ? 100.634 -32.268 51.883  1.00 19.02 ? 100  GLU B CD  1 
ATOM   4092 O  OE1 . GLU B 1 98  ? 101.576 -31.708 52.483  1.00 17.71 ? 100  GLU B OE1 1 
ATOM   4093 O  OE2 . GLU B 1 98  ? 100.292 -31.959 50.721  1.00 18.54 ? 100  GLU B OE2 1 
ATOM   4094 N  N   . SER B 1 99  ? 96.968  -34.806 53.742  1.00 20.04 ? 101  SER B N   1 
ATOM   4095 C  CA  . SER B 1 99  ? 96.091  -35.606 52.902  1.00 21.42 ? 101  SER B CA  1 
ATOM   4096 C  C   . SER B 1 99  ? 96.013  -34.981 51.515  1.00 21.12 ? 101  SER B C   1 
ATOM   4097 O  O   . SER B 1 99  ? 96.153  -33.766 51.370  1.00 20.28 ? 101  SER B O   1 
ATOM   4098 C  CB  . SER B 1 99  ? 94.697  -35.677 53.533  1.00 21.79 ? 101  SER B CB  1 
ATOM   4099 O  OG  . SER B 1 99  ? 93.717  -36.046 52.582  1.00 22.98 ? 101  SER B OG  1 
ATOM   4100 N  N   . THR B 1 100 ? 95.807  -35.809 50.495  1.00 20.30 ? 102  THR B N   1 
ATOM   4101 C  CA  . THR B 1 100 ? 95.665  -35.308 49.131  1.00 20.79 ? 102  THR B CA  1 
ATOM   4102 C  C   . THR B 1 100 ? 94.237  -34.861 48.822  1.00 22.61 ? 102  THR B C   1 
ATOM   4103 O  O   . THR B 1 100 ? 93.941  -34.439 47.704  1.00 21.52 ? 102  THR B O   1 
ATOM   4104 C  CB  . THR B 1 100 ? 96.101  -36.352 48.084  1.00 21.27 ? 102  THR B CB  1 
ATOM   4105 O  OG1 . THR B 1 100 ? 95.251  -37.502 48.168  1.00 22.58 ? 102  THR B OG1 1 
ATOM   4106 C  CG2 . THR B 1 100 ? 97.544  -36.771 48.313  1.00 21.09 ? 102  THR B CG2 1 
ATOM   4107 N  N   . SER B 1 101 ? 93.355  -34.950 49.814  1.00 24.98 ? 103  SER B N   1 
ATOM   4108 C  CA  . SER B 1 101 ? 91.936  -34.674 49.595  1.00 24.51 ? 103  SER B CA  1 
ATOM   4109 C  C   . SER B 1 101 ? 91.649  -33.198 49.310  1.00 24.89 ? 103  SER B C   1 
ATOM   4110 O  O   . SER B 1 101 ? 90.616  -32.863 48.734  1.00 27.77 ? 103  SER B O   1 
ATOM   4111 C  CB  . SER B 1 101 ? 91.094  -35.171 50.774  1.00 25.05 ? 103  SER B CB  1 
ATOM   4112 O  OG  . SER B 1 101 ? 91.525  -34.584 51.988  1.00 26.76 ? 103  SER B OG  1 
ATOM   4113 N  N   . SER B 1 102 ? 92.573  -32.322 49.690  1.00 24.17 ? 104  SER B N   1 
ATOM   4114 C  CA  . SER B 1 102 ? 92.431  -30.897 49.407  1.00 24.50 ? 104  SER B CA  1 
ATOM   4115 C  C   . SER B 1 102 ? 93.288  -30.459 48.218  1.00 22.27 ? 104  SER B C   1 
ATOM   4116 O  O   . SER B 1 102 ? 93.352  -29.274 47.887  1.00 20.83 ? 104  SER B O   1 
ATOM   4117 C  CB  . SER B 1 102 ? 92.786  -30.066 50.643  1.00 28.47 ? 104  SER B CB  1 
ATOM   4118 O  OG  . SER B 1 102 ? 94.175  -30.136 50.927  1.00 29.86 ? 104  SER B OG  1 
ATOM   4119 N  N   . TRP B 1 103 ? 93.953  -31.420 47.585  1.00 19.02 ? 105  TRP B N   1 
ATOM   4120 C  CA  . TRP B 1 103 ? 94.860  -31.123 46.479  1.00 17.03 ? 105  TRP B CA  1 
ATOM   4121 C  C   . TRP B 1 103 ? 94.083  -30.686 45.246  1.00 16.10 ? 105  TRP B C   1 
ATOM   4122 O  O   . TRP B 1 103 ? 92.931  -31.073 45.063  1.00 16.08 ? 105  TRP B O   1 
ATOM   4123 C  CB  . TRP B 1 103 ? 95.694  -32.360 46.140  1.00 15.88 ? 105  TRP B CB  1 
ATOM   4124 C  CG  . TRP B 1 103 ? 96.884  -32.552 47.023  1.00 16.06 ? 105  TRP B CG  1 
ATOM   4125 C  CD1 . TRP B 1 103 ? 97.038  -32.111 48.306  1.00 15.16 ? 105  TRP B CD1 1 
ATOM   4126 C  CD2 . TRP B 1 103 ? 98.091  -33.245 46.689  1.00 14.94 ? 105  TRP B CD2 1 
ATOM   4127 N  NE1 . TRP B 1 103 ? 98.268  -32.487 48.791  1.00 14.80 ? 105  TRP B NE1 1 
ATOM   4128 C  CE2 . TRP B 1 103 ? 98.934  -33.185 47.818  1.00 14.93 ? 105  TRP B CE2 1 
ATOM   4129 C  CE3 . TRP B 1 103 ? 98.543  -33.908 45.543  1.00 14.13 ? 105  TRP B CE3 1 
ATOM   4130 C  CZ2 . TRP B 1 103 ? 100.208 -33.756 47.832  1.00 14.49 ? 105  TRP B CZ2 1 
ATOM   4131 C  CZ3 . TRP B 1 103 ? 99.806  -34.478 45.560  1.00 13.87 ? 105  TRP B CZ3 1 
ATOM   4132 C  CH2 . TRP B 1 103 ? 100.623 -34.397 46.696  1.00 14.17 ? 105  TRP B CH2 1 
ATOM   4133 N  N   . VAL B 1 104 ? 94.724  -29.896 44.389  1.00 14.81 ? 106  VAL B N   1 
ATOM   4134 C  CA  . VAL B 1 104 ? 94.308  -29.815 42.998  1.00 15.18 ? 106  VAL B CA  1 
ATOM   4135 C  C   . VAL B 1 104 ? 94.143  -31.235 42.470  1.00 15.13 ? 106  VAL B C   1 
ATOM   4136 O  O   . VAL B 1 104 ? 95.083  -32.028 42.516  1.00 15.38 ? 106  VAL B O   1 
ATOM   4137 C  CB  . VAL B 1 104 ? 95.355  -29.084 42.138  1.00 14.76 ? 106  VAL B CB  1 
ATOM   4138 C  CG1 . VAL B 1 104 ? 94.837  -28.895 40.720  1.00 15.05 ? 106  VAL B CG1 1 
ATOM   4139 C  CG2 . VAL B 1 104 ? 95.729  -27.752 42.768  1.00 14.60 ? 106  VAL B CG2 1 
ATOM   4140 N  N   . PRO B 1 105 ? 92.932  -31.574 42.001  1.00 15.08 ? 107  PRO B N   1 
ATOM   4141 C  CA  . PRO B 1 105 ? 92.625  -32.947 41.603  1.00 14.91 ? 107  PRO B CA  1 
ATOM   4142 C  C   . PRO B 1 105 ? 93.694  -33.536 40.684  1.00 14.78 ? 107  PRO B C   1 
ATOM   4143 O  O   . PRO B 1 105 ? 94.091  -34.687 40.853  1.00 14.83 ? 107  PRO B O   1 
ATOM   4144 C  CB  . PRO B 1 105 ? 91.297  -32.803 40.856  1.00 15.38 ? 107  PRO B CB  1 
ATOM   4145 C  CG  . PRO B 1 105 ? 90.653  -31.611 41.484  1.00 15.29 ? 107  PRO B CG  1 
ATOM   4146 C  CD  . PRO B 1 105 ? 91.776  -30.673 41.837  1.00 15.04 ? 107  PRO B CD  1 
ATOM   4147 N  N   . GLN B 1 106 ? 94.190  -32.733 39.749  1.00 15.49 ? 108  GLN B N   1 
ATOM   4148 C  CA  . GLN B 1 106 ? 95.168  -33.209 38.775  1.00 15.25 ? 108  GLN B CA  1 
ATOM   4149 C  C   . GLN B 1 106 ? 96.503  -33.614 39.406  1.00 14.51 ? 108  GLN B C   1 
ATOM   4150 O  O   . GLN B 1 106 ? 97.242  -34.413 38.831  1.00 13.69 ? 108  GLN B O   1 
ATOM   4151 C  CB  . GLN B 1 106 ? 95.389  -32.170 37.674  1.00 15.37 ? 108  GLN B CB  1 
ATOM   4152 C  CG  . GLN B 1 106 ? 94.239  -32.063 36.682  1.00 16.68 ? 108  GLN B CG  1 
ATOM   4153 C  CD  . GLN B 1 106 ? 93.074  -31.247 37.213  1.00 17.85 ? 108  GLN B CD  1 
ATOM   4154 O  OE1 . GLN B 1 106 ? 93.213  -30.493 38.178  1.00 16.95 ? 108  GLN B OE1 1 
ATOM   4155 N  NE2 . GLN B 1 106 ? 91.910  -31.408 36.592  1.00 19.81 ? 108  GLN B NE2 1 
ATOM   4156 N  N   . PHE B 1 107 ? 96.802  -33.074 40.586  1.00 14.17 ? 109  PHE B N   1 
ATOM   4157 C  CA  . PHE B 1 107 ? 98.035  -33.416 41.299  1.00 14.02 ? 109  PHE B CA  1 
ATOM   4158 C  C   . PHE B 1 107 ? 97.894  -34.732 42.066  1.00 14.96 ? 109  PHE B C   1 
ATOM   4159 O  O   . PHE B 1 107 ? 98.888  -35.389 42.387  1.00 13.16 ? 109  PHE B O   1 
ATOM   4160 C  CB  . PHE B 1 107 ? 98.432  -32.300 42.275  1.00 14.17 ? 109  PHE B CB  1 
ATOM   4161 C  CG  . PHE B 1 107 ? 99.036  -31.090 41.612  1.00 14.45 ? 109  PHE B CG  1 
ATOM   4162 C  CD1 . PHE B 1 107 ? 99.866  -31.225 40.509  1.00 14.62 ? 109  PHE B CD1 1 
ATOM   4163 C  CD2 . PHE B 1 107 ? 98.818  -29.823 42.129  1.00 14.90 ? 109  PHE B CD2 1 
ATOM   4164 C  CE1 . PHE B 1 107 ? 100.421 -30.111 39.900  1.00 15.57 ? 109  PHE B CE1 1 
ATOM   4165 C  CE2 . PHE B 1 107 ? 99.370  -28.706 41.527  1.00 15.12 ? 109  PHE B CE2 1 
ATOM   4166 C  CZ  . PHE B 1 107 ? 100.171 -28.851 40.409  1.00 14.67 ? 109  PHE B CZ  1 
ATOM   4167 N  N   . ALA B 1 108 ? 96.655  -35.090 42.388  1.00 14.93 ? 110  ALA B N   1 
ATOM   4168 C  CA  . ALA B 1 108 ? 96.384  -36.215 43.272  1.00 15.86 ? 110  ALA B CA  1 
ATOM   4169 C  C   . ALA B 1 108 ? 96.358  -37.520 42.484  1.00 17.06 ? 110  ALA B C   1 
ATOM   4170 O  O   . ALA B 1 108 ? 95.319  -38.167 42.367  1.00 17.13 ? 110  ALA B O   1 
ATOM   4171 C  CB  . ALA B 1 108 ? 95.067  -36.004 44.005  1.00 15.64 ? 110  ALA B CB  1 
ATOM   4172 N  N   . GLY B 1 109 ? 97.514  -37.897 41.950  1.00 16.12 ? 111  GLY B N   1 
ATOM   4173 C  CA  . GLY B 1 109 ? 97.608  -38.971 40.970  1.00 16.03 ? 111  GLY B CA  1 
ATOM   4174 C  C   . GLY B 1 109 ? 98.921  -38.850 40.221  1.00 15.26 ? 111  GLY B C   1 
ATOM   4175 O  O   . GLY B 1 109 ? 99.794  -38.082 40.619  1.00 15.86 ? 111  GLY B O   1 
ATOM   4176 N  N   . THR B 1 110 ? 99.055  -39.576 39.118  1.00 14.39 ? 112  THR B N   1 
ATOM   4177 C  CA  . THR B 1 110 ? 100.226 -39.433 38.264  1.00 13.60 ? 112  THR B CA  1 
ATOM   4178 C  C   . THR B 1 110 ? 99.834  -39.265 36.797  1.00 12.29 ? 112  THR B C   1 
ATOM   4179 O  O   . THR B 1 110 ? 100.540 -39.714 35.896  1.00 11.60 ? 112  THR B O   1 
ATOM   4180 C  CB  . THR B 1 110 ? 101.213 -40.607 38.439  1.00 13.93 ? 112  THR B CB  1 
ATOM   4181 O  OG1 . THR B 1 110 ? 100.522 -41.849 38.258  1.00 14.96 ? 112  THR B OG1 1 
ATOM   4182 C  CG2 . THR B 1 110 ? 101.826 -40.580 39.833  1.00 14.47 ? 112  THR B CG2 1 
ATOM   4183 N  N   . GLY B 1 111 ? 98.722  -38.572 36.563  1.00 11.82 ? 113  GLY B N   1 
ATOM   4184 C  CA  . GLY B 1 111 ? 98.290  -38.265 35.205  1.00 11.27 ? 113  GLY B CA  1 
ATOM   4185 C  C   . GLY B 1 111 ? 99.142  -37.200 34.540  1.00 10.63 ? 113  GLY B C   1 
ATOM   4186 O  O   . GLY B 1 111 ? 99.236  -37.139 33.312  1.00 10.33 ? 113  GLY B O   1 
ATOM   4187 N  N   . ILE B 1 112 ? 99.768  -36.353 35.348  1.00 10.14 ? 114  ILE B N   1 
ATOM   4188 C  CA  . ILE B 1 112 ? 100.589 -35.274 34.803  1.00 9.71  ? 114  ILE B CA  1 
ATOM   4189 C  C   . ILE B 1 112 ? 101.936 -35.811 34.335  1.00 9.24  ? 114  ILE B C   1 
ATOM   4190 O  O   . ILE B 1 112 ? 102.656 -36.451 35.106  1.00 8.85  ? 114  ILE B O   1 
ATOM   4191 C  CB  . ILE B 1 112 ? 100.809 -34.151 35.831  1.00 9.62  ? 114  ILE B CB  1 
ATOM   4192 C  CG1 . ILE B 1 112 ? 99.524  -33.342 36.009  1.00 10.14 ? 114  ILE B CG1 1 
ATOM   4193 C  CG2 . ILE B 1 112 ? 101.950 -33.241 35.392  1.00 9.45  ? 114  ILE B CG2 1 
ATOM   4194 C  CD1 . ILE B 1 112 ? 99.473  -32.563 37.307  1.00 11.16 ? 114  ILE B CD1 1 
ATOM   4195 N  N   . HIS B 1 113 ? 102.264 -35.558 33.070  1.00 8.83  ? 115  HIS B N   1 
ATOM   4196 C  CA  . HIS B 1 113 ? 103.484 -36.087 32.470  1.00 8.72  ? 115  HIS B CA  1 
ATOM   4197 C  C   . HIS B 1 113 ? 104.635 -35.092 32.502  1.00 8.45  ? 115  HIS B C   1 
ATOM   4198 O  O   . HIS B 1 113 ? 105.795 -35.475 32.379  1.00 8.46  ? 115  HIS B O   1 
ATOM   4199 C  CB  . HIS B 1 113 ? 103.229 -36.548 31.032  1.00 9.18  ? 115  HIS B CB  1 
ATOM   4200 C  CG  . HIS B 1 113 ? 102.383 -37.778 30.940  1.00 9.87  ? 115  HIS B CG  1 
ATOM   4201 N  ND1 . HIS B 1 113 ? 101.695 -38.129 29.799  1.00 10.67 ? 115  HIS B ND1 1 
ATOM   4202 C  CD2 . HIS B 1 113 ? 102.108 -38.737 31.855  1.00 10.05 ? 115  HIS B CD2 1 
ATOM   4203 C  CE1 . HIS B 1 113 ? 101.032 -39.251 30.014  1.00 10.84 ? 115  HIS B CE1 1 
ATOM   4204 N  NE2 . HIS B 1 113 ? 101.263 -39.639 31.256  1.00 10.30 ? 115  HIS B NE2 1 
ATOM   4205 N  N   . GLY B 1 114 ? 104.320 -33.816 32.684  1.00 7.94  ? 116  GLY B N   1 
ATOM   4206 C  CA  . GLY B 1 114 ? 105.369 -32.814 32.776  1.00 8.33  ? 116  GLY B CA  1 
ATOM   4207 C  C   . GLY B 1 114 ? 104.861 -31.402 32.971  1.00 8.19  ? 116  GLY B C   1 
ATOM   4208 O  O   . GLY B 1 114 ? 103.659 -31.165 33.096  1.00 7.90  ? 116  GLY B O   1 
ATOM   4209 N  N   . VAL B 1 115 ? 105.795 -30.463 33.022  1.00 8.24  ? 117  VAL B N   1 
ATOM   4210 C  CA  . VAL B 1 115 ? 105.450 -29.066 33.184  1.00 8.19  ? 117  VAL B CA  1 
ATOM   4211 C  C   . VAL B 1 115 ? 106.326 -28.225 32.279  1.00 8.41  ? 117  VAL B C   1 
ATOM   4212 O  O   . VAL B 1 115 ? 107.531 -28.458 32.169  1.00 7.86  ? 117  VAL B O   1 
ATOM   4213 C  CB  . VAL B 1 115 ? 105.616 -28.604 34.647  1.00 8.26  ? 117  VAL B CB  1 
ATOM   4214 C  CG1 . VAL B 1 115 ? 107.026 -28.888 35.143  1.00 7.92  ? 117  VAL B CG1 1 
ATOM   4215 C  CG2 . VAL B 1 115 ? 105.272 -27.124 34.786  1.00 8.12  ? 117  VAL B CG2 1 
ATOM   4216 N  N   . ILE B 1 116 ? 105.699 -27.294 31.573  1.00 8.44  ? 118  ILE B N   1 
ATOM   4217 C  CA  . ILE B 1 116 ? 106.438 -26.261 30.878  1.00 9.09  ? 118  ILE B CA  1 
ATOM   4218 C  C   . ILE B 1 116 ? 106.398 -25.004 31.730  1.00 9.22  ? 118  ILE B C   1 
ATOM   4219 O  O   . ILE B 1 116 ? 105.331 -24.596 32.181  1.00 9.52  ? 118  ILE B O   1 
ATOM   4220 C  CB  . ILE B 1 116 ? 105.823 -25.963 29.499  1.00 9.07  ? 118  ILE B CB  1 
ATOM   4221 C  CG1 . ILE B 1 116 ? 105.805 -27.233 28.649  1.00 9.29  ? 118  ILE B CG1 1 
ATOM   4222 C  CG2 . ILE B 1 116 ? 106.604 -24.861 28.802  1.00 9.23  ? 118  ILE B CG2 1 
ATOM   4223 C  CD1 . ILE B 1 116 ? 105.095 -27.072 27.321  1.00 9.23  ? 118  ILE B CD1 1 
ATOM   4224 N  N   . ILE B 1 117 ? 107.569 -24.456 32.036  1.00 9.50  ? 119  ILE B N   1 
ATOM   4225 C  CA  . ILE B 1 117 ? 107.636 -23.178 32.731  1.00 9.83  ? 119  ILE B CA  1 
ATOM   4226 C  C   . ILE B 1 117 ? 107.919 -22.072 31.727  1.00 10.52 ? 119  ILE B C   1 
ATOM   4227 O  O   . ILE B 1 117 ? 108.961 -22.078 31.069  1.00 10.45 ? 119  ILE B O   1 
ATOM   4228 C  CB  . ILE B 1 117 ? 108.738 -23.169 33.803  1.00 10.43 ? 119  ILE B CB  1 
ATOM   4229 C  CG1 . ILE B 1 117 ? 108.558 -24.342 34.769  1.00 10.82 ? 119  ILE B CG1 1 
ATOM   4230 C  CG2 . ILE B 1 117 ? 108.730 -21.848 34.560  1.00 11.09 ? 119  ILE B CG2 1 
ATOM   4231 C  CD1 . ILE B 1 117 ? 109.783 -24.624 35.614  1.00 12.17 ? 119  ILE B CD1 1 
ATOM   4232 N  N   . LEU B 1 118 ? 106.971 -21.151 31.583  1.00 10.69 ? 120  LEU B N   1 
ATOM   4233 C  CA  . LEU B 1 118 ? 107.171 -19.967 30.755  1.00 11.91 ? 120  LEU B CA  1 
ATOM   4234 C  C   . LEU B 1 118 ? 107.329 -18.740 31.638  1.00 11.93 ? 120  LEU B C   1 
ATOM   4235 O  O   . LEU B 1 118 ? 106.596 -18.570 32.611  1.00 12.77 ? 120  LEU B O   1 
ATOM   4236 C  CB  . LEU B 1 118 ? 105.995 -19.773 29.794  1.00 12.00 ? 120  LEU B CB  1 
ATOM   4237 C  CG  . LEU B 1 118 ? 105.719 -20.908 28.807  1.00 13.04 ? 120  LEU B CG  1 
ATOM   4238 C  CD1 . LEU B 1 118 ? 104.443 -20.637 28.029  1.00 14.26 ? 120  LEU B CD1 1 
ATOM   4239 C  CD2 . LEU B 1 118 ? 106.886 -21.080 27.850  1.00 14.26 ? 120  LEU B CD2 1 
ATOM   4240 N  N   . ALA B 1 119 ? 108.327 -17.919 31.330  1.00 12.43 ? 121  ALA B N   1 
ATOM   4241 C  CA  . ALA B 1 119 ? 108.586 -16.704 32.090  1.00 12.72 ? 121  ALA B CA  1 
ATOM   4242 C  C   . ALA B 1 119 ? 108.827 -15.535 31.142  1.00 13.16 ? 121  ALA B C   1 
ATOM   4243 O  O   . ALA B 1 119 ? 109.525 -15.670 30.141  1.00 13.03 ? 121  ALA B O   1 
ATOM   4244 C  CB  . ALA B 1 119 ? 109.784 -16.897 33.007  1.00 13.10 ? 121  ALA B CB  1 
ATOM   4245 N  N   . SER B 1 120 ? 108.210 -14.399 31.442  1.00 14.04 ? 122  SER B N   1 
ATOM   4246 C  CA  . SER B 1 120 ? 108.366 -13.206 30.623  1.00 14.24 ? 122  SER B CA  1 
ATOM   4247 C  C   . SER B 1 120 ? 107.957 -11.998 31.444  1.00 14.95 ? 122  SER B C   1 
ATOM   4248 O  O   . SER B 1 120 ? 107.352 -12.137 32.503  1.00 14.21 ? 122  SER B O   1 
ATOM   4249 C  CB  . SER B 1 120 ? 107.491 -13.296 29.370  1.00 14.21 ? 122  SER B CB  1 
ATOM   4250 O  OG  . SER B 1 120 ? 107.877 -12.325 28.412  1.00 15.85 ? 122  SER B OG  1 
ATOM   4251 N  N   . ASP B 1 121 ? 108.281 -10.810 30.952  1.00 17.17 ? 123  ASP B N   1 
ATOM   4252 C  CA  . ASP B 1 121 ? 107.959 -9.596  31.687  1.00 18.80 ? 123  ASP B CA  1 
ATOM   4253 C  C   . ASP B 1 121 ? 106.519 -9.144  31.447  1.00 18.03 ? 123  ASP B C   1 
ATOM   4254 O  O   . ASP B 1 121 ? 106.013 -8.279  32.155  1.00 19.28 ? 123  ASP B O   1 
ATOM   4255 C  CB  . ASP B 1 121 ? 108.956 -8.481  31.364  1.00 20.95 ? 123  ASP B CB  1 
ATOM   4256 C  CG  . ASP B 1 121 ? 110.301 -8.685  32.046  1.00 23.00 ? 123  ASP B CG  1 
ATOM   4257 O  OD1 . ASP B 1 121 ? 110.345 -9.327  33.119  1.00 22.13 ? 123  ASP B OD1 1 
ATOM   4258 O  OD2 . ASP B 1 121 ? 111.317 -8.198  31.510  1.00 27.61 ? 123  ASP B OD2 1 
ATOM   4259 N  N   . THR B 1 122 ? 105.842 -9.772  30.490  1.00 17.33 ? 124  THR B N   1 
ATOM   4260 C  CA  . THR B 1 122 ? 104.403 -9.562  30.324  1.00 17.58 ? 124  THR B CA  1 
ATOM   4261 C  C   . THR B 1 122 ? 103.629 -10.869 30.188  1.00 18.06 ? 124  THR B C   1 
ATOM   4262 O  O   . THR B 1 122 ? 104.141 -11.858 29.664  1.00 16.79 ? 124  THR B O   1 
ATOM   4263 C  CB  . THR B 1 122 ? 104.081 -8.658  29.116  1.00 18.95 ? 124  THR B CB  1 
ATOM   4264 O  OG1 . THR B 1 122 ? 104.194 -9.411  27.902  1.00 18.26 ? 124  THR B OG1 1 
ATOM   4265 C  CG2 . THR B 1 122 ? 105.032 -7.471  29.066  1.00 18.25 ? 124  THR B CG2 1 
ATOM   4266 N  N   . THR B 1 123 ? 102.373 -10.851 30.616  1.00 17.35 ? 125  THR B N   1 
ATOM   4267 C  CA  . THR B 1 123 ? 101.511 -12.015 30.475  1.00 17.64 ? 125  THR B CA  1 
ATOM   4268 C  C   . THR B 1 123 ? 101.168 -12.275 29.008  1.00 17.80 ? 125  THR B C   1 
ATOM   4269 O  O   . THR B 1 123 ? 100.969 -13.420 28.602  1.00 16.09 ? 125  THR B O   1 
ATOM   4270 C  CB  . THR B 1 123 ? 100.219 -11.861 31.296  1.00 18.62 ? 125  THR B CB  1 
ATOM   4271 O  OG1 . THR B 1 123 ? 99.679  -10.550 31.100  1.00 23.13 ? 125  THR B OG1 1 
ATOM   4272 C  CG2 . THR B 1 123 ? 100.511 -12.055 32.778  1.00 18.63 ? 125  THR B CG2 1 
ATOM   4273 N  N   . ASP B 1 124 ? 101.111 -11.208 28.217  1.00 17.50 ? 126  ASP B N   1 
ATOM   4274 C  CA  . ASP B 1 124 ? 100.788 -11.329 26.797  1.00 18.05 ? 126  ASP B CA  1 
ATOM   4275 C  C   . ASP B 1 124 ? 101.802 -12.193 26.050  1.00 16.72 ? 126  ASP B C   1 
ATOM   4276 O  O   . ASP B 1 124 ? 101.431 -13.041 25.240  1.00 16.77 ? 126  ASP B O   1 
ATOM   4277 C  CB  . ASP B 1 124 ? 100.688 -9.950  26.145  1.00 20.26 ? 126  ASP B CB  1 
ATOM   4278 C  CG  . ASP B 1 124 ? 99.336  -9.299  26.366  1.00 22.40 ? 126  ASP B CG  1 
ATOM   4279 O  OD1 . ASP B 1 124 ? 98.424  -9.984  26.873  1.00 22.91 ? 126  ASP B OD1 1 
ATOM   4280 O  OD2 . ASP B 1 124 ? 99.179  -8.108  26.017  1.00 25.41 ? 126  ASP B OD2 1 
ATOM   4281 N  N   . LEU B 1 125 ? 103.083 -11.969 26.319  1.00 15.91 ? 127  LEU B N   1 
ATOM   4282 C  CA  . LEU B 1 125 ? 104.131 -12.745 25.669  1.00 15.52 ? 127  LEU B CA  1 
ATOM   4283 C  C   . LEU B 1 125 ? 104.036 -14.226 26.044  1.00 14.70 ? 127  LEU B C   1 
ATOM   4284 O  O   . LEU B 1 125 ? 104.201 -15.101 25.193  1.00 14.25 ? 127  LEU B O   1 
ATOM   4285 C  CB  . LEU B 1 125 ? 105.512 -12.178 26.001  1.00 15.91 ? 127  LEU B CB  1 
ATOM   4286 C  CG  . LEU B 1 125 ? 105.828 -10.813 25.379  1.00 16.50 ? 127  LEU B CG  1 
ATOM   4287 C  CD1 . LEU B 1 125 ? 106.957 -10.109 26.117  1.00 16.88 ? 127  LEU B CD1 1 
ATOM   4288 C  CD2 . LEU B 1 125 ? 106.150 -10.951 23.899  1.00 16.41 ? 127  LEU B CD2 1 
ATOM   4289 N  N   . ILE B 1 126 ? 103.727 -14.497 27.310  1.00 14.13 ? 128  ILE B N   1 
ATOM   4290 C  CA  . ILE B 1 126 ? 103.498 -15.867 27.767  1.00 13.54 ? 128  ILE B CA  1 
ATOM   4291 C  C   . ILE B 1 126 ? 102.305 -16.502 27.055  1.00 13.87 ? 128  ILE B C   1 
ATOM   4292 O  O   . ILE B 1 126 ? 102.383 -17.639 26.595  1.00 12.56 ? 128  ILE B O   1 
ATOM   4293 C  CB  . ILE B 1 126 ? 103.267 -15.926 29.292  1.00 13.77 ? 128  ILE B CB  1 
ATOM   4294 C  CG1 . ILE B 1 126 ? 104.559 -15.592 30.043  1.00 13.15 ? 128  ILE B CG1 1 
ATOM   4295 C  CG2 . ILE B 1 126 ? 102.746 -17.296 29.704  1.00 12.38 ? 128  ILE B CG2 1 
ATOM   4296 C  CD1 . ILE B 1 126 ? 104.418 -15.643 31.550  1.00 13.34 ? 128  ILE B CD1 1 
ATOM   4297 N  N   . ASP B 1 127 ? 101.199 -15.764 26.976  1.00 15.36 ? 129  ASP B N   1 
ATOM   4298 C  CA  . ASP B 1 127 ? 99.963  -16.290 26.403  1.00 15.91 ? 129  ASP B CA  1 
ATOM   4299 C  C   . ASP B 1 127 ? 100.128 -16.624 24.920  1.00 14.75 ? 129  ASP B C   1 
ATOM   4300 O  O   . ASP B 1 127 ? 99.595  -17.622 24.436  1.00 14.12 ? 129  ASP B O   1 
ATOM   4301 C  CB  . ASP B 1 127 ? 98.810  -15.303 26.595  1.00 17.76 ? 129  ASP B CB  1 
ATOM   4302 C  CG  . ASP B 1 127 ? 98.298  -15.270 28.025  1.00 20.45 ? 129  ASP B CG  1 
ATOM   4303 O  OD1 . ASP B 1 127 ? 98.726  -16.113 28.841  1.00 22.01 ? 129  ASP B OD1 1 
ATOM   4304 O  OD2 . ASP B 1 127 ? 97.457  -14.401 28.333  1.00 25.92 ? 129  ASP B OD2 1 
ATOM   4305 N  N   . GLN B 1 128 ? 100.869 -15.789 24.201  1.00 14.36 ? 130  GLN B N   1 
ATOM   4306 C  CA  . GLN B 1 128 ? 101.107 -16.037 22.788  1.00 14.61 ? 130  GLN B CA  1 
ATOM   4307 C  C   . GLN B 1 128 ? 102.037 -17.234 22.597  1.00 15.29 ? 130  GLN B C   1 
ATOM   4308 O  O   . GLN B 1 128 ? 101.897 -17.992 21.637  1.00 15.48 ? 130  GLN B O   1 
ATOM   4309 C  CB  . GLN B 1 128 ? 101.690 -14.805 22.104  1.00 14.43 ? 130  GLN B CB  1 
ATOM   4310 C  CG  . GLN B 1 128 ? 101.714 -14.911 20.589  1.00 14.73 ? 130  GLN B CG  1 
ATOM   4311 C  CD  . GLN B 1 128 ? 100.320 -15.033 20.005  1.00 15.18 ? 130  GLN B CD  1 
ATOM   4312 O  OE1 . GLN B 1 128 ? 99.401  -14.321 20.418  1.00 13.41 ? 130  GLN B OE1 1 
ATOM   4313 N  NE2 . GLN B 1 128 ? 100.150 -15.948 19.050  1.00 13.67 ? 130  GLN B NE2 1 
ATOM   4314 N  N   . GLN B 1 129 ? 102.977 -17.405 23.521  1.00 15.02 ? 131  GLN B N   1 
ATOM   4315 C  CA  . GLN B 1 129 ? 103.877 -18.554 23.484  1.00 16.98 ? 131  GLN B CA  1 
ATOM   4316 C  C   . GLN B 1 129 ? 103.127 -19.857 23.773  1.00 14.40 ? 131  GLN B C   1 
ATOM   4317 O  O   . GLN B 1 129 ? 103.408 -20.890 23.168  1.00 14.31 ? 131  GLN B O   1 
ATOM   4318 C  CB  . GLN B 1 129 ? 105.032 -18.367 24.473  1.00 20.41 ? 131  GLN B CB  1 
ATOM   4319 C  CG  . GLN B 1 129 ? 106.168 -19.362 24.306  1.00 24.04 ? 131  GLN B CG  1 
ATOM   4320 C  CD  . GLN B 1 129 ? 107.011 -19.085 23.075  1.00 26.99 ? 131  GLN B CD  1 
ATOM   4321 O  OE1 . GLN B 1 129 ? 107.676 -19.979 22.551  1.00 34.35 ? 131  GLN B OE1 1 
ATOM   4322 N  NE2 . GLN B 1 129 ? 106.973 -17.845 22.596  1.00 26.61 ? 131  GLN B NE2 1 
ATOM   4323 N  N   . VAL B 1 130 ? 102.164 -19.802 24.687  1.00 12.78 ? 132  VAL B N   1 
ATOM   4324 C  CA  . VAL B 1 130 ? 101.326 -20.961 24.973  1.00 12.26 ? 132  VAL B CA  1 
ATOM   4325 C  C   . VAL B 1 130 ? 100.491 -21.339 23.756  1.00 11.69 ? 132  VAL B C   1 
ATOM   4326 O  O   . VAL B 1 130 ? 100.380 -22.515 23.403  1.00 10.40 ? 132  VAL B O   1 
ATOM   4327 C  CB  . VAL B 1 130 ? 100.378 -20.714 26.159  1.00 11.82 ? 132  VAL B CB  1 
ATOM   4328 C  CG1 . VAL B 1 130 ? 99.320  -21.804 26.216  1.00 11.66 ? 132  VAL B CG1 1 
ATOM   4329 C  CG2 . VAL B 1 130 ? 101.159 -20.665 27.465  1.00 11.73 ? 132  VAL B CG2 1 
ATOM   4330 N  N   . ALA B 1 131 ? 99.910  -20.331 23.115  1.00 10.63 ? 133  ALA B N   1 
ATOM   4331 C  CA  . ALA B 1 131 ? 99.148  -20.551 21.893  1.00 10.87 ? 133  ALA B CA  1 
ATOM   4332 C  C   . ALA B 1 131 ? 100.005 -21.286 20.868  1.00 11.20 ? 133  ALA B C   1 
ATOM   4333 O  O   . ALA B 1 131 ? 99.546  -22.224 20.217  1.00 12.10 ? 133  ALA B O   1 
ATOM   4334 C  CB  . ALA B 1 131 ? 98.667  -19.222 21.327  1.00 10.42 ? 133  ALA B CB  1 
ATOM   4335 N  N   . SER B 1 132 ? 101.252 -20.853 20.733  1.00 12.08 ? 134  SER B N   1 
ATOM   4336 C  CA  . SER B 1 132 ? 102.146 -21.397 19.715  1.00 13.69 ? 134  SER B CA  1 
ATOM   4337 C  C   . SER B 1 132 ? 102.545 -22.837 20.022  1.00 13.15 ? 134  SER B C   1 
ATOM   4338 O  O   . SER B 1 132 ? 102.671 -23.666 19.120  1.00 13.45 ? 134  SER B O   1 
ATOM   4339 C  CB  . SER B 1 132 ? 103.393 -20.524 19.584  1.00 15.31 ? 134  SER B CB  1 
ATOM   4340 O  OG  . SER B 1 132 ? 104.186 -20.952 18.492  1.00 19.02 ? 134  SER B OG  1 
ATOM   4341 N  N   . ILE B 1 133 ? 102.751 -23.122 21.302  1.00 12.05 ? 135  ILE B N   1 
ATOM   4342 C  CA  . ILE B 1 133 ? 103.088 -24.464 21.757  1.00 11.59 ? 135  ILE B CA  1 
ATOM   4343 C  C   . ILE B 1 133 ? 101.937 -25.430 21.487  1.00 11.61 ? 135  ILE B C   1 
ATOM   4344 O  O   . ILE B 1 133 ? 102.132 -26.489 20.893  1.00 10.61 ? 135  ILE B O   1 
ATOM   4345 C  CB  . ILE B 1 133 ? 103.442 -24.465 23.259  1.00 11.50 ? 135  ILE B CB  1 
ATOM   4346 C  CG1 . ILE B 1 133 ? 104.776 -23.745 23.482  1.00 12.53 ? 135  ILE B CG1 1 
ATOM   4347 C  CG2 . ILE B 1 133 ? 103.505 -25.886 23.797  1.00 11.77 ? 135  ILE B CG2 1 
ATOM   4348 C  CD1 . ILE B 1 133 ? 105.083 -23.438 24.934  1.00 12.70 ? 135  ILE B CD1 1 
ATOM   4349 N  N   . GLU B 1 134 ? 100.727 -25.014 21.850  1.00 11.61 ? 136  GLU B N   1 
ATOM   4350 C  CA  . GLU B 1 134 ? 99.537  -25.831 21.650  1.00 11.94 ? 136  GLU B CA  1 
ATOM   4351 C  C   . GLU B 1 134 ? 99.267  -26.116 20.175  1.00 11.39 ? 136  GLU B C   1 
ATOM   4352 O  O   . GLU B 1 134 ? 98.921  -27.239 19.808  1.00 11.45 ? 136  GLU B O   1 
ATOM   4353 C  CB  . GLU B 1 134 ? 98.315  -25.176 22.304  1.00 11.83 ? 136  GLU B CB  1 
ATOM   4354 C  CG  . GLU B 1 134 ? 98.372  -25.183 23.824  1.00 12.86 ? 136  GLU B CG  1 
ATOM   4355 C  CD  . GLU B 1 134 ? 97.090  -24.711 24.480  1.00 14.39 ? 136  GLU B CD  1 
ATOM   4356 O  OE1 . GLU B 1 134 ? 96.221  -24.149 23.778  1.00 13.53 ? 136  GLU B OE1 1 
ATOM   4357 O  OE2 . GLU B 1 134 ? 96.967  -24.871 25.713  1.00 14.95 ? 136  GLU B OE2 1 
ATOM   4358 N  N   . SER B 1 135 ? 99.411  -25.102 19.330  1.00 11.42 ? 137  SER B N   1 
ATOM   4359 C  CA  . SER B 1 135 ? 99.171  -25.290 17.903  1.00 11.83 ? 137  SER B CA  1 
ATOM   4360 C  C   . SER B 1 135 ? 100.258 -26.155 17.264  1.00 12.16 ? 137  SER B C   1 
ATOM   4361 O  O   . SER B 1 135 ? 99.980  -26.956 16.370  1.00 11.93 ? 137  SER B O   1 
ATOM   4362 C  CB  . SER B 1 135 ? 99.044  -23.945 17.181  1.00 11.94 ? 137  SER B CB  1 
ATOM   4363 O  OG  . SER B 1 135 ? 100.307 -23.331 17.003  1.00 12.33 ? 137  SER B OG  1 
ATOM   4364 N  N   . THR B 1 136 ? 101.488 -26.018 17.752  1.00 12.05 ? 138  THR B N   1 
ATOM   4365 C  CA  . THR B 1 136 ? 102.602 -26.810 17.245  1.00 12.39 ? 138  THR B CA  1 
ATOM   4366 C  C   . THR B 1 136 ? 102.427 -28.292 17.578  1.00 12.26 ? 138  THR B C   1 
ATOM   4367 O  O   . THR B 1 136 ? 102.581 -29.156 16.716  1.00 11.28 ? 138  THR B O   1 
ATOM   4368 C  CB  . THR B 1 136 ? 103.947 -26.321 17.810  1.00 13.97 ? 138  THR B CB  1 
ATOM   4369 O  OG1 . THR B 1 136 ? 104.206 -24.990 17.346  1.00 14.70 ? 138  THR B OG1 1 
ATOM   4370 C  CG2 . THR B 1 136 ? 105.078 -27.238 17.361  1.00 15.12 ? 138  THR B CG2 1 
ATOM   4371 N  N   . PHE B 1 137 ? 102.103 -28.578 18.835  1.00 11.76 ? 139  PHE B N   1 
ATOM   4372 C  CA  . PHE B 1 137 ? 101.967 -29.952 19.296  1.00 11.29 ? 139  PHE B CA  1 
ATOM   4373 C  C   . PHE B 1 137 ? 100.633 -30.566 18.881  1.00 12.60 ? 139  PHE B C   1 
ATOM   4374 O  O   . PHE B 1 137 ? 100.518 -31.786 18.739  1.00 12.20 ? 139  PHE B O   1 
ATOM   4375 C  CB  . PHE B 1 137 ? 102.135 -30.024 20.815  1.00 10.98 ? 139  PHE B CB  1 
ATOM   4376 C  CG  . PHE B 1 137 ? 103.569 -30.045 21.261  1.00 11.13 ? 139  PHE B CG  1 
ATOM   4377 C  CD1 . PHE B 1 137 ? 104.290 -28.869 21.375  1.00 10.94 ? 139  PHE B CD1 1 
ATOM   4378 C  CD2 . PHE B 1 137 ? 104.215 -31.248 21.496  1.00 11.13 ? 139  PHE B CD2 1 
ATOM   4379 C  CE1 . PHE B 1 137 ? 105.623 -28.887 21.751  1.00 11.36 ? 139  PHE B CE1 1 
ATOM   4380 C  CE2 . PHE B 1 137 ? 105.544 -31.273 21.883  1.00 11.24 ? 139  PHE B CE2 1 
ATOM   4381 C  CZ  . PHE B 1 137 ? 106.250 -30.093 22.002  1.00 10.84 ? 139  PHE B CZ  1 
ATOM   4382 N  N   . GLY B 1 138 ? 99.622  -29.719 18.706  1.00 12.62 ? 140  GLY B N   1 
ATOM   4383 C  CA  . GLY B 1 138 ? 98.281  -30.188 18.387  1.00 14.05 ? 140  GLY B CA  1 
ATOM   4384 C  C   . GLY B 1 138 ? 97.767  -31.190 19.404  1.00 14.35 ? 140  GLY B C   1 
ATOM   4385 O  O   . GLY B 1 138 ? 97.938  -31.013 20.612  1.00 13.76 ? 140  GLY B O   1 
ATOM   4386 N  N   . SER B 1 139 ? 97.181  -32.274 18.910  1.00 15.88 ? 141  SER B N   1 
ATOM   4387 C  CA  . SER B 1 139 ? 96.534  -33.255 19.773  1.00 16.74 ? 141  SER B CA  1 
ATOM   4388 C  C   . SER B 1 139 ? 97.534  -34.136 20.524  1.00 15.55 ? 141  SER B C   1 
ATOM   4389 O  O   . SER B 1 139 ? 97.136  -34.997 21.309  1.00 16.22 ? 141  SER B O   1 
ATOM   4390 C  CB  . SER B 1 139 ? 95.593  -34.137 18.953  1.00 18.42 ? 141  SER B CB  1 
ATOM   4391 O  OG  . SER B 1 139 ? 96.295  -34.747 17.885  1.00 24.07 ? 141  SER B OG  1 
ATOM   4392 N  N   . SER B 1 140 ? 98.825  -33.935 20.274  1.00 15.00 ? 142  SER B N   1 
ATOM   4393 C  CA  . SER B 1 140 ? 99.855  -34.748 20.925  1.00 14.79 ? 142  SER B CA  1 
ATOM   4394 C  C   . SER B 1 140 ? 100.078 -34.347 22.384  1.00 15.52 ? 142  SER B C   1 
ATOM   4395 O  O   . SER B 1 140 ? 100.715 -35.072 23.149  1.00 15.27 ? 142  SER B O   1 
ATOM   4396 C  CB  . SER B 1 140 ? 101.169 -34.711 20.142  1.00 14.27 ? 142  SER B CB  1 
ATOM   4397 O  OG  . SER B 1 140 ? 101.842 -33.472 20.288  1.00 14.07 ? 142  SER B OG  1 
ATOM   4398 N  N   . ILE B 1 141 ? 99.507  -33.213 22.774  1.00 16.04 ? 143  ILE B N   1 
ATOM   4399 C  CA  . ILE B 1 141 ? 99.622  -32.721 24.143  1.00 16.04 ? 143  ILE B CA  1 
ATOM   4400 C  C   . ILE B 1 141 ? 98.245  -32.354 24.689  1.00 16.09 ? 143  ILE B C   1 
ATOM   4401 O  O   . ILE B 1 141 ? 97.395  -31.854 23.953  1.00 16.78 ? 143  ILE B O   1 
ATOM   4402 C  CB  . ILE B 1 141 ? 100.539 -31.482 24.200  1.00 16.65 ? 143  ILE B CB  1 
ATOM   4403 C  CG1 . ILE B 1 141 ? 100.987 -31.198 25.632  1.00 17.89 ? 143  ILE B CG1 1 
ATOM   4404 C  CG2 . ILE B 1 141 ? 99.839  -30.266 23.615  1.00 16.81 ? 143  ILE B CG2 1 
ATOM   4405 C  CD1 . ILE B 1 141 ? 102.040 -30.112 25.722  1.00 18.45 ? 143  ILE B CD1 1 
ATOM   4406 N  N   . SER B 1 142 ? 98.013  -32.637 25.968  1.00 15.73 ? 144  SER B N   1 
ATOM   4407 C  CA  . SER B 1 142 ? 96.821  -32.154 26.660  1.00 15.36 ? 144  SER B CA  1 
ATOM   4408 C  C   . SER B 1 142 ? 97.200  -31.287 27.852  1.00 14.53 ? 144  SER B C   1 
ATOM   4409 O  O   . SER B 1 142 ? 98.082  -31.642 28.628  1.00 12.86 ? 144  SER B O   1 
ATOM   4410 C  CB  . SER B 1 142 ? 95.958  -33.327 27.137  1.00 16.04 ? 144  SER B CB  1 
ATOM   4411 O  OG  . SER B 1 142 ? 95.221  -33.896 26.068  1.00 18.62 ? 144  SER B OG  1 
ATOM   4412 N  N   . LYS B 1 143 ? 96.529  -30.150 27.999  1.00 14.52 ? 145  LYS B N   1 
ATOM   4413 C  CA  . LYS B 1 143 ? 96.676  -29.338 29.201  1.00 13.44 ? 145  LYS B CA  1 
ATOM   4414 C  C   . LYS B 1 143 ? 95.830  -29.918 30.329  1.00 13.24 ? 145  LYS B C   1 
ATOM   4415 O  O   . LYS B 1 143 ? 94.619  -30.070 30.188  1.00 13.34 ? 145  LYS B O   1 
ATOM   4416 C  CB  . LYS B 1 143 ? 96.259  -27.891 28.934  1.00 14.47 ? 145  LYS B CB  1 
ATOM   4417 C  CG  . LYS B 1 143 ? 96.517  -26.958 30.107  1.00 15.67 ? 145  LYS B CG  1 
ATOM   4418 C  CD  . LYS B 1 143 ? 95.822  -25.620 29.918  1.00 17.87 ? 145  LYS B CD  1 
ATOM   4419 C  CE  . LYS B 1 143 ? 95.944  -24.770 31.170  1.00 19.44 ? 145  LYS B CE  1 
ATOM   4420 N  NZ  . LYS B 1 143 ? 96.029  -23.317 30.851  1.00 23.06 ? 145  LYS B NZ  1 
ATOM   4421 N  N   . LEU B 1 144 ? 96.468  -30.218 31.454  1.00 11.79 ? 146  LEU B N   1 
ATOM   4422 C  CA  . LEU B 1 144 ? 95.763  -30.790 32.597  1.00 11.71 ? 146  LEU B CA  1 
ATOM   4423 C  C   . LEU B 1 144 ? 95.475  -29.731 33.653  1.00 11.36 ? 146  LEU B C   1 
ATOM   4424 O  O   . LEU B 1 144 ? 94.445  -29.777 34.324  1.00 11.18 ? 146  LEU B O   1 
ATOM   4425 C  CB  . LEU B 1 144 ? 96.575  -31.933 33.215  1.00 11.87 ? 146  LEU B CB  1 
ATOM   4426 C  CG  . LEU B 1 144 ? 96.787  -33.156 32.322  1.00 12.89 ? 146  LEU B CG  1 
ATOM   4427 C  CD1 . LEU B 1 144 ? 97.417  -34.293 33.113  1.00 12.48 ? 146  LEU B CD1 1 
ATOM   4428 C  CD2 . LEU B 1 144 ? 95.471  -33.598 31.705  1.00 12.71 ? 146  LEU B CD2 1 
ATOM   4429 N  N   . TYR B 1 145 ? 96.385  -28.771 33.776  1.00 9.92  ? 147  TYR B N   1 
ATOM   4430 C  CA  . TYR B 1 145 ? 96.307  -27.753 34.818  1.00 9.94  ? 147  TYR B CA  1 
ATOM   4431 C  C   . TYR B 1 145 ? 97.341  -26.675 34.518  1.00 9.87  ? 147  TYR B C   1 
ATOM   4432 O  O   . TYR B 1 145 ? 98.369  -26.954 33.904  1.00 9.72  ? 147  TYR B O   1 
ATOM   4433 C  CB  . TYR B 1 145 ? 96.590  -28.378 36.189  1.00 9.72  ? 147  TYR B CB  1 
ATOM   4434 C  CG  . TYR B 1 145 ? 96.439  -27.420 37.350  1.00 9.98  ? 147  TYR B CG  1 
ATOM   4435 C  CD1 . TYR B 1 145 ? 95.223  -26.796 37.609  1.00 9.85  ? 147  TYR B CD1 1 
ATOM   4436 C  CD2 . TYR B 1 145 ? 97.513  -27.144 38.193  1.00 10.35 ? 147  TYR B CD2 1 
ATOM   4437 C  CE1 . TYR B 1 145 ? 95.082  -25.914 38.666  1.00 9.97  ? 147  TYR B CE1 1 
ATOM   4438 C  CE2 . TYR B 1 145 ? 97.384  -26.263 39.252  1.00 10.20 ? 147  TYR B CE2 1 
ATOM   4439 C  CZ  . TYR B 1 145 ? 96.165  -25.652 39.484  1.00 10.51 ? 147  TYR B CZ  1 
ATOM   4440 O  OH  . TYR B 1 145 ? 96.033  -24.784 40.547  1.00 10.76 ? 147  TYR B OH  1 
ATOM   4441 N  N   . SER B 1 146 ? 97.073  -25.445 34.943  1.00 10.02 ? 148  SER B N   1 
ATOM   4442 C  CA  . SER B 1 146 ? 98.112  -24.419 34.941  1.00 10.55 ? 148  SER B CA  1 
ATOM   4443 C  C   . SER B 1 146 ? 97.984  -23.456 36.112  1.00 10.91 ? 148  SER B C   1 
ATOM   4444 O  O   . SER B 1 146 ? 96.904  -23.286 36.681  1.00 11.50 ? 148  SER B O   1 
ATOM   4445 C  CB  . SER B 1 146 ? 98.125  -23.655 33.613  1.00 10.97 ? 148  SER B CB  1 
ATOM   4446 O  OG  . SER B 1 146 ? 96.955  -22.872 33.464  1.00 11.52 ? 148  SER B OG  1 
ATOM   4447 N  N   . LEU B 1 147 ? 99.105  -22.846 36.481  1.00 10.29 ? 149  LEU B N   1 
ATOM   4448 C  CA  . LEU B 1 147 ? 99.125  -21.837 37.525  1.00 10.41 ? 149  LEU B CA  1 
ATOM   4449 C  C   . LEU B 1 147 ? 99.910  -20.631 37.037  1.00 10.83 ? 149  LEU B C   1 
ATOM   4450 O  O   . LEU B 1 147 ? 101.078 -20.753 36.668  1.00 9.64  ? 149  LEU B O   1 
ATOM   4451 C  CB  . LEU B 1 147 ? 99.759  -22.399 38.803  1.00 9.73  ? 149  LEU B CB  1 
ATOM   4452 C  CG  . LEU B 1 147 ? 99.749  -21.478 40.029  1.00 10.45 ? 149  LEU B CG  1 
ATOM   4453 C  CD1 . LEU B 1 147 ? 98.326  -21.063 40.383  1.00 9.59  ? 149  LEU B CD1 1 
ATOM   4454 C  CD2 . LEU B 1 147 ? 100.423 -22.162 41.208  1.00 9.62  ? 149  LEU B CD2 1 
ATOM   4455 N  N   . SER B 1 148 ? 99.252  -19.477 37.003  1.00 11.67 ? 150  SER B N   1 
ATOM   4456 C  CA  . SER B 1 148 ? 99.925  -18.223 36.700  1.00 12.35 ? 150  SER B CA  1 
ATOM   4457 C  C   . SER B 1 148 ? 100.498 -17.593 37.965  1.00 12.91 ? 150  SER B C   1 
ATOM   4458 O  O   . SER B 1 148 ? 99.906  -17.687 39.042  1.00 14.53 ? 150  SER B O   1 
ATOM   4459 C  CB  . SER B 1 148 ? 98.964  -17.255 36.007  1.00 13.78 ? 150  SER B CB  1 
ATOM   4460 O  OG  . SER B 1 148 ? 98.417  -17.847 34.838  1.00 14.22 ? 150  SER B OG  1 
ATOM   4461 N  N   . ALA B 1 149 ? 101.669 -16.982 37.836  1.00 12.25 ? 151  ALA B N   1 
ATOM   4462 C  CA  . ALA B 1 149 ? 102.377 -16.434 38.987  1.00 11.75 ? 151  ALA B CA  1 
ATOM   4463 C  C   . ALA B 1 149 ? 103.030 -15.111 38.610  1.00 11.58 ? 151  ALA B C   1 
ATOM   4464 O  O   . ALA B 1 149 ? 103.199 -14.810 37.432  1.00 11.61 ? 151  ALA B O   1 
ATOM   4465 C  CB  . ALA B 1 149 ? 103.422 -17.422 39.488  1.00 10.70 ? 151  ALA B CB  1 
ATOM   4466 N  N   . SER B 1 150 ? 103.388 -14.323 39.616  1.00 11.06 ? 152  SER B N   1 
ATOM   4467 C  CA  . SER B 1 150 ? 103.901 -12.981 39.379  1.00 11.97 ? 152  SER B CA  1 
ATOM   4468 C  C   . SER B 1 150 ? 104.731 -12.469 40.549  1.00 12.05 ? 152  SER B C   1 
ATOM   4469 O  O   . SER B 1 150 ? 104.405 -12.711 41.713  1.00 11.78 ? 152  SER B O   1 
ATOM   4470 C  CB  . SER B 1 150 ? 102.748 -12.012 39.099  1.00 13.10 ? 152  SER B CB  1 
ATOM   4471 O  OG  . SER B 1 150 ? 103.232 -10.707 38.831  1.00 12.95 ? 152  SER B OG  1 
ATOM   4472 N  N   . ILE B 1 151 ? 105.804 -11.754 40.228  1.00 12.19 ? 153  ILE B N   1 
ATOM   4473 C  CA  . ILE B 1 151 ? 106.449 -10.864 41.184  1.00 12.95 ? 153  ILE B CA  1 
ATOM   4474 C  C   . ILE B 1 151 ? 105.426 -9.857  41.694  1.00 13.14 ? 153  ILE B C   1 
ATOM   4475 O  O   . ILE B 1 151 ? 104.601 -9.361  40.926  1.00 12.14 ? 153  ILE B O   1 
ATOM   4476 C  CB  . ILE B 1 151 ? 107.620 -10.107 40.525  1.00 13.69 ? 153  ILE B CB  1 
ATOM   4477 C  CG1 . ILE B 1 151 ? 108.557 -11.088 39.814  1.00 14.38 ? 153  ILE B CG1 1 
ATOM   4478 C  CG2 . ILE B 1 151 ? 108.381 -9.283  41.551  1.00 14.07 ? 153  ILE B CG2 1 
ATOM   4479 C  CD1 . ILE B 1 151 ? 109.070 -12.199 40.706  1.00 15.31 ? 153  ILE B CD1 1 
ATOM   4480 N  N   . ARG B 1 152 ? 105.463 -9.581  42.995  1.00 12.20 ? 154  ARG B N   1 
ATOM   4481 C  CA  . ARG B 1 152 ? 104.516 -8.663  43.605  1.00 12.67 ? 154  ARG B CA  1 
ATOM   4482 C  C   . ARG B 1 152 ? 104.874 -7.216  43.271  1.00 13.83 ? 154  ARG B C   1 
ATOM   4483 O  O   . ARG B 1 152 ? 105.999 -6.932  42.863  1.00 13.48 ? 154  ARG B O   1 
ATOM   4484 C  CB  . ARG B 1 152 ? 104.454 -8.886  45.119  1.00 13.14 ? 154  ARG B CB  1 
ATOM   4485 C  CG  . ARG B 1 152 ? 103.936 -10.265 45.505  1.00 13.16 ? 154  ARG B CG  1 
ATOM   4486 C  CD  . ARG B 1 152 ? 103.626 -10.352 46.991  1.00 13.72 ? 154  ARG B CD  1 
ATOM   4487 N  NE  . ARG B 1 152 ? 102.837 -9.206  47.425  1.00 13.59 ? 154  ARG B NE  1 
ATOM   4488 C  CZ  . ARG B 1 152 ? 103.034 -8.548  48.560  1.00 13.83 ? 154  ARG B CZ  1 
ATOM   4489 N  NH1 . ARG B 1 152 ? 103.988 -8.933  49.400  1.00 13.96 ? 154  ARG B NH1 1 
ATOM   4490 N  NH2 . ARG B 1 152 ? 102.281 -7.496  48.848  1.00 14.24 ? 154  ARG B NH2 1 
ATOM   4491 N  N   . PRO B 1 153 ? 103.893 -6.308  43.379  1.00 14.69 ? 155  PRO B N   1 
ATOM   4492 C  CA  . PRO B 1 153 ? 104.024 -4.980  42.782  1.00 15.81 ? 155  PRO B CA  1 
ATOM   4493 C  C   . PRO B 1 153 ? 104.897 -4.040  43.608  1.00 16.33 ? 155  PRO B C   1 
ATOM   4494 O  O   . PRO B 1 153 ? 105.027 -4.216  44.819  1.00 15.63 ? 155  PRO B O   1 
ATOM   4495 C  CB  . PRO B 1 153 ? 102.581 -4.467  42.740  1.00 16.36 ? 155  PRO B CB  1 
ATOM   4496 C  CG  . PRO B 1 153 ? 101.865 -5.234  43.795  1.00 16.72 ? 155  PRO B CG  1 
ATOM   4497 C  CD  . PRO B 1 153 ? 102.522 -6.581  43.846  1.00 14.99 ? 155  PRO B CD  1 
ATOM   4498 N  N   . GLY B 1 154 ? 105.515 -3.070  42.938  1.00 17.01 ? 156  GLY B N   1 
ATOM   4499 C  CA  . GLY B 1 154 ? 106.145 -1.935  43.611  1.00 17.69 ? 156  GLY B CA  1 
ATOM   4500 C  C   . GLY B 1 154 ? 107.167 -2.320  44.663  1.00 18.87 ? 156  GLY B C   1 
ATOM   4501 O  O   . GLY B 1 154 ? 108.099 -3.081  44.395  1.00 17.76 ? 156  GLY B O   1 
ATOM   4502 N  N   . ASN B 1 155 ? 106.983 -1.793  45.870  1.00 21.11 ? 157  ASN B N   1 
ATOM   4503 C  CA  . ASN B 1 155 ? 107.930 -1.992  46.963  1.00 22.64 ? 157  ASN B CA  1 
ATOM   4504 C  C   . ASN B 1 155 ? 107.975 -3.427  47.464  1.00 20.18 ? 157  ASN B C   1 
ATOM   4505 O  O   . ASN B 1 155 ? 108.858 -3.792  48.239  1.00 21.83 ? 157  ASN B O   1 
ATOM   4506 C  CB  . ASN B 1 155 ? 107.593 -1.065  48.134  1.00 25.21 ? 157  ASN B CB  1 
ATOM   4507 C  CG  . ASN B 1 155 ? 108.443 0.186   48.143  1.00 28.09 ? 157  ASN B CG  1 
ATOM   4508 O  OD1 . ASN B 1 155 ? 109.454 0.267   47.444  1.00 29.27 ? 157  ASN B OD1 1 
ATOM   4509 N  ND2 . ASN B 1 155 ? 108.038 1.171   48.935  1.00 33.46 ? 157  ASN B ND2 1 
ATOM   4510 N  N   . GLU B 1 156 ? 106.975 -4.214  47.086  1.00 18.87 ? 158  GLU B N   1 
ATOM   4511 C  CA  . GLU B 1 156 ? 106.884 -5.592  47.545  1.00 18.04 ? 158  GLU B CA  1 
ATOM   4512 C  C   . GLU B 1 156 ? 107.446 -6.557  46.507  1.00 16.13 ? 158  GLU B C   1 
ATOM   4513 O  O   . GLU B 1 156 ? 107.350 -7.775  46.662  1.00 15.05 ? 158  GLU B O   1 
ATOM   4514 C  CB  . GLU B 1 156 ? 105.434 -5.948  47.882  1.00 19.36 ? 158  GLU B CB  1 
ATOM   4515 C  CG  . GLU B 1 156 ? 104.879 -5.196  49.083  1.00 20.38 ? 158  GLU B CG  1 
ATOM   4516 C  CD  . GLU B 1 156 ? 105.497 -5.654  50.389  1.00 23.15 ? 158  GLU B CD  1 
ATOM   4517 O  OE1 . GLU B 1 156 ? 105.597 -6.880  50.605  1.00 22.50 ? 158  GLU B OE1 1 
ATOM   4518 O  OE2 . GLU B 1 156 ? 105.893 -4.789  51.199  1.00 25.63 ? 158  GLU B OE2 1 
ATOM   4519 N  N   . ALA B 1 157 ? 108.038 -6.011  45.449  1.00 15.44 ? 159  ALA B N   1 
ATOM   4520 C  CA  . ALA B 1 157 ? 108.698 -6.842  44.448  1.00 14.94 ? 159  ALA B CA  1 
ATOM   4521 C  C   . ALA B 1 157 ? 109.815 -7.643  45.104  1.00 14.66 ? 159  ALA B C   1 
ATOM   4522 O  O   . ALA B 1 157 ? 110.679 -7.079  45.775  1.00 15.14 ? 159  ALA B O   1 
ATOM   4523 C  CB  . ALA B 1 157 ? 109.248 -5.985  43.316  1.00 15.32 ? 159  ALA B CB  1 
ATOM   4524 N  N   . GLY B 1 158 ? 109.781 -8.959  44.920  1.00 13.84 ? 160  GLY B N   1 
ATOM   4525 C  CA  . GLY B 1 158 ? 110.753 -9.850  45.547  1.00 13.84 ? 160  GLY B CA  1 
ATOM   4526 C  C   . GLY B 1 158 ? 110.311 -10.332 46.918  1.00 13.63 ? 160  GLY B C   1 
ATOM   4527 O  O   . GLY B 1 158 ? 110.988 -11.145 47.544  1.00 14.21 ? 160  GLY B O   1 
ATOM   4528 N  N   . HIS B 1 159 ? 109.193 -9.802  47.405  1.00 13.06 ? 161  HIS B N   1 
ATOM   4529 C  CA  . HIS B 1 159 ? 108.598 -10.293 48.645  1.00 13.11 ? 161  HIS B CA  1 
ATOM   4530 C  C   . HIS B 1 159 ? 107.521 -11.320 48.311  1.00 12.83 ? 161  HIS B C   1 
ATOM   4531 O  O   . HIS B 1 159 ? 106.917 -11.270 47.238  1.00 13.06 ? 161  HIS B O   1 
ATOM   4532 C  CB  . HIS B 1 159 ? 107.985 -9.141  49.447  1.00 13.28 ? 161  HIS B CB  1 
ATOM   4533 C  CG  . HIS B 1 159 ? 108.978 -8.117  49.907  1.00 13.54 ? 161  HIS B CG  1 
ATOM   4534 N  ND1 . HIS B 1 159 ? 109.099 -7.743  51.229  1.00 13.88 ? 161  HIS B ND1 1 
ATOM   4535 C  CD2 . HIS B 1 159 ? 109.829 -7.326  49.214  1.00 13.71 ? 161  HIS B CD2 1 
ATOM   4536 C  CE1 . HIS B 1 159 ? 110.011 -6.793  51.334  1.00 13.54 ? 161  HIS B CE1 1 
ATOM   4537 N  NE2 . HIS B 1 159 ? 110.475 -6.527  50.126  1.00 14.52 ? 161  HIS B NE2 1 
ATOM   4538 N  N   . GLU B 1 160 ? 107.287 -12.261 49.217  1.00 12.76 ? 162  GLU B N   1 
ATOM   4539 C  CA  . GLU B 1 160 ? 106.168 -13.177 49.047  1.00 13.35 ? 162  GLU B CA  1 
ATOM   4540 C  C   . GLU B 1 160 ? 104.916 -12.633 49.727  1.00 13.25 ? 162  GLU B C   1 
ATOM   4541 O  O   . GLU B 1 160 ? 104.899 -11.488 50.184  1.00 12.22 ? 162  GLU B O   1 
ATOM   4542 C  CB  . GLU B 1 160 ? 106.517 -14.587 49.532  1.00 14.51 ? 162  GLU B CB  1 
ATOM   4543 C  CG  . GLU B 1 160 ? 107.100 -14.649 50.929  1.00 15.26 ? 162  GLU B CG  1 
ATOM   4544 C  CD  . GLU B 1 160 ? 106.057 -14.390 51.996  1.00 16.04 ? 162  GLU B CD  1 
ATOM   4545 O  OE1 . GLU B 1 160 ? 105.001 -15.060 51.973  1.00 16.98 ? 162  GLU B OE1 1 
ATOM   4546 O  OE2 . GLU B 1 160 ? 106.290 -13.511 52.851  1.00 16.72 ? 162  GLU B OE2 1 
ATOM   4547 N  N   . MET B 1 161 ? 103.852 -13.431 49.742  1.00 12.93 ? 163  MET B N   1 
ATOM   4548 C  CA  . MET B 1 161 ? 102.524 -12.913 50.059  1.00 12.55 ? 163  MET B CA  1 
ATOM   4549 C  C   . MET B 1 161 ? 102.363 -12.496 51.524  1.00 12.58 ? 163  MET B C   1 
ATOM   4550 O  O   . MET B 1 161 ? 101.528 -11.648 51.838  1.00 13.28 ? 163  MET B O   1 
ATOM   4551 C  CB  . MET B 1 161 ? 101.436 -13.911 49.651  1.00 12.41 ? 163  MET B CB  1 
ATOM   4552 C  CG  . MET B 1 161 ? 101.053 -13.850 48.178  1.00 12.58 ? 163  MET B CG  1 
ATOM   4553 S  SD  . MET B 1 161 ? 100.239 -12.299 47.733  1.00 12.91 ? 163  MET B SD  1 
ATOM   4554 C  CE  . MET B 1 161 ? 100.257 -12.397 45.939  1.00 12.31 ? 163  MET B CE  1 
ATOM   4555 N  N   . PHE B 1 162 ? 103.137 -13.102 52.421  1.00 13.14 ? 164  PHE B N   1 
ATOM   4556 C  CA  . PHE B 1 162 ? 103.127 -12.687 53.830  1.00 13.56 ? 164  PHE B CA  1 
ATOM   4557 C  C   . PHE B 1 162 ? 103.847 -11.351 54.002  1.00 13.48 ? 164  PHE B C   1 
ATOM   4558 O  O   . PHE B 1 162 ? 103.713 -10.690 55.031  1.00 14.89 ? 164  PHE B O   1 
ATOM   4559 C  CB  . PHE B 1 162 ? 103.770 -13.747 54.736  1.00 13.04 ? 164  PHE B CB  1 
ATOM   4560 C  CG  . PHE B 1 162 ? 102.913 -14.961 54.962  1.00 13.41 ? 164  PHE B CG  1 
ATOM   4561 C  CD1 . PHE B 1 162 ? 101.535 -14.847 55.076  1.00 12.70 ? 164  PHE B CD1 1 
ATOM   4562 C  CD2 . PHE B 1 162 ? 103.490 -16.215 55.097  1.00 14.54 ? 164  PHE B CD2 1 
ATOM   4563 C  CE1 . PHE B 1 162 ? 100.747 -15.965 55.282  1.00 13.21 ? 164  PHE B CE1 1 
ATOM   4564 C  CE2 . PHE B 1 162 ? 102.709 -17.337 55.313  1.00 13.96 ? 164  PHE B CE2 1 
ATOM   4565 C  CZ  . PHE B 1 162 ? 101.334 -17.213 55.401  1.00 13.64 ? 164  PHE B CZ  1 
ATOM   4566 N  N   . GLY B 1 163 ? 104.645 -10.981 53.007  1.00 13.20 ? 165  GLY B N   1 
ATOM   4567 C  CA  . GLY B 1 163 ? 105.289 -9.673  52.985  1.00 12.58 ? 165  GLY B CA  1 
ATOM   4568 C  C   . GLY B 1 163 ? 106.794 -9.701  53.192  1.00 12.59 ? 165  GLY B C   1 
ATOM   4569 O  O   . GLY B 1 163 ? 107.429 -8.651  53.281  1.00 12.45 ? 165  GLY B O   1 
ATOM   4570 N  N   . PHE B 1 164 ? 107.373 -10.897 53.251  1.00 12.22 ? 166  PHE B N   1 
ATOM   4571 C  CA  . PHE B 1 164 ? 108.803 -11.035 53.525  1.00 12.91 ? 166  PHE B CA  1 
ATOM   4572 C  C   . PHE B 1 164 ? 109.649 -11.109 52.259  1.00 13.06 ? 166  PHE B C   1 
ATOM   4573 O  O   . PHE B 1 164 ? 109.313 -11.830 51.318  1.00 12.30 ? 166  PHE B O   1 
ATOM   4574 C  CB  . PHE B 1 164 ? 109.068 -12.254 54.407  1.00 13.22 ? 166  PHE B CB  1 
ATOM   4575 C  CG  . PHE B 1 164 ? 108.490 -12.132 55.786  1.00 12.74 ? 166  PHE B CG  1 
ATOM   4576 C  CD1 . PHE B 1 164 ? 107.139 -12.343 56.004  1.00 12.78 ? 166  PHE B CD1 1 
ATOM   4577 C  CD2 . PHE B 1 164 ? 109.288 -11.772 56.856  1.00 13.11 ? 166  PHE B CD2 1 
ATOM   4578 C  CE1 . PHE B 1 164 ? 106.596 -12.200 57.267  1.00 13.18 ? 166  PHE B CE1 1 
ATOM   4579 C  CE2 . PHE B 1 164 ? 108.754 -11.629 58.121  1.00 12.84 ? 166  PHE B CE2 1 
ATOM   4580 C  CZ  . PHE B 1 164 ? 107.406 -11.844 58.329  1.00 12.80 ? 166  PHE B CZ  1 
ATOM   4581 N  N   . LEU B 1 165 ? 110.755 -10.369 52.248  1.00 13.03 ? 167  LEU B N   1 
ATOM   4582 C  CA  . LEU B 1 165 ? 111.721 -10.466 51.160  1.00 13.72 ? 167  LEU B CA  1 
ATOM   4583 C  C   . LEU B 1 165 ? 112.202 -11.903 51.031  1.00 14.36 ? 167  LEU B C   1 
ATOM   4584 O  O   . LEU B 1 165 ? 112.575 -12.532 52.019  1.00 14.34 ? 167  LEU B O   1 
ATOM   4585 C  CB  . LEU B 1 165 ? 112.910 -9.533  51.395  1.00 13.65 ? 167  LEU B CB  1 
ATOM   4586 C  CG  . LEU B 1 165 ? 113.884 -9.397  50.221  1.00 14.06 ? 167  LEU B CG  1 
ATOM   4587 C  CD1 . LEU B 1 165 ? 113.191 -8.767  49.020  1.00 14.17 ? 167  LEU B CD1 1 
ATOM   4588 C  CD2 . LEU B 1 165 ? 115.124 -8.604  50.613  1.00 13.79 ? 167  LEU B CD2 1 
ATOM   4589 N  N   A ASP B 1 166 ? 112.196 -12.415 49.805  0.50 15.22 ? 168  ASP B N   1 
ATOM   4590 N  N   B ASP B 1 166 ? 112.153 -12.431 49.814  0.50 15.73 ? 168  ASP B N   1 
ATOM   4591 C  CA  A ASP B 1 166 ? 112.494 -13.821 49.564  0.50 17.14 ? 168  ASP B CA  1 
ATOM   4592 C  CA  B ASP B 1 166 ? 112.510 -13.822 49.578  0.50 17.42 ? 168  ASP B CA  1 
ATOM   4593 C  C   A ASP B 1 166 ? 113.542 -13.977 48.465  0.50 18.49 ? 168  ASP B C   1 
ATOM   4594 C  C   B ASP B 1 166 ? 113.702 -13.923 48.633  0.50 18.47 ? 168  ASP B C   1 
ATOM   4595 O  O   A ASP B 1 166 ? 113.769 -13.059 47.675  0.50 20.04 ? 168  ASP B O   1 
ATOM   4596 O  O   B ASP B 1 166 ? 114.191 -12.914 48.124  0.50 19.90 ? 168  ASP B O   1 
ATOM   4597 C  CB  A ASP B 1 166 ? 111.214 -14.577 49.197  0.50 17.95 ? 168  ASP B CB  1 
ATOM   4598 C  CB  B ASP B 1 166 ? 111.311 -14.596 49.022  0.50 18.72 ? 168  ASP B CB  1 
ATOM   4599 C  CG  A ASP B 1 166 ? 111.417 -16.077 49.154  0.50 18.83 ? 168  ASP B CG  1 
ATOM   4600 C  CG  B ASP B 1 166 ? 110.906 -14.129 47.637  0.50 19.19 ? 168  ASP B CG  1 
ATOM   4601 O  OD1 A ASP B 1 166 ? 112.571 -16.525 49.322  0.50 17.96 ? 168  ASP B OD1 1 
ATOM   4602 O  OD1 B ASP B 1 166 ? 111.796 -13.724 46.859  0.50 19.64 ? 168  ASP B OD1 1 
ATOM   4603 O  OD2 A ASP B 1 166 ? 110.425 -16.807 48.944  0.50 20.38 ? 168  ASP B OD2 1 
ATOM   4604 O  OD2 B ASP B 1 166 ? 109.698 -14.179 47.320  0.50 22.03 ? 168  ASP B OD2 1 
ATOM   4605 N  N   . GLY B 1 167 ? 114.180 -15.143 48.419  1.00 19.24 ? 169  GLY B N   1 
ATOM   4606 C  CA  . GLY B 1 167 ? 115.275 -15.377 47.485  1.00 18.28 ? 169  GLY B CA  1 
ATOM   4607 C  C   . GLY B 1 167 ? 116.558 -14.674 47.884  1.00 17.51 ? 169  GLY B C   1 
ATOM   4608 O  O   . GLY B 1 167 ? 117.360 -14.291 47.032  1.00 18.30 ? 169  GLY B O   1 
ATOM   4609 N  N   . ILE B 1 168 ? 116.750 -14.490 49.184  1.00 16.37 ? 170  ILE B N   1 
ATOM   4610 C  CA  . ILE B 1 168 ? 118.026 -14.015 49.698  1.00 15.09 ? 170  ILE B CA  1 
ATOM   4611 C  C   . ILE B 1 168 ? 119.045 -15.150 49.722  1.00 14.05 ? 170  ILE B C   1 
ATOM   4612 O  O   . ILE B 1 168 ? 120.175 -14.991 49.267  1.00 14.10 ? 170  ILE B O   1 
ATOM   4613 C  CB  . ILE B 1 168 ? 117.886 -13.444 51.122  1.00 15.57 ? 170  ILE B CB  1 
ATOM   4614 C  CG1 . ILE B 1 168 ? 116.994 -12.199 51.112  1.00 15.94 ? 170  ILE B CG1 1 
ATOM   4615 C  CG2 . ILE B 1 168 ? 119.253 -13.103 51.692  1.00 14.97 ? 170  ILE B CG2 1 
ATOM   4616 C  CD1 . ILE B 1 168 ? 116.571 -11.741 52.492  1.00 16.75 ? 170  ILE B CD1 1 
ATOM   4617 N  N   . ALA B 1 169 ? 118.634 -16.297 50.252  1.00 14.20 ? 171  ALA B N   1 
ATOM   4618 C  CA  . ALA B 1 169 ? 119.576 -17.350 50.622  1.00 13.37 ? 171  ALA B CA  1 
ATOM   4619 C  C   . ALA B 1 169 ? 119.500 -18.567 49.698  1.00 13.40 ? 171  ALA B C   1 
ATOM   4620 O  O   . ALA B 1 169 ? 118.443 -19.178 49.547  1.00 14.49 ? 171  ALA B O   1 
ATOM   4621 C  CB  . ALA B 1 169 ? 119.365 -17.760 52.071  1.00 13.62 ? 171  ALA B CB  1 
ATOM   4622 N  N   . GLN B 1 170 ? 120.627 -18.896 49.070  1.00 12.79 ? 172  GLN B N   1 
ATOM   4623 C  CA  . GLN B 1 170 ? 120.755 -20.102 48.252  1.00 12.67 ? 172  GLN B CA  1 
ATOM   4624 C  C   . GLN B 1 170 ? 122.129 -20.726 48.496  1.00 12.26 ? 172  GLN B C   1 
ATOM   4625 O  O   . GLN B 1 170 ? 123.068 -20.032 48.865  1.00 12.40 ? 172  GLN B O   1 
ATOM   4626 C  CB  . GLN B 1 170 ? 120.618 -19.757 46.766  1.00 12.66 ? 172  GLN B CB  1 
ATOM   4627 C  CG  . GLN B 1 170 ? 119.457 -18.832 46.434  1.00 13.61 ? 172  GLN B CG  1 
ATOM   4628 C  CD  . GLN B 1 170 ? 118.178 -19.587 46.125  1.00 14.22 ? 172  GLN B CD  1 
ATOM   4629 O  OE1 . GLN B 1 170 ? 118.048 -20.769 46.448  1.00 13.02 ? 172  GLN B OE1 1 
ATOM   4630 N  NE2 . GLN B 1 170 ? 117.217 -18.900 45.508  1.00 15.03 ? 172  GLN B NE2 1 
ATOM   4631 N  N   . PRO B 1 171 ? 122.260 -22.040 48.274  1.00 12.25 ? 173  PRO B N   1 
ATOM   4632 C  CA  . PRO B 1 171 ? 123.606 -22.604 48.309  1.00 11.91 ? 173  PRO B CA  1 
ATOM   4633 C  C   . PRO B 1 171 ? 124.451 -22.033 47.178  1.00 12.48 ? 173  PRO B C   1 
ATOM   4634 O  O   . PRO B 1 171 ? 123.935 -21.798 46.083  1.00 13.34 ? 173  PRO B O   1 
ATOM   4635 C  CB  . PRO B 1 171 ? 123.369 -24.102 48.093  1.00 11.32 ? 173  PRO B CB  1 
ATOM   4636 C  CG  . PRO B 1 171 ? 122.037 -24.190 47.423  1.00 11.26 ? 173  PRO B CG  1 
ATOM   4637 C  CD  . PRO B 1 171 ? 121.232 -23.052 47.981  1.00 11.28 ? 173  PRO B CD  1 
ATOM   4638 N  N   . ALA B 1 172 ? 125.717 -21.742 47.465  1.00 12.08 ? 174  ALA B N   1 
ATOM   4639 C  CA  . ALA B 1 172 ? 126.681 -21.433 46.418  1.00 12.49 ? 174  ALA B CA  1 
ATOM   4640 C  C   . ALA B 1 172 ? 127.269 -22.728 45.874  1.00 13.45 ? 174  ALA B C   1 
ATOM   4641 O  O   . ALA B 1 172 ? 127.689 -23.595 46.638  1.00 13.59 ? 174  ALA B O   1 
ATOM   4642 C  CB  . ALA B 1 172 ? 127.783 -20.532 46.955  1.00 12.80 ? 174  ALA B CB  1 
ATOM   4643 N  N   . ILE B 1 173 ? 127.249 -22.872 44.553  1.00 14.18 ? 175  ILE B N   1 
ATOM   4644 C  CA  . ILE B 1 173 ? 127.829 -24.037 43.905  1.00 15.22 ? 175  ILE B CA  1 
ATOM   4645 C  C   . ILE B 1 173 ? 129.330 -23.831 43.750  1.00 16.00 ? 175  ILE B C   1 
ATOM   4646 O  O   . ILE B 1 173 ? 129.767 -22.939 43.024  1.00 15.65 ? 175  ILE B O   1 
ATOM   4647 C  CB  . ILE B 1 173 ? 127.213 -24.271 42.513  1.00 15.55 ? 175  ILE B CB  1 
ATOM   4648 C  CG1 . ILE B 1 173 ? 125.709 -24.540 42.621  1.00 16.53 ? 175  ILE B CG1 1 
ATOM   4649 C  CG2 . ILE B 1 173 ? 127.931 -25.406 41.798  1.00 15.37 ? 175  ILE B CG2 1 
ATOM   4650 C  CD1 . ILE B 1 173 ? 125.351 -25.683 43.545  1.00 16.46 ? 175  ILE B CD1 1 
ATOM   4651 N  N   . ASN B 1 174 ? 130.112 -24.631 44.467  1.00 16.95 ? 176  ASN B N   1 
ATOM   4652 C  CA  . ASN B 1 174 ? 131.566 -24.541 44.401  1.00 18.03 ? 176  ASN B CA  1 
ATOM   4653 C  C   . ASN B 1 174 ? 132.067 -24.686 42.969  1.00 18.76 ? 176  ASN B C   1 
ATOM   4654 O  O   . ASN B 1 174 ? 131.780 -25.677 42.301  1.00 18.99 ? 176  ASN B O   1 
ATOM   4655 C  CB  . ASN B 1 174 ? 132.210 -25.604 45.295  1.00 19.29 ? 176  ASN B CB  1 
ATOM   4656 C  CG  . ASN B 1 174 ? 133.719 -25.473 45.361  1.00 20.82 ? 176  ASN B CG  1 
ATOM   4657 O  OD1 . ASN B 1 174 ? 134.259 -24.368 45.329  1.00 21.99 ? 176  ASN B OD1 1 
ATOM   4658 N  ND2 . ASN B 1 174 ? 134.408 -26.604 45.455  1.00 22.30 ? 176  ASN B ND2 1 
ATOM   4659 N  N   . GLY B 1 175 ? 132.787 -23.675 42.495  1.00 19.30 ? 177  GLY B N   1 
ATOM   4660 C  CA  . GLY B 1 175 ? 133.343 -23.696 41.151  1.00 19.48 ? 177  GLY B CA  1 
ATOM   4661 C  C   . GLY B 1 175 ? 132.459 -23.002 40.133  1.00 19.74 ? 177  GLY B C   1 
ATOM   4662 O  O   . GLY B 1 175 ? 132.841 -22.851 38.973  1.00 21.48 ? 177  GLY B O   1 
ATOM   4663 N  N   . PHE B 1 176 ? 131.263 -22.603 40.555  1.00 18.28 ? 178  PHE B N   1 
ATOM   4664 C  CA  . PHE B 1 176 ? 130.370 -21.842 39.692  1.00 17.98 ? 178  PHE B CA  1 
ATOM   4665 C  C   . PHE B 1 176 ? 129.999 -20.503 40.322  1.00 18.69 ? 178  PHE B C   1 
ATOM   4666 O  O   . PHE B 1 176 ? 130.170 -19.451 39.708  1.00 18.04 ? 178  PHE B O   1 
ATOM   4667 C  CB  . PHE B 1 176 ? 129.110 -22.648 39.359  1.00 18.25 ? 178  PHE B CB  1 
ATOM   4668 C  CG  . PHE B 1 176 ? 128.025 -21.833 38.714  1.00 18.39 ? 178  PHE B CG  1 
ATOM   4669 C  CD1 . PHE B 1 176 ? 128.217 -21.265 37.465  1.00 18.67 ? 178  PHE B CD1 1 
ATOM   4670 C  CD2 . PHE B 1 176 ? 126.827 -21.605 39.372  1.00 17.32 ? 178  PHE B CD2 1 
ATOM   4671 C  CE1 . PHE B 1 176 ? 127.234 -20.484 36.882  1.00 18.59 ? 178  PHE B CE1 1 
ATOM   4672 C  CE2 . PHE B 1 176 ? 125.836 -20.837 38.789  1.00 17.38 ? 178  PHE B CE2 1 
ATOM   4673 C  CZ  . PHE B 1 176 ? 126.037 -20.281 37.539  1.00 17.51 ? 178  PHE B CZ  1 
ATOM   4674 N  N   . ASN B 1 177 ? 129.508 -20.548 41.556  1.00 18.33 ? 179  ASN B N   1 
ATOM   4675 C  CA  . ASN B 1 177 ? 129.107 -19.337 42.265  1.00 19.62 ? 179  ASN B CA  1 
ATOM   4676 C  C   . ASN B 1 177 ? 130.271 -18.713 43.016  1.00 19.91 ? 179  ASN B C   1 
ATOM   4677 O  O   . ASN B 1 177 ? 131.089 -19.415 43.608  1.00 20.49 ? 179  ASN B O   1 
ATOM   4678 C  CB  . ASN B 1 177 ? 127.980 -19.638 43.254  1.00 18.52 ? 179  ASN B CB  1 
ATOM   4679 C  CG  . ASN B 1 177 ? 126.671 -19.944 42.566  1.00 18.25 ? 179  ASN B CG  1 
ATOM   4680 O  OD1 . ASN B 1 177 ? 126.068 -20.992 42.796  1.00 17.49 ? 179  ASN B OD1 1 
ATOM   4681 N  ND2 . ASN B 1 177 ? 126.218 -19.026 41.718  1.00 18.66 ? 179  ASN B ND2 1 
ATOM   4682 N  N   . THR B 1 178 ? 130.328 -17.387 42.999  1.00 21.11 ? 180  THR B N   1 
ATOM   4683 C  CA  . THR B 1 178 ? 131.167 -16.645 43.927  1.00 20.91 ? 180  THR B CA  1 
ATOM   4684 C  C   . THR B 1 178 ? 130.418 -16.450 45.235  1.00 19.84 ? 180  THR B C   1 
ATOM   4685 O  O   . THR B 1 178 ? 129.443 -15.702 45.287  1.00 20.96 ? 180  THR B O   1 
ATOM   4686 C  CB  . THR B 1 178 ? 131.539 -15.264 43.358  1.00 23.45 ? 180  THR B CB  1 
ATOM   4687 O  OG1 . THR B 1 178 ? 132.115 -15.424 42.058  1.00 25.18 ? 180  THR B OG1 1 
ATOM   4688 C  CG2 . THR B 1 178 ? 132.533 -14.570 44.264  1.00 23.60 ? 180  THR B CG2 1 
ATOM   4689 N  N   . PRO B 1 179 ? 130.857 -17.143 46.294  1.00 18.94 ? 181  PRO B N   1 
ATOM   4690 C  CA  . PRO B 1 179 ? 130.113 -17.191 47.547  1.00 19.20 ? 181  PRO B CA  1 
ATOM   4691 C  C   . PRO B 1 179 ? 129.952 -15.808 48.174  1.00 18.69 ? 181  PRO B C   1 
ATOM   4692 O  O   . PRO B 1 179 ? 130.865 -14.987 48.110  1.00 19.06 ? 181  PRO B O   1 
ATOM   4693 C  CB  . PRO B 1 179 ? 130.984 -18.081 48.445  1.00 20.37 ? 181  PRO B CB  1 
ATOM   4694 C  CG  . PRO B 1 179 ? 131.853 -18.853 47.508  1.00 21.20 ? 181  PRO B CG  1 
ATOM   4695 C  CD  . PRO B 1 179 ? 132.103 -17.925 46.357  1.00 19.07 ? 181  PRO B CD  1 
ATOM   4696 N  N   . LEU B 1 180 ? 128.785 -15.556 48.757  1.00 17.70 ? 182  LEU B N   1 
ATOM   4697 C  CA  . LEU B 1 180 ? 128.568 -14.370 49.577  1.00 16.89 ? 182  LEU B CA  1 
ATOM   4698 C  C   . LEU B 1 180 ? 128.825 -14.699 51.047  1.00 15.95 ? 182  LEU B C   1 
ATOM   4699 O  O   . LEU B 1 180 ? 128.761 -15.862 51.447  1.00 15.80 ? 182  LEU B O   1 
ATOM   4700 C  CB  . LEU B 1 180 ? 127.136 -13.857 49.399  1.00 16.43 ? 182  LEU B CB  1 
ATOM   4701 C  CG  . LEU B 1 180 ? 126.686 -13.553 47.967  1.00 17.11 ? 182  LEU B CG  1 
ATOM   4702 C  CD1 . LEU B 1 180 ? 125.169 -13.494 47.880  1.00 16.22 ? 182  LEU B CD1 1 
ATOM   4703 C  CD2 . LEU B 1 180 ? 127.302 -12.248 47.488  1.00 16.54 ? 182  LEU B CD2 1 
ATOM   4704 N  N   . PRO B 1 181 ? 129.109 -13.674 51.862  1.00 15.47 ? 183  PRO B N   1 
ATOM   4705 C  CA  . PRO B 1 181 ? 129.357 -13.915 53.279  1.00 14.92 ? 183  PRO B CA  1 
ATOM   4706 C  C   . PRO B 1 181 ? 128.237 -14.714 53.935  1.00 13.94 ? 183  PRO B C   1 
ATOM   4707 O  O   . PRO B 1 181 ? 127.068 -14.329 53.857  1.00 13.82 ? 183  PRO B O   1 
ATOM   4708 C  CB  . PRO B 1 181 ? 129.421 -12.504 53.859  1.00 14.54 ? 183  PRO B CB  1 
ATOM   4709 C  CG  . PRO B 1 181 ? 129.980 -11.688 52.742  1.00 15.32 ? 183  PRO B CG  1 
ATOM   4710 C  CD  . PRO B 1 181 ? 129.433 -12.289 51.472  1.00 15.97 ? 183  PRO B CD  1 
ATOM   4711 N  N   . GLY B 1 182 ? 128.599 -15.823 54.572  1.00 13.14 ? 184  GLY B N   1 
ATOM   4712 C  CA  . GLY B 1 182 ? 127.645 -16.637 55.313  1.00 12.30 ? 184  GLY B CA  1 
ATOM   4713 C  C   . GLY B 1 182 ? 127.031 -17.745 54.473  1.00 12.68 ? 184  GLY B C   1 
ATOM   4714 O  O   . GLY B 1 182 ? 126.519 -18.728 55.004  1.00 11.69 ? 184  GLY B O   1 
ATOM   4715 N  N   . GLN B 1 183 ? 127.102 -17.588 53.155  1.00 12.40 ? 185  GLN B N   1 
ATOM   4716 C  CA  . GLN B 1 183 ? 126.483 -18.530 52.226  1.00 13.00 ? 185  GLN B CA  1 
ATOM   4717 C  C   . GLN B 1 183 ? 127.124 -19.911 52.349  1.00 12.69 ? 185  GLN B C   1 
ATOM   4718 O  O   . GLN B 1 183 ? 128.344 -20.029 52.437  1.00 12.71 ? 185  GLN B O   1 
ATOM   4719 C  CB  . GLN B 1 183 ? 126.635 -18.010 50.794  1.00 13.41 ? 185  GLN B CB  1 
ATOM   4720 C  CG  . GLN B 1 183 ? 125.638 -18.573 49.795  1.00 13.38 ? 185  GLN B CG  1 
ATOM   4721 C  CD  . GLN B 1 183 ? 125.818 -17.986 48.408  1.00 13.97 ? 185  GLN B CD  1 
ATOM   4722 O  OE1 . GLN B 1 183 ? 126.773 -17.249 48.149  1.00 14.44 ? 185  GLN B OE1 1 
ATOM   4723 N  NE2 . GLN B 1 183 ? 124.905 -18.320 47.500  1.00 12.91 ? 185  GLN B NE2 1 
ATOM   4724 N  N   . ASN B 1 184 ? 126.306 -20.959 52.345  1.00 12.13 ? 186  ASN B N   1 
ATOM   4725 C  CA  . ASN B 1 184 ? 126.842 -22.311 52.251  1.00 11.75 ? 186  ASN B CA  1 
ATOM   4726 C  C   . ASN B 1 184 ? 127.464 -22.556 50.879  1.00 12.85 ? 186  ASN B C   1 
ATOM   4727 O  O   . ASN B 1 184 ? 127.001 -22.020 49.870  1.00 12.64 ? 186  ASN B O   1 
ATOM   4728 C  CB  . ASN B 1 184 ? 125.767 -23.360 52.558  1.00 11.97 ? 186  ASN B CB  1 
ATOM   4729 C  CG  . ASN B 1 184 ? 126.344 -24.626 53.170  1.00 11.61 ? 186  ASN B CG  1 
ATOM   4730 O  OD1 . ASN B 1 184 ? 127.556 -24.831 53.161  1.00 12.53 ? 186  ASN B OD1 1 
ATOM   4731 N  ND2 . ASN B 1 184 ? 125.475 -25.502 53.666  1.00 11.47 ? 186  ASN B ND2 1 
ATOM   4732 N  N   . ILE B 1 185 ? 128.560 -23.306 50.866  1.00 13.21 ? 187  ILE B N   1 
ATOM   4733 C  CA  . ILE B 1 185 ? 129.246 -23.658 49.633  1.00 14.24 ? 187  ILE B CA  1 
ATOM   4734 C  C   . ILE B 1 185 ? 129.218 -25.172 49.485  1.00 14.03 ? 187  ILE B C   1 
ATOM   4735 O  O   . ILE B 1 185 ? 129.638 -25.894 50.390  1.00 14.21 ? 187  ILE B O   1 
ATOM   4736 C  CB  . ILE B 1 185 ? 130.711 -23.180 49.652  1.00 14.83 ? 187  ILE B CB  1 
ATOM   4737 C  CG1 . ILE B 1 185 ? 130.774 -21.663 49.856  1.00 15.23 ? 187  ILE B CG1 1 
ATOM   4738 C  CG2 . ILE B 1 185 ? 131.425 -23.592 48.371  1.00 14.82 ? 187  ILE B CG2 1 
ATOM   4739 C  CD1 . ILE B 1 185 ? 132.061 -21.180 50.492  1.00 14.87 ? 187  ILE B CD1 1 
ATOM   4740 N  N   . VAL B 1 186 ? 128.680 -25.650 48.367  1.00 12.98 ? 188  VAL B N   1 
ATOM   4741 C  CA  . VAL B 1 186 ? 128.386 -27.069 48.216  1.00 13.18 ? 188  VAL B CA  1 
ATOM   4742 C  C   . VAL B 1 186 ? 128.879 -27.603 46.875  1.00 13.14 ? 188  VAL B C   1 
ATOM   4743 O  O   . VAL B 1 186 ? 129.042 -26.849 45.919  1.00 13.62 ? 188  VAL B O   1 
ATOM   4744 C  CB  . VAL B 1 186 ? 126.876 -27.353 48.365  1.00 12.76 ? 188  VAL B CB  1 
ATOM   4745 C  CG1 . VAL B 1 186 ? 126.332 -26.675 49.615  1.00 12.47 ? 188  VAL B CG1 1 
ATOM   4746 C  CG2 . VAL B 1 186 ? 126.115 -26.887 47.131  1.00 12.11 ? 188  VAL B CG2 1 
ATOM   4747 N  N   . ASP B 1 187 ? 129.115 -28.909 46.814  1.00 14.12 ? 189  ASP B N   1 
ATOM   4748 C  CA  . ASP B 1 187 ? 129.425 -29.571 45.552  1.00 14.52 ? 189  ASP B CA  1 
ATOM   4749 C  C   . ASP B 1 187 ? 128.259 -29.454 44.575  1.00 13.23 ? 189  ASP B C   1 
ATOM   4750 O  O   . ASP B 1 187 ? 127.093 -29.533 44.969  1.00 13.43 ? 189  ASP B O   1 
ATOM   4751 C  CB  . ASP B 1 187 ? 129.762 -31.043 45.792  1.00 15.36 ? 189  ASP B CB  1 
ATOM   4752 C  CG  . ASP B 1 187 ? 130.999 -31.224 46.653  1.00 17.89 ? 189  ASP B CG  1 
ATOM   4753 O  OD1 . ASP B 1 187 ? 131.979 -30.476 46.452  1.00 19.14 ? 189  ASP B OD1 1 
ATOM   4754 O  OD2 . ASP B 1 187 ? 130.992 -32.118 47.527  1.00 19.17 ? 189  ASP B OD2 1 
ATOM   4755 N  N   . ALA B 1 188 ? 128.577 -29.262 43.300  1.00 12.46 ? 190  ALA B N   1 
ATOM   4756 C  CA  . ALA B 1 188 ? 127.557 -29.143 42.266  1.00 11.47 ? 190  ALA B CA  1 
ATOM   4757 C  C   . ALA B 1 188 ? 126.576 -30.313 42.327  1.00 11.56 ? 190  ALA B C   1 
ATOM   4758 O  O   . ALA B 1 188 ? 125.383 -30.153 42.057  1.00 10.96 ? 190  ALA B O   1 
ATOM   4759 C  CB  . ALA B 1 188 ? 128.208 -29.071 40.893  1.00 11.28 ? 190  ALA B CB  1 
ATOM   4760 N  N   . GLY B 1 189 ? 127.081 -31.484 42.703  1.00 11.03 ? 191  GLY B N   1 
ATOM   4761 C  CA  . GLY B 1 189 ? 126.295 -32.708 42.659  1.00 10.31 ? 191  GLY B CA  1 
ATOM   4762 C  C   . GLY B 1 189 ? 125.180 -32.752 43.686  1.00 10.39 ? 191  GLY B C   1 
ATOM   4763 O  O   . GLY B 1 189 ? 124.329 -33.639 43.651  1.00 9.73  ? 191  GLY B O   1 
ATOM   4764 N  N   . VAL B 1 190 ? 125.190 -31.807 44.618  1.00 10.45 ? 192  VAL B N   1 
ATOM   4765 C  CA  . VAL B 1 190 ? 124.077 -31.660 45.545  1.00 9.83  ? 192  VAL B CA  1 
ATOM   4766 C  C   . VAL B 1 190 ? 122.810 -31.198 44.823  1.00 9.73  ? 192  VAL B C   1 
ATOM   4767 O  O   . VAL B 1 190 ? 121.706 -31.590 45.185  1.00 9.62  ? 192  VAL B O   1 
ATOM   4768 C  CB  . VAL B 1 190 ? 124.417 -30.691 46.693  1.00 10.41 ? 192  VAL B CB  1 
ATOM   4769 C  CG1 . VAL B 1 190 ? 123.202 -30.476 47.586  1.00 9.23  ? 192  VAL B CG1 1 
ATOM   4770 C  CG2 . VAL B 1 190 ? 125.591 -31.231 47.497  1.00 10.46 ? 192  VAL B CG2 1 
ATOM   4771 N  N   . ILE B 1 191 ? 122.984 -30.410 43.766  1.00 9.23  ? 193  ILE B N   1 
ATOM   4772 C  CA  . ILE B 1 191 ? 121.854 -29.846 43.035  1.00 9.39  ? 193  ILE B CA  1 
ATOM   4773 C  C   . ILE B 1 191 ? 121.715 -30.461 41.644  1.00 9.83  ? 193  ILE B C   1 
ATOM   4774 O  O   . ILE B 1 191 ? 120.604 -30.686 41.162  1.00 9.45  ? 193  ILE B O   1 
ATOM   4775 C  CB  . ILE B 1 191 ? 121.981 -28.316 42.903  1.00 9.40  ? 193  ILE B CB  1 
ATOM   4776 C  CG1 . ILE B 1 191 ? 122.126 -27.672 44.287  1.00 9.21  ? 193  ILE B CG1 1 
ATOM   4777 C  CG2 . ILE B 1 191 ? 120.790 -27.737 42.152  1.00 9.68  ? 193  ILE B CG2 1 
ATOM   4778 C  CD1 . ILE B 1 191 ? 120.949 -27.918 45.207  1.00 8.54  ? 193  ILE B CD1 1 
ATOM   4779 N  N   . ILE B 1 192 ? 122.846 -30.715 40.995  1.00 9.94  ? 194  ILE B N   1 
ATOM   4780 C  CA  . ILE B 1 192 ? 122.843 -31.172 39.607  1.00 10.32 ? 194  ILE B CA  1 
ATOM   4781 C  C   . ILE B 1 192 ? 123.116 -32.671 39.544  1.00 10.71 ? 194  ILE B C   1 
ATOM   4782 O  O   . ILE B 1 192 ? 124.146 -33.137 40.028  1.00 10.97 ? 194  ILE B O   1 
ATOM   4783 C  CB  . ILE B 1 192 ? 123.916 -30.438 38.777  1.00 10.59 ? 194  ILE B CB  1 
ATOM   4784 C  CG1 . ILE B 1 192 ? 123.717 -28.918 38.856  1.00 10.56 ? 194  ILE B CG1 1 
ATOM   4785 C  CG2 . ILE B 1 192 ? 123.919 -30.931 37.336  1.00 10.17 ? 194  ILE B CG2 1 
ATOM   4786 C  CD1 . ILE B 1 192 ? 122.399 -28.436 38.287  1.00 10.28 ? 194  ILE B CD1 1 
ATOM   4787 N  N   . THR B 1 193 ? 122.199 -33.428 38.950  1.00 10.37 ? 195  THR B N   1 
ATOM   4788 C  CA  . THR B 1 193 ? 122.398 -34.872 38.825  1.00 11.04 ? 195  THR B CA  1 
ATOM   4789 C  C   . THR B 1 193 ? 123.628 -35.197 37.977  1.00 11.02 ? 195  THR B C   1 
ATOM   4790 O  O   . THR B 1 193 ? 123.777 -34.694 36.860  1.00 10.68 ? 195  THR B O   1 
ATOM   4791 C  CB  . THR B 1 193 ? 121.155 -35.588 38.260  1.00 10.39 ? 195  THR B CB  1 
ATOM   4792 O  OG1 . THR B 1 193 ? 120.780 -35.003 37.006  1.00 10.58 ? 195  THR B OG1 1 
ATOM   4793 C  CG2 . THR B 1 193 ? 119.992 -35.474 39.229  1.00 10.57 ? 195  THR B CG2 1 
ATOM   4794 N  N   . GLY B 1 194 ? 124.527 -36.004 38.534  1.00 10.90 ? 196  GLY B N   1 
ATOM   4795 C  CA  . GLY B 1 194 ? 125.719 -36.442 37.812  1.00 11.65 ? 196  GLY B CA  1 
ATOM   4796 C  C   . GLY B 1 194 ? 126.884 -35.474 37.905  1.00 12.78 ? 196  GLY B C   1 
ATOM   4797 O  O   . GLY B 1 194 ? 127.969 -35.744 37.395  1.00 13.58 ? 196  GLY B O   1 
ATOM   4798 N  N   . ALA B 1 195 ? 126.669 -34.346 38.571  1.00 12.66 ? 197  ALA B N   1 
ATOM   4799 C  CA  . ALA B 1 195 ? 127.735 -33.370 38.761  1.00 13.26 ? 197  ALA B CA  1 
ATOM   4800 C  C   . ALA B 1 195 ? 128.639 -33.759 39.929  1.00 13.20 ? 197  ALA B C   1 
ATOM   4801 O  O   . ALA B 1 195 ? 128.430 -34.785 40.572  1.00 13.30 ? 197  ALA B O   1 
ATOM   4802 C  CB  . ALA B 1 195 ? 127.155 -31.979 38.965  1.00 13.01 ? 197  ALA B CB  1 
ATOM   4803 N  N   . THR B 1 196 ? 129.647 -32.935 40.193  1.00 14.13 ? 198  THR B N   1 
ATOM   4804 C  CA  . THR B 1 196 ? 130.694 -33.280 41.150  1.00 14.11 ? 198  THR B CA  1 
ATOM   4805 C  C   . THR B 1 196 ? 130.146 -33.831 42.462  1.00 13.91 ? 198  THR B C   1 
ATOM   4806 O  O   . THR B 1 196 ? 129.362 -33.171 43.147  1.00 12.89 ? 198  THR B O   1 
ATOM   4807 C  CB  . THR B 1 196 ? 131.601 -32.073 41.448  1.00 14.53 ? 198  THR B CB  1 
ATOM   4808 O  OG1 . THR B 1 196 ? 132.271 -31.679 40.246  1.00 17.08 ? 198  THR B OG1 1 
ATOM   4809 C  CG2 . THR B 1 196 ? 132.635 -32.429 42.504  1.00 14.74 ? 198  THR B CG2 1 
ATOM   4810 N  N   . ASN B 1 197 ? 130.551 -35.055 42.790  1.00 14.24 ? 199  ASN B N   1 
ATOM   4811 C  CA  . ASN B 1 197 ? 130.270 -35.659 44.094  1.00 15.41 ? 199  ASN B CA  1 
ATOM   4812 C  C   . ASN B 1 197 ? 128.812 -36.052 44.327  1.00 13.63 ? 199  ASN B C   1 
ATOM   4813 O  O   . ASN B 1 197 ? 128.404 -36.297 45.461  1.00 13.20 ? 199  ASN B O   1 
ATOM   4814 C  CB  . ASN B 1 197 ? 130.777 -34.772 45.235  1.00 16.40 ? 199  ASN B CB  1 
ATOM   4815 C  CG  . ASN B 1 197 ? 132.292 -34.769 45.341  1.00 20.10 ? 199  ASN B CG  1 
ATOM   4816 O  OD1 . ASN B 1 197 ? 132.876 -33.939 46.039  1.00 23.08 ? 199  ASN B OD1 1 
ATOM   4817 N  ND2 . ASN B 1 197 ? 132.939 -35.695 44.640  1.00 20.34 ? 199  ASN B ND2 1 
ATOM   4818 N  N   . ASP B 1 198 ? 128.037 -36.130 43.249  1.00 12.66 ? 200  ASP B N   1 
ATOM   4819 C  CA  . ASP B 1 198 ? 126.757 -36.837 43.276  1.00 12.28 ? 200  ASP B CA  1 
ATOM   4820 C  C   . ASP B 1 198 ? 127.029 -38.344 43.281  1.00 12.34 ? 200  ASP B C   1 
ATOM   4821 O  O   . ASP B 1 198 ? 127.565 -38.880 42.316  1.00 12.79 ? 200  ASP B O   1 
ATOM   4822 C  CB  . ASP B 1 198 ? 125.915 -36.443 42.054  1.00 10.65 ? 200  ASP B CB  1 
ATOM   4823 C  CG  . ASP B 1 198 ? 124.600 -37.205 41.965  1.00 11.18 ? 200  ASP B CG  1 
ATOM   4824 O  OD1 . ASP B 1 198 ? 124.162 -37.771 42.991  1.00 10.03 ? 200  ASP B OD1 1 
ATOM   4825 O  OD2 . ASP B 1 198 ? 124.006 -37.242 40.861  1.00 9.79  ? 200  ASP B OD2 1 
ATOM   4826 N  N   . PRO B 1 199 ? 126.715 -39.020 44.397  1.00 13.01 ? 201  PRO B N   1 
ATOM   4827 C  CA  . PRO B 1 199 ? 127.085 -40.429 44.542  1.00 13.19 ? 201  PRO B CA  1 
ATOM   4828 C  C   . PRO B 1 199 ? 126.154 -41.371 43.780  1.00 13.91 ? 201  PRO B C   1 
ATOM   4829 O  O   . PRO B 1 199 ? 126.457 -42.558 43.641  1.00 15.11 ? 201  PRO B O   1 
ATOM   4830 C  CB  . PRO B 1 199 ? 126.959 -40.666 46.046  1.00 13.64 ? 201  PRO B CB  1 
ATOM   4831 C  CG  . PRO B 1 199 ? 125.917 -39.696 46.485  1.00 14.05 ? 201  PRO B CG  1 
ATOM   4832 C  CD  . PRO B 1 199 ? 126.097 -38.478 45.621  1.00 13.03 ? 201  PRO B CD  1 
ATOM   4833 N  N   . ILE B 1 200 ? 125.028 -40.850 43.298  1.00 12.49 ? 202  ILE B N   1 
ATOM   4834 C  CA  . ILE B 1 200 ? 124.015 -41.685 42.658  1.00 12.26 ? 202  ILE B CA  1 
ATOM   4835 C  C   . ILE B 1 200 ? 124.272 -41.804 41.154  1.00 11.71 ? 202  ILE B C   1 
ATOM   4836 O  O   . ILE B 1 200 ? 124.458 -40.800 40.470  1.00 11.15 ? 202  ILE B O   1 
ATOM   4837 C  CB  . ILE B 1 200 ? 122.595 -41.126 42.896  1.00 12.64 ? 202  ILE B CB  1 
ATOM   4838 C  CG1 . ILE B 1 200 ? 122.358 -40.862 44.388  1.00 12.83 ? 202  ILE B CG1 1 
ATOM   4839 C  CG2 . ILE B 1 200 ? 121.540 -42.071 42.339  1.00 11.83 ? 202  ILE B CG2 1 
ATOM   4840 C  CD1 . ILE B 1 200 ? 122.260 -42.115 45.231  1.00 13.42 ? 202  ILE B CD1 1 
ATOM   4841 N  N   . THR B 1 201 ? 124.319 -43.034 40.653  1.00 11.35 ? 203  THR B N   1 
ATOM   4842 C  CA  . THR B 1 201 ? 124.510 -43.266 39.225  1.00 10.80 ? 203  THR B CA  1 
ATOM   4843 C  C   . THR B 1 201 ? 123.276 -42.834 38.445  1.00 10.64 ? 203  THR B C   1 
ATOM   4844 O  O   . THR B 1 201 ? 122.143 -43.133 38.834  1.00 10.12 ? 203  THR B O   1 
ATOM   4845 C  CB  . THR B 1 201 ? 124.822 -44.743 38.924  1.00 11.64 ? 203  THR B CB  1 
ATOM   4846 O  OG1 . THR B 1 201 ? 126.091 -45.086 39.490  1.00 11.72 ? 203  THR B OG1 1 
ATOM   4847 C  CG2 . THR B 1 201 ? 124.865 -44.991 37.419  1.00 11.24 ? 203  THR B CG2 1 
ATOM   4848 N  N   . ARG B 1 202 ? 123.503 -42.078 37.378  1.00 9.85  ? 204  ARG B N   1 
ATOM   4849 C  CA  . ARG B 1 202 ? 122.420 -41.597 36.531  1.00 9.56  ? 204  ARG B CA  1 
ATOM   4850 C  C   . ARG B 1 202 ? 122.646 -42.071 35.101  1.00 9.66  ? 204  ARG B C   1 
ATOM   4851 O  O   . ARG B 1 202 ? 123.772 -42.368 34.716  1.00 9.77  ? 204  ARG B O   1 
ATOM   4852 C  CB  . ARG B 1 202 ? 122.370 -40.069 36.553  1.00 9.62  ? 204  ARG B CB  1 
ATOM   4853 C  CG  . ARG B 1 202 ? 122.656 -39.452 37.912  1.00 9.94  ? 204  ARG B CG  1 
ATOM   4854 C  CD  . ARG B 1 202 ? 121.479 -39.612 38.862  1.00 9.27  ? 204  ARG B CD  1 
ATOM   4855 N  NE  . ARG B 1 202 ? 121.706 -38.898 40.116  1.00 9.56  ? 204  ARG B NE  1 
ATOM   4856 C  CZ  . ARG B 1 202 ? 120.784 -38.721 41.058  1.00 10.09 ? 204  ARG B CZ  1 
ATOM   4857 N  NH1 . ARG B 1 202 ? 119.565 -39.216 40.895  1.00 10.61 ? 204  ARG B NH1 1 
ATOM   4858 N  NH2 . ARG B 1 202 ? 121.089 -38.066 42.172  1.00 9.57  ? 204  ARG B NH2 1 
ATOM   4859 N  N   . PRO B 1 203 ? 121.575 -42.121 34.297  1.00 9.53  ? 205  PRO B N   1 
ATOM   4860 C  CA  . PRO B 1 203 ? 121.778 -42.270 32.858  1.00 9.81  ? 205  PRO B CA  1 
ATOM   4861 C  C   . PRO B 1 203 ? 122.619 -41.110 32.332  1.00 9.44  ? 205  PRO B C   1 
ATOM   4862 O  O   . PRO B 1 203 ? 122.433 -39.975 32.764  1.00 9.31  ? 205  PRO B O   1 
ATOM   4863 C  CB  . PRO B 1 203 ? 120.357 -42.189 32.286  1.00 9.67  ? 205  PRO B CB  1 
ATOM   4864 C  CG  . PRO B 1 203 ? 119.444 -42.465 33.435  1.00 9.81  ? 205  PRO B CG  1 
ATOM   4865 C  CD  . PRO B 1 203 ? 120.157 -41.972 34.659  1.00 9.81  ? 205  PRO B CD  1 
ATOM   4866 N  N   . SER B 1 204 ? 123.549 -41.387 31.423  1.00 9.39  ? 206  SER B N   1 
ATOM   4867 C  CA  . SER B 1 204 ? 124.418 -40.330 30.904  1.00 9.56  ? 206  SER B CA  1 
ATOM   4868 C  C   . SER B 1 204 ? 123.616 -39.129 30.393  1.00 10.07 ? 206  SER B C   1 
ATOM   4869 O  O   . SER B 1 204 ? 124.007 -37.978 30.602  1.00 11.01 ? 206  SER B O   1 
ATOM   4870 C  CB  . SER B 1 204 ? 125.344 -40.867 29.806  1.00 9.47  ? 206  SER B CB  1 
ATOM   4871 O  OG  . SER B 1 204 ? 124.603 -41.421 28.735  1.00 8.81  ? 206  SER B OG  1 
ATOM   4872 N  N   . TRP B 1 205 ? 122.488 -39.390 29.736  1.00 10.06 ? 207  TRP B N   1 
ATOM   4873 C  CA  . TRP B 1 205 ? 121.691 -38.302 29.161  1.00 10.25 ? 207  TRP B CA  1 
ATOM   4874 C  C   . TRP B 1 205 ? 121.097 -37.383 30.230  1.00 10.43 ? 207  TRP B C   1 
ATOM   4875 O  O   . TRP B 1 205 ? 120.713 -36.250 29.934  1.00 10.49 ? 207  TRP B O   1 
ATOM   4876 C  CB  . TRP B 1 205 ? 120.595 -38.836 28.231  1.00 10.39 ? 207  TRP B CB  1 
ATOM   4877 C  CG  . TRP B 1 205 ? 119.581 -39.700 28.924  1.00 10.55 ? 207  TRP B CG  1 
ATOM   4878 C  CD1 . TRP B 1 205 ? 119.535 -41.064 28.932  1.00 10.47 ? 207  TRP B CD1 1 
ATOM   4879 C  CD2 . TRP B 1 205 ? 118.466 -39.257 29.710  1.00 10.51 ? 207  TRP B CD2 1 
ATOM   4880 N  NE1 . TRP B 1 205 ? 118.471 -41.497 29.687  1.00 10.50 ? 207  TRP B NE1 1 
ATOM   4881 C  CE2 . TRP B 1 205 ? 117.793 -40.408 30.168  1.00 10.53 ? 207  TRP B CE2 1 
ATOM   4882 C  CE3 . TRP B 1 205 ? 117.966 -37.997 30.066  1.00 10.67 ? 207  TRP B CE3 1 
ATOM   4883 C  CZ2 . TRP B 1 205 ? 116.658 -40.340 30.978  1.00 10.83 ? 207  TRP B CZ2 1 
ATOM   4884 C  CZ3 . TRP B 1 205 ? 116.836 -37.929 30.870  1.00 10.71 ? 207  TRP B CZ3 1 
ATOM   4885 C  CH2 . TRP B 1 205 ? 116.196 -39.096 31.319  1.00 10.54 ? 207  TRP B CH2 1 
ATOM   4886 N  N   . ALA B 1 206 ? 121.076 -37.851 31.477  1.00 9.64  ? 208  ALA B N   1 
ATOM   4887 C  CA  . ALA B 1 206 ? 120.508 -37.071 32.580  1.00 9.51  ? 208  ALA B CA  1 
ATOM   4888 C  C   . ALA B 1 206 ? 121.535 -36.243 33.358  1.00 9.59  ? 208  ALA B C   1 
ATOM   4889 O  O   . ALA B 1 206 ? 121.171 -35.478 34.252  1.00 8.91  ? 208  ALA B O   1 
ATOM   4890 C  CB  . ALA B 1 206 ? 119.726 -37.970 33.526  1.00 9.59  ? 208  ALA B CB  1 
ATOM   4891 N  N   . VAL B 1 207 ? 122.811 -36.381 33.011  1.00 9.29  ? 209  VAL B N   1 
ATOM   4892 C  CA  . VAL B 1 207 ? 123.855 -35.587 33.652  1.00 9.37  ? 209  VAL B CA  1 
ATOM   4893 C  C   . VAL B 1 207 ? 123.722 -34.118 33.262  1.00 9.65  ? 209  VAL B C   1 
ATOM   4894 O  O   . VAL B 1 207 ? 123.741 -33.775 32.079  1.00 9.67  ? 209  VAL B O   1 
ATOM   4895 C  CB  . VAL B 1 207 ? 125.264 -36.084 33.277  1.00 9.43  ? 209  VAL B CB  1 
ATOM   4896 C  CG1 . VAL B 1 207 ? 126.327 -35.140 33.831  1.00 9.27  ? 209  VAL B CG1 1 
ATOM   4897 C  CG2 . VAL B 1 207 ? 125.479 -37.500 33.791  1.00 9.24  ? 209  VAL B CG2 1 
ATOM   4898 N  N   . GLY B 1 208 ? 123.557 -33.257 34.259  1.00 9.46  ? 210  GLY B N   1 
ATOM   4899 C  CA  . GLY B 1 208 ? 123.285 -31.847 34.005  1.00 9.71  ? 210  GLY B CA  1 
ATOM   4900 C  C   . GLY B 1 208 ? 121.866 -31.440 34.361  1.00 10.05 ? 210  GLY B C   1 
ATOM   4901 O  O   . GLY B 1 208 ? 121.505 -30.267 34.255  1.00 10.05 ? 210  GLY B O   1 
ATOM   4902 N  N   . GLY B 1 209 ? 121.059 -32.408 34.784  1.00 9.40  ? 211  GLY B N   1 
ATOM   4903 C  CA  . GLY B 1 209 ? 119.677 -32.138 35.177  1.00 9.24  ? 211  GLY B CA  1 
ATOM   4904 C  C   . GLY B 1 209 ? 119.515 -31.901 36.669  1.00 9.53  ? 211  GLY B C   1 
ATOM   4905 O  O   . GLY B 1 209 ? 120.499 -31.831 37.407  1.00 9.45  ? 211  GLY B O   1 
ATOM   4906 N  N   . SER B 1 210 ? 118.268 -31.732 37.102  1.00 9.17  ? 212  SER B N   1 
ATOM   4907 C  CA  . SER B 1 210 ? 117.943 -31.592 38.520  1.00 9.10  ? 212  SER B CA  1 
ATOM   4908 C  C   . SER B 1 210 ? 116.490 -31.989 38.761  1.00 9.22  ? 212  SER B C   1 
ATOM   4909 O  O   . SER B 1 210 ? 115.668 -31.922 37.850  1.00 9.07  ? 212  SER B O   1 
ATOM   4910 C  CB  . SER B 1 210 ? 118.174 -30.154 38.990  1.00 9.03  ? 212  SER B CB  1 
ATOM   4911 O  OG  . SER B 1 210 ? 118.012 -30.050 40.394  1.00 9.24  ? 212  SER B OG  1 
ATOM   4912 N  N   . PHE B 1 211 ? 116.174 -32.400 39.986  1.00 8.56  ? 213  PHE B N   1 
ATOM   4913 C  CA  . PHE B 1 211 ? 114.803 -32.753 40.327  1.00 8.39  ? 213  PHE B CA  1 
ATOM   4914 C  C   . PHE B 1 211 ? 114.055 -31.538 40.841  1.00 8.30  ? 213  PHE B C   1 
ATOM   4915 O  O   . PHE B 1 211 ? 114.549 -30.801 41.701  1.00 8.10  ? 213  PHE B O   1 
ATOM   4916 C  CB  . PHE B 1 211 ? 114.753 -33.874 41.368  1.00 8.05  ? 213  PHE B CB  1 
ATOM   4917 C  CG  . PHE B 1 211 ? 115.204 -35.202 40.844  1.00 8.43  ? 213  PHE B CG  1 
ATOM   4918 C  CD1 . PHE B 1 211 ? 114.355 -35.980 40.066  1.00 8.50  ? 213  PHE B CD1 1 
ATOM   4919 C  CD2 . PHE B 1 211 ? 116.483 -35.669 41.113  1.00 8.46  ? 213  PHE B CD2 1 
ATOM   4920 C  CE1 . PHE B 1 211 ? 114.775 -37.199 39.569  1.00 8.42  ? 213  PHE B CE1 1 
ATOM   4921 C  CE2 . PHE B 1 211 ? 116.907 -36.892 40.623  1.00 8.44  ? 213  PHE B CE2 1 
ATOM   4922 C  CZ  . PHE B 1 211 ? 116.054 -37.653 39.842  1.00 8.27  ? 213  PHE B CZ  1 
ATOM   4923 N  N   . LEU B 1 212 ? 112.853 -31.355 40.312  1.00 8.31  ? 214  LEU B N   1 
ATOM   4924 C  CA  . LEU B 1 212 ? 112.038 -30.187 40.588  1.00 8.26  ? 214  LEU B CA  1 
ATOM   4925 C  C   . LEU B 1 212 ? 110.870 -30.608 41.473  1.00 8.62  ? 214  LEU B C   1 
ATOM   4926 O  O   . LEU B 1 212 ? 110.003 -31.378 41.052  1.00 8.91  ? 214  LEU B O   1 
ATOM   4927 C  CB  . LEU B 1 212 ? 111.520 -29.615 39.265  1.00 8.27  ? 214  LEU B CB  1 
ATOM   4928 C  CG  . LEU B 1 212 ? 110.821 -28.256 39.241  1.00 8.27  ? 214  LEU B CG  1 
ATOM   4929 C  CD1 . LEU B 1 212 ? 110.457 -27.904 37.809  1.00 8.30  ? 214  LEU B CD1 1 
ATOM   4930 C  CD2 . LEU B 1 212 ? 109.576 -28.251 40.115  1.00 8.27  ? 214  LEU B CD2 1 
ATOM   4931 N  N   . ALA B 1 213 ? 110.889 -30.169 42.726  1.00 8.80  ? 215  ALA B N   1 
ATOM   4932 C  CA  . ALA B 1 213 ? 109.734 -30.356 43.596  1.00 8.72  ? 215  ALA B CA  1 
ATOM   4933 C  C   . ALA B 1 213 ? 108.834 -29.134 43.485  1.00 8.74  ? 215  ALA B C   1 
ATOM   4934 O  O   . ALA B 1 213 ? 109.236 -28.027 43.846  1.00 8.78  ? 215  ALA B O   1 
ATOM   4935 C  CB  . ALA B 1 213 ? 110.175 -30.564 45.038  1.00 8.73  ? 215  ALA B CB  1 
ATOM   4936 N  N   . PHE B 1 214 ? 107.650 -29.327 42.915  1.00 8.99  ? 216  PHE B N   1 
ATOM   4937 C  CA  . PHE B 1 214 ? 106.653 -28.263 42.843  1.00 9.31  ? 216  PHE B CA  1 
ATOM   4938 C  C   . PHE B 1 214 ? 105.594 -28.428 43.923  1.00 9.30  ? 216  PHE B C   1 
ATOM   4939 O  O   . PHE B 1 214 ? 105.077 -29.524 44.132  1.00 8.99  ? 216  PHE B O   1 
ATOM   4940 C  CB  . PHE B 1 214 ? 105.986 -28.232 41.463  1.00 9.12  ? 216  PHE B CB  1 
ATOM   4941 C  CG  . PHE B 1 214 ? 104.957 -27.144 41.315  1.00 9.42  ? 216  PHE B CG  1 
ATOM   4942 C  CD1 . PHE B 1 214 ? 103.637 -27.368 41.659  1.00 9.36  ? 216  PHE B CD1 1 
ATOM   4943 C  CD2 . PHE B 1 214 ? 105.318 -25.889 40.852  1.00 10.21 ? 216  PHE B CD2 1 
ATOM   4944 C  CE1 . PHE B 1 214 ? 102.692 -26.364 41.542  1.00 9.60  ? 216  PHE B CE1 1 
ATOM   4945 C  CE2 . PHE B 1 214 ? 104.379 -24.877 40.737  1.00 10.11 ? 216  PHE B CE2 1 
ATOM   4946 C  CZ  . PHE B 1 214 ? 103.062 -25.120 41.076  1.00 9.77  ? 216  PHE B CZ  1 
ATOM   4947 N  N   . ARG B 1 215 ? 105.246 -27.320 44.572  1.00 9.61  ? 217  ARG B N   1 
ATOM   4948 C  CA  . ARG B 1 215 ? 104.178 -27.298 45.564  1.00 9.79  ? 217  ARG B CA  1 
ATOM   4949 C  C   . ARG B 1 215 ? 103.344 -26.032 45.391  1.00 9.31  ? 217  ARG B C   1 
ATOM   4950 O  O   . ARG B 1 215 ? 103.884 -24.930 45.326  1.00 8.96  ? 217  ARG B O   1 
ATOM   4951 C  CB  . ARG B 1 215 ? 104.771 -27.333 46.975  1.00 10.25 ? 217  ARG B CB  1 
ATOM   4952 C  CG  . ARG B 1 215 ? 105.715 -28.499 47.220  1.00 10.27 ? 217  ARG B CG  1 
ATOM   4953 C  CD  . ARG B 1 215 ? 104.964 -29.716 47.731  1.00 11.30 ? 217  ARG B CD  1 
ATOM   4954 N  NE  . ARG B 1 215 ? 104.525 -29.535 49.112  1.00 11.57 ? 217  ARG B NE  1 
ATOM   4955 C  CZ  . ARG B 1 215 ? 103.629 -30.302 49.722  1.00 11.91 ? 217  ARG B CZ  1 
ATOM   4956 N  NH1 . ARG B 1 215 ? 103.051 -31.303 49.071  1.00 12.23 ? 217  ARG B NH1 1 
ATOM   4957 N  NH2 . ARG B 1 215 ? 103.316 -30.069 50.991  1.00 12.49 ? 217  ARG B NH2 1 
ATOM   4958 N  N   . GLN B 1 216 ? 102.032 -26.191 45.278  1.00 9.08  ? 218  GLN B N   1 
ATOM   4959 C  CA  . GLN B 1 216 ? 101.148 -25.033 45.296  1.00 9.45  ? 218  GLN B CA  1 
ATOM   4960 C  C   . GLN B 1 216 ? 100.714 -24.751 46.725  1.00 9.38  ? 218  GLN B C   1 
ATOM   4961 O  O   . GLN B 1 216 ? 99.890  -25.470 47.288  1.00 9.67  ? 218  GLN B O   1 
ATOM   4962 C  CB  . GLN B 1 216 ? 99.931  -25.259 44.406  1.00 9.50  ? 218  GLN B CB  1 
ATOM   4963 C  CG  . GLN B 1 216 ? 98.953  -24.097 44.404  1.00 10.44 ? 218  GLN B CG  1 
ATOM   4964 C  CD  . GLN B 1 216 ? 97.863  -24.270 43.369  1.00 11.12 ? 218  GLN B CD  1 
ATOM   4965 O  OE1 . GLN B 1 216 ? 98.079  -24.890 42.329  1.00 11.33 ? 218  GLN B OE1 1 
ATOM   4966 N  NE2 . GLN B 1 216 ? 96.678  -23.736 43.655  1.00 11.44 ? 218  GLN B NE2 1 
ATOM   4967 N  N   . LEU B 1 217 ? 101.326 -23.743 47.331  1.00 9.71  ? 219  LEU B N   1 
ATOM   4968 C  CA  . LEU B 1 217 ? 101.135 -23.488 48.749  1.00 10.13 ? 219  LEU B CA  1 
ATOM   4969 C  C   . LEU B 1 217 ? 100.285 -22.241 48.963  1.00 10.94 ? 219  LEU B C   1 
ATOM   4970 O  O   . LEU B 1 217 ? 100.772 -21.119 48.837  1.00 10.98 ? 219  LEU B O   1 
ATOM   4971 C  CB  . LEU B 1 217 ? 102.489 -23.344 49.447  1.00 10.48 ? 219  LEU B CB  1 
ATOM   4972 C  CG  . LEU B 1 217 ? 103.437 -24.538 49.280  1.00 10.19 ? 219  LEU B CG  1 
ATOM   4973 C  CD1 . LEU B 1 217 ? 104.749 -24.303 50.015  1.00 10.40 ? 219  LEU B CD1 1 
ATOM   4974 C  CD2 . LEU B 1 217 ? 102.770 -25.820 49.750  1.00 10.34 ? 219  LEU B CD2 1 
ATOM   4975 N  N   . GLU B 1 218 ? 99.007  -22.442 49.259  1.00 11.98 ? 220  GLU B N   1 
ATOM   4976 C  CA  . GLU B 1 218 ? 98.124  -21.324 49.557  1.00 12.17 ? 220  GLU B CA  1 
ATOM   4977 C  C   . GLU B 1 218 ? 98.533  -20.662 50.867  1.00 12.86 ? 220  GLU B C   1 
ATOM   4978 O  O   . GLU B 1 218 ? 98.848  -21.340 51.845  1.00 12.76 ? 220  GLU B O   1 
ATOM   4979 C  CB  . GLU B 1 218 ? 96.664  -21.775 49.639  1.00 14.28 ? 220  GLU B CB  1 
ATOM   4980 C  CG  . GLU B 1 218 ? 95.738  -20.683 50.160  1.00 15.18 ? 220  GLU B CG  1 
ATOM   4981 C  CD  . GLU B 1 218 ? 94.268  -21.050 50.090  1.00 17.74 ? 220  GLU B CD  1 
ATOM   4982 O  OE1 . GLU B 1 218 ? 93.949  -22.252 50.008  1.00 19.30 ? 220  GLU B OE1 1 
ATOM   4983 O  OE2 . GLU B 1 218 ? 93.429  -20.127 50.127  1.00 19.16 ? 220  GLU B OE2 1 
ATOM   4984 N  N   . GLN B 1 219 ? 98.503  -19.335 50.884  1.00 13.12 ? 221  GLN B N   1 
ATOM   4985 C  CA  . GLN B 1 219 ? 98.839  -18.576 52.082  1.00 13.66 ? 221  GLN B CA  1 
ATOM   4986 C  C   . GLN B 1 219 ? 97.638  -17.781 52.576  1.00 13.92 ? 221  GLN B C   1 
ATOM   4987 O  O   . GLN B 1 219 ? 97.032  -17.014 51.824  1.00 12.92 ? 221  GLN B O   1 
ATOM   4988 C  CB  . GLN B 1 219 ? 100.007 -17.630 51.805  1.00 13.36 ? 221  GLN B CB  1 
ATOM   4989 C  CG  . GLN B 1 219 ? 101.335 -18.339 51.609  1.00 13.95 ? 221  GLN B CG  1 
ATOM   4990 C  CD  . GLN B 1 219 ? 102.426 -17.406 51.131  1.00 14.31 ? 221  GLN B CD  1 
ATOM   4991 O  OE1 . GLN B 1 219 ? 102.701 -17.316 49.933  1.00 15.35 ? 221  GLN B OE1 1 
ATOM   4992 N  NE2 . GLN B 1 219 ? 103.040 -16.687 52.063  1.00 14.76 ? 221  GLN B NE2 1 
ATOM   4993 N  N   . LEU B 1 220 ? 97.314  -17.955 53.852  1.00 13.82 ? 222  LEU B N   1 
ATOM   4994 C  CA  . LEU B 1 220 ? 96.199  -17.250 54.464  1.00 14.23 ? 222  LEU B CA  1 
ATOM   4995 C  C   . LEU B 1 220 ? 96.691  -15.979 55.148  1.00 13.88 ? 222  LEU B C   1 
ATOM   4996 O  O   . LEU B 1 220 ? 96.988  -15.981 56.344  1.00 14.21 ? 222  LEU B O   1 
ATOM   4997 C  CB  . LEU B 1 220 ? 95.496  -18.158 55.475  1.00 14.06 ? 222  LEU B CB  1 
ATOM   4998 C  CG  . LEU B 1 220 ? 95.013  -19.508 54.935  1.00 14.60 ? 222  LEU B CG  1 
ATOM   4999 C  CD1 . LEU B 1 220 ? 94.543  -20.407 56.069  1.00 15.50 ? 222  LEU B CD1 1 
ATOM   5000 C  CD2 . LEU B 1 220 ? 93.901  -19.303 53.916  1.00 14.99 ? 222  LEU B CD2 1 
ATOM   5001 N  N   . VAL B 1 221 ? 96.765  -14.893 54.386  1.00 13.33 ? 223  VAL B N   1 
ATOM   5002 C  CA  . VAL B 1 221 ? 97.545  -13.728 54.794  1.00 13.48 ? 223  VAL B CA  1 
ATOM   5003 C  C   . VAL B 1 221 ? 96.844  -12.889 55.866  1.00 14.38 ? 223  VAL B C   1 
ATOM   5004 O  O   . VAL B 1 221 ? 97.452  -12.548 56.884  1.00 15.01 ? 223  VAL B O   1 
ATOM   5005 C  CB  . VAL B 1 221 ? 97.943  -12.857 53.582  1.00 12.90 ? 223  VAL B CB  1 
ATOM   5006 C  CG1 . VAL B 1 221 ? 98.700  -11.617 54.034  1.00 13.12 ? 223  VAL B CG1 1 
ATOM   5007 C  CG2 . VAL B 1 221 ? 98.777  -13.669 52.599  1.00 12.40 ? 223  VAL B CG2 1 
ATOM   5008 N  N   . PRO B 1 222 ? 95.551  -12.585 55.664  1.00 14.99 ? 224  PRO B N   1 
ATOM   5009 C  CA  . PRO B 1 222 ? 94.789  -11.883 56.698  1.00 15.10 ? 224  PRO B CA  1 
ATOM   5010 C  C   . PRO B 1 222 ? 94.769  -12.657 58.013  1.00 16.11 ? 224  PRO B C   1 
ATOM   5011 O  O   . PRO B 1 222 ? 94.907  -12.064 59.087  1.00 15.06 ? 224  PRO B O   1 
ATOM   5012 C  CB  . PRO B 1 222 ? 93.378  -11.813 56.105  1.00 15.32 ? 224  PRO B CB  1 
ATOM   5013 C  CG  . PRO B 1 222 ? 93.598  -11.829 54.632  1.00 13.96 ? 224  PRO B CG  1 
ATOM   5014 C  CD  . PRO B 1 222 ? 94.791  -12.717 54.409  1.00 14.07 ? 224  PRO B CD  1 
ATOM   5015 N  N   . GLU B 1 223 ? 94.616  -13.974 57.917  1.00 16.11 ? 225  GLU B N   1 
ATOM   5016 C  CA  . GLU B 1 223 ? 94.619  -14.840 59.088  1.00 15.71 ? 225  GLU B CA  1 
ATOM   5017 C  C   . GLU B 1 223 ? 95.966  -14.807 59.812  1.00 16.58 ? 225  GLU B C   1 
ATOM   5018 O  O   . GLU B 1 223 ? 96.022  -14.667 61.035  1.00 15.99 ? 225  GLU B O   1 
ATOM   5019 C  CB  . GLU B 1 223 ? 94.252  -16.273 58.689  1.00 15.36 ? 225  GLU B CB  1 
ATOM   5020 C  CG  . GLU B 1 223 ? 92.793  -16.455 58.291  1.00 15.81 ? 225  GLU B CG  1 
ATOM   5021 C  CD  . GLU B 1 223 ? 92.535  -16.181 56.817  1.00 15.88 ? 225  GLU B CD  1 
ATOM   5022 O  OE1 . GLU B 1 223 ? 93.402  -15.570 56.152  1.00 15.21 ? 225  GLU B OE1 1 
ATOM   5023 O  OE2 . GLU B 1 223 ? 91.450  -16.562 56.326  1.00 15.48 ? 225  GLU B OE2 1 
ATOM   5024 N  N   . PHE B 1 224 ? 97.046  -14.925 59.046  1.00 15.97 ? 226  PHE B N   1 
ATOM   5025 C  CA  . PHE B 1 224 ? 98.404  -14.734 59.559  1.00 16.56 ? 226  PHE B CA  1 
ATOM   5026 C  C   . PHE B 1 224 ? 98.527  -13.424 60.333  1.00 17.13 ? 226  PHE B C   1 
ATOM   5027 O  O   . PHE B 1 224 ? 98.953  -13.412 61.491  1.00 16.38 ? 226  PHE B O   1 
ATOM   5028 C  CB  . PHE B 1 224 ? 99.404  -14.762 58.397  1.00 17.18 ? 226  PHE B CB  1 
ATOM   5029 C  CG  . PHE B 1 224 ? 100.838 -14.558 58.808  1.00 17.86 ? 226  PHE B CG  1 
ATOM   5030 C  CD1 . PHE B 1 224 ? 101.526 -15.549 59.491  1.00 19.15 ? 226  PHE B CD1 1 
ATOM   5031 C  CD2 . PHE B 1 224 ? 101.530 -13.427 58.406  1.00 18.03 ? 226  PHE B CD2 1 
ATOM   5032 C  CE1 . PHE B 1 224 ? 102.860 -15.387 59.821  1.00 19.22 ? 226  PHE B CE1 1 
ATOM   5033 C  CE2 . PHE B 1 224 ? 102.863 -13.258 58.730  1.00 19.55 ? 226  PHE B CE2 1 
ATOM   5034 C  CZ  . PHE B 1 224 ? 103.530 -14.241 59.439  1.00 18.55 ? 226  PHE B CZ  1 
ATOM   5035 N  N   . ASN B 1 225 ? 98.124  -12.327 59.698  1.00 17.49 ? 227  ASN B N   1 
ATOM   5036 C  CA  . ASN B 1 225 ? 98.282  -10.993 60.274  1.00 18.27 ? 227  ASN B CA  1 
ATOM   5037 C  C   . ASN B 1 225 ? 97.515  -10.817 61.582  1.00 19.17 ? 227  ASN B C   1 
ATOM   5038 O  O   . ASN B 1 225 ? 98.004  -10.185 62.520  1.00 19.16 ? 227  ASN B O   1 
ATOM   5039 C  CB  . ASN B 1 225 ? 97.836  -9.924  59.273  1.00 18.37 ? 227  ASN B CB  1 
ATOM   5040 C  CG  . ASN B 1 225 ? 98.674  -9.921  58.011  1.00 19.53 ? 227  ASN B CG  1 
ATOM   5041 O  OD1 . ASN B 1 225 ? 99.834  -10.333 58.020  1.00 20.31 ? 227  ASN B OD1 1 
ATOM   5042 N  ND2 . ASN B 1 225 ? 98.094  -9.435  56.919  1.00 20.08 ? 227  ASN B ND2 1 
ATOM   5043 N  N   . LYS B 1 226 ? 96.296  -11.348 61.623  1.00 19.57 ? 228  LYS B N   1 
ATOM   5044 C  CA  . LYS B 1 226 ? 95.469  -11.272 62.820  1.00 20.79 ? 228  LYS B CA  1 
ATOM   5045 C  C   . LYS B 1 226 ? 96.084  -12.081 63.958  1.00 21.43 ? 228  LYS B C   1 
ATOM   5046 O  O   . LYS B 1 226 ? 96.142  -11.617 65.096  1.00 21.25 ? 228  LYS B O   1 
ATOM   5047 C  CB  . LYS B 1 226 ? 94.050  -11.763 62.524  1.00 22.74 ? 228  LYS B CB  1 
ATOM   5048 C  CG  . LYS B 1 226 ? 93.146  -11.836 63.746  1.00 26.43 ? 228  LYS B CG  1 
ATOM   5049 C  CD  . LYS B 1 226 ? 91.921  -12.696 63.478  1.00 30.44 ? 228  LYS B CD  1 
ATOM   5050 C  CE  . LYS B 1 226 ? 91.207  -13.068 64.770  1.00 34.10 ? 228  LYS B CE  1 
ATOM   5051 N  NZ  . LYS B 1 226 ? 90.942  -11.874 65.621  1.00 35.19 ? 228  LYS B NZ  1 
ATOM   5052 N  N   . TYR B 1 227 ? 96.562  -13.282 63.644  1.00 21.02 ? 229  TYR B N   1 
ATOM   5053 C  CA  . TYR B 1 227 ? 97.189  -14.132 64.652  1.00 21.41 ? 229  TYR B CA  1 
ATOM   5054 C  C   . TYR B 1 227 ? 98.346  -13.416 65.342  1.00 21.20 ? 229  TYR B C   1 
ATOM   5055 O  O   . TYR B 1 227 ? 98.485  -13.478 66.566  1.00 22.63 ? 229  TYR B O   1 
ATOM   5056 C  CB  . TYR B 1 227 ? 97.677  -15.452 64.048  1.00 20.75 ? 229  TYR B CB  1 
ATOM   5057 C  CG  . TYR B 1 227 ? 98.212  -16.410 65.089  1.00 21.25 ? 229  TYR B CG  1 
ATOM   5058 C  CD1 . TYR B 1 227 ? 99.539  -16.356 65.497  1.00 20.79 ? 229  TYR B CD1 1 
ATOM   5059 C  CD2 . TYR B 1 227 ? 97.371  -17.316 65.719  1.00 21.31 ? 229  TYR B CD2 1 
ATOM   5060 C  CE1 . TYR B 1 227 ? 100.017 -17.198 66.487  1.00 20.66 ? 229  TYR B CE1 1 
ATOM   5061 C  CE2 . TYR B 1 227 ? 97.841  -18.169 66.701  1.00 21.73 ? 229  TYR B CE2 1 
ATOM   5062 C  CZ  . TYR B 1 227 ? 99.162  -18.106 67.081  1.00 21.72 ? 229  TYR B CZ  1 
ATOM   5063 O  OH  . TYR B 1 227 ? 99.622  -18.948 68.070  1.00 21.12 ? 229  TYR B OH  1 
ATOM   5064 N  N   . LEU B 1 228 ? 99.178  -12.744 64.553  1.00 19.74 ? 230  LEU B N   1 
ATOM   5065 C  CA  . LEU B 1 228 ? 100.303 -11.994 65.098  1.00 19.63 ? 230  LEU B CA  1 
ATOM   5066 C  C   . LEU B 1 228 ? 99.810  -10.920 66.063  1.00 20.54 ? 230  LEU B C   1 
ATOM   5067 O  O   . LEU B 1 228 ? 100.349 -10.762 67.159  1.00 19.37 ? 230  LEU B O   1 
ATOM   5068 C  CB  . LEU B 1 228 ? 101.123 -11.352 63.977  1.00 18.37 ? 230  LEU B CB  1 
ATOM   5069 C  CG  . LEU B 1 228 ? 101.798 -12.292 62.974  1.00 18.48 ? 230  LEU B CG  1 
ATOM   5070 C  CD1 . LEU B 1 228 ? 102.716 -11.504 62.049  1.00 16.99 ? 230  LEU B CD1 1 
ATOM   5071 C  CD2 . LEU B 1 228 ? 102.571 -13.384 63.697  1.00 17.62 ? 230  LEU B CD2 1 
ATOM   5072 N  N   . LEU B 1 229 ? 98.774  -10.195 65.651  1.00 19.62 ? 231  LEU B N   1 
ATOM   5073 C  CA  . LEU B 1 229 ? 98.179  -9.161  66.491  1.00 20.28 ? 231  LEU B CA  1 
ATOM   5074 C  C   . LEU B 1 229 ? 97.626  -9.751  67.783  1.00 21.62 ? 231  LEU B C   1 
ATOM   5075 O  O   . LEU B 1 229 ? 97.787  -9.172  68.859  1.00 23.64 ? 231  LEU B O   1 
ATOM   5076 C  CB  . LEU B 1 229 ? 97.076  -8.415  65.733  1.00 19.59 ? 231  LEU B CB  1 
ATOM   5077 C  CG  . LEU B 1 229 ? 97.523  -7.473  64.613  1.00 19.16 ? 231  LEU B CG  1 
ATOM   5078 C  CD1 . LEU B 1 229 ? 96.334  -7.021  63.778  1.00 19.18 ? 231  LEU B CD1 1 
ATOM   5079 C  CD2 . LEU B 1 229 ? 98.279  -6.276  65.168  1.00 18.14 ? 231  LEU B CD2 1 
ATOM   5080 N  N   . ASP B 1 230 ? 96.989  -10.912 67.673  1.00 22.24 ? 232  ASP B N   1 
ATOM   5081 C  CA  . ASP B 1 230 ? 96.320  -11.531 68.812  1.00 22.13 ? 232  ASP B CA  1 
ATOM   5082 C  C   . ASP B 1 230 ? 97.306  -12.152 69.794  1.00 23.43 ? 232  ASP B C   1 
ATOM   5083 O  O   . ASP B 1 230 ? 96.989  -12.327 70.968  1.00 21.88 ? 232  ASP B O   1 
ATOM   5084 C  CB  . ASP B 1 230 ? 95.330  -12.596 68.341  1.00 23.21 ? 232  ASP B CB  1 
ATOM   5085 C  CG  . ASP B 1 230 ? 94.077  -12.003 67.734  1.00 24.54 ? 232  ASP B CG  1 
ATOM   5086 O  OD1 . ASP B 1 230 ? 93.945  -10.760 67.720  1.00 24.21 ? 232  ASP B OD1 1 
ATOM   5087 O  OD2 . ASP B 1 230 ? 93.223  -12.784 67.267  1.00 27.55 ? 232  ASP B OD2 1 
ATOM   5088 N  N   . ASN B 1 231 ? 98.485  -12.526 69.304  1.00 22.59 ? 233  ASN B N   1 
ATOM   5089 C  CA  . ASN B 1 231 ? 99.440  -13.268 70.121  1.00 22.65 ? 233  ASN B CA  1 
ATOM   5090 C  C   . ASN B 1 231 ? 100.778 -12.557 70.285  1.00 22.82 ? 233  ASN B C   1 
ATOM   5091 O  O   . ASN B 1 231 ? 101.761 -13.161 70.713  1.00 23.78 ? 233  ASN B O   1 
ATOM   5092 C  CB  . ASN B 1 231 ? 99.658  -14.667 69.551  1.00 22.24 ? 233  ASN B CB  1 
ATOM   5093 C  CG  . ASN B 1 231 ? 98.381  -15.478 69.499  1.00 23.06 ? 233  ASN B CG  1 
ATOM   5094 O  OD1 . ASN B 1 231 ? 97.714  -15.545 68.464  1.00 23.80 ? 233  ASN B OD1 1 
ATOM   5095 N  ND2 . ASN B 1 231 ? 98.035  -16.105 70.616  1.00 21.60 ? 233  ASN B ND2 1 
ATOM   5096 N  N   . ALA B 1 232 ? 100.811 -11.274 69.945  1.00 21.32 ? 234  ALA B N   1 
ATOM   5097 C  CA  . ALA B 1 232 ? 102.029 -10.484 70.068  1.00 22.99 ? 234  ALA B CA  1 
ATOM   5098 C  C   . ALA B 1 232 ? 102.548 -10.527 71.503  1.00 25.53 ? 234  ALA B C   1 
ATOM   5099 O  O   . ALA B 1 232 ? 101.764 -10.522 72.451  1.00 23.61 ? 234  ALA B O   1 
ATOM   5100 C  CB  . ALA B 1 232 ? 101.773 -9.050  69.637  1.00 21.98 ? 234  ALA B CB  1 
ATOM   5101 N  N   . PRO B 1 233 ? 103.877 -10.601 71.667  1.00 26.84 ? 235  PRO B N   1 
ATOM   5102 C  CA  . PRO B 1 233 ? 104.450 -10.599 73.009  1.00 28.31 ? 235  PRO B CA  1 
ATOM   5103 C  C   . PRO B 1 233 ? 104.159 -9.292  73.737  1.00 27.60 ? 235  PRO B C   1 
ATOM   5104 O  O   . PRO B 1 233 ? 104.176 -8.223  73.127  1.00 25.82 ? 235  PRO B O   1 
ATOM   5105 C  CB  . PRO B 1 233 ? 105.956 -10.744 72.755  1.00 27.74 ? 235  PRO B CB  1 
ATOM   5106 C  CG  . PRO B 1 233 ? 106.158 -10.301 71.343  1.00 28.73 ? 235  PRO B CG  1 
ATOM   5107 C  CD  . PRO B 1 233 ? 104.906 -10.697 70.619  1.00 27.83 ? 235  PRO B CD  1 
ATOM   5108 N  N   . ALA B 1 234 ? 103.855 -9.386  75.027  1.00 30.95 ? 236  ALA B N   1 
ATOM   5109 C  CA  . ALA B 1 234 ? 103.777 -8.205  75.871  1.00 29.01 ? 236  ALA B CA  1 
ATOM   5110 C  C   . ALA B 1 234 ? 105.081 -7.430  75.766  1.00 29.76 ? 236  ALA B C   1 
ATOM   5111 O  O   . ALA B 1 234 ? 106.164 -8.015  75.750  1.00 33.14 ? 236  ALA B O   1 
ATOM   5112 C  CB  . ALA B 1 234 ? 103.503 -8.599  77.315  1.00 30.20 ? 236  ALA B CB  1 
ATOM   5113 N  N   . GLY B 1 235 ? 104.975 -6.113  75.655  1.00 29.05 ? 237  GLY B N   1 
ATOM   5114 C  CA  . GLY B 1 235 ? 106.157 -5.280  75.508  1.00 29.08 ? 237  GLY B CA  1 
ATOM   5115 C  C   . GLY B 1 235 ? 105.810 -3.810  75.461  1.00 28.37 ? 237  GLY B C   1 
ATOM   5116 O  O   . GLY B 1 235 ? 104.644 -3.435  75.572  1.00 29.21 ? 237  GLY B O   1 
ATOM   5117 N  N   . SER B 1 236 ? 106.827 -2.981  75.266  1.00 31.02 ? 238  SER B N   1 
ATOM   5118 C  CA  . SER B 1 236 ? 106.667 -1.536  75.332  1.00 31.71 ? 238  SER B CA  1 
ATOM   5119 C  C   . SER B 1 236 ? 106.077 -0.956  74.052  1.00 31.36 ? 238  SER B C   1 
ATOM   5120 O  O   . SER B 1 236 ? 105.360 0.043   74.089  1.00 34.98 ? 238  SER B O   1 
ATOM   5121 C  CB  . SER B 1 236 ? 108.013 -0.873  75.627  1.00 32.25 ? 238  SER B CB  1 
ATOM   5122 O  OG  . SER B 1 236 ? 109.010 -1.346  74.741  1.00 32.84 ? 238  SER B OG  1 
ATOM   5123 N  N   . GLY B 1 237 ? 106.403 -1.568  72.917  1.00 31.59 ? 239  GLY B N   1 
ATOM   5124 C  CA  . GLY B 1 237 ? 106.034 -1.010  71.618  1.00 30.05 ? 239  GLY B CA  1 
ATOM   5125 C  C   . GLY B 1 237 ? 104.548 -1.097  71.313  1.00 30.45 ? 239  GLY B C   1 
ATOM   5126 O  O   . GLY B 1 237 ? 103.794 -1.774  72.018  1.00 29.48 ? 239  GLY B O   1 
ATOM   5127 N  N   . SER B 1 238 ? 104.127 -0.426  70.245  1.00 29.15 ? 240  SER B N   1 
ATOM   5128 C  CA  . SER B 1 238 ? 102.763 -0.565  69.741  1.00 27.61 ? 240  SER B CA  1 
ATOM   5129 C  C   . SER B 1 238 ? 102.426 -2.024  69.453  1.00 26.64 ? 240  SER B C   1 
ATOM   5130 O  O   . SER B 1 238 ? 103.316 -2.874  69.357  1.00 24.64 ? 240  SER B O   1 
ATOM   5131 C  CB  . SER B 1 238 ? 102.562 0.282   68.484  1.00 29.33 ? 240  SER B CB  1 
ATOM   5132 O  OG  . SER B 1 238 ? 103.081 -0.370  67.337  1.00 31.11 ? 240  SER B OG  1 
ATOM   5133 N  N   . LEU B 1 239 ? 101.135 -2.317  69.338  1.00 25.26 ? 241  LEU B N   1 
ATOM   5134 C  CA  . LEU B 1 239 ? 100.694 -3.676  69.051  1.00 25.22 ? 241  LEU B CA  1 
ATOM   5135 C  C   . LEU B 1 239 ? 101.259 -4.178  67.725  1.00 23.69 ? 241  LEU B C   1 
ATOM   5136 O  O   . LEU B 1 239 ? 101.705 -5.319  67.629  1.00 22.91 ? 241  LEU B O   1 
ATOM   5137 C  CB  . LEU B 1 239 ? 99.167  -3.766  69.049  1.00 24.22 ? 241  LEU B CB  1 
ATOM   5138 C  CG  . LEU B 1 239 ? 98.587  -5.172  68.880  1.00 23.95 ? 241  LEU B CG  1 
ATOM   5139 C  CD1 . LEU B 1 239 ? 99.059  -6.092  69.996  1.00 24.06 ? 241  LEU B CD1 1 
ATOM   5140 C  CD2 . LEU B 1 239 ? 97.066  -5.128  68.819  1.00 25.43 ? 241  LEU B CD2 1 
ATOM   5141 N  N   . GLN B 1 240 ? 101.247 -3.319  66.710  1.00 24.01 ? 242  GLN B N   1 
ATOM   5142 C  CA  . GLN B 1 240 ? 101.681 -3.713  65.370  1.00 25.69 ? 242  GLN B CA  1 
ATOM   5143 C  C   . GLN B 1 240 ? 103.188 -3.951  65.309  1.00 26.29 ? 242  GLN B C   1 
ATOM   5144 O  O   . GLN B 1 240 ? 103.657 -4.838  64.592  1.00 25.06 ? 242  GLN B O   1 
ATOM   5145 C  CB  . GLN B 1 240 ? 101.271 -2.665  64.334  1.00 24.98 ? 242  GLN B CB  1 
ATOM   5146 C  CG  . GLN B 1 240 ? 101.607 -3.046  62.898  1.00 25.41 ? 242  GLN B CG  1 
ATOM   5147 C  CD  . GLN B 1 240 ? 100.987 -4.366  62.481  1.00 25.97 ? 242  GLN B CD  1 
ATOM   5148 O  OE1 . GLN B 1 240 ? 101.692 -5.341  62.220  1.00 24.88 ? 242  GLN B OE1 1 
ATOM   5149 N  NE2 . GLN B 1 240 ? 99.660  -4.408  62.427  1.00 23.74 ? 242  GLN B NE2 1 
ATOM   5150 N  N   . ALA B 1 241 ? 103.940 -3.154  66.061  1.00 25.64 ? 243  ALA B N   1 
ATOM   5151 C  CA  . ALA B 1 241 ? 105.378 -3.363  66.201  1.00 25.54 ? 243  ALA B CA  1 
ATOM   5152 C  C   . ALA B 1 241 ? 105.679 -4.716  66.836  1.00 24.82 ? 243  ALA B C   1 
ATOM   5153 O  O   . ALA B 1 241 ? 106.554 -5.449  66.375  1.00 25.18 ? 243  ALA B O   1 
ATOM   5154 C  CB  . ALA B 1 241 ? 106.000 -2.240  67.019  1.00 25.36 ? 243  ALA B CB  1 
ATOM   5155 N  N   . ARG B 1 242 ? 104.946 -5.050  67.892  1.00 23.06 ? 244  ARG B N   1 
ATOM   5156 C  CA  . ARG B 1 242 ? 105.157 -6.313  68.587  1.00 21.61 ? 244  ARG B CA  1 
ATOM   5157 C  C   . ARG B 1 242 ? 104.602 -7.497  67.799  1.00 20.83 ? 244  ARG B C   1 
ATOM   5158 O  O   . ARG B 1 242 ? 105.105 -8.615  67.905  1.00 18.94 ? 244  ARG B O   1 
ATOM   5159 C  CB  . ARG B 1 242 ? 104.554 -6.266  69.991  1.00 21.38 ? 244  ARG B CB  1 
ATOM   5160 C  CG  . ARG B 1 242 ? 105.223 -5.255  70.910  1.00 22.90 ? 244  ARG B CG  1 
ATOM   5161 C  CD  . ARG B 1 242 ? 104.623 -5.288  72.306  1.00 24.18 ? 244  ARG B CD  1 
ATOM   5162 N  NE  . ARG B 1 242 ? 103.392 -4.507  72.392  1.00 23.41 ? 244  ARG B NE  1 
ATOM   5163 C  CZ  . ARG B 1 242 ? 102.188 -5.027  72.610  1.00 23.82 ? 244  ARG B CZ  1 
ATOM   5164 N  NH1 . ARG B 1 242 ? 102.041 -6.337  72.762  1.00 24.39 ? 244  ARG B NH1 1 
ATOM   5165 N  NH2 . ARG B 1 242 ? 101.127 -4.236  72.671  1.00 25.16 ? 244  ARG B NH2 1 
ATOM   5166 N  N   . ALA B 1 243 ? 103.570 -7.244  66.999  1.00 20.70 ? 245  ALA B N   1 
ATOM   5167 C  CA  . ALA B 1 243 ? 103.083 -8.242  66.053  1.00 19.76 ? 245  ALA B CA  1 
ATOM   5168 C  C   . ALA B 1 243 ? 104.147 -8.527  64.997  1.00 18.87 ? 245  ALA B C   1 
ATOM   5169 O  O   . ALA B 1 243 ? 104.438 -9.685  64.690  1.00 19.32 ? 245  ALA B O   1 
ATOM   5170 C  CB  . ALA B 1 243 ? 101.789 -7.774  65.398  1.00 18.30 ? 245  ALA B CB  1 
ATOM   5171 N  N   . ASP B 1 244 ? 104.742 -7.464  64.467  1.00 18.31 ? 246  ASP B N   1 
ATOM   5172 C  CA  . ASP B 1 244 ? 105.821 -7.589  63.497  1.00 18.17 ? 246  ASP B CA  1 
ATOM   5173 C  C   . ASP B 1 244 ? 106.971 -8.420  64.057  1.00 18.37 ? 246  ASP B C   1 
ATOM   5174 O  O   . ASP B 1 244 ? 107.503 -9.299  63.378  1.00 16.90 ? 246  ASP B O   1 
ATOM   5175 C  CB  . ASP B 1 244 ? 106.330 -6.209  63.073  1.00 18.68 ? 246  ASP B CB  1 
ATOM   5176 C  CG  . ASP B 1 244 ? 105.332 -5.457  62.209  1.00 21.62 ? 246  ASP B CG  1 
ATOM   5177 O  OD1 . ASP B 1 244 ? 104.387 -6.093  61.692  1.00 22.15 ? 246  ASP B OD1 1 
ATOM   5178 O  OD2 . ASP B 1 244 ? 105.497 -4.230  62.041  1.00 20.91 ? 246  ASP B OD2 1 
ATOM   5179 N  N   . LEU B 1 245 ? 107.353 -8.134  65.299  1.00 18.04 ? 247  LEU B N   1 
ATOM   5180 C  CA  . LEU B 1 245 ? 108.418 -8.875  65.964  1.00 17.39 ? 247  LEU B CA  1 
ATOM   5181 C  C   . LEU B 1 245 ? 108.118 -10.367 65.990  1.00 17.37 ? 247  LEU B C   1 
ATOM   5182 O  O   . LEU B 1 245 ? 108.983 -11.187 65.668  1.00 17.98 ? 247  LEU B O   1 
ATOM   5183 C  CB  . LEU B 1 245 ? 108.632 -8.354  67.389  1.00 16.82 ? 247  LEU B CB  1 
ATOM   5184 C  CG  . LEU B 1 245 ? 109.625 -9.132  68.256  1.00 16.89 ? 247  LEU B CG  1 
ATOM   5185 C  CD1 . LEU B 1 245 ? 111.004 -9.115  67.617  1.00 17.65 ? 247  LEU B CD1 1 
ATOM   5186 C  CD2 . LEU B 1 245 ? 109.680 -8.556  69.665  1.00 16.56 ? 247  LEU B CD2 1 
ATOM   5187 N  N   . LEU B 1 246 ? 106.892 -10.720 66.371  1.00 16.44 ? 248  LEU B N   1 
ATOM   5188 C  CA  . LEU B 1 246 ? 106.494 -12.121 66.409  1.00 16.61 ? 248  LEU B CA  1 
ATOM   5189 C  C   . LEU B 1 246 ? 106.589 -12.758 65.027  1.00 16.67 ? 248  LEU B C   1 
ATOM   5190 O  O   . LEU B 1 246 ? 107.087 -13.874 64.884  1.00 16.45 ? 248  LEU B O   1 
ATOM   5191 C  CB  . LEU B 1 246 ? 105.082 -12.281 66.975  1.00 16.33 ? 248  LEU B CB  1 
ATOM   5192 C  CG  . LEU B 1 246 ? 104.570 -13.720 67.085  1.00 17.36 ? 248  LEU B CG  1 
ATOM   5193 C  CD1 . LEU B 1 246 ? 105.571 -14.605 67.815  1.00 17.24 ? 248  LEU B CD1 1 
ATOM   5194 C  CD2 . LEU B 1 246 ? 103.211 -13.766 67.768  1.00 18.95 ? 248  LEU B CD2 1 
ATOM   5195 N  N   . GLY B 1 247 ? 106.129 -12.034 64.011  1.00 16.30 ? 249  GLY B N   1 
ATOM   5196 C  CA  . GLY B 1 247 ? 106.235 -12.493 62.629  1.00 15.25 ? 249  GLY B CA  1 
ATOM   5197 C  C   . GLY B 1 247 ? 107.668 -12.779 62.221  1.00 15.58 ? 249  GLY B C   1 
ATOM   5198 O  O   . GLY B 1 247 ? 107.965 -13.824 61.637  1.00 15.76 ? 249  GLY B O   1 
ATOM   5199 N  N   . ALA B 1 248 ? 108.559 -11.840 62.520  1.00 14.89 ? 250  ALA B N   1 
ATOM   5200 C  CA  . ALA B 1 248 ? 109.965 -11.984 62.176  1.00 15.39 ? 250  ALA B CA  1 
ATOM   5201 C  C   . ALA B 1 248 ? 110.614 -13.132 62.943  1.00 15.81 ? 250  ALA B C   1 
ATOM   5202 O  O   . ALA B 1 248 ? 111.481 -13.829 62.419  1.00 15.20 ? 250  ALA B O   1 
ATOM   5203 C  CB  . ALA B 1 248 ? 110.712 -10.680 62.419  1.00 14.27 ? 250  ALA B CB  1 
ATOM   5204 N  N   . ARG B 1 249 ? 110.165 -13.356 64.174  1.00 16.49 ? 251  ARG B N   1 
ATOM   5205 C  CA  . ARG B 1 249 ? 110.684 -14.461 64.963  1.00 16.54 ? 251  ARG B CA  1 
ATOM   5206 C  C   . ARG B 1 249 ? 110.173 -15.822 64.481  1.00 16.75 ? 251  ARG B C   1 
ATOM   5207 O  O   . ARG B 1 249 ? 110.823 -16.843 64.691  1.00 17.31 ? 251  ARG B O   1 
ATOM   5208 C  CB  . ARG B 1 249 ? 110.424 -14.243 66.458  1.00 18.17 ? 251  ARG B CB  1 
ATOM   5209 C  CG  . ARG B 1 249 ? 111.500 -13.386 67.113  1.00 18.71 ? 251  ARG B CG  1 
ATOM   5210 C  CD  . ARG B 1 249 ? 111.288 -13.216 68.607  1.00 20.72 ? 251  ARG B CD  1 
ATOM   5211 N  NE  . ARG B 1 249 ? 111.546 -14.439 69.365  1.00 20.44 ? 251  ARG B NE  1 
ATOM   5212 C  CZ  . ARG B 1 249 ? 112.752 -14.847 69.752  1.00 18.50 ? 251  ARG B CZ  1 
ATOM   5213 N  NH1 . ARG B 1 249 ? 113.837 -14.180 69.381  1.00 17.65 ? 251  ARG B NH1 1 
ATOM   5214 N  NH2 . ARG B 1 249 ? 112.875 -15.952 70.475  1.00 19.83 ? 251  ARG B NH2 1 
ATOM   5215 N  N   . MET B 1 250 ? 109.071 -15.815 63.739  1.00 16.12 ? 252  MET B N   1 
ATOM   5216 C  CA  . MET B 1 250 ? 108.586 -17.028 63.094  1.00 16.57 ? 252  MET B CA  1 
ATOM   5217 C  C   . MET B 1 250 ? 109.401 -17.373 61.856  1.00 15.11 ? 252  MET B C   1 
ATOM   5218 O  O   . MET B 1 250 ? 109.716 -18.537 61.619  1.00 13.68 ? 252  MET B O   1 
ATOM   5219 C  CB  . MET B 1 250 ? 107.109 -16.897 62.722  1.00 17.24 ? 252  MET B CB  1 
ATOM   5220 C  CG  . MET B 1 250 ? 106.160 -17.211 63.864  1.00 19.63 ? 252  MET B CG  1 
ATOM   5221 S  SD  . MET B 1 250 ? 104.445 -16.886 63.424  1.00 22.82 ? 252  MET B SD  1 
ATOM   5222 C  CE  . MET B 1 250 ? 103.661 -16.971 65.032  1.00 22.31 ? 252  MET B CE  1 
ATOM   5223 N  N   . VAL B 1 251 ? 109.715 -16.357 61.057  1.00 14.82 ? 253  VAL B N   1 
ATOM   5224 C  CA  . VAL B 1 251 ? 110.432 -16.559 59.802  1.00 14.91 ? 253  VAL B CA  1 
ATOM   5225 C  C   . VAL B 1 251 ? 111.932 -16.719 60.034  1.00 14.73 ? 253  VAL B C   1 
ATOM   5226 O  O   . VAL B 1 251 ? 112.572 -17.585 59.435  1.00 13.31 ? 253  VAL B O   1 
ATOM   5227 C  CB  . VAL B 1 251 ? 110.181 -15.397 58.818  1.00 14.36 ? 253  VAL B CB  1 
ATOM   5228 C  CG1 . VAL B 1 251 ? 111.055 -15.541 57.583  1.00 14.56 ? 253  VAL B CG1 1 
ATOM   5229 C  CG2 . VAL B 1 251 ? 108.710 -15.344 58.433  1.00 13.75 ? 253  VAL B CG2 1 
ATOM   5230 N  N   . GLY B 1 252 ? 112.481 -15.897 60.926  1.00 14.78 ? 254  GLY B N   1 
ATOM   5231 C  CA  . GLY B 1 252 ? 113.925 -15.807 61.101  1.00 13.56 ? 254  GLY B CA  1 
ATOM   5232 C  C   . GLY B 1 252 ? 114.476 -14.559 60.443  1.00 13.26 ? 254  GLY B C   1 
ATOM   5233 O  O   . GLY B 1 252 ? 115.676 -14.290 60.498  1.00 12.66 ? 254  GLY B O   1 
ATOM   5234 N  N   . ARG B 1 253 ? 113.591 -13.808 59.793  1.00 13.53 ? 255  ARG B N   1 
ATOM   5235 C  CA  . ARG B 1 253 ? 113.966 -12.557 59.146  1.00 13.39 ? 255  ARG B CA  1 
ATOM   5236 C  C   . ARG B 1 253 ? 112.841 -11.549 59.327  1.00 13.52 ? 255  ARG B C   1 
ATOM   5237 O  O   . ARG B 1 253 ? 111.673 -11.924 59.373  1.00 14.90 ? 255  ARG B O   1 
ATOM   5238 C  CB  . ARG B 1 253 ? 114.200 -12.774 57.649  1.00 13.43 ? 255  ARG B CB  1 
ATOM   5239 C  CG  . ARG B 1 253 ? 115.469 -13.536 57.300  1.00 13.52 ? 255  ARG B CG  1 
ATOM   5240 C  CD  . ARG B 1 253 ? 115.660 -13.583 55.790  1.00 13.62 ? 255  ARG B CD  1 
ATOM   5241 N  NE  . ARG B 1 253 ? 116.806 -14.400 55.407  1.00 13.74 ? 255  ARG B NE  1 
ATOM   5242 C  CZ  . ARG B 1 253 ? 118.067 -13.980 55.436  1.00 13.05 ? 255  ARG B CZ  1 
ATOM   5243 N  NH1 . ARG B 1 253 ? 118.351 -12.739 55.814  1.00 13.24 ? 255  ARG B NH1 1 
ATOM   5244 N  NH2 . ARG B 1 253 ? 119.047 -14.804 55.095  1.00 12.86 ? 255  ARG B NH2 1 
ATOM   5245 N  N   . TRP B 1 254 ? 113.197 -10.273 59.418  1.00 13.36 ? 256  TRP B N   1 
ATOM   5246 C  CA  . TRP B 1 254 ? 112.222 -9.205  59.258  1.00 14.07 ? 256  TRP B CA  1 
ATOM   5247 C  C   . TRP B 1 254 ? 111.735 -9.182  57.813  1.00 13.68 ? 256  TRP B C   1 
ATOM   5248 O  O   . TRP B 1 254 ? 112.361 -9.771  56.936  1.00 13.26 ? 256  TRP B O   1 
ATOM   5249 C  CB  . TRP B 1 254 ? 112.841 -7.858  59.642  1.00 14.95 ? 256  TRP B CB  1 
ATOM   5250 C  CG  . TRP B 1 254 ? 113.263 -7.803  61.083  1.00 15.64 ? 256  TRP B CG  1 
ATOM   5251 C  CD1 . TRP B 1 254 ? 114.468 -8.187  61.599  1.00 16.08 ? 256  TRP B CD1 1 
ATOM   5252 C  CD2 . TRP B 1 254 ? 112.455 -7.410  62.200  1.00 17.24 ? 256  TRP B CD2 1 
ATOM   5253 N  NE1 . TRP B 1 254 ? 114.466 -8.037  62.968  1.00 17.80 ? 256  TRP B NE1 1 
ATOM   5254 C  CE2 . TRP B 1 254 ? 113.243 -7.558  63.360  1.00 16.95 ? 256  TRP B CE2 1 
ATOM   5255 C  CE3 . TRP B 1 254 ? 111.144 -6.940  62.332  1.00 16.55 ? 256  TRP B CE3 1 
ATOM   5256 C  CZ2 . TRP B 1 254 ? 112.767 -7.244  64.632  1.00 18.53 ? 256  TRP B CZ2 1 
ATOM   5257 C  CZ3 . TRP B 1 254 ? 110.673 -6.624  63.597  1.00 17.69 ? 256  TRP B CZ3 1 
ATOM   5258 C  CH2 . TRP B 1 254 ? 111.482 -6.782  64.731  1.00 18.74 ? 256  TRP B CH2 1 
ATOM   5259 N  N   . LYS B 1 255 ? 110.614 -8.513  57.567  1.00 13.79 ? 257  LYS B N   1 
ATOM   5260 C  CA  . LYS B 1 255 ? 110.068 -8.426  56.214  1.00 14.02 ? 257  LYS B CA  1 
ATOM   5261 C  C   . LYS B 1 255 ? 111.040 -7.750  55.250  1.00 14.19 ? 257  LYS B C   1 
ATOM   5262 O  O   . LYS B 1 255 ? 110.971 -7.954  54.040  1.00 15.30 ? 257  LYS B O   1 
ATOM   5263 C  CB  . LYS B 1 255 ? 108.721 -7.698  56.223  1.00 13.54 ? 257  LYS B CB  1 
ATOM   5264 C  CG  . LYS B 1 255 ? 107.591 -8.531  56.804  1.00 13.87 ? 257  LYS B CG  1 
ATOM   5265 C  CD  . LYS B 1 255 ? 106.290 -7.748  56.891  1.00 14.00 ? 257  LYS B CD  1 
ATOM   5266 C  CE  . LYS B 1 255 ? 105.140 -8.656  57.303  1.00 14.82 ? 257  LYS B CE  1 
ATOM   5267 N  NZ  . LYS B 1 255 ? 103.881 -7.887  57.524  1.00 15.93 ? 257  LYS B NZ  1 
ATOM   5268 N  N   . SER B 1 256 ? 111.959 -6.960  55.796  1.00 14.12 ? 258  SER B N   1 
ATOM   5269 C  CA  . SER B 1 256 ? 112.961 -6.264  54.988  1.00 14.92 ? 258  SER B CA  1 
ATOM   5270 C  C   . SER B 1 256 ? 114.079 -7.201  54.541  1.00 14.79 ? 258  SER B C   1 
ATOM   5271 O  O   . SER B 1 256 ? 114.916 -6.832  53.717  1.00 16.31 ? 258  SER B O   1 
ATOM   5272 C  CB  . SER B 1 256 ? 113.574 -5.123  55.793  1.00 16.48 ? 258  SER B CB  1 
ATOM   5273 O  OG  . SER B 1 256 ? 114.360 -5.645  56.850  1.00 15.99 ? 258  SER B OG  1 
ATOM   5274 N  N   . GLY B 1 257 ? 114.131 -8.387  55.136  1.00 13.86 ? 259  GLY B N   1 
ATOM   5275 C  CA  . GLY B 1 257 ? 115.181 -9.350  54.815  1.00 13.54 ? 259  GLY B CA  1 
ATOM   5276 C  C   . GLY B 1 257 ? 116.329 -9.351  55.809  1.00 13.93 ? 259  GLY B C   1 
ATOM   5277 O  O   . GLY B 1 257 ? 117.231 -10.184 55.726  1.00 12.96 ? 259  GLY B O   1 
ATOM   5278 N  N   . ALA B 1 258 ? 116.306 -8.414  56.751  1.00 13.99 ? 260  ALA B N   1 
ATOM   5279 C  CA  . ALA B 1 258 ? 117.295 -8.411  57.824  1.00 14.60 ? 260  ALA B CA  1 
ATOM   5280 C  C   . ALA B 1 258 ? 117.128 -9.658  58.682  1.00 14.23 ? 260  ALA B C   1 
ATOM   5281 O  O   . ALA B 1 258 ? 116.045 -9.911  59.206  1.00 15.08 ? 260  ALA B O   1 
ATOM   5282 C  CB  . ALA B 1 258 ? 117.157 -7.155  58.675  1.00 14.80 ? 260  ALA B CB  1 
ATOM   5283 N  N   . PRO B 1 259 ? 118.205 -10.442 58.834  1.00 14.17 ? 261  PRO B N   1 
ATOM   5284 C  CA  . PRO B 1 259 ? 118.137 -11.645 59.656  1.00 14.60 ? 261  PRO B CA  1 
ATOM   5285 C  C   . PRO B 1 259 ? 118.070 -11.301 61.141  1.00 15.00 ? 261  PRO B C   1 
ATOM   5286 O  O   . PRO B 1 259 ? 118.907 -10.555 61.642  1.00 15.59 ? 261  PRO B O   1 
ATOM   5287 C  CB  . PRO B 1 259 ? 119.454 -12.357 59.339  1.00 14.86 ? 261  PRO B CB  1 
ATOM   5288 C  CG  . PRO B 1 259 ? 120.391 -11.259 58.966  1.00 14.53 ? 261  PRO B CG  1 
ATOM   5289 C  CD  . PRO B 1 259 ? 119.552 -10.214 58.282  1.00 14.26 ? 261  PRO B CD  1 
ATOM   5290 N  N   . ILE B 1 260 ? 117.082 -11.847 61.840  1.00 16.61 ? 262  ILE B N   1 
ATOM   5291 C  CA  . ILE B 1 260 ? 116.886 -11.510 63.247  1.00 18.72 ? 262  ILE B CA  1 
ATOM   5292 C  C   . ILE B 1 260 ? 118.084 -11.913 64.107  1.00 18.99 ? 262  ILE B C   1 
ATOM   5293 O  O   . ILE B 1 260 ? 118.309 -11.347 65.176  1.00 19.83 ? 262  ILE B O   1 
ATOM   5294 C  CB  . ILE B 1 260 ? 115.590 -12.121 63.814  1.00 18.43 ? 262  ILE B CB  1 
ATOM   5295 C  CG1 . ILE B 1 260 ? 115.654 -13.650 63.794  1.00 18.36 ? 262  ILE B CG1 1 
ATOM   5296 C  CG2 . ILE B 1 260 ? 114.382 -11.623 63.036  1.00 17.77 ? 262  ILE B CG2 1 
ATOM   5297 C  CD1 . ILE B 1 260 ? 114.441 -14.316 64.404  1.00 19.33 ? 262  ILE B CD1 1 
ATOM   5298 N  N   . ASP B 1 261 ? 118.879 -12.855 63.610  1.00 19.03 ? 263  ASP B N   1 
ATOM   5299 C  CA  . ASP B 1 261 ? 120.074 -13.301 64.322  1.00 20.28 ? 263  ASP B CA  1 
ATOM   5300 C  C   . ASP B 1 261 ? 121.104 -12.182 64.455  1.00 21.29 ? 263  ASP B C   1 
ATOM   5301 O  O   . ASP B 1 261 ? 121.907 -12.170 65.390  1.00 21.50 ? 263  ASP B O   1 
ATOM   5302 C  CB  . ASP B 1 261 ? 120.700 -14.505 63.615  1.00 21.46 ? 263  ASP B CB  1 
ATOM   5303 C  CG  . ASP B 1 261 ? 121.807 -15.148 64.431  1.00 21.12 ? 263  ASP B CG  1 
ATOM   5304 O  OD1 . ASP B 1 261 ? 121.497 -15.755 65.477  1.00 22.28 ? 263  ASP B OD1 1 
ATOM   5305 O  OD2 . ASP B 1 261 ? 122.983 -15.046 64.025  1.00 21.87 ? 263  ASP B OD2 1 
ATOM   5306 N  N   . LEU B 1 262 ? 121.072 -11.239 63.518  1.00 19.85 ? 264  LEU B N   1 
ATOM   5307 C  CA  . LEU B 1 262 ? 121.974 -10.094 63.554  1.00 20.28 ? 264  LEU B CA  1 
ATOM   5308 C  C   . LEU B 1 262 ? 121.294 -8.844  64.115  1.00 21.09 ? 264  LEU B C   1 
ATOM   5309 O  O   . LEU B 1 262 ? 121.955 -7.846  64.403  1.00 21.99 ? 264  LEU B O   1 
ATOM   5310 C  CB  . LEU B 1 262 ? 122.538 -9.807  62.161  1.00 19.38 ? 264  LEU B CB  1 
ATOM   5311 C  CG  . LEU B 1 262 ? 123.370 -10.920 61.520  1.00 19.71 ? 264  LEU B CG  1 
ATOM   5312 C  CD1 . LEU B 1 262 ? 124.018 -10.430 60.233  1.00 20.08 ? 264  LEU B CD1 1 
ATOM   5313 C  CD2 . LEU B 1 262 ? 124.420 -11.442 62.491  1.00 20.12 ? 264  LEU B CD2 1 
ATOM   5314 N  N   . THR B 1 263 ? 119.972 -8.898  64.257  1.00 20.53 ? 265  THR B N   1 
ATOM   5315 C  CA  . THR B 1 263 ? 119.215 -7.768  64.787  1.00 20.56 ? 265  THR B CA  1 
ATOM   5316 C  C   . THR B 1 263 ? 117.897 -8.222  65.406  1.00 20.95 ? 265  THR B C   1 
ATOM   5317 O  O   . THR B 1 263 ? 116.845 -8.145  64.776  1.00 21.20 ? 265  THR B O   1 
ATOM   5318 C  CB  . THR B 1 263 ? 118.960 -6.695  63.714  1.00 21.67 ? 265  THR B CB  1 
ATOM   5319 O  OG1 . THR B 1 263 ? 118.263 -5.586  64.299  1.00 24.04 ? 265  THR B OG1 1 
ATOM   5320 C  CG2 . THR B 1 263 ? 118.144 -7.263  62.556  1.00 20.38 ? 265  THR B CG2 1 
ATOM   5321 N  N   . PRO B 1 264 ? 117.960 -8.696  66.658  1.00 20.72 ? 266  PRO B N   1 
ATOM   5322 C  CA  . PRO B 1 264 ? 116.934 -9.571  67.216  1.00 20.88 ? 266  PRO B CA  1 
ATOM   5323 C  C   . PRO B 1 264 ? 115.623 -8.875  67.574  1.00 19.23 ? 266  PRO B C   1 
ATOM   5324 O  O   . PRO B 1 264 ? 114.590 -9.535  67.655  1.00 20.04 ? 266  PRO B O   1 
ATOM   5325 C  CB  . PRO B 1 264 ? 117.602 -10.132 68.476  1.00 20.62 ? 266  PRO B CB  1 
ATOM   5326 C  CG  . PRO B 1 264 ? 119.062 -10.049 68.189  1.00 20.74 ? 266  PRO B CG  1 
ATOM   5327 C  CD  . PRO B 1 264 ? 119.217 -8.771  67.421  1.00 20.40 ? 266  PRO B CD  1 
ATOM   5328 N  N   . THR B 1 265 ? 115.658 -7.568  67.816  1.00 19.73 ? 267  THR B N   1 
ATOM   5329 C  CA  . THR B 1 265 ? 114.477 -6.885  68.347  1.00 20.47 ? 267  THR B CA  1 
ATOM   5330 C  C   . THR B 1 265 ? 114.104 -5.608  67.599  1.00 21.87 ? 267  THR B C   1 
ATOM   5331 O  O   . THR B 1 265 ? 113.126 -4.945  67.941  1.00 21.89 ? 267  THR B O   1 
ATOM   5332 C  CB  . THR B 1 265 ? 114.605 -6.587  69.855  1.00 20.16 ? 267  THR B CB  1 
ATOM   5333 O  OG1 . THR B 1 265 ? 115.783 -5.809  70.098  1.00 20.18 ? 267  THR B OG1 1 
ATOM   5334 C  CG2 . THR B 1 265 ? 114.678 -7.881  70.651  1.00 19.96 ? 267  THR B CG2 1 
ATOM   5335 N  N   . ALA B 1 266 ? 114.865 -5.278  66.564  1.00 21.27 ? 268  ALA B N   1 
ATOM   5336 C  CA  . ALA B 1 266 ? 114.478 -4.199  65.667  1.00 21.64 ? 268  ALA B CA  1 
ATOM   5337 C  C   . ALA B 1 266 ? 114.859 -4.523  64.230  1.00 22.62 ? 268  ALA B C   1 
ATOM   5338 O  O   . ALA B 1 266 ? 115.910 -5.107  63.971  1.00 20.83 ? 268  ALA B O   1 
ATOM   5339 C  CB  . ALA B 1 266 ? 115.112 -2.887  66.104  1.00 22.92 ? 268  ALA B CB  1 
ATOM   5340 N  N   . ASP B 1 267 ? 114.003 -4.126  63.294  1.00 21.57 ? 269  ASP B N   1 
ATOM   5341 C  CA  . ASP B 1 267 ? 114.311 -4.269  61.879  1.00 20.81 ? 269  ASP B CA  1 
ATOM   5342 C  C   . ASP B 1 267 ? 115.489 -3.375  61.503  1.00 21.45 ? 269  ASP B C   1 
ATOM   5343 O  O   . ASP B 1 267 ? 115.781 -2.398  62.191  1.00 23.00 ? 269  ASP B O   1 
ATOM   5344 C  CB  . ASP B 1 267 ? 113.083 -3.927  61.034  1.00 20.80 ? 269  ASP B CB  1 
ATOM   5345 C  CG  . ASP B 1 267 ? 113.317 -4.127  59.549  1.00 21.39 ? 269  ASP B CG  1 
ATOM   5346 O  OD1 . ASP B 1 267 ? 114.199 -4.933  59.177  1.00 18.94 ? 269  ASP B OD1 1 
ATOM   5347 O  OD2 . ASP B 1 267 ? 112.621 -3.463  58.756  1.00 21.37 ? 269  ASP B OD2 1 
ATOM   5348 N  N   . ASP B 1 268 ? 116.210 -3.764  60.457  1.00 21.24 ? 270  ASP B N   1 
ATOM   5349 C  CA  . ASP B 1 268 ? 117.317 -2.971  59.936  1.00 21.42 ? 270  ASP B CA  1 
ATOM   5350 C  C   . ASP B 1 268 ? 117.306 -3.033  58.413  1.00 20.93 ? 270  ASP B C   1 
ATOM   5351 O  O   . ASP B 1 268 ? 117.994 -3.862  57.816  1.00 20.18 ? 270  ASP B O   1 
ATOM   5352 C  CB  . ASP B 1 268 ? 118.649 -3.499  60.478  1.00 22.12 ? 270  ASP B CB  1 
ATOM   5353 C  CG  . ASP B 1 268 ? 119.834 -2.635  60.076  1.00 23.00 ? 270  ASP B CG  1 
ATOM   5354 O  OD1 . ASP B 1 268 ? 119.734 -1.906  59.068  1.00 23.45 ? 270  ASP B OD1 1 
ATOM   5355 O  OD2 . ASP B 1 268 ? 120.878 -2.704  60.760  1.00 24.45 ? 270  ASP B OD2 1 
ATOM   5356 N  N   . PRO B 1 269 ? 116.483 -2.182  57.781  1.00 21.06 ? 271  PRO B N   1 
ATOM   5357 C  CA  . PRO B 1 269 ? 116.232 -2.244  56.343  1.00 21.28 ? 271  PRO B CA  1 
ATOM   5358 C  C   . PRO B 1 269 ? 117.515 -2.236  55.515  1.00 20.34 ? 271  PRO B C   1 
ATOM   5359 O  O   . PRO B 1 269 ? 117.607 -2.940  54.510  1.00 20.42 ? 271  PRO B O   1 
ATOM   5360 C  CB  . PRO B 1 269 ? 115.424 -0.973  56.080  1.00 21.69 ? 271  PRO B CB  1 
ATOM   5361 C  CG  . PRO B 1 269 ? 114.693 -0.736  57.357  1.00 22.77 ? 271  PRO B CG  1 
ATOM   5362 C  CD  . PRO B 1 269 ? 115.602 -1.212  58.458  1.00 21.70 ? 271  PRO B CD  1 
ATOM   5363 N  N   . ALA B 1 270 ? 118.483 -1.422  55.919  1.00 20.49 ? 272  ALA B N   1 
ATOM   5364 C  CA  . ALA B 1 270 ? 119.756 -1.344  55.213  1.00 20.00 ? 272  ALA B CA  1 
ATOM   5365 C  C   . ALA B 1 270 ? 120.462 -2.696  55.221  1.00 19.34 ? 272  ALA B C   1 
ATOM   5366 O  O   . ALA B 1 270 ? 120.950 -3.158  54.192  1.00 20.62 ? 272  ALA B O   1 
ATOM   5367 C  CB  . ALA B 1 270 ? 120.645 -0.274  55.835  1.00 19.72 ? 272  ALA B CB  1 
ATOM   5368 N  N   . LEU B 1 271 ? 120.512 -3.326  56.388  1.00 18.95 ? 273  LEU B N   1 
ATOM   5369 C  CA  . LEU B 1 271 ? 121.050 -4.676  56.504  1.00 18.92 ? 273  LEU B CA  1 
ATOM   5370 C  C   . LEU B 1 271 ? 120.335 -5.643  55.557  1.00 18.95 ? 273  LEU B C   1 
ATOM   5371 O  O   . LEU B 1 271 ? 120.976 -6.365  54.792  1.00 18.96 ? 273  LEU B O   1 
ATOM   5372 C  CB  . LEU B 1 271 ? 120.948 -5.169  57.948  1.00 18.93 ? 273  LEU B CB  1 
ATOM   5373 C  CG  . LEU B 1 271 ? 121.366 -6.616  58.218  1.00 19.05 ? 273  LEU B CG  1 
ATOM   5374 C  CD1 . LEU B 1 271 ? 122.733 -6.898  57.614  1.00 19.41 ? 273  LEU B CD1 1 
ATOM   5375 C  CD2 . LEU B 1 271 ? 121.371 -6.894  59.714  1.00 19.50 ? 273  LEU B CD2 1 
ATOM   5376 N  N   . GLY B 1 272 ? 119.007 -5.642  55.605  1.00 17.79 ? 274  GLY B N   1 
ATOM   5377 C  CA  . GLY B 1 272 ? 118.208 -6.565  54.804  1.00 18.65 ? 274  GLY B CA  1 
ATOM   5378 C  C   . GLY B 1 272 ? 118.464 -6.445  53.313  1.00 19.54 ? 274  GLY B C   1 
ATOM   5379 O  O   . GLY B 1 272 ? 118.380 -7.429  52.579  1.00 20.32 ? 274  GLY B O   1 
ATOM   5380 N  N   . ALA B 1 273 ? 118.779 -5.235  52.863  1.00 20.32 ? 275  ALA B N   1 
ATOM   5381 C  CA  . ALA B 1 273 ? 118.943 -4.968  51.440  1.00 20.81 ? 275  ALA B CA  1 
ATOM   5382 C  C   . ALA B 1 273 ? 120.361 -5.273  50.959  1.00 21.74 ? 275  ALA B C   1 
ATOM   5383 O  O   . ALA B 1 273 ? 120.642 -5.236  49.761  1.00 22.59 ? 275  ALA B O   1 
ATOM   5384 C  CB  . ALA B 1 273 ? 118.570 -3.528  51.126  1.00 21.80 ? 275  ALA B CB  1 
ATOM   5385 N  N   . ASP B 1 274 ? 121.243 -5.609  51.894  1.00 19.96 ? 276  ASP B N   1 
ATOM   5386 C  CA  . ASP B 1 274 ? 122.665 -5.726  51.597  1.00 19.56 ? 276  ASP B CA  1 
ATOM   5387 C  C   . ASP B 1 274 ? 123.110 -7.189  51.560  1.00 18.36 ? 276  ASP B C   1 
ATOM   5388 O  O   . ASP B 1 274 ? 123.230 -7.838  52.600  1.00 17.13 ? 276  ASP B O   1 
ATOM   5389 C  CB  . ASP B 1 274 ? 123.480 -4.944  52.630  1.00 19.32 ? 276  ASP B CB  1 
ATOM   5390 C  CG  . ASP B 1 274 ? 124.969 -4.959  52.338  1.00 21.04 ? 276  ASP B CG  1 
ATOM   5391 O  OD1 . ASP B 1 274 ? 125.399 -5.685  51.416  1.00 21.26 ? 276  ASP B OD1 1 
ATOM   5392 O  OD2 . ASP B 1 274 ? 125.713 -4.244  53.040  1.00 20.99 ? 276  ASP B OD2 1 
ATOM   5393 N  N   . ALA B 1 275 ? 123.362 -7.697  50.357  1.00 18.69 ? 277  ALA B N   1 
ATOM   5394 C  CA  . ALA B 1 275 ? 123.672 -9.114  50.167  1.00 17.90 ? 277  ALA B CA  1 
ATOM   5395 C  C   . ALA B 1 275 ? 125.018 -9.489  50.778  1.00 18.00 ? 277  ALA B C   1 
ATOM   5396 O  O   . ALA B 1 275 ? 125.315 -10.668 50.969  1.00 17.59 ? 277  ALA B O   1 
ATOM   5397 C  CB  . ALA B 1 275 ? 123.643 -9.471  48.689  1.00 18.41 ? 277  ALA B CB  1 
ATOM   5398 N  N   . GLN B 1 276 ? 125.821 -8.479  51.098  1.00 18.23 ? 278  GLN B N   1 
ATOM   5399 C  CA  . GLN B 1 276 ? 127.129 -8.701  51.701  1.00 18.64 ? 278  GLN B CA  1 
ATOM   5400 C  C   . GLN B 1 276 ? 127.037 -8.952  53.201  1.00 19.19 ? 278  GLN B C   1 
ATOM   5401 O  O   . GLN B 1 276 ? 128.011 -9.372  53.823  1.00 19.62 ? 278  GLN B O   1 
ATOM   5402 C  CB  . GLN B 1 276 ? 128.062 -7.521  51.419  1.00 19.67 ? 278  GLN B CB  1 
ATOM   5403 C  CG  . GLN B 1 276 ? 128.590 -7.482  49.994  1.00 19.52 ? 278  GLN B CG  1 
ATOM   5404 C  CD  . GLN B 1 276 ? 129.337 -8.747  49.619  1.00 20.22 ? 278  GLN B CD  1 
ATOM   5405 O  OE1 . GLN B 1 276 ? 130.224 -9.195  50.345  1.00 19.98 ? 278  GLN B OE1 1 
ATOM   5406 N  NE2 . GLN B 1 276 ? 128.984 -9.328  48.478  1.00 19.29 ? 278  GLN B NE2 1 
ATOM   5407 N  N   . ARG B 1 277 ? 125.858 -8.729  53.776  1.00 18.72 ? 279  ARG B N   1 
ATOM   5408 C  CA  . ARG B 1 277 ? 125.695 -8.829  55.222  1.00 18.85 ? 279  ARG B CA  1 
ATOM   5409 C  C   . ARG B 1 277 ? 124.465 -9.626  55.651  1.00 18.41 ? 279  ARG B C   1 
ATOM   5410 O  O   . ARG B 1 277 ? 124.445 -10.198 56.741  1.00 18.31 ? 279  ARG B O   1 
ATOM   5411 C  CB  . ARG B 1 277 ? 125.669 -7.435  55.858  1.00 20.88 ? 279  ARG B CB  1 
ATOM   5412 C  CG  . ARG B 1 277 ? 126.902 -6.602  55.556  1.00 21.73 ? 279  ARG B CG  1 
ATOM   5413 C  CD  . ARG B 1 277 ? 127.018 -5.420  56.504  1.00 25.28 ? 279  ARG B CD  1 
ATOM   5414 N  NE  . ARG B 1 277 ? 125.909 -4.485  56.355  1.00 22.95 ? 279  ARG B NE  1 
ATOM   5415 C  CZ  . ARG B 1 277 ? 125.133 -4.082  57.355  1.00 26.07 ? 279  ARG B CZ  1 
ATOM   5416 N  NH1 . ARG B 1 277 ? 125.341 -4.533  58.585  1.00 27.04 ? 279  ARG B NH1 1 
ATOM   5417 N  NH2 . ARG B 1 277 ? 124.152 -3.220  57.127  1.00 25.03 ? 279  ARG B NH2 1 
ATOM   5418 N  N   . ASN B 1 278 ? 123.442 -9.668  54.801  1.00 16.97 ? 280  ASN B N   1 
ATOM   5419 C  CA  . ASN B 1 278 ? 122.148 -10.209 55.220  1.00 16.58 ? 280  ASN B CA  1 
ATOM   5420 C  C   . ASN B 1 278 ? 122.110 -11.728 55.401  1.00 15.60 ? 280  ASN B C   1 
ATOM   5421 O  O   . ASN B 1 278 ? 121.128 -12.273 55.907  1.00 15.12 ? 280  ASN B O   1 
ATOM   5422 C  CB  . ASN B 1 278 ? 121.011 -9.729  54.309  1.00 16.13 ? 280  ASN B CB  1 
ATOM   5423 C  CG  . ASN B 1 278 ? 121.096 -10.303 52.908  1.00 16.24 ? 280  ASN B CG  1 
ATOM   5424 O  OD1 . ASN B 1 278 ? 121.877 -11.215 52.641  1.00 16.07 ? 280  ASN B OD1 1 
ATOM   5425 N  ND2 . ASN B 1 278 ? 120.292 -9.761  52.002  1.00 16.54 ? 280  ASN B ND2 1 
ATOM   5426 N  N   . ASN B 1 279 ? 123.196 -12.402 55.033  1.00 15.33 ? 281  ASN B N   1 
ATOM   5427 C  CA  . ASN B 1 279 ? 123.313 -13.840 55.270  1.00 15.26 ? 281  ASN B CA  1 
ATOM   5428 C  C   . ASN B 1 279 ? 124.531 -14.187 56.113  1.00 15.61 ? 281  ASN B C   1 
ATOM   5429 O  O   . ASN B 1 279 ? 124.859 -15.359 56.292  1.00 14.50 ? 281  ASN B O   1 
ATOM   5430 C  CB  . ASN B 1 279 ? 123.363 -14.609 53.946  1.00 14.14 ? 281  ASN B CB  1 
ATOM   5431 C  CG  . ASN B 1 279 ? 122.629 -15.937 54.015  1.00 13.70 ? 281  ASN B CG  1 
ATOM   5432 O  OD1 . ASN B 1 279 ? 121.783 -16.151 54.888  1.00 12.85 ? 281  ASN B OD1 1 
ATOM   5433 N  ND2 . ASN B 1 279 ? 122.931 -16.829 53.077  1.00 13.72 ? 281  ASN B ND2 1 
ATOM   5434 N  N   . ASN B 1 280 ? 125.190 -13.159 56.640  1.00 16.05 ? 282  ASN B N   1 
ATOM   5435 C  CA  . ASN B 1 280 ? 126.493 -13.318 57.279  1.00 17.01 ? 282  ASN B CA  1 
ATOM   5436 C  C   . ASN B 1 280 ? 126.396 -13.742 58.749  1.00 18.47 ? 282  ASN B C   1 
ATOM   5437 O  O   . ASN B 1 280 ? 126.849 -13.027 59.649  1.00 17.93 ? 282  ASN B O   1 
ATOM   5438 C  CB  . ASN B 1 280 ? 127.299 -12.025 57.130  1.00 18.26 ? 282  ASN B CB  1 
ATOM   5439 C  CG  . ASN B 1 280 ? 128.735 -12.172 57.589  1.00 20.17 ? 282  ASN B CG  1 
ATOM   5440 O  OD1 . ASN B 1 280 ? 129.349 -13.225 57.423  1.00 18.64 ? 282  ASN B OD1 1 
ATOM   5441 N  ND2 . ASN B 1 280 ? 129.280 -11.105 58.164  1.00 22.20 ? 282  ASN B ND2 1 
ATOM   5442 N  N   . PHE B 1 281 ? 125.809 -14.912 58.989  1.00 16.46 ? 283  PHE B N   1 
ATOM   5443 C  CA  . PHE B 1 281 ? 125.606 -15.404 60.349  1.00 17.27 ? 283  PHE B CA  1 
ATOM   5444 C  C   . PHE B 1 281 ? 125.596 -16.931 60.408  1.00 17.21 ? 283  PHE B C   1 
ATOM   5445 O  O   . PHE B 1 281 ? 125.379 -17.603 59.399  1.00 15.62 ? 283  PHE B O   1 
ATOM   5446 C  CB  . PHE B 1 281 ? 124.310 -14.838 60.944  1.00 16.88 ? 283  PHE B CB  1 
ATOM   5447 C  CG  . PHE B 1 281 ? 123.075 -15.205 60.168  1.00 15.73 ? 283  PHE B CG  1 
ATOM   5448 C  CD1 . PHE B 1 281 ? 122.724 -14.504 59.025  1.00 15.70 ? 283  PHE B CD1 1 
ATOM   5449 C  CD2 . PHE B 1 281 ? 122.272 -16.258 60.574  1.00 15.53 ? 283  PHE B CD2 1 
ATOM   5450 C  CE1 . PHE B 1 281 ? 121.597 -14.850 58.301  1.00 14.64 ? 283  PHE B CE1 1 
ATOM   5451 C  CE2 . PHE B 1 281 ? 121.139 -16.601 59.860  1.00 14.60 ? 283  PHE B CE2 1 
ATOM   5452 C  CZ  . PHE B 1 281 ? 120.801 -15.896 58.723  1.00 14.92 ? 283  PHE B CZ  1 
ATOM   5453 N  N   . THR B 1 282 ? 125.834 -17.473 61.598  1.00 17.03 ? 284  THR B N   1 
ATOM   5454 C  CA  . THR B 1 282 ? 125.889 -18.916 61.793  1.00 17.07 ? 284  THR B CA  1 
ATOM   5455 C  C   . THR B 1 282 ? 124.892 -19.357 62.860  1.00 16.87 ? 284  THR B C   1 
ATOM   5456 O  O   . THR B 1 282 ? 124.623 -20.548 63.015  1.00 15.26 ? 284  THR B O   1 
ATOM   5457 C  CB  . THR B 1 282 ? 127.294 -19.364 62.234  1.00 17.37 ? 284  THR B CB  1 
ATOM   5458 O  OG1 . THR B 1 282 ? 127.578 -18.833 63.536  1.00 17.63 ? 284  THR B OG1 1 
ATOM   5459 C  CG2 . THR B 1 282 ? 128.340 -18.880 61.249  1.00 17.75 ? 284  THR B CG2 1 
ATOM   5460 N  N   . TYR B 1 283 ? 124.328 -18.378 63.566  1.00 16.64 ? 285  TYR B N   1 
ATOM   5461 C  CA  . TYR B 1 283 ? 123.496 -18.610 64.753  1.00 17.02 ? 285  TYR B CA  1 
ATOM   5462 C  C   . TYR B 1 283 ? 124.310 -18.665 66.043  1.00 17.60 ? 285  TYR B C   1 
ATOM   5463 O  O   . TYR B 1 283 ? 123.751 -18.720 67.139  1.00 17.85 ? 285  TYR B O   1 
ATOM   5464 C  CB  . TYR B 1 283 ? 122.616 -19.855 64.609  1.00 16.80 ? 285  TYR B CB  1 
ATOM   5465 C  CG  . TYR B 1 283 ? 121.547 -19.719 63.547  1.00 17.04 ? 285  TYR B CG  1 
ATOM   5466 C  CD1 . TYR B 1 283 ? 120.662 -18.645 63.555  1.00 17.10 ? 285  TYR B CD1 1 
ATOM   5467 C  CD2 . TYR B 1 283 ? 121.448 -20.642 62.514  1.00 16.73 ? 285  TYR B CD2 1 
ATOM   5468 C  CE1 . TYR B 1 283 ? 119.704 -18.501 62.567  1.00 16.79 ? 285  TYR B CE1 1 
ATOM   5469 C  CE2 . TYR B 1 283 ? 120.504 -20.502 61.517  1.00 16.24 ? 285  TYR B CE2 1 
ATOM   5470 C  CZ  . TYR B 1 283 ? 119.630 -19.436 61.550  1.00 16.80 ? 285  TYR B CZ  1 
ATOM   5471 O  OH  . TYR B 1 283 ? 118.690 -19.302 60.556  1.00 15.11 ? 285  TYR B OH  1 
ATOM   5472 N  N   . SER B 1 284 ? 125.631 -18.629 65.910  1.00 19.18 ? 286  SER B N   1 
ATOM   5473 C  CA  . SER B 1 284 ? 126.505 -18.603 67.076  1.00 19.93 ? 286  SER B CA  1 
ATOM   5474 C  C   . SER B 1 284 ? 126.796 -17.171 67.511  1.00 20.28 ? 286  SER B C   1 
ATOM   5475 O  O   . SER B 1 284 ? 126.956 -16.280 66.676  1.00 20.66 ? 286  SER B O   1 
ATOM   5476 C  CB  . SER B 1 284 ? 127.814 -19.336 66.786  1.00 21.19 ? 286  SER B CB  1 
ATOM   5477 O  OG  . SER B 1 284 ? 128.647 -19.336 67.931  1.00 21.62 ? 286  SER B OG  1 
ATOM   5478 N  N   . HIS B 1 285 ? 126.859 -16.958 68.824  1.00 20.60 ? 287  HIS B N   1 
ATOM   5479 C  CA  . HIS B 1 285 ? 127.194 -15.650 69.374  1.00 22.09 ? 287  HIS B CA  1 
ATOM   5480 C  C   . HIS B 1 285 ? 128.093 -15.779 70.602  1.00 21.46 ? 287  HIS B C   1 
ATOM   5481 O  O   . HIS B 1 285 ? 127.828 -16.582 71.495  1.00 21.26 ? 287  HIS B O   1 
ATOM   5482 C  CB  . HIS B 1 285 ? 125.923 -14.878 69.740  1.00 20.60 ? 287  HIS B CB  1 
ATOM   5483 C  CG  . HIS B 1 285 ? 124.969 -14.712 68.599  1.00 20.28 ? 287  HIS B CG  1 
ATOM   5484 N  ND1 . HIS B 1 285 ? 125.008 -13.628 67.748  1.00 21.43 ? 287  HIS B ND1 1 
ATOM   5485 C  CD2 . HIS B 1 285 ? 123.955 -15.496 68.163  1.00 20.27 ? 287  HIS B CD2 1 
ATOM   5486 C  CE1 . HIS B 1 285 ? 124.057 -13.750 66.840  1.00 20.35 ? 287  HIS B CE1 1 
ATOM   5487 N  NE2 . HIS B 1 285 ? 123.408 -14.878 67.065  1.00 20.63 ? 287  HIS B NE2 1 
ATOM   5488 N  N   . ALA B 1 286 ? 129.157 -14.985 70.628  1.00 23.30 ? 288  ALA B N   1 
ATOM   5489 C  CA  . ALA B 1 286 ? 129.978 -14.826 71.824  1.00 27.42 ? 288  ALA B CA  1 
ATOM   5490 C  C   . ALA B 1 286 ? 129.314 -13.855 72.796  1.00 29.28 ? 288  ALA B C   1 
ATOM   5491 O  O   . ALA B 1 286 ? 128.885 -12.773 72.400  1.00 33.56 ? 288  ALA B O   1 
ATOM   5492 C  CB  . ALA B 1 286 ? 131.360 -14.321 71.442  1.00 25.31 ? 288  ALA B CB  1 
ATOM   5493 N  N   . GLY B 1 287 ? 129.181 -14.258 74.054  1.00 33.80 ? 289  GLY B N   1 
ATOM   5494 C  CA  . GLY B 1 287 ? 129.236 -15.659 74.440  1.00 30.06 ? 289  GLY B CA  1 
ATOM   5495 C  C   . GLY B 1 287 ? 127.883 -16.107 74.956  1.00 30.69 ? 289  GLY B C   1 
ATOM   5496 O  O   . GLY B 1 287 ? 127.508 -15.810 76.093  1.00 32.00 ? 289  GLY B O   1 
ATOM   5497 N  N   . PHE B 1 288 ? 127.120 -16.761 74.088  1.00 27.45 ? 290  PHE B N   1 
ATOM   5498 C  CA  . PHE B 1 288 ? 125.871 -17.401 74.478  1.00 26.39 ? 290  PHE B CA  1 
ATOM   5499 C  C   . PHE B 1 288 ? 125.995 -18.907 74.294  1.00 26.05 ? 290  PHE B C   1 
ATOM   5500 O  O   . PHE B 1 288 ? 126.791 -19.376 73.482  1.00 27.49 ? 290  PHE B O   1 
ATOM   5501 C  CB  . PHE B 1 288 ? 124.711 -16.880 73.622  1.00 26.24 ? 290  PHE B CB  1 
ATOM   5502 C  CG  . PHE B 1 288 ? 124.401 -15.425 73.830  1.00 24.72 ? 290  PHE B CG  1 
ATOM   5503 C  CD1 . PHE B 1 288 ? 125.243 -14.444 73.334  1.00 23.61 ? 290  PHE B CD1 1 
ATOM   5504 C  CD2 . PHE B 1 288 ? 123.233 -15.039 74.466  1.00 23.28 ? 290  PHE B CD2 1 
ATOM   5505 C  CE1 . PHE B 1 288 ? 124.944 -13.106 73.501  1.00 24.85 ? 290  PHE B CE1 1 
ATOM   5506 C  CE2 . PHE B 1 288 ? 122.929 -13.701 74.637  1.00 23.69 ? 290  PHE B CE2 1 
ATOM   5507 C  CZ  . PHE B 1 288 ? 123.781 -12.733 74.147  1.00 22.69 ? 290  PHE B CZ  1 
ATOM   5508 N  N   . ASP B 1 289 ? 125.189 -19.659 75.037  1.00 26.75 ? 291  ASP B N   1 
ATOM   5509 C  CA  . ASP B 1 289 ? 125.105 -21.107 74.869  1.00 27.42 ? 291  ASP B CA  1 
ATOM   5510 C  C   . ASP B 1 289 ? 124.233 -21.465 73.664  1.00 26.48 ? 291  ASP B C   1 
ATOM   5511 O  O   . ASP B 1 289 ? 123.003 -21.480 73.757  1.00 25.65 ? 291  ASP B O   1 
ATOM   5512 C  CB  . ASP B 1 289 ? 124.546 -21.751 76.141  1.00 28.53 ? 291  ASP B CB  1 
ATOM   5513 C  CG  . ASP B 1 289 ? 124.352 -23.251 76.006  1.00 32.68 ? 291  ASP B CG  1 
ATOM   5514 O  OD1 . ASP B 1 289 ? 124.736 -23.819 74.963  1.00 35.41 ? 291  ASP B OD1 1 
ATOM   5515 O  OD2 . ASP B 1 289 ? 123.807 -23.866 76.948  1.00 37.18 ? 291  ASP B OD2 1 
ATOM   5516 N  N   . LEU B 1 290 ? 124.878 -21.766 72.540  1.00 24.44 ? 292  LEU B N   1 
ATOM   5517 C  CA  . LEU B 1 290 ? 124.168 -22.093 71.304  1.00 23.55 ? 292  LEU B CA  1 
ATOM   5518 C  C   . LEU B 1 290 ? 122.993 -23.029 71.553  1.00 23.36 ? 292  LEU B C   1 
ATOM   5519 O  O   . LEU B 1 290 ? 121.974 -22.956 70.866  1.00 24.53 ? 292  LEU B O   1 
ATOM   5520 C  CB  . LEU B 1 290 ? 125.121 -22.718 70.280  1.00 23.19 ? 292  LEU B CB  1 
ATOM   5521 C  CG  . LEU B 1 290 ? 124.514 -23.022 68.907  1.00 21.77 ? 292  LEU B CG  1 
ATOM   5522 C  CD1 . LEU B 1 290 ? 124.230 -21.734 68.155  1.00 20.06 ? 292  LEU B CD1 1 
ATOM   5523 C  CD2 . LEU B 1 290 ? 125.427 -23.929 68.094  1.00 23.08 ? 292  LEU B CD2 1 
ATOM   5524 N  N   . GLY B 1 291 ? 123.135 -23.903 72.545  1.00 21.97 ? 293  GLY B N   1 
ATOM   5525 C  CA  . GLY B 1 291 ? 122.147 -24.942 72.800  1.00 22.09 ? 293  GLY B CA  1 
ATOM   5526 C  C   . GLY B 1 291 ? 120.910 -24.465 73.537  1.00 21.21 ? 293  GLY B C   1 
ATOM   5527 O  O   . GLY B 1 291 ? 119.881 -25.138 73.532  1.00 21.26 ? 293  GLY B O   1 
ATOM   5528 N  N   A SER B 1 292 ? 121.005 -23.293 74.157  0.50 22.55 ? 294  SER B N   1 
ATOM   5529 N  N   B SER B 1 292 ? 121.014 -23.306 74.180  0.50 22.43 ? 294  SER B N   1 
ATOM   5530 C  CA  A SER B 1 292 ? 119.956 -22.815 75.052  0.50 23.43 ? 294  SER B CA  1 
ATOM   5531 C  CA  B SER B 1 292 ? 119.952 -22.811 75.052  0.50 23.25 ? 294  SER B CA  1 
ATOM   5532 C  C   A SER B 1 292 ? 119.446 -21.435 74.650  0.50 23.32 ? 294  SER B C   1 
ATOM   5533 C  C   B SER B 1 292 ? 119.415 -21.462 74.586  0.50 23.13 ? 294  SER B C   1 
ATOM   5534 O  O   A SER B 1 292 ? 118.345 -21.036 75.032  0.50 23.99 ? 294  SER B O   1 
ATOM   5535 O  O   B SER B 1 292 ? 118.269 -21.110 74.867  0.50 23.89 ? 294  SER B O   1 
ATOM   5536 C  CB  A SER B 1 292 ? 120.460 -22.781 76.497  0.50 23.40 ? 294  SER B CB  1 
ATOM   5537 C  CB  B SER B 1 292 ? 120.450 -22.695 76.495  0.50 23.09 ? 294  SER B CB  1 
ATOM   5538 O  OG  A SER B 1 292 ? 121.569 -21.909 76.627  0.50 23.76 ? 294  SER B OG  1 
ATOM   5539 O  OG  B SER B 1 292 ? 120.297 -23.918 77.192  0.50 23.19 ? 294  SER B OG  1 
ATOM   5540 N  N   . ASP B 1 293 ? 120.257 -20.701 73.896  1.00 22.53 ? 295  ASP B N   1 
ATOM   5541 C  CA  . ASP B 1 293 ? 119.950 -19.314 73.575  1.00 22.60 ? 295  ASP B CA  1 
ATOM   5542 C  C   . ASP B 1 293 ? 119.022 -19.175 72.369  1.00 22.53 ? 295  ASP B C   1 
ATOM   5543 O  O   . ASP B 1 293 ? 119.424 -19.417 71.231  1.00 21.67 ? 295  ASP B O   1 
ATOM   5544 C  CB  . ASP B 1 293 ? 121.234 -18.524 73.338  1.00 22.28 ? 295  ASP B CB  1 
ATOM   5545 C  CG  . ASP B 1 293 ? 120.967 -17.125 72.829  1.00 23.10 ? 295  ASP B CG  1 
ATOM   5546 O  OD1 . ASP B 1 293 ? 120.099 -16.438 73.408  1.00 24.85 ? 295  ASP B OD1 1 
ATOM   5547 O  OD2 . ASP B 1 293 ? 121.611 -16.719 71.838  1.00 23.93 ? 295  ASP B OD2 1 
ATOM   5548 N  N   . GLN B 1 294 ? 117.792 -18.742 72.624  1.00 21.49 ? 296  GLN B N   1 
ATOM   5549 C  CA  . GLN B 1 294 ? 116.858 -18.416 71.555  1.00 21.80 ? 296  GLN B CA  1 
ATOM   5550 C  C   . GLN B 1 294 ? 116.540 -16.925 71.534  1.00 22.20 ? 296  GLN B C   1 
ATOM   5551 O  O   . GLN B 1 294 ? 115.548 -16.501 70.941  1.00 23.05 ? 296  GLN B O   1 
ATOM   5552 C  CB  . GLN B 1 294 ? 115.575 -19.233 71.705  1.00 21.52 ? 296  GLN B CB  1 
ATOM   5553 C  CG  . GLN B 1 294 ? 115.817 -20.732 71.695  1.00 21.47 ? 296  GLN B CG  1 
ATOM   5554 C  CD  . GLN B 1 294 ? 114.537 -21.538 71.652  1.00 22.68 ? 296  GLN B CD  1 
ATOM   5555 O  OE1 . GLN B 1 294 ? 113.867 -21.607 70.620  1.00 23.24 ? 296  GLN B OE1 1 
ATOM   5556 N  NE2 . GLN B 1 294 ? 114.216 -22.196 72.760  1.00 22.55 ? 296  GLN B NE2 1 
ATOM   5557 N  N   . SER B 1 295 ? 117.394 -16.130 72.172  1.00 22.26 ? 297  SER B N   1 
ATOM   5558 C  CA  . SER B 1 295 ? 117.156 -14.695 72.281  1.00 23.10 ? 297  SER B CA  1 
ATOM   5559 C  C   . SER B 1 295 ? 117.444 -13.968 70.970  1.00 22.65 ? 297  SER B C   1 
ATOM   5560 O  O   . SER B 1 295 ? 116.875 -12.911 70.701  1.00 21.92 ? 297  SER B O   1 
ATOM   5561 C  CB  . SER B 1 295 ? 117.971 -14.089 73.428  1.00 22.74 ? 297  SER B CB  1 
ATOM   5562 O  OG  . SER B 1 295 ? 119.277 -13.740 73.005  1.00 22.94 ? 297  SER B OG  1 
ATOM   5563 N  N   . HIS B 1 296 ? 118.322 -14.540 70.152  1.00 21.68 ? 298  HIS B N   1 
ATOM   5564 C  CA  . HIS B 1 296 ? 118.622 -13.973 68.842  1.00 20.87 ? 298  HIS B CA  1 
ATOM   5565 C  C   . HIS B 1 296 ? 117.663 -14.512 67.780  1.00 19.94 ? 298  HIS B C   1 
ATOM   5566 O  O   . HIS B 1 296 ? 117.090 -13.751 67.005  1.00 20.32 ? 298  HIS B O   1 
ATOM   5567 C  CB  . HIS B 1 296 ? 120.068 -14.270 68.439  1.00 21.95 ? 298  HIS B CB  1 
ATOM   5568 C  CG  . HIS B 1 296 ? 121.088 -13.716 69.386  1.00 23.52 ? 298  HIS B CG  1 
ATOM   5569 N  ND1 . HIS B 1 296 ? 121.421 -14.339 70.570  1.00 22.65 ? 298  HIS B ND1 1 
ATOM   5570 C  CD2 . HIS B 1 296 ? 121.871 -12.614 69.308  1.00 22.54 ? 298  HIS B CD2 1 
ATOM   5571 C  CE1 . HIS B 1 296 ? 122.352 -13.635 71.188  1.00 22.18 ? 298  HIS B CE1 1 
ATOM   5572 N  NE2 . HIS B 1 296 ? 122.641 -12.583 70.446  1.00 22.31 ? 298  HIS B NE2 1 
ATOM   5573 N  N   . CYS B 1 297 ? 117.505 -15.829 67.743  1.00 19.18 ? 299  CYS B N   1 
ATOM   5574 C  CA  . CYS B 1 297 ? 116.589 -16.470 66.800  1.00 19.86 ? 299  CYS B CA  1 
ATOM   5575 C  C   . CYS B 1 297 ? 116.040 -17.747 67.416  1.00 19.12 ? 299  CYS B C   1 
ATOM   5576 O  O   . CYS B 1 297 ? 116.800 -18.549 67.960  1.00 20.64 ? 299  CYS B O   1 
ATOM   5577 C  CB  . CYS B 1 297 ? 117.307 -16.781 65.482  1.00 18.27 ? 299  CYS B CB  1 
ATOM   5578 S  SG  . CYS B 1 297 ? 116.277 -17.563 64.212  1.00 18.21 ? 299  CYS B SG  1 
ATOM   5579 N  N   . PRO B 1 298 ? 114.710 -17.922 67.377  1.00 17.93 ? 300  PRO B N   1 
ATOM   5580 C  CA  . PRO B 1 298 ? 114.113 -19.150 67.887  1.00 17.79 ? 300  PRO B CA  1 
ATOM   5581 C  C   . PRO B 1 298 ? 114.679 -20.371 67.171  1.00 17.94 ? 300  PRO B C   1 
ATOM   5582 O  O   . PRO B 1 298 ? 115.021 -20.293 65.990  1.00 18.62 ? 300  PRO B O   1 
ATOM   5583 C  CB  . PRO B 1 298 ? 112.628 -18.987 67.546  1.00 18.28 ? 300  PRO B CB  1 
ATOM   5584 C  CG  . PRO B 1 298 ? 112.418 -17.515 67.452  1.00 18.09 ? 300  PRO B CG  1 
ATOM   5585 C  CD  . PRO B 1 298 ? 113.698 -16.966 66.896  1.00 17.76 ? 300  PRO B CD  1 
ATOM   5586 N  N   . PHE B 1 299 ? 114.758 -21.495 67.876  1.00 16.68 ? 301  PHE B N   1 
ATOM   5587 C  CA  . PHE B 1 299 ? 115.193 -22.742 67.260  1.00 16.35 ? 301  PHE B CA  1 
ATOM   5588 C  C   . PHE B 1 299 ? 114.181 -23.203 66.217  1.00 16.16 ? 301  PHE B C   1 
ATOM   5589 O  O   . PHE B 1 299 ? 114.500 -24.006 65.336  1.00 15.45 ? 301  PHE B O   1 
ATOM   5590 C  CB  . PHE B 1 299 ? 115.380 -23.825 68.321  1.00 16.71 ? 301  PHE B CB  1 
ATOM   5591 C  CG  . PHE B 1 299 ? 116.428 -23.495 69.344  1.00 16.84 ? 301  PHE B CG  1 
ATOM   5592 C  CD1 . PHE B 1 299 ? 117.536 -22.740 68.999  1.00 16.85 ? 301  PHE B CD1 1 
ATOM   5593 C  CD2 . PHE B 1 299 ? 116.311 -23.951 70.648  1.00 18.27 ? 301  PHE B CD2 1 
ATOM   5594 C  CE1 . PHE B 1 299 ? 118.506 -22.437 69.938  1.00 18.14 ? 301  PHE B CE1 1 
ATOM   5595 C  CE2 . PHE B 1 299 ? 117.279 -23.653 71.591  1.00 18.47 ? 301  PHE B CE2 1 
ATOM   5596 C  CZ  . PHE B 1 299 ? 118.372 -22.888 71.237  1.00 17.88 ? 301  PHE B CZ  1 
ATOM   5597 N  N   . SER B 1 300 ? 112.965 -22.676 66.321  1.00 15.83 ? 302  SER B N   1 
ATOM   5598 C  CA  . SER B 1 300 ? 111.837 -23.160 65.533  1.00 15.01 ? 302  SER B CA  1 
ATOM   5599 C  C   . SER B 1 300 ? 111.575 -22.290 64.305  1.00 14.22 ? 302  SER B C   1 
ATOM   5600 O  O   . SER B 1 300 ? 110.682 -22.588 63.513  1.00 13.54 ? 302  SER B O   1 
ATOM   5601 C  CB  . SER B 1 300 ? 110.577 -23.219 66.399  1.00 15.02 ? 302  SER B CB  1 
ATOM   5602 O  OG  . SER B 1 300 ? 110.378 -21.989 67.074  1.00 15.89 ? 302  SER B OG  1 
ATOM   5603 N  N   . ALA B 1 301 ? 112.334 -21.207 64.165  1.00 13.21 ? 303  ALA B N   1 
ATOM   5604 C  CA  . ALA B 1 301 ? 112.159 -20.282 63.046  1.00 13.74 ? 303  ALA B CA  1 
ATOM   5605 C  C   . ALA B 1 301 ? 112.379 -20.971 61.698  1.00 13.27 ? 303  ALA B C   1 
ATOM   5606 O  O   . ALA B 1 301 ? 113.254 -21.826 61.575  1.00 12.45 ? 303  ALA B O   1 
ATOM   5607 C  CB  . ALA B 1 301 ? 113.097 -19.091 63.193  1.00 13.55 ? 303  ALA B CB  1 
ATOM   5608 N  N   . HIS B 1 302 ? 111.602 -20.568 60.690  1.00 12.72 ? 304  HIS B N   1 
ATOM   5609 C  CA  . HIS B 1 302 ? 111.627 -21.199 59.360  1.00 12.12 ? 304  HIS B CA  1 
ATOM   5610 C  C   . HIS B 1 302 ? 113.048 -21.408 58.842  1.00 11.54 ? 304  HIS B C   1 
ATOM   5611 O  O   . HIS B 1 302 ? 113.444 -22.538 58.555  1.00 11.61 ? 304  HIS B O   1 
ATOM   5612 C  CB  . HIS B 1 302 ? 110.782 -20.390 58.352  1.00 12.23 ? 304  HIS B CB  1 
ATOM   5613 C  CG  . HIS B 1 302 ? 110.810 -20.916 56.940  1.00 11.87 ? 304  HIS B CG  1 
ATOM   5614 N  ND1 . HIS B 1 302 ? 110.411 -22.193 56.608  1.00 12.05 ? 304  HIS B ND1 1 
ATOM   5615 C  CD2 . HIS B 1 302 ? 111.055 -20.286 55.763  1.00 12.28 ? 304  HIS B CD2 1 
ATOM   5616 C  CE1 . HIS B 1 302 ? 110.467 -22.346 55.294  1.00 11.73 ? 304  HIS B CE1 1 
ATOM   5617 N  NE2 . HIS B 1 302 ? 110.855 -21.202 54.755  1.00 11.88 ? 304  HIS B NE2 1 
ATOM   5618 N  N   . ILE B 1 303 ? 113.815 -20.330 58.704  1.00 11.49 ? 305  ILE B N   1 
ATOM   5619 C  CA  . ILE B 1 303 ? 115.116 -20.449 58.048  1.00 11.52 ? 305  ILE B CA  1 
ATOM   5620 C  C   . ILE B 1 303 ? 116.088 -21.300 58.857  1.00 11.88 ? 305  ILE B C   1 
ATOM   5621 O  O   . ILE B 1 303 ? 116.958 -21.962 58.299  1.00 11.65 ? 305  ILE B O   1 
ATOM   5622 C  CB  . ILE B 1 303 ? 115.756 -19.088 57.715  1.00 11.60 ? 305  ILE B CB  1 
ATOM   5623 C  CG1 . ILE B 1 303 ? 115.959 -18.251 58.979  1.00 11.59 ? 305  ILE B CG1 1 
ATOM   5624 C  CG2 . ILE B 1 303 ? 114.933 -18.341 56.674  1.00 11.68 ? 305  ILE B CG2 1 
ATOM   5625 C  CD1 . ILE B 1 303 ? 116.973 -17.144 58.795  1.00 11.73 ? 305  ILE B CD1 1 
ATOM   5626 N  N   . ARG B 1 304 ? 115.931 -21.291 60.177  1.00 12.01 ? 306  ARG B N   1 
ATOM   5627 C  CA  . ARG B 1 304 ? 116.810 -22.066 61.044  1.00 12.97 ? 306  ARG B CA  1 
ATOM   5628 C  C   . ARG B 1 304 ? 116.432 -23.538 60.989  1.00 12.93 ? 306  ARG B C   1 
ATOM   5629 O  O   . ARG B 1 304 ? 117.287 -24.417 61.109  1.00 14.36 ? 306  ARG B O   1 
ATOM   5630 C  CB  . ARG B 1 304 ? 116.732 -21.551 62.484  1.00 13.62 ? 306  ARG B CB  1 
ATOM   5631 C  CG  . ARG B 1 304 ? 117.782 -22.144 63.411  1.00 14.19 ? 306  ARG B CG  1 
ATOM   5632 C  CD  . ARG B 1 304 ? 117.844 -21.389 64.728  1.00 16.50 ? 306  ARG B CD  1 
ATOM   5633 N  NE  . ARG B 1 304 ? 118.956 -21.846 65.558  1.00 17.56 ? 306  ARG B NE  1 
ATOM   5634 C  CZ  . ARG B 1 304 ? 119.545 -21.106 66.489  1.00 17.77 ? 306  ARG B CZ  1 
ATOM   5635 N  NH1 . ARG B 1 304 ? 119.123 -19.870 66.719  1.00 18.89 ? 306  ARG B NH1 1 
ATOM   5636 N  NH2 . ARG B 1 304 ? 120.557 -21.601 67.189  1.00 18.65 ? 306  ARG B NH2 1 
ATOM   5637 N  N   . LYS B 1 305 ? 115.141 -23.803 60.812  1.00 12.78 ? 307  LYS B N   1 
ATOM   5638 C  CA  . LYS B 1 305 ? 114.661 -25.161 60.601  1.00 12.68 ? 307  LYS B CA  1 
ATOM   5639 C  C   . LYS B 1 305 ? 115.146 -25.726 59.271  1.00 12.62 ? 307  LYS B C   1 
ATOM   5640 O  O   . LYS B 1 305 ? 115.426 -26.918 59.168  1.00 13.85 ? 307  LYS B O   1 
ATOM   5641 C  CB  . LYS B 1 305 ? 113.132 -25.210 60.660  1.00 12.58 ? 307  LYS B CB  1 
ATOM   5642 C  CG  . LYS B 1 305 ? 112.568 -25.253 62.072  1.00 13.07 ? 307  LYS B CG  1 
ATOM   5643 C  CD  . LYS B 1 305 ? 112.562 -26.673 62.612  1.00 14.20 ? 307  LYS B CD  1 
ATOM   5644 C  CE  . LYS B 1 305 ? 111.470 -26.863 63.649  1.00 14.78 ? 307  LYS B CE  1 
ATOM   5645 N  NZ  . LYS B 1 305 ? 111.335 -28.290 64.055  1.00 14.47 ? 307  LYS B NZ  1 
ATOM   5646 N  N   . THR B 1 306 ? 115.240 -24.871 58.256  1.00 12.00 ? 308  THR B N   1 
ATOM   5647 C  CA  . THR B 1 306 ? 115.498 -25.340 56.896  1.00 12.08 ? 308  THR B CA  1 
ATOM   5648 C  C   . THR B 1 306 ? 116.965 -25.231 56.472  1.00 12.48 ? 308  THR B C   1 
ATOM   5649 O  O   . THR B 1 306 ? 117.400 -25.934 55.560  1.00 12.48 ? 308  THR B O   1 
ATOM   5650 C  CB  . THR B 1 306 ? 114.600 -24.638 55.859  1.00 11.89 ? 308  THR B CB  1 
ATOM   5651 O  OG1 . THR B 1 306 ? 114.740 -23.219 55.981  1.00 11.42 ? 308  THR B OG1 1 
ATOM   5652 C  CG2 . THR B 1 306 ? 113.135 -25.027 56.063  1.00 11.77 ? 308  THR B CG2 1 
ATOM   5653 N  N   . ARG B 1 307 ? 117.706 -24.316 57.092  1.00 11.91 ? 309  ARG B N   1 
ATOM   5654 C  CA  . ARG B 1 307 ? 119.167 -24.382 57.084  1.00 11.90 ? 309  ARG B CA  1 
ATOM   5655 C  C   . ARG B 1 307 ? 119.734 -24.118 58.474  1.00 12.01 ? 309  ARG B C   1 
ATOM   5656 O  O   . ARG B 1 307 ? 119.910 -22.967 58.870  1.00 11.28 ? 309  ARG B O   1 
ATOM   5657 C  CB  . ARG B 1 307 ? 119.783 -23.409 56.075  1.00 11.78 ? 309  ARG B CB  1 
ATOM   5658 C  CG  . ARG B 1 307 ? 121.271 -23.658 55.865  1.00 12.49 ? 309  ARG B CG  1 
ATOM   5659 C  CD  . ARG B 1 307 ? 122.006 -22.475 55.254  1.00 12.64 ? 309  ARG B CD  1 
ATOM   5660 N  NE  . ARG B 1 307 ? 123.435 -22.557 55.542  1.00 12.81 ? 309  ARG B NE  1 
ATOM   5661 C  CZ  . ARG B 1 307 ? 124.300 -21.560 55.382  1.00 12.93 ? 309  ARG B CZ  1 
ATOM   5662 N  NH1 . ARG B 1 307 ? 123.900 -20.393 54.897  1.00 13.06 ? 309  ARG B NH1 1 
ATOM   5663 N  NH2 . ARG B 1 307 ? 125.575 -21.737 55.700  1.00 13.40 ? 309  ARG B NH2 1 
ATOM   5664 N  N   . PRO B 1 308 ? 120.023 -25.195 59.214  1.00 12.54 ? 310  PRO B N   1 
ATOM   5665 C  CA  . PRO B 1 308 ? 120.373 -25.148 60.636  1.00 12.83 ? 310  PRO B CA  1 
ATOM   5666 C  C   . PRO B 1 308 ? 121.700 -24.439 60.919  1.00 13.52 ? 310  PRO B C   1 
ATOM   5667 O  O   . PRO B 1 308 ? 121.919 -23.957 62.034  1.00 15.31 ? 310  PRO B O   1 
ATOM   5668 C  CB  . PRO B 1 308 ? 120.471 -26.626 61.015  1.00 12.83 ? 310  PRO B CB  1 
ATOM   5669 C  CG  . PRO B 1 308 ? 119.590 -27.323 60.033  1.00 13.76 ? 310  PRO B CG  1 
ATOM   5670 C  CD  . PRO B 1 308 ? 119.791 -26.573 58.751  1.00 12.18 ? 310  PRO B CD  1 
ATOM   5671 N  N   . ARG B 1 309 ? 122.578 -24.381 59.924  1.00 13.31 ? 311  ARG B N   1 
ATOM   5672 C  CA  . ARG B 1 309 ? 123.910 -23.818 60.111  1.00 13.63 ? 311  ARG B CA  1 
ATOM   5673 C  C   . ARG B 1 309 ? 124.612 -24.444 61.323  1.00 14.76 ? 311  ARG B C   1 
ATOM   5674 O  O   . ARG B 1 309 ? 124.769 -25.664 61.388  1.00 14.23 ? 311  ARG B O   1 
ATOM   5675 C  CB  . ARG B 1 309 ? 123.842 -22.288 60.203  1.00 13.23 ? 311  ARG B CB  1 
ATOM   5676 C  CG  . ARG B 1 309 ? 123.047 -21.680 59.053  1.00 14.08 ? 311  ARG B CG  1 
ATOM   5677 C  CD  . ARG B 1 309 ? 123.127 -20.162 58.977  1.00 14.09 ? 311  ARG B CD  1 
ATOM   5678 N  NE  . ARG B 1 309 ? 122.136 -19.648 58.032  1.00 13.98 ? 311  ARG B NE  1 
ATOM   5679 C  CZ  . ARG B 1 309 ? 122.321 -18.611 57.220  1.00 13.97 ? 311  ARG B CZ  1 
ATOM   5680 N  NH1 . ARG B 1 309 ? 123.461 -17.931 57.242  1.00 13.92 ? 311  ARG B NH1 1 
ATOM   5681 N  NH2 . ARG B 1 309 ? 121.360 -18.258 56.372  1.00 14.40 ? 311  ARG B NH2 1 
ATOM   5682 N  N   . ALA B 1 310 ? 125.012 -23.623 62.288  1.00 15.28 ? 312  ALA B N   1 
ATOM   5683 C  CA  . ALA B 1 310 ? 125.855 -24.107 63.383  1.00 15.73 ? 312  ALA B CA  1 
ATOM   5684 C  C   . ALA B 1 310 ? 125.121 -25.058 64.327  1.00 16.53 ? 312  ALA B C   1 
ATOM   5685 O  O   . ALA B 1 310 ? 125.751 -25.753 65.124  1.00 16.85 ? 312  ALA B O   1 
ATOM   5686 C  CB  . ALA B 1 310 ? 126.468 -22.945 64.151  1.00 16.29 ? 312  ALA B CB  1 
ATOM   5687 N  N   . ASP B 1 311 ? 123.799 -25.136 64.189  1.00 16.17 ? 313  ASP B N   1 
ATOM   5688 C  CA  . ASP B 1 311 ? 123.008 -26.116 64.932  1.00 16.47 ? 313  ASP B CA  1 
ATOM   5689 C  C   . ASP B 1 311 ? 123.406 -27.549 64.579  1.00 15.94 ? 313  ASP B C   1 
ATOM   5690 O  O   . ASP B 1 311 ? 123.178 -28.473 65.355  1.00 16.21 ? 313  ASP B O   1 
ATOM   5691 C  CB  . ASP B 1 311 ? 121.510 -25.919 64.676  1.00 17.88 ? 313  ASP B CB  1 
ATOM   5692 C  CG  . ASP B 1 311 ? 120.913 -24.798 65.506  1.00 19.05 ? 313  ASP B CG  1 
ATOM   5693 O  OD1 . ASP B 1 311 ? 121.632 -24.233 66.357  1.00 18.00 ? 313  ASP B OD1 1 
ATOM   5694 O  OD2 . ASP B 1 311 ? 119.729 -24.462 65.283  1.00 20.08 ? 313  ASP B OD2 1 
ATOM   5695 N  N   . LEU B 1 312 ? 124.001 -27.728 63.405  1.00 14.90 ? 314  LEU B N   1 
ATOM   5696 C  CA  . LEU B 1 312 ? 124.437 -29.049 62.971  1.00 14.19 ? 314  LEU B CA  1 
ATOM   5697 C  C   . LEU B 1 312 ? 125.959 -29.145 62.890  1.00 15.23 ? 314  LEU B C   1 
ATOM   5698 O  O   . LEU B 1 312 ? 126.497 -29.969 62.147  1.00 14.08 ? 314  LEU B O   1 
ATOM   5699 C  CB  . LEU B 1 312 ? 123.818 -29.396 61.614  1.00 14.05 ? 314  LEU B CB  1 
ATOM   5700 C  CG  . LEU B 1 312 ? 122.340 -29.782 61.634  1.00 13.36 ? 314  LEU B CG  1 
ATOM   5701 C  CD1 . LEU B 1 312 ? 121.870 -30.182 60.245  1.00 13.27 ? 314  LEU B CD1 1 
ATOM   5702 C  CD2 . LEU B 1 312 ? 122.104 -30.905 62.627  1.00 13.81 ? 314  LEU B CD2 1 
ATOM   5703 N  N   . GLY B 1 313 ? 126.646 -28.290 63.642  1.00 14.28 ? 315  GLY B N   1 
ATOM   5704 C  CA  . GLY B 1 313 ? 128.101 -28.335 63.727  1.00 16.07 ? 315  GLY B CA  1 
ATOM   5705 C  C   . GLY B 1 313 ? 128.786 -27.427 62.724  1.00 17.01 ? 315  GLY B C   1 
ATOM   5706 O  O   . GLY B 1 313 ? 128.148 -26.573 62.109  1.00 15.64 ? 315  GLY B O   1 
ATOM   5707 N  N   . GLY B 1 314 ? 130.095 -27.608 62.569  1.00 17.98 ? 316  GLY B N   1 
ATOM   5708 C  CA  . GLY B 1 314 ? 130.876 -26.797 61.644  1.00 17.45 ? 316  GLY B CA  1 
ATOM   5709 C  C   . GLY B 1 314 ? 131.292 -25.466 62.241  1.00 18.86 ? 316  GLY B C   1 
ATOM   5710 O  O   . GLY B 1 314 ? 131.258 -25.284 63.456  1.00 19.42 ? 316  GLY B O   1 
ATOM   5711 N  N   . SER B 1 315 ? 131.681 -24.529 61.381  1.00 18.28 ? 317  SER B N   1 
ATOM   5712 C  CA  . SER B 1 315 ? 132.280 -23.278 61.834  1.00 20.17 ? 317  SER B CA  1 
ATOM   5713 C  C   . SER B 1 315 ? 131.290 -22.398 62.595  1.00 21.27 ? 317  SER B C   1 
ATOM   5714 O  O   . SER B 1 315 ? 130.172 -22.156 62.133  1.00 19.87 ? 317  SER B O   1 
ATOM   5715 C  CB  . SER B 1 315 ? 132.869 -22.506 60.656  1.00 20.11 ? 317  SER B CB  1 
ATOM   5716 O  OG  . SER B 1 315 ? 133.432 -21.278 61.088  1.00 22.01 ? 317  SER B OG  1 
ATOM   5717 N  N   . LEU B 1 316 ? 131.714 -21.917 63.760  1.00 20.07 ? 318  LEU B N   1 
ATOM   5718 C  CA  . LEU B 1 316 ? 130.921 -20.978 64.547  1.00 19.92 ? 318  LEU B CA  1 
ATOM   5719 C  C   . LEU B 1 316 ? 130.986 -19.577 63.949  1.00 19.93 ? 318  LEU B C   1 
ATOM   5720 O  O   . LEU B 1 316 ? 130.116 -18.744 64.201  1.00 20.08 ? 318  LEU B O   1 
ATOM   5721 C  CB  . LEU B 1 316 ? 131.422 -20.939 65.992  1.00 20.10 ? 318  LEU B CB  1 
ATOM   5722 C  CG  . LEU B 1 316 ? 131.287 -22.230 66.799  1.00 19.78 ? 318  LEU B CG  1 
ATOM   5723 C  CD1 . LEU B 1 316 ? 131.605 -21.972 68.263  1.00 18.53 ? 318  LEU B CD1 1 
ATOM   5724 C  CD2 . LEU B 1 316 ? 129.890 -22.812 66.641  1.00 20.04 ? 318  LEU B CD2 1 
ATOM   5725 N  N   . THR B 1 317 ? 132.052 -19.313 63.200  1.00 18.64 ? 319  THR B N   1 
ATOM   5726 C  CA  . THR B 1 317 ? 132.191 -18.068 62.455  1.00 19.37 ? 319  THR B CA  1 
ATOM   5727 C  C   . THR B 1 317 ? 131.859 -18.299 60.981  1.00 18.88 ? 319  THR B C   1 
ATOM   5728 O  O   . THR B 1 317 ? 132.070 -19.391 60.458  1.00 18.36 ? 319  THR B O   1 
ATOM   5729 C  CB  . THR B 1 317 ? 133.628 -17.523 62.545  1.00 19.65 ? 319  THR B CB  1 
ATOM   5730 O  OG1 . THR B 1 317 ? 134.544 -18.526 62.095  1.00 19.60 ? 319  THR B OG1 1 
ATOM   5731 C  CG2 . THR B 1 317 ? 133.970 -17.133 63.977  1.00 20.87 ? 319  THR B CG2 1 
ATOM   5732 N  N   . PRO B 1 318 ? 131.331 -17.268 60.309  1.00 19.14 ? 320  PRO B N   1 
ATOM   5733 C  CA  . PRO B 1 318 ? 130.956 -17.381 58.900  1.00 18.78 ? 320  PRO B CA  1 
ATOM   5734 C  C   . PRO B 1 318 ? 132.155 -17.724 58.016  1.00 18.59 ? 320  PRO B C   1 
ATOM   5735 O  O   . PRO B 1 318 ? 133.248 -17.203 58.235  1.00 18.88 ? 320  PRO B O   1 
ATOM   5736 C  CB  . PRO B 1 318 ? 130.443 -15.979 58.567  1.00 19.18 ? 320  PRO B CB  1 
ATOM   5737 C  CG  . PRO B 1 318 ? 129.936 -15.451 59.865  1.00 19.82 ? 320  PRO B CG  1 
ATOM   5738 C  CD  . PRO B 1 318 ? 130.836 -16.022 60.922  1.00 19.23 ? 320  PRO B CD  1 
ATOM   5739 N  N   . PRO B 1 319 ? 131.953 -18.592 57.028  1.00 17.92 ? 321  PRO B N   1 
ATOM   5740 C  CA  . PRO B 1 319 ? 130.657 -19.217 56.790  1.00 17.06 ? 321  PRO B CA  1 
ATOM   5741 C  C   . PRO B 1 319 ? 130.568 -20.578 57.461  1.00 16.93 ? 321  PRO B C   1 
ATOM   5742 O  O   . PRO B 1 319 ? 131.546 -21.326 57.478  1.00 17.52 ? 321  PRO B O   1 
ATOM   5743 C  CB  . PRO B 1 319 ? 130.635 -19.396 55.272  1.00 16.82 ? 321  PRO B CB  1 
ATOM   5744 C  CG  . PRO B 1 319 ? 132.069 -19.564 54.905  1.00 18.14 ? 321  PRO B CG  1 
ATOM   5745 C  CD  . PRO B 1 319 ? 132.828 -18.663 55.844  1.00 18.17 ? 321  PRO B CD  1 
ATOM   5746 N  N   . ASN B 1 320 ? 129.399 -20.901 58.001  1.00 15.89 ? 322  ASN B N   1 
ATOM   5747 C  CA  . ASN B 1 320 ? 129.115 -22.268 58.408  1.00 16.30 ? 322  ASN B CA  1 
ATOM   5748 C  C   . ASN B 1 320 ? 128.800 -23.130 57.190  1.00 16.19 ? 322  ASN B C   1 
ATOM   5749 O  O   . ASN B 1 320 ? 128.092 -22.696 56.280  1.00 15.80 ? 322  ASN B O   1 
ATOM   5750 C  CB  . ASN B 1 320 ? 127.956 -22.300 59.403  1.00 16.02 ? 322  ASN B CB  1 
ATOM   5751 C  CG  . ASN B 1 320 ? 127.620 -23.703 59.860  1.00 16.62 ? 322  ASN B CG  1 
ATOM   5752 O  OD1 . ASN B 1 320 ? 126.843 -24.408 59.216  1.00 16.66 ? 322  ASN B OD1 1 
ATOM   5753 N  ND2 . ASN B 1 320 ? 128.189 -24.111 60.991  1.00 16.97 ? 322  ASN B ND2 1 
ATOM   5754 N  N   . LEU B 1 321 ? 129.349 -24.340 57.163  1.00 15.73 ? 323  LEU B N   1 
ATOM   5755 C  CA  . LEU B 1 321 ? 129.269 -25.178 55.973  1.00 16.08 ? 323  LEU B CA  1 
ATOM   5756 C  C   . LEU B 1 321 ? 128.526 -26.485 56.232  1.00 15.23 ? 323  LEU B C   1 
ATOM   5757 O  O   . LEU B 1 321 ? 128.617 -27.424 55.440  1.00 15.46 ? 323  LEU B O   1 
ATOM   5758 C  CB  . LEU B 1 321 ? 130.671 -25.465 55.424  1.00 16.02 ? 323  LEU B CB  1 
ATOM   5759 C  CG  . LEU B 1 321 ? 131.490 -24.243 54.998  1.00 16.56 ? 323  LEU B CG  1 
ATOM   5760 C  CD1 . LEU B 1 321 ? 132.907 -24.646 54.610  1.00 17.36 ? 323  LEU B CD1 1 
ATOM   5761 C  CD2 . LEU B 1 321 ? 130.810 -23.498 53.858  1.00 16.46 ? 323  LEU B CD2 1 
ATOM   5762 N  N   . SER B 1 322 ? 127.764 -26.531 57.321  1.00 14.17 ? 324  SER B N   1 
ATOM   5763 C  CA  . SER B 1 322 ? 127.099 -27.766 57.737  1.00 13.75 ? 324  SER B CA  1 
ATOM   5764 C  C   . SER B 1 322 ? 126.017 -28.204 56.757  1.00 13.36 ? 324  SER B C   1 
ATOM   5765 O  O   . SER B 1 322 ? 125.425 -27.376 56.059  1.00 14.47 ? 324  SER B O   1 
ATOM   5766 C  CB  . SER B 1 322 ? 126.494 -27.614 59.134  1.00 13.44 ? 324  SER B CB  1 
ATOM   5767 O  OG  . SER B 1 322 ? 125.235 -26.959 59.079  1.00 13.12 ? 324  SER B OG  1 
ATOM   5768 N  N   . ALA B 1 323 ? 125.748 -29.507 56.739  1.00 12.52 ? 325  ALA B N   1 
ATOM   5769 C  CA  . ALA B 1 323 ? 124.584 -30.067 56.054  1.00 12.94 ? 325  ALA B CA  1 
ATOM   5770 C  C   . ALA B 1 323 ? 124.475 -29.577 54.616  1.00 13.15 ? 325  ALA B C   1 
ATOM   5771 O  O   . ALA B 1 323 ? 123.378 -29.288 54.132  1.00 13.96 ? 325  ALA B O   1 
ATOM   5772 C  CB  . ALA B 1 323 ? 123.308 -29.748 56.820  1.00 12.44 ? 325  ALA B CB  1 
ATOM   5773 N  N   . GLY B 1 324 ? 125.613 -29.477 53.938  1.00 12.32 ? 326  GLY B N   1 
ATOM   5774 C  CA  . GLY B 1 324 ? 125.628 -29.054 52.542  1.00 11.98 ? 326  GLY B CA  1 
ATOM   5775 C  C   . GLY B 1 324 ? 124.772 -29.949 51.665  1.00 13.06 ? 326  GLY B C   1 
ATOM   5776 O  O   . GLY B 1 324 ? 124.098 -29.477 50.744  1.00 13.12 ? 326  GLY B O   1 
ATOM   5777 N  N   . ALA B 1 325 ? 124.789 -31.246 51.954  1.00 13.20 ? 327  ALA B N   1 
ATOM   5778 C  CA  . ALA B 1 325 ? 124.065 -32.218 51.140  1.00 13.84 ? 327  ALA B CA  1 
ATOM   5779 C  C   . ALA B 1 325 ? 122.556 -32.002 51.216  1.00 12.85 ? 327  ALA B C   1 
ATOM   5780 O  O   . ALA B 1 325 ? 121.808 -32.514 50.385  1.00 12.69 ? 327  ALA B O   1 
ATOM   5781 C  CB  . ALA B 1 325 ? 124.419 -33.634 51.562  1.00 15.68 ? 327  ALA B CB  1 
ATOM   5782 N  N   . ASN B 1 326 ? 122.112 -31.273 52.234  1.00 12.20 ? 328  ASN B N   1 
ATOM   5783 C  CA  . ASN B 1 326 ? 120.688 -31.010 52.422  1.00 12.69 ? 328  ASN B CA  1 
ATOM   5784 C  C   . ASN B 1 326 ? 120.253 -29.656 51.860  1.00 12.15 ? 328  ASN B C   1 
ATOM   5785 O  O   . ASN B 1 326 ? 119.226 -29.104 52.261  1.00 12.56 ? 328  ASN B O   1 
ATOM   5786 C  CB  . ASN B 1 326 ? 120.315 -31.122 53.901  1.00 12.84 ? 328  ASN B CB  1 
ATOM   5787 C  CG  . ASN B 1 326 ? 120.611 -32.498 54.472  1.00 14.65 ? 328  ASN B CG  1 
ATOM   5788 O  OD1 . ASN B 1 326 ? 121.410 -32.640 55.401  1.00 16.16 ? 328  ASN B OD1 1 
ATOM   5789 N  ND2 . ASN B 1 326 ? 119.985 -33.523 53.901  1.00 14.05 ? 328  ASN B ND2 1 
ATOM   5790 N  N   . SER B 1 327 ? 121.036 -29.124 50.929  1.00 11.95 ? 329  SER B N   1 
ATOM   5791 C  CA  . SER B 1 327 ? 120.738 -27.825 50.340  1.00 11.56 ? 329  SER B CA  1 
ATOM   5792 C  C   . SER B 1 327 ? 119.693 -27.951 49.242  1.00 11.19 ? 329  SER B C   1 
ATOM   5793 O  O   . SER B 1 327 ? 119.615 -28.977 48.566  1.00 11.02 ? 329  SER B O   1 
ATOM   5794 C  CB  . SER B 1 327 ? 122.009 -27.182 49.780  1.00 11.50 ? 329  SER B CB  1 
ATOM   5795 O  OG  . SER B 1 327 ? 122.961 -26.959 50.806  1.00 12.21 ? 329  SER B OG  1 
ATOM   5796 N  N   . ILE B 1 328 ? 118.887 -26.907 49.071  1.00 11.17 ? 330  ILE B N   1 
ATOM   5797 C  CA  . ILE B 1 328 ? 118.004 -26.809 47.910  1.00 11.11 ? 330  ILE B CA  1 
ATOM   5798 C  C   . ILE B 1 328 ? 118.134 -25.450 47.221  1.00 10.97 ? 330  ILE B C   1 
ATOM   5799 O  O   . ILE B 1 328 ? 118.403 -24.442 47.870  1.00 10.01 ? 330  ILE B O   1 
ATOM   5800 C  CB  . ILE B 1 328 ? 116.532 -27.065 48.289  1.00 10.77 ? 330  ILE B CB  1 
ATOM   5801 C  CG1 . ILE B 1 328 ? 116.037 -26.013 49.284  1.00 10.49 ? 330  ILE B CG1 1 
ATOM   5802 C  CG2 . ILE B 1 328 ? 116.365 -28.461 48.875  1.00 10.93 ? 330  ILE B CG2 1 
ATOM   5803 C  CD1 . ILE B 1 328 ? 114.537 -26.039 49.500  1.00 10.05 ? 330  ILE B CD1 1 
ATOM   5804 N  N   . MET B 1 329 ? 117.999 -25.442 45.897  1.00 11.72 ? 331  MET B N   1 
ATOM   5805 C  CA  . MET B 1 329 ? 117.838 -24.199 45.149  1.00 12.41 ? 331  MET B CA  1 
ATOM   5806 C  C   . MET B 1 329 ? 116.360 -23.836 45.033  1.00 12.11 ? 331  MET B C   1 
ATOM   5807 O  O   . MET B 1 329 ? 115.555 -24.630 44.550  1.00 12.63 ? 331  MET B O   1 
ATOM   5808 C  CB  . MET B 1 329 ? 118.444 -24.333 43.751  1.00 13.03 ? 331  MET B CB  1 
ATOM   5809 C  CG  . MET B 1 329 ? 119.960 -24.324 43.732  1.00 15.31 ? 331  MET B CG  1 
ATOM   5810 S  SD  . MET B 1 329 ? 120.628 -22.709 44.179  1.00 18.36 ? 331  MET B SD  1 
ATOM   5811 C  CE  . MET B 1 329 ? 122.245 -22.824 43.415  1.00 21.60 ? 331  MET B CE  1 
ATOM   5812 N  N   . ARG B 1 330 ? 116.008 -22.634 45.474  1.00 11.99 ? 332  ARG B N   1 
ATOM   5813 C  CA  . ARG B 1 330 ? 114.613 -22.203 45.480  1.00 11.82 ? 332  ARG B CA  1 
ATOM   5814 C  C   . ARG B 1 330 ? 114.327 -21.215 44.353  1.00 12.05 ? 332  ARG B C   1 
ATOM   5815 O  O   . ARG B 1 330 ? 115.021 -20.205 44.212  1.00 12.89 ? 332  ARG B O   1 
ATOM   5816 C  CB  . ARG B 1 330 ? 114.249 -21.584 46.834  1.00 12.34 ? 332  ARG B CB  1 
ATOM   5817 C  CG  . ARG B 1 330 ? 114.077 -22.602 47.952  1.00 12.87 ? 332  ARG B CG  1 
ATOM   5818 C  CD  . ARG B 1 330 ? 113.909 -21.928 49.307  1.00 13.55 ? 332  ARG B CD  1 
ATOM   5819 N  NE  . ARG B 1 330 ? 114.949 -20.929 49.544  1.00 13.13 ? 332  ARG B NE  1 
ATOM   5820 C  CZ  . ARG B 1 330 ? 114.716 -19.642 49.774  1.00 13.91 ? 332  ARG B CZ  1 
ATOM   5821 N  NH1 . ARG B 1 330 ? 113.468 -19.190 49.855  1.00 13.36 ? 332  ARG B NH1 1 
ATOM   5822 N  NH2 . ARG B 1 330 ? 115.734 -18.807 49.951  1.00 14.45 ? 332  ARG B NH2 1 
ATOM   5823 N  N   . SER B 1 331 ? 113.318 -21.523 43.543  1.00 11.28 ? 333  SER B N   1 
ATOM   5824 C  CA  . SER B 1 331 ? 112.889 -20.636 42.467  1.00 11.79 ? 333  SER B CA  1 
ATOM   5825 C  C   . SER B 1 331 ? 111.383 -20.382 42.513  1.00 11.28 ? 333  SER B C   1 
ATOM   5826 O  O   . SER B 1 331 ? 110.730 -20.279 41.475  1.00 11.25 ? 333  SER B O   1 
ATOM   5827 C  CB  . SER B 1 331 ? 113.270 -21.218 41.104  1.00 12.08 ? 333  SER B CB  1 
ATOM   5828 O  OG  . SER B 1 331 ? 114.666 -21.446 41.025  1.00 14.47 ? 333  SER B OG  1 
ATOM   5829 N  N   . GLY B 1 332 ? 110.835 -20.307 43.721  1.00 11.87 ? 334  GLY B N   1 
ATOM   5830 C  CA  . GLY B 1 332 ? 109.409 -20.047 43.901  1.00 12.21 ? 334  GLY B CA  1 
ATOM   5831 C  C   . GLY B 1 332 ? 109.004 -18.633 43.526  1.00 11.29 ? 334  GLY B C   1 
ATOM   5832 O  O   . GLY B 1 332 ? 109.839 -17.727 43.466  1.00 11.60 ? 334  GLY B O   1 
ATOM   5833 N  N   . ILE B 1 333 ? 107.710 -18.443 43.288  1.00 10.43 ? 335  ILE B N   1 
ATOM   5834 C  CA  . ILE B 1 333 ? 107.176 -17.142 42.901  1.00 10.01 ? 335  ILE B CA  1 
ATOM   5835 C  C   . ILE B 1 333 ? 105.714 -17.049 43.343  1.00 9.99  ? 335  ILE B C   1 
ATOM   5836 O  O   . ILE B 1 333 ? 104.982 -18.037 43.281  1.00 9.55  ? 335  ILE B O   1 
ATOM   5837 C  CB  . ILE B 1 333 ? 107.302 -16.933 41.373  1.00 10.48 ? 335  ILE B CB  1 
ATOM   5838 C  CG1 . ILE B 1 333 ? 106.600 -15.648 40.932  1.00 10.27 ? 335  ILE B CG1 1 
ATOM   5839 C  CG2 . ILE B 1 333 ? 106.763 -18.141 40.620  1.00 10.01 ? 335  ILE B CG2 1 
ATOM   5840 C  CD1 . ILE B 1 333 ? 107.017 -15.178 39.553  1.00 10.91 ? 335  ILE B CD1 1 
ATOM   5841 N  N   . PRO B 1 334 ? 105.299 -15.879 43.861  1.00 10.05 ? 336  PRO B N   1 
ATOM   5842 C  CA  . PRO B 1 334 ? 103.949 -15.776 44.419  1.00 9.82  ? 336  PRO B CA  1 
ATOM   5843 C  C   . PRO B 1 334 ? 102.885 -15.916 43.338  1.00 10.54 ? 336  PRO B C   1 
ATOM   5844 O  O   . PRO B 1 334 ? 103.182 -15.724 42.156  1.00 10.67 ? 336  PRO B O   1 
ATOM   5845 C  CB  . PRO B 1 334 ? 103.921 -14.363 45.018  1.00 9.89  ? 336  PRO B CB  1 
ATOM   5846 C  CG  . PRO B 1 334 ? 105.356 -14.026 45.262  1.00 9.94  ? 336  PRO B CG  1 
ATOM   5847 C  CD  . PRO B 1 334 ? 106.103 -14.676 44.133  1.00 9.95  ? 336  PRO B CD  1 
ATOM   5848 N  N   . TYR B 1 335 ? 101.682 -16.329 43.737  1.00 10.76 ? 337  TYR B N   1 
ATOM   5849 C  CA  . TYR B 1 335 ? 100.532 -16.357 42.837  1.00 11.53 ? 337  TYR B CA  1 
ATOM   5850 C  C   . TYR B 1 335 ? 99.289  -15.765 43.492  1.00 11.61 ? 337  TYR B C   1 
ATOM   5851 O  O   . TYR B 1 335 ? 99.172  -15.729 44.720  1.00 11.11 ? 337  TYR B O   1 
ATOM   5852 C  CB  . TYR B 1 335 ? 100.238 -17.786 42.351  1.00 11.52 ? 337  TYR B CB  1 
ATOM   5853 C  CG  . TYR B 1 335 ? 99.595  -18.692 43.384  1.00 11.68 ? 337  TYR B CG  1 
ATOM   5854 C  CD1 . TYR B 1 335 ? 98.210  -18.765 43.517  1.00 12.66 ? 337  TYR B CD1 1 
ATOM   5855 C  CD2 . TYR B 1 335 ? 100.373 -19.501 44.203  1.00 12.43 ? 337  TYR B CD2 1 
ATOM   5856 C  CE1 . TYR B 1 335 ? 97.623  -19.596 44.459  1.00 13.32 ? 337  TYR B CE1 1 
ATOM   5857 C  CE2 . TYR B 1 335 ? 99.796  -20.341 45.138  1.00 12.74 ? 337  TYR B CE2 1 
ATOM   5858 C  CZ  . TYR B 1 335 ? 98.423  -20.390 45.260  1.00 13.48 ? 337  TYR B CZ  1 
ATOM   5859 O  OH  . TYR B 1 335 ? 97.859  -21.232 46.196  1.00 13.48 ? 337  TYR B OH  1 
ATOM   5860 N  N   . GLY B 1 336 ? 98.361  -15.304 42.663  1.00 12.39 ? 338  GLY B N   1 
ATOM   5861 C  CA  . GLY B 1 336 ? 97.083  -14.808 43.153  1.00 11.89 ? 338  GLY B CA  1 
ATOM   5862 C  C   . GLY B 1 336 ? 97.075  -13.303 43.297  1.00 12.40 ? 338  GLY B C   1 
ATOM   5863 O  O   . GLY B 1 336 ? 98.107  -12.648 43.129  1.00 13.03 ? 338  GLY B O   1 
ATOM   5864 N  N   . PRO B 1 337 ? 95.901  -12.740 43.609  1.00 11.96 ? 339  PRO B N   1 
ATOM   5865 C  CA  . PRO B 1 337 ? 95.753  -11.299 43.777  1.00 12.02 ? 339  PRO B CA  1 
ATOM   5866 C  C   . PRO B 1 337 ? 96.382  -10.809 45.077  1.00 12.47 ? 339  PRO B C   1 
ATOM   5867 O  O   . PRO B 1 337 ? 96.550  -11.587 46.020  1.00 11.40 ? 339  PRO B O   1 
ATOM   5868 C  CB  . PRO B 1 337 ? 94.236  -11.108 43.822  1.00 11.68 ? 339  PRO B CB  1 
ATOM   5869 C  CG  . PRO B 1 337 ? 93.711  -12.403 44.345  1.00 11.83 ? 339  PRO B CG  1 
ATOM   5870 C  CD  . PRO B 1 337 ? 94.631  -13.462 43.805  1.00 11.91 ? 339  PRO B CD  1 
ATOM   5871 N  N   . GLU B 1 338 ? 96.726  -9.525  45.121  1.00 12.28 ? 340  GLU B N   1 
ATOM   5872 C  CA  . GLU B 1 338 ? 97.069  -8.875  46.378  1.00 12.55 ? 340  GLU B CA  1 
ATOM   5873 C  C   . GLU B 1 338 ? 95.887  -8.955  47.331  1.00 12.54 ? 340  GLU B C   1 
ATOM   5874 O  O   . GLU B 1 338 ? 94.737  -9.060  46.899  1.00 12.15 ? 340  GLU B O   1 
ATOM   5875 C  CB  . GLU B 1 338 ? 97.452  -7.413  46.141  1.00 13.25 ? 340  GLU B CB  1 
ATOM   5876 C  CG  . GLU B 1 338 ? 98.754  -7.230  45.380  1.00 13.57 ? 340  GLU B CG  1 
ATOM   5877 C  CD  . GLU B 1 338 ? 99.957  -7.666  46.192  1.00 13.89 ? 340  GLU B CD  1 
ATOM   5878 O  OE1 . GLU B 1 338 ? 100.195 -7.069  47.264  1.00 15.29 ? 340  GLU B OE1 1 
ATOM   5879 O  OE2 . GLU B 1 338 ? 100.637 -8.629  45.782  1.00 14.33 ? 340  GLU B OE2 1 
ATOM   5880 N  N   . VAL B 1 339 ? 96.169  -8.903  48.629  1.00 12.33 ? 341  VAL B N   1 
ATOM   5881 C  CA  . VAL B 1 339 ? 95.111  -8.871  49.627  1.00 12.50 ? 341  VAL B CA  1 
ATOM   5882 C  C   . VAL B 1 339 ? 94.205  -7.659  49.421  1.00 13.59 ? 341  VAL B C   1 
ATOM   5883 O  O   . VAL B 1 339 ? 94.681  -6.535  49.272  1.00 13.39 ? 341  VAL B O   1 
ATOM   5884 C  CB  . VAL B 1 339 ? 95.691  -8.851  51.053  1.00 12.34 ? 341  VAL B CB  1 
ATOM   5885 C  CG1 . VAL B 1 339 ? 94.571  -8.878  52.080  1.00 11.84 ? 341  VAL B CG1 1 
ATOM   5886 C  CG2 . VAL B 1 339 ? 96.637  -10.030 51.253  1.00 12.59 ? 341  VAL B CG2 1 
ATOM   5887 N  N   . THR B 1 340 ? 92.900  -7.903  49.372  1.00 13.73 ? 342  THR B N   1 
ATOM   5888 C  CA  . THR B 1 340 ? 91.927  -6.841  49.141  1.00 15.35 ? 342  THR B CA  1 
ATOM   5889 C  C   . THR B 1 340 ? 91.584  -6.158  50.458  1.00 16.13 ? 342  THR B C   1 
ATOM   5890 O  O   . THR B 1 340 ? 91.821  -6.711  51.528  1.00 16.13 ? 342  THR B O   1 
ATOM   5891 C  CB  . THR B 1 340 ? 90.633  -7.405  48.533  1.00 15.89 ? 342  THR B CB  1 
ATOM   5892 O  OG1 . THR B 1 340 ? 90.055  -8.347  49.442  1.00 15.88 ? 342  THR B OG1 1 
ATOM   5893 C  CG2 . THR B 1 340 ? 90.920  -8.100  47.203  1.00 15.03 ? 342  THR B CG2 1 
ATOM   5894 N  N   . SER B 1 341 ? 90.992  -4.971  50.382  1.00 18.39 ? 343  SER B N   1 
ATOM   5895 C  CA  . SER B 1 341 ? 90.621  -4.246  51.592  1.00 19.40 ? 343  SER B CA  1 
ATOM   5896 C  C   . SER B 1 341 ? 89.551  -4.983  52.397  1.00 18.64 ? 343  SER B C   1 
ATOM   5897 O  O   . SER B 1 341 ? 89.581  -4.982  53.628  1.00 19.31 ? 343  SER B O   1 
ATOM   5898 C  CB  . SER B 1 341 ? 90.163  -2.825  51.258  1.00 20.80 ? 343  SER B CB  1 
ATOM   5899 O  OG  . SER B 1 341 ? 89.105  -2.845  50.321  1.00 25.50 ? 343  SER B OG  1 
ATOM   5900 N  N   . ALA B 1 342 ? 88.637  -5.653  51.700  1.00 18.54 ? 344  ALA B N   1 
ATOM   5901 C  CA  . ALA B 1 342 ? 87.574  -6.407  52.363  1.00 17.80 ? 344  ALA B CA  1 
ATOM   5902 C  C   . ALA B 1 342 ? 88.122  -7.586  53.165  1.00 18.91 ? 344  ALA B C   1 
ATOM   5903 O  O   . ALA B 1 342 ? 87.687  -7.842  54.291  1.00 17.63 ? 344  ALA B O   1 
ATOM   5904 C  CB  . ALA B 1 342 ? 86.545  -6.884  51.351  1.00 17.68 ? 344  ALA B CB  1 
ATOM   5905 N  N   . GLU B 1 343 ? 89.051  -8.323  52.567  1.00 17.50 ? 345  GLU B N   1 
ATOM   5906 C  CA  . GLU B 1 343 ? 89.700  -9.434  53.253  1.00 17.14 ? 345  GLU B CA  1 
ATOM   5907 C  C   . GLU B 1 343 ? 90.461  -8.939  54.473  1.00 18.29 ? 345  GLU B C   1 
ATOM   5908 O  O   . GLU B 1 343 ? 90.422  -9.555  55.536  1.00 18.50 ? 345  GLU B O   1 
ATOM   5909 C  CB  . GLU B 1 343 ? 90.651  -10.162 52.305  1.00 15.30 ? 345  GLU B CB  1 
ATOM   5910 C  CG  . GLU B 1 343 ? 89.954  -11.113 51.348  1.00 15.30 ? 345  GLU B CG  1 
ATOM   5911 C  CD  . GLU B 1 343 ? 90.887  -11.627 50.273  1.00 14.26 ? 345  GLU B CD  1 
ATOM   5912 O  OE1 . GLU B 1 343 ? 91.419  -10.797 49.505  1.00 13.79 ? 345  GLU B OE1 1 
ATOM   5913 O  OE2 . GLU B 1 343 ? 91.101  -12.856 50.211  1.00 13.94 ? 345  GLU B OE2 1 
ATOM   5914 N  N   . SER B 1 344 ? 91.144  -7.812  54.315  1.00 21.10 ? 346  SER B N   1 
ATOM   5915 C  CA  . SER B 1 344 ? 91.918  -7.234  55.405  1.00 23.90 ? 346  SER B CA  1 
ATOM   5916 C  C   . SER B 1 344 ? 91.024  -6.803  56.559  1.00 22.84 ? 346  SER B C   1 
ATOM   5917 O  O   . SER B 1 344 ? 91.343  -7.039  57.724  1.00 22.34 ? 346  SER B O   1 
ATOM   5918 C  CB  . SER B 1 344 ? 92.738  -6.046  54.909  1.00 25.17 ? 346  SER B CB  1 
ATOM   5919 O  OG  . SER B 1 344 ? 93.740  -5.710  55.851  1.00 32.78 ? 346  SER B OG  1 
ATOM   5920 N  N   . ALA B 1 345 ? 89.911  -6.157  56.232  1.00 23.30 ? 347  ALA B N   1 
ATOM   5921 C  CA  . ALA B 1 345 ? 88.987  -5.676  57.250  1.00 24.22 ? 347  ALA B CA  1 
ATOM   5922 C  C   . ALA B 1 345 ? 88.365  -6.829  58.031  1.00 24.03 ? 347  ALA B C   1 
ATOM   5923 O  O   . ALA B 1 345 ? 88.091  -6.704  59.224  1.00 25.77 ? 347  ALA B O   1 
ATOM   5924 C  CB  . ALA B 1 345 ? 87.905  -4.811  56.620  1.00 24.76 ? 347  ALA B CB  1 
ATOM   5925 N  N   . SER B 1 346 ? 88.159  -7.958  57.361  1.00 22.59 ? 348  SER B N   1 
ATOM   5926 C  CA  . SER B 1 346 ? 87.449  -9.079  57.966  1.00 20.49 ? 348  SER B CA  1 
ATOM   5927 C  C   . SER B 1 346 ? 88.398  -10.111 58.568  1.00 19.22 ? 348  SER B C   1 
ATOM   5928 O  O   . SER B 1 346 ? 87.965  -11.022 59.268  1.00 18.30 ? 348  SER B O   1 
ATOM   5929 C  CB  . SER B 1 346 ? 86.530  -9.747  56.942  1.00 20.67 ? 348  SER B CB  1 
ATOM   5930 O  OG  . SER B 1 346 ? 87.283  -10.385 55.925  1.00 21.12 ? 348  SER B OG  1 
ATOM   5931 N  N   . ASN B 1 347 ? 89.688  -9.970  58.284  1.00 19.17 ? 349  ASN B N   1 
ATOM   5932 C  CA  . ASN B 1 347 ? 90.684  -10.957 58.699  1.00 19.47 ? 349  ASN B CA  1 
ATOM   5933 C  C   . ASN B 1 347 ? 90.454  -12.331 58.085  1.00 18.22 ? 349  ASN B C   1 
ATOM   5934 O  O   . ASN B 1 347 ? 90.917  -13.341 58.615  1.00 16.47 ? 349  ASN B O   1 
ATOM   5935 C  CB  . ASN B 1 347 ? 90.723  -11.082 60.222  1.00 19.67 ? 349  ASN B CB  1 
ATOM   5936 C  CG  . ASN B 1 347 ? 90.910  -9.750  60.911  1.00 20.76 ? 349  ASN B CG  1 
ATOM   5937 O  OD1 . ASN B 1 347 ? 91.805  -8.977  60.565  1.00 18.89 ? 349  ASN B OD1 1 
ATOM   5938 N  ND2 . ASN B 1 347 ? 90.062  -9.471  61.891  1.00 23.45 ? 349  ASN B ND2 1 
ATOM   5939 N  N   . THR B 1 348 ? 89.753  -12.364 56.958  1.00 18.38 ? 350  THR B N   1 
ATOM   5940 C  CA  . THR B 1 348 ? 89.372  -13.625 56.342  1.00 18.94 ? 350  THR B CA  1 
ATOM   5941 C  C   . THR B 1 348 ? 89.718  -13.642 54.857  1.00 17.30 ? 350  THR B C   1 
ATOM   5942 O  O   . THR B 1 348 ? 89.284  -12.775 54.100  1.00 16.35 ? 350  THR B O   1 
ATOM   5943 C  CB  . THR B 1 348 ? 87.867  -13.897 56.514  1.00 20.22 ? 350  THR B CB  1 
ATOM   5944 O  OG1 . THR B 1 348 ? 87.539  -13.893 57.909  1.00 23.70 ? 350  THR B OG1 1 
ATOM   5945 C  CG2 . THR B 1 348 ? 87.494  -15.244 55.912  1.00 19.54 ? 350  THR B CG2 1 
ATOM   5946 N  N   . THR B 1 349 ? 90.491  -14.643 54.449  1.00 15.96 ? 351  THR B N   1 
ATOM   5947 C  CA  . THR B 1 349 ? 90.787  -14.865 53.038  1.00 14.82 ? 351  THR B CA  1 
ATOM   5948 C  C   . THR B 1 349 ? 89.532  -15.267 52.265  1.00 15.29 ? 351  THR B C   1 
ATOM   5949 O  O   . THR B 1 349 ? 88.791  -16.145 52.698  1.00 15.72 ? 351  THR B O   1 
ATOM   5950 C  CB  . THR B 1 349 ? 91.841  -15.978 52.869  1.00 14.56 ? 351  THR B CB  1 
ATOM   5951 O  OG1 . THR B 1 349 ? 93.096  -15.532 53.397  1.00 13.66 ? 351  THR B OG1 1 
ATOM   5952 C  CG2 . THR B 1 349 ? 92.009  -16.338 51.392  1.00 13.98 ? 351  THR B CG2 1 
ATOM   5953 N  N   . THR B 1 350 ? 89.316  -14.654 51.103  1.00 15.67 ? 352  THR B N   1 
ATOM   5954 C  CA  . THR B 1 350 ? 88.321  -15.155 50.154  1.00 15.79 ? 352  THR B CA  1 
ATOM   5955 C  C   . THR B 1 350 ? 88.903  -15.438 48.770  1.00 15.47 ? 352  THR B C   1 
ATOM   5956 O  O   . THR B 1 350 ? 88.313  -16.182 47.984  1.00 16.21 ? 352  THR B O   1 
ATOM   5957 C  CB  . THR B 1 350 ? 87.117  -14.200 50.006  1.00 16.28 ? 352  THR B CB  1 
ATOM   5958 O  OG1 . THR B 1 350 ? 87.538  -12.991 49.362  1.00 14.95 ? 352  THR B OG1 1 
ATOM   5959 C  CG2 . THR B 1 350 ? 86.523  -13.871 51.367  1.00 17.38 ? 352  THR B CG2 1 
ATOM   5960 N  N   . GLN B 1 351 ? 90.029  -14.807 48.455  1.00 14.84 ? 353  GLN B N   1 
ATOM   5961 C  CA  . GLN B 1 351 ? 90.690  -15.021 47.171  1.00 14.71 ? 353  GLN B CA  1 
ATOM   5962 C  C   . GLN B 1 351 ? 91.959  -15.849 47.371  1.00 15.50 ? 353  GLN B C   1 
ATOM   5963 O  O   . GLN B 1 351 ? 92.801  -15.509 48.200  1.00 15.37 ? 353  GLN B O   1 
ATOM   5964 C  CB  . GLN B 1 351 ? 91.033  -13.680 46.514  1.00 15.01 ? 353  GLN B CB  1 
ATOM   5965 C  CG  . GLN B 1 351 ? 89.927  -12.635 46.607  1.00 15.11 ? 353  GLN B CG  1 
ATOM   5966 C  CD  . GLN B 1 351 ? 88.602  -13.138 46.067  1.00 15.07 ? 353  GLN B CD  1 
ATOM   5967 O  OE1 . GLN B 1 351 ? 87.610  -13.212 46.794  1.00 14.49 ? 353  GLN B OE1 1 
ATOM   5968 N  NE2 . GLN B 1 351 ? 88.586  -13.515 44.791  1.00 14.69 ? 353  GLN B NE2 1 
ATOM   5969 N  N   . GLU B 1 352 ? 92.069  -16.966 46.658  1.00 14.34 ? 354  GLU B N   1 
ATOM   5970 C  CA  . GLU B 1 352 ? 93.222  -17.840 46.833  1.00 15.14 ? 354  GLU B CA  1 
ATOM   5971 C  C   . GLU B 1 352 ? 94.496  -17.156 46.351  1.00 14.75 ? 354  GLU B C   1 
ATOM   5972 O  O   . GLU B 1 352 ? 94.541  -16.599 45.255  1.00 13.67 ? 354  GLU B O   1 
ATOM   5973 C  CB  . GLU B 1 352 ? 93.030  -19.188 46.130  1.00 16.24 ? 354  GLU B CB  1 
ATOM   5974 C  CG  . GLU B 1 352 ? 93.902  -20.296 46.714  1.00 18.22 ? 354  GLU B CG  1 
ATOM   5975 C  CD  . GLU B 1 352 ? 94.126  -21.454 45.757  1.00 19.74 ? 354  GLU B CD  1 
ATOM   5976 O  OE1 . GLU B 1 352 ? 93.212  -21.760 44.964  1.00 21.68 ? 354  GLU B OE1 1 
ATOM   5977 O  OE2 . GLU B 1 352 ? 95.210  -22.079 45.818  1.00 19.78 ? 354  GLU B OE2 1 
ATOM   5978 N  N   . ARG B 1 353 ? 95.495  -17.123 47.221  1.00 13.17 ? 355  ARG B N   1 
ATOM   5979 C  CA  . ARG B 1 353 ? 96.805  -16.595 46.878  1.00 12.85 ? 355  ARG B CA  1 
ATOM   5980 C  C   . ARG B 1 353 ? 97.839  -17.409 47.637  1.00 12.10 ? 355  ARG B C   1 
ATOM   5981 O  O   . ARG B 1 353 ? 97.503  -18.103 48.595  1.00 12.39 ? 355  ARG B O   1 
ATOM   5982 C  CB  . ARG B 1 353 ? 96.904  -15.120 47.286  1.00 12.23 ? 355  ARG B CB  1 
ATOM   5983 C  CG  . ARG B 1 353 ? 96.640  -14.875 48.765  1.00 11.97 ? 355  ARG B CG  1 
ATOM   5984 C  CD  . ARG B 1 353 ? 96.780  -13.405 49.130  1.00 12.32 ? 355  ARG B CD  1 
ATOM   5985 N  NE  . ARG B 1 353 ? 95.784  -12.573 48.456  1.00 12.17 ? 355  ARG B NE  1 
ATOM   5986 C  CZ  . ARG B 1 353 ? 94.521  -12.442 48.854  1.00 11.86 ? 355  ARG B CZ  1 
ATOM   5987 N  NH1 . ARG B 1 353 ? 94.091  -13.078 49.936  1.00 11.55 ? 355  ARG B NH1 1 
ATOM   5988 N  NH2 . ARG B 1 353 ? 93.687  -11.666 48.170  1.00 11.41 ? 355  ARG B NH2 1 
ATOM   5989 N  N   . GLY B 1 354 ? 99.102  -17.293 47.245  1.00 12.47 ? 356  GLY B N   1 
ATOM   5990 C  CA  . GLY B 1 354 ? 100.172 -17.969 47.971  1.00 11.70 ? 356  GLY B CA  1 
ATOM   5991 C  C   . GLY B 1 354 ? 101.482 -18.042 47.216  1.00 11.12 ? 356  GLY B C   1 
ATOM   5992 O  O   . GLY B 1 354 ? 101.878 -17.093 46.539  1.00 10.61 ? 356  GLY B O   1 
ATOM   5993 N  N   . LEU B 1 355 ? 102.170 -19.171 47.362  1.00 10.49 ? 357  LEU B N   1 
ATOM   5994 C  CA  . LEU B 1 355 ? 103.489 -19.356 46.774  1.00 10.12 ? 357  LEU B CA  1 
ATOM   5995 C  C   . LEU B 1 355 ? 103.496 -20.559 45.845  1.00 9.88  ? 357  LEU B C   1 
ATOM   5996 O  O   . LEU B 1 355 ? 103.193 -21.673 46.265  1.00 10.14 ? 357  LEU B O   1 
ATOM   5997 C  CB  . LEU B 1 355 ? 104.535 -19.559 47.874  1.00 10.47 ? 357  LEU B CB  1 
ATOM   5998 C  CG  . LEU B 1 355 ? 105.989 -19.663 47.405  1.00 10.61 ? 357  LEU B CG  1 
ATOM   5999 C  CD1 . LEU B 1 355 ? 106.448 -18.368 46.751  1.00 10.52 ? 357  LEU B CD1 1 
ATOM   6000 C  CD2 . LEU B 1 355 ? 106.898 -20.042 48.566  1.00 11.05 ? 357  LEU B CD2 1 
ATOM   6001 N  N   . ALA B 1 356 ? 103.836 -20.331 44.581  1.00 9.25  ? 358  ALA B N   1 
ATOM   6002 C  CA  . ALA B 1 356 ? 104.206 -21.418 43.687  1.00 9.16  ? 358  ALA B CA  1 
ATOM   6003 C  C   . ALA B 1 356 ? 105.625 -21.875 44.009  1.00 9.15  ? 358  ALA B C   1 
ATOM   6004 O  O   . ALA B 1 356 ? 106.600 -21.333 43.487  1.00 9.37  ? 358  ALA B O   1 
ATOM   6005 C  CB  . ALA B 1 356 ? 104.101 -20.974 42.234  1.00 9.04  ? 358  ALA B CB  1 
ATOM   6006 N  N   . PHE B 1 357 ? 105.732 -22.821 44.934  1.00 9.34  ? 359  PHE B N   1 
ATOM   6007 C  CA  . PHE B 1 357 ? 107.016 -23.205 45.499  1.00 9.51  ? 359  PHE B CA  1 
ATOM   6008 C  C   . PHE B 1 357 ? 107.760 -24.138 44.552  1.00 9.47  ? 359  PHE B C   1 
ATOM   6009 O  O   . PHE B 1 357 ? 107.206 -25.135 44.089  1.00 9.24  ? 359  PHE B O   1 
ATOM   6010 C  CB  . PHE B 1 357 ? 106.807 -23.887 46.854  1.00 10.02 ? 359  PHE B CB  1 
ATOM   6011 C  CG  . PHE B 1 357 ? 108.071 -24.409 47.475  1.00 10.34 ? 359  PHE B CG  1 
ATOM   6012 C  CD1 . PHE B 1 357 ? 108.862 -23.589 48.265  1.00 10.63 ? 359  PHE B CD1 1 
ATOM   6013 C  CD2 . PHE B 1 357 ? 108.456 -25.727 47.289  1.00 10.54 ? 359  PHE B CD2 1 
ATOM   6014 C  CE1 . PHE B 1 357 ? 110.014 -24.075 48.857  1.00 11.01 ? 359  PHE B CE1 1 
ATOM   6015 C  CE2 . PHE B 1 357 ? 109.601 -26.223 47.889  1.00 9.99  ? 359  PHE B CE2 1 
ATOM   6016 C  CZ  . PHE B 1 357 ? 110.388 -25.392 48.663  1.00 10.22 ? 359  PHE B CZ  1 
ATOM   6017 N  N   . VAL B 1 358 ? 109.012 -23.799 44.259  1.00 8.61  ? 360  VAL B N   1 
ATOM   6018 C  CA  . VAL B 1 358 ? 109.866 -24.646 43.438  1.00 8.71  ? 360  VAL B CA  1 
ATOM   6019 C  C   . VAL B 1 358 ? 111.197 -24.876 44.144  1.00 8.59  ? 360  VAL B C   1 
ATOM   6020 O  O   . VAL B 1 358 ? 111.876 -23.922 44.535  1.00 9.00  ? 360  VAL B O   1 
ATOM   6021 C  CB  . VAL B 1 358 ? 110.133 -24.008 42.054  1.00 8.80  ? 360  VAL B CB  1 
ATOM   6022 C  CG1 . VAL B 1 358 ? 111.007 -24.919 41.204  1.00 8.53  ? 360  VAL B CG1 1 
ATOM   6023 C  CG2 . VAL B 1 358 ? 108.825 -23.698 41.337  1.00 8.84  ? 360  VAL B CG2 1 
ATOM   6024 N  N   . ALA B 1 359 ? 111.554 -26.144 44.330  1.00 8.51  ? 361  ALA B N   1 
ATOM   6025 C  CA  . ALA B 1 359 ? 112.861 -26.508 44.865  1.00 8.41  ? 361  ALA B CA  1 
ATOM   6026 C  C   . ALA B 1 359 ? 113.596 -27.446 43.912  1.00 8.44  ? 361  ALA B C   1 
ATOM   6027 O  O   . ALA B 1 359 ? 113.018 -28.410 43.411  1.00 8.12  ? 361  ALA B O   1 
ATOM   6028 C  CB  . ALA B 1 359 ? 112.715 -27.158 46.234  1.00 8.13  ? 361  ALA B CB  1 
ATOM   6029 N  N   . TYR B 1 360 ? 114.878 -27.168 43.691  1.00 8.21  ? 362  TYR B N   1 
ATOM   6030 C  CA  . TYR B 1 360 ? 115.728 -28.037 42.886  1.00 8.13  ? 362  TYR B CA  1 
ATOM   6031 C  C   . TYR B 1 360 ? 116.770 -28.729 43.757  1.00 7.80  ? 362  TYR B C   1 
ATOM   6032 O  O   . TYR B 1 360 ? 117.321 -28.129 44.683  1.00 7.75  ? 362  TYR B O   1 
ATOM   6033 C  CB  . TYR B 1 360 ? 116.424 -27.236 41.786  1.00 8.33  ? 362  TYR B CB  1 
ATOM   6034 C  CG  . TYR B 1 360 ? 115.491 -26.730 40.714  1.00 8.71  ? 362  TYR B CG  1 
ATOM   6035 C  CD1 . TYR B 1 360 ? 115.064 -27.565 39.693  1.00 8.81  ? 362  TYR B CD1 1 
ATOM   6036 C  CD2 . TYR B 1 360 ? 115.019 -25.422 40.734  1.00 9.33  ? 362  TYR B CD2 1 
ATOM   6037 C  CE1 . TYR B 1 360 ? 114.222 -27.107 38.701  1.00 9.39  ? 362  TYR B CE1 1 
ATOM   6038 C  CE2 . TYR B 1 360 ? 114.160 -24.958 39.755  1.00 9.30  ? 362  TYR B CE2 1 
ATOM   6039 C  CZ  . TYR B 1 360 ? 113.768 -25.805 38.741  1.00 9.44  ? 362  TYR B CZ  1 
ATOM   6040 O  OH  . TYR B 1 360 ? 112.918 -25.355 37.760  1.00 10.44 ? 362  TYR B OH  1 
ATOM   6041 N  N   . GLN B 1 361 ? 117.021 -30.001 43.462  1.00 7.67  ? 363  GLN B N   1 
ATOM   6042 C  CA  . GLN B 1 361 ? 117.996 -30.798 44.200  1.00 7.83  ? 363  GLN B CA  1 
ATOM   6043 C  C   . GLN B 1 361 ? 118.280 -32.065 43.404  1.00 8.15  ? 363  GLN B C   1 
ATOM   6044 O  O   . GLN B 1 361 ? 117.464 -32.479 42.578  1.00 8.42  ? 363  GLN B O   1 
ATOM   6045 C  CB  . GLN B 1 361 ? 117.454 -31.165 45.587  1.00 7.62  ? 363  GLN B CB  1 
ATOM   6046 C  CG  . GLN B 1 361 ? 116.178 -31.999 45.561  1.00 7.62  ? 363  GLN B CG  1 
ATOM   6047 C  CD  . GLN B 1 361 ? 114.918 -31.158 45.668  1.00 7.89  ? 363  GLN B CD  1 
ATOM   6048 O  OE1 . GLN B 1 361 ? 114.546 -30.718 46.756  1.00 8.61  ? 363  GLN B OE1 1 
ATOM   6049 N  NE2 . GLN B 1 361 ? 114.257 -30.923 44.532  1.00 7.13  ? 363  GLN B NE2 1 
ATOM   6050 N  N   . ALA B 1 362 ? 119.442 -32.669 43.637  1.00 8.32  ? 364  ALA B N   1 
ATOM   6051 C  CA  . ALA B 1 362 ? 119.824 -33.872 42.908  1.00 8.53  ? 364  ALA B CA  1 
ATOM   6052 C  C   . ALA B 1 362 ? 119.242 -35.132 43.542  1.00 9.01  ? 364  ALA B C   1 
ATOM   6053 O  O   . ALA B 1 362 ? 119.081 -36.153 42.874  1.00 8.71  ? 364  ALA B O   1 
ATOM   6054 C  CB  . ALA B 1 362 ? 121.337 -33.974 42.797  1.00 8.45  ? 364  ALA B CB  1 
ATOM   6055 N  N   . GLN B 1 363 ? 118.969 -35.061 44.843  1.00 9.80  ? 365  GLN B N   1 
ATOM   6056 C  CA  . GLN B 1 363 ? 118.289 -36.136 45.557  1.00 10.22 ? 365  GLN B CA  1 
ATOM   6057 C  C   . GLN B 1 363 ? 117.116 -35.574 46.354  1.00 10.52 ? 365  GLN B C   1 
ATOM   6058 O  O   . GLN B 1 363 ? 117.303 -34.775 47.275  1.00 10.45 ? 365  GLN B O   1 
ATOM   6059 C  CB  . GLN B 1 363 ? 119.256 -36.851 46.509  1.00 11.24 ? 365  GLN B CB  1 
ATOM   6060 C  CG  . GLN B 1 363 ? 120.495 -37.423 45.839  1.00 11.85 ? 365  GLN B CG  1 
ATOM   6061 C  CD  . GLN B 1 363 ? 121.401 -38.149 46.819  1.00 13.33 ? 365  GLN B CD  1 
ATOM   6062 O  OE1 . GLN B 1 363 ? 122.552 -37.760 47.025  1.00 15.34 ? 365  GLN B OE1 1 
ATOM   6063 N  NE2 . GLN B 1 363 ? 120.876 -39.188 47.450  1.00 12.55 ? 365  GLN B NE2 1 
ATOM   6064 N  N   . LEU B 1 364 ? 115.908 -36.005 46.009  1.00 10.36 ? 366  LEU B N   1 
ATOM   6065 C  CA  . LEU B 1 364 ? 114.717 -35.545 46.712  1.00 10.73 ? 366  LEU B CA  1 
ATOM   6066 C  C   . LEU B 1 364 ? 114.738 -35.956 48.183  1.00 11.33 ? 366  LEU B C   1 
ATOM   6067 O  O   . LEU B 1 364 ? 114.222 -35.244 49.042  1.00 11.29 ? 366  LEU B O   1 
ATOM   6068 C  CB  . LEU B 1 364 ? 113.454 -36.061 46.022  1.00 10.66 ? 366  LEU B CB  1 
ATOM   6069 C  CG  . LEU B 1 364 ? 113.050 -35.295 44.761  1.00 10.76 ? 366  LEU B CG  1 
ATOM   6070 C  CD1 . LEU B 1 364 ? 112.044 -36.093 43.944  1.00 10.79 ? 366  LEU B CD1 1 
ATOM   6071 C  CD2 . LEU B 1 364 ? 112.486 -33.929 45.133  1.00 10.60 ? 366  LEU B CD2 1 
ATOM   6072 N  N   . SER B 1 365 ? 115.378 -37.085 48.473  1.00 11.69 ? 367  SER B N   1 
ATOM   6073 C  CA  . SER B 1 365 ? 115.413 -37.614 49.834  1.00 11.52 ? 367  SER B CA  1 
ATOM   6074 C  C   . SER B 1 365 ? 116.298 -36.780 50.754  1.00 12.19 ? 367  SER B C   1 
ATOM   6075 O  O   . SER B 1 365 ? 116.193 -36.873 51.979  1.00 13.18 ? 367  SER B O   1 
ATOM   6076 C  CB  . SER B 1 365 ? 115.900 -39.063 49.827  1.00 12.02 ? 367  SER B CB  1 
ATOM   6077 O  OG  . SER B 1 365 ? 117.261 -39.125 49.448  1.00 11.33 ? 367  SER B OG  1 
ATOM   6078 N  N   . GLN B 1 366 ? 117.171 -35.972 50.158  1.00 13.20 ? 368  GLN B N   1 
ATOM   6079 C  CA  . GLN B 1 366 ? 118.095 -35.124 50.907  1.00 14.40 ? 368  GLN B CA  1 
ATOM   6080 C  C   . GLN B 1 366 ? 117.601 -33.684 50.932  1.00 13.90 ? 368  GLN B C   1 
ATOM   6081 O  O   . GLN B 1 366 ? 117.992 -32.895 51.796  1.00 12.78 ? 368  GLN B O   1 
ATOM   6082 C  CB  . GLN B 1 366 ? 119.486 -35.159 50.265  1.00 16.25 ? 368  GLN B CB  1 
ATOM   6083 C  CG  . GLN B 1 366 ? 120.098 -36.546 50.179  1.00 18.34 ? 368  GLN B CG  1 
ATOM   6084 C  CD  . GLN B 1 366 ? 120.154 -37.231 51.527  1.00 22.10 ? 368  GLN B CD  1 
ATOM   6085 O  OE1 . GLN B 1 366 ? 120.780 -36.732 52.462  1.00 25.66 ? 368  GLN B OE1 1 
ATOM   6086 N  NE2 . GLN B 1 366 ? 119.480 -38.371 51.642  1.00 23.60 ? 368  GLN B NE2 1 
ATOM   6087 N  N   . GLY B 1 367 ? 116.771 -33.338 49.954  1.00 12.71 ? 369  GLY B N   1 
ATOM   6088 C  CA  . GLY B 1 367 ? 116.365 -31.954 49.749  1.00 11.78 ? 369  GLY B CA  1 
ATOM   6089 C  C   . GLY B 1 367 ? 114.995 -31.669 50.326  1.00 12.17 ? 369  GLY B C   1 
ATOM   6090 O  O   . GLY B 1 367 ? 114.760 -31.859 51.521  1.00 12.11 ? 369  GLY B O   1 
ATOM   6091 N  N   . PHE B 1 368 ? 114.084 -31.226 49.466  1.00 12.17 ? 370  PHE B N   1 
ATOM   6092 C  CA  . PHE B 1 368 ? 112.752 -30.803 49.893  1.00 12.69 ? 370  PHE B CA  1 
ATOM   6093 C  C   . PHE B 1 368 ? 112.099 -31.794 50.855  1.00 13.05 ? 370  PHE B C   1 
ATOM   6094 O  O   . PHE B 1 368 ? 111.571 -31.406 51.901  1.00 13.30 ? 370  PHE B O   1 
ATOM   6095 C  CB  . PHE B 1 368 ? 111.841 -30.587 48.683  1.00 12.31 ? 370  PHE B CB  1 
ATOM   6096 C  CG  . PHE B 1 368 ? 110.379 -30.648 49.018  1.00 12.71 ? 370  PHE B CG  1 
ATOM   6097 C  CD1 . PHE B 1 368 ? 109.773 -29.614 49.713  1.00 12.95 ? 370  PHE B CD1 1 
ATOM   6098 C  CD2 . PHE B 1 368 ? 109.633 -31.777 48.721  1.00 13.29 ? 370  PHE B CD2 1 
ATOM   6099 C  CE1 . PHE B 1 368 ? 108.441 -29.688 50.074  1.00 12.35 ? 370  PHE B CE1 1 
ATOM   6100 C  CE2 . PHE B 1 368 ? 108.298 -31.857 49.079  1.00 13.01 ? 370  PHE B CE2 1 
ATOM   6101 C  CZ  . PHE B 1 368 ? 107.704 -30.812 49.760  1.00 12.58 ? 370  PHE B CZ  1 
ATOM   6102 N  N   . HIS B 1 369 ? 112.078 -33.063 50.460  1.00 13.29 ? 371  HIS B N   1 
ATOM   6103 C  CA  . HIS B 1 369 ? 111.385 -34.100 51.220  1.00 13.42 ? 371  HIS B CA  1 
ATOM   6104 C  C   . HIS B 1 369 ? 111.962 -34.192 52.630  1.00 13.80 ? 371  HIS B C   1 
ATOM   6105 O  O   . HIS B 1 369 ? 111.222 -34.276 53.611  1.00 13.41 ? 371  HIS B O   1 
ATOM   6106 C  CB  . HIS B 1 369 ? 111.499 -35.444 50.491  1.00 13.71 ? 371  HIS B CB  1 
ATOM   6107 C  CG  . HIS B 1 369 ? 111.179 -36.635 51.341  1.00 14.17 ? 371  HIS B CG  1 
ATOM   6108 N  ND1 . HIS B 1 369 ? 109.994 -37.328 51.230  1.00 13.95 ? 371  HIS B ND1 1 
ATOM   6109 C  CD2 . HIS B 1 369 ? 111.927 -37.312 52.246  1.00 15.47 ? 371  HIS B CD2 1 
ATOM   6110 C  CE1 . HIS B 1 369 ? 110.008 -38.358 52.058  1.00 15.74 ? 371  HIS B CE1 1 
ATOM   6111 N  NE2 . HIS B 1 369 ? 111.170 -38.370 52.688  1.00 16.26 ? 371  HIS B NE2 1 
ATOM   6112 N  N   . PHE B 1 370 ? 113.285 -34.102 52.722  1.00 13.37 ? 372  PHE B N   1 
ATOM   6113 C  CA  . PHE B 1 370 ? 113.989 -34.220 53.994  1.00 13.45 ? 372  PHE B CA  1 
ATOM   6114 C  C   . PHE B 1 370 ? 113.735 -32.996 54.868  1.00 13.12 ? 372  PHE B C   1 
ATOM   6115 O  O   . PHE B 1 370 ? 113.434 -33.122 56.056  1.00 13.62 ? 372  PHE B O   1 
ATOM   6116 C  CB  . PHE B 1 370 ? 115.492 -34.384 53.753  1.00 13.73 ? 372  PHE B CB  1 
ATOM   6117 C  CG  . PHE B 1 370 ? 116.272 -34.741 54.988  1.00 13.85 ? 372  PHE B CG  1 
ATOM   6118 C  CD1 . PHE B 1 370 ? 116.261 -36.037 55.481  1.00 13.94 ? 372  PHE B CD1 1 
ATOM   6119 C  CD2 . PHE B 1 370 ? 117.031 -33.786 55.644  1.00 14.07 ? 372  PHE B CD2 1 
ATOM   6120 C  CE1 . PHE B 1 370 ? 116.985 -36.369 56.615  1.00 14.39 ? 372  PHE B CE1 1 
ATOM   6121 C  CE2 . PHE B 1 370 ? 117.755 -34.111 56.778  1.00 14.03 ? 372  PHE B CE2 1 
ATOM   6122 C  CZ  . PHE B 1 370 ? 117.733 -35.405 57.263  1.00 13.84 ? 372  PHE B CZ  1 
ATOM   6123 N  N   . LEU B 1 371 ? 113.848 -31.816 54.269  1.00 12.36 ? 373  LEU B N   1 
ATOM   6124 C  CA  . LEU B 1 371 ? 113.616 -30.567 54.986  1.00 12.97 ? 373  LEU B CA  1 
ATOM   6125 C  C   . LEU B 1 371 ? 112.200 -30.511 55.560  1.00 12.87 ? 373  LEU B C   1 
ATOM   6126 O  O   . LEU B 1 371 ? 112.002 -30.088 56.696  1.00 13.66 ? 373  LEU B O   1 
ATOM   6127 C  CB  . LEU B 1 371 ? 113.870 -29.363 54.075  1.00 12.14 ? 373  LEU B CB  1 
ATOM   6128 C  CG  . LEU B 1 371 ? 115.271 -28.744 54.058  1.00 12.46 ? 373  LEU B CG  1 
ATOM   6129 C  CD1 . LEU B 1 371 ? 116.347 -29.806 53.885  1.00 12.36 ? 373  LEU B CD1 1 
ATOM   6130 C  CD2 . LEU B 1 371 ? 115.383 -27.686 52.970  1.00 11.92 ? 373  LEU B CD2 1 
ATOM   6131 N  N   . GLN B 1 372 ? 111.222 -30.960 54.780  1.00 13.41 ? 374  GLN B N   1 
ATOM   6132 C  CA  . GLN B 1 372 ? 109.830 -30.937 55.224  1.00 14.38 ? 374  GLN B CA  1 
ATOM   6133 C  C   . GLN B 1 372 ? 109.568 -31.939 56.346  1.00 14.91 ? 374  GLN B C   1 
ATOM   6134 O  O   . GLN B 1 372 ? 109.031 -31.577 57.393  1.00 15.10 ? 374  GLN B O   1 
ATOM   6135 C  CB  . GLN B 1 372 ? 108.876 -31.187 54.053  1.00 14.57 ? 374  GLN B CB  1 
ATOM   6136 C  CG  . GLN B 1 372 ? 107.399 -31.091 54.417  1.00 14.29 ? 374  GLN B CG  1 
ATOM   6137 C  CD  . GLN B 1 372 ? 106.943 -29.665 54.674  1.00 15.23 ? 374  GLN B CD  1 
ATOM   6138 O  OE1 . GLN B 1 372 ? 107.034 -28.805 53.798  1.00 15.24 ? 374  GLN B OE1 1 
ATOM   6139 N  NE2 . GLN B 1 372 ? 106.408 -29.419 55.866  1.00 14.50 ? 374  GLN B NE2 1 
ATOM   6140 N  N   . GLN B 1 373 ? 109.960 -33.192 56.127  1.00 14.75 ? 375  GLN B N   1 
ATOM   6141 C  CA  . GLN B 1 373 ? 109.581 -34.281 57.028  1.00 15.72 ? 375  GLN B CA  1 
ATOM   6142 C  C   . GLN B 1 373 ? 110.451 -34.344 58.279  1.00 16.16 ? 375  GLN B C   1 
ATOM   6143 O  O   . GLN B 1 373 ? 109.941 -34.484 59.388  1.00 16.34 ? 375  GLN B O   1 
ATOM   6144 C  CB  . GLN B 1 373 ? 109.619 -35.632 56.307  1.00 15.98 ? 375  GLN B CB  1 
ATOM   6145 C  CG  . GLN B 1 373 ? 109.331 -36.814 57.222  1.00 17.72 ? 375  GLN B CG  1 
ATOM   6146 C  CD  . GLN B 1 373 ? 109.393 -38.152 56.508  1.00 18.07 ? 375  GLN B CD  1 
ATOM   6147 O  OE1 . GLN B 1 373 ? 108.585 -39.045 56.766  1.00 20.49 ? 375  GLN B OE1 1 
ATOM   6148 N  NE2 . GLN B 1 373 ? 110.375 -38.310 55.634  1.00 17.72 ? 375  GLN B NE2 1 
ATOM   6149 N  N   . THR B 1 374 ? 111.766 -34.281 58.090  1.00 15.19 ? 376  THR B N   1 
ATOM   6150 C  CA  . THR B 1 374 ? 112.706 -34.598 59.161  1.00 15.10 ? 376  THR B CA  1 
ATOM   6151 C  C   . THR B 1 374 ? 113.103 -33.369 59.975  1.00 14.72 ? 376  THR B C   1 
ATOM   6152 O  O   . THR B 1 374 ? 113.513 -33.485 61.132  1.00 15.03 ? 376  THR B O   1 
ATOM   6153 C  CB  . THR B 1 374 ? 113.963 -35.293 58.607  1.00 15.53 ? 376  THR B CB  1 
ATOM   6154 O  OG1 . THR B 1 374 ? 113.577 -36.491 57.921  1.00 15.66 ? 376  THR B OG1 1 
ATOM   6155 C  CG2 . THR B 1 374 ? 114.933 -35.641 59.732  1.00 15.64 ? 376  THR B CG2 1 
ATOM   6156 N  N   . TRP B 1 375 ? 112.961 -32.190 59.374  1.00 13.69 ? 377  TRP B N   1 
ATOM   6157 C  CA  . TRP B 1 375 ? 113.337 -30.948 60.038  1.00 13.18 ? 377  TRP B CA  1 
ATOM   6158 C  C   . TRP B 1 375 ? 112.122 -30.094 60.412  1.00 13.36 ? 377  TRP B C   1 
ATOM   6159 O  O   . TRP B 1 375 ? 111.838 -29.890 61.596  1.00 12.06 ? 377  TRP B O   1 
ATOM   6160 C  CB  . TRP B 1 375 ? 114.326 -30.148 59.181  1.00 13.10 ? 377  TRP B CB  1 
ATOM   6161 C  CG  . TRP B 1 375 ? 115.697 -30.768 59.091  1.00 13.47 ? 377  TRP B CG  1 
ATOM   6162 C  CD1 . TRP B 1 375 ? 116.138 -31.885 59.742  1.00 14.20 ? 377  TRP B CD1 1 
ATOM   6163 C  CD2 . TRP B 1 375 ? 116.815 -30.280 58.333  1.00 13.36 ? 377  TRP B CD2 1 
ATOM   6164 N  NE1 . TRP B 1 375 ? 117.452 -32.136 59.419  1.00 13.84 ? 377  TRP B NE1 1 
ATOM   6165 C  CE2 . TRP B 1 375 ? 117.891 -31.164 58.558  1.00 13.59 ? 377  TRP B CE2 1 
ATOM   6166 C  CE3 . TRP B 1 375 ? 117.009 -29.184 57.487  1.00 12.93 ? 377  TRP B CE3 1 
ATOM   6167 C  CZ2 . TRP B 1 375 ? 119.143 -30.980 57.973  1.00 13.56 ? 377  TRP B CZ2 1 
ATOM   6168 C  CZ3 . TRP B 1 375 ? 118.248 -29.008 56.899  1.00 13.06 ? 377  TRP B CZ3 1 
ATOM   6169 C  CH2 . TRP B 1 375 ? 119.298 -29.905 57.141  1.00 13.26 ? 377  TRP B CH2 1 
ATOM   6170 N  N   . ALA B 1 376 ? 111.398 -29.612 59.406  1.00 12.68 ? 378  ALA B N   1 
ATOM   6171 C  CA  . ALA B 1 376 ? 110.265 -28.718 59.641  1.00 13.38 ? 378  ALA B CA  1 
ATOM   6172 C  C   . ALA B 1 376 ? 109.160 -29.375 60.471  1.00 13.53 ? 378  ALA B C   1 
ATOM   6173 O  O   . ALA B 1 376 ? 108.640 -28.774 61.409  1.00 15.42 ? 378  ALA B O   1 
ATOM   6174 C  CB  . ALA B 1 376 ? 109.704 -28.211 58.322  1.00 13.03 ? 378  ALA B CB  1 
ATOM   6175 N  N   . ASP B 1 377 ? 108.800 -30.604 60.110  1.00 14.10 ? 379  ASP B N   1 
ATOM   6176 C  CA  . ASP B 1 377 ? 107.684 -31.303 60.741  1.00 14.94 ? 379  ASP B CA  1 
ATOM   6177 C  C   . ASP B 1 377 ? 108.107 -31.999 62.033  1.00 15.39 ? 379  ASP B C   1 
ATOM   6178 O  O   . ASP B 1 377 ? 107.322 -32.730 62.639  1.00 16.06 ? 379  ASP B O   1 
ATOM   6179 C  CB  . ASP B 1 377 ? 107.091 -32.338 59.781  1.00 14.98 ? 379  ASP B CB  1 
ATOM   6180 C  CG  . ASP B 1 377 ? 106.310 -31.705 58.645  1.00 15.34 ? 379  ASP B CG  1 
ATOM   6181 O  OD1 . ASP B 1 377 ? 106.319 -30.462 58.530  1.00 14.72 ? 379  ASP B OD1 1 
ATOM   6182 O  OD2 . ASP B 1 377 ? 105.701 -32.459 57.856  1.00 16.22 ? 379  ASP B OD2 1 
ATOM   6183 N  N   . ASN B 1 378 ? 109.361 -31.802 62.424  1.00 15.27 ? 380  ASN B N   1 
ATOM   6184 C  CA  . ASN B 1 378 ? 109.958 -32.563 63.518  1.00 15.78 ? 380  ASN B CA  1 
ATOM   6185 C  C   . ASN B 1 378 ? 110.089 -31.720 64.781  1.00 15.99 ? 380  ASN B C   1 
ATOM   6186 O  O   . ASN B 1 378 ? 110.920 -30.815 64.847  1.00 15.41 ? 380  ASN B O   1 
ATOM   6187 C  CB  . ASN B 1 378 ? 111.329 -33.099 63.092  1.00 15.56 ? 380  ASN B CB  1 
ATOM   6188 C  CG  . ASN B 1 378 ? 111.923 -34.064 64.101  1.00 16.59 ? 380  ASN B CG  1 
ATOM   6189 O  OD1 . ASN B 1 378 ? 111.422 -34.203 65.217  1.00 16.59 ? 380  ASN B OD1 1 
ATOM   6190 N  ND2 . ASN B 1 378 ? 113.016 -34.717 63.720  1.00 14.29 ? 380  ASN B ND2 1 
ATOM   6191 N  N   . ALA B 1 379 ? 109.265 -32.023 65.781  1.00 16.85 ? 381  ALA B N   1 
ATOM   6192 C  CA  . ALA B 1 379 ? 109.200 -31.222 67.003  1.00 16.79 ? 381  ALA B CA  1 
ATOM   6193 C  C   . ALA B 1 379 ? 110.506 -31.258 67.787  1.00 18.26 ? 381  ALA B C   1 
ATOM   6194 O  O   . ALA B 1 379 ? 110.734 -30.433 68.674  1.00 18.74 ? 381  ALA B O   1 
ATOM   6195 C  CB  . ALA B 1 379 ? 108.046 -31.685 67.881  1.00 17.84 ? 381  ALA B CB  1 
ATOM   6196 N  N   . ASN B 1 380 ? 111.358 -32.224 67.467  1.00 18.75 ? 382  ASN B N   1 
ATOM   6197 C  CA  . ASN B 1 380 ? 112.599 -32.418 68.207  1.00 19.48 ? 382  ASN B CA  1 
ATOM   6198 C  C   . ASN B 1 380 ? 113.837 -32.091 67.384  1.00 19.43 ? 382  ASN B C   1 
ATOM   6199 O  O   . ASN B 1 380 ? 114.936 -32.570 67.676  1.00 19.32 ? 382  ASN B O   1 
ATOM   6200 C  CB  . ASN B 1 380 ? 112.669 -33.845 68.737  1.00 21.44 ? 382  ASN B CB  1 
ATOM   6201 C  CG  . ASN B 1 380 ? 111.480 -34.192 69.606  1.00 21.47 ? 382  ASN B CG  1 
ATOM   6202 O  OD1 . ASN B 1 380 ? 110.702 -35.087 69.283  1.00 22.83 ? 382  ASN B OD1 1 
ATOM   6203 N  ND2 . ASN B 1 380 ? 111.299 -33.437 70.684  1.00 21.56 ? 382  ASN B ND2 1 
ATOM   6204 N  N   . PHE B 1 381 ? 113.645 -31.283 66.346  1.00 17.40 ? 383  PHE B N   1 
ATOM   6205 C  CA  . PHE B 1 381 ? 114.750 -30.748 65.560  1.00 17.08 ? 383  PHE B CA  1 
ATOM   6206 C  C   . PHE B 1 381 ? 114.745 -29.222 65.645  1.00 16.81 ? 383  PHE B C   1 
ATOM   6207 O  O   . PHE B 1 381 ? 113.689 -28.601 65.549  1.00 17.94 ? 383  PHE B O   1 
ATOM   6208 C  CB  . PHE B 1 381 ? 114.630 -31.194 64.098  1.00 16.05 ? 383  PHE B CB  1 
ATOM   6209 C  CG  . PHE B 1 381 ? 115.795 -30.781 63.248  1.00 16.39 ? 383  PHE B CG  1 
ATOM   6210 C  CD1 . PHE B 1 381 ? 116.922 -31.581 63.164  1.00 15.92 ? 383  PHE B CD1 1 
ATOM   6211 C  CD2 . PHE B 1 381 ? 115.809 -29.541 62.627  1.00 16.97 ? 383  PHE B CD2 1 
ATOM   6212 C  CE1 . PHE B 1 381 ? 118.026 -31.175 62.441  1.00 16.17 ? 383  PHE B CE1 1 
ATOM   6213 C  CE2 . PHE B 1 381 ? 116.908 -29.130 61.895  1.00 16.48 ? 383  PHE B CE2 1 
ATOM   6214 C  CZ  . PHE B 1 381 ? 118.020 -29.949 61.804  1.00 16.16 ? 383  PHE B CZ  1 
ATOM   6215 N  N   . PRO B 1 382 ? 115.917 -28.617 65.819  1.00 16.77 ? 384  PRO B N   1 
ATOM   6216 C  CA  . PRO B 1 382 ? 117.190 -29.334 65.804  1.00 17.22 ? 384  PRO B CA  1 
ATOM   6217 C  C   . PRO B 1 382 ? 117.479 -30.060 67.117  1.00 18.57 ? 384  PRO B C   1 
ATOM   6218 O  O   . PRO B 1 382 ? 116.783 -29.842 68.109  1.00 18.85 ? 384  PRO B O   1 
ATOM   6219 C  CB  . PRO B 1 382 ? 118.213 -28.215 65.595  1.00 17.74 ? 384  PRO B CB  1 
ATOM   6220 C  CG  . PRO B 1 382 ? 117.551 -26.993 66.135  1.00 17.52 ? 384  PRO B CG  1 
ATOM   6221 C  CD  . PRO B 1 382 ? 116.102 -27.157 65.783  1.00 16.60 ? 384  PRO B CD  1 
ATOM   6222 N  N   . PRO B 1 383 ? 118.519 -30.908 67.124  1.00 19.43 ? 385  PRO B N   1 
ATOM   6223 C  CA  . PRO B 1 383 ? 118.907 -31.699 68.286  1.00 19.81 ? 385  PRO B CA  1 
ATOM   6224 C  C   . PRO B 1 383 ? 119.734 -30.889 69.278  1.00 21.01 ? 385  PRO B C   1 
ATOM   6225 O  O   . PRO B 1 383 ? 120.295 -29.851 68.919  1.00 21.05 ? 385  PRO B O   1 
ATOM   6226 C  CB  . PRO B 1 383 ? 119.771 -32.803 67.674  1.00 20.09 ? 385  PRO B CB  1 
ATOM   6227 C  CG  . PRO B 1 383 ? 120.397 -32.154 66.486  1.00 19.70 ? 385  PRO B CG  1 
ATOM   6228 C  CD  . PRO B 1 383 ? 119.367 -31.191 65.952  1.00 19.60 ? 385  PRO B CD  1 
ATOM   6229 N  N   . GLY B 1 384 ? 119.812 -31.367 70.516  1.00 22.26 ? 386  GLY B N   1 
ATOM   6230 C  CA  . GLY B 1 384 ? 120.764 -30.832 71.487  1.00 21.11 ? 386  GLY B CA  1 
ATOM   6231 C  C   . GLY B 1 384 ? 120.372 -29.491 72.077  1.00 21.87 ? 386  GLY B C   1 
ATOM   6232 O  O   . GLY B 1 384 ? 121.214 -28.773 72.623  1.00 19.97 ? 386  GLY B O   1 
ATOM   6233 N  N   . LYS B 1 385 ? 119.088 -29.157 71.990  1.00 21.33 ? 387  LYS B N   1 
ATOM   6234 C  CA  . LYS B 1 385 ? 118.599 -27.890 72.524  1.00 21.40 ? 387  LYS B CA  1 
ATOM   6235 C  C   . LYS B 1 385 ? 117.964 -28.056 73.906  1.00 21.63 ? 387  LYS B C   1 
ATOM   6236 O  O   . LYS B 1 385 ? 117.616 -29.162 74.315  1.00 21.39 ? 387  LYS B O   1 
ATOM   6237 C  CB  . LYS B 1 385 ? 117.610 -27.236 71.553  1.00 20.58 ? 387  LYS B CB  1 
ATOM   6238 C  CG  . LYS B 1 385 ? 118.180 -26.973 70.166  1.00 19.70 ? 387  LYS B CG  1 
ATOM   6239 C  CD  . LYS B 1 385 ? 119.430 -26.107 70.226  1.00 19.09 ? 387  LYS B CD  1 
ATOM   6240 C  CE  . LYS B 1 385 ? 119.910 -25.728 68.833  1.00 17.61 ? 387  LYS B CE  1 
ATOM   6241 N  NZ  . LYS B 1 385 ? 121.144 -24.894 68.866  1.00 16.34 ? 387  LYS B NZ  1 
ATOM   6242 N  N   . THR B 1 386 ? 117.853 -26.950 74.633  1.00 23.44 ? 388  THR B N   1 
ATOM   6243 C  CA  . THR B 1 386 ? 117.146 -26.941 75.909  1.00 26.45 ? 388  THR B CA  1 
ATOM   6244 C  C   . THR B 1 386 ? 116.273 -25.696 75.990  1.00 24.61 ? 388  THR B C   1 
ATOM   6245 O  O   . THR B 1 386 ? 116.767 -24.583 75.819  1.00 25.39 ? 388  THR B O   1 
ATOM   6246 C  CB  . THR B 1 386 ? 118.129 -26.943 77.100  1.00 28.29 ? 388  THR B CB  1 
ATOM   6247 O  OG1 . THR B 1 386 ? 118.820 -28.199 77.159  1.00 30.72 ? 388  THR B OG1 1 
ATOM   6248 C  CG2 . THR B 1 386 ? 117.378 -26.725 78.408  1.00 29.94 ? 388  THR B CG2 1 
ATOM   6249 N  N   . PRO B 1 387 ? 114.969 -25.879 76.190  1.00 24.97 ? 389  PRO B N   1 
ATOM   6250 C  CA  . PRO B 1 387 ? 114.346 -27.204 76.280  1.00 25.87 ? 389  PRO B CA  1 
ATOM   6251 C  C   . PRO B 1 387 ? 114.464 -28.015 74.989  1.00 25.90 ? 389  PRO B C   1 
ATOM   6252 O  O   . PRO B 1 387 ? 114.538 -27.442 73.902  1.00 27.76 ? 389  PRO B O   1 
ATOM   6253 C  CB  . PRO B 1 387 ? 112.869 -26.880 76.544  1.00 25.67 ? 389  PRO B CB  1 
ATOM   6254 C  CG  . PRO B 1 387 ? 112.855 -25.481 77.058  1.00 24.40 ? 389  PRO B CG  1 
ATOM   6255 C  CD  . PRO B 1 387 ? 113.996 -24.792 76.378  1.00 25.14 ? 389  PRO B CD  1 
ATOM   6256 N  N   . ALA B 1 388 ? 114.398 -29.338 75.114  1.00 26.13 ? 390  ALA B N   1 
ATOM   6257 C  CA  . ALA B 1 388 ? 114.650 -30.239 73.994  1.00 25.00 ? 390  ALA B CA  1 
ATOM   6258 C  C   . ALA B 1 388 ? 113.603 -30.108 72.891  1.00 25.92 ? 390  ALA B C   1 
ATOM   6259 O  O   . ALA B 1 388 ? 113.933 -30.124 71.705  1.00 24.04 ? 390  ALA B O   1 
ATOM   6260 C  CB  . ALA B 1 388 ? 114.732 -31.677 74.478  1.00 25.03 ? 390  ALA B CB  1 
ATOM   6261 N  N   . THR B 1 389 ? 112.339 -29.993 73.283  1.00 26.43 ? 391  THR B N   1 
ATOM   6262 C  CA  . THR B 1 389 ? 111.257 -29.884 72.311  1.00 25.15 ? 391  THR B CA  1 
ATOM   6263 C  C   . THR B 1 389 ? 111.219 -28.504 71.666  1.00 24.14 ? 391  THR B C   1 
ATOM   6264 O  O   . THR B 1 389 ? 110.816 -27.520 72.288  1.00 23.76 ? 391  THR B O   1 
ATOM   6265 C  CB  . THR B 1 389 ? 109.890 -30.220 72.932  1.00 25.73 ? 391  THR B CB  1 
ATOM   6266 O  OG1 . THR B 1 389 ? 109.872 -31.599 73.313  1.00 25.04 ? 391  THR B OG1 1 
ATOM   6267 C  CG2 . THR B 1 389 ? 108.776 -29.970 71.929  1.00 24.18 ? 391  THR B CG2 1 
ATOM   6268 N  N   . VAL B 1 390 ? 111.654 -28.443 70.413  1.00 21.76 ? 392  VAL B N   1 
ATOM   6269 C  CA  . VAL B 1 390 ? 111.687 -27.197 69.666  1.00 20.81 ? 392  VAL B CA  1 
ATOM   6270 C  C   . VAL B 1 390 ? 110.284 -26.793 69.216  1.00 19.48 ? 392  VAL B C   1 
ATOM   6271 O  O   . VAL B 1 390 ? 109.943 -25.611 69.200  1.00 19.29 ? 392  VAL B O   1 
ATOM   6272 C  CB  . VAL B 1 390 ? 112.602 -27.324 68.431  1.00 21.07 ? 392  VAL B CB  1 
ATOM   6273 C  CG1 . VAL B 1 390 ? 112.477 -26.099 67.540  1.00 19.96 ? 392  VAL B CG1 1 
ATOM   6274 C  CG2 . VAL B 1 390 ? 114.045 -27.533 68.867  1.00 22.49 ? 392  VAL B CG2 1 
ATOM   6275 N  N   . GLY B 1 391 ? 109.464 -27.785 68.886  1.00 19.65 ? 393  GLY B N   1 
ATOM   6276 C  CA  . GLY B 1 391 ? 108.197 -27.538 68.210  1.00 20.06 ? 393  GLY B CA  1 
ATOM   6277 C  C   . GLY B 1 391 ? 108.353 -27.583 66.700  1.00 19.65 ? 393  GLY B C   1 
ATOM   6278 O  O   . GLY B 1 391 ? 109.440 -27.860 66.188  1.00 17.94 ? 393  GLY B O   1 
ATOM   6279 N  N   . LEU B 1 392 ? 107.265 -27.310 65.987  1.00 18.16 ? 394  LEU B N   1 
ATOM   6280 C  CA  . LEU B 1 392 ? 107.269 -27.383 64.528  1.00 17.29 ? 394  LEU B CA  1 
ATOM   6281 C  C   . LEU B 1 392 ? 107.626 -26.040 63.891  1.00 16.30 ? 394  LEU B C   1 
ATOM   6282 O  O   . LEU B 1 392 ? 107.540 -24.991 64.533  1.00 16.58 ? 394  LEU B O   1 
ATOM   6283 C  CB  . LEU B 1 392 ? 105.910 -27.865 64.014  1.00 16.67 ? 394  LEU B CB  1 
ATOM   6284 C  CG  . LEU B 1 392 ? 105.398 -29.205 64.548  1.00 17.64 ? 394  LEU B CG  1 
ATOM   6285 C  CD1 . LEU B 1 392 ? 104.208 -29.688 63.735  1.00 18.59 ? 394  LEU B CD1 1 
ATOM   6286 C  CD2 . LEU B 1 392 ? 106.501 -30.251 64.560  1.00 16.65 ? 394  LEU B CD2 1 
ATOM   6287 N  N   . ASP B 1 393 ? 108.041 -26.085 62.628  1.00 15.62 ? 395  ASP B N   1 
ATOM   6288 C  CA  . ASP B 1 393 ? 108.185 -24.886 61.809  1.00 14.62 ? 395  ASP B CA  1 
ATOM   6289 C  C   . ASP B 1 393 ? 106.846 -24.153 61.750  1.00 14.35 ? 395  ASP B C   1 
ATOM   6290 O  O   . ASP B 1 393 ? 105.843 -24.733 61.349  1.00 14.60 ? 395  ASP B O   1 
ATOM   6291 C  CB  . ASP B 1 393 ? 108.628 -25.276 60.394  1.00 14.06 ? 395  ASP B CB  1 
ATOM   6292 C  CG  . ASP B 1 393 ? 109.000 -24.076 59.536  1.00 14.34 ? 395  ASP B CG  1 
ATOM   6293 O  OD1 . ASP B 1 393 ? 108.185 -23.136 59.421  1.00 14.78 ? 395  ASP B OD1 1 
ATOM   6294 O  OD2 . ASP B 1 393 ? 110.096 -24.094 58.935  1.00 14.77 ? 395  ASP B OD2 1 
ATOM   6295 N  N   . PRO B 1 394 ? 106.823 -22.881 62.176  1.00 14.01 ? 396  PRO B N   1 
ATOM   6296 C  CA  . PRO B 1 394 ? 105.561 -22.141 62.237  1.00 14.56 ? 396  PRO B CA  1 
ATOM   6297 C  C   . PRO B 1 394 ? 105.049 -21.752 60.850  1.00 15.49 ? 396  PRO B C   1 
ATOM   6298 O  O   . PRO B 1 394 ? 103.856 -21.489 60.679  1.00 17.02 ? 396  PRO B O   1 
ATOM   6299 C  CB  . PRO B 1 394 ? 105.927 -20.890 63.039  1.00 14.72 ? 396  PRO B CB  1 
ATOM   6300 C  CG  . PRO B 1 394 ? 107.383 -20.698 62.791  1.00 14.08 ? 396  PRO B CG  1 
ATOM   6301 C  CD  . PRO B 1 394 ? 107.966 -22.076 62.643  1.00 13.84 ? 396  PRO B CD  1 
ATOM   6302 N  N   . ILE B 1 395 ? 105.944 -21.726 59.869  1.00 15.50 ? 397  ILE B N   1 
ATOM   6303 C  CA  . ILE B 1 395 ? 105.564 -21.369 58.506  1.00 15.68 ? 397  ILE B CA  1 
ATOM   6304 C  C   . ILE B 1 395 ? 105.052 -22.576 57.724  1.00 15.40 ? 397  ILE B C   1 
ATOM   6305 O  O   . ILE B 1 395 ? 103.937 -22.551 57.205  1.00 17.65 ? 397  ILE B O   1 
ATOM   6306 C  CB  . ILE B 1 395 ? 106.714 -20.672 57.751  1.00 15.33 ? 397  ILE B CB  1 
ATOM   6307 C  CG1 . ILE B 1 395 ? 107.151 -19.407 58.498  1.00 15.64 ? 397  ILE B CG1 1 
ATOM   6308 C  CG2 . ILE B 1 395 ? 106.299 -20.335 56.324  1.00 15.67 ? 397  ILE B CG2 1 
ATOM   6309 C  CD1 . ILE B 1 395 ? 106.006 -18.498 58.896  1.00 15.71 ? 397  ILE B CD1 1 
ATOM   6310 N  N   . ILE B 1 396 ? 105.837 -23.649 57.686  1.00 15.42 ? 398  ILE B N   1 
ATOM   6311 C  CA  . ILE B 1 396 ? 105.514 -24.790 56.831  1.00 14.44 ? 398  ILE B CA  1 
ATOM   6312 C  C   . ILE B 1 396 ? 105.265 -26.084 57.598  1.00 14.20 ? 398  ILE B C   1 
ATOM   6313 O  O   . ILE B 1 396 ? 104.859 -27.084 57.011  1.00 14.22 ? 398  ILE B O   1 
ATOM   6314 C  CB  . ILE B 1 396 ? 106.606 -25.041 55.770  1.00 14.57 ? 398  ILE B CB  1 
ATOM   6315 C  CG1 . ILE B 1 396 ? 107.951 -25.340 56.440  1.00 14.17 ? 398  ILE B CG1 1 
ATOM   6316 C  CG2 . ILE B 1 396 ? 106.716 -23.854 54.826  1.00 13.77 ? 398  ILE B CG2 1 
ATOM   6317 C  CD1 . ILE B 1 396 ? 108.944 -26.024 55.523  1.00 14.49 ? 398  ILE B CD1 1 
ATOM   6318 N  N   . GLY B 1 397 ? 105.491 -26.060 58.908  1.00 14.13 ? 399  GLY B N   1 
ATOM   6319 C  CA  . GLY B 1 397 ? 105.279 -27.244 59.736  1.00 13.99 ? 399  GLY B CA  1 
ATOM   6320 C  C   . GLY B 1 397 ? 103.869 -27.795 59.641  1.00 14.80 ? 399  GLY B C   1 
ATOM   6321 O  O   . GLY B 1 397 ? 102.892 -27.058 59.786  1.00 15.44 ? 399  GLY B O   1 
ATOM   6322 N  N   . GLN B 1 398 ? 103.763 -29.101 59.413  1.00 15.01 ? 400  GLN B N   1 
ATOM   6323 C  CA  . GLN B 1 398 ? 102.467 -29.752 59.261  1.00 16.28 ? 400  GLN B CA  1 
ATOM   6324 C  C   . GLN B 1 398 ? 102.257 -30.882 60.267  1.00 18.08 ? 400  GLN B C   1 
ATOM   6325 O  O   . GLN B 1 398 ? 103.203 -31.572 60.652  1.00 16.87 ? 400  GLN B O   1 
ATOM   6326 C  CB  . GLN B 1 398 ? 102.290 -30.273 57.832  1.00 16.01 ? 400  GLN B CB  1 
ATOM   6327 C  CG  . GLN B 1 398 ? 102.155 -29.164 56.801  1.00 16.82 ? 400  GLN B CG  1 
ATOM   6328 C  CD  . GLN B 1 398 ? 101.810 -29.674 55.417  1.00 17.72 ? 400  GLN B CD  1 
ATOM   6329 O  OE1 . GLN B 1 398 ? 101.316 -28.925 54.578  1.00 19.44 ? 400  GLN B OE1 1 
ATOM   6330 N  NE2 . GLN B 1 398 ? 102.063 -30.953 55.172  1.00 17.34 ? 400  GLN B NE2 1 
ATOM   6331 N  N   . ASN B 1 399 ? 101.007 -31.063 60.684  1.00 18.40 ? 401  ASN B N   1 
ATOM   6332 C  CA  . ASN B 1 399 ? 100.636 -32.159 61.571  1.00 21.06 ? 401  ASN B CA  1 
ATOM   6333 C  C   . ASN B 1 399 ? 99.206  -32.625 61.315  1.00 22.11 ? 401  ASN B C   1 
ATOM   6334 O  O   . ASN B 1 399 ? 98.332  -32.499 62.175  1.00 21.31 ? 401  ASN B O   1 
ATOM   6335 C  CB  . ASN B 1 399 ? 100.813 -31.746 63.035  1.00 21.92 ? 401  ASN B CB  1 
ATOM   6336 C  CG  . ASN B 1 399 ? 100.666 -32.914 63.993  1.00 23.61 ? 401  ASN B CG  1 
ATOM   6337 O  OD1 . ASN B 1 399 ? 100.939 -34.064 63.642  1.00 22.81 ? 401  ASN B OD1 1 
ATOM   6338 N  ND2 . ASN B 1 399 ? 100.246 -32.621 65.218  1.00 25.17 ? 401  ASN B ND2 1 
ATOM   6339 N  N   . ASN B 1 400 ? 98.969  -33.131 60.109  1.00 21.48 ? 402  ASN B N   1 
ATOM   6340 C  CA  . ASN B 1 400 ? 97.653  -33.620 59.718  1.00 23.70 ? 402  ASN B CA  1 
ATOM   6341 C  C   . ASN B 1 400 ? 96.555  -32.573 59.884  1.00 24.07 ? 402  ASN B C   1 
ATOM   6342 O  O   . ASN B 1 400 ? 95.421  -32.899 60.229  1.00 24.37 ? 402  ASN B O   1 
ATOM   6343 C  CB  . ASN B 1 400 ? 97.304  -34.897 60.486  1.00 23.41 ? 402  ASN B CB  1 
ATOM   6344 C  CG  . ASN B 1 400 ? 98.237  -36.047 60.154  1.00 25.05 ? 402  ASN B CG  1 
ATOM   6345 O  OD1 . ASN B 1 400 ? 98.308  -36.491 59.008  1.00 24.07 ? 402  ASN B OD1 1 
ATOM   6346 N  ND2 . ASN B 1 400 ? 98.969  -36.526 61.155  1.00 25.51 ? 402  ASN B ND2 1 
ATOM   6347 N  N   . GLY B 1 401 ? 96.902  -31.314 59.636  1.00 23.81 ? 403  GLY B N   1 
ATOM   6348 C  CA  . GLY B 1 401 ? 95.918  -30.238 59.599  1.00 23.43 ? 403  GLY B CA  1 
ATOM   6349 C  C   . GLY B 1 401 ? 95.609  -29.662 60.968  1.00 24.81 ? 403  GLY B C   1 
ATOM   6350 O  O   . GLY B 1 401 ? 94.877  -28.678 61.084  1.00 25.45 ? 403  GLY B O   1 
ATOM   6351 N  N   . GLN B 1 402 ? 96.176  -30.271 62.007  1.00 23.93 ? 404  GLN B N   1 
ATOM   6352 C  CA  . GLN B 1 402 ? 96.026  -29.773 63.373  1.00 26.18 ? 404  GLN B CA  1 
ATOM   6353 C  C   . GLN B 1 402 ? 96.836  -28.498 63.593  1.00 24.55 ? 404  GLN B C   1 
ATOM   6354 O  O   . GLN B 1 402 ? 97.815  -28.248 62.889  1.00 24.24 ? 404  GLN B O   1 
ATOM   6355 C  CB  . GLN B 1 402 ? 96.457  -30.841 64.383  1.00 27.28 ? 404  GLN B CB  1 
ATOM   6356 C  CG  . GLN B 1 402 ? 95.662  -32.132 64.298  1.00 28.92 ? 404  GLN B CG  1 
ATOM   6357 C  CD  . GLN B 1 402 ? 94.206  -31.940 64.672  1.00 32.48 ? 404  GLN B CD  1 
ATOM   6358 O  OE1 . GLN B 1 402 ? 93.866  -31.824 65.850  1.00 36.76 ? 404  GLN B OE1 1 
ATOM   6359 N  NE2 . GLN B 1 402 ? 93.337  -31.897 63.668  1.00 34.26 ? 404  GLN B NE2 1 
ATOM   6360 N  N   . PRO B 1 403 ? 96.441  -27.696 64.593  1.00 23.65 ? 405  PRO B N   1 
ATOM   6361 C  CA  . PRO B 1 403 ? 97.275  -26.589 65.058  1.00 23.19 ? 405  PRO B CA  1 
ATOM   6362 C  C   . PRO B 1 403 ? 98.678  -27.067 65.439  1.00 22.50 ? 405  PRO B C   1 
ATOM   6363 O  O   . PRO B 1 403 ? 98.830  -28.153 65.994  1.00 23.92 ? 405  PRO B O   1 
ATOM   6364 C  CB  . PRO B 1 403 ? 96.533  -26.088 66.303  1.00 24.85 ? 405  PRO B CB  1 
ATOM   6365 C  CG  . PRO B 1 403 ? 95.125  -26.538 66.117  1.00 25.38 ? 405  PRO B CG  1 
ATOM   6366 C  CD  . PRO B 1 403 ? 95.220  -27.853 65.402  1.00 24.44 ? 405  PRO B CD  1 
ATOM   6367 N  N   . ARG B 1 404 ? 99.688  -26.263 65.121  1.00 20.53 ? 406  ARG B N   1 
ATOM   6368 C  CA  . ARG B 1 404 ? 101.081 -26.635 65.350  1.00 19.96 ? 406  ARG B CA  1 
ATOM   6369 C  C   . ARG B 1 404 ? 101.578 -26.059 66.671  1.00 19.49 ? 406  ARG B C   1 
ATOM   6370 O  O   . ARG B 1 404 ? 101.460 -24.858 66.915  1.00 19.70 ? 406  ARG B O   1 
ATOM   6371 C  CB  . ARG B 1 404 ? 101.964 -26.122 64.208  1.00 19.58 ? 406  ARG B CB  1 
ATOM   6372 C  CG  . ARG B 1 404 ? 101.786 -26.856 62.885  1.00 18.07 ? 406  ARG B CG  1 
ATOM   6373 C  CD  . ARG B 1 404 ? 100.708 -26.220 62.017  1.00 18.29 ? 406  ARG B CD  1 
ATOM   6374 N  NE  . ARG B 1 404 ? 100.711 -24.760 62.099  1.00 17.27 ? 406  ARG B NE  1 
ATOM   6375 C  CZ  . ARG B 1 404 ? 101.621 -23.976 61.529  1.00 17.03 ? 406  ARG B CZ  1 
ATOM   6376 N  NH1 . ARG B 1 404 ? 102.618 -24.505 60.832  1.00 16.80 ? 406  ARG B NH1 1 
ATOM   6377 N  NH2 . ARG B 1 404 ? 101.542 -22.658 61.666  1.00 16.89 ? 406  ARG B NH2 1 
ATOM   6378 N  N   . VAL B 1 405 ? 102.144 -26.914 67.515  1.00 19.97 ? 407  VAL B N   1 
ATOM   6379 C  CA  . VAL B 1 405 ? 102.791 -26.452 68.737  1.00 19.63 ? 407  VAL B CA  1 
ATOM   6380 C  C   . VAL B 1 405 ? 104.223 -26.014 68.450  1.00 20.24 ? 407  VAL B C   1 
ATOM   6381 O  O   . VAL B 1 405 ? 105.040 -26.803 67.974  1.00 21.39 ? 407  VAL B O   1 
ATOM   6382 C  CB  . VAL B 1 405 ? 102.779 -27.533 69.836  1.00 20.34 ? 407  VAL B CB  1 
ATOM   6383 C  CG1 . VAL B 1 405 ? 103.508 -27.038 71.079  1.00 20.03 ? 407  VAL B CG1 1 
ATOM   6384 C  CG2 . VAL B 1 405 ? 101.346 -27.918 70.175  1.00 20.92 ? 407  VAL B CG2 1 
ATOM   6385 N  N   . VAL B 1 406 ? 104.508 -24.742 68.713  1.00 19.47 ? 408  VAL B N   1 
ATOM   6386 C  CA  . VAL B 1 406 ? 105.800 -24.153 68.389  1.00 19.96 ? 408  VAL B CA  1 
ATOM   6387 C  C   . VAL B 1 406 ? 106.369 -23.438 69.612  1.00 21.79 ? 408  VAL B C   1 
ATOM   6388 O  O   . VAL B 1 406 ? 105.698 -22.599 70.215  1.00 20.82 ? 408  VAL B O   1 
ATOM   6389 C  CB  . VAL B 1 406 ? 105.674 -23.136 67.235  1.00 19.87 ? 408  VAL B CB  1 
ATOM   6390 C  CG1 . VAL B 1 406 ? 107.040 -22.589 66.854  1.00 18.52 ? 408  VAL B CG1 1 
ATOM   6391 C  CG2 . VAL B 1 406 ? 104.996 -23.778 66.033  1.00 19.25 ? 408  VAL B CG2 1 
ATOM   6392 N  N   . ASN B 1 407 ? 107.606 -23.769 69.975  1.00 21.27 ? 409  ASN B N   1 
ATOM   6393 C  CA  . ASN B 1 407 ? 108.244 -23.176 71.149  1.00 22.40 ? 409  ASN B CA  1 
ATOM   6394 C  C   . ASN B 1 407 ? 109.356 -22.189 70.794  1.00 22.64 ? 409  ASN B C   1 
ATOM   6395 O  O   . ASN B 1 407 ? 109.921 -22.238 69.699  1.00 21.80 ? 409  ASN B O   1 
ATOM   6396 C  CB  . ASN B 1 407 ? 108.789 -24.270 72.078  1.00 22.92 ? 409  ASN B CB  1 
ATOM   6397 C  CG  . ASN B 1 407 ? 107.737 -25.296 72.452  1.00 23.93 ? 409  ASN B CG  1 
ATOM   6398 O  OD1 . ASN B 1 407 ? 108.019 -26.491 72.532  1.00 24.36 ? 409  ASN B OD1 1 
ATOM   6399 N  ND2 . ASN B 1 407 ? 106.512 -24.836 72.663  1.00 24.12 ? 409  ASN B ND2 1 
ATOM   6400 N  N   . GLY B 1 408 ? 109.658 -21.285 71.723  1.00 22.56 ? 410  GLY B N   1 
ATOM   6401 C  CA  . GLY B 1 408 ? 110.832 -20.424 71.605  1.00 20.93 ? 410  GLY B CA  1 
ATOM   6402 C  C   . GLY B 1 408 ? 110.567 -19.072 70.966  1.00 20.65 ? 410  GLY B C   1 
ATOM   6403 O  O   . GLY B 1 408 ? 111.445 -18.210 70.941  1.00 19.81 ? 410  GLY B O   1 
ATOM   6404 N  N   . LEU B 1 409 ? 109.355 -18.880 70.452  1.00 21.51 ? 411  LEU B N   1 
ATOM   6405 C  CA  . LEU B 1 409 ? 109.035 -17.680 69.676  1.00 21.35 ? 411  LEU B CA  1 
ATOM   6406 C  C   . LEU B 1 409 ? 109.015 -16.412 70.530  1.00 23.32 ? 411  LEU B C   1 
ATOM   6407 O  O   . LEU B 1 409 ? 109.319 -15.321 70.045  1.00 23.12 ? 411  LEU B O   1 
ATOM   6408 C  CB  . LEU B 1 409 ? 107.695 -17.848 68.957  1.00 20.34 ? 411  LEU B CB  1 
ATOM   6409 C  CG  . LEU B 1 409 ? 107.639 -18.944 67.892  1.00 19.57 ? 411  LEU B CG  1 
ATOM   6410 C  CD1 . LEU B 1 409 ? 106.223 -19.088 67.356  1.00 19.07 ? 411  LEU B CD1 1 
ATOM   6411 C  CD2 . LEU B 1 409 ? 108.620 -18.648 66.767  1.00 19.61 ? 411  LEU B CD2 1 
ATOM   6412 N  N   . LEU B 1 410 ? 108.656 -16.565 71.800  1.00 26.04 ? 412  LEU B N   1 
ATOM   6413 C  CA  . LEU B 1 410 ? 108.527 -15.429 72.707  1.00 29.34 ? 412  LEU B CA  1 
ATOM   6414 C  C   . LEU B 1 410 ? 109.814 -15.210 73.496  1.00 30.40 ? 412  LEU B C   1 
ATOM   6415 O  O   . LEU B 1 410 ? 110.192 -16.042 74.319  1.00 29.94 ? 412  LEU B O   1 
ATOM   6416 C  CB  . LEU B 1 410 ? 107.347 -15.640 73.658  1.00 31.36 ? 412  LEU B CB  1 
ATOM   6417 C  CG  . LEU B 1 410 ? 106.024 -15.992 72.972  1.00 31.70 ? 412  LEU B CG  1 
ATOM   6418 C  CD1 . LEU B 1 410 ? 105.029 -16.582 73.961  1.00 34.20 ? 412  LEU B CD1 1 
ATOM   6419 C  CD2 . LEU B 1 410 ? 105.443 -14.773 72.272  1.00 31.56 ? 412  LEU B CD2 1 
ATOM   6420 N  N   . PRO B 1 411 ? 110.480 -14.073 73.248  1.00 29.16 ? 413  PRO B N   1 
ATOM   6421 C  CA  . PRO B 1 411 ? 111.872 -13.811 73.613  1.00 32.45 ? 413  PRO B CA  1 
ATOM   6422 C  C   . PRO B 1 411 ? 112.163 -13.851 75.115  1.00 35.41 ? 413  PRO B C   1 
ATOM   6423 O  O   . PRO B 1 411 ? 113.322 -13.730 75.513  1.00 36.92 ? 413  PRO B O   1 
ATOM   6424 C  CB  . PRO B 1 411 ? 112.113 -12.398 73.076  1.00 31.19 ? 413  PRO B CB  1 
ATOM   6425 C  CG  . PRO B 1 411 ? 111.147 -12.256 71.950  1.00 30.19 ? 413  PRO B CG  1 
ATOM   6426 C  CD  . PRO B 1 411 ? 109.929 -13.017 72.380  1.00 28.36 ? 413  PRO B CD  1 
ATOM   6427 N  N   . SER B 1 412 ? 111.134 -14.023 75.938  1.00 33.98 ? 414  SER B N   1 
ATOM   6428 C  CA  . SER B 1 412 ? 111.298 -13.872 77.381  1.00 36.97 ? 414  SER B CA  1 
ATOM   6429 C  C   . SER B 1 412 ? 110.829 -15.092 78.173  1.00 38.03 ? 414  SER B C   1 
ATOM   6430 O  O   . SER B 1 412 ? 110.821 -15.077 79.404  1.00 37.75 ? 414  SER B O   1 
ATOM   6431 C  CB  . SER B 1 412 ? 110.591 -12.607 77.875  1.00 39.42 ? 414  SER B CB  1 
ATOM   6432 O  OG  . SER B 1 412 ? 109.195 -12.679 77.647  1.00 36.35 ? 414  SER B OG  1 
ATOM   6433 N  N   . ASN B 1 413 ? 110.436 -16.144 77.462  1.00 34.81 ? 415  ASN B N   1 
ATOM   6434 C  CA  . ASN B 1 413 ? 110.264 -17.461 78.068  1.00 35.26 ? 415  ASN B CA  1 
ATOM   6435 C  C   . ASN B 1 413 ? 110.333 -18.557 77.010  1.00 32.86 ? 415  ASN B C   1 
ATOM   6436 O  O   . ASN B 1 413 ? 109.306 -19.065 76.554  1.00 29.39 ? 415  ASN B O   1 
ATOM   6437 C  CB  . ASN B 1 413 ? 108.944 -17.540 78.846  1.00 35.16 ? 415  ASN B CB  1 
ATOM   6438 C  CG  . ASN B 1 413 ? 108.772 -18.862 79.575  1.00 36.77 ? 415  ASN B CG  1 
ATOM   6439 O  OD1 . ASN B 1 413 ? 109.647 -19.727 79.532  1.00 37.00 ? 415  ASN B OD1 1 
ATOM   6440 N  ND2 . ASN B 1 413 ? 107.636 -19.026 80.248  1.00 36.69 ? 415  ASN B ND2 1 
ATOM   6441 N  N   . SER B 1 414 ? 111.553 -18.906 76.616  1.00 30.40 ? 416  SER B N   1 
ATOM   6442 C  CA  . SER B 1 414 ? 111.770 -19.869 75.544  1.00 28.31 ? 416  SER B CA  1 
ATOM   6443 C  C   . SER B 1 414 ? 110.979 -21.144 75.785  1.00 28.98 ? 416  SER B C   1 
ATOM   6444 O  O   . SER B 1 414 ? 110.812 -21.962 74.881  1.00 27.84 ? 416  SER B O   1 
ATOM   6445 C  CB  . SER B 1 414 ? 113.259 -20.190 75.403  1.00 29.97 ? 416  SER B CB  1 
ATOM   6446 O  OG  . SER B 1 414 ? 113.723 -20.961 76.497  1.00 31.84 ? 416  SER B OG  1 
ATOM   6447 N  N   . SER B 1 415 ? 110.480 -21.299 77.008  1.00 29.74 ? 417  SER B N   1 
ATOM   6448 C  CA  . SER B 1 415 ? 109.621 -22.424 77.355  1.00 28.85 ? 417  SER B CA  1 
ATOM   6449 C  C   . SER B 1 415 ? 108.172 -22.180 76.937  1.00 27.78 ? 417  SER B C   1 
ATOM   6450 O  O   . SER B 1 415 ? 107.378 -23.117 76.844  1.00 28.56 ? 417  SER B O   1 
ATOM   6451 C  CB  . SER B 1 415 ? 109.696 -22.709 78.857  1.00 30.86 ? 417  SER B CB  1 
ATOM   6452 O  OG  . SER B 1 415 ? 110.649 -23.719 79.138  1.00 30.29 ? 417  SER B OG  1 
ATOM   6453 N  N   . ALA B 1 416 ? 107.835 -20.920 76.679  1.00 27.16 ? 418  ALA B N   1 
ATOM   6454 C  CA  . ALA B 1 416 ? 106.471 -20.552 76.314  1.00 26.95 ? 418  ALA B CA  1 
ATOM   6455 C  C   . ALA B 1 416 ? 106.087 -21.112 74.946  1.00 28.14 ? 418  ALA B C   1 
ATOM   6456 O  O   . ALA B 1 416 ? 106.749 -20.836 73.947  1.00 28.75 ? 418  ALA B O   1 
ATOM   6457 C  CB  . ALA B 1 416 ? 106.312 -19.041 76.333  1.00 26.44 ? 418  ALA B CB  1 
ATOM   6458 N  N   . SER B 1 417 ? 105.024 -21.910 74.914  1.00 29.68 ? 419  SER B N   1 
ATOM   6459 C  CA  . SER B 1 417 ? 104.559 -22.527 73.676  1.00 30.54 ? 419  SER B CA  1 
ATOM   6460 C  C   . SER B 1 417 ? 103.446 -21.711 73.032  1.00 31.76 ? 419  SER B C   1 
ATOM   6461 O  O   . SER B 1 417 ? 102.709 -20.996 73.715  1.00 32.00 ? 419  SER B O   1 
ATOM   6462 C  CB  . SER B 1 417 ? 104.061 -23.949 73.937  1.00 30.28 ? 419  SER B CB  1 
ATOM   6463 O  OG  . SER B 1 417 ? 105.053 -24.729 74.578  1.00 35.93 ? 419  SER B OG  1 
ATOM   6464 N  N   . LEU B 1 418 ? 103.329 -21.822 71.713  1.00 29.78 ? 420  LEU B N   1 
ATOM   6465 C  CA  . LEU B 1 418 ? 102.132 -21.372 71.011  1.00 28.24 ? 420  LEU B CA  1 
ATOM   6466 C  C   . LEU B 1 418 ? 101.526 -22.505 70.196  1.00 27.69 ? 420  LEU B C   1 
ATOM   6467 O  O   . LEU B 1 418 ? 102.245 -23.314 69.606  1.00 24.69 ? 420  LEU B O   1 
ATOM   6468 C  CB  . LEU B 1 418 ? 102.450 -20.185 70.102  1.00 28.65 ? 420  LEU B CB  1 
ATOM   6469 C  CG  . LEU B 1 418 ? 102.714 -18.845 70.790  1.00 29.31 ? 420  LEU B CG  1 
ATOM   6470 C  CD1 . LEU B 1 418 ? 103.171 -17.807 69.778  1.00 28.10 ? 420  LEU B CD1 1 
ATOM   6471 C  CD2 . LEU B 1 418 ? 101.477 -18.367 71.534  1.00 28.30 ? 420  LEU B CD2 1 
ATOM   6472 N  N   . SER B 1 419 ? 100.199 -22.577 70.196  1.00 25.68 ? 421  SER B N   1 
ATOM   6473 C  CA  . SER B 1 419 ? 99.479  -23.461 69.294  1.00 24.31 ? 421  SER B CA  1 
ATOM   6474 C  C   . SER B 1 419 ? 98.963  -22.663 68.104  1.00 24.86 ? 421  SER B C   1 
ATOM   6475 O  O   . SER B 1 419 ? 98.136  -21.763 68.257  1.00 23.42 ? 421  SER B O   1 
ATOM   6476 C  CB  . SER B 1 419 ? 98.317  -24.135 70.021  1.00 27.32 ? 421  SER B CB  1 
ATOM   6477 O  OG  . SER B 1 419 ? 97.630  -25.025 69.160  1.00 33.80 ? 421  SER B OG  1 
ATOM   6478 N  N   . ILE B 1 420 ? 99.490  -22.968 66.923  1.00 22.23 ? 422  ILE B N   1 
ATOM   6479 C  CA  . ILE B 1 420 ? 99.348  -22.084 65.775  1.00 20.14 ? 422  ILE B CA  1 
ATOM   6480 C  C   . ILE B 1 420 ? 98.629  -22.800 64.641  1.00 18.77 ? 422  ILE B C   1 
ATOM   6481 O  O   . ILE B 1 420 ? 99.109  -23.816 64.141  1.00 16.65 ? 422  ILE B O   1 
ATOM   6482 C  CB  . ILE B 1 420 ? 100.718 -21.584 65.278  1.00 19.90 ? 422  ILE B CB  1 
ATOM   6483 C  CG1 . ILE B 1 420 ? 101.489 -20.913 66.418  1.00 19.88 ? 422  ILE B CG1 1 
ATOM   6484 C  CG2 . ILE B 1 420 ? 100.549 -20.611 64.122  1.00 18.30 ? 422  ILE B CG2 1 
ATOM   6485 C  CD1 . ILE B 1 420 ? 102.913 -20.548 66.060  1.00 19.21 ? 422  ILE B CD1 1 
ATOM   6486 N  N   . PRO B 1 421 ? 97.450  -22.290 64.256  1.00 18.19 ? 423  PRO B N   1 
ATOM   6487 C  CA  . PRO B 1 421 ? 96.770  -22.823 63.083  1.00 19.25 ? 423  PRO B CA  1 
ATOM   6488 C  C   . PRO B 1 421 ? 97.677  -22.702 61.864  1.00 18.39 ? 423  PRO B C   1 
ATOM   6489 O  O   . PRO B 1 421 ? 98.563  -21.849 61.842  1.00 18.36 ? 423  PRO B O   1 
ATOM   6490 C  CB  . PRO B 1 421 ? 95.553  -21.897 62.925  1.00 19.53 ? 423  PRO B CB  1 
ATOM   6491 C  CG  . PRO B 1 421 ? 95.408  -21.200 64.240  1.00 20.30 ? 423  PRO B CG  1 
ATOM   6492 C  CD  . PRO B 1 421 ? 96.803  -21.073 64.769  1.00 19.32 ? 423  PRO B CD  1 
ATOM   6493 N  N   . GLN B 1 422 ? 97.468  -23.559 60.870  1.00 20.47 ? 424  GLN B N   1 
ATOM   6494 C  CA  . GLN B 1 422 ? 98.193  -23.454 59.607  1.00 19.70 ? 424  GLN B CA  1 
ATOM   6495 C  C   . GLN B 1 422 ? 97.861  -22.152 58.891  1.00 19.24 ? 424  GLN B C   1 
ATOM   6496 O  O   . GLN B 1 422 ? 96.692  -21.824 58.702  1.00 18.53 ? 424  GLN B O   1 
ATOM   6497 C  CB  . GLN B 1 422 ? 97.849  -24.630 58.695  1.00 21.31 ? 424  GLN B CB  1 
ATOM   6498 C  CG  . GLN B 1 422 ? 98.453  -25.954 59.123  1.00 21.64 ? 424  GLN B CG  1 
ATOM   6499 C  CD  . GLN B 1 422 ? 98.302  -27.027 58.065  1.00 21.95 ? 424  GLN B CD  1 
ATOM   6500 O  OE1 . GLN B 1 422 ? 98.332  -26.743 56.867  1.00 24.54 ? 424  GLN B OE1 1 
ATOM   6501 N  NE2 . GLN B 1 422 ? 98.139  -28.267 58.501  1.00 21.59 ? 424  GLN B NE2 1 
ATOM   6502 N  N   . PHE B 1 423 ? 98.891  -21.434 58.455  1.00 19.76 ? 425  PHE B N   1 
ATOM   6503 C  CA  . PHE B 1 423 ? 98.698  -20.285 57.576  1.00 19.58 ? 425  PHE B CA  1 
ATOM   6504 C  C   . PHE B 1 423 ? 99.070  -20.635 56.142  1.00 17.47 ? 425  PHE B C   1 
ATOM   6505 O  O   . PHE B 1 423 ? 98.783  -19.881 55.211  1.00 16.19 ? 425  PHE B O   1 
ATOM   6506 C  CB  . PHE B 1 423 ? 99.529  -19.098 58.058  1.00 22.00 ? 425  PHE B CB  1 
ATOM   6507 C  CG  . PHE B 1 423 ? 99.277  -18.730 59.490  1.00 25.50 ? 425  PHE B CG  1 
ATOM   6508 C  CD1 . PHE B 1 423 ? 97.987  -18.524 59.946  1.00 27.29 ? 425  PHE B CD1 1 
ATOM   6509 C  CD2 . PHE B 1 423 ? 100.328 -18.604 60.382  1.00 28.62 ? 425  PHE B CD2 1 
ATOM   6510 C  CE1 . PHE B 1 423 ? 97.748  -18.190 61.266  1.00 30.25 ? 425  PHE B CE1 1 
ATOM   6511 C  CE2 . PHE B 1 423 ? 100.098 -18.257 61.700  1.00 30.10 ? 425  PHE B CE2 1 
ATOM   6512 C  CZ  . PHE B 1 423 ? 98.806  -18.058 62.144  1.00 30.03 ? 425  PHE B CZ  1 
ATOM   6513 N  N   . VAL B 1 424 ? 99.751  -21.765 55.983  1.00 16.21 ? 426  VAL B N   1 
ATOM   6514 C  CA  . VAL B 1 424 ? 100.120 -22.273 54.670  1.00 15.92 ? 426  VAL B CA  1 
ATOM   6515 C  C   . VAL B 1 424 ? 99.407  -23.597 54.421  1.00 16.99 ? 426  VAL B C   1 
ATOM   6516 O  O   . VAL B 1 424 ? 99.490  -24.522 55.233  1.00 17.92 ? 426  VAL B O   1 
ATOM   6517 C  CB  . VAL B 1 424 ? 101.642 -22.486 54.561  1.00 16.00 ? 426  VAL B CB  1 
ATOM   6518 C  CG1 . VAL B 1 424 ? 101.999 -23.136 53.232  1.00 17.03 ? 426  VAL B CG1 1 
ATOM   6519 C  CG2 . VAL B 1 424 ? 102.374 -21.164 54.726  1.00 16.23 ? 426  VAL B CG2 1 
ATOM   6520 N  N   . VAL B 1 425 ? 98.655  -23.664 53.327  1.00 15.34 ? 427  VAL B N   1 
ATOM   6521 C  CA  . VAL B 1 425 ? 97.833  -24.830 53.049  1.00 15.30 ? 427  VAL B CA  1 
ATOM   6522 C  C   . VAL B 1 425 ? 98.232  -25.455 51.720  1.00 15.09 ? 427  VAL B C   1 
ATOM   6523 O  O   . VAL B 1 425 ? 98.102  -24.833 50.665  1.00 13.95 ? 427  VAL B O   1 
ATOM   6524 C  CB  . VAL B 1 425 ? 96.334  -24.477 53.032  1.00 15.30 ? 427  VAL B CB  1 
ATOM   6525 C  CG1 . VAL B 1 425 ? 95.506  -25.699 52.664  1.00 15.55 ? 427  VAL B CG1 1 
ATOM   6526 C  CG2 . VAL B 1 425 ? 95.907  -23.924 54.388  1.00 16.54 ? 427  VAL B CG2 1 
ATOM   6527 N  N   . SER B 1 426 ? 98.741  -26.681 51.781  1.00 14.93 ? 428  SER B N   1 
ATOM   6528 C  CA  . SER B 1 426 ? 99.204  -27.364 50.583  1.00 15.23 ? 428  SER B CA  1 
ATOM   6529 C  C   . SER B 1 426 ? 98.041  -27.771 49.692  1.00 15.06 ? 428  SER B C   1 
ATOM   6530 O  O   . SER B 1 426 ? 97.123  -28.464 50.129  1.00 15.31 ? 428  SER B O   1 
ATOM   6531 C  CB  . SER B 1 426 ? 100.032 -28.595 50.946  1.00 16.70 ? 428  SER B CB  1 
ATOM   6532 O  OG  . SER B 1 426 ? 100.270 -29.386 49.792  1.00 17.82 ? 428  SER B OG  1 
ATOM   6533 N  N   . HIS B 1 427 ? 98.092  -27.356 48.432  1.00 14.82 ? 429  HIS B N   1 
ATOM   6534 C  CA  . HIS B 1 427 ? 97.184  -27.890 47.429  1.00 14.60 ? 429  HIS B CA  1 
ATOM   6535 C  C   . HIS B 1 427 ? 97.904  -28.874 46.524  1.00 13.53 ? 429  HIS B C   1 
ATOM   6536 O  O   . HIS B 1 427 ? 97.427  -29.209 45.439  1.00 11.85 ? 429  HIS B O   1 
ATOM   6537 C  CB  . HIS B 1 427 ? 96.554  -26.758 46.621  1.00 16.69 ? 429  HIS B CB  1 
ATOM   6538 C  CG  . HIS B 1 427 ? 95.667  -25.868 47.433  1.00 18.39 ? 429  HIS B CG  1 
ATOM   6539 N  ND1 . HIS B 1 427 ? 94.638  -26.356 48.209  1.00 21.97 ? 429  HIS B ND1 1 
ATOM   6540 C  CD2 . HIS B 1 427 ? 95.684  -24.529 47.628  1.00 20.37 ? 429  HIS B CD2 1 
ATOM   6541 C  CE1 . HIS B 1 427 ? 94.042  -25.351 48.827  1.00 23.86 ? 429  HIS B CE1 1 
ATOM   6542 N  NE2 . HIS B 1 427 ? 94.657  -24.231 48.491  1.00 21.94 ? 429  HIS B NE2 1 
ATOM   6543 N  N   . GLY B 1 428 ? 99.051  -29.350 46.992  1.00 13.12 ? 430  GLY B N   1 
ATOM   6544 C  CA  . GLY B 1 428 ? 99.742  -30.450 46.337  1.00 12.86 ? 430  GLY B CA  1 
ATOM   6545 C  C   . GLY B 1 428 ? 100.677 -29.989 45.238  1.00 12.15 ? 430  GLY B C   1 
ATOM   6546 O  O   . GLY B 1 428 ? 100.962 -28.797 45.100  1.00 11.88 ? 430  GLY B O   1 
ATOM   6547 N  N   . GLY B 1 429 ? 101.133 -30.944 44.439  1.00 11.72 ? 431  GLY B N   1 
ATOM   6548 C  CA  . GLY B 1 429 ? 102.153 -30.691 43.434  1.00 10.52 ? 431  GLY B CA  1 
ATOM   6549 C  C   . GLY B 1 429 ? 102.689 -32.002 42.900  1.00 10.37 ? 431  GLY B C   1 
ATOM   6550 O  O   . GLY B 1 429 ? 102.067 -33.052 43.064  1.00 9.58  ? 431  GLY B O   1 
ATOM   6551 N  N   . GLU B 1 430 ? 103.861 -31.944 42.281  1.00 10.07 ? 432  GLU B N   1 
ATOM   6552 C  CA  . GLU B 1 430 ? 104.469 -33.123 41.687  1.00 9.78  ? 432  GLU B CA  1 
ATOM   6553 C  C   . GLU B 1 430 ? 105.988 -33.011 41.732  1.00 9.83  ? 432  GLU B C   1 
ATOM   6554 O  O   . GLU B 1 430 ? 106.540 -31.920 41.913  1.00 9.26  ? 432  GLU B O   1 
ATOM   6555 C  CB  . GLU B 1 430 ? 103.975 -33.315 40.248  1.00 10.31 ? 432  GLU B CB  1 
ATOM   6556 C  CG  . GLU B 1 430 ? 104.425 -34.609 39.580  1.00 10.49 ? 432  GLU B CG  1 
ATOM   6557 C  CD  . GLU B 1 430 ? 104.091 -35.845 40.399  1.00 11.80 ? 432  GLU B CD  1 
ATOM   6558 O  OE1 . GLU B 1 430 ? 104.838 -36.145 41.355  1.00 10.76 ? 432  GLU B OE1 1 
ATOM   6559 O  OE2 . GLU B 1 430 ? 103.104 -36.540 40.062  1.00 11.94 ? 432  GLU B OE2 1 
ATOM   6560 N  N   . TYR B 1 431 ? 106.645 -34.162 41.658  1.00 9.67  ? 433  TYR B N   1 
ATOM   6561 C  CA  . TYR B 1 431 ? 108.085 -34.237 41.476  1.00 9.42  ? 433  TYR B CA  1 
ATOM   6562 C  C   . TYR B 1 431 ? 108.406 -34.411 39.992  1.00 9.31  ? 433  TYR B C   1 
ATOM   6563 O  O   . TYR B 1 431 ? 107.872 -35.308 39.334  1.00 9.26  ? 433  TYR B O   1 
ATOM   6564 C  CB  . TYR B 1 431 ? 108.648 -35.422 42.265  1.00 9.51  ? 433  TYR B CB  1 
ATOM   6565 C  CG  . TYR B 1 431 ? 108.449 -35.336 43.766  1.00 9.62  ? 433  TYR B CG  1 
ATOM   6566 C  CD1 . TYR B 1 431 ? 108.597 -34.132 44.437  1.00 10.07 ? 433  TYR B CD1 1 
ATOM   6567 C  CD2 . TYR B 1 431 ? 108.191 -36.477 44.519  1.00 9.91  ? 433  TYR B CD2 1 
ATOM   6568 C  CE1 . TYR B 1 431 ? 108.461 -34.056 45.814  1.00 10.22 ? 433  TYR B CE1 1 
ATOM   6569 C  CE2 . TYR B 1 431 ? 108.050 -36.411 45.898  1.00 10.68 ? 433  TYR B CE2 1 
ATOM   6570 C  CZ  . TYR B 1 431 ? 108.186 -35.196 46.539  1.00 10.57 ? 433  TYR B CZ  1 
ATOM   6571 O  OH  . TYR B 1 431 ? 108.051 -35.113 47.912  1.00 11.30 ? 433  TYR B OH  1 
ATOM   6572 N  N   . PHE B 1 432 ? 109.265 -33.543 39.464  1.00 8.81  ? 434  PHE B N   1 
ATOM   6573 C  CA  . PHE B 1 432 ? 109.668 -33.627 38.059  1.00 9.00  ? 434  PHE B CA  1 
ATOM   6574 C  C   . PHE B 1 432 ? 111.178 -33.758 37.948  1.00 8.67  ? 434  PHE B C   1 
ATOM   6575 O  O   . PHE B 1 432 ? 111.906 -33.463 38.895  1.00 8.35  ? 434  PHE B O   1 
ATOM   6576 C  CB  . PHE B 1 432 ? 109.231 -32.381 37.278  1.00 8.46  ? 434  PHE B CB  1 
ATOM   6577 C  CG  . PHE B 1 432 ? 107.754 -32.121 37.318  1.00 9.44  ? 434  PHE B CG  1 
ATOM   6578 C  CD1 . PHE B 1 432 ? 107.194 -31.386 38.353  1.00 9.50  ? 434  PHE B CD1 1 
ATOM   6579 C  CD2 . PHE B 1 432 ? 106.925 -32.602 36.316  1.00 9.20  ? 434  PHE B CD2 1 
ATOM   6580 C  CE1 . PHE B 1 432 ? 105.834 -31.141 38.393  1.00 9.68  ? 434  PHE B CE1 1 
ATOM   6581 C  CE2 . PHE B 1 432 ? 105.563 -32.357 36.348  1.00 9.93  ? 434  PHE B CE2 1 
ATOM   6582 C  CZ  . PHE B 1 432 ? 105.018 -31.624 37.387  1.00 10.08 ? 434  PHE B CZ  1 
ATOM   6583 N  N   . PHE B 1 433 ? 111.644 -34.120 36.756  1.00 8.46  ? 435  PHE B N   1 
ATOM   6584 C  CA  . PHE B 1 433 ? 113.064 -34.039 36.436  1.00 8.79  ? 435  PHE B CA  1 
ATOM   6585 C  C   . PHE B 1 433 ? 113.268 -33.049 35.298  1.00 8.86  ? 435  PHE B C   1 
ATOM   6586 O  O   . PHE B 1 433 ? 112.718 -33.228 34.211  1.00 9.10  ? 435  PHE B O   1 
ATOM   6587 C  CB  . PHE B 1 433 ? 113.605 -35.415 36.036  1.00 8.27  ? 435  PHE B CB  1 
ATOM   6588 C  CG  . PHE B 1 433 ? 115.072 -35.415 35.691  1.00 8.76  ? 435  PHE B CG  1 
ATOM   6589 C  CD1 . PHE B 1 433 ? 116.023 -35.165 36.667  1.00 8.63  ? 435  PHE B CD1 1 
ATOM   6590 C  CD2 . PHE B 1 433 ? 115.496 -35.649 34.391  1.00 8.97  ? 435  PHE B CD2 1 
ATOM   6591 C  CE1 . PHE B 1 433 ? 117.372 -35.158 36.358  1.00 8.67  ? 435  PHE B CE1 1 
ATOM   6592 C  CE2 . PHE B 1 433 ? 116.842 -35.640 34.072  1.00 8.81  ? 435  PHE B CE2 1 
ATOM   6593 C  CZ  . PHE B 1 433 ? 117.782 -35.397 35.058  1.00 8.87  ? 435  PHE B CZ  1 
ATOM   6594 N  N   . SER B 1 434 ? 114.016 -31.982 35.564  1.00 9.34  ? 436  SER B N   1 
ATOM   6595 C  CA  . SER B 1 434 ? 114.416 -31.051 34.514  1.00 9.48  ? 436  SER B CA  1 
ATOM   6596 C  C   . SER B 1 434 ? 115.708 -31.537 33.871  1.00 9.50  ? 436  SER B C   1 
ATOM   6597 O  O   . SER B 1 434 ? 116.774 -31.448 34.480  1.00 9.32  ? 436  SER B O   1 
ATOM   6598 C  CB  . SER B 1 434 ? 114.630 -29.640 35.077  1.00 9.80  ? 436  SER B CB  1 
ATOM   6599 O  OG  . SER B 1 434 ? 113.506 -29.202 35.824  1.00 12.50 ? 436  SER B OG  1 
ATOM   6600 N  N   . PRO B 1 435 ? 115.620 -32.035 32.629  1.00 9.32  ? 437  PRO B N   1 
ATOM   6601 C  CA  . PRO B 1 435 ? 116.778 -32.647 31.992  1.00 9.26  ? 437  PRO B CA  1 
ATOM   6602 C  C   . PRO B 1 435 ? 117.791 -31.599 31.550  1.00 9.41  ? 437  PRO B C   1 
ATOM   6603 O  O   . PRO B 1 435 ? 117.449 -30.425 31.422  1.00 9.16  ? 437  PRO B O   1 
ATOM   6604 C  CB  . PRO B 1 435 ? 116.179 -33.346 30.768  1.00 9.54  ? 437  PRO B CB  1 
ATOM   6605 C  CG  . PRO B 1 435 ? 114.942 -32.578 30.462  1.00 10.03 ? 437  PRO B CG  1 
ATOM   6606 C  CD  . PRO B 1 435 ? 114.410 -32.118 31.793  1.00 9.74  ? 437  PRO B CD  1 
ATOM   6607 N  N   . PRO B 1 436 ? 119.042 -32.019 31.333  1.00 9.37  ? 438  PRO B N   1 
ATOM   6608 C  CA  . PRO B 1 436 ? 119.963 -31.164 30.597  1.00 10.02 ? 438  PRO B CA  1 
ATOM   6609 C  C   . PRO B 1 436 ? 119.391 -30.860 29.217  1.00 10.00 ? 438  PRO B C   1 
ATOM   6610 O  O   . PRO B 1 436 ? 118.604 -31.644 28.684  1.00 10.70 ? 438  PRO B O   1 
ATOM   6611 C  CB  . PRO B 1 436 ? 121.227 -32.020 30.480  1.00 9.84  ? 438  PRO B CB  1 
ATOM   6612 C  CG  . PRO B 1 436 ? 120.754 -33.426 30.620  1.00 10.14 ? 438  PRO B CG  1 
ATOM   6613 C  CD  . PRO B 1 436 ? 119.571 -33.377 31.542  1.00 9.69  ? 438  PRO B CD  1 
ATOM   6614 N  N   . ILE B 1 437 ? 119.737 -29.704 28.668  1.00 10.26 ? 439  ILE B N   1 
ATOM   6615 C  CA  . ILE B 1 437 ? 119.126 -29.254 27.422  1.00 10.76 ? 439  ILE B CA  1 
ATOM   6616 C  C   . ILE B 1 437 ? 119.406 -30.224 26.276  1.00 11.09 ? 439  ILE B C   1 
ATOM   6617 O  O   . ILE B 1 437 ? 118.532 -30.485 25.452  1.00 10.67 ? 439  ILE B O   1 
ATOM   6618 C  CB  . ILE B 1 437 ? 119.557 -27.817 27.068  1.00 11.16 ? 439  ILE B CB  1 
ATOM   6619 C  CG1 . ILE B 1 437 ? 119.102 -26.853 28.169  1.00 10.64 ? 439  ILE B CG1 1 
ATOM   6620 C  CG2 . ILE B 1 437 ? 118.986 -27.395 25.722  1.00 11.68 ? 439  ILE B CG2 1 
ATOM   6621 C  CD1 . ILE B 1 437 ? 119.594 -25.432 27.994  1.00 11.07 ? 439  ILE B CD1 1 
ATOM   6622 N  N   . SER B 1 438 ? 120.583 -30.848 26.297  1.00 11.43 ? 440  SER B N   1 
ATOM   6623 C  CA  . SER B 1 438 ? 120.952 -31.827 25.274  1.00 11.57 ? 440  SER B CA  1 
ATOM   6624 C  C   . SER B 1 438 ? 120.013 -33.037 25.236  1.00 11.40 ? 440  SER B C   1 
ATOM   6625 O  O   . SER B 1 438 ? 119.843 -33.663 24.192  1.00 12.19 ? 440  SER B O   1 
ATOM   6626 C  CB  . SER B 1 438 ? 122.399 -32.290 25.467  1.00 12.17 ? 440  SER B CB  1 
ATOM   6627 O  OG  . SER B 1 438 ? 122.580 -32.883 26.743  1.00 12.78 ? 440  SER B OG  1 
ATOM   6628 N  N   . ALA B 1 439 ? 119.391 -33.357 26.367  1.00 11.12 ? 441  ALA B N   1 
ATOM   6629 C  CA  . ALA B 1 439 ? 118.512 -34.528 26.444  1.00 11.08 ? 441  ALA B CA  1 
ATOM   6630 C  C   . ALA B 1 439 ? 117.140 -34.266 25.824  1.00 11.13 ? 441  ALA B C   1 
ATOM   6631 O  O   . ALA B 1 439 ? 116.413 -35.199 25.487  1.00 10.02 ? 441  ALA B O   1 
ATOM   6632 C  CB  . ALA B 1 439 ? 118.361 -34.988 27.884  1.00 11.11 ? 441  ALA B CB  1 
ATOM   6633 N  N   . ILE B 1 440 ? 116.784 -32.994 25.684  1.00 10.75 ? 442  ILE B N   1 
ATOM   6634 C  CA  . ILE B 1 440 ? 115.450 -32.629 25.222  1.00 11.24 ? 442  ILE B CA  1 
ATOM   6635 C  C   . ILE B 1 440 ? 115.271 -32.934 23.735  1.00 11.51 ? 442  ILE B C   1 
ATOM   6636 O  O   . ILE B 1 440 ? 114.328 -33.627 23.343  1.00 12.20 ? 442  ILE B O   1 
ATOM   6637 C  CB  . ILE B 1 440 ? 115.142 -31.146 25.511  1.00 11.49 ? 442  ILE B CB  1 
ATOM   6638 C  CG1 . ILE B 1 440 ? 115.196 -30.886 27.020  1.00 11.48 ? 442  ILE B CG1 1 
ATOM   6639 C  CG2 . ILE B 1 440 ? 113.773 -30.767 24.961  1.00 10.97 ? 442  ILE B CG2 1 
ATOM   6640 C  CD1 . ILE B 1 440 ? 115.096 -29.422 27.403  1.00 12.19 ? 442  ILE B CD1 1 
ATOM   6641 N  N   . GLY B 1 441 ? 116.211 -32.470 22.919  1.00 11.12 ? 443  GLY B N   1 
ATOM   6642 C  CA  . GLY B 1 441 ? 116.260 -32.856 21.513  1.00 11.46 ? 443  GLY B CA  1 
ATOM   6643 C  C   . GLY B 1 441 ? 117.074 -34.119 21.303  1.00 11.74 ? 443  GLY B C   1 
ATOM   6644 O  O   . GLY B 1 441 ? 117.250 -34.574 20.172  1.00 11.99 ? 443  GLY B O   1 
ATOM   6645 N  N   . GLY B 1 442 ? 117.573 -34.681 22.400  1.00 10.91 ? 444  GLY B N   1 
ATOM   6646 C  CA  . GLY B 1 442 ? 118.339 -35.924 22.358  1.00 10.47 ? 444  GLY B CA  1 
ATOM   6647 C  C   . GLY B 1 442 ? 117.502 -37.110 22.798  1.00 10.86 ? 444  GLY B C   1 
ATOM   6648 O  O   . GLY B 1 442 ? 116.470 -37.416 22.188  1.00 10.78 ? 444  GLY B O   1 
ATOM   6649 N  N   . ARG B 1 443 ? 117.919 -37.752 23.887  1.00 10.54 ? 445  ARG B N   1 
ATOM   6650 C  CA  . ARG B 1 443 ? 117.307 -39.008 24.319  1.00 10.36 ? 445  ARG B CA  1 
ATOM   6651 C  C   . ARG B 1 443 ? 115.784 -38.918 24.389  1.00 10.19 ? 445  ARG B C   1 
ATOM   6652 O  O   . ARG B 1 443 ? 115.083 -39.846 23.987  1.00 9.98  ? 445  ARG B O   1 
ATOM   6653 C  CB  . ARG B 1 443 ? 117.862 -39.451 25.678  1.00 10.01 ? 445  ARG B CB  1 
ATOM   6654 C  CG  . ARG B 1 443 ? 117.160 -40.666 26.268  1.00 10.12 ? 445  ARG B CG  1 
ATOM   6655 C  CD  . ARG B 1 443 ? 117.338 -41.886 25.376  1.00 10.16 ? 445  ARG B CD  1 
ATOM   6656 N  NE  . ARG B 1 443 ? 116.584 -43.053 25.829  1.00 10.46 ? 445  ARG B NE  1 
ATOM   6657 C  CZ  . ARG B 1 443 ? 115.373 -43.382 25.384  1.00 11.00 ? 445  ARG B CZ  1 
ATOM   6658 N  NH1 . ARG B 1 443 ? 114.742 -42.587 24.531  1.00 10.38 ? 445  ARG B NH1 1 
ATOM   6659 N  NH2 . ARG B 1 443 ? 114.779 -44.489 25.816  1.00 10.77 ? 445  ARG B NH2 1 
ATOM   6660 N  N   . LEU B 1 444 ? 115.267 -37.824 24.932  1.00 10.24 ? 446  LEU B N   1 
ATOM   6661 C  CA  . LEU B 1 444 ? 113.831 -37.742 25.185  1.00 10.45 ? 446  LEU B CA  1 
ATOM   6662 C  C   . LEU B 1 444 ? 113.035 -37.677 23.878  1.00 11.16 ? 446  LEU B C   1 
ATOM   6663 O  O   . LEU B 1 444 ? 111.857 -38.031 23.840  1.00 11.40 ? 446  LEU B O   1 
ATOM   6664 C  CB  . LEU B 1 444 ? 113.496 -36.554 26.086  1.00 10.22 ? 446  LEU B CB  1 
ATOM   6665 C  CG  . LEU B 1 444 ? 114.139 -36.547 27.478  1.00 11.01 ? 446  LEU B CG  1 
ATOM   6666 C  CD1 . LEU B 1 444 ? 113.580 -35.407 28.317  1.00 11.27 ? 446  LEU B CD1 1 
ATOM   6667 C  CD2 . LEU B 1 444 ? 113.950 -37.879 28.189  1.00 10.38 ? 446  LEU B CD2 1 
ATOM   6668 N  N   . SER B 1 445 ? 113.694 -37.257 22.804  1.00 12.37 ? 447  SER B N   1 
ATOM   6669 C  CA  . SER B 1 445 ? 113.050 -37.182 21.496  1.00 13.32 ? 447  SER B CA  1 
ATOM   6670 C  C   . SER B 1 445 ? 113.296 -38.428 20.643  1.00 15.12 ? 447  SER B C   1 
ATOM   6671 O  O   . SER B 1 445 ? 112.731 -38.562 19.557  1.00 15.11 ? 447  SER B O   1 
ATOM   6672 C  CB  . SER B 1 445 ? 113.516 -35.937 20.742  1.00 13.36 ? 447  SER B CB  1 
ATOM   6673 O  OG  . SER B 1 445 ? 113.009 -34.756 21.343  1.00 13.94 ? 447  SER B OG  1 
ATOM   6674 N  N   . ALA B 1 446 ? 114.137 -39.335 21.134  1.00 16.07 ? 448  ALA B N   1 
ATOM   6675 C  CA  . ALA B 1 446 ? 114.569 -40.480 20.336  1.00 18.26 ? 448  ALA B CA  1 
ATOM   6676 C  C   . ALA B 1 446 ? 113.566 -41.626 20.403  1.00 20.16 ? 448  ALA B C   1 
ATOM   6677 O  O   . ALA B 1 446 ? 113.490 -42.448 19.492  1.00 22.89 ? 448  ALA B O   1 
ATOM   6678 C  CB  . ALA B 1 446 ? 115.947 -40.952 20.776  1.00 18.58 ? 448  ALA B CB  1 
ATOM   6679 O  OXT . ALA B 1 446 ? 112.804 -41.758 21.362  1.00 20.54 ? 448  ALA B OXT 1 
HETATM 6680 AS AS  . CAC C 2 .   ? 80.911  9.552   -7.700  1.00 27.72 ? 1449 CAC A AS  1 
HETATM 6681 O  O1  . CAC C 2 .   ? 81.558  8.059   -8.323  1.00 22.52 ? 1449 CAC A O1  1 
HETATM 6682 O  O2  . CAC C 2 .   ? 79.478  9.983   -8.584  1.00 25.70 ? 1449 CAC A O2  1 
HETATM 6683 C  C1  . CAC C 2 .   ? 80.484  9.335   -5.796  1.00 24.00 ? 1449 CAC A C1  1 
HETATM 6684 C  C2  . CAC C 2 .   ? 82.260  10.968  -7.890  1.00 24.46 ? 1449 CAC A C2  1 
HETATM 6685 C  C1  . GOL D 3 .   ? 99.129  -9.397  39.541  1.00 28.44 ? 1450 GOL A C1  1 
HETATM 6686 O  O1  . GOL D 3 .   ? 100.314 -10.052 40.008  1.00 30.38 ? 1450 GOL A O1  1 
HETATM 6687 C  C2  . GOL D 3 .   ? 98.009  -9.621  40.549  1.00 27.40 ? 1450 GOL A C2  1 
HETATM 6688 O  O2  . GOL D 3 .   ? 98.370  -9.032  41.805  1.00 26.81 ? 1450 GOL A O2  1 
HETATM 6689 C  C3  . GOL D 3 .   ? 96.734  -8.966  40.035  1.00 26.91 ? 1450 GOL A C3  1 
HETATM 6690 O  O3  . GOL D 3 .   ? 95.661  -9.264  40.935  1.00 24.84 ? 1450 GOL A O3  1 
HETATM 6691 C  C1  . GOL E 3 .   ? 95.513  -9.517  8.435   1.00 27.32 ? 1451 GOL A C1  1 
HETATM 6692 O  O1  . GOL E 3 .   ? 96.407  -8.769  7.600   1.00 27.46 ? 1451 GOL A O1  1 
HETATM 6693 C  C2  . GOL E 3 .   ? 96.255  -10.661 9.117   1.00 30.23 ? 1451 GOL A C2  1 
HETATM 6694 O  O2  . GOL E 3 .   ? 95.599  -11.902 8.812   1.00 31.34 ? 1451 GOL A O2  1 
HETATM 6695 C  C3  . GOL E 3 .   ? 96.254  -10.441 10.627  1.00 29.90 ? 1451 GOL A C3  1 
HETATM 6696 O  O3  . GOL E 3 .   ? 97.160  -9.381  10.965  1.00 30.07 ? 1451 GOL A O3  1 
HETATM 6697 C  C1  . GOL F 3 .   ? 95.266  12.930  2.409   1.00 34.91 ? 1452 GOL A C1  1 
HETATM 6698 O  O1  . GOL F 3 .   ? 94.610  13.777  1.459   1.00 39.24 ? 1452 GOL A O1  1 
HETATM 6699 C  C2  . GOL F 3 .   ? 94.380  12.765  3.635   1.00 32.30 ? 1452 GOL A C2  1 
HETATM 6700 O  O2  . GOL F 3 .   ? 93.427  11.720  3.402   1.00 34.59 ? 1452 GOL A O2  1 
HETATM 6701 C  C3  . GOL F 3 .   ? 95.235  12.441  4.857   1.00 32.52 ? 1452 GOL A C3  1 
HETATM 6702 O  O3  . GOL F 3 .   ? 96.160  11.384  4.565   1.00 27.97 ? 1452 GOL A O3  1 
HETATM 6703 C  C1  . GOL G 3 .   ? 58.635  10.483  23.483  1.00 41.65 ? 1453 GOL A C1  1 
HETATM 6704 O  O1  . GOL G 3 .   ? 58.762  9.219   22.818  1.00 45.47 ? 1453 GOL A O1  1 
HETATM 6705 C  C2  . GOL G 3 .   ? 60.017  11.094  23.675  1.00 37.16 ? 1453 GOL A C2  1 
HETATM 6706 O  O2  . GOL G 3 .   ? 60.917  10.098  24.175  1.00 39.37 ? 1453 GOL A O2  1 
HETATM 6707 C  C3  . GOL G 3 .   ? 60.529  11.616  22.340  1.00 35.31 ? 1453 GOL A C3  1 
HETATM 6708 O  O3  . GOL G 3 .   ? 60.731  13.031  22.430  1.00 42.17 ? 1453 GOL A O3  1 
HETATM 6709 C  C1  . NAG H 4 .   ? 82.335  14.033  0.329   1.00 19.22 ? 1454 NAG A C1  1 
HETATM 6710 C  C2  . NAG H 4 .   ? 83.427  15.094  0.245   1.00 21.73 ? 1454 NAG A C2  1 
HETATM 6711 C  C3  . NAG H 4 .   ? 82.947  16.274  -0.592  1.00 23.17 ? 1454 NAG A C3  1 
HETATM 6712 C  C4  . NAG H 4 .   ? 82.404  15.800  -1.936  1.00 23.10 ? 1454 NAG A C4  1 
HETATM 6713 C  C5  . NAG H 4 .   ? 81.432  14.636  -1.761  1.00 21.22 ? 1454 NAG A C5  1 
HETATM 6714 C  C6  . NAG H 4 .   ? 81.040  14.056  -3.114  1.00 21.07 ? 1454 NAG A C6  1 
HETATM 6715 C  C7  . NAG H 4 .   ? 85.100  15.516  1.946   1.00 22.76 ? 1454 NAG A C7  1 
HETATM 6716 C  C8  . NAG H 4 .   ? 85.406  16.009  3.329   1.00 22.48 ? 1454 NAG A C8  1 
HETATM 6717 N  N2  . NAG H 4 .   ? 83.826  15.550  1.565   1.00 21.62 ? 1454 NAG A N2  1 
HETATM 6718 O  O3  . NAG H 4 .   ? 84.018  17.169  -0.794  1.00 23.93 ? 1454 NAG A O3  1 
HETATM 6719 O  O4  . NAG H 4 .   ? 81.712  16.866  -2.545  1.00 26.95 ? 1454 NAG A O4  1 
HETATM 6720 O  O5  . NAG H 4 .   ? 82.028  13.621  -0.985  1.00 20.11 ? 1454 NAG A O5  1 
HETATM 6721 O  O6  . NAG H 4 .   ? 80.133  12.994  -2.931  1.00 20.27 ? 1454 NAG A O6  1 
HETATM 6722 O  O7  . NAG H 4 .   ? 86.002  15.099  1.220   1.00 24.15 ? 1454 NAG A O7  1 
HETATM 6723 C  C1  . NAG I 4 .   ? 82.254  17.111  -3.853  1.00 28.51 ? 1457 NAG A C1  1 
HETATM 6724 C  C2  . NAG I 4 .   ? 81.264  17.970  -4.636  1.00 30.58 ? 1457 NAG A C2  1 
HETATM 6725 C  C3  . NAG I 4 .   ? 81.828  18.365  -5.994  1.00 31.98 ? 1457 NAG A C3  1 
HETATM 6726 C  C4  . NAG I 4 .   ? 83.222  18.949  -5.826  1.00 34.40 ? 1457 NAG A C4  1 
HETATM 6727 C  C5  . NAG I 4 .   ? 84.091  17.964  -5.053  1.00 34.71 ? 1457 NAG A C5  1 
HETATM 6728 C  C6  . NAG I 4 .   ? 85.507  18.497  -4.878  1.00 34.70 ? 1457 NAG A C6  1 
HETATM 6729 C  C7  . NAG I 4 .   ? 79.003  17.381  -3.969  1.00 32.28 ? 1457 NAG A C7  1 
HETATM 6730 C  C8  . NAG I 4 .   ? 77.761  16.600  -4.283  1.00 31.68 ? 1457 NAG A C8  1 
HETATM 6731 N  N2  . NAG I 4 .   ? 80.012  17.262  -4.827  1.00 29.79 ? 1457 NAG A N2  1 
HETATM 6732 O  O3  . NAG I 4 .   ? 80.981  19.315  -6.592  1.00 33.38 ? 1457 NAG A O3  1 
HETATM 6733 O  O4  . NAG I 4 .   ? 83.778  19.208  -7.095  1.00 38.52 ? 1457 NAG A O4  1 
HETATM 6734 O  O5  . NAG I 4 .   ? 83.514  17.743  -3.782  1.00 31.60 ? 1457 NAG A O5  1 
HETATM 6735 O  O6  . NAG I 4 .   ? 85.470  19.660  -4.079  1.00 36.39 ? 1457 NAG A O6  1 
HETATM 6736 O  O7  . NAG I 4 .   ? 79.062  18.077  -2.956  1.00 32.93 ? 1457 NAG A O7  1 
HETATM 6737 C  C1  . NAG J 4 .   ? 97.680  -23.733 2.800   1.00 17.99 ? 1455 NAG A C1  1 
HETATM 6738 C  C2  . NAG J 4 .   ? 98.470  -24.970 2.379   1.00 18.88 ? 1455 NAG A C2  1 
HETATM 6739 C  C3  . NAG J 4 .   ? 99.417  -24.616 1.241   1.00 19.96 ? 1455 NAG A C3  1 
HETATM 6740 C  C4  . NAG J 4 .   ? 98.644  -23.939 0.115   1.00 20.22 ? 1455 NAG A C4  1 
HETATM 6741 C  C5  . NAG J 4 .   ? 97.858  -22.756 0.666   1.00 20.15 ? 1455 NAG A C5  1 
HETATM 6742 C  C6  . NAG J 4 .   ? 97.045  -22.076 -0.431  1.00 19.12 ? 1455 NAG A C6  1 
HETATM 6743 C  C7  . NAG J 4 .   ? 99.100  -26.799 3.849   1.00 20.62 ? 1455 NAG A C7  1 
HETATM 6744 C  C8  . NAG J 4 .   ? 99.937  -27.272 5.001   1.00 19.86 ? 1455 NAG A C8  1 
HETATM 6745 N  N2  . NAG J 4 .   ? 99.229  -25.523 3.487   1.00 19.11 ? 1455 NAG A N2  1 
HETATM 6746 O  O3  . NAG J 4 .   ? 100.052 -25.783 0.769   1.00 21.02 ? 1455 NAG A O3  1 
HETATM 6747 O  O4  . NAG J 4 .   ? 99.542  -23.476 -0.868  1.00 21.64 ? 1455 NAG A O4  1 
HETATM 6748 O  O5  . NAG J 4 .   ? 96.992  -23.199 1.686   1.00 18.20 ? 1455 NAG A O5  1 
HETATM 6749 O  O6  . NAG J 4 .   ? 95.869  -22.812 -0.674  1.00 20.15 ? 1455 NAG A O6  1 
HETATM 6750 O  O7  . NAG J 4 .   ? 98.319  -27.573 3.302   1.00 20.81 ? 1455 NAG A O7  1 
HETATM 6751 C  C1  . NAG K 4 .   ? 78.755  -15.376 -15.217 1.00 19.36 ? 1456 NAG A C1  1 
HETATM 6752 C  C2  . NAG K 4 .   ? 79.054  -16.169 -16.486 1.00 21.01 ? 1456 NAG A C2  1 
HETATM 6753 C  C3  . NAG K 4 .   ? 77.826  -16.946 -16.940 1.00 20.89 ? 1456 NAG A C3  1 
HETATM 6754 C  C4  . NAG K 4 .   ? 77.330  -17.797 -15.778 1.00 20.56 ? 1456 NAG A C4  1 
HETATM 6755 C  C5  . NAG K 4 .   ? 77.128  -16.923 -14.542 1.00 19.93 ? 1456 NAG A C5  1 
HETATM 6756 C  C6  . NAG K 4 .   ? 76.634  -17.755 -13.363 1.00 19.12 ? 1456 NAG A C6  1 
HETATM 6757 C  C7  . NAG K 4 .   ? 80.839  -15.316 -17.864 1.00 22.53 ? 1456 NAG A C7  1 
HETATM 6758 C  C8  . NAG K 4 .   ? 81.270  -14.385 -18.959 1.00 21.66 ? 1456 NAG A C8  1 
HETATM 6759 N  N2  . NAG K 4 .   ? 79.549  -15.303 -17.537 1.00 22.19 ? 1456 NAG A N2  1 
HETATM 6760 O  O3  . NAG K 4 .   ? 78.160  -17.777 -18.028 1.00 22.20 ? 1456 NAG A O3  1 
HETATM 6761 O  O4  . NAG K 4 .   ? 76.120  -18.435 -16.125 1.00 19.78 ? 1456 NAG A O4  1 
HETATM 6762 O  O5  . NAG K 4 .   ? 78.340  -16.273 -14.206 1.00 19.27 ? 1456 NAG A O5  1 
HETATM 6763 O  O6  . NAG K 4 .   ? 77.606  -18.720 -13.031 1.00 19.29 ? 1456 NAG A O6  1 
HETATM 6764 O  O7  . NAG K 4 .   ? 81.656  -16.049 -17.311 1.00 23.49 ? 1456 NAG A O7  1 
HETATM 6765 FE FE  . N7H L 5 .   ? 80.677  -5.915  11.240  1.00 9.05  ? 1458 N7H A FE  1 
HETATM 6766 N  N1  . N7H L 5 .   ? 85.020  -7.413  9.781   1.00 14.22 ? 1458 N7H A N1  1 
HETATM 6767 O  O1  . N7H L 5 .   ? 84.883  -7.925  8.484   1.00 16.91 ? 1458 N7H A O1  1 
HETATM 6768 O  O2  . N7H L 5 .   ? 86.103  -7.410  10.347  1.00 17.15 ? 1458 N7H A O2  1 
HETATM 6769 N  NA  . N7H L 5 .   ? 82.265  -5.048  10.400  1.00 10.13 ? 1458 N7H A NA  1 
HETATM 6770 N  NB  . N7H L 5 .   ? 81.807  -7.636  11.619  1.00 10.18 ? 1458 N7H A NB  1 
HETATM 6771 N  NC  . N7H L 5 .   ? 79.046  -6.848  12.133  1.00 9.13  ? 1458 N7H A NC  1 
HETATM 6772 N  ND  . N7H L 5 .   ? 79.646  -4.355  10.928  1.00 8.90  ? 1458 N7H A ND  1 
HETATM 6773 C  C1A . N7H L 5 .   ? 82.334  -3.733  9.998   1.00 10.14 ? 1458 N7H A C1A 1 
HETATM 6774 O  O1A . N7H L 5 .   ? 82.995  0.332   9.289   1.00 14.77 ? 1458 N7H A O1A 1 
HETATM 6775 C  C1B . N7H L 5 .   ? 83.084  -7.815  11.282  1.00 10.85 ? 1458 N7H A C1B 1 
HETATM 6776 C  C1C . N7H L 5 .   ? 79.027  -8.065  12.762  1.00 9.42  ? 1458 N7H A C1C 1 
HETATM 6777 C  C1D . N7H L 5 .   ? 78.349  -4.166  11.252  1.00 9.00  ? 1458 N7H A C1D 1 
HETATM 6778 O  O1D . N7H L 5 .   ? 78.614  1.231   7.075   1.00 10.14 ? 1458 N7H A O1D 1 
HETATM 6779 C  C2A . N7H L 5 .   ? 83.616  -3.476  9.468   1.00 10.79 ? 1458 N7H A C2A 1 
HETATM 6780 O  O2A . N7H L 5 .   ? 83.667  0.451   11.340  1.00 16.39 ? 1458 N7H A O2A 1 
HETATM 6781 C  C2B . N7H L 5 .   ? 83.531  -9.083  11.769  1.00 11.23 ? 1458 N7H A C2B 1 
HETATM 6782 C  C2C . N7H L 5 .   ? 77.708  -8.344  13.161  1.00 9.53  ? 1458 N7H A C2C 1 
HETATM 6783 C  C2D . N7H L 5 .   ? 77.924  -2.792  10.956  1.00 9.05  ? 1458 N7H A C2D 1 
HETATM 6784 O  O2D . N7H L 5 .   ? 77.779  1.766   8.993   1.00 9.98  ? 1458 N7H A O2D 1 
HETATM 6785 C  C3A . N7H L 5 .   ? 84.339  -4.618  9.572   1.00 11.09 ? 1458 N7H A C3A 1 
HETATM 6786 C  C3B . N7H L 5 .   ? 82.494  -9.636  12.471  1.00 10.52 ? 1458 N7H A C3B 1 
HETATM 6787 C  C3C . N7H L 5 .   ? 76.930  -7.249  12.798  1.00 9.38  ? 1458 N7H A C3C 1 
HETATM 6788 C  C3D . N7H L 5 .   ? 79.001  -2.150  10.485  1.00 9.11  ? 1458 N7H A C3D 1 
HETATM 6789 C  C4A . N7H L 5 .   ? 83.513  -5.593  10.179  1.00 10.91 ? 1458 N7H A C4A 1 
HETATM 6790 C  C4B . N7H L 5 .   ? 81.383  -8.662  12.380  1.00 10.23 ? 1458 N7H A C4B 1 
HETATM 6791 C  C4C . N7H L 5 .   ? 77.792  -6.314  12.165  1.00 9.02  ? 1458 N7H A C4C 1 
HETATM 6792 C  C4D . N7H L 5 .   ? 80.089  -3.142  10.515  1.00 9.21  ? 1458 N7H A C4D 1 
HETATM 6793 C  CAA . N7H L 5 .   ? 84.094  -2.167  8.888   1.00 11.44 ? 1458 N7H A CAA 1 
HETATM 6794 C  CAB . N7H L 5 .   ? 82.436  -10.924 13.196  1.00 10.62 ? 1458 N7H A CAB 1 
HETATM 6795 C  CAC . N7H L 5 .   ? 75.483  -7.035  13.003  1.00 9.71  ? 1458 N7H A CAC 1 
HETATM 6796 C  CAD . N7H L 5 .   ? 79.066  -0.699  10.041  1.00 9.32  ? 1458 N7H A CAD 1 
HETATM 6797 C  CBA . N7H L 5 .   ? 84.621  -1.276  10.012  1.00 12.30 ? 1458 N7H A CBA 1 
HETATM 6798 C  CBB . N7H L 5 .   ? 83.498  -11.441 13.807  1.00 10.38 ? 1458 N7H A CBB 1 
HETATM 6799 C  CBC . N7H L 5 .   ? 74.633  -8.044  13.129  1.00 11.32 ? 1458 N7H A CBC 1 
HETATM 6800 C  CBD . N7H L 5 .   ? 78.399  -0.544  8.665   1.00 9.66  ? 1458 N7H A CBD 1 
HETATM 6801 C  CGA . N7H L 5 .   ? 83.705  -0.101  10.223  1.00 14.51 ? 1458 N7H A CGA 1 
HETATM 6802 C  CGD . N7H L 5 .   ? 78.279  0.901   8.234   1.00 9.48  ? 1458 N7H A CGD 1 
HETATM 6803 C  CHA . N7H L 5 .   ? 81.347  -2.790  10.067  1.00 9.76  ? 1458 N7H A CHA 1 
HETATM 6804 C  CHB . N7H L 5 .   ? 83.898  -6.901  10.431  1.00 12.23 ? 1458 N7H A CHB 1 
HETATM 6805 C  CHC . N7H L 5 .   ? 80.129  -8.895  12.953  1.00 9.45  ? 1458 N7H A CHC 1 
HETATM 6806 C  CHD . N7H L 5 .   ? 77.408  -5.091  11.700  1.00 8.94  ? 1458 N7H A CHD 1 
HETATM 6807 C  CMA . N7H L 5 .   ? 85.770  -4.810  9.136   1.00 11.83 ? 1458 N7H A CMA 1 
HETATM 6808 C  CMB . N7H L 5 .   ? 84.896  -9.700  11.570  1.00 11.47 ? 1458 N7H A CMB 1 
HETATM 6809 C  CMC . N7H L 5 .   ? 77.253  -9.588  13.889  1.00 9.54  ? 1458 N7H A CMC 1 
HETATM 6810 C  CMD . N7H L 5 .   ? 76.538  -2.220  11.133  1.00 9.05  ? 1458 N7H A CMD 1 
HETATM 6811 C  C   . FMT M 6 .   ? 73.707  -18.309 48.805  1.00 49.40 ? 1459 FMT A C   1 
HETATM 6812 O  O1  . FMT M 6 .   ? 73.722  -19.206 47.978  1.00 48.28 ? 1459 FMT A O1  1 
HETATM 6813 O  O2  . FMT M 6 .   ? 74.342  -17.166 48.556  1.00 44.99 ? 1459 FMT A O2  1 
HETATM 6814 N  N   . NO2 N 7 .   ? 81.402  -5.386  14.726  1.00 19.05 ? 1460 NO2 A N   1 
HETATM 6815 O  O1  . NO2 N 7 .   ? 81.315  -5.330  13.329  1.00 16.50 ? 1460 NO2 A O1  1 
HETATM 6816 O  O2  . NO2 N 7 .   ? 82.392  -4.945  15.287  1.00 26.41 ? 1460 NO2 A O2  1 
HETATM 6817 AS AS  . CAC O 2 .   ? 128.749 -12.276 67.472  1.00 58.22 ? 1449 CAC B AS  1 
HETATM 6818 O  O1  . CAC O 2 .   ? 129.581 -13.553 68.315  1.00 48.05 ? 1449 CAC B O1  1 
HETATM 6819 O  O2  . CAC O 2 .   ? 127.219 -11.974 68.246  1.00 49.20 ? 1449 CAC B O2  1 
HETATM 6820 C  C1  . CAC O 2 .   ? 129.842 -10.647 67.517  1.00 53.14 ? 1449 CAC B C1  1 
HETATM 6821 C  C2  . CAC O 2 .   ? 128.446 -12.816 65.609  1.00 50.63 ? 1449 CAC B C2  1 
HETATM 6822 C  C1  . GOL P 3 .   ? 97.510  -10.568 23.694  1.00 26.78 ? 1450 GOL B C1  1 
HETATM 6823 O  O1  . GOL P 3 .   ? 96.283  -9.847  23.533  1.00 25.19 ? 1450 GOL B O1  1 
HETATM 6824 C  C2  . GOL P 3 .   ? 97.405  -11.906 22.969  1.00 27.92 ? 1450 GOL B C2  1 
HETATM 6825 O  O2  . GOL P 3 .   ? 97.676  -11.716 21.576  1.00 25.18 ? 1450 GOL B O2  1 
HETATM 6826 C  C3  . GOL P 3 .   ? 98.419  -12.882 23.552  1.00 26.40 ? 1450 GOL B C3  1 
HETATM 6827 O  O3  . GOL P 3 .   ? 97.993  -14.221 23.278  1.00 24.13 ? 1450 GOL B O3  1 
HETATM 6828 C  C1  . GOL Q 3 .   ? 125.994 -47.048 43.692  1.00 29.28 ? 1451 GOL B C1  1 
HETATM 6829 O  O1  . GOL Q 3 .   ? 127.182 -47.158 44.482  1.00 34.55 ? 1451 GOL B O1  1 
HETATM 6830 C  C2  . GOL Q 3 .   ? 125.352 -45.689 43.950  1.00 28.86 ? 1451 GOL B C2  1 
HETATM 6831 O  O2  . GOL Q 3 .   ? 124.226 -45.841 44.822  1.00 32.07 ? 1451 GOL B O2  1 
HETATM 6832 C  C3  . GOL Q 3 .   ? 124.891 -45.095 42.625  1.00 23.28 ? 1451 GOL B C3  1 
HETATM 6833 O  O3  . GOL Q 3 .   ? 123.614 -45.629 42.274  1.00 23.36 ? 1451 GOL B O3  1 
HETATM 6834 C  C1  . GOL R 3 .   ? 115.564 -17.749 75.318  1.00 29.74 ? 1452 GOL B C1  1 
HETATM 6835 O  O1  . GOL R 3 .   ? 116.967 -17.705 75.027  1.00 27.43 ? 1452 GOL B O1  1 
HETATM 6836 C  C2  . GOL R 3 .   ? 114.785 -16.950 74.276  1.00 28.31 ? 1452 GOL B C2  1 
HETATM 6837 O  O2  . GOL R 3 .   ? 115.181 -15.576 74.330  1.00 30.97 ? 1452 GOL B O2  1 
HETATM 6838 C  C3  . GOL R 3 .   ? 113.290 -17.044 74.560  1.00 31.87 ? 1452 GOL B C3  1 
HETATM 6839 O  O3  . GOL R 3 .   ? 112.590 -17.462 73.380  1.00 28.92 ? 1452 GOL B O3  1 
HETATM 6840 C  C1  . GOL S 3 .   ? 99.566  -13.138 39.620  1.00 31.45 ? 1453 GOL B C1  1 
HETATM 6841 O  O1  . GOL S 3 .   ? 99.782  -13.282 41.032  1.00 27.72 ? 1453 GOL B O1  1 
HETATM 6842 C  C2  . GOL S 3 .   ? 99.060  -14.447 39.019  1.00 31.33 ? 1453 GOL B C2  1 
HETATM 6843 O  O2  . GOL S 3 .   ? 98.525  -15.287 40.049  1.00 33.45 ? 1453 GOL B O2  1 
HETATM 6844 C  C3  . GOL S 3 .   ? 97.970  -14.160 37.991  1.00 34.52 ? 1453 GOL B C3  1 
HETATM 6845 O  O3  . GOL S 3 .   ? 96.953  -13.339 38.580  1.00 37.41 ? 1453 GOL B O3  1 
HETATM 6846 C  C1  . NAG T 4 .   ? 130.623 -11.121 58.683  1.00 25.79 ? 1454 NAG B C1  1 
HETATM 6847 C  C2  . NAG T 4 .   ? 131.225 -9.745  58.429  1.00 27.88 ? 1454 NAG B C2  1 
HETATM 6848 C  C3  . NAG T 4 .   ? 132.641 -9.699  58.992  1.00 29.80 ? 1454 NAG B C3  1 
HETATM 6849 C  C4  . NAG T 4 .   ? 132.624 -10.092 60.464  1.00 31.44 ? 1454 NAG B C4  1 
HETATM 6850 C  C5  . NAG T 4 .   ? 131.885 -11.409 60.672  1.00 29.15 ? 1454 NAG B C5  1 
HETATM 6851 C  C6  . NAG T 4 .   ? 131.700 -11.674 62.160  1.00 28.33 ? 1454 NAG B C6  1 
HETATM 6852 C  C7  . NAG T 4 .   ? 130.601 -8.366  56.509  1.00 26.78 ? 1454 NAG B C7  1 
HETATM 6853 C  C8  . NAG T 4 .   ? 130.706 -8.174  55.026  1.00 24.87 ? 1454 NAG B C8  1 
HETATM 6854 N  N2  . NAG T 4 .   ? 131.223 -9.435  57.012  1.00 27.08 ? 1454 NAG B N2  1 
HETATM 6855 O  O3  . NAG T 4 .   ? 133.156 -8.395  58.867  1.00 29.96 ? 1454 NAG B O3  1 
HETATM 6856 O  O4  . NAG T 4 .   ? 133.943 -10.197 60.957  1.00 34.12 ? 1454 NAG B O4  1 
HETATM 6857 O  O5  . NAG T 4 .   ? 130.606 -11.348 60.075  1.00 29.81 ? 1454 NAG B O5  1 
HETATM 6858 O  O6  . NAG T 4 .   ? 131.115 -12.943 62.343  1.00 29.63 ? 1454 NAG B O6  1 
HETATM 6859 O  O7  . NAG T 4 .   ? 129.961 -7.564  57.189  1.00 25.76 ? 1454 NAG B O7  1 
HETATM 6860 C  C1  . NAG U 4 .   ? 90.175  -8.242  62.629  1.00 30.25 ? 1455 NAG B C1  1 
HETATM 6861 C  C2  . NAG U 4 .   ? 88.906  -7.596  63.172  1.00 32.66 ? 1455 NAG B C2  1 
HETATM 6862 C  C3  . NAG U 4 .   ? 89.241  -6.228  63.744  1.00 37.43 ? 1455 NAG B C3  1 
HETATM 6863 C  C4  . NAG U 4 .   ? 90.331  -6.378  64.796  1.00 39.25 ? 1455 NAG B C4  1 
HETATM 6864 C  C5  . NAG U 4 .   ? 91.523  -7.153  64.243  1.00 37.84 ? 1455 NAG B C5  1 
HETATM 6865 C  C6  . NAG U 4 .   ? 92.525  -7.446  65.353  1.00 38.15 ? 1455 NAG B C6  1 
HETATM 6866 C  C7  . NAG U 4 .   ? 86.741  -8.155  62.268  1.00 30.56 ? 1455 NAG B C7  1 
HETATM 6867 C  C8  . NAG U 4 .   ? 85.733  -7.982  61.170  1.00 30.21 ? 1455 NAG B C8  1 
HETATM 6868 N  N2  . NAG U 4 .   ? 87.884  -7.485  62.150  1.00 30.91 ? 1455 NAG B N2  1 
HETATM 6869 O  O3  . NAG U 4 .   ? 88.089  -5.656  64.320  1.00 39.50 ? 1455 NAG B O3  1 
HETATM 6870 O  O4  . NAG U 4 .   ? 90.758  -5.101  65.209  1.00 47.52 ? 1455 NAG B O4  1 
HETATM 6871 O  O5  . NAG U 4 .   ? 91.101  -8.381  63.685  1.00 34.52 ? 1455 NAG B O5  1 
HETATM 6872 O  O6  . NAG U 4 .   ? 92.307  -8.752  65.847  1.00 37.60 ? 1455 NAG B O6  1 
HETATM 6873 O  O7  . NAG U 4 .   ? 86.501  -8.889  63.224  1.00 28.85 ? 1455 NAG B O7  1 
HETATM 6874 FE FE  . N7H V 5 .   ? 110.960 -20.986 52.890  1.00 11.81 ? 1456 N7H B FE  1 
HETATM 6875 N  N1  . N7H V 5 .   ? 108.344 -17.066 53.990  1.00 17.44 ? 1456 N7H B N1  1 
HETATM 6876 O  O1  . N7H V 5 .   ? 108.139 -17.009 55.374  1.00 18.60 ? 1456 N7H B O1  1 
HETATM 6877 O  O2  . N7H V 5 .   ? 107.900 -16.188 53.261  1.00 18.44 ? 1456 N7H B O2  1 
HETATM 6878 N  NA  . N7H V 5 .   ? 111.368 -19.075 53.278  1.00 13.06 ? 1456 N7H B NA  1 
HETATM 6879 N  NB  . N7H V 5 .   ? 108.917 -20.532 52.752  1.00 12.79 ? 1456 N7H B NB  1 
HETATM 6880 N  NC  . N7H V 5 .   ? 110.492 -22.970 52.473  1.00 11.82 ? 1456 N7H B NC  1 
HETATM 6881 N  ND  . N7H V 5 .   ? 112.803 -21.412 52.986  1.00 12.20 ? 1456 N7H B ND  1 
HETATM 6882 C  C1A . N7H V 5 .   ? 112.628 -18.520 53.348  1.00 13.33 ? 1456 N7H B C1A 1 
HETATM 6883 O  O1A . N7H V 5 .   ? 115.547 -16.277 50.849  1.00 20.20 ? 1456 N7H B O1A 1 
HETATM 6884 C  C1B . N7H V 5 .   ? 108.376 -19.328 52.954  1.00 13.37 ? 1456 N7H B C1B 1 
HETATM 6885 C  C1C . N7H V 5 .   ? 109.263 -23.482 52.151  1.00 11.13 ? 1456 N7H B C1C 1 
HETATM 6886 C  C1D . N7H V 5 .   ? 113.354 -22.636 52.833  1.00 11.86 ? 1456 N7H B C1D 1 
HETATM 6887 O  O1D . N7H V 5 .   ? 119.453 -20.849 53.657  1.00 11.71 ? 1456 N7H B O1D 1 
HETATM 6888 C  C2A . N7H V 5 .   ? 112.510 -17.137 53.616  1.00 14.24 ? 1456 N7H B C2A 1 
HETATM 6889 O  O2A . N7H V 5 .   ? 116.223 -16.501 52.898  1.00 18.43 ? 1456 N7H B O2A 1 
HETATM 6890 C  C2B . N7H V 5 .   ? 106.973 -19.382 52.692  1.00 13.00 ? 1456 N7H B C2B 1 
HETATM 6891 C  C2C . N7H V 5 .   ? 109.377 -24.872 51.997  1.00 11.15 ? 1456 N7H B C2C 1 
HETATM 6892 C  C2D . N7H V 5 .   ? 114.820 -22.558 52.868  1.00 12.03 ? 1456 N7H B C2D 1 
HETATM 6893 O  O2D . N7H V 5 .   ? 118.951 -19.795 55.474  1.00 11.86 ? 1456 N7H B O2D 1 
HETATM 6894 C  C3A . N7H V 5 .   ? 111.187 -16.849 53.696  1.00 15.07 ? 1456 N7H B C3A 1 
HETATM 6895 C  C3B . N7H V 5 .   ? 106.692 -20.658 52.287  1.00 12.05 ? 1456 N7H B C3B 1 
HETATM 6896 C  C3C . N7H V 5 .   ? 110.704 -25.204 52.235  1.00 11.33 ? 1456 N7H B C3C 1 
HETATM 6897 C  C3D . N7H V 5 .   ? 115.130 -21.259 53.008  1.00 12.00 ? 1456 N7H B C3D 1 
HETATM 6898 C  C4A . N7H V 5 .   ? 110.472 -18.039 53.454  1.00 13.97 ? 1456 N7H B C4A 1 
HETATM 6899 C  C4B . N7H V 5 .   ? 107.986 -21.381 52.291  1.00 11.91 ? 1456 N7H B C4B 1 
HETATM 6900 C  C4C . N7H V 5 .   ? 111.393 -23.993 52.525  1.00 11.39 ? 1456 N7H B C4C 1 
HETATM 6901 C  C4D . N7H V 5 .   ? 113.844 -20.545 53.044  1.00 11.83 ? 1456 N7H B C4D 1 
HETATM 6902 C  CAA . N7H V 5 .   ? 113.635 -16.156 53.850  1.00 15.37 ? 1456 N7H B CAA 1 
HETATM 6903 C  CAB . N7H V 5 .   ? 105.395 -21.235 51.887  1.00 12.42 ? 1456 N7H B CAB 1 
HETATM 6904 C  CAC . N7H V 5 .   ? 111.320 -26.545 52.210  1.00 11.42 ? 1456 N7H B CAC 1 
HETATM 6905 C  CAD . N7H V 5 .   ? 116.517 -20.662 53.095  1.00 11.80 ? 1456 N7H B CAD 1 
HETATM 6906 C  CBA . N7H V 5 .   ? 114.081 -15.483 52.552  1.00 16.04 ? 1456 N7H B CBA 1 
HETATM 6907 C  CBB . N7H V 5 .   ? 104.316 -20.478 51.703  1.00 12.98 ? 1456 N7H B CBB 1 
HETATM 6908 C  CBC . N7H V 5 .   ? 110.586 -27.645 52.342  1.00 11.85 ? 1456 N7H B CBC 1 
HETATM 6909 C  CBD . N7H V 5 .   ? 117.183 -21.042 54.425  1.00 11.69 ? 1456 N7H B CBD 1 
HETATM 6910 C  CGA . N7H V 5 .   ? 115.355 -16.125 52.075  1.00 17.94 ? 1456 N7H B CGA 1 
HETATM 6911 C  CGD . N7H V 5 .   ? 118.603 -20.524 54.514  1.00 11.92 ? 1456 N7H B CGD 1 
HETATM 6912 C  CHA . N7H V 5 .   ? 113.825 -19.170 53.201  1.00 12.89 ? 1456 N7H B CHA 1 
HETATM 6913 C  CHB . N7H V 5 .   ? 109.088 -18.120 53.451  1.00 14.54 ? 1456 N7H B CHB 1 
HETATM 6914 C  CHC . N7H V 5 .   ? 108.099 -22.739 51.970  1.00 11.73 ? 1456 N7H B CHC 1 
HETATM 6915 C  CHD . N7H V 5 .   ? 112.733 -23.883 52.756  1.00 11.65 ? 1456 N7H B CHD 1 
HETATM 6916 C  CMA . N7H V 5 .   ? 110.590 -15.489 53.963  1.00 16.00 ? 1456 N7H B CMA 1 
HETATM 6917 C  CMB . N7H V 5 .   ? 105.982 -18.254 52.846  1.00 13.33 ? 1456 N7H B CMB 1 
HETATM 6918 C  CMC . N7H V 5 .   ? 108.247 -25.812 51.651  1.00 11.00 ? 1456 N7H B CMC 1 
HETATM 6919 C  CMD . N7H V 5 .   ? 115.791 -23.711 52.765  1.00 12.05 ? 1456 N7H B CMD 1 
HETATM 6920 N  N   . NO2 W 7 .   ? 110.659 -20.933 49.273  1.00 22.96 ? 1457 NO2 B N   1 
HETATM 6921 O  O1  . NO2 W 7 .   ? 110.930 -20.543 50.592  1.00 21.98 ? 1457 NO2 B O1  1 
HETATM 6922 O  O2  . NO2 W 7 .   ? 110.612 -20.093 48.389  1.00 28.08 ? 1457 NO2 B O2  1 
HETATM 6923 O  O   . HOH X 8 .   ? 75.063  15.838  29.840  1.00 34.25 ? 2001 HOH A O   1 
HETATM 6924 O  O   . HOH X 8 .   ? 74.808  16.520  26.865  1.00 45.61 ? 2002 HOH A O   1 
HETATM 6925 O  O   . HOH X 8 .   ? 76.804  18.135  28.918  1.00 39.47 ? 2003 HOH A O   1 
HETATM 6926 O  O   . HOH X 8 .   ? 75.682  19.867  26.326  1.00 37.51 ? 2004 HOH A O   1 
HETATM 6927 O  O   . HOH X 8 .   ? 69.071  11.463  28.655  1.00 36.06 ? 2005 HOH A O   1 
HETATM 6928 O  O   . HOH X 8 .   ? 70.196  9.903   30.282  1.00 30.90 ? 2006 HOH A O   1 
HETATM 6929 O  O   . HOH X 8 .   ? 76.787  12.056  38.508  1.00 43.71 ? 2007 HOH A O   1 
HETATM 6930 O  O   . HOH X 8 .   ? 81.988  12.894  35.894  1.00 45.67 ? 2008 HOH A O   1 
HETATM 6931 O  O   . HOH X 8 .   ? 81.822  3.645   20.356  1.00 30.46 ? 2009 HOH A O   1 
HETATM 6932 O  O   . HOH X 8 .   ? 78.004  10.388  36.558  1.00 37.09 ? 2010 HOH A O   1 
HETATM 6933 O  O   . HOH X 8 .   ? 79.740  11.578  35.024  1.00 32.53 ? 2011 HOH A O   1 
HETATM 6934 O  O   . HOH X 8 .   ? 75.276  14.417  37.341  1.00 35.58 ? 2012 HOH A O   1 
HETATM 6935 O  O   . HOH X 8 .   ? 73.813  9.538   37.874  1.00 30.29 ? 2013 HOH A O   1 
HETATM 6936 O  O   . HOH X 8 .   ? 69.077  8.889   32.495  1.00 22.31 ? 2014 HOH A O   1 
HETATM 6937 O  O   . HOH X 8 .   ? 88.331  -0.803  22.394  1.00 30.44 ? 2015 HOH A O   1 
HETATM 6938 O  O   . HOH X 8 .   ? 96.811  2.297   33.220  1.00 38.60 ? 2016 HOH A O   1 
HETATM 6939 O  O   . HOH X 8 .   ? 94.984  9.169   33.412  1.00 29.14 ? 2017 HOH A O   1 
HETATM 6940 O  O   . HOH X 8 .   ? 99.787  -4.365  22.495  1.00 27.90 ? 2018 HOH A O   1 
HETATM 6941 O  O   . HOH X 8 .   ? 94.142  -9.941  27.473  1.00 26.43 ? 2019 HOH A O   1 
HETATM 6942 O  O   . HOH X 8 .   ? 73.237  3.778   30.586  1.00 9.65  ? 2020 HOH A O   1 
HETATM 6943 O  O   . HOH X 8 .   ? 79.578  2.182   21.383  1.00 18.94 ? 2021 HOH A O   1 
HETATM 6944 O  O   . HOH X 8 .   ? 82.663  -3.303  24.972  1.00 13.49 ? 2022 HOH A O   1 
HETATM 6945 O  O   . HOH X 8 .   ? 84.656  -0.783  24.582  1.00 15.32 ? 2023 HOH A O   1 
HETATM 6946 O  O   . HOH X 8 .   ? 66.490  -6.113  49.253  1.00 34.17 ? 2024 HOH A O   1 
HETATM 6947 O  O   . HOH X 8 .   ? 70.217  -9.930  54.008  1.00 37.96 ? 2025 HOH A O   1 
HETATM 6948 O  O   . HOH X 8 .   ? 78.417  8.387   20.344  1.00 24.46 ? 2026 HOH A O   1 
HETATM 6949 O  O   . HOH X 8 .   ? 84.432  7.718   21.148  1.00 35.11 ? 2027 HOH A O   1 
HETATM 6950 O  O   . HOH X 8 .   ? 86.291  4.154   21.757  1.00 38.08 ? 2028 HOH A O   1 
HETATM 6951 O  O   . HOH X 8 .   ? 71.678  -0.606  50.128  1.00 35.91 ? 2029 HOH A O   1 
HETATM 6952 O  O   . HOH X 8 .   ? 82.839  -4.695  52.027  1.00 34.36 ? 2030 HOH A O   1 
HETATM 6953 O  O   . HOH X 8 .   ? 80.316  -4.853  54.083  1.00 41.86 ? 2031 HOH A O   1 
HETATM 6954 O  O   . HOH X 8 .   ? 83.369  -9.212  53.708  1.00 31.12 ? 2032 HOH A O   1 
HETATM 6955 O  O   . HOH X 8 .   ? 79.550  -7.354  55.531  1.00 40.78 ? 2033 HOH A O   1 
HETATM 6956 O  O   . HOH X 8 .   ? 77.194  5.352   47.441  1.00 46.00 ? 2034 HOH A O   1 
HETATM 6957 O  O   . HOH X 8 .   ? 88.690  4.514   30.148  1.00 31.50 ? 2035 HOH A O   1 
HETATM 6958 O  O   . HOH X 8 .   ? 76.603  4.487   49.687  1.00 44.65 ? 2036 HOH A O   1 
HETATM 6959 O  O   . HOH X 8 .   ? 77.677  -4.245  53.985  1.00 44.90 ? 2037 HOH A O   1 
HETATM 6960 O  O   . HOH X 8 .   ? 86.843  0.183   43.877  1.00 39.87 ? 2038 HOH A O   1 
HETATM 6961 O  O   . HOH X 8 .   ? 88.226  -0.764  25.376  1.00 22.29 ? 2039 HOH A O   1 
HETATM 6962 O  O   . HOH X 8 .   ? 92.716  5.318   27.219  1.00 38.23 ? 2040 HOH A O   1 
HETATM 6963 O  O   . HOH X 8 .   ? 91.849  5.386   29.768  1.00 32.03 ? 2041 HOH A O   1 
HETATM 6964 O  O   . HOH X 8 .   ? 93.975  1.846   32.816  1.00 18.67 ? 2042 HOH A O   1 
HETATM 6965 O  O   . HOH X 8 .   ? 94.248  5.698   33.502  1.00 44.39 ? 2043 HOH A O   1 
HETATM 6966 O  O   . HOH X 8 .   ? 97.909  -2.438  20.874  1.00 22.64 ? 2044 HOH A O   1 
HETATM 6967 O  O   . HOH X 8 .   ? 97.222  0.372   21.045  1.00 33.62 ? 2045 HOH A O   1 
HETATM 6968 O  O   . HOH X 8 .   ? 80.583  15.430  28.327  1.00 42.55 ? 2046 HOH A O   1 
HETATM 6969 O  O   . HOH X 8 .   ? 82.631  17.684  33.437  1.00 37.54 ? 2047 HOH A O   1 
HETATM 6970 O  O   . HOH X 8 .   ? 85.982  17.774  35.600  1.00 41.79 ? 2048 HOH A O   1 
HETATM 6971 O  O   . HOH X 8 .   ? 92.118  -8.959  28.677  1.00 16.45 ? 2049 HOH A O   1 
HETATM 6972 O  O   . HOH X 8 .   ? 88.606  7.889   38.350  1.00 35.01 ? 2050 HOH A O   1 
HETATM 6973 O  O   . HOH X 8 .   ? 91.863  5.690   41.246  1.00 39.06 ? 2051 HOH A O   1 
HETATM 6974 O  O   . HOH X 8 .   ? 63.394  -16.835 30.863  1.00 21.03 ? 2052 HOH A O   1 
HETATM 6975 O  O   . HOH X 8 .   ? 63.198  -16.696 36.068  1.00 33.53 ? 2053 HOH A O   1 
HETATM 6976 O  O   . HOH X 8 .   ? 61.768  -12.077 43.766  1.00 29.41 ? 2054 HOH A O   1 
HETATM 6977 O  O   . HOH X 8 .   ? 58.961  -12.571 39.389  1.00 32.35 ? 2055 HOH A O   1 
HETATM 6978 O  O   . HOH X 8 .   ? 71.708  -18.390 41.332  1.00 47.86 ? 2056 HOH A O   1 
HETATM 6979 O  O   . HOH X 8 .   ? 60.380  -3.952  45.266  1.00 39.68 ? 2057 HOH A O   1 
HETATM 6980 O  O   . HOH X 8 .   ? 69.512  -17.791 44.954  1.00 34.86 ? 2058 HOH A O   1 
HETATM 6981 O  O   . HOH X 8 .   ? 69.348  -17.248 48.227  1.00 41.34 ? 2059 HOH A O   1 
HETATM 6982 O  O   . HOH X 8 .   ? 59.953  -9.881  44.960  1.00 34.21 ? 2060 HOH A O   1 
HETATM 6983 O  O   . HOH X 8 .   ? 55.899  -3.643  41.061  1.00 40.98 ? 2061 HOH A O   1 
HETATM 6984 O  O   . HOH X 8 .   ? 68.298  -12.403 49.950  1.00 34.14 ? 2062 HOH A O   1 
HETATM 6985 O  O   . HOH X 8 .   ? 75.741  -14.173 50.204  1.00 28.27 ? 2063 HOH A O   1 
HETATM 6986 O  O   . HOH X 8 .   ? 57.027  -0.058  34.470  1.00 36.10 ? 2064 HOH A O   1 
HETATM 6987 O  O   . HOH X 8 .   ? 54.338  0.641   32.140  1.00 40.96 ? 2065 HOH A O   1 
HETATM 6988 O  O   . HOH X 8 .   ? 54.587  -1.241  29.554  1.00 35.68 ? 2066 HOH A O   1 
HETATM 6989 O  O   . HOH X 8 .   ? 60.486  -8.971  18.347  1.00 26.83 ? 2067 HOH A O   1 
HETATM 6990 O  O   . HOH X 8 .   ? 66.539  -8.302  47.667  1.00 26.34 ? 2068 HOH A O   1 
HETATM 6991 O  O   . HOH X 8 .   ? 69.641  -5.155  50.347  1.00 29.42 ? 2069 HOH A O   1 
HETATM 6992 O  O   . HOH X 8 .   ? 72.202  -8.628  53.361  1.00 37.87 ? 2070 HOH A O   1 
HETATM 6993 O  O   . HOH X 8 .   ? 66.732  -20.330 26.745  1.00 24.11 ? 2071 HOH A O   1 
HETATM 6994 O  O   . HOH X 8 .   ? 67.815  -23.705 19.192  1.00 27.46 ? 2072 HOH A O   1 
HETATM 6995 O  O   . HOH X 8 .   ? 61.826  -13.429 16.633  1.00 39.70 ? 2073 HOH A O   1 
HETATM 6996 O  O   . HOH X 8 .   ? 74.617  -0.226  50.282  1.00 24.38 ? 2074 HOH A O   1 
HETATM 6997 O  O   . HOH X 8 .   ? 73.519  -6.668  52.786  1.00 34.50 ? 2075 HOH A O   1 
HETATM 6998 O  O   . HOH X 8 .   ? 70.571  -18.634 0.668   1.00 25.38 ? 2076 HOH A O   1 
HETATM 6999 O  O   . HOH X 8 .   ? 81.239  -3.017  50.868  1.00 35.51 ? 2077 HOH A O   1 
HETATM 7000 O  O   . HOH X 8 .   ? 81.917  -7.190  51.792  1.00 24.61 ? 2078 HOH A O   1 
HETATM 7001 O  O   . HOH X 8 .   ? 78.783  -8.724  53.154  1.00 36.03 ? 2079 HOH A O   1 
HETATM 7002 O  O   . HOH X 8 .   ? 74.877  4.167   45.219  1.00 25.46 ? 2080 HOH A O   1 
HETATM 7003 O  O   . HOH X 8 .   ? 79.707  3.770   48.753  1.00 35.46 ? 2081 HOH A O   1 
HETATM 7004 O  O   . HOH X 8 .   ? 75.149  2.569   49.695  1.00 37.16 ? 2082 HOH A O   1 
HETATM 7005 O  O   . HOH X 8 .   ? 79.064  -2.053  51.624  1.00 35.06 ? 2083 HOH A O   1 
HETATM 7006 O  O   . HOH X 8 .   ? 69.484  -19.594 37.445  1.00 27.87 ? 2084 HOH A O   1 
HETATM 7007 O  O   . HOH X 8 .   ? 65.255  -21.246 35.326  1.00 31.31 ? 2085 HOH A O   1 
HETATM 7008 O  O   . HOH X 8 .   ? 84.212  0.641   44.455  1.00 26.30 ? 2086 HOH A O   1 
HETATM 7009 O  O   . HOH X 8 .   ? 82.382  0.236   50.263  1.00 44.32 ? 2087 HOH A O   1 
HETATM 7010 O  O   . HOH X 8 .   ? 79.455  6.182   38.828  1.00 21.79 ? 2088 HOH A O   1 
HETATM 7011 O  O   . HOH X 8 .   ? 84.963  3.108   36.163  1.00 14.87 ? 2089 HOH A O   1 
HETATM 7012 O  O   . HOH X 8 .   ? 85.020  5.640   37.370  1.00 32.93 ? 2090 HOH A O   1 
HETATM 7013 O  O   . HOH X 8 .   ? 98.911  -3.356  38.540  1.00 34.59 ? 2091 HOH A O   1 
HETATM 7014 O  O   . HOH X 8 .   ? 102.021 -3.891  30.591  1.00 39.11 ? 2092 HOH A O   1 
HETATM 7015 O  O   . HOH X 8 .   ? 95.263  -2.651  41.429  1.00 29.10 ? 2093 HOH A O   1 
HETATM 7016 O  O   . HOH X 8 .   ? 83.468  15.010  29.362  1.00 24.29 ? 2094 HOH A O   1 
HETATM 7017 O  O   . HOH X 8 .   ? 83.118  -13.939 51.303  1.00 37.36 ? 2095 HOH A O   1 
HETATM 7018 O  O   . HOH X 8 .   ? 84.578  -12.946 54.493  1.00 41.81 ? 2096 HOH A O   1 
HETATM 7019 O  O   . HOH X 8 .   ? 88.857  10.527  26.512  1.00 30.61 ? 2097 HOH A O   1 
HETATM 7020 O  O   . HOH X 8 .   ? 88.876  15.570  26.974  1.00 24.59 ? 2098 HOH A O   1 
HETATM 7021 O  O   . HOH X 8 .   ? 80.829  12.126  24.536  1.00 29.40 ? 2099 HOH A O   1 
HETATM 7022 O  O   . HOH X 8 .   ? 89.975  17.636  29.615  1.00 28.25 ? 2100 HOH A O   1 
HETATM 7023 O  O   . HOH X 8 .   ? 83.921  16.205  31.540  1.00 26.07 ? 2101 HOH A O   1 
HETATM 7024 O  O   . HOH X 8 .   ? 88.193  18.351  34.077  1.00 42.65 ? 2102 HOH A O   1 
HETATM 7025 O  O   . HOH X 8 .   ? 82.641  -23.009 23.245  1.00 29.35 ? 2103 HOH A O   1 
HETATM 7026 O  O   . HOH X 8 .   ? 92.980  10.647  32.732  1.00 26.36 ? 2104 HOH A O   1 
HETATM 7027 O  O   . HOH X 8 .   ? 93.722  11.418  35.535  1.00 39.83 ? 2105 HOH A O   1 
HETATM 7028 O  O   . HOH X 8 .   ? 90.891  11.116  37.901  1.00 36.64 ? 2106 HOH A O   1 
HETATM 7029 O  O   . HOH X 8 .   ? 84.560  13.791  33.704  1.00 30.08 ? 2107 HOH A O   1 
HETATM 7030 O  O   . HOH X 8 .   ? 90.775  8.361   26.974  1.00 35.43 ? 2108 HOH A O   1 
HETATM 7031 O  O   . HOH X 8 .   ? 97.403  -5.013  6.163   1.00 25.77 ? 2109 HOH A O   1 
HETATM 7032 O  O   . HOH X 8 .   ? 94.000  4.357   10.954  1.00 23.21 ? 2110 HOH A O   1 
HETATM 7033 O  O   . HOH X 8 .   ? 89.547  2.795   38.629  1.00 20.63 ? 2111 HOH A O   1 
HETATM 7034 O  O   . HOH X 8 .   ? 90.785  5.553   38.606  1.00 22.85 ? 2112 HOH A O   1 
HETATM 7035 O  O   . HOH X 8 .   ? 92.142  -9.956  3.052   1.00 19.64 ? 2113 HOH A O   1 
HETATM 7036 O  O   . HOH X 8 .   ? 87.598  2.297   39.609  1.00 29.23 ? 2114 HOH A O   1 
HETATM 7037 O  O   . HOH X 8 .   ? 86.404  8.958   13.761  1.00 21.41 ? 2115 HOH A O   1 
HETATM 7038 O  O   . HOH X 8 .   ? 77.442  -0.727  28.923  1.00 14.72 ? 2116 HOH A O   1 
HETATM 7039 O  O   . HOH X 8 .   ? 70.209  -15.137 30.767  1.00 12.92 ? 2117 HOH A O   1 
HETATM 7040 O  O   . HOH X 8 .   ? 67.996  -11.499 28.656  1.00 9.00  ? 2118 HOH A O   1 
HETATM 7041 O  O   . HOH X 8 .   ? 67.729  -13.830 30.337  1.00 10.81 ? 2119 HOH A O   1 
HETATM 7042 O  O   . HOH X 8 .   ? 60.717  -10.183 33.124  1.00 21.42 ? 2120 HOH A O   1 
HETATM 7043 O  O   . HOH X 8 .   ? 63.033  -7.874  32.069  1.00 14.52 ? 2121 HOH A O   1 
HETATM 7044 O  O   . HOH X 8 .   ? 65.167  -14.731 30.165  1.00 12.03 ? 2122 HOH A O   1 
HETATM 7045 O  O   . HOH X 8 .   ? 65.776  -15.300 37.690  1.00 16.68 ? 2123 HOH A O   1 
HETATM 7046 O  O   . HOH X 8 .   ? 61.256  -11.551 40.869  1.00 32.52 ? 2124 HOH A O   1 
HETATM 7047 O  O   . HOH X 8 .   ? 64.518  -11.301 44.708  1.00 23.71 ? 2125 HOH A O   1 
HETATM 7048 O  O   . HOH X 8 .   ? 63.107  -5.484  43.728  1.00 17.74 ? 2126 HOH A O   1 
HETATM 7049 O  O   . HOH X 8 .   ? 64.949  -8.469  45.381  1.00 24.16 ? 2127 HOH A O   1 
HETATM 7050 O  O   . HOH X 8 .   ? 56.162  7.147   25.085  1.00 25.20 ? 2128 HOH A O   1 
HETATM 7051 O  O   . HOH X 8 .   ? 59.327  -4.411  39.762  1.00 14.34 ? 2129 HOH A O   1 
HETATM 7052 O  O   . HOH X 8 .   ? 59.466  -7.515  43.344  1.00 29.86 ? 2130 HOH A O   1 
HETATM 7053 O  O   . HOH X 8 .   ? 53.675  -1.870  27.285  1.00 35.42 ? 2131 HOH A O   1 
HETATM 7054 O  O   . HOH X 8 .   ? 52.204  -0.208  26.269  1.00 35.59 ? 2132 HOH A O   1 
HETATM 7055 O  O   . HOH X 8 .   ? 61.748  -7.609  34.479  1.00 15.56 ? 2133 HOH A O   1 
HETATM 7056 O  O   . HOH X 8 .   ? 58.159  -9.916  34.671  1.00 23.91 ? 2134 HOH A O   1 
HETATM 7057 O  O   . HOH X 8 .   ? 56.499  -5.104  37.701  1.00 21.45 ? 2135 HOH A O   1 
HETATM 7058 O  O   . HOH X 8 .   ? 56.889  -7.787  41.362  1.00 24.57 ? 2136 HOH A O   1 
HETATM 7059 O  O   . HOH X 8 .   ? 63.442  4.642   40.089  1.00 20.34 ? 2137 HOH A O   1 
HETATM 7060 O  O   . HOH X 8 .   ? 54.870  -9.541  37.823  1.00 32.48 ? 2138 HOH A O   1 
HETATM 7061 O  O   . HOH X 8 .   ? 58.994  -8.510  31.364  1.00 27.30 ? 2139 HOH A O   1 
HETATM 7062 O  O   . HOH X 8 .   ? 61.053  -7.091  30.394  1.00 15.12 ? 2140 HOH A O   1 
HETATM 7063 O  O   . HOH X 8 .   ? 59.895  -1.009  39.596  1.00 13.65 ? 2141 HOH A O   1 
HETATM 7064 O  O   . HOH X 8 .   ? 56.294  -2.743  33.718  1.00 24.86 ? 2142 HOH A O   1 
HETATM 7065 O  O   . HOH X 8 .   ? 57.022  -0.495  30.994  1.00 28.90 ? 2143 HOH A O   1 
HETATM 7066 O  O   . HOH X 8 .   ? 57.179  -1.629  28.550  1.00 30.50 ? 2144 HOH A O   1 
HETATM 7067 O  O   . HOH X 8 .   ? 56.019  -5.906  25.507  1.00 31.71 ? 2145 HOH A O   1 
HETATM 7068 O  O   . HOH X 8 .   ? 61.438  -6.597  27.860  1.00 14.25 ? 2146 HOH A O   1 
HETATM 7069 O  O   . HOH X 8 .   ? 62.483  -2.664  22.991  1.00 12.02 ? 2147 HOH A O   1 
HETATM 7070 O  O   . HOH X 8 .   ? 62.916  -5.337  20.282  1.00 11.68 ? 2148 HOH A O   1 
HETATM 7071 O  O   . HOH X 8 .   ? 61.534  -7.602  20.639  1.00 15.37 ? 2149 HOH A O   1 
HETATM 7072 O  O   . HOH X 8 .   ? 59.152  -6.483  21.716  1.00 23.20 ? 2150 HOH A O   1 
HETATM 7073 O  O   . HOH X 8 .   ? 97.222  -15.631 2.626   1.00 24.00 ? 2151 HOH A O   1 
HETATM 7074 O  O   . HOH X 8 .   ? 99.017  -13.452 4.933   1.00 43.55 ? 2152 HOH A O   1 
HETATM 7075 O  O   . HOH X 8 .   ? 99.637  -19.996 2.606   1.00 23.28 ? 2153 HOH A O   1 
HETATM 7076 O  O   . HOH X 8 .   ? 93.422  -26.993 4.806   1.00 24.41 ? 2154 HOH A O   1 
HETATM 7077 O  O   . HOH X 8 .   ? 65.169  -13.764 22.159  1.00 13.92 ? 2155 HOH A O   1 
HETATM 7078 O  O   . HOH X 8 .   ? 87.005  -17.008 -10.606 1.00 28.10 ? 2156 HOH A O   1 
HETATM 7079 O  O   . HOH X 8 .   ? 89.169  -8.433  -11.349 1.00 29.16 ? 2157 HOH A O   1 
HETATM 7080 O  O   . HOH X 8 .   ? 63.127  -17.595 27.711  1.00 15.24 ? 2158 HOH A O   1 
HETATM 7081 O  O   . HOH X 8 .   ? 67.009  -17.829 25.779  1.00 12.72 ? 2159 HOH A O   1 
HETATM 7082 O  O   . HOH X 8 .   ? 62.826  -14.835 21.112  1.00 20.83 ? 2160 HOH A O   1 
HETATM 7083 O  O   . HOH X 8 .   ? 94.873  -17.059 -13.363 1.00 31.76 ? 2161 HOH A O   1 
HETATM 7084 O  O   . HOH X 8 .   ? 94.455  -6.852  -8.561  1.00 23.19 ? 2162 HOH A O   1 
HETATM 7085 O  O   . HOH X 8 .   ? 101.257 -6.384  -10.388 1.00 40.58 ? 2163 HOH A O   1 
HETATM 7086 O  O   . HOH X 8 .   ? 93.291  -4.044  -13.144 1.00 32.58 ? 2164 HOH A O   1 
HETATM 7087 O  O   . HOH X 8 .   ? 69.506  -16.931 26.576  1.00 11.38 ? 2165 HOH A O   1 
HETATM 7088 O  O   . HOH X 8 .   ? 66.586  -21.055 19.231  1.00 20.22 ? 2166 HOH A O   1 
HETATM 7089 O  O   . HOH X 8 .   ? 64.874  -18.238 17.234  1.00 23.72 ? 2167 HOH A O   1 
HETATM 7090 O  O   . HOH X 8 .   ? 62.983  -14.979 18.438  1.00 23.67 ? 2168 HOH A O   1 
HETATM 7091 O  O   . HOH X 8 .   ? 64.843  -16.439 9.573   1.00 33.94 ? 2169 HOH A O   1 
HETATM 7092 O  O   . HOH X 8 .   ? 68.444  -15.971 9.739   1.00 17.56 ? 2170 HOH A O   1 
HETATM 7093 O  O   . HOH X 8 .   ? 89.557  -5.394  -9.957  1.00 22.01 ? 2171 HOH A O   1 
HETATM 7094 O  O   . HOH X 8 .   ? 96.831  -4.914  -8.297  1.00 22.17 ? 2172 HOH A O   1 
HETATM 7095 O  O   . HOH X 8 .   ? 93.870  -2.515  -11.135 1.00 26.86 ? 2173 HOH A O   1 
HETATM 7096 O  O   . HOH X 8 .   ? 74.946  -21.551 10.907  1.00 18.49 ? 2174 HOH A O   1 
HETATM 7097 O  O   . HOH X 8 .   ? 69.067  -18.413 2.640   1.00 20.53 ? 2175 HOH A O   1 
HETATM 7098 O  O   . HOH X 8 .   ? 70.183  -17.636 5.231   1.00 14.88 ? 2176 HOH A O   1 
HETATM 7099 O  O   . HOH X 8 .   ? 97.643  6.297   8.626   1.00 32.47 ? 2177 HOH A O   1 
HETATM 7100 O  O   . HOH X 8 .   ? 93.652  12.051  8.016   1.00 26.76 ? 2178 HOH A O   1 
HETATM 7101 O  O   . HOH X 8 .   ? 96.372  6.073   11.318  1.00 33.99 ? 2179 HOH A O   1 
HETATM 7102 O  O   . HOH X 8 .   ? 88.785  10.548  14.002  1.00 30.80 ? 2180 HOH A O   1 
HETATM 7103 O  O   . HOH X 8 .   ? 75.415  -23.109 13.159  1.00 30.55 ? 2181 HOH A O   1 
HETATM 7104 O  O   . HOH X 8 .   ? 70.999  -28.007 16.072  1.00 32.42 ? 2182 HOH A O   1 
HETATM 7105 O  O   . HOH X 8 .   ? 75.923  -25.908 24.081  1.00 38.52 ? 2183 HOH A O   1 
HETATM 7106 O  O   . HOH X 8 .   ? 72.318  -27.539 22.295  1.00 40.11 ? 2184 HOH A O   1 
HETATM 7107 O  O   . HOH X 8 .   ? 68.784  -24.563 21.476  1.00 32.56 ? 2185 HOH A O   1 
HETATM 7108 O  O   . HOH X 8 .   ? 79.843  -25.975 22.645  1.00 27.91 ? 2186 HOH A O   1 
HETATM 7109 O  O   . HOH X 8 .   ? 83.396  10.946  -3.804  1.00 21.68 ? 2187 HOH A O   1 
HETATM 7110 O  O   . HOH X 8 .   ? 86.536  10.676  -2.099  1.00 36.41 ? 2188 HOH A O   1 
HETATM 7111 O  O   . HOH X 8 .   ? 73.387  11.887  -7.811  1.00 29.54 ? 2189 HOH A O   1 
HETATM 7112 O  O   . HOH X 8 .   ? 73.315  -23.503 30.103  1.00 27.74 ? 2190 HOH A O   1 
HETATM 7113 O  O   . HOH X 8 .   ? 72.653  -21.334 31.511  1.00 28.76 ? 2191 HOH A O   1 
HETATM 7114 O  O   . HOH X 8 .   ? 72.814  -17.945 30.470  1.00 13.70 ? 2192 HOH A O   1 
HETATM 7115 O  O   . HOH X 8 .   ? 83.980  -22.270 30.163  1.00 35.37 ? 2193 HOH A O   1 
HETATM 7116 O  O   . HOH X 8 .   ? 86.334  -0.071  -10.894 1.00 23.66 ? 2194 HOH A O   1 
HETATM 7117 O  O   . HOH X 8 .   ? 85.881  -3.767  -12.543 1.00 26.48 ? 2195 HOH A O   1 
HETATM 7118 O  O   . HOH X 8 .   ? 82.907  -0.455  -15.035 1.00 24.77 ? 2196 HOH A O   1 
HETATM 7119 O  O   . HOH X 8 .   ? 72.740  -16.731 28.085  1.00 17.54 ? 2197 HOH A O   1 
HETATM 7120 O  O   . HOH X 8 .   ? 68.930  -22.147 31.562  1.00 21.63 ? 2198 HOH A O   1 
HETATM 7121 O  O   . HOH X 8 .   ? 68.507  -17.661 35.921  1.00 27.46 ? 2199 HOH A O   1 
HETATM 7122 O  O   . HOH X 8 .   ? 67.171  -19.354 34.353  1.00 31.46 ? 2200 HOH A O   1 
HETATM 7123 O  O   . HOH X 8 .   ? 71.940  -18.819 37.629  1.00 22.97 ? 2201 HOH A O   1 
HETATM 7124 O  O   . HOH X 8 .   ? 100.712 -4.608  34.658  1.00 33.22 ? 2202 HOH A O   1 
HETATM 7125 O  O   . HOH X 8 .   ? 99.267  -2.742  35.899  1.00 21.01 ? 2203 HOH A O   1 
HETATM 7126 O  O   . HOH X 8 .   ? 99.423  0.869   33.064  1.00 36.21 ? 2204 HOH A O   1 
HETATM 7127 O  O   . HOH X 8 .   ? 98.389  -6.575  30.483  1.00 20.85 ? 2205 HOH A O   1 
HETATM 7128 O  O   . HOH X 8 .   ? 99.248  -6.716  33.217  1.00 23.36 ? 2206 HOH A O   1 
HETATM 7129 O  O   . HOH X 8 .   ? 98.147  -8.829  29.490  1.00 22.95 ? 2207 HOH A O   1 
HETATM 7130 O  O   . HOH X 8 .   ? 99.373  -9.385  33.447  1.00 30.55 ? 2208 HOH A O   1 
HETATM 7131 O  O   . HOH X 8 .   ? 96.884  -4.535  39.812  1.00 28.19 ? 2209 HOH A O   1 
HETATM 7132 O  O   . HOH X 8 .   ? 100.040 -11.564 36.452  1.00 31.42 ? 2210 HOH A O   1 
HETATM 7133 O  O   . HOH X 8 .   ? 97.402  -10.666 37.193  1.00 32.67 ? 2211 HOH A O   1 
HETATM 7134 O  O   . HOH X 8 .   ? 102.824 -6.059  35.358  1.00 33.80 ? 2212 HOH A O   1 
HETATM 7135 O  O   . HOH X 8 .   ? 92.748  -2.634  39.927  1.00 27.16 ? 2213 HOH A O   1 
HETATM 7136 O  O   . HOH X 8 .   ? 91.629  -12.060 40.496  1.00 24.90 ? 2214 HOH A O   1 
HETATM 7137 O  O   . HOH X 8 .   ? 92.731  -10.676 33.122  1.00 34.03 ? 2215 HOH A O   1 
HETATM 7138 O  O   . HOH X 8 .   ? 94.739  -29.057 18.940  1.00 27.58 ? 2216 HOH A O   1 
HETATM 7139 O  O   . HOH X 8 .   ? 91.240  -3.064  43.114  1.00 33.73 ? 2217 HOH A O   1 
HETATM 7140 O  O   . HOH X 8 .   ? 97.993  -5.983  41.935  1.00 29.52 ? 2218 HOH A O   1 
HETATM 7141 O  O   . HOH X 8 .   ? 92.114  -4.818  45.703  1.00 27.39 ? 2219 HOH A O   1 
HETATM 7142 O  O   . HOH X 8 .   ? 90.598  0.540   40.175  1.00 31.70 ? 2220 HOH A O   1 
HETATM 7143 O  O   . HOH X 8 .   ? 87.861  -5.485  48.648  1.00 21.86 ? 2221 HOH A O   1 
HETATM 7144 O  O   . HOH X 8 .   ? 82.807  -14.273 45.151  1.00 32.06 ? 2222 HOH A O   1 
HETATM 7145 O  O   . HOH X 8 .   ? 87.547  -14.802 39.149  1.00 17.67 ? 2223 HOH A O   1 
HETATM 7146 O  O   . HOH X 8 .   ? 82.997  -11.257 51.818  1.00 40.21 ? 2224 HOH A O   1 
HETATM 7147 O  O   . HOH X 8 .   ? 86.550  -10.550 51.459  1.00 26.28 ? 2225 HOH A O   1 
HETATM 7148 O  O   . HOH X 8 .   ? 60.605  -10.153 6.855   1.00 30.42 ? 2226 HOH A O   1 
HETATM 7149 O  O   . HOH X 8 .   ? 78.271  -12.366 51.525  1.00 39.97 ? 2227 HOH A O   1 
HETATM 7150 O  O   . HOH X 8 .   ? 80.221  -14.189 51.442  1.00 27.74 ? 2228 HOH A O   1 
HETATM 7151 O  O   . HOH X 8 .   ? 83.497  -15.888 49.210  1.00 27.67 ? 2229 HOH A O   1 
HETATM 7152 O  O   . HOH X 8 .   ? 80.254  -17.592 45.324  1.00 31.79 ? 2230 HOH A O   1 
HETATM 7153 O  O   . HOH X 8 .   ? 82.505  -17.170 41.761  1.00 23.14 ? 2231 HOH A O   1 
HETATM 7154 O  O   . HOH X 8 .   ? 88.423  -13.764 35.106  1.00 37.72 ? 2232 HOH A O   1 
HETATM 7155 O  O   . HOH X 8 .   ? 79.846  -22.060 35.331  1.00 27.77 ? 2233 HOH A O   1 
HETATM 7156 O  O   . HOH X 8 .   ? 84.831  -20.588 24.100  1.00 24.28 ? 2234 HOH A O   1 
HETATM 7157 O  O   . HOH X 8 .   ? 86.973  -17.412 28.180  1.00 27.35 ? 2235 HOH A O   1 
HETATM 7158 O  O   . HOH X 8 .   ? 88.813  -14.751 31.013  1.00 25.59 ? 2236 HOH A O   1 
HETATM 7159 O  O   . HOH X 8 .   ? 71.370  -18.149 -3.681  1.00 29.70 ? 2237 HOH A O   1 
HETATM 7160 O  O   . HOH X 8 .   ? 89.125  -15.612 27.946  1.00 25.25 ? 2238 HOH A O   1 
HETATM 7161 O  O   . HOH X 8 .   ? 91.332  -13.465 24.941  1.00 24.76 ? 2239 HOH A O   1 
HETATM 7162 O  O   . HOH X 8 .   ? 92.924  -11.480 25.258  1.00 26.54 ? 2240 HOH A O   1 
HETATM 7163 O  O   . HOH X 8 .   ? 91.090  -9.724  31.071  1.00 20.96 ? 2241 HOH A O   1 
HETATM 7164 O  O   . HOH X 8 .   ? 93.386  -9.340  20.607  1.00 18.99 ? 2242 HOH A O   1 
HETATM 7165 O  O   . HOH X 8 .   ? 93.111  -11.019 22.596  1.00 18.36 ? 2243 HOH A O   1 
HETATM 7166 O  O   . HOH X 8 .   ? 97.201  -7.825  21.837  1.00 25.03 ? 2244 HOH A O   1 
HETATM 7167 O  O   . HOH X 8 .   ? 92.430  -4.097  17.660  1.00 12.87 ? 2245 HOH A O   1 
HETATM 7168 O  O   . HOH X 8 .   ? 97.158  -12.623 14.133  1.00 11.70 ? 2246 HOH A O   1 
HETATM 7169 O  O   . HOH X 8 .   ? 87.190  -24.105 5.676   1.00 36.45 ? 2247 HOH A O   1 
HETATM 7170 O  O   . HOH X 8 .   ? 85.604  -25.922 4.540   1.00 36.72 ? 2248 HOH A O   1 
HETATM 7171 O  O   . HOH X 8 .   ? 99.701  -0.413  19.246  1.00 26.88 ? 2249 HOH A O   1 
HETATM 7172 O  O   . HOH X 8 .   ? 103.533 -3.531  14.614  1.00 33.40 ? 2250 HOH A O   1 
HETATM 7173 O  O   . HOH X 8 .   ? 95.966  -5.655  8.487   1.00 16.33 ? 2251 HOH A O   1 
HETATM 7174 O  O   . HOH X 8 .   ? 70.277  1.155   48.481  1.00 42.50 ? 2252 HOH A O   1 
HETATM 7175 O  O   . HOH X 8 .   ? 95.768  1.214   10.426  1.00 20.75 ? 2253 HOH A O   1 
HETATM 7176 O  O   . HOH X 8 .   ? 96.908  -0.030  8.573   1.00 34.94 ? 2254 HOH A O   1 
HETATM 7177 O  O   . HOH X 8 .   ? 88.403  -9.852  15.872  1.00 10.08 ? 2255 HOH A O   1 
HETATM 7178 O  O   . HOH X 8 .   ? 92.826  -11.239 5.837   1.00 16.08 ? 2256 HOH A O   1 
HETATM 7179 O  O   . HOH X 8 .   ? 88.153  -1.775  7.319   1.00 9.30  ? 2257 HOH A O   1 
HETATM 7180 O  O   . HOH X 8 .   ? 88.831  0.084   17.030  1.00 29.15 ? 2258 HOH A O   1 
HETATM 7181 O  O   . HOH X 8 .   ? 83.612  -3.252  16.648  1.00 27.61 ? 2259 HOH A O   1 
HETATM 7182 O  O   . HOH X 8 .   ? 87.327  -4.464  17.549  1.00 20.58 ? 2260 HOH A O   1 
HETATM 7183 O  O   . HOH X 8 .   ? 89.868  -2.981  18.078  1.00 17.78 ? 2261 HOH A O   1 
HETATM 7184 O  O   . HOH X 8 .   ? 84.040  -0.536  16.858  1.00 37.27 ? 2262 HOH A O   1 
HETATM 7185 O  O   . HOH X 8 .   ? 84.065  3.450   17.171  1.00 23.17 ? 2263 HOH A O   1 
HETATM 7186 O  O   . HOH X 8 .   ? 81.467  7.057   12.390  1.00 11.45 ? 2264 HOH A O   1 
HETATM 7187 O  O   . HOH X 8 .   ? 85.282  7.516   11.712  1.00 14.60 ? 2265 HOH A O   1 
HETATM 7188 O  O   . HOH X 8 .   ? 77.928  0.864   14.056  1.00 10.74 ? 2266 HOH A O   1 
HETATM 7189 O  O   . HOH X 8 .   ? 76.837  6.062   10.316  1.00 8.47  ? 2267 HOH A O   1 
HETATM 7190 O  O   . HOH X 8 .   ? 75.184  4.113   11.274  1.00 9.10  ? 2268 HOH A O   1 
HETATM 7191 O  O   . HOH X 8 .   ? 78.367  8.270   17.580  1.00 20.76 ? 2269 HOH A O   1 
HETATM 7192 O  O   . HOH X 8 .   ? 68.307  12.936  19.243  1.00 16.80 ? 2270 HOH A O   1 
HETATM 7193 O  O   . HOH X 8 .   ? 66.689  13.869  17.310  1.00 25.49 ? 2271 HOH A O   1 
HETATM 7194 O  O   . HOH X 8 .   ? 73.916  16.745  15.929  1.00 24.01 ? 2272 HOH A O   1 
HETATM 7195 O  O   . HOH X 8 .   ? 80.324  12.215  14.656  1.00 22.89 ? 2273 HOH A O   1 
HETATM 7196 O  O   . HOH X 8 .   ? 76.837  13.070  8.182   1.00 11.88 ? 2274 HOH A O   1 
HETATM 7197 O  O   . HOH X 8 .   ? 84.002  10.360  6.235   1.00 12.88 ? 2275 HOH A O   1 
HETATM 7198 O  O   . HOH X 8 .   ? 78.024  14.031  4.671   1.00 16.31 ? 2276 HOH A O   1 
HETATM 7199 O  O   . HOH X 8 .   ? 76.401  8.536   3.437   1.00 11.40 ? 2277 HOH A O   1 
HETATM 7200 O  O   . HOH X 8 .   ? 81.918  7.901   15.030  1.00 17.45 ? 2278 HOH A O   1 
HETATM 7201 O  O   . HOH X 8 .   ? 68.618  8.281   9.722   1.00 13.61 ? 2279 HOH A O   1 
HETATM 7202 O  O   . HOH X 8 .   ? 72.049  5.372   5.643   1.00 11.01 ? 2280 HOH A O   1 
HETATM 7203 O  O   . HOH X 8 .   ? 72.638  3.533   10.096  1.00 10.59 ? 2281 HOH A O   1 
HETATM 7204 O  O   . HOH X 8 .   ? 66.377  8.157   13.644  1.00 17.68 ? 2282 HOH A O   1 
HETATM 7205 O  O   . HOH X 8 .   ? 64.028  7.801   14.738  1.00 30.19 ? 2283 HOH A O   1 
HETATM 7206 O  O   . HOH X 8 .   ? 63.539  2.967   19.963  1.00 12.89 ? 2284 HOH A O   1 
HETATM 7207 O  O   . HOH X 8 .   ? 66.822  0.431   18.101  1.00 9.24  ? 2285 HOH A O   1 
HETATM 7208 O  O   . HOH X 8 .   ? 61.100  8.833   28.200  1.00 20.98 ? 2286 HOH A O   1 
HETATM 7209 O  O   . HOH X 8 .   ? 67.019  11.887  24.530  1.00 23.95 ? 2287 HOH A O   1 
HETATM 7210 O  O   . HOH X 8 .   ? 68.551  13.817  22.615  1.00 30.95 ? 2288 HOH A O   1 
HETATM 7211 O  O   . HOH X 8 .   ? 63.302  6.276   16.819  1.00 31.88 ? 2289 HOH A O   1 
HETATM 7212 O  O   . HOH X 8 .   ? 60.125  5.574   25.135  1.00 17.19 ? 2290 HOH A O   1 
HETATM 7213 O  O   . HOH X 8 .   ? 55.060  4.661   24.354  1.00 15.83 ? 2291 HOH A O   1 
HETATM 7214 O  O   . HOH X 8 .   ? 55.142  0.615   24.235  1.00 15.91 ? 2292 HOH A O   1 
HETATM 7215 O  O   . HOH X 8 .   ? 56.082  -1.603  26.287  1.00 33.39 ? 2293 HOH A O   1 
HETATM 7216 O  O   . HOH X 8 .   ? 52.392  2.183   27.403  1.00 13.76 ? 2294 HOH A O   1 
HETATM 7217 O  O   . HOH X 8 .   ? 65.062  7.725   36.420  1.00 29.66 ? 2295 HOH A O   1 
HETATM 7218 O  O   . HOH X 8 .   ? 66.339  7.098   34.450  1.00 27.87 ? 2296 HOH A O   1 
HETATM 7219 O  O   . HOH X 8 .   ? 62.103  6.177   38.273  1.00 16.03 ? 2297 HOH A O   1 
HETATM 7220 O  O   . HOH X 8 .   ? 67.085  5.444   37.184  1.00 21.17 ? 2298 HOH A O   1 
HETATM 7221 O  O   . HOH X 8 .   ? 76.148  -13.042 14.701  1.00 14.57 ? 2299 HOH A O   1 
HETATM 7222 O  O   . HOH X 8 .   ? 89.486  -19.269 15.996  1.00 14.31 ? 2300 HOH A O   1 
HETATM 7223 O  O   . HOH X 8 .   ? 91.566  -18.476 13.675  1.00 8.79  ? 2301 HOH A O   1 
HETATM 7224 O  O   . HOH X 8 .   ? 96.155  -19.429 5.642   1.00 17.21 ? 2302 HOH A O   1 
HETATM 7225 O  O   . HOH X 8 .   ? 89.829  -22.207 3.581   1.00 20.07 ? 2303 HOH A O   1 
HETATM 7226 O  O   . HOH X 8 .   ? 89.575  -25.347 12.766  1.00 30.86 ? 2304 HOH A O   1 
HETATM 7227 O  O   . HOH X 8 .   ? 95.365  -14.329 1.579   1.00 24.04 ? 2305 HOH A O   1 
HETATM 7228 O  O   . HOH X 8 .   ? 96.556  -16.764 8.709   1.00 18.75 ? 2306 HOH A O   1 
HETATM 7229 O  O   . HOH X 8 .   ? 96.995  -11.918 6.182   1.00 36.67 ? 2307 HOH A O   1 
HETATM 7230 O  O   . HOH X 8 .   ? 96.787  -18.484 3.095   1.00 25.15 ? 2308 HOH A O   1 
HETATM 7231 O  O   . HOH X 8 .   ? 95.670  -26.402 3.706   1.00 17.73 ? 2309 HOH A O   1 
HETATM 7232 O  O   . HOH X 8 .   ? 84.459  -21.849 -3.598  1.00 29.59 ? 2310 HOH A O   1 
HETATM 7233 O  O   . HOH X 8 .   ? 93.683  -18.454 -6.963  1.00 23.72 ? 2311 HOH A O   1 
HETATM 7234 O  O   . HOH X 8 .   ? 88.970  -22.977 -5.308  1.00 36.90 ? 2312 HOH A O   1 
HETATM 7235 O  O   . HOH X 8 .   ? 90.001  -20.680 -8.593  1.00 38.63 ? 2313 HOH A O   1 
HETATM 7236 O  O   . HOH X 8 .   ? 90.180  -22.676 -0.044  1.00 26.26 ? 2314 HOH A O   1 
HETATM 7237 O  O   . HOH X 8 .   ? 86.677  -17.102 -7.919  1.00 19.80 ? 2315 HOH A O   1 
HETATM 7238 O  O   . HOH X 8 .   ? 86.425  -19.796 -7.236  1.00 14.95 ? 2316 HOH A O   1 
HETATM 7239 O  O   . HOH X 8 .   ? 87.951  -22.908 -1.788  1.00 15.01 ? 2317 HOH A O   1 
HETATM 7240 O  O   . HOH X 8 .   ? 88.470  -15.241 -12.174 1.00 30.25 ? 2318 HOH A O   1 
HETATM 7241 O  O   . HOH X 8 .   ? 91.503  -9.376  -10.931 1.00 18.95 ? 2319 HOH A O   1 
HETATM 7242 O  O   . HOH X 8 .   ? 95.224  -14.505 -13.786 1.00 23.36 ? 2320 HOH A O   1 
HETATM 7243 O  O   . HOH X 8 .   ? 94.374  -8.048  -11.118 1.00 16.28 ? 2321 HOH A O   1 
HETATM 7244 O  O   . HOH X 8 .   ? 101.590 -9.069  -11.182 1.00 31.67 ? 2322 HOH A O   1 
HETATM 7245 O  O   . HOH X 8 .   ? 95.060  -5.863  -12.910 1.00 29.19 ? 2323 HOH A O   1 
HETATM 7246 O  O   . HOH X 8 .   ? 97.640  -5.172  -12.417 1.00 27.58 ? 2324 HOH A O   1 
HETATM 7247 O  O   . HOH X 8 .   ? 99.439  -6.493  -8.299  1.00 11.73 ? 2325 HOH A O   1 
HETATM 7248 O  O   . HOH X 8 .   ? 101.748 -7.967  -4.339  1.00 30.91 ? 2326 HOH A O   1 
HETATM 7249 O  O   . HOH X 8 .   ? 101.336 -13.487 -8.231  1.00 18.46 ? 2327 HOH A O   1 
HETATM 7250 O  O   . HOH X 8 .   ? 96.774  -12.504 3.127   1.00 37.42 ? 2328 HOH A O   1 
HETATM 7251 O  O   . HOH X 8 .   ? 99.495  -15.178 1.144   1.00 16.34 ? 2329 HOH A O   1 
HETATM 7252 O  O   . HOH X 8 .   ? 102.139 -12.106 0.131   1.00 22.42 ? 2330 HOH A O   1 
HETATM 7253 O  O   . HOH X 8 .   ? 94.705  -5.470  -4.232  1.00 16.76 ? 2331 HOH A O   1 
HETATM 7254 O  O   . HOH X 8 .   ? 94.494  -17.133 -8.925  1.00 32.95 ? 2332 HOH A O   1 
HETATM 7255 O  O   . HOH X 8 .   ? 91.902  -7.525  1.960   1.00 13.49 ? 2333 HOH A O   1 
HETATM 7256 O  O   . HOH X 8 .   ? 94.219  -11.695 1.949   1.00 27.55 ? 2334 HOH A O   1 
HETATM 7257 O  O   . HOH X 8 .   ? 96.426  -8.870  3.356   1.00 23.06 ? 2335 HOH A O   1 
HETATM 7258 O  O   . HOH X 8 .   ? 85.616  -3.264  -5.458  1.00 13.87 ? 2336 HOH A O   1 
HETATM 7259 O  O   . HOH X 8 .   ? 80.312  -8.287  -9.478  1.00 13.21 ? 2337 HOH A O   1 
HETATM 7260 O  O   . HOH X 8 .   ? 82.579  0.658   0.380   1.00 10.02 ? 2338 HOH A O   1 
HETATM 7261 O  O   . HOH X 8 .   ? 81.413  1.108   7.175   1.00 13.45 ? 2339 HOH A O   1 
HETATM 7262 O  O   . HOH X 8 .   ? 93.084  -5.065  2.310   1.00 13.59 ? 2340 HOH A O   1 
HETATM 7263 O  O   . HOH X 8 .   ? 96.228  -1.876  6.928   1.00 32.58 ? 2341 HOH A O   1 
HETATM 7264 O  O   . HOH X 8 .   ? 94.366  2.908   8.691   1.00 13.24 ? 2342 HOH A O   1 
HETATM 7265 O  O   . HOH X 8 .   ? 85.003  4.761   -6.788  1.00 25.92 ? 2343 HOH A O   1 
HETATM 7266 O  O   . HOH X 8 .   ? 78.370  1.088   -5.269  1.00 11.60 ? 2344 HOH A O   1 
HETATM 7267 O  O   . HOH X 8 .   ? 78.915  6.339   -3.446  1.00 11.68 ? 2345 HOH A O   1 
HETATM 7268 O  O   . HOH X 8 .   ? 90.578  1.969   -7.074  1.00 26.32 ? 2346 HOH A O   1 
HETATM 7269 O  O   . HOH X 8 .   ? 92.272  5.425   -4.712  1.00 30.81 ? 2347 HOH A O   1 
HETATM 7270 O  O   . HOH X 8 .   ? 87.621  -4.425  -8.286  1.00 18.25 ? 2348 HOH A O   1 
HETATM 7271 O  O   . HOH X 8 .   ? 87.985  1.876   -10.480 1.00 30.44 ? 2349 HOH A O   1 
HETATM 7272 O  O   . HOH X 8 .   ? 94.943  -4.311  -6.597  1.00 24.38 ? 2350 HOH A O   1 
HETATM 7273 O  O   . HOH X 8 .   ? 92.420  -4.776  -8.857  1.00 26.71 ? 2351 HOH A O   1 
HETATM 7274 O  O   . HOH X 8 .   ? 95.577  -3.200  -2.452  1.00 25.29 ? 2352 HOH A O   1 
HETATM 7275 O  O   . HOH X 8 .   ? 97.327  0.635   -4.047  1.00 19.57 ? 2353 HOH A O   1 
HETATM 7276 O  O   . HOH X 8 .   ? 95.245  -3.989  1.906   1.00 31.76 ? 2354 HOH A O   1 
HETATM 7277 O  O   . HOH X 8 .   ? 94.113  9.473   -0.812  1.00 18.92 ? 2355 HOH A O   1 
HETATM 7278 O  O   . HOH X 8 .   ? 96.971  6.303   0.130   1.00 17.23 ? 2356 HOH A O   1 
HETATM 7279 O  O   . HOH X 8 .   ? 96.129  3.986   6.865   1.00 13.97 ? 2357 HOH A O   1 
HETATM 7280 O  O   . HOH X 8 .   ? 94.914  10.086  6.149   1.00 23.98 ? 2358 HOH A O   1 
HETATM 7281 O  O   . HOH X 8 .   ? 91.044  11.486  10.636  1.00 22.49 ? 2359 HOH A O   1 
HETATM 7282 O  O   . HOH X 8 .   ? 95.026  8.311   11.720  1.00 41.29 ? 2360 HOH A O   1 
HETATM 7283 O  O   . HOH X 8 .   ? 90.391  15.358  4.221   1.00 30.15 ? 2361 HOH A O   1 
HETATM 7284 O  O   . HOH X 8 .   ? 93.601  14.532  7.391   1.00 37.81 ? 2362 HOH A O   1 
HETATM 7285 O  O   . HOH X 8 .   ? 84.690  8.515   9.349   1.00 13.05 ? 2363 HOH A O   1 
HETATM 7286 O  O   . HOH X 8 .   ? 88.038  6.689   11.022  1.00 15.38 ? 2364 HOH A O   1 
HETATM 7287 O  O   . HOH X 8 .   ? 78.220  4.477   8.685   1.00 8.30  ? 2365 HOH A O   1 
HETATM 7288 O  O   . HOH X 8 .   ? 81.722  8.397   10.012  1.00 12.58 ? 2366 HOH A O   1 
HETATM 7289 O  O   . HOH X 8 .   ? 81.224  10.351  -2.291  1.00 18.09 ? 2367 HOH A O   1 
HETATM 7290 O  O   . HOH X 8 .   ? 79.943  14.734  2.896   1.00 18.42 ? 2368 HOH A O   1 
HETATM 7291 O  O   . HOH X 8 .   ? 85.416  12.105  0.323   1.00 23.13 ? 2369 HOH A O   1 
HETATM 7292 O  O   . HOH X 8 .   ? 79.140  9.020   -2.795  1.00 16.29 ? 2370 HOH A O   1 
HETATM 7293 O  O   . HOH X 8 .   ? 76.584  2.270   -8.291  1.00 14.18 ? 2371 HOH A O   1 
HETATM 7294 O  O   . HOH X 8 .   ? 77.590  0.841   4.485   1.00 9.97  ? 2372 HOH A O   1 
HETATM 7295 O  O   . HOH X 8 .   ? 75.197  9.867   -7.882  1.00 30.28 ? 2373 HOH A O   1 
HETATM 7296 O  O   . HOH X 8 .   ? 74.951  4.239   -9.081  1.00 14.03 ? 2374 HOH A O   1 
HETATM 7297 O  O   . HOH X 8 .   ? 83.920  7.174   -6.644  1.00 29.69 ? 2375 HOH A O   1 
HETATM 7298 O  O   . HOH X 8 .   ? 71.261  4.792   -10.643 1.00 25.23 ? 2376 HOH A O   1 
HETATM 7299 O  O   . HOH X 8 .   ? 75.772  0.695   -14.312 1.00 22.02 ? 2377 HOH A O   1 
HETATM 7300 O  O   . HOH X 8 .   ? 75.363  0.018   -6.959  1.00 13.52 ? 2378 HOH A O   1 
HETATM 7301 O  O   . HOH X 8 .   ? 67.708  -3.501  -10.590 1.00 17.06 ? 2379 HOH A O   1 
HETATM 7302 O  O   . HOH X 8 .   ? 78.652  -4.774  -11.943 1.00 17.56 ? 2380 HOH A O   1 
HETATM 7303 O  O   . HOH X 8 .   ? 74.912  -6.821  -10.912 1.00 13.37 ? 2381 HOH A O   1 
HETATM 7304 O  O   . HOH X 8 .   ? 75.611  -1.748  -14.244 1.00 23.44 ? 2382 HOH A O   1 
HETATM 7305 O  O   . HOH X 8 .   ? 79.120  -0.739  -7.075  1.00 10.39 ? 2383 HOH A O   1 
HETATM 7306 O  O   . HOH X 8 .   ? 78.880  -2.111  -13.590 1.00 23.07 ? 2384 HOH A O   1 
HETATM 7307 O  O   . HOH X 8 .   ? 80.866  -6.017  -11.135 1.00 14.52 ? 2385 HOH A O   1 
HETATM 7308 O  O   . HOH X 8 .   ? 75.104  -9.362  -5.256  1.00 11.77 ? 2386 HOH A O   1 
HETATM 7309 O  O   . HOH X 8 .   ? 73.265  -9.717  -7.596  1.00 18.09 ? 2387 HOH A O   1 
HETATM 7310 O  O   . HOH X 8 .   ? 85.874  -3.137  -9.956  1.00 19.11 ? 2388 HOH A O   1 
HETATM 7311 O  O   . HOH X 8 .   ? 83.789  0.922   -12.146 1.00 25.73 ? 2389 HOH A O   1 
HETATM 7312 O  O   . HOH X 8 .   ? 72.254  -2.948  0.922   1.00 12.04 ? 2390 HOH A O   1 
HETATM 7313 O  O   . HOH X 8 .   ? 72.543  -0.127  10.065  1.00 11.40 ? 2391 HOH A O   1 
HETATM 7314 O  O   . HOH X 8 .   ? 71.172  2.374   5.639   1.00 11.27 ? 2392 HOH A O   1 
HETATM 7315 O  O   . HOH X 8 .   ? 68.429  -1.420  -3.703  1.00 20.58 ? 2393 HOH A O   1 
HETATM 7316 O  O   . HOH X 8 .   ? 64.462  5.667   2.793   1.00 22.09 ? 2394 HOH A O   1 
HETATM 7317 O  O   . HOH X 8 .   ? 64.225  7.262   -2.078  1.00 13.82 ? 2395 HOH A O   1 
HETATM 7318 O  O   . HOH X 8 .   ? 68.992  10.269  2.632   1.00 12.24 ? 2396 HOH A O   1 
HETATM 7319 O  O   . HOH X 8 .   ? 77.287  10.278  -4.362  1.00 17.38 ? 2397 HOH A O   1 
HETATM 7320 O  O   . HOH X 8 .   ? 69.929  12.450  -4.330  1.00 21.24 ? 2398 HOH A O   1 
HETATM 7321 O  O   . HOH X 8 .   ? 65.965  6.714   8.448   1.00 16.86 ? 2399 HOH A O   1 
HETATM 7322 O  O   . HOH X 8 .   ? 64.600  4.381   5.321   1.00 21.51 ? 2400 HOH A O   1 
HETATM 7323 O  O   . HOH X 8 .   ? 71.058  1.726   8.566   1.00 10.34 ? 2401 HOH A O   1 
HETATM 7324 O  O   . HOH X 8 .   ? 64.489  4.361   9.885   1.00 18.68 ? 2402 HOH A O   1 
HETATM 7325 O  O   . HOH X 8 .   ? 64.711  1.435   16.554  1.00 13.89 ? 2403 HOH A O   1 
HETATM 7326 O  O   . HOH X 8 .   ? 68.432  -0.324  15.919  1.00 10.26 ? 2404 HOH A O   1 
HETATM 7327 O  O   . HOH X 8 .   ? 63.880  1.413   9.767   1.00 28.28 ? 2405 HOH A O   1 
HETATM 7328 O  O   . HOH X 8 .   ? 62.645  -1.739  10.605  1.00 26.60 ? 2406 HOH A O   1 
HETATM 7329 O  O   . HOH X 8 .   ? 74.351  0.728   12.282  1.00 10.63 ? 2407 HOH A O   1 
HETATM 7330 O  O   . HOH X 8 .   ? 80.864  -4.933  18.028  1.00 13.22 ? 2408 HOH A O   1 
HETATM 7331 O  O   . HOH X 8 .   ? 84.899  -0.910  19.536  1.00 34.37 ? 2409 HOH A O   1 
HETATM 7332 O  O   . HOH X 8 .   ? 95.870  -15.464 24.277  1.00 22.34 ? 2410 HOH A O   1 
HETATM 7333 O  O   . HOH X 8 .   ? 100.672 -10.156 15.279  1.00 30.09 ? 2411 HOH A O   1 
HETATM 7334 O  O   . HOH X 8 .   ? 95.822  -10.004 20.014  1.00 18.84 ? 2412 HOH A O   1 
HETATM 7335 O  O   . HOH X 8 .   ? 102.453 -14.669 16.526  1.00 34.11 ? 2413 HOH A O   1 
HETATM 7336 O  O   . HOH X 8 .   ? 102.856 -22.244 16.203  1.00 13.56 ? 2414 HOH A O   1 
HETATM 7337 O  O   . HOH X 8 .   ? 103.718 -18.566 16.536  1.00 17.54 ? 2415 HOH A O   1 
HETATM 7338 O  O   . HOH X 8 .   ? 97.221  -25.720 12.997  1.00 22.72 ? 2416 HOH A O   1 
HETATM 7339 O  O   . HOH X 8 .   ? 101.499 -26.595 10.759  1.00 21.86 ? 2417 HOH A O   1 
HETATM 7340 O  O   . HOH X 8 .   ? 97.520  -17.654 7.046   1.00 21.27 ? 2418 HOH A O   1 
HETATM 7341 O  O   . HOH X 8 .   ? 99.784  -15.600 6.426   1.00 41.66 ? 2419 HOH A O   1 
HETATM 7342 O  O   . HOH X 8 .   ? 96.858  -28.663 6.380   1.00 16.97 ? 2420 HOH A O   1 
HETATM 7343 O  O   . HOH X 8 .   ? 91.991  -24.885 6.036   1.00 31.47 ? 2421 HOH A O   1 
HETATM 7344 O  O   . HOH X 8 .   ? 95.034  -26.253 20.831  1.00 22.58 ? 2422 HOH A O   1 
HETATM 7345 O  O   . HOH X 8 .   ? 95.456  -20.121 22.862  1.00 17.72 ? 2423 HOH A O   1 
HETATM 7346 O  O   . HOH X 8 .   ? 91.336  -22.557 22.031  1.00 22.04 ? 2424 HOH A O   1 
HETATM 7347 O  O   . HOH X 8 .   ? 92.324  -19.553 22.398  1.00 19.31 ? 2425 HOH A O   1 
HETATM 7348 O  O   . HOH X 8 .   ? 60.301  1.537   16.167  1.00 25.51 ? 2426 HOH A O   1 
HETATM 7349 O  O   . HOH X 8 .   ? 63.384  3.823   16.907  1.00 31.50 ? 2427 HOH A O   1 
HETATM 7350 O  O   . HOH X 8 .   ? 59.078  -1.379  17.127  1.00 22.75 ? 2428 HOH A O   1 
HETATM 7351 O  O   . HOH X 8 .   ? 60.867  -3.601  20.146  1.00 18.52 ? 2429 HOH A O   1 
HETATM 7352 O  O   . HOH X 8 .   ? 63.058  -7.977  13.726  1.00 16.25 ? 2430 HOH A O   1 
HETATM 7353 O  O   . HOH X 8 .   ? 61.977  -9.708  16.125  1.00 33.52 ? 2431 HOH A O   1 
HETATM 7354 O  O   . HOH X 8 .   ? 64.509  -9.517  11.738  1.00 14.56 ? 2432 HOH A O   1 
HETATM 7355 O  O   . HOH X 8 .   ? 66.622  -15.409 7.585   1.00 24.91 ? 2433 HOH A O   1 
HETATM 7356 O  O   . HOH X 8 .   ? 62.996  -11.241 8.272   1.00 21.13 ? 2434 HOH A O   1 
HETATM 7357 O  O   . HOH X 8 .   ? 64.531  -3.741  5.330   1.00 17.14 ? 2435 HOH A O   1 
HETATM 7358 O  O   . HOH X 8 .   ? 67.621  -7.773  -4.812  1.00 11.68 ? 2436 HOH A O   1 
HETATM 7359 O  O   . HOH X 8 .   ? 64.991  -7.078  -8.315  1.00 18.92 ? 2437 HOH A O   1 
HETATM 7360 O  O   . HOH X 8 .   ? 66.268  -8.225  -11.837 1.00 47.78 ? 2438 HOH A O   1 
HETATM 7361 O  O   . HOH X 8 .   ? 69.053  -0.194  -6.036  1.00 17.61 ? 2439 HOH A O   1 
HETATM 7362 O  O   . HOH X 8 .   ? 67.158  -10.478 -11.821 1.00 34.85 ? 2440 HOH A O   1 
HETATM 7363 O  O   . HOH X 8 .   ? 69.252  -13.666 -9.244  1.00 20.73 ? 2441 HOH A O   1 
HETATM 7364 O  O   . HOH X 8 .   ? 74.463  -12.052 -8.848  1.00 18.03 ? 2442 HOH A O   1 
HETATM 7365 O  O   . HOH X 8 .   ? 81.290  -16.543 8.042   1.00 15.73 ? 2443 HOH A O   1 
HETATM 7366 O  O   . HOH X 8 .   ? 77.550  -14.416 12.421  1.00 18.96 ? 2444 HOH A O   1 
HETATM 7367 O  O   . HOH X 8 .   ? 78.780  -17.191 9.064   1.00 15.67 ? 2445 HOH A O   1 
HETATM 7368 O  O   . HOH X 8 .   ? 77.704  -20.039 13.556  1.00 15.49 ? 2446 HOH A O   1 
HETATM 7369 O  O   . HOH X 8 .   ? 78.464  -16.615 11.727  1.00 15.12 ? 2447 HOH A O   1 
HETATM 7370 O  O   . HOH X 8 .   ? 75.869  -21.430 7.401   1.00 12.22 ? 2448 HOH A O   1 
HETATM 7371 O  O   . HOH X 8 .   ? 73.262  -22.369 2.305   1.00 20.19 ? 2449 HOH A O   1 
HETATM 7372 O  O   . HOH X 8 .   ? 71.446  -25.350 12.467  1.00 28.08 ? 2450 HOH A O   1 
HETATM 7373 O  O   . HOH X 8 .   ? 80.605  -23.788 6.763   1.00 44.93 ? 2451 HOH A O   1 
HETATM 7374 O  O   . HOH X 8 .   ? 73.287  -19.672 0.983   1.00 16.11 ? 2452 HOH A O   1 
HETATM 7375 O  O   . HOH X 8 .   ? 72.268  -17.024 -1.235  1.00 18.01 ? 2453 HOH A O   1 
HETATM 7376 O  O   . HOH X 8 .   ? 80.272  -13.834 -5.834  1.00 10.02 ? 2454 HOH A O   1 
HETATM 7377 O  O   . HOH X 8 .   ? 80.370  -12.165 -8.879  1.00 10.38 ? 2455 HOH A O   1 
HETATM 7378 O  O   . HOH X 8 .   ? 86.767  -10.553 -11.477 1.00 15.58 ? 2456 HOH A O   1 
HETATM 7379 O  O   . HOH X 8 .   ? 80.889  -6.864  -15.364 1.00 28.21 ? 2457 HOH A O   1 
HETATM 7380 O  O   . HOH X 8 .   ? 80.944  -10.927 -17.707 1.00 27.57 ? 2458 HOH A O   1 
HETATM 7381 O  O   . HOH X 8 .   ? 82.455  -16.016 -14.316 1.00 22.32 ? 2459 HOH A O   1 
HETATM 7382 O  O   . HOH X 8 .   ? 79.026  -8.340  -14.519 1.00 17.75 ? 2460 HOH A O   1 
HETATM 7383 O  O   . HOH X 8 .   ? 75.464  -10.189 -13.993 1.00 16.50 ? 2461 HOH A O   1 
HETATM 7384 O  O   . HOH X 8 .   ? 77.209  -6.050  -13.870 1.00 21.89 ? 2462 HOH A O   1 
HETATM 7385 O  O   . HOH X 8 .   ? 77.871  -19.119 -10.479 1.00 21.33 ? 2463 HOH A O   1 
HETATM 7386 O  O   . HOH X 8 .   ? 74.333  -19.686 -7.145  1.00 25.82 ? 2464 HOH A O   1 
HETATM 7387 O  O   . HOH X 8 .   ? 82.428  -21.404 -5.077  1.00 20.41 ? 2465 HOH A O   1 
HETATM 7388 O  O   . HOH X 8 .   ? 83.572  -23.208 8.656   1.00 22.44 ? 2466 HOH A O   1 
HETATM 7389 O  O   . HOH X 8 .   ? 86.055  -21.990 7.100   1.00 29.91 ? 2467 HOH A O   1 
HETATM 7390 O  O   . HOH X 8 .   ? 73.350  4.719   41.110  1.00 17.73 ? 2468 HOH A O   1 
HETATM 7391 O  O   . HOH X 8 .   ? 68.252  1.659   46.332  1.00 30.61 ? 2469 HOH A O   1 
HETATM 7392 O  O   . HOH X 8 .   ? 72.551  4.388   46.433  1.00 29.74 ? 2470 HOH A O   1 
HETATM 7393 O  O   . HOH X 8 .   ? 66.291  4.168   39.900  1.00 13.37 ? 2471 HOH A O   1 
HETATM 7394 O  O   . HOH X 8 .   ? 67.709  -3.461  49.162  1.00 31.43 ? 2472 HOH A O   1 
HETATM 7395 O  O   . HOH X 8 .   ? 63.067  -6.025  46.117  1.00 33.65 ? 2473 HOH A O   1 
HETATM 7396 O  O   . HOH X 8 .   ? 100.649 -9.626  43.232  1.00 19.53 ? 2474 HOH A O   1 
HETATM 7397 O  O   . HOH X 8 .   ? 94.559  -11.806 40.356  1.00 26.03 ? 2475 HOH A O   1 
HETATM 7398 O  O   . HOH X 8 .   ? 97.233  -14.241 9.826   1.00 27.14 ? 2476 HOH A O   1 
HETATM 7399 O  O   . HOH X 8 .   ? 81.982  16.784  2.964   1.00 21.93 ? 2477 HOH A O   1 
HETATM 7400 O  O   . HOH X 8 .   ? 78.380  12.784  -4.756  1.00 28.70 ? 2478 HOH A O   1 
HETATM 7401 O  O   . HOH X 8 .   ? 98.350  -30.267 2.741   1.00 25.60 ? 2479 HOH A O   1 
HETATM 7402 O  O   . HOH X 8 .   ? 82.769  -18.680 -17.254 1.00 29.70 ? 2480 HOH A O   1 
HETATM 7403 O  O   . HOH X 8 .   ? 80.082  -19.508 -17.852 1.00 29.76 ? 2481 HOH A O   1 
HETATM 7404 O  O   . HOH X 8 .   ? 76.366  -20.939 -16.596 1.00 25.51 ? 2482 HOH A O   1 
HETATM 7405 O  O   . HOH X 8 .   ? 76.761  1.898   11.630  1.00 8.90  ? 2483 HOH A O   1 
HETATM 7406 O  O   . HOH Y 8 .   ? 125.785 -29.725 32.608  1.00 22.88 ? 2001 HOH B O   1 
HETATM 7407 O  O   . HOH Y 8 .   ? 129.270 -24.399 29.352  1.00 30.44 ? 2002 HOH B O   1 
HETATM 7408 O  O   . HOH Y 8 .   ? 128.056 -17.785 33.911  1.00 39.00 ? 2003 HOH B O   1 
HETATM 7409 O  O   . HOH Y 8 .   ? 129.231 -20.667 33.623  1.00 31.34 ? 2004 HOH B O   1 
HETATM 7410 O  O   . HOH Y 8 .   ? 113.235 -17.135 40.553  1.00 23.71 ? 2005 HOH B O   1 
HETATM 7411 O  O   . HOH Y 8 .   ? 122.519 -23.945 25.397  1.00 31.28 ? 2006 HOH B O   1 
HETATM 7412 O  O   . HOH Y 8 .   ? 129.364 -25.783 25.569  1.00 40.99 ? 2007 HOH B O   1 
HETATM 7413 O  O   . HOH Y 8 .   ? 122.255 -15.095 38.202  1.00 42.88 ? 2008 HOH B O   1 
HETATM 7414 O  O   . HOH Y 8 .   ? 123.349 -28.144 25.099  1.00 22.79 ? 2009 HOH B O   1 
HETATM 7415 O  O   . HOH Y 8 .   ? 126.078 -31.761 26.300  1.00 32.83 ? 2010 HOH B O   1 
HETATM 7416 O  O   . HOH Y 8 .   ? 125.059 -31.789 30.683  1.00 20.55 ? 2011 HOH B O   1 
HETATM 7417 O  O   . HOH Y 8 .   ? 111.729 -15.051 39.897  1.00 28.75 ? 2012 HOH B O   1 
HETATM 7418 O  O   . HOH Y 8 .   ? 119.127 -28.937 33.200  1.00 9.01  ? 2013 HOH B O   1 
HETATM 7419 O  O   . HOH Y 8 .   ? 117.204 -21.645 41.426  1.00 19.79 ? 2014 HOH B O   1 
HETATM 7420 O  O   . HOH Y 8 .   ? 112.164 -18.520 38.406  1.00 17.22 ? 2015 HOH B O   1 
HETATM 7421 O  O   . HOH Y 8 .   ? 110.191 -21.258 38.918  1.00 10.16 ? 2016 HOH B O   1 
HETATM 7422 O  O   . HOH Y 8 .   ? 109.415 -42.156 18.032  1.00 36.08 ? 2017 HOH B O   1 
HETATM 7423 O  O   . HOH Y 8 .   ? 116.444 -14.707 40.883  1.00 36.13 ? 2018 HOH B O   1 
HETATM 7424 O  O   . HOH Y 8 .   ? 120.278 -15.443 40.330  1.00 32.73 ? 2019 HOH B O   1 
HETATM 7425 O  O   . HOH Y 8 .   ? 115.112 -15.055 38.818  1.00 37.42 ? 2020 HOH B O   1 
HETATM 7426 O  O   . HOH Y 8 .   ? 115.391 -13.917 31.741  1.00 34.73 ? 2021 HOH B O   1 
HETATM 7427 O  O   . HOH Y 8 .   ? 109.861 -20.308 18.920  1.00 36.38 ? 2022 HOH B O   1 
HETATM 7428 O  O   . HOH Y 8 .   ? 110.779 -15.026 37.335  1.00 21.61 ? 2023 HOH B O   1 
HETATM 7429 O  O   . HOH Y 8 .   ? 114.449 -9.448  34.435  1.00 35.16 ? 2024 HOH B O   1 
HETATM 7430 O  O   . HOH Y 8 .   ? 112.060 -8.668  35.190  1.00 33.15 ? 2025 HOH B O   1 
HETATM 7431 O  O   . HOH Y 8 .   ? 115.180 -10.644 32.102  1.00 33.61 ? 2026 HOH B O   1 
HETATM 7432 O  O   . HOH Y 8 .   ? 121.412 -13.481 36.379  1.00 28.97 ? 2027 HOH B O   1 
HETATM 7433 O  O   . HOH Y 8 .   ? 110.462 -10.530 29.014  1.00 23.19 ? 2028 HOH B O   1 
HETATM 7434 O  O   . HOH Y 8 .   ? 104.518 -7.513  38.289  1.00 41.61 ? 2029 HOH B O   1 
HETATM 7435 O  O   . HOH Y 8 .   ? 106.769 -5.842  40.525  1.00 20.46 ? 2030 HOH B O   1 
HETATM 7436 O  O   . HOH Y 8 .   ? 101.617 -14.786 34.993  1.00 24.08 ? 2031 HOH B O   1 
HETATM 7437 O  O   . HOH Y 8 .   ? 96.349  -28.115 24.709  1.00 30.13 ? 2032 HOH B O   1 
HETATM 7438 O  O   . HOH Y 8 .   ? 112.714 -45.796 37.700  1.00 22.55 ? 2033 HOH B O   1 
HETATM 7439 O  O   . HOH Y 8 .   ? 103.581 -45.462 29.946  1.00 31.55 ? 2034 HOH B O   1 
HETATM 7440 O  O   . HOH Y 8 .   ? 103.301 -45.193 33.499  1.00 34.32 ? 2035 HOH B O   1 
HETATM 7441 O  O   . HOH Y 8 .   ? 100.993 -41.295 25.860  1.00 24.65 ? 2036 HOH B O   1 
HETATM 7442 O  O   . HOH Y 8 .   ? 97.505  -39.092 27.947  1.00 43.76 ? 2037 HOH B O   1 
HETATM 7443 O  O   . HOH Y 8 .   ? 98.989  -42.791 24.014  1.00 36.15 ? 2038 HOH B O   1 
HETATM 7444 O  O   . HOH Y 8 .   ? 103.258 -42.689 19.175  1.00 28.13 ? 2039 HOH B O   1 
HETATM 7445 O  O   . HOH Y 8 .   ? 98.786  -36.365 17.760  1.00 25.01 ? 2040 HOH B O   1 
HETATM 7446 O  O   . HOH Y 8 .   ? 112.475 -46.779 40.213  1.00 32.69 ? 2041 HOH B O   1 
HETATM 7447 O  O   . HOH Y 8 .   ? 113.900 -41.948 49.367  1.00 24.57 ? 2042 HOH B O   1 
HETATM 7448 O  O   . HOH Y 8 .   ? 107.639 -42.818 20.009  1.00 31.26 ? 2043 HOH B O   1 
HETATM 7449 O  O   . HOH Y 8 .   ? 109.155 -38.925 16.704  1.00 22.72 ? 2044 HOH B O   1 
HETATM 7450 O  O   . HOH Y 8 .   ? 112.212 -43.769 23.858  1.00 15.69 ? 2045 HOH B O   1 
HETATM 7451 O  O   . HOH Y 8 .   ? 110.490 -36.010 12.730  1.00 27.79 ? 2046 HOH B O   1 
HETATM 7452 O  O   . HOH Y 8 .   ? 104.126 -31.814 67.344  1.00 24.06 ? 2047 HOH B O   1 
HETATM 7453 O  O   . HOH Y 8 .   ? 116.736 -30.223 18.685  1.00 22.63 ? 2048 HOH B O   1 
HETATM 7454 O  O   . HOH Y 8 .   ? 114.123 -26.546 14.701  1.00 28.13 ? 2049 HOH B O   1 
HETATM 7455 O  O   . HOH Y 8 .   ? 97.660  -42.060 34.569  1.00 34.32 ? 2050 HOH B O   1 
HETATM 7456 O  O   . HOH Y 8 .   ? 111.377 -23.015 18.021  1.00 30.61 ? 2051 HOH B O   1 
HETATM 7457 O  O   . HOH Y 8 .   ? 119.264 -27.851 21.886  1.00 27.05 ? 2052 HOH B O   1 
HETATM 7458 O  O   . HOH Y 8 .   ? 118.252 -24.322 23.878  1.00 19.33 ? 2053 HOH B O   1 
HETATM 7459 O  O   . HOH Y 8 .   ? 113.846 -19.538 26.299  1.00 18.59 ? 2054 HOH B O   1 
HETATM 7460 O  O   . HOH Y 8 .   ? 116.343 -19.115 24.852  1.00 26.63 ? 2055 HOH B O   1 
HETATM 7461 O  O   . HOH Y 8 .   ? 103.227 -8.672  23.547  1.00 29.66 ? 2056 HOH B O   1 
HETATM 7462 O  O   . HOH Y 8 .   ? 105.826 -6.115  25.399  1.00 36.83 ? 2057 HOH B O   1 
HETATM 7463 O  O   . HOH Y 8 .   ? 103.292 -4.034  28.483  1.00 37.02 ? 2058 HOH B O   1 
HETATM 7464 O  O   . HOH Y 8 .   ? 95.696  -29.814 16.214  1.00 28.14 ? 2059 HOH B O   1 
HETATM 7465 O  O   . HOH Y 8 .   ? 123.003 -11.095 36.653  1.00 34.41 ? 2060 HOH B O   1 
HETATM 7466 O  O   . HOH Y 8 .   ? 124.757 -14.100 37.356  1.00 35.98 ? 2061 HOH B O   1 
HETATM 7467 O  O   . HOH Y 8 .   ? 92.917  -27.564 26.902  1.00 33.19 ? 2062 HOH B O   1 
HETATM 7468 O  O   . HOH Y 8 .   ? 94.599  -16.118 40.749  1.00 35.64 ? 2063 HOH B O   1 
HETATM 7469 O  O   . HOH Y 8 .   ? 110.655 -4.210  53.093  1.00 24.56 ? 2064 HOH B O   1 
HETATM 7470 O  O   . HOH Y 8 .   ? 133.454 -11.093 53.286  1.00 33.87 ? 2065 HOH B O   1 
HETATM 7471 O  O   . HOH Y 8 .   ? 106.920 -4.198  55.480  1.00 23.11 ? 2066 HOH B O   1 
HETATM 7472 O  O   . HOH Y 8 .   ? 114.332 -13.407 22.994  1.00 26.07 ? 2067 HOH B O   1 
HETATM 7473 O  O   . HOH Y 8 .   ? 112.087 -15.418 23.695  1.00 27.26 ? 2068 HOH B O   1 
HETATM 7474 O  O   . HOH Y 8 .   ? 111.259 -18.849 23.945  1.00 33.88 ? 2069 HOH B O   1 
HETATM 7475 O  O   . HOH Y 8 .   ? 118.039 -9.738  47.911  1.00 38.76 ? 2070 HOH B O   1 
HETATM 7476 O  O   . HOH Y 8 .   ? 122.219 -12.321 46.143  1.00 25.51 ? 2071 HOH B O   1 
HETATM 7477 O  O   . HOH Y 8 .   ? 113.839 -26.029 35.189  1.00 8.79  ? 2072 HOH B O   1 
HETATM 7478 O  O   . HOH Y 8 .   ? 127.548 -16.424 38.119  1.00 34.24 ? 2073 HOH B O   1 
HETATM 7479 O  O   . HOH Y 8 .   ? 102.903 -37.726 37.577  1.00 10.35 ? 2074 HOH B O   1 
HETATM 7480 O  O   . HOH Y 8 .   ? 132.591 -17.245 52.247  1.00 25.20 ? 2075 HOH B O   1 
HETATM 7481 O  O   . HOH Y 8 .   ? 104.992 -39.523 38.052  1.00 10.65 ? 2076 HOH B O   1 
HETATM 7482 O  O   . HOH Y 8 .   ? 107.220 -38.124 39.146  1.00 10.23 ? 2077 HOH B O   1 
HETATM 7483 O  O   . HOH Y 8 .   ? 110.144 -45.749 36.701  1.00 25.74 ? 2078 HOH B O   1 
HETATM 7484 O  O   . HOH Y 8 .   ? 111.833 -42.268 35.656  1.00 14.12 ? 2079 HOH B O   1 
HETATM 7485 O  O   . HOH Y 8 .   ? 106.683 -46.263 37.349  1.00 21.94 ? 2080 HOH B O   1 
HETATM 7486 O  O   . HOH Y 8 .   ? 104.939 -42.069 38.935  1.00 15.48 ? 2081 HOH B O   1 
HETATM 7487 O  O   . HOH Y 8 .   ? 129.550 -30.552 51.874  1.00 28.02 ? 2082 HOH B O   1 
HETATM 7488 O  O   . HOH Y 8 .   ? 103.062 -43.020 31.417  1.00 17.13 ? 2083 HOH B O   1 
HETATM 7489 O  O   . HOH Y 8 .   ? 128.176 -33.852 52.082  1.00 37.28 ? 2084 HOH B O   1 
HETATM 7490 O  O   . HOH Y 8 .   ? 107.585 -46.876 28.871  1.00 21.80 ? 2085 HOH B O   1 
HETATM 7491 O  O   . HOH Y 8 .   ? 111.851 -47.598 24.988  1.00 23.64 ? 2086 HOH B O   1 
HETATM 7492 O  O   . HOH Y 8 .   ? 112.036 -44.133 33.630  1.00 13.23 ? 2087 HOH B O   1 
HETATM 7493 O  O   . HOH Y 8 .   ? 115.229 -46.147 28.042  1.00 18.41 ? 2088 HOH B O   1 
HETATM 7494 O  O   . HOH Y 8 .   ? 113.777 -47.988 36.174  1.00 26.14 ? 2089 HOH B O   1 
HETATM 7495 O  O   . HOH Y 8 .   ? 111.484 -46.956 35.079  1.00 32.65 ? 2090 HOH B O   1 
HETATM 7496 O  O   . HOH Y 8 .   ? 116.032 -48.753 30.445  1.00 23.48 ? 2091 HOH B O   1 
HETATM 7497 O  O   . HOH Y 8 .   ? 113.632 -43.363 37.425  1.00 12.94 ? 2092 HOH B O   1 
HETATM 7498 O  O   . HOH Y 8 .   ? 118.247 -47.925 34.210  1.00 23.40 ? 2093 HOH B O   1 
HETATM 7499 O  O   . HOH Y 8 .   ? 120.344 -45.284 39.022  1.00 32.78 ? 2094 HOH B O   1 
HETATM 7500 O  O   . HOH Y 8 .   ? 114.011 -44.981 41.152  1.00 27.72 ? 2095 HOH B O   1 
HETATM 7501 O  O   . HOH Y 8 .   ? 116.632 -46.768 42.533  1.00 37.38 ? 2096 HOH B O   1 
HETATM 7502 O  O   . HOH Y 8 .   ? 114.225 -42.173 39.663  1.00 12.06 ? 2097 HOH B O   1 
HETATM 7503 O  O   . HOH Y 8 .   ? 116.147 -43.437 45.661  1.00 16.57 ? 2098 HOH B O   1 
HETATM 7504 O  O   . HOH Y 8 .   ? 118.399 -39.286 43.378  1.00 12.18 ? 2099 HOH B O   1 
HETATM 7505 O  O   . HOH Y 8 .   ? 116.120 -39.241 46.527  1.00 12.17 ? 2100 HOH B O   1 
HETATM 7506 O  O   . HOH Y 8 .   ? 95.724  -6.629  60.256  1.00 35.96 ? 2101 HOH B O   1 
HETATM 7507 O  O   . HOH Y 8 .   ? 114.372 -41.389 46.855  1.00 12.23 ? 2102 HOH B O   1 
HETATM 7508 O  O   . HOH Y 8 .   ? 107.256 -40.370 46.161  1.00 11.31 ? 2103 HOH B O   1 
HETATM 7509 O  O   . HOH Y 8 .   ? 102.186 -40.376 43.549  1.00 13.85 ? 2104 HOH B O   1 
HETATM 7510 O  O   . HOH Y 8 .   ? 103.159 -43.762 41.617  1.00 27.77 ? 2105 HOH B O   1 
HETATM 7511 O  O   . HOH Y 8 .   ? 109.189 -0.634  69.928  1.00 44.42 ? 2106 HOH B O   1 
HETATM 7512 O  O   . HOH Y 8 .   ? 97.251  -1.950  64.978  1.00 34.99 ? 2107 HOH B O   1 
HETATM 7513 O  O   . HOH Y 8 .   ? 102.026 -37.954 42.183  1.00 12.85 ? 2108 HOH B O   1 
HETATM 7514 O  O   . HOH Y 8 .   ? 101.367 -4.396  58.422  1.00 36.36 ? 2109 HOH B O   1 
HETATM 7515 O  O   . HOH Y 8 .   ? 106.534 -4.096  58.154  1.00 28.90 ? 2110 HOH B O   1 
HETATM 7516 O  O   . HOH Y 8 .   ? 108.717 -5.288  59.694  1.00 27.06 ? 2111 HOH B O   1 
HETATM 7517 O  O   . HOH Y 8 .   ? 100.348 -40.021 50.445  1.00 19.66 ? 2112 HOH B O   1 
HETATM 7518 O  O   . HOH Y 8 .   ? 105.246 -42.534 51.595  1.00 30.19 ? 2113 HOH B O   1 
HETATM 7519 O  O   . HOH Y 8 .   ? 99.706  -41.585 42.999  1.00 19.84 ? 2114 HOH B O   1 
HETATM 7520 O  O   . HOH Y 8 .   ? 107.496 -41.819 50.441  1.00 15.13 ? 2115 HOH B O   1 
HETATM 7521 O  O   . HOH Y 8 .   ? 109.820 -3.804  55.560  1.00 24.33 ? 2116 HOH B O   1 
HETATM 7522 O  O   . HOH Y 8 .   ? 115.986 -5.486  49.042  1.00 33.16 ? 2117 HOH B O   1 
HETATM 7523 O  O   . HOH Y 8 .   ? 105.955 -34.986 58.522  1.00 17.94 ? 2118 HOH B O   1 
HETATM 7524 O  O   . HOH Y 8 .   ? 106.934 -38.264 59.301  1.00 27.45 ? 2119 HOH B O   1 
HETATM 7525 O  O   . HOH Y 8 .   ? 98.791  -30.876 57.180  1.00 23.33 ? 2120 HOH B O   1 
HETATM 7526 O  O   . HOH Y 8 .   ? 107.287 -35.773 63.176  1.00 31.46 ? 2121 HOH B O   1 
HETATM 7527 O  O   . HOH Y 8 .   ? 104.488 -33.064 62.648  1.00 17.73 ? 2122 HOH B O   1 
HETATM 7528 O  O   . HOH Y 8 .   ? 104.298 -33.382 65.358  1.00 25.75 ? 2123 HOH B O   1 
HETATM 7529 O  O   . HOH Y 8 .   ? 118.779 0.640   62.324  1.00 38.34 ? 2124 HOH B O   1 
HETATM 7530 O  O   . HOH Y 8 .   ? 119.580 0.355   51.323  1.00 40.33 ? 2125 HOH B O   1 
HETATM 7531 O  O   . HOH Y 8 .   ? 96.132  -35.425 57.165  1.00 37.08 ? 2126 HOH B O   1 
HETATM 7532 O  O   . HOH Y 8 .   ? 95.699  -38.648 51.030  1.00 30.08 ? 2127 HOH B O   1 
HETATM 7533 O  O   . HOH Y 8 .   ? 96.254  -39.723 45.778  1.00 25.73 ? 2128 HOH B O   1 
HETATM 7534 O  O   . HOH Y 8 .   ? 92.555  -26.591 44.987  1.00 37.22 ? 2129 HOH B O   1 
HETATM 7535 O  O   . HOH Y 8 .   ? 92.279  -37.052 41.576  1.00 36.17 ? 2130 HOH B O   1 
HETATM 7536 O  O   . HOH Y 8 .   ? 118.741 -20.624 79.337  1.00 48.00 ? 2131 HOH B O   1 
HETATM 7537 O  O   . HOH Y 8 .   ? 121.114 -19.505 80.407  1.00 42.93 ? 2132 HOH B O   1 
HETATM 7538 O  O   . HOH Y 8 .   ? 96.353  -37.399 37.829  1.00 26.05 ? 2133 HOH B O   1 
HETATM 7539 O  O   . HOH Y 8 .   ? 99.476  -36.250 38.229  1.00 12.80 ? 2134 HOH B O   1 
HETATM 7540 O  O   . HOH Y 8 .   ? 91.715  -28.366 38.771  1.00 24.30 ? 2135 HOH B O   1 
HETATM 7541 O  O   . HOH Y 8 .   ? 89.175  -30.131 37.081  1.00 35.30 ? 2136 HOH B O   1 
HETATM 7542 O  O   . HOH Y 8 .   ? 118.534 -9.066  72.045  1.00 28.65 ? 2137 HOH B O   1 
HETATM 7543 O  O   . HOH Y 8 .   ? 120.256 -11.144 78.710  1.00 32.57 ? 2138 HOH B O   1 
HETATM 7544 O  O   . HOH Y 8 .   ? 100.912 -35.132 40.265  1.00 21.51 ? 2139 HOH B O   1 
HETATM 7545 O  O   . HOH Y 8 .   ? 96.838  -41.328 38.299  1.00 21.06 ? 2140 HOH B O   1 
HETATM 7546 O  O   . HOH Y 8 .   ? 100.220 -41.259 33.520  1.00 17.39 ? 2141 HOH B O   1 
HETATM 7547 O  O   . HOH Y 8 .   ? 102.932 -43.627 38.751  1.00 25.90 ? 2142 HOH B O   1 
HETATM 7548 O  O   . HOH Y 8 .   ? 98.607  -42.553 36.832  1.00 32.35 ? 2143 HOH B O   1 
HETATM 7549 O  O   . HOH Y 8 .   ? 97.691  -38.458 31.613  1.00 13.83 ? 2144 HOH B O   1 
HETATM 7550 O  O   . HOH Y 8 .   ? 126.674 -27.786 69.258  1.00 34.32 ? 2145 HOH B O   1 
HETATM 7551 O  O   . HOH Y 8 .   ? 131.002 -27.969 58.421  1.00 26.02 ? 2146 HOH B O   1 
HETATM 7552 O  O   . HOH Y 8 .   ? 134.119 -24.618 57.863  1.00 26.09 ? 2147 HOH B O   1 
HETATM 7553 O  O   . HOH Y 8 .   ? 103.810 -7.842  25.851  1.00 24.66 ? 2148 HOH B O   1 
HETATM 7554 O  O   . HOH Y 8 .   ? 100.698 -8.452  29.076  1.00 22.72 ? 2149 HOH B O   1 
HETATM 7555 O  O   . HOH Y 8 .   ? 101.566 -8.370  31.901  1.00 26.33 ? 2150 HOH B O   1 
HETATM 7556 O  O   . HOH Y 8 .   ? 102.352 -11.294 22.963  1.00 25.87 ? 2151 HOH B O   1 
HETATM 7557 O  O   . HOH Y 8 .   ? 101.747 -6.516  27.182  1.00 29.72 ? 2152 HOH B O   1 
HETATM 7558 O  O   . HOH Y 8 .   ? 84.971  -4.588  54.260  1.00 37.82 ? 2153 HOH B O   1 
HETATM 7559 O  O   . HOH Y 8 .   ? 105.387 -14.674 22.848  1.00 22.65 ? 2154 HOH B O   1 
HETATM 7560 O  O   . HOH Y 8 .   ? 83.149  -9.558  58.171  1.00 35.15 ? 2155 HOH B O   1 
HETATM 7561 O  O   . HOH Y 8 .   ? 96.798  -18.311 24.705  1.00 25.46 ? 2156 HOH B O   1 
HETATM 7562 O  O   . HOH Y 8 .   ? 99.356  -15.702 31.569  1.00 29.27 ? 2157 HOH B O   1 
HETATM 7563 O  O   . HOH Y 8 .   ? 84.212  -15.545 53.687  1.00 38.56 ? 2158 HOH B O   1 
HETATM 7564 O  O   . HOH Y 8 .   ? 102.699 -16.926 18.254  1.00 20.59 ? 2159 HOH B O   1 
HETATM 7565 O  O   . HOH Y 8 .   ? 107.248 -22.372 19.466  1.00 31.78 ? 2160 HOH B O   1 
HETATM 7566 O  O   . HOH Y 8 .   ? 95.932  -23.014 27.243  1.00 19.18 ? 2161 HOH B O   1 
HETATM 7567 O  O   . HOH Y 8 .   ? 98.011  -28.438 15.198  1.00 28.15 ? 2162 HOH B O   1 
HETATM 7568 O  O   . HOH Y 8 .   ? 106.403 -33.470 71.340  1.00 31.82 ? 2163 HOH B O   1 
HETATM 7569 O  O   . HOH Y 8 .   ? 97.063  -32.491 15.837  1.00 29.45 ? 2164 HOH B O   1 
HETATM 7570 O  O   . HOH Y 8 .   ? 94.526  -35.341 15.568  1.00 44.88 ? 2165 HOH B O   1 
HETATM 7571 O  O   . HOH Y 8 .   ? 95.969  -37.673 15.839  1.00 41.67 ? 2166 HOH B O   1 
HETATM 7572 O  O   . HOH Y 8 .   ? 96.946  -34.985 14.757  1.00 43.29 ? 2167 HOH B O   1 
HETATM 7573 O  O   . HOH Y 8 .   ? 94.062  -31.650 24.129  1.00 34.42 ? 2168 HOH B O   1 
HETATM 7574 O  O   . HOH Y 8 .   ? 112.233 -34.035 75.054  1.00 41.10 ? 2169 HOH B O   1 
HETATM 7575 O  O   . HOH Y 8 .   ? 94.734  -29.174 25.915  1.00 18.82 ? 2170 HOH B O   1 
HETATM 7576 O  O   . HOH Y 8 .   ? 92.474  -28.785 29.619  1.00 22.42 ? 2171 HOH B O   1 
HETATM 7577 O  O   . HOH Y 8 .   ? 92.565  -28.038 34.789  1.00 19.02 ? 2172 HOH B O   1 
HETATM 7578 O  O   . HOH Y 8 .   ? 95.376  -22.030 38.500  1.00 22.10 ? 2173 HOH B O   1 
HETATM 7579 O  O   . HOH Y 8 .   ? 94.767  -21.798 41.224  1.00 30.51 ? 2174 HOH B O   1 
HETATM 7580 O  O   . HOH Y 8 .   ? 92.679  -24.805 41.664  1.00 38.61 ? 2175 HOH B O   1 
HETATM 7581 O  O   . HOH Y 8 .   ? 96.800  -20.221 34.663  1.00 28.85 ? 2176 HOH B O   1 
HETATM 7582 O  O   . HOH Y 8 .   ? 93.587  -24.730 63.285  1.00 37.74 ? 2177 HOH B O   1 
HETATM 7583 O  O   . HOH Y 8 .   ? 105.281 -30.298 71.184  1.00 25.23 ? 2178 HOH B O   1 
HETATM 7584 O  O   . HOH Y 8 .   ? 96.440  -19.443 37.625  1.00 16.75 ? 2179 HOH B O   1 
HETATM 7585 O  O   . HOH Y 8 .   ? 96.918  -17.595 39.888  1.00 33.70 ? 2180 HOH B O   1 
HETATM 7586 O  O   . HOH Y 8 .   ? 100.604 -16.502 33.289  1.00 24.28 ? 2181 HOH B O   1 
HETATM 7587 O  O   . HOH Y 8 .   ? 102.073 -11.932 42.773  1.00 18.29 ? 2182 HOH B O   1 
HETATM 7588 O  O   . HOH Y 8 .   ? 113.555 -9.866  75.770  1.00 30.37 ? 2183 HOH B O   1 
HETATM 7589 O  O   . HOH Y 8 .   ? 112.260 -7.933  74.129  1.00 37.79 ? 2184 HOH B O   1 
HETATM 7590 O  O   . HOH Y 8 .   ? 107.623 -10.882 44.766  1.00 11.93 ? 2185 HOH B O   1 
HETATM 7591 O  O   . HOH Y 8 .   ? 100.197 -9.840  50.478  1.00 32.52 ? 2186 HOH B O   1 
HETATM 7592 O  O   . HOH Y 8 .   ? 98.822  -8.155  49.371  1.00 17.87 ? 2187 HOH B O   1 
HETATM 7593 O  O   . HOH Y 8 .   ? 101.802 -5.449  50.866  1.00 31.65 ? 2188 HOH B O   1 
HETATM 7594 O  O   . HOH Y 8 .   ? 102.410 -2.887  46.934  1.00 34.43 ? 2189 HOH B O   1 
HETATM 7595 O  O   . HOH Y 8 .   ? 105.466 -3.200  40.012  1.00 30.08 ? 2190 HOH B O   1 
HETATM 7596 O  O   . HOH Y 8 .   ? 104.585 -0.232  46.511  1.00 38.22 ? 2191 HOH B O   1 
HETATM 7597 O  O   . HOH Y 8 .   ? 111.640 -4.668  46.591  1.00 29.35 ? 2192 HOH B O   1 
HETATM 7598 O  O   . HOH Y 8 .   ? 108.742 -3.467  50.990  1.00 22.81 ? 2193 HOH B O   1 
HETATM 7599 O  O   . HOH Y 8 .   ? 107.337 4.216   47.620  1.00 15.26 ? 2194 HOH B O   1 
HETATM 7600 O  O   . HOH Y 8 .   ? 106.213 -6.154  53.595  1.00 18.36 ? 2195 HOH B O   1 
HETATM 7601 O  O   . HOH Y 8 .   ? 112.361 -4.801  49.723  1.00 25.37 ? 2196 HOH B O   1 
HETATM 7602 O  O   . HOH Y 8 .   ? 103.894 -15.894 48.131  1.00 11.92 ? 2197 HOH B O   1 
HETATM 7603 O  O   . HOH Y 8 .   ? 101.603 -8.301  52.624  1.00 37.86 ? 2198 HOH B O   1 
HETATM 7604 O  O   . HOH Y 8 .   ? 112.845 -11.846 54.687  1.00 12.34 ? 2199 HOH B O   1 
HETATM 7605 O  O   . HOH Y 8 .   ? 115.242 -10.858 46.634  1.00 34.29 ? 2200 HOH B O   1 
HETATM 7606 O  O   . HOH Y 8 .   ? 111.385 -18.734 46.362  1.00 31.17 ? 2201 HOH B O   1 
HETATM 7607 O  O   . HOH Y 8 .   ? 109.333 -12.851 44.197  1.00 14.38 ? 2202 HOH B O   1 
HETATM 7608 O  O   . HOH Y 8 .   ? 117.615 -16.235 44.778  1.00 22.50 ? 2203 HOH B O   1 
HETATM 7609 O  O   . HOH Y 8 .   ? 122.433 -16.540 48.666  1.00 13.00 ? 2204 HOH B O   1 
HETATM 7610 O  O   . HOH Y 8 .   ? 121.696 -12.708 48.709  1.00 17.19 ? 2205 HOH B O   1 
HETATM 7611 O  O   . HOH Y 8 .   ? 117.568 -22.116 49.186  1.00 12.31 ? 2206 HOH B O   1 
HETATM 7612 O  O   . HOH Y 8 .   ? 123.569 -20.796 51.399  1.00 11.90 ? 2207 HOH B O   1 
HETATM 7613 O  O   . HOH Y 8 .   ? 113.811 -17.968 45.537  1.00 33.68 ? 2208 HOH B O   1 
HETATM 7614 O  O   . HOH Y 8 .   ? 122.138 -23.086 51.405  1.00 10.96 ? 2209 HOH B O   1 
HETATM 7615 O  O   . HOH Y 8 .   ? 123.374 -19.925 44.317  1.00 22.95 ? 2210 HOH B O   1 
HETATM 7616 O  O   . HOH Y 8 .   ? 131.276 -28.387 42.662  1.00 15.21 ? 2211 HOH B O   1 
HETATM 7617 O  O   . HOH Y 8 .   ? 131.253 -26.141 39.665  1.00 27.09 ? 2212 HOH B O   1 
HETATM 7618 O  O   . HOH Y 8 .   ? 132.919 -21.292 44.045  1.00 22.62 ? 2213 HOH B O   1 
HETATM 7619 O  O   . HOH Y 8 .   ? 133.125 -29.232 44.411  1.00 23.12 ? 2214 HOH B O   1 
HETATM 7620 O  O   . HOH Y 8 .   ? 135.564 -22.803 38.385  1.00 37.18 ? 2215 HOH B O   1 
HETATM 7621 O  O   . HOH Y 8 .   ? 127.745 -16.215 41.890  1.00 32.70 ? 2216 HOH B O   1 
HETATM 7622 O  O   . HOH Y 8 .   ? 129.778 -15.560 40.164  1.00 37.46 ? 2217 HOH B O   1 
HETATM 7623 O  O   . HOH Y 8 .   ? 126.785 -16.763 45.391  1.00 23.80 ? 2218 HOH B O   1 
HETATM 7624 O  O   . HOH Y 8 .   ? 133.477 -15.229 48.151  1.00 24.67 ? 2219 HOH B O   1 
HETATM 7625 O  O   . HOH Y 8 .   ? 130.689 -12.187 47.336  1.00 25.26 ? 2220 HOH B O   1 
HETATM 7626 O  O   . HOH Y 8 .   ? 130.320 -18.106 51.907  1.00 14.74 ? 2221 HOH B O   1 
HETATM 7627 O  O   . HOH Y 8 .   ? 132.569 -14.469 51.358  1.00 38.07 ? 2222 HOH B O   1 
HETATM 7628 O  O   . HOH Y 8 .   ? 125.646 -11.914 53.534  1.00 16.35 ? 2223 HOH B O   1 
HETATM 7629 O  O   . HOH Y 8 .   ? 131.439 -15.858 54.937  1.00 15.95 ? 2224 HOH B O   1 
HETATM 7630 O  O   . HOH Y 8 .   ? 127.037 -18.974 57.542  1.00 12.75 ? 2225 HOH B O   1 
HETATM 7631 O  O   . HOH Y 8 .   ? 122.400 -16.369 46.082  1.00 16.90 ? 2226 HOH B O   1 
HETATM 7632 O  O   . HOH Y 8 .   ? 128.733 -27.512 52.598  1.00 13.86 ? 2227 HOH B O   1 
HETATM 7633 O  O   . HOH Y 8 .   ? 122.584 -25.575 52.926  1.00 12.65 ? 2228 HOH B O   1 
HETATM 7634 O  O   . HOH Y 8 .   ? 125.320 -24.430 56.743  1.00 14.41 ? 2229 HOH B O   1 
HETATM 7635 O  O   . HOH Y 8 .   ? 128.677 -30.285 49.179  1.00 17.00 ? 2230 HOH B O   1 
HETATM 7636 O  O   . HOH Y 8 .   ? 133.103 -32.051 49.352  1.00 32.06 ? 2231 HOH B O   1 
HETATM 7637 O  O   . HOH Y 8 .   ? 128.583 -33.179 48.648  1.00 21.54 ? 2232 HOH B O   1 
HETATM 7638 O  O   . HOH Y 8 .   ? 123.553 -35.978 45.001  1.00 12.11 ? 2233 HOH B O   1 
HETATM 7639 O  O   . HOH Y 8 .   ? 120.362 -33.239 46.840  1.00 9.14  ? 2234 HOH B O   1 
HETATM 7640 O  O   . HOH Y 8 .   ? 128.686 -37.801 35.999  1.00 29.48 ? 2235 HOH B O   1 
HETATM 7641 O  O   . HOH Y 8 .   ? 130.125 -30.875 38.014  1.00 21.68 ? 2236 HOH B O   1 
HETATM 7642 O  O   . HOH Y 8 .   ? 131.584 -29.019 39.773  1.00 27.83 ? 2237 HOH B O   1 
HETATM 7643 O  O   . HOH Y 8 .   ? 131.917 -37.161 40.664  1.00 21.50 ? 2238 HOH B O   1 
HETATM 7644 O  O   . HOH Y 8 .   ? 126.519 -39.194 39.739  1.00 14.82 ? 2239 HOH B O   1 
HETATM 7645 O  O   . HOH Y 8 .   ? 127.679 -43.708 40.992  1.00 22.12 ? 2240 HOH B O   1 
HETATM 7646 O  O   . HOH Y 8 .   ? 125.163 -36.375 27.756  1.00 24.28 ? 2241 HOH B O   1 
HETATM 7647 O  O   . HOH Y 8 .   ? 124.549 -39.721 26.680  1.00 18.42 ? 2242 HOH B O   1 
HETATM 7648 O  O   . HOH Y 8 .   ? 121.707 -35.423 27.139  1.00 14.86 ? 2243 HOH B O   1 
HETATM 7649 O  O   . HOH Y 8 .   ? 105.382 -27.868 51.730  1.00 15.39 ? 2244 HOH B O   1 
HETATM 7650 O  O   . HOH Y 8 .   ? 90.593  -19.702 49.570  1.00 30.22 ? 2245 HOH B O   1 
HETATM 7651 O  O   . HOH Y 8 .   ? 94.727  -17.632 50.105  1.00 13.84 ? 2246 HOH B O   1 
HETATM 7652 O  O   . HOH Y 8 .   ? 95.235  -14.956 51.776  1.00 11.45 ? 2247 HOH B O   1 
HETATM 7653 O  O   . HOH Y 8 .   ? 94.085  -9.395  58.889  1.00 21.19 ? 2248 HOH B O   1 
HETATM 7654 O  O   . HOH Y 8 .   ? 93.825  -15.343 62.497  1.00 25.08 ? 2249 HOH B O   1 
HETATM 7655 O  O   . HOH Y 8 .   ? 99.694  -8.373  62.010  1.00 23.28 ? 2250 HOH B O   1 
HETATM 7656 O  O   . HOH Y 8 .   ? 101.614 -8.804  59.734  1.00 24.46 ? 2251 HOH B O   1 
HETATM 7657 O  O   . HOH Y 8 .   ? 95.358  -7.873  57.436  1.00 25.76 ? 2252 HOH B O   1 
HETATM 7658 O  O   . HOH Y 8 .   ? 98.438  -8.114  54.108  1.00 32.67 ? 2253 HOH B O   1 
HETATM 7659 O  O   . HOH Y 8 .   ? 93.931  -15.053 65.810  1.00 26.91 ? 2254 HOH B O   1 
HETATM 7660 O  O   . HOH Y 8 .   ? 101.893 -14.527 73.057  1.00 28.65 ? 2255 HOH B O   1 
HETATM 7661 O  O   . HOH Y 8 .   ? 94.952  -16.710 68.161  1.00 29.49 ? 2256 HOH B O   1 
HETATM 7662 O  O   . HOH Y 8 .   ? 99.160  -16.089 73.230  1.00 25.55 ? 2257 HOH B O   1 
HETATM 7663 O  O   . HOH Y 8 .   ? 109.717 -8.862  73.239  1.00 29.29 ? 2258 HOH B O   1 
HETATM 7664 O  O   . HOH Y 8 .   ? 110.720 -7.068  76.859  1.00 31.17 ? 2259 HOH B O   1 
HETATM 7665 O  O   . HOH Y 8 .   ? 109.137 0.913   73.118  1.00 26.79 ? 2260 HOH B O   1 
HETATM 7666 O  O   . HOH Y 8 .   ? 105.866 0.861   69.176  1.00 33.45 ? 2261 HOH B O   1 
HETATM 7667 O  O   . HOH Y 8 .   ? 99.356  -1.043  66.584  1.00 27.58 ? 2262 HOH B O   1 
HETATM 7668 O  O   . HOH Y 8 .   ? 98.295  -6.278  60.961  1.00 36.54 ? 2263 HOH B O   1 
HETATM 7669 O  O   . HOH Y 8 .   ? 98.185  -2.414  62.460  1.00 33.50 ? 2264 HOH B O   1 
HETATM 7670 O  O   . HOH Y 8 .   ? 108.506 -4.604  65.515  1.00 31.24 ? 2265 HOH B O   1 
HETATM 7671 O  O   . HOH Y 8 .   ? 107.110 -9.184  60.722  1.00 19.96 ? 2266 HOH B O   1 
HETATM 7672 O  O   . HOH Y 8 .   ? 104.324 -8.228  60.360  1.00 21.69 ? 2267 HOH B O   1 
HETATM 7673 O  O   . HOH Y 8 .   ? 104.022 -5.141  58.966  1.00 33.81 ? 2268 HOH B O   1 
HETATM 7674 O  O   . HOH Y 8 .   ? 108.683 -3.393  62.070  1.00 35.57 ? 2269 HOH B O   1 
HETATM 7675 O  O   . HOH Y 8 .   ? 104.479 -2.333  60.368  1.00 33.13 ? 2270 HOH B O   1 
HETATM 7676 O  O   . HOH Y 8 .   ? 114.948 -12.382 67.615  1.00 22.52 ? 2271 HOH B O   1 
HETATM 7677 O  O   . HOH Y 8 .   ? 118.146 -15.107 61.460  1.00 14.63 ? 2272 HOH B O   1 
HETATM 7678 O  O   . HOH Y 8 .   ? 117.843 -17.399 55.130  1.00 14.35 ? 2273 HOH B O   1 
HETATM 7679 O  O   . HOH Y 8 .   ? 108.959 -7.727  59.781  1.00 18.94 ? 2274 HOH B O   1 
HETATM 7680 O  O   . HOH Y 8 .   ? 110.778 -5.188  57.828  1.00 20.22 ? 2275 HOH B O   1 
HETATM 7681 O  O   . HOH Y 8 .   ? 103.725 -6.298  54.765  1.00 21.48 ? 2276 HOH B O   1 
HETATM 7682 O  O   . HOH Y 8 .   ? 114.765 -5.236  51.434  1.00 28.19 ? 2277 HOH B O   1 
HETATM 7683 O  O   . HOH Y 8 .   ? 123.136 -10.025 67.014  1.00 34.27 ? 2278 HOH B O   1 
HETATM 7684 O  O   . HOH Y 8 .   ? 121.124 -17.660 67.434  1.00 18.05 ? 2279 HOH B O   1 
HETATM 7685 O  O   . HOH Y 8 .   ? 125.566 -15.740 64.358  1.00 22.06 ? 2280 HOH B O   1 
HETATM 7686 O  O   . HOH Y 8 .   ? 122.967 -7.250  67.867  1.00 29.18 ? 2281 HOH B O   1 
HETATM 7687 O  O   . HOH Y 8 .   ? 122.257 -5.295  65.790  1.00 40.74 ? 2282 HOH B O   1 
HETATM 7688 O  O   . HOH Y 8 .   ? 119.932 -3.606  64.109  1.00 28.74 ? 2283 HOH B O   1 
HETATM 7689 O  O   . HOH Y 8 .   ? 112.727 -2.832  69.899  1.00 28.33 ? 2284 HOH B O   1 
HETATM 7690 O  O   . HOH Y 8 .   ? 115.221 -3.306  70.217  1.00 28.78 ? 2285 HOH B O   1 
HETATM 7691 O  O   . HOH Y 8 .   ? 111.919 -1.886  64.269  1.00 34.57 ? 2286 HOH B O   1 
HETATM 7692 O  O   . HOH Y 8 .   ? 118.207 -1.350  63.802  1.00 40.73 ? 2287 HOH B O   1 
HETATM 7693 O  O   . HOH Y 8 .   ? 111.433 -1.171  59.358  1.00 27.22 ? 2288 HOH B O   1 
HETATM 7694 O  O   . HOH Y 8 .   ? 118.530 0.387   58.173  1.00 28.34 ? 2289 HOH B O   1 
HETATM 7695 O  O   . HOH Y 8 .   ? 122.862 -1.537  58.673  1.00 33.76 ? 2290 HOH B O   1 
HETATM 7696 O  O   . HOH Y 8 .   ? 123.266 -4.106  62.149  1.00 38.75 ? 2291 HOH B O   1 
HETATM 7697 O  O   . HOH Y 8 .   ? 123.955 -0.815  60.903  1.00 35.82 ? 2292 HOH B O   1 
HETATM 7698 O  O   . HOH Y 8 .   ? 115.624 -3.233  52.979  1.00 28.91 ? 2293 HOH B O   1 
HETATM 7699 O  O   . HOH Y 8 .   ? 121.821 -1.807  52.245  1.00 26.57 ? 2294 HOH B O   1 
HETATM 7700 O  O   . HOH Y 8 .   ? 119.101 -7.806  48.972  1.00 36.22 ? 2295 HOH B O   1 
HETATM 7701 O  O   . HOH Y 8 .   ? 122.924 -6.178  47.993  1.00 26.61 ? 2296 HOH B O   1 
HETATM 7702 O  O   . HOH Y 8 .   ? 123.334 -12.472 50.814  1.00 16.89 ? 2297 HOH B O   1 
HETATM 7703 O  O   . HOH Y 8 .   ? 132.160 -10.900 49.124  1.00 27.92 ? 2298 HOH B O   1 
HETATM 7704 O  O   . HOH Y 8 .   ? 131.812 -7.451  51.840  1.00 31.22 ? 2299 HOH B O   1 
HETATM 7705 O  O   . HOH Y 8 .   ? 127.184 -6.295  59.529  1.00 29.87 ? 2300 HOH B O   1 
HETATM 7706 O  O   . HOH Y 8 .   ? 120.159 -10.389 49.152  1.00 21.85 ? 2301 HOH B O   1 
HETATM 7707 O  O   . HOH Y 8 .   ? 121.775 -19.583 53.257  1.00 12.02 ? 2302 HOH B O   1 
HETATM 7708 O  O   . HOH Y 8 .   ? 124.001 -15.331 50.719  1.00 14.94 ? 2303 HOH B O   1 
HETATM 7709 O  O   . HOH Y 8 .   ? 128.309 -12.775 62.027  1.00 18.72 ? 2304 HOH B O   1 
HETATM 7710 O  O   . HOH Y 8 .   ? 131.858 -13.764 56.470  1.00 21.22 ? 2305 HOH B O   1 
HETATM 7711 O  O   . HOH Y 8 .   ? 127.530 -8.803  58.538  1.00 27.71 ? 2306 HOH B O   1 
HETATM 7712 O  O   . HOH Y 8 .   ? 127.673 -15.289 63.135  1.00 25.94 ? 2307 HOH B O   1 
HETATM 7713 O  O   . HOH Y 8 .   ? 123.352 -18.237 70.332  1.00 18.82 ? 2308 HOH B O   1 
HETATM 7714 O  O   . HOH Y 8 .   ? 119.434 -20.471 58.303  1.00 12.52 ? 2309 HOH B O   1 
HETATM 7715 O  O   . HOH Y 8 .   ? 129.877 -15.856 64.577  1.00 26.78 ? 2310 HOH B O   1 
HETATM 7716 O  O   . HOH Y 8 .   ? 126.035 -19.042 70.478  1.00 19.16 ? 2311 HOH B O   1 
HETATM 7717 O  O   . HOH Y 8 .   ? 129.540 -19.303 73.055  1.00 34.35 ? 2312 HOH B O   1 
HETATM 7718 O  O   . HOH Y 8 .   ? 127.366 -11.697 71.347  1.00 33.38 ? 2313 HOH B O   1 
HETATM 7719 O  O   . HOH Y 8 .   ? 122.905 -18.377 76.728  1.00 26.00 ? 2314 HOH B O   1 
HETATM 7720 O  O   . HOH Y 8 .   ? 121.408 -20.312 69.606  1.00 18.03 ? 2315 HOH B O   1 
HETATM 7721 O  O   . HOH Y 8 .   ? 115.833 -22.141 75.286  1.00 28.91 ? 2316 HOH B O   1 
HETATM 7722 O  O   . HOH Y 8 .   ? 117.003 -19.267 77.496  1.00 43.76 ? 2317 HOH B O   1 
HETATM 7723 O  O   . HOH Y 8 .   ? 120.773 -19.528 77.313  1.00 31.67 ? 2318 HOH B O   1 
HETATM 7724 O  O   . HOH Y 8 .   ? 119.477 -17.093 69.430  1.00 18.60 ? 2319 HOH B O   1 
HETATM 7725 O  O   . HOH Y 8 .   ? 112.342 -24.038 70.475  1.00 22.54 ? 2320 HOH B O   1 
HETATM 7726 O  O   . HOH Y 8 .   ? 113.024 -24.786 72.947  1.00 23.14 ? 2321 HOH B O   1 
HETATM 7727 O  O   . HOH Y 8 .   ? 116.423 -10.414 72.304  1.00 28.02 ? 2322 HOH B O   1 
HETATM 7728 O  O   . HOH Y 8 .   ? 120.019 -10.346 73.830  1.00 34.90 ? 2323 HOH B O   1 
HETATM 7729 O  O   . HOH Y 8 .   ? 119.467 -12.865 76.754  1.00 32.14 ? 2324 HOH B O   1 
HETATM 7730 O  O   . HOH Y 8 .   ? 118.181 -25.747 63.237  1.00 16.59 ? 2325 HOH B O   1 
HETATM 7731 O  O   . HOH Y 8 .   ? 119.297 -26.690 53.833  1.00 12.56 ? 2326 HOH B O   1 
HETATM 7732 O  O   . HOH Y 8 .   ? 122.916 -26.243 57.675  1.00 14.54 ? 2327 HOH B O   1 
HETATM 7733 O  O   . HOH Y 8 .   ? 127.732 -26.237 66.794  1.00 19.27 ? 2328 HOH B O   1 
HETATM 7734 O  O   . HOH Y 8 .   ? 122.180 -28.235 67.765  1.00 21.47 ? 2329 HOH B O   1 
HETATM 7735 O  O   . HOH Y 8 .   ? 128.744 -30.130 60.328  1.00 24.02 ? 2330 HOH B O   1 
HETATM 7736 O  O   . HOH Y 8 .   ? 130.607 -26.377 65.992  1.00 24.45 ? 2331 HOH B O   1 
HETATM 7737 O  O   . HOH Y 8 .   ? 131.671 -25.240 58.590  1.00 17.93 ? 2332 HOH B O   1 
HETATM 7738 O  O   . HOH Y 8 .   ? 134.278 -22.610 64.814  1.00 22.96 ? 2333 HOH B O   1 
HETATM 7739 O  O   . HOH Y 8 .   ? 134.087 -21.989 57.234  1.00 23.24 ? 2334 HOH B O   1 
HETATM 7740 O  O   . HOH Y 8 .   ? 128.490 -30.238 54.559  1.00 22.15 ? 2335 HOH B O   1 
HETATM 7741 O  O   . HOH Y 8 .   ? 127.041 -31.465 58.419  1.00 21.75 ? 2336 HOH B O   1 
HETATM 7742 O  O   . HOH Y 8 .   ? 121.764 -27.109 55.037  1.00 12.33 ? 2337 HOH B O   1 
HETATM 7743 O  O   . HOH Y 8 .   ? 126.586 -32.658 53.829  1.00 25.07 ? 2338 HOH B O   1 
HETATM 7744 O  O   . HOH Y 8 .   ? 119.572 -31.637 48.804  1.00 9.96  ? 2339 HOH B O   1 
HETATM 7745 O  O   . HOH Y 8 .   ? 122.213 -34.527 48.459  1.00 13.53 ? 2340 HOH B O   1 
HETATM 7746 O  O   . HOH Y 8 .   ? 121.715 -33.898 58.047  1.00 20.63 ? 2341 HOH B O   1 
HETATM 7747 O  O   . HOH Y 8 .   ? 120.498 -36.155 54.719  1.00 24.25 ? 2342 HOH B O   1 
HETATM 7748 O  O   . HOH Y 8 .   ? 119.146 -25.098 51.336  1.00 11.78 ? 2343 HOH B O   1 
HETATM 7749 O  O   . HOH Y 8 .   ? 110.565 -21.818 46.258  1.00 16.08 ? 2344 HOH B O   1 
HETATM 7750 O  O   . HOH Y 8 .   ? 112.455 -17.159 43.572  1.00 31.36 ? 2345 HOH B O   1 
HETATM 7751 O  O   . HOH Y 8 .   ? 99.898  -4.441  47.361  1.00 23.66 ? 2346 HOH B O   1 
HETATM 7752 O  O   . HOH Y 8 .   ? 97.599  -5.914  50.333  1.00 30.99 ? 2347 HOH B O   1 
HETATM 7753 O  O   . HOH Y 8 .   ? 90.592  -4.119  47.614  1.00 22.38 ? 2348 HOH B O   1 
HETATM 7754 O  O   . HOH Y 8 .   ? 86.314  -3.140  50.347  1.00 38.93 ? 2349 HOH B O   1 
HETATM 7755 O  O   . HOH Y 8 .   ? 85.052  -7.160  54.980  1.00 31.56 ? 2350 HOH B O   1 
HETATM 7756 O  O   . HOH Y 8 .   ? 84.686  -7.313  57.899  1.00 26.69 ? 2351 HOH B O   1 
HETATM 7757 O  O   . HOH Y 8 .   ? 88.296  -11.206 62.898  1.00 22.40 ? 2352 HOH B O   1 
HETATM 7758 O  O   . HOH Y 8 .   ? 86.561  -11.497 53.915  1.00 29.16 ? 2353 HOH B O   1 
HETATM 7759 O  O   . HOH Y 8 .   ? 83.867  -13.708 56.969  1.00 50.68 ? 2354 HOH B O   1 
HETATM 7760 O  O   . HOH Y 8 .   ? 86.350  -17.198 53.010  1.00 29.11 ? 2355 HOH B O   1 
HETATM 7761 O  O   . HOH Y 8 .   ? 90.870  -13.878 43.009  1.00 26.06 ? 2356 HOH B O   1 
HETATM 7762 O  O   . HOH Y 8 .   ? 90.266  -17.642 44.279  1.00 25.65 ? 2357 HOH B O   1 
HETATM 7763 O  O   . HOH Y 8 .   ? 92.586  -16.084 43.447  1.00 21.10 ? 2358 HOH B O   1 
HETATM 7764 O  O   . HOH Y 8 .   ? 124.632 -35.102 47.413  1.00 21.99 ? 2359 HOH B O   1 
HETATM 7765 O  O   . HOH Y 8 .   ? 124.227 -38.289 49.307  1.00 24.25 ? 2360 HOH B O   1 
HETATM 7766 O  O   . HOH Y 8 .   ? 118.666 -40.632 46.684  1.00 18.33 ? 2361 HOH B O   1 
HETATM 7767 O  O   . HOH Y 8 .   ? 121.575 -40.742 49.472  1.00 27.29 ? 2362 HOH B O   1 
HETATM 7768 O  O   . HOH Y 8 .   ? 114.602 -38.683 53.648  1.00 25.06 ? 2363 HOH B O   1 
HETATM 7769 O  O   . HOH Y 8 .   ? 118.664 -38.267 53.913  1.00 33.04 ? 2364 HOH B O   1 
HETATM 7770 O  O   . HOH Y 8 .   ? 111.637 -40.576 54.228  1.00 33.68 ? 2365 HOH B O   1 
HETATM 7771 O  O   . HOH Y 8 .   ? 112.790 -37.142 55.491  1.00 18.66 ? 2366 HOH B O   1 
HETATM 7772 O  O   . HOH Y 8 .   ? 107.791 -35.907 60.381  1.00 23.93 ? 2367 HOH B O   1 
HETATM 7773 O  O   . HOH Y 8 .   ? 118.939 -34.488 60.769  1.00 33.11 ? 2368 HOH B O   1 
HETATM 7774 O  O   . HOH Y 8 .   ? 107.409 -34.330 65.596  1.00 22.77 ? 2369 HOH B O   1 
HETATM 7775 O  O   . HOH Y 8 .   ? 114.738 -36.442 65.496  1.00 33.03 ? 2370 HOH B O   1 
HETATM 7776 O  O   . HOH Y 8 .   ? 107.592 -35.690 67.812  1.00 30.82 ? 2371 HOH B O   1 
HETATM 7777 O  O   . HOH Y 8 .   ? 108.302 -35.536 70.372  1.00 32.52 ? 2372 HOH B O   1 
HETATM 7778 O  O   . HOH Y 8 .   ? 109.155 -33.916 72.043  1.00 26.41 ? 2373 HOH B O   1 
HETATM 7779 O  O   . HOH Y 8 .   ? 116.610 -30.412 70.799  1.00 16.38 ? 2374 HOH B O   1 
HETATM 7780 O  O   . HOH Y 8 .   ? 123.853 -28.536 72.262  1.00 27.97 ? 2375 HOH B O   1 
HETATM 7781 O  O   . HOH Y 8 .   ? 123.126 -26.521 69.740  1.00 23.33 ? 2376 HOH B O   1 
HETATM 7782 O  O   . HOH Y 8 .   ? 111.643 -30.948 76.098  1.00 42.79 ? 2377 HOH B O   1 
HETATM 7783 O  O   . HOH Y 8 .   ? 109.247 -29.818 76.209  1.00 38.04 ? 2378 HOH B O   1 
HETATM 7784 O  O   . HOH Y 8 .   ? 101.463 -22.834 58.195  1.00 16.91 ? 2379 HOH B O   1 
HETATM 7785 O  O   . HOH Y 8 .   ? 101.642 -25.632 57.721  1.00 22.55 ? 2380 HOH B O   1 
HETATM 7786 O  O   . HOH Y 8 .   ? 103.960 -26.656 53.919  1.00 24.08 ? 2381 HOH B O   1 
HETATM 7787 O  O   . HOH Y 8 .   ? 98.914  -28.145 54.098  1.00 21.06 ? 2382 HOH B O   1 
HETATM 7788 O  O   . HOH Y 8 .   ? 101.362 -26.277 55.181  1.00 23.69 ? 2383 HOH B O   1 
HETATM 7789 O  O   . HOH Y 8 .   ? 99.082  -29.230 60.531  1.00 16.70 ? 2384 HOH B O   1 
HETATM 7790 O  O   . HOH Y 8 .   ? 95.577  -25.793 61.696  1.00 37.13 ? 2385 HOH B O   1 
HETATM 7791 O  O   . HOH Y 8 .   ? 97.702  -29.587 68.353  1.00 36.66 ? 2386 HOH B O   1 
HETATM 7792 O  O   . HOH Y 8 .   ? 102.429 -29.556 66.937  1.00 21.95 ? 2387 HOH B O   1 
HETATM 7793 O  O   . HOH Y 8 .   ? 105.381 -29.591 68.562  1.00 26.39 ? 2388 HOH B O   1 
HETATM 7794 O  O   . HOH Y 8 .   ? 106.604 -20.114 71.198  1.00 21.05 ? 2389 HOH B O   1 
HETATM 7795 O  O   . HOH Y 8 .   ? 105.896 -28.781 73.332  1.00 28.29 ? 2390 HOH B O   1 
HETATM 7796 O  O   . HOH Y 8 .   ? 108.613 -19.142 73.531  1.00 25.09 ? 2391 HOH B O   1 
HETATM 7797 O  O   . HOH Y 8 .   ? 115.597 -11.276 74.698  1.00 34.74 ? 2392 HOH B O   1 
HETATM 7798 O  O   . HOH Y 8 .   ? 110.943 -24.389 74.655  1.00 29.25 ? 2393 HOH B O   1 
HETATM 7799 O  O   . HOH Y 8 .   ? 109.527 -26.044 76.389  1.00 30.97 ? 2394 HOH B O   1 
HETATM 7800 O  O   . HOH Y 8 .   ? 110.216 -26.073 78.724  1.00 32.15 ? 2395 HOH B O   1 
HETATM 7801 O  O   . HOH Y 8 .   ? 103.619 -22.329 77.389  1.00 34.06 ? 2396 HOH B O   1 
HETATM 7802 O  O   . HOH Y 8 .   ? 102.145 -19.001 75.646  1.00 38.84 ? 2397 HOH B O   1 
HETATM 7803 O  O   . HOH Y 8 .   ? 103.171 -25.201 77.547  1.00 44.83 ? 2398 HOH B O   1 
HETATM 7804 O  O   . HOH Y 8 .   ? 98.640  -20.944 71.804  1.00 23.33 ? 2399 HOH B O   1 
HETATM 7805 O  O   . HOH Y 8 .   ? 97.826  -27.492 70.138  1.00 34.77 ? 2400 HOH B O   1 
HETATM 7806 O  O   . HOH Y 8 .   ? 94.248  -23.256 59.078  1.00 26.04 ? 2401 HOH B O   1 
HETATM 7807 O  O   . HOH Y 8 .   ? 96.873  -29.587 55.410  1.00 30.73 ? 2402 HOH B O   1 
HETATM 7808 O  O   . HOH Y 8 .   ? 118.457 -30.683 22.780  1.00 13.51 ? 2403 HOH B O   1 
HETATM 7809 O  O   . HOH Y 8 .   ? 121.031 -33.307 21.744  1.00 25.25 ? 2404 HOH B O   1 
HETATM 7810 O  O   . HOH Y 8 .   ? 120.582 -37.155 25.073  1.00 12.89 ? 2405 HOH B O   1 
HETATM 7811 O  O   . HOH Y 8 .   ? 111.781 -40.560 17.608  1.00 34.29 ? 2406 HOH B O   1 
HETATM 7812 O  O   . HOH Y 8 .   ? 123.612 -48.025 41.049  1.00 24.13 ? 2407 HOH B O   1 
HETATM 7813 O  O   . HOH Y 8 .   ? 132.653 -11.104 55.811  1.00 27.02 ? 2408 HOH B O   1 
HETATM 7814 O  O   . HOH Y 8 .   ? 119.421 -22.273 51.313  1.00 12.08 ? 2409 HOH B O   1 
HETATM 7815 O  O   . HOH Y 8 .   ? 111.942 -7.887  79.584  1.00 41.91 ? 2410 HOH B 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   SER 1   3   3   SER SER A . n 
A 1 2   LEU 2   4   4   LEU LEU A . n 
A 1 3   ASN 3   5   5   ASN ASN A . n 
A 1 4   THR 4   6   6   THR THR A . n 
A 1 5   ASP 5   7   7   ASP ASP A . n 
A 1 6   ASP 6   8   8   ASP ASP A . n 
A 1 7   ILE 7   9   9   ILE ILE A . n 
A 1 8   GLN 8   10  10  GLN GLN A . n 
A 1 9   GLY 9   11  11  GLY GLY A . n 
A 1 10  ASP 10  12  12  ASP ASP A . n 
A 1 11  ILE 11  13  13  ILE ILE A . n 
A 1 12  LEU 12  14  14  LEU LEU A . n 
A 1 13  VAL 13  15  15  VAL VAL A . n 
A 1 14  GLY 14  16  16  GLY GLY A . n 
A 1 15  MET 15  17  17  MET MET A . n 
A 1 16  HIS 16  18  18  HIS HIS A . n 
A 1 17  LYS 17  19  19  LYS LYS A . n 
A 1 18  GLN 18  20  20  GLN GLN A . n 
A 1 19  LYS 19  21  21  LYS LYS A . n 
A 1 20  GLN 20  22  22  GLN GLN A . n 
A 1 21  LEU 21  23  23  LEU LEU A . n 
A 1 22  PHE 22  24  24  PHE PHE A . n 
A 1 23  TYR 23  25  25  TYR TYR A . n 
A 1 24  PHE 24  26  26  PHE PHE A . n 
A 1 25  PHE 25  27  27  PHE PHE A . n 
A 1 26  ALA 26  28  28  ALA ALA A . n 
A 1 27  ILE 27  29  29  ILE ILE A . n 
A 1 28  ASN 28  30  30  ASN ASN A . n 
A 1 29  ASP 29  31  31  ASP ASP A . n 
A 1 30  PRO 30  32  32  PRO PRO A . n 
A 1 31  ALA 31  33  33  ALA ALA A . n 
A 1 32  THR 32  34  34  THR THR A . n 
A 1 33  PHE 33  35  35  PHE PHE A . n 
A 1 34  LYS 34  36  36  LYS LYS A . n 
A 1 35  THR 35  37  37  THR THR A . n 
A 1 36  HIS 36  38  38  HIS HIS A . n 
A 1 37  LEU 37  39  39  LEU LEU A . n 
A 1 38  ALA 38  40  40  ALA ALA A . n 
A 1 39  SER 39  41  41  SER SER A . n 
A 1 40  ASP 40  42  42  ASP ASP A . n 
A 1 41  ILE 41  43  43  ILE ILE A . n 
A 1 42  ALA 42  44  44  ALA ALA A . n 
A 1 43  PRO 43  45  45  PRO PRO A . n 
A 1 44  VAL 44  46  46  VAL VAL A . n 
A 1 45  VAL 45  47  47  VAL VAL A . n 
A 1 46  ALA 46  48  48  ALA ALA A . n 
A 1 47  SER 47  49  49  SER SER A . n 
A 1 48  VAL 48  50  50  VAL VAL A . n 
A 1 49  THR 49  51  51  THR THR A . n 
A 1 50  GLN 50  52  52  GLN GLN A . n 
A 1 51  LEU 51  53  53  LEU LEU A . n 
A 1 52  SER 52  54  54  SER SER A . n 
A 1 53  ASN 53  55  55  ASN ASN A . n 
A 1 54  VAL 54  56  56  VAL VAL A . n 
A 1 55  ALA 55  57  57  ALA ALA A . n 
A 1 56  THR 56  58  58  THR THR A . n 
A 1 57  GLN 57  59  59  GLN GLN A . n 
A 1 58  PRO 58  60  60  PRO PRO A . n 
A 1 59  LEU 59  61  61  LEU LEU A . n 
A 1 60  VAL 60  62  62  VAL VAL A . n 
A 1 61  ALA 61  63  63  ALA ALA A . n 
A 1 62  LEU 62  64  64  LEU LEU A . n 
A 1 63  ASN 63  65  65  ASN ASN A . n 
A 1 64  ILE 64  66  66  ILE ILE A . n 
A 1 65  ALA 65  67  67  ALA ALA A . n 
A 1 66  PHE 66  68  68  PHE PHE A . n 
A 1 67  SER 67  69  69  SER SER A . n 
A 1 68  ASN 68  70  70  ASN ASN A . n 
A 1 69  THR 69  71  71  THR THR A . n 
A 1 70  GLY 70  72  72  GLY GLY A . n 
A 1 71  LEU 71  73  73  LEU LEU A . n 
A 1 72  LEU 72  74  74  LEU LEU A . n 
A 1 73  ALA 73  75  75  ALA ALA A . n 
A 1 74  LEU 74  76  76  LEU LEU A . n 
A 1 75  GLY 75  77  77  GLY GLY A . n 
A 1 76  VAL 76  78  78  VAL VAL A . n 
A 1 77  THR 77  79  79  THR THR A . n 
A 1 78  ASP 78  80  80  ASP ASP A . n 
A 1 79  ASN 79  81  81  ASN ASN A . n 
A 1 80  LEU 80  82  82  LEU LEU A . n 
A 1 81  GLY 81  83  83  GLY GLY A . n 
A 1 82  ASP 82  84  84  ASP ASP A . n 
A 1 83  SER 83  85  85  SER SER A . n 
A 1 84  LEU 84  86  86  LEU LEU A . n 
A 1 85  PHE 85  87  87  PHE PHE A . n 
A 1 86  ALA 86  88  88  ALA ALA A . n 
A 1 87  ASN 87  89  89  ASN ASN A . n 
A 1 88  GLY 88  90  90  GLY GLY A . n 
A 1 89  GLN 89  91  91  GLN GLN A . n 
A 1 90  ALA 90  92  92  ALA ALA A . n 
A 1 91  LYS 91  93  93  LYS LYS A . n 
A 1 92  ASP 92  94  94  ASP ASP A . n 
A 1 93  ALA 93  95  95  ALA ALA A . n 
A 1 94  THR 94  96  96  THR THR A . n 
A 1 95  SER 95  97  97  SER SER A . n 
A 1 96  PHE 96  98  98  PHE PHE A . n 
A 1 97  LYS 97  99  99  LYS LYS A . n 
A 1 98  GLU 98  100 100 GLU GLU A . n 
A 1 99  SER 99  101 101 SER SER A . n 
A 1 100 THR 100 102 102 THR THR A . n 
A 1 101 SER 101 103 103 SER SER A . n 
A 1 102 SER 102 104 104 SER SER A . n 
A 1 103 TRP 103 105 105 TRP TRP A . n 
A 1 104 VAL 104 106 106 VAL VAL A . n 
A 1 105 PRO 105 107 107 PRO PRO A . n 
A 1 106 GLN 106 108 108 GLN GLN A . n 
A 1 107 PHE 107 109 109 PHE PHE A . n 
A 1 108 ALA 108 110 110 ALA ALA A . n 
A 1 109 GLY 109 111 111 GLY GLY A . n 
A 1 110 THR 110 112 112 THR THR A . n 
A 1 111 GLY 111 113 113 GLY GLY A . n 
A 1 112 ILE 112 114 114 ILE ILE A . n 
A 1 113 HIS 113 115 115 HIS HIS A . n 
A 1 114 GLY 114 116 116 GLY GLY A . n 
A 1 115 VAL 115 117 117 VAL VAL A . n 
A 1 116 ILE 116 118 118 ILE ILE A . n 
A 1 117 ILE 117 119 119 ILE ILE A . n 
A 1 118 LEU 118 120 120 LEU LEU A . n 
A 1 119 ALA 119 121 121 ALA ALA A . n 
A 1 120 SER 120 122 122 SER SER A . n 
A 1 121 ASP 121 123 123 ASP ASP A . n 
A 1 122 THR 122 124 124 THR THR A . n 
A 1 123 THR 123 125 125 THR THR A . n 
A 1 124 ASP 124 126 126 ASP ASP A . n 
A 1 125 LEU 125 127 127 LEU LEU A . n 
A 1 126 ILE 126 128 128 ILE ILE A . n 
A 1 127 ASP 127 129 129 ASP ASP A . n 
A 1 128 GLN 128 130 130 GLN GLN A . n 
A 1 129 GLN 129 131 131 GLN GLN A . n 
A 1 130 VAL 130 132 132 VAL VAL A . n 
A 1 131 ALA 131 133 133 ALA ALA A . n 
A 1 132 SER 132 134 134 SER SER A . n 
A 1 133 ILE 133 135 135 ILE ILE A . n 
A 1 134 GLU 134 136 136 GLU GLU A . n 
A 1 135 SER 135 137 137 SER SER A . n 
A 1 136 THR 136 138 138 THR THR A . n 
A 1 137 PHE 137 139 139 PHE PHE A . n 
A 1 138 GLY 138 140 140 GLY GLY A . n 
A 1 139 SER 139 141 141 SER SER A . n 
A 1 140 SER 140 142 142 SER SER A . n 
A 1 141 ILE 141 143 143 ILE ILE A . n 
A 1 142 SER 142 144 144 SER SER A . n 
A 1 143 LYS 143 145 145 LYS LYS A . n 
A 1 144 LEU 144 146 146 LEU LEU A . n 
A 1 145 TYR 145 147 147 TYR TYR A . n 
A 1 146 SER 146 148 148 SER SER A . n 
A 1 147 LEU 147 149 149 LEU LEU A . n 
A 1 148 SER 148 150 150 SER SER A . n 
A 1 149 ALA 149 151 151 ALA ALA A . n 
A 1 150 SER 150 152 152 SER SER A . n 
A 1 151 ILE 151 153 153 ILE ILE A . n 
A 1 152 ARG 152 154 154 ARG ARG A . n 
A 1 153 PRO 153 155 155 PRO PRO A . n 
A 1 154 GLY 154 156 156 GLY GLY A . n 
A 1 155 ASN 155 157 157 ASN ASN A . n 
A 1 156 GLU 156 158 158 GLU GLU A . n 
A 1 157 ALA 157 159 159 ALA ALA A . n 
A 1 158 GLY 158 160 160 GLY GLY A . n 
A 1 159 HIS 159 161 161 HIS HIS A . n 
A 1 160 GLU 160 162 162 GLU GLU A . n 
A 1 161 MET 161 163 163 MET MET A . n 
A 1 162 PHE 162 164 164 PHE PHE A . n 
A 1 163 GLY 163 165 165 GLY GLY A . n 
A 1 164 PHE 164 166 166 PHE PHE A . n 
A 1 165 LEU 165 167 167 LEU LEU A . n 
A 1 166 ASP 166 168 168 ASP ASP A . n 
A 1 167 GLY 167 169 169 GLY GLY A . n 
A 1 168 ILE 168 170 170 ILE ILE A . n 
A 1 169 ALA 169 171 171 ALA ALA A . n 
A 1 170 GLN 170 172 172 GLN GLN A . n 
A 1 171 PRO 171 173 173 PRO PRO A . n 
A 1 172 ALA 172 174 174 ALA ALA A . n 
A 1 173 ILE 173 175 175 ILE ILE A . n 
A 1 174 ASN 174 176 176 ASN ASN A . n 
A 1 175 GLY 175 177 177 GLY GLY A . n 
A 1 176 PHE 176 178 178 PHE PHE A . n 
A 1 177 ASN 177 179 179 ASN ASN A . n 
A 1 178 THR 178 180 180 THR THR A . n 
A 1 179 PRO 179 181 181 PRO PRO A . n 
A 1 180 LEU 180 182 182 LEU LEU A . n 
A 1 181 PRO 181 183 183 PRO PRO A . n 
A 1 182 GLY 182 184 184 GLY GLY A . n 
A 1 183 GLN 183 185 185 GLN GLN A . n 
A 1 184 ASN 184 186 186 ASN ASN A . n 
A 1 185 ILE 185 187 187 ILE ILE A . n 
A 1 186 VAL 186 188 188 VAL VAL A . n 
A 1 187 ASP 187 189 189 ASP ASP A . n 
A 1 188 ALA 188 190 190 ALA ALA A . n 
A 1 189 GLY 189 191 191 GLY GLY A . n 
A 1 190 VAL 190 192 192 VAL VAL A . n 
A 1 191 ILE 191 193 193 ILE ILE A . n 
A 1 192 ILE 192 194 194 ILE ILE A . n 
A 1 193 THR 193 195 195 THR THR A . n 
A 1 194 GLY 194 196 196 GLY GLY A . n 
A 1 195 ALA 195 197 197 ALA ALA A . n 
A 1 196 THR 196 198 198 THR THR A . n 
A 1 197 ASN 197 199 199 ASN ASN A . n 
A 1 198 ASP 198 200 200 ASP ASP A . n 
A 1 199 PRO 199 201 201 PRO PRO A . n 
A 1 200 ILE 200 202 202 ILE ILE A . n 
A 1 201 THR 201 203 203 THR THR A . n 
A 1 202 ARG 202 204 204 ARG ARG A . n 
A 1 203 PRO 203 205 205 PRO PRO A . n 
A 1 204 SER 204 206 206 SER SER A . n 
A 1 205 TRP 205 207 207 TRP TRP A . n 
A 1 206 ALA 206 208 208 ALA ALA A . n 
A 1 207 VAL 207 209 209 VAL VAL A . n 
A 1 208 GLY 208 210 210 GLY GLY A . n 
A 1 209 GLY 209 211 211 GLY GLY A . n 
A 1 210 SER 210 212 212 SER SER A . n 
A 1 211 PHE 211 213 213 PHE PHE A . n 
A 1 212 LEU 212 214 214 LEU LEU A . n 
A 1 213 ALA 213 215 215 ALA ALA A . n 
A 1 214 PHE 214 216 216 PHE PHE A . n 
A 1 215 ARG 215 217 217 ARG ARG A . n 
A 1 216 GLN 216 218 218 GLN GLN A . n 
A 1 217 LEU 217 219 219 LEU LEU A . n 
A 1 218 GLU 218 220 220 GLU GLU A . n 
A 1 219 GLN 219 221 221 GLN GLN A . n 
A 1 220 LEU 220 222 222 LEU LEU A . n 
A 1 221 VAL 221 223 223 VAL VAL A . n 
A 1 222 PRO 222 224 224 PRO PRO A . n 
A 1 223 GLU 223 225 225 GLU GLU A . n 
A 1 224 PHE 224 226 226 PHE PHE A . n 
A 1 225 ASN 225 227 227 ASN ASN A . n 
A 1 226 LYS 226 228 228 LYS LYS A . n 
A 1 227 TYR 227 229 229 TYR TYR A . n 
A 1 228 LEU 228 230 230 LEU LEU A . n 
A 1 229 LEU 229 231 231 LEU LEU A . n 
A 1 230 ASP 230 232 232 ASP ASP A . n 
A 1 231 ASN 231 233 233 ASN ASN A . n 
A 1 232 ALA 232 234 234 ALA ALA A . n 
A 1 233 PRO 233 235 235 PRO PRO A . n 
A 1 234 ALA 234 236 236 ALA ALA A . n 
A 1 235 GLY 235 237 237 GLY GLY A . n 
A 1 236 SER 236 238 238 SER SER A . n 
A 1 237 GLY 237 239 239 GLY GLY A . n 
A 1 238 SER 238 240 240 SER SER A . n 
A 1 239 LEU 239 241 241 LEU LEU A . n 
A 1 240 GLN 240 242 242 GLN GLN A . n 
A 1 241 ALA 241 243 243 ALA ALA A . n 
A 1 242 ARG 242 244 244 ARG ARG A . n 
A 1 243 ALA 243 245 245 ALA ALA A . n 
A 1 244 ASP 244 246 246 ASP ASP A . n 
A 1 245 LEU 245 247 247 LEU LEU A . n 
A 1 246 LEU 246 248 248 LEU LEU A . n 
A 1 247 GLY 247 249 249 GLY GLY A . n 
A 1 248 ALA 248 250 250 ALA ALA A . n 
A 1 249 ARG 249 251 251 ARG ARG A . n 
A 1 250 MET 250 252 252 MET MET A . n 
A 1 251 VAL 251 253 253 VAL VAL A . n 
A 1 252 GLY 252 254 254 GLY GLY A . n 
A 1 253 ARG 253 255 255 ARG ARG A . n 
A 1 254 TRP 254 256 256 TRP TRP A . n 
A 1 255 LYS 255 257 257 LYS LYS A . n 
A 1 256 SER 256 258 258 SER SER A . n 
A 1 257 GLY 257 259 259 GLY GLY A . n 
A 1 258 ALA 258 260 260 ALA ALA A . n 
A 1 259 PRO 259 261 261 PRO PRO A . n 
A 1 260 ILE 260 262 262 ILE ILE A . n 
A 1 261 ASP 261 263 263 ASP ASP A . n 
A 1 262 LEU 262 264 264 LEU LEU A . n 
A 1 263 THR 263 265 265 THR THR A . n 
A 1 264 PRO 264 266 266 PRO PRO A . n 
A 1 265 THR 265 267 267 THR THR A . n 
A 1 266 ALA 266 268 268 ALA ALA A . n 
A 1 267 ASP 267 269 269 ASP ASP A . n 
A 1 268 ASP 268 270 270 ASP ASP A . n 
A 1 269 PRO 269 271 271 PRO PRO A . n 
A 1 270 ALA 270 272 272 ALA ALA A . n 
A 1 271 LEU 271 273 273 LEU LEU A . n 
A 1 272 GLY 272 274 274 GLY GLY A . n 
A 1 273 ALA 273 275 275 ALA ALA A . n 
A 1 274 ASP 274 276 276 ASP ASP A . n 
A 1 275 ALA 275 277 277 ALA ALA A . n 
A 1 276 GLN 276 278 278 GLN GLN A . n 
A 1 277 ARG 277 279 279 ARG ARG A . n 
A 1 278 ASN 278 280 280 ASN ASN A . n 
A 1 279 ASN 279 281 281 ASN ASN A . n 
A 1 280 ASN 280 282 282 ASN ASN A . n 
A 1 281 PHE 281 283 283 PHE PHE A . n 
A 1 282 THR 282 284 284 THR THR A . n 
A 1 283 TYR 283 285 285 TYR TYR A . n 
A 1 284 SER 284 286 286 SER SER A . n 
A 1 285 HIS 285 287 287 HIS HIS A . n 
A 1 286 ALA 286 288 288 ALA ALA A . n 
A 1 287 GLY 287 289 289 GLY GLY A . n 
A 1 288 PHE 288 290 290 PHE PHE A . n 
A 1 289 ASP 289 291 291 ASP ASP A . n 
A 1 290 LEU 290 292 292 LEU LEU A . n 
A 1 291 GLY 291 293 293 GLY GLY A . n 
A 1 292 SER 292 294 294 SER SER A . n 
A 1 293 ASP 293 295 295 ASP ASP A . n 
A 1 294 GLN 294 296 296 GLN GLN A . n 
A 1 295 SER 295 297 297 SER SER A . n 
A 1 296 HIS 296 298 298 HIS HIS A . n 
A 1 297 CYS 297 299 299 CYS CYS A . n 
A 1 298 PRO 298 300 300 PRO PRO A . n 
A 1 299 PHE 299 301 301 PHE PHE A . n 
A 1 300 SER 300 302 302 SER SER A . n 
A 1 301 ALA 301 303 303 ALA ALA A . n 
A 1 302 HIS 302 304 304 HIS HIS A . n 
A 1 303 ILE 303 305 305 ILE ILE A . n 
A 1 304 ARG 304 306 306 ARG ARG A . n 
A 1 305 LYS 305 307 307 LYS LYS A . n 
A 1 306 THR 306 308 308 THR THR A . n 
A 1 307 ARG 307 309 309 ARG ARG A . n 
A 1 308 PRO 308 310 310 PRO PRO A . n 
A 1 309 ARG 309 311 311 ARG ARG A . n 
A 1 310 ALA 310 312 312 ALA ALA A . n 
A 1 311 ASP 311 313 313 ASP ASP A . n 
A 1 312 LEU 312 314 314 LEU LEU A . n 
A 1 313 GLY 313 315 315 GLY GLY A . n 
A 1 314 GLY 314 316 316 GLY GLY A . n 
A 1 315 SER 315 317 317 SER SER A . n 
A 1 316 LEU 316 318 318 LEU LEU A . n 
A 1 317 THR 317 319 319 THR THR A . n 
A 1 318 PRO 318 320 320 PRO PRO A . n 
A 1 319 PRO 319 321 321 PRO PRO A . n 
A 1 320 ASN 320 322 322 ASN ASN A . n 
A 1 321 LEU 321 323 323 LEU LEU A . n 
A 1 322 SER 322 324 324 SER SER A . n 
A 1 323 ALA 323 325 325 ALA ALA A . n 
A 1 324 GLY 324 326 326 GLY GLY A . n 
A 1 325 ALA 325 327 327 ALA ALA A . n 
A 1 326 ASN 326 328 328 ASN ASN A . n 
A 1 327 SER 327 329 329 SER SER A . n 
A 1 328 ILE 328 330 330 ILE ILE A . n 
A 1 329 MET 329 331 331 MET MET A . n 
A 1 330 ARG 330 332 332 ARG ARG A . n 
A 1 331 SER 331 333 333 SER SER A . n 
A 1 332 GLY 332 334 334 GLY GLY A . n 
A 1 333 ILE 333 335 335 ILE ILE A . n 
A 1 334 PRO 334 336 336 PRO PRO A . n 
A 1 335 TYR 335 337 337 TYR TYR A . n 
A 1 336 GLY 336 338 338 GLY GLY A . n 
A 1 337 PRO 337 339 339 PRO PRO A . n 
A 1 338 GLU 338 340 340 GLU GLU A . n 
A 1 339 VAL 339 341 341 VAL VAL A . n 
A 1 340 THR 340 342 342 THR THR A . n 
A 1 341 SER 341 343 343 SER SER A . n 
A 1 342 ALA 342 344 344 ALA ALA A . n 
A 1 343 GLU 343 345 345 GLU GLU A . n 
A 1 344 SER 344 346 346 SER SER A . n 
A 1 345 ALA 345 347 347 ALA ALA A . n 
A 1 346 SER 346 348 348 SER SER A . n 
A 1 347 ASN 347 349 349 ASN ASN A . n 
A 1 348 THR 348 350 350 THR THR A . n 
A 1 349 THR 349 351 351 THR THR A . n 
A 1 350 THR 350 352 352 THR THR A . n 
A 1 351 GLN 351 353 353 GLN GLN A . n 
A 1 352 GLU 352 354 354 GLU GLU A . n 
A 1 353 ARG 353 355 355 ARG ARG A . n 
A 1 354 GLY 354 356 356 GLY GLY A . n 
A 1 355 LEU 355 357 357 LEU LEU A . n 
A 1 356 ALA 356 358 358 ALA ALA A . n 
A 1 357 PHE 357 359 359 PHE PHE A . n 
A 1 358 VAL 358 360 360 VAL VAL A . n 
A 1 359 ALA 359 361 361 ALA ALA A . n 
A 1 360 TYR 360 362 362 TYR TYR A . n 
A 1 361 GLN 361 363 363 GLN GLN A . n 
A 1 362 ALA 362 364 364 ALA ALA A . n 
A 1 363 GLN 363 365 365 GLN GLN A . n 
A 1 364 LEU 364 366 366 LEU LEU A . n 
A 1 365 SER 365 367 367 SER SER A . n 
A 1 366 GLN 366 368 368 GLN GLN A . n 
A 1 367 GLY 367 369 369 GLY GLY A . n 
A 1 368 PHE 368 370 370 PHE PHE A . n 
A 1 369 HIS 369 371 371 HIS HIS A . n 
A 1 370 PHE 370 372 372 PHE PHE A . n 
A 1 371 LEU 371 373 373 LEU LEU A . n 
A 1 372 GLN 372 374 374 GLN GLN A . n 
A 1 373 GLN 373 375 375 GLN GLN A . n 
A 1 374 THR 374 376 376 THR THR A . n 
A 1 375 TRP 375 377 377 TRP TRP A . n 
A 1 376 ALA 376 378 378 ALA ALA A . n 
A 1 377 ASP 377 379 379 ASP ASP A . n 
A 1 378 ASN 378 380 380 ASN ASN A . n 
A 1 379 ALA 379 381 381 ALA ALA A . n 
A 1 380 ASN 380 382 382 ASN ASN A . n 
A 1 381 PHE 381 383 383 PHE PHE A . n 
A 1 382 PRO 382 384 384 PRO PRO A . n 
A 1 383 PRO 383 385 385 PRO PRO A . n 
A 1 384 GLY 384 386 386 GLY GLY A . n 
A 1 385 LYS 385 387 387 LYS LYS A . n 
A 1 386 THR 386 388 388 THR THR A . n 
A 1 387 PRO 387 389 389 PRO PRO A . n 
A 1 388 ALA 388 390 390 ALA ALA A . n 
A 1 389 THR 389 391 391 THR THR A . n 
A 1 390 VAL 390 392 392 VAL VAL A . n 
A 1 391 GLY 391 393 393 GLY GLY A . n 
A 1 392 LEU 392 394 394 LEU LEU A . n 
A 1 393 ASP 393 395 395 ASP ASP A . n 
A 1 394 PRO 394 396 396 PRO PRO A . n 
A 1 395 ILE 395 397 397 ILE ILE A . n 
A 1 396 ILE 396 398 398 ILE ILE A . n 
A 1 397 GLY 397 399 399 GLY GLY A . n 
A 1 398 GLN 398 400 400 GLN GLN A . n 
A 1 399 ASN 399 401 401 ASN ASN A . n 
A 1 400 ASN 400 402 402 ASN ASN A . n 
A 1 401 GLY 401 403 403 GLY GLY A . n 
A 1 402 GLN 402 404 404 GLN GLN A . n 
A 1 403 PRO 403 405 405 PRO PRO A . n 
A 1 404 ARG 404 406 406 ARG ARG A . n 
A 1 405 VAL 405 407 407 VAL VAL A . n 
A 1 406 VAL 406 408 408 VAL VAL A . n 
A 1 407 ASN 407 409 409 ASN ASN A . n 
A 1 408 GLY 408 410 410 GLY GLY A . n 
A 1 409 LEU 409 411 411 LEU LEU A . n 
A 1 410 LEU 410 412 412 LEU LEU A . n 
A 1 411 PRO 411 413 413 PRO PRO A . n 
A 1 412 SER 412 414 414 SER SER A . n 
A 1 413 ASN 413 415 415 ASN ASN A . n 
A 1 414 SER 414 416 416 SER SER A . n 
A 1 415 SER 415 417 417 SER SER A . n 
A 1 416 ALA 416 418 418 ALA ALA A . n 
A 1 417 SER 417 419 419 SER SER A . n 
A 1 418 LEU 418 420 420 LEU LEU A . n 
A 1 419 SER 419 421 421 SER SER A . n 
A 1 420 ILE 420 422 422 ILE ILE A . n 
A 1 421 PRO 421 423 423 PRO PRO A . n 
A 1 422 GLN 422 424 424 GLN GLN A . n 
A 1 423 PHE 423 425 425 PHE PHE A . n 
A 1 424 VAL 424 426 426 VAL VAL A . n 
A 1 425 VAL 425 427 427 VAL VAL A . n 
A 1 426 SER 426 428 428 SER SER A . n 
A 1 427 HIS 427 429 429 HIS HIS A . n 
A 1 428 GLY 428 430 430 GLY GLY A . n 
A 1 429 GLY 429 431 431 GLY GLY A . n 
A 1 430 GLU 430 432 432 GLU GLU A . n 
A 1 431 TYR 431 433 433 TYR TYR A . n 
A 1 432 PHE 432 434 434 PHE PHE A . n 
A 1 433 PHE 433 435 435 PHE PHE A . n 
A 1 434 SER 434 436 436 SER SER A . n 
A 1 435 PRO 435 437 437 PRO PRO A . n 
A 1 436 PRO 436 438 438 PRO PRO A . n 
A 1 437 ILE 437 439 439 ILE ILE A . n 
A 1 438 SER 438 440 440 SER SER A . n 
A 1 439 ALA 439 441 441 ALA ALA A . n 
A 1 440 ILE 440 442 442 ILE ILE A . n 
A 1 441 GLY 441 443 443 GLY GLY A . n 
A 1 442 GLY 442 444 444 GLY GLY A . n 
A 1 443 ARG 443 445 445 ARG ARG A . n 
A 1 444 LEU 444 446 446 LEU LEU A . n 
A 1 445 SER 445 447 447 SER SER A . n 
A 1 446 ALA 446 448 448 ALA ALA A . n 
B 1 1   SER 1   3   ?   ?   ?   B . n 
B 1 2   LEU 2   4   4   LEU LEU B . n 
B 1 3   ASN 3   5   5   ASN ASN B . n 
B 1 4   THR 4   6   6   THR THR B . n 
B 1 5   ASP 5   7   7   ASP ASP B . n 
B 1 6   ASP 6   8   8   ASP ASP B . n 
B 1 7   ILE 7   9   9   ILE ILE B . n 
B 1 8   GLN 8   10  10  GLN GLN B . n 
B 1 9   GLY 9   11  11  GLY GLY B . n 
B 1 10  ASP 10  12  12  ASP ASP B . n 
B 1 11  ILE 11  13  13  ILE ILE B . n 
B 1 12  LEU 12  14  14  LEU LEU B . n 
B 1 13  VAL 13  15  15  VAL VAL B . n 
B 1 14  GLY 14  16  16  GLY GLY B . n 
B 1 15  MET 15  17  17  MET MET B . n 
B 1 16  HIS 16  18  18  HIS HIS B . n 
B 1 17  LYS 17  19  19  LYS LYS B . n 
B 1 18  GLN 18  20  20  GLN GLN B . n 
B 1 19  LYS 19  21  21  LYS LYS B . n 
B 1 20  GLN 20  22  22  GLN GLN B . n 
B 1 21  LEU 21  23  23  LEU LEU B . n 
B 1 22  PHE 22  24  24  PHE PHE B . n 
B 1 23  TYR 23  25  25  TYR TYR B . n 
B 1 24  PHE 24  26  26  PHE PHE B . n 
B 1 25  PHE 25  27  27  PHE PHE B . n 
B 1 26  ALA 26  28  28  ALA ALA B . n 
B 1 27  ILE 27  29  29  ILE ILE B . n 
B 1 28  ASN 28  30  30  ASN ASN B . n 
B 1 29  ASP 29  31  31  ASP ASP B . n 
B 1 30  PRO 30  32  32  PRO PRO B . n 
B 1 31  ALA 31  33  33  ALA ALA B . n 
B 1 32  THR 32  34  34  THR THR B . n 
B 1 33  PHE 33  35  35  PHE PHE B . n 
B 1 34  LYS 34  36  36  LYS LYS B . n 
B 1 35  THR 35  37  37  THR THR B . n 
B 1 36  HIS 36  38  38  HIS HIS B . n 
B 1 37  LEU 37  39  39  LEU LEU B . n 
B 1 38  ALA 38  40  40  ALA ALA B . n 
B 1 39  SER 39  41  41  SER SER B . n 
B 1 40  ASP 40  42  42  ASP ASP B . n 
B 1 41  ILE 41  43  43  ILE ILE B . n 
B 1 42  ALA 42  44  44  ALA ALA B . n 
B 1 43  PRO 43  45  45  PRO PRO B . n 
B 1 44  VAL 44  46  46  VAL VAL B . n 
B 1 45  VAL 45  47  47  VAL VAL B . n 
B 1 46  ALA 46  48  48  ALA ALA B . n 
B 1 47  SER 47  49  49  SER SER B . n 
B 1 48  VAL 48  50  50  VAL VAL B . n 
B 1 49  THR 49  51  51  THR THR B . n 
B 1 50  GLN 50  52  52  GLN GLN B . n 
B 1 51  LEU 51  53  53  LEU LEU B . n 
B 1 52  SER 52  54  54  SER SER B . n 
B 1 53  ASN 53  55  55  ASN ASN B . n 
B 1 54  VAL 54  56  56  VAL VAL B . n 
B 1 55  ALA 55  57  57  ALA ALA B . n 
B 1 56  THR 56  58  58  THR THR B . n 
B 1 57  GLN 57  59  59  GLN GLN B . n 
B 1 58  PRO 58  60  60  PRO PRO B . n 
B 1 59  LEU 59  61  61  LEU LEU B . n 
B 1 60  VAL 60  62  62  VAL VAL B . n 
B 1 61  ALA 61  63  63  ALA ALA B . n 
B 1 62  LEU 62  64  64  LEU LEU B . n 
B 1 63  ASN 63  65  65  ASN ASN B . n 
B 1 64  ILE 64  66  66  ILE ILE B . n 
B 1 65  ALA 65  67  67  ALA ALA B . n 
B 1 66  PHE 66  68  68  PHE PHE B . n 
B 1 67  SER 67  69  69  SER SER B . n 
B 1 68  ASN 68  70  70  ASN ASN B . n 
B 1 69  THR 69  71  71  THR THR B . n 
B 1 70  GLY 70  72  72  GLY GLY B . n 
B 1 71  LEU 71  73  73  LEU LEU B . n 
B 1 72  LEU 72  74  74  LEU LEU B . n 
B 1 73  ALA 73  75  75  ALA ALA B . n 
B 1 74  LEU 74  76  76  LEU LEU B . n 
B 1 75  GLY 75  77  77  GLY GLY B . n 
B 1 76  VAL 76  78  78  VAL VAL B . n 
B 1 77  THR 77  79  79  THR THR B . n 
B 1 78  ASP 78  80  80  ASP ASP B . n 
B 1 79  ASN 79  81  81  ASN ASN B . n 
B 1 80  LEU 80  82  82  LEU LEU B . n 
B 1 81  GLY 81  83  83  GLY GLY B . n 
B 1 82  ASP 82  84  84  ASP ASP B . n 
B 1 83  SER 83  85  85  SER SER B . n 
B 1 84  LEU 84  86  86  LEU LEU B . n 
B 1 85  PHE 85  87  87  PHE PHE B . n 
B 1 86  ALA 86  88  88  ALA ALA B . n 
B 1 87  ASN 87  89  89  ASN ASN B . n 
B 1 88  GLY 88  90  90  GLY GLY B . n 
B 1 89  GLN 89  91  91  GLN GLN B . n 
B 1 90  ALA 90  92  92  ALA ALA B . n 
B 1 91  LYS 91  93  93  LYS LYS B . n 
B 1 92  ASP 92  94  94  ASP ASP B . n 
B 1 93  ALA 93  95  95  ALA ALA B . n 
B 1 94  THR 94  96  96  THR THR B . n 
B 1 95  SER 95  97  97  SER SER B . n 
B 1 96  PHE 96  98  98  PHE PHE B . n 
B 1 97  LYS 97  99  99  LYS LYS B . n 
B 1 98  GLU 98  100 100 GLU GLU B . n 
B 1 99  SER 99  101 101 SER SER B . n 
B 1 100 THR 100 102 102 THR THR B . n 
B 1 101 SER 101 103 103 SER SER B . n 
B 1 102 SER 102 104 104 SER SER B . n 
B 1 103 TRP 103 105 105 TRP TRP B . n 
B 1 104 VAL 104 106 106 VAL VAL B . n 
B 1 105 PRO 105 107 107 PRO PRO B . n 
B 1 106 GLN 106 108 108 GLN GLN B . n 
B 1 107 PHE 107 109 109 PHE PHE B . n 
B 1 108 ALA 108 110 110 ALA ALA B . n 
B 1 109 GLY 109 111 111 GLY GLY B . n 
B 1 110 THR 110 112 112 THR THR B . n 
B 1 111 GLY 111 113 113 GLY GLY B . n 
B 1 112 ILE 112 114 114 ILE ILE B . n 
B 1 113 HIS 113 115 115 HIS HIS B . n 
B 1 114 GLY 114 116 116 GLY GLY B . n 
B 1 115 VAL 115 117 117 VAL VAL B . n 
B 1 116 ILE 116 118 118 ILE ILE B . n 
B 1 117 ILE 117 119 119 ILE ILE B . n 
B 1 118 LEU 118 120 120 LEU LEU B . n 
B 1 119 ALA 119 121 121 ALA ALA B . n 
B 1 120 SER 120 122 122 SER SER B . n 
B 1 121 ASP 121 123 123 ASP ASP B . n 
B 1 122 THR 122 124 124 THR THR B . n 
B 1 123 THR 123 125 125 THR THR B . n 
B 1 124 ASP 124 126 126 ASP ASP B . n 
B 1 125 LEU 125 127 127 LEU LEU B . n 
B 1 126 ILE 126 128 128 ILE ILE B . n 
B 1 127 ASP 127 129 129 ASP ASP B . n 
B 1 128 GLN 128 130 130 GLN GLN B . n 
B 1 129 GLN 129 131 131 GLN GLN B . n 
B 1 130 VAL 130 132 132 VAL VAL B . n 
B 1 131 ALA 131 133 133 ALA ALA B . n 
B 1 132 SER 132 134 134 SER SER B . n 
B 1 133 ILE 133 135 135 ILE ILE B . n 
B 1 134 GLU 134 136 136 GLU GLU B . n 
B 1 135 SER 135 137 137 SER SER B . n 
B 1 136 THR 136 138 138 THR THR B . n 
B 1 137 PHE 137 139 139 PHE PHE B . n 
B 1 138 GLY 138 140 140 GLY GLY B . n 
B 1 139 SER 139 141 141 SER SER B . n 
B 1 140 SER 140 142 142 SER SER B . n 
B 1 141 ILE 141 143 143 ILE ILE B . n 
B 1 142 SER 142 144 144 SER SER B . n 
B 1 143 LYS 143 145 145 LYS LYS B . n 
B 1 144 LEU 144 146 146 LEU LEU B . n 
B 1 145 TYR 145 147 147 TYR TYR B . n 
B 1 146 SER 146 148 148 SER SER B . n 
B 1 147 LEU 147 149 149 LEU LEU B . n 
B 1 148 SER 148 150 150 SER SER B . n 
B 1 149 ALA 149 151 151 ALA ALA B . n 
B 1 150 SER 150 152 152 SER SER B . n 
B 1 151 ILE 151 153 153 ILE ILE B . n 
B 1 152 ARG 152 154 154 ARG ARG B . n 
B 1 153 PRO 153 155 155 PRO PRO B . n 
B 1 154 GLY 154 156 156 GLY GLY B . n 
B 1 155 ASN 155 157 157 ASN ASN B . n 
B 1 156 GLU 156 158 158 GLU GLU B . n 
B 1 157 ALA 157 159 159 ALA ALA B . n 
B 1 158 GLY 158 160 160 GLY GLY B . n 
B 1 159 HIS 159 161 161 HIS HIS B . n 
B 1 160 GLU 160 162 162 GLU GLU B . n 
B 1 161 MET 161 163 163 MET MET B . n 
B 1 162 PHE 162 164 164 PHE PHE B . n 
B 1 163 GLY 163 165 165 GLY GLY B . n 
B 1 164 PHE 164 166 166 PHE PHE B . n 
B 1 165 LEU 165 167 167 LEU LEU B . n 
B 1 166 ASP 166 168 168 ASP ASP B . n 
B 1 167 GLY 167 169 169 GLY GLY B . n 
B 1 168 ILE 168 170 170 ILE ILE B . n 
B 1 169 ALA 169 171 171 ALA ALA B . n 
B 1 170 GLN 170 172 172 GLN GLN B . n 
B 1 171 PRO 171 173 173 PRO PRO B . n 
B 1 172 ALA 172 174 174 ALA ALA B . n 
B 1 173 ILE 173 175 175 ILE ILE B . n 
B 1 174 ASN 174 176 176 ASN ASN B . n 
B 1 175 GLY 175 177 177 GLY GLY B . n 
B 1 176 PHE 176 178 178 PHE PHE B . n 
B 1 177 ASN 177 179 179 ASN ASN B . n 
B 1 178 THR 178 180 180 THR THR B . n 
B 1 179 PRO 179 181 181 PRO PRO B . n 
B 1 180 LEU 180 182 182 LEU LEU B . n 
B 1 181 PRO 181 183 183 PRO PRO B . n 
B 1 182 GLY 182 184 184 GLY GLY B . n 
B 1 183 GLN 183 185 185 GLN GLN B . n 
B 1 184 ASN 184 186 186 ASN ASN B . n 
B 1 185 ILE 185 187 187 ILE ILE B . n 
B 1 186 VAL 186 188 188 VAL VAL B . n 
B 1 187 ASP 187 189 189 ASP ASP B . n 
B 1 188 ALA 188 190 190 ALA ALA B . n 
B 1 189 GLY 189 191 191 GLY GLY B . n 
B 1 190 VAL 190 192 192 VAL VAL B . n 
B 1 191 ILE 191 193 193 ILE ILE B . n 
B 1 192 ILE 192 194 194 ILE ILE B . n 
B 1 193 THR 193 195 195 THR THR B . n 
B 1 194 GLY 194 196 196 GLY GLY B . n 
B 1 195 ALA 195 197 197 ALA ALA B . n 
B 1 196 THR 196 198 198 THR THR B . n 
B 1 197 ASN 197 199 199 ASN ASN B . n 
B 1 198 ASP 198 200 200 ASP ASP B . n 
B 1 199 PRO 199 201 201 PRO PRO B . n 
B 1 200 ILE 200 202 202 ILE ILE B . n 
B 1 201 THR 201 203 203 THR THR B . n 
B 1 202 ARG 202 204 204 ARG ARG B . n 
B 1 203 PRO 203 205 205 PRO PRO B . n 
B 1 204 SER 204 206 206 SER SER B . n 
B 1 205 TRP 205 207 207 TRP TRP B . n 
B 1 206 ALA 206 208 208 ALA ALA B . n 
B 1 207 VAL 207 209 209 VAL VAL B . n 
B 1 208 GLY 208 210 210 GLY GLY B . n 
B 1 209 GLY 209 211 211 GLY GLY B . n 
B 1 210 SER 210 212 212 SER SER B . n 
B 1 211 PHE 211 213 213 PHE PHE B . n 
B 1 212 LEU 212 214 214 LEU LEU B . n 
B 1 213 ALA 213 215 215 ALA ALA B . n 
B 1 214 PHE 214 216 216 PHE PHE B . n 
B 1 215 ARG 215 217 217 ARG ARG B . n 
B 1 216 GLN 216 218 218 GLN GLN B . n 
B 1 217 LEU 217 219 219 LEU LEU B . n 
B 1 218 GLU 218 220 220 GLU GLU B . n 
B 1 219 GLN 219 221 221 GLN GLN B . n 
B 1 220 LEU 220 222 222 LEU LEU B . n 
B 1 221 VAL 221 223 223 VAL VAL B . n 
B 1 222 PRO 222 224 224 PRO PRO B . n 
B 1 223 GLU 223 225 225 GLU GLU B . n 
B 1 224 PHE 224 226 226 PHE PHE B . n 
B 1 225 ASN 225 227 227 ASN ASN B . n 
B 1 226 LYS 226 228 228 LYS LYS B . n 
B 1 227 TYR 227 229 229 TYR TYR B . n 
B 1 228 LEU 228 230 230 LEU LEU B . n 
B 1 229 LEU 229 231 231 LEU LEU B . n 
B 1 230 ASP 230 232 232 ASP ASP B . n 
B 1 231 ASN 231 233 233 ASN ASN B . n 
B 1 232 ALA 232 234 234 ALA ALA B . n 
B 1 233 PRO 233 235 235 PRO PRO B . n 
B 1 234 ALA 234 236 236 ALA ALA B . n 
B 1 235 GLY 235 237 237 GLY GLY B . n 
B 1 236 SER 236 238 238 SER SER B . n 
B 1 237 GLY 237 239 239 GLY GLY B . n 
B 1 238 SER 238 240 240 SER SER B . n 
B 1 239 LEU 239 241 241 LEU LEU B . n 
B 1 240 GLN 240 242 242 GLN GLN B . n 
B 1 241 ALA 241 243 243 ALA ALA B . n 
B 1 242 ARG 242 244 244 ARG ARG B . n 
B 1 243 ALA 243 245 245 ALA ALA B . n 
B 1 244 ASP 244 246 246 ASP ASP B . n 
B 1 245 LEU 245 247 247 LEU LEU B . n 
B 1 246 LEU 246 248 248 LEU LEU B . n 
B 1 247 GLY 247 249 249 GLY GLY B . n 
B 1 248 ALA 248 250 250 ALA ALA B . n 
B 1 249 ARG 249 251 251 ARG ARG B . n 
B 1 250 MET 250 252 252 MET MET B . n 
B 1 251 VAL 251 253 253 VAL VAL B . n 
B 1 252 GLY 252 254 254 GLY GLY B . n 
B 1 253 ARG 253 255 255 ARG ARG B . n 
B 1 254 TRP 254 256 256 TRP TRP B . n 
B 1 255 LYS 255 257 257 LYS LYS B . n 
B 1 256 SER 256 258 258 SER SER B . n 
B 1 257 GLY 257 259 259 GLY GLY B . n 
B 1 258 ALA 258 260 260 ALA ALA B . n 
B 1 259 PRO 259 261 261 PRO PRO B . n 
B 1 260 ILE 260 262 262 ILE ILE B . n 
B 1 261 ASP 261 263 263 ASP ASP B . n 
B 1 262 LEU 262 264 264 LEU LEU B . n 
B 1 263 THR 263 265 265 THR THR B . n 
B 1 264 PRO 264 266 266 PRO PRO B . n 
B 1 265 THR 265 267 267 THR THR B . n 
B 1 266 ALA 266 268 268 ALA ALA B . n 
B 1 267 ASP 267 269 269 ASP ASP B . n 
B 1 268 ASP 268 270 270 ASP ASP B . n 
B 1 269 PRO 269 271 271 PRO PRO B . n 
B 1 270 ALA 270 272 272 ALA ALA B . n 
B 1 271 LEU 271 273 273 LEU LEU B . n 
B 1 272 GLY 272 274 274 GLY GLY B . n 
B 1 273 ALA 273 275 275 ALA ALA B . n 
B 1 274 ASP 274 276 276 ASP ASP B . n 
B 1 275 ALA 275 277 277 ALA ALA B . n 
B 1 276 GLN 276 278 278 GLN GLN B . n 
B 1 277 ARG 277 279 279 ARG ARG B . n 
B 1 278 ASN 278 280 280 ASN ASN B . n 
B 1 279 ASN 279 281 281 ASN ASN B . n 
B 1 280 ASN 280 282 282 ASN ASN B . n 
B 1 281 PHE 281 283 283 PHE PHE B . n 
B 1 282 THR 282 284 284 THR THR B . n 
B 1 283 TYR 283 285 285 TYR TYR B . n 
B 1 284 SER 284 286 286 SER SER B . n 
B 1 285 HIS 285 287 287 HIS HIS B . n 
B 1 286 ALA 286 288 288 ALA ALA B . n 
B 1 287 GLY 287 289 289 GLY GLY B . n 
B 1 288 PHE 288 290 290 PHE PHE B . n 
B 1 289 ASP 289 291 291 ASP ASP B . n 
B 1 290 LEU 290 292 292 LEU LEU B . n 
B 1 291 GLY 291 293 293 GLY GLY B . n 
B 1 292 SER 292 294 294 SER SER B . n 
B 1 293 ASP 293 295 295 ASP ASP B . n 
B 1 294 GLN 294 296 296 GLN GLN B . n 
B 1 295 SER 295 297 297 SER SER B . n 
B 1 296 HIS 296 298 298 HIS HIS B . n 
B 1 297 CYS 297 299 299 CYS CYS B . n 
B 1 298 PRO 298 300 300 PRO PRO B . n 
B 1 299 PHE 299 301 301 PHE PHE B . n 
B 1 300 SER 300 302 302 SER SER B . n 
B 1 301 ALA 301 303 303 ALA ALA B . n 
B 1 302 HIS 302 304 304 HIS HIS B . n 
B 1 303 ILE 303 305 305 ILE ILE B . n 
B 1 304 ARG 304 306 306 ARG ARG B . n 
B 1 305 LYS 305 307 307 LYS LYS B . n 
B 1 306 THR 306 308 308 THR THR B . n 
B 1 307 ARG 307 309 309 ARG ARG B . n 
B 1 308 PRO 308 310 310 PRO PRO B . n 
B 1 309 ARG 309 311 311 ARG ARG B . n 
B 1 310 ALA 310 312 312 ALA ALA B . n 
B 1 311 ASP 311 313 313 ASP ASP B . n 
B 1 312 LEU 312 314 314 LEU LEU B . n 
B 1 313 GLY 313 315 315 GLY GLY B . n 
B 1 314 GLY 314 316 316 GLY GLY B . n 
B 1 315 SER 315 317 317 SER SER B . n 
B 1 316 LEU 316 318 318 LEU LEU B . n 
B 1 317 THR 317 319 319 THR THR B . n 
B 1 318 PRO 318 320 320 PRO PRO B . n 
B 1 319 PRO 319 321 321 PRO PRO B . n 
B 1 320 ASN 320 322 322 ASN ASN B . n 
B 1 321 LEU 321 323 323 LEU LEU B . n 
B 1 322 SER 322 324 324 SER SER B . n 
B 1 323 ALA 323 325 325 ALA ALA B . n 
B 1 324 GLY 324 326 326 GLY GLY B . n 
B 1 325 ALA 325 327 327 ALA ALA B . n 
B 1 326 ASN 326 328 328 ASN ASN B . n 
B 1 327 SER 327 329 329 SER SER B . n 
B 1 328 ILE 328 330 330 ILE ILE B . n 
B 1 329 MET 329 331 331 MET MET B . n 
B 1 330 ARG 330 332 332 ARG ARG B . n 
B 1 331 SER 331 333 333 SER SER B . n 
B 1 332 GLY 332 334 334 GLY GLY B . n 
B 1 333 ILE 333 335 335 ILE ILE B . n 
B 1 334 PRO 334 336 336 PRO PRO B . n 
B 1 335 TYR 335 337 337 TYR TYR B . n 
B 1 336 GLY 336 338 338 GLY GLY B . n 
B 1 337 PRO 337 339 339 PRO PRO B . n 
B 1 338 GLU 338 340 340 GLU GLU B . n 
B 1 339 VAL 339 341 341 VAL VAL B . n 
B 1 340 THR 340 342 342 THR THR B . n 
B 1 341 SER 341 343 343 SER SER B . n 
B 1 342 ALA 342 344 344 ALA ALA B . n 
B 1 343 GLU 343 345 345 GLU GLU B . n 
B 1 344 SER 344 346 346 SER SER B . n 
B 1 345 ALA 345 347 347 ALA ALA B . n 
B 1 346 SER 346 348 348 SER SER B . n 
B 1 347 ASN 347 349 349 ASN ASN B . n 
B 1 348 THR 348 350 350 THR THR B . n 
B 1 349 THR 349 351 351 THR THR B . n 
B 1 350 THR 350 352 352 THR THR B . n 
B 1 351 GLN 351 353 353 GLN GLN B . n 
B 1 352 GLU 352 354 354 GLU GLU B . n 
B 1 353 ARG 353 355 355 ARG ARG B . n 
B 1 354 GLY 354 356 356 GLY GLY B . n 
B 1 355 LEU 355 357 357 LEU LEU B . n 
B 1 356 ALA 356 358 358 ALA ALA B . n 
B 1 357 PHE 357 359 359 PHE PHE B . n 
B 1 358 VAL 358 360 360 VAL VAL B . n 
B 1 359 ALA 359 361 361 ALA ALA B . n 
B 1 360 TYR 360 362 362 TYR TYR B . n 
B 1 361 GLN 361 363 363 GLN GLN B . n 
B 1 362 ALA 362 364 364 ALA ALA B . n 
B 1 363 GLN 363 365 365 GLN GLN B . n 
B 1 364 LEU 364 366 366 LEU LEU B . n 
B 1 365 SER 365 367 367 SER SER B . n 
B 1 366 GLN 366 368 368 GLN GLN B . n 
B 1 367 GLY 367 369 369 GLY GLY B . n 
B 1 368 PHE 368 370 370 PHE PHE B . n 
B 1 369 HIS 369 371 371 HIS HIS B . n 
B 1 370 PHE 370 372 372 PHE PHE B . n 
B 1 371 LEU 371 373 373 LEU LEU B . n 
B 1 372 GLN 372 374 374 GLN GLN B . n 
B 1 373 GLN 373 375 375 GLN GLN B . n 
B 1 374 THR 374 376 376 THR THR B . n 
B 1 375 TRP 375 377 377 TRP TRP B . n 
B 1 376 ALA 376 378 378 ALA ALA B . n 
B 1 377 ASP 377 379 379 ASP ASP B . n 
B 1 378 ASN 378 380 380 ASN ASN B . n 
B 1 379 ALA 379 381 381 ALA ALA B . n 
B 1 380 ASN 380 382 382 ASN ASN B . n 
B 1 381 PHE 381 383 383 PHE PHE B . n 
B 1 382 PRO 382 384 384 PRO PRO B . n 
B 1 383 PRO 383 385 385 PRO PRO B . n 
B 1 384 GLY 384 386 386 GLY GLY B . n 
B 1 385 LYS 385 387 387 LYS LYS B . n 
B 1 386 THR 386 388 388 THR THR B . n 
B 1 387 PRO 387 389 389 PRO PRO B . n 
B 1 388 ALA 388 390 390 ALA ALA B . n 
B 1 389 THR 389 391 391 THR THR B . n 
B 1 390 VAL 390 392 392 VAL VAL B . n 
B 1 391 GLY 391 393 393 GLY GLY B . n 
B 1 392 LEU 392 394 394 LEU LEU B . n 
B 1 393 ASP 393 395 395 ASP ASP B . n 
B 1 394 PRO 394 396 396 PRO PRO B . n 
B 1 395 ILE 395 397 397 ILE ILE B . n 
B 1 396 ILE 396 398 398 ILE ILE B . n 
B 1 397 GLY 397 399 399 GLY GLY B . n 
B 1 398 GLN 398 400 400 GLN GLN B . n 
B 1 399 ASN 399 401 401 ASN ASN B . n 
B 1 400 ASN 400 402 402 ASN ASN B . n 
B 1 401 GLY 401 403 403 GLY GLY B . n 
B 1 402 GLN 402 404 404 GLN GLN B . n 
B 1 403 PRO 403 405 405 PRO PRO B . n 
B 1 404 ARG 404 406 406 ARG ARG B . n 
B 1 405 VAL 405 407 407 VAL VAL B . n 
B 1 406 VAL 406 408 408 VAL VAL B . n 
B 1 407 ASN 407 409 409 ASN ASN B . n 
B 1 408 GLY 408 410 410 GLY GLY B . n 
B 1 409 LEU 409 411 411 LEU LEU B . n 
B 1 410 LEU 410 412 412 LEU LEU B . n 
B 1 411 PRO 411 413 413 PRO PRO B . n 
B 1 412 SER 412 414 414 SER SER B . n 
B 1 413 ASN 413 415 415 ASN ASN B . n 
B 1 414 SER 414 416 416 SER SER B . n 
B 1 415 SER 415 417 417 SER SER B . n 
B 1 416 ALA 416 418 418 ALA ALA B . n 
B 1 417 SER 417 419 419 SER SER B . n 
B 1 418 LEU 418 420 420 LEU LEU B . n 
B 1 419 SER 419 421 421 SER SER B . n 
B 1 420 ILE 420 422 422 ILE ILE B . n 
B 1 421 PRO 421 423 423 PRO PRO B . n 
B 1 422 GLN 422 424 424 GLN GLN B . n 
B 1 423 PHE 423 425 425 PHE PHE B . n 
B 1 424 VAL 424 426 426 VAL VAL B . n 
B 1 425 VAL 425 427 427 VAL VAL B . n 
B 1 426 SER 426 428 428 SER SER B . n 
B 1 427 HIS 427 429 429 HIS HIS B . n 
B 1 428 GLY 428 430 430 GLY GLY B . n 
B 1 429 GLY 429 431 431 GLY GLY B . n 
B 1 430 GLU 430 432 432 GLU GLU B . n 
B 1 431 TYR 431 433 433 TYR TYR B . n 
B 1 432 PHE 432 434 434 PHE PHE B . n 
B 1 433 PHE 433 435 435 PHE PHE B . n 
B 1 434 SER 434 436 436 SER SER B . n 
B 1 435 PRO 435 437 437 PRO PRO B . n 
B 1 436 PRO 436 438 438 PRO PRO B . n 
B 1 437 ILE 437 439 439 ILE ILE B . n 
B 1 438 SER 438 440 440 SER SER B . n 
B 1 439 ALA 439 441 441 ALA ALA B . n 
B 1 440 ILE 440 442 442 ILE ILE B . n 
B 1 441 GLY 441 443 443 GLY GLY B . n 
B 1 442 GLY 442 444 444 GLY GLY B . n 
B 1 443 ARG 443 445 445 ARG ARG B . n 
B 1 444 LEU 444 446 446 LEU LEU B . n 
B 1 445 SER 445 447 447 SER SER B . n 
B 1 446 ALA 446 448 448 ALA ALA B . 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 
C 2 CAC 1   1449 1449 CAC CAC A . 
D 3 GOL 1   1450 1450 GOL GOL A . 
E 3 GOL 1   1451 1451 GOL GOL A . 
F 3 GOL 1   1452 1452 GOL GOL A . 
G 3 GOL 1   1453 1453 GOL GOL A . 
H 4 NAG 1   1454 1454 NAG NAG A . 
I 4 NAG 2   1457 1457 NAG NAG A . 
J 4 NAG 1   1455 1455 NAG NAG A . 
K 4 NAG 1   1456 1456 NAG NAG A . 
L 5 N7H 1   1458 1458 N7H N7H A . 
M 6 FMT 1   1459 1459 FMT FMT A . 
N 7 NO2 1   1460 1460 NO2 NO2 A . 
O 2 CAC 1   1449 1449 CAC CAC B . 
P 3 GOL 1   1450 1450 GOL GOL B . 
Q 3 GOL 1   1451 1451 GOL GOL B . 
R 3 GOL 1   1452 1452 GOL GOL B . 
S 3 GOL 1   1453 1453 GOL GOL B . 
T 4 NAG 1   1454 1454 NAG NAG B . 
U 4 NAG 1   1455 1455 NAG NAG B . 
V 5 N7H 1   1456 1456 N7H N7H B . 
W 7 NO2 1   1457 1457 NO2 NO2 B . 
X 8 HOH 1   2001 2001 HOH HOH A . 
X 8 HOH 2   2002 2002 HOH HOH A . 
X 8 HOH 3   2003 2003 HOH HOH A . 
X 8 HOH 4   2004 2004 HOH HOH A . 
X 8 HOH 5   2005 2005 HOH HOH A . 
X 8 HOH 6   2006 2006 HOH HOH A . 
X 8 HOH 7   2007 2007 HOH HOH A . 
X 8 HOH 8   2008 2008 HOH HOH A . 
X 8 HOH 9   2009 2009 HOH HOH A . 
X 8 HOH 10  2010 2010 HOH HOH A . 
X 8 HOH 11  2011 2011 HOH HOH A . 
X 8 HOH 12  2012 2012 HOH HOH A . 
X 8 HOH 13  2013 2013 HOH HOH A . 
X 8 HOH 14  2014 2014 HOH HOH A . 
X 8 HOH 15  2015 2015 HOH HOH A . 
X 8 HOH 16  2016 2016 HOH HOH A . 
X 8 HOH 17  2017 2017 HOH HOH A . 
X 8 HOH 18  2018 2018 HOH HOH A . 
X 8 HOH 19  2019 2019 HOH HOH A . 
X 8 HOH 20  2020 2020 HOH HOH A . 
X 8 HOH 21  2021 2021 HOH HOH A . 
X 8 HOH 22  2022 2022 HOH HOH A . 
X 8 HOH 23  2023 2023 HOH HOH A . 
X 8 HOH 24  2024 2024 HOH HOH A . 
X 8 HOH 25  2025 2025 HOH HOH A . 
X 8 HOH 26  2026 2026 HOH HOH A . 
X 8 HOH 27  2027 2027 HOH HOH A . 
X 8 HOH 28  2028 2028 HOH HOH A . 
X 8 HOH 29  2029 2029 HOH HOH A . 
X 8 HOH 30  2030 2030 HOH HOH A . 
X 8 HOH 31  2031 2031 HOH HOH A . 
X 8 HOH 32  2032 2032 HOH HOH A . 
X 8 HOH 33  2033 2033 HOH HOH A . 
X 8 HOH 34  2034 2034 HOH HOH A . 
X 8 HOH 35  2035 2035 HOH HOH A . 
X 8 HOH 36  2036 2036 HOH HOH A . 
X 8 HOH 37  2037 2037 HOH HOH A . 
X 8 HOH 38  2038 2038 HOH HOH A . 
X 8 HOH 39  2039 2039 HOH HOH A . 
X 8 HOH 40  2040 2040 HOH HOH A . 
X 8 HOH 41  2041 2041 HOH HOH A . 
X 8 HOH 42  2042 2042 HOH HOH A . 
X 8 HOH 43  2043 2043 HOH HOH A . 
X 8 HOH 44  2044 2044 HOH HOH A . 
X 8 HOH 45  2045 2045 HOH HOH A . 
X 8 HOH 46  2046 2046 HOH HOH A . 
X 8 HOH 47  2047 2047 HOH HOH A . 
X 8 HOH 48  2048 2048 HOH HOH A . 
X 8 HOH 49  2049 2049 HOH HOH A . 
X 8 HOH 50  2050 2050 HOH HOH A . 
X 8 HOH 51  2051 2051 HOH HOH A . 
X 8 HOH 52  2052 2052 HOH HOH A . 
X 8 HOH 53  2053 2053 HOH HOH A . 
X 8 HOH 54  2054 2054 HOH HOH A . 
X 8 HOH 55  2055 2055 HOH HOH A . 
X 8 HOH 56  2056 2056 HOH HOH A . 
X 8 HOH 57  2057 2057 HOH HOH A . 
X 8 HOH 58  2058 2058 HOH HOH A . 
X 8 HOH 59  2059 2059 HOH HOH A . 
X 8 HOH 60  2060 2060 HOH HOH A . 
X 8 HOH 61  2061 2061 HOH HOH A . 
X 8 HOH 62  2062 2062 HOH HOH A . 
X 8 HOH 63  2063 2063 HOH HOH A . 
X 8 HOH 64  2064 2064 HOH HOH A . 
X 8 HOH 65  2065 2065 HOH HOH A . 
X 8 HOH 66  2066 2066 HOH HOH A . 
X 8 HOH 67  2067 2067 HOH HOH A . 
X 8 HOH 68  2068 2068 HOH HOH A . 
X 8 HOH 69  2069 2069 HOH HOH A . 
X 8 HOH 70  2070 2070 HOH HOH A . 
X 8 HOH 71  2071 2071 HOH HOH A . 
X 8 HOH 72  2072 2072 HOH HOH A . 
X 8 HOH 73  2073 2073 HOH HOH A . 
X 8 HOH 74  2074 2074 HOH HOH A . 
X 8 HOH 75  2075 2075 HOH HOH A . 
X 8 HOH 76  2076 2076 HOH HOH A . 
X 8 HOH 77  2077 2077 HOH HOH A . 
X 8 HOH 78  2078 2078 HOH HOH A . 
X 8 HOH 79  2079 2079 HOH HOH A . 
X 8 HOH 80  2080 2080 HOH HOH A . 
X 8 HOH 81  2081 2081 HOH HOH A . 
X 8 HOH 82  2082 2082 HOH HOH A . 
X 8 HOH 83  2083 2083 HOH HOH A . 
X 8 HOH 84  2084 2084 HOH HOH A . 
X 8 HOH 85  2085 2085 HOH HOH A . 
X 8 HOH 86  2086 2086 HOH HOH A . 
X 8 HOH 87  2087 2087 HOH HOH A . 
X 8 HOH 88  2088 2088 HOH HOH A . 
X 8 HOH 89  2089 2089 HOH HOH A . 
X 8 HOH 90  2090 2090 HOH HOH A . 
X 8 HOH 91  2091 2091 HOH HOH A . 
X 8 HOH 92  2092 2092 HOH HOH A . 
X 8 HOH 93  2093 2093 HOH HOH A . 
X 8 HOH 94  2094 2094 HOH HOH A . 
X 8 HOH 95  2095 2095 HOH HOH A . 
X 8 HOH 96  2096 2096 HOH HOH A . 
X 8 HOH 97  2097 2097 HOH HOH A . 
X 8 HOH 98  2098 2098 HOH HOH A . 
X 8 HOH 99  2099 2099 HOH HOH A . 
X 8 HOH 100 2100 2100 HOH HOH A . 
X 8 HOH 101 2101 2101 HOH HOH A . 
X 8 HOH 102 2102 2102 HOH HOH A . 
X 8 HOH 103 2103 2103 HOH HOH A . 
X 8 HOH 104 2104 2104 HOH HOH A . 
X 8 HOH 105 2105 2105 HOH HOH A . 
X 8 HOH 106 2106 2106 HOH HOH A . 
X 8 HOH 107 2107 2107 HOH HOH A . 
X 8 HOH 108 2108 2108 HOH HOH A . 
X 8 HOH 109 2109 2109 HOH HOH A . 
X 8 HOH 110 2110 2110 HOH HOH A . 
X 8 HOH 111 2111 2111 HOH HOH A . 
X 8 HOH 112 2112 2112 HOH HOH A . 
X 8 HOH 113 2113 2113 HOH HOH A . 
X 8 HOH 114 2114 2114 HOH HOH A . 
X 8 HOH 115 2115 2115 HOH HOH A . 
X 8 HOH 116 2116 2116 HOH HOH A . 
X 8 HOH 117 2117 2117 HOH HOH A . 
X 8 HOH 118 2118 2118 HOH HOH A . 
X 8 HOH 119 2119 2119 HOH HOH A . 
X 8 HOH 120 2120 2120 HOH HOH A . 
X 8 HOH 121 2121 2121 HOH HOH A . 
X 8 HOH 122 2122 2122 HOH HOH A . 
X 8 HOH 123 2123 2123 HOH HOH A . 
X 8 HOH 124 2124 2124 HOH HOH A . 
X 8 HOH 125 2125 2125 HOH HOH A . 
X 8 HOH 126 2126 2126 HOH HOH A . 
X 8 HOH 127 2127 2127 HOH HOH A . 
X 8 HOH 128 2128 2128 HOH HOH A . 
X 8 HOH 129 2129 2129 HOH HOH A . 
X 8 HOH 130 2130 2130 HOH HOH A . 
X 8 HOH 131 2131 2131 HOH HOH A . 
X 8 HOH 132 2132 2132 HOH HOH A . 
X 8 HOH 133 2133 2133 HOH HOH A . 
X 8 HOH 134 2134 2134 HOH HOH A . 
X 8 HOH 135 2135 2135 HOH HOH A . 
X 8 HOH 136 2136 2136 HOH HOH A . 
X 8 HOH 137 2137 2137 HOH HOH A . 
X 8 HOH 138 2138 2138 HOH HOH A . 
X 8 HOH 139 2139 2139 HOH HOH A . 
X 8 HOH 140 2140 2140 HOH HOH A . 
X 8 HOH 141 2141 2141 HOH HOH A . 
X 8 HOH 142 2142 2142 HOH HOH A . 
X 8 HOH 143 2143 2143 HOH HOH A . 
X 8 HOH 144 2144 2144 HOH HOH A . 
X 8 HOH 145 2145 2145 HOH HOH A . 
X 8 HOH 146 2146 2146 HOH HOH A . 
X 8 HOH 147 2147 2147 HOH HOH A . 
X 8 HOH 148 2148 2148 HOH HOH A . 
X 8 HOH 149 2149 2149 HOH HOH A . 
X 8 HOH 150 2150 2150 HOH HOH A . 
X 8 HOH 151 2151 2151 HOH HOH A . 
X 8 HOH 152 2152 2152 HOH HOH A . 
X 8 HOH 153 2153 2153 HOH HOH A . 
X 8 HOH 154 2154 2154 HOH HOH A . 
X 8 HOH 155 2155 2155 HOH HOH A . 
X 8 HOH 156 2156 2156 HOH HOH A . 
X 8 HOH 157 2157 2157 HOH HOH A . 
X 8 HOH 158 2158 2158 HOH HOH A . 
X 8 HOH 159 2159 2159 HOH HOH A . 
X 8 HOH 160 2160 2160 HOH HOH A . 
X 8 HOH 161 2161 2161 HOH HOH A . 
X 8 HOH 162 2162 2162 HOH HOH A . 
X 8 HOH 163 2163 2163 HOH HOH A . 
X 8 HOH 164 2164 2164 HOH HOH A . 
X 8 HOH 165 2165 2165 HOH HOH A . 
X 8 HOH 166 2166 2166 HOH HOH A . 
X 8 HOH 167 2167 2167 HOH HOH A . 
X 8 HOH 168 2168 2168 HOH HOH A . 
X 8 HOH 169 2169 2169 HOH HOH A . 
X 8 HOH 170 2170 2170 HOH HOH A . 
X 8 HOH 171 2171 2171 HOH HOH A . 
X 8 HOH 172 2172 2172 HOH HOH A . 
X 8 HOH 173 2173 2173 HOH HOH A . 
X 8 HOH 174 2174 2174 HOH HOH A . 
X 8 HOH 175 2175 2175 HOH HOH A . 
X 8 HOH 176 2176 2176 HOH HOH A . 
X 8 HOH 177 2177 2177 HOH HOH A . 
X 8 HOH 178 2178 2178 HOH HOH A . 
X 8 HOH 179 2179 2179 HOH HOH A . 
X 8 HOH 180 2180 2180 HOH HOH A . 
X 8 HOH 181 2181 2181 HOH HOH A . 
X 8 HOH 182 2182 2182 HOH HOH A . 
X 8 HOH 183 2183 2183 HOH HOH A . 
X 8 HOH 184 2184 2184 HOH HOH A . 
X 8 HOH 185 2185 2185 HOH HOH A . 
X 8 HOH 186 2186 2186 HOH HOH A . 
X 8 HOH 187 2187 2187 HOH HOH A . 
X 8 HOH 188 2188 2188 HOH HOH A . 
X 8 HOH 189 2189 2189 HOH HOH A . 
X 8 HOH 190 2190 2190 HOH HOH A . 
X 8 HOH 191 2191 2191 HOH HOH A . 
X 8 HOH 192 2192 2192 HOH HOH A . 
X 8 HOH 193 2193 2193 HOH HOH A . 
X 8 HOH 194 2194 2194 HOH HOH A . 
X 8 HOH 195 2195 2195 HOH HOH A . 
X 8 HOH 196 2196 2196 HOH HOH A . 
X 8 HOH 197 2197 2197 HOH HOH A . 
X 8 HOH 198 2198 2198 HOH HOH A . 
X 8 HOH 199 2199 2199 HOH HOH A . 
X 8 HOH 200 2200 2200 HOH HOH A . 
X 8 HOH 201 2201 2201 HOH HOH A . 
X 8 HOH 202 2202 2202 HOH HOH A . 
X 8 HOH 203 2203 2203 HOH HOH A . 
X 8 HOH 204 2204 2204 HOH HOH A . 
X 8 HOH 205 2205 2205 HOH HOH A . 
X 8 HOH 206 2206 2206 HOH HOH A . 
X 8 HOH 207 2207 2207 HOH HOH A . 
X 8 HOH 208 2208 2208 HOH HOH A . 
X 8 HOH 209 2209 2209 HOH HOH A . 
X 8 HOH 210 2210 2210 HOH HOH A . 
X 8 HOH 211 2211 2211 HOH HOH A . 
X 8 HOH 212 2212 2212 HOH HOH A . 
X 8 HOH 213 2213 2213 HOH HOH A . 
X 8 HOH 214 2214 2214 HOH HOH A . 
X 8 HOH 215 2215 2215 HOH HOH A . 
X 8 HOH 216 2216 2216 HOH HOH A . 
X 8 HOH 217 2217 2217 HOH HOH A . 
X 8 HOH 218 2218 2218 HOH HOH A . 
X 8 HOH 219 2219 2219 HOH HOH A . 
X 8 HOH 220 2220 2220 HOH HOH A . 
X 8 HOH 221 2221 2221 HOH HOH A . 
X 8 HOH 222 2222 2222 HOH HOH A . 
X 8 HOH 223 2223 2223 HOH HOH A . 
X 8 HOH 224 2224 2224 HOH HOH A . 
X 8 HOH 225 2225 2225 HOH HOH A . 
X 8 HOH 226 2226 2226 HOH HOH A . 
X 8 HOH 227 2227 2227 HOH HOH A . 
X 8 HOH 228 2228 2228 HOH HOH A . 
X 8 HOH 229 2229 2229 HOH HOH A . 
X 8 HOH 230 2230 2230 HOH HOH A . 
X 8 HOH 231 2231 2231 HOH HOH A . 
X 8 HOH 232 2232 2232 HOH HOH A . 
X 8 HOH 233 2233 2233 HOH HOH A . 
X 8 HOH 234 2234 2234 HOH HOH A . 
X 8 HOH 235 2235 2235 HOH HOH A . 
X 8 HOH 236 2236 2236 HOH HOH A . 
X 8 HOH 237 2237 2237 HOH HOH A . 
X 8 HOH 238 2238 2238 HOH HOH A . 
X 8 HOH 239 2239 2239 HOH HOH A . 
X 8 HOH 240 2240 2240 HOH HOH A . 
X 8 HOH 241 2241 2241 HOH HOH A . 
X 8 HOH 242 2242 2242 HOH HOH A . 
X 8 HOH 243 2243 2243 HOH HOH A . 
X 8 HOH 244 2244 2244 HOH HOH A . 
X 8 HOH 245 2245 2245 HOH HOH A . 
X 8 HOH 246 2246 2246 HOH HOH A . 
X 8 HOH 247 2247 2247 HOH HOH A . 
X 8 HOH 248 2248 2248 HOH HOH A . 
X 8 HOH 249 2249 2249 HOH HOH A . 
X 8 HOH 250 2250 2250 HOH HOH A . 
X 8 HOH 251 2251 2251 HOH HOH A . 
X 8 HOH 252 2252 2252 HOH HOH A . 
X 8 HOH 253 2253 2253 HOH HOH A . 
X 8 HOH 254 2254 2254 HOH HOH A . 
X 8 HOH 255 2255 2255 HOH HOH A . 
X 8 HOH 256 2256 2256 HOH HOH A . 
X 8 HOH 257 2257 2257 HOH HOH A . 
X 8 HOH 258 2258 2258 HOH HOH A . 
X 8 HOH 259 2259 2259 HOH HOH A . 
X 8 HOH 260 2260 2260 HOH HOH A . 
X 8 HOH 261 2261 2261 HOH HOH A . 
X 8 HOH 262 2262 2262 HOH HOH A . 
X 8 HOH 263 2263 2263 HOH HOH A . 
X 8 HOH 264 2264 2264 HOH HOH A . 
X 8 HOH 265 2265 2265 HOH HOH A . 
X 8 HOH 266 2266 2266 HOH HOH A . 
X 8 HOH 267 2267 2267 HOH HOH A . 
X 8 HOH 268 2268 2268 HOH HOH A . 
X 8 HOH 269 2269 2269 HOH HOH A . 
X 8 HOH 270 2270 2270 HOH HOH A . 
X 8 HOH 271 2271 2271 HOH HOH A . 
X 8 HOH 272 2272 2272 HOH HOH A . 
X 8 HOH 273 2273 2273 HOH HOH A . 
X 8 HOH 274 2274 2274 HOH HOH A . 
X 8 HOH 275 2275 2275 HOH HOH A . 
X 8 HOH 276 2276 2276 HOH HOH A . 
X 8 HOH 277 2277 2277 HOH HOH A . 
X 8 HOH 278 2278 2278 HOH HOH A . 
X 8 HOH 279 2279 2279 HOH HOH A . 
X 8 HOH 280 2280 2280 HOH HOH A . 
X 8 HOH 281 2281 2281 HOH HOH A . 
X 8 HOH 282 2282 2282 HOH HOH A . 
X 8 HOH 283 2283 2283 HOH HOH A . 
X 8 HOH 284 2284 2284 HOH HOH A . 
X 8 HOH 285 2285 2285 HOH HOH A . 
X 8 HOH 286 2286 2286 HOH HOH A . 
X 8 HOH 287 2287 2287 HOH HOH A . 
X 8 HOH 288 2288 2288 HOH HOH A . 
X 8 HOH 289 2289 2289 HOH HOH A . 
X 8 HOH 290 2290 2290 HOH HOH A . 
X 8 HOH 291 2291 2291 HOH HOH A . 
X 8 HOH 292 2292 2292 HOH HOH A . 
X 8 HOH 293 2293 2293 HOH HOH A . 
X 8 HOH 294 2294 2294 HOH HOH A . 
X 8 HOH 295 2295 2295 HOH HOH A . 
X 8 HOH 296 2296 2296 HOH HOH A . 
X 8 HOH 297 2297 2297 HOH HOH A . 
X 8 HOH 298 2298 2298 HOH HOH A . 
X 8 HOH 299 2299 2299 HOH HOH A . 
X 8 HOH 300 2300 2300 HOH HOH A . 
X 8 HOH 301 2301 2301 HOH HOH A . 
X 8 HOH 302 2302 2302 HOH HOH A . 
X 8 HOH 303 2303 2303 HOH HOH A . 
X 8 HOH 304 2304 2304 HOH HOH A . 
X 8 HOH 305 2305 2305 HOH HOH A . 
X 8 HOH 306 2306 2306 HOH HOH A . 
X 8 HOH 307 2307 2307 HOH HOH A . 
X 8 HOH 308 2308 2308 HOH HOH A . 
X 8 HOH 309 2309 2309 HOH HOH A . 
X 8 HOH 310 2310 2310 HOH HOH A . 
X 8 HOH 311 2311 2311 HOH HOH A . 
X 8 HOH 312 2312 2312 HOH HOH A . 
X 8 HOH 313 2313 2313 HOH HOH A . 
X 8 HOH 314 2314 2314 HOH HOH A . 
X 8 HOH 315 2315 2315 HOH HOH A . 
X 8 HOH 316 2316 2316 HOH HOH A . 
X 8 HOH 317 2317 2317 HOH HOH A . 
X 8 HOH 318 2318 2318 HOH HOH A . 
X 8 HOH 319 2319 2319 HOH HOH A . 
X 8 HOH 320 2320 2320 HOH HOH A . 
X 8 HOH 321 2321 2321 HOH HOH A . 
X 8 HOH 322 2322 2322 HOH HOH A . 
X 8 HOH 323 2323 2323 HOH HOH A . 
X 8 HOH 324 2324 2324 HOH HOH A . 
X 8 HOH 325 2325 2325 HOH HOH A . 
X 8 HOH 326 2326 2326 HOH HOH A . 
X 8 HOH 327 2327 2327 HOH HOH A . 
X 8 HOH 328 2328 2328 HOH HOH A . 
X 8 HOH 329 2329 2329 HOH HOH A . 
X 8 HOH 330 2330 2330 HOH HOH A . 
X 8 HOH 331 2331 2331 HOH HOH A . 
X 8 HOH 332 2332 2332 HOH HOH A . 
X 8 HOH 333 2333 2333 HOH HOH A . 
X 8 HOH 334 2334 2334 HOH HOH A . 
X 8 HOH 335 2335 2335 HOH HOH A . 
X 8 HOH 336 2336 2336 HOH HOH A . 
X 8 HOH 337 2337 2337 HOH HOH A . 
X 8 HOH 338 2338 2338 HOH HOH A . 
X 8 HOH 339 2339 2339 HOH HOH A . 
X 8 HOH 340 2340 2340 HOH HOH A . 
X 8 HOH 341 2341 2341 HOH HOH A . 
X 8 HOH 342 2342 2342 HOH HOH A . 
X 8 HOH 343 2343 2343 HOH HOH A . 
X 8 HOH 344 2344 2344 HOH HOH A . 
X 8 HOH 345 2345 2345 HOH HOH A . 
X 8 HOH 346 2346 2346 HOH HOH A . 
X 8 HOH 347 2347 2347 HOH HOH A . 
X 8 HOH 348 2348 2348 HOH HOH A . 
X 8 HOH 349 2349 2349 HOH HOH A . 
X 8 HOH 350 2350 2350 HOH HOH A . 
X 8 HOH 351 2351 2351 HOH HOH A . 
X 8 HOH 352 2352 2352 HOH HOH A . 
X 8 HOH 353 2353 2353 HOH HOH A . 
X 8 HOH 354 2354 2354 HOH HOH A . 
X 8 HOH 355 2355 2355 HOH HOH A . 
X 8 HOH 356 2356 2356 HOH HOH A . 
X 8 HOH 357 2357 2357 HOH HOH A . 
X 8 HOH 358 2358 2358 HOH HOH A . 
X 8 HOH 359 2359 2359 HOH HOH A . 
X 8 HOH 360 2360 2360 HOH HOH A . 
X 8 HOH 361 2361 2361 HOH HOH A . 
X 8 HOH 362 2362 2362 HOH HOH A . 
X 8 HOH 363 2363 2363 HOH HOH A . 
X 8 HOH 364 2364 2364 HOH HOH A . 
X 8 HOH 365 2365 2365 HOH HOH A . 
X 8 HOH 366 2366 2366 HOH HOH A . 
X 8 HOH 367 2367 2367 HOH HOH A . 
X 8 HOH 368 2368 2368 HOH HOH A . 
X 8 HOH 369 2369 2369 HOH HOH A . 
X 8 HOH 370 2370 2370 HOH HOH A . 
X 8 HOH 371 2371 2371 HOH HOH A . 
X 8 HOH 372 2372 2372 HOH HOH A . 
X 8 HOH 373 2373 2373 HOH HOH A . 
X 8 HOH 374 2374 2374 HOH HOH A . 
X 8 HOH 375 2375 2375 HOH HOH A . 
X 8 HOH 376 2376 2376 HOH HOH A . 
X 8 HOH 377 2377 2377 HOH HOH A . 
X 8 HOH 378 2378 2378 HOH HOH A . 
X 8 HOH 379 2379 2379 HOH HOH A . 
X 8 HOH 380 2380 2380 HOH HOH A . 
X 8 HOH 381 2381 2381 HOH HOH A . 
X 8 HOH 382 2382 2382 HOH HOH A . 
X 8 HOH 383 2383 2383 HOH HOH A . 
X 8 HOH 384 2384 2384 HOH HOH A . 
X 8 HOH 385 2385 2385 HOH HOH A . 
X 8 HOH 386 2386 2386 HOH HOH A . 
X 8 HOH 387 2387 2387 HOH HOH A . 
X 8 HOH 388 2388 2388 HOH HOH A . 
X 8 HOH 389 2389 2389 HOH HOH A . 
X 8 HOH 390 2390 2390 HOH HOH A . 
X 8 HOH 391 2391 2391 HOH HOH A . 
X 8 HOH 392 2392 2392 HOH HOH A . 
X 8 HOH 393 2393 2393 HOH HOH A . 
X 8 HOH 394 2394 2394 HOH HOH A . 
X 8 HOH 395 2395 2395 HOH HOH A . 
X 8 HOH 396 2396 2396 HOH HOH A . 
X 8 HOH 397 2397 2397 HOH HOH A . 
X 8 HOH 398 2398 2398 HOH HOH A . 
X 8 HOH 399 2399 2399 HOH HOH A . 
X 8 HOH 400 2400 2400 HOH HOH A . 
X 8 HOH 401 2401 2401 HOH HOH A . 
X 8 HOH 402 2402 2402 HOH HOH A . 
X 8 HOH 403 2403 2403 HOH HOH A . 
X 8 HOH 404 2404 2404 HOH HOH A . 
X 8 HOH 405 2405 2405 HOH HOH A . 
X 8 HOH 406 2406 2406 HOH HOH A . 
X 8 HOH 407 2407 2407 HOH HOH A . 
X 8 HOH 408 2408 2408 HOH HOH A . 
X 8 HOH 409 2409 2409 HOH HOH A . 
X 8 HOH 410 2410 2410 HOH HOH A . 
X 8 HOH 411 2411 2411 HOH HOH A . 
X 8 HOH 412 2412 2412 HOH HOH A . 
X 8 HOH 413 2413 2413 HOH HOH A . 
X 8 HOH 414 2414 2414 HOH HOH A . 
X 8 HOH 415 2415 2415 HOH HOH A . 
X 8 HOH 416 2416 2416 HOH HOH A . 
X 8 HOH 417 2417 2417 HOH HOH A . 
X 8 HOH 418 2418 2418 HOH HOH A . 
X 8 HOH 419 2419 2419 HOH HOH A . 
X 8 HOH 420 2420 2420 HOH HOH A . 
X 8 HOH 421 2421 2421 HOH HOH A . 
X 8 HOH 422 2422 2422 HOH HOH A . 
X 8 HOH 423 2423 2423 HOH HOH A . 
X 8 HOH 424 2424 2424 HOH HOH A . 
X 8 HOH 425 2425 2425 HOH HOH A . 
X 8 HOH 426 2426 2426 HOH HOH A . 
X 8 HOH 427 2427 2427 HOH HOH A . 
X 8 HOH 428 2428 2428 HOH HOH A . 
X 8 HOH 429 2429 2429 HOH HOH A . 
X 8 HOH 430 2430 2430 HOH HOH A . 
X 8 HOH 431 2431 2431 HOH HOH A . 
X 8 HOH 432 2432 2432 HOH HOH A . 
X 8 HOH 433 2433 2433 HOH HOH A . 
X 8 HOH 434 2434 2434 HOH HOH A . 
X 8 HOH 435 2435 2435 HOH HOH A . 
X 8 HOH 436 2436 2436 HOH HOH A . 
X 8 HOH 437 2437 2437 HOH HOH A . 
X 8 HOH 438 2438 2438 HOH HOH A . 
X 8 HOH 439 2439 2439 HOH HOH A . 
X 8 HOH 440 2440 2440 HOH HOH A . 
X 8 HOH 441 2441 2441 HOH HOH A . 
X 8 HOH 442 2442 2442 HOH HOH A . 
X 8 HOH 443 2443 2443 HOH HOH A . 
X 8 HOH 444 2444 2444 HOH HOH A . 
X 8 HOH 445 2445 2445 HOH HOH A . 
X 8 HOH 446 2446 2446 HOH HOH A . 
X 8 HOH 447 2447 2447 HOH HOH A . 
X 8 HOH 448 2448 2448 HOH HOH A . 
X 8 HOH 449 2449 2449 HOH HOH A . 
X 8 HOH 450 2450 2450 HOH HOH A . 
X 8 HOH 451 2451 2451 HOH HOH A . 
X 8 HOH 452 2452 2452 HOH HOH A . 
X 8 HOH 453 2453 2453 HOH HOH A . 
X 8 HOH 454 2454 2454 HOH HOH A . 
X 8 HOH 455 2455 2455 HOH HOH A . 
X 8 HOH 456 2456 2456 HOH HOH A . 
X 8 HOH 457 2457 2457 HOH HOH A . 
X 8 HOH 458 2458 2458 HOH HOH A . 
X 8 HOH 459 2459 2459 HOH HOH A . 
X 8 HOH 460 2460 2460 HOH HOH A . 
X 8 HOH 461 2461 2461 HOH HOH A . 
X 8 HOH 462 2462 2462 HOH HOH A . 
X 8 HOH 463 2463 2463 HOH HOH A . 
X 8 HOH 464 2464 2464 HOH HOH A . 
X 8 HOH 465 2465 2465 HOH HOH A . 
X 8 HOH 466 2466 2466 HOH HOH A . 
X 8 HOH 467 2467 2467 HOH HOH A . 
X 8 HOH 468 2468 2468 HOH HOH A . 
X 8 HOH 469 2469 2469 HOH HOH A . 
X 8 HOH 470 2470 2470 HOH HOH A . 
X 8 HOH 471 2471 2471 HOH HOH A . 
X 8 HOH 472 2472 2472 HOH HOH A . 
X 8 HOH 473 2473 2473 HOH HOH A . 
X 8 HOH 474 2474 2474 HOH HOH A . 
X 8 HOH 475 2475 2475 HOH HOH A . 
X 8 HOH 476 2476 2476 HOH HOH A . 
X 8 HOH 477 2477 2477 HOH HOH A . 
X 8 HOH 478 2478 2478 HOH HOH A . 
X 8 HOH 479 2479 2479 HOH HOH A . 
X 8 HOH 480 2480 2480 HOH HOH A . 
X 8 HOH 481 2481 2481 HOH HOH A . 
X 8 HOH 482 2482 2482 HOH HOH A . 
X 8 HOH 483 2483 2483 HOH HOH A . 
Y 8 HOH 1   2001 2001 HOH HOH B . 
Y 8 HOH 2   2002 2002 HOH HOH B . 
Y 8 HOH 3   2003 2003 HOH HOH B . 
Y 8 HOH 4   2004 2004 HOH HOH B . 
Y 8 HOH 5   2005 2005 HOH HOH B . 
Y 8 HOH 6   2006 2006 HOH HOH B . 
Y 8 HOH 7   2007 2007 HOH HOH B . 
Y 8 HOH 8   2008 2008 HOH HOH B . 
Y 8 HOH 9   2009 2009 HOH HOH B . 
Y 8 HOH 10  2010 2010 HOH HOH B . 
Y 8 HOH 11  2011 2011 HOH HOH B . 
Y 8 HOH 12  2012 2012 HOH HOH B . 
Y 8 HOH 13  2013 2013 HOH HOH B . 
Y 8 HOH 14  2014 2014 HOH HOH B . 
Y 8 HOH 15  2015 2015 HOH HOH B . 
Y 8 HOH 16  2016 2016 HOH HOH B . 
Y 8 HOH 17  2017 2017 HOH HOH B . 
Y 8 HOH 18  2018 2018 HOH HOH B . 
Y 8 HOH 19  2019 2019 HOH HOH B . 
Y 8 HOH 20  2020 2020 HOH HOH B . 
Y 8 HOH 21  2021 2021 HOH HOH B . 
Y 8 HOH 22  2022 2022 HOH HOH B . 
Y 8 HOH 23  2023 2023 HOH HOH B . 
Y 8 HOH 24  2024 2024 HOH HOH B . 
Y 8 HOH 25  2025 2025 HOH HOH B . 
Y 8 HOH 26  2026 2026 HOH HOH B . 
Y 8 HOH 27  2027 2027 HOH HOH B . 
Y 8 HOH 28  2028 2028 HOH HOH B . 
Y 8 HOH 29  2029 2029 HOH HOH B . 
Y 8 HOH 30  2030 2030 HOH HOH B . 
Y 8 HOH 31  2031 2031 HOH HOH B . 
Y 8 HOH 32  2032 2032 HOH HOH B . 
Y 8 HOH 33  2033 2033 HOH HOH B . 
Y 8 HOH 34  2034 2034 HOH HOH B . 
Y 8 HOH 35  2035 2035 HOH HOH B . 
Y 8 HOH 36  2036 2036 HOH HOH B . 
Y 8 HOH 37  2037 2037 HOH HOH B . 
Y 8 HOH 38  2038 2038 HOH HOH B . 
Y 8 HOH 39  2039 2039 HOH HOH B . 
Y 8 HOH 40  2040 2040 HOH HOH B . 
Y 8 HOH 41  2041 2041 HOH HOH B . 
Y 8 HOH 42  2042 2042 HOH HOH B . 
Y 8 HOH 43  2043 2043 HOH HOH B . 
Y 8 HOH 44  2044 2044 HOH HOH B . 
Y 8 HOH 45  2045 2045 HOH HOH B . 
Y 8 HOH 46  2046 2046 HOH HOH B . 
Y 8 HOH 47  2047 2047 HOH HOH B . 
Y 8 HOH 48  2048 2048 HOH HOH B . 
Y 8 HOH 49  2049 2049 HOH HOH B . 
Y 8 HOH 50  2050 2050 HOH HOH B . 
Y 8 HOH 51  2051 2051 HOH HOH B . 
Y 8 HOH 52  2052 2052 HOH HOH B . 
Y 8 HOH 53  2053 2053 HOH HOH B . 
Y 8 HOH 54  2054 2054 HOH HOH B . 
Y 8 HOH 55  2055 2055 HOH HOH B . 
Y 8 HOH 56  2056 2056 HOH HOH B . 
Y 8 HOH 57  2057 2057 HOH HOH B . 
Y 8 HOH 58  2058 2058 HOH HOH B . 
Y 8 HOH 59  2059 2059 HOH HOH B . 
Y 8 HOH 60  2060 2060 HOH HOH B . 
Y 8 HOH 61  2061 2061 HOH HOH B . 
Y 8 HOH 62  2062 2062 HOH HOH B . 
Y 8 HOH 63  2063 2063 HOH HOH B . 
Y 8 HOH 64  2064 2064 HOH HOH B . 
Y 8 HOH 65  2065 2065 HOH HOH B . 
Y 8 HOH 66  2066 2066 HOH HOH B . 
Y 8 HOH 67  2067 2067 HOH HOH B . 
Y 8 HOH 68  2068 2068 HOH HOH B . 
Y 8 HOH 69  2069 2069 HOH HOH B . 
Y 8 HOH 70  2070 2070 HOH HOH B . 
Y 8 HOH 71  2071 2071 HOH HOH B . 
Y 8 HOH 72  2072 2072 HOH HOH B . 
Y 8 HOH 73  2073 2073 HOH HOH B . 
Y 8 HOH 74  2074 2074 HOH HOH B . 
Y 8 HOH 75  2075 2075 HOH HOH B . 
Y 8 HOH 76  2076 2076 HOH HOH B . 
Y 8 HOH 77  2077 2077 HOH HOH B . 
Y 8 HOH 78  2078 2078 HOH HOH B . 
Y 8 HOH 79  2079 2079 HOH HOH B . 
Y 8 HOH 80  2080 2080 HOH HOH B . 
Y 8 HOH 81  2081 2081 HOH HOH B . 
Y 8 HOH 82  2082 2082 HOH HOH B . 
Y 8 HOH 83  2083 2083 HOH HOH B . 
Y 8 HOH 84  2084 2084 HOH HOH B . 
Y 8 HOH 85  2085 2085 HOH HOH B . 
Y 8 HOH 86  2086 2086 HOH HOH B . 
Y 8 HOH 87  2087 2087 HOH HOH B . 
Y 8 HOH 88  2088 2088 HOH HOH B . 
Y 8 HOH 89  2089 2089 HOH HOH B . 
Y 8 HOH 90  2090 2090 HOH HOH B . 
Y 8 HOH 91  2091 2091 HOH HOH B . 
Y 8 HOH 92  2092 2092 HOH HOH B . 
Y 8 HOH 93  2093 2093 HOH HOH B . 
Y 8 HOH 94  2094 2094 HOH HOH B . 
Y 8 HOH 95  2095 2095 HOH HOH B . 
Y 8 HOH 96  2096 2096 HOH HOH B . 
Y 8 HOH 97  2097 2097 HOH HOH B . 
Y 8 HOH 98  2098 2098 HOH HOH B . 
Y 8 HOH 99  2099 2099 HOH HOH B . 
Y 8 HOH 100 2100 2100 HOH HOH B . 
Y 8 HOH 101 2101 2101 HOH HOH B . 
Y 8 HOH 102 2102 2102 HOH HOH B . 
Y 8 HOH 103 2103 2103 HOH HOH B . 
Y 8 HOH 104 2104 2104 HOH HOH B . 
Y 8 HOH 105 2105 2105 HOH HOH B . 
Y 8 HOH 106 2106 2106 HOH HOH B . 
Y 8 HOH 107 2107 2107 HOH HOH B . 
Y 8 HOH 108 2108 2108 HOH HOH B . 
Y 8 HOH 109 2109 2109 HOH HOH B . 
Y 8 HOH 110 2110 2110 HOH HOH B . 
Y 8 HOH 111 2111 2111 HOH HOH B . 
Y 8 HOH 112 2112 2112 HOH HOH B . 
Y 8 HOH 113 2113 2113 HOH HOH B . 
Y 8 HOH 114 2114 2114 HOH HOH B . 
Y 8 HOH 115 2115 2115 HOH HOH B . 
Y 8 HOH 116 2116 2116 HOH HOH B . 
Y 8 HOH 117 2117 2117 HOH HOH B . 
Y 8 HOH 118 2118 2118 HOH HOH B . 
Y 8 HOH 119 2119 2119 HOH HOH B . 
Y 8 HOH 120 2120 2120 HOH HOH B . 
Y 8 HOH 121 2121 2121 HOH HOH B . 
Y 8 HOH 122 2122 2122 HOH HOH B . 
Y 8 HOH 123 2123 2123 HOH HOH B . 
Y 8 HOH 124 2124 2124 HOH HOH B . 
Y 8 HOH 125 2125 2125 HOH HOH B . 
Y 8 HOH 126 2126 2126 HOH HOH B . 
Y 8 HOH 127 2127 2127 HOH HOH B . 
Y 8 HOH 128 2128 2128 HOH HOH B . 
Y 8 HOH 129 2129 2129 HOH HOH B . 
Y 8 HOH 130 2130 2130 HOH HOH B . 
Y 8 HOH 131 2131 2131 HOH HOH B . 
Y 8 HOH 132 2132 2132 HOH HOH B . 
Y 8 HOH 133 2133 2133 HOH HOH B . 
Y 8 HOH 134 2134 2134 HOH HOH B . 
Y 8 HOH 135 2135 2135 HOH HOH B . 
Y 8 HOH 136 2136 2136 HOH HOH B . 
Y 8 HOH 137 2137 2137 HOH HOH B . 
Y 8 HOH 138 2138 2138 HOH HOH B . 
Y 8 HOH 139 2139 2139 HOH HOH B . 
Y 8 HOH 140 2140 2140 HOH HOH B . 
Y 8 HOH 141 2141 2141 HOH HOH B . 
Y 8 HOH 142 2142 2142 HOH HOH B . 
Y 8 HOH 143 2143 2143 HOH HOH B . 
Y 8 HOH 144 2144 2144 HOH HOH B . 
Y 8 HOH 145 2145 2145 HOH HOH B . 
Y 8 HOH 146 2146 2146 HOH HOH B . 
Y 8 HOH 147 2147 2147 HOH HOH B . 
Y 8 HOH 148 2148 2148 HOH HOH B . 
Y 8 HOH 149 2149 2149 HOH HOH B . 
Y 8 HOH 150 2150 2150 HOH HOH B . 
Y 8 HOH 151 2151 2151 HOH HOH B . 
Y 8 HOH 152 2152 2152 HOH HOH B . 
Y 8 HOH 153 2153 2153 HOH HOH B . 
Y 8 HOH 154 2154 2154 HOH HOH B . 
Y 8 HOH 155 2155 2155 HOH HOH B . 
Y 8 HOH 156 2156 2156 HOH HOH B . 
Y 8 HOH 157 2157 2157 HOH HOH B . 
Y 8 HOH 158 2158 2158 HOH HOH B . 
Y 8 HOH 159 2159 2159 HOH HOH B . 
Y 8 HOH 160 2160 2160 HOH HOH B . 
Y 8 HOH 161 2161 2161 HOH HOH B . 
Y 8 HOH 162 2162 2162 HOH HOH B . 
Y 8 HOH 163 2163 2163 HOH HOH B . 
Y 8 HOH 164 2164 2164 HOH HOH B . 
Y 8 HOH 165 2165 2165 HOH HOH B . 
Y 8 HOH 166 2166 2166 HOH HOH B . 
Y 8 HOH 167 2167 2167 HOH HOH B . 
Y 8 HOH 168 2168 2168 HOH HOH B . 
Y 8 HOH 169 2169 2169 HOH HOH B . 
Y 8 HOH 170 2170 2170 HOH HOH B . 
Y 8 HOH 171 2171 2171 HOH HOH B . 
Y 8 HOH 172 2172 2172 HOH HOH B . 
Y 8 HOH 173 2173 2173 HOH HOH B . 
Y 8 HOH 174 2174 2174 HOH HOH B . 
Y 8 HOH 175 2175 2175 HOH HOH B . 
Y 8 HOH 176 2176 2176 HOH HOH B . 
Y 8 HOH 177 2177 2177 HOH HOH B . 
Y 8 HOH 178 2178 2178 HOH HOH B . 
Y 8 HOH 179 2179 2179 HOH HOH B . 
Y 8 HOH 180 2180 2180 HOH HOH B . 
Y 8 HOH 181 2181 2181 HOH HOH B . 
Y 8 HOH 182 2182 2182 HOH HOH B . 
Y 8 HOH 183 2183 2183 HOH HOH B . 
Y 8 HOH 184 2184 2184 HOH HOH B . 
Y 8 HOH 185 2185 2185 HOH HOH B . 
Y 8 HOH 186 2186 2186 HOH HOH B . 
Y 8 HOH 187 2187 2187 HOH HOH B . 
Y 8 HOH 188 2188 2188 HOH HOH B . 
Y 8 HOH 189 2189 2189 HOH HOH B . 
Y 8 HOH 190 2190 2190 HOH HOH B . 
Y 8 HOH 191 2191 2191 HOH HOH B . 
Y 8 HOH 192 2192 2192 HOH HOH B . 
Y 8 HOH 193 2193 2193 HOH HOH B . 
Y 8 HOH 194 2194 2194 HOH HOH B . 
Y 8 HOH 195 2195 2195 HOH HOH B . 
Y 8 HOH 196 2196 2196 HOH HOH B . 
Y 8 HOH 197 2197 2197 HOH HOH B . 
Y 8 HOH 198 2198 2198 HOH HOH B . 
Y 8 HOH 199 2199 2199 HOH HOH B . 
Y 8 HOH 200 2200 2200 HOH HOH B . 
Y 8 HOH 201 2201 2201 HOH HOH B . 
Y 8 HOH 202 2202 2202 HOH HOH B . 
Y 8 HOH 203 2203 2203 HOH HOH B . 
Y 8 HOH 204 2204 2204 HOH HOH B . 
Y 8 HOH 205 2205 2205 HOH HOH B . 
Y 8 HOH 206 2206 2206 HOH HOH B . 
Y 8 HOH 207 2207 2207 HOH HOH B . 
Y 8 HOH 208 2208 2208 HOH HOH B . 
Y 8 HOH 209 2209 2209 HOH HOH B . 
Y 8 HOH 210 2210 2210 HOH HOH B . 
Y 8 HOH 211 2211 2211 HOH HOH B . 
Y 8 HOH 212 2212 2212 HOH HOH B . 
Y 8 HOH 213 2213 2213 HOH HOH B . 
Y 8 HOH 214 2214 2214 HOH HOH B . 
Y 8 HOH 215 2215 2215 HOH HOH B . 
Y 8 HOH 216 2216 2216 HOH HOH B . 
Y 8 HOH 217 2217 2217 HOH HOH B . 
Y 8 HOH 218 2218 2218 HOH HOH B . 
Y 8 HOH 219 2219 2219 HOH HOH B . 
Y 8 HOH 220 2220 2220 HOH HOH B . 
Y 8 HOH 221 2221 2221 HOH HOH B . 
Y 8 HOH 222 2222 2222 HOH HOH B . 
Y 8 HOH 223 2223 2223 HOH HOH B . 
Y 8 HOH 224 2224 2224 HOH HOH B . 
Y 8 HOH 225 2225 2225 HOH HOH B . 
Y 8 HOH 226 2226 2226 HOH HOH B . 
Y 8 HOH 227 2227 2227 HOH HOH B . 
Y 8 HOH 228 2228 2228 HOH HOH B . 
Y 8 HOH 229 2229 2229 HOH HOH B . 
Y 8 HOH 230 2230 2230 HOH HOH B . 
Y 8 HOH 231 2231 2231 HOH HOH B . 
Y 8 HOH 232 2232 2232 HOH HOH B . 
Y 8 HOH 233 2233 2233 HOH HOH B . 
Y 8 HOH 234 2234 2234 HOH HOH B . 
Y 8 HOH 235 2235 2235 HOH HOH B . 
Y 8 HOH 236 2236 2236 HOH HOH B . 
Y 8 HOH 237 2237 2237 HOH HOH B . 
Y 8 HOH 238 2238 2238 HOH HOH B . 
Y 8 HOH 239 2239 2239 HOH HOH B . 
Y 8 HOH 240 2240 2240 HOH HOH B . 
Y 8 HOH 241 2241 2241 HOH HOH B . 
Y 8 HOH 242 2242 2242 HOH HOH B . 
Y 8 HOH 243 2243 2243 HOH HOH B . 
Y 8 HOH 244 2244 2244 HOH HOH B . 
Y 8 HOH 245 2245 2245 HOH HOH B . 
Y 8 HOH 246 2246 2246 HOH HOH B . 
Y 8 HOH 247 2247 2247 HOH HOH B . 
Y 8 HOH 248 2248 2248 HOH HOH B . 
Y 8 HOH 249 2249 2249 HOH HOH B . 
Y 8 HOH 250 2250 2250 HOH HOH B . 
Y 8 HOH 251 2251 2251 HOH HOH B . 
Y 8 HOH 252 2252 2252 HOH HOH B . 
Y 8 HOH 253 2253 2253 HOH HOH B . 
Y 8 HOH 254 2254 2254 HOH HOH B . 
Y 8 HOH 255 2255 2255 HOH HOH B . 
Y 8 HOH 256 2256 2256 HOH HOH B . 
Y 8 HOH 257 2257 2257 HOH HOH B . 
Y 8 HOH 258 2258 2258 HOH HOH B . 
Y 8 HOH 259 2259 2259 HOH HOH B . 
Y 8 HOH 260 2260 2260 HOH HOH B . 
Y 8 HOH 261 2261 2261 HOH HOH B . 
Y 8 HOH 262 2262 2262 HOH HOH B . 
Y 8 HOH 263 2263 2263 HOH HOH B . 
Y 8 HOH 264 2264 2264 HOH HOH B . 
Y 8 HOH 265 2265 2265 HOH HOH B . 
Y 8 HOH 266 2266 2266 HOH HOH B . 
Y 8 HOH 267 2267 2267 HOH HOH B . 
Y 8 HOH 268 2268 2268 HOH HOH B . 
Y 8 HOH 269 2269 2269 HOH HOH B . 
Y 8 HOH 270 2270 2270 HOH HOH B . 
Y 8 HOH 271 2271 2271 HOH HOH B . 
Y 8 HOH 272 2272 2272 HOH HOH B . 
Y 8 HOH 273 2273 2273 HOH HOH B . 
Y 8 HOH 274 2274 2274 HOH HOH B . 
Y 8 HOH 275 2275 2275 HOH HOH B . 
Y 8 HOH 276 2276 2276 HOH HOH B . 
Y 8 HOH 277 2277 2277 HOH HOH B . 
Y 8 HOH 278 2278 2278 HOH HOH B . 
Y 8 HOH 279 2279 2279 HOH HOH B . 
Y 8 HOH 280 2280 2280 HOH HOH B . 
Y 8 HOH 281 2281 2281 HOH HOH B . 
Y 8 HOH 282 2282 2282 HOH HOH B . 
Y 8 HOH 283 2283 2283 HOH HOH B . 
Y 8 HOH 284 2284 2284 HOH HOH B . 
Y 8 HOH 285 2285 2285 HOH HOH B . 
Y 8 HOH 286 2286 2286 HOH HOH B . 
Y 8 HOH 287 2287 2287 HOH HOH B . 
Y 8 HOH 288 2288 2288 HOH HOH B . 
Y 8 HOH 289 2289 2289 HOH HOH B . 
Y 8 HOH 290 2290 2290 HOH HOH B . 
Y 8 HOH 291 2291 2291 HOH HOH B . 
Y 8 HOH 292 2292 2292 HOH HOH B . 
Y 8 HOH 293 2293 2293 HOH HOH B . 
Y 8 HOH 294 2294 2294 HOH HOH B . 
Y 8 HOH 295 2295 2295 HOH HOH B . 
Y 8 HOH 296 2296 2296 HOH HOH B . 
Y 8 HOH 297 2297 2297 HOH HOH B . 
Y 8 HOH 298 2298 2298 HOH HOH B . 
Y 8 HOH 299 2299 2299 HOH HOH B . 
Y 8 HOH 300 2300 2300 HOH HOH B . 
Y 8 HOH 301 2301 2301 HOH HOH B . 
Y 8 HOH 302 2302 2302 HOH HOH B . 
Y 8 HOH 303 2303 2303 HOH HOH B . 
Y 8 HOH 304 2304 2304 HOH HOH B . 
Y 8 HOH 305 2305 2305 HOH HOH B . 
Y 8 HOH 306 2306 2306 HOH HOH B . 
Y 8 HOH 307 2307 2307 HOH HOH B . 
Y 8 HOH 308 2308 2308 HOH HOH B . 
Y 8 HOH 309 2309 2309 HOH HOH B . 
Y 8 HOH 310 2310 2310 HOH HOH B . 
Y 8 HOH 311 2311 2311 HOH HOH B . 
Y 8 HOH 312 2312 2312 HOH HOH B . 
Y 8 HOH 313 2313 2313 HOH HOH B . 
Y 8 HOH 314 2314 2314 HOH HOH B . 
Y 8 HOH 315 2315 2315 HOH HOH B . 
Y 8 HOH 316 2316 2316 HOH HOH B . 
Y 8 HOH 317 2317 2317 HOH HOH B . 
Y 8 HOH 318 2318 2318 HOH HOH B . 
Y 8 HOH 319 2319 2319 HOH HOH B . 
Y 8 HOH 320 2320 2320 HOH HOH B . 
Y 8 HOH 321 2321 2321 HOH HOH B . 
Y 8 HOH 322 2322 2322 HOH HOH B . 
Y 8 HOH 323 2323 2323 HOH HOH B . 
Y 8 HOH 324 2324 2324 HOH HOH B . 
Y 8 HOH 325 2325 2325 HOH HOH B . 
Y 8 HOH 326 2326 2326 HOH HOH B . 
Y 8 HOH 327 2327 2327 HOH HOH B . 
Y 8 HOH 328 2328 2328 HOH HOH B . 
Y 8 HOH 329 2329 2329 HOH HOH B . 
Y 8 HOH 330 2330 2330 HOH HOH B . 
Y 8 HOH 331 2331 2331 HOH HOH B . 
Y 8 HOH 332 2332 2332 HOH HOH B . 
Y 8 HOH 333 2333 2333 HOH HOH B . 
Y 8 HOH 334 2334 2334 HOH HOH B . 
Y 8 HOH 335 2335 2335 HOH HOH B . 
Y 8 HOH 336 2336 2336 HOH HOH B . 
Y 8 HOH 337 2337 2337 HOH HOH B . 
Y 8 HOH 338 2338 2338 HOH HOH B . 
Y 8 HOH 339 2339 2339 HOH HOH B . 
Y 8 HOH 340 2340 2340 HOH HOH B . 
Y 8 HOH 341 2341 2341 HOH HOH B . 
Y 8 HOH 342 2342 2342 HOH HOH B . 
Y 8 HOH 343 2343 2343 HOH HOH B . 
Y 8 HOH 344 2344 2344 HOH HOH B . 
Y 8 HOH 345 2345 2345 HOH HOH B . 
Y 8 HOH 346 2346 2346 HOH HOH B . 
Y 8 HOH 347 2347 2347 HOH HOH B . 
Y 8 HOH 348 2348 2348 HOH HOH B . 
Y 8 HOH 349 2349 2349 HOH HOH B . 
Y 8 HOH 350 2350 2350 HOH HOH B . 
Y 8 HOH 351 2351 2351 HOH HOH B . 
Y 8 HOH 352 2352 2352 HOH HOH B . 
Y 8 HOH 353 2353 2353 HOH HOH B . 
Y 8 HOH 354 2354 2354 HOH HOH B . 
Y 8 HOH 355 2355 2355 HOH HOH B . 
Y 8 HOH 356 2356 2356 HOH HOH B . 
Y 8 HOH 357 2357 2357 HOH HOH B . 
Y 8 HOH 358 2358 2358 HOH HOH B . 
Y 8 HOH 359 2359 2359 HOH HOH B . 
Y 8 HOH 360 2360 2360 HOH HOH B . 
Y 8 HOH 361 2361 2361 HOH HOH B . 
Y 8 HOH 362 2362 2362 HOH HOH B . 
Y 8 HOH 363 2363 2363 HOH HOH B . 
Y 8 HOH 364 2364 2364 HOH HOH B . 
Y 8 HOH 365 2365 2365 HOH HOH B . 
Y 8 HOH 366 2366 2366 HOH HOH B . 
Y 8 HOH 367 2367 2367 HOH HOH B . 
Y 8 HOH 368 2368 2368 HOH HOH B . 
Y 8 HOH 369 2369 2369 HOH HOH B . 
Y 8 HOH 370 2370 2370 HOH HOH B . 
Y 8 HOH 371 2371 2371 HOH HOH B . 
Y 8 HOH 372 2372 2372 HOH HOH B . 
Y 8 HOH 373 2373 2373 HOH HOH B . 
Y 8 HOH 374 2374 2374 HOH HOH B . 
Y 8 HOH 375 2375 2375 HOH HOH B . 
Y 8 HOH 376 2376 2376 HOH HOH B . 
Y 8 HOH 377 2377 2377 HOH HOH B . 
Y 8 HOH 378 2378 2378 HOH HOH B . 
Y 8 HOH 379 2379 2379 HOH HOH B . 
Y 8 HOH 380 2380 2380 HOH HOH B . 
Y 8 HOH 381 2381 2381 HOH HOH B . 
Y 8 HOH 382 2382 2382 HOH HOH B . 
Y 8 HOH 383 2383 2383 HOH HOH B . 
Y 8 HOH 384 2384 2384 HOH HOH B . 
Y 8 HOH 385 2385 2385 HOH HOH B . 
Y 8 HOH 386 2386 2386 HOH HOH B . 
Y 8 HOH 387 2387 2387 HOH HOH B . 
Y 8 HOH 388 2388 2388 HOH HOH B . 
Y 8 HOH 389 2389 2389 HOH HOH B . 
Y 8 HOH 390 2390 2390 HOH HOH B . 
Y 8 HOH 391 2391 2391 HOH HOH B . 
Y 8 HOH 392 2392 2392 HOH HOH B . 
Y 8 HOH 393 2393 2393 HOH HOH B . 
Y 8 HOH 394 2394 2394 HOH HOH B . 
Y 8 HOH 395 2395 2395 HOH HOH B . 
Y 8 HOH 396 2396 2396 HOH HOH B . 
Y 8 HOH 397 2397 2397 HOH HOH B . 
Y 8 HOH 398 2398 2398 HOH HOH B . 
Y 8 HOH 399 2399 2399 HOH HOH B . 
Y 8 HOH 400 2400 2400 HOH HOH B . 
Y 8 HOH 401 2401 2401 HOH HOH B . 
Y 8 HOH 402 2402 2402 HOH HOH B . 
Y 8 HOH 403 2403 2403 HOH HOH B . 
Y 8 HOH 404 2404 2404 HOH HOH B . 
Y 8 HOH 405 2405 2405 HOH HOH B . 
Y 8 HOH 406 2406 2406 HOH HOH B . 
Y 8 HOH 407 2407 2407 HOH HOH B . 
Y 8 HOH 408 2408 2408 HOH HOH B . 
Y 8 HOH 409 2409 2409 HOH HOH B . 
Y 8 HOH 410 2410 2410 HOH HOH B . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 280 A ASN 282 ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 347 A ASN 349 ? ASN 'GLYCOSYLATION SITE' 
3 A ASN 413 A ASN 415 ? ASN 'GLYCOSYLATION SITE' 
4 B ASN 280 B ASN 282 ? ASN 'GLYCOSYLATION SITE' 
5 B ASN 347 B ASN 349 ? ASN 'GLYCOSYLATION SITE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,J,K,L,M,N,X 
2 1 B,O,P,Q,R,S,T,U,V,W,Y       
# 
_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_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 302 ? A HIS 304  ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 NA ? L N7H . ? A N7H 1458 ? 1_555 83.9  ? 
2  NE2 ? A HIS 302 ? A HIS 304  ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 NB ? L N7H . ? A N7H 1458 ? 1_555 91.3  ? 
3  NA  ? L N7H .   ? A N7H 1458 ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 NB ? L N7H . ? A N7H 1458 ? 1_555 90.2  ? 
4  NE2 ? A HIS 302 ? A HIS 304  ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 NC ? L N7H . ? A N7H 1458 ? 1_555 96.4  ? 
5  NA  ? L N7H .   ? A N7H 1458 ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 NC ? L N7H . ? A N7H 1458 ? 1_555 178.8 ? 
6  NB  ? L N7H .   ? A N7H 1458 ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 NC ? L N7H . ? A N7H 1458 ? 1_555 88.7  ? 
7  NE2 ? A HIS 302 ? A HIS 304  ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 ND ? L N7H . ? A N7H 1458 ? 1_555 89.5  ? 
8  NA  ? L N7H .   ? A N7H 1458 ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 ND ? L N7H . ? A N7H 1458 ? 1_555 90.3  ? 
9  NB  ? L N7H .   ? A N7H 1458 ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 ND ? L N7H . ? A N7H 1458 ? 1_555 179.0 ? 
10 NC  ? L N7H .   ? A N7H 1458 ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 ND ? L N7H . ? A N7H 1458 ? 1_555 90.8  ? 
11 NE2 ? A HIS 302 ? A HIS 304  ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 O1 ? N NO2 . ? A NO2 1460 ? 1_555 174.2 ? 
12 NA  ? L N7H .   ? A N7H 1458 ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 O1 ? N NO2 . ? A NO2 1460 ? 1_555 93.0  ? 
13 NB  ? L N7H .   ? A N7H 1458 ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 O1 ? N NO2 . ? A NO2 1460 ? 1_555 83.9  ? 
14 NC  ? L N7H .   ? A N7H 1458 ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 O1 ? N NO2 . ? A NO2 1460 ? 1_555 86.6  ? 
15 ND  ? L N7H .   ? A N7H 1458 ? 1_555 FE ? L N7H . ? A N7H 1458 ? 1_555 O1 ? N NO2 . ? A NO2 1460 ? 1_555 95.3  ? 
16 NE2 ? B HIS 302 ? B HIS 304  ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 NA ? V N7H . ? B N7H 1456 ? 1_555 85.9  ? 
17 NE2 ? B HIS 302 ? B HIS 304  ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 NB ? V N7H . ? B N7H 1456 ? 1_555 92.0  ? 
18 NA  ? V N7H .   ? B N7H 1456 ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 NB ? V N7H . ? B N7H 1456 ? 1_555 90.3  ? 
19 NE2 ? B HIS 302 ? B HIS 304  ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 NC ? V N7H . ? B N7H 1456 ? 1_555 94.4  ? 
20 NA  ? V N7H .   ? B N7H 1456 ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 NC ? V N7H . ? B N7H 1456 ? 1_555 178.8 ? 
21 NB  ? V N7H .   ? B N7H 1456 ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 NC ? V N7H . ? B N7H 1456 ? 1_555 88.5  ? 
22 NE2 ? B HIS 302 ? B HIS 304  ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 ND ? V N7H . ? B N7H 1456 ? 1_555 88.8  ? 
23 NA  ? V N7H .   ? B N7H 1456 ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 ND ? V N7H . ? B N7H 1456 ? 1_555 90.4  ? 
24 NB  ? V N7H .   ? B N7H 1456 ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 ND ? V N7H . ? B N7H 1456 ? 1_555 179.0 ? 
25 NC  ? V N7H .   ? B N7H 1456 ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 ND ? V N7H . ? B N7H 1456 ? 1_555 90.8  ? 
26 NE2 ? B HIS 302 ? B HIS 304  ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 O1 ? W NO2 . ? B NO2 1457 ? 1_555 174.2 ? 
27 NA  ? V N7H .   ? B N7H 1456 ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 O1 ? W NO2 . ? B NO2 1457 ? 1_555 90.7  ? 
28 NB  ? V N7H .   ? B N7H 1456 ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 O1 ? W NO2 . ? B NO2 1457 ? 1_555 83.2  ? 
29 NC  ? V N7H .   ? B N7H 1456 ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 O1 ? W NO2 . ? B NO2 1457 ? 1_555 88.9  ? 
30 ND  ? V N7H .   ? B N7H 1456 ? 1_555 FE ? V N7H . ? B N7H 1456 ? 1_555 O1 ? W NO2 . ? B NO2 1457 ? 1_555 96.0  ? 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2016-03-02 
# 
_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         ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC refinement       5.8.0073 ? 1 
XDS    'data reduction' .        ? 2 
XDS    'data scaling'   .        ? 3 
PHASER phasing          .        ? 4 
# 
_pdbx_entry_details.entry_id             5AG1 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   
;DELTA-MESO NITROHEME (N7H): IRON PROTOPORPHYRIN IX WITH A
 NITRO GROUP AT THE DELTA-MESO CARBON.
;
_pdbx_entry_details.sequence_details     'PRECURSOR SEQUENCE IN GENBANK WITH PROLONGED N-TERMINUS.' 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 2306 ? ? O A HOH 2418 ? ? 2.12 
2 1 O   B ALA 288  ? ? O B HOH 2313 ? ? 2.14 
3 1 OG1 A THR 96   ? B O A HOH 2167 ? ? 2.19 
# 
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 TYR A 285 ? ? 89.01   -9.48   
2 1 ARG A 311 ? ? 49.49   -125.16 
3 1 TRP A 377 ? ? -109.18 -65.08  
4 1 PHE B 178 ? ? -122.23 -53.01  
5 1 THR B 265 ? ? -155.64 81.66   
6 1 TYR B 285 ? ? 88.66   -6.23   
7 1 ARG B 311 ? ? 51.24   -122.14 
8 1 TRP B 377 ? ? -109.96 -65.10  
9 1 ASN B 415 ? ? -158.55 79.79   
# 
loop_
_pdbx_validate_chiral.id 
_pdbx_validate_chiral.PDB_model_num 
_pdbx_validate_chiral.auth_atom_id 
_pdbx_validate_chiral.label_alt_id 
_pdbx_validate_chiral.auth_asym_id 
_pdbx_validate_chiral.auth_comp_id 
_pdbx_validate_chiral.auth_seq_id 
_pdbx_validate_chiral.PDB_ins_code 
_pdbx_validate_chiral.details 
_pdbx_validate_chiral.omega 
1 1 NA ? A N7H 1458 ? PLANAR . 
2 1 NB ? A N7H 1458 ? PLANAR . 
3 1 ND ? A N7H 1458 ? PLANAR . 
4 1 NA ? B N7H 1456 ? PLANAR . 
5 1 NB ? B N7H 1456 ? PLANAR . 
6 1 ND ? B N7H 1456 ? PLANAR . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 2004 ? 6.22 . 
2 1 O ? A HOH 2248 ? 5.82 . 
3 1 O ? B HOH 2138 ? 6.34 . 
4 1 O ? B HOH 2410 ? 5.85 . 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     SER 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      3 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    B 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    SER 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CACODYLATE ION'       CAC 
3 GLYCEROL               GOL 
4 N-ACETYL-D-GLUCOSAMINE NAG 
5 'DELTA-MESO NITROHEME' N7H 
6 'FORMIC ACID'          FMT 
7 'NITRITE ION'          NO2 
8 water                  HOH 
# 
